diff --git "a/4BDU.cif" "b/4BDU.cif" new file mode 100644--- /dev/null +++ "b/4BDU.cif" @@ -0,0 +1,23014 @@ +data_4BDU +# +_entry.id 4BDU +# +_audit_conform.dict_name mmcif_pdbx.dic +_audit_conform.dict_version 5.399 +_audit_conform.dict_location http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic +# +loop_ +_database_2.database_id +_database_2.database_code +_database_2.pdbx_database_accession +_database_2.pdbx_DOI +PDB 4BDU pdb_00004bdu 10.2210/pdb4bdu/pdb +PDBE EBI-54332 ? ? +WWPDB D_1290054332 ? ? +# +loop_ +_pdbx_audit_revision_history.ordinal +_pdbx_audit_revision_history.data_content_type +_pdbx_audit_revision_history.major_revision +_pdbx_audit_revision_history.minor_revision +_pdbx_audit_revision_history.revision_date +1 'Structure model' 1 0 2013-02-13 +2 'Structure model' 1 1 2017-03-15 +3 'Structure model' 1 2 2019-10-23 +4 'Structure model' 1 3 2024-11-20 +# +_pdbx_audit_revision_details.ordinal 1 +_pdbx_audit_revision_details.revision_ordinal 1 +_pdbx_audit_revision_details.data_content_type 'Structure model' +_pdbx_audit_revision_details.provider repository +_pdbx_audit_revision_details.type 'Initial release' +_pdbx_audit_revision_details.description ? +_pdbx_audit_revision_details.details ? +# +loop_ +_pdbx_audit_revision_group.ordinal +_pdbx_audit_revision_group.revision_ordinal +_pdbx_audit_revision_group.data_content_type +_pdbx_audit_revision_group.group +1 2 'Structure model' 'Source and taxonomy' +2 3 'Structure model' 'Data collection' +3 3 'Structure model' 'Database references' +4 3 'Structure model' 'Derived calculations' +5 3 'Structure model' Other +6 4 'Structure model' 'Data collection' +7 4 'Structure model' 'Database references' +8 4 'Structure model' 'Derived calculations' +9 4 'Structure model' 'Structure summary' +# +loop_ +_pdbx_audit_revision_category.ordinal +_pdbx_audit_revision_category.revision_ordinal +_pdbx_audit_revision_category.data_content_type +_pdbx_audit_revision_category.category +1 3 'Structure model' pdbx_database_status +2 3 'Structure model' struct_conn +3 3 'Structure model' struct_ref_seq_dif +4 4 'Structure model' chem_comp_atom +5 4 'Structure model' chem_comp_bond +6 4 'Structure model' database_2 +7 4 'Structure model' pdbx_entry_details +8 4 'Structure model' pdbx_modification_feature +9 4 'Structure model' struct_conn +# +loop_ +_pdbx_audit_revision_item.ordinal +_pdbx_audit_revision_item.revision_ordinal +_pdbx_audit_revision_item.data_content_type +_pdbx_audit_revision_item.item +1 3 'Structure model' '_pdbx_database_status.status_code_sf' +2 3 'Structure model' '_struct_conn.pdbx_leaving_atom_flag' +3 3 'Structure model' '_struct_ref_seq_dif.details' +4 4 'Structure model' '_database_2.pdbx_DOI' +5 4 'Structure model' '_database_2.pdbx_database_accession' +6 4 'Structure model' '_pdbx_entry_details.has_protein_modification' +7 4 'Structure model' '_struct_conn.pdbx_dist_value' +8 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id' +9 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id' +10 4 'Structure model' '_struct_conn.ptnr1_label_atom_id' +11 4 'Structure model' '_struct_conn.ptnr1_label_comp_id' +12 4 'Structure model' '_struct_conn.ptnr1_label_seq_id' +13 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id' +14 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id' +15 4 'Structure model' '_struct_conn.ptnr2_label_atom_id' +16 4 'Structure model' '_struct_conn.ptnr2_label_comp_id' +17 4 'Structure model' '_struct_conn.ptnr2_label_seq_id' +# +_pdbx_database_status.status_code REL +_pdbx_database_status.entry_id 4BDU +_pdbx_database_status.deposit_site PDBE +_pdbx_database_status.process_site PDBE +_pdbx_database_status.SG_entry . +_pdbx_database_status.recvd_initial_deposition_date 2012-10-08 +_pdbx_database_status.pdb_format_compatible Y +_pdbx_database_status.status_code_sf REL +_pdbx_database_status.status_code_mr ? +_pdbx_database_status.status_code_cs ? +_pdbx_database_status.methods_development_category ? +_pdbx_database_status.status_code_nmr_data ? +# +loop_ +_pdbx_database_related.db_name +_pdbx_database_related.db_id +_pdbx_database_related.content_type +_pdbx_database_related.details +PDB 4BD2 unspecified 'BAX DOMAIN SWAPPED DIMER IN COMPLEX WITH BIDBH3' +PDB 4BD6 unspecified 'BAX DOMAIN SWAPPED DIMER IN COMPLEX WITH BAXBH3' +PDB 4BD7 unspecified 'BAX DOMAIN SWAPPED DIMER INDUCED BY OCTYLMALTOSIDE' +PDB 4BD8 unspecified 'BAX DOMAIN SWAPPED DIMER INDUCED BY BIMBH3 WITH CHAPS' +# +loop_ +_audit_author.name +_audit_author.pdbx_ordinal +'Czabotar, P.E.' 1 +'Colman, P.M.' 2 +# +_citation.id primary +_citation.title +'Bax Crystal Structures Reveal How Bh3 Domains Activate Bax and Nucleate its Oligomerization to Induce Apoptosis.' +_citation.journal_abbrev 'Cell(Cambridge,Mass.)' +_citation.journal_volume 152 +_citation.page_first 519 +_citation.page_last ? +_citation.year 2013 +_citation.journal_id_ASTM CELLB5 +_citation.country US +_citation.journal_id_ISSN 0092-8674 +_citation.journal_id_CSD 0998 +_citation.book_publisher ? +_citation.pdbx_database_id_PubMed 23374347 +_citation.pdbx_database_id_DOI 10.1016/J.CELL.2012.12.031 +# +loop_ +_citation_author.citation_id +_citation_author.name +_citation_author.ordinal +_citation_author.identifier_ORCID +primary 'Czabotar, P.E.' 1 ? +primary 'Westphal, D.' 2 ? +primary 'Dewson, G.' 3 ? +primary 'Ma, S.' 4 ? +primary 'Hockings, C.' 5 ? +primary 'Fairlie, W.D.' 6 ? +primary 'Lee, E.F.' 7 ? +primary 'Yao, S.' 8 ? +primary 'Robin, A.Y.' 9 ? +primary 'Smith, B.J.' 10 ? +primary 'Huang, D.C.' 11 ? +primary 'Kluck, R.M.' 12 ? +primary 'Adams, J.M.' 13 ? +primary 'Colman, P.M.' 14 ? +# +loop_ +_entity.id +_entity.type +_entity.src_method +_entity.pdbx_description +_entity.formula_weight +_entity.pdbx_number_of_molecules +_entity.pdbx_ec +_entity.pdbx_mutation +_entity.pdbx_fragment +_entity.details +1 polymer man 'GREEN FLUORESCENT PROTEIN, APOPTOSIS REGULATOR BAX' 34908.332 4 ? YES 'BAX RESIDUES 53-128' ? +2 water nat water 18.015 84 ? ? ? ? +# +_entity_name_com.entity_id 1 +_entity_name_com.name 'GFP, BCL-2-LIKE PROTEIN 4, BCL2-L-4' +# +_entity_poly.entity_id 1 +_entity_poly.type 'polypeptide(L)' +_entity_poly.nstd_linkage no +_entity_poly.nstd_monomer yes +_entity_poly.pdbx_seq_one_letter_code +;GSHMSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTF(CR2)VQCFSRYP +DHMKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMAD +KQKNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSNLSKDPNEKRDHMVLLEFVTAAGITGSDAS +TKKLSESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALSTK +; +_entity_poly.pdbx_seq_one_letter_code_can +;GSHMSKGEELFTGVVPILVELDGDVNGHKFSVSGEGEGDATYGKLTLKFICTTGKLPVPWPTLVTTFGYGVQCFSRYPDH +MKQHDFFKSAMPEGYVQERTIFFKDDGNYKTRAEVKFEGDTLVNRIELKGIDFKEDGNILGHKLEYNYNSHNVYIMADKQ +KNGIKVNFKIRHNIEDGSVQLADHYQQNTPIGDGPVLLPDNHYLSTQSNLSKDPNEKRDHMVLLEFVTAAGITGSDASTK +KLSESLKRIGDELDSNMELQRMIAAVDTDSPREVFFRVAADMFSDGNFNWGRVVALFYFASKLVLKALSTK +; +_entity_poly.pdbx_strand_id A,B,C,D +_entity_poly.pdbx_target_identifier ? +# +_pdbx_entity_nonpoly.entity_id 2 +_pdbx_entity_nonpoly.name water +_pdbx_entity_nonpoly.comp_id HOH +# +loop_ +_entity_poly_seq.entity_id +_entity_poly_seq.num +_entity_poly_seq.mon_id +_entity_poly_seq.hetero +1 1 GLY n +1 2 SER n +1 3 HIS n +1 4 MET n +1 5 SER n +1 6 LYS n +1 7 GLY n +1 8 GLU n +1 9 GLU n +1 10 LEU n +1 11 PHE n +1 12 THR n +1 13 GLY n +1 14 VAL n +1 15 VAL n +1 16 PRO n +1 17 ILE n +1 18 LEU n +1 19 VAL n +1 20 GLU n +1 21 LEU n +1 22 ASP n +1 23 GLY n +1 24 ASP n +1 25 VAL n +1 26 ASN n +1 27 GLY n +1 28 HIS n +1 29 LYS n +1 30 PHE n +1 31 SER n +1 32 VAL n +1 33 SER n +1 34 GLY n +1 35 GLU n +1 36 GLY n +1 37 GLU n +1 38 GLY n +1 39 ASP n +1 40 ALA n +1 41 THR n +1 42 TYR n +1 43 GLY n +1 44 LYS n +1 45 LEU n +1 46 THR n +1 47 LEU n +1 48 LYS n +1 49 PHE n +1 50 ILE n +1 51 CYS n +1 52 THR n +1 53 THR n +1 54 GLY n +1 55 LYS n +1 56 LEU n +1 57 PRO n +1 58 VAL n +1 59 PRO n +1 60 TRP n +1 61 PRO n +1 62 THR n +1 63 LEU n +1 64 VAL n +1 65 THR n +1 66 THR n +1 67 PHE n +1 68 CR2 n +1 69 VAL n +1 70 GLN n +1 71 CYS n +1 72 PHE n +1 73 SER n +1 74 ARG n +1 75 TYR n +1 76 PRO n +1 77 ASP n +1 78 HIS n +1 79 MET n +1 80 LYS n +1 81 GLN n +1 82 HIS n +1 83 ASP n +1 84 PHE n +1 85 PHE n +1 86 LYS n +1 87 SER n +1 88 ALA n +1 89 MET n +1 90 PRO n +1 91 GLU n +1 92 GLY n +1 93 TYR n +1 94 VAL n +1 95 GLN n +1 96 GLU n +1 97 ARG n +1 98 THR n +1 99 ILE n +1 100 PHE n +1 101 PHE n +1 102 LYS n +1 103 ASP n +1 104 ASP n +1 105 GLY n +1 106 ASN n +1 107 TYR n +1 108 LYS n +1 109 THR n +1 110 ARG n +1 111 ALA n +1 112 GLU n +1 113 VAL n +1 114 LYS n +1 115 PHE n +1 116 GLU n +1 117 GLY n +1 118 ASP n +1 119 THR n +1 120 LEU n +1 121 VAL n +1 122 ASN n +1 123 ARG n +1 124 ILE n +1 125 GLU n +1 126 LEU n +1 127 LYS n +1 128 GLY n +1 129 ILE n +1 130 ASP n +1 131 PHE n +1 132 LYS n +1 133 GLU n +1 134 ASP n +1 135 GLY n +1 136 ASN n +1 137 ILE n +1 138 LEU n +1 139 GLY n +1 140 HIS n +1 141 LYS n +1 142 LEU n +1 143 GLU n +1 144 TYR n +1 145 ASN n +1 146 TYR n +1 147 ASN n +1 148 SER n +1 149 HIS n +1 150 ASN n +1 151 VAL n +1 152 TYR n +1 153 ILE n +1 154 MET n +1 155 ALA n +1 156 ASP n +1 157 LYS n +1 158 GLN n +1 159 LYS n +1 160 ASN n +1 161 GLY n +1 162 ILE n +1 163 LYS n +1 164 VAL n +1 165 ASN n +1 166 PHE n +1 167 LYS n +1 168 ILE n +1 169 ARG n +1 170 HIS n +1 171 ASN n +1 172 ILE n +1 173 GLU n +1 174 ASP n +1 175 GLY n +1 176 SER n +1 177 VAL n +1 178 GLN n +1 179 LEU n +1 180 ALA n +1 181 ASP n +1 182 HIS n +1 183 TYR n +1 184 GLN n +1 185 GLN n +1 186 ASN n +1 187 THR n +1 188 PRO n +1 189 ILE n +1 190 GLY n +1 191 ASP n +1 192 GLY n +1 193 PRO n +1 194 VAL n +1 195 LEU n +1 196 LEU n +1 197 PRO n +1 198 ASP n +1 199 ASN n +1 200 HIS n +1 201 TYR n +1 202 LEU n +1 203 SER n +1 204 THR n +1 205 GLN n +1 206 SER n +1 207 ASN n +1 208 LEU n +1 209 SER n +1 210 LYS n +1 211 ASP n +1 212 PRO n +1 213 ASN n +1 214 GLU n +1 215 LYS n +1 216 ARG n +1 217 ASP n +1 218 HIS n +1 219 MET n +1 220 VAL n +1 221 LEU n +1 222 LEU n +1 223 GLU n +1 224 PHE n +1 225 VAL n +1 226 THR n +1 227 ALA n +1 228 ALA n +1 229 GLY n +1 230 ILE n +1 231 THR n +1 232 GLY n +1 233 SER n +1 234 ASP n +1 235 ALA n +1 236 SER n +1 237 THR n +1 238 LYS n +1 239 LYS n +1 240 LEU n +1 241 SER n +1 242 GLU n +1 243 SER n +1 244 LEU n +1 245 LYS n +1 246 ARG n +1 247 ILE n +1 248 GLY n +1 249 ASP n +1 250 GLU n +1 251 LEU n +1 252 ASP n +1 253 SER n +1 254 ASN n +1 255 MET n +1 256 GLU n +1 257 LEU n +1 258 GLN n +1 259 ARG n +1 260 MET n +1 261 ILE n +1 262 ALA n +1 263 ALA n +1 264 VAL n +1 265 ASP n +1 266 THR n +1 267 ASP n +1 268 SER n +1 269 PRO n +1 270 ARG n +1 271 GLU n +1 272 VAL n +1 273 PHE n +1 274 PHE n +1 275 ARG n +1 276 VAL n +1 277 ALA n +1 278 ALA n +1 279 ASP n +1 280 MET n +1 281 PHE n +1 282 SER n +1 283 ASP n +1 284 GLY n +1 285 ASN n +1 286 PHE n +1 287 ASN n +1 288 TRP n +1 289 GLY n +1 290 ARG n +1 291 VAL n +1 292 VAL n +1 293 ALA n +1 294 LEU n +1 295 PHE n +1 296 TYR n +1 297 PHE n +1 298 ALA n +1 299 SER n +1 300 LYS n +1 301 LEU n +1 302 VAL n +1 303 LEU n +1 304 LYS n +1 305 ALA n +1 306 LEU n +1 307 SER n +1 308 THR n +1 309 LYS n +# +loop_ +_entity_src_gen.entity_id +_entity_src_gen.pdbx_src_id +_entity_src_gen.pdbx_alt_source_flag +_entity_src_gen.pdbx_seq_type +_entity_src_gen.pdbx_beg_seq_num +_entity_src_gen.pdbx_end_seq_num +_entity_src_gen.gene_src_common_name +_entity_src_gen.gene_src_genus +_entity_src_gen.pdbx_gene_src_gene +_entity_src_gen.gene_src_species +_entity_src_gen.gene_src_strain +_entity_src_gen.gene_src_tissue +_entity_src_gen.gene_src_tissue_fraction +_entity_src_gen.gene_src_details +_entity_src_gen.pdbx_gene_src_fragment +_entity_src_gen.pdbx_gene_src_scientific_name +_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id +_entity_src_gen.pdbx_gene_src_variant +_entity_src_gen.pdbx_gene_src_cell_line +_entity_src_gen.pdbx_gene_src_atcc +_entity_src_gen.pdbx_gene_src_organ +_entity_src_gen.pdbx_gene_src_organelle +_entity_src_gen.pdbx_gene_src_cell +_entity_src_gen.pdbx_gene_src_cellular_location +_entity_src_gen.host_org_common_name +_entity_src_gen.pdbx_host_org_scientific_name +_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id +_entity_src_gen.host_org_genus +_entity_src_gen.pdbx_host_org_gene +_entity_src_gen.pdbx_host_org_organ +_entity_src_gen.host_org_species +_entity_src_gen.pdbx_host_org_tissue +_entity_src_gen.pdbx_host_org_tissue_fraction +_entity_src_gen.pdbx_host_org_strain +_entity_src_gen.pdbx_host_org_variant +_entity_src_gen.pdbx_host_org_cell_line +_entity_src_gen.pdbx_host_org_atcc +_entity_src_gen.pdbx_host_org_culture_collection +_entity_src_gen.pdbx_host_org_cell +_entity_src_gen.pdbx_host_org_organelle +_entity_src_gen.pdbx_host_org_cellular_location +_entity_src_gen.pdbx_host_org_vector_type +_entity_src_gen.pdbx_host_org_vector +_entity_src_gen.host_org_details +_entity_src_gen.expression_system_id +_entity_src_gen.plasmid_name +_entity_src_gen.plasmid_details +_entity_src_gen.pdbx_description +1 1 sample ? 4 231 ? ? ? ? ? ? ? ? ? 'AEQUOREA VICTORIA' 6100 ? ? ? ? ? ? ? ? 'ESCHERICHIA COLI' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? +PLASMID ? ? ? PET-22B ? ? +1 2 sample ? 234 309 ? ? ? ? ? ? ? ? ? 'HOMO SAPIENS' 9606 ? ? ? ? ? ? ? ? 'ESCHERICHIA COLI' 562 ? ? ? ? ? ? ? ? ? ? ? ? ? ? +PLASMID ? ? ? PET-22B ? ? +# +loop_ +_chem_comp.id +_chem_comp.type +_chem_comp.mon_nstd_flag +_chem_comp.name +_chem_comp.pdbx_synonyms +_chem_comp.formula +_chem_comp.formula_weight +ALA 'L-peptide linking' y ALANINE +? 'C3 H7 N O2' 89.093 +ARG 'L-peptide linking' y ARGININE +? 'C6 H15 N4 O2 1' 175.209 +ASN 'L-peptide linking' y ASPARAGINE +? 'C4 H8 N2 O3' 132.118 +ASP 'L-peptide linking' y 'ASPARTIC ACID' +? 'C4 H7 N O4' 133.103 +CR2 'L-peptide linking' n '{(4Z)-2-(aminomethyl)-4-[(4-hydroxyphenyl)methylidene]-5-oxo-4,5-dihydro-1H-imidazol-1-yl}acetic acid' +'CHROMOPHORE (GLY-TYR-GLY)' 'C13 H13 N3 O4' 275.260 +CYS 'L-peptide linking' y CYSTEINE +? 'C3 H7 N O2 S' 121.158 +GLN 'L-peptide linking' y GLUTAMINE +? 'C5 H10 N2 O3' 146.144 +GLU 'L-peptide linking' y 'GLUTAMIC ACID' +? 'C5 H9 N O4' 147.129 +GLY 'peptide linking' y GLYCINE +? 'C2 H5 N O2' 75.067 +HIS 'L-peptide linking' y HISTIDINE +? 'C6 H10 N3 O2 1' 156.162 +HOH non-polymer . WATER +? 'H2 O' 18.015 +ILE 'L-peptide linking' y ISOLEUCINE +? 'C6 H13 N O2' 131.173 +LEU 'L-peptide linking' y LEUCINE +? 'C6 H13 N O2' 131.173 +LYS 'L-peptide linking' y LYSINE +? 'C6 H15 N2 O2 1' 147.195 +MET 'L-peptide linking' y METHIONINE +? 'C5 H11 N O2 S' 149.211 +PHE 'L-peptide linking' y PHENYLALANINE +? 'C9 H11 N O2' 165.189 +PRO 'L-peptide linking' y PROLINE +? 'C5 H9 N O2' 115.130 +SER 'L-peptide linking' y SERINE +? 'C3 H7 N O3' 105.093 +THR 'L-peptide linking' y THREONINE +? 'C4 H9 N O3' 119.119 +TRP 'L-peptide linking' y TRYPTOPHAN +? 'C11 H12 N2 O2' 204.225 +TYR 'L-peptide linking' y TYROSINE +? 'C9 H11 N O3' 181.189 +VAL 'L-peptide linking' y VALINE +? 'C5 H11 N O2' 117.146 +# +loop_ +_pdbx_poly_seq_scheme.asym_id +_pdbx_poly_seq_scheme.entity_id +_pdbx_poly_seq_scheme.seq_id +_pdbx_poly_seq_scheme.mon_id +_pdbx_poly_seq_scheme.ndb_seq_num +_pdbx_poly_seq_scheme.pdb_seq_num +_pdbx_poly_seq_scheme.auth_seq_num +_pdbx_poly_seq_scheme.pdb_mon_id +_pdbx_poly_seq_scheme.auth_mon_id +_pdbx_poly_seq_scheme.pdb_strand_id +_pdbx_poly_seq_scheme.pdb_ins_code +_pdbx_poly_seq_scheme.hetero +A 1 1 GLY 1 -2 ? ? ? A . n +A 1 2 SER 2 -1 ? ? ? A . n +A 1 3 HIS 3 0 ? ? ? A . n +A 1 4 MET 4 1 ? ? ? A . n +A 1 5 SER 5 2 2 SER SER A . n +A 1 6 LYS 6 3 3 LYS LYS A . n +A 1 7 GLY 7 4 4 GLY GLY A . n +A 1 8 GLU 8 5 5 GLU GLU A . n +A 1 9 GLU 9 6 6 GLU GLU A . n +A 1 10 LEU 10 7 7 LEU LEU A . n +A 1 11 PHE 11 8 8 PHE PHE A . n +A 1 12 THR 12 9 9 THR THR A . n +A 1 13 GLY 13 10 10 GLY GLY A . n +A 1 14 VAL 14 11 11 VAL VAL A . n +A 1 15 VAL 15 12 12 VAL VAL A . n +A 1 16 PRO 16 13 13 PRO PRO A . n +A 1 17 ILE 17 14 14 ILE ILE A . n +A 1 18 LEU 18 15 15 LEU LEU A . n +A 1 19 VAL 19 16 16 VAL VAL A . n +A 1 20 GLU 20 17 17 GLU GLU A . n +A 1 21 LEU 21 18 18 LEU LEU A . n +A 1 22 ASP 22 19 19 ASP ASP A . n +A 1 23 GLY 23 20 20 GLY GLY A . n +A 1 24 ASP 24 21 21 ASP ASP A . n +A 1 25 VAL 25 22 22 VAL VAL A . n +A 1 26 ASN 26 23 23 ASN ASN A . n +A 1 27 GLY 27 24 24 GLY GLY A . n +A 1 28 HIS 28 25 25 HIS HIS A . n +A 1 29 LYS 29 26 26 LYS LYS A . n +A 1 30 PHE 30 27 27 PHE PHE A . n +A 1 31 SER 31 28 28 SER SER A . n +A 1 32 VAL 32 29 29 VAL VAL A . n +A 1 33 SER 33 30 30 SER SER A . n +A 1 34 GLY 34 31 31 GLY GLY A . n +A 1 35 GLU 35 32 32 GLU GLU A . n +A 1 36 GLY 36 33 33 GLY GLY A . n +A 1 37 GLU 37 34 34 GLU GLU A . n +A 1 38 GLY 38 35 35 GLY GLY A . n +A 1 39 ASP 39 36 36 ASP ASP A . n +A 1 40 ALA 40 37 37 ALA ALA A . n +A 1 41 THR 41 38 38 THR THR A . n +A 1 42 TYR 42 39 39 TYR TYR A . n +A 1 43 GLY 43 40 40 GLY GLY A . n +A 1 44 LYS 44 41 41 LYS LYS A . n +A 1 45 LEU 45 42 42 LEU LEU A . n +A 1 46 THR 46 43 43 THR THR A . n +A 1 47 LEU 47 44 44 LEU LEU A . n +A 1 48 LYS 48 45 45 LYS LYS A . n +A 1 49 PHE 49 46 46 PHE PHE A . n +A 1 50 ILE 50 47 47 ILE ILE A . n +A 1 51 CYS 51 48 48 CYS CYS A . n +A 1 52 THR 52 49 49 THR THR A . n +A 1 53 THR 53 50 50 THR THR A . n +A 1 54 GLY 54 51 51 GLY GLY A . n +A 1 55 LYS 55 52 52 LYS LYS A . n +A 1 56 LEU 56 53 53 LEU LEU A . n +A 1 57 PRO 57 54 54 PRO PRO A . n +A 1 58 VAL 58 55 55 VAL VAL A . n +A 1 59 PRO 59 56 56 PRO PRO A . n +A 1 60 TRP 60 57 57 TRP TRP A . n +A 1 61 PRO 61 58 58 PRO PRO A . n +A 1 62 THR 62 59 59 THR THR A . n +A 1 63 LEU 63 60 60 LEU LEU A . n +A 1 64 VAL 64 61 61 VAL VAL A . n +A 1 65 THR 65 62 62 THR THR A . n +A 1 66 THR 66 63 63 THR THR A . n +A 1 67 PHE 67 64 64 PHE PHE A . n +A 1 68 CR2 68 65 65 CR2 CR2 A . n +A 1 69 VAL 69 68 68 VAL VAL A . n +A 1 70 GLN 70 69 69 GLN GLN A . n +A 1 71 CYS 71 70 70 CYS CYS A . n +A 1 72 PHE 72 71 71 PHE PHE A . n +A 1 73 SER 73 72 72 SER SER A . n +A 1 74 ARG 74 73 73 ARG ARG A . n +A 1 75 TYR 75 74 74 TYR TYR A . n +A 1 76 PRO 76 75 75 PRO PRO A . n +A 1 77 ASP 77 76 76 ASP ASP A . n +A 1 78 HIS 78 77 77 HIS HIS A . n +A 1 79 MET 79 78 78 MET MET A . n +A 1 80 LYS 80 79 79 LYS LYS A . n +A 1 81 GLN 81 80 80 GLN GLN A . n +A 1 82 HIS 82 81 81 HIS HIS A . n +A 1 83 ASP 83 82 82 ASP ASP A . n +A 1 84 PHE 84 83 83 PHE PHE A . n +A 1 85 PHE 85 84 84 PHE PHE A . n +A 1 86 LYS 86 85 85 LYS LYS A . n +A 1 87 SER 87 86 86 SER SER A . n +A 1 88 ALA 88 87 87 ALA ALA A . n +A 1 89 MET 89 88 88 MET MET A . n +A 1 90 PRO 90 89 89 PRO PRO A . n +A 1 91 GLU 91 90 90 GLU GLU A . n +A 1 92 GLY 92 91 91 GLY GLY A . n +A 1 93 TYR 93 92 92 TYR TYR A . n +A 1 94 VAL 94 93 93 VAL VAL A . n +A 1 95 GLN 95 94 94 GLN GLN A . n +A 1 96 GLU 96 95 95 GLU GLU A . n +A 1 97 ARG 97 96 96 ARG ARG A . n +A 1 98 THR 98 97 97 THR THR A . n +A 1 99 ILE 99 98 98 ILE ILE A . n +A 1 100 PHE 100 99 99 PHE PHE A . n +A 1 101 PHE 101 100 100 PHE PHE A . n +A 1 102 LYS 102 101 101 LYS LYS A . n +A 1 103 ASP 103 102 102 ASP ASP A . n +A 1 104 ASP 104 103 103 ASP ASP A . n +A 1 105 GLY 105 104 104 GLY GLY A . n +A 1 106 ASN 106 105 105 ASN ASN A . n +A 1 107 TYR 107 106 106 TYR TYR A . n +A 1 108 LYS 108 107 107 LYS LYS A . n +A 1 109 THR 109 108 108 THR THR A . n +A 1 110 ARG 110 109 109 ARG ARG A . n +A 1 111 ALA 111 110 110 ALA ALA A . n +A 1 112 GLU 112 111 111 GLU GLU A . n +A 1 113 VAL 113 112 112 VAL VAL A . n +A 1 114 LYS 114 113 113 LYS LYS A . n +A 1 115 PHE 115 114 114 PHE PHE A . n +A 1 116 GLU 116 115 115 GLU GLU A . n +A 1 117 GLY 117 116 116 GLY GLY A . n +A 1 118 ASP 118 117 117 ASP ASP A . n +A 1 119 THR 119 118 118 THR THR A . n +A 1 120 LEU 120 119 119 LEU LEU A . n +A 1 121 VAL 121 120 120 VAL VAL A . n +A 1 122 ASN 122 121 121 ASN ASN A . n +A 1 123 ARG 123 122 122 ARG ARG A . n +A 1 124 ILE 124 123 123 ILE ILE A . n +A 1 125 GLU 125 124 124 GLU GLU A . n +A 1 126 LEU 126 125 125 LEU LEU A . n +A 1 127 LYS 127 126 126 LYS LYS A . n +A 1 128 GLY 128 127 127 GLY GLY A . n +A 1 129 ILE 129 128 128 ILE ILE A . n +A 1 130 ASP 130 129 129 ASP ASP A . n +A 1 131 PHE 131 130 130 PHE PHE A . n +A 1 132 LYS 132 131 131 LYS LYS A . n +A 1 133 GLU 133 132 132 GLU GLU A . n +A 1 134 ASP 134 133 133 ASP ASP A . n +A 1 135 GLY 135 134 134 GLY GLY A . n +A 1 136 ASN 136 135 135 ASN ASN A . n +A 1 137 ILE 137 136 136 ILE ILE A . n +A 1 138 LEU 138 137 137 LEU LEU A . n +A 1 139 GLY 139 138 138 GLY GLY A . n +A 1 140 HIS 140 139 139 HIS HIS A . n +A 1 141 LYS 141 140 140 LYS LYS A . n +A 1 142 LEU 142 141 141 LEU LEU A . n +A 1 143 GLU 143 142 142 GLU GLU A . n +A 1 144 TYR 144 143 143 TYR TYR A . n +A 1 145 ASN 145 144 144 ASN ASN A . n +A 1 146 TYR 146 145 145 TYR TYR A . n +A 1 147 ASN 147 146 146 ASN ASN A . n +A 1 148 SER 148 147 147 SER SER A . n +A 1 149 HIS 149 148 148 HIS HIS A . n +A 1 150 ASN 150 149 149 ASN ASN A . n +A 1 151 VAL 151 150 150 VAL VAL A . n +A 1 152 TYR 152 151 151 TYR TYR A . n +A 1 153 ILE 153 152 152 ILE ILE A . n +A 1 154 MET 154 153 153 MET MET A . n +A 1 155 ALA 155 154 154 ALA ALA A . n +A 1 156 ASP 156 155 155 ASP ASP A . n +A 1 157 LYS 157 156 156 LYS LYS A . n +A 1 158 GLN 158 157 157 GLN GLN A . n +A 1 159 LYS 159 158 158 LYS LYS A . n +A 1 160 ASN 160 159 159 ASN ASN A . n +A 1 161 GLY 161 160 160 GLY GLY A . n +A 1 162 ILE 162 161 161 ILE ILE A . n +A 1 163 LYS 163 162 162 LYS LYS A . n +A 1 164 VAL 164 163 163 VAL VAL A . n +A 1 165 ASN 165 164 164 ASN ASN A . n +A 1 166 PHE 166 165 165 PHE PHE A . n +A 1 167 LYS 167 166 166 LYS LYS A . n +A 1 168 ILE 168 167 167 ILE ILE A . n +A 1 169 ARG 169 168 168 ARG ARG A . n +A 1 170 HIS 170 169 169 HIS HIS A . n +A 1 171 ASN 171 170 170 ASN ASN A . n +A 1 172 ILE 172 171 171 ILE ILE A . n +A 1 173 GLU 173 172 172 GLU GLU A . n +A 1 174 ASP 174 173 173 ASP ASP A . n +A 1 175 GLY 175 174 174 GLY GLY A . n +A 1 176 SER 176 175 175 SER SER A . n +A 1 177 VAL 177 176 176 VAL VAL A . n +A 1 178 GLN 178 177 177 GLN GLN A . n +A 1 179 LEU 179 178 178 LEU LEU A . n +A 1 180 ALA 180 179 179 ALA ALA A . n +A 1 181 ASP 181 180 180 ASP ASP A . n +A 1 182 HIS 182 181 181 HIS HIS A . n +A 1 183 TYR 183 182 182 TYR TYR A . n +A 1 184 GLN 184 183 183 GLN GLN A . n +A 1 185 GLN 185 184 184 GLN GLN A . n +A 1 186 ASN 186 185 185 ASN ASN A . n +A 1 187 THR 187 186 186 THR THR A . n +A 1 188 PRO 188 187 187 PRO PRO A . n +A 1 189 ILE 189 188 188 ILE ILE A . n +A 1 190 GLY 190 189 189 GLY GLY A . n +A 1 191 ASP 191 190 190 ASP ASP A . n +A 1 192 GLY 192 191 191 GLY GLY A . n +A 1 193 PRO 193 192 192 PRO PRO A . n +A 1 194 VAL 194 193 193 VAL VAL A . n +A 1 195 LEU 195 194 194 LEU LEU A . n +A 1 196 LEU 196 195 195 LEU LEU A . n +A 1 197 PRO 197 196 196 PRO PRO A . n +A 1 198 ASP 198 197 197 ASP ASP A . n +A 1 199 ASN 199 198 198 ASN ASN A . n +A 1 200 HIS 200 199 199 HIS HIS A . n +A 1 201 TYR 201 200 200 TYR TYR A . n +A 1 202 LEU 202 201 201 LEU LEU A . n +A 1 203 SER 203 202 202 SER SER A . n +A 1 204 THR 204 203 203 THR THR A . n +A 1 205 GLN 205 204 204 GLN GLN A . n +A 1 206 SER 206 205 205 SER SER A . n +A 1 207 ASN 207 206 206 ASN ASN A . n +A 1 208 LEU 208 207 207 LEU LEU A . n +A 1 209 SER 209 208 208 SER SER A . n +A 1 210 LYS 210 209 209 LYS LYS A . n +A 1 211 ASP 211 210 210 ASP ASP A . n +A 1 212 PRO 212 211 211 PRO PRO A . n +A 1 213 ASN 213 212 212 ASN ASN A . n +A 1 214 GLU 214 213 213 GLU GLU A . n +A 1 215 LYS 215 214 214 LYS LYS A . n +A 1 216 ARG 216 215 215 ARG ARG A . n +A 1 217 ASP 217 216 216 ASP ASP A . n +A 1 218 HIS 218 217 217 HIS HIS A . n +A 1 219 MET 219 218 218 MET MET A . n +A 1 220 VAL 220 219 219 VAL VAL A . n +A 1 221 LEU 221 220 220 LEU LEU A . n +A 1 222 LEU 222 221 221 LEU LEU A . n +A 1 223 GLU 223 222 222 GLU GLU A . n +A 1 224 PHE 224 223 223 PHE PHE A . n +A 1 225 VAL 225 224 224 VAL VAL A . n +A 1 226 THR 226 225 225 THR THR A . n +A 1 227 ALA 227 226 226 ALA ALA A . n +A 1 228 ALA 228 227 227 ALA ALA A . n +A 1 229 GLY 229 228 228 GLY GLY A . n +A 1 230 ILE 230 229 229 ILE ILE A . n +A 1 231 THR 231 230 230 THR THR A . n +A 1 232 GLY 232 231 ? ? ? A . n +A 1 233 SER 233 232 ? ? ? A . n +A 1 234 ASP 234 1053 ? ? ? A . n +A 1 235 ALA 235 1054 1054 ALA ALA A . n +A 1 236 SER 236 1055 1055 SER SER A . n +A 1 237 THR 237 1056 1056 THR THR A . n +A 1 238 LYS 238 1057 1057 LYS LYS A . n +A 1 239 LYS 239 1058 1058 LYS LYS A . n +A 1 240 LEU 240 1059 1059 LEU LEU A . n +A 1 241 SER 241 1060 1060 SER SER A . n +A 1 242 GLU 242 1061 1061 GLU GLU A . n +A 1 243 SER 243 1062 1062 SER SER A . n +A 1 244 LEU 244 1063 1063 LEU LEU A . n +A 1 245 LYS 245 1064 1064 LYS LYS A . n +A 1 246 ARG 246 1065 1065 ARG ARG A . n +A 1 247 ILE 247 1066 1066 ILE ILE A . n +A 1 248 GLY 248 1067 1067 GLY GLY A . n +A 1 249 ASP 249 1068 1068 ASP ASP A . n +A 1 250 GLU 250 1069 1069 GLU GLU A . n +A 1 251 LEU 251 1070 1070 LEU LEU A . n +A 1 252 ASP 252 1071 1071 ASP ASP A . n +A 1 253 SER 253 1072 1072 SER SER A . n +A 1 254 ASN 254 1073 1073 ASN ASN A . n +A 1 255 MET 255 1074 1074 MET MET A . n +A 1 256 GLU 256 1075 1075 GLU GLU A . n +A 1 257 LEU 257 1076 1076 LEU LEU A . n +A 1 258 GLN 258 1077 1077 GLN GLN A . n +A 1 259 ARG 259 1078 1078 ARG ARG A . n +A 1 260 MET 260 1079 1079 MET MET A . n +A 1 261 ILE 261 1080 1080 ILE ILE A . n +A 1 262 ALA 262 1081 1081 ALA ALA A . n +A 1 263 ALA 263 1082 1082 ALA ALA A . n +A 1 264 VAL 264 1083 1083 VAL VAL A . n +A 1 265 ASP 265 1084 1084 ASP ASP A . n +A 1 266 THR 266 1085 1085 THR THR A . n +A 1 267 ASP 267 1086 1086 ASP ASP A . n +A 1 268 SER 268 1087 1087 SER SER A . n +A 1 269 PRO 269 1088 1088 PRO PRO A . n +A 1 270 ARG 270 1089 1089 ARG ARG A . n +A 1 271 GLU 271 1090 1090 GLU GLU A . n +A 1 272 VAL 272 1091 1091 VAL VAL A . n +A 1 273 PHE 273 1092 1092 PHE PHE A . n +A 1 274 PHE 274 1093 1093 PHE PHE A . n +A 1 275 ARG 275 1094 1094 ARG ARG A . n +A 1 276 VAL 276 1095 1095 VAL VAL A . n +A 1 277 ALA 277 1096 1096 ALA ALA A . n +A 1 278 ALA 278 1097 1097 ALA ALA A . n +A 1 279 ASP 279 1098 1098 ASP ASP A . n +A 1 280 MET 280 1099 1099 MET MET A . n +A 1 281 PHE 281 1100 1100 PHE PHE A . n +A 1 282 SER 282 1101 1101 SER SER A . n +A 1 283 ASP 283 1102 1102 ASP ASP A . n +A 1 284 GLY 284 1103 1103 GLY GLY A . n +A 1 285 ASN 285 1104 1104 ASN ASN A . n +A 1 286 PHE 286 1105 1105 PHE PHE A . n +A 1 287 ASN 287 1106 1106 ASN ASN A . n +A 1 288 TRP 288 1107 1107 TRP TRP A . n +A 1 289 GLY 289 1108 1108 GLY GLY A . n +A 1 290 ARG 290 1109 1109 ARG ARG A . n +A 1 291 VAL 291 1110 1110 VAL VAL A . n +A 1 292 VAL 292 1111 1111 VAL VAL A . n +A 1 293 ALA 293 1112 1112 ALA ALA A . n +A 1 294 LEU 294 1113 1113 LEU LEU A . n +A 1 295 PHE 295 1114 1114 PHE PHE A . n +A 1 296 TYR 296 1115 1115 TYR TYR A . n +A 1 297 PHE 297 1116 1116 PHE PHE A . n +A 1 298 ALA 298 1117 1117 ALA ALA A . n +A 1 299 SER 299 1118 1118 SER SER A . n +A 1 300 LYS 300 1119 1119 LYS LYS A . n +A 1 301 LEU 301 1120 1120 LEU LEU A . n +A 1 302 VAL 302 1121 1121 VAL VAL A . n +A 1 303 LEU 303 1122 1122 LEU LEU A . n +A 1 304 LYS 304 1123 ? ? ? A . n +A 1 305 ALA 305 1124 ? ? ? A . n +A 1 306 LEU 306 1125 ? ? ? A . n +A 1 307 SER 307 1126 ? ? ? A . n +A 1 308 THR 308 1127 ? ? ? A . n +A 1 309 LYS 309 1128 ? ? ? A . n +B 1 1 GLY 1 -2 ? ? ? B . n +B 1 2 SER 2 -1 ? ? ? B . n +B 1 3 HIS 3 0 ? ? ? B . n +B 1 4 MET 4 1 ? ? ? B . n +B 1 5 SER 5 2 2 SER SER B . n +B 1 6 LYS 6 3 3 LYS LYS B . n +B 1 7 GLY 7 4 4 GLY GLY B . n +B 1 8 GLU 8 5 5 GLU GLU B . n +B 1 9 GLU 9 6 6 GLU GLU B . n +B 1 10 LEU 10 7 7 LEU LEU B . n +B 1 11 PHE 11 8 8 PHE PHE B . n +B 1 12 THR 12 9 9 THR THR B . n +B 1 13 GLY 13 10 10 GLY GLY B . n +B 1 14 VAL 14 11 11 VAL VAL B . n +B 1 15 VAL 15 12 12 VAL VAL B . n +B 1 16 PRO 16 13 13 PRO PRO B . n +B 1 17 ILE 17 14 14 ILE ILE B . n +B 1 18 LEU 18 15 15 LEU LEU B . n +B 1 19 VAL 19 16 16 VAL VAL B . n +B 1 20 GLU 20 17 17 GLU GLU B . n +B 1 21 LEU 21 18 18 LEU LEU B . n +B 1 22 ASP 22 19 19 ASP ASP B . n +B 1 23 GLY 23 20 20 GLY GLY B . n +B 1 24 ASP 24 21 21 ASP ASP B . n +B 1 25 VAL 25 22 22 VAL VAL B . n +B 1 26 ASN 26 23 23 ASN ASN B . n +B 1 27 GLY 27 24 24 GLY GLY B . n +B 1 28 HIS 28 25 25 HIS HIS B . n +B 1 29 LYS 29 26 26 LYS LYS B . n +B 1 30 PHE 30 27 27 PHE PHE B . n +B 1 31 SER 31 28 28 SER SER B . n +B 1 32 VAL 32 29 29 VAL VAL B . n +B 1 33 SER 33 30 30 SER SER B . n +B 1 34 GLY 34 31 31 GLY GLY B . n +B 1 35 GLU 35 32 32 GLU GLU B . n +B 1 36 GLY 36 33 33 GLY GLY B . n +B 1 37 GLU 37 34 34 GLU GLU B . n +B 1 38 GLY 38 35 35 GLY GLY B . n +B 1 39 ASP 39 36 36 ASP ASP B . n +B 1 40 ALA 40 37 37 ALA ALA B . n +B 1 41 THR 41 38 38 THR THR B . n +B 1 42 TYR 42 39 39 TYR TYR B . n +B 1 43 GLY 43 40 40 GLY GLY B . n +B 1 44 LYS 44 41 41 LYS LYS B . n +B 1 45 LEU 45 42 42 LEU LEU B . n +B 1 46 THR 46 43 43 THR THR B . n +B 1 47 LEU 47 44 44 LEU LEU B . n +B 1 48 LYS 48 45 45 LYS LYS B . n +B 1 49 PHE 49 46 46 PHE PHE B . n +B 1 50 ILE 50 47 47 ILE ILE B . n +B 1 51 CYS 51 48 48 CYS CYS B . n +B 1 52 THR 52 49 49 THR THR B . n +B 1 53 THR 53 50 50 THR THR B . n +B 1 54 GLY 54 51 51 GLY GLY B . n +B 1 55 LYS 55 52 52 LYS LYS B . n +B 1 56 LEU 56 53 53 LEU LEU B . n +B 1 57 PRO 57 54 54 PRO PRO B . n +B 1 58 VAL 58 55 55 VAL VAL B . n +B 1 59 PRO 59 56 56 PRO PRO B . n +B 1 60 TRP 60 57 57 TRP TRP B . n +B 1 61 PRO 61 58 58 PRO PRO B . n +B 1 62 THR 62 59 59 THR THR B . n +B 1 63 LEU 63 60 60 LEU LEU B . n +B 1 64 VAL 64 61 61 VAL VAL B . n +B 1 65 THR 65 62 62 THR THR B . n +B 1 66 THR 66 63 63 THR THR B . n +B 1 67 PHE 67 64 64 PHE PHE B . n +B 1 68 CR2 68 65 65 CR2 CR2 B . n +B 1 69 VAL 69 68 68 VAL VAL B . n +B 1 70 GLN 70 69 69 GLN GLN B . n +B 1 71 CYS 71 70 70 CYS CYS B . n +B 1 72 PHE 72 71 71 PHE PHE B . n +B 1 73 SER 73 72 72 SER SER B . n +B 1 74 ARG 74 73 73 ARG ARG B . n +B 1 75 TYR 75 74 74 TYR TYR B . n +B 1 76 PRO 76 75 75 PRO PRO B . n +B 1 77 ASP 77 76 76 ASP ASP B . n +B 1 78 HIS 78 77 77 HIS HIS B . n +B 1 79 MET 79 78 78 MET MET B . n +B 1 80 LYS 80 79 79 LYS LYS B . n +B 1 81 GLN 81 80 80 GLN GLN B . n +B 1 82 HIS 82 81 81 HIS HIS B . n +B 1 83 ASP 83 82 82 ASP ASP B . n +B 1 84 PHE 84 83 83 PHE PHE B . n +B 1 85 PHE 85 84 84 PHE PHE B . n +B 1 86 LYS 86 85 85 LYS LYS B . n +B 1 87 SER 87 86 86 SER SER B . n +B 1 88 ALA 88 87 87 ALA ALA B . n +B 1 89 MET 89 88 88 MET MET B . n +B 1 90 PRO 90 89 89 PRO PRO B . n +B 1 91 GLU 91 90 90 GLU GLU B . n +B 1 92 GLY 92 91 91 GLY GLY B . n +B 1 93 TYR 93 92 92 TYR TYR B . n +B 1 94 VAL 94 93 93 VAL VAL B . n +B 1 95 GLN 95 94 94 GLN GLN B . n +B 1 96 GLU 96 95 95 GLU GLU B . n +B 1 97 ARG 97 96 96 ARG ARG B . n +B 1 98 THR 98 97 97 THR THR B . n +B 1 99 ILE 99 98 98 ILE ILE B . n +B 1 100 PHE 100 99 99 PHE PHE B . n +B 1 101 PHE 101 100 100 PHE PHE B . n +B 1 102 LYS 102 101 101 LYS LYS B . n +B 1 103 ASP 103 102 102 ASP ASP B . n +B 1 104 ASP 104 103 103 ASP ASP B . n +B 1 105 GLY 105 104 104 GLY GLY B . n +B 1 106 ASN 106 105 105 ASN ASN B . n +B 1 107 TYR 107 106 106 TYR TYR B . n +B 1 108 LYS 108 107 107 LYS LYS B . n +B 1 109 THR 109 108 108 THR THR B . n +B 1 110 ARG 110 109 109 ARG ARG B . n +B 1 111 ALA 111 110 110 ALA ALA B . n +B 1 112 GLU 112 111 111 GLU GLU B . n +B 1 113 VAL 113 112 112 VAL VAL B . n +B 1 114 LYS 114 113 113 LYS LYS B . n +B 1 115 PHE 115 114 114 PHE PHE B . n +B 1 116 GLU 116 115 115 GLU GLU B . n +B 1 117 GLY 117 116 116 GLY GLY B . n +B 1 118 ASP 118 117 117 ASP ASP B . n +B 1 119 THR 119 118 118 THR THR B . n +B 1 120 LEU 120 119 119 LEU LEU B . n +B 1 121 VAL 121 120 120 VAL VAL B . n +B 1 122 ASN 122 121 121 ASN ASN B . n +B 1 123 ARG 123 122 122 ARG ARG B . n +B 1 124 ILE 124 123 123 ILE ILE B . n +B 1 125 GLU 125 124 124 GLU GLU B . n +B 1 126 LEU 126 125 125 LEU LEU B . n +B 1 127 LYS 127 126 126 LYS LYS B . n +B 1 128 GLY 128 127 127 GLY GLY B . n +B 1 129 ILE 129 128 128 ILE ILE B . n +B 1 130 ASP 130 129 129 ASP ASP B . n +B 1 131 PHE 131 130 130 PHE PHE B . n +B 1 132 LYS 132 131 131 LYS LYS B . n +B 1 133 GLU 133 132 132 GLU GLU B . n +B 1 134 ASP 134 133 133 ASP ASP B . n +B 1 135 GLY 135 134 134 GLY GLY B . n +B 1 136 ASN 136 135 135 ASN ASN B . n +B 1 137 ILE 137 136 136 ILE ILE B . n +B 1 138 LEU 138 137 137 LEU LEU B . n +B 1 139 GLY 139 138 138 GLY GLY B . n +B 1 140 HIS 140 139 139 HIS HIS B . n +B 1 141 LYS 141 140 140 LYS LYS B . n +B 1 142 LEU 142 141 141 LEU LEU B . n +B 1 143 GLU 143 142 142 GLU GLU B . n +B 1 144 TYR 144 143 143 TYR TYR B . n +B 1 145 ASN 145 144 144 ASN ASN B . n +B 1 146 TYR 146 145 145 TYR TYR B . n +B 1 147 ASN 147 146 146 ASN ASN B . n +B 1 148 SER 148 147 147 SER SER B . n +B 1 149 HIS 149 148 148 HIS HIS B . n +B 1 150 ASN 150 149 149 ASN ASN B . n +B 1 151 VAL 151 150 150 VAL VAL B . n +B 1 152 TYR 152 151 151 TYR TYR B . n +B 1 153 ILE 153 152 152 ILE ILE B . n +B 1 154 MET 154 153 153 MET MET B . n +B 1 155 ALA 155 154 154 ALA ALA B . n +B 1 156 ASP 156 155 155 ASP ASP B . n +B 1 157 LYS 157 156 156 LYS LYS B . n +B 1 158 GLN 158 157 157 GLN GLN B . n +B 1 159 LYS 159 158 158 LYS LYS B . n +B 1 160 ASN 160 159 159 ASN ASN B . n +B 1 161 GLY 161 160 160 GLY GLY B . n +B 1 162 ILE 162 161 161 ILE ILE B . n +B 1 163 LYS 163 162 162 LYS LYS B . n +B 1 164 VAL 164 163 163 VAL VAL B . n +B 1 165 ASN 165 164 164 ASN ASN B . n +B 1 166 PHE 166 165 165 PHE PHE B . n +B 1 167 LYS 167 166 166 LYS LYS B . n +B 1 168 ILE 168 167 167 ILE ILE B . n +B 1 169 ARG 169 168 168 ARG ARG B . n +B 1 170 HIS 170 169 169 HIS HIS B . n +B 1 171 ASN 171 170 170 ASN ASN B . n +B 1 172 ILE 172 171 171 ILE ILE B . n +B 1 173 GLU 173 172 172 GLU GLU B . n +B 1 174 ASP 174 173 173 ASP ASP B . n +B 1 175 GLY 175 174 174 GLY GLY B . n +B 1 176 SER 176 175 175 SER SER B . n +B 1 177 VAL 177 176 176 VAL VAL B . n +B 1 178 GLN 178 177 177 GLN GLN B . n +B 1 179 LEU 179 178 178 LEU LEU B . n +B 1 180 ALA 180 179 179 ALA ALA B . n +B 1 181 ASP 181 180 180 ASP ASP B . n +B 1 182 HIS 182 181 181 HIS HIS B . n +B 1 183 TYR 183 182 182 TYR TYR B . n +B 1 184 GLN 184 183 183 GLN GLN B . n +B 1 185 GLN 185 184 184 GLN GLN B . n +B 1 186 ASN 186 185 185 ASN ASN B . n +B 1 187 THR 187 186 186 THR THR B . n +B 1 188 PRO 188 187 187 PRO PRO B . n +B 1 189 ILE 189 188 188 ILE ILE B . n +B 1 190 GLY 190 189 189 GLY GLY B . n +B 1 191 ASP 191 190 190 ASP ASP B . n +B 1 192 GLY 192 191 191 GLY GLY B . n +B 1 193 PRO 193 192 192 PRO PRO B . n +B 1 194 VAL 194 193 193 VAL VAL B . n +B 1 195 LEU 195 194 194 LEU LEU B . n +B 1 196 LEU 196 195 195 LEU LEU B . n +B 1 197 PRO 197 196 196 PRO PRO B . n +B 1 198 ASP 198 197 197 ASP ASP B . n +B 1 199 ASN 199 198 198 ASN ASN B . n +B 1 200 HIS 200 199 199 HIS HIS B . n +B 1 201 TYR 201 200 200 TYR TYR B . n +B 1 202 LEU 202 201 201 LEU LEU B . n +B 1 203 SER 203 202 202 SER SER B . n +B 1 204 THR 204 203 203 THR THR B . n +B 1 205 GLN 205 204 204 GLN GLN B . n +B 1 206 SER 206 205 205 SER SER B . n +B 1 207 ASN 207 206 206 ASN ASN B . n +B 1 208 LEU 208 207 207 LEU LEU B . n +B 1 209 SER 209 208 208 SER SER B . n +B 1 210 LYS 210 209 209 LYS LYS B . n +B 1 211 ASP 211 210 210 ASP ASP B . n +B 1 212 PRO 212 211 211 PRO PRO B . n +B 1 213 ASN 213 212 212 ASN ASN B . n +B 1 214 GLU 214 213 213 GLU GLU B . n +B 1 215 LYS 215 214 214 LYS LYS B . n +B 1 216 ARG 216 215 215 ARG ARG B . n +B 1 217 ASP 217 216 216 ASP ASP B . n +B 1 218 HIS 218 217 217 HIS HIS B . n +B 1 219 MET 219 218 218 MET MET B . n +B 1 220 VAL 220 219 219 VAL VAL B . n +B 1 221 LEU 221 220 220 LEU LEU B . n +B 1 222 LEU 222 221 221 LEU LEU B . n +B 1 223 GLU 223 222 222 GLU GLU B . n +B 1 224 PHE 224 223 223 PHE PHE B . n +B 1 225 VAL 225 224 224 VAL VAL B . n +B 1 226 THR 226 225 225 THR THR B . n +B 1 227 ALA 227 226 226 ALA ALA B . n +B 1 228 ALA 228 227 227 ALA ALA B . n +B 1 229 GLY 229 228 228 GLY GLY B . n +B 1 230 ILE 230 229 229 ILE ILE B . n +B 1 231 THR 231 230 230 THR THR B . n +B 1 232 GLY 232 231 ? ? ? B . n +B 1 233 SER 233 232 ? ? ? B . n +B 1 234 ASP 234 1053 ? ? ? B . n +B 1 235 ALA 235 1054 1054 ALA ALA B . n +B 1 236 SER 236 1055 1055 SER SER B . n +B 1 237 THR 237 1056 1056 THR THR B . n +B 1 238 LYS 238 1057 1057 LYS LYS B . n +B 1 239 LYS 239 1058 1058 LYS LYS B . n +B 1 240 LEU 240 1059 1059 LEU LEU B . n +B 1 241 SER 241 1060 1060 SER SER B . n +B 1 242 GLU 242 1061 1061 GLU GLU B . n +B 1 243 SER 243 1062 1062 SER SER B . n +B 1 244 LEU 244 1063 1063 LEU LEU B . n +B 1 245 LYS 245 1064 1064 LYS LYS B . n +B 1 246 ARG 246 1065 1065 ARG ARG B . n +B 1 247 ILE 247 1066 1066 ILE ILE B . n +B 1 248 GLY 248 1067 1067 GLY GLY B . n +B 1 249 ASP 249 1068 1068 ASP ASP B . n +B 1 250 GLU 250 1069 1069 GLU GLU B . n +B 1 251 LEU 251 1070 1070 LEU LEU B . n +B 1 252 ASP 252 1071 1071 ASP ASP B . n +B 1 253 SER 253 1072 1072 SER SER B . n +B 1 254 ASN 254 1073 1073 ASN ASN B . n +B 1 255 MET 255 1074 1074 MET MET B . n +B 1 256 GLU 256 1075 1075 GLU GLU B . n +B 1 257 LEU 257 1076 1076 LEU LEU B . n +B 1 258 GLN 258 1077 1077 GLN GLN B . n +B 1 259 ARG 259 1078 1078 ARG ARG B . n +B 1 260 MET 260 1079 1079 MET MET B . n +B 1 261 ILE 261 1080 1080 ILE ILE B . n +B 1 262 ALA 262 1081 1081 ALA ALA B . n +B 1 263 ALA 263 1082 1082 ALA ALA B . n +B 1 264 VAL 264 1083 1083 VAL VAL B . n +B 1 265 ASP 265 1084 1084 ASP ASP B . n +B 1 266 THR 266 1085 1085 THR THR B . n +B 1 267 ASP 267 1086 1086 ASP ASP B . n +B 1 268 SER 268 1087 1087 SER SER B . n +B 1 269 PRO 269 1088 1088 PRO PRO B . n +B 1 270 ARG 270 1089 1089 ARG ARG B . n +B 1 271 GLU 271 1090 1090 GLU GLU B . n +B 1 272 VAL 272 1091 1091 VAL VAL B . n +B 1 273 PHE 273 1092 1092 PHE PHE B . n +B 1 274 PHE 274 1093 1093 PHE PHE B . n +B 1 275 ARG 275 1094 1094 ARG ARG B . n +B 1 276 VAL 276 1095 1095 VAL VAL B . n +B 1 277 ALA 277 1096 1096 ALA ALA B . n +B 1 278 ALA 278 1097 1097 ALA ALA B . n +B 1 279 ASP 279 1098 1098 ASP ASP B . n +B 1 280 MET 280 1099 1099 MET MET B . n +B 1 281 PHE 281 1100 1100 PHE PHE B . n +B 1 282 SER 282 1101 1101 SER SER B . n +B 1 283 ASP 283 1102 1102 ASP ASP B . n +B 1 284 GLY 284 1103 1103 GLY GLY B . n +B 1 285 ASN 285 1104 1104 ASN ASN B . n +B 1 286 PHE 286 1105 1105 PHE PHE B . n +B 1 287 ASN 287 1106 1106 ASN ASN B . n +B 1 288 TRP 288 1107 1107 TRP TRP B . n +B 1 289 GLY 289 1108 1108 GLY GLY B . n +B 1 290 ARG 290 1109 1109 ARG ARG B . n +B 1 291 VAL 291 1110 1110 VAL VAL B . n +B 1 292 VAL 292 1111 1111 VAL VAL B . n +B 1 293 ALA 293 1112 1112 ALA ALA B . n +B 1 294 LEU 294 1113 1113 LEU LEU B . n +B 1 295 PHE 295 1114 1114 PHE PHE B . n +B 1 296 TYR 296 1115 1115 TYR TYR B . n +B 1 297 PHE 297 1116 1116 PHE PHE B . n +B 1 298 ALA 298 1117 1117 ALA ALA B . n +B 1 299 SER 299 1118 1118 SER SER B . n +B 1 300 LYS 300 1119 1119 LYS LYS B . n +B 1 301 LEU 301 1120 1120 LEU LEU B . n +B 1 302 VAL 302 1121 1121 VAL VAL B . n +B 1 303 LEU 303 1122 1122 LEU LEU B . n +B 1 304 LYS 304 1123 ? ? ? B . n +B 1 305 ALA 305 1124 ? ? ? B . n +B 1 306 LEU 306 1125 ? ? ? B . n +B 1 307 SER 307 1126 ? ? ? B . n +B 1 308 THR 308 1127 ? ? ? B . n +B 1 309 LYS 309 1128 ? ? ? B . n +C 1 1 GLY 1 -2 ? ? ? C . n +C 1 2 SER 2 -1 ? ? ? C . n +C 1 3 HIS 3 0 ? ? ? C . n +C 1 4 MET 4 1 ? ? ? C . n +C 1 5 SER 5 2 2 SER SER C . n +C 1 6 LYS 6 3 3 LYS LYS C . n +C 1 7 GLY 7 4 4 GLY GLY C . n +C 1 8 GLU 8 5 5 GLU GLU C . n +C 1 9 GLU 9 6 6 GLU GLU C . n +C 1 10 LEU 10 7 7 LEU LEU C . n +C 1 11 PHE 11 8 8 PHE PHE C . n +C 1 12 THR 12 9 9 THR THR C . n +C 1 13 GLY 13 10 10 GLY GLY C . n +C 1 14 VAL 14 11 11 VAL VAL C . n +C 1 15 VAL 15 12 12 VAL VAL C . n +C 1 16 PRO 16 13 13 PRO PRO C . n +C 1 17 ILE 17 14 14 ILE ILE C . n +C 1 18 LEU 18 15 15 LEU LEU C . n +C 1 19 VAL 19 16 16 VAL VAL C . n +C 1 20 GLU 20 17 17 GLU GLU C . n +C 1 21 LEU 21 18 18 LEU LEU C . n +C 1 22 ASP 22 19 19 ASP ASP C . n +C 1 23 GLY 23 20 20 GLY GLY C . n +C 1 24 ASP 24 21 21 ASP ASP C . n +C 1 25 VAL 25 22 22 VAL VAL C . n +C 1 26 ASN 26 23 23 ASN ASN C . n +C 1 27 GLY 27 24 24 GLY GLY C . n +C 1 28 HIS 28 25 25 HIS HIS C . n +C 1 29 LYS 29 26 26 LYS LYS C . n +C 1 30 PHE 30 27 27 PHE PHE C . n +C 1 31 SER 31 28 28 SER SER C . n +C 1 32 VAL 32 29 29 VAL VAL C . n +C 1 33 SER 33 30 30 SER SER C . n +C 1 34 GLY 34 31 31 GLY GLY C . n +C 1 35 GLU 35 32 32 GLU GLU C . n +C 1 36 GLY 36 33 33 GLY GLY C . n +C 1 37 GLU 37 34 34 GLU GLU C . n +C 1 38 GLY 38 35 35 GLY GLY C . n +C 1 39 ASP 39 36 36 ASP ASP C . n +C 1 40 ALA 40 37 37 ALA ALA C . n +C 1 41 THR 41 38 38 THR THR C . n +C 1 42 TYR 42 39 39 TYR TYR C . n +C 1 43 GLY 43 40 40 GLY GLY C . n +C 1 44 LYS 44 41 41 LYS LYS C . n +C 1 45 LEU 45 42 42 LEU LEU C . n +C 1 46 THR 46 43 43 THR THR C . n +C 1 47 LEU 47 44 44 LEU LEU C . n +C 1 48 LYS 48 45 45 LYS LYS C . n +C 1 49 PHE 49 46 46 PHE PHE C . n +C 1 50 ILE 50 47 47 ILE ILE C . n +C 1 51 CYS 51 48 48 CYS CYS C . n +C 1 52 THR 52 49 49 THR THR C . n +C 1 53 THR 53 50 50 THR THR C . n +C 1 54 GLY 54 51 51 GLY GLY C . n +C 1 55 LYS 55 52 52 LYS LYS C . n +C 1 56 LEU 56 53 53 LEU LEU C . n +C 1 57 PRO 57 54 54 PRO PRO C . n +C 1 58 VAL 58 55 55 VAL VAL C . n +C 1 59 PRO 59 56 56 PRO PRO C . n +C 1 60 TRP 60 57 57 TRP TRP C . n +C 1 61 PRO 61 58 58 PRO PRO C . n +C 1 62 THR 62 59 59 THR THR C . n +C 1 63 LEU 63 60 60 LEU LEU C . n +C 1 64 VAL 64 61 61 VAL VAL C . n +C 1 65 THR 65 62 62 THR THR C . n +C 1 66 THR 66 63 63 THR THR C . n +C 1 67 PHE 67 64 64 PHE PHE C . n +C 1 68 CR2 68 65 65 CR2 CR2 C . n +C 1 69 VAL 69 68 68 VAL VAL C . n +C 1 70 GLN 70 69 69 GLN GLN C . n +C 1 71 CYS 71 70 70 CYS CYS C . n +C 1 72 PHE 72 71 71 PHE PHE C . n +C 1 73 SER 73 72 72 SER SER C . n +C 1 74 ARG 74 73 73 ARG ARG C . n +C 1 75 TYR 75 74 74 TYR TYR C . n +C 1 76 PRO 76 75 75 PRO PRO C . n +C 1 77 ASP 77 76 76 ASP ASP C . n +C 1 78 HIS 78 77 77 HIS HIS C . n +C 1 79 MET 79 78 78 MET MET C . n +C 1 80 LYS 80 79 79 LYS LYS C . n +C 1 81 GLN 81 80 80 GLN GLN C . n +C 1 82 HIS 82 81 81 HIS HIS C . n +C 1 83 ASP 83 82 82 ASP ASP C . n +C 1 84 PHE 84 83 83 PHE PHE C . n +C 1 85 PHE 85 84 84 PHE PHE C . n +C 1 86 LYS 86 85 85 LYS LYS C . n +C 1 87 SER 87 86 86 SER SER C . n +C 1 88 ALA 88 87 87 ALA ALA C . n +C 1 89 MET 89 88 88 MET MET C . n +C 1 90 PRO 90 89 89 PRO PRO C . n +C 1 91 GLU 91 90 90 GLU GLU C . n +C 1 92 GLY 92 91 91 GLY GLY C . n +C 1 93 TYR 93 92 92 TYR TYR C . n +C 1 94 VAL 94 93 93 VAL VAL C . n +C 1 95 GLN 95 94 94 GLN GLN C . n +C 1 96 GLU 96 95 95 GLU GLU C . n +C 1 97 ARG 97 96 96 ARG ARG C . n +C 1 98 THR 98 97 97 THR THR C . n +C 1 99 ILE 99 98 98 ILE ILE C . n +C 1 100 PHE 100 99 99 PHE PHE C . n +C 1 101 PHE 101 100 100 PHE PHE C . n +C 1 102 LYS 102 101 101 LYS LYS C . n +C 1 103 ASP 103 102 102 ASP ASP C . n +C 1 104 ASP 104 103 103 ASP ASP C . n +C 1 105 GLY 105 104 104 GLY GLY C . n +C 1 106 ASN 106 105 105 ASN ASN C . n +C 1 107 TYR 107 106 106 TYR TYR C . n +C 1 108 LYS 108 107 107 LYS LYS C . n +C 1 109 THR 109 108 108 THR THR C . n +C 1 110 ARG 110 109 109 ARG ARG C . n +C 1 111 ALA 111 110 110 ALA ALA C . n +C 1 112 GLU 112 111 111 GLU GLU C . n +C 1 113 VAL 113 112 112 VAL VAL C . n +C 1 114 LYS 114 113 113 LYS LYS C . n +C 1 115 PHE 115 114 114 PHE PHE C . n +C 1 116 GLU 116 115 115 GLU GLU C . n +C 1 117 GLY 117 116 116 GLY GLY C . n +C 1 118 ASP 118 117 117 ASP ASP C . n +C 1 119 THR 119 118 118 THR THR C . n +C 1 120 LEU 120 119 119 LEU LEU C . n +C 1 121 VAL 121 120 120 VAL VAL C . n +C 1 122 ASN 122 121 121 ASN ASN C . n +C 1 123 ARG 123 122 122 ARG ARG C . n +C 1 124 ILE 124 123 123 ILE ILE C . n +C 1 125 GLU 125 124 124 GLU GLU C . n +C 1 126 LEU 126 125 125 LEU LEU C . n +C 1 127 LYS 127 126 126 LYS LYS C . n +C 1 128 GLY 128 127 127 GLY GLY C . n +C 1 129 ILE 129 128 128 ILE ILE C . n +C 1 130 ASP 130 129 129 ASP ASP C . n +C 1 131 PHE 131 130 130 PHE PHE C . n +C 1 132 LYS 132 131 131 LYS LYS C . n +C 1 133 GLU 133 132 132 GLU GLU C . n +C 1 134 ASP 134 133 133 ASP ASP C . n +C 1 135 GLY 135 134 134 GLY GLY C . n +C 1 136 ASN 136 135 135 ASN ASN C . n +C 1 137 ILE 137 136 136 ILE ILE C . n +C 1 138 LEU 138 137 137 LEU LEU C . n +C 1 139 GLY 139 138 138 GLY GLY C . n +C 1 140 HIS 140 139 139 HIS HIS C . n +C 1 141 LYS 141 140 140 LYS LYS C . n +C 1 142 LEU 142 141 141 LEU LEU C . n +C 1 143 GLU 143 142 142 GLU GLU C . n +C 1 144 TYR 144 143 143 TYR TYR C . n +C 1 145 ASN 145 144 144 ASN ASN C . n +C 1 146 TYR 146 145 145 TYR TYR C . n +C 1 147 ASN 147 146 146 ASN ASN C . n +C 1 148 SER 148 147 147 SER SER C . n +C 1 149 HIS 149 148 148 HIS HIS C . n +C 1 150 ASN 150 149 149 ASN ASN C . n +C 1 151 VAL 151 150 150 VAL VAL C . n +C 1 152 TYR 152 151 151 TYR TYR C . n +C 1 153 ILE 153 152 152 ILE ILE C . n +C 1 154 MET 154 153 153 MET MET C . n +C 1 155 ALA 155 154 154 ALA ALA C . n +C 1 156 ASP 156 155 155 ASP ASP C . n +C 1 157 LYS 157 156 156 LYS LYS C . n +C 1 158 GLN 158 157 157 GLN GLN C . n +C 1 159 LYS 159 158 158 LYS LYS C . n +C 1 160 ASN 160 159 159 ASN ASN C . n +C 1 161 GLY 161 160 160 GLY GLY C . n +C 1 162 ILE 162 161 161 ILE ILE C . n +C 1 163 LYS 163 162 162 LYS LYS C . n +C 1 164 VAL 164 163 163 VAL VAL C . n +C 1 165 ASN 165 164 164 ASN ASN C . n +C 1 166 PHE 166 165 165 PHE PHE C . n +C 1 167 LYS 167 166 166 LYS LYS C . n +C 1 168 ILE 168 167 167 ILE ILE C . n +C 1 169 ARG 169 168 168 ARG ARG C . n +C 1 170 HIS 170 169 169 HIS HIS C . n +C 1 171 ASN 171 170 170 ASN ASN C . n +C 1 172 ILE 172 171 171 ILE ILE C . n +C 1 173 GLU 173 172 172 GLU GLU C . n +C 1 174 ASP 174 173 173 ASP ASP C . n +C 1 175 GLY 175 174 174 GLY GLY C . n +C 1 176 SER 176 175 175 SER SER C . n +C 1 177 VAL 177 176 176 VAL VAL C . n +C 1 178 GLN 178 177 177 GLN GLN C . n +C 1 179 LEU 179 178 178 LEU LEU C . n +C 1 180 ALA 180 179 179 ALA ALA C . n +C 1 181 ASP 181 180 180 ASP ASP C . n +C 1 182 HIS 182 181 181 HIS HIS C . n +C 1 183 TYR 183 182 182 TYR TYR C . n +C 1 184 GLN 184 183 183 GLN GLN C . n +C 1 185 GLN 185 184 184 GLN GLN C . n +C 1 186 ASN 186 185 185 ASN ASN C . n +C 1 187 THR 187 186 186 THR THR C . n +C 1 188 PRO 188 187 187 PRO PRO C . n +C 1 189 ILE 189 188 188 ILE ILE C . n +C 1 190 GLY 190 189 189 GLY GLY C . n +C 1 191 ASP 191 190 190 ASP ASP C . n +C 1 192 GLY 192 191 191 GLY GLY C . n +C 1 193 PRO 193 192 192 PRO PRO C . n +C 1 194 VAL 194 193 193 VAL VAL C . n +C 1 195 LEU 195 194 194 LEU LEU C . n +C 1 196 LEU 196 195 195 LEU LEU C . n +C 1 197 PRO 197 196 196 PRO PRO C . n +C 1 198 ASP 198 197 197 ASP ASP C . n +C 1 199 ASN 199 198 198 ASN ASN C . n +C 1 200 HIS 200 199 199 HIS HIS C . n +C 1 201 TYR 201 200 200 TYR TYR C . n +C 1 202 LEU 202 201 201 LEU LEU C . n +C 1 203 SER 203 202 202 SER SER C . n +C 1 204 THR 204 203 203 THR THR C . n +C 1 205 GLN 205 204 204 GLN GLN C . n +C 1 206 SER 206 205 205 SER SER C . n +C 1 207 ASN 207 206 206 ASN ASN C . n +C 1 208 LEU 208 207 207 LEU LEU C . n +C 1 209 SER 209 208 208 SER SER C . n +C 1 210 LYS 210 209 209 LYS LYS C . n +C 1 211 ASP 211 210 210 ASP ASP C . n +C 1 212 PRO 212 211 211 PRO PRO C . n +C 1 213 ASN 213 212 212 ASN ASN C . n +C 1 214 GLU 214 213 213 GLU GLU C . n +C 1 215 LYS 215 214 214 LYS LYS C . n +C 1 216 ARG 216 215 215 ARG ARG C . n +C 1 217 ASP 217 216 216 ASP ASP C . n +C 1 218 HIS 218 217 217 HIS HIS C . n +C 1 219 MET 219 218 218 MET MET C . n +C 1 220 VAL 220 219 219 VAL VAL C . n +C 1 221 LEU 221 220 220 LEU LEU C . n +C 1 222 LEU 222 221 221 LEU LEU C . n +C 1 223 GLU 223 222 222 GLU GLU C . n +C 1 224 PHE 224 223 223 PHE PHE C . n +C 1 225 VAL 225 224 224 VAL VAL C . n +C 1 226 THR 226 225 225 THR THR C . n +C 1 227 ALA 227 226 226 ALA ALA C . n +C 1 228 ALA 228 227 227 ALA ALA C . n +C 1 229 GLY 229 228 228 GLY GLY C . n +C 1 230 ILE 230 229 229 ILE ILE C . n +C 1 231 THR 231 230 230 THR THR C . n +C 1 232 GLY 232 231 ? ? ? C . n +C 1 233 SER 233 232 ? ? ? C . n +C 1 234 ASP 234 1053 ? ? ? C . n +C 1 235 ALA 235 1054 1054 ALA ALA C . n +C 1 236 SER 236 1055 1055 SER SER C . n +C 1 237 THR 237 1056 1056 THR THR C . n +C 1 238 LYS 238 1057 1057 LYS LYS C . n +C 1 239 LYS 239 1058 1058 LYS LYS C . n +C 1 240 LEU 240 1059 1059 LEU LEU C . n +C 1 241 SER 241 1060 1060 SER SER C . n +C 1 242 GLU 242 1061 1061 GLU GLU C . n +C 1 243 SER 243 1062 1062 SER SER C . n +C 1 244 LEU 244 1063 1063 LEU LEU C . n +C 1 245 LYS 245 1064 1064 LYS LYS C . n +C 1 246 ARG 246 1065 1065 ARG ARG C . n +C 1 247 ILE 247 1066 1066 ILE ILE C . n +C 1 248 GLY 248 1067 1067 GLY GLY C . n +C 1 249 ASP 249 1068 1068 ASP ASP C . n +C 1 250 GLU 250 1069 1069 GLU GLU C . n +C 1 251 LEU 251 1070 1070 LEU LEU C . n +C 1 252 ASP 252 1071 1071 ASP ASP C . n +C 1 253 SER 253 1072 1072 SER SER C . n +C 1 254 ASN 254 1073 1073 ASN ASN C . n +C 1 255 MET 255 1074 1074 MET MET C . n +C 1 256 GLU 256 1075 1075 GLU GLU C . n +C 1 257 LEU 257 1076 1076 LEU LEU C . n +C 1 258 GLN 258 1077 1077 GLN GLN C . n +C 1 259 ARG 259 1078 1078 ARG ARG C . n +C 1 260 MET 260 1079 1079 MET MET C . n +C 1 261 ILE 261 1080 1080 ILE ILE C . n +C 1 262 ALA 262 1081 1081 ALA ALA C . n +C 1 263 ALA 263 1082 1082 ALA ALA C . n +C 1 264 VAL 264 1083 1083 VAL VAL C . n +C 1 265 ASP 265 1084 1084 ASP ASP C . n +C 1 266 THR 266 1085 1085 THR THR C . n +C 1 267 ASP 267 1086 1086 ASP ASP C . n +C 1 268 SER 268 1087 1087 SER SER C . n +C 1 269 PRO 269 1088 1088 PRO PRO C . n +C 1 270 ARG 270 1089 1089 ARG ARG C . n +C 1 271 GLU 271 1090 1090 GLU GLU C . n +C 1 272 VAL 272 1091 1091 VAL VAL C . n +C 1 273 PHE 273 1092 1092 PHE PHE C . n +C 1 274 PHE 274 1093 1093 PHE PHE C . n +C 1 275 ARG 275 1094 1094 ARG ARG C . n +C 1 276 VAL 276 1095 1095 VAL VAL C . n +C 1 277 ALA 277 1096 1096 ALA ALA C . n +C 1 278 ALA 278 1097 1097 ALA ALA C . n +C 1 279 ASP 279 1098 1098 ASP ASP C . n +C 1 280 MET 280 1099 1099 MET MET C . n +C 1 281 PHE 281 1100 1100 PHE PHE C . n +C 1 282 SER 282 1101 1101 SER SER C . n +C 1 283 ASP 283 1102 1102 ASP ASP C . n +C 1 284 GLY 284 1103 1103 GLY GLY C . n +C 1 285 ASN 285 1104 1104 ASN ASN C . n +C 1 286 PHE 286 1105 1105 PHE PHE C . n +C 1 287 ASN 287 1106 1106 ASN ASN C . n +C 1 288 TRP 288 1107 1107 TRP TRP C . n +C 1 289 GLY 289 1108 1108 GLY GLY C . n +C 1 290 ARG 290 1109 1109 ARG ARG C . n +C 1 291 VAL 291 1110 1110 VAL VAL C . n +C 1 292 VAL 292 1111 1111 VAL VAL C . n +C 1 293 ALA 293 1112 1112 ALA ALA C . n +C 1 294 LEU 294 1113 1113 LEU LEU C . n +C 1 295 PHE 295 1114 1114 PHE PHE C . n +C 1 296 TYR 296 1115 1115 TYR TYR C . n +C 1 297 PHE 297 1116 1116 PHE PHE C . n +C 1 298 ALA 298 1117 1117 ALA ALA C . n +C 1 299 SER 299 1118 1118 SER SER C . n +C 1 300 LYS 300 1119 1119 LYS LYS C . n +C 1 301 LEU 301 1120 1120 LEU LEU C . n +C 1 302 VAL 302 1121 1121 VAL VAL C . n +C 1 303 LEU 303 1122 1122 LEU LEU C . n +C 1 304 LYS 304 1123 ? ? ? C . n +C 1 305 ALA 305 1124 ? ? ? C . n +C 1 306 LEU 306 1125 ? ? ? C . n +C 1 307 SER 307 1126 ? ? ? C . n +C 1 308 THR 308 1127 ? ? ? C . n +C 1 309 LYS 309 1128 ? ? ? C . n +D 1 1 GLY 1 -2 ? ? ? D . n +D 1 2 SER 2 -1 ? ? ? D . n +D 1 3 HIS 3 0 ? ? ? D . n +D 1 4 MET 4 1 ? ? ? D . n +D 1 5 SER 5 2 2 SER SER D . n +D 1 6 LYS 6 3 3 LYS LYS D . n +D 1 7 GLY 7 4 4 GLY GLY D . n +D 1 8 GLU 8 5 5 GLU GLU D . n +D 1 9 GLU 9 6 6 GLU GLU D . n +D 1 10 LEU 10 7 7 LEU LEU D . n +D 1 11 PHE 11 8 8 PHE PHE D . n +D 1 12 THR 12 9 9 THR THR D . n +D 1 13 GLY 13 10 10 GLY GLY D . n +D 1 14 VAL 14 11 11 VAL VAL D . n +D 1 15 VAL 15 12 12 VAL VAL D . n +D 1 16 PRO 16 13 13 PRO PRO D . n +D 1 17 ILE 17 14 14 ILE ILE D . n +D 1 18 LEU 18 15 15 LEU LEU D . n +D 1 19 VAL 19 16 16 VAL VAL D . n +D 1 20 GLU 20 17 17 GLU GLU D . n +D 1 21 LEU 21 18 18 LEU LEU D . n +D 1 22 ASP 22 19 19 ASP ASP D . n +D 1 23 GLY 23 20 20 GLY GLY D . n +D 1 24 ASP 24 21 21 ASP ASP D . n +D 1 25 VAL 25 22 22 VAL VAL D . n +D 1 26 ASN 26 23 23 ASN ASN D . n +D 1 27 GLY 27 24 24 GLY GLY D . n +D 1 28 HIS 28 25 25 HIS HIS D . n +D 1 29 LYS 29 26 26 LYS LYS D . n +D 1 30 PHE 30 27 27 PHE PHE D . n +D 1 31 SER 31 28 28 SER SER D . n +D 1 32 VAL 32 29 29 VAL VAL D . n +D 1 33 SER 33 30 30 SER SER D . n +D 1 34 GLY 34 31 31 GLY GLY D . n +D 1 35 GLU 35 32 32 GLU GLU D . n +D 1 36 GLY 36 33 33 GLY GLY D . n +D 1 37 GLU 37 34 34 GLU GLU D . n +D 1 38 GLY 38 35 35 GLY GLY D . n +D 1 39 ASP 39 36 36 ASP ASP D . n +D 1 40 ALA 40 37 37 ALA ALA D . n +D 1 41 THR 41 38 38 THR THR D . n +D 1 42 TYR 42 39 39 TYR TYR D . n +D 1 43 GLY 43 40 40 GLY GLY D . n +D 1 44 LYS 44 41 41 LYS LYS D . n +D 1 45 LEU 45 42 42 LEU LEU D . n +D 1 46 THR 46 43 43 THR THR D . n +D 1 47 LEU 47 44 44 LEU LEU D . n +D 1 48 LYS 48 45 45 LYS LYS D . n +D 1 49 PHE 49 46 46 PHE PHE D . n +D 1 50 ILE 50 47 47 ILE ILE D . n +D 1 51 CYS 51 48 48 CYS CYS D . n +D 1 52 THR 52 49 49 THR THR D . n +D 1 53 THR 53 50 50 THR THR D . n +D 1 54 GLY 54 51 51 GLY GLY D . n +D 1 55 LYS 55 52 52 LYS LYS D . n +D 1 56 LEU 56 53 53 LEU LEU D . n +D 1 57 PRO 57 54 54 PRO PRO D . n +D 1 58 VAL 58 55 55 VAL VAL D . n +D 1 59 PRO 59 56 56 PRO PRO D . n +D 1 60 TRP 60 57 57 TRP TRP D . n +D 1 61 PRO 61 58 58 PRO PRO D . n +D 1 62 THR 62 59 59 THR THR D . n +D 1 63 LEU 63 60 60 LEU LEU D . n +D 1 64 VAL 64 61 61 VAL VAL D . n +D 1 65 THR 65 62 62 THR THR D . n +D 1 66 THR 66 63 63 THR THR D . n +D 1 67 PHE 67 64 64 PHE PHE D . n +D 1 68 CR2 68 65 65 CR2 CR2 D . n +D 1 69 VAL 69 68 68 VAL VAL D . n +D 1 70 GLN 70 69 69 GLN GLN D . n +D 1 71 CYS 71 70 70 CYS CYS D . n +D 1 72 PHE 72 71 71 PHE PHE D . n +D 1 73 SER 73 72 72 SER SER D . n +D 1 74 ARG 74 73 73 ARG ARG D . n +D 1 75 TYR 75 74 74 TYR TYR D . n +D 1 76 PRO 76 75 75 PRO PRO D . n +D 1 77 ASP 77 76 76 ASP ASP D . n +D 1 78 HIS 78 77 77 HIS HIS D . n +D 1 79 MET 79 78 78 MET MET D . n +D 1 80 LYS 80 79 79 LYS LYS D . n +D 1 81 GLN 81 80 80 GLN GLN D . n +D 1 82 HIS 82 81 81 HIS HIS D . n +D 1 83 ASP 83 82 82 ASP ASP D . n +D 1 84 PHE 84 83 83 PHE PHE D . n +D 1 85 PHE 85 84 84 PHE PHE D . n +D 1 86 LYS 86 85 85 LYS LYS D . n +D 1 87 SER 87 86 86 SER SER D . n +D 1 88 ALA 88 87 87 ALA ALA D . n +D 1 89 MET 89 88 88 MET MET D . n +D 1 90 PRO 90 89 89 PRO PRO D . n +D 1 91 GLU 91 90 90 GLU GLU D . n +D 1 92 GLY 92 91 91 GLY GLY D . n +D 1 93 TYR 93 92 92 TYR TYR D . n +D 1 94 VAL 94 93 93 VAL VAL D . n +D 1 95 GLN 95 94 94 GLN GLN D . n +D 1 96 GLU 96 95 95 GLU GLU D . n +D 1 97 ARG 97 96 96 ARG ARG D . n +D 1 98 THR 98 97 97 THR THR D . n +D 1 99 ILE 99 98 98 ILE ILE D . n +D 1 100 PHE 100 99 99 PHE PHE D . n +D 1 101 PHE 101 100 100 PHE PHE D . n +D 1 102 LYS 102 101 101 LYS LYS D . n +D 1 103 ASP 103 102 102 ASP ASP D . n +D 1 104 ASP 104 103 103 ASP ASP D . n +D 1 105 GLY 105 104 104 GLY GLY D . n +D 1 106 ASN 106 105 105 ASN ASN D . n +D 1 107 TYR 107 106 106 TYR TYR D . n +D 1 108 LYS 108 107 107 LYS LYS D . n +D 1 109 THR 109 108 108 THR THR D . n +D 1 110 ARG 110 109 109 ARG ARG D . n +D 1 111 ALA 111 110 110 ALA ALA D . n +D 1 112 GLU 112 111 111 GLU GLU D . n +D 1 113 VAL 113 112 112 VAL VAL D . n +D 1 114 LYS 114 113 113 LYS LYS D . n +D 1 115 PHE 115 114 114 PHE PHE D . n +D 1 116 GLU 116 115 115 GLU GLU D . n +D 1 117 GLY 117 116 116 GLY GLY D . n +D 1 118 ASP 118 117 117 ASP ASP D . n +D 1 119 THR 119 118 118 THR THR D . n +D 1 120 LEU 120 119 119 LEU LEU D . n +D 1 121 VAL 121 120 120 VAL VAL D . n +D 1 122 ASN 122 121 121 ASN ASN D . n +D 1 123 ARG 123 122 122 ARG ARG D . n +D 1 124 ILE 124 123 123 ILE ILE D . n +D 1 125 GLU 125 124 124 GLU GLU D . n +D 1 126 LEU 126 125 125 LEU LEU D . n +D 1 127 LYS 127 126 126 LYS LYS D . n +D 1 128 GLY 128 127 127 GLY GLY D . n +D 1 129 ILE 129 128 128 ILE ILE D . n +D 1 130 ASP 130 129 129 ASP ASP D . n +D 1 131 PHE 131 130 130 PHE PHE D . n +D 1 132 LYS 132 131 131 LYS LYS D . n +D 1 133 GLU 133 132 132 GLU GLU D . n +D 1 134 ASP 134 133 133 ASP ASP D . n +D 1 135 GLY 135 134 134 GLY GLY D . n +D 1 136 ASN 136 135 135 ASN ASN D . n +D 1 137 ILE 137 136 136 ILE ILE D . n +D 1 138 LEU 138 137 137 LEU LEU D . n +D 1 139 GLY 139 138 138 GLY GLY D . n +D 1 140 HIS 140 139 139 HIS HIS D . n +D 1 141 LYS 141 140 140 LYS LYS D . n +D 1 142 LEU 142 141 141 LEU LEU D . n +D 1 143 GLU 143 142 142 GLU GLU D . n +D 1 144 TYR 144 143 143 TYR TYR D . n +D 1 145 ASN 145 144 144 ASN ASN D . n +D 1 146 TYR 146 145 145 TYR TYR D . n +D 1 147 ASN 147 146 146 ASN ASN D . n +D 1 148 SER 148 147 147 SER SER D . n +D 1 149 HIS 149 148 148 HIS HIS D . n +D 1 150 ASN 150 149 149 ASN ASN D . n +D 1 151 VAL 151 150 150 VAL VAL D . n +D 1 152 TYR 152 151 151 TYR TYR D . n +D 1 153 ILE 153 152 152 ILE ILE D . n +D 1 154 MET 154 153 153 MET MET D . n +D 1 155 ALA 155 154 154 ALA ALA D . n +D 1 156 ASP 156 155 155 ASP ASP D . n +D 1 157 LYS 157 156 156 LYS LYS D . n +D 1 158 GLN 158 157 157 GLN GLN D . n +D 1 159 LYS 159 158 158 LYS LYS D . n +D 1 160 ASN 160 159 159 ASN ASN D . n +D 1 161 GLY 161 160 160 GLY GLY D . n +D 1 162 ILE 162 161 161 ILE ILE D . n +D 1 163 LYS 163 162 162 LYS LYS D . n +D 1 164 VAL 164 163 163 VAL VAL D . n +D 1 165 ASN 165 164 164 ASN ASN D . n +D 1 166 PHE 166 165 165 PHE PHE D . n +D 1 167 LYS 167 166 166 LYS LYS D . n +D 1 168 ILE 168 167 167 ILE ILE D . n +D 1 169 ARG 169 168 168 ARG ARG D . n +D 1 170 HIS 170 169 169 HIS HIS D . n +D 1 171 ASN 171 170 170 ASN ASN D . n +D 1 172 ILE 172 171 171 ILE ILE D . n +D 1 173 GLU 173 172 172 GLU GLU D . n +D 1 174 ASP 174 173 173 ASP ASP D . n +D 1 175 GLY 175 174 174 GLY GLY D . n +D 1 176 SER 176 175 175 SER SER D . n +D 1 177 VAL 177 176 176 VAL VAL D . n +D 1 178 GLN 178 177 177 GLN GLN D . n +D 1 179 LEU 179 178 178 LEU LEU D . n +D 1 180 ALA 180 179 179 ALA ALA D . n +D 1 181 ASP 181 180 180 ASP ASP D . n +D 1 182 HIS 182 181 181 HIS HIS D . n +D 1 183 TYR 183 182 182 TYR TYR D . n +D 1 184 GLN 184 183 183 GLN GLN D . n +D 1 185 GLN 185 184 184 GLN GLN D . n +D 1 186 ASN 186 185 185 ASN ASN D . n +D 1 187 THR 187 186 186 THR THR D . n +D 1 188 PRO 188 187 187 PRO PRO D . n +D 1 189 ILE 189 188 188 ILE ILE D . n +D 1 190 GLY 190 189 189 GLY GLY D . n +D 1 191 ASP 191 190 190 ASP ASP D . n +D 1 192 GLY 192 191 191 GLY GLY D . n +D 1 193 PRO 193 192 192 PRO PRO D . n +D 1 194 VAL 194 193 193 VAL VAL D . n +D 1 195 LEU 195 194 194 LEU LEU D . n +D 1 196 LEU 196 195 195 LEU LEU D . n +D 1 197 PRO 197 196 196 PRO PRO D . n +D 1 198 ASP 198 197 197 ASP ASP D . n +D 1 199 ASN 199 198 198 ASN ASN D . n +D 1 200 HIS 200 199 199 HIS HIS D . n +D 1 201 TYR 201 200 200 TYR TYR D . n +D 1 202 LEU 202 201 201 LEU LEU D . n +D 1 203 SER 203 202 202 SER SER D . n +D 1 204 THR 204 203 203 THR THR D . n +D 1 205 GLN 205 204 204 GLN GLN D . n +D 1 206 SER 206 205 205 SER SER D . n +D 1 207 ASN 207 206 206 ASN ASN D . n +D 1 208 LEU 208 207 207 LEU LEU D . n +D 1 209 SER 209 208 208 SER SER D . n +D 1 210 LYS 210 209 209 LYS LYS D . n +D 1 211 ASP 211 210 210 ASP ASP D . n +D 1 212 PRO 212 211 211 PRO PRO D . n +D 1 213 ASN 213 212 212 ASN ASN D . n +D 1 214 GLU 214 213 213 GLU GLU D . n +D 1 215 LYS 215 214 214 LYS LYS D . n +D 1 216 ARG 216 215 215 ARG ARG D . n +D 1 217 ASP 217 216 216 ASP ASP D . n +D 1 218 HIS 218 217 217 HIS HIS D . n +D 1 219 MET 219 218 218 MET MET D . n +D 1 220 VAL 220 219 219 VAL VAL D . n +D 1 221 LEU 221 220 220 LEU LEU D . n +D 1 222 LEU 222 221 221 LEU LEU D . n +D 1 223 GLU 223 222 222 GLU GLU D . n +D 1 224 PHE 224 223 223 PHE PHE D . n +D 1 225 VAL 225 224 224 VAL VAL D . n +D 1 226 THR 226 225 225 THR THR D . n +D 1 227 ALA 227 226 226 ALA ALA D . n +D 1 228 ALA 228 227 227 ALA ALA D . n +D 1 229 GLY 229 228 228 GLY GLY D . n +D 1 230 ILE 230 229 229 ILE ILE D . n +D 1 231 THR 231 230 230 THR THR D . n +D 1 232 GLY 232 231 ? ? ? D . n +D 1 233 SER 233 232 ? ? ? D . n +D 1 234 ASP 234 1053 ? ? ? D . n +D 1 235 ALA 235 1054 1054 ALA ALA D . n +D 1 236 SER 236 1055 1055 SER SER D . n +D 1 237 THR 237 1056 1056 THR THR D . n +D 1 238 LYS 238 1057 1057 LYS LYS D . n +D 1 239 LYS 239 1058 1058 LYS LYS D . n +D 1 240 LEU 240 1059 1059 LEU LEU D . n +D 1 241 SER 241 1060 1060 SER SER D . n +D 1 242 GLU 242 1061 1061 GLU GLU D . n +D 1 243 SER 243 1062 1062 SER SER D . n +D 1 244 LEU 244 1063 1063 LEU LEU D . n +D 1 245 LYS 245 1064 1064 LYS LYS D . n +D 1 246 ARG 246 1065 1065 ARG ARG D . n +D 1 247 ILE 247 1066 1066 ILE ILE D . n +D 1 248 GLY 248 1067 1067 GLY GLY D . n +D 1 249 ASP 249 1068 1068 ASP ASP D . n +D 1 250 GLU 250 1069 1069 GLU GLU D . n +D 1 251 LEU 251 1070 1070 LEU LEU D . n +D 1 252 ASP 252 1071 1071 ASP ASP D . n +D 1 253 SER 253 1072 1072 SER SER D . n +D 1 254 ASN 254 1073 1073 ASN ASN D . n +D 1 255 MET 255 1074 1074 MET MET D . n +D 1 256 GLU 256 1075 1075 GLU GLU D . n +D 1 257 LEU 257 1076 1076 LEU LEU D . n +D 1 258 GLN 258 1077 1077 GLN GLN D . n +D 1 259 ARG 259 1078 1078 ARG ARG D . n +D 1 260 MET 260 1079 1079 MET MET D . n +D 1 261 ILE 261 1080 1080 ILE ILE D . n +D 1 262 ALA 262 1081 1081 ALA ALA D . n +D 1 263 ALA 263 1082 1082 ALA ALA D . n +D 1 264 VAL 264 1083 1083 VAL VAL D . n +D 1 265 ASP 265 1084 1084 ASP ASP D . n +D 1 266 THR 266 1085 1085 THR THR D . n +D 1 267 ASP 267 1086 1086 ASP ASP D . n +D 1 268 SER 268 1087 1087 SER SER D . n +D 1 269 PRO 269 1088 1088 PRO PRO D . n +D 1 270 ARG 270 1089 1089 ARG ARG D . n +D 1 271 GLU 271 1090 1090 GLU GLU D . n +D 1 272 VAL 272 1091 1091 VAL VAL D . n +D 1 273 PHE 273 1092 1092 PHE PHE D . n +D 1 274 PHE 274 1093 1093 PHE PHE D . n +D 1 275 ARG 275 1094 1094 ARG ARG D . n +D 1 276 VAL 276 1095 1095 VAL VAL D . n +D 1 277 ALA 277 1096 1096 ALA ALA D . n +D 1 278 ALA 278 1097 1097 ALA ALA D . n +D 1 279 ASP 279 1098 1098 ASP ASP D . n +D 1 280 MET 280 1099 1099 MET MET D . n +D 1 281 PHE 281 1100 1100 PHE PHE D . n +D 1 282 SER 282 1101 1101 SER SER D . n +D 1 283 ASP 283 1102 1102 ASP ASP D . n +D 1 284 GLY 284 1103 1103 GLY GLY D . n +D 1 285 ASN 285 1104 1104 ASN ASN D . n +D 1 286 PHE 286 1105 1105 PHE PHE D . n +D 1 287 ASN 287 1106 1106 ASN ASN D . n +D 1 288 TRP 288 1107 1107 TRP TRP D . n +D 1 289 GLY 289 1108 1108 GLY GLY D . n +D 1 290 ARG 290 1109 1109 ARG ARG D . n +D 1 291 VAL 291 1110 1110 VAL VAL D . n +D 1 292 VAL 292 1111 1111 VAL VAL D . n +D 1 293 ALA 293 1112 1112 ALA ALA D . n +D 1 294 LEU 294 1113 1113 LEU LEU D . n +D 1 295 PHE 295 1114 1114 PHE PHE D . n +D 1 296 TYR 296 1115 1115 TYR TYR D . n +D 1 297 PHE 297 1116 1116 PHE PHE D . n +D 1 298 ALA 298 1117 1117 ALA ALA D . n +D 1 299 SER 299 1118 1118 SER SER D . n +D 1 300 LYS 300 1119 1119 LYS LYS D . n +D 1 301 LEU 301 1120 1120 LEU LEU D . n +D 1 302 VAL 302 1121 1121 VAL VAL D . n +D 1 303 LEU 303 1122 1122 LEU LEU D . n +D 1 304 LYS 304 1123 ? ? ? D . n +D 1 305 ALA 305 1124 ? ? ? D . n +D 1 306 LEU 306 1125 ? ? ? D . n +D 1 307 SER 307 1126 ? ? ? D . n +D 1 308 THR 308 1127 ? ? ? D . n +D 1 309 LYS 309 1128 ? ? ? D . n +# +loop_ +_pdbx_nonpoly_scheme.asym_id +_pdbx_nonpoly_scheme.entity_id +_pdbx_nonpoly_scheme.mon_id +_pdbx_nonpoly_scheme.ndb_seq_num +_pdbx_nonpoly_scheme.pdb_seq_num +_pdbx_nonpoly_scheme.auth_seq_num +_pdbx_nonpoly_scheme.pdb_mon_id +_pdbx_nonpoly_scheme.auth_mon_id +_pdbx_nonpoly_scheme.pdb_strand_id +_pdbx_nonpoly_scheme.pdb_ins_code +E 2 HOH 1 2001 2001 HOH HOH A . +E 2 HOH 2 2002 2002 HOH HOH A . +E 2 HOH 3 2003 2003 HOH HOH A . +E 2 HOH 4 2004 2004 HOH HOH A . +E 2 HOH 5 2005 2005 HOH HOH A . +E 2 HOH 6 2006 2006 HOH HOH A . +E 2 HOH 7 2007 2007 HOH HOH A . +E 2 HOH 8 2008 2008 HOH HOH A . +E 2 HOH 9 2009 2009 HOH HOH A . +E 2 HOH 10 2010 2010 HOH HOH A . +E 2 HOH 11 2011 2011 HOH HOH A . +E 2 HOH 12 2012 2012 HOH HOH A . +E 2 HOH 13 2013 2013 HOH HOH A . +E 2 HOH 14 2014 2014 HOH HOH A . +E 2 HOH 15 2015 2015 HOH HOH A . +E 2 HOH 16 2016 2016 HOH HOH A . +E 2 HOH 17 2017 2017 HOH HOH A . +E 2 HOH 18 2018 2018 HOH HOH A . +F 2 HOH 1 4001 4001 HOH HOH A . +F 2 HOH 2 4002 4002 HOH HOH A . +G 2 HOH 1 2001 2001 HOH HOH B . +G 2 HOH 2 2002 2002 HOH HOH B . +G 2 HOH 3 2003 2003 HOH HOH B . +G 2 HOH 4 2004 2004 HOH HOH B . +G 2 HOH 5 2005 2005 HOH HOH B . +G 2 HOH 6 2006 2006 HOH HOH B . +G 2 HOH 7 2007 2007 HOH HOH B . +G 2 HOH 8 2008 2008 HOH HOH B . +G 2 HOH 9 2009 2009 HOH HOH B . +G 2 HOH 10 2010 2010 HOH HOH B . +G 2 HOH 11 2011 2011 HOH HOH B . +G 2 HOH 12 2012 2012 HOH HOH B . +G 2 HOH 13 2013 2013 HOH HOH B . +G 2 HOH 14 2014 2014 HOH HOH B . +G 2 HOH 15 2015 2015 HOH HOH B . +G 2 HOH 16 2016 2016 HOH HOH B . +G 2 HOH 17 2017 2017 HOH HOH B . +G 2 HOH 18 2018 2018 HOH HOH B . +H 2 HOH 1 4001 4001 HOH HOH B . +H 2 HOH 2 4002 4002 HOH HOH B . +H 2 HOH 3 4003 4003 HOH HOH B . +H 2 HOH 4 4004 4004 HOH HOH B . +I 2 HOH 1 2001 2001 HOH HOH C . +I 2 HOH 2 2002 2002 HOH HOH C . +I 2 HOH 3 2003 2003 HOH HOH C . +I 2 HOH 4 2004 2004 HOH HOH C . +I 2 HOH 5 2005 2005 HOH HOH C . +I 2 HOH 6 2006 2006 HOH HOH C . +I 2 HOH 7 2007 2007 HOH HOH C . +I 2 HOH 8 2008 2008 HOH HOH C . +I 2 HOH 9 2009 2009 HOH HOH C . +I 2 HOH 10 2010 2010 HOH HOH C . +I 2 HOH 11 2011 2011 HOH HOH C . +I 2 HOH 12 2012 2012 HOH HOH C . +I 2 HOH 13 2013 2013 HOH HOH C . +I 2 HOH 14 2014 2014 HOH HOH C . +I 2 HOH 15 2015 2015 HOH HOH C . +I 2 HOH 16 2016 2016 HOH HOH C . +I 2 HOH 17 2017 2017 HOH HOH C . +I 2 HOH 18 2018 2018 HOH HOH C . +I 2 HOH 19 2019 2019 HOH HOH C . +J 2 HOH 1 4001 4001 HOH HOH C . +J 2 HOH 2 4002 4002 HOH HOH C . +J 2 HOH 3 4003 4003 HOH HOH C . +J 2 HOH 4 4004 4004 HOH HOH C . +K 2 HOH 1 2001 2001 HOH HOH D . +K 2 HOH 2 2002 2002 HOH HOH D . +K 2 HOH 3 2003 2003 HOH HOH D . +K 2 HOH 4 2004 2004 HOH HOH D . +K 2 HOH 5 2005 2005 HOH HOH D . +K 2 HOH 6 2006 2006 HOH HOH D . +K 2 HOH 7 2007 2007 HOH HOH D . +K 2 HOH 8 2008 2008 HOH HOH D . +K 2 HOH 9 2009 2009 HOH HOH D . +K 2 HOH 10 2010 2010 HOH HOH D . +K 2 HOH 11 2011 2011 HOH HOH D . +K 2 HOH 12 2012 2012 HOH HOH D . +K 2 HOH 13 2013 2013 HOH HOH D . +K 2 HOH 14 2014 2014 HOH HOH D . +K 2 HOH 15 2015 2015 HOH HOH D . +K 2 HOH 16 2016 2016 HOH HOH D . +K 2 HOH 17 2017 2017 HOH HOH D . +K 2 HOH 18 2018 2018 HOH HOH D . +L 2 HOH 1 4001 4001 HOH HOH D . +# +loop_ +_pdbx_unobs_or_zero_occ_atoms.id +_pdbx_unobs_or_zero_occ_atoms.PDB_model_num +_pdbx_unobs_or_zero_occ_atoms.polymer_flag +_pdbx_unobs_or_zero_occ_atoms.occupancy_flag +_pdbx_unobs_or_zero_occ_atoms.auth_asym_id +_pdbx_unobs_or_zero_occ_atoms.auth_comp_id +_pdbx_unobs_or_zero_occ_atoms.auth_seq_id +_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code +_pdbx_unobs_or_zero_occ_atoms.auth_atom_id +_pdbx_unobs_or_zero_occ_atoms.label_alt_id +_pdbx_unobs_or_zero_occ_atoms.label_asym_id +_pdbx_unobs_or_zero_occ_atoms.label_comp_id +_pdbx_unobs_or_zero_occ_atoms.label_seq_id +_pdbx_unobs_or_zero_occ_atoms.label_atom_id +1 1 Y 1 A SER 72 ? OG ? A SER 73 OG +2 1 Y 1 B SER 72 ? OG ? B SER 73 OG +3 1 Y 1 C SER 72 ? OG ? C SER 73 OG +4 1 Y 1 D SER 72 ? OG ? D SER 73 OG +# +loop_ +_software.name +_software.classification +_software.version +_software.citation_id +_software.pdbx_ordinal +PHENIX refinement '(PHENIX.REFINE)' ? 1 +XDS 'data reduction' . ? 2 +XDS 'data scaling' . ? 3 +PHASER phasing . ? 4 +# +_cell.entry_id 4BDU +_cell.length_a 112.314 +_cell.length_b 112.314 +_cell.length_c 293.270 +_cell.angle_alpha 90.00 +_cell.angle_beta 90.00 +_cell.angle_gamma 120.00 +_cell.Z_PDB 24 +_cell.pdbx_unique_axis ? +# +_symmetry.entry_id 4BDU +_symmetry.space_group_name_H-M 'P 64' +_symmetry.pdbx_full_space_group_name_H-M ? +_symmetry.cell_setting ? +_symmetry.Int_Tables_number 172 +# +_exptl.entry_id 4BDU +_exptl.method 'X-RAY DIFFRACTION' +_exptl.crystals_number 1 +# +_exptl_crystal.id 1 +_exptl_crystal.density_meas ? +_exptl_crystal.density_Matthews 3.75 +_exptl_crystal.density_percent_sol 67.22 +_exptl_crystal.description NONE +# +_exptl_crystal_grow.crystal_id 1 +_exptl_crystal_grow.method ? +_exptl_crystal_grow.temp ? +_exptl_crystal_grow.temp_details ? +_exptl_crystal_grow.pH ? +_exptl_crystal_grow.pdbx_pH_range ? +_exptl_crystal_grow.pdbx_details '10% PEG3350, 20% MPD, 0.5% CHAPS, 0.1 M TRIS PH 8.0' +# +_diffrn.id 1 +_diffrn.ambient_temp 100 +_diffrn.ambient_temp_details ? +_diffrn.crystal_id 1 +# +_diffrn_detector.diffrn_id 1 +_diffrn_detector.detector CCD +_diffrn_detector.type 'ADSC QUANTUM 315r' +_diffrn_detector.pdbx_collection_date 2012-05-25 +_diffrn_detector.details ? +# +_diffrn_radiation.diffrn_id 1 +_diffrn_radiation.wavelength_id 1 +_diffrn_radiation.pdbx_monochromatic_or_laue_m_l M +_diffrn_radiation.monochromator 'SI(111)' +_diffrn_radiation.pdbx_diffrn_protocol 'SINGLE WAVELENGTH' +_diffrn_radiation.pdbx_scattering_type x-ray +# +_diffrn_radiation_wavelength.id 1 +_diffrn_radiation_wavelength.wavelength 0.9537 +_diffrn_radiation_wavelength.wt 1.0 +# +_diffrn_source.diffrn_id 1 +_diffrn_source.source SYNCHROTRON +_diffrn_source.type 'AUSTRALIAN SYNCHROTRON BEAMLINE MX2' +_diffrn_source.pdbx_synchrotron_site 'Australian Synchrotron' +_diffrn_source.pdbx_synchrotron_beamline MX2 +_diffrn_source.pdbx_wavelength 0.9537 +_diffrn_source.pdbx_wavelength_list ? +# +_reflns.pdbx_diffrn_id 1 +_reflns.pdbx_ordinal 1 +_reflns.entry_id 4BDU +_reflns.observed_criterion_sigma_I -3.0 +_reflns.observed_criterion_sigma_F ? +_reflns.d_resolution_low 19.90 +_reflns.d_resolution_high 3.00 +_reflns.number_obs 41413 +_reflns.number_all ? +_reflns.percent_possible_obs 99.5 +_reflns.pdbx_Rmerge_I_obs 0.1731 +_reflns.pdbx_Rsym_value ? +_reflns.pdbx_netI_over_sigmaI 17.74 +_reflns.B_iso_Wilson_estimate 82.07 +_reflns.pdbx_redundancy 20.7 +# +_reflns_shell.pdbx_diffrn_id 1 +_reflns_shell.pdbx_ordinal 1 +_reflns_shell.d_res_high 3.00 +_reflns_shell.d_res_low 3.10 +_reflns_shell.percent_possible_all 95.7 +_reflns_shell.Rmerge_I_obs 1.731 +_reflns_shell.pdbx_Rsym_value ? +_reflns_shell.meanI_over_sigI_obs 2.26 +_reflns_shell.pdbx_redundancy 17.5 +# +_refine.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine.entry_id 4BDU +_refine.pdbx_diffrn_id 1 +_refine.pdbx_TLS_residual_ADP_flag ? +_refine.ls_number_reflns_obs 41413 +_refine.ls_number_reflns_all ? +_refine.pdbx_ls_sigma_I ? +_refine.pdbx_ls_sigma_F 1.99 +_refine.pdbx_data_cutoff_high_absF ? +_refine.pdbx_data_cutoff_low_absF ? +_refine.pdbx_data_cutoff_high_rms_absF ? +_refine.ls_d_res_low 19.959 +_refine.ls_d_res_high 2.998 +_refine.ls_percent_reflns_obs 99.38 +_refine.ls_R_factor_obs 0.2165 +_refine.ls_R_factor_all ? +_refine.ls_R_factor_R_work 0.2149 +_refine.ls_R_factor_R_free 0.2460 +_refine.ls_R_factor_R_free_error ? +_refine.ls_R_factor_R_free_error_details ? +_refine.ls_percent_reflns_R_free 5.0 +_refine.ls_number_reflns_R_free 2071 +_refine.ls_number_parameters ? +_refine.ls_number_restraints ? +_refine.occupancy_min ? +_refine.occupancy_max ? +_refine.correlation_coeff_Fo_to_Fc ? +_refine.correlation_coeff_Fo_to_Fc_free ? +_refine.B_iso_mean 120.51 +_refine.aniso_B[1][1] 2.8299 +_refine.aniso_B[2][2] 2.8299 +_refine.aniso_B[3][3] -5.6597 +_refine.aniso_B[1][2] 0.0000 +_refine.aniso_B[1][3] 0.0000 +_refine.aniso_B[2][3] 0.0000 +_refine.solvent_model_details 'FLAT BULK SOLVENT MODEL' +_refine.solvent_model_param_ksol 0.263 +_refine.solvent_model_param_bsol 51.524 +_refine.pdbx_solvent_vdw_probe_radii 1.10 +_refine.pdbx_solvent_ion_probe_radii ? +_refine.pdbx_solvent_shrinkage_radii 0.86 +_refine.pdbx_ls_cross_valid_method ? +_refine.details +'CONSTRUCT USED FOR CRYSTALLISATION CONSISTED OF GFP FUSED TO BAX AS DESCRIBED IN SUZUKI ET AL. (2010) ACTA CRYS D 66, 1059.' +_refine.pdbx_starting_model ? +_refine.pdbx_method_to_determine_struct 'MOLECULAR REPLACEMENT' +_refine.pdbx_isotropic_thermal_model ? +_refine.pdbx_stereochemistry_target_values ML +_refine.pdbx_stereochem_target_val_spec_case ? +_refine.pdbx_R_Free_selection_details ? +_refine.pdbx_overall_ESU_R ? +_refine.pdbx_overall_ESU_R_Free ? +_refine.overall_SU_ML 0.32 +_refine.pdbx_overall_phase_error 31.34 +_refine.overall_SU_B ? +_refine.overall_SU_R_Cruickshank_DPI ? +_refine.pdbx_overall_SU_R_free_Cruickshank_DPI ? +_refine.pdbx_overall_SU_R_Blow_DPI ? +_refine.pdbx_overall_SU_R_free_Blow_DPI ? +# +_refine_hist.pdbx_refine_id 'X-RAY DIFFRACTION' +_refine_hist.cycle_id LAST +_refine_hist.pdbx_number_atoms_protein 9464 +_refine_hist.pdbx_number_atoms_nucleic_acid 0 +_refine_hist.pdbx_number_atoms_ligand 0 +_refine_hist.number_atoms_solvent 84 +_refine_hist.number_atoms_total 9548 +_refine_hist.d_res_high 2.998 +_refine_hist.d_res_low 19.959 +# +loop_ +_refine_ls_restr.type +_refine_ls_restr.dev_ideal +_refine_ls_restr.dev_ideal_target +_refine_ls_restr.weight +_refine_ls_restr.number +_refine_ls_restr.pdbx_refine_id +_refine_ls_restr.pdbx_restraint_function +f_bond_d 0.009 ? ? 9676 'X-RAY DIFFRACTION' ? +f_angle_d 1.390 ? ? 13072 'X-RAY DIFFRACTION' ? +f_dihedral_angle_d 15.087 ? ? 3544 'X-RAY DIFFRACTION' ? +f_chiral_restr 0.112 ? ? 1404 'X-RAY DIFFRACTION' ? +f_plane_restr 0.004 ? ? 1696 'X-RAY DIFFRACTION' ? +# +loop_ +_refine_ls_restr_ncs.dom_id +_refine_ls_restr_ncs.pdbx_auth_asym_id +_refine_ls_restr_ncs.pdbx_number +_refine_ls_restr_ncs.rms_dev_position +_refine_ls_restr_ncs.weight_position +_refine_ls_restr_ncs.pdbx_type +_refine_ls_restr_ncs.pdbx_ens_id +_refine_ls_restr_ncs.pdbx_ordinal +_refine_ls_restr_ncs.pdbx_refine_id +_refine_ls_restr_ncs.ncs_model_details +_refine_ls_restr_ncs.rms_dev_B_iso +_refine_ls_restr_ncs.weight_B_iso +_refine_ls_restr_ncs.pdbx_asym_id +_refine_ls_restr_ncs.pdbx_rms +_refine_ls_restr_ncs.pdbx_weight +1 A 1799 ? ? POSITIONAL 1 1 'X-RAY DIFFRACTION' ? ? ? ? ? ? +2 B 1799 0.223 ? POSITIONAL 1 2 'X-RAY DIFFRACTION' ? ? ? ? ? ? +3 C 1799 0.225 ? POSITIONAL 1 3 'X-RAY DIFFRACTION' ? ? ? ? ? ? +4 D 1799 0.111 ? POSITIONAL 1 4 'X-RAY DIFFRACTION' ? ? ? ? ? ? +1 A 548 ? ? POSITIONAL 2 5 'X-RAY DIFFRACTION' ? ? ? ? ? ? +2 B 548 0.021 ? POSITIONAL 2 6 'X-RAY DIFFRACTION' ? ? ? ? ? ? +3 C 548 0.022 ? POSITIONAL 2 7 'X-RAY DIFFRACTION' ? ? ? ? ? ? +4 D 548 0.007 ? POSITIONAL 2 8 'X-RAY DIFFRACTION' ? ? ? ? ? ? +# +loop_ +_refine_ls_shell.pdbx_refine_id +_refine_ls_shell.pdbx_total_number_of_bins_used +_refine_ls_shell.d_res_high +_refine_ls_shell.d_res_low +_refine_ls_shell.number_reflns_R_work +_refine_ls_shell.R_factor_R_work +_refine_ls_shell.percent_reflns_obs +_refine_ls_shell.R_factor_R_free +_refine_ls_shell.R_factor_R_free_error +_refine_ls_shell.percent_reflns_R_free +_refine_ls_shell.number_reflns_R_free +_refine_ls_shell.number_reflns_all +_refine_ls_shell.R_factor_all +'X-RAY DIFFRACTION' . 2.9984 3.0679 2478 0.3547 94.00 0.3656 . . 107 . . +'X-RAY DIFFRACTION' . 3.0679 3.1444 2568 0.3099 100.00 0.3242 . . 210 . . +'X-RAY DIFFRACTION' . 3.1444 3.2290 2657 0.2763 100.00 0.3685 . . 109 . . +'X-RAY DIFFRACTION' . 3.2290 3.3236 2646 0.2731 100.00 0.3306 . . 108 . . +'X-RAY DIFFRACTION' . 3.3236 3.4304 2675 0.2473 100.00 0.3225 . . 103 . . +'X-RAY DIFFRACTION' . 3.4304 3.5523 2569 0.2445 100.00 0.2854 . . 209 . . +'X-RAY DIFFRACTION' . 3.5523 3.6937 2668 0.2334 100.00 0.3642 . . 106 . . +'X-RAY DIFFRACTION' . 3.6937 3.8607 2688 0.2314 100.00 0.2652 . . 102 . . +'X-RAY DIFFRACTION' . 3.8607 4.0626 2552 0.2097 100.00 0.2690 . . 211 . . +'X-RAY DIFFRACTION' . 4.0626 4.3147 2667 0.1919 100.00 0.2098 . . 105 . . +'X-RAY DIFFRACTION' . 4.3147 4.6440 2675 0.1696 100.00 0.1842 . . 101 . . +'X-RAY DIFFRACTION' . 4.6440 5.1043 2587 0.1654 100.00 0.1956 . . 205 . . +'X-RAY DIFFRACTION' . 5.1043 5.8267 2661 0.1996 100.00 0.2796 . . 101 . . +'X-RAY DIFFRACTION' . 5.8267 7.2813 2681 0.2266 100.00 0.2310 . . 102 . . +'X-RAY DIFFRACTION' . 7.2813 19.9592 2570 0.1998 98.00 0.2039 . . 192 . . +# +loop_ +_struct_ncs_dom.id +_struct_ncs_dom.details +_struct_ncs_dom.pdbx_ens_id +1 ? 1 +2 ? 1 +3 ? 1 +4 ? 1 +1 ? 2 +2 ? 2 +3 ? 2 +4 ? 2 +# +loop_ +_struct_ncs_dom_lim.dom_id +_struct_ncs_dom_lim.beg_auth_asym_id +_struct_ncs_dom_lim.beg_auth_seq_id +_struct_ncs_dom_lim.end_auth_asym_id +_struct_ncs_dom_lim.end_auth_seq_id +_struct_ncs_dom_lim.pdbx_component_id +_struct_ncs_dom_lim.pdbx_refine_code +_struct_ncs_dom_lim.beg_label_asym_id +_struct_ncs_dom_lim.beg_label_comp_id +_struct_ncs_dom_lim.beg_label_seq_id +_struct_ncs_dom_lim.beg_label_alt_id +_struct_ncs_dom_lim.end_label_asym_id +_struct_ncs_dom_lim.end_label_comp_id +_struct_ncs_dom_lim.end_label_seq_id +_struct_ncs_dom_lim.end_label_alt_id +_struct_ncs_dom_lim.pdbx_ens_id +_struct_ncs_dom_lim.selection_details +_struct_ncs_dom_lim.beg_auth_comp_id +_struct_ncs_dom_lim.end_auth_comp_id +1 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN A AND (RESSEQ 2:64 OR RESSEQ 68:230)' ? ? +2 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN B AND (RESSEQ 2:64 OR RESSEQ 68:230)' ? ? +3 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN C AND (RESSEQ 2:64 OR RESSEQ 68:230)' ? ? +4 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 1 'CHAIN D AND (RESSEQ 2:64 OR RESSEQ 68:230)' ? ? +1 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'CHAIN A AND (RESSEQ 1054:1122)' ? ? +2 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'CHAIN B AND (RESSEQ 1054:1122)' ? ? +3 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'CHAIN C AND (RESSEQ 1054:1122)' ? ? +4 ? ? ? ? 1 ? ? ? ? ? ? ? ? ? 2 'CHAIN D AND (RESSEQ 1054:1122)' ? ? +# +loop_ +_struct_ncs_ens.id +_struct_ncs_ens.details +1 ? +2 ? +# +_database_PDB_matrix.entry_id 4BDU +_database_PDB_matrix.origx[1][1] 1.000000 +_database_PDB_matrix.origx[1][2] 0.000000 +_database_PDB_matrix.origx[1][3] 0.000000 +_database_PDB_matrix.origx[2][1] 0.000000 +_database_PDB_matrix.origx[2][2] 1.000000 +_database_PDB_matrix.origx[2][3] 0.000000 +_database_PDB_matrix.origx[3][1] 0.000000 +_database_PDB_matrix.origx[3][2] 0.000000 +_database_PDB_matrix.origx[3][3] 1.000000 +_database_PDB_matrix.origx_vector[1] 0.00000 +_database_PDB_matrix.origx_vector[2] 0.00000 +_database_PDB_matrix.origx_vector[3] 0.00000 +# +_struct.entry_id 4BDU +_struct.title 'Bax BH3-in-Groove dimer (GFP)' +_struct.pdbx_model_details ? +_struct.pdbx_CASP_flag ? +_struct.pdbx_model_type_details ? +# +_struct_keywords.entry_id 4BDU +_struct_keywords.pdbx_keywords APOPTOSIS +_struct_keywords.text 'APOPTOSIS, PROGRAMMED CELL DEATH, BCL-2 FAMILY, CHIMERA' +# +loop_ +_struct_asym.id +_struct_asym.pdbx_blank_PDB_chainid_flag +_struct_asym.pdbx_modified +_struct_asym.entity_id +_struct_asym.details +A N N 1 ? +B N N 1 ? +C N N 1 ? +D N N 1 ? +E N N 2 ? +F N N 2 ? +G N N 2 ? +H N N 2 ? +I N N 2 ? +J N N 2 ? +K N N 2 ? +L N N 2 ? +# +loop_ +_struct_ref.id +_struct_ref.db_name +_struct_ref.db_code +_struct_ref.entity_id +_struct_ref.pdbx_seq_one_letter_code +_struct_ref.pdbx_align_begin +_struct_ref.pdbx_db_accession +_struct_ref.pdbx_db_isoform +1 UNP GFP_AEQVI 1 ? ? P42212 ? +2 UNP BAX_HUMAN 1 ? ? Q07812 ? +# +loop_ +_struct_ref_seq.align_id +_struct_ref_seq.ref_id +_struct_ref_seq.pdbx_PDB_id_code +_struct_ref_seq.pdbx_strand_id +_struct_ref_seq.seq_align_beg +_struct_ref_seq.pdbx_seq_align_beg_ins_code +_struct_ref_seq.seq_align_end +_struct_ref_seq.pdbx_seq_align_end_ins_code +_struct_ref_seq.pdbx_db_accession +_struct_ref_seq.db_align_beg +_struct_ref_seq.pdbx_db_align_beg_ins_code +_struct_ref_seq.db_align_end +_struct_ref_seq.pdbx_db_align_end_ins_code +_struct_ref_seq.pdbx_auth_seq_align_beg +_struct_ref_seq.pdbx_auth_seq_align_end +1 1 4BDU A 4 ? 231 ? P42212 1 ? 230 ? 1 230 +2 2 4BDU A 234 ? 309 ? Q07812 53 ? 128 ? 1053 1128 +3 1 4BDU B 4 ? 231 ? P42212 1 ? 230 ? 1 230 +4 2 4BDU B 234 ? 309 ? Q07812 53 ? 128 ? 1053 1128 +5 1 4BDU C 4 ? 231 ? P42212 1 ? 230 ? 1 230 +6 2 4BDU C 234 ? 309 ? Q07812 53 ? 128 ? 1053 1128 +7 1 4BDU D 4 ? 231 ? P42212 1 ? 230 ? 1 230 +8 2 4BDU D 234 ? 309 ? Q07812 53 ? 128 ? 1053 1128 +# +loop_ +_struct_ref_seq_dif.align_id +_struct_ref_seq_dif.pdbx_pdb_id_code +_struct_ref_seq_dif.mon_id +_struct_ref_seq_dif.pdbx_pdb_strand_id +_struct_ref_seq_dif.seq_num +_struct_ref_seq_dif.pdbx_pdb_ins_code +_struct_ref_seq_dif.pdbx_seq_db_name +_struct_ref_seq_dif.pdbx_seq_db_accession_code +_struct_ref_seq_dif.db_mon_id +_struct_ref_seq_dif.pdbx_seq_db_seq_num +_struct_ref_seq_dif.details +_struct_ref_seq_dif.pdbx_auth_seq_num +_struct_ref_seq_dif.pdbx_ordinal +1 4BDU GLY A 1 ? UNP P42212 ? ? 'expression tag' -2 1 +1 4BDU SER A 2 ? UNP P42212 ? ? 'expression tag' -1 2 +1 4BDU HIS A 3 ? UNP P42212 ? ? 'expression tag' 0 3 +1 4BDU CR2 A 68 ? UNP P42212 SER 65 'engineered mutation' 65 4 +1 4BDU CR2 A 68 ? UNP P42212 SER 65 chromophore 65 5 +1 4BDU CR2 A 68 ? UNP P42212 TYR 66 chromophore 65 6 +1 4BDU CR2 A 68 ? UNP P42212 GLY 67 chromophore 65 7 +1 4BDU ASN A 207 ? UNP P42212 ALA 206 'engineered mutation' 206 8 +1 4BDU GLY A 232 ? UNP P42212 ? ? linker 231 9 +1 4BDU SER A 233 ? UNP P42212 ? ? linker 232 10 +1 4BDU SER A 307 ? UNP Q07812 CYS 1126 'engineered mutation' 1126 11 +3 4BDU GLY B 1 ? UNP P42212 ? ? 'expression tag' -2 12 +3 4BDU SER B 2 ? UNP P42212 ? ? 'expression tag' -1 13 +3 4BDU HIS B 3 ? UNP P42212 ? ? 'expression tag' 0 14 +3 4BDU CR2 B 68 ? UNP P42212 SER 65 'engineered mutation' 65 15 +3 4BDU CR2 B 68 ? UNP P42212 SER 65 chromophore 65 16 +3 4BDU CR2 B 68 ? UNP P42212 TYR 66 chromophore 65 17 +3 4BDU CR2 B 68 ? UNP P42212 GLY 67 chromophore 65 18 +3 4BDU ASN B 207 ? UNP P42212 ALA 206 'engineered mutation' 206 19 +3 4BDU GLY B 232 ? UNP P42212 ? ? linker 231 20 +3 4BDU SER B 233 ? UNP P42212 ? ? linker 232 21 +3 4BDU SER B 307 ? UNP Q07812 CYS 1126 'engineered mutation' 1126 22 +5 4BDU GLY C 1 ? UNP P42212 ? ? 'expression tag' -2 23 +5 4BDU SER C 2 ? UNP P42212 ? ? 'expression tag' -1 24 +5 4BDU HIS C 3 ? UNP P42212 ? ? 'expression tag' 0 25 +5 4BDU CR2 C 68 ? UNP P42212 SER 65 'engineered mutation' 65 26 +5 4BDU CR2 C 68 ? UNP P42212 SER 65 chromophore 65 27 +5 4BDU CR2 C 68 ? UNP P42212 TYR 66 chromophore 65 28 +5 4BDU CR2 C 68 ? UNP P42212 GLY 67 chromophore 65 29 +5 4BDU ASN C 207 ? UNP P42212 ALA 206 'engineered mutation' 206 30 +5 4BDU GLY C 232 ? UNP P42212 ? ? linker 231 31 +5 4BDU SER C 233 ? UNP P42212 ? ? linker 232 32 +5 4BDU SER C 307 ? UNP Q07812 CYS 1126 'engineered mutation' 1126 33 +7 4BDU GLY D 1 ? UNP P42212 ? ? 'expression tag' -2 34 +7 4BDU SER D 2 ? UNP P42212 ? ? 'expression tag' -1 35 +7 4BDU HIS D 3 ? UNP P42212 ? ? 'expression tag' 0 36 +7 4BDU CR2 D 68 ? UNP P42212 SER 65 'engineered mutation' 65 37 +7 4BDU CR2 D 68 ? UNP P42212 SER 65 chromophore 65 38 +7 4BDU CR2 D 68 ? UNP P42212 TYR 66 chromophore 65 39 +7 4BDU CR2 D 68 ? UNP P42212 GLY 67 chromophore 65 40 +7 4BDU ASN D 207 ? UNP P42212 ALA 206 'engineered mutation' 206 41 +7 4BDU GLY D 232 ? UNP P42212 ? ? linker 231 42 +7 4BDU SER D 233 ? UNP P42212 ? ? linker 232 43 +7 4BDU SER D 307 ? UNP Q07812 CYS 1126 'engineered mutation' 1126 44 +# +loop_ +_pdbx_struct_assembly.id +_pdbx_struct_assembly.details +_pdbx_struct_assembly.method_details +_pdbx_struct_assembly.oligomeric_details +_pdbx_struct_assembly.oligomeric_count +1 author_and_software_defined_assembly PISA tetrameric 4 +2 author_and_software_defined_assembly PISA tetrameric 4 +# +loop_ +_pdbx_struct_assembly_prop.biol_id +_pdbx_struct_assembly_prop.type +_pdbx_struct_assembly_prop.value +_pdbx_struct_assembly_prop.details +1 'ABSA (A^2)' 11450 ? +1 MORE -82.0 ? +1 'SSA (A^2)' 55010 ? +2 'ABSA (A^2)' 11450 ? +2 MORE -81.0 ? +2 'SSA (A^2)' 55010 ? +# +loop_ +_pdbx_struct_assembly_gen.assembly_id +_pdbx_struct_assembly_gen.oper_expression +_pdbx_struct_assembly_gen.asym_id_list +1 1,2 A,B,E,F,G,H +2 1,3 C,D,I,J,K,L +# +loop_ +_pdbx_struct_oper_list.id +_pdbx_struct_oper_list.type +_pdbx_struct_oper_list.name +_pdbx_struct_oper_list.symmetry_operation +_pdbx_struct_oper_list.matrix[1][1] +_pdbx_struct_oper_list.matrix[1][2] +_pdbx_struct_oper_list.matrix[1][3] +_pdbx_struct_oper_list.vector[1] +_pdbx_struct_oper_list.matrix[2][1] +_pdbx_struct_oper_list.matrix[2][2] +_pdbx_struct_oper_list.matrix[2][3] +_pdbx_struct_oper_list.vector[2] +_pdbx_struct_oper_list.matrix[3][1] +_pdbx_struct_oper_list.matrix[3][2] +_pdbx_struct_oper_list.matrix[3][3] +_pdbx_struct_oper_list.vector[3] +1 'identity operation' 1_555 x,y,z 1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 +0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000 0.0000000000 +2 'crystal symmetry operation' 4_675 -x+1,-y+2,z -1.0000000000 0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 +0.0000000000 194.5335544013 0.0000000000 0.0000000000 1.0000000000 0.0000000000 +3 'crystal symmetry operation' 4_665 -x+1,-y+1,z -1.0000000000 0.0000000000 0.0000000000 56.1570000000 0.0000000000 -1.0000000000 +0.0000000000 97.2667772006 0.0000000000 0.0000000000 1.0000000000 0.0000000000 +# +_struct_biol.id 1 +# +loop_ +_struct_conf.conf_type_id +_struct_conf.id +_struct_conf.pdbx_PDB_helix_id +_struct_conf.beg_label_comp_id +_struct_conf.beg_label_asym_id +_struct_conf.beg_label_seq_id +_struct_conf.pdbx_beg_PDB_ins_code +_struct_conf.end_label_comp_id +_struct_conf.end_label_asym_id +_struct_conf.end_label_seq_id +_struct_conf.pdbx_end_PDB_ins_code +_struct_conf.beg_auth_comp_id +_struct_conf.beg_auth_asym_id +_struct_conf.beg_auth_seq_id +_struct_conf.end_auth_comp_id +_struct_conf.end_auth_asym_id +_struct_conf.end_auth_seq_id +_struct_conf.pdbx_PDB_helix_class +_struct_conf.details +_struct_conf.pdbx_PDB_helix_length +HELX_P HELX_P1 1 LYS A 6 ? PHE A 11 ? LYS A 3 PHE A 8 5 ? 6 +HELX_P HELX_P2 2 ALA A 40 ? TYR A 42 ? ALA A 37 TYR A 39 5 ? 3 +HELX_P HELX_P3 3 PRO A 59 ? VAL A 64 ? PRO A 56 VAL A 61 5 ? 6 +HELX_P HELX_P4 4 VAL A 69 ? SER A 73 ? VAL A 68 SER A 72 5 ? 5 +HELX_P HELX_P5 5 ASP A 83 ? ALA A 88 ? ASP A 82 ALA A 87 1 ? 6 +HELX_P HELX_P6 6 SER A 236 ? ASN A 254 ? SER A 1055 ASN A 1073 1 ? 19 +HELX_P HELX_P7 7 ASN A 254 ? ALA A 263 ? ASN A 1073 ALA A 1082 1 ? 10 +HELX_P HELX_P8 8 SER A 268 ? PHE A 281 ? SER A 1087 PHE A 1100 1 ? 14 +HELX_P HELX_P9 9 ASN A 287 ? LEU A 301 ? ASN A 1106 LEU A 1120 1 ? 15 +HELX_P HELX_P10 10 LYS B 6 ? PHE B 11 ? LYS B 3 PHE B 8 5 ? 6 +HELX_P HELX_P11 11 ALA B 40 ? TYR B 42 ? ALA B 37 TYR B 39 5 ? 3 +HELX_P HELX_P12 12 PRO B 59 ? VAL B 64 ? PRO B 56 VAL B 61 5 ? 6 +HELX_P HELX_P13 13 VAL B 69 ? SER B 73 ? VAL B 68 SER B 72 5 ? 5 +HELX_P HELX_P14 14 ASP B 83 ? ALA B 88 ? ASP B 82 ALA B 87 1 ? 6 +HELX_P HELX_P15 15 SER B 236 ? ASN B 254 ? SER B 1055 ASN B 1073 1 ? 19 +HELX_P HELX_P16 16 ASN B 254 ? ALA B 263 ? ASN B 1073 ALA B 1082 1 ? 10 +HELX_P HELX_P17 17 SER B 268 ? PHE B 281 ? SER B 1087 PHE B 1100 1 ? 14 +HELX_P HELX_P18 18 ASN B 287 ? LEU B 301 ? ASN B 1106 LEU B 1120 1 ? 15 +HELX_P HELX_P19 19 LYS C 6 ? PHE C 11 ? LYS C 3 PHE C 8 5 ? 6 +HELX_P HELX_P20 20 ALA C 40 ? TYR C 42 ? ALA C 37 TYR C 39 5 ? 3 +HELX_P HELX_P21 21 PRO C 59 ? VAL C 64 ? PRO C 56 VAL C 61 5 ? 6 +HELX_P HELX_P22 22 ASP C 83 ? ALA C 88 ? ASP C 82 ALA C 87 1 ? 6 +HELX_P HELX_P23 23 SER C 236 ? ASN C 254 ? SER C 1055 ASN C 1073 1 ? 19 +HELX_P HELX_P24 24 ASN C 254 ? ALA C 263 ? ASN C 1073 ALA C 1082 1 ? 10 +HELX_P HELX_P25 25 SER C 268 ? PHE C 281 ? SER C 1087 PHE C 1100 1 ? 14 +HELX_P HELX_P26 26 ASN C 287 ? LEU C 301 ? ASN C 1106 LEU C 1120 1 ? 15 +HELX_P HELX_P27 27 LYS D 6 ? PHE D 11 ? LYS D 3 PHE D 8 5 ? 6 +HELX_P HELX_P28 28 ALA D 40 ? TYR D 42 ? ALA D 37 TYR D 39 5 ? 3 +HELX_P HELX_P29 29 PRO D 59 ? VAL D 64 ? PRO D 56 VAL D 61 5 ? 6 +HELX_P HELX_P30 30 VAL D 69 ? SER D 73 ? VAL D 68 SER D 72 5 ? 5 +HELX_P HELX_P31 31 ASP D 83 ? ALA D 88 ? ASP D 82 ALA D 87 1 ? 6 +HELX_P HELX_P32 32 SER D 236 ? ASN D 254 ? SER D 1055 ASN D 1073 1 ? 19 +HELX_P HELX_P33 33 ASN D 254 ? ALA D 263 ? ASN D 1073 ALA D 1082 1 ? 10 +HELX_P HELX_P34 34 SER D 268 ? PHE D 281 ? SER D 1087 PHE D 1100 1 ? 14 +HELX_P HELX_P35 35 ASN D 287 ? LEU D 301 ? ASN D 1106 LEU D 1120 1 ? 15 +# +_struct_conf_type.id HELX_P +_struct_conf_type.criteria ? +_struct_conf_type.reference ? +# +loop_ +_struct_conn.id +_struct_conn.conn_type_id +_struct_conn.pdbx_leaving_atom_flag +_struct_conn.pdbx_PDB_id +_struct_conn.ptnr1_label_asym_id +_struct_conn.ptnr1_label_comp_id +_struct_conn.ptnr1_label_seq_id +_struct_conn.ptnr1_label_atom_id +_struct_conn.pdbx_ptnr1_label_alt_id +_struct_conn.pdbx_ptnr1_PDB_ins_code +_struct_conn.pdbx_ptnr1_standard_comp_id +_struct_conn.ptnr1_symmetry +_struct_conn.ptnr2_label_asym_id +_struct_conn.ptnr2_label_comp_id +_struct_conn.ptnr2_label_seq_id +_struct_conn.ptnr2_label_atom_id +_struct_conn.pdbx_ptnr2_label_alt_id +_struct_conn.pdbx_ptnr2_PDB_ins_code +_struct_conn.ptnr1_auth_asym_id +_struct_conn.ptnr1_auth_comp_id +_struct_conn.ptnr1_auth_seq_id +_struct_conn.ptnr2_auth_asym_id +_struct_conn.ptnr2_auth_comp_id +_struct_conn.ptnr2_auth_seq_id +_struct_conn.ptnr2_symmetry +_struct_conn.pdbx_ptnr3_label_atom_id +_struct_conn.pdbx_ptnr3_label_seq_id +_struct_conn.pdbx_ptnr3_label_comp_id +_struct_conn.pdbx_ptnr3_label_asym_id +_struct_conn.pdbx_ptnr3_label_alt_id +_struct_conn.pdbx_ptnr3_PDB_ins_code +_struct_conn.details +_struct_conn.pdbx_dist_value +_struct_conn.pdbx_value_order +_struct_conn.pdbx_role +covale1 covale both ? A PHE 67 C ? ? ? 1_555 A CR2 68 N1 ? ? A PHE 64 A CR2 65 1_555 ? ? ? ? ? ? ? 1.326 ? ? +covale2 covale both ? A CR2 68 C3 ? ? ? 1_555 A VAL 69 N ? ? A CR2 65 A VAL 68 1_555 ? ? ? ? ? ? ? 1.333 ? ? +covale3 covale both ? B PHE 67 C ? ? ? 1_555 B CR2 68 N1 ? ? B PHE 64 B CR2 65 1_555 ? ? ? ? ? ? ? 1.332 ? ? +covale4 covale both ? B CR2 68 C3 ? ? ? 1_555 B VAL 69 N ? ? B CR2 65 B VAL 68 1_555 ? ? ? ? ? ? ? 1.332 ? ? +covale5 covale both ? C PHE 67 C ? ? ? 1_555 C CR2 68 N1 ? ? C PHE 64 C CR2 65 1_555 ? ? ? ? ? ? ? 1.329 ? ? +covale6 covale both ? C CR2 68 C3 ? ? ? 1_555 C VAL 69 N ? ? C CR2 65 C VAL 68 1_555 ? ? ? ? ? ? ? 1.333 ? ? +covale7 covale both ? D PHE 67 C ? ? ? 1_555 D CR2 68 N1 ? ? D PHE 64 D CR2 65 1_555 ? ? ? ? ? ? ? 1.314 ? ? +covale8 covale both ? D CR2 68 C3 ? ? ? 1_555 D VAL 69 N ? ? D CR2 65 D VAL 68 1_555 ? ? ? ? ? ? ? 1.333 ? ? +# +_struct_conn_type.id covale +_struct_conn_type.criteria ? +_struct_conn_type.reference ? +# +loop_ +_pdbx_modification_feature.ordinal +_pdbx_modification_feature.label_comp_id +_pdbx_modification_feature.label_asym_id +_pdbx_modification_feature.label_seq_id +_pdbx_modification_feature.label_alt_id +_pdbx_modification_feature.modified_residue_label_comp_id +_pdbx_modification_feature.modified_residue_label_asym_id +_pdbx_modification_feature.modified_residue_label_seq_id +_pdbx_modification_feature.modified_residue_label_alt_id +_pdbx_modification_feature.auth_comp_id +_pdbx_modification_feature.auth_asym_id +_pdbx_modification_feature.auth_seq_id +_pdbx_modification_feature.PDB_ins_code +_pdbx_modification_feature.symmetry +_pdbx_modification_feature.modified_residue_auth_comp_id +_pdbx_modification_feature.modified_residue_auth_asym_id +_pdbx_modification_feature.modified_residue_auth_seq_id +_pdbx_modification_feature.modified_residue_PDB_ins_code +_pdbx_modification_feature.modified_residue_symmetry +_pdbx_modification_feature.comp_id_linking_atom +_pdbx_modification_feature.modified_residue_id_linking_atom +_pdbx_modification_feature.modified_residue_id +_pdbx_modification_feature.ref_pcm_id +_pdbx_modification_feature.ref_comp_id +_pdbx_modification_feature.type +_pdbx_modification_feature.category +1 CR2 A 68 ? . . . . CR2 A 65 ? 1_555 . . . . . . . 'GLY, TYR, GLY' 1 CR2 None Chromophore/chromophore-like +2 CR2 B 68 ? . . . . CR2 B 65 ? 1_555 . . . . . . . 'GLY, TYR, GLY' 1 CR2 None Chromophore/chromophore-like +3 CR2 C 68 ? . . . . CR2 C 65 ? 1_555 . . . . . . . 'GLY, TYR, GLY' 1 CR2 None Chromophore/chromophore-like +4 CR2 D 68 ? . . . . CR2 D 65 ? 1_555 . . . . . . . 'GLY, TYR, GLY' 1 CR2 None Chromophore/chromophore-like +# +loop_ +_struct_mon_prot_cis.pdbx_id +_struct_mon_prot_cis.label_comp_id +_struct_mon_prot_cis.label_seq_id +_struct_mon_prot_cis.label_asym_id +_struct_mon_prot_cis.label_alt_id +_struct_mon_prot_cis.pdbx_PDB_ins_code +_struct_mon_prot_cis.auth_comp_id +_struct_mon_prot_cis.auth_seq_id +_struct_mon_prot_cis.auth_asym_id +_struct_mon_prot_cis.pdbx_label_comp_id_2 +_struct_mon_prot_cis.pdbx_label_seq_id_2 +_struct_mon_prot_cis.pdbx_label_asym_id_2 +_struct_mon_prot_cis.pdbx_PDB_ins_code_2 +_struct_mon_prot_cis.pdbx_auth_comp_id_2 +_struct_mon_prot_cis.pdbx_auth_seq_id_2 +_struct_mon_prot_cis.pdbx_auth_asym_id_2 +_struct_mon_prot_cis.pdbx_PDB_model_num +_struct_mon_prot_cis.pdbx_omega_angle +1 MET 89 A . ? MET 88 A PRO 90 A ? PRO 89 A 1 1.77 +2 MET 89 B . ? MET 88 B PRO 90 B ? PRO 89 B 1 2.91 +3 MET 89 C . ? MET 88 C PRO 90 C ? PRO 89 C 1 1.77 +4 MET 89 D . ? MET 88 D PRO 90 D ? PRO 89 D 1 3.93 +# +loop_ +_struct_sheet.id +_struct_sheet.type +_struct_sheet.number_strands +_struct_sheet.details +AA ? 12 ? +BA ? 12 ? +CA ? 12 ? +DA ? 12 ? +# +loop_ +_struct_sheet_order.sheet_id +_struct_sheet_order.range_id_1 +_struct_sheet_order.range_id_2 +_struct_sheet_order.offset +_struct_sheet_order.sense +AA 1 2 ? anti-parallel +AA 2 3 ? anti-parallel +AA 3 4 ? anti-parallel +AA 4 5 ? anti-parallel +AA 5 6 ? anti-parallel +AA 6 7 ? parallel +AA 7 8 ? anti-parallel +AA 8 9 ? anti-parallel +AA 9 10 ? anti-parallel +AA 10 11 ? anti-parallel +AA 11 12 ? anti-parallel +BA 1 2 ? anti-parallel +BA 2 3 ? anti-parallel +BA 3 4 ? anti-parallel +BA 4 5 ? anti-parallel +BA 5 6 ? anti-parallel +BA 6 7 ? anti-parallel +BA 7 8 ? anti-parallel +BA 8 9 ? anti-parallel +BA 9 10 ? anti-parallel +BA 10 11 ? anti-parallel +BA 11 12 ? parallel +CA 1 2 ? anti-parallel +CA 2 3 ? anti-parallel +CA 3 4 ? anti-parallel +CA 4 5 ? anti-parallel +CA 5 6 ? anti-parallel +CA 6 7 ? anti-parallel +CA 7 8 ? anti-parallel +CA 8 9 ? anti-parallel +CA 9 10 ? anti-parallel +CA 10 11 ? anti-parallel +CA 11 12 ? parallel +DA 1 2 ? anti-parallel +DA 2 3 ? anti-parallel +DA 3 4 ? anti-parallel +DA 4 5 ? anti-parallel +DA 5 6 ? anti-parallel +DA 6 7 ? parallel +DA 7 8 ? anti-parallel +DA 8 9 ? anti-parallel +DA 9 10 ? anti-parallel +DA 10 11 ? anti-parallel +DA 11 12 ? anti-parallel +# +loop_ +_struct_sheet_range.sheet_id +_struct_sheet_range.id +_struct_sheet_range.beg_label_comp_id +_struct_sheet_range.beg_label_asym_id +_struct_sheet_range.beg_label_seq_id +_struct_sheet_range.pdbx_beg_PDB_ins_code +_struct_sheet_range.end_label_comp_id +_struct_sheet_range.end_label_asym_id +_struct_sheet_range.end_label_seq_id +_struct_sheet_range.pdbx_end_PDB_ins_code +_struct_sheet_range.beg_auth_comp_id +_struct_sheet_range.beg_auth_asym_id +_struct_sheet_range.beg_auth_seq_id +_struct_sheet_range.end_auth_comp_id +_struct_sheet_range.end_auth_asym_id +_struct_sheet_range.end_auth_seq_id +AA 1 HIS A 149 ? ASN A 150 ? HIS A 148 ASN A 149 +AA 2 TYR A 201 ? SER A 209 ? TYR A 200 SER A 208 +AA 3 HIS A 218 ? ALA A 228 ? HIS A 217 ALA A 227 +AA 4 LYS A 44 ? CYS A 51 ? LYS A 41 CYS A 48 +AA 5 HIS A 28 ? ASP A 39 ? HIS A 25 ASP A 36 +AA 6 VAL A 15 ? VAL A 25 ? VAL A 12 VAL A 22 +AA 7 THR A 119 ? GLY A 128 ? THR A 118 GLY A 127 +AA 8 ASN A 106 ? GLU A 116 ? ASN A 105 GLU A 115 +AA 9 TYR A 93 ? PHE A 101 ? TYR A 92 PHE A 100 +AA 10 VAL A 177 ? PRO A 188 ? VAL A 176 PRO A 187 +AA 11 GLY A 161 ? ASN A 171 ? GLY A 160 ASN A 170 +AA 12 TYR A 152 ? ASP A 156 ? TYR A 151 ASP A 155 +BA 1 VAL B 15 ? VAL B 25 ? VAL B 12 VAL B 22 +BA 2 HIS B 28 ? ASP B 39 ? HIS B 25 ASP B 36 +BA 3 LYS B 44 ? CYS B 51 ? LYS B 41 CYS B 48 +BA 4 HIS B 218 ? ALA B 228 ? HIS B 217 ALA B 227 +BA 5 HIS B 200 ? SER B 209 ? HIS B 199 SER B 208 +BA 6 HIS B 149 ? ASP B 156 ? HIS B 148 ASP B 155 +BA 7 GLY B 161 ? ASN B 171 ? GLY B 160 ASN B 170 +BA 8 VAL B 177 ? PRO B 188 ? VAL B 176 PRO B 187 +BA 9 TYR B 93 ? PHE B 101 ? TYR B 92 PHE B 100 +BA 10 ASN B 106 ? GLU B 116 ? ASN B 105 GLU B 115 +BA 11 THR B 119 ? ILE B 129 ? THR B 118 ILE B 128 +BA 12 VAL B 15 ? VAL B 25 ? VAL B 12 VAL B 22 +CA 1 VAL C 15 ? VAL C 25 ? VAL C 12 VAL C 22 +CA 2 HIS C 28 ? ASP C 39 ? HIS C 25 ASP C 36 +CA 3 LYS C 44 ? CYS C 51 ? LYS C 41 CYS C 48 +CA 4 HIS C 218 ? ALA C 228 ? HIS C 217 ALA C 227 +CA 5 HIS C 200 ? SER C 209 ? HIS C 199 SER C 208 +CA 6 HIS C 149 ? ASP C 156 ? HIS C 148 ASP C 155 +CA 7 GLY C 161 ? ASN C 171 ? GLY C 160 ASN C 170 +CA 8 VAL C 177 ? PRO C 188 ? VAL C 176 PRO C 187 +CA 9 TYR C 93 ? PHE C 101 ? TYR C 92 PHE C 100 +CA 10 ASN C 106 ? GLU C 116 ? ASN C 105 GLU C 115 +CA 11 THR C 119 ? ILE C 129 ? THR C 118 ILE C 128 +CA 12 VAL C 15 ? VAL C 25 ? VAL C 12 VAL C 22 +DA 1 HIS D 149 ? ASN D 150 ? HIS D 148 ASN D 149 +DA 2 TYR D 201 ? SER D 209 ? TYR D 200 SER D 208 +DA 3 HIS D 218 ? ALA D 228 ? HIS D 217 ALA D 227 +DA 4 LYS D 44 ? CYS D 51 ? LYS D 41 CYS D 48 +DA 5 HIS D 28 ? ASP D 39 ? HIS D 25 ASP D 36 +DA 6 VAL D 15 ? VAL D 25 ? VAL D 12 VAL D 22 +DA 7 THR D 119 ? GLY D 128 ? THR D 118 GLY D 127 +DA 8 ASN D 106 ? GLU D 116 ? ASN D 105 GLU D 115 +DA 9 TYR D 93 ? PHE D 101 ? TYR D 92 PHE D 100 +DA 10 VAL D 177 ? PRO D 188 ? VAL D 176 PRO D 187 +DA 11 GLY D 161 ? ASN D 171 ? GLY D 160 ASN D 170 +DA 12 TYR D 152 ? ASP D 156 ? TYR D 151 ASP D 155 +# +loop_ +_pdbx_struct_sheet_hbond.sheet_id +_pdbx_struct_sheet_hbond.range_id_1 +_pdbx_struct_sheet_hbond.range_id_2 +_pdbx_struct_sheet_hbond.range_1_label_atom_id +_pdbx_struct_sheet_hbond.range_1_label_comp_id +_pdbx_struct_sheet_hbond.range_1_label_asym_id +_pdbx_struct_sheet_hbond.range_1_label_seq_id +_pdbx_struct_sheet_hbond.range_1_PDB_ins_code +_pdbx_struct_sheet_hbond.range_1_auth_atom_id +_pdbx_struct_sheet_hbond.range_1_auth_comp_id +_pdbx_struct_sheet_hbond.range_1_auth_asym_id +_pdbx_struct_sheet_hbond.range_1_auth_seq_id +_pdbx_struct_sheet_hbond.range_2_label_atom_id +_pdbx_struct_sheet_hbond.range_2_label_comp_id +_pdbx_struct_sheet_hbond.range_2_label_asym_id +_pdbx_struct_sheet_hbond.range_2_label_seq_id +_pdbx_struct_sheet_hbond.range_2_PDB_ins_code +_pdbx_struct_sheet_hbond.range_2_auth_atom_id +_pdbx_struct_sheet_hbond.range_2_auth_comp_id +_pdbx_struct_sheet_hbond.range_2_auth_asym_id +_pdbx_struct_sheet_hbond.range_2_auth_seq_id +AA 1 2 N HIS A 149 ? N HIS A 148 O THR A 204 ? O THR A 203 +AA 2 3 N SER A 209 ? N SER A 208 O VAL A 220 ? O VAL A 219 +AA 3 4 N GLU A 223 ? N GLU A 222 O LEU A 45 ? O LEU A 42 +AA 4 5 N ILE A 50 ? N ILE A 47 O SER A 33 ? O SER A 30 +AA 5 6 N GLY A 38 ? N GLY A 35 O VAL A 15 ? O VAL A 12 +AA 6 7 N LEU A 18 ? N LEU A 15 O LEU A 120 ? O LEU A 119 +AA 7 8 N LYS A 127 ? N LYS A 126 O LYS A 108 ? O LYS A 107 +AA 8 9 N VAL A 113 ? N VAL A 112 O TYR A 93 ? O TYR A 92 +AA 9 10 N PHE A 100 ? N PHE A 99 O ASP A 181 ? O ASP A 180 +AA 10 11 N ASN A 186 ? N ASN A 185 O ILE A 162 ? O ILE A 161 +AA 11 12 N ASN A 165 ? N ASN A 164 O TYR A 152 ? O TYR A 151 +BA 1 2 N VAL B 25 ? N VAL B 22 O HIS B 28 ? O HIS B 25 +BA 2 3 N ASP B 39 ? N ASP B 36 O LYS B 44 ? O LYS B 41 +BA 3 4 N PHE B 49 ? N PHE B 46 O MET B 219 ? O MET B 218 +BA 4 5 N ALA B 228 ? N ALA B 227 O TYR B 201 ? O TYR B 200 +BA 5 6 N THR B 204 ? N THR B 203 O HIS B 149 ? O HIS B 148 +BA 6 7 N ASP B 156 ? N ASP B 155 O GLY B 161 ? O GLY B 160 +BA 7 8 N HIS B 170 ? N HIS B 169 O GLN B 178 ? O GLN B 177 +BA 8 9 N THR B 187 ? N THR B 186 O VAL B 94 ? O VAL B 93 +BA 9 10 N ILE B 99 ? N ILE B 98 O TYR B 107 ? O TYR B 106 +BA 10 11 N GLU B 116 ? N GLU B 115 O THR B 119 ? O THR B 118 +BA 11 12 N LEU B 120 ? N LEU B 119 O PRO B 16 ? O PRO B 13 +CA 1 2 N VAL C 25 ? N VAL C 22 O HIS C 28 ? O HIS C 25 +CA 2 3 N ASP C 39 ? N ASP C 36 O LYS C 44 ? O LYS C 41 +CA 3 4 N PHE C 49 ? N PHE C 46 O MET C 219 ? O MET C 218 +CA 4 5 N ALA C 228 ? N ALA C 227 O TYR C 201 ? O TYR C 200 +CA 5 6 N THR C 204 ? N THR C 203 O HIS C 149 ? O HIS C 148 +CA 6 7 N ASP C 156 ? N ASP C 155 O GLY C 161 ? O GLY C 160 +CA 7 8 N HIS C 170 ? N HIS C 169 O GLN C 178 ? O GLN C 177 +CA 8 9 N THR C 187 ? N THR C 186 O VAL C 94 ? O VAL C 93 +CA 9 10 N ILE C 99 ? N ILE C 98 O TYR C 107 ? O TYR C 106 +CA 10 11 N GLU C 116 ? N GLU C 115 O THR C 119 ? O THR C 118 +CA 11 12 N LEU C 120 ? N LEU C 119 O PRO C 16 ? O PRO C 13 +DA 1 2 N HIS D 149 ? N HIS D 148 O THR D 204 ? O THR D 203 +DA 2 3 N SER D 209 ? N SER D 208 O VAL D 220 ? O VAL D 219 +DA 3 4 N GLU D 223 ? N GLU D 222 O LEU D 45 ? O LEU D 42 +DA 4 5 N ILE D 50 ? N ILE D 47 O SER D 33 ? O SER D 30 +DA 5 6 N GLY D 38 ? N GLY D 35 O VAL D 15 ? O VAL D 12 +DA 6 7 N LEU D 18 ? N LEU D 15 O LEU D 120 ? O LEU D 119 +DA 7 8 N LYS D 127 ? N LYS D 126 O LYS D 108 ? O LYS D 107 +DA 8 9 N VAL D 113 ? N VAL D 112 O TYR D 93 ? O TYR D 92 +DA 9 10 N PHE D 100 ? N PHE D 99 O ASP D 181 ? O ASP D 180 +DA 10 11 N ASN D 186 ? N ASN D 185 O ILE D 162 ? O ILE D 161 +DA 11 12 N ASN D 165 ? N ASN D 164 O TYR D 152 ? O TYR D 151 +# +_pdbx_entry_details.entry_id 4BDU +_pdbx_entry_details.compound_details ? +_pdbx_entry_details.source_details ? +_pdbx_entry_details.nonpolymer_details ? +_pdbx_entry_details.sequence_details +;THE SEQUENCE OF GFP IS AS DESCRIBED IN SUZUKI ET AL. (2010) + ACTA CRYS D 66, 1059, BEARING THE EXTRA MUTATION, A206N + BAX TRUNCATED TO LEAVE ALPHA2 TO ALPHA5, MUTATIONS S62C, + S126C. + GFP AND BAX CRYSTALLIZED AS A SINGLE FUSION PROTEIN. + 1000 HAS BEEN ADDED TO THE SEQUENCE NUMBERING OF BAX TO + PRESERVE UNP NUMBERING. +; +_pdbx_entry_details.has_ligand_of_interest ? +_pdbx_entry_details.has_protein_modification Y +# +loop_ +_pdbx_validate_close_contact.id +_pdbx_validate_close_contact.PDB_model_num +_pdbx_validate_close_contact.auth_atom_id_1 +_pdbx_validate_close_contact.auth_asym_id_1 +_pdbx_validate_close_contact.auth_comp_id_1 +_pdbx_validate_close_contact.auth_seq_id_1 +_pdbx_validate_close_contact.PDB_ins_code_1 +_pdbx_validate_close_contact.label_alt_id_1 +_pdbx_validate_close_contact.auth_atom_id_2 +_pdbx_validate_close_contact.auth_asym_id_2 +_pdbx_validate_close_contact.auth_comp_id_2 +_pdbx_validate_close_contact.auth_seq_id_2 +_pdbx_validate_close_contact.PDB_ins_code_2 +_pdbx_validate_close_contact.label_alt_id_2 +_pdbx_validate_close_contact.dist +1 1 OH C TYR 143 ? ? O C HOH 2014 ? ? 1.93 +2 1 OE1 A GLU 5 ? ? O A HOH 2001 ? ? 2.00 +3 1 OD1 B ASP 1071 ? ? O B HOH 4001 ? ? 2.05 +4 1 OG1 C THR 50 ? ? O C HOH 2003 ? ? 2.12 +5 1 OE2 A GLU 90 ? ? O A HOH 2011 ? ? 2.13 +6 1 OD1 C ASN 105 ? ? O C HOH 2011 ? ? 2.18 +# +loop_ +_pdbx_validate_torsion.id +_pdbx_validate_torsion.PDB_model_num +_pdbx_validate_torsion.auth_comp_id +_pdbx_validate_torsion.auth_asym_id +_pdbx_validate_torsion.auth_seq_id +_pdbx_validate_torsion.PDB_ins_code +_pdbx_validate_torsion.label_alt_id +_pdbx_validate_torsion.phi +_pdbx_validate_torsion.psi +1 1 GLN A 69 ? ? -59.06 1.15 +2 1 LYS A 79 ? ? -41.86 3.24 +3 1 ASP A 103 ? ? -170.85 -173.40 +4 1 GLU A 132 ? ? -39.97 -17.87 +5 1 ILE A 136 ? ? -60.65 -84.93 +6 1 VAL A 150 ? ? -108.09 79.32 +7 1 ASP A 180 ? ? -57.64 103.47 +8 1 ALA A 227 ? ? -162.84 -164.82 +9 1 ASN A 1073 ? ? -62.96 97.90 +10 1 SER A 1087 ? ? -111.83 77.98 +11 1 ASN A 1104 ? ? -106.46 76.45 +12 1 VAL A 1121 ? ? -146.07 -62.57 +13 1 GLN B 69 ? ? -49.07 9.07 +14 1 LYS B 79 ? ? -47.78 3.21 +15 1 GLU B 132 ? ? -53.09 -7.55 +16 1 ILE B 136 ? ? -69.69 -72.62 +17 1 HIS B 139 ? ? 60.21 65.86 +18 1 PHE B 165 ? ? -170.18 -176.88 +19 1 ASP B 173 ? ? -66.44 3.89 +20 1 ALA B 227 ? ? -167.32 -166.20 +21 1 ASN B 1073 ? ? -63.17 99.03 +22 1 SER B 1087 ? ? -111.54 78.14 +23 1 ASN B 1104 ? ? -104.94 76.93 +24 1 VAL B 1121 ? ? -145.60 -62.46 +25 1 GLN C 69 ? ? -51.12 11.35 +26 1 LYS C 79 ? ? -47.59 3.02 +27 1 GLU C 132 ? ? -59.35 -8.95 +28 1 ILE C 136 ? ? -73.04 -73.62 +29 1 HIS C 139 ? ? 60.43 64.20 +30 1 TYR C 143 ? ? -68.17 63.56 +31 1 PHE C 165 ? ? -170.97 -178.63 +32 1 ASP C 173 ? ? -68.24 10.02 +33 1 ALA C 227 ? ? -171.24 -169.90 +34 1 ASN C 1073 ? ? -63.32 99.10 +35 1 SER C 1087 ? ? -111.59 78.24 +36 1 ASN C 1104 ? ? -104.85 77.08 +37 1 VAL C 1121 ? ? -145.85 -62.61 +38 1 GLN D 69 ? ? -58.58 0.47 +39 1 LYS D 79 ? ? -44.46 0.64 +40 1 ASP D 103 ? ? -170.29 -172.90 +41 1 GLU D 132 ? ? -40.19 -15.80 +42 1 ILE D 136 ? ? -57.09 -84.02 +43 1 ASP D 180 ? ? -56.24 109.63 +44 1 ALA D 227 ? ? -161.48 -163.36 +45 1 ASN D 1073 ? ? -62.87 97.85 +46 1 SER D 1087 ? ? -111.71 78.05 +47 1 ASN D 1104 ? ? -106.30 76.65 +48 1 VAL D 1121 ? ? -146.17 -62.72 +# +loop_ +_pdbx_struct_mod_residue.id +_pdbx_struct_mod_residue.label_asym_id +_pdbx_struct_mod_residue.label_comp_id +_pdbx_struct_mod_residue.label_seq_id +_pdbx_struct_mod_residue.auth_asym_id +_pdbx_struct_mod_residue.auth_comp_id +_pdbx_struct_mod_residue.auth_seq_id +_pdbx_struct_mod_residue.PDB_ins_code +_pdbx_struct_mod_residue.parent_comp_id +_pdbx_struct_mod_residue.details +1 A CR2 68 A CR2 65 ? GLY ? +2 A CR2 68 A CR2 65 ? TYR ? +3 A CR2 68 A CR2 65 ? GLY ? +4 B CR2 68 B CR2 65 ? GLY ? +5 B CR2 68 B CR2 65 ? TYR ? +6 B CR2 68 B CR2 65 ? GLY ? +7 C CR2 68 C CR2 65 ? GLY ? +8 C CR2 68 C CR2 65 ? TYR ? +9 C CR2 68 C CR2 65 ? GLY ? +10 D CR2 68 D CR2 65 ? GLY ? +11 D CR2 68 D CR2 65 ? TYR ? +12 D CR2 68 D CR2 65 ? GLY ? +# +loop_ +_pdbx_refine_tls.pdbx_refine_id +_pdbx_refine_tls.id +_pdbx_refine_tls.details +_pdbx_refine_tls.method +_pdbx_refine_tls.origin_x +_pdbx_refine_tls.origin_y +_pdbx_refine_tls.origin_z +_pdbx_refine_tls.T[1][1] +_pdbx_refine_tls.T[2][2] +_pdbx_refine_tls.T[3][3] +_pdbx_refine_tls.T[1][2] +_pdbx_refine_tls.T[1][3] +_pdbx_refine_tls.T[2][3] +_pdbx_refine_tls.L[1][1] +_pdbx_refine_tls.L[2][2] +_pdbx_refine_tls.L[3][3] +_pdbx_refine_tls.L[1][2] +_pdbx_refine_tls.L[1][3] +_pdbx_refine_tls.L[2][3] +_pdbx_refine_tls.S[1][1] +_pdbx_refine_tls.S[1][2] +_pdbx_refine_tls.S[1][3] +_pdbx_refine_tls.S[2][1] +_pdbx_refine_tls.S[2][2] +_pdbx_refine_tls.S[2][3] +_pdbx_refine_tls.S[3][1] +_pdbx_refine_tls.S[3][2] +_pdbx_refine_tls.S[3][3] +'X-RAY DIFFRACTION' 1 ? refined 14.5202 102.1189 103.9046 1.2765 0.2384 0.3127 -0.4146 0.1666 -0.0782 0.0498 0.0309 0.0261 +-0.0009 0.0190 0.0099 -0.0241 0.1045 -0.0535 -0.0223 -0.0383 -0.0212 -0.0238 0.0694 -0.0356 +'X-RAY DIFFRACTION' 2 ? refined 14.5013 92.4246 30.2147 0.6942 0.7536 0.3502 0.6282 -0.0913 -0.0031 0.0389 0.0236 0.0382 +-0.0185 0.0045 -0.0048 -0.0470 -0.1196 0.0881 0.0122 -0.0234 -0.0044 0.0850 0.2035 -0.0696 +'X-RAY DIFFRACTION' 3 ? refined 31.1308 63.6067 135.2657 0.9775 0.0606 0.6445 0.3701 0.0371 0.0406 0.0187 0.0524 0.0409 +0.0067 0.0183 0.0079 -0.0315 0.0364 -0.0381 -0.1100 0.0500 0.0388 -0.2535 0.0339 0.0014 +'X-RAY DIFFRACTION' 4 ? refined 39.5524 58.7886 61.5724 -0.1656 1.1744 0.6591 0.4455 -0.0369 -0.1724 0.0624 0.0461 0.0149 +0.0185 -0.0226 -0.0160 0.0454 0.0213 0.0122 0.0967 -0.0544 0.0103 -0.1039 0.0877 -0.0227 +'X-RAY DIFFRACTION' 5 ? refined 14.3873 97.0167 67.0126 1.1897 1.0481 0.7476 0.1920 -0.0236 0.0933 -0.0018 0.0043 0.0034 +-0.0010 0.0015 0.0042 0.0585 0.0818 0.0567 0.0057 0.1131 0.0990 0.0154 0.1163 -0.0000 +'X-RAY DIFFRACTION' 6 ? refined 35.0428 61.2253 98.5901 1.0241 0.9144 0.6982 0.2132 -0.0403 0.0942 0.0077 0.0019 0.0067 +-0.0043 -0.0095 0.0020 0.1256 -0.0392 -0.1049 0.0432 0.0423 0.0062 -0.1035 0.0470 0.0000 +# +loop_ +_pdbx_refine_tls_group.pdbx_refine_id +_pdbx_refine_tls_group.id +_pdbx_refine_tls_group.refine_tls_id +_pdbx_refine_tls_group.beg_auth_asym_id +_pdbx_refine_tls_group.beg_auth_seq_id +_pdbx_refine_tls_group.beg_label_asym_id +_pdbx_refine_tls_group.beg_label_seq_id +_pdbx_refine_tls_group.end_auth_asym_id +_pdbx_refine_tls_group.end_auth_seq_id +_pdbx_refine_tls_group.end_label_asym_id +_pdbx_refine_tls_group.end_label_seq_id +_pdbx_refine_tls_group.selection +_pdbx_refine_tls_group.selection_details +'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? 'CHAIN A AND RESID 1:230' +'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? 'CHAIN B AND RESID 1:230' +'X-RAY DIFFRACTION' 3 3 ? ? ? ? ? ? ? ? ? 'CHAIN C AND RESID 1:230' +'X-RAY DIFFRACTION' 4 4 ? ? ? ? ? ? ? ? ? 'CHAIN D AND RESID 1:230' +'X-RAY DIFFRACTION' 5 5 ? ? ? ? ? ? ? ? ? 'CHAIN A OR CHAIN B AND RESID 1053:1125' +'X-RAY DIFFRACTION' 6 6 ? ? ? ? ? ? ? ? ? 'CHAIN C OR CHAIN D AND RESID 1053:1125' +# +_pdbx_database_remark.id 700 +_pdbx_database_remark.text +; +SHEET +DETERMINATION METHOD: DSSP +THE SHEETS PRESENTED AS "BA" IN EACH CHAIN ON SHEET RECORDS +BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY +A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS +ARE IDENTICAL. + +THE SHEETS PRESENTED AS "CA" IN EACH CHAIN ON SHEET RECORDS +BELOW IS ACTUALLY AN 11-STRANDED BARREL THIS IS REPRESENTED BY +A 12-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS +ARE IDENTICAL. +; +# +loop_ +_pdbx_unobs_or_zero_occ_residues.id +_pdbx_unobs_or_zero_occ_residues.PDB_model_num +_pdbx_unobs_or_zero_occ_residues.polymer_flag +_pdbx_unobs_or_zero_occ_residues.occupancy_flag +_pdbx_unobs_or_zero_occ_residues.auth_asym_id +_pdbx_unobs_or_zero_occ_residues.auth_comp_id +_pdbx_unobs_or_zero_occ_residues.auth_seq_id +_pdbx_unobs_or_zero_occ_residues.PDB_ins_code +_pdbx_unobs_or_zero_occ_residues.label_asym_id +_pdbx_unobs_or_zero_occ_residues.label_comp_id +_pdbx_unobs_or_zero_occ_residues.label_seq_id +1 1 Y 1 A GLY -2 ? A GLY 1 +2 1 Y 1 A SER -1 ? A SER 2 +3 1 Y 1 A HIS 0 ? A HIS 3 +4 1 Y 1 A MET 1 ? A MET 4 +5 1 Y 1 A GLY 231 ? A GLY 232 +6 1 Y 1 A SER 232 ? A SER 233 +7 1 Y 1 A ASP 1053 ? A ASP 234 +8 1 Y 1 A LYS 1123 ? A LYS 304 +9 1 Y 1 A ALA 1124 ? A ALA 305 +10 1 Y 1 A LEU 1125 ? A LEU 306 +11 1 Y 1 A SER 1126 ? A SER 307 +12 1 Y 1 A THR 1127 ? A THR 308 +13 1 Y 1 A LYS 1128 ? A LYS 309 +14 1 Y 1 B GLY -2 ? B GLY 1 +15 1 Y 1 B SER -1 ? B SER 2 +16 1 Y 1 B HIS 0 ? B HIS 3 +17 1 Y 1 B MET 1 ? B MET 4 +18 1 Y 1 B GLY 231 ? B GLY 232 +19 1 Y 1 B SER 232 ? B SER 233 +20 1 Y 1 B ASP 1053 ? B ASP 234 +21 1 Y 1 B LYS 1123 ? B LYS 304 +22 1 Y 1 B ALA 1124 ? B ALA 305 +23 1 Y 1 B LEU 1125 ? B LEU 306 +24 1 Y 1 B SER 1126 ? B SER 307 +25 1 Y 1 B THR 1127 ? B THR 308 +26 1 Y 1 B LYS 1128 ? B LYS 309 +27 1 Y 1 C GLY -2 ? C GLY 1 +28 1 Y 1 C SER -1 ? C SER 2 +29 1 Y 1 C HIS 0 ? C HIS 3 +30 1 Y 1 C MET 1 ? C MET 4 +31 1 Y 1 C GLY 231 ? C GLY 232 +32 1 Y 1 C SER 232 ? C SER 233 +33 1 Y 1 C ASP 1053 ? C ASP 234 +34 1 Y 1 C LYS 1123 ? C LYS 304 +35 1 Y 1 C ALA 1124 ? C ALA 305 +36 1 Y 1 C LEU 1125 ? C LEU 306 +37 1 Y 1 C SER 1126 ? C SER 307 +38 1 Y 1 C THR 1127 ? C THR 308 +39 1 Y 1 C LYS 1128 ? C LYS 309 +40 1 Y 1 D GLY -2 ? D GLY 1 +41 1 Y 1 D SER -1 ? D SER 2 +42 1 Y 1 D HIS 0 ? D HIS 3 +43 1 Y 1 D MET 1 ? D MET 4 +44 1 Y 1 D GLY 231 ? D GLY 232 +45 1 Y 1 D SER 232 ? D SER 233 +46 1 Y 1 D ASP 1053 ? D ASP 234 +47 1 Y 1 D LYS 1123 ? D LYS 304 +48 1 Y 1 D ALA 1124 ? D ALA 305 +49 1 Y 1 D LEU 1125 ? D LEU 306 +50 1 Y 1 D SER 1126 ? D SER 307 +51 1 Y 1 D THR 1127 ? D THR 308 +52 1 Y 1 D LYS 1128 ? D LYS 309 +# +loop_ +_chem_comp_atom.comp_id +_chem_comp_atom.atom_id +_chem_comp_atom.type_symbol +_chem_comp_atom.pdbx_aromatic_flag +_chem_comp_atom.pdbx_stereo_config +_chem_comp_atom.pdbx_ordinal +ALA N N N N 1 +ALA CA C N S 2 +ALA C C N N 3 +ALA O O N N 4 +ALA CB C N N 5 +ALA OXT O N N 6 +ALA H H N N 7 +ALA H2 H N N 8 +ALA HA H N N 9 +ALA HB1 H N N 10 +ALA HB2 H N N 11 +ALA HB3 H N N 12 +ALA HXT H N N 13 +ARG N N N N 14 +ARG CA C N S 15 +ARG C C N N 16 +ARG O O N N 17 +ARG CB C N N 18 +ARG CG C N N 19 +ARG CD C N N 20 +ARG NE N N N 21 +ARG CZ C N N 22 +ARG NH1 N N N 23 +ARG NH2 N N N 24 +ARG OXT O N N 25 +ARG H H N N 26 +ARG H2 H N N 27 +ARG HA H N N 28 +ARG HB2 H N N 29 +ARG HB3 H N N 30 +ARG HG2 H N N 31 +ARG HG3 H N N 32 +ARG HD2 H N N 33 +ARG HD3 H N N 34 +ARG HE H N N 35 +ARG HH11 H N N 36 +ARG HH12 H N N 37 +ARG HH21 H N N 38 +ARG HH22 H N N 39 +ARG HXT H N N 40 +ASN N N N N 41 +ASN CA C N S 42 +ASN C C N N 43 +ASN O O N N 44 +ASN CB C N N 45 +ASN CG C N N 46 +ASN OD1 O N N 47 +ASN ND2 N N N 48 +ASN OXT O N N 49 +ASN H H N N 50 +ASN H2 H N N 51 +ASN HA H N N 52 +ASN HB2 H N N 53 +ASN HB3 H N N 54 +ASN HD21 H N N 55 +ASN HD22 H N N 56 +ASN HXT H N N 57 +ASP N N N N 58 +ASP CA C N S 59 +ASP C C N N 60 +ASP O O N N 61 +ASP CB C N N 62 +ASP CG C N N 63 +ASP OD1 O N N 64 +ASP OD2 O N N 65 +ASP OXT O N N 66 +ASP H H N N 67 +ASP H2 H N N 68 +ASP HA H N N 69 +ASP HB2 H N N 70 +ASP HB3 H N N 71 +ASP HD2 H N N 72 +ASP HXT H N N 73 +CR2 N1 N N N 74 +CR2 CA1 C N N 75 +CR2 C1 C N N 76 +CR2 N2 N N N 77 +CR2 N3 N N N 78 +CR2 C2 C N N 79 +CR2 O2 O N N 80 +CR2 CA2 C N N 81 +CR2 CA3 C N N 82 +CR2 C3 C N N 83 +CR2 O3 O N N 84 +CR2 CB2 C N N 85 +CR2 CG2 C Y N 86 +CR2 CD1 C Y N 87 +CR2 CD2 C Y N 88 +CR2 CE1 C Y N 89 +CR2 CE2 C Y N 90 +CR2 CZ C Y N 91 +CR2 OH O N N 92 +CR2 OXT O N N 93 +CR2 H H N N 94 +CR2 H2 H N N 95 +CR2 HA1 H N N 96 +CR2 HA12 H N N 97 +CR2 HA31 H N N 98 +CR2 HA32 H N N 99 +CR2 HB2 H N N 100 +CR2 HD1 H N N 101 +CR2 HD2 H N N 102 +CR2 HE1 H N N 103 +CR2 HE2 H N N 104 +CR2 HOH H N N 105 +CR2 HXT H N N 106 +CYS N N N N 107 +CYS CA C N R 108 +CYS C C N N 109 +CYS O O N N 110 +CYS CB C N N 111 +CYS SG S N N 112 +CYS OXT O N N 113 +CYS H H N N 114 +CYS H2 H N N 115 +CYS HA H N N 116 +CYS HB2 H N N 117 +CYS HB3 H N N 118 +CYS HG H N N 119 +CYS HXT H N N 120 +GLN N N N N 121 +GLN CA C N S 122 +GLN C C N N 123 +GLN O O N N 124 +GLN CB C N N 125 +GLN CG C N N 126 +GLN CD C N N 127 +GLN OE1 O N N 128 +GLN NE2 N N N 129 +GLN OXT O N N 130 +GLN H H N N 131 +GLN H2 H N N 132 +GLN HA H N N 133 +GLN HB2 H N N 134 +GLN HB3 H N N 135 +GLN HG2 H N N 136 +GLN HG3 H N N 137 +GLN HE21 H N N 138 +GLN HE22 H N N 139 +GLN HXT H N N 140 +GLU N N N N 141 +GLU CA C N S 142 +GLU C C N N 143 +GLU O O N N 144 +GLU CB C N N 145 +GLU CG C N N 146 +GLU CD C N N 147 +GLU OE1 O N N 148 +GLU OE2 O N N 149 +GLU OXT O N N 150 +GLU H H N N 151 +GLU H2 H N N 152 +GLU HA H N N 153 +GLU HB2 H N N 154 +GLU HB3 H N N 155 +GLU HG2 H N N 156 +GLU HG3 H N N 157 +GLU HE2 H N N 158 +GLU HXT H N N 159 +GLY N N N N 160 +GLY CA C N N 161 +GLY C C N N 162 +GLY O O N N 163 +GLY OXT O N N 164 +GLY H H N N 165 +GLY H2 H N N 166 +GLY HA2 H N N 167 +GLY HA3 H N N 168 +GLY HXT H N N 169 +HIS N N N N 170 +HIS CA C N S 171 +HIS C C N N 172 +HIS O O N N 173 +HIS CB C N N 174 +HIS CG C Y N 175 +HIS ND1 N Y N 176 +HIS CD2 C Y N 177 +HIS CE1 C Y N 178 +HIS NE2 N Y N 179 +HIS OXT O N N 180 +HIS H H N N 181 +HIS H2 H N N 182 +HIS HA H N N 183 +HIS HB2 H N N 184 +HIS HB3 H N N 185 +HIS HD1 H N N 186 +HIS HD2 H N N 187 +HIS HE1 H N N 188 +HIS HE2 H N N 189 +HIS HXT H N N 190 +HOH O O N N 191 +HOH H1 H N N 192 +HOH H2 H N N 193 +ILE N N N N 194 +ILE CA C N S 195 +ILE C C N N 196 +ILE O O N N 197 +ILE CB C N S 198 +ILE CG1 C N N 199 +ILE CG2 C N N 200 +ILE CD1 C N N 201 +ILE OXT O N N 202 +ILE H H N N 203 +ILE H2 H N N 204 +ILE HA H N N 205 +ILE HB H N N 206 +ILE HG12 H N N 207 +ILE HG13 H N N 208 +ILE HG21 H N N 209 +ILE HG22 H N N 210 +ILE HG23 H N N 211 +ILE HD11 H N N 212 +ILE HD12 H N N 213 +ILE HD13 H N N 214 +ILE HXT H N N 215 +LEU N N N N 216 +LEU CA C N S 217 +LEU C C N N 218 +LEU O O N N 219 +LEU CB C N N 220 +LEU CG C N N 221 +LEU CD1 C N N 222 +LEU CD2 C N N 223 +LEU OXT O N N 224 +LEU H H N N 225 +LEU H2 H N N 226 +LEU HA H N N 227 +LEU HB2 H N N 228 +LEU HB3 H N N 229 +LEU HG H N N 230 +LEU HD11 H N N 231 +LEU HD12 H N N 232 +LEU HD13 H N N 233 +LEU HD21 H N N 234 +LEU HD22 H N N 235 +LEU HD23 H N N 236 +LEU HXT H N N 237 +LYS N N N N 238 +LYS CA C N S 239 +LYS C C N N 240 +LYS O O N N 241 +LYS CB C N N 242 +LYS CG C N N 243 +LYS CD C N N 244 +LYS CE C N N 245 +LYS NZ N N N 246 +LYS OXT O N N 247 +LYS H H N N 248 +LYS H2 H N N 249 +LYS HA H N N 250 +LYS HB2 H N N 251 +LYS HB3 H N N 252 +LYS HG2 H N N 253 +LYS HG3 H N N 254 +LYS HD2 H N N 255 +LYS HD3 H N N 256 +LYS HE2 H N N 257 +LYS HE3 H N N 258 +LYS HZ1 H N N 259 +LYS HZ2 H N N 260 +LYS HZ3 H N N 261 +LYS HXT H N N 262 +MET N N N N 263 +MET CA C N S 264 +MET C C N N 265 +MET O O N N 266 +MET CB C N N 267 +MET CG C N N 268 +MET SD S N N 269 +MET CE C N N 270 +MET OXT O N N 271 +MET H H N N 272 +MET H2 H N N 273 +MET HA H N N 274 +MET HB2 H N N 275 +MET HB3 H N N 276 +MET HG2 H N N 277 +MET HG3 H N N 278 +MET HE1 H N N 279 +MET HE2 H N N 280 +MET HE3 H N N 281 +MET HXT H N N 282 +PHE N N N N 283 +PHE CA C N S 284 +PHE C C N N 285 +PHE O O N N 286 +PHE CB C N N 287 +PHE CG C Y N 288 +PHE CD1 C Y N 289 +PHE CD2 C Y N 290 +PHE CE1 C Y N 291 +PHE CE2 C Y N 292 +PHE CZ C Y N 293 +PHE OXT O N N 294 +PHE H H N N 295 +PHE H2 H N N 296 +PHE HA H N N 297 +PHE HB2 H N N 298 +PHE HB3 H N N 299 +PHE HD1 H N N 300 +PHE HD2 H N N 301 +PHE HE1 H N N 302 +PHE HE2 H N N 303 +PHE HZ H N N 304 +PHE HXT H N N 305 +PRO N N N N 306 +PRO CA C N S 307 +PRO C C N N 308 +PRO O O N N 309 +PRO CB C N N 310 +PRO CG C N N 311 +PRO CD C N N 312 +PRO OXT O N N 313 +PRO H H N N 314 +PRO HA H N N 315 +PRO HB2 H N N 316 +PRO HB3 H N N 317 +PRO HG2 H N N 318 +PRO HG3 H N N 319 +PRO HD2 H N N 320 +PRO HD3 H N N 321 +PRO HXT H N N 322 +SER N N N N 323 +SER CA C N S 324 +SER C C N N 325 +SER O O N N 326 +SER CB C N N 327 +SER OG O N N 328 +SER OXT O N N 329 +SER H H N N 330 +SER H2 H N N 331 +SER HA H N N 332 +SER HB2 H N N 333 +SER HB3 H N N 334 +SER HG H N N 335 +SER HXT H N N 336 +THR N N N N 337 +THR CA C N S 338 +THR C C N N 339 +THR O O N N 340 +THR CB C N R 341 +THR OG1 O N N 342 +THR CG2 C N N 343 +THR OXT O N N 344 +THR H H N N 345 +THR H2 H N N 346 +THR HA H N N 347 +THR HB H N N 348 +THR HG1 H N N 349 +THR HG21 H N N 350 +THR HG22 H N N 351 +THR HG23 H N N 352 +THR HXT H N N 353 +TRP N N N N 354 +TRP CA C N S 355 +TRP C C N N 356 +TRP O O N N 357 +TRP CB C N N 358 +TRP CG C Y N 359 +TRP CD1 C Y N 360 +TRP CD2 C Y N 361 +TRP NE1 N Y N 362 +TRP CE2 C Y N 363 +TRP CE3 C Y N 364 +TRP CZ2 C Y N 365 +TRP CZ3 C Y N 366 +TRP CH2 C Y N 367 +TRP OXT O N N 368 +TRP H H N N 369 +TRP H2 H N N 370 +TRP HA H N N 371 +TRP HB2 H N N 372 +TRP HB3 H N N 373 +TRP HD1 H N N 374 +TRP HE1 H N N 375 +TRP HE3 H N N 376 +TRP HZ2 H N N 377 +TRP HZ3 H N N 378 +TRP HH2 H N N 379 +TRP HXT H N N 380 +TYR N N N N 381 +TYR CA C N S 382 +TYR C C N N 383 +TYR O O N N 384 +TYR CB C N N 385 +TYR CG C Y N 386 +TYR CD1 C Y N 387 +TYR CD2 C Y N 388 +TYR CE1 C Y N 389 +TYR CE2 C Y N 390 +TYR CZ C Y N 391 +TYR OH O N N 392 +TYR OXT O N N 393 +TYR H H N N 394 +TYR H2 H N N 395 +TYR HA H N N 396 +TYR HB2 H N N 397 +TYR HB3 H N N 398 +TYR HD1 H N N 399 +TYR HD2 H N N 400 +TYR HE1 H N N 401 +TYR HE2 H N N 402 +TYR HH H N N 403 +TYR HXT H N N 404 +VAL N N N N 405 +VAL CA C N S 406 +VAL C C N N 407 +VAL O O N N 408 +VAL CB C N N 409 +VAL CG1 C N N 410 +VAL CG2 C N N 411 +VAL OXT O N N 412 +VAL H H N N 413 +VAL H2 H N N 414 +VAL HA H N N 415 +VAL HB H N N 416 +VAL HG11 H N N 417 +VAL HG12 H N N 418 +VAL HG13 H N N 419 +VAL HG21 H N N 420 +VAL HG22 H N N 421 +VAL HG23 H N N 422 +VAL HXT H N N 423 +# +loop_ +_chem_comp_bond.comp_id +_chem_comp_bond.atom_id_1 +_chem_comp_bond.atom_id_2 +_chem_comp_bond.value_order +_chem_comp_bond.pdbx_aromatic_flag +_chem_comp_bond.pdbx_stereo_config +_chem_comp_bond.pdbx_ordinal +ALA N CA sing N N 1 +ALA N H sing N N 2 +ALA N H2 sing N N 3 +ALA CA C sing N N 4 +ALA CA CB sing N N 5 +ALA CA HA sing N N 6 +ALA C O doub N N 7 +ALA C OXT sing N N 8 +ALA CB HB1 sing N N 9 +ALA CB HB2 sing N N 10 +ALA CB HB3 sing N N 11 +ALA OXT HXT sing N N 12 +ARG N CA sing N N 13 +ARG N H sing N N 14 +ARG N H2 sing N N 15 +ARG CA C sing N N 16 +ARG CA CB sing N N 17 +ARG CA HA sing N N 18 +ARG C O doub N N 19 +ARG C OXT sing N N 20 +ARG CB CG sing N N 21 +ARG CB HB2 sing N N 22 +ARG CB HB3 sing N N 23 +ARG CG CD sing N N 24 +ARG CG HG2 sing N N 25 +ARG CG HG3 sing N N 26 +ARG CD NE sing N N 27 +ARG CD HD2 sing N N 28 +ARG CD HD3 sing N N 29 +ARG NE CZ sing N N 30 +ARG NE HE sing N N 31 +ARG CZ NH1 sing N N 32 +ARG CZ NH2 doub N N 33 +ARG NH1 HH11 sing N N 34 +ARG NH1 HH12 sing N N 35 +ARG NH2 HH21 sing N N 36 +ARG NH2 HH22 sing N N 37 +ARG OXT HXT sing N N 38 +ASN N CA sing N N 39 +ASN N H sing N N 40 +ASN N H2 sing N N 41 +ASN CA C sing N N 42 +ASN CA CB sing N N 43 +ASN CA HA sing N N 44 +ASN C O doub N N 45 +ASN C OXT sing N N 46 +ASN CB CG sing N N 47 +ASN CB HB2 sing N N 48 +ASN CB HB3 sing N N 49 +ASN CG OD1 doub N N 50 +ASN CG ND2 sing N N 51 +ASN ND2 HD21 sing N N 52 +ASN ND2 HD22 sing N N 53 +ASN OXT HXT sing N N 54 +ASP N CA sing N N 55 +ASP N H sing N N 56 +ASP N H2 sing N N 57 +ASP CA C sing N N 58 +ASP CA CB sing N N 59 +ASP CA HA sing N N 60 +ASP C O doub N N 61 +ASP C OXT sing N N 62 +ASP CB CG sing N N 63 +ASP CB HB2 sing N N 64 +ASP CB HB3 sing N N 65 +ASP CG OD1 doub N N 66 +ASP CG OD2 sing N N 67 +ASP OD2 HD2 sing N N 68 +ASP OXT HXT sing N N 69 +CR2 O3 C3 doub N N 70 +CR2 CA3 C3 sing N N 71 +CR2 CA3 N3 sing N N 72 +CR2 C3 OXT sing N N 73 +CR2 N1 CA1 sing N N 74 +CR2 O2 C2 doub N N 75 +CR2 N3 C2 sing N N 76 +CR2 N3 C1 sing N N 77 +CR2 C2 CA2 sing N N 78 +CR2 CA1 C1 sing N N 79 +CR2 C1 N2 doub N N 80 +CR2 CA2 N2 sing N N 81 +CR2 CA2 CB2 doub N Z 82 +CR2 CB2 CG2 sing N N 83 +CR2 CG2 CD2 doub Y N 84 +CR2 CG2 CD1 sing Y N 85 +CR2 CD2 CE2 sing Y N 86 +CR2 CD1 CE1 doub Y N 87 +CR2 CE2 CZ doub Y N 88 +CR2 CE1 CZ sing Y N 89 +CR2 CZ OH sing N N 90 +CR2 N1 H sing N N 91 +CR2 N1 H2 sing N N 92 +CR2 CA1 HA1 sing N N 93 +CR2 CA1 HA12 sing N N 94 +CR2 CA3 HA31 sing N N 95 +CR2 CA3 HA32 sing N N 96 +CR2 CB2 HB2 sing N N 97 +CR2 CD1 HD1 sing N N 98 +CR2 CD2 HD2 sing N N 99 +CR2 CE1 HE1 sing N N 100 +CR2 CE2 HE2 sing N N 101 +CR2 OH HOH sing N N 102 +CR2 OXT HXT sing N N 103 +CYS N CA sing N N 104 +CYS N H sing N N 105 +CYS N H2 sing N N 106 +CYS CA C sing N N 107 +CYS CA CB sing N N 108 +CYS CA HA sing N N 109 +CYS C O doub N N 110 +CYS C OXT sing N N 111 +CYS CB SG sing N N 112 +CYS CB HB2 sing N N 113 +CYS CB HB3 sing N N 114 +CYS SG HG sing N N 115 +CYS OXT HXT sing N N 116 +GLN N CA sing N N 117 +GLN N H sing N N 118 +GLN N H2 sing N N 119 +GLN CA C sing N N 120 +GLN CA CB sing N N 121 +GLN CA HA sing N N 122 +GLN C O doub N N 123 +GLN C OXT sing N N 124 +GLN CB CG sing N N 125 +GLN CB HB2 sing N N 126 +GLN CB HB3 sing N N 127 +GLN CG CD sing N N 128 +GLN CG HG2 sing N N 129 +GLN CG HG3 sing N N 130 +GLN CD OE1 doub N N 131 +GLN CD NE2 sing N N 132 +GLN NE2 HE21 sing N N 133 +GLN NE2 HE22 sing N N 134 +GLN OXT HXT sing N N 135 +GLU N CA sing N N 136 +GLU N H sing N N 137 +GLU N H2 sing N N 138 +GLU CA C sing N N 139 +GLU CA CB sing N N 140 +GLU CA HA sing N N 141 +GLU C O doub N N 142 +GLU C OXT sing N N 143 +GLU CB CG sing N N 144 +GLU CB HB2 sing N N 145 +GLU CB HB3 sing N N 146 +GLU CG CD sing N N 147 +GLU CG HG2 sing N N 148 +GLU CG HG3 sing N N 149 +GLU CD OE1 doub N N 150 +GLU CD OE2 sing N N 151 +GLU OE2 HE2 sing N N 152 +GLU OXT HXT sing N N 153 +GLY N CA sing N N 154 +GLY N H sing N N 155 +GLY N H2 sing N N 156 +GLY CA C sing N N 157 +GLY CA HA2 sing N N 158 +GLY CA HA3 sing N N 159 +GLY C O doub N N 160 +GLY C OXT sing N N 161 +GLY OXT HXT sing N N 162 +HIS N CA sing N N 163 +HIS N H sing N N 164 +HIS N H2 sing N N 165 +HIS CA C sing N N 166 +HIS CA CB sing N N 167 +HIS CA HA sing N N 168 +HIS C O doub N N 169 +HIS C OXT sing N N 170 +HIS CB CG sing N N 171 +HIS CB HB2 sing N N 172 +HIS CB HB3 sing N N 173 +HIS CG ND1 sing Y N 174 +HIS CG CD2 doub Y N 175 +HIS ND1 CE1 doub Y N 176 +HIS ND1 HD1 sing N N 177 +HIS CD2 NE2 sing Y N 178 +HIS CD2 HD2 sing N N 179 +HIS CE1 NE2 sing Y N 180 +HIS CE1 HE1 sing N N 181 +HIS NE2 HE2 sing N N 182 +HIS OXT HXT sing N N 183 +HOH O H1 sing N N 184 +HOH O H2 sing N N 185 +ILE N CA sing N N 186 +ILE N H sing N N 187 +ILE N H2 sing N N 188 +ILE CA C sing N N 189 +ILE CA CB sing N N 190 +ILE CA HA sing N N 191 +ILE C O doub N N 192 +ILE C OXT sing N N 193 +ILE CB CG1 sing N N 194 +ILE CB CG2 sing N N 195 +ILE CB HB sing N N 196 +ILE CG1 CD1 sing N N 197 +ILE CG1 HG12 sing N N 198 +ILE CG1 HG13 sing N N 199 +ILE CG2 HG21 sing N N 200 +ILE CG2 HG22 sing N N 201 +ILE CG2 HG23 sing N N 202 +ILE CD1 HD11 sing N N 203 +ILE CD1 HD12 sing N N 204 +ILE CD1 HD13 sing N N 205 +ILE OXT HXT sing N N 206 +LEU N CA sing N N 207 +LEU N H sing N N 208 +LEU N H2 sing N N 209 +LEU CA C sing N N 210 +LEU CA CB sing N N 211 +LEU CA HA sing N N 212 +LEU C O doub N N 213 +LEU C OXT sing N N 214 +LEU CB CG sing N N 215 +LEU CB HB2 sing N N 216 +LEU CB HB3 sing N N 217 +LEU CG CD1 sing N N 218 +LEU CG CD2 sing N N 219 +LEU CG HG sing N N 220 +LEU CD1 HD11 sing N N 221 +LEU CD1 HD12 sing N N 222 +LEU CD1 HD13 sing N N 223 +LEU CD2 HD21 sing N N 224 +LEU CD2 HD22 sing N N 225 +LEU CD2 HD23 sing N N 226 +LEU OXT HXT sing N N 227 +LYS N CA sing N N 228 +LYS N H sing N N 229 +LYS N H2 sing N N 230 +LYS CA C sing N N 231 +LYS CA CB sing N N 232 +LYS CA HA sing N N 233 +LYS C O doub N N 234 +LYS C OXT sing N N 235 +LYS CB CG sing N N 236 +LYS CB HB2 sing N N 237 +LYS CB HB3 sing N N 238 +LYS CG CD sing N N 239 +LYS CG HG2 sing N N 240 +LYS CG HG3 sing N N 241 +LYS CD CE sing N N 242 +LYS CD HD2 sing N N 243 +LYS CD HD3 sing N N 244 +LYS CE NZ sing N N 245 +LYS CE HE2 sing N N 246 +LYS CE HE3 sing N N 247 +LYS NZ HZ1 sing N N 248 +LYS NZ HZ2 sing N N 249 +LYS NZ HZ3 sing N N 250 +LYS OXT HXT sing N N 251 +MET N CA sing N N 252 +MET N H sing N N 253 +MET N H2 sing N N 254 +MET CA C sing N N 255 +MET CA CB sing N N 256 +MET CA HA sing N N 257 +MET C O doub N N 258 +MET C OXT sing N N 259 +MET CB CG sing N N 260 +MET CB HB2 sing N N 261 +MET CB HB3 sing N N 262 +MET CG SD sing N N 263 +MET CG HG2 sing N N 264 +MET CG HG3 sing N N 265 +MET SD CE sing N N 266 +MET CE HE1 sing N N 267 +MET CE HE2 sing N N 268 +MET CE HE3 sing N N 269 +MET OXT HXT sing N N 270 +PHE N CA sing N N 271 +PHE N H sing N N 272 +PHE N H2 sing N N 273 +PHE CA C sing N N 274 +PHE CA CB sing N N 275 +PHE CA HA sing N N 276 +PHE C O doub N N 277 +PHE C OXT sing N N 278 +PHE CB CG sing N N 279 +PHE CB HB2 sing N N 280 +PHE CB HB3 sing N N 281 +PHE CG CD1 doub Y N 282 +PHE CG CD2 sing Y N 283 +PHE CD1 CE1 sing Y N 284 +PHE CD1 HD1 sing N N 285 +PHE CD2 CE2 doub Y N 286 +PHE CD2 HD2 sing N N 287 +PHE CE1 CZ doub Y N 288 +PHE CE1 HE1 sing N N 289 +PHE CE2 CZ sing Y N 290 +PHE CE2 HE2 sing N N 291 +PHE CZ HZ sing N N 292 +PHE OXT HXT sing N N 293 +PRO N CA sing N N 294 +PRO N CD sing N N 295 +PRO N H sing N N 296 +PRO CA C sing N N 297 +PRO CA CB sing N N 298 +PRO CA HA sing N N 299 +PRO C O doub N N 300 +PRO C OXT sing N N 301 +PRO CB CG sing N N 302 +PRO CB HB2 sing N N 303 +PRO CB HB3 sing N N 304 +PRO CG CD sing N N 305 +PRO CG HG2 sing N N 306 +PRO CG HG3 sing N N 307 +PRO CD HD2 sing N N 308 +PRO CD HD3 sing N N 309 +PRO OXT HXT sing N N 310 +SER N CA sing N N 311 +SER N H sing N N 312 +SER N H2 sing N N 313 +SER CA C sing N N 314 +SER CA CB sing N N 315 +SER CA HA sing N N 316 +SER C O doub N N 317 +SER C OXT sing N N 318 +SER CB OG sing N N 319 +SER CB HB2 sing N N 320 +SER CB HB3 sing N N 321 +SER OG HG sing N N 322 +SER OXT HXT sing N N 323 +THR N CA sing N N 324 +THR N H sing N N 325 +THR N H2 sing N N 326 +THR CA C sing N N 327 +THR CA CB sing N N 328 +THR CA HA sing N N 329 +THR C O doub N N 330 +THR C OXT sing N N 331 +THR CB OG1 sing N N 332 +THR CB CG2 sing N N 333 +THR CB HB sing N N 334 +THR OG1 HG1 sing N N 335 +THR CG2 HG21 sing N N 336 +THR CG2 HG22 sing N N 337 +THR CG2 HG23 sing N N 338 +THR OXT HXT sing N N 339 +TRP N CA sing N N 340 +TRP N H sing N N 341 +TRP N H2 sing N N 342 +TRP CA C sing N N 343 +TRP CA CB sing N N 344 +TRP CA HA sing N N 345 +TRP C O doub N N 346 +TRP C OXT sing N N 347 +TRP CB CG sing N N 348 +TRP CB HB2 sing N N 349 +TRP CB HB3 sing N N 350 +TRP CG CD1 doub Y N 351 +TRP CG CD2 sing Y N 352 +TRP CD1 NE1 sing Y N 353 +TRP CD1 HD1 sing N N 354 +TRP CD2 CE2 doub Y N 355 +TRP CD2 CE3 sing Y N 356 +TRP NE1 CE2 sing Y N 357 +TRP NE1 HE1 sing N N 358 +TRP CE2 CZ2 sing Y N 359 +TRP CE3 CZ3 doub Y N 360 +TRP CE3 HE3 sing N N 361 +TRP CZ2 CH2 doub Y N 362 +TRP CZ2 HZ2 sing N N 363 +TRP CZ3 CH2 sing Y N 364 +TRP CZ3 HZ3 sing N N 365 +TRP CH2 HH2 sing N N 366 +TRP OXT HXT sing N N 367 +TYR N CA sing N N 368 +TYR N H sing N N 369 +TYR N H2 sing N N 370 +TYR CA C sing N N 371 +TYR CA CB sing N N 372 +TYR CA HA sing N N 373 +TYR C O doub N N 374 +TYR C OXT sing N N 375 +TYR CB CG sing N N 376 +TYR CB HB2 sing N N 377 +TYR CB HB3 sing N N 378 +TYR CG CD1 doub Y N 379 +TYR CG CD2 sing Y N 380 +TYR CD1 CE1 sing Y N 381 +TYR CD1 HD1 sing N N 382 +TYR CD2 CE2 doub Y N 383 +TYR CD2 HD2 sing N N 384 +TYR CE1 CZ doub Y N 385 +TYR CE1 HE1 sing N N 386 +TYR CE2 CZ sing Y N 387 +TYR CE2 HE2 sing N N 388 +TYR CZ OH sing N N 389 +TYR OH HH sing N N 390 +TYR OXT HXT sing N N 391 +VAL N CA sing N N 392 +VAL N H sing N N 393 +VAL N H2 sing N N 394 +VAL CA C sing N N 395 +VAL CA CB sing N N 396 +VAL CA HA sing N N 397 +VAL C O doub N N 398 +VAL C OXT sing N N 399 +VAL CB CG1 sing N N 400 +VAL CB CG2 sing N N 401 +VAL CB HB sing N N 402 +VAL CG1 HG11 sing N N 403 +VAL CG1 HG12 sing N N 404 +VAL CG1 HG13 sing N N 405 +VAL CG2 HG21 sing N N 406 +VAL CG2 HG22 sing N N 407 +VAL CG2 HG23 sing N N 408 +VAL OXT HXT sing N N 409 +# +_atom_sites.entry_id 4BDU +_atom_sites.fract_transf_matrix[1][1] 0.008904 +_atom_sites.fract_transf_matrix[1][2] 0.005141 +_atom_sites.fract_transf_matrix[1][3] 0.000000 +_atom_sites.fract_transf_matrix[2][1] 0.000000 +_atom_sites.fract_transf_matrix[2][2] 0.010281 +_atom_sites.fract_transf_matrix[2][3] 0.000000 +_atom_sites.fract_transf_matrix[3][1] 0.000000 +_atom_sites.fract_transf_matrix[3][2] 0.000000 +_atom_sites.fract_transf_matrix[3][3] 0.003410 +_atom_sites.fract_transf_vector[1] 0.00000 +_atom_sites.fract_transf_vector[2] 0.00000 +_atom_sites.fract_transf_vector[3] 0.00000 +# +loop_ +_atom_type.symbol +C +N +O +S +# +loop_ +_atom_site.group_PDB +_atom_site.id +_atom_site.type_symbol +_atom_site.label_atom_id +_atom_site.label_alt_id +_atom_site.label_comp_id +_atom_site.label_asym_id +_atom_site.label_entity_id +_atom_site.label_seq_id +_atom_site.pdbx_PDB_ins_code +_atom_site.Cartn_x +_atom_site.Cartn_y +_atom_site.Cartn_z +_atom_site.occupancy +_atom_site.B_iso_or_equiv +_atom_site.pdbx_formal_charge +_atom_site.auth_seq_id +_atom_site.auth_comp_id +_atom_site.auth_asym_id +_atom_site.auth_atom_id +_atom_site.pdbx_PDB_model_num +ATOM 1 N N . SER A 1 5 ? 21.854 80.059 105.006 1.00 92.68 ? 2 SER A N 1 +ATOM 2 C CA . SER A 1 5 ? 22.503 81.112 105.789 1.00 149.92 ? 2 SER A CA 1 +ATOM 3 C C . SER A 1 5 ? 22.331 80.944 107.306 1.00 147.56 ? 2 SER A C 1 +ATOM 4 O O . SER A 1 5 ? 21.301 80.460 107.782 1.00 108.25 ? 2 SER A O 1 +ATOM 5 C CB . SER A 1 5 ? 22.002 82.497 105.352 1.00 147.35 ? 2 SER A CB 1 +ATOM 6 O OG . SER A 1 5 ? 20.918 82.945 106.150 1.00 142.43 ? 2 SER A OG 1 +ATOM 7 N N . LYS A 1 6 ? 23.349 81.356 108.059 1.00 151.74 ? 3 LYS A N 1 +ATOM 8 C CA . LYS A 1 6 ? 23.297 81.309 109.519 1.00 148.15 ? 3 LYS A CA 1 +ATOM 9 C C . LYS A 1 6 ? 22.492 82.496 110.047 1.00 146.08 ? 3 LYS A C 1 +ATOM 10 O O . LYS A 1 6 ? 21.951 82.457 111.153 1.00 136.60 ? 3 LYS A O 1 +ATOM 11 C CB . LYS A 1 6 ? 24.708 81.309 110.131 1.00 170.15 ? 3 LYS A CB 1 +ATOM 12 C CG . LYS A 1 6 ? 25.759 80.483 109.371 1.00 189.86 ? 3 LYS A CG 1 +ATOM 13 C CD . LYS A 1 6 ? 25.328 79.033 109.149 1.00 197.45 ? 3 LYS A CD 1 +ATOM 14 C CE . LYS A 1 6 ? 25.462 78.630 107.679 1.00 174.32 ? 3 LYS A CE 1 +ATOM 15 N NZ . LYS A 1 6 ? 24.711 77.381 107.358 1.00 150.33 ? 3 LYS A NZ 1 +ATOM 16 N N . GLY A 1 7 ? 22.419 83.550 109.241 1.00 144.10 ? 4 GLY A N 1 +ATOM 17 C CA . GLY A 1 7 ? 21.643 84.724 109.588 1.00 134.21 ? 4 GLY A CA 1 +ATOM 18 C C . GLY A 1 7 ? 20.159 84.429 109.644 1.00 127.00 ? 4 GLY A C 1 +ATOM 19 O O . GLY A 1 7 ? 19.438 85.004 110.461 1.00 101.93 ? 4 GLY A O 1 +ATOM 20 N N . GLU A 1 8 ? 19.714 83.520 108.780 1.00 105.13 ? 5 GLU A N 1 +ATOM 21 C CA . GLU A 1 8 ? 18.300 83.183 108.653 1.00 94.39 ? 5 GLU A CA 1 +ATOM 22 C C . GLU A 1 8 ? 17.669 82.776 109.990 1.00 99.31 ? 5 GLU A C 1 +ATOM 23 O O . GLU A 1 8 ? 16.489 83.032 110.229 1.00 120.55 ? 5 GLU A O 1 +ATOM 24 C CB . GLU A 1 8 ? 18.115 82.088 107.618 1.00 113.32 ? 5 GLU A CB 1 +ATOM 25 C CG . GLU A 1 8 ? 16.647 81.701 107.319 1.00 160.01 ? 5 GLU A CG 1 +ATOM 26 C CD . GLU A 1 8 ? 16.002 82.560 106.228 1.00 181.31 ? 5 GLU A CD 1 +ATOM 27 O OE1 . GLU A 1 8 ? 16.554 82.641 105.108 1.00 193.32 ? 5 GLU A OE1 1 +ATOM 28 O OE2 . GLU A 1 8 ? 14.931 83.139 106.501 1.00 156.68 ? 5 GLU A OE2 1 +ATOM 29 N N . GLU A 1 9 ? 18.461 82.167 110.869 1.00 110.35 ? 6 GLU A N 1 +ATOM 30 C CA . GLU A 1 9 ? 17.950 81.703 112.160 1.00 100.21 ? 6 GLU A CA 1 +ATOM 31 C C . GLU A 1 9 ? 17.787 82.814 113.193 1.00 101.65 ? 6 GLU A C 1 +ATOM 32 O O . GLU A 1 9 ? 17.357 82.556 114.319 1.00 119.07 ? 6 GLU A O 1 +ATOM 33 C CB . GLU A 1 9 ? 18.848 80.607 112.740 1.00 147.38 ? 6 GLU A CB 1 +ATOM 34 C CG . GLU A 1 9 ? 18.844 79.307 111.957 1.00 172.98 ? 6 GLU A CG 1 +ATOM 35 C CD . GLU A 1 9 ? 19.801 78.281 112.532 1.00 184.61 ? 6 GLU A CD 1 +ATOM 36 O OE1 . GLU A 1 9 ? 20.599 78.652 113.421 1.00 169.61 ? 6 GLU A OE1 1 +ATOM 37 O OE2 . GLU A 1 9 ? 19.754 77.111 112.092 1.00 197.75 ? 6 GLU A OE2 1 +ATOM 38 N N . LEU A 1 10 ? 18.151 84.038 112.822 1.00 90.50 ? 7 LEU A N 1 +ATOM 39 C CA . LEU A 1 10 ? 17.956 85.189 113.699 1.00 94.58 ? 7 LEU A CA 1 +ATOM 40 C C . LEU A 1 10 ? 16.597 85.840 113.442 1.00 112.03 ? 7 LEU A C 1 +ATOM 41 O O . LEU A 1 10 ? 16.084 86.595 114.277 1.00 84.95 ? 7 LEU A O 1 +ATOM 42 C CB . LEU A 1 10 ? 19.091 86.204 113.514 1.00 90.57 ? 7 LEU A CB 1 +ATOM 43 C CG . LEU A 1 10 ? 20.443 85.804 114.117 1.00 111.98 ? 7 LEU A CG 1 +ATOM 44 C CD1 . LEU A 1 10 ? 21.625 86.355 113.327 1.00 96.34 ? 7 LEU A CD1 1 +ATOM 45 C CD2 . LEU A 1 10 ? 20.526 86.240 115.576 1.00 112.43 ? 7 LEU A CD2 1 +ATOM 46 N N . PHE A 1 11 ? 16.000 85.506 112.300 1.00 113.24 ? 8 PHE A N 1 +ATOM 47 C CA . PHE A 1 11 ? 14.825 86.228 111.818 1.00 102.00 ? 8 PHE A CA 1 +ATOM 48 C C . PHE A 1 11 ? 13.485 85.494 111.860 1.00 107.33 ? 8 PHE A C 1 +ATOM 49 O O . PHE A 1 11 ? 12.462 86.041 111.433 1.00 109.88 ? 8 PHE A O 1 +ATOM 50 C CB . PHE A 1 11 ? 15.111 86.852 110.452 1.00 96.36 ? 8 PHE A CB 1 +ATOM 51 C CG . PHE A 1 11 ? 16.063 87.997 110.536 1.00 109.39 ? 8 PHE A CG 1 +ATOM 52 C CD1 . PHE A 1 11 ? 15.609 89.253 110.885 1.00 94.41 ? 8 PHE A CD1 1 +ATOM 53 C CD2 . PHE A 1 11 ? 17.417 87.810 110.336 1.00 98.41 ? 8 PHE A CD2 1 +ATOM 54 C CE1 . PHE A 1 11 ? 16.474 90.300 110.996 1.00 100.52 ? 8 PHE A CE1 1 +ATOM 55 C CE2 . PHE A 1 11 ? 18.290 88.866 110.445 1.00 104.24 ? 8 PHE A CE2 1 +ATOM 56 C CZ . PHE A 1 11 ? 17.817 90.111 110.776 1.00 94.62 ? 8 PHE A CZ 1 +ATOM 57 N N . THR A 1 12 ? 13.497 84.272 112.392 1.00 95.77 ? 9 THR A N 1 +ATOM 58 C CA . THR A 1 12 ? 12.271 83.622 112.849 1.00 99.86 ? 9 THR A CA 1 +ATOM 59 C C . THR A 1 12 ? 11.771 84.390 114.080 1.00 113.45 ? 9 THR A C 1 +ATOM 60 O O . THR A 1 12 ? 12.574 84.910 114.859 1.00 115.81 ? 9 THR A O 1 +ATOM 61 C CB . THR A 1 12 ? 12.508 82.132 113.200 1.00 52.45 ? 9 THR A CB 1 +ATOM 62 O OG1 . THR A 1 12 ? 13.192 82.027 114.453 1.00 101.02 ? 9 THR A OG1 1 +ATOM 63 C CG2 . THR A 1 12 ? 13.357 81.468 112.146 1.00 72.12 ? 9 THR A CG2 1 +ATOM 64 N N . GLY A 1 13 ? 10.454 84.496 114.242 1.00 88.45 ? 10 GLY A N 1 +ATOM 65 C CA . GLY A 1 13 ? 9.888 85.234 115.364 1.00 141.41 ? 10 GLY A CA 1 +ATOM 66 C C . GLY A 1 13 ? 10.171 86.735 115.415 1.00 94.94 ? 10 GLY A C 1 +ATOM 67 O O . GLY A 1 13 ? 11.211 87.202 114.948 1.00 92.25 ? 10 GLY A O 1 +ATOM 68 N N . VAL A 1 14 ? 9.236 87.481 116.005 1.00 80.80 ? 11 VAL A N 1 +ATOM 69 C CA . VAL A 1 14 ? 9.285 88.947 116.119 1.00 81.02 ? 11 VAL A CA 1 +ATOM 70 C C . VAL A 1 14 ? 10.601 89.519 116.713 1.00 87.55 ? 11 VAL A C 1 +ATOM 71 O O . VAL A 1 14 ? 10.958 89.226 117.858 1.00 93.04 ? 11 VAL A O 1 +ATOM 72 C CB . VAL A 1 14 ? 8.047 89.458 116.928 1.00 69.05 ? 11 VAL A CB 1 +ATOM 73 C CG1 . VAL A 1 14 ? 8.128 90.932 117.159 1.00 97.18 ? 11 VAL A CG1 1 +ATOM 74 C CG2 . VAL A 1 14 ? 6.747 89.106 116.212 1.00 71.42 ? 11 VAL A CG2 1 +ATOM 75 N N . VAL A 1 15 ? 11.315 90.327 115.925 1.00 74.10 ? 12 VAL A N 1 +ATOM 76 C CA . VAL A 1 15 ? 12.572 90.956 116.361 1.00 93.62 ? 12 VAL A CA 1 +ATOM 77 C C . VAL A 1 15 ? 12.405 92.437 116.692 1.00 99.23 ? 12 VAL A C 1 +ATOM 78 O O . VAL A 1 15 ? 11.766 93.172 115.937 1.00 85.55 ? 12 VAL A O 1 +ATOM 79 C CB . VAL A 1 15 ? 13.645 90.892 115.270 1.00 75.25 ? 12 VAL A CB 1 +ATOM 80 C CG1 . VAL A 1 15 ? 14.957 91.473 115.789 1.00 84.92 ? 12 VAL A CG1 1 +ATOM 81 C CG2 . VAL A 1 15 ? 13.828 89.469 114.786 1.00 60.83 ? 12 VAL A CG2 1 +ATOM 82 N N . PRO A 1 16 ? 12.983 92.886 117.818 1.00 79.88 ? 13 PRO A N 1 +ATOM 83 C CA . PRO A 1 16 ? 12.912 94.319 118.130 1.00 97.89 ? 13 PRO A CA 1 +ATOM 84 C C . PRO A 1 16 ? 13.842 95.201 117.266 1.00 86.80 ? 13 PRO A C 1 +ATOM 85 O O . PRO A 1 16 ? 15.003 94.850 117.018 1.00 91.49 ? 13 PRO A O 1 +ATOM 86 C CB . PRO A 1 16 ? 13.278 94.374 119.622 1.00 59.98 ? 13 PRO A CB 1 +ATOM 87 C CG . PRO A 1 16 ? 14.040 93.132 119.881 1.00 90.88 ? 13 PRO A CG 1 +ATOM 88 C CD . PRO A 1 16 ? 13.498 92.093 118.948 1.00 86.51 ? 13 PRO A CD 1 +ATOM 89 N N . ILE A 1 17 ? 13.300 96.330 116.801 1.00 94.89 ? 14 ILE A N 1 +ATOM 90 C CA . ILE A 1 17 ? 14.030 97.278 115.954 1.00 86.98 ? 14 ILE A CA 1 +ATOM 91 C C . ILE A 1 17 ? 14.169 98.641 116.615 1.00 86.60 ? 14 ILE A C 1 +ATOM 92 O O . ILE A 1 17 ? 13.247 99.141 117.276 1.00 79.24 ? 14 ILE A O 1 +ATOM 93 C CB . ILE A 1 17 ? 13.341 97.510 114.590 1.00 68.82 ? 14 ILE A CB 1 +ATOM 94 C CG1 . ILE A 1 17 ? 12.953 96.192 113.942 1.00 83.94 ? 14 ILE A CG1 1 +ATOM 95 C CG2 . ILE A 1 17 ? 14.243 98.293 113.646 1.00 70.04 ? 14 ILE A CG2 1 +ATOM 96 C CD1 . ILE A 1 17 ? 12.207 96.380 112.645 1.00 110.72 ? 14 ILE A CD1 1 +ATOM 97 N N . LEU A 1 18 ? 15.329 99.243 116.391 1.00 76.43 ? 15 LEU A N 1 +ATOM 98 C CA . LEU A 1 18 ? 15.676 100.533 116.950 1.00 98.83 ? 15 LEU A CA 1 +ATOM 99 C C . LEU A 1 18 ? 16.425 101.320 115.867 1.00 95.93 ? 15 LEU A C 1 +ATOM 100 O O . LEU A 1 18 ? 17.356 100.800 115.254 1.00 75.06 ? 15 LEU A O 1 +ATOM 101 C CB . LEU A 1 18 ? 16.541 100.301 118.188 1.00 70.49 ? 15 LEU A CB 1 +ATOM 102 C CG . LEU A 1 18 ? 17.130 101.455 118.980 1.00 106.54 ? 15 LEU A CG 1 +ATOM 103 C CD1 . LEU A 1 18 ? 16.010 102.297 119.567 1.00 117.39 ? 15 LEU A CD1 1 +ATOM 104 C CD2 . LEU A 1 18 ? 18.056 100.907 120.071 1.00 115.00 ? 15 LEU A CD2 1 +ATOM 105 N N . VAL A 1 19 ? 16.003 102.558 115.610 1.00 85.89 ? 16 VAL A N 1 +ATOM 106 C CA . VAL A 1 19 ? 16.589 103.370 114.537 1.00 82.47 ? 16 VAL A CA 1 +ATOM 107 C C . VAL A 1 19 ? 17.080 104.761 114.991 1.00 86.24 ? 16 VAL A C 1 +ATOM 108 O O . VAL A 1 19 ? 16.344 105.501 115.655 1.00 83.90 ? 16 VAL A O 1 +ATOM 109 C CB . VAL A 1 19 ? 15.583 103.541 113.379 1.00 75.61 ? 16 VAL A CB 1 +ATOM 110 C CG1 . VAL A 1 19 ? 16.180 104.358 112.259 1.00 75.38 ? 16 VAL A CG1 1 +ATOM 111 C CG2 . VAL A 1 19 ? 15.146 102.192 112.863 1.00 87.24 ? 16 VAL A CG2 1 +ATOM 112 N N . GLU A 1 20 ? 18.323 105.096 114.615 1.00 78.07 ? 17 GLU A N 1 +ATOM 113 C CA . GLU A 1 20 ? 18.931 106.423 114.844 1.00 72.95 ? 17 GLU A CA 1 +ATOM 114 C C . GLU A 1 20 ? 19.316 107.173 113.547 1.00 96.55 ? 17 GLU A C 1 +ATOM 115 O O . GLU A 1 20 ? 20.094 106.662 112.730 1.00 75.13 ? 17 GLU A O 1 +ATOM 116 C CB . GLU A 1 20 ? 20.188 106.315 115.731 1.00 100.08 ? 17 GLU A CB 1 +ATOM 117 C CG . GLU A 1 20 ? 19.969 105.811 117.159 1.00 113.26 ? 17 GLU A CG 1 +ATOM 118 C CD . GLU A 1 20 ? 18.977 106.654 117.946 1.00 133.33 ? 17 GLU A CD 1 +ATOM 119 O OE1 . GLU A 1 20 ? 18.710 107.809 117.538 1.00 135.54 ? 17 GLU A OE1 1 +ATOM 120 O OE2 . GLU A 1 20 ? 18.462 106.155 118.974 1.00 131.01 ? 17 GLU A OE2 1 +ATOM 121 N N . LEU A 1 21 ? 18.797 108.393 113.378 1.00 87.99 ? 18 LEU A N 1 +ATOM 122 C CA . LEU A 1 21 ? 19.148 109.239 112.229 1.00 90.23 ? 18 LEU A CA 1 +ATOM 123 C C . LEU A 1 21 ? 19.694 110.635 112.613 1.00 88.13 ? 18 LEU A C 1 +ATOM 124 O O . LEU A 1 21 ? 19.141 111.302 113.493 1.00 90.62 ? 18 LEU A O 1 +ATOM 125 C CB . LEU A 1 21 ? 17.938 109.387 111.298 1.00 96.54 ? 18 LEU A CB 1 +ATOM 126 C CG . LEU A 1 21 ? 18.127 110.305 110.085 1.00 82.46 ? 18 LEU A CG 1 +ATOM 127 C CD1 . LEU A 1 21 ? 19.192 109.781 109.169 1.00 128.46 ? 18 LEU A CD1 1 +ATOM 128 C CD2 . LEU A 1 21 ? 16.833 110.485 109.317 1.00 106.42 ? 18 LEU A CD2 1 +ATOM 129 N N . ASP A 1 22 ? 20.787 111.050 111.962 1.00 88.80 ? 19 ASP A N 1 +ATOM 130 C CA . ASP A 1 22 ? 21.285 112.441 112.005 1.00 108.07 ? 19 ASP A CA 1 +ATOM 131 C C . ASP A 1 22 ? 21.254 113.080 110.611 1.00 101.00 ? 19 ASP A C 1 +ATOM 132 O O . ASP A 1 22 ? 22.034 112.714 109.727 1.00 104.01 ? 19 ASP A O 1 +ATOM 133 C CB . ASP A 1 22 ? 22.714 112.527 112.569 1.00 95.84 ? 19 ASP A CB 1 +ATOM 134 C CG . ASP A 1 22 ? 22.765 112.410 114.089 1.00 126.47 ? 19 ASP A CG 1 +ATOM 135 O OD1 . ASP A 1 22 ? 21.791 112.817 114.762 1.00 138.81 ? 19 ASP A OD1 1 +ATOM 136 O OD2 . ASP A 1 22 ? 23.789 111.914 114.611 1.00 155.17 ? 19 ASP A OD2 1 +ATOM 137 N N . GLY A 1 23 ? 20.356 114.043 110.422 1.00 105.54 ? 20 GLY A N 1 +ATOM 138 C CA . GLY A 1 23 ? 20.163 114.665 109.124 1.00 65.01 ? 20 GLY A CA 1 +ATOM 139 C C . GLY A 1 23 ? 20.639 116.102 109.014 1.00 105.13 ? 20 GLY A C 1 +ATOM 140 O O . GLY A 1 23 ? 20.730 116.829 110.005 1.00 102.21 ? 20 GLY A O 1 +ATOM 141 N N . ASP A 1 24 ? 20.932 116.500 107.778 1.00 117.53 ? 21 ASP A N 1 +ATOM 142 C CA . ASP A 1 24 ? 21.421 117.832 107.442 1.00 88.01 ? 21 ASP A CA 1 +ATOM 143 C C . ASP A 1 24 ? 20.963 118.189 106.013 1.00 97.14 ? 21 ASP A C 1 +ATOM 144 O O . ASP A 1 24 ? 21.610 117.809 105.036 1.00 106.13 ? 21 ASP A O 1 +ATOM 145 C CB . ASP A 1 24 ? 22.954 117.852 107.543 1.00 150.24 ? 21 ASP A CB 1 +ATOM 146 C CG . ASP A 1 24 ? 23.541 119.263 107.538 1.00 156.71 ? 21 ASP A CG 1 +ATOM 147 O OD1 . ASP A 1 24 ? 22.841 120.218 107.131 1.00 139.29 ? 21 ASP A OD1 1 +ATOM 148 O OD2 . ASP A 1 24 ? 24.720 119.409 107.936 1.00 109.94 ? 21 ASP A OD2 1 +ATOM 149 N N . VAL A 1 25 ? 19.845 118.908 105.894 1.00 94.00 ? 22 VAL A N 1 +ATOM 150 C CA . VAL A 1 25 ? 19.281 119.263 104.583 1.00 94.88 ? 22 VAL A CA 1 +ATOM 151 C C . VAL A 1 25 ? 19.183 120.776 104.343 1.00 96.58 ? 22 VAL A C 1 +ATOM 152 O O . VAL A 1 25 ? 18.364 121.469 104.957 1.00 83.45 ? 22 VAL A O 1 +ATOM 153 C CB . VAL A 1 25 ? 17.905 118.593 104.355 1.00 85.83 ? 22 VAL A CB 1 +ATOM 154 C CG1 . VAL A 1 25 ? 17.161 119.232 103.177 1.00 90.83 ? 22 VAL A CG1 1 +ATOM 155 C CG2 . VAL A 1 25 ? 18.083 117.107 104.136 1.00 96.50 ? 22 VAL A CG2 1 +ATOM 156 N N . ASN A 1 26 ? 20.018 121.264 103.425 1.00 99.82 ? 23 ASN A N 1 +ATOM 157 C CA . ASN A 1 26 ? 20.180 122.696 103.164 1.00 79.07 ? 23 ASN A CA 1 +ATOM 158 C C . ASN A 1 26 ? 20.466 123.431 104.478 1.00 112.37 ? 23 ASN A C 1 +ATOM 159 O O . ASN A 1 26 ? 19.787 124.395 104.854 1.00 84.12 ? 23 ASN A O 1 +ATOM 160 C CB . ASN A 1 26 ? 18.971 123.279 102.413 1.00 82.70 ? 23 ASN A CB 1 +ATOM 161 C CG . ASN A 1 26 ? 18.977 122.950 100.908 1.00 121.35 ? 23 ASN A CG 1 +ATOM 162 O OD1 . ASN A 1 26 ? 19.806 122.175 100.416 1.00 98.14 ? 23 ASN A OD1 1 +ATOM 163 N ND2 . ASN A 1 26 ? 18.038 123.545 100.174 1.00 91.90 ? 23 ASN A ND2 1 +ATOM 164 N N . GLY A 1 27 ? 21.473 122.924 105.184 1.00 101.57 ? 24 GLY A N 1 +ATOM 165 C CA . GLY A 1 27 ? 21.872 123.456 106.472 1.00 89.15 ? 24 GLY A CA 1 +ATOM 166 C C . GLY A 1 27 ? 20.865 123.340 107.604 1.00 98.09 ? 24 GLY A C 1 +ATOM 167 O O . GLY A 1 27 ? 21.135 123.836 108.700 1.00 92.62 ? 24 GLY A O 1 +ATOM 168 N N . HIS A 1 28 ? 19.705 122.730 107.345 1.00 98.31 ? 25 HIS A N 1 +ATOM 169 C CA . HIS A 1 28 ? 18.796 122.319 108.417 1.00 107.40 ? 25 HIS A CA 1 +ATOM 170 C C . HIS A 1 28 ? 19.248 120.994 108.990 1.00 111.37 ? 25 HIS A C 1 +ATOM 171 O O . HIS A 1 28 ? 19.206 119.962 108.313 1.00 80.40 ? 25 HIS A O 1 +ATOM 172 C CB . HIS A 1 28 ? 17.375 122.111 107.922 1.00 76.20 ? 25 HIS A CB 1 +ATOM 173 C CG . HIS A 1 28 ? 16.674 123.366 107.525 1.00 133.05 ? 25 HIS A CG 1 +ATOM 174 N ND1 . HIS A 1 28 ? 16.814 123.927 106.274 1.00 113.08 ? 25 HIS A ND1 1 +ATOM 175 C CD2 . HIS A 1 28 ? 15.804 124.154 108.198 1.00 115.95 ? 25 HIS A CD2 1 +ATOM 176 C CE1 . HIS A 1 28 ? 16.065 125.011 106.197 1.00 84.76 ? 25 HIS A CE1 1 +ATOM 177 N NE2 . HIS A 1 28 ? 15.444 125.173 107.352 1.00 125.90 ? 25 HIS A NE2 1 +ATOM 178 N N . LYS A 1 29 ? 19.674 121.025 110.243 1.00 93.23 ? 26 LYS A N 1 +ATOM 179 C CA . LYS A 1 29 ? 20.046 119.813 110.932 1.00 91.59 ? 26 LYS A CA 1 +ATOM 180 C C . LYS A 1 29 ? 18.787 119.281 111.608 1.00 107.55 ? 26 LYS A C 1 +ATOM 181 O O . LYS A 1 29 ? 17.799 120.013 111.743 1.00 94.74 ? 26 LYS A O 1 +ATOM 182 C CB . LYS A 1 29 ? 21.160 120.107 111.936 1.00 93.85 ? 26 LYS A CB 1 +ATOM 183 C CG . LYS A 1 29 ? 22.414 120.706 111.299 1.00 81.75 ? 26 LYS A CG 1 +ATOM 184 C CD . LYS A 1 29 ? 23.459 121.078 112.343 1.00 115.55 ? 26 LYS A CD 1 +ATOM 185 C CE . LYS A 1 29 ? 24.799 121.427 111.711 1.00 105.64 ? 26 LYS A CE 1 +ATOM 186 N NZ . LYS A 1 29 ? 25.463 120.256 111.068 1.00 129.39 ? 26 LYS A NZ 1 +ATOM 187 N N . PHE A 1 30 ? 18.814 118.002 111.983 1.00 86.78 ? 27 PHE A N 1 +ATOM 188 C CA . PHE A 1 30 ? 17.712 117.349 112.698 1.00 89.45 ? 27 PHE A CA 1 +ATOM 189 C C . PHE A 1 30 ? 18.084 115.933 113.114 1.00 95.43 ? 27 PHE A C 1 +ATOM 190 O O . PHE A 1 30 ? 19.035 115.350 112.591 1.00 80.65 ? 27 PHE A O 1 +ATOM 191 C CB . PHE A 1 30 ? 16.418 117.316 111.870 1.00 109.28 ? 27 PHE A CB 1 +ATOM 192 C CG . PHE A 1 30 ? 16.510 116.519 110.597 1.00 96.17 ? 27 PHE A CG 1 +ATOM 193 C CD1 . PHE A 1 30 ? 17.156 117.035 109.489 1.00 104.35 ? 27 PHE A CD1 1 +ATOM 194 C CD2 . PHE A 1 30 ? 15.939 115.263 110.500 1.00 84.82 ? 27 PHE A CD2 1 +ATOM 195 C CE1 . PHE A 1 30 ? 17.243 116.314 108.317 1.00 101.33 ? 27 PHE A CE1 1 +ATOM 196 C CE2 . PHE A 1 30 ? 16.026 114.537 109.325 1.00 92.90 ? 27 PHE A CE2 1 +ATOM 197 C CZ . PHE A 1 30 ? 16.681 115.067 108.234 1.00 85.34 ? 27 PHE A CZ 1 +ATOM 198 N N . SER A 1 31 ? 17.329 115.387 114.061 1.00 88.67 ? 28 SER A N 1 +ATOM 199 C CA . SER A 1 31 ? 17.543 114.018 114.509 1.00 82.51 ? 28 SER A CA 1 +ATOM 200 C C . SER A 1 31 ? 16.239 113.259 114.707 1.00 96.09 ? 28 SER A C 1 +ATOM 201 O O . SER A 1 31 ? 15.240 113.806 115.197 1.00 79.65 ? 28 SER A O 1 +ATOM 202 C CB . SER A 1 31 ? 18.387 113.979 115.782 1.00 87.98 ? 28 SER A CB 1 +ATOM 203 O OG . SER A 1 31 ? 19.691 114.462 115.520 1.00 130.09 ? 28 SER A OG 1 +ATOM 204 N N . VAL A 1 32 ? 16.262 111.995 114.287 1.00 91.79 ? 29 VAL A N 1 +ATOM 205 C CA . VAL A 1 32 ? 15.127 111.094 114.462 1.00 95.41 ? 29 VAL A CA 1 +ATOM 206 C C . VAL A 1 32 ? 15.524 109.782 115.137 1.00 78.19 ? 29 VAL A C 1 +ATOM 207 O O . VAL A 1 32 ? 16.527 109.157 114.774 1.00 74.53 ? 29 VAL A O 1 +ATOM 208 C CB . VAL A 1 32 ? 14.425 110.768 113.127 1.00 82.99 ? 29 VAL A CB 1 +ATOM 209 C CG1 . VAL A 1 32 ? 13.077 110.136 113.400 1.00 86.92 ? 29 VAL A CG1 1 +ATOM 210 C CG2 . VAL A 1 32 ? 14.237 112.018 112.301 1.00 62.08 ? 29 VAL A CG2 1 +ATOM 211 N N . SER A 1 33 ? 14.729 109.397 116.135 1.00 75.78 ? 30 SER A N 1 +ATOM 212 C CA . SER A 1 33 ? 14.833 108.100 116.810 1.00 100.79 ? 30 SER A CA 1 +ATOM 213 C C . SER A 1 33 ? 13.583 107.255 116.581 1.00 96.87 ? 30 SER A C 1 +ATOM 214 O O . SER A 1 33 ? 12.454 107.707 116.801 1.00 80.97 ? 30 SER A O 1 +ATOM 215 C CB . SER A 1 33 ? 15.046 108.274 118.314 1.00 79.47 ? 30 SER A CB 1 +ATOM 216 O OG . SER A 1 33 ? 16.422 108.338 118.631 1.00 124.20 ? 30 SER A OG 1 +ATOM 217 N N . GLY A 1 34 ? 13.784 106.020 116.141 1.00 91.09 ? 31 GLY A N 1 +ATOM 218 C CA . GLY A 1 34 ? 12.665 105.141 115.889 1.00 73.78 ? 31 GLY A CA 1 +ATOM 219 C C . GLY A 1 34 ? 12.768 103.811 116.606 1.00 93.55 ? 31 GLY A C 1 +ATOM 220 O O . GLY A 1 34 ? 13.858 103.251 116.737 1.00 79.47 ? 31 GLY A O 1 +ATOM 221 N N . GLU A 1 35 ? 11.629 103.305 117.074 1.00 68.11 ? 32 GLU A N 1 +ATOM 222 C CA . GLU A 1 35 ? 11.576 101.966 117.651 1.00 94.83 ? 32 GLU A CA 1 +ATOM 223 C C . GLU A 1 35 ? 10.368 101.158 117.189 1.00 87.47 ? 32 GLU A C 1 +ATOM 224 O O . GLU A 1 35 ? 9.300 101.703 116.900 1.00 84.15 ? 32 GLU A O 1 +ATOM 225 C CB . GLU A 1 35 ? 11.559 102.034 119.176 1.00 78.40 ? 32 GLU A CB 1 +ATOM 226 C CG . GLU A 1 35 ? 10.225 102.475 119.750 1.00 87.34 ? 32 GLU A CG 1 +ATOM 227 C CD . GLU A 1 35 ? 10.312 102.816 121.219 1.00 164.89 ? 32 GLU A CD 1 +ATOM 228 O OE1 . GLU A 1 35 ? 10.685 101.936 122.006 1.00 166.76 ? 32 GLU A OE1 1 +ATOM 229 O OE2 . GLU A 1 35 ? 10.021 103.967 121.589 1.00 208.38 ? 32 GLU A OE2 1 +ATOM 230 N N . GLY A 1 36 ? 10.548 99.844 117.149 1.00 103.37 ? 33 GLY A N 1 +ATOM 231 C CA . GLY A 1 36 ? 9.448 98.927 116.939 1.00 86.14 ? 33 GLY A CA 1 +ATOM 232 C C . GLY A 1 36 ? 9.928 97.508 116.713 1.00 82.86 ? 33 GLY A C 1 +ATOM 233 O O . GLY A 1 36 ? 10.958 97.092 117.245 1.00 86.88 ? 33 GLY A O 1 +ATOM 234 N N . GLU A 1 37 ? 9.186 96.774 115.892 1.00 89.57 ? 34 GLU A N 1 +ATOM 235 C CA . GLU A 1 37 ? 9.458 95.363 115.664 1.00 88.58 ? 34 GLU A CA 1 +ATOM 236 C C . GLU A 1 37 ? 9.100 94.907 114.252 1.00 77.04 ? 34 GLU A C 1 +ATOM 237 O O . GLU A 1 37 ? 8.223 95.471 113.589 1.00 84.11 ? 34 GLU A O 1 +ATOM 238 C CB . GLU A 1 37 ? 8.693 94.519 116.681 1.00 84.87 ? 34 GLU A CB 1 +ATOM 239 C CG . GLU A 1 37 ? 7.190 94.682 116.539 1.00 136.09 ? 34 GLU A CG 1 +ATOM 240 C CD . GLU A 1 37 ? 6.412 93.961 117.606 1.00 135.76 ? 34 GLU A CD 1 +ATOM 241 O OE1 . GLU A 1 37 ? 6.988 93.074 118.259 1.00 152.89 ? 34 GLU A OE1 1 +ATOM 242 O OE2 . GLU A 1 37 ? 5.225 94.307 117.797 1.00 137.56 ? 34 GLU A OE2 1 +ATOM 243 N N . GLY A 1 38 ? 9.792 93.865 113.810 1.00 79.74 ? 35 GLY A N 1 +ATOM 244 C CA . GLY A 1 38 ? 9.576 93.297 112.497 1.00 88.10 ? 35 GLY A CA 1 +ATOM 245 C C . GLY A 1 38 ? 9.465 91.787 112.524 1.00 83.62 ? 35 GLY A C 1 +ATOM 246 O O . GLY A 1 38 ? 10.194 91.105 113.242 1.00 83.64 ? 35 GLY A O 1 +ATOM 247 N N . ASP A 1 39 ? 8.541 91.272 111.721 1.00 93.48 ? 36 ASP A N 1 +ATOM 248 C CA . ASP A 1 39 ? 8.292 89.842 111.611 1.00 92.27 ? 36 ASP A CA 1 +ATOM 249 C C . ASP A 1 39 ? 8.624 89.347 110.201 1.00 66.38 ? 36 ASP A C 1 +ATOM 250 O O . ASP A 1 39 ? 7.766 89.359 109.322 1.00 68.99 ? 36 ASP A O 1 +ATOM 251 C CB . ASP A 1 39 ? 6.825 89.554 111.938 1.00 78.59 ? 36 ASP A CB 1 +ATOM 252 C CG . ASP A 1 39 ? 6.637 88.228 112.630 1.00 125.18 ? 36 ASP A CG 1 +ATOM 253 O OD1 . ASP A 1 39 ? 7.541 87.373 112.500 1.00 120.49 ? 36 ASP A OD1 1 +ATOM 254 O OD2 . ASP A 1 39 ? 5.592 88.044 113.299 1.00 107.87 ? 36 ASP A OD2 1 +ATOM 255 N N . ALA A 1 40 ? 9.868 88.920 109.987 1.00 90.76 ? 37 ALA A N 1 +ATOM 256 C CA . ALA A 1 40 ? 10.321 88.475 108.662 1.00 84.98 ? 37 ALA A CA 1 +ATOM 257 C C . ALA A 1 40 ? 9.402 87.418 108.054 1.00 81.61 ? 37 ALA A C 1 +ATOM 258 O O . ALA A 1 40 ? 9.036 87.501 106.889 1.00 82.77 ? 37 ALA A O 1 +ATOM 259 C CB . ALA A 1 40 ? 11.759 87.954 108.726 1.00 65.82 ? 37 ALA A CB 1 +ATOM 260 N N . THR A 1 41 ? 9.031 86.442 108.874 1.00 111.83 ? 38 THR A N 1 +ATOM 261 C CA . THR A 1 41 ? 8.160 85.339 108.498 1.00 73.95 ? 38 THR A CA 1 +ATOM 262 C C . THR A 1 41 ? 6.934 85.765 107.691 1.00 88.76 ? 38 THR A C 1 +ATOM 263 O O . THR A 1 41 ? 6.497 85.039 106.806 1.00 92.06 ? 38 THR A O 1 +ATOM 264 C CB . THR A 1 41 ? 7.685 84.588 109.758 1.00 84.06 ? 38 THR A CB 1 +ATOM 265 O OG1 . THR A 1 41 ? 8.784 84.411 110.661 1.00 94.53 ? 38 THR A OG1 1 +ATOM 266 C CG2 . THR A 1 41 ? 7.117 83.241 109.392 1.00 55.68 ? 38 THR A CG2 1 +ATOM 267 N N . TYR A 1 42 ? 6.378 86.935 107.991 1.00 70.06 ? 39 TYR A N 1 +ATOM 268 C CA . TYR A 1 42 ? 5.217 87.415 107.244 1.00 93.09 ? 39 TYR A CA 1 +ATOM 269 C C . TYR A 1 42 ? 5.504 88.753 106.571 1.00 73.38 ? 39 TYR A C 1 +ATOM 270 O O . TYR A 1 42 ? 4.583 89.477 106.180 1.00 82.63 ? 39 TYR A O 1 +ATOM 271 C CB . TYR A 1 42 ? 3.984 87.482 108.149 1.00 57.70 ? 39 TYR A CB 1 +ATOM 272 C CG . TYR A 1 42 ? 3.880 86.250 108.998 1.00 81.00 ? 39 TYR A CG 1 +ATOM 273 C CD1 . TYR A 1 42 ? 3.265 85.095 108.520 1.00 92.23 ? 39 TYR A CD1 1 +ATOM 274 C CD2 . TYR A 1 42 ? 4.447 86.219 110.266 1.00 91.99 ? 39 TYR A CD2 1 +ATOM 275 C CE1 . TYR A 1 42 ? 3.198 83.941 109.303 1.00 92.77 ? 39 TYR A CE1 1 +ATOM 276 C CE2 . TYR A 1 42 ? 4.387 85.085 111.050 1.00 114.15 ? 39 TYR A CE2 1 +ATOM 277 C CZ . TYR A 1 42 ? 3.765 83.946 110.568 1.00 106.44 ? 39 TYR A CZ 1 +ATOM 278 O OH . TYR A 1 42 ? 3.715 82.824 111.367 1.00 85.10 ? 39 TYR A OH 1 +ATOM 279 N N . GLY A 1 43 ? 6.797 89.051 106.433 1.00 81.56 ? 40 GLY A N 1 +ATOM 280 C CA . GLY A 1 43 ? 7.283 90.259 105.784 1.00 80.81 ? 40 GLY A CA 1 +ATOM 281 C C . GLY A 1 43 ? 6.655 91.524 106.337 1.00 94.24 ? 40 GLY A C 1 +ATOM 282 O O . GLY A 1 43 ? 6.088 92.332 105.602 1.00 77.90 ? 40 GLY A O 1 +ATOM 283 N N . LYS A 1 44 ? 6.760 91.702 107.644 1.00 71.72 ? 41 LYS A N 1 +ATOM 284 C CA . LYS A 1 44 ? 5.999 92.736 108.309 1.00 60.49 ? 41 LYS A CA 1 +ATOM 285 C C . LYS A 1 44 ? 6.892 93.654 109.131 1.00 97.46 ? 41 LYS A C 1 +ATOM 286 O O . LYS A 1 44 ? 7.788 93.196 109.841 1.00 80.46 ? 41 LYS A O 1 +ATOM 287 C CB . LYS A 1 44 ? 4.953 92.089 109.197 1.00 68.04 ? 41 LYS A CB 1 +ATOM 288 C CG . LYS A 1 44 ? 3.877 93.029 109.615 1.00 86.26 ? 41 LYS A CG 1 +ATOM 289 C CD . LYS A 1 44 ? 2.933 92.341 110.557 1.00 66.30 ? 41 LYS A CD 1 +ATOM 290 C CE . LYS A 1 44 ? 2.554 93.267 111.680 1.00 108.19 ? 41 LYS A CE 1 +ATOM 291 N NZ . LYS A 1 44 ? 1.388 92.759 112.445 1.00 108.64 ? 41 LYS A NZ 1 +ATOM 292 N N . LEU A 1 45 ? 6.644 94.955 109.016 1.00 101.30 ? 42 LEU A N 1 +ATOM 293 C CA . LEU A 1 45 ? 7.386 95.961 109.765 1.00 83.58 ? 42 LEU A CA 1 +ATOM 294 C C . LEU A 1 45 ? 6.408 96.921 110.447 1.00 57.00 ? 42 LEU A C 1 +ATOM 295 O O . LEU A 1 45 ? 5.420 97.338 109.849 1.00 95.46 ? 42 LEU A O 1 +ATOM 296 C CB . LEU A 1 45 ? 8.327 96.725 108.830 1.00 70.33 ? 42 LEU A CB 1 +ATOM 297 C CG . LEU A 1 45 ? 9.740 97.064 109.304 1.00 90.98 ? 42 LEU A CG 1 +ATOM 298 C CD1 . LEU A 1 45 ? 10.538 95.814 109.598 1.00 120.24 ? 42 LEU A CD1 1 +ATOM 299 C CD2 . LEU A 1 45 ? 10.447 97.899 108.259 1.00 99.61 ? 42 LEU A CD2 1 +ATOM 300 N N . THR A 1 46 ? 6.652 97.229 111.716 1.00 79.52 ? 43 THR A N 1 +ATOM 301 C CA . THR A 1 46 ? 5.929 98.310 112.394 1.00 102.43 ? 43 THR A CA 1 +ATOM 302 C C . THR A 1 46 ? 6.953 99.184 113.105 1.00 86.85 ? 43 THR A C 1 +ATOM 303 O O . THR A 1 46 ? 7.802 98.679 113.835 1.00 84.64 ? 43 THR A O 1 +ATOM 304 C CB . THR A 1 46 ? 4.910 97.816 113.449 1.00 79.33 ? 43 THR A CB 1 +ATOM 305 O OG1 . THR A 1 46 ? 5.561 97.692 114.714 1.00 133.58 ? 43 THR A OG1 1 +ATOM 306 C CG2 . THR A 1 46 ? 4.286 96.478 113.063 1.00 85.81 ? 43 THR A CG2 1 +ATOM 307 N N . LEU A 1 47 ? 6.880 100.490 112.887 1.00 81.27 ? 44 LEU A N 1 +ATOM 308 C CA . LEU A 1 47 ? 7.892 101.396 113.409 1.00 84.22 ? 44 LEU A CA 1 +ATOM 309 C C . LEU A 1 47 ? 7.284 102.733 113.775 1.00 72.15 ? 44 LEU A C 1 +ATOM 310 O O . LEU A 1 47 ? 6.380 103.218 113.089 1.00 66.81 ? 44 LEU A O 1 +ATOM 311 C CB . LEU A 1 47 ? 9.014 101.588 112.388 1.00 71.00 ? 44 LEU A CB 1 +ATOM 312 C CG . LEU A 1 47 ? 10.032 100.449 112.304 1.00 88.83 ? 44 LEU A CG 1 +ATOM 313 C CD1 . LEU A 1 47 ? 10.928 100.649 111.104 1.00 91.09 ? 44 LEU A CD1 1 +ATOM 314 C CD2 . LEU A 1 47 ? 10.864 100.349 113.569 1.00 78.27 ? 44 LEU A CD2 1 +ATOM 315 N N . LYS A 1 48 ? 7.758 103.299 114.886 1.00 74.43 ? 45 LYS A N 1 +ATOM 316 C CA . LYS A 1 48 ? 7.386 104.655 115.292 1.00 59.47 ? 45 LYS A CA 1 +ATOM 317 C C . LYS A 1 48 ? 8.577 105.590 115.370 1.00 90.97 ? 45 LYS A C 1 +ATOM 318 O O . LYS A 1 48 ? 9.601 105.301 116.008 1.00 76.33 ? 45 LYS A O 1 +ATOM 319 C CB . LYS A 1 48 ? 6.644 104.691 116.625 1.00 58.97 ? 45 LYS A CB 1 +ATOM 320 C CG . LYS A 1 48 ? 5.916 106.008 116.860 1.00 52.72 ? 45 LYS A CG 1 +ATOM 321 C CD . LYS A 1 48 ? 5.571 106.222 118.324 1.00 67.24 ? 45 LYS A CD 1 +ATOM 322 C CE . LYS A 1 48 ? 4.406 107.183 118.472 1.00 88.31 ? 45 LYS A CE 1 +ATOM 323 N NZ . LYS A 1 48 ? 4.013 107.363 119.890 1.00 80.96 ? 45 LYS A NZ 1 +ATOM 324 N N . PHE A 1 49 ? 8.407 106.731 114.720 1.00 87.61 ? 46 PHE A N 1 +ATOM 325 C CA . PHE A 1 49 ? 9.432 107.745 114.683 1.00 79.00 ? 46 PHE A CA 1 +ATOM 326 C C . PHE A 1 49 ? 9.004 109.002 115.421 1.00 75.41 ? 46 PHE A C 1 +ATOM 327 O O . PHE A 1 49 ? 7.893 109.492 115.247 1.00 81.88 ? 46 PHE A O 1 +ATOM 328 C CB . PHE A 1 49 ? 9.792 108.038 113.237 1.00 80.01 ? 46 PHE A CB 1 +ATOM 329 C CG . PHE A 1 49 ? 10.226 106.820 112.480 1.00 79.97 ? 46 PHE A CG 1 +ATOM 330 C CD1 . PHE A 1 49 ? 11.479 106.267 112.691 1.00 83.86 ? 46 PHE A CD1 1 +ATOM 331 C CD2 . PHE A 1 49 ? 9.384 106.218 111.573 1.00 82.77 ? 46 PHE A CD2 1 +ATOM 332 C CE1 . PHE A 1 49 ? 11.886 105.150 112.002 1.00 74.00 ? 46 PHE A CE1 1 +ATOM 333 C CE2 . PHE A 1 49 ? 9.791 105.101 110.877 1.00 96.28 ? 46 PHE A CE2 1 +ATOM 334 C CZ . PHE A 1 49 ? 11.040 104.565 111.099 1.00 68.79 ? 46 PHE A CZ 1 +ATOM 335 N N . ILE A 1 50 ? 9.905 109.478 116.274 1.00 94.60 ? 47 ILE A N 1 +ATOM 336 C CA . ILE A 1 50 ? 9.759 110.731 117.001 1.00 59.94 ? 47 ILE A CA 1 +ATOM 337 C C . ILE A 1 50 ? 10.830 111.690 116.491 1.00 101.11 ? 47 ILE A C 1 +ATOM 338 O O . ILE A 1 50 ? 12.013 111.334 116.446 1.00 78.98 ? 47 ILE A O 1 +ATOM 339 C CB . ILE A 1 50 ? 10.012 110.525 118.514 1.00 74.45 ? 47 ILE A CB 1 +ATOM 340 C CG1 . ILE A 1 50 ? 8.969 109.591 119.138 1.00 105.78 ? 47 ILE A CG1 1 +ATOM 341 C CG2 . ILE A 1 50 ? 10.028 111.850 119.244 1.00 109.34 ? 47 ILE A CG2 1 +ATOM 342 C CD1 . ILE A 1 50 ? 7.545 110.086 119.032 1.00 107.76 ? 47 ILE A CD1 1 +ATOM 343 N N . CYS A 1 51 ? 10.442 112.899 116.098 1.00 106.25 ? 48 CYS A N 1 +ATOM 344 C CA . CYS A 1 51 ? 11.452 113.934 115.871 1.00 110.97 ? 48 CYS A CA 1 +ATOM 345 C C . CYS A 1 51 ? 12.010 114.464 117.194 1.00 82.42 ? 48 CYS A C 1 +ATOM 346 O O . CYS A 1 51 ? 11.300 115.156 117.930 1.00 106.35 ? 48 CYS A O 1 +ATOM 347 C CB . CYS A 1 51 ? 10.899 115.096 115.057 1.00 132.05 ? 48 CYS A CB 1 +ATOM 348 S SG . CYS A 1 51 ? 12.212 116.117 114.372 1.00 91.22 ? 48 CYS A SG 1 +ATOM 349 N N . THR A 1 52 ? 13.279 114.150 117.476 1.00 92.47 ? 49 THR A N 1 +ATOM 350 C CA . THR A 1 52 ? 13.929 114.472 118.759 1.00 99.09 ? 49 THR A CA 1 +ATOM 351 C C . THR A 1 52 ? 14.536 115.879 118.818 1.00 85.18 ? 49 THR A C 1 +ATOM 352 O O . THR A 1 52 ? 15.084 116.287 119.846 1.00 91.85 ? 49 THR A O 1 +ATOM 353 C CB . THR A 1 52 ? 15.029 113.416 119.178 1.00 84.16 ? 49 THR A CB 1 +ATOM 354 O OG1 . THR A 1 52 ? 15.959 113.187 118.109 1.00 77.96 ? 49 THR A OG1 1 +ATOM 355 C CG2 . THR A 1 52 ? 14.408 112.101 119.570 1.00 75.12 ? 49 THR A CG2 1 +ATOM 356 N N . THR A 1 53 ? 14.441 116.611 117.710 1.00 103.32 ? 50 THR A N 1 +ATOM 357 C CA . THR A 1 53 ? 14.981 117.968 117.627 1.00 63.92 ? 50 THR A CA 1 +ATOM 358 C C . THR A 1 53 ? 13.891 119.016 117.399 1.00 95.11 ? 50 THR A C 1 +ATOM 359 O O . THR A 1 53 ? 14.185 120.149 117.034 1.00 131.91 ? 50 THR A O 1 +ATOM 360 C CB . THR A 1 53 ? 16.037 118.101 116.497 1.00 81.41 ? 50 THR A CB 1 +ATOM 361 O OG1 . THR A 1 53 ? 15.442 117.811 115.224 1.00 83.09 ? 50 THR A OG1 1 +ATOM 362 C CG2 . THR A 1 53 ? 17.187 117.162 116.731 1.00 79.36 ? 50 THR A CG2 1 +ATOM 363 N N . GLY A 1 54 ? 12.635 118.638 117.609 1.00 80.34 ? 51 GLY A N 1 +ATOM 364 C CA . GLY A 1 54 ? 11.521 119.557 117.442 1.00 86.00 ? 51 GLY A CA 1 +ATOM 365 C C . GLY A 1 54 ? 10.679 119.193 116.239 1.00 66.47 ? 51 GLY A C 1 +ATOM 366 O O . GLY A 1 54 ? 10.300 118.034 116.094 1.00 147.13 ? 51 GLY A O 1 +ATOM 367 N N . LYS A 1 55 ? 10.385 120.176 115.387 1.00 110.33 ? 52 LYS A N 1 +ATOM 368 C CA . LYS A 1 55 ? 9.696 119.931 114.119 1.00 89.95 ? 52 LYS A CA 1 +ATOM 369 C C . LYS A 1 55 ? 10.666 119.477 113.061 1.00 77.44 ? 52 LYS A C 1 +ATOM 370 O O . LYS A 1 55 ? 11.870 119.705 113.163 1.00 80.60 ? 52 LYS A O 1 +ATOM 371 C CB . LYS A 1 55 ? 8.975 121.175 113.621 1.00 67.02 ? 52 LYS A CB 1 +ATOM 372 C CG . LYS A 1 55 ? 7.457 120.967 113.523 1.00 125.17 ? 52 LYS A CG 1 +ATOM 373 C CD . LYS A 1 55 ? 6.733 122.118 112.781 1.00 168.00 ? 52 LYS A CD 1 +ATOM 374 C CE . LYS A 1 55 ? 5.606 122.675 113.632 1.00 180.13 ? 52 LYS A CE 1 +ATOM 375 N NZ . LYS A 1 55 ? 4.789 123.738 112.954 1.00 161.25 ? 52 LYS A NZ 1 +ATOM 376 N N . LEU A 1 56 ? 10.123 118.839 112.035 1.00 87.64 ? 53 LEU A N 1 +ATOM 377 C CA . LEU A 1 56 ? 10.944 118.270 110.986 1.00 80.30 ? 53 LEU A CA 1 +ATOM 378 C C . LEU A 1 56 ? 11.095 119.263 109.822 1.00 72.00 ? 53 LEU A C 1 +ATOM 379 O O . LEU A 1 56 ? 10.122 119.881 109.378 1.00 89.29 ? 53 LEU A O 1 +ATOM 380 C CB . LEU A 1 56 ? 10.366 116.920 110.536 1.00 85.21 ? 53 LEU A CB 1 +ATOM 381 C CG . LEU A 1 56 ? 11.314 115.894 109.906 1.00 91.10 ? 53 LEU A CG 1 +ATOM 382 C CD1 . LEU A 1 56 ? 12.220 115.264 110.931 1.00 62.51 ? 53 LEU A CD1 1 +ATOM 383 C CD2 . LEU A 1 56 ? 10.535 114.829 109.183 1.00 49.52 ? 53 LEU A CD2 1 +ATOM 384 N N . PRO A 1 57 ? 12.335 119.449 109.348 1.00 98.29 ? 54 PRO A N 1 +ATOM 385 C CA . PRO A 1 57 ? 12.586 120.339 108.207 1.00 83.67 ? 54 PRO A CA 1 +ATOM 386 C C . PRO A 1 57 ? 11.908 119.855 106.917 1.00 98.37 ? 54 PRO A C 1 +ATOM 387 O O . PRO A 1 57 ? 11.319 120.637 106.172 1.00 88.54 ? 54 PRO A O 1 +ATOM 388 C CB . PRO A 1 57 ? 14.111 120.290 108.056 1.00 76.71 ? 54 PRO A CB 1 +ATOM 389 C CG . PRO A 1 57 ? 14.553 119.054 108.792 1.00 83.34 ? 54 PRO A CG 1 +ATOM 390 C CD . PRO A 1 57 ? 13.575 118.879 109.903 1.00 88.38 ? 54 PRO A CD 1 +ATOM 391 N N . VAL A 1 58 ? 11.981 118.552 106.688 1.00 96.47 ? 55 VAL A N 1 +ATOM 392 C CA . VAL A 1 58 ? 11.537 117.919 105.456 1.00 96.09 ? 55 VAL A CA 1 +ATOM 393 C C . VAL A 1 58 ? 10.205 117.198 105.706 1.00 102.75 ? 55 VAL A C 1 +ATOM 394 O O . VAL A 1 58 ? 9.854 116.974 106.862 1.00 87.69 ? 55 VAL A O 1 +ATOM 395 C CB . VAL A 1 58 ? 12.627 116.946 105.023 1.00 86.36 ? 55 VAL A CB 1 +ATOM 396 C CG1 . VAL A 1 58 ? 13.901 117.718 104.784 1.00 82.73 ? 55 VAL A CG1 1 +ATOM 397 C CG2 . VAL A 1 58 ? 12.878 115.940 106.117 1.00 98.84 ? 55 VAL A CG2 1 +ATOM 398 N N . PRO A 1 59 ? 9.443 116.852 104.645 1.00 82.83 ? 56 PRO A N 1 +ATOM 399 C CA . PRO A 1 59 ? 8.189 116.146 104.927 1.00 99.70 ? 56 PRO A CA 1 +ATOM 400 C C . PRO A 1 59 ? 8.498 114.734 105.395 1.00 111.38 ? 56 PRO A C 1 +ATOM 401 O O . PRO A 1 59 ? 9.553 114.183 105.047 1.00 86.28 ? 56 PRO A O 1 +ATOM 402 C CB . PRO A 1 59 ? 7.487 116.085 103.563 1.00 76.01 ? 56 PRO A CB 1 +ATOM 403 C CG . PRO A 1 59 ? 8.331 116.834 102.625 1.00 85.15 ? 56 PRO A CG 1 +ATOM 404 C CD . PRO A 1 59 ? 9.703 116.915 103.200 1.00 91.05 ? 56 PRO A CD 1 +ATOM 405 N N . TRP A 1 60 ? 7.608 114.156 106.191 1.00 97.57 ? 57 TRP A N 1 +ATOM 406 C CA . TRP A 1 60 ? 7.848 112.800 106.667 1.00 67.78 ? 57 TRP A CA 1 +ATOM 407 C C . TRP A 1 60 ? 8.011 111.779 105.529 1.00 74.09 ? 57 TRP A C 1 +ATOM 408 O O . TRP A 1 60 ? 9.001 111.046 105.525 1.00 72.43 ? 57 TRP A O 1 +ATOM 409 C CB . TRP A 1 60 ? 6.809 112.359 107.700 1.00 69.79 ? 57 TRP A CB 1 +ATOM 410 C CG . TRP A 1 60 ? 7.103 112.821 109.086 1.00 79.35 ? 57 TRP A CG 1 +ATOM 411 C CD1 . TRP A 1 60 ? 6.415 113.753 109.803 1.00 65.35 ? 57 TRP A CD1 1 +ATOM 412 C CD2 . TRP A 1 60 ? 8.161 112.362 109.929 1.00 82.75 ? 57 TRP A CD2 1 +ATOM 413 N NE1 . TRP A 1 60 ? 6.982 113.905 111.043 1.00 80.48 ? 57 TRP A NE1 1 +ATOM 414 C CE2 . TRP A 1 60 ? 8.055 113.059 111.148 1.00 83.79 ? 57 TRP A CE2 1 +ATOM 415 C CE3 . TRP A 1 60 ? 9.189 111.426 109.774 1.00 77.70 ? 57 TRP A CE3 1 +ATOM 416 C CZ2 . TRP A 1 60 ? 8.938 112.851 112.208 1.00 73.96 ? 57 TRP A CZ2 1 +ATOM 417 C CZ3 . TRP A 1 60 ? 10.065 111.220 110.824 1.00 75.14 ? 57 TRP A CZ3 1 +ATOM 418 C CH2 . TRP A 1 60 ? 9.935 111.932 112.025 1.00 79.19 ? 57 TRP A CH2 1 +ATOM 419 N N . PRO A 1 61 ? 7.072 111.753 104.550 1.00 80.36 ? 58 PRO A N 1 +ATOM 420 C CA . PRO A 1 61 ? 7.144 110.804 103.431 1.00 51.64 ? 58 PRO A CA 1 +ATOM 421 C C . PRO A 1 61 ? 8.509 110.664 102.758 1.00 69.68 ? 58 PRO A C 1 +ATOM 422 O O . PRO A 1 61 ? 8.806 109.576 102.278 1.00 88.86 ? 58 PRO A O 1 +ATOM 423 C CB . PRO A 1 61 ? 6.135 111.379 102.441 1.00 77.49 ? 58 PRO A CB 1 +ATOM 424 C CG . PRO A 1 61 ? 5.101 111.957 103.295 1.00 81.90 ? 58 PRO A CG 1 +ATOM 425 C CD . PRO A 1 61 ? 5.822 112.536 104.477 1.00 75.59 ? 58 PRO A CD 1 +ATOM 426 N N . THR A 1 62 ? 9.320 111.718 102.742 1.00 91.99 ? 59 THR A N 1 +ATOM 427 C CA . THR A 1 62 ? 10.631 111.691 102.081 1.00 94.46 ? 59 THR A CA 1 +ATOM 428 C C . THR A 1 62 ? 11.665 110.769 102.713 1.00 90.38 ? 59 THR A C 1 +ATOM 429 O O . THR A 1 62 ? 12.730 110.530 102.135 1.00 82.78 ? 59 THR A O 1 +ATOM 430 C CB . THR A 1 62 ? 11.269 113.075 102.082 1.00 92.12 ? 59 THR A CB 1 +ATOM 431 O OG1 . THR A 1 62 ? 11.282 113.584 103.420 1.00 93.23 ? 59 THR A OG1 1 +ATOM 432 C CG2 . THR A 1 62 ? 10.487 114.006 101.217 1.00 88.23 ? 59 THR A CG2 1 +ATOM 433 N N . LEU A 1 63 ? 11.366 110.266 103.904 1.00 85.83 ? 60 LEU A N 1 +ATOM 434 C CA . LEU A 1 63 ? 12.358 109.524 104.672 1.00 76.36 ? 60 LEU A CA 1 +ATOM 435 C C . LEU A 1 63 ? 12.029 108.046 104.864 1.00 101.13 ? 60 LEU A C 1 +ATOM 436 O O . LEU A 1 63 ? 12.892 107.274 105.295 1.00 72.24 ? 60 LEU A O 1 +ATOM 437 C CB . LEU A 1 63 ? 12.563 110.180 106.031 1.00 81.96 ? 60 LEU A CB 1 +ATOM 438 C CG . LEU A 1 63 ? 13.074 111.614 105.995 1.00 96.60 ? 60 LEU A CG 1 +ATOM 439 C CD1 . LEU A 1 63 ? 12.961 112.226 107.384 1.00 91.04 ? 60 LEU A CD1 1 +ATOM 440 C CD2 . LEU A 1 63 ? 14.508 111.629 105.502 1.00 76.48 ? 60 LEU A CD2 1 +ATOM 441 N N . VAL A 1 64 ? 10.790 107.672 104.545 1.00 95.84 ? 61 VAL A N 1 +ATOM 442 C CA . VAL A 1 64 ? 10.303 106.299 104.673 1.00 79.63 ? 61 VAL A CA 1 +ATOM 443 C C . VAL A 1 64 ? 11.322 105.257 104.230 1.00 70.17 ? 61 VAL A C 1 +ATOM 444 O O . VAL A 1 64 ? 11.555 104.268 104.916 1.00 80.91 ? 61 VAL A O 1 +ATOM 445 C CB . VAL A 1 64 ? 9.007 106.088 103.869 1.00 78.42 ? 61 VAL A CB 1 +ATOM 446 C CG1 . VAL A 1 64 ? 8.661 104.624 103.811 1.00 67.45 ? 61 VAL A CG1 1 +ATOM 447 C CG2 . VAL A 1 64 ? 7.866 106.880 104.485 1.00 65.33 ? 61 VAL A CG2 1 +ATOM 448 N N . THR A 1 65 ? 11.953 105.501 103.094 1.00 78.20 ? 62 THR A N 1 +ATOM 449 C CA . THR A 1 65 ? 12.881 104.542 102.527 1.00 88.53 ? 62 THR A CA 1 +ATOM 450 C C . THR A 1 65 ? 14.187 104.554 103.277 1.00 66.58 ? 62 THR A C 1 +ATOM 451 O O . THR A 1 65 ? 14.960 103.607 103.219 1.00 100.19 ? 62 THR A O 1 +ATOM 452 C CB . THR A 1 65 ? 13.215 104.916 101.095 1.00 90.91 ? 62 THR A CB 1 +ATOM 453 O OG1 . THR A 1 65 ? 14.027 106.098 101.102 1.00 119.74 ? 62 THR A OG1 1 +ATOM 454 C CG2 . THR A 1 65 ? 11.949 105.189 100.324 1.00 89.04 ? 62 THR A CG2 1 +ATOM 455 N N . THR A 1 66 ? 14.470 105.650 103.952 1.00 89.13 ? 63 THR A N 1 +ATOM 456 C CA . THR A 1 66 ? 15.785 105.768 104.537 1.00 100.54 ? 63 THR A CA 1 +ATOM 457 C C . THR A 1 66 ? 15.716 105.043 105.851 1.00 98.54 ? 63 THR A C 1 +ATOM 458 O O . THR A 1 66 ? 16.662 104.347 106.252 1.00 98.81 ? 63 THR A O 1 +ATOM 459 C CB . THR A 1 66 ? 16.219 107.242 104.718 1.00 105.83 ? 63 THR A CB 1 +ATOM 460 O OG1 . THR A 1 66 ? 15.916 107.994 103.528 1.00 91.79 ? 63 THR A OG1 1 +ATOM 461 C CG2 . THR A 1 66 ? 17.721 107.323 105.032 1.00 81.64 ? 63 THR A CG2 1 +ATOM 462 N N . PHE A 1 67 ? 14.546 105.193 106.473 1.00 93.64 ? 64 PHE A N 1 +ATOM 463 C CA . PHE A 1 67 ? 14.249 104.599 107.779 1.00 89.89 ? 64 PHE A CA 1 +ATOM 464 C C . PHE A 1 67 ? 13.898 103.068 107.735 1.00 97.23 ? 64 PHE A C 1 +ATOM 465 O O . PHE A 1 67 ? 14.533 102.193 108.523 1.00 102.50 ? 64 PHE A O 1 +ATOM 466 C CB . PHE A 1 67 ? 12.959 105.160 108.390 1.00 93.28 ? 64 PHE A CB 1 +ATOM 467 C CG . PHE A 1 67 ? 13.019 106.557 108.894 1.00 68.97 ? 64 PHE A CG 1 +ATOM 468 C CD1 . PHE A 1 67 ? 14.175 107.083 109.435 1.00 84.60 ? 64 PHE A CD1 1 +ATOM 469 C CD2 . PHE A 1 67 ? 11.873 107.352 108.830 1.00 92.49 ? 64 PHE A CD2 1 +ATOM 470 C CE1 . PHE A 1 67 ? 14.202 108.385 109.888 1.00 80.89 ? 64 PHE A CE1 1 +ATOM 471 C CE2 . PHE A 1 67 ? 11.890 108.654 109.279 1.00 91.41 ? 64 PHE A CE2 1 +ATOM 472 C CZ . PHE A 1 67 ? 13.054 109.174 109.808 1.00 85.83 ? 64 PHE A CZ 1 +HETATM 473 N N1 . CR2 A 1 68 ? 12.930 102.717 106.900 1.00 89.95 ? 65 CR2 A N1 1 +HETATM 474 C CA1 . CR2 A 1 68 ? 12.789 101.251 106.360 1.00 75.27 ? 65 CR2 A CA1 1 +HETATM 475 C C1 . CR2 A 1 68 ? 13.261 100.932 104.903 1.00 99.79 ? 65 CR2 A C1 1 +HETATM 476 N N2 . CR2 A 1 68 ? 12.566 100.906 103.708 1.00 92.99 ? 65 CR2 A N2 1 +HETATM 477 N N3 . CR2 A 1 68 ? 14.550 100.657 104.664 1.00 84.57 ? 65 CR2 A N3 1 +HETATM 478 C C2 . CR2 A 1 68 ? 14.747 100.483 103.390 1.00 79.84 ? 65 CR2 A C2 1 +HETATM 479 O O2 . CR2 A 1 68 ? 15.866 100.230 102.810 1.00 81.97 ? 65 CR2 A O2 1 +HETATM 480 C CA2 . CR2 A 1 68 ? 13.460 100.645 102.733 1.00 97.63 ? 65 CR2 A CA2 1 +HETATM 481 C CA3 . CR2 A 1 68 ? 15.625 100.729 105.607 1.00 62.31 ? 65 CR2 A CA3 1 +HETATM 482 C C3 . CR2 A 1 68 ? 15.930 99.386 106.229 1.00 92.95 ? 65 CR2 A C3 1 +HETATM 483 O O3 . CR2 A 1 68 ? 17.301 98.976 106.194 1.00 83.65 ? 65 CR2 A O3 1 +HETATM 484 C CB2 . CR2 A 1 68 ? 13.081 100.530 101.297 1.00 87.36 ? 65 CR2 A CB2 1 +HETATM 485 C CG2 . CR2 A 1 68 ? 11.716 100.774 100.748 1.00 85.03 ? 65 CR2 A CG2 1 +HETATM 486 C CD1 . CR2 A 1 68 ? 10.656 101.127 101.567 1.00 83.31 ? 65 CR2 A CD1 1 +HETATM 487 C CD2 . CR2 A 1 68 ? 11.515 100.821 99.367 1.00 87.20 ? 65 CR2 A CD2 1 +HETATM 488 C CE1 . CR2 A 1 68 ? 9.412 101.414 101.035 1.00 98.43 ? 65 CR2 A CE1 1 +HETATM 489 C CE2 . CR2 A 1 68 ? 10.264 101.106 98.826 1.00 77.63 ? 65 CR2 A CE2 1 +HETATM 490 C CZ . CR2 A 1 68 ? 9.207 101.404 99.667 1.00 98.85 ? 65 CR2 A CZ 1 +HETATM 491 O OH . CR2 A 1 68 ? 7.957 101.679 99.157 1.00 99.14 ? 65 CR2 A OH 1 +ATOM 492 N N . VAL A 1 69 ? 14.915 98.524 106.284 1.00 111.95 ? 68 VAL A N 1 +ATOM 493 C CA . VAL A 1 69 ? 15.247 97.322 106.996 1.00 87.68 ? 68 VAL A CA 1 +ATOM 494 C C . VAL A 1 69 ? 15.056 96.064 106.277 1.00 69.26 ? 68 VAL A C 1 +ATOM 495 O O . VAL A 1 69 ? 14.651 95.071 106.838 1.00 103.03 ? 68 VAL A O 1 +ATOM 496 C CB . VAL A 1 69 ? 15.226 97.260 108.555 1.00 76.10 ? 68 VAL A CB 1 +ATOM 497 C CG1 . VAL A 1 69 ? 16.295 98.182 109.071 1.00 73.53 ? 68 VAL A CG1 1 +ATOM 498 C CG2 . VAL A 1 69 ? 13.903 97.527 109.225 1.00 124.85 ? 68 VAL A CG2 1 +ATOM 499 N N . GLN A 1 70 ? 15.477 96.102 105.020 1.00 104.85 ? 69 GLN A N 1 +ATOM 500 C CA . GLN A 1 70 ? 15.078 95.091 104.048 1.00 102.25 ? 69 GLN A CA 1 +ATOM 501 C C . GLN A 1 70 ? 15.447 93.649 104.389 1.00 78.87 ? 69 GLN A C 1 +ATOM 502 O O . GLN A 1 70 ? 15.162 92.730 103.623 1.00 115.97 ? 69 GLN A O 1 +ATOM 503 C CB . GLN A 1 70 ? 15.589 95.476 102.668 1.00 78.86 ? 69 GLN A CB 1 +ATOM 504 C CG . GLN A 1 70 ? 14.891 96.680 102.066 1.00 101.28 ? 69 GLN A CG 1 +ATOM 505 C CD . GLN A 1 70 ? 15.729 97.326 100.988 1.00 116.44 ? 69 GLN A CD 1 +ATOM 506 O OE1 . GLN A 1 70 ? 16.926 97.046 100.873 1.00 104.31 ? 69 GLN A OE1 1 +ATOM 507 N NE2 . GLN A 1 70 ? 15.112 98.193 100.187 1.00 111.51 ? 69 GLN A NE2 1 +ATOM 508 N N . CYS A 1 71 ? 16.072 93.464 105.547 1.00 95.42 ? 70 CYS A N 1 +ATOM 509 C CA . CYS A 1 71 ? 16.296 92.147 106.120 1.00 90.39 ? 70 CYS A CA 1 +ATOM 510 C C . CYS A 1 71 ? 15.012 91.559 106.722 1.00 105.44 ? 70 CYS A C 1 +ATOM 511 O O . CYS A 1 71 ? 14.999 90.423 107.179 1.00 104.55 ? 70 CYS A O 1 +ATOM 512 C CB . CYS A 1 71 ? 17.421 92.203 107.169 1.00 77.14 ? 70 CYS A CB 1 +ATOM 513 S SG . CYS A 1 71 ? 17.299 93.517 108.429 1.00 109.46 ? 70 CYS A SG 1 +ATOM 514 N N . PHE A 1 72 ? 13.932 92.333 106.721 1.00 90.68 ? 71 PHE A N 1 +ATOM 515 C CA . PHE A 1 72 ? 12.663 91.854 107.257 1.00 87.82 ? 71 PHE A CA 1 +ATOM 516 C C . PHE A 1 72 ? 11.705 91.567 106.113 1.00 89.27 ? 71 PHE A C 1 +ATOM 517 O O . PHE A 1 72 ? 10.494 91.494 106.300 1.00 128.56 ? 71 PHE A O 1 +ATOM 518 C CB . PHE A 1 72 ? 12.054 92.864 108.238 1.00 76.88 ? 71 PHE A CB 1 +ATOM 519 C CG . PHE A 1 72 ? 12.734 92.898 109.584 1.00 82.93 ? 71 PHE A CG 1 +ATOM 520 C CD1 . PHE A 1 72 ? 13.835 93.705 109.798 1.00 95.36 ? 71 PHE A CD1 1 +ATOM 521 C CD2 . PHE A 1 72 ? 12.266 92.127 110.635 1.00 102.44 ? 71 PHE A CD2 1 +ATOM 522 C CE1 . PHE A 1 72 ? 14.443 93.743 111.026 1.00 81.20 ? 71 PHE A CE1 1 +ATOM 523 C CE2 . PHE A 1 72 ? 12.886 92.158 111.870 1.00 86.83 ? 71 PHE A CE2 1 +ATOM 524 C CZ . PHE A 1 72 ? 13.979 92.965 112.067 1.00 110.70 ? 71 PHE A CZ 1 +ATOM 525 N N . SER A 1 73 ? 12.251 91.412 104.918 1.00 72.01 ? 72 SER A N 1 +ATOM 526 C CA . SER A 1 73 ? 11.436 91.003 103.794 1.00 94.39 ? 72 SER A CA 1 +ATOM 527 C C . SER A 1 73 ? 11.120 89.521 103.936 1.00 97.60 ? 72 SER A C 1 +ATOM 528 O O . SER A 1 73 ? 11.908 88.761 104.497 1.00 125.56 ? 72 SER A O 1 +ATOM 529 C CB . SER A 1 73 ? 12.165 91.265 102.498 1.00 82.31 ? 72 SER A CB 1 +ATOM 530 N N . ARG A 1 74 ? 9.966 89.107 103.432 1.00 93.33 ? 73 ARG A N 1 +ATOM 531 C CA . ARG A 1 74 ? 9.639 87.690 103.411 1.00 96.66 ? 73 ARG A CA 1 +ATOM 532 C C . ARG A 1 74 ? 10.117 87.034 102.127 1.00 86.87 ? 73 ARG A C 1 +ATOM 533 O O . ARG A 1 74 ? 9.607 87.320 101.042 1.00 92.32 ? 73 ARG A O 1 +ATOM 534 C CB . ARG A 1 74 ? 8.139 87.462 103.561 1.00 99.05 ? 73 ARG A CB 1 +ATOM 535 C CG . ARG A 1 74 ? 7.777 85.993 103.633 1.00 93.90 ? 73 ARG A CG 1 +ATOM 536 C CD . ARG A 1 74 ? 6.309 85.790 103.905 1.00 80.81 ? 73 ARG A CD 1 +ATOM 537 N NE . ARG A 1 74 ? 5.478 86.165 102.769 1.00 86.34 ? 73 ARG A NE 1 +ATOM 538 C CZ . ARG A 1 74 ? 5.432 85.496 101.623 1.00 104.79 ? 73 ARG A CZ 1 +ATOM 539 N NH1 . ARG A 1 74 ? 6.191 84.413 101.437 1.00 53.62 ? 73 ARG A NH1 1 +ATOM 540 N NH2 . ARG A 1 74 ? 4.625 85.921 100.658 1.00 85.11 ? 73 ARG A NH2 1 +ATOM 541 N N . TYR A 1 75 ? 11.101 86.151 102.268 1.00 93.37 ? 74 TYR A N 1 +ATOM 542 C CA . TYR A 1 75 ? 11.603 85.355 101.155 1.00 108.76 ? 74 TYR A CA 1 +ATOM 543 C C . TYR A 1 75 ? 10.878 83.996 101.100 1.00 106.54 ? 74 TYR A C 1 +ATOM 544 O O . TYR A 1 75 ? 10.915 83.230 102.068 1.00 120.67 ? 74 TYR A O 1 +ATOM 545 C CB . TYR A 1 75 ? 13.132 85.179 101.273 1.00 84.00 ? 74 TYR A CB 1 +ATOM 546 C CG . TYR A 1 75 ? 13.953 86.306 100.650 1.00 93.82 ? 74 TYR A CG 1 +ATOM 547 C CD1 . TYR A 1 75 ? 14.103 87.534 101.287 1.00 90.86 ? 74 TYR A CD1 1 +ATOM 548 C CD2 . TYR A 1 75 ? 14.581 86.133 99.423 1.00 107.55 ? 74 TYR A CD2 1 +ATOM 549 C CE1 . TYR A 1 75 ? 14.851 88.561 100.711 1.00 101.08 ? 74 TYR A CE1 1 +ATOM 550 C CE2 . TYR A 1 75 ? 15.328 87.151 98.839 1.00 93.01 ? 74 TYR A CE2 1 +ATOM 551 C CZ . TYR A 1 75 ? 15.460 88.363 99.483 1.00 109.99 ? 74 TYR A CZ 1 +ATOM 552 O OH . TYR A 1 75 ? 16.205 89.366 98.889 1.00 110.11 ? 74 TYR A OH 1 +ATOM 553 N N . PRO A 1 76 ? 10.192 83.705 99.975 1.00 95.98 ? 75 PRO A N 1 +ATOM 554 C CA . PRO A 1 76 ? 9.611 82.376 99.769 1.00 87.12 ? 75 PRO A CA 1 +ATOM 555 C C . PRO A 1 76 ? 10.713 81.326 99.818 1.00 130.68 ? 75 PRO A C 1 +ATOM 556 O O . PRO A 1 76 ? 11.875 81.645 99.555 1.00 117.69 ? 75 PRO A O 1 +ATOM 557 C CB . PRO A 1 76 ? 9.043 82.453 98.349 1.00 91.88 ? 75 PRO A CB 1 +ATOM 558 C CG . PRO A 1 76 ? 8.854 83.865 98.080 1.00 101.35 ? 75 PRO A CG 1 +ATOM 559 C CD . PRO A 1 76 ? 9.931 84.589 98.829 1.00 107.60 ? 75 PRO A CD 1 +ATOM 560 N N . ASP A 1 77 ? 10.348 80.092 100.143 1.00 129.15 ? 76 ASP A N 1 +ATOM 561 C CA . ASP A 1 77 ? 11.320 79.030 100.376 1.00 126.79 ? 76 ASP A CA 1 +ATOM 562 C C . ASP A 1 77 ? 12.222 78.761 99.175 1.00 131.50 ? 76 ASP A C 1 +ATOM 563 O O . ASP A 1 77 ? 13.425 78.532 99.326 1.00 100.37 ? 76 ASP A O 1 +ATOM 564 C CB . ASP A 1 77 ? 10.600 77.753 100.807 1.00 156.04 ? 76 ASP A CB 1 +ATOM 565 C CG . ASP A 1 77 ? 9.769 77.952 102.062 1.00 172.28 ? 76 ASP A CG 1 +ATOM 566 O OD1 . ASP A 1 77 ? 10.371 78.197 103.130 1.00 159.13 ? 76 ASP A OD1 1 +ATOM 567 O OD2 . ASP A 1 77 ? 8.524 77.862 101.983 1.00 182.03 ? 76 ASP A OD2 1 +ATOM 568 N N . HIS A 1 78 ? 11.643 78.813 97.981 1.00 122.22 ? 77 HIS A N 1 +ATOM 569 C CA . HIS A 1 78 ? 12.399 78.546 96.764 1.00 81.92 ? 77 HIS A CA 1 +ATOM 570 C C . HIS A 1 78 ? 13.377 79.668 96.410 1.00 122.35 ? 77 HIS A C 1 +ATOM 571 O O . HIS A 1 78 ? 14.140 79.548 95.449 1.00 127.89 ? 77 HIS A O 1 +ATOM 572 C CB . HIS A 1 78 ? 11.448 78.293 95.598 1.00 93.30 ? 77 HIS A CB 1 +ATOM 573 C CG . HIS A 1 78 ? 10.751 79.521 95.104 1.00 110.74 ? 77 HIS A CG 1 +ATOM 574 N ND1 . HIS A 1 78 ? 9.537 79.943 95.605 1.00 105.21 ? 77 HIS A ND1 1 +ATOM 575 C CD2 . HIS A 1 78 ? 11.087 80.407 94.137 1.00 97.37 ? 77 HIS A CD2 1 +ATOM 576 C CE1 . HIS A 1 78 ? 9.160 81.040 94.973 1.00 117.54 ? 77 HIS A CE1 1 +ATOM 577 N NE2 . HIS A 1 78 ? 10.083 81.343 94.078 1.00 127.65 ? 77 HIS A NE2 1 +ATOM 578 N N . MET A 1 79 ? 13.348 80.750 97.190 1.00 126.41 ? 78 MET A N 1 +ATOM 579 C CA . MET A 1 79 ? 14.199 81.917 96.957 1.00 104.57 ? 78 MET A CA 1 +ATOM 580 C C . MET A 1 79 ? 15.269 82.102 98.043 1.00 121.54 ? 78 MET A C 1 +ATOM 581 O O . MET A 1 79 ? 16.355 82.625 97.773 1.00 104.09 ? 78 MET A O 1 +ATOM 582 C CB . MET A 1 79 ? 13.347 83.188 96.821 1.00 88.73 ? 78 MET A CB 1 +ATOM 583 C CG . MET A 1 79 ? 12.464 83.210 95.580 1.00 115.36 ? 78 MET A CG 1 +ATOM 584 S SD . MET A 1 79 ? 11.768 84.830 95.213 1.00 113.70 ? 78 MET A SD 1 +ATOM 585 C CE . MET A 1 79 ? 13.236 85.831 95.403 1.00 91.92 ? 78 MET A CE 1 +ATOM 586 N N . LYS A 1 80 ? 14.965 81.637 99.255 1.00 100.18 ? 79 LYS A N 1 +ATOM 587 C CA . LYS A 1 80 ? 15.796 81.839 100.455 1.00 107.29 ? 79 LYS A CA 1 +ATOM 588 C C . LYS A 1 80 ? 17.330 81.698 100.334 1.00 108.04 ? 79 LYS A C 1 +ATOM 589 O O . LYS A 1 80 ? 18.035 81.803 101.337 1.00 141.46 ? 79 LYS A O 1 +ATOM 590 C CB . LYS A 1 80 ? 15.298 80.943 101.602 1.00 85.86 ? 79 LYS A CB 1 +ATOM 591 C CG . LYS A 1 80 ? 13.902 81.266 102.115 1.00 111.86 ? 79 LYS A CG 1 +ATOM 592 C CD . LYS A 1 80 ? 13.628 80.534 103.420 1.00 82.82 ? 79 LYS A CD 1 +ATOM 593 C CE . LYS A 1 80 ? 12.232 80.822 103.951 1.00 103.31 ? 79 LYS A CE 1 +ATOM 594 N NZ . LYS A 1 80 ? 12.140 82.128 104.659 1.00 115.11 ? 79 LYS A NZ 1 +ATOM 595 N N . GLN A 1 81 ? 17.850 81.463 99.133 1.00 120.96 ? 80 GLN A N 1 +ATOM 596 C CA . GLN A 1 81 ? 19.297 81.408 98.941 1.00 132.95 ? 80 GLN A CA 1 +ATOM 597 C C . GLN A 1 81 ? 19.773 82.645 98.176 1.00 134.27 ? 80 GLN A C 1 +ATOM 598 O O . GLN A 1 81 ? 20.927 82.737 97.755 1.00 143.41 ? 80 GLN A O 1 +ATOM 599 C CB . GLN A 1 81 ? 19.732 80.101 98.256 1.00 127.39 ? 80 GLN A CB 1 +ATOM 600 C CG . GLN A 1 81 ? 19.299 79.937 96.799 1.00 115.58 ? 80 GLN A CG 1 +ATOM 601 C CD . GLN A 1 81 ? 17.845 79.508 96.637 1.00 139.64 ? 80 GLN A CD 1 +ATOM 602 O OE1 . GLN A 1 81 ? 17.156 79.203 97.613 1.00 156.28 ? 80 GLN A OE1 1 +ATOM 603 N NE2 . GLN A 1 81 ? 17.373 79.481 95.392 1.00 117.03 ? 80 GLN A NE2 1 +ATOM 604 N N . HIS A 1 82 ? 18.858 83.595 98.011 1.00 124.90 ? 81 HIS A N 1 +ATOM 605 C CA . HIS A 1 82 ? 19.173 84.906 97.450 1.00 129.79 ? 81 HIS A CA 1 +ATOM 606 C C . HIS A 1 82 ? 18.886 86.027 98.462 1.00 128.81 ? 81 HIS A C 1 +ATOM 607 O O . HIS A 1 82 ? 18.682 87.185 98.085 1.00 113.37 ? 81 HIS A O 1 +ATOM 608 C CB . HIS A 1 82 ? 18.365 85.150 96.179 1.00 126.12 ? 81 HIS A CB 1 +ATOM 609 C CG . HIS A 1 82 ? 18.583 84.128 95.107 1.00 122.29 ? 81 HIS A CG 1 +ATOM 610 N ND1 . HIS A 1 82 ? 19.789 83.965 94.460 1.00 124.23 ? 81 HIS A ND1 1 +ATOM 611 C CD2 . HIS A 1 82 ? 17.735 83.233 94.552 1.00 89.18 ? 81 HIS A CD2 1 +ATOM 612 C CE1 . HIS A 1 82 ? 19.676 83.010 93.556 1.00 136.59 ? 81 HIS A CE1 1 +ATOM 613 N NE2 . HIS A 1 82 ? 18.438 82.551 93.588 1.00 141.91 ? 81 HIS A NE2 1 +ATOM 614 N N . ASP A 1 83 ? 18.863 85.665 99.744 1.00 112.16 ? 82 ASP A N 1 +ATOM 615 C CA . ASP A 1 83 ? 18.645 86.609 100.838 1.00 110.73 ? 82 ASP A CA 1 +ATOM 616 C C . ASP A 1 83 ? 19.991 87.073 101.382 1.00 106.02 ? 82 ASP A C 1 +ATOM 617 O O . ASP A 1 83 ? 20.524 86.490 102.331 1.00 123.15 ? 82 ASP A O 1 +ATOM 618 C CB . ASP A 1 83 ? 17.830 85.945 101.955 1.00 151.86 ? 82 ASP A CB 1 +ATOM 619 C CG . ASP A 1 83 ? 17.256 86.945 102.956 1.00 138.95 ? 82 ASP A CG 1 +ATOM 620 O OD1 . ASP A 1 83 ? 17.918 87.953 103.280 1.00 112.03 ? 82 ASP A OD1 1 +ATOM 621 O OD2 . ASP A 1 83 ? 16.128 86.709 103.435 1.00 152.10 ? 82 ASP A OD2 1 +ATOM 622 N N . PHE A 1 84 ? 20.526 88.123 100.763 1.00 106.70 ? 83 PHE A N 1 +ATOM 623 C CA . PHE A 1 84 ? 21.802 88.720 101.139 1.00 86.13 ? 83 PHE A CA 1 +ATOM 624 C C . PHE A 1 84 ? 21.701 89.381 102.501 1.00 103.54 ? 83 PHE A C 1 +ATOM 625 O O . PHE A 1 84 ? 22.540 89.171 103.377 1.00 132.83 ? 83 PHE A O 1 +ATOM 626 C CB . PHE A 1 84 ? 22.206 89.778 100.108 1.00 89.29 ? 83 PHE A CB 1 +ATOM 627 C CG . PHE A 1 84 ? 23.226 90.761 100.621 1.00 112.71 ? 83 PHE A CG 1 +ATOM 628 C CD1 . PHE A 1 84 ? 24.552 90.381 100.785 1.00 135.11 ? 83 PHE A CD1 1 +ATOM 629 C CD2 . PHE A 1 84 ? 22.861 92.057 100.955 1.00 101.90 ? 83 PHE A CD2 1 +ATOM 630 C CE1 . PHE A 1 84 ? 25.500 91.276 101.271 1.00 126.99 ? 83 PHE A CE1 1 +ATOM 631 C CE2 . PHE A 1 84 ? 23.801 92.954 101.442 1.00 131.65 ? 83 PHE A CE2 1 +ATOM 632 C CZ . PHE A 1 84 ? 25.124 92.563 101.597 1.00 134.53 ? 83 PHE A CZ 1 +ATOM 633 N N . PHE A 1 85 ? 20.663 90.197 102.645 1.00 92.93 ? 84 PHE A N 1 +ATOM 634 C CA . PHE A 1 85 ? 20.379 90.955 103.856 1.00 94.66 ? 84 PHE A CA 1 +ATOM 635 C C . PHE A 1 85 ? 20.522 90.154 105.140 1.00 109.06 ? 84 PHE A C 1 +ATOM 636 O O . PHE A 1 85 ? 21.331 90.492 106.005 1.00 135.84 ? 84 PHE A O 1 +ATOM 637 C CB . PHE A 1 85 ? 18.974 91.533 103.762 1.00 103.80 ? 84 PHE A CB 1 +ATOM 638 C CG . PHE A 1 85 ? 18.781 92.436 102.587 1.00 104.95 ? 84 PHE A CG 1 +ATOM 639 C CD1 . PHE A 1 85 ? 19.727 93.389 102.272 1.00 103.63 ? 84 PHE A CD1 1 +ATOM 640 C CD2 . PHE A 1 85 ? 17.668 92.318 101.783 1.00 104.10 ? 84 PHE A CD2 1 +ATOM 641 C CE1 . PHE A 1 85 ? 19.555 94.214 101.196 1.00 107.24 ? 84 PHE A CE1 1 +ATOM 642 C CE2 . PHE A 1 85 ? 17.489 93.143 100.700 1.00 75.42 ? 84 PHE A CE2 1 +ATOM 643 C CZ . PHE A 1 85 ? 18.434 94.093 100.407 1.00 96.61 ? 84 PHE A CZ 1 +ATOM 644 N N . LYS A 1 86 ? 19.740 89.090 105.263 1.00 116.37 ? 85 LYS A N 1 +ATOM 645 C CA . LYS A 1 86 ? 19.808 88.255 106.453 1.00 123.65 ? 85 LYS A CA 1 +ATOM 646 C C . LYS A 1 86 ? 21.158 87.542 106.568 1.00 123.42 ? 85 LYS A C 1 +ATOM 647 O O . LYS A 1 86 ? 21.727 87.451 107.653 1.00 104.07 ? 85 LYS A O 1 +ATOM 648 C CB . LYS A 1 86 ? 18.656 87.252 106.472 1.00 100.91 ? 85 LYS A CB 1 +ATOM 649 C CG . LYS A 1 86 ? 17.281 87.895 106.488 1.00 97.78 ? 85 LYS A CG 1 +ATOM 650 C CD . LYS A 1 86 ? 16.209 86.847 106.732 1.00 98.05 ? 85 LYS A CD 1 +ATOM 651 C CE . LYS A 1 86 ? 14.803 87.419 106.613 1.00 89.38 ? 85 LYS A CE 1 +ATOM 652 N NZ . LYS A 1 86 ? 14.545 88.043 105.280 1.00 122.64 ? 85 LYS A NZ 1 +ATOM 653 N N . SER A 1 87 ? 21.681 87.066 105.443 1.00 122.96 ? 86 SER A N 1 +ATOM 654 C CA . SER A 1 87 ? 22.910 86.273 105.450 1.00 122.85 ? 86 SER A CA 1 +ATOM 655 C C . SER A 1 87 ? 24.105 87.043 106.009 1.00 118.84 ? 86 SER A C 1 +ATOM 656 O O . SER A 1 87 ? 25.093 86.446 106.445 1.00 118.47 ? 86 SER A O 1 +ATOM 657 C CB . SER A 1 87 ? 23.225 85.764 104.040 1.00 130.69 ? 86 SER A CB 1 +ATOM 658 O OG . SER A 1 87 ? 23.598 86.824 103.178 1.00 123.08 ? 86 SER A OG 1 +ATOM 659 N N . ALA A 1 88 ? 23.996 88.368 105.995 1.00 123.54 ? 87 ALA A N 1 +ATOM 660 C CA . ALA A 1 88 ? 25.072 89.257 106.423 1.00 108.38 ? 87 ALA A CA 1 +ATOM 661 C C . ALA A 1 88 ? 25.101 89.406 107.940 1.00 101.29 ? 87 ALA A C 1 +ATOM 662 O O . ALA A 1 88 ? 26.077 89.895 108.512 1.00 120.81 ? 87 ALA A O 1 +ATOM 663 C CB . ALA A 1 88 ? 24.922 90.621 105.756 1.00 105.43 ? 87 ALA A CB 1 +ATOM 664 N N . MET A 1 89 ? 24.022 88.974 108.579 1.00 97.25 ? 88 MET A N 1 +ATOM 665 C CA . MET A 1 89 ? 23.871 89.078 110.023 1.00 112.55 ? 88 MET A CA 1 +ATOM 666 C C . MET A 1 89 ? 24.672 87.973 110.718 1.00 101.19 ? 88 MET A C 1 +ATOM 667 O O . MET A 1 89 ? 25.051 86.994 110.078 1.00 114.66 ? 88 MET A O 1 +ATOM 668 C CB . MET A 1 89 ? 22.382 89.004 110.375 1.00 103.24 ? 88 MET A CB 1 +ATOM 669 C CG . MET A 1 89 ? 21.554 90.102 109.733 1.00 125.98 ? 88 MET A CG 1 +ATOM 670 S SD . MET A 1 89 ? 21.999 91.747 110.319 1.00 113.43 ? 88 MET A SD 1 +ATOM 671 C CE . MET A 1 89 ? 21.185 92.754 109.079 1.00 128.47 ? 88 MET A CE 1 +ATOM 672 N N . PRO A 1 90 ? 24.946 88.130 112.027 1.00 98.32 ? 89 PRO A N 1 +ATOM 673 C CA . PRO A 1 90 ? 24.528 89.242 112.891 1.00 129.82 ? 89 PRO A CA 1 +ATOM 674 C C . PRO A 1 90 ? 25.455 90.452 112.787 1.00 122.28 ? 89 PRO A C 1 +ATOM 675 O O . PRO A 1 90 ? 25.138 91.520 113.322 1.00 126.90 ? 89 PRO A O 1 +ATOM 676 C CB . PRO A 1 90 ? 24.621 88.634 114.288 1.00 112.51 ? 89 PRO A CB 1 +ATOM 677 C CG . PRO A 1 90 ? 25.781 87.699 114.178 1.00 111.54 ? 89 PRO A CG 1 +ATOM 678 C CD . PRO A 1 90 ? 25.747 87.140 112.771 1.00 104.43 ? 89 PRO A CD 1 +ATOM 679 N N . GLU A 1 91 ? 26.589 90.276 112.114 1.00 101.21 ? 90 GLU A N 1 +ATOM 680 C CA . GLU A 1 91 ? 27.584 91.334 111.999 1.00 124.90 ? 90 GLU A CA 1 +ATOM 681 C C . GLU A 1 91 ? 27.016 92.519 111.232 1.00 118.95 ? 90 GLU A C 1 +ATOM 682 O O . GLU A 1 91 ? 27.221 93.670 111.612 1.00 109.30 ? 90 GLU A O 1 +ATOM 683 C CB . GLU A 1 91 ? 28.864 90.812 111.342 1.00 152.00 ? 90 GLU A CB 1 +ATOM 684 C CG . GLU A 1 91 ? 29.515 89.665 112.105 1.00 163.55 ? 90 GLU A CG 1 +ATOM 685 C CD . GLU A 1 91 ? 31.030 89.692 112.035 1.00 181.32 ? 90 GLU A CD 1 +ATOM 686 O OE1 . GLU A 1 91 ? 31.652 90.439 112.824 1.00 170.29 ? 90 GLU A OE1 1 +ATOM 687 O OE2 . GLU A 1 91 ? 31.595 88.959 111.194 1.00 190.45 ? 90 GLU A OE2 1 +ATOM 688 N N . GLY A 1 92 ? 26.296 92.234 110.156 1.00 108.88 ? 91 GLY A N 1 +ATOM 689 C CA . GLY A 1 92 ? 25.572 93.273 109.454 1.00 102.88 ? 91 GLY A CA 1 +ATOM 690 C C . GLY A 1 92 ? 26.184 93.786 108.169 1.00 102.17 ? 91 GLY A C 1 +ATOM 691 O O . GLY A 1 92 ? 27.193 93.271 107.680 1.00 119.61 ? 91 GLY A O 1 +ATOM 692 N N . TYR A 1 93 ? 25.545 94.819 107.630 1.00 98.58 ? 92 TYR A N 1 +ATOM 693 C CA . TYR A 1 93 ? 25.937 95.420 106.364 1.00 108.11 ? 92 TYR A CA 1 +ATOM 694 C C . TYR A 1 93 ? 25.898 96.954 106.418 1.00 111.14 ? 92 TYR A C 1 +ATOM 695 O O . TYR A 1 93 ? 25.446 97.536 107.405 1.00 113.25 ? 92 TYR A O 1 +ATOM 696 C CB . TYR A 1 93 ? 25.055 94.883 105.225 1.00 92.06 ? 92 TYR A CB 1 +ATOM 697 C CG . TYR A 1 93 ? 23.551 95.139 105.347 1.00 114.68 ? 92 TYR A CG 1 +ATOM 698 C CD1 . TYR A 1 93 ? 23.000 96.374 105.013 1.00 132.67 ? 92 TYR A CD1 1 +ATOM 699 C CD2 . TYR A 1 93 ? 22.679 94.131 105.749 1.00 93.58 ? 92 TYR A CD2 1 +ATOM 700 C CE1 . TYR A 1 93 ? 21.622 96.607 105.104 1.00 123.60 ? 92 TYR A CE1 1 +ATOM 701 C CE2 . TYR A 1 93 ? 21.300 94.355 105.839 1.00 113.95 ? 92 TYR A CE2 1 +ATOM 702 C CZ . TYR A 1 93 ? 20.779 95.595 105.515 1.00 113.96 ? 92 TYR A CZ 1 +ATOM 703 O OH . TYR A 1 93 ? 19.420 95.826 105.602 1.00 117.14 ? 92 TYR A OH 1 +ATOM 704 N N . VAL A 1 94 ? 26.390 97.596 105.359 1.00 116.36 ? 93 VAL A N 1 +ATOM 705 C CA . VAL A 1 94 ? 26.347 99.054 105.219 1.00 115.82 ? 93 VAL A CA 1 +ATOM 706 C C . VAL A 1 94 ? 25.486 99.413 104.009 1.00 116.57 ? 93 VAL A C 1 +ATOM 707 O O . VAL A 1 94 ? 25.685 98.872 102.922 1.00 114.23 ? 93 VAL A O 1 +ATOM 708 C CB . VAL A 1 94 ? 27.762 99.662 105.005 1.00 117.35 ? 93 VAL A CB 1 +ATOM 709 C CG1 . VAL A 1 94 ? 27.694 101.189 104.949 1.00 105.65 ? 93 VAL A CG1 1 +ATOM 710 C CG2 . VAL A 1 94 ? 28.737 99.200 106.087 1.00 118.19 ? 93 VAL A CG2 1 +ATOM 711 N N . GLN A 1 95 ? 24.533 100.322 104.188 1.00 88.66 ? 94 GLN A N 1 +ATOM 712 C CA . GLN A 1 95 ? 23.631 100.682 103.099 1.00 104.40 ? 94 GLN A CA 1 +ATOM 713 C C . GLN A 1 95 ? 23.833 102.138 102.681 1.00 118.11 ? 94 GLN A C 1 +ATOM 714 O O . GLN A 1 95 ? 23.511 103.062 103.432 1.00 93.55 ? 94 GLN A O 1 +ATOM 715 C CB . GLN A 1 95 ? 22.172 100.407 103.494 1.00 92.91 ? 94 GLN A CB 1 +ATOM 716 C CG . GLN A 1 95 ? 21.146 100.773 102.432 1.00 86.28 ? 94 GLN A CG 1 +ATOM 717 C CD . GLN A 1 95 ? 19.741 100.256 102.734 1.00 104.11 ? 94 GLN A CD 1 +ATOM 718 O OE1 . GLN A 1 95 ? 19.525 99.055 102.902 1.00 97.97 ? 94 GLN A OE1 1 +ATOM 719 N NE2 . GLN A 1 95 ? 18.776 101.168 102.782 1.00 112.97 ? 94 GLN A NE2 1 +ATOM 720 N N . GLU A 1 96 ? 24.387 102.327 101.486 1.00 106.64 ? 95 GLU A N 1 +ATOM 721 C CA . GLU A 1 96 ? 24.625 103.657 100.936 1.00 79.24 ? 95 GLU A CA 1 +ATOM 722 C C . GLU A 1 96 ? 23.644 103.948 99.809 1.00 100.69 ? 95 GLU A C 1 +ATOM 723 O O . GLU A 1 96 ? 23.478 103.147 98.890 1.00 107.05 ? 95 GLU A O 1 +ATOM 724 C CB . GLU A 1 96 ? 26.067 103.784 100.426 1.00 112.16 ? 95 GLU A CB 1 +ATOM 725 C CG . GLU A 1 96 ? 27.113 104.024 101.521 1.00 143.86 ? 95 GLU A CG 1 +ATOM 726 C CD . GLU A 1 96 ? 28.555 103.820 101.040 1.00 180.17 ? 95 GLU A CD 1 +ATOM 727 O OE1 . GLU A 1 96 ? 28.842 102.769 100.430 1.00 187.67 ? 95 GLU A OE1 1 +ATOM 728 O OE2 . GLU A 1 96 ? 29.404 104.707 101.274 1.00 177.10 ? 95 GLU A OE2 1 +ATOM 729 N N . ARG A 1 97 ? 22.980 105.091 99.889 1.00 80.68 ? 96 ARG A N 1 +ATOM 730 C CA . ARG A 1 97 ? 22.071 105.484 98.830 1.00 100.66 ? 96 ARG A CA 1 +ATOM 731 C C . ARG A 1 97 ? 22.389 106.871 98.325 1.00 114.99 ? 96 ARG A C 1 +ATOM 732 O O . ARG A 1 97 ? 23.091 107.644 98.975 1.00 102.62 ? 96 ARG A O 1 +ATOM 733 C CB . ARG A 1 97 ? 20.622 105.468 99.310 1.00 77.57 ? 96 ARG A CB 1 +ATOM 734 C CG . ARG A 1 97 ? 19.991 104.103 99.364 1.00 125.08 ? 96 ARG A CG 1 +ATOM 735 C CD . ARG A 1 97 ? 18.502 104.180 99.060 1.00 103.24 ? 96 ARG A CD 1 +ATOM 736 N NE . ARG A 1 97 ? 17.822 102.948 99.441 1.00 114.10 ? 96 ARG A NE 1 +ATOM 737 C CZ . ARG A 1 97 ? 17.078 102.812 100.533 1.00 108.19 ? 96 ARG A CZ 1 +ATOM 738 N NH1 . ARG A 1 97 ? 16.895 103.841 101.351 1.00 116.71 ? 96 ARG A NH1 1 +ATOM 739 N NH2 . ARG A 1 97 ? 16.506 101.646 100.801 1.00 105.74 ? 96 ARG A NH2 1 +ATOM 740 N N . THR A 1 98 ? 21.863 107.167 97.146 1.00 102.15 ? 97 THR A N 1 +ATOM 741 C CA . THR A 1 98 ? 21.804 108.520 96.641 1.00 124.38 ? 97 THR A CA 1 +ATOM 742 C C . THR A 1 98 ? 20.388 108.694 96.098 1.00 107.47 ? 97 THR A C 1 +ATOM 743 O O . THR A 1 98 ? 19.876 107.838 95.377 1.00 88.63 ? 97 THR A O 1 +ATOM 744 C CB . THR A 1 98 ? 22.860 108.777 95.544 1.00 129.79 ? 97 THR A CB 1 +ATOM 745 O OG1 . THR A 1 98 ? 24.165 108.403 96.017 1.00 97.70 ? 97 THR A OG1 1 +ATOM 746 C CG2 . THR A 1 98 ? 22.862 110.246 95.152 1.00 73.96 ? 97 THR A CG2 1 +ATOM 747 N N . ILE A 1 99 ? 19.734 109.783 96.471 1.00 84.39 ? 98 ILE A N 1 +ATOM 748 C CA . ILE A 1 99 ? 18.336 109.944 96.115 1.00 104.76 ? 98 ILE A CA 1 +ATOM 749 C C . ILE A 1 99 ? 18.096 111.240 95.359 1.00 116.65 ? 98 ILE A C 1 +ATOM 750 O O . ILE A 1 99 ? 18.068 112.322 95.940 1.00 95.41 ? 98 ILE A O 1 +ATOM 751 C CB . ILE A 1 99 ? 17.450 109.879 97.364 1.00 90.98 ? 98 ILE A CB 1 +ATOM 752 C CG1 . ILE A 1 99 ? 17.744 108.583 98.129 1.00 70.12 ? 98 ILE A CG1 1 +ATOM 753 C CG2 . ILE A 1 99 ? 15.966 110.036 96.991 1.00 65.91 ? 98 ILE A CG2 1 +ATOM 754 C CD1 . ILE A 1 99 ? 17.115 108.507 99.488 1.00 86.67 ? 98 ILE A CD1 1 +ATOM 755 N N . PHE A 1 100 ? 17.928 111.120 94.051 1.00 90.35 ? 99 PHE A N 1 +ATOM 756 C CA . PHE A 1 100 ? 17.651 112.275 93.228 1.00 79.24 ? 99 PHE A CA 1 +ATOM 757 C C . PHE A 1 100 ? 16.152 112.504 93.172 1.00 84.59 ? 99 PHE A C 1 +ATOM 758 O O . PHE A 1 100 ? 15.422 111.675 92.649 1.00 91.15 ? 99 PHE A O 1 +ATOM 759 C CB . PHE A 1 100 ? 18.200 112.052 91.823 1.00 64.04 ? 99 PHE A CB 1 +ATOM 760 C CG . PHE A 1 100 ? 19.668 111.705 91.794 1.00 106.99 ? 99 PHE A CG 1 +ATOM 761 C CD1 . PHE A 1 100 ? 20.636 112.688 91.960 1.00 109.74 ? 99 PHE A CD1 1 +ATOM 762 C CD2 . PHE A 1 100 ? 20.084 110.398 91.595 1.00 113.71 ? 99 PHE A CD2 1 +ATOM 763 C CE1 . PHE A 1 100 ? 21.997 112.372 91.932 1.00 101.91 ? 99 PHE A CE1 1 +ATOM 764 C CE2 . PHE A 1 100 ? 21.444 110.076 91.565 1.00 99.07 ? 99 PHE A CE2 1 +ATOM 765 C CZ . PHE A 1 100 ? 22.399 111.065 91.735 1.00 92.68 ? 99 PHE A CZ 1 +ATOM 766 N N . PHE A 1 101 ? 15.682 113.612 93.733 1.00 80.56 ? 100 PHE A N 1 +ATOM 767 C CA . PHE A 1 101 ? 14.313 114.031 93.476 1.00 89.39 ? 100 PHE A CA 1 +ATOM 768 C C . PHE A 1 101 ? 14.360 114.814 92.172 1.00 96.63 ? 100 PHE A C 1 +ATOM 769 O O . PHE A 1 101 ? 15.300 115.562 91.914 1.00 96.88 ? 100 PHE A O 1 +ATOM 770 C CB . PHE A 1 101 ? 13.750 114.897 94.608 1.00 65.96 ? 100 PHE A CB 1 +ATOM 771 C CG . PHE A 1 101 ? 13.702 114.209 95.954 1.00 97.77 ? 100 PHE A CG 1 +ATOM 772 C CD1 . PHE A 1 101 ? 14.871 113.858 96.616 1.00 114.09 ? 100 PHE A CD1 1 +ATOM 773 C CD2 . PHE A 1 101 ? 12.490 113.951 96.576 1.00 104.41 ? 100 PHE A CD2 1 +ATOM 774 C CE1 . PHE A 1 101 ? 14.833 113.249 97.846 1.00 70.39 ? 100 PHE A CE1 1 +ATOM 775 C CE2 . PHE A 1 101 ? 12.452 113.341 97.810 1.00 94.45 ? 100 PHE A CE2 1 +ATOM 776 C CZ . PHE A 1 101 ? 13.623 112.991 98.441 1.00 101.76 ? 100 PHE A CZ 1 +ATOM 777 N N . LYS A 1 102 ? 13.363 114.627 91.328 1.00 86.06 ? 101 LYS A N 1 +ATOM 778 C CA . LYS A 1 102 ? 13.415 115.245 90.019 1.00 119.03 ? 101 LYS A CA 1 +ATOM 779 C C . LYS A 1 102 ? 13.107 116.726 90.153 1.00 134.71 ? 101 LYS A C 1 +ATOM 780 O O . LYS A 1 102 ? 12.176 117.095 90.876 1.00 89.27 ? 101 LYS A O 1 +ATOM 781 C CB . LYS A 1 102 ? 12.413 114.580 89.083 1.00 92.56 ? 101 LYS A CB 1 +ATOM 782 C CG . LYS A 1 102 ? 12.497 115.043 87.645 1.00 115.16 ? 101 LYS A CG 1 +ATOM 783 C CD . LYS A 1 102 ? 11.300 114.551 86.851 1.00 139.60 ? 101 LYS A CD 1 +ATOM 784 C CE . LYS A 1 102 ? 11.630 114.401 85.377 1.00 125.10 ? 101 LYS A CE 1 +ATOM 785 N NZ . LYS A 1 102 ? 10.647 115.124 84.528 1.00 140.19 ? 101 LYS A NZ 1 +ATOM 786 N N . ASP A 1 103 ? 13.893 117.553 89.458 1.00 113.65 ? 102 ASP A N 1 +ATOM 787 C CA . ASP A 1 103 ? 13.738 119.010 89.455 1.00 112.38 ? 102 ASP A CA 1 +ATOM 788 C C . ASP A 1 103 ? 13.992 119.588 90.832 1.00 106.25 ? 102 ASP A C 1 +ATOM 789 O O . ASP A 1 103 ? 13.364 120.574 91.219 1.00 108.88 ? 102 ASP A O 1 +ATOM 790 C CB . ASP A 1 103 ? 12.338 119.431 88.988 1.00 130.70 ? 102 ASP A CB 1 +ATOM 791 C CG . ASP A 1 103 ? 12.065 119.064 87.549 1.00 143.30 ? 102 ASP A CG 1 +ATOM 792 O OD1 . ASP A 1 103 ? 13.040 118.835 86.802 1.00 139.33 ? 102 ASP A OD1 1 +ATOM 793 O OD2 . ASP A 1 103 ? 10.873 119.013 87.168 1.00 135.90 ? 102 ASP A OD2 1 +ATOM 794 N N . ASP A 1 104 ? 14.904 118.970 91.572 1.00 92.07 ? 103 ASP A N 1 +ATOM 795 C CA . ASP A 1 104 ? 15.118 119.361 92.954 1.00 89.84 ? 103 ASP A CA 1 +ATOM 796 C C . ASP A 1 104 ? 16.351 118.680 93.535 1.00 98.14 ? 103 ASP A C 1 +ATOM 797 O O . ASP A 1 104 ? 17.096 118.008 92.820 1.00 76.74 ? 103 ASP A O 1 +ATOM 798 C CB . ASP A 1 104 ? 13.871 119.062 93.792 1.00 64.60 ? 103 ASP A CB 1 +ATOM 799 C CG . ASP A 1 104 ? 14.000 119.544 95.209 1.00 126.29 ? 103 ASP A CG 1 +ATOM 800 O OD1 . ASP A 1 104 ? 15.064 120.123 95.512 1.00 82.39 ? 103 ASP A OD1 1 +ATOM 801 O OD2 . ASP A 1 104 ? 13.075 119.363 96.007 1.00 215.86 ? 103 ASP A OD2 1 +ATOM 802 N N . GLY A 1 105 ? 16.563 118.861 94.836 1.00 96.95 ? 104 GLY A N 1 +ATOM 803 C CA . GLY A 1 105 ? 17.782 118.449 95.493 1.00 68.73 ? 104 GLY A CA 1 +ATOM 804 C C . GLY A 1 105 ? 17.947 116.952 95.681 1.00 110.26 ? 104 GLY A C 1 +ATOM 805 O O . GLY A 1 105 ? 17.136 116.157 95.207 1.00 101.45 ? 104 GLY A O 1 +ATOM 806 N N . ASN A 1 106 ? 19.003 116.561 96.385 1.00 89.36 ? 105 ASN A N 1 +ATOM 807 C CA . ASN A 1 106 ? 19.253 115.147 96.625 1.00 97.00 ? 105 ASN A CA 1 +ATOM 808 C C . ASN A 1 106 ? 19.655 114.828 98.061 1.00 114.12 ? 105 ASN A C 1 +ATOM 809 O O . ASN A 1 106 ? 20.213 115.677 98.758 1.00 107.40 ? 105 ASN A O 1 +ATOM 810 C CB . ASN A 1 106 ? 20.322 114.622 95.662 1.00 102.19 ? 105 ASN A CB 1 +ATOM 811 C CG . ASN A 1 106 ? 21.629 115.391 95.758 1.00 93.82 ? 105 ASN A CG 1 +ATOM 812 O OD1 . ASN A 1 106 ? 22.436 115.184 96.674 1.00 93.97 ? 105 ASN A OD1 1 +ATOM 813 N ND2 . ASN A 1 106 ? 21.850 116.279 94.799 1.00 88.34 ? 105 ASN A ND2 1 +ATOM 814 N N . TYR A 1 107 ? 19.361 113.601 98.495 1.00 92.99 ? 106 TYR A N 1 +ATOM 815 C CA . TYR A 1 107 ? 19.902 113.068 99.743 1.00 92.29 ? 106 TYR A CA 1 +ATOM 816 C C . TYR A 1 107 ? 21.087 112.140 99.453 1.00 99.60 ? 106 TYR A C 1 +ATOM 817 O O . TYR A 1 107 ? 21.113 111.436 98.442 1.00 77.48 ? 106 TYR A O 1 +ATOM 818 C CB . TYR A 1 107 ? 18.850 112.266 100.515 1.00 85.02 ? 106 TYR A CB 1 +ATOM 819 C CG . TYR A 1 107 ? 17.612 113.009 100.990 1.00 92.34 ? 106 TYR A CG 1 +ATOM 820 C CD1 . TYR A 1 107 ? 17.627 114.374 101.256 1.00 93.27 ? 106 TYR A CD1 1 +ATOM 821 C CD2 . TYR A 1 107 ? 16.425 112.320 101.199 1.00 102.47 ? 106 TYR A CD2 1 +ATOM 822 C CE1 . TYR A 1 107 ? 16.473 115.031 101.705 1.00 70.15 ? 106 TYR A CE1 1 +ATOM 823 C CE2 . TYR A 1 107 ? 15.283 112.959 101.640 1.00 69.55 ? 106 TYR A CE2 1 +ATOM 824 C CZ . TYR A 1 107 ? 15.304 114.310 101.890 1.00 96.76 ? 106 TYR A CZ 1 +ATOM 825 O OH . TYR A 1 107 ? 14.143 114.915 102.327 1.00 88.49 ? 106 TYR A OH 1 +ATOM 826 N N . LYS A 1 108 ? 22.070 112.134 100.341 1.00 82.30 ? 107 LYS A N 1 +ATOM 827 C CA . LYS A 1 108 ? 23.095 111.104 100.298 1.00 89.16 ? 107 LYS A CA 1 +ATOM 828 C C . LYS A 1 108 ? 23.242 110.523 101.695 1.00 106.95 ? 107 LYS A C 1 +ATOM 829 O O . LYS A 1 108 ? 23.541 111.242 102.650 1.00 112.14 ? 107 LYS A O 1 +ATOM 830 C CB . LYS A 1 108 ? 24.416 111.649 99.754 1.00 93.73 ? 107 LYS A CB 1 +ATOM 831 C CG . LYS A 1 108 ? 24.404 111.853 98.245 1.00 104.76 ? 107 LYS A CG 1 +ATOM 832 C CD . LYS A 1 108 ? 25.598 112.671 97.762 1.00 105.58 ? 107 LYS A CD 1 +ATOM 833 C CE . LYS A 1 108 ? 25.780 112.574 96.244 1.00 120.68 ? 107 LYS A CE 1 +ATOM 834 N NZ . LYS A 1 108 ? 26.061 111.172 95.789 1.00 119.87 ? 107 LYS A NZ 1 +ATOM 835 N N . THR A 1 109 ? 22.994 109.221 101.807 1.00 104.39 ? 108 THR A N 1 +ATOM 836 C CA . THR A 1 109 ? 22.913 108.559 103.101 1.00 104.01 ? 108 THR A CA 1 +ATOM 837 C C . THR A 1 109 ? 23.934 107.441 103.238 1.00 104.72 ? 108 THR A C 1 +ATOM 838 O O . THR A 1 109 ? 24.424 106.900 102.248 1.00 77.55 ? 108 THR A O 1 +ATOM 839 C CB . THR A 1 109 ? 21.513 107.950 103.345 1.00 98.37 ? 108 THR A CB 1 +ATOM 840 O OG1 . THR A 1 109 ? 21.358 106.760 102.558 1.00 87.36 ? 108 THR A OG1 1 +ATOM 841 C CG2 . THR A 1 109 ? 20.410 108.950 103.004 1.00 106.98 ? 108 THR A CG2 1 +ATOM 842 N N . ARG A 1 110 ? 24.254 107.116 104.485 1.00 88.33 ? 109 ARG A N 1 +ATOM 843 C CA . ARG A 1 110 ? 25.058 105.949 104.807 1.00 88.47 ? 109 ARG A CA 1 +ATOM 844 C C . ARG A 1 110 ? 24.630 105.402 106.162 1.00 89.52 ? 109 ARG A C 1 +ATOM 845 O O . ARG A 1 110 ? 24.807 106.053 107.194 1.00 85.12 ? 109 ARG A O 1 +ATOM 846 C CB . ARG A 1 110 ? 26.553 106.268 104.823 1.00 91.62 ? 109 ARG A CB 1 +ATOM 847 C CG . ARG A 1 110 ? 27.385 105.091 105.295 1.00 117.00 ? 109 ARG A CG 1 +ATOM 848 C CD . ARG A 1 110 ? 28.798 105.480 105.670 1.00 86.32 ? 109 ARG A CD 1 +ATOM 849 N NE . ARG A 1 110 ? 29.638 104.298 105.847 1.00 116.03 ? 109 ARG A NE 1 +ATOM 850 C CZ . ARG A 1 110 ? 29.889 103.715 107.017 1.00 126.32 ? 109 ARG A CZ 1 +ATOM 851 N NH1 . ARG A 1 110 ? 29.374 104.205 108.139 1.00 131.14 ? 109 ARG A NH1 1 +ATOM 852 N NH2 . ARG A 1 110 ? 30.665 102.639 107.065 1.00 116.44 ? 109 ARG A NH2 1 +ATOM 853 N N . ALA A 1 111 ? 24.063 104.199 106.131 1.00 109.42 ? 110 ALA A N 1 +ATOM 854 C CA . ALA A 1 111 ? 23.583 103.506 107.318 1.00 91.00 ? 110 ALA A CA 1 +ATOM 855 C C . ALA A 1 111 ? 24.395 102.246 107.616 1.00 107.31 ? 110 ALA A C 1 +ATOM 856 O O . ALA A 1 111 ? 24.912 101.599 106.703 1.00 90.78 ? 110 ALA A O 1 +ATOM 857 C CB . ALA A 1 111 ? 22.116 103.147 107.151 1.00 103.36 ? 110 ALA A CB 1 +ATOM 858 N N . GLU A 1 112 ? 24.520 101.920 108.901 1.00 91.38 ? 111 GLU A N 1 +ATOM 859 C CA . GLU A 1 112 ? 24.998 100.608 109.321 1.00 103.65 ? 111 GLU A CA 1 +ATOM 860 C C . GLU A 1 112 ? 23.828 99.855 109.948 1.00 121.16 ? 111 GLU A C 1 +ATOM 861 O O . GLU A 1 112 ? 23.259 100.298 110.951 1.00 121.49 ? 111 GLU A O 1 +ATOM 862 C CB . GLU A 1 112 ? 26.161 100.723 110.318 1.00 118.40 ? 111 GLU A CB 1 +ATOM 863 C CG . GLU A 1 112 ? 27.462 101.249 109.712 1.00 161.05 ? 111 GLU A CG 1 +ATOM 864 C CD . GLU A 1 112 ? 28.595 101.468 110.729 1.00 165.91 ? 111 GLU A CD 1 +ATOM 865 O OE1 . GLU A 1 112 ? 28.415 101.221 111.948 1.00 131.75 ? 111 GLU A OE1 1 +ATOM 866 O OE2 . GLU A 1 112 ? 29.682 101.898 110.284 1.00 160.29 ? 111 GLU A OE2 1 +ATOM 867 N N . VAL A 1 113 ? 23.449 98.739 109.334 1.00 110.85 ? 112 VAL A N 1 +ATOM 868 C CA . VAL A 1 113 ? 22.416 97.882 109.900 1.00 101.59 ? 112 VAL A CA 1 +ATOM 869 C C . VAL A 1 113 ? 23.044 96.628 110.482 1.00 107.04 ? 112 VAL A C 1 +ATOM 870 O O . VAL A 1 113 ? 23.698 95.864 109.774 1.00 96.83 ? 112 VAL A O 1 +ATOM 871 C CB . VAL A 1 113 ? 21.365 97.475 108.867 1.00 73.95 ? 112 VAL A CB 1 +ATOM 872 C CG1 . VAL A 1 113 ? 20.158 96.909 109.575 1.00 105.18 ? 112 VAL A CG1 1 +ATOM 873 C CG2 . VAL A 1 113 ? 20.958 98.671 108.047 1.00 112.89 ? 112 VAL A CG2 1 +ATOM 874 N N . LYS A 1 114 ? 22.848 96.430 111.780 1.00 83.26 ? 113 LYS A N 1 +ATOM 875 C CA . LYS A 1 114 ? 23.421 95.283 112.472 1.00 103.50 ? 113 LYS A CA 1 +ATOM 876 C C . LYS A 1 114 ? 22.701 94.978 113.785 1.00 116.31 ? 113 LYS A C 1 +ATOM 877 O O . LYS A 1 114 ? 21.793 95.701 114.208 1.00 97.22 ? 113 LYS A O 1 +ATOM 878 C CB . LYS A 1 114 ? 24.930 95.476 112.709 1.00 129.42 ? 113 LYS A CB 1 +ATOM 879 C CG . LYS A 1 114 ? 25.324 96.750 113.479 1.00 130.23 ? 113 LYS A CG 1 +ATOM 880 C CD . LYS A 1 114 ? 26.845 96.875 113.688 1.00 114.91 ? 113 LYS A CD 1 +ATOM 881 C CE . LYS A 1 114 ? 27.195 97.990 114.681 1.00 132.81 ? 113 LYS A CE 1 +ATOM 882 N NZ . LYS A 1 114 ? 26.997 99.353 114.117 1.00 119.85 ? 113 LYS A NZ 1 +ATOM 883 N N . PHE A 1 115 ? 23.116 93.895 114.426 1.00 97.97 ? 114 PHE A N 1 +ATOM 884 C CA . PHE A 1 115 ? 22.493 93.461 115.661 1.00 103.61 ? 114 PHE A CA 1 +ATOM 885 C C . PHE A 1 115 ? 23.286 93.962 116.847 1.00 103.83 ? 114 PHE A C 1 +ATOM 886 O O . PHE A 1 115 ? 24.506 93.850 116.874 1.00 109.66 ? 114 PHE A O 1 +ATOM 887 C CB . PHE A 1 115 ? 22.412 91.935 115.709 1.00 131.60 ? 114 PHE A CB 1 +ATOM 888 C CG . PHE A 1 115 ? 21.090 91.381 115.256 1.00 134.35 ? 114 PHE A CG 1 +ATOM 889 C CD1 . PHE A 1 115 ? 20.045 91.222 116.157 1.00 115.73 ? 114 PHE A CD1 1 +ATOM 890 C CD2 . PHE A 1 115 ? 20.891 91.021 113.934 1.00 109.63 ? 114 PHE A CD2 1 +ATOM 891 C CE1 . PHE A 1 115 ? 18.828 90.714 115.749 1.00 103.37 ? 114 PHE A CE1 1 +ATOM 892 C CE2 . PHE A 1 115 ? 19.679 90.513 113.518 1.00 88.02 ? 114 PHE A CE2 1 +ATOM 893 C CZ . PHE A 1 115 ? 18.644 90.358 114.427 1.00 104.15 ? 114 PHE A CZ 1 +ATOM 894 N N . GLU A 1 116 ? 22.592 94.519 117.830 1.00 96.02 ? 115 GLU A N 1 +ATOM 895 C CA . GLU A 1 116 ? 23.239 94.896 119.075 1.00 91.26 ? 115 GLU A CA 1 +ATOM 896 C C . GLU A 1 116 ? 22.545 94.179 120.221 1.00 98.04 ? 115 GLU A C 1 +ATOM 897 O O . GLU A 1 116 ? 21.686 94.740 120.907 1.00 93.74 ? 115 GLU A O 1 +ATOM 898 C CB . GLU A 1 116 ? 23.211 96.407 119.272 1.00 108.85 ? 115 GLU A CB 1 +ATOM 899 C CG . GLU A 1 116 ? 24.103 97.173 118.324 1.00 120.65 ? 115 GLU A CG 1 +ATOM 900 C CD . GLU A 1 116 ? 24.105 98.663 118.604 1.00 157.54 ? 115 GLU A CD 1 +ATOM 901 O OE1 . GLU A 1 116 ? 23.441 99.087 119.577 1.00 151.84 ? 115 GLU A OE1 1 +ATOM 902 O OE2 . GLU A 1 116 ? 24.773 99.404 117.848 1.00 142.77 ? 115 GLU A OE2 1 +ATOM 903 N N . GLY A 1 117 ? 22.923 92.921 120.409 1.00 107.91 ? 116 GLY A N 1 +ATOM 904 C CA . GLY A 1 117 ? 22.233 92.049 121.334 1.00 96.43 ? 116 GLY A CA 1 +ATOM 905 C C . GLY A 1 117 ? 21.026 91.444 120.649 1.00 121.36 ? 116 GLY A C 1 +ATOM 906 O O . GLY A 1 117 ? 21.125 90.924 119.532 1.00 96.63 ? 116 GLY A O 1 +ATOM 907 N N . ASP A 1 118 ? 19.877 91.530 121.313 1.00 144.00 ? 117 ASP A N 1 +ATOM 908 C CA . ASP A 1 118 ? 18.638 91.008 120.753 1.00 136.18 ? 117 ASP A CA 1 +ATOM 909 C C . ASP A 1 118 ? 17.990 91.994 119.776 1.00 123.16 ? 117 ASP A C 1 +ATOM 910 O O . ASP A 1 118 ? 16.986 91.673 119.146 1.00 114.79 ? 117 ASP A O 1 +ATOM 911 C CB . ASP A 1 118 ? 17.648 90.577 121.861 1.00 134.33 ? 117 ASP A CB 1 +ATOM 912 C CG . ASP A 1 118 ? 17.056 91.762 122.644 1.00 159.13 ? 117 ASP A CG 1 +ATOM 913 O OD1 . ASP A 1 118 ? 17.815 92.694 122.991 1.00 146.95 ? 117 ASP A OD1 1 +ATOM 914 O OD2 . ASP A 1 118 ? 15.830 91.755 122.922 1.00 139.64 ? 117 ASP A OD2 1 +ATOM 915 N N . THR A 1 119 ? 18.569 93.183 119.629 1.00 116.23 ? 118 THR A N 1 +ATOM 916 C CA . THR A 1 119 ? 17.941 94.209 118.793 1.00 109.61 ? 118 THR A CA 1 +ATOM 917 C C . THR A 1 119 ? 18.646 94.468 117.444 1.00 105.84 ? 118 THR A C 1 +ATOM 918 O O . THR A 1 119 ? 19.874 94.387 117.332 1.00 103.54 ? 118 THR A O 1 +ATOM 919 C CB . THR A 1 119 ? 17.688 95.527 119.596 1.00 87.66 ? 118 THR A CB 1 +ATOM 920 O OG1 . THR A 1 119 ? 16.913 95.231 120.767 1.00 99.08 ? 118 THR A OG1 1 +ATOM 921 C CG2 . THR A 1 119 ? 16.936 96.561 118.765 1.00 85.54 ? 118 THR A CG2 1 +ATOM 922 N N . LEU A 1 120 ? 17.830 94.733 116.422 1.00 102.10 ? 119 LEU A N 1 +ATOM 923 C CA . LEU A 1 120 ? 18.287 95.141 115.099 1.00 73.79 ? 119 LEU A CA 1 +ATOM 924 C C . LEU A 1 120 ? 18.247 96.662 115.019 1.00 106.17 ? 119 LEU A C 1 +ATOM 925 O O . LEU A 1 120 ? 17.174 97.275 115.066 1.00 80.13 ? 119 LEU A O 1 +ATOM 926 C CB . LEU A 1 120 ? 17.394 94.525 114.019 1.00 67.02 ? 119 LEU A CB 1 +ATOM 927 C CG . LEU A 1 120 ? 17.754 94.640 112.534 1.00 61.58 ? 119 LEU A CG 1 +ATOM 928 C CD1 . LEU A 1 120 ? 17.303 93.413 111.831 1.00 143.37 ? 119 LEU A CD1 1 +ATOM 929 C CD2 . LEU A 1 120 ? 17.131 95.867 111.906 1.00 75.00 ? 119 LEU A CD2 1 +ATOM 930 N N . VAL A 1 121 ? 19.428 97.263 114.912 1.00 95.78 ? 120 VAL A N 1 +ATOM 931 C CA . VAL A 1 121 ? 19.544 98.711 114.895 1.00 81.79 ? 120 VAL A CA 1 +ATOM 932 C C . VAL A 1 121 ? 19.929 99.260 113.513 1.00 106.59 ? 120 VAL A C 1 +ATOM 933 O O . VAL A 1 121 ? 20.771 98.695 112.805 1.00 90.15 ? 120 VAL A O 1 +ATOM 934 C CB . VAL A 1 121 ? 20.525 99.219 115.988 1.00 101.44 ? 120 VAL A CB 1 +ATOM 935 C CG1 . VAL A 1 121 ? 20.138 98.670 117.358 1.00 76.27 ? 120 VAL A CG1 1 +ATOM 936 C CG2 . VAL A 1 121 ? 21.951 98.827 115.661 1.00 124.92 ? 120 VAL A CG2 1 +ATOM 937 N N . ASN A 1 122 ? 19.280 100.357 113.132 1.00 92.85 ? 121 ASN A N 1 +ATOM 938 C CA . ASN A 1 122 ? 19.629 101.089 111.921 1.00 96.02 ? 121 ASN A CA 1 +ATOM 939 C C . ASN A 1 122 ? 20.194 102.468 112.250 1.00 110.99 ? 121 ASN A C 1 +ATOM 940 O O . ASN A 1 122 ? 19.476 103.327 112.767 1.00 91.10 ? 121 ASN A O 1 +ATOM 941 C CB . ASN A 1 122 ? 18.406 101.253 111.029 1.00 62.96 ? 121 ASN A CB 1 +ATOM 942 C CG . ASN A 1 122 ? 18.773 101.642 109.623 1.00 80.50 ? 121 ASN A CG 1 +ATOM 943 O OD1 . ASN A 1 122 ? 19.919 101.482 109.210 1.00 126.48 ? 121 ASN A OD1 1 +ATOM 944 N ND2 . ASN A 1 122 ? 17.804 102.150 108.873 1.00 92.09 ? 121 ASN A ND2 1 +ATOM 945 N N . ARG A 1 123 ? 21.475 102.676 111.949 1.00 93.98 ? 122 ARG A N 1 +ATOM 946 C CA . ARG A 1 123 ? 22.142 103.943 112.253 1.00 94.28 ? 122 ARG A CA 1 +ATOM 947 C C . ARG A 1 123 ? 22.511 104.765 111.020 1.00 102.20 ? 122 ARG A C 1 +ATOM 948 O O . ARG A 1 123 ? 23.381 104.386 110.240 1.00 88.61 ? 122 ARG A O 1 +ATOM 949 C CB . ARG A 1 123 ? 23.377 103.716 113.121 1.00 96.59 ? 122 ARG A CB 1 +ATOM 950 C CG . ARG A 1 123 ? 23.066 103.532 114.589 1.00 91.81 ? 122 ARG A CG 1 +ATOM 951 C CD . ARG A 1 123 ? 24.337 103.598 115.417 1.00 105.63 ? 122 ARG A CD 1 +ATOM 952 N NE . ARG A 1 123 ? 24.313 102.651 116.528 1.00 123.34 ? 122 ARG A NE 1 +ATOM 953 C CZ . ARG A 1 123 ? 23.659 102.849 117.666 1.00 134.18 ? 122 ARG A CZ 1 +ATOM 954 N NH1 . ARG A 1 123 ? 22.961 103.966 117.852 1.00 108.81 ? 122 ARG A NH1 1 +ATOM 955 N NH2 . ARG A 1 123 ? 23.699 101.924 118.617 1.00 123.22 ? 122 ARG A NH2 1 +ATOM 956 N N . ILE A 1 124 ? 21.870 105.925 110.900 1.00 104.42 ? 123 ILE A N 1 +ATOM 957 C CA . ILE A 1 124 ? 21.851 106.696 109.662 1.00 98.83 ? 123 ILE A CA 1 +ATOM 958 C C . ILE A 1 124 ? 22.449 108.109 109.770 1.00 105.33 ? 123 ILE A C 1 +ATOM 959 O O . ILE A 1 124 ? 22.123 108.871 110.683 1.00 79.27 ? 123 ILE A O 1 +ATOM 960 C CB . ILE A 1 124 ? 20.394 106.805 109.153 1.00 114.52 ? 123 ILE A CB 1 +ATOM 961 C CG1 . ILE A 1 124 ? 19.603 105.551 109.524 1.00 99.94 ? 123 ILE A CG1 1 +ATOM 962 C CG2 . ILE A 1 124 ? 20.348 107.092 107.646 1.00 76.69 ? 123 ILE A CG2 1 +ATOM 963 C CD1 . ILE A 1 124 ? 18.117 105.661 109.304 1.00 109.08 ? 123 ILE A CD1 1 +ATOM 964 N N . GLU A 1 125 ? 23.331 108.434 108.825 1.00 106.85 ? 124 GLU A N 1 +ATOM 965 C CA . GLU A 1 125 ? 23.747 109.812 108.550 1.00 94.30 ? 124 GLU A CA 1 +ATOM 966 C C . GLU A 1 125 ? 23.214 110.227 107.171 1.00 99.06 ? 124 GLU A C 1 +ATOM 967 O O . GLU A 1 125 ? 23.490 109.554 106.177 1.00 104.78 ? 124 GLU A O 1 +ATOM 968 C CB . GLU A 1 125 ? 25.275 109.926 108.545 1.00 97.38 ? 124 GLU A CB 1 +ATOM 969 C CG . GLU A 1 125 ? 25.950 109.516 109.835 1.00 135.84 ? 124 GLU A CG 1 +ATOM 970 C CD . GLU A 1 125 ? 27.466 109.570 109.750 1.00 160.27 ? 124 GLU A CD 1 +ATOM 971 O OE1 . GLU A 1 125 ? 28.061 108.879 108.893 1.00 175.56 ? 124 GLU A OE1 1 +ATOM 972 O OE2 . GLU A 1 125 ? 28.062 110.310 110.552 1.00 143.57 ? 124 GLU A OE2 1 +ATOM 973 N N . LEU A 1 126 ? 22.457 111.326 107.112 1.00 89.44 ? 125 LEU A N 1 +ATOM 974 C CA . LEU A 1 126 ? 21.877 111.827 105.853 1.00 104.14 ? 125 LEU A CA 1 +ATOM 975 C C . LEU A 1 126 ? 22.256 113.294 105.597 1.00 105.76 ? 125 LEU A C 1 +ATOM 976 O O . LEU A 1 126 ? 22.354 114.082 106.540 1.00 101.28 ? 125 LEU A O 1 +ATOM 977 C CB . LEU A 1 126 ? 20.351 111.644 105.859 1.00 82.08 ? 125 LEU A CB 1 +ATOM 978 C CG . LEU A 1 126 ? 19.468 112.434 104.886 1.00 75.49 ? 125 LEU A CG 1 +ATOM 979 C CD1 . LEU A 1 126 ? 18.253 111.638 104.501 1.00 88.16 ? 125 LEU A CD1 1 +ATOM 980 C CD2 . LEU A 1 126 ? 19.006 113.744 105.491 1.00 103.45 ? 125 LEU A CD2 1 +ATOM 981 N N . LYS A 1 127 ? 22.456 113.657 104.326 1.00 107.74 ? 126 LYS A N 1 +ATOM 982 C CA . LYS A 1 127 ? 22.949 114.995 103.963 1.00 84.69 ? 126 LYS A CA 1 +ATOM 983 C C . LYS A 1 127 ? 22.375 115.568 102.658 1.00 93.46 ? 126 LYS A C 1 +ATOM 984 O O . LYS A 1 127 ? 22.898 115.303 101.574 1.00 113.98 ? 126 LYS A O 1 +ATOM 985 C CB . LYS A 1 127 ? 24.481 114.990 103.881 1.00 99.48 ? 126 LYS A CB 1 +ATOM 986 C CG . LYS A 1 127 ? 25.070 116.332 103.495 1.00 125.92 ? 126 LYS A CG 1 +ATOM 987 C CD . LYS A 1 127 ? 26.519 116.493 103.912 1.00 139.54 ? 126 LYS A CD 1 +ATOM 988 C CE . LYS A 1 127 ? 26.940 117.928 103.670 1.00 127.49 ? 126 LYS A CE 1 +ATOM 989 N NZ . LYS A 1 127 ? 25.794 118.838 103.976 1.00 112.63 ? 126 LYS A NZ 1 +ATOM 990 N N . GLY A 1 128 ? 21.321 116.375 102.771 1.00 111.64 ? 127 GLY A N 1 +ATOM 991 C CA . GLY A 1 128 ? 20.668 116.974 101.610 1.00 106.54 ? 127 GLY A CA 1 +ATOM 992 C C . GLY A 1 128 ? 21.187 118.343 101.183 1.00 118.38 ? 127 GLY A C 1 +ATOM 993 O O . GLY A 1 128 ? 21.513 119.182 102.022 1.00 124.70 ? 127 GLY A O 1 +ATOM 994 N N . ILE A 1 129 ? 21.269 118.561 99.869 1.00 130.99 ? 128 ILE A N 1 +ATOM 995 C CA . ILE A 1 129 ? 21.759 119.818 99.284 1.00 109.14 ? 128 ILE A CA 1 +ATOM 996 C C . ILE A 1 129 ? 20.982 120.151 98.010 1.00 93.03 ? 128 ILE A C 1 +ATOM 997 O O . ILE A 1 129 ? 20.420 119.262 97.377 1.00 114.74 ? 128 ILE A O 1 +ATOM 998 C CB . ILE A 1 129 ? 23.273 119.737 98.913 1.00 95.35 ? 128 ILE A CB 1 +ATOM 999 C CG1 . ILE A 1 129 ? 24.140 119.574 100.164 1.00 143.94 ? 128 ILE A CG1 1 +ATOM 1000 C CG2 . ILE A 1 129 ? 23.731 120.954 98.093 1.00 166.52 ? 128 ILE A CG2 1 +ATOM 1001 C CD1 . ILE A 1 129 ? 24.593 118.150 100.421 1.00 138.26 ? 128 ILE A CD1 1 +ATOM 1002 N N . ASP A 1 130 ? 20.946 121.432 97.643 1.00 125.01 ? 129 ASP A N 1 +ATOM 1003 C CA . ASP A 1 130 ? 20.419 121.891 96.353 1.00 127.83 ? 129 ASP A CA 1 +ATOM 1004 C C . ASP A 1 130 ? 18.905 121.851 96.253 1.00 81.65 ? 129 ASP A C 1 +ATOM 1005 O O . ASP A 1 130 ? 18.351 121.826 95.163 1.00 79.19 ? 129 ASP A O 1 +ATOM 1006 C CB . ASP A 1 130 ? 21.039 121.139 95.162 1.00 115.17 ? 129 ASP A CB 1 +ATOM 1007 C CG . ASP A 1 130 ? 22.537 121.319 95.074 1.00 128.98 ? 129 ASP A CG 1 +ATOM 1008 O OD1 . ASP A 1 130 ? 23.003 122.472 95.210 1.00 106.90 ? 129 ASP A OD1 1 +ATOM 1009 O OD2 . ASP A 1 130 ? 23.245 120.304 94.887 1.00 132.82 ? 129 ASP A OD2 1 +ATOM 1010 N N . PHE A 1 131 ? 18.220 121.868 97.381 1.00 77.06 ? 130 PHE A N 1 +ATOM 1011 C CA . PHE A 1 131 ? 16.773 121.920 97.296 1.00 110.74 ? 130 PHE A CA 1 +ATOM 1012 C C . PHE A 1 131 ? 16.295 123.353 97.006 1.00 81.88 ? 130 PHE A C 1 +ATOM 1013 O O . PHE A 1 131 ? 17.035 124.307 97.207 1.00 104.40 ? 130 PHE A O 1 +ATOM 1014 C CB . PHE A 1 131 ? 16.131 121.277 98.535 1.00 98.67 ? 130 PHE A CB 1 +ATOM 1015 C CG . PHE A 1 131 ? 16.326 119.777 98.600 1.00 91.59 ? 130 PHE A CG 1 +ATOM 1016 C CD1 . PHE A 1 131 ? 17.519 119.231 99.070 1.00 105.89 ? 130 PHE A CD1 1 +ATOM 1017 C CD2 . PHE A 1 131 ? 15.334 118.915 98.154 1.00 93.03 ? 130 PHE A CD2 1 +ATOM 1018 C CE1 . PHE A 1 131 ? 17.714 117.851 99.105 1.00 69.37 ? 130 PHE A CE1 1 +ATOM 1019 C CE2 . PHE A 1 131 ? 15.516 117.537 98.185 1.00 77.39 ? 130 PHE A CE2 1 +ATOM 1020 C CZ . PHE A 1 131 ? 16.708 117.005 98.665 1.00 111.78 ? 130 PHE A CZ 1 +ATOM 1021 N N . LYS A 1 132 ? 15.077 123.494 96.500 1.00 79.96 ? 131 LYS A N 1 +ATOM 1022 C CA . LYS A 1 132 ? 14.529 124.802 96.167 1.00 92.49 ? 131 LYS A CA 1 +ATOM 1023 C C . LYS A 1 132 ? 13.567 125.260 97.239 1.00 94.33 ? 131 LYS A C 1 +ATOM 1024 O O . LYS A 1 132 ? 12.474 124.719 97.314 1.00 161.62 ? 131 LYS A O 1 +ATOM 1025 C CB . LYS A 1 132 ? 13.704 124.703 94.892 1.00 68.89 ? 131 LYS A CB 1 +ATOM 1026 C CG . LYS A 1 132 ? 14.356 123.998 93.731 1.00 86.73 ? 131 LYS A CG 1 +ATOM 1027 C CD . LYS A 1 132 ? 13.369 123.953 92.584 1.00 95.33 ? 131 LYS A CD 1 +ATOM 1028 C CE . LYS A 1 132 ? 14.036 123.623 91.272 1.00 118.50 ? 131 LYS A CE 1 +ATOM 1029 N NZ . LYS A 1 132 ? 12.994 123.413 90.224 1.00 119.08 ? 131 LYS A NZ 1 +ATOM 1030 N N . GLU A 1 133 ? 13.929 126.285 98.013 1.00 105.78 ? 132 GLU A N 1 +ATOM 1031 C CA . GLU A 1 133 ? 13.084 126.809 99.106 1.00 134.53 ? 132 GLU A CA 1 +ATOM 1032 C C . GLU A 1 133 ? 11.568 126.885 98.809 1.00 119.07 ? 132 GLU A C 1 +ATOM 1033 O O . GLU A 1 133 ? 10.752 126.967 99.724 1.00 107.24 ? 132 GLU A O 1 +ATOM 1034 C CB . GLU A 1 133 ? 13.603 128.175 99.617 1.00 106.06 ? 132 GLU A CB 1 +ATOM 1035 C CG . GLU A 1 133 ? 14.897 128.134 100.489 1.00 212.95 ? 132 GLU A CG 1 +ATOM 1036 C CD . GLU A 1 133 ? 14.671 127.875 102.005 1.00 192.48 ? 132 GLU A CD 1 +ATOM 1037 O OE1 . GLU A 1 133 ? 13.672 128.367 102.582 1.00 184.99 ? 132 GLU A OE1 1 +ATOM 1038 O OE2 . GLU A 1 133 ? 15.516 127.186 102.629 1.00 146.79 ? 132 GLU A OE2 1 +ATOM 1039 N N . ASP A 1 134 ? 11.195 126.835 97.536 1.00 100.91 ? 133 ASP A N 1 +ATOM 1040 C CA . ASP A 1 134 ? 9.788 126.867 97.151 1.00 103.80 ? 133 ASP A CA 1 +ATOM 1041 C C . ASP A 1 134 ? 9.316 125.533 96.580 1.00 124.34 ? 133 ASP A C 1 +ATOM 1042 O O . ASP A 1 134 ? 8.173 125.415 96.140 1.00 128.40 ? 133 ASP A O 1 +ATOM 1043 C CB . ASP A 1 134 ? 9.567 127.961 96.111 1.00 164.36 ? 133 ASP A CB 1 +ATOM 1044 C CG . ASP A 1 134 ? 10.627 127.947 95.026 1.00 189.78 ? 133 ASP A CG 1 +ATOM 1045 O OD1 . ASP A 1 134 ? 11.804 127.678 95.357 1.00 188.32 ? 133 ASP A OD1 1 +ATOM 1046 O OD2 . ASP A 1 134 ? 10.284 128.192 93.848 1.00 200.08 ? 133 ASP A OD2 1 +ATOM 1047 N N . GLY A 1 135 ? 10.198 124.537 96.592 1.00 140.10 ? 134 GLY A N 1 +ATOM 1048 C CA . GLY A 1 135 ? 9.921 123.262 95.965 1.00 135.42 ? 134 GLY A CA 1 +ATOM 1049 C C . GLY A 1 135 ? 8.823 122.399 96.575 1.00 135.06 ? 134 GLY A C 1 +ATOM 1050 O O . GLY A 1 135 ? 7.965 122.887 97.315 1.00 121.18 ? 134 GLY A O 1 +ATOM 1051 N N . ASN A 1 136 ? 8.837 121.111 96.236 1.00 132.82 ? 135 ASN A N 1 +ATOM 1052 C CA . ASN A 1 136 ? 7.869 120.162 96.782 1.00 90.94 ? 135 ASN A CA 1 +ATOM 1053 C C . ASN A 1 136 ? 8.288 119.713 98.194 1.00 111.98 ? 135 ASN A C 1 +ATOM 1054 O O . ASN A 1 136 ? 7.469 119.671 99.120 1.00 97.54 ? 135 ASN A O 1 +ATOM 1055 C CB . ASN A 1 136 ? 7.692 118.955 95.843 1.00 102.20 ? 135 ASN A CB 1 +ATOM 1056 C CG . ASN A 1 136 ? 6.830 119.265 94.608 1.00 107.25 ? 135 ASN A CG 1 +ATOM 1057 O OD1 . ASN A 1 136 ? 5.945 120.130 94.637 1.00 72.59 ? 135 ASN A OD1 1 +ATOM 1058 N ND2 . ASN A 1 136 ? 7.079 118.529 93.525 1.00 76.43 ? 135 ASN A ND2 1 +ATOM 1059 N N . ILE A 1 137 ? 9.570 119.391 98.346 1.00 94.91 ? 136 ILE A N 1 +ATOM 1060 C CA . ILE A 1 137 ? 10.159 119.085 99.651 1.00 112.68 ? 136 ILE A CA 1 +ATOM 1061 C C . ILE A 1 137 ? 10.039 120.285 100.594 1.00 123.74 ? 136 ILE A C 1 +ATOM 1062 O O . ILE A 1 137 ? 9.072 120.389 101.362 1.00 92.23 ? 136 ILE A O 1 +ATOM 1063 C CB . ILE A 1 137 ? 11.664 118.678 99.549 1.00 91.37 ? 136 ILE A CB 1 +ATOM 1064 C CG1 . ILE A 1 137 ? 11.840 117.355 98.805 1.00 65.00 ? 136 ILE A CG1 1 +ATOM 1065 C CG2 . ILE A 1 137 ? 12.294 118.518 100.934 1.00 54.28 ? 136 ILE A CG2 1 +ATOM 1066 C CD1 . ILE A 1 137 ? 11.689 117.431 97.323 1.00 98.17 ? 136 ILE A CD1 1 +ATOM 1067 N N . LEU A 1 138 ? 11.004 121.203 100.493 1.00 107.89 ? 137 LEU A N 1 +ATOM 1068 C CA . LEU A 1 138 ? 11.192 122.269 101.472 1.00 112.94 ? 137 LEU A CA 1 +ATOM 1069 C C . LEU A 1 138 ? 9.993 123.183 101.581 1.00 116.45 ? 137 LEU A C 1 +ATOM 1070 O O . LEU A 1 138 ? 9.879 123.949 102.536 1.00 85.71 ? 137 LEU A O 1 +ATOM 1071 C CB . LEU A 1 138 ? 12.447 123.078 101.160 1.00 88.27 ? 137 LEU A CB 1 +ATOM 1072 C CG . LEU A 1 138 ? 13.728 122.319 101.484 1.00 103.76 ? 137 LEU A CG 1 +ATOM 1073 C CD1 . LEU A 1 138 ? 14.921 123.213 101.280 1.00 126.63 ? 137 LEU A CD1 1 +ATOM 1074 C CD2 . LEU A 1 138 ? 13.676 121.817 102.913 1.00 80.49 ? 137 LEU A CD2 1 +ATOM 1075 N N . GLY A 1 139 ? 9.098 123.089 100.603 1.00 76.54 ? 138 GLY A N 1 +ATOM 1076 C CA . GLY A 1 139 ? 7.833 123.791 100.666 1.00 87.49 ? 138 GLY A CA 1 +ATOM 1077 C C . GLY A 1 139 ? 6.750 122.997 101.379 1.00 108.18 ? 138 GLY A C 1 +ATOM 1078 O O . GLY A 1 139 ? 5.690 123.544 101.688 1.00 108.11 ? 138 GLY A O 1 +ATOM 1079 N N . HIS A 1 140 ? 7.016 121.716 101.638 1.00 116.12 ? 139 HIS A N 1 +ATOM 1080 C CA . HIS A 1 140 ? 6.038 120.814 102.260 1.00 101.80 ? 139 HIS A CA 1 +ATOM 1081 C C . HIS A 1 140 ? 4.731 120.711 101.453 1.00 90.08 ? 139 HIS A C 1 +ATOM 1082 O O . HIS A 1 140 ? 3.661 121.093 101.934 1.00 97.82 ? 139 HIS A O 1 +ATOM 1083 C CB . HIS A 1 140 ? 5.761 121.207 103.725 1.00 100.47 ? 139 HIS A CB 1 +ATOM 1084 C CG . HIS A 1 140 ? 6.885 120.885 104.662 1.00 105.09 ? 139 HIS A CG 1 +ATOM 1085 N ND1 . HIS A 1 140 ? 7.134 119.679 105.151 1.00 125.22 ? 139 HIS A ND1 1 +ATOM 1086 C CD2 . HIS A 1 140 ? 7.833 121.617 105.208 1.00 121.05 ? 139 HIS A CD2 1 +ATOM 1087 C CE1 . HIS A 1 140 ? 8.180 119.658 105.949 1.00 110.62 ? 139 HIS A CE1 1 +ATOM 1088 N NE2 . HIS A 1 140 ? 8.633 120.840 106.001 1.00 103.79 ? 139 HIS A NE2 1 +ATOM 1089 N N . LYS A 1 141 ? 4.836 120.189 100.229 1.00 101.18 ? 140 LYS A N 1 +ATOM 1090 C CA . LYS A 1 141 ? 3.686 120.006 99.332 1.00 106.36 ? 140 LYS A CA 1 +ATOM 1091 C C . LYS A 1 141 ? 3.392 118.523 99.102 1.00 120.34 ? 140 LYS A C 1 +ATOM 1092 O O . LYS A 1 141 ? 2.470 118.156 98.363 1.00 93.45 ? 140 LYS A O 1 +ATOM 1093 C CB . LYS A 1 141 ? 3.916 120.707 97.988 1.00 105.13 ? 140 LYS A CB 1 +ATOM 1094 C CG . LYS A 1 141 ? 3.788 122.221 98.033 1.00 107.97 ? 140 LYS A CG 1 +ATOM 1095 C CD . LYS A 1 141 ? 4.684 122.868 96.984 1.00 132.48 ? 140 LYS A CD 1 +ATOM 1096 C CE . LYS A 1 141 ? 4.707 124.390 97.115 1.00 124.31 ? 140 LYS A CE 1 +ATOM 1097 N NZ . LYS A 1 141 ? 5.719 125.038 96.227 1.00 142.04 ? 140 LYS A NZ 1 +ATOM 1098 N N . LEU A 1 142 ? 4.185 117.673 99.743 1.00 100.87 ? 141 LEU A N 1 +ATOM 1099 C CA . LEU A 1 142 ? 3.929 116.246 99.723 1.00 87.25 ? 141 LEU A CA 1 +ATOM 1100 C C . LEU A 1 142 ? 2.737 115.898 100.602 1.00 96.08 ? 141 LEU A C 1 +ATOM 1101 O O . LEU A 1 142 ? 2.507 116.514 101.657 1.00 72.73 ? 141 LEU A O 1 +ATOM 1102 C CB . LEU A 1 142 ? 5.159 115.465 100.174 1.00 94.23 ? 141 LEU A CB 1 +ATOM 1103 C CG . LEU A 1 142 ? 6.379 115.572 99.260 1.00 61.57 ? 141 LEU A CG 1 +ATOM 1104 C CD1 . LEU A 1 142 ? 7.585 114.884 99.852 1.00 76.14 ? 141 LEU A CD1 1 +ATOM 1105 C CD2 . LEU A 1 142 ? 6.065 114.992 97.911 1.00 87.52 ? 141 LEU A CD2 1 +ATOM 1106 N N . GLU A 1 143 ? 1.985 114.907 100.130 1.00 84.13 ? 142 GLU A N 1 +ATOM 1107 C CA . GLU A 1 143 ? 0.825 114.379 100.829 1.00 96.68 ? 142 GLU A CA 1 +ATOM 1108 C C . GLU A 1 143 ? 1.289 113.326 101.815 1.00 98.93 ? 142 GLU A C 1 +ATOM 1109 O O . GLU A 1 143 ? 2.220 112.568 101.527 1.00 91.06 ? 142 GLU A O 1 +ATOM 1110 C CB . GLU A 1 143 ? -0.173 113.768 99.838 1.00 96.82 ? 142 GLU A CB 1 +ATOM 1111 C CG . GLU A 1 143 ? -1.195 114.760 99.270 1.00 99.23 ? 142 GLU A CG 1 +ATOM 1112 C CD . GLU A 1 143 ? -2.309 114.081 98.478 1.00 123.55 ? 142 GLU A CD 1 +ATOM 1113 O OE1 . GLU A 1 143 ? -2.162 112.885 98.138 1.00 124.58 ? 142 GLU A OE1 1 +ATOM 1114 O OE2 . GLU A 1 143 ? -3.336 114.742 98.204 1.00 101.89 ? 142 GLU A OE2 1 +ATOM 1115 N N . TYR A 1 144 ? 0.653 113.295 102.983 1.00 74.65 ? 143 TYR A N 1 +ATOM 1116 C CA . TYR A 1 144 ? 0.982 112.301 103.997 1.00 70.87 ? 143 TYR A CA 1 +ATOM 1117 C C . TYR A 1 144 ? 0.533 110.898 103.610 1.00 84.47 ? 143 TYR A C 1 +ATOM 1118 O O . TYR A 1 144 ? -0.355 110.324 104.236 1.00 73.46 ? 143 TYR A O 1 +ATOM 1119 C CB . TYR A 1 144 ? 0.389 112.655 105.360 1.00 58.41 ? 143 TYR A CB 1 +ATOM 1120 C CG . TYR A 1 144 ? 1.135 111.965 106.477 1.00 66.52 ? 143 TYR A CG 1 +ATOM 1121 C CD1 . TYR A 1 144 ? 2.505 111.798 106.398 1.00 90.24 ? 143 TYR A CD1 1 +ATOM 1122 C CD2 . TYR A 1 144 ? 0.481 111.474 107.591 1.00 83.15 ? 143 TYR A CD2 1 +ATOM 1123 C CE1 . TYR A 1 144 ? 3.204 111.175 107.388 1.00 75.77 ? 143 TYR A CE1 1 +ATOM 1124 C CE2 . TYR A 1 144 ? 1.178 110.845 108.593 1.00 85.33 ? 143 TYR A CE2 1 +ATOM 1125 C CZ . TYR A 1 144 ? 2.541 110.703 108.482 1.00 90.79 ? 143 TYR A CZ 1 +ATOM 1126 O OH . TYR A 1 144 ? 3.257 110.087 109.472 1.00 80.77 ? 143 TYR A OH 1 +ATOM 1127 N N . ASN A 1 145 ? 1.153 110.344 102.581 1.00 59.40 ? 144 ASN A N 1 +ATOM 1128 C CA . ASN A 1 145 ? 0.809 109.002 102.156 1.00 63.44 ? 144 ASN A CA 1 +ATOM 1129 C C . ASN A 1 145 ? 1.945 108.320 101.418 1.00 64.57 ? 144 ASN A C 1 +ATOM 1130 O O . ASN A 1 145 ? 3.073 108.812 101.401 1.00 83.70 ? 144 ASN A O 1 +ATOM 1131 C CB . ASN A 1 145 ? -0.490 108.991 101.344 1.00 47.09 ? 144 ASN A CB 1 +ATOM 1132 C CG . ASN A 1 145 ? -0.392 109.762 100.042 1.00 107.97 ? 144 ASN A CG 1 +ATOM 1133 O OD1 . ASN A 1 145 ? 0.628 109.727 99.336 1.00 69.24 ? 144 ASN A OD1 1 +ATOM 1134 N ND2 . ASN A 1 145 ? -1.479 110.449 99.698 1.00 94.20 ? 144 ASN A ND2 1 +ATOM 1135 N N . TYR A 1 146 ? 1.643 107.176 100.825 1.00 70.63 ? 145 TYR A N 1 +ATOM 1136 C CA . TYR A 1 146 ? 2.665 106.391 100.165 1.00 97.26 ? 145 TYR A CA 1 +ATOM 1137 C C . TYR A 1 146 ? 2.046 105.447 99.151 1.00 76.71 ? 145 TYR A C 1 +ATOM 1138 O O . TYR A 1 146 ? 0.839 105.192 99.180 1.00 80.93 ? 145 TYR A O 1 +ATOM 1139 C CB . TYR A 1 146 ? 3.474 105.617 101.194 1.00 63.58 ? 145 TYR A CB 1 +ATOM 1140 C CG . TYR A 1 146 ? 4.945 105.660 100.926 1.00 67.30 ? 145 TYR A CG 1 +ATOM 1141 C CD1 . TYR A 1 146 ? 5.702 106.754 101.295 1.00 68.47 ? 145 TYR A CD1 1 +ATOM 1142 C CD2 . TYR A 1 146 ? 5.578 104.609 100.296 1.00 105.10 ? 145 TYR A CD2 1 +ATOM 1143 C CE1 . TYR A 1 146 ? 7.060 106.795 101.047 1.00 90.81 ? 145 TYR A CE1 1 +ATOM 1144 C CE2 . TYR A 1 146 ? 6.932 104.636 100.045 1.00 82.49 ? 145 TYR A CE2 1 +ATOM 1145 C CZ . TYR A 1 146 ? 7.668 105.726 100.421 1.00 76.47 ? 145 TYR A CZ 1 +ATOM 1146 O OH . TYR A 1 146 ? 9.014 105.730 100.165 1.00 88.85 ? 145 TYR A OH 1 +ATOM 1147 N N . ASN A 1 147 ? 2.889 104.960 98.244 1.00 102.52 ? 146 ASN A N 1 +ATOM 1148 C CA . ASN A 1 147 ? 2.482 104.071 97.164 1.00 87.40 ? 146 ASN A CA 1 +ATOM 1149 C C . ASN A 1 147 ? 3.328 102.810 97.217 1.00 90.75 ? 146 ASN A C 1 +ATOM 1150 O O . ASN A 1 147 ? 4.195 102.664 98.085 1.00 91.42 ? 146 ASN A O 1 +ATOM 1151 C CB . ASN A 1 147 ? 2.655 104.745 95.794 1.00 86.29 ? 146 ASN A CB 1 +ATOM 1152 C CG . ASN A 1 147 ? 1.733 105.944 95.598 1.00 84.79 ? 146 ASN A CG 1 +ATOM 1153 O OD1 . ASN A 1 147 ? 0.552 105.904 95.947 1.00 79.52 ? 146 ASN A OD1 1 +ATOM 1154 N ND2 . ASN A 1 147 ? 2.277 107.021 95.036 1.00 119.82 ? 146 ASN A ND2 1 +ATOM 1155 N N . SER A 1 148 ? 3.079 101.902 96.282 1.00 82.82 ? 147 SER A N 1 +ATOM 1156 C CA . SER A 1 148 ? 3.773 100.626 96.275 1.00 70.01 ? 147 SER A CA 1 +ATOM 1157 C C . SER A 1 148 ? 4.838 100.607 95.195 1.00 60.24 ? 147 SER A C 1 +ATOM 1158 O O . SER A 1 148 ? 4.662 101.206 94.143 1.00 110.61 ? 147 SER A O 1 +ATOM 1159 C CB . SER A 1 148 ? 2.775 99.490 96.093 1.00 74.22 ? 147 SER A CB 1 +ATOM 1160 O OG . SER A 1 148 ? 2.004 99.328 97.271 1.00 95.91 ? 147 SER A OG 1 +ATOM 1161 N N . HIS A 1 149 ? 5.953 99.936 95.460 1.00 79.88 ? 148 HIS A N 1 +ATOM 1162 C CA . HIS A 1 149 ? 7.091 99.984 94.551 1.00 84.72 ? 148 HIS A CA 1 +ATOM 1163 C C . HIS A 1 149 ? 7.765 98.613 94.456 1.00 86.33 ? 148 HIS A C 1 +ATOM 1164 O O . HIS A 1 149 ? 7.484 97.724 95.255 1.00 86.10 ? 148 HIS A O 1 +ATOM 1165 C CB . HIS A 1 149 ? 8.074 101.090 94.986 1.00 83.85 ? 148 HIS A CB 1 +ATOM 1166 C CG . HIS A 1 149 ? 7.439 102.446 95.098 1.00 92.01 ? 148 HIS A CG 1 +ATOM 1167 N ND1 . HIS A 1 149 ? 7.156 103.043 96.308 1.00 87.63 ? 148 HIS A ND1 1 +ATOM 1168 C CD2 . HIS A 1 149 ? 6.985 103.298 94.147 1.00 128.31 ? 148 HIS A CD2 1 +ATOM 1169 C CE1 . HIS A 1 149 ? 6.571 104.209 96.098 1.00 93.43 ? 148 HIS A CE1 1 +ATOM 1170 N NE2 . HIS A 1 149 ? 6.453 104.387 94.796 1.00 75.26 ? 148 HIS A NE2 1 +ATOM 1171 N N . ASN A 1 150 ? 8.622 98.433 93.456 1.00 85.92 ? 149 ASN A N 1 +ATOM 1172 C CA . ASN A 1 150 ? 9.361 97.184 93.289 1.00 94.25 ? 149 ASN A CA 1 +ATOM 1173 C C . ASN A 1 150 ? 10.862 97.493 93.333 1.00 83.22 ? 149 ASN A C 1 +ATOM 1174 O O . ASN A 1 150 ? 11.328 98.390 92.642 1.00 98.31 ? 149 ASN A O 1 +ATOM 1175 C CB . ASN A 1 150 ? 8.968 96.462 91.984 1.00 101.86 ? 149 ASN A CB 1 +ATOM 1176 C CG . ASN A 1 150 ? 7.451 96.213 91.859 1.00 96.37 ? 149 ASN A CG 1 +ATOM 1177 O OD1 . ASN A 1 150 ? 6.844 95.527 92.683 1.00 118.95 ? 149 ASN A OD1 1 +ATOM 1178 N ND2 . ASN A 1 150 ? 6.848 96.758 90.806 1.00 118.94 ? 149 ASN A ND2 1 +ATOM 1179 N N . VAL A 1 151 ? 11.606 96.749 94.148 1.00 100.05 ? 150 VAL A N 1 +ATOM 1180 C CA . VAL A 1 151 ? 12.965 97.125 94.553 1.00 79.36 ? 150 VAL A CA 1 +ATOM 1181 C C . VAL A 1 151 ? 14.028 96.235 93.886 1.00 108.96 ? 150 VAL A C 1 +ATOM 1182 O O . VAL A 1 151 ? 14.555 95.314 94.505 1.00 112.03 ? 150 VAL A O 1 +ATOM 1183 C CB . VAL A 1 151 ? 13.080 97.073 96.119 1.00 97.01 ? 150 VAL A CB 1 +ATOM 1184 C CG1 . VAL A 1 151 ? 14.475 97.395 96.620 1.00 71.60 ? 150 VAL A CG1 1 +ATOM 1185 C CG2 . VAL A 1 151 ? 12.089 98.024 96.754 1.00 78.80 ? 150 VAL A CG2 1 +ATOM 1186 N N . TYR A 1 152 ? 14.349 96.516 92.626 1.00 91.14 ? 151 TYR A N 1 +ATOM 1187 C CA . TYR A 1 152 ? 15.182 95.602 91.839 1.00 91.06 ? 151 TYR A CA 1 +ATOM 1188 C C . TYR A 1 152 ? 16.597 95.415 92.384 1.00 98.39 ? 151 TYR A C 1 +ATOM 1189 O O . TYR A 1 152 ? 17.411 96.330 92.377 1.00 103.93 ? 151 TYR A O 1 +ATOM 1190 C CB . TYR A 1 152 ? 15.179 95.990 90.355 1.00 78.27 ? 151 TYR A CB 1 +ATOM 1191 C CG . TYR A 1 152 ? 13.772 96.202 89.840 1.00 97.31 ? 151 TYR A CG 1 +ATOM 1192 C CD1 . TYR A 1 152 ? 13.010 95.138 89.363 1.00 101.26 ? 151 TYR A CD1 1 +ATOM 1193 C CD2 . TYR A 1 152 ? 13.192 97.463 89.861 1.00 78.03 ? 151 TYR A CD2 1 +ATOM 1194 C CE1 . TYR A 1 152 ? 11.705 95.330 88.903 1.00 89.29 ? 151 TYR A CE1 1 +ATOM 1195 C CE2 . TYR A 1 152 ? 11.890 97.668 89.405 1.00 123.32 ? 151 TYR A CE2 1 +ATOM 1196 C CZ . TYR A 1 152 ? 11.150 96.600 88.926 1.00 119.92 ? 151 TYR A CZ 1 +ATOM 1197 O OH . TYR A 1 152 ? 9.855 96.805 88.479 1.00 94.69 ? 151 TYR A OH 1 +ATOM 1198 N N . ILE A 1 153 ? 16.861 94.210 92.876 1.00 85.04 ? 152 ILE A N 1 +ATOM 1199 C CA . ILE A 1 153 ? 18.175 93.831 93.380 1.00 95.43 ? 152 ILE A CA 1 +ATOM 1200 C C . ILE A 1 153 ? 19.001 93.172 92.266 1.00 116.48 ? 152 ILE A C 1 +ATOM 1201 O O . ILE A 1 153 ? 18.460 92.660 91.279 1.00 124.72 ? 152 ILE A O 1 +ATOM 1202 C CB . ILE A 1 153 ? 18.048 92.906 94.628 1.00 94.90 ? 152 ILE A CB 1 +ATOM 1203 C CG1 . ILE A 1 153 ? 17.009 93.472 95.596 1.00 82.37 ? 152 ILE A CG1 1 +ATOM 1204 C CG2 . ILE A 1 153 ? 19.385 92.717 95.350 1.00 77.57 ? 152 ILE A CG2 1 +ATOM 1205 C CD1 . ILE A 1 153 ? 16.911 92.705 96.877 1.00 121.55 ? 152 ILE A CD1 1 +ATOM 1206 N N . MET A 1 154 ? 20.316 93.210 92.434 1.00 116.92 ? 153 MET A N 1 +ATOM 1207 C CA . MET A 1 154 ? 21.258 92.733 91.442 1.00 136.49 ? 153 MET A CA 1 +ATOM 1208 C C . MET A 1 154 ? 22.555 92.504 92.193 1.00 123.53 ? 153 MET A C 1 +ATOM 1209 O O . MET A 1 154 ? 22.909 93.282 93.074 1.00 115.17 ? 153 MET A O 1 +ATOM 1210 C CB . MET A 1 154 ? 21.436 93.798 90.358 1.00 133.28 ? 153 MET A CB 1 +ATOM 1211 C CG . MET A 1 154 ? 22.437 93.462 89.275 1.00 136.31 ? 153 MET A CG 1 +ATOM 1212 S SD . MET A 1 154 ? 21.949 94.099 87.668 1.00 202.28 ? 153 MET A SD 1 +ATOM 1213 C CE . MET A 1 154 ? 21.377 95.725 88.065 1.00 118.39 ? 153 MET A CE 1 +ATOM 1214 N N . ALA A 1 155 ? 23.254 91.423 91.882 1.00 122.14 ? 154 ALA A N 1 +ATOM 1215 C CA . ALA A 1 155 ? 24.492 91.149 92.591 1.00 116.96 ? 154 ALA A CA 1 +ATOM 1216 C C . ALA A 1 155 ? 25.629 92.018 92.067 1.00 147.18 ? 154 ALA A C 1 +ATOM 1217 O O . ALA A 1 155 ? 25.617 92.465 90.916 1.00 123.74 ? 154 ALA A O 1 +ATOM 1218 C CB . ALA A 1 155 ? 24.856 89.671 92.508 1.00 90.29 ? 154 ALA A CB 1 +ATOM 1219 N N . ASP A 1 156 ? 26.593 92.272 92.940 1.00 150.78 ? 155 ASP A N 1 +ATOM 1220 C CA . ASP A 1 156 ? 27.847 92.889 92.548 1.00 171.91 ? 155 ASP A CA 1 +ATOM 1221 C C . ASP A 1 156 ? 28.952 91.950 93.013 1.00 187.03 ? 155 ASP A C 1 +ATOM 1222 O O . ASP A 1 156 ? 29.541 92.136 94.083 1.00 136.58 ? 155 ASP A O 1 +ATOM 1223 C CB . ASP A 1 156 ? 27.984 94.275 93.175 1.00 164.61 ? 155 ASP A CB 1 +ATOM 1224 C CG . ASP A 1 156 ? 29.247 94.995 92.738 1.00 170.01 ? 155 ASP A CG 1 +ATOM 1225 O OD1 . ASP A 1 156 ? 30.007 94.446 91.908 1.00 177.48 ? 155 ASP A OD1 1 +ATOM 1226 O OD2 . ASP A 1 156 ? 29.468 96.125 93.223 1.00 139.16 ? 155 ASP A OD2 1 +ATOM 1227 N N . LYS A 1 157 ? 29.215 90.931 92.198 1.00 206.60 ? 156 LYS A N 1 +ATOM 1228 C CA . LYS A 1 157 ? 30.120 89.850 92.574 1.00 196.27 ? 156 LYS A CA 1 +ATOM 1229 C C . LYS A 1 157 ? 31.536 90.350 92.817 1.00 174.95 ? 156 LYS A C 1 +ATOM 1230 O O . LYS A 1 157 ? 32.290 89.755 93.589 1.00 135.11 ? 156 LYS A O 1 +ATOM 1231 C CB . LYS A 1 157 ? 30.103 88.733 91.522 1.00 189.86 ? 156 LYS A CB 1 +ATOM 1232 C CG . LYS A 1 157 ? 28.813 87.923 91.527 1.00 189.60 ? 156 LYS A CG 1 +ATOM 1233 C CD . LYS A 1 157 ? 28.787 86.851 90.451 1.00 175.68 ? 156 LYS A CD 1 +ATOM 1234 C CE . LYS A 1 157 ? 27.576 85.934 90.613 1.00 166.50 ? 156 LYS A CE 1 +ATOM 1235 N NZ . LYS A 1 157 ? 26.287 86.683 90.656 1.00 166.59 ? 156 LYS A NZ 1 +ATOM 1236 N N . GLN A 1 158 ? 31.885 91.458 92.171 1.00 193.79 ? 157 GLN A N 1 +ATOM 1237 C CA . GLN A 1 158 ? 33.212 92.037 92.330 1.00 194.69 ? 157 GLN A CA 1 +ATOM 1238 C C . GLN A 1 158 ? 33.379 92.699 93.702 1.00 176.84 ? 157 GLN A C 1 +ATOM 1239 O O . GLN A 1 158 ? 34.429 92.568 94.333 1.00 153.02 ? 157 GLN A O 1 +ATOM 1240 C CB . GLN A 1 158 ? 33.535 93.018 91.189 1.00 186.58 ? 157 GLN A CB 1 +ATOM 1241 C CG . GLN A 1 158 ? 33.585 92.392 89.776 1.00 203.22 ? 157 GLN A CG 1 +ATOM 1242 C CD . GLN A 1 158 ? 34.755 91.420 89.555 1.00 206.45 ? 157 GLN A CD 1 +ATOM 1243 O OE1 . GLN A 1 158 ? 34.773 90.311 90.091 1.00 212.12 ? 157 GLN A OE1 1 +ATOM 1244 N NE2 . GLN A 1 158 ? 35.721 91.833 88.742 1.00 182.95 ? 157 GLN A NE2 1 +ATOM 1245 N N . LYS A 1 159 ? 32.342 93.392 94.172 1.00 183.38 ? 158 LYS A N 1 +ATOM 1246 C CA . LYS A 1 159 ? 32.428 94.103 95.450 1.00 162.05 ? 158 LYS A CA 1 +ATOM 1247 C C . LYS A 1 159 ? 31.738 93.364 96.599 1.00 155.61 ? 158 LYS A C 1 +ATOM 1248 O O . LYS A 1 159 ? 31.510 93.943 97.663 1.00 133.52 ? 158 LYS A O 1 +ATOM 1249 C CB . LYS A 1 159 ? 31.894 95.535 95.322 1.00 146.45 ? 158 LYS A CB 1 +ATOM 1250 C CG . LYS A 1 159 ? 32.457 96.289 94.115 1.00 195.23 ? 158 LYS A CG 1 +ATOM 1251 C CD . LYS A 1 159 ? 33.981 96.161 94.011 1.00 204.07 ? 158 LYS A CD 1 +ATOM 1252 C CE . LYS A 1 159 ? 34.471 96.298 92.567 1.00 177.52 ? 158 LYS A CE 1 +ATOM 1253 N NZ . LYS A 1 159 ? 35.919 95.973 92.424 1.00 164.27 ? 158 LYS A NZ 1 +ATOM 1254 N N . ASN A 1 160 ? 31.413 92.091 96.370 1.00 153.66 ? 159 ASN A N 1 +ATOM 1255 C CA . ASN A 1 160 ? 30.868 91.207 97.405 1.00 158.01 ? 159 ASN A CA 1 +ATOM 1256 C C . ASN A 1 160 ? 29.604 91.764 98.068 1.00 142.02 ? 159 ASN A C 1 +ATOM 1257 O O . ASN A 1 160 ? 29.344 91.539 99.250 1.00 120.07 ? 159 ASN A O 1 +ATOM 1258 C CB . ASN A 1 160 ? 31.944 90.891 98.456 1.00 156.81 ? 159 ASN A CB 1 +ATOM 1259 C CG . ASN A 1 160 ? 31.630 89.644 99.273 1.00 171.34 ? 159 ASN A CG 1 +ATOM 1260 O OD1 . ASN A 1 160 ? 31.100 88.660 98.754 1.00 171.22 ? 159 ASN A OD1 1 +ATOM 1261 N ND2 . ASN A 1 160 ? 31.954 89.684 100.563 1.00 152.54 ? 159 ASN A ND2 1 +ATOM 1262 N N . GLY A 1 161 ? 28.820 92.505 97.302 1.00 130.72 ? 160 GLY A N 1 +ATOM 1263 C CA . GLY A 1 161 ? 27.627 93.111 97.849 1.00 133.18 ? 160 GLY A CA 1 +ATOM 1264 C C . GLY A 1 161 ? 26.563 93.121 96.787 1.00 121.03 ? 160 GLY A C 1 +ATOM 1265 O O . GLY A 1 161 ? 26.641 92.363 95.826 1.00 118.76 ? 160 GLY A O 1 +ATOM 1266 N N . ILE A 1 162 ? 25.567 93.981 96.947 1.00 124.09 ? 161 ILE A N 1 +ATOM 1267 C CA . ILE A 1 162 ? 24.526 94.095 95.941 1.00 117.06 ? 161 ILE A CA 1 +ATOM 1268 C C . ILE A 1 162 ? 24.377 95.530 95.464 1.00 109.25 ? 161 ILE A C 1 +ATOM 1269 O O . ILE A 1 162 ? 24.799 96.470 96.136 1.00 107.18 ? 161 ILE A O 1 +ATOM 1270 C CB . ILE A 1 162 ? 23.172 93.583 96.462 1.00 123.81 ? 161 ILE A CB 1 +ATOM 1271 C CG1 . ILE A 1 162 ? 22.711 94.407 97.664 1.00 122.38 ? 161 ILE A CG1 1 +ATOM 1272 C CG2 . ILE A 1 162 ? 23.268 92.108 96.836 1.00 131.30 ? 161 ILE A CG2 1 +ATOM 1273 C CD1 . ILE A 1 162 ? 21.297 94.090 98.111 1.00 87.17 ? 161 ILE A CD1 1 +ATOM 1274 N N . LYS A 1 163 ? 23.788 95.686 94.288 1.00 96.75 ? 162 LYS A N 1 +ATOM 1275 C CA . LYS A 1 163 ? 23.445 96.997 93.765 1.00 112.48 ? 162 LYS A CA 1 +ATOM 1276 C C . LYS A 1 163 ? 21.931 97.070 93.705 1.00 118.58 ? 162 LYS A C 1 +ATOM 1277 O O . LYS A 1 163 ? 21.284 96.166 93.195 1.00 129.94 ? 162 LYS A O 1 +ATOM 1278 C CB . LYS A 1 163 ? 24.030 97.188 92.365 1.00 132.03 ? 162 LYS A CB 1 +ATOM 1279 C CG . LYS A 1 163 ? 25.115 98.253 92.273 1.00 165.52 ? 162 LYS A CG 1 +ATOM 1280 C CD . LYS A 1 163 ? 25.562 98.490 90.834 1.00 162.47 ? 162 LYS A CD 1 +ATOM 1281 C CE . LYS A 1 163 ? 26.834 99.338 90.773 1.00 158.16 ? 162 LYS A CE 1 +ATOM 1282 N NZ . LYS A 1 163 ? 28.010 98.663 91.398 1.00 157.38 ? 162 LYS A NZ 1 +ATOM 1283 N N . VAL A 1 164 ? 21.347 98.136 94.227 1.00 106.31 ? 163 VAL A N 1 +ATOM 1284 C CA . VAL A 1 164 ? 19.897 98.219 94.228 1.00 100.88 ? 163 VAL A CA 1 +ATOM 1285 C C . VAL A 1 164 ? 19.446 99.503 93.549 1.00 81.13 ? 163 VAL A C 1 +ATOM 1286 O O . VAL A 1 164 ? 20.143 100.513 93.602 1.00 110.13 ? 163 VAL A O 1 +ATOM 1287 C CB . VAL A 1 164 ? 19.348 98.134 95.675 1.00 121.43 ? 163 VAL A CB 1 +ATOM 1288 C CG1 . VAL A 1 164 ? 17.825 98.053 95.692 1.00 90.13 ? 163 VAL A CG1 1 +ATOM 1289 C CG2 . VAL A 1 164 ? 19.954 96.939 96.402 1.00 113.16 ? 163 VAL A CG2 1 +ATOM 1290 N N . ASN A 1 165 ? 18.289 99.467 92.900 1.00 84.29 ? 164 ASN A N 1 +ATOM 1291 C CA . ASN A 1 165 ? 17.721 100.691 92.360 1.00 111.90 ? 164 ASN A CA 1 +ATOM 1292 C C . ASN A 1 165 ? 16.203 100.640 92.221 1.00 103.68 ? 164 ASN A C 1 +ATOM 1293 O O . ASN A 1 165 ? 15.628 99.576 92.003 1.00 113.68 ? 164 ASN A O 1 +ATOM 1294 C CB . ASN A 1 165 ? 18.381 101.042 91.023 1.00 101.52 ? 164 ASN A CB 1 +ATOM 1295 C CG . ASN A 1 165 ? 18.010 100.078 89.921 1.00 121.07 ? 164 ASN A CG 1 +ATOM 1296 O OD1 . ASN A 1 165 ? 18.359 98.895 89.969 1.00 145.51 ? 164 ASN A OD1 1 +ATOM 1297 N ND2 . ASN A 1 165 ? 17.308 100.581 88.907 1.00 155.23 ? 164 ASN A ND2 1 +ATOM 1298 N N . PHE A 1 166 ? 15.561 101.797 92.360 1.00 86.79 ? 165 PHE A N 1 +ATOM 1299 C CA . PHE A 1 166 ? 14.113 101.909 92.214 1.00 97.35 ? 165 PHE A CA 1 +ATOM 1300 C C . PHE A 1 166 ? 13.687 103.352 92.169 1.00 84.16 ? 165 PHE A C 1 +ATOM 1301 O O . PHE A 1 166 ? 14.483 104.253 92.411 1.00 106.60 ? 165 PHE A O 1 +ATOM 1302 C CB . PHE A 1 166 ? 13.367 101.210 93.351 1.00 99.06 ? 165 PHE A CB 1 +ATOM 1303 C CG . PHE A 1 166 ? 13.852 101.575 94.733 1.00 89.11 ? 165 PHE A CG 1 +ATOM 1304 C CD1 . PHE A 1 166 ? 15.013 101.011 95.253 1.00 83.10 ? 165 PHE A CD1 1 +ATOM 1305 C CD2 . PHE A 1 166 ? 13.116 102.432 95.533 1.00 67.08 ? 165 PHE A CD2 1 +ATOM 1306 C CE1 . PHE A 1 166 ? 15.449 101.320 96.521 1.00 71.90 ? 165 PHE A CE1 1 +ATOM 1307 C CE2 . PHE A 1 166 ? 13.541 102.740 96.801 1.00 80.84 ? 165 PHE A CE2 1 +ATOM 1308 C CZ . PHE A 1 166 ? 14.713 102.185 97.296 1.00 84.20 ? 165 PHE A CZ 1 +ATOM 1309 N N . LYS A 1 167 ? 12.413 103.566 91.885 1.00 84.60 ? 166 LYS A N 1 +ATOM 1310 C CA . LYS A 1 167 ? 11.913 104.915 91.720 1.00 97.09 ? 166 LYS A CA 1 +ATOM 1311 C C . LYS A 1 167 ? 10.633 105.133 92.505 1.00 94.39 ? 166 LYS A C 1 +ATOM 1312 O O . LYS A 1 167 ? 9.570 104.623 92.137 1.00 98.82 ? 166 LYS A O 1 +ATOM 1313 C CB . LYS A 1 167 ? 11.684 105.206 90.238 1.00 86.70 ? 166 LYS A CB 1 +ATOM 1314 C CG . LYS A 1 167 ? 11.235 106.629 89.927 1.00 130.29 ? 166 LYS A CG 1 +ATOM 1315 C CD . LYS A 1 167 ? 10.923 106.780 88.442 1.00 151.08 ? 166 LYS A CD 1 +ATOM 1316 C CE . LYS A 1 167 ? 12.037 106.202 87.560 1.00 127.93 ? 166 LYS A CE 1 +ATOM 1317 N NZ . LYS A 1 167 ? 13.323 106.948 87.683 1.00 158.74 ? 166 LYS A NZ 1 +ATOM 1318 N N . ILE A 1 168 ? 10.747 105.907 93.581 1.00 81.12 ? 167 ILE A N 1 +ATOM 1319 C CA . ILE A 1 168 ? 9.613 106.196 94.451 1.00 102.49 ? 167 ILE A CA 1 +ATOM 1320 C C . ILE A 1 168 ? 8.774 107.344 93.909 1.00 86.39 ? 167 ILE A C 1 +ATOM 1321 O O . ILE A 1 168 ? 9.303 108.388 93.556 1.00 83.50 ? 167 ILE A O 1 +ATOM 1322 C CB . ILE A 1 168 ? 10.074 106.584 95.879 1.00 72.19 ? 167 ILE A CB 1 +ATOM 1323 C CG1 . ILE A 1 168 ? 10.880 105.458 96.533 1.00 85.69 ? 167 ILE A CG1 1 +ATOM 1324 C CG2 . ILE A 1 168 ? 8.887 106.968 96.740 1.00 78.14 ? 167 ILE A CG2 1 +ATOM 1325 C CD1 . ILE A 1 168 ? 10.122 104.190 96.764 1.00 101.14 ? 167 ILE A CD1 1 +ATOM 1326 N N . ARG A 1 169 ? 7.463 107.146 93.852 1.00 73.75 ? 168 ARG A N 1 +ATOM 1327 C CA . ARG A 1 169 ? 6.544 108.223 93.519 1.00 88.57 ? 168 ARG A CA 1 +ATOM 1328 C C . ARG A 1 169 ? 5.943 108.844 94.784 1.00 75.28 ? 168 ARG A C 1 +ATOM 1329 O O . ARG A 1 169 ? 5.358 108.135 95.596 1.00 104.28 ? 168 ARG A O 1 +ATOM 1330 C CB . ARG A 1 169 ? 5.418 107.686 92.629 1.00 91.54 ? 168 ARG A CB 1 +ATOM 1331 C CG . ARG A 1 169 ? 5.875 107.188 91.260 1.00 104.05 ? 168 ARG A CG 1 +ATOM 1332 C CD . ARG A 1 169 ? 4.707 106.741 90.351 1.00 97.95 ? 168 ARG A CD 1 +ATOM 1333 N NE . ARG A 1 169 ? 4.026 105.549 90.855 1.00 122.00 ? 168 ARG A NE 1 +ATOM 1334 C CZ . ARG A 1 169 ? 4.587 104.345 90.976 1.00 144.29 ? 168 ARG A CZ 1 +ATOM 1335 N NH1 . ARG A 1 169 ? 5.856 104.139 90.633 1.00 117.26 ? 168 ARG A NH1 1 +ATOM 1336 N NH2 . ARG A 1 169 ? 3.873 103.335 91.453 1.00 127.81 ? 168 ARG A NH2 1 +ATOM 1337 N N . HIS A 1 170 ? 6.081 110.158 94.951 1.00 66.72 ? 169 HIS A N 1 +ATOM 1338 C CA . HIS A 1 170 ? 5.372 110.868 96.021 1.00 89.84 ? 169 HIS A CA 1 +ATOM 1339 C C . HIS A 1 170 ? 4.162 111.642 95.494 1.00 72.72 ? 169 HIS A C 1 +ATOM 1340 O O . HIS A 1 170 ? 4.273 112.366 94.521 1.00 108.54 ? 169 HIS A O 1 +ATOM 1341 C CB . HIS A 1 170 ? 6.304 111.836 96.729 1.00 67.59 ? 169 HIS A CB 1 +ATOM 1342 C CG . HIS A 1 170 ? 7.502 111.187 97.343 1.00 98.67 ? 169 HIS A CG 1 +ATOM 1343 N ND1 . HIS A 1 170 ? 7.481 110.626 98.600 1.00 98.22 ? 169 HIS A ND1 1 +ATOM 1344 C CD2 . HIS A 1 170 ? 8.762 111.018 96.875 1.00 107.47 ? 169 HIS A CD2 1 +ATOM 1345 C CE1 . HIS A 1 170 ? 8.675 110.136 98.880 1.00 86.64 ? 169 HIS A CE1 1 +ATOM 1346 N NE2 . HIS A 1 170 ? 9.471 110.359 97.850 1.00 70.32 ? 169 HIS A NE2 1 +ATOM 1347 N N . ASN A 1 171 ? 3.009 111.492 96.133 1.00 110.02 ? 170 ASN A N 1 +ATOM 1348 C CA . ASN A 1 171 ? 1.839 112.279 95.756 1.00 80.73 ? 170 ASN A CA 1 +ATOM 1349 C C . ASN A 1 171 ? 1.962 113.712 96.257 1.00 107.58 ? 170 ASN A C 1 +ATOM 1350 O O . ASN A 1 171 ? 2.552 113.943 97.310 1.00 137.32 ? 170 ASN A O 1 +ATOM 1351 C CB . ASN A 1 171 ? 0.571 111.665 96.345 1.00 110.41 ? 170 ASN A CB 1 +ATOM 1352 C CG . ASN A 1 171 ? 0.103 110.443 95.587 1.00 108.30 ? 170 ASN A CG 1 +ATOM 1353 O OD1 . ASN A 1 171 ? 0.893 109.754 94.944 1.00 94.82 ? 170 ASN A OD1 1 +ATOM 1354 N ND2 . ASN A 1 171 ? -1.196 110.168 95.658 1.00 94.80 ? 170 ASN A ND2 1 +ATOM 1355 N N . ILE A 1 172 ? 1.386 114.655 95.507 1.00 108.79 ? 171 ILE A N 1 +ATOM 1356 C CA . ILE A 1 172 ? 1.345 116.087 95.843 1.00 100.60 ? 171 ILE A CA 1 +ATOM 1357 C C . ILE A 1 172 ? -0.130 116.486 95.753 1.00 118.73 ? 171 ILE A C 1 +ATOM 1358 O O . ILE A 1 172 ? -0.909 115.740 95.163 1.00 147.05 ? 171 ILE A O 1 +ATOM 1359 C CB . ILE A 1 172 ? 2.204 116.888 94.837 1.00 95.60 ? 171 ILE A CB 1 +ATOM 1360 C CG1 . ILE A 1 172 ? 3.651 116.400 94.890 1.00 96.71 ? 171 ILE A CG1 1 +ATOM 1361 C CG2 . ILE A 1 172 ? 2.151 118.388 95.093 1.00 79.23 ? 171 ILE A CG2 1 +ATOM 1362 C CD1 . ILE A 1 172 ? 4.417 116.634 93.612 1.00 93.70 ? 171 ILE A CD1 1 +ATOM 1363 N N . GLU A 1 173 ? -0.548 117.615 96.330 1.00 78.84 ? 172 GLU A N 1 +ATOM 1364 C CA . GLU A 1 173 ? -1.989 117.911 96.331 1.00 124.99 ? 172 GLU A CA 1 +ATOM 1365 C C . GLU A 1 173 ? -2.624 118.256 94.968 1.00 145.99 ? 172 GLU A C 1 +ATOM 1366 O O . GLU A 1 173 ? -3.797 117.960 94.733 1.00 155.65 ? 172 GLU A O 1 +ATOM 1367 C CB . GLU A 1 173 ? -2.404 118.937 97.393 1.00 95.47 ? 172 GLU A CB 1 +ATOM 1368 C CG . GLU A 1 173 ? -3.920 118.872 97.628 1.00 157.68 ? 172 GLU A CG 1 +ATOM 1369 C CD . GLU A 1 173 ? -4.479 119.944 98.543 1.00 197.60 ? 172 GLU A CD 1 +ATOM 1370 O OE1 . GLU A 1 173 ? -4.329 121.145 98.238 1.00 177.90 ? 172 GLU A OE1 1 +ATOM 1371 O OE2 . GLU A 1 173 ? -5.100 119.574 99.562 1.00 207.94 ? 172 GLU A OE2 1 +ATOM 1372 N N . ASP A 1 174 ? -1.865 118.862 94.063 1.00 116.01 ? 173 ASP A N 1 +ATOM 1373 C CA . ASP A 1 174 ? -2.410 119.197 92.747 1.00 120.63 ? 173 ASP A CA 1 +ATOM 1374 C C . ASP A 1 174 ? -2.618 117.971 91.835 1.00 152.41 ? 173 ASP A C 1 +ATOM 1375 O O . ASP A 1 174 ? -3.032 118.103 90.683 1.00 214.09 ? 173 ASP A O 1 +ATOM 1376 C CB . ASP A 1 174 ? -1.530 120.245 92.058 1.00 143.38 ? 173 ASP A CB 1 +ATOM 1377 C CG . ASP A 1 174 ? -0.056 119.864 92.057 1.00 140.76 ? 173 ASP A CG 1 +ATOM 1378 O OD1 . ASP A 1 174 ? 0.254 118.655 92.078 1.00 136.59 ? 173 ASP A OD1 1 +ATOM 1379 O OD2 . ASP A 1 174 ? 0.798 120.775 92.034 1.00 132.96 ? 173 ASP A OD2 1 +ATOM 1380 N N . GLY A 1 175 ? -2.321 116.783 92.353 1.00 97.82 ? 174 GLY A N 1 +ATOM 1381 C CA . GLY A 1 175 ? -2.489 115.557 91.593 1.00 97.72 ? 174 GLY A CA 1 +ATOM 1382 C C . GLY A 1 175 ? -1.212 115.091 90.921 1.00 115.84 ? 174 GLY A C 1 +ATOM 1383 O O . GLY A 1 175 ? -1.157 113.988 90.369 1.00 117.61 ? 174 GLY A O 1 +ATOM 1384 N N . SER A 1 176 ? -0.179 115.927 90.965 1.00 78.21 ? 175 SER A N 1 +ATOM 1385 C CA . SER A 1 176 ? 1.081 115.588 90.313 1.00 112.22 ? 175 SER A CA 1 +ATOM 1386 C C . SER A 1 176 ? 1.927 114.703 91.212 1.00 96.45 ? 175 SER A C 1 +ATOM 1387 O O . SER A 1 176 ? 1.532 114.401 92.334 1.00 111.75 ? 175 SER A O 1 +ATOM 1388 C CB . SER A 1 176 ? 1.850 116.840 89.890 1.00 108.36 ? 175 SER A CB 1 +ATOM 1389 O OG . SER A 1 176 ? 2.026 117.731 90.973 1.00 107.22 ? 175 SER A OG 1 +ATOM 1390 N N . VAL A 1 177 ? 3.088 114.284 90.718 1.00 89.57 ? 176 VAL A N 1 +ATOM 1391 C CA . VAL A 1 177 ? 3.847 113.216 91.367 1.00 84.62 ? 176 VAL A CA 1 +ATOM 1392 C C . VAL A 1 177 ? 5.356 113.457 91.394 1.00 109.62 ? 176 VAL A C 1 +ATOM 1393 O O . VAL A 1 177 ? 6.027 113.420 90.362 1.00 129.88 ? 176 VAL A O 1 +ATOM 1394 C CB . VAL A 1 177 ? 3.578 111.848 90.683 1.00 84.89 ? 176 VAL A CB 1 +ATOM 1395 C CG1 . VAL A 1 177 ? 4.477 110.751 91.265 1.00 98.50 ? 176 VAL A CG1 1 +ATOM 1396 C CG2 . VAL A 1 177 ? 2.108 111.466 90.791 1.00 96.68 ? 176 VAL A CG2 1 +ATOM 1397 N N . GLN A 1 178 ? 5.891 113.665 92.589 1.00 82.11 ? 177 GLN A N 1 +ATOM 1398 C CA . GLN A 1 178 ? 7.312 113.940 92.747 1.00 92.20 ? 177 GLN A CA 1 +ATOM 1399 C C . GLN A 1 178 ? 8.185 112.677 92.682 1.00 104.94 ? 177 GLN A C 1 +ATOM 1400 O O . GLN A 1 178 ? 8.093 111.806 93.542 1.00 99.51 ? 177 GLN A O 1 +ATOM 1401 C CB . GLN A 1 178 ? 7.540 114.677 94.063 1.00 63.75 ? 177 GLN A CB 1 +ATOM 1402 C CG . GLN A 1 178 ? 9.001 114.854 94.407 1.00 106.89 ? 177 GLN A CG 1 +ATOM 1403 C CD . GLN A 1 178 ? 9.681 115.869 93.526 1.00 94.45 ? 177 GLN A CD 1 +ATOM 1404 O OE1 . GLN A 1 178 ? 9.170 116.974 93.333 1.00 105.67 ? 177 GLN A OE1 1 +ATOM 1405 N NE2 . GLN A 1 178 ? 10.839 115.503 92.977 1.00 103.47 ? 177 GLN A NE2 1 +ATOM 1406 N N . LEU A 1 179 ? 9.041 112.570 91.672 1.00 98.26 ? 178 LEU A N 1 +ATOM 1407 C CA . LEU A 1 179 ? 9.827 111.346 91.514 1.00 85.01 ? 178 LEU A CA 1 +ATOM 1408 C C . LEU A 1 179 ? 11.061 111.352 92.410 1.00 83.69 ? 178 LEU A C 1 +ATOM 1409 O O . LEU A 1 179 ? 11.620 112.410 92.683 1.00 103.02 ? 178 LEU A O 1 +ATOM 1410 C CB . LEU A 1 179 ? 10.214 111.114 90.046 1.00 89.04 ? 178 LEU A CB 1 +ATOM 1411 C CG . LEU A 1 179 ? 9.087 110.837 89.035 1.00 112.32 ? 178 LEU A CG 1 +ATOM 1412 C CD1 . LEU A 1 179 ? 9.606 110.771 87.600 1.00 132.14 ? 178 LEU A CD1 1 +ATOM 1413 C CD2 . LEU A 1 179 ? 8.329 109.553 89.372 1.00 78.79 ? 178 LEU A CD2 1 +ATOM 1414 N N . ALA A 1 180 ? 11.479 110.171 92.862 1.00 77.31 ? 179 ALA A N 1 +ATOM 1415 C CA . ALA A 1 180 ? 12.640 110.050 93.749 1.00 85.64 ? 179 ALA A CA 1 +ATOM 1416 C C . ALA A 1 180 ? 13.591 108.909 93.367 1.00 85.80 ? 179 ALA A C 1 +ATOM 1417 O O . ALA A 1 180 ? 13.645 107.870 94.022 1.00 101.91 ? 179 ALA A O 1 +ATOM 1418 C CB . ALA A 1 180 ? 12.195 109.919 95.202 1.00 96.16 ? 179 ALA A CB 1 +ATOM 1419 N N . ASP A 1 181 ? 14.357 109.132 92.311 1.00 85.53 ? 180 ASP A N 1 +ATOM 1420 C CA . ASP A 1 181 ? 15.273 108.135 91.762 1.00 109.65 ? 180 ASP A CA 1 +ATOM 1421 C C . ASP A 1 181 ? 16.328 107.614 92.776 1.00 95.09 ? 180 ASP A C 1 +ATOM 1422 O O . ASP A 1 181 ? 17.310 108.293 93.070 1.00 99.22 ? 180 ASP A O 1 +ATOM 1423 C CB . ASP A 1 181 ? 15.934 108.742 90.518 1.00 103.76 ? 180 ASP A CB 1 +ATOM 1424 C CG . ASP A 1 181 ? 16.329 107.709 89.489 1.00 113.90 ? 180 ASP A CG 1 +ATOM 1425 O OD1 . ASP A 1 181 ? 16.598 106.547 89.856 1.00 133.33 ? 180 ASP A OD1 1 +ATOM 1426 O OD2 . ASP A 1 181 ? 16.388 108.075 88.301 1.00 126.53 ? 180 ASP A OD2 1 +ATOM 1427 N N . HIS A 1 182 ? 16.126 106.404 93.300 1.00 79.88 ? 181 HIS A N 1 +ATOM 1428 C CA . HIS A 1 182 ? 17.043 105.839 94.306 1.00 101.38 ? 181 HIS A CA 1 +ATOM 1429 C C . HIS A 1 182 ? 18.130 104.936 93.739 1.00 91.98 ? 181 HIS A C 1 +ATOM 1430 O O . HIS A 1 182 ? 17.826 103.955 93.065 1.00 83.92 ? 181 HIS A O 1 +ATOM 1431 C CB . HIS A 1 182 ? 16.292 104.985 95.329 1.00 87.40 ? 181 HIS A CB 1 +ATOM 1432 C CG . HIS A 1 182 ? 15.391 105.751 96.240 1.00 77.31 ? 181 HIS A CG 1 +ATOM 1433 N ND1 . HIS A 1 182 ? 14.275 106.419 95.791 1.00 89.77 ? 181 HIS A ND1 1 +ATOM 1434 C CD2 . HIS A 1 182 ? 15.417 105.917 97.583 1.00 72.94 ? 181 HIS A CD2 1 +ATOM 1435 C CE1 . HIS A 1 182 ? 13.666 106.988 96.817 1.00 102.03 ? 181 HIS A CE1 1 +ATOM 1436 N NE2 . HIS A 1 182 ? 14.335 106.694 97.916 1.00 75.97 ? 181 HIS A NE2 1 +ATOM 1437 N N . TYR A 1 183 ? 19.383 105.232 94.076 1.00 114.32 ? 182 TYR A N 1 +ATOM 1438 C CA . TYR A 1 183 ? 20.525 104.391 93.706 1.00 108.17 ? 182 TYR A CA 1 +ATOM 1439 C C . TYR A 1 183 ? 21.217 103.873 94.969 1.00 95.95 ? 182 TYR A C 1 +ATOM 1440 O O . TYR A 1 183 ? 21.876 104.636 95.677 1.00 120.01 ? 182 TYR A O 1 +ATOM 1441 C CB . TYR A 1 183 ? 21.523 105.175 92.838 1.00 82.37 ? 182 TYR A CB 1 +ATOM 1442 C CG . TYR A 1 183 ? 20.995 105.529 91.462 1.00 94.41 ? 182 TYR A CG 1 +ATOM 1443 C CD1 . TYR A 1 183 ? 20.046 106.528 91.299 1.00 109.70 ? 182 TYR A CD1 1 +ATOM 1444 C CD2 . TYR A 1 183 ? 21.442 104.866 90.329 1.00 72.85 ? 182 TYR A CD2 1 +ATOM 1445 C CE1 . TYR A 1 183 ? 19.551 106.856 90.050 1.00 100.73 ? 182 TYR A CE1 1 +ATOM 1446 C CE2 . TYR A 1 183 ? 20.952 105.188 89.070 1.00 106.00 ? 182 TYR A CE2 1 +ATOM 1447 C CZ . TYR A 1 183 ? 20.000 106.186 88.936 1.00 108.51 ? 182 TYR A CZ 1 +ATOM 1448 O OH . TYR A 1 183 ? 19.494 106.521 87.692 1.00 110.03 ? 182 TYR A OH 1 +ATOM 1449 N N . GLN A 1 184 ? 21.083 102.576 95.239 1.00 92.97 ? 183 GLN A N 1 +ATOM 1450 C CA . GLN A 1 184 ? 21.506 102.002 96.521 1.00 115.60 ? 183 GLN A CA 1 +ATOM 1451 C C . GLN A 1 184 ? 22.628 100.966 96.408 1.00 107.75 ? 183 GLN A C 1 +ATOM 1452 O O . GLN A 1 184 ? 22.777 100.312 95.375 1.00 95.87 ? 183 GLN A O 1 +ATOM 1453 C CB . GLN A 1 184 ? 20.292 101.369 97.204 1.00 104.71 ? 183 GLN A CB 1 +ATOM 1454 C CG . GLN A 1 184 ? 20.575 100.594 98.471 1.00 105.61 ? 183 GLN A CG 1 +ATOM 1455 C CD . GLN A 1 184 ? 19.358 99.839 98.936 1.00 116.55 ? 183 GLN A CD 1 +ATOM 1456 O OE1 . GLN A 1 184 ? 18.228 100.205 98.601 1.00 89.93 ? 183 GLN A OE1 1 +ATOM 1457 N NE2 . GLN A 1 184 ? 19.575 98.769 99.699 1.00 87.55 ? 183 GLN A NE2 1 +ATOM 1458 N N . GLN A 1 185 ? 23.416 100.807 97.468 1.00 84.22 ? 184 GLN A N 1 +ATOM 1459 C CA . GLN A 1 185 ? 24.429 99.761 97.469 1.00 93.01 ? 184 GLN A CA 1 +ATOM 1460 C C . GLN A 1 185 ? 24.761 99.197 98.856 1.00 125.07 ? 184 GLN A C 1 +ATOM 1461 O O . GLN A 1 185 ? 24.953 99.941 99.822 1.00 98.22 ? 184 GLN A O 1 +ATOM 1462 C CB . GLN A 1 185 ? 25.689 100.230 96.740 1.00 117.21 ? 184 GLN A CB 1 +ATOM 1463 C CG . GLN A 1 185 ? 26.460 101.342 97.416 1.00 146.92 ? 184 GLN A CG 1 +ATOM 1464 C CD . GLN A 1 185 ? 27.790 101.586 96.733 1.00 176.31 ? 184 GLN A CD 1 +ATOM 1465 O OE1 . GLN A 1 185 ? 27.980 101.209 95.575 1.00 184.43 ? 184 GLN A OE1 1 +ATOM 1466 N NE2 . GLN A 1 185 ? 28.724 102.204 97.450 1.00 185.94 ? 184 GLN A NE2 1 +ATOM 1467 N N . ASN A 1 186 ? 24.832 97.869 98.933 1.00 114.33 ? 185 ASN A N 1 +ATOM 1468 C CA . ASN A 1 186 ? 25.011 97.168 100.200 1.00 112.67 ? 185 ASN A CA 1 +ATOM 1469 C C . ASN A 1 186 ? 26.292 96.333 100.254 1.00 129.22 ? 185 ASN A C 1 +ATOM 1470 O O . ASN A 1 186 ? 26.747 95.821 99.228 1.00 108.34 ? 185 ASN A O 1 +ATOM 1471 C CB . ASN A 1 186 ? 23.795 96.289 100.474 1.00 113.83 ? 185 ASN A CB 1 +ATOM 1472 C CG . ASN A 1 186 ? 22.541 97.098 100.746 1.00 108.78 ? 185 ASN A CG 1 +ATOM 1473 O OD1 . ASN A 1 186 ? 21.836 97.523 99.827 1.00 105.25 ? 185 ASN A OD1 1 +ATOM 1474 N ND2 . ASN A 1 186 ? 22.252 97.307 102.021 1.00 86.04 ? 185 ASN A ND2 1 +ATOM 1475 N N . THR A 1 187 ? 26.851 96.196 101.461 1.00 109.70 ? 186 THR A N 1 +ATOM 1476 C CA . THR A 1 187 ? 28.182 95.611 101.671 1.00 112.50 ? 186 THR A CA 1 +ATOM 1477 C C . THR A 1 187 ? 28.443 95.166 103.117 1.00 106.28 ? 186 THR A C 1 +ATOM 1478 O O . THR A 1 187 ? 28.358 95.975 104.044 1.00 125.41 ? 186 THR A O 1 +ATOM 1479 C CB . THR A 1 187 ? 29.299 96.601 101.273 1.00 111.59 ? 186 THR A CB 1 +ATOM 1480 O OG1 . THR A 1 187 ? 29.354 96.714 99.845 1.00 129.24 ? 186 THR A OG1 1 +ATOM 1481 C CG2 . THR A 1 187 ? 30.659 96.130 101.806 1.00 102.58 ? 186 THR A CG2 1 +ATOM 1482 N N . PRO A 1 188 ? 28.797 93.881 103.305 1.00 119.14 ? 187 PRO A N 1 +ATOM 1483 C CA . PRO A 1 188 ? 29.022 93.288 104.631 1.00 121.64 ? 187 PRO A CA 1 +ATOM 1484 C C . PRO A 1 188 ? 30.189 93.873 105.427 1.00 121.61 ? 187 PRO A C 1 +ATOM 1485 O O . PRO A 1 188 ? 31.342 93.874 104.989 1.00 129.67 ? 187 PRO A O 1 +ATOM 1486 C CB . PRO A 1 188 ? 29.307 91.815 104.315 1.00 121.23 ? 187 PRO A CB 1 +ATOM 1487 C CG . PRO A 1 188 ? 29.807 91.815 102.897 1.00 117.08 ? 187 PRO A CG 1 +ATOM 1488 C CD . PRO A 1 188 ? 29.006 92.899 102.224 1.00 109.85 ? 187 PRO A CD 1 +ATOM 1489 N N . ILE A 1 189 ? 29.857 94.355 106.617 1.00 123.15 ? 188 ILE A N 1 +ATOM 1490 C CA . ILE A 1 189 ? 30.828 94.742 107.625 1.00 124.13 ? 188 ILE A CA 1 +ATOM 1491 C C . ILE A 1 189 ? 31.631 93.519 108.054 1.00 136.03 ? 188 ILE A C 1 +ATOM 1492 O O . ILE A 1 189 ? 32.806 93.623 108.415 1.00 129.61 ? 188 ILE A O 1 +ATOM 1493 C CB . ILE A 1 189 ? 30.088 95.307 108.846 1.00 111.32 ? 188 ILE A CB 1 +ATOM 1494 C CG1 . ILE A 1 189 ? 29.188 96.470 108.403 1.00 114.92 ? 188 ILE A CG1 1 +ATOM 1495 C CG2 . ILE A 1 189 ? 31.069 95.705 109.944 1.00 98.78 ? 188 ILE A CG2 1 +ATOM 1496 C CD1 . ILE A 1 189 ? 28.122 96.878 109.400 1.00 118.51 ? 188 ILE A CD1 1 +ATOM 1497 N N . GLY A 1 190 ? 30.981 92.360 108.001 1.00 145.79 ? 189 GLY A N 1 +ATOM 1498 C CA . GLY A 1 190 ? 31.584 91.107 108.417 1.00 148.80 ? 189 GLY A CA 1 +ATOM 1499 C C . GLY A 1 190 ? 32.439 90.449 107.350 1.00 158.68 ? 189 GLY A C 1 +ATOM 1500 O O . GLY A 1 190 ? 32.269 90.696 106.153 1.00 134.74 ? 189 GLY A O 1 +ATOM 1501 N N . ASP A 1 191 ? 33.362 89.599 107.793 1.00 160.51 ? 190 ASP A N 1 +ATOM 1502 C CA . ASP A 1 191 ? 34.322 88.966 106.892 1.00 164.96 ? 190 ASP A CA 1 +ATOM 1503 C C . ASP A 1 191 ? 33.816 87.617 106.381 1.00 162.28 ? 190 ASP A C 1 +ATOM 1504 O O . ASP A 1 191 ? 34.343 87.073 105.407 1.00 146.61 ? 190 ASP A O 1 +ATOM 1505 C CB . ASP A 1 191 ? 35.691 88.811 107.569 1.00 165.57 ? 190 ASP A CB 1 +ATOM 1506 C CG . ASP A 1 191 ? 36.348 90.147 107.890 1.00 181.23 ? 190 ASP A CG 1 +ATOM 1507 O OD1 . ASP A 1 191 ? 36.408 91.023 107.003 1.00 165.10 ? 190 ASP A OD1 1 +ATOM 1508 O OD2 . ASP A 1 191 ? 36.817 90.317 109.034 1.00 188.21 ? 190 ASP A OD2 1 +ATOM 1509 N N . GLY A 1 192 ? 32.788 87.088 107.041 1.00 165.09 ? 191 GLY A N 1 +ATOM 1510 C CA . GLY A 1 192 ? 32.175 85.830 106.644 1.00 165.26 ? 191 GLY A CA 1 +ATOM 1511 C C . GLY A 1 192 ? 31.491 85.893 105.288 1.00 177.76 ? 191 GLY A C 1 +ATOM 1512 O O . GLY A 1 192 ? 31.192 86.980 104.791 1.00 176.79 ? 191 GLY A O 1 +ATOM 1513 N N . PRO A 1 193 ? 31.234 84.722 104.678 1.00 180.05 ? 192 PRO A N 1 +ATOM 1514 C CA . PRO A 1 193 ? 30.629 84.694 103.343 1.00 179.80 ? 192 PRO A CA 1 +ATOM 1515 C C . PRO A 1 193 ? 29.146 85.053 103.383 1.00 168.93 ? 192 PRO A C 1 +ATOM 1516 O O . PRO A 1 193 ? 28.481 84.864 104.406 1.00 133.10 ? 192 PRO A O 1 +ATOM 1517 C CB . PRO A 1 193 ? 30.820 83.242 102.905 1.00 170.10 ? 192 PRO A CB 1 +ATOM 1518 C CG . PRO A 1 193 ? 30.808 82.473 104.182 1.00 156.44 ? 192 PRO A CG 1 +ATOM 1519 C CD . PRO A 1 193 ? 31.441 83.368 105.222 1.00 159.57 ? 192 PRO A CD 1 +ATOM 1520 N N . VAL A 1 194 ? 28.645 85.584 102.273 1.00 155.47 ? 193 VAL A N 1 +ATOM 1521 C CA . VAL A 1 194 ? 27.256 86.008 102.182 1.00 144.80 ? 193 VAL A CA 1 +ATOM 1522 C C . VAL A 1 194 ? 26.671 85.516 100.871 1.00 120.05 ? 193 VAL A C 1 +ATOM 1523 O O . VAL A 1 194 ? 27.403 85.202 99.942 1.00 121.80 ? 193 VAL A O 1 +ATOM 1524 C CB . VAL A 1 194 ? 27.119 87.545 102.247 1.00 152.46 ? 193 VAL A CB 1 +ATOM 1525 C CG1 . VAL A 1 194 ? 27.659 88.081 103.575 1.00 107.04 ? 193 VAL A CG1 1 +ATOM 1526 C CG2 . VAL A 1 194 ? 27.817 88.200 101.054 1.00 136.12 ? 193 VAL A CG2 1 +ATOM 1527 N N . LEU A 1 195 ? 25.351 85.444 100.800 1.00 109.40 ? 194 LEU A N 1 +ATOM 1528 C CA . LEU A 1 195 ? 24.687 85.000 99.586 1.00 100.32 ? 194 LEU A CA 1 +ATOM 1529 C C . LEU A 1 195 ? 24.715 86.118 98.564 1.00 107.18 ? 194 LEU A C 1 +ATOM 1530 O O . LEU A 1 195 ? 24.420 87.263 98.886 1.00 133.02 ? 194 LEU A O 1 +ATOM 1531 C CB . LEU A 1 195 ? 23.249 84.583 99.884 1.00 93.27 ? 194 LEU A CB 1 +ATOM 1532 C CG . LEU A 1 195 ? 23.114 83.547 101.004 1.00 118.79 ? 194 LEU A CG 1 +ATOM 1533 C CD1 . LEU A 1 195 ? 21.665 83.102 101.157 1.00 111.03 ? 194 LEU A CD1 1 +ATOM 1534 C CD2 . LEU A 1 195 ? 24.048 82.353 100.784 1.00 93.11 ? 194 LEU A CD2 1 +ATOM 1535 N N . LEU A 1 196 ? 25.093 85.790 97.336 1.00 100.26 ? 195 LEU A N 1 +ATOM 1536 C CA . LEU A 1 196 ? 25.102 86.781 96.272 1.00 131.35 ? 195 LEU A CA 1 +ATOM 1537 C C . LEU A 1 196 ? 24.044 86.399 95.241 1.00 120.00 ? 195 LEU A C 1 +ATOM 1538 O O . LEU A 1 196 ? 24.249 85.491 94.439 1.00 125.52 ? 195 LEU A O 1 +ATOM 1539 C CB . LEU A 1 196 ? 26.503 86.908 95.669 1.00 154.15 ? 195 LEU A CB 1 +ATOM 1540 C CG . LEU A 1 196 ? 27.572 87.158 96.746 1.00 132.86 ? 195 LEU A CG 1 +ATOM 1541 C CD1 . LEU A 1 196 ? 28.985 87.105 96.190 1.00 118.55 ? 195 LEU A CD1 1 +ATOM 1542 C CD2 . LEU A 1 196 ? 27.331 88.482 97.461 1.00 120.25 ? 195 LEU A CD2 1 +ATOM 1543 N N . PRO A 1 197 ? 22.898 87.097 95.280 1.00 117.94 ? 196 PRO A N 1 +ATOM 1544 C CA . PRO A 1 197 ? 21.643 86.759 94.588 1.00 121.53 ? 196 PRO A CA 1 +ATOM 1545 C C . PRO A 1 197 ? 21.631 86.866 93.061 1.00 115.58 ? 196 PRO A C 1 +ATOM 1546 O O . PRO A 1 197 ? 22.425 87.588 92.455 1.00 115.51 ? 196 PRO A O 1 +ATOM 1547 C CB . PRO A 1 197 ? 20.648 87.774 95.163 1.00 119.34 ? 196 PRO A CB 1 +ATOM 1548 C CG . PRO A 1 197 ? 21.491 88.934 95.581 1.00 109.73 ? 196 PRO A CG 1 +ATOM 1549 C CD . PRO A 1 197 ? 22.766 88.324 96.086 1.00 102.20 ? 196 PRO A CD 1 +ATOM 1550 N N . ASP A 1 198 ? 20.705 86.130 92.453 1.00 129.35 ? 197 ASP A N 1 +ATOM 1551 C CA . ASP A 1 198 ? 20.346 86.335 91.059 1.00 136.90 ? 197 ASP A CA 1 +ATOM 1552 C C . ASP A 1 198 ? 19.411 87.535 91.037 1.00 120.61 ? 197 ASP A C 1 +ATOM 1553 O O . ASP A 1 198 ? 18.904 87.941 92.080 1.00 112.96 ? 197 ASP A O 1 +ATOM 1554 C CB . ASP A 1 198 ? 19.645 85.096 90.481 1.00 140.22 ? 197 ASP A CB 1 +ATOM 1555 C CG . ASP A 1 198 ? 20.597 83.916 90.274 1.00 152.53 ? 197 ASP A CG 1 +ATOM 1556 O OD1 . ASP A 1 198 ? 21.829 84.129 90.315 1.00 151.93 ? 197 ASP A OD1 1 +ATOM 1557 O OD2 . ASP A 1 198 ? 20.112 82.778 90.057 1.00 137.13 ? 197 ASP A OD2 1 +ATOM 1558 N N . ASN A 1 199 ? 19.197 88.111 89.861 1.00 110.46 ? 198 ASN A N 1 +ATOM 1559 C CA . ASN A 1 199 ? 18.267 89.225 89.718 1.00 126.32 ? 198 ASN A CA 1 +ATOM 1560 C C . ASN A 1 199 ? 16.877 88.888 90.239 1.00 120.74 ? 198 ASN A C 1 +ATOM 1561 O O . ASN A 1 199 ? 16.257 87.934 89.774 1.00 116.05 ? 198 ASN A O 1 +ATOM 1562 C CB . ASN A 1 199 ? 18.146 89.633 88.249 1.00 147.39 ? 198 ASN A CB 1 +ATOM 1563 C CG . ASN A 1 199 ? 19.414 90.253 87.703 1.00 144.71 ? 198 ASN A CG 1 +ATOM 1564 O OD1 . ASN A 1 199 ? 20.492 90.123 88.293 1.00 102.88 ? 198 ASN A OD1 1 +ATOM 1565 N ND2 . ASN A 1 199 ? 19.294 90.933 86.564 1.00 134.83 ? 198 ASN A ND2 1 +ATOM 1566 N N . HIS A 1 200 ? 16.395 89.667 91.203 1.00 108.94 ? 199 HIS A N 1 +ATOM 1567 C CA . HIS A 1 200 ? 15.001 89.588 91.645 1.00 112.28 ? 199 HIS A CA 1 +ATOM 1568 C C . HIS A 1 200 ? 14.598 90.927 92.217 1.00 102.64 ? 199 HIS A C 1 +ATOM 1569 O O . HIS A 1 200 ? 15.412 91.836 92.273 1.00 102.19 ? 199 HIS A O 1 +ATOM 1570 C CB . HIS A 1 200 ? 14.806 88.512 92.706 1.00 93.81 ? 199 HIS A CB 1 +ATOM 1571 C CG . HIS A 1 200 ? 15.479 88.814 94.008 1.00 91.68 ? 199 HIS A CG 1 +ATOM 1572 N ND1 . HIS A 1 200 ? 16.835 88.660 94.195 1.00 101.70 ? 199 HIS A ND1 1 +ATOM 1573 C CD2 . HIS A 1 200 ? 14.982 89.245 95.192 1.00 104.46 ? 199 HIS A CD2 1 +ATOM 1574 C CE1 . HIS A 1 200 ? 17.147 88.988 95.436 1.00 103.48 ? 199 HIS A CE1 1 +ATOM 1575 N NE2 . HIS A 1 200 ? 16.040 89.344 96.063 1.00 110.68 ? 199 HIS A NE2 1 +ATOM 1576 N N . TYR A 1 201 ? 13.353 91.053 92.656 1.00 93.04 ? 200 TYR A N 1 +ATOM 1577 C CA . TYR A 1 201 ? 12.900 92.315 93.233 1.00 93.83 ? 200 TYR A CA 1 +ATOM 1578 C C . TYR A 1 201 ? 12.183 92.137 94.590 1.00 88.70 ? 200 TYR A C 1 +ATOM 1579 O O . TYR A 1 201 ? 11.925 91.010 94.998 1.00 91.70 ? 200 TYR A O 1 +ATOM 1580 C CB . TYR A 1 201 ? 12.065 93.087 92.203 1.00 88.85 ? 200 TYR A CB 1 +ATOM 1581 C CG . TYR A 1 201 ? 10.710 92.498 91.884 1.00 108.96 ? 200 TYR A CG 1 +ATOM 1582 C CD1 . TYR A 1 201 ? 10.570 91.436 90.994 1.00 102.99 ? 200 TYR A CD1 1 +ATOM 1583 C CD2 . TYR A 1 201 ? 9.561 93.021 92.459 1.00 110.91 ? 200 TYR A CD2 1 +ATOM 1584 C CE1 . TYR A 1 201 ? 9.309 90.904 90.698 1.00 99.51 ? 200 TYR A CE1 1 +ATOM 1585 C CE2 . TYR A 1 201 ? 8.303 92.500 92.171 1.00 120.85 ? 200 TYR A CE2 1 +ATOM 1586 C CZ . TYR A 1 201 ? 8.181 91.441 91.290 1.00 105.74 ? 200 TYR A CZ 1 +ATOM 1587 O OH . TYR A 1 201 ? 6.934 90.922 91.008 1.00 100.68 ? 200 TYR A OH 1 +ATOM 1588 N N . LEU A 1 202 ? 11.926 93.231 95.313 1.00 103.65 ? 201 LEU A N 1 +ATOM 1589 C CA . LEU A 1 202 ? 11.127 93.180 96.548 1.00 109.25 ? 201 LEU A CA 1 +ATOM 1590 C C . LEU A 1 202 ? 9.872 93.993 96.305 1.00 87.54 ? 201 LEU A C 1 +ATOM 1591 O O . LEU A 1 202 ? 9.946 95.145 95.913 1.00 72.91 ? 201 LEU A O 1 +ATOM 1592 C CB . LEU A 1 202 ? 11.878 93.745 97.769 1.00 71.21 ? 201 LEU A CB 1 +ATOM 1593 C CG . LEU A 1 202 ? 13.194 93.135 98.288 1.00 98.35 ? 201 LEU A CG 1 +ATOM 1594 C CD1 . LEU A 1 202 ? 13.581 93.662 99.669 1.00 80.69 ? 201 LEU A CD1 1 +ATOM 1595 C CD2 . LEU A 1 202 ? 13.168 91.614 98.305 1.00 112.11 ? 201 LEU A CD2 1 +ATOM 1596 N N . SER A 1 203 ? 8.712 93.397 96.502 1.00 85.80 ? 202 SER A N 1 +ATOM 1597 C CA . SER A 1 203 ? 7.492 94.142 96.288 1.00 85.63 ? 202 SER A CA 1 +ATOM 1598 C C . SER A 1 203 ? 7.137 94.783 97.610 1.00 71.51 ? 202 SER A C 1 +ATOM 1599 O O . SER A 1 203 ? 6.832 94.084 98.580 1.00 100.95 ? 202 SER A O 1 +ATOM 1600 C CB . SER A 1 203 ? 6.378 93.216 95.818 1.00 79.53 ? 202 SER A CB 1 +ATOM 1601 O OG . SER A 1 203 ? 5.179 93.934 95.607 1.00 113.86 ? 202 SER A OG 1 +ATOM 1602 N N . THR A 1 204 ? 7.198 96.111 97.654 1.00 94.85 ? 203 THR A N 1 +ATOM 1603 C CA . THR A 1 204 ? 6.942 96.838 98.892 1.00 103.14 ? 203 THR A CA 1 +ATOM 1604 C C . THR A 1 204 ? 5.597 97.562 98.881 1.00 93.47 ? 203 THR A C 1 +ATOM 1605 O O . THR A 1 204 ? 5.172 98.083 97.851 1.00 94.11 ? 203 THR A O 1 +ATOM 1606 C CB . THR A 1 204 ? 8.051 97.862 99.216 1.00 94.78 ? 203 THR A CB 1 +ATOM 1607 O OG1 . THR A 1 204 ? 9.337 97.237 99.118 1.00 91.50 ? 203 THR A OG1 1 +ATOM 1608 C CG2 . THR A 1 204 ? 7.873 98.378 100.633 1.00 139.10 ? 203 THR A CG2 1 +ATOM 1609 N N . GLN A 1 205 ? 4.926 97.546 100.034 1.00 85.42 ? 204 GLN A N 1 +ATOM 1610 C CA . GLN A 1 205 ? 3.753 98.380 100.304 1.00 84.58 ? 204 GLN A CA 1 +ATOM 1611 C C . GLN A 1 205 ? 3.848 98.969 101.712 1.00 88.68 ? 204 GLN A C 1 +ATOM 1612 O O . GLN A 1 205 ? 4.302 98.307 102.649 1.00 67.91 ? 204 GLN A O 1 +ATOM 1613 C CB . GLN A 1 205 ? 2.449 97.590 100.179 1.00 89.75 ? 204 GLN A CB 1 +ATOM 1614 C CG . GLN A 1 205 ? 2.344 96.735 98.944 1.00 82.97 ? 204 GLN A CG 1 +ATOM 1615 C CD . GLN A 1 205 ? 1.767 95.382 99.252 1.00 105.45 ? 204 GLN A CD 1 +ATOM 1616 O OE1 . GLN A 1 205 ? 0.548 95.226 99.353 1.00 147.93 ? 204 GLN A OE1 1 +ATOM 1617 N NE2 . GLN A 1 205 ? 2.641 94.387 99.423 1.00 102.88 ? 204 GLN A NE2 1 +ATOM 1618 N N . SER A 1 206 ? 3.397 100.214 101.843 1.00 87.39 ? 205 SER A N 1 +ATOM 1619 C CA . SER A 1 206 ? 3.532 100.993 103.068 1.00 74.16 ? 205 SER A CA 1 +ATOM 1620 C C . SER A 1 206 ? 2.312 101.901 103.251 1.00 60.23 ? 205 SER A C 1 +ATOM 1621 O O . SER A 1 206 ? 1.678 102.286 102.270 1.00 95.58 ? 205 SER A O 1 +ATOM 1622 C CB . SER A 1 206 ? 4.819 101.830 103.019 1.00 70.49 ? 205 SER A CB 1 +ATOM 1623 O OG . SER A 1 206 ? 5.960 101.013 102.799 1.00 113.07 ? 205 SER A OG 1 +ATOM 1624 N N . ASN A 1 207 ? 1.955 102.181 104.507 1.00 73.99 ? 206 ASN A N 1 +ATOM 1625 C CA . ASN A 1 207 ? 1.017 103.258 104.853 1.00 78.25 ? 206 ASN A CA 1 +ATOM 1626 C C . ASN A 1 207 ? 1.570 104.075 106.019 1.00 93.70 ? 206 ASN A C 1 +ATOM 1627 O O . ASN A 1 207 ? 2.285 103.536 106.871 1.00 72.76 ? 206 ASN A O 1 +ATOM 1628 C CB . ASN A 1 207 ? -0.410 102.735 105.126 1.00 58.69 ? 206 ASN A CB 1 +ATOM 1629 C CG . ASN A 1 207 ? -1.018 103.256 106.441 1.00 73.14 ? 206 ASN A CG 1 +ATOM 1630 O OD1 . ASN A 1 207 ? -0.409 103.171 107.503 1.00 66.19 ? 206 ASN A OD1 1 +ATOM 1631 N ND2 . ASN A 1 207 ? -2.253 103.750 106.370 1.00 63.35 ? 206 ASN A ND2 1 +ATOM 1632 N N . LEU A 1 208 ? 1.215 105.360 106.060 1.00 64.44 ? 207 LEU A N 1 +ATOM 1633 C CA . LEU A 1 208 ? 1.697 106.276 107.089 1.00 50.42 ? 207 LEU A CA 1 +ATOM 1634 C C . LEU A 1 208 ? 0.552 106.836 107.915 1.00 46.47 ? 207 LEU A C 1 +ATOM 1635 O O . LEU A 1 208 ? -0.458 107.283 107.365 1.00 97.82 ? 207 LEU A O 1 +ATOM 1636 C CB . LEU A 1 208 ? 2.437 107.439 106.443 1.00 63.89 ? 207 LEU A CB 1 +ATOM 1637 C CG . LEU A 1 208 ? 3.291 107.121 105.224 1.00 65.13 ? 207 LEU A CG 1 +ATOM 1638 C CD1 . LEU A 1 208 ? 3.630 108.422 104.554 1.00 79.86 ? 207 LEU A CD1 1 +ATOM 1639 C CD2 . LEU A 1 208 ? 4.549 106.367 105.601 1.00 70.99 ? 207 LEU A CD2 1 +ATOM 1640 N N . SER A 1 209 ? 0.739 106.840 109.237 1.00 73.81 ? 208 SER A N 1 +ATOM 1641 C CA . SER A 1 209 ? -0.288 107.274 110.195 1.00 61.04 ? 208 SER A CA 1 +ATOM 1642 C C . SER A 1 209 ? 0.225 108.087 111.400 1.00 86.83 ? 208 SER A C 1 +ATOM 1643 O O . SER A 1 209 ? 1.437 108.245 111.612 1.00 67.32 ? 208 SER A O 1 +ATOM 1644 C CB . SER A 1 209 ? -1.050 106.058 110.713 1.00 68.06 ? 208 SER A CB 1 +ATOM 1645 O OG . SER A 1 209 ? -0.145 105.028 111.074 1.00 90.14 ? 208 SER A OG 1 +ATOM 1646 N N . LYS A 1 210 ? -0.725 108.591 112.189 1.00 84.61 ? 209 LYS A N 1 +ATOM 1647 C CA . LYS A 1 210 ? -0.421 109.298 113.433 1.00 62.62 ? 209 LYS A CA 1 +ATOM 1648 C C . LYS A 1 210 ? -0.995 108.587 114.656 1.00 82.12 ? 209 LYS A C 1 +ATOM 1649 O O . LYS A 1 210 ? -2.160 108.201 114.670 1.00 96.79 ? 209 LYS A O 1 +ATOM 1650 C CB . LYS A 1 210 ? -1.000 110.721 113.421 1.00 91.11 ? 209 LYS A CB 1 +ATOM 1651 C CG . LYS A 1 210 ? -0.546 111.636 112.290 1.00 79.52 ? 209 LYS A CG 1 +ATOM 1652 C CD . LYS A 1 210 ? 0.919 112.008 112.395 1.00 83.87 ? 209 LYS A CD 1 +ATOM 1653 C CE . LYS A 1 210 ? 1.255 113.091 111.388 1.00 69.29 ? 209 LYS A CE 1 +ATOM 1654 N NZ . LYS A 1 210 ? 2.721 113.218 111.221 1.00 74.35 ? 209 LYS A NZ 1 +ATOM 1655 N N . ASP A 1 211 ? -0.161 108.438 115.680 1.00 97.84 ? 210 ASP A N 1 +ATOM 1656 C CA . ASP A 1 211 ? -0.577 108.139 117.051 1.00 70.39 ? 210 ASP A CA 1 +ATOM 1657 C C . ASP A 1 211 ? -1.347 109.324 117.641 1.00 83.96 ? 210 ASP A C 1 +ATOM 1658 O O . ASP A 1 211 ? -0.854 110.445 117.638 1.00 96.39 ? 210 ASP A O 1 +ATOM 1659 C CB . ASP A 1 211 ? 0.675 107.902 117.895 1.00 78.62 ? 210 ASP A CB 1 +ATOM 1660 C CG . ASP A 1 211 ? 0.365 107.354 119.272 1.00 106.72 ? 210 ASP A CG 1 +ATOM 1661 O OD1 . ASP A 1 211 ? -0.782 107.512 119.739 1.00 102.80 ? 210 ASP A OD1 1 +ATOM 1662 O OD2 . ASP A 1 211 ? 1.280 106.764 119.891 1.00 96.43 ? 210 ASP A OD2 1 +ATOM 1663 N N . PRO A 1 212 ? -2.553 109.083 118.170 1.00 107.31 ? 211 PRO A N 1 +ATOM 1664 C CA . PRO A 1 212 ? -3.310 110.220 118.713 1.00 103.44 ? 211 PRO A CA 1 +ATOM 1665 C C . PRO A 1 212 ? -2.990 110.600 120.181 1.00 104.72 ? 211 PRO A C 1 +ATOM 1666 O O . PRO A 1 212 ? -3.610 111.525 120.715 1.00 89.74 ? 211 PRO A O 1 +ATOM 1667 C CB . PRO A 1 212 ? -4.762 109.760 118.563 1.00 103.60 ? 211 PRO A CB 1 +ATOM 1668 C CG . PRO A 1 212 ? -4.684 108.260 118.694 1.00 108.33 ? 211 PRO A CG 1 +ATOM 1669 C CD . PRO A 1 212 ? -3.365 107.853 118.083 1.00 88.48 ? 211 PRO A CD 1 +ATOM 1670 N N . ASN A 1 213 ? -2.049 109.906 120.820 1.00 126.83 ? 212 ASN A N 1 +ATOM 1671 C CA . ASN A 1 213 ? -1.601 110.276 122.169 1.00 142.20 ? 212 ASN A CA 1 +ATOM 1672 C C . ASN A 1 213 ? -0.128 110.681 122.142 1.00 124.60 ? 212 ASN A C 1 +ATOM 1673 O O . ASN A 1 213 ? 0.621 110.520 123.113 1.00 109.00 ? 212 ASN A O 1 +ATOM 1674 C CB . ASN A 1 213 ? -1.827 109.135 123.163 1.00 120.18 ? 212 ASN A CB 1 +ATOM 1675 C CG . ASN A 1 213 ? -3.189 108.486 123.012 1.00 106.60 ? 212 ASN A CG 1 +ATOM 1676 O OD1 . ASN A 1 213 ? -4.221 109.161 122.920 1.00 96.99 ? 212 ASN A OD1 1 +ATOM 1677 N ND2 . ASN A 1 213 ? -3.195 107.162 122.973 1.00 114.05 ? 212 ASN A ND2 1 +ATOM 1678 N N . GLU A 1 214 ? 0.276 111.200 120.994 1.00 109.79 ? 213 GLU A N 1 +ATOM 1679 C CA . GLU A 1 214 ? 1.637 111.614 120.780 1.00 83.33 ? 213 GLU A CA 1 +ATOM 1680 C C . GLU A 1 214 ? 1.610 113.025 120.256 1.00 83.54 ? 213 GLU A C 1 +ATOM 1681 O O . GLU A 1 214 ? 0.977 113.291 119.238 1.00 100.31 ? 213 GLU A O 1 +ATOM 1682 C CB . GLU A 1 214 ? 2.302 110.719 119.755 1.00 82.50 ? 213 GLU A CB 1 +ATOM 1683 C CG . GLU A 1 214 ? 3.672 111.186 119.438 1.00 74.26 ? 213 GLU A CG 1 +ATOM 1684 C CD . GLU A 1 214 ? 4.490 111.329 120.683 1.00 111.26 ? 213 GLU A CD 1 +ATOM 1685 O OE1 . GLU A 1 214 ? 5.100 110.325 121.099 1.00 93.79 ? 213 GLU A OE1 1 +ATOM 1686 O OE2 . GLU A 1 214 ? 4.514 112.438 121.255 1.00 131.52 ? 213 GLU A OE2 1 +ATOM 1687 N N . LYS A 1 215 ? 2.293 113.928 120.953 1.00 97.50 ? 214 LYS A N 1 +ATOM 1688 C CA . LYS A 1 215 ? 2.199 115.355 120.650 1.00 108.57 ? 214 LYS A CA 1 +ATOM 1689 C C . LYS A 1 215 ? 3.456 115.929 119.995 1.00 95.64 ? 214 LYS A C 1 +ATOM 1690 O O . LYS A 1 215 ? 3.411 117.007 119.402 1.00 109.24 ? 214 LYS A O 1 +ATOM 1691 C CB . LYS A 1 215 ? 1.803 116.162 121.896 1.00 89.17 ? 214 LYS A CB 1 +ATOM 1692 C CG . LYS A 1 215 ? 0.425 115.811 122.457 1.00 134.33 ? 214 LYS A CG 1 +ATOM 1693 C CD . LYS A 1 215 ? -0.034 116.803 123.532 1.00 142.79 ? 214 LYS A CD 1 +ATOM 1694 C CE . LYS A 1 215 ? 0.546 116.501 124.910 1.00 139.10 ? 214 LYS A CE 1 +ATOM 1695 N NZ . LYS A 1 215 ? 0.047 115.214 125.446 1.00 125.76 ? 214 LYS A NZ 1 +ATOM 1696 N N . ARG A 1 216 ? 4.568 115.207 120.104 1.00 56.14 ? 215 ARG A N 1 +ATOM 1697 C CA . ARG A 1 216 ? 5.776 115.529 119.346 1.00 80.02 ? 215 ARG A CA 1 +ATOM 1698 C C . ARG A 1 216 ? 5.609 115.189 117.854 1.00 69.27 ? 215 ARG A C 1 +ATOM 1699 O O . ARG A 1 216 ? 4.739 114.402 117.491 1.00 86.05 ? 215 ARG A O 1 +ATOM 1700 C CB . ARG A 1 216 ? 6.968 114.763 119.924 1.00 77.81 ? 215 ARG A CB 1 +ATOM 1701 C CG . ARG A 1 216 ? 7.358 115.168 121.342 1.00 99.08 ? 215 ARG A CG 1 +ATOM 1702 C CD . ARG A 1 216 ? 8.248 114.118 121.968 1.00 85.03 ? 215 ARG A CD 1 +ATOM 1703 N NE . ARG A 1 216 ? 7.498 112.897 122.223 1.00 115.88 ? 215 ARG A NE 1 +ATOM 1704 C CZ . ARG A 1 216 ? 7.985 111.800 122.792 1.00 106.47 ? 215 ARG A CZ 1 +ATOM 1705 N NH1 . ARG A 1 216 ? 9.253 111.744 123.182 1.00 98.25 ? 215 ARG A NH1 1 +ATOM 1706 N NH2 . ARG A 1 216 ? 7.192 110.751 122.965 1.00 76.51 ? 215 ARG A NH2 1 +ATOM 1707 N N . ASP A 1 217 ? 6.441 115.773 116.990 1.00 75.49 ? 216 ASP A N 1 +ATOM 1708 C CA . ASP A 1 217 ? 6.379 115.469 115.553 1.00 92.61 ? 216 ASP A CA 1 +ATOM 1709 C C . ASP A 1 217 ? 6.788 114.013 115.282 1.00 99.87 ? 216 ASP A C 1 +ATOM 1710 O O . ASP A 1 217 ? 7.914 113.590 115.585 1.00 89.16 ? 216 ASP A O 1 +ATOM 1711 C CB . ASP A 1 217 ? 7.233 116.453 114.734 1.00 79.48 ? 216 ASP A CB 1 +ATOM 1712 C CG . ASP A 1 217 ? 6.668 116.715 113.333 1.00 113.02 ? 216 ASP A CG 1 +ATOM 1713 O OD1 . ASP A 1 217 ? 5.486 116.388 113.089 1.00 124.30 ? 216 ASP A OD1 1 +ATOM 1714 O OD2 . ASP A 1 217 ? 7.405 117.263 112.478 1.00 73.21 ? 216 ASP A OD2 1 +ATOM 1715 N N . HIS A 1 218 ? 5.861 113.250 114.707 1.00 96.53 ? 217 HIS A N 1 +ATOM 1716 C CA . HIS A 1 218 ? 6.038 111.808 114.594 1.00 84.34 ? 217 HIS A CA 1 +ATOM 1717 C C . HIS A 1 218 ? 5.369 111.171 113.365 1.00 65.54 ? 217 HIS A C 1 +ATOM 1718 O O . HIS A 1 218 ? 4.397 111.693 112.808 1.00 90.89 ? 217 HIS A O 1 +ATOM 1719 C CB . HIS A 1 218 ? 5.546 111.123 115.880 1.00 70.45 ? 217 HIS A CB 1 +ATOM 1720 C CG . HIS A 1 218 ? 4.059 111.038 115.979 1.00 63.77 ? 217 HIS A CG 1 +ATOM 1721 N ND1 . HIS A 1 218 ? 3.257 112.153 116.084 1.00 113.00 ? 217 HIS A ND1 1 +ATOM 1722 C CD2 . HIS A 1 218 ? 3.225 109.974 115.964 1.00 90.54 ? 217 HIS A CD2 1 +ATOM 1723 C CE1 . HIS A 1 218 ? 1.991 111.780 116.132 1.00 86.16 ? 217 HIS A CE1 1 +ATOM 1724 N NE2 . HIS A 1 218 ? 1.944 110.463 116.060 1.00 98.14 ? 217 HIS A NE2 1 +ATOM 1725 N N . MET A 1 219 ? 5.911 110.031 112.953 1.00 80.43 ? 218 MET A N 1 +ATOM 1726 C CA . MET A 1 219 ? 5.277 109.183 111.948 1.00 72.04 ? 218 MET A CA 1 +ATOM 1727 C C . MET A 1 219 ? 5.161 107.740 112.454 1.00 78.35 ? 218 MET A C 1 +ATOM 1728 O O . MET A 1 219 ? 6.138 107.180 112.978 1.00 79.40 ? 218 MET A O 1 +ATOM 1729 C CB . MET A 1 219 ? 6.075 109.232 110.639 1.00 64.90 ? 218 MET A CB 1 +ATOM 1730 C CG . MET A 1 219 ? 5.648 108.250 109.579 1.00 53.36 ? 218 MET A CG 1 +ATOM 1731 S SD . MET A 1 219 ? 6.705 108.294 108.125 1.00 76.41 ? 218 MET A SD 1 +ATOM 1732 C CE . MET A 1 219 ? 8.223 107.557 108.718 1.00 76.44 ? 218 MET A CE 1 +ATOM 1733 N N . VAL A 1 220 ? 3.959 107.164 112.316 1.00 82.97 ? 219 VAL A N 1 +ATOM 1734 C CA . VAL A 1 220 ? 3.739 105.713 112.436 1.00 70.08 ? 219 VAL A CA 1 +ATOM 1735 C C . VAL A 1 220 ? 3.856 105.058 111.055 1.00 55.45 ? 219 VAL A C 1 +ATOM 1736 O O . VAL A 1 220 ? 3.016 105.300 110.175 1.00 86.26 ? 219 VAL A O 1 +ATOM 1737 C CB . VAL A 1 220 ? 2.336 105.339 113.004 1.00 72.52 ? 219 VAL A CB 1 +ATOM 1738 C CG1 . VAL A 1 220 ? 2.338 103.909 113.463 1.00 53.92 ? 219 VAL A CG1 1 +ATOM 1739 C CG2 . VAL A 1 220 ? 1.911 106.249 114.159 1.00 84.40 ? 219 VAL A CG2 1 +ATOM 1740 N N . LEU A 1 221 ? 4.891 104.227 110.885 1.00 87.51 ? 220 LEU A N 1 +ATOM 1741 C CA . LEU A 1 221 ? 5.214 103.553 109.614 1.00 79.80 ? 220 LEU A CA 1 +ATOM 1742 C C . LEU A 1 221 ? 4.945 102.050 109.619 1.00 72.32 ? 220 LEU A C 1 +ATOM 1743 O O . LEU A 1 221 ? 5.603 101.314 110.351 1.00 87.43 ? 220 LEU A O 1 +ATOM 1744 C CB . LEU A 1 221 ? 6.698 103.744 109.261 1.00 66.27 ? 220 LEU A CB 1 +ATOM 1745 C CG . LEU A 1 221 ? 7.178 102.940 108.042 1.00 64.92 ? 220 LEU A CG 1 +ATOM 1746 C CD1 . LEU A 1 221 ? 6.462 103.412 106.790 1.00 72.86 ? 220 LEU A CD1 1 +ATOM 1747 C CD2 . LEU A 1 221 ? 8.687 102.988 107.837 1.00 77.75 ? 220 LEU A CD2 1 +ATOM 1748 N N . LEU A 1 222 ? 4.003 101.603 108.783 1.00 124.19 ? 221 LEU A N 1 +ATOM 1749 C CA . LEU A 1 222 ? 3.785 100.176 108.495 1.00 67.56 ? 221 LEU A CA 1 +ATOM 1750 C C . LEU A 1 222 ? 4.258 99.780 107.098 1.00 91.15 ? 221 LEU A C 1 +ATOM 1751 O O . LEU A 1 222 ? 3.745 100.276 106.095 1.00 85.79 ? 221 LEU A O 1 +ATOM 1752 C CB . LEU A 1 222 ? 2.308 99.810 108.608 1.00 73.00 ? 221 LEU A CB 1 +ATOM 1753 C CG . LEU A 1 222 ? 1.653 99.905 109.983 1.00 93.49 ? 221 LEU A CG 1 +ATOM 1754 C CD1 . LEU A 1 222 ? 0.145 99.648 109.894 1.00 57.00 ? 221 LEU A CD1 1 +ATOM 1755 C CD2 . LEU A 1 222 ? 2.328 98.906 110.915 1.00 80.46 ? 221 LEU A CD2 1 +ATOM 1756 N N . GLU A 1 223 ? 5.226 98.869 107.052 1.00 81.18 ? 222 GLU A N 1 +ATOM 1757 C CA . GLU A 1 223 ? 5.733 98.307 105.802 1.00 92.07 ? 222 GLU A CA 1 +ATOM 1758 C C . GLU A 1 223 ? 5.351 96.840 105.600 1.00 79.18 ? 222 GLU A C 1 +ATOM 1759 O O . GLU A 1 223 ? 5.419 96.040 106.535 1.00 84.76 ? 222 GLU A O 1 +ATOM 1760 C CB . GLU A 1 223 ? 7.254 98.407 105.770 1.00 75.70 ? 222 GLU A CB 1 +ATOM 1761 C CG . GLU A 1 223 ? 7.775 99.578 104.977 1.00 130.36 ? 222 GLU A CG 1 +ATOM 1762 C CD . GLU A 1 223 ? 9.291 99.581 104.858 1.00 162.92 ? 222 GLU A CD 1 +ATOM 1763 O OE1 . GLU A 1 223 ? 9.901 98.490 104.937 1.00 156.79 ? 222 GLU A OE1 1 +ATOM 1764 O OE2 . GLU A 1 223 ? 9.869 100.679 104.691 1.00 159.88 ? 222 GLU A OE2 1 +ATOM 1765 N N . PHE A 1 224 ? 4.962 96.496 104.373 1.00 90.38 ? 223 PHE A N 1 +ATOM 1766 C CA . PHE A 1 224 ? 4.857 95.096 103.947 1.00 74.73 ? 223 PHE A CA 1 +ATOM 1767 C C . PHE A 1 224 ? 5.945 94.830 102.909 1.00 61.70 ? 223 PHE A C 1 +ATOM 1768 O O . PHE A 1 224 ? 6.133 95.622 101.996 1.00 96.37 ? 223 PHE A O 1 +ATOM 1769 C CB . PHE A 1 224 ? 3.495 94.803 103.315 1.00 75.16 ? 223 PHE A CB 1 +ATOM 1770 C CG . PHE A 1 224 ? 2.320 95.095 104.208 1.00 84.96 ? 223 PHE A CG 1 +ATOM 1771 C CD1 . PHE A 1 224 ? 2.470 95.186 105.590 1.00 70.61 ? 223 PHE A CD1 1 +ATOM 1772 C CD2 . PHE A 1 224 ? 1.054 95.276 103.656 1.00 69.96 ? 223 PHE A CD2 1 +ATOM 1773 C CE1 . PHE A 1 224 ? 1.381 95.462 106.407 1.00 71.70 ? 223 PHE A CE1 1 +ATOM 1774 C CE2 . PHE A 1 224 ? -0.044 95.550 104.464 1.00 88.01 ? 223 PHE A CE2 1 +ATOM 1775 C CZ . PHE A 1 224 ? 0.121 95.639 105.846 1.00 96.57 ? 223 PHE A CZ 1 +ATOM 1776 N N . VAL A 1 225 ? 6.686 93.738 103.047 1.00 88.28 ? 224 VAL A N 1 +ATOM 1777 C CA . VAL A 1 225 ? 7.739 93.445 102.076 1.00 88.12 ? 224 VAL A CA 1 +ATOM 1778 C C . VAL A 1 225 ? 7.795 91.965 101.682 1.00 100.97 ? 224 VAL A C 1 +ATOM 1779 O O . VAL A 1 225 ? 7.923 91.098 102.546 1.00 91.76 ? 224 VAL A O 1 +ATOM 1780 C CB . VAL A 1 225 ? 9.137 93.854 102.600 1.00 75.58 ? 224 VAL A CB 1 +ATOM 1781 C CG1 . VAL A 1 225 ? 10.107 93.962 101.449 1.00 85.59 ? 224 VAL A CG1 1 +ATOM 1782 C CG2 . VAL A 1 225 ? 9.087 95.173 103.356 1.00 86.29 ? 224 VAL A CG2 1 +ATOM 1783 N N . THR A 1 226 ? 7.717 91.684 100.381 1.00 85.01 ? 225 THR A N 1 +ATOM 1784 C CA . THR A 1 226 ? 7.862 90.315 99.868 1.00 95.96 ? 225 THR A CA 1 +ATOM 1785 C C . THR A 1 226 ? 8.863 90.183 98.701 1.00 95.76 ? 225 THR A C 1 +ATOM 1786 O O . THR A 1 226 ? 8.818 90.954 97.744 1.00 85.23 ? 225 THR A O 1 +ATOM 1787 C CB . THR A 1 226 ? 6.508 89.730 99.388 1.00 87.92 ? 225 THR A CB 1 +ATOM 1788 O OG1 . THR A 1 226 ? 5.500 89.884 100.398 1.00 74.07 ? 225 THR A OG1 1 +ATOM 1789 C CG2 . THR A 1 226 ? 6.670 88.262 99.051 1.00 107.34 ? 225 THR A CG2 1 +ATOM 1790 N N . ALA A 1 227 ? 9.755 89.198 98.773 1.00 88.96 ? 226 ALA A N 1 +ATOM 1791 C CA . ALA A 1 227 ? 10.633 88.886 97.642 1.00 84.05 ? 226 ALA A CA 1 +ATOM 1792 C C . ALA A 1 227 ? 9.895 88.094 96.548 1.00 94.05 ? 226 ALA A C 1 +ATOM 1793 O O . ALA A 1 227 ? 8.973 87.326 96.833 1.00 109.42 ? 226 ALA A O 1 +ATOM 1794 C CB . ALA A 1 227 ? 11.869 88.139 98.118 1.00 87.73 ? 226 ALA A CB 1 +ATOM 1795 N N . ALA A 1 228 ? 10.311 88.289 95.299 1.00 77.89 ? 227 ALA A N 1 +ATOM 1796 C CA . ALA A 1 228 ? 9.601 87.750 94.142 1.00 100.64 ? 227 ALA A CA 1 +ATOM 1797 C C . ALA A 1 228 ? 10.515 87.766 92.918 1.00 110.85 ? 227 ALA A C 1 +ATOM 1798 O O . ALA A 1 228 ? 11.727 87.905 93.062 1.00 101.69 ? 227 ALA A O 1 +ATOM 1799 C CB . ALA A 1 228 ? 8.342 88.564 93.878 1.00 79.66 ? 227 ALA A CB 1 +ATOM 1800 N N . GLY A 1 229 ? 9.939 87.604 91.726 1.00 109.73 ? 228 GLY A N 1 +ATOM 1801 C CA . GLY A 1 229 ? 10.672 87.776 90.477 1.00 116.82 ? 228 GLY A CA 1 +ATOM 1802 C C . GLY A 1 229 ? 11.638 86.690 90.020 1.00 125.93 ? 228 GLY A C 1 +ATOM 1803 O O . GLY A 1 229 ? 12.243 86.802 88.955 1.00 130.41 ? 228 GLY A O 1 +ATOM 1804 N N . ILE A 1 230 ? 11.815 85.657 90.832 1.00 119.68 ? 229 ILE A N 1 +ATOM 1805 C CA . ILE A 1 230 ? 12.458 84.433 90.377 1.00 129.09 ? 229 ILE A CA 1 +ATOM 1806 C C . ILE A 1 230 ? 11.348 83.397 90.267 1.00 206.01 ? 229 ILE A C 1 +ATOM 1807 O O . ILE A 1 230 ? 10.554 83.259 91.197 1.00 236.69 ? 229 ILE A O 1 +ATOM 1808 C CB . ILE A 1 230 ? 13.520 83.946 91.371 1.00 128.13 ? 229 ILE A CB 1 +ATOM 1809 C CG1 . ILE A 1 230 ? 14.750 84.848 91.310 1.00 125.94 ? 229 ILE A CG1 1 +ATOM 1810 C CG2 . ILE A 1 230 ? 13.911 82.505 91.084 1.00 148.16 ? 229 ILE A CG2 1 +ATOM 1811 C CD1 . ILE A 1 230 ? 15.884 84.385 92.180 1.00 116.21 ? 229 ILE A CD1 1 +ATOM 1812 N N . THR A 1 231 ? 11.274 82.689 89.140 1.00 226.51 ? 230 THR A N 1 +ATOM 1813 C CA . THR A 1 231 ? 10.177 81.740 88.893 1.00 240.78 ? 230 THR A CA 1 +ATOM 1814 C C . THR A 1 231 ? 9.885 80.790 90.070 1.00 246.21 ? 230 THR A C 1 +ATOM 1815 O O . THR A 1 231 ? 9.966 79.573 89.975 1.00 223.09 ? 230 THR A O 1 +ATOM 1816 C CB . THR A 1 231 ? 10.366 80.957 87.562 1.00 216.66 ? 230 THR A CB 1 +ATOM 1817 O OG1 . THR A 1 231 ? 9.361 79.943 87.450 1.00 211.18 ? 230 THR A OG1 1 +ATOM 1818 C CG2 . THR A 1 231 ? 11.749 80.313 87.488 1.00 204.11 ? 230 THR A CG2 1 +ATOM 1819 N N . ALA A 1 235 ? 16.472 77.632 82.321 1.00 139.45 ? 1054 ALA A N 1 +ATOM 1820 C CA . ALA A 1 235 ? 16.674 76.910 81.067 1.00 166.07 ? 1054 ALA A CA 1 +ATOM 1821 C C . ALA A 1 235 ? 17.770 77.526 80.187 1.00 177.56 ? 1054 ALA A C 1 +ATOM 1822 O O . ALA A 1 235 ? 18.659 78.235 80.672 1.00 145.74 ? 1054 ALA A O 1 +ATOM 1823 C CB . ALA A 1 235 ? 15.353 76.806 80.288 1.00 137.76 ? 1054 ALA A CB 1 +ATOM 1824 N N . SER A 1 236 ? 17.707 77.230 78.892 1.00 191.09 ? 1055 SER A N 1 +ATOM 1825 C CA . SER A 1 236 ? 18.598 77.846 77.916 1.00 205.77 ? 1055 SER A CA 1 +ATOM 1826 C C . SER A 1 236 ? 17.925 79.108 77.397 1.00 223.46 ? 1055 SER A C 1 +ATOM 1827 O O . SER A 1 236 ? 18.542 79.938 76.722 1.00 191.25 ? 1055 SER A O 1 +ATOM 1828 C CB . SER A 1 236 ? 18.893 76.884 76.764 1.00 178.58 ? 1055 SER A CB 1 +ATOM 1829 O OG . SER A 1 236 ? 19.894 77.409 75.908 1.00 146.97 ? 1055 SER A OG 1 +ATOM 1830 N N . THR A 1 237 ? 16.644 79.237 77.735 1.00 238.95 ? 1056 THR A N 1 +ATOM 1831 C CA . THR A 1 237 ? 15.867 80.432 77.442 1.00 213.79 ? 1056 THR A CA 1 +ATOM 1832 C C . THR A 1 237 ? 16.509 81.638 78.129 1.00 176.88 ? 1056 THR A C 1 +ATOM 1833 O O . THR A 1 237 ? 16.357 82.775 77.688 1.00 135.22 ? 1056 THR A O 1 +ATOM 1834 C CB . THR A 1 237 ? 14.390 80.261 77.884 1.00 170.14 ? 1056 THR A CB 1 +ATOM 1835 O OG1 . THR A 1 237 ? 14.296 80.283 79.315 1.00 156.33 ? 1056 THR A OG1 1 +ATOM 1836 C CG2 . THR A 1 237 ? 13.828 78.939 77.365 1.00 152.35 ? 1056 THR A CG2 1 +ATOM 1837 N N . LYS A 1 238 ? 17.236 81.369 79.210 1.00 204.11 ? 1057 LYS A N 1 +ATOM 1838 C CA . LYS A 1 238 ? 18.037 82.383 79.883 1.00 193.66 ? 1057 LYS A CA 1 +ATOM 1839 C C . LYS A 1 238 ? 18.987 83.042 78.891 1.00 164.78 ? 1057 LYS A C 1 +ATOM 1840 O O . LYS A 1 238 ? 18.927 84.247 78.677 1.00 127.41 ? 1057 LYS A O 1 +ATOM 1841 C CB . LYS A 1 238 ? 18.841 81.765 81.035 1.00 179.08 ? 1057 LYS A CB 1 +ATOM 1842 C CG . LYS A 1 238 ? 18.130 81.744 82.387 1.00 168.39 ? 1057 LYS A CG 1 +ATOM 1843 C CD . LYS A 1 238 ? 16.854 80.922 82.346 1.00 150.95 ? 1057 LYS A CD 1 +ATOM 1844 C CE . LYS A 1 238 ? 16.304 80.678 83.739 1.00 132.12 ? 1057 LYS A CE 1 +ATOM 1845 N NZ . LYS A 1 238 ? 14.975 79.985 83.722 1.00 129.56 ? 1057 LYS A NZ 1 +ATOM 1846 N N . LYS A 1 239 ? 19.834 82.227 78.269 1.00 184.26 ? 1058 LYS A N 1 +ATOM 1847 C CA . LYS A 1 239 ? 20.892 82.695 77.372 1.00 197.83 ? 1058 LYS A CA 1 +ATOM 1848 C C . LYS A 1 239 ? 20.393 83.557 76.203 1.00 182.11 ? 1058 LYS A C 1 +ATOM 1849 O O . LYS A 1 239 ? 21.139 84.377 75.657 1.00 160.36 ? 1058 LYS A O 1 +ATOM 1850 C CB . LYS A 1 239 ? 21.677 81.493 76.833 1.00 206.93 ? 1058 LYS A CB 1 +ATOM 1851 C CG . LYS A 1 239 ? 22.214 80.544 77.904 1.00 181.75 ? 1058 LYS A CG 1 +ATOM 1852 C CD . LYS A 1 239 ? 23.102 79.479 77.272 1.00 180.55 ? 1058 LYS A CD 1 +ATOM 1853 C CE . LYS A 1 239 ? 24.163 80.118 76.371 1.00 173.54 ? 1058 LYS A CE 1 +ATOM 1854 N NZ . LYS A 1 239 ? 24.881 79.142 75.502 1.00 137.98 ? 1058 LYS A NZ 1 +ATOM 1855 N N . LEU A 1 240 ? 19.132 83.364 75.829 1.00 168.98 ? 1059 LEU A N 1 +ATOM 1856 C CA . LEU A 1 240 ? 18.526 84.060 74.695 1.00 179.00 ? 1059 LEU A CA 1 +ATOM 1857 C C . LEU A 1 240 ? 18.185 85.515 74.993 1.00 172.91 ? 1059 LEU A C 1 +ATOM 1858 O O . LEU A 1 240 ? 18.522 86.422 74.221 1.00 105.85 ? 1059 LEU A O 1 +ATOM 1859 C CB . LEU A 1 240 ? 17.251 83.335 74.272 1.00 190.56 ? 1059 LEU A CB 1 +ATOM 1860 C CG . LEU A 1 240 ? 16.371 84.058 73.256 1.00 171.15 ? 1059 LEU A CG 1 +ATOM 1861 C CD1 . LEU A 1 240 ? 17.133 84.263 71.956 1.00 161.31 ? 1059 LEU A CD1 1 +ATOM 1862 C CD2 . LEU A 1 240 ? 15.098 83.268 73.026 1.00 148.07 ? 1059 LEU A CD2 1 +ATOM 1863 N N . SER A 1 241 ? 17.491 85.714 76.112 1.00 201.65 ? 1060 SER A N 1 +ATOM 1864 C CA . SER A 1 241 ? 17.028 87.030 76.538 1.00 177.98 ? 1060 SER A CA 1 +ATOM 1865 C C . SER A 1 241 ? 18.182 87.898 77.026 1.00 147.58 ? 1060 SER A C 1 +ATOM 1866 O O . SER A 1 241 ? 18.047 89.112 77.131 1.00 136.01 ? 1060 SER A O 1 +ATOM 1867 C CB . SER A 1 241 ? 15.972 86.898 77.637 1.00 125.95 ? 1060 SER A CB 1 +ATOM 1868 O OG . SER A 1 241 ? 16.569 86.550 78.868 1.00 121.87 ? 1060 SER A OG 1 +ATOM 1869 N N . GLU A 1 242 ? 19.316 87.272 77.327 1.00 143.99 ? 1061 GLU A N 1 +ATOM 1870 C CA . GLU A 1 242 ? 20.516 88.025 77.670 1.00 175.28 ? 1061 GLU A CA 1 +ATOM 1871 C C . GLU A 1 242 ? 20.956 88.832 76.453 1.00 158.12 ? 1061 GLU A C 1 +ATOM 1872 O O . GLU A 1 242 ? 21.455 89.955 76.576 1.00 112.43 ? 1061 GLU A O 1 +ATOM 1873 C CB . GLU A 1 242 ? 21.647 87.094 78.124 1.00 183.39 ? 1061 GLU A CB 1 +ATOM 1874 C CG . GLU A 1 242 ? 21.261 86.055 79.180 1.00 184.48 ? 1061 GLU A CG 1 +ATOM 1875 C CD . GLU A 1 242 ? 20.605 86.645 80.427 1.00 191.48 ? 1061 GLU A CD 1 +ATOM 1876 O OE1 . GLU A 1 242 ? 20.830 87.835 80.736 1.00 195.96 ? 1061 GLU A OE1 1 +ATOM 1877 O OE2 . GLU A 1 242 ? 19.861 85.906 81.108 1.00 178.74 ? 1061 GLU A OE2 1 +ATOM 1878 N N . SER A 1 243 ? 20.750 88.247 75.276 1.00 176.09 ? 1062 SER A N 1 +ATOM 1879 C CA . SER A 1 243 ? 21.096 88.889 74.011 1.00 198.27 ? 1062 SER A CA 1 +ATOM 1880 C C . SER A 1 243 ? 20.059 89.936 73.600 1.00 178.63 ? 1062 SER A C 1 +ATOM 1881 O O . SER A 1 243 ? 20.408 91.073 73.262 1.00 130.40 ? 1062 SER A O 1 +ATOM 1882 C CB . SER A 1 243 ? 21.265 87.836 72.914 1.00 202.68 ? 1062 SER A CB 1 +ATOM 1883 O OG . SER A 1 243 ? 22.326 86.949 73.229 1.00 196.37 ? 1062 SER A OG 1 +ATOM 1884 N N . LEU A 1 244 ? 18.788 89.544 73.631 1.00 165.04 ? 1063 LEU A N 1 +ATOM 1885 C CA . LEU A 1 244 ? 17.698 90.473 73.365 1.00 143.94 ? 1063 LEU A CA 1 +ATOM 1886 C C . LEU A 1 244 ? 17.837 91.699 74.244 1.00 157.57 ? 1063 LEU A C 1 +ATOM 1887 O O . LEU A 1 244 ? 17.599 92.823 73.798 1.00 130.83 ? 1063 LEU A O 1 +ATOM 1888 C CB . LEU A 1 244 ? 16.354 89.804 73.619 1.00 121.28 ? 1063 LEU A CB 1 +ATOM 1889 C CG . LEU A 1 244 ? 15.791 89.063 72.410 1.00 147.18 ? 1063 LEU A CG 1 +ATOM 1890 C CD1 . LEU A 1 244 ? 14.400 88.534 72.723 1.00 139.01 ? 1063 LEU A CD1 1 +ATOM 1891 C CD2 . LEU A 1 244 ? 15.791 89.967 71.173 1.00 118.65 ? 1063 LEU A CD2 1 +ATOM 1892 N N . LYS A 1 245 ? 18.230 91.461 75.493 1.00 171.35 ? 1064 LYS A N 1 +ATOM 1893 C CA . LYS A 1 245 ? 18.610 92.525 76.410 1.00 163.73 ? 1064 LYS A CA 1 +ATOM 1894 C C . LYS A 1 245 ? 19.603 93.479 75.753 1.00 172.66 ? 1064 LYS A C 1 +ATOM 1895 O O . LYS A 1 245 ? 19.261 94.627 75.477 1.00 178.22 ? 1064 LYS A O 1 +ATOM 1896 C CB . LYS A 1 245 ? 19.209 91.950 77.698 1.00 136.23 ? 1064 LYS A CB 1 +ATOM 1897 C CG . LYS A 1 245 ? 18.199 91.660 78.808 1.00 163.67 ? 1064 LYS A CG 1 +ATOM 1898 C CD . LYS A 1 245 ? 18.890 91.049 80.032 1.00 196.97 ? 1064 LYS A CD 1 +ATOM 1899 C CE . LYS A 1 245 ? 17.937 90.885 81.212 1.00 181.28 ? 1064 LYS A CE 1 +ATOM 1900 N NZ . LYS A 1 245 ? 18.626 90.441 82.457 1.00 127.00 ? 1064 LYS A NZ 1 +ATOM 1901 N N . ARG A 1 246 ? 20.818 93.003 75.482 1.00 163.61 ? 1065 ARG A N 1 +ATOM 1902 C CA . ARG A 1 246 ? 21.868 93.889 74.975 1.00 175.98 ? 1065 ARG A CA 1 +ATOM 1903 C C . ARG A 1 246 ? 21.512 94.566 73.641 1.00 165.25 ? 1065 ARG A C 1 +ATOM 1904 O O . ARG A 1 246 ? 21.862 95.727 73.424 1.00 153.26 ? 1065 ARG A O 1 +ATOM 1905 C CB . ARG A 1 246 ? 23.236 93.182 74.906 1.00 169.66 ? 1065 ARG A CB 1 +ATOM 1906 C CG . ARG A 1 246 ? 23.857 92.815 76.250 1.00 185.43 ? 1065 ARG A CG 1 +ATOM 1907 C CD . ARG A 1 246 ? 25.231 92.170 76.058 1.00 203.37 ? 1065 ARG A CD 1 +ATOM 1908 N NE . ARG A 1 246 ? 25.829 91.736 77.322 1.00 222.84 ? 1065 ARG A NE 1 +ATOM 1909 C CZ . ARG A 1 246 ? 26.965 91.048 77.426 1.00 201.17 ? 1065 ARG A CZ 1 +ATOM 1910 N NH1 . ARG A 1 246 ? 27.644 90.707 76.338 1.00 185.36 ? 1065 ARG A NH1 1 +ATOM 1911 N NH2 . ARG A 1 246 ? 27.426 90.698 78.622 1.00 155.09 ? 1065 ARG A NH2 1 +ATOM 1912 N N . ILE A 1 247 ? 20.790 93.860 72.774 1.00 142.64 ? 1066 ILE A N 1 +ATOM 1913 C CA . ILE A 1 247 ? 20.431 94.404 71.462 1.00 151.38 ? 1066 ILE A CA 1 +ATOM 1914 C C . ILE A 1 247 ? 19.493 95.615 71.578 1.00 154.34 ? 1066 ILE A C 1 +ATOM 1915 O O . ILE A 1 247 ? 19.656 96.604 70.860 1.00 120.02 ? 1066 ILE A O 1 +ATOM 1916 C CB . ILE A 1 247 ? 19.853 93.300 70.519 1.00 158.17 ? 1066 ILE A CB 1 +ATOM 1917 C CG1 . ILE A 1 247 ? 20.937 92.263 70.167 1.00 192.05 ? 1066 ILE A CG1 1 +ATOM 1918 C CG2 . ILE A 1 247 ? 19.232 93.909 69.266 1.00 115.21 ? 1066 ILE A CG2 1 +ATOM 1919 C CD1 . ILE A 1 247 ? 20.442 90.999 69.473 1.00 207.16 ? 1066 ILE A CD1 1 +ATOM 1920 N N . GLY A 1 248 ? 18.532 95.539 72.494 1.00 163.17 ? 1067 GLY A N 1 +ATOM 1921 C CA . GLY A 1 248 ? 17.664 96.666 72.784 1.00 138.60 ? 1067 GLY A CA 1 +ATOM 1922 C C . GLY A 1 248 ? 18.399 97.678 73.641 1.00 154.95 ? 1067 GLY A C 1 +ATOM 1923 O O . GLY A 1 248 ? 18.031 98.852 73.690 1.00 138.10 ? 1067 GLY A O 1 +ATOM 1924 N N . ASP A 1 249 ? 19.452 97.214 74.312 1.00 173.12 ? 1068 ASP A N 1 +ATOM 1925 C CA . ASP A 1 249 ? 20.250 98.059 75.200 1.00 164.46 ? 1068 ASP A CA 1 +ATOM 1926 C C . ASP A 1 249 ? 21.197 98.975 74.431 1.00 161.18 ? 1068 ASP A C 1 +ATOM 1927 O O . ASP A 1 249 ? 21.100 100.200 74.543 1.00 126.46 ? 1068 ASP A O 1 +ATOM 1928 C CB . ASP A 1 249 ? 21.026 97.213 76.216 1.00 167.21 ? 1068 ASP A CB 1 +ATOM 1929 C CG . ASP A 1 249 ? 20.178 96.813 77.414 1.00 186.16 ? 1068 ASP A CG 1 +ATOM 1930 O OD1 . ASP A 1 249 ? 18.938 96.958 77.342 1.00 192.58 ? 1068 ASP A OD1 1 +ATOM 1931 O OD2 . ASP A 1 249 ? 20.751 96.349 78.425 1.00 176.30 ? 1068 ASP A OD2 1 +ATOM 1932 N N . GLU A 1 250 ? 22.107 98.376 73.659 1.00 183.19 ? 1069 GLU A N 1 +ATOM 1933 C CA . GLU A 1 250 ? 23.015 99.121 72.784 1.00 188.85 ? 1069 GLU A CA 1 +ATOM 1934 C C . GLU A 1 250 ? 22.216 100.099 71.929 1.00 171.42 ? 1069 GLU A C 1 +ATOM 1935 O O . GLU A 1 250 ? 22.649 101.222 71.661 1.00 120.71 ? 1069 GLU A O 1 +ATOM 1936 C CB . GLU A 1 250 ? 23.790 98.162 71.872 1.00 172.81 ? 1069 GLU A CB 1 +ATOM 1937 C CG . GLU A 1 250 ? 24.667 97.145 72.601 1.00 197.69 ? 1069 GLU A CG 1 +ATOM 1938 C CD . GLU A 1 250 ? 25.087 95.982 71.708 1.00 199.57 ? 1069 GLU A CD 1 +ATOM 1939 O OE1 . GLU A 1 250 ? 24.795 96.028 70.492 1.00 176.77 ? 1069 GLU A OE1 1 +ATOM 1940 O OE2 . GLU A 1 250 ? 25.699 95.018 72.224 1.00 182.07 ? 1069 GLU A OE2 1 +ATOM 1941 N N . LEU A 1 251 ? 21.037 99.645 71.519 1.00 160.74 ? 1070 LEU A N 1 +ATOM 1942 C CA . LEU A 1 251 ? 20.093 100.442 70.752 1.00 141.84 ? 1070 LEU A CA 1 +ATOM 1943 C C . LEU A 1 251 ? 19.663 101.707 71.505 1.00 152.36 ? 1070 LEU A C 1 +ATOM 1944 O O . LEU A 1 251 ? 19.846 102.823 71.018 1.00 103.47 ? 1070 LEU A O 1 +ATOM 1945 C CB . LEU A 1 251 ? 18.884 99.571 70.401 1.00 143.60 ? 1070 LEU A CB 1 +ATOM 1946 C CG . LEU A 1 251 ? 17.792 100.070 69.453 1.00 154.53 ? 1070 LEU A CG 1 +ATOM 1947 C CD1 . LEU A 1 251 ? 18.364 100.901 68.311 1.00 143.37 ? 1070 LEU A CD1 1 +ATOM 1948 C CD2 . LEU A 1 251 ? 16.973 98.896 68.910 1.00 118.77 ? 1070 LEU A CD2 1 +ATOM 1949 N N . ASP A 1 252 ? 19.107 101.543 72.698 1.00 170.61 ? 1071 ASP A N 1 +ATOM 1950 C CA . ASP A 1 252 ? 18.616 102.701 73.430 1.00 149.27 ? 1071 ASP A CA 1 +ATOM 1951 C C . ASP A 1 252 ? 19.762 103.562 73.967 1.00 149.79 ? 1071 ASP A C 1 +ATOM 1952 O O . ASP A 1 252 ? 19.586 104.753 74.238 1.00 135.76 ? 1071 ASP A O 1 +ATOM 1953 C CB . ASP A 1 252 ? 17.651 102.282 74.542 1.00 116.57 ? 1071 ASP A CB 1 +ATOM 1954 C CG . ASP A 1 252 ? 17.096 103.472 75.314 1.00 203.26 ? 1071 ASP A CG 1 +ATOM 1955 O OD1 . ASP A 1 252 ? 16.365 104.296 74.719 1.00 193.72 ? 1071 ASP A OD1 1 +ATOM 1956 O OD2 . ASP A 1 252 ? 17.389 103.585 76.523 1.00 245.58 ? 1071 ASP A OD2 1 +ATOM 1957 N N . SER A 1 253 ? 20.945 102.965 74.084 1.00 151.37 ? 1072 SER A N 1 +ATOM 1958 C CA . SER A 1 253 ? 22.103 103.683 74.609 1.00 178.73 ? 1072 SER A CA 1 +ATOM 1959 C C . SER A 1 253 ? 23.033 104.234 73.525 1.00 194.89 ? 1072 SER A C 1 +ATOM 1960 O O . SER A 1 253 ? 23.960 104.984 73.837 1.00 181.38 ? 1072 SER A O 1 +ATOM 1961 C CB . SER A 1 253 ? 22.898 102.807 75.583 1.00 181.93 ? 1072 SER A CB 1 +ATOM 1962 O OG . SER A 1 253 ? 23.640 101.814 74.897 1.00 167.16 ? 1072 SER A OG 1 +ATOM 1963 N N . ASN A 1 254 ? 22.791 103.861 72.267 1.00 218.49 ? 1073 ASN A N 1 +ATOM 1964 C CA . ASN A 1 254 ? 23.583 104.361 71.136 1.00 215.14 ? 1073 ASN A CA 1 +ATOM 1965 C C . ASN A 1 254 ? 23.447 105.869 70.971 1.00 207.95 ? 1073 ASN A C 1 +ATOM 1966 O O . ASN A 1 254 ? 22.484 106.354 70.372 1.00 163.39 ? 1073 ASN A O 1 +ATOM 1967 C CB . ASN A 1 254 ? 23.177 103.671 69.830 1.00 205.29 ? 1073 ASN A CB 1 +ATOM 1968 C CG . ASN A 1 254 ? 24.363 103.090 69.084 1.00 187.31 ? 1073 ASN A CG 1 +ATOM 1969 O OD1 . ASN A 1 254 ? 25.352 102.684 69.693 1.00 177.57 ? 1073 ASN A OD1 1 +ATOM 1970 N ND2 . ASN A 1 254 ? 24.268 103.044 67.758 1.00 173.02 ? 1073 ASN A ND2 1 +ATOM 1971 N N . MET A 1 255 ? 24.421 106.604 71.498 1.00 231.43 ? 1074 MET A N 1 +ATOM 1972 C CA . MET A 1 255 ? 24.336 108.060 71.569 1.00 233.12 ? 1074 MET A CA 1 +ATOM 1973 C C . MET A 1 255 ? 24.303 108.734 70.200 1.00 221.15 ? 1074 MET A C 1 +ATOM 1974 O O . MET A 1 255 ? 23.791 109.849 70.071 1.00 189.87 ? 1074 MET A O 1 +ATOM 1975 C CB . MET A 1 255 ? 25.470 108.632 72.427 1.00 234.66 ? 1074 MET A CB 1 +ATOM 1976 C CG . MET A 1 255 ? 25.296 108.400 73.921 1.00 227.17 ? 1074 MET A CG 1 +ATOM 1977 S SD . MET A 1 255 ? 23.715 109.013 74.541 1.00 248.96 ? 1074 MET A SD 1 +ATOM 1978 C CE . MET A 1 255 ? 23.830 110.762 74.159 1.00 135.36 ? 1074 MET A CE 1 +ATOM 1979 N N . GLU A 1 256 ? 24.851 108.060 69.190 1.00 230.36 ? 1075 GLU A N 1 +ATOM 1980 C CA . GLU A 1 256 ? 24.806 108.552 67.817 1.00 220.96 ? 1075 GLU A CA 1 +ATOM 1981 C C . GLU A 1 256 ? 23.360 108.754 67.428 1.00 190.61 ? 1075 GLU A C 1 +ATOM 1982 O O . GLU A 1 256 ? 22.929 109.856 67.086 1.00 147.99 ? 1075 GLU A O 1 +ATOM 1983 C CB . GLU A 1 256 ? 25.385 107.520 66.854 1.00 219.74 ? 1075 GLU A CB 1 +ATOM 1984 C CG . GLU A 1 256 ? 26.733 106.964 67.225 1.00 215.89 ? 1075 GLU A CG 1 +ATOM 1985 C CD . GLU A 1 256 ? 27.140 105.843 66.298 1.00 213.74 ? 1075 GLU A CD 1 +ATOM 1986 O OE1 . GLU A 1 256 ? 26.243 105.110 65.830 1.00 215.84 ? 1075 GLU A OE1 1 +ATOM 1987 O OE2 . GLU A 1 256 ? 28.351 105.702 66.028 1.00 204.74 ? 1075 GLU A OE2 1 +ATOM 1988 N N . LEU A 1 257 ? 22.628 107.648 67.501 1.00 181.33 ? 1076 LEU A N 1 +ATOM 1989 C CA . LEU A 1 257 ? 21.234 107.556 67.097 1.00 177.12 ? 1076 LEU A CA 1 +ATOM 1990 C C . LEU A 1 257 ? 20.298 108.467 67.900 1.00 173.46 ? 1076 LEU A C 1 +ATOM 1991 O O . LEU A 1 257 ? 19.486 109.196 67.322 1.00 112.46 ? 1076 LEU A O 1 +ATOM 1992 C CB . LEU A 1 257 ? 20.790 106.093 67.193 1.00 162.80 ? 1076 LEU A CB 1 +ATOM 1993 C CG . LEU A 1 257 ? 19.329 105.716 66.956 1.00 162.35 ? 1076 LEU A CG 1 +ATOM 1994 C CD1 . LEU A 1 257 ? 18.798 106.304 65.653 1.00 136.86 ? 1076 LEU A CD1 1 +ATOM 1995 C CD2 . LEU A 1 257 ? 19.189 104.203 66.981 1.00 172.48 ? 1076 LEU A CD2 1 +ATOM 1996 N N . GLN A 1 258 ? 20.413 108.421 69.226 1.00 187.83 ? 1077 GLN A N 1 +ATOM 1997 C CA . GLN A 1 258 ? 19.554 109.224 70.095 1.00 177.88 ? 1077 GLN A CA 1 +ATOM 1998 C C . GLN A 1 258 ? 19.691 110.717 69.763 1.00 181.31 ? 1077 GLN A C 1 +ATOM 1999 O O . GLN A 1 258 ? 18.690 111.429 69.649 1.00 163.18 ? 1077 GLN A O 1 +ATOM 2000 C CB . GLN A 1 258 ? 19.856 108.944 71.576 1.00 157.32 ? 1077 GLN A CB 1 +ATOM 2001 C CG . GLN A 1 258 ? 19.731 107.471 71.990 1.00 176.08 ? 1077 GLN A CG 1 +ATOM 2002 C CD . GLN A 1 258 ? 18.306 106.933 71.903 1.00 173.26 ? 1077 GLN A CD 1 +ATOM 2003 O OE1 . GLN A 1 258 ? 17.338 107.661 72.129 1.00 167.30 ? 1077 GLN A OE1 1 +ATOM 2004 N NE2 . GLN A 1 258 ? 18.177 105.649 71.573 1.00 129.53 ? 1077 GLN A NE2 1 +ATOM 2005 N N . ARG A 1 259 ? 20.931 111.169 69.581 1.00 181.33 ? 1078 ARG A N 1 +ATOM 2006 C CA . ARG A 1 259 ? 21.214 112.542 69.162 1.00 181.87 ? 1078 ARG A CA 1 +ATOM 2007 C C . ARG A 1 259 ? 20.553 112.834 67.822 1.00 185.88 ? 1078 ARG A C 1 +ATOM 2008 O O . ARG A 1 259 ? 19.880 113.853 67.663 1.00 171.34 ? 1078 ARG A O 1 +ATOM 2009 C CB . ARG A 1 259 ? 22.727 112.767 69.036 1.00 197.63 ? 1078 ARG A CB 1 +ATOM 2010 C CG . ARG A 1 259 ? 23.135 114.211 68.734 1.00 197.69 ? 1078 ARG A CG 1 +ATOM 2011 C CD . ARG A 1 259 ? 24.342 114.285 67.796 1.00 214.60 ? 1078 ARG A CD 1 +ATOM 2012 N NE . ARG A 1 259 ? 25.516 113.587 68.319 1.00 223.10 ? 1078 ARG A NE 1 +ATOM 2013 C CZ . ARG A 1 259 ? 26.340 112.850 67.579 1.00 199.04 ? 1078 ARG A CZ 1 +ATOM 2014 N NH1 . ARG A 1 259 ? 26.119 112.707 66.278 1.00 172.58 ? 1078 ARG A NH1 1 +ATOM 2015 N NH2 . ARG A 1 259 ? 27.384 112.252 68.141 1.00 167.31 ? 1078 ARG A NH2 1 +ATOM 2016 N N . MET A 1 260 ? 20.756 111.922 66.871 1.00 189.69 ? 1079 MET A N 1 +ATOM 2017 C CA . MET A 1 260 ? 20.253 112.044 65.501 1.00 187.09 ? 1079 MET A CA 1 +ATOM 2018 C C . MET A 1 260 ? 18.744 112.247 65.422 1.00 192.88 ? 1079 MET A C 1 +ATOM 2019 O O . MET A 1 260 ? 18.264 113.057 64.628 1.00 192.60 ? 1079 MET A O 1 +ATOM 2020 C CB . MET A 1 260 ? 20.628 110.799 64.683 1.00 168.90 ? 1079 MET A CB 1 +ATOM 2021 C CG . MET A 1 260 ? 21.590 111.049 63.530 1.00 135.68 ? 1079 MET A CG 1 +ATOM 2022 S SD . MET A 1 260 ? 21.858 109.584 62.500 1.00 236.46 ? 1079 MET A SD 1 +ATOM 2023 C CE . MET A 1 260 ? 22.817 108.517 63.581 1.00 95.17 ? 1079 MET A CE 1 +ATOM 2024 N N . ILE A 1 261 ? 17.994 111.503 66.229 1.00 183.03 ? 1080 ILE A N 1 +ATOM 2025 C CA . ILE A 1 261 ? 16.539 111.565 66.146 1.00 185.04 ? 1080 ILE A CA 1 +ATOM 2026 C C . ILE A 1 261 ? 15.987 112.781 66.867 1.00 190.01 ? 1080 ILE A C 1 +ATOM 2027 O O . ILE A 1 261 ? 15.047 113.412 66.389 1.00 197.11 ? 1080 ILE A O 1 +ATOM 2028 C CB . ILE A 1 261 ? 15.860 110.310 66.702 1.00 167.67 ? 1080 ILE A CB 1 +ATOM 2029 C CG1 . ILE A 1 261 ? 16.608 109.055 66.260 1.00 148.25 ? 1080 ILE A CG1 1 +ATOM 2030 C CG2 . ILE A 1 261 ? 14.407 110.263 66.250 1.00 170.39 ? 1080 ILE A CG2 1 +ATOM 2031 C CD1 . ILE A 1 261 ? 15.848 107.779 66.529 1.00 147.18 ? 1080 ILE A CD1 1 +ATOM 2032 N N . ALA A 1 262 ? 16.566 113.093 68.024 1.00 175.62 ? 1081 ALA A N 1 +ATOM 2033 C CA . ALA A 1 262 ? 16.233 114.319 68.739 1.00 175.03 ? 1081 ALA A CA 1 +ATOM 2034 C C . ALA A 1 262 ? 16.411 115.498 67.781 1.00 194.98 ? 1081 ALA A C 1 +ATOM 2035 O O . ALA A 1 262 ? 15.545 116.370 67.668 1.00 177.94 ? 1081 ALA A O 1 +ATOM 2036 C CB . ALA A 1 262 ? 17.117 114.474 69.981 1.00 125.76 ? 1081 ALA A CB 1 +ATOM 2037 N N . ALA A 1 263 ? 17.531 115.490 67.063 1.00 195.46 ? 1082 ALA A N 1 +ATOM 2038 C CA . ALA A 1 263 ? 17.772 116.466 66.010 1.00 194.87 ? 1082 ALA A CA 1 +ATOM 2039 C C . ALA A 1 263 ? 16.928 116.158 64.771 1.00 223.78 ? 1082 ALA A C 1 +ATOM 2040 O O . ALA A 1 263 ? 17.425 115.597 63.792 1.00 214.53 ? 1082 ALA A O 1 +ATOM 2041 C CB . ALA A 1 263 ? 19.257 116.514 65.655 1.00 182.00 ? 1082 ALA A CB 1 +ATOM 2042 N N . VAL A 1 264 ? 15.646 116.514 64.831 1.00 239.46 ? 1083 VAL A N 1 +ATOM 2043 C CA . VAL A 1 264 ? 14.768 116.457 63.662 1.00 243.98 ? 1083 VAL A CA 1 +ATOM 2044 C C . VAL A 1 264 ? 13.578 117.416 63.817 1.00 216.97 ? 1083 VAL A C 1 +ATOM 2045 O O . VAL A 1 264 ? 13.096 117.655 64.931 1.00 152.50 ? 1083 VAL A O 1 +ATOM 2046 C CB . VAL A 1 264 ? 14.292 115.012 63.346 1.00 210.80 ? 1083 VAL A CB 1 +ATOM 2047 C CG1 . VAL A 1 264 ? 13.147 114.602 64.261 1.00 186.55 ? 1083 VAL A CG1 1 +ATOM 2048 C CG2 . VAL A 1 264 ? 13.885 114.889 61.879 1.00 193.29 ? 1083 VAL A CG2 1 +ATOM 2049 N N . ASP A 1 265 ? 13.129 117.979 62.695 1.00 225.20 ? 1084 ASP A N 1 +ATOM 2050 C CA . ASP A 1 265 ? 12.047 118.964 62.700 1.00 236.79 ? 1084 ASP A CA 1 +ATOM 2051 C C . ASP A 1 265 ? 10.689 118.276 62.611 1.00 232.36 ? 1084 ASP A C 1 +ATOM 2052 O O . ASP A 1 265 ? 10.283 117.804 61.547 1.00 192.37 ? 1084 ASP A O 1 +ATOM 2053 C CB . ASP A 1 265 ? 12.218 119.970 61.555 1.00 236.38 ? 1084 ASP A CB 1 +ATOM 2054 C CG . ASP A 1 265 ? 11.565 121.315 61.853 1.00 217.37 ? 1084 ASP A CG 1 +ATOM 2055 O OD1 . ASP A 1 265 ? 10.489 121.334 62.488 1.00 213.58 ? 1084 ASP A OD1 1 +ATOM 2056 O OD2 . ASP A 1 265 ? 12.135 122.356 61.457 1.00 185.76 ? 1084 ASP A OD2 1 +ATOM 2057 N N . THR A 1 266 ? 9.986 118.242 63.739 1.00 250.58 ? 1085 THR A N 1 +ATOM 2058 C CA . THR A 1 266 ? 8.786 117.427 63.876 1.00 267.26 ? 1085 THR A CA 1 +ATOM 2059 C C . THR A 1 266 ? 7.544 118.235 64.264 1.00 269.51 ? 1085 THR A C 1 +ATOM 2060 O O . THR A 1 266 ? 6.658 117.756 64.971 1.00 270.89 ? 1085 THR A O 1 +ATOM 2061 C CB . THR A 1 266 ? 9.015 116.302 64.907 1.00 267.33 ? 1085 THR A CB 1 +ATOM 2062 O OG1 . THR A 1 266 ? 10.085 115.460 64.465 1.00 263.99 ? 1085 THR A OG1 1 +ATOM 2063 C CG2 . THR A 1 266 ? 7.775 115.443 65.082 1.00 261.73 ? 1085 THR A CG2 1 +ATOM 2064 N N . ASP A 1 267 ? 7.474 119.481 63.805 1.00 263.66 ? 1086 ASP A N 1 +ATOM 2065 C CA . ASP A 1 267 ? 6.269 120.291 63.971 1.00 250.38 ? 1086 ASP A CA 1 +ATOM 2066 C C . ASP A 1 267 ? 5.279 119.896 62.880 1.00 238.21 ? 1086 ASP A C 1 +ATOM 2067 O O . ASP A 1 267 ? 4.061 119.867 63.086 1.00 200.64 ? 1086 ASP A O 1 +ATOM 2068 C CB . ASP A 1 267 ? 6.605 121.778 63.867 1.00 241.37 ? 1086 ASP A CB 1 +ATOM 2069 C CG . ASP A 1 267 ? 7.817 122.161 64.694 1.00 244.66 ? 1086 ASP A CG 1 +ATOM 2070 O OD1 . ASP A 1 267 ? 8.207 121.381 65.590 1.00 243.99 ? 1086 ASP A OD1 1 +ATOM 2071 O OD2 . ASP A 1 267 ? 8.380 123.249 64.447 1.00 242.86 ? 1086 ASP A OD2 1 +ATOM 2072 N N . SER A 1 268 ? 5.836 119.597 61.711 1.00 247.69 ? 1087 SER A N 1 +ATOM 2073 C CA . SER A 1 268 ? 5.109 118.985 60.611 1.00 235.81 ? 1087 SER A CA 1 +ATOM 2074 C C . SER A 1 268 ? 5.668 117.570 60.446 1.00 252.88 ? 1087 SER A C 1 +ATOM 2075 O O . SER A 1 268 ? 6.473 117.319 59.546 1.00 233.02 ? 1087 SER A O 1 +ATOM 2076 C CB . SER A 1 268 ? 5.317 119.803 59.333 1.00 185.99 ? 1087 SER A CB 1 +ATOM 2077 O OG . SER A 1 268 ? 4.549 119.298 58.257 1.00 155.21 ? 1087 SER A OG 1 +ATOM 2078 N N . PRO A 1 269 ? 5.245 116.642 61.327 1.00 255.59 ? 1088 PRO A N 1 +ATOM 2079 C CA . PRO A 1 269 ? 5.859 115.315 61.486 1.00 219.65 ? 1088 PRO A CA 1 +ATOM 2080 C C . PRO A 1 269 ? 5.523 114.317 60.379 1.00 215.70 ? 1088 PRO A C 1 +ATOM 2081 O O . PRO A 1 269 ? 6.393 113.539 59.991 1.00 201.68 ? 1088 PRO A O 1 +ATOM 2082 C CB . PRO A 1 269 ? 5.281 114.826 62.816 1.00 177.50 ? 1088 PRO A CB 1 +ATOM 2083 C CG . PRO A 1 269 ? 3.957 115.484 62.910 1.00 201.92 ? 1088 PRO A CG 1 +ATOM 2084 C CD . PRO A 1 269 ? 4.089 116.820 62.227 1.00 239.76 ? 1088 PRO A CD 1 +ATOM 2085 N N . ARG A 1 270 ? 4.283 114.347 59.895 1.00 219.41 ? 1089 ARG A N 1 +ATOM 2086 C CA . ARG A 1 270 ? 3.771 113.390 58.909 1.00 202.83 ? 1089 ARG A CA 1 +ATOM 2087 C C . ARG A 1 270 ? 4.658 113.201 57.661 1.00 206.43 ? 1089 ARG A C 1 +ATOM 2088 O O . ARG A 1 270 ? 4.915 112.067 57.235 1.00 123.11 ? 1089 ARG A O 1 +ATOM 2089 C CB . ARG A 1 270 ? 2.335 113.772 58.515 1.00 168.80 ? 1089 ARG A CB 1 +ATOM 2090 C CG . ARG A 1 270 ? 1.942 113.353 57.113 1.00 190.23 ? 1089 ARG A CG 1 +ATOM 2091 C CD . ARG A 1 270 ? 0.483 113.650 56.811 1.00 185.58 ? 1089 ARG A CD 1 +ATOM 2092 N NE . ARG A 1 270 ? 0.190 113.464 55.391 1.00 193.80 ? 1089 ARG A NE 1 +ATOM 2093 C CZ . ARG A 1 270 ? -0.004 112.281 54.813 1.00 193.27 ? 1089 ARG A CZ 1 +ATOM 2094 N NH1 . ARG A 1 270 ? 0.065 111.168 55.531 1.00 199.40 ? 1089 ARG A NH1 1 +ATOM 2095 N NH2 . ARG A 1 270 ? -0.264 112.211 53.513 1.00 165.98 ? 1089 ARG A NH2 1 +ATOM 2096 N N . GLU A 1 271 ? 5.122 114.309 57.087 1.00 235.09 ? 1090 GLU A N 1 +ATOM 2097 C CA . GLU A 1 271 ? 6.006 114.262 55.925 1.00 227.31 ? 1090 GLU A CA 1 +ATOM 2098 C C . GLU A 1 271 ? 7.350 113.654 56.306 1.00 216.97 ? 1090 GLU A C 1 +ATOM 2099 O O . GLU A 1 271 ? 7.893 112.821 55.581 1.00 183.30 ? 1090 GLU A O 1 +ATOM 2100 C CB . GLU A 1 271 ? 6.245 115.667 55.368 1.00 227.46 ? 1090 GLU A CB 1 +ATOM 2101 C CG . GLU A 1 271 ? 5.013 116.551 55.293 1.00 236.58 ? 1090 GLU A CG 1 +ATOM 2102 C CD . GLU A 1 271 ? 5.367 118.000 54.999 1.00 240.61 ? 1090 GLU A CD 1 +ATOM 2103 O OE1 . GLU A 1 271 ? 6.509 118.251 54.555 1.00 232.06 ? 1090 GLU A OE1 1 +ATOM 2104 O OE2 . GLU A 1 271 ? 4.513 118.885 55.221 1.00 238.51 ? 1090 GLU A OE2 1 +ATOM 2105 N N . VAL A 1 272 ? 7.876 114.087 57.450 1.00 230.92 ? 1091 VAL A N 1 +ATOM 2106 C CA . VAL A 1 272 ? 9.203 113.686 57.911 1.00 223.28 ? 1091 VAL A CA 1 +ATOM 2107 C C . VAL A 1 272 ? 9.343 112.169 58.013 1.00 223.86 ? 1091 VAL A C 1 +ATOM 2108 O O . VAL A 1 272 ? 10.347 111.602 57.588 1.00 214.88 ? 1091 VAL A O 1 +ATOM 2109 C CB . VAL A 1 272 ? 9.544 114.325 59.276 1.00 179.24 ? 1091 VAL A CB 1 +ATOM 2110 C CG1 . VAL A 1 272 ? 11.003 114.069 59.636 1.00 169.95 ? 1091 VAL A CG1 1 +ATOM 2111 C CG2 . VAL A 1 272 ? 9.252 115.818 59.251 1.00 160.15 ? 1091 VAL A CG2 1 +ATOM 2112 N N . PHE A 1 273 ? 8.326 111.519 58.570 1.00 225.47 ? 1092 PHE A N 1 +ATOM 2113 C CA . PHE A 1 273 ? 8.324 110.066 58.693 1.00 219.18 ? 1092 PHE A CA 1 +ATOM 2114 C C . PHE A 1 273 ? 8.292 109.406 57.321 1.00 200.27 ? 1092 PHE A C 1 +ATOM 2115 O O . PHE A 1 273 ? 9.135 108.566 57.009 1.00 195.19 ? 1092 PHE A O 1 +ATOM 2116 C CB . PHE A 1 273 ? 7.130 109.601 59.532 1.00 232.65 ? 1092 PHE A CB 1 +ATOM 2117 C CG . PHE A 1 273 ? 6.935 108.109 59.542 1.00 234.10 ? 1092 PHE A CG 1 +ATOM 2118 C CD1 . PHE A 1 273 ? 7.779 107.290 60.271 1.00 225.35 ? 1092 PHE A CD1 1 +ATOM 2119 C CD2 . PHE A 1 273 ? 5.904 107.528 58.823 1.00 231.94 ? 1092 PHE A CD2 1 +ATOM 2120 C CE1 . PHE A 1 273 ? 7.602 105.923 60.277 1.00 207.66 ? 1092 PHE A CE1 1 +ATOM 2121 C CE2 . PHE A 1 273 ? 5.721 106.161 58.830 1.00 221.13 ? 1092 PHE A CE2 1 +ATOM 2122 C CZ . PHE A 1 273 ? 6.569 105.359 59.560 1.00 206.23 ? 1092 PHE A CZ 1 +ATOM 2123 N N . PHE A 1 274 ? 7.322 109.804 56.504 1.00 183.76 ? 1093 PHE A N 1 +ATOM 2124 C CA . PHE A 1 274 ? 7.108 109.201 55.191 1.00 203.91 ? 1093 PHE A CA 1 +ATOM 2125 C C . PHE A 1 274 ? 8.331 109.261 54.273 1.00 213.86 ? 1093 PHE A C 1 +ATOM 2126 O O . PHE A 1 274 ? 8.639 108.287 53.585 1.00 207.09 ? 1093 PHE A O 1 +ATOM 2127 C CB . PHE A 1 274 ? 5.906 109.850 54.500 1.00 227.38 ? 1093 PHE A CB 1 +ATOM 2128 C CG . PHE A 1 274 ? 5.659 109.337 53.109 1.00 238.43 ? 1093 PHE A CG 1 +ATOM 2129 C CD1 . PHE A 1 274 ? 4.999 108.134 52.908 1.00 207.32 ? 1093 PHE A CD1 1 +ATOM 2130 C CD2 . PHE A 1 274 ? 6.087 110.057 52.002 1.00 231.90 ? 1093 PHE A CD2 1 +ATOM 2131 C CE1 . PHE A 1 274 ? 4.772 107.657 51.630 1.00 199.31 ? 1093 PHE A CE1 1 +ATOM 2132 C CE2 . PHE A 1 274 ? 5.864 109.588 50.720 1.00 187.07 ? 1093 PHE A CE2 1 +ATOM 2133 C CZ . PHE A 1 274 ? 5.205 108.385 50.533 1.00 180.18 ? 1093 PHE A CZ 1 +ATOM 2134 N N . ARG A 1 275 ? 9.018 110.400 54.257 1.00 215.93 ? 1094 ARG A N 1 +ATOM 2135 C CA . ARG A 1 275 ? 10.181 110.568 53.386 1.00 206.20 ? 1094 ARG A CA 1 +ATOM 2136 C C . ARG A 1 275 ? 11.344 109.713 53.877 1.00 194.06 ? 1094 ARG A C 1 +ATOM 2137 O O . ARG A 1 275 ? 12.043 109.088 53.080 1.00 188.45 ? 1094 ARG A O 1 +ATOM 2138 C CB . ARG A 1 275 ? 10.604 112.039 53.292 1.00 212.48 ? 1094 ARG A CB 1 +ATOM 2139 C CG . ARG A 1 275 ? 11.141 112.453 51.918 1.00 213.95 ? 1094 ARG A CG 1 +ATOM 2140 C CD . ARG A 1 275 ? 11.735 113.834 51.971 1.00 212.17 ? 1094 ARG A CD 1 +ATOM 2141 N NE . ARG A 1 275 ? 11.146 114.707 52.958 1.00 210.97 ? 1094 ARG A NE 1 +ATOM 2142 C CZ . ARG A 1 275 ? 10.135 115.540 52.726 1.00 189.87 ? 1094 ARG A CZ 1 +ATOM 2143 N NH1 . ARG A 1 275 ? 9.613 115.637 51.509 1.00 159.07 ? 1094 ARG A NH1 1 +ATOM 2144 N NH2 . ARG A 1 275 ? 9.646 116.279 53.716 1.00 157.53 ? 1094 ARG A NH2 1 +ATOM 2145 N N . VAL A 1 276 ? 11.542 109.693 55.193 1.00 179.92 ? 1095 VAL A N 1 +ATOM 2146 C CA . VAL A 1 276 ? 12.575 108.864 55.807 1.00 172.75 ? 1095 VAL A CA 1 +ATOM 2147 C C . VAL A 1 276 ? 12.249 107.392 55.598 1.00 167.47 ? 1095 VAL A C 1 +ATOM 2148 O O . VAL A 1 276 ? 13.144 106.564 55.405 1.00 154.50 ? 1095 VAL A O 1 +ATOM 2149 C CB . VAL A 1 276 ? 12.712 109.159 57.313 1.00 177.36 ? 1095 VAL A CB 1 +ATOM 2150 C CG1 . VAL A 1 276 ? 13.560 108.100 57.998 1.00 148.12 ? 1095 VAL A CG1 1 +ATOM 2151 C CG2 . VAL A 1 276 ? 13.309 110.539 57.525 1.00 209.15 ? 1095 VAL A CG2 1 +ATOM 2152 N N . ALA A 1 277 ? 10.955 107.083 55.627 1.00 179.17 ? 1096 ALA A N 1 +ATOM 2153 C CA . ALA A 1 277 ? 10.468 105.742 55.332 1.00 159.19 ? 1096 ALA A CA 1 +ATOM 2154 C C . ALA A 1 277 ? 10.814 105.371 53.895 1.00 153.02 ? 1096 ALA A C 1 +ATOM 2155 O O . ALA A 1 277 ? 11.400 104.315 53.638 1.00 123.07 ? 1096 ALA A O 1 +ATOM 2156 C CB . ALA A 1 277 ? 8.960 105.659 55.563 1.00 131.66 ? 1096 ALA A CB 1 +ATOM 2157 N N . ALA A 1 278 ? 10.461 106.262 52.970 1.00 166.84 ? 1097 ALA A N 1 +ATOM 2158 C CA . ALA A 1 278 ? 10.712 106.058 51.545 1.00 155.04 ? 1097 ALA A CA 1 +ATOM 2159 C C . ALA A 1 278 ? 12.195 106.146 51.189 1.00 148.02 ? 1097 ALA A C 1 +ATOM 2160 O O . ALA A 1 278 ? 12.631 105.571 50.193 1.00 134.06 ? 1097 ALA A O 1 +ATOM 2161 C CB . ALA A 1 278 ? 9.894 107.044 50.706 1.00 128.49 ? 1097 ALA A CB 1 +ATOM 2162 N N . ASP A 1 279 ? 12.972 106.864 51.997 1.00 145.89 ? 1098 ASP A N 1 +ATOM 2163 C CA . ASP A 1 279 ? 14.414 106.924 51.776 1.00 152.47 ? 1098 ASP A CA 1 +ATOM 2164 C C . ASP A 1 279 ? 15.080 105.616 52.212 1.00 177.99 ? 1098 ASP A C 1 +ATOM 2165 O O . ASP A 1 279 ? 16.022 105.136 51.571 1.00 148.18 ? 1098 ASP A O 1 +ATOM 2166 C CB . ASP A 1 279 ? 15.036 108.121 52.499 1.00 144.74 ? 1098 ASP A CB 1 +ATOM 2167 C CG . ASP A 1 279 ? 16.312 108.606 51.832 1.00 167.41 ? 1098 ASP A CG 1 +ATOM 2168 O OD1 . ASP A 1 279 ? 17.393 108.062 52.146 1.00 158.34 ? 1098 ASP A OD1 1 +ATOM 2169 O OD2 . ASP A 1 279 ? 16.230 109.529 50.990 1.00 175.02 ? 1098 ASP A OD2 1 +ATOM 2170 N N . MET A 1 280 ? 14.579 105.039 53.302 1.00 184.09 ? 1099 MET A N 1 +ATOM 2171 C CA . MET A 1 280 ? 15.066 103.749 53.772 1.00 169.89 ? 1099 MET A CA 1 +ATOM 2172 C C . MET A 1 280 ? 14.843 102.674 52.718 1.00 147.14 ? 1099 MET A C 1 +ATOM 2173 O O . MET A 1 280 ? 15.599 101.707 52.635 1.00 136.83 ? 1099 MET A O 1 +ATOM 2174 C CB . MET A 1 280 ? 14.361 103.339 55.067 1.00 187.00 ? 1099 MET A CB 1 +ATOM 2175 C CG . MET A 1 280 ? 14.941 103.947 56.332 1.00 201.31 ? 1099 MET A CG 1 +ATOM 2176 S SD . MET A 1 280 ? 14.256 103.189 57.816 1.00 195.68 ? 1099 MET A SD 1 +ATOM 2177 C CE . MET A 1 280 ? 14.550 101.462 57.448 1.00 118.93 ? 1099 MET A CE 1 +ATOM 2178 N N . PHE A 1 281 ? 13.802 102.856 51.910 1.00 143.85 ? 1100 PHE A N 1 +ATOM 2179 C CA . PHE A 1 281 ? 13.374 101.829 50.967 1.00 155.01 ? 1100 PHE A CA 1 +ATOM 2180 C C . PHE A 1 281 ? 13.524 102.237 49.509 1.00 171.24 ? 1100 PHE A C 1 +ATOM 2181 O O . PHE A 1 281 ? 12.741 101.823 48.649 1.00 158.70 ? 1100 PHE A O 1 +ATOM 2182 C CB . PHE A 1 281 ? 11.936 101.424 51.264 1.00 137.10 ? 1100 PHE A CB 1 +ATOM 2183 C CG . PHE A 1 281 ? 11.774 100.730 52.582 1.00 165.68 ? 1100 PHE A CG 1 +ATOM 2184 C CD1 . PHE A 1 281 ? 12.669 99.740 52.969 1.00 162.46 ? 1100 PHE A CD1 1 +ATOM 2185 C CD2 . PHE A 1 281 ? 10.744 101.077 53.444 1.00 137.62 ? 1100 PHE A CD2 1 +ATOM 2186 C CE1 . PHE A 1 281 ? 12.530 99.098 54.181 1.00 151.21 ? 1100 PHE A CE1 1 +ATOM 2187 C CE2 . PHE A 1 281 ? 10.596 100.436 54.659 1.00 133.38 ? 1100 PHE A CE2 1 +ATOM 2188 C CZ . PHE A 1 281 ? 11.493 99.446 55.030 1.00 147.47 ? 1100 PHE A CZ 1 +ATOM 2189 N N . SER A 1 282 ? 14.542 103.047 49.244 1.00 197.35 ? 1101 SER A N 1 +ATOM 2190 C CA . SER A 1 282 ? 14.875 103.459 47.890 1.00 212.12 ? 1101 SER A CA 1 +ATOM 2191 C C . SER A 1 282 ? 15.715 102.378 47.210 1.00 210.96 ? 1101 SER A C 1 +ATOM 2192 O O . SER A 1 282 ? 15.723 102.256 45.981 1.00 169.44 ? 1101 SER A O 1 +ATOM 2193 C CB . SER A 1 282 ? 15.630 104.784 47.926 1.00 214.33 ? 1101 SER A CB 1 +ATOM 2194 O OG . SER A 1 282 ? 16.878 104.641 48.591 1.00 210.16 ? 1101 SER A OG 1 +ATOM 2195 N N . ASP A 1 283 ? 16.425 101.599 48.023 1.00 215.08 ? 1102 ASP A N 1 +ATOM 2196 C CA . ASP A 1 283 ? 17.144 100.435 47.524 1.00 179.58 ? 1102 ASP A CA 1 +ATOM 2197 C C . ASP A 1 283 ? 16.218 99.218 47.496 1.00 147.94 ? 1102 ASP A C 1 +ATOM 2198 O O . ASP A 1 283 ? 16.556 98.174 46.929 1.00 101.24 ? 1102 ASP A O 1 +ATOM 2199 C CB . ASP A 1 283 ? 18.434 100.177 48.324 1.00 173.06 ? 1102 ASP A CB 1 +ATOM 2200 C CG . ASP A 1 283 ? 18.202 99.971 49.807 1.00 179.45 ? 1102 ASP A CG 1 +ATOM 2201 O OD1 . ASP A 1 283 ? 17.199 100.499 50.328 1.00 196.55 ? 1102 ASP A OD1 1 +ATOM 2202 O OD2 . ASP A 1 283 ? 19.039 99.292 50.454 1.00 140.01 ? 1102 ASP A OD2 1 +ATOM 2203 N N . GLY A 1 284 ? 15.045 99.378 48.108 1.00 145.11 ? 1103 GLY A N 1 +ATOM 2204 C CA . GLY A 1 284 ? 13.963 98.411 48.012 1.00 153.13 ? 1103 GLY A CA 1 +ATOM 2205 C C . GLY A 1 284 ? 14.326 97.014 48.473 1.00 179.57 ? 1103 GLY A C 1 +ATOM 2206 O O . GLY A 1 284 ? 13.821 96.018 47.936 1.00 111.97 ? 1103 GLY A O 1 +ATOM 2207 N N . ASN A 1 285 ? 15.219 96.958 49.461 1.00 219.31 ? 1104 ASN A N 1 +ATOM 2208 C CA . ASN A 1 285 ? 15.646 95.711 50.093 1.00 196.26 ? 1104 ASN A CA 1 +ATOM 2209 C C . ASN A 1 285 ? 15.043 95.574 51.492 1.00 153.28 ? 1104 ASN A C 1 +ATOM 2210 O O . ASN A 1 285 ? 15.728 95.782 52.496 1.00 145.98 ? 1104 ASN A O 1 +ATOM 2211 C CB . ASN A 1 285 ? 17.179 95.625 50.180 1.00 176.80 ? 1104 ASN A CB 1 +ATOM 2212 C CG . ASN A 1 285 ? 17.857 95.672 48.814 1.00 179.89 ? 1104 ASN A CG 1 +ATOM 2213 O OD1 . ASN A 1 285 ? 17.231 95.424 47.782 1.00 166.11 ? 1104 ASN A OD1 1 +ATOM 2214 N ND2 . ASN A 1 285 ? 19.150 95.988 48.809 1.00 148.28 ? 1104 ASN A ND2 1 +ATOM 2215 N N . PHE A 1 286 ? 13.756 95.222 51.531 1.00 143.05 ? 1105 PHE A N 1 +ATOM 2216 C CA . PHE A 1 286 ? 12.989 95.070 52.767 1.00 161.18 ? 1105 PHE A CA 1 +ATOM 2217 C C . PHE A 1 286 ? 13.433 93.851 53.573 1.00 199.28 ? 1105 PHE A C 1 +ATOM 2218 O O . PHE A 1 286 ? 13.610 92.761 53.026 1.00 208.22 ? 1105 PHE A O 1 +ATOM 2219 C CB . PHE A 1 286 ? 11.491 94.888 52.463 1.00 147.65 ? 1105 PHE A CB 1 +ATOM 2220 C CG . PHE A 1 286 ? 10.827 96.075 51.803 1.00 194.31 ? 1105 PHE A CG 1 +ATOM 2221 C CD1 . PHE A 1 286 ? 10.374 97.141 52.563 1.00 227.01 ? 1105 PHE A CD1 1 +ATOM 2222 C CD2 . PHE A 1 286 ? 10.601 96.096 50.430 1.00 159.35 ? 1105 PHE A CD2 1 +ATOM 2223 C CE1 . PHE A 1 286 ? 9.742 98.220 51.968 1.00 224.86 ? 1105 PHE A CE1 1 +ATOM 2224 C CE2 . PHE A 1 286 ? 9.977 97.175 49.829 1.00 126.39 ? 1105 PHE A CE2 1 +ATOM 2225 C CZ . PHE A 1 286 ? 9.545 98.237 50.600 1.00 174.96 ? 1105 PHE A CZ 1 +ATOM 2226 N N . ASN A 1 287 ? 13.594 94.047 54.878 1.00 206.91 ? 1106 ASN A N 1 +ATOM 2227 C CA . ASN A 1 287 ? 13.756 92.959 55.837 1.00 178.77 ? 1106 ASN A CA 1 +ATOM 2228 C C . ASN A 1 287 ? 13.145 93.386 57.172 1.00 173.34 ? 1106 ASN A C 1 +ATOM 2229 O O . ASN A 1 287 ? 13.099 94.580 57.479 1.00 150.31 ? 1106 ASN A O 1 +ATOM 2230 C CB . ASN A 1 287 ? 15.229 92.561 56.001 1.00 164.31 ? 1106 ASN A CB 1 +ATOM 2231 C CG . ASN A 1 287 ? 16.167 93.758 55.996 1.00 157.58 ? 1106 ASN A CG 1 +ATOM 2232 O OD1 . ASN A 1 287 ? 16.113 94.612 56.882 1.00 151.83 ? 1106 ASN A OD1 1 +ATOM 2233 N ND2 . ASN A 1 287 ? 17.045 93.816 55.001 1.00 131.42 ? 1106 ASN A ND2 1 +ATOM 2234 N N . TRP A 1 288 ? 12.669 92.418 57.953 1.00 169.71 ? 1107 TRP A N 1 +ATOM 2235 C CA . TRP A 1 288 ? 11.994 92.696 59.221 1.00 125.59 ? 1107 TRP A CA 1 +ATOM 2236 C C . TRP A 1 288 ? 12.772 93.603 60.166 1.00 130.78 ? 1107 TRP A C 1 +ATOM 2237 O O . TRP A 1 288 ? 12.178 94.312 60.970 1.00 124.42 ? 1107 TRP A O 1 +ATOM 2238 C CB . TRP A 1 288 ? 11.662 91.398 59.944 1.00 134.17 ? 1107 TRP A CB 1 +ATOM 2239 C CG . TRP A 1 288 ? 10.221 91.124 59.968 1.00 172.73 ? 1107 TRP A CG 1 +ATOM 2240 C CD1 . TRP A 1 288 ? 9.570 90.127 59.314 1.00 203.78 ? 1107 TRP A CD1 1 +ATOM 2241 C CD2 . TRP A 1 288 ? 9.220 91.871 60.666 1.00 191.67 ? 1107 TRP A CD2 1 +ATOM 2242 N NE1 . TRP A 1 288 ? 8.223 90.195 59.572 1.00 228.56 ? 1107 TRP A NE1 1 +ATOM 2243 C CE2 . TRP A 1 288 ? 7.982 91.260 60.401 1.00 221.30 ? 1107 TRP A CE2 1 +ATOM 2244 C CE3 . TRP A 1 288 ? 9.252 92.994 61.496 1.00 178.54 ? 1107 TRP A CE3 1 +ATOM 2245 C CZ2 . TRP A 1 288 ? 6.783 91.735 60.936 1.00 199.05 ? 1107 TRP A CZ2 1 +ATOM 2246 C CZ3 . TRP A 1 288 ? 8.060 93.465 62.029 1.00 159.44 ? 1107 TRP A CZ3 1 +ATOM 2247 C CH2 . TRP A 1 288 ? 6.843 92.838 61.744 1.00 150.95 ? 1107 TRP A CH2 1 +ATOM 2248 N N . GLY A 1 289 ? 14.097 93.567 60.075 1.00 126.75 ? 1108 GLY A N 1 +ATOM 2249 C CA . GLY A 1 289 ? 14.937 94.442 60.873 1.00 141.61 ? 1108 GLY A CA 1 +ATOM 2250 C C . GLY A 1 289 ? 14.618 95.912 60.659 1.00 164.68 ? 1108 GLY A C 1 +ATOM 2251 O O . GLY A 1 289 ? 14.561 96.689 61.613 1.00 144.77 ? 1108 GLY A O 1 +ATOM 2252 N N . ARG A 1 290 ? 14.405 96.290 59.401 1.00 165.96 ? 1109 ARG A N 1 +ATOM 2253 C CA . ARG A 1 290 ? 14.089 97.672 59.056 1.00 135.37 ? 1109 ARG A CA 1 +ATOM 2254 C C . ARG A 1 290 ? 12.648 98.030 59.394 1.00 141.45 ? 1109 ARG A C 1 +ATOM 2255 O O . ARG A 1 290 ? 12.358 99.159 59.790 1.00 137.50 ? 1109 ARG A O 1 +ATOM 2256 C CB . ARG A 1 290 ? 14.342 97.924 57.576 1.00 102.14 ? 1109 ARG A CB 1 +ATOM 2257 C CG . ARG A 1 290 ? 15.800 97.991 57.196 1.00 133.86 ? 1109 ARG A CG 1 +ATOM 2258 C CD . ARG A 1 290 ? 15.927 98.462 55.766 1.00 154.36 ? 1109 ARG A CD 1 +ATOM 2259 N NE . ARG A 1 290 ? 17.306 98.460 55.298 1.00 161.44 ? 1109 ARG A NE 1 +ATOM 2260 C CZ . ARG A 1 290 ? 17.660 98.702 54.041 1.00 179.41 ? 1109 ARG A CZ 1 +ATOM 2261 N NH1 . ARG A 1 290 ? 16.731 98.962 53.128 1.00 194.97 ? 1109 ARG A NH1 1 +ATOM 2262 N NH2 . ARG A 1 290 ? 18.940 98.680 53.698 1.00 164.71 ? 1109 ARG A NH2 1 +ATOM 2263 N N . VAL A 1 291 ? 11.750 97.064 59.219 1.00 139.48 ? 1110 VAL A N 1 +ATOM 2264 C CA . VAL A 1 291 ? 10.351 97.217 59.598 1.00 125.28 ? 1110 VAL A CA 1 +ATOM 2265 C C . VAL A 1 291 ? 10.261 97.575 61.079 1.00 128.27 ? 1110 VAL A C 1 +ATOM 2266 O O . VAL A 1 291 ? 9.447 98.404 61.495 1.00 131.74 ? 1110 VAL A O 1 +ATOM 2267 C CB . VAL A 1 291 ? 9.578 95.910 59.347 1.00 146.17 ? 1110 VAL A CB 1 +ATOM 2268 C CG1 . VAL A 1 291 ? 8.118 96.059 59.745 1.00 146.75 ? 1110 VAL A CG1 1 +ATOM 2269 C CG2 . VAL A 1 291 ? 9.706 95.497 57.893 1.00 112.99 ? 1110 VAL A CG2 1 +ATOM 2270 N N . VAL A 1 292 ? 11.129 96.949 61.866 1.00 125.02 ? 1111 VAL A N 1 +ATOM 2271 C CA . VAL A 1 292 ? 11.168 97.171 63.300 1.00 132.44 ? 1111 VAL A CA 1 +ATOM 2272 C C . VAL A 1 292 ? 11.931 98.450 63.645 1.00 134.70 ? 1111 VAL A C 1 +ATOM 2273 O O . VAL A 1 292 ? 11.481 99.234 64.481 1.00 140.41 ? 1111 VAL A O 1 +ATOM 2274 C CB . VAL A 1 292 ? 11.779 95.960 64.023 1.00 118.24 ? 1111 VAL A CB 1 +ATOM 2275 C CG1 . VAL A 1 292 ? 11.961 96.250 65.478 1.00 87.27 ? 1111 VAL A CG1 1 +ATOM 2276 C CG2 . VAL A 1 292 ? 10.883 94.761 63.866 1.00 137.15 ? 1111 VAL A CG2 1 +ATOM 2277 N N . ALA A 1 293 ? 13.071 98.670 62.993 1.00 125.20 ? 1112 ALA A N 1 +ATOM 2278 C CA . ALA A 1 293 ? 13.865 99.874 63.253 1.00 127.01 ? 1112 ALA A CA 1 +ATOM 2279 C C . ALA A 1 293 ? 13.116 101.133 62.830 1.00 150.41 ? 1112 ALA A C 1 +ATOM 2280 O O . ALA A 1 293 ? 13.339 102.213 63.373 1.00 136.82 ? 1112 ALA A O 1 +ATOM 2281 C CB . ALA A 1 293 ? 15.238 99.798 62.574 1.00 110.94 ? 1112 ALA A CB 1 +ATOM 2282 N N . LEU A 1 294 ? 12.215 100.989 61.868 1.00 158.28 ? 1113 LEU A N 1 +ATOM 2283 C CA . LEU A 1 294 ? 11.372 102.104 61.478 1.00 146.68 ? 1113 LEU A CA 1 +ATOM 2284 C C . LEU A 1 294 ? 10.148 102.168 62.389 1.00 131.93 ? 1113 LEU A C 1 +ATOM 2285 O O . LEU A 1 294 ? 9.513 103.213 62.521 1.00 140.10 ? 1113 LEU A O 1 +ATOM 2286 C CB . LEU A 1 294 ? 10.982 101.986 60.007 1.00 112.17 ? 1113 LEU A CB 1 +ATOM 2287 C CG . LEU A 1 294 ? 10.168 103.124 59.413 1.00 136.69 ? 1113 LEU A CG 1 +ATOM 2288 C CD1 . LEU A 1 294 ? 10.645 103.374 58.012 1.00 130.19 ? 1113 LEU A CD1 1 +ATOM 2289 C CD2 . LEU A 1 294 ? 8.707 102.745 59.409 1.00 170.53 ? 1113 LEU A CD2 1 +ATOM 2290 N N . PHE A 1 295 ? 9.831 101.050 63.033 1.00 114.43 ? 1114 PHE A N 1 +ATOM 2291 C CA . PHE A 1 295 ? 8.745 101.022 64.005 1.00 137.85 ? 1114 PHE A CA 1 +ATOM 2292 C C . PHE A 1 295 ? 9.239 101.447 65.387 1.00 150.04 ? 1114 PHE A C 1 +ATOM 2293 O O . PHE A 1 295 ? 8.446 101.590 66.309 1.00 167.63 ? 1114 PHE A O 1 +ATOM 2294 C CB . PHE A 1 295 ? 8.104 99.634 64.071 1.00 142.70 ? 1114 PHE A CB 1 +ATOM 2295 C CG . PHE A 1 295 ? 6.747 99.619 64.728 1.00 169.32 ? 1114 PHE A CG 1 +ATOM 2296 C CD1 . PHE A 1 295 ? 5.618 100.022 64.027 1.00 175.40 ? 1114 PHE A CD1 1 +ATOM 2297 C CD2 . PHE A 1 295 ? 6.598 99.188 66.040 1.00 149.41 ? 1114 PHE A CD2 1 +ATOM 2298 C CE1 . PHE A 1 295 ? 4.365 100.004 64.624 1.00 178.42 ? 1114 PHE A CE1 1 +ATOM 2299 C CE2 . PHE A 1 295 ? 5.348 99.168 66.646 1.00 160.04 ? 1114 PHE A CE2 1 +ATOM 2300 C CZ . PHE A 1 295 ? 4.230 99.574 65.935 1.00 183.12 ? 1114 PHE A CZ 1 +ATOM 2301 N N . TYR A 1 296 ? 10.551 101.621 65.526 1.00 149.91 ? 1115 TYR A N 1 +ATOM 2302 C CA . TYR A 1 296 ? 11.146 102.230 66.716 1.00 154.95 ? 1115 TYR A CA 1 +ATOM 2303 C C . TYR A 1 296 ? 11.152 103.721 66.424 1.00 170.50 ? 1115 TYR A C 1 +ATOM 2304 O O . TYR A 1 296 ? 11.035 104.550 67.324 1.00 142.94 ? 1115 TYR A O 1 +ATOM 2305 C CB . TYR A 1 296 ? 12.572 101.656 66.934 1.00 155.57 ? 1115 TYR A CB 1 +ATOM 2306 C CG . TYR A 1 296 ? 13.451 102.226 68.069 1.00 169.05 ? 1115 TYR A CG 1 +ATOM 2307 C CD1 . TYR A 1 296 ? 13.281 101.844 69.406 1.00 195.23 ? 1115 TYR A CD1 1 +ATOM 2308 C CD2 . TYR A 1 296 ? 14.443 103.152 67.793 1.00 163.04 ? 1115 TYR A CD2 1 +ATOM 2309 C CE1 . TYR A 1 296 ? 14.091 102.375 70.421 1.00 202.50 ? 1115 TYR A CE1 1 +ATOM 2310 C CE2 . TYR A 1 296 ? 15.248 103.680 68.796 1.00 159.11 ? 1115 TYR A CE2 1 +ATOM 2311 C CZ . TYR A 1 296 ? 15.069 103.296 70.106 1.00 160.54 ? 1115 TYR A CZ 1 +ATOM 2312 O OH . TYR A 1 296 ? 15.877 103.837 71.088 1.00 137.91 ? 1115 TYR A OH 1 +ATOM 2313 N N . PHE A 1 297 ? 11.269 104.056 65.142 1.00 176.24 ? 1116 PHE A N 1 +ATOM 2314 C CA . PHE A 1 297 ? 11.218 105.448 64.725 1.00 160.37 ? 1116 PHE A CA 1 +ATOM 2315 C C . PHE A 1 297 ? 9.798 105.998 64.892 1.00 143.64 ? 1116 PHE A C 1 +ATOM 2316 O O . PHE A 1 297 ? 9.562 106.856 65.741 1.00 120.87 ? 1116 PHE A O 1 +ATOM 2317 C CB . PHE A 1 297 ? 11.717 105.601 63.290 1.00 159.58 ? 1116 PHE A CB 1 +ATOM 2318 C CG . PHE A 1 297 ? 12.056 107.011 62.920 1.00 187.02 ? 1116 PHE A CG 1 +ATOM 2319 C CD1 . PHE A 1 297 ? 13.231 107.593 63.362 1.00 170.61 ? 1116 PHE A CD1 1 +ATOM 2320 C CD2 . PHE A 1 297 ? 11.194 107.761 62.140 1.00 220.62 ? 1116 PHE A CD2 1 +ATOM 2321 C CE1 . PHE A 1 297 ? 13.544 108.889 63.022 1.00 194.15 ? 1116 PHE A CE1 1 +ATOM 2322 C CE2 . PHE A 1 297 ? 11.501 109.063 61.799 1.00 219.32 ? 1116 PHE A CE2 1 +ATOM 2323 C CZ . PHE A 1 297 ? 12.676 109.627 62.242 1.00 213.35 ? 1116 PHE A CZ 1 +ATOM 2324 N N . ALA A 1 298 ? 8.852 105.483 64.108 1.00 130.91 ? 1117 ALA A N 1 +ATOM 2325 C CA . ALA A 1 298 ? 7.439 105.841 64.261 1.00 148.51 ? 1117 ALA A CA 1 +ATOM 2326 C C . ALA A 1 298 ? 6.978 105.738 65.723 1.00 185.95 ? 1117 ALA A C 1 +ATOM 2327 O O . ALA A 1 298 ? 6.058 106.439 66.153 1.00 180.11 ? 1117 ALA A O 1 +ATOM 2328 C CB . ALA A 1 298 ? 6.576 104.968 63.366 1.00 146.91 ? 1117 ALA A CB 1 +ATOM 2329 N N . SER A 1 299 ? 7.628 104.852 66.474 1.00 198.92 ? 1118 SER A N 1 +ATOM 2330 C CA . SER A 1 299 ? 7.477 104.798 67.921 1.00 182.47 ? 1118 SER A CA 1 +ATOM 2331 C C . SER A 1 299 ? 7.907 106.141 68.506 1.00 171.25 ? 1118 SER A C 1 +ATOM 2332 O O . SER A 1 299 ? 7.077 106.892 69.011 1.00 181.91 ? 1118 SER A O 1 +ATOM 2333 C CB . SER A 1 299 ? 8.326 103.660 68.502 1.00 174.15 ? 1118 SER A CB 1 +ATOM 2334 O OG . SER A 1 299 ? 8.008 103.367 69.851 1.00 177.25 ? 1118 SER A OG 1 +ATOM 2335 N N . LYS A 1 300 ? 9.198 106.454 68.402 1.00 144.45 ? 1119 LYS A N 1 +ATOM 2336 C CA . LYS A 1 300 ? 9.760 107.694 68.953 1.00 150.65 ? 1119 LYS A CA 1 +ATOM 2337 C C . LYS A 1 300 ? 9.066 108.990 68.490 1.00 194.92 ? 1119 LYS A C 1 +ATOM 2338 O O . LYS A 1 300 ? 9.281 110.052 69.075 1.00 195.35 ? 1119 LYS A O 1 +ATOM 2339 C CB . LYS A 1 300 ? 11.262 107.782 68.659 1.00 148.53 ? 1119 LYS A CB 1 +ATOM 2340 C CG . LYS A 1 300 ? 12.144 106.837 69.469 1.00 141.78 ? 1119 LYS A CG 1 +ATOM 2341 C CD . LYS A 1 300 ? 12.424 107.372 70.869 1.00 112.05 ? 1119 LYS A CD 1 +ATOM 2342 C CE . LYS A 1 300 ? 13.653 106.698 71.487 1.00 136.34 ? 1119 LYS A CE 1 +ATOM 2343 N NZ . LYS A 1 300 ? 13.690 106.810 72.985 1.00 140.92 ? 1119 LYS A NZ 1 +ATOM 2344 N N . LEU A 1 301 ? 8.246 108.903 67.445 1.00 213.14 ? 1120 LEU A N 1 +ATOM 2345 C CA . LEU A 1 301 ? 7.451 110.046 66.992 1.00 184.55 ? 1120 LEU A CA 1 +ATOM 2346 C C . LEU A 1 301 ? 6.175 110.164 67.812 1.00 179.75 ? 1120 LEU A C 1 +ATOM 2347 O O . LEU A 1 301 ? 5.068 110.097 67.272 1.00 147.12 ? 1120 LEU A O 1 +ATOM 2348 C CB . LEU A 1 301 ? 7.107 109.912 65.509 1.00 157.40 ? 1120 LEU A CB 1 +ATOM 2349 C CG . LEU A 1 301 ? 8.337 109.895 64.601 1.00 177.41 ? 1120 LEU A CG 1 +ATOM 2350 C CD1 . LEU A 1 301 ? 7.949 109.758 63.130 1.00 169.77 ? 1120 LEU A CD1 1 +ATOM 2351 C CD2 . LEU A 1 301 ? 9.200 111.136 64.840 1.00 159.76 ? 1120 LEU A CD2 1 +ATOM 2352 N N . VAL A 1 302 ? 6.352 110.338 69.120 1.00 201.69 ? 1121 VAL A N 1 +ATOM 2353 C CA . VAL A 1 302 ? 5.251 110.374 70.075 1.00 221.91 ? 1121 VAL A CA 1 +ATOM 2354 C C . VAL A 1 302 ? 5.554 111.346 71.223 1.00 223.26 ? 1121 VAL A C 1 +ATOM 2355 O O . VAL A 1 302 ? 4.857 112.351 71.390 1.00 235.09 ? 1121 VAL A O 1 +ATOM 2356 C CB . VAL A 1 302 ? 4.944 108.952 70.637 1.00 175.40 ? 1121 VAL A CB 1 +ATOM 2357 C CG1 . VAL A 1 302 ? 4.127 109.024 71.925 1.00 155.24 ? 1121 VAL A CG1 1 +ATOM 2358 C CG2 . VAL A 1 302 ? 4.228 108.095 69.592 1.00 153.72 ? 1121 VAL A CG2 1 +ATOM 2359 N N . LEU A 1 303 ? 6.607 111.051 71.985 1.00 199.08 ? 1122 LEU A N 1 +ATOM 2360 C CA . LEU A 1 303 ? 6.935 111.785 73.213 1.00 207.32 ? 1122 LEU A CA 1 +ATOM 2361 C C . LEU A 1 303 ? 7.024 113.305 73.048 1.00 210.59 ? 1122 LEU A C 1 +ATOM 2362 O O . LEU A 1 303 ? 6.630 114.062 73.942 1.00 194.54 ? 1122 LEU A O 1 +ATOM 2363 C CB . LEU A 1 303 ? 8.234 111.246 73.831 1.00 195.46 ? 1122 LEU A CB 1 +ATOM 2364 C CG . LEU A 1 303 ? 8.115 110.223 74.970 1.00 177.93 ? 1122 LEU A CG 1 +ATOM 2365 C CD1 . LEU A 1 303 ? 9.487 109.712 75.412 1.00 138.83 ? 1122 LEU A CD1 1 +ATOM 2366 C CD2 . LEU A 1 303 ? 7.352 110.801 76.164 1.00 134.93 ? 1122 LEU A CD2 1 +ATOM 2367 N N . SER B 1 5 ? 21.565 114.478 29.082 1.00 107.25 ? 2 SER B N 1 +ATOM 2368 C CA . SER B 1 5 ? 22.316 113.522 28.263 1.00 152.20 ? 2 SER B CA 1 +ATOM 2369 C C . SER B 1 5 ? 22.098 113.710 26.749 1.00 148.85 ? 2 SER B C 1 +ATOM 2370 O O . SER B 1 5 ? 21.056 114.211 26.316 1.00 112.79 ? 2 SER B O 1 +ATOM 2371 C CB . SER B 1 5 ? 21.996 112.077 28.687 1.00 146.85 ? 2 SER B CB 1 +ATOM 2372 O OG . SER B 1 5 ? 20.774 111.610 28.135 1.00 153.71 ? 2 SER B OG 1 +ATOM 2373 N N . LYS B 1 6 ? 23.094 113.313 25.954 1.00 146.22 ? 3 LYS B N 1 +ATOM 2374 C CA . LYS B 1 6 ? 22.987 113.349 24.492 1.00 140.75 ? 3 LYS B CA 1 +ATOM 2375 C C . LYS B 1 6 ? 22.273 112.087 24.009 1.00 146.27 ? 3 LYS B C 1 +ATOM 2376 O O . LYS B 1 6 ? 21.712 112.051 22.910 1.00 131.74 ? 3 LYS B O 1 +ATOM 2377 C CB . LYS B 1 6 ? 24.365 113.460 23.814 1.00 161.49 ? 3 LYS B CB 1 +ATOM 2378 C CG . LYS B 1 6 ? 25.468 114.141 24.636 1.00 184.35 ? 3 LYS B CG 1 +ATOM 2379 C CD . LYS B 1 6 ? 25.125 115.577 25.035 1.00 196.42 ? 3 LYS B CD 1 +ATOM 2380 C CE . LYS B 1 6 ? 25.706 115.920 26.408 1.00 171.83 ? 3 LYS B CE 1 +ATOM 2381 N NZ . LYS B 1 6 ? 25.187 117.204 26.965 1.00 142.24 ? 3 LYS B NZ 1 +ATOM 2382 N N . GLY B 1 7 ? 22.306 111.052 24.843 1.00 147.66 ? 4 GLY B N 1 +ATOM 2383 C CA . GLY B 1 7 ? 21.606 109.814 24.559 1.00 131.86 ? 4 GLY B CA 1 +ATOM 2384 C C . GLY B 1 7 ? 20.108 110.028 24.505 1.00 128.75 ? 4 GLY B C 1 +ATOM 2385 O O . GLY B 1 7 ? 19.425 109.470 23.646 1.00 117.90 ? 4 GLY B O 1 +ATOM 2386 N N . GLU B 1 8 ? 19.609 110.853 25.420 1.00 105.80 ? 5 GLU B N 1 +ATOM 2387 C CA . GLU B 1 8 ? 18.187 111.160 25.520 1.00 84.83 ? 5 GLU B CA 1 +ATOM 2388 C C . GLU B 1 8 ? 17.559 111.598 24.185 1.00 91.43 ? 5 GLU B C 1 +ATOM 2389 O O . GLU B 1 8 ? 16.388 111.314 23.925 1.00 126.15 ? 5 GLU B O 1 +ATOM 2390 C CB . GLU B 1 8 ? 17.968 112.230 26.601 1.00 112.80 ? 5 GLU B CB 1 +ATOM 2391 C CG . GLU B 1 8 ? 16.518 112.684 26.783 1.00 159.08 ? 5 GLU B CG 1 +ATOM 2392 C CD . GLU B 1 8 ? 15.772 111.922 27.872 1.00 184.56 ? 5 GLU B CD 1 +ATOM 2393 O OE1 . GLU B 1 8 ? 16.133 112.078 29.058 1.00 189.68 ? 5 GLU B OE1 1 +ATOM 2394 O OE2 . GLU B 1 8 ? 14.814 111.183 27.545 1.00 166.28 ? 5 GLU B OE2 1 +ATOM 2395 N N . GLU B 1 9 ? 18.339 112.266 23.336 1.00 102.74 ? 6 GLU B N 1 +ATOM 2396 C CA . GLU B 1 9 ? 17.826 112.819 22.078 1.00 99.59 ? 6 GLU B CA 1 +ATOM 2397 C C . GLU B 1 9 ? 17.576 111.759 21.015 1.00 107.10 ? 6 GLU B C 1 +ATOM 2398 O O . GLU B 1 9 ? 16.980 112.044 19.976 1.00 107.64 ? 6 GLU B O 1 +ATOM 2399 C CB . GLU B 1 9 ? 18.782 113.872 21.515 1.00 143.01 ? 6 GLU B CB 1 +ATOM 2400 C CG . GLU B 1 9 ? 18.894 115.137 22.347 1.00 173.21 ? 6 GLU B CG 1 +ATOM 2401 C CD . GLU B 1 9 ? 19.910 116.121 21.785 1.00 186.14 ? 6 GLU B CD 1 +ATOM 2402 O OE1 . GLU B 1 9 ? 20.662 115.746 20.857 1.00 171.86 ? 6 GLU B OE1 1 +ATOM 2403 O OE2 . GLU B 1 9 ? 19.961 117.270 22.275 1.00 198.01 ? 6 GLU B OE2 1 +ATOM 2404 N N . LEU B 1 10 ? 18.048 110.543 21.276 1.00 97.60 ? 7 LEU B N 1 +ATOM 2405 C CA . LEU B 1 10 ? 17.853 109.417 20.366 1.00 91.74 ? 7 LEU B CA 1 +ATOM 2406 C C . LEU B 1 10 ? 16.542 108.682 20.644 1.00 108.49 ? 7 LEU B C 1 +ATOM 2407 O O . LEU B 1 10 ? 16.100 107.847 19.850 1.00 88.11 ? 7 LEU B O 1 +ATOM 2408 C CB . LEU B 1 10 ? 19.021 108.437 20.490 1.00 85.30 ? 7 LEU B CB 1 +ATOM 2409 C CG . LEU B 1 10 ? 20.410 108.998 20.195 1.00 106.77 ? 7 LEU B CG 1 +ATOM 2410 C CD1 . LEU B 1 10 ? 21.494 108.128 20.805 1.00 104.33 ? 7 LEU B CD1 1 +ATOM 2411 C CD2 . LEU B 1 10 ? 20.613 109.128 18.701 1.00 105.23 ? 7 LEU B CD2 1 +ATOM 2412 N N . PHE B 1 11 ? 15.918 109.004 21.771 1.00 114.85 ? 8 PHE B N 1 +ATOM 2413 C CA . PHE B 1 11 ? 14.776 108.233 22.243 1.00 98.50 ? 8 PHE B CA 1 +ATOM 2414 C C . PHE B 1 11 ? 13.458 108.991 22.255 1.00 94.37 ? 8 PHE B C 1 +ATOM 2415 O O . PHE B 1 11 ? 12.443 108.463 22.716 1.00 91.28 ? 8 PHE B O 1 +ATOM 2416 C CB . PHE B 1 11 ? 15.076 107.624 23.609 1.00 100.41 ? 8 PHE B CB 1 +ATOM 2417 C CG . PHE B 1 11 ? 16.016 106.453 23.548 1.00 109.51 ? 8 PHE B CG 1 +ATOM 2418 C CD1 . PHE B 1 11 ? 15.529 105.172 23.360 1.00 91.14 ? 8 PHE B CD1 1 +ATOM 2419 C CD2 . PHE B 1 11 ? 17.383 106.634 23.665 1.00 92.44 ? 8 PHE B CD2 1 +ATOM 2420 C CE1 . PHE B 1 11 ? 16.376 104.105 23.307 1.00 98.87 ? 8 PHE B CE1 1 +ATOM 2421 C CE2 . PHE B 1 11 ? 18.239 105.559 23.607 1.00 101.41 ? 8 PHE B CE2 1 +ATOM 2422 C CZ . PHE B 1 11 ? 17.736 104.296 23.430 1.00 103.58 ? 8 PHE B CZ 1 +ATOM 2423 N N . THR B 1 12 ? 13.484 110.222 21.750 1.00 106.51 ? 9 THR B N 1 +ATOM 2424 C CA . THR B 1 12 ? 12.264 110.890 21.310 1.00 109.27 ? 9 THR B CA 1 +ATOM 2425 C C . THR B 1 12 ? 11.766 110.106 20.099 1.00 122.02 ? 9 THR B C 1 +ATOM 2426 O O . THR B 1 12 ? 12.567 109.594 19.315 1.00 131.66 ? 9 THR B O 1 +ATOM 2427 C CB . THR B 1 12 ? 12.522 112.354 20.887 1.00 60.03 ? 9 THR B CB 1 +ATOM 2428 O OG1 . THR B 1 12 ? 13.144 112.382 19.596 1.00 105.01 ? 9 THR B OG1 1 +ATOM 2429 C CG2 . THR B 1 12 ? 13.426 113.048 21.874 1.00 66.50 ? 9 THR B CG2 1 +ATOM 2430 N N . GLY B 1 13 ? 10.452 109.978 19.952 1.00 76.67 ? 10 GLY B N 1 +ATOM 2431 C CA . GLY B 1 13 ? 9.903 109.288 18.796 1.00 131.03 ? 10 GLY B CA 1 +ATOM 2432 C C . GLY B 1 13 ? 10.118 107.784 18.786 1.00 76.99 ? 10 GLY B C 1 +ATOM 2433 O O . GLY B 1 13 ? 10.930 107.258 19.539 1.00 86.52 ? 10 GLY B O 1 +ATOM 2434 N N . VAL B 1 14 ? 9.388 107.094 17.915 1.00 80.81 ? 11 VAL B N 1 +ATOM 2435 C CA . VAL B 1 14 ? 9.393 105.631 17.859 1.00 73.71 ? 11 VAL B CA 1 +ATOM 2436 C C . VAL B 1 14 ? 10.688 105.052 17.263 1.00 72.93 ? 11 VAL B C 1 +ATOM 2437 O O . VAL B 1 14 ? 11.072 105.373 16.136 1.00 86.63 ? 11 VAL B O 1 +ATOM 2438 C CB . VAL B 1 14 ? 8.157 105.100 17.085 1.00 63.76 ? 11 VAL B CB 1 +ATOM 2439 C CG1 . VAL B 1 14 ? 8.149 103.597 17.066 1.00 105.83 ? 11 VAL B CG1 1 +ATOM 2440 C CG2 . VAL B 1 14 ? 6.872 105.620 17.705 1.00 73.23 ? 11 VAL B CG2 1 +ATOM 2441 N N . VAL B 1 15 ? 11.350 104.197 18.042 1.00 76.44 ? 12 VAL B N 1 +ATOM 2442 C CA . VAL B 1 15 ? 12.612 103.569 17.653 1.00 90.16 ? 12 VAL B CA 1 +ATOM 2443 C C . VAL B 1 15 ? 12.409 102.104 17.315 1.00 94.24 ? 12 VAL B C 1 +ATOM 2444 O O . VAL B 1 15 ? 11.779 101.376 18.085 1.00 88.49 ? 12 VAL B O 1 +ATOM 2445 C CB . VAL B 1 15 ? 13.630 103.595 18.802 1.00 76.90 ? 12 VAL B CB 1 +ATOM 2446 C CG1 . VAL B 1 15 ? 14.918 102.901 18.380 1.00 74.17 ? 12 VAL B CG1 1 +ATOM 2447 C CG2 . VAL B 1 15 ? 13.902 105.017 19.252 1.00 79.58 ? 12 VAL B CG2 1 +ATOM 2448 N N . PRO B 1 16 ? 12.949 101.659 16.171 1.00 77.89 ? 13 PRO B N 1 +ATOM 2449 C CA . PRO B 1 16 ? 12.874 100.227 15.865 1.00 101.92 ? 13 PRO B CA 1 +ATOM 2450 C C . PRO B 1 16 ? 13.802 99.372 16.762 1.00 68.19 ? 13 PRO B C 1 +ATOM 2451 O O . PRO B 1 16 ? 14.917 99.783 17.091 1.00 90.90 ? 13 PRO B O 1 +ATOM 2452 C CB . PRO B 1 16 ? 13.244 100.163 14.372 1.00 64.38 ? 13 PRO B CB 1 +ATOM 2453 C CG . PRO B 1 16 ? 14.038 101.392 14.119 1.00 85.12 ? 13 PRO B CG 1 +ATOM 2454 C CD . PRO B 1 16 ? 13.568 102.441 15.083 1.00 77.58 ? 13 PRO B CD 1 +ATOM 2455 N N . ILE B 1 17 ? 13.309 98.203 17.179 1.00 89.36 ? 14 ILE B N 1 +ATOM 2456 C CA . ILE B 1 17 ? 14.045 97.306 18.077 1.00 84.73 ? 14 ILE B CA 1 +ATOM 2457 C C . ILE B 1 17 ? 14.250 95.937 17.453 1.00 77.46 ? 14 ILE B C 1 +ATOM 2458 O O . ILE B 1 17 ? 13.348 95.384 16.819 1.00 76.69 ? 14 ILE B O 1 +ATOM 2459 C CB . ILE B 1 17 ? 13.308 97.081 19.416 1.00 73.30 ? 14 ILE B CB 1 +ATOM 2460 C CG1 . ILE B 1 17 ? 13.100 98.388 20.159 1.00 76.25 ? 14 ILE B CG1 1 +ATOM 2461 C CG2 . ILE B 1 17 ? 14.087 96.155 20.329 1.00 63.89 ? 14 ILE B CG2 1 +ATOM 2462 C CD1 . ILE B 1 17 ? 12.304 98.191 21.417 1.00 102.69 ? 14 ILE B CD1 1 +ATOM 2463 N N . LEU B 1 18 ? 15.441 95.390 17.662 1.00 73.55 ? 15 LEU B N 1 +ATOM 2464 C CA . LEU B 1 18 ? 15.797 94.076 17.164 1.00 94.19 ? 15 LEU B CA 1 +ATOM 2465 C C . LEU B 1 18 ? 16.434 93.270 18.303 1.00 87.70 ? 15 LEU B C 1 +ATOM 2466 O O . LEU B 1 18 ? 17.316 93.772 18.995 1.00 77.62 ? 15 LEU B O 1 +ATOM 2467 C CB . LEU B 1 18 ? 16.769 94.251 16.002 1.00 71.34 ? 15 LEU B CB 1 +ATOM 2468 C CG . LEU B 1 18 ? 17.360 93.023 15.332 1.00 114.46 ? 15 LEU B CG 1 +ATOM 2469 C CD1 . LEU B 1 18 ? 16.254 92.199 14.689 1.00 112.47 ? 15 LEU B CD1 1 +ATOM 2470 C CD2 . LEU B 1 18 ? 18.402 93.464 14.309 1.00 122.00 ? 15 LEU B CD2 1 +ATOM 2471 N N . VAL B 1 19 ? 15.982 92.031 18.507 1.00 83.59 ? 16 VAL B N 1 +ATOM 2472 C CA . VAL B 1 19 ? 16.486 91.192 19.605 1.00 83.51 ? 16 VAL B CA 1 +ATOM 2473 C C . VAL B 1 19 ? 16.945 89.779 19.183 1.00 92.35 ? 16 VAL B C 1 +ATOM 2474 O O . VAL B 1 19 ? 16.171 89.020 18.580 1.00 84.75 ? 16 VAL B O 1 +ATOM 2475 C CB . VAL B 1 19 ? 15.434 91.063 20.726 1.00 73.98 ? 16 VAL B CB 1 +ATOM 2476 C CG1 . VAL B 1 19 ? 15.866 90.037 21.753 1.00 70.42 ? 16 VAL B CG1 1 +ATOM 2477 C CG2 . VAL B 1 19 ? 15.199 92.407 21.384 1.00 87.75 ? 16 VAL B CG2 1 +ATOM 2478 N N . GLU B 1 20 ? 18.200 89.445 19.521 1.00 83.71 ? 17 GLU B N 1 +ATOM 2479 C CA . GLU B 1 20 ? 18.812 88.125 19.251 1.00 61.65 ? 17 GLU B CA 1 +ATOM 2480 C C . GLU B 1 20 ? 19.265 87.361 20.518 1.00 94.35 ? 17 GLU B C 1 +ATOM 2481 O O . GLU B 1 20 ? 20.091 87.860 21.293 1.00 92.27 ? 17 GLU B O 1 +ATOM 2482 C CB . GLU B 1 20 ? 20.025 88.267 18.314 1.00 89.92 ? 17 GLU B CB 1 +ATOM 2483 C CG . GLU B 1 20 ? 19.755 88.897 16.948 1.00 110.15 ? 17 GLU B CG 1 +ATOM 2484 C CD . GLU B 1 20 ? 18.846 88.059 16.059 1.00 129.72 ? 17 GLU B CD 1 +ATOM 2485 O OE1 . GLU B 1 20 ? 18.601 86.875 16.385 1.00 135.67 ? 17 GLU B OE1 1 +ATOM 2486 O OE2 . GLU B 1 20 ? 18.376 88.595 15.030 1.00 130.10 ? 17 GLU B OE2 1 +ATOM 2487 N N . LEU B 1 21 ? 18.758 86.141 20.712 1.00 76.17 ? 18 LEU B N 1 +ATOM 2488 C CA . LEU B 1 21 ? 19.158 85.318 21.864 1.00 72.26 ? 18 LEU B CA 1 +ATOM 2489 C C . LEU B 1 21 ? 19.653 83.900 21.510 1.00 86.63 ? 18 LEU B C 1 +ATOM 2490 O O . LEU B 1 21 ? 19.052 83.215 20.680 1.00 107.08 ? 18 LEU B O 1 +ATOM 2491 C CB . LEU B 1 21 ? 18.011 85.238 22.877 1.00 96.05 ? 18 LEU B CB 1 +ATOM 2492 C CG . LEU B 1 21 ? 18.209 84.364 24.121 1.00 67.27 ? 18 LEU B CG 1 +ATOM 2493 C CD1 . LEU B 1 21 ? 19.336 84.869 24.956 1.00 125.27 ? 18 LEU B CD1 1 +ATOM 2494 C CD2 . LEU B 1 21 ? 16.943 84.282 24.957 1.00 98.65 ? 18 LEU B CD2 1 +ATOM 2495 N N . ASP B 1 22 ? 20.753 83.483 22.149 1.00 84.50 ? 19 ASP B N 1 +ATOM 2496 C CA . ASP B 1 22 ? 21.292 82.112 22.069 1.00 104.49 ? 19 ASP B CA 1 +ATOM 2497 C C . ASP B 1 22 ? 21.274 81.422 23.445 1.00 105.09 ? 19 ASP B C 1 +ATOM 2498 O O . ASP B 1 22 ? 21.961 81.853 24.371 1.00 96.37 ? 19 ASP B O 1 +ATOM 2499 C CB . ASP B 1 22 ? 22.736 82.119 21.549 1.00 95.05 ? 19 ASP B CB 1 +ATOM 2500 C CG . ASP B 1 22 ? 22.831 82.278 20.038 1.00 126.45 ? 19 ASP B CG 1 +ATOM 2501 O OD1 . ASP B 1 22 ? 21.897 81.862 19.314 1.00 135.11 ? 19 ASP B OD1 1 +ATOM 2502 O OD2 . ASP B 1 22 ? 23.864 82.811 19.576 1.00 159.23 ? 19 ASP B OD2 1 +ATOM 2503 N N . GLY B 1 23 ? 20.511 80.341 23.581 1.00 101.37 ? 20 GLY B N 1 +ATOM 2504 C CA . GLY B 1 23 ? 20.305 79.745 24.890 1.00 55.98 ? 20 GLY B CA 1 +ATOM 2505 C C . GLY B 1 23 ? 20.745 78.304 25.075 1.00 105.17 ? 20 GLY B C 1 +ATOM 2506 O O . GLY B 1 23 ? 20.866 77.546 24.116 1.00 107.72 ? 20 GLY B O 1 +ATOM 2507 N N . ASP B 1 24 ? 20.972 77.942 26.337 1.00 117.82 ? 21 ASP B N 1 +ATOM 2508 C CA . ASP B 1 24 ? 21.381 76.599 26.744 1.00 79.58 ? 21 ASP B CA 1 +ATOM 2509 C C . ASP B 1 24 ? 20.843 76.315 28.164 1.00 93.87 ? 21 ASP B C 1 +ATOM 2510 O O . ASP B 1 24 ? 21.384 76.823 29.147 1.00 99.59 ? 21 ASP B O 1 +ATOM 2511 C CB . ASP B 1 24 ? 22.915 76.491 26.707 1.00 148.33 ? 21 ASP B CB 1 +ATOM 2512 C CG . ASP B 1 24 ? 23.419 75.045 26.624 1.00 160.12 ? 21 ASP B CG 1 +ATOM 2513 O OD1 . ASP B 1 24 ? 22.664 74.113 26.977 1.00 141.71 ? 21 ASP B OD1 1 +ATOM 2514 O OD2 . ASP B 1 24 ? 24.589 74.846 26.213 1.00 112.70 ? 21 ASP B OD2 1 +ATOM 2515 N N . VAL B 1 25 ? 19.774 75.524 28.269 1.00 94.53 ? 22 VAL B N 1 +ATOM 2516 C CA . VAL B 1 25 ? 19.150 75.227 29.571 1.00 99.95 ? 22 VAL B CA 1 +ATOM 2517 C C . VAL B 1 25 ? 19.077 73.718 29.836 1.00 99.72 ? 22 VAL B C 1 +ATOM 2518 O O . VAL B 1 25 ? 18.222 73.015 29.285 1.00 75.50 ? 22 VAL B O 1 +ATOM 2519 C CB . VAL B 1 25 ? 17.755 75.923 29.730 1.00 74.05 ? 22 VAL B CB 1 +ATOM 2520 C CG1 . VAL B 1 25 ? 16.947 75.339 30.884 1.00 80.30 ? 22 VAL B CG1 1 +ATOM 2521 C CG2 . VAL B 1 25 ? 17.937 77.404 29.946 1.00 102.45 ? 22 VAL B CG2 1 +ATOM 2522 N N . ASN B 1 26 ? 19.990 73.244 30.685 1.00 91.36 ? 23 ASN B N 1 +ATOM 2523 C CA . ASN B 1 26 ? 20.174 71.816 30.958 1.00 88.01 ? 23 ASN B CA 1 +ATOM 2524 C C . ASN B 1 26 ? 20.550 71.079 29.665 1.00 117.29 ? 23 ASN B C 1 +ATOM 2525 O O . ASN B 1 26 ? 19.961 70.048 29.316 1.00 82.19 ? 23 ASN B O 1 +ATOM 2526 C CB . ASN B 1 26 ? 18.926 71.191 31.609 1.00 81.63 ? 23 ASN B CB 1 +ATOM 2527 C CG . ASN B 1 26 ? 18.808 71.475 33.119 1.00 118.21 ? 23 ASN B CG 1 +ATOM 2528 O OD1 . ASN B 1 26 ? 19.494 72.334 33.687 1.00 89.81 ? 23 ASN B OD1 1 +ATOM 2529 N ND2 . ASN B 1 26 ? 17.912 70.741 33.770 1.00 96.90 ? 23 ASN B ND2 1 +ATOM 2530 N N . GLY B 1 27 ? 21.527 71.635 28.952 1.00 97.87 ? 24 GLY B N 1 +ATOM 2531 C CA . GLY B 1 27 ? 21.952 71.110 27.668 1.00 92.50 ? 24 GLY B CA 1 +ATOM 2532 C C . GLY B 1 27 ? 20.920 71.176 26.549 1.00 107.17 ? 24 GLY B C 1 +ATOM 2533 O O . GLY B 1 27 ? 21.124 70.565 25.493 1.00 103.81 ? 24 GLY B O 1 +ATOM 2534 N N . HIS B 1 28 ? 19.808 71.878 26.785 1.00 103.83 ? 25 HIS B N 1 +ATOM 2535 C CA . HIS B 1 28 ? 18.859 72.215 25.720 1.00 108.38 ? 25 HIS B CA 1 +ATOM 2536 C C . HIS B 1 28 ? 19.236 73.545 25.138 1.00 110.47 ? 25 HIS B C 1 +ATOM 2537 O O . HIS B 1 28 ? 19.219 74.566 25.829 1.00 74.52 ? 25 HIS B O 1 +ATOM 2538 C CB . HIS B 1 28 ? 17.436 72.355 26.233 1.00 69.04 ? 25 HIS B CB 1 +ATOM 2539 C CG . HIS B 1 28 ? 16.825 71.069 26.667 1.00 133.31 ? 25 HIS B CG 1 +ATOM 2540 N ND1 . HIS B 1 28 ? 17.116 70.485 27.880 1.00 117.70 ? 25 HIS B ND1 1 +ATOM 2541 C CD2 . HIS B 1 28 ? 15.935 70.252 26.056 1.00 127.86 ? 25 HIS B CD2 1 +ATOM 2542 C CE1 . HIS B 1 28 ? 16.431 69.363 27.999 1.00 101.92 ? 25 HIS B CE1 1 +ATOM 2543 N NE2 . HIS B 1 28 ? 15.706 69.198 26.907 1.00 138.74 ? 25 HIS B NE2 1 +ATOM 2544 N N . LYS B 1 29 ? 19.572 73.530 23.860 1.00 82.30 ? 26 LYS B N 1 +ATOM 2545 C CA . LYS B 1 29 ? 19.962 74.742 23.188 1.00 85.47 ? 26 LYS B CA 1 +ATOM 2546 C C . LYS B 1 29 ? 18.719 75.273 22.490 1.00 100.65 ? 26 LYS B C 1 +ATOM 2547 O O . LYS B 1 29 ? 17.741 74.539 22.332 1.00 103.36 ? 26 LYS B O 1 +ATOM 2548 C CB . LYS B 1 29 ? 21.110 74.463 22.214 1.00 96.24 ? 26 LYS B CB 1 +ATOM 2549 C CG . LYS B 1 29 ? 22.399 73.955 22.881 1.00 70.53 ? 26 LYS B CG 1 +ATOM 2550 C CD . LYS B 1 29 ? 23.490 73.702 21.844 1.00 113.45 ? 26 LYS B CD 1 +ATOM 2551 C CE . LYS B 1 29 ? 24.850 73.404 22.475 1.00 107.26 ? 26 LYS B CE 1 +ATOM 2552 N NZ . LYS B 1 29 ? 25.487 74.582 23.132 1.00 132.29 ? 26 LYS B NZ 1 +ATOM 2553 N N . PHE B 1 30 ? 18.745 76.555 22.128 1.00 88.32 ? 27 PHE B N 1 +ATOM 2554 C CA . PHE B 1 30 ? 17.648 77.206 21.405 1.00 86.50 ? 27 PHE B CA 1 +ATOM 2555 C C . PHE B 1 30 ? 18.032 78.625 21.014 1.00 89.72 ? 27 PHE B C 1 +ATOM 2556 O O . PHE B 1 30 ? 18.947 79.217 21.589 1.00 90.44 ? 27 PHE B O 1 +ATOM 2557 C CB . PHE B 1 30 ? 16.345 77.234 22.222 1.00 100.34 ? 27 PHE B CB 1 +ATOM 2558 C CG . PHE B 1 30 ? 16.454 77.984 23.529 1.00 97.73 ? 27 PHE B CG 1 +ATOM 2559 C CD1 . PHE B 1 30 ? 16.890 77.345 24.671 1.00 96.84 ? 27 PHE B CD1 1 +ATOM 2560 C CD2 . PHE B 1 30 ? 16.129 79.324 23.613 1.00 88.24 ? 27 PHE B CD2 1 +ATOM 2561 C CE1 . PHE B 1 30 ? 16.988 78.015 25.869 1.00 97.63 ? 27 PHE B CE1 1 +ATOM 2562 C CE2 . PHE B 1 30 ? 16.237 80.003 24.814 1.00 88.10 ? 27 PHE B CE2 1 +ATOM 2563 C CZ . PHE B 1 30 ? 16.668 79.345 25.941 1.00 85.30 ? 27 PHE B CZ 1 +ATOM 2564 N N . SER B 1 31 ? 17.321 79.164 20.032 1.00 83.96 ? 28 SER B N 1 +ATOM 2565 C CA . SER B 1 31 ? 17.527 80.538 19.598 1.00 80.23 ? 28 SER B CA 1 +ATOM 2566 C C . SER B 1 31 ? 16.204 81.280 19.399 1.00 91.64 ? 28 SER B C 1 +ATOM 2567 O O . SER B 1 31 ? 15.178 80.685 19.031 1.00 84.21 ? 28 SER B O 1 +ATOM 2568 C CB . SER B 1 31 ? 18.385 80.584 18.335 1.00 83.90 ? 28 SER B CB 1 +ATOM 2569 O OG . SER B 1 31 ? 19.691 80.104 18.601 1.00 116.17 ? 28 SER B OG 1 +ATOM 2570 N N . VAL B 1 32 ? 16.243 82.584 19.682 1.00 84.01 ? 29 VAL B N 1 +ATOM 2571 C CA . VAL B 1 32 ? 15.083 83.471 19.574 1.00 82.13 ? 29 VAL B CA 1 +ATOM 2572 C C . VAL B 1 32 ? 15.434 84.803 18.896 1.00 73.39 ? 29 VAL B C 1 +ATOM 2573 O O . VAL B 1 32 ? 16.417 85.468 19.258 1.00 70.81 ? 29 VAL B O 1 +ATOM 2574 C CB . VAL B 1 32 ? 14.451 83.782 20.960 1.00 89.38 ? 29 VAL B CB 1 +ATOM 2575 C CG1 . VAL B 1 32 ? 13.164 84.577 20.793 1.00 86.82 ? 29 VAL B CG1 1 +ATOM 2576 C CG2 . VAL B 1 32 ? 14.166 82.510 21.732 1.00 52.44 ? 29 VAL B CG2 1 +ATOM 2577 N N . SER B 1 33 ? 14.631 85.169 17.898 1.00 78.42 ? 30 SER B N 1 +ATOM 2578 C CA . SER B 1 33 ? 14.676 86.500 17.287 1.00 97.25 ? 30 SER B CA 1 +ATOM 2579 C C . SER B 1 33 ? 13.403 87.294 17.573 1.00 101.23 ? 30 SER B C 1 +ATOM 2580 O O . SER B 1 33 ? 12.279 86.787 17.437 1.00 78.54 ? 30 SER B O 1 +ATOM 2581 C CB . SER B 1 33 ? 14.898 86.423 15.777 1.00 74.72 ? 30 SER B CB 1 +ATOM 2582 O OG . SER B 1 33 ? 16.203 85.971 15.480 1.00 118.18 ? 30 SER B OG 1 +ATOM 2583 N N . GLY B 1 34 ? 13.593 88.544 17.976 1.00 100.01 ? 31 GLY B N 1 +ATOM 2584 C CA . GLY B 1 34 ? 12.485 89.429 18.249 1.00 60.15 ? 31 GLY B CA 1 +ATOM 2585 C C . GLY B 1 34 ? 12.624 90.748 17.523 1.00 84.87 ? 31 GLY B C 1 +ATOM 2586 O O . GLY B 1 34 ? 13.709 91.328 17.487 1.00 80.41 ? 31 GLY B O 1 +ATOM 2587 N N . GLU B 1 35 ? 11.526 91.211 16.928 1.00 67.37 ? 32 GLU B N 1 +ATOM 2588 C CA . GLU B 1 35 ? 11.460 92.568 16.389 1.00 88.48 ? 32 GLU B CA 1 +ATOM 2589 C C . GLU B 1 35 ? 10.244 93.342 16.911 1.00 86.70 ? 32 GLU B C 1 +ATOM 2590 O O . GLU B 1 35 ? 9.175 92.775 17.153 1.00 86.40 ? 32 GLU B O 1 +ATOM 2591 C CB . GLU B 1 35 ? 11.481 92.569 14.853 1.00 78.77 ? 32 GLU B CB 1 +ATOM 2592 C CG . GLU B 1 35 ? 10.245 91.973 14.179 1.00 87.69 ? 32 GLU B CG 1 +ATOM 2593 C CD . GLU B 1 35 ? 10.547 91.374 12.799 1.00 168.35 ? 32 GLU B CD 1 +ATOM 2594 O OE1 . GLU B 1 35 ? 11.481 91.845 12.124 1.00 170.63 ? 32 GLU B OE1 1 +ATOM 2595 O OE2 . GLU B 1 35 ? 9.857 90.418 12.391 1.00 206.83 ? 32 GLU B OE2 1 +ATOM 2596 N N . GLY B 1 36 ? 10.431 94.644 17.091 1.00 107.15 ? 33 GLY B N 1 +ATOM 2597 C CA . GLY B 1 36 ? 9.340 95.547 17.405 1.00 79.00 ? 33 GLY B CA 1 +ATOM 2598 C C . GLY B 1 36 ? 9.834 96.978 17.435 1.00 71.84 ? 33 GLY B C 1 +ATOM 2599 O O . GLY B 1 36 ? 10.763 97.328 16.711 1.00 78.21 ? 33 GLY B O 1 +ATOM 2600 N N . GLU B 1 37 ? 9.221 97.792 18.291 1.00 88.45 ? 34 GLU B N 1 +ATOM 2601 C CA . GLU B 1 37 ? 9.533 99.214 18.399 1.00 84.74 ? 34 GLU B CA 1 +ATOM 2602 C C . GLU B 1 37 ? 9.276 99.723 19.814 1.00 75.76 ? 34 GLU B C 1 +ATOM 2603 O O . GLU B 1 37 ? 8.485 99.140 20.561 1.00 88.68 ? 34 GLU B O 1 +ATOM 2604 C CB . GLU B 1 37 ? 8.685 100.009 17.414 1.00 73.80 ? 34 GLU B CB 1 +ATOM 2605 C CG . GLU B 1 37 ? 7.201 99.890 17.711 1.00 142.22 ? 34 GLU B CG 1 +ATOM 2606 C CD . GLU B 1 37 ? 6.334 100.565 16.682 1.00 140.65 ? 34 GLU B CD 1 +ATOM 2607 O OE1 . GLU B 1 37 ? 6.852 101.404 15.921 1.00 141.52 ? 34 GLU B OE1 1 +ATOM 2608 O OE2 . GLU B 1 37 ? 5.129 100.239 16.633 1.00 139.05 ? 34 GLU B OE2 1 +ATOM 2609 N N . GLY B 1 38 ? 9.942 100.819 20.169 1.00 82.94 ? 35 GLY B N 1 +ATOM 2610 C CA . GLY B 1 38 ? 9.861 101.372 21.510 1.00 90.07 ? 35 GLY B CA 1 +ATOM 2611 C C . GLY B 1 38 ? 9.627 102.870 21.556 1.00 89.52 ? 35 GLY B C 1 +ATOM 2612 O O . GLY B 1 38 ? 10.180 103.625 20.760 1.00 89.55 ? 35 GLY B O 1 +ATOM 2613 N N . ASP B 1 39 ? 8.801 103.298 22.505 1.00 89.73 ? 36 ASP B N 1 +ATOM 2614 C CA . ASP B 1 39 ? 8.434 104.702 22.651 1.00 89.25 ? 36 ASP B CA 1 +ATOM 2615 C C . ASP B 1 39 ? 8.730 105.182 24.071 1.00 65.02 ? 36 ASP B C 1 +ATOM 2616 O O . ASP B 1 39 ? 7.896 105.045 24.963 1.00 82.69 ? 36 ASP B O 1 +ATOM 2617 C CB . ASP B 1 39 ? 6.946 104.880 22.342 1.00 81.82 ? 36 ASP B CB 1 +ATOM 2618 C CG . ASP B 1 39 ? 6.675 106.061 21.433 1.00 123.62 ? 36 ASP B CG 1 +ATOM 2619 O OD1 . ASP B 1 39 ? 7.517 106.985 21.409 1.00 122.30 ? 36 ASP B OD1 1 +ATOM 2620 O OD2 . ASP B 1 39 ? 5.622 106.062 20.750 1.00 106.76 ? 36 ASP B OD2 1 +ATOM 2621 N N . ALA B 1 40 ? 9.915 105.742 24.285 1.00 94.64 ? 37 ALA B N 1 +ATOM 2622 C CA . ALA B 1 40 ? 10.322 106.147 25.630 1.00 74.21 ? 37 ALA B CA 1 +ATOM 2623 C C . ALA B 1 40 ? 9.496 107.312 26.152 1.00 64.78 ? 37 ALA B C 1 +ATOM 2624 O O . ALA B 1 40 ? 9.353 107.481 27.356 1.00 94.99 ? 37 ALA B O 1 +ATOM 2625 C CB . ALA B 1 40 ? 11.794 106.496 25.660 1.00 60.76 ? 37 ALA B CB 1 +ATOM 2626 N N . THR B 1 41 ? 8.966 108.111 25.233 1.00 95.70 ? 38 THR B N 1 +ATOM 2627 C CA . THR B 1 41 ? 8.159 109.275 25.561 1.00 64.81 ? 38 THR B CA 1 +ATOM 2628 C C . THR B 1 41 ? 6.960 108.891 26.416 1.00 86.52 ? 38 THR B C 1 +ATOM 2629 O O . THR B 1 41 ? 6.633 109.592 27.369 1.00 87.39 ? 38 THR B O 1 +ATOM 2630 C CB . THR B 1 41 ? 7.653 109.958 24.288 1.00 85.04 ? 38 THR B CB 1 +ATOM 2631 O OG1 . THR B 1 41 ? 8.757 110.244 23.420 1.00 97.50 ? 38 THR B OG1 1 +ATOM 2632 C CG2 . THR B 1 41 ? 6.953 111.232 24.631 1.00 45.47 ? 38 THR B CG2 1 +ATOM 2633 N N . TYR B 1 42 ? 6.312 107.779 26.070 1.00 75.31 ? 39 TYR B N 1 +ATOM 2634 C CA . TYR B 1 42 ? 5.189 107.262 26.853 1.00 88.73 ? 39 TYR B CA 1 +ATOM 2635 C C . TYR B 1 42 ? 5.489 105.877 27.396 1.00 68.99 ? 39 TYR B C 1 +ATOM 2636 O O . TYR B 1 42 ? 4.578 105.061 27.567 1.00 79.97 ? 39 TYR B O 1 +ATOM 2637 C CB . TYR B 1 42 ? 3.909 107.218 26.023 1.00 63.27 ? 39 TYR B CB 1 +ATOM 2638 C CG . TYR B 1 42 ? 3.786 108.389 25.103 1.00 75.46 ? 39 TYR B CG 1 +ATOM 2639 C CD1 . TYR B 1 42 ? 3.203 109.579 25.529 1.00 79.86 ? 39 TYR B CD1 1 +ATOM 2640 C CD2 . TYR B 1 42 ? 4.276 108.317 23.805 1.00 89.04 ? 39 TYR B CD2 1 +ATOM 2641 C CE1 . TYR B 1 42 ? 3.104 110.667 24.675 1.00 84.82 ? 39 TYR B CE1 1 +ATOM 2642 C CE2 . TYR B 1 42 ? 4.185 109.387 22.949 1.00 108.10 ? 39 TYR B CE2 1 +ATOM 2643 C CZ . TYR B 1 42 ? 3.600 110.561 23.383 1.00 103.77 ? 39 TYR B CZ 1 +ATOM 2644 O OH . TYR B 1 42 ? 3.525 111.621 22.507 1.00 84.65 ? 39 TYR B OH 1 +ATOM 2645 N N . GLY B 1 43 ? 6.773 105.630 27.649 1.00 75.59 ? 40 GLY B N 1 +ATOM 2646 C CA . GLY B 1 43 ? 7.259 104.410 28.282 1.00 80.94 ? 40 GLY B CA 1 +ATOM 2647 C C . GLY B 1 43 ? 6.680 103.109 27.753 1.00 90.27 ? 40 GLY B C 1 +ATOM 2648 O O . GLY B 1 43 ? 6.208 102.266 28.522 1.00 68.75 ? 40 GLY B O 1 +ATOM 2649 N N . LYS B 1 44 ? 6.745 102.934 26.439 1.00 75.63 ? 41 LYS B N 1 +ATOM 2650 C CA . LYS B 1 44 ? 5.960 101.912 25.765 1.00 56.72 ? 41 LYS B CA 1 +ATOM 2651 C C . LYS B 1 44 ? 6.814 100.959 24.921 1.00 89.17 ? 41 LYS B C 1 +ATOM 2652 O O . LYS B 1 44 ? 7.766 101.372 24.256 1.00 90.41 ? 41 LYS B O 1 +ATOM 2653 C CB . LYS B 1 44 ? 4.909 102.596 24.904 1.00 69.75 ? 41 LYS B CB 1 +ATOM 2654 C CG . LYS B 1 44 ? 3.805 101.695 24.501 1.00 90.79 ? 41 LYS B CG 1 +ATOM 2655 C CD . LYS B 1 44 ? 2.962 102.342 23.443 1.00 74.97 ? 41 LYS B CD 1 +ATOM 2656 C CE . LYS B 1 44 ? 2.406 101.278 22.535 1.00 110.53 ? 41 LYS B CE 1 +ATOM 2657 N NZ . LYS B 1 44 ? 1.124 101.677 21.897 1.00 113.17 ? 41 LYS B NZ 1 +ATOM 2658 N N . LEU B 1 45 ? 6.462 99.679 24.952 1.00 103.96 ? 42 LEU B N 1 +ATOM 2659 C CA . LEU B 1 45 ? 7.282 98.645 24.329 1.00 93.28 ? 42 LEU B CA 1 +ATOM 2660 C C . LEU B 1 45 ? 6.413 97.560 23.687 1.00 55.82 ? 42 LEU B C 1 +ATOM 2661 O O . LEU B 1 45 ? 5.536 96.999 24.340 1.00 88.00 ? 42 LEU B O 1 +ATOM 2662 C CB . LEU B 1 45 ? 8.187 98.033 25.393 1.00 71.53 ? 42 LEU B CB 1 +ATOM 2663 C CG . LEU B 1 45 ? 9.501 97.370 25.018 1.00 81.89 ? 42 LEU B CG 1 +ATOM 2664 C CD1 . LEU B 1 45 ? 10.429 98.380 24.408 1.00 122.63 ? 42 LEU B CD1 1 +ATOM 2665 C CD2 . LEU B 1 45 ? 10.106 96.794 26.266 1.00 86.39 ? 42 LEU B CD2 1 +ATOM 2666 N N . THR B 1 46 ? 6.635 97.281 22.407 1.00 75.46 ? 43 THR B N 1 +ATOM 2667 C CA . THR B 1 46 ? 5.903 96.209 21.725 1.00 91.14 ? 43 THR B CA 1 +ATOM 2668 C C . THR B 1 46 ? 6.885 95.324 20.983 1.00 78.56 ? 43 THR B C 1 +ATOM 2669 O O . THR B 1 46 ? 7.615 95.798 20.118 1.00 88.23 ? 43 THR B O 1 +ATOM 2670 C CB . THR B 1 46 ? 4.901 96.733 20.674 1.00 67.66 ? 43 THR B CB 1 +ATOM 2671 O OG1 . THR B 1 46 ? 5.625 97.289 19.579 1.00 116.68 ? 43 THR B OG1 1 +ATOM 2672 C CG2 . THR B 1 46 ? 3.976 97.797 21.250 1.00 84.91 ? 43 THR B CG2 1 +ATOM 2673 N N . LEU B 1 47 ? 6.895 94.037 21.309 1.00 84.61 ? 44 LEU B N 1 +ATOM 2674 C CA . LEU B 1 47 ? 7.868 93.115 20.740 1.00 84.52 ? 44 LEU B CA 1 +ATOM 2675 C C . LEU B 1 47 ? 7.238 91.781 20.382 1.00 77.45 ? 44 LEU B C 1 +ATOM 2676 O O . LEU B 1 47 ? 6.364 91.290 21.102 1.00 67.15 ? 44 LEU B O 1 +ATOM 2677 C CB . LEU B 1 47 ? 9.017 92.901 21.722 1.00 67.05 ? 44 LEU B CB 1 +ATOM 2678 C CG . LEU B 1 47 ? 9.988 94.078 21.853 1.00 93.89 ? 44 LEU B CG 1 +ATOM 2679 C CD1 . LEU B 1 47 ? 10.970 93.848 22.990 1.00 88.06 ? 44 LEU B CD1 1 +ATOM 2680 C CD2 . LEU B 1 47 ? 10.728 94.319 20.546 1.00 78.89 ? 44 LEU B CD2 1 +ATOM 2681 N N . LYS B 1 48 ? 7.673 91.215 19.254 1.00 65.48 ? 45 LYS B N 1 +ATOM 2682 C CA . LYS B 1 48 ? 7.290 89.856 18.858 1.00 55.49 ? 45 LYS B CA 1 +ATOM 2683 C C . LYS B 1 48 ? 8.495 88.936 18.776 1.00 87.25 ? 45 LYS B C 1 +ATOM 2684 O O . LYS B 1 48 ? 9.518 89.285 18.186 1.00 67.77 ? 45 LYS B O 1 +ATOM 2685 C CB . LYS B 1 48 ? 6.570 89.830 17.516 1.00 58.32 ? 45 LYS B CB 1 +ATOM 2686 C CG . LYS B 1 48 ? 5.888 88.507 17.239 1.00 67.56 ? 45 LYS B CG 1 +ATOM 2687 C CD . LYS B 1 48 ? 5.575 88.338 15.771 1.00 74.39 ? 45 LYS B CD 1 +ATOM 2688 C CE . LYS B 1 48 ? 4.531 87.268 15.575 1.00 88.24 ? 45 LYS B CE 1 +ATOM 2689 N NZ . LYS B 1 48 ? 4.436 86.898 14.154 1.00 76.38 ? 45 LYS B NZ 1 +ATOM 2690 N N . PHE B 1 49 ? 8.348 87.751 19.361 1.00 99.77 ? 46 PHE B N 1 +ATOM 2691 C CA . PHE B 1 49 ? 9.430 86.786 19.440 1.00 85.84 ? 46 PHE B CA 1 +ATOM 2692 C C . PHE B 1 49 ? 9.095 85.507 18.696 1.00 63.67 ? 46 PHE B C 1 +ATOM 2693 O O . PHE B 1 49 ? 8.023 84.943 18.857 1.00 84.58 ? 46 PHE B O 1 +ATOM 2694 C CB . PHE B 1 49 ? 9.774 86.517 20.902 1.00 79.80 ? 46 PHE B CB 1 +ATOM 2695 C CG . PHE B 1 49 ? 10.240 87.742 21.629 1.00 73.62 ? 46 PHE B CG 1 +ATOM 2696 C CD1 . PHE B 1 49 ? 11.541 88.188 21.488 1.00 86.37 ? 46 PHE B CD1 1 +ATOM 2697 C CD2 . PHE B 1 49 ? 9.381 88.464 22.419 1.00 77.18 ? 46 PHE B CD2 1 +ATOM 2698 C CE1 . PHE B 1 49 ? 11.976 89.313 22.131 1.00 70.00 ? 46 PHE B CE1 1 +ATOM 2699 C CE2 . PHE B 1 49 ? 9.820 89.591 23.064 1.00 86.96 ? 46 PHE B CE2 1 +ATOM 2700 C CZ . PHE B 1 49 ? 11.119 90.013 22.914 1.00 69.96 ? 46 PHE B CZ 1 +ATOM 2701 N N . ILE B 1 50 ? 10.014 85.092 17.838 1.00 88.42 ? 47 ILE B N 1 +ATOM 2702 C CA . ILE B 1 50 ? 9.905 83.830 17.130 1.00 67.57 ? 47 ILE B CA 1 +ATOM 2703 C C . ILE B 1 50 ? 10.959 82.882 17.703 1.00 98.60 ? 47 ILE B C 1 +ATOM 2704 O O . ILE B 1 50 ? 12.121 83.258 17.884 1.00 83.31 ? 47 ILE B O 1 +ATOM 2705 C CB . ILE B 1 50 ? 10.176 84.008 15.614 1.00 77.48 ? 47 ILE B CB 1 +ATOM 2706 C CG1 . ILE B 1 50 ? 9.279 85.089 14.998 1.00 104.25 ? 47 ILE B CG1 1 +ATOM 2707 C CG2 . ILE B 1 50 ? 9.991 82.696 14.874 1.00 106.58 ? 47 ILE B CG2 1 +ATOM 2708 C CD1 . ILE B 1 50 ? 7.869 84.623 14.686 1.00 114.44 ? 47 ILE B CD1 1 +ATOM 2709 N N . CYS B 1 51 ? 10.566 81.653 18.009 1.00 102.48 ? 48 CYS B N 1 +ATOM 2710 C CA . CYS B 1 51 ? 11.571 80.626 18.242 1.00 105.71 ? 48 CYS B CA 1 +ATOM 2711 C C . CYS B 1 51 ? 12.104 80.100 16.903 1.00 96.92 ? 48 CYS B C 1 +ATOM 2712 O O . CYS B 1 51 ? 11.361 79.476 16.133 1.00 103.20 ? 48 CYS B O 1 +ATOM 2713 C CB . CYS B 1 51 ? 11.008 79.479 19.069 1.00 129.29 ? 48 CYS B CB 1 +ATOM 2714 S SG . CYS B 1 51 ? 12.298 78.465 19.803 1.00 104.01 ? 48 CYS B SG 1 +ATOM 2715 N N . THR B 1 52 ? 13.388 80.355 16.635 1.00 94.84 ? 49 THR B N 1 +ATOM 2716 C CA . THR B 1 52 ? 14.013 79.984 15.360 1.00 95.37 ? 49 THR B CA 1 +ATOM 2717 C C . THR B 1 52 ? 14.479 78.525 15.318 1.00 88.71 ? 49 THR B C 1 +ATOM 2718 O O . THR B 1 52 ? 14.890 78.033 14.267 1.00 92.28 ? 49 THR B O 1 +ATOM 2719 C CB . THR B 1 52 ? 15.217 80.902 15.003 1.00 91.12 ? 49 THR B CB 1 +ATOM 2720 O OG1 . THR B 1 52 ? 16.026 81.118 16.166 1.00 75.40 ? 49 THR B OG1 1 +ATOM 2721 C CG2 . THR B 1 52 ? 14.750 82.243 14.474 1.00 66.22 ? 49 THR B CG2 1 +ATOM 2722 N N . THR B 1 53 ? 14.411 77.839 16.459 1.00 104.34 ? 50 THR B N 1 +ATOM 2723 C CA . THR B 1 53 ? 14.875 76.451 16.568 1.00 67.23 ? 50 THR B CA 1 +ATOM 2724 C C . THR B 1 53 ? 13.756 75.432 16.854 1.00 94.39 ? 50 THR B C 1 +ATOM 2725 O O . THR B 1 53 ? 13.998 74.417 17.498 1.00 135.12 ? 50 THR B O 1 +ATOM 2726 C CB . THR B 1 53 ? 15.962 76.295 17.682 1.00 92.86 ? 50 THR B CB 1 +ATOM 2727 O OG1 . THR B 1 53 ? 15.393 76.562 18.974 1.00 83.84 ? 50 THR B OG1 1 +ATOM 2728 C CG2 . THR B 1 53 ? 17.120 77.233 17.461 1.00 54.60 ? 50 THR B CG2 1 +ATOM 2729 N N . GLY B 1 54 ? 12.540 75.687 16.380 1.00 75.78 ? 51 GLY B N 1 +ATOM 2730 C CA . GLY B 1 54 ? 11.411 74.817 16.692 1.00 93.35 ? 51 GLY B CA 1 +ATOM 2731 C C . GLY B 1 54 ? 10.730 75.247 17.979 1.00 56.36 ? 51 GLY B C 1 +ATOM 2732 O O . GLY B 1 54 ? 10.665 76.440 18.241 1.00 154.25 ? 51 GLY B O 1 +ATOM 2733 N N . LYS B 1 55 ? 10.229 74.299 18.775 1.00 98.95 ? 52 LYS B N 1 +ATOM 2734 C CA . LYS B 1 55 ? 9.666 74.607 20.100 1.00 93.09 ? 52 LYS B CA 1 +ATOM 2735 C C . LYS B 1 55 ? 10.677 75.110 21.109 1.00 85.47 ? 52 LYS B C 1 +ATOM 2736 O O . LYS B 1 55 ? 11.874 74.840 21.008 1.00 90.91 ? 52 LYS B O 1 +ATOM 2737 C CB . LYS B 1 55 ? 8.968 73.402 20.695 1.00 62.98 ? 52 LYS B CB 1 +ATOM 2738 C CG . LYS B 1 55 ? 7.467 73.366 20.375 1.00 123.71 ? 52 LYS B CG 1 +ATOM 2739 C CD . LYS B 1 55 ? 6.710 72.301 21.209 1.00 169.85 ? 52 LYS B CD 1 +ATOM 2740 C CE . LYS B 1 55 ? 5.689 71.596 20.375 1.00 181.38 ? 52 LYS B CE 1 +ATOM 2741 N NZ . LYS B 1 55 ? 5.008 70.481 21.102 1.00 165.45 ? 52 LYS B NZ 1 +ATOM 2742 N N . LEU B 1 56 ? 10.164 75.830 22.100 1.00 94.85 ? 53 LEU B N 1 +ATOM 2743 C CA . LEU B 1 56 ? 10.993 76.380 23.156 1.00 91.30 ? 53 LEU B CA 1 +ATOM 2744 C C . LEU B 1 56 ? 11.133 75.335 24.274 1.00 76.42 ? 53 LEU B C 1 +ATOM 2745 O O . LEU B 1 56 ? 10.159 74.671 24.640 1.00 88.08 ? 53 LEU B O 1 +ATOM 2746 C CB . LEU B 1 56 ? 10.379 77.693 23.666 1.00 82.42 ? 53 LEU B CB 1 +ATOM 2747 C CG . LEU B 1 56 ? 11.289 78.726 24.342 1.00 90.88 ? 53 LEU B CG 1 +ATOM 2748 C CD1 . LEU B 1 56 ? 12.159 79.458 23.340 1.00 77.09 ? 53 LEU B CD1 1 +ATOM 2749 C CD2 . LEU B 1 56 ? 10.457 79.702 25.137 1.00 61.11 ? 53 LEU B CD2 1 +ATOM 2750 N N . PRO B 1 57 ? 12.355 75.154 24.802 1.00 98.74 ? 54 PRO B N 1 +ATOM 2751 C CA . PRO B 1 57 ? 12.513 74.168 25.880 1.00 75.69 ? 54 PRO B CA 1 +ATOM 2752 C C . PRO B 1 57 ? 11.988 74.659 27.232 1.00 89.37 ? 54 PRO B C 1 +ATOM 2753 O O . PRO B 1 57 ? 11.670 73.850 28.097 1.00 90.05 ? 54 PRO B O 1 +ATOM 2754 C CB . PRO B 1 57 ? 14.027 73.969 25.946 1.00 78.48 ? 54 PRO B CB 1 +ATOM 2755 C CG . PRO B 1 57 ? 14.594 75.236 25.450 1.00 82.47 ? 54 PRO B CG 1 +ATOM 2756 C CD . PRO B 1 57 ? 13.644 75.737 24.390 1.00 87.56 ? 54 PRO B CD 1 +ATOM 2757 N N . VAL B 1 58 ? 11.892 75.972 27.396 1.00 86.59 ? 55 VAL B N 1 +ATOM 2758 C CA . VAL B 1 58 ? 11.435 76.584 28.639 1.00 97.95 ? 55 VAL B CA 1 +ATOM 2759 C C . VAL B 1 58 ? 10.083 77.291 28.425 1.00 103.15 ? 55 VAL B C 1 +ATOM 2760 O O . VAL B 1 58 ? 9.649 77.433 27.284 1.00 78.91 ? 55 VAL B O 1 +ATOM 2761 C CB . VAL B 1 58 ? 12.503 77.556 29.128 1.00 80.13 ? 55 VAL B CB 1 +ATOM 2762 C CG1 . VAL B 1 58 ? 13.694 76.781 29.617 1.00 90.39 ? 55 VAL B CG1 1 +ATOM 2763 C CG2 . VAL B 1 58 ? 12.927 78.445 27.996 1.00 90.62 ? 55 VAL B CG2 1 +ATOM 2764 N N . PRO B 1 59 ? 9.393 77.714 29.507 1.00 97.15 ? 56 PRO B N 1 +ATOM 2765 C CA . PRO B 1 59 ? 8.141 78.421 29.222 1.00 99.48 ? 56 PRO B CA 1 +ATOM 2766 C C . PRO B 1 59 ? 8.472 79.837 28.780 1.00 108.23 ? 56 PRO B C 1 +ATOM 2767 O O . PRO B 1 59 ? 9.486 80.389 29.215 1.00 88.37 ? 56 PRO B O 1 +ATOM 2768 C CB . PRO B 1 59 ? 7.426 78.462 30.584 1.00 80.12 ? 56 PRO B CB 1 +ATOM 2769 C CG . PRO B 1 59 ? 8.287 77.728 31.526 1.00 87.77 ? 56 PRO B CG 1 +ATOM 2770 C CD . PRO B 1 59 ? 9.663 77.692 30.951 1.00 83.74 ? 56 PRO B CD 1 +ATOM 2771 N N . TRP B 1 60 ? 7.648 80.413 27.917 1.00 97.54 ? 57 TRP B N 1 +ATOM 2772 C CA . TRP B 1 60 ? 7.892 81.777 27.465 1.00 64.58 ? 57 TRP B CA 1 +ATOM 2773 C C . TRP B 1 60 ? 8.087 82.801 28.600 1.00 73.20 ? 57 TRP B C 1 +ATOM 2774 O O . TRP B 1 60 ? 9.046 83.574 28.554 1.00 65.25 ? 57 TRP B O 1 +ATOM 2775 C CB . TRP B 1 60 ? 6.818 82.229 26.477 1.00 71.08 ? 57 TRP B CB 1 +ATOM 2776 C CG . TRP B 1 60 ? 7.043 81.727 25.097 1.00 80.96 ? 57 TRP B CG 1 +ATOM 2777 C CD1 . TRP B 1 60 ? 6.321 80.778 24.427 1.00 64.04 ? 57 TRP B CD1 1 +ATOM 2778 C CD2 . TRP B 1 60 ? 8.069 82.155 24.210 1.00 82.57 ? 57 TRP B CD2 1 +ATOM 2779 N NE1 . TRP B 1 60 ? 6.841 80.593 23.167 1.00 70.91 ? 57 TRP B NE1 1 +ATOM 2780 C CE2 . TRP B 1 60 ? 7.915 81.431 23.011 1.00 75.64 ? 57 TRP B CE2 1 +ATOM 2781 C CE3 . TRP B 1 60 ? 9.105 83.086 24.311 1.00 80.00 ? 57 TRP B CE3 1 +ATOM 2782 C CZ2 . TRP B 1 60 ? 8.759 81.609 21.927 1.00 67.57 ? 57 TRP B CZ2 1 +ATOM 2783 C CZ3 . TRP B 1 60 ? 9.937 83.263 23.238 1.00 79.43 ? 57 TRP B CZ3 1 +ATOM 2784 C CH2 . TRP B 1 60 ? 9.765 82.527 22.060 1.00 70.69 ? 57 TRP B CH2 1 +ATOM 2785 N N . PRO B 1 61 ? 7.200 82.794 29.624 1.00 84.07 ? 58 PRO B N 1 +ATOM 2786 C CA . PRO B 1 61 ? 7.279 83.748 30.741 1.00 58.47 ? 58 PRO B CA 1 +ATOM 2787 C C . PRO B 1 61 ? 8.655 83.917 31.389 1.00 66.91 ? 58 PRO B C 1 +ATOM 2788 O O . PRO B 1 61 ? 9.024 85.032 31.757 1.00 85.44 ? 58 PRO B O 1 +ATOM 2789 C CB . PRO B 1 61 ? 6.307 83.149 31.748 1.00 75.02 ? 58 PRO B CB 1 +ATOM 2790 C CG . PRO B 1 61 ? 5.253 82.565 30.890 1.00 76.60 ? 58 PRO B CG 1 +ATOM 2791 C CD . PRO B 1 61 ? 5.981 81.964 29.738 1.00 60.31 ? 58 PRO B CD 1 +ATOM 2792 N N . THR B 1 62 ? 9.401 82.829 31.516 1.00 81.94 ? 59 THR B N 1 +ATOM 2793 C CA . THR B 1 62 ? 10.730 82.859 32.118 1.00 88.22 ? 59 THR B CA 1 +ATOM 2794 C C . THR B 1 62 ? 11.711 83.765 31.385 1.00 88.17 ? 59 THR B C 1 +ATOM 2795 O O . THR B 1 62 ? 12.753 84.144 31.924 1.00 86.90 ? 59 THR B O 1 +ATOM 2796 C CB . THR B 1 62 ? 11.320 81.460 32.133 1.00 93.92 ? 59 THR B CB 1 +ATOM 2797 O OG1 . THR B 1 62 ? 11.134 80.864 30.844 1.00 90.79 ? 59 THR B OG1 1 +ATOM 2798 C CG2 . THR B 1 62 ? 10.612 80.623 33.172 1.00 80.59 ? 59 THR B CG2 1 +ATOM 2799 N N . LEU B 1 63 ? 11.372 84.115 30.154 1.00 79.00 ? 60 LEU B N 1 +ATOM 2800 C CA . LEU B 1 63 ? 12.299 84.830 29.297 1.00 59.51 ? 60 LEU B CA 1 +ATOM 2801 C C . LEU B 1 63 ? 11.989 86.318 29.129 1.00 95.80 ? 60 LEU B C 1 +ATOM 2802 O O . LEU B 1 63 ? 12.821 87.062 28.604 1.00 70.19 ? 60 LEU B O 1 +ATOM 2803 C CB . LEU B 1 63 ? 12.382 84.148 27.939 1.00 81.48 ? 60 LEU B CB 1 +ATOM 2804 C CG . LEU B 1 63 ? 13.102 82.805 27.909 1.00 88.05 ? 60 LEU B CG 1 +ATOM 2805 C CD1 . LEU B 1 63 ? 13.084 82.268 26.490 1.00 72.78 ? 60 LEU B CD1 1 +ATOM 2806 C CD2 . LEU B 1 63 ? 14.519 82.981 28.415 1.00 64.19 ? 60 LEU B CD2 1 +ATOM 2807 N N . VAL B 1 64 ? 10.809 86.740 29.585 1.00 88.69 ? 61 VAL B N 1 +ATOM 2808 C CA . VAL B 1 64 ? 10.360 88.124 29.438 1.00 74.19 ? 61 VAL B CA 1 +ATOM 2809 C C . VAL B 1 64 ? 11.406 89.134 29.887 1.00 73.35 ? 61 VAL B C 1 +ATOM 2810 O O . VAL B 1 64 ? 11.714 90.077 29.168 1.00 78.87 ? 61 VAL B O 1 +ATOM 2811 C CB . VAL B 1 64 ? 9.053 88.393 30.215 1.00 72.44 ? 61 VAL B CB 1 +ATOM 2812 C CG1 . VAL B 1 64 ? 8.732 89.876 30.228 1.00 57.83 ? 61 VAL B CG1 1 +ATOM 2813 C CG2 . VAL B 1 64 ? 7.908 87.621 29.600 1.00 67.48 ? 61 VAL B CG2 1 +ATOM 2814 N N . THR B 1 65 ? 11.976 88.935 31.064 1.00 71.92 ? 62 THR B N 1 +ATOM 2815 C CA . THR B 1 65 ? 12.867 89.952 31.598 1.00 83.51 ? 62 THR B CA 1 +ATOM 2816 C C . THR B 1 65 ? 14.191 89.965 30.862 1.00 70.31 ? 62 THR B C 1 +ATOM 2817 O O . THR B 1 65 ? 14.932 90.944 30.904 1.00 102.71 ? 62 THR B O 1 +ATOM 2818 C CB . THR B 1 65 ? 13.144 89.725 33.075 1.00 80.44 ? 62 THR B CB 1 +ATOM 2819 O OG1 . THR B 1 65 ? 14.039 88.619 33.222 1.00 106.79 ? 62 THR B OG1 1 +ATOM 2820 C CG2 . THR B 1 65 ? 11.857 89.426 33.804 1.00 81.75 ? 62 THR B CG2 1 +ATOM 2821 N N . THR B 1 66 ? 14.494 88.863 30.196 1.00 81.91 ? 63 THR B N 1 +ATOM 2822 C CA . THR B 1 66 ? 15.796 88.717 29.584 1.00 83.45 ? 63 THR B CA 1 +ATOM 2823 C C . THR B 1 66 ? 15.702 89.458 28.278 1.00 87.02 ? 63 THR B C 1 +ATOM 2824 O O . THR B 1 66 ? 16.614 90.225 27.910 1.00 79.43 ? 63 THR B O 1 +ATOM 2825 C CB . THR B 1 66 ? 16.145 87.226 29.358 1.00 87.67 ? 63 THR B CB 1 +ATOM 2826 O OG1 . THR B 1 66 ? 15.796 86.462 30.527 1.00 82.49 ? 63 THR B OG1 1 +ATOM 2827 C CG2 . THR B 1 66 ? 17.630 87.058 29.043 1.00 68.57 ? 63 THR B CG2 1 +ATOM 2828 N N . PHE B 1 67 ? 14.541 89.228 27.642 1.00 100.39 ? 64 PHE B N 1 +ATOM 2829 C CA . PHE B 1 67 ? 14.126 89.830 26.364 1.00 89.06 ? 64 PHE B CA 1 +ATOM 2830 C C . PHE B 1 67 ? 13.867 91.389 26.409 1.00 76.04 ? 64 PHE B C 1 +ATOM 2831 O O . PHE B 1 67 ? 14.660 92.220 25.789 1.00 98.13 ? 64 PHE B O 1 +ATOM 2832 C CB . PHE B 1 67 ? 12.844 89.209 25.778 1.00 96.78 ? 64 PHE B CB 1 +ATOM 2833 C CG . PHE B 1 67 ? 12.958 87.806 25.282 1.00 71.95 ? 64 PHE B CG 1 +ATOM 2834 C CD1 . PHE B 1 67 ? 14.132 87.280 24.768 1.00 76.29 ? 64 PHE B CD1 1 +ATOM 2835 C CD2 . PHE B 1 67 ? 11.819 87.013 25.307 1.00 89.90 ? 64 PHE B CD2 1 +ATOM 2836 C CE1 . PHE B 1 67 ? 14.157 85.973 24.315 1.00 80.72 ? 64 PHE B CE1 1 +ATOM 2837 C CE2 . PHE B 1 67 ? 11.839 85.714 24.859 1.00 85.56 ? 64 PHE B CE2 1 +ATOM 2838 C CZ . PHE B 1 67 ? 13.006 85.190 24.365 1.00 80.40 ? 64 PHE B CZ 1 +HETATM 2839 N N1 . CR2 B 1 68 ? 12.793 91.783 27.091 1.00 84.97 ? 65 CR2 B N1 1 +HETATM 2840 C CA1 . CR2 B 1 68 ? 12.658 93.242 27.661 1.00 91.26 ? 65 CR2 B CA1 1 +HETATM 2841 C C1 . CR2 B 1 68 ? 13.203 93.535 29.084 1.00 97.40 ? 65 CR2 B C1 1 +HETATM 2842 N N2 . CR2 B 1 68 ? 12.508 93.546 30.275 1.00 110.25 ? 65 CR2 B N2 1 +HETATM 2843 N N3 . CR2 B 1 68 ? 14.490 93.835 29.332 1.00 86.29 ? 65 CR2 B N3 1 +HETATM 2844 C C2 . CR2 B 1 68 ? 14.681 93.990 30.613 1.00 79.44 ? 65 CR2 B C2 1 +HETATM 2845 O O2 . CR2 B 1 68 ? 15.791 94.251 31.203 1.00 78.81 ? 65 CR2 B O2 1 +HETATM 2846 C CA2 . CR2 B 1 68 ? 13.396 93.791 31.264 1.00 94.17 ? 65 CR2 B CA2 1 +HETATM 2847 C CA3 . CR2 B 1 68 ? 15.572 93.826 28.388 1.00 47.31 ? 65 CR2 B CA3 1 +HETATM 2848 C C3 . CR2 B 1 68 ? 15.836 95.161 27.709 1.00 113.03 ? 65 CR2 B C3 1 +HETATM 2849 O O3 . CR2 B 1 68 ? 17.176 95.597 27.704 1.00 72.85 ? 65 CR2 B O3 1 +HETATM 2850 C CB2 . CR2 B 1 68 ? 13.013 93.883 32.694 1.00 71.15 ? 65 CR2 B CB2 1 +HETATM 2851 C CG2 . CR2 B 1 68 ? 11.651 93.635 33.259 1.00 99.97 ? 65 CR2 B CG2 1 +HETATM 2852 C CD1 . CR2 B 1 68 ? 10.574 93.222 32.483 1.00 67.89 ? 65 CR2 B CD1 1 +HETATM 2853 C CD2 . CR2 B 1 68 ? 11.472 93.704 34.637 1.00 104.00 ? 65 CR2 B CD2 1 +HETATM 2854 C CE1 . CR2 B 1 68 ? 9.343 92.959 33.074 1.00 103.95 ? 65 CR2 B CE1 1 +HETATM 2855 C CE2 . CR2 B 1 68 ? 10.243 93.443 35.227 1.00 69.60 ? 65 CR2 B CE2 1 +HETATM 2856 C CZ . CR2 B 1 68 ? 9.167 93.068 34.448 1.00 92.94 ? 65 CR2 B CZ 1 +HETATM 2857 O OH . CR2 B 1 68 ? 7.946 92.821 35.045 1.00 110.56 ? 65 CR2 B OH 1 +ATOM 2858 N N . VAL B 1 69 ? 14.800 95.996 27.639 1.00 106.05 ? 68 VAL B N 1 +ATOM 2859 C CA . VAL B 1 69 ? 15.162 97.234 27.007 1.00 86.55 ? 68 VAL B CA 1 +ATOM 2860 C C . VAL B 1 69 ? 14.929 98.464 27.778 1.00 61.74 ? 68 VAL B C 1 +ATOM 2861 O O . VAL B 1 69 ? 14.616 99.499 27.229 1.00 119.40 ? 68 VAL B O 1 +ATOM 2862 C CB . VAL B 1 69 ? 15.187 97.368 25.443 1.00 76.24 ? 68 VAL B CB 1 +ATOM 2863 C CG1 . VAL B 1 69 ? 16.265 96.470 24.887 1.00 74.89 ? 68 VAL B CG1 1 +ATOM 2864 C CG2 . VAL B 1 69 ? 13.875 97.156 24.738 1.00 130.40 ? 68 VAL B CG2 1 +ATOM 2865 N N . GLN B 1 70 ? 15.219 98.355 29.065 1.00 90.64 ? 69 GLN B N 1 +ATOM 2866 C CA . GLN B 1 70 ? 14.950 99.412 30.039 1.00 98.03 ? 69 GLN B CA 1 +ATOM 2867 C C . GLN B 1 70 ? 15.415 100.832 29.677 1.00 82.80 ? 69 GLN B C 1 +ATOM 2868 O O . GLN B 1 70 ? 15.366 101.728 30.510 1.00 112.93 ? 69 GLN B O 1 +ATOM 2869 C CB . GLN B 1 70 ? 15.513 99.014 31.404 1.00 84.23 ? 69 GLN B CB 1 +ATOM 2870 C CG . GLN B 1 70 ? 14.809 97.834 32.059 1.00 107.50 ? 69 GLN B CG 1 +ATOM 2871 C CD . GLN B 1 70 ? 15.612 97.252 33.212 1.00 111.96 ? 69 GLN B CD 1 +ATOM 2872 O OE1 . GLN B 1 70 ? 16.797 97.555 33.370 1.00 103.06 ? 69 GLN B OE1 1 +ATOM 2873 N NE2 . GLN B 1 70 ? 14.971 96.416 34.024 1.00 108.70 ? 69 GLN B NE2 1 +ATOM 2874 N N . CYS B 1 71 ? 15.856 101.032 28.441 1.00 100.22 ? 70 CYS B N 1 +ATOM 2875 C CA . CYS B 1 71 ? 16.166 102.356 27.923 1.00 91.70 ? 70 CYS B CA 1 +ATOM 2876 C C . CYS B 1 71 ? 14.928 102.972 27.272 1.00 102.10 ? 70 CYS B C 1 +ATOM 2877 O O . CYS B 1 71 ? 14.979 104.077 26.733 1.00 100.56 ? 70 CYS B O 1 +ATOM 2878 C CB . CYS B 1 71 ? 17.322 102.273 26.916 1.00 86.42 ? 70 CYS B CB 1 +ATOM 2879 S SG . CYS B 1 71 ? 17.184 100.967 25.661 1.00 115.56 ? 70 CYS B SG 1 +ATOM 2880 N N . PHE B 1 72 ? 13.820 102.238 27.324 1.00 89.54 ? 71 PHE B N 1 +ATOM 2881 C CA . PHE B 1 72 ? 12.540 102.706 26.805 1.00 78.57 ? 71 PHE B CA 1 +ATOM 2882 C C . PHE B 1 72 ? 11.577 103.053 27.936 1.00 76.38 ? 71 PHE B C 1 +ATOM 2883 O O . PHE B 1 72 ? 10.379 103.203 27.727 1.00 111.60 ? 71 PHE B O 1 +ATOM 2884 C CB . PHE B 1 72 ? 11.939 101.675 25.847 1.00 75.97 ? 71 PHE B CB 1 +ATOM 2885 C CG . PHE B 1 72 ? 12.632 101.630 24.525 1.00 79.64 ? 71 PHE B CG 1 +ATOM 2886 C CD1 . PHE B 1 72 ? 12.435 102.636 23.600 1.00 88.88 ? 71 PHE B CD1 1 +ATOM 2887 C CD2 . PHE B 1 72 ? 13.506 100.608 24.217 1.00 95.21 ? 71 PHE B CD2 1 +ATOM 2888 C CE1 . PHE B 1 72 ? 13.083 102.617 22.388 1.00 74.91 ? 71 PHE B CE1 1 +ATOM 2889 C CE2 . PHE B 1 72 ? 14.163 100.584 23.004 1.00 75.07 ? 71 PHE B CE2 1 +ATOM 2890 C CZ . PHE B 1 72 ? 13.947 101.589 22.087 1.00 107.90 ? 71 PHE B CZ 1 +ATOM 2891 N N . SER B 1 73 ? 12.116 103.193 29.138 1.00 79.58 ? 72 SER B N 1 +ATOM 2892 C CA . SER B 1 73 ? 11.331 103.664 30.265 1.00 97.65 ? 72 SER B CA 1 +ATOM 2893 C C . SER B 1 73 ? 11.073 105.163 30.152 1.00 96.97 ? 72 SER B C 1 +ATOM 2894 O O . SER B 1 73 ? 11.943 105.931 29.743 1.00 133.23 ? 72 SER B O 1 +ATOM 2895 C CB . SER B 1 73 ? 12.050 103.354 31.570 1.00 86.62 ? 72 SER B CB 1 +ATOM 2896 N N . ARG B 1 74 ? 9.869 105.575 30.520 1.00 84.17 ? 73 ARG B N 1 +ATOM 2897 C CA . ARG B 1 74 ? 9.561 106.990 30.637 1.00 91.93 ? 73 ARG B CA 1 +ATOM 2898 C C . ARG B 1 74 ? 10.149 107.533 31.936 1.00 90.03 ? 73 ARG B C 1 +ATOM 2899 O O . ARG B 1 74 ? 9.769 107.103 33.028 1.00 80.84 ? 73 ARG B O 1 +ATOM 2900 C CB . ARG B 1 74 ? 8.045 107.196 30.619 1.00 88.15 ? 73 ARG B CB 1 +ATOM 2901 C CG . ARG B 1 74 ? 7.598 108.645 30.570 1.00 86.43 ? 73 ARG B CG 1 +ATOM 2902 C CD . ARG B 1 74 ? 6.105 108.761 30.287 1.00 73.35 ? 73 ARG B CD 1 +ATOM 2903 N NE . ARG B 1 74 ? 5.251 108.315 31.387 1.00 84.02 ? 73 ARG B NE 1 +ATOM 2904 C CZ . ARG B 1 74 ? 5.182 108.903 32.580 1.00 107.10 ? 73 ARG B CZ 1 +ATOM 2905 N NH1 . ARG B 1 74 ? 5.942 109.965 32.862 1.00 57.48 ? 73 ARG B NH1 1 +ATOM 2906 N NH2 . ARG B 1 74 ? 4.353 108.422 33.503 1.00 72.85 ? 73 ARG B NH2 1 +ATOM 2907 N N . TYR B 1 75 ? 11.092 108.463 31.814 1.00 99.40 ? 74 TYR B N 1 +ATOM 2908 C CA . TYR B 1 75 ? 11.598 109.197 32.972 1.00 106.98 ? 74 TYR B CA 1 +ATOM 2909 C C . TYR B 1 75 ? 10.874 110.544 33.078 1.00 105.59 ? 74 TYR B C 1 +ATOM 2910 O O . TYR B 1 75 ? 10.940 111.356 32.155 1.00 127.86 ? 74 TYR B O 1 +ATOM 2911 C CB . TYR B 1 75 ? 13.126 109.385 32.890 1.00 75.33 ? 74 TYR B CB 1 +ATOM 2912 C CG . TYR B 1 75 ? 13.918 108.239 33.498 1.00 89.30 ? 74 TYR B CG 1 +ATOM 2913 C CD1 . TYR B 1 75 ? 14.050 107.024 32.835 1.00 102.72 ? 74 TYR B CD1 1 +ATOM 2914 C CD2 . TYR B 1 75 ? 14.521 108.370 34.740 1.00 102.36 ? 74 TYR B CD2 1 +ATOM 2915 C CE1 . TYR B 1 75 ? 14.760 105.972 33.393 1.00 94.00 ? 74 TYR B CE1 1 +ATOM 2916 C CE2 . TYR B 1 75 ? 15.233 107.327 35.305 1.00 91.65 ? 74 TYR B CE2 1 +ATOM 2917 C CZ . TYR B 1 75 ? 15.349 106.131 34.630 1.00 101.62 ? 74 TYR B CZ 1 +ATOM 2918 O OH . TYR B 1 75 ? 16.059 105.097 35.200 1.00 109.75 ? 74 TYR B OH 1 +ATOM 2919 N N . PRO B 1 76 ? 10.156 110.774 34.193 1.00 91.75 ? 75 PRO B N 1 +ATOM 2920 C CA . PRO B 1 76 ? 9.507 112.071 34.411 1.00 87.35 ? 75 PRO B CA 1 +ATOM 2921 C C . PRO B 1 76 ? 10.549 113.185 34.371 1.00 130.63 ? 75 PRO B C 1 +ATOM 2922 O O . PRO B 1 76 ? 11.727 112.919 34.622 1.00 121.84 ? 75 PRO B O 1 +ATOM 2923 C CB . PRO B 1 76 ? 8.929 111.945 35.826 1.00 102.09 ? 75 PRO B CB 1 +ATOM 2924 C CG . PRO B 1 76 ? 8.816 110.496 36.079 1.00 98.49 ? 75 PRO B CG 1 +ATOM 2925 C CD . PRO B 1 76 ? 9.927 109.845 35.312 1.00 105.35 ? 75 PRO B CD 1 +ATOM 2926 N N . ASP B 1 77 ? 10.124 114.404 34.055 1.00 118.45 ? 76 ASP B N 1 +ATOM 2927 C CA . ASP B 1 77 ? 11.050 115.520 33.862 1.00 130.34 ? 76 ASP B CA 1 +ATOM 2928 C C . ASP B 1 77 ? 12.034 115.703 35.011 1.00 137.54 ? 76 ASP B C 1 +ATOM 2929 O O . ASP B 1 77 ? 13.240 115.867 34.797 1.00 102.59 ? 76 ASP B O 1 +ATOM 2930 C CB . ASP B 1 77 ? 10.275 116.816 33.639 1.00 154.93 ? 76 ASP B CB 1 +ATOM 2931 C CG . ASP B 1 77 ? 9.718 116.924 32.240 1.00 172.49 ? 76 ASP B CG 1 +ATOM 2932 O OD1 . ASP B 1 77 ? 10.479 116.687 31.275 1.00 161.34 ? 76 ASP B OD1 1 +ATOM 2933 O OD2 . ASP B 1 77 ? 8.517 117.240 32.111 1.00 179.81 ? 76 ASP B OD2 1 +ATOM 2934 N N . HIS B 1 78 ? 11.511 115.656 36.232 1.00 130.63 ? 77 HIS B N 1 +ATOM 2935 C CA . HIS B 1 78 ? 12.328 115.876 37.418 1.00 85.88 ? 77 HIS B CA 1 +ATOM 2936 C C . HIS B 1 78 ? 13.334 114.752 37.676 1.00 125.54 ? 77 HIS B C 1 +ATOM 2937 O O . HIS B 1 78 ? 14.167 114.856 38.577 1.00 133.60 ? 77 HIS B O 1 +ATOM 2938 C CB . HIS B 1 78 ? 11.450 116.126 38.651 1.00 84.34 ? 77 HIS B CB 1 +ATOM 2939 C CG . HIS B 1 78 ? 10.636 114.945 39.085 1.00 105.21 ? 77 HIS B CG 1 +ATOM 2940 N ND1 . HIS B 1 78 ? 9.449 114.591 38.479 1.00 99.67 ? 77 HIS B ND1 1 +ATOM 2941 C CD2 . HIS B 1 78 ? 10.815 114.066 40.101 1.00 111.54 ? 77 HIS B CD2 1 +ATOM 2942 C CE1 . HIS B 1 78 ? 8.946 113.531 39.086 1.00 122.17 ? 77 HIS B CE1 1 +ATOM 2943 N NE2 . HIS B 1 78 ? 9.756 113.193 40.074 1.00 128.84 ? 77 HIS B NE2 1 +ATOM 2944 N N . MET B 1 79 ? 13.267 113.694 36.871 1.00 124.45 ? 78 MET B N 1 +ATOM 2945 C CA . MET B 1 79 ? 14.143 112.540 37.048 1.00 99.35 ? 78 MET B CA 1 +ATOM 2946 C C . MET B 1 79 ? 15.186 112.379 35.927 1.00 119.10 ? 78 MET B C 1 +ATOM 2947 O O . MET B 1 79 ? 16.252 111.799 36.147 1.00 109.18 ? 78 MET B O 1 +ATOM 2948 C CB . MET B 1 79 ? 13.310 111.258 37.223 1.00 87.58 ? 78 MET B CB 1 +ATOM 2949 C CG . MET B 1 79 ? 12.552 111.197 38.546 1.00 108.67 ? 78 MET B CG 1 +ATOM 2950 S SD . MET B 1 79 ? 11.674 109.655 38.887 1.00 101.86 ? 78 MET B SD 1 +ATOM 2951 C CE . MET B 1 79 ? 12.991 108.464 38.736 1.00 86.79 ? 78 MET B CE 1 +ATOM 2952 N N . LYS B 1 80 ? 14.900 112.932 34.749 1.00 85.09 ? 79 LYS B N 1 +ATOM 2953 C CA . LYS B 1 80 ? 15.691 112.684 33.529 1.00 100.46 ? 79 LYS B CA 1 +ATOM 2954 C C . LYS B 1 80 ? 17.222 112.788 33.607 1.00 110.54 ? 79 LYS B C 1 +ATOM 2955 O O . LYS B 1 80 ? 17.901 112.646 32.589 1.00 135.09 ? 79 LYS B O 1 +ATOM 2956 C CB . LYS B 1 80 ? 15.191 113.565 32.383 1.00 74.79 ? 79 LYS B CB 1 +ATOM 2957 C CG . LYS B 1 80 ? 13.788 113.226 31.928 1.00 123.28 ? 79 LYS B CG 1 +ATOM 2958 C CD . LYS B 1 80 ? 13.426 113.944 30.641 1.00 97.12 ? 79 LYS B CD 1 +ATOM 2959 C CE . LYS B 1 80 ? 12.013 113.590 30.197 1.00 100.81 ? 79 LYS B CE 1 +ATOM 2960 N NZ . LYS B 1 80 ? 11.887 112.160 29.785 1.00 113.74 ? 79 LYS B NZ 1 +ATOM 2961 N N . GLN B 1 81 ? 17.759 113.035 34.798 1.00 128.19 ? 80 GLN B N 1 +ATOM 2962 C CA . GLN B 1 81 ? 19.202 113.109 34.985 1.00 130.02 ? 80 GLN B CA 1 +ATOM 2963 C C . GLN B 1 81 ? 19.710 111.850 35.684 1.00 126.96 ? 80 GLN B C 1 +ATOM 2964 O O . GLN B 1 81 ? 20.913 111.647 35.818 1.00 148.05 ? 80 GLN B O 1 +ATOM 2965 C CB . GLN B 1 81 ? 19.598 114.378 35.759 1.00 114.51 ? 80 GLN B CB 1 +ATOM 2966 C CG . GLN B 1 81 ? 19.122 114.443 37.219 1.00 108.24 ? 80 GLN B CG 1 +ATOM 2967 C CD . GLN B 1 81 ? 17.686 114.944 37.375 1.00 143.60 ? 80 GLN B CD 1 +ATOM 2968 O OE1 . GLN B 1 81 ? 17.021 115.285 36.393 1.00 160.90 ? 80 GLN B OE1 1 +ATOM 2969 N NE2 . GLN B 1 81 ? 17.204 114.990 38.619 1.00 121.54 ? 80 GLN B NE2 1 +ATOM 2970 N N . HIS B 1 82 ? 18.782 111.003 36.120 1.00 106.74 ? 81 HIS B N 1 +ATOM 2971 C CA . HIS B 1 82 ? 19.127 109.722 36.733 1.00 126.33 ? 81 HIS B CA 1 +ATOM 2972 C C . HIS B 1 82 ? 18.854 108.570 35.766 1.00 130.13 ? 81 HIS B C 1 +ATOM 2973 O O . HIS B 1 82 ? 18.817 107.399 36.150 1.00 109.54 ? 81 HIS B O 1 +ATOM 2974 C CB . HIS B 1 82 ? 18.348 109.519 38.030 1.00 118.91 ? 81 HIS B CB 1 +ATOM 2975 C CG . HIS B 1 82 ? 18.575 110.593 39.050 1.00 126.10 ? 81 HIS B CG 1 +ATOM 2976 N ND1 . HIS B 1 82 ? 19.746 110.703 39.770 1.00 135.08 ? 81 HIS B ND1 1 +ATOM 2977 C CD2 . HIS B 1 82 ? 17.775 111.598 39.476 1.00 91.93 ? 81 HIS B CD2 1 +ATOM 2978 C CE1 . HIS B 1 82 ? 19.658 111.733 40.593 1.00 135.36 ? 81 HIS B CE1 1 +ATOM 2979 N NE2 . HIS B 1 82 ? 18.473 112.293 40.434 1.00 131.45 ? 81 HIS B NE2 1 +ATOM 2980 N N . ASP B 1 83 ? 18.659 108.932 34.505 1.00 110.93 ? 82 ASP B N 1 +ATOM 2981 C CA . ASP B 1 83 ? 18.434 107.979 33.437 1.00 106.77 ? 82 ASP B CA 1 +ATOM 2982 C C . ASP B 1 83 ? 19.787 107.518 32.930 1.00 104.00 ? 82 ASP B C 1 +ATOM 2983 O O . ASP B 1 83 ? 20.407 108.186 32.104 1.00 123.15 ? 82 ASP B O 1 +ATOM 2984 C CB . ASP B 1 83 ? 17.659 108.664 32.312 1.00 145.86 ? 82 ASP B CB 1 +ATOM 2985 C CG . ASP B 1 83 ? 17.119 107.691 31.282 1.00 137.70 ? 82 ASP B CG 1 +ATOM 2986 O OD1 . ASP B 1 83 ? 17.729 106.623 31.063 1.00 113.74 ? 82 ASP B OD1 1 +ATOM 2987 O OD2 . ASP B 1 83 ? 16.077 108.009 30.675 1.00 154.10 ? 82 ASP B OD2 1 +ATOM 2988 N N . PHE B 1 84 ? 20.238 106.374 33.437 1.00 104.41 ? 83 PHE B N 1 +ATOM 2989 C CA . PHE B 1 84 ? 21.514 105.789 33.043 1.00 99.95 ? 83 PHE B CA 1 +ATOM 2990 C C . PHE B 1 84 ? 21.471 105.174 31.654 1.00 96.85 ? 83 PHE B C 1 +ATOM 2991 O O . PHE B 1 84 ? 22.345 105.419 30.821 1.00 123.88 ? 83 PHE B O 1 +ATOM 2992 C CB . PHE B 1 84 ? 21.918 104.700 34.031 1.00 102.45 ? 83 PHE B CB 1 +ATOM 2993 C CG . PHE B 1 84 ? 23.032 103.832 33.535 1.00 110.22 ? 83 PHE B CG 1 +ATOM 2994 C CD1 . PHE B 1 84 ? 24.289 104.370 33.302 1.00 129.69 ? 83 PHE B CD1 1 +ATOM 2995 C CD2 . PHE B 1 84 ? 22.827 102.484 33.290 1.00 109.20 ? 83 PHE B CD2 1 +ATOM 2996 C CE1 . PHE B 1 84 ? 25.326 103.581 32.836 1.00 127.21 ? 83 PHE B CE1 1 +ATOM 2997 C CE2 . PHE B 1 84 ? 23.860 101.687 32.826 1.00 131.39 ? 83 PHE B CE2 1 +ATOM 2998 C CZ . PHE B 1 84 ? 25.112 102.238 32.598 1.00 129.79 ? 83 PHE B CZ 1 +ATOM 2999 N N . PHE B 1 85 ? 20.448 104.359 31.428 1.00 104.62 ? 84 PHE B N 1 +ATOM 3000 C CA . PHE B 1 85 ? 20.316 103.587 30.201 1.00 99.96 ? 84 PHE B CA 1 +ATOM 3001 C C . PHE B 1 85 ? 20.439 104.430 28.937 1.00 106.28 ? 84 PHE B C 1 +ATOM 3002 O O . PHE B 1 85 ? 21.260 104.135 28.073 1.00 133.16 ? 84 PHE B O 1 +ATOM 3003 C CB . PHE B 1 85 ? 19.005 102.808 30.212 1.00 101.78 ? 84 PHE B CB 1 +ATOM 3004 C CG . PHE B 1 85 ? 18.802 101.994 31.455 1.00 100.84 ? 84 PHE B CG 1 +ATOM 3005 C CD1 . PHE B 1 85 ? 19.475 100.803 31.637 1.00 103.06 ? 84 PHE B CD1 1 +ATOM 3006 C CD2 . PHE B 1 85 ? 17.942 102.424 32.446 1.00 97.87 ? 84 PHE B CD2 1 +ATOM 3007 C CE1 . PHE B 1 85 ? 19.289 100.056 32.776 1.00 100.06 ? 84 PHE B CE1 1 +ATOM 3008 C CE2 . PHE B 1 85 ? 17.750 101.676 33.585 1.00 80.10 ? 84 PHE B CE2 1 +ATOM 3009 C CZ . PHE B 1 85 ? 18.426 100.491 33.749 1.00 96.00 ? 84 PHE B CZ 1 +ATOM 3010 N N . LYS B 1 86 ? 19.648 105.488 28.829 1.00 107.81 ? 85 LYS B N 1 +ATOM 3011 C CA . LYS B 1 86 ? 19.721 106.315 27.631 1.00 127.45 ? 85 LYS B CA 1 +ATOM 3012 C C . LYS B 1 86 ? 21.074 107.024 27.499 1.00 128.68 ? 85 LYS B C 1 +ATOM 3013 O O . LYS B 1 86 ? 21.611 107.156 26.397 1.00 115.51 ? 85 LYS B O 1 +ATOM 3014 C CB . LYS B 1 86 ? 18.577 107.325 27.599 1.00 109.41 ? 85 LYS B CB 1 +ATOM 3015 C CG . LYS B 1 86 ? 17.202 106.703 27.644 1.00 93.65 ? 85 LYS B CG 1 +ATOM 3016 C CD . LYS B 1 86 ? 16.142 107.757 27.410 1.00 100.93 ? 85 LYS B CD 1 +ATOM 3017 C CE . LYS B 1 86 ? 14.755 107.147 27.375 1.00 76.83 ? 85 LYS B CE 1 +ATOM 3018 N NZ . LYS B 1 86 ? 14.358 106.549 28.680 1.00 118.43 ? 85 LYS B NZ 1 +ATOM 3019 N N . SER B 1 87 ? 21.625 107.454 28.632 1.00 124.36 ? 86 SER B N 1 +ATOM 3020 C CA . SER B 1 87 ? 22.839 108.271 28.659 1.00 119.23 ? 86 SER B CA 1 +ATOM 3021 C C . SER B 1 87 ? 24.075 107.525 28.169 1.00 120.91 ? 86 SER B C 1 +ATOM 3022 O O . SER B 1 87 ? 25.090 108.139 27.831 1.00 122.87 ? 86 SER B O 1 +ATOM 3023 C CB . SER B 1 87 ? 23.096 108.770 30.079 1.00 133.13 ? 86 SER B CB 1 +ATOM 3024 O OG . SER B 1 87 ? 23.588 107.723 30.900 1.00 117.63 ? 86 SER B OG 1 +ATOM 3025 N N . ALA B 1 88 ? 23.984 106.199 28.153 1.00 121.07 ? 87 ALA B N 1 +ATOM 3026 C CA . ALA B 1 88 ? 25.087 105.346 27.734 1.00 102.36 ? 87 ALA B CA 1 +ATOM 3027 C C . ALA B 1 88 ? 25.082 105.147 26.222 1.00 94.40 ? 87 ALA B C 1 +ATOM 3028 O O . ALA B 1 88 ? 26.028 104.603 25.658 1.00 113.93 ? 87 ALA B O 1 +ATOM 3029 C CB . ALA B 1 88 ? 25.015 103.998 28.451 1.00 94.72 ? 87 ALA B CB 1 +ATOM 3030 N N . MET B 1 89 ? 24.011 105.597 25.575 1.00 103.53 ? 88 MET B N 1 +ATOM 3031 C CA . MET B 1 89 ? 23.832 105.427 24.134 1.00 117.82 ? 88 MET B CA 1 +ATOM 3032 C C . MET B 1 89 ? 24.554 106.540 23.375 1.00 103.10 ? 88 MET B C 1 +ATOM 3033 O O . MET B 1 89 ? 24.874 107.571 23.963 1.00 117.46 ? 88 MET B O 1 +ATOM 3034 C CB . MET B 1 89 ? 22.338 105.417 23.805 1.00 104.69 ? 88 MET B CB 1 +ATOM 3035 C CG . MET B 1 89 ? 21.584 104.284 24.463 1.00 119.39 ? 88 MET B CG 1 +ATOM 3036 S SD . MET B 1 89 ? 22.070 102.696 23.772 1.00 112.49 ? 88 MET B SD 1 +ATOM 3037 C CE . MET B 1 89 ? 21.273 101.565 24.913 1.00 126.86 ? 88 MET B CE 1 +ATOM 3038 N N . PRO B 1 90 ? 24.823 106.342 22.070 1.00 94.13 ? 89 PRO B N 1 +ATOM 3039 C CA . PRO B 1 90 ? 24.465 105.199 21.221 1.00 124.02 ? 89 PRO B CA 1 +ATOM 3040 C C . PRO B 1 90 ? 25.469 104.063 21.318 1.00 110.86 ? 89 PRO B C 1 +ATOM 3041 O O . PRO B 1 90 ? 25.276 103.014 20.696 1.00 117.04 ? 89 PRO B O 1 +ATOM 3042 C CB . PRO B 1 90 ? 24.481 105.795 19.810 1.00 113.05 ? 89 PRO B CB 1 +ATOM 3043 C CG . PRO B 1 90 ? 25.446 106.948 19.886 1.00 107.18 ? 89 PRO B CG 1 +ATOM 3044 C CD . PRO B 1 90 ? 25.599 107.354 21.331 1.00 103.76 ? 89 PRO B CD 1 +ATOM 3045 N N . GLU B 1 91 ? 26.531 104.276 22.086 1.00 95.49 ? 90 GLU B N 1 +ATOM 3046 C CA . GLU B 1 91 ? 27.607 103.302 22.169 1.00 125.98 ? 90 GLU B CA 1 +ATOM 3047 C C . GLU B 1 91 ? 27.116 102.047 22.873 1.00 120.59 ? 90 GLU B C 1 +ATOM 3048 O O . GLU B 1 91 ? 27.415 100.929 22.455 1.00 119.69 ? 90 GLU B O 1 +ATOM 3049 C CB . GLU B 1 91 ? 28.828 103.901 22.870 1.00 157.27 ? 90 GLU B CB 1 +ATOM 3050 C CG . GLU B 1 91 ? 29.341 105.177 22.207 1.00 168.15 ? 90 GLU B CG 1 +ATOM 3051 C CD . GLU B 1 91 ? 30.856 105.259 22.170 1.00 184.12 ? 90 GLU B CD 1 +ATOM 3052 O OE1 . GLU B 1 91 ? 31.484 104.488 21.408 1.00 175.87 ? 90 GLU B OE1 1 +ATOM 3053 O OE2 . GLU B 1 91 ? 31.416 106.106 22.897 1.00 189.11 ? 90 GLU B OE2 1 +ATOM 3054 N N . GLY B 1 92 ? 26.346 102.235 23.937 1.00 103.44 ? 91 GLY B N 1 +ATOM 3055 C CA . GLY B 1 92 ? 25.655 101.121 24.548 1.00 98.09 ? 91 GLY B CA 1 +ATOM 3056 C C . GLY B 1 92 ? 26.069 100.735 25.949 1.00 98.56 ? 91 GLY B C 1 +ATOM 3057 O O . GLY B 1 92 ? 26.847 101.424 26.608 1.00 116.45 ? 91 GLY B O 1 +ATOM 3058 N N . TYR B 1 93 ? 25.520 99.616 26.404 1.00 95.92 ? 92 TYR B N 1 +ATOM 3059 C CA . TYR B 1 93 ? 25.825 99.085 27.722 1.00 102.29 ? 92 TYR B CA 1 +ATOM 3060 C C . TYR B 1 93 ? 25.733 97.554 27.745 1.00 112.94 ? 92 TYR B C 1 +ATOM 3061 O O . TYR B 1 93 ? 25.172 96.942 26.831 1.00 113.40 ? 92 TYR B O 1 +ATOM 3062 C CB . TYR B 1 93 ? 24.930 99.733 28.792 1.00 87.03 ? 92 TYR B CB 1 +ATOM 3063 C CG . TYR B 1 93 ? 23.431 99.456 28.695 1.00 108.16 ? 92 TYR B CG 1 +ATOM 3064 C CD1 . TYR B 1 93 ? 22.889 98.270 29.175 1.00 123.67 ? 92 TYR B CD1 1 +ATOM 3065 C CD2 . TYR B 1 93 ? 22.555 100.402 28.168 1.00 105.93 ? 92 TYR B CD2 1 +ATOM 3066 C CE1 . TYR B 1 93 ? 21.522 98.017 29.108 1.00 117.53 ? 92 TYR B CE1 1 +ATOM 3067 C CE2 . TYR B 1 93 ? 21.180 100.158 28.099 1.00 116.53 ? 92 TYR B CE2 1 +ATOM 3068 C CZ . TYR B 1 93 ? 20.670 98.961 28.573 1.00 111.32 ? 92 TYR B CZ 1 +ATOM 3069 O OH . TYR B 1 93 ? 19.313 98.698 28.518 1.00 119.77 ? 92 TYR B OH 1 +ATOM 3070 N N . VAL B 1 94 ? 26.306 96.946 28.783 1.00 122.99 ? 93 VAL B N 1 +ATOM 3071 C CA . VAL B 1 94 ? 26.294 95.494 28.960 1.00 111.40 ? 93 VAL B CA 1 +ATOM 3072 C C . VAL B 1 94 ? 25.446 95.145 30.181 1.00 111.26 ? 93 VAL B C 1 +ATOM 3073 O O . VAL B 1 94 ? 25.631 95.726 31.252 1.00 113.90 ? 93 VAL B O 1 +ATOM 3074 C CB . VAL B 1 94 ? 27.722 94.924 29.186 1.00 109.47 ? 93 VAL B CB 1 +ATOM 3075 C CG1 . VAL B 1 94 ? 27.715 93.401 29.074 1.00 98.08 ? 93 VAL B CG1 1 +ATOM 3076 C CG2 . VAL B 1 94 ? 28.733 95.540 28.217 1.00 112.76 ? 93 VAL B CG2 1 +ATOM 3077 N N . GLN B 1 95 ? 24.524 94.198 30.027 1.00 83.60 ? 94 GLN B N 1 +ATOM 3078 C CA . GLN B 1 95 ? 23.608 93.837 31.110 1.00 104.39 ? 94 GLN B CA 1 +ATOM 3079 C C . GLN B 1 95 ? 23.771 92.373 31.499 1.00 112.55 ? 94 GLN B C 1 +ATOM 3080 O O . GLN B 1 95 ? 23.388 91.471 30.747 1.00 90.76 ? 94 GLN B O 1 +ATOM 3081 C CB . GLN B 1 95 ? 22.156 94.131 30.707 1.00 94.06 ? 94 GLN B CB 1 +ATOM 3082 C CG . GLN B 1 95 ? 21.108 93.742 31.742 1.00 90.17 ? 94 GLN B CG 1 +ATOM 3083 C CD . GLN B 1 95 ? 19.718 94.273 31.416 1.00 97.87 ? 94 GLN B CD 1 +ATOM 3084 O OE1 . GLN B 1 95 ? 19.506 95.482 31.309 1.00 93.25 ? 94 GLN B OE1 1 +ATOM 3085 N NE2 . GLN B 1 95 ? 18.762 93.365 31.268 1.00 103.34 ? 94 GLN B NE2 1 +ATOM 3086 N N . GLU B 1 96 ? 24.348 92.153 32.676 1.00 95.85 ? 95 GLU B N 1 +ATOM 3087 C CA . GLU B 1 96 ? 24.591 90.810 33.182 1.00 80.75 ? 95 GLU B CA 1 +ATOM 3088 C C . GLU B 1 96 ? 23.622 90.510 34.316 1.00 95.67 ? 95 GLU B C 1 +ATOM 3089 O O . GLU B 1 96 ? 23.458 91.310 35.237 1.00 102.30 ? 95 GLU B O 1 +ATOM 3090 C CB . GLU B 1 96 ? 26.045 90.673 33.663 1.00 114.92 ? 95 GLU B CB 1 +ATOM 3091 C CG . GLU B 1 96 ? 27.098 90.678 32.537 1.00 146.89 ? 95 GLU B CG 1 +ATOM 3092 C CD . GLU B 1 96 ? 28.535 90.946 33.025 1.00 173.69 ? 95 GLU B CD 1 +ATOM 3093 O OE1 . GLU B 1 96 ? 28.873 92.119 33.289 1.00 180.04 ? 95 GLU B OE1 1 +ATOM 3094 O OE2 . GLU B 1 96 ? 29.333 89.988 33.130 1.00 171.93 ? 95 GLU B OE2 1 +ATOM 3095 N N . ARG B 1 97 ? 22.963 89.362 34.240 1.00 74.34 ? 96 ARG B N 1 +ATOM 3096 C CA . ARG B 1 97 ? 22.053 88.967 35.300 1.00 98.22 ? 96 ARG B CA 1 +ATOM 3097 C C . ARG B 1 97 ? 22.349 87.565 35.786 1.00 113.64 ? 96 ARG B C 1 +ATOM 3098 O O . ARG B 1 97 ? 22.998 86.776 35.108 1.00 105.24 ? 96 ARG B O 1 +ATOM 3099 C CB . ARG B 1 97 ? 20.598 89.020 34.828 1.00 77.39 ? 96 ARG B CB 1 +ATOM 3100 C CG . ARG B 1 97 ? 19.993 90.406 34.753 1.00 118.05 ? 96 ARG B CG 1 +ATOM 3101 C CD . ARG B 1 97 ? 18.484 90.372 34.996 1.00 95.81 ? 96 ARG B CD 1 +ATOM 3102 N NE . ARG B 1 97 ? 17.853 91.627 34.597 1.00 121.14 ? 96 ARG B NE 1 +ATOM 3103 C CZ . ARG B 1 97 ? 17.103 91.783 33.510 1.00 107.84 ? 96 ARG B CZ 1 +ATOM 3104 N NH1 . ARG B 1 97 ? 16.860 90.753 32.709 1.00 118.91 ? 96 ARG B NH1 1 +ATOM 3105 N NH2 . ARG B 1 97 ? 16.583 92.971 33.234 1.00 101.80 ? 96 ARG B NH2 1 +ATOM 3106 N N . THR B 1 98 ? 21.858 87.265 36.976 1.00 96.90 ? 97 THR B N 1 +ATOM 3107 C CA . THR B 1 98 ? 21.759 85.898 37.433 1.00 118.05 ? 97 THR B CA 1 +ATOM 3108 C C . THR B 1 98 ? 20.334 85.776 37.970 1.00 102.04 ? 97 THR B C 1 +ATOM 3109 O O . THR B 1 98 ? 19.793 86.736 38.516 1.00 100.20 ? 97 THR B O 1 +ATOM 3110 C CB . THR B 1 98 ? 22.814 85.593 38.504 1.00 123.03 ? 97 THR B CB 1 +ATOM 3111 O OG1 . THR B 1 98 ? 24.086 86.121 38.088 1.00 96.00 ? 97 THR B OG1 1 +ATOM 3112 C CG2 . THR B 1 98 ? 22.918 84.085 38.740 1.00 71.11 ? 97 THR B CG2 1 +ATOM 3113 N N . ILE B 1 99 ? 19.704 84.623 37.779 1.00 89.75 ? 98 ILE B N 1 +ATOM 3114 C CA . ILE B 1 99 ? 18.275 84.494 38.065 1.00 108.00 ? 98 ILE B CA 1 +ATOM 3115 C C . ILE B 1 99 ? 17.938 83.180 38.794 1.00 115.09 ? 98 ILE B C 1 +ATOM 3116 O O . ILE B 1 99 ? 17.774 82.122 38.183 1.00 94.08 ? 98 ILE B O 1 +ATOM 3117 C CB . ILE B 1 99 ? 17.432 84.693 36.764 1.00 91.17 ? 98 ILE B CB 1 +ATOM 3118 C CG1 . ILE B 1 99 ? 17.687 86.091 36.174 1.00 76.20 ? 98 ILE B CG1 1 +ATOM 3119 C CG2 . ILE B 1 99 ? 15.938 84.464 37.025 1.00 69.47 ? 98 ILE B CG2 1 +ATOM 3120 C CD1 . ILE B 1 99 ? 17.667 86.172 34.672 1.00 73.33 ? 98 ILE B CD1 1 +ATOM 3121 N N . PHE B 1 100 ? 17.846 83.259 40.115 1.00 87.72 ? 99 PHE B N 1 +ATOM 3122 C CA . PHE B 1 100 ? 17.606 82.079 40.928 1.00 79.52 ? 99 PHE B CA 1 +ATOM 3123 C C . PHE B 1 100 ? 16.125 81.802 41.052 1.00 80.14 ? 99 PHE B C 1 +ATOM 3124 O O . PHE B 1 100 ? 15.439 82.462 41.815 1.00 97.64 ? 99 PHE B O 1 +ATOM 3125 C CB . PHE B 1 100 ? 18.194 82.274 42.326 1.00 77.37 ? 99 PHE B CB 1 +ATOM 3126 C CG . PHE B 1 100 ? 19.623 82.708 42.314 1.00 90.89 ? 99 PHE B CG 1 +ATOM 3127 C CD1 . PHE B 1 100 ? 20.643 81.773 42.287 1.00 104.81 ? 99 PHE B CD1 1 +ATOM 3128 C CD2 . PHE B 1 100 ? 19.952 84.053 42.311 1.00 104.42 ? 99 PHE B CD2 1 +ATOM 3129 C CE1 . PHE B 1 100 ? 21.970 82.171 42.264 1.00 101.57 ? 99 PHE B CE1 1 +ATOM 3130 C CE2 . PHE B 1 100 ? 21.280 84.460 42.287 1.00 108.00 ? 99 PHE B CE2 1 +ATOM 3131 C CZ . PHE B 1 100 ? 22.289 83.518 42.264 1.00 93.44 ? 99 PHE B CZ 1 +ATOM 3132 N N . PHE B 1 101 ? 15.618 80.832 40.306 1.00 77.18 ? 100 PHE B N 1 +ATOM 3133 C CA . PHE B 1 101 ? 14.270 80.361 40.573 1.00 91.63 ? 100 PHE B CA 1 +ATOM 3134 C C . PHE B 1 101 ? 14.321 79.603 41.891 1.00 96.78 ? 100 PHE B C 1 +ATOM 3135 O O . PHE B 1 101 ? 15.108 78.675 42.046 1.00 98.94 ? 100 PHE B O 1 +ATOM 3136 C CB . PHE B 1 101 ? 13.760 79.475 39.437 1.00 62.48 ? 100 PHE B CB 1 +ATOM 3137 C CG . PHE B 1 101 ? 13.649 80.192 38.122 1.00 83.07 ? 100 PHE B CG 1 +ATOM 3138 C CD1 . PHE B 1 101 ? 14.788 80.529 37.403 1.00 99.25 ? 100 PHE B CD1 1 +ATOM 3139 C CD2 . PHE B 1 101 ? 12.410 80.542 37.609 1.00 95.62 ? 100 PHE B CD2 1 +ATOM 3140 C CE1 . PHE B 1 101 ? 14.696 81.196 36.204 1.00 71.46 ? 100 PHE B CE1 1 +ATOM 3141 C CE2 . PHE B 1 101 ? 12.310 81.211 36.405 1.00 91.75 ? 100 PHE B CE2 1 +ATOM 3142 C CZ . PHE B 1 101 ? 13.453 81.536 35.703 1.00 105.24 ? 100 PHE B CZ 1 +ATOM 3143 N N . LYS B 1 102 ? 13.521 80.029 42.859 1.00 85.18 ? 101 LYS B N 1 +ATOM 3144 C CA . LYS B 1 102 ? 13.506 79.359 44.152 1.00 119.14 ? 101 LYS B CA 1 +ATOM 3145 C C . LYS B 1 102 ? 13.170 77.877 44.001 1.00 135.88 ? 101 LYS B C 1 +ATOM 3146 O O . LYS B 1 102 ? 12.259 77.515 43.245 1.00 78.68 ? 101 LYS B O 1 +ATOM 3147 C CB . LYS B 1 102 ? 12.535 80.037 45.113 1.00 85.92 ? 101 LYS B CB 1 +ATOM 3148 C CG . LYS B 1 102 ? 12.272 79.212 46.379 1.00 112.85 ? 101 LYS B CG 1 +ATOM 3149 C CD . LYS B 1 102 ? 11.182 79.830 47.233 1.00 130.21 ? 101 LYS B CD 1 +ATOM 3150 C CE . LYS B 1 102 ? 11.652 80.020 48.664 1.00 116.42 ? 101 LYS B CE 1 +ATOM 3151 N NZ . LYS B 1 102 ? 10.927 79.132 49.613 1.00 133.22 ? 101 LYS B NZ 1 +ATOM 3152 N N . ASP B 1 103 ? 13.921 77.042 44.725 1.00 113.00 ? 102 ASP B N 1 +ATOM 3153 C CA . ASP B 1 103 ? 13.778 75.583 44.716 1.00 114.19 ? 102 ASP B CA 1 +ATOM 3154 C C . ASP B 1 103 ? 14.143 74.999 43.357 1.00 105.95 ? 102 ASP B C 1 +ATOM 3155 O O . ASP B 1 103 ? 13.627 73.950 42.969 1.00 113.11 ? 102 ASP B O 1 +ATOM 3156 C CB . ASP B 1 103 ? 12.360 75.141 45.129 1.00 133.06 ? 102 ASP B CB 1 +ATOM 3157 C CG . ASP B 1 103 ? 12.064 75.397 46.604 1.00 147.27 ? 102 ASP B CG 1 +ATOM 3158 O OD1 . ASP B 1 103 ? 13.025 75.456 47.401 1.00 131.64 ? 102 ASP B OD1 1 +ATOM 3159 O OD2 . ASP B 1 103 ? 10.872 75.530 46.966 1.00 143.73 ? 102 ASP B OD2 1 +ATOM 3160 N N . ASP B 1 104 ? 15.040 75.671 42.642 1.00 96.98 ? 103 ASP B N 1 +ATOM 3161 C CA . ASP B 1 104 ? 15.260 75.335 41.243 1.00 95.55 ? 103 ASP B CA 1 +ATOM 3162 C C . ASP B 1 104 ? 16.508 75.968 40.618 1.00 100.98 ? 103 ASP B C 1 +ATOM 3163 O O . ASP B 1 104 ? 17.323 76.597 41.297 1.00 77.54 ? 103 ASP B O 1 +ATOM 3164 C CB . ASP B 1 104 ? 14.018 75.691 40.424 1.00 60.50 ? 103 ASP B CB 1 +ATOM 3165 C CG . ASP B 1 104 ? 14.132 75.277 38.984 1.00 124.78 ? 103 ASP B CG 1 +ATOM 3166 O OD1 . ASP B 1 104 ? 15.185 74.692 38.640 1.00 86.66 ? 103 ASP B OD1 1 +ATOM 3167 O OD2 . ASP B 1 104 ? 13.205 75.518 38.213 1.00 213.05 ? 103 ASP B OD2 1 +ATOM 3168 N N . GLY B 1 105 ? 16.640 75.792 39.304 1.00 99.65 ? 104 GLY B N 1 +ATOM 3169 C CA . GLY B 1 105 ? 17.832 76.118 38.561 1.00 85.91 ? 104 GLY B CA 1 +ATOM 3170 C C . GLY B 1 105 ? 18.118 77.600 38.458 1.00 97.27 ? 104 GLY B C 1 +ATOM 3171 O O . GLY B 1 105 ? 17.539 78.391 39.180 1.00 98.32 ? 104 GLY B O 1 +ATOM 3172 N N . ASN B 1 106 ? 19.014 77.990 37.564 1.00 82.24 ? 105 ASN B N 1 +ATOM 3173 C CA . ASN B 1 106 ? 19.316 79.405 37.413 1.00 82.96 ? 105 ASN B CA 1 +ATOM 3174 C C . ASN B 1 106 ? 19.729 79.791 35.996 1.00 106.02 ? 105 ASN B C 1 +ATOM 3175 O O . ASN B 1 106 ? 20.301 78.980 35.274 1.00 115.80 ? 105 ASN B O 1 +ATOM 3176 C CB . ASN B 1 106 ? 20.389 79.839 38.422 1.00 103.10 ? 105 ASN B CB 1 +ATOM 3177 C CG . ASN B 1 106 ? 21.693 79.063 38.275 1.00 96.36 ? 105 ASN B CG 1 +ATOM 3178 O OD1 . ASN B 1 106 ? 22.394 79.172 37.264 1.00 103.32 ? 105 ASN B OD1 1 +ATOM 3179 N ND2 . ASN B 1 106 ? 22.034 78.293 39.303 1.00 79.95 ? 105 ASN B ND2 1 +ATOM 3180 N N . TYR B 1 107 ? 19.428 81.027 35.604 1.00 85.86 ? 106 TYR B N 1 +ATOM 3181 C CA . TYR B 1 107 ? 19.921 81.582 34.346 1.00 93.51 ? 106 TYR B CA 1 +ATOM 3182 C C . TYR B 1 107 ? 21.115 82.516 34.594 1.00 99.28 ? 106 TYR B C 1 +ATOM 3183 O O . TYR B 1 107 ? 21.100 83.337 35.513 1.00 83.80 ? 106 TYR B O 1 +ATOM 3184 C CB . TYR B 1 107 ? 18.828 82.385 33.634 1.00 83.77 ? 106 TYR B CB 1 +ATOM 3185 C CG . TYR B 1 107 ? 17.601 81.626 33.167 1.00 88.41 ? 106 TYR B CG 1 +ATOM 3186 C CD1 . TYR B 1 107 ? 17.628 80.257 32.948 1.00 104.36 ? 106 TYR B CD1 1 +ATOM 3187 C CD2 . TYR B 1 107 ? 16.410 82.300 32.920 1.00 107.04 ? 106 TYR B CD2 1 +ATOM 3188 C CE1 . TYR B 1 107 ? 16.489 79.580 32.506 1.00 81.79 ? 106 TYR B CE1 1 +ATOM 3189 C CE2 . TYR B 1 107 ? 15.275 81.636 32.483 1.00 83.08 ? 106 TYR B CE2 1 +ATOM 3190 C CZ . TYR B 1 107 ? 15.319 80.279 32.279 1.00 94.33 ? 106 TYR B CZ 1 +ATOM 3191 O OH . TYR B 1 107 ? 14.186 79.628 31.847 1.00 81.97 ? 106 TYR B OH 1 +ATOM 3192 N N . LYS B 1 108 ? 22.149 82.404 33.771 1.00 83.38 ? 107 LYS B N 1 +ATOM 3193 C CA . LYS B 1 108 ? 23.228 83.381 33.816 1.00 89.67 ? 107 LYS B CA 1 +ATOM 3194 C C . LYS B 1 108 ? 23.376 84.009 32.441 1.00 96.08 ? 107 LYS B C 1 +ATOM 3195 O O . LYS B 1 108 ? 23.803 83.354 31.490 1.00 114.55 ? 107 LYS B O 1 +ATOM 3196 C CB . LYS B 1 108 ? 24.544 82.757 34.306 1.00 95.37 ? 107 LYS B CB 1 +ATOM 3197 C CG . LYS B 1 108 ? 24.607 82.548 35.824 1.00 93.80 ? 107 LYS B CG 1 +ATOM 3198 C CD . LYS B 1 108 ? 25.921 81.913 36.285 1.00 99.25 ? 107 LYS B CD 1 +ATOM 3199 C CE . LYS B 1 108 ? 26.037 81.873 37.819 1.00 111.40 ? 107 LYS B CE 1 +ATOM 3200 N NZ . LYS B 1 108 ? 26.176 83.240 38.421 1.00 106.27 ? 107 LYS B NZ 1 +ATOM 3201 N N . THR B 1 109 ? 22.996 85.281 32.344 1.00 94.63 ? 108 THR B N 1 +ATOM 3202 C CA . THR B 1 109 ? 22.955 85.977 31.063 1.00 102.70 ? 108 THR B CA 1 +ATOM 3203 C C . THR B 1 109 ? 24.018 87.051 30.928 1.00 99.23 ? 108 THR B C 1 +ATOM 3204 O O . THR B 1 109 ? 24.512 87.602 31.914 1.00 84.14 ? 108 THR B O 1 +ATOM 3205 C CB . THR B 1 109 ? 21.587 86.666 30.806 1.00 95.83 ? 108 THR B CB 1 +ATOM 3206 O OG1 . THR B 1 109 ? 21.469 87.844 31.619 1.00 86.28 ? 108 THR B OG1 1 +ATOM 3207 C CG2 . THR B 1 109 ? 20.425 85.713 31.075 1.00 105.64 ? 108 THR B CG2 1 +ATOM 3208 N N . ARG B 1 110 ? 24.369 87.330 29.681 1.00 76.83 ? 109 ARG B N 1 +ATOM 3209 C CA . ARG B 1 110 ? 25.108 88.528 29.346 1.00 91.13 ? 109 ARG B CA 1 +ATOM 3210 C C . ARG B 1 110 ? 24.582 89.030 28.022 1.00 97.11 ? 109 ARG B C 1 +ATOM 3211 O O . ARG B 1 110 ? 24.549 88.287 27.036 1.00 94.33 ? 109 ARG B O 1 +ATOM 3212 C CB . ARG B 1 110 ? 26.608 88.270 29.241 1.00 102.95 ? 109 ARG B CB 1 +ATOM 3213 C CG . ARG B 1 110 ? 27.382 89.507 28.820 1.00 117.92 ? 109 ARG B CG 1 +ATOM 3214 C CD . ARG B 1 110 ? 28.857 89.223 28.635 1.00 86.42 ? 109 ARG B CD 1 +ATOM 3215 N NE . ARG B 1 110 ? 29.623 90.451 28.429 1.00 115.33 ? 109 ARG B NE 1 +ATOM 3216 C CZ . ARG B 1 110 ? 29.817 91.029 27.247 1.00 120.96 ? 109 ARG B CZ 1 +ATOM 3217 N NH1 . ARG B 1 110 ? 29.302 90.493 26.146 1.00 124.62 ? 109 ARG B NH1 1 +ATOM 3218 N NH2 . ARG B 1 110 ? 30.530 92.145 27.163 1.00 108.03 ? 109 ARG B NH2 1 +ATOM 3219 N N . ALA B 1 111 ? 24.166 90.294 28.024 1.00 110.85 ? 110 ALA B N 1 +ATOM 3220 C CA . ALA B 1 111 ? 23.606 90.958 26.856 1.00 93.99 ? 110 ALA B CA 1 +ATOM 3221 C C . ALA B 1 111 ? 24.317 92.275 26.570 1.00 95.68 ? 110 ALA B C 1 +ATOM 3222 O O . ALA B 1 111 ? 24.670 93.011 27.492 1.00 87.52 ? 110 ALA B O 1 +ATOM 3223 C CB . ALA B 1 111 ? 22.125 91.205 27.059 1.00 105.59 ? 110 ALA B CB 1 +ATOM 3224 N N . GLU B 1 112 ? 24.537 92.554 25.288 1.00 76.43 ? 111 GLU B N 1 +ATOM 3225 C CA . GLU B 1 112 ? 25.005 93.863 24.845 1.00 108.71 ? 111 GLU B CA 1 +ATOM 3226 C C . GLU B 1 112 ? 23.849 94.610 24.175 1.00 119.01 ? 111 GLU B C 1 +ATOM 3227 O O . GLU B 1 112 ? 23.332 94.173 23.140 1.00 108.29 ? 111 GLU B O 1 +ATOM 3228 C CB . GLU B 1 112 ? 26.183 93.734 23.864 1.00 127.17 ? 111 GLU B CB 1 +ATOM 3229 C CG . GLU B 1 112 ? 27.516 93.284 24.476 1.00 160.26 ? 111 GLU B CG 1 +ATOM 3230 C CD . GLU B 1 112 ? 28.612 93.009 23.430 1.00 160.22 ? 111 GLU B CD 1 +ATOM 3231 O OE1 . GLU B 1 112 ? 28.457 93.400 22.250 1.00 133.41 ? 111 GLU B OE1 1 +ATOM 3232 O OE2 . GLU B 1 112 ? 29.637 92.394 23.799 1.00 150.19 ? 111 GLU B OE2 1 +ATOM 3233 N N . VAL B 1 113 ? 23.432 95.720 24.782 1.00 98.30 ? 112 VAL B N 1 +ATOM 3234 C CA . VAL B 1 113 ? 22.415 96.580 24.191 1.00 84.26 ? 112 VAL B CA 1 +ATOM 3235 C C . VAL B 1 113 ? 23.058 97.854 23.680 1.00 107.81 ? 112 VAL B C 1 +ATOM 3236 O O . VAL B 1 113 ? 23.730 98.562 24.432 1.00 103.11 ? 112 VAL B O 1 +ATOM 3237 C CB . VAL B 1 113 ? 21.323 96.989 25.189 1.00 69.01 ? 112 VAL B CB 1 +ATOM 3238 C CG1 . VAL B 1 113 ? 20.139 97.561 24.440 1.00 89.91 ? 112 VAL B CG1 1 +ATOM 3239 C CG2 . VAL B 1 113 ? 20.884 95.815 26.020 1.00 106.76 ? 112 VAL B CG2 1 +ATOM 3240 N N . LYS B 1 114 ? 22.841 98.134 22.397 1.00 90.50 ? 113 LYS B N 1 +ATOM 3241 C CA . LYS B 1 114 ? 23.391 99.312 21.739 1.00 97.99 ? 113 LYS B CA 1 +ATOM 3242 C C . LYS B 1 114 ? 22.670 99.584 20.419 1.00 111.05 ? 113 LYS B C 1 +ATOM 3243 O O . LYS B 1 114 ? 21.834 98.794 19.974 1.00 91.63 ? 113 LYS B O 1 +ATOM 3244 C CB . LYS B 1 114 ? 24.907 99.160 21.502 1.00 129.01 ? 113 LYS B CB 1 +ATOM 3245 C CG . LYS B 1 114 ? 25.322 97.923 20.679 1.00 123.14 ? 113 LYS B CG 1 +ATOM 3246 C CD . LYS B 1 114 ? 26.844 97.804 20.464 1.00 103.01 ? 113 LYS B CD 1 +ATOM 3247 C CE . LYS B 1 114 ? 27.190 96.674 19.483 1.00 126.91 ? 113 LYS B CE 1 +ATOM 3248 N NZ . LYS B 1 114 ? 26.787 95.313 19.956 1.00 115.80 ? 113 LYS B NZ 1 +ATOM 3249 N N . PHE B 1 115 ? 23.005 100.713 19.802 1.00 104.53 ? 114 PHE B N 1 +ATOM 3250 C CA . PHE B 1 115 ? 22.423 101.109 18.527 1.00 105.96 ? 114 PHE B CA 1 +ATOM 3251 C C . PHE B 1 115 ? 23.286 100.615 17.384 1.00 106.67 ? 114 PHE B C 1 +ATOM 3252 O O . PHE B 1 115 ? 24.511 100.691 17.454 1.00 111.86 ? 114 PHE B O 1 +ATOM 3253 C CB . PHE B 1 115 ? 22.325 102.636 18.428 1.00 118.97 ? 114 PHE B CB 1 +ATOM 3254 C CG . PHE B 1 115 ? 21.002 103.199 18.878 1.00 130.50 ? 114 PHE B CG 1 +ATOM 3255 C CD1 . PHE B 1 115 ? 19.921 103.256 18.004 1.00 116.65 ? 114 PHE B CD1 1 +ATOM 3256 C CD2 . PHE B 1 115 ? 20.842 103.685 20.170 1.00 109.87 ? 114 PHE B CD2 1 +ATOM 3257 C CE1 . PHE B 1 115 ? 18.703 103.777 18.411 1.00 96.31 ? 114 PHE B CE1 1 +ATOM 3258 C CE2 . PHE B 1 115 ? 19.628 104.208 20.588 1.00 96.88 ? 114 PHE B CE2 1 +ATOM 3259 C CZ . PHE B 1 115 ? 18.556 104.255 19.707 1.00 105.32 ? 114 PHE B CZ 1 +ATOM 3260 N N . GLU B 1 116 ? 22.641 100.121 16.332 1.00 98.11 ? 115 GLU B N 1 +ATOM 3261 C CA . GLU B 1 116 ? 23.329 99.783 15.091 1.00 98.32 ? 115 GLU B CA 1 +ATOM 3262 C C . GLU B 1 116 ? 22.653 100.522 13.946 1.00 102.56 ? 115 GLU B C 1 +ATOM 3263 O O . GLU B 1 116 ? 21.809 99.973 13.234 1.00 101.82 ? 115 GLU B O 1 +ATOM 3264 C CB . GLU B 1 116 ? 23.305 98.280 14.850 1.00 94.64 ? 115 GLU B CB 1 +ATOM 3265 C CG . GLU B 1 116 ? 23.768 97.482 16.039 1.00 115.81 ? 115 GLU B CG 1 +ATOM 3266 C CD . GLU B 1 116 ? 24.050 96.039 15.696 1.00 156.93 ? 115 GLU B CD 1 +ATOM 3267 O OE1 . GLU B 1 116 ? 23.444 95.530 14.725 1.00 159.42 ? 115 GLU B OE1 1 +ATOM 3268 O OE2 . GLU B 1 116 ? 24.885 95.422 16.399 1.00 133.94 ? 115 GLU B OE2 1 +ATOM 3269 N N . GLY B 1 117 ? 23.027 101.783 13.783 1.00 99.91 ? 116 GLY B N 1 +ATOM 3270 C CA . GLY B 1 117 ? 22.309 102.662 12.892 1.00 82.45 ? 116 GLY B CA 1 +ATOM 3271 C C . GLY B 1 117 ? 21.069 103.154 13.603 1.00 114.74 ? 116 GLY B C 1 +ATOM 3272 O O . GLY B 1 117 ? 21.153 103.709 14.703 1.00 105.76 ? 116 GLY B O 1 +ATOM 3273 N N . ASP B 1 118 ? 19.914 102.929 12.984 1.00 138.13 ? 117 ASP B N 1 +ATOM 3274 C CA . ASP B 1 118 ? 18.646 103.443 13.493 1.00 126.51 ? 117 ASP B CA 1 +ATOM 3275 C C . ASP B 1 118 ? 17.977 102.471 14.454 1.00 117.86 ? 117 ASP B C 1 +ATOM 3276 O O . ASP B 1 118 ? 17.055 102.839 15.176 1.00 116.31 ? 117 ASP B O 1 +ATOM 3277 C CB . ASP B 1 118 ? 17.688 103.791 12.337 1.00 125.39 ? 117 ASP B CB 1 +ATOM 3278 C CG . ASP B 1 118 ? 17.223 102.555 11.540 1.00 158.66 ? 117 ASP B CG 1 +ATOM 3279 O OD1 . ASP B 1 118 ? 18.046 101.644 11.292 1.00 147.93 ? 117 ASP B OD1 1 +ATOM 3280 O OD2 . ASP B 1 118 ? 16.029 102.503 11.150 1.00 145.08 ? 117 ASP B OD2 1 +ATOM 3281 N N . THR B 1 119 ? 18.442 101.229 14.466 1.00 114.55 ? 118 THR B N 1 +ATOM 3282 C CA . THR B 1 119 ? 17.785 100.198 15.257 1.00 102.01 ? 118 THR B CA 1 +ATOM 3283 C C . THR B 1 119 ? 18.500 99.993 16.602 1.00 87.73 ? 118 THR B C 1 +ATOM 3284 O O . THR B 1 119 ? 19.704 100.218 16.709 1.00 96.05 ? 118 THR B O 1 +ATOM 3285 C CB . THR B 1 119 ? 17.629 98.886 14.434 1.00 81.83 ? 118 THR B CB 1 +ATOM 3286 O OG1 . THR B 1 119 ? 16.793 99.136 13.292 1.00 100.92 ? 118 THR B OG1 1 +ATOM 3287 C CG2 . THR B 1 119 ? 16.998 97.782 15.256 1.00 100.85 ? 118 THR B CG2 1 +ATOM 3288 N N . LEU B 1 120 ? 17.741 99.623 17.634 1.00 87.05 ? 119 LEU B N 1 +ATOM 3289 C CA . LEU B 1 120 ? 18.288 99.362 18.966 1.00 71.86 ? 119 LEU B CA 1 +ATOM 3290 C C . LEU B 1 120 ? 18.293 97.868 19.207 1.00 101.74 ? 119 LEU B C 1 +ATOM 3291 O O . LEU B 1 120 ? 17.230 97.258 19.332 1.00 88.94 ? 119 LEU B O 1 +ATOM 3292 C CB . LEU B 1 120 ? 17.440 100.053 20.038 1.00 77.66 ? 119 LEU B CB 1 +ATOM 3293 C CG . LEU B 1 120 ? 17.875 100.104 21.509 1.00 61.52 ? 119 LEU B CG 1 +ATOM 3294 C CD1 . LEU B 1 120 ? 17.407 101.376 22.160 1.00 152.89 ? 119 LEU B CD1 1 +ATOM 3295 C CD2 . LEU B 1 120 ? 17.363 98.900 22.269 1.00 72.86 ? 119 LEU B CD2 1 +ATOM 3296 N N . VAL B 1 121 ? 19.482 97.278 19.280 1.00 84.15 ? 120 VAL B N 1 +ATOM 3297 C CA . VAL B 1 121 ? 19.580 95.829 19.377 1.00 83.79 ? 120 VAL B CA 1 +ATOM 3298 C C . VAL B 1 121 ? 20.013 95.303 20.750 1.00 102.89 ? 120 VAL B C 1 +ATOM 3299 O O . VAL B 1 121 ? 20.909 95.845 21.407 1.00 80.40 ? 120 VAL B O 1 +ATOM 3300 C CB . VAL B 1 121 ? 20.469 95.222 18.261 1.00 91.22 ? 120 VAL B CB 1 +ATOM 3301 C CG1 . VAL B 1 121 ? 20.096 95.794 16.903 1.00 79.25 ? 120 VAL B CG1 1 +ATOM 3302 C CG2 . VAL B 1 121 ? 21.932 95.471 18.544 1.00 120.83 ? 120 VAL B CG2 1 +ATOM 3303 N N . ASN B 1 122 ? 19.336 94.239 21.167 1.00 87.80 ? 121 ASN B N 1 +ATOM 3304 C CA . ASN B 1 122 ? 19.680 93.497 22.362 1.00 93.31 ? 121 ASN B CA 1 +ATOM 3305 C C . ASN B 1 122 ? 20.152 92.111 21.935 1.00 108.70 ? 121 ASN B C 1 +ATOM 3306 O O . ASN B 1 122 ? 19.362 91.304 21.432 1.00 87.82 ? 121 ASN B O 1 +ATOM 3307 C CB . ASN B 1 122 ? 18.457 93.389 23.270 1.00 73.55 ? 121 ASN B CB 1 +ATOM 3308 C CG . ASN B 1 122 ? 18.802 92.928 24.666 1.00 83.42 ? 121 ASN B CG 1 +ATOM 3309 O OD1 . ASN B 1 122 ? 19.942 93.046 25.111 1.00 126.68 ? 121 ASN B OD1 1 +ATOM 3310 N ND2 . ASN B 1 122 ? 17.812 92.400 25.372 1.00 85.91 ? 121 ASN B ND2 1 +ATOM 3311 N N . ARG B 1 123 ? 21.451 91.865 22.107 1.00 99.98 ? 122 ARG B N 1 +ATOM 3312 C CA . ARG B 1 123 ? 22.084 90.588 21.772 1.00 88.85 ? 122 ARG B CA 1 +ATOM 3313 C C . ARG B 1 123 ? 22.428 89.784 23.027 1.00 106.65 ? 122 ARG B C 1 +ATOM 3314 O O . ARG B 1 123 ? 23.198 90.235 23.874 1.00 78.71 ? 122 ARG B O 1 +ATOM 3315 C CB . ARG B 1 123 ? 23.353 90.815 20.945 1.00 90.98 ? 122 ARG B CB 1 +ATOM 3316 C CG . ARG B 1 123 ? 23.103 91.190 19.496 1.00 97.04 ? 122 ARG B CG 1 +ATOM 3317 C CD . ARG B 1 123 ? 24.389 91.188 18.674 1.00 99.30 ? 122 ARG B CD 1 +ATOM 3318 N NE . ARG B 1 123 ? 24.233 91.982 17.459 1.00 103.63 ? 122 ARG B NE 1 +ATOM 3319 C CZ . ARG B 1 123 ? 23.593 91.565 16.372 1.00 121.09 ? 122 ARG B CZ 1 +ATOM 3320 N NH1 . ARG B 1 123 ? 23.047 90.355 16.336 1.00 110.93 ? 122 ARG B NH1 1 +ATOM 3321 N NH2 . ARG B 1 123 ? 23.493 92.362 15.318 1.00 109.30 ? 122 ARG B NH2 1 +ATOM 3322 N N . ILE B 1 124 ? 21.877 88.576 23.123 1.00 106.32 ? 123 ILE B N 1 +ATOM 3323 C CA . ILE B 1 124 ? 21.870 87.828 24.378 1.00 92.04 ? 123 ILE B CA 1 +ATOM 3324 C C . ILE B 1 124 ? 22.438 86.397 24.267 1.00 104.12 ? 123 ILE B C 1 +ATOM 3325 O O . ILE B 1 124 ? 22.118 85.667 23.325 1.00 81.09 ? 123 ILE B O 1 +ATOM 3326 C CB . ILE B 1 124 ? 20.421 87.780 24.956 1.00 117.52 ? 123 ILE B CB 1 +ATOM 3327 C CG1 . ILE B 1 124 ? 19.669 89.087 24.713 1.00 94.71 ? 123 ILE B CG1 1 +ATOM 3328 C CG2 . ILE B 1 124 ? 20.421 87.416 26.447 1.00 89.18 ? 123 ILE B CG2 1 +ATOM 3329 C CD1 . ILE B 1 124 ? 18.182 89.037 25.030 1.00 106.31 ? 123 ILE B CD1 1 +ATOM 3330 N N . GLU B 1 125 ? 23.289 86.025 25.229 1.00 91.95 ? 124 GLU B N 1 +ATOM 3331 C CA . GLU B 1 125 ? 23.683 84.630 25.480 1.00 87.69 ? 124 GLU B CA 1 +ATOM 3332 C C . GLU B 1 125 ? 23.172 84.222 26.871 1.00 81.84 ? 124 GLU B C 1 +ATOM 3333 O O . GLU B 1 125 ? 23.440 84.924 27.847 1.00 107.97 ? 124 GLU B O 1 +ATOM 3334 C CB . GLU B 1 125 ? 25.212 84.476 25.447 1.00 97.13 ? 124 GLU B CB 1 +ATOM 3335 C CG . GLU B 1 125 ? 25.893 84.969 24.174 1.00 138.63 ? 124 GLU B CG 1 +ATOM 3336 C CD . GLU B 1 125 ? 27.404 85.167 24.330 1.00 162.51 ? 124 GLU B CD 1 +ATOM 3337 O OE1 . GLU B 1 125 ? 27.870 85.524 25.434 1.00 176.40 ? 124 GLU B OE1 1 +ATOM 3338 O OE2 . GLU B 1 125 ? 28.128 84.971 23.334 1.00 150.73 ? 124 GLU B OE2 1 +ATOM 3339 N N . LEU B 1 126 ? 22.446 83.104 26.968 1.00 76.95 ? 125 LEU B N 1 +ATOM 3340 C CA . LEU B 1 126 ? 21.876 82.633 28.251 1.00 96.02 ? 125 LEU B CA 1 +ATOM 3341 C C . LEU B 1 126 ? 22.241 81.179 28.586 1.00 95.03 ? 125 LEU B C 1 +ATOM 3342 O O . LEU B 1 126 ? 22.192 80.312 27.716 1.00 109.35 ? 125 LEU B O 1 +ATOM 3343 C CB . LEU B 1 126 ? 20.347 82.804 28.260 1.00 91.55 ? 125 LEU B CB 1 +ATOM 3344 C CG . LEU B 1 126 ? 19.460 82.060 29.275 1.00 74.95 ? 125 LEU B CG 1 +ATOM 3345 C CD1 . LEU B 1 126 ? 18.293 82.923 29.663 1.00 86.04 ? 125 LEU B CD1 1 +ATOM 3346 C CD2 . LEU B 1 126 ? 18.918 80.747 28.732 1.00 99.82 ? 125 LEU B CD2 1 +ATOM 3347 N N . LYS B 1 127 ? 22.580 80.911 29.849 1.00 100.10 ? 126 LYS B N 1 +ATOM 3348 C CA . LYS B 1 127 ? 23.037 79.572 30.258 1.00 82.48 ? 126 LYS B CA 1 +ATOM 3349 C C . LYS B 1 127 ? 22.425 79.018 31.566 1.00 92.55 ? 126 LYS B C 1 +ATOM 3350 O O . LYS B 1 127 ? 22.867 79.353 32.664 1.00 110.78 ? 126 LYS B O 1 +ATOM 3351 C CB . LYS B 1 127 ? 24.571 79.538 30.339 1.00 104.61 ? 126 LYS B CB 1 +ATOM 3352 C CG . LYS B 1 127 ? 25.145 78.140 30.520 1.00 126.43 ? 126 LYS B CG 1 +ATOM 3353 C CD . LYS B 1 127 ? 26.668 78.117 30.534 1.00 137.24 ? 126 LYS B CD 1 +ATOM 3354 C CE . LYS B 1 127 ? 27.169 76.773 31.039 1.00 129.15 ? 126 LYS B CE 1 +ATOM 3355 N NZ . LYS B 1 127 ? 26.164 75.710 30.752 1.00 133.65 ? 126 LYS B NZ 1 +ATOM 3356 N N . GLY B 1 128 ? 21.433 78.138 31.438 1.00 98.64 ? 127 GLY B N 1 +ATOM 3357 C CA . GLY B 1 128 ? 20.745 77.577 32.594 1.00 89.50 ? 127 GLY B CA 1 +ATOM 3358 C C . GLY B 1 128 ? 21.179 76.184 33.043 1.00 125.22 ? 127 GLY B C 1 +ATOM 3359 O O . GLY B 1 128 ? 21.253 75.263 32.228 1.00 138.59 ? 127 GLY B O 1 +ATOM 3360 N N . ILE B 1 129 ? 21.453 76.037 34.343 1.00 126.37 ? 128 ILE B N 1 +ATOM 3361 C CA . ILE B 1 129 ? 21.885 74.766 34.950 1.00 106.07 ? 128 ILE B CA 1 +ATOM 3362 C C . ILE B 1 129 ? 21.080 74.465 36.208 1.00 89.66 ? 128 ILE B C 1 +ATOM 3363 O O . ILE B 1 129 ? 20.555 75.377 36.830 1.00 109.86 ? 128 ILE B O 1 +ATOM 3364 C CB . ILE B 1 129 ? 23.392 74.790 35.358 1.00 95.14 ? 128 ILE B CB 1 +ATOM 3365 C CG1 . ILE B 1 129 ? 24.298 74.903 34.122 1.00 140.68 ? 128 ILE B CG1 1 +ATOM 3366 C CG2 . ILE B 1 129 ? 23.764 73.577 36.237 1.00 163.22 ? 128 ILE B CG2 1 +ATOM 3367 C CD1 . ILE B 1 129 ? 24.832 76.313 33.843 1.00 132.15 ? 128 ILE B CD1 1 +ATOM 3368 N N . ASP B 1 130 ? 20.978 73.187 36.571 1.00 120.79 ? 129 ASP B N 1 +ATOM 3369 C CA . ASP B 1 130 ? 20.422 72.746 37.857 1.00 122.48 ? 129 ASP B CA 1 +ATOM 3370 C C . ASP B 1 130 ? 18.894 72.743 37.924 1.00 85.64 ? 129 ASP B C 1 +ATOM 3371 O O . ASP B 1 130 ? 18.318 72.769 39.003 1.00 83.09 ? 129 ASP B O 1 +ATOM 3372 C CB . ASP B 1 130 ? 20.999 73.531 39.058 1.00 120.71 ? 129 ASP B CB 1 +ATOM 3373 C CG . ASP B 1 130 ? 22.482 73.270 39.288 1.00 130.34 ? 129 ASP B CG 1 +ATOM 3374 O OD1 . ASP B 1 130 ? 22.887 72.088 39.312 1.00 123.35 ? 129 ASP B OD1 1 +ATOM 3375 O OD2 . ASP B 1 130 ? 23.245 74.252 39.441 1.00 128.75 ? 129 ASP B OD2 1 +ATOM 3376 N N . PHE B 1 131 ? 18.218 72.687 36.789 1.00 78.64 ? 130 PHE B N 1 +ATOM 3377 C CA . PHE B 1 131 ? 16.766 72.637 36.869 1.00 113.59 ? 130 PHE B CA 1 +ATOM 3378 C C . PHE B 1 131 ? 16.301 71.210 37.171 1.00 75.63 ? 130 PHE B C 1 +ATOM 3379 O O . PHE B 1 131 ? 17.094 70.283 37.125 1.00 108.65 ? 130 PHE B O 1 +ATOM 3380 C CB . PHE B 1 131 ? 16.123 73.257 35.618 1.00 110.23 ? 130 PHE B CB 1 +ATOM 3381 C CG . PHE B 1 131 ? 16.274 74.759 35.553 1.00 91.28 ? 130 PHE B CG 1 +ATOM 3382 C CD1 . PHE B 1 131 ? 17.462 75.336 35.115 1.00 98.36 ? 130 PHE B CD1 1 +ATOM 3383 C CD2 . PHE B 1 131 ? 15.247 75.590 35.968 1.00 90.27 ? 130 PHE B CD2 1 +ATOM 3384 C CE1 . PHE B 1 131 ? 17.616 76.707 35.081 1.00 65.43 ? 130 PHE B CE1 1 +ATOM 3385 C CE2 . PHE B 1 131 ? 15.391 76.959 35.940 1.00 83.53 ? 130 PHE B CE2 1 +ATOM 3386 C CZ . PHE B 1 131 ? 16.580 77.520 35.493 1.00 116.99 ? 130 PHE B CZ 1 +ATOM 3387 N N . LYS B 1 132 ? 15.032 71.041 37.521 1.00 91.96 ? 131 LYS B N 1 +ATOM 3388 C CA . LYS B 1 132 ? 14.489 69.717 37.812 1.00 94.77 ? 131 LYS B CA 1 +ATOM 3389 C C . LYS B 1 132 ? 13.606 69.225 36.673 1.00 93.44 ? 131 LYS B C 1 +ATOM 3390 O O . LYS B 1 132 ? 12.606 69.860 36.364 1.00 159.86 ? 131 LYS B O 1 +ATOM 3391 C CB . LYS B 1 132 ? 13.634 69.764 39.080 1.00 73.07 ? 131 LYS B CB 1 +ATOM 3392 C CG . LYS B 1 132 ? 14.289 70.418 40.283 1.00 88.52 ? 131 LYS B CG 1 +ATOM 3393 C CD . LYS B 1 132 ? 13.343 70.406 41.477 1.00 105.28 ? 131 LYS B CD 1 +ATOM 3394 C CE . LYS B 1 132 ? 14.045 70.839 42.750 1.00 120.89 ? 131 LYS B CE 1 +ATOM 3395 N NZ . LYS B 1 132 ? 13.061 71.051 43.856 1.00 127.16 ? 131 LYS B NZ 1 +ATOM 3396 N N . GLU B 1 133 ? 13.932 68.074 36.088 1.00 114.38 ? 132 GLU B N 1 +ATOM 3397 C CA . GLU B 1 133 ? 13.152 67.526 34.966 1.00 139.24 ? 132 GLU B CA 1 +ATOM 3398 C C . GLU B 1 133 ? 11.635 67.394 35.235 1.00 122.77 ? 132 GLU B C 1 +ATOM 3399 O O . GLU B 1 133 ? 10.870 67.092 34.325 1.00 118.57 ? 132 GLU B O 1 +ATOM 3400 C CB . GLU B 1 133 ? 13.743 66.189 34.461 1.00 100.90 ? 132 GLU B CB 1 +ATOM 3401 C CG . GLU B 1 133 ? 15.037 66.300 33.594 1.00 209.57 ? 132 GLU B CG 1 +ATOM 3402 C CD . GLU B 1 133 ? 14.811 66.702 32.109 1.00 188.28 ? 132 GLU B CD 1 +ATOM 3403 O OE1 . GLU B 1 133 ? 13.837 66.230 31.473 1.00 182.23 ? 132 GLU B OE1 1 +ATOM 3404 O OE2 . GLU B 1 133 ? 15.631 67.487 31.571 1.00 139.70 ? 132 GLU B OE2 1 +ATOM 3405 N N . ASP B 1 134 ? 11.206 67.631 36.470 1.00 99.69 ? 133 ASP B N 1 +ATOM 3406 C CA . ASP B 1 134 ? 9.785 67.626 36.815 1.00 101.82 ? 133 ASP B CA 1 +ATOM 3407 C C . ASP B 1 134 ? 9.391 68.937 37.491 1.00 129.25 ? 133 ASP B C 1 +ATOM 3408 O O . ASP B 1 134 ? 8.297 69.052 38.053 1.00 122.90 ? 133 ASP B O 1 +ATOM 3409 C CB . ASP B 1 134 ? 9.480 66.464 37.759 1.00 166.71 ? 133 ASP B CB 1 +ATOM 3410 C CG . ASP B 1 134 ? 10.397 66.448 38.977 1.00 189.04 ? 133 ASP B CG 1 +ATOM 3411 O OD1 . ASP B 1 134 ? 11.626 66.613 38.803 1.00 180.32 ? 133 ASP B OD1 1 +ATOM 3412 O OD2 . ASP B 1 134 ? 9.889 66.285 40.108 1.00 201.82 ? 133 ASP B OD2 1 +ATOM 3413 N N . GLY B 1 135 ? 10.295 69.915 37.436 1.00 142.51 ? 134 GLY B N 1 +ATOM 3414 C CA . GLY B 1 135 ? 10.101 71.178 38.123 1.00 129.18 ? 134 GLY B CA 1 +ATOM 3415 C C . GLY B 1 135 ? 9.018 72.075 37.534 1.00 137.00 ? 134 GLY B C 1 +ATOM 3416 O O . GLY B 1 135 ? 8.192 71.615 36.746 1.00 134.01 ? 134 GLY B O 1 +ATOM 3417 N N . ASN B 1 136 ? 9.005 73.346 37.936 1.00 133.72 ? 135 ASN B N 1 +ATOM 3418 C CA . ASN B 1 136 ? 8.018 74.291 37.415 1.00 75.09 ? 135 ASN B CA 1 +ATOM 3419 C C . ASN B 1 136 ? 8.371 74.761 35.998 1.00 107.96 ? 135 ASN B C 1 +ATOM 3420 O O . ASN B 1 136 ? 7.498 74.884 35.136 1.00 92.03 ? 135 ASN B O 1 +ATOM 3421 C CB . ASN B 1 136 ? 7.838 75.485 38.358 1.00 84.01 ? 135 ASN B CB 1 +ATOM 3422 C CG . ASN B 1 136 ? 6.834 75.214 39.477 1.00 101.66 ? 135 ASN B CG 1 +ATOM 3423 O OD1 . ASN B 1 136 ? 5.968 74.340 39.369 1.00 78.26 ? 135 ASN B OD1 1 +ATOM 3424 N ND2 . ASN B 1 136 ? 6.944 75.980 40.555 1.00 87.06 ? 135 ASN B ND2 1 +ATOM 3425 N N . ILE B 1 137 ? 9.656 75.006 35.762 1.00 94.14 ? 136 ILE B N 1 +ATOM 3426 C CA . ILE B 1 137 ? 10.153 75.384 34.437 1.00 107.47 ? 136 ILE B CA 1 +ATOM 3427 C C . ILE B 1 137 ? 10.087 74.227 33.427 1.00 118.63 ? 136 ILE B C 1 +ATOM 3428 O O . ILE B 1 137 ? 9.237 74.222 32.530 1.00 84.20 ? 136 ILE B O 1 +ATOM 3429 C CB . ILE B 1 137 ? 11.609 75.928 34.492 1.00 93.09 ? 136 ILE B CB 1 +ATOM 3430 C CG1 . ILE B 1 137 ? 11.679 77.256 35.251 1.00 66.60 ? 136 ILE B CG1 1 +ATOM 3431 C CG2 . ILE B 1 137 ? 12.172 76.127 33.084 1.00 60.18 ? 136 ILE B CG2 1 +ATOM 3432 C CD1 . ILE B 1 137 ? 11.585 77.150 36.743 1.00 94.61 ? 136 ILE B CD1 1 +ATOM 3433 N N . LEU B 1 138 ? 10.975 73.246 33.592 1.00 101.79 ? 137 LEU B N 1 +ATOM 3434 C CA . LEU B 1 138 ? 11.149 72.177 32.610 1.00 102.80 ? 137 LEU B CA 1 +ATOM 3435 C C . LEU B 1 138 ? 9.940 71.285 32.488 1.00 109.46 ? 137 LEU B C 1 +ATOM 3436 O O . LEU B 1 138 ? 9.817 70.526 31.530 1.00 79.48 ? 137 LEU B O 1 +ATOM 3437 C CB . LEU B 1 138 ? 12.360 71.330 32.954 1.00 82.03 ? 137 LEU B CB 1 +ATOM 3438 C CG . LEU B 1 138 ? 13.662 72.058 32.676 1.00 102.39 ? 137 LEU B CG 1 +ATOM 3439 C CD1 . LEU B 1 138 ? 14.795 71.194 33.142 1.00 123.66 ? 137 LEU B CD1 1 +ATOM 3440 C CD2 . LEU B 1 138 ? 13.784 72.374 31.188 1.00 67.49 ? 137 LEU B CD2 1 +ATOM 3441 N N . GLY B 1 139 ? 9.053 71.373 33.470 1.00 85.32 ? 138 GLY B N 1 +ATOM 3442 C CA . GLY B 1 139 ? 7.800 70.651 33.414 1.00 102.19 ? 138 GLY B CA 1 +ATOM 3443 C C . GLY B 1 139 ? 6.714 71.460 32.733 1.00 113.52 ? 138 GLY B C 1 +ATOM 3444 O O . GLY B 1 139 ? 5.659 70.917 32.395 1.00 108.93 ? 138 GLY B O 1 +ATOM 3445 N N . HIS B 1 140 ? 6.981 72.755 32.539 1.00 112.38 ? 139 HIS B N 1 +ATOM 3446 C CA . HIS B 1 140 ? 6.031 73.700 31.939 1.00 104.98 ? 139 HIS B CA 1 +ATOM 3447 C C . HIS B 1 140 ? 4.714 73.833 32.741 1.00 86.68 ? 139 HIS B C 1 +ATOM 3448 O O . HIS B 1 140 ? 3.635 73.462 32.273 1.00 89.23 ? 139 HIS B O 1 +ATOM 3449 C CB . HIS B 1 140 ? 5.786 73.380 30.448 1.00 100.34 ? 139 HIS B CB 1 +ATOM 3450 C CG . HIS B 1 140 ? 6.949 73.709 29.555 1.00 106.83 ? 139 HIS B CG 1 +ATOM 3451 N ND1 . HIS B 1 140 ? 7.566 72.792 28.763 1.00 103.85 ? 139 HIS B ND1 1 +ATOM 3452 C CD2 . HIS B 1 140 ? 7.601 74.859 29.322 1.00 140.84 ? 139 HIS B CD2 1 +ATOM 3453 C CE1 . HIS B 1 140 ? 8.552 73.351 28.087 1.00 81.65 ? 139 HIS B CE1 1 +ATOM 3454 N NE2 . HIS B 1 140 ? 8.596 74.611 28.410 1.00 110.23 ? 139 HIS B NE2 1 +ATOM 3455 N N . LYS B 1 141 ? 4.823 74.371 33.956 1.00 109.14 ? 140 LYS B N 1 +ATOM 3456 C CA . LYS B 1 141 ? 3.661 74.604 34.820 1.00 113.40 ? 140 LYS B CA 1 +ATOM 3457 C C . LYS B 1 141 ? 3.463 76.093 35.106 1.00 115.33 ? 140 LYS B C 1 +ATOM 3458 O O . LYS B 1 141 ? 2.715 76.475 36.007 1.00 94.27 ? 140 LYS B O 1 +ATOM 3459 C CB . LYS B 1 141 ? 3.780 73.834 36.140 1.00 112.31 ? 140 LYS B CB 1 +ATOM 3460 C CG . LYS B 1 141 ? 3.723 72.324 36.014 1.00 109.62 ? 140 LYS B CG 1 +ATOM 3461 C CD . LYS B 1 141 ? 4.477 71.683 37.170 1.00 128.99 ? 140 LYS B CD 1 +ATOM 3462 C CE . LYS B 1 141 ? 4.662 70.182 36.982 1.00 131.57 ? 140 LYS B CE 1 +ATOM 3463 N NZ . LYS B 1 141 ? 5.480 69.561 38.069 1.00 135.65 ? 140 LYS B NZ 1 +ATOM 3464 N N . LEU B 1 142 ? 4.142 76.933 34.337 1.00 91.80 ? 141 LEU B N 1 +ATOM 3465 C CA . LEU B 1 142 ? 3.873 78.357 34.385 1.00 95.73 ? 141 LEU B CA 1 +ATOM 3466 C C . LEU B 1 142 ? 2.641 78.687 33.546 1.00 101.57 ? 141 LEU B C 1 +ATOM 3467 O O . LEU B 1 142 ? 2.444 78.129 32.459 1.00 87.80 ? 141 LEU B O 1 +ATOM 3468 C CB . LEU B 1 142 ? 5.084 79.148 33.899 1.00 96.91 ? 141 LEU B CB 1 +ATOM 3469 C CG . LEU B 1 142 ? 6.338 79.033 34.771 1.00 59.19 ? 141 LEU B CG 1 +ATOM 3470 C CD1 . LEU B 1 142 ? 7.520 79.735 34.141 1.00 76.38 ? 141 LEU B CD1 1 +ATOM 3471 C CD2 . LEU B 1 142 ? 6.085 79.576 36.149 1.00 81.56 ? 141 LEU B CD2 1 +ATOM 3472 N N . GLU B 1 143 ? 1.803 79.573 34.084 1.00 86.80 ? 142 GLU B N 1 +ATOM 3473 C CA . GLU B 1 143 ? 0.655 80.114 33.372 1.00 86.10 ? 142 GLU B CA 1 +ATOM 3474 C C . GLU B 1 143 ? 1.159 81.165 32.399 1.00 97.59 ? 142 GLU B C 1 +ATOM 3475 O O . GLU B 1 143 ? 2.086 81.919 32.718 1.00 99.59 ? 142 GLU B O 1 +ATOM 3476 C CB . GLU B 1 143 ? -0.332 80.762 34.347 1.00 83.01 ? 142 GLU B CB 1 +ATOM 3477 C CG . GLU B 1 143 ? -1.321 79.815 35.023 1.00 81.35 ? 142 GLU B CG 1 +ATOM 3478 C CD . GLU B 1 143 ? -2.377 80.552 35.856 1.00 118.82 ? 142 GLU B CD 1 +ATOM 3479 O OE1 . GLU B 1 143 ? -2.147 81.726 36.233 1.00 118.23 ? 142 GLU B OE1 1 +ATOM 3480 O OE2 . GLU B 1 143 ? -3.443 79.957 36.129 1.00 111.25 ? 142 GLU B OE2 1 +ATOM 3481 N N . TYR B 1 144 ? 0.557 81.211 31.215 1.00 76.63 ? 143 TYR B N 1 +ATOM 3482 C CA . TYR B 1 144 ? 0.947 82.184 30.198 1.00 72.78 ? 143 TYR B CA 1 +ATOM 3483 C C . TYR B 1 144 ? 0.552 83.622 30.549 1.00 88.10 ? 143 TYR B C 1 +ATOM 3484 O O . TYR B 1 144 ? -0.270 84.234 29.863 1.00 76.43 ? 143 TYR B O 1 +ATOM 3485 C CB . TYR B 1 144 ? 0.353 81.826 28.832 1.00 67.83 ? 143 TYR B CB 1 +ATOM 3486 C CG . TYR B 1 144 ? 1.058 82.529 27.690 1.00 70.70 ? 143 TYR B CG 1 +ATOM 3487 C CD1 . TYR B 1 144 ? 2.385 82.919 27.811 1.00 98.72 ? 143 TYR B CD1 1 +ATOM 3488 C CD2 . TYR B 1 144 ? 0.403 82.814 26.506 1.00 75.06 ? 143 TYR B CD2 1 +ATOM 3489 C CE1 . TYR B 1 144 ? 3.043 83.556 26.791 1.00 73.34 ? 143 TYR B CE1 1 +ATOM 3490 C CE2 . TYR B 1 144 ? 1.055 83.462 25.479 1.00 80.97 ? 143 TYR B CE2 1 +ATOM 3491 C CZ . TYR B 1 144 ? 2.377 83.828 25.629 1.00 90.00 ? 143 TYR B CZ 1 +ATOM 3492 O OH . TYR B 1 144 ? 3.049 84.463 24.613 1.00 75.22 ? 143 TYR B OH 1 +ATOM 3493 N N . ASN B 1 145 ? 1.140 84.168 31.604 1.00 68.75 ? 144 ASN B N 1 +ATOM 3494 C CA . ASN B 1 145 ? 0.825 85.537 31.985 1.00 74.14 ? 144 ASN B CA 1 +ATOM 3495 C C . ASN B 1 145 ? 1.946 86.258 32.722 1.00 59.78 ? 144 ASN B C 1 +ATOM 3496 O O . ASN B 1 145 ? 3.072 85.779 32.782 1.00 74.38 ? 144 ASN B O 1 +ATOM 3497 C CB . ASN B 1 145 ? -0.472 85.592 32.786 1.00 44.93 ? 144 ASN B CB 1 +ATOM 3498 C CG . ASN B 1 145 ? -0.426 84.751 34.034 1.00 106.54 ? 144 ASN B CG 1 +ATOM 3499 O OD1 . ASN B 1 145 ? 0.445 84.917 34.895 1.00 69.79 ? 144 ASN B OD1 1 +ATOM 3500 N ND2 . ASN B 1 145 ? -1.392 83.858 34.161 1.00 97.19 ? 144 ASN B ND2 1 +ATOM 3501 N N . TYR B 1 146 ? 1.631 87.425 33.262 1.00 65.56 ? 145 TYR B N 1 +ATOM 3502 C CA . TYR B 1 146 ? 2.632 88.206 33.966 1.00 91.73 ? 145 TYR B CA 1 +ATOM 3503 C C . TYR B 1 146 ? 2.008 89.089 35.047 1.00 82.26 ? 145 TYR B C 1 +ATOM 3504 O O . TYR B 1 146 ? 0.790 89.284 35.066 1.00 79.28 ? 145 TYR B O 1 +ATOM 3505 C CB . TYR B 1 146 ? 3.449 89.019 32.970 1.00 50.00 ? 145 TYR B CB 1 +ATOM 3506 C CG . TYR B 1 146 ? 4.927 88.888 33.190 1.00 75.86 ? 145 TYR B CG 1 +ATOM 3507 C CD1 . TYR B 1 146 ? 5.587 87.690 32.947 1.00 78.63 ? 145 TYR B CD1 1 +ATOM 3508 C CD2 . TYR B 1 146 ? 5.667 89.960 33.646 1.00 101.19 ? 145 TYR B CD2 1 +ATOM 3509 C CE1 . TYR B 1 146 ? 6.956 87.572 33.159 1.00 89.23 ? 145 TYR B CE1 1 +ATOM 3510 C CE2 . TYR B 1 146 ? 7.026 89.855 33.859 1.00 79.76 ? 145 TYR B CE2 1 +ATOM 3511 C CZ . TYR B 1 146 ? 7.666 88.667 33.616 1.00 75.71 ? 145 TYR B CZ 1 +ATOM 3512 O OH . TYR B 1 146 ? 9.017 88.597 33.836 1.00 78.55 ? 145 TYR B OH 1 +ATOM 3513 N N . ASN B 1 147 ? 2.845 89.571 35.967 1.00 91.60 ? 146 ASN B N 1 +ATOM 3514 C CA . ASN B 1 147 ? 2.422 90.438 37.067 1.00 81.54 ? 146 ASN B CA 1 +ATOM 3515 C C . ASN B 1 147 ? 3.303 91.656 37.030 1.00 86.54 ? 146 ASN B C 1 +ATOM 3516 O O . ASN B 1 147 ? 4.213 91.734 36.206 1.00 86.69 ? 146 ASN B O 1 +ATOM 3517 C CB . ASN B 1 147 ? 2.592 89.768 38.430 1.00 82.91 ? 146 ASN B CB 1 +ATOM 3518 C CG . ASN B 1 147 ? 1.746 88.535 38.595 1.00 74.49 ? 146 ASN B CG 1 +ATOM 3519 O OD1 . ASN B 1 147 ? 0.583 88.507 38.194 1.00 83.69 ? 146 ASN B OD1 1 +ATOM 3520 N ND2 . ASN B 1 147 ? 2.329 87.492 39.177 1.00 121.82 ? 146 ASN B ND2 1 +ATOM 3521 N N . SER B 1 148 ? 3.053 92.597 37.935 1.00 82.44 ? 147 SER B N 1 +ATOM 3522 C CA . SER B 1 148 ? 3.747 93.876 37.885 1.00 70.22 ? 147 SER B CA 1 +ATOM 3523 C C . SER B 1 148 ? 4.786 93.989 38.989 1.00 52.44 ? 147 SER B C 1 +ATOM 3524 O O . SER B 1 148 ? 4.581 93.482 40.086 1.00 118.30 ? 147 SER B O 1 +ATOM 3525 C CB . SER B 1 148 ? 2.747 95.034 37.898 1.00 60.41 ? 147 SER B CB 1 +ATOM 3526 O OG . SER B 1 148 ? 2.053 95.109 36.659 1.00 92.85 ? 147 SER B OG 1 +ATOM 3527 N N . HIS B 1 149 ? 5.913 94.630 38.689 1.00 70.45 ? 148 HIS B N 1 +ATOM 3528 C CA . HIS B 1 149 ? 7.072 94.576 39.577 1.00 93.63 ? 148 HIS B CA 1 +ATOM 3529 C C . HIS B 1 149 ? 7.809 95.908 39.660 1.00 88.93 ? 148 HIS B C 1 +ATOM 3530 O O . HIS B 1 149 ? 7.816 96.680 38.712 1.00 98.49 ? 148 HIS B O 1 +ATOM 3531 C CB . HIS B 1 149 ? 8.037 93.475 39.113 1.00 72.41 ? 148 HIS B CB 1 +ATOM 3532 C CG . HIS B 1 149 ? 7.404 92.123 39.017 1.00 79.54 ? 148 HIS B CG 1 +ATOM 3533 N ND1 . HIS B 1 149 ? 7.241 91.459 37.820 1.00 85.47 ? 148 HIS B ND1 1 +ATOM 3534 C CD2 . HIS B 1 149 ? 6.866 91.322 39.966 1.00 128.48 ? 148 HIS B CD2 1 +ATOM 3535 C CE1 . HIS B 1 149 ? 6.636 90.305 38.038 1.00 98.71 ? 148 HIS B CE1 1 +ATOM 3536 N NE2 . HIS B 1 149 ? 6.399 90.196 39.332 1.00 73.87 ? 148 HIS B NE2 1 +ATOM 3537 N N . ASN B 1 150 ? 8.438 96.175 40.797 1.00 85.50 ? 149 ASN B N 1 +ATOM 3538 C CA . ASN B 1 150 ? 9.251 97.375 40.926 1.00 86.85 ? 149 ASN B CA 1 +ATOM 3539 C C . ASN B 1 150 ? 10.737 97.017 40.830 1.00 78.51 ? 149 ASN B C 1 +ATOM 3540 O O . ASN B 1 150 ? 11.225 96.161 41.559 1.00 98.83 ? 149 ASN B O 1 +ATOM 3541 C CB . ASN B 1 150 ? 8.920 98.123 42.225 1.00 108.07 ? 149 ASN B CB 1 +ATOM 3542 C CG . ASN B 1 150 ? 7.459 98.587 42.287 1.00 103.62 ? 149 ASN B CG 1 +ATOM 3543 O OD1 . ASN B 1 150 ? 6.957 99.229 41.362 1.00 129.07 ? 149 ASN B OD1 1 +ATOM 3544 N ND2 . ASN B 1 150 ? 6.775 98.254 43.380 1.00 108.83 ? 149 ASN B ND2 1 +ATOM 3545 N N . VAL B 1 151 ? 11.434 97.673 39.908 1.00 96.77 ? 150 VAL B N 1 +ATOM 3546 C CA . VAL B 1 151 ? 12.805 97.332 39.523 1.00 66.86 ? 150 VAL B CA 1 +ATOM 3547 C C . VAL B 1 151 ? 13.788 98.271 40.235 1.00 102.78 ? 150 VAL B C 1 +ATOM 3548 O O . VAL B 1 151 ? 14.100 99.343 39.723 1.00 113.06 ? 150 VAL B O 1 +ATOM 3549 C CB . VAL B 1 151 ? 12.939 97.413 37.946 1.00 101.97 ? 150 VAL B CB 1 +ATOM 3550 C CG1 . VAL B 1 151 ? 14.382 97.585 37.446 1.00 66.67 ? 150 VAL B CG1 1 +ATOM 3551 C CG2 . VAL B 1 151 ? 12.293 96.206 37.284 1.00 79.12 ? 150 VAL B CG2 1 +ATOM 3552 N N . TYR B 1 152 ? 14.269 97.901 41.424 1.00 90.71 ? 151 TYR B N 1 +ATOM 3553 C CA . TYR B 1 152 ? 15.106 98.843 42.189 1.00 88.94 ? 151 TYR B CA 1 +ATOM 3554 C C . TYR B 1 152 ? 16.524 99.037 41.627 1.00 99.31 ? 151 TYR B C 1 +ATOM 3555 O O . TYR B 1 152 ? 17.257 98.085 41.387 1.00 94.73 ? 151 TYR B O 1 +ATOM 3556 C CB . TYR B 1 152 ? 15.099 98.551 43.701 1.00 77.04 ? 151 TYR B CB 1 +ATOM 3557 C CG . TYR B 1 152 ? 13.697 98.357 44.249 1.00 95.99 ? 151 TYR B CG 1 +ATOM 3558 C CD1 . TYR B 1 152 ? 13.092 97.111 44.193 1.00 80.11 ? 151 TYR B CD1 1 +ATOM 3559 C CD2 . TYR B 1 152 ? 12.968 99.416 44.798 1.00 103.80 ? 151 TYR B CD2 1 +ATOM 3560 C CE1 . TYR B 1 152 ? 11.807 96.907 44.672 1.00 120.69 ? 151 TYR B CE1 1 +ATOM 3561 C CE2 . TYR B 1 152 ? 11.665 99.218 45.287 1.00 90.46 ? 151 TYR B CE2 1 +ATOM 3562 C CZ . TYR B 1 152 ? 11.095 97.953 45.216 1.00 109.52 ? 151 TYR B CZ 1 +ATOM 3563 O OH . TYR B 1 152 ? 9.816 97.704 45.676 1.00 86.14 ? 151 TYR B OH 1 +ATOM 3564 N N . ILE B 1 153 ? 16.881 100.294 41.398 1.00 88.42 ? 152 ILE B N 1 +ATOM 3565 C CA . ILE B 1 153 ? 18.175 100.659 40.836 1.00 86.12 ? 152 ILE B CA 1 +ATOM 3566 C C . ILE B 1 153 ? 19.012 101.344 41.917 1.00 116.22 ? 152 ILE B C 1 +ATOM 3567 O O . ILE B 1 153 ? 18.479 101.848 42.908 1.00 121.25 ? 152 ILE B O 1 +ATOM 3568 C CB . ILE B 1 153 ? 17.983 101.568 39.601 1.00 85.85 ? 152 ILE B CB 1 +ATOM 3569 C CG1 . ILE B 1 153 ? 17.045 100.883 38.611 1.00 64.54 ? 152 ILE B CG1 1 +ATOM 3570 C CG2 . ILE B 1 153 ? 19.305 101.919 38.925 1.00 71.75 ? 152 ILE B CG2 1 +ATOM 3571 C CD1 . ILE B 1 153 ? 16.823 101.670 37.366 1.00 114.22 ? 152 ILE B CD1 1 +ATOM 3572 N N . MET B 1 154 ? 20.327 101.330 41.737 1.00 124.57 ? 153 MET B N 1 +ATOM 3573 C CA . MET B 1 154 ? 21.248 101.859 42.721 1.00 129.90 ? 153 MET B CA 1 +ATOM 3574 C C . MET B 1 154 ? 22.554 102.103 41.992 1.00 118.15 ? 153 MET B C 1 +ATOM 3575 O O . MET B 1 154 ? 22.979 101.279 41.187 1.00 129.54 ? 153 MET B O 1 +ATOM 3576 C CB . MET B 1 154 ? 21.442 100.839 43.843 1.00 128.12 ? 153 MET B CB 1 +ATOM 3577 C CG . MET B 1 154 ? 22.150 101.382 45.066 1.00 144.76 ? 153 MET B CG 1 +ATOM 3578 S SD . MET B 1 154 ? 22.030 100.317 46.512 1.00 215.45 ? 153 MET B SD 1 +ATOM 3579 C CE . MET B 1 154 ? 20.603 99.331 46.146 1.00 113.26 ? 153 MET B CE 1 +ATOM 3580 N N . ALA B 1 155 ? 23.183 103.243 42.237 1.00 113.89 ? 154 ALA B N 1 +ATOM 3581 C CA . ALA B 1 155 ? 24.440 103.521 41.562 1.00 120.13 ? 154 ALA B CA 1 +ATOM 3582 C C . ALA B 1 155 ? 25.553 102.613 42.069 1.00 143.88 ? 154 ALA B C 1 +ATOM 3583 O O . ALA B 1 155 ? 25.525 102.138 43.210 1.00 119.37 ? 154 ALA B O 1 +ATOM 3584 C CB . ALA B 1 155 ? 24.829 104.979 41.714 1.00 103.38 ? 154 ALA B CB 1 +ATOM 3585 N N . ASP B 1 156 ? 26.515 102.361 41.188 1.00 149.34 ? 155 ASP B N 1 +ATOM 3586 C CA . ASP B 1 156 ? 27.753 101.681 41.535 1.00 172.75 ? 155 ASP B CA 1 +ATOM 3587 C C . ASP B 1 156 ? 28.902 102.577 41.071 1.00 189.70 ? 155 ASP B C 1 +ATOM 3588 O O . ASP B 1 156 ? 29.509 102.352 40.015 1.00 149.29 ? 155 ASP B O 1 +ATOM 3589 C CB . ASP B 1 156 ? 27.811 100.301 40.880 1.00 166.13 ? 155 ASP B CB 1 +ATOM 3590 C CG . ASP B 1 156 ? 29.024 99.503 41.303 1.00 167.39 ? 155 ASP B CG 1 +ATOM 3591 O OD1 . ASP B 1 156 ? 29.776 99.971 42.187 1.00 178.19 ? 155 ASP B OD1 1 +ATOM 3592 O OD2 . ASP B 1 156 ? 29.211 98.398 40.755 1.00 134.49 ? 155 ASP B OD2 1 +ATOM 3593 N N . LYS B 1 157 ? 29.175 103.603 41.876 1.00 204.99 ? 156 LYS B N 1 +ATOM 3594 C CA . LYS B 1 157 ? 30.095 104.677 41.512 1.00 193.16 ? 156 LYS B CA 1 +ATOM 3595 C C . LYS B 1 157 ? 31.503 104.169 41.236 1.00 172.16 ? 156 LYS B C 1 +ATOM 3596 O O . LYS B 1 157 ? 32.245 104.765 40.454 1.00 134.02 ? 156 LYS B O 1 +ATOM 3597 C CB . LYS B 1 157 ? 30.097 105.781 42.583 1.00 185.39 ? 156 LYS B CB 1 +ATOM 3598 C CG . LYS B 1 157 ? 28.949 106.786 42.423 1.00 185.74 ? 156 LYS B CG 1 +ATOM 3599 C CD . LYS B 1 157 ? 28.773 107.697 43.634 1.00 173.95 ? 156 LYS B CD 1 +ATOM 3600 C CE . LYS B 1 157 ? 27.795 108.844 43.348 1.00 169.34 ? 156 LYS B CE 1 +ATOM 3601 N NZ . LYS B 1 157 ? 26.373 108.415 43.200 1.00 162.69 ? 156 LYS B NZ 1 +ATOM 3602 N N . GLN B 1 158 ? 31.857 103.050 41.858 1.00 187.44 ? 157 GLN B N 1 +ATOM 3603 C CA . GLN B 1 158 ? 33.181 102.482 41.661 1.00 187.58 ? 157 GLN B CA 1 +ATOM 3604 C C . GLN B 1 158 ? 33.306 101.801 40.296 1.00 170.21 ? 157 GLN B C 1 +ATOM 3605 O O . GLN B 1 158 ? 34.364 101.863 39.668 1.00 150.86 ? 157 GLN B O 1 +ATOM 3606 C CB . GLN B 1 158 ? 33.567 101.537 42.810 1.00 180.44 ? 157 GLN B CB 1 +ATOM 3607 C CG . GLN B 1 158 ? 33.687 102.209 44.199 1.00 201.57 ? 157 GLN B CG 1 +ATOM 3608 C CD . GLN B 1 158 ? 34.884 103.163 44.348 1.00 206.69 ? 157 GLN B CD 1 +ATOM 3609 O OE1 . GLN B 1 158 ? 35.065 104.095 43.564 1.00 213.51 ? 157 GLN B OE1 1 +ATOM 3610 N NE2 . GLN B 1 158 ? 35.692 102.937 45.377 1.00 186.65 ? 157 GLN B NE2 1 +ATOM 3611 N N . LYS B 1 159 ? 32.229 101.175 39.824 1.00 177.51 ? 158 LYS B N 1 +ATOM 3612 C CA . LYS B 1 159 ? 32.283 100.450 38.549 1.00 161.86 ? 158 LYS B CA 1 +ATOM 3613 C C . LYS B 1 159 ? 31.655 101.222 37.385 1.00 154.66 ? 158 LYS B C 1 +ATOM 3614 O O . LYS B 1 159 ? 31.496 100.681 36.286 1.00 116.48 ? 158 LYS B O 1 +ATOM 3615 C CB . LYS B 1 159 ? 31.663 99.051 38.671 1.00 139.04 ? 158 LYS B CB 1 +ATOM 3616 C CG . LYS B 1 159 ? 32.167 98.242 39.870 1.00 188.53 ? 158 LYS B CG 1 +ATOM 3617 C CD . LYS B 1 159 ? 33.675 98.379 40.082 1.00 201.30 ? 158 LYS B CD 1 +ATOM 3618 C CE . LYS B 1 159 ? 34.046 98.216 41.554 1.00 175.95 ? 158 LYS B CE 1 +ATOM 3619 N NZ . LYS B 1 159 ? 35.436 98.672 41.838 1.00 169.99 ? 158 LYS B NZ 1 +ATOM 3620 N N . ASN B 1 160 ? 31.308 102.483 37.636 1.00 154.15 ? 159 ASN B N 1 +ATOM 3621 C CA . ASN B 1 160 ? 30.795 103.385 36.601 1.00 156.23 ? 159 ASN B CA 1 +ATOM 3622 C C . ASN B 1 160 ? 29.547 102.825 35.913 1.00 146.07 ? 159 ASN B C 1 +ATOM 3623 O O . ASN B 1 160 ? 29.297 103.066 34.732 1.00 121.75 ? 159 ASN B O 1 +ATOM 3624 C CB . ASN B 1 160 ? 31.897 103.715 35.582 1.00 152.30 ? 159 ASN B CB 1 +ATOM 3625 C CG . ASN B 1 160 ? 31.555 104.914 34.700 1.00 167.79 ? 159 ASN B CG 1 +ATOM 3626 O OD1 . ASN B 1 160 ? 30.999 105.911 35.164 1.00 162.37 ? 159 ASN B OD1 1 +ATOM 3627 N ND2 . ASN B 1 160 ? 31.886 104.812 33.415 1.00 152.46 ? 159 ASN B ND2 1 +ATOM 3628 N N . GLY B 1 161 ? 28.760 102.069 36.664 1.00 141.01 ? 160 GLY B N 1 +ATOM 3629 C CA . GLY B 1 161 ? 27.568 101.471 36.108 1.00 135.61 ? 160 GLY B CA 1 +ATOM 3630 C C . GLY B 1 161 ? 26.461 101.526 37.126 1.00 121.32 ? 160 GLY B C 1 +ATOM 3631 O O . GLY B 1 161 ? 26.411 102.452 37.928 1.00 123.26 ? 160 GLY B O 1 +ATOM 3632 N N . ILE B 1 162 ? 25.573 100.540 37.099 1.00 117.28 ? 161 ILE B N 1 +ATOM 3633 C CA . ILE B 1 162 ? 24.491 100.478 38.072 1.00 118.76 ? 161 ILE B CA 1 +ATOM 3634 C C . ILE B 1 162 ? 24.284 99.046 38.554 1.00 109.37 ? 161 ILE B C 1 +ATOM 3635 O O . ILE B 1 162 ? 24.530 98.093 37.818 1.00 116.72 ? 161 ILE B O 1 +ATOM 3636 C CB . ILE B 1 162 ? 23.149 101.040 37.510 1.00 121.26 ? 161 ILE B CB 1 +ATOM 3637 C CG1 . ILE B 1 162 ? 22.671 100.238 36.303 1.00 116.21 ? 161 ILE B CG1 1 +ATOM 3638 C CG2 . ILE B 1 162 ? 23.273 102.512 37.121 1.00 125.28 ? 161 ILE B CG2 1 +ATOM 3639 C CD1 . ILE B 1 162 ? 21.259 100.576 35.891 1.00 84.60 ? 161 ILE B CD1 1 +ATOM 3640 N N . LYS B 1 163 ? 23.857 98.897 39.800 1.00 100.31 ? 162 LYS B N 1 +ATOM 3641 C CA . LYS B 1 163 ? 23.447 97.597 40.306 1.00 106.54 ? 162 LYS B CA 1 +ATOM 3642 C C . LYS B 1 163 ? 21.943 97.578 40.183 1.00 114.20 ? 162 LYS B C 1 +ATOM 3643 O O . LYS B 1 163 ? 21.306 98.618 40.247 1.00 121.96 ? 162 LYS B O 1 +ATOM 3644 C CB . LYS B 1 163 ? 23.863 97.412 41.768 1.00 129.11 ? 162 LYS B CB 1 +ATOM 3645 C CG . LYS B 1 163 ? 24.938 96.345 41.983 1.00 166.21 ? 162 LYS B CG 1 +ATOM 3646 C CD . LYS B 1 163 ? 25.500 96.350 43.405 1.00 166.94 ? 162 LYS B CD 1 +ATOM 3647 C CE . LYS B 1 163 ? 26.667 95.362 43.566 1.00 163.03 ? 162 LYS B CE 1 +ATOM 3648 N NZ . LYS B 1 163 ? 27.826 95.635 42.660 1.00 161.80 ? 162 LYS B NZ 1 +ATOM 3649 N N . VAL B 1 164 ? 21.362 96.411 39.972 1.00 100.43 ? 163 VAL B N 1 +ATOM 3650 C CA . VAL B 1 164 ? 19.919 96.340 39.852 1.00 98.09 ? 163 VAL B CA 1 +ATOM 3651 C C . VAL B 1 164 ? 19.434 95.079 40.542 1.00 75.44 ? 163 VAL B C 1 +ATOM 3652 O O . VAL B 1 164 ? 20.027 94.013 40.391 1.00 113.50 ? 163 VAL B O 1 +ATOM 3653 C CB . VAL B 1 164 ? 19.454 96.316 38.360 1.00 115.60 ? 163 VAL B CB 1 +ATOM 3654 C CG1 . VAL B 1 164 ? 17.934 96.356 38.264 1.00 78.77 ? 163 VAL B CG1 1 +ATOM 3655 C CG2 . VAL B 1 164 ? 20.061 97.459 37.545 1.00 101.46 ? 163 VAL B CG2 1 +ATOM 3656 N N . ASN B 1 165 ? 18.352 95.182 41.296 1.00 89.79 ? 164 ASN B N 1 +ATOM 3657 C CA . ASN B 1 165 ? 17.759 93.967 41.817 1.00 100.19 ? 164 ASN B CA 1 +ATOM 3658 C C . ASN B 1 165 ? 16.246 94.026 41.954 1.00 90.43 ? 164 ASN B C 1 +ATOM 3659 O O . ASN B 1 165 ? 15.676 95.091 42.174 1.00 113.56 ? 164 ASN B O 1 +ATOM 3660 C CB . ASN B 1 165 ? 18.430 93.557 43.128 1.00 98.73 ? 164 ASN B CB 1 +ATOM 3661 C CG . ASN B 1 165 ? 18.304 94.605 44.200 1.00 117.33 ? 164 ASN B CG 1 +ATOM 3662 O OD1 . ASN B 1 165 ? 18.745 95.746 44.035 1.00 138.14 ? 164 ASN B OD1 1 +ATOM 3663 N ND2 . ASN B 1 165 ? 17.690 94.225 45.315 1.00 158.89 ? 164 ASN B ND2 1 +ATOM 3664 N N . PHE B 1 166 ? 15.612 92.868 41.799 1.00 73.95 ? 165 PHE B N 1 +ATOM 3665 C CA . PHE B 1 166 ? 14.165 92.729 41.927 1.00 96.73 ? 165 PHE B CA 1 +ATOM 3666 C C . PHE B 1 166 ? 13.755 91.272 41.937 1.00 81.76 ? 165 PHE B C 1 +ATOM 3667 O O . PHE B 1 166 ? 14.596 90.385 41.867 1.00 107.99 ? 165 PHE B O 1 +ATOM 3668 C CB . PHE B 1 166 ? 13.428 93.459 40.810 1.00 100.18 ? 165 PHE B CB 1 +ATOM 3669 C CG . PHE B 1 166 ? 13.888 93.100 39.424 1.00 90.13 ? 165 PHE B CG 1 +ATOM 3670 C CD1 . PHE B 1 166 ? 15.027 93.686 38.880 1.00 79.07 ? 165 PHE B CD1 1 +ATOM 3671 C CD2 . PHE B 1 166 ? 13.147 92.224 38.647 1.00 51.93 ? 165 PHE B CD2 1 +ATOM 3672 C CE1 . PHE B 1 166 ? 15.437 93.385 37.601 1.00 66.62 ? 165 PHE B CE1 1 +ATOM 3673 C CE2 . PHE B 1 166 ? 13.544 91.921 37.373 1.00 72.32 ? 165 PHE B CE2 1 +ATOM 3674 C CZ . PHE B 1 166 ? 14.697 92.503 36.846 1.00 81.53 ? 165 PHE B CZ 1 +ATOM 3675 N N . LYS B 1 167 ? 12.452 91.029 41.985 1.00 78.95 ? 166 LYS B N 1 +ATOM 3676 C CA . LYS B 1 167 ? 11.955 89.693 42.269 1.00 95.63 ? 166 LYS B CA 1 +ATOM 3677 C C . LYS B 1 167 ? 10.636 89.385 41.559 1.00 97.77 ? 166 LYS B C 1 +ATOM 3678 O O . LYS B 1 167 ? 9.563 89.804 41.997 1.00 96.18 ? 166 LYS B O 1 +ATOM 3679 C CB . LYS B 1 167 ? 11.809 89.528 43.783 1.00 70.06 ? 166 LYS B CB 1 +ATOM 3680 C CG . LYS B 1 167 ? 11.283 88.177 44.239 1.00 121.61 ? 166 LYS B CG 1 +ATOM 3681 C CD . LYS B 1 167 ? 10.811 88.242 45.690 1.00 151.88 ? 166 LYS B CD 1 +ATOM 3682 C CE . LYS B 1 167 ? 11.868 88.842 46.622 1.00 126.55 ? 166 LYS B CE 1 +ATOM 3683 N NZ . LYS B 1 167 ? 13.024 87.935 46.832 1.00 162.75 ? 166 LYS B NZ 1 +ATOM 3684 N N . ILE B 1 168 ? 10.731 88.630 40.469 1.00 89.35 ? 167 ILE B N 1 +ATOM 3685 C CA . ILE B 1 168 ? 9.579 88.322 39.630 1.00 94.76 ? 167 ILE B CA 1 +ATOM 3686 C C . ILE B 1 168 ? 8.726 87.199 40.187 1.00 90.88 ? 167 ILE B C 1 +ATOM 3687 O O . ILE B 1 168 ? 9.233 86.156 40.583 1.00 91.99 ? 167 ILE B O 1 +ATOM 3688 C CB . ILE B 1 168 ? 10.021 87.857 38.244 1.00 65.82 ? 167 ILE B CB 1 +ATOM 3689 C CG1 . ILE B 1 168 ? 10.989 88.857 37.619 1.00 90.82 ? 167 ILE B CG1 1 +ATOM 3690 C CG2 . ILE B 1 168 ? 8.823 87.621 37.359 1.00 83.34 ? 167 ILE B CG2 1 +ATOM 3691 C CD1 . ILE B 1 168 ? 10.391 90.181 37.295 1.00 109.95 ? 167 ILE B CD1 1 +ATOM 3692 N N . ARG B 1 169 ? 7.419 87.399 40.183 1.00 72.23 ? 168 ARG B N 1 +ATOM 3693 C CA . ARG B 1 169 ? 6.513 86.349 40.592 1.00 82.03 ? 168 ARG B CA 1 +ATOM 3694 C C . ARG B 1 169 ? 5.850 85.721 39.368 1.00 71.42 ? 168 ARG B C 1 +ATOM 3695 O O . ARG B 1 169 ? 5.113 86.400 38.655 1.00 103.63 ? 168 ARG B O 1 +ATOM 3696 C CB . ARG B 1 169 ? 5.468 86.929 41.545 1.00 94.31 ? 168 ARG B CB 1 +ATOM 3697 C CG . ARG B 1 169 ? 6.069 87.541 42.806 1.00 104.31 ? 168 ARG B CG 1 +ATOM 3698 C CD . ARG B 1 169 ? 5.003 88.039 43.792 1.00 100.67 ? 168 ARG B CD 1 +ATOM 3699 N NE . ARG B 1 169 ? 4.379 89.279 43.336 1.00 114.92 ? 168 ARG B NE 1 +ATOM 3700 C CZ . ARG B 1 169 ? 4.983 90.466 43.330 1.00 139.35 ? 168 ARG B CZ 1 +ATOM 3701 N NH1 . ARG B 1 169 ? 6.235 90.586 43.755 1.00 119.63 ? 168 ARG B NH1 1 +ATOM 3702 N NH2 . ARG B 1 169 ? 4.337 91.540 42.891 1.00 133.64 ? 168 ARG B NH2 1 +ATOM 3703 N N . HIS B 1 170 ? 6.118 84.437 39.115 1.00 69.72 ? 169 HIS B N 1 +ATOM 3704 C CA . HIS B 1 170 ? 5.437 83.714 38.033 1.00 94.78 ? 169 HIS B CA 1 +ATOM 3705 C C . HIS B 1 170 ? 4.235 82.933 38.560 1.00 65.43 ? 169 HIS B C 1 +ATOM 3706 O O . HIS B 1 170 ? 4.356 82.193 39.522 1.00 103.72 ? 169 HIS B O 1 +ATOM 3707 C CB . HIS B 1 170 ? 6.385 82.748 37.320 1.00 66.91 ? 169 HIS B CB 1 +ATOM 3708 C CG . HIS B 1 170 ? 7.581 83.397 36.699 1.00 83.49 ? 169 HIS B CG 1 +ATOM 3709 N ND1 . HIS B 1 170 ? 7.615 83.792 35.380 1.00 98.34 ? 169 HIS B ND1 1 +ATOM 3710 C CD2 . HIS B 1 170 ? 8.797 83.701 37.212 1.00 106.69 ? 169 HIS B CD2 1 +ATOM 3711 C CE1 . HIS B 1 170 ? 8.794 84.323 35.111 1.00 86.41 ? 169 HIS B CE1 1 +ATOM 3712 N NE2 . HIS B 1 170 ? 9.529 84.282 36.205 1.00 59.14 ? 169 HIS B NE2 1 +ATOM 3713 N N . ASN B 1 171 ? 3.078 83.093 37.930 1.00 114.07 ? 170 ASN B N 1 +ATOM 3714 C CA . ASN B 1 171 ? 1.899 82.317 38.302 1.00 92.37 ? 170 ASN B CA 1 +ATOM 3715 C C . ASN B 1 171 ? 1.984 80.882 37.783 1.00 111.45 ? 170 ASN B C 1 +ATOM 3716 O O . ASN B 1 171 ? 2.453 80.662 36.664 1.00 119.51 ? 170 ASN B O 1 +ATOM 3717 C CB . ASN B 1 171 ? 0.639 82.973 37.739 1.00 101.20 ? 170 ASN B CB 1 +ATOM 3718 C CG . ASN B 1 171 ? 0.209 84.189 38.524 1.00 104.30 ? 170 ASN B CG 1 +ATOM 3719 O OD1 . ASN B 1 171 ? 1.001 84.784 39.256 1.00 102.96 ? 170 ASN B OD1 1 +ATOM 3720 N ND2 . ASN B 1 171 ? -1.059 84.566 38.378 1.00 106.30 ? 170 ASN B ND2 1 +ATOM 3721 N N . ILE B 1 172 ? 1.505 79.931 38.591 1.00 107.28 ? 171 ILE B N 1 +ATOM 3722 C CA . ILE B 1 172 ? 1.470 78.492 38.281 1.00 109.50 ? 171 ILE B CA 1 +ATOM 3723 C C . ILE B 1 172 ? 0.001 78.065 38.378 1.00 125.21 ? 171 ILE B C 1 +ATOM 3724 O O . ILE B 1 172 ? -0.777 78.783 38.999 1.00 153.44 ? 171 ILE B O 1 +ATOM 3725 C CB . ILE B 1 172 ? 2.343 77.724 39.298 1.00 97.67 ? 171 ILE B CB 1 +ATOM 3726 C CG1 . ILE B 1 172 ? 3.791 78.202 39.193 1.00 92.84 ? 171 ILE B CG1 1 +ATOM 3727 C CG2 . ILE B 1 172 ? 2.288 76.224 39.088 1.00 76.33 ? 171 ILE B CG2 1 +ATOM 3728 C CD1 . ILE B 1 172 ? 4.576 78.038 40.456 1.00 101.55 ? 171 ILE B CD1 1 +ATOM 3729 N N . GLU B 1 173 ? -0.409 76.940 37.778 1.00 81.28 ? 172 GLU B N 1 +ATOM 3730 C CA . GLU B 1 173 ? -1.852 76.635 37.765 1.00 131.13 ? 172 GLU B CA 1 +ATOM 3731 C C . GLU B 1 173 ? -2.517 76.376 39.134 1.00 136.20 ? 172 GLU B C 1 +ATOM 3732 O O . GLU B 1 173 ? -3.622 76.853 39.386 1.00 147.93 ? 172 GLU B O 1 +ATOM 3733 C CB . GLU B 1 173 ? -2.245 75.549 36.750 1.00 112.83 ? 172 GLU B CB 1 +ATOM 3734 C CG . GLU B 1 173 ? -3.759 75.608 36.445 1.00 163.36 ? 172 GLU B CG 1 +ATOM 3735 C CD . GLU B 1 173 ? -4.273 74.524 35.502 1.00 202.03 ? 172 GLU B CD 1 +ATOM 3736 O OE1 . GLU B 1 173 ? -3.843 73.359 35.625 1.00 182.34 ? 172 GLU B OE1 1 +ATOM 3737 O OE2 . GLU B 1 173 ? -5.129 74.837 34.643 1.00 216.45 ? 172 GLU B OE2 1 +ATOM 3738 N N . ASP B 1 174 ? -1.852 75.650 40.024 1.00 99.63 ? 173 ASP B N 1 +ATOM 3739 C CA . ASP B 1 174 ? -2.437 75.351 41.334 1.00 125.27 ? 173 ASP B CA 1 +ATOM 3740 C C . ASP B 1 174 ? -2.631 76.571 42.256 1.00 149.65 ? 173 ASP B C 1 +ATOM 3741 O O . ASP B 1 174 ? -3.038 76.428 43.411 1.00 209.84 ? 173 ASP B O 1 +ATOM 3742 C CB . ASP B 1 174 ? -1.602 74.288 42.048 1.00 144.97 ? 173 ASP B CB 1 +ATOM 3743 C CG . ASP B 1 174 ? -0.119 74.601 42.022 1.00 135.27 ? 173 ASP B CG 1 +ATOM 3744 O OD1 . ASP B 1 174 ? 0.241 75.793 41.938 1.00 128.91 ? 173 ASP B OD1 1 +ATOM 3745 O OD2 . ASP B 1 174 ? 0.691 73.653 42.084 1.00 134.27 ? 173 ASP B OD2 1 +ATOM 3746 N N . GLY B 1 175 ? -2.331 77.763 41.756 1.00 104.87 ? 174 GLY B N 1 +ATOM 3747 C CA . GLY B 1 175 ? -2.481 78.969 42.549 1.00 101.50 ? 174 GLY B CA 1 +ATOM 3748 C C . GLY B 1 175 ? -1.220 79.412 43.269 1.00 111.36 ? 174 GLY B C 1 +ATOM 3749 O O . GLY B 1 175 ? -1.182 80.509 43.827 1.00 122.53 ? 174 GLY B O 1 +ATOM 3750 N N . SER B 1 176 ? -0.189 78.570 43.267 1.00 76.72 ? 175 SER B N 1 +ATOM 3751 C CA . SER B 1 176 ? 1.069 78.932 43.919 1.00 113.08 ? 175 SER B CA 1 +ATOM 3752 C C . SER B 1 176 ? 1.876 79.889 43.048 1.00 105.34 ? 175 SER B C 1 +ATOM 3753 O O . SER B 1 176 ? 1.434 80.256 41.963 1.00 103.70 ? 175 SER B O 1 +ATOM 3754 C CB . SER B 1 176 ? 1.891 77.694 44.309 1.00 120.49 ? 175 SER B CB 1 +ATOM 3755 O OG . SER B 1 176 ? 2.031 76.776 43.238 1.00 101.35 ? 175 SER B OG 1 +ATOM 3756 N N . VAL B 1 177 ? 3.051 80.296 43.523 1.00 104.40 ? 176 VAL B N 1 +ATOM 3757 C CA . VAL B 1 177 ? 3.835 81.326 42.835 1.00 86.49 ? 176 VAL B CA 1 +ATOM 3758 C C . VAL B 1 177 ? 5.345 81.073 42.840 1.00 101.73 ? 176 VAL B C 1 +ATOM 3759 O O . VAL B 1 177 ? 5.974 80.992 43.895 1.00 142.42 ? 176 VAL B O 1 +ATOM 3760 C CB . VAL B 1 177 ? 3.556 82.731 43.428 1.00 79.65 ? 176 VAL B CB 1 +ATOM 3761 C CG1 . VAL B 1 177 ? 4.606 83.742 42.969 1.00 97.89 ? 176 VAL B CG1 1 +ATOM 3762 C CG2 . VAL B 1 177 ? 2.153 83.198 43.067 1.00 100.45 ? 176 VAL B CG2 1 +ATOM 3763 N N . GLN B 1 178 ? 5.927 80.982 41.651 1.00 68.35 ? 177 GLN B N 1 +ATOM 3764 C CA . GLN B 1 178 ? 7.353 80.716 41.517 1.00 99.50 ? 177 GLN B CA 1 +ATOM 3765 C C . GLN B 1 178 ? 8.198 81.991 41.543 1.00 96.93 ? 177 GLN B C 1 +ATOM 3766 O O . GLN B 1 178 ? 8.105 82.818 40.640 1.00 94.76 ? 177 GLN B O 1 +ATOM 3767 C CB . GLN B 1 178 ? 7.615 79.929 40.234 1.00 80.55 ? 177 GLN B CB 1 +ATOM 3768 C CG . GLN B 1 178 ? 9.079 79.794 39.868 1.00 108.47 ? 177 GLN B CG 1 +ATOM 3769 C CD . GLN B 1 178 ? 9.815 78.799 40.732 1.00 94.80 ? 177 GLN B CD 1 +ATOM 3770 O OE1 . GLN B 1 178 ? 9.394 77.650 40.869 1.00 99.63 ? 177 GLN B OE1 1 +ATOM 3771 N NE2 . GLN B 1 178 ? 10.928 79.233 41.317 1.00 105.43 ? 177 GLN B NE2 1 +ATOM 3772 N N . LEU B 1 179 ? 9.026 82.149 42.572 1.00 80.64 ? 178 LEU B N 1 +ATOM 3773 C CA . LEU B 1 179 ? 9.875 83.337 42.675 1.00 81.40 ? 178 LEU B CA 1 +ATOM 3774 C C . LEU B 1 179 ? 11.048 83.297 41.697 1.00 76.49 ? 178 LEU B C 1 +ATOM 3775 O O . LEU B 1 179 ? 11.534 82.225 41.353 1.00 98.79 ? 178 LEU B O 1 +ATOM 3776 C CB . LEU B 1 179 ? 10.390 83.531 44.106 1.00 87.65 ? 178 LEU B CB 1 +ATOM 3777 C CG . LEU B 1 179 ? 9.368 83.841 45.207 1.00 109.66 ? 178 LEU B CG 1 +ATOM 3778 C CD1 . LEU B 1 179 ? 10.028 83.857 46.575 1.00 122.50 ? 178 LEU B CD1 1 +ATOM 3779 C CD2 . LEU B 1 179 ? 8.666 85.169 44.948 1.00 79.47 ? 178 LEU B CD2 1 +ATOM 3780 N N . ALA B 1 180 ? 11.499 84.471 41.258 1.00 82.70 ? 179 ALA B N 1 +ATOM 3781 C CA . ALA B 1 180 ? 12.652 84.575 40.358 1.00 95.93 ? 179 ALA B CA 1 +ATOM 3782 C C . ALA B 1 180 ? 13.596 85.725 40.735 1.00 92.90 ? 179 ALA B C 1 +ATOM 3783 O O . ALA B 1 180 ? 13.597 86.803 40.135 1.00 102.90 ? 179 ALA B O 1 +ATOM 3784 C CB . ALA B 1 180 ? 12.205 84.679 38.902 1.00 104.88 ? 179 ALA B CB 1 +ATOM 3785 N N . ASP B 1 181 ? 14.416 85.458 41.737 1.00 82.48 ? 180 ASP B N 1 +ATOM 3786 C CA . ASP B 1 181 ? 15.283 86.456 42.341 1.00 110.17 ? 180 ASP B CA 1 +ATOM 3787 C C . ASP B 1 181 ? 16.327 87.018 41.350 1.00 93.66 ? 180 ASP B C 1 +ATOM 3788 O O . ASP B 1 181 ? 17.327 86.369 41.055 1.00 98.78 ? 180 ASP B O 1 +ATOM 3789 C CB . ASP B 1 181 ? 15.954 85.805 43.551 1.00 111.07 ? 180 ASP B CB 1 +ATOM 3790 C CG . ASP B 1 181 ? 16.405 86.798 44.587 1.00 115.72 ? 180 ASP B CG 1 +ATOM 3791 O OD1 . ASP B 1 181 ? 16.346 88.019 44.343 1.00 125.15 ? 180 ASP B OD1 1 +ATOM 3792 O OD2 . ASP B 1 181 ? 16.846 86.336 45.655 1.00 134.32 ? 180 ASP B OD2 1 +ATOM 3793 N N . HIS B 1 182 ? 16.098 88.231 40.845 1.00 76.18 ? 181 HIS B N 1 +ATOM 3794 C CA . HIS B 1 182 ? 16.973 88.807 39.811 1.00 99.17 ? 181 HIS B CA 1 +ATOM 3795 C C . HIS B 1 182 ? 18.114 89.680 40.316 1.00 80.87 ? 181 HIS B C 1 +ATOM 3796 O O . HIS B 1 182 ? 17.874 90.715 40.926 1.00 79.78 ? 181 HIS B O 1 +ATOM 3797 C CB . HIS B 1 182 ? 16.172 89.660 38.829 1.00 86.83 ? 181 HIS B CB 1 +ATOM 3798 C CG . HIS B 1 182 ? 15.365 88.873 37.850 1.00 72.79 ? 181 HIS B CG 1 +ATOM 3799 N ND1 . HIS B 1 182 ? 14.409 87.961 38.237 1.00 95.80 ? 181 HIS B ND1 1 +ATOM 3800 C CD2 . HIS B 1 182 ? 15.349 88.883 36.496 1.00 71.34 ? 181 HIS B CD2 1 +ATOM 3801 C CE1 . HIS B 1 182 ? 13.853 87.428 37.165 1.00 93.80 ? 181 HIS B CE1 1 +ATOM 3802 N NE2 . HIS B 1 182 ? 14.400 87.975 36.095 1.00 78.16 ? 181 HIS B NE2 1 +ATOM 3803 N N . TYR B 1 183 ? 19.347 89.297 39.994 1.00 102.39 ? 182 TYR B N 1 +ATOM 3804 C CA . TYR B 1 183 ? 20.538 90.075 40.356 1.00 101.93 ? 182 TYR B CA 1 +ATOM 3805 C C . TYR B 1 183 ? 21.245 90.640 39.120 1.00 79.47 ? 182 TYR B C 1 +ATOM 3806 O O . TYR B 1 183 ? 21.931 89.908 38.411 1.00 116.61 ? 182 TYR B O 1 +ATOM 3807 C CB . TYR B 1 183 ? 21.517 89.214 41.172 1.00 82.70 ? 182 TYR B CB 1 +ATOM 3808 C CG . TYR B 1 183 ? 20.996 88.879 42.550 1.00 89.44 ? 182 TYR B CG 1 +ATOM 3809 C CD1 . TYR B 1 183 ? 20.184 87.770 42.758 1.00 104.71 ? 182 TYR B CD1 1 +ATOM 3810 C CD2 . TYR B 1 183 ? 21.289 89.686 43.636 1.00 82.62 ? 182 TYR B CD2 1 +ATOM 3811 C CE1 . TYR B 1 183 ? 19.681 87.465 44.022 1.00 96.56 ? 182 TYR B CE1 1 +ATOM 3812 C CE2 . TYR B 1 183 ? 20.793 89.394 44.904 1.00 108.87 ? 182 TYR B CE2 1 +ATOM 3813 C CZ . TYR B 1 183 ? 19.988 88.281 45.096 1.00 107.65 ? 182 TYR B CZ 1 +ATOM 3814 O OH . TYR B 1 183 ? 19.492 87.991 46.360 1.00 109.45 ? 182 TYR B OH 1 +ATOM 3815 N N . GLN B 1 184 ? 21.104 91.939 38.877 1.00 74.44 ? 183 GLN B N 1 +ATOM 3816 C CA . GLN B 1 184 ? 21.555 92.530 37.609 1.00 106.79 ? 183 GLN B CA 1 +ATOM 3817 C C . GLN B 1 184 ? 22.683 93.563 37.750 1.00 98.51 ? 183 GLN B C 1 +ATOM 3818 O O . GLN B 1 184 ? 22.895 94.123 38.824 1.00 104.36 ? 183 GLN B O 1 +ATOM 3819 C CB . GLN B 1 184 ? 20.349 93.149 36.885 1.00 102.08 ? 183 GLN B CB 1 +ATOM 3820 C CG . GLN B 1 184 ? 20.637 93.905 35.593 1.00 105.50 ? 183 GLN B CG 1 +ATOM 3821 C CD . GLN B 1 184 ? 19.441 94.708 35.127 1.00 116.57 ? 183 GLN B CD 1 +ATOM 3822 O OE1 . GLN B 1 184 ? 18.295 94.306 35.334 1.00 85.47 ? 183 GLN B OE1 1 +ATOM 3823 N NE2 . GLN B 1 184 ? 19.699 95.855 34.505 1.00 79.65 ? 183 GLN B NE2 1 +ATOM 3824 N N . GLN B 1 185 ? 23.417 93.803 36.666 1.00 77.68 ? 184 GLN B N 1 +ATOM 3825 C CA . GLN B 1 185 ? 24.366 94.909 36.645 1.00 96.52 ? 184 GLN B CA 1 +ATOM 3826 C C . GLN B 1 185 ? 24.647 95.463 35.244 1.00 118.42 ? 184 GLN B C 1 +ATOM 3827 O O . GLN B 1 185 ? 24.838 94.709 34.283 1.00 95.90 ? 184 GLN B O 1 +ATOM 3828 C CB . GLN B 1 185 ? 25.663 94.534 37.366 1.00 124.44 ? 184 GLN B CB 1 +ATOM 3829 C CG . GLN B 1 185 ? 26.408 93.347 36.785 1.00 152.30 ? 184 GLN B CG 1 +ATOM 3830 C CD . GLN B 1 185 ? 27.710 93.075 37.522 1.00 176.78 ? 184 GLN B CD 1 +ATOM 3831 O OE1 . GLN B 1 185 ? 27.863 93.442 38.691 1.00 181.41 ? 184 GLN B OE1 1 +ATOM 3832 N NE2 . GLN B 1 185 ? 28.659 92.438 36.837 1.00 181.60 ? 184 GLN B NE2 1 +ATOM 3833 N N . ASN B 1 186 ? 24.673 96.791 35.148 1.00 94.47 ? 185 ASN B N 1 +ATOM 3834 C CA . ASN B 1 186 ? 24.869 97.478 33.874 1.00 111.07 ? 185 ASN B CA 1 +ATOM 3835 C C . ASN B 1 186 ? 26.128 98.348 33.814 1.00 121.96 ? 185 ASN B C 1 +ATOM 3836 O O . ASN B 1 186 ? 26.456 99.045 34.771 1.00 105.83 ? 185 ASN B O 1 +ATOM 3837 C CB . ASN B 1 186 ? 23.629 98.295 33.518 1.00 105.96 ? 185 ASN B CB 1 +ATOM 3838 C CG . ASN B 1 186 ? 22.427 97.424 33.230 1.00 105.21 ? 185 ASN B CG 1 +ATOM 3839 O OD1 . ASN B 1 186 ? 21.629 97.128 34.117 1.00 107.77 ? 185 ASN B OD1 1 +ATOM 3840 N ND2 . ASN B 1 186 ? 22.297 97.003 31.985 1.00 85.15 ? 185 ASN B ND2 1 +ATOM 3841 N N . THR B 1 187 ? 26.805 98.297 32.666 1.00 99.98 ? 186 THR B N 1 +ATOM 3842 C CA . THR B 1 187 ? 28.141 98.862 32.466 1.00 106.61 ? 186 THR B CA 1 +ATOM 3843 C C . THR B 1 187 ? 28.328 99.338 31.020 1.00 112.12 ? 186 THR B C 1 +ATOM 3844 O O . THR B 1 187 ? 28.163 98.558 30.081 1.00 126.54 ? 186 THR B O 1 +ATOM 3845 C CB . THR B 1 187 ? 29.232 97.802 32.761 1.00 101.55 ? 186 THR B CB 1 +ATOM 3846 O OG1 . THR B 1 187 ? 29.290 97.540 34.167 1.00 110.29 ? 186 THR B OG1 1 +ATOM 3847 C CG2 . THR B 1 187 ? 30.600 98.278 32.279 1.00 93.44 ? 186 THR B CG2 1 +ATOM 3848 N N . PRO B 1 188 ? 28.692 100.619 30.837 1.00 113.57 ? 187 PRO B N 1 +ATOM 3849 C CA . PRO B 1 188 ? 28.847 101.232 29.509 1.00 119.85 ? 187 PRO B CA 1 +ATOM 3850 C C . PRO B 1 188 ? 30.030 100.713 28.694 1.00 122.67 ? 187 PRO B C 1 +ATOM 3851 O O . PRO B 1 188 ? 31.169 100.656 29.159 1.00 126.46 ? 187 PRO B O 1 +ATOM 3852 C CB . PRO B 1 188 ? 29.047 102.716 29.829 1.00 111.31 ? 187 PRO B CB 1 +ATOM 3853 C CG . PRO B 1 188 ? 29.622 102.726 31.205 1.00 113.84 ? 187 PRO B CG 1 +ATOM 3854 C CD . PRO B 1 188 ? 28.953 101.582 31.919 1.00 98.60 ? 187 PRO B CD 1 +ATOM 3855 N N . ILE B 1 189 ? 29.735 100.351 27.455 1.00 121.42 ? 188 ILE B N 1 +ATOM 3856 C CA . ILE B 1 189 ? 30.739 99.923 26.499 1.00 124.75 ? 188 ILE B CA 1 +ATOM 3857 C C . ILE B 1 189 ? 31.624 101.098 26.101 1.00 137.66 ? 188 ILE B C 1 +ATOM 3858 O O . ILE B 1 189 ? 32.820 100.936 25.841 1.00 126.23 ? 188 ILE B O 1 +ATOM 3859 C CB . ILE B 1 189 ? 30.040 99.359 25.259 1.00 114.76 ? 188 ILE B CB 1 +ATOM 3860 C CG1 . ILE B 1 189 ? 29.146 98.185 25.672 1.00 111.52 ? 188 ILE B CG1 1 +ATOM 3861 C CG2 . ILE B 1 189 ? 31.054 98.966 24.195 1.00 108.31 ? 188 ILE B CG2 1 +ATOM 3862 C CD1 . ILE B 1 189 ? 28.187 97.713 24.600 1.00 120.33 ? 188 ILE B CD1 1 +ATOM 3863 N N . GLY B 1 190 ? 31.025 102.284 26.067 1.00 145.98 ? 189 GLY B N 1 +ATOM 3864 C CA . GLY B 1 190 ? 31.720 103.486 25.649 1.00 150.15 ? 189 GLY B CA 1 +ATOM 3865 C C . GLY B 1 190 ? 32.580 104.090 26.741 1.00 160.35 ? 189 GLY B C 1 +ATOM 3866 O O . GLY B 1 190 ? 32.509 103.679 27.903 1.00 135.15 ? 189 GLY B O 1 +ATOM 3867 N N . ASP B 1 191 ? 33.399 105.068 26.354 1.00 163.59 ? 190 ASP B N 1 +ATOM 3868 C CA . ASP B 1 191 ? 34.291 105.762 27.283 1.00 172.29 ? 190 ASP B CA 1 +ATOM 3869 C C . ASP B 1 191 ? 33.711 107.116 27.682 1.00 163.52 ? 190 ASP B C 1 +ATOM 3870 O O . ASP B 1 191 ? 34.173 107.742 28.638 1.00 144.26 ? 190 ASP B O 1 +ATOM 3871 C CB . ASP B 1 191 ? 35.697 105.938 26.685 1.00 168.10 ? 190 ASP B CB 1 +ATOM 3872 C CG . ASP B 1 191 ? 36.536 104.670 26.764 1.00 180.27 ? 190 ASP B CG 1 +ATOM 3873 O OD1 . ASP B 1 191 ? 36.807 104.194 27.884 1.00 157.33 ? 190 ASP B OD1 1 +ATOM 3874 O OD2 . ASP B 1 191 ? 36.937 104.156 25.701 1.00 194.34 ? 190 ASP B OD2 1 +ATOM 3875 N N . GLY B 1 192 ? 32.695 107.557 26.945 1.00 162.21 ? 191 GLY B N 1 +ATOM 3876 C CA . GLY B 1 192 ? 31.998 108.793 27.256 1.00 162.33 ? 191 GLY B CA 1 +ATOM 3877 C C . GLY B 1 192 ? 31.374 108.792 28.642 1.00 170.81 ? 191 GLY B C 1 +ATOM 3878 O O . GLY B 1 192 ? 31.150 107.728 29.223 1.00 164.46 ? 191 GLY B O 1 +ATOM 3879 N N . PRO B 1 193 ? 31.093 109.989 29.185 1.00 179.73 ? 192 PRO B N 1 +ATOM 3880 C CA . PRO B 1 193 ? 30.522 110.096 30.532 1.00 180.98 ? 192 PRO B CA 1 +ATOM 3881 C C . PRO B 1 193 ? 29.038 109.728 30.566 1.00 168.00 ? 192 PRO B C 1 +ATOM 3882 O O . PRO B 1 193 ? 28.285 110.055 29.646 1.00 130.54 ? 192 PRO B O 1 +ATOM 3883 C CB . PRO B 1 193 ? 30.726 111.573 30.882 1.00 170.96 ? 192 PRO B CB 1 +ATOM 3884 C CG . PRO B 1 193 ? 30.714 112.275 29.563 1.00 154.03 ? 192 PRO B CG 1 +ATOM 3885 C CD . PRO B 1 193 ? 31.294 111.309 28.557 1.00 163.16 ? 192 PRO B CD 1 +ATOM 3886 N N . VAL B 1 194 ? 28.629 109.037 31.623 1.00 155.69 ? 193 VAL B N 1 +ATOM 3887 C CA . VAL B 1 194 ? 27.247 108.604 31.757 1.00 142.91 ? 193 VAL B CA 1 +ATOM 3888 C C . VAL B 1 194 ? 26.644 109.227 33.009 1.00 131.43 ? 193 VAL B C 1 +ATOM 3889 O O . VAL B 1 194 ? 27.311 109.972 33.719 1.00 115.67 ? 193 VAL B O 1 +ATOM 3890 C CB . VAL B 1 194 ? 27.131 107.060 31.818 1.00 153.67 ? 193 VAL B CB 1 +ATOM 3891 C CG1 . VAL B 1 194 ? 27.783 106.418 30.594 1.00 114.14 ? 193 VAL B CG1 1 +ATOM 3892 C CG2 . VAL B 1 194 ? 27.747 106.523 33.102 1.00 142.88 ? 193 VAL B CG2 1 +ATOM 3893 N N . LEU B 1 195 ? 25.377 108.933 33.269 1.00 120.44 ? 194 LEU B N 1 +ATOM 3894 C CA . LEU B 1 195 ? 24.697 109.455 34.447 1.00 103.08 ? 194 LEU B CA 1 +ATOM 3895 C C . LEU B 1 195 ? 24.645 108.380 35.520 1.00 115.85 ? 194 LEU B C 1 +ATOM 3896 O O . LEU B 1 195 ? 24.270 107.244 35.246 1.00 136.79 ? 194 LEU B O 1 +ATOM 3897 C CB . LEU B 1 195 ? 23.287 109.922 34.083 1.00 93.64 ? 194 LEU B CB 1 +ATOM 3898 C CG . LEU B 1 195 ? 23.241 110.969 32.965 1.00 122.18 ? 194 LEU B CG 1 +ATOM 3899 C CD1 . LEU B 1 195 ? 21.804 111.344 32.612 1.00 119.52 ? 194 LEU B CD1 1 +ATOM 3900 C CD2 . LEU B 1 195 ? 24.065 112.206 33.331 1.00 90.62 ? 194 LEU B CD2 1 +ATOM 3901 N N . LEU B 1 196 ? 25.038 108.728 36.738 1.00 113.68 ? 195 LEU B N 1 +ATOM 3902 C CA . LEU B 1 196 ? 25.022 107.756 37.823 1.00 130.77 ? 195 LEU B CA 1 +ATOM 3903 C C . LEU B 1 196 ? 23.941 108.114 38.850 1.00 127.56 ? 195 LEU B C 1 +ATOM 3904 O O . LEU B 1 196 ? 24.120 109.010 39.675 1.00 128.45 ? 195 LEU B O 1 +ATOM 3905 C CB . LEU B 1 196 ? 26.419 107.616 38.441 1.00 151.09 ? 195 LEU B CB 1 +ATOM 3906 C CG . LEU B 1 196 ? 27.511 107.330 37.395 1.00 127.78 ? 195 LEU B CG 1 +ATOM 3907 C CD1 . LEU B 1 196 ? 28.900 107.307 38.007 1.00 116.90 ? 195 LEU B CD1 1 +ATOM 3908 C CD2 . LEU B 1 196 ? 27.237 106.031 36.645 1.00 123.86 ? 195 LEU B CD2 1 +ATOM 3909 N N . PRO B 1 197 ? 22.806 107.397 38.791 1.00 119.57 ? 196 PRO B N 1 +ATOM 3910 C CA . PRO B 1 197 ? 21.542 107.723 39.469 1.00 115.27 ? 196 PRO B CA 1 +ATOM 3911 C C . PRO B 1 197 ? 21.531 107.585 40.989 1.00 116.17 ? 196 PRO B C 1 +ATOM 3912 O O . PRO B 1 197 ? 22.248 106.767 41.560 1.00 120.67 ? 196 PRO B O 1 +ATOM 3913 C CB . PRO B 1 197 ? 20.567 106.701 38.879 1.00 107.83 ? 196 PRO B CB 1 +ATOM 3914 C CG . PRO B 1 197 ? 21.428 105.540 38.515 1.00 106.51 ? 196 PRO B CG 1 +ATOM 3915 C CD . PRO B 1 197 ? 22.710 106.142 38.025 1.00 100.22 ? 196 PRO B CD 1 +ATOM 3916 N N . ASP B 1 198 ? 20.695 108.392 41.632 1.00 122.12 ? 197 ASP B N 1 +ATOM 3917 C CA . ASP B 1 198 ? 20.320 108.165 43.019 1.00 134.04 ? 197 ASP B CA 1 +ATOM 3918 C C . ASP B 1 198 ? 19.341 107.004 43.037 1.00 113.19 ? 197 ASP B C 1 +ATOM 3919 O O . ASP B 1 198 ? 18.751 106.683 42.010 1.00 112.54 ? 197 ASP B O 1 +ATOM 3920 C CB . ASP B 1 198 ? 19.645 109.406 43.601 1.00 140.58 ? 197 ASP B CB 1 +ATOM 3921 C CG . ASP B 1 198 ? 20.633 110.504 43.942 1.00 151.69 ? 197 ASP B CG 1 +ATOM 3922 O OD1 . ASP B 1 198 ? 21.837 110.195 44.077 1.00 153.15 ? 197 ASP B OD1 1 +ATOM 3923 O OD2 . ASP B 1 198 ? 20.199 111.669 44.085 1.00 136.37 ? 197 ASP B OD2 1 +ATOM 3924 N N . ASN B 1 199 ? 19.167 106.375 44.193 1.00 104.67 ? 198 ASN B N 1 +ATOM 3925 C CA . ASN B 1 199 ? 18.189 105.304 44.329 1.00 124.01 ? 198 ASN B CA 1 +ATOM 3926 C C . ASN B 1 199 ? 16.821 105.693 43.788 1.00 120.50 ? 198 ASN B C 1 +ATOM 3927 O O . ASN B 1 199 ? 16.225 106.662 44.256 1.00 113.96 ? 198 ASN B O 1 +ATOM 3928 C CB . ASN B 1 199 ? 18.011 104.924 45.790 1.00 140.81 ? 198 ASN B CB 1 +ATOM 3929 C CG . ASN B 1 199 ? 19.249 104.335 46.406 1.00 140.70 ? 198 ASN B CG 1 +ATOM 3930 O OD1 . ASN B 1 199 ? 20.310 104.298 45.786 1.00 101.62 ? 198 ASN B OD1 1 +ATOM 3931 N ND2 . ASN B 1 199 ? 19.126 103.876 47.647 1.00 135.66 ? 198 ASN B ND2 1 +ATOM 3932 N N . HIS B 1 200 ? 16.340 104.935 42.803 1.00 116.76 ? 199 HIS B N 1 +ATOM 3933 C CA . HIS B 1 200 ? 14.947 105.007 42.358 1.00 110.62 ? 199 HIS B CA 1 +ATOM 3934 C C . HIS B 1 200 ? 14.489 103.643 41.873 1.00 96.74 ? 199 HIS B C 1 +ATOM 3935 O O . HIS B 1 200 ? 15.149 102.649 42.140 1.00 93.61 ? 199 HIS B O 1 +ATOM 3936 C CB . HIS B 1 200 ? 14.770 106.033 41.250 1.00 96.81 ? 199 HIS B CB 1 +ATOM 3937 C CG . HIS B 1 200 ? 15.492 105.693 39.988 1.00 93.42 ? 199 HIS B CG 1 +ATOM 3938 N ND1 . HIS B 1 200 ? 16.831 105.959 39.807 1.00 102.38 ? 199 HIS B ND1 1 +ATOM 3939 C CD2 . HIS B 1 200 ? 15.061 105.128 38.837 1.00 105.25 ? 199 HIS B CD2 1 +ATOM 3940 C CE1 . HIS B 1 200 ? 17.196 105.566 38.600 1.00 106.89 ? 199 HIS B CE1 1 +ATOM 3941 N NE2 . HIS B 1 200 ? 16.140 105.059 37.990 1.00 112.17 ? 199 HIS B NE2 1 +ATOM 3942 N N . TYR B 1 201 ? 13.369 103.586 41.159 1.00 95.37 ? 200 TYR B N 1 +ATOM 3943 C CA . TYR B 1 201 ? 12.864 102.297 40.682 1.00 98.52 ? 200 TYR B CA 1 +ATOM 3944 C C . TYR B 1 201 ? 12.006 102.392 39.417 1.00 89.02 ? 200 TYR B C 1 +ATOM 3945 O O . TYR B 1 201 ? 11.442 103.439 39.134 1.00 93.50 ? 200 TYR B O 1 +ATOM 3946 C CB . TYR B 1 201 ? 12.126 101.564 41.812 1.00 96.25 ? 200 TYR B CB 1 +ATOM 3947 C CG . TYR B 1 201 ? 10.765 102.116 42.175 1.00 97.78 ? 200 TYR B CG 1 +ATOM 3948 C CD1 . TYR B 1 201 ? 10.634 103.252 42.961 1.00 99.86 ? 200 TYR B CD1 1 +ATOM 3949 C CD2 . TYR B 1 201 ? 9.607 101.480 41.754 1.00 104.44 ? 200 TYR B CD2 1 +ATOM 3950 C CE1 . TYR B 1 201 ? 9.382 103.749 43.305 1.00 96.05 ? 200 TYR B CE1 1 +ATOM 3951 C CE2 . TYR B 1 201 ? 8.353 101.970 42.093 1.00 119.64 ? 200 TYR B CE2 1 +ATOM 3952 C CZ . TYR B 1 201 ? 8.247 103.107 42.869 1.00 102.97 ? 200 TYR B CZ 1 +ATOM 3953 O OH . TYR B 1 201 ? 7.007 103.603 43.206 1.00 88.25 ? 200 TYR B OH 1 +ATOM 3954 N N . LEU B 1 202 ? 11.932 101.310 38.642 1.00 99.68 ? 201 LEU B N 1 +ATOM 3955 C CA . LEU B 1 202 ? 11.074 101.288 37.459 1.00 102.44 ? 201 LEU B CA 1 +ATOM 3956 C C . LEU B 1 202 ? 9.815 100.475 37.753 1.00 87.38 ? 201 LEU B C 1 +ATOM 3957 O O . LEU B 1 202 ? 9.886 99.346 38.221 1.00 83.33 ? 201 LEU B O 1 +ATOM 3958 C CB . LEU B 1 202 ? 11.814 100.737 36.229 1.00 74.13 ? 201 LEU B CB 1 +ATOM 3959 C CG . LEU B 1 202 ? 13.185 101.300 35.817 1.00 88.43 ? 201 LEU B CG 1 +ATOM 3960 C CD1 . LEU B 1 202 ? 13.579 100.834 34.427 1.00 88.44 ? 201 LEU B CD1 1 +ATOM 3961 C CD2 . LEU B 1 202 ? 13.263 102.815 35.890 1.00 110.32 ? 201 LEU B CD2 1 +ATOM 3962 N N . SER B 1 203 ? 8.660 101.072 37.510 1.00 80.39 ? 202 SER B N 1 +ATOM 3963 C CA . SER B 1 203 ? 7.401 100.390 37.731 1.00 85.39 ? 202 SER B CA 1 +ATOM 3964 C C . SER B 1 203 ? 7.017 99.752 36.412 1.00 75.92 ? 202 SER B C 1 +ATOM 3965 O O . SER B 1 203 ? 6.655 100.455 35.467 1.00 101.60 ? 202 SER B O 1 +ATOM 3966 C CB . SER B 1 203 ? 6.331 101.391 38.164 1.00 75.39 ? 202 SER B CB 1 +ATOM 3967 O OG . SER B 1 203 ? 5.112 100.741 38.470 1.00 104.16 ? 202 SER B OG 1 +ATOM 3968 N N . THR B 1 204 ? 7.109 98.426 36.349 1.00 81.40 ? 203 THR B N 1 +ATOM 3969 C CA . THR B 1 204 ? 6.846 97.690 35.118 1.00 93.76 ? 203 THR B CA 1 +ATOM 3970 C C . THR B 1 204 ? 5.487 97.011 35.151 1.00 92.70 ? 203 THR B C 1 +ATOM 3971 O O . THR B 1 204 ? 5.081 96.481 36.184 1.00 98.00 ? 203 THR B O 1 +ATOM 3972 C CB . THR B 1 204 ? 7.908 96.603 34.857 1.00 85.47 ? 203 THR B CB 1 +ATOM 3973 O OG1 . THR B 1 204 ? 9.215 97.178 34.915 1.00 81.95 ? 203 THR B OG1 1 +ATOM 3974 C CG2 . THR B 1 204 ? 7.713 96.001 33.480 1.00 133.04 ? 203 THR B CG2 1 +ATOM 3975 N N . GLN B 1 205 ? 4.785 97.046 34.019 1.00 78.37 ? 204 GLN B N 1 +ATOM 3976 C CA . GLN B 1 205 ? 3.593 96.229 33.803 1.00 78.60 ? 204 GLN B CA 1 +ATOM 3977 C C . GLN B 1 205 ? 3.641 95.614 32.402 1.00 85.98 ? 204 GLN B C 1 +ATOM 3978 O O . GLN B 1 205 ? 4.088 96.257 31.450 1.00 74.02 ? 204 GLN B O 1 +ATOM 3979 C CB . GLN B 1 205 ? 2.316 97.056 33.956 1.00 90.19 ? 204 GLN B CB 1 +ATOM 3980 C CG . GLN B 1 205 ? 2.273 97.974 35.161 1.00 74.14 ? 204 GLN B CG 1 +ATOM 3981 C CD . GLN B 1 205 ? 1.728 99.332 34.803 1.00 99.41 ? 204 GLN B CD 1 +ATOM 3982 O OE1 . GLN B 1 205 ? 0.510 99.526 34.739 1.00 148.60 ? 204 GLN B OE1 1 +ATOM 3983 N NE2 . GLN B 1 205 ? 2.628 100.285 34.542 1.00 100.33 ? 204 GLN B NE2 1 +ATOM 3984 N N . SER B 1 206 ? 3.153 94.378 32.286 1.00 88.12 ? 205 SER B N 1 +ATOM 3985 C CA . SER B 1 206 ? 3.351 93.549 31.093 1.00 71.29 ? 205 SER B CA 1 +ATOM 3986 C C . SER B 1 206 ? 2.179 92.592 30.785 1.00 58.63 ? 205 SER B C 1 +ATOM 3987 O O . SER B 1 206 ? 1.461 92.154 31.681 1.00 81.38 ? 205 SER B O 1 +ATOM 3988 C CB . SER B 1 206 ? 4.671 92.769 31.214 1.00 69.98 ? 205 SER B CB 1 +ATOM 3989 O OG . SER B 1 206 ? 5.789 93.646 31.236 1.00 94.17 ? 205 SER B OG 1 +ATOM 3990 N N . ASN B 1 207 ? 1.978 92.297 29.500 1.00 76.32 ? 206 ASN B N 1 +ATOM 3991 C CA . ASN B 1 207 ? 0.970 91.323 29.077 1.00 77.89 ? 206 ASN B CA 1 +ATOM 3992 C C . ASN B 1 207 ? 1.533 90.449 27.967 1.00 83.32 ? 206 ASN B C 1 +ATOM 3993 O O . ASN B 1 207 ? 2.228 90.938 27.077 1.00 73.43 ? 206 ASN B O 1 +ATOM 3994 C CB . ASN B 1 207 ? -0.356 92.013 28.690 1.00 69.43 ? 206 ASN B CB 1 +ATOM 3995 C CG . ASN B 1 207 ? -1.127 91.289 27.582 1.00 63.78 ? 206 ASN B CG 1 +ATOM 3996 O OD1 . ASN B 1 207 ? -0.718 91.303 26.426 1.00 68.25 ? 206 ASN B OD1 1 +ATOM 3997 N ND2 . ASN B 1 207 ? -2.282 90.717 27.924 1.00 75.38 ? 206 ASN B ND2 1 +ATOM 3998 N N . LEU B 1 208 ? 1.253 89.152 28.056 1.00 75.45 ? 207 LEU B N 1 +ATOM 3999 C CA . LEU B 1 208 ? 1.739 88.176 27.090 1.00 58.76 ? 207 LEU B CA 1 +ATOM 4000 C C . LEU B 1 208 ? 0.579 87.651 26.249 1.00 51.04 ? 207 LEU B C 1 +ATOM 4001 O O . LEU B 1 208 ? -0.471 87.261 26.778 1.00 70.78 ? 207 LEU B O 1 +ATOM 4002 C CB . LEU B 1 208 ? 2.422 87.007 27.803 1.00 63.96 ? 207 LEU B CB 1 +ATOM 4003 C CG . LEU B 1 208 ? 3.352 87.311 28.976 1.00 63.77 ? 207 LEU B CG 1 +ATOM 4004 C CD1 . LEU B 1 208 ? 3.782 86.026 29.630 1.00 78.16 ? 207 LEU B CD1 1 +ATOM 4005 C CD2 . LEU B 1 208 ? 4.558 88.100 28.524 1.00 72.67 ? 207 LEU B CD2 1 +ATOM 4006 N N . SER B 1 209 ? 0.785 87.637 24.937 1.00 68.00 ? 208 SER B N 1 +ATOM 4007 C CA . SER B 1 209 ? -0.229 87.161 24.007 1.00 61.41 ? 208 SER B CA 1 +ATOM 4008 C C . SER B 1 209 ? 0.325 86.442 22.786 1.00 77.93 ? 208 SER B C 1 +ATOM 4009 O O . SER B 1 209 ? 1.540 86.387 22.548 1.00 66.21 ? 208 SER B O 1 +ATOM 4010 C CB . SER B 1 209 ? -1.070 88.329 23.519 1.00 67.06 ? 208 SER B CB 1 +ATOM 4011 O OG . SER B 1 209 ? -0.220 89.327 22.990 1.00 92.86 ? 208 SER B OG 1 +ATOM 4012 N N . LYS B 1 210 ? -0.614 85.910 22.010 1.00 81.87 ? 209 LYS B N 1 +ATOM 4013 C CA . LYS B 1 210 ? -0.329 85.280 20.736 1.00 61.84 ? 209 LYS B CA 1 +ATOM 4014 C C . LYS B 1 210 ? -0.868 86.114 19.577 1.00 67.30 ? 209 LYS B C 1 +ATOM 4015 O O . LYS B 1 210 ? -1.769 86.930 19.739 1.00 90.33 ? 209 LYS B O 1 +ATOM 4016 C CB . LYS B 1 210 ? -0.957 83.885 20.682 1.00 88.65 ? 209 LYS B CB 1 +ATOM 4017 C CG . LYS B 1 210 ? -0.549 82.938 21.806 1.00 78.23 ? 209 LYS B CG 1 +ATOM 4018 C CD . LYS B 1 210 ? 0.920 82.588 21.745 1.00 69.56 ? 209 LYS B CD 1 +ATOM 4019 C CE . LYS B 1 210 ? 1.260 81.439 22.678 1.00 69.70 ? 209 LYS B CE 1 +ATOM 4020 N NZ . LYS B 1 210 ? 2.731 81.352 22.864 1.00 73.21 ? 209 LYS B NZ 1 +ATOM 4021 N N . ASP B 1 211 ? -0.277 85.884 18.412 1.00 82.63 ? 210 ASP B N 1 +ATOM 4022 C CA . ASP B 1 211 ? -0.700 86.391 17.115 1.00 69.09 ? 210 ASP B CA 1 +ATOM 4023 C C . ASP B 1 211 ? -1.406 85.233 16.421 1.00 91.52 ? 210 ASP B C 1 +ATOM 4024 O O . ASP B 1 211 ? -0.837 84.152 16.292 1.00 93.89 ? 210 ASP B O 1 +ATOM 4025 C CB . ASP B 1 211 ? 0.559 86.790 16.342 1.00 72.45 ? 210 ASP B CB 1 +ATOM 4026 C CG . ASP B 1 211 ? 0.305 87.101 14.874 1.00 103.04 ? 210 ASP B CG 1 +ATOM 4027 O OD1 . ASP B 1 211 ? -0.850 87.035 14.402 1.00 104.44 ? 210 ASP B OD1 1 +ATOM 4028 O OD2 . ASP B 1 211 ? 1.297 87.437 14.189 1.00 76.25 ? 210 ASP B OD2 1 +ATOM 4029 N N . PRO B 1 212 ? -2.651 85.445 15.966 1.00 117.85 ? 211 PRO B N 1 +ATOM 4030 C CA . PRO B 1 212 ? -3.387 84.278 15.461 1.00 104.84 ? 211 PRO B CA 1 +ATOM 4031 C C . PRO B 1 212 ? -3.038 83.850 14.018 1.00 99.67 ? 211 PRO B C 1 +ATOM 4032 O O . PRO B 1 212 ? -3.560 82.839 13.552 1.00 88.37 ? 211 PRO B O 1 +ATOM 4033 C CB . PRO B 1 212 ? -4.850 84.709 15.598 1.00 89.58 ? 211 PRO B CB 1 +ATOM 4034 C CG . PRO B 1 212 ? -4.804 86.205 15.438 1.00 108.57 ? 211 PRO B CG 1 +ATOM 4035 C CD . PRO B 1 212 ? -3.479 86.667 15.995 1.00 88.01 ? 211 PRO B CD 1 +ATOM 4036 N N . ASN B 1 213 ? -2.164 84.589 13.333 1.00 126.46 ? 212 ASN B N 1 +ATOM 4037 C CA . ASN B 1 213 ? -1.660 84.166 12.017 1.00 131.20 ? 212 ASN B CA 1 +ATOM 4038 C C . ASN B 1 213 ? -0.214 83.689 12.085 1.00 112.13 ? 212 ASN B C 1 +ATOM 4039 O O . ASN B 1 213 ? 0.493 83.645 11.074 1.00 107.80 ? 212 ASN B O 1 +ATOM 4040 C CB . ASN B 1 213 ? -1.726 85.293 10.987 1.00 111.61 ? 212 ASN B CB 1 +ATOM 4041 C CG . ASN B 1 213 ? -3.002 86.086 11.058 1.00 105.38 ? 212 ASN B CG 1 +ATOM 4042 O OD1 . ASN B 1 213 ? -4.093 85.538 11.236 1.00 103.70 ? 212 ASN B OD1 1 +ATOM 4043 N ND2 . ASN B 1 213 ? -2.871 87.399 10.913 1.00 99.79 ? 212 ASN B ND2 1 +ATOM 4044 N N . GLU B 1 214 ? 0.238 83.372 13.285 1.00 107.46 ? 213 GLU B N 1 +ATOM 4045 C CA . GLU B 1 214 ? 1.571 82.849 13.452 1.00 78.16 ? 213 GLU B CA 1 +ATOM 4046 C C . GLU B 1 214 ? 1.457 81.400 13.854 1.00 90.97 ? 213 GLU B C 1 +ATOM 4047 O O . GLU B 1 214 ? 0.696 81.062 14.758 1.00 97.77 ? 213 GLU B O 1 +ATOM 4048 C CB . GLU B 1 214 ? 2.340 83.623 14.509 1.00 78.14 ? 213 GLU B CB 1 +ATOM 4049 C CG . GLU B 1 214 ? 3.730 83.113 14.659 1.00 80.93 ? 213 GLU B CG 1 +ATOM 4050 C CD . GLU B 1 214 ? 4.432 83.028 13.324 1.00 111.50 ? 213 GLU B CD 1 +ATOM 4051 O OE1 . GLU B 1 214 ? 4.317 81.981 12.650 1.00 124.98 ? 213 GLU B OE1 1 +ATOM 4052 O OE2 . GLU B 1 214 ? 5.101 84.010 12.945 1.00 88.90 ? 213 GLU B OE2 1 +ATOM 4053 N N . LYS B 1 215 ? 2.200 80.543 13.164 1.00 92.89 ? 214 LYS B N 1 +ATOM 4054 C CA . LYS B 1 215 ? 2.118 79.109 13.399 1.00 97.94 ? 214 LYS B CA 1 +ATOM 4055 C C . LYS B 1 215 ? 3.376 78.577 14.084 1.00 90.37 ? 214 LYS B C 1 +ATOM 4056 O O . LYS B 1 215 ? 3.354 77.503 14.679 1.00 103.28 ? 214 LYS B O 1 +ATOM 4057 C CB . LYS B 1 215 ? 1.845 78.361 12.088 1.00 89.22 ? 214 LYS B CB 1 +ATOM 4058 C CG . LYS B 1 215 ? 0.592 78.825 11.336 1.00 129.32 ? 214 LYS B CG 1 +ATOM 4059 C CD . LYS B 1 215 ? 0.157 77.813 10.256 1.00 146.28 ? 214 LYS B CD 1 +ATOM 4060 C CE . LYS B 1 215 ? 0.971 77.899 8.953 1.00 143.53 ? 214 LYS B CE 1 +ATOM 4061 N NZ . LYS B 1 215 ? 0.385 78.831 7.947 1.00 123.15 ? 214 LYS B NZ 1 +ATOM 4062 N N . ARG B 1 216 ? 4.462 79.344 13.996 1.00 72.85 ? 215 ARG B N 1 +ATOM 4063 C CA . ARG B 1 216 ? 5.709 79.072 14.718 1.00 60.81 ? 215 ARG B CA 1 +ATOM 4064 C C . ARG B 1 216 ? 5.608 79.418 16.218 1.00 81.41 ? 215 ARG B C 1 +ATOM 4065 O O . ARG B 1 216 ? 4.712 80.152 16.629 1.00 88.12 ? 215 ARG B O 1 +ATOM 4066 C CB . ARG B 1 216 ? 6.842 79.879 14.086 1.00 67.19 ? 215 ARG B CB 1 +ATOM 4067 C CG . ARG B 1 216 ? 7.227 79.458 12.675 1.00 83.32 ? 215 ARG B CG 1 +ATOM 4068 C CD . ARG B 1 216 ? 8.157 80.487 12.054 1.00 81.93 ? 215 ARG B CD 1 +ATOM 4069 N NE . ARG B 1 216 ? 7.427 81.682 11.640 1.00 114.49 ? 215 ARG B NE 1 +ATOM 4070 C CZ . ARG B 1 216 ? 7.973 82.778 11.115 1.00 116.70 ? 215 ARG B CZ 1 +ATOM 4071 N NH1 . ARG B 1 216 ? 9.287 82.864 10.929 1.00 106.30 ? 215 ARG B NH1 1 +ATOM 4072 N NH2 . ARG B 1 216 ? 7.193 83.799 10.778 1.00 79.26 ? 215 ARG B NH2 1 +ATOM 4073 N N . ASP B 1 217 ? 6.525 78.911 17.042 1.00 69.28 ? 216 ASP B N 1 +ATOM 4074 C CA . ASP B 1 217 ? 6.435 79.163 18.485 1.00 80.81 ? 216 ASP B CA 1 +ATOM 4075 C C . ASP B 1 217 ? 6.859 80.596 18.819 1.00 95.89 ? 216 ASP B C 1 +ATOM 4076 O O . ASP B 1 217 ? 8.015 80.986 18.619 1.00 81.90 ? 216 ASP B O 1 +ATOM 4077 C CB . ASP B 1 217 ? 7.228 78.129 19.302 1.00 83.91 ? 216 ASP B CB 1 +ATOM 4078 C CG . ASP B 1 217 ? 6.652 77.910 20.711 1.00 108.17 ? 216 ASP B CG 1 +ATOM 4079 O OD1 . ASP B 1 217 ? 5.502 78.328 20.970 1.00 109.16 ? 216 ASP B OD1 1 +ATOM 4080 O OD2 . ASP B 1 217 ? 7.347 77.306 21.560 1.00 84.94 ? 216 ASP B OD2 1 +ATOM 4081 N N . HIS B 1 218 ? 5.901 81.363 19.336 1.00 89.81 ? 217 HIS B N 1 +ATOM 4082 C CA . HIS B 1 218 ? 6.052 82.803 19.484 1.00 74.02 ? 217 HIS B CA 1 +ATOM 4083 C C . HIS B 1 218 ? 5.415 83.407 20.749 1.00 70.96 ? 217 HIS B C 1 +ATOM 4084 O O . HIS B 1 218 ? 4.521 82.829 21.374 1.00 80.54 ? 217 HIS B O 1 +ATOM 4085 C CB . HIS B 1 218 ? 5.481 83.505 18.245 1.00 66.75 ? 217 HIS B CB 1 +ATOM 4086 C CG . HIS B 1 218 ? 3.990 83.547 18.224 1.00 62.05 ? 217 HIS B CG 1 +ATOM 4087 N ND1 . HIS B 1 218 ? 3.216 82.410 18.126 1.00 104.20 ? 217 HIS B ND1 1 +ATOM 4088 C CD2 . HIS B 1 218 ? 3.125 84.581 18.331 1.00 92.96 ? 217 HIS B CD2 1 +ATOM 4089 C CE1 . HIS B 1 218 ? 1.940 82.745 18.161 1.00 75.91 ? 217 HIS B CE1 1 +ATOM 4090 N NE2 . HIS B 1 218 ? 1.857 84.055 18.287 1.00 85.98 ? 217 HIS B NE2 1 +ATOM 4091 N N . MET B 1 219 ? 5.894 84.591 21.107 1.00 78.18 ? 218 MET B N 1 +ATOM 4092 C CA . MET B 1 219 ? 5.285 85.397 22.152 1.00 68.82 ? 218 MET B CA 1 +ATOM 4093 C C . MET B 1 219 ? 5.187 86.854 21.684 1.00 84.71 ? 218 MET B C 1 +ATOM 4094 O O . MET B 1 219 ? 6.168 87.411 21.170 1.00 82.97 ? 218 MET B O 1 +ATOM 4095 C CB . MET B 1 219 ? 6.117 85.312 23.429 1.00 55.35 ? 218 MET B CB 1 +ATOM 4096 C CG . MET B 1 219 ? 5.614 86.169 24.565 1.00 46.76 ? 218 MET B CG 1 +ATOM 4097 S SD . MET B 1 219 ? 6.711 86.203 25.996 1.00 80.77 ? 218 MET B SD 1 +ATOM 4098 C CE . MET B 1 219 ? 8.149 87.090 25.392 1.00 68.27 ? 218 MET B CE 1 +ATOM 4099 N N . VAL B 1 220 ? 4.002 87.449 21.841 1.00 72.75 ? 219 VAL B N 1 +ATOM 4100 C CA . VAL B 1 220 ? 3.815 88.895 21.679 1.00 78.25 ? 219 VAL B CA 1 +ATOM 4101 C C . VAL B 1 220 ? 3.896 89.572 23.049 1.00 60.88 ? 219 VAL B C 1 +ATOM 4102 O O . VAL B 1 220 ? 3.041 89.343 23.910 1.00 76.82 ? 219 VAL B O 1 +ATOM 4103 C CB . VAL B 1 220 ? 2.454 89.258 21.027 1.00 75.44 ? 219 VAL B CB 1 +ATOM 4104 C CG1 . VAL B 1 220 ? 2.485 90.676 20.518 1.00 67.25 ? 219 VAL B CG1 1 +ATOM 4105 C CG2 . VAL B 1 220 ? 2.124 88.318 19.883 1.00 77.08 ? 219 VAL B CG2 1 +ATOM 4106 N N . LEU B 1 221 ? 4.925 90.402 23.237 1.00 76.96 ? 220 LEU B N 1 +ATOM 4107 C CA . LEU B 1 221 ? 5.205 91.065 24.519 1.00 66.53 ? 220 LEU B CA 1 +ATOM 4108 C C . LEU B 1 221 ? 4.881 92.563 24.517 1.00 80.73 ? 220 LEU B C 1 +ATOM 4109 O O . LEU B 1 221 ? 5.407 93.313 23.697 1.00 93.73 ? 220 LEU B O 1 +ATOM 4110 C CB . LEU B 1 221 ? 6.678 90.870 24.919 1.00 61.26 ? 220 LEU B CB 1 +ATOM 4111 C CG . LEU B 1 221 ? 7.186 91.647 26.146 1.00 74.12 ? 220 LEU B CG 1 +ATOM 4112 C CD1 . LEU B 1 221 ? 6.517 91.147 27.403 1.00 62.22 ? 220 LEU B CD1 1 +ATOM 4113 C CD2 . LEU B 1 221 ? 8.705 91.614 26.316 1.00 70.42 ? 220 LEU B CD2 1 +ATOM 4114 N N . LEU B 1 222 ? 4.027 92.990 25.446 1.00 124.35 ? 221 LEU B N 1 +ATOM 4115 C CA . LEU B 1 222 ? 3.759 94.412 25.675 1.00 77.51 ? 221 LEU B CA 1 +ATOM 4116 C C . LEU B 1 222 ? 4.200 94.866 27.064 1.00 88.22 ? 221 LEU B C 1 +ATOM 4117 O O . LEU B 1 222 ? 3.671 94.408 28.075 1.00 80.74 ? 221 LEU B O 1 +ATOM 4118 C CB . LEU B 1 222 ? 2.277 94.724 25.493 1.00 75.83 ? 221 LEU B CB 1 +ATOM 4119 C CG . LEU B 1 222 ? 1.691 94.556 24.097 1.00 86.09 ? 221 LEU B CG 1 +ATOM 4120 C CD1 . LEU B 1 222 ? 0.200 94.759 24.120 1.00 56.83 ? 221 LEU B CD1 1 +ATOM 4121 C CD2 . LEU B 1 222 ? 2.318 95.576 23.198 1.00 76.23 ? 221 LEU B CD2 1 +ATOM 4122 N N . GLU B 1 223 ? 5.169 95.776 27.090 1.00 73.79 ? 222 GLU B N 1 +ATOM 4123 C CA . GLU B 1 223 ? 5.707 96.328 28.328 1.00 89.53 ? 222 GLU B CA 1 +ATOM 4124 C C . GLU B 1 223 ? 5.388 97.800 28.545 1.00 78.40 ? 222 GLU B C 1 +ATOM 4125 O O . GLU B 1 223 ? 5.518 98.621 27.633 1.00 91.37 ? 222 GLU B O 1 +ATOM 4126 C CB . GLU B 1 223 ? 7.223 96.191 28.340 1.00 77.17 ? 222 GLU B CB 1 +ATOM 4127 C CG . GLU B 1 223 ? 7.732 94.942 29.002 1.00 129.95 ? 222 GLU B CG 1 +ATOM 4128 C CD . GLU B 1 223 ? 9.247 94.941 29.188 1.00 164.32 ? 222 GLU B CD 1 +ATOM 4129 O OE1 . GLU B 1 223 ? 9.844 96.034 29.354 1.00 162.16 ? 222 GLU B OE1 1 +ATOM 4130 O OE2 . GLU B 1 223 ? 9.836 93.836 29.169 1.00 161.32 ? 222 GLU B OE2 1 +ATOM 4131 N N . PHE B 1 224 ? 4.998 98.132 29.768 1.00 85.10 ? 223 PHE B N 1 +ATOM 4132 C CA . PHE B 1 224 ? 4.938 99.522 30.200 1.00 73.93 ? 223 PHE B CA 1 +ATOM 4133 C C . PHE B 1 224 ? 6.025 99.707 31.259 1.00 59.73 ? 223 PHE B C 1 +ATOM 4134 O O . PHE B 1 224 ? 6.180 98.865 32.138 1.00 102.45 ? 223 PHE B O 1 +ATOM 4135 C CB . PHE B 1 224 ? 3.569 99.860 30.799 1.00 79.30 ? 223 PHE B CB 1 +ATOM 4136 C CG . PHE B 1 224 ? 2.396 99.502 29.920 1.00 88.57 ? 223 PHE B CG 1 +ATOM 4137 C CD1 . PHE B 1 224 ? 2.525 99.411 28.530 1.00 76.29 ? 223 PHE B CD1 1 +ATOM 4138 C CD2 . PHE B 1 224 ? 1.150 99.267 30.497 1.00 62.35 ? 223 PHE B CD2 1 +ATOM 4139 C CE1 . PHE B 1 224 ? 1.440 99.078 27.735 1.00 63.81 ? 223 PHE B CE1 1 +ATOM 4140 C CE2 . PHE B 1 224 ? 0.059 98.936 29.714 1.00 85.34 ? 223 PHE B CE2 1 +ATOM 4141 C CZ . PHE B 1 224 ? 0.202 98.847 28.327 1.00 90.69 ? 223 PHE B CZ 1 +ATOM 4142 N N . VAL B 1 225 ? 6.808 100.778 31.167 1.00 87.91 ? 224 VAL B N 1 +ATOM 4143 C CA . VAL B 1 225 ? 7.864 101.018 32.150 1.00 88.34 ? 224 VAL B CA 1 +ATOM 4144 C C . VAL B 1 225 ? 7.968 102.493 32.535 1.00 101.16 ? 224 VAL B C 1 +ATOM 4145 O O . VAL B 1 225 ? 8.246 103.336 31.679 1.00 83.60 ? 224 VAL B O 1 +ATOM 4146 C CB . VAL B 1 225 ? 9.251 100.602 31.621 1.00 84.98 ? 224 VAL B CB 1 +ATOM 4147 C CG1 . VAL B 1 225 ? 10.223 100.463 32.779 1.00 76.40 ? 224 VAL B CG1 1 +ATOM 4148 C CG2 . VAL B 1 225 ? 9.186 99.308 30.816 1.00 83.83 ? 224 VAL B CG2 1 +ATOM 4149 N N . THR B 1 226 ? 7.766 102.800 33.819 1.00 89.42 ? 225 THR B N 1 +ATOM 4150 C CA . THR B 1 226 ? 7.897 104.176 34.316 1.00 90.21 ? 225 THR B CA 1 +ATOM 4151 C C . THR B 1 226 ? 8.841 104.322 35.521 1.00 81.14 ? 225 THR B C 1 +ATOM 4152 O O . THR B 1 226 ? 8.661 103.665 36.539 1.00 88.40 ? 225 THR B O 1 +ATOM 4153 C CB . THR B 1 226 ? 6.528 104.796 34.713 1.00 87.16 ? 225 THR B CB 1 +ATOM 4154 O OG1 . THR B 1 226 ? 5.518 104.440 33.761 1.00 72.08 ? 225 THR B OG1 1 +ATOM 4155 C CG2 . THR B 1 226 ? 6.644 106.304 34.772 1.00 98.66 ? 225 THR B CG2 1 +ATOM 4156 N N . ALA B 1 227 ? 9.835 105.199 35.408 1.00 84.18 ? 226 ALA B N 1 +ATOM 4157 C CA . ALA B 1 227 ? 10.697 105.538 36.547 1.00 86.80 ? 226 ALA B CA 1 +ATOM 4158 C C . ALA B 1 227 ? 9.939 106.326 37.641 1.00 102.55 ? 226 ALA B C 1 +ATOM 4159 O O . ALA B 1 227 ? 8.948 107.002 37.353 1.00 106.58 ? 226 ALA B O 1 +ATOM 4160 C CB . ALA B 1 227 ? 11.923 106.301 36.064 1.00 91.78 ? 226 ALA B CB 1 +ATOM 4161 N N . ALA B 1 228 ? 10.412 106.239 38.887 1.00 100.30 ? 227 ALA B N 1 +ATOM 4162 C CA . ALA B 1 228 ? 9.661 106.722 40.053 1.00 95.81 ? 227 ALA B CA 1 +ATOM 4163 C C . ALA B 1 228 ? 10.562 106.779 41.281 1.00 103.63 ? 227 ALA B C 1 +ATOM 4164 O O . ALA B 1 228 ? 11.775 106.700 41.150 1.00 96.74 ? 227 ALA B O 1 +ATOM 4165 C CB . ALA B 1 228 ? 8.480 105.804 40.325 1.00 83.79 ? 227 ALA B CB 1 +ATOM 4166 N N . GLY B 1 229 ? 9.967 106.924 42.466 1.00 109.61 ? 228 GLY B N 1 +ATOM 4167 C CA . GLY B 1 229 ? 10.686 106.758 43.726 1.00 124.59 ? 228 GLY B CA 1 +ATOM 4168 C C . GLY B 1 229 ? 11.688 107.811 44.173 1.00 134.35 ? 228 GLY B C 1 +ATOM 4169 O O . GLY B 1 229 ? 12.425 107.608 45.143 1.00 127.23 ? 228 GLY B O 1 +ATOM 4170 N N . ILE B 1 230 ? 11.736 108.920 43.446 1.00 133.05 ? 229 ILE B N 1 +ATOM 4171 C CA . ILE B 1 230 ? 12.384 110.144 43.902 1.00 136.68 ? 229 ILE B CA 1 +ATOM 4172 C C . ILE B 1 230 ? 11.261 111.176 43.998 1.00 209.44 ? 229 ILE B C 1 +ATOM 4173 O O . ILE B 1 230 ? 10.406 111.231 43.111 1.00 240.51 ? 229 ILE B O 1 +ATOM 4174 C CB . ILE B 1 230 ? 13.448 110.628 42.889 1.00 122.13 ? 229 ILE B CB 1 +ATOM 4175 C CG1 . ILE B 1 230 ? 14.668 109.711 42.911 1.00 115.45 ? 229 ILE B CG1 1 +ATOM 4176 C CG2 . ILE B 1 230 ? 13.872 112.061 43.174 1.00 143.67 ? 229 ILE B CG2 1 +ATOM 4177 C CD1 . ILE B 1 230 ? 15.678 110.034 41.837 1.00 108.76 ? 229 ILE B CD1 1 +ATOM 4178 N N . THR B 1 231 ? 11.242 111.970 45.070 1.00 227.10 ? 230 THR B N 1 +ATOM 4179 C CA . THR B 1 231 ? 10.231 113.027 45.241 1.00 242.41 ? 230 THR B CA 1 +ATOM 4180 C C . THR B 1 231 ? 10.161 114.001 44.051 1.00 249.13 ? 230 THR B C 1 +ATOM 4181 O O . THR B 1 231 ? 9.471 115.022 44.082 1.00 221.39 ? 230 THR B O 1 +ATOM 4182 C CB . THR B 1 231 ? 10.462 113.833 46.542 1.00 220.08 ? 230 THR B CB 1 +ATOM 4183 O OG1 . THR B 1 231 ? 9.485 114.877 46.642 1.00 209.80 ? 230 THR B OG1 1 +ATOM 4184 C CG2 . THR B 1 231 ? 11.859 114.447 46.553 1.00 205.17 ? 230 THR B CG2 1 +ATOM 4185 N N . ALA B 1 235 ? 17.443 116.320 51.798 1.00 145.64 ? 1054 ALA B N 1 +ATOM 4186 C CA . ALA B 1 235 ? 17.645 117.046 53.050 1.00 161.11 ? 1054 ALA B CA 1 +ATOM 4187 C C . ALA B 1 235 ? 18.705 116.399 53.951 1.00 176.23 ? 1054 ALA B C 1 +ATOM 4188 O O . ALA B 1 235 ? 19.579 115.658 53.486 1.00 136.96 ? 1054 ALA B O 1 +ATOM 4189 C CB . ALA B 1 235 ? 16.315 117.194 53.802 1.00 108.30 ? 1054 ALA B CB 1 +ATOM 4190 N N . SER B 1 236 ? 18.627 116.705 55.243 1.00 194.06 ? 1055 SER B N 1 +ATOM 4191 C CA . SER B 1 236 ? 19.469 116.056 56.241 1.00 206.54 ? 1055 SER B CA 1 +ATOM 4192 C C . SER B 1 236 ? 18.741 114.816 56.745 1.00 225.80 ? 1055 SER B C 1 +ATOM 4193 O O . SER B 1 236 ? 19.316 113.964 57.429 1.00 195.51 ? 1055 SER B O 1 +ATOM 4194 C CB . SER B 1 236 ? 19.760 117.009 57.398 1.00 175.67 ? 1055 SER B CB 1 +ATOM 4195 O OG . SER B 1 236 ? 20.714 116.449 58.282 1.00 152.96 ? 1055 SER B OG 1 +ATOM 4196 N N . THR B 1 237 ? 17.462 114.732 56.388 1.00 241.34 ? 1056 THR B N 1 +ATOM 4197 C CA . THR B 1 237 ? 16.639 113.562 56.663 1.00 212.13 ? 1056 THR B CA 1 +ATOM 4198 C C . THR B 1 237 ? 17.249 112.331 55.988 1.00 181.31 ? 1056 THR B C 1 +ATOM 4199 O O . THR B 1 237 ? 17.033 111.199 56.425 1.00 134.27 ? 1056 THR B O 1 +ATOM 4200 C CB . THR B 1 237 ? 15.181 113.783 56.187 1.00 175.04 ? 1056 THR B CB 1 +ATOM 4201 O OG1 . THR B 1 237 ? 15.124 113.760 54.754 1.00 153.21 ? 1056 THR B OG1 1 +ATOM 4202 C CG2 . THR B 1 237 ? 14.646 115.129 56.696 1.00 149.54 ? 1056 THR B CG2 1 +ATOM 4203 N N . LYS B 1 238 ? 18.015 112.572 54.924 1.00 208.51 ? 1057 LYS B N 1 +ATOM 4204 C CA . LYS B 1 238 ? 18.799 111.539 54.256 1.00 192.08 ? 1057 LYS B CA 1 +ATOM 4205 C C . LYS B 1 238 ? 19.702 110.845 55.263 1.00 163.16 ? 1057 LYS B C 1 +ATOM 4206 O O . LYS B 1 238 ? 19.589 109.643 55.477 1.00 136.42 ? 1057 LYS B O 1 +ATOM 4207 C CB . LYS B 1 238 ? 19.652 112.143 53.129 1.00 176.70 ? 1057 LYS B CB 1 +ATOM 4208 C CG . LYS B 1 238 ? 18.978 112.203 51.753 1.00 173.79 ? 1057 LYS B CG 1 +ATOM 4209 C CD . LYS B 1 238 ? 17.725 113.069 51.754 1.00 148.43 ? 1057 LYS B CD 1 +ATOM 4210 C CE . LYS B 1 238 ? 17.188 113.277 50.348 1.00 120.59 ? 1057 LYS B CE 1 +ATOM 4211 N NZ . LYS B 1 238 ? 15.910 114.043 50.349 1.00 126.84 ? 1057 LYS B NZ 1 +ATOM 4212 N N . LYS B 1 239 ? 20.569 111.629 55.899 1.00 178.08 ? 1058 LYS B N 1 +ATOM 4213 C CA . LYS B 1 239 ? 21.586 111.128 56.820 1.00 195.37 ? 1058 LYS B CA 1 +ATOM 4214 C C . LYS B 1 239 ? 21.031 110.275 57.967 1.00 185.64 ? 1058 LYS B C 1 +ATOM 4215 O O . LYS B 1 239 ? 21.729 109.413 58.506 1.00 169.18 ? 1058 LYS B O 1 +ATOM 4216 C CB . LYS B 1 239 ? 22.385 112.304 57.389 1.00 204.02 ? 1058 LYS B CB 1 +ATOM 4217 C CG . LYS B 1 239 ? 22.979 113.235 56.334 1.00 179.74 ? 1058 LYS B CG 1 +ATOM 4218 C CD . LYS B 1 239 ? 23.891 114.271 56.983 1.00 178.86 ? 1058 LYS B CD 1 +ATOM 4219 C CE . LYS B 1 239 ? 24.913 113.600 57.905 1.00 175.93 ? 1058 LYS B CE 1 +ATOM 4220 N NZ . LYS B 1 239 ? 25.637 114.550 58.804 1.00 140.69 ? 1058 LYS B NZ 1 +ATOM 4221 N N . LEU B 1 240 ? 19.773 110.521 58.325 1.00 180.67 ? 1059 LEU B N 1 +ATOM 4222 C CA . LEU B 1 240 ? 19.120 109.840 59.442 1.00 185.57 ? 1059 LEU B CA 1 +ATOM 4223 C C . LEU B 1 240 ? 18.732 108.398 59.125 1.00 179.60 ? 1059 LEU B C 1 +ATOM 4224 O O . LEU B 1 240 ? 19.026 107.477 59.895 1.00 132.31 ? 1059 LEU B O 1 +ATOM 4225 C CB . LEU B 1 240 ? 17.868 110.615 59.854 1.00 190.43 ? 1059 LEU B CB 1 +ATOM 4226 C CG . LEU B 1 240 ? 16.938 109.923 60.849 1.00 174.80 ? 1059 LEU B CG 1 +ATOM 4227 C CD1 . LEU B 1 240 ? 17.660 109.663 62.160 1.00 169.47 ? 1059 LEU B CD1 1 +ATOM 4228 C CD2 . LEU B 1 240 ? 15.705 110.776 61.070 1.00 153.01 ? 1059 LEU B CD2 1 +ATOM 4229 N N . SER B 1 241 ? 18.058 108.221 57.992 1.00 199.17 ? 1060 SER B N 1 +ATOM 4230 C CA . SER B 1 241 ? 17.558 106.918 57.572 1.00 174.67 ? 1060 SER B CA 1 +ATOM 4231 C C . SER B 1 241 ? 18.695 106.014 57.123 1.00 147.78 ? 1060 SER B C 1 +ATOM 4232 O O . SER B 1 241 ? 18.525 104.802 57.016 1.00 138.77 ? 1060 SER B O 1 +ATOM 4233 C CB . SER B 1 241 ? 16.532 107.072 56.447 1.00 134.14 ? 1060 SER B CB 1 +ATOM 4234 O OG . SER B 1 241 ? 17.160 107.409 55.226 1.00 139.53 ? 1060 SER B OG 1 +ATOM 4235 N N . GLU B 1 242 ? 19.855 106.609 56.862 1.00 138.31 ? 1061 GLU B N 1 +ATOM 4236 C CA . GLU B 1 242 ? 21.028 105.823 56.519 1.00 172.06 ? 1061 GLU B CA 1 +ATOM 4237 C C . GLU B 1 242 ? 21.409 105.003 57.737 1.00 155.55 ? 1061 GLU B C 1 +ATOM 4238 O O . GLU B 1 242 ? 21.864 103.865 57.623 1.00 127.18 ? 1061 GLU B O 1 +ATOM 4239 C CB . GLU B 1 242 ? 22.198 106.716 56.098 1.00 179.04 ? 1061 GLU B CB 1 +ATOM 4240 C CG . GLU B 1 242 ? 21.876 107.759 55.025 1.00 184.58 ? 1061 GLU B CG 1 +ATOM 4241 C CD . GLU B 1 242 ? 21.229 107.190 53.761 1.00 189.97 ? 1061 GLU B CD 1 +ATOM 4242 O OE1 . GLU B 1 242 ? 21.425 105.994 53.453 1.00 198.37 ? 1061 GLU B OE1 1 +ATOM 4243 O OE2 . GLU B 1 242 ? 20.524 107.954 53.066 1.00 170.40 ? 1061 GLU B OE2 1 +ATOM 4244 N N . SER B 1 243 ? 21.197 105.592 58.908 1.00 167.86 ? 1062 SER B N 1 +ATOM 4245 C CA . SER B 1 243 ? 21.503 104.932 60.168 1.00 197.30 ? 1062 SER B CA 1 +ATOM 4246 C C . SER B 1 243 ? 20.431 103.912 60.550 1.00 176.80 ? 1062 SER B C 1 +ATOM 4247 O O . SER B 1 243 ? 20.747 102.765 60.887 1.00 120.70 ? 1062 SER B O 1 +ATOM 4248 C CB . SER B 1 243 ? 21.683 105.970 61.276 1.00 206.57 ? 1062 SER B CB 1 +ATOM 4249 O OG . SER B 1 243 ? 22.780 106.821 60.989 1.00 198.38 ? 1062 SER B OG 1 +ATOM 4250 N N . LEU B 1 244 ? 19.170 104.338 60.497 1.00 167.47 ? 1063 LEU B N 1 +ATOM 4251 C CA . LEU B 1 244 ? 18.045 103.443 60.748 1.00 148.60 ? 1063 LEU B CA 1 +ATOM 4252 C C . LEU B 1 244 ? 18.161 102.219 59.864 1.00 160.79 ? 1063 LEU B C 1 +ATOM 4253 O O . LEU B 1 244 ? 17.869 101.101 60.296 1.00 138.00 ? 1063 LEU B O 1 +ATOM 4254 C CB . LEU B 1 244 ? 16.719 104.146 60.486 1.00 118.72 ? 1063 LEU B CB 1 +ATOM 4255 C CG . LEU B 1 244 ? 16.159 104.913 61.677 1.00 150.70 ? 1063 LEU B CG 1 +ATOM 4256 C CD1 . LEU B 1 244 ? 14.794 105.478 61.324 1.00 147.37 ? 1063 LEU B CD1 1 +ATOM 4257 C CD2 . LEU B 1 244 ? 16.097 104.006 62.906 1.00 127.10 ? 1063 LEU B CD2 1 +ATOM 4258 N N . LYS B 1 245 ? 18.593 102.449 58.627 1.00 169.16 ? 1064 LYS B N 1 +ATOM 4259 C CA . LYS B 1 245 ? 18.954 101.373 57.717 1.00 161.49 ? 1064 LYS B CA 1 +ATOM 4260 C C . LYS B 1 245 ? 19.894 100.381 58.395 1.00 165.69 ? 1064 LYS B C 1 +ATOM 4261 O O . LYS B 1 245 ? 19.503 99.247 58.661 1.00 174.76 ? 1064 LYS B O 1 +ATOM 4262 C CB . LYS B 1 245 ? 19.604 101.925 56.445 1.00 140.84 ? 1064 LYS B CB 1 +ATOM 4263 C CG . LYS B 1 245 ? 18.627 102.259 55.321 1.00 165.28 ? 1064 LYS B CG 1 +ATOM 4264 C CD . LYS B 1 245 ? 19.364 102.845 54.117 1.00 193.93 ? 1064 LYS B CD 1 +ATOM 4265 C CE . LYS B 1 245 ? 18.441 103.042 52.918 1.00 184.15 ? 1064 LYS B CE 1 +ATOM 4266 N NZ . LYS B 1 245 ? 19.167 103.469 51.687 1.00 130.28 ? 1064 LYS B NZ 1 +ATOM 4267 N N . ARG B 1 246 ? 21.118 100.811 58.694 1.00 158.12 ? 1065 ARG B N 1 +ATOM 4268 C CA . ARG B 1 246 ? 22.124 99.887 59.221 1.00 173.06 ? 1065 ARG B CA 1 +ATOM 4269 C C . ARG B 1 246 ? 21.718 99.220 60.545 1.00 166.61 ? 1065 ARG B C 1 +ATOM 4270 O O . ARG B 1 246 ? 22.014 98.045 60.759 1.00 150.39 ? 1065 ARG B O 1 +ATOM 4271 C CB . ARG B 1 246 ? 23.514 100.542 59.324 1.00 167.88 ? 1065 ARG B CB 1 +ATOM 4272 C CG . ARG B 1 246 ? 24.180 100.893 57.994 1.00 180.73 ? 1065 ARG B CG 1 +ATOM 4273 C CD . ARG B 1 246 ? 25.575 101.488 58.219 1.00 203.43 ? 1065 ARG B CD 1 +ATOM 4274 N NE . ARG B 1 246 ? 26.218 101.905 56.972 1.00 226.38 ? 1065 ARG B NE 1 +ATOM 4275 C CZ . ARG B 1 246 ? 27.381 102.553 56.900 1.00 204.25 ? 1065 ARG B CZ 1 +ATOM 4276 N NH1 . ARG B 1 246 ? 28.042 102.864 58.008 1.00 184.53 ? 1065 ARG B NH1 1 +ATOM 4277 N NH2 . ARG B 1 246 ? 27.885 102.890 55.718 1.00 157.95 ? 1065 ARG B NH2 1 +ATOM 4278 N N . ILE B 1 247 ? 21.021 99.953 61.410 1.00 152.06 ? 1066 ILE B N 1 +ATOM 4279 C CA . ILE B 1 247 ? 20.603 99.415 62.708 1.00 150.72 ? 1066 ILE B CA 1 +ATOM 4280 C C . ILE B 1 247 ? 19.626 98.237 62.561 1.00 154.24 ? 1066 ILE B C 1 +ATOM 4281 O O . ILE B 1 247 ? 19.729 97.239 63.280 1.00 109.39 ? 1066 ILE B O 1 +ATOM 4282 C CB . ILE B 1 247 ? 20.033 100.539 63.637 1.00 150.88 ? 1066 ILE B CB 1 +ATOM 4283 C CG1 . ILE B 1 247 ? 21.141 101.537 64.027 1.00 191.68 ? 1066 ILE B CG1 1 +ATOM 4284 C CG2 . ILE B 1 247 ? 19.352 99.953 64.867 1.00 108.09 ? 1066 ILE B CG2 1 +ATOM 4285 C CD1 . ILE B 1 247 ? 20.668 102.811 64.707 1.00 206.41 ? 1066 ILE B CD1 1 +ATOM 4286 N N . GLY B 1 248 ? 18.698 98.350 61.614 1.00 166.12 ? 1067 GLY B N 1 +ATOM 4287 C CA . GLY B 1 248 ? 17.790 97.260 61.307 1.00 145.46 ? 1067 GLY B CA 1 +ATOM 4288 C C . GLY B 1 248 ? 18.518 96.220 60.480 1.00 156.10 ? 1067 GLY B C 1 +ATOM 4289 O O . GLY B 1 248 ? 18.127 95.050 60.422 1.00 138.27 ? 1067 GLY B O 1 +ATOM 4290 N N . ASP B 1 249 ? 19.597 96.658 59.840 1.00 168.33 ? 1068 ASP B N 1 +ATOM 4291 C CA . ASP B 1 249 ? 20.365 95.790 58.959 1.00 159.23 ? 1068 ASP B CA 1 +ATOM 4292 C C . ASP B 1 249 ? 21.252 94.837 59.746 1.00 156.72 ? 1068 ASP B C 1 +ATOM 4293 O O . ASP B 1 249 ? 21.093 93.619 59.635 1.00 127.42 ? 1068 ASP B O 1 +ATOM 4294 C CB . ASP B 1 249 ? 21.187 96.610 57.961 1.00 165.32 ? 1068 ASP B CB 1 +ATOM 4295 C CG . ASP B 1 249 ? 20.372 97.045 56.751 1.00 185.41 ? 1068 ASP B CG 1 +ATOM 4296 O OD1 . ASP B 1 249 ? 19.126 96.946 56.798 1.00 190.02 ? 1068 ASP B OD1 1 +ATOM 4297 O OD2 . ASP B 1 249 ? 20.977 97.490 55.753 1.00 180.00 ? 1068 ASP B OD2 1 +ATOM 4298 N N . GLU B 1 250 ? 22.171 95.395 60.540 1.00 185.24 ? 1069 GLU B N 1 +ATOM 4299 C CA . GLU B 1 250 ? 23.035 94.614 61.431 1.00 191.31 ? 1069 GLU B CA 1 +ATOM 4300 C C . GLU B 1 250 ? 22.184 93.670 62.274 1.00 166.43 ? 1069 GLU B C 1 +ATOM 4301 O O . GLU B 1 250 ? 22.575 92.542 62.574 1.00 108.71 ? 1069 GLU B O 1 +ATOM 4302 C CB . GLU B 1 250 ? 23.837 95.540 62.358 1.00 179.20 ? 1069 GLU B CB 1 +ATOM 4303 C CG . GLU B 1 250 ? 24.754 96.538 61.653 1.00 198.64 ? 1069 GLU B CG 1 +ATOM 4304 C CD . GLU B 1 250 ? 25.187 97.685 62.561 1.00 198.00 ? 1069 GLU B CD 1 +ATOM 4305 O OE1 . GLU B 1 250 ? 24.871 97.644 63.770 1.00 171.57 ? 1069 GLU B OE1 1 +ATOM 4306 O OE2 . GLU B 1 250 ? 25.838 98.631 62.063 1.00 188.01 ? 1069 GLU B OE2 1 +ATOM 4307 N N . LEU B 1 251 ? 21.006 94.160 62.641 1.00 157.40 ? 1070 LEU B N 1 +ATOM 4308 C CA . LEU B 1 251 ? 20.025 93.400 63.395 1.00 143.90 ? 1070 LEU B CA 1 +ATOM 4309 C C . LEU B 1 251 ? 19.569 92.147 62.640 1.00 155.12 ? 1070 LEU B C 1 +ATOM 4310 O O . LEU B 1 251 ? 19.685 91.026 63.142 1.00 97.71 ? 1070 LEU B O 1 +ATOM 4311 C CB . LEU B 1 251 ? 18.838 94.312 63.710 1.00 139.24 ? 1070 LEU B CB 1 +ATOM 4312 C CG . LEU B 1 251 ? 17.704 93.852 64.624 1.00 145.09 ? 1070 LEU B CG 1 +ATOM 4313 C CD1 . LEU B 1 251 ? 18.211 92.981 65.774 1.00 141.36 ? 1070 LEU B CD1 1 +ATOM 4314 C CD2 . LEU B 1 251 ? 16.921 95.069 65.143 1.00 107.64 ? 1070 LEU B CD2 1 +ATOM 4315 N N . ASP B 1 252 ? 19.059 92.332 61.428 1.00 180.21 ? 1071 ASP B N 1 +ATOM 4316 C CA . ASP B 1 252 ? 18.536 91.198 60.679 1.00 158.62 ? 1071 ASP B CA 1 +ATOM 4317 C C . ASP B 1 252 ? 19.658 90.293 60.165 1.00 156.26 ? 1071 ASP B C 1 +ATOM 4318 O O . ASP B 1 252 ? 19.443 89.107 59.894 1.00 141.36 ? 1071 ASP B O 1 +ATOM 4319 C CB . ASP B 1 252 ? 17.613 91.656 59.548 1.00 117.17 ? 1071 ASP B CB 1 +ATOM 4320 C CG . ASP B 1 252 ? 17.031 90.489 58.764 1.00 202.20 ? 1071 ASP B CG 1 +ATOM 4321 O OD1 . ASP B 1 252 ? 16.259 89.692 59.342 1.00 193.76 ? 1071 ASP B OD1 1 +ATOM 4322 O OD2 . ASP B 1 252 ? 17.345 90.370 57.562 1.00 246.16 ? 1071 ASP B OD2 1 +ATOM 4323 N N . SER B 1 253 ? 20.862 90.850 60.071 1.00 158.99 ? 1072 SER B N 1 +ATOM 4324 C CA . SER B 1 253 ? 22.010 90.095 59.574 1.00 183.42 ? 1072 SER B CA 1 +ATOM 4325 C C . SER B 1 253 ? 22.891 89.515 60.682 1.00 196.36 ? 1072 SER B C 1 +ATOM 4326 O O . SER B 1 253 ? 23.801 88.737 60.396 1.00 180.94 ? 1072 SER B O 1 +ATOM 4327 C CB . SER B 1 253 ? 22.857 90.937 58.605 1.00 184.17 ? 1072 SER B CB 1 +ATOM 4328 O OG . SER B 1 253 ? 23.652 91.899 59.282 1.00 180.38 ? 1072 SER B OG 1 +ATOM 4329 N N . ASN B 1 254 ? 22.628 89.892 61.934 1.00 218.33 ? 1073 ASN B N 1 +ATOM 4330 C CA . ASN B 1 254 ? 23.380 89.367 63.079 1.00 216.68 ? 1073 ASN B CA 1 +ATOM 4331 C C . ASN B 1 254 ? 23.189 87.862 63.229 1.00 208.41 ? 1073 ASN B C 1 +ATOM 4332 O O . ASN B 1 254 ? 22.185 87.405 63.781 1.00 171.62 ? 1073 ASN B O 1 +ATOM 4333 C CB . ASN B 1 254 ? 22.974 90.069 64.378 1.00 209.24 ? 1073 ASN B CB 1 +ATOM 4334 C CG . ASN B 1 254 ? 24.163 90.601 65.152 1.00 188.76 ? 1073 ASN B CG 1 +ATOM 4335 O OD1 . ASN B 1 254 ? 25.180 90.977 64.568 1.00 184.85 ? 1073 ASN B OD1 1 +ATOM 4336 N ND2 . ASN B 1 254 ? 24.041 90.639 66.476 1.00 169.97 ? 1073 ASN B ND2 1 +ATOM 4337 N N . MET B 1 255 ? 24.159 87.098 62.739 1.00 229.44 ? 1074 MET B N 1 +ATOM 4338 C CA . MET B 1 255 ? 24.028 85.647 62.666 1.00 233.91 ? 1074 MET B CA 1 +ATOM 4339 C C . MET B 1 255 ? 23.942 84.972 64.032 1.00 223.87 ? 1074 MET B C 1 +ATOM 4340 O O . MET B 1 255 ? 23.384 83.880 64.149 1.00 196.66 ? 1074 MET B O 1 +ATOM 4341 C CB . MET B 1 255 ? 25.159 85.036 61.832 1.00 236.76 ? 1074 MET B CB 1 +ATOM 4342 C CG . MET B 1 255 ? 25.019 85.269 60.332 1.00 231.33 ? 1074 MET B CG 1 +ATOM 4343 S SD . MET B 1 255 ? 23.431 84.713 59.671 1.00 247.79 ? 1074 MET B SD 1 +ATOM 4344 C CE . MET B 1 255 ? 23.483 82.958 60.034 1.00 136.91 ? 1074 MET B CE 1 +ATOM 4345 N N . GLU B 1 256 ? 24.499 85.621 65.054 1.00 231.36 ? 1075 GLU B N 1 +ATOM 4346 C CA . GLU B 1 256 ? 24.400 85.130 66.425 1.00 218.76 ? 1075 GLU B CA 1 +ATOM 4347 C C . GLU B 1 256 ? 22.936 84.982 66.774 1.00 194.10 ? 1075 GLU B C 1 +ATOM 4348 O O . GLU B 1 256 ? 22.453 83.894 67.095 1.00 161.84 ? 1075 GLU B O 1 +ATOM 4349 C CB . GLU B 1 256 ? 24.993 86.141 67.404 1.00 219.25 ? 1075 GLU B CB 1 +ATOM 4350 C CG . GLU B 1 256 ? 26.368 86.654 67.067 1.00 215.31 ? 1075 GLU B CG 1 +ATOM 4351 C CD . GLU B 1 256 ? 26.791 87.771 68.001 1.00 212.31 ? 1075 GLU B CD 1 +ATOM 4352 O OE1 . GLU B 1 256 ? 25.908 88.534 68.452 1.00 213.35 ? 1075 GLU B OE1 1 +ATOM 4353 O OE2 . GLU B 1 256 ? 28.000 87.880 68.292 1.00 200.27 ? 1075 GLU B OE2 1 +ATOM 4354 N N . LEU B 1 257 ? 22.247 86.115 66.691 1.00 182.89 ? 1076 LEU B N 1 +ATOM 4355 C CA . LEU B 1 257 ? 20.851 86.251 67.068 1.00 175.38 ? 1076 LEU B CA 1 +ATOM 4356 C C . LEU B 1 257 ? 19.910 85.374 66.238 1.00 169.35 ? 1076 LEU B C 1 +ATOM 4357 O O . LEU B 1 257 ? 19.052 84.680 66.791 1.00 117.44 ? 1076 LEU B O 1 +ATOM 4358 C CB . LEU B 1 257 ? 20.457 87.728 66.971 1.00 157.77 ? 1076 LEU B CB 1 +ATOM 4359 C CG . LEU B 1 257 ? 19.006 88.151 67.181 1.00 158.61 ? 1076 LEU B CG 1 +ATOM 4360 C CD1 . LEU B 1 257 ? 18.448 87.587 68.478 1.00 138.64 ? 1076 LEU B CD1 1 +ATOM 4361 C CD2 . LEU B 1 257 ? 18.917 89.666 67.153 1.00 170.78 ? 1076 LEU B CD2 1 +ATOM 4362 N N . GLN B 1 258 ? 20.077 85.404 64.917 1.00 176.36 ? 1077 GLN B N 1 +ATOM 4363 C CA . GLN B 1 258 ? 19.206 84.644 64.023 1.00 169.34 ? 1077 GLN B CA 1 +ATOM 4364 C C . GLN B 1 258 ? 19.273 83.148 64.346 1.00 177.67 ? 1077 GLN B C 1 +ATOM 4365 O O . GLN B 1 258 ? 18.243 82.471 64.421 1.00 172.42 ? 1077 GLN B O 1 +ATOM 4366 C CB . GLN B 1 258 ? 19.549 84.921 62.552 1.00 144.18 ? 1077 GLN B CB 1 +ATOM 4367 C CG . GLN B 1 258 ? 19.472 86.403 62.134 1.00 169.87 ? 1077 GLN B CG 1 +ATOM 4368 C CD . GLN B 1 258 ? 18.061 86.993 62.179 1.00 167.79 ? 1077 GLN B CD 1 +ATOM 4369 O OE1 . GLN B 1 258 ? 17.072 86.304 61.922 1.00 162.54 ? 1077 GLN B OE1 1 +ATOM 4370 N NE2 . GLN B 1 258 ? 17.970 88.283 62.503 1.00 121.47 ? 1077 GLN B NE2 1 +ATOM 4371 N N . ARG B 1 259 ? 20.488 82.653 64.565 1.00 169.64 ? 1078 ARG B N 1 +ATOM 4372 C CA . ARG B 1 259 ? 20.705 81.274 64.989 1.00 173.93 ? 1078 ARG B CA 1 +ATOM 4373 C C . ARG B 1 259 ? 20.001 81.010 66.314 1.00 181.67 ? 1078 ARG B C 1 +ATOM 4374 O O . ARG B 1 259 ? 19.288 80.018 66.459 1.00 174.35 ? 1078 ARG B O 1 +ATOM 4375 C CB . ARG B 1 259 ? 22.204 80.994 65.150 1.00 194.97 ? 1078 ARG B CB 1 +ATOM 4376 C CG . ARG B 1 259 ? 22.556 79.535 65.450 1.00 196.64 ? 1078 ARG B CG 1 +ATOM 4377 C CD . ARG B 1 259 ? 23.741 79.417 66.414 1.00 213.85 ? 1078 ARG B CD 1 +ATOM 4378 N NE . ARG B 1 259 ? 24.950 80.077 65.920 1.00 222.43 ? 1078 ARG B NE 1 +ATOM 4379 C CZ . ARG B 1 259 ? 25.780 80.788 66.678 1.00 199.66 ? 1078 ARG B CZ 1 +ATOM 4380 N NH1 . ARG B 1 259 ? 25.536 80.941 67.975 1.00 175.02 ? 1078 ARG B NH1 1 +ATOM 4381 N NH2 . ARG B 1 259 ? 26.855 81.353 66.140 1.00 160.11 ? 1078 ARG B NH2 1 +ATOM 4382 N N . MET B 1 260 ? 20.211 81.916 67.270 1.00 183.73 ? 1079 MET B N 1 +ATOM 4383 C CA . MET B 1 260 ? 19.676 81.805 68.630 1.00 186.05 ? 1079 MET B CA 1 +ATOM 4384 C C . MET B 1 260 ? 18.158 81.654 68.679 1.00 194.79 ? 1079 MET B C 1 +ATOM 4385 O O . MET B 1 260 ? 17.632 80.869 69.472 1.00 194.03 ? 1079 MET B O 1 +ATOM 4386 C CB . MET B 1 260 ? 20.076 83.035 69.461 1.00 175.62 ? 1079 MET B CB 1 +ATOM 4387 C CG . MET B 1 260 ? 21.016 82.761 70.635 1.00 149.58 ? 1079 MET B CG 1 +ATOM 4388 S SD . MET B 1 260 ? 21.316 84.216 71.679 1.00 245.26 ? 1079 MET B SD 1 +ATOM 4389 C CE . MET B 1 260 ? 22.346 85.251 70.630 1.00 90.20 ? 1079 MET B CE 1 +ATOM 4390 N N . ILE B 1 261 ? 17.454 82.417 67.850 1.00 182.47 ? 1080 ILE B N 1 +ATOM 4391 C CA . ILE B 1 261 ? 15.998 82.407 67.906 1.00 185.91 ? 1080 ILE B CA 1 +ATOM 4392 C C . ILE B 1 261 ? 15.423 81.214 67.169 1.00 188.15 ? 1080 ILE B C 1 +ATOM 4393 O O . ILE B 1 261 ? 14.453 80.609 67.627 1.00 203.10 ? 1080 ILE B O 1 +ATOM 4394 C CB . ILE B 1 261 ? 15.375 83.685 67.341 1.00 166.88 ? 1080 ILE B CB 1 +ATOM 4395 C CG1 . ILE B 1 261 ? 16.175 84.909 67.780 1.00 141.24 ? 1080 ILE B CG1 1 +ATOM 4396 C CG2 . ILE B 1 261 ? 13.931 83.808 67.770 1.00 172.69 ? 1080 ILE B CG2 1 +ATOM 4397 C CD1 . ILE B 1 261 ? 15.475 86.208 67.495 1.00 144.19 ? 1080 ILE B CD1 1 +ATOM 4398 N N . ALA B 1 262 ? 16.014 80.890 66.022 1.00 151.30 ? 1081 ALA B N 1 +ATOM 4399 C CA . ALA B 1 262 ? 15.658 79.678 65.301 1.00 164.70 ? 1081 ALA B CA 1 +ATOM 4400 C C . ALA B 1 262 ? 15.782 78.497 66.260 1.00 190.99 ? 1081 ALA B C 1 +ATOM 4401 O O . ALA B 1 262 ? 14.888 77.656 66.349 1.00 187.99 ? 1081 ALA B O 1 +ATOM 4402 C CB . ALA B 1 262 ? 16.555 79.492 64.084 1.00 130.91 ? 1081 ALA B CB 1 +ATOM 4403 N N . ALA B 1 263 ? 16.884 78.461 67.004 1.00 189.59 ? 1082 ALA B N 1 +ATOM 4404 C CA . ALA B 1 263 ? 17.059 77.473 68.058 1.00 195.45 ? 1082 ALA B CA 1 +ATOM 4405 C C . ALA B 1 263 ? 16.198 77.812 69.281 1.00 224.93 ? 1082 ALA B C 1 +ATOM 4406 O O . ALA B 1 263 ? 16.690 78.362 70.270 1.00 213.93 ? 1082 ALA B O 1 +ATOM 4407 C CB . ALA B 1 263 ? 18.534 77.352 68.444 1.00 181.43 ? 1082 ALA B CB 1 +ATOM 4408 N N . VAL B 1 264 ? 14.908 77.494 69.194 1.00 238.69 ? 1083 VAL B N 1 +ATOM 4409 C CA . VAL B 1 264 ? 14.005 77.580 70.343 1.00 242.78 ? 1083 VAL B CA 1 +ATOM 4410 C C . VAL B 1 264 ? 12.790 76.653 70.163 1.00 215.96 ? 1083 VAL B C 1 +ATOM 4411 O O . VAL B 1 264 ? 12.329 76.423 69.039 1.00 157.78 ? 1083 VAL B O 1 +ATOM 4412 C CB . VAL B 1 264 ? 13.572 79.043 70.648 1.00 206.55 ? 1083 VAL B CB 1 +ATOM 4413 C CG1 . VAL B 1 264 ? 12.462 79.492 69.708 1.00 180.18 ? 1083 VAL B CG1 1 +ATOM 4414 C CG2 . VAL B 1 264 ? 13.143 79.184 72.109 1.00 190.00 ? 1083 VAL B CG2 1 +ATOM 4415 N N . ASP B 1 265 ? 12.297 76.107 71.273 1.00 224.28 ? 1084 ASP B N 1 +ATOM 4416 C CA . ASP B 1 265 ? 11.179 75.164 71.245 1.00 234.37 ? 1084 ASP B CA 1 +ATOM 4417 C C . ASP B 1 265 ? 9.841 75.894 71.310 1.00 231.51 ? 1084 ASP B C 1 +ATOM 4418 O O . ASP B 1 265 ? 9.424 76.371 72.368 1.00 189.84 ? 1084 ASP B O 1 +ATOM 4419 C CB . ASP B 1 265 ? 11.294 74.154 72.388 1.00 232.29 ? 1084 ASP B CB 1 +ATOM 4420 C CG . ASP B 1 265 ? 10.607 72.838 72.074 1.00 214.67 ? 1084 ASP B CG 1 +ATOM 4421 O OD1 . ASP B 1 265 ? 9.549 72.860 71.410 1.00 213.87 ? 1084 ASP B OD1 1 +ATOM 4422 O OD2 . ASP B 1 265 ? 11.130 71.780 72.485 1.00 185.04 ? 1084 ASP B OD2 1 +ATOM 4423 N N . THR B 1 266 ? 9.166 75.957 70.167 1.00 249.71 ? 1085 THR B N 1 +ATOM 4424 C CA . THR B 1 266 ? 7.998 76.812 70.006 1.00 265.66 ? 1085 THR B CA 1 +ATOM 4425 C C . THR B 1 266 ? 6.738 76.045 69.588 1.00 268.21 ? 1085 THR B C 1 +ATOM 4426 O O . THR B 1 266 ? 5.883 76.552 68.864 1.00 271.17 ? 1085 THR B O 1 +ATOM 4427 C CB . THR B 1 266 ? 8.289 77.931 68.982 1.00 268.02 ? 1085 THR B CB 1 +ATOM 4428 O OG1 . THR B 1 266 ? 9.377 78.739 69.448 1.00 263.82 ? 1085 THR B OG1 1 +ATOM 4429 C CG2 . THR B 1 266 ? 7.084 78.830 68.782 1.00 264.39 ? 1085 THR B CG2 1 +ATOM 4430 N N . ASP B 1 267 ? 6.616 74.802 70.042 1.00 260.42 ? 1086 ASP B N 1 +ATOM 4431 C CA . ASP B 1 267 ? 5.389 74.036 69.843 1.00 247.01 ? 1086 ASP B CA 1 +ATOM 4432 C C . ASP B 1 267 ? 4.393 74.471 70.909 1.00 237.85 ? 1086 ASP B C 1 +ATOM 4433 O O . ASP B 1 267 ? 3.185 74.555 70.669 1.00 205.16 ? 1086 ASP B O 1 +ATOM 4434 C CB . ASP B 1 267 ? 5.662 72.537 69.958 1.00 238.55 ? 1086 ASP B CB 1 +ATOM 4435 C CG . ASP B 1 267 ? 6.870 72.103 69.156 1.00 243.64 ? 1086 ASP B CG 1 +ATOM 4436 O OD1 . ASP B 1 267 ? 7.303 72.871 68.272 1.00 246.72 ? 1086 ASP B OD1 1 +ATOM 4437 O OD2 . ASP B 1 267 ? 7.384 70.993 69.408 1.00 240.77 ? 1086 ASP B OD2 1 +ATOM 4438 N N . SER B 1 268 ? 4.929 74.741 72.095 1.00 245.06 ? 1087 SER B N 1 +ATOM 4439 C CA . SER B 1 268 ? 4.194 75.371 73.179 1.00 234.11 ? 1087 SER B CA 1 +ATOM 4440 C C . SER B 1 268 ? 4.798 76.764 73.360 1.00 252.98 ? 1087 SER B C 1 +ATOM 4441 O O . SER B 1 268 ? 5.591 76.986 74.276 1.00 236.08 ? 1087 SER B O 1 +ATOM 4442 C CB . SER B 1 268 ? 4.341 74.544 74.458 1.00 186.81 ? 1087 SER B CB 1 +ATOM 4443 O OG . SER B 1 268 ? 3.569 75.078 75.517 1.00 159.27 ? 1087 SER B OG 1 +ATOM 4444 N N . PRO B 1 269 ? 4.426 77.706 72.473 1.00 256.44 ? 1088 PRO B N 1 +ATOM 4445 C CA . PRO B 1 269 ? 5.089 79.010 72.333 1.00 224.04 ? 1088 PRO B CA 1 +ATOM 4446 C C . PRO B 1 269 ? 4.763 80.019 73.436 1.00 221.56 ? 1088 PRO B C 1 +ATOM 4447 O O . PRO B 1 269 ? 5.656 80.763 73.845 1.00 209.03 ? 1088 PRO B O 1 +ATOM 4448 C CB . PRO B 1 269 ? 4.559 79.520 70.991 1.00 183.51 ? 1088 PRO B CB 1 +ATOM 4449 C CG . PRO B 1 269 ? 3.211 78.911 70.869 1.00 202.32 ? 1088 PRO B CG 1 +ATOM 4450 C CD . PRO B 1 269 ? 3.283 77.571 71.549 1.00 239.07 ? 1088 PRO B CD 1 +ATOM 4451 N N . ARG B 1 270 ? 3.512 80.033 73.896 1.00 222.45 ? 1089 ARG B N 1 +ATOM 4452 C CA . ARG B 1 270 ? 3.013 81.011 74.869 1.00 201.53 ? 1089 ARG B CA 1 +ATOM 4453 C C . ARG B 1 270 ? 3.870 81.170 76.136 1.00 205.18 ? 1089 ARG B C 1 +ATOM 4454 O O . ARG B 1 270 ? 4.149 82.293 76.572 1.00 137.95 ? 1089 ARG B O 1 +ATOM 4455 C CB . ARG B 1 270 ? 1.559 80.681 75.233 1.00 168.25 ? 1089 ARG B CB 1 +ATOM 4456 C CG . ARG B 1 270 ? 1.159 81.108 76.630 1.00 188.28 ? 1089 ARG B CG 1 +ATOM 4457 C CD . ARG B 1 270 ? -0.315 80.871 76.899 1.00 187.23 ? 1089 ARG B CD 1 +ATOM 4458 N NE . ARG B 1 270 ? -0.643 81.070 78.311 1.00 196.89 ? 1089 ARG B NE 1 +ATOM 4459 C CZ . ARG B 1 270 ? -0.817 82.259 78.885 1.00 194.20 ? 1089 ARG B CZ 1 +ATOM 4460 N NH1 . ARG B 1 270 ? -0.689 83.371 78.173 1.00 199.43 ? 1089 ARG B NH1 1 +ATOM 4461 N NH2 . ARG B 1 270 ? -1.115 82.337 80.177 1.00 162.89 ? 1089 ARG B NH2 1 +ATOM 4462 N N . GLU B 1 271 ? 4.285 80.048 76.719 1.00 231.32 ? 1090 GLU B N 1 +ATOM 4463 C CA . GLU B 1 271 ? 5.147 80.068 77.896 1.00 225.81 ? 1090 GLU B CA 1 +ATOM 4464 C C . GLU B 1 271 ? 6.519 80.635 77.543 1.00 220.85 ? 1090 GLU B C 1 +ATOM 4465 O O . GLU B 1 271 ? 7.068 81.455 78.281 1.00 191.19 ? 1090 GLU B O 1 +ATOM 4466 C CB . GLU B 1 271 ? 5.330 78.658 78.460 1.00 229.31 ? 1090 GLU B CB 1 +ATOM 4467 C CG . GLU B 1 271 ? 4.072 77.807 78.501 1.00 237.76 ? 1090 GLU B CG 1 +ATOM 4468 C CD . GLU B 1 271 ? 4.376 76.345 78.794 1.00 239.89 ? 1090 GLU B CD 1 +ATOM 4469 O OE1 . GLU B 1 271 ? 5.497 76.051 79.265 1.00 228.41 ? 1090 GLU B OE1 1 +ATOM 4470 O OE2 . GLU B 1 271 ? 3.500 75.489 78.546 1.00 238.99 ? 1090 GLU B OE2 1 +ATOM 4471 N N . VAL B 1 272 ? 7.059 80.184 76.411 1.00 236.51 ? 1091 VAL B N 1 +ATOM 4472 C CA . VAL B 1 272 ? 8.411 80.539 75.972 1.00 231.23 ? 1091 VAL B CA 1 +ATOM 4473 C C . VAL B 1 272 ? 8.608 82.051 75.881 1.00 226.38 ? 1091 VAL B C 1 +ATOM 4474 O O . VAL B 1 272 ? 9.616 82.585 76.340 1.00 220.44 ? 1091 VAL B O 1 +ATOM 4475 C CB . VAL B 1 272 ? 8.760 79.886 74.606 1.00 179.19 ? 1091 VAL B CB 1 +ATOM 4476 C CG1 . VAL B 1 272 ? 10.233 80.090 74.270 1.00 171.68 ? 1091 VAL B CG1 1 +ATOM 4477 C CG2 . VAL B 1 272 ? 8.425 78.402 74.619 1.00 165.83 ? 1091 VAL B CG2 1 +ATOM 4478 N N . PHE B 1 273 ? 7.633 82.736 75.294 1.00 227.55 ? 1092 PHE B N 1 +ATOM 4479 C CA . PHE B 1 273 ? 7.681 84.187 75.180 1.00 222.34 ? 1092 PHE B CA 1 +ATOM 4480 C C . PHE B 1 273 ? 7.645 84.837 76.559 1.00 199.76 ? 1092 PHE B C 1 +ATOM 4481 O O . PHE B 1 273 ? 8.524 85.626 76.904 1.00 196.05 ? 1092 PHE B O 1 +ATOM 4482 C CB . PHE B 1 273 ? 6.519 84.689 74.318 1.00 238.15 ? 1092 PHE B CB 1 +ATOM 4483 C CG . PHE B 1 273 ? 6.369 86.185 74.303 1.00 241.12 ? 1092 PHE B CG 1 +ATOM 4484 C CD1 . PHE B 1 273 ? 7.255 86.977 73.590 1.00 230.56 ? 1092 PHE B CD1 1 +ATOM 4485 C CD2 . PHE B 1 273 ? 5.340 86.800 75.000 1.00 234.97 ? 1092 PHE B CD2 1 +ATOM 4486 C CE1 . PHE B 1 273 ? 7.120 88.350 73.579 1.00 213.70 ? 1092 PHE B CE1 1 +ATOM 4487 C CE2 . PHE B 1 273 ? 5.198 88.175 74.987 1.00 222.18 ? 1092 PHE B CE2 1 +ATOM 4488 C CZ . PHE B 1 273 ? 6.088 88.949 74.273 1.00 208.45 ? 1092 PHE B CZ 1 +ATOM 4489 N N . PHE B 1 274 ? 6.632 84.484 77.344 1.00 173.19 ? 1093 PHE B N 1 +ATOM 4490 C CA . PHE B 1 274 ? 6.414 85.091 78.655 1.00 201.36 ? 1093 PHE B CA 1 +ATOM 4491 C C . PHE B 1 274 ? 7.619 84.989 79.596 1.00 215.78 ? 1093 PHE B C 1 +ATOM 4492 O O . PHE B 1 274 ? 7.953 85.953 80.286 1.00 209.82 ? 1093 PHE B O 1 +ATOM 4493 C CB . PHE B 1 274 ? 5.175 84.482 79.319 1.00 225.70 ? 1093 PHE B CB 1 +ATOM 4494 C CG . PHE B 1 274 ? 4.915 85.000 80.709 1.00 238.25 ? 1093 PHE B CG 1 +ATOM 4495 C CD1 . PHE B 1 274 ? 4.293 86.224 80.901 1.00 209.34 ? 1093 PHE B CD1 1 +ATOM 4496 C CD2 . PHE B 1 274 ? 5.298 84.263 81.823 1.00 229.49 ? 1093 PHE B CD2 1 +ATOM 4497 C CE1 . PHE B 1 274 ? 4.056 86.705 82.178 1.00 199.31 ? 1093 PHE B CE1 1 +ATOM 4498 C CE2 . PHE B 1 274 ? 5.066 84.738 83.103 1.00 183.68 ? 1093 PHE B CE2 1 +ATOM 4499 C CZ . PHE B 1 274 ? 4.444 85.960 83.281 1.00 181.04 ? 1093 PHE B CZ 1 +ATOM 4500 N N . ARG B 1 275 ? 8.265 83.825 79.628 1.00 217.44 ? 1094 ARG B N 1 +ATOM 4501 C CA . ARG B 1 275 ? 9.397 83.618 80.531 1.00 208.01 ? 1094 ARG B CA 1 +ATOM 4502 C C . ARG B 1 275 ? 10.596 84.431 80.064 1.00 194.81 ? 1094 ARG B C 1 +ATOM 4503 O O . ARG B 1 275 ? 11.295 85.035 80.877 1.00 193.45 ? 1094 ARG B O 1 +ATOM 4504 C CB . ARG B 1 275 ? 9.769 82.133 80.638 1.00 216.25 ? 1094 ARG B CB 1 +ATOM 4505 C CG . ARG B 1 275 ? 10.262 81.703 82.025 1.00 212.92 ? 1094 ARG B CG 1 +ATOM 4506 C CD . ARG B 1 275 ? 10.842 80.290 82.006 1.00 210.32 ? 1094 ARG B CD 1 +ATOM 4507 N NE . ARG B 1 275 ? 10.216 79.451 80.986 1.00 213.54 ? 1094 ARG B NE 1 +ATOM 4508 C CZ . ARG B 1 275 ? 9.171 78.655 81.195 1.00 190.29 ? 1094 ARG B CZ 1 +ATOM 4509 N NH1 . ARG B 1 275 ? 8.620 78.577 82.401 1.00 137.64 ? 1094 ARG B NH1 1 +ATOM 4510 N NH2 . ARG B 1 275 ? 8.677 77.935 80.192 1.00 166.67 ? 1094 ARG B NH2 1 +ATOM 4511 N N . VAL B 1 276 ? 10.825 84.441 78.752 1.00 174.86 ? 1095 VAL B N 1 +ATOM 4512 C CA . VAL B 1 276 ? 11.898 85.235 78.159 1.00 171.46 ? 1095 VAL B CA 1 +ATOM 4513 C C . VAL B 1 276 ? 11.611 86.716 78.360 1.00 172.52 ? 1095 VAL B C 1 +ATOM 4514 O O . VAL B 1 276 ? 12.528 87.518 78.560 1.00 160.43 ? 1095 VAL B O 1 +ATOM 4515 C CB . VAL B 1 276 ? 12.061 84.936 76.657 1.00 178.98 ? 1095 VAL B CB 1 +ATOM 4516 C CG1 . VAL B 1 276 ? 12.961 85.964 75.995 1.00 150.75 ? 1095 VAL B CG1 1 +ATOM 4517 C CG2 . VAL B 1 276 ? 12.626 83.546 76.462 1.00 212.71 ? 1095 VAL B CG2 1 +ATOM 4518 N N . ALA B 1 277 ? 10.328 87.064 78.311 1.00 181.43 ? 1096 ALA B N 1 +ATOM 4519 C CA . ALA B 1 277 ? 9.878 88.419 78.608 1.00 154.62 ? 1096 ALA B CA 1 +ATOM 4520 C C . ALA B 1 277 ? 10.211 88.768 80.046 1.00 152.74 ? 1096 ALA B C 1 +ATOM 4521 O O . ALA B 1 277 ? 10.830 89.799 80.316 1.00 143.86 ? 1096 ALA B O 1 +ATOM 4522 C CB . ALA B 1 277 ? 8.382 88.555 78.367 1.00 126.92 ? 1096 ALA B CB 1 +ATOM 4523 N N . ALA B 1 278 ? 9.808 87.893 80.963 1.00 160.25 ? 1097 ALA B N 1 +ATOM 4524 C CA . ALA B 1 278 ? 10.048 88.101 82.386 1.00 146.30 ? 1097 ALA B CA 1 +ATOM 4525 C C . ALA B 1 278 ? 11.519 87.944 82.779 1.00 141.00 ? 1097 ALA B C 1 +ATOM 4526 O O . ALA B 1 278 ? 11.949 88.477 83.798 1.00 136.74 ? 1097 ALA B O 1 +ATOM 4527 C CB . ALA B 1 278 ? 9.172 87.180 83.216 1.00 127.29 ? 1097 ALA B CB 1 +ATOM 4528 N N . ASP B 1 279 ? 12.292 87.217 81.980 1.00 135.34 ? 1098 ASP B N 1 +ATOM 4529 C CA . ASP B 1 279 ? 13.723 87.111 82.244 1.00 139.27 ? 1098 ASP B CA 1 +ATOM 4530 C C . ASP B 1 279 ? 14.445 88.392 81.819 1.00 169.62 ? 1098 ASP B C 1 +ATOM 4531 O O . ASP B 1 279 ? 15.397 88.830 82.471 1.00 140.82 ? 1098 ASP B O 1 +ATOM 4532 C CB . ASP B 1 279 ? 14.322 85.895 81.538 1.00 147.36 ? 1098 ASP B CB 1 +ATOM 4533 C CG . ASP B 1 279 ? 15.570 85.377 82.228 1.00 169.54 ? 1098 ASP B CG 1 +ATOM 4534 O OD1 . ASP B 1 279 ? 16.671 85.897 81.937 1.00 155.04 ? 1098 ASP B OD1 1 +ATOM 4535 O OD2 . ASP B 1 279 ? 15.449 84.451 83.062 1.00 179.67 ? 1098 ASP B OD2 1 +ATOM 4536 N N . MET B 1 280 ? 13.979 88.993 80.727 1.00 184.82 ? 1099 MET B N 1 +ATOM 4537 C CA . MET B 1 280 ? 14.515 90.268 80.265 1.00 171.50 ? 1099 MET B CA 1 +ATOM 4538 C C . MET B 1 280 ? 14.313 91.352 81.314 1.00 150.26 ? 1099 MET B C 1 +ATOM 4539 O O . MET B 1 280 ? 15.107 92.284 81.421 1.00 143.95 ? 1099 MET B O 1 +ATOM 4540 C CB . MET B 1 280 ? 13.845 90.700 78.957 1.00 183.66 ? 1099 MET B CB 1 +ATOM 4541 C CG . MET B 1 280 ? 14.423 90.072 77.697 1.00 201.65 ? 1099 MET B CG 1 +ATOM 4542 S SD . MET B 1 280 ? 13.767 90.831 76.196 1.00 187.35 ? 1099 MET B SD 1 +ATOM 4543 C CE . MET B 1 280 ? 14.124 92.555 76.525 1.00 134.03 ? 1099 MET B CE 1 +ATOM 4544 N N . PHE B 1 281 ? 13.247 91.218 82.095 1.00 142.02 ? 1100 PHE B N 1 +ATOM 4545 C CA . PHE B 1 281 ? 12.851 92.260 83.033 1.00 144.51 ? 1100 PHE B CA 1 +ATOM 4546 C C . PHE B 1 281 ? 12.966 91.840 84.491 1.00 162.52 ? 1100 PHE B C 1 +ATOM 4547 O O . PHE B 1 281 ? 12.194 92.282 85.342 1.00 147.51 ? 1100 PHE B O 1 +ATOM 4548 C CB . PHE B 1 281 ? 11.432 92.712 82.717 1.00 126.07 ? 1100 PHE B CB 1 +ATOM 4549 C CG . PHE B 1 281 ? 11.313 93.396 81.393 1.00 153.96 ? 1100 PHE B CG 1 +ATOM 4550 C CD1 . PHE B 1 281 ? 12.259 94.330 81.005 1.00 163.92 ? 1100 PHE B CD1 1 +ATOM 4551 C CD2 . PHE B 1 281 ? 10.271 93.098 80.527 1.00 124.91 ? 1100 PHE B CD2 1 +ATOM 4552 C CE1 . PHE B 1 281 ? 12.162 94.971 79.788 1.00 159.25 ? 1100 PHE B CE1 1 +ATOM 4553 C CE2 . PHE B 1 281 ? 10.166 93.735 79.304 1.00 120.68 ? 1100 PHE B CE2 1 +ATOM 4554 C CZ . PHE B 1 281 ? 11.115 94.672 78.932 1.00 143.69 ? 1100 PHE B CZ 1 +ATOM 4555 N N . SER B 1 282 ? 13.943 90.984 84.767 1.00 189.25 ? 1101 SER B N 1 +ATOM 4556 C CA . SER B 1 282 ? 14.224 90.553 86.126 1.00 205.43 ? 1101 SER B CA 1 +ATOM 4557 C C . SER B 1 282 ? 15.078 91.603 86.822 1.00 205.26 ? 1101 SER B C 1 +ATOM 4558 O O . SER B 1 282 ? 15.058 91.717 88.048 1.00 163.44 ? 1101 SER B O 1 +ATOM 4559 C CB . SER B 1 282 ? 14.947 89.206 86.119 1.00 210.59 ? 1101 SER B CB 1 +ATOM 4560 O OG . SER B 1 282 ? 16.209 89.309 85.482 1.00 199.60 ? 1101 SER B OG 1 +ATOM 4561 N N . ASP B 1 283 ? 15.839 92.359 86.034 1.00 214.88 ? 1102 ASP B N 1 +ATOM 4562 C CA . ASP B 1 283 ? 16.594 93.489 86.567 1.00 179.25 ? 1102 ASP B CA 1 +ATOM 4563 C C . ASP B 1 283 ? 15.719 94.738 86.560 1.00 150.09 ? 1102 ASP B C 1 +ATOM 4564 O O . ASP B 1 283 ? 16.089 95.771 87.124 1.00 116.15 ? 1102 ASP B O 1 +ATOM 4565 C CB . ASP B 1 283 ? 17.914 93.712 85.810 1.00 169.59 ? 1102 ASP B CB 1 +ATOM 4566 C CG . ASP B 1 283 ? 17.719 93.916 84.315 1.00 177.19 ? 1102 ASP B CG 1 +ATOM 4567 O OD1 . ASP B 1 283 ? 16.707 93.424 83.770 1.00 198.76 ? 1102 ASP B OD1 1 +ATOM 4568 O OD2 . ASP B 1 283 ? 18.589 94.561 83.685 1.00 129.38 ? 1102 ASP B OD2 1 +ATOM 4569 N N . GLY B 1 284 ? 14.555 94.619 85.919 1.00 145.66 ? 1103 GLY B N 1 +ATOM 4570 C CA . GLY B 1 284 ? 13.499 95.616 85.995 1.00 146.78 ? 1103 GLY B CA 1 +ATOM 4571 C C . GLY B 1 284 ? 13.893 96.999 85.524 1.00 174.39 ? 1103 GLY B C 1 +ATOM 4572 O O . GLY B 1 284 ? 13.366 98.004 86.007 1.00 112.65 ? 1103 GLY B O 1 +ATOM 4573 N N . ASN B 1 285 ? 14.831 97.034 84.579 1.00 218.85 ? 1104 ASN B N 1 +ATOM 4574 C CA . ASN B 1 285 ? 15.299 98.274 83.969 1.00 194.67 ? 1104 ASN B CA 1 +ATOM 4575 C C . ASN B 1 285 ? 14.734 98.435 82.563 1.00 144.62 ? 1104 ASN B C 1 +ATOM 4576 O O . ASN B 1 285 ? 15.438 98.213 81.580 1.00 143.30 ? 1104 ASN B O 1 +ATOM 4577 C CB . ASN B 1 285 ? 16.832 98.313 83.918 1.00 177.26 ? 1104 ASN B CB 1 +ATOM 4578 C CG . ASN B 1 285 ? 17.474 98.239 85.301 1.00 184.60 ? 1104 ASN B CG 1 +ATOM 4579 O OD1 . ASN B 1 285 ? 16.833 98.518 86.319 1.00 162.98 ? 1104 ASN B OD1 1 +ATOM 4580 N ND2 . ASN B 1 285 ? 18.751 97.868 85.339 1.00 157.97 ? 1104 ASN B ND2 1 +ATOM 4581 N N . PHE B 1 286 ? 13.460 98.825 82.492 1.00 132.78 ? 1105 PHE B N 1 +ATOM 4582 C CA . PHE B 1 286 ? 12.731 98.996 81.236 1.00 154.55 ? 1105 PHE B CA 1 +ATOM 4583 C C . PHE B 1 286 ? 13.235 100.198 80.439 1.00 198.51 ? 1105 PHE B C 1 +ATOM 4584 O O . PHE B 1 286 ? 13.447 101.279 80.993 1.00 210.40 ? 1105 PHE B O 1 +ATOM 4585 C CB . PHE B 1 286 ? 11.231 99.227 81.495 1.00 148.97 ? 1105 PHE B CB 1 +ATOM 4586 C CG . PHE B 1 286 ? 10.512 98.065 82.138 1.00 194.07 ? 1105 PHE B CG 1 +ATOM 4587 C CD1 . PHE B 1 286 ? 10.050 97.012 81.365 1.00 225.31 ? 1105 PHE B CD1 1 +ATOM 4588 C CD2 . PHE B 1 286 ? 10.248 98.055 83.507 1.00 162.38 ? 1105 PHE B CD2 1 +ATOM 4589 C CE1 . PHE B 1 286 ? 9.369 95.954 81.942 1.00 224.38 ? 1105 PHE B CE1 1 +ATOM 4590 C CE2 . PHE B 1 286 ? 9.572 96.996 84.093 1.00 126.02 ? 1105 PHE B CE2 1 +ATOM 4591 C CZ . PHE B 1 286 ? 9.131 95.943 83.308 1.00 175.79 ? 1105 PHE B CZ 1 +ATOM 4592 N N . ASN B 1 287 ? 13.405 99.999 79.136 1.00 208.25 ? 1106 ASN B N 1 +ATOM 4593 C CA . ASN B 1 287 ? 13.629 101.083 78.182 1.00 177.01 ? 1106 ASN B CA 1 +ATOM 4594 C C . ASN B 1 287 ? 13.035 100.683 76.836 1.00 163.89 ? 1106 ASN B C 1 +ATOM 4595 O O . ASN B 1 287 ? 12.955 99.496 76.528 1.00 142.91 ? 1106 ASN B O 1 +ATOM 4596 C CB . ASN B 1 287 ? 15.119 101.424 78.046 1.00 161.55 ? 1106 ASN B CB 1 +ATOM 4597 C CG . ASN B 1 287 ? 16.010 100.195 78.069 1.00 156.58 ? 1106 ASN B CG 1 +ATOM 4598 O OD1 . ASN B 1 287 ? 15.941 99.344 77.182 1.00 147.76 ? 1106 ASN B OD1 1 +ATOM 4599 N ND2 . ASN B 1 287 ? 16.869 100.109 79.079 1.00 133.73 ? 1106 ASN B ND2 1 +ATOM 4600 N N . TRP B 1 288 ? 12.612 101.666 76.046 1.00 163.87 ? 1107 TRP B N 1 +ATOM 4601 C CA . TRP B 1 288 ? 11.959 101.408 74.763 1.00 117.33 ? 1107 TRP B CA 1 +ATOM 4602 C C . TRP B 1 288 ? 12.733 100.471 73.836 1.00 137.33 ? 1107 TRP B C 1 +ATOM 4603 O O . TRP B 1 288 ? 12.137 99.774 73.016 1.00 120.35 ? 1107 TRP B O 1 +ATOM 4604 C CB . TRP B 1 288 ? 11.683 102.716 74.036 1.00 127.38 ? 1107 TRP B CB 1 +ATOM 4605 C CG . TRP B 1 288 ? 10.248 103.042 73.985 1.00 175.41 ? 1107 TRP B CG 1 +ATOM 4606 C CD1 . TRP B 1 288 ? 9.617 104.061 74.629 1.00 204.86 ? 1107 TRP B CD1 1 +ATOM 4607 C CD2 . TRP B 1 288 ? 9.238 102.335 73.258 1.00 192.40 ? 1107 TRP B CD2 1 +ATOM 4608 N NE1 . TRP B 1 288 ? 8.274 104.040 74.339 1.00 227.18 ? 1107 TRP B NE1 1 +ATOM 4609 C CE2 . TRP B 1 288 ? 8.017 102.987 73.499 1.00 221.78 ? 1107 TRP B CE2 1 +ATOM 4610 C CE3 . TRP B 1 288 ? 9.250 101.216 72.422 1.00 170.76 ? 1107 TRP B CE3 1 +ATOM 4611 C CZ2 . TRP B 1 288 ? 6.815 102.556 72.935 1.00 199.44 ? 1107 TRP B CZ2 1 +ATOM 4612 C CZ3 . TRP B 1 288 ? 8.058 100.792 71.859 1.00 148.69 ? 1107 TRP B CZ3 1 +ATOM 4613 C CH2 . TRP B 1 288 ? 6.858 101.457 72.120 1.00 149.02 ? 1107 TRP B CH2 1 +ATOM 4614 N N . GLY B 1 289 ? 14.056 100.460 73.966 1.00 130.29 ? 1108 GLY B N 1 +ATOM 4615 C CA . GLY B 1 289 ? 14.887 99.563 73.183 1.00 139.18 ? 1108 GLY B CA 1 +ATOM 4616 C C . GLY B 1 289 ? 14.506 98.105 73.371 1.00 161.75 ? 1108 GLY B C 1 +ATOM 4617 O O . GLY B 1 289 ? 14.438 97.340 72.406 1.00 151.09 ? 1108 GLY B O 1 +ATOM 4618 N N . ARG B 1 290 ? 14.246 97.727 74.620 1.00 161.11 ? 1109 ARG B N 1 +ATOM 4619 C CA . ARG B 1 290 ? 13.867 96.357 74.956 1.00 134.72 ? 1109 ARG B CA 1 +ATOM 4620 C C . ARG B 1 290 ? 12.422 96.051 74.589 1.00 139.57 ? 1109 ARG B C 1 +ATOM 4621 O O . ARG B 1 290 ? 12.095 94.932 74.202 1.00 122.45 ? 1109 ARG B O 1 +ATOM 4622 C CB . ARG B 1 290 ? 14.068 96.093 76.445 1.00 102.39 ? 1109 ARG B CB 1 +ATOM 4623 C CG . ARG B 1 290 ? 15.511 95.990 76.880 1.00 137.17 ? 1109 ARG B CG 1 +ATOM 4624 C CD . ARG B 1 290 ? 15.584 95.522 78.319 1.00 148.18 ? 1109 ARG B CD 1 +ATOM 4625 N NE . ARG B 1 290 ? 16.953 95.478 78.814 1.00 155.76 ? 1109 ARG B NE 1 +ATOM 4626 C CZ . ARG B 1 290 ? 17.273 95.222 80.076 1.00 174.28 ? 1109 ARG B CZ 1 +ATOM 4627 N NH1 . ARG B 1 290 ? 16.316 94.992 80.965 1.00 188.35 ? 1109 ARG B NH1 1 +ATOM 4628 N NH2 . ARG B 1 290 ? 18.545 95.199 80.448 1.00 162.55 ? 1109 ARG B NH2 1 +ATOM 4629 N N . VAL B 1 291 ? 11.559 97.050 74.736 1.00 140.05 ? 1110 VAL B N 1 +ATOM 4630 C CA . VAL B 1 291 ? 10.163 96.934 74.347 1.00 122.47 ? 1110 VAL B CA 1 +ATOM 4631 C C . VAL B 1 291 ? 10.090 96.589 72.868 1.00 119.60 ? 1110 VAL B C 1 +ATOM 4632 O O . VAL B 1 291 ? 9.255 95.793 72.436 1.00 124.32 ? 1110 VAL B O 1 +ATOM 4633 C CB . VAL B 1 291 ? 9.429 98.264 74.588 1.00 155.45 ? 1110 VAL B CB 1 +ATOM 4634 C CG1 . VAL B 1 291 ? 7.968 98.173 74.145 1.00 149.55 ? 1110 VAL B CG1 1 +ATOM 4635 C CG2 . VAL B 1 291 ? 9.554 98.683 76.056 1.00 126.23 ? 1110 VAL B CG2 1 +ATOM 4636 N N . VAL B 1 292 ? 10.993 97.189 72.102 1.00 123.95 ? 1111 VAL B N 1 +ATOM 4637 C CA . VAL B 1 292 ? 11.056 96.969 70.666 1.00 138.08 ? 1111 VAL B CA 1 +ATOM 4638 C C . VAL B 1 292 ? 11.785 95.666 70.337 1.00 136.77 ? 1111 VAL B C 1 +ATOM 4639 O O . VAL B 1 292 ? 11.311 94.886 69.512 1.00 137.27 ? 1111 VAL B O 1 +ATOM 4640 C CB . VAL B 1 292 ? 11.716 98.165 69.946 1.00 128.71 ? 1111 VAL B CB 1 +ATOM 4641 C CG1 . VAL B 1 292 ? 11.888 97.881 68.489 1.00 80.43 ? 1111 VAL B CG1 1 +ATOM 4642 C CG2 . VAL B 1 292 ? 10.863 99.397 70.099 1.00 149.06 ? 1111 VAL B CG2 1 +ATOM 4643 N N . ALA B 1 293 ? 12.922 95.420 70.990 1.00 131.46 ? 1112 ALA B N 1 +ATOM 4644 C CA . ALA B 1 293 ? 13.670 94.178 70.769 1.00 130.01 ? 1112 ALA B CA 1 +ATOM 4645 C C . ALA B 1 293 ? 12.857 92.952 71.178 1.00 143.73 ? 1112 ALA B C 1 +ATOM 4646 O O . ALA B 1 293 ? 13.044 91.862 70.649 1.00 120.35 ? 1112 ALA B O 1 +ATOM 4647 C CB . ALA B 1 293 ? 15.022 94.202 71.488 1.00 108.75 ? 1112 ALA B CB 1 +ATOM 4648 N N . LEU B 1 294 ? 11.941 93.128 72.117 1.00 159.13 ? 1113 LEU B N 1 +ATOM 4649 C CA . LEU B 1 294 ? 11.067 92.032 72.476 1.00 146.47 ? 1113 LEU B CA 1 +ATOM 4650 C C . LEU B 1 294 ? 9.865 92.014 71.537 1.00 134.94 ? 1113 LEU B C 1 +ATOM 4651 O O . LEU B 1 294 ? 9.188 90.997 71.405 1.00 142.88 ? 1113 LEU B O 1 +ATOM 4652 C CB . LEU B 1 294 ? 10.644 92.147 73.937 1.00 128.97 ? 1113 LEU B CB 1 +ATOM 4653 C CG . LEU B 1 294 ? 9.769 91.039 74.505 1.00 143.35 ? 1113 LEU B CG 1 +ATOM 4654 C CD1 . LEU B 1 294 ? 10.214 90.749 75.912 1.00 137.08 ? 1113 LEU B CD1 1 +ATOM 4655 C CD2 . LEU B 1 294 ? 8.318 91.474 74.487 1.00 168.65 ? 1113 LEU B CD2 1 +ATOM 4656 N N . PHE B 1 295 ? 9.608 93.141 70.877 1.00 116.81 ? 1114 PHE B N 1 +ATOM 4657 C CA . PHE B 1 295 ? 8.526 93.207 69.899 1.00 144.20 ? 1114 PHE B CA 1 +ATOM 4658 C C . PHE B 1 295 ? 9.018 92.757 68.525 1.00 159.72 ? 1114 PHE B C 1 +ATOM 4659 O O . PHE B 1 295 ? 8.231 92.641 67.592 1.00 168.41 ? 1114 PHE B O 1 +ATOM 4660 C CB . PHE B 1 295 ? 7.934 94.617 69.822 1.00 151.39 ? 1114 PHE B CB 1 +ATOM 4661 C CG . PHE B 1 295 ? 6.589 94.681 69.139 1.00 172.24 ? 1114 PHE B CG 1 +ATOM 4662 C CD1 . PHE B 1 295 ? 5.433 94.315 69.816 1.00 180.27 ? 1114 PHE B CD1 1 +ATOM 4663 C CD2 . PHE B 1 295 ? 6.479 95.123 67.828 1.00 148.37 ? 1114 PHE B CD2 1 +ATOM 4664 C CE1 . PHE B 1 295 ? 4.194 94.380 69.196 1.00 181.62 ? 1114 PHE B CE1 1 +ATOM 4665 C CE2 . PHE B 1 295 ? 5.243 95.190 67.201 1.00 162.79 ? 1114 PHE B CE2 1 +ATOM 4666 C CZ . PHE B 1 295 ? 4.099 94.819 67.888 1.00 185.14 ? 1114 PHE B CZ 1 +ATOM 4667 N N . TYR B 1 296 ? 10.327 92.529 68.409 1.00 163.89 ? 1115 TYR B N 1 +ATOM 4668 C CA . TYR B 1 296 ? 10.933 91.893 67.232 1.00 163.75 ? 1115 TYR B CA 1 +ATOM 4669 C C . TYR B 1 296 ? 10.895 90.404 67.520 1.00 168.83 ? 1115 TYR B C 1 +ATOM 4670 O O . TYR B 1 296 ? 10.784 89.577 66.615 1.00 136.25 ? 1115 TYR B O 1 +ATOM 4671 C CB . TYR B 1 296 ? 12.383 92.421 67.044 1.00 162.66 ? 1115 TYR B CB 1 +ATOM 4672 C CG . TYR B 1 296 ? 13.271 91.815 65.932 1.00 175.00 ? 1115 TYR B CG 1 +ATOM 4673 C CD1 . TYR B 1 296 ? 13.145 92.193 64.590 1.00 197.36 ? 1115 TYR B CD1 1 +ATOM 4674 C CD2 . TYR B 1 296 ? 14.227 90.859 66.239 1.00 165.15 ? 1115 TYR B CD2 1 +ATOM 4675 C CE1 . TYR B 1 296 ? 13.962 91.625 63.602 1.00 200.09 ? 1115 TYR B CE1 1 +ATOM 4676 C CE2 . TYR B 1 296 ? 15.037 90.295 65.264 1.00 159.31 ? 1115 TYR B CE2 1 +ATOM 4677 C CZ . TYR B 1 296 ? 14.902 90.673 63.954 1.00 158.10 ? 1115 TYR B CZ 1 +ATOM 4678 O OH . TYR B 1 296 ? 15.722 90.085 63.013 1.00 132.49 ? 1115 TYR B OH 1 +ATOM 4679 N N . PHE B 1 297 ? 10.971 90.070 68.803 1.00 181.08 ? 1116 PHE B N 1 +ATOM 4680 C CA . PHE B 1 297 ? 10.862 88.685 69.220 1.00 168.31 ? 1116 PHE B CA 1 +ATOM 4681 C C . PHE B 1 297 ? 9.428 88.186 69.017 1.00 151.42 ? 1116 PHE B C 1 +ATOM 4682 O O . PHE B 1 297 ? 9.187 87.348 68.151 1.00 121.77 ? 1116 PHE B O 1 +ATOM 4683 C CB . PHE B 1 297 ? 11.314 88.521 70.669 1.00 172.12 ? 1116 PHE B CB 1 +ATOM 4684 C CG . PHE B 1 297 ? 11.595 87.100 71.051 1.00 197.17 ? 1116 PHE B CG 1 +ATOM 4685 C CD1 . PHE B 1 297 ? 12.762 86.478 70.638 1.00 181.53 ? 1116 PHE B CD1 1 +ATOM 4686 C CD2 . PHE B 1 297 ? 10.690 86.382 71.816 1.00 220.84 ? 1116 PHE B CD2 1 +ATOM 4687 C CE1 . PHE B 1 297 ? 13.023 85.173 70.988 1.00 198.07 ? 1116 PHE B CE1 1 +ATOM 4688 C CE2 . PHE B 1 297 ? 10.944 85.073 72.168 1.00 215.26 ? 1116 PHE B CE2 1 +ATOM 4689 C CZ . PHE B 1 297 ? 12.112 84.468 71.753 1.00 212.56 ? 1116 PHE B CZ 1 +ATOM 4690 N N . ALA B 1 298 ? 8.481 88.719 69.790 1.00 143.54 ? 1117 ALA B N 1 +ATOM 4691 C CA . ALA B 1 298 ? 7.056 88.420 69.604 1.00 155.92 ? 1117 ALA B CA 1 +ATOM 4692 C C . ALA B 1 298 ? 6.624 88.547 68.135 1.00 188.97 ? 1117 ALA B C 1 +ATOM 4693 O O . ALA B 1 298 ? 5.690 87.873 67.686 1.00 175.75 ? 1117 ALA B O 1 +ATOM 4694 C CB . ALA B 1 298 ? 6.209 89.322 70.487 1.00 145.27 ? 1117 ALA B CB 1 +ATOM 4695 N N . SER B 1 299 ? 7.309 89.423 67.402 1.00 198.79 ? 1118 SER B N 1 +ATOM 4696 C CA . SER B 1 299 ? 7.196 89.482 65.949 1.00 187.30 ? 1118 SER B CA 1 +ATOM 4697 C C . SER B 1 299 ? 7.592 88.121 65.379 1.00 175.22 ? 1118 SER B C 1 +ATOM 4698 O O . SER B 1 299 ? 6.749 87.404 64.845 1.00 178.34 ? 1118 SER B O 1 +ATOM 4699 C CB . SER B 1 299 ? 8.097 90.590 65.382 1.00 181.72 ? 1118 SER B CB 1 +ATOM 4700 O OG . SER B 1 299 ? 7.830 90.883 64.018 1.00 174.45 ? 1118 SER B OG 1 +ATOM 4701 N N . LYS B 1 300 ? 8.867 87.754 65.532 1.00 154.13 ? 1119 LYS B N 1 +ATOM 4702 C CA . LYS B 1 300 ? 9.408 86.504 64.978 1.00 162.39 ? 1119 LYS B CA 1 +ATOM 4703 C C . LYS B 1 300 ? 8.661 85.230 65.415 1.00 197.73 ? 1119 LYS B C 1 +ATOM 4704 O O . LYS B 1 300 ? 8.858 84.165 64.827 1.00 192.11 ? 1119 LYS B O 1 +ATOM 4705 C CB . LYS B 1 300 ? 10.906 86.366 65.296 1.00 156.61 ? 1119 LYS B CB 1 +ATOM 4706 C CG . LYS B 1 300 ? 11.838 87.290 64.507 1.00 146.14 ? 1119 LYS B CG 1 +ATOM 4707 C CD . LYS B 1 300 ? 12.124 86.762 63.107 1.00 115.15 ? 1119 LYS B CD 1 +ATOM 4708 C CE . LYS B 1 300 ? 13.394 87.389 62.543 1.00 133.13 ? 1119 LYS B CE 1 +ATOM 4709 N NZ . LYS B 1 300 ? 13.460 87.310 61.051 1.00 153.50 ? 1119 LYS B NZ 1 +ATOM 4710 N N . LEU B 1 301 ? 7.813 85.341 66.439 1.00 217.21 ? 1120 LEU B N 1 +ATOM 4711 C CA . LEU B 1 301 ? 6.965 84.230 66.879 1.00 188.42 ? 1120 LEU B CA 1 +ATOM 4712 C C . LEU B 1 301 ? 5.703 84.151 66.035 1.00 183.14 ? 1120 LEU B C 1 +ATOM 4713 O O . LEU B 1 301 ? 4.588 84.241 66.556 1.00 153.62 ? 1120 LEU B O 1 +ATOM 4714 C CB . LEU B 1 301 ? 6.602 84.375 68.353 1.00 158.49 ? 1120 LEU B CB 1 +ATOM 4715 C CG . LEU B 1 301 ? 7.801 84.373 69.282 1.00 176.77 ? 1120 LEU B CG 1 +ATOM 4716 C CD1 . LEU B 1 301 ? 7.396 84.526 70.745 1.00 172.25 ? 1120 LEU B CD1 1 +ATOM 4717 C CD2 . LEU B 1 301 ? 8.631 83.107 69.055 1.00 166.42 ? 1120 LEU B CD2 1 +ATOM 4718 N N . VAL B 1 302 ? 5.903 83.983 64.729 1.00 205.22 ? 1121 VAL B N 1 +ATOM 4719 C CA . VAL B 1 302 ? 4.828 83.980 63.740 1.00 222.37 ? 1121 VAL B CA 1 +ATOM 4720 C C . VAL B 1 302 ? 5.119 83.004 62.589 1.00 223.94 ? 1121 VAL B C 1 +ATOM 4721 O O . VAL B 1 302 ? 4.385 82.030 62.399 1.00 233.82 ? 1121 VAL B O 1 +ATOM 4722 C CB . VAL B 1 302 ? 4.578 85.410 63.177 1.00 180.51 ? 1121 VAL B CB 1 +ATOM 4723 C CG1 . VAL B 1 302 ? 3.782 85.365 61.870 1.00 156.24 ? 1121 VAL B CG1 1 +ATOM 4724 C CG2 . VAL B 1 302 ? 3.877 86.288 64.214 1.00 159.22 ? 1121 VAL B CG2 1 +ATOM 4725 N N . LEU B 1 303 ? 6.199 83.261 61.847 1.00 204.73 ? 1122 LEU B N 1 +ATOM 4726 C CA . LEU B 1 303 ? 6.542 82.514 60.627 1.00 210.95 ? 1122 LEU B CA 1 +ATOM 4727 C C . LEU B 1 303 ? 6.577 80.992 60.795 1.00 209.08 ? 1122 LEU B C 1 +ATOM 4728 O O . LEU B 1 303 ? 6.181 80.248 59.893 1.00 194.96 ? 1122 LEU B O 1 +ATOM 4729 C CB . LEU B 1 303 ? 7.877 83.008 60.046 1.00 197.09 ? 1122 LEU B CB 1 +ATOM 4730 C CG . LEU B 1 303 ? 7.827 84.032 58.903 1.00 180.80 ? 1122 LEU B CG 1 +ATOM 4731 C CD1 . LEU B 1 303 ? 9.232 84.507 58.515 1.00 143.05 ? 1122 LEU B CD1 1 +ATOM 4732 C CD2 . LEU B 1 303 ? 7.078 83.473 57.683 1.00 135.52 ? 1122 LEU B CD2 1 +ATOM 4733 N N . SER C 1 5 ? 53.691 58.683 136.387 1.00 101.76 ? 2 SER C N 1 +ATOM 4734 C CA . SER C 1 5 ? 53.276 59.818 137.217 1.00 150.56 ? 2 SER C CA 1 +ATOM 4735 C C . SER C 1 5 ? 53.378 59.548 138.730 1.00 150.65 ? 2 SER C C 1 +ATOM 4736 O O . SER C 1 5 ? 53.360 58.395 139.169 1.00 115.92 ? 2 SER C O 1 +ATOM 4737 C CB . SER C 1 5 ? 51.854 60.272 136.845 1.00 146.04 ? 2 SER C CB 1 +ATOM 4738 O OG . SER C 1 5 ? 50.855 59.442 137.417 1.00 146.79 ? 2 SER C OG 1 +ATOM 4739 N N . LYS C 1 6 ? 53.493 60.620 139.517 1.00 143.50 ? 3 LYS C N 1 +ATOM 4740 C CA . LYS C 1 6 ? 53.487 60.521 140.979 1.00 136.88 ? 3 LYS C CA 1 +ATOM 4741 C C . LYS C 1 6 ? 52.043 60.507 141.484 1.00 145.00 ? 3 LYS C C 1 +ATOM 4742 O O . LYS C 1 6 ? 51.751 59.987 142.562 1.00 133.26 ? 3 LYS C O 1 +ATOM 4743 C CB . LYS C 1 6 ? 54.267 61.673 141.640 1.00 161.82 ? 3 LYS C CB 1 +ATOM 4744 C CG . LYS C 1 6 ? 55.419 62.267 140.816 1.00 184.34 ? 3 LYS C CG 1 +ATOM 4745 C CD . LYS C 1 6 ? 56.478 61.235 140.415 1.00 196.02 ? 3 LYS C CD 1 +ATOM 4746 C CE . LYS C 1 6 ? 56.988 61.493 138.991 1.00 172.80 ? 3 LYS C CE 1 +ATOM 4747 N NZ . LYS C 1 6 ? 57.874 60.409 138.472 1.00 143.82 ? 3 LYS C NZ 1 +ATOM 4748 N N . GLY C 1 7 ? 51.143 61.083 140.691 1.00 144.30 ? 4 GLY C N 1 +ATOM 4749 C CA . GLY C 1 7 ? 49.727 61.072 141.007 1.00 129.76 ? 4 GLY C CA 1 +ATOM 4750 C C . GLY C 1 7 ? 49.161 59.667 141.014 1.00 124.45 ? 4 GLY C C 1 +ATOM 4751 O O . GLY C 1 7 ? 48.315 59.331 141.845 1.00 110.85 ? 4 GLY C O 1 +ATOM 4752 N N . GLU C 1 8 ? 49.644 58.847 140.087 1.00 102.77 ? 5 GLU C N 1 +ATOM 4753 C CA . GLU C 1 8 ? 49.211 57.461 139.952 1.00 93.87 ? 5 GLU C CA 1 +ATOM 4754 C C . GLU C 1 8 ? 49.285 56.681 141.276 1.00 95.29 ? 5 GLU C C 1 +ATOM 4755 O O . GLU C 1 8 ? 48.468 55.792 141.524 1.00 120.47 ? 5 GLU C O 1 +ATOM 4756 C CB . GLU C 1 8 ? 50.046 56.770 138.865 1.00 114.42 ? 5 GLU C CB 1 +ATOM 4757 C CG . GLU C 1 8 ? 49.777 55.280 138.681 1.00 157.76 ? 5 GLU C CG 1 +ATOM 4758 C CD . GLU C 1 8 ? 48.729 54.985 137.620 1.00 182.18 ? 5 GLU C CD 1 +ATOM 4759 O OE1 . GLU C 1 8 ? 48.993 55.272 136.432 1.00 188.63 ? 5 GLU C OE1 1 +ATOM 4760 O OE2 . GLU C 1 8 ? 47.650 54.456 137.974 1.00 162.36 ? 5 GLU C OE2 1 +ATOM 4761 N N . GLU C 1 9 ? 50.248 57.036 142.127 1.00 100.46 ? 6 GLU C N 1 +ATOM 4762 C CA . GLU C 1 9 ? 50.482 56.343 143.399 1.00 92.20 ? 6 GLU C CA 1 +ATOM 4763 C C . GLU C 1 9 ? 49.413 56.621 144.449 1.00 105.15 ? 6 GLU C C 1 +ATOM 4764 O O . GLU C 1 9 ? 49.356 55.943 145.474 1.00 105.96 ? 6 GLU C O 1 +ATOM 4765 C CB . GLU C 1 9 ? 51.848 56.720 143.978 1.00 138.48 ? 6 GLU C CB 1 +ATOM 4766 C CG . GLU C 1 9 ? 53.044 56.231 143.172 1.00 168.54 ? 6 GLU C CG 1 +ATOM 4767 C CD . GLU C 1 9 ? 54.376 56.694 143.751 1.00 182.81 ? 6 GLU C CD 1 +ATOM 4768 O OE1 . GLU C 1 9 ? 54.375 57.549 144.664 1.00 172.83 ? 6 GLU C OE1 1 +ATOM 4769 O OE2 . GLU C 1 9 ? 55.428 56.203 143.289 1.00 190.16 ? 6 GLU C OE2 1 +ATOM 4770 N N . LEU C 1 10 ? 48.583 57.629 144.196 1.00 98.08 ? 7 LEU C N 1 +ATOM 4771 C CA . LEU C 1 10 ? 47.502 57.996 145.108 1.00 83.25 ? 7 LEU C CA 1 +ATOM 4772 C C . LEU C 1 10 ? 46.216 57.213 144.829 1.00 109.83 ? 7 LEU C C 1 +ATOM 4773 O O . LEU C 1 10 ? 45.273 57.232 145.624 1.00 89.50 ? 7 LEU C O 1 +ATOM 4774 C CB . LEU C 1 10 ? 47.225 59.498 145.011 1.00 83.33 ? 7 LEU C CB 1 +ATOM 4775 C CG . LEU C 1 10 ? 48.399 60.416 145.352 1.00 103.89 ? 7 LEU C CG 1 +ATOM 4776 C CD1 . LEU C 1 10 ? 48.196 61.813 144.799 1.00 96.25 ? 7 LEU C CD1 1 +ATOM 4777 C CD2 . LEU C 1 10 ? 48.603 60.466 146.851 1.00 105.38 ? 7 LEU C CD2 1 +ATOM 4778 N N . PHE C 1 11 ? 46.189 56.512 143.702 1.00 116.31 ? 8 PHE C N 1 +ATOM 4779 C CA . PHE C 1 11 ? 44.951 55.906 143.232 1.00 96.43 ? 8 PHE C CA 1 +ATOM 4780 C C . PHE C 1 11 ? 44.947 54.386 143.239 1.00 95.36 ? 8 PHE C C 1 +ATOM 4781 O O . PHE C 1 11 ? 43.978 53.765 142.793 1.00 99.04 ? 8 PHE C O 1 +ATOM 4782 C CB . PHE C 1 11 ? 44.578 56.461 141.861 1.00 101.65 ? 8 PHE C CB 1 +ATOM 4783 C CG . PHE C 1 11 ? 44.047 57.865 141.914 1.00 106.10 ? 8 PHE C CG 1 +ATOM 4784 C CD1 . PHE C 1 11 ? 44.905 58.950 141.887 1.00 82.08 ? 8 PHE C CD1 1 +ATOM 4785 C CD2 . PHE C 1 11 ? 42.687 58.095 142.015 1.00 84.62 ? 8 PHE C CD2 1 +ATOM 4786 C CE1 . PHE C 1 11 ? 44.412 60.235 141.942 1.00 97.45 ? 8 PHE C CE1 1 +ATOM 4787 C CE2 . PHE C 1 11 ? 42.195 59.369 142.064 1.00 96.26 ? 8 PHE C CE2 1 +ATOM 4788 C CZ . PHE C 1 11 ? 43.057 60.444 142.030 1.00 100.58 ? 8 PHE C CZ 1 +ATOM 4789 N N . THR C 1 12 ? 46.029 53.799 143.745 1.00 102.81 ? 9 THR C N 1 +ATOM 4790 C CA . THR C 1 12 ? 45.994 52.415 144.203 1.00 114.06 ? 9 THR C CA 1 +ATOM 4791 C C . THR C 1 12 ? 45.076 52.391 145.425 1.00 121.21 ? 9 THR C C 1 +ATOM 4792 O O . THR C 1 12 ? 45.058 53.338 146.215 1.00 125.16 ? 9 THR C O 1 +ATOM 4793 C CB . THR C 1 12 ? 47.396 51.888 144.605 1.00 63.46 ? 9 THR C CB 1 +ATOM 4794 O OG1 . THR C 1 12 ? 47.701 52.285 145.947 1.00 99.45 ? 9 THR C OG1 1 +ATOM 4795 C CG2 . THR C 1 12 ? 48.458 52.435 143.686 1.00 75.74 ? 9 THR C CG2 1 +ATOM 4796 N N . GLY C 1 13 ? 44.295 51.328 145.574 1.00 85.60 ? 10 GLY C N 1 +ATOM 4797 C CA . GLY C 1 13 ? 43.420 51.210 146.729 1.00 129.43 ? 10 GLY C CA 1 +ATOM 4798 C C . GLY C 1 13 ? 42.233 52.155 146.719 1.00 63.58 ? 10 GLY C C 1 +ATOM 4799 O O . GLY C 1 13 ? 42.221 53.155 146.007 1.00 86.47 ? 10 GLY C O 1 +ATOM 4800 N N . VAL C 1 14 ? 41.233 51.827 147.530 1.00 79.84 ? 11 VAL C N 1 +ATOM 4801 C CA . VAL C 1 14 ? 39.983 52.580 147.604 1.00 76.86 ? 11 VAL C CA 1 +ATOM 4802 C C . VAL C 1 14 ? 40.167 53.990 148.200 1.00 81.51 ? 11 VAL C C 1 +ATOM 4803 O O . VAL C 1 14 ? 40.642 54.149 149.328 1.00 83.47 ? 11 VAL C O 1 +ATOM 4804 C CB . VAL C 1 14 ? 38.913 51.783 148.399 1.00 60.63 ? 11 VAL C CB 1 +ATOM 4805 C CG1 . VAL C 1 14 ? 37.613 52.535 148.440 1.00 96.88 ? 11 VAL C CG1 1 +ATOM 4806 C CG2 . VAL C 1 14 ? 38.702 50.412 147.780 1.00 71.30 ? 11 VAL C CG2 1 +ATOM 4807 N N . VAL C 1 15 ? 39.801 55.003 147.413 1.00 78.38 ? 12 VAL C N 1 +ATOM 4808 C CA . VAL C 1 15 ? 39.877 56.409 147.820 1.00 91.58 ? 12 VAL C CA 1 +ATOM 4809 C C . VAL C 1 15 ? 38.498 56.951 148.158 1.00 95.67 ? 12 VAL C C 1 +ATOM 4810 O O . VAL C 1 15 ? 37.558 56.763 147.384 1.00 76.89 ? 12 VAL C O 1 +ATOM 4811 C CB . VAL C 1 15 ? 40.395 57.302 146.681 1.00 74.59 ? 12 VAL C CB 1 +ATOM 4812 C CG1 . VAL C 1 15 ? 40.399 58.758 147.117 1.00 76.23 ? 12 VAL C CG1 1 +ATOM 4813 C CG2 . VAL C 1 15 ? 41.776 56.870 146.234 1.00 72.04 ? 12 VAL C CG2 1 +ATOM 4814 N N . PRO C 1 16 ? 38.370 57.639 149.306 1.00 79.66 ? 13 PRO C N 1 +ATOM 4815 C CA . PRO C 1 16 ? 37.086 58.273 149.631 1.00 99.11 ? 13 PRO C CA 1 +ATOM 4816 C C . PRO C 1 16 ? 36.783 59.521 148.761 1.00 74.44 ? 13 PRO C C 1 +ATOM 4817 O O . PRO C 1 16 ? 37.674 60.331 148.487 1.00 85.45 ? 13 PRO C O 1 +ATOM 4818 C CB . PRO C 1 16 ? 37.222 58.598 151.129 1.00 59.41 ? 13 PRO C CB 1 +ATOM 4819 C CG . PRO C 1 16 ? 38.685 58.672 151.377 1.00 84.66 ? 13 PRO C CG 1 +ATOM 4820 C CD . PRO C 1 16 ? 39.353 57.755 150.399 1.00 73.48 ? 13 PRO C CD 1 +ATOM 4821 N N . ILE C 1 17 ? 35.531 59.644 148.315 1.00 84.42 ? 14 ILE C N 1 +ATOM 4822 C CA . ILE C 1 17 ? 35.108 60.727 147.419 1.00 83.28 ? 14 ILE C CA 1 +ATOM 4823 C C . ILE C 1 17 ? 34.024 61.596 148.034 1.00 73.87 ? 14 ILE C C 1 +ATOM 4824 O O . ILE C 1 17 ? 33.100 61.102 148.685 1.00 70.95 ? 14 ILE C O 1 +ATOM 4825 C CB . ILE C 1 17 ? 34.572 60.186 146.079 1.00 78.05 ? 14 ILE C CB 1 +ATOM 4826 C CG1 . ILE C 1 17 ? 35.665 59.467 145.315 1.00 75.93 ? 14 ILE C CG1 1 +ATOM 4827 C CG2 . ILE C 1 17 ? 34.043 61.299 145.193 1.00 53.00 ? 14 ILE C CG2 1 +ATOM 4828 C CD1 . ILE C 1 17 ? 35.147 58.856 144.054 1.00 96.84 ? 14 ILE C CD1 1 +ATOM 4829 N N . LEU C 1 18 ? 34.143 62.898 147.800 1.00 69.37 ? 15 LEU C N 1 +ATOM 4830 C CA . LEU C 1 18 ? 33.199 63.873 148.311 1.00 85.79 ? 15 LEU C CA 1 +ATOM 4831 C C . LEU C 1 18 ? 32.830 64.856 147.194 1.00 86.81 ? 15 LEU C C 1 +ATOM 4832 O O . LEU C 1 18 ? 33.707 65.382 146.512 1.00 67.72 ? 15 LEU C O 1 +ATOM 4833 C CB . LEU C 1 18 ? 33.841 64.596 149.490 1.00 55.54 ? 15 LEU C CB 1 +ATOM 4834 C CG . LEU C 1 18 ? 33.068 65.721 150.153 1.00 110.49 ? 15 LEU C CG 1 +ATOM 4835 C CD1 . LEU C 1 18 ? 31.784 65.179 150.767 1.00 115.49 ? 15 LEU C CD1 1 +ATOM 4836 C CD2 . LEU C 1 18 ? 33.958 66.404 151.190 1.00 121.22 ? 15 LEU C CD2 1 +ATOM 4837 N N . VAL C 1 19 ? 31.532 65.094 147.000 1.00 77.81 ? 16 VAL C N 1 +ATOM 4838 C CA . VAL C 1 19 ? 31.059 65.944 145.903 1.00 89.07 ? 16 VAL C CA 1 +ATOM 4839 C C . VAL C 1 19 ? 30.054 67.034 146.327 1.00 90.35 ? 16 VAL C C 1 +ATOM 4840 O O . VAL C 1 19 ? 29.028 66.739 146.955 1.00 79.13 ? 16 VAL C O 1 +ATOM 4841 C CB . VAL C 1 19 ? 30.452 65.089 144.769 1.00 79.81 ? 16 VAL C CB 1 +ATOM 4842 C CG1 . VAL C 1 19 ? 29.722 65.959 143.761 1.00 68.65 ? 16 VAL C CG1 1 +ATOM 4843 C CG2 . VAL C 1 19 ? 31.535 64.273 144.089 1.00 75.95 ? 16 VAL C CG2 1 +ATOM 4844 N N . GLU C 1 20 ? 30.370 68.286 145.962 1.00 86.31 ? 17 GLU C N 1 +ATOM 4845 C CA . GLU C 1 20 ? 29.541 69.473 146.248 1.00 64.23 ? 17 GLU C CA 1 +ATOM 4846 C C . GLU C 1 20 ? 29.104 70.253 144.988 1.00 92.26 ? 17 GLU C C 1 +ATOM 4847 O O . GLU C 1 20 ? 29.949 70.757 144.241 1.00 84.12 ? 17 GLU C O 1 +ATOM 4848 C CB . GLU C 1 20 ? 30.299 70.444 147.168 1.00 86.30 ? 17 GLU C CB 1 +ATOM 4849 C CG . GLU C 1 20 ? 30.750 69.880 148.512 1.00 112.53 ? 17 GLU C CG 1 +ATOM 4850 C CD . GLU C 1 20 ? 29.600 69.575 149.460 1.00 132.24 ? 17 GLU C CD 1 +ATOM 4851 O OE1 . GLU C 1 20 ? 28.428 69.818 149.092 1.00 132.44 ? 17 GLU C OE1 1 +ATOM 4852 O OE2 . GLU C 1 20 ? 29.875 69.090 150.580 1.00 130.72 ? 17 GLU C OE2 1 +ATOM 4853 N N . LEU C 1 21 ? 27.794 70.386 144.767 1.00 71.68 ? 18 LEU C N 1 +ATOM 4854 C CA . LEU C 1 21 ? 27.299 71.164 143.622 1.00 73.37 ? 18 LEU C CA 1 +ATOM 4855 C C . LEU C 1 21 ? 26.338 72.319 143.982 1.00 82.59 ? 18 LEU C C 1 +ATOM 4856 O O . LEU C 1 21 ? 25.437 72.152 144.808 1.00 102.49 ? 18 LEU C O 1 +ATOM 4857 C CB . LEU C 1 21 ? 26.656 70.234 142.584 1.00 91.17 ? 18 LEU C CB 1 +ATOM 4858 C CG . LEU C 1 21 ? 26.013 70.862 141.342 1.00 69.29 ? 18 LEU C CG 1 +ATOM 4859 C CD1 . LEU C 1 21 ? 27.028 71.587 140.530 1.00 125.51 ? 18 LEU C CD1 1 +ATOM 4860 C CD2 . LEU C 1 21 ? 25.312 69.822 140.481 1.00 103.08 ? 18 LEU C CD2 1 +ATOM 4861 N N . ASP C 1 22 ? 26.555 73.486 143.361 1.00 85.92 ? 19 ASP C N 1 +ATOM 4862 C CA . ASP C 1 22 ? 25.624 74.631 143.418 1.00 105.53 ? 19 ASP C CA 1 +ATOM 4863 C C . ASP C 1 22 ? 25.021 74.939 142.034 1.00 96.70 ? 19 ASP C C 1 +ATOM 4864 O O . ASP C 1 22 ? 25.740 75.287 141.096 1.00 95.99 ? 19 ASP C O 1 +ATOM 4865 C CB . ASP C 1 22 ? 26.319 75.889 143.963 1.00 92.49 ? 19 ASP C CB 1 +ATOM 4866 C CG . ASP C 1 22 ? 26.487 75.872 145.481 1.00 129.79 ? 19 ASP C CG 1 +ATOM 4867 O OD1 . ASP C 1 22 ? 25.639 75.282 146.189 1.00 138.28 ? 19 ASP C OD1 1 +ATOM 4868 O OD2 . ASP C 1 22 ? 27.473 76.469 145.965 1.00 159.40 ? 19 ASP C OD2 1 +ATOM 4869 N N . GLY C 1 23 ? 23.703 74.827 141.909 1.00 91.45 ? 20 GLY C N 1 +ATOM 4870 C CA . GLY C 1 23 ? 23.072 74.931 140.604 1.00 55.68 ? 20 GLY C CA 1 +ATOM 4871 C C . GLY C 1 23 ? 22.037 76.029 140.430 1.00 111.25 ? 20 GLY C C 1 +ATOM 4872 O O . GLY C 1 23 ? 21.436 76.494 141.397 1.00 110.86 ? 20 GLY C O 1 +ATOM 4873 N N . ASP C 1 24 ? 21.836 76.426 139.174 1.00 117.22 ? 21 ASP C N 1 +ATOM 4874 C CA . ASP C 1 24 ? 20.873 77.455 138.782 1.00 81.92 ? 21 ASP C CA 1 +ATOM 4875 C C . ASP C 1 24 ? 20.364 77.153 137.354 1.00 94.43 ? 21 ASP C C 1 +ATOM 4876 O O . ASP C 1 24 ? 21.088 77.366 136.380 1.00 100.63 ? 21 ASP C O 1 +ATOM 4877 C CB . ASP C 1 24 ? 21.545 78.839 138.841 1.00 148.23 ? 21 ASP C CB 1 +ATOM 4878 C CG . ASP C 1 24 ? 20.543 80.001 138.866 1.00 158.17 ? 21 ASP C CG 1 +ATOM 4879 O OD1 . ASP C 1 24 ? 19.345 79.783 138.578 1.00 135.32 ? 21 ASP C OD1 1 +ATOM 4880 O OD2 . ASP C 1 24 ? 20.964 81.143 139.172 1.00 116.05 ? 21 ASP C OD2 1 +ATOM 4881 N N . VAL C 1 25 ? 19.133 76.646 137.230 1.00 89.18 ? 22 VAL C N 1 +ATOM 4882 C CA . VAL C 1 25 ? 18.571 76.260 135.922 1.00 90.36 ? 22 VAL C CA 1 +ATOM 4883 C C . VAL C 1 25 ? 17.227 76.947 135.637 1.00 99.51 ? 22 VAL C C 1 +ATOM 4884 O O . VAL C 1 25 ? 16.187 76.568 136.190 1.00 81.06 ? 22 VAL C O 1 +ATOM 4885 C CB . VAL C 1 25 ? 18.467 74.705 135.758 1.00 74.02 ? 22 VAL C CB 1 +ATOM 4886 C CG1 . VAL C 1 25 ? 17.545 74.312 134.609 1.00 80.14 ? 22 VAL C CG1 1 +ATOM 4887 C CG2 . VAL C 1 25 ? 19.832 74.110 135.528 1.00 98.24 ? 22 VAL C CG2 1 +ATOM 4888 N N . ASN C 1 26 ? 17.273 77.954 134.761 1.00 92.43 ? 23 ASN C N 1 +ATOM 4889 C CA . ASN C 1 26 ? 16.135 78.833 134.486 1.00 88.83 ? 23 ASN C CA 1 +ATOM 4890 C C . ASN C 1 26 ? 15.663 79.486 135.796 1.00 114.15 ? 23 ASN C C 1 +ATOM 4891 O O . ASN C 1 26 ? 14.478 79.455 136.145 1.00 88.01 ? 23 ASN C O 1 +ATOM 4892 C CB . ASN C 1 26 ? 14.989 78.086 133.771 1.00 84.28 ? 23 ASN C CB 1 +ATOM 4893 C CG . ASN C 1 26 ? 15.231 77.883 132.257 1.00 112.66 ? 23 ASN C CG 1 +ATOM 4894 O OD1 . ASN C 1 26 ? 16.322 78.123 131.727 1.00 89.10 ? 23 ASN C OD1 1 +ATOM 4895 N ND2 . ASN C 1 26 ? 14.193 77.426 131.564 1.00 87.38 ? 23 ASN C ND2 1 +ATOM 4896 N N . GLY C 1 27 ? 16.621 80.052 136.528 1.00 95.62 ? 24 GLY C N 1 +ATOM 4897 C CA . GLY C 1 27 ? 16.352 80.667 137.815 1.00 96.07 ? 24 GLY C CA 1 +ATOM 4898 C C . GLY C 1 27 ? 15.925 79.738 138.945 1.00 106.48 ? 24 GLY C C 1 +ATOM 4899 O O . GLY C 1 27 ? 15.564 80.222 140.026 1.00 99.05 ? 24 GLY C O 1 +ATOM 4900 N N . HIS C 1 28 ? 15.931 78.425 138.699 1.00 97.55 ? 25 HIS C N 1 +ATOM 4901 C CA . HIS C 1 28 ? 15.784 77.436 139.771 1.00 104.92 ? 25 HIS C CA 1 +ATOM 4902 C C . HIS C 1 28 ? 17.140 77.124 140.342 1.00 111.86 ? 25 HIS C C 1 +ATOM 4903 O O . HIS C 1 28 ? 18.014 76.593 139.649 1.00 77.39 ? 25 HIS C O 1 +ATOM 4904 C CB . HIS C 1 28 ? 15.205 76.123 139.274 1.00 63.63 ? 25 HIS C CB 1 +ATOM 4905 C CG . HIS C 1 28 ? 13.790 76.220 138.819 1.00 128.19 ? 25 HIS C CG 1 +ATOM 4906 N ND1 . HIS C 1 28 ? 13.439 76.790 137.615 1.00 108.40 ? 25 HIS C ND1 1 +ATOM 4907 C CD2 . HIS C 1 28 ? 12.637 75.810 139.396 1.00 123.37 ? 25 HIS C CD2 1 +ATOM 4908 C CE1 . HIS C 1 28 ? 12.127 76.729 137.471 1.00 99.07 ? 25 HIS C CE1 1 +ATOM 4909 N NE2 . HIS C 1 28 ? 11.618 76.138 138.537 1.00 129.35 ? 25 HIS C NE2 1 +ATOM 4910 N N . LYS C 1 29 ? 17.310 77.454 141.612 1.00 81.95 ? 26 LYS C N 1 +ATOM 4911 C CA . LYS C 1 29 ? 18.551 77.180 142.287 1.00 82.53 ? 26 LYS C CA 1 +ATOM 4912 C C . LYS C 1 29 ? 18.380 75.837 142.977 1.00 104.37 ? 26 LYS C C 1 +ATOM 4913 O O . LYS C 1 29 ? 17.249 75.374 143.154 1.00 96.26 ? 26 LYS C O 1 +ATOM 4914 C CB . LYS C 1 29 ? 18.875 78.301 143.277 1.00 90.12 ? 26 LYS C CB 1 +ATOM 4915 C CG . LYS C 1 29 ? 19.093 79.667 142.616 1.00 76.24 ? 26 LYS C CG 1 +ATOM 4916 C CD . LYS C 1 29 ? 19.390 80.753 143.648 1.00 122.01 ? 26 LYS C CD 1 +ATOM 4917 C CE . LYS C 1 29 ? 19.826 82.066 143.000 1.00 105.81 ? 26 LYS C CE 1 +ATOM 4918 N NZ . LYS C 1 29 ? 21.159 81.991 142.335 1.00 130.70 ? 26 LYS C NZ 1 +ATOM 4919 N N . PHE C 1 30 ? 19.500 75.199 143.316 1.00 77.98 ? 27 PHE C N 1 +ATOM 4920 C CA . PHE C 1 30 ? 19.511 73.931 144.047 1.00 71.95 ? 27 PHE C CA 1 +ATOM 4921 C C . PHE C 1 30 ? 20.926 73.554 144.453 1.00 84.14 ? 27 PHE C C 1 +ATOM 4922 O O . PHE C 1 30 ? 21.901 74.060 143.896 1.00 81.60 ? 27 PHE C O 1 +ATOM 4923 C CB . PHE C 1 30 ? 18.895 72.789 143.225 1.00 98.02 ? 27 PHE C CB 1 +ATOM 4924 C CG . PHE C 1 30 ? 19.584 72.491 141.937 1.00 93.75 ? 27 PHE C CG 1 +ATOM 4925 C CD1 . PHE C 1 30 ? 19.324 73.244 140.812 1.00 97.61 ? 27 PHE C CD1 1 +ATOM 4926 C CD2 . PHE C 1 30 ? 20.505 71.466 141.842 1.00 91.80 ? 27 PHE C CD2 1 +ATOM 4927 C CE1 . PHE C 1 30 ? 19.958 72.983 139.622 1.00 93.77 ? 27 PHE C CE1 1 +ATOM 4928 C CE2 . PHE C 1 30 ? 21.149 71.205 140.647 1.00 94.78 ? 27 PHE C CE2 1 +ATOM 4929 C CZ . PHE C 1 30 ? 20.873 71.967 139.539 1.00 81.21 ? 27 PHE C CZ 1 +ATOM 4930 N N . SER C 1 31 ? 21.028 72.660 145.430 1.00 84.76 ? 28 SER C N 1 +ATOM 4931 C CA . SER C 1 31 ? 22.321 72.166 145.883 1.00 86.42 ? 28 SER C CA 1 +ATOM 4932 C C . SER C 1 31 ? 22.319 70.651 146.093 1.00 89.70 ? 28 SER C C 1 +ATOM 4933 O O . SER C 1 31 ? 21.316 70.056 146.518 1.00 69.67 ? 28 SER C O 1 +ATOM 4934 C CB . SER C 1 31 ? 22.772 72.897 147.148 1.00 86.25 ? 28 SER C CB 1 +ATOM 4935 O OG . SER C 1 31 ? 23.004 74.267 146.877 1.00 111.78 ? 28 SER C OG 1 +ATOM 4936 N N . VAL C 1 32 ? 23.455 70.041 145.755 1.00 78.18 ? 29 VAL C N 1 +ATOM 4937 C CA . VAL C 1 32 ? 23.657 68.598 145.889 1.00 91.96 ? 29 VAL C CA 1 +ATOM 4938 C C . VAL C 1 32 ? 24.990 68.256 146.569 1.00 79.08 ? 29 VAL C C 1 +ATOM 4939 O O . VAL C 1 32 ? 26.051 68.791 146.210 1.00 62.61 ? 29 VAL C O 1 +ATOM 4940 C CB . VAL C 1 32 ? 23.597 67.862 144.519 1.00 76.14 ? 29 VAL C CB 1 +ATOM 4941 C CG1 . VAL C 1 32 ? 23.645 66.355 144.723 1.00 81.11 ? 29 VAL C CG1 1 +ATOM 4942 C CG2 . VAL C 1 32 ? 22.344 68.233 143.749 1.00 56.76 ? 29 VAL C CG2 1 +ATOM 4943 N N . SER C 1 33 ? 24.914 67.372 147.563 1.00 72.80 ? 30 SER C N 1 +ATOM 4944 C CA . SER C 1 33 ? 26.092 66.768 148.190 1.00 96.59 ? 30 SER C CA 1 +ATOM 4945 C C . SER C 1 33 ? 26.159 65.266 147.935 1.00 99.48 ? 30 SER C C 1 +ATOM 4946 O O . SER C 1 33 ? 25.165 64.544 148.084 1.00 70.43 ? 30 SER C O 1 +ATOM 4947 C CB . SER C 1 33 ? 26.118 67.025 149.694 1.00 77.42 ? 30 SER C CB 1 +ATOM 4948 O OG . SER C 1 33 ? 26.622 68.316 149.966 1.00 111.60 ? 30 SER C OG 1 +ATOM 4949 N N . GLY C 1 34 ? 27.341 64.804 147.547 1.00 100.16 ? 31 GLY C N 1 +ATOM 4950 C CA . GLY C 1 34 ? 27.546 63.401 147.266 1.00 53.39 ? 31 GLY C CA 1 +ATOM 4951 C C . GLY C 1 34 ? 28.767 62.851 147.966 1.00 76.29 ? 31 GLY C C 1 +ATOM 4952 O O . GLY C 1 34 ? 29.820 63.490 147.980 1.00 72.29 ? 31 GLY C O 1 +ATOM 4953 N N . GLU C 1 35 ? 28.622 61.670 148.561 1.00 65.83 ? 32 GLU C N 1 +ATOM 4954 C CA . GLU C 1 35 ? 29.772 60.928 149.072 1.00 87.51 ? 32 GLU C CA 1 +ATOM 4955 C C . GLU C 1 35 ? 29.831 59.490 148.549 1.00 77.92 ? 32 GLU C C 1 +ATOM 4956 O O . GLU C 1 35 ? 28.803 58.861 148.278 1.00 84.00 ? 32 GLU C O 1 +ATOM 4957 C CB . GLU C 1 35 ? 29.821 60.950 150.608 1.00 78.43 ? 32 GLU C CB 1 +ATOM 4958 C CG . GLU C 1 35 ? 28.694 60.202 151.313 1.00 88.78 ? 32 GLU C CG 1 +ATOM 4959 C CD . GLU C 1 35 ? 28.321 60.831 152.661 1.00 169.55 ? 32 GLU C CD 1 +ATOM 4960 O OE1 . GLU C 1 35 ? 29.158 61.535 153.247 1.00 169.24 ? 32 GLU C OE1 1 +ATOM 4961 O OE2 . GLU C 1 35 ? 27.184 60.638 153.136 1.00 208.34 ? 32 GLU C OE2 1 +ATOM 4962 N N . GLY C 1 36 ? 31.053 58.989 148.404 1.00 97.71 ? 33 GLY C N 1 +ATOM 4963 C CA . GLY C 1 36 ? 31.299 57.591 148.105 1.00 69.09 ? 33 GLY C CA 1 +ATOM 4964 C C . GLY C 1 36 ? 32.786 57.299 148.060 1.00 68.64 ? 33 GLY C C 1 +ATOM 4965 O O . GLY C 1 36 ? 33.575 57.945 148.750 1.00 82.51 ? 33 GLY C O 1 +ATOM 4966 N N . GLU C 1 37 ? 33.161 56.333 147.225 1.00 77.32 ? 34 GLU C N 1 +ATOM 4967 C CA . GLU C 1 37 ? 34.537 55.867 147.109 1.00 80.16 ? 34 GLU C CA 1 +ATOM 4968 C C . GLU C 1 37 ? 34.838 55.398 145.687 1.00 75.90 ? 34 GLU C C 1 +ATOM 4969 O O . GLU C 1 37 ? 33.935 54.984 144.951 1.00 75.05 ? 34 GLU C O 1 +ATOM 4970 C CB . GLU C 1 37 ? 34.780 54.717 148.083 1.00 74.23 ? 34 GLU C CB 1 +ATOM 4971 C CG . GLU C 1 37 ? 33.911 53.503 147.782 1.00 139.93 ? 34 GLU C CG 1 +ATOM 4972 C CD . GLU C 1 37 ? 34.044 52.399 148.805 1.00 136.62 ? 34 GLU C CD 1 +ATOM 4973 O OE1 . GLU C 1 37 ? 35.033 52.399 149.564 1.00 141.77 ? 34 GLU C OE1 1 +ATOM 4974 O OE2 . GLU C 1 37 ? 33.139 51.537 148.853 1.00 136.37 ? 34 GLU C OE2 1 +ATOM 4975 N N . GLY C 1 38 ? 36.115 55.454 145.315 1.00 73.52 ? 35 GLY C N 1 +ATOM 4976 C CA . GLY C 1 38 ? 36.543 55.098 143.974 1.00 85.78 ? 35 GLY C CA 1 +ATOM 4977 C C . GLY C 1 38 ? 37.734 54.158 143.928 1.00 77.98 ? 35 GLY C C 1 +ATOM 4978 O O . GLY C 1 38 ? 38.680 54.293 144.702 1.00 78.23 ? 35 GLY C O 1 +ATOM 4979 N N . ASP C 1 39 ? 37.683 53.204 143.005 1.00 89.07 ? 36 ASP C N 1 +ATOM 4980 C CA . ASP C 1 39 ? 38.727 52.196 142.857 1.00 85.65 ? 36 ASP C CA 1 +ATOM 4981 C C . ASP C 1 39 ? 39.297 52.225 141.443 1.00 66.32 ? 36 ASP C C 1 +ATOM 4982 O O . ASP C 1 39 ? 38.783 51.555 140.550 1.00 85.83 ? 36 ASP C O 1 +ATOM 4983 C CB . ASP C 1 39 ? 38.151 50.809 143.148 1.00 83.15 ? 36 ASP C CB 1 +ATOM 4984 C CG . ASP C 1 39 ? 39.054 49.978 144.029 1.00 121.82 ? 36 ASP C CG 1 +ATOM 4985 O OD1 . ASP C 1 39 ? 40.263 50.292 144.075 1.00 125.00 ? 36 ASP C OD1 1 +ATOM 4986 O OD2 . ASP C 1 39 ? 38.558 49.019 144.670 1.00 106.41 ? 36 ASP C OD2 1 +ATOM 4987 N N . ALA C 1 40 ? 40.356 53.000 141.236 1.00 90.37 ? 37 ALA C N 1 +ATOM 4988 C CA . ALA C 1 40 ? 40.929 53.161 139.899 1.00 75.72 ? 37 ALA C CA 1 +ATOM 4989 C C . ALA C 1 40 ? 41.508 51.863 139.350 1.00 74.61 ? 37 ALA C C 1 +ATOM 4990 O O . ALA C 1 40 ? 41.617 51.693 138.145 1.00 88.69 ? 37 ALA C O 1 +ATOM 4991 C CB . ALA C 1 40 ? 41.993 54.235 139.908 1.00 55.65 ? 37 ALA C CB 1 +ATOM 4992 N N . THR C 1 41 ? 41.885 50.962 140.248 1.00 93.87 ? 38 THR C N 1 +ATOM 4993 C CA . THR C 1 41 ? 42.530 49.712 139.887 1.00 63.42 ? 38 THR C CA 1 +ATOM 4994 C C . THR C 1 41 ? 41.601 48.844 139.055 1.00 85.86 ? 38 THR C C 1 +ATOM 4995 O O . THR C 1 41 ? 42.040 48.166 138.129 1.00 89.38 ? 38 THR C O 1 +ATOM 4996 C CB . THR C 1 41 ? 42.932 48.934 141.143 1.00 82.10 ? 38 THR C CB 1 +ATOM 4997 O OG1 . THR C 1 41 ? 43.646 49.797 142.035 1.00 97.73 ? 38 THR C OG1 1 +ATOM 4998 C CG2 . THR C 1 41 ? 43.807 47.781 140.777 1.00 48.98 ? 38 THR C CG2 1 +ATOM 4999 N N . TYR C 1 42 ? 40.315 48.870 139.393 1.00 76.60 ? 39 TYR C N 1 +ATOM 5000 C CA . TYR C 1 42 ? 39.310 48.133 138.636 1.00 84.30 ? 39 TYR C CA 1 +ATOM 5001 C C . TYR C 1 42 ? 38.288 49.094 138.070 1.00 59.67 ? 39 TYR C C 1 +ATOM 5002 O O . TYR C 1 42 ? 37.149 48.708 137.798 1.00 75.70 ? 39 TYR C O 1 +ATOM 5003 C CB . TYR C 1 42 ? 38.627 47.087 139.511 1.00 65.21 ? 39 TYR C CB 1 +ATOM 5004 C CG . TYR C 1 42 ? 39.603 46.397 140.412 1.00 80.37 ? 39 TYR C CG 1 +ATOM 5005 C CD1 . TYR C 1 42 ? 40.321 45.288 139.975 1.00 81.26 ? 39 TYR C CD1 1 +ATOM 5006 C CD2 . TYR C 1 42 ? 39.837 46.876 141.695 1.00 96.59 ? 39 TYR C CD2 1 +ATOM 5007 C CE1 . TYR C 1 42 ? 41.238 44.661 140.809 1.00 82.78 ? 39 TYR C CE1 1 +ATOM 5008 C CE2 . TYR C 1 42 ? 40.742 46.265 142.530 1.00 109.91 ? 39 TYR C CE2 1 +ATOM 5009 C CZ . TYR C 1 42 ? 41.443 45.159 142.089 1.00 101.76 ? 39 TYR C CZ 1 +ATOM 5010 O OH . TYR C 1 42 ? 42.348 44.566 142.944 1.00 85.93 ? 39 TYR C OH 1 +ATOM 5011 N N . GLY C 1 43 ? 38.717 50.346 137.914 1.00 73.26 ? 40 GLY C N 1 +ATOM 5012 C CA . GLY C 1 43 ? 37.941 51.395 137.268 1.00 81.04 ? 40 GLY C CA 1 +ATOM 5013 C C . GLY C 1 43 ? 36.502 51.495 137.736 1.00 97.17 ? 40 GLY C C 1 +ATOM 5014 O O . GLY C 1 43 ? 35.566 51.491 136.931 1.00 64.57 ? 40 GLY C O 1 +ATOM 5015 N N . LYS C 1 44 ? 36.334 51.604 139.049 1.00 85.01 ? 41 LYS C N 1 +ATOM 5016 C CA . LYS C 1 44 ? 35.039 51.435 139.678 1.00 52.93 ? 41 LYS C CA 1 +ATOM 5017 C C . LYS C 1 44 ? 34.672 52.652 140.530 1.00 81.89 ? 41 LYS C C 1 +ATOM 5018 O O . LYS C 1 44 ? 35.530 53.258 141.175 1.00 79.41 ? 41 LYS C O 1 +ATOM 5019 C CB . LYS C 1 44 ? 35.082 50.172 140.527 1.00 69.37 ? 41 LYS C CB 1 +ATOM 5020 C CG . LYS C 1 44 ? 33.751 49.709 140.973 1.00 92.84 ? 41 LYS C CG 1 +ATOM 5021 C CD . LYS C 1 44 ? 33.895 48.638 142.012 1.00 71.06 ? 41 LYS C CD 1 +ATOM 5022 C CE . LYS C 1 44 ? 32.748 48.731 142.985 1.00 114.93 ? 41 LYS C CE 1 +ATOM 5023 N NZ . LYS C 1 44 ? 32.436 47.432 143.637 1.00 110.01 ? 41 LYS C NZ 1 +ATOM 5024 N N . LEU C 1 45 ? 33.391 53.008 140.524 1.00 102.72 ? 42 LEU C N 1 +ATOM 5025 C CA . LEU C 1 45 ? 32.922 54.224 141.183 1.00 82.56 ? 42 LEU C CA 1 +ATOM 5026 C C . LEU C 1 45 ? 31.550 54.008 141.833 1.00 62.73 ? 42 LEU C C 1 +ATOM 5027 O O . LEU C 1 45 ? 30.625 53.517 141.187 1.00 80.76 ? 42 LEU C O 1 +ATOM 5028 C CB . LEU C 1 45 ? 32.844 55.343 140.146 1.00 64.47 ? 42 LEU C CB 1 +ATOM 5029 C CG . LEU C 1 45 ? 32.890 56.817 140.520 1.00 81.80 ? 42 LEU C CG 1 +ATOM 5030 C CD1 . LEU C 1 45 ? 34.198 57.158 141.174 1.00 118.17 ? 42 LEU C CD1 1 +ATOM 5031 C CD2 . LEU C 1 45 ? 32.711 57.632 139.264 1.00 76.84 ? 42 LEU C CD2 1 +ATOM 5032 N N . THR C 1 46 ? 31.424 54.348 143.114 1.00 81.75 ? 43 THR C N 1 +ATOM 5033 C CA . THR C 1 46 ? 30.130 54.277 143.804 1.00 90.78 ? 43 THR C CA 1 +ATOM 5034 C C . THR C 1 46 ? 29.864 55.598 144.506 1.00 71.82 ? 43 THR C C 1 +ATOM 5035 O O . THR C 1 46 ? 30.673 56.043 145.311 1.00 83.36 ? 43 THR C O 1 +ATOM 5036 C CB . THR C 1 46 ? 30.081 53.175 144.888 1.00 71.02 ? 43 THR C CB 1 +ATOM 5037 O OG1 . THR C 1 46 ? 30.936 53.541 145.970 1.00 125.75 ? 43 THR C OG1 1 +ATOM 5038 C CG2 . THR C 1 46 ? 30.513 51.819 144.345 1.00 87.88 ? 43 THR C CG2 1 +ATOM 5039 N N . LEU C 1 47 ? 28.729 56.221 144.216 1.00 74.86 ? 44 LEU C N 1 +ATOM 5040 C CA . LEU C 1 47 ? 28.438 57.542 144.759 1.00 72.69 ? 44 LEU C CA 1 +ATOM 5041 C C . LEU C 1 47 ? 26.967 57.681 145.115 1.00 78.14 ? 44 LEU C C 1 +ATOM 5042 O O . LEU C 1 47 ? 26.101 57.185 144.389 1.00 53.51 ? 44 LEU C O 1 +ATOM 5043 C CB . LEU C 1 47 ? 28.843 58.626 143.760 1.00 61.30 ? 44 LEU C CB 1 +ATOM 5044 C CG . LEU C 1 47 ? 30.348 58.877 143.613 1.00 91.01 ? 44 LEU C CG 1 +ATOM 5045 C CD1 . LEU C 1 47 ? 30.637 59.832 142.461 1.00 84.05 ? 44 LEU C CD1 1 +ATOM 5046 C CD2 . LEU C 1 47 ? 30.934 59.411 144.907 1.00 70.10 ? 44 LEU C CD2 1 +ATOM 5047 N N . LYS C 1 48 ? 26.695 58.330 146.251 1.00 63.94 ? 45 LYS C N 1 +ATOM 5048 C CA . LYS C 1 48 ? 25.323 58.675 146.646 1.00 57.70 ? 45 LYS C CA 1 +ATOM 5049 C C . LYS C 1 48 ? 25.101 60.181 146.733 1.00 86.78 ? 45 LYS C C 1 +ATOM 5050 O O . LYS C 1 48 ? 25.882 60.910 147.351 1.00 63.61 ? 45 LYS C O 1 +ATOM 5051 C CB . LYS C 1 48 ? 24.923 58.039 147.974 1.00 64.35 ? 45 LYS C CB 1 +ATOM 5052 C CG . LYS C 1 48 ? 23.426 58.061 148.217 1.00 59.74 ? 45 LYS C CG 1 +ATOM 5053 C CD . LYS C 1 48 ? 23.122 57.908 149.687 1.00 72.44 ? 45 LYS C CD 1 +ATOM 5054 C CE . LYS C 1 48 ? 21.678 57.538 149.913 1.00 93.09 ? 45 LYS C CE 1 +ATOM 5055 N NZ . LYS C 1 48 ? 21.372 57.586 151.353 1.00 64.04 ? 45 LYS C NZ 1 +ATOM 5056 N N . PHE C 1 49 ? 24.015 60.628 146.115 1.00 88.72 ? 46 PHE C N 1 +ATOM 5057 C CA . PHE C 1 49 ? 23.714 62.043 146.024 1.00 81.05 ? 46 PHE C CA 1 +ATOM 5058 C C . PHE C 1 49 ? 22.429 62.381 146.754 1.00 67.18 ? 46 PHE C C 1 +ATOM 5059 O O . PHE C 1 49 ? 21.402 61.749 146.556 1.00 71.11 ? 46 PHE C O 1 +ATOM 5060 C CB . PHE C 1 49 ? 23.666 62.472 144.557 1.00 81.03 ? 46 PHE C CB 1 +ATOM 5061 C CG . PHE C 1 49 ? 24.963 62.249 143.836 1.00 78.89 ? 46 PHE C CG 1 +ATOM 5062 C CD1 . PHE C 1 49 ? 26.014 63.134 143.995 1.00 76.65 ? 46 PHE C CD1 1 +ATOM 5063 C CD2 . PHE C 1 49 ? 25.147 61.149 143.031 1.00 71.23 ? 46 PHE C CD2 1 +ATOM 5064 C CE1 . PHE C 1 49 ? 27.212 62.937 143.357 1.00 70.20 ? 46 PHE C CE1 1 +ATOM 5065 C CE2 . PHE C 1 49 ? 26.348 60.955 142.390 1.00 80.09 ? 46 PHE C CE2 1 +ATOM 5066 C CZ . PHE C 1 49 ? 27.379 61.852 142.558 1.00 73.85 ? 46 PHE C CZ 1 +ATOM 5067 N N . ILE C 1 50 ? 22.526 63.362 147.640 1.00 88.11 ? 47 ILE C N 1 +ATOM 5068 C CA . ILE C 1 50 ? 21.373 63.919 148.320 1.00 70.43 ? 47 ILE C CA 1 +ATOM 5069 C C . ILE C 1 50 ? 21.089 65.304 147.729 1.00 98.32 ? 47 ILE C C 1 +ATOM 5070 O O . ILE C 1 50 ? 22.003 66.112 147.539 1.00 77.86 ? 47 ILE C O 1 +ATOM 5071 C CB . ILE C 1 50 ? 21.645 64.090 149.834 1.00 80.60 ? 47 ILE C CB 1 +ATOM 5072 C CG1 . ILE C 1 50 ? 22.182 62.799 150.459 1.00 96.30 ? 47 ILE C CG1 1 +ATOM 5073 C CG2 . ILE C 1 50 ? 20.388 64.531 150.559 1.00 107.24 ? 47 ILE C CG2 1 +ATOM 5074 C CD1 . ILE C 1 50 ? 21.112 61.769 150.752 1.00 104.15 ? 47 ILE C CD1 1 +ATOM 5075 N N . CYS C 1 51 ? 19.830 65.587 147.426 1.00 107.15 ? 48 CYS C N 1 +ATOM 5076 C CA . CYS C 1 51 ? 19.442 66.977 147.219 1.00 112.44 ? 48 CYS C CA 1 +ATOM 5077 C C . CYS C 1 51 ? 19.267 67.685 148.576 1.00 99.36 ? 48 CYS C C 1 +ATOM 5078 O O . CYS C 1 51 ? 18.357 67.347 149.345 1.00 105.21 ? 48 CYS C O 1 +ATOM 5079 C CB . CYS C 1 51 ? 18.158 67.072 146.403 1.00 128.13 ? 48 CYS C CB 1 +ATOM 5080 S SG . CYS C 1 51 ? 17.883 68.711 145.723 1.00 95.34 ? 48 CYS C SG 1 +ATOM 5081 N N . THR C 1 52 ? 20.139 68.658 148.863 1.00 92.57 ? 49 THR C N 1 +ATOM 5082 C CA . THR C 1 52 ? 20.124 69.381 150.142 1.00 87.04 ? 49 THR C CA 1 +ATOM 5083 C C . THR C 1 52 ? 19.089 70.512 150.177 1.00 83.30 ? 49 THR C C 1 +ATOM 5084 O O . THR C 1 52 ? 18.845 71.100 151.231 1.00 100.98 ? 49 THR C O 1 +ATOM 5085 C CB . THR C 1 52 ? 21.521 69.972 150.515 1.00 87.09 ? 49 THR C CB 1 +ATOM 5086 O OG1 . THR C 1 52 ? 22.128 70.562 149.361 1.00 78.32 ? 49 THR C OG1 1 +ATOM 5087 C CG2 . THR C 1 52 ? 22.455 68.912 151.056 1.00 70.89 ? 49 THR C CG2 1 +ATOM 5088 N N . THR C 1 53 ? 18.486 70.811 149.025 1.00 104.54 ? 50 THR C N 1 +ATOM 5089 C CA . THR C 1 53 ? 17.504 71.896 148.907 1.00 56.59 ? 50 THR C CA 1 +ATOM 5090 C C . THR C 1 53 ? 16.082 71.415 148.558 1.00 88.52 ? 50 THR C C 1 +ATOM 5091 O O . THR C 1 53 ? 15.352 72.108 147.860 1.00 124.44 ? 50 THR C O 1 +ATOM 5092 C CB . THR C 1 53 ? 17.936 72.951 147.840 1.00 82.24 ? 50 THR C CB 1 +ATOM 5093 O OG1 . THR C 1 53 ? 17.837 72.396 146.522 1.00 87.78 ? 50 THR C OG1 1 +ATOM 5094 C CG2 . THR C 1 53 ? 19.351 73.410 148.062 1.00 59.48 ? 50 THR C CG2 1 +ATOM 5095 N N . GLY C 1 54 ? 15.684 70.239 149.036 1.00 70.85 ? 51 GLY C N 1 +ATOM 5096 C CA . GLY C 1 54 ? 14.352 69.717 148.752 1.00 88.60 ? 51 GLY C CA 1 +ATOM 5097 C C . GLY C 1 54 ? 14.340 68.847 147.509 1.00 62.67 ? 51 GLY C C 1 +ATOM 5098 O O . GLY C 1 54 ? 15.274 68.078 147.309 1.00 154.08 ? 51 GLY C O 1 +ATOM 5099 N N . LYS C 1 55 ? 13.293 68.957 146.685 1.00 100.93 ? 52 LYS C N 1 +ATOM 5100 C CA . LYS C 1 55 ? 13.271 68.309 145.367 1.00 89.80 ? 52 LYS C CA 1 +ATOM 5101 C C . LYS C 1 55 ? 14.224 68.939 144.376 1.00 89.42 ? 52 LYS C C 1 +ATOM 5102 O O . LYS C 1 55 ? 14.575 70.113 144.481 1.00 80.42 ? 52 LYS C O 1 +ATOM 5103 C CB . LYS C 1 55 ? 11.877 68.318 144.762 1.00 54.70 ? 52 LYS C CB 1 +ATOM 5104 C CG . LYS C 1 55 ? 11.104 67.037 145.034 1.00 120.63 ? 52 LYS C CG 1 +ATOM 5105 C CD . LYS C 1 55 ? 9.842 66.918 144.179 1.00 166.90 ? 52 LYS C CD 1 +ATOM 5106 C CE . LYS C 1 55 ? 8.697 66.317 144.978 1.00 177.53 ? 52 LYS C CE 1 +ATOM 5107 N NZ . LYS C 1 55 ? 7.424 66.238 144.202 1.00 161.11 ? 52 LYS C NZ 1 +ATOM 5108 N N . LEU C 1 56 ? 14.619 68.134 143.397 1.00 103.77 ? 53 LEU C N 1 +ATOM 5109 C CA . LEU C 1 56 ? 15.515 68.580 142.349 1.00 90.37 ? 53 LEU C CA 1 +ATOM 5110 C C . LEU C 1 56 ? 14.682 69.213 141.224 1.00 74.28 ? 53 LEU C C 1 +ATOM 5111 O O . LEU C 1 56 ? 13.622 68.697 140.862 1.00 85.07 ? 53 LEU C O 1 +ATOM 5112 C CB . LEU C 1 56 ? 16.351 67.395 141.847 1.00 76.81 ? 53 LEU C CB 1 +ATOM 5113 C CG . LEU C 1 56 ? 17.676 67.698 141.142 1.00 90.97 ? 53 LEU C CG 1 +ATOM 5114 C CD1 . LEU C 1 56 ? 18.762 68.072 142.129 1.00 69.53 ? 53 LEU C CD1 1 +ATOM 5115 C CD2 . LEU C 1 56 ? 18.097 66.522 140.296 1.00 54.32 ? 53 LEU C CD2 1 +ATOM 5116 N N . PRO C 1 57 ? 15.138 70.357 140.688 1.00 97.14 ? 54 PRO C N 1 +ATOM 5117 C CA . PRO C 1 57 ? 14.372 70.991 139.605 1.00 76.59 ? 54 PRO C CA 1 +ATOM 5118 C C . PRO C 1 57 ? 14.536 70.288 138.253 1.00 92.95 ? 54 PRO C C 1 +ATOM 5119 O O . PRO C 1 57 ? 13.657 70.383 137.402 1.00 84.65 ? 54 PRO C O 1 +ATOM 5120 C CB . PRO C 1 57 ? 14.953 72.404 139.550 1.00 73.43 ? 54 PRO C CB 1 +ATOM 5121 C CG . PRO C 1 57 ? 16.329 72.267 140.071 1.00 82.28 ? 54 PRO C CG 1 +ATOM 5122 C CD . PRO C 1 57 ? 16.287 71.178 141.111 1.00 87.26 ? 54 PRO C CD 1 +ATOM 5123 N N . VAL C 1 58 ? 15.646 69.581 138.074 1.00 94.78 ? 55 VAL C N 1 +ATOM 5124 C CA . VAL C 1 58 ? 15.936 68.866 136.834 1.00 95.20 ? 55 VAL C CA 1 +ATOM 5125 C C . VAL C 1 58 ? 15.810 67.344 137.042 1.00 100.80 ? 55 VAL C C 1 +ATOM 5126 O O . VAL C 1 58 ? 15.680 66.896 138.178 1.00 78.43 ? 55 VAL C O 1 +ATOM 5127 C CB . VAL C 1 58 ? 17.331 69.258 136.350 1.00 78.19 ? 55 VAL C CB 1 +ATOM 5128 C CG1 . VAL C 1 58 ? 17.281 70.631 135.751 1.00 90.51 ? 55 VAL C CG1 1 +ATOM 5129 C CG2 . VAL C 1 58 ? 18.282 69.264 137.506 1.00 89.93 ? 55 VAL C CG2 1 +ATOM 5130 N N . PRO C 1 59 ? 15.813 66.537 135.958 1.00 96.80 ? 56 PRO C N 1 +ATOM 5131 C CA . PRO C 1 59 ? 15.776 65.103 136.257 1.00 98.00 ? 56 PRO C CA 1 +ATOM 5132 C C . PRO C 1 59 ? 17.162 64.679 136.699 1.00 108.15 ? 56 PRO C C 1 +ATOM 5133 O O . PRO C 1 59 ? 18.141 65.306 136.284 1.00 82.90 ? 56 PRO C O 1 +ATOM 5134 C CB . PRO C 1 59 ? 15.443 64.457 134.904 1.00 81.45 ? 56 PRO C CB 1 +ATOM 5135 C CG . PRO C 1 59 ? 15.358 65.553 133.928 1.00 81.71 ? 56 PRO C CG 1 +ATOM 5136 C CD . PRO C 1 59 ? 15.975 66.771 134.517 1.00 89.99 ? 56 PRO C CD 1 +ATOM 5137 N N . TRP C 1 60 ? 17.259 63.659 137.541 1.00 92.94 ? 57 TRP C N 1 +ATOM 5138 C CA . TRP C 1 60 ? 18.574 63.204 137.974 1.00 61.46 ? 57 TRP C CA 1 +ATOM 5139 C C . TRP C 1 60 ? 19.534 62.865 136.820 1.00 72.34 ? 57 TRP C C 1 +ATOM 5140 O O . TRP C 1 60 ? 20.678 63.319 136.838 1.00 61.22 ? 57 TRP C O 1 +ATOM 5141 C CB . TRP C 1 60 ? 18.464 62.056 138.977 1.00 75.19 ? 57 TRP C CB 1 +ATOM 5142 C CG . TRP C 1 60 ? 18.145 62.509 140.361 1.00 87.93 ? 57 TRP C CG 1 +ATOM 5143 C CD1 . TRP C 1 60 ? 16.961 62.364 141.029 1.00 66.04 ? 57 TRP C CD1 1 +ATOM 5144 C CD2 . TRP C 1 60 ? 19.030 63.185 141.252 1.00 83.72 ? 57 TRP C CD2 1 +ATOM 5145 N NE1 . TRP C 1 60 ? 17.060 62.910 142.286 1.00 70.52 ? 57 TRP C NE1 1 +ATOM 5146 C CE2 . TRP C 1 60 ? 18.323 63.417 142.447 1.00 71.86 ? 57 TRP C CE2 1 +ATOM 5147 C CE3 . TRP C 1 60 ? 20.358 63.615 141.155 1.00 77.56 ? 57 TRP C CE3 1 +ATOM 5148 C CZ2 . TRP C 1 60 ? 18.895 64.060 143.533 1.00 67.99 ? 57 TRP C CZ2 1 +ATOM 5149 C CZ3 . TRP C 1 60 ? 20.924 64.249 142.232 1.00 78.79 ? 57 TRP C CZ3 1 +ATOM 5150 C CH2 . TRP C 1 60 ? 20.195 64.469 143.407 1.00 76.81 ? 57 TRP C CH2 1 +ATOM 5151 N N . PRO C 1 61 ? 19.069 62.096 135.806 1.00 89.05 ? 58 PRO C N 1 +ATOM 5152 C CA . PRO C 1 61 ? 19.944 61.683 134.697 1.00 51.21 ? 58 PRO C CA 1 +ATOM 5153 C C . PRO C 1 61 ? 20.758 62.794 134.022 1.00 71.00 ? 58 PRO C C 1 +ATOM 5154 O O . PRO C 1 61 ? 21.877 62.544 133.571 1.00 85.75 ? 58 PRO C O 1 +ATOM 5155 C CB . PRO C 1 61 ? 18.954 61.087 133.704 1.00 81.41 ? 58 PRO C CB 1 +ATOM 5156 C CG . PRO C 1 61 ? 17.926 60.483 134.570 1.00 78.84 ? 58 PRO C CG 1 +ATOM 5157 C CD . PRO C 1 61 ? 17.745 61.449 135.689 1.00 64.80 ? 58 PRO C CD 1 +ATOM 5158 N N . THR C 1 62 ? 20.214 64.002 133.971 1.00 82.97 ? 59 THR C N 1 +ATOM 5159 C CA . THR C 1 62 ? 20.903 65.136 133.359 1.00 89.50 ? 59 THR C CA 1 +ATOM 5160 C C . THR C 1 62 ? 22.194 65.523 134.073 1.00 88.73 ? 59 THR C C 1 +ATOM 5161 O O . THR C 1 62 ? 23.015 66.279 133.543 1.00 82.33 ? 59 THR C O 1 +ATOM 5162 C CB . THR C 1 62 ? 20.001 66.356 133.373 1.00 93.19 ? 59 THR C CB 1 +ATOM 5163 O OG1 . THR C 1 62 ? 19.522 66.567 134.707 1.00 85.21 ? 59 THR C OG1 1 +ATOM 5164 C CG2 . THR C 1 62 ? 18.830 66.126 132.457 1.00 79.10 ? 59 THR C CG2 1 +ATOM 5165 N N . LEU C 1 63 ? 22.369 65.005 135.279 1.00 81.90 ? 60 LEU C N 1 +ATOM 5166 C CA . LEU C 1 63 ? 23.450 65.466 136.130 1.00 61.33 ? 60 LEU C CA 1 +ATOM 5167 C C . LEU C 1 63 ? 24.585 64.463 136.292 1.00 95.91 ? 60 LEU C C 1 +ATOM 5168 O O . LEU C 1 63 ? 25.655 64.822 136.790 1.00 68.07 ? 60 LEU C O 1 +ATOM 5169 C CB . LEU C 1 63 ? 22.901 65.871 137.497 1.00 80.75 ? 60 LEU C CB 1 +ATOM 5170 C CG . LEU C 1 63 ? 22.120 67.179 137.555 1.00 91.72 ? 60 LEU C CG 1 +ATOM 5171 C CD1 . LEU C 1 63 ? 21.661 67.423 138.981 1.00 81.74 ? 60 LEU C CD1 1 +ATOM 5172 C CD2 . LEU C 1 63 ? 22.995 68.313 137.061 1.00 63.65 ? 60 LEU C CD2 1 +ATOM 5173 N N . VAL C 1 64 ? 24.351 63.224 135.858 1.00 85.25 ? 61 VAL C N 1 +ATOM 5174 C CA . VAL C 1 64 ? 25.321 62.138 136.005 1.00 67.70 ? 61 VAL C CA 1 +ATOM 5175 C C . VAL C 1 64 ? 26.724 62.540 135.575 1.00 70.43 ? 61 VAL C C 1 +ATOM 5176 O O . VAL C 1 64 ? 27.688 62.325 136.298 1.00 74.25 ? 61 VAL C O 1 +ATOM 5177 C CB . VAL C 1 64 ? 24.896 60.878 135.216 1.00 72.79 ? 61 VAL C CB 1 +ATOM 5178 C CG1 . VAL C 1 64 ? 26.033 59.870 135.157 1.00 46.13 ? 61 VAL C CG1 1 +ATOM 5179 C CG2 . VAL C 1 64 ? 23.660 60.256 135.841 1.00 57.92 ? 61 VAL C CG2 1 +ATOM 5180 N N . THR C 1 65 ? 26.840 63.155 134.410 1.00 83.66 ? 62 THR C N 1 +ATOM 5181 C CA . THR C 1 65 ? 28.156 63.412 133.853 1.00 82.63 ? 62 THR C CA 1 +ATOM 5182 C C . THR C 1 65 ? 28.838 64.556 134.568 1.00 69.88 ? 62 THR C C 1 +ATOM 5183 O O . THR C 1 65 ? 30.057 64.700 134.515 1.00 95.72 ? 62 THR C O 1 +ATOM 5184 C CB . THR C 1 65 ? 28.050 63.779 132.389 1.00 90.86 ? 62 THR C CB 1 +ATOM 5185 O OG1 . THR C 1 65 ? 27.683 65.158 132.279 1.00 114.07 ? 62 THR C OG1 1 +ATOM 5186 C CG2 . THR C 1 65 ? 26.994 62.938 131.727 1.00 79.32 ? 62 THR C CG2 1 +ATOM 5187 N N . THR C 1 66 ? 28.040 65.382 135.226 1.00 87.87 ? 63 THR C N 1 +ATOM 5188 C CA . THR C 1 66 ? 28.565 66.582 135.844 1.00 86.32 ? 63 THR C CA 1 +ATOM 5189 C C . THR C 1 66 ? 29.173 66.140 137.148 1.00 87.84 ? 63 THR C C 1 +ATOM 5190 O O . THR C 1 66 ? 30.272 66.587 137.534 1.00 80.58 ? 63 THR C O 1 +ATOM 5191 C CB . THR C 1 66 ? 27.439 67.611 136.097 1.00 89.43 ? 63 THR C CB 1 +ATOM 5192 O OG1 . THR C 1 66 ? 26.579 67.693 134.945 1.00 82.11 ? 63 THR C OG1 1 +ATOM 5193 C CG2 . THR C 1 66 ? 28.021 68.986 136.432 1.00 69.28 ? 63 THR C CG2 1 +ATOM 5194 N N . PHE C 1 67 ? 28.424 65.218 137.770 1.00 97.99 ? 64 PHE C N 1 +ATOM 5195 C CA . PHE C 1 67 ? 28.750 64.591 139.063 1.00 85.74 ? 64 PHE C CA 1 +ATOM 5196 C C . PHE C 1 67 ? 29.924 63.538 139.057 1.00 74.91 ? 64 PHE C C 1 +ATOM 5197 O O . PHE C 1 67 ? 31.022 63.747 139.742 1.00 92.00 ? 64 PHE C O 1 +ATOM 5198 C CB . PHE C 1 67 ? 27.584 63.804 139.693 1.00 90.56 ? 64 PHE C CB 1 +ATOM 5199 C CG . PHE C 1 67 ? 26.422 64.602 140.193 1.00 65.29 ? 64 PHE C CG 1 +ATOM 5200 C CD1 . PHE C 1 67 ? 26.546 65.878 140.706 1.00 71.30 ? 64 PHE C CD1 1 +ATOM 5201 C CD2 . PHE C 1 67 ? 25.168 64.003 140.177 1.00 85.10 ? 64 PHE C CD2 1 +ATOM 5202 C CE1 . PHE C 1 67 ? 25.425 66.546 141.163 1.00 76.17 ? 64 PHE C CE1 1 +ATOM 5203 C CE2 . PHE C 1 67 ? 24.050 64.666 140.627 1.00 82.01 ? 64 PHE C CE2 1 +ATOM 5204 C CZ . PHE C 1 67 ? 24.174 65.936 141.118 1.00 75.04 ? 64 PHE C CZ 1 +HETATM 5205 N N1 . CR2 C 1 68 ? 29.716 62.436 138.344 1.00 90.29 ? 65 CR2 C N1 1 +HETATM 5206 C CA1 . CR2 C 1 68 ? 30.905 61.567 137.782 1.00 89.06 ? 65 CR2 C CA1 1 +HETATM 5207 C C1 . CR2 C 1 68 ? 31.437 61.903 136.362 1.00 97.53 ? 65 CR2 C C1 1 +HETATM 5208 N N2 . CR2 C 1 68 ? 31.085 61.309 135.179 1.00 100.27 ? 65 CR2 C N2 1 +HETATM 5209 N N3 . CR2 C 1 68 ? 32.329 62.878 136.118 1.00 72.28 ? 65 CR2 C N3 1 +HETATM 5210 C C2 . CR2 C 1 68 ? 32.550 62.978 134.841 1.00 85.68 ? 65 CR2 C C2 1 +HETATM 5211 O O2 . CR2 C 1 68 ? 33.326 63.814 134.245 1.00 76.15 ? 65 CR2 C O2 1 +HETATM 5212 C CA2 . CR2 C 1 68 ? 31.741 61.958 134.203 1.00 91.84 ? 65 CR2 C CA2 1 +HETATM 5213 C CA3 . CR2 C 1 68 ? 32.849 63.833 137.046 1.00 47.59 ? 65 CR2 C CA3 1 +HETATM 5214 C C3 . CR2 C 1 68 ? 34.125 63.432 137.746 1.00 90.12 ? 65 CR2 C C3 1 +HETATM 5215 O O3 . CR2 C 1 68 ? 35.163 64.389 137.737 1.00 77.21 ? 65 CR2 C O3 1 +HETATM 5216 C CB2 . CR2 C 1 68 ? 31.607 61.596 132.772 1.00 83.28 ? 65 CR2 C CB2 1 +HETATM 5217 C CG2 . CR2 C 1 68 ? 30.716 60.533 132.220 1.00 96.77 ? 65 CR2 C CG2 1 +HETATM 5218 C CD1 . CR2 C 1 68 ? 29.814 59.810 132.994 1.00 70.02 ? 65 CR2 C CD1 1 +HETATM 5219 C CD2 . CR2 C 1 68 ? 30.712 60.335 130.847 1.00 90.15 ? 65 CR2 C CD2 1 +HETATM 5220 C CE1 . CR2 C 1 68 ? 28.983 58.864 132.406 1.00 95.88 ? 65 CR2 C CE1 1 +HETATM 5221 C CE2 . CR2 C 1 68 ? 29.884 59.392 130.261 1.00 75.90 ? 65 CR2 C CE2 1 +HETATM 5222 C CZ . CR2 C 1 68 ? 29.013 58.649 131.034 1.00 93.36 ? 65 CR2 C CZ 1 +HETATM 5223 O OH . CR2 C 1 68 ? 28.205 57.706 130.425 1.00 90.87 ? 65 CR2 C OH 1 +ATOM 5224 N N . VAL C 1 69 ? 34.347 62.122 137.851 1.00 105.80 ? 68 VAL C N 1 +ATOM 5225 C CA . VAL C 1 69 ? 35.595 61.808 138.488 1.00 94.05 ? 68 VAL C CA 1 +ATOM 5226 C C . VAL C 1 69 ? 36.551 61.002 137.717 1.00 63.66 ? 68 VAL C C 1 +ATOM 5227 O O . VAL C 1 69 ? 37.279 60.201 138.260 1.00 107.83 ? 68 VAL C O 1 +ATOM 5228 C CB . VAL C 1 69 ? 35.731 61.772 140.048 1.00 74.54 ? 68 VAL C CB 1 +ATOM 5229 C CG1 . VAL C 1 69 ? 35.503 63.156 140.587 1.00 74.33 ? 68 VAL C CG1 1 +ATOM 5230 C CG2 . VAL C 1 69 ? 34.894 60.749 140.765 1.00 128.85 ? 68 VAL C CG2 1 +ATOM 5231 N N . GLN C 1 70 ? 36.624 61.340 136.438 1.00 96.71 ? 69 GLN C N 1 +ATOM 5232 C CA . GLN C 1 70 ? 37.380 60.576 135.451 1.00 93.11 ? 69 GLN C CA 1 +ATOM 5233 C C . GLN C 1 70 ? 38.841 60.232 135.773 1.00 82.43 ? 69 GLN C C 1 +ATOM 5234 O O . GLN C 1 70 ? 39.569 59.767 134.906 1.00 119.79 ? 69 GLN C O 1 +ATOM 5235 C CB . GLN C 1 70 ? 37.302 61.278 134.101 1.00 86.15 ? 69 GLN C CB 1 +ATOM 5236 C CG . GLN C 1 70 ? 35.926 61.224 133.461 1.00 112.76 ? 69 GLN C CG 1 +ATOM 5237 C CD . GLN C 1 70 ? 35.799 62.171 132.284 1.00 114.28 ? 69 GLN C CD 1 +ATOM 5238 O OE1 . GLN C 1 70 ? 36.642 63.050 132.085 1.00 104.25 ? 69 GLN C OE1 1 +ATOM 5239 N NE2 . GLN C 1 70 ? 34.745 61.996 131.496 1.00 112.98 ? 69 GLN C NE2 1 +ATOM 5240 N N . CYS C 1 71 ? 39.253 60.447 137.015 1.00 96.49 ? 70 CYS C N 1 +ATOM 5241 C CA . CYS C 1 71 ? 40.564 60.040 137.494 1.00 86.38 ? 70 CYS C CA 1 +ATOM 5242 C C . CYS C 1 71 ? 40.484 58.664 138.164 1.00 96.64 ? 70 CYS C C 1 +ATOM 5243 O O . CYS C 1 71 ? 41.465 58.172 138.720 1.00 86.21 ? 70 CYS C O 1 +ATOM 5244 C CB . CYS C 1 71 ? 41.099 61.087 138.476 1.00 79.40 ? 70 CYS C CB 1 +ATOM 5245 S SG . CYS C 1 71 ? 39.926 61.618 139.761 1.00 102.81 ? 70 CYS C SG 1 +ATOM 5246 N N . PHE C 1 72 ? 39.299 58.061 138.115 1.00 82.72 ? 71 PHE C N 1 +ATOM 5247 C CA . PHE C 1 72 ? 39.086 56.718 138.643 1.00 75.89 ? 71 PHE C CA 1 +ATOM 5248 C C . PHE C 1 72 ? 38.904 55.715 137.514 1.00 70.52 ? 71 PHE C C 1 +ATOM 5249 O O . PHE C 1 72 ? 38.522 54.575 137.738 1.00 117.76 ? 71 PHE C O 1 +ATOM 5250 C CB . PHE C 1 72 ? 37.899 56.693 139.611 1.00 84.40 ? 71 PHE C CB 1 +ATOM 5251 C CG . PHE C 1 72 ? 38.199 57.338 140.924 1.00 79.69 ? 71 PHE C CG 1 +ATOM 5252 C CD1 . PHE C 1 72 ? 38.931 56.667 141.884 1.00 86.80 ? 71 PHE C CD1 1 +ATOM 5253 C CD2 . PHE C 1 72 ? 37.783 58.626 141.190 1.00 91.09 ? 71 PHE C CD2 1 +ATOM 5254 C CE1 . PHE C 1 72 ? 39.232 57.262 143.086 1.00 73.20 ? 71 PHE C CE1 1 +ATOM 5255 C CE2 . PHE C 1 72 ? 38.084 59.227 142.393 1.00 74.75 ? 71 PHE C CE2 1 +ATOM 5256 C CZ . PHE C 1 72 ? 38.806 58.541 143.343 1.00 103.56 ? 71 PHE C CZ 1 +ATOM 5257 N N . SER C 1 73 ? 39.188 56.149 136.296 1.00 77.72 ? 72 SER C N 1 +ATOM 5258 C CA . SER C 1 73 ? 39.252 55.240 135.165 1.00 100.66 ? 72 SER C CA 1 +ATOM 5259 C C . SER C 1 73 ? 40.403 54.249 135.325 1.00 90.98 ? 72 SER C C 1 +ATOM 5260 O O . SER C 1 73 ? 41.470 54.584 135.842 1.00 127.16 ? 72 SER C O 1 +ATOM 5261 C CB . SER C 1 73 ? 39.419 56.026 133.874 1.00 91.13 ? 72 SER C CB 1 +ATOM 5262 N N . ARG C 1 74 ? 40.180 53.024 134.870 1.00 78.44 ? 73 ARG C N 1 +ATOM 5263 C CA . ARG C 1 74 ? 41.243 52.034 134.802 1.00 92.17 ? 73 ARG C CA 1 +ATOM 5264 C C . ARG C 1 74 ? 42.018 52.225 133.498 1.00 90.38 ? 73 ARG C C 1 +ATOM 5265 O O . ARG C 1 74 ? 41.460 52.080 132.404 1.00 84.94 ? 73 ARG C O 1 +ATOM 5266 C CB . ARG C 1 74 ? 40.647 50.625 134.873 1.00 83.82 ? 73 ARG C CB 1 +ATOM 5267 C CG . ARG C 1 74 ? 41.663 49.500 134.968 1.00 82.31 ? 73 ARG C CG 1 +ATOM 5268 C CD . ARG C 1 74 ? 41.001 48.154 135.249 1.00 76.20 ? 73 ARG C CD 1 +ATOM 5269 N NE . ARG C 1 74 ? 40.204 47.623 134.141 1.00 79.05 ? 73 ARG C NE 1 +ATOM 5270 C CZ . ARG C 1 74 ? 40.687 47.296 132.942 1.00 108.64 ? 73 ARG C CZ 1 +ATOM 5271 N NH1 . ARG C 1 74 ? 41.981 47.471 132.658 1.00 48.65 ? 73 ARG C NH1 1 +ATOM 5272 N NH2 . ARG C 1 74 ? 39.866 46.804 132.015 1.00 75.32 ? 73 ARG C NH2 1 +ATOM 5273 N N . TYR C 1 75 ? 43.296 52.573 133.620 1.00 93.15 ? 74 TYR C N 1 +ATOM 5274 C CA . TYR C 1 75 ? 44.189 52.657 132.465 1.00 104.24 ? 74 TYR C CA 1 +ATOM 5275 C C . TYR C 1 75 ? 45.000 51.358 132.334 1.00 99.26 ? 74 TYR C C 1 +ATOM 5276 O O . TYR C 1 75 ? 45.773 51.018 133.230 1.00 125.47 ? 74 TYR C O 1 +ATOM 5277 C CB . TYR C 1 75 ? 45.110 53.893 132.573 1.00 77.87 ? 74 TYR C CB 1 +ATOM 5278 C CG . TYR C 1 75 ? 44.526 55.160 131.966 1.00 89.40 ? 74 TYR C CG 1 +ATOM 5279 C CD1 . TYR C 1 75 ? 43.496 55.854 132.595 1.00 99.01 ? 74 TYR C CD1 1 +ATOM 5280 C CD2 . TYR C 1 75 ? 44.999 55.657 130.760 1.00 102.86 ? 74 TYR C CD2 1 +ATOM 5281 C CE1 . TYR C 1 75 ? 42.951 57.003 132.035 1.00 93.93 ? 74 TYR C CE1 1 +ATOM 5282 C CE2 . TYR C 1 75 ? 44.463 56.803 130.195 1.00 90.26 ? 74 TYR C CE2 1 +ATOM 5283 C CZ . TYR C 1 75 ? 43.440 57.472 130.835 1.00 101.11 ? 74 TYR C CZ 1 +ATOM 5284 O OH . TYR C 1 75 ? 42.912 58.611 130.267 1.00 101.44 ? 74 TYR C OH 1 +ATOM 5285 N N . PRO C 1 76 ? 44.805 50.614 131.229 1.00 87.87 ? 75 PRO C N 1 +ATOM 5286 C CA . PRO C 1 76 ? 45.606 49.409 130.983 1.00 80.73 ? 75 PRO C CA 1 +ATOM 5287 C C . PRO C 1 76 ? 47.087 49.769 131.021 1.00 125.11 ? 75 PRO C C 1 +ATOM 5288 O O . PRO C 1 76 ? 47.427 50.912 130.715 1.00 110.69 ? 75 PRO C O 1 +ATOM 5289 C CB . PRO C 1 76 ? 45.201 49.000 129.562 1.00 96.77 ? 75 PRO C CB 1 +ATOM 5290 C CG . PRO C 1 76 ? 43.867 49.591 129.351 1.00 97.55 ? 75 PRO C CG 1 +ATOM 5291 C CD . PRO C 1 76 ? 43.839 50.866 130.146 1.00 108.42 ? 75 PRO C CD 1 +ATOM 5292 N N . ASP C 1 77 ? 47.940 48.821 131.399 1.00 120.93 ? 76 ASP C N 1 +ATOM 5293 C CA . ASP C 1 77 ? 49.361 49.096 131.628 1.00 129.39 ? 76 ASP C CA 1 +ATOM 5294 C C . ASP C 1 77 ? 50.025 49.853 130.487 1.00 137.13 ? 76 ASP C C 1 +ATOM 5295 O O . ASP C 1 77 ? 50.734 50.842 130.708 1.00 91.58 ? 76 ASP C O 1 +ATOM 5296 C CB . ASP C 1 77 ? 50.119 47.796 131.884 1.00 156.89 ? 76 ASP C CB 1 +ATOM 5297 C CG . ASP C 1 77 ? 49.948 47.295 133.297 1.00 171.18 ? 76 ASP C CG 1 +ATOM 5298 O OD1 . ASP C 1 77 ? 50.092 48.107 134.238 1.00 155.54 ? 76 ASP C OD1 1 +ATOM 5299 O OD2 . ASP C 1 77 ? 49.662 46.091 133.462 1.00 178.85 ? 76 ASP C OD2 1 +ATOM 5300 N N . HIS C 1 78 ? 49.774 49.391 129.267 1.00 133.58 ? 77 HIS C N 1 +ATOM 5301 C CA . HIS C 1 78 ? 50.375 49.990 128.084 1.00 87.73 ? 77 HIS C CA 1 +ATOM 5302 C C . HIS C 1 78 ? 49.935 51.437 127.837 1.00 123.03 ? 77 HIS C C 1 +ATOM 5303 O O . HIS C 1 78 ? 50.513 52.130 126.997 1.00 132.50 ? 77 HIS C O 1 +ATOM 5304 C CB . HIS C 1 78 ? 50.146 49.111 126.846 1.00 85.77 ? 77 HIS C CB 1 +ATOM 5305 C CG . HIS C 1 78 ? 48.714 48.999 126.412 1.00 102.13 ? 77 HIS C CG 1 +ATOM 5306 N ND1 . HIS C 1 78 ? 47.835 48.092 126.962 1.00 100.92 ? 77 HIS C ND1 1 +ATOM 5307 C CD2 . HIS C 1 78 ? 48.028 49.642 125.436 1.00 109.36 ? 77 HIS C CD2 1 +ATOM 5308 C CE1 . HIS C 1 78 ? 46.661 48.200 126.364 1.00 118.54 ? 77 HIS C CE1 1 +ATOM 5309 N NE2 . HIS C 1 78 ? 46.751 49.134 125.434 1.00 125.18 ? 77 HIS C NE2 1 +ATOM 5310 N N . MET C 1 79 ? 48.935 51.891 128.589 1.00 118.73 ? 78 MET C N 1 +ATOM 5311 C CA . MET C 1 79 ? 48.373 53.227 128.410 1.00 92.21 ? 78 MET C CA 1 +ATOM 5312 C C . MET C 1 79 ? 48.758 54.216 129.526 1.00 112.56 ? 78 MET C C 1 +ATOM 5313 O O . MET C 1 79 ? 48.803 55.426 129.296 1.00 92.78 ? 78 MET C O 1 +ATOM 5314 C CB . MET C 1 79 ? 46.845 53.145 128.254 1.00 82.97 ? 78 MET C CB 1 +ATOM 5315 C CG . MET C 1 79 ? 46.388 52.468 126.962 1.00 107.14 ? 78 MET C CG 1 +ATOM 5316 S SD . MET C 1 79 ? 44.615 52.541 126.604 1.00 99.67 ? 78 MET C SD 1 +ATOM 5317 C CE . MET C 1 79 ? 44.327 54.300 126.641 1.00 81.29 ? 78 MET C CE 1 +ATOM 5318 N N . LYS C 1 80 ? 49.072 53.701 130.713 1.00 89.88 ? 79 LYS C N 1 +ATOM 5319 C CA . LYS C 1 80 ? 49.247 54.520 131.926 1.00 103.56 ? 79 LYS C CA 1 +ATOM 5320 C C . LYS C 1 80 ? 50.115 55.783 131.844 1.00 110.85 ? 79 LYS C C 1 +ATOM 5321 O O . LYS C 1 80 ? 50.325 56.447 132.859 1.00 128.39 ? 79 LYS C O 1 +ATOM 5322 C CB . LYS C 1 80 ? 49.749 53.655 133.084 1.00 77.38 ? 79 LYS C CB 1 +ATOM 5323 C CG . LYS C 1 80 ? 48.755 52.612 133.544 1.00 119.62 ? 79 LYS C CG 1 +ATOM 5324 C CD . LYS C 1 80 ? 49.185 51.979 134.853 1.00 83.86 ? 79 LYS C CD 1 +ATOM 5325 C CE . LYS C 1 80 ? 48.166 50.957 135.326 1.00 94.85 ? 79 LYS C CE 1 +ATOM 5326 N NZ . LYS C 1 80 ? 46.873 51.601 135.687 1.00 117.38 ? 79 LYS C NZ 1 +ATOM 5327 N N . GLN C 1 81 ? 50.620 56.111 130.659 1.00 128.36 ? 80 GLN C N 1 +ATOM 5328 C CA . GLN C 1 81 ? 51.396 57.333 130.482 1.00 127.17 ? 80 GLN C CA 1 +ATOM 5329 C C . GLN C 1 81 ? 50.551 58.412 129.809 1.00 122.24 ? 80 GLN C C 1 +ATOM 5330 O O . GLN C 1 81 ? 50.970 59.561 129.699 1.00 144.76 ? 80 GLN C O 1 +ATOM 5331 C CB . GLN C 1 81 ? 52.688 57.067 129.694 1.00 106.94 ? 80 GLN C CB 1 +ATOM 5332 C CG . GLN C 1 81 ? 52.490 56.644 128.232 1.00 112.32 ? 80 GLN C CG 1 +ATOM 5333 C CD . GLN C 1 81 ? 52.188 55.157 128.068 1.00 143.83 ? 80 GLN C CD 1 +ATOM 5334 O OE1 . GLN C 1 81 ? 52.204 54.398 129.038 1.00 163.48 ? 80 GLN C OE1 1 +ATOM 5335 N NE2 . GLN C 1 81 ? 51.909 54.738 126.833 1.00 118.19 ? 80 GLN C NE2 1 +ATOM 5336 N N . HIS C 1 82 ? 49.355 58.035 129.367 1.00 93.71 ? 81 HIS C N 1 +ATOM 5337 C CA . HIS C 1 82 ? 48.418 58.987 128.772 1.00 125.53 ? 81 HIS C CA 1 +ATOM 5338 C C . HIS C 1 82 ? 47.298 59.331 129.753 1.00 129.09 ? 81 HIS C C 1 +ATOM 5339 O O . HIS C 1 82 ? 46.278 59.926 129.393 1.00 114.36 ? 81 HIS C O 1 +ATOM 5340 C CB . HIS C 1 82 ? 47.843 58.433 127.471 1.00 118.58 ? 81 HIS C CB 1 +ATOM 5341 C CG . HIS C 1 82 ? 48.882 58.103 126.444 1.00 122.53 ? 81 HIS C CG 1 +ATOM 5342 N ND1 . HIS C 1 82 ? 49.539 59.068 125.712 1.00 125.63 ? 81 HIS C ND1 1 +ATOM 5343 C CD2 . HIS C 1 82 ? 49.371 56.914 126.023 1.00 89.25 ? 81 HIS C CD2 1 +ATOM 5344 C CE1 . HIS C 1 82 ? 50.390 58.487 124.884 1.00 133.21 ? 81 HIS C CE1 1 +ATOM 5345 N NE2 . HIS C 1 82 ? 50.308 57.180 125.054 1.00 130.62 ? 81 HIS C NE2 1 +ATOM 5346 N N . ASP C 1 83 ? 47.511 58.945 131.003 1.00 109.44 ? 82 ASP C N 1 +ATOM 5347 C CA . ASP C 1 83 ? 46.593 59.243 132.083 1.00 109.15 ? 82 ASP C CA 1 +ATOM 5348 C C . ASP C 1 83 ? 46.858 60.655 132.576 1.00 104.27 ? 82 ASP C C 1 +ATOM 5349 O O . ASP C 1 83 ? 47.737 60.872 133.408 1.00 119.78 ? 82 ASP C O 1 +ATOM 5350 C CB . ASP C 1 83 ? 46.819 58.253 133.221 1.00 145.89 ? 82 ASP C CB 1 +ATOM 5351 C CG . ASP C 1 83 ? 45.681 58.230 134.217 1.00 139.02 ? 82 ASP C CG 1 +ATOM 5352 O OD1 . ASP C 1 83 ? 45.097 59.297 134.501 1.00 116.28 ? 82 ASP C OD1 1 +ATOM 5353 O OD2 . ASP C 1 83 ? 45.374 57.131 134.722 1.00 158.42 ? 82 ASP C OD2 1 +ATOM 5354 N N . PHE C 1 84 ? 46.091 61.608 132.057 1.00 102.94 ? 83 PHE C N 1 +ATOM 5355 C CA . PHE C 1 84 ? 46.210 63.006 132.450 1.00 97.00 ? 83 PHE C CA 1 +ATOM 5356 C C . PHE C 1 84 ? 45.674 63.264 133.848 1.00 97.94 ? 83 PHE C C 1 +ATOM 5357 O O . PHE C 1 84 ? 46.348 63.859 134.690 1.00 125.07 ? 83 PHE C O 1 +ATOM 5358 C CB . PHE C 1 84 ? 45.437 63.894 131.482 1.00 102.98 ? 83 PHE C CB 1 +ATOM 5359 C CG . PHE C 1 84 ? 45.240 65.287 131.988 1.00 110.53 ? 83 PHE C CG 1 +ATOM 5360 C CD1 . PHE C 1 84 ? 46.335 66.111 132.212 1.00 127.13 ? 83 PHE C CD1 1 +ATOM 5361 C CD2 . PHE C 1 84 ? 43.971 65.772 132.258 1.00 107.88 ? 83 PHE C CD2 1 +ATOM 5362 C CE1 . PHE C 1 84 ? 46.170 67.396 132.690 1.00 120.65 ? 83 PHE C CE1 1 +ATOM 5363 C CE2 . PHE C 1 84 ? 43.799 67.060 132.736 1.00 127.28 ? 83 PHE C CE2 1 +ATOM 5364 C CZ . PHE C 1 84 ? 44.901 67.873 132.951 1.00 125.34 ? 83 PHE C CZ 1 +ATOM 5365 N N . PHE C 1 85 ? 44.443 62.818 134.067 1.00 111.14 ? 84 PHE C N 1 +ATOM 5366 C CA . PHE C 1 85 ? 43.709 63.074 135.299 1.00 105.75 ? 84 PHE C CA 1 +ATOM 5367 C C . PHE C 1 85 ? 44.494 62.736 136.561 1.00 103.19 ? 84 PHE C C 1 +ATOM 5368 O O . PHE C 1 85 ? 44.648 63.581 137.438 1.00 125.70 ? 84 PHE C O 1 +ATOM 5369 C CB . PHE C 1 85 ? 42.386 62.314 135.280 1.00 101.49 ? 84 PHE C CB 1 +ATOM 5370 C CG . PHE C 1 85 ? 41.594 62.517 134.024 1.00 100.06 ? 84 PHE C CG 1 +ATOM 5371 C CD1 . PHE C 1 85 ? 40.833 63.651 133.844 1.00 104.16 ? 84 PHE C CD1 1 +ATOM 5372 C CD2 . PHE C 1 85 ? 41.610 61.569 133.024 1.00 103.92 ? 84 PHE C CD2 1 +ATOM 5373 C CE1 . PHE C 1 85 ? 40.104 63.831 132.696 1.00 99.53 ? 84 PHE C CE1 1 +ATOM 5374 C CE2 . PHE C 1 85 ? 40.881 61.746 131.876 1.00 76.49 ? 84 PHE C CE2 1 +ATOM 5375 C CZ . PHE C 1 85 ? 40.127 62.878 131.713 1.00 94.57 ? 84 PHE C CZ 1 +ATOM 5376 N N . LYS C 1 86 ? 45.000 61.514 136.656 1.00 105.07 ? 85 LYS C N 1 +ATOM 5377 C CA . LYS C 1 86 ? 45.753 61.137 137.845 1.00 122.08 ? 85 LYS C CA 1 +ATOM 5378 C C . LYS C 1 86 ? 47.052 61.944 137.979 1.00 125.86 ? 85 LYS C C 1 +ATOM 5379 O O . LYS C 1 86 ? 47.457 62.299 139.087 1.00 116.72 ? 85 LYS C O 1 +ATOM 5380 C CB . LYS C 1 86 ? 46.043 59.635 137.857 1.00 106.83 ? 85 LYS C CB 1 +ATOM 5381 C CG . LYS C 1 86 ? 44.814 58.758 137.935 1.00 86.45 ? 85 LYS C CG 1 +ATOM 5382 C CD . LYS C 1 86 ? 45.220 57.299 138.011 1.00 92.90 ? 85 LYS C CD 1 +ATOM 5383 C CE . LYS C 1 86 ? 44.018 56.374 138.055 1.00 69.89 ? 85 LYS C CE 1 +ATOM 5384 N NZ . LYS C 1 86 ? 43.199 56.425 136.810 1.00 113.89 ? 85 LYS C NZ 1 +ATOM 5385 N N . SER C 1 87 ? 47.680 62.251 136.847 1.00 118.56 ? 86 SER C N 1 +ATOM 5386 C CA . SER C 1 87 ? 49.000 62.884 136.831 1.00 115.38 ? 86 SER C CA 1 +ATOM 5387 C C . SER C 1 87 ? 48.987 64.328 137.330 1.00 116.51 ? 86 SER C C 1 +ATOM 5388 O O . SER C 1 87 ? 50.030 64.883 137.691 1.00 114.75 ? 86 SER C O 1 +ATOM 5389 C CB . SER C 1 87 ? 49.584 62.844 135.420 1.00 133.38 ? 86 SER C CB 1 +ATOM 5390 O OG . SER C 1 87 ? 49.019 63.857 134.605 1.00 122.67 ? 86 SER C OG 1 +ATOM 5391 N N . ALA C 1 88 ? 47.802 64.931 137.334 1.00 119.72 ? 87 ALA C N 1 +ATOM 5392 C CA . ALA C 1 88 ? 47.632 66.315 137.756 1.00 97.62 ? 87 ALA C CA 1 +ATOM 5393 C C . ALA C 1 88 ? 47.443 66.417 139.267 1.00 97.01 ? 87 ALA C C 1 +ATOM 5394 O O . ALA C 1 88 ? 47.408 67.512 139.821 1.00 116.00 ? 87 ALA C O 1 +ATOM 5395 C CB . ALA C 1 88 ? 46.450 66.948 137.027 1.00 95.85 ? 87 ALA C CB 1 +ATOM 5396 N N . MET C 1 89 ? 47.329 65.267 139.925 1.00 99.03 ? 88 MET C N 1 +ATOM 5397 C CA . MET C 1 89 ? 47.081 65.210 141.364 1.00 115.49 ? 88 MET C CA 1 +ATOM 5398 C C . MET C 1 89 ? 48.396 65.308 142.143 1.00 102.37 ? 88 MET C C 1 +ATOM 5399 O O . MET C 1 89 ? 49.461 65.091 141.571 1.00 113.63 ? 88 MET C O 1 +ATOM 5400 C CB . MET C 1 89 ? 46.333 63.917 141.701 1.00 105.13 ? 88 MET C CB 1 +ATOM 5401 C CG . MET C 1 89 ? 44.964 63.827 141.061 1.00 117.04 ? 88 MET C CG 1 +ATOM 5402 S SD . MET C 1 89 ? 43.841 65.066 141.725 1.00 111.35 ? 88 MET C SD 1 +ATOM 5403 C CE . MET C 1 89 ? 42.452 64.916 140.599 1.00 123.23 ? 88 MET C CE 1 +ATOM 5404 N N . PRO C 1 90 ? 48.335 65.640 143.447 1.00 96.59 ? 89 PRO C N 1 +ATOM 5405 C CA . PRO C 1 90 ? 47.159 65.902 144.287 1.00 120.28 ? 89 PRO C CA 1 +ATOM 5406 C C . PRO C 1 90 ? 46.654 67.325 144.146 1.00 108.54 ? 89 PRO C C 1 +ATOM 5407 O O . PRO C 1 90 ? 45.608 67.670 144.703 1.00 110.19 ? 89 PRO C O 1 +ATOM 5408 C CB . PRO C 1 90 ? 47.688 65.693 145.713 1.00 111.01 ? 89 PRO C CB 1 +ATOM 5409 C CG . PRO C 1 90 ? 49.177 65.536 145.596 1.00 102.43 ? 89 PRO C CG 1 +ATOM 5410 C CD . PRO C 1 90 ? 49.583 65.833 144.200 1.00 100.51 ? 89 PRO C CD 1 +ATOM 5411 N N . GLU C 1 91 ? 47.405 68.142 143.418 1.00 101.36 ? 90 GLU C N 1 +ATOM 5412 C CA . GLU C 1 91 ? 47.098 69.557 143.309 1.00 123.60 ? 90 GLU C CA 1 +ATOM 5413 C C . GLU C 1 91 ? 45.769 69.736 142.594 1.00 123.85 ? 90 GLU C C 1 +ATOM 5414 O O . GLU C 1 91 ? 44.942 70.561 142.986 1.00 114.21 ? 90 GLU C O 1 +ATOM 5415 C CB . GLU C 1 91 ? 48.231 70.297 142.599 1.00 151.34 ? 90 GLU C CB 1 +ATOM 5416 C CG . GLU C 1 91 ? 49.582 70.134 143.295 1.00 164.22 ? 90 GLU C CG 1 +ATOM 5417 C CD . GLU C 1 91 ? 50.415 71.403 143.275 1.00 182.61 ? 90 GLU C CD 1 +ATOM 5418 O OE1 . GLU C 1 91 ? 50.209 72.265 144.160 1.00 175.53 ? 90 GLU C OE1 1 +ATOM 5419 O OE2 . GLU C 1 91 ? 51.276 71.535 142.378 1.00 187.20 ? 90 GLU C OE2 1 +ATOM 5420 N N . GLY C 1 92 ? 45.560 68.940 141.554 1.00 110.45 ? 91 GLY C N 1 +ATOM 5421 C CA . GLY C 1 92 ? 44.256 68.859 140.933 1.00 92.37 ? 91 GLY C CA 1 +ATOM 5422 C C . GLY C 1 92 ? 44.135 69.501 139.573 1.00 96.50 ? 91 GLY C C 1 +ATOM 5423 O O . GLY C 1 92 ? 45.116 69.951 138.978 1.00 115.08 ? 91 GLY C O 1 +ATOM 5424 N N . TYR C 1 93 ? 42.904 69.531 139.081 1.00 94.41 ? 92 TYR C N 1 +ATOM 5425 C CA . TYR C 1 93 ? 42.606 70.097 137.779 1.00 100.32 ? 92 TYR C CA 1 +ATOM 5426 C C . TYR C 1 93 ? 41.233 70.775 137.781 1.00 110.36 ? 92 TYR C C 1 +ATOM 5427 O O . TYR C 1 93 ? 40.456 70.613 138.725 1.00 114.77 ? 92 TYR C O 1 +ATOM 5428 C CB . TYR C 1 93 ? 42.708 69.020 136.685 1.00 92.04 ? 92 TYR C CB 1 +ATOM 5429 C CG . TYR C 1 93 ? 41.726 67.856 136.786 1.00 104.19 ? 92 TYR C CG 1 +ATOM 5430 C CD1 . TYR C 1 93 ? 40.418 67.979 136.331 1.00 122.92 ? 92 TYR C CD1 1 +ATOM 5431 C CD2 . TYR C 1 93 ? 42.119 66.623 137.299 1.00 99.40 ? 92 TYR C CD2 1 +ATOM 5432 C CE1 . TYR C 1 93 ? 39.521 66.917 136.407 1.00 120.66 ? 92 TYR C CE1 1 +ATOM 5433 C CE2 . TYR C 1 93 ? 41.225 65.551 137.377 1.00 111.71 ? 92 TYR C CE2 1 +ATOM 5434 C CZ . TYR C 1 93 ? 39.927 65.705 136.927 1.00 107.58 ? 92 TYR C CZ 1 +ATOM 5435 O OH . TYR C 1 93 ? 39.028 64.657 136.995 1.00 119.09 ? 92 TYR C OH 1 +ATOM 5436 N N . VAL C 1 94 ? 40.955 71.540 136.726 1.00 121.43 ? 93 VAL C N 1 +ATOM 5437 C CA . VAL C 1 94 ? 39.691 72.260 136.566 1.00 106.72 ? 93 VAL C CA 1 +ATOM 5438 C C . VAL C 1 94 ? 38.962 71.740 135.327 1.00 106.06 ? 93 VAL C C 1 +ATOM 5439 O O . VAL C 1 94 ? 39.552 71.652 134.250 1.00 104.79 ? 93 VAL C O 1 +ATOM 5440 C CB . VAL C 1 94 ? 39.921 73.783 136.386 1.00 106.90 ? 93 VAL C CB 1 +ATOM 5441 C CG1 . VAL C 1 94 ? 38.589 74.530 136.355 1.00 102.23 ? 93 VAL C CG1 1 +ATOM 5442 C CG2 . VAL C 1 94 ? 40.829 74.338 137.479 1.00 105.14 ? 93 VAL C CG2 1 +ATOM 5443 N N . GLN C 1 95 ? 37.683 71.406 135.475 1.00 80.79 ? 94 GLN C N 1 +ATOM 5444 C CA . GLN C 1 95 ? 36.917 70.798 134.387 1.00 94.99 ? 94 GLN C CA 1 +ATOM 5445 C C . GLN C 1 95 ? 35.726 71.666 133.990 1.00 110.78 ? 94 GLN C C 1 +ATOM 5446 O O . GLN C 1 95 ? 34.773 71.825 134.760 1.00 92.49 ? 94 GLN C O 1 +ATOM 5447 C CB . GLN C 1 95 ? 36.461 69.386 134.786 1.00 90.94 ? 94 GLN C CB 1 +ATOM 5448 C CG . GLN C 1 95 ? 35.470 68.726 133.842 1.00 83.42 ? 94 GLN C CG 1 +ATOM 5449 C CD . GLN C 1 95 ? 35.328 67.231 134.088 1.00 97.60 ? 94 GLN C CD 1 +ATOM 5450 O OE1 . GLN C 1 95 ? 36.319 66.514 134.237 1.00 91.19 ? 94 GLN C OE1 1 +ATOM 5451 N NE2 . GLN C 1 95 ? 34.090 66.756 134.126 1.00 99.27 ? 94 GLN C NE2 1 +ATOM 5452 N N . GLU C 1 96 ? 35.798 72.227 132.785 1.00 102.15 ? 95 GLU C N 1 +ATOM 5453 C CA . GLU C 1 96 ? 34.767 73.127 132.276 1.00 86.59 ? 95 GLU C CA 1 +ATOM 5454 C C . GLU C 1 96 ? 34.008 72.477 131.125 1.00 96.19 ? 95 GLU C C 1 +ATOM 5455 O O . GLU C 1 96 ? 34.611 71.979 130.174 1.00 102.96 ? 95 GLU C O 1 +ATOM 5456 C CB . GLU C 1 96 ? 35.396 74.452 131.816 1.00 114.35 ? 95 GLU C CB 1 +ATOM 5457 C CG . GLU C 1 96 ? 35.871 75.375 132.955 1.00 149.60 ? 95 GLU C CG 1 +ATOM 5458 C CD . GLU C 1 96 ? 36.848 76.476 132.499 1.00 177.74 ? 95 GLU C CD 1 +ATOM 5459 O OE1 . GLU C 1 96 ? 38.052 76.186 132.347 1.00 180.66 ? 95 GLU C OE1 1 +ATOM 5460 O OE2 . GLU C 1 96 ? 36.420 77.635 132.309 1.00 174.29 ? 95 GLU C OE2 1 +ATOM 5461 N N . ARG C 1 97 ? 32.682 72.475 131.216 1.00 74.25 ? 96 ARG C N 1 +ATOM 5462 C CA . ARG C 1 97 ? 31.861 71.898 130.162 1.00 94.15 ? 96 ARG C CA 1 +ATOM 5463 C C . ARG C 1 97 ? 30.776 72.845 129.699 1.00 110.57 ? 96 ARG C C 1 +ATOM 5464 O O . ARG C 1 97 ? 30.349 73.734 130.426 1.00 105.46 ? 96 ARG C O 1 +ATOM 5465 C CB . ARG C 1 97 ? 31.182 70.612 130.633 1.00 68.87 ? 96 ARG C CB 1 +ATOM 5466 C CG . ARG C 1 97 ? 32.071 69.396 130.696 1.00 118.37 ? 96 ARG C CG 1 +ATOM 5467 C CD . ARG C 1 97 ? 31.264 68.116 130.513 1.00 97.46 ? 96 ARG C CD 1 +ATOM 5468 N NE . ARG C 1 97 ? 32.044 66.950 130.913 1.00 121.08 ? 96 ARG C NE 1 +ATOM 5469 C CZ . ARG C 1 97 ? 31.795 66.202 131.983 1.00 106.99 ? 96 ARG C CZ 1 +ATOM 5470 N NH1 . ARG C 1 97 ? 30.760 66.471 132.769 1.00 118.25 ? 96 ARG C NH1 1 +ATOM 5471 N NH2 . ARG C 1 97 ? 32.578 65.169 132.257 1.00 101.97 ? 96 ARG C NH2 1 +ATOM 5472 N N . THR C 1 98 ? 30.326 72.630 128.476 1.00 93.79 ? 97 THR C N 1 +ATOM 5473 C CA . THR C 1 98 ? 29.079 73.196 128.018 1.00 119.20 ? 97 THR C CA 1 +ATOM 5474 C C . THR C 1 98 ? 28.266 72.007 127.507 1.00 97.96 ? 97 THR C C 1 +ATOM 5475 O O . THR C 1 98 ? 28.828 71.046 126.985 1.00 89.36 ? 97 THR C O 1 +ATOM 5476 C CB . THR C 1 98 ? 29.316 74.246 126.925 1.00 120.43 ? 97 THR C CB 1 +ATOM 5477 O OG1 . THR C 1 98 ? 30.362 75.141 127.339 1.00 90.68 ? 97 THR C OG1 1 +ATOM 5478 C CG2 . THR C 1 98 ? 28.032 75.026 126.647 1.00 60.39 ? 97 THR C CG2 1 +ATOM 5479 N N . ILE C 1 99 ? 26.952 72.037 127.694 1.00 82.93 ? 98 ILE C N 1 +ATOM 5480 C CA . ILE C 1 99 ? 26.139 70.859 127.408 1.00 103.09 ? 98 ILE C CA 1 +ATOM 5481 C C . ILE C 1 99 ? 24.839 71.233 126.677 1.00 113.40 ? 98 ILE C C 1 +ATOM 5482 O O . ILE C 1 99 ? 23.860 71.668 127.283 1.00 92.99 ? 98 ILE C O 1 +ATOM 5483 C CB . ILE C 1 99 ? 25.888 70.037 128.713 1.00 84.83 ? 98 ILE C CB 1 +ATOM 5484 C CG1 . ILE C 1 99 ? 27.226 69.580 129.324 1.00 67.53 ? 98 ILE C CG1 1 +ATOM 5485 C CG2 . ILE C 1 99 ? 24.947 68.851 128.458 1.00 63.36 ? 98 ILE C CG2 1 +ATOM 5486 C CD1 . ILE C 1 99 ? 27.244 69.451 130.825 1.00 68.26 ? 98 ILE C CD1 1 +ATOM 5487 N N . PHE C 1 100 ? 24.847 71.068 125.359 1.00 92.75 ? 99 PHE C N 1 +ATOM 5488 C CA . PHE C 1 100 ? 23.708 71.450 124.542 1.00 82.38 ? 99 PHE C CA 1 +ATOM 5489 C C . PHE C 1 100 ? 22.721 70.308 124.422 1.00 75.41 ? 99 PHE C C 1 +ATOM 5490 O O . PHE C 1 100 ? 22.942 69.375 123.667 1.00 100.17 ? 99 PHE C O 1 +ATOM 5491 C CB . PHE C 1 100 ? 24.172 71.868 123.145 1.00 73.33 ? 99 PHE C CB 1 +ATOM 5492 C CG . PHE C 1 100 ? 25.251 72.906 123.157 1.00 91.91 ? 99 PHE C CG 1 +ATOM 5493 C CD1 . PHE C 1 100 ? 26.586 72.535 123.188 1.00 99.79 ? 99 PHE C CD1 1 +ATOM 5494 C CD2 . PHE C 1 100 ? 24.935 74.256 123.147 1.00 104.57 ? 99 PHE C CD2 1 +ATOM 5495 C CE1 . PHE C 1 100 ? 27.595 73.496 123.208 1.00 99.58 ? 99 PHE C CE1 1 +ATOM 5496 C CE2 . PHE C 1 100 ? 25.935 75.223 123.167 1.00 94.50 ? 99 PHE C CE2 1 +ATOM 5497 C CZ . PHE C 1 100 ? 27.269 74.841 123.197 1.00 88.76 ? 99 PHE C CZ 1 +ATOM 5498 N N . PHE C 1 101 ? 21.630 70.369 125.168 1.00 70.97 ? 100 PHE C N 1 +ATOM 5499 C CA . PHE C 1 101 ? 20.535 69.447 124.915 1.00 87.21 ? 100 PHE C CA 1 +ATOM 5500 C C . PHE C 1 101 ? 19.885 69.856 123.600 1.00 96.58 ? 100 PHE C C 1 +ATOM 5501 O O . PHE C 1 101 ? 19.418 70.980 123.455 1.00 98.94 ? 100 PHE C O 1 +ATOM 5502 C CB . PHE C 1 101 ? 19.534 69.461 126.068 1.00 69.21 ? 100 PHE C CB 1 +ATOM 5503 C CG . PHE C 1 101 ? 20.118 68.992 127.365 1.00 90.19 ? 100 PHE C CG 1 +ATOM 5504 C CD1 . PHE C 1 101 ? 21.019 69.787 128.057 1.00 99.89 ? 100 PHE C CD1 1 +ATOM 5505 C CD2 . PHE C 1 101 ? 19.784 67.751 127.882 1.00 97.73 ? 100 PHE C CD2 1 +ATOM 5506 C CE1 . PHE C 1 101 ? 21.570 69.360 129.233 1.00 62.54 ? 100 PHE C CE1 1 +ATOM 5507 C CE2 . PHE C 1 101 ? 20.331 67.317 129.064 1.00 94.34 ? 100 PHE C CE2 1 +ATOM 5508 C CZ . PHE C 1 101 ? 21.224 68.120 129.739 1.00 108.01 ? 100 PHE C CZ 1 +ATOM 5509 N N . LYS C 1 102 ? 19.895 68.959 122.626 1.00 85.59 ? 101 LYS C N 1 +ATOM 5510 C CA . LYS C 1 102 ? 19.314 69.265 121.327 1.00 121.62 ? 101 LYS C CA 1 +ATOM 5511 C C . LYS C 1 102 ? 17.852 69.685 121.457 1.00 136.76 ? 101 LYS C C 1 +ATOM 5512 O O . LYS C 1 102 ? 17.082 69.048 122.186 1.00 86.21 ? 101 LYS C O 1 +ATOM 5513 C CB . LYS C 1 102 ? 19.431 68.069 120.381 1.00 83.21 ? 101 LYS C CB 1 +ATOM 5514 C CG . LYS C 1 102 ? 18.706 68.263 119.062 1.00 110.22 ? 101 LYS C CG 1 +ATOM 5515 C CD . LYS C 1 102 ? 18.812 67.030 118.198 1.00 129.74 ? 101 LYS C CD 1 +ATOM 5516 C CE . LYS C 1 102 ? 18.994 67.378 116.725 1.00 120.36 ? 101 LYS C CE 1 +ATOM 5517 N NZ . LYS C 1 102 ? 17.742 67.179 115.949 1.00 133.14 ? 101 LYS C NZ 1 +ATOM 5518 N N . ASP C 1 103 ? 17.502 70.761 120.746 1.00 108.73 ? 102 ASP C N 1 +ATOM 5519 C CA . ASP C 1 103 ? 16.161 71.355 120.748 1.00 116.45 ? 102 ASP C CA 1 +ATOM 5520 C C . ASP C 1 103 ? 15.835 71.979 122.099 1.00 108.24 ? 102 ASP C C 1 +ATOM 5521 O O . ASP C 1 103 ? 14.668 72.050 122.487 1.00 105.04 ? 102 ASP C O 1 +ATOM 5522 C CB . ASP C 1 103 ? 15.077 70.334 120.346 1.00 136.00 ? 102 ASP C CB 1 +ATOM 5523 C CG . ASP C 1 103 ? 15.125 69.972 118.864 1.00 149.54 ? 102 ASP C CG 1 +ATOM 5524 O OD1 . ASP C 1 103 ? 15.620 70.798 118.068 1.00 135.75 ? 102 ASP C OD1 1 +ATOM 5525 O OD2 . ASP C 1 103 ? 14.662 68.867 118.494 1.00 144.88 ? 102 ASP C OD2 1 +ATOM 5526 N N . ASP C 1 104 ? 16.863 72.443 122.805 1.00 100.33 ? 103 ASP C N 1 +ATOM 5527 C CA . ASP C 1 104 ? 16.686 72.815 124.204 1.00 97.09 ? 103 ASP C CA 1 +ATOM 5528 C C . ASP C 1 104 ? 17.864 73.570 124.840 1.00 100.75 ? 103 ASP C C 1 +ATOM 5529 O O . ASP C 1 104 ? 18.819 73.966 124.166 1.00 77.82 ? 103 ASP C O 1 +ATOM 5530 C CB . ASP C 1 104 ? 16.348 71.566 125.021 1.00 69.77 ? 103 ASP C CB 1 +ATOM 5531 C CG . ASP C 1 104 ? 16.045 71.875 126.459 1.00 125.36 ? 103 ASP C CG 1 +ATOM 5532 O OD1 . ASP C 1 104 ? 16.082 73.079 126.804 1.00 81.09 ? 103 ASP C OD1 1 +ATOM 5533 O OD2 . ASP C 1 104 ? 15.778 70.947 127.232 1.00 212.25 ? 103 ASP C OD2 1 +ATOM 5534 N N . GLY C 1 105 ? 17.779 73.758 126.158 1.00 103.04 ? 104 GLY C N 1 +ATOM 5535 C CA . GLY C 1 105 ? 18.645 74.633 126.912 1.00 81.49 ? 104 GLY C CA 1 +ATOM 5536 C C . GLY C 1 105 ? 20.085 74.181 126.986 1.00 99.90 ? 104 GLY C C 1 +ATOM 5537 O O . GLY C 1 105 ? 20.508 73.347 126.207 1.00 104.69 ? 104 GLY C O 1 +ATOM 5538 N N . ASN C 1 106 ? 20.855 74.727 127.916 1.00 79.40 ? 105 ASN C N 1 +ATOM 5539 C CA . ASN C 1 106 ? 22.233 74.283 128.065 1.00 83.06 ? 105 ASN C CA 1 +ATOM 5540 C C . ASN C 1 106 ? 22.782 74.458 129.477 1.00 105.90 ? 105 ASN C C 1 +ATOM 5541 O O . ASN C 1 106 ? 22.401 75.388 130.179 1.00 112.63 ? 105 ASN C O 1 +ATOM 5542 C CB . ASN C 1 106 ? 23.149 74.972 127.041 1.00 95.87 ? 105 ASN C CB 1 +ATOM 5543 C CG . ASN C 1 106 ? 23.162 76.491 127.178 1.00 93.02 ? 105 ASN C CG 1 +ATOM 5544 O OD1 . ASN C 1 106 ? 23.585 77.040 128.200 1.00 110.71 ? 105 ASN C OD1 1 +ATOM 5545 N ND2 . ASN C 1 106 ? 22.724 77.175 126.128 1.00 79.41 ? 105 ASN C ND2 1 +ATOM 5546 N N . TYR C 1 107 ? 23.671 73.553 129.882 1.00 86.36 ? 106 TYR C N 1 +ATOM 5547 C CA . TYR C 1 107 ? 24.419 73.697 131.127 1.00 84.88 ? 106 TYR C CA 1 +ATOM 5548 C C . TYR C 1 107 ? 25.824 74.263 130.871 1.00 88.76 ? 106 TYR C C 1 +ATOM 5549 O O . TYR C 1 107 ? 26.540 73.802 129.983 1.00 76.61 ? 106 TYR C O 1 +ATOM 5550 C CB . TYR C 1 107 ? 24.580 72.340 131.819 1.00 79.07 ? 106 TYR C CB 1 +ATOM 5551 C CG . TYR C 1 107 ? 23.311 71.664 132.296 1.00 75.32 ? 106 TYR C CG 1 +ATOM 5552 C CD1 . TYR C 1 107 ? 22.174 72.391 132.607 1.00 97.20 ? 106 TYR C CD1 1 +ATOM 5553 C CD2 . TYR C 1 107 ? 23.265 70.284 132.455 1.00 96.54 ? 106 TYR C CD2 1 +ATOM 5554 C CE1 . TYR C 1 107 ? 21.019 71.756 133.056 1.00 74.51 ? 106 TYR C CE1 1 +ATOM 5555 C CE2 . TYR C 1 107 ? 22.121 69.644 132.900 1.00 70.88 ? 106 TYR C CE2 1 +ATOM 5556 C CZ . TYR C 1 107 ? 21.001 70.382 133.197 1.00 91.35 ? 106 TYR C CZ 1 +ATOM 5557 O OH . TYR C 1 107 ? 19.862 69.743 133.634 1.00 93.06 ? 106 TYR C OH 1 +ATOM 5558 N N . LYS C 1 108 ? 26.229 75.254 131.652 1.00 88.35 ? 107 LYS C N 1 +ATOM 5559 C CA . LYS C 1 108 ? 27.631 75.653 131.650 1.00 80.97 ? 107 LYS C CA 1 +ATOM 5560 C C . LYS C 1 108 ? 28.201 75.445 133.042 1.00 91.51 ? 107 LYS C C 1 +ATOM 5561 O O . LYS C 1 108 ? 27.768 76.087 134.001 1.00 113.14 ? 107 LYS C O 1 +ATOM 5562 C CB . LYS C 1 108 ? 27.814 77.099 131.178 1.00 94.25 ? 107 LYS C CB 1 +ATOM 5563 C CG . LYS C 1 108 ? 27.703 77.282 129.664 1.00 100.53 ? 107 LYS C CG 1 +ATOM 5564 C CD . LYS C 1 108 ? 27.783 78.749 129.246 1.00 101.23 ? 107 LYS C CD 1 +ATOM 5565 C CE . LYS C 1 108 ? 27.834 78.909 127.720 1.00 105.78 ? 107 LYS C CE 1 +ATOM 5566 N NZ . LYS C 1 108 ? 29.097 78.369 127.123 1.00 98.12 ? 107 LYS C NZ 1 +ATOM 5567 N N . THR C 1 109 ? 29.164 74.533 133.143 1.00 93.56 ? 108 THR C N 1 +ATOM 5568 C CA . THR C 1 109 ? 29.725 74.131 134.429 1.00 99.40 ? 108 THR C CA 1 +ATOM 5569 C C . THR C 1 109 ? 31.191 74.498 134.587 1.00 98.32 ? 108 THR C C 1 +ATOM 5570 O O . THR C 1 109 ? 31.933 74.622 133.612 1.00 81.23 ? 108 THR C O 1 +ATOM 5571 C CB . THR C 1 109 ? 29.627 72.602 134.652 1.00 92.77 ? 108 THR C CB 1 +ATOM 5572 O OG1 . THR C 1 109 ? 30.617 71.927 133.859 1.00 77.05 ? 108 THR C OG1 1 +ATOM 5573 C CG2 . THR C 1 109 ? 28.226 72.083 134.325 1.00 102.39 ? 108 THR C CG2 1 +ATOM 5574 N N . ARG C 1 110 ? 31.597 74.670 135.838 1.00 74.04 ? 109 ARG C N 1 +ATOM 5575 C CA . ARG C 1 110 ? 33.005 74.702 136.178 1.00 85.22 ? 109 ARG C CA 1 +ATOM 5576 C C . ARG C 1 110 ? 33.208 73.985 137.495 1.00 90.95 ? 109 ARG C C 1 +ATOM 5577 O O . ARG C 1 110 ? 32.587 74.332 138.504 1.00 95.81 ? 109 ARG C O 1 +ATOM 5578 C CB . ARG C 1 110 ? 33.534 76.126 136.284 1.00 95.28 ? 109 ARG C CB 1 +ATOM 5579 C CG . ARG C 1 110 ? 34.987 76.172 136.714 1.00 121.11 ? 109 ARG C CG 1 +ATOM 5580 C CD . ARG C 1 110 ? 35.460 77.593 136.939 1.00 90.61 ? 109 ARG C CD 1 +ATOM 5581 N NE . ARG C 1 110 ? 36.914 77.672 137.055 1.00 116.13 ? 109 ARG C NE 1 +ATOM 5582 C CZ . ARG C 1 110 ? 37.584 77.587 138.201 1.00 122.18 ? 109 ARG C CZ 1 +ATOM 5583 N NH1 . ARG C 1 110 ? 36.934 77.418 139.346 1.00 129.08 ? 109 ARG C NH1 1 +ATOM 5584 N NH2 . ARG C 1 110 ? 38.907 77.672 138.200 1.00 103.10 ? 109 ARG C NH2 1 +ATOM 5585 N N . ALA C 1 111 ? 34.086 72.986 137.465 1.00 108.26 ? 110 ALA C N 1 +ATOM 5586 C CA . ALA C 1 111 ? 34.403 72.169 138.629 1.00 88.22 ? 110 ALA C CA 1 +ATOM 5587 C C . ALA C 1 111 ? 35.900 72.161 138.927 1.00 94.98 ? 110 ALA C C 1 +ATOM 5588 O O . ALA C 1 111 ? 36.723 72.169 138.010 1.00 85.51 ? 110 ALA C O 1 +ATOM 5589 C CB . ALA C 1 111 ? 33.910 70.751 138.420 1.00 100.59 ? 110 ALA C CB 1 +ATOM 5590 N N . GLU C 1 112 ? 36.242 72.161 140.213 1.00 77.11 ? 111 GLU C N 1 +ATOM 5591 C CA . GLU C 1 112 ? 37.617 71.948 140.649 1.00 106.55 ? 111 GLU C CA 1 +ATOM 5592 C C . GLU C 1 112 ? 37.701 70.587 141.335 1.00 116.53 ? 111 GLU C C 1 +ATOM 5593 O O . GLU C 1 112 ? 37.100 70.374 142.395 1.00 106.65 ? 111 GLU C O 1 +ATOM 5594 C CB . GLU C 1 112 ? 38.084 73.054 141.610 1.00 123.59 ? 111 GLU C CB 1 +ATOM 5595 C CG . GLU C 1 112 ? 38.370 74.417 140.970 1.00 159.52 ? 111 GLU C CG 1 +ATOM 5596 C CD . GLU C 1 112 ? 38.636 75.534 141.994 1.00 162.44 ? 111 GLU C CD 1 +ATOM 5597 O OE1 . GLU C 1 112 ? 38.760 75.242 143.207 1.00 137.04 ? 111 GLU C OE1 1 +ATOM 5598 O OE2 . GLU C 1 112 ? 38.718 76.712 141.578 1.00 153.02 ? 111 GLU C OE2 1 +ATOM 5599 N N . VAL C 1 113 ? 38.425 69.662 140.711 1.00 101.76 ? 112 VAL C N 1 +ATOM 5600 C CA . VAL C 1 113 ? 38.669 68.357 141.303 1.00 84.84 ? 112 VAL C CA 1 +ATOM 5601 C C . VAL C 1 113 ? 40.100 68.288 141.793 1.00 106.34 ? 112 VAL C C 1 +ATOM 5602 O O . VAL C 1 113 ? 41.038 68.494 141.020 1.00 101.16 ? 112 VAL C O 1 +ATOM 5603 C CB . VAL C 1 113 ? 38.456 67.210 140.313 1.00 72.61 ? 112 VAL C CB 1 +ATOM 5604 C CG1 . VAL C 1 113 ? 38.317 65.910 141.068 1.00 95.05 ? 112 VAL C CG1 1 +ATOM 5605 C CG2 . VAL C 1 113 ? 37.226 67.448 139.477 1.00 105.54 ? 112 VAL C CG2 1 +ATOM 5606 N N . LYS C 1 114 ? 40.250 68.005 143.084 1.00 90.56 ? 113 LYS C N 1 +ATOM 5607 C CA . LYS C 1 114 ? 41.554 67.904 143.729 1.00 98.74 ? 113 LYS C CA 1 +ATOM 5608 C C . LYS C 1 114 ? 41.448 67.155 145.061 1.00 109.39 ? 113 LYS C C 1 +ATOM 5609 O O . LYS C 1 114 ? 40.352 66.824 145.520 1.00 91.58 ? 113 LYS C O 1 +ATOM 5610 C CB . LYS C 1 114 ? 42.178 69.297 143.936 1.00 126.66 ? 113 LYS C CB 1 +ATOM 5611 C CG . LYS C 1 114 ? 41.304 70.291 144.725 1.00 126.78 ? 113 LYS C CG 1 +ATOM 5612 C CD . LYS C 1 114 ? 42.002 71.633 145.006 1.00 101.63 ? 113 LYS C CD 1 +ATOM 5613 C CE . LYS C 1 114 ? 41.164 72.525 145.931 1.00 126.52 ? 113 LYS C CE 1 +ATOM 5614 N NZ . LYS C 1 114 ? 39.851 72.927 145.346 1.00 110.97 ? 113 LYS C NZ 1 +ATOM 5615 N N . PHE C 1 115 ? 42.598 66.890 145.672 1.00 100.18 ? 114 PHE C N 1 +ATOM 5616 C CA . PHE C 1 115 ? 42.666 66.161 146.934 1.00 104.42 ? 114 PHE C CA 1 +ATOM 5617 C C . PHE C 1 115 ? 42.675 67.133 148.100 1.00 106.74 ? 114 PHE C C 1 +ATOM 5618 O O . PHE C 1 115 ? 43.376 68.144 148.057 1.00 118.36 ? 114 PHE C O 1 +ATOM 5619 C CB . PHE C 1 115 ? 43.946 65.318 146.997 1.00 122.59 ? 114 PHE C CB 1 +ATOM 5620 C CG . PHE C 1 115 ? 43.763 63.879 146.584 1.00 126.70 ? 114 PHE C CG 1 +ATOM 5621 C CD1 . PHE C 1 115 ? 43.288 62.935 147.490 1.00 112.61 ? 114 PHE C CD1 1 +ATOM 5622 C CD2 . PHE C 1 115 ? 44.092 63.464 145.300 1.00 105.89 ? 114 PHE C CD2 1 +ATOM 5623 C CE1 . PHE C 1 115 ? 43.129 61.609 147.119 1.00 99.52 ? 114 PHE C CE1 1 +ATOM 5624 C CE2 . PHE C 1 115 ? 43.935 62.141 144.920 1.00 97.49 ? 114 PHE C CE2 1 +ATOM 5625 C CZ . PHE C 1 115 ? 43.454 61.210 145.831 1.00 107.51 ? 114 PHE C CZ 1 +ATOM 5626 N N . GLU C 1 116 ? 41.908 66.821 149.142 1.00 95.38 ? 115 GLU C N 1 +ATOM 5627 C CA . GLU C 1 116 ? 41.921 67.602 150.378 1.00 100.16 ? 115 GLU C CA 1 +ATOM 5628 C C . GLU C 1 116 ? 42.220 66.677 151.549 1.00 100.52 ? 115 GLU C C 1 +ATOM 5629 O O . GLU C 1 116 ? 41.332 66.313 152.322 1.00 100.71 ? 115 GLU C O 1 +ATOM 5630 C CB . GLU C 1 116 ? 40.584 68.304 150.589 1.00 96.72 ? 115 GLU C CB 1 +ATOM 5631 C CG . GLU C 1 116 ? 40.116 69.075 149.383 1.00 118.70 ? 115 GLU C CG 1 +ATOM 5632 C CD . GLU C 1 116 ? 39.006 70.049 149.706 1.00 156.93 ? 115 GLU C CD 1 +ATOM 5633 O OE1 . GLU C 1 116 ? 38.275 69.808 150.694 1.00 155.60 ? 115 GLU C OE1 1 +ATOM 5634 O OE2 . GLU C 1 116 ? 38.876 71.056 148.970 1.00 132.37 ? 115 GLU C OE2 1 +ATOM 5635 N N . GLY C 1 117 ? 43.484 66.297 151.671 1.00 94.22 ? 116 GLY C N 1 +ATOM 5636 C CA . GLY C 1 117 ? 43.858 65.239 152.581 1.00 80.52 ? 116 GLY C CA 1 +ATOM 5637 C C . GLY C 1 117 ? 43.643 63.914 151.881 1.00 115.04 ? 116 GLY C C 1 +ATOM 5638 O O . GLY C 1 117 ? 44.113 63.717 150.757 1.00 103.52 ? 116 GLY C O 1 +ATOM 5639 N N . ASP C 1 118 ? 42.912 63.017 152.537 1.00 139.96 ? 117 ASP C N 1 +ATOM 5640 C CA . ASP C 1 118 ? 42.717 61.662 152.030 1.00 124.35 ? 117 ASP C CA 1 +ATOM 5641 C C . ASP C 1 118 ? 41.547 61.576 151.058 1.00 113.55 ? 117 ASP C C 1 +ATOM 5642 O O . ASP C 1 118 ? 41.378 60.575 150.368 1.00 119.44 ? 117 ASP C O 1 +ATOM 5643 C CB . ASP C 1 118 ? 42.531 60.657 153.185 1.00 129.82 ? 117 ASP C CB 1 +ATOM 5644 C CG . ASP C 1 118 ? 41.167 60.790 153.893 1.00 160.05 ? 117 ASP C CG 1 +ATOM 5645 O OD1 . ASP C 1 118 ? 40.709 61.934 154.118 1.00 145.67 ? 117 ASP C OD1 1 +ATOM 5646 O OD2 . ASP C 1 118 ? 40.560 59.741 154.233 1.00 149.29 ? 117 ASP C OD2 1 +ATOM 5647 N N . THR C 1 119 ? 40.743 62.627 150.998 1.00 116.12 ? 118 THR C N 1 +ATOM 5648 C CA . THR C 1 119 ? 39.521 62.571 150.208 1.00 108.46 ? 118 THR C CA 1 +ATOM 5649 C C . THR C 1 119 ? 39.684 63.314 148.871 1.00 92.15 ? 118 THR C C 1 +ATOM 5650 O O . THR C 1 119 ? 40.462 64.264 148.775 1.00 92.75 ? 118 THR C O 1 +ATOM 5651 C CB . THR C 1 119 ? 38.301 63.056 151.041 1.00 87.77 ? 118 THR C CB 1 +ATOM 5652 O OG1 . THR C 1 119 ? 38.111 62.182 152.168 1.00 98.01 ? 118 THR C OG1 1 +ATOM 5653 C CG2 . THR C 1 119 ? 37.033 63.067 150.207 1.00 101.22 ? 118 THR C CG2 1 +ATOM 5654 N N . LEU C 1 120 ? 38.994 62.833 147.836 1.00 91.89 ? 119 LEU C N 1 +ATOM 5655 C CA . LEU C 1 120 ? 39.024 63.434 146.502 1.00 72.19 ? 119 LEU C CA 1 +ATOM 5656 C C . LEU C 1 120 ? 37.729 64.189 146.276 1.00 97.13 ? 119 LEU C C 1 +ATOM 5657 O O . LEU C 1 120 ? 36.661 63.581 146.192 1.00 78.91 ? 119 LEU C O 1 +ATOM 5658 C CB . LEU C 1 120 ? 39.174 62.347 145.433 1.00 77.65 ? 119 LEU C CB 1 +ATOM 5659 C CG . LEU C 1 120 ? 39.414 62.705 143.961 1.00 67.28 ? 119 LEU C CG 1 +ATOM 5660 C CD1 . LEU C 1 120 ? 40.269 61.660 143.301 1.00 151.66 ? 119 LEU C CD1 1 +ATOM 5661 C CD2 . LEU C 1 120 ? 38.102 62.865 143.219 1.00 75.74 ? 119 LEU C CD2 1 +ATOM 5662 N N . VAL C 1 121 ? 37.820 65.511 146.172 1.00 83.08 ? 120 VAL C N 1 +ATOM 5663 C CA . VAL C 1 121 ? 36.619 66.331 146.097 1.00 90.11 ? 120 VAL C CA 1 +ATOM 5664 C C . VAL C 1 121 ? 36.373 66.972 144.727 1.00 101.87 ? 120 VAL C C 1 +ATOM 5665 O O . VAL C 1 121 ? 37.281 67.502 144.080 1.00 82.52 ? 120 VAL C O 1 +ATOM 5666 C CB . VAL C 1 121 ? 36.574 67.404 147.215 1.00 90.66 ? 120 VAL C CB 1 +ATOM 5667 C CG1 . VAL C 1 121 ? 36.912 66.791 148.565 1.00 71.29 ? 120 VAL C CG1 1 +ATOM 5668 C CG2 . VAL C 1 121 ? 37.532 68.527 146.914 1.00 123.01 ? 120 VAL C CG2 1 +ATOM 5669 N N . ASN C 1 122 ? 35.120 66.891 144.296 1.00 85.77 ? 121 ASN C N 1 +ATOM 5670 C CA . ASN C 1 122 ? 34.658 67.536 143.085 1.00 89.48 ? 121 ASN C CA 1 +ATOM 5671 C C . ASN C 1 122 ? 33.674 68.622 143.499 1.00 107.51 ? 121 ASN C C 1 +ATOM 5672 O O . ASN C 1 122 ? 32.572 68.324 143.972 1.00 86.90 ? 121 ASN C O 1 +ATOM 5673 C CB . ASN C 1 122 ? 33.976 66.509 142.185 1.00 75.79 ? 121 ASN C CB 1 +ATOM 5674 C CG . ASN C 1 122 ? 33.704 67.035 140.795 1.00 82.37 ? 121 ASN C CG 1 +ATOM 5675 O OD1 . ASN C 1 122 ? 34.338 67.982 140.341 1.00 118.83 ? 121 ASN C OD1 1 +ATOM 5676 N ND2 . ASN C 1 122 ? 32.755 66.414 140.107 1.00 87.02 ? 121 ASN C ND2 1 +ATOM 5677 N N . ARG C 1 123 ? 34.103 69.876 143.359 1.00 101.16 ? 122 ARG C N 1 +ATOM 5678 C CA . ARG C 1 123 ? 33.289 71.046 143.696 1.00 90.88 ? 122 ARG C CA 1 +ATOM 5679 C C . ARG C 1 123 ? 32.770 71.738 142.438 1.00 102.33 ? 122 ARG C C 1 +ATOM 5680 O O . ARG C 1 123 ? 33.550 72.173 141.593 1.00 80.24 ? 122 ARG C O 1 +ATOM 5681 C CB . ARG C 1 123 ? 34.092 72.047 144.532 1.00 95.50 ? 122 ARG C CB 1 +ATOM 5682 C CG . ARG C 1 123 ? 34.348 71.624 145.965 1.00 98.62 ? 122 ARG C CG 1 +ATOM 5683 C CD . ARG C 1 123 ? 34.942 72.765 146.785 1.00 98.86 ? 122 ARG C CD 1 +ATOM 5684 N NE . ARG C 1 123 ? 35.597 72.264 147.990 1.00 117.76 ? 122 ARG C NE 1 +ATOM 5685 C CZ . ARG C 1 123 ? 34.955 71.908 149.098 1.00 123.97 ? 122 ARG C CZ 1 +ATOM 5686 N NH1 . ARG C 1 123 ? 33.631 72.000 149.165 1.00 105.05 ? 122 ARG C NH1 1 +ATOM 5687 N NH2 . ARG C 1 123 ? 35.638 71.455 150.139 1.00 109.33 ? 122 ARG C NH2 1 +ATOM 5688 N N . ILE C 1 124 ? 31.449 71.862 142.337 1.00 102.67 ? 123 ILE C N 1 +ATOM 5689 C CA . ILE C 1 124 ? 30.805 72.240 141.081 1.00 86.51 ? 123 ILE C CA 1 +ATOM 5690 C C . ILE C 1 124 ? 29.829 73.427 141.199 1.00 98.07 ? 123 ILE C C 1 +ATOM 5691 O O . ILE C 1 124 ? 28.963 73.445 142.077 1.00 82.36 ? 123 ILE C O 1 +ATOM 5692 C CB . ILE C 1 124 ? 30.064 71.009 140.470 1.00 112.70 ? 123 ILE C CB 1 +ATOM 5693 C CG1 . ILE C 1 124 ? 30.826 69.708 140.707 1.00 94.10 ? 123 ILE C CG1 1 +ATOM 5694 C CG2 . ILE C 1 124 ? 29.765 71.214 138.975 1.00 88.67 ? 123 ILE C CG2 1 +ATOM 5695 C CD1 . ILE C 1 124 ? 30.019 68.442 140.462 1.00 103.56 ? 123 ILE C CD1 1 +ATOM 5696 N N . GLU C 1 125 ? 29.993 74.414 140.313 1.00 93.97 ? 124 GLU C N 1 +ATOM 5697 C CA . GLU C 1 125 ? 28.982 75.447 140.039 1.00 89.37 ? 124 GLU C CA 1 +ATOM 5698 C C . GLU C 1 125 ? 28.391 75.203 138.641 1.00 88.40 ? 124 GLU C C 1 +ATOM 5699 O O . GLU C 1 125 ? 29.145 75.065 137.675 1.00 103.56 ? 124 GLU C O 1 +ATOM 5700 C CB . GLU C 1 125 ? 29.613 76.846 140.067 1.00 96.15 ? 124 GLU C CB 1 +ATOM 5701 C CG . GLU C 1 125 ? 30.375 77.195 141.340 1.00 142.08 ? 124 GLU C CG 1 +ATOM 5702 C CD . GLU C 1 125 ? 31.305 78.400 141.177 1.00 162.78 ? 124 GLU C CD 1 +ATOM 5703 O OE1 . GLU C 1 125 ? 31.825 78.628 140.065 1.00 176.06 ? 124 GLU C OE1 1 +ATOM 5704 O OE2 . GLU C 1 125 ? 31.521 79.119 142.172 1.00 148.62 ? 124 GLU C OE2 1 +ATOM 5705 N N . LEU C 1 126 ? 27.060 75.154 138.529 1.00 80.19 ? 125 LEU C N 1 +ATOM 5706 C CA . LEU C 1 126 ? 26.377 74.890 137.245 1.00 84.00 ? 125 LEU C CA 1 +ATOM 5707 C C . LEU C 1 126 ? 25.313 75.942 136.910 1.00 92.65 ? 125 LEU C C 1 +ATOM 5708 O O . LEU C 1 126 ? 24.555 76.358 137.784 1.00 107.30 ? 125 LEU C O 1 +ATOM 5709 C CB . LEU C 1 126 ? 25.744 73.487 137.240 1.00 81.41 ? 125 LEU C CB 1 +ATOM 5710 C CG . LEU C 1 126 ? 24.631 73.126 136.240 1.00 73.92 ? 125 LEU C CG 1 +ATOM 5711 C CD1 . LEU C 1 126 ? 24.795 71.708 135.768 1.00 83.88 ? 125 LEU C CD1 1 +ATOM 5712 C CD2 . LEU C 1 126 ? 23.237 73.278 136.833 1.00 90.53 ? 125 LEU C CD2 1 +ATOM 5713 N N . LYS C 1 127 ? 25.242 76.355 135.643 1.00 102.92 ? 126 LYS C N 1 +ATOM 5714 C CA . LYS C 1 127 ? 24.312 77.419 135.233 1.00 88.97 ? 126 LYS C CA 1 +ATOM 5715 C C . LYS C 1 127 ? 23.537 77.175 133.921 1.00 96.70 ? 126 LYS C C 1 +ATOM 5716 O O . LYS C 1 127 ? 24.049 77.423 132.827 1.00 113.64 ? 126 LYS C O 1 +ATOM 5717 C CB . LYS C 1 127 ? 25.041 78.770 135.166 1.00 105.92 ? 126 LYS C CB 1 +ATOM 5718 C CG . LYS C 1 127 ? 24.127 79.943 134.833 1.00 125.39 ? 126 LYS C CG 1 +ATOM 5719 C CD . LYS C 1 127 ? 24.818 81.296 134.940 1.00 137.02 ? 126 LYS C CD 1 +ATOM 5720 C CE . LYS C 1 127 ? 23.867 82.390 134.483 1.00 132.20 ? 126 LYS C CE 1 +ATOM 5721 N NZ . LYS C 1 127 ? 22.459 81.989 134.787 1.00 131.37 ? 126 LYS C NZ 1 +ATOM 5722 N N . GLY C 1 128 ? 22.287 76.731 134.038 1.00 97.19 ? 127 GLY C N 1 +ATOM 5723 C CA . GLY C 1 128 ? 21.460 76.440 132.874 1.00 92.61 ? 127 GLY C CA 1 +ATOM 5724 C C . GLY C 1 128 ? 20.444 77.502 132.463 1.00 119.32 ? 127 GLY C C 1 +ATOM 5725 O O . GLY C 1 128 ? 19.708 78.015 133.305 1.00 130.53 ? 127 GLY C O 1 +ATOM 5726 N N . ILE C 1 129 ? 20.409 77.821 131.164 1.00 126.44 ? 128 ILE C N 1 +ATOM 5727 C CA . ILE C 1 129 ? 19.486 78.813 130.581 1.00 111.18 ? 128 ILE C CA 1 +ATOM 5728 C C . ILE C 1 129 ? 18.845 78.262 129.318 1.00 85.02 ? 128 ILE C C 1 +ATOM 5729 O O . ILE C 1 129 ? 19.354 77.316 128.735 1.00 114.68 ? 128 ILE C O 1 +ATOM 5730 C CB . ILE C 1 129 ? 20.215 80.133 130.173 1.00 92.57 ? 128 ILE C CB 1 +ATOM 5731 C CG1 . ILE C 1 129 ? 20.765 80.864 131.406 1.00 139.74 ? 128 ILE C CG1 1 +ATOM 5732 C CG2 . ILE C 1 129 ? 19.317 81.047 129.307 1.00 167.39 ? 128 ILE C CG2 1 +ATOM 5733 C CD1 . ILE C 1 129 ? 22.267 80.667 131.662 1.00 128.96 ? 128 ILE C CD1 1 +ATOM 5734 N N . ASP C 1 130 ? 17.726 78.854 128.901 1.00 116.78 ? 129 ASP C N 1 +ATOM 5735 C CA . ASP C 1 130 ? 17.097 78.590 127.607 1.00 121.56 ? 129 ASP C CA 1 +ATOM 5736 C C . ASP C 1 130 ? 16.309 77.280 127.541 1.00 79.82 ? 129 ASP C C 1 +ATOM 5737 O O . ASP C 1 130 ? 15.991 76.798 126.463 1.00 89.41 ? 129 ASP C O 1 +ATOM 5738 C CB . ASP C 1 130 ? 18.102 78.678 126.438 1.00 119.90 ? 129 ASP C CB 1 +ATOM 5739 C CG . ASP C 1 130 ? 18.601 80.096 126.189 1.00 135.55 ? 129 ASP C CG 1 +ATOM 5740 O OD1 . ASP C 1 130 ? 17.760 81.019 126.116 1.00 123.63 ? 129 ASP C OD1 1 +ATOM 5741 O OD2 . ASP C 1 130 ? 19.834 80.287 126.073 1.00 130.74 ? 129 ASP C OD2 1 +ATOM 5742 N N . PHE C 1 131 ? 15.956 76.703 128.675 1.00 71.32 ? 130 PHE C N 1 +ATOM 5743 C CA . PHE C 1 131 ? 15.168 75.482 128.594 1.00 110.32 ? 130 PHE C CA 1 +ATOM 5744 C C . PHE C 1 131 ? 13.706 75.804 128.267 1.00 61.07 ? 130 PHE C C 1 +ATOM 5745 O O . PHE C 1 131 ? 13.326 76.962 128.235 1.00 104.16 ? 130 PHE C O 1 +ATOM 5746 C CB . PHE C 1 131 ? 15.360 74.618 129.850 1.00 105.52 ? 130 PHE C CB 1 +ATOM 5747 C CG . PHE C 1 131 ? 16.730 73.988 129.928 1.00 81.31 ? 130 PHE C CG 1 +ATOM 5748 C CD1 . PHE C 1 131 ? 17.824 74.718 130.387 1.00 96.30 ? 130 PHE C CD1 1 +ATOM 5749 C CD2 . PHE C 1 131 ? 16.937 72.688 129.493 1.00 89.33 ? 130 PHE C CD2 1 +ATOM 5750 C CE1 . PHE C 1 131 ? 19.094 74.158 130.430 1.00 61.78 ? 130 PHE C CE1 1 +ATOM 5751 C CE2 . PHE C 1 131 ? 18.199 72.120 129.532 1.00 85.82 ? 130 PHE C CE2 1 +ATOM 5752 C CZ . PHE C 1 131 ? 19.282 72.860 130.003 1.00 110.58 ? 130 PHE C CZ 1 +ATOM 5753 N N . LYS C 1 132 ? 12.903 74.790 127.979 1.00 79.14 ? 131 LYS C N 1 +ATOM 5754 C CA . LYS C 1 132 ? 11.488 74.999 127.691 1.00 82.71 ? 131 LYS C CA 1 +ATOM 5755 C C . LYS C 1 132 ? 10.642 74.473 128.836 1.00 87.61 ? 131 LYS C C 1 +ATOM 5756 O O . LYS C 1 132 ? 10.796 73.329 129.236 1.00 164.21 ? 131 LYS C O 1 +ATOM 5757 C CB . LYS C 1 132 ? 11.085 74.256 126.419 1.00 74.96 ? 131 LYS C CB 1 +ATOM 5758 C CG . LYS C 1 132 ? 11.975 74.503 125.216 1.00 85.23 ? 131 LYS C CG 1 +ATOM 5759 C CD . LYS C 1 132 ? 11.497 73.680 124.033 1.00 108.31 ? 131 LYS C CD 1 +ATOM 5760 C CE . LYS C 1 132 ? 12.237 74.045 122.762 1.00 122.28 ? 131 LYS C CE 1 +ATOM 5761 N NZ . LYS C 1 132 ? 11.956 73.046 121.687 1.00 128.05 ? 131 LYS C NZ 1 +ATOM 5762 N N . GLU C 1 133 ? 9.719 75.283 129.338 1.00 116.38 ? 132 GLU C N 1 +ATOM 5763 C CA . GLU C 1 133 ? 8.887 74.876 130.475 1.00 140.39 ? 132 GLU C CA 1 +ATOM 5764 C C . GLU C 1 133 ? 8.050 73.609 130.215 1.00 121.95 ? 132 GLU C C 1 +ATOM 5765 O O . GLU C 1 133 ? 7.456 73.057 131.136 1.00 111.52 ? 132 GLU C O 1 +ATOM 5766 C CB . GLU C 1 133 ? 8.006 76.041 130.975 1.00 106.40 ? 132 GLU C CB 1 +ATOM 5767 C CG . GLU C 1 133 ? 8.749 77.123 131.813 1.00 210.95 ? 132 GLU C CG 1 +ATOM 5768 C CD . GLU C 1 133 ? 8.995 76.745 133.298 1.00 191.71 ? 132 GLU C CD 1 +ATOM 5769 O OE1 . GLU C 1 133 ? 8.109 76.123 133.933 1.00 185.53 ? 132 GLU C OE1 1 +ATOM 5770 O OE2 . GLU C 1 133 ? 10.078 77.089 133.835 1.00 141.09 ? 132 GLU C OE2 1 +ATOM 5771 N N . ASP C 1 134 ? 8.024 73.140 128.972 1.00 100.79 ? 133 ASP C N 1 +ATOM 5772 C CA . ASP C 1 134 ? 7.302 71.918 128.627 1.00 101.98 ? 133 ASP C CA 1 +ATOM 5773 C C . ASP C 1 134 ? 8.239 70.900 127.987 1.00 126.85 ? 133 ASP C C 1 +ATOM 5774 O O . ASP C 1 134 ? 7.794 69.863 127.485 1.00 123.64 ? 133 ASP C O 1 +ATOM 5775 C CB . ASP C 1 134 ? 6.167 72.240 127.657 1.00 165.34 ? 133 ASP C CB 1 +ATOM 5776 C CG . ASP C 1 134 ? 6.638 73.057 126.459 1.00 191.29 ? 133 ASP C CG 1 +ATOM 5777 O OD1 . ASP C 1 134 ? 7.392 74.036 126.658 1.00 186.47 ? 133 ASP C OD1 1 +ATOM 5778 O OD2 . ASP C 1 134 ? 6.265 72.712 125.317 1.00 203.13 ? 133 ASP C OD2 1 +ATOM 5779 N N . GLY C 1 135 ? 9.535 71.211 128.011 1.00 139.15 ? 134 GLY C N 1 +ATOM 5780 C CA . GLY C 1 135 ? 10.526 70.410 127.335 1.00 126.73 ? 134 GLY C CA 1 +ATOM 5781 C C . GLY C 1 135 ? 10.784 69.032 127.938 1.00 132.89 ? 134 GLY C C 1 +ATOM 5782 O O . GLY C 1 135 ? 10.002 68.560 128.760 1.00 130.02 ? 134 GLY C O 1 +ATOM 5783 N N . ASN C 1 136 ? 11.870 68.383 127.515 1.00 133.47 ? 135 ASN C N 1 +ATOM 5784 C CA . ASN C 1 136 ? 12.205 67.058 128.035 1.00 76.23 ? 135 ASN C CA 1 +ATOM 5785 C C . ASN C 1 136 ? 12.809 67.131 129.444 1.00 107.74 ? 135 ASN C C 1 +ATOM 5786 O O . ASN C 1 136 ? 12.524 66.291 130.300 1.00 91.39 ? 135 ASN C O 1 +ATOM 5787 C CB . ASN C 1 136 ? 13.125 66.299 127.069 1.00 82.83 ? 135 ASN C CB 1 +ATOM 5788 C CG . ASN C 1 136 ? 12.360 65.591 125.949 1.00 102.05 ? 135 ASN C CG 1 +ATOM 5789 O OD1 . ASN C 1 136 ? 11.179 65.262 126.088 1.00 74.90 ? 135 ASN C OD1 1 +ATOM 5790 N ND2 . ASN C 1 136 ? 13.044 65.342 124.839 1.00 85.11 ? 135 ASN C ND2 1 +ATOM 5791 N N . ILE C 1 137 ? 13.623 68.155 129.686 1.00 92.03 ? 136 ILE C N 1 +ATOM 5792 C CA . ILE C 1 137 ? 14.218 68.380 131.004 1.00 112.28 ? 136 ILE C CA 1 +ATOM 5793 C C . ILE C 1 137 ? 13.188 68.898 132.019 1.00 119.22 ? 136 ILE C C 1 +ATOM 5794 O O . ILE C 1 137 ? 12.739 68.150 132.897 1.00 80.85 ? 136 ILE C O 1 +ATOM 5795 C CB . ILE C 1 137 ? 15.428 69.359 130.955 1.00 95.58 ? 136 ILE C CB 1 +ATOM 5796 C CG1 . ILE C 1 137 ? 16.626 68.741 130.225 1.00 68.83 ? 136 ILE C CG1 1 +ATOM 5797 C CG2 . ILE C 1 137 ? 15.869 69.739 132.367 1.00 53.55 ? 136 ILE C CG2 1 +ATOM 5798 C CD1 . ILE C 1 137 ? 16.455 68.534 128.741 1.00 94.35 ? 136 ILE C CD1 1 +ATOM 5799 N N . LEU C 1 138 ? 12.802 70.168 131.875 1.00 94.12 ? 137 LEU C N 1 +ATOM 5800 C CA . LEU C 1 138 ? 11.960 70.850 132.856 1.00 98.84 ? 137 LEU C CA 1 +ATOM 5801 C C . LEU C 1 138 ? 10.581 70.253 132.976 1.00 109.24 ? 137 LEU C C 1 +ATOM 5802 O O . LEU C 1 138 ? 9.849 70.557 133.915 1.00 83.30 ? 137 LEU C O 1 +ATOM 5803 C CB . LEU C 1 138 ? 11.831 72.323 132.519 1.00 84.12 ? 137 LEU C CB 1 +ATOM 5804 C CG . LEU C 1 138 ? 13.100 73.088 132.845 1.00 98.55 ? 137 LEU C CG 1 +ATOM 5805 C CD1 . LEU C 1 138 ? 12.930 74.508 132.388 1.00 119.42 ? 137 LEU C CD1 1 +ATOM 5806 C CD2 . LEU C 1 138 ? 13.366 73.015 134.338 1.00 71.10 ? 137 LEU C CD2 1 +ATOM 5807 N N . GLY C 1 139 ? 10.231 69.409 132.014 1.00 80.18 ? 138 GLY C N 1 +ATOM 5808 C CA . GLY C 1 139 ? 8.982 68.682 132.065 1.00 87.71 ? 138 GLY C CA 1 +ATOM 5809 C C . GLY C 1 139 ? 9.119 67.349 132.775 1.00 110.57 ? 138 GLY C C 1 +ATOM 5810 O O . GLY C 1 139 ? 8.109 66.741 133.131 1.00 108.41 ? 138 GLY C O 1 +ATOM 5811 N N . HIS C 1 140 ? 10.363 66.905 132.978 1.00 108.09 ? 139 HIS C N 1 +ATOM 5812 C CA . HIS C 1 140 ? 10.668 65.595 133.572 1.00 102.12 ? 139 HIS C CA 1 +ATOM 5813 C C . HIS C 1 140 ? 10.113 64.400 132.757 1.00 87.01 ? 139 HIS C C 1 +ATOM 5814 O O . HIS C 1 140 ? 9.253 63.646 133.222 1.00 86.75 ? 139 HIS C O 1 +ATOM 5815 C CB . HIS C 1 140 ? 10.251 65.533 135.059 1.00 103.44 ? 139 HIS C CB 1 +ATOM 5816 C CG . HIS C 1 140 ? 11.122 66.347 135.972 1.00 112.34 ? 139 HIS C CG 1 +ATOM 5817 N ND1 . HIS C 1 140 ? 10.672 67.421 136.677 1.00 97.14 ? 139 HIS C ND1 1 +ATOM 5818 C CD2 . HIS C 1 140 ? 12.420 66.243 136.301 1.00 142.23 ? 139 HIS C CD2 1 +ATOM 5819 C CE1 . HIS C 1 140 ? 11.646 67.947 137.395 1.00 74.35 ? 139 HIS C CE1 1 +ATOM 5820 N NE2 . HIS C 1 140 ? 12.723 67.250 137.182 1.00 107.96 ? 139 HIS C NE2 1 +ATOM 5821 N N . LYS C 1 141 ? 10.622 64.238 131.536 1.00 110.61 ? 140 LYS C N 1 +ATOM 5822 C CA . LYS C 1 141 ? 10.248 63.115 130.669 1.00 112.25 ? 140 LYS C CA 1 +ATOM 5823 C C . LYS C 1 141 ? 11.447 62.199 130.387 1.00 115.93 ? 140 LYS C C 1 +ATOM 5824 O O . LYS C 1 141 ? 11.403 61.343 129.501 1.00 91.37 ? 140 LYS C O 1 +ATOM 5825 C CB . LYS C 1 141 ? 9.642 63.611 129.350 1.00 105.36 ? 140 LYS C CB 1 +ATOM 5826 C CG . LYS C 1 141 ? 8.331 64.369 129.482 1.00 108.34 ? 140 LYS C CG 1 +ATOM 5827 C CD . LYS C 1 141 ? 8.181 65.364 128.337 1.00 131.28 ? 140 LYS C CD 1 +ATOM 5828 C CE . LYS C 1 141 ? 6.884 66.161 128.425 1.00 125.13 ? 140 LYS C CE 1 +ATOM 5829 N NZ . LYS C 1 141 ? 6.744 67.170 127.331 1.00 137.49 ? 140 LYS C NZ 1 +ATOM 5830 N N . LEU C 1 142 ? 12.520 62.388 131.143 1.00 91.07 ? 141 LEU C N 1 +ATOM 5831 C CA . LEU C 1 142 ? 13.634 61.462 131.091 1.00 86.83 ? 141 LEU C CA 1 +ATOM 5832 C C . LEU C 1 142 ? 13.313 60.234 131.932 1.00 98.36 ? 141 LEU C C 1 +ATOM 5833 O O . LEU C 1 142 ? 12.732 60.347 133.017 1.00 87.98 ? 141 LEU C O 1 +ATOM 5834 C CB . LEU C 1 142 ? 14.912 62.132 131.585 1.00 86.42 ? 141 LEU C CB 1 +ATOM 5835 C CG . LEU C 1 142 ? 15.409 63.286 130.712 1.00 59.64 ? 141 LEU C CG 1 +ATOM 5836 C CD1 . LEU C 1 142 ? 16.593 63.980 131.334 1.00 74.36 ? 141 LEU C CD1 1 +ATOM 5837 C CD2 . LEU C 1 142 ? 15.765 62.801 129.336 1.00 81.01 ? 141 LEU C CD2 1 +ATOM 5838 N N . GLU C 1 143 ? 13.669 59.064 131.402 1.00 82.35 ? 142 GLU C N 1 +ATOM 5839 C CA . GLU C 1 143 ? 13.535 57.806 132.121 1.00 87.51 ? 142 GLU C CA 1 +ATOM 5840 C C . GLU C 1 143 ? 14.684 57.724 133.109 1.00 96.26 ? 142 GLU C C 1 +ATOM 5841 O O . GLU C 1 143 ? 15.799 58.162 132.805 1.00 92.14 ? 142 GLU C O 1 +ATOM 5842 C CB . GLU C 1 143 ? 13.604 56.611 131.160 1.00 81.53 ? 142 GLU C CB 1 +ATOM 5843 C CG . GLU C 1 143 ? 12.312 56.277 130.415 1.00 83.30 ? 142 GLU C CG 1 +ATOM 5844 C CD . GLU C 1 143 ? 12.394 54.962 129.624 1.00 121.06 ? 142 GLU C CD 1 +ATOM 5845 O OE1 . GLU C 1 143 ? 13.516 54.533 129.261 1.00 115.74 ? 142 GLU C OE1 1 +ATOM 5846 O OE2 . GLU C 1 143 ? 11.329 54.354 129.370 1.00 109.19 ? 142 GLU C OE2 1 +ATOM 5847 N N . TYR C 1 144 ? 14.417 57.172 134.289 1.00 64.61 ? 143 TYR C N 1 +ATOM 5848 C CA . TYR C 1 144 ? 15.465 56.992 135.290 1.00 71.11 ? 143 TYR C CA 1 +ATOM 5849 C C . TYR C 1 144 ? 16.515 55.955 134.893 1.00 85.14 ? 143 TYR C C 1 +ATOM 5850 O O . TYR C 1 144 ? 16.658 54.934 135.563 1.00 68.38 ? 143 TYR C O 1 +ATOM 5851 C CB . TYR C 1 144 ? 14.882 56.594 136.650 1.00 67.11 ? 143 TYR C CB 1 +ATOM 5852 C CG . TYR C 1 144 ? 15.839 56.882 137.790 1.00 73.13 ? 143 TYR C CG 1 +ATOM 5853 C CD1 . TYR C 1 144 ? 16.791 57.885 137.670 1.00 92.89 ? 143 TYR C CD1 1 +ATOM 5854 C CD2 . TYR C 1 144 ? 15.806 56.154 138.966 1.00 84.04 ? 143 TYR C CD2 1 +ATOM 5855 C CE1 . TYR C 1 144 ? 17.669 58.166 138.682 1.00 81.37 ? 143 TYR C CE1 1 +ATOM 5856 C CE2 . TYR C 1 144 ? 16.694 56.426 139.988 1.00 75.87 ? 143 TYR C CE2 1 +ATOM 5857 C CZ . TYR C 1 144 ? 17.621 57.438 139.836 1.00 85.42 ? 143 TYR C CZ 1 +ATOM 5858 O OH . TYR C 1 144 ? 18.507 57.740 140.837 1.00 78.26 ? 143 TYR C OH 1 +ATOM 5859 N N . ASN C 1 145 ? 17.257 56.203 133.823 1.00 70.98 ? 144 ASN C N 1 +ATOM 5860 C CA . ASN C 1 145 ? 18.298 55.255 133.451 1.00 72.02 ? 144 ASN C CA 1 +ATOM 5861 C C . ASN C 1 145 ? 19.516 55.857 132.768 1.00 53.18 ? 144 ASN C C 1 +ATOM 5862 O O . ASN C 1 145 ? 19.726 57.065 132.802 1.00 75.33 ? 144 ASN C O 1 +ATOM 5863 C CB . ASN C 1 145 ? 17.728 54.091 132.641 1.00 46.42 ? 144 ASN C CB 1 +ATOM 5864 C CG . ASN C 1 145 ? 17.037 54.532 131.382 1.00 97.97 ? 144 ASN C CG 1 +ATOM 5865 O OD1 . ASN C 1 145 ? 17.611 55.229 130.541 1.00 69.45 ? 144 ASN C OD1 1 +ATOM 5866 N ND2 . ASN C 1 145 ? 15.802 54.089 131.219 1.00 88.91 ? 144 ASN C ND2 1 +ATOM 5867 N N . TYR C 1 146 ? 20.335 54.995 132.179 1.00 73.32 ? 145 TYR C N 1 +ATOM 5868 C CA . TYR C 1 146 ? 21.541 55.450 131.510 1.00 89.10 ? 145 TYR C CA 1 +ATOM 5869 C C . TYR C 1 146 ? 22.012 54.482 130.421 1.00 78.54 ? 145 TYR C C 1 +ATOM 5870 O O . TYR C 1 146 ? 21.585 53.326 130.382 1.00 83.90 ? 145 TYR C O 1 +ATOM 5871 C CB . TYR C 1 146 ? 22.637 55.727 132.535 1.00 55.30 ? 145 TYR C CB 1 +ATOM 5872 C CG . TYR C 1 146 ? 23.290 57.054 132.304 1.00 70.73 ? 145 TYR C CG 1 +ATOM 5873 C CD1 . TYR C 1 146 ? 22.624 58.238 132.595 1.00 67.01 ? 145 TYR C CD1 1 +ATOM 5874 C CD2 . TYR C 1 146 ? 24.560 57.130 131.767 1.00 97.11 ? 145 TYR C CD2 1 +ATOM 5875 C CE1 . TYR C 1 146 ? 23.221 59.463 132.365 1.00 80.90 ? 145 TYR C CE1 1 +ATOM 5876 C CE2 . TYR C 1 146 ? 25.163 58.344 131.536 1.00 85.33 ? 145 TYR C CE2 1 +ATOM 5877 C CZ . TYR C 1 146 ? 24.495 59.503 131.835 1.00 62.41 ? 145 TYR C CZ 1 +ATOM 5878 O OH . TYR C 1 146 ? 25.126 60.690 131.595 1.00 69.76 ? 145 TYR C OH 1 +ATOM 5879 N N . ASN C 1 147 ? 22.853 54.979 129.516 1.00 95.21 ? 146 ASN C N 1 +ATOM 5880 C CA . ASN C 1 147 ? 23.408 54.178 128.426 1.00 69.56 ? 146 ASN C CA 1 +ATOM 5881 C C . ASN C 1 147 ? 24.906 54.315 128.480 1.00 84.08 ? 146 ASN C C 1 +ATOM 5882 O O . ASN C 1 147 ? 25.432 55.079 129.291 1.00 79.82 ? 146 ASN C O 1 +ATOM 5883 C CB . ASN C 1 147 ? 22.937 54.664 127.052 1.00 81.52 ? 146 ASN C CB 1 +ATOM 5884 C CG . ASN C 1 147 ? 21.443 54.551 126.865 1.00 73.95 ? 146 ASN C CG 1 +ATOM 5885 O OD1 . ASN C 1 147 ? 20.842 53.528 127.179 1.00 78.41 ? 146 ASN C OD1 1 +ATOM 5886 N ND2 . ASN C 1 147 ? 20.832 55.613 126.352 1.00 120.39 ? 146 ASN C ND2 1 +ATOM 5887 N N . SER C 1 148 ? 25.595 53.592 127.604 1.00 84.81 ? 147 SER C N 1 +ATOM 5888 C CA . SER C 1 148 ? 27.049 53.555 127.652 1.00 73.75 ? 147 SER C CA 1 +ATOM 5889 C C . SER C 1 148 ? 27.625 54.405 126.533 1.00 55.80 ? 147 SER C C 1 +ATOM 5890 O O . SER C 1 148 ? 27.036 54.496 125.461 1.00 120.13 ? 147 SER C O 1 +ATOM 5891 C CB . SER C 1 148 ? 27.560 52.113 127.615 1.00 61.96 ? 147 SER C CB 1 +ATOM 5892 O OG . SER C 1 148 ? 27.250 51.432 128.825 1.00 92.14 ? 147 SER C OG 1 +ATOM 5893 N N . HIS C 1 149 ? 28.758 55.050 126.795 1.00 66.30 ? 148 HIS C N 1 +ATOM 5894 C CA . HIS C 1 149 ? 29.278 56.068 125.888 1.00 88.39 ? 148 HIS C CA 1 +ATOM 5895 C C . HIS C 1 149 ? 30.796 56.004 125.771 1.00 87.93 ? 148 HIS C C 1 +ATOM 5896 O O . HIS C 1 149 ? 31.476 55.518 126.667 1.00 94.70 ? 148 HIS C O 1 +ATOM 5897 C CB . HIS C 1 149 ? 28.845 57.463 126.363 1.00 69.61 ? 148 HIS C CB 1 +ATOM 5898 C CG . HIS C 1 149 ? 27.361 57.625 126.481 1.00 79.04 ? 148 HIS C CG 1 +ATOM 5899 N ND1 . HIS C 1 149 ? 26.730 57.876 127.679 1.00 83.96 ? 148 HIS C ND1 1 +ATOM 5900 C CD2 . HIS C 1 149 ? 26.379 57.546 125.550 1.00 124.25 ? 148 HIS C CD2 1 +ATOM 5901 C CE1 . HIS C 1 149 ? 25.430 57.952 127.479 1.00 100.19 ? 148 HIS C CE1 1 +ATOM 5902 N NE2 . HIS C 1 149 ? 25.187 57.751 126.198 1.00 71.29 ? 148 HIS C NE2 1 +ATOM 5903 N N . ASN C 1 150 ? 31.332 56.492 124.662 1.00 81.91 ? 149 ASN C N 1 +ATOM 5904 C CA . ASN C 1 150 ? 32.777 56.568 124.528 1.00 91.24 ? 149 ASN C CA 1 +ATOM 5905 C C . ASN C 1 150 ? 33.213 58.031 124.635 1.00 76.55 ? 149 ASN C C 1 +ATOM 5906 O O . ASN C 1 150 ? 32.719 58.887 123.909 1.00 97.57 ? 149 ASN C O 1 +ATOM 5907 C CB . ASN C 1 150 ? 33.247 55.913 123.219 1.00 104.50 ? 149 ASN C CB 1 +ATOM 5908 C CG . ASN C 1 150 ? 32.867 54.423 123.123 1.00 98.79 ? 149 ASN C CG 1 +ATOM 5909 O OD1 . ASN C 1 150 ? 33.191 53.622 124.004 1.00 123.18 ? 149 ASN C OD1 1 +ATOM 5910 N ND2 . ASN C 1 150 ? 32.177 54.056 122.042 1.00 110.38 ? 149 ASN C ND2 1 +ATOM 5911 N N . VAL C 1 151 ? 34.119 58.302 125.569 1.00 93.11 ? 150 VAL C N 1 +ATOM 5912 C CA . VAL C 1 151 ? 34.522 59.659 125.942 1.00 66.46 ? 150 VAL C CA 1 +ATOM 5913 C C . VAL C 1 151 ? 35.835 60.023 125.244 1.00 103.73 ? 150 VAL C C 1 +ATOM 5914 O O . VAL C 1 151 ? 36.910 59.696 125.741 1.00 111.59 ? 150 VAL C O 1 +ATOM 5915 C CB . VAL C 1 151 ? 34.672 59.756 127.512 1.00 101.92 ? 150 VAL C CB 1 +ATOM 5916 C CG1 . VAL C 1 151 ? 35.495 60.966 127.976 1.00 62.64 ? 150 VAL C CG1 1 +ATOM 5917 C CG2 . VAL C 1 151 ? 33.310 59.757 128.188 1.00 79.85 ? 150 VAL C CG2 1 +ATOM 5918 N N . TYR C 1 152 ? 35.770 60.686 124.090 1.00 85.93 ? 151 TYR C N 1 +ATOM 5919 C CA . TYR C 1 152 ? 37.004 60.943 123.331 1.00 89.71 ? 151 TYR C CA 1 +ATOM 5920 C C . TYR C 1 152 ? 37.874 62.078 123.879 1.00 88.25 ? 151 TYR C C 1 +ATOM 5921 O O . TYR C 1 152 ? 37.404 63.174 124.148 1.00 93.75 ? 151 TYR C O 1 +ATOM 5922 C CB . TYR C 1 152 ? 36.736 61.100 121.829 1.00 82.10 ? 151 TYR C CB 1 +ATOM 5923 C CG . TYR C 1 152 ? 35.891 59.977 121.272 1.00 91.74 ? 151 TYR C CG 1 +ATOM 5924 C CD1 . TYR C 1 152 ? 34.507 60.065 121.295 1.00 78.88 ? 151 TYR C CD1 1 +ATOM 5925 C CD2 . TYR C 1 152 ? 36.468 58.825 120.740 1.00 93.62 ? 151 TYR C CD2 1 +ATOM 5926 C CE1 . TYR C 1 152 ? 33.710 59.043 120.799 1.00 123.38 ? 151 TYR C CE1 1 +ATOM 5927 C CE2 . TYR C 1 152 ? 35.672 57.788 120.237 1.00 86.88 ? 151 TYR C CE2 1 +ATOM 5928 C CZ . TYR C 1 152 ? 34.290 57.907 120.273 1.00 108.77 ? 151 TYR C CZ 1 +ATOM 5929 O OH . TYR C 1 152 ? 33.466 56.907 119.792 1.00 85.86 ? 151 TYR C OH 1 +ATOM 5930 N N . ILE C 1 153 ? 39.155 61.780 124.054 1.00 88.13 ? 152 ILE C N 1 +ATOM 5931 C CA . ILE C 1 153 ? 40.117 62.720 124.614 1.00 96.52 ? 152 ILE C CA 1 +ATOM 5932 C C . ILE C 1 153 ? 41.148 63.067 123.540 1.00 119.47 ? 152 ILE C C 1 +ATOM 5933 O O . ILE C 1 153 ? 41.294 62.351 122.547 1.00 118.80 ? 152 ILE C O 1 +ATOM 5934 C CB . ILE C 1 153 ? 40.791 62.119 125.868 1.00 86.93 ? 152 ILE C CB 1 +ATOM 5935 C CG1 . ILE C 1 153 ? 39.722 61.613 126.832 1.00 63.44 ? 152 ILE C CG1 1 +ATOM 5936 C CG2 . ILE C 1 153 ? 41.700 63.121 126.571 1.00 73.21 ? 152 ILE C CG2 1 +ATOM 5937 C CD1 . ILE C 1 153 ? 40.293 60.949 128.029 1.00 110.68 ? 152 ILE C CD1 1 +ATOM 5938 N N . MET C 1 154 ? 41.841 64.181 123.736 1.00 126.89 ? 153 MET C N 1 +ATOM 5939 C CA . MET C 1 154 ? 42.757 64.708 122.750 1.00 130.69 ? 153 MET C CA 1 +ATOM 5940 C C . MET C 1 154 ? 43.603 65.724 123.485 1.00 114.99 ? 153 MET C C 1 +ATOM 5941 O O . MET C 1 154 ? 43.086 66.497 124.289 1.00 118.01 ? 153 MET C O 1 +ATOM 5942 C CB . MET C 1 154 ? 41.961 65.386 121.638 1.00 131.96 ? 153 MET C CB 1 +ATOM 5943 C CG . MET C 1 154 ? 42.737 65.654 120.373 1.00 148.01 ? 153 MET C CG 1 +ATOM 5944 S SD . MET C 1 154 ? 41.710 66.366 119.093 1.00 212.97 ? 153 MET C SD 1 +ATOM 5945 C CE . MET C 1 154 ? 40.218 65.452 119.259 1.00 106.55 ? 153 MET C CE 1 +ATOM 5946 N N . ALA C 1 155 ? 44.905 65.714 123.244 1.00 108.73 ? 154 ALA C N 1 +ATOM 5947 C CA . ALA C 1 155 ? 45.771 66.658 123.928 1.00 115.66 ? 154 ALA C CA 1 +ATOM 5948 C C . ALA C 1 155 ? 45.561 68.070 123.401 1.00 142.04 ? 154 ALA C C 1 +ATOM 5949 O O . ALA C 1 155 ? 45.252 68.274 122.222 1.00 119.63 ? 154 ALA C O 1 +ATOM 5950 C CB . ALA C 1 155 ? 47.226 66.253 123.795 1.00 95.61 ? 154 ALA C CB 1 +ATOM 5951 N N . ASP C 1 156 ? 45.706 69.037 124.300 1.00 148.99 ? 155 ASP C N 1 +ATOM 5952 C CA . ASP C 1 156 ? 45.755 70.445 123.938 1.00 169.35 ? 155 ASP C CA 1 +ATOM 5953 C C . ASP C 1 156 ? 47.104 70.987 124.410 1.00 187.23 ? 155 ASP C C 1 +ATOM 5954 O O . ASP C 1 156 ? 47.214 71.590 125.485 1.00 147.51 ? 155 ASP C O 1 +ATOM 5955 C CB . ASP C 1 156 ? 44.586 71.203 124.568 1.00 163.44 ? 155 ASP C CB 1 +ATOM 5956 C CG . ASP C 1 156 ? 44.508 72.644 124.111 1.00 167.00 ? 155 ASP C CG 1 +ATOM 5957 O OD1 . ASP C 1 156 ? 45.345 73.061 123.279 1.00 175.97 ? 155 ASP C OD1 1 +ATOM 5958 O OD2 . ASP C 1 156 ? 43.597 73.356 124.581 1.00 136.01 ? 155 ASP C OD2 1 +ATOM 5959 N N . LYS C 1 157 ? 48.127 70.748 123.590 1.00 203.39 ? 156 LYS C N 1 +ATOM 5960 C CA . LYS C 1 157 ? 49.516 70.990 123.969 1.00 191.15 ? 156 LYS C CA 1 +ATOM 5961 C C . LYS C 1 157 ? 49.794 72.459 124.244 1.00 169.48 ? 156 LYS C C 1 +ATOM 5962 O O . LYS C 1 157 ? 50.682 72.798 125.028 1.00 130.91 ? 156 LYS C O 1 +ATOM 5963 C CB . LYS C 1 157 ? 50.477 70.422 122.911 1.00 182.41 ? 156 LYS C CB 1 +ATOM 5964 C CG . LYS C 1 157 ? 50.752 68.924 123.090 1.00 184.15 ? 156 LYS C CG 1 +ATOM 5965 C CD . LYS C 1 157 ? 51.507 68.308 121.920 1.00 173.80 ? 156 LYS C CD 1 +ATOM 5966 C CE . LYS C 1 157 ? 51.994 66.893 122.250 1.00 168.61 ? 156 LYS C CE 1 +ATOM 5967 N NZ . LYS C 1 157 ? 50.893 65.914 122.486 1.00 160.79 ? 156 LYS C NZ 1 +ATOM 5968 N N . GLN C 1 158 ? 49.011 73.330 123.618 1.00 186.12 ? 157 GLN C N 1 +ATOM 5969 C CA . GLN C 1 158 ? 49.181 74.759 123.823 1.00 187.63 ? 157 GLN C CA 1 +ATOM 5970 C C . GLN C 1 158 ? 48.642 75.206 125.186 1.00 171.60 ? 157 GLN C C 1 +ATOM 5971 O O . GLN C 1 158 ? 49.216 76.093 125.817 1.00 151.49 ? 157 GLN C O 1 +ATOM 5972 C CB . GLN C 1 158 ? 48.565 75.567 122.669 1.00 182.31 ? 157 GLN C CB 1 +ATOM 5973 C CG . GLN C 1 158 ? 49.229 75.348 121.291 1.00 201.41 ? 157 GLN C CG 1 +ATOM 5974 C CD . GLN C 1 158 ? 50.652 75.920 121.174 1.00 205.59 ? 157 GLN C CD 1 +ATOM 5975 O OE1 . GLN C 1 158 ? 51.558 75.544 121.919 1.00 212.58 ? 157 GLN C OE1 1 +ATOM 5976 N NE2 . GLN C 1 158 ? 50.846 76.820 120.217 1.00 186.82 ? 157 GLN C NE2 1 +ATOM 5977 N N . LYS C 1 159 ? 47.562 74.582 125.654 1.00 178.59 ? 158 LYS C N 1 +ATOM 5978 C CA . LYS C 1 159 ? 46.957 74.996 126.926 1.00 162.20 ? 158 LYS C CA 1 +ATOM 5979 C C . LYS C 1 159 ? 47.344 74.090 128.101 1.00 152.53 ? 158 LYS C C 1 +ATOM 5980 O O . LYS C 1 159 ? 46.831 74.247 129.213 1.00 114.70 ? 158 LYS C O 1 +ATOM 5981 C CB . LYS C 1 159 ? 45.432 75.130 126.807 1.00 136.89 ? 158 LYS C CB 1 +ATOM 5982 C CG . LYS C 1 159 ? 44.963 75.995 125.628 1.00 187.18 ? 158 LYS C CG 1 +ATOM 5983 C CD . LYS C 1 159 ? 45.842 77.232 125.413 1.00 199.77 ? 158 LYS C CD 1 +ATOM 5984 C CE . LYS C 1 159 ? 45.928 77.607 123.932 1.00 175.98 ? 158 LYS C CE 1 +ATOM 5985 N NZ . LYS C 1 159 ? 47.037 78.565 123.640 1.00 170.56 ? 158 LYS C NZ 1 +ATOM 5986 N N . ASN C 1 160 ? 48.255 73.152 127.842 1.00 151.59 ? 159 ASN C N 1 +ATOM 5987 C CA . ASN C 1 160 ? 48.798 72.265 128.875 1.00 153.53 ? 159 ASN C CA 1 +ATOM 5988 C C . ASN C 1 160 ? 47.700 71.453 129.571 1.00 141.41 ? 159 ASN C C 1 +ATOM 5989 O O . ASN C 1 160 ? 47.783 71.145 130.759 1.00 126.44 ? 159 ASN C O 1 +ATOM 5990 C CB . ASN C 1 160 ? 49.634 73.067 129.887 1.00 150.42 ? 159 ASN C CB 1 +ATOM 5991 C CG . ASN C 1 160 ? 50.530 72.187 130.756 1.00 167.25 ? 159 ASN C CG 1 +ATOM 5992 O OD1 . ASN C 1 160 ? 51.079 71.183 130.297 1.00 161.87 ? 159 ASN C OD1 1 +ATOM 5993 N ND2 . ASN C 1 160 ? 50.674 72.565 132.024 1.00 153.36 ? 159 ASN C ND2 1 +ATOM 5994 N N . GLY C 1 161 ? 46.666 71.106 128.818 1.00 128.97 ? 160 GLY C N 1 +ATOM 5995 C CA . GLY C 1 161 ? 45.550 70.375 129.379 1.00 126.63 ? 160 GLY C CA 1 +ATOM 5996 C C . GLY C 1 161 ? 45.023 69.398 128.359 1.00 116.88 ? 160 GLY C C 1 +ATOM 5997 O O . GLY C 1 161 ? 45.782 68.917 127.523 1.00 120.21 ? 160 GLY C O 1 +ATOM 5998 N N . ILE C 1 162 ? 43.732 69.096 128.424 1.00 115.88 ? 161 ILE C N 1 +ATOM 5999 C CA . ILE C 1 162 ? 43.116 68.205 127.447 1.00 116.76 ? 161 ILE C CA 1 +ATOM 6000 C C . ILE C 1 162 ? 41.790 68.773 126.955 1.00 109.46 ? 161 ILE C C 1 +ATOM 6001 O O . ILE C 1 162 ? 41.123 69.518 127.670 1.00 105.91 ? 161 ILE C O 1 +ATOM 6002 C CB . ILE C 1 162 ? 42.880 66.771 128.007 1.00 114.01 ? 161 ILE C CB 1 +ATOM 6003 C CG1 . ILE C 1 162 ? 41.858 66.782 129.143 1.00 120.18 ? 161 ILE C CG1 1 +ATOM 6004 C CG2 . ILE C 1 162 ? 44.181 66.134 128.485 1.00 120.21 ? 161 ILE C CG2 1 +ATOM 6005 C CD1 . ILE C 1 162 ? 41.445 65.401 129.599 1.00 81.92 ? 161 ILE C CD1 1 +ATOM 6006 N N . LYS C 1 163 ? 41.424 68.435 125.725 1.00 103.24 ? 162 LYS C N 1 +ATOM 6007 C CA . LYS C 1 163 ? 40.101 68.755 125.210 1.00 103.37 ? 162 LYS C CA 1 +ATOM 6008 C C . LYS C 1 163 ? 39.315 67.472 125.309 1.00 110.11 ? 162 LYS C C 1 +ATOM 6009 O O . LYS C 1 163 ? 39.876 66.395 125.181 1.00 122.16 ? 162 LYS C O 1 +ATOM 6010 C CB . LYS C 1 163 ? 40.171 69.221 123.752 1.00 127.58 ? 162 LYS C CB 1 +ATOM 6011 C CG . LYS C 1 163 ? 39.639 70.636 123.518 1.00 163.71 ? 162 LYS C CG 1 +ATOM 6012 C CD . LYS C 1 163 ? 39.994 71.174 122.132 1.00 163.37 ? 162 LYS C CD 1 +ATOM 6013 C CE . LYS C 1 163 ? 39.739 72.684 122.016 1.00 162.16 ? 162 LYS C CE 1 +ATOM 6014 N NZ . LYS C 1 163 ? 40.575 73.517 122.936 1.00 158.62 ? 162 LYS C NZ 1 +ATOM 6015 N N . VAL C 1 164 ? 38.021 67.560 125.566 1.00 90.22 ? 163 VAL C N 1 +ATOM 6016 C CA . VAL C 1 164 ? 37.234 66.344 125.677 1.00 94.45 ? 163 VAL C CA 1 +ATOM 6017 C C . VAL C 1 164 ? 35.898 66.529 124.978 1.00 77.47 ? 163 VAL C C 1 +ATOM 6018 O O . VAL C 1 164 ? 35.270 67.578 125.101 1.00 114.39 ? 163 VAL C O 1 +ATOM 6019 C CB . VAL C 1 164 ? 36.973 65.955 127.164 1.00 117.38 ? 163 VAL C CB 1 +ATOM 6020 C CG1 . VAL C 1 164 ? 36.330 64.579 127.258 1.00 77.81 ? 163 VAL C CG1 1 +ATOM 6021 C CG2 . VAL C 1 164 ? 38.252 65.999 127.999 1.00 107.10 ? 163 VAL C CG2 1 +ATOM 6022 N N . ASN C 1 165 ? 35.440 65.516 124.257 1.00 80.62 ? 164 ASN C N 1 +ATOM 6023 C CA . ASN C 1 165 ? 34.092 65.607 123.722 1.00 95.85 ? 164 ASN C CA 1 +ATOM 6024 C C . ASN C 1 165 ? 33.371 64.280 123.539 1.00 83.91 ? 164 ASN C C 1 +ATOM 6025 O O . ASN C 1 165 ? 33.993 63.250 123.291 1.00 109.35 ? 164 ASN C O 1 +ATOM 6026 C CB . ASN C 1 165 ? 34.091 66.423 122.434 1.00 92.78 ? 164 ASN C CB 1 +ATOM 6027 C CG . ASN C 1 165 ? 34.906 65.785 121.349 1.00 121.50 ? 164 ASN C CG 1 +ATOM 6028 O OD1 . ASN C 1 165 ? 36.123 65.622 121.476 1.00 140.23 ? 164 ASN C OD1 1 +ATOM 6029 N ND2 . ASN C 1 165 ? 34.244 65.423 120.258 1.00 157.37 ? 164 ASN C ND2 1 +ATOM 6030 N N . PHE C 1 166 ? 32.050 64.328 123.677 1.00 61.92 ? 165 PHE C N 1 +ATOM 6031 C CA . PHE C 1 166 ? 31.198 63.152 123.556 1.00 91.83 ? 165 PHE C CA 1 +ATOM 6032 C C . PHE C 1 166 ? 29.732 63.528 123.540 1.00 68.14 ? 165 PHE C C 1 +ATOM 6033 O O . PHE C 1 166 ? 29.384 64.699 123.627 1.00 104.90 ? 165 PHE C O 1 +ATOM 6034 C CB . PHE C 1 166 ? 31.455 62.159 124.686 1.00 98.12 ? 165 PHE C CB 1 +ATOM 6035 C CG . PHE C 1 166 ? 31.393 62.756 126.066 1.00 98.13 ? 165 PHE C CG 1 +ATOM 6036 C CD1 . PHE C 1 166 ? 32.479 63.451 126.592 1.00 80.65 ? 165 PHE C CD1 1 +ATOM 6037 C CD2 . PHE C 1 166 ? 30.275 62.568 126.857 1.00 46.69 ? 165 PHE C CD2 1 +ATOM 6038 C CE1 . PHE C 1 166 ? 32.441 63.973 127.864 1.00 63.61 ? 165 PHE C CE1 1 +ATOM 6039 C CE2 . PHE C 1 166 ? 30.228 63.081 128.124 1.00 74.97 ? 165 PHE C CE2 1 +ATOM 6040 C CZ . PHE C 1 166 ? 31.318 63.789 128.632 1.00 86.65 ? 165 PHE C CZ 1 +ATOM 6041 N N . LYS C 1 167 ? 28.870 62.525 123.461 1.00 73.44 ? 166 LYS C N 1 +ATOM 6042 C CA . LYS C 1 167 ? 27.460 62.778 123.221 1.00 95.88 ? 166 LYS C CA 1 +ATOM 6043 C C . LYS C 1 167 ? 26.553 61.798 123.958 1.00 102.47 ? 166 LYS C C 1 +ATOM 6044 O O . LYS C 1 167 ? 26.379 60.648 123.546 1.00 97.13 ? 166 LYS C O 1 +ATOM 6045 C CB . LYS C 1 167 ? 27.191 62.740 121.719 1.00 67.03 ? 166 LYS C CB 1 +ATOM 6046 C CG . LYS C 1 167 ? 25.733 62.866 121.324 1.00 122.61 ? 166 LYS C CG 1 +ATOM 6047 C CD . LYS C 1 167 ? 25.560 62.520 119.849 1.00 147.89 ? 166 LYS C CD 1 +ATOM 6048 C CE . LYS C 1 167 ? 26.636 63.173 118.974 1.00 123.14 ? 166 LYS C CE 1 +ATOM 6049 N NZ . LYS C 1 167 ? 26.531 64.658 118.960 1.00 159.51 ? 166 LYS C NZ 1 +ATOM 6050 N N . ILE C 1 168 ? 25.965 62.276 125.046 1.00 84.70 ? 167 ILE C N 1 +ATOM 6051 C CA . ILE C 1 168 ? 25.128 61.444 125.894 1.00 91.63 ? 167 ILE C CA 1 +ATOM 6052 C C . ILE C 1 168 ? 23.724 61.269 125.341 1.00 84.74 ? 167 ILE C C 1 +ATOM 6053 O O . ILE C 1 168 ? 23.060 62.233 124.977 1.00 83.03 ? 167 ILE C O 1 +ATOM 6054 C CB . ILE C 1 168 ? 24.986 62.061 127.280 1.00 73.39 ? 167 ILE C CB 1 +ATOM 6055 C CG1 . ILE C 1 168 ? 26.360 62.371 127.872 1.00 89.96 ? 167 ILE C CG1 1 +ATOM 6056 C CG2 . ILE C 1 168 ? 24.163 61.163 128.177 1.00 75.51 ? 167 ILE C CG2 1 +ATOM 6057 C CD1 . ILE C 1 168 ? 27.156 61.177 128.263 1.00 109.91 ? 167 ILE C CD1 1 +ATOM 6058 N N . ARG C 1 169 ? 23.261 60.032 125.302 1.00 63.13 ? 168 ARG C N 1 +ATOM 6059 C CA . ARG C 1 169 ? 21.904 59.768 124.883 1.00 76.34 ? 168 ARG C CA 1 +ATOM 6060 C C . ARG C 1 169 ? 21.029 59.512 126.104 1.00 73.47 ? 168 ARG C C 1 +ATOM 6061 O O . ARG C 1 169 ? 21.248 58.537 126.817 1.00 96.94 ? 168 ARG C O 1 +ATOM 6062 C CB . ARG C 1 169 ? 21.885 58.556 123.951 1.00 90.37 ? 168 ARG C CB 1 +ATOM 6063 C CG . ARG C 1 169 ? 22.672 58.754 122.662 1.00 101.34 ? 168 ARG C CG 1 +ATOM 6064 C CD . ARG C 1 169 ? 22.552 57.554 121.711 1.00 98.57 ? 168 ARG C CD 1 +ATOM 6065 N NE . ARG C 1 169 ? 23.278 56.387 122.210 1.00 115.25 ? 168 ARG C NE 1 +ATOM 6066 C CZ . ARG C 1 169 ? 24.605 56.279 122.233 1.00 138.93 ? 168 ARG C CZ 1 +ATOM 6067 N NH1 . ARG C 1 169 ? 25.368 57.269 121.784 1.00 114.74 ? 168 ARG C NH1 1 +ATOM 6068 N NH2 . ARG C 1 169 ? 25.175 55.181 122.712 1.00 131.43 ? 168 ARG C NH2 1 +ATOM 6069 N N . HIS C 1 170 ? 20.047 60.379 126.354 1.00 71.53 ? 169 HIS C N 1 +ATOM 6070 C CA . HIS C 1 170 ? 19.077 60.118 127.423 1.00 89.08 ? 169 HIS C CA 1 +ATOM 6071 C C . HIS C 1 170 ? 17.822 59.462 126.875 1.00 62.49 ? 169 HIS C C 1 +ATOM 6072 O O . HIS C 1 170 ? 17.283 59.902 125.875 1.00 107.95 ? 169 HIS C O 1 +ATOM 6073 C CB . HIS C 1 170 ? 18.685 61.398 128.161 1.00 68.09 ? 169 HIS C CB 1 +ATOM 6074 C CG . HIS C 1 170 ? 19.837 62.131 128.767 1.00 80.45 ? 169 HIS C CG 1 +ATOM 6075 N ND1 . HIS C 1 170 ? 20.246 61.935 130.067 1.00 94.00 ? 169 HIS C ND1 1 +ATOM 6076 C CD2 . HIS C 1 170 ? 20.667 63.067 128.249 1.00 101.06 ? 169 HIS C CD2 1 +ATOM 6077 C CE1 . HIS C 1 170 ? 21.281 62.716 130.324 1.00 89.38 ? 169 HIS C CE1 1 +ATOM 6078 N NE2 . HIS C 1 170 ? 21.557 63.411 129.236 1.00 61.78 ? 169 HIS C NE2 1 +ATOM 6079 N N . ASN C 1 171 ? 17.356 58.409 127.533 1.00 114.58 ? 170 ASN C N 1 +ATOM 6080 C CA . ASN C 1 171 ? 16.103 57.773 127.155 1.00 86.54 ? 170 ASN C CA 1 +ATOM 6081 C C . ASN C 1 171 ? 14.917 58.573 127.677 1.00 102.24 ? 170 ASN C C 1 +ATOM 6082 O O . ASN C 1 171 ? 14.985 59.120 128.778 1.00 120.29 ? 170 ASN C O 1 +ATOM 6083 C CB . ASN C 1 171 ? 16.039 56.358 127.729 1.00 105.01 ? 170 ASN C CB 1 +ATOM 6084 C CG . ASN C 1 171 ? 16.862 55.371 126.943 1.00 103.06 ? 170 ASN C CG 1 +ATOM 6085 O OD1 . ASN C 1 171 ? 17.796 55.748 126.235 1.00 100.33 ? 170 ASN C OD1 1 +ATOM 6086 N ND2 . ASN C 1 171 ? 16.516 54.089 127.055 1.00 100.07 ? 170 ASN C ND2 1 +ATOM 6087 N N . ILE C 1 172 ? 13.836 58.604 126.890 1.00 98.30 ? 171 ILE C N 1 +ATOM 6088 C CA . ILE C 1 172 ? 12.577 59.297 127.201 1.00 97.04 ? 171 ILE C CA 1 +ATOM 6089 C C . ILE C 1 172 ? 11.476 58.237 127.124 1.00 116.14 ? 171 ILE C C 1 +ATOM 6090 O O . ILE C 1 172 ? 11.716 57.186 126.533 1.00 151.00 ? 171 ILE C O 1 +ATOM 6091 C CB . ILE C 1 172 ? 12.348 60.418 126.166 1.00 93.22 ? 171 ILE C CB 1 +ATOM 6092 C CG1 . ILE C 1 172 ? 13.509 61.411 126.235 1.00 90.23 ? 171 ILE C CG1 1 +ATOM 6093 C CG2 . ILE C 1 172 ? 11.034 61.143 126.381 1.00 75.71 ? 171 ILE C CG2 1 +ATOM 6094 C CD1 . ILE C 1 172 ? 13.668 62.250 125.010 1.00 102.73 ? 171 ILE C CD1 1 +ATOM 6095 N N . GLU C 1 173 ? 10.293 58.457 127.709 1.00 73.25 ? 172 GLU C N 1 +ATOM 6096 C CA . GLU C 1 173 ? 9.301 57.367 127.719 1.00 130.38 ? 172 GLU C CA 1 +ATOM 6097 C C . GLU C 1 173 ? 8.756 56.927 126.345 1.00 138.49 ? 172 GLU C C 1 +ATOM 6098 O O . GLU C 1 173 ? 8.633 55.731 126.081 1.00 148.16 ? 172 GLU C O 1 +ATOM 6099 C CB . GLU C 1 173 ? 8.154 57.581 128.718 1.00 109.52 ? 172 GLU C CB 1 +ATOM 6100 C CG . GLU C 1 173 ? 7.424 56.250 128.992 1.00 162.39 ? 172 GLU C CG 1 +ATOM 6101 C CD . GLU C 1 173 ? 6.227 56.345 129.934 1.00 202.30 ? 172 GLU C CD 1 +ATOM 6102 O OE1 . GLU C 1 173 ? 5.473 57.334 129.860 1.00 182.06 ? 172 GLU C OE1 1 +ATOM 6103 O OE2 . GLU C 1 173 ? 6.032 55.410 130.743 1.00 216.84 ? 172 GLU C OE2 1 +ATOM 6104 N N . ASP C 1 174 ? 8.453 57.872 125.464 1.00 101.58 ? 173 ASP C N 1 +ATOM 6105 C CA . ASP C 1 174 ? 7.898 57.521 124.155 1.00 125.25 ? 173 ASP C CA 1 +ATOM 6106 C C . ASP C 1 174 ? 8.873 56.791 123.209 1.00 149.14 ? 173 ASP C C 1 +ATOM 6107 O O . ASP C 1 174 ? 8.587 56.617 122.023 1.00 207.54 ? 173 ASP C O 1 +ATOM 6108 C CB . ASP C 1 174 ? 7.342 58.771 123.473 1.00 142.57 ? 173 ASP C CB 1 +ATOM 6109 C CG . ASP C 1 174 ? 8.353 59.901 123.415 1.00 137.78 ? 173 ASP C CG 1 +ATOM 6110 O OD1 . ASP C 1 174 ? 9.567 59.625 123.519 1.00 135.19 ? 173 ASP C OD1 1 +ATOM 6111 O OD2 . ASP C 1 174 ? 7.937 61.067 123.260 1.00 134.05 ? 173 ASP C OD2 1 +ATOM 6112 N N . GLY C 1 175 ? 10.022 56.375 123.728 1.00 104.36 ? 174 GLY C N 1 +ATOM 6113 C CA . GLY C 1 175 ? 10.997 55.658 122.928 1.00 97.73 ? 174 GLY C CA 1 +ATOM 6114 C C . GLY C 1 175 ? 12.024 56.538 122.239 1.00 111.92 ? 174 GLY C C 1 +ATOM 6115 O O . GLY C 1 175 ? 13.019 56.034 121.718 1.00 116.91 ? 174 GLY C O 1 +ATOM 6116 N N . SER C 1 176 ? 11.797 57.849 122.226 1.00 77.19 ? 175 SER C N 1 +ATOM 6117 C CA . SER C 1 176 ? 12.746 58.750 121.573 1.00 110.48 ? 175 SER C CA 1 +ATOM 6118 C C . SER C 1 176 ? 13.977 58.967 122.441 1.00 101.21 ? 175 SER C C 1 +ATOM 6119 O O . SER C 1 176 ? 14.064 58.421 123.537 1.00 97.91 ? 175 SER C O 1 +ATOM 6120 C CB . SER C 1 176 ? 12.095 60.084 121.179 1.00 113.70 ? 175 SER C CB 1 +ATOM 6121 O OG . SER C 1 176 ? 11.349 60.656 122.238 1.00 106.89 ? 175 SER C OG 1 +ATOM 6122 N N . VAL C 1 177 ? 14.929 59.757 121.953 1.00 95.69 ? 176 VAL C N 1 +ATOM 6123 C CA . VAL C 1 177 ? 16.203 59.930 122.651 1.00 87.04 ? 176 VAL C CA 1 +ATOM 6124 C C . VAL C 1 177 ? 16.731 61.368 122.633 1.00 105.48 ? 176 VAL C C 1 +ATOM 6125 O O . VAL C 1 177 ? 17.001 61.933 121.574 1.00 144.20 ? 176 VAL C O 1 +ATOM 6126 C CB . VAL C 1 177 ? 17.289 58.971 122.092 1.00 76.07 ? 176 VAL C CB 1 +ATOM 6127 C CG1 . VAL C 1 177 ? 18.684 59.390 122.548 1.00 92.71 ? 176 VAL C CG1 1 +ATOM 6128 C CG2 . VAL C 1 177 ? 16.994 57.533 122.496 1.00 89.14 ? 176 VAL C CG2 1 +ATOM 6129 N N . GLN C 1 178 ? 16.898 61.944 123.819 1.00 67.94 ? 177 GLN C N 1 +ATOM 6130 C CA . GLN C 1 178 ? 17.401 63.307 123.948 1.00 97.53 ? 177 GLN C CA 1 +ATOM 6131 C C . GLN C 1 178 ? 18.927 63.389 123.914 1.00 99.50 ? 177 GLN C C 1 +ATOM 6132 O O . GLN C 1 178 ? 19.591 62.887 124.815 1.00 90.19 ? 177 GLN C O 1 +ATOM 6133 C CB . GLN C 1 178 ? 16.893 63.926 125.246 1.00 77.16 ? 177 GLN C CB 1 +ATOM 6134 C CG . GLN C 1 178 ? 17.561 65.243 125.597 1.00 107.67 ? 177 GLN C CG 1 +ATOM 6135 C CD . GLN C 1 178 ? 17.017 66.401 124.799 1.00 94.57 ? 177 GLN C CD 1 +ATOM 6136 O OE1 . GLN C 1 178 ? 15.801 66.559 124.672 1.00 92.84 ? 177 GLN C OE1 1 +ATOM 6137 N NE2 . GLN C 1 178 ? 17.912 67.220 124.250 1.00 105.86 ? 177 GLN C NE2 1 +ATOM 6138 N N . LEU C 1 179 ? 19.489 64.038 122.898 1.00 89.25 ? 178 LEU C N 1 +ATOM 6139 C CA . LEU C 1 179 ? 20.947 64.176 122.822 1.00 85.33 ? 178 LEU C CA 1 +ATOM 6140 C C . LEU C 1 179 ? 21.515 65.201 123.810 1.00 74.91 ? 178 LEU C C 1 +ATOM 6141 O O . LEU C 1 179 ? 20.854 66.179 124.139 1.00 99.23 ? 178 LEU C O 1 +ATOM 6142 C CB . LEU C 1 179 ? 21.404 64.510 121.395 1.00 87.49 ? 178 LEU C CB 1 +ATOM 6143 C CG . LEU C 1 179 ? 21.179 63.456 120.304 1.00 107.93 ? 178 LEU C CG 1 +ATOM 6144 C CD1 . LEU C 1 179 ? 21.551 64.000 118.930 1.00 120.75 ? 178 LEU C CD1 1 +ATOM 6145 C CD2 . LEU C 1 179 ? 21.950 62.167 120.594 1.00 86.54 ? 178 LEU C CD2 1 +ATOM 6146 N N . ALA C 1 180 ? 22.743 64.972 124.272 1.00 77.24 ? 179 ALA C N 1 +ATOM 6147 C CA . ALA C 1 180 ? 23.435 65.928 125.146 1.00 84.80 ? 179 ALA C CA 1 +ATOM 6148 C C . ALA C 1 180 ? 24.901 66.180 124.748 1.00 86.55 ? 179 ALA C C 1 +ATOM 6149 O O . ALA C 1 180 ? 25.843 65.631 125.321 1.00 93.87 ? 179 ALA C O 1 +ATOM 6150 C CB . ALA C 1 180 ? 23.323 65.514 126.614 1.00 101.65 ? 179 ALA C CB 1 +ATOM 6151 N N . ASP C 1 181 ? 25.072 67.050 123.769 1.00 75.03 ? 180 ASP C N 1 +ATOM 6152 C CA . ASP C 1 181 ? 26.370 67.301 123.160 1.00 109.25 ? 180 ASP C CA 1 +ATOM 6153 C C . ASP C 1 181 ? 27.405 67.913 124.138 1.00 94.51 ? 180 ASP C C 1 +ATOM 6154 O O . ASP C 1 181 ? 27.369 69.108 124.435 1.00 96.65 ? 180 ASP C O 1 +ATOM 6155 C CB . ASP C 1 181 ? 26.138 68.197 121.943 1.00 110.96 ? 180 ASP C CB 1 +ATOM 6156 C CG . ASP C 1 181 ? 27.198 68.045 120.885 1.00 117.83 ? 180 ASP C CG 1 +ATOM 6157 O OD1 . ASP C 1 181 ? 28.241 67.412 121.143 1.00 132.22 ? 180 ASP C OD1 1 +ATOM 6158 O OD2 . ASP C 1 181 ? 26.986 68.589 119.786 1.00 130.19 ? 180 ASP C OD2 1 +ATOM 6159 N N . HIS C 1 182 ? 28.336 67.095 124.630 1.00 67.58 ? 181 HIS C N 1 +ATOM 6160 C CA . HIS C 1 182 ? 29.270 67.548 125.670 1.00 99.66 ? 181 HIS C CA 1 +ATOM 6161 C C . HIS C 1 182 ? 30.606 68.098 125.180 1.00 78.38 ? 181 HIS C C 1 +ATOM 6162 O O . HIS C 1 182 ? 31.407 67.368 124.611 1.00 75.10 ? 181 HIS C O 1 +ATOM 6163 C CB . HIS C 1 182 ? 29.577 66.424 126.659 1.00 87.72 ? 181 HIS C CB 1 +ATOM 6164 C CG . HIS C 1 182 ? 28.481 66.149 127.638 1.00 63.39 ? 181 HIS C CG 1 +ATOM 6165 N ND1 . HIS C 1 182 ? 27.206 65.800 127.249 1.00 95.46 ? 181 HIS C ND1 1 +ATOM 6166 C CD2 . HIS C 1 182 ? 28.478 66.139 128.991 1.00 69.39 ? 181 HIS C CD2 1 +ATOM 6167 C CE1 . HIS C 1 182 ? 26.459 65.607 128.322 1.00 89.02 ? 181 HIS C CE1 1 +ATOM 6168 N NE2 . HIS C 1 182 ? 27.208 65.800 129.392 1.00 78.63 ? 181 HIS C NE2 1 +ATOM 6169 N N . TYR C 1 183 ? 30.860 69.372 125.466 1.00 97.16 ? 182 TYR C N 1 +ATOM 6170 C CA . TYR C 1 183 ? 32.122 70.028 125.113 1.00 103.68 ? 182 TYR C CA 1 +ATOM 6171 C C . TYR C 1 183 ? 32.936 70.361 126.362 1.00 78.85 ? 182 TYR C C 1 +ATOM 6172 O O . TYR C 1 183 ? 32.620 71.314 127.071 1.00 119.66 ? 182 TYR C O 1 +ATOM 6173 C CB . TYR C 1 183 ? 31.855 71.309 124.307 1.00 87.46 ? 182 TYR C CB 1 +ATOM 6174 C CG . TYR C 1 183 ? 31.287 71.029 122.938 1.00 90.99 ? 182 TYR C CG 1 +ATOM 6175 C CD1 . TYR C 1 183 ? 29.921 70.848 122.754 1.00 101.97 ? 182 TYR C CD1 1 +ATOM 6176 C CD2 . TYR C 1 183 ? 32.117 70.910 121.836 1.00 77.63 ? 182 TYR C CD2 1 +ATOM 6177 C CE1 . TYR C 1 183 ? 29.391 70.567 121.499 1.00 99.12 ? 182 TYR C CE1 1 +ATOM 6178 C CE2 . TYR C 1 183 ? 31.600 70.630 120.577 1.00 106.59 ? 182 TYR C CE2 1 +ATOM 6179 C CZ . TYR C 1 183 ? 30.234 70.457 120.409 1.00 107.56 ? 182 TYR C CZ 1 +ATOM 6180 O OH . TYR C 1 183 ? 29.718 70.174 119.154 1.00 101.70 ? 182 TYR C OH 1 +ATOM 6181 N N . GLN C 1 184 ? 33.993 69.598 126.619 1.00 77.48 ? 183 GLN C N 1 +ATOM 6182 C CA . GLN C 1 184 ? 34.714 69.691 127.893 1.00 105.25 ? 183 GLN C CA 1 +ATOM 6183 C C . GLN C 1 184 ? 36.170 70.146 127.735 1.00 100.06 ? 183 GLN C C 1 +ATOM 6184 O O . GLN C 1 184 ? 36.733 70.085 126.641 1.00 100.87 ? 183 GLN C O 1 +ATOM 6185 C CB . GLN C 1 184 ? 34.647 68.331 128.604 1.00 106.40 ? 183 GLN C CB 1 +ATOM 6186 C CG . GLN C 1 184 ? 35.400 68.199 129.921 1.00 101.68 ? 183 GLN C CG 1 +ATOM 6187 C CD . GLN C 1 184 ? 35.566 66.752 130.335 1.00 112.26 ? 183 GLN C CD 1 +ATOM 6188 O OE1 . GLN C 1 184 ? 34.696 65.916 130.074 1.00 80.49 ? 183 GLN C OE1 1 +ATOM 6189 N NE2 . GLN C 1 184 ? 36.690 66.442 130.972 1.00 76.32 ? 183 GLN C NE2 1 +ATOM 6190 N N . GLN C 1 185 ? 36.771 70.623 128.821 1.00 83.36 ? 184 GLN C N 1 +ATOM 6191 C CA . GLN C 1 185 ? 38.203 70.894 128.826 1.00 86.40 ? 184 GLN C CA 1 +ATOM 6192 C C . GLN C 1 185 ? 38.826 70.859 130.225 1.00 113.67 ? 184 GLN C C 1 +ATOM 6193 O O . GLN C 1 185 ? 38.253 71.373 131.192 1.00 97.27 ? 184 GLN C O 1 +ATOM 6194 C CB . GLN C 1 185 ? 38.520 72.210 128.106 1.00 124.98 ? 184 GLN C CB 1 +ATOM 6195 C CG . GLN C 1 185 ? 37.932 73.465 128.731 1.00 154.90 ? 184 GLN C CG 1 +ATOM 6196 C CD . GLN C 1 185 ? 38.404 74.730 128.027 1.00 175.32 ? 184 GLN C CD 1 +ATOM 6197 O OE1 . GLN C 1 185 ? 38.772 74.700 126.848 1.00 179.73 ? 184 GLN C OE1 1 +ATOM 6198 N NE2 . GLN C 1 185 ? 38.407 75.846 128.751 1.00 181.20 ? 184 GLN C NE2 1 +ATOM 6199 N N . ASN C 1 186 ? 40.005 70.248 130.316 1.00 95.56 ? 185 ASN C N 1 +ATOM 6200 C CA . ASN C 1 186 ? 40.691 70.063 131.595 1.00 107.44 ? 185 ASN C CA 1 +ATOM 6201 C C . ASN C 1 186 ? 42.079 70.700 131.653 1.00 119.08 ? 185 ASN C C 1 +ATOM 6202 O O . ASN C 1 186 ? 42.847 70.629 130.695 1.00 103.43 ? 185 ASN C O 1 +ATOM 6203 C CB . ASN C 1 186 ? 40.770 68.579 131.953 1.00 102.23 ? 185 ASN C CB 1 +ATOM 6204 C CG . ASN C 1 186 ? 39.412 67.979 132.240 1.00 98.83 ? 185 ASN C CG 1 +ATOM 6205 O OD1 . ASN C 1 186 ? 38.716 67.523 131.336 1.00 104.71 ? 185 ASN C OD1 1 +ATOM 6206 N ND2 . ASN C 1 186 ? 39.028 67.976 133.505 1.00 86.66 ? 185 ASN C ND2 1 +ATOM 6207 N N . THR C 1 187 ? 42.383 71.303 132.802 1.00 100.22 ? 186 THR C N 1 +ATOM 6208 C CA . THR C 1 187 ? 43.564 72.144 132.998 1.00 109.30 ? 186 THR C CA 1 +ATOM 6209 C C . THR C 1 187 ? 44.046 72.065 134.452 1.00 103.84 ? 186 THR C C 1 +ATOM 6210 O O . THR C 1 187 ? 43.262 72.266 135.379 1.00 122.33 ? 186 THR C O 1 +ATOM 6211 C CB . THR C 1 187 ? 43.245 73.624 132.655 1.00 107.57 ? 186 THR C CB 1 +ATOM 6212 O OG1 . THR C 1 187 ? 43.096 73.773 131.238 1.00 116.43 ? 186 THR C OG1 1 +ATOM 6213 C CG2 . THR C 1 187 ? 44.350 74.557 133.150 1.00 89.24 ? 186 THR C CG2 1 +ATOM 6214 N N . PRO C 1 188 ? 45.344 71.779 134.654 1.00 109.72 ? 187 PRO C N 1 +ATOM 6215 C CA . PRO C 1 188 ? 45.943 71.611 135.987 1.00 121.68 ? 187 PRO C CA 1 +ATOM 6216 C C . PRO C 1 188 ? 46.095 72.901 136.796 1.00 119.10 ? 187 PRO C C 1 +ATOM 6217 O O . PRO C 1 188 ? 46.648 73.897 136.332 1.00 129.83 ? 187 PRO C O 1 +ATOM 6218 C CB . PRO C 1 188 ? 47.323 71.025 135.678 1.00 111.22 ? 187 PRO C CB 1 +ATOM 6219 C CG . PRO C 1 188 ? 47.634 71.512 134.304 1.00 110.04 ? 187 PRO C CG 1 +ATOM 6220 C CD . PRO C 1 188 ? 46.316 71.520 133.579 1.00 86.70 ? 187 PRO C CD 1 +ATOM 6221 N N . ILE C 1 189 ? 45.603 72.852 138.026 1.00 119.66 ? 188 ILE C N 1 +ATOM 6222 C CA . ILE C 1 189 ? 45.735 73.944 138.975 1.00 128.78 ? 188 ILE C CA 1 +ATOM 6223 C C . ILE C 1 189 ? 47.194 74.134 139.381 1.00 139.21 ? 188 ILE C C 1 +ATOM 6224 O O . ILE C 1 189 ? 47.642 75.254 139.643 1.00 126.06 ? 188 ILE C O 1 +ATOM 6225 C CB . ILE C 1 189 ? 44.893 73.635 140.219 1.00 108.90 ? 188 ILE C CB 1 +ATOM 6226 C CG1 . ILE C 1 189 ? 43.435 73.418 139.804 1.00 109.02 ? 188 ILE C CG1 1 +ATOM 6227 C CG2 . ILE C 1 189 ? 45.034 74.733 141.264 1.00 103.06 ? 188 ILE C CG2 1 +ATOM 6228 C CD1 . ILE C 1 189 ? 42.551 72.844 140.887 1.00 113.57 ? 188 ILE C CD1 1 +ATOM 6229 N N . GLY C 1 190 ? 47.931 73.027 139.423 1.00 145.05 ? 189 GLY C N 1 +ATOM 6230 C CA . GLY C 1 190 ? 49.324 73.045 139.830 1.00 148.73 ? 189 GLY C CA 1 +ATOM 6231 C C . GLY C 1 190 ? 50.272 73.466 138.724 1.00 155.86 ? 189 GLY C C 1 +ATOM 6232 O O . GLY C 1 190 ? 49.872 73.591 137.562 1.00 131.09 ? 189 GLY C O 1 +ATOM 6233 N N . ASP C 1 191 ? 51.532 73.689 139.099 1.00 158.58 ? 190 ASP C N 1 +ATOM 6234 C CA . ASP C 1 191 ? 52.587 74.077 138.161 1.00 168.80 ? 190 ASP C CA 1 +ATOM 6235 C C . ASP C 1 191 ? 53.454 72.879 137.790 1.00 160.02 ? 190 ASP C C 1 +ATOM 6236 O O . ASP C 1 191 ? 54.261 72.949 136.862 1.00 141.19 ? 190 ASP C O 1 +ATOM 6237 C CB . ASP C 1 191 ? 53.470 75.194 138.739 1.00 166.20 ? 190 ASP C CB 1 +ATOM 6238 C CG . ASP C 1 191 ? 52.816 76.565 138.664 1.00 181.24 ? 190 ASP C CG 1 +ATOM 6239 O OD1 . ASP C 1 191 ? 52.476 77.017 137.552 1.00 160.22 ? 190 ASP C OD1 1 +ATOM 6240 O OD2 . ASP C 1 191 ? 52.655 77.199 139.725 1.00 194.28 ? 190 ASP C OD2 1 +ATOM 6241 N N . GLY C 1 192 ? 53.284 71.784 138.524 1.00 158.74 ? 191 GLY C N 1 +ATOM 6242 C CA . GLY C 1 192 ? 53.995 70.551 138.235 1.00 159.34 ? 191 GLY C CA 1 +ATOM 6243 C C . GLY C 1 192 ? 53.736 70.048 136.826 1.00 169.41 ? 191 GLY C C 1 +ATOM 6244 O O . GLY C 1 192 ? 52.738 70.423 136.205 1.00 162.83 ? 191 GLY C O 1 +ATOM 6245 N N . PRO C 1 193 ? 54.639 69.199 136.305 1.00 178.39 ? 192 PRO C N 1 +ATOM 6246 C CA . PRO C 1 193 ? 54.445 68.664 134.954 1.00 179.21 ? 192 PRO C CA 1 +ATOM 6247 C C . PRO C 1 193 ? 53.368 67.581 134.934 1.00 166.87 ? 192 PRO C C 1 +ATOM 6248 O O . PRO C 1 193 ? 53.196 66.844 135.908 1.00 132.60 ? 192 PRO C O 1 +ATOM 6249 C CB . PRO C 1 193 ? 55.820 68.087 134.602 1.00 169.65 ? 192 PRO C CB 1 +ATOM 6250 C CG . PRO C 1 193 ? 56.423 67.717 135.919 1.00 148.51 ? 192 PRO C CG 1 +ATOM 6251 C CD . PRO C 1 193 ? 55.872 68.691 136.937 1.00 161.04 ? 192 PRO C CD 1 +ATOM 6252 N N . VAL C 1 194 ? 52.629 67.510 133.833 1.00 154.45 ? 193 VAL C N 1 +ATOM 6253 C CA . VAL C 1 194 ? 51.547 66.549 133.708 1.00 142.39 ? 193 VAL C CA 1 +ATOM 6254 C C . VAL C 1 194 ? 51.768 65.725 132.450 1.00 128.89 ? 193 VAL C C 1 +ATOM 6255 O O . VAL C 1 194 ? 52.704 65.973 131.696 1.00 117.46 ? 193 VAL C O 1 +ATOM 6256 C CB . VAL C 1 194 ? 50.166 67.245 133.645 1.00 149.74 ? 193 VAL C CB 1 +ATOM 6257 C CG1 . VAL C 1 194 ? 49.940 68.120 134.881 1.00 110.05 ? 193 VAL C CG1 1 +ATOM 6258 C CG2 . VAL C 1 194 ? 50.033 68.062 132.365 1.00 142.89 ? 193 VAL C CG2 1 +ATOM 6259 N N . LEU C 1 195 ? 50.910 64.739 132.231 1.00 115.82 ? 194 LEU C N 1 +ATOM 6260 C CA . LEU C 1 195 ? 51.011 63.890 131.054 1.00 103.42 ? 194 LEU C CA 1 +ATOM 6261 C C . LEU C 1 195 ? 50.038 64.375 129.990 1.00 114.49 ? 194 LEU C C 1 +ATOM 6262 O O . LEU C 1 195 ? 48.866 64.604 130.272 1.00 137.39 ? 194 LEU C O 1 +ATOM 6263 C CB . LEU C 1 195 ? 50.730 62.434 131.428 1.00 96.48 ? 194 LEU C CB 1 +ATOM 6264 C CG . LEU C 1 195 ? 51.636 61.900 132.545 1.00 119.54 ? 194 LEU C CG 1 +ATOM 6265 C CD1 . LEU C 1 195 ? 51.314 60.446 132.878 1.00 114.67 ? 194 LEU C CD1 1 +ATOM 6266 C CD2 . LEU C 1 195 ? 53.117 62.072 132.194 1.00 90.10 ? 194 LEU C CD2 1 +ATOM 6267 N N . LEU C 1 196 ? 50.529 64.552 128.770 1.00 111.79 ? 195 LEU C N 1 +ATOM 6268 C CA . LEU C 1 196 ? 49.675 65.007 127.680 1.00 128.91 ? 195 LEU C CA 1 +ATOM 6269 C C . LEU C 1 196 ? 49.446 63.883 126.662 1.00 126.38 ? 195 LEU C C 1 +ATOM 6270 O O . LEU C 1 196 ? 50.321 63.567 125.854 1.00 119.92 ? 195 LEU C O 1 +ATOM 6271 C CB . LEU C 1 196 ? 50.248 66.277 127.042 1.00 150.60 ? 195 LEU C CB 1 +ATOM 6272 C CG . LEU C 1 196 ? 50.551 67.370 128.080 1.00 130.63 ? 195 LEU C CG 1 +ATOM 6273 C CD1 . LEU C 1 196 ? 51.201 68.589 127.450 1.00 123.32 ? 195 LEU C CD1 1 +ATOM 6274 C CD2 . LEU C 1 196 ? 49.292 67.765 128.842 1.00 121.34 ? 195 LEU C CD2 1 +ATOM 6275 N N . PRO C 1 197 ? 48.250 63.279 126.711 1.00 115.00 ? 196 PRO C N 1 +ATOM 6276 C CA . PRO C 1 197 ? 47.881 62.028 126.033 1.00 115.81 ? 196 PRO C CA 1 +ATOM 6277 C C . PRO C 1 197 ? 47.742 62.104 124.516 1.00 111.99 ? 196 PRO C C 1 +ATOM 6278 O O . PRO C 1 197 ? 47.368 63.133 123.961 1.00 119.59 ? 196 PRO C O 1 +ATOM 6279 C CB . PRO C 1 197 ? 46.508 61.716 126.631 1.00 116.06 ? 196 PRO C CB 1 +ATOM 6280 C CG . PRO C 1 197 ? 45.947 63.054 126.970 1.00 105.19 ? 196 PRO C CG 1 +ATOM 6281 C CD . PRO C 1 197 ? 47.119 63.847 127.464 1.00 92.91 ? 196 PRO C CD 1 +ATOM 6282 N N . ASP C 1 198 ? 48.037 60.990 123.857 1.00 120.24 ? 197 ASP C N 1 +ATOM 6283 C CA . ASP C 1 198 ? 47.662 60.806 122.466 1.00 131.04 ? 197 ASP C CA 1 +ATOM 6284 C C . ASP C 1 198 ? 46.168 60.546 122.436 1.00 112.96 ? 197 ASP C C 1 +ATOM 6285 O O . ASP C 1 198 ? 45.584 60.207 123.458 1.00 109.73 ? 197 ASP C O 1 +ATOM 6286 C CB . ASP C 1 198 ? 48.400 59.608 121.868 1.00 136.50 ? 197 ASP C CB 1 +ATOM 6287 C CG . ASP C 1 198 ? 49.842 59.921 121.529 1.00 149.29 ? 197 ASP C CG 1 +ATOM 6288 O OD1 . ASP C 1 198 ? 50.175 61.120 121.407 1.00 151.07 ? 197 ASP C OD1 1 +ATOM 6289 O OD2 . ASP C 1 198 ? 50.636 58.967 121.375 1.00 131.02 ? 197 ASP C OD2 1 +ATOM 6290 N N . ASN C 1 199 ? 45.552 60.707 121.272 1.00 102.97 ? 198 ASN C N 1 +ATOM 6291 C CA . ASN C 1 199 ? 44.142 60.387 121.114 1.00 115.74 ? 198 ASN C CA 1 +ATOM 6292 C C . ASN C 1 199 ? 43.796 59.010 121.666 1.00 115.85 ? 198 ASN C C 1 +ATOM 6293 O O . ASN C 1 199 ? 44.370 58.010 121.239 1.00 116.76 ? 198 ASN C O 1 +ATOM 6294 C CB . ASN C 1 199 ? 43.762 60.419 119.646 1.00 140.41 ? 198 ASN C CB 1 +ATOM 6295 C CG . ASN C 1 199 ? 43.767 61.805 119.050 1.00 145.05 ? 198 ASN C CG 1 +ATOM 6296 O OD1 . ASN C 1 199 ? 44.364 62.726 119.602 1.00 105.88 ? 198 ASN C OD1 1 +ATOM 6297 N ND2 . ASN C 1 199 ? 43.101 61.962 117.907 1.00 142.18 ? 198 ASN C ND2 1 +ATOM 6298 N N . HIS C 1 200 ? 42.870 58.975 122.625 1.00 116.32 ? 199 HIS C N 1 +ATOM 6299 C CA . HIS C 1 200 ? 42.254 57.731 123.093 1.00 107.62 ? 199 HIS C CA 1 +ATOM 6300 C C . HIS C 1 200 ? 40.851 57.998 123.618 1.00 93.70 ? 199 HIS C C 1 +ATOM 6301 O O . HIS C 1 200 ? 40.327 59.088 123.433 1.00 94.25 ? 199 HIS C O 1 +ATOM 6302 C CB . HIS C 1 200 ? 43.096 57.065 124.174 1.00 94.93 ? 199 HIS C CB 1 +ATOM 6303 C CG . HIS C 1 200 ? 43.152 57.826 125.459 1.00 89.07 ? 199 HIS C CG 1 +ATOM 6304 N ND1 . HIS C 1 200 ? 44.084 58.813 125.695 1.00 100.68 ? 199 HIS C ND1 1 +ATOM 6305 C CD2 . HIS C 1 200 ? 42.413 57.730 126.589 1.00 99.04 ? 199 HIS C CD2 1 +ATOM 6306 C CE1 . HIS C 1 200 ? 43.911 59.298 126.911 1.00 98.07 ? 199 HIS C CE1 1 +ATOM 6307 N NE2 . HIS C 1 200 ? 42.903 58.658 127.475 1.00 109.41 ? 199 HIS C NE2 1 +ATOM 6308 N N . TYR C 1 201 ? 40.240 57.016 124.274 1.00 92.83 ? 200 TYR C N 1 +ATOM 6309 C CA . TYR C 1 201 ? 38.891 57.222 124.802 1.00 97.57 ? 200 TYR C CA 1 +ATOM 6310 C C . TYR C 1 201 ? 38.573 56.462 126.096 1.00 93.14 ? 200 TYR C C 1 +ATOM 6311 O O . TYR C 1 201 ? 39.266 55.516 126.448 1.00 88.68 ? 200 TYR C O 1 +ATOM 6312 C CB . TYR C 1 201 ? 37.845 56.963 123.712 1.00 84.95 ? 200 TYR C CB 1 +ATOM 6313 C CG . TYR C 1 201 ? 37.628 55.520 123.318 1.00 89.62 ? 200 TYR C CG 1 +ATOM 6314 C CD1 . TYR C 1 201 ? 38.576 54.819 122.587 1.00 97.79 ? 200 TYR C CD1 1 +ATOM 6315 C CD2 . TYR C 1 201 ? 36.454 54.868 123.652 1.00 102.27 ? 200 TYR C CD2 1 +ATOM 6316 C CE1 . TYR C 1 201 ? 38.362 53.497 122.212 1.00 98.29 ? 200 TYR C CE1 1 +ATOM 6317 C CE2 . TYR C 1 201 ? 36.230 53.550 123.279 1.00 117.23 ? 200 TYR C CE2 1 +ATOM 6318 C CZ . TYR C 1 201 ? 37.189 52.868 122.561 1.00 101.09 ? 200 TYR C CZ 1 +ATOM 6319 O OH . TYR C 1 201 ? 36.982 51.557 122.191 1.00 91.49 ? 200 TYR C OH 1 +ATOM 6320 N N . LEU C 1 202 ? 37.549 56.910 126.819 1.00 90.96 ? 201 LEU C N 1 +ATOM 6321 C CA . LEU C 1 202 ? 37.104 56.214 128.021 1.00 99.08 ? 201 LEU C CA 1 +ATOM 6322 C C . LEU C 1 202 ? 35.792 55.503 127.708 1.00 85.67 ? 201 LEU C C 1 +ATOM 6323 O O . LEU C 1 202 ? 34.869 56.087 127.153 1.00 73.39 ? 201 LEU C O 1 +ATOM 6324 C CB . LEU C 1 202 ? 36.952 57.171 129.217 1.00 73.94 ? 201 LEU C CB 1 +ATOM 6325 C CG . LEU C 1 202 ? 38.136 58.049 129.666 1.00 84.21 ? 201 LEU C CG 1 +ATOM 6326 C CD1 . LEU C 1 202 ? 37.927 58.634 131.054 1.00 79.86 ? 201 LEU C CD1 1 +ATOM 6327 C CD2 . LEU C 1 202 ? 39.467 57.325 129.613 1.00 109.22 ? 201 LEU C CD2 1 +ATOM 6328 N N . SER C 1 203 ? 35.728 54.223 128.030 1.00 81.56 ? 202 SER C N 1 +ATOM 6329 C CA . SER C 1 203 ? 34.524 53.461 127.781 1.00 77.91 ? 202 SER C CA 1 +ATOM 6330 C C . SER C 1 203 ? 33.763 53.432 129.085 1.00 82.21 ? 202 SER C C 1 +ATOM 6331 O O . SER C 1 203 ? 34.176 52.753 130.030 1.00 105.92 ? 202 SER C O 1 +ATOM 6332 C CB . SER C 1 203 ? 34.876 52.045 127.336 1.00 68.90 ? 202 SER C CB 1 +ATOM 6333 O OG . SER C 1 203 ? 33.721 51.332 126.942 1.00 94.06 ? 202 SER C OG 1 +ATOM 6334 N N . THR C 1 204 ? 32.664 54.181 129.135 1.00 83.92 ? 203 THR C N 1 +ATOM 6335 C CA . THR C 1 204 ? 31.875 54.326 130.352 1.00 86.67 ? 203 THR C CA 1 +ATOM 6336 C C . THR C 1 204 ? 30.624 53.468 130.311 1.00 87.99 ? 203 THR C C 1 +ATOM 6337 O O . THR C 1 204 ? 30.015 53.308 129.258 1.00 92.95 ? 203 THR C O 1 +ATOM 6338 C CB . THR C 1 204 ? 31.437 55.783 130.581 1.00 78.99 ? 203 THR C CB 1 +ATOM 6339 O OG1 . THR C 1 204 ? 32.575 56.644 130.495 1.00 83.36 ? 203 THR C OG1 1 +ATOM 6340 C CG2 . THR C 1 204 ? 30.824 55.934 131.962 1.00 133.20 ? 203 THR C CG2 1 +ATOM 6341 N N . GLN C 1 205 ? 30.270 52.900 131.463 1.00 80.28 ? 204 GLN C N 1 +ATOM 6342 C CA . GLN C 1 205 ? 28.972 52.260 131.679 1.00 82.69 ? 204 GLN C CA 1 +ATOM 6343 C C . GLN C 1 205 ? 28.453 52.609 133.082 1.00 86.56 ? 204 GLN C C 1 +ATOM 6344 O O . GLN C 1 205 ? 29.223 52.635 134.049 1.00 73.09 ? 204 GLN C O 1 +ATOM 6345 C CB . GLN C 1 205 ? 29.072 50.740 131.529 1.00 83.07 ? 204 GLN C CB 1 +ATOM 6346 C CG . GLN C 1 205 ? 29.819 50.252 130.303 1.00 69.40 ? 204 GLN C CG 1 +ATOM 6347 C CD . GLN C 1 205 ? 30.725 49.090 130.622 1.00 100.03 ? 204 GLN C CD 1 +ATOM 6348 O OE1 . GLN C 1 205 ? 30.281 47.940 130.668 1.00 148.94 ? 204 GLN C OE1 1 +ATOM 6349 N NE2 . GLN C 1 205 ? 32.006 49.382 130.863 1.00 100.89 ? 204 GLN C NE2 1 +ATOM 6350 N N . SER C 1 206 ? 27.143 52.851 133.184 1.00 77.33 ? 205 SER C N 1 +ATOM 6351 C CA . SER C 1 206 ? 26.527 53.420 134.389 1.00 62.36 ? 205 SER C CA 1 +ATOM 6352 C C . SER C 1 206 ? 25.126 52.859 134.709 1.00 56.75 ? 205 SER C C 1 +ATOM 6353 O O . SER C 1 206 ? 24.402 52.408 133.819 1.00 87.19 ? 205 SER C O 1 +ATOM 6354 C CB . SER C 1 206 ? 26.478 54.952 134.278 1.00 68.57 ? 205 SER C CB 1 +ATOM 6355 O OG . SER C 1 206 ? 27.787 55.501 134.249 1.00 98.78 ? 205 SER C OG 1 +ATOM 6356 N N . ASN C 1 207 ? 24.766 52.864 135.992 1.00 67.79 ? 206 ASN C N 1 +ATOM 6357 C CA . ASN C 1 207 ? 23.427 52.454 136.426 1.00 76.22 ? 206 ASN C CA 1 +ATOM 6358 C C . ASN C 1 207 ? 22.930 53.363 137.542 1.00 84.32 ? 206 ASN C C 1 +ATOM 6359 O O . ASN C 1 207 ? 23.685 53.727 138.446 1.00 75.64 ? 206 ASN C O 1 +ATOM 6360 C CB . ASN C 1 207 ? 23.384 50.950 136.787 1.00 73.22 ? 206 ASN C CB 1 +ATOM 6361 C CG . ASN C 1 207 ? 22.297 50.587 137.810 1.00 66.02 ? 206 ASN C CG 1 +ATOM 6362 O OD1 . ASN C 1 207 ? 22.393 50.949 138.975 1.00 54.88 ? 206 ASN C OD1 1 +ATOM 6363 N ND2 . ASN C 1 207 ? 21.309 49.801 137.387 1.00 76.70 ? 206 ASN C ND2 1 +ATOM 6364 N N . LEU C 1 208 ? 21.661 53.747 137.436 1.00 70.28 ? 207 LEU C N 1 +ATOM 6365 C CA . LEU C 1 208 ? 21.027 54.669 138.365 1.00 51.10 ? 207 LEU C CA 1 +ATOM 6366 C C . LEU C 1 208 ? 20.007 53.916 139.212 1.00 59.28 ? 207 LEU C C 1 +ATOM 6367 O O . LEU C 1 208 ? 19.161 53.181 138.683 1.00 69.39 ? 207 LEU C O 1 +ATOM 6368 C CB . LEU C 1 208 ? 20.333 55.801 137.598 1.00 73.11 ? 207 LEU C CB 1 +ATOM 6369 C CG . LEU C 1 208 ? 21.149 56.524 136.525 1.00 54.14 ? 207 LEU C CG 1 +ATOM 6370 C CD1 . LEU C 1 208 ? 20.343 57.632 135.912 1.00 74.89 ? 207 LEU C CD1 1 +ATOM 6371 C CD2 . LEU C 1 208 ? 22.446 57.067 137.083 1.00 63.28 ? 207 LEU C CD2 1 +ATOM 6372 N N . SER C 1 209 ? 20.099 54.108 140.527 1.00 61.35 ? 208 SER C N 1 +ATOM 6373 C CA . SER C 1 209 ? 19.210 53.440 141.476 1.00 69.86 ? 208 SER C CA 1 +ATOM 6374 C C . SER C 1 209 ? 18.843 54.268 142.705 1.00 84.98 ? 208 SER C C 1 +ATOM 6375 O O . SER C 1 209 ? 19.382 55.354 142.948 1.00 64.41 ? 208 SER C O 1 +ATOM 6376 C CB . SER C 1 209 ? 19.835 52.135 141.956 1.00 66.92 ? 208 SER C CB 1 +ATOM 6377 O OG . SER C 1 209 ? 21.169 52.356 142.378 1.00 85.23 ? 208 SER C OG 1 +ATOM 6378 N N . LYS C 1 210 ? 17.921 53.709 143.483 1.00 80.00 ? 209 LYS C N 1 +ATOM 6379 C CA . LYS C 1 210 ? 17.518 54.277 144.758 1.00 62.47 ? 209 LYS C CA 1 +ATOM 6380 C C . LYS C 1 210 ? 17.978 53.405 145.924 1.00 68.87 ? 209 LYS C C 1 +ATOM 6381 O O . LYS C 1 210 ? 18.198 52.206 145.776 1.00 88.22 ? 209 LYS C O 1 +ATOM 6382 C CB . LYS C 1 210 ? 15.995 54.434 144.818 1.00 83.50 ? 209 LYS C CB 1 +ATOM 6383 C CG . LYS C 1 210 ? 15.372 55.276 143.705 1.00 70.58 ? 209 LYS C CG 1 +ATOM 6384 C CD . LYS C 1 210 ? 15.855 56.717 143.717 1.00 64.04 ? 209 LYS C CD 1 +ATOM 6385 C CE . LYS C 1 210 ? 15.019 57.598 142.790 1.00 67.96 ? 209 LYS C CE 1 +ATOM 6386 N NZ . LYS C 1 210 ? 15.606 58.958 142.663 1.00 68.80 ? 209 LYS C NZ 1 +ATOM 6387 N N . ASP C 1 211 ? 18.134 54.056 147.072 1.00 80.98 ? 210 ASP C N 1 +ATOM 6388 C CA . ASP C 1 211 ? 18.327 53.463 148.389 1.00 69.46 ? 210 ASP C CA 1 +ATOM 6389 C C . ASP C 1 211 ? 16.947 53.426 149.029 1.00 91.75 ? 210 ASP C C 1 +ATOM 6390 O O . ASP C 1 211 ? 16.281 54.455 149.114 1.00 99.54 ? 210 ASP C O 1 +ATOM 6391 C CB . ASP C 1 211 ? 19.238 54.398 149.190 1.00 77.87 ? 210 ASP C CB 1 +ATOM 6392 C CG . ASP C 1 211 ? 19.422 53.979 150.644 1.00 104.57 ? 210 ASP C CG 1 +ATOM 6393 O OD1 . ASP C 1 211 ? 18.724 53.064 151.130 1.00 102.63 ? 210 ASP C OD1 1 +ATOM 6394 O OD2 . ASP C 1 211 ? 20.285 54.597 151.309 1.00 75.09 ? 210 ASP C OD2 1 +ATOM 6395 N N . PRO C 1 212 ? 16.506 52.249 149.493 1.00 111.47 ? 211 PRO C N 1 +ATOM 6396 C CA . PRO C 1 212 ? 15.118 52.200 149.972 1.00 102.41 ? 211 PRO C CA 1 +ATOM 6397 C C . PRO C 1 212 ? 14.896 52.709 151.418 1.00 100.61 ? 211 PRO C C 1 +ATOM 6398 O O . PRO C 1 212 ? 13.751 52.757 151.865 1.00 94.26 ? 211 PRO C O 1 +ATOM 6399 C CB . PRO C 1 212 ? 14.752 50.722 149.812 1.00 81.79 ? 211 PRO C CB 1 +ATOM 6400 C CG . PRO C 1 212 ? 16.060 50.004 149.991 1.00 102.13 ? 211 PRO C CG 1 +ATOM 6401 C CD . PRO C 1 212 ? 17.147 50.920 149.481 1.00 78.82 ? 211 PRO C CD 1 +ATOM 6402 N N . ASN C 1 213 ? 15.960 53.102 152.121 1.00 124.07 ? 212 ASN C N 1 +ATOM 6403 C CA . ASN C 1 213 ? 15.824 53.724 153.451 1.00 132.27 ? 212 ASN C CA 1 +ATOM 6404 C C . ASN C 1 213 ? 16.058 55.230 153.421 1.00 116.45 ? 212 ASN C C 1 +ATOM 6405 O O . ASN C 1 213 ? 16.221 55.873 154.458 1.00 107.92 ? 212 ASN C O 1 +ATOM 6406 C CB . ASN C 1 213 ? 16.815 53.141 154.455 1.00 115.22 ? 212 ASN C CB 1 +ATOM 6407 C CG . ASN C 1 213 ? 16.909 51.646 154.392 1.00 104.61 ? 212 ASN C CG 1 +ATOM 6408 O OD1 . ASN C 1 213 ? 15.920 50.947 154.153 1.00 100.24 ? 212 ASN C OD1 1 +ATOM 6409 N ND2 . ASN C 1 213 ? 18.113 51.137 154.615 1.00 89.66 ? 212 ASN C ND2 1 +ATOM 6410 N N . GLU C 1 214 ? 16.119 55.783 152.224 1.00 109.27 ? 213 GLU C N 1 +ATOM 6411 C CA . GLU C 1 214 ? 16.338 57.198 152.078 1.00 76.46 ? 213 GLU C CA 1 +ATOM 6412 C C . GLU C 1 214 ? 15.024 57.818 151.671 1.00 81.07 ? 213 GLU C C 1 +ATOM 6413 O O . GLU C 1 214 ? 14.356 57.319 150.771 1.00 95.94 ? 213 GLU C O 1 +ATOM 6414 C CB . GLU C 1 214 ? 17.394 57.465 151.019 1.00 70.63 ? 213 GLU C CB 1 +ATOM 6415 C CG . GLU C 1 214 ? 17.643 58.917 150.824 1.00 82.57 ? 213 GLU C CG 1 +ATOM 6416 C CD . GLU C 1 214 ? 17.892 59.608 152.138 1.00 115.78 ? 213 GLU C CD 1 +ATOM 6417 O OE1 . GLU C 1 214 ? 16.913 60.076 152.760 1.00 124.40 ? 213 GLU C OE1 1 +ATOM 6418 O OE2 . GLU C 1 214 ? 19.067 59.679 152.553 1.00 90.66 ? 213 GLU C OE2 1 +ATOM 6419 N N . LYS C 1 215 ? 14.643 58.892 152.351 1.00 86.57 ? 214 LYS C N 1 +ATOM 6420 C CA . LYS C 1 215 ? 13.362 59.528 152.088 1.00 98.68 ? 214 LYS C CA 1 +ATOM 6421 C C . LYS C 1 215 ? 13.544 60.882 151.413 1.00 89.89 ? 214 LYS C C 1 +ATOM 6422 O O . LYS C 1 215 ? 12.598 61.422 150.850 1.00 101.87 ? 214 LYS C O 1 +ATOM 6423 C CB . LYS C 1 215 ? 12.546 59.670 153.378 1.00 89.24 ? 214 LYS C CB 1 +ATOM 6424 C CG . LYS C 1 215 ? 12.354 58.365 154.152 1.00 137.74 ? 214 LYS C CG 1 +ATOM 6425 C CD . LYS C 1 215 ? 11.281 58.497 155.245 1.00 149.67 ? 214 LYS C CD 1 +ATOM 6426 C CE . LYS C 1 215 ? 11.787 59.181 156.522 1.00 138.19 ? 214 LYS C CE 1 +ATOM 6427 N NZ . LYS C 1 215 ? 12.354 58.225 157.513 1.00 118.09 ? 214 LYS C NZ 1 +ATOM 6428 N N . ARG C 1 216 ? 14.762 61.417 151.476 1.00 74.11 ? 215 ARG C N 1 +ATOM 6429 C CA . ARG C 1 216 ? 15.142 62.635 150.754 1.00 66.39 ? 215 ARG C CA 1 +ATOM 6430 C C . ARG C 1 216 ? 15.383 62.361 149.263 1.00 73.55 ? 215 ARG C C 1 +ATOM 6431 O O . ARG C 1 216 ? 15.586 61.217 148.867 1.00 98.38 ? 215 ARG C O 1 +ATOM 6432 C CB . ARG C 1 216 ? 16.416 63.219 151.361 1.00 61.21 ? 215 ARG C CB 1 +ATOM 6433 C CG . ARG C 1 216 ? 16.253 63.823 152.740 1.00 87.92 ? 215 ARG C CG 1 +ATOM 6434 C CD . ARG C 1 216 ? 17.613 64.099 153.335 1.00 83.34 ? 215 ARG C CD 1 +ATOM 6435 N NE . ARG C 1 216 ? 18.282 62.862 153.713 1.00 112.62 ? 215 ARG C NE 1 +ATOM 6436 C CZ . ARG C 1 216 ? 19.477 62.777 154.293 1.00 116.41 ? 215 ARG C CZ 1 +ATOM 6437 N NH1 . ARG C 1 216 ? 20.175 63.872 154.571 1.00 105.75 ? 215 ARG C NH1 1 +ATOM 6438 N NH2 . ARG C 1 216 ? 19.974 61.582 154.592 1.00 89.75 ? 215 ARG C NH2 1 +ATOM 6439 N N . ASP C 1 217 ? 15.384 63.400 148.432 1.00 67.30 ? 216 ASP C N 1 +ATOM 6440 C CA . ASP C 1 217 ? 15.565 63.186 146.993 1.00 94.44 ? 216 ASP C CA 1 +ATOM 6441 C C . ASP C 1 217 ? 17.024 62.858 146.665 1.00 97.40 ? 216 ASP C C 1 +ATOM 6442 O O . ASP C 1 217 ? 17.935 63.666 146.894 1.00 74.62 ? 216 ASP C O 1 +ATOM 6443 C CB . ASP C 1 217 ? 15.048 64.376 146.172 1.00 83.97 ? 216 ASP C CB 1 +ATOM 6444 C CG . ASP C 1 217 ? 14.613 63.975 144.762 1.00 109.76 ? 216 ASP C CG 1 +ATOM 6445 O OD1 . ASP C 1 217 ? 14.483 62.763 144.497 1.00 110.95 ? 216 ASP C OD1 1 +ATOM 6446 O OD2 . ASP C 1 217 ? 14.391 64.871 143.919 1.00 88.66 ? 216 ASP C OD2 1 +ATOM 6447 N N . HIS C 1 218 ? 17.223 61.661 146.118 1.00 85.26 ? 217 HIS C N 1 +ATOM 6448 C CA . HIS C 1 218 ? 18.553 61.091 145.973 1.00 74.39 ? 217 HIS C CA 1 +ATOM 6449 C C . HIS C 1 218 ? 18.775 60.239 144.711 1.00 63.14 ? 217 HIS C C 1 +ATOM 6450 O O . HIS C 1 218 ? 17.840 59.776 144.050 1.00 75.79 ? 217 HIS C O 1 +ATOM 6451 C CB . HIS C 1 218 ? 18.884 60.256 147.215 1.00 62.76 ? 217 HIS C CB 1 +ATOM 6452 C CG . HIS C 1 218 ? 18.185 58.940 147.241 1.00 60.08 ? 217 HIS C CG 1 +ATOM 6453 N ND1 . HIS C 1 218 ? 16.815 58.829 147.325 1.00 97.67 ? 217 HIS C ND1 1 +ATOM 6454 C CD2 . HIS C 1 218 ? 18.660 57.676 147.152 1.00 89.76 ? 217 HIS C CD2 1 +ATOM 6455 C CE1 . HIS C 1 218 ? 16.477 57.552 147.300 1.00 70.44 ? 217 HIS C CE1 1 +ATOM 6456 N NE2 . HIS C 1 218 ? 17.577 56.834 147.192 1.00 79.78 ? 217 HIS C NE2 1 +ATOM 6457 N N . MET C 1 219 ? 20.050 60.046 144.399 1.00 74.95 ? 218 MET C N 1 +ATOM 6458 C CA . MET C 1 219 ? 20.506 59.158 143.369 1.00 69.32 ? 218 MET C CA 1 +ATOM 6459 C C . MET C 1 219 ? 21.673 58.311 143.830 1.00 74.12 ? 218 MET C C 1 +ATOM 6460 O O . MET C 1 219 ? 22.646 58.879 144.344 1.00 75.89 ? 218 MET C O 1 +ATOM 6461 C CB . MET C 1 219 ? 20.802 59.899 142.076 1.00 59.96 ? 218 MET C CB 1 +ATOM 6462 C CG . MET C 1 219 ? 21.314 59.037 140.948 1.00 47.32 ? 218 MET C CG 1 +ATOM 6463 S SD . MET C 1 219 ? 21.849 59.978 139.511 1.00 71.72 ? 218 MET C SD 1 +ATOM 6464 C CE . MET C 1 219 ? 23.322 60.829 140.086 1.00 65.55 ? 218 MET C CE 1 +ATOM 6465 N N . VAL C 1 220 ? 21.582 56.983 143.688 1.00 67.27 ? 219 VAL C N 1 +ATOM 6466 C CA . VAL C 1 220 ? 22.744 56.097 143.822 1.00 70.74 ? 219 VAL C CA 1 +ATOM 6467 C C . VAL C 1 220 ? 23.344 55.841 142.437 1.00 45.37 ? 219 VAL C C 1 +ATOM 6468 O O . VAL C 1 220 ? 22.705 55.210 141.587 1.00 76.15 ? 219 VAL C O 1 +ATOM 6469 C CB . VAL C 1 220 ? 22.404 54.732 144.491 1.00 63.58 ? 219 VAL C CB 1 +ATOM 6470 C CG1 . VAL C 1 220 ? 23.660 54.083 145.008 1.00 59.60 ? 219 VAL C CG1 1 +ATOM 6471 C CG2 . VAL C 1 220 ? 21.429 54.908 145.636 1.00 72.26 ? 219 VAL C CG2 1 +ATOM 6472 N N . LEU C 1 221 ? 24.566 56.344 142.228 1.00 71.95 ? 220 LEU C N 1 +ATOM 6473 C CA . LEU C 1 221 ? 25.296 56.247 140.953 1.00 64.00 ? 220 LEU C CA 1 +ATOM 6474 C C . LEU C 1 221 ? 26.414 55.200 140.991 1.00 77.20 ? 220 LEU C C 1 +ATOM 6475 O O . LEU C 1 221 ? 27.240 55.195 141.899 1.00 92.84 ? 220 LEU C O 1 +ATOM 6476 C CB . LEU C 1 221 ? 25.892 57.612 140.552 1.00 55.72 ? 220 LEU C CB 1 +ATOM 6477 C CG . LEU C 1 221 ? 26.817 57.656 139.318 1.00 76.38 ? 220 LEU C CG 1 +ATOM 6478 C CD1 . LEU C 1 221 ? 26.061 57.311 138.053 1.00 63.01 ? 220 LEU C CD1 1 +ATOM 6479 C CD2 . LEU C 1 221 ? 27.546 58.988 139.133 1.00 69.52 ? 220 LEU C CD2 1 +ATOM 6480 N N . LEU C 1 222 ? 26.430 54.323 139.990 1.00 122.70 ? 221 LEU C N 1 +ATOM 6481 C CA . LEU C 1 222 ? 27.487 53.331 139.815 1.00 75.25 ? 221 LEU C CA 1 +ATOM 6482 C C . LEU C 1 222 ? 28.119 53.475 138.442 1.00 84.17 ? 221 LEU C C 1 +ATOM 6483 O O . LEU C 1 222 ? 27.468 53.253 137.425 1.00 77.80 ? 221 LEU C O 1 +ATOM 6484 C CB . LEU C 1 222 ? 26.928 51.922 139.954 1.00 72.97 ? 221 LEU C CB 1 +ATOM 6485 C CG . LEU C 1 222 ? 26.386 51.518 141.318 1.00 94.38 ? 221 LEU C CG 1 +ATOM 6486 C CD1 . LEU C 1 222 ? 25.748 50.166 141.232 1.00 50.91 ? 221 LEU C CD1 1 +ATOM 6487 C CD2 . LEU C 1 222 ? 27.524 51.470 142.292 1.00 70.89 ? 221 LEU C CD2 1 +ATOM 6488 N N . GLU C 1 223 ? 29.393 53.843 138.426 1.00 76.86 ? 222 GLU C N 1 +ATOM 6489 C CA . GLU C 1 223 ? 30.134 54.030 137.188 1.00 85.94 ? 222 GLU C CA 1 +ATOM 6490 C C . GLU C 1 223 ? 31.231 53.002 136.971 1.00 75.77 ? 222 GLU C C 1 +ATOM 6491 O O . GLU C 1 223 ? 31.993 52.680 137.887 1.00 85.73 ? 222 GLU C O 1 +ATOM 6492 C CB . GLU C 1 223 ? 30.792 55.403 137.177 1.00 75.09 ? 222 GLU C CB 1 +ATOM 6493 C CG . GLU C 1 223 ? 29.922 56.511 136.663 1.00 124.75 ? 222 GLU C CG 1 +ATOM 6494 C CD . GLU C 1 223 ? 30.711 57.777 136.350 1.00 164.06 ? 222 GLU C CD 1 +ATOM 6495 O OE1 . GLU C 1 223 ? 31.941 57.686 136.115 1.00 161.08 ? 222 GLU C OE1 1 +ATOM 6496 O OE2 . GLU C 1 223 ? 30.090 58.863 136.338 1.00 165.48 ? 222 GLU C OE2 1 +ATOM 6497 N N . PHE C 1 224 ? 31.319 52.504 135.744 1.00 87.14 ? 223 PHE C N 1 +ATOM 6498 C CA . PHE C 1 224 ? 32.492 51.757 135.312 1.00 74.13 ? 223 PHE C CA 1 +ATOM 6499 C C . PHE C 1 224 ? 33.191 52.611 134.261 1.00 56.64 ? 223 PHE C C 1 +ATOM 6500 O O . PHE C 1 224 ? 32.534 53.202 133.410 1.00 99.89 ? 223 PHE C O 1 +ATOM 6501 C CB . PHE C 1 224 ? 32.113 50.403 134.704 1.00 76.17 ? 223 PHE C CB 1 +ATOM 6502 C CG . PHE C 1 224 ? 31.210 49.558 135.570 1.00 90.38 ? 223 PHE C CG 1 +ATOM 6503 C CD1 . PHE C 1 224 ? 31.180 49.714 136.958 1.00 80.06 ? 223 PHE C CD1 1 +ATOM 6504 C CD2 . PHE C 1 224 ? 30.392 48.596 134.981 1.00 69.81 ? 223 PHE C CD2 1 +ATOM 6505 C CE1 . PHE C 1 224 ? 30.341 48.941 137.739 1.00 69.25 ? 223 PHE C CE1 1 +ATOM 6506 C CE2 . PHE C 1 224 ? 29.554 47.813 135.750 1.00 72.16 ? 223 PHE C CE2 1 +ATOM 6507 C CZ . PHE C 1 224 ? 29.532 47.982 137.136 1.00 97.90 ? 223 PHE C CZ 1 +ATOM 6508 N N . VAL C 1 225 ? 34.516 52.709 134.330 1.00 90.07 ? 224 VAL C N 1 +ATOM 6509 C CA . VAL C 1 225 ? 35.271 53.495 133.355 1.00 83.32 ? 224 VAL C CA 1 +ATOM 6510 C C . VAL C 1 225 ? 36.574 52.793 132.961 1.00 97.36 ? 224 VAL C C 1 +ATOM 6511 O O . VAL C 1 225 ? 37.403 52.510 133.828 1.00 85.21 ? 224 VAL C O 1 +ATOM 6512 C CB . VAL C 1 225 ? 35.643 54.890 133.908 1.00 78.11 ? 224 VAL C CB 1 +ATOM 6513 C CG1 . VAL C 1 225 ? 36.097 55.789 132.782 1.00 84.90 ? 224 VAL C CG1 1 +ATOM 6514 C CG2 . VAL C 1 225 ? 34.473 55.532 134.643 1.00 91.70 ? 224 VAL C CG2 1 +ATOM 6515 N N . THR C 1 226 ? 36.751 52.511 131.666 1.00 93.25 ? 225 THR C N 1 +ATOM 6516 C CA . THR C 1 226 ? 38.022 51.973 131.151 1.00 94.55 ? 225 THR C CA 1 +ATOM 6517 C C . THR C 1 226 ? 38.612 52.785 129.989 1.00 79.68 ? 225 THR C C 1 +ATOM 6518 O O . THR C 1 226 ? 37.929 53.057 129.009 1.00 91.77 ? 225 THR C O 1 +ATOM 6519 C CB . THR C 1 226 ? 37.916 50.495 130.654 1.00 82.70 ? 225 THR C CB 1 +ATOM 6520 O OG1 . THR C 1 226 ? 36.998 49.740 131.453 1.00 72.05 ? 225 THR C OG1 1 +ATOM 6521 C CG2 . THR C 1 226 ? 39.278 49.837 130.706 1.00 96.11 ? 225 THR C CG2 1 +ATOM 6522 N N . ALA C 1 227 ? 39.887 53.150 130.085 1.00 74.57 ? 226 ALA C N 1 +ATOM 6523 C CA . ALA C 1 227 ? 40.592 53.735 128.939 1.00 83.72 ? 226 ALA C CA 1 +ATOM 6524 C C . ALA C 1 227 ? 40.852 52.682 127.837 1.00 99.22 ? 226 ALA C C 1 +ATOM 6525 O O . ALA C 1 227 ? 40.854 51.479 128.110 1.00 108.21 ? 226 ALA C O 1 +ATOM 6526 C CB . ALA C 1 227 ? 41.888 54.401 129.394 1.00 83.29 ? 226 ALA C CB 1 +ATOM 6527 N N . ALA C 1 228 ? 41.068 53.137 126.601 1.00 91.58 ? 227 ALA C N 1 +ATOM 6528 C CA . ALA C 1 228 ? 41.082 52.256 125.428 1.00 94.24 ? 227 ALA C CA 1 +ATOM 6529 C C . ALA C 1 228 ? 41.563 53.018 124.200 1.00 108.51 ? 227 ALA C C 1 +ATOM 6530 O O . ALA C 1 228 ? 42.049 54.134 124.327 1.00 104.75 ? 227 ALA C O 1 +ATOM 6531 C CB . ALA C 1 228 ? 39.687 51.706 125.172 1.00 84.91 ? 227 ALA C CB 1 +ATOM 6532 N N . GLY C 1 229 ? 41.434 52.412 123.020 1.00 110.44 ? 228 GLY C N 1 +ATOM 6533 C CA . GLY C 1 229 ? 41.655 53.112 121.760 1.00 121.51 ? 228 GLY C CA 1 +ATOM 6534 C C . GLY C 1 229 ? 43.075 53.453 121.329 1.00 134.77 ? 228 GLY C C 1 +ATOM 6535 O O . GLY C 1 229 ? 43.276 54.166 120.343 1.00 131.24 ? 228 GLY C O 1 +ATOM 6536 N N . ILE C 1 230 ? 44.056 52.977 122.087 1.00 131.96 ? 229 ILE C N 1 +ATOM 6537 C CA . ILE C 1 230 ? 45.439 52.908 121.626 1.00 136.58 ? 229 ILE C CA 1 +ATOM 6538 C C . ILE C 1 230 ? 45.778 51.420 121.548 1.00 208.82 ? 229 ILE C C 1 +ATOM 6539 O O . ILE C 1 230 ? 45.452 50.671 122.473 1.00 240.23 ? 229 ILE C O 1 +ATOM 6540 C CB . ILE C 1 230 ? 46.409 53.603 122.609 1.00 118.37 ? 229 ILE C CB 1 +ATOM 6541 C CG1 . ILE C 1 230 ? 46.269 55.121 122.526 1.00 113.36 ? 229 ILE C CG1 1 +ATOM 6542 C CG2 . ILE C 1 230 ? 47.849 53.206 122.325 1.00 141.94 ? 229 ILE C CG2 1 +ATOM 6543 C CD1 . ILE C 1 230 ? 47.087 55.860 123.564 1.00 108.75 ? 229 ILE C CD1 1 +ATOM 6544 N N . THR C 1 231 ? 46.402 50.987 120.450 1.00 227.27 ? 230 THR C N 1 +ATOM 6545 C CA . THR C 1 231 ? 46.804 49.580 120.273 1.00 242.80 ? 230 THR C CA 1 +ATOM 6546 C C . THR C 1 231 ? 47.594 49.002 121.462 1.00 249.69 ? 230 THR C C 1 +ATOM 6547 O O . THR C 1 231 ? 48.145 47.901 121.404 1.00 221.57 ? 230 THR C O 1 +ATOM 6548 C CB . THR C 1 231 ? 47.626 49.383 118.975 1.00 219.96 ? 230 THR C CB 1 +ATOM 6549 O OG1 . THR C 1 231 ? 48.040 48.015 118.866 1.00 209.09 ? 230 THR C OG1 1 +ATOM 6550 C CG2 . THR C 1 231 ? 48.859 50.281 118.977 1.00 205.17 ? 230 THR C CG2 1 +ATOM 6551 N N . ALA C 1 235 ? 53.312 54.242 113.795 1.00 142.92 ? 1054 ALA C N 1 +ATOM 6552 C CA . ALA C 1 235 ? 54.036 54.046 112.542 1.00 158.67 ? 1054 ALA C CA 1 +ATOM 6553 C C . ALA C 1 235 ? 54.001 55.286 111.639 1.00 176.69 ? 1054 ALA C C 1 +ATOM 6554 O O . ALA C 1 235 ? 53.794 56.413 112.103 1.00 140.45 ? 1054 ALA C O 1 +ATOM 6555 C CB . ALA C 1 235 ? 53.493 52.820 111.796 1.00 109.63 ? 1054 ALA C CB 1 +ATOM 6556 N N . SER C 1 236 ? 54.222 55.066 110.346 1.00 193.53 ? 1055 SER C N 1 +ATOM 6557 C CA . SER C 1 236 ? 54.081 56.117 109.344 1.00 205.58 ? 1055 SER C CA 1 +ATOM 6558 C C . SER C 1 236 ? 52.642 56.106 108.842 1.00 225.61 ? 1055 SER C C 1 +ATOM 6559 O O . SER C 1 236 ? 52.191 57.030 108.156 1.00 194.60 ? 1055 SER C O 1 +ATOM 6560 C CB . SER C 1 236 ? 55.052 55.888 108.187 1.00 172.73 ? 1055 SER C CB 1 +ATOM 6561 O OG . SER C 1 236 ? 55.048 56.991 107.299 1.00 156.68 ? 1055 SER C OG 1 +ATOM 6562 N N . THR C 1 237 ? 51.931 55.041 109.202 1.00 241.48 ? 1056 THR C N 1 +ATOM 6563 C CA . THR C 1 237 ? 50.506 54.912 108.931 1.00 214.78 ? 1056 THR C CA 1 +ATOM 6564 C C . THR C 1 237 ? 49.744 56.057 109.604 1.00 182.14 ? 1056 THR C C 1 +ATOM 6565 O O . THR C 1 237 ? 48.654 56.433 109.172 1.00 136.67 ? 1056 THR C O 1 +ATOM 6566 C CB . THR C 1 237 ? 49.971 53.539 109.411 1.00 173.42 ? 1056 THR C CB 1 +ATOM 6567 O OG1 . THR C 1 237 ? 49.926 53.502 110.844 1.00 161.56 ? 1056 THR C OG1 1 +ATOM 6568 C CG2 . THR C 1 237 ? 50.868 52.404 108.899 1.00 150.65 ? 1056 THR C CG2 1 +ATOM 6569 N N . LYS C 1 238 ? 50.340 56.602 110.665 1.00 207.67 ? 1057 LYS C N 1 +ATOM 6570 C CA . LYS C 1 238 ? 49.839 57.799 111.333 1.00 192.20 ? 1057 LYS C CA 1 +ATOM 6571 C C . LYS C 1 238 ? 49.691 58.929 110.326 1.00 162.99 ? 1057 LYS C C 1 +ATOM 6572 O O . LYS C 1 238 ? 48.596 59.443 110.121 1.00 135.22 ? 1057 LYS C O 1 +ATOM 6573 C CB . LYS C 1 238 ? 50.790 58.234 112.459 1.00 176.99 ? 1057 LYS C CB 1 +ATOM 6574 C CG . LYS C 1 238 ? 50.505 57.626 113.838 1.00 172.44 ? 1057 LYS C CG 1 +ATOM 6575 C CD . LYS C 1 238 ? 50.628 56.109 113.842 1.00 147.74 ? 1057 LYS C CD 1 +ATOM 6576 C CE . LYS C 1 238 ? 50.539 55.548 115.249 1.00 125.41 ? 1057 LYS C CE 1 +ATOM 6577 N NZ . LYS C 1 238 ? 50.567 54.058 115.262 1.00 124.22 ? 1057 LYS C NZ 1 +ATOM 6578 N N . LYS C 1 239 ? 50.800 59.277 109.680 1.00 176.55 ? 1058 LYS C N 1 +ATOM 6579 C CA . LYS C 1 239 ? 50.874 60.410 108.759 1.00 195.06 ? 1058 LYS C CA 1 +ATOM 6580 C C . LYS C 1 239 ? 49.856 60.354 107.614 1.00 186.41 ? 1058 LYS C C 1 +ATOM 6581 O O . LYS C 1 239 ? 49.456 61.389 107.074 1.00 169.86 ? 1058 LYS C O 1 +ATOM 6582 C CB . LYS C 1 239 ? 52.291 60.514 108.190 1.00 203.60 ? 1058 LYS C CB 1 +ATOM 6583 C CG . LYS C 1 239 ? 53.397 60.568 109.243 1.00 179.76 ? 1058 LYS C CG 1 +ATOM 6584 C CD . LYS C 1 239 ? 54.751 60.835 108.591 1.00 178.63 ? 1058 LYS C CD 1 +ATOM 6585 C CE . LYS C 1 239 ? 54.684 62.053 107.665 1.00 175.83 ? 1058 LYS C CE 1 +ATOM 6586 N NZ . LYS C 1 239 ? 55.868 62.199 106.762 1.00 142.24 ? 1058 LYS C NZ 1 +ATOM 6587 N N . LEU C 1 240 ? 49.440 59.143 107.258 1.00 181.01 ? 1059 LEU C N 1 +ATOM 6588 C CA . LEU C 1 240 ? 48.520 58.917 106.145 1.00 186.36 ? 1059 LEU C CA 1 +ATOM 6589 C C . LEU C 1 240 ? 47.079 59.307 106.465 1.00 178.77 ? 1059 LEU C C 1 +ATOM 6590 O O . LEU C 1 240 ? 46.428 60.026 105.698 1.00 129.87 ? 1059 LEU C O 1 +ATOM 6591 C CB . LEU C 1 240 ? 48.561 57.445 105.736 1.00 191.55 ? 1059 LEU C CB 1 +ATOM 6592 C CG . LEU C 1 240 ? 47.496 56.985 104.743 1.00 175.26 ? 1059 LEU C CG 1 +ATOM 6593 C CD1 . LEU C 1 240 ? 47.632 57.734 103.428 1.00 169.55 ? 1059 LEU C CD1 1 +ATOM 6594 C CD2 . LEU C 1 240 ? 47.616 55.491 104.527 1.00 152.45 ? 1059 LEU C CD2 1 +ATOM 6595 N N . SER C 1 241 ? 46.588 58.810 107.598 1.00 197.64 ? 1060 SER C N 1 +ATOM 6596 C CA . SER C 1 241 ? 45.210 59.031 108.020 1.00 173.16 ? 1060 SER C CA 1 +ATOM 6597 C C . SER C 1 241 ? 45.000 60.469 108.463 1.00 151.26 ? 1060 SER C C 1 +ATOM 6598 O O . SER C 1 241 ? 43.865 60.932 108.564 1.00 143.60 ? 1060 SER C O 1 +ATOM 6599 C CB . SER C 1 241 ? 44.832 58.071 109.150 1.00 139.23 ? 1060 SER C CB 1 +ATOM 6600 O OG . SER C 1 241 ? 45.444 58.444 110.369 1.00 141.28 ? 1060 SER C OG 1 +ATOM 6601 N N . GLU C 1 242 ? 46.096 61.172 108.729 1.00 144.11 ? 1061 GLU C N 1 +ATOM 6602 C CA . GLU C 1 242 ? 46.006 62.582 109.067 1.00 173.31 ? 1061 GLU C CA 1 +ATOM 6603 C C . GLU C 1 242 ? 45.486 63.319 107.849 1.00 156.94 ? 1061 GLU C C 1 +ATOM 6604 O O . GLU C 1 242 ? 44.731 64.284 107.965 1.00 135.34 ? 1061 GLU C O 1 +ATOM 6605 C CB . GLU C 1 242 ? 47.365 63.150 109.483 1.00 178.02 ? 1061 GLU C CB 1 +ATOM 6606 C CG . GLU C 1 242 ? 48.109 62.355 110.557 1.00 183.81 ? 1061 GLU C CG 1 +ATOM 6607 C CD . GLU C 1 242 ? 47.295 62.082 111.822 1.00 190.46 ? 1061 GLU C CD 1 +ATOM 6608 O OE1 . GLU C 1 242 ? 46.358 62.851 112.132 1.00 198.56 ? 1061 GLU C OE1 1 +ATOM 6609 O OE2 . GLU C 1 242 ? 47.608 61.090 112.518 1.00 171.94 ? 1061 GLU C OE2 1 +ATOM 6610 N N . SER C 1 243 ? 45.884 62.838 106.677 1.00 165.79 ? 1062 SER C N 1 +ATOM 6611 C CA . SER C 1 243 ? 45.464 63.433 105.418 1.00 194.60 ? 1062 SER C CA 1 +ATOM 6612 C C . SER C 1 243 ? 44.043 63.016 105.042 1.00 176.14 ? 1062 SER C C 1 +ATOM 6613 O O . SER C 1 243 ? 43.206 63.865 104.708 1.00 118.49 ? 1062 SER C O 1 +ATOM 6614 C CB . SER C 1 243 ? 46.450 63.068 104.308 1.00 205.73 ? 1062 SER C CB 1 +ATOM 6615 O OG . SER C 1 243 ? 47.736 63.593 104.591 1.00 195.87 ? 1062 SER C OG 1 +ATOM 6616 N N . LEU C 1 244 ? 43.778 61.711 105.104 1.00 169.93 ? 1063 LEU C N 1 +ATOM 6617 C CA . LEU C 1 244 ? 42.442 61.185 104.849 1.00 151.42 ? 1063 LEU C CA 1 +ATOM 6618 C C . LEU C 1 244 ? 41.440 61.900 105.731 1.00 160.80 ? 1063 LEU C C 1 +ATOM 6619 O O . LEU C 1 244 ? 40.327 62.207 105.299 1.00 137.33 ? 1063 LEU C O 1 +ATOM 6620 C CB . LEU C 1 244 ? 42.384 59.684 105.110 1.00 123.64 ? 1063 LEU C CB 1 +ATOM 6621 C CG . LEU C 1 244 ? 42.770 58.819 103.916 1.00 145.61 ? 1063 LEU C CG 1 +ATOM 6622 C CD1 . LEU C 1 244 ? 42.575 57.356 104.266 1.00 146.25 ? 1063 LEU C CD1 1 +ATOM 6623 C CD2 . LEU C 1 244 ? 41.952 59.219 102.692 1.00 123.83 ? 1063 LEU C CD2 1 +ATOM 6624 N N . LYS C 1 245 ? 41.859 62.163 106.967 1.00 167.23 ? 1064 LYS C N 1 +ATOM 6625 C CA . LYS C 1 245 ? 41.109 63.014 107.875 1.00 161.38 ? 1064 LYS C CA 1 +ATOM 6626 C C . LYS C 1 245 ? 40.720 64.322 107.194 1.00 165.39 ? 1064 LYS C C 1 +ATOM 6627 O O . LYS C 1 245 ? 39.542 64.551 106.926 1.00 172.60 ? 1064 LYS C O 1 +ATOM 6628 C CB . LYS C 1 245 ? 41.917 63.303 109.144 1.00 140.30 ? 1064 LYS C CB 1 +ATOM 6629 C CG . LYS C 1 245 ? 41.722 62.292 110.270 1.00 164.03 ? 1064 LYS C CG 1 +ATOM 6630 C CD . LYS C 1 245 ? 42.599 62.641 111.471 1.00 193.30 ? 1064 LYS C CD 1 +ATOM 6631 C CE . LYS C 1 245 ? 42.309 61.749 112.673 1.00 184.75 ? 1064 LYS C CE 1 +ATOM 6632 N NZ . LYS C 1 245 ? 43.044 62.167 113.902 1.00 137.19 ? 1064 LYS C NZ 1 +ATOM 6633 N N . ARG C 1 246 ? 41.705 65.165 106.889 1.00 158.97 ? 1065 ARG C N 1 +ATOM 6634 C CA . ARG C 1 246 ? 41.409 66.498 106.361 1.00 175.56 ? 1065 ARG C CA 1 +ATOM 6635 C C . ARG C 1 246 ? 40.625 66.479 105.039 1.00 165.95 ? 1065 ARG C C 1 +ATOM 6636 O O . ARG C 1 246 ? 39.756 67.323 104.826 1.00 145.72 ? 1065 ARG C O 1 +ATOM 6637 C CB . ARG C 1 246 ? 42.674 67.372 106.256 1.00 171.33 ? 1065 ARG C CB 1 +ATOM 6638 C CG . ARG C 1 246 ? 43.312 67.774 107.585 1.00 184.44 ? 1065 ARG C CG 1 +ATOM 6639 C CD . ARG C 1 246 ? 44.526 68.680 107.358 1.00 204.62 ? 1065 ARG C CD 1 +ATOM 6640 N NE . ARG C 1 246 ? 45.210 69.029 108.605 1.00 225.65 ? 1065 ARG C NE 1 +ATOM 6641 C CZ . ARG C 1 246 ? 46.353 69.710 108.676 1.00 203.12 ? 1065 ARG C CZ 1 +ATOM 6642 N NH1 . ARG C 1 246 ? 46.956 70.125 107.569 1.00 182.57 ? 1065 ARG C NH1 1 +ATOM 6643 N NH2 . ARG C 1 246 ? 46.896 69.979 109.859 1.00 156.89 ? 1065 ARG C NH2 1 +ATOM 6644 N N . ILE C 1 247 ? 40.907 65.506 104.176 1.00 152.25 ? 1066 ILE C N 1 +ATOM 6645 C CA . ILE C 1 247 ? 40.233 65.411 102.877 1.00 153.18 ? 1066 ILE C CA 1 +ATOM 6646 C C . ILE C 1 247 ? 38.723 65.155 103.028 1.00 156.23 ? 1066 ILE C C 1 +ATOM 6647 O O . ILE C 1 247 ? 37.907 65.741 102.308 1.00 110.56 ? 1066 ILE C O 1 +ATOM 6648 C CB . ILE C 1 247 ? 40.920 64.353 101.953 1.00 153.53 ? 1066 ILE C CB 1 +ATOM 6649 C CG1 . ILE C 1 247 ? 42.339 64.810 101.563 1.00 190.99 ? 1066 ILE C CG1 1 +ATOM 6650 C CG2 . ILE C 1 247 ? 40.076 64.056 100.722 1.00 102.72 ? 1066 ILE C CG2 1 +ATOM 6651 C CD1 . ILE C 1 247 ? 43.204 63.758 100.888 1.00 206.49 ? 1066 ILE C CD1 1 +ATOM 6652 N N . GLY C 1 248 ? 38.361 64.298 103.978 1.00 166.38 ? 1067 GLY C N 1 +ATOM 6653 C CA . GLY C 1 248 ? 36.964 64.058 104.289 1.00 144.39 ? 1067 GLY C CA 1 +ATOM 6654 C C . GLY C 1 248 ? 36.430 65.208 105.118 1.00 156.03 ? 1067 GLY C C 1 +ATOM 6655 O O . GLY C 1 248 ? 35.222 65.450 105.179 1.00 139.06 ? 1067 GLY C O 1 +ATOM 6656 N N . ASP C 1 249 ? 37.349 65.926 105.757 1.00 167.43 ? 1068 ASP C N 1 +ATOM 6657 C CA . ASP C 1 249 ? 36.985 67.031 106.633 1.00 159.35 ? 1068 ASP C CA 1 +ATOM 6658 C C . ASP C 1 249 ? 36.604 68.275 105.844 1.00 157.58 ? 1068 ASP C C 1 +ATOM 6659 O O . ASP C 1 249 ? 35.472 68.749 105.955 1.00 131.57 ? 1068 ASP C O 1 +ATOM 6660 C CB . ASP C 1 249 ? 38.108 67.334 107.626 1.00 165.27 ? 1068 ASP C CB 1 +ATOM 6661 C CG . ASP C 1 249 ? 38.080 66.414 108.836 1.00 185.46 ? 1068 ASP C CG 1 +ATOM 6662 O OD1 . ASP C 1 249 ? 37.369 65.387 108.791 1.00 189.61 ? 1068 ASP C OD1 1 +ATOM 6663 O OD2 . ASP C 1 249 ? 38.770 66.716 109.833 1.00 181.25 ? 1068 ASP C OD2 1 +ATOM 6664 N N . GLU C 1 250 ? 37.547 68.791 105.051 1.00 183.85 ? 1069 GLU C N 1 +ATOM 6665 C CA . GLU C 1 250 ? 37.302 69.925 104.154 1.00 190.75 ? 1069 GLU C CA 1 +ATOM 6666 C C . GLU C 1 250 ? 36.055 69.661 103.316 1.00 167.87 ? 1069 GLU C C 1 +ATOM 6667 O O . GLU C 1 250 ? 35.273 70.565 103.021 1.00 106.35 ? 1069 GLU C O 1 +ATOM 6668 C CB . GLU C 1 250 ? 38.502 70.150 103.222 1.00 179.14 ? 1069 GLU C CB 1 +ATOM 6669 C CG . GLU C 1 250 ? 39.825 70.448 103.924 1.00 199.01 ? 1069 GLU C CG 1 +ATOM 6670 C CD . GLU C 1 250 ? 41.033 70.250 103.015 1.00 198.35 ? 1069 GLU C CD 1 +ATOM 6671 O OE1 . GLU C 1 250 ? 40.835 69.994 101.807 1.00 173.12 ? 1069 GLU C OE1 1 +ATOM 6672 O OE2 . GLU C 1 250 ? 42.179 70.341 103.511 1.00 186.76 ? 1069 GLU C OE2 1 +ATOM 6673 N N . LEU C 1 251 ? 35.889 68.395 102.950 1.00 165.19 ? 1070 LEU C N 1 +ATOM 6674 C CA . LEU C 1 251 ? 34.738 67.920 102.199 1.00 149.64 ? 1070 LEU C CA 1 +ATOM 6675 C C . LEU C 1 251 ? 33.426 68.149 102.954 1.00 157.02 ? 1070 LEU C C 1 +ATOM 6676 O O . LEU C 1 251 ? 32.512 68.804 102.447 1.00 103.61 ? 1070 LEU C O 1 +ATOM 6677 C CB . LEU C 1 251 ? 34.936 66.435 101.885 1.00 142.54 ? 1070 LEU C CB 1 +ATOM 6678 C CG . LEU C 1 251 ? 33.971 65.682 100.969 1.00 147.57 ? 1070 LEU C CG 1 +ATOM 6679 C CD1 . LEU C 1 251 ? 33.469 66.556 99.820 1.00 136.93 ? 1070 LEU C CD1 1 +ATOM 6680 C CD2 . LEU C 1 251 ? 34.639 64.395 100.450 1.00 106.64 ? 1070 LEU C CD2 1 +ATOM 6681 N N . ASP C 1 252 ? 33.332 67.622 104.169 1.00 177.47 ? 1071 ASP C N 1 +ATOM 6682 C CA . ASP C 1 252 ? 32.089 67.741 104.917 1.00 157.53 ? 1071 ASP C CA 1 +ATOM 6683 C C . ASP C 1 252 ? 31.867 69.166 105.431 1.00 155.87 ? 1071 ASP C C 1 +ATOM 6684 O O . ASP C 1 252 ? 30.732 69.571 105.710 1.00 135.26 ? 1071 ASP C O 1 +ATOM 6685 C CB . ASP C 1 252 ? 32.022 66.714 106.048 1.00 119.00 ? 1071 ASP C CB 1 +ATOM 6686 C CG . ASP C 1 252 ? 30.722 66.797 106.834 1.00 202.30 ? 1071 ASP C CG 1 +ATOM 6687 O OD1 . ASP C 1 252 ? 29.642 66.529 106.257 1.00 193.16 ? 1071 ASP C OD1 1 +ATOM 6688 O OD2 . ASP C 1 252 ? 30.779 67.130 108.035 1.00 245.68 ? 1071 ASP C OD2 1 +ATOM 6689 N N . SER C 1 253 ? 32.952 69.931 105.518 1.00 160.40 ? 1072 SER C N 1 +ATOM 6690 C CA . SER C 1 253 ? 32.877 71.305 106.012 1.00 184.86 ? 1072 SER C CA 1 +ATOM 6691 C C . SER C 1 253 ? 32.816 72.357 104.901 1.00 195.91 ? 1072 SER C C 1 +ATOM 6692 O O . SER C 1 253 ? 32.603 73.535 105.183 1.00 180.93 ? 1072 SER C O 1 +ATOM 6693 C CB . SER C 1 253 ? 34.034 71.616 106.977 1.00 183.53 ? 1072 SER C CB 1 +ATOM 6694 O OG . SER C 1 253 ? 35.261 71.826 106.295 1.00 180.22 ? 1072 SER C OG 1 +ATOM 6695 N N . ASN C 1 254 ? 33.007 71.936 103.650 1.00 218.98 ? 1073 ASN C N 1 +ATOM 6696 C CA . ASN C 1 254 ? 32.926 72.848 102.503 1.00 218.55 ? 1073 ASN C CA 1 +ATOM 6697 C C . ASN C 1 254 ? 31.526 73.433 102.355 1.00 210.64 ? 1073 ASN C C 1 +ATOM 6698 O O . ASN C 1 254 ? 30.627 72.791 101.808 1.00 173.22 ? 1073 ASN C O 1 +ATOM 6699 C CB . ASN C 1 254 ? 33.326 72.141 101.204 1.00 210.12 ? 1073 ASN C CB 1 +ATOM 6700 C CG . ASN C 1 254 ? 34.384 72.901 100.426 1.00 189.43 ? 1073 ASN C CG 1 +ATOM 6701 O OD1 . ASN C 1 254 ? 35.221 73.592 101.008 1.00 185.60 ? 1073 ASN C OD1 1 +ATOM 6702 N ND2 . ASN C 1 254 ? 34.354 72.774 99.102 1.00 171.19 ? 1073 ASN C ND2 1 +ATOM 6703 N N . MET C 1 255 ? 31.350 74.657 102.843 1.00 231.29 ? 1074 MET C N 1 +ATOM 6704 C CA . MET C 1 255 ? 30.028 75.270 102.916 1.00 234.55 ? 1074 MET C CA 1 +ATOM 6705 C C . MET C 1 255 ? 29.399 75.531 101.550 1.00 222.91 ? 1074 MET C C 1 +ATOM 6706 O O . MET C 1 255 ? 28.173 75.596 101.436 1.00 193.08 ? 1074 MET C O 1 +ATOM 6707 C CB . MET C 1 255 ? 30.067 76.556 103.747 1.00 236.95 ? 1074 MET C CB 1 +ATOM 6708 C CG . MET C 1 255 ? 30.202 76.318 105.248 1.00 231.17 ? 1074 MET C CG 1 +ATOM 6709 S SD . MET C 1 255 ? 28.927 75.222 105.911 1.00 248.46 ? 1074 MET C SD 1 +ATOM 6710 C CE . MET C 1 255 ? 27.433 76.149 105.553 1.00 135.37 ? 1074 MET C CE 1 +ATOM 6711 N N . GLU C 1 256 ? 30.237 75.685 100.526 1.00 231.81 ? 1075 GLU C N 1 +ATOM 6712 C CA . GLU C 1 256 ? 29.762 75.843 99.155 1.00 219.28 ? 1075 GLU C CA 1 +ATOM 6713 C C . GLU C 1 256 ? 28.899 74.650 98.809 1.00 194.84 ? 1075 GLU C C 1 +ATOM 6714 O O . GLU C 1 256 ? 27.714 74.777 98.491 1.00 163.23 ? 1075 GLU C O 1 +ATOM 6715 C CB . GLU C 1 256 ? 30.931 75.847 98.174 1.00 218.96 ? 1075 GLU C CB 1 +ATOM 6716 C CG . GLU C 1 256 ? 32.065 76.781 98.507 1.00 214.24 ? 1075 GLU C CG 1 +ATOM 6717 C CD . GLU C 1 256 ? 33.241 76.585 97.572 1.00 212.68 ? 1075 GLU C CD 1 +ATOM 6718 O OE1 . GLU C 1 256 ? 33.459 75.438 97.125 1.00 215.81 ? 1075 GLU C OE1 1 +ATOM 6719 O OE2 . GLU C 1 256 ? 33.938 77.577 97.274 1.00 201.02 ? 1075 GLU C OE2 1 +ATOM 6720 N N . LEU C 1 257 ? 29.535 73.486 98.889 1.00 181.44 ? 1076 LEU C N 1 +ATOM 6721 C CA . LEU C 1 257 ? 28.953 72.206 98.519 1.00 174.63 ? 1076 LEU C CA 1 +ATOM 6722 C C . LEU C 1 257 ? 27.724 71.834 99.353 1.00 170.74 ? 1076 LEU C C 1 +ATOM 6723 O O . LEU C 1 257 ? 26.691 71.443 98.802 1.00 122.33 ? 1076 LEU C O 1 +ATOM 6724 C CB . LEU C 1 257 ? 30.036 71.128 98.621 1.00 160.04 ? 1076 LEU C CB 1 +ATOM 6725 C CG . LEU C 1 257 ? 29.679 69.658 98.417 1.00 158.95 ? 1076 LEU C CG 1 +ATOM 6726 C CD1 . LEU C 1 257 ? 28.907 69.455 97.123 1.00 139.57 ? 1076 LEU C CD1 1 +ATOM 6727 C CD2 . LEU C 1 257 ? 30.947 68.827 98.440 1.00 172.98 ? 1076 LEU C CD2 1 +ATOM 6728 N N . GLN C 1 258 ? 27.837 71.960 100.675 1.00 176.98 ? 1077 GLN C N 1 +ATOM 6729 C CA . GLN C 1 258 ? 26.745 71.591 101.572 1.00 169.79 ? 1077 GLN C CA 1 +ATOM 6730 C C . GLN C 1 258 ? 25.482 72.398 101.251 1.00 177.86 ? 1077 GLN C C 1 +ATOM 6731 O O . GLN C 1 258 ? 24.380 71.846 101.180 1.00 169.62 ? 1077 GLN C O 1 +ATOM 6732 C CB . GLN C 1 258 ? 27.160 71.757 103.041 1.00 147.09 ? 1077 GLN C CB 1 +ATOM 6733 C CG . GLN C 1 258 ? 28.406 70.952 103.460 1.00 170.40 ? 1077 GLN C CG 1 +ATOM 6734 C CD . GLN C 1 258 ? 28.212 69.434 103.421 1.00 168.22 ? 1077 GLN C CD 1 +ATOM 6735 O OE1 . GLN C 1 258 ? 27.121 68.922 103.682 1.00 166.96 ? 1077 GLN C OE1 1 +ATOM 6736 N NE2 . GLN C 1 258 ? 29.283 68.712 103.097 1.00 121.04 ? 1077 GLN C NE2 1 +ATOM 6737 N N . ARG C 1 259 ? 25.662 73.699 101.032 1.00 171.62 ? 1078 ARG C N 1 +ATOM 6738 C CA . ARG C 1 259 ? 24.576 74.577 100.605 1.00 175.73 ? 1078 ARG C CA 1 +ATOM 6739 C C . ARG C 1 259 ? 23.994 74.093 99.282 1.00 183.26 ? 1078 ARG C C 1 +ATOM 6740 O O . ARG C 1 259 ? 22.778 73.967 99.141 1.00 176.62 ? 1078 ARG C O 1 +ATOM 6741 C CB . ARG C 1 259 ? 25.085 76.013 100.440 1.00 195.68 ? 1078 ARG C CB 1 +ATOM 6742 C CG . ARG C 1 259 ? 23.998 77.049 100.141 1.00 198.12 ? 1078 ARG C CG 1 +ATOM 6743 C CD . ARG C 1 259 ? 24.488 78.132 99.173 1.00 214.66 ? 1078 ARG C CD 1 +ATOM 6744 N NE . ARG C 1 259 ? 25.665 78.851 99.663 1.00 223.00 ? 1078 ARG C NE 1 +ATOM 6745 C CZ . ARG C 1 259 ? 26.694 79.214 98.900 1.00 200.88 ? 1078 ARG C CZ 1 +ATOM 6746 N NH1 . ARG C 1 259 ? 26.702 78.923 97.604 1.00 178.44 ? 1078 ARG C NH1 1 +ATOM 6747 N NH2 . ARG C 1 259 ? 27.720 79.866 99.435 1.00 161.40 ? 1078 ARG C NH2 1 +ATOM 6748 N N . MET C 1 260 ? 24.883 73.820 98.326 1.00 184.23 ? 1079 MET C N 1 +ATOM 6749 C CA . MET C 1 260 ? 24.517 73.410 96.967 1.00 185.74 ? 1079 MET C CA 1 +ATOM 6750 C C . MET C 1 260 ? 23.625 72.174 96.922 1.00 193.15 ? 1079 MET C C 1 +ATOM 6751 O O . MET C 1 260 ? 22.680 72.110 96.131 1.00 192.55 ? 1079 MET C O 1 +ATOM 6752 C CB . MET C 1 260 ? 25.781 73.137 96.136 1.00 172.80 ? 1079 MET C CB 1 +ATOM 6753 C CG . MET C 1 260 ? 26.016 74.083 94.960 1.00 144.06 ? 1079 MET C CG 1 +ATOM 6754 S SD . MET C 1 260 ? 27.425 73.603 93.919 1.00 242.14 ? 1079 MET C SD 1 +ATOM 6755 C CE . MET C 1 260 ? 28.838 73.974 94.966 1.00 92.26 ? 1079 MET C CE 1 +ATOM 6756 N N . ILE C 1 261 ? 23.934 71.184 97.754 1.00 179.43 ? 1080 ILE C N 1 +ATOM 6757 C CA . ILE C 1 261 ? 23.197 69.928 97.702 1.00 185.48 ? 1080 ILE C CA 1 +ATOM 6758 C C . ILE C 1 261 ? 21.876 70.029 98.439 1.00 189.20 ? 1080 ILE C C 1 +ATOM 6759 O O . ILE C 1 261 ? 20.867 69.488 97.985 1.00 203.86 ? 1080 ILE C O 1 +ATOM 6760 C CB . ILE C 1 261 ? 23.992 68.749 98.268 1.00 165.87 ? 1080 ILE C CB 1 +ATOM 6761 C CG1 . ILE C 1 261 ? 25.449 68.825 97.820 1.00 139.05 ? 1080 ILE C CG1 1 +ATOM 6762 C CG2 . ILE C 1 261 ? 23.385 67.437 97.853 1.00 171.56 ? 1080 ILE C CG2 1 +ATOM 6763 C CD1 . ILE C 1 261 ? 26.226 67.572 98.113 1.00 140.92 ? 1080 ILE C CD1 1 +ATOM 6764 N N . ALA C 1 262 ? 21.893 70.711 99.582 1.00 158.83 ? 1081 ALA C N 1 +ATOM 6765 C CA . ALA C 1 262 ? 20.668 71.012 100.307 1.00 165.72 ? 1081 ALA C CA 1 +ATOM 6766 C C . ALA C 1 262 ? 19.706 71.708 99.348 1.00 192.43 ? 1081 ALA C C 1 +ATOM 6767 O O . ALA C 1 262 ? 18.529 71.356 99.267 1.00 190.85 ? 1081 ALA C O 1 +ATOM 6768 C CB . ALA C 1 262 ? 20.964 71.888 101.519 1.00 128.18 ? 1081 ALA C CB 1 +ATOM 6769 N N . ALA C 1 263 ? 20.226 72.674 98.599 1.00 187.59 ? 1082 ALA C N 1 +ATOM 6770 C CA . ALA C 1 263 ? 19.455 73.318 97.545 1.00 192.70 ? 1082 ALA C CA 1 +ATOM 6771 C C . ALA C 1 263 ? 19.317 72.401 96.326 1.00 222.07 ? 1082 ALA C C 1 +ATOM 6772 O O . ALA C 1 263 ? 20.041 72.549 95.337 1.00 211.60 ? 1082 ALA C O 1 +ATOM 6773 C CB . ALA C 1 263 ? 20.089 74.652 97.153 1.00 181.22 ? 1082 ALA C CB 1 +ATOM 6774 N N . VAL C 1 264 ? 18.395 71.444 96.416 1.00 237.87 ? 1083 VAL C N 1 +ATOM 6775 C CA . VAL C 1 264 ? 18.014 70.616 95.269 1.00 239.34 ? 1083 VAL C CA 1 +ATOM 6776 C C . VAL C 1 264 ? 16.605 70.027 95.453 1.00 212.74 ? 1083 VAL C C 1 +ATOM 6777 O O . VAL C 1 264 ? 16.176 69.745 96.578 1.00 155.60 ? 1083 VAL C O 1 +ATOM 6778 C CB . VAL C 1 264 ? 19.028 69.519 94.955 1.00 210.63 ? 1083 VAL C CB 1 +ATOM 6779 C CG1 . VAL C 1 264 ? 18.868 68.315 95.913 1.00 184.36 ? 1083 VAL C CG1 1 +ATOM 6780 C CG2 . VAL C 1 264 ? 18.971 69.064 93.501 1.00 189.24 ? 1083 VAL C CG2 1 +ATOM 6781 N N . ASP C 1 265 ? 15.884 69.872 94.344 1.00 219.81 ? 1084 ASP C N 1 +ATOM 6782 C CA . ASP C 1 265 ? 14.508 69.376 94.375 1.00 232.34 ? 1084 ASP C CA 1 +ATOM 6783 C C . ASP C 1 265 ? 14.470 67.852 94.314 1.00 230.76 ? 1084 ASP C C 1 +ATOM 6784 O O . ASP C 1 265 ? 14.670 67.250 93.257 1.00 190.19 ? 1084 ASP C O 1 +ATOM 6785 C CB . ASP C 1 265 ? 13.689 69.979 93.231 1.00 232.89 ? 1084 ASP C CB 1 +ATOM 6786 C CG . ASP C 1 265 ? 12.205 70.043 93.547 1.00 214.35 ? 1084 ASP C CG 1 +ATOM 6787 O OD1 . ASP C 1 265 ? 11.696 69.117 94.215 1.00 212.42 ? 1084 ASP C OD1 1 +ATOM 6788 O OD2 . ASP C 1 265 ? 11.548 71.024 93.134 1.00 185.29 ? 1084 ASP C OD2 1 +ATOM 6789 N N . THR C 1 266 ? 14.189 67.239 95.460 1.00 249.72 ? 1085 THR C N 1 +ATOM 6790 C CA . THR C 1 266 ? 14.345 65.800 95.624 1.00 265.74 ? 1085 THR C CA 1 +ATOM 6791 C C . THR C 1 266 ? 13.049 65.094 96.046 1.00 267.67 ? 1085 THR C C 1 +ATOM 6792 O O . THR C 1 266 ? 13.061 64.102 96.775 1.00 270.85 ? 1085 THR C O 1 +ATOM 6793 C CB . THR C 1 266 ? 15.461 65.493 96.648 1.00 267.74 ? 1085 THR C CB 1 +ATOM 6794 O OG1 . THR C 1 266 ? 16.704 66.029 96.179 1.00 263.60 ? 1085 THR C OG1 1 +ATOM 6795 C CG2 . THR C 1 266 ? 15.635 63.999 96.854 1.00 264.01 ? 1085 THR C CG2 1 +ATOM 6796 N N . ASP C 1 267 ? 11.912 65.610 95.590 1.00 258.93 ? 1086 ASP C N 1 +ATOM 6797 C CA . ASP C 1 267 ? 10.634 64.933 95.794 1.00 245.64 ? 1086 ASP C CA 1 +ATOM 6798 C C . ASP C 1 267 ? 10.510 63.850 94.732 1.00 236.92 ? 1086 ASP C C 1 +ATOM 6799 O O . ASP C 1 267 ? 9.978 62.765 94.976 1.00 203.78 ? 1086 ASP C O 1 +ATOM 6800 C CB . ASP C 1 267 ? 9.473 65.920 95.677 1.00 237.92 ? 1086 ASP C CB 1 +ATOM 6801 C CG . ASP C 1 267 ? 9.703 67.184 96.478 1.00 242.80 ? 1086 ASP C CG 1 +ATOM 6802 O OD1 . ASP C 1 267 ? 10.586 67.177 97.360 1.00 246.49 ? 1086 ASP C OD1 1 +ATOM 6803 O OD2 . ASP C 1 267 ? 8.998 68.184 96.227 1.00 239.41 ? 1086 ASP C OD2 1 +ATOM 6804 N N . SER C 1 268 ? 11.011 64.176 93.545 1.00 246.42 ? 1087 SER C N 1 +ATOM 6805 C CA . SER C 1 268 ? 11.188 63.221 92.463 1.00 234.85 ? 1087 SER C CA 1 +ATOM 6806 C C . SER C 1 268 ? 12.696 63.047 92.280 1.00 253.15 ? 1087 SER C C 1 +ATOM 6807 O O . SER C 1 268 ? 13.283 63.620 91.361 1.00 235.91 ? 1087 SER C O 1 +ATOM 6808 C CB . SER C 1 268 ? 10.545 63.759 91.182 1.00 186.73 ? 1087 SER C CB 1 +ATOM 6809 O OG . SER C 1 268 ? 10.614 62.817 90.127 1.00 162.30 ? 1087 SER C OG 1 +ATOM 6810 N N . PRO C 1 269 ? 13.327 62.254 93.168 1.00 256.83 ? 1088 PRO C N 1 +ATOM 6811 C CA . PRO C 1 269 ? 14.787 62.176 93.306 1.00 224.40 ? 1088 PRO C CA 1 +ATOM 6812 C C . PRO C 1 269 ? 15.495 61.387 92.203 1.00 222.33 ? 1088 PRO C C 1 +ATOM 6813 O O . PRO C 1 269 ? 16.586 61.785 91.792 1.00 210.69 ? 1088 PRO C O 1 +ATOM 6814 C CB . PRO C 1 269 ? 14.966 61.464 94.649 1.00 183.51 ? 1088 PRO C CB 1 +ATOM 6815 C CG . PRO C 1 269 ? 13.763 60.603 94.775 1.00 201.96 ? 1088 PRO C CG 1 +ATOM 6816 C CD . PRO C 1 269 ? 12.638 61.335 94.094 1.00 238.68 ? 1088 PRO C CD 1 +ATOM 6817 N N . ARG C 1 270 ? 14.879 60.297 91.745 1.00 223.97 ? 1089 ARG C N 1 +ATOM 6818 C CA . ARG C 1 270 ? 15.473 59.372 90.774 1.00 204.65 ? 1089 ARG C CA 1 +ATOM 6819 C C . ARG C 1 270 ? 16.036 60.030 89.503 1.00 206.77 ? 1089 ARG C C 1 +ATOM 6820 O O . ARG C 1 270 ? 17.146 59.704 89.065 1.00 140.83 ? 1089 ARG C O 1 +ATOM 6821 C CB . ARG C 1 270 ? 14.462 58.275 90.416 1.00 172.27 ? 1089 ARG C CB 1 +ATOM 6822 C CG . ARG C 1 270 ? 14.628 57.712 89.021 1.00 188.17 ? 1089 ARG C CG 1 +ATOM 6823 C CD . ARG C 1 270 ? 13.685 56.553 88.758 1.00 186.85 ? 1089 ARG C CD 1 +ATOM 6824 N NE . ARG C 1 270 ? 13.689 56.169 87.347 1.00 197.99 ? 1089 ARG C NE 1 +ATOM 6825 C CZ . ARG C 1 270 ? 14.632 55.428 86.769 1.00 195.69 ? 1089 ARG C CZ 1 +ATOM 6826 N NH1 . ARG C 1 270 ? 15.662 54.986 87.479 1.00 200.62 ? 1089 ARG C NH1 1 +ATOM 6827 N NH2 . ARG C 1 270 ? 14.548 55.130 85.478 1.00 162.70 ? 1089 ARG C NH2 1 +ATOM 6828 N N . GLU C 1 271 ? 15.273 60.951 88.921 1.00 230.83 ? 1090 GLU C N 1 +ATOM 6829 C CA . GLU C 1 271 ? 15.722 61.684 87.740 1.00 225.25 ? 1090 GLU C CA 1 +ATOM 6830 C C . GLU C 1 271 ? 16.899 62.588 88.088 1.00 221.27 ? 1090 GLU C C 1 +ATOM 6831 O O . GLU C 1 271 ? 17.883 62.651 87.348 1.00 191.46 ? 1090 GLU C O 1 +ATOM 6832 C CB . GLU C 1 271 ? 14.591 62.547 87.177 1.00 228.81 ? 1090 GLU C CB 1 +ATOM 6833 C CG . GLU C 1 271 ? 13.226 61.884 87.140 1.00 237.43 ? 1090 GLU C CG 1 +ATOM 6834 C CD . GLU C 1 271 ? 12.111 62.879 86.849 1.00 240.19 ? 1090 GLU C CD 1 +ATOM 6835 O OE1 . GLU C 1 271 ? 12.416 63.996 86.377 1.00 229.68 ? 1090 GLU C OE1 1 +ATOM 6836 O OE2 . GLU C 1 271 ? 10.932 62.548 87.099 1.00 238.52 ? 1090 GLU C OE2 1 +ATOM 6837 N N . VAL C 1 272 ? 16.780 63.287 89.219 1.00 236.45 ? 1091 VAL C N 1 +ATOM 6838 C CA . VAL C 1 272 ? 17.767 64.279 89.655 1.00 231.70 ? 1091 VAL C CA 1 +ATOM 6839 C C . VAL C 1 272 ? 19.175 63.692 89.746 1.00 227.58 ? 1091 VAL C C 1 +ATOM 6840 O O . VAL C 1 272 ? 20.142 64.297 89.285 1.00 221.23 ? 1091 VAL C O 1 +ATOM 6841 C CB . VAL C 1 272 ? 17.378 64.910 91.020 1.00 179.59 ? 1091 VAL C CB 1 +ATOM 6842 C CG1 . VAL C 1 272 ? 18.295 66.082 91.353 1.00 171.95 ? 1091 VAL C CG1 1 +ATOM 6843 C CG2 . VAL C 1 272 ? 15.925 65.360 91.008 1.00 167.65 ? 1091 VAL C CG2 1 +ATOM 6844 N N . PHE C 1 273 ? 19.281 62.506 90.335 1.00 228.22 ? 1092 PHE C N 1 +ATOM 6845 C CA . PHE C 1 273 ? 20.561 61.822 90.449 1.00 221.41 ? 1092 PHE C CA 1 +ATOM 6846 C C . PHE C 1 273 ? 21.104 61.461 89.071 1.00 201.65 ? 1092 PHE C C 1 +ATOM 6847 O O . PHE C 1 273 ? 22.229 61.822 88.726 1.00 199.01 ? 1092 PHE C O 1 +ATOM 6848 C CB . PHE C 1 273 ? 20.415 60.566 91.314 1.00 235.70 ? 1092 PHE C CB 1 +ATOM 6849 C CG . PHE C 1 273 ? 21.635 59.688 91.330 1.00 238.93 ? 1092 PHE C CG 1 +ATOM 6850 C CD1 . PHE C 1 273 ? 22.765 60.060 92.039 1.00 228.51 ? 1092 PHE C CD1 1 +ATOM 6851 C CD2 . PHE C 1 273 ? 21.650 58.487 90.636 1.00 234.83 ? 1092 PHE C CD2 1 +ATOM 6852 C CE1 . PHE C 1 273 ? 23.887 59.255 92.052 1.00 210.46 ? 1092 PHE C CE1 1 +ATOM 6853 C CE2 . PHE C 1 273 ? 22.770 57.677 90.650 1.00 222.54 ? 1092 PHE C CE2 1 +ATOM 6854 C CZ . PHE C 1 273 ? 23.887 58.060 91.360 1.00 206.85 ? 1092 PHE C CZ 1 +ATOM 6855 N N . PHE C 1 274 ? 20.289 60.762 88.285 1.00 174.80 ? 1093 PHE C N 1 +ATOM 6856 C CA . PHE C 1 274 ? 20.704 60.266 86.976 1.00 200.23 ? 1093 PHE C CA 1 +ATOM 6857 C C . PHE C 1 274 ? 21.215 61.358 86.032 1.00 214.66 ? 1093 PHE C C 1 +ATOM 6858 O O . PHE C 1 274 ? 22.216 61.165 85.341 1.00 207.91 ? 1093 PHE C O 1 +ATOM 6859 C CB . PHE C 1 274 ? 19.555 59.495 86.315 1.00 226.07 ? 1093 PHE C CB 1 +ATOM 6860 C CG . PHE C 1 274 ? 19.873 59.007 84.926 1.00 238.72 ? 1093 PHE C CG 1 +ATOM 6861 C CD1 . PHE C 1 274 ? 20.621 57.854 84.737 1.00 209.62 ? 1093 PHE C CD1 1 +ATOM 6862 C CD2 . PHE C 1 274 ? 19.424 59.702 83.809 1.00 229.30 ? 1093 PHE C CD2 1 +ATOM 6863 C CE1 . PHE C 1 274 ? 20.917 57.403 83.460 1.00 199.88 ? 1093 PHE C CE1 1 +ATOM 6864 C CE2 . PHE C 1 274 ? 19.718 59.257 82.530 1.00 183.40 ? 1093 PHE C CE2 1 +ATOM 6865 C CZ . PHE C 1 274 ? 20.464 58.106 82.356 1.00 181.54 ? 1093 PHE C CZ 1 +ATOM 6866 N N . ARG C 1 275 ? 20.530 62.500 86.000 1.00 216.68 ? 1094 ARG C N 1 +ATOM 6867 C CA . ARG C 1 275 ? 20.916 63.581 85.095 1.00 206.92 ? 1094 ARG C CA 1 +ATOM 6868 C C . ARG C 1 275 ? 22.221 64.213 85.557 1.00 193.26 ? 1094 ARG C C 1 +ATOM 6869 O O . ARG C 1 275 ? 23.092 64.515 84.741 1.00 192.68 ? 1094 ARG C O 1 +ATOM 6870 C CB . ARG C 1 275 ? 19.818 64.647 84.987 1.00 216.10 ? 1094 ARG C CB 1 +ATOM 6871 C CG . ARG C 1 275 ? 19.691 65.286 83.598 1.00 213.21 ? 1094 ARG C CG 1 +ATOM 6872 C CD . ARG C 1 275 ? 18.758 66.495 83.614 1.00 209.96 ? 1094 ARG C CD 1 +ATOM 6873 N NE . ARG C 1 275 ? 17.723 66.373 84.639 1.00 214.13 ? 1094 ARG C NE 1 +ATOM 6874 C CZ . ARG C 1 275 ? 16.511 65.864 84.433 1.00 191.96 ? 1094 ARG C CZ 1 +ATOM 6875 N NH1 . ARG C 1 275 ? 16.165 65.429 83.226 1.00 141.45 ? 1094 ARG C NH1 1 +ATOM 6876 N NH2 . ARG C 1 275 ? 15.644 65.793 85.439 1.00 168.53 ? 1094 ARG C NH2 1 +ATOM 6877 N N . VAL C 1 276 ? 22.348 64.409 86.868 1.00 176.02 ? 1095 VAL C N 1 +ATOM 6878 C CA . VAL C 1 276 ? 23.573 64.940 87.457 1.00 171.74 ? 1095 VAL C CA 1 +ATOM 6879 C C . VAL C 1 276 ? 24.711 63.952 87.257 1.00 171.07 ? 1095 VAL C C 1 +ATOM 6880 O O . VAL C 1 276 ? 25.864 64.345 87.054 1.00 157.66 ? 1095 VAL C O 1 +ATOM 6881 C CB . VAL C 1 276 ? 23.399 65.233 88.959 1.00 179.27 ? 1095 VAL C CB 1 +ATOM 6882 C CG1 . VAL C 1 276 ? 24.740 65.496 89.619 1.00 152.24 ? 1095 VAL C CG1 1 +ATOM 6883 C CG2 . VAL C 1 276 ? 22.479 66.419 89.155 1.00 212.33 ? 1095 VAL C CG2 1 +ATOM 6884 N N . ALA C 1 277 ? 24.371 62.666 87.308 1.00 182.53 ? 1096 ALA C N 1 +ATOM 6885 C CA . ALA C 1 277 ? 25.317 61.597 87.011 1.00 156.50 ? 1096 ALA C CA 1 +ATOM 6886 C C . ALA C 1 277 ? 25.785 61.708 85.572 1.00 151.38 ? 1096 ALA C C 1 +ATOM 6887 O O . ALA C 1 277 ? 26.986 61.724 85.299 1.00 139.23 ? 1096 ALA C O 1 +ATOM 6888 C CB . ALA C 1 277 ? 24.683 60.234 87.253 1.00 123.51 ? 1096 ALA C CB 1 +ATOM 6889 N N . ALA C 1 278 ? 24.823 61.796 84.657 1.00 159.36 ? 1097 ALA C N 1 +ATOM 6890 C CA . ALA C 1 278 ? 25.120 61.899 83.231 1.00 149.15 ? 1097 ALA C CA 1 +ATOM 6891 C C . ALA C 1 278 ? 25.720 63.249 82.832 1.00 140.35 ? 1097 ALA C C 1 +ATOM 6892 O O . ALA C 1 278 ? 26.391 63.352 81.808 1.00 132.48 ? 1097 ALA C O 1 +ATOM 6893 C CB . ALA C 1 278 ? 23.880 61.599 82.402 1.00 129.68 ? 1097 ALA C CB 1 +ATOM 6894 N N . ASP C 1 279 ? 25.481 64.284 83.630 1.00 134.68 ? 1098 ASP C N 1 +ATOM 6895 C CA . ASP C 1 279 ? 26.107 65.574 83.365 1.00 138.41 ? 1098 ASP C CA 1 +ATOM 6896 C C . ASP C 1 279 ? 27.577 65.558 83.790 1.00 170.67 ? 1098 ASP C C 1 +ATOM 6897 O O . ASP C 1 279 ? 28.430 66.161 83.136 1.00 143.94 ? 1098 ASP C O 1 +ATOM 6898 C CB . ASP C 1 279 ? 25.356 66.703 84.068 1.00 151.52 ? 1098 ASP C CB 1 +ATOM 6899 C CG . ASP C 1 279 ? 25.532 68.040 83.372 1.00 170.39 ? 1098 ASP C CG 1 +ATOM 6900 O OD1 . ASP C 1 279 ? 26.535 68.730 83.655 1.00 153.20 ? 1098 ASP C OD1 1 +ATOM 6901 O OD2 . ASP C 1 279 ? 24.667 68.397 82.539 1.00 180.71 ? 1098 ASP C OD2 1 +ATOM 6902 N N . MET C 1 280 ? 27.865 64.857 84.883 1.00 184.18 ? 1099 MET C N 1 +ATOM 6903 C CA . MET C 1 280 ? 29.239 64.683 85.341 1.00 170.69 ? 1099 MET C CA 1 +ATOM 6904 C C . MET C 1 280 ? 30.074 63.962 84.290 1.00 150.08 ? 1099 MET C C 1 +ATOM 6905 O O . MET C 1 280 ? 31.278 64.182 84.181 1.00 145.56 ? 1099 MET C O 1 +ATOM 6906 C CB . MET C 1 280 ? 29.279 63.888 86.649 1.00 185.89 ? 1099 MET C CB 1 +ATOM 6907 C CG . MET C 1 280 ? 29.030 64.702 87.910 1.00 203.68 ? 1099 MET C CG 1 +ATOM 6908 S SD . MET C 1 280 ? 29.358 63.751 89.410 1.00 188.27 ? 1099 MET C SD 1 +ATOM 6909 C CE . MET C 1 280 ? 31.031 63.201 89.087 1.00 129.98 ? 1099 MET C CE 1 +ATOM 6910 N N . PHE C 1 281 ? 29.424 63.104 83.513 1.00 140.14 ? 1100 PHE C N 1 +ATOM 6911 C CA . PHE C 1 281 ? 30.128 62.238 82.577 1.00 142.67 ? 1100 PHE C CA 1 +ATOM 6912 C C . PHE C 1 281 ? 29.820 62.545 81.120 1.00 160.94 ? 1100 PHE C C 1 +ATOM 6913 O O . PHE C 1 281 ? 29.824 61.655 80.270 1.00 144.86 ? 1100 PHE C O 1 +ATOM 6914 C CB . PHE C 1 281 ? 29.811 60.783 82.896 1.00 125.71 ? 1100 PHE C CB 1 +ATOM 6915 C CG . PHE C 1 281 ? 30.344 60.340 84.219 1.00 150.71 ? 1100 PHE C CG 1 +ATOM 6916 C CD1 . PHE C 1 281 ? 31.627 60.692 84.605 1.00 162.36 ? 1100 PHE C CD1 1 +ATOM 6917 C CD2 . PHE C 1 281 ? 29.567 59.591 85.088 1.00 122.86 ? 1100 PHE C CD2 1 +ATOM 6918 C CE1 . PHE C 1 281 ? 32.134 60.291 85.823 1.00 158.75 ? 1100 PHE C CE1 1 +ATOM 6919 C CE2 . PHE C 1 281 ? 30.068 59.183 86.311 1.00 123.40 ? 1100 PHE C CE2 1 +ATOM 6920 C CZ . PHE C 1 281 ? 31.353 59.535 86.681 1.00 142.80 ? 1100 PHE C CZ 1 +ATOM 6921 N N . SER C 1 282 ? 29.560 63.817 80.843 1.00 188.29 ? 1101 SER C N 1 +ATOM 6922 C CA . SER C 1 282 ? 29.329 64.275 79.484 1.00 206.62 ? 1101 SER C CA 1 +ATOM 6923 C C . SER C 1 282 ? 30.663 64.486 78.783 1.00 205.24 ? 1101 SER C C 1 +ATOM 6924 O O . SER C 1 282 ? 30.749 64.406 77.558 1.00 162.31 ? 1101 SER C O 1 +ATOM 6925 C CB . SER C 1 282 ? 28.526 65.575 79.489 1.00 210.96 ? 1101 SER C CB 1 +ATOM 6926 O OG . SER C 1 282 ? 29.248 66.618 80.121 1.00 199.73 ? 1101 SER C OG 1 +ATOM 6927 N N . ASP C 1 283 ? 31.701 64.769 79.568 1.00 213.75 ? 1102 ASP C N 1 +ATOM 6928 C CA . ASP C 1 283 ? 33.056 64.855 79.032 1.00 178.63 ? 1102 ASP C CA 1 +ATOM 6929 C C . ASP C 1 283 ? 33.699 63.471 79.040 1.00 149.66 ? 1102 ASP C C 1 +ATOM 6930 O O . ASP C 1 283 ? 34.774 63.268 78.468 1.00 113.14 ? 1102 ASP C O 1 +ATOM 6931 C CB . ASP C 1 283 ? 33.908 65.889 79.786 1.00 167.16 ? 1102 ASP C CB 1 +ATOM 6932 C CG . ASP C 1 283 ? 33.993 65.617 81.279 1.00 177.03 ? 1102 ASP C CG 1 +ATOM 6933 O OD1 . ASP C 1 283 ? 33.064 64.987 81.829 1.00 198.05 ? 1102 ASP C OD1 1 +ATOM 6934 O OD2 . ASP C 1 283 ? 34.990 66.049 81.905 1.00 134.96 ? 1102 ASP C OD2 1 +ATOM 6935 N N . GLY C 1 284 ? 33.015 62.527 79.689 1.00 144.33 ? 1103 GLY C N 1 +ATOM 6936 C CA . GLY C 1 284 ? 33.346 61.114 79.613 1.00 148.52 ? 1103 GLY C CA 1 +ATOM 6937 C C . GLY C 1 284 ? 34.742 60.763 80.082 1.00 175.91 ? 1103 GLY C C 1 +ATOM 6938 O O . GLY C 1 284 ? 35.345 59.800 79.600 1.00 111.54 ? 1103 GLY C O 1 +ATOM 6939 N N . ASN C 1 285 ? 35.246 61.560 81.023 1.00 218.88 ? 1104 ASN C N 1 +ATOM 6940 C CA . ASN C 1 285 ? 36.554 61.345 81.632 1.00 193.54 ? 1104 ASN C CA 1 +ATOM 6941 C C . ASN C 1 285 ? 36.409 60.780 83.039 1.00 142.82 ? 1104 ASN C C 1 +ATOM 6942 O O . ASN C 1 285 ? 36.565 61.504 84.020 1.00 145.55 ? 1104 ASN C O 1 +ATOM 6943 C CB . ASN C 1 285 ? 37.357 62.652 81.680 1.00 175.47 ? 1104 ASN C CB 1 +ATOM 6944 C CG . ASN C 1 285 ? 37.610 63.244 80.297 1.00 183.15 ? 1104 ASN C CG 1 +ATOM 6945 O OD1 . ASN C 1 285 ? 37.528 62.549 79.279 1.00 164.57 ? 1104 ASN C OD1 1 +ATOM 6946 N ND2 . ASN C 1 285 ? 37.927 64.536 80.257 1.00 153.89 ? 1104 ASN C ND2 1 +ATOM 6947 N N . PHE C 1 286 ? 36.110 59.483 83.114 1.00 130.01 ? 1105 PHE C N 1 +ATOM 6948 C CA . PHE C 1 286 ? 35.897 58.770 84.373 1.00 153.74 ? 1105 PHE C CA 1 +ATOM 6949 C C . PHE C 1 286 ? 37.193 58.603 85.166 1.00 198.28 ? 1105 PHE C C 1 +ATOM 6950 O O . PHE C 1 286 ? 38.234 58.244 84.610 1.00 206.58 ? 1105 PHE C O 1 +ATOM 6951 C CB . PHE C 1 286 ? 35.342 57.356 84.119 1.00 143.09 ? 1105 PHE C CB 1 +ATOM 6952 C CG . PHE C 1 286 ? 33.974 57.315 83.481 1.00 191.57 ? 1105 PHE C CG 1 +ATOM 6953 C CD1 . PHE C 1 286 ? 32.835 57.446 84.257 1.00 225.63 ? 1105 PHE C CD1 1 +ATOM 6954 C CD2 . PHE C 1 286 ? 33.829 57.083 82.113 1.00 161.56 ? 1105 PHE C CD2 1 +ATOM 6955 C CE1 . PHE C 1 286 ? 31.575 57.385 83.685 1.00 225.00 ? 1105 PHE C CE1 1 +ATOM 6956 C CE2 . PHE C 1 286 ? 32.571 57.026 81.531 1.00 124.05 ? 1105 PHE C CE2 1 +ATOM 6957 C CZ . PHE C 1 286 ? 31.442 57.176 82.319 1.00 176.61 ? 1105 PHE C CZ 1 +ATOM 6958 N N . ASN C 1 287 ? 37.110 58.852 86.470 1.00 208.77 ? 1106 ASN C N 1 +ATOM 6959 C CA . ASN C 1 287 ? 38.162 58.505 87.423 1.00 176.59 ? 1106 ASN C CA 1 +ATOM 6960 C C . ASN C 1 287 ? 37.520 58.192 88.771 1.00 162.74 ? 1106 ASN C C 1 +ATOM 6961 O O . ASN C 1 287 ? 36.452 58.715 89.079 1.00 145.88 ? 1106 ASN C O 1 +ATOM 6962 C CB . ASN C 1 287 ? 39.200 59.626 87.557 1.00 163.50 ? 1106 ASN C CB 1 +ATOM 6963 C CG . ASN C 1 287 ? 38.581 61.012 87.533 1.00 157.37 ? 1106 ASN C CG 1 +ATOM 6964 O OD1 . ASN C 1 287 ? 37.810 61.379 88.421 1.00 151.30 ? 1106 ASN C OD1 1 +ATOM 6965 N ND2 . ASN C 1 287 ? 38.935 61.799 86.522 1.00 133.10 ? 1106 ASN C ND2 1 +ATOM 6966 N N . TRP C 1 288 ? 38.161 57.337 89.563 1.00 160.22 ? 1107 TRP C N 1 +ATOM 6967 C CA . TRP C 1 288 ? 37.611 56.905 90.849 1.00 116.23 ? 1107 TRP C CA 1 +ATOM 6968 C C . TRP C 1 288 ? 37.190 58.044 91.776 1.00 137.48 ? 1107 TRP C C 1 +ATOM 6969 O O . TRP C 1 288 ? 36.296 57.876 92.605 1.00 122.73 ? 1107 TRP C O 1 +ATOM 6970 C CB . TRP C 1 288 ? 38.607 56.013 91.576 1.00 126.92 ? 1107 TRP C CB 1 +ATOM 6971 C CG . TRP C 1 288 ? 38.171 54.606 91.631 1.00 175.68 ? 1107 TRP C CG 1 +ATOM 6972 C CD1 . TRP C 1 288 ? 38.735 53.548 90.989 1.00 205.99 ? 1107 TRP C CD1 1 +ATOM 6973 C CD2 . TRP C 1 288 ? 37.053 54.088 92.360 1.00 192.26 ? 1107 TRP C CD2 1 +ATOM 6974 N NE1 . TRP C 1 288 ? 38.045 52.396 91.282 1.00 228.89 ? 1107 TRP C NE1 1 +ATOM 6975 C CE2 . TRP C 1 288 ? 37.006 52.703 92.122 1.00 222.35 ? 1107 TRP C CE2 1 +ATOM 6976 C CE3 . TRP C 1 288 ? 36.092 54.660 93.195 1.00 170.31 ? 1107 TRP C CE3 1 +ATOM 6977 C CZ2 . TRP C 1 288 ? 36.031 51.880 92.690 1.00 199.90 ? 1107 TRP C CZ2 1 +ATOM 6978 C CZ3 . TRP C 1 288 ? 35.128 53.843 93.760 1.00 149.48 ? 1107 TRP C CZ3 1 +ATOM 6979 C CH2 . TRP C 1 288 ? 35.103 52.471 93.502 1.00 149.97 ? 1107 TRP C CH2 1 +ATOM 6980 N N . GLY C 1 289 ? 37.839 59.196 91.641 1.00 129.43 ? 1108 GLY C N 1 +ATOM 6981 C CA . GLY C 1 289 ? 37.480 60.364 92.424 1.00 140.42 ? 1108 GLY C CA 1 +ATOM 6982 C C . GLY C 1 289 ? 36.027 60.762 92.237 1.00 164.14 ? 1108 GLY C C 1 +ATOM 6983 O O . GLY C 1 289 ? 35.331 61.087 93.202 1.00 152.98 ? 1108 GLY C O 1 +ATOM 6984 N N . ARG C 1 290 ? 35.569 60.723 90.988 1.00 160.89 ? 1109 ARG C N 1 +ATOM 6985 C CA . ARG C 1 290 ? 34.195 61.084 90.650 1.00 130.14 ? 1109 ARG C CA 1 +ATOM 6986 C C . ARG C 1 290 ? 33.207 59.990 91.021 1.00 133.83 ? 1109 ARG C C 1 +ATOM 6987 O O . ARG C 1 290 ? 32.075 60.270 91.408 1.00 116.75 ? 1109 ARG C O 1 +ATOM 6988 C CB . ARG C 1 290 ? 34.072 61.382 89.159 1.00 102.35 ? 1109 ARG C CB 1 +ATOM 6989 C CG . ARG C 1 290 ? 34.696 62.689 88.722 1.00 136.32 ? 1109 ARG C CG 1 +ATOM 6990 C CD . ARG C 1 290 ? 34.323 62.982 87.284 1.00 147.99 ? 1109 ARG C CD 1 +ATOM 6991 N NE . ARG C 1 290 ? 34.972 64.185 86.782 1.00 161.81 ? 1109 ARG C NE 1 +ATOM 6992 C CZ . ARG C 1 290 ? 34.905 64.588 85.520 1.00 175.99 ? 1109 ARG C CZ 1 +ATOM 6993 N NH1 . ARG C 1 290 ? 34.220 63.874 84.636 1.00 187.91 ? 1109 ARG C NH1 1 +ATOM 6994 N NH2 . ARG C 1 290 ? 35.525 65.697 85.140 1.00 162.56 ? 1109 ARG C NH2 1 +ATOM 6995 N N . VAL C 1 291 ? 33.638 58.744 90.875 1.00 135.96 ? 1110 VAL C N 1 +ATOM 6996 C CA . VAL C 1 291 ? 32.840 57.594 91.268 1.00 122.16 ? 1110 VAL C CA 1 +ATOM 6997 C C . VAL C 1 291 ? 32.508 57.710 92.746 1.00 117.50 ? 1110 VAL C C 1 +ATOM 6998 O O . VAL C 1 291 ? 31.401 57.394 93.179 1.00 126.62 ? 1110 VAL C O 1 +ATOM 6999 C CB . VAL C 1 291 ? 33.624 56.290 91.026 1.00 158.12 ? 1110 VAL C CB 1 +ATOM 7000 C CG1 . VAL C 1 291 ? 32.818 55.070 91.482 1.00 151.57 ? 1110 VAL C CG1 1 +ATOM 7001 C CG2 . VAL C 1 291 ? 34.040 56.181 89.553 1.00 127.93 ? 1110 VAL C CG2 1 +ATOM 7002 N N . VAL C 1 292 ? 33.483 58.188 93.510 1.00 124.10 ? 1111 VAL C N 1 +ATOM 7003 C CA . VAL C 1 292 ? 33.327 58.355 94.945 1.00 140.36 ? 1111 VAL C CA 1 +ATOM 7004 C C . VAL C 1 292 ? 32.563 59.639 95.274 1.00 140.21 ? 1111 VAL C C 1 +ATOM 7005 O O . VAL C 1 292 ? 31.654 59.619 96.102 1.00 139.70 ? 1111 VAL C O 1 +ATOM 7006 C CB . VAL C 1 292 ? 34.694 58.332 95.663 1.00 125.00 ? 1111 VAL C CB 1 +ATOM 7007 C CG1 . VAL C 1 292 ? 34.531 58.621 97.116 1.00 82.71 ? 1111 VAL C CG1 1 +ATOM 7008 C CG2 . VAL C 1 292 ? 35.335 56.980 95.511 1.00 146.02 ? 1111 VAL C CG2 1 +ATOM 7009 N N . ALA C 1 293 ? 32.918 60.745 94.617 1.00 131.04 ? 1112 ALA C N 1 +ATOM 7010 C CA . ALA C 1 293 ? 32.216 62.015 94.832 1.00 132.23 ? 1112 ALA C CA 1 +ATOM 7011 C C . ALA C 1 293 ? 30.746 61.927 94.428 1.00 145.08 ? 1112 ALA C C 1 +ATOM 7012 O O . ALA C 1 293 ? 29.900 62.640 94.956 1.00 128.47 ? 1112 ALA C O 1 +ATOM 7013 C CB . ALA C 1 293 ? 32.911 63.167 94.102 1.00 112.67 ? 1112 ALA C CB 1 +ATOM 7014 N N . LEU C 1 294 ? 30.437 61.044 93.493 1.00 158.49 ? 1113 LEU C N 1 +ATOM 7015 C CA . LEU C 1 294 ? 29.049 60.830 93.138 1.00 144.80 ? 1113 LEU C CA 1 +ATOM 7016 C C . LEU C 1 294 ? 28.434 59.799 94.082 1.00 136.19 ? 1113 LEU C C 1 +ATOM 7017 O O . LEU C 1 294 ? 27.214 59.723 94.220 1.00 145.30 ? 1113 LEU C O 1 +ATOM 7018 C CB . LEU C 1 294 ? 28.938 60.402 91.679 1.00 124.04 ? 1113 LEU C CB 1 +ATOM 7019 C CG . LEU C 1 294 ? 27.540 60.201 91.114 1.00 141.67 ? 1113 LEU C CG 1 +ATOM 7020 C CD1 . LEU C 1 294 ? 27.506 60.726 89.705 1.00 133.73 ? 1113 LEU C CD1 1 +ATOM 7021 C CD2 . LEU C 1 294 ? 27.193 58.729 91.139 1.00 170.04 ? 1113 LEU C CD2 1 +ATOM 7022 N N . PHE C 1 295 ? 29.281 59.013 94.740 1.00 111.59 ? 1114 PHE C N 1 +ATOM 7023 C CA . PHE C 1 295 ? 28.799 58.048 95.723 1.00 141.09 ? 1114 PHE C CA 1 +ATOM 7024 C C . PHE C 1 295 ? 28.658 58.704 97.097 1.00 159.20 ? 1114 PHE C C 1 +ATOM 7025 O O . PHE C 1 295 ? 28.163 58.083 98.032 1.00 167.01 ? 1114 PHE C O 1 +ATOM 7026 C CB . PHE C 1 295 ? 29.723 56.830 95.801 1.00 150.51 ? 1114 PHE C CB 1 +ATOM 7027 C CG . PHE C 1 295 ? 29.107 55.636 96.489 1.00 170.26 ? 1114 PHE C CG 1 +ATOM 7028 C CD1 . PHE C 1 295 ? 28.208 54.819 95.817 1.00 175.86 ? 1114 PHE C CD1 1 +ATOM 7029 C CD2 . PHE C 1 295 ? 29.437 55.324 97.802 1.00 147.73 ? 1114 PHE C CD2 1 +ATOM 7030 C CE1 . PHE C 1 295 ? 27.645 53.716 96.441 1.00 180.34 ? 1114 PHE C CE1 1 +ATOM 7031 C CE2 . PHE C 1 295 ? 28.878 54.223 98.433 1.00 162.40 ? 1114 PHE C CE2 1 +ATOM 7032 C CZ . PHE C 1 295 ? 27.980 53.418 97.750 1.00 186.04 ? 1114 PHE C CZ 1 +ATOM 7033 N N . TYR C 1 296 ? 29.117 59.951 97.210 1.00 164.36 ? 1115 TYR C N 1 +ATOM 7034 C CA . TYR C 1 296 ? 28.873 60.797 98.385 1.00 166.26 ? 1115 TYR C CA 1 +ATOM 7035 C C . TYR C 1 296 ? 27.563 61.509 98.096 1.00 170.82 ? 1115 TYR C C 1 +ATOM 7036 O O . TYR C 1 296 ? 26.792 61.832 99.000 1.00 140.44 ? 1115 TYR C O 1 +ATOM 7037 C CB . TYR C 1 296 ? 30.057 61.790 98.567 1.00 162.92 ? 1115 TYR C CB 1 +ATOM 7038 C CG . TYR C 1 296 ? 29.979 62.863 99.676 1.00 176.32 ? 1115 TYR C CG 1 +ATOM 7039 C CD1 . TYR C 1 296 ? 30.247 62.568 101.018 1.00 199.12 ? 1115 TYR C CD1 1 +ATOM 7040 C CD2 . TYR C 1 296 ? 29.627 64.168 99.367 1.00 166.04 ? 1115 TYR C CD2 1 +ATOM 7041 C CE1 . TYR C 1 296 ? 30.167 63.561 102.003 1.00 202.03 ? 1115 TYR C CE1 1 +ATOM 7042 C CE2 . TYR C 1 296 ? 29.546 65.153 100.339 1.00 156.63 ? 1115 TYR C CE2 1 +ATOM 7043 C CZ . TYR C 1 296 ? 29.810 64.849 101.648 1.00 157.50 ? 1115 TYR C CZ 1 +ATOM 7044 O OH . TYR C 1 296 ? 29.714 65.854 102.585 1.00 137.20 ? 1115 TYR C OH 1 +ATOM 7045 N N . PHE C 1 297 ? 27.311 61.736 96.812 1.00 177.25 ? 1116 PHE C N 1 +ATOM 7046 C CA . PHE C 1 297 ? 26.060 62.338 96.397 1.00 163.41 ? 1116 PHE C CA 1 +ATOM 7047 C C . PHE C 1 297 ? 24.915 61.346 96.610 1.00 146.04 ? 1116 PHE C C 1 +ATOM 7048 O O . PHE C 1 297 ? 24.075 61.558 97.482 1.00 119.88 ? 1116 PHE C O 1 +ATOM 7049 C CB . PHE C 1 297 ? 26.139 62.805 94.947 1.00 171.99 ? 1116 PHE C CB 1 +ATOM 7050 C CG . PHE C 1 297 ? 25.049 63.760 94.565 1.00 198.50 ? 1116 PHE C CG 1 +ATOM 7051 C CD1 . PHE C 1 297 ? 25.095 65.082 94.976 1.00 181.81 ? 1116 PHE C CD1 1 +ATOM 7052 C CD2 . PHE C 1 297 ? 23.973 63.335 93.803 1.00 222.55 ? 1116 PHE C CD2 1 +ATOM 7053 C CE1 . PHE C 1 297 ? 24.095 65.961 94.627 1.00 197.92 ? 1116 PHE C CE1 1 +ATOM 7054 C CE2 . PHE C 1 297 ? 22.966 64.210 93.451 1.00 215.53 ? 1116 PHE C CE2 1 +ATOM 7055 C CZ . PHE C 1 297 ? 23.027 65.524 93.864 1.00 212.64 ? 1116 PHE C CZ 1 +ATOM 7056 N N . ALA C 1 298 ? 24.901 60.258 95.840 1.00 141.14 ? 1117 ALA C N 1 +ATOM 7057 C CA . ALA C 1 298 ? 23.926 59.177 96.026 1.00 156.30 ? 1117 ALA C CA 1 +ATOM 7058 C C . ALA C 1 298 ? 23.819 58.742 97.495 1.00 189.02 ? 1117 ALA C C 1 +ATOM 7059 O O . ALA C 1 298 ? 22.767 58.274 97.944 1.00 177.21 ? 1117 ALA C O 1 +ATOM 7060 C CB . ALA C 1 298 ? 24.279 57.989 95.146 1.00 150.84 ? 1117 ALA C CB 1 +ATOM 7061 N N . SER C 1 299 ? 24.921 58.896 98.227 1.00 200.88 ? 1118 SER C N 1 +ATOM 7062 C CA . SER C 1 299 ? 24.917 58.772 99.680 1.00 187.21 ? 1118 SER C CA 1 +ATOM 7063 C C . SER C 1 299 ? 23.938 59.797 100.250 1.00 174.24 ? 1118 SER C C 1 +ATOM 7064 O O . SER C 1 299 ? 22.896 59.425 100.784 1.00 178.03 ? 1118 SER C O 1 +ATOM 7065 C CB . SER C 1 299 ? 26.328 58.999 100.245 1.00 181.18 ? 1118 SER C CB 1 +ATOM 7066 O OG . SER C 1 299 ? 26.444 58.634 101.612 1.00 173.40 ? 1118 SER C OG 1 +ATOM 7067 N N . LYS C 1 300 ? 24.260 61.083 100.096 1.00 153.49 ? 1119 LYS C N 1 +ATOM 7068 C CA . LYS C 1 300 ? 23.448 62.180 100.645 1.00 159.77 ? 1119 LYS C CA 1 +ATOM 7069 C C . LYS C 1 300 ? 21.971 62.171 100.210 1.00 196.54 ? 1119 LYS C C 1 +ATOM 7070 O O . LYS C 1 300 ? 21.149 62.876 100.797 1.00 190.44 ? 1119 LYS C O 1 +ATOM 7071 C CB . LYS C 1 300 ? 24.078 63.544 100.322 1.00 152.61 ? 1119 LYS C CB 1 +ATOM 7072 C CG . LYS C 1 300 ? 25.343 63.892 101.113 1.00 144.18 ? 1119 LYS C CG 1 +ATOM 7073 C CD . LYS C 1 300 ? 25.031 64.410 102.513 1.00 113.62 ? 1119 LYS C CD 1 +ATOM 7074 C CE . LYS C 1 300 ? 26.211 65.197 103.068 1.00 134.47 ? 1119 LYS C CE 1 +ATOM 7075 N NZ . LYS C 1 300 ? 26.185 65.302 104.559 1.00 156.09 ? 1119 LYS C NZ 1 +ATOM 7076 N N . LEU C 1 301 ? 21.643 61.380 99.186 1.00 216.82 ? 1120 LEU C N 1 +ATOM 7077 C CA . LEU C 1 301 ? 20.256 61.197 98.750 1.00 187.81 ? 1120 LEU C CA 1 +ATOM 7078 C C . LEU C 1 301 ? 19.561 60.145 99.600 1.00 183.06 ? 1120 LEU C C 1 +ATOM 7079 O O . LEU C 1 301 ? 19.087 59.129 99.084 1.00 149.62 ? 1120 LEU C O 1 +ATOM 7080 C CB . LEU C 1 301 ? 20.195 60.792 97.278 1.00 153.43 ? 1120 LEU C CB 1 +ATOM 7081 C CG . LEU C 1 301 ? 20.793 61.847 96.348 1.00 175.26 ? 1120 LEU C CG 1 +ATOM 7082 C CD1 . LEU C 1 301 ? 20.713 61.419 94.886 1.00 172.53 ? 1120 LEU C CD1 1 +ATOM 7083 C CD2 . LEU C 1 301 ? 20.118 63.201 96.576 1.00 165.86 ? 1120 LEU C CD2 1 +ATOM 7084 N N . VAL C 1 302 ? 19.513 60.409 100.905 1.00 207.20 ? 1121 VAL C N 1 +ATOM 7085 C CA . VAL C 1 302 ? 18.972 59.483 101.896 1.00 224.59 ? 1121 VAL C CA 1 +ATOM 7086 C C . VAL C 1 302 ? 18.274 60.228 103.046 1.00 224.55 ? 1121 VAL C C 1 +ATOM 7087 O O . VAL C 1 302 ? 17.063 60.083 103.235 1.00 235.15 ? 1121 VAL C O 1 +ATOM 7088 C CB . VAL C 1 302 ? 20.085 58.552 102.460 1.00 181.67 ? 1121 VAL C CB 1 +ATOM 7089 C CG1 . VAL C 1 302 ? 19.651 57.888 103.770 1.00 156.40 ? 1121 VAL C CG1 1 +ATOM 7090 C CG2 . VAL C 1 302 ? 20.492 57.503 101.422 1.00 161.08 ? 1121 VAL C CG2 1 +ATOM 7091 N N . LEU C 1 303 ? 19.040 61.032 103.786 1.00 204.17 ? 1122 LEU C N 1 +ATOM 7092 C CA . LEU C 1 303 ? 18.566 61.706 105.006 1.00 210.97 ? 1122 LEU C CA 1 +ATOM 7093 C C . LEU C 1 303 ? 17.266 62.499 104.836 1.00 209.01 ? 1122 LEU C C 1 +ATOM 7094 O O . LEU C 1 303 ? 16.425 62.531 105.739 1.00 194.23 ? 1122 LEU C O 1 +ATOM 7095 C CB . LEU C 1 303 ? 19.662 62.616 105.584 1.00 198.38 ? 1122 LEU C CB 1 +ATOM 7096 C CG . LEU C 1 303 ? 20.529 62.060 106.724 1.00 180.43 ? 1122 LEU C CG 1 +ATOM 7097 C CD1 . LEU C 1 303 ? 21.649 63.037 107.106 1.00 141.83 ? 1122 LEU C CD1 1 +ATOM 7098 C CD2 . LEU C 1 303 ? 19.672 61.692 107.947 1.00 134.31 ? 1122 LEU C CD2 1 +ATOM 7099 N N . SER D 1 5 ? 24.103 76.205 60.459 1.00 91.80 ? 2 SER D N 1 +ATOM 7100 C CA . SER D 1 5 ? 25.350 76.225 59.691 1.00 150.71 ? 2 SER D CA 1 +ATOM 7101 C C . SER D 1 5 ? 25.146 76.127 58.168 1.00 148.21 ? 2 SER D C 1 +ATOM 7102 O O . SER D 1 5 ? 24.257 75.420 57.687 1.00 109.19 ? 2 SER D O 1 +ATOM 7103 C CB . SER D 1 5 ? 26.303 75.121 60.177 1.00 148.54 ? 2 SER D CB 1 +ATOM 7104 O OG . SER D 1 5 ? 26.069 73.884 59.519 1.00 143.22 ? 2 SER D OG 1 +ATOM 7105 N N . LYS D 1 6 ? 25.986 76.839 57.417 1.00 149.85 ? 3 LYS D N 1 +ATOM 7106 C CA . LYS D 1 6 ? 25.939 76.805 55.954 1.00 144.38 ? 3 LYS D CA 1 +ATOM 7107 C C . LYS D 1 6 ? 26.598 75.525 55.444 1.00 144.89 ? 3 LYS D C 1 +ATOM 7108 O O . LYS D 1 6 ? 26.363 75.092 54.313 1.00 132.65 ? 3 LYS D O 1 +ATOM 7109 C CB . LYS D 1 6 ? 26.637 78.031 55.341 1.00 169.93 ? 3 LYS D CB 1 +ATOM 7110 C CG . LYS D 1 6 ? 26.445 79.357 56.093 1.00 189.31 ? 3 LYS D CG 1 +ATOM 7111 C CD . LYS D 1 6 ? 24.977 79.707 56.317 1.00 195.90 ? 3 LYS D CD 1 +ATOM 7112 C CE . LYS D 1 6 ? 24.695 79.971 57.795 1.00 172.33 ? 3 LYS D CE 1 +ATOM 7113 N NZ . LYS D 1 6 ? 23.240 79.930 58.119 1.00 147.37 ? 3 LYS D NZ 1 +ATOM 7114 N N . GLY D 1 7 ? 27.431 74.930 56.290 1.00 142.94 ? 4 GLY D N 1 +ATOM 7115 C CA . GLY D 1 7 ? 28.078 73.676 55.966 1.00 132.84 ? 4 GLY D CA 1 +ATOM 7116 C C . GLY D 1 7 ? 27.079 72.544 55.850 1.00 126.12 ? 4 GLY D C 1 +ATOM 7117 O O . GLY D 1 7 ? 27.214 71.680 54.982 1.00 106.47 ? 4 GLY D O 1 +ATOM 7118 N N . GLU D 1 8 ? 26.072 72.566 56.721 1.00 100.68 ? 5 GLU D N 1 +ATOM 7119 C CA . GLU D 1 8 ? 25.072 71.504 56.802 1.00 91.19 ? 5 GLU D CA 1 +ATOM 7120 C C . GLU D 1 8 ? 24.398 71.204 55.453 1.00 99.67 ? 5 GLU D C 1 +ATOM 7121 O O . GLU D 1 8 ? 24.010 70.067 55.185 1.00 122.32 ? 5 GLU D O 1 +ATOM 7122 C CB . GLU D 1 8 ? 24.027 71.848 57.874 1.00 113.67 ? 5 GLU D CB 1 +ATOM 7123 C CG . GLU D 1 8 ? 22.984 70.764 58.100 1.00 161.05 ? 5 GLU D CG 1 +ATOM 7124 C CD . GLU D 1 8 ? 23.353 69.757 59.199 1.00 183.42 ? 5 GLU D CD 1 +ATOM 7125 O OE1 . GLU D 1 8 ? 23.684 70.182 60.331 1.00 187.96 ? 5 GLU D OE1 1 +ATOM 7126 O OE2 . GLU D 1 8 ? 23.295 68.542 58.918 1.00 159.18 ? 5 GLU D OE2 1 +ATOM 7127 N N . GLU D 1 9 ? 24.282 72.215 54.596 1.00 107.02 ? 6 GLU D N 1 +ATOM 7128 C CA . GLU D 1 9 ? 23.623 72.038 53.299 1.00 98.99 ? 6 GLU D CA 1 +ATOM 7129 C C . GLU D 1 9 ? 24.488 71.322 52.265 1.00 107.38 ? 6 GLU D C 1 +ATOM 7130 O O . GLU D 1 9 ? 24.042 71.080 51.140 1.00 115.54 ? 6 GLU D O 1 +ATOM 7131 C CB . GLU D 1 9 ? 23.169 73.382 52.727 1.00 143.16 ? 6 GLU D CB 1 +ATOM 7132 C CG . GLU D 1 9 ? 22.059 74.060 53.507 1.00 168.35 ? 6 GLU D CG 1 +ATOM 7133 C CD . GLU D 1 9 ? 21.699 75.417 52.936 1.00 181.82 ? 6 GLU D CD 1 +ATOM 7134 O OE1 . GLU D 1 9 ? 22.442 75.902 52.054 1.00 170.04 ? 6 GLU D OE1 1 +ATOM 7135 O OE2 . GLU D 1 9 ? 20.679 75.996 53.372 1.00 193.52 ? 6 GLU D OE2 1 +ATOM 7136 N N . LEU D 1 10 ? 25.724 71.007 52.638 1.00 93.29 ? 7 LEU D N 1 +ATOM 7137 C CA . LEU D 1 10 ? 26.623 70.271 51.758 1.00 82.54 ? 7 LEU D CA 1 +ATOM 7138 C C . LEU D 1 10 ? 26.510 68.770 52.017 1.00 111.06 ? 7 LEU D C 1 +ATOM 7139 O O . LEU D 1 10 ? 26.923 67.947 51.190 1.00 84.72 ? 7 LEU D O 1 +ATOM 7140 C CB . LEU D 1 10 ? 28.067 70.742 51.960 1.00 86.43 ? 7 LEU D CB 1 +ATOM 7141 C CG . LEU D 1 10 ? 28.440 72.115 51.391 1.00 107.03 ? 7 LEU D CG 1 +ATOM 7142 C CD1 . LEU D 1 10 ? 29.554 72.783 52.192 1.00 103.08 ? 7 LEU D CD1 1 +ATOM 7143 C CD2 . LEU D 1 10 ? 28.833 72.001 49.923 1.00 106.20 ? 7 LEU D CD2 1 +ATOM 7144 N N . PHE D 1 11 ? 25.913 68.423 53.155 1.00 113.15 ? 8 PHE D N 1 +ATOM 7145 C CA . PHE D 1 11 ? 25.956 67.048 53.648 1.00 105.36 ? 8 PHE D CA 1 +ATOM 7146 C C . PHE D 1 11 ? 24.647 66.258 53.640 1.00 107.08 ? 8 PHE D C 1 +ATOM 7147 O O . PHE D 1 11 ? 24.609 65.117 54.107 1.00 109.01 ? 8 PHE D O 1 +ATOM 7148 C CB . PHE D 1 11 ? 26.653 66.995 55.008 1.00 97.32 ? 8 PHE D CB 1 +ATOM 7149 C CG . PHE D 1 11 ? 28.128 67.213 54.909 1.00 109.70 ? 8 PHE D CG 1 +ATOM 7150 C CD1 . PHE D 1 11 ? 28.963 66.171 54.551 1.00 83.56 ? 8 PHE D CD1 1 +ATOM 7151 C CD2 . PHE D 1 11 ? 28.676 68.465 55.114 1.00 99.88 ? 8 PHE D CD2 1 +ATOM 7152 C CE1 . PHE D 1 11 ? 30.309 66.364 54.430 1.00 93.26 ? 8 PHE D CE1 1 +ATOM 7153 C CE2 . PHE D 1 11 ? 30.035 68.660 54.994 1.00 104.33 ? 8 PHE D CE2 1 +ATOM 7154 C CZ . PHE D 1 11 ? 30.850 67.608 54.653 1.00 88.52 ? 8 PHE D CZ 1 +ATOM 7155 N N . THR D 1 12 ? 23.589 66.864 53.103 1.00 103.62 ? 9 THR D N 1 +ATOM 7156 C CA . THR D 1 12 ? 22.412 66.117 52.668 1.00 109.61 ? 9 THR D CA 1 +ATOM 7157 C C . THR D 1 12 ? 22.837 65.273 51.460 1.00 114.69 ? 9 THR D C 1 +ATOM 7158 O O . THR D 1 12 ? 23.712 65.685 50.696 1.00 117.76 ? 9 THR D O 1 +ATOM 7159 C CB . THR D 1 12 ? 21.258 67.063 52.268 1.00 51.86 ? 9 THR D CB 1 +ATOM 7160 O OG1 . THR D 1 12 ? 21.593 67.748 51.058 1.00 101.91 ? 9 THR D OG1 1 +ATOM 7161 C CG2 . THR D 1 12 ? 21.034 68.098 53.339 1.00 81.44 ? 9 THR D CG2 1 +ATOM 7162 N N . GLY D 1 13 ? 22.259 64.087 51.298 1.00 90.84 ? 10 GLY D N 1 +ATOM 7163 C CA . GLY D 1 13 ? 22.606 63.230 50.169 1.00 139.01 ? 10 GLY D CA 1 +ATOM 7164 C C . GLY D 1 13 ? 24.050 62.739 50.073 1.00 86.16 ? 10 GLY D C 1 +ATOM 7165 O O . GLY D 1 13 ? 24.973 63.378 50.573 1.00 98.36 ? 10 GLY D O 1 +ATOM 7166 N N . VAL D 1 14 ? 24.236 61.604 49.400 1.00 73.48 ? 11 VAL D N 1 +ATOM 7167 C CA . VAL D 1 14 ? 25.524 60.900 49.320 1.00 71.38 ? 11 VAL D CA 1 +ATOM 7168 C C . VAL D 1 14 ? 26.698 61.709 48.717 1.00 84.73 ? 11 VAL D C 1 +ATOM 7169 O O . VAL D 1 14 ? 26.697 62.044 47.529 1.00 92.48 ? 11 VAL D O 1 +ATOM 7170 C CB . VAL D 1 14 ? 25.357 59.546 48.565 1.00 73.76 ? 11 VAL D CB 1 +ATOM 7171 C CG1 . VAL D 1 14 ? 26.678 58.851 48.412 1.00 96.90 ? 11 VAL D CG1 1 +ATOM 7172 C CG2 . VAL D 1 14 ? 24.376 58.645 49.293 1.00 70.18 ? 11 VAL D CG2 1 +ATOM 7173 N N . VAL D 1 15 ? 27.698 62.006 49.551 1.00 71.71 ? 12 VAL D N 1 +ATOM 7174 C CA . VAL D 1 15 ? 28.905 62.728 49.128 1.00 89.26 ? 12 VAL D CA 1 +ATOM 7175 C C . VAL D 1 15 ? 30.078 61.800 48.805 1.00 100.31 ? 12 VAL D C 1 +ATOM 7176 O O . VAL D 1 15 ? 30.356 60.862 49.555 1.00 80.70 ? 12 VAL D O 1 +ATOM 7177 C CB . VAL D 1 15 ? 29.396 63.676 50.224 1.00 76.08 ? 12 VAL D CB 1 +ATOM 7178 C CG1 . VAL D 1 15 ? 30.624 64.450 49.744 1.00 78.79 ? 12 VAL D CG1 1 +ATOM 7179 C CG2 . VAL D 1 15 ? 28.282 64.610 50.654 1.00 55.41 ? 12 VAL D CG2 1 +ATOM 7180 N N . PRO D 1 16 ? 30.774 62.061 47.687 1.00 84.00 ? 13 PRO D N 1 +ATOM 7181 C CA . PRO D 1 16 ? 31.967 61.264 47.377 1.00 98.99 ? 13 PRO D CA 1 +ATOM 7182 C C . PRO D 1 16 ? 33.213 61.639 48.211 1.00 82.83 ? 13 PRO D C 1 +ATOM 7183 O O . PRO D 1 16 ? 33.510 62.822 48.420 1.00 91.75 ? 13 PRO D O 1 +ATOM 7184 C CB . PRO D 1 16 ? 32.172 61.504 45.872 1.00 65.63 ? 13 PRO D CB 1 +ATOM 7185 C CG . PRO D 1 16 ? 31.496 62.791 45.590 1.00 88.61 ? 13 PRO D CG 1 +ATOM 7186 C CD . PRO D 1 16 ? 30.355 62.908 46.554 1.00 83.31 ? 13 PRO D CD 1 +ATOM 7187 N N . ILE D 1 17 ? 33.917 60.612 48.694 1.00 90.32 ? 14 ILE D N 1 +ATOM 7188 C CA . ILE D 1 17 ? 35.116 60.783 49.520 1.00 88.65 ? 14 ILE D CA 1 +ATOM 7189 C C . ILE D 1 17 ? 36.360 60.233 48.837 1.00 84.20 ? 14 ILE D C 1 +ATOM 7190 O O . ILE D 1 17 ? 36.324 59.200 48.154 1.00 78.82 ? 14 ILE D O 1 +ATOM 7191 C CB . ILE D 1 17 ? 34.997 60.079 50.897 1.00 75.91 ? 14 ILE D CB 1 +ATOM 7192 C CG1 . ILE D 1 17 ? 33.671 60.406 51.566 1.00 78.48 ? 14 ILE D CG1 1 +ATOM 7193 C CG2 . ILE D 1 17 ? 36.129 60.485 51.825 1.00 60.43 ? 14 ILE D CG2 1 +ATOM 7194 C CD1 . ILE D 1 17 ? 33.427 59.588 52.812 1.00 109.43 ? 14 ILE D CD1 1 +ATOM 7195 N N . LEU D 1 18 ? 37.466 60.932 49.059 1.00 81.27 ? 15 LEU D N 1 +ATOM 7196 C CA . LEU D 1 18 ? 38.757 60.580 48.505 1.00 96.08 ? 15 LEU D CA 1 +ATOM 7197 C C . LEU D 1 18 ? 39.805 60.802 49.604 1.00 91.99 ? 15 LEU D C 1 +ATOM 7198 O O . LEU D 1 18 ? 39.814 61.851 50.246 1.00 68.94 ? 15 LEU D O 1 +ATOM 7199 C CB . LEU D 1 18 ? 39.012 61.471 47.289 1.00 61.62 ? 15 LEU D CB 1 +ATOM 7200 C CG . LEU D 1 18 ? 40.313 61.404 46.506 1.00 104.62 ? 15 LEU D CG 1 +ATOM 7201 C CD1 . LEU D 1 18 ? 40.463 60.024 45.892 1.00 111.97 ? 15 LEU D CD1 1 +ATOM 7202 C CD2 . LEU D 1 18 ? 40.334 62.501 45.434 1.00 113.23 ? 15 LEU D CD2 1 +ATOM 7203 N N . VAL D 1 19 ? 40.664 59.810 49.848 1.00 79.21 ? 16 VAL D N 1 +ATOM 7204 C CA . VAL D 1 19 ? 41.677 59.916 50.907 1.00 83.41 ? 16 VAL D CA 1 +ATOM 7205 C C . VAL D 1 19 ? 43.129 59.633 50.453 1.00 81.69 ? 16 VAL D C 1 +ATOM 7206 O O . VAL D 1 19 ? 43.397 58.625 49.783 1.00 80.01 ? 16 VAL D O 1 +ATOM 7207 C CB . VAL D 1 19 ? 41.321 59.002 52.101 1.00 79.26 ? 16 VAL D CB 1 +ATOM 7208 C CG1 . VAL D 1 19 ? 42.307 59.184 53.224 1.00 74.84 ? 16 VAL D CG1 1 +ATOM 7209 C CG2 . VAL D 1 19 ? 39.933 59.306 52.594 1.00 81.01 ? 16 VAL D CG2 1 +ATOM 7210 N N . GLU D 1 20 ? 44.045 60.536 50.833 1.00 85.88 ? 17 GLU D N 1 +ATOM 7211 C CA . GLU D 1 20 ? 45.498 60.415 50.591 1.00 74.04 ? 17 GLU D CA 1 +ATOM 7212 C C . GLU D 1 20 ? 46.344 60.373 51.887 1.00 95.28 ? 17 GLU D C 1 +ATOM 7213 O O . GLU D 1 20 ? 46.296 61.302 52.703 1.00 66.11 ? 17 GLU D O 1 +ATOM 7214 C CB . GLU D 1 20 ? 46.018 61.576 49.718 1.00 89.58 ? 17 GLU D CB 1 +ATOM 7215 C CG . GLU D 1 20 ? 45.536 61.617 48.268 1.00 106.33 ? 17 GLU D CG 1 +ATOM 7216 C CD . GLU D 1 20 ? 45.859 60.350 47.488 1.00 132.42 ? 17 GLU D CD 1 +ATOM 7217 O OE1 . GLU D 1 20 ? 46.755 59.584 47.916 1.00 134.22 ? 17 GLU D OE1 1 +ATOM 7218 O OE2 . GLU D 1 20 ? 45.205 60.121 46.445 1.00 121.73 ? 17 GLU D OE2 1 +ATOM 7219 N N . LEU D 1 21 ? 47.142 59.316 52.055 1.00 79.87 ? 18 LEU D N 1 +ATOM 7220 C CA . LEU D 1 21 ? 48.035 59.197 53.214 1.00 86.62 ? 18 LEU D CA 1 +ATOM 7221 C C . LEU D 1 21 ? 49.523 58.982 52.851 1.00 83.53 ? 18 LEU D C 1 +ATOM 7222 O O . LEU D 1 21 ? 49.839 58.181 51.968 1.00 93.99 ? 18 LEU D O 1 +ATOM 7223 C CB . LEU D 1 21 ? 47.552 58.071 54.134 1.00 100.19 ? 18 LEU D CB 1 +ATOM 7224 C CG . LEU D 1 21 ? 48.439 57.789 55.351 1.00 88.45 ? 18 LEU D CG 1 +ATOM 7225 C CD1 . LEU D 1 21 ? 48.506 58.977 56.277 1.00 124.72 ? 18 LEU D CD1 1 +ATOM 7226 C CD2 . LEU D 1 21 ? 47.964 56.563 56.104 1.00 108.82 ? 18 LEU D CD2 1 +ATOM 7227 N N . ASP D 1 22 ? 50.420 59.711 53.527 1.00 87.14 ? 19 ASP D N 1 +ATOM 7228 C CA . ASP D 1 22 ? 51.879 59.472 53.469 1.00 105.38 ? 19 ASP D CA 1 +ATOM 7229 C C . ASP D 1 22 ? 52.441 59.108 54.849 1.00 105.95 ? 19 ASP D C 1 +ATOM 7230 O O . ASP D 1 22 ? 52.576 59.968 55.724 1.00 100.73 ? 19 ASP D O 1 +ATOM 7231 C CB . ASP D 1 22 ? 52.644 60.691 52.928 1.00 90.59 ? 19 ASP D CB 1 +ATOM 7232 C CG . ASP D 1 22 ? 52.648 60.766 51.407 1.00 124.18 ? 19 ASP D CG 1 +ATOM 7233 O OD1 . ASP D 1 22 ? 52.570 59.704 50.752 1.00 139.85 ? 19 ASP D OD1 1 +ATOM 7234 O OD2 . ASP D 1 22 ? 52.735 61.892 50.866 1.00 151.61 ? 19 ASP D OD2 1 +ATOM 7235 N N . GLY D 1 23 ? 52.785 57.837 55.029 1.00 103.57 ? 20 GLY D N 1 +ATOM 7236 C CA . GLY D 1 23 ? 53.229 57.339 56.319 1.00 58.95 ? 20 GLY D CA 1 +ATOM 7237 C C . GLY D 1 23 ? 54.716 57.060 56.449 1.00 108.22 ? 20 GLY D C 1 +ATOM 7238 O O . GLY D 1 23 ? 55.416 56.835 55.461 1.00 95.95 ? 20 GLY D O 1 +ATOM 7239 N N . ASP D 1 24 ? 55.180 57.069 57.697 1.00 123.36 ? 21 ASP D N 1 +ATOM 7240 C CA . ASP D 1 24 ? 56.579 56.858 58.057 1.00 84.72 ? 21 ASP D CA 1 +ATOM 7241 C C . ASP D 1 24 ? 56.646 56.274 59.485 1.00 98.61 ? 21 ASP D C 1 +ATOM 7242 O O . ASP D 1 24 ? 56.569 57.010 60.469 1.00 102.62 ? 21 ASP D O 1 +ATOM 7243 C CB . ASP D 1 24 ? 57.332 58.196 57.977 1.00 149.80 ? 21 ASP D CB 1 +ATOM 7244 C CG . ASP D 1 24 ? 58.847 58.033 57.964 1.00 155.61 ? 21 ASP D CG 1 +ATOM 7245 O OD1 . ASP D 1 24 ? 59.350 56.973 58.395 1.00 136.44 ? 21 ASP D OD1 1 +ATOM 7246 O OD2 . ASP D 1 24 ? 59.537 58.981 57.523 1.00 101.11 ? 21 ASP D OD2 1 +ATOM 7247 N N . VAL D 1 25 ? 56.776 54.953 59.595 1.00 90.87 ? 22 VAL D N 1 +ATOM 7248 C CA . VAL D 1 25 ? 56.791 54.286 60.903 1.00 89.41 ? 22 VAL D CA 1 +ATOM 7249 C C . VAL D 1 25 ? 58.058 53.460 61.147 1.00 95.65 ? 22 VAL D C 1 +ATOM 7250 O O . VAL D 1 25 ? 58.236 52.381 60.570 1.00 83.16 ? 22 VAL D O 1 +ATOM 7251 C CB . VAL D 1 25 ? 55.535 53.408 61.109 1.00 86.08 ? 22 VAL D CB 1 +ATOM 7252 C CG1 . VAL D 1 25 ? 55.693 52.488 62.322 1.00 88.17 ? 22 VAL D CG1 1 +ATOM 7253 C CG2 . VAL D 1 25 ? 54.313 54.283 61.262 1.00 92.38 ? 22 VAL D CG2 1 +ATOM 7254 N N . ASN D 1 26 ? 58.920 53.977 62.023 1.00 94.95 ? 23 ASN D N 1 +ATOM 7255 C CA . ASN D 1 26 ? 60.234 53.393 62.294 1.00 83.35 ? 23 ASN D CA 1 +ATOM 7256 C C . ASN D 1 26 ? 61.018 53.295 60.983 1.00 111.98 ? 23 ASN D C 1 +ATOM 7257 O O . ASN D 1 26 ? 61.560 52.240 60.624 1.00 83.54 ? 23 ASN D O 1 +ATOM 7258 C CB . ASN D 1 26 ? 60.116 52.028 62.995 1.00 87.11 ? 23 ASN D CB 1 +ATOM 7259 C CG . ASN D 1 26 ? 59.860 52.140 64.510 1.00 118.75 ? 23 ASN D CG 1 +ATOM 7260 O OD1 . ASN D 1 26 ? 59.582 53.218 65.050 1.00 91.47 ? 23 ASN D OD1 1 +ATOM 7261 N ND2 . ASN D 1 26 ? 59.951 51.003 65.198 1.00 91.42 ? 23 ASN D ND2 1 +ATOM 7262 N N . GLY D 1 27 ? 61.036 54.415 60.264 1.00 102.50 ? 24 GLY D N 1 +ATOM 7263 C CA . GLY D 1 27 ? 61.672 54.509 58.964 1.00 93.11 ? 24 GLY D CA 1 +ATOM 7264 C C . GLY D 1 27 ? 61.092 53.641 57.858 1.00 99.40 ? 24 GLY D C 1 +ATOM 7265 O O . GLY D 1 27 ? 61.694 53.542 56.787 1.00 98.73 ? 24 GLY D O 1 +ATOM 7266 N N . HIS D 1 28 ? 59.959 52.986 58.116 1.00 100.09 ? 25 HIS D N 1 +ATOM 7267 C CA . HIS D 1 28 ? 59.174 52.376 57.043 1.00 104.39 ? 25 HIS D CA 1 +ATOM 7268 C C . HIS D 1 28 ? 58.235 53.415 56.487 1.00 110.48 ? 25 HIS D C 1 +ATOM 7269 O O . HIS D 1 28 ? 57.300 53.853 57.166 1.00 73.94 ? 25 HIS D O 1 +ATOM 7270 C CB . HIS D 1 28 ? 58.318 51.220 57.531 1.00 66.74 ? 25 HIS D CB 1 +ATOM 7271 C CG . HIS D 1 28 ? 59.097 50.019 57.948 1.00 128.13 ? 25 HIS D CG 1 +ATOM 7272 N ND1 . HIS D 1 28 ? 59.749 49.943 59.159 1.00 109.72 ? 25 HIS D ND1 1 +ATOM 7273 C CD2 . HIS D 1 28 ? 59.312 48.836 57.326 1.00 116.45 ? 25 HIS D CD2 1 +ATOM 7274 C CE1 . HIS D 1 28 ? 60.337 48.765 59.264 1.00 93.44 ? 25 HIS D CE1 1 +ATOM 7275 N NE2 . HIS D 1 28 ? 60.089 48.075 58.165 1.00 123.07 ? 25 HIS D NE2 1 +ATOM 7276 N N . LYS D 1 29 ? 58.490 53.812 55.252 1.00 95.78 ? 26 LYS D N 1 +ATOM 7277 C CA . LYS D 1 29 ? 57.627 54.745 54.572 1.00 92.35 ? 26 LYS D CA 1 +ATOM 7278 C C . LYS D 1 29 ? 56.555 53.908 53.888 1.00 109.20 ? 26 LYS D C 1 +ATOM 7279 O O . LYS D 1 29 ? 56.699 52.684 53.789 1.00 94.11 ? 26 LYS D O 1 +ATOM 7280 C CB . LYS D 1 29 ? 58.442 55.580 53.584 1.00 91.05 ? 26 LYS D CB 1 +ATOM 7281 C CG . LYS D 1 29 ? 59.576 56.370 54.250 1.00 79.53 ? 26 LYS D CG 1 +ATOM 7282 C CD . LYS D 1 29 ? 60.530 56.988 53.233 1.00 116.67 ? 26 LYS D CD 1 +ATOM 7283 C CE . LYS D 1 29 ? 61.443 58.033 53.868 1.00 102.61 ? 26 LYS D CE 1 +ATOM 7284 N NZ . LYS D 1 29 ? 60.764 59.331 54.136 1.00 127.72 ? 26 LYS D NZ 1 +ATOM 7285 N N . PHE D 1 30 ? 55.468 54.562 53.476 1.00 80.52 ? 27 PHE D N 1 +ATOM 7286 C CA . PHE D 1 30 ? 54.360 53.923 52.758 1.00 87.24 ? 27 PHE D CA 1 +ATOM 7287 C C . PHE D 1 30 ? 53.320 54.963 52.369 1.00 96.22 ? 27 PHE D C 1 +ATOM 7288 O O . PHE D 1 30 ? 53.296 56.066 52.916 1.00 80.06 ? 27 PHE D O 1 +ATOM 7289 C CB . PHE D 1 30 ? 53.692 52.803 53.576 1.00 100.06 ? 27 PHE D CB 1 +ATOM 7290 C CG . PHE D 1 30 ? 53.029 53.275 54.849 1.00 92.43 ? 27 PHE D CG 1 +ATOM 7291 C CD1 . PHE D 1 30 ? 53.783 53.566 55.971 1.00 104.15 ? 27 PHE D CD1 1 +ATOM 7292 C CD2 . PHE D 1 30 ? 51.656 53.413 54.928 1.00 93.21 ? 27 PHE D CD2 1 +ATOM 7293 C CE1 . PHE D 1 30 ? 53.187 53.990 57.143 1.00 101.68 ? 27 PHE D CE1 1 +ATOM 7294 C CE2 . PHE D 1 30 ? 51.053 53.843 56.101 1.00 100.76 ? 27 PHE D CE2 1 +ATOM 7295 C CZ . PHE D 1 30 ? 51.823 54.132 57.207 1.00 88.07 ? 27 PHE D CZ 1 +ATOM 7296 N N . SER D 1 31 ? 52.465 54.605 51.418 1.00 88.96 ? 28 SER D N 1 +ATOM 7297 C CA . SER D 1 31 ? 51.388 55.486 50.995 1.00 89.56 ? 28 SER D CA 1 +ATOM 7298 C C . SER D 1 31 ? 50.083 54.724 50.805 1.00 94.31 ? 28 SER D C 1 +ATOM 7299 O O . SER D 1 31 ? 50.076 53.567 50.362 1.00 76.34 ? 28 SER D O 1 +ATOM 7300 C CB . SER D 1 31 ? 51.770 56.236 49.720 1.00 93.94 ? 28 SER D CB 1 +ATOM 7301 O OG . SER D 1 31 ? 52.858 57.109 49.962 1.00 136.05 ? 28 SER D OG 1 +ATOM 7302 N N . VAL D 1 32 ? 48.984 55.382 51.176 1.00 87.10 ? 29 VAL D N 1 +ATOM 7303 C CA . VAL D 1 32 ? 47.639 54.831 51.005 1.00 91.48 ? 29 VAL D CA 1 +ATOM 7304 C C . VAL D 1 32 ? 46.687 55.798 50.290 1.00 81.85 ? 29 VAL D C 1 +ATOM 7305 O O . VAL D 1 32 ? 46.652 56.998 50.589 1.00 64.74 ? 29 VAL D O 1 +ATOM 7306 C CB . VAL D 1 32 ? 46.996 54.413 52.349 1.00 80.04 ? 29 VAL D CB 1 +ATOM 7307 C CG1 . VAL D 1 32 ? 45.693 53.686 52.096 1.00 82.85 ? 29 VAL D CG1 1 +ATOM 7308 C CG2 . VAL D 1 32 ? 47.927 53.513 53.137 1.00 67.50 ? 29 VAL D CG2 1 +ATOM 7309 N N . SER D 1 33 ? 45.933 55.257 49.332 1.00 76.44 ? 30 SER D N 1 +ATOM 7310 C CA . SER D 1 33 ? 44.855 55.977 48.646 1.00 98.08 ? 30 SER D CA 1 +ATOM 7311 C C . SER D 1 33 ? 43.494 55.335 48.911 1.00 93.90 ? 30 SER D C 1 +ATOM 7312 O O . SER D 1 33 ? 43.321 54.118 48.770 1.00 76.10 ? 30 SER D O 1 +ATOM 7313 C CB . SER D 1 33 ? 45.097 56.038 47.135 1.00 86.78 ? 30 SER D CB 1 +ATOM 7314 O OG . SER D 1 33 ? 45.819 57.202 46.779 1.00 119.45 ? 30 SER D OG 1 +ATOM 7315 N N . GLY D 1 34 ? 42.525 56.157 49.292 1.00 90.53 ? 31 GLY D N 1 +ATOM 7316 C CA . GLY D 1 34 ? 41.196 55.653 49.564 1.00 69.55 ? 31 GLY D CA 1 +ATOM 7317 C C . GLY D 1 34 ? 40.105 56.423 48.852 1.00 85.06 ? 31 GLY D C 1 +ATOM 7318 O O . GLY D 1 34 ? 40.175 57.647 48.728 1.00 77.97 ? 31 GLY D O 1 +ATOM 7319 N N . GLU D 1 35 ? 39.093 55.700 48.381 1.00 71.92 ? 32 GLU D N 1 +ATOM 7320 C CA . GLU D 1 35 ? 37.909 56.326 47.800 1.00 97.68 ? 32 GLU D CA 1 +ATOM 7321 C C . GLU D 1 35 ? 36.610 55.682 48.278 1.00 86.40 ? 32 GLU D C 1 +ATOM 7322 O O . GLU D 1 35 ? 36.567 54.494 48.618 1.00 77.66 ? 32 GLU D O 1 +ATOM 7323 C CB . GLU D 1 35 ? 37.951 56.252 46.275 1.00 82.29 ? 32 GLU D CB 1 +ATOM 7324 C CG . GLU D 1 35 ? 37.735 54.851 45.731 1.00 83.15 ? 32 GLU D CG 1 +ATOM 7325 C CD . GLU D 1 35 ? 38.036 54.750 44.254 1.00 164.44 ? 32 GLU D CD 1 +ATOM 7326 O OE1 . GLU D 1 35 ? 37.511 55.573 43.490 1.00 167.38 ? 32 GLU D OE1 1 +ATOM 7327 O OE2 . GLU D 1 35 ? 38.810 53.858 43.853 1.00 209.21 ? 32 GLU D OE2 1 +ATOM 7328 N N . GLY D 1 36 ? 35.549 56.480 48.275 1.00 98.99 ? 33 GLY D N 1 +ATOM 7329 C CA . GLY D 1 36 ? 34.209 55.987 48.522 1.00 76.86 ? 33 GLY D CA 1 +ATOM 7330 C C . GLY D 1 36 ? 33.229 57.117 48.766 1.00 75.75 ? 33 GLY D C 1 +ATOM 7331 O O . GLY D 1 36 ? 33.367 58.207 48.210 1.00 76.39 ? 33 GLY D O 1 +ATOM 7332 N N . GLU D 1 37 ? 32.251 56.862 49.626 1.00 85.41 ? 34 GLU D N 1 +ATOM 7333 C CA . GLU D 1 37 ? 31.163 57.805 49.840 1.00 89.51 ? 34 GLU D CA 1 +ATOM 7334 C C . GLU D 1 37 ? 30.570 57.715 51.244 1.00 80.11 ? 34 GLU D C 1 +ATOM 7335 O O . GLU D 1 37 ? 30.597 56.665 51.890 1.00 75.40 ? 34 GLU D O 1 +ATOM 7336 C CB . GLU D 1 37 ? 30.066 57.562 48.809 1.00 82.68 ? 34 GLU D CB 1 +ATOM 7337 C CG . GLU D 1 37 ? 29.453 56.181 48.945 1.00 136.51 ? 34 GLU D CG 1 +ATOM 7338 C CD . GLU D 1 37 ? 28.456 55.868 47.865 1.00 138.15 ? 34 GLU D CD 1 +ATOM 7339 O OE1 . GLU D 1 37 ? 27.982 56.810 47.204 1.00 149.49 ? 34 GLU D OE1 1 +ATOM 7340 O OE2 . GLU D 1 37 ? 28.167 54.667 47.672 1.00 138.63 ? 34 GLU D OE2 1 +ATOM 7341 N N . GLY D 1 38 ? 30.021 58.834 51.700 1.00 75.25 ? 35 GLY D N 1 +ATOM 7342 C CA . GLY D 1 38 ? 29.415 58.909 53.011 1.00 87.68 ? 35 GLY D CA 1 +ATOM 7343 C C . GLY D 1 38 ? 28.069 59.605 52.999 1.00 81.36 ? 35 GLY D C 1 +ATOM 7344 O O . GLY D 1 38 ? 27.863 60.588 52.289 1.00 78.41 ? 35 GLY D O 1 +ATOM 7345 N N . ASP D 1 39 ? 27.155 59.083 53.808 1.00 94.96 ? 36 ASP D N 1 +ATOM 7346 C CA . ASP D 1 39 ? 25.795 59.593 53.909 1.00 93.01 ? 36 ASP D CA 1 +ATOM 7347 C C . ASP D 1 39 ? 25.537 60.131 55.319 1.00 67.22 ? 36 ASP D C 1 +ATOM 7348 O O . ASP D 1 39 ? 25.145 59.376 56.207 1.00 69.57 ? 36 ASP D O 1 +ATOM 7349 C CB . ASP D 1 39 ? 24.807 58.467 53.583 1.00 83.55 ? 36 ASP D CB 1 +ATOM 7350 C CG . ASP D 1 39 ? 23.579 58.961 52.846 1.00 127.40 ? 36 ASP D CG 1 +ATOM 7351 O OD1 . ASP D 1 39 ? 23.239 60.154 53.001 1.00 128.06 ? 36 ASP D OD1 1 +ATOM 7352 O OD2 . ASP D 1 39 ? 22.954 58.156 52.116 1.00 104.82 ? 36 ASP D OD2 1 +ATOM 7353 N N . ALA D 1 40 ? 25.761 61.427 55.528 1.00 88.89 ? 37 ALA D N 1 +ATOM 7354 C CA . ALA D 1 40 ? 25.619 62.020 56.863 1.00 80.36 ? 37 ALA D CA 1 +ATOM 7355 C C . ALA D 1 40 ? 24.238 61.769 57.456 1.00 77.15 ? 37 ALA D C 1 +ATOM 7356 O O . ALA D 1 40 ? 24.109 61.457 58.631 1.00 83.99 ? 37 ALA D O 1 +ATOM 7357 C CB . ALA D 1 40 ? 25.918 63.518 56.830 1.00 66.76 ? 37 ALA D CB 1 +ATOM 7358 N N . THR D 1 41 ? 23.220 61.898 56.612 1.00 111.73 ? 38 THR D N 1 +ATOM 7359 C CA . THR D 1 41 ? 21.825 61.704 56.976 1.00 73.24 ? 38 THR D CA 1 +ATOM 7360 C C . THR D 1 41 ? 21.579 60.437 57.794 1.00 75.69 ? 38 THR D C 1 +ATOM 7361 O O . THR D 1 41 ? 20.748 60.438 58.693 1.00 86.37 ? 38 THR D O 1 +ATOM 7362 C CB . THR D 1 41 ? 20.946 61.667 55.707 1.00 85.26 ? 38 THR D CB 1 +ATOM 7363 O OG1 . THR D 1 41 ? 21.319 62.739 54.831 1.00 97.87 ? 38 THR D OG1 1 +ATOM 7364 C CG2 . THR D 1 41 ? 19.485 61.798 56.057 1.00 55.78 ? 38 THR D CG2 1 +ATOM 7365 N N . TYR D 1 42 ? 22.301 59.360 57.492 1.00 70.78 ? 39 TYR D N 1 +ATOM 7366 C CA . TYR D 1 42 ? 22.134 58.112 58.236 1.00 84.60 ? 39 TYR D CA 1 +ATOM 7367 C C . TYR D 1 42 ? 23.445 57.675 58.871 1.00 73.13 ? 39 TYR D C 1 +ATOM 7368 O O . TYR D 1 42 ? 23.633 56.494 59.185 1.00 73.22 ? 39 TYR D O 1 +ATOM 7369 C CB . TYR D 1 42 ? 21.558 57.011 57.341 1.00 57.88 ? 39 TYR D CB 1 +ATOM 7370 C CG . TYR D 1 42 ? 20.446 57.535 56.485 1.00 80.77 ? 39 TYR D CG 1 +ATOM 7371 C CD1 . TYR D 1 42 ? 20.722 58.122 55.259 1.00 90.29 ? 39 TYR D CD1 1 +ATOM 7372 C CD2 . TYR D 1 42 ? 19.122 57.493 56.915 1.00 90.70 ? 39 TYR D CD2 1 +ATOM 7373 C CE1 . TYR D 1 42 ? 19.720 58.638 54.470 1.00 113.47 ? 39 TYR D CE1 1 +ATOM 7374 C CE2 . TYR D 1 42 ? 18.096 58.011 56.123 1.00 86.33 ? 39 TYR D CE2 1 +ATOM 7375 C CZ . TYR D 1 42 ? 18.409 58.584 54.900 1.00 102.42 ? 39 TYR D CZ 1 +ATOM 7376 O OH . TYR D 1 42 ? 17.427 59.106 54.087 1.00 87.60 ? 39 TYR D OH 1 +ATOM 7377 N N . GLY D 1 43 ? 24.337 58.651 59.055 1.00 77.97 ? 40 GLY D N 1 +ATOM 7378 C CA . GLY D 1 43 ? 25.633 58.461 59.688 1.00 72.70 ? 40 GLY D CA 1 +ATOM 7379 C C . GLY D 1 43 ? 26.408 57.276 59.146 1.00 91.85 ? 40 GLY D C 1 +ATOM 7380 O O . GLY D 1 43 ? 26.837 56.398 59.895 1.00 75.12 ? 40 GLY D O 1 +ATOM 7381 N N . LYS D 1 44 ? 26.592 57.254 57.834 1.00 74.60 ? 41 LYS D N 1 +ATOM 7382 C CA . LYS D 1 44 ? 27.094 56.069 57.174 1.00 51.64 ? 41 LYS D CA 1 +ATOM 7383 C C . LYS D 1 44 ? 28.342 56.390 56.372 1.00 91.84 ? 41 LYS D C 1 +ATOM 7384 O O . LYS D 1 44 ? 28.408 57.414 55.693 1.00 88.52 ? 41 LYS D O 1 +ATOM 7385 C CB . LYS D 1 44 ? 26.012 55.510 56.266 1.00 69.69 ? 41 LYS D CB 1 +ATOM 7386 C CG . LYS D 1 44 ? 26.271 54.101 55.843 1.00 85.56 ? 41 LYS D CG 1 +ATOM 7387 C CD . LYS D 1 44 ? 25.207 53.617 54.894 1.00 67.06 ? 41 LYS D CD 1 +ATOM 7388 C CE . LYS D 1 44 ? 25.843 52.823 53.774 1.00 113.26 ? 41 LYS D CE 1 +ATOM 7389 N NZ . LYS D 1 44 ? 24.865 52.011 52.999 1.00 108.25 ? 41 LYS D NZ 1 +ATOM 7390 N N . LEU D 1 45 ? 29.337 55.514 56.471 1.00 90.66 ? 42 LEU D N 1 +ATOM 7391 C CA . LEU D 1 45 ? 30.597 55.682 55.760 1.00 77.74 ? 42 LEU D CA 1 +ATOM 7392 C C . LEU D 1 45 ? 30.983 54.373 55.071 1.00 55.38 ? 42 LEU D C 1 +ATOM 7393 O O . LEU D 1 45 ? 30.881 53.299 55.662 1.00 87.43 ? 42 LEU D O 1 +ATOM 7394 C CB . LEU D 1 45 ? 31.693 56.116 56.735 1.00 73.36 ? 42 LEU D CB 1 +ATOM 7395 C CG . LEU D 1 45 ? 32.738 57.123 56.259 1.00 86.15 ? 42 LEU D CG 1 +ATOM 7396 C CD1 . LEU D 1 45 ? 32.104 58.461 55.940 1.00 113.76 ? 42 LEU D CD1 1 +ATOM 7397 C CD2 . LEU D 1 45 ? 33.811 57.283 57.314 1.00 90.80 ? 42 LEU D CD2 1 +ATOM 7398 N N . THR D 1 46 ? 31.381 54.448 53.807 1.00 75.77 ? 43 THR D N 1 +ATOM 7399 C CA . THR D 1 46 ? 31.944 53.278 53.128 1.00 100.64 ? 43 THR D CA 1 +ATOM 7400 C C . THR D 1 46 ? 33.214 53.684 52.389 1.00 84.02 ? 43 THR D C 1 +ATOM 7401 O O . THR D 1 46 ? 33.210 54.646 51.622 1.00 88.91 ? 43 THR D O 1 +ATOM 7402 C CB . THR D 1 46 ? 30.979 52.627 52.111 1.00 77.36 ? 43 THR D CB 1 +ATOM 7403 O OG1 . THR D 1 46 ? 31.251 53.147 50.811 1.00 130.17 ? 43 THR D OG1 1 +ATOM 7404 C CG2 . THR D 1 46 ? 29.520 52.879 52.463 1.00 84.29 ? 43 THR D CG2 1 +ATOM 7405 N N . LEU D 1 47 ? 34.298 52.951 52.619 1.00 73.93 ? 44 LEU D N 1 +ATOM 7406 C CA . LEU D 1 47 ? 35.602 53.345 52.105 1.00 74.14 ? 44 LEU D CA 1 +ATOM 7407 C C . LEU D 1 47 ? 36.458 52.149 51.736 1.00 69.25 ? 44 LEU D C 1 +ATOM 7408 O O . LEU D 1 47 ? 36.419 51.114 52.407 1.00 63.04 ? 44 LEU D O 1 +ATOM 7409 C CB . LEU D 1 47 ? 36.324 54.225 53.123 1.00 66.49 ? 44 LEU D CB 1 +ATOM 7410 C CG . LEU D 1 47 ? 35.864 55.685 53.108 1.00 88.51 ? 44 LEU D CG 1 +ATOM 7411 C CD1 . LEU D 1 47 ? 36.426 56.447 54.289 1.00 92.49 ? 44 LEU D CD1 1 +ATOM 7412 C CD2 . LEU D 1 47 ? 36.257 56.360 51.805 1.00 74.71 ? 44 LEU D CD2 1 +ATOM 7413 N N . LYS D 1 48 ? 37.202 52.290 50.638 1.00 74.17 ? 45 LYS D N 1 +ATOM 7414 C CA . LYS D 1 48 ? 38.191 51.292 50.231 1.00 62.81 ? 45 LYS D CA 1 +ATOM 7415 C C . LYS D 1 48 ? 39.592 51.869 50.121 1.00 88.79 ? 45 LYS D C 1 +ATOM 7416 O O . LYS D 1 48 ? 39.828 52.904 49.481 1.00 70.04 ? 45 LYS D O 1 +ATOM 7417 C CB . LYS D 1 48 ? 37.824 50.609 48.920 1.00 64.22 ? 45 LYS D CB 1 +ATOM 7418 C CG . LYS D 1 48 ? 38.701 49.408 48.606 1.00 56.28 ? 45 LYS D CG 1 +ATOM 7419 C CD . LYS D 1 48 ? 38.594 49.001 47.144 1.00 65.89 ? 45 LYS D CD 1 +ATOM 7420 C CE . LYS D 1 48 ? 39.106 47.588 46.944 1.00 87.24 ? 45 LYS D CE 1 +ATOM 7421 N NZ . LYS D 1 48 ? 38.765 47.036 45.619 1.00 80.56 ? 45 LYS D NZ 1 +ATOM 7422 N N . PHE D 1 49 ? 40.519 51.164 50.752 1.00 79.17 ? 46 PHE D N 1 +ATOM 7423 C CA . PHE D 1 49 ? 41.901 51.574 50.779 1.00 72.51 ? 46 PHE D CA 1 +ATOM 7424 C C . PHE D 1 49 ? 42.782 50.595 50.019 1.00 70.84 ? 46 PHE D C 1 +ATOM 7425 O O . PHE D 1 49 ? 42.675 49.383 50.186 1.00 74.05 ? 46 PHE D O 1 +ATOM 7426 C CB . PHE D 1 49 ? 42.340 51.734 52.225 1.00 78.11 ? 46 PHE D CB 1 +ATOM 7427 C CG . PHE D 1 49 ? 41.509 52.723 52.988 1.00 80.52 ? 46 PHE D CG 1 +ATOM 7428 C CD1 . PHE D 1 49 ? 41.663 54.083 52.777 1.00 78.35 ? 46 PHE D CD1 1 +ATOM 7429 C CD2 . PHE D 1 49 ? 40.565 52.301 53.898 1.00 82.18 ? 46 PHE D CD2 1 +ATOM 7430 C CE1 . PHE D 1 49 ? 40.903 55.000 53.470 1.00 74.86 ? 46 PHE D CE1 1 +ATOM 7431 C CE2 . PHE D 1 49 ? 39.805 53.219 54.594 1.00 93.45 ? 46 PHE D CE2 1 +ATOM 7432 C CZ . PHE D 1 49 ? 39.972 54.567 54.373 1.00 65.05 ? 46 PHE D CZ 1 +ATOM 7433 N N . ILE D 1 50 ? 43.619 51.149 49.149 1.00 87.11 ? 47 ILE D N 1 +ATOM 7434 C CA . ILE D 1 50 ? 44.620 50.391 48.417 1.00 67.91 ? 47 ILE D CA 1 +ATOM 7435 C C . ILE D 1 50 ? 45.984 50.821 48.941 1.00 91.75 ? 47 ILE D C 1 +ATOM 7436 O O . ILE D 1 50 ? 46.277 52.019 49.003 1.00 67.63 ? 47 ILE D O 1 +ATOM 7437 C CB . ILE D 1 50 ? 44.571 50.711 46.900 1.00 81.77 ? 47 ILE D CB 1 +ATOM 7438 C CG1 . ILE D 1 50 ? 43.255 50.252 46.268 1.00 97.68 ? 47 ILE D CG1 1 +ATOM 7439 C CG2 . ILE D 1 50 ? 45.727 50.059 46.179 1.00 110.33 ? 47 ILE D CG2 1 +ATOM 7440 C CD1 . ILE D 1 50 ? 43.007 48.768 46.377 1.00 96.15 ? 47 ILE D CD1 1 +ATOM 7441 N N . CYS D 1 51 ? 46.822 49.868 49.335 1.00 95.85 ? 48 CYS D N 1 +ATOM 7442 C CA . CYS D 1 51 ? 48.221 50.216 49.574 1.00 114.85 ? 48 CYS D CA 1 +ATOM 7443 C C . CYS D 1 51 ? 48.968 50.436 48.257 1.00 88.33 ? 48 CYS D C 1 +ATOM 7444 O O . CYS D 1 51 ? 49.208 49.485 47.504 1.00 104.80 ? 48 CYS D O 1 +ATOM 7445 C CB . CYS D 1 51 ? 48.948 49.163 50.398 1.00 134.45 ? 48 CYS D CB 1 +ATOM 7446 S SG . CYS D 1 51 ? 50.529 49.779 50.982 1.00 91.29 ? 48 CYS D SG 1 +ATOM 7447 N N . THR D 1 52 ? 49.341 51.692 48.001 1.00 85.44 ? 49 THR D N 1 +ATOM 7448 C CA . THR D 1 52 ? 49.952 52.101 46.732 1.00 92.46 ? 49 THR D CA 1 +ATOM 7449 C C . THR D 1 52 ? 51.470 51.872 46.671 1.00 81.06 ? 49 THR D C 1 +ATOM 7450 O O . THR D 1 52 ? 52.093 52.067 45.626 1.00 97.79 ? 49 THR D O 1 +ATOM 7451 C CB . THR D 1 52 ? 49.603 53.589 46.344 1.00 85.86 ? 49 THR D CB 1 +ATOM 7452 O OG1 . THR D 1 52 ? 49.866 54.482 47.437 1.00 73.87 ? 49 THR D OG1 1 +ATOM 7453 C CG2 . THR D 1 52 ? 48.149 53.725 45.956 1.00 78.44 ? 49 THR D CG2 1 +ATOM 7454 N N . THR D 1 53 ? 52.059 51.446 47.787 1.00 103.94 ? 50 THR D N 1 +ATOM 7455 C CA . THR D 1 53 ? 53.506 51.229 47.861 1.00 60.87 ? 50 THR D CA 1 +ATOM 7456 C C . THR D 1 53 ? 53.910 49.759 48.045 1.00 87.48 ? 50 THR D C 1 +ATOM 7457 O O . THR D 1 53 ? 55.075 49.466 48.284 1.00 125.41 ? 50 THR D O 1 +ATOM 7458 C CB . THR D 1 53 ? 54.170 52.087 48.983 1.00 79.94 ? 50 THR D CB 1 +ATOM 7459 O OG1 . THR D 1 53 ? 53.644 51.724 50.268 1.00 80.97 ? 50 THR D OG1 1 +ATOM 7460 C CG2 . THR D 1 53 ? 53.933 53.560 48.748 1.00 70.37 ? 50 THR D CG2 1 +ATOM 7461 N N . GLY D 1 54 ? 52.959 48.839 47.932 1.00 76.34 ? 51 GLY D N 1 +ATOM 7462 C CA . GLY D 1 54 ? 53.247 47.420 48.096 1.00 87.06 ? 51 GLY D CA 1 +ATOM 7463 C C . GLY D 1 54 ? 52.466 46.843 49.258 1.00 70.76 ? 51 GLY D C 1 +ATOM 7464 O O . GLY D 1 54 ? 51.265 47.074 49.349 1.00 147.64 ? 51 GLY D O 1 +ATOM 7465 N N . LYS D 1 55 ? 53.137 46.094 50.135 1.00 110.60 ? 52 LYS D N 1 +ATOM 7466 C CA . LYS D 1 55 ? 52.542 45.670 51.402 1.00 88.34 ? 52 LYS D CA 1 +ATOM 7467 C C . LYS D 1 55 ? 52.640 46.766 52.429 1.00 75.36 ? 52 LYS D C 1 +ATOM 7468 O O . LYS D 1 55 ? 53.420 47.708 52.284 1.00 85.38 ? 52 LYS D O 1 +ATOM 7469 C CB . LYS D 1 55 ? 53.225 44.426 51.950 1.00 58.42 ? 52 LYS D CB 1 +ATOM 7470 C CG . LYS D 1 55 ? 52.359 43.159 51.797 1.00 124.50 ? 52 LYS D CG 1 +ATOM 7471 C CD . LYS D 1 55 ? 52.902 41.970 52.612 1.00 167.15 ? 52 LYS D CD 1 +ATOM 7472 C CE . LYS D 1 55 ? 52.942 40.713 51.754 1.00 176.93 ? 52 LYS D CE 1 +ATOM 7473 N NZ . LYS D 1 55 ? 53.333 39.480 52.511 1.00 157.61 ? 52 LYS D NZ 1 +ATOM 7474 N N . LEU D 1 56 ? 51.847 46.619 53.480 1.00 96.62 ? 53 LEU D N 1 +ATOM 7475 C CA . LEU D 1 56 ? 51.773 47.621 54.522 1.00 87.77 ? 53 LEU D CA 1 +ATOM 7476 C C . LEU D 1 56 ? 52.723 47.261 55.674 1.00 77.74 ? 53 LEU D C 1 +ATOM 7477 O O . LEU D 1 56 ? 52.783 46.107 56.115 1.00 88.64 ? 53 LEU D O 1 +ATOM 7478 C CB . LEU D 1 56 ? 50.320 47.776 54.998 1.00 82.09 ? 53 LEU D CB 1 +ATOM 7479 C CG . LEU D 1 56 ? 49.892 49.144 55.540 1.00 92.41 ? 53 LEU D CG 1 +ATOM 7480 C CD1 . LEU D 1 56 ? 49.854 50.164 54.440 1.00 72.93 ? 53 LEU D CD1 1 +ATOM 7481 C CD2 . LEU D 1 56 ? 48.551 49.053 56.207 1.00 52.48 ? 53 LEU D CD2 1 +ATOM 7482 N N . PRO D 1 57 ? 53.498 48.247 56.145 1.00 94.62 ? 54 PRO D N 1 +ATOM 7483 C CA . PRO D 1 57 ? 54.405 48.018 57.277 1.00 81.26 ? 54 PRO D CA 1 +ATOM 7484 C C . PRO D 1 57 ? 53.658 47.667 58.566 1.00 98.03 ? 54 PRO D C 1 +ATOM 7485 O O . PRO D 1 57 ? 54.106 46.834 59.352 1.00 87.95 ? 54 PRO D O 1 +ATOM 7486 C CB . PRO D 1 57 ? 55.110 49.369 57.435 1.00 75.28 ? 54 PRO D CB 1 +ATOM 7487 C CG . PRO D 1 57 ? 54.242 50.363 56.730 1.00 76.07 ? 54 PRO D CG 1 +ATOM 7488 C CD . PRO D 1 57 ? 53.608 49.613 55.607 1.00 93.44 ? 54 PRO D CD 1 +ATOM 7489 N N . VAL D 1 58 ? 52.507 48.300 58.749 1.00 96.29 ? 55 VAL D N 1 +ATOM 7490 C CA . VAL D 1 58 ? 51.746 48.246 59.985 1.00 93.58 ? 55 VAL D CA 1 +ATOM 7491 C C . VAL D 1 58 ? 50.455 47.451 59.749 1.00 103.28 ? 55 VAL D C 1 +ATOM 7492 O O . VAL D 1 58 ? 50.082 47.237 58.599 1.00 86.43 ? 55 VAL D O 1 +ATOM 7493 C CB . VAL D 1 58 ? 51.450 49.682 60.402 1.00 83.19 ? 55 VAL D CB 1 +ATOM 7494 C CG1 . VAL D 1 58 ? 52.754 50.393 60.664 1.00 78.99 ? 55 VAL D CG1 1 +ATOM 7495 C CG2 . VAL D 1 58 ? 50.722 50.396 59.291 1.00 91.19 ? 55 VAL D CG2 1 +ATOM 7496 N N . PRO D 1 59 ? 49.775 46.987 60.820 1.00 94.04 ? 56 PRO D N 1 +ATOM 7497 C CA . PRO D 1 59 ? 48.525 46.260 60.574 1.00 92.44 ? 56 PRO D CA 1 +ATOM 7498 C C . PRO D 1 59 ? 47.454 47.235 60.108 1.00 110.96 ? 56 PRO D C 1 +ATOM 7499 O O . PRO D 1 59 ? 47.489 48.412 60.487 1.00 90.55 ? 56 PRO D O 1 +ATOM 7500 C CB . PRO D 1 59 ? 48.144 45.710 61.954 1.00 73.26 ? 56 PRO D CB 1 +ATOM 7501 C CG . PRO D 1 59 ? 49.238 46.068 62.863 1.00 92.18 ? 56 PRO D CG 1 +ATOM 7502 C CD . PRO D 1 59 ? 49.996 47.194 62.258 1.00 91.14 ? 56 PRO D CD 1 +ATOM 7503 N N . TRP D 1 60 ? 46.525 46.769 59.284 1.00 101.22 ? 57 TRP D N 1 +ATOM 7504 C CA . TRP D 1 60 ? 45.474 47.655 58.800 1.00 60.84 ? 57 TRP D CA 1 +ATOM 7505 C C . TRP D 1 60 ? 44.666 48.329 59.921 1.00 71.88 ? 57 TRP D C 1 +ATOM 7506 O O . TRP D 1 60 ? 44.538 49.557 59.907 1.00 66.49 ? 57 TRP D O 1 +ATOM 7507 C CB . TRP D 1 60 ? 44.573 46.965 57.772 1.00 71.47 ? 57 TRP D CB 1 +ATOM 7508 C CG . TRP D 1 60 ? 45.108 47.006 56.388 1.00 77.79 ? 57 TRP D CG 1 +ATOM 7509 C CD1 . TRP D 1 60 ? 45.579 45.956 55.660 1.00 62.36 ? 57 TRP D CD1 1 +ATOM 7510 C CD2 . TRP D 1 60 ? 45.222 48.161 55.554 1.00 76.66 ? 57 TRP D CD2 1 +ATOM 7511 N NE1 . TRP D 1 60 ? 45.980 46.385 54.421 1.00 72.45 ? 57 TRP D NE1 1 +ATOM 7512 C CE2 . TRP D 1 60 ? 45.769 47.736 54.329 1.00 73.21 ? 57 TRP D CE2 1 +ATOM 7513 C CE3 . TRP D 1 60 ? 44.909 49.515 55.723 1.00 71.06 ? 57 TRP D CE3 1 +ATOM 7514 C CZ2 . TRP D 1 60 ? 46.013 48.616 53.275 1.00 67.17 ? 57 TRP D CZ2 1 +ATOM 7515 C CZ3 . TRP D 1 60 ? 45.151 50.387 54.678 1.00 73.43 ? 57 TRP D CZ3 1 +ATOM 7516 C CH2 . TRP D 1 60 ? 45.701 49.934 53.469 1.00 78.62 ? 57 TRP D CH2 1 +ATOM 7517 N N . PRO D 1 61 ? 44.149 47.542 60.900 1.00 88.50 ? 58 PRO D N 1 +ATOM 7518 C CA . PRO D 1 61 ? 43.386 48.085 62.032 1.00 52.04 ? 58 PRO D CA 1 +ATOM 7519 C C . PRO D 1 61 ? 43.941 49.357 62.672 1.00 59.38 ? 58 PRO D C 1 +ATOM 7520 O O . PRO D 1 61 ? 43.144 50.180 63.109 1.00 82.48 ? 58 PRO D O 1 +ATOM 7521 C CB . PRO D 1 61 ? 43.436 46.943 63.043 1.00 74.78 ? 58 PRO D CB 1 +ATOM 7522 C CG . PRO D 1 61 ? 43.387 45.735 62.207 1.00 86.36 ? 58 PRO D CG 1 +ATOM 7523 C CD . PRO D 1 61 ? 44.169 46.065 60.958 1.00 73.77 ? 58 PRO D CD 1 +ATOM 7524 N N . THR D 1 62 ? 45.261 49.521 62.715 1.00 90.13 ? 59 THR D N 1 +ATOM 7525 C CA . THR D 1 62 ? 45.888 50.669 63.382 1.00 83.00 ? 59 THR D CA 1 +ATOM 7526 C C . THR D 1 62 ? 45.642 52.013 62.721 1.00 86.78 ? 59 THR D C 1 +ATOM 7527 O O . THR D 1 62 ? 46.007 53.058 63.265 1.00 79.55 ? 59 THR D O 1 +ATOM 7528 C CB . THR D 1 62 ? 47.401 50.505 63.444 1.00 87.89 ? 59 THR D CB 1 +ATOM 7529 O OG1 . THR D 1 62 ? 47.886 50.111 62.156 1.00 93.96 ? 59 THR D OG1 1 +ATOM 7530 C CG2 . THR D 1 62 ? 47.763 49.458 64.453 1.00 89.20 ? 59 THR D CG2 1 +ATOM 7531 N N . LEU D 1 63 ? 45.029 51.987 61.547 1.00 93.30 ? 60 LEU D N 1 +ATOM 7532 C CA . LEU D 1 63 ? 44.895 53.194 60.747 1.00 66.45 ? 60 LEU D CA 1 +ATOM 7533 C C . LEU D 1 63 ? 43.460 53.668 60.567 1.00 94.88 ? 60 LEU D C 1 +ATOM 7534 O O . LEU D 1 63 ? 43.240 54.793 60.112 1.00 72.01 ? 60 LEU D O 1 +ATOM 7535 C CB . LEU D 1 63 ? 45.533 52.974 59.385 1.00 85.91 ? 60 LEU D CB 1 +ATOM 7536 C CG . LEU D 1 63 ? 47.038 52.756 59.441 1.00 101.80 ? 60 LEU D CG 1 +ATOM 7537 C CD1 . LEU D 1 63 ? 47.519 52.190 58.114 1.00 95.18 ? 60 LEU D CD1 1 +ATOM 7538 C CD2 . LEU D 1 63 ? 47.714 54.078 59.766 1.00 77.43 ? 60 LEU D CD2 1 +ATOM 7539 N N . VAL D 1 64 ? 42.502 52.813 60.926 1.00 89.00 ? 61 VAL D N 1 +ATOM 7540 C CA . VAL D 1 64 ? 41.079 53.111 60.784 1.00 76.54 ? 61 VAL D CA 1 +ATOM 7541 C C . VAL D 1 64 ? 40.717 54.515 61.258 1.00 67.39 ? 61 VAL D C 1 +ATOM 7542 O O . VAL D 1 64 ? 40.038 55.262 60.562 1.00 76.89 ? 61 VAL D O 1 +ATOM 7543 C CB . VAL D 1 64 ? 40.203 52.102 61.546 1.00 73.75 ? 61 VAL D CB 1 +ATOM 7544 C CG1 . VAL D 1 64 ? 38.761 52.556 61.529 1.00 55.14 ? 61 VAL D CG1 1 +ATOM 7545 C CG2 . VAL D 1 64 ? 40.340 50.707 60.951 1.00 51.91 ? 61 VAL D CG2 1 +ATOM 7546 N N . THR D 1 65 ? 41.196 54.884 62.435 1.00 77.22 ? 62 THR D N 1 +ATOM 7547 C CA . THR D 1 65 ? 40.840 56.171 63.006 1.00 89.11 ? 62 THR D CA 1 +ATOM 7548 C C . THR D 1 65 ? 41.490 57.299 62.246 1.00 68.11 ? 62 THR D C 1 +ATOM 7549 O O . THR D 1 65 ? 41.064 58.445 62.319 1.00 95.97 ? 62 THR D O 1 +ATOM 7550 C CB . THR D 1 65 ? 41.315 56.274 64.447 1.00 90.55 ? 62 THR D CB 1 +ATOM 7551 O OG1 . THR D 1 65 ? 42.739 56.127 64.483 1.00 114.93 ? 62 THR D OG1 1 +ATOM 7552 C CG2 . THR D 1 65 ? 40.683 55.189 65.278 1.00 88.70 ? 62 THR D CG2 1 +ATOM 7553 N N . THR D 1 66 ? 42.553 56.987 61.532 1.00 84.46 ? 63 THR D N 1 +ATOM 7554 C CA . THR D 1 66 ? 43.328 58.059 60.957 1.00 99.89 ? 63 THR D CA 1 +ATOM 7555 C C . THR D 1 66 ? 42.681 58.355 59.641 1.00 98.72 ? 63 THR D C 1 +ATOM 7556 O O . THR D 1 66 ? 42.567 59.518 59.227 1.00 89.83 ? 63 THR D O 1 +ATOM 7557 C CB . THR D 1 66 ? 44.810 57.670 60.790 1.00 103.25 ? 63 THR D CB 1 +ATOM 7558 O OG1 . THR D 1 66 ? 45.314 57.145 62.032 1.00 78.24 ? 63 THR D OG1 1 +ATOM 7559 C CG2 . THR D 1 66 ? 45.636 58.889 60.359 1.00 75.29 ? 63 THR D CG2 1 +ATOM 7560 N N . PHE D 1 67 ? 42.215 57.258 59.041 1.00 100.35 ? 64 PHE D N 1 +ATOM 7561 C CA . PHE D 1 67 ? 41.525 57.262 57.749 1.00 87.10 ? 64 PHE D CA 1 +ATOM 7562 C C . PHE D 1 67 ? 40.030 57.768 57.751 1.00 92.61 ? 64 PHE D C 1 +ATOM 7563 O O . PHE D 1 67 ? 39.649 58.776 56.976 1.00 96.24 ? 64 PHE D O 1 +ATOM 7564 C CB . PHE D 1 67 ? 41.379 55.857 57.162 1.00 83.71 ? 64 PHE D CB 1 +ATOM 7565 C CG . PHE D 1 67 ? 42.621 55.228 56.633 1.00 57.25 ? 64 PHE D CG 1 +ATOM 7566 C CD1 . PHE D 1 67 ? 43.648 55.977 56.089 1.00 81.01 ? 64 PHE D CD1 1 +ATOM 7567 C CD2 . PHE D 1 67 ? 42.737 53.838 56.667 1.00 87.84 ? 64 PHE D CD2 1 +ATOM 7568 C CE1 . PHE D 1 67 ? 44.783 55.357 55.609 1.00 76.29 ? 64 PHE D CE1 1 +ATOM 7569 C CE2 . PHE D 1 67 ? 43.864 53.211 56.190 1.00 85.01 ? 64 PHE D CE2 1 +ATOM 7570 C CZ . PHE D 1 67 ? 44.891 53.970 55.663 1.00 77.19 ? 64 PHE D CZ 1 +HETATM 7571 N N1 . CR2 D 1 68 ? 39.200 57.110 58.528 1.00 89.59 ? 65 CR2 D N1 1 +HETATM 7572 C CA1 . CR2 D 1 68 ? 37.873 57.768 59.086 1.00 77.58 ? 65 CR2 D CA1 1 +HETATM 7573 C C1 . CR2 D 1 68 ? 37.859 58.328 60.545 1.00 92.24 ? 65 CR2 D C1 1 +HETATM 7574 N N2 . CR2 D 1 68 ? 37.500 57.729 61.736 1.00 103.58 ? 65 CR2 D N2 1 +HETATM 7575 N N3 . CR2 D 1 68 ? 38.275 59.576 60.793 1.00 96.08 ? 65 CR2 D N3 1 +HETATM 7576 C C2 . CR2 D 1 68 ? 38.245 59.820 62.065 1.00 95.42 ? 65 CR2 D C2 1 +HETATM 7577 O O2 . CR2 D 1 68 ? 38.607 60.913 62.637 1.00 82.00 ? 65 CR2 D O2 1 +HETATM 7578 C CA2 . CR2 D 1 68 ? 37.741 58.622 62.718 1.00 100.39 ? 65 CR2 D CA2 1 +HETATM 7579 C CA3 . CR2 D 1 68 ? 38.867 60.493 59.869 1.00 62.79 ? 65 CR2 D CA3 1 +HETATM 7580 C C3 . CR2 D 1 68 ? 37.865 61.384 59.214 1.00 82.40 ? 65 CR2 D C3 1 +HETATM 7581 O O3 . CR2 D 1 68 ? 38.171 62.759 59.209 1.00 77.62 ? 65 CR2 D O3 1 +HETATM 7582 C CB2 . CR2 D 1 68 ? 37.466 58.341 64.154 1.00 84.03 ? 65 CR2 D CB2 1 +HETATM 7583 C CG2 . CR2 D 1 68 ? 36.992 57.037 64.704 1.00 81.76 ? 65 CR2 D CG2 1 +HETATM 7584 C CD1 . CR2 D 1 68 ? 36.752 55.937 63.893 1.00 80.63 ? 65 CR2 D CD1 1 +HETATM 7585 C CD2 . CR2 D 1 68 ? 36.930 56.857 66.084 1.00 75.24 ? 65 CR2 D CD2 1 +HETATM 7586 C CE1 . CR2 D 1 68 ? 36.376 54.721 64.440 1.00 94.57 ? 65 CR2 D CE1 1 +HETATM 7587 C CE2 . CR2 D 1 68 ? 36.551 55.640 66.638 1.00 83.94 ? 65 CR2 D CE2 1 +HETATM 7588 C CZ . CR2 D 1 68 ? 36.271 54.567 65.811 1.00 99.29 ? 65 CR2 D CZ 1 +HETATM 7589 O OH . CR2 D 1 68 ? 35.884 53.358 66.347 1.00 80.45 ? 65 CR2 D OH 1 +ATOM 7590 N N . VAL D 1 69 ? 36.617 60.919 59.157 1.00 115.14 ? 68 VAL D N 1 +ATOM 7591 C CA . VAL D 1 69 ? 35.717 61.767 58.467 1.00 91.76 ? 68 VAL D CA 1 +ATOM 7592 C C . VAL D 1 69 ? 34.521 62.252 59.208 1.00 71.24 ? 68 VAL D C 1 +ATOM 7593 O O . VAL D 1 69 ? 33.471 62.433 58.643 1.00 104.68 ? 68 VAL D O 1 +ATOM 7594 C CB . VAL D 1 69 ? 35.668 61.810 56.923 1.00 77.47 ? 68 VAL D CB 1 +ATOM 7595 C CG1 . VAL D 1 69 ? 37.000 62.317 56.423 1.00 69.83 ? 68 VAL D CG1 1 +ATOM 7596 C CG2 . VAL D 1 69 ? 35.289 60.513 56.255 1.00 119.22 ? 68 VAL D CG2 1 +ATOM 7597 N N . GLN D 1 70 ? 34.784 62.612 60.462 1.00 108.30 ? 69 GLN D N 1 +ATOM 7598 C CA . GLN D 1 70 ? 33.724 62.810 61.442 1.00 101.42 ? 69 GLN D CA 1 +ATOM 7599 C C . GLN D 1 70 ? 32.676 63.866 61.079 1.00 80.57 ? 69 GLN D C 1 +ATOM 7600 O O . GLN D 1 70 ? 31.741 64.109 61.841 1.00 123.94 ? 69 GLN D O 1 +ATOM 7601 C CB . GLN D 1 70 ? 34.329 63.089 62.814 1.00 84.24 ? 69 GLN D CB 1 +ATOM 7602 C CG . GLN D 1 70 ? 35.002 61.878 63.455 1.00 108.70 ? 69 GLN D CG 1 +ATOM 7603 C CD . GLN D 1 70 ? 35.970 62.281 64.556 1.00 117.81 ? 69 GLN D CD 1 +ATOM 7604 O OE1 . GLN D 1 70 ? 36.282 63.464 64.715 1.00 108.95 ? 69 GLN D OE1 1 +ATOM 7605 N NE2 . GLN D 1 70 ? 36.453 61.300 65.318 1.00 95.29 ? 69 GLN D NE2 1 +ATOM 7606 N N . CYS D 1 71 ? 32.841 64.477 59.911 1.00 86.60 ? 70 CYS D N 1 +ATOM 7607 C CA . CYS D 1 71 ? 31.831 65.340 59.321 1.00 87.61 ? 70 CYS D CA 1 +ATOM 7608 C C . CYS D 1 71 ? 30.694 64.529 58.687 1.00 104.73 ? 70 CYS D C 1 +ATOM 7609 O O . CYS D 1 71 ? 29.735 65.092 58.174 1.00 97.71 ? 70 CYS D O 1 +ATOM 7610 C CB . CYS D 1 71 ? 32.470 66.283 58.289 1.00 64.94 ? 70 CYS D CB 1 +ATOM 7611 S SG . CYS D 1 71 ? 33.495 65.501 57.006 1.00 106.96 ? 70 CYS D SG 1 +ATOM 7612 N N . PHE D 1 72 ? 30.807 63.206 58.722 1.00 91.16 ? 71 PHE D N 1 +ATOM 7613 C CA . PHE D 1 72 ? 29.760 62.344 58.187 1.00 83.56 ? 71 PHE D CA 1 +ATOM 7614 C C . PHE D 1 72 ? 29.034 61.647 59.324 1.00 89.47 ? 71 PHE D C 1 +ATOM 7615 O O . PHE D 1 72 ? 28.396 60.617 59.128 1.00 128.06 ? 71 PHE D O 1 +ATOM 7616 C CB . PHE D 1 72 ? 30.336 61.306 57.219 1.00 80.23 ? 71 PHE D CB 1 +ATOM 7617 C CG . PHE D 1 72 ? 30.683 61.861 55.865 1.00 83.03 ? 71 PHE D CG 1 +ATOM 7618 C CD1 . PHE D 1 72 ? 31.930 62.404 55.625 1.00 95.10 ? 71 PHE D CD1 1 +ATOM 7619 C CD2 . PHE D 1 72 ? 29.764 61.833 54.832 1.00 100.98 ? 71 PHE D CD2 1 +ATOM 7620 C CE1 . PHE D 1 72 ? 32.247 62.898 54.387 1.00 84.94 ? 71 PHE D CE1 1 +ATOM 7621 C CE2 . PHE D 1 72 ? 30.080 62.339 53.587 1.00 78.57 ? 71 PHE D CE2 1 +ATOM 7622 C CZ . PHE D 1 72 ? 31.323 62.876 53.363 1.00 109.08 ? 71 PHE D CZ 1 +ATOM 7623 N N . SER D 1 73 ? 29.144 62.202 60.521 1.00 79.59 ? 72 SER D N 1 +ATOM 7624 C CA . SER D 1 73 ? 28.389 61.676 61.642 1.00 97.93 ? 72 SER D CA 1 +ATOM 7625 C C . SER D 1 73 ? 26.952 62.169 61.543 1.00 94.95 ? 72 SER D C 1 +ATOM 7626 O O . SER D 1 73 ? 26.701 63.272 61.058 1.00 124.54 ? 72 SER D O 1 +ATOM 7627 C CB . SER D 1 73 ? 29.011 62.117 62.946 1.00 85.40 ? 72 SER D CB 1 +ATOM 7628 N N . ARG D 1 74 ? 26.006 61.355 61.994 1.00 81.42 ? 73 ARG D N 1 +ATOM 7629 C CA . ARG D 1 74 ? 24.618 61.796 62.040 1.00 96.89 ? 73 ARG D CA 1 +ATOM 7630 C C . ARG D 1 74 ? 24.309 62.542 63.328 1.00 90.69 ? 73 ARG D C 1 +ATOM 7631 O O . ARG D 1 74 ? 24.307 61.953 64.414 1.00 86.75 ? 73 ARG D O 1 +ATOM 7632 C CB . ARG D 1 74 ? 23.647 60.627 61.899 1.00 98.33 ? 73 ARG D CB 1 +ATOM 7633 C CG . ARG D 1 74 ? 22.195 61.064 61.996 1.00 92.78 ? 73 ARG D CG 1 +ATOM 7634 C CD . ARG D 1 74 ? 21.243 59.945 61.677 1.00 79.02 ? 73 ARG D CD 1 +ATOM 7635 N NE . ARG D 1 74 ? 21.181 58.944 62.736 1.00 81.07 ? 73 ARG D NE 1 +ATOM 7636 C CZ . ARG D 1 74 ? 20.607 59.140 63.919 1.00 110.63 ? 73 ARG D CZ 1 +ATOM 7637 N NH1 . ARG D 1 74 ? 20.060 60.321 64.220 1.00 51.27 ? 73 ARG D NH1 1 +ATOM 7638 N NH2 . ARG D 1 74 ? 20.592 58.152 64.808 1.00 78.89 ? 73 ARG D NH2 1 +ATOM 7639 N N . TYR D 1 75 ? 24.041 63.836 63.193 1.00 88.68 ? 74 TYR D N 1 +ATOM 7640 C CA . TYR D 1 75 ? 23.592 64.661 64.308 1.00 106.02 ? 74 TYR D CA 1 +ATOM 7641 C C . TYR D 1 75 ? 22.056 64.713 64.346 1.00 104.61 ? 74 TYR D C 1 +ATOM 7642 O O . TYR D 1 75 ? 21.424 65.110 63.362 1.00 113.63 ? 74 TYR D O 1 +ATOM 7643 C CB . TYR D 1 75 ? 24.197 66.075 64.209 1.00 83.04 ? 74 TYR D CB 1 +ATOM 7644 C CG . TYR D 1 75 ? 25.578 66.211 64.837 1.00 92.95 ? 74 TYR D CG 1 +ATOM 7645 C CD1 . TYR D 1 75 ? 26.716 65.735 64.193 1.00 92.36 ? 74 TYR D CD1 1 +ATOM 7646 C CD2 . TYR D 1 75 ? 25.739 66.817 66.076 1.00 110.14 ? 74 TYR D CD2 1 +ATOM 7647 C CE1 . TYR D 1 75 ? 27.977 65.855 64.774 1.00 101.51 ? 74 TYR D CE1 1 +ATOM 7648 C CE2 . TYR D 1 75 ? 26.990 66.942 66.664 1.00 94.04 ? 74 TYR D CE2 1 +ATOM 7649 C CZ . TYR D 1 75 ? 28.106 66.459 66.013 1.00 110.13 ? 74 TYR D CZ 1 +ATOM 7650 O OH . TYR D 1 75 ? 29.346 66.590 66.612 1.00 107.12 ? 74 TYR D OH 1 +ATOM 7651 N N . PRO D 1 76 ? 21.449 64.295 65.476 1.00 95.63 ? 75 PRO D N 1 +ATOM 7652 C CA . PRO D 1 76 ? 20.001 64.439 65.646 1.00 86.18 ? 75 PRO D CA 1 +ATOM 7653 C C . PRO D 1 76 ? 19.632 65.918 65.634 1.00 126.81 ? 75 PRO D C 1 +ATOM 7654 O O . PRO D 1 76 ? 20.475 66.765 65.935 1.00 113.42 ? 75 PRO D O 1 +ATOM 7655 C CB . PRO D 1 76 ? 19.745 63.856 67.041 1.00 92.73 ? 75 PRO D CB 1 +ATOM 7656 C CG . PRO D 1 76 ? 20.931 63.064 67.371 1.00 95.95 ? 75 PRO D CG 1 +ATOM 7657 C CD . PRO D 1 76 ? 22.077 63.720 66.675 1.00 101.25 ? 75 PRO D CD 1 +ATOM 7658 N N . ASP D 1 77 ? 18.380 66.212 65.300 1.00 121.61 ? 76 ASP D N 1 +ATOM 7659 C CA . ASP D 1 77 ? 17.914 67.580 65.095 1.00 126.81 ? 76 ASP D CA 1 +ATOM 7660 C C . ASP D 1 77 ? 18.130 68.498 66.294 1.00 133.76 ? 76 ASP D C 1 +ATOM 7661 O O . ASP D 1 77 ? 18.461 69.675 66.137 1.00 100.10 ? 76 ASP D O 1 +ATOM 7662 C CB . ASP D 1 77 ? 16.436 67.562 64.706 1.00 155.76 ? 76 ASP D CB 1 +ATOM 7663 C CG . ASP D 1 77 ? 16.188 66.808 63.414 1.00 171.00 ? 76 ASP D CG 1 +ATOM 7664 O OD1 . ASP D 1 77 ? 16.740 67.225 62.371 1.00 155.38 ? 76 ASP D OD1 1 +ATOM 7665 O OD2 . ASP D 1 77 ? 15.448 65.801 63.441 1.00 179.75 ? 76 ASP D OD2 1 +ATOM 7666 N N . HIS D 1 78 ? 17.952 67.955 67.491 1.00 127.71 ? 77 HIS D N 1 +ATOM 7667 C CA . HIS D 1 78 ? 18.090 68.749 68.704 1.00 86.90 ? 77 HIS D CA 1 +ATOM 7668 C C . HIS D 1 78 ? 19.549 69.050 69.052 1.00 123.52 ? 77 HIS D C 1 +ATOM 7669 O O . HIS D 1 78 ? 19.823 69.814 69.981 1.00 129.92 ? 77 HIS D O 1 +ATOM 7670 C CB . HIS D 1 78 ? 17.409 68.049 69.876 1.00 89.07 ? 77 HIS D CB 1 +ATOM 7671 C CG . HIS D 1 78 ? 18.129 66.830 70.357 1.00 108.00 ? 77 HIS D CG 1 +ATOM 7672 N ND1 . HIS D 1 78 ? 17.894 65.574 69.840 1.00 104.88 ? 77 HIS D ND1 1 +ATOM 7673 C CD2 . HIS D 1 78 ? 19.068 66.672 71.319 1.00 103.05 ? 77 HIS D CD2 1 +ATOM 7674 C CE1 . HIS D 1 78 ? 18.663 64.695 70.460 1.00 118.97 ? 77 HIS D CE1 1 +ATOM 7675 N NE2 . HIS D 1 78 ? 19.383 65.336 71.362 1.00 130.00 ? 77 HIS D NE2 1 +ATOM 7676 N N . MET D 1 79 ? 20.474 68.446 68.306 1.00 125.00 ? 78 MET D N 1 +ATOM 7677 C CA . MET D 1 79 ? 21.910 68.616 68.541 1.00 104.30 ? 78 MET D CA 1 +ATOM 7678 C C . MET D 1 79 ? 22.598 69.462 67.463 1.00 118.61 ? 78 MET D C 1 +ATOM 7679 O O . MET D 1 79 ? 23.618 70.106 67.727 1.00 99.62 ? 78 MET D O 1 +ATOM 7680 C CB . MET D 1 79 ? 22.604 67.252 68.670 1.00 92.43 ? 78 MET D CB 1 +ATOM 7681 C CG . MET D 1 79 ? 22.231 66.479 69.930 1.00 111.56 ? 78 MET D CG 1 +ATOM 7682 S SD . MET D 1 79 ? 23.243 65.015 70.203 1.00 110.91 ? 78 MET D SD 1 +ATOM 7683 C CE . MET D 1 79 ? 24.865 65.734 69.986 1.00 96.20 ? 78 MET D CE 1 +ATOM 7684 N N . LYS D 1 80 ? 22.009 69.482 66.268 1.00 104.71 ? 79 LYS D N 1 +ATOM 7685 C CA . LYS D 1 80 ? 22.615 70.066 65.059 1.00 111.32 ? 79 LYS D CA 1 +ATOM 7686 C C . LYS D 1 80 ? 23.312 71.440 65.168 1.00 110.55 ? 79 LYS D C 1 +ATOM 7687 O O . LYS D 1 80 ? 23.817 71.953 64.170 1.00 140.06 ? 79 LYS D O 1 +ATOM 7688 C CB . LYS D 1 80 ? 21.587 70.100 63.916 1.00 85.59 ? 79 LYS D CB 1 +ATOM 7689 C CG . LYS D 1 80 ? 21.173 68.734 63.385 1.00 113.11 ? 79 LYS D CG 1 +ATOM 7690 C CD . LYS D 1 80 ? 20.468 68.868 62.044 1.00 82.76 ? 79 LYS D CD 1 +ATOM 7691 C CE . LYS D 1 80 ? 19.947 67.529 61.547 1.00 97.58 ? 79 LYS D CE 1 +ATOM 7692 N NZ . LYS D 1 80 ? 21.004 66.686 60.922 1.00 116.51 ? 79 LYS D NZ 1 +ATOM 7693 N N . GLN D 1 81 ? 23.346 72.033 66.358 1.00 125.08 ? 80 GLN D N 1 +ATOM 7694 C CA . GLN D 1 81 ? 24.045 73.302 66.548 1.00 135.84 ? 80 GLN D CA 1 +ATOM 7695 C C . GLN D 1 81 ? 25.360 73.068 67.295 1.00 132.18 ? 80 GLN D C 1 +ATOM 7696 O O . GLN D 1 81 ? 26.037 74.007 67.718 1.00 139.72 ? 80 GLN D O 1 +ATOM 7697 C CB . GLN D 1 81 ? 23.155 74.328 67.265 1.00 121.48 ? 80 GLN D CB 1 +ATOM 7698 C CG . GLN D 1 81 ? 22.809 73.995 68.718 1.00 113.90 ? 80 GLN D CG 1 +ATOM 7699 C CD . GLN D 1 81 ? 21.685 72.973 68.865 1.00 138.48 ? 80 GLN D CD 1 +ATOM 7700 O OE1 . GLN D 1 81 ? 21.048 72.581 67.885 1.00 155.57 ? 80 GLN D OE1 1 +ATOM 7701 N NE2 . GLN D 1 81 ? 21.438 72.540 70.100 1.00 120.16 ? 80 GLN D NE2 1 +ATOM 7702 N N . HIS D 1 82 ? 25.708 71.794 67.447 1.00 123.80 ? 81 HIS D N 1 +ATOM 7703 C CA . HIS D 1 82 ? 26.988 71.387 68.016 1.00 126.11 ? 81 HIS D CA 1 +ATOM 7704 C C . HIS D 1 82 ? 27.812 70.574 67.005 1.00 125.84 ? 81 HIS D C 1 +ATOM 7705 O O . HIS D 1 82 ? 28.715 69.821 67.382 1.00 122.09 ? 81 HIS D O 1 +ATOM 7706 C CB . HIS D 1 82 ? 26.767 70.555 69.277 1.00 124.13 ? 81 HIS D CB 1 +ATOM 7707 C CG . HIS D 1 82 ? 25.994 71.259 70.350 1.00 124.34 ? 81 HIS D CG 1 +ATOM 7708 N ND1 . HIS D 1 82 ? 26.484 72.353 71.032 1.00 124.36 ? 81 HIS D ND1 1 +ATOM 7709 C CD2 . HIS D 1 82 ? 24.773 71.006 70.874 1.00 87.59 ? 81 HIS D CD2 1 +ATOM 7710 C CE1 . HIS D 1 82 ? 25.596 72.745 71.927 1.00 131.24 ? 81 HIS D CE1 1 +ATOM 7711 N NE2 . HIS D 1 82 ? 24.549 71.941 71.855 1.00 135.94 ? 81 HIS D NE2 1 +ATOM 7712 N N . ASP D 1 83 ? 27.480 70.726 65.726 1.00 112.55 ? 82 ASP D N 1 +ATOM 7713 C CA . ASP D 1 83 ? 28.201 70.075 64.635 1.00 111.28 ? 82 ASP D CA 1 +ATOM 7714 C C . ASP D 1 83 ? 29.273 71.023 64.113 1.00 107.91 ? 82 ASP D C 1 +ATOM 7715 O O . ASP D 1 83 ? 29.026 71.803 63.190 1.00 121.17 ? 82 ASP D O 1 +ATOM 7716 C CB . ASP D 1 83 ? 27.232 69.701 63.505 1.00 145.76 ? 82 ASP D CB 1 +ATOM 7717 C CG . ASP D 1 83 ? 27.855 68.775 62.463 1.00 133.63 ? 82 ASP D CG 1 +ATOM 7718 O OD1 . ASP D 1 83 ? 29.018 68.986 62.068 1.00 114.55 ? 82 ASP D OD1 1 +ATOM 7719 O OD2 . ASP D 1 83 ? 27.171 67.828 62.027 1.00 149.02 ? 82 ASP D OD2 1 +ATOM 7720 N N . PHE D 1 84 ? 30.458 70.943 64.717 1.00 110.39 ? 83 PHE D N 1 +ATOM 7721 C CA . PHE D 1 84 ? 31.612 71.757 64.341 1.00 91.05 ? 83 PHE D CA 1 +ATOM 7722 C C . PHE D 1 84 ? 32.153 71.350 62.981 1.00 99.96 ? 83 PHE D C 1 +ATOM 7723 O O . PHE D 1 84 ? 32.420 72.191 62.121 1.00 130.93 ? 83 PHE D O 1 +ATOM 7724 C CB . PHE D 1 84 ? 32.729 71.606 65.380 1.00 92.76 ? 83 PHE D CB 1 +ATOM 7725 C CG . PHE D 1 84 ? 34.085 72.019 64.870 1.00 111.58 ? 83 PHE D CG 1 +ATOM 7726 C CD1 . PHE D 1 84 ? 34.364 73.356 64.604 1.00 131.29 ? 83 PHE D CD1 1 +ATOM 7727 C CD2 . PHE D 1 84 ? 35.075 71.075 64.637 1.00 103.03 ? 83 PHE D CD2 1 +ATOM 7728 C CE1 . PHE D 1 84 ? 35.611 73.746 64.118 1.00 119.76 ? 83 PHE D CE1 1 +ATOM 7729 C CE2 . PHE D 1 84 ? 36.320 71.458 64.151 1.00 130.98 ? 83 PHE D CE2 1 +ATOM 7730 C CZ . PHE D 1 84 ? 36.588 72.795 63.893 1.00 132.58 ? 83 PHE D CZ 1 +ATOM 7731 N N . PHE D 1 85 ? 32.319 70.043 62.817 1.00 97.27 ? 84 PHE D N 1 +ATOM 7732 C CA . PHE D 1 85 ? 32.841 69.442 61.600 1.00 94.40 ? 84 PHE D CA 1 +ATOM 7733 C C . PHE D 1 85 ? 32.204 69.974 60.327 1.00 105.27 ? 84 PHE D C 1 +ATOM 7734 O O . PHE D 1 85 ? 32.893 70.521 59.464 1.00 136.60 ? 84 PHE D O 1 +ATOM 7735 C CB . PHE D 1 85 ? 32.668 67.934 61.684 1.00 103.51 ? 84 PHE D CB 1 +ATOM 7736 C CG . PHE D 1 85 ? 33.341 67.329 62.871 1.00 102.81 ? 84 PHE D CG 1 +ATOM 7737 C CD1 . PHE D 1 85 ? 34.652 67.644 63.163 1.00 101.89 ? 84 PHE D CD1 1 +ATOM 7738 C CD2 . PHE D 1 85 ? 32.660 66.474 63.711 1.00 103.30 ? 84 PHE D CD2 1 +ATOM 7739 C CE1 . PHE D 1 85 ? 35.274 67.100 64.251 1.00 107.61 ? 84 PHE D CE1 1 +ATOM 7740 C CE2 . PHE D 1 85 ? 33.281 65.924 64.807 1.00 83.00 ? 84 PHE D CE2 1 +ATOM 7741 C CZ . PHE D 1 85 ? 34.589 66.238 65.078 1.00 100.56 ? 84 PHE D CZ 1 +ATOM 7742 N N . LYS D 1 86 ? 30.891 69.824 60.210 1.00 107.77 ? 85 LYS D N 1 +ATOM 7743 C CA . LYS D 1 86 ? 30.200 70.298 59.019 1.00 119.30 ? 85 LYS D CA 1 +ATOM 7744 C C . LYS D 1 86 ? 30.248 71.822 58.908 1.00 123.48 ? 85 LYS D C 1 +ATOM 7745 O O . LYS D 1 86 ? 30.461 72.363 57.826 1.00 114.54 ? 85 LYS D O 1 +ATOM 7746 C CB . LYS D 1 86 ? 28.759 69.793 58.990 1.00 101.67 ? 85 LYS D CB 1 +ATOM 7747 C CG . LYS D 1 86 ? 28.643 68.281 58.970 1.00 101.48 ? 85 LYS D CG 1 +ATOM 7748 C CD . LYS D 1 86 ? 27.216 67.862 58.664 1.00 96.20 ? 85 LYS D CD 1 +ATOM 7749 C CE . LYS D 1 86 ? 27.004 66.365 58.836 1.00 85.26 ? 85 LYS D CE 1 +ATOM 7750 N NZ . LYS D 1 86 ? 27.262 65.912 60.233 1.00 126.70 ? 85 LYS D NZ 1 +ATOM 7751 N N . SER D 1 87 ? 30.079 72.508 60.034 1.00 120.08 ? 86 SER D N 1 +ATOM 7752 C CA . SER D 1 87 ? 30.006 73.969 60.040 1.00 118.71 ? 86 SER D CA 1 +ATOM 7753 C C . SER D 1 87 ? 31.271 74.617 59.484 1.00 117.81 ? 86 SER D C 1 +ATOM 7754 O O . SER D 1 87 ? 31.249 75.765 59.036 1.00 118.28 ? 86 SER D O 1 +ATOM 7755 C CB . SER D 1 87 ? 29.748 74.483 61.457 1.00 130.68 ? 86 SER D CB 1 +ATOM 7756 O OG . SER D 1 87 ? 30.895 74.330 62.275 1.00 115.86 ? 86 SER D OG 1 +ATOM 7757 N N . ALA D 1 88 ? 32.367 73.865 59.518 1.00 121.14 ? 87 ALA D N 1 +ATOM 7758 C CA . ALA D 1 88 ? 33.673 74.357 59.095 1.00 106.51 ? 87 ALA D CA 1 +ATOM 7759 C C . ALA D 1 88 ? 33.817 74.335 57.577 1.00 106.03 ? 87 ALA D C 1 +ATOM 7760 O O . ALA D 1 88 ? 34.726 74.949 57.016 1.00 124.93 ? 87 ALA D O 1 +ATOM 7761 C CB . ALA D 1 88 ? 34.778 73.533 59.748 1.00 105.32 ? 87 ALA D CB 1 +ATOM 7762 N N . MET D 1 89 ? 32.902 73.630 56.923 1.00 101.70 ? 88 MET D N 1 +ATOM 7763 C CA . MET D 1 89 ? 32.936 73.449 55.480 1.00 109.94 ? 88 MET D CA 1 +ATOM 7764 C C . MET D 1 89 ? 32.368 74.681 54.763 1.00 98.30 ? 88 MET D C 1 +ATOM 7765 O O . MET D 1 89 ? 31.666 75.484 55.380 1.00 109.28 ? 88 MET D O 1 +ATOM 7766 C CB . MET D 1 89 ? 32.159 72.178 55.119 1.00 98.74 ? 88 MET D CB 1 +ATOM 7767 C CG . MET D 1 89 ? 32.728 70.916 55.748 1.00 116.92 ? 88 MET D CG 1 +ATOM 7768 S SD . MET D 1 89 ? 34.336 70.451 55.084 1.00 103.93 ? 88 MET D SD 1 +ATOM 7769 C CE . MET D 1 89 ? 34.866 69.269 56.323 1.00 128.50 ? 88 MET D CE 1 +ATOM 7770 N N . PRO D 1 90 ? 32.670 74.840 53.459 1.00 99.24 ? 89 PRO D N 1 +ATOM 7771 C CA . PRO D 1 90 ? 33.429 73.916 52.604 1.00 129.21 ? 89 PRO D CA 1 +ATOM 7772 C C . PRO D 1 90 ? 34.943 74.094 52.722 1.00 119.39 ? 89 PRO D C 1 +ATOM 7773 O O . PRO D 1 90 ? 35.705 73.272 52.204 1.00 119.54 ? 89 PRO D O 1 +ATOM 7774 C CB . PRO D 1 90 ? 32.970 74.306 51.202 1.00 108.63 ? 89 PRO D CB 1 +ATOM 7775 C CG . PRO D 1 90 ? 32.767 75.783 51.308 1.00 109.09 ? 89 PRO D CG 1 +ATOM 7776 C CD . PRO D 1 90 ? 32.259 76.045 52.713 1.00 99.18 ? 89 PRO D CD 1 +ATOM 7777 N N . GLU D 1 91 ? 35.363 75.163 53.392 1.00 101.71 ? 90 GLU D N 1 +ATOM 7778 C CA . GLU D 1 91 ? 36.776 75.497 53.494 1.00 119.90 ? 90 GLU D CA 1 +ATOM 7779 C C . GLU D 1 91 ? 37.513 74.426 54.281 1.00 115.90 ? 90 GLU D C 1 +ATOM 7780 O O . GLU D 1 91 ? 38.632 74.048 53.938 1.00 102.97 ? 90 GLU D O 1 +ATOM 7781 C CB . GLU D 1 91 ? 36.967 76.877 54.127 1.00 150.06 ? 90 GLU D CB 1 +ATOM 7782 C CG . GLU D 1 91 ? 36.232 77.990 53.394 1.00 164.85 ? 90 GLU D CG 1 +ATOM 7783 C CD . GLU D 1 91 ? 36.964 79.318 53.449 1.00 181.75 ? 90 GLU D CD 1 +ATOM 7784 O OE1 . GLU D 1 91 ? 37.927 79.495 52.669 1.00 172.18 ? 90 GLU D OE1 1 +ATOM 7785 O OE2 . GLU D 1 91 ? 36.572 80.181 54.265 1.00 187.50 ? 90 GLU D OE2 1 +ATOM 7786 N N . GLY D 1 92 ? 36.874 73.931 55.332 1.00 109.90 ? 91 GLY D N 1 +ATOM 7787 C CA . GLY D 1 92 ? 37.393 72.778 56.037 1.00 106.89 ? 91 GLY D CA 1 +ATOM 7788 C C . GLY D 1 92 ? 38.135 73.045 57.326 1.00 102.77 ? 91 GLY D C 1 +ATOM 7789 O O . GLY D 1 92 ? 38.185 74.173 57.826 1.00 113.34 ? 91 GLY D O 1 +ATOM 7790 N N . TYR D 1 93 ? 38.714 71.972 57.859 1.00 96.64 ? 92 TYR D N 1 +ATOM 7791 C CA . TYR D 1 93 ? 39.446 72.011 59.117 1.00 104.18 ? 92 TYR D CA 1 +ATOM 7792 C C . TYR D 1 93 ? 40.776 71.243 59.042 1.00 105.75 ? 92 TYR D C 1 +ATOM 7793 O O . TYR D 1 93 ? 41.093 70.638 58.018 1.00 114.22 ? 92 TYR D O 1 +ATOM 7794 C CB . TYR D 1 93 ? 38.564 71.494 60.266 1.00 94.34 ? 92 TYR D CB 1 +ATOM 7795 C CG . TYR D 1 93 ? 38.039 70.064 60.134 1.00 113.95 ? 92 TYR D CG 1 +ATOM 7796 C CD1 . TYR D 1 93 ? 38.841 68.969 60.453 1.00 130.27 ? 92 TYR D CD1 1 +ATOM 7797 C CD2 . TYR D 1 93 ? 36.729 69.811 59.738 1.00 91.29 ? 92 TYR D CD2 1 +ATOM 7798 C CE1 . TYR D 1 93 ? 38.360 67.658 60.353 1.00 121.39 ? 92 TYR D CE1 1 +ATOM 7799 C CE2 . TYR D 1 93 ? 36.239 68.502 59.637 1.00 107.23 ? 92 TYR D CE2 1 +ATOM 7800 C CZ . TYR D 1 93 ? 37.060 67.432 59.947 1.00 109.05 ? 92 TYR D CZ 1 +ATOM 7801 O OH . TYR D 1 93 ? 36.589 66.137 59.852 1.00 106.21 ? 92 TYR D OH 1 +ATOM 7802 N N . VAL D 1 94 ? 41.555 71.297 60.122 1.00 114.13 ? 93 VAL D N 1 +ATOM 7803 C CA . VAL D 1 94 ? 42.809 70.548 60.250 1.00 114.35 ? 93 VAL D CA 1 +ATOM 7804 C C . VAL D 1 94 ? 42.696 69.616 61.456 1.00 113.80 ? 93 VAL D C 1 +ATOM 7805 O O . VAL D 1 94 ? 42.345 70.059 62.549 1.00 112.97 ? 93 VAL D O 1 +ATOM 7806 C CB . VAL D 1 94 ? 44.034 71.480 60.492 1.00 117.50 ? 93 VAL D CB 1 +ATOM 7807 C CG1 . VAL D 1 94 ? 45.339 70.681 60.457 1.00 106.72 ? 93 VAL D CG1 1 +ATOM 7808 C CG2 . VAL D 1 94 ? 44.074 72.638 59.491 1.00 113.82 ? 93 VAL D CG2 1 +ATOM 7809 N N . GLN D 1 95 ? 42.998 68.335 61.275 1.00 82.95 ? 94 GLN D N 1 +ATOM 7810 C CA . GLN D 1 95 ? 42.863 67.377 62.369 1.00 95.72 ? 94 GLN D CA 1 +ATOM 7811 C C . GLN D 1 95 ? 44.226 66.820 62.790 1.00 111.78 ? 94 GLN D C 1 +ATOM 7812 O O . GLN D 1 95 ? 44.844 66.033 62.066 1.00 91.42 ? 94 GLN D O 1 +ATOM 7813 C CB . GLN D 1 95 ? 41.878 66.259 61.990 1.00 89.83 ? 94 GLN D CB 1 +ATOM 7814 C CG . GLN D 1 95 ? 41.679 65.187 63.050 1.00 83.42 ? 94 GLN D CG 1 +ATOM 7815 C CD . GLN D 1 95 ? 40.524 64.234 62.747 1.00 102.55 ? 94 GLN D CD 1 +ATOM 7816 O OE1 . GLN D 1 95 ? 39.380 64.657 62.563 1.00 99.64 ? 94 GLN D OE1 1 +ATOM 7817 N NE2 . GLN D 1 95 ? 40.820 62.938 62.717 1.00 103.86 ? 94 GLN D NE2 1 +ATOM 7818 N N . GLU D 1 96 ? 44.691 67.255 63.959 1.00 107.16 ? 95 GLU D N 1 +ATOM 7819 C CA . GLU D 1 96 ? 45.973 66.817 64.501 1.00 82.93 ? 95 GLU D CA 1 +ATOM 7820 C C . GLU D 1 96 ? 45.751 65.838 65.640 1.00 93.51 ? 95 GLU D C 1 +ATOM 7821 O O . GLU D 1 96 ? 45.000 66.112 66.574 1.00 100.96 ? 95 GLU D O 1 +ATOM 7822 C CB . GLU D 1 96 ? 46.790 68.016 64.996 1.00 108.47 ? 95 GLU D CB 1 +ATOM 7823 C CG . GLU D 1 96 ? 47.516 68.801 63.896 1.00 142.63 ? 95 GLU D CG 1 +ATOM 7824 C CD . GLU D 1 96 ? 48.014 70.176 64.361 1.00 178.77 ? 95 GLU D CD 1 +ATOM 7825 O OE1 . GLU D 1 96 ? 47.217 70.936 64.947 1.00 185.32 ? 95 GLU D OE1 1 +ATOM 7826 O OE2 . GLU D 1 96 ? 49.201 70.503 64.142 1.00 175.67 ? 95 GLU D OE2 1 +ATOM 7827 N N . ARG D 1 97 ? 46.398 64.686 65.558 1.00 65.08 ? 96 ARG D N 1 +ATOM 7828 C CA . ARG D 1 97 ? 46.275 63.705 66.616 1.00 95.79 ? 96 ARG D CA 1 +ATOM 7829 C C . ARG D 1 97 ? 47.625 63.300 67.165 1.00 114.68 ? 96 ARG D C 1 +ATOM 7830 O O . ARG D 1 97 ? 48.669 63.590 66.583 1.00 104.03 ? 96 ARG D O 1 +ATOM 7831 C CB . ARG D 1 97 ? 45.554 62.457 66.118 1.00 76.30 ? 96 ARG D CB 1 +ATOM 7832 C CG . ARG D 1 97 ? 44.055 62.577 66.071 1.00 122.28 ? 96 ARG D CG 1 +ATOM 7833 C CD . ARG D 1 97 ? 43.403 61.239 66.373 1.00 101.24 ? 96 ARG D CD 1 +ATOM 7834 N NE . ARG D 1 97 ? 41.973 61.266 66.087 1.00 117.74 ? 96 ARG D NE 1 +ATOM 7835 C CZ . ARG D 1 97 ? 41.414 60.735 65.005 1.00 108.04 ? 96 ARG D CZ 1 +ATOM 7836 N NH1 . ARG D 1 97 ? 42.162 60.111 64.102 1.00 114.74 ? 96 ARG D NH1 1 +ATOM 7837 N NH2 . ARG D 1 97 ? 40.103 60.818 64.834 1.00 109.34 ? 96 ARG D NH2 1 +ATOM 7838 N N . THR D 1 98 ? 47.581 62.637 68.311 1.00 100.10 ? 97 THR D N 1 +ATOM 7839 C CA . THR D 1 98 ? 48.710 61.890 68.819 1.00 123.97 ? 97 THR D CA 1 +ATOM 7840 C C . THR D 1 98 ? 48.126 60.577 69.329 1.00 104.89 ? 97 THR D C 1 +ATOM 7841 O O . THR D 1 98 ? 47.077 60.562 69.973 1.00 93.51 ? 97 THR D O 1 +ATOM 7842 C CB . THR D 1 98 ? 49.446 62.633 69.952 1.00 126.44 ? 97 THR D CB 1 +ATOM 7843 O OG1 . THR D 1 98 ? 49.828 63.948 69.517 1.00 95.70 ? 97 THR D OG1 1 +ATOM 7844 C CG2 . THR D 1 98 ? 50.683 61.855 70.362 1.00 76.18 ? 97 THR D CG2 1 +ATOM 7845 N N . ILE D 1 99 ? 48.780 59.468 69.020 1.00 83.19 ? 98 ILE D N 1 +ATOM 7846 C CA . ILE D 1 99 ? 48.210 58.173 69.348 1.00 95.97 ? 98 ILE D CA 1 +ATOM 7847 C C . ILE D 1 99 ? 49.207 57.292 70.090 1.00 117.33 ? 98 ILE D C 1 +ATOM 7848 O O . ILE D 1 99 ? 50.071 56.658 69.482 1.00 95.14 ? 98 ILE D O 1 +ATOM 7849 C CB . ILE D 1 99 ? 47.714 57.466 68.077 1.00 91.52 ? 98 ILE D CB 1 +ATOM 7850 C CG1 . ILE D 1 99 ? 46.776 58.400 67.299 1.00 61.79 ? 98 ILE D CG1 1 +ATOM 7851 C CG2 . ILE D 1 99 ? 47.081 56.106 68.419 1.00 62.54 ? 98 ILE D CG2 1 +ATOM 7852 C CD1 . ILE D 1 99 ? 46.425 57.931 65.919 1.00 76.68 ? 98 ILE D CD1 1 +ATOM 7853 N N . PHE D 1 100 ? 49.089 57.262 71.410 1.00 93.42 ? 99 PHE D N 1 +ATOM 7854 C CA . PHE D 1 100 ? 49.954 56.419 72.212 1.00 82.58 ? 99 PHE D CA 1 +ATOM 7855 C C . PHE D 1 100 ? 49.389 55.010 72.265 1.00 79.04 ? 99 PHE D C 1 +ATOM 7856 O O . PHE D 1 100 ? 48.295 54.806 72.771 1.00 93.22 ? 99 PHE D O 1 +ATOM 7857 C CB . PHE D 1 100 ? 50.072 56.976 73.629 1.00 69.95 ? 99 PHE D CB 1 +ATOM 7858 C CG . PHE D 1 100 ? 50.484 58.425 73.683 1.00 105.83 ? 99 PHE D CG 1 +ATOM 7859 C CD1 . PHE D 1 100 ? 51.819 58.790 73.567 1.00 107.59 ? 99 PHE D CD1 1 +ATOM 7860 C CD2 . PHE D 1 100 ? 49.540 59.422 73.865 1.00 111.90 ? 99 PHE D CD2 1 +ATOM 7861 C CE1 . PHE D 1 100 ? 52.204 60.129 73.623 1.00 101.68 ? 99 PHE D CE1 1 +ATOM 7862 C CE2 . PHE D 1 100 ? 49.922 60.763 73.925 1.00 91.06 ? 99 PHE D CE2 1 +ATOM 7863 C CZ . PHE D 1 100 ? 51.253 61.113 73.801 1.00 83.39 ? 99 PHE D CZ 1 +ATOM 7864 N N . PHE D 1 101 ? 50.115 54.040 71.724 1.00 69.07 ? 100 PHE D N 1 +ATOM 7865 C CA . PHE D 1 101 ? 49.784 52.648 71.995 1.00 88.11 ? 100 PHE D CA 1 +ATOM 7866 C C . PHE D 1 101 ? 50.486 52.291 73.299 1.00 98.90 ? 100 PHE D C 1 +ATOM 7867 O O . PHE D 1 101 ? 51.626 52.684 73.537 1.00 92.83 ? 100 PHE D O 1 +ATOM 7868 C CB . PHE D 1 101 ? 50.236 51.715 70.865 1.00 63.55 ? 100 PHE D CB 1 +ATOM 7869 C CG . PHE D 1 101 ? 49.619 52.023 69.520 1.00 96.12 ? 100 PHE D CG 1 +ATOM 7870 C CD1 . PHE D 1 101 ? 49.959 53.179 68.831 1.00 109.94 ? 100 PHE D CD1 1 +ATOM 7871 C CD2 . PHE D 1 101 ? 48.728 51.141 68.928 1.00 108.58 ? 100 PHE D CD2 1 +ATOM 7872 C CE1 . PHE D 1 101 ? 49.410 53.457 67.602 1.00 64.87 ? 100 PHE D CE1 1 +ATOM 7873 C CE2 . PHE D 1 101 ? 48.179 51.419 67.695 1.00 97.33 ? 100 PHE D CE2 1 +ATOM 7874 C CZ . PHE D 1 101 ? 48.522 52.575 67.035 1.00 104.58 ? 100 PHE D CZ 1 +ATOM 7875 N N . LYS D 1 102 ? 49.801 51.567 74.165 1.00 85.66 ? 101 LYS D N 1 +ATOM 7876 C CA . LYS D 1 102 ? 50.365 51.305 75.476 1.00 122.80 ? 101 LYS D CA 1 +ATOM 7877 C C . LYS D 1 102 ? 51.472 50.268 75.363 1.00 131.73 ? 101 LYS D C 1 +ATOM 7878 O O . LYS D 1 102 ? 51.303 49.263 74.666 1.00 90.71 ? 101 LYS D O 1 +ATOM 7879 C CB . LYS D 1 102 ? 49.279 50.823 76.431 1.00 98.41 ? 101 LYS D CB 1 +ATOM 7880 C CG . LYS D 1 102 ? 49.734 50.649 77.864 1.00 114.08 ? 101 LYS D CG 1 +ATOM 7881 C CD . LYS D 1 102 ? 48.742 49.798 78.632 1.00 138.68 ? 101 LYS D CD 1 +ATOM 7882 C CE . LYS D 1 102 ? 48.824 50.042 80.126 1.00 129.50 ? 101 LYS D CE 1 +ATOM 7883 N NZ . LYS D 1 102 ? 48.763 48.764 80.876 1.00 138.70 ? 101 LYS D NZ 1 +ATOM 7884 N N . ASP D 1 103 ? 52.588 50.526 76.052 1.00 108.82 ? 102 ASP D N 1 +ATOM 7885 C CA . ASP D 1 103 ? 53.771 49.659 76.048 1.00 117.48 ? 102 ASP D CA 1 +ATOM 7886 C C . ASP D 1 103 ? 54.401 49.603 74.673 1.00 113.53 ? 102 ASP D C 1 +ATOM 7887 O O . ASP D 1 103 ? 54.946 48.570 74.282 1.00 107.86 ? 102 ASP D O 1 +ATOM 7888 C CB . ASP D 1 103 ? 53.441 48.226 76.488 1.00 133.36 ? 102 ASP D CB 1 +ATOM 7889 C CG . ASP D 1 103 ? 53.027 48.137 77.934 1.00 142.96 ? 102 ASP D CG 1 +ATOM 7890 O OD1 . ASP D 1 103 ? 53.310 49.091 78.690 1.00 135.25 ? 102 ASP D OD1 1 +ATOM 7891 O OD2 . ASP D 1 103 ? 52.428 47.104 78.310 1.00 137.98 ? 102 ASP D OD2 1 +ATOM 7892 N N . ASP D 1 104 ? 54.317 50.702 73.936 1.00 97.72 ? 103 ASP D N 1 +ATOM 7893 C CA . ASP D 1 104 ? 54.756 50.687 72.555 1.00 85.36 ? 103 ASP D CA 1 +ATOM 7894 C C . ASP D 1 104 ? 54.796 52.093 71.970 1.00 97.77 ? 103 ASP D C 1 +ATOM 7895 O O . ASP D 1 104 ? 54.607 53.079 72.685 1.00 75.80 ? 103 ASP D O 1 +ATOM 7896 C CB . ASP D 1 104 ? 53.855 49.768 71.725 1.00 79.40 ? 103 ASP D CB 1 +ATOM 7897 C CG . ASP D 1 104 ? 54.325 49.628 70.304 1.00 131.46 ? 103 ASP D CG 1 +ATOM 7898 O OD1 . ASP D 1 104 ? 55.367 50.245 69.988 1.00 85.99 ? 103 ASP D OD1 1 +ATOM 7899 O OD2 . ASP D 1 104 ? 53.690 48.922 69.518 1.00 218.05 ? 103 ASP D OD2 1 +ATOM 7900 N N . GLY D 1 105 ? 55.045 52.176 70.665 1.00 94.71 ? 104 GLY D N 1 +ATOM 7901 C CA . GLY D 1 105 ? 55.296 53.430 69.991 1.00 64.17 ? 104 GLY D CA 1 +ATOM 7902 C C . GLY D 1 105 ? 54.079 54.312 69.783 1.00 102.81 ? 104 GLY D C 1 +ATOM 7903 O O . GLY D 1 105 ? 52.996 54.020 70.286 1.00 96.16 ? 104 GLY D O 1 +ATOM 7904 N N . ASN D 1 106 ? 54.251 55.393 69.028 1.00 86.50 ? 105 ASN D N 1 +ATOM 7905 C CA . ASN D 1 106 ? 53.160 56.332 68.801 1.00 94.41 ? 105 ASN D CA 1 +ATOM 7906 C C . ASN D 1 106 ? 53.097 56.899 67.384 1.00 115.34 ? 105 ASN D C 1 +ATOM 7907 O O . ASN D 1 106 ? 54.128 57.060 66.727 1.00 111.75 ? 105 ASN D O 1 +ATOM 7908 C CB . ASN D 1 106 ? 53.254 57.491 69.793 1.00 103.26 ? 105 ASN D CB 1 +ATOM 7909 C CG . ASN D 1 106 ? 54.574 58.241 69.692 1.00 103.36 ? 105 ASN D CG 1 +ATOM 7910 O OD1 . ASN D 1 106 ? 54.768 59.099 68.819 1.00 91.76 ? 105 ASN D OD1 1 +ATOM 7911 N ND2 . ASN D 1 106 ? 55.490 57.921 70.594 1.00 85.53 ? 105 ASN D ND2 1 +ATOM 7912 N N . TYR D 1 107 ? 51.883 57.210 66.930 1.00 91.22 ? 106 TYR D N 1 +ATOM 7913 C CA . TYR D 1 107 ? 51.687 57.983 65.705 1.00 88.59 ? 106 TYR D CA 1 +ATOM 7914 C C . TYR D 1 107 ? 51.481 59.467 66.017 1.00 98.38 ? 106 TYR D C 1 +ATOM 7915 O O . TYR D 1 107 ? 50.850 59.826 67.011 1.00 84.19 ? 106 TYR D O 1 +ATOM 7916 C CB . TYR D 1 107 ? 50.461 57.495 64.934 1.00 84.27 ? 106 TYR D CB 1 +ATOM 7917 C CG . TYR D 1 107 ? 50.481 56.055 64.463 1.00 88.01 ? 106 TYR D CG 1 +ATOM 7918 C CD1 . TYR D 1 107 ? 51.669 55.383 64.204 1.00 85.55 ? 106 TYR D CD1 1 +ATOM 7919 C CD2 . TYR D 1 107 ? 49.290 55.376 64.253 1.00 96.84 ? 106 TYR D CD2 1 +ATOM 7920 C CE1 . TYR D 1 107 ? 51.660 54.057 63.758 1.00 69.75 ? 106 TYR D CE1 1 +ATOM 7921 C CE2 . TYR D 1 107 ? 49.271 54.068 63.815 1.00 59.44 ? 106 TYR D CE2 1 +ATOM 7922 C CZ . TYR D 1 107 ? 50.450 53.409 63.570 1.00 91.84 ? 106 TYR D CZ 1 +ATOM 7923 O OH . TYR D 1 107 ? 50.394 52.101 63.136 1.00 90.11 ? 106 TYR D OH 1 +ATOM 7924 N N . LYS D 1 108 ? 52.007 60.334 65.163 1.00 87.11 ? 107 LYS D N 1 +ATOM 7925 C CA . LYS D 1 108 ? 51.639 61.739 65.224 1.00 89.38 ? 107 LYS D CA 1 +ATOM 7926 C C . LYS D 1 108 ? 51.230 62.174 63.830 1.00 107.11 ? 107 LYS D C 1 +ATOM 7927 O O . LYS D 1 108 ? 52.024 62.116 62.889 1.00 111.81 ? 107 LYS D O 1 +ATOM 7928 C CB . LYS D 1 108 ? 52.773 62.596 65.782 1.00 94.78 ? 107 LYS D CB 1 +ATOM 7929 C CG . LYS D 1 108 ? 52.954 62.443 67.284 1.00 109.71 ? 107 LYS D CG 1 +ATOM 7930 C CD . LYS D 1 108 ? 54.242 63.096 67.771 1.00 108.02 ? 107 LYS D CD 1 +ATOM 7931 C CE . LYS D 1 108 ? 54.240 63.300 69.287 1.00 118.41 ? 107 LYS D CE 1 +ATOM 7932 N NZ . LYS D 1 108 ? 53.150 64.225 69.738 1.00 117.25 ? 107 LYS D NZ 1 +ATOM 7933 N N . THR D 1 109 ? 49.971 62.584 63.707 1.00 106.78 ? 108 THR D N 1 +ATOM 7934 C CA . THR D 1 109 ? 49.361 62.831 62.410 1.00 96.99 ? 108 THR D CA 1 +ATOM 7935 C C . THR D 1 109 ? 48.893 64.271 62.270 1.00 96.15 ? 108 THR D C 1 +ATOM 7936 O O . THR D 1 109 ? 48.682 64.969 63.258 1.00 73.72 ? 108 THR D O 1 +ATOM 7937 C CB . THR D 1 109 ? 48.157 61.890 62.160 1.00 92.36 ? 108 THR D CB 1 +ATOM 7938 O OG1 . THR D 1 109 ? 47.069 62.251 63.021 1.00 90.51 ? 108 THR D OG1 1 +ATOM 7939 C CG2 . THR D 1 109 ? 48.543 60.435 62.403 1.00 101.98 ? 108 THR D CG2 1 +ATOM 7940 N N . ARG D 1 110 ? 48.764 64.710 61.023 1.00 89.44 ? 109 ARG D N 1 +ATOM 7941 C CA . ARG D 1 110 ? 48.155 65.991 60.702 1.00 90.19 ? 109 ARG D CA 1 +ATOM 7942 C C . ARG D 1 110 ? 47.462 65.887 59.352 1.00 97.63 ? 109 ARG D C 1 +ATOM 7943 O O . ARG D 1 110 ? 48.116 65.731 58.319 1.00 89.35 ? 109 ARG D O 1 +ATOM 7944 C CB . ARG D 1 110 ? 49.178 67.131 60.677 1.00 94.00 ? 109 ARG D CB 1 +ATOM 7945 C CG . ARG D 1 110 ? 48.571 68.447 60.200 1.00 114.22 ? 109 ARG D CG 1 +ATOM 7946 C CD . ARG D 1 110 ? 49.607 69.513 59.894 1.00 88.49 ? 109 ARG D CD 1 +ATOM 7947 N NE . ARG D 1 110 ? 48.983 70.813 59.640 1.00 109.68 ? 109 ARG D NE 1 +ATOM 7948 C CZ . ARG D 1 110 ? 48.644 71.272 58.436 1.00 124.19 ? 109 ARG D CZ 1 +ATOM 7949 N NH1 . ARG D 1 110 ? 48.867 70.544 57.347 1.00 128.93 ? 109 ARG D NH1 1 +ATOM 7950 N NH2 . ARG D 1 110 ? 48.081 72.468 58.320 1.00 104.76 ? 109 ARG D NH2 1 +ATOM 7951 N N . ALA D 1 111 ? 46.134 65.972 59.387 1.00 108.62 ? 110 ALA D N 1 +ATOM 7952 C CA . ALA D 1 111 ? 45.290 65.909 58.200 1.00 86.61 ? 110 ALA D CA 1 +ATOM 7953 C C . ALA D 1 111 ? 44.619 67.251 57.908 1.00 103.77 ? 110 ALA D C 1 +ATOM 7954 O O . ALA D 1 111 ? 44.337 68.028 58.821 1.00 95.62 ? 110 ALA D O 1 +ATOM 7955 C CB . ALA D 1 111 ? 44.234 64.827 58.368 1.00 98.64 ? 110 ALA D CB 1 +ATOM 7956 N N . GLU D 1 112 ? 44.390 67.524 56.628 1.00 82.72 ? 111 GLU D N 1 +ATOM 7957 C CA . GLU D 1 112 ? 43.504 68.607 56.220 1.00 105.39 ? 111 GLU D CA 1 +ATOM 7958 C C . GLU D 1 112 ? 42.253 67.978 55.602 1.00 120.68 ? 111 GLU D C 1 +ATOM 7959 O O . GLU D 1 112 ? 42.344 67.242 54.614 1.00 118.24 ? 111 GLU D O 1 +ATOM 7960 C CB . GLU D 1 112 ? 44.194 69.550 55.220 1.00 122.24 ? 111 GLU D CB 1 +ATOM 7961 C CG . GLU D 1 112 ? 45.349 70.376 55.805 1.00 161.70 ? 111 GLU D CG 1 +ATOM 7962 C CD . GLU D 1 112 ? 46.060 71.291 54.789 1.00 163.69 ? 111 GLU D CD 1 +ATOM 7963 O OE1 . GLU D 1 112 ? 45.771 71.234 53.570 1.00 131.57 ? 111 GLU D OE1 1 +ATOM 7964 O OE2 . GLU D 1 112 ? 46.924 72.080 55.231 1.00 160.08 ? 111 GLU D OE2 1 +ATOM 7965 N N . VAL D 1 113 ? 41.094 68.234 56.203 1.00 112.46 ? 112 VAL D N 1 +ATOM 7966 C CA . VAL D 1 113 ? 39.835 67.752 55.643 1.00 101.34 ? 112 VAL D CA 1 +ATOM 7967 C C . VAL D 1 113 ? 39.051 68.910 55.048 1.00 102.75 ? 112 VAL D C 1 +ATOM 7968 O O . VAL D 1 113 ? 38.686 69.846 55.756 1.00 90.52 ? 112 VAL D O 1 +ATOM 7969 C CB . VAL D 1 113 ? 38.955 67.039 56.682 1.00 72.17 ? 112 VAL D CB 1 +ATOM 7970 C CG1 . VAL D 1 113 ? 37.807 66.349 55.983 1.00 109.63 ? 112 VAL D CG1 1 +ATOM 7971 C CG2 . VAL D 1 113 ? 39.762 66.023 57.450 1.00 105.65 ? 112 VAL D CG2 1 +ATOM 7972 N N . LYS D 1 114 ? 38.800 68.841 53.744 1.00 82.51 ? 113 LYS D N 1 +ATOM 7973 C CA . LYS D 1 114 ? 38.107 69.914 53.035 1.00 100.17 ? 113 LYS D CA 1 +ATOM 7974 C C . LYS D 1 114 ? 37.479 69.448 51.718 1.00 112.45 ? 113 LYS D C 1 +ATOM 7975 O O . LYS D 1 114 ? 37.657 68.305 51.290 1.00 93.91 ? 113 LYS D O 1 +ATOM 7976 C CB . LYS D 1 114 ? 39.045 71.112 52.792 1.00 127.54 ? 113 LYS D CB 1 +ATOM 7977 C CG . LYS D 1 114 ? 40.268 70.834 51.894 1.00 128.11 ? 113 LYS D CG 1 +ATOM 7978 C CD . LYS D 1 114 ? 41.154 72.080 51.698 1.00 112.36 ? 113 LYS D CD 1 +ATOM 7979 C CE . LYS D 1 114 ? 42.310 71.820 50.724 1.00 133.79 ? 113 LYS D CE 1 +ATOM 7980 N NZ . LYS D 1 114 ? 43.365 70.933 51.291 1.00 114.89 ? 113 LYS D NZ 1 +ATOM 7981 N N . PHE D 1 115 ? 36.740 70.347 51.079 1.00 92.63 ? 114 PHE D N 1 +ATOM 7982 C CA . PHE D 1 115 ? 36.049 70.020 49.842 1.00 101.89 ? 114 PHE D CA 1 +ATOM 7983 C C . PHE D 1 115 ? 36.869 70.443 48.643 1.00 100.33 ? 114 PHE D C 1 +ATOM 7984 O O . PHE D 1 115 ? 37.371 71.561 48.595 1.00 109.84 ? 114 PHE D O 1 +ATOM 7985 C CB . PHE D 1 115 ? 34.687 70.716 49.785 1.00 128.14 ? 114 PHE D CB 1 +ATOM 7986 C CG . PHE D 1 115 ? 33.537 69.845 50.213 1.00 133.19 ? 114 PHE D CG 1 +ATOM 7987 C CD1 . PHE D 1 115 ? 32.874 69.042 49.292 1.00 119.79 ? 114 PHE D CD1 1 +ATOM 7988 C CD2 . PHE D 1 115 ? 33.117 69.832 51.532 1.00 108.65 ? 114 PHE D CD2 1 +ATOM 7989 C CE1 . PHE D 1 115 ? 31.817 68.242 49.681 1.00 100.84 ? 114 PHE D CE1 1 +ATOM 7990 C CE2 . PHE D 1 115 ? 32.062 69.039 51.926 1.00 95.16 ? 114 PHE D CE2 1 +ATOM 7991 C CZ . PHE D 1 115 ? 31.409 68.241 51.000 1.00 97.06 ? 114 PHE D CZ 1 +ATOM 7992 N N . GLU D 1 116 ? 37.006 69.555 47.671 1.00 93.17 ? 115 GLU D N 1 +ATOM 7993 C CA . GLU D 1 116 ? 37.651 69.933 46.423 1.00 100.68 ? 115 GLU D CA 1 +ATOM 7994 C C . GLU D 1 116 ? 36.671 69.732 45.276 1.00 95.82 ? 115 GLU D C 1 +ATOM 7995 O O . GLU D 1 116 ? 36.709 68.727 44.558 1.00 89.46 ? 115 GLU D O 1 +ATOM 7996 C CB . GLU D 1 116 ? 38.947 69.156 46.211 1.00 105.74 ? 115 GLU D CB 1 +ATOM 7997 C CG . GLU D 1 116 ? 40.027 69.496 47.216 1.00 116.11 ? 115 GLU D CG 1 +ATOM 7998 C CD . GLU D 1 116 ? 41.375 68.910 46.850 1.00 156.51 ? 115 GLU D CD 1 +ATOM 7999 O OE1 . GLU D 1 116 ? 41.455 68.190 45.828 1.00 152.98 ? 115 GLU D OE1 1 +ATOM 8000 O OE2 . GLU D 1 116 ? 42.352 69.174 47.587 1.00 139.47 ? 115 GLU D OE2 1 +ATOM 8001 N N . GLY D 1 117 ? 35.782 70.708 45.128 1.00 100.93 ? 116 GLY D N 1 +ATOM 8002 C CA . GLY D 1 117 ? 34.661 70.595 44.221 1.00 95.80 ? 116 GLY D CA 1 +ATOM 8003 C C . GLY D 1 117 ? 33.539 69.829 44.889 1.00 117.99 ? 116 GLY D C 1 +ATOM 8004 O O . GLY D 1 117 ? 33.102 70.173 45.993 1.00 89.33 ? 116 GLY D O 1 +ATOM 8005 N N . ASP D 1 118 ? 33.081 68.774 44.223 1.00 142.10 ? 117 ASP D N 1 +ATOM 8006 C CA . ASP D 1 118 ? 32.011 67.948 44.762 1.00 135.34 ? 117 ASP D CA 1 +ATOM 8007 C C . ASP D 1 118 ? 32.544 66.867 45.702 1.00 120.40 ? 117 ASP D C 1 +ATOM 8008 O O . ASP D 1 118 ? 31.770 66.100 46.266 1.00 121.95 ? 117 ASP D O 1 +ATOM 8009 C CB . ASP D 1 118 ? 31.151 67.327 43.640 1.00 134.68 ? 117 ASP D CB 1 +ATOM 8010 C CG . ASP D 1 118 ? 31.877 66.217 42.867 1.00 160.82 ? 117 ASP D CG 1 +ATOM 8011 O OD1 . ASP D 1 118 ? 33.029 66.444 42.437 1.00 145.20 ? 117 ASP D OD1 1 +ATOM 8012 O OD2 . ASP D 1 118 ? 31.290 65.121 42.683 1.00 142.89 ? 117 ASP D OD2 1 +ATOM 8013 N N . THR D 1 119 ? 33.858 66.808 45.890 1.00 117.91 ? 118 THR D N 1 +ATOM 8014 C CA . THR D 1 119 ? 34.427 65.739 46.712 1.00 111.26 ? 118 THR D CA 1 +ATOM 8015 C C . THR D 1 119 ? 35.007 66.202 48.067 1.00 99.82 ? 118 THR D C 1 +ATOM 8016 O O . THR D 1 119 ? 35.571 67.295 48.185 1.00 99.36 ? 118 THR D O 1 +ATOM 8017 C CB . THR D 1 119 ? 35.428 64.858 45.896 1.00 88.97 ? 118 THR D CB 1 +ATOM 8018 O OG1 . THR D 1 119 ? 34.747 64.281 44.774 1.00 101.94 ? 118 THR D OG1 1 +ATOM 8019 C CG2 . THR D 1 119 ? 36.004 63.729 46.739 1.00 78.83 ? 118 THR D CG2 1 +ATOM 8020 N N . LEU D 1 120 ? 34.807 65.366 49.088 1.00 95.26 ? 119 LEU D N 1 +ATOM 8021 C CA . LEU D 1 120 ? 35.405 65.543 50.407 1.00 66.23 ? 119 LEU D CA 1 +ATOM 8022 C C . LEU D 1 120 ? 36.694 64.739 50.476 1.00 100.53 ? 119 LEU D C 1 +ATOM 8023 O O . LEU D 1 120 ? 36.678 63.504 50.410 1.00 70.02 ? 119 LEU D O 1 +ATOM 8024 C CB . LEU D 1 120 ? 34.438 65.078 51.498 1.00 65.49 ? 119 LEU D CB 1 +ATOM 8025 C CG . LEU D 1 120 ? 34.761 65.331 52.974 1.00 60.34 ? 119 LEU D CG 1 +ATOM 8026 C CD1 . LEU D 1 120 ? 33.500 65.565 53.730 1.00 138.85 ? 119 LEU D CD1 1 +ATOM 8027 C CD2 . LEU D 1 120 ? 35.538 64.179 53.583 1.00 76.90 ? 119 LEU D CD2 1 +ATOM 8028 N N . VAL D 1 121 ? 37.810 65.451 50.603 1.00 90.90 ? 120 VAL D N 1 +ATOM 8029 C CA . VAL D 1 121 ? 39.118 64.819 50.610 1.00 88.69 ? 120 VAL D CA 1 +ATOM 8030 C C . VAL D 1 121 ? 39.797 64.881 51.990 1.00 106.53 ? 120 VAL D C 1 +ATOM 8031 O O . VAL D 1 121 ? 39.775 65.913 52.674 1.00 85.06 ? 120 VAL D O 1 +ATOM 8032 C CB . VAL D 1 121 ? 40.040 65.389 49.487 1.00 98.01 ? 120 VAL D CB 1 +ATOM 8033 C CG1 . VAL D 1 121 ? 39.342 65.334 48.129 1.00 76.60 ? 120 VAL D CG1 1 +ATOM 8034 C CG2 . VAL D 1 121 ? 40.456 66.813 49.793 1.00 122.23 ? 120 VAL D CG2 1 +ATOM 8035 N N . ASN D 1 122 ? 40.370 63.752 52.399 1.00 86.96 ? 121 ASN D N 1 +ATOM 8036 C CA . ASN D 1 122 ? 41.192 63.688 53.602 1.00 93.14 ? 121 ASN D CA 1 +ATOM 8037 C C . ASN D 1 122 ? 42.662 63.460 53.266 1.00 113.66 ? 121 ASN D C 1 +ATOM 8038 O O . ASN D 1 122 ? 43.030 62.389 52.773 1.00 83.59 ? 121 ASN D O 1 +ATOM 8039 C CB . ASN D 1 122 ? 40.720 62.569 54.520 1.00 63.27 ? 121 ASN D CB 1 +ATOM 8040 C CG . ASN D 1 122 ? 41.281 62.699 55.913 1.00 83.65 ? 121 ASN D CG 1 +ATOM 8041 O OD1 . ASN D 1 122 ? 41.689 63.783 56.325 1.00 119.82 ? 121 ASN D OD1 1 +ATOM 8042 N ND2 . ASN D 1 122 ? 41.303 61.598 56.653 1.00 92.25 ? 121 ASN D ND2 1 +ATOM 8043 N N . ARG D 1 123 ? 43.493 64.464 53.541 1.00 99.51 ? 122 ARG D N 1 +ATOM 8044 C CA . ARG D 1 123 ? 44.920 64.410 53.221 1.00 90.57 ? 122 ARG D CA 1 +ATOM 8045 C C . ARG D 1 123 ? 45.815 64.325 54.452 1.00 100.37 ? 122 ARG D C 1 +ATOM 8046 O O . ARG D 1 123 ? 45.898 65.261 55.248 1.00 78.59 ? 122 ARG D O 1 +ATOM 8047 C CB . ARG D 1 123 ? 45.330 65.605 52.366 1.00 98.58 ? 122 ARG D CB 1 +ATOM 8048 C CG . ARG D 1 123 ? 45.002 65.456 50.897 1.00 95.56 ? 122 ARG D CG 1 +ATOM 8049 C CD . ARG D 1 123 ? 45.673 66.551 50.084 1.00 107.85 ? 122 ARG D CD 1 +ATOM 8050 N NE . ARG D 1 123 ? 44.852 66.968 48.952 1.00 125.26 ? 122 ARG D NE 1 +ATOM 8051 C CZ . ARG D 1 123 ? 44.750 66.295 47.811 1.00 134.46 ? 122 ARG D CZ 1 +ATOM 8052 N NH1 . ARG D 1 123 ? 45.416 65.156 47.643 1.00 112.01 ? 122 ARG D NH1 1 +ATOM 8053 N NH2 . ARG D 1 123 ? 43.974 66.759 46.840 1.00 119.18 ? 122 ARG D NH2 1 +ATOM 8054 N N . ILE D 1 124 ? 46.520 63.204 54.567 1.00 100.77 ? 123 ILE D N 1 +ATOM 8055 C CA . ILE D 1 124 ? 47.186 62.833 55.806 1.00 89.55 ? 123 ILE D CA 1 +ATOM 8056 C C . ILE D 1 124 ? 48.707 62.659 55.691 1.00 99.21 ? 123 ILE D C 1 +ATOM 8057 O O . ILE D 1 124 ? 49.214 62.070 54.733 1.00 75.69 ? 123 ILE D O 1 +ATOM 8058 C CB . ILE D 1 124 ? 46.561 61.536 56.366 1.00 111.33 ? 123 ILE D CB 1 +ATOM 8059 C CG1 . ILE D 1 124 ? 45.097 61.425 55.940 1.00 95.04 ? 123 ILE D CG1 1 +ATOM 8060 C CG2 . ILE D 1 124 ? 46.730 61.450 57.889 1.00 88.69 ? 123 ILE D CG2 1 +ATOM 8061 C CD1 . ILE D 1 124 ? 44.464 60.084 56.203 1.00 106.38 ? 123 ILE D CD1 1 +ATOM 8062 N N . GLU D 1 125 ? 49.413 63.198 56.685 1.00 109.68 ? 124 GLU D N 1 +ATOM 8063 C CA . GLU D 1 125 ? 50.817 62.888 56.955 1.00 97.39 ? 124 GLU D CA 1 +ATOM 8064 C C . GLU D 1 125 ? 50.899 62.219 58.331 1.00 96.55 ? 124 GLU D C 1 +ATOM 8065 O O . GLU D 1 125 ? 50.416 62.783 59.313 1.00 103.89 ? 124 GLU D O 1 +ATOM 8066 C CB . GLU D 1 125 ? 51.656 64.166 56.992 1.00 96.02 ? 124 GLU D CB 1 +ATOM 8067 C CG . GLU D 1 125 ? 51.664 64.968 55.712 1.00 134.11 ? 124 GLU D CG 1 +ATOM 8068 C CD . GLU D 1 125 ? 52.552 66.196 55.801 1.00 157.06 ? 124 GLU D CD 1 +ATOM 8069 O OE1 . GLU D 1 125 ? 52.335 67.041 56.697 1.00 177.99 ? 124 GLU D OE1 1 +ATOM 8070 O OE2 . GLU D 1 125 ? 53.471 66.310 54.968 1.00 137.04 ? 124 GLU D OE2 1 +ATOM 8071 N N . LEU D 1 126 ? 51.502 61.031 58.402 1.00 87.20 ? 125 LEU D N 1 +ATOM 8072 C CA . LEU D 1 126 ? 51.647 60.286 59.665 1.00 99.57 ? 125 LEU D CA 1 +ATOM 8073 C C . LEU D 1 126 ? 53.105 59.868 59.906 1.00 102.39 ? 125 LEU D C 1 +ATOM 8074 O O . LEU D 1 126 ? 53.822 59.534 58.958 1.00 99.92 ? 125 LEU D O 1 +ATOM 8075 C CB . LEU D 1 126 ? 50.709 59.065 59.685 1.00 78.58 ? 125 LEU D CB 1 +ATOM 8076 C CG . LEU D 1 126 ? 50.948 57.884 60.639 1.00 69.03 ? 125 LEU D CG 1 +ATOM 8077 C CD1 . LEU D 1 126 ? 49.652 57.199 60.964 1.00 83.78 ? 125 LEU D CD1 1 +ATOM 8078 C CD2 . LEU D 1 126 ? 51.878 56.853 60.041 1.00 96.66 ? 125 LEU D CD2 1 +ATOM 8079 N N . LYS D 1 127 ? 53.536 59.878 61.169 1.00 105.08 ? 126 LYS D N 1 +ATOM 8080 C CA . LYS D 1 127 ? 54.940 59.610 61.509 1.00 84.79 ? 126 LYS D CA 1 +ATOM 8081 C C . LYS D 1 127 ? 55.145 58.830 62.811 1.00 94.82 ? 126 LYS D C 1 +ATOM 8082 O O . LYS D 1 127 ? 55.176 59.422 63.890 1.00 115.58 ? 126 LYS D O 1 +ATOM 8083 C CB . LYS D 1 127 ? 55.729 60.922 61.578 1.00 97.12 ? 126 LYS D CB 1 +ATOM 8084 C CG . LYS D 1 127 ? 57.194 60.729 61.912 1.00 122.75 ? 126 LYS D CG 1 +ATOM 8085 C CD . LYS D 1 127 ? 58.056 61.912 61.510 1.00 134.90 ? 126 LYS D CD 1 +ATOM 8086 C CE . LYS D 1 127 ? 59.499 61.640 61.892 1.00 126.06 ? 126 LYS D CE 1 +ATOM 8087 N NZ . LYS D 1 127 ? 59.792 60.181 61.755 1.00 114.70 ? 126 LYS D NZ 1 +ATOM 8088 N N . GLY D 1 128 ? 55.314 57.512 62.701 1.00 100.97 ? 127 GLY D N 1 +ATOM 8089 C CA . GLY D 1 128 ? 55.484 56.640 63.859 1.00 98.55 ? 127 GLY D CA 1 +ATOM 8090 C C . GLY D 1 128 ? 56.926 56.401 64.294 1.00 118.96 ? 127 GLY D C 1 +ATOM 8091 O O . GLY D 1 128 ? 57.811 56.226 63.459 1.00 131.00 ? 127 GLY D O 1 +ATOM 8092 N N . ILE D 1 129 ? 57.159 56.405 65.609 1.00 132.07 ? 128 ILE D N 1 +ATOM 8093 C CA . ILE D 1 129 ? 58.495 56.218 66.194 1.00 111.36 ? 128 ILE D CA 1 +ATOM 8094 C C . ILE D 1 129 ? 58.402 55.382 67.469 1.00 89.38 ? 128 ILE D C 1 +ATOM 8095 O O . ILE D 1 129 ? 57.356 55.345 68.108 1.00 115.00 ? 128 ILE D O 1 +ATOM 8096 C CB . ILE D 1 129 ? 59.168 57.578 66.562 1.00 95.23 ? 128 ILE D CB 1 +ATOM 8097 C CG1 . ILE D 1 129 ? 59.451 58.412 65.309 1.00 141.02 ? 128 ILE D CG1 1 +ATOM 8098 C CG2 . ILE D 1 129 ? 60.452 57.382 67.382 1.00 168.15 ? 128 ILE D CG2 1 +ATOM 8099 C CD1 . ILE D 1 129 ? 58.431 59.504 65.052 1.00 133.60 ? 128 ILE D CD1 1 +ATOM 8100 N N . ASP D 1 130 ? 59.494 54.707 67.829 1.00 118.50 ? 129 ASP D N 1 +ATOM 8101 C CA . ASP D 1 130 ? 59.627 54.011 69.115 1.00 125.79 ? 129 ASP D CA 1 +ATOM 8102 C C . ASP D 1 130 ? 58.856 52.708 69.204 1.00 88.05 ? 129 ASP D C 1 +ATOM 8103 O O . ASP D 1 130 ? 58.571 52.228 70.294 1.00 81.91 ? 129 ASP D O 1 +ATOM 8104 C CB . ASP D 1 130 ? 59.259 54.904 70.313 1.00 107.00 ? 129 ASP D CB 1 +ATOM 8105 C CG . ASP D 1 130 ? 60.181 56.088 70.459 1.00 127.94 ? 129 ASP D CG 1 +ATOM 8106 O OD1 . ASP D 1 130 ? 61.410 55.890 70.338 1.00 110.49 ? 129 ASP D OD1 1 +ATOM 8107 O OD2 . ASP D 1 130 ? 59.677 57.213 70.677 1.00 125.58 ? 129 ASP D OD2 1 +ATOM 8108 N N . PHE D 1 131 ? 58.527 52.109 68.074 1.00 68.30 ? 130 PHE D N 1 +ATOM 8109 C CA . PHE D 1 131 ? 57.839 50.833 68.164 1.00 110.31 ? 130 PHE D CA 1 +ATOM 8110 C C . PHE D 1 131 ? 58.830 49.694 68.450 1.00 69.19 ? 130 PHE D C 1 +ATOM 8111 O O . PHE D 1 131 ? 60.020 49.828 68.209 1.00 93.39 ? 130 PHE D O 1 +ATOM 8112 C CB . PHE D 1 131 ? 56.963 50.599 66.926 1.00 99.93 ? 130 PHE D CB 1 +ATOM 8113 C CG . PHE D 1 131 ? 55.746 51.497 66.871 1.00 80.99 ? 130 PHE D CG 1 +ATOM 8114 C CD1 . PHE D 1 131 ? 55.847 52.810 66.413 1.00 108.20 ? 130 PHE D CD1 1 +ATOM 8115 C CD2 . PHE D 1 131 ? 54.510 51.039 67.304 1.00 91.46 ? 130 PHE D CD2 1 +ATOM 8116 C CE1 . PHE D 1 131 ? 54.732 53.650 66.378 1.00 64.75 ? 130 PHE D CE1 1 +ATOM 8117 C CE2 . PHE D 1 131 ? 53.389 51.865 67.274 1.00 81.44 ? 130 PHE D CE2 1 +ATOM 8118 C CZ . PHE D 1 131 ? 53.502 53.174 66.808 1.00 109.00 ? 130 PHE D CZ 1 +ATOM 8119 N N . LYS D 1 132 ? 58.337 48.590 68.995 1.00 79.40 ? 131 LYS D N 1 +ATOM 8120 C CA . LYS D 1 132 ? 59.180 47.446 69.317 1.00 88.33 ? 131 LYS D CA 1 +ATOM 8121 C C . LYS D 1 132 ? 59.100 46.395 68.235 1.00 83.64 ? 131 LYS D C 1 +ATOM 8122 O O . LYS D 1 132 ? 58.089 45.713 68.150 1.00 161.79 ? 131 LYS D O 1 +ATOM 8123 C CB . LYS D 1 132 ? 58.666 46.768 70.577 1.00 70.16 ? 131 LYS D CB 1 +ATOM 8124 C CG . LYS D 1 132 ? 58.310 47.680 71.716 1.00 90.34 ? 131 LYS D CG 1 +ATOM 8125 C CD . LYS D 1 132 ? 57.808 46.834 72.861 1.00 103.11 ? 131 LYS D CD 1 +ATOM 8126 C CE . LYS D 1 132 ? 57.892 47.560 74.176 1.00 115.19 ? 131 LYS D CE 1 +ATOM 8127 N NZ . LYS D 1 132 ? 57.177 46.759 75.208 1.00 117.28 ? 131 LYS D NZ 1 +ATOM 8128 N N . GLU D 1 133 ? 60.172 46.207 67.465 1.00 111.92 ? 132 GLU D N 1 +ATOM 8129 C CA . GLU D 1 133 ? 60.218 45.220 66.368 1.00 136.41 ? 132 GLU D CA 1 +ATOM 8130 C C . GLU D 1 133 ? 59.543 43.859 66.649 1.00 120.71 ? 132 GLU D C 1 +ATOM 8131 O O . GLU D 1 133 ? 59.259 43.098 65.726 1.00 102.99 ? 132 GLU D O 1 +ATOM 8132 C CB . GLU D 1 133 ? 61.666 45.005 65.873 1.00 108.32 ? 132 GLU D CB 1 +ATOM 8133 C CG . GLU D 1 133 ? 62.254 46.138 64.979 1.00 215.53 ? 132 GLU D CG 1 +ATOM 8134 C CD . GLU D 1 133 ? 61.914 46.032 63.466 1.00 191.80 ? 132 GLU D CD 1 +ATOM 8135 O OE1 . GLU D 1 133 ? 61.973 44.920 62.892 1.00 182.94 ? 132 GLU D OE1 1 +ATOM 8136 O OE2 . GLU D 1 133 ? 61.606 47.078 62.843 1.00 144.19 ? 132 GLU D OE2 1 +ATOM 8137 N N . ASP D 1 134 ? 59.273 43.565 67.914 1.00 102.35 ? 133 ASP D N 1 +ATOM 8138 C CA . ASP D 1 134 ? 58.598 42.328 68.286 1.00 102.09 ? 133 ASP D CA 1 +ATOM 8139 C C . ASP D 1 134 ? 57.215 42.599 68.868 1.00 124.47 ? 133 ASP D C 1 +ATOM 8140 O O . ASP D 1 134 ? 56.525 41.673 69.295 1.00 127.27 ? 133 ASP D O 1 +ATOM 8141 C CB . ASP D 1 134 ? 59.441 41.581 69.313 1.00 165.11 ? 133 ASP D CB 1 +ATOM 8142 C CG . ASP D 1 134 ? 59.967 42.499 70.401 1.00 189.66 ? 133 ASP D CG 1 +ATOM 8143 O OD1 . ASP D 1 134 ? 60.244 43.680 70.094 1.00 185.36 ? 133 ASP D OD1 1 +ATOM 8144 O OD2 . ASP D 1 134 ? 60.093 42.043 71.558 1.00 203.24 ? 133 ASP D OD2 1 +ATOM 8145 N N . GLY D 1 135 ? 56.822 43.871 68.882 1.00 142.78 ? 134 GLY D N 1 +ATOM 8146 C CA . GLY D 1 135 ? 55.588 44.283 69.506 1.00 131.46 ? 134 GLY D CA 1 +ATOM 8147 C C . GLY D 1 135 ? 54.292 43.771 68.884 1.00 129.75 ? 134 GLY D C 1 +ATOM 8148 O O . GLY D 1 135 ? 54.297 42.838 68.082 1.00 117.25 ? 134 GLY D O 1 +ATOM 8149 N N . ASN D 1 136 ? 53.174 44.378 69.278 1.00 134.87 ? 135 ASN D N 1 +ATOM 8150 C CA . ASN D 1 136 ? 51.875 44.010 68.720 1.00 87.52 ? 135 ASN D CA 1 +ATOM 8151 C C . ASN D 1 136 ? 51.706 44.572 67.294 1.00 113.28 ? 135 ASN D C 1 +ATOM 8152 O O . ASN D 1 136 ? 51.336 43.848 66.362 1.00 97.00 ? 135 ASN D O 1 +ATOM 8153 C CB . ASN D 1 136 ? 50.735 44.462 69.648 1.00 100.78 ? 135 ASN D CB 1 +ATOM 8154 C CG . ASN D 1 136 ? 50.513 43.515 70.840 1.00 104.92 ? 135 ASN D CG 1 +ATOM 8155 O OD1 . ASN D 1 136 ? 50.824 42.319 70.779 1.00 65.44 ? 135 ASN D OD1 1 +ATOM 8156 N ND2 . ASN D 1 136 ? 49.949 44.057 71.920 1.00 81.36 ? 135 ASN D ND2 1 +ATOM 8157 N N . ILE D 1 137 ? 51.996 45.862 67.141 1.00 90.36 ? 136 ILE D N 1 +ATOM 8158 C CA . ILE D 1 137 ? 52.031 46.529 65.837 1.00 109.98 ? 136 ILE D CA 1 +ATOM 8159 C C . ILE D 1 137 ? 53.014 45.847 64.879 1.00 119.90 ? 136 ILE D C 1 +ATOM 8160 O O . ILE D 1 137 ? 52.622 44.981 64.084 1.00 88.81 ? 136 ILE D O 1 +ATOM 8161 C CB . ILE D 1 137 ? 52.419 48.038 65.961 1.00 87.71 ? 136 ILE D CB 1 +ATOM 8162 C CG1 . ILE D 1 137 ? 51.361 48.829 66.731 1.00 65.75 ? 136 ILE D CG1 1 +ATOM 8163 C CG2 . ILE D 1 137 ? 52.588 48.686 64.586 1.00 61.28 ? 136 ILE D CG2 1 +ATOM 8164 C CD1 . ILE D 1 137 ? 51.362 48.628 68.217 1.00 100.89 ? 136 ILE D CD1 1 +ATOM 8165 N N . LEU D 1 138 ? 54.290 46.220 64.994 1.00 101.88 ? 137 LEU D N 1 +ATOM 8166 C CA . LEU D 1 138 ? 55.316 45.857 64.023 1.00 103.11 ? 137 LEU D CA 1 +ATOM 8167 C C . LEU D 1 138 ? 55.514 44.365 63.889 1.00 113.97 ? 137 LEU D C 1 +ATOM 8168 O O . LEU D 1 138 ? 56.112 43.906 62.919 1.00 90.15 ? 137 LEU D O 1 +ATOM 8169 C CB . LEU D 1 138 ? 56.640 46.523 64.366 1.00 80.67 ? 137 LEU D CB 1 +ATOM 8170 C CG . LEU D 1 138 ? 56.660 47.994 63.985 1.00 99.48 ? 137 LEU D CG 1 +ATOM 8171 C CD1 . LEU D 1 138 ? 58.038 48.544 64.212 1.00 127.89 ? 137 LEU D CD1 1 +ATOM 8172 C CD2 . LEU D 1 138 ? 56.253 48.152 62.533 1.00 82.55 ? 137 LEU D CD2 1 +ATOM 8173 N N . GLY D 1 139 ? 55.007 43.613 64.861 1.00 78.97 ? 138 GLY D N 1 +ATOM 8174 C CA . GLY D 1 139 ? 55.005 42.167 64.776 1.00 83.58 ? 138 GLY D CA 1 +ATOM 8175 C C . GLY D 1 139 ? 53.757 41.620 64.103 1.00 105.49 ? 138 GLY D C 1 +ATOM 8176 O O . GLY D 1 139 ? 53.675 40.419 63.842 1.00 100.78 ? 138 GLY D O 1 +ATOM 8177 N N . HIS D 1 140 ? 52.792 42.497 63.819 1.00 114.46 ? 139 HIS D N 1 +ATOM 8178 C CA . HIS D 1 140 ? 51.500 42.105 63.236 1.00 104.13 ? 139 HIS D CA 1 +ATOM 8179 C C . HIS D 1 140 ? 50.754 41.037 64.058 1.00 93.71 ? 139 HIS D C 1 +ATOM 8180 O O . HIS D 1 140 ? 50.553 39.912 63.596 1.00 92.43 ? 139 HIS D O 1 +ATOM 8181 C CB . HIS D 1 140 ? 51.645 41.677 61.761 1.00 95.12 ? 139 HIS D CB 1 +ATOM 8182 C CG . HIS D 1 140 ? 51.868 42.824 60.818 1.00 111.20 ? 139 HIS D CG 1 +ATOM 8183 N ND1 . HIS D 1 140 ? 53.027 43.017 60.140 1.00 94.55 ? 139 HIS D ND1 1 +ATOM 8184 C CD2 . HIS D 1 140 ? 51.087 43.852 60.453 1.00 144.88 ? 139 HIS D CD2 1 +ATOM 8185 C CE1 . HIS D 1 140 ? 52.954 44.102 59.394 1.00 78.20 ? 139 HIS D CE1 1 +ATOM 8186 N NE2 . HIS D 1 140 ? 51.776 44.628 59.563 1.00 106.61 ? 139 HIS D NE2 1 +ATOM 8187 N N . LYS D 1 141 ? 50.343 41.407 65.272 1.00 103.06 ? 140 LYS D N 1 +ATOM 8188 C CA . LYS D 1 141 ? 49.609 40.508 66.170 1.00 112.76 ? 140 LYS D CA 1 +ATOM 8189 C C . LYS D 1 141 ? 48.180 40.995 66.411 1.00 121.88 ? 140 LYS D C 1 +ATOM 8190 O O . LYS D 1 141 ? 47.412 40.396 67.175 1.00 89.06 ? 140 LYS D O 1 +ATOM 8191 C CB . LYS D 1 141 ? 50.341 40.355 67.506 1.00 104.02 ? 140 LYS D CB 1 +ATOM 8192 C CG . LYS D 1 141 ? 51.563 39.465 67.452 1.00 108.94 ? 140 LYS D CG 1 +ATOM 8193 C CD . LYS D 1 141 ? 52.558 39.890 68.515 1.00 131.77 ? 140 LYS D CD 1 +ATOM 8194 C CE . LYS D 1 141 ? 53.895 39.181 68.362 1.00 121.93 ? 140 LYS D CE 1 +ATOM 8195 N NZ . LYS D 1 141 ? 54.956 39.848 69.164 1.00 142.39 ? 140 LYS D NZ 1 +ATOM 8196 N N . LEU D 1 142 ? 47.831 42.090 65.749 1.00 91.76 ? 141 LEU D N 1 +ATOM 8197 C CA . LEU D 1 142 ? 46.469 42.574 65.780 1.00 81.35 ? 141 LEU D CA 1 +ATOM 8198 C C . LEU D 1 142 ? 45.582 41.702 64.909 1.00 88.66 ? 141 LEU D C 1 +ATOM 8199 O O . LEU D 1 142 ? 46.013 41.181 63.868 1.00 71.19 ? 141 LEU D O 1 +ATOM 8200 C CB . LEU D 1 142 ? 46.398 44.028 65.323 1.00 88.69 ? 141 LEU D CB 1 +ATOM 8201 C CG . LEU D 1 142 ? 47.106 45.038 66.229 1.00 65.84 ? 141 LEU D CG 1 +ATOM 8202 C CD1 . LEU D 1 142 ? 47.106 46.424 65.638 1.00 72.88 ? 141 LEU D CD1 1 +ATOM 8203 C CD2 . LEU D 1 142 ? 46.457 45.069 67.580 1.00 92.65 ? 141 LEU D CD2 1 +ATOM 8204 N N . GLU D 1 143 ? 44.345 41.543 65.372 1.00 85.14 ? 142 GLU D N 1 +ATOM 8205 C CA . GLU D 1 143 ? 43.317 40.794 64.669 1.00 90.60 ? 142 GLU D CA 1 +ATOM 8206 C C . GLU D 1 143 ? 42.637 41.724 63.679 1.00 100.52 ? 142 GLU D C 1 +ATOM 8207 O O . GLU D 1 143 ? 42.453 42.914 63.967 1.00 87.35 ? 142 GLU D O 1 +ATOM 8208 C CB . GLU D 1 143 ? 42.293 40.218 65.657 1.00 87.52 ? 142 GLU D CB 1 +ATOM 8209 C CG . GLU D 1 143 ? 42.586 38.783 66.125 1.00 96.12 ? 142 GLU D CG 1 +ATOM 8210 C CD . GLU D 1 143 ? 41.462 38.189 66.976 1.00 127.22 ? 142 GLU D CD 1 +ATOM 8211 O OE1 . GLU D 1 143 ? 40.589 38.956 67.440 1.00 121.87 ? 142 GLU D OE1 1 +ATOM 8212 O OE2 . GLU D 1 143 ? 41.447 36.952 67.174 1.00 114.47 ? 142 GLU D OE2 1 +ATOM 8213 N N . TYR D 1 144 ? 42.292 41.190 62.507 1.00 71.94 ? 143 TYR D N 1 +ATOM 8214 C CA . TYR D 1 144 ? 41.609 41.980 61.485 1.00 72.93 ? 143 TYR D CA 1 +ATOM 8215 C C . TYR D 1 144 ? 40.171 42.323 61.856 1.00 82.02 ? 143 TYR D C 1 +ATOM 8216 O O . TYR D 1 144 ? 39.229 41.836 61.231 1.00 74.63 ? 143 TYR D O 1 +ATOM 8217 C CB . TYR D 1 144 ? 41.598 41.285 60.124 1.00 63.07 ? 143 TYR D CB 1 +ATOM 8218 C CG . TYR D 1 144 ? 41.382 42.284 59.012 1.00 60.63 ? 143 TYR D CG 1 +ATOM 8219 C CD1 . TYR D 1 144 ? 41.886 43.569 59.123 1.00 97.55 ? 143 TYR D CD1 1 +ATOM 8220 C CD2 . TYR D 1 144 ? 40.659 41.963 57.880 1.00 79.59 ? 143 TYR D CD2 1 +ATOM 8221 C CE1 . TYR D 1 144 ? 41.699 44.495 58.140 1.00 89.20 ? 143 TYR D CE1 1 +ATOM 8222 C CE2 . TYR D 1 144 ? 40.463 42.891 56.887 1.00 80.76 ? 143 TYR D CE2 1 +ATOM 8223 C CZ . TYR D 1 144 ? 40.990 44.154 57.026 1.00 90.08 ? 143 TYR D CZ 1 +ATOM 8224 O OH . TYR D 1 144 ? 40.819 45.095 56.048 1.00 73.48 ? 143 TYR D OH 1 +ATOM 8225 N N . ASN D 1 145 ? 40.001 43.165 62.862 1.00 55.40 ? 144 ASN D N 1 +ATOM 8226 C CA . ASN D 1 145 ? 38.663 43.527 63.296 1.00 69.39 ? 144 ASN D CA 1 +ATOM 8227 C C . ASN D 1 145 ? 38.636 44.814 64.094 1.00 55.81 ? 144 ASN D C 1 +ATOM 8228 O O . ASN D 1 145 ? 39.648 45.502 64.219 1.00 82.83 ? 144 ASN D O 1 +ATOM 8229 C CB . ASN D 1 145 ? 37.990 42.376 64.050 1.00 51.84 ? 144 ASN D CB 1 +ATOM 8230 C CG . ASN D 1 145 ? 38.702 42.004 65.332 1.00 106.78 ? 144 ASN D CG 1 +ATOM 8231 O OD1 . ASN D 1 145 ? 39.199 42.862 66.076 1.00 65.73 ? 144 ASN D OD1 1 +ATOM 8232 N ND2 . ASN D 1 145 ? 38.731 40.706 65.617 1.00 83.74 ? 144 ASN D ND2 1 +ATOM 8233 N N . TYR D 1 146 ? 37.471 45.142 64.626 1.00 65.82 ? 145 TYR D N 1 +ATOM 8234 C CA . TYR D 1 146 ? 37.306 46.412 65.299 1.00 96.90 ? 145 TYR D CA 1 +ATOM 8235 C C . TYR D 1 146 ? 36.177 46.364 66.315 1.00 72.34 ? 145 TYR D C 1 +ATOM 8236 O O . TYR D 1 146 ? 35.321 45.480 66.268 1.00 81.24 ? 145 TYR D O 1 +ATOM 8237 C CB . TYR D 1 146 ? 37.058 47.504 64.274 1.00 59.88 ? 145 TYR D CB 1 +ATOM 8238 C CG . TYR D 1 146 ? 37.827 48.756 64.548 1.00 69.69 ? 145 TYR D CG 1 +ATOM 8239 C CD1 . TYR D 1 146 ? 39.163 48.859 64.209 1.00 66.49 ? 145 TYR D CD1 1 +ATOM 8240 C CD2 . TYR D 1 146 ? 37.217 49.840 65.139 1.00 99.58 ? 145 TYR D CD2 1 +ATOM 8241 C CE1 . TYR D 1 146 ? 39.869 50.019 64.455 1.00 88.09 ? 145 TYR D CE1 1 +ATOM 8242 C CE2 . TYR D 1 146 ? 37.908 51.000 65.387 1.00 79.29 ? 145 TYR D CE2 1 +ATOM 8243 C CZ . TYR D 1 146 ? 39.230 51.087 65.047 1.00 59.62 ? 145 TYR D CZ 1 +ATOM 8244 O OH . TYR D 1 146 ? 39.901 52.256 65.298 1.00 81.55 ? 145 TYR D OH 1 +ATOM 8245 N N . ASN D 1 147 ? 36.213 47.309 67.250 1.00 98.81 ? 146 ASN D N 1 +ATOM 8246 C CA . ASN D 1 147 ? 35.238 47.399 68.330 1.00 80.34 ? 146 ASN D CA 1 +ATOM 8247 C C . ASN D 1 147 ? 34.567 48.764 68.273 1.00 88.58 ? 146 ASN D C 1 +ATOM 8248 O O . ASN D 1 147 ? 34.858 49.577 67.388 1.00 84.14 ? 146 ASN D O 1 +ATOM 8249 C CB . ASN D 1 147 ? 35.902 47.199 69.705 1.00 86.36 ? 146 ASN D CB 1 +ATOM 8250 C CG . ASN D 1 147 ? 36.479 45.797 69.892 1.00 82.07 ? 146 ASN D CG 1 +ATOM 8251 O OD1 . ASN D 1 147 ? 35.879 44.804 69.479 1.00 75.71 ? 146 ASN D OD1 1 +ATOM 8252 N ND2 . ASN D 1 147 ? 37.649 45.715 70.521 1.00 121.69 ? 146 ASN D ND2 1 +ATOM 8253 N N . SER D 1 148 ? 33.669 49.016 69.216 1.00 83.90 ? 147 SER D N 1 +ATOM 8254 C CA . SER D 1 148 ? 32.900 50.248 69.200 1.00 74.40 ? 147 SER D CA 1 +ATOM 8255 C C . SER D 1 148 ? 33.384 51.202 70.279 1.00 60.22 ? 147 SER D C 1 +ATOM 8256 O O . SER D 1 148 ? 33.768 50.772 71.359 1.00 113.00 ? 147 SER D O 1 +ATOM 8257 C CB . SER D 1 148 ? 31.416 49.938 69.351 1.00 72.14 ? 147 SER D CB 1 +ATOM 8258 O OG . SER D 1 148 ? 30.912 49.388 68.147 1.00 93.13 ? 147 SER D OG 1 +ATOM 8259 N N . HIS D 1 149 ? 33.386 52.495 69.985 1.00 71.84 ? 148 HIS D N 1 +ATOM 8260 C CA . HIS D 1 149 ? 33.980 53.453 70.910 1.00 87.19 ? 148 HIS D CA 1 +ATOM 8261 C C . HIS D 1 149 ? 33.147 54.730 71.008 1.00 85.38 ? 148 HIS D C 1 +ATOM 8262 O O . HIS D 1 149 ? 32.242 54.949 70.206 1.00 88.29 ? 148 HIS D O 1 +ATOM 8263 C CB . HIS D 1 149 ? 35.445 53.736 70.519 1.00 84.24 ? 148 HIS D CB 1 +ATOM 8264 C CG . HIS D 1 149 ? 36.274 52.493 70.373 1.00 80.83 ? 148 HIS D CG 1 +ATOM 8265 N ND1 . HIS D 1 149 ? 36.679 52.005 69.149 1.00 82.44 ? 148 HIS D ND1 1 +ATOM 8266 C CD2 . HIS D 1 149 ? 36.723 51.609 71.295 1.00 122.47 ? 148 HIS D CD2 1 +ATOM 8267 C CE1 . HIS D 1 149 ? 37.357 50.886 69.326 1.00 95.91 ? 148 HIS D CE1 1 +ATOM 8268 N NE2 . HIS D 1 149 ? 37.396 50.621 70.619 1.00 71.43 ? 148 HIS D NE2 1 +ATOM 8269 N N . ASN D 1 150 ? 33.429 55.549 72.014 1.00 81.09 ? 149 ASN D N 1 +ATOM 8270 C CA . ASN D 1 150 ? 32.731 56.820 72.183 1.00 93.88 ? 149 ASN D CA 1 +ATOM 8271 C C . ASN D 1 150 ? 33.743 57.969 72.137 1.00 81.19 ? 149 ASN D C 1 +ATOM 8272 O O . ASN D 1 150 ? 34.732 57.963 72.861 1.00 106.94 ? 149 ASN D O 1 +ATOM 8273 C CB . ASN D 1 150 ? 31.896 56.839 73.479 1.00 101.23 ? 149 ASN D CB 1 +ATOM 8274 C CG . ASN D 1 150 ? 30.878 55.684 73.558 1.00 95.27 ? 149 ASN D CG 1 +ATOM 8275 O OD1 . ASN D 1 150 ? 29.917 55.626 72.788 1.00 129.52 ? 149 ASN D OD1 1 +ATOM 8276 N ND2 . ASN D 1 150 ? 31.082 54.780 74.511 1.00 106.80 ? 149 ASN D ND2 1 +ATOM 8277 N N . VAL D 1 151 ? 33.484 58.947 71.276 1.00 98.88 ? 150 VAL D N 1 +ATOM 8278 C CA . VAL D 1 151 ? 34.477 59.945 70.876 1.00 76.96 ? 150 VAL D CA 1 +ATOM 8279 C C . VAL D 1 151 ? 34.214 61.290 71.566 1.00 105.78 ? 150 VAL D C 1 +ATOM 8280 O O . VAL D 1 151 ? 33.626 62.194 70.975 1.00 109.13 ? 150 VAL D O 1 +ATOM 8281 C CB . VAL D 1 151 ? 34.466 60.093 69.313 1.00 96.93 ? 150 VAL D CB 1 +ATOM 8282 C CG1 . VAL D 1 151 ? 35.401 61.181 68.816 1.00 66.93 ? 150 VAL D CG1 1 +ATOM 8283 C CG2 . VAL D 1 151 ? 34.826 58.774 68.653 1.00 73.15 ? 150 VAL D CG2 1 +ATOM 8284 N N . TYR D 1 152 ? 34.649 61.426 72.816 1.00 90.96 ? 151 TYR D N 1 +ATOM 8285 C CA . TYR D 1 152 ? 34.276 62.599 73.614 1.00 93.71 ? 151 TYR D CA 1 +ATOM 8286 C C . TYR D 1 152 ? 34.818 63.925 73.075 1.00 93.41 ? 151 TYR D C 1 +ATOM 8287 O O . TYR D 1 152 ? 36.021 64.160 73.050 1.00 92.93 ? 151 TYR D O 1 +ATOM 8288 C CB . TYR D 1 152 ? 34.607 62.394 75.101 1.00 77.46 ? 151 TYR D CB 1 +ATOM 8289 C CG . TYR D 1 152 ? 34.051 61.089 75.631 1.00 88.70 ? 151 TYR D CG 1 +ATOM 8290 C CD1 . TYR D 1 152 ? 32.750 61.002 76.127 1.00 96.26 ? 151 TYR D CD1 1 +ATOM 8291 C CD2 . TYR D 1 152 ? 34.817 59.932 75.603 1.00 64.98 ? 151 TYR D CD2 1 +ATOM 8292 C CE1 . TYR D 1 152 ? 32.234 59.789 76.601 1.00 83.90 ? 151 TYR D CE1 1 +ATOM 8293 C CE2 . TYR D 1 152 ? 34.315 58.720 76.071 1.00 121.13 ? 151 TYR D CE2 1 +ATOM 8294 C CZ . TYR D 1 152 ? 33.024 58.650 76.570 1.00 117.29 ? 151 TYR D CZ 1 +ATOM 8295 O OH . TYR D 1 152 ? 32.535 57.438 77.029 1.00 91.61 ? 151 TYR D OH 1 +ATOM 8296 N N . ILE D 1 153 ? 33.899 64.775 72.630 1.00 75.13 ? 152 ILE D N 1 +ATOM 8297 C CA . ILE D 1 153 ? 34.221 66.100 72.110 1.00 102.56 ? 152 ILE D CA 1 +ATOM 8298 C C . ILE D 1 153 ? 34.086 67.151 73.224 1.00 119.34 ? 152 ILE D C 1 +ATOM 8299 O O . ILE D 1 153 ? 33.412 66.929 74.236 1.00 119.31 ? 152 ILE D O 1 +ATOM 8300 C CB . ILE D 1 153 ? 33.330 66.442 70.873 1.00 93.66 ? 152 ILE D CB 1 +ATOM 8301 C CG1 . ILE D 1 153 ? 33.276 65.245 69.923 1.00 75.51 ? 152 ILE D CG1 1 +ATOM 8302 C CG2 . ILE D 1 153 ? 33.820 67.687 70.122 1.00 77.96 ? 152 ILE D CG2 1 +ATOM 8303 C CD1 . ILE D 1 153 ? 32.580 65.535 68.628 1.00 122.27 ? 152 ILE D CD1 1 +ATOM 8304 N N . MET D 1 154 ? 34.750 68.285 73.030 1.00 115.47 ? 153 MET D N 1 +ATOM 8305 C CA . MET D 1 154 ? 34.845 69.330 74.032 1.00 131.20 ? 153 MET D CA 1 +ATOM 8306 C C . MET D 1 154 ? 35.296 70.581 73.301 1.00 118.89 ? 153 MET D C 1 +ATOM 8307 O O . MET D 1 154 ? 36.174 70.518 72.446 1.00 120.75 ? 153 MET D O 1 +ATOM 8308 C CB . MET D 1 154 ? 35.870 68.922 75.092 1.00 134.84 ? 153 MET D CB 1 +ATOM 8309 C CG . MET D 1 154 ? 36.087 69.915 76.211 1.00 133.75 ? 153 MET D CG 1 +ATOM 8310 S SD . MET D 1 154 ? 36.318 69.116 77.803 1.00 201.79 ? 153 MET D SD 1 +ATOM 8311 C CE . MET D 1 154 ? 37.395 67.768 77.407 1.00 112.70 ? 153 MET D CE 1 +ATOM 8312 N N . ALA D 1 155 ? 34.685 71.717 73.602 1.00 110.88 ? 154 ALA D N 1 +ATOM 8313 C CA . ALA D 1 155 ? 35.064 72.936 72.905 1.00 112.89 ? 154 ALA D CA 1 +ATOM 8314 C C . ALA D 1 155 ? 36.385 73.495 73.427 1.00 145.14 ? 154 ALA D C 1 +ATOM 8315 O O . ALA D 1 155 ? 36.754 73.293 74.588 1.00 124.58 ? 154 ALA D O 1 +ATOM 8316 C CB . ALA D 1 155 ? 33.958 73.982 72.991 1.00 89.44 ? 154 ALA D CB 1 +ATOM 8317 N N . ASP D 1 156 ? 37.106 74.171 72.541 1.00 150.93 ? 155 ASP D N 1 +ATOM 8318 C CA . ASP D 1 156 ? 38.261 74.964 72.924 1.00 171.11 ? 155 ASP D CA 1 +ATOM 8319 C C . ASP D 1 156 ? 37.972 76.388 72.473 1.00 186.26 ? 155 ASP D C 1 +ATOM 8320 O O . ASP D 1 156 ? 38.368 76.799 71.377 1.00 141.64 ? 155 ASP D O 1 +ATOM 8321 C CB . ASP D 1 156 ? 39.527 74.436 72.252 1.00 164.91 ? 155 ASP D CB 1 +ATOM 8322 C CG . ASP D 1 156 ? 40.786 75.132 72.741 1.00 166.83 ? 155 ASP D CG 1 +ATOM 8323 O OD1 . ASP D 1 156 ? 40.685 76.071 73.564 1.00 175.39 ? 155 ASP D OD1 1 +ATOM 8324 O OD2 . ASP D 1 156 ? 41.881 74.730 72.292 1.00 133.81 ? 155 ASP D OD2 1 +ATOM 8325 N N . LYS D 1 157 ? 37.266 77.132 73.319 1.00 202.82 ? 156 LYS D N 1 +ATOM 8326 C CA . LYS D 1 157 ? 36.771 78.454 72.949 1.00 193.47 ? 156 LYS D CA 1 +ATOM 8327 C C . LYS D 1 157 ? 37.903 79.439 72.684 1.00 175.46 ? 156 LYS D C 1 +ATOM 8328 O O . LYS D 1 157 ? 37.740 80.399 71.929 1.00 135.92 ? 156 LYS D O 1 +ATOM 8329 C CB . LYS D 1 157 ? 35.799 78.990 74.008 1.00 187.84 ? 156 LYS D CB 1 +ATOM 8330 C CG . LYS D 1 157 ? 34.454 78.276 73.994 1.00 188.27 ? 156 LYS D CG 1 +ATOM 8331 C CD . LYS D 1 157 ? 33.492 78.791 75.050 1.00 175.30 ? 156 LYS D CD 1 +ATOM 8332 C CE . LYS D 1 157 ? 32.098 78.199 74.847 1.00 164.90 ? 156 LYS D CE 1 +ATOM 8333 N NZ . LYS D 1 157 ? 32.095 76.705 74.820 1.00 163.07 ? 156 LYS D NZ 1 +ATOM 8334 N N . GLN D 1 158 ? 39.057 79.181 73.291 1.00 194.53 ? 157 GLN D N 1 +ATOM 8335 C CA . GLN D 1 158 ? 40.212 80.052 73.121 1.00 195.11 ? 157 GLN D CA 1 +ATOM 8336 C C . GLN D 1 158 ? 40.859 79.866 71.744 1.00 175.95 ? 157 GLN D C 1 +ATOM 8337 O O . GLN D 1 158 ? 41.268 80.842 71.114 1.00 150.69 ? 157 GLN D O 1 +ATOM 8338 C CB . GLN D 1 158 ? 41.232 79.853 74.255 1.00 185.42 ? 157 GLN D CB 1 +ATOM 8339 C CG . GLN D 1 158 ? 40.713 80.198 75.670 1.00 200.82 ? 157 GLN D CG 1 +ATOM 8340 C CD . GLN D 1 158 ? 40.442 81.694 75.896 1.00 204.64 ? 157 GLN D CD 1 +ATOM 8341 O OE1 . GLN D 1 158 ? 39.444 82.240 75.423 1.00 211.09 ? 157 GLN D OE1 1 +ATOM 8342 N NE2 . GLN D 1 158 ? 41.324 82.349 76.643 1.00 179.78 ? 157 GLN D NE2 1 +ATOM 8343 N N . LYS D 1 159 ? 40.929 78.623 71.269 1.00 179.82 ? 158 LYS D N 1 +ATOM 8344 C CA . LYS D 1 159 ? 41.586 78.338 69.991 1.00 158.57 ? 158 LYS D CA 1 +ATOM 8345 C C . LYS D 1 159 ? 40.597 78.081 68.849 1.00 154.99 ? 158 LYS D C 1 +ATOM 8346 O O . LYS D 1 159 ? 40.984 77.583 67.789 1.00 127.43 ? 158 LYS D O 1 +ATOM 8347 C CB . LYS D 1 159 ? 42.572 77.171 70.129 1.00 143.74 ? 158 LYS D CB 1 +ATOM 8348 C CG . LYS D 1 159 ? 43.461 77.253 71.376 1.00 193.08 ? 158 LYS D CG 1 +ATOM 8349 C CD . LYS D 1 159 ? 44.131 78.622 71.528 1.00 203.52 ? 158 LYS D CD 1 +ATOM 8350 C CE . LYS D 1 159 ? 44.512 78.910 72.981 1.00 177.51 ? 158 LYS D CE 1 +ATOM 8351 N NZ . LYS D 1 159 ? 44.834 80.350 73.208 1.00 165.03 ? 158 LYS D NZ 1 +ATOM 8352 N N . ASN D 1 160 ? 39.327 78.419 69.079 1.00 157.42 ? 159 ASN D N 1 +ATOM 8353 C CA . ASN D 1 160 ? 38.285 78.375 68.045 1.00 156.65 ? 159 ASN D CA 1 +ATOM 8354 C C . ASN D 1 160 ? 38.147 77.004 67.369 1.00 135.47 ? 159 ASN D C 1 +ATOM 8355 O O . ASN D 1 160 ? 37.789 76.896 66.196 1.00 116.18 ? 159 ASN D O 1 +ATOM 8356 C CB . ASN D 1 160 ? 38.521 79.482 67.005 1.00 153.72 ? 159 ASN D CB 1 +ATOM 8357 C CG . ASN D 1 160 ? 37.285 79.781 66.163 1.00 167.26 ? 159 ASN D CG 1 +ATOM 8358 O OD1 . ASN D 1 160 ? 36.155 79.725 66.650 1.00 165.72 ? 159 ASN D OD1 1 +ATOM 8359 N ND2 . ASN D 1 160 ? 37.501 80.095 64.889 1.00 148.77 ? 159 ASN D ND2 1 +ATOM 8360 N N . GLY D 1 161 ? 38.436 75.952 68.117 1.00 123.59 ? 160 GLY D N 1 +ATOM 8361 C CA . GLY D 1 161 ? 38.320 74.616 67.577 1.00 126.57 ? 160 GLY D CA 1 +ATOM 8362 C C . GLY D 1 161 ? 37.798 73.711 68.662 1.00 125.80 ? 160 GLY D C 1 +ATOM 8363 O O . GLY D 1 161 ? 37.234 74.187 69.642 1.00 129.10 ? 160 GLY D O 1 +ATOM 8364 N N . ILE D 1 162 ? 37.989 72.410 68.497 1.00 123.74 ? 161 ILE D N 1 +ATOM 8365 C CA . ILE D 1 162 ? 37.588 71.463 69.527 1.00 117.78 ? 161 ILE D CA 1 +ATOM 8366 C C . ILE D 1 162 ? 38.776 70.648 70.017 1.00 105.38 ? 161 ILE D C 1 +ATOM 8367 O O . ILE D 1 162 ? 39.812 70.585 69.360 1.00 110.63 ? 161 ILE D O 1 +ATOM 8368 C CB . ILE D 1 162 ? 36.489 70.506 69.028 1.00 120.93 ? 161 ILE D CB 1 +ATOM 8369 C CG1 . ILE D 1 162 ? 36.954 69.753 67.780 1.00 121.27 ? 161 ILE D CG1 1 +ATOM 8370 C CG2 . ILE D 1 162 ? 35.204 71.270 68.736 1.00 128.16 ? 161 ILE D CG2 1 +ATOM 8371 C CD1 . ILE D 1 162 ? 35.989 68.678 67.327 1.00 82.54 ? 161 ILE D CD1 1 +ATOM 8372 N N . LYS D 1 163 ? 38.618 70.041 71.186 1.00 93.01 ? 162 LYS D N 1 +ATOM 8373 C CA . LYS D 1 163 ? 39.587 69.090 71.708 1.00 110.18 ? 162 LYS D CA 1 +ATOM 8374 C C . LYS D 1 163 ? 38.909 67.734 71.786 1.00 117.27 ? 162 LYS D C 1 +ATOM 8375 O O . LYS D 1 163 ? 37.812 67.618 72.315 1.00 129.70 ? 162 LYS D O 1 +ATOM 8376 C CB . LYS D 1 163 ? 40.048 69.503 73.105 1.00 133.77 ? 162 LYS D CB 1 +ATOM 8377 C CG . LYS D 1 163 ? 41.472 70.021 73.178 1.00 169.22 ? 162 LYS D CG 1 +ATOM 8378 C CD . LYS D 1 163 ? 41.931 70.191 74.621 1.00 168.51 ? 162 LYS D CD 1 +ATOM 8379 C CE . LYS D 1 163 ? 43.303 70.856 74.697 1.00 162.09 ? 162 LYS D CE 1 +ATOM 8380 N NZ . LYS D 1 163 ? 43.304 72.225 74.108 1.00 161.15 ? 162 LYS D NZ 1 +ATOM 8381 N N . VAL D 1 164 ? 39.544 66.697 71.265 1.00 97.14 ? 163 VAL D N 1 +ATOM 8382 C CA . VAL D 1 164 ? 38.897 65.396 71.257 1.00 93.87 ? 163 VAL D CA 1 +ATOM 8383 C C . VAL D 1 164 ? 39.781 64.345 71.912 1.00 76.64 ? 163 VAL D C 1 +ATOM 8384 O O . VAL D 1 164 ? 41.002 64.386 71.786 1.00 115.14 ? 163 VAL D O 1 +ATOM 8385 C CB . VAL D 1 164 ? 38.532 64.976 69.810 1.00 119.60 ? 163 VAL D CB 1 +ATOM 8386 C CG1 . VAL D 1 164 ? 37.725 63.679 69.787 1.00 81.20 ? 163 VAL D CG1 1 +ATOM 8387 C CG2 . VAL D 1 164 ? 37.765 66.092 69.113 1.00 108.29 ? 163 VAL D CG2 1 +ATOM 8388 N N . ASN D 1 165 ? 39.170 63.403 72.618 1.00 82.64 ? 164 ASN D N 1 +ATOM 8389 C CA . ASN D 1 165 ? 39.937 62.288 73.149 1.00 104.56 ? 164 ASN D CA 1 +ATOM 8390 C C . ASN D 1 165 ? 39.119 61.004 73.252 1.00 94.01 ? 164 ASN D C 1 +ATOM 8391 O O . ASN D 1 165 ? 37.907 61.052 73.438 1.00 111.74 ? 164 ASN D O 1 +ATOM 8392 C CB . ASN D 1 165 ? 40.548 62.661 74.500 1.00 103.86 ? 164 ASN D CB 1 +ATOM 8393 C CG . ASN D 1 165 ? 39.513 62.788 75.591 1.00 126.66 ? 164 ASN D CG 1 +ATOM 8394 O OD1 . ASN D 1 165 ? 38.726 63.737 75.612 1.00 149.68 ? 164 ASN D OD1 1 +ATOM 8395 N ND2 . ASN D 1 165 ? 39.511 61.831 76.514 1.00 156.30 ? 164 ASN D ND2 1 +ATOM 8396 N N . PHE D 1 166 ? 39.792 59.865 73.113 1.00 76.77 ? 165 PHE D N 1 +ATOM 8397 C CA . PHE D 1 166 ? 39.164 58.552 73.254 1.00 88.93 ? 165 PHE D CA 1 +ATOM 8398 C C . PHE D 1 166 ? 40.202 57.460 73.299 1.00 70.36 ? 165 PHE D C 1 +ATOM 8399 O O . PHE D 1 166 ? 41.386 57.705 73.096 1.00 100.90 ? 165 PHE D O 1 +ATOM 8400 C CB . PHE D 1 166 ? 38.187 58.253 72.117 1.00 99.06 ? 165 PHE D CB 1 +ATOM 8401 C CG . PHE D 1 166 ? 38.751 58.476 70.734 1.00 100.76 ? 165 PHE D CG 1 +ATOM 8402 C CD1 . PHE D 1 166 ? 38.843 59.761 70.203 1.00 78.44 ? 165 PHE D CD1 1 +ATOM 8403 C CD2 . PHE D 1 166 ? 39.133 57.402 69.947 1.00 60.25 ? 165 PHE D CD2 1 +ATOM 8404 C CE1 . PHE D 1 166 ? 39.333 59.972 68.933 1.00 67.85 ? 165 PHE D CE1 1 +ATOM 8405 C CE2 . PHE D 1 166 ? 39.618 57.604 68.680 1.00 76.25 ? 165 PHE D CE2 1 +ATOM 8406 C CZ . PHE D 1 166 ? 39.721 58.895 68.171 1.00 91.09 ? 165 PHE D CZ 1 +ATOM 8407 N N . LYS D 1 167 ? 39.742 56.242 73.539 1.00 79.74 ? 166 LYS D N 1 +ATOM 8408 C CA . LYS D 1 167 ? 40.651 55.130 73.728 1.00 97.26 ? 166 LYS D CA 1 +ATOM 8409 C C . LYS D 1 167 ? 40.190 53.900 72.962 1.00 95.40 ? 166 LYS D C 1 +ATOM 8410 O O . LYS D 1 167 ? 39.221 53.240 73.347 1.00 98.47 ? 166 LYS D O 1 +ATOM 8411 C CB . LYS D 1 167 ? 40.787 54.814 75.220 1.00 74.62 ? 166 LYS D CB 1 +ATOM 8412 C CG . LYS D 1 167 ? 41.772 53.695 75.552 1.00 126.71 ? 166 LYS D CG 1 +ATOM 8413 C CD . LYS D 1 167 ? 41.754 53.354 77.044 1.00 149.32 ? 166 LYS D CD 1 +ATOM 8414 C CE . LYS D 1 167 ? 41.793 54.605 77.937 1.00 128.25 ? 166 LYS D CE 1 +ATOM 8415 N NZ . LYS D 1 167 ? 43.049 55.402 77.808 1.00 158.89 ? 166 LYS D NZ 1 +ATOM 8416 N N . ILE D 1 168 ? 40.909 53.597 71.886 1.00 84.60 ? 167 ILE D N 1 +ATOM 8417 C CA . ILE D 1 168 ? 40.594 52.464 71.026 1.00 99.90 ? 167 ILE D CA 1 +ATOM 8418 C C . ILE D 1 168 ? 41.155 51.166 71.591 1.00 83.48 ? 167 ILE D C 1 +ATOM 8419 O O . ILE D 1 168 ? 42.318 51.104 71.960 1.00 86.57 ? 167 ILE D O 1 +ATOM 8420 C CB . ILE D 1 168 ? 41.194 52.653 69.612 1.00 72.77 ? 167 ILE D CB 1 +ATOM 8421 C CG1 . ILE D 1 168 ? 40.683 53.939 68.954 1.00 78.93 ? 167 ILE D CG1 1 +ATOM 8422 C CG2 . ILE D 1 168 ? 40.919 51.439 68.745 1.00 77.97 ? 167 ILE D CG2 1 +ATOM 8423 C CD1 . ILE D 1 168 ? 39.199 53.981 68.698 1.00 98.78 ? 167 ILE D CD1 1 +ATOM 8424 N N . ARG D 1 169 ? 40.329 50.129 71.651 1.00 70.52 ? 168 ARG D N 1 +ATOM 8425 C CA . ARG D 1 169 ? 40.812 48.793 71.976 1.00 87.92 ? 168 ARG D CA 1 +ATOM 8426 C C . ARG D 1 169 ? 41.036 47.968 70.702 1.00 70.21 ? 168 ARG D C 1 +ATOM 8427 O O . ARG D 1 169 ? 40.106 47.779 69.921 1.00 101.12 ? 168 ARG D O 1 +ATOM 8428 C CB . ARG D 1 169 ? 39.804 48.075 72.885 1.00 94.63 ? 168 ARG D CB 1 +ATOM 8429 C CG . ARG D 1 169 ? 39.601 48.720 74.260 1.00 105.42 ? 168 ARG D CG 1 +ATOM 8430 C CD . ARG D 1 169 ? 38.621 47.941 75.168 1.00 94.87 ? 168 ARG D CD 1 +ATOM 8431 N NE . ARG D 1 169 ? 37.263 47.899 74.626 1.00 120.09 ? 168 ARG D NE 1 +ATOM 8432 C CZ . ARG D 1 169 ? 36.466 48.958 74.486 1.00 142.52 ? 168 ARG D CZ 1 +ATOM 8433 N NH1 . ARG D 1 169 ? 36.872 50.173 74.845 1.00 119.27 ? 168 ARG D NH1 1 +ATOM 8434 N NH2 . ARG D 1 169 ? 35.253 48.803 73.973 1.00 123.38 ? 168 ARG D NH2 1 +ATOM 8435 N N . HIS D 1 170 ? 42.258 47.479 70.492 1.00 59.57 ? 169 HIS D N 1 +ATOM 8436 C CA . HIS D 1 170 ? 42.524 46.506 69.424 1.00 85.43 ? 169 HIS D CA 1 +ATOM 8437 C C . HIS D 1 170 ? 42.593 45.079 69.964 1.00 59.85 ? 169 HIS D C 1 +ATOM 8438 O O . HIS D 1 170 ? 43.233 44.838 70.970 1.00 112.69 ? 169 HIS D O 1 +ATOM 8439 C CB . HIS D 1 170 ? 43.833 46.824 68.718 1.00 57.12 ? 169 HIS D CB 1 +ATOM 8440 C CG . HIS D 1 170 ? 43.891 48.197 68.132 1.00 94.71 ? 169 HIS D CG 1 +ATOM 8441 N ND1 . HIS D 1 170 ? 43.473 48.476 66.850 1.00 101.31 ? 169 HIS D ND1 1 +ATOM 8442 C CD2 . HIS D 1 170 ? 44.328 49.368 68.650 1.00 102.58 ? 169 HIS D CD2 1 +ATOM 8443 C CE1 . HIS D 1 170 ? 43.645 49.762 66.605 1.00 86.34 ? 169 HIS D CE1 1 +ATOM 8444 N NE2 . HIS D 1 170 ? 44.159 50.328 67.681 1.00 66.94 ? 169 HIS D NE2 1 +ATOM 8445 N N . ASN D 1 171 ? 41.933 44.133 69.306 1.00 110.06 ? 170 ASN D N 1 +ATOM 8446 C CA . ASN D 1 171 ? 42.009 42.735 69.720 1.00 71.94 ? 170 ASN D CA 1 +ATOM 8447 C C . ASN D 1 171 ? 43.301 42.106 69.225 1.00 96.13 ? 170 ASN D C 1 +ATOM 8448 O O . ASN D 1 171 ? 43.811 42.500 68.179 1.00 129.47 ? 170 ASN D O 1 +ATOM 8449 C CB . ASN D 1 171 ? 40.834 41.942 69.148 1.00 112.38 ? 170 ASN D CB 1 +ATOM 8450 C CG . ASN D 1 171 ? 39.556 42.134 69.931 1.00 106.49 ? 170 ASN D CG 1 +ATOM 8451 O OD1 . ASN D 1 171 ? 39.380 43.134 70.626 1.00 86.72 ? 170 ASN D OD1 1 +ATOM 8452 N ND2 . ASN D 1 171 ? 38.649 41.169 69.817 1.00 101.08 ? 170 ASN D ND2 1 +ATOM 8453 N N . ILE D 1 172 ? 43.806 41.121 69.971 1.00 103.23 ? 171 ILE D N 1 +ATOM 8454 C CA . ILE D 1 172 ? 45.019 40.359 69.642 1.00 97.96 ? 171 ILE D CA 1 +ATOM 8455 C C . ILE D 1 172 ? 44.627 38.882 69.733 1.00 116.79 ? 171 ILE D C 1 +ATOM 8456 O O . ILE D 1 172 ? 43.599 38.577 70.332 1.00 146.95 ? 171 ILE D O 1 +ATOM 8457 C CB . ILE D 1 172 ? 46.145 40.703 70.643 1.00 92.01 ? 171 ILE D CB 1 +ATOM 8458 C CG1 . ILE D 1 172 ? 46.478 42.191 70.550 1.00 95.19 ? 171 ILE D CG1 1 +ATOM 8459 C CG2 . ILE D 1 172 ? 47.399 39.872 70.412 1.00 69.57 ? 171 ILE D CG2 1 +ATOM 8460 C CD1 . ILE D 1 172 ? 46.976 42.778 71.844 1.00 100.96 ? 171 ILE D CD1 1 +ATOM 8461 N N . GLU D 1 173 ? 45.390 37.959 69.145 1.00 78.35 ? 172 GLU D N 1 +ATOM 8462 C CA . GLU D 1 173 ? 44.924 36.565 69.149 1.00 127.89 ? 172 GLU D CA 1 +ATOM 8463 C C . GLU D 1 173 ? 44.929 35.844 70.512 1.00 143.53 ? 172 GLU D C 1 +ATOM 8464 O O . GLU D 1 173 ? 44.099 34.966 70.755 1.00 154.94 ? 172 GLU D O 1 +ATOM 8465 C CB . GLU D 1 173 ? 45.592 35.697 68.076 1.00 101.91 ? 172 GLU D CB 1 +ATOM 8466 C CG . GLU D 1 173 ? 44.738 34.453 67.790 1.00 163.57 ? 172 GLU D CG 1 +ATOM 8467 C CD . GLU D 1 173 ? 45.410 33.396 66.933 1.00 200.31 ? 172 GLU D CD 1 +ATOM 8468 O OE1 . GLU D 1 173 ? 46.511 32.932 67.292 1.00 177.32 ? 172 GLU D OE1 1 +ATOM 8469 O OE2 . GLU D 1 173 ? 44.813 33.012 65.906 1.00 208.95 ? 172 GLU D OE2 1 +ATOM 8470 N N . ASP D 1 174 ? 45.837 36.210 71.407 1.00 116.16 ? 173 ASP D N 1 +ATOM 8471 C CA . ASP D 1 174 ? 45.876 35.570 72.722 1.00 125.14 ? 173 ASP D CA 1 +ATOM 8472 C C . ASP D 1 174 ? 44.707 35.981 73.638 1.00 153.97 ? 173 ASP D C 1 +ATOM 8473 O O . ASP D 1 174 ? 44.602 35.518 74.774 1.00 214.60 ? 173 ASP D O 1 +ATOM 8474 C CB . ASP D 1 174 ? 47.221 35.831 73.406 1.00 141.84 ? 173 ASP D CB 1 +ATOM 8475 C CG . ASP D 1 174 ? 47.584 37.307 73.444 1.00 140.86 ? 173 ASP D CG 1 +ATOM 8476 O OD1 . ASP D 1 174 ? 46.668 38.157 73.451 1.00 136.32 ? 173 ASP D OD1 1 +ATOM 8477 O OD2 . ASP D 1 174 ? 48.793 37.622 73.470 1.00 135.82 ? 173 ASP D OD2 1 +ATOM 8478 N N . GLY D 1 175 ? 43.837 36.857 73.145 1.00 98.56 ? 174 GLY D N 1 +ATOM 8479 C CA . GLY D 1 175 ? 42.689 37.302 73.913 1.00 99.93 ? 174 GLY D CA 1 +ATOM 8480 C C . GLY D 1 175 ? 42.902 38.649 74.575 1.00 117.35 ? 174 GLY D C 1 +ATOM 8481 O O . GLY D 1 175 ? 41.963 39.238 75.117 1.00 114.94 ? 174 GLY D O 1 +ATOM 8482 N N . SER D 1 176 ? 44.139 39.138 74.536 1.00 82.97 ? 175 SER D N 1 +ATOM 8483 C CA . SER D 1 176 ? 44.463 40.416 75.166 1.00 111.81 ? 175 SER D CA 1 +ATOM 8484 C C . SER D 1 176 ? 44.120 41.572 74.245 1.00 95.86 ? 175 SER D C 1 +ATOM 8485 O O . SER D 1 176 ? 43.664 41.360 73.126 1.00 110.14 ? 175 SER D O 1 +ATOM 8486 C CB . SER D 1 176 ? 45.930 40.477 75.598 1.00 107.31 ? 175 SER D CB 1 +ATOM 8487 O OG . SER D 1 176 ? 46.803 40.193 74.522 1.00 107.44 ? 175 SER D OG 1 +ATOM 8488 N N . VAL D 1 177 ? 44.350 42.793 74.717 1.00 91.57 ? 176 VAL D N 1 +ATOM 8489 C CA . VAL D 1 177 ? 43.805 43.985 74.072 1.00 84.34 ? 176 VAL D CA 1 +ATOM 8490 C C . VAL D 1 177 ? 44.784 45.156 74.048 1.00 106.05 ? 176 VAL D C 1 +ATOM 8491 O O . VAL D 1 177 ? 45.099 45.738 75.084 1.00 131.19 ? 176 VAL D O 1 +ATOM 8492 C CB . VAL D 1 177 ? 42.507 44.452 74.783 1.00 81.00 ? 176 VAL D CB 1 +ATOM 8493 C CG1 . VAL D 1 177 ? 42.042 45.812 74.253 1.00 94.79 ? 176 VAL D CG1 1 +ATOM 8494 C CG2 . VAL D 1 177 ? 41.409 43.401 74.660 1.00 90.68 ? 176 VAL D CG2 1 +ATOM 8495 N N . GLN D 1 178 ? 45.239 45.518 72.857 1.00 81.48 ? 177 GLN D N 1 +ATOM 8496 C CA . GLN D 1 178 ? 46.184 46.617 72.704 1.00 93.34 ? 177 GLN D CA 1 +ATOM 8497 C C . GLN D 1 178 ? 45.505 47.994 72.785 1.00 94.32 ? 177 GLN D C 1 +ATOM 8498 O O . GLN D 1 178 ? 44.683 48.332 71.944 1.00 101.06 ? 177 GLN D O 1 +ATOM 8499 C CB . GLN D 1 178 ? 46.920 46.461 71.375 1.00 74.01 ? 177 GLN D CB 1 +ATOM 8500 C CG . GLN D 1 178 ? 47.832 47.620 71.035 1.00 106.19 ? 177 GLN D CG 1 +ATOM 8501 C CD . GLN D 1 178 ? 49.062 47.669 71.908 1.00 94.57 ? 177 GLN D CD 1 +ATOM 8502 O OE1 . GLN D 1 178 ? 49.774 46.671 72.052 1.00 95.23 ? 177 GLN D OE1 1 +ATOM 8503 N NE2 . GLN D 1 178 ? 49.323 48.834 72.500 1.00 99.38 ? 177 GLN D NE2 1 +ATOM 8504 N N . LEU D 1 179 ? 45.843 48.796 73.788 1.00 89.84 ? 178 LEU D N 1 +ATOM 8505 C CA . LEU D 1 179 ? 45.162 50.083 73.945 1.00 79.75 ? 178 LEU D CA 1 +ATOM 8506 C C . LEU D 1 179 ? 45.784 51.146 73.049 1.00 76.08 ? 178 LEU D C 1 +ATOM 8507 O O . LEU D 1 179 ? 46.988 51.129 72.816 1.00 109.34 ? 178 LEU D O 1 +ATOM 8508 C CB . LEU D 1 179 ? 45.162 50.545 75.411 1.00 90.70 ? 178 LEU D CB 1 +ATOM 8509 C CG . LEU D 1 179 ? 44.387 49.728 76.460 1.00 111.91 ? 178 LEU D CG 1 +ATOM 8510 C CD1 . LEU D 1 179 ? 44.612 50.241 77.878 1.00 131.90 ? 178 LEU D CD1 1 +ATOM 8511 C CD2 . LEU D 1 179 ? 42.892 49.704 76.154 1.00 80.69 ? 178 LEU D CD2 1 +ATOM 8512 N N . ALA D 1 180 ? 44.962 52.067 72.550 1.00 73.44 ? 179 ALA D N 1 +ATOM 8513 C CA . ALA D 1 180 ? 45.454 53.148 71.691 1.00 87.52 ? 179 ALA D CA 1 +ATOM 8514 C C . ALA D 1 180 ? 44.944 54.536 72.093 1.00 86.89 ? 179 ALA D C 1 +ATOM 8515 O O . ALA D 1 180 ? 44.095 55.125 71.429 1.00 101.40 ? 179 ALA D O 1 +ATOM 8516 C CB . ALA D 1 180 ? 45.143 52.859 70.224 1.00 94.76 ? 179 ALA D CB 1 +ATOM 8517 N N . ASP D 1 181 ? 45.496 55.056 73.179 1.00 73.41 ? 180 ASP D N 1 +ATOM 8518 C CA . ASP D 1 181 ? 45.103 56.349 73.734 1.00 108.55 ? 180 ASP D CA 1 +ATOM 8519 C C . ASP D 1 181 ? 45.218 57.523 72.720 1.00 86.13 ? 180 ASP D C 1 +ATOM 8520 O O . ASP D 1 181 ? 46.317 57.935 72.351 1.00 94.79 ? 180 ASP D O 1 +ATOM 8521 C CB . ASP D 1 181 ? 45.940 56.591 75.000 1.00 102.58 ? 180 ASP D CB 1 +ATOM 8522 C CG . ASP D 1 181 ? 45.306 57.572 75.957 1.00 108.88 ? 180 ASP D CG 1 +ATOM 8523 O OD1 . ASP D 1 181 ? 44.452 58.374 75.535 1.00 134.61 ? 180 ASP D OD1 1 +ATOM 8524 O OD2 . ASP D 1 181 ? 45.688 57.548 77.143 1.00 126.17 ? 180 ASP D OD2 1 +ATOM 8525 N N . HIS D 1 182 ? 44.077 58.056 72.275 1.00 70.33 ? 181 HIS D N 1 +ATOM 8526 C CA . HIS D 1 182 ? 44.054 59.118 71.251 1.00 101.41 ? 181 HIS D CA 1 +ATOM 8527 C C . HIS D 1 182 ? 43.826 60.529 71.782 1.00 85.61 ? 181 HIS D C 1 +ATOM 8528 O O . HIS D 1 182 ? 42.827 60.779 72.451 1.00 80.07 ? 181 HIS D O 1 +ATOM 8529 C CB . HIS D 1 182 ? 42.922 58.892 70.247 1.00 85.77 ? 181 HIS D CB 1 +ATOM 8530 C CG . HIS D 1 182 ? 43.146 57.765 69.292 1.00 74.25 ? 181 HIS D CG 1 +ATOM 8531 N ND1 . HIS D 1 182 ? 43.200 56.449 69.693 1.00 89.56 ? 181 HIS D ND1 1 +ATOM 8532 C CD2 . HIS D 1 182 ? 43.275 57.754 67.944 1.00 64.80 ? 181 HIS D CD2 1 +ATOM 8533 C CE1 . HIS D 1 182 ? 43.382 55.678 68.636 1.00 91.73 ? 181 HIS D CE1 1 +ATOM 8534 N NE2 . HIS D 1 182 ? 43.426 56.444 67.563 1.00 79.46 ? 181 HIS D NE2 1 +ATOM 8535 N N . TYR D 1 183 ? 44.703 61.460 71.409 1.00 107.16 ? 182 TYR D N 1 +ATOM 8536 C CA . TYR D 1 183 ? 44.549 62.878 71.757 1.00 106.61 ? 182 TYR D CA 1 +ATOM 8537 C C . TYR D 1 183 ? 44.438 63.746 70.491 1.00 90.99 ? 182 TYR D C 1 +ATOM 8538 O O . TYR D 1 183 ? 45.426 63.955 69.785 1.00 123.98 ? 182 TYR D O 1 +ATOM 8539 C CB . TYR D 1 183 ? 45.714 63.351 72.650 1.00 85.34 ? 182 TYR D CB 1 +ATOM 8540 C CG . TYR D 1 183 ? 45.737 62.697 74.022 1.00 96.14 ? 182 TYR D CG 1 +ATOM 8541 C CD1 . TYR D 1 183 ? 46.177 61.389 74.181 1.00 101.46 ? 182 TYR D CD1 1 +ATOM 8542 C CD2 . TYR D 1 183 ? 45.313 63.383 75.154 1.00 68.28 ? 182 TYR D CD2 1 +ATOM 8543 C CE1 . TYR D 1 183 ? 46.194 60.777 75.426 1.00 92.34 ? 182 TYR D CE1 1 +ATOM 8544 C CE2 . TYR D 1 183 ? 45.325 62.779 76.407 1.00 105.17 ? 182 TYR D CE2 1 +ATOM 8545 C CZ . TYR D 1 183 ? 45.765 61.470 76.538 1.00 110.67 ? 182 TYR D CZ 1 +ATOM 8546 O OH . TYR D 1 183 ? 45.782 60.849 77.777 1.00 102.35 ? 182 TYR D OH 1 +ATOM 8547 N N . GLN D 1 184 ? 43.240 64.256 70.215 1.00 87.25 ? 183 GLN D N 1 +ATOM 8548 C CA . GLN D 1 184 ? 42.947 64.920 68.936 1.00 109.53 ? 183 GLN D CA 1 +ATOM 8549 C C . GLN D 1 184 ? 42.622 66.414 69.050 1.00 100.79 ? 183 GLN D C 1 +ATOM 8550 O O . GLN D 1 184 ? 42.104 66.870 70.067 1.00 92.49 ? 183 GLN D O 1 +ATOM 8551 C CB . GLN D 1 184 ? 41.783 64.197 68.249 1.00 105.44 ? 183 GLN D CB 1 +ATOM 8552 C CG . GLN D 1 184 ? 41.216 64.877 67.015 1.00 106.81 ? 183 GLN D CG 1 +ATOM 8553 C CD . GLN D 1 184 ? 39.978 64.178 66.516 1.00 113.87 ? 183 GLN D CD 1 +ATOM 8554 O OE1 . GLN D 1 184 ? 39.749 63.007 66.832 1.00 80.76 ? 183 GLN D OE1 1 +ATOM 8555 N NE2 . GLN D 1 184 ? 39.160 64.891 65.742 1.00 81.07 ? 183 GLN D NE2 1 +ATOM 8556 N N . GLN D 1 185 ? 42.914 67.179 68.004 1.00 88.18 ? 184 GLN D N 1 +ATOM 8557 C CA . GLN D 1 185 ? 42.485 68.569 67.987 1.00 92.41 ? 184 GLN D CA 1 +ATOM 8558 C C . GLN D 1 185 ? 42.156 69.102 66.590 1.00 123.42 ? 184 GLN D C 1 +ATOM 8559 O O . GLN D 1 185 ? 42.879 68.848 65.621 1.00 91.92 ? 184 GLN D O 1 +ATOM 8560 C CB . GLN D 1 185 ? 43.505 69.459 68.696 1.00 117.54 ? 184 GLN D CB 1 +ATOM 8561 C CG . GLN D 1 185 ? 44.856 69.539 68.024 1.00 152.83 ? 184 GLN D CG 1 +ATOM 8562 C CD . GLN D 1 185 ? 45.789 70.490 68.745 1.00 178.39 ? 184 GLN D CD 1 +ATOM 8563 O OE1 . GLN D 1 185 ? 45.592 70.800 69.922 1.00 184.47 ? 184 GLN D OE1 1 +ATOM 8564 N NE2 . GLN D 1 185 ? 46.808 70.967 68.039 1.00 187.73 ? 184 GLN D NE2 1 +ATOM 8565 N N . ASN D 1 186 ? 41.055 69.845 66.510 1.00 111.27 ? 185 ASN D N 1 +ATOM 8566 C CA . ASN D 1 186 ? 40.540 70.348 65.243 1.00 108.14 ? 185 ASN D CA 1 +ATOM 8567 C C . ASN D 1 186 ? 40.459 71.870 65.195 1.00 125.54 ? 185 ASN D C 1 +ATOM 8568 O O . ASN D 1 186 ? 40.229 72.517 66.220 1.00 102.80 ? 185 ASN D O 1 +ATOM 8569 C CB . ASN D 1 186 ? 39.175 69.734 64.961 1.00 100.42 ? 185 ASN D CB 1 +ATOM 8570 C CG . ASN D 1 186 ? 39.247 68.241 64.732 1.00 105.20 ? 185 ASN D CG 1 +ATOM 8571 O OD1 . ASN D 1 186 ? 39.248 67.447 65.676 1.00 103.44 ? 185 ASN D OD1 1 +ATOM 8572 N ND2 . ASN D 1 186 ? 39.305 67.848 63.470 1.00 90.40 ? 185 ASN D ND2 1 +ATOM 8573 N N . THR D 1 187 ? 40.643 72.421 63.994 1.00 113.15 ? 186 THR D N 1 +ATOM 8574 C CA . THR D 1 187 ? 40.811 73.863 63.784 1.00 116.48 ? 186 THR D CA 1 +ATOM 8575 C C . THR D 1 187 ? 40.523 74.297 62.343 1.00 102.13 ? 186 THR D C 1 +ATOM 8576 O O . THR D 1 187 ? 41.152 73.807 61.404 1.00 122.57 ? 186 THR D O 1 +ATOM 8577 C CB . THR D 1 187 ? 42.243 74.321 64.150 1.00 115.34 ? 186 THR D CB 1 +ATOM 8578 O OG1 . THR D 1 187 ? 42.377 74.380 65.576 1.00 133.42 ? 186 THR D OG1 1 +ATOM 8579 C CG2 . THR D 1 187 ? 42.547 75.701 63.545 1.00 98.74 ? 186 THR D CG2 1 +ATOM 8580 N N . PRO D 1 188 ? 39.581 75.241 62.172 1.00 116.69 ? 187 PRO D N 1 +ATOM 8581 C CA . PRO D 1 188 ? 39.173 75.737 60.852 1.00 123.50 ? 187 PRO D CA 1 +ATOM 8582 C C . PRO D 1 188 ? 40.260 76.471 60.070 1.00 123.46 ? 187 PRO D C 1 +ATOM 8583 O O . PRO D 1 188 ? 40.828 77.472 60.513 1.00 131.75 ? 187 PRO D O 1 +ATOM 8584 C CB . PRO D 1 188 ? 38.031 76.709 61.174 1.00 117.79 ? 187 PRO D CB 1 +ATOM 8585 C CG . PRO D 1 188 ? 38.264 77.121 62.599 1.00 111.02 ? 187 PRO D CG 1 +ATOM 8586 C CD . PRO D 1 188 ? 38.817 75.883 63.257 1.00 108.59 ? 187 PRO D CD 1 +ATOM 8587 N N . ILE D 1 189 ? 40.523 75.943 58.884 1.00 126.16 ? 188 ILE D N 1 +ATOM 8588 C CA . ILE D 1 189 ? 41.314 76.610 57.868 1.00 121.13 ? 188 ILE D CA 1 +ATOM 8589 C C . ILE D 1 189 ? 40.635 77.917 57.478 1.00 137.34 ? 188 ILE D C 1 +ATOM 8590 O O . ILE D 1 189 ? 41.299 78.920 57.207 1.00 131.21 ? 188 ILE D O 1 +ATOM 8591 C CB . ILE D 1 189 ? 41.401 75.706 56.634 1.00 101.06 ? 188 ILE D CB 1 +ATOM 8592 C CG1 . ILE D 1 189 ? 41.937 74.329 57.053 1.00 109.91 ? 188 ILE D CG1 1 +ATOM 8593 C CG2 . ILE D 1 189 ? 42.231 76.361 55.537 1.00 101.55 ? 188 ILE D CG2 1 +ATOM 8594 C CD1 . ILE D 1 189 ? 41.809 73.234 56.009 1.00 115.79 ? 188 ILE D CD1 1 +ATOM 8595 N N . GLY D 1 190 ? 39.304 77.893 57.465 1.00 147.14 ? 189 GLY D N 1 +ATOM 8596 C CA . GLY D 1 190 ? 38.497 79.030 57.057 1.00 149.68 ? 189 GLY D CA 1 +ATOM 8597 C C . GLY D 1 190 ? 38.365 80.127 58.098 1.00 158.11 ? 189 GLY D C 1 +ATOM 8598 O O . GLY D 1 190 ? 38.482 79.880 59.302 1.00 132.39 ? 189 GLY D O 1 +ATOM 8599 N N . ASP D 1 191 ? 38.110 81.346 57.627 1.00 157.10 ? 190 ASP D N 1 +ATOM 8600 C CA . ASP D 1 191 ? 38.072 82.515 58.504 1.00 166.54 ? 190 ASP D CA 1 +ATOM 8601 C C . ASP D 1 191 ? 36.664 82.801 59.029 1.00 162.60 ? 190 ASP D C 1 +ATOM 8602 O O . ASP D 1 191 ? 36.488 83.569 59.979 1.00 148.51 ? 190 ASP D O 1 +ATOM 8603 C CB . ASP D 1 191 ? 38.656 83.753 57.806 1.00 165.53 ? 190 ASP D CB 1 +ATOM 8604 C CG . ASP D 1 191 ? 40.142 83.612 57.489 1.00 179.22 ? 190 ASP D CG 1 +ATOM 8605 O OD1 . ASP D 1 191 ? 40.901 83.095 58.332 1.00 163.22 ? 190 ASP D OD1 1 +ATOM 8606 O OD2 . ASP D 1 191 ? 40.555 84.030 56.390 1.00 185.43 ? 190 ASP D OD2 1 +ATOM 8607 N N . GLY D 1 192 ? 35.669 82.170 58.411 1.00 164.98 ? 191 GLY D N 1 +ATOM 8608 C CA . GLY D 1 192 ? 34.286 82.293 58.844 1.00 164.31 ? 191 GLY D CA 1 +ATOM 8609 C C . GLY D 1 192 ? 34.007 81.609 60.172 1.00 176.17 ? 191 GLY D C 1 +ATOM 8610 O O . GLY D 1 192 ? 34.803 80.785 60.629 1.00 171.03 ? 191 GLY D O 1 +ATOM 8611 N N . PRO D 1 193 ? 32.867 81.943 60.801 1.00 179.36 ? 192 PRO D N 1 +ATOM 8612 C CA . PRO D 1 193 ? 32.538 81.410 62.128 1.00 178.37 ? 192 PRO D CA 1 +ATOM 8613 C C . PRO D 1 193 ? 32.081 79.955 62.084 1.00 167.32 ? 192 PRO D C 1 +ATOM 8614 O O . PRO D 1 193 ? 31.561 79.483 61.068 1.00 131.62 ? 192 PRO D O 1 +ATOM 8615 C CB . PRO D 1 193 ? 31.392 82.312 62.588 1.00 167.41 ? 192 PRO D CB 1 +ATOM 8616 C CG . PRO D 1 193 ? 30.717 82.708 61.328 1.00 153.28 ? 192 PRO D CG 1 +ATOM 8617 C CD . PRO D 1 193 ? 31.804 82.821 60.283 1.00 157.78 ? 192 PRO D CD 1 +ATOM 8618 N N . VAL D 1 194 ? 32.289 79.254 63.193 1.00 153.95 ? 193 VAL D N 1 +ATOM 8619 C CA . VAL D 1 194 ? 31.954 77.843 63.291 1.00 142.69 ? 193 VAL D CA 1 +ATOM 8620 C C . VAL D 1 194 ? 31.231 77.593 64.602 1.00 121.40 ? 193 VAL D C 1 +ATOM 8621 O O . VAL D 1 194 ? 31.285 78.414 65.509 1.00 123.21 ? 193 VAL D O 1 +ATOM 8622 C CB . VAL D 1 194 ? 33.215 76.957 63.237 1.00 150.24 ? 193 VAL D CB 1 +ATOM 8623 C CG1 . VAL D 1 194 ? 33.941 77.131 61.902 1.00 110.25 ? 193 VAL D CG1 1 +ATOM 8624 C CG2 . VAL D 1 194 ? 34.138 77.271 64.411 1.00 139.55 ? 193 VAL D CG2 1 +ATOM 8625 N N . LEU D 1 195 ? 30.555 76.457 64.699 1.00 111.18 ? 194 LEU D N 1 +ATOM 8626 C CA . LEU D 1 195 ? 29.812 76.111 65.901 1.00 103.53 ? 194 LEU D CA 1 +ATOM 8627 C C . LEU D 1 195 ? 30.755 75.546 66.944 1.00 111.74 ? 194 LEU D C 1 +ATOM 8628 O O . LEU D 1 195 ? 31.508 74.621 66.663 1.00 133.37 ? 194 LEU D O 1 +ATOM 8629 C CB . LEU D 1 195 ? 28.725 75.088 65.576 1.00 103.62 ? 194 LEU D CB 1 +ATOM 8630 C CG . LEU D 1 195 ? 27.763 75.508 64.462 1.00 119.85 ? 194 LEU D CG 1 +ATOM 8631 C CD1 . LEU D 1 195 ? 26.688 74.449 64.260 1.00 112.21 ? 194 LEU D CD1 1 +ATOM 8632 C CD2 . LEU D 1 195 ? 27.154 76.885 64.739 1.00 85.78 ? 194 LEU D CD2 1 +ATOM 8633 N N . LEU D 1 196 ? 30.723 76.102 68.146 1.00 99.91 ? 195 LEU D N 1 +ATOM 8634 C CA . LEU D 1 196 ? 31.581 75.601 69.207 1.00 129.97 ? 195 LEU D CA 1 +ATOM 8635 C C . LEU D 1 196 ? 30.734 74.879 70.252 1.00 117.85 ? 195 LEU D C 1 +ATOM 8636 O O . LEU D 1 196 ? 30.101 75.514 71.089 1.00 124.99 ? 195 LEU D O 1 +ATOM 8637 C CB . LEU D 1 196 ? 32.412 76.740 69.801 1.00 155.93 ? 195 LEU D CB 1 +ATOM 8638 C CG . LEU D 1 196 ? 33.157 77.526 68.710 1.00 135.20 ? 195 LEU D CG 1 +ATOM 8639 C CD1 . LEU D 1 196 ? 33.923 78.716 69.265 1.00 120.72 ? 195 LEU D CD1 1 +ATOM 8640 C CD2 . LEU D 1 196 ? 34.089 76.617 67.921 1.00 114.82 ? 195 LEU D CD2 1 +ATOM 8641 N N . PRO D 1 197 ? 30.726 73.536 70.192 1.00 117.79 ? 196 PRO D N 1 +ATOM 8642 C CA . PRO D 1 197 ? 29.793 72.640 70.894 1.00 121.79 ? 196 PRO D CA 1 +ATOM 8643 C C . PRO D 1 197 ? 29.873 72.596 72.422 1.00 117.48 ? 196 PRO D C 1 +ATOM 8644 O O . PRO D 1 197 ? 30.886 72.949 73.026 1.00 119.68 ? 196 PRO D O 1 +ATOM 8645 C CB . PRO D 1 197 ? 30.156 71.255 70.339 1.00 114.76 ? 196 PRO D CB 1 +ATOM 8646 C CG . PRO D 1 197 ? 31.572 71.382 69.896 1.00 110.62 ? 196 PRO D CG 1 +ATOM 8647 C CD . PRO D 1 197 ? 31.695 72.785 69.374 1.00 102.72 ? 196 PRO D CD 1 +ATOM 8648 N N . ASP D 1 198 ? 28.776 72.155 73.030 1.00 129.55 ? 197 ASP D N 1 +ATOM 8649 C CA . ASP D 1 198 ? 28.779 71.736 74.423 1.00 135.30 ? 197 ASP D CA 1 +ATOM 8650 C C . ASP D 1 198 ? 29.327 70.317 74.435 1.00 115.66 ? 197 ASP D C 1 +ATOM 8651 O O . ASP D 1 198 ? 29.381 69.664 73.394 1.00 112.11 ? 197 ASP D O 1 +ATOM 8652 C CB . ASP D 1 198 ? 27.361 71.766 75.014 1.00 139.00 ? 197 ASP D CB 1 +ATOM 8653 C CG . ASP D 1 198 ? 26.828 73.186 75.212 1.00 150.52 ? 197 ASP D CG 1 +ATOM 8654 O OD1 . ASP D 1 198 ? 27.642 74.135 75.199 1.00 147.22 ? 197 ASP D OD1 1 +ATOM 8655 O OD2 . ASP D 1 198 ? 25.597 73.349 75.392 1.00 133.45 ? 197 ASP D OD2 1 +ATOM 8656 N N . ASN D 1 199 ? 29.743 69.845 75.602 1.00 105.80 ? 198 ASN D N 1 +ATOM 8657 C CA . ASN D 1 199 ? 30.244 68.484 75.737 1.00 123.69 ? 198 ASN D CA 1 +ATOM 8658 C C . ASN D 1 199 ? 29.255 67.439 75.237 1.00 119.35 ? 198 ASN D C 1 +ATOM 8659 O O . ASN D 1 199 ? 28.127 67.370 75.721 1.00 112.65 ? 198 ASN D O 1 +ATOM 8660 C CB . ASN D 1 199 ? 30.572 68.185 77.200 1.00 143.41 ? 198 ASN D CB 1 +ATOM 8661 C CG . ASN D 1 199 ? 31.766 68.967 77.704 1.00 142.60 ? 198 ASN D CG 1 +ATOM 8662 O OD1 . ASN D 1 199 ? 32.185 69.958 77.096 1.00 89.17 ? 198 ASN D OD1 1 +ATOM 8663 N ND2 . ASN D 1 199 ? 32.323 68.525 78.829 1.00 139.81 ? 198 ASN D ND2 1 +ATOM 8664 N N . HIS D 1 200 ? 29.685 66.635 74.268 1.00 112.07 ? 199 HIS D N 1 +ATOM 8665 C CA . HIS D 1 200 ? 28.934 65.453 73.838 1.00 110.09 ? 199 HIS D CA 1 +ATOM 8666 C C . HIS D 1 200 ? 29.909 64.416 73.317 1.00 99.23 ? 199 HIS D C 1 +ATOM 8667 O O . HIS D 1 200 ? 31.115 64.624 73.378 1.00 107.60 ? 199 HIS D O 1 +ATOM 8668 C CB . HIS D 1 200 ? 27.920 65.795 72.752 1.00 95.82 ? 199 HIS D CB 1 +ATOM 8669 C CG . HIS D 1 200 ? 28.535 66.263 71.471 1.00 95.87 ? 199 HIS D CG 1 +ATOM 8670 N ND1 . HIS D 1 200 ? 29.114 67.506 71.339 1.00 109.66 ? 199 HIS D ND1 1 +ATOM 8671 C CD2 . HIS D 1 200 ? 28.649 65.664 70.263 1.00 101.37 ? 199 HIS D CD2 1 +ATOM 8672 C CE1 . HIS D 1 200 ? 29.564 67.651 70.105 1.00 107.91 ? 199 HIS D CE1 1 +ATOM 8673 N NE2 . HIS D 1 200 ? 29.292 66.548 69.431 1.00 110.58 ? 199 HIS D NE2 1 +ATOM 8674 N N . TYR D 1 201 ? 29.397 63.304 72.801 1.00 80.65 ? 200 TYR D N 1 +ATOM 8675 C CA . TYR D 1 201 ? 30.269 62.268 72.252 1.00 93.85 ? 200 TYR D CA 1 +ATOM 8676 C C . TYR D 1 201 ? 29.740 61.708 70.916 1.00 95.65 ? 200 TYR D C 1 +ATOM 8677 O O . TYR D 1 201 ? 28.610 62.005 70.542 1.00 94.14 ? 200 TYR D O 1 +ATOM 8678 C CB . TYR D 1 201 ? 30.505 61.177 73.302 1.00 90.38 ? 200 TYR D CB 1 +ATOM 8679 C CG . TYR D 1 201 ? 29.305 60.319 73.627 1.00 105.70 ? 200 TYR D CG 1 +ATOM 8680 C CD1 . TYR D 1 201 ? 28.351 60.730 74.552 1.00 106.07 ? 200 TYR D CD1 1 +ATOM 8681 C CD2 . TYR D 1 201 ? 29.136 59.082 73.023 1.00 106.95 ? 200 TYR D CD2 1 +ATOM 8682 C CE1 . TYR D 1 201 ? 27.250 59.928 74.857 1.00 101.90 ? 200 TYR D CE1 1 +ATOM 8683 C CE2 . TYR D 1 201 ? 28.040 58.276 73.319 1.00 119.66 ? 200 TYR D CE2 1 +ATOM 8684 C CZ . TYR D 1 201 ? 27.100 58.705 74.236 1.00 108.34 ? 200 TYR D CZ 1 +ATOM 8685 O OH . TYR D 1 201 ? 26.011 57.912 74.532 1.00 102.20 ? 200 TYR D OH 1 +ATOM 8686 N N . LEU D 1 202 ? 30.564 60.959 70.177 1.00 96.91 ? 201 LEU D N 1 +ATOM 8687 C CA . LEU D 1 202 ? 30.113 60.286 68.947 1.00 100.62 ? 201 LEU D CA 1 +ATOM 8688 C C . LEU D 1 202 ? 30.205 58.790 69.169 1.00 81.44 ? 201 LEU D C 1 +ATOM 8689 O O . LEU D 1 202 ? 31.254 58.276 69.516 1.00 70.01 ? 201 LEU D O 1 +ATOM 8690 C CB . LEU D 1 202 ? 30.949 60.669 67.711 1.00 70.44 ? 201 LEU D CB 1 +ATOM 8691 C CG . LEU D 1 202 ? 31.085 62.114 67.201 1.00 96.61 ? 201 LEU D CG 1 +ATOM 8692 C CD1 . LEU D 1 202 ? 31.663 62.184 65.786 1.00 79.97 ? 201 LEU D CD1 1 +ATOM 8693 C CD2 . LEU D 1 202 ? 29.774 62.878 67.265 1.00 112.35 ? 201 LEU D CD2 1 +ATOM 8694 N N . SER D 1 203 ? 29.103 58.086 68.998 1.00 81.70 ? 202 SER D N 1 +ATOM 8695 C CA . SER D 1 203 ? 29.136 56.656 69.200 1.00 86.71 ? 202 SER D CA 1 +ATOM 8696 C C . SER D 1 203 ? 29.521 56.059 67.868 1.00 73.95 ? 202 SER D C 1 +ATOM 8697 O O . SER D 1 203 ? 28.761 56.161 66.904 1.00 107.51 ? 202 SER D O 1 +ATOM 8698 C CB . SER D 1 203 ? 27.766 56.155 69.653 1.00 67.37 ? 202 SER D CB 1 +ATOM 8699 O OG . SER D 1 203 ? 27.666 54.750 69.554 1.00 105.11 ? 202 SER D OG 1 +ATOM 8700 N N . THR D 1 204 ? 30.706 55.461 67.806 1.00 88.36 ? 203 THR D N 1 +ATOM 8701 C CA . THR D 1 204 ? 31.190 54.871 66.564 1.00 99.87 ? 203 THR D CA 1 +ATOM 8702 C C . THR D 1 204 ? 31.113 53.348 66.577 1.00 93.61 ? 203 THR D C 1 +ATOM 8703 O O . THR D 1 204 ? 31.308 52.718 67.616 1.00 99.15 ? 203 THR D O 1 +ATOM 8704 C CB . THR D 1 204 ? 32.639 55.278 66.241 1.00 93.85 ? 203 THR D CB 1 +ATOM 8705 O OG1 . THR D 1 204 ? 32.804 56.688 66.432 1.00 83.78 ? 203 THR D OG1 1 +ATOM 8706 C CG2 . THR D 1 204 ? 32.952 54.945 64.793 1.00 137.45 ? 203 THR D CG2 1 +ATOM 8707 N N . GLN D 1 205 ? 30.790 52.778 65.415 1.00 88.79 ? 204 GLN D N 1 +ATOM 8708 C CA . GLN D 1 205 ? 30.906 51.344 65.150 1.00 87.80 ? 204 GLN D CA 1 +ATOM 8709 C C . GLN D 1 205 ? 31.480 51.131 63.751 1.00 90.17 ? 204 GLN D C 1 +ATOM 8710 O O . GLN D 1 205 ? 31.144 51.858 62.813 1.00 65.65 ? 204 GLN D O 1 +ATOM 8711 C CB . GLN D 1 205 ? 29.555 50.636 65.238 1.00 88.48 ? 204 GLN D CB 1 +ATOM 8712 C CG . GLN D 1 205 ? 28.772 50.915 66.489 1.00 71.98 ? 204 GLN D CG 1 +ATOM 8713 C CD . GLN D 1 205 ? 27.314 51.110 66.189 1.00 100.56 ? 204 GLN D CD 1 +ATOM 8714 O OE1 . GLN D 1 205 ? 26.564 50.140 66.061 1.00 146.31 ? 204 GLN D OE1 1 +ATOM 8715 N NE2 . GLN D 1 205 ? 26.898 52.371 66.052 1.00 96.69 ? 204 GLN D NE2 1 +ATOM 8716 N N . SER D 1 206 ? 32.329 50.112 63.629 1.00 74.91 ? 205 SER D N 1 +ATOM 8717 C CA . SER D 1 206 ? 33.098 49.848 62.417 1.00 64.54 ? 205 SER D CA 1 +ATOM 8718 C C . SER D 1 206 ? 33.261 48.339 62.208 1.00 53.90 ? 205 SER D C 1 +ATOM 8719 O O . SER D 1 206 ? 33.255 47.576 63.175 1.00 93.10 ? 205 SER D O 1 +ATOM 8720 C CB . SER D 1 206 ? 34.475 50.521 62.503 1.00 67.84 ? 205 SER D CB 1 +ATOM 8721 O OG . SER D 1 206 ? 34.355 51.930 62.638 1.00 108.04 ? 205 SER D OG 1 +ATOM 8722 N N . ASN D 1 207 ? 33.346 47.915 60.945 1.00 69.99 ? 206 ASN D N 1 +ATOM 8723 C CA . ASN D 1 207 ? 33.798 46.566 60.591 1.00 73.59 ? 206 ASN D CA 1 +ATOM 8724 C C . ASN D 1 207 ? 34.780 46.616 59.424 1.00 95.00 ? 206 ASN D C 1 +ATOM 8725 O O . ASN D 1 207 ? 34.662 47.472 58.536 1.00 67.52 ? 206 ASN D O 1 +ATOM 8726 C CB . ASN D 1 207 ? 32.630 45.596 60.321 1.00 64.31 ? 206 ASN D CB 1 +ATOM 8727 C CG . ASN D 1 207 ? 32.753 44.849 58.988 1.00 73.92 ? 206 ASN D CG 1 +ATOM 8728 O OD1 . ASN D 1 207 ? 32.917 45.455 57.933 1.00 62.82 ? 206 ASN D OD1 1 +ATOM 8729 N ND2 . ASN D 1 207 ? 32.627 43.525 59.036 1.00 51.80 ? 206 ASN D ND2 1 +ATOM 8730 N N . LEU D 1 208 ? 35.727 45.680 59.427 1.00 71.78 ? 207 LEU D N 1 +ATOM 8731 C CA . LEU D 1 208 ? 36.783 45.631 58.431 1.00 51.94 ? 207 LEU D CA 1 +ATOM 8732 C C . LEU D 1 208 ? 36.668 44.374 57.593 1.00 51.99 ? 207 LEU D C 1 +ATOM 8733 O O . LEU D 1 208 ? 36.512 43.275 58.131 1.00 87.49 ? 207 LEU D O 1 +ATOM 8734 C CB . LEU D 1 208 ? 38.139 45.632 59.123 1.00 80.47 ? 207 LEU D CB 1 +ATOM 8735 C CG . LEU D 1 208 ? 38.283 46.582 60.305 1.00 64.08 ? 207 LEU D CG 1 +ATOM 8736 C CD1 . LEU D 1 208 ? 39.565 46.244 61.022 1.00 83.87 ? 207 LEU D CD1 1 +ATOM 8737 C CD2 . LEU D 1 208 ? 38.268 48.039 59.865 1.00 65.37 ? 207 LEU D CD2 1 +ATOM 8738 N N . SER D 1 209 ? 36.776 44.548 56.274 1.00 78.61 ? 208 SER D N 1 +ATOM 8739 C CA . SER D 1 209 ? 36.607 43.460 55.303 1.00 61.30 ? 208 SER D CA 1 +ATOM 8740 C C . SER D 1 209 ? 37.564 43.493 54.098 1.00 88.28 ? 208 SER D C 1 +ATOM 8741 O O . SER D 1 209 ? 38.295 44.470 53.869 1.00 63.04 ? 208 SER D O 1 +ATOM 8742 C CB . SER D 1 209 ? 35.172 43.445 54.787 1.00 63.09 ? 208 SER D CB 1 +ATOM 8743 O OG . SER D 1 209 ? 34.738 44.765 54.508 1.00 87.97 ? 208 SER D OG 1 +ATOM 8744 N N . LYS D 1 210 ? 37.531 42.404 53.331 1.00 84.13 ? 209 LYS D N 1 +ATOM 8745 C CA . LYS D 1 210 ? 38.298 42.272 52.095 1.00 64.43 ? 209 LYS D CA 1 +ATOM 8746 C C . LYS D 1 210 ? 37.395 42.143 50.864 1.00 82.27 ? 209 LYS D C 1 +ATOM 8747 O O . LYS D 1 210 ? 36.439 41.373 50.865 1.00 91.48 ? 209 LYS D O 1 +ATOM 8748 C CB . LYS D 1 210 ? 39.190 41.021 52.140 1.00 86.98 ? 209 LYS D CB 1 +ATOM 8749 C CG . LYS D 1 210 ? 40.231 40.962 53.250 1.00 76.88 ? 209 LYS D CG 1 +ATOM 8750 C CD . LYS D 1 210 ? 41.282 42.034 53.091 1.00 86.42 ? 209 LYS D CD 1 +ATOM 8751 C CE . LYS D 1 210 ? 42.421 41.811 54.061 1.00 72.48 ? 209 LYS D CE 1 +ATOM 8752 N NZ . LYS D 1 210 ? 43.171 43.070 54.242 1.00 76.86 ? 209 LYS D NZ 1 +ATOM 8753 N N . ASP D 1 211 ? 37.729 42.895 49.818 1.00 96.02 ? 210 ASP D N 1 +ATOM 8754 C CA . ASP D 1 211 ? 37.248 42.686 48.448 1.00 71.10 ? 210 ASP D CA 1 +ATOM 8755 C C . ASP D 1 211 ? 37.873 41.432 47.823 1.00 84.64 ? 210 ASP D C 1 +ATOM 8756 O O . ASP D 1 211 ? 39.092 41.290 47.805 1.00 92.80 ? 210 ASP D O 1 +ATOM 8757 C CB . ASP D 1 211 ? 37.660 43.895 47.610 1.00 74.49 ? 210 ASP D CB 1 +ATOM 8758 C CG . ASP D 1 211 ? 36.992 43.933 46.258 1.00 105.92 ? 210 ASP D CG 1 +ATOM 8759 O OD1 . ASP D 1 211 ? 36.494 42.884 45.804 1.00 100.72 ? 210 ASP D OD1 1 +ATOM 8760 O OD2 . ASP D 1 211 ? 36.970 45.025 45.646 1.00 99.37 ? 210 ASP D OD2 1 +ATOM 8761 N N . PRO D 1 212 ? 37.047 40.525 47.281 1.00 103.42 ? 211 PRO D N 1 +ATOM 8762 C CA . PRO D 1 212 ? 37.621 39.296 46.711 1.00 103.54 ? 211 PRO D CA 1 +ATOM 8763 C C . PRO D 1 212 ? 38.088 39.388 45.236 1.00 106.67 ? 211 PRO D C 1 +ATOM 8764 O O . PRO D 1 212 ? 38.513 38.379 44.667 1.00 85.40 ? 211 PRO D O 1 +ATOM 8765 C CB . PRO D 1 212 ? 36.476 38.294 46.857 1.00 99.36 ? 211 PRO D CB 1 +ATOM 8766 C CG . PRO D 1 212 ? 35.240 39.143 46.721 1.00 98.85 ? 211 PRO D CG 1 +ATOM 8767 C CD . PRO D 1 212 ? 35.575 40.463 47.372 1.00 80.25 ? 211 PRO D CD 1 +ATOM 8768 N N . ASN D 1 213 ? 38.003 40.570 44.629 1.00 129.67 ? 212 ASN D N 1 +ATOM 8769 C CA . ASN D 1 213 ? 38.519 40.787 43.272 1.00 141.51 ? 212 ASN D CA 1 +ATOM 8770 C C . ASN D 1 213 ? 39.603 41.863 43.309 1.00 123.51 ? 212 ASN D C 1 +ATOM 8771 O O . ASN D 1 213 ? 39.820 42.616 42.354 1.00 108.79 ? 212 ASN D O 1 +ATOM 8772 C CB . ASN D 1 213 ? 37.396 41.185 42.310 1.00 119.30 ? 212 ASN D CB 1 +ATOM 8773 C CG . ASN D 1 213 ? 36.170 40.302 42.444 1.00 103.57 ? 212 ASN D CG 1 +ATOM 8774 O OD1 . ASN D 1 213 ? 36.254 39.070 42.420 1.00 98.80 ? 212 ASN D OD1 1 +ATOM 8775 N ND2 . ASN D 1 213 ? 35.017 40.935 42.600 1.00 110.95 ? 212 ASN D ND2 1 +ATOM 8776 N N . GLU D 1 214 ? 40.274 41.925 44.448 1.00 103.45 ? 213 GLU D N 1 +ATOM 8777 C CA . GLU D 1 214 ? 41.291 42.915 44.692 1.00 81.88 ? 213 GLU D CA 1 +ATOM 8778 C C . GLU D 1 214 ? 42.506 42.203 45.226 1.00 83.14 ? 213 GLU D C 1 +ATOM 8779 O O . GLU D 1 214 ? 42.426 41.555 46.267 1.00 90.23 ? 213 GLU D O 1 +ATOM 8780 C CB . GLU D 1 214 ? 40.813 43.906 45.735 1.00 79.73 ? 213 GLU D CB 1 +ATOM 8781 C CG . GLU D 1 214 ? 41.851 44.920 46.041 1.00 72.70 ? 213 GLU D CG 1 +ATOM 8782 C CD . GLU D 1 214 ? 42.398 45.527 44.780 1.00 107.71 ? 213 GLU D CD 1 +ATOM 8783 O OE1 . GLU D 1 214 ? 41.814 46.520 44.305 1.00 88.38 ? 213 GLU D OE1 1 +ATOM 8784 O OE2 . GLU D 1 214 ? 43.404 45.006 44.256 1.00 124.75 ? 213 GLU D OE2 1 +ATOM 8785 N N . LYS D 1 215 ? 43.626 42.322 44.519 1.00 96.10 ? 214 LYS D N 1 +ATOM 8786 C CA . LYS D 1 215 ? 44.808 41.514 44.825 1.00 107.96 ? 214 LYS D CA 1 +ATOM 8787 C C . LYS D 1 215 ? 45.951 42.305 45.467 1.00 94.59 ? 214 LYS D C 1 +ATOM 8788 O O . LYS D 1 215 ? 46.862 41.718 46.051 1.00 95.85 ? 214 LYS D O 1 +ATOM 8789 C CB . LYS D 1 215 ? 45.290 40.735 43.588 1.00 83.53 ? 214 LYS D CB 1 +ATOM 8790 C CG . LYS D 1 215 ? 44.255 39.760 43.019 1.00 135.29 ? 214 LYS D CG 1 +ATOM 8791 C CD . LYS D 1 215 ? 44.870 38.787 42.003 1.00 143.72 ? 214 LYS D CD 1 +ATOM 8792 C CE . LYS D 1 215 ? 45.061 39.401 40.617 1.00 133.73 ? 214 LYS D CE 1 +ATOM 8793 N NZ . LYS D 1 215 ? 43.772 39.611 39.916 1.00 120.10 ? 214 LYS D NZ 1 +ATOM 8794 N N . ARG D 1 216 ? 45.892 43.630 45.363 1.00 61.37 ? 215 ARG D N 1 +ATOM 8795 C CA . ARG D 1 216 ? 46.789 44.509 46.114 1.00 78.64 ? 215 ARG D CA 1 +ATOM 8796 C C . ARG D 1 216 ? 46.415 44.528 47.608 1.00 71.38 ? 215 ARG D C 1 +ATOM 8797 O O . ARG D 1 216 ? 45.295 44.175 47.968 1.00 94.93 ? 215 ARG D O 1 +ATOM 8798 C CB . ARG D 1 216 ? 46.724 45.927 45.536 1.00 73.44 ? 215 ARG D CB 1 +ATOM 8799 C CG . ARG D 1 216 ? 47.196 46.052 44.083 1.00 97.92 ? 215 ARG D CG 1 +ATOM 8800 C CD . ARG D 1 216 ? 46.734 47.356 43.469 1.00 87.00 ? 215 ARG D CD 1 +ATOM 8801 N NE . ARG D 1 216 ? 45.315 47.331 43.155 1.00 113.00 ? 215 ARG D NE 1 +ATOM 8802 C CZ . ARG D 1 216 ? 44.616 48.331 42.621 1.00 108.74 ? 215 ARG D CZ 1 +ATOM 8803 N NH1 . ARG D 1 216 ? 45.199 49.487 42.318 1.00 98.49 ? 215 ARG D NH1 1 +ATOM 8804 N NH2 . ARG D 1 216 ? 43.320 48.165 42.393 1.00 80.20 ? 215 ARG D NH2 1 +ATOM 8805 N N . ASP D 1 217 ? 47.339 44.940 48.478 1.00 72.81 ? 216 ASP D N 1 +ATOM 8806 C CA . ASP D 1 217 ? 47.048 45.026 49.920 1.00 91.81 ? 216 ASP D CA 1 +ATOM 8807 C C . ASP D 1 217 ? 45.999 46.120 50.202 1.00 100.65 ? 216 ASP D C 1 +ATOM 8808 O O . ASP D 1 217 ? 46.206 47.304 49.893 1.00 83.67 ? 216 ASP D O 1 +ATOM 8809 C CB . ASP D 1 217 ? 48.338 45.248 50.734 1.00 85.96 ? 216 ASP D CB 1 +ATOM 8810 C CG . ASP D 1 217 ? 48.257 44.686 52.163 1.00 113.09 ? 216 ASP D CG 1 +ATOM 8811 O OD1 . ASP D 1 217 ? 47.401 43.815 52.428 1.00 122.37 ? 216 ASP D OD1 1 +ATOM 8812 O OD2 . ASP D 1 217 ? 49.069 45.108 53.021 1.00 75.04 ? 216 ASP D OD2 1 +ATOM 8813 N N . HIS D 1 218 ? 44.874 45.712 50.789 1.00 91.57 ? 217 HIS D N 1 +ATOM 8814 C CA . HIS D 1 218 ? 43.709 46.591 50.900 1.00 80.89 ? 217 HIS D CA 1 +ATOM 8815 C C . HIS D 1 218 ? 42.810 46.341 52.128 1.00 66.56 ? 217 HIS D C 1 +ATOM 8816 O O . HIS D 1 218 ? 42.782 45.248 52.704 1.00 87.07 ? 217 HIS D O 1 +ATOM 8817 C CB . HIS D 1 218 ? 42.869 46.506 49.613 1.00 66.19 ? 217 HIS D CB 1 +ATOM 8818 C CG . HIS D 1 218 ? 42.034 45.272 49.528 1.00 63.89 ? 217 HIS D CG 1 +ATOM 8819 N ND1 . HIS D 1 218 ? 42.580 44.009 49.465 1.00 107.75 ? 217 HIS D ND1 1 +ATOM 8820 C CD2 . HIS D 1 218 ? 40.693 45.100 49.529 1.00 80.61 ? 217 HIS D CD2 1 +ATOM 8821 C CE1 . HIS D 1 218 ? 41.612 43.112 49.426 1.00 76.67 ? 217 HIS D CE1 1 +ATOM 8822 N NE2 . HIS D 1 218 ? 40.457 43.749 49.465 1.00 91.40 ? 217 HIS D NE2 1 +ATOM 8823 N N . MET D 1 219 ? 42.070 47.377 52.512 1.00 73.57 ? 218 MET D N 1 +ATOM 8824 C CA . MET D 1 219 ? 41.032 47.267 53.535 1.00 70.34 ? 218 MET D CA 1 +ATOM 8825 C C . MET D 1 219 ? 39.727 47.910 53.060 1.00 76.33 ? 218 MET D C 1 +ATOM 8826 O O . MET D 1 219 ? 39.738 49.060 52.596 1.00 76.78 ? 218 MET D O 1 +ATOM 8827 C CB . MET D 1 219 ? 41.492 47.944 54.831 1.00 73.40 ? 218 MET D CB 1 +ATOM 8828 C CG . MET D 1 219 ? 40.435 48.058 55.902 1.00 52.14 ? 218 MET D CG 1 +ATOM 8829 S SD . MET D 1 219 ? 40.989 48.932 57.372 1.00 76.40 ? 218 MET D SD 1 +ATOM 8830 C CE . MET D 1 219 ? 41.080 50.628 56.809 1.00 70.44 ? 218 MET D CE 1 +ATOM 8831 N N . VAL D 1 220 ? 38.622 47.159 53.170 1.00 78.12 ? 219 VAL D N 1 +ATOM 8832 C CA . VAL D 1 220 ? 37.256 47.701 53.056 1.00 66.59 ? 219 VAL D CA 1 +ATOM 8833 C C . VAL D 1 220 ? 36.749 48.152 54.433 1.00 57.26 ? 219 VAL D C 1 +ATOM 8834 O O . VAL D 1 220 ? 36.528 47.322 55.327 1.00 75.83 ? 219 VAL D O 1 +ATOM 8835 C CB . VAL D 1 220 ? 36.222 46.675 52.496 1.00 69.04 ? 219 VAL D CB 1 +ATOM 8836 C CG1 . VAL D 1 220 ? 35.004 47.398 51.980 1.00 52.92 ? 219 VAL D CG1 1 +ATOM 8837 C CG2 . VAL D 1 220 ? 36.809 45.797 51.390 1.00 80.41 ? 219 VAL D CG2 1 +ATOM 8838 N N . LEU D 1 221 ? 36.558 49.464 54.588 1.00 78.76 ? 220 LEU D N 1 +ATOM 8839 C CA . LEU D 1 221 ? 36.153 50.074 55.863 1.00 74.98 ? 220 LEU D CA 1 +ATOM 8840 C C . LEU D 1 221 ? 34.711 50.577 55.876 1.00 74.10 ? 220 LEU D C 1 +ATOM 8841 O O . LEU D 1 221 ? 34.377 51.505 55.144 1.00 90.06 ? 220 LEU D O 1 +ATOM 8842 C CB . LEU D 1 221 ? 37.063 51.259 56.214 1.00 66.55 ? 220 LEU D CB 1 +ATOM 8843 C CG . LEU D 1 221 ? 36.597 52.079 57.423 1.00 64.60 ? 220 LEU D CG 1 +ATOM 8844 C CD1 . LEU D 1 221 ? 36.607 51.209 58.664 1.00 69.54 ? 220 LEU D CD1 1 +ATOM 8845 C CD2 . LEU D 1 221 ? 37.424 53.338 57.644 1.00 74.10 ? 220 LEU D CD2 1 +ATOM 8846 N N . LEU D 1 222 ? 33.879 49.977 56.730 1.00 124.36 ? 221 LEU D N 1 +ATOM 8847 C CA . LEU D 1 222 ? 32.518 50.463 57.004 1.00 82.15 ? 221 LEU D CA 1 +ATOM 8848 C C . LEU D 1 222 ? 32.360 51.046 58.407 1.00 94.69 ? 221 LEU D C 1 +ATOM 8849 O O . LEU D 1 222 ? 32.447 50.328 59.402 1.00 81.17 ? 221 LEU D O 1 +ATOM 8850 C CB . LEU D 1 222 ? 31.494 49.344 56.836 1.00 73.54 ? 221 LEU D CB 1 +ATOM 8851 C CG . LEU D 1 222 ? 31.312 48.783 55.432 1.00 97.19 ? 221 LEU D CG 1 +ATOM 8852 C CD1 . LEU D 1 222 ? 30.371 47.580 55.438 1.00 57.23 ? 221 LEU D CD1 1 +ATOM 8853 C CD2 . LEU D 1 222 ? 30.776 49.894 54.551 1.00 86.32 ? 221 LEU D CD2 1 +ATOM 8854 N N . GLU D 1 223 ? 32.106 52.351 58.463 1.00 73.28 ? 222 GLU D N 1 +ATOM 8855 C CA . GLU D 1 223 ? 31.860 53.067 59.710 1.00 82.20 ? 222 GLU D CA 1 +ATOM 8856 C C . GLU D 1 223 ? 30.402 53.472 59.903 1.00 80.11 ? 222 GLU D C 1 +ATOM 8857 O O . GLU D 1 223 ? 29.743 53.911 58.959 1.00 83.95 ? 222 GLU D O 1 +ATOM 8858 C CB . GLU D 1 223 ? 32.703 54.337 59.751 1.00 71.38 ? 222 GLU D CB 1 +ATOM 8859 C CG . GLU D 1 223 ? 34.000 54.181 60.501 1.00 127.49 ? 222 GLU D CG 1 +ATOM 8860 C CD . GLU D 1 223 ? 34.748 55.492 60.666 1.00 159.93 ? 222 GLU D CD 1 +ATOM 8861 O OE1 . GLU D 1 223 ? 34.093 56.560 60.675 1.00 155.22 ? 222 GLU D OE1 1 +ATOM 8862 O OE2 . GLU D 1 223 ? 35.995 55.446 60.782 1.00 159.57 ? 222 GLU D OE2 1 +ATOM 8863 N N . PHE D 1 224 ? 29.915 53.334 61.136 1.00 96.28 ? 223 PHE D N 1 +ATOM 8864 C CA . PHE D 1 224 ? 28.652 53.942 61.563 1.00 70.99 ? 223 PHE D CA 1 +ATOM 8865 C C . PHE D 1 224 ? 28.960 55.013 62.613 1.00 57.67 ? 223 PHE D C 1 +ATOM 8866 O O . PHE D 1 224 ? 29.718 54.767 63.541 1.00 91.47 ? 223 PHE D O 1 +ATOM 8867 C CB . PHE D 1 224 ? 27.718 52.901 62.184 1.00 74.08 ? 223 PHE D CB 1 +ATOM 8868 C CG . PHE D 1 224 ? 27.384 51.748 61.278 1.00 90.14 ? 223 PHE D CG 1 +ATOM 8869 C CD1 . PHE D 1 224 ? 27.525 51.850 59.897 1.00 81.21 ? 223 PHE D CD1 1 +ATOM 8870 C CD2 . PHE D 1 224 ? 26.914 50.554 61.818 1.00 68.87 ? 223 PHE D CD2 1 +ATOM 8871 C CE1 . PHE D 1 224 ? 27.216 50.778 59.069 1.00 73.21 ? 223 PHE D CE1 1 +ATOM 8872 C CE2 . PHE D 1 224 ? 26.599 49.477 61.000 1.00 84.30 ? 223 PHE D CE2 1 +ATOM 8873 C CZ . PHE D 1 224 ? 26.748 49.591 59.621 1.00 96.47 ? 223 PHE D CZ 1 +ATOM 8874 N N . VAL D 1 225 ? 28.402 56.209 62.473 1.00 81.68 ? 224 VAL D N 1 +ATOM 8875 C CA . VAL D 1 225 ? 28.679 57.260 63.452 1.00 81.51 ? 224 VAL D CA 1 +ATOM 8876 C C . VAL D 1 225 ? 27.440 58.076 63.828 1.00 93.45 ? 224 VAL D C 1 +ATOM 8877 O O . VAL D 1 225 ? 26.825 58.696 62.963 1.00 88.92 ? 224 VAL D O 1 +ATOM 8878 C CB . VAL D 1 225 ? 29.744 58.256 62.937 1.00 81.06 ? 224 VAL D CB 1 +ATOM 8879 C CG1 . VAL D 1 225 ? 30.362 59.005 64.100 1.00 89.16 ? 224 VAL D CG1 1 +ATOM 8880 C CG2 . VAL D 1 225 ? 30.826 57.554 62.125 1.00 87.52 ? 224 VAL D CG2 1 +ATOM 8881 N N . THR D 1 226 ? 27.097 58.102 65.117 1.00 91.33 ? 225 THR D N 1 +ATOM 8882 C CA . THR D 1 226 ? 25.987 58.930 65.609 1.00 98.06 ? 225 THR D CA 1 +ATOM 8883 C C . THR D 1 226 ? 26.356 59.853 66.792 1.00 92.46 ? 225 THR D C 1 +ATOM 8884 O O . THR D 1 226 ? 26.941 59.411 67.778 1.00 87.84 ? 225 THR D O 1 +ATOM 8885 C CB . THR D 1 226 ? 24.780 58.068 66.052 1.00 84.68 ? 225 THR D CB 1 +ATOM 8886 O OG1 . THR D 1 226 ? 24.409 57.147 65.016 1.00 78.37 ? 225 THR D OG1 1 +ATOM 8887 C CG2 . THR D 1 226 ? 23.601 58.964 66.395 1.00 103.55 ? 225 THR D CG2 1 +ATOM 8888 N N . ALA D 1 227 ? 25.998 61.132 66.699 1.00 84.62 ? 226 ALA D N 1 +ATOM 8889 C CA . ALA D 1 227 ? 26.165 62.052 67.829 1.00 83.83 ? 226 ALA D CA 1 +ATOM 8890 C C . ALA D 1 227 ? 25.098 61.841 68.921 1.00 93.10 ? 226 ALA D C 1 +ATOM 8891 O O . ALA D 1 227 ? 23.954 61.485 68.630 1.00 102.64 ? 226 ALA D O 1 +ATOM 8892 C CB . ALA D 1 227 ? 26.173 63.495 67.344 1.00 83.76 ? 226 ALA D CB 1 +ATOM 8893 N N . ALA D 1 228 ? 25.487 62.068 70.174 1.00 89.70 ? 227 ALA D N 1 +ATOM 8894 C CA . ALA D 1 228 ? 24.657 61.740 71.333 1.00 103.41 ? 227 ALA D CA 1 +ATOM 8895 C C . ALA D 1 228 ? 25.154 62.517 72.551 1.00 108.85 ? 227 ALA D C 1 +ATOM 8896 O O . ALA D 1 228 ? 25.882 63.492 72.394 1.00 102.47 ? 227 ALA D O 1 +ATOM 8897 C CB . ALA D 1 228 ? 24.706 60.244 71.601 1.00 79.38 ? 227 ALA D CB 1 +ATOM 8898 N N . GLY D 1 229 ? 24.752 62.103 73.752 1.00 108.62 ? 228 GLY D N 1 +ATOM 8899 C CA . GLY D 1 229 ? 25.289 62.671 74.983 1.00 119.00 ? 228 GLY D CA 1 +ATOM 8900 C C . GLY D 1 229 ? 24.743 63.995 75.501 1.00 126.42 ? 228 GLY D C 1 +ATOM 8901 O O . GLY D 1 229 ? 25.014 64.375 76.638 1.00 130.42 ? 228 GLY D O 1 +ATOM 8902 N N . ILE D 1 230 ? 24.005 64.717 74.667 1.00 109.55 ? 229 ILE D N 1 +ATOM 8903 C CA . ILE D 1 230 ? 23.235 65.868 75.121 1.00 121.49 ? 229 ILE D CA 1 +ATOM 8904 C C . ILE D 1 230 ? 21.783 65.420 75.223 1.00 204.37 ? 229 ILE D C 1 +ATOM 8905 O O . ILE D 1 230 ? 21.276 64.786 74.297 1.00 237.58 ? 229 ILE D O 1 +ATOM 8906 C CB . ILE D 1 230 ? 23.324 67.025 74.118 1.00 126.34 ? 229 ILE D CB 1 +ATOM 8907 C CG1 . ILE D 1 230 ? 24.693 67.692 74.199 1.00 124.95 ? 229 ILE D CG1 1 +ATOM 8908 C CG2 . ILE D 1 230 ? 22.228 68.049 74.370 1.00 153.83 ? 229 ILE D CG2 1 +ATOM 8909 C CD1 . ILE D 1 230 ? 24.841 68.859 73.267 1.00 113.02 ? 229 ILE D CD1 1 +ATOM 8910 N N . THR D 1 231 ? 21.119 65.729 76.335 1.00 223.72 ? 230 THR D N 1 +ATOM 8911 C CA . THR D 1 231 ? 19.735 65.304 76.562 1.00 238.52 ? 230 THR D CA 1 +ATOM 8912 C C . THR D 1 231 ? 18.795 65.615 75.381 1.00 247.28 ? 230 THR D C 1 +ATOM 8913 O O . THR D 1 231 ? 17.636 65.997 75.547 1.00 224.30 ? 230 THR D O 1 +ATOM 8914 C CB . THR D 1 231 ? 19.162 65.948 77.840 1.00 219.63 ? 230 THR D CB 1 +ATOM 8915 O OG1 . THR D 1 231 ? 17.907 65.363 78.157 1.00 211.88 ? 230 THR D OG1 1 +ATOM 8916 C CG2 . THR D 1 231 ? 18.875 67.415 77.620 1.00 206.29 ? 230 THR D CG2 1 +ATOM 8917 N N . ALA D 1 235 ? 19.262 72.642 83.252 1.00 142.69 ? 1054 ALA D N 1 +ATOM 8918 C CA . ALA D 1 235 ? 18.737 73.180 84.507 1.00 166.84 ? 1054 ALA D CA 1 +ATOM 8919 C C . ALA D 1 235 ? 19.817 73.825 85.385 1.00 178.02 ? 1054 ALA D C 1 +ATOM 8920 O O . ALA D 1 235 ? 20.875 74.240 84.898 1.00 143.40 ? 1054 ALA D O 1 +ATOM 8921 C CB . ALA D 1 235 ? 17.990 72.087 85.286 1.00 135.63 ? 1054 ALA D CB 1 +ATOM 8922 N N . SER D 1 236 ? 19.531 73.922 86.681 1.00 192.69 ? 1055 SER D N 1 +ATOM 8923 C CA . SER D 1 236 ? 20.512 74.390 87.653 1.00 205.31 ? 1055 SER D CA 1 +ATOM 8924 C C . SER D 1 236 ? 21.272 73.178 88.174 1.00 221.42 ? 1055 SER D C 1 +ATOM 8925 O O . SER D 1 236 ? 22.304 73.300 88.844 1.00 187.91 ? 1055 SER D O 1 +ATOM 8926 C CB . SER D 1 236 ? 19.830 75.127 88.805 1.00 177.63 ? 1055 SER D CB 1 +ATOM 8927 O OG . SER D 1 236 ? 20.787 75.735 89.655 1.00 147.09 ? 1055 SER D OG 1 +ATOM 8928 N N . THR D 1 237 ? 20.742 72.003 87.843 1.00 237.76 ? 1056 THR D N 1 +ATOM 8929 C CA . THR D 1 237 ? 21.390 70.734 88.139 1.00 213.37 ? 1056 THR D CA 1 +ATOM 8930 C C . THR D 1 237 ? 22.756 70.690 87.454 1.00 177.35 ? 1056 THR D C 1 +ATOM 8931 O O . THR D 1 237 ? 23.669 69.999 87.902 1.00 138.16 ? 1056 THR D O 1 +ATOM 8932 C CB . THR D 1 237 ? 20.506 69.537 87.698 1.00 171.54 ? 1056 THR D CB 1 +ATOM 8933 O OG1 . THR D 1 237 ? 20.478 69.444 86.268 1.00 157.32 ? 1056 THR D OG1 1 +ATOM 8934 C CG2 . THR D 1 237 ? 19.079 69.711 88.216 1.00 151.84 ? 1056 THR D CG2 1 +ATOM 8935 N N . LYS D 1 238 ? 22.883 71.444 86.366 1.00 202.37 ? 1057 LYS D N 1 +ATOM 8936 C CA . LYS D 1 238 ? 24.159 71.632 85.692 1.00 191.00 ? 1057 LYS D CA 1 +ATOM 8937 C C . LYS D 1 238 ? 25.203 72.130 86.683 1.00 164.76 ? 1057 LYS D C 1 +ATOM 8938 O O . LYS D 1 238 ? 26.218 71.477 86.897 1.00 130.32 ? 1057 LYS D O 1 +ATOM 8939 C CB . LYS D 1 238 ? 24.020 72.633 84.537 1.00 178.58 ? 1057 LYS D CB 1 +ATOM 8940 C CG . LYS D 1 238 ? 23.647 72.025 83.185 1.00 170.38 ? 1057 LYS D CG 1 +ATOM 8941 C CD . LYS D 1 238 ? 22.297 71.327 83.218 1.00 154.35 ? 1057 LYS D CD 1 +ATOM 8942 C CE . LYS D 1 238 ? 21.844 70.922 81.820 1.00 130.49 ? 1057 LYS D CE 1 +ATOM 8943 N NZ . LYS D 1 238 ? 20.557 70.159 81.825 1.00 133.38 ? 1057 LYS D NZ 1 +ATOM 8944 N N . LYS D 1 239 ? 24.918 73.272 87.305 1.00 182.92 ? 1058 LYS D N 1 +ATOM 8945 C CA . LYS D 1 239 ? 25.853 73.961 88.196 1.00 196.52 ? 1058 LYS D CA 1 +ATOM 8946 C C . LYS D 1 239 ? 26.354 73.105 89.367 1.00 181.80 ? 1058 LYS D C 1 +ATOM 8947 O O . LYS D 1 239 ? 27.436 73.346 89.910 1.00 161.92 ? 1058 LYS D O 1 +ATOM 8948 C CB . LYS D 1 239 ? 25.202 75.241 88.732 1.00 205.87 ? 1058 LYS D CB 1 +ATOM 8949 C CG . LYS D 1 239 ? 24.651 76.180 87.660 1.00 180.06 ? 1058 LYS D CG 1 +ATOM 8950 C CD . LYS D 1 239 ? 24.169 77.482 88.286 1.00 178.40 ? 1058 LYS D CD 1 +ATOM 8951 C CE . LYS D 1 239 ? 25.252 78.087 89.183 1.00 172.56 ? 1058 LYS D CE 1 +ATOM 8952 N NZ . LYS D 1 239 ? 24.759 79.196 90.048 1.00 142.09 ? 1058 LYS D NZ 1 +ATOM 8953 N N . LEU D 1 240 ? 25.560 72.107 89.744 1.00 173.02 ? 1059 LEU D N 1 +ATOM 8954 C CA . LEU D 1 240 ? 25.867 71.240 90.881 1.00 181.36 ? 1059 LEU D CA 1 +ATOM 8955 C C . LEU D 1 240 ? 26.957 70.218 90.584 1.00 173.44 ? 1059 LEU D C 1 +ATOM 8956 O O . LEU D 1 240 ? 27.913 70.062 91.355 1.00 109.11 ? 1059 LEU D O 1 +ATOM 8957 C CB . LEU D 1 240 ? 24.604 70.496 91.308 1.00 190.56 ? 1059 LEU D CB 1 +ATOM 8958 C CG . LEU D 1 240 ? 24.792 69.377 92.328 1.00 169.78 ? 1059 LEU D CG 1 +ATOM 8959 C CD1 . LEU D 1 240 ? 25.353 69.938 93.625 1.00 160.93 ? 1059 LEU D CD1 1 +ATOM 8960 C CD2 . LEU D 1 240 ? 23.470 68.670 92.562 1.00 146.06 ? 1059 LEU D CD2 1 +ATOM 8961 N N . SER D 1 241 ? 26.783 69.513 89.468 1.00 201.83 ? 1060 SER D N 1 +ATOM 8962 C CA . SER D 1 241 ? 27.695 68.456 89.044 1.00 180.06 ? 1060 SER D CA 1 +ATOM 8963 C C . SER D 1 241 ? 29.018 69.025 88.547 1.00 148.53 ? 1060 SER D C 1 +ATOM 8964 O O . SER D 1 241 ? 30.002 68.303 88.433 1.00 141.30 ? 1060 SER D O 1 +ATOM 8965 C CB . SER D 1 241 ? 27.053 67.600 87.951 1.00 137.03 ? 1060 SER D CB 1 +ATOM 8966 O OG . SER D 1 241 ? 27.044 68.284 86.715 1.00 125.20 ? 1060 SER D OG 1 +ATOM 8967 N N . GLU D 1 242 ? 29.038 70.318 88.246 1.00 143.14 ? 1061 GLU D N 1 +ATOM 8968 C CA . GLU D 1 242 ? 30.288 70.981 87.899 1.00 175.06 ? 1061 GLU D CA 1 +ATOM 8969 C C . GLU D 1 242 ? 31.208 70.961 89.115 1.00 161.19 ? 1061 GLU D C 1 +ATOM 8970 O O . GLU D 1 242 ? 32.429 70.830 88.989 1.00 118.74 ? 1061 GLU D O 1 +ATOM 8971 C CB . GLU D 1 242 ? 30.045 72.424 87.444 1.00 182.88 ? 1061 GLU D CB 1 +ATOM 8972 C CG . GLU D 1 242 ? 28.953 72.604 86.389 1.00 184.23 ? 1061 GLU D CG 1 +ATOM 8973 C CD . GLU D 1 242 ? 29.137 71.738 85.144 1.00 190.33 ? 1061 GLU D CD 1 +ATOM 8974 O OE1 . GLU D 1 242 ? 30.280 71.340 84.834 1.00 193.80 ? 1061 GLU D OE1 1 +ATOM 8975 O OE2 . GLU D 1 242 ? 28.124 71.462 84.465 1.00 177.34 ? 1061 GLU D OE2 1 +ATOM 8976 N N . SER D 1 243 ? 30.600 71.080 90.292 1.00 176.02 ? 1062 SER D N 1 +ATOM 8977 C CA . SER D 1 243 ? 31.330 71.067 91.556 1.00 198.14 ? 1062 SER D CA 1 +ATOM 8978 C C . SER D 1 243 ? 31.726 69.648 91.971 1.00 179.05 ? 1062 SER D C 1 +ATOM 8979 O O . SER D 1 243 ? 32.888 69.389 92.310 1.00 131.08 ? 1062 SER D O 1 +ATOM 8980 C CB . SER D 1 243 ? 30.500 71.739 92.653 1.00 202.78 ? 1062 SER D CB 1 +ATOM 8981 O OG . SER D 1 243 ? 30.255 73.098 92.335 1.00 192.19 ? 1062 SER D OG 1 +ATOM 8982 N N . LEU D 1 244 ? 30.754 68.738 91.941 1.00 166.23 ? 1063 LEU D N 1 +ATOM 8983 C CA . LEU D 1 244 ? 31.013 67.330 92.214 1.00 147.68 ? 1063 LEU D CA 1 +ATOM 8984 C C . LEU D 1 244 ? 32.145 66.836 91.338 1.00 155.28 ? 1063 LEU D C 1 +ATOM 8985 O O . LEU D 1 244 ? 33.001 66.071 91.788 1.00 125.55 ? 1063 LEU D O 1 +ATOM 8986 C CB . LEU D 1 244 ? 29.762 66.497 91.965 1.00 124.96 ? 1063 LEU D CB 1 +ATOM 8987 C CG . LEU D 1 244 ? 28.838 66.386 93.175 1.00 147.57 ? 1063 LEU D CG 1 +ATOM 8988 C CD1 . LEU D 1 244 ? 27.685 65.445 92.870 1.00 137.01 ? 1063 LEU D CD1 1 +ATOM 8989 C CD2 . LEU D 1 244 ? 29.623 65.937 94.413 1.00 123.35 ? 1063 LEU D CD2 1 +ATOM 8990 N N . LYS D 1 245 ? 32.133 67.291 90.088 1.00 169.76 ? 1064 LYS D N 1 +ATOM 8991 C CA . LYS D 1 245 ? 33.243 67.088 89.170 1.00 163.48 ? 1064 LYS D CA 1 +ATOM 8992 C C . LYS D 1 245 ? 34.564 67.475 89.826 1.00 173.15 ? 1064 LYS D C 1 +ATOM 8993 O O . LYS D 1 245 ? 35.391 66.608 90.101 1.00 176.59 ? 1064 LYS D O 1 +ATOM 8994 C CB . LYS D 1 245 ? 33.042 67.892 87.881 1.00 136.25 ? 1064 LYS D CB 1 +ATOM 8995 C CG . LYS D 1 245 ? 32.288 67.157 86.773 1.00 162.26 ? 1064 LYS D CG 1 +ATOM 8996 C CD . LYS D 1 245 ? 32.101 68.058 85.548 1.00 196.11 ? 1064 LYS D CD 1 +ATOM 8997 C CE . LYS D 1 245 ? 31.485 67.313 84.369 1.00 181.58 ? 1064 LYS D CE 1 +ATOM 8998 N NZ . LYS D 1 245 ? 31.445 68.133 83.124 1.00 131.65 ? 1064 LYS D NZ 1 +ATOM 8999 N N . ARG D 1 246 ? 34.753 68.765 90.101 1.00 165.67 ? 1065 ARG D N 1 +ATOM 9000 C CA . ARG D 1 246 ? 36.047 69.239 90.598 1.00 176.26 ? 1065 ARG D CA 1 +ATOM 9001 C C . ARG D 1 246 ? 36.465 68.597 91.932 1.00 167.31 ? 1065 ARG D C 1 +ATOM 9002 O O . ARG D 1 246 ? 37.647 68.321 92.142 1.00 155.76 ? 1065 ARG D O 1 +ATOM 9003 C CB . ARG D 1 246 ? 36.115 70.776 90.663 1.00 169.83 ? 1065 ARG D CB 1 +ATOM 9004 C CG . ARG D 1 246 ? 36.097 71.494 89.318 1.00 183.88 ? 1065 ARG D CG 1 +ATOM 9005 C CD . ARG D 1 246 ? 36.223 73.006 89.507 1.00 202.98 ? 1065 ARG D CD 1 +ATOM 9006 N NE . ARG D 1 246 ? 36.137 73.740 88.242 1.00 222.28 ? 1065 ARG D NE 1 +ATOM 9007 C CZ . ARG D 1 246 ? 36.104 75.068 88.137 1.00 199.58 ? 1065 ARG D CZ 1 +ATOM 9008 N NH1 . ARG D 1 246 ? 36.149 75.829 89.223 1.00 182.20 ? 1065 ARG D NH1 1 +ATOM 9009 N NH2 . ARG D 1 246 ? 36.024 75.639 86.941 1.00 154.93 ? 1065 ARG D NH2 1 +ATOM 9010 N N . ILE D 1 247 ? 35.498 68.333 92.808 1.00 145.44 ? 1066 ILE D N 1 +ATOM 9011 C CA . ILE D 1 247 ? 35.792 67.745 94.118 1.00 149.12 ? 1066 ILE D CA 1 +ATOM 9012 C C . ILE D 1 247 ? 36.371 66.325 94.002 1.00 157.22 ? 1066 ILE D C 1 +ATOM 9013 O O . ILE D 1 247 ? 37.314 65.972 94.716 1.00 121.46 ? 1066 ILE D O 1 +ATOM 9014 C CB . ILE D 1 247 ? 34.546 67.797 95.060 1.00 156.68 ? 1066 ILE D CB 1 +ATOM 9015 C CG1 . ILE D 1 247 ? 34.196 69.255 95.415 1.00 188.69 ? 1066 ILE D CG1 1 +ATOM 9016 C CG2 . ILE D 1 247 ? 34.758 66.950 96.313 1.00 116.09 ? 1066 ILE D CG2 1 +ATOM 9017 C CD1 . ILE D 1 247 ? 32.856 69.457 96.107 1.00 205.08 ? 1066 ILE D CD1 1 +ATOM 9018 N N . GLY D 1 248 ? 35.819 65.528 93.091 1.00 167.00 ? 1067 GLY D N 1 +ATOM 9019 C CA . GLY D 1 248 ? 36.362 64.213 92.802 1.00 140.75 ? 1067 GLY D CA 1 +ATOM 9020 C C . GLY D 1 248 ? 37.608 64.345 91.946 1.00 155.44 ? 1067 GLY D C 1 +ATOM 9021 O O . GLY D 1 248 ? 38.444 63.442 91.902 1.00 145.60 ? 1067 GLY D O 1 +ATOM 9022 N N . ASP D 1 249 ? 37.729 65.486 91.270 1.00 168.90 ? 1068 ASP D N 1 +ATOM 9023 C CA . ASP D 1 249 ? 38.859 65.757 90.382 1.00 160.46 ? 1068 ASP D CA 1 +ATOM 9024 C C . ASP D 1 249 ? 40.125 66.124 91.151 1.00 159.94 ? 1068 ASP D C 1 +ATOM 9025 O O . ASP D 1 249 ? 41.137 65.425 91.049 1.00 134.75 ? 1068 ASP D O 1 +ATOM 9026 C CB . ASP D 1 249 ? 38.511 66.849 89.364 1.00 167.44 ? 1068 ASP D CB 1 +ATOM 9027 C CG . ASP D 1 249 ? 37.744 66.310 88.165 1.00 186.85 ? 1068 ASP D CG 1 +ATOM 9028 O OD1 . ASP D 1 249 ? 37.251 65.163 88.239 1.00 193.50 ? 1068 ASP D OD1 1 +ATOM 9029 O OD2 . ASP D 1 249 ? 37.631 67.033 87.151 1.00 174.14 ? 1068 ASP D OD2 1 +ATOM 9030 N N . GLU D 1 250 ? 40.062 67.217 91.914 1.00 181.61 ? 1069 GLU D N 1 +ATOM 9031 C CA . GLU D 1 250 ? 41.162 67.633 92.788 1.00 188.61 ? 1069 GLU D CA 1 +ATOM 9032 C C . GLU D 1 250 ? 41.613 66.452 93.640 1.00 172.36 ? 1069 GLU D C 1 +ATOM 9033 O O . GLU D 1 250 ? 42.805 66.267 93.902 1.00 122.53 ? 1069 GLU D O 1 +ATOM 9034 C CB . GLU D 1 250 ? 40.719 68.784 93.699 1.00 172.98 ? 1069 GLU D CB 1 +ATOM 9035 C CG . GLU D 1 250 ? 40.273 70.048 92.966 1.00 198.96 ? 1069 GLU D CG 1 +ATOM 9036 C CD . GLU D 1 250 ? 39.475 70.994 93.856 1.00 200.23 ? 1069 GLU D CD 1 +ATOM 9037 O OE1 . GLU D 1 250 ? 39.372 70.719 95.072 1.00 176.98 ? 1069 GLU D OE1 1 +ATOM 9038 O OE2 . GLU D 1 250 ? 38.947 72.006 93.339 1.00 182.07 ? 1069 GLU D OE2 1 +ATOM 9039 N N . LEU D 1 251 ? 40.633 65.655 94.052 1.00 162.33 ? 1070 LEU D N 1 +ATOM 9040 C CA . LEU D 1 251 ? 40.852 64.444 94.827 1.00 146.14 ? 1070 LEU D CA 1 +ATOM 9041 C C . LEU D 1 251 ? 41.733 63.438 94.082 1.00 151.72 ? 1070 LEU D C 1 +ATOM 9042 O O . LEU D 1 251 ? 42.788 63.035 94.576 1.00 103.21 ? 1070 LEU D O 1 +ATOM 9043 C CB . LEU D 1 251 ? 39.494 63.829 95.180 1.00 148.63 ? 1070 LEU D CB 1 +ATOM 9044 C CG . LEU D 1 251 ? 39.383 62.641 96.138 1.00 157.87 ? 1070 LEU D CG 1 +ATOM 9045 C CD1 . LEU D 1 251 ? 40.393 62.726 97.277 1.00 143.26 ? 1070 LEU D CD1 1 +ATOM 9046 C CD2 . LEU D 1 251 ? 37.957 62.524 96.688 1.00 119.45 ? 1070 LEU D CD2 1 +ATOM 9047 N N . ASP D 1 252 ? 41.316 63.039 92.887 1.00 170.97 ? 1071 ASP D N 1 +ATOM 9048 C CA . ASP D 1 252 ? 42.072 62.033 92.155 1.00 153.55 ? 1071 ASP D CA 1 +ATOM 9049 C C . ASP D 1 252 ? 43.389 62.597 91.616 1.00 151.25 ? 1071 ASP D C 1 +ATOM 9050 O O . ASP D 1 252 ? 44.334 61.850 91.349 1.00 135.50 ? 1071 ASP D O 1 +ATOM 9051 C CB . ASP D 1 252 ? 41.229 61.399 91.045 1.00 114.35 ? 1071 ASP D CB 1 +ATOM 9052 C CG . ASP D 1 252 ? 41.987 60.322 90.276 1.00 204.31 ? 1071 ASP D CG 1 +ATOM 9053 O OD1 . ASP D 1 252 ? 42.341 59.280 90.874 1.00 195.11 ? 1071 ASP D OD1 1 +ATOM 9054 O OD2 . ASP D 1 252 ? 42.229 60.515 89.067 1.00 247.22 ? 1071 ASP D OD2 1 +ATOM 9055 N N . SER D 1 253 ? 43.459 63.919 91.494 1.00 150.41 ? 1072 SER D N 1 +ATOM 9056 C CA . SER D 1 253 ? 44.659 64.564 90.968 1.00 179.57 ? 1072 SER D CA 1 +ATOM 9057 C C . SER D 1 253 ? 45.602 65.096 92.051 1.00 196.00 ? 1072 SER D C 1 +ATOM 9058 O O . SER D 1 253 ? 46.716 65.520 91.738 1.00 182.40 ? 1072 SER D O 1 +ATOM 9059 C CB . SER D 1 253 ? 44.296 65.689 89.993 1.00 181.59 ? 1072 SER D CB 1 +ATOM 9060 O OG . SER D 1 253 ? 43.806 66.829 90.676 1.00 167.81 ? 1072 SER D OG 1 +ATOM 9061 N N . ASN D 1 254 ? 45.159 65.077 93.309 1.00 219.44 ? 1073 ASN D N 1 +ATOM 9062 C CA . ASN D 1 254 ? 45.988 65.517 94.439 1.00 216.16 ? 1073 ASN D CA 1 +ATOM 9063 C C . ASN D 1 254 ? 47.228 64.647 94.605 1.00 208.69 ? 1073 ASN D C 1 +ATOM 9064 O O . ASN D 1 254 ? 47.169 63.575 95.212 1.00 167.12 ? 1073 ASN D O 1 +ATOM 9065 C CB . ASN D 1 254 ? 45.188 65.511 95.745 1.00 208.42 ? 1073 ASN D CB 1 +ATOM 9066 C CG . ASN D 1 254 ? 45.275 66.830 96.491 1.00 190.76 ? 1073 ASN D CG 1 +ATOM 9067 O OD1 . ASN D 1 254 ? 45.415 67.890 95.880 1.00 183.48 ? 1073 ASN D OD1 1 +ATOM 9068 N ND2 . ASN D 1 254 ? 45.186 66.772 97.817 1.00 173.18 ? 1073 ASN D ND2 1 +ATOM 9069 N N . MET D 1 255 ? 48.350 65.124 94.075 1.00 230.99 ? 1074 MET D N 1 +ATOM 9070 C CA . MET D 1 255 ? 49.571 64.325 94.005 1.00 233.50 ? 1074 MET D CA 1 +ATOM 9071 C C . MET D 1 255 ? 50.141 63.964 95.374 1.00 222.25 ? 1074 MET D C 1 +ATOM 9072 O O . MET D 1 255 ? 50.853 62.966 95.505 1.00 191.62 ? 1074 MET D O 1 +ATOM 9073 C CB . MET D 1 255 ? 50.630 65.023 93.144 1.00 235.33 ? 1074 MET D CB 1 +ATOM 9074 C CG . MET D 1 255 ? 50.339 64.985 91.650 1.00 226.38 ? 1074 MET D CG 1 +ATOM 9075 S SD . MET D 1 255 ? 50.083 63.308 91.031 1.00 246.94 ? 1074 MET D SD 1 +ATOM 9076 C CE . MET D 1 255 ? 51.655 62.535 91.420 1.00 133.52 ? 1074 MET D CE 1 +ATOM 9077 N N . GLU D 1 256 ? 49.830 64.777 96.383 1.00 231.08 ? 1075 GLU D N 1 +ATOM 9078 C CA . GLU D 1 256 ? 50.234 64.494 97.757 1.00 220.43 ? 1075 GLU D CA 1 +ATOM 9079 C C . GLU D 1 256 ? 49.686 63.142 98.151 1.00 193.15 ? 1075 GLU D C 1 +ATOM 9080 O O . GLU D 1 256 ? 50.426 62.219 98.500 1.00 159.00 ? 1075 GLU D O 1 +ATOM 9081 C CB . GLU D 1 256 ? 49.631 65.516 98.717 1.00 217.80 ? 1075 GLU D CB 1 +ATOM 9082 C CG . GLU D 1 256 ? 49.820 66.960 98.341 1.00 214.12 ? 1075 GLU D CG 1 +ATOM 9083 C CD . GLU D 1 256 ? 49.051 67.876 99.265 1.00 211.19 ? 1075 GLU D CD 1 +ATOM 9084 O OE1 . GLU D 1 256 ? 47.969 67.462 99.738 1.00 213.38 ? 1075 GLU D OE1 1 +ATOM 9085 O OE2 . GLU D 1 256 ? 49.529 68.998 99.529 1.00 201.26 ? 1075 GLU D OE2 1 +ATOM 9086 N N . LEU D 1 257 ? 48.363 63.059 98.080 1.00 182.55 ? 1076 LEU D N 1 +ATOM 9087 C CA . LEU D 1 257 ? 47.590 61.897 98.488 1.00 177.36 ? 1076 LEU D CA 1 +ATOM 9088 C C . LEU D 1 257 ? 47.919 60.632 97.689 1.00 172.05 ? 1076 LEU D C 1 +ATOM 9089 O O . LEU D 1 257 ? 48.156 59.568 98.270 1.00 114.47 ? 1076 LEU D O 1 +ATOM 9090 C CB . LEU D 1 257 ? 46.100 62.236 98.383 1.00 163.61 ? 1076 LEU D CB 1 +ATOM 9091 C CG . LEU D 1 257 ? 45.046 61.158 98.625 1.00 161.60 ? 1076 LEU D CG 1 +ATOM 9092 C CD1 . LEU D 1 257 ? 45.291 60.411 99.933 1.00 137.96 ? 1076 LEU D CD1 1 +ATOM 9093 C CD2 . LEU D 1 257 ? 43.668 61.793 98.600 1.00 170.83 ? 1076 LEU D CD2 1 +ATOM 9094 N N . GLN D 1 258 ? 47.933 60.751 96.363 1.00 186.80 ? 1077 GLN D N 1 +ATOM 9095 C CA . GLN D 1 258 ? 48.199 59.606 95.494 1.00 178.38 ? 1077 GLN D CA 1 +ATOM 9096 C C . GLN D 1 258 ? 49.561 58.980 95.825 1.00 178.75 ? 1077 GLN D C 1 +ATOM 9097 O O . GLN D 1 258 ? 49.679 57.757 95.938 1.00 160.85 ? 1077 GLN D O 1 +ATOM 9098 C CB . GLN D 1 258 ? 48.106 60.002 94.012 1.00 157.67 ? 1077 GLN D CB 1 +ATOM 9099 C CG . GLN D 1 258 ? 46.764 60.625 93.595 1.00 174.52 ? 1077 GLN D CG 1 +ATOM 9100 C CD . GLN D 1 258 ? 45.589 59.657 93.680 1.00 170.45 ? 1077 GLN D CD 1 +ATOM 9101 O OE1 . GLN D 1 258 ? 45.740 58.453 93.465 1.00 165.81 ? 1077 GLN D OE1 1 +ATOM 9102 N NE2 . GLN D 1 258 ? 44.409 60.186 93.997 1.00 122.29 ? 1077 GLN D NE2 1 +ATOM 9103 N N . ARG D 1 259 ? 50.572 59.830 96.003 1.00 177.60 ? 1078 ARG D N 1 +ATOM 9104 C CA . ARG D 1 259 ? 51.903 59.393 96.424 1.00 182.16 ? 1078 ARG D CA 1 +ATOM 9105 C C . ARG D 1 259 ? 51.827 58.677 97.768 1.00 187.80 ? 1078 ARG D C 1 +ATOM 9106 O O . ARG D 1 259 ? 52.377 57.586 97.930 1.00 171.52 ? 1078 ARG D O 1 +ATOM 9107 C CB . ARG D 1 259 ? 52.852 60.594 96.543 1.00 198.31 ? 1078 ARG D CB 1 +ATOM 9108 C CG . ARG D 1 259 ? 54.307 60.229 96.845 1.00 198.91 ? 1078 ARG D CG 1 +ATOM 9109 C CD . ARG D 1 259 ? 54.972 61.239 97.782 1.00 215.88 ? 1078 ARG D CD 1 +ATOM 9110 N NE . ARG D 1 259 ? 54.952 62.603 97.256 1.00 223.85 ? 1078 ARG D NE 1 +ATOM 9111 C CZ . ARG D 1 259 ? 54.725 63.687 97.994 1.00 199.56 ? 1078 ARG D CZ 1 +ATOM 9112 N NH1 . ARG D 1 259 ? 54.492 63.569 99.295 1.00 175.46 ? 1078 ARG D NH1 1 +ATOM 9113 N NH2 . ARG D 1 259 ? 54.727 64.889 97.430 1.00 166.07 ? 1078 ARG D NH2 1 +ATOM 9114 N N . MET D 1 260 ? 51.136 59.310 98.716 1.00 190.66 ? 1079 MET D N 1 +ATOM 9115 C CA . MET D 1 260 ? 50.992 58.817 100.088 1.00 186.66 ? 1079 MET D CA 1 +ATOM 9116 C C . MET D 1 260 ? 50.417 57.407 100.172 1.00 192.13 ? 1079 MET D C 1 +ATOM 9117 O O . MET D 1 260 ? 50.882 56.590 100.968 1.00 192.21 ? 1079 MET D O 1 +ATOM 9118 C CB . MET D 1 260 ? 50.102 59.765 100.903 1.00 168.76 ? 1079 MET D CB 1 +ATOM 9119 C CG . MET D 1 260 ? 50.799 60.477 102.051 1.00 135.84 ? 1079 MET D CG 1 +ATOM 9120 S SD . MET D 1 260 ? 49.667 61.440 103.082 1.00 237.55 ? 1079 MET D SD 1 +ATOM 9121 C CE . MET D 1 260 ? 49.212 62.788 101.989 1.00 97.67 ? 1079 MET D CE 1 +ATOM 9122 N N . ILE D 1 261 ? 49.398 57.124 99.366 1.00 181.11 ? 1080 ILE D N 1 +ATOM 9123 C CA . ILE D 1 261 ? 48.728 55.832 99.453 1.00 183.79 ? 1080 ILE D CA 1 +ATOM 9124 C C . ILE D 1 261 ? 49.507 54.746 98.731 1.00 189.64 ? 1080 ILE D C 1 +ATOM 9125 O O . ILE D 1 261 ? 49.585 53.616 99.210 1.00 197.73 ? 1080 ILE D O 1 +ATOM 9126 C CB . ILE D 1 261 ? 47.300 55.867 98.898 1.00 166.19 ? 1080 ILE D CB 1 +ATOM 9127 C CG1 . ILE D 1 261 ? 46.582 57.140 99.339 1.00 148.88 ? 1080 ILE D CG1 1 +ATOM 9128 C CG2 . ILE D 1 261 ? 46.537 54.630 99.356 1.00 170.71 ? 1080 ILE D CG2 1 +ATOM 9129 C CD1 . ILE D 1 261 ? 45.096 57.113 99.070 1.00 141.94 ? 1080 ILE D CD1 1 +ATOM 9130 N N . ALA D 1 262 ? 50.067 55.092 97.574 1.00 176.03 ? 1081 ALA D N 1 +ATOM 9131 C CA . ALA D 1 262 ? 50.965 54.191 96.859 1.00 175.94 ? 1081 ALA D CA 1 +ATOM 9132 C C . ALA D 1 262 ? 52.075 53.761 97.818 1.00 194.67 ? 1081 ALA D C 1 +ATOM 9133 O O . ALA D 1 262 ? 52.401 52.575 97.931 1.00 176.44 ? 1081 ALA D O 1 +ATOM 9134 C CB . ALA D 1 262 ? 51.541 54.879 95.617 1.00 125.59 ? 1081 ALA D CB 1 +ATOM 9135 N N . ALA D 1 263 ? 52.625 54.736 98.534 1.00 195.18 ? 1082 ALA D N 1 +ATOM 9136 C CA . ALA D 1 263 ? 53.592 54.460 99.587 1.00 196.09 ? 1082 ALA D CA 1 +ATOM 9137 C C . ALA D 1 263 ? 52.904 53.885 100.828 1.00 224.08 ? 1082 ALA D C 1 +ATOM 9138 O O . ALA D 1 263 ? 52.665 54.598 101.806 1.00 213.71 ? 1082 ALA D O 1 +ATOM 9139 C CB . ALA D 1 263 ? 54.377 55.724 99.939 1.00 182.93 ? 1082 ALA D CB 1 +ATOM 9140 N N . VAL D 1 264 ? 52.575 52.596 100.772 1.00 238.99 ? 1083 VAL D N 1 +ATOM 9141 C CA . VAL D 1 264 ? 52.090 51.866 101.944 1.00 242.87 ? 1083 VAL D CA 1 +ATOM 9142 C C . VAL D 1 264 ? 52.329 50.356 101.795 1.00 217.02 ? 1083 VAL D C 1 +ATOM 9143 O O . VAL D 1 264 ? 52.296 49.815 100.683 1.00 157.52 ? 1083 VAL D O 1 +ATOM 9144 C CB . VAL D 1 264 ? 50.600 52.176 102.262 1.00 209.56 ? 1083 VAL D CB 1 +ATOM 9145 C CG1 . VAL D 1 264 ? 49.672 51.388 101.352 1.00 186.58 ? 1083 VAL D CG1 1 +ATOM 9146 C CG2 . VAL D 1 264 ? 50.294 51.886 103.730 1.00 190.58 ? 1083 VAL D CG2 1 +ATOM 9147 N N . ASP D 1 265 ? 52.592 49.689 102.917 1.00 225.17 ? 1084 ASP D N 1 +ATOM 9148 C CA . ASP D 1 265 ? 52.907 48.260 102.917 1.00 236.75 ? 1084 ASP D CA 1 +ATOM 9149 C C . ASP D 1 265 ? 51.634 47.423 103.007 1.00 232.61 ? 1084 ASP D C 1 +ATOM 9150 O O . ASP D 1 265 ? 51.024 47.305 104.072 1.00 194.92 ? 1084 ASP D O 1 +ATOM 9151 C CB . ASP D 1 265 ? 53.866 47.911 104.060 1.00 236.37 ? 1084 ASP D CB 1 +ATOM 9152 C CG . ASP D 1 265 ? 54.708 46.676 103.764 1.00 217.36 ? 1084 ASP D CG 1 +ATOM 9153 O OD1 . ASP D 1 265 ? 54.190 45.732 103.129 1.00 213.42 ? 1084 ASP D OD1 1 +ATOM 9154 O OD2 . ASP D 1 265 ? 55.894 46.653 104.160 1.00 186.55 ? 1084 ASP D OD2 1 +ATOM 9155 N N . THR D 1 266 ? 51.253 46.830 101.880 1.00 250.37 ? 1085 THR D N 1 +ATOM 9156 C CA . THR D 1 266 ? 49.948 46.196 101.748 1.00 266.54 ? 1085 THR D CA 1 +ATOM 9157 C C . THR D 1 266 ? 50.030 44.715 101.363 1.00 269.27 ? 1085 THR D C 1 +ATOM 9158 O O . THR D 1 266 ? 49.172 44.183 100.659 1.00 270.87 ? 1085 THR D O 1 +ATOM 9159 C CB . THR D 1 266 ? 49.086 46.952 100.717 1.00 267.04 ? 1085 THR D CB 1 +ATOM 9160 O OG1 . THR D 1 266 ? 48.891 48.301 101.155 1.00 263.60 ? 1085 THR D OG1 1 +ATOM 9161 C CG2 . THR D 1 266 ? 47.723 46.305 100.545 1.00 261.57 ? 1085 THR D CG2 1 +ATOM 9162 N N . ASP D 1 267 ? 51.076 44.036 101.822 1.00 263.84 ? 1086 ASP D N 1 +ATOM 9163 C CA . ASP D 1 267 ? 51.177 42.587 101.660 1.00 250.07 ? 1086 ASP D CA 1 +ATOM 9164 C C . ASP D 1 267 ? 50.342 41.930 102.754 1.00 238.23 ? 1086 ASP D C 1 +ATOM 9165 O O . ASP D 1 267 ? 49.711 40.888 102.549 1.00 199.77 ? 1086 ASP D O 1 +ATOM 9166 C CB . ASP D 1 267 ? 52.634 42.136 101.764 1.00 241.40 ? 1086 ASP D CB 1 +ATOM 9167 C CG . ASP D 1 267 ? 53.571 42.993 100.934 1.00 244.98 ? 1086 ASP D CG 1 +ATOM 9168 O OD1 . ASP D 1 267 ? 53.088 43.716 100.035 1.00 244.96 ? 1086 ASP D OD1 1 +ATOM 9169 O OD2 . ASP D 1 267 ? 54.794 42.941 101.181 1.00 242.85 ? 1086 ASP D OD2 1 +ATOM 9170 N N . SER D 1 268 ? 50.362 42.563 103.922 1.00 248.57 ? 1087 SER D N 1 +ATOM 9171 C CA . SER D 1 268 ? 49.469 42.240 105.024 1.00 235.61 ? 1087 SER D CA 1 +ATOM 9172 C C . SER D 1 268 ? 48.520 43.431 105.186 1.00 252.17 ? 1087 SER D C 1 +ATOM 9173 O O . SER D 1 268 ? 48.703 44.254 106.085 1.00 230.99 ? 1087 SER D O 1 +ATOM 9174 C CB . SER D 1 268 ? 50.282 42.016 106.302 1.00 184.85 ? 1087 SER D CB 1 +ATOM 9175 O OG . SER D 1 268 ? 49.462 41.605 107.380 1.00 155.93 ? 1087 SER D OG 1 +ATOM 9176 N N . PRO D 1 269 ? 47.503 43.524 104.306 1.00 256.02 ? 1088 PRO D N 1 +ATOM 9177 C CA . PRO D 1 269 ? 46.659 44.718 104.145 1.00 219.87 ? 1088 PRO D CA 1 +ATOM 9178 C C . PRO D 1 269 ? 45.628 44.928 105.252 1.00 215.01 ? 1088 PRO D C 1 +ATOM 9179 O O . PRO D 1 269 ? 45.389 46.072 105.640 1.00 201.84 ? 1088 PRO D O 1 +ATOM 9180 C CB . PRO D 1 269 ? 45.945 44.455 102.816 1.00 180.41 ? 1088 PRO D CB 1 +ATOM 9181 C CG . PRO D 1 269 ? 45.854 42.978 102.727 1.00 202.38 ? 1088 PRO D CG 1 +ATOM 9182 C CD . PRO D 1 269 ? 47.082 42.431 103.408 1.00 240.77 ? 1088 PRO D CD 1 +ATOM 9183 N N . ARG D 1 270 ? 45.036 43.840 105.738 1.00 218.40 ? 1089 ARG D N 1 +ATOM 9184 C CA . ARG D 1 270 ? 43.953 43.876 106.725 1.00 203.15 ? 1089 ARG D CA 1 +ATOM 9185 C C . ARG D 1 270 ? 44.234 44.741 107.970 1.00 205.67 ? 1089 ARG D C 1 +ATOM 9186 O O . ARG D 1 270 ? 43.381 45.532 108.394 1.00 119.54 ? 1089 ARG D O 1 +ATOM 9187 C CB . ARG D 1 270 ? 43.567 42.443 107.124 1.00 173.05 ? 1089 ARG D CB 1 +ATOM 9188 C CG . ARG D 1 270 ? 43.013 42.312 108.528 1.00 192.17 ? 1089 ARG D CG 1 +ATOM 9189 C CD . ARG D 1 270 ? 42.547 40.900 108.836 1.00 186.31 ? 1089 ARG D CD 1 +ATOM 9190 N NE . ARG D 1 270 ? 42.241 40.743 110.256 1.00 194.97 ? 1089 ARG D NE 1 +ATOM 9191 C CZ . ARG D 1 270 ? 41.119 41.164 110.834 1.00 194.63 ? 1089 ARG D CZ 1 +ATOM 9192 N NH1 . ARG D 1 270 ? 40.185 41.773 110.115 1.00 198.62 ? 1089 ARG D NH1 1 +ATOM 9193 N NH2 . ARG D 1 270 ? 40.931 40.977 112.136 1.00 168.28 ? 1089 ARG D NH2 1 +ATOM 9194 N N . GLU D 1 271 ? 45.426 44.593 108.543 1.00 234.76 ? 1090 GLU D N 1 +ATOM 9195 C CA . GLU D 1 271 ? 45.826 45.385 109.703 1.00 226.93 ? 1090 GLU D CA 1 +ATOM 9196 C C . GLU D 1 271 ? 45.968 46.852 109.320 1.00 217.12 ? 1090 GLU D C 1 +ATOM 9197 O O . GLU D 1 271 ? 45.517 47.739 110.045 1.00 184.11 ? 1090 GLU D O 1 +ATOM 9198 C CB . GLU D 1 271 ? 47.164 44.894 110.260 1.00 226.79 ? 1090 GLU D CB 1 +ATOM 9199 C CG . GLU D 1 271 ? 47.317 43.387 110.340 1.00 234.73 ? 1090 GLU D CG 1 +ATOM 9200 C CD . GLU D 1 271 ? 48.748 42.975 110.634 1.00 239.63 ? 1090 GLU D CD 1 +ATOM 9201 O OE1 . GLU D 1 271 ? 49.534 43.840 111.076 1.00 231.68 ? 1090 GLU D OE1 1 +ATOM 9202 O OE2 . GLU D 1 271 ? 49.088 41.792 110.416 1.00 238.41 ? 1090 GLU D OE2 1 +ATOM 9203 N N . VAL D 1 272 ? 46.603 47.090 108.174 1.00 231.29 ? 1091 VAL D N 1 +ATOM 9204 C CA . VAL D 1 272 ? 46.917 48.439 107.710 1.00 222.45 ? 1091 VAL D CA 1 +ATOM 9205 C C . VAL D 1 272 ? 45.672 49.314 107.606 1.00 223.07 ? 1091 VAL D C 1 +ATOM 9206 O O . VAL D 1 272 ? 45.681 50.469 108.027 1.00 214.10 ? 1091 VAL D O 1 +ATOM 9207 C CB . VAL D 1 272 ? 47.639 48.412 106.345 1.00 180.42 ? 1091 VAL D CB 1 +ATOM 9208 C CG1 . VAL D 1 272 ? 48.143 49.804 105.980 1.00 171.16 ? 1091 VAL D CG1 1 +ATOM 9209 C CG2 . VAL D 1 272 ? 48.788 47.417 106.373 1.00 162.69 ? 1091 VAL D CG2 1 +ATOM 9210 N N . PHE D 1 273 ? 44.602 48.755 107.051 1.00 225.44 ? 1092 PHE D N 1 +ATOM 9211 C CA . PHE D 1 273 ? 43.341 49.477 106.925 1.00 218.10 ? 1092 PHE D CA 1 +ATOM 9212 C C . PHE D 1 273 ? 42.753 49.783 108.296 1.00 201.52 ? 1092 PHE D C 1 +ATOM 9213 O O . PHE D 1 273 ? 42.444 50.933 108.605 1.00 197.86 ? 1092 PHE D O 1 +ATOM 9214 C CB . PHE D 1 273 ? 42.343 48.670 106.090 1.00 230.84 ? 1092 PHE D CB 1 +ATOM 9215 C CG . PHE D 1 273 ? 40.952 49.244 106.079 1.00 233.52 ? 1092 PHE D CG 1 +ATOM 9216 C CD1 . PHE D 1 273 ? 40.662 50.382 105.347 1.00 224.63 ? 1092 PHE D CD1 1 +ATOM 9217 C CD2 . PHE D 1 273 ? 39.935 48.642 106.801 1.00 232.31 ? 1092 PHE D CD2 1 +ATOM 9218 C CE1 . PHE D 1 273 ? 39.387 50.909 105.339 1.00 207.31 ? 1092 PHE D CE1 1 +ATOM 9219 C CE2 . PHE D 1 273 ? 38.658 49.165 106.791 1.00 221.47 ? 1092 PHE D CE2 1 +ATOM 9220 C CZ . PHE D 1 273 ? 38.385 50.297 106.058 1.00 205.70 ? 1092 PHE D CZ 1 +ATOM 9221 N N . PHE D 1 274 ? 42.616 48.745 109.116 1.00 185.37 ? 1093 PHE D N 1 +ATOM 9222 C CA . PHE D 1 274 ? 41.988 48.864 110.429 1.00 202.86 ? 1093 PHE D CA 1 +ATOM 9223 C C . PHE D 1 274 ? 42.649 49.897 111.344 1.00 214.45 ? 1093 PHE D C 1 +ATOM 9224 O O . PHE D 1 274 ? 41.958 50.654 112.029 1.00 208.74 ? 1093 PHE D O 1 +ATOM 9225 C CB . PHE D 1 274 ? 41.952 47.501 111.125 1.00 225.26 ? 1093 PHE D CB 1 +ATOM 9226 C CG . PHE D 1 274 ? 41.386 47.547 112.516 1.00 237.86 ? 1093 PHE D CG 1 +ATOM 9227 C CD1 . PHE D 1 274 ? 40.014 47.578 112.718 1.00 208.06 ? 1093 PHE D CD1 1 +ATOM 9228 C CD2 . PHE D 1 274 ? 42.225 47.562 113.622 1.00 230.78 ? 1093 PHE D CD2 1 +ATOM 9229 C CE1 . PHE D 1 274 ? 39.488 47.624 113.995 1.00 199.59 ? 1093 PHE D CE1 1 +ATOM 9230 C CE2 . PHE D 1 274 ? 41.706 47.608 114.903 1.00 185.62 ? 1093 PHE D CE2 1 +ATOM 9231 C CZ . PHE D 1 274 ? 40.336 47.639 115.091 1.00 179.66 ? 1093 PHE D CZ 1 +ATOM 9232 N N . ARG D 1 275 ? 43.980 49.923 111.362 1.00 216.86 ? 1094 ARG D N 1 +ATOM 9233 C CA . ARG D 1 275 ? 44.705 50.852 112.228 1.00 206.30 ? 1094 ARG D CA 1 +ATOM 9234 C C . ARG D 1 275 ? 44.540 52.284 111.731 1.00 193.51 ? 1094 ARG D C 1 +ATOM 9235 O O . ARG D 1 275 ? 44.342 53.204 112.525 1.00 190.63 ? 1094 ARG D O 1 +ATOM 9236 C CB . ARG D 1 275 ? 46.192 50.487 112.321 1.00 212.02 ? 1094 ARG D CB 1 +ATOM 9237 C CG . ARG D 1 275 ? 46.820 50.752 113.695 1.00 213.49 ? 1094 ARG D CG 1 +ATOM 9238 C CD . ARG D 1 275 ? 48.340 50.596 113.666 1.00 210.19 ? 1094 ARG D CD 1 +ATOM 9239 N NE . ARG D 1 275 ? 48.776 49.629 112.660 1.00 211.70 ? 1094 ARG D NE 1 +ATOM 9240 C CZ . ARG D 1 275 ? 48.995 48.338 112.894 1.00 192.35 ? 1094 ARG D CZ 1 +ATOM 9241 N NH1 . ARG D 1 275 ? 48.827 47.841 114.113 1.00 161.46 ? 1094 ARG D NH1 1 +ATOM 9242 N NH2 . ARG D 1 275 ? 49.388 47.542 111.904 1.00 160.62 ? 1094 ARG D NH2 1 +ATOM 9243 N N . VAL D 1 276 ? 44.621 52.463 110.416 1.00 178.76 ? 1095 VAL D N 1 +ATOM 9244 C CA . VAL D 1 276 ? 44.419 53.771 109.799 1.00 172.95 ? 1095 VAL D CA 1 +ATOM 9245 C C . VAL D 1 276 ? 42.982 54.222 110.012 1.00 167.87 ? 1095 VAL D C 1 +ATOM 9246 O O . VAL D 1 276 ? 42.709 55.411 110.201 1.00 153.34 ? 1095 VAL D O 1 +ATOM 9247 C CB . VAL D 1 276 ? 44.741 53.740 108.291 1.00 177.59 ? 1095 VAL D CB 1 +ATOM 9248 C CG1 . VAL D 1 276 ? 44.243 54.999 107.602 1.00 146.39 ? 1095 VAL D CG1 1 +ATOM 9249 C CG2 . VAL D 1 276 ? 46.234 53.572 108.076 1.00 209.69 ? 1095 VAL D CG2 1 +ATOM 9250 N N . ALA D 1 277 ? 42.070 53.252 109.988 1.00 180.61 ? 1096 ALA D N 1 +ATOM 9251 C CA . ALA D 1 277 ? 40.665 53.497 110.284 1.00 160.25 ? 1096 ALA D CA 1 +ATOM 9252 C C . ALA D 1 277 ? 40.517 53.986 111.720 1.00 154.59 ? 1096 ALA D C 1 +ATOM 9253 O O . ALA D 1 277 ? 39.894 55.021 111.974 1.00 132.68 ? 1096 ALA D O 1 +ATOM 9254 C CB . ALA D 1 277 ? 39.839 52.229 110.056 1.00 130.25 ? 1096 ALA D CB 1 +ATOM 9255 N N . ALA D 1 278 ? 41.115 53.239 112.647 1.00 164.68 ? 1097 ALA D N 1 +ATOM 9256 C CA . ALA D 1 278 ? 41.063 53.564 114.070 1.00 153.70 ? 1097 ALA D CA 1 +ATOM 9257 C C . ALA D 1 278 ? 41.879 54.807 114.419 1.00 149.84 ? 1097 ALA D C 1 +ATOM 9258 O O . ALA D 1 278 ? 41.598 55.475 115.414 1.00 142.40 ? 1097 ALA D O 1 +ATOM 9259 C CB . ALA D 1 278 ? 41.512 52.370 114.913 1.00 127.99 ? 1097 ALA D CB 1 +ATOM 9260 N N . ASP D 1 279 ? 42.886 55.121 113.608 1.00 144.30 ? 1098 ASP D N 1 +ATOM 9261 C CA . ASP D 1 279 ? 43.658 56.343 113.823 1.00 153.64 ? 1098 ASP D CA 1 +ATOM 9262 C C . ASP D 1 279 ? 42.855 57.571 113.383 1.00 177.93 ? 1098 ASP D C 1 +ATOM 9263 O O . ASP D 1 279 ? 42.907 58.628 114.023 1.00 144.03 ? 1098 ASP D O 1 +ATOM 9264 C CB . ASP D 1 279 ? 45.005 56.282 113.097 1.00 146.08 ? 1098 ASP D CB 1 +ATOM 9265 C CG . ASP D 1 279 ? 46.063 57.148 113.759 1.00 167.36 ? 1098 ASP D CG 1 +ATOM 9266 O OD1 . ASP D 1 279 ? 46.131 58.354 113.438 1.00 157.94 ? 1098 ASP D OD1 1 +ATOM 9267 O OD2 . ASP D 1 279 ? 46.820 56.621 114.605 1.00 175.78 ? 1098 ASP D OD2 1 +ATOM 9268 N N . MET D 1 280 ? 42.104 57.421 112.296 1.00 185.46 ? 1099 MET D N 1 +ATOM 9269 C CA . MET D 1 280 ? 41.226 58.482 111.822 1.00 169.58 ? 1099 MET D CA 1 +ATOM 9270 C C . MET D 1 280 ? 40.184 58.826 112.876 1.00 148.29 ? 1099 MET D C 1 +ATOM 9271 O O . MET D 1 280 ? 39.722 59.963 112.956 1.00 141.12 ? 1099 MET D O 1 +ATOM 9272 C CB . MET D 1 280 ? 40.518 58.071 110.530 1.00 186.88 ? 1099 MET D CB 1 +ATOM 9273 C CG . MET D 1 280 ? 41.334 58.267 109.263 1.00 201.16 ? 1099 MET D CG 1 +ATOM 9274 S SD . MET D 1 280 ? 40.334 58.049 107.780 1.00 191.76 ? 1099 MET D SD 1 +ATOM 9275 C CE . MET D 1 280 ? 38.980 59.158 108.155 1.00 112.77 ? 1099 MET D CE 1 +ATOM 9276 N N . PHE D 1 281 ? 39.827 57.836 113.690 1.00 139.86 ? 1100 PHE D N 1 +ATOM 9277 C CA . PHE D 1 281 ? 38.724 57.981 114.634 1.00 153.85 ? 1100 PHE D CA 1 +ATOM 9278 C C . PHE D 1 281 ? 39.152 57.915 116.093 1.00 171.38 ? 1100 PHE D C 1 +ATOM 9279 O O . PHE D 1 281 ? 38.402 57.454 116.957 1.00 158.17 ? 1100 PHE D O 1 +ATOM 9280 C CB . PHE D 1 281 ? 37.653 56.936 114.342 1.00 134.20 ? 1100 PHE D CB 1 +ATOM 9281 C CG . PHE D 1 281 ? 36.972 57.138 113.024 1.00 165.07 ? 1100 PHE D CG 1 +ATOM 9282 C CD1 . PHE D 1 281 ? 36.561 58.406 112.632 1.00 164.60 ? 1100 PHE D CD1 1 +ATOM 9283 C CD2 . PHE D 1 281 ? 36.760 56.070 112.165 1.00 135.21 ? 1100 PHE D CD2 1 +ATOM 9284 C CE1 . PHE D 1 281 ? 35.936 58.602 111.417 1.00 152.60 ? 1100 PHE D CE1 1 +ATOM 9285 C CE2 . PHE D 1 281 ? 36.135 56.257 110.947 1.00 126.42 ? 1100 PHE D CE2 1 +ATOM 9286 C CZ . PHE D 1 281 ? 35.723 57.526 110.571 1.00 146.67 ? 1100 PHE D CZ 1 +ATOM 9287 N N . SER D 1 282 ? 40.362 58.393 116.354 1.00 197.16 ? 1101 SER D N 1 +ATOM 9288 C CA . SER D 1 282 ? 40.886 58.479 117.707 1.00 211.55 ? 1101 SER D CA 1 +ATOM 9289 C C . SER D 1 282 ? 40.372 59.748 118.386 1.00 209.99 ? 1101 SER D C 1 +ATOM 9290 O O . SER D 1 282 ? 40.275 59.819 119.616 1.00 162.17 ? 1101 SER D O 1 +ATOM 9291 C CB . SER D 1 282 ? 42.407 58.467 117.661 1.00 213.44 ? 1101 SER D CB 1 +ATOM 9292 O OG . SER D 1 282 ? 42.907 59.622 116.998 1.00 207.59 ? 1101 SER D OG 1 +ATOM 9293 N N . ASP D 1 283 ? 40.048 60.748 117.571 1.00 215.73 ? 1102 ASP D N 1 +ATOM 9294 C CA . ASP D 1 283 ? 39.396 61.952 118.064 1.00 181.09 ? 1102 ASP D CA 1 +ATOM 9295 C C . ASP D 1 283 ? 37.879 61.756 118.100 1.00 149.10 ? 1102 ASP D C 1 +ATOM 9296 O O . ASP D 1 283 ? 37.143 62.563 118.676 1.00 106.53 ? 1102 ASP D O 1 +ATOM 9297 C CB . ASP D 1 283 ? 39.818 63.189 117.256 1.00 174.53 ? 1102 ASP D CB 1 +ATOM 9298 C CG . ASP D 1 283 ? 39.522 63.093 115.781 1.00 179.69 ? 1102 ASP D CG 1 +ATOM 9299 O OD1 . ASP D 1 283 ? 39.480 61.961 115.263 1.00 195.04 ? 1102 ASP D OD1 1 +ATOM 9300 O OD2 . ASP D 1 283 ? 39.351 64.159 115.135 1.00 143.73 ? 1102 ASP D OD2 1 +ATOM 9301 N N . GLY D 1 284 ? 37.431 60.661 117.485 1.00 141.06 ? 1103 GLY D N 1 +ATOM 9302 C CA . GLY D 1 284 ? 36.053 60.207 117.585 1.00 148.07 ? 1103 GLY D CA 1 +ATOM 9303 C C . GLY D 1 284 ? 35.024 61.216 117.119 1.00 177.29 ? 1103 GLY D C 1 +ATOM 9304 O O . GLY D 1 284 ? 33.906 61.279 117.653 1.00 110.52 ? 1103 GLY D O 1 +ATOM 9305 N N . ASN D 1 285 ? 35.422 62.015 116.130 1.00 218.73 ? 1104 ASN D N 1 +ATOM 9306 C CA . ASN D 1 285 ? 34.555 63.005 115.495 1.00 198.02 ? 1104 ASN D CA 1 +ATOM 9307 C C . ASN D 1 285 ? 34.135 62.544 114.099 1.00 155.04 ? 1104 ASN D C 1 +ATOM 9308 O O . ASN D 1 285 ? 34.658 63.027 113.092 1.00 138.05 ? 1104 ASN D O 1 +ATOM 9309 C CB . ASN D 1 285 ? 35.247 64.375 115.406 1.00 178.03 ? 1104 ASN D CB 1 +ATOM 9310 C CG . ASN D 1 285 ? 35.628 64.941 116.771 1.00 179.05 ? 1104 ASN D CG 1 +ATOM 9311 O OD1 . ASN D 1 285 ? 35.099 64.524 117.803 1.00 170.13 ? 1104 ASN D OD1 1 +ATOM 9312 N ND2 . ASN D 1 285 ? 36.547 65.903 116.776 1.00 141.48 ? 1104 ASN D ND2 1 +ATOM 9313 N N . PHE D 1 286 ? 33.184 61.607 114.064 1.00 146.11 ? 1105 PHE D N 1 +ATOM 9314 C CA . PHE D 1 286 ? 32.669 61.013 112.831 1.00 159.87 ? 1105 PHE D CA 1 +ATOM 9315 C C . PHE D 1 286 ? 31.832 62.002 112.021 1.00 197.51 ? 1105 PHE D C 1 +ATOM 9316 O O . PHE D 1 286 ? 30.974 62.698 112.564 1.00 207.01 ? 1105 PHE D O 1 +ATOM 9317 C CB . PHE D 1 286 ? 31.766 59.806 113.139 1.00 147.58 ? 1105 PHE D CB 1 +ATOM 9318 C CG . PHE D 1 286 ? 32.465 58.640 113.802 1.00 192.99 ? 1105 PHE D CG 1 +ATOM 9319 C CD1 . PHE D 1 286 ? 33.162 57.714 113.045 1.00 225.62 ? 1105 PHE D CD1 1 +ATOM 9320 C CD2 . PHE D 1 286 ? 32.372 58.439 115.176 1.00 158.84 ? 1105 PHE D CD2 1 +ATOM 9321 C CE1 . PHE D 1 286 ? 33.783 56.630 113.645 1.00 224.38 ? 1105 PHE D CE1 1 +ATOM 9322 C CE2 . PHE D 1 286 ? 32.996 57.362 115.782 1.00 127.78 ? 1105 PHE D CE2 1 +ATOM 9323 C CZ . PHE D 1 286 ? 33.701 56.455 115.015 1.00 175.91 ? 1105 PHE D CZ 1 +ATOM 9324 N N . ASN D 1 287 ? 32.083 62.039 110.717 1.00 207.08 ? 1106 ASN D N 1 +ATOM 9325 C CA . ASN D 1 287 ? 31.219 62.719 109.756 1.00 180.15 ? 1106 ASN D CA 1 +ATOM 9326 C C . ASN D 1 287 ? 31.286 61.977 108.422 1.00 173.33 ? 1106 ASN D C 1 +ATOM 9327 O O . ASN D 1 287 ? 32.302 61.350 108.111 1.00 149.79 ? 1106 ASN D O 1 +ATOM 9328 C CB . ASN D 1 287 ? 31.610 64.193 109.590 1.00 168.06 ? 1106 ASN D CB 1 +ATOM 9329 C CG . ASN D 1 287 ? 33.115 64.407 109.591 1.00 161.26 ? 1106 ASN D CG 1 +ATOM 9330 O OD1 . ASN D 1 287 ? 33.827 63.924 108.709 1.00 149.31 ? 1106 ASN D OD1 1 +ATOM 9331 N ND2 . ASN D 1 287 ? 33.604 65.147 110.580 1.00 137.67 ? 1106 ASN D ND2 1 +ATOM 9332 N N . TRP D 1 288 ? 30.206 62.039 107.645 1.00 170.85 ? 1107 TRP D N 1 +ATOM 9333 C CA . TRP D 1 288 ? 30.111 61.312 106.378 1.00 129.01 ? 1107 TRP D CA 1 +ATOM 9334 C C . TRP D 1 288 ? 31.284 61.533 105.432 1.00 133.05 ? 1107 TRP D C 1 +ATOM 9335 O O . TRP D 1 288 ? 31.601 60.664 104.627 1.00 128.93 ? 1107 TRP D O 1 +ATOM 9336 C CB . TRP D 1 288 ? 28.821 61.669 105.654 1.00 132.69 ? 1107 TRP D CB 1 +ATOM 9337 C CG . TRP D 1 288 ? 27.864 60.556 105.635 1.00 173.61 ? 1107 TRP D CG 1 +ATOM 9338 C CD1 . TRP D 1 288 ? 26.673 60.492 106.287 1.00 204.44 ? 1107 TRP D CD1 1 +ATOM 9339 C CD2 . TRP D 1 288 ? 28.014 59.313 104.940 1.00 191.54 ? 1107 TRP D CD2 1 +ATOM 9340 N NE1 . TRP D 1 288 ? 26.061 59.289 106.032 1.00 228.49 ? 1107 TRP D NE1 1 +ATOM 9341 C CE2 . TRP D 1 288 ? 26.865 58.547 105.207 1.00 221.37 ? 1107 TRP D CE2 1 +ATOM 9342 C CE3 . TRP D 1 288 ? 29.003 58.778 104.113 1.00 176.44 ? 1107 TRP D CE3 1 +ATOM 9343 C CZ2 . TRP D 1 288 ? 26.680 57.268 104.676 1.00 199.22 ? 1107 TRP D CZ2 1 +ATOM 9344 C CZ3 . TRP D 1 288 ? 28.817 57.509 103.584 1.00 157.01 ? 1107 TRP D CZ3 1 +ATOM 9345 C CH2 . TRP D 1 288 ? 27.667 56.768 103.872 1.00 148.63 ? 1107 TRP D CH2 1 +ATOM 9346 N N . GLY D 1 289 ? 31.915 62.698 105.523 1.00 128.84 ? 1108 GLY D N 1 +ATOM 9347 C CA . GLY D 1 289 ? 33.089 62.990 104.724 1.00 144.35 ? 1108 GLY D CA 1 +ATOM 9348 C C . GLY D 1 289 ? 34.202 61.979 104.937 1.00 164.96 ? 1108 GLY D C 1 +ATOM 9349 O O . GLY D 1 289 ? 34.841 61.534 103.983 1.00 144.86 ? 1108 GLY D O 1 +ATOM 9350 N N . ARG D 1 290 ? 34.428 61.611 106.195 1.00 166.04 ? 1109 ARG D N 1 +ATOM 9351 C CA . ARG D 1 290 ? 35.470 60.649 106.539 1.00 137.65 ? 1109 ARG D CA 1 +ATOM 9352 C C . ARG D 1 290 ? 35.062 59.220 106.205 1.00 143.84 ? 1109 ARG D C 1 +ATOM 9353 O O . ARG D 1 290 ? 35.897 58.406 105.809 1.00 135.70 ? 1109 ARG D O 1 +ATOM 9354 C CB . ARG D 1 290 ? 35.814 60.746 108.019 1.00 106.14 ? 1109 ARG D CB 1 +ATOM 9355 C CG . ARG D 1 290 ? 36.599 61.978 108.396 1.00 135.74 ? 1109 ARG D CG 1 +ATOM 9356 C CD . ARG D 1 290 ? 37.072 61.857 109.827 1.00 159.18 ? 1109 ARG D CD 1 +ATOM 9357 N NE . ARG D 1 290 ? 37.760 63.054 110.291 1.00 165.07 ? 1109 ARG D NE 1 +ATOM 9358 C CZ . ARG D 1 290 ? 38.145 63.244 111.548 1.00 180.87 ? 1109 ARG D CZ 1 +ATOM 9359 N NH1 . ARG D 1 290 ? 37.902 62.313 112.464 1.00 193.12 ? 1109 ARG D NH1 1 +ATOM 9360 N NH2 . ARG D 1 290 ? 38.767 64.364 111.889 1.00 167.19 ? 1109 ARG D NH2 1 +ATOM 9361 N N . VAL D 1 291 ? 33.778 58.923 106.383 1.00 141.41 ? 1110 VAL D N 1 +ATOM 9362 C CA . VAL D 1 291 ? 33.212 57.633 106.010 1.00 119.77 ? 1110 VAL D CA 1 +ATOM 9363 C C . VAL D 1 291 ? 33.476 57.374 104.530 1.00 127.91 ? 1110 VAL D C 1 +ATOM 9364 O O . VAL D 1 291 ? 33.792 56.254 104.118 1.00 132.79 ? 1110 VAL D O 1 +ATOM 9365 C CB . VAL D 1 291 ? 31.695 57.617 106.263 1.00 143.43 ? 1110 VAL D CB 1 +ATOM 9366 C CG1 . VAL D 1 291 ? 31.092 56.278 105.864 1.00 144.47 ? 1110 VAL D CG1 1 +ATOM 9367 C CG2 . VAL D 1 291 ? 31.407 57.933 107.717 1.00 115.57 ? 1110 VAL D CG2 1 +ATOM 9368 N N . VAL D 1 292 ? 33.363 58.435 103.741 1.00 129.73 ? 1111 VAL D N 1 +ATOM 9369 C CA . VAL D 1 292 ? 33.574 58.356 102.307 1.00 130.96 ? 1111 VAL D CA 1 +ATOM 9370 C C . VAL D 1 292 ? 35.062 58.383 101.959 1.00 130.31 ? 1111 VAL D C 1 +ATOM 9371 O O . VAL D 1 292 ? 35.515 57.607 101.119 1.00 139.92 ? 1111 VAL D O 1 +ATOM 9372 C CB . VAL D 1 292 ? 32.831 59.487 101.578 1.00 118.02 ? 1111 VAL D CB 1 +ATOM 9373 C CG1 . VAL D 1 292 ? 33.166 59.483 100.118 1.00 79.22 ? 1111 VAL D CG1 1 +ATOM 9374 C CG2 . VAL D 1 292 ? 31.344 59.321 101.751 1.00 136.43 ? 1111 VAL D CG2 1 +ATOM 9375 N N . ALA D 1 293 ? 35.823 59.258 102.613 1.00 122.36 ? 1112 ALA D N 1 +ATOM 9376 C CA . ALA D 1 293 ? 37.262 59.344 102.350 1.00 127.90 ? 1112 ALA D CA 1 +ATOM 9377 C C . ALA D 1 293 ? 37.980 58.066 102.777 1.00 149.56 ? 1112 ALA D C 1 +ATOM 9378 O O . ALA D 1 293 ? 39.030 57.716 102.238 1.00 136.99 ? 1112 ALA D O 1 +ATOM 9379 C CB . ALA D 1 293 ? 37.882 60.571 103.025 1.00 119.61 ? 1112 ALA D CB 1 +ATOM 9380 N N . LEU D 1 294 ? 37.404 57.361 103.739 1.00 155.95 ? 1113 LEU D N 1 +ATOM 9381 C CA . LEU D 1 294 ? 37.952 56.077 104.130 1.00 148.17 ? 1113 LEU D CA 1 +ATOM 9382 C C . LEU D 1 294 ? 37.395 54.978 103.224 1.00 134.05 ? 1113 LEU D C 1 +ATOM 9383 O O . LEU D 1 294 ? 37.981 53.905 103.097 1.00 139.40 ? 1113 LEU D O 1 +ATOM 9384 C CB . LEU D 1 294 ? 37.662 55.803 105.603 1.00 116.02 ? 1113 LEU D CB 1 +ATOM 9385 C CG . LEU D 1 294 ? 38.243 54.529 106.196 1.00 138.49 ? 1113 LEU D CG 1 +ATOM 9386 C CD1 . LEU D 1 294 ? 38.702 54.817 107.595 1.00 128.33 ? 1113 LEU D CD1 1 +ATOM 9387 C CD2 . LEU D 1 294 ? 37.183 53.453 106.203 1.00 171.20 ? 1113 LEU D CD2 1 +ATOM 9388 N N . PHE D 1 295 ? 36.267 55.260 102.582 1.00 110.36 ? 1114 PHE D N 1 +ATOM 9389 C CA . PHE D 1 295 ? 35.704 54.334 101.608 1.00 137.03 ? 1114 PHE D CA 1 +ATOM 9390 C C . PHE D 1 295 ? 36.318 54.549 100.224 1.00 152.36 ? 1114 PHE D C 1 +ATOM 9391 O O . PHE D 1 295 ? 36.042 53.794 99.300 1.00 166.77 ? 1114 PHE D O 1 +ATOM 9392 C CB . PHE D 1 295 ? 34.181 54.470 101.544 1.00 143.37 ? 1114 PHE D CB 1 +ATOM 9393 C CG . PHE D 1 295 ? 33.489 53.302 100.889 1.00 171.32 ? 1114 PHE D CG 1 +ATOM 9394 C CD1 . PHE D 1 295 ? 33.278 52.122 101.592 1.00 176.47 ? 1114 PHE D CD1 1 +ATOM 9395 C CD2 . PHE D 1 295 ? 33.039 53.385 99.577 1.00 147.73 ? 1114 PHE D CD2 1 +ATOM 9396 C CE1 . PHE D 1 295 ? 32.635 51.046 100.998 1.00 178.50 ? 1114 PHE D CE1 1 +ATOM 9397 C CE2 . PHE D 1 295 ? 32.396 52.312 98.975 1.00 156.96 ? 1114 PHE D CE2 1 +ATOM 9398 C CZ . PHE D 1 295 ? 32.193 51.141 99.688 1.00 181.78 ? 1114 PHE D CZ 1 +ATOM 9399 N N . TYR D 1 296 ? 37.128 55.597 100.084 1.00 153.28 ? 1115 TYR D N 1 +ATOM 9400 C CA . TYR D 1 296 ? 37.950 55.810 98.892 1.00 154.84 ? 1115 TYR D CA 1 +ATOM 9401 C C . TYR D 1 296 ? 39.247 55.077 99.186 1.00 169.43 ? 1115 TYR D C 1 +ATOM 9402 O O . TYR D 1 296 ? 39.910 54.564 98.286 1.00 148.39 ? 1115 TYR D O 1 +ATOM 9403 C CB . TYR D 1 296 ? 38.162 57.332 98.672 1.00 153.83 ? 1115 TYR D CB 1 +ATOM 9404 C CG . TYR D 1 296 ? 39.091 57.806 97.533 1.00 167.92 ? 1115 TYR D CG 1 +ATOM 9405 C CD1 . TYR D 1 296 ? 38.672 57.844 96.198 1.00 194.46 ? 1115 TYR D CD1 1 +ATOM 9406 C CD2 . TYR D 1 296 ? 40.388 58.205 97.805 1.00 161.17 ? 1115 TYR D CD2 1 +ATOM 9407 C CE1 . TYR D 1 296 ? 39.535 58.277 95.180 1.00 200.13 ? 1115 TYR D CE1 1 +ATOM 9408 C CE2 . TYR D 1 296 ? 41.245 58.636 96.800 1.00 158.27 ? 1115 TYR D CE2 1 +ATOM 9409 C CZ . TYR D 1 296 ? 40.820 58.668 95.492 1.00 158.53 ? 1115 TYR D CZ 1 +ATOM 9410 O OH . TYR D 1 296 ? 41.689 59.094 94.508 1.00 130.91 ? 1115 TYR D OH 1 +ATOM 9411 N N . PHE D 1 297 ? 39.594 55.012 100.467 1.00 173.52 ? 1116 PHE D N 1 +ATOM 9412 C CA . PHE D 1 297 ? 40.776 54.276 100.882 1.00 162.43 ? 1116 PHE D CA 1 +ATOM 9413 C C . PHE D 1 297 ? 40.549 52.770 100.721 1.00 146.72 ? 1116 PHE D C 1 +ATOM 9414 O O . PHE D 1 297 ? 41.184 52.133 99.882 1.00 114.16 ? 1116 PHE D O 1 +ATOM 9415 C CB . PHE D 1 297 ? 41.160 54.635 102.316 1.00 164.62 ? 1116 PHE D CB 1 +ATOM 9416 C CG . PHE D 1 297 ? 42.552 54.224 102.685 1.00 188.48 ? 1116 PHE D CG 1 +ATOM 9417 C CD1 . PHE D 1 297 ? 43.641 54.949 102.238 1.00 170.82 ? 1116 PHE D CD1 1 +ATOM 9418 C CD2 . PHE D 1 297 ? 42.772 53.107 103.472 1.00 220.77 ? 1116 PHE D CD2 1 +ATOM 9419 C CE1 . PHE D 1 297 ? 44.920 54.575 102.576 1.00 193.28 ? 1116 PHE D CE1 1 +ATOM 9420 C CE2 . PHE D 1 297 ? 44.053 52.724 103.811 1.00 218.53 ? 1116 PHE D CE2 1 +ATOM 9421 C CZ . PHE D 1 297 ? 45.127 53.458 103.362 1.00 211.87 ? 1116 PHE D CZ 1 +ATOM 9422 N N . ALA D 1 298 ? 39.624 52.210 101.502 1.00 139.16 ? 1117 ALA D N 1 +ATOM 9423 C CA . ALA D 1 298 ? 39.229 50.806 101.356 1.00 153.95 ? 1117 ALA D CA 1 +ATOM 9424 C C . ALA D 1 298 ? 38.911 50.452 99.897 1.00 183.44 ? 1117 ALA D C 1 +ATOM 9425 O O . ALA D 1 298 ? 39.064 49.304 99.470 1.00 175.07 ? 1117 ALA D O 1 +ATOM 9426 C CB . ALA D 1 298 ? 38.039 50.496 102.255 1.00 150.75 ? 1117 ALA D CB 1 +ATOM 9427 N N . SER D 1 299 ? 38.464 51.452 99.142 1.00 196.96 ? 1118 SER D N 1 +ATOM 9428 C CA . SER D 1 299 ? 38.343 51.343 97.695 1.00 183.53 ? 1118 SER D CA 1 +ATOM 9429 C C . SER D 1 299 ? 39.722 51.044 97.108 1.00 170.70 ? 1118 SER D C 1 +ATOM 9430 O O . SER D 1 299 ? 39.957 49.950 96.602 1.00 181.68 ? 1118 SER D O 1 +ATOM 9431 C CB . SER D 1 299 ? 37.778 52.643 97.110 1.00 175.38 ? 1118 SER D CB 1 +ATOM 9432 O OG . SER D 1 299 ? 37.363 52.507 95.762 1.00 175.08 ? 1118 SER D OG 1 +ATOM 9433 N N . LYS D 1 300 ? 40.639 52.007 97.211 1.00 142.12 ? 1119 LYS D N 1 +ATOM 9434 C CA . LYS D 1 300 ? 41.992 51.875 96.659 1.00 147.65 ? 1119 LYS D CA 1 +ATOM 9435 C C . LYS D 1 300 ? 42.769 50.631 97.126 1.00 195.46 ? 1119 LYS D C 1 +ATOM 9436 O O . LYS D 1 300 ? 43.795 50.285 96.539 1.00 196.81 ? 1119 LYS D O 1 +ATOM 9437 C CB . LYS D 1 300 ? 42.814 53.135 96.950 1.00 145.02 ? 1119 LYS D CB 1 +ATOM 9438 C CG . LYS D 1 300 ? 42.430 54.368 96.139 1.00 138.23 ? 1119 LYS D CG 1 +ATOM 9439 C CD . LYS D 1 300 ? 43.031 54.340 94.739 1.00 108.79 ? 1119 LYS D CD 1 +ATOM 9440 C CE . LYS D 1 300 ? 43.077 55.739 94.117 1.00 136.84 ? 1119 LYS D CE 1 +ATOM 9441 N NZ . LYS D 1 300 ? 43.188 55.716 92.615 1.00 139.11 ? 1119 LYS D NZ 1 +ATOM 9442 N N . LEU D 1 301 ? 42.288 49.967 98.175 1.00 213.91 ? 1120 LEU D N 1 +ATOM 9443 C CA . LEU D 1 301 ? 42.880 48.708 98.631 1.00 184.38 ? 1120 LEU D CA 1 +ATOM 9444 C C . LEU D 1 301 ? 42.345 47.540 97.815 1.00 178.04 ? 1120 LEU D C 1 +ATOM 9445 O O . LEU D 1 301 ? 41.733 46.615 98.356 1.00 141.59 ? 1120 LEU D O 1 +ATOM 9446 C CB . LEU D 1 301 ? 42.595 48.483 100.115 1.00 160.78 ? 1120 LEU D CB 1 +ATOM 9447 C CG . LEU D 1 301 ? 43.192 49.563 101.017 1.00 177.72 ? 1120 LEU D CG 1 +ATOM 9448 C CD1 . LEU D 1 301 ? 42.885 49.296 102.490 1.00 168.84 ? 1120 LEU D CD1 1 +ATOM 9449 C CD2 . LEU D 1 301 ? 44.696 49.698 100.768 1.00 160.74 ? 1120 LEU D CD2 1 +ATOM 9450 N N . VAL D 1 302 ? 42.585 47.602 96.507 1.00 202.34 ? 1121 VAL D N 1 +ATOM 9451 C CA . VAL D 1 302 ? 42.068 46.628 95.553 1.00 222.53 ? 1121 VAL D CA 1 +ATOM 9452 C C . VAL D 1 302 ? 43.060 46.403 94.405 1.00 223.56 ? 1121 VAL D C 1 +ATOM 9453 O O . VAL D 1 302 ? 43.584 45.298 94.240 1.00 237.03 ? 1121 VAL D O 1 +ATOM 9454 C CB . VAL D 1 302 ? 40.684 47.070 94.990 1.00 173.02 ? 1121 VAL D CB 1 +ATOM 9455 C CG1 . VAL D 1 302 ? 40.338 46.320 93.706 1.00 154.21 ? 1121 VAL D CG1 1 +ATOM 9456 C CG2 . VAL D 1 302 ? 39.582 46.884 96.037 1.00 155.20 ? 1121 VAL D CG2 1 +ATOM 9457 N N . LEU D 1 303 ? 43.327 47.461 93.638 1.00 197.31 ? 1122 LEU D N 1 +ATOM 9458 C CA . LEU D 1 303 ? 44.127 47.377 92.410 1.00 207.15 ? 1122 LEU D CA 1 +ATOM 9459 C C . LEU D 1 303 ? 45.489 46.696 92.579 1.00 211.26 ? 1122 LEU D C 1 +ATOM 9460 O O . LEU D 1 303 ? 45.945 45.972 91.689 1.00 196.84 ? 1122 LEU D O 1 +ATOM 9461 C CB . LEU D 1 303 ? 44.309 48.771 91.789 1.00 196.42 ? 1122 LEU D CB 1 +ATOM 9462 C CG . LEU D 1 303 ? 43.367 49.177 90.645 1.00 178.49 ? 1122 LEU D CG 1 +ATOM 9463 C CD1 . LEU D 1 303 ? 43.612 50.621 90.201 1.00 137.44 ? 1122 LEU D CD1 1 +ATOM 9464 C CD2 . LEU D 1 303 ? 43.486 48.224 89.454 1.00 135.41 ? 1122 LEU D CD2 1 +HETATM 9465 O O . HOH E 2 . ? 17.948 82.663 103.679 1.00 111.61 ? 2001 HOH A O 1 +HETATM 9466 O O . HOH E 2 . ? 17.970 80.897 105.286 1.00 123.87 ? 2002 HOH A O 1 +HETATM 9467 O O . HOH E 2 . ? 8.966 83.223 113.024 1.00 95.94 ? 2003 HOH A O 1 +HETATM 9468 O O . HOH E 2 . ? 14.721 119.076 113.307 1.00 108.67 ? 2004 HOH A O 1 +HETATM 9469 O O . HOH E 2 . ? 8.167 120.568 111.255 1.00 72.31 ? 2005 HOH A O 1 +HETATM 9470 O O . HOH E 2 . ? 7.571 118.071 110.049 1.00 80.40 ? 2006 HOH A O 1 +HETATM 9471 O O . HOH E 2 . ? 18.178 101.777 106.140 1.00 101.60 ? 2007 HOH A O 1 +HETATM 9472 O O . HOH E 2 . ? 5.600 101.229 99.907 1.00 105.93 ? 2008 HOH A O 1 +HETATM 9473 O O . HOH E 2 . ? 13.404 97.495 104.608 1.00 94.35 ? 2009 HOH A O 1 +HETATM 9474 O O . HOH E 2 . ? 17.912 97.405 104.155 1.00 146.00 ? 2010 HOH A O 1 +HETATM 9475 O O . HOH E 2 . ? 32.829 88.233 109.617 1.00 102.09 ? 2011 HOH A O 1 +HETATM 9476 O O . HOH E 2 . ? 17.985 115.502 92.696 1.00 98.40 ? 2012 HOH A O 1 +HETATM 9477 O O . HOH E 2 . ? 11.482 121.392 96.756 1.00 121.24 ? 2013 HOH A O 1 +HETATM 9478 O O . HOH E 2 . ? 23.285 114.874 98.966 1.00 99.10 ? 2014 HOH A O 1 +HETATM 9479 O O . HOH E 2 . ? 3.382 112.520 99.217 1.00 112.58 ? 2015 HOH A O 1 +HETATM 9480 O O . HOH E 2 . ? 1.371 103.571 109.516 1.00 93.66 ? 2016 HOH A O 1 +HETATM 9481 O O . HOH E 2 . ? 11.004 114.313 122.424 1.00 78.32 ? 2017 HOH A O 1 +HETATM 9482 O O . HOH E 2 . ? 12.803 83.449 87.500 1.00 104.39 ? 2018 HOH A O 1 +HETATM 9483 O O . HOH F 2 . ? 13.477 114.588 50.503 1.00 110.16 ? 4001 HOH A O 1 +HETATM 9484 O O . HOH F 2 . ? 4.167 114.487 69.668 1.00 84.24 ? 4002 HOH A O 1 +HETATM 9485 O O . HOH G 2 . ? 11.389 105.836 22.223 1.00 93.99 ? 2001 HOH B O 1 +HETATM 9486 O O . HOH G 2 . ? 7.701 73.915 22.754 1.00 80.36 ? 2002 HOH B O 1 +HETATM 9487 O O . HOH G 2 . ? 5.118 79.369 27.395 1.00 51.28 ? 2003 HOH B O 1 +HETATM 9488 O O . HOH G 2 . ? 10.855 86.572 33.123 1.00 100.55 ? 2004 HOH B O 1 +HETATM 9489 O O . HOH G 2 . ? 13.823 86.037 31.417 1.00 118.65 ? 2005 HOH B O 1 +HETATM 9490 O O . HOH G 2 . ? 18.058 87.676 31.536 1.00 90.27 ? 2006 HOH B O 1 +HETATM 9491 O O . HOH G 2 . ? 5.656 93.318 34.820 1.00 107.62 ? 2007 HOH B O 1 +HETATM 9492 O O . HOH G 2 . ? 12.592 95.839 30.009 1.00 96.70 ? 2008 HOH B O 1 +HETATM 9493 O O . HOH G 2 . ? 17.533 97.760 29.854 1.00 117.55 ? 2009 HOH B O 1 +HETATM 9494 O O . HOH G 2 . ? 19.298 93.690 27.676 1.00 99.54 ? 2010 HOH B O 1 +HETATM 9495 O O . HOH G 2 . ? 10.384 78.722 44.675 1.00 93.65 ? 2011 HOH B O 1 +HETATM 9496 O O . HOH G 2 . ? 11.588 72.598 36.836 1.00 113.77 ? 2012 HOH B O 1 +HETATM 9497 O O . HOH G 2 . ? 23.136 79.032 35.196 1.00 86.43 ? 2013 HOH B O 1 +HETATM 9498 O O . HOH G 2 . ? -0.929 87.495 29.562 1.00 67.40 ? 2014 HOH B O 1 +HETATM 9499 O O . HOH G 2 . ? 3.225 90.796 41.018 1.00 109.65 ? 2015 HOH B O 1 +HETATM 9500 O O . HOH G 2 . ? 8.254 80.121 44.262 1.00 91.42 ? 2016 HOH B O 1 +HETATM 9501 O O . HOH G 2 . ? 0.625 91.091 24.307 1.00 76.66 ? 2017 HOH B O 1 +HETATM 9502 O O . HOH G 2 . ? 10.971 80.350 11.578 1.00 73.47 ? 2018 HOH B O 1 +HETATM 9503 O O . HOH H 2 . ? 16.012 87.842 60.195 1.00 113.34 ? 4001 HOH B O 1 +HETATM 9504 O O . HOH H 2 . ? 12.327 82.035 68.478 1.00 99.21 ? 4002 HOH B O 1 +HETATM 9505 O O . HOH H 2 . ? 4.091 85.220 68.521 1.00 104.76 ? 4003 HOH B O 1 +HETATM 9506 O O . HOH H 2 . ? 2.490 80.075 63.383 1.00 95.16 ? 4004 HOH B O 1 +HETATM 9507 O O . HOH I 2 . ? 41.431 54.358 143.317 1.00 86.29 ? 2001 HOH C O 1 +HETATM 9508 O O . HOH I 2 . ? 42.882 51.170 143.770 1.00 156.10 ? 2002 HOH C O 1 +HETATM 9509 O O . HOH I 2 . ? 16.831 72.370 144.658 1.00 112.76 ? 2003 HOH C O 1 +HETATM 9510 O O . HOH I 2 . ? 12.011 67.173 142.516 1.00 86.79 ? 2004 HOH C O 1 +HETATM 9511 O O . HOH I 2 . ? 14.984 61.812 138.106 1.00 50.91 ? 2005 HOH C O 1 +HETATM 9512 O O . HOH I 2 . ? 28.635 69.126 133.733 1.00 83.11 ? 2006 HOH C O 1 +HETATM 9513 O O . HOH I 2 . ? 33.884 60.506 135.699 1.00 89.77 ? 2007 HOH C O 1 +HETATM 9514 O O . HOH I 2 . ? 37.160 63.546 136.415 1.00 130.78 ? 2008 HOH C O 1 +HETATM 9515 O O . HOH I 2 . ? 13.508 69.343 125.874 1.00 88.42 ? 2009 HOH C O 1 +HETATM 9516 O O . HOH I 2 . ? 12.762 70.824 128.168 1.00 107.31 ? 2010 HOH C O 1 +HETATM 9517 O O . HOH I 2 . ? 24.566 77.751 130.011 1.00 90.38 ? 2011 HOH C O 1 +HETATM 9518 O O . HOH I 2 . ? 12.795 80.204 127.755 1.00 73.70 ? 2012 HOH C O 1 +HETATM 9519 O O . HOH I 2 . ? 19.099 52.696 135.644 1.00 71.46 ? 2013 HOH C O 1 +HETATM 9520 O O . HOH I 2 . ? 18.740 57.822 142.756 1.00 134.15 ? 2014 HOH C O 1 +HETATM 9521 O O . HOH I 2 . ? 19.596 58.527 130.386 1.00 85.11 ? 2015 HOH C O 1 +HETATM 9522 O O . HOH I 2 . ? 23.130 57.359 128.644 1.00 102.36 ? 2016 HOH C O 1 +HETATM 9523 O O . HOH I 2 . ? 17.878 64.082 121.085 1.00 103.38 ? 2017 HOH C O 1 +HETATM 9524 O O . HOH I 2 . ? 23.236 52.406 141.225 1.00 78.85 ? 2018 HOH C O 1 +HETATM 9525 O O . HOH I 2 . ? 18.910 66.479 153.799 1.00 80.60 ? 2019 HOH C O 1 +HETATM 9526 O O . HOH J 2 . ? 27.469 67.399 105.602 1.00 120.62 ? 4001 HOH C O 1 +HETATM 9527 O O . HOH J 2 . ? 21.290 68.796 95.539 1.00 199.84 ? 4002 HOH C O 1 +HETATM 9528 O O . HOH J 2 . ? 21.189 67.065 97.034 1.00 107.94 ? 4003 HOH C O 1 +HETATM 9529 O O . HOH J 2 . ? 14.681 60.011 102.100 1.00 96.71 ? 4004 HOH C O 1 +HETATM 9530 O O . HOH K 2 . ? 21.353 71.453 59.782 1.00 97.69 ? 2001 HOH D O 1 +HETATM 9531 O O . HOH K 2 . ? 20.095 63.826 52.022 1.00 83.51 ? 2002 HOH D O 1 +HETATM 9532 O O . HOH K 2 . ? 54.343 50.124 51.924 1.00 117.40 ? 2003 HOH D O 1 +HETATM 9533 O O . HOH K 2 . ? 52.029 44.056 54.054 1.00 87.14 ? 2004 HOH D O 1 +HETATM 9534 O O . HOH K 2 . ? 46.407 44.373 58.788 1.00 45.28 ? 2005 HOH D O 1 +HETATM 9535 O O . HOH K 2 . ? 40.914 62.686 58.907 1.00 89.91 ? 2006 HOH D O 1 +HETATM 9536 O O . HOH K 2 . ? 34.587 51.255 65.361 1.00 118.93 ? 2007 HOH D O 1 +HETATM 9537 O O . HOH K 2 . ? 35.832 64.191 58.779 1.00 144.05 ? 2008 HOH D O 1 +HETATM 9538 O O . HOH K 2 . ? 34.576 59.812 60.213 1.00 83.92 ? 2009 HOH D O 1 +HETATM 9539 O O . HOH K 2 . ? 29.435 66.249 61.831 1.00 102.60 ? 2010 HOH D O 1 +HETATM 9540 O O . HOH K 2 . ? 53.003 55.352 72.707 1.00 89.14 ? 2011 HOH D O 1 +HETATM 9541 O O . HOH K 2 . ? 54.508 46.472 68.871 1.00 119.48 ? 2012 HOH D O 1 +HETATM 9542 O O . HOH K 2 . ? 49.272 42.401 59.693 1.00 77.92 ? 2013 HOH D O 1 +HETATM 9543 O O . HOH K 2 . ? 42.987 43.880 66.402 1.00 109.01 ? 2014 HOH D O 1 +HETATM 9544 O O . HOH K 2 . ? 38.202 48.346 68.454 1.00 146.44 ? 2015 HOH D O 1 +HETATM 9545 O O . HOH K 2 . ? 33.836 46.315 55.794 1.00 84.03 ? 2016 HOH D O 1 +HETATM 9546 O O . HOH K 2 . ? 48.133 49.483 42.805 1.00 86.16 ? 2017 HOH D O 1 +HETATM 9547 O O . HOH K 2 . ? 22.542 66.382 78.683 1.00 94.52 ? 2018 HOH D O 1 +HETATM 9548 O O . HOH L 2 . ? 45.179 43.993 95.906 1.00 73.49 ? 4001 HOH D O 1 +# +loop_ +_atom_site_anisotrop.id +_atom_site_anisotrop.type_symbol +_atom_site_anisotrop.pdbx_label_atom_id +_atom_site_anisotrop.pdbx_label_alt_id +_atom_site_anisotrop.pdbx_label_comp_id +_atom_site_anisotrop.pdbx_label_asym_id +_atom_site_anisotrop.pdbx_label_seq_id +_atom_site_anisotrop.pdbx_PDB_ins_code +_atom_site_anisotrop.U[1][1] +_atom_site_anisotrop.U[2][2] +_atom_site_anisotrop.U[3][3] +_atom_site_anisotrop.U[1][2] +_atom_site_anisotrop.U[1][3] +_atom_site_anisotrop.U[2][3] +_atom_site_anisotrop.pdbx_auth_seq_id +_atom_site_anisotrop.pdbx_auth_comp_id +_atom_site_anisotrop.pdbx_auth_asym_id +_atom_site_anisotrop.pdbx_auth_atom_id +1 N N . SER A 5 ? 1.6562 0.9542 0.9110 -0.2770 0.1713 -0.0623 2 SER A N +2 C CA . SER A 5 ? 2.3820 1.6802 1.6343 -0.2773 0.1694 -0.0611 2 SER A CA +3 C C . SER A 5 ? 2.3502 1.6500 1.6063 -0.2753 0.1680 -0.0605 2 SER A C +4 O O . SER A 5 ? 1.8507 1.1517 1.1105 -0.2735 0.1678 -0.0606 2 SER A O +5 C CB . SER A 5 ? 2.3509 1.6489 1.5987 -0.2781 0.1680 -0.0603 2 SER A CB +6 O OG . SER A 5 ? 2.2875 1.5871 1.5371 -0.2764 0.1664 -0.0595 2 SER A OG +7 N N . LYS A 6 ? 2.4036 1.7032 1.6588 -0.2755 0.1669 -0.0599 3 LYS A N +8 C CA . LYS A 6 ? 2.3565 1.6575 1.6149 -0.2738 0.1655 -0.0593 3 LYS A CA +9 C C . LYS A 6 ? 2.3304 1.6325 1.5874 -0.2731 0.1633 -0.0582 3 LYS A C +10 O O . LYS A 6 ? 2.2088 1.5124 1.4689 -0.2714 0.1621 -0.0577 3 LYS A O +11 C CB . LYS A 6 ? 2.6354 1.9359 1.8936 -0.2743 0.1651 -0.0590 3 LYS A CB +12 C CG . LYS A 6 ? 2.8857 2.1847 2.1435 -0.2757 0.1672 -0.0600 3 LYS A CG +13 C CD . LYS A 6 ? 2.9804 2.2795 2.2424 -0.2747 0.1690 -0.0611 3 LYS A CD +14 C CE . LYS A 6 ? 2.6886 1.9863 1.9486 -0.2763 0.1711 -0.0622 3 LYS A CE +15 N NZ . LYS A 6 ? 2.3833 1.6813 1.6473 -0.2753 0.1727 -0.0633 3 LYS A NZ +16 N N . GLY A 7 ? 2.3071 1.6085 1.5595 -0.2745 0.1628 -0.0578 4 GLY A N +17 C CA . GLY A 7 ? 2.1821 1.4844 1.4328 -0.2741 0.1608 -0.0569 4 GLY A CA +18 C C . GLY A 7 ? 2.0896 1.3930 1.3430 -0.2726 0.1609 -0.0569 4 GLY A C +19 O O . GLY A 7 ? 1.7712 1.0760 1.0256 -0.2714 0.1592 -0.0561 4 GLY A O +20 N N . GLU A 8 ? 1.8122 1.1153 1.0671 -0.2727 0.1627 -0.0579 5 GLU A N +21 C CA . GLU A 8 ? 1.6750 0.9791 0.9325 -0.2714 0.1630 -0.0581 5 GLU A CA +22 C C . GLU A 8 ? 1.7351 1.0410 0.9972 -0.2692 0.1620 -0.0578 5 GLU A C +23 O O . GLU A 8 ? 2.0033 1.3104 1.2668 -0.2681 0.1612 -0.0575 5 GLU A O +24 C CB . GLU A 8 ? 1.9145 1.2179 1.1734 -0.2718 0.1652 -0.0593 5 GLU A CB +25 C CG . GLU A 8 ? 2.5045 1.8089 1.7662 -0.2707 0.1655 -0.0597 5 GLU A CG +26 C CD . GLU A 8 ? 2.7758 2.0796 2.0338 -0.2718 0.1654 -0.0594 5 GLU A CD +27 O OE1 . GLU A 8 ? 2.9294 2.2317 2.1842 -0.2736 0.1665 -0.0599 5 GLU A OE1 +28 O OE2 . GLU A 8 ? 2.4633 1.7682 1.7217 -0.2708 0.1641 -0.0588 5 GLU A OE2 +29 N N . GLU A 9 ? 1.8740 1.1802 1.1386 -0.2686 0.1620 -0.0579 6 GLU A N +30 C CA . GLU A 9 ? 1.7435 1.0513 1.0126 -0.2666 0.1612 -0.0576 6 GLU A CA +31 C C . GLU A 9 ? 1.7617 1.0706 1.0299 -0.2659 0.1589 -0.0564 6 GLU A C +32 O O . GLU A 9 ? 1.9808 1.2911 1.2524 -0.2643 0.1580 -0.0561 6 GLU A O +33 C CB . GLU A 9 ? 2.3399 1.6476 1.6122 -0.2661 0.1621 -0.0581 6 GLU A CB +34 C CG . GLU A 9 ? 2.6636 1.9706 1.9382 -0.2663 0.1643 -0.0594 6 GLU A CG +35 C CD . GLU A 9 ? 2.8100 2.1168 2.0875 -0.2659 0.1651 -0.0599 6 GLU A CD +36 O OE1 . GLU A 9 ? 2.6201 1.9270 1.8972 -0.2659 0.1640 -0.0592 6 GLU A OE1 +37 O OE2 . GLU A 9 ? 2.9756 2.2821 2.2558 -0.2657 0.1668 -0.0610 6 GLU A OE2 +38 N N . LEU A 10 ? 1.6224 0.9305 0.8859 -0.2673 0.1579 -0.0557 7 LEU A N +39 C CA . LEU A 10 ? 1.6741 0.9832 0.9364 -0.2667 0.1556 -0.0546 7 LEU A CA +40 C C . LEU A 10 ? 1.8951 1.2049 1.1567 -0.2662 0.1548 -0.0543 7 LEU A C +41 O O . LEU A 10 ? 1.5517 0.8627 0.8135 -0.2653 0.1531 -0.0534 7 LEU A O +42 C CB . LEU A 10 ? 1.6252 0.9331 0.8830 -0.2684 0.1547 -0.0541 7 LEU A CB +43 C CG . LEU A 10 ? 1.8961 1.2037 1.1548 -0.2686 0.1547 -0.0542 7 LEU A CG +44 C CD1 . LEU A 10 ? 1.7001 1.0060 0.9545 -0.2707 0.1550 -0.0542 7 LEU A CD1 +45 C CD2 . LEU A 10 ? 1.9007 1.2096 1.1613 -0.2674 0.1528 -0.0533 7 LEU A CD2 +46 N N . PHE A 11 ? 1.9108 1.2200 1.1718 -0.2668 0.1562 -0.0549 8 PHE A N +47 C CA . PHE A 11 ? 1.7688 1.0784 1.0283 -0.2667 0.1556 -0.0545 8 PHE A CA +48 C C . PHE A 11 ? 1.8346 1.1454 1.0982 -0.2652 0.1562 -0.0550 8 PHE A C +49 O O . PHE A 11 ? 1.8669 1.1782 1.1297 -0.2650 0.1557 -0.0547 8 PHE A O +50 C CB . PHE A 11 ? 1.6995 1.0075 0.9542 -0.2687 0.1561 -0.0546 8 PHE A CB +51 C CG . PHE A 11 ? 1.8663 1.1735 1.1166 -0.2700 0.1548 -0.0539 8 PHE A CG +52 C CD1 . PHE A 11 ? 1.6771 0.9848 0.9253 -0.2698 0.1528 -0.0530 8 PHE A CD1 +53 C CD2 . PHE A 11 ? 1.7281 1.0340 0.9768 -0.2712 0.1554 -0.0542 8 PHE A CD2 +54 C CE1 . PHE A 11 ? 1.7560 1.0630 1.0004 -0.2709 0.1515 -0.0524 8 PHE A CE1 +55 C CE2 . PHE A 11 ? 1.8034 1.1087 1.0484 -0.2724 0.1541 -0.0536 8 PHE A CE2 +56 C CZ . PHE A 11 ? 1.6821 0.9879 0.9249 -0.2722 0.1521 -0.0527 8 PHE A CZ +57 N N . THR A 12 ? 1.6863 0.9978 0.9545 -0.2640 0.1571 -0.0556 9 THR A N +58 C CA . THR A 12 ? 1.7362 1.0492 1.0088 -0.2622 0.1572 -0.0559 9 THR A CA +59 C C . THR A 12 ? 1.9076 1.2221 1.1809 -0.2610 0.1551 -0.0549 9 THR A C +60 O O . THR A 12 ? 1.9379 1.2524 1.2100 -0.2611 0.1540 -0.0542 9 THR A O +61 C CB . THR A 12 ? 1.1341 0.4475 0.4113 -0.2613 0.1586 -0.0568 9 THR A CB +62 O OG1 . THR A 12 ? 1.7485 1.0624 1.0273 -0.2606 0.1577 -0.0564 9 THR A OG1 +63 C CG2 . THR A 12 ? 1.3841 0.6959 0.6602 -0.2627 0.1604 -0.0578 9 THR A CG2 +64 N N . GLY A 13 ? 1.5899 0.9057 0.8651 -0.2599 0.1546 -0.0547 10 GLY A N +65 C CA . GLY A 13 ? 2.2600 1.5771 1.5359 -0.2587 0.1527 -0.0538 10 GLY A CA +66 C C . GLY A 13 ? 1.6730 0.9898 0.9444 -0.2596 0.1510 -0.0528 10 GLY A C +67 O O . GLY A 13 ? 1.6406 0.9560 0.9083 -0.2611 0.1510 -0.0526 10 GLY A O +68 N N . VAL A 14 ? 1.4934 0.8114 0.7652 -0.2586 0.1495 -0.0521 11 VAL A N +69 C CA . VAL A 14 ? 1.4976 0.8155 0.7654 -0.2593 0.1477 -0.0511 11 VAL A CA +70 C C . VAL A 14 ? 1.5813 0.8986 0.8468 -0.2600 0.1466 -0.0505 11 VAL A C +71 O O . VAL A 14 ? 1.6497 0.9678 0.9177 -0.2590 0.1461 -0.0504 11 VAL A O +72 C CB . VAL A 14 ? 1.3448 0.6643 0.6144 -0.2578 0.1462 -0.0504 11 VAL A CB +73 C CG1 . VAL A 14 ? 1.7023 1.0218 0.9683 -0.2583 0.1443 -0.0494 11 VAL A CG1 +74 C CG2 . VAL A 14 ? 1.3742 0.6942 0.6454 -0.2573 0.1470 -0.0509 11 VAL A CG2 +75 N N . VAL A 15 ? 1.4129 0.7287 0.6738 -0.2617 0.1464 -0.0503 12 VAL A N +76 C CA . VAL A 15 ? 1.6611 0.9764 0.9197 -0.2625 0.1454 -0.0499 12 VAL A CA +77 C C . VAL A 15 ? 1.7330 1.0486 0.9886 -0.2627 0.1432 -0.0489 12 VAL A C +78 O O . VAL A 15 ? 1.5608 0.8759 0.8137 -0.2633 0.1428 -0.0487 12 VAL A O +79 C CB . VAL A 15 ? 1.4302 0.7436 0.6854 -0.2644 0.1465 -0.0503 12 VAL A CB +80 C CG1 . VAL A 15 ? 1.5534 0.8663 0.8067 -0.2652 0.1454 -0.0499 12 VAL A CG1 +81 C CG2 . VAL A 15 ? 1.2468 0.5598 0.5046 -0.2644 0.1487 -0.0514 12 VAL A CG2 +82 N N . PRO A 16 ? 1.4876 0.8038 0.7437 -0.2622 0.1417 -0.0483 13 PRO A N +83 C CA . PRO A 16 ? 1.7166 1.0330 0.9698 -0.2625 0.1395 -0.0474 13 PRO A CA +84 C C . PRO A 16 ? 1.5774 0.8930 0.8275 -0.2641 0.1387 -0.0473 13 PRO A C +85 O O . PRO A 16 ? 1.6377 0.9521 0.8864 -0.2652 0.1395 -0.0477 13 PRO A O +86 C CB . PRO A 16 ? 1.2353 0.5529 0.4909 -0.2613 0.1382 -0.0470 13 PRO A CB +87 C CG . PRO A 16 ? 1.6257 0.9431 0.8841 -0.2611 0.1396 -0.0476 13 PRO A CG +88 C CD . PRO A 16 ? 1.5701 0.8871 0.8298 -0.2611 0.1417 -0.0484 13 PRO A CD +89 N N . ILE A 17 ? 1.6796 0.9962 0.9295 -0.2642 0.1370 -0.0467 14 ILE A N +90 C CA . ILE A 17 ? 1.5801 0.8965 0.8281 -0.2655 0.1359 -0.0465 14 ILE A CA +91 C C . ILE A 17 ? 1.5748 0.8926 0.8231 -0.2652 0.1331 -0.0456 14 ILE A C +92 O O . ILE A 17 ? 1.4806 0.7997 0.7304 -0.2640 0.1318 -0.0450 14 ILE A O +93 C CB . ILE A 17 ? 1.3504 0.6667 0.5978 -0.2661 0.1363 -0.0467 14 ILE A CB +94 C CG1 . ILE A 17 ? 1.5422 0.8574 0.7898 -0.2663 0.1391 -0.0476 14 ILE A CG1 +95 C CG2 . ILE A 17 ? 1.3668 0.6825 0.6120 -0.2677 0.1356 -0.0466 14 ILE A CG2 +96 C CD1 . ILE A 17 ? 1.8815 1.1966 1.1286 -0.2668 0.1395 -0.0478 14 ILE A CD1 +97 N N . LEU A 18 ? 1.4468 0.7640 0.6933 -0.2664 0.1322 -0.0454 15 LEU A N +98 C CA . LEU A 18 ? 1.7303 1.0484 0.9766 -0.2664 0.1296 -0.0445 15 LEU A CA +99 C C . LEU A 18 ? 1.6945 1.0121 0.9386 -0.2680 0.1289 -0.0445 15 LEU A C +100 O O . LEU A 18 ? 1.4310 0.7473 0.6736 -0.2693 0.1302 -0.0451 15 LEU A O +101 C CB . LEU A 18 ? 1.3712 0.6893 0.6178 -0.2661 0.1293 -0.0444 15 LEU A CB +102 C CG . LEU A 18 ? 1.8276 1.1465 1.0740 -0.2661 0.1268 -0.0436 15 LEU A CG +103 C CD1 . LEU A 18 ? 1.9639 1.2845 1.2119 -0.2647 0.1249 -0.0429 15 LEU A CD1 +104 C CD2 . LEU A 18 ? 1.9349 1.2532 1.1814 -0.2659 0.1270 -0.0437 15 LEU A CD2 +105 N N . VAL A 19 ? 1.5670 0.8856 0.8109 -0.2680 0.1269 -0.0438 16 VAL A N +106 C CA . VAL A 19 ? 1.5245 0.8426 0.7664 -0.2696 0.1261 -0.0437 16 VAL A CA +107 C C . VAL A 19 ? 1.5721 0.8910 0.8135 -0.2698 0.1234 -0.0429 16 VAL A C +108 O O . VAL A 19 ? 1.5417 0.8619 0.7843 -0.2687 0.1217 -0.0422 16 VAL A O +109 C CB . VAL A 19 ? 1.4376 0.7559 0.6794 -0.2697 0.1265 -0.0439 16 VAL A CB +110 C CG1 . VAL A 19 ? 1.4357 0.7534 0.6752 -0.2713 0.1258 -0.0438 16 VAL A CG1 +111 C CG2 . VAL A 19 ? 1.5850 0.9024 0.8272 -0.2696 0.1292 -0.0447 16 VAL A CG2 +112 N N . GLU A 20 ? 1.4697 0.7877 0.7091 -0.2713 0.1231 -0.0430 17 GLU A N +113 C CA . GLU A 20 ? 1.4050 0.7234 0.6435 -0.2719 0.1206 -0.0422 17 GLU A CA +114 C C . GLU A 20 ? 1.7047 1.0226 0.9410 -0.2735 0.1201 -0.0423 17 GLU A C +115 O O . GLU A 20 ? 1.4345 0.7511 0.6692 -0.2749 0.1215 -0.0429 17 GLU A O +116 C CB . GLU A 20 ? 1.7489 1.0669 0.9869 -0.2723 0.1203 -0.0422 17 GLU A CB +117 C CG . GLU A 20 ? 1.9149 1.2335 1.1548 -0.2708 0.1203 -0.0420 17 GLU A CG +118 C CD . GLU A 20 ? 2.1681 1.4883 1.4097 -0.2693 0.1183 -0.0413 17 GLU A CD +119 O OE1 . GLU A 20 ? 2.1960 1.5169 1.4372 -0.2696 0.1166 -0.0407 17 GLU A OE1 +120 O OE2 . GLU A 20 ? 2.1378 1.4587 1.3812 -0.2679 0.1186 -0.0412 17 GLU A OE2 +121 N N . LEU A 21 ? 1.5961 0.9149 0.8324 -0.2734 0.1180 -0.0416 18 LEU A N +122 C CA . LEU A 21 ? 1.6252 0.9436 0.8595 -0.2750 0.1172 -0.0415 18 LEU A CA +123 C C . LEU A 21 ? 1.5987 0.9176 0.8322 -0.2754 0.1145 -0.0407 18 LEU A C +124 O O . LEU A 21 ? 1.6294 0.9496 0.8643 -0.2742 0.1128 -0.0400 18 LEU A O +125 C CB . LEU A 21 ? 1.7050 1.0237 0.9395 -0.2747 0.1174 -0.0415 18 LEU A CB +126 C CG . LEU A 21 ? 1.5275 0.8458 0.7599 -0.2761 0.1165 -0.0413 18 LEU A CG +127 C CD1 . LEU A 21 ? 2.1112 1.4280 1.3416 -0.2779 0.1180 -0.0420 18 LEU A CD1 +128 C CD2 . LEU A 21 ? 1.8305 1.1493 1.0635 -0.2756 0.1166 -0.0413 18 LEU A CD2 +129 N N . ASP A 22 ? 1.6083 0.9262 0.8396 -0.2772 0.1142 -0.0408 19 ASP A N +130 C CA . ASP A 22 ? 1.8526 1.1708 1.0828 -0.2780 0.1117 -0.0401 19 ASP A CA +131 C C . ASP A 22 ? 1.7639 1.0816 0.9922 -0.2794 0.1113 -0.0401 19 ASP A C +132 O O . ASP A 22 ? 1.8030 1.1194 1.0295 -0.2810 0.1125 -0.0407 19 ASP A O +133 C CB . ASP A 22 ? 1.6983 1.0157 0.9274 -0.2790 0.1112 -0.0400 19 ASP A CB +134 C CG . ASP A 22 ? 2.0854 1.4037 1.3163 -0.2777 0.1105 -0.0396 19 ASP A CG +135 O OD1 . ASP A 22 ? 2.2406 1.5602 1.4733 -0.2761 0.1094 -0.0391 19 ASP A OD1 +136 O OD2 . ASP A 22 ? 2.4493 1.7668 1.6797 -0.2781 0.1111 -0.0399 19 ASP A OD2 +137 N N . GLY A 23 ? 1.8209 1.1395 1.0496 -0.2789 0.1097 -0.0395 20 GLY A N +138 C CA . GLY A 23 ? 1.3082 0.6264 0.5353 -0.2801 0.1093 -0.0395 20 GLY A CA +139 C C . GLY A 23 ? 1.8168 1.1351 1.0425 -0.2811 0.1068 -0.0388 20 GLY A C +140 O O . GLY A 23 ? 1.7792 1.0984 1.0057 -0.2804 0.1050 -0.0381 20 GLY A O +141 N N . ASP A 24 ? 1.9749 1.2924 1.1985 -0.2827 0.1068 -0.0390 21 ASP A N +142 C CA . ASP A 24 ? 1.6015 0.9189 0.8235 -0.2839 0.1046 -0.0384 21 ASP A CA +143 C C . ASP A 24 ? 1.7179 1.0347 0.9383 -0.2849 0.1047 -0.0386 21 ASP A C +144 O O . ASP A 24 ? 1.8327 1.1483 1.0513 -0.2865 0.1060 -0.0392 21 ASP A O +145 C CB . ASP A 24 ? 2.3906 1.7069 1.6109 -0.2855 0.1045 -0.0386 21 ASP A CB +146 C CG . ASP A 24 ? 2.4730 1.7893 1.6919 -0.2866 0.1020 -0.0379 21 ASP A CG +147 O OD1 . ASP A 24 ? 2.2522 1.5691 1.4709 -0.2865 0.1005 -0.0374 21 ASP A OD1 +148 O OD2 . ASP A 24 ? 1.8812 1.1969 1.0992 -0.2877 0.1015 -0.0378 21 ASP A OD2 +149 N N . VAL A 25 ? 1.6775 0.9953 0.8987 -0.2840 0.1035 -0.0380 22 VAL A N +150 C CA . VAL A 25 ? 1.6893 1.0066 0.9092 -0.2848 0.1036 -0.0381 22 VAL A CA +151 C C . VAL A 25 ? 1.7111 1.0287 0.9299 -0.2854 0.1009 -0.0373 22 VAL A C +152 O O . VAL A 25 ? 1.5439 0.8627 0.7641 -0.2841 0.0994 -0.0366 22 VAL A O +153 C CB . VAL A 25 ? 1.5740 0.8919 0.7954 -0.2834 0.1049 -0.0383 22 VAL A CB +154 C CG1 . VAL A 25 ? 1.6378 0.9554 0.8580 -0.2839 0.1043 -0.0381 22 VAL A CG1 +155 C CG2 . VAL A 25 ? 1.7092 1.0263 0.9309 -0.2834 0.1077 -0.0392 22 VAL A CG2 +156 N N . ASN A 26 ? 1.7533 1.0698 0.9696 -0.2874 0.1005 -0.0374 23 ASN A N +157 C CA . ASN A 26 ? 1.4909 0.8074 0.7059 -0.2883 0.0981 -0.0368 23 ASN A CA +158 C C . ASN A 26 ? 1.9120 1.2294 1.1281 -0.2875 0.0961 -0.0360 23 ASN A C +159 O O . ASN A 26 ? 1.5537 0.8720 0.7705 -0.2867 0.0941 -0.0353 23 ASN A O +160 C CB . ASN A 26 ? 1.5368 0.8536 0.7517 -0.2879 0.0974 -0.0364 23 ASN A CB +161 C CG . ASN A 26 ? 2.0273 1.3430 1.2403 -0.2894 0.0988 -0.0370 23 ASN A CG +162 O OD1 . ASN A 26 ? 1.7341 1.0488 0.9459 -0.2906 0.1005 -0.0378 23 ASN A OD1 +163 N ND2 . ASN A 26 ? 1.6545 0.9703 0.8671 -0.2893 0.0981 -0.0367 23 ASN A ND2 +164 N N . GLY A 27 ? 1.7753 1.0924 0.9915 -0.2878 0.0966 -0.0362 24 GLY A N +165 C CA . GLY A 27 ? 1.6174 0.9353 0.8347 -0.2871 0.0950 -0.0356 24 GLY A CA +166 C C . GLY A 27 ? 1.7292 1.0485 0.9492 -0.2848 0.0946 -0.0352 24 GLY A C +167 O O . GLY A 27 ? 1.6595 0.9795 0.8804 -0.2842 0.0932 -0.0347 24 GLY A O +168 N N . HIS A 28 ? 1.7315 1.0513 0.9528 -0.2836 0.0959 -0.0355 25 HIS A N +169 C CA . HIS A 28 ? 1.8453 1.1663 1.0692 -0.2814 0.0961 -0.0353 25 HIS A CA +170 C C . HIS A 28 ? 1.8953 1.2161 1.1202 -0.2809 0.0981 -0.0359 25 HIS A C +171 O O . HIS A 28 ? 1.5034 0.8235 0.7280 -0.2813 0.1003 -0.0367 25 HIS A O +172 C CB . HIS A 28 ? 1.4496 0.7712 0.6746 -0.2803 0.0967 -0.0354 25 HIS A CB +173 C CG . HIS A 28 ? 2.1696 1.4916 1.3941 -0.2803 0.0947 -0.0347 25 HIS A CG +174 N ND1 . HIS A 28 ? 1.9176 1.2388 1.1400 -0.2818 0.0943 -0.0347 25 HIS A ND1 +175 C CD2 . HIS A 28 ? 1.9522 1.2754 1.1781 -0.2789 0.0930 -0.0339 25 HIS A CD2 +176 C CE1 . HIS A 28 ? 1.5587 0.8805 0.7812 -0.2814 0.0924 -0.0340 25 HIS A CE1 +177 N NE2 . HIS A 28 ? 2.0786 1.4017 1.3033 -0.2797 0.0916 -0.0335 25 HIS A NE2 +178 N N . LYS A 29 ? 1.6650 0.9863 0.8910 -0.2802 0.0974 -0.0356 26 LYS A N +179 C CA . LYS A 29 ? 1.6439 0.9651 0.8710 -0.2796 0.0992 -0.0362 26 LYS A CA +180 C C . LYS A 29 ? 1.8448 1.1671 1.0744 -0.2775 0.0998 -0.0361 26 LYS A C +181 O O . LYS A 29 ? 1.6819 1.0053 0.9125 -0.2765 0.0984 -0.0356 26 LYS A O +182 C CB . LYS A 29 ? 1.6726 0.9937 0.8995 -0.2800 0.0981 -0.0359 26 LYS A CB +183 C CG . LYS A 29 ? 1.5206 0.8406 0.7449 -0.2821 0.0974 -0.0359 26 LYS A CG +184 C CD . LYS A 29 ? 1.9487 1.2687 1.1730 -0.2825 0.0961 -0.0355 26 LYS A CD +185 C CE . LYS A 29 ? 1.8245 1.1431 1.0462 -0.2847 0.0958 -0.0356 26 LYS A CE +186 N NZ . LYS A 29 ? 2.1261 1.4435 1.3468 -0.2857 0.0983 -0.0365 26 LYS A NZ +187 N N . PHE A 30 ? 1.5815 0.9037 0.8122 -0.2769 0.1018 -0.0367 27 PHE A N +188 C CA . PHE A 30 ? 1.6142 0.9374 0.8472 -0.2749 0.1026 -0.0368 27 PHE A CA +189 C C . PHE A 30 ? 1.6898 1.0124 0.9235 -0.2746 0.1049 -0.0375 27 PHE A C +190 O O . PHE A 30 ? 1.5036 0.8250 0.7359 -0.2759 0.1062 -0.0380 27 PHE A O +191 C CB . PHE A 30 ? 1.8651 1.1886 1.0986 -0.2744 0.1031 -0.0368 27 PHE A CB +192 C CG . PHE A 30 ? 1.6999 1.0222 0.9321 -0.2754 0.1052 -0.0376 27 PHE A CG +193 C CD1 . PHE A 30 ? 1.8045 1.1259 1.0343 -0.2772 0.1049 -0.0377 27 PHE A CD1 +194 C CD2 . PHE A 30 ? 1.5557 0.8779 0.7890 -0.2747 0.1075 -0.0382 27 PHE A CD2 +195 C CE1 . PHE A 30 ? 1.7670 1.0873 0.9956 -0.2782 0.1068 -0.0384 27 PHE A CE1 +196 C CE2 . PHE A 30 ? 1.6589 0.9800 0.8910 -0.2757 0.1094 -0.0389 27 PHE A CE2 +197 C CZ . PHE A 30 ? 1.5642 0.8843 0.7939 -0.2775 0.1091 -0.0390 27 PHE A CZ +198 N N . SER A 31 ? 1.6032 0.9268 0.8392 -0.2728 0.1053 -0.0374 28 SER A N +199 C CA . SER A 31 ? 1.5250 0.8481 0.7619 -0.2724 0.1075 -0.0381 28 SER A CA +200 C C . SER A 31 ? 1.6961 1.0199 0.9349 -0.2708 0.1087 -0.0383 28 SER A C +201 O O . SER A 31 ? 1.4869 0.8120 0.7273 -0.2695 0.1075 -0.0377 28 SER A O +202 C CB . SER A 31 ? 1.5941 0.9174 0.8315 -0.2721 0.1068 -0.0378 28 SER A CB +203 O OG . SER A 31 ? 2.1283 1.4507 1.3637 -0.2737 0.1061 -0.0378 28 SER A OG +204 N N . VAL A 32 ? 1.6420 0.9649 0.8808 -0.2709 0.1111 -0.0391 29 VAL A N +205 C CA . VAL A 32 ? 1.6870 1.0105 0.9277 -0.2695 0.1126 -0.0394 29 VAL A CA +206 C C . VAL A 32 ? 1.4688 0.7917 0.7103 -0.2691 0.1145 -0.0400 29 VAL A C +207 O O . VAL A 32 ? 1.4233 0.7450 0.6635 -0.2702 0.1158 -0.0405 29 VAL A O +208 C CB . VAL A 32 ? 1.5301 0.8530 0.7702 -0.2700 0.1139 -0.0398 29 VAL A CB +209 C CG1 . VAL A 32 ? 1.5790 0.9026 0.8211 -0.2684 0.1149 -0.0399 29 VAL A CG1 +210 C CG2 . VAL A 32 ? 1.2657 0.5888 0.5045 -0.2708 0.1122 -0.0393 29 VAL A CG2 +211 N N . SER A 33 ? 1.4372 0.7611 0.6809 -0.2674 0.1146 -0.0398 30 SER A N +212 C CA . SER A 33 ? 1.7538 1.0773 0.9985 -0.2668 0.1165 -0.0404 30 SER A CA +213 C C . SER A 33 ? 1.7035 1.0272 0.9497 -0.2657 0.1181 -0.0408 30 SER A C +214 O O . SER A 33 ? 1.5014 0.8263 0.7489 -0.2647 0.1172 -0.0403 30 SER A O +215 C CB . SER A 33 ? 1.4830 0.8073 0.7290 -0.2657 0.1153 -0.0399 30 SER A CB +216 O OG . SER A 33 ? 2.0502 1.3737 1.2950 -0.2667 0.1150 -0.0399 30 SER A OG +217 N N . GLY A 34 ? 1.6308 0.9535 0.8767 -0.2661 0.1205 -0.0416 31 GLY A N +218 C CA . GLY A 34 ? 1.4111 0.7338 0.6583 -0.2653 0.1222 -0.0420 31 GLY A CA +219 C C . GLY A 34 ? 1.6613 0.9835 0.9095 -0.2646 0.1241 -0.0425 31 GLY A C +220 O O . GLY A 34 ? 1.4837 0.8049 0.7311 -0.2653 0.1250 -0.0429 31 GLY A O +221 N N . GLU A 35 ? 1.3382 0.6612 0.5884 -0.2632 0.1247 -0.0426 32 GLU A N +222 C CA . GLU A 35 ? 1.6765 0.9989 0.9277 -0.2626 0.1266 -0.0432 32 GLU A CA +223 C C . GLU A 35 ? 1.5829 0.9053 0.8352 -0.2619 0.1283 -0.0436 32 GLU A C +224 O O . GLU A 35 ? 1.5404 0.8636 0.7934 -0.2614 0.1276 -0.0433 32 GLU A O +225 C CB . GLU A 35 ? 1.4676 0.7909 0.7203 -0.2613 0.1256 -0.0428 32 GLU A CB +226 C CG . GLU A 35 ? 1.5797 0.9045 0.8343 -0.2599 0.1246 -0.0423 32 GLU A CG +227 C CD . GLU A 35 ? 2.5612 1.8870 1.8171 -0.2588 0.1232 -0.0417 32 GLU A CD +228 O OE1 . GLU A 35 ? 2.5848 1.9102 1.8413 -0.2585 0.1242 -0.0420 32 GLU A OE1 +229 O OE2 . GLU A 35 ? 3.1114 2.4384 2.3676 -0.2585 0.1210 -0.0410 32 GLU A OE2 +230 N N . GLY A 36 ? 1.7846 1.1059 1.0370 -0.2620 0.1306 -0.0444 33 GLY A N +231 C CA . GLY A 36 ? 1.5660 0.8872 0.8196 -0.2613 0.1323 -0.0449 33 GLY A CA +232 C C . GLY A 36 ? 1.5251 0.8449 0.7784 -0.2617 0.1349 -0.0458 33 GLY A C +233 O O . GLY A 36 ? 1.5764 0.8955 0.8292 -0.2620 0.1353 -0.0460 33 GLY A O +234 N N . GLU A 37 ? 1.6102 0.9294 0.8637 -0.2618 0.1367 -0.0464 34 GLU A N +235 C CA . GLU A 37 ? 1.5982 0.9160 0.8515 -0.2621 0.1393 -0.0473 34 GLU A CA +236 C C . GLU A 37 ? 1.4527 0.7695 0.7051 -0.2630 0.1410 -0.0479 34 GLU A C +237 O O . GLU A 37 ? 1.5420 0.8593 0.7945 -0.2629 0.1404 -0.0477 34 GLU A O +238 C CB . GLU A 37 ? 1.5504 0.8686 0.8058 -0.2607 0.1401 -0.0474 34 GLU A CB +239 C CG . GLU A 37 ? 2.1982 1.5174 1.4550 -0.2597 0.1399 -0.0473 34 GLU A CG +240 C CD . GLU A 37 ? 2.1921 1.5128 1.4533 -0.2579 0.1400 -0.0474 34 GLU A CD +241 O OE1 . GLU A 37 ? 2.4080 1.7291 1.6719 -0.2573 0.1407 -0.0478 34 GLU A OE1 +242 O OE2 . GLU A 37 ? 2.2142 1.5359 1.4765 -0.2570 0.1393 -0.0471 34 GLU A OE2 +243 N N . GLY A 38 ? 1.4876 0.8029 0.7391 -0.2638 0.1431 -0.0487 35 GLY A N +244 C CA . GLY A 38 ? 1.5942 0.9083 0.8448 -0.2648 0.1450 -0.0494 35 GLY A CA +245 C C . GLY A 38 ? 1.5368 0.8505 0.7898 -0.2643 0.1472 -0.0503 35 GLY A C +246 O O . GLY A 38 ? 1.5363 0.8503 0.7915 -0.2638 0.1476 -0.0506 35 GLY A O +247 N N . ASP A 39 ? 1.6612 0.9750 0.9155 -0.2641 0.1484 -0.0508 36 ASP A N +248 C CA . ASP A 39 ? 1.6444 0.9585 0.9029 -0.2634 0.1502 -0.0518 36 ASP A CA +249 C C . ASP A 39 ? 1.3176 0.6302 0.5744 -0.2648 0.1520 -0.0526 36 ASP A C +250 O O . ASP A 39 ? 1.3507 0.6632 0.6074 -0.2650 0.1525 -0.0529 36 ASP A O +251 C CB . ASP A 39 ? 1.4693 0.7851 0.7316 -0.2617 0.1499 -0.0519 36 ASP A CB +252 C CG . ASP A 39 ? 2.0573 1.3742 1.3249 -0.2602 0.1509 -0.0526 36 ASP A CG +253 O OD1 . ASP A 39 ? 1.9978 1.3139 1.2662 -0.2607 0.1522 -0.0533 36 ASP A OD1 +254 O OD2 . ASP A 39 ? 1.8363 1.1548 1.1074 -0.2587 0.1503 -0.0525 36 ASP A OD2 +255 N N . ALA A 40 ? 1.6271 0.9385 0.8828 -0.2659 0.1530 -0.0531 37 ALA A N +256 C CA . ALA A 40 ? 1.5550 0.8649 0.8088 -0.2674 0.1547 -0.0538 37 ALA A CA +257 C C . ALA A 40 ? 1.5110 0.8213 0.7683 -0.2667 0.1563 -0.0548 37 ALA A C +258 O O . ALA A 40 ? 1.5267 0.8361 0.7823 -0.2677 0.1571 -0.0551 37 ALA A O +259 C CB . ALA A 40 ? 1.3130 0.6218 0.5661 -0.2683 0.1557 -0.0543 37 ALA A CB +260 N N . THR A 41 ? 1.8916 1.2033 1.1540 -0.2651 0.1566 -0.0552 38 THR A N +261 C CA . THR A 41 ? 1.4103 0.7226 0.6768 -0.2641 0.1579 -0.0562 38 THR A CA +262 C C . THR A 41 ? 1.5980 0.9106 0.8640 -0.2641 0.1577 -0.0562 38 THR A C +263 O O . THR A 41 ? 1.6393 0.9516 0.9069 -0.2643 0.1591 -0.0571 38 THR A O +264 C CB . THR A 41 ? 1.5360 0.8501 0.8077 -0.2621 0.1576 -0.0564 38 THR A CB +265 O OG1 . THR A 41 ? 1.6686 0.9826 0.9405 -0.2620 0.1573 -0.0562 38 THR A OG1 +266 C CG2 . THR A 41 ? 1.1749 0.4895 0.4511 -0.2612 0.1591 -0.0576 38 THR A CG2 +267 N N . TYR A 42 ? 1.3617 0.6747 0.6256 -0.2640 0.1560 -0.0551 39 TYR A N +268 C CA . TYR A 42 ? 1.6535 0.9667 0.9169 -0.2640 0.1557 -0.0550 39 TYR A CA +269 C C . TYR A 42 ? 1.4062 0.7181 0.6638 -0.2656 0.1548 -0.0541 39 TYR A C +270 O O . TYR A 42 ? 1.5237 0.8358 0.7802 -0.2656 0.1540 -0.0537 39 TYR A O +271 C CB . TYR A 42 ? 1.2034 0.5185 0.4703 -0.2621 0.1546 -0.0547 39 TYR A CB +272 C CG . TYR A 42 ? 1.4963 0.8127 0.7685 -0.2605 0.1552 -0.0554 39 TYR A CG +273 C CD1 . TYR A 42 ? 1.6370 0.9539 0.9132 -0.2599 0.1566 -0.0566 39 TYR A CD1 +274 C CD2 . TYR A 42 ? 1.6349 0.9520 0.9082 -0.2598 0.1544 -0.0550 39 TYR A CD2 +275 C CE1 . TYR A 42 ? 1.6419 0.9599 0.9229 -0.2585 0.1572 -0.0573 39 TYR A CE1 +276 C CE2 . TYR A 42 ? 1.9136 1.2317 1.1917 -0.2584 0.1550 -0.0556 39 TYR A CE2 +277 C CZ . TYR A 42 ? 1.8146 1.1332 1.0965 -0.2577 0.1564 -0.0568 39 TYR A CZ +278 O OH . TYR A 42 ? 1.5423 0.8620 0.8289 -0.2564 0.1570 -0.0574 39 TYR A OH +279 N N . GLY A 43 ? 1.5114 0.8219 0.7655 -0.2671 0.1550 -0.0539 40 GLY A N +280 C CA . GLY A 43 ? 1.5043 0.8134 0.7527 -0.2688 0.1543 -0.0532 40 GLY A CA +281 C C . GLY A 43 ? 1.6744 0.9845 0.9219 -0.2682 0.1519 -0.0521 40 GLY A C +282 O O . GLY A 43 ? 1.4675 0.7780 0.7145 -0.2685 0.1509 -0.0517 40 GLY A O +283 N N . LYS A 44 ? 1.3883 0.6995 0.6372 -0.2670 0.1508 -0.0516 41 LYS A N +284 C CA . LYS A 44 ? 1.2451 0.5580 0.4951 -0.2659 0.1484 -0.0507 41 LYS A CA +285 C C . LYS A 44 ? 1.7132 1.0269 0.9629 -0.2658 0.1463 -0.0499 41 LYS A C +286 O O . LYS A 44 ? 1.4980 0.8113 0.7477 -0.2658 0.1467 -0.0501 41 LYS A O +287 C CB . LYS A 44 ? 1.3394 0.6533 0.5927 -0.2642 0.1487 -0.0508 41 LYS A CB +288 C CG . LYS A 44 ? 1.5697 0.8847 0.8231 -0.2633 0.1470 -0.0500 41 LYS A CG +289 C CD . LYS A 44 ? 1.3145 0.6315 0.5731 -0.2613 0.1469 -0.0502 41 LYS A CD +290 C CE . LYS A 44 ? 1.8446 1.1628 1.1032 -0.2603 0.1449 -0.0492 41 LYS A CE +291 N NZ . LYS A 44 ? 1.8481 1.1682 1.1116 -0.2584 0.1447 -0.0494 41 LYS A NZ +292 N N . LEU A 45 ? 1.7616 1.0764 1.0110 -0.2658 0.1441 -0.0491 42 LEU A N +293 C CA . LEU A 45 ? 1.5369 0.8526 0.7860 -0.2657 0.1418 -0.0484 42 LEU A CA +294 C C . LEU A 45 ? 1.1993 0.5167 0.4499 -0.2644 0.1397 -0.0475 42 LEU A C +295 O O . LEU A 45 ? 1.6861 1.0039 0.9369 -0.2642 0.1393 -0.0473 42 LEU A O +296 C CB . LEU A 45 ? 1.3700 0.6851 0.6169 -0.2672 0.1411 -0.0482 42 LEU A CB +297 C CG . LEU A 45 ? 1.6320 0.9469 0.8778 -0.2679 0.1403 -0.0480 42 LEU A CG +298 C CD1 . LEU A 45 ? 2.0031 1.3168 1.2488 -0.2682 0.1424 -0.0488 42 LEU A CD1 +299 C CD2 . LEU A 45 ? 1.7423 1.0567 0.9859 -0.2694 0.1395 -0.0479 42 LEU A CD2 +300 N N . THR A 46 ? 1.4838 0.8022 0.7355 -0.2635 0.1384 -0.0470 43 THR A N +301 C CA . THR A 46 ? 1.7731 1.0931 1.0259 -0.2624 0.1361 -0.0461 43 THR A CA +302 C C . THR A 46 ? 1.5757 0.8962 0.8279 -0.2626 0.1341 -0.0455 43 THR A C +303 O O . THR A 46 ? 1.5479 0.8680 0.8001 -0.2626 0.1346 -0.0457 43 THR A O +304 C CB . THR A 46 ? 1.4794 0.8002 0.7345 -0.2608 0.1363 -0.0461 43 THR A CB +305 O OG1 . THR A 46 ? 2.1661 1.4874 1.4219 -0.2602 0.1358 -0.0459 43 THR A OG1 +306 C CG2 . THR A 46 ? 1.5616 0.8815 0.8173 -0.2607 0.1388 -0.0469 43 THR A CG2 +307 N N . LEU A 47 ? 1.5050 0.8263 0.7566 -0.2628 0.1320 -0.0448 44 LEU A N +308 C CA . LEU A 47 ? 1.5425 0.8642 0.7933 -0.2632 0.1301 -0.0442 44 LEU A CA +309 C C . LEU A 47 ? 1.3889 0.7120 0.6403 -0.2625 0.1276 -0.0433 44 LEU A C +310 O O . LEU A 47 ? 1.3212 0.6447 0.5726 -0.2625 0.1271 -0.0431 44 LEU A O +311 C CB . LEU A 47 ? 1.3762 0.6967 0.6247 -0.2649 0.1304 -0.0445 44 LEU A CB +312 C CG . LEU A 47 ? 1.6028 0.9219 0.8505 -0.2657 0.1324 -0.0453 44 LEU A CG +313 C CD1 . LEU A 47 ? 1.6325 0.9505 0.8779 -0.2675 0.1328 -0.0456 44 LEU A CD1 +314 C CD2 . LEU A 47 ? 1.4688 0.7881 0.7170 -0.2653 0.1319 -0.0451 44 LEU A CD2 +315 N N . LYS A 48 ? 1.4174 0.7413 0.6693 -0.2620 0.1260 -0.0428 45 LYS A N +316 C CA . LYS A 48 ? 1.2273 0.5526 0.4797 -0.2615 0.1234 -0.0419 45 LYS A CA +317 C C . LYS A 48 ? 1.6268 0.9520 0.8777 -0.2624 0.1217 -0.0415 45 LYS A C +318 O O . LYS A 48 ? 1.4416 0.7664 0.6922 -0.2627 0.1219 -0.0416 45 LYS A O +319 C CB . LYS A 48 ? 1.2199 0.5464 0.4744 -0.2598 0.1226 -0.0415 45 LYS A CB +320 C CG . LYS A 48 ? 1.1401 0.4680 0.3952 -0.2592 0.1203 -0.0407 45 LYS A CG +321 C CD . LYS A 48 ? 1.3229 0.6521 0.5798 -0.2578 0.1192 -0.0402 45 LYS A CD +322 C CE . LYS A 48 ? 1.5890 0.9195 0.8470 -0.2570 0.1175 -0.0396 45 LYS A CE +323 N NZ . LYS A 48 ? 1.4949 0.8266 0.7547 -0.2556 0.1165 -0.0391 45 LYS A NZ +324 N N . PHE A 49 ? 1.5844 0.9100 0.8343 -0.2630 0.1201 -0.0410 46 PHE A N +325 C CA . PHE A 49 ? 1.4759 0.8013 0.7243 -0.2639 0.1184 -0.0405 46 PHE A CA +326 C C . PHE A 49 ? 1.4297 0.7565 0.6789 -0.2631 0.1158 -0.0396 46 PHE A C +327 O O . PHE A 49 ? 1.5112 0.8388 0.7612 -0.2624 0.1151 -0.0393 46 PHE A O +328 C CB . PHE A 49 ? 1.4898 0.8142 0.7361 -0.2655 0.1187 -0.0407 46 PHE A CB +329 C CG . PHE A 49 ? 1.4900 0.8130 0.7354 -0.2663 0.1212 -0.0416 46 PHE A CG +330 C CD1 . PHE A 49 ? 1.5399 0.8620 0.7844 -0.2671 0.1221 -0.0420 46 PHE A CD1 +331 C CD2 . PHE A 49 ? 1.5256 0.8482 0.7711 -0.2664 0.1228 -0.0421 46 PHE A CD2 +332 C CE1 . PHE A 49 ? 1.4157 0.7365 0.6594 -0.2679 0.1244 -0.0429 46 PHE A CE1 +333 C CE2 . PHE A 49 ? 1.6975 1.0187 0.9421 -0.2672 0.1251 -0.0429 46 PHE A CE2 +334 C CZ . PHE A 49 ? 1.3499 0.6702 0.5937 -0.2680 0.1260 -0.0433 46 PHE A CZ +335 N N . ILE A 50 ? 1.6727 0.9998 0.9218 -0.2632 0.1145 -0.0393 47 ILE A N +336 C CA . ILE A 50 ? 1.2332 0.5615 0.4828 -0.2627 0.1120 -0.0384 47 ILE A CA +337 C C . ILE A 50 ? 1.7555 1.0833 1.0030 -0.2641 0.1106 -0.0381 47 ILE A C +338 O O . ILE A 50 ? 1.4759 0.8027 0.7222 -0.2651 0.1112 -0.0384 47 ILE A O +339 C CB . ILE A 50 ? 1.4163 0.7452 0.6673 -0.2616 0.1116 -0.0382 47 ILE A CB +340 C CG1 . ILE A 50 ? 1.8122 1.1417 1.0653 -0.2602 0.1129 -0.0385 47 ILE A CG1 +341 C CG2 . ILE A 50 ? 1.8577 1.1878 1.1090 -0.2612 0.1089 -0.0373 47 ILE A CG2 +342 C CD1 . ILE A 50 ? 1.8365 1.1671 1.0909 -0.2592 0.1122 -0.0381 47 ILE A CD1 +343 N N . CYS A 51 ? 1.8205 1.1488 1.0675 -0.2643 0.1088 -0.0375 48 CYS A N +344 C CA . CYS A 51 ? 1.8811 1.2091 1.1263 -0.2655 0.1071 -0.0371 48 CYS A CA +345 C C . CYS A 51 ? 1.5190 0.8477 0.7649 -0.2650 0.1055 -0.0366 48 CYS A C +346 O O . CYS A 51 ? 1.8213 1.1512 1.0685 -0.2639 0.1039 -0.0360 48 CYS A O +347 C CB . CYS A 51 ? 2.1482 1.4765 1.3926 -0.2660 0.1055 -0.0366 48 CYS A CB +348 S SG . CYS A 51 ? 1.6322 0.9597 0.8739 -0.2679 0.1041 -0.0364 48 CYS A SG +349 N N . THR A 52 ? 1.6468 0.9747 0.8918 -0.2659 0.1058 -0.0368 49 THR A N +350 C CA . THR A 52 ? 1.7303 1.0587 0.9759 -0.2655 0.1045 -0.0364 49 THR A CA +351 C C . THR A 52 ? 1.5544 0.8830 0.7989 -0.2662 0.1021 -0.0357 49 THR A C +352 O O . THR A 52 ? 1.6388 0.9678 0.8835 -0.2660 0.1008 -0.0353 49 THR A O +353 C CB . THR A 52 ? 1.5417 0.8691 0.7869 -0.2659 0.1061 -0.0370 49 THR A CB +354 O OG1 . THR A 52 ? 1.4643 0.7903 0.7073 -0.2676 0.1070 -0.0374 49 THR A OG1 +355 C CG2 . THR A 52 ? 1.4267 0.7541 0.6735 -0.2648 0.1081 -0.0375 49 THR A CG2 +356 N N . THR A 53 ? 1.7848 1.1131 1.0277 -0.2672 0.1014 -0.0356 50 THR A N +357 C CA . THR A 53 ? 1.2863 0.6146 0.5280 -0.2681 0.0991 -0.0349 50 THR A CA +358 C C . THR A 53 ? 1.6807 1.0100 0.9229 -0.2675 0.0975 -0.0343 50 THR A C +359 O O . THR A 53 ? 2.1473 1.4766 1.3882 -0.2683 0.0957 -0.0338 50 THR A O +360 C CB . THR A 53 ? 1.5090 0.8360 0.7482 -0.2701 0.0994 -0.0352 50 THR A CB +361 O OG1 . THR A 53 ? 1.5307 0.8572 0.7691 -0.2705 0.1006 -0.0356 50 THR A OG1 +362 C CG2 . THR A 53 ? 1.4835 0.8095 0.7221 -0.2708 0.1008 -0.0358 50 THR A CG2 +363 N N . GLY A 54 ? 1.4929 0.8230 0.7368 -0.2661 0.0981 -0.0343 51 GLY A N +364 C CA . GLY A 54 ? 1.5640 0.8950 0.8086 -0.2654 0.0967 -0.0338 51 GLY A CA +365 C C . GLY A 54 ? 1.3170 0.6476 0.5611 -0.2655 0.0980 -0.0342 51 GLY A C +366 O O . GLY A 54 ? 2.3384 1.6687 1.5833 -0.2651 0.1000 -0.0348 51 GLY A O +367 N N . LYS A 55 ? 1.8728 1.2033 1.1158 -0.2662 0.0967 -0.0338 52 LYS A N +368 C CA . LYS A 55 ? 1.6151 0.9451 0.8574 -0.2666 0.0978 -0.0341 52 LYS A CA +369 C C . LYS A 55 ? 1.4579 0.7865 0.6981 -0.2683 0.0990 -0.0347 52 LYS A C +370 O O . LYS A 55 ? 1.4984 0.8264 0.7374 -0.2694 0.0985 -0.0347 52 LYS A O +371 C CB . LYS A 55 ? 1.3247 0.6551 0.5665 -0.2667 0.0959 -0.0335 52 LYS A CB +372 C CG . LYS A 55 ? 2.0605 1.3915 1.3038 -0.2654 0.0964 -0.0334 52 LYS A CG +373 C CD . LYS A 55 ? 2.6032 1.9344 1.8457 -0.2656 0.0949 -0.0329 52 LYS A CD +374 C CE . LYS A 55 ? 2.7557 2.0882 2.0001 -0.2640 0.0936 -0.0323 52 LYS A CE +375 N NZ . LYS A 55 ? 2.5168 1.8493 1.7605 -0.2641 0.0922 -0.0318 52 LYS A NZ +376 N N . LEU A 56 ? 1.5874 0.9154 0.8272 -0.2686 0.1006 -0.0352 53 LEU A N +377 C CA . LEU A 56 ? 1.4955 0.8221 0.7334 -0.2701 0.1021 -0.0358 53 LEU A CA +378 C C . LEU A 56 ? 1.3913 0.7173 0.6270 -0.2715 0.1010 -0.0356 53 LEU A C +379 O O . LEU A 56 ? 1.6102 0.9365 0.8460 -0.2712 0.1001 -0.0352 53 LEU A O +380 C CB . LEU A 56 ? 1.5577 0.8838 0.7962 -0.2698 0.1047 -0.0366 53 LEU A CB +381 C CG . LEU A 56 ? 1.6331 0.9579 0.8703 -0.2710 0.1068 -0.0374 53 LEU A CG +382 C CD1 . LEU A 56 ? 1.2708 0.5956 0.5087 -0.2708 0.1073 -0.0376 53 LEU A CD1 +383 C CD2 . LEU A 56 ? 1.1065 0.4308 0.3441 -0.2707 0.1090 -0.0380 53 LEU A CD2 +384 N N . PRO A 57 ? 1.7252 1.0502 0.9589 -0.2732 0.1008 -0.0357 54 PRO A N +385 C CA . PRO A 57 ? 1.5412 0.8654 0.7726 -0.2747 0.0998 -0.0355 54 PRO A CA +386 C C . PRO A 57 ? 1.7278 1.0513 0.9585 -0.2751 0.1013 -0.0360 54 PRO A C +387 O O . PRO A 57 ? 1.6036 0.9272 0.8335 -0.2755 0.1004 -0.0356 54 PRO A O +388 C CB . PRO A 57 ? 1.4539 0.7772 0.6836 -0.2763 0.0999 -0.0358 54 PRO A CB +389 C CG . PRO A 57 ? 1.5376 0.8608 0.7684 -0.2758 0.1017 -0.0364 54 PRO A CG +390 C CD . PRO A 57 ? 1.6000 0.9245 0.8334 -0.2737 0.1015 -0.0361 54 PRO A CD +391 N N . VAL A 58 ? 1.7038 1.0268 0.9348 -0.2751 0.1038 -0.0368 55 VAL A N +392 C CA . VAL A 58 ? 1.6996 1.0217 0.9297 -0.2757 0.1055 -0.0373 55 VAL A CA +393 C C . VAL A 58 ? 1.7830 1.1057 1.0152 -0.2741 0.1067 -0.0374 55 VAL A C +394 O O . VAL A 58 ? 1.5913 0.9150 0.8256 -0.2727 0.1065 -0.0373 55 VAL A O +395 C CB . VAL A 58 ? 1.5772 0.8981 0.8061 -0.2770 0.1075 -0.0381 55 VAL A CB +396 C CG1 . VAL A 58 ? 1.5321 0.8524 0.7590 -0.2786 0.1062 -0.0380 55 VAL A CG1 +397 C CG2 . VAL A 58 ? 1.7345 1.0557 0.9651 -0.2760 0.1087 -0.0385 55 VAL A CG2 +398 N N . PRO A 59 ? 1.5311 0.8532 0.7628 -0.2744 0.1079 -0.0377 56 PRO A N +399 C CA . PRO A 59 ? 1.7438 1.0666 0.9776 -0.2729 0.1090 -0.0379 56 PRO A CA +400 C C . PRO A 59 ? 1.8915 1.2140 1.1263 -0.2724 0.1112 -0.0386 56 PRO A C +401 O O . PRO A 59 ? 1.5744 0.8959 0.8079 -0.2736 0.1124 -0.0391 56 PRO A O +402 C CB . PRO A 59 ? 1.4445 0.7664 0.6771 -0.2736 0.1098 -0.0381 56 PRO A CB +403 C CG . PRO A 59 ? 1.5614 0.8825 0.7914 -0.2753 0.1089 -0.0380 56 PRO A CG +404 C CD . PRO A 59 ? 1.6363 0.9573 0.8657 -0.2760 0.1085 -0.0381 56 PRO A CD +405 N N . TRP A 60 ? 1.7157 1.0389 0.9527 -0.2708 0.1118 -0.0386 57 TRP A N +406 C CA . TRP A 60 ? 1.3381 0.6611 0.5762 -0.2704 0.1139 -0.0393 57 TRP A CA +407 C C . TRP A 60 ? 1.4188 0.7405 0.6558 -0.2714 0.1164 -0.0402 57 TRP A C +408 O O . TRP A 60 ? 1.3983 0.7192 0.6346 -0.2722 0.1177 -0.0407 57 TRP A O +409 C CB . TRP A 60 ? 1.3622 0.6863 0.6030 -0.2685 0.1142 -0.0392 57 TRP A CB +410 C CG . TRP A 60 ? 1.4826 0.8078 0.7246 -0.2676 0.1126 -0.0387 57 TRP A CG +411 C CD1 . TRP A 60 ? 1.3044 0.6309 0.5476 -0.2665 0.1107 -0.0380 57 TRP A CD1 +412 C CD2 . TRP A 60 ? 1.5256 0.8507 0.7678 -0.2676 0.1130 -0.0389 57 TRP A CD2 +413 N NE1 . TRP A 60 ? 1.4956 0.8228 0.7397 -0.2659 0.1098 -0.0377 57 TRP A NE1 +414 C CE2 . TRP A 60 ? 1.5379 0.8643 0.7814 -0.2666 0.1111 -0.0382 57 TRP A CE2 +415 C CE3 . TRP A 60 ? 1.4623 0.7863 0.7036 -0.2685 0.1147 -0.0396 57 TRP A CE3 +416 C CZ2 . TRP A 60 ? 1.4132 0.7397 0.6571 -0.2663 0.1109 -0.0382 57 TRP A CZ2 +417 C CZ3 . TRP A 60 ? 1.4297 0.7539 0.6715 -0.2683 0.1145 -0.0396 57 TRP A CZ3 +418 C CH2 . TRP A 60 ? 1.4801 0.8055 0.7232 -0.2672 0.1126 -0.0389 57 TRP A CH2 +419 N N . PRO A 61 ? 1.4985 0.8198 0.7351 -0.2716 0.1169 -0.0403 58 PRO A N +420 C CA . PRO A 61 ? 1.1356 0.4555 0.3711 -0.2726 0.1192 -0.0410 58 PRO A CA +421 C C . PRO A 61 ? 1.3651 0.6839 0.5984 -0.2744 0.1199 -0.0415 58 PRO A C +422 O O . PRO A 61 ? 1.6086 0.9263 0.8415 -0.2750 0.1221 -0.0423 58 PRO A O +423 C CB . PRO A 61 ? 1.4632 0.7830 0.6981 -0.2728 0.1187 -0.0408 58 PRO A CB +424 C CG . PRO A 61 ? 1.5180 0.8391 0.7548 -0.2712 0.1172 -0.0401 58 PRO A CG +425 C CD . PRO A 61 ? 1.4375 0.7596 0.6749 -0.2707 0.1156 -0.0396 58 PRO A CD +426 N N . THR A 62 ? 1.6481 0.9669 0.8800 -0.2752 0.1180 -0.0410 59 THR A N +427 C CA . THR A 62 ? 1.6805 0.9982 0.9103 -0.2770 0.1185 -0.0414 59 THR A CA +428 C C . THR A 62 ? 1.6289 0.9462 0.8589 -0.2772 0.1198 -0.0419 59 THR A C +429 O O . THR A 62 ? 1.5336 0.8498 0.7618 -0.2787 0.1206 -0.0424 59 THR A O +430 C CB . THR A 62 ? 1.6512 0.9692 0.8796 -0.2778 0.1160 -0.0407 59 THR A CB +431 O OG1 . THR A 62 ? 1.6644 0.9836 0.8943 -0.2766 0.1143 -0.0401 59 THR A OG1 +432 C CG2 . THR A 62 ? 1.6023 0.9203 0.8298 -0.2782 0.1148 -0.0402 59 THR A CG2 +433 N N . LEU A 63 ? 1.5703 0.8884 0.8024 -0.2757 0.1200 -0.0419 60 LEU A N +434 C CA . LEU A 63 ? 1.4504 0.7682 0.6828 -0.2757 0.1209 -0.0423 60 LEU A CA +435 C C . LEU A 63 ? 1.7638 1.0812 0.9975 -0.2750 0.1235 -0.0430 60 LEU A C +436 O O . LEU A 63 ? 1.3980 0.7149 0.6318 -0.2752 0.1246 -0.0435 60 LEU A O +437 C CB . LEU A 63 ? 1.5205 0.8395 0.7542 -0.2747 0.1190 -0.0416 60 LEU A CB +438 C CG . LEU A 63 ? 1.7062 1.0256 0.9386 -0.2754 0.1165 -0.0409 60 LEU A CG +439 C CD1 . LEU A 63 ? 1.6348 0.9554 0.8688 -0.2741 0.1146 -0.0402 60 LEU A CD1 +440 C CD2 . LEU A 63 ? 1.4526 0.7707 0.6828 -0.2772 0.1167 -0.0413 60 LEU A CD2 +441 N N . VAL A 64 ? 1.6964 1.0140 0.9311 -0.2742 0.1243 -0.0431 61 VAL A N +442 C CA . VAL A 64 ? 1.4908 0.8080 0.7269 -0.2735 0.1266 -0.0438 61 VAL A CA +443 C C . VAL A 64 ? 1.3719 0.6877 0.6068 -0.2746 0.1288 -0.0447 61 VAL A C +444 O O . VAL A 64 ? 1.5075 0.8231 0.7435 -0.2741 0.1302 -0.0451 61 VAL A O +445 C CB . VAL A 64 ? 1.4753 0.7925 0.7118 -0.2731 0.1274 -0.0440 61 VAL A CB +446 C CG1 . VAL A 64 ? 1.3363 0.6527 0.5737 -0.2728 0.1301 -0.0448 61 VAL A CG1 +447 C CG2 . VAL A 64 ? 1.3085 0.6271 0.5466 -0.2717 0.1256 -0.0432 61 VAL A CG2 +448 N N . THR A 65 ? 1.4746 0.7894 0.7073 -0.2763 0.1291 -0.0449 62 THR A N +449 C CA . THR A 65 ? 1.6063 0.9196 0.8377 -0.2776 0.1312 -0.0458 62 THR A CA +450 C C . THR A 65 ? 1.3285 0.6417 0.5595 -0.2780 0.1308 -0.0458 62 THR A C +451 O O . THR A 65 ? 1.7547 1.0669 0.9852 -0.2786 0.1327 -0.0465 62 THR A O +452 C CB . THR A 65 ? 1.6376 0.9500 0.8667 -0.2794 0.1315 -0.0460 62 THR A CB +453 O OG1 . THR A 65 ? 2.0031 1.3157 1.2308 -0.2802 0.1294 -0.0455 62 THR A OG1 +454 C CG2 . THR A 65 ? 1.6138 0.9264 0.8431 -0.2791 0.1314 -0.0458 62 THR A CG2 +455 N N . THR A 66 ? 1.6138 0.9279 0.8448 -0.2777 0.1284 -0.0450 63 THR A N +456 C CA . THR A 66 ? 1.7587 1.0725 0.9890 -0.2784 0.1280 -0.0450 63 THR A CA +457 C C . THR A 66 ? 1.7324 1.0468 0.9647 -0.2769 0.1284 -0.0451 63 THR A C +458 O O . THR A 66 ? 1.7362 1.0499 0.9682 -0.2773 0.1295 -0.0455 63 THR A O +459 C CB . THR A 66 ? 1.8257 1.1402 1.0551 -0.2788 0.1252 -0.0442 63 THR A CB +460 O OG1 . THR A 66 ? 1.6485 0.9628 0.8764 -0.2799 0.1245 -0.0441 63 THR A OG1 +461 C CG2 . THR A 66 ? 1.5200 0.8338 0.7480 -0.2800 0.1249 -0.0443 63 THR A CG2 +462 N N . PHE A 67 ? 1.6693 0.9849 0.9036 -0.2753 0.1277 -0.0446 64 PHE A N +463 C CA . PHE A 67 ? 1.6209 0.9372 0.8573 -0.2737 0.1280 -0.0446 64 PHE A CA +464 C C . PHE A 67 ? 1.7138 1.0294 0.9512 -0.2733 0.1307 -0.0454 64 PHE A C +465 O O . PHE A 67 ? 1.7806 1.0957 1.0185 -0.2730 0.1319 -0.0458 64 PHE A O +466 C CB . PHE A 67 ? 1.6627 0.9805 0.9011 -0.2721 0.1266 -0.0439 64 PHE A CB +467 C CG . PHE A 67 ? 1.3545 0.6733 0.5928 -0.2719 0.1238 -0.0430 64 PHE A CG +468 C CD1 . PHE A 67 ? 1.5527 0.8715 0.7902 -0.2725 0.1226 -0.0427 64 PHE A CD1 +469 C CD2 . PHE A 67 ? 1.6517 0.9716 0.8908 -0.2710 0.1224 -0.0424 64 PHE A CD2 +470 C CE1 . PHE A 67 ? 1.5053 0.8251 0.7428 -0.2723 0.1200 -0.0419 64 PHE A CE1 +471 C CE2 . PHE A 67 ? 1.6377 0.9586 0.8769 -0.2708 0.1198 -0.0416 64 PHE A CE2 +472 C CZ . PHE A 67 ? 1.5673 0.8881 0.8056 -0.2715 0.1186 -0.0413 64 PHE A CZ +473 N N1 . CR2 A 68 ? 1.6216 0.9369 0.8592 -0.2732 0.1318 -0.0457 65 CR2 A N1 +474 C CA1 . CR2 A 68 ? 1.4361 0.7502 0.6737 -0.2734 0.1348 -0.0467 65 CR2 A CA1 +475 C C1 . CR2 A 68 ? 1.7477 1.0604 0.9833 -0.2752 0.1363 -0.0474 65 CR2 A C1 +476 N N2 . CR2 A 68 ? 1.6621 0.9743 0.8970 -0.2757 0.1371 -0.0476 65 CR2 A N2 +477 N N3 . CR2 A 68 ? 1.5559 0.8674 0.7899 -0.2765 0.1371 -0.0478 65 CR2 A N3 +478 C C2 . CR2 A 68 ? 1.4969 0.8073 0.7292 -0.2779 0.1383 -0.0483 65 CR2 A C2 +479 O O2 . CR2 A 68 ? 1.5250 0.8342 0.7554 -0.2794 0.1392 -0.0488 65 CR2 A O2 +480 C CA2 . CR2 A 68 ? 1.7220 1.0328 0.9548 -0.2774 0.1383 -0.0482 65 CR2 A CA2 +481 C CA3 . CR2 A 68 ? 1.2740 0.5856 0.5079 -0.2765 0.1364 -0.0476 65 CR2 A CA3 +482 C C3 . CR2 A 68 ? 1.6620 0.9729 0.8968 -0.2760 0.1385 -0.0483 65 CR2 A C3 +483 O O3 . CR2 A 68 ? 1.5450 0.8548 0.7784 -0.2772 0.1394 -0.0488 65 CR2 A O3 +484 C CB2 . CR2 A 68 ? 1.5926 0.9025 0.8241 -0.2785 0.1394 -0.0486 65 CR2 A CB2 +485 C CG2 . CR2 A 68 ? 1.5628 0.8731 0.7950 -0.2780 0.1392 -0.0484 65 CR2 A CG2 +486 C CD1 . CR2 A 68 ? 1.5399 0.8516 0.7740 -0.2763 0.1379 -0.0478 65 CR2 A CD1 +487 C CD2 . CR2 A 68 ? 1.5911 0.9005 0.8216 -0.2792 0.1399 -0.0487 65 CR2 A CD2 +488 C CE1 . CR2 A 68 ? 1.7311 1.0431 0.9656 -0.2758 0.1376 -0.0476 65 CR2 A CE1 +489 C CE2 . CR2 A 68 ? 1.4697 0.7794 0.7007 -0.2788 0.1396 -0.0485 65 CR2 A CE2 +490 C CZ . CR2 A 68 ? 1.7373 1.0483 0.9703 -0.2771 0.1385 -0.0479 65 CR2 A CZ +491 O OH . CR2 A 68 ? 1.7407 1.0519 0.9741 -0.2766 0.1382 -0.0477 65 CR2 A OH +492 N N . VAL A 69 ? 1.9021 1.2130 1.1384 -0.2750 0.1400 -0.0487 68 VAL A N +493 C CA . VAL A 69 ? 1.5946 0.9050 0.8318 -0.2745 0.1417 -0.0492 68 VAL A CA +494 C C . VAL A 69 ? 1.3618 0.6708 0.5989 -0.2749 0.1445 -0.0502 68 VAL A C +495 O O . VAL A 69 ? 1.7892 1.0980 1.0277 -0.2740 0.1459 -0.0506 68 VAL A O +496 C CB . VAL A 69 ? 1.4471 0.7583 0.6861 -0.2730 0.1408 -0.0488 68 VAL A CB +497 C CG1 . VAL A 69 ? 1.4147 0.7263 0.6528 -0.2735 0.1389 -0.0482 68 VAL A CG1 +498 C CG2 . VAL A 69 ? 2.0633 1.3761 1.3045 -0.2713 0.1398 -0.0483 68 VAL A CG2 +499 N N . GLN A 70 ? 1.8136 1.1216 1.0487 -0.2765 0.1453 -0.0506 69 GLN A N +500 C CA . GLN A 70 ? 1.7811 1.0879 1.0160 -0.2770 0.1478 -0.0514 69 GLN A CA +501 C C . GLN A 70 ? 1.4852 0.7910 0.7206 -0.2769 0.1502 -0.0523 69 GLN A C +502 O O . GLN A 70 ? 1.9556 1.2602 1.1907 -0.2774 0.1525 -0.0531 69 GLN A O +503 C CB . GLN A 70 ? 1.4859 0.7918 0.7185 -0.2789 0.1481 -0.0517 69 GLN A CB +504 C CG . GLN A 70 ? 1.7698 1.0766 1.0019 -0.2790 0.1462 -0.0510 69 GLN A CG +505 C CD . GLN A 70 ? 1.9628 1.2689 1.1925 -0.2809 0.1458 -0.0511 69 GLN A CD +506 O OE1 . GLN A 70 ? 1.8100 1.1151 1.0383 -0.2820 0.1466 -0.0515 69 GLN A OE1 +507 N NE2 . GLN A 70 ? 1.9005 1.2069 1.1294 -0.2812 0.1447 -0.0507 69 GLN A NE2 +508 N N . CYS A 71 ? 1.6945 1.0004 0.9306 -0.2763 0.1499 -0.0521 70 CYS A N +509 C CA . CYS A 71 ? 1.6309 0.9359 0.8678 -0.2758 0.1519 -0.0528 70 CYS A CA +510 C C . CYS A 71 ? 1.8205 1.1262 1.0596 -0.2742 0.1524 -0.0528 70 CYS A C +511 O O . CYS A 71 ? 1.8091 1.1141 1.0491 -0.2737 0.1542 -0.0534 70 CYS A O +512 C CB . CYS A 71 ? 1.4631 0.7681 0.6998 -0.2758 0.1512 -0.0526 70 CYS A CB +513 S SG . CYS A 71 ? 1.8714 1.1783 1.1092 -0.2746 0.1479 -0.0514 70 CYS A SG +514 N N . PHE A 72 ? 1.6328 0.9398 0.8729 -0.2733 0.1509 -0.0522 71 PHE A N +515 C CA . PHE A 72 ? 1.5956 0.9034 0.8378 -0.2718 0.1513 -0.0522 71 PHE A CA +516 C C . PHE A 72 ? 1.6141 0.9214 0.8562 -0.2721 0.1525 -0.0526 71 PHE A C +517 O O . PHE A 72 ? 2.1110 1.4190 1.3546 -0.2710 0.1524 -0.0525 71 PHE A O +518 C CB . PHE A 72 ? 1.4560 0.7655 0.6996 -0.2704 0.1487 -0.0512 71 PHE A CB +519 C CG . PHE A 72 ? 1.5322 0.8423 0.7765 -0.2697 0.1478 -0.0508 71 PHE A CG +520 C CD1 . PHE A 72 ? 1.6901 1.0002 0.9331 -0.2705 0.1463 -0.0504 71 PHE A CD1 +521 C CD2 . PHE A 72 ? 1.7786 1.0889 1.0247 -0.2684 0.1485 -0.0509 71 PHE A CD2 +522 C CE1 . PHE A 72 ? 1.5104 0.8209 0.7540 -0.2699 0.1454 -0.0501 71 PHE A CE1 +523 C CE2 . PHE A 72 ? 1.5805 0.8912 0.8272 -0.2678 0.1476 -0.0506 71 PHE A CE2 +524 C CZ . PHE A 72 ? 1.8832 1.1940 1.1287 -0.2685 0.1461 -0.0502 71 PHE A CZ +525 N N . SER A 73 ? 1.3965 0.7026 0.6368 -0.2737 0.1536 -0.0532 72 SER A N +526 C CA . SER A 73 ? 1.6804 0.9857 0.9203 -0.2741 0.1551 -0.0537 72 SER A CA +527 C C . SER A 73 ? 1.7210 1.0254 0.9620 -0.2737 0.1577 -0.0546 72 SER A C +528 O O . SER A 73 ? 2.0747 1.3790 1.3171 -0.2735 0.1585 -0.0550 72 SER A O +529 C CB . SER A 73 ? 1.5285 0.8328 0.7662 -0.2760 0.1556 -0.0540 72 SER A CB +530 N N . ARG A 74 ? 1.6663 0.9710 0.9090 -0.2731 0.1584 -0.0549 73 ARG A N +531 C CA . ARG A 74 ? 1.7065 1.0119 0.9542 -0.2721 0.1600 -0.0561 73 ARG A CA +532 C C . ARG A 74 ? 1.5833 0.8872 0.8299 -0.2736 0.1620 -0.0571 73 ARG A C +533 O O . ARG A 74 ? 1.6533 0.9564 0.8980 -0.2745 0.1624 -0.0572 73 ARG A O +534 C CB . ARG A 74 ? 1.7350 1.0420 0.9865 -0.2704 0.1596 -0.0562 73 ARG A CB +535 C CG . ARG A 74 ? 1.6677 0.9755 0.9246 -0.2692 0.1611 -0.0574 73 ARG A CG +536 C CD . ARG A 74 ? 1.5000 0.8095 0.7609 -0.2675 0.1605 -0.0575 73 ARG A CD +537 N NE . ARG A 74 ? 1.5706 0.8797 0.8301 -0.2681 0.1607 -0.0576 73 ARG A NE +538 C CZ . ARG A 74 ? 1.8044 1.1127 1.0643 -0.2689 0.1622 -0.0587 73 ARG A CZ +539 N NH1 . ARG A 74 ? 1.1560 0.4638 0.4176 -0.2692 0.1639 -0.0597 73 ARG A NH1 +540 N NH2 . ARG A 74 ? 1.5557 0.8636 0.8144 -0.2694 0.1622 -0.0587 73 ARG A NH2 +541 N N . TYR A 75 ? 1.6655 0.9689 0.9133 -0.2738 0.1633 -0.0578 74 TYR A N +542 C CA . TYR A 75 ? 1.8610 1.1631 1.1085 -0.2751 0.1653 -0.0589 74 TYR A CA +543 C C . TYR A 75 ? 1.8306 1.1338 1.0838 -0.2736 0.1666 -0.0601 74 TYR A C +544 O O . TYR A 75 ? 2.0078 1.3121 1.2650 -0.2721 0.1666 -0.0605 74 TYR A O +545 C CB . TYR A 75 ? 1.5485 0.8494 0.7939 -0.2763 0.1660 -0.0591 74 TYR A CB +546 C CG . TYR A 75 ? 1.6755 0.9748 0.9147 -0.2784 0.1656 -0.0584 74 TYR A CG +547 C CD1 . TYR A 75 ? 1.6389 0.9383 0.8751 -0.2785 0.1636 -0.0572 74 TYR A CD1 +548 C CD2 . TYR A 75 ? 1.8508 1.1484 1.0872 -0.2804 0.1671 -0.0590 74 TYR A CD2 +549 C CE1 . TYR A 75 ? 1.7692 1.0684 1.0029 -0.2799 0.1623 -0.0568 74 TYR A CE1 +550 C CE2 . TYR A 75 ? 1.6686 0.9651 0.9003 -0.2822 0.1665 -0.0585 74 TYR A CE2 +551 C CZ . TYR A 75 ? 1.8831 1.1810 1.1149 -0.2817 0.1637 -0.0574 74 TYR A CZ +552 O OH . TYR A 75 ? 1.8852 1.1833 1.1152 -0.2829 0.1624 -0.0571 74 TYR A OH +553 N N . PRO A 76 ? 1.6967 0.9996 0.9503 -0.2740 0.1675 -0.0609 75 PRO A N +554 C CA . PRO A 76 ? 1.5825 0.8862 0.8414 -0.2729 0.1688 -0.0622 75 PRO A CA +555 C C . PRO A 76 ? 2.1340 1.4371 1.3942 -0.2732 0.1704 -0.0632 75 PRO A C +556 O O . PRO A 76 ? 1.9712 1.2728 1.2277 -0.2748 0.1708 -0.0630 75 PRO A O +557 C CB . PRO A 76 ? 1.6435 0.9464 0.9010 -0.2739 0.1696 -0.0628 75 PRO A CB +558 C CG . PRO A 76 ? 1.7653 1.0675 1.0180 -0.2750 0.1683 -0.0615 75 PRO A CG +559 C CD . PRO A 76 ? 1.8458 1.1474 1.0951 -0.2756 0.1674 -0.0605 75 PRO A CD +560 N N . ASP A 77 ? 2.1124 1.4166 1.3780 -0.2717 0.1712 -0.0643 76 ASP A N +561 C CA . ASP A 77 ? 2.0820 1.3858 1.3496 -0.2717 0.1725 -0.0652 76 ASP A CA +562 C C . ASP A 77 ? 2.1432 1.4451 1.4081 -0.2737 0.1742 -0.0661 76 ASP A C +563 O O . ASP A 77 ? 1.7497 1.0506 1.0133 -0.2745 0.1749 -0.0662 76 ASP A O +564 C CB . ASP A 77 ? 2.4498 1.7551 1.7238 -0.2697 0.1730 -0.0664 76 ASP A CB +565 C CG . ASP A 77 ? 2.6540 1.9611 1.9308 -0.2678 0.1714 -0.0656 76 ASP A CG +566 O OD1 . ASP A 77 ? 2.4875 1.7947 1.7639 -0.2674 0.1706 -0.0647 76 ASP A OD1 +567 O OD2 . ASP A 77 ? 2.7763 2.0846 2.0556 -0.2667 0.1710 -0.0658 76 ASP A OD2 +568 N N . HIS A 78 ? 2.0261 1.3275 1.2902 -0.2744 0.1749 -0.0666 77 HIS A N +569 C CA . HIS A 78 ? 1.5171 0.8169 0.7788 -0.2763 0.1765 -0.0675 77 HIS A CA +570 C C . HIS A 78 ? 2.0318 1.3299 1.2871 -0.2785 0.1763 -0.0665 77 HIS A C +571 O O . HIS A 78 ? 2.1034 1.3999 1.3561 -0.2803 0.1776 -0.0670 77 HIS A O +572 C CB . HIS A 78 ? 1.6607 0.9606 0.9235 -0.2764 0.1772 -0.0685 77 HIS A CB +573 C CG . HIS A 78 ? 1.8829 1.1825 1.1421 -0.2772 0.1760 -0.0674 77 HIS A CG +574 N ND1 . HIS A 78 ? 1.8118 1.1129 1.0728 -0.2757 0.1745 -0.0668 77 HIS A ND1 +575 C CD2 . HIS A 78 ? 1.7159 1.0139 0.9699 -0.2792 0.1761 -0.0669 77 HIS A CD2 +576 C CE1 . HIS A 78 ? 1.9695 1.2699 1.2266 -0.2768 0.1738 -0.0659 77 HIS A CE1 +577 N NE2 . HIS A 78 ? 2.0996 1.3982 1.3524 -0.2789 0.1747 -0.0659 77 HIS A NE2 +578 N N . MET A 79 ? 2.0840 1.3823 1.3368 -0.2783 0.1745 -0.0649 78 MET A N +579 C CA . MET A 79 ? 1.8099 1.1068 1.0567 -0.2802 0.1739 -0.0639 78 MET A CA +580 C C . MET A 79 ? 2.0250 1.3219 1.2710 -0.2801 0.1732 -0.0632 78 MET A C +581 O O . MET A 79 ? 1.8059 1.1014 1.0476 -0.2819 0.1734 -0.0629 78 MET A O +582 C CB . MET A 79 ? 1.6101 0.9072 0.8540 -0.2804 0.1723 -0.0627 78 MET A CB +583 C CG . MET A 79 ? 1.9476 1.2444 1.1912 -0.2810 0.1729 -0.0631 78 MET A CG +584 S SD . MET A 79 ? 1.9283 1.2247 1.1671 -0.2818 0.1711 -0.0616 78 MET A SD +585 C CE . MET A 79 ? 1.6550 0.9498 0.8878 -0.2837 0.1706 -0.0606 78 MET A CE +586 N N . LYS A 80 ? 1.7526 1.0510 1.0028 -0.2781 0.1725 -0.0631 79 LYS A N +587 C CA . LYS A 80 ? 1.8425 1.1412 1.0926 -0.2777 0.1715 -0.0625 79 LYS A CA +588 C C . LYS A 80 ? 1.8533 1.1506 1.1010 -0.2792 0.1724 -0.0627 79 LYS A C +589 O O . LYS A 80 ? 2.2764 1.5740 1.5244 -0.2788 0.1716 -0.0622 79 LYS A O +590 C CB . LYS A 80 ? 1.5687 0.8691 0.8246 -0.2753 0.1712 -0.0628 79 LYS A CB +591 C CG . LYS A 80 ? 1.8966 1.1987 1.1548 -0.2737 0.1699 -0.0622 79 LYS A CG +592 C CD . LYS A 80 ? 1.5266 0.8304 0.7899 -0.2715 0.1694 -0.0623 79 LYS A CD +593 C CE . LYS A 80 ? 1.7847 1.0901 1.0504 -0.2699 0.1680 -0.0618 79 LYS A CE +594 N NZ . LYS A 80 ? 1.9349 1.2408 1.1979 -0.2698 0.1660 -0.0604 79 LYS A NZ +595 N N . GLN A 81 ? 2.0183 1.3140 1.2637 -0.2810 0.1741 -0.0635 80 GLN A N +596 C CA . GLN A 81 ? 2.1715 1.4658 1.4142 -0.2826 0.1749 -0.0637 80 GLN A CA +597 C C . GLN A 81 ? 2.1908 1.4837 1.4272 -0.2848 0.1745 -0.0630 80 GLN A C +598 O O . GLN A 81 ? 2.3081 1.5995 1.5413 -0.2865 0.1752 -0.0632 80 GLN A O +599 C CB . GLN A 81 ? 2.1005 1.3941 1.3456 -0.2830 0.1772 -0.0652 80 GLN A CB +600 C CG . GLN A 81 ? 1.9517 1.2444 1.1955 -0.2842 0.1786 -0.0661 80 GLN A CG +601 C CD . GLN A 81 ? 2.2546 1.5486 1.5023 -0.2826 0.1785 -0.0665 80 GLN A CD +602 O OE1 . GLN A 81 ? 2.4635 1.7592 1.7151 -0.2806 0.1776 -0.0663 80 GLN A OE1 +603 N NE2 . GLN A 81 ? 1.9689 1.2623 1.2155 -0.2836 0.1795 -0.0671 80 GLN A NE2 +604 N N . HIS A 82 ? 2.0727 1.3659 1.3071 -0.2847 0.1731 -0.0621 81 HIS A N +605 C CA . HIS A 82 ? 2.1370 1.4290 1.3655 -0.2865 0.1723 -0.0613 81 HIS A CA +606 C C . HIS A 82 ? 2.1244 1.4177 1.3523 -0.2855 0.1696 -0.0600 81 HIS A C +607 O O . HIS A 82 ? 1.9287 1.2228 1.1559 -0.2858 0.1676 -0.0592 81 HIS A O +608 C CB . HIS A 82 ? 2.0913 1.3827 1.3179 -0.2875 0.1729 -0.0614 81 HIS A CB +609 C CG . HIS A 82 ? 2.0428 1.3332 1.2705 -0.2884 0.1753 -0.0627 81 HIS A CG +610 N ND1 . HIS A 82 ? 2.0688 1.3577 1.2936 -0.2904 0.1766 -0.0633 81 HIS A ND1 +611 C CD2 . HIS A 82 ? 1.6221 0.9130 0.8534 -0.2876 0.1764 -0.0637 81 HIS A CD2 +612 C CE1 . HIS A 82 ? 2.2249 1.5132 1.4516 -0.2908 0.1786 -0.0645 81 HIS A CE1 +613 N NE2 . HIS A 82 ? 2.2905 1.5802 1.5213 -0.2891 0.1784 -0.0649 81 HIS A NE2 +614 N N . ASP A 83 ? 1.9120 1.2065 1.1431 -0.2838 0.1689 -0.0598 82 ASP A N +615 C CA . ASP A 83 ? 1.8937 1.1892 1.1243 -0.2828 0.1666 -0.0586 82 ASP A CA +616 C C . ASP A 83 ? 1.8345 1.1298 1.0639 -0.2834 0.1656 -0.0583 82 ASP A C +617 O O . ASP A 83 ? 2.0508 1.3464 1.2821 -0.2826 0.1658 -0.0584 82 ASP A O +618 C CB . ASP A 83 ? 2.4121 1.7095 1.6484 -0.2803 0.1661 -0.0586 82 ASP A CB +619 C CG . ASP A 83 ? 2.2482 1.5469 1.4843 -0.2791 0.1637 -0.0574 82 ASP A CG +620 O OD1 . ASP A 83 ? 1.9082 1.2069 1.1417 -0.2798 0.1621 -0.0567 82 ASP A OD1 +621 O OD2 . ASP A 83 ? 2.4131 1.7132 1.6527 -0.2774 0.1632 -0.0573 82 ASP A OD2 +622 N N . PHE A 84 ? 1.8435 1.1392 1.0713 -0.2846 0.1641 -0.0579 83 PHE A N +623 C CA . PHE A 84 ? 1.5834 0.8790 0.8099 -0.2854 0.1629 -0.0576 83 PHE A CA +624 C C . PHE A 84 ? 1.8031 1.1001 1.0309 -0.2840 0.1606 -0.0566 83 PHE A C +625 O O . PHE A 84 ? 2.1741 1.4709 1.4020 -0.2838 0.1605 -0.0566 83 PHE A O +626 C CB . PHE A 84 ? 1.6242 0.9199 0.8487 -0.2870 0.1618 -0.0573 83 PHE A CB +627 C CG . PHE A 84 ? 1.9210 1.2172 1.1445 -0.2874 0.1597 -0.0567 83 PHE A CG +628 C CD1 . PHE A 84 ? 2.2055 1.5005 1.4277 -0.2885 0.1605 -0.0571 83 PHE A CD1 +629 C CD2 . PHE A 84 ? 1.7834 1.0811 1.0072 -0.2869 0.1569 -0.0557 83 PHE A CD2 +630 C CE1 . PHE A 84 ? 2.1028 1.3982 1.3241 -0.2890 0.1586 -0.0566 83 PHE A CE1 +631 C CE2 . PHE A 84 ? 2.1603 1.4584 1.3832 -0.2874 0.1549 -0.0551 83 PHE A CE2 +632 C CZ . PHE A 84 ? 2.1976 1.4946 1.4192 -0.2884 0.1558 -0.0556 83 PHE A CZ +633 N N . PHE A 85 ? 1.6678 0.9663 0.8967 -0.2829 0.1588 -0.0559 84 PHE A N +634 C CA . PHE A 85 ? 1.6888 0.9889 0.9190 -0.2815 0.1564 -0.0549 84 PHE A CA +635 C C . PHE A 85 ? 1.8707 1.1707 1.1025 -0.2803 0.1569 -0.0550 84 PHE A C +636 O O . PHE A 85 ? 2.2098 1.5100 1.4414 -0.2802 0.1558 -0.0546 84 PHE A O +637 C CB . PHE A 85 ? 1.8037 1.1051 1.0352 -0.2804 0.1551 -0.0544 84 PHE A CB +638 C CG . PHE A 85 ? 1.8187 1.1203 1.0488 -0.2815 0.1542 -0.0542 84 PHE A CG +639 C CD1 . PHE A 85 ? 1.8025 1.1041 1.0308 -0.2827 0.1528 -0.0538 84 PHE A CD1 +640 C CD2 . PHE A 85 ? 1.8078 1.1094 1.0383 -0.2813 0.1549 -0.0543 84 PHE A CD2 +641 C CE1 . PHE A 85 ? 1.8487 1.1504 1.0757 -0.2838 0.1520 -0.0536 84 PHE A CE1 +642 C CE2 . PHE A 85 ? 1.4449 0.7466 0.6740 -0.2823 0.1541 -0.0541 84 PHE A CE2 +643 C CZ . PHE A 85 ? 1.7139 1.0157 0.9413 -0.2836 0.1526 -0.0538 84 PHE A CZ +644 N N . LYS A 86 ? 1.9630 1.2626 1.1961 -0.2794 0.1587 -0.0555 85 LYS A N +645 C CA . LYS A 86 ? 2.0540 1.3541 1.2900 -0.2780 0.1591 -0.0556 85 LYS A CA +646 C C . LYS A 86 ? 2.0511 1.3504 1.2878 -0.2787 0.1602 -0.0562 85 LYS A C +647 O O . LYS A 86 ? 1.8051 1.1052 1.0438 -0.2778 0.1593 -0.0559 85 LYS A O +648 C CB . LYS A 86 ? 1.7642 1.0653 1.0047 -0.2764 0.1602 -0.0561 85 LYS A CB +649 C CG . LYS A 86 ? 1.7241 1.0262 0.9647 -0.2755 0.1590 -0.0556 85 LYS A CG +650 C CD . LYS A 86 ? 1.7254 1.0288 0.9711 -0.2737 0.1599 -0.0561 85 LYS A CD +651 C CE . LYS A 86 ? 1.6152 0.9196 0.8611 -0.2729 0.1589 -0.0556 85 LYS A CE +652 N NZ . LYS A 86 ? 2.0383 1.3413 1.2800 -0.2746 0.1594 -0.0556 85 LYS A NZ +653 N N . SER A 87 ? 2.0464 1.3443 1.2813 -0.2802 0.1621 -0.0570 86 SER A N +654 C CA . SER A 87 ? 2.0450 1.3420 1.2807 -0.2809 0.1633 -0.0577 86 SER A CA +655 C C . SER A 87 ? 1.9951 1.2918 1.2286 -0.2817 0.1619 -0.0572 86 SER A C +656 O O . SER A 87 ? 1.9899 1.2864 1.2249 -0.2817 0.1625 -0.0575 86 SER A O +657 C CB . SER A 87 ? 2.1455 1.4409 1.3792 -0.2826 0.1656 -0.0587 86 SER A CB +658 O OG . SER A 87 ? 2.0514 1.3455 1.2795 -0.2846 0.1652 -0.0584 86 SER A OG +659 N N . ALA A 88 ? 2.0558 1.3524 1.2856 -0.2823 0.1601 -0.0564 87 ALA A N +660 C CA . ALA A 88 ? 1.8644 1.1610 1.0924 -0.2831 0.1584 -0.0558 87 ALA A CA +661 C C . ALA A 88 ? 1.7733 1.0712 1.0040 -0.2815 0.1567 -0.0551 87 ALA A C +662 O O . ALA A 88 ? 2.0208 1.3187 1.2508 -0.2819 0.1555 -0.0548 87 ALA A O +663 C CB . ALA A 88 ? 1.8271 1.1247 1.0541 -0.2838 0.1563 -0.0552 87 ALA A CB +664 N N . MET A 89 ? 1.7205 1.0198 0.9548 -0.2795 0.1566 -0.0550 88 MET A N +665 C CA . MET A 89 ? 1.9126 1.2135 1.1502 -0.2777 0.1549 -0.0543 88 MET A CA +666 C C . MET A 89 ? 1.7674 1.0686 1.0088 -0.2771 0.1558 -0.0547 88 MET A C +667 O O . MET A 89 ? 1.9381 1.2384 1.1802 -0.2776 0.1578 -0.0556 88 MET A O +668 C CB . MET A 89 ? 1.7935 1.0958 1.0335 -0.2760 0.1545 -0.0540 88 MET A CB +669 C CG . MET A 89 ? 2.0827 1.3849 1.3192 -0.2766 0.1535 -0.0535 88 MET A CG +670 S SD . MET A 89 ? 1.9240 1.2270 1.1587 -0.2768 0.1504 -0.0524 88 MET A SD +671 C CE . MET A 89 ? 2.1144 1.4183 1.3486 -0.2773 0.1493 -0.0521 88 MET A CE +672 N N . PRO A 90 ? 1.7298 1.0321 0.9736 -0.2759 0.1542 -0.0540 89 PRO A N +673 C CA . PRO A 90 ? 2.1286 1.4321 1.3719 -0.2751 0.1518 -0.0530 89 PRO A CA +674 C C . PRO A 90 ? 2.0346 1.3375 1.2741 -0.2765 0.1502 -0.0525 89 PRO A C +675 O O . PRO A 90 ? 2.0932 1.3968 1.3316 -0.2762 0.1481 -0.0517 89 PRO A O +676 C CB . PRO A 90 ? 1.9073 1.2122 1.1554 -0.2733 0.1512 -0.0527 89 PRO A CB +677 C CG . PRO A 90 ? 1.8949 1.1989 1.1442 -0.2739 0.1527 -0.0533 89 PRO A CG +678 C CD . PRO A 90 ? 1.8060 1.1085 1.0535 -0.2752 0.1549 -0.0543 89 PRO A CD +679 N N . GLU A 91 ? 1.7688 1.0702 1.0063 -0.2782 0.1512 -0.0530 90 GLU A N +680 C CA . GLU A 91 ? 2.0703 1.3711 1.3044 -0.2797 0.1498 -0.0526 90 GLU A CA +681 C C . GLU A 91 ? 1.9964 1.2967 1.2262 -0.2807 0.1488 -0.0523 90 GLU A C +682 O O . GLU A 91 ? 1.8742 1.1753 1.1033 -0.2808 0.1465 -0.0516 90 GLU A O +683 C CB . GLU A 91 ? 2.4143 1.7137 1.6473 -0.2814 0.1513 -0.0533 90 GLU A CB +684 C CG . GLU A 91 ? 2.5590 1.8587 1.7963 -0.2805 0.1522 -0.0535 90 GLU A CG +685 C CD . GLU A 91 ? 2.7848 2.0836 2.0211 -0.2819 0.1523 -0.0536 90 GLU A CD +686 O OE1 . GLU A 91 ? 2.6447 1.9441 1.8812 -0.2818 0.1503 -0.0528 90 GLU A OE1 +687 O OE2 . GLU A 91 ? 2.9011 2.1986 2.1367 -0.2830 0.1543 -0.0544 90 GLU A OE2 +688 N N . GLY A 92 ? 1.8692 1.1692 1.0984 -0.2810 0.1502 -0.0528 91 GLY A N +689 C CA . GLY A 92 ? 1.7930 1.0941 1.0220 -0.2811 0.1486 -0.0523 91 GLY A CA +690 C C . GLY A 92 ? 1.7849 1.0854 1.0118 -0.2830 0.1487 -0.0526 91 GLY A C +691 O O . GLY A 92 ? 2.0068 1.3058 1.2321 -0.2845 0.1502 -0.0533 91 GLY A O +692 N N . TYR A 93 ? 1.7392 1.0407 0.9659 -0.2831 0.1471 -0.0521 92 TYR A N +693 C CA . TYR A 93 ? 1.8607 1.1618 1.0854 -0.2848 0.1469 -0.0522 92 TYR A CA +694 C C . TYR A 93 ? 1.8988 1.2011 1.1230 -0.2850 0.1440 -0.0513 92 TYR A C +695 O O . TYR A 93 ? 1.9245 1.2281 1.1502 -0.2836 0.1421 -0.0505 92 TYR A O +696 C CB . TYR A 93 ? 1.6574 0.9582 0.8822 -0.2850 0.1486 -0.0528 92 TYR A CB +697 C CG . TYR A 93 ? 1.9429 1.2450 1.1695 -0.2834 0.1478 -0.0524 92 TYR A CG +698 C CD1 . TYR A 93 ? 2.1704 1.4737 1.3968 -0.2834 0.1457 -0.0516 92 TYR A CD1 +699 C CD2 . TYR A 93 ? 1.6751 0.9772 0.9035 -0.2821 0.1493 -0.0527 92 TYR A CD2 +700 C CE1 . TYR A 93 ? 2.0546 1.3591 1.2827 -0.2820 0.1450 -0.0512 92 TYR A CE1 +701 C CE2 . TYR A 93 ? 1.9321 1.2355 1.1622 -0.2807 0.1487 -0.0523 92 TYR A CE2 +702 C CZ . TYR A 93 ? 1.9318 1.2363 1.1617 -0.2807 0.1465 -0.0516 92 TYR A CZ +703 O OH . TYR A 93 ? 1.9713 1.2769 1.2027 -0.2794 0.1458 -0.0512 92 TYR A OH +704 N N . VAL A 94 ? 1.9656 1.2675 1.1879 -0.2866 0.1436 -0.0514 93 VAL A N +705 C CA . VAL A 94 ? 1.9587 1.2616 1.1803 -0.2870 0.1409 -0.0506 93 VAL A CA +706 C C . VAL A 94 ? 1.9683 1.2714 1.1894 -0.2874 0.1410 -0.0506 93 VAL A C +707 O O . VAL A 94 ? 1.9394 1.2415 1.1593 -0.2886 0.1428 -0.0514 93 VAL A O +708 C CB . VAL A 94 ? 1.9791 1.2812 1.1985 -0.2888 0.1401 -0.0505 93 VAL A CB +709 C CG1 . VAL A 94 ? 1.8308 1.1339 1.0495 -0.2891 0.1373 -0.0497 93 VAL A CG1 +710 C CG2 . VAL A 94 ? 1.9899 1.2914 1.2094 -0.2887 0.1404 -0.0506 93 VAL A CG2 +711 N N . GLN A 95 ? 1.6140 0.9185 0.8361 -0.2864 0.1391 -0.0498 94 GLN A N +712 C CA . GLN A 95 ? 1.8134 1.1182 1.0351 -0.2866 0.1390 -0.0498 94 GLN A CA +713 C C . GLN A 95 ? 1.9873 1.2927 1.2077 -0.2875 0.1366 -0.0492 94 GLN A C +714 O O . GLN A 95 ? 1.6755 0.9821 0.8968 -0.2866 0.1343 -0.0483 94 GLN A O +715 C CB . GLN A 95 ? 1.6667 0.9726 0.8907 -0.2847 0.1391 -0.0496 94 GLN A CB +716 C CG . GLN A 95 ? 1.5828 0.8889 0.8066 -0.2848 0.1390 -0.0495 94 GLN A CG +717 C CD . GLN A 95 ? 1.8076 1.1145 1.0336 -0.2831 0.1396 -0.0495 94 GLN A CD +718 O OE1 . GLN A 95 ? 1.7296 1.0360 0.9566 -0.2825 0.1417 -0.0501 94 GLN A OE1 +719 N NE2 . GLN A 95 ? 1.9191 1.2273 1.1459 -0.2822 0.1378 -0.0487 94 GLN A NE2 +720 N N . GLU A 96 ? 1.8431 1.1475 1.0613 -0.2894 0.1371 -0.0496 95 GLU A N +721 C CA . GLU A 96 ? 1.4964 0.8011 0.7130 -0.2905 0.1350 -0.0490 95 GLU A CA +722 C C . GLU A 96 ? 1.7683 1.0731 0.9845 -0.2907 0.1351 -0.0490 95 GLU A C +723 O O . GLU A 96 ? 1.8493 1.1532 1.0649 -0.2913 0.1373 -0.0497 95 GLU A O +724 C CB . GLU A 96 ? 1.9146 1.2181 1.1288 -0.2926 0.1353 -0.0494 95 GLU A CB +725 C CG . GLU A 96 ? 2.3162 1.6197 1.5304 -0.2927 0.1342 -0.0491 95 GLU A CG +726 C CD . GLU A 96 ? 2.7772 2.0792 1.9891 -0.2947 0.1351 -0.0497 95 GLU A CD +727 O OE1 . GLU A 96 ? 2.8728 2.1736 2.0841 -0.2955 0.1376 -0.0506 95 GLU A OE1 +728 O OE2 . GLU A 96 ? 2.7388 2.0407 1.9495 -0.2957 0.1334 -0.0493 95 GLU A OE2 +729 N N . ARG A 97 ? 1.5143 0.8203 0.7309 -0.2901 0.1328 -0.0482 96 ARG A N +730 C CA . ARG A 97 ? 1.7675 1.0736 0.9835 -0.2904 0.1327 -0.0481 96 ARG A CA +731 C C . ARG A 97 ? 1.9494 1.2558 1.1637 -0.2915 0.1304 -0.0475 96 ARG A C +732 O O . ARG A 97 ? 1.7928 1.0994 1.0067 -0.2918 0.1286 -0.0470 96 ARG A O +733 C CB . ARG A 97 ? 1.4739 0.7812 0.6922 -0.2884 0.1322 -0.0476 96 ARG A CB +734 C CG . ARG A 97 ? 2.0752 1.3822 1.2950 -0.2874 0.1347 -0.0483 96 ARG A CG +735 C CD . ARG A 97 ? 1.7979 1.1056 1.0190 -0.2863 0.1346 -0.0480 96 ARG A CD +736 N NE . ARG A 97 ? 1.9350 1.2426 1.1578 -0.2850 0.1366 -0.0485 96 ARG A NE +737 C CZ . ARG A 97 ? 1.8589 1.1676 1.0841 -0.2832 0.1360 -0.0481 96 ARG A CZ +738 N NH1 . ARG A 97 ? 1.9662 1.2761 1.1921 -0.2823 0.1336 -0.0472 96 ARG A NH1 +739 N NH2 . ARG A 97 ? 1.8275 1.1359 1.0541 -0.2822 0.1380 -0.0486 96 ARG A NH2 +740 N N . THR A 98 ? 1.7874 1.0934 1.0006 -0.2923 0.1306 -0.0476 97 THR A N +741 C CA . THR A 98 ? 2.0692 1.3755 1.2810 -0.2931 0.1283 -0.0470 97 THR A CA +742 C C . THR A 98 ? 1.8546 1.1616 1.0672 -0.2922 0.1282 -0.0467 97 THR A C +743 O O . THR A 98 ? 1.6162 0.9225 0.8289 -0.2923 0.1303 -0.0473 97 THR A O +744 C CB . THR A 98 ? 2.1392 1.4443 1.3481 -0.2955 0.1287 -0.0474 97 THR A CB +745 O OG1 . THR A 98 ? 1.7332 1.0376 0.9415 -0.2964 0.1292 -0.0478 97 THR A OG1 +746 C CG2 . THR A 98 ? 1.4324 0.7378 0.6400 -0.2963 0.1261 -0.0467 97 THR A CG2 +747 N N . ILE A 99 ? 1.5617 0.8698 0.7749 -0.2914 0.1259 -0.0458 98 ILE A N +748 C CA . ILE A 99 ? 1.8192 1.1278 1.0334 -0.2903 0.1257 -0.0455 98 ILE A CA +749 C C . ILE A 99 ? 1.9703 1.2791 1.1830 -0.2912 0.1237 -0.0449 98 ILE A C +750 O O . ILE A 99 ? 1.7009 1.0105 0.9138 -0.2908 0.1213 -0.0441 98 ILE A O +751 C CB . ILE A 99 ? 1.6433 0.9533 0.8603 -0.2881 0.1249 -0.0450 98 ILE A CB +752 C CG1 . ILE A 99 ? 1.3787 0.6884 0.5970 -0.2873 0.1269 -0.0455 98 ILE A CG1 +753 C CG2 . ILE A 99 ? 1.3252 0.6358 0.5432 -0.2870 0.1248 -0.0446 98 ILE A CG2 +754 C CD1 . ILE A 99 ? 1.5871 0.8981 0.8080 -0.2852 0.1261 -0.0451 98 ILE A CD1 +755 N N . PHE A 100 ? 1.6380 0.9459 0.8491 -0.2924 0.1247 -0.0453 99 PHE A N +756 C CA . PHE A 100 ? 1.4978 0.8056 0.7072 -0.2933 0.1230 -0.0448 99 PHE A CA +757 C C . PHE A 100 ? 1.5649 0.8735 0.7758 -0.2919 0.1225 -0.0443 99 PHE A C +758 O O . PHE A 100 ? 1.6479 0.9561 0.8592 -0.2916 0.1243 -0.0447 99 PHE A O +759 C CB . PHE A 100 ? 1.3067 0.6131 0.5136 -0.2955 0.1243 -0.0454 99 PHE A CB +760 C CG . PHE A 100 ? 1.8514 1.1569 1.0568 -0.2970 0.1251 -0.0460 99 PHE A CG +761 C CD1 . PHE A 100 ? 1.8867 1.1922 1.0908 -0.2981 0.1232 -0.0457 99 PHE A CD1 +762 C CD2 . PHE A 100 ? 1.9368 1.2414 1.1423 -0.2974 0.1278 -0.0470 99 PHE A CD2 +763 C CE1 . PHE A 100 ? 1.7883 1.0929 0.9910 -0.2996 0.1240 -0.0463 99 PHE A CE1 +764 C CE2 . PHE A 100 ? 1.7521 1.0559 0.9563 -0.2988 0.1286 -0.0475 99 PHE A CE2 +765 C CZ . PHE A 100 ? 1.6716 0.9754 0.8744 -0.2999 0.1267 -0.0472 99 PHE A CZ +766 N N . PHE A 101 ? 1.5132 0.8229 0.7247 -0.2910 0.1200 -0.0434 100 PHE A N +767 C CA . PHE A 101 ? 1.6246 0.9348 0.8369 -0.2900 0.1193 -0.0428 100 PHE A CA +768 C C . PHE A 101 ? 1.7175 1.0269 0.9273 -0.2917 0.1186 -0.0427 100 PHE A C +769 O O . PHE A 101 ? 1.7214 1.0303 0.9293 -0.2931 0.1174 -0.0426 100 PHE A O +770 C CB . PHE A 101 ? 1.3268 0.6384 0.5409 -0.2884 0.1170 -0.0419 100 PHE A CB +771 C CG . PHE A 101 ? 1.7287 1.0411 0.9451 -0.2867 0.1175 -0.0420 100 PHE A CG +772 C CD1 . PHE A 101 ? 1.9354 1.2478 1.1519 -0.2871 0.1178 -0.0423 100 PHE A CD1 +773 C CD2 . PHE A 101 ? 1.8116 1.1250 1.0304 -0.2848 0.1175 -0.0417 100 PHE A CD2 +774 C CE1 . PHE A 101 ? 1.3810 0.6940 0.5995 -0.2856 0.1182 -0.0423 100 PHE A CE1 +775 C CE2 . PHE A 101 ? 1.6845 0.9987 0.9055 -0.2834 0.1180 -0.0418 100 PHE A CE2 +776 C CZ . PHE A 101 ? 1.7772 1.0912 0.9981 -0.2838 0.1183 -0.0421 100 PHE A CZ +777 N N . LYS A 102 ? 1.5837 0.8927 0.7933 -0.2916 0.1194 -0.0428 101 LYS A N +778 C CA . LYS A 102 ? 2.0025 1.3105 1.2096 -0.2933 0.1190 -0.0427 101 LYS A CA +779 C C . LYS A 102 ? 2.2009 1.5097 1.4076 -0.2931 0.1161 -0.0418 101 LYS A C +780 O O . LYS A 102 ? 1.6245 0.9343 0.8330 -0.2915 0.1149 -0.0412 101 LYS A O +781 C CB . LYS A 102 ? 1.6674 0.9748 0.8746 -0.2933 0.1207 -0.0430 101 LYS A CB +782 C CG . LYS A 102 ? 1.9549 1.2612 1.1594 -0.2951 0.1207 -0.0431 101 LYS A CG +783 C CD . LYS A 102 ? 2.2645 1.5702 1.4693 -0.2948 0.1220 -0.0432 101 LYS A CD +784 C CE . LYS A 102 ? 2.0823 1.3865 1.2845 -0.2969 0.1232 -0.0436 101 LYS A CE +785 N NZ . LYS A 102 ? 2.2738 1.5776 1.4750 -0.2971 0.1223 -0.0431 101 LYS A NZ +786 N N . ASP A 103 ? 1.9353 1.2434 1.1395 -0.2949 0.1149 -0.0417 102 ASP A N +787 C CA . ASP A 103 ? 1.9193 1.2278 1.1227 -0.2951 0.1122 -0.0409 102 ASP A CA +788 C C . ASP A 103 ? 1.8408 1.1505 1.0457 -0.2939 0.1103 -0.0403 102 ASP A C +789 O O . ASP A 103 ? 1.8737 1.1842 1.0792 -0.2931 0.1082 -0.0395 102 ASP A O +790 C CB . ASP A 103 ? 2.1512 1.4600 1.3550 -0.2943 0.1116 -0.0403 102 ASP A CB +791 C CG . ASP A 103 ? 2.3118 1.6193 1.5138 -0.2956 0.1130 -0.0407 102 ASP A CG +792 O OD1 . ASP A 103 ? 2.2626 1.5690 1.4625 -0.2975 0.1140 -0.0413 102 ASP A OD1 +793 O OD2 . ASP A 103 ? 2.2179 1.5254 1.4205 -0.2949 0.1133 -0.0405 102 ASP A OD2 +794 N N . ASP A 104 ? 1.6609 0.9707 0.8665 -0.2939 0.1111 -0.0407 103 ASP A N +795 C CA . ASP A 104 ? 1.6318 0.9427 0.8391 -0.2927 0.1096 -0.0402 103 ASP A CA +796 C C . ASP A 104 ? 1.7370 1.0476 0.9443 -0.2932 0.1106 -0.0408 103 ASP A C +797 O O . ASP A 104 ? 1.4668 0.7763 0.6726 -0.2946 0.1123 -0.0416 103 ASP A O +798 C CB . ASP A 104 ? 1.3108 0.6229 0.5209 -0.2903 0.1097 -0.0399 103 ASP A CB +799 C CG . ASP A 104 ? 2.0910 1.4044 1.3029 -0.2890 0.1080 -0.0393 103 ASP A CG +800 O OD1 . ASP A 104 ? 1.5355 0.8486 0.7463 -0.2900 0.1068 -0.0392 103 ASP A OD1 +801 O OD2 . ASP A 104 ? 3.2244 2.5388 2.4385 -0.2872 0.1079 -0.0390 103 ASP A OD2 +802 N N . GLY A 105 ? 1.7210 1.0326 0.9300 -0.2920 0.1096 -0.0404 104 GLY A N +803 C CA . GLY A 105 ? 1.3637 0.6750 0.5726 -0.2925 0.1100 -0.0408 104 GLY A CA +804 C C . GLY A 105 ? 1.8895 1.2005 1.0994 -0.2921 0.1127 -0.0416 104 GLY A C +805 O O . GLY A 105 ? 1.7778 1.0886 0.9883 -0.2915 0.1144 -0.0419 104 GLY A O +806 N N . ASN A 106 ? 1.6248 0.9357 0.8349 -0.2923 0.1131 -0.0419 105 ASN A N +807 C CA . ASN A 106 ? 1.7214 1.0319 0.9324 -0.2920 0.1156 -0.0426 105 ASN A CA +808 C C . ASN A 106 ? 1.9374 1.2485 1.1502 -0.2908 0.1154 -0.0425 105 ASN A C +809 O O . ASN A 106 ? 1.8521 1.1637 1.0648 -0.2909 0.1134 -0.0419 105 ASN A O +810 C CB . ASN A 106 ? 1.7884 1.0974 0.9971 -0.2941 0.1173 -0.0435 105 ASN A CB +811 C CG . ASN A 106 ? 1.6831 0.9915 0.8900 -0.2957 0.1158 -0.0433 105 ASN A CG +812 O OD1 . ASN A 106 ? 1.6848 0.9933 0.8922 -0.2955 0.1157 -0.0434 105 ASN A OD1 +813 N ND2 . ASN A 106 ? 1.6147 0.9226 0.8194 -0.2973 0.1147 -0.0432 105 ASN A ND2 +814 N N . TYR A 107 ? 1.6693 0.9805 0.8836 -0.2897 0.1174 -0.0430 106 TYR A N +815 C CA . TYR A 107 ? 1.6597 0.9713 0.8755 -0.2888 0.1177 -0.0430 106 TYR A CA +816 C C . TYR A 107 ? 1.7532 1.0635 0.9678 -0.2902 0.1197 -0.0439 106 TYR A C +817 O O . TYR A 107 ? 1.4738 0.7830 0.6873 -0.2911 0.1216 -0.0446 106 TYR A O +818 C CB . TYR A 107 ? 1.5665 0.8789 0.7850 -0.2867 0.1187 -0.0430 106 TYR A CB +819 C CG . TYR A 107 ? 1.6582 0.9720 0.8783 -0.2851 0.1170 -0.0422 106 TYR A CG +820 C CD1 . TYR A 107 ? 1.6699 0.9844 0.8896 -0.2851 0.1143 -0.0414 106 TYR A CD1 +821 C CD2 . TYR A 107 ? 1.7856 1.1000 1.0077 -0.2835 0.1180 -0.0423 106 TYR A CD2 +822 C CE1 . TYR A 107 ? 1.3761 0.6918 0.5974 -0.2836 0.1128 -0.0407 106 TYR A CE1 +823 C CE2 . TYR A 107 ? 1.3678 0.6833 0.5913 -0.2821 0.1166 -0.0416 106 TYR A CE2 +824 C CZ . TYR A 107 ? 1.7124 1.0286 0.9355 -0.2821 0.1140 -0.0408 106 TYR A CZ +825 O OH . TYR A 107 ? 1.6067 0.9241 0.8314 -0.2807 0.1126 -0.0402 106 TYR A OH +826 N N . LYS A 108 ? 1.5341 0.8443 0.7487 -0.2903 0.1192 -0.0438 107 LYS A N +827 C CA . LYS A 108 ? 1.6215 0.9306 0.8354 -0.2912 0.1213 -0.0446 107 LYS A CA +828 C C . LYS A 108 ? 1.8461 1.1557 1.0620 -0.2898 0.1215 -0.0446 107 LYS A C +829 O O . LYS A 108 ? 1.9113 1.2216 1.1277 -0.2893 0.1196 -0.0439 107 LYS A O +830 C CB . LYS A 108 ? 1.6806 0.9886 0.8920 -0.2934 0.1207 -0.0448 107 LYS A CB +831 C CG . LYS A 108 ? 1.8214 1.1285 1.0306 -0.2951 0.1212 -0.0452 107 LYS A CG +832 C CD . LYS A 108 ? 1.8328 1.1391 1.0396 -0.2973 0.1201 -0.0451 107 LYS A CD +833 C CE . LYS A 108 ? 2.0252 1.3303 1.2296 -0.2992 0.1212 -0.0458 107 LYS A CE +834 N NZ . LYS A 108 ? 2.0154 1.3196 1.2197 -0.2996 0.1243 -0.0468 107 LYS A NZ +835 N N . THR A 109 ? 1.8134 1.1226 1.0304 -0.2890 0.1238 -0.0452 108 THR A N +836 C CA . THR A 109 ? 1.8077 1.1175 1.0267 -0.2875 0.1242 -0.0452 108 THR A CA +837 C C . THR A 109 ? 1.8173 1.1259 1.0358 -0.2882 0.1263 -0.0459 108 THR A C +838 O O . THR A 109 ? 1.4741 0.7815 0.6910 -0.2896 0.1280 -0.0467 108 THR A O +839 C CB . THR A 109 ? 1.7352 1.0458 0.9565 -0.2856 0.1251 -0.0452 108 THR A CB +840 O OG1 . THR A 109 ? 1.5962 0.9058 0.8172 -0.2860 0.1278 -0.0460 108 THR A OG1 +841 C CG2 . THR A 109 ? 1.8438 1.1555 1.0655 -0.2850 0.1234 -0.0445 108 THR A CG2 +842 N N . ARG A 110 ? 1.6091 0.9181 0.8290 -0.2872 0.1261 -0.0458 109 ARG A N +843 C CA . ARG A 110 ? 1.6112 0.9192 0.8310 -0.2874 0.1282 -0.0465 109 ARG A CA +844 C C . ARG A 110 ? 1.6235 0.9322 0.8456 -0.2855 0.1282 -0.0463 109 ARG A C +845 O O . ARG A 110 ? 1.5672 0.8768 0.7902 -0.2848 0.1264 -0.0456 109 ARG A O +846 C CB . ARG A 110 ? 1.6521 0.9591 0.8700 -0.2891 0.1277 -0.0466 109 ARG A CB +847 C CG . ARG A 110 ? 1.9739 1.2798 1.1918 -0.2893 0.1297 -0.0472 109 ARG A CG +848 C CD . ARG A 110 ? 1.5860 0.8912 0.8024 -0.2906 0.1288 -0.0471 109 ARG A CD +849 N NE . ARG A 110 ? 1.9629 1.2668 1.1790 -0.2911 0.1310 -0.0479 109 ARG A NE +850 C CZ . ARG A 110 ? 2.0928 1.3968 1.3101 -0.2901 0.1314 -0.0478 109 ARG A CZ +851 N NH1 . ARG A 110 ? 2.1528 1.4581 1.3719 -0.2885 0.1296 -0.0470 109 ARG A NH1 +852 N NH2 . ARG A 110 ? 1.9682 1.2709 1.1851 -0.2906 0.1334 -0.0486 109 ARG A NH2 +853 N N . ALA A 111 ? 1.8753 1.1837 1.0986 -0.2847 0.1304 -0.0469 110 ALA A N +854 C CA . ALA A 111 ? 1.6410 0.9500 0.8665 -0.2829 0.1309 -0.0468 110 ALA A CA +855 C C . ALA A 111 ? 1.8480 1.1558 1.0735 -0.2832 0.1331 -0.0476 110 ALA A C +856 O O . ALA A 111 ? 1.6395 0.9460 0.8636 -0.2845 0.1350 -0.0483 110 ALA A O +857 C CB . ALA A 111 ? 1.7967 1.1065 1.0240 -0.2815 0.1315 -0.0468 110 ALA A CB +858 N N . GLU A 112 ? 1.6457 0.9539 0.8726 -0.2820 0.1328 -0.0473 111 GLU A N +859 C CA . GLU A 112 ? 1.8013 1.1084 1.0285 -0.2819 0.1350 -0.0480 111 GLU A CA +860 C C . GLU A 112 ? 2.0221 1.3299 1.2517 -0.2800 0.1359 -0.0481 111 GLU A C +861 O O . GLU A 112 ? 2.0253 1.3344 1.2565 -0.2785 0.1343 -0.0474 111 GLU A O +862 C CB . GLU A 112 ? 1.9884 1.2951 1.2152 -0.2821 0.1342 -0.0478 111 GLU A CB +863 C CG . GLU A 112 ? 2.5297 1.8355 1.7540 -0.2842 0.1338 -0.0479 111 GLU A CG +864 C CD . GLU A 112 ? 2.5914 1.8969 1.8153 -0.2845 0.1328 -0.0476 111 GLU A CD +865 O OE1 . GLU A 112 ? 2.1581 1.4641 1.3836 -0.2831 0.1324 -0.0473 111 GLU A OE1 +866 O OE2 . GLU A 112 ? 2.5213 1.8259 1.7432 -0.2862 0.1325 -0.0476 111 GLU A OE2 +867 N N . VAL A 113 ? 1.8917 1.1987 1.1215 -0.2800 0.1383 -0.0489 112 VAL A N +868 C CA . VAL A 113 ? 1.7735 1.0810 1.0054 -0.2783 0.1394 -0.0490 112 VAL A CA +869 C C . VAL A 113 ? 1.8428 1.1491 1.0750 -0.2782 0.1413 -0.0496 112 VAL A C +870 O O . VAL A 113 ? 1.7144 1.0193 0.9453 -0.2794 0.1433 -0.0504 112 VAL A O +871 C CB . VAL A 113 ? 1.4234 0.7308 0.6556 -0.2782 0.1407 -0.0494 112 VAL A CB +872 C CG1 . VAL A 113 ? 1.8178 1.1261 1.0524 -0.2764 0.1412 -0.0494 112 VAL A CG1 +873 C CG2 . VAL A 113 ? 1.9166 1.2247 1.1480 -0.2788 0.1391 -0.0489 112 VAL A CG2 +874 N N . LYS A 114 ? 1.5409 0.8479 0.7747 -0.2768 0.1408 -0.0493 113 LYS A N +875 C CA . LYS A 114 ? 1.7975 1.1034 1.0316 -0.2766 0.1425 -0.0498 113 LYS A CA +876 C C . LYS A 114 ? 1.9587 1.2656 1.1950 -0.2747 0.1420 -0.0494 113 LYS A C +877 O O . LYS A 114 ? 1.7159 1.0243 0.9536 -0.2735 0.1403 -0.0488 113 LYS A O +878 C CB . LYS A 114 ? 2.1266 1.4316 1.3590 -0.2778 0.1421 -0.0498 113 LYS A CB +879 C CG . LYS A 114 ? 2.1366 1.4426 1.3689 -0.2777 0.1393 -0.0489 113 LYS A CG +880 C CD . LYS A 114 ? 1.9436 1.2485 1.1741 -0.2790 0.1390 -0.0489 113 LYS A CD +881 C CE . LYS A 114 ? 2.1698 1.4758 1.4006 -0.2787 0.1363 -0.0480 113 LYS A CE +882 N NZ . LYS A 114 ? 2.0056 1.3125 1.2357 -0.2792 0.1342 -0.0474 113 LYS A NZ +883 N N . PHE A 115 ? 1.7265 1.0325 0.9633 -0.2743 0.1436 -0.0499 114 PHE A N +884 C CA . PHE A 115 ? 1.7959 1.1036 1.0372 -0.2722 0.1430 -0.0496 114 PHE A CA +885 C C . PHE A 115 ? 1.7981 1.1065 1.0404 -0.2718 0.1411 -0.0489 114 PHE A C +886 O O . PHE A 115 ? 1.8723 1.1801 1.1143 -0.2727 0.1412 -0.0490 114 PHE A O +887 C CB . PHE A 115 ? 2.1491 1.4569 1.3941 -0.2714 0.1451 -0.0503 114 PHE A CB +888 C CG . PHE A 115 ? 2.1834 1.4916 1.4297 -0.2706 0.1463 -0.0506 114 PHE A CG +889 C CD1 . PHE A 115 ? 1.9459 1.2557 1.1955 -0.2687 0.1456 -0.0503 114 PHE A CD1 +890 C CD2 . PHE A 115 ? 1.8714 1.1783 1.1158 -0.2717 0.1481 -0.0513 114 PHE A CD2 +891 C CE1 . PHE A 115 ? 1.7888 1.0990 1.0399 -0.2679 0.1466 -0.0506 114 PHE A CE1 +892 C CE2 . PHE A 115 ? 1.5971 0.9044 0.8430 -0.2709 0.1491 -0.0517 114 PHE A CE2 +893 C CZ . PHE A 115 ? 1.7996 1.1086 1.0489 -0.2690 0.1484 -0.0513 114 PHE A CZ +894 N N . GLU A 116 ? 1.6982 1.0081 0.9421 -0.2705 0.1394 -0.0482 115 GLU A N +895 C CA . GLU A 116 ? 1.6370 0.9478 0.8826 -0.2698 0.1377 -0.0475 115 GLU A CA +896 C C . GLU A 116 ? 1.7209 1.0332 0.9710 -0.2677 0.1377 -0.0473 115 GLU A C +897 O O . GLU A 116 ? 1.6657 0.9793 0.9167 -0.2666 0.1363 -0.0468 115 GLU A O +898 C CB . GLU A 116 ? 1.8606 1.1717 1.1034 -0.2702 0.1353 -0.0467 115 GLU A CB +899 C CG . GLU A 116 ? 2.0120 1.3216 1.2505 -0.2723 0.1350 -0.0468 115 GLU A CG +900 C CD . GLU A 116 ? 2.4789 1.7898 1.7171 -0.2723 0.1322 -0.0459 115 GLU A CD +901 O OE1 . GLU A 116 ? 2.4057 1.7179 1.6455 -0.2710 0.1307 -0.0453 115 GLU A OE1 +902 O OE2 . GLU A 116 ? 2.2926 1.6031 1.5291 -0.2737 0.1314 -0.0458 115 GLU A OE2 +903 N N . GLY A 117 ? 1.8449 1.1572 1.0981 -0.2673 0.1393 -0.0478 116 GLY A N +904 C CA . GLY A 117 ? 1.6975 1.0111 0.9552 -0.2654 0.1396 -0.0479 116 GLY A CA +905 C C . GLY A 117 ? 2.0131 1.3267 1.2714 -0.2649 0.1411 -0.0484 116 GLY A C +906 O O . GLY A 117 ? 1.7007 1.0131 0.9576 -0.2659 0.1429 -0.0491 116 GLY A O +907 N N . ASP A 118 ? 2.2987 1.6137 1.5590 -0.2634 0.1404 -0.0481 117 ASP A N +908 C CA . ASP A 118 ? 2.1993 1.5145 1.4606 -0.2628 0.1416 -0.0486 117 ASP A CA +909 C C . ASP A 118 ? 2.0358 1.3505 1.2932 -0.2637 0.1412 -0.0484 117 ASP A C +910 O O . ASP A 118 ? 1.9297 1.2445 1.1874 -0.2634 0.1422 -0.0488 117 ASP A O +911 C CB . ASP A 118 ? 2.1739 1.4909 1.4393 -0.2607 0.1412 -0.0483 117 ASP A CB +912 C CG . ASP A 118 ? 2.4878 1.8060 1.7525 -0.2601 0.1390 -0.0474 117 ASP A CG +913 O OD1 . ASP A 118 ? 2.3343 1.6523 1.5970 -0.2607 0.1374 -0.0468 117 ASP A OD1 +914 O OD2 . ASP A 118 ? 2.2401 1.5593 1.5064 -0.2589 0.1387 -0.0473 117 ASP A OD2 +915 N N . THR A 119 ? 1.9494 1.2636 1.2032 -0.2648 0.1397 -0.0479 118 THR A N +916 C CA . THR A 119 ? 1.8669 1.1807 1.1170 -0.2656 0.1391 -0.0477 118 THR A CA +917 C C . THR A 119 ? 1.8213 1.1332 1.0671 -0.2677 0.1399 -0.0481 118 THR A C +918 O O . THR A 119 ? 1.7927 1.1037 1.0375 -0.2688 0.1401 -0.0482 118 THR A O +919 C CB . THR A 119 ? 1.5891 0.9037 0.8380 -0.2652 0.1366 -0.0467 118 THR A CB +920 O OG1 . THR A 119 ? 1.7318 1.0481 0.9845 -0.2633 0.1360 -0.0464 118 THR A OG1 +921 C CG2 . THR A 119 ? 1.5624 0.8776 0.8100 -0.2655 0.1355 -0.0464 118 THR A CG2 +922 N N . LEU A 120 ? 1.7743 1.0861 1.0191 -0.2680 0.1403 -0.0482 119 LEU A N +923 C CA . LEU A 120 ? 1.4166 0.7277 0.6595 -0.2696 0.1405 -0.0484 119 LEU A CA +924 C C . LEU A 120 ? 1.8264 1.1388 1.0689 -0.2698 0.1378 -0.0476 119 LEU A C +925 O O . LEU A 120 ? 1.4958 0.8095 0.7394 -0.2689 0.1366 -0.0471 119 LEU A O +926 C CB . LEU A 120 ? 1.3309 0.6416 0.5739 -0.2697 0.1422 -0.0490 119 LEU A CB +927 C CG . LEU A 120 ? 1.2629 0.5727 0.5040 -0.2713 0.1431 -0.0494 119 LEU A CG +928 C CD1 . LEU A 120 ? 2.2991 1.6079 1.5404 -0.2715 0.1457 -0.0503 119 LEU A CD1 +929 C CD2 . LEU A 120 ? 1.4327 0.7436 0.6735 -0.2715 0.1412 -0.0488 119 LEU A CD2 +930 N N . VAL A 121 ? 1.6955 1.0074 0.9363 -0.2710 0.1369 -0.0474 120 VAL A N +931 C CA . VAL A 121 ? 1.5181 0.8310 0.7584 -0.2713 0.1343 -0.0466 120 VAL A CA +932 C C . VAL A 121 ? 1.8331 1.1454 1.0714 -0.2729 0.1342 -0.0467 120 VAL A C +933 O O . VAL A 121 ? 1.6259 0.9368 0.8626 -0.2742 0.1358 -0.0474 120 VAL A O +934 C CB . VAL A 121 ? 1.7670 1.0801 1.0070 -0.2713 0.1327 -0.0461 120 VAL A CB +935 C CG1 . VAL A 121 ? 1.4474 0.7610 0.6893 -0.2697 0.1328 -0.0459 120 VAL A CG1 +936 C CG2 . VAL A 121 ? 2.0656 1.3770 1.3036 -0.2728 0.1337 -0.0466 120 VAL A CG2 +937 N N . ASN A 122 ? 1.6587 0.9721 0.8970 -0.2728 0.1325 -0.0462 121 ASN A N +938 C CA . ASN A 122 ? 1.6997 1.0127 0.9360 -0.2743 0.1320 -0.0462 121 ASN A CA +939 C C . ASN A 122 ? 1.8894 1.2030 1.1249 -0.2747 0.1293 -0.0454 121 ASN A C +940 O O . ASN A 122 ? 1.6365 0.9515 0.8732 -0.2737 0.1274 -0.0446 121 ASN A O +941 C CB . ASN A 122 ? 1.2806 0.5941 0.5173 -0.2740 0.1322 -0.0462 121 ASN A CB +942 C CG . ASN A 122 ? 1.5039 0.8165 0.7384 -0.2757 0.1324 -0.0464 121 ASN A CG +943 O OD1 . ASN A 122 ? 2.0871 1.3986 1.3200 -0.2771 0.1330 -0.0468 121 ASN A OD1 +944 N ND2 . ASN A 122 ? 1.6503 0.9635 0.8850 -0.2756 0.1319 -0.0462 121 ASN A ND2 +945 N N . ARG A 123 ? 1.6748 0.9875 0.9084 -0.2763 0.1292 -0.0455 122 ARG A N +946 C CA . ARG A 123 ? 1.6788 0.9919 0.9115 -0.2769 0.1268 -0.0448 122 ARG A CA +947 C C . ARG A 123 ? 1.7799 1.0926 1.0105 -0.2785 0.1261 -0.0448 122 ARG A C +948 O O . ARG A 123 ? 1.6088 0.9201 0.8376 -0.2801 0.1273 -0.0453 122 ARG A O +949 C CB . ARG A 123 ? 1.7085 1.0209 0.9407 -0.2773 0.1267 -0.0448 122 ARG A CB +950 C CG . ARG A 123 ? 1.6470 0.9603 0.8812 -0.2756 0.1260 -0.0444 122 ARG A CG +951 C CD . ARG A 123 ? 1.8224 1.1352 1.0559 -0.2762 0.1255 -0.0443 122 ARG A CD +952 N NE . ARG A 123 ? 2.0463 1.3590 1.2812 -0.2750 0.1264 -0.0444 122 ARG A NE +953 C CZ . ARG A 123 ? 2.1825 1.4964 1.4193 -0.2734 0.1253 -0.0439 122 ARG A CZ +954 N NH1 . ARG A 123 ? 1.8605 1.1758 1.0980 -0.2728 0.1232 -0.0431 122 ARG A NH1 +955 N NH2 . ARG A 123 ? 2.0434 1.3570 1.2813 -0.2725 0.1263 -0.0441 122 ARG A NH2 +956 N N . ILE A 124 ? 1.8077 1.1214 1.0385 -0.2782 0.1240 -0.0441 123 ILE A N +957 C CA . ILE A 124 ? 1.7374 1.0510 0.9665 -0.2795 0.1234 -0.0440 123 ILE A CA +958 C C . ILE A 124 ? 1.8201 1.1340 1.0480 -0.2803 0.1208 -0.0433 123 ILE A C +959 O O . ILE A 124 ? 1.4892 0.8043 0.7183 -0.2793 0.1189 -0.0425 123 ILE A O +960 C CB . ILE A 124 ? 1.9356 1.2500 1.1658 -0.2785 0.1235 -0.0439 123 ILE A CB +961 C CG1 . ILE A 124 ? 1.7502 1.0647 0.9823 -0.2772 0.1254 -0.0444 123 ILE A CG1 +962 C CG2 . ILE A 124 ? 1.4573 0.7709 0.6856 -0.2800 0.1239 -0.0442 123 ILE A CG2 +963 C CD1 . ILE A 124 ? 1.8652 1.1806 1.0986 -0.2760 0.1253 -0.0441 123 ILE A CD1 +964 N N . GLU A 125 ? 1.8404 1.1533 1.0661 -0.2822 0.1209 -0.0435 124 GLU A N +965 C CA . GLU A 125 ? 1.6819 0.9949 0.9061 -0.2832 0.1186 -0.0429 124 GLU A CA +966 C C . GLU A 125 ? 1.7426 1.0555 0.9657 -0.2841 0.1186 -0.0430 124 GLU A C +967 O O . GLU A 125 ? 1.8158 1.1276 1.0376 -0.2852 0.1205 -0.0437 124 GLU A O +968 C CB . GLU A 125 ? 1.7219 1.0339 0.9442 -0.2849 0.1184 -0.0430 124 GLU A CB +969 C CG . GLU A 125 ? 2.2087 1.5207 1.4319 -0.2843 0.1184 -0.0430 124 GLU A CG +970 C CD . GLU A 125 ? 2.5192 1.8299 1.7404 -0.2861 0.1185 -0.0432 124 GLU A CD +971 O OE1 . GLU A 125 ? 2.7138 2.0231 1.9335 -0.2874 0.1203 -0.0439 124 GLU A OE1 +972 O OE2 . GLU A 125 ? 2.3076 1.6186 1.5287 -0.2862 0.1166 -0.0426 124 GLU A OE2 +973 N N . LEU A 126 ? 1.6204 0.9343 0.8438 -0.2836 0.1166 -0.0423 125 LEU A N +974 C CA . LEU A 126 ? 1.8069 1.1207 1.0291 -0.2844 0.1164 -0.0423 125 LEU A CA +975 C C . LEU A 126 ? 1.8279 1.1419 1.0487 -0.2854 0.1139 -0.0416 125 LEU A C +976 O O . LEU A 126 ? 1.7706 1.0854 0.9921 -0.2848 0.1119 -0.0409 125 LEU A O +977 C CB . LEU A 126 ? 1.5266 0.8413 0.7507 -0.2827 0.1167 -0.0421 125 LEU A CB +978 C CG . LEU A 126 ? 1.4432 0.7583 0.6667 -0.2829 0.1158 -0.0418 125 LEU A CG +979 C CD1 . LEU A 126 ? 1.6032 0.9185 0.8280 -0.2819 0.1174 -0.0422 125 LEU A CD1 +980 C CD2 . LEU A 126 ? 1.7967 1.1129 1.0208 -0.2822 0.1130 -0.0409 125 LEU A CD2 +981 N N . LYS A 127 ? 1.8539 1.1671 1.0727 -0.2870 0.1140 -0.0418 126 LYS A N +982 C CA . LYS A 127 ? 1.5627 0.8757 0.7797 -0.2883 0.1118 -0.0413 126 LYS A CA +983 C C . LYS A 127 ? 1.6742 0.9870 0.8899 -0.2891 0.1115 -0.0413 126 LYS A C +984 O O . LYS A 127 ? 1.9351 1.2467 1.1488 -0.2908 0.1126 -0.0418 126 LYS A O +985 C CB . LYS A 127 ? 1.7510 1.0629 0.9661 -0.2901 0.1119 -0.0416 126 LYS A CB +986 C CG . LYS A 127 ? 2.0865 1.3981 1.2997 -0.2916 0.1097 -0.0410 126 LYS A CG +987 C CD . LYS A 127 ? 2.2597 1.5706 1.4717 -0.2930 0.1092 -0.0410 126 LYS A CD +988 C CE . LYS A 127 ? 2.1076 1.4184 1.3180 -0.2942 0.1067 -0.0404 126 LYS A CE +989 N NZ . LYS A 127 ? 1.9185 1.2307 1.1302 -0.2928 0.1048 -0.0396 126 LYS A NZ +990 N N . GLY A 128 ? 1.9038 1.2176 1.1204 -0.2881 0.1099 -0.0406 127 GLY A N +991 C CA . GLY A 128 ? 1.8396 1.1533 1.0551 -0.2887 0.1094 -0.0405 127 GLY A CA +992 C C . GLY A 128 ? 1.9903 1.3037 1.2038 -0.2902 0.1072 -0.0399 127 GLY A C +993 O O . GLY A 128 ? 2.0701 1.3841 1.2839 -0.2899 0.1051 -0.0393 127 GLY A O +994 N N . ILE A 129 ? 2.1510 1.4635 1.3624 -0.2917 0.1075 -0.0402 128 ILE A N +995 C CA . ILE A 129 ? 1.8751 1.1872 1.0845 -0.2933 0.1055 -0.0398 128 ILE A CA +996 C C . ILE A 129 ? 1.6717 0.9834 0.8798 -0.2939 0.1055 -0.0398 128 ILE A C +997 O O . ILE A 129 ? 1.9466 1.2580 1.1550 -0.2936 0.1075 -0.0404 128 ILE A O +998 C CB . ILE A 129 ? 1.7017 1.0125 0.9088 -0.2955 0.1059 -0.0403 128 ILE A CB +999 C CG1 . ILE A 129 ? 2.3167 1.6278 1.5247 -0.2951 0.1056 -0.0401 128 ILE A CG1 +1000 C CG2 . ILE A 129 ? 2.6041 1.9142 1.8088 -0.2974 0.1041 -0.0399 128 ILE A CG2 +1001 C CD1 . ILE A 129 ? 2.2448 1.5553 1.4534 -0.2949 0.1081 -0.0409 128 ILE A CD1 +1002 N N . ASP A 130 ? 2.0771 1.3888 1.2840 -0.2947 0.1033 -0.0392 129 ASP A N +1003 C CA . ASP A 130 ? 2.1135 1.4246 1.3187 -0.2956 0.1032 -0.0392 129 ASP A CA +1004 C C . ASP A 130 ? 1.5278 0.8398 0.7346 -0.2939 0.1033 -0.0390 129 ASP A C +1005 O O . ASP A 130 ? 1.4973 0.8087 0.7030 -0.2945 0.1039 -0.0391 129 ASP A O +1006 C CB . ASP A 130 ? 1.9544 1.2641 1.1576 -0.2974 0.1052 -0.0402 129 ASP A CB +1007 C CG . ASP A 130 ? 2.1302 1.4390 1.3316 -0.2994 0.1050 -0.0405 129 ASP A CG +1008 O OD1 . ASP A 130 ? 1.8508 1.1596 1.0512 -0.3003 0.1028 -0.0399 129 ASP A OD1 +1009 O OD2 . ASP A 130 ? 2.1792 1.4872 1.3801 -0.3002 0.1071 -0.0413 129 ASP A OD2 +1010 N N . PHE A 131 ? 1.4685 0.7818 0.6777 -0.2919 0.1026 -0.0385 130 PHE A N +1011 C CA . PHE A 131 ? 1.8943 1.2084 1.1049 -0.2904 0.1025 -0.0381 130 PHE A CA +1012 C C . PHE A 131 ? 1.5290 0.8433 0.7387 -0.2906 0.1000 -0.0373 130 PHE A C +1013 O O . PHE A 131 ? 1.8146 1.1288 1.0233 -0.2915 0.0982 -0.0369 130 PHE A O +1014 C CB . PHE A 131 ? 1.7400 1.0553 0.9536 -0.2882 0.1031 -0.0380 130 PHE A CB +1015 C CG . PHE A 131 ? 1.6503 0.9651 0.8646 -0.2879 0.1058 -0.0389 130 PHE A CG +1016 C CD1 . PHE A 131 ? 1.8316 1.1460 1.0457 -0.2886 0.1066 -0.0393 130 PHE A CD1 +1017 C CD2 . PHE A 131 ? 1.6682 0.9831 0.8835 -0.2871 0.1076 -0.0392 130 PHE A CD2 +1018 C CE1 . PHE A 131 ? 1.3691 0.6831 0.5838 -0.2884 0.1091 -0.0401 130 PHE A CE1 +1019 C CE2 . PHE A 131 ? 1.4701 0.7845 0.6860 -0.2869 0.1101 -0.0400 130 PHE A CE2 +1020 C CZ . PHE A 131 ? 1.9059 1.2198 1.1215 -0.2875 0.1109 -0.0405 130 PHE A CZ +1021 N N . LYS A 132 ? 1.5045 0.8190 0.7146 -0.2899 0.1000 -0.0371 131 LYS A N +1022 C CA . LYS A 132 ? 1.6633 0.9781 0.8727 -0.2900 0.0978 -0.0363 131 LYS A CA +1023 C C . LYS A 132 ? 1.6854 1.0016 0.8972 -0.2880 0.0964 -0.0356 131 LYS A C +1024 O O . LYS A 132 ? 2.5369 1.8536 1.7503 -0.2866 0.0974 -0.0356 131 LYS A O +1025 C CB . LYS A 132 ? 1.3651 0.6792 0.5734 -0.2905 0.0986 -0.0365 131 LYS A CB +1026 C CG . LYS A 132 ? 1.5921 0.9049 0.7984 -0.2923 0.1005 -0.0373 131 LYS A CG +1027 C CD . LYS A 132 ? 1.7015 1.0137 0.9070 -0.2925 0.1011 -0.0374 131 LYS A CD +1028 C CE . LYS A 132 ? 1.9962 1.3070 1.1991 -0.2946 0.1024 -0.0380 131 LYS A CE +1029 N NZ . LYS A 132 ? 2.0040 1.3143 1.2064 -0.2946 0.1034 -0.0381 131 LYS A NZ +1030 N N . GLU A 133 ? 1.8301 1.1469 1.0421 -0.2879 0.0941 -0.0349 132 GLU A N +1031 C CA . GLU A 133 ? 2.1931 1.5112 1.4072 -0.2859 0.0927 -0.0342 132 GLU A CA +1032 C C . GLU A 133 ? 1.9967 1.3153 1.2119 -0.2847 0.0927 -0.0339 132 GLU A C +1033 O O . GLU A 133 ? 1.8458 1.1656 1.0631 -0.2829 0.0921 -0.0335 132 GLU A O +1034 C CB . GLU A 133 ? 1.8327 1.1511 1.0462 -0.2864 0.0899 -0.0334 132 GLU A CB +1035 C CG . GLU A 133 ? 3.1864 2.5048 2.3999 -0.2869 0.0896 -0.0335 132 GLU A CG +1036 C CD . GLU A 133 ? 2.9258 2.2455 2.1420 -0.2850 0.0893 -0.0332 132 GLU A CD +1037 O OE1 . GLU A 133 ? 2.8301 2.1508 2.0479 -0.2835 0.0882 -0.0326 132 GLU A OE1 +1038 O OE2 . GLU A 133 ? 2.3470 1.6667 1.5637 -0.2851 0.0903 -0.0336 132 GLU A OE2 +1039 N N . ASP A 134 ? 1.7676 1.0853 0.9811 -0.2856 0.0934 -0.0341 133 ASP A N +1040 C CA . ASP A 134 ? 1.8038 1.1218 1.0182 -0.2846 0.0935 -0.0339 133 ASP A CA +1041 C C . ASP A 134 ? 2.0640 1.3815 1.2788 -0.2843 0.0963 -0.0346 133 ASP A C +1042 O O . ASP A 134 ? 2.1153 1.4328 1.3306 -0.2837 0.0967 -0.0345 133 ASP A O +1043 C CB . ASP A 134 ? 2.5718 1.8891 1.7840 -0.2858 0.0920 -0.0334 133 ASP A CB +1044 C CG . ASP A 134 ? 2.8952 2.2110 2.1046 -0.2880 0.0925 -0.0339 133 ASP A CG +1045 O OD1 . ASP A 134 ? 2.8769 2.1925 2.0859 -0.2888 0.0929 -0.0343 133 ASP A OD1 +1046 O OD2 . ASP A 134 ? 3.0265 2.3414 2.2341 -0.2890 0.0926 -0.0340 133 ASP A OD2 +1047 N N . GLY A 135 ? 2.2638 1.5809 1.4784 -0.2850 0.0981 -0.0354 134 GLY A N +1048 C CA . GLY A 135 ? 2.2047 1.5212 1.4195 -0.2850 0.1007 -0.0361 134 GLY A CA +1049 C C . GLY A 135 ? 2.1991 1.5163 1.4164 -0.2831 0.1020 -0.0362 134 GLY A C +1050 O O . GLY A 135 ? 2.0224 1.3406 1.2413 -0.2816 0.1007 -0.0356 134 GLY A O +1051 N N . ASN A 136 ? 2.1707 1.4874 1.3883 -0.2832 0.1045 -0.0370 135 ASN A N +1052 C CA . ASN A 136 ? 1.6393 0.9566 0.8593 -0.2815 0.1060 -0.0372 135 ASN A CA +1053 C C . ASN A 136 ? 1.9048 1.2230 1.1268 -0.2803 0.1060 -0.0373 135 ASN A C +1054 O O . ASN A 136 ? 1.7209 1.0402 0.9451 -0.2786 0.1057 -0.0369 135 ASN A O +1055 C CB . ASN A 136 ? 1.7825 1.0987 1.0020 -0.2821 0.1086 -0.0380 135 ASN A CB +1056 C CG . ASN A 136 ? 1.8472 1.1626 1.0654 -0.2827 0.1087 -0.0379 135 ASN A CG +1057 O OD1 . ASN A 136 ? 1.4079 0.7239 0.6265 -0.2820 0.1071 -0.0372 135 ASN A OD1 +1058 N ND2 . ASN A 136 ? 1.4576 0.7718 0.6744 -0.2839 0.1106 -0.0386 135 ASN A ND2 +1059 N N . ILE A 137 ? 1.6890 1.0068 0.9102 -0.2813 0.1066 -0.0377 136 ILE A N +1060 C CA . ILE A 137 ? 1.9134 1.2320 1.1361 -0.2804 0.1064 -0.0377 136 ILE A CA +1061 C C . ILE A 137 ? 2.0528 1.3725 1.2763 -0.2796 0.1038 -0.0368 136 ILE A C +1062 O O . ILE A 137 ? 1.6527 0.9734 0.8782 -0.2780 0.1032 -0.0364 136 ILE A O +1063 C CB . ILE A 137 ? 1.6442 0.9619 0.8655 -0.2819 0.1072 -0.0382 136 ILE A CB +1064 C CG1 . ILE A 137 ? 1.3108 0.6274 0.5315 -0.2825 0.1100 -0.0392 136 ILE A CG1 +1065 C CG2 . ILE A 137 ? 1.1738 0.4922 0.3965 -0.2811 0.1068 -0.0381 136 ILE A CG2 +1066 C CD1 . ILE A 137 ? 1.7319 1.0474 0.9506 -0.2840 0.1107 -0.0394 136 ILE A CD1 +1067 N N . LEU A 138 ? 1.8527 1.1721 1.0745 -0.2809 0.1022 -0.0365 137 LEU A N +1068 C CA . LEU A 138 ? 1.9162 1.2365 1.1386 -0.2803 0.0998 -0.0358 137 LEU A CA +1069 C C . LEU A 138 ? 1.9600 1.2812 1.1833 -0.2793 0.0981 -0.0350 137 LEU A C +1070 O O . LEU A 138 ? 1.5701 0.8921 0.7943 -0.2784 0.0963 -0.0344 137 LEU A O +1071 C CB . LEU A 138 ? 1.6047 0.9243 0.8249 -0.2821 0.0985 -0.0356 137 LEU A CB +1072 C CG . LEU A 138 ? 1.8012 1.1203 1.0210 -0.2829 0.0996 -0.0362 137 LEU A CG +1073 C CD1 . LEU A 138 ? 2.0918 1.4102 1.3095 -0.2846 0.0981 -0.0360 137 LEU A CD1 +1074 C CD2 . LEU A 138 ? 1.5053 0.8254 0.7275 -0.2813 0.0998 -0.0361 137 LEU A CD2 +1075 N N . GLY A 139 ? 1.4549 0.7756 0.6777 -0.2794 0.0988 -0.0351 138 GLY A N +1076 C CA . GLY A 139 ? 1.5931 0.9145 0.8167 -0.2783 0.0975 -0.0344 138 GLY A CA +1077 C C . GLY A 139 ? 1.8539 1.1762 1.0802 -0.2764 0.0986 -0.0345 138 GLY A C +1078 O O . GLY A 139 ? 1.8525 1.1755 1.0798 -0.2752 0.0975 -0.0340 138 GLY A O +1079 N N . HIS A 140 ? 1.9542 1.2763 1.1814 -0.2761 0.1008 -0.0352 139 HIS A N +1080 C CA . HIS A 140 ? 1.7719 1.0947 1.0014 -0.2744 0.1021 -0.0355 139 HIS A CA +1081 C C . HIS A 140 ? 1.6235 0.9461 0.8532 -0.2741 0.1027 -0.0354 139 HIS A C +1082 O O . HIS A 140 ? 1.7208 1.0442 0.9519 -0.2727 0.1018 -0.0350 139 HIS A O +1083 C CB . HIS A 140 ? 1.7539 1.0781 0.9855 -0.2728 0.1007 -0.0349 139 HIS A CB +1084 C CG . HIS A 140 ? 1.8122 1.1367 1.0443 -0.2729 0.1008 -0.0351 139 HIS A CG +1085 N ND1 . HIS A 140 ? 2.0667 1.3912 1.2999 -0.2724 0.1027 -0.0357 139 HIS A ND1 +1086 C CD2 . HIS A 140 ? 2.0144 1.3391 1.2459 -0.2733 0.0992 -0.0348 139 HIS A CD2 +1087 C CE1 . HIS A 140 ? 1.8817 1.2064 1.1150 -0.2726 0.1023 -0.0357 139 HIS A CE1 +1088 N NE2 . HIS A 140 ? 1.7955 1.1202 1.0277 -0.2732 0.1002 -0.0351 139 HIS A NE2 +1089 N N . LYS A 141 ? 1.7650 1.0863 0.9931 -0.2753 0.1042 -0.0360 140 LYS A N +1090 C CA . LYS A 141 ? 1.8309 1.1517 1.0588 -0.2751 0.1050 -0.0360 140 LYS A CA +1091 C C . LYS A 141 ? 2.0077 1.3281 1.2365 -0.2749 0.1077 -0.0369 140 LYS A C +1092 O O . LYS A 141 ? 1.6674 0.9872 0.8961 -0.2748 0.1087 -0.0371 140 LYS A O +1093 C CB . LYS A 141 ? 1.8164 1.1362 1.0417 -0.2768 0.1044 -0.0359 140 LYS A CB +1094 C CG . LYS A 141 ? 1.8526 1.1728 1.0771 -0.2770 0.1016 -0.0350 140 LYS A CG +1095 C CD . LYS A 141 ? 2.1643 1.4834 1.3859 -0.2789 0.1010 -0.0350 140 LYS A CD +1096 C CE . LYS A 141 ? 2.0610 1.3804 1.2817 -0.2791 0.0982 -0.0341 140 LYS A CE +1097 N NZ . LYS A 141 ? 2.2868 1.6052 1.5048 -0.2811 0.0974 -0.0341 140 LYS A NZ +1098 N N . LEU A 142 ? 1.7609 1.0813 0.9904 -0.2748 0.1089 -0.0374 141 LEU A N +1099 C CA . LEU A 142 ? 1.5882 0.9082 0.8187 -0.2744 0.1115 -0.0382 141 LEU A CA +1100 C C . LEU A 142 ? 1.6988 1.0199 0.9319 -0.2725 0.1116 -0.0380 141 LEU A C +1101 O O . LEU A 142 ? 1.4022 0.7245 0.6367 -0.2713 0.1100 -0.0374 141 LEU A O +1102 C CB . LEU A 142 ? 1.6767 0.9965 0.9072 -0.2748 0.1126 -0.0387 141 LEU A CB +1103 C CG . LEU A 142 ? 1.2642 0.5828 0.4921 -0.2768 0.1129 -0.0390 141 LEU A CG +1104 C CD1 . LEU A 142 ? 1.4489 0.7673 0.6769 -0.2771 0.1139 -0.0395 141 LEU A CD1 +1105 C CD2 . LEU A 142 ? 1.5938 0.9111 0.8204 -0.2778 0.1147 -0.0396 141 LEU A CD2 +1106 N N . GLU A 143 ? 1.5474 0.8680 0.7811 -0.2722 0.1136 -0.0386 142 GLU A N +1107 C CA . GLU A 143 ? 1.7054 1.0267 0.9414 -0.2705 0.1142 -0.0386 142 GLU A CA +1108 C C . GLU A 143 ? 1.7332 1.0548 0.9707 -0.2698 0.1155 -0.0391 142 GLU A C +1109 O O . GLU A 143 ? 1.6341 0.9549 0.8708 -0.2707 0.1170 -0.0397 142 GLU A O +1110 C CB . GLU A 143 ? 1.7075 1.0279 0.9433 -0.2707 0.1158 -0.0390 142 GLU A CB +1111 C CG . GLU A 143 ? 1.7382 1.0587 0.9735 -0.2706 0.1143 -0.0384 142 GLU A CG +1112 C CD . GLU A 143 ? 2.0465 1.3661 1.2819 -0.2705 0.1159 -0.0389 142 GLU A CD +1113 O OE1 . GLU A 143 ? 2.0597 1.3786 1.2953 -0.2709 0.1181 -0.0397 142 GLU A OE1 +1114 O OE2 . GLU A 143 ? 1.7720 1.0917 1.0075 -0.2701 0.1148 -0.0384 142 GLU A OE2 +1115 N N . TYR A 144 ? 1.4246 0.7474 0.6643 -0.2682 0.1150 -0.0388 143 TYR A N +1116 C CA . TYR A 144 ? 1.3761 0.6993 0.6175 -0.2674 0.1162 -0.0393 143 TYR A CA +1117 C C . TYR A 144 ? 1.5484 0.8709 0.7904 -0.2673 0.1189 -0.0401 143 TYR A C +1118 O O . TYR A 144 ? 1.4081 0.7311 0.6520 -0.2660 0.1196 -0.0403 143 TYR A O +1119 C CB . TYR A 144 ? 1.2169 0.5417 0.4605 -0.2657 0.1149 -0.0388 143 TYR A CB +1120 C CG . TYR A 144 ? 1.3192 0.6444 0.5639 -0.2652 0.1156 -0.0390 143 TYR A CG +1121 C CD1 . TYR A 144 ? 1.6202 0.9448 0.8637 -0.2663 0.1159 -0.0393 143 TYR A CD1 +1122 C CD2 . TYR A 144 ? 1.5287 0.8549 0.7757 -0.2636 0.1159 -0.0390 143 TYR A CD2 +1123 C CE1 . TYR A 144 ? 1.4365 0.7614 0.6809 -0.2658 0.1164 -0.0395 143 TYR A CE1 +1124 C CE2 . TYR A 144 ? 1.5559 0.8824 0.8039 -0.2632 0.1164 -0.0393 143 TYR A CE2 +1125 C CZ . TYR A 144 ? 1.6258 0.9516 0.8724 -0.2643 0.1167 -0.0395 143 TYR A CZ +1126 O OH . TYR A 144 ? 1.4984 0.8244 0.7459 -0.2639 0.1173 -0.0397 143 TYR A OH +1127 N N . ASN A 145 ? 1.2319 0.5530 0.4722 -0.2687 0.1204 -0.0407 144 ASN A N +1128 C CA . ASN A 145 ? 1.2832 0.6035 0.5239 -0.2687 0.1230 -0.0416 144 ASN A CA +1129 C C . ASN A 145 ? 1.2985 0.6175 0.5375 -0.2702 0.1246 -0.0423 144 ASN A C +1130 O O . ASN A 145 ? 1.5413 0.8601 0.7790 -0.2711 0.1238 -0.0421 144 ASN A O +1131 C CB . ASN A 145 ? 1.0761 0.3960 0.3169 -0.2686 0.1234 -0.0416 144 ASN A CB +1132 C CG . ASN A 145 ? 1.8483 1.1673 1.0867 -0.2700 0.1227 -0.0414 144 ASN A CG +1133 O OD1 . ASN A 145 ? 1.3587 0.6767 0.5952 -0.2714 0.1232 -0.0417 144 ASN A OD1 +1134 N ND2 . ASN A 145 ? 1.6738 0.9930 0.9123 -0.2696 0.1217 -0.0410 144 ASN A ND2 +1135 N N . TYR A 146 ? 1.3755 0.6935 0.6145 -0.2705 0.1269 -0.0431 145 TYR A N +1136 C CA . TYR A 146 ? 1.7138 1.0304 0.9514 -0.2718 0.1287 -0.0438 145 TYR A CA +1137 C C . TYR A 146 ? 1.4540 0.7694 0.6912 -0.2723 0.1310 -0.0446 145 TYR A C +1138 O O . TYR A 146 ? 1.5069 0.8225 0.7454 -0.2714 0.1313 -0.0446 145 TYR A O +1139 C CB . TYR A 146 ? 1.2867 0.6036 0.5253 -0.2714 0.1296 -0.0442 145 TYR A CB +1140 C CG . TYR A 146 ? 1.3347 0.6509 0.5715 -0.2728 0.1297 -0.0444 145 TYR A CG +1141 C CD1 . TYR A 146 ? 1.3495 0.6663 0.5856 -0.2731 0.1276 -0.0437 145 TYR A CD1 +1142 C CD2 . TYR A 146 ? 1.8141 1.1290 1.0501 -0.2738 0.1320 -0.0452 145 TYR A CD2 +1143 C CE1 . TYR A 146 ? 1.6332 0.9493 0.8676 -0.2744 0.1277 -0.0439 145 TYR A CE1 +1144 C CE2 . TYR A 146 ? 1.5286 0.8427 0.7628 -0.2751 0.1322 -0.0455 145 TYR A CE2 +1145 C CZ . TYR A 146 ? 1.4524 0.7671 0.6859 -0.2754 0.1300 -0.0448 145 TYR A CZ +1146 O OH . TYR A 146 ? 1.6100 0.9240 0.8418 -0.2768 0.1303 -0.0451 145 TYR A OH +1147 N N . ASN A 147 ? 1.7819 1.0960 1.0174 -0.2739 0.1324 -0.0452 146 ASN A N +1148 C CA . ASN A 147 ? 1.5911 0.9038 0.8259 -0.2746 0.1346 -0.0460 146 ASN A CA +1149 C C . ASN A 147 ? 1.6338 0.9456 0.8685 -0.2751 0.1369 -0.0469 146 ASN A C +1150 O O . ASN A 147 ? 1.6421 0.9543 0.8773 -0.2749 0.1367 -0.0468 146 ASN A O +1151 C CB . ASN A 147 ? 1.5782 0.8900 0.8106 -0.2762 0.1342 -0.0459 146 ASN A CB +1152 C CG . ASN A 147 ? 1.5591 0.8715 0.7913 -0.2758 0.1321 -0.0450 146 ASN A CG +1153 O OD1 . ASN A 147 ? 1.4915 0.8045 0.7253 -0.2746 0.1319 -0.0448 146 ASN A OD1 +1154 N ND2 . ASN A 147 ? 2.0034 1.3156 1.2337 -0.2769 0.1305 -0.0445 146 ASN A ND2 +1155 N N . SER A 148 ? 1.5341 0.8446 0.7682 -0.2759 0.1391 -0.0477 147 SER A N +1156 C CA . SER A 148 ? 1.3722 0.6817 0.6062 -0.2763 0.1415 -0.0486 147 SER A CA +1157 C C . SER A 148 ? 1.2497 0.5578 0.4812 -0.2783 0.1423 -0.0490 147 SER A C +1158 O O . SER A 148 ? 1.8884 1.1960 1.1184 -0.2793 0.1418 -0.0488 147 SER A O +1159 C CB . SER A 148 ? 1.4253 0.7342 0.6605 -0.2758 0.1436 -0.0493 147 SER A CB +1160 O OG . SER A 148 ? 1.6988 1.0089 0.9364 -0.2740 0.1431 -0.0491 147 SER A OG +1161 N N . HIS A 149 ? 1.4988 0.8064 0.7300 -0.2788 0.1435 -0.0495 148 HIS A N +1162 C CA . HIS A 149 ? 1.5612 0.8677 0.7901 -0.2807 0.1441 -0.0499 148 HIS A CA +1163 C C . HIS A 149 ? 1.5821 0.8874 0.8109 -0.2813 0.1468 -0.0509 148 HIS A C +1164 O O . HIS A 149 ? 1.5784 0.8839 0.8090 -0.2801 0.1479 -0.0513 148 HIS A O +1165 C CB . HIS A 149 ? 1.5502 0.8575 0.7782 -0.2811 0.1419 -0.0491 148 HIS A CB +1166 C CG . HIS A 149 ? 1.6531 0.9615 0.8812 -0.2805 0.1392 -0.0481 148 HIS A CG +1167 N ND1 . HIS A 149 ? 1.5966 0.9065 0.8263 -0.2791 0.1374 -0.0474 148 HIS A ND1 +1168 C CD2 . HIS A 149 ? 2.1134 1.4216 1.3402 -0.2813 0.1382 -0.0477 148 HIS A CD2 +1169 C CE1 . HIS A 149 ? 1.6700 0.9806 0.8994 -0.2789 0.1353 -0.0466 148 HIS A CE1 +1170 N NE2 . HIS A 149 ? 1.4407 0.7503 0.6683 -0.2802 0.1358 -0.0468 148 HIS A NE2 +1171 N N . ASN A 150 ? 1.5779 0.8819 0.8046 -0.2831 0.1479 -0.0514 149 ASN A N +1172 C CA . ASN A 150 ? 1.6840 0.9867 0.9103 -0.2838 0.1504 -0.0524 149 ASN A CA +1173 C C . ASN A 150 ? 1.5448 0.8473 0.7697 -0.2850 0.1501 -0.0524 149 ASN A C +1174 O O . ASN A 150 ? 1.7367 1.0390 0.9596 -0.2862 0.1489 -0.0521 149 ASN A O +1175 C CB . ASN A 150 ? 1.7813 1.0825 1.0066 -0.2849 0.1526 -0.0533 149 ASN A CB +1176 C CG . ASN A 150 ? 1.7112 1.0125 0.9379 -0.2839 0.1530 -0.0533 149 ASN A CG +1177 O OD1 . ASN A 150 ? 1.9964 1.2982 1.2251 -0.2824 0.1536 -0.0535 149 ASN A OD1 +1178 N ND2 . ASN A 150 ? 1.9976 1.2985 1.2231 -0.2846 0.1525 -0.0532 149 ASN A ND2 +1179 N N . VAL A 151 ? 1.7578 1.0602 0.9834 -0.2846 0.1510 -0.0528 150 VAL A N +1180 C CA . VAL A 151 ? 1.4961 0.7986 0.7207 -0.2854 0.1502 -0.0527 150 VAL A CA +1181 C C . VAL A 151 ? 1.8720 1.1728 1.0950 -0.2870 0.1525 -0.0536 150 VAL A C +1182 O O . VAL A 151 ? 1.9108 1.2113 1.1345 -0.2867 0.1539 -0.0542 150 VAL A O +1183 C CB . VAL A 151 ? 1.7187 1.0223 0.9451 -0.2837 0.1493 -0.0523 150 VAL A CB +1184 C CG1 . VAL A 151 ? 1.3971 0.7007 0.6226 -0.2844 0.1485 -0.0521 150 VAL A CG1 +1185 C CG2 . VAL A 151 ? 1.4870 0.7922 0.7149 -0.2823 0.1469 -0.0513 150 VAL A CG2 +1186 N N . TYR A 152 ? 1.6474 0.9473 0.8683 -0.2887 0.1530 -0.0539 151 TYR A N +1187 C CA . TYR A 152 ? 1.6474 0.9457 0.8668 -0.2903 0.1554 -0.0549 151 TYR A CA +1188 C C . TYR A 152 ? 1.7406 1.0386 0.9593 -0.2909 0.1556 -0.0551 151 TYR A C +1189 O O . TYR A 152 ? 1.8110 1.1093 1.0284 -0.2917 0.1540 -0.0547 151 TYR A O +1190 C CB . TYR A 152 ? 1.4865 0.7838 0.7037 -0.2920 0.1557 -0.0551 151 TYR A CB +1191 C CG . TYR A 152 ? 1.7273 1.0249 0.9452 -0.2914 0.1554 -0.0549 151 TYR A CG +1192 C CD1 . TYR A 152 ? 1.7775 1.0741 0.9960 -0.2913 0.1577 -0.0556 151 TYR A CD1 +1193 C CD2 . TYR A 152 ? 1.4828 0.7815 0.7006 -0.2910 0.1529 -0.0539 151 TYR A CD2 +1194 C CE1 . TYR A 152 ? 1.6257 0.9224 0.8447 -0.2908 0.1574 -0.0554 151 TYR A CE1 +1195 C CE2 . TYR A 152 ? 2.0561 1.3550 1.2745 -0.2904 0.1526 -0.0536 151 TYR A CE2 +1196 C CZ . TYR A 152 ? 2.0133 1.3111 1.2322 -0.2903 0.1548 -0.0544 151 TYR A CZ +1197 O OH . TYR A 152 ? 1.6935 0.9914 0.9129 -0.2898 0.1545 -0.0542 151 TYR A OH +1198 N N . ILE A 153 ? 1.5713 0.8687 0.7910 -0.2905 0.1577 -0.0559 152 ILE A N +1199 C CA . ILE A 153 ? 1.7033 1.0001 0.9224 -0.2910 0.1583 -0.0562 152 ILE A CA +1200 C C . ILE A 153 ? 1.9712 1.2663 1.1884 -0.2930 0.1605 -0.0572 152 ILE A C +1201 O O . ILE A 153 ? 2.0760 1.3702 1.2927 -0.2937 0.1622 -0.0578 152 ILE A O +1202 C CB . ILE A 153 ? 1.6959 0.9929 0.9172 -0.2894 0.1591 -0.0564 152 ILE A CB +1203 C CG1 . ILE A 153 ? 1.5359 0.8346 0.7593 -0.2875 0.1571 -0.0555 152 ILE A CG1 +1204 C CG2 . ILE A 153 ? 1.4766 0.7734 0.6974 -0.2898 0.1592 -0.0565 152 ILE A CG2 +1205 C CD1 . ILE A 153 ? 2.0313 1.3304 1.2567 -0.2859 0.1576 -0.0556 152 ILE A CD1 +1206 N N . MET A 154 ? 1.9772 1.2719 1.1932 -0.2941 0.1606 -0.0574 153 MET A N +1207 C CA . MET A 154 ? 2.2263 1.5195 1.4403 -0.2961 0.1625 -0.0583 153 MET A CA +1208 C C . MET A 154 ? 2.0624 1.3553 1.2760 -0.2964 0.1627 -0.0584 153 MET A C +1209 O O . MET A 154 ? 1.9561 1.2500 1.1700 -0.2958 0.1605 -0.0577 153 MET A O +1210 C CB . MET A 154 ? 2.1863 1.4795 1.3982 -0.2977 0.1613 -0.0579 153 MET A CB +1211 C CG . MET A 154 ? 2.2260 1.5177 1.4355 -0.2999 0.1630 -0.0588 153 MET A CG +1212 S SD . MET A 154 ? 3.0623 2.3535 2.2699 -0.3015 0.1629 -0.0588 153 MET A SD +1213 C CE . MET A 154 ? 1.9992 1.2922 1.2070 -0.3006 0.1592 -0.0574 153 MET A CE +1214 N N . ALA A 155 ? 2.0455 1.3369 1.2584 -0.2974 0.1652 -0.0595 154 ALA A N +1215 C CA . ALA A 155 ? 1.9801 1.2711 1.1927 -0.2977 0.1655 -0.0597 154 ALA A CA +1216 C C . ALA A 155 ? 2.3638 1.6546 1.5740 -0.2996 0.1644 -0.0595 154 ALA A C +1217 O O . ALA A 155 ? 2.0675 1.3579 1.2760 -0.3010 0.1645 -0.0597 154 ALA A O +1218 C CB . ALA A 155 ? 1.6428 0.9323 0.8556 -0.2980 0.1686 -0.0608 154 ALA A CB +1219 N N . ASP A 156 ? 2.4094 1.7003 1.6194 -0.2995 0.1635 -0.0593 155 ASP A N +1220 C CA . ASP A 156 ? 2.6779 1.9684 1.8857 -0.3014 0.1628 -0.0594 155 ASP A CA +1221 C C . ASP A 156 ? 2.8698 2.1591 2.0773 -0.3019 0.1646 -0.0601 155 ASP A C +1222 O O . ASP A 156 ? 2.2306 1.5203 1.4386 -0.3013 0.1635 -0.0597 155 ASP A O +1223 C CB . ASP A 156 ? 2.5850 1.8769 1.7927 -0.3010 0.1596 -0.0583 155 ASP A CB +1224 C CG . ASP A 156 ? 2.6544 1.9457 1.8596 -0.3030 0.1588 -0.0583 155 ASP A CG +1225 O OD1 . ASP A 156 ? 2.7499 2.0400 1.9536 -0.3047 0.1607 -0.0592 155 ASP A OD1 +1226 O OD2 . ASP A 156 ? 2.2634 1.5557 1.4684 -0.3029 0.1562 -0.0575 155 ASP A OD2 +1227 N N . LYS A 157 ? 3.1183 2.4063 2.3251 -0.3030 0.1674 -0.0612 156 LYS A N +1228 C CA . LYS A 157 ? 2.9880 2.2747 2.1947 -0.3034 0.1695 -0.0620 156 LYS A CA +1229 C C . LYS A 157 ? 2.7186 2.0049 1.9237 -0.3047 0.1687 -0.0619 156 LYS A C +1230 O O . LYS A 157 ? 2.2141 1.4998 1.4195 -0.3045 0.1695 -0.0622 156 LYS A O +1231 C CB . LYS A 157 ? 2.9075 2.1927 2.1137 -0.3045 0.1727 -0.0632 156 LYS A CB +1232 C CG . LYS A 157 ? 2.9035 2.1887 2.1115 -0.3030 0.1740 -0.0634 156 LYS A CG +1233 C CD . LYS A 157 ? 2.7281 2.0117 1.9354 -0.3042 0.1771 -0.0646 156 LYS A CD +1234 C CE . LYS A 157 ? 2.6111 1.8947 1.8205 -0.3027 0.1784 -0.0649 156 LYS A CE +1235 N NZ . LYS A 157 ? 2.6114 1.8963 1.8219 -0.3014 0.1765 -0.0640 156 LYS A NZ +1236 N N . GLN A 158 ? 2.9577 2.2444 2.1610 -0.3060 0.1671 -0.0616 157 GLN A N +1237 C CA . GLN A 158 ? 2.9698 2.2562 2.1714 -0.3074 0.1661 -0.0615 157 GLN A CA +1238 C C . GLN A 158 ? 2.7431 2.0305 1.9457 -0.3061 0.1637 -0.0605 157 GLN A C +1239 O O . GLN A 158 ? 2.4417 1.7285 1.6438 -0.3065 0.1637 -0.0606 157 GLN A O +1240 C CB . GLN A 158 ? 2.8678 2.1542 2.0671 -0.3094 0.1651 -0.0614 157 GLN A CB +1241 C CG . GLN A 158 ? 3.0795 2.3647 2.2774 -0.3110 0.1676 -0.0625 157 GLN A CG +1242 C CD . GLN A 158 ? 3.1212 2.4048 2.3180 -0.3125 0.1702 -0.0636 157 GLN A CD +1243 O OE1 . GLN A 158 ? 3.1928 2.4758 2.3909 -0.3117 0.1720 -0.0641 157 GLN A OE1 +1244 N NE2 . GLN A 158 ? 2.8246 2.1076 2.0190 -0.3148 0.1703 -0.0640 157 GLN A NE2 +1245 N N . LYS A 159 ? 2.8249 2.1138 2.0290 -0.3045 0.1616 -0.0596 158 LYS A N +1246 C CA . LYS A 159 ? 2.5540 1.8439 1.7591 -0.3032 0.1591 -0.0587 158 LYS A CA +1247 C C . LYS A 159 ? 2.4715 1.7619 1.6791 -0.3010 0.1595 -0.0585 158 LYS A C +1248 O O . LYS A 159 ? 2.1910 1.4825 1.3998 -0.2996 0.1575 -0.0576 158 LYS A O +1249 C CB . LYS A 159 ? 2.3561 1.6474 1.5610 -0.3031 0.1563 -0.0577 158 LYS A CB +1250 C CG . LYS A 159 ? 2.9749 2.2657 2.1773 -0.3053 0.1558 -0.0579 158 LYS A CG +1251 C CD . LYS A 159 ? 3.0879 2.3775 2.2884 -0.3072 0.1565 -0.0584 158 LYS A CD +1252 C CE . LYS A 159 ? 2.7527 2.0414 1.9508 -0.3095 0.1575 -0.0591 158 LYS A CE +1253 N NZ . LYS A 159 ? 2.5860 1.8733 1.7822 -0.3114 0.1587 -0.0598 158 LYS A NZ +1254 N N . ASN A 160 ? 2.4469 1.7364 1.6553 -0.3007 0.1622 -0.0593 159 ASN A N +1255 C CA . ASN A 160 ? 2.5011 1.7908 1.7118 -0.2988 0.1630 -0.0593 159 ASN A CA +1256 C C . ASN A 160 ? 2.2974 1.5887 1.5100 -0.2967 0.1611 -0.0584 159 ASN A C +1257 O O . ASN A 160 ? 2.0186 1.3105 1.2330 -0.2951 0.1605 -0.0580 159 ASN A O +1258 C CB . ASN A 160 ? 2.4861 1.7752 1.6967 -0.2987 0.1630 -0.0593 159 ASN A CB +1259 C CG . ASN A 160 ? 2.6697 1.9583 1.8821 -0.2973 0.1648 -0.0597 159 ASN A CG +1260 O OD1 . ASN A 160 ? 2.6683 1.9562 1.8812 -0.2971 0.1670 -0.0604 159 ASN A OD1 +1261 N ND2 . ASN A 160 ? 2.4312 1.7202 1.6446 -0.2962 0.1637 -0.0592 159 ASN A ND2 +1262 N N . GLY A 161 ? 2.1541 1.4463 1.3665 -0.2969 0.1600 -0.0580 160 GLY A N +1263 C CA . GLY A 161 ? 2.1841 1.4778 1.3983 -0.2951 0.1581 -0.0571 160 GLY A CA +1264 C C . GLY A 161 ? 2.0302 1.3241 1.2444 -0.2952 0.1587 -0.0573 160 GLY A C +1265 O O . GLY A 161 ? 2.0021 1.2948 1.2155 -0.2963 0.1610 -0.0582 160 GLY A O +1266 N N . ILE A 162 ? 2.0682 1.3634 1.2833 -0.2941 0.1567 -0.0565 161 ILE A N +1267 C CA . ILE A 162 ? 1.9790 1.2744 1.1942 -0.2942 0.1571 -0.0565 161 ILE A CA +1268 C C . ILE A 162 ? 1.8802 1.1765 1.0942 -0.2948 0.1546 -0.0557 161 ILE A C +1269 O O . ILE A 162 ? 1.8538 1.1509 1.0677 -0.2946 0.1523 -0.0550 161 ILE A O +1270 C CB . ILE A 162 ? 2.0635 1.3596 1.2810 -0.2922 0.1574 -0.0564 161 ILE A CB +1271 C CG1 . ILE A 162 ? 2.0444 1.3421 1.2635 -0.2905 0.1548 -0.0553 161 ILE A CG1 +1272 C CG2 . ILE A 162 ? 2.1584 1.4535 1.3770 -0.2917 0.1600 -0.0572 161 ILE A CG2 +1273 C CD1 . ILE A 162 ? 1.5973 0.8959 0.8187 -0.2887 0.1548 -0.0551 161 ILE A CD1 +1274 N N . LYS A 163 ? 1.7223 1.0183 0.9355 -0.2955 0.1551 -0.0559 162 LYS A N +1275 C CA . LYS A 163 ? 1.9215 1.2184 1.1338 -0.2960 0.1528 -0.0552 162 LYS A CA +1276 C C . LYS A 163 ? 1.9980 1.2957 1.2119 -0.2945 0.1524 -0.0548 162 LYS A C +1277 O O . LYS A 163 ? 2.1419 1.4389 1.3563 -0.2944 0.1545 -0.0554 162 LYS A O +1278 C CB . LYS A 163 ? 2.1704 1.4662 1.3801 -0.2982 0.1536 -0.0557 162 LYS A CB +1279 C CG . LYS A 163 ? 2.5951 1.8910 1.8029 -0.2996 0.1518 -0.0553 162 LYS A CG +1280 C CD . LYS A 163 ? 2.5577 1.8526 1.7630 -0.3018 0.1525 -0.0558 162 LYS A CD +1281 C CE . LYS A 163 ? 2.5038 1.7984 1.7070 -0.3034 0.1511 -0.0556 162 LYS A CE +1282 N NZ . LYS A 163 ? 2.4943 1.7882 1.6973 -0.3039 0.1522 -0.0562 162 LYS A NZ +1283 N N . VAL A 164 ? 1.8419 1.1410 1.0565 -0.2935 0.1499 -0.0538 163 VAL A N +1284 C CA . VAL A 164 ? 1.7723 1.0721 0.9885 -0.2921 0.1495 -0.0534 163 VAL A CA +1285 C C . VAL A 164 ? 1.5224 0.8228 0.7375 -0.2926 0.1474 -0.0527 163 VAL A C +1286 O O . VAL A 164 ? 1.8899 1.1907 1.1038 -0.2933 0.1455 -0.0522 163 VAL A O +1287 C CB . VAL A 164 ? 2.0313 1.3324 1.2500 -0.2899 0.1485 -0.0529 163 VAL A CB +1288 C CG1 . VAL A 164 ? 1.6341 0.9359 0.8546 -0.2885 0.1484 -0.0526 163 VAL A CG1 +1289 C CG2 . VAL A 164 ? 1.9265 1.2269 1.1460 -0.2896 0.1504 -0.0535 163 VAL A CG2 +1290 N N . ASN A 165 ? 1.5622 0.8627 0.7777 -0.2922 0.1478 -0.0526 164 ASN A N +1291 C CA . ASN A 165 ? 1.9120 1.2131 1.1267 -0.2925 0.1457 -0.0519 164 ASN A CA +1292 C C . ASN A 165 ? 1.8072 1.1089 1.0234 -0.2912 0.1457 -0.0516 164 ASN A C +1293 O O . ASN A 165 ? 1.9338 1.2348 1.1509 -0.2908 0.1478 -0.0523 164 ASN A O +1294 C CB . ASN A 165 ? 1.7817 1.0818 0.9937 -0.2947 0.1461 -0.0522 164 ASN A CB +1295 C CG . ASN A 165 ? 2.0300 1.3288 1.2414 -0.2955 0.1487 -0.0531 164 ASN A CG +1296 O OD1 . ASN A 165 ? 2.3396 1.6376 1.5515 -0.2957 0.1510 -0.0539 164 ASN A OD1 +1297 N ND2 . ASN A 165 ? 2.4630 1.7616 1.6735 -0.2961 0.1483 -0.0529 164 ASN A ND2 +1298 N N . PHE A 166 ? 1.5928 0.8956 0.8093 -0.2906 0.1433 -0.0507 165 PHE A N +1299 C CA . PHE A 166 ? 1.7259 1.0292 0.9437 -0.2894 0.1429 -0.0504 165 PHE A CA +1300 C C . PHE A 166 ? 1.5586 0.8629 0.7759 -0.2892 0.1402 -0.0494 165 PHE A C +1301 O O . PHE A 166 ? 1.8431 1.1478 1.0594 -0.2898 0.1384 -0.0489 165 PHE A O +1302 C CB . PHE A 166 ? 1.7464 1.0505 0.9668 -0.2874 0.1434 -0.0504 165 PHE A CB +1303 C CG . PHE A 166 ? 1.6196 0.9249 0.8413 -0.2863 0.1418 -0.0499 165 PHE A CG +1304 C CD1 . PHE A 166 ? 1.5437 0.8485 0.7651 -0.2867 0.1427 -0.0503 165 PHE A CD1 +1305 C CD2 . PHE A 166 ? 1.3396 0.6463 0.5626 -0.2849 0.1396 -0.0490 165 PHE A CD2 +1306 C CE1 . PHE A 166 ? 1.4013 0.7070 0.6237 -0.2857 0.1413 -0.0498 165 PHE A CE1 +1307 C CE2 . PHE A 166 ? 1.5133 0.8209 0.7374 -0.2839 0.1383 -0.0485 165 PHE A CE2 +1308 C CZ . PHE A 166 ? 1.5561 0.8633 0.7799 -0.2843 0.1391 -0.0489 165 PHE A CZ +1309 N N . LYS A 167 ? 1.5639 0.8686 0.7820 -0.2884 0.1398 -0.0491 166 LYS A N +1310 C CA . LYS A 167 ? 1.7220 1.0274 0.9396 -0.2883 0.1373 -0.0481 166 LYS A CA +1311 C C . LYS A 167 ? 1.6866 0.9933 0.9065 -0.2863 0.1362 -0.0476 166 LYS A C +1312 O O . LYS A 167 ? 1.7426 1.0489 0.9632 -0.2858 0.1373 -0.0478 166 LYS A O +1313 C CB . LYS A 167 ? 1.5915 0.8958 0.8070 -0.2899 0.1377 -0.0483 166 LYS A CB +1314 C CG . LYS A 167 ? 2.1436 1.4486 1.3582 -0.2900 0.1351 -0.0473 166 LYS A CG +1315 C CD . LYS A 167 ? 2.4080 1.7118 1.6206 -0.2915 0.1358 -0.0475 166 LYS A CD +1316 C CE . LYS A 167 ? 2.1160 1.4184 1.3266 -0.2935 0.1376 -0.0483 166 LYS A CE +1317 N NZ . LYS A 167 ? 2.5066 1.8091 1.7156 -0.2946 0.1363 -0.0481 166 LYS A NZ +1318 N N . ILE A 168 ? 1.5178 0.8258 0.7387 -0.2853 0.1341 -0.0468 167 ILE A N +1319 C CA . ILE A 168 ? 1.7872 1.0965 1.0103 -0.2834 0.1329 -0.0462 167 ILE A CA +1320 C C . ILE A 168 ? 1.5834 0.8931 0.8059 -0.2834 0.1311 -0.0455 167 ILE A C +1321 O O . ILE A 168 ? 1.5473 0.8570 0.7682 -0.2844 0.1294 -0.0450 167 ILE A O +1322 C CB . ILE A 168 ? 1.4027 0.7132 0.6271 -0.2823 0.1314 -0.0457 167 ILE A CB +1323 C CG1 . ILE A 168 ? 1.5735 0.8837 0.7986 -0.2821 0.1331 -0.0464 167 ILE A CG1 +1324 C CG2 . ILE A 168 ? 1.4768 0.7886 0.7034 -0.2804 0.1301 -0.0451 167 ILE A CG2 +1325 C CD1 . ILE A 168 ? 1.7686 1.0786 0.9955 -0.2811 0.1353 -0.0470 167 ILE A CD1 +1326 N N . ARG A 169 ? 1.4228 0.7327 0.6466 -0.2823 0.1314 -0.0454 168 ARG A N +1327 C CA . ARG A 169 ? 1.6104 0.9208 0.8340 -0.2820 0.1295 -0.0446 168 ARG A CA +1328 C C . ARG A 169 ? 1.4409 0.7529 0.6666 -0.2802 0.1276 -0.0439 168 ARG A C +1329 O O . ARG A 169 ? 1.8072 1.1198 1.0350 -0.2788 0.1284 -0.0441 168 ARG A O +1330 C CB . ARG A 169 ? 1.6483 0.9579 0.8719 -0.2821 0.1309 -0.0450 168 ARG A CB +1331 C CG . ARG A 169 ? 1.8080 1.1159 1.0295 -0.2839 0.1327 -0.0457 168 ARG A CG +1332 C CD . ARG A 169 ? 1.7311 1.0381 0.9525 -0.2840 0.1339 -0.0460 168 ARG A CD +1333 N NE . ARG A 169 ? 2.0350 1.3420 1.2585 -0.2828 0.1358 -0.0466 168 ARG A NE +1334 C CZ . ARG A 169 ? 2.3174 1.6238 1.5412 -0.2830 0.1380 -0.0475 168 ARG A CZ +1335 N NH1 . ARG A 169 ? 1.9758 1.2814 1.1981 -0.2844 0.1387 -0.0479 168 ARG A NH1 +1336 N NH2 . ARG A 169 ? 2.1081 1.4145 1.3338 -0.2818 0.1395 -0.0480 168 ARG A NH2 +1337 N N . HIS A 170 ? 1.3324 0.6452 0.5574 -0.2803 0.1251 -0.0431 169 HIS A N +1338 C CA . HIS A 170 ? 1.6242 0.9384 0.8510 -0.2787 0.1231 -0.0423 169 HIS A CA +1339 C C . HIS A 170 ? 1.4073 0.7217 0.6341 -0.2783 0.1220 -0.0417 169 HIS A C +1340 O O . HIS A 170 ? 1.8618 1.1755 1.0866 -0.2795 0.1212 -0.0415 169 HIS A O +1341 C CB . HIS A 170 ? 1.3423 0.6573 0.5687 -0.2788 0.1210 -0.0417 169 HIS A CB +1342 C CG . HIS A 170 ? 1.7358 1.0507 0.9624 -0.2791 0.1219 -0.0422 169 HIS A CG +1343 N ND1 . HIS A 170 ? 1.7291 1.0449 0.9578 -0.2777 0.1222 -0.0422 169 HIS A ND1 +1344 C CD2 . HIS A 170 ? 1.8482 1.1621 1.0729 -0.2806 0.1226 -0.0426 169 HIS A CD2 +1345 C CE1 . HIS A 170 ? 1.5829 0.8982 0.8110 -0.2783 0.1230 -0.0427 169 HIS A CE1 +1346 N NE2 . HIS A 170 ? 1.3772 0.6915 0.6030 -0.2801 0.1232 -0.0429 169 HIS A NE2 +1347 N N . ASN A 171 ? 1.8788 1.1940 1.1076 -0.2767 0.1218 -0.0415 170 ASN A N +1348 C CA . ASN A 171 ? 1.5077 0.8231 0.7366 -0.2763 0.1206 -0.0410 170 ASN A CA +1349 C C . ASN A 171 ? 1.8474 1.1639 1.0761 -0.2760 0.1177 -0.0400 170 ASN A C +1350 O O . ASN A 171 ? 2.2236 1.5410 1.4531 -0.2754 0.1168 -0.0397 170 ASN A O +1351 C CB . ASN A 171 ? 1.8826 1.1987 1.1138 -0.2746 0.1213 -0.0411 170 ASN A CB +1352 C CG . ASN A 171 ? 1.8563 1.1712 1.0875 -0.2749 0.1239 -0.0419 170 ASN A CG +1353 O OD1 . ASN A 171 ? 1.6863 1.0001 0.9163 -0.2762 0.1255 -0.0426 170 ASN A OD1 +1354 N ND2 . ASN A 171 ? 1.6847 0.9998 0.9173 -0.2739 0.1243 -0.0420 170 ASN A ND2 +1355 N N . ILE A 172 ? 1.8633 1.1795 1.0908 -0.2764 0.1164 -0.0395 171 ILE A N +1356 C CA . ILE A 172 ? 1.7594 1.0764 0.9866 -0.2762 0.1137 -0.0385 171 ILE A CA +1357 C C . ILE A 172 ? 1.9886 1.3059 1.2167 -0.2752 0.1130 -0.0381 171 ILE A C +1358 O O . ILE A 172 ? 2.3474 1.6640 1.5757 -0.2751 0.1146 -0.0386 171 ILE A O +1359 C CB . ILE A 172 ? 1.6972 1.0133 0.9216 -0.2781 0.1128 -0.0384 171 ILE A CB +1360 C CG1 . ILE A 172 ? 1.7118 1.0275 0.9352 -0.2791 0.1137 -0.0389 171 ILE A CG1 +1361 C CG2 . ILE A 172 ? 1.4899 0.8067 0.7138 -0.2780 0.1099 -0.0374 171 ILE A CG2 +1362 C CD1 . ILE A 172 ? 1.6751 0.9895 0.8957 -0.2812 0.1139 -0.0391 171 ILE A CD1 +1363 N N . GLU A 173 ? 1.4829 0.8012 0.7116 -0.2744 0.1107 -0.0373 172 GLU A N +1364 C CA . GLU A 173 ? 2.0670 1.3856 1.2966 -0.2734 0.1101 -0.0369 172 GLU A CA +1365 C C . GLU A 173 ? 2.3339 1.6513 1.5618 -0.2743 0.1102 -0.0368 172 GLU A C +1366 O O . GLU A 173 ? 2.4560 1.7732 1.6847 -0.2737 0.1108 -0.0369 172 GLU A O +1367 C CB . GLU A 173 ? 1.6922 1.0122 0.9232 -0.2721 0.1078 -0.0361 172 GLU A CB +1368 C CG . GLU A 173 ? 2.4793 1.7998 1.7119 -0.2707 0.1078 -0.0359 172 GLU A CG +1369 C CD . GLU A 173 ? 2.9841 2.3059 2.2180 -0.2695 0.1055 -0.0351 172 GLU A CD +1370 O OE1 . GLU A 173 ? 2.7350 2.0567 1.9675 -0.2701 0.1036 -0.0344 172 GLU A OE1 +1371 O OE2 . GLU A 173 ? 3.1139 2.4367 2.3500 -0.2680 0.1057 -0.0351 172 GLU A OE2 +1372 N N . ASP A 174 ? 1.9553 1.2719 1.1808 -0.2759 0.1095 -0.0367 173 ASP A N +1373 C CA . ASP A 174 ? 2.0149 1.3302 1.2385 -0.2770 0.1095 -0.0366 173 ASP A CA +1374 C C . ASP A 174 ? 2.4180 1.7319 1.6411 -0.2777 0.1122 -0.0375 173 ASP A C +1375 O O . ASP A 174 ? 3.2001 2.5129 2.4216 -0.2786 0.1125 -0.0375 173 ASP A O +1376 C CB . ASP A 174 ? 2.3041 1.6188 1.5251 -0.2785 0.1080 -0.0362 173 ASP A CB +1377 C CG . ASP A 174 ? 2.2713 1.5858 1.4913 -0.2797 0.1087 -0.0367 173 ASP A CG +1378 O OD1 . ASP A 174 ? 2.2183 1.5325 1.4389 -0.2797 0.1109 -0.0374 173 ASP A OD1 +1379 O OD2 . ASP A 174 ? 2.1728 1.4874 1.3915 -0.2805 0.1071 -0.0363 173 ASP A OD2 +1380 N N . GLY A 175 ? 1.7260 1.0401 0.9504 -0.2772 0.1141 -0.0382 174 GLY A N +1381 C CA . GLY A 175 ? 1.7252 1.0382 0.9494 -0.2778 0.1166 -0.0391 174 GLY A CA +1382 C C . GLY A 175 ? 1.9556 1.2676 1.1780 -0.2794 0.1179 -0.0396 174 GLY A C +1383 O O . GLY A 175 ? 1.9785 1.2895 1.2006 -0.2800 0.1202 -0.0405 174 GLY A O +1384 N N . SER A 176 ? 1.4795 0.7917 0.7005 -0.2803 0.1164 -0.0392 175 SER A N +1385 C CA . SER A 176 ? 1.9111 1.2224 1.1302 -0.2820 0.1174 -0.0397 175 SER A CA +1386 C C . SER A 176 ? 1.7108 1.0226 0.9312 -0.2815 0.1186 -0.0403 175 SER A C +1387 O O . SER A 176 ? 1.9034 1.2163 1.1261 -0.2799 0.1185 -0.0402 175 SER A O +1388 C CB . SER A 176 ? 1.8631 1.1742 1.0800 -0.2832 0.1154 -0.0392 175 SER A CB +1389 O OG . SER A 176 ? 1.8479 1.1604 1.0658 -0.2823 0.1132 -0.0385 175 SER A OG +1390 N N . VAL A 177 ? 1.6245 0.9354 0.8433 -0.2830 0.1197 -0.0408 176 VAL A N +1391 C CA . VAL A 177 ? 1.5614 0.8725 0.7812 -0.2828 0.1214 -0.0415 176 VAL A CA +1392 C C . VAL A 177 ? 1.8786 1.1895 1.0969 -0.2840 0.1210 -0.0416 176 VAL A C +1393 O O . VAL A 177 ? 2.1364 1.4461 1.3525 -0.2857 0.1217 -0.0419 176 VAL A O +1394 C CB . VAL A 177 ? 1.5652 0.8751 0.7851 -0.2832 0.1242 -0.0424 176 VAL A CB +1395 C CG1 . VAL A 177 ? 1.7374 1.0472 0.9580 -0.2831 0.1260 -0.0432 176 VAL A CG1 +1396 C CG2 . VAL A 177 ? 1.7139 1.0240 0.9355 -0.2818 0.1248 -0.0424 176 VAL A CG2 +1397 N N . GLN A 178 ? 1.5294 0.8414 0.7490 -0.2832 0.1200 -0.0414 177 GLN A N +1398 C CA . GLN A 178 ? 1.6576 0.9695 0.8759 -0.2843 0.1195 -0.0414 177 GLN A CA +1399 C C . GLN A 178 ? 1.8193 1.1305 1.0374 -0.2849 0.1219 -0.0424 177 GLN A C +1400 O O . GLN A 178 ? 1.7498 1.0614 0.9698 -0.2838 0.1230 -0.0427 177 GLN A O +1401 C CB . GLN A 178 ? 1.2965 0.6098 0.5161 -0.2831 0.1174 -0.0408 177 GLN A CB +1402 C CG . GLN A 178 ? 1.8431 1.1564 1.0617 -0.2841 0.1169 -0.0409 177 GLN A CG +1403 C CD . GLN A 178 ? 1.6868 0.9993 0.9027 -0.2858 0.1156 -0.0407 177 GLN A CD +1404 O OE1 . GLN A 178 ? 1.8289 1.1418 1.0443 -0.2858 0.1136 -0.0400 177 GLN A OE1 +1405 N NE2 . GLN A 178 ? 1.8019 1.1135 1.0161 -0.2875 0.1166 -0.0413 177 GLN A NE2 +1406 N N . LEU A 179 ? 1.7359 1.0458 0.9517 -0.2868 0.1227 -0.0428 178 LEU A N +1407 C CA . LEU A 179 ? 1.5685 0.8775 0.7840 -0.2875 0.1252 -0.0438 178 LEU A CA +1408 C C . LEU A 179 ? 1.5516 0.8611 0.7673 -0.2876 0.1247 -0.0438 178 LEU A C +1409 O O . LEU A 179 ? 1.7965 1.1064 1.0113 -0.2880 0.1226 -0.0433 178 LEU A O +1410 C CB . LEU A 179 ? 1.6209 0.9284 0.8340 -0.2895 0.1265 -0.0443 178 LEU A CB +1411 C CG . LEU A 179 ? 1.9160 1.2228 1.1289 -0.2896 0.1275 -0.0444 178 LEU A CG +1412 C CD1 . LEU A 179 ? 2.1684 1.4736 1.3785 -0.2918 0.1286 -0.0449 178 LEU A CD1 +1413 C CD2 . LEU A 179 ? 1.4907 0.7974 0.7056 -0.2884 0.1297 -0.0450 178 LEU A CD2 +1414 N N . ALA A 180 ? 1.4705 0.7797 0.6871 -0.2873 0.1267 -0.0445 179 ALA A N +1415 C CA . ALA A 180 ? 1.5759 0.8853 0.7927 -0.2874 0.1265 -0.0447 179 ALA A CA +1416 C C . ALA A 180 ? 1.5785 0.8868 0.7945 -0.2885 0.1289 -0.0456 179 ALA A C +1417 O O . ALA A 180 ? 1.7822 1.0904 0.9996 -0.2877 0.1305 -0.0461 179 ALA A O +1418 C CB . ALA A 180 ? 1.7078 1.0186 0.9272 -0.2853 0.1258 -0.0443 179 ALA A CB +1419 N N . ASP A 181 ? 1.5764 0.8836 0.7899 -0.2905 0.1292 -0.0460 180 ASP A N +1420 C CA . ASP A 181 ? 1.8827 1.1886 1.0950 -0.2918 0.1316 -0.0469 180 ASP A CA +1421 C C . ASP A 181 ? 1.6980 1.0041 0.9110 -0.2916 0.1320 -0.0472 180 ASP A C +1422 O O . ASP A 181 ? 1.7506 1.0568 0.9626 -0.2924 0.1306 -0.0470 180 ASP A O +1423 C CB . ASP A 181 ? 1.8094 1.1143 1.0188 -0.2940 0.1313 -0.0470 180 ASP A CB +1424 C CG . ASP A 181 ? 1.9387 1.2422 1.1468 -0.2954 0.1340 -0.0480 180 ASP A CG +1425 O OD1 . ASP A 181 ? 2.1846 1.4877 1.3937 -0.2951 0.1360 -0.0487 180 ASP A OD1 +1426 O OD2 . ASP A 181 ? 2.0996 1.4023 1.3056 -0.2970 0.1341 -0.0481 180 ASP A OD2 +1427 N N . HIS A 182 ? 1.5048 0.8107 0.7194 -0.2906 0.1339 -0.0477 181 HIS A N +1428 C CA . HIS A 182 ? 1.7769 1.0828 0.9922 -0.2903 0.1345 -0.0480 181 HIS A CA +1429 C C . HIS A 182 ? 1.6589 0.9634 0.8727 -0.2919 0.1367 -0.0490 181 HIS A C +1430 O O . HIS A 182 ? 1.5570 0.8606 0.7708 -0.2922 0.1390 -0.0497 181 HIS A O +1431 C CB . HIS A 182 ? 1.5987 0.9054 0.8168 -0.2883 0.1353 -0.0481 181 HIS A CB +1432 C CG . HIS A 182 ? 1.4698 0.7779 0.6896 -0.2866 0.1332 -0.0472 181 HIS A CG +1433 N ND1 . HIS A 182 ? 1.6274 0.9361 0.8475 -0.2861 0.1321 -0.0467 181 HIS A ND1 +1434 C CD2 . HIS A 182 ? 1.4136 0.7228 0.6352 -0.2852 0.1320 -0.0467 181 HIS A CD2 +1435 C CE1 . HIS A 182 ? 1.7816 1.0916 1.0034 -0.2845 0.1304 -0.0460 181 HIS A CE1 +1436 N NE2 . HIS A 182 ? 1.4511 0.7615 0.6739 -0.2839 0.1303 -0.0460 181 HIS A NE2 +1437 N N . TYR A 183 ? 1.9422 1.2465 1.1550 -0.2928 0.1360 -0.0490 182 TYR A N +1438 C CA . TYR A 183 ? 1.8652 1.1682 1.0767 -0.2942 0.1380 -0.0499 182 TYR A CA +1439 C C . TYR A 183 ? 1.7100 1.0132 0.9227 -0.2934 0.1383 -0.0500 182 TYR A C +1440 O O . TYR A 183 ? 2.0145 1.3182 1.2270 -0.2934 0.1364 -0.0495 182 TYR A O +1441 C CB . TYR A 183 ? 1.5395 0.8418 0.7483 -0.2964 0.1373 -0.0500 182 TYR A CB +1442 C CG . TYR A 183 ? 1.6927 0.9945 0.8999 -0.2975 0.1374 -0.0500 182 TYR A CG +1443 C CD1 . TYR A 183 ? 1.8860 1.1887 1.0935 -0.2969 0.1355 -0.0492 182 TYR A CD1 +1444 C CD2 . TYR A 183 ? 1.4207 0.7212 0.6262 -0.2992 0.1396 -0.0509 182 TYR A CD2 +1445 C CE1 . TYR A 183 ? 1.7731 1.0753 0.9791 -0.2979 0.1356 -0.0493 182 TYR A CE1 +1446 C CE2 . TYR A 183 ? 1.8412 1.1412 1.0453 -0.3002 0.1398 -0.0509 182 TYR A CE2 +1447 C CZ . TYR A 183 ? 1.8726 1.1734 1.0769 -0.2996 0.1378 -0.0501 182 TYR A CZ +1448 O OH . TYR A 183 ? 1.8925 1.1928 1.0953 -0.3006 0.1379 -0.0501 182 TYR A OH +1449 N N . GLN A 184 ? 1.6719 0.9747 0.8859 -0.2927 0.1406 -0.0507 183 GLN A N +1450 C CA . GLN A 184 ? 1.9579 1.2609 1.1733 -0.2917 0.1408 -0.0507 183 GLN A CA +1451 C C . GLN A 184 ? 1.8593 1.1609 1.0738 -0.2928 0.1430 -0.0516 183 GLN A C +1452 O O . GLN A 184 ? 1.7096 1.0100 0.9229 -0.2940 0.1451 -0.0524 183 GLN A O +1453 C CB . GLN A 184 ? 1.8189 1.1226 1.0369 -0.2896 0.1414 -0.0506 183 GLN A CB +1454 C CG . GLN A 184 ? 1.8297 1.1336 1.0493 -0.2884 0.1420 -0.0508 183 GLN A CG +1455 C CD . GLN A 184 ? 1.9674 1.2718 1.1894 -0.2866 0.1430 -0.0508 183 GLN A CD +1456 O OE1 . GLN A 184 ? 1.6297 0.9348 0.8524 -0.2859 0.1424 -0.0505 183 GLN A OE1 +1457 N NE2 . GLN A 184 ? 1.5998 0.9039 0.8230 -0.2859 0.1445 -0.0513 183 GLN A NE2 +1458 N N . GLN A 185 ? 1.5611 0.8628 0.7762 -0.2924 0.1427 -0.0516 184 GLN A N +1459 C CA . GLN A 185 ? 1.6730 0.9734 0.8874 -0.2932 0.1449 -0.0524 184 GLN A CA +1460 C C . GLN A 185 ? 2.0784 1.3791 1.2944 -0.2920 0.1450 -0.0524 184 GLN A C +1461 O O . GLN A 185 ? 1.7379 1.0395 0.9545 -0.2913 0.1429 -0.0516 184 GLN A O +1462 C CB . GLN A 185 ? 1.9808 1.2802 1.1925 -0.2955 0.1447 -0.0527 184 GLN A CB +1463 C CG . GLN A 185 ? 2.3571 1.6571 1.5682 -0.2958 0.1422 -0.0520 184 GLN A CG +1464 C CD . GLN A 185 ? 2.7305 2.0294 1.9391 -0.2981 0.1424 -0.0524 184 GLN A CD +1465 O OE1 . GLN A 185 ? 2.8342 2.1320 2.0412 -0.2995 0.1440 -0.0531 184 GLN A OE1 +1466 N NE2 . GLN A 185 ? 2.8526 2.1516 2.0606 -0.2985 0.1408 -0.0520 184 GLN A NE2 +1467 N N . ASN A 186 ? 1.9425 1.2422 1.1591 -0.2918 0.1475 -0.0532 185 ASN A N +1468 C CA . ASN A 186 ? 1.9210 1.2208 1.1392 -0.2905 0.1480 -0.0532 185 ASN A CA +1469 C C . ASN A 186 ? 2.1314 1.4298 1.3485 -0.2916 0.1498 -0.0540 185 ASN A C +1470 O O . ASN A 186 ? 1.8679 1.1651 1.0836 -0.2931 0.1516 -0.0547 185 ASN A O +1471 C CB . ASN A 186 ? 1.9348 1.2349 1.1552 -0.2888 0.1493 -0.0534 185 ASN A CB +1472 C CG . ASN A 186 ? 1.8699 1.1716 1.0917 -0.2874 0.1473 -0.0525 185 ASN A CG +1473 O OD1 . ASN A 186 ? 1.8253 1.1272 1.0466 -0.2877 0.1471 -0.0524 185 ASN A OD1 +1474 N ND2 . ASN A 186 ? 1.5810 0.8838 0.8045 -0.2858 0.1460 -0.0519 185 ASN A ND2 +1475 N N . THR A 187 ? 1.8839 1.1824 1.1018 -0.2909 0.1492 -0.0537 186 THR A N +1476 C CA . THR A 187 ? 1.9202 1.2174 1.1369 -0.2920 0.1504 -0.0543 186 THR A CA +1477 C C . THR A 187 ? 1.8408 1.1382 1.0590 -0.2906 0.1502 -0.0540 186 THR A C +1478 O O . THR A 187 ? 2.0825 1.3810 1.3016 -0.2897 0.1480 -0.0532 186 THR A O +1479 C CB . THR A 187 ? 1.9095 1.2064 1.1240 -0.2938 0.1490 -0.0541 186 THR A CB +1480 O OG1 . THR A 187 ? 2.1338 1.4300 1.3466 -0.2954 0.1499 -0.0545 186 THR A OG1 +1481 C CG2 . THR A 187 ? 1.7961 1.0918 1.0097 -0.2946 0.1498 -0.0544 186 THR A CG2 +1482 N N . PRO A 188 ? 2.0040 1.3002 1.2225 -0.2906 0.1526 -0.0548 187 PRO A N +1483 C CA . PRO A 188 ? 2.0353 1.3314 1.2551 -0.2894 0.1528 -0.0547 187 PRO A CA +1484 C C . PRO A 188 ? 2.0352 1.3312 1.2542 -0.2899 0.1513 -0.0543 187 PRO A C +1485 O O . PRO A 188 ? 2.1383 1.4332 1.3554 -0.2916 0.1518 -0.0547 187 PRO A O +1486 C CB . PRO A 188 ? 2.0306 1.3251 1.2503 -0.2898 0.1559 -0.0558 187 PRO A CB +1487 C CG . PRO A 188 ? 1.9792 1.2727 1.1968 -0.2918 0.1572 -0.0565 187 PRO A CG +1488 C CD . PRO A 188 ? 1.8872 1.1819 1.1046 -0.2918 0.1554 -0.0559 187 PRO A CD +1489 N N . ILE A 189 ? 2.0538 1.3510 1.2743 -0.2884 0.1494 -0.0535 188 ILE A N +1490 C CA . ILE A 189 ? 2.0663 1.3635 1.2865 -0.2885 0.1480 -0.0530 188 ILE A CA +1491 C C . ILE A 189 ? 2.2176 1.5133 1.4376 -0.2887 0.1502 -0.0537 188 ILE A C +1492 O O . ILE A 189 ? 2.1370 1.4319 1.3558 -0.2897 0.1499 -0.0537 188 ILE A O +1493 C CB . ILE A 189 ? 1.9030 1.2017 1.1251 -0.2866 0.1459 -0.0521 188 ILE A CB +1494 C CG1 . ILE A 189 ? 1.9479 1.2481 1.1703 -0.2863 0.1439 -0.0514 188 ILE A CG1 +1495 C CG2 . ILE A 189 ? 1.7442 1.0429 0.9660 -0.2867 0.1445 -0.0516 188 ILE A CG2 +1496 C CD1 . ILE A 189 ? 1.9921 1.2940 1.2168 -0.2843 0.1423 -0.0506 188 ILE A CD1 +1497 N N . GLY A 190 ? 2.3411 1.6363 1.5622 -0.2879 0.1523 -0.0543 189 GLY A N +1498 C CA . GLY A 190 ? 2.3785 1.6733 1.6020 -0.2875 0.1541 -0.0549 189 GLY A CA +1499 C C . GLY A 190 ? 2.5048 1.7979 1.7266 -0.2894 0.1563 -0.0558 189 GLY A C +1500 O O . GLY A 190 ? 2.2031 1.4950 1.4213 -0.2908 0.1573 -0.0563 189 GLY A O +1501 N N . ASP A 191 ? 2.5270 1.8200 1.7515 -0.2892 0.1572 -0.0561 190 ASP A N +1502 C CA . ASP A 191 ? 2.5843 1.8758 1.8075 -0.2909 0.1593 -0.0570 190 ASP A CA +1503 C C . ASP A 191 ? 2.5499 1.8410 1.7751 -0.2905 0.1619 -0.0579 190 ASP A C +1504 O O . ASP A 191 ? 2.3524 1.6421 1.5761 -0.2919 0.1639 -0.0588 190 ASP A O +1505 C CB . ASP A 191 ? 2.5915 1.8830 1.8164 -0.2913 0.1588 -0.0568 190 ASP A CB +1506 C CG . ASP A 191 ? 2.7905 2.0823 2.0133 -0.2921 0.1563 -0.0559 190 ASP A CG +1507 O OD1 . ASP A 191 ? 2.5878 1.8788 1.8063 -0.2938 0.1559 -0.0560 190 ASP A OD1 +1508 O OD2 . ASP A 191 ? 2.8775 2.1704 2.1030 -0.2912 0.1548 -0.0551 190 ASP A OD2 +1509 N N . GLY A 192 ? 2.5839 1.8762 1.8127 -0.2884 0.1619 -0.0577 191 GLY A N +1510 C CA . GLY A 192 ? 2.5852 1.8773 1.8165 -0.2877 0.1641 -0.0586 191 GLY A CA +1511 C C . GLY A 192 ? 2.7449 2.0360 1.9730 -0.2888 0.1655 -0.0592 191 GLY A C +1512 O O . GLY A 192 ? 2.7341 2.0249 1.9583 -0.2897 0.1644 -0.0588 191 GLY A O +1513 N N . PRO A 193 ? 2.7736 2.0641 2.0034 -0.2887 0.1678 -0.0602 192 PRO A N +1514 C CA . PRO A 193 ? 2.7717 2.0612 1.9988 -0.2899 0.1693 -0.0608 192 PRO A CA +1515 C C . PRO A 193 ? 2.6334 1.9240 1.8610 -0.2886 0.1685 -0.0603 192 PRO A C +1516 O O . PRO A 193 ? 2.1779 1.4700 1.4092 -0.2866 0.1675 -0.0598 192 PRO A O +1517 C CB . PRO A 193 ? 2.6480 1.9370 1.8779 -0.2898 0.1719 -0.0619 192 PRO A CB +1518 C CG . PRO A 193 ? 2.4728 1.7631 1.7081 -0.2877 0.1715 -0.0618 192 PRO A CG +1519 C CD . PRO A 193 ? 2.5124 1.8033 1.7471 -0.2875 0.1692 -0.0607 192 PRO A CD +1520 N N . VAL A 194 ? 2.4645 1.7542 1.6884 -0.2899 0.1689 -0.0604 193 VAL A N +1521 C CA . VAL A 194 ? 2.3291 1.6196 1.5529 -0.2889 0.1682 -0.0600 193 VAL A CA +1522 C C . VAL A 194 ? 2.0163 1.3060 1.2392 -0.2898 0.1702 -0.0607 193 VAL A C +1523 O O . VAL A 194 ? 2.0396 1.3278 1.2603 -0.2915 0.1718 -0.0615 193 VAL A O +1524 C CB . VAL A 194 ? 2.4265 1.7180 1.6484 -0.2892 0.1654 -0.0589 193 VAL A CB +1525 C CG1 . VAL A 194 ? 1.8508 1.1430 1.0732 -0.2884 0.1634 -0.0581 193 VAL A CG1 +1526 C CG2 . VAL A 194 ? 2.2204 1.5114 1.4399 -0.2912 0.1653 -0.0591 193 VAL A CG2 +1527 N N . LEU A 195 ? 1.8806 1.1711 1.1051 -0.2886 0.1700 -0.0606 194 LEU A N +1528 C CA . LEU A 195 ? 1.7659 1.0557 0.9900 -0.2892 0.1718 -0.0612 194 LEU A CA +1529 C C . LEU A 195 ? 1.8537 1.1435 1.0751 -0.2907 0.1707 -0.0609 194 LEU A C +1530 O O . LEU A 195 ? 2.1804 1.4717 1.4020 -0.2901 0.1681 -0.0599 194 LEU A O +1531 C CB . LEU A 195 ? 1.6748 0.9661 0.9028 -0.2872 0.1716 -0.0612 194 LEU A CB +1532 C CG . LEU A 195 ? 1.9956 1.2883 1.2295 -0.2850 0.1716 -0.0615 194 LEU A CG +1533 C CD1 . LEU A 195 ? 1.8957 1.1897 1.1334 -0.2832 0.1716 -0.0616 194 LEU A CD1 +1534 C CD2 . LEU A 195 ? 1.6700 0.9619 0.9058 -0.2855 0.1736 -0.0626 194 LEU A CD2 +1535 N N . LEU A 196 ? 1.7671 1.0557 0.9868 -0.2924 0.1724 -0.0617 195 LEU A N +1536 C CA . LEU A 196 ? 2.1612 1.4502 1.3794 -0.2937 0.1713 -0.0614 195 LEU A CA +1537 C C . LEU A 196 ? 2.0175 1.3061 1.2358 -0.2938 0.1727 -0.0619 195 LEU A C +1538 O O . LEU A 196 ? 2.0881 1.3753 1.3058 -0.2949 0.1752 -0.0629 195 LEU A O +1539 C CB . LEU A 196 ? 2.4511 1.7390 1.6670 -0.2957 0.1719 -0.0619 195 LEU A CB +1540 C CG . LEU A 196 ? 2.1815 1.4695 1.3971 -0.2956 0.1708 -0.0615 195 LEU A CG +1541 C CD1 . LEU A 196 ? 2.0014 1.2882 1.2149 -0.2976 0.1717 -0.0621 195 LEU A CD1 +1542 C CD2 . LEU A 196 ? 2.0210 1.3107 1.2371 -0.2947 0.1675 -0.0602 195 LEU A CD2 +1543 N N . PRO A 197 ? 1.9906 1.2806 1.2100 -0.2927 0.1710 -0.0611 196 PRO A N +1544 C CA . PRO A 197 ? 2.0358 1.3258 1.2560 -0.2923 0.1719 -0.0614 196 PRO A CA +1545 C C . PRO A 197 ? 1.9614 1.2504 1.1797 -0.2941 0.1729 -0.0619 196 PRO A C +1546 O O . PRO A 197 ? 1.9612 1.2501 1.1777 -0.2956 0.1722 -0.0618 196 PRO A O +1547 C CB . PRO A 197 ? 2.0071 1.2988 1.2285 -0.2908 0.1692 -0.0603 196 PRO A CB +1548 C CG . PRO A 197 ? 1.8854 1.1780 1.1059 -0.2912 0.1668 -0.0595 196 PRO A CG +1549 C CD . PRO A 197 ? 1.7905 1.0821 1.0104 -0.2918 0.1679 -0.0599 196 PRO A CD +1550 N N . ASP A 198 ? 2.1357 1.4241 1.3547 -0.2940 0.1746 -0.0625 197 ASP A N +1551 C CA . ASP A 198 ? 2.2321 1.5198 1.4496 -0.2953 0.1753 -0.0629 197 ASP A CA +1552 C C . ASP A 198 ? 2.0252 1.3145 1.2431 -0.2946 0.1727 -0.0618 197 ASP A C +1553 O O . ASP A 198 ? 1.9272 1.2179 1.1468 -0.2929 0.1709 -0.0610 197 ASP A O +1554 C CB . ASP A 198 ? 2.2744 1.5609 1.4925 -0.2953 0.1780 -0.0639 197 ASP A CB +1555 C CG . ASP A 198 ? 2.4311 1.7158 1.6485 -0.2964 0.1808 -0.0651 197 ASP A CG +1556 O OD1 . ASP A 198 ? 2.4240 1.7085 1.6402 -0.2975 0.1807 -0.0652 197 ASP A OD1 +1557 O OD2 . ASP A 198 ? 2.2350 1.5198 1.4556 -0.2957 0.1825 -0.0662 197 ASP A OD2 +1558 N N . ASN A 199 ? 1.8973 1.1862 1.1137 -0.2958 0.1724 -0.0618 198 ASN A N +1559 C CA . ASN A 199 ? 2.0975 1.3877 1.3142 -0.2952 0.1701 -0.0608 198 ASN A CA +1560 C C . ASN A 199 ? 2.0259 1.3168 1.2448 -0.2933 0.1700 -0.0606 198 ASN A C +1561 O O . ASN A 199 ? 1.9667 1.2566 1.1861 -0.2933 0.1721 -0.0614 198 ASN A O +1562 C CB . ASN A 199 ? 2.3653 1.6548 1.5800 -0.2969 0.1704 -0.0610 198 ASN A CB +1563 C CG . ASN A 199 ? 2.3323 1.6214 1.5447 -0.2988 0.1699 -0.0610 198 ASN A CG +1564 O OD1 . ASN A 199 ? 1.8026 1.0916 1.0147 -0.2990 0.1700 -0.0611 198 ASN A OD1 +1565 N ND2 . ASN A 199 ? 2.2078 1.4966 1.4184 -0.3002 0.1694 -0.0609 198 ASN A ND2 +1566 N N . HIS A 200 ? 1.8754 1.1680 1.0957 -0.2918 0.1676 -0.0596 199 HIS A N +1567 C CA . HIS A 200 ? 1.9169 1.2103 1.1391 -0.2901 0.1671 -0.0593 199 HIS A CA +1568 C C . HIS A 200 ? 1.7940 1.0891 1.0168 -0.2891 0.1640 -0.0580 199 HIS A C +1569 O O . HIS A 200 ? 1.7885 1.0841 1.0101 -0.2898 0.1624 -0.0575 199 HIS A O +1570 C CB . HIS A 200 ? 1.6822 0.9756 0.9065 -0.2886 0.1684 -0.0597 199 HIS A CB +1571 C CG . HIS A 200 ? 1.6546 0.9490 0.8797 -0.2877 0.1670 -0.0591 199 HIS A CG +1572 N ND1 . HIS A 200 ? 1.7821 1.0759 1.0061 -0.2886 0.1674 -0.0593 199 HIS A ND1 +1573 C CD2 . HIS A 200 ? 1.8154 1.1112 1.0422 -0.2860 0.1651 -0.0583 199 HIS A CD2 +1574 C CE1 . HIS A 200 ? 1.8041 1.0988 1.0290 -0.2875 0.1659 -0.0587 199 HIS A CE1 +1575 N NE2 . HIS A 200 ? 1.8941 1.1902 1.1209 -0.2859 0.1645 -0.0580 199 HIS A NE2 +1576 N N . TYR A 201 ? 1.6714 0.9675 0.8960 -0.2875 0.1632 -0.0576 200 TYR A N +1577 C CA . TYR A 201 ? 1.6807 0.9784 0.9058 -0.2865 0.1603 -0.0564 200 TYR A CA +1578 C C . TYR A 201 ? 1.6145 0.9135 0.8421 -0.2844 0.1595 -0.0560 200 TYR A C +1579 O O . TYR A 201 ? 1.6522 0.9507 0.8811 -0.2837 0.1613 -0.0566 200 TYR A O +1580 C CB . TYR A 201 ? 1.6180 0.9158 0.8422 -0.2871 0.1594 -0.0561 200 TYR A CB +1581 C CG . TYR A 201 ? 1.8724 1.1699 1.0978 -0.2863 0.1605 -0.0564 200 TYR A CG +1582 C CD1 . TYR A 201 ? 1.7975 1.0934 1.0223 -0.2872 0.1632 -0.0575 200 TYR A CD1 +1583 C CD2 . TYR A 201 ? 1.8960 1.1949 1.1230 -0.2848 0.1589 -0.0557 200 TYR A CD2 +1584 C CE1 . TYR A 201 ? 1.7531 1.0488 0.9790 -0.2866 0.1642 -0.0579 200 TYR A CE1 +1585 C CE2 . TYR A 201 ? 2.0217 1.3203 1.2498 -0.2841 0.1599 -0.0560 200 TYR A CE2 +1586 C CZ . TYR A 201 ? 1.8311 1.1281 1.0586 -0.2850 0.1625 -0.0571 200 TYR A CZ +1587 O OH . TYR A 201 ? 1.7667 1.0634 0.9952 -0.2844 0.1635 -0.0575 200 TYR A OH +1588 N N . LEU A 202 ? 1.8031 1.1036 1.0314 -0.2834 0.1569 -0.0549 201 LEU A N +1589 C CA . LEU A 202 ? 1.8728 1.1747 1.1036 -0.2814 0.1560 -0.0545 201 LEU A CA +1590 C C . LEU A 202 ? 1.5974 0.9002 0.8287 -0.2807 0.1545 -0.0538 201 LEU A C +1591 O O . LEU A 202 ? 1.4123 0.7156 0.6425 -0.2813 0.1526 -0.0532 201 LEU A O +1592 C CB . LEU A 202 ? 1.3905 0.6934 0.6218 -0.2808 0.1542 -0.0538 201 LEU A CB +1593 C CG . LEU A 202 ? 1.7346 1.0368 0.9654 -0.2812 0.1552 -0.0542 201 LEU A CG +1594 C CD1 . LEU A 202 ? 1.5102 0.8137 0.7421 -0.2801 0.1533 -0.0535 201 LEU A CD1 +1595 C CD2 . LEU A 202 ? 1.9090 1.2100 1.1405 -0.2811 0.1580 -0.0553 201 LEU A CD2 +1596 N N . SER A 203 ? 1.5747 0.8777 0.8077 -0.2796 0.1553 -0.0540 202 SER A N +1597 C CA . SER A 203 ? 1.5720 0.8758 0.8056 -0.2789 0.1539 -0.0534 202 SER A CA +1598 C C . SER A 203 ? 1.3921 0.6976 0.6274 -0.2773 0.1517 -0.0526 202 SER A C +1599 O O . SER A 203 ? 1.7642 1.0702 1.0014 -0.2760 0.1524 -0.0527 202 SER A O +1600 C CB . SER A 203 ? 1.4948 0.7978 0.7292 -0.2786 0.1557 -0.0541 202 SER A CB +1601 O OG . SER A 203 ? 1.9291 1.2330 1.1640 -0.2779 0.1544 -0.0536 202 SER A OG +1602 N N . THR A 204 ? 1.6875 0.9940 0.9222 -0.2773 0.1493 -0.0516 203 THR A N +1603 C CA . THR A 204 ? 1.7914 1.0996 1.0277 -0.2758 0.1471 -0.0508 203 THR A CA +1604 C C . THR A 204 ? 1.6683 0.9775 0.9056 -0.2749 0.1456 -0.0502 203 THR A C +1605 O O . THR A 204 ? 1.6770 0.9858 0.9130 -0.2756 0.1453 -0.0500 203 THR A O +1606 C CB . THR A 204 ? 1.6858 0.9946 0.9210 -0.2764 0.1451 -0.0501 203 THR A CB +1607 O OG1 . THR A 204 ? 1.6449 0.9526 0.8790 -0.2775 0.1465 -0.0507 203 THR A OG1 +1608 C CG2 . THR A 204 ? 2.2460 1.5563 1.4829 -0.2748 0.1433 -0.0494 203 THR A CG2 +1609 N N . GLN A 205 ? 1.5653 0.8757 0.8047 -0.2732 0.1449 -0.0498 204 GLN A N +1610 C CA . GLN A 205 ? 1.5538 0.8655 0.7943 -0.2721 0.1431 -0.0490 204 GLN A CA +1611 C C . GLN A 205 ? 1.6048 0.9180 0.8467 -0.2708 0.1412 -0.0483 204 GLN A C +1612 O O . GLN A 205 ? 1.3414 0.6547 0.5843 -0.2702 0.1418 -0.0485 204 GLN A O +1613 C CB . GLN A 205 ? 1.6190 0.9304 0.8608 -0.2713 0.1445 -0.0495 204 GLN A CB +1614 C CG . GLN A 205 ? 1.5340 0.8438 0.7747 -0.2724 0.1468 -0.0504 204 GLN A CG +1615 C CD . GLN A 205 ? 1.8183 1.1276 1.0605 -0.2717 0.1490 -0.0512 204 GLN A CD +1616 O OE1 . GLN A 205 ? 2.3558 1.6655 1.5992 -0.2708 0.1491 -0.0512 204 GLN A OE1 +1617 N NE2 . GLN A 205 ? 1.7861 1.0946 1.0281 -0.2721 0.1508 -0.0519 204 GLN A NE2 +1618 N N . SER A 206 ? 1.5881 0.9024 0.8301 -0.2704 0.1388 -0.0474 205 SER A N +1619 C CA . SER A 206 ? 1.4196 0.7354 0.6627 -0.2693 0.1367 -0.0466 205 SER A CA +1620 C C . SER A 206 ? 1.2425 0.5594 0.4866 -0.2683 0.1350 -0.0459 205 SER A C +1621 O O . SER A 206 ? 1.6907 1.0072 0.9339 -0.2688 0.1348 -0.0458 205 SER A O +1622 C CB . SER A 206 ? 1.3736 0.6894 0.6151 -0.2703 0.1353 -0.0462 205 SER A CB +1623 O OG . SER A 206 ? 1.9138 1.2284 1.1542 -0.2714 0.1370 -0.0469 205 SER A OG +1624 N N . ASN A 207 ? 1.4157 0.7340 0.6616 -0.2669 0.1337 -0.0454 206 ASN A N +1625 C CA . ASN A 207 ? 1.4690 0.7885 0.7157 -0.2659 0.1316 -0.0446 206 ASN A CA +1626 C C . ASN A 207 ? 1.6640 0.9848 0.9114 -0.2653 0.1295 -0.0438 206 ASN A C +1627 O O . ASN A 207 ? 1.3985 0.7195 0.6465 -0.2650 0.1300 -0.0440 206 ASN A O +1628 C CB . ASN A 207 ? 1.2205 0.5405 0.4691 -0.2647 0.1323 -0.0447 206 ASN A CB +1629 C CG . ASN A 207 ? 1.4022 0.7239 0.6528 -0.2631 0.1307 -0.0441 206 ASN A CG +1630 O OD1 . ASN A 207 ? 1.3138 0.6360 0.5652 -0.2625 0.1303 -0.0439 206 ASN A OD1 +1631 N ND2 . ASN A 207 ? 1.2778 0.6000 0.5292 -0.2624 0.1299 -0.0437 206 ASN A ND2 +1632 N N . LEU A 208 ? 1.2932 0.6149 0.5404 -0.2651 0.1273 -0.0430 207 LEU A N +1633 C CA . LEU A 208 ? 1.1150 0.4379 0.3627 -0.2645 0.1251 -0.0423 207 LEU A CA +1634 C C . LEU A 208 ? 1.0639 0.3882 0.3134 -0.2630 0.1237 -0.0417 207 LEU A C +1635 O O . LEU A 208 ? 1.7143 1.0387 0.9639 -0.2628 0.1232 -0.0415 207 LEU A O +1636 C CB . LEU A 208 ? 1.2864 0.6091 0.5320 -0.2657 0.1234 -0.0418 207 LEU A CB +1637 C CG . LEU A 208 ? 1.3034 0.6246 0.5468 -0.2675 0.1247 -0.0423 207 LEU A CG +1638 C CD1 . LEU A 208 ? 1.4905 0.8117 0.7321 -0.2685 0.1227 -0.0418 207 LEU A CD1 +1639 C CD2 . LEU A 208 ? 1.3780 0.6985 0.6210 -0.2680 0.1258 -0.0428 207 LEU A CD2 +1640 N N . SER A 209 ? 1.4094 0.7346 0.6603 -0.2620 0.1230 -0.0414 208 SER A N +1641 C CA . SER A 209 ? 1.2465 0.5732 0.4994 -0.2605 0.1218 -0.0409 208 SER A CA +1642 C C . SER A 209 ? 1.5726 0.9004 0.8262 -0.2598 0.1198 -0.0402 208 SER A C +1643 O O . SER A 209 ? 1.3259 0.6534 0.5785 -0.2605 0.1194 -0.0402 208 SER A O +1644 C CB . SER A 209 ? 1.3348 0.6616 0.5896 -0.2594 0.1236 -0.0415 208 SER A CB +1645 O OG . SER A 209 ? 1.6147 0.9408 0.8695 -0.2597 0.1252 -0.0420 208 SER A OG +1646 N N . LYS A 210 ? 1.5435 0.8726 0.7987 -0.2586 0.1185 -0.0397 209 LYS A N +1647 C CA . LYS A 210 ? 1.2643 0.5945 0.5204 -0.2578 0.1167 -0.0391 209 LYS A CA +1648 C C . LYS A 210 ? 1.5102 0.8413 0.7686 -0.2563 0.1174 -0.0392 209 LYS A C +1649 O O . LYS A 210 ? 1.6956 1.0269 0.9551 -0.2555 0.1181 -0.0394 209 LYS A O +1650 C CB . LYS A 210 ? 1.6249 0.9560 0.8809 -0.2575 0.1144 -0.0382 209 LYS A CB +1651 C CG . LYS A 210 ? 1.4791 0.8095 0.7329 -0.2588 0.1133 -0.0380 209 LYS A CG +1652 C CD . LYS A 210 ? 1.5347 0.8648 0.7871 -0.2598 0.1126 -0.0379 209 LYS A CD +1653 C CE . LYS A 210 ? 1.3509 0.6805 0.6013 -0.2610 0.1112 -0.0375 209 LYS A CE +1654 N NZ . LYS A 210 ? 1.4157 0.7447 0.6645 -0.2623 0.1110 -0.0376 209 LYS A NZ +1655 N N . ASP A 211 ? 1.7091 1.0405 0.9679 -0.2561 0.1171 -0.0391 210 ASP A N +1656 C CA . ASP A 211 ? 1.3604 0.6928 0.6213 -0.2547 0.1169 -0.0390 210 ASP A CA +1657 C C . ASP A 211 ? 1.5316 0.8653 0.7933 -0.2538 0.1147 -0.0382 210 ASP A C +1658 O O . ASP A 211 ? 1.6892 1.0233 0.9501 -0.2542 0.1128 -0.0376 210 ASP A O +1659 C CB . ASP A 211 ? 1.4648 0.7971 0.7254 -0.2549 0.1168 -0.0391 210 ASP A CB +1660 C CG . ASP A 211 ? 1.8196 1.1528 1.0823 -0.2535 0.1171 -0.0391 210 ASP A CG +1661 O OD1 . ASP A 211 ? 1.7692 1.1033 1.0334 -0.2524 0.1167 -0.0388 210 ASP A OD1 +1662 O OD2 . ASP A 211 ? 1.6894 1.0222 0.9521 -0.2537 0.1177 -0.0393 210 ASP A OD2 +1663 N N . PRO A 212 ? 1.8264 1.1609 1.0899 -0.2526 0.1149 -0.0382 211 PRO A N +1664 C CA . PRO A 212 ? 1.7768 1.1125 1.0411 -0.2518 0.1129 -0.0374 211 PRO A CA +1665 C C . PRO A 212 ? 1.7922 1.1290 1.0577 -0.2509 0.1116 -0.0370 211 PRO A C +1666 O O . PRO A 212 ? 1.6018 0.9396 0.8681 -0.2502 0.1099 -0.0363 211 PRO A O +1667 C CB . PRO A 212 ? 1.7782 1.1142 1.0439 -0.2510 0.1138 -0.0376 211 PRO A CB +1668 C CG . PRO A 212 ? 1.8382 1.1735 1.1045 -0.2508 0.1162 -0.0385 211 PRO A CG +1669 C CD . PRO A 212 ? 1.5877 0.9219 0.8524 -0.2521 0.1171 -0.0389 211 PRO A CD +1670 N N . ASN A 213 ? 2.0722 1.4088 1.3379 -0.2510 0.1123 -0.0373 212 ASN A N +1671 C CA . ASN A 213 ? 2.2663 1.6038 1.5329 -0.2503 0.1110 -0.0368 212 ASN A CA +1672 C C . ASN A 213 ? 2.0442 1.3811 1.3092 -0.2513 0.1102 -0.0367 212 ASN A C +1673 O O . ASN A 213 ? 1.8464 1.1835 1.1117 -0.2511 0.1100 -0.0366 212 ASN A O +1674 C CB . ASN A 213 ? 1.9874 1.3242 1.2546 -0.2497 0.1126 -0.0373 212 ASN A CB +1675 C CG . ASN A 213 ? 1.8155 1.1518 1.0831 -0.2492 0.1140 -0.0377 212 ASN A CG +1676 O OD1 . ASN A 213 ? 1.6938 1.0302 0.9612 -0.2489 0.1132 -0.0373 212 ASN A OD1 +1677 N ND2 . ASN A 213 ? 1.9098 1.2456 1.1780 -0.2491 0.1162 -0.0384 212 ASN A ND2 +1678 N N . GLU A 214 ? 1.8574 1.1936 1.1206 -0.2525 0.1099 -0.0366 213 GLU A N +1679 C CA . GLU A 214 ? 1.5230 0.8586 0.7845 -0.2536 0.1092 -0.0365 213 GLU A CA +1680 C C . GLU A 214 ? 1.5259 0.8618 0.7864 -0.2541 0.1071 -0.0359 213 GLU A C +1681 O O . GLU A 214 ? 1.7386 1.0742 0.9985 -0.2545 0.1072 -0.0359 213 GLU A O +1682 C CB . GLU A 214 ? 1.5135 0.8477 0.7736 -0.2548 0.1111 -0.0372 213 GLU A CB +1683 C CG . GLU A 214 ? 1.4100 0.7434 0.6682 -0.2561 0.1104 -0.0371 213 GLU A CG +1684 C CD . GLU A 214 ? 1.8782 1.2122 1.1370 -0.2557 0.1095 -0.0369 213 GLU A CD +1685 O OE1 . GLU A 214 ? 1.6571 0.9905 0.9160 -0.2558 0.1109 -0.0374 213 GLU A OE1 +1686 O OE2 . GLU A 214 ? 2.1345 1.4693 1.3935 -0.2554 0.1073 -0.0362 213 GLU A OE2 +1687 N N . LYS A 215 ? 1.7027 1.0391 0.9629 -0.2542 0.1052 -0.0353 214 LYS A N +1688 C CA . LYS A 215 ? 1.8430 1.1798 1.1024 -0.2545 0.1030 -0.0346 214 LYS A CA +1689 C C . LYS A 215 ? 1.6802 1.0162 0.9375 -0.2560 0.1023 -0.0345 214 LYS A C +1690 O O . LYS A 215 ? 1.8528 1.1888 1.1089 -0.2566 0.1007 -0.0340 214 LYS A O +1691 C CB . LYS A 215 ? 1.5963 0.9345 0.8572 -0.2534 0.1012 -0.0339 214 LYS A CB +1692 C CG . LYS A 215 ? 2.1673 1.5064 1.4302 -0.2520 0.1017 -0.0339 214 LYS A CG +1693 C CD . LYS A 215 ? 2.2743 1.6137 1.5372 -0.2514 0.0998 -0.0333 214 LYS A CD +1694 C CE . LYS A 215 ? 2.2277 1.5668 1.4906 -0.2511 0.0998 -0.0333 214 LYS A CE +1695 N NZ . LYS A 215 ? 2.0587 1.3972 1.3223 -0.2504 0.1018 -0.0338 214 LYS A NZ +1696 N N . ARG A 216 ? 1.1805 0.5157 0.4370 -0.2567 0.1033 -0.0349 215 ARG A N +1697 C CA . ARG A 216 ? 1.4839 0.8181 0.7383 -0.2583 0.1030 -0.0350 215 ARG A CA +1698 C C . ARG A 216 ? 1.3486 0.6818 0.6016 -0.2593 0.1043 -0.0355 215 ARG A C +1699 O O . ARG A 216 ? 1.5609 0.8939 0.8147 -0.2588 0.1059 -0.0359 215 ARG A O +1700 C CB . ARG A 216 ? 1.4562 0.7898 0.7103 -0.2587 0.1039 -0.0354 215 ARG A CB +1701 C CG . ARG A 216 ? 1.7251 1.0595 0.9802 -0.2579 0.1025 -0.0349 215 ARG A CG +1702 C CD . ARG A 216 ? 1.5472 0.8810 0.8025 -0.2580 0.1039 -0.0354 215 ARG A CD +1703 N NE . ARG A 216 ? 1.9374 1.2713 1.1942 -0.2570 0.1059 -0.0359 215 ARG A NE +1704 C CZ . ARG A 216 ? 1.8183 1.1517 1.0755 -0.2569 0.1074 -0.0364 215 ARG A CZ +1705 N NH1 . ARG A 216 ? 1.7146 1.0475 0.9710 -0.2576 0.1072 -0.0365 215 ARG A NH1 +1706 N NH2 . ARG A 216 ? 1.4384 0.7719 0.6970 -0.2560 0.1091 -0.0369 215 ARG A NH2 +1707 N N . ASP A 217 ? 1.4283 0.7607 0.6792 -0.2607 0.1037 -0.0354 216 ASP A N +1708 C CA . ASP A 217 ? 1.6460 0.9773 0.8955 -0.2618 0.1049 -0.0358 216 ASP A CA +1709 C C . ASP A 217 ? 1.7383 1.0686 0.9876 -0.2621 0.1075 -0.0367 216 ASP A C +1710 O O . ASP A 217 ? 1.6031 0.9328 0.8518 -0.2627 0.1080 -0.0370 216 ASP A O +1711 C CB . ASP A 217 ? 1.4807 0.8113 0.7278 -0.2633 0.1036 -0.0356 216 ASP A CB +1712 C CG . ASP A 217 ? 1.9062 1.2362 1.1521 -0.2641 0.1038 -0.0357 216 ASP A CG +1713 O OD1 . ASP A 217 ? 2.0485 1.3788 1.2954 -0.2633 0.1046 -0.0357 216 ASP A OD1 +1714 O OD2 . ASP A 217 ? 1.4028 0.7320 0.6467 -0.2655 0.1033 -0.0356 216 ASP A OD2 +1715 N N . HIS A 218 ? 1.6959 1.0260 0.9459 -0.2618 0.1091 -0.0372 217 HIS A N +1716 C CA . HIS A 218 ? 1.5416 0.8709 0.7918 -0.2618 0.1116 -0.0380 217 HIS A CA +1717 C C . HIS A 218 ? 1.3040 0.6325 0.5537 -0.2622 0.1133 -0.0385 217 HIS A C +1718 O O . HIS A 218 ? 1.6249 0.9537 0.8747 -0.2620 0.1128 -0.0383 217 HIS A O +1719 C CB . HIS A 218 ? 1.3647 0.6948 0.6172 -0.2603 0.1121 -0.0381 217 HIS A CB +1720 C CG . HIS A 218 ? 1.2794 0.6103 0.5335 -0.2591 0.1123 -0.0380 217 HIS A CG +1721 N ND1 . HIS A 218 ? 1.9024 1.2342 1.1569 -0.2585 0.1104 -0.0373 217 HIS A ND1 +1722 C CD2 . HIS A 218 ? 1.6180 0.9488 0.8733 -0.2584 0.1141 -0.0385 217 HIS A CD2 +1723 C CE1 . HIS A 218 ? 1.5618 0.8941 0.8177 -0.2575 0.1111 -0.0374 217 HIS A CE1 +1724 N NE2 . HIS A 218 ? 1.7136 1.0453 0.9701 -0.2574 0.1133 -0.0381 217 HIS A NE2 +1725 N N . MET A 219 ? 1.4932 0.8206 0.7423 -0.2629 0.1155 -0.0393 218 MET A N +1726 C CA . MET A 219 ? 1.3872 0.7137 0.6361 -0.2631 0.1175 -0.0399 218 MET A CA +1727 C C . MET A 219 ? 1.4668 0.7930 0.7171 -0.2625 0.1197 -0.0406 218 MET A C +1728 O O . MET A 219 ? 1.4803 0.8061 0.7304 -0.2627 0.1204 -0.0409 218 MET A O +1729 C CB . MET A 219 ? 1.2980 0.6232 0.5445 -0.2649 0.1181 -0.0403 218 MET A CB +1730 C CG . MET A 219 ? 1.1524 0.4766 0.3985 -0.2654 0.1203 -0.0410 218 MET A CG +1731 S SD . MET A 219 ? 1.4458 0.7683 0.6890 -0.2675 0.1211 -0.0414 218 MET A SD +1732 C CE . MET A 219 ? 1.4466 0.7685 0.6893 -0.2681 0.1220 -0.0419 218 MET A CE +1733 N N . VAL A 220 ? 1.5249 0.8513 0.7764 -0.2616 0.1208 -0.0409 219 VAL A N +1734 C CA . VAL A 220 ? 1.3615 0.6873 0.6139 -0.2613 0.1232 -0.0416 219 VAL A CA +1735 C C . VAL A 220 ? 1.1771 0.5015 0.4281 -0.2625 0.1251 -0.0423 219 VAL A C +1736 O O . VAL A 220 ? 1.5676 0.8918 0.8182 -0.2627 0.1251 -0.0423 219 VAL A O +1737 C CB . VAL A 220 ? 1.3914 0.7181 0.6460 -0.2598 0.1236 -0.0416 219 VAL A CB +1738 C CG1 . VAL A 220 ? 1.1556 0.4818 0.4112 -0.2593 0.1258 -0.0423 219 VAL A CG1 +1739 C CG2 . VAL A 220 ? 1.5409 0.8691 0.7969 -0.2586 0.1214 -0.0408 219 VAL A CG2 +1740 N N . LEU A 221 ? 1.5839 0.9072 0.8339 -0.2633 0.1266 -0.0429 220 LEU A N +1741 C CA . LEU A 221 ? 1.4873 0.8090 0.7357 -0.2646 0.1285 -0.0437 220 LEU A CA +1742 C C . LEU A 221 ? 1.3925 0.7135 0.6418 -0.2643 0.1311 -0.0445 220 LEU A C +1743 O O . LEU A 221 ? 1.5838 0.9045 0.8335 -0.2641 0.1320 -0.0448 220 LEU A O +1744 C CB . LEU A 221 ? 1.3168 0.6377 0.5633 -0.2661 0.1284 -0.0438 220 LEU A CB +1745 C CG . LEU A 221 ? 1.3009 0.6202 0.5457 -0.2675 0.1305 -0.0446 220 LEU A CG +1746 C CD1 . LEU A 221 ? 1.4018 0.7208 0.6457 -0.2681 0.1304 -0.0445 220 LEU A CD1 +1747 C CD2 . LEU A 221 ? 1.4642 0.7827 0.7073 -0.2688 0.1306 -0.0448 220 LEU A CD2 +1748 N N . LEU A 222 ? 2.0496 1.3701 1.2990 -0.2644 0.1324 -0.0449 221 LEU A N +1749 C CA . LEU A 222 ? 1.3326 0.6521 0.5824 -0.2644 0.1350 -0.0458 221 LEU A CA +1750 C C . LEU A 222 ? 1.6324 0.9504 0.8803 -0.2660 0.1365 -0.0464 221 LEU A C +1751 O O . LEU A 222 ? 1.5650 0.8827 0.8120 -0.2666 0.1362 -0.0463 221 LEU A O +1752 C CB . LEU A 222 ? 1.4007 0.7207 0.6522 -0.2633 0.1356 -0.0459 221 LEU A CB +1753 C CG . LEU A 222 ? 1.6590 0.9804 0.9128 -0.2616 0.1346 -0.0455 221 LEU A CG +1754 C CD1 . LEU A 222 ? 1.1963 0.5181 0.4514 -0.2607 0.1351 -0.0456 221 LEU A CD1 +1755 C CD2 . LEU A 222 ? 1.4939 0.8150 0.7484 -0.2612 0.1358 -0.0459 221 LEU A CD2 +1756 N N . GLU A 223 ? 1.5068 0.8236 0.7540 -0.2667 0.1382 -0.0471 222 GLU A N +1757 C CA . GLU A 223 ? 1.6458 0.9611 0.8912 -0.2682 0.1400 -0.0478 222 GLU A CA +1758 C C . GLU A 223 ? 1.4826 0.7969 0.7288 -0.2680 0.1427 -0.0488 222 GLU A C +1759 O O . GLU A 223 ? 1.5529 0.8673 0.8004 -0.2672 0.1436 -0.0490 222 GLU A O +1760 C CB . GLU A 223 ? 1.4392 0.7538 0.6831 -0.2693 0.1399 -0.0479 222 GLU A CB +1761 C CG . GLU A 223 ? 2.1322 1.4467 1.3741 -0.2706 0.1384 -0.0475 222 GLU A CG +1762 C CD . GLU A 223 ? 2.5455 1.8592 1.7857 -0.2718 0.1385 -0.0477 222 GLU A CD +1763 O OE1 . GLU A 223 ? 2.4681 1.7809 1.7082 -0.2722 0.1405 -0.0484 222 GLU A OE1 +1764 O OE2 . GLU A 223 ? 2.5072 1.8213 1.7462 -0.2725 0.1367 -0.0471 222 GLU A OE2 +1765 N N . PHE A 224 ? 1.6252 0.9384 0.8703 -0.2689 0.1441 -0.0493 223 PHE A N +1766 C CA . PHE A 224 ? 1.4274 0.7393 0.6727 -0.2692 0.1469 -0.0503 223 PHE A CA +1767 C C . PHE A 224 ? 1.2636 0.5740 0.5066 -0.2710 0.1481 -0.0509 223 PHE A C +1768 O O . PHE A 224 ? 1.7034 1.0136 0.9448 -0.2720 0.1472 -0.0506 223 PHE A O +1769 C CB . PHE A 224 ? 1.4326 0.7444 0.6785 -0.2689 0.1477 -0.0506 223 PHE A CB +1770 C CG . PHE A 224 ? 1.5556 0.8688 0.8036 -0.2672 0.1465 -0.0500 223 PHE A CG +1771 C CD1 . PHE A 224 ? 1.3730 0.6873 0.6225 -0.2660 0.1455 -0.0496 223 PHE A CD1 +1772 C CD2 . PHE A 224 ? 1.3654 0.6788 0.6139 -0.2669 0.1465 -0.0500 223 PHE A CD2 +1773 C CE1 . PHE A 224 ? 1.3858 0.7014 0.6372 -0.2645 0.1445 -0.0491 223 PHE A CE1 +1774 C CE2 . PHE A 224 ? 1.5930 0.9076 0.8433 -0.2654 0.1454 -0.0495 223 PHE A CE2 +1775 C CZ . PHE A 224 ? 1.7005 1.0163 0.9523 -0.2642 0.1444 -0.0491 223 PHE A CZ +1776 N N . VAL A 225 ? 1.6006 0.9100 0.8436 -0.2714 0.1500 -0.0516 224 VAL A N +1777 C CA . VAL A 225 ? 1.5999 0.9078 0.8407 -0.2731 0.1513 -0.0522 224 VAL A CA +1778 C C . VAL A 225 ? 1.7630 1.0694 1.0038 -0.2735 0.1543 -0.0533 224 VAL A C +1779 O O . VAL A 225 ? 1.6460 0.9523 0.8881 -0.2727 0.1553 -0.0536 224 VAL A O +1780 C CB . VAL A 225 ? 1.4413 0.7492 0.6812 -0.2736 0.1504 -0.0519 224 VAL A CB +1781 C CG1 . VAL A 225 ? 1.5692 0.8760 0.8068 -0.2755 0.1510 -0.0523 224 VAL A CG1 +1782 C CG2 . VAL A 225 ? 1.5762 0.8858 0.8165 -0.2729 0.1475 -0.0508 224 VAL A CG2 +1783 N N . THR A 226 ? 1.5618 0.8670 0.8012 -0.2748 0.1557 -0.0539 225 THR A N +1784 C CA . THR A 226 ? 1.7010 1.0046 0.9403 -0.2754 0.1586 -0.0550 225 THR A CA +1785 C C . THR A 226 ? 1.6998 1.0019 0.9367 -0.2773 0.1598 -0.0556 225 THR A C +1786 O O . THR A 226 ? 1.5670 0.8690 0.8024 -0.2783 0.1590 -0.0554 225 THR A O +1787 C CB . THR A 226 ? 1.5990 0.9023 0.8393 -0.2749 0.1598 -0.0555 225 THR A CB +1788 O OG1 . THR A 226 ? 1.4218 0.7271 0.6654 -0.2729 0.1584 -0.0550 225 THR A OG1 +1789 C CG2 . THR A 226 ? 1.8436 1.1471 1.0878 -0.2745 0.1618 -0.0569 225 THR A CG2 +1790 N N . ALA A 227 ? 1.6142 0.9151 0.8507 -0.2779 0.1617 -0.0564 226 ALA A N +1791 C CA . ALA A 227 ? 1.5533 0.8527 0.7876 -0.2798 0.1632 -0.0571 226 ALA A CA +1792 C C . ALA A 227 ? 1.6805 0.9786 0.9145 -0.2804 0.1654 -0.0580 226 ALA A C +1793 O O . ALA A 227 ? 1.8730 1.1726 1.1119 -0.2787 0.1657 -0.0586 226 ALA A O +1794 C CB . ALA A 227 ? 1.6002 0.8988 0.8342 -0.2802 0.1645 -0.0576 226 ALA A CB +1795 N N . ALA A 228 ? 1.4768 0.7739 0.7088 -0.2821 0.1660 -0.0583 227 ALA A N +1796 C CA . ALA A 228 ? 1.7654 1.0614 0.9971 -0.2828 0.1677 -0.0591 227 ALA A CA +1797 C C . ALA A 228 ? 1.8961 1.1907 1.1252 -0.2849 0.1688 -0.0596 227 ALA A C +1798 O O . ALA A 228 ? 1.7804 1.0748 1.0084 -0.2857 0.1687 -0.0596 227 ALA A O +1799 C CB . ALA A 228 ? 1.4992 0.7961 0.7312 -0.2822 0.1662 -0.0584 227 ALA A CB +1800 N N . GLY A 229 ? 1.8825 1.1762 1.1107 -0.2858 0.1699 -0.0601 228 GLY A N +1801 C CA . GLY A 229 ? 1.9735 1.2659 1.1992 -0.2879 0.1706 -0.0605 228 GLY A CA +1802 C C . GLY A 229 ? 2.0897 1.3805 1.3145 -0.2892 0.1733 -0.0617 228 GLY A C +1803 O O . GLY A 229 ? 2.1476 1.4373 1.3703 -0.2910 0.1740 -0.0621 228 GLY A O +1804 N N . ILE A 230 ? 2.0088 1.3006 1.2378 -0.2877 0.1739 -0.0625 229 ILE A N +1805 C CA . ILE A 230 ? 2.1275 1.4188 1.3587 -0.2880 0.1759 -0.0640 229 ILE A CA +1806 C C . ILE A 230 ? 3.0991 2.3920 2.3364 -0.2862 0.1764 -0.0653 229 ILE A C +1807 O O . ILE A 230 ? 3.4859 2.7805 2.7268 -0.2841 0.1753 -0.0651 229 ILE A O +1808 C CB . ILE A 230 ? 2.1149 1.4064 1.3471 -0.2876 0.1762 -0.0641 229 ILE A CB +1809 C CG1 . ILE A 230 ? 2.0896 1.3795 1.3159 -0.2897 0.1760 -0.0632 229 ILE A CG1 +1810 C CG2 . ILE A 230 ? 2.3673 1.6589 1.6034 -0.2873 0.1782 -0.0659 229 ILE A CG2 +1811 C CD1 . ILE A 230 ? 1.9661 1.2560 1.1931 -0.2895 0.1764 -0.0634 229 ILE A CD1 +1812 N N . THR A 231 ? 3.3585 2.6509 2.5969 -0.2869 0.1779 -0.0667 230 THR A N +1813 C CA . THR A 231 ? 3.5369 2.8308 2.7809 -0.2852 0.1783 -0.0681 230 THR A CA +1814 C C . THR A 231 ? 3.6031 2.8988 2.8528 -0.2827 0.1781 -0.0687 230 THR A C +1815 O O . THR A 231 ? 3.3088 2.6051 2.5626 -0.2820 0.1794 -0.0703 230 THR A O +1816 C CB . THR A 231 ? 3.2315 2.5246 2.4762 -0.2862 0.1801 -0.0699 230 THR A CB +1817 O OG1 . THR A 231 ? 3.1595 2.4542 2.4101 -0.2843 0.1804 -0.0714 230 THR A OG1 +1818 C CG2 . THR A 231 ? 3.0731 2.3651 2.3170 -0.2874 0.1817 -0.0706 230 THR A CG2 +1819 N N . ALA A 235 ? 1.9977 1.8058 1.4948 0.2465 -0.0754 0.0400 1054 ALA A N +1820 C CA . ALA A 235 ? 2.3342 2.1466 1.8291 0.2469 -0.0805 0.0392 1054 ALA A CA +1821 C C . ALA A 235 ? 2.4778 2.2978 1.9707 0.2451 -0.0797 0.0355 1054 ALA A C +1822 O O . ALA A 235 ? 2.0744 1.8969 1.5660 0.2444 -0.0761 0.0316 1054 ALA A O +1823 C CB . ALA A 235 ? 1.9751 1.7846 1.4745 0.2459 -0.0821 0.0464 1054 ALA A CB +1824 N N . SER A 236 ? 2.6481 2.4717 2.1408 0.2445 -0.0831 0.0367 1055 SER A N +1825 C CA . SER A 236 ? 2.8320 2.6627 2.3235 0.2425 -0.0825 0.0341 1055 SER A CA +1826 C C . SER A 236 ? 3.0542 2.8846 2.5515 0.2393 -0.0782 0.0398 1055 SER A C +1827 O O . SER A 236 ? 2.6446 2.4801 2.1421 0.2371 -0.0761 0.0385 1055 SER A O +1828 C CB . SER A 236 ? 2.4873 2.3223 1.9757 0.2435 -0.0884 0.0324 1055 SER A CB +1829 O OG . SER A 236 ? 2.0852 1.9272 1.5717 0.2419 -0.0879 0.0290 1055 SER A OG +1830 N N . THR A 237 ? 3.2510 3.0752 2.7530 0.2390 -0.0769 0.0460 1056 THR A N +1831 C CA . THR A 237 ? 2.9309 2.7536 2.4388 0.2360 -0.0725 0.0519 1056 THR A CA +1832 C C . THR A 237 ? 2.4628 2.2866 1.9714 0.2344 -0.0665 0.0497 1056 THR A C +1833 O O . THR A 237 ? 1.9334 1.7587 1.4456 0.2317 -0.0627 0.0525 1056 THR A O +1834 C CB . THR A 237 ? 2.3789 2.1941 1.8914 0.2364 -0.0722 0.0585 1056 THR A CB +1835 O OG1 . THR A 237 ? 2.2057 2.0161 1.7181 0.2376 -0.0696 0.0576 1056 THR A OG1 +1836 C CG2 . THR A 237 ? 2.1546 1.9684 1.6657 0.2384 -0.0783 0.0600 1056 THR A CG2 +1837 N N . LYS A 238 ? 2.8089 2.6322 2.3140 0.2362 -0.0658 0.0446 1057 LYS A N +1838 C CA . LYS A 238 ? 2.6762 2.5012 2.1810 0.2351 -0.0607 0.0414 1057 LYS A CA +1839 C C . LYS A 238 ? 2.3084 2.1408 1.8119 0.2331 -0.0599 0.0386 1057 LYS A C +1840 O O . LYS A 238 ? 1.8336 1.6671 1.3405 0.2304 -0.0554 0.0409 1057 LYS A O +1841 C CB . LYS A 238 ? 2.4933 2.3175 1.9934 0.2377 -0.0613 0.0354 1057 LYS A CB +1842 C CG . LYS A 238 ? 2.3597 2.1768 1.8618 0.2388 -0.0589 0.0375 1057 LYS A CG +1843 C CD . LYS A 238 ? 2.1398 1.9514 1.6442 0.2400 -0.0621 0.0427 1057 LYS A CD +1844 C CE . LYS A 238 ? 1.9033 1.7081 1.4085 0.2417 -0.0606 0.0437 1057 LYS A CE +1845 N NZ . LYS A 238 ? 1.8719 1.6709 1.3800 0.2427 -0.0633 0.0494 1057 LYS A NZ +1846 N N . LYS A 239 ? 2.5551 2.3924 2.0537 0.2344 -0.0643 0.0338 1058 LYS A N +1847 C CA . LYS A 239 ? 2.7251 2.5698 2.2215 0.2329 -0.0641 0.0301 1058 LYS A CA +1848 C C . LYS A 239 ? 2.5240 2.3708 2.0246 0.2298 -0.0626 0.0350 1058 LYS A C +1849 O O . LYS A 239 ? 2.2469 2.0989 1.7472 0.2279 -0.0603 0.0330 1058 LYS A O +1850 C CB . LYS A 239 ? 2.8409 2.6897 2.3316 0.2350 -0.0700 0.0250 1058 LYS A CB +1851 C CG . LYS A 239 ? 2.5242 2.3713 2.0103 0.2381 -0.0721 0.0199 1058 LYS A CG +1852 C CD . LYS A 239 ? 2.5092 2.3612 1.9896 0.2400 -0.0776 0.0146 1058 LYS A CD +1853 C CE . LYS A 239 ? 2.4185 2.2780 1.8972 0.2381 -0.0767 0.0111 1058 LYS A CE +1854 N NZ . LYS A 239 ? 1.9680 1.8326 1.4419 0.2395 -0.0822 0.0069 1058 LYS A NZ +1855 N N . LEU A 240 ? 2.3578 2.2005 1.8624 0.2295 -0.0639 0.0414 1059 LEU A N +1856 C CA . LEU A 240 ? 2.4828 2.3270 1.9916 0.2268 -0.0629 0.0466 1059 LEU A CA +1857 C C . LEU A 240 ? 2.4045 2.2472 1.9181 0.2241 -0.0565 0.0500 1059 LEU A C +1858 O O . LEU A 240 ? 1.5533 1.4004 1.0683 0.2216 -0.0542 0.0504 1059 LEU A O +1859 C CB . LEU A 240 ? 2.6297 2.4696 2.1411 0.2275 -0.0664 0.0523 1059 LEU A CB +1860 C CG . LEU A 240 ? 2.3822 2.2221 1.8988 0.2248 -0.0652 0.0587 1059 LEU A CG +1861 C CD1 . LEU A 240 ? 2.2556 2.1028 1.7705 0.2234 -0.0667 0.0565 1059 LEU A CD1 +1862 C CD2 . LEU A 240 ? 2.0906 1.9256 1.6096 0.2258 -0.0686 0.0642 1059 LEU A CD2 +1863 N N . SER A 241 ? 2.7696 2.6061 2.2859 0.2245 -0.0537 0.0527 1060 SER A N +1864 C CA . SER A 241 ? 2.4691 2.3032 1.9902 0.2221 -0.0476 0.0564 1060 SER A CA +1865 C C . SER A 241 ? 2.0834 1.9212 1.6027 0.2212 -0.0434 0.0515 1060 SER A C +1866 O O . SER A 241 ? 1.9358 1.7734 1.4587 0.2188 -0.0383 0.0538 1060 SER A O +1867 C CB . SER A 241 ? 1.8117 1.6380 1.3359 0.2231 -0.0461 0.0604 1060 SER A CB +1868 O OG . SER A 241 ? 1.7616 1.5863 1.2825 0.2252 -0.0455 0.0557 1060 SER A OG +1869 N N . GLU A 242 ? 2.0388 1.8798 1.5524 0.2231 -0.0456 0.0446 1061 GLU A N +1870 C CA . GLU A 242 ? 2.4344 2.2798 1.9458 0.2222 -0.0421 0.0394 1061 GLU A CA +1871 C C . GLU A 242 ? 2.2147 2.0661 1.7270 0.2195 -0.0410 0.0395 1061 GLU A C +1872 O O . GLU A 242 ? 1.6350 1.4886 1.1484 0.2175 -0.0363 0.0385 1061 GLU A O +1873 C CB . GLU A 242 ? 2.5384 2.3863 2.0434 0.2249 -0.0452 0.0319 1061 GLU A CB +1874 C CG . GLU A 242 ? 2.5546 2.3970 2.0579 0.2279 -0.0475 0.0313 1061 GLU A CG +1875 C CD . GLU A 242 ? 2.6442 2.4804 2.1510 0.2277 -0.0429 0.0342 1061 GLU A CD +1876 O OE1 . GLU A 242 ? 2.6999 2.5368 2.2090 0.2256 -0.0376 0.0345 1061 GLU A OE1 +1877 O OE2 . GLU A 242 ? 2.4844 2.3151 1.9917 0.2296 -0.0446 0.0361 1061 GLU A OE2 +1878 N N . SER A 243 ? 2.4417 2.2955 1.9534 0.2195 -0.0453 0.0409 1062 SER A N +1879 C CA . SER A 243 ? 2.7205 2.5801 2.2330 0.2171 -0.0450 0.0413 1062 SER A CA +1880 C C . SER A 243 ? 2.4703 2.3276 1.9892 0.2143 -0.0414 0.0484 1062 SER A C +1881 O O . SER A 243 ? 1.8579 1.7182 1.3786 0.2117 -0.0374 0.0487 1062 SER A O +1882 C CB . SER A 243 ? 2.7761 2.6392 2.2856 0.2182 -0.0511 0.0401 1062 SER A CB +1883 O OG . SER A 243 ? 2.6973 2.5632 2.2008 0.2206 -0.0543 0.0332 1062 SER A OG +1884 N N . LEU A 244 ? 2.2989 2.1506 1.8211 0.2147 -0.0427 0.0542 1063 LEU A N +1885 C CA . LEU A 244 ? 2.0307 1.8794 1.5592 0.2123 -0.0393 0.0612 1063 LEU A CA +1886 C C . LEU A 244 ? 2.2030 2.0502 1.7338 0.2107 -0.0329 0.0614 1063 LEU A C +1887 O O . LEU A 244 ? 1.8627 1.7110 1.3974 0.2079 -0.0291 0.0646 1063 LEU A O +1888 C CB . LEU A 244 ? 1.7450 1.5870 1.2763 0.2135 -0.0414 0.0667 1063 LEU A CB +1889 C CG . LEU A 244 ? 2.0724 1.9155 1.6041 0.2137 -0.0464 0.0696 1063 LEU A CG +1890 C CD1 . LEU A 244 ? 1.9702 1.8064 1.5052 0.2147 -0.0478 0.0755 1063 LEU A CD1 +1891 C CD2 . LEU A 244 ? 1.7089 1.5563 1.2431 0.2107 -0.0449 0.0721 1063 LEU A CD2 +1892 N N . LYS A 245 ? 2.3790 2.2238 1.9077 0.2125 -0.0317 0.0578 1064 LYS A N +1893 C CA . LYS A 245 ? 2.2824 2.1265 1.8122 0.2113 -0.0259 0.0566 1064 LYS A CA +1894 C C . LYS A 245 ? 2.3935 2.2442 1.9225 0.2090 -0.0233 0.0536 1064 LYS A C +1895 O O . LYS A 245 ? 2.4625 2.3133 1.9956 0.2063 -0.0191 0.0573 1064 LYS A O +1896 C CB . LYS A 245 ? 1.9360 1.7782 1.4620 0.2139 -0.0261 0.0515 1064 LYS A CB +1897 C CG . LYS A 245 ? 2.2852 2.1197 1.8137 0.2153 -0.0252 0.0550 1064 LYS A CG +1898 C CD . LYS A 245 ? 2.7089 2.5420 2.2331 0.2179 -0.0256 0.0494 1064 LYS A CD +1899 C CE . LYS A 245 ? 2.5119 2.3373 2.0386 0.2191 -0.0241 0.0528 1064 LYS A CE +1900 N NZ . LYS A 245 ? 1.8261 1.6502 1.3490 0.2214 -0.0239 0.0475 1064 LYS A NZ +1901 N N . ARG A 246 ? 2.2788 2.1351 1.8025 0.2101 -0.0258 0.0472 1065 ARG A N +1902 C CA . ARG A 246 ? 2.4338 2.2963 1.9562 0.2081 -0.0233 0.0437 1065 ARG A CA +1903 C C . ARG A 246 ? 2.2958 2.1614 1.8214 0.2053 -0.0228 0.0478 1065 ARG A C +1904 O O . ARG A 246 ? 2.1425 2.0108 1.6699 0.2028 -0.0185 0.0479 1065 ARG A O +1905 C CB . ARG A 246 ? 2.3542 2.2221 1.8701 0.2098 -0.0264 0.0359 1065 ARG A CB +1906 C CG . ARG A 246 ? 2.5557 2.4217 2.0682 0.2121 -0.0256 0.0310 1065 ARG A CG +1907 C CD . ARG A 246 ? 2.7830 2.6549 2.2893 0.2136 -0.0287 0.0234 1065 ARG A CD +1908 N NE . ARG A 246 ? 3.0313 2.9015 2.5341 0.2159 -0.0284 0.0185 1065 ARG A NE +1909 C CZ . ARG A 246 ? 2.7574 2.6315 2.2545 0.2177 -0.0311 0.0117 1065 ARG A CZ +1910 N NH1 . ARG A 246 ? 2.5562 2.4362 2.0503 0.2175 -0.0344 0.0089 1065 ARG A NH1 +1911 N NH2 . ARG A 246 ? 2.1755 2.0475 1.6698 0.2197 -0.0305 0.0077 1065 ARG A NH2 +1912 N N . ILE A 247 ? 2.0094 1.8744 1.5360 0.2057 -0.0271 0.0512 1066 ILE A N +1913 C CA . ILE A 247 ? 2.1181 1.9860 1.6476 0.2032 -0.0271 0.0551 1066 ILE A CA +1914 C C . ILE A 247 ? 2.1547 2.0191 1.6905 0.2006 -0.0219 0.0614 1066 ILE A C +1915 O O . ILE A 247 ? 1.7182 1.5859 1.2560 0.1980 -0.0192 0.0627 1066 ILE A O +1916 C CB . ILE A 247 ? 2.2044 2.0722 1.7333 0.2044 -0.0331 0.0573 1066 ILE A CB +1917 C CG1 . ILE A 247 ? 2.6339 2.5066 2.1565 0.2065 -0.0380 0.0508 1066 ILE A CG1 +1918 C CG2 . ILE A 247 ? 1.6584 1.5279 1.1913 0.2018 -0.0327 0.0625 1066 ILE A CG2 +1919 C CD1 . ILE A 247 ? 2.8260 2.6981 2.3472 0.2083 -0.0442 0.0521 1066 ILE A CD1 +1920 N N . GLY A 248 ? 2.2679 2.1254 1.8065 0.2014 -0.0205 0.0652 1067 GLY A N +1921 C CA . GLY A 248 ? 1.9559 1.8097 1.5004 0.1992 -0.0154 0.0708 1067 GLY A CA +1922 C C . GLY A 248 ? 2.1628 2.0175 1.7071 0.1981 -0.0100 0.0678 1067 GLY A C +1923 O O . GLY A 248 ? 1.9483 1.8020 1.4969 0.1957 -0.0051 0.0712 1067 GLY A O +1924 N N . ASP A 249 ? 2.3939 2.2505 1.9332 0.2000 -0.0108 0.0612 1068 ASP A N +1925 C CA . ASP A 249 ? 2.2842 2.1418 1.8227 0.1994 -0.0059 0.0575 1068 ASP A CA +1926 C C . ASP A 249 ? 2.2407 2.1050 1.7785 0.1970 -0.0037 0.0549 1068 ASP A C +1927 O O . ASP A 249 ? 1.7998 1.6640 1.3410 0.1946 0.0014 0.0570 1068 ASP A O +1928 C CB . ASP A 249 ? 2.3209 2.1780 1.8544 0.2023 -0.0077 0.0514 1068 ASP A CB +1929 C CG . ASP A 249 ? 2.5628 2.4126 2.0979 0.2040 -0.0071 0.0539 1068 ASP A CG +1930 O OD1 . ASP A 249 ? 2.6441 2.4891 2.1839 0.2033 -0.0065 0.0604 1068 ASP A OD1 +1931 O OD2 . ASP A 249 ? 2.4394 2.2881 1.9712 0.2061 -0.0073 0.0494 1068 ASP A OD2 +1932 N N . GLU A 250 ? 2.5190 2.3891 2.0523 0.1978 -0.0075 0.0503 1069 GLU A N +1933 C CA . GLU A 250 ? 2.5888 2.4657 2.1211 0.1956 -0.0061 0.0477 1069 GLU A CA +1934 C C . GLU A 250 ? 2.3663 2.2431 1.9039 0.1926 -0.0036 0.0539 1069 GLU A C +1935 O O . GLU A 250 ? 1.7225 1.6025 1.2616 0.1902 0.0004 0.0536 1069 GLU A O +1936 C CB . GLU A 250 ? 2.3854 2.2678 1.9128 0.1969 -0.0116 0.0433 1069 GLU A CB +1937 C CG . GLU A 250 ? 2.7022 2.5853 2.2238 0.1999 -0.0146 0.0368 1069 GLU A CG +1938 C CD . GLU A 250 ? 2.7262 2.6131 2.2436 0.2016 -0.0208 0.0339 1069 GLU A CD +1939 O OE1 . GLU A 250 ? 2.4360 2.3255 1.9548 0.2002 -0.0227 0.0366 1069 GLU A OE1 +1940 O OE2 . GLU A 250 ? 2.5059 2.3932 2.0187 0.2042 -0.0239 0.0289 1069 GLU A OE2 +1941 N N . LEU A 251 ? 2.2312 2.1042 1.7718 0.1928 -0.0060 0.0595 1070 LEU A N +1942 C CA . LEU A 251 ? 1.9904 1.8624 1.5365 0.1902 -0.0040 0.0661 1070 LEU A CA +1943 C C . LEU A 251 ? 2.1232 1.9918 1.6738 0.1882 0.0024 0.0693 1070 LEU A C +1944 O O . LEU A 251 ? 1.5024 1.3738 1.0553 0.1855 0.0061 0.0705 1070 LEU A O +1945 C CB . LEU A 251 ? 2.0135 1.8811 1.5616 0.1913 -0.0080 0.0713 1070 LEU A CB +1946 C CG . LEU A 251 ? 2.1506 2.0170 1.7039 0.1891 -0.0075 0.0783 1070 LEU A CG +1947 C CD1 . LEU A 251 ? 2.0070 1.8797 1.5607 0.1864 -0.0062 0.0778 1070 LEU A CD1 +1948 C CD2 . LEU A 251 ? 1.6984 1.5625 1.2517 0.1907 -0.0131 0.0813 1070 LEU A CD2 +1949 N N . ASP A 252 ? 2.3559 2.2185 1.9078 0.1896 0.0039 0.0707 1071 ASP A N +1950 C CA . ASP A 252 ? 2.0854 1.9444 1.6417 0.1878 0.0098 0.0741 1071 ASP A CA +1951 C C . ASP A 252 ? 2.0915 1.9539 1.6459 0.1869 0.0141 0.0691 1071 ASP A C +1952 O O . ASP A 252 ? 1.9129 1.7744 1.4709 0.1847 0.0194 0.0714 1071 ASP A O +1953 C CB . ASP A 252 ? 1.6731 1.5245 1.2315 0.1894 0.0102 0.0772 1071 ASP A CB +1954 C CG . ASP A 252 ? 2.7709 2.6183 2.3339 0.1876 0.0163 0.0809 1071 ASP A CG +1955 O OD1 . ASP A 252 ? 2.6487 2.4954 2.2165 0.1852 0.0187 0.0863 1071 ASP A OD1 +1956 O OD2 . ASP A 252 ? 3.3079 3.1529 2.8700 0.1886 0.0188 0.0784 1071 ASP A OD2 +1957 N N . SER A 253 ? 2.1120 1.9786 1.6608 0.1885 0.0118 0.0622 1072 SER A N +1958 C CA . SER A 253 ? 2.4581 2.3281 2.0046 0.1879 0.0155 0.0569 1072 SER A CA +1959 C C . SER A 253 ? 2.6608 2.5383 2.2057 0.1860 0.0157 0.0542 1072 SER A C +1960 O O . SER A 253 ? 2.4891 2.3698 2.0327 0.1850 0.0192 0.0503 1072 SER A O +1961 C CB . SER A 253 ? 2.5004 2.3702 2.0418 0.1908 0.0135 0.0508 1072 SER A CB +1962 O OG . SER A 253 ? 2.3135 2.1879 1.8500 0.1924 0.0083 0.0463 1072 SER A OG +1963 N N . ASN A 254 ? 2.9588 2.8389 2.5039 0.1854 0.0121 0.0561 1073 ASN A N +1964 C CA . ASN A 254 ? 2.9145 2.8016 2.4583 0.1835 0.0121 0.0540 1073 ASN A CA +1965 C C . ASN A 254 ? 2.8218 2.7096 2.3699 0.1803 0.0179 0.0570 1073 ASN A C +1966 O O . ASN A 254 ? 2.2564 2.1424 1.8092 0.1784 0.0189 0.0631 1073 ASN A O +1967 C CB . ASN A 254 ? 2.7890 2.6781 2.3328 0.1836 0.0071 0.0563 1073 ASN A CB +1968 C CG . ASN A 254 ? 2.5609 2.4568 2.0993 0.1843 0.0034 0.0503 1073 ASN A CG +1969 O OD1 . ASN A 254 ? 2.4384 2.3362 1.9723 0.1860 0.0027 0.0442 1073 ASN A OD1 +1970 N ND2 . ASN A 254 ? 2.3785 2.2780 1.9174 0.1831 0.0009 0.0520 1073 ASN A ND2 +1971 N N . MET A 255 ? 3.1187 3.0093 2.6653 0.1795 0.0216 0.0526 1074 MET A N +1972 C CA . MET A 255 ? 3.1387 3.0295 2.6891 0.1766 0.0276 0.0551 1074 MET A CA +1973 C C . MET A 255 ? 2.9850 2.8802 2.5375 0.1739 0.0280 0.0576 1074 MET A C +1974 O O . MET A 255 ? 2.5877 2.4817 2.1447 0.1714 0.0323 0.0618 1074 MET A O +1975 C CB . MET A 255 ? 3.1583 3.0515 2.7062 0.1766 0.0313 0.0494 1074 MET A CB +1976 C CG . MET A 255 ? 3.0654 2.9531 2.6130 0.1785 0.0329 0.0485 1074 MET A CG +1977 S SD . MET A 255 ? 3.3417 3.2214 2.8961 0.1774 0.0366 0.0566 1074 MET A SD +1978 C CE . MET A 255 ? 1.9008 1.7830 1.4592 0.1735 0.0429 0.0589 1074 MET A CE +1979 N N . GLU A 256 ? 3.1011 3.0012 2.6502 0.1744 0.0235 0.0549 1075 GLU A N +1980 C CA . GLU A 256 ? 2.9801 2.8845 2.5309 0.1721 0.0231 0.0571 1075 GLU A CA +1981 C C . GLU A 256 ? 2.5954 2.4952 2.1517 0.1709 0.0234 0.0650 1075 GLU A C +1982 O O . GLU A 256 ? 2.0542 1.9538 1.6147 0.1682 0.0273 0.0691 1075 GLU A O +1983 C CB . GLU A 256 ? 2.9645 2.8737 2.5109 0.1734 0.0173 0.0537 1075 GLU A CB +1984 C CG . GLU A 256 ? 2.9164 2.8296 2.4567 0.1752 0.0156 0.0458 1075 GLU A CG +1985 C CD . GLU A 256 ? 2.8893 2.8064 2.4256 0.1767 0.0094 0.0431 1075 GLU A CD +1986 O OE1 . GLU A 256 ? 2.9163 2.8308 2.4539 0.1775 0.0058 0.0470 1075 GLU A OE1 +1987 O OE2 . GLU A 256 ? 2.7749 2.6977 2.3067 0.1771 0.0083 0.0371 1075 GLU A OE2 +1988 N N . LEU A 257 ? 2.4793 2.3753 2.0353 0.1731 0.0191 0.0670 1076 LEU A N +1989 C CA . LEU A 257 ? 2.4259 2.3174 1.9866 0.1725 0.0182 0.0742 1076 LEU A CA +1990 C C . LEU A 257 ? 2.3797 2.2654 1.9457 0.1712 0.0233 0.0794 1076 LEU A C +1991 O O . LEU A 257 ? 1.6059 1.4905 1.1766 0.1689 0.0253 0.0851 1076 LEU A O +1992 C CB . LEU A 257 ? 2.2462 2.1348 1.8047 0.1754 0.0125 0.0743 1076 LEU A CB +1993 C CG . LEU A 257 ? 2.2409 2.1241 1.8035 0.1756 0.0107 0.0812 1076 LEU A CG +1994 C CD1 . LEU A 257 ? 1.9162 1.8015 1.4823 0.1730 0.0109 0.0860 1076 LEU A CD1 +1995 C CD2 . LEU A 257 ? 2.3708 2.2526 1.9302 0.1787 0.0047 0.0797 1076 LEU A CD2 +1996 N N . GLN A 258 ? 2.5631 2.4453 2.1283 0.1726 0.0254 0.0775 1077 GLN A N +1997 C CA . GLN A 258 ? 2.4373 2.3138 2.0074 0.1716 0.0302 0.0820 1077 GLN A CA +1998 C C . GLN A 258 ? 2.4790 2.3577 2.0523 0.1682 0.0356 0.0838 1077 GLN A C +1999 O O . GLN A 258 ? 2.2487 2.1241 1.8273 0.1664 0.0383 0.0899 1077 GLN A O +2000 C CB . GLN A 258 ? 2.1788 2.0518 1.7468 0.1736 0.0316 0.0787 1077 GLN A CB +2001 C CG . GLN A 258 ? 2.4183 2.2888 1.9831 0.1770 0.0264 0.0768 1077 GLN A CG +2002 C CD . GLN A 258 ? 2.3834 2.2481 1.9517 0.1776 0.0242 0.0832 1077 GLN A CD +2003 O OE1 . GLN A 258 ? 2.3077 2.1681 1.8811 0.1761 0.0276 0.0888 1077 GLN A OE1 +2004 N NE2 . GLN A 258 ? 1.8305 1.6950 1.3961 0.1799 0.0185 0.0823 1077 GLN A NE2 +2005 N N . ARG A 259 ? 2.4783 2.3629 2.0485 0.1675 0.0370 0.0785 1078 ARG A N +2006 C CA . ARG A 259 ? 2.4833 2.3710 2.0560 0.1643 0.0417 0.0794 1078 ARG A CA +2007 C C . ARG A 259 ? 2.5325 2.4217 2.1085 0.1623 0.0407 0.0845 1078 ARG A C +2008 O O . ARG A 259 ? 2.3472 2.2347 1.9280 0.1599 0.0445 0.0894 1078 ARG A O +2009 C CB . ARG A 259 ? 2.6822 2.5766 2.2503 0.1641 0.0423 0.0723 1078 ARG A CB +2010 C CG . ARG A 259 ? 2.6811 2.5788 2.2514 0.1610 0.0475 0.0727 1078 ARG A CG +2011 C CD . ARG A 259 ? 2.8939 2.7994 2.4605 0.1602 0.0461 0.0677 1078 ARG A CD +2012 N NE . ARG A 259 ? 3.0025 2.9109 2.5633 0.1625 0.0441 0.0603 1078 ARG A NE +2013 C CZ . ARG A 259 ? 2.6976 2.6112 2.2538 0.1635 0.0398 0.0559 1078 ARG A CZ +2014 N NH1 . ARG A 259 ? 2.3613 2.2778 1.9181 0.1624 0.0371 0.0581 1078 ARG A NH1 +2015 N NH2 . ARG A 259 ? 2.2967 2.2125 1.8477 0.1655 0.0383 0.0493 1078 ARG A NH2 +2016 N N . MET A 260 ? 2.5805 2.4730 2.1537 0.1633 0.0354 0.0831 1079 MET A N +2017 C CA . MET A 260 ? 2.5461 2.4408 2.1215 0.1616 0.0335 0.0871 1079 MET A CA +2018 C C . MET A 260 ? 2.6196 2.5084 2.2007 0.1607 0.0343 0.0950 1079 MET A C +2019 O O . MET A 260 ? 2.6144 2.5041 2.1993 0.1582 0.0363 0.0993 1079 MET A O +2020 C CB . MET A 260 ? 2.3160 2.2140 1.8872 0.1634 0.0271 0.0843 1079 MET A CB +2021 C CG . MET A 260 ? 1.8937 1.7992 1.4624 0.1620 0.0261 0.0810 1079 MET A CG +2022 S SD . MET A 260 ? 3.1704 3.0794 2.7347 0.1641 0.0184 0.0786 1079 MET A SD +2023 C CE . MET A 260 ? 1.3829 1.2920 0.9411 0.1675 0.0159 0.0712 1079 MET A CE +2024 N N . ILE A 261 ? 2.4966 2.3795 2.0783 0.1628 0.0328 0.0969 1080 ILE A N +2025 C CA . ILE A 261 ? 2.5221 2.3995 2.1090 0.1622 0.0330 0.1043 1080 ILE A CA +2026 C C . ILE A 261 ? 2.5847 2.4582 2.1764 0.1603 0.0392 0.1080 1080 ILE A C +2027 O O . ILE A 261 ? 2.6738 2.5453 2.2704 0.1583 0.0410 0.1141 1080 ILE A O +2028 C CB . ILE A 261 ? 2.3042 2.1764 1.8902 0.1651 0.0290 0.1053 1080 ILE A CB +2029 C CG1 . ILE A 261 ? 2.0588 1.9348 1.6392 0.1674 0.0232 0.1002 1080 ILE A CG1 +2030 C CG2 . ILE A 261 ? 2.3385 2.2062 1.9295 0.1644 0.0282 0.1129 1080 ILE A CG2 +2031 C CD1 . ILE A 261 ? 2.0469 1.9183 1.6267 0.1701 0.0186 0.1019 1080 ILE A CD1 +2032 N N . ALA A 262 ? 2.4034 2.2759 1.9936 0.1609 0.0424 0.1045 1081 ALA A N +2033 C CA . ALA A 262 ? 2.3955 2.2651 1.9898 0.1590 0.0485 0.1072 1081 ALA A CA +2034 C C . ALA A 262 ? 2.6459 2.5197 2.2426 0.1558 0.0516 0.1089 1081 ALA A C +2035 O O . ALA A 262 ? 2.4293 2.3004 2.0312 0.1537 0.0550 0.1146 1081 ALA A O +2036 C CB . ALA A 262 ? 1.7724 1.6419 1.3638 0.1602 0.0512 0.1018 1081 ALA A CB +2037 N N . ALA A 263 ? 2.6510 2.5316 2.2440 0.1554 0.0502 0.1040 1082 ALA A N +2038 C CA . ALA A 263 ? 2.6414 2.5266 2.2361 0.1524 0.0523 0.1053 1082 ALA A CA +2039 C C . ALA A 263 ? 3.0068 2.8921 2.6038 0.1517 0.0490 0.1102 1082 ALA A C +2040 O O . ALA A 263 ? 2.8890 2.7790 2.4831 0.1520 0.0451 0.1079 1082 ALA A O +2041 C CB . ALA A 263 ? 2.4777 2.3701 2.0675 0.1524 0.0518 0.0983 1082 ALA A CB +2042 N N . VAL A 264 ? 3.2053 3.0854 2.8076 0.1507 0.0506 0.1170 1083 VAL A N +2043 C CA . VAL A 264 ? 3.2616 3.1416 2.8670 0.1495 0.0485 0.1225 1083 VAL A CA +2044 C C . VAL A 264 ? 2.9189 2.7941 2.5307 0.1474 0.0526 0.1296 1083 VAL A C +2045 O O . VAL A 264 ? 2.1035 1.9735 1.7174 0.1478 0.0556 0.1312 1083 VAL A O +2046 C CB . VAL A 264 ? 2.8425 2.7208 2.4460 0.1520 0.0422 0.1231 1083 VAL A CB +2047 C CG1 . VAL A 264 ? 2.5370 2.4077 2.1433 0.1534 0.0422 0.1273 1083 VAL A CG1 +2048 C CG2 . VAL A 264 ? 2.6195 2.5005 2.2243 0.1507 0.0392 0.1264 1083 VAL A CG2 +2049 N N . ASP A 265 ? 3.0216 2.8986 2.6365 0.1450 0.0530 0.1337 1084 ASP A N +2050 C CA . ASP A 265 ? 3.1676 3.0407 2.7886 0.1428 0.0570 0.1405 1084 ASP A CA +2051 C C . ASP A 265 ? 3.1124 2.9798 2.7364 0.1438 0.0542 0.1463 1084 ASP A C +2052 O O . ASP A 265 ? 2.6053 2.4741 2.2297 0.1436 0.0505 0.1487 1084 ASP A O +2053 C CB . ASP A 265 ? 3.1603 3.0379 2.7833 0.1397 0.0590 0.1422 1084 ASP A CB +2054 C CG . ASP A 265 ? 2.9186 2.7934 2.5471 0.1371 0.0650 0.1470 1084 ASP A CG +2055 O OD1 . ASP A 265 ? 2.8715 2.7400 2.5037 0.1374 0.0662 0.1518 1084 ASP A OD1 +2056 O OD2 . ASP A 265 ? 2.5167 2.3955 2.1459 0.1347 0.0684 0.1461 1084 ASP A OD2 +2057 N N . THR A 266 ? 3.3445 3.2058 2.9707 0.1447 0.0561 0.1486 1085 THR A N +2058 C CA . THR A 266 ? 3.5569 3.4125 3.1853 0.1462 0.0531 0.1533 1085 THR A CA +2059 C C . THR A 266 ? 3.5852 3.4350 3.2198 0.1447 0.0571 0.1602 1085 THR A C +2060 O O . THR A 266 ? 3.6041 3.4479 3.2405 0.1461 0.0565 0.1632 1085 THR A O +2061 C CB . THR A 266 ? 3.5599 3.4127 3.1846 0.1495 0.0504 0.1495 1085 THR A CB +2062 O OG1 . THR A 266 ? 3.5177 3.3759 3.1367 0.1511 0.0462 0.1435 1085 THR A OG1 +2063 C CG2 . THR A 266 ? 3.4903 3.3372 3.1171 0.1512 0.0474 0.1542 1085 THR A CG2 +2064 N N . ASP A 267 ? 3.5095 3.3609 3.1474 0.1417 0.0613 0.1627 1086 ASP A N +2065 C CA . ASP A 267 ? 3.3409 3.1874 2.9850 0.1399 0.0649 0.1697 1086 ASP A CA +2066 C C . ASP A 267 ? 3.1862 3.0317 2.8329 0.1394 0.0615 0.1751 1086 ASP A C +2067 O O . ASP A 267 ? 2.7109 2.5509 2.3617 0.1394 0.0618 0.1808 1086 ASP A O +2068 C CB . ASP A 267 ? 3.2252 3.0740 2.8717 0.1369 0.0706 0.1702 1086 ASP A CB +2069 C CG . ASP A 267 ? 3.2671 3.1186 2.9103 0.1372 0.0735 0.1640 1086 ASP A CG +2070 O OD1 . ASP A 267 ? 3.2602 3.1103 2.9000 0.1397 0.0719 0.1601 1086 ASP A OD1 +2071 O OD2 . ASP A 267 ? 3.2429 3.0979 2.8867 0.1349 0.0774 0.1630 1086 ASP A OD2 +2072 N N . SER A 268 ? 3.3052 3.1563 2.9494 0.1391 0.0582 0.1730 1087 SER A N +2073 C CA . SER A 268 ? 3.1544 3.0055 2.7997 0.1391 0.0539 0.1768 1087 SER A CA +2074 C C . SER A 268 ? 3.3717 3.2249 3.0117 0.1419 0.0480 0.1722 1087 SER A C +2075 O O . SER A 268 ? 3.1193 2.9784 2.7560 0.1418 0.0454 0.1688 1087 SER A O +2076 C CB . SER A 268 ? 2.5213 2.3775 2.1680 0.1363 0.0550 0.1782 1087 SER A CB +2077 O OG . SER A 268 ? 2.1310 1.9870 1.7793 0.1361 0.0511 0.1823 1087 SER A OG +2078 N N . PRO A 269 ? 3.4080 3.2564 3.0470 0.1445 0.0458 0.1721 1088 PRO A N +2079 C CA . PRO A 269 ? 2.9540 2.8038 2.5877 0.1475 0.0408 0.1670 1088 PRO A CA +2080 C C . PRO A 269 ? 2.9039 2.7551 2.5364 0.1484 0.0349 0.1684 1088 PRO A C +2081 O O . PRO A 269 ? 2.7266 2.5821 2.3543 0.1498 0.0310 0.1634 1088 PRO A O +2082 C CB . PRO A 269 ? 2.4222 2.2654 2.0565 0.1496 0.0412 0.1679 1088 PRO A CB +2083 C CG . PRO A 269 ? 2.7312 2.5692 2.3717 0.1481 0.0440 0.1753 1088 PRO A CG +2084 C CD . PRO A 269 ? 3.2084 3.0496 2.8518 0.1448 0.0482 0.1772 1088 PRO A CD +2085 N N . ARG A 270 ? 2.9507 2.7984 2.5877 0.1476 0.0342 0.1750 1089 ARG A N +2086 C CA . ARG A 270 ? 2.7406 2.5887 2.3772 0.1485 0.0288 0.1771 1089 ARG A CA +2087 C C . ARG A 270 ? 2.7849 2.6402 2.4181 0.1479 0.0258 0.1737 1089 ARG A C +2088 O O . ARG A 270 ? 1.7303 1.5874 1.3600 0.1499 0.0205 0.1713 1089 ARG A O +2089 C CB . ARG A 270 ? 2.3091 2.1528 1.9517 0.1470 0.0297 0.1851 1089 ARG A CB +2090 C CG . ARG A 270 ? 2.5796 2.4256 2.2227 0.1464 0.0256 0.1879 1089 ARG A CG +2091 C CD . ARG A 270 ? 2.5204 2.3616 2.1693 0.1452 0.0264 0.1958 1089 ARG A CD +2092 N NE . ARG A 270 ? 2.6233 2.4674 2.2730 0.1442 0.0232 0.1983 1089 ARG A NE +2093 C CZ . ARG A 270 ? 2.6171 2.4616 2.2647 0.1460 0.0175 0.1982 1089 ARG A CZ +2094 N NH1 . ARG A 270 ? 2.6966 2.5386 2.3411 0.1489 0.0143 0.1956 1089 ARG A NH1 +2095 N NH2 . ARG A 270 ? 2.2703 2.1175 1.9187 0.1448 0.0149 0.2006 1089 ARG A NH2 +2096 N N . GLU A 271 ? 3.1462 3.0056 2.7806 0.1452 0.0292 0.1736 1090 GLU A N +2097 C CA . GLU A 271 ? 3.0463 2.9127 2.6777 0.1444 0.0269 0.1703 1090 GLU A CA +2098 C C . GLU A 271 ? 2.9161 2.7865 2.5412 0.1463 0.0251 0.1624 1090 GLU A C +2099 O O . GLU A 271 ? 2.4895 2.3640 2.1109 0.1475 0.0204 0.1592 1090 GLU A O +2100 C CB . GLU A 271 ? 3.0462 2.9159 2.6802 0.1411 0.0315 0.1716 1090 GLU A CB +2101 C CG . GLU A 271 ? 3.1611 3.0264 2.8015 0.1390 0.0350 0.1790 1090 GLU A CG +2102 C CD . GLU A 271 ? 3.2104 3.0787 2.8531 0.1358 0.0403 0.1796 1090 GLU A CD +2103 O OE1 . GLU A 271 ? 3.1011 2.9755 2.7406 0.1352 0.0404 0.1748 1090 GLU A OE1 +2104 O OE2 . GLU A 271 ? 3.1832 3.0479 2.8311 0.1341 0.0442 0.1849 1090 GLU A OE2 +2105 N N . VAL A 272 ? 3.0934 2.9628 2.7177 0.1467 0.0287 0.1593 1091 VAL A N +2106 C CA . VAL A 272 ? 2.9972 2.8705 2.6159 0.1482 0.0278 0.1517 1091 VAL A CA +2107 C C . VAL A 272 ? 3.0062 2.8790 2.6206 0.1515 0.0219 0.1488 1091 VAL A C +2108 O O . VAL A 272 ? 2.8924 2.7702 2.5020 0.1524 0.0189 0.1434 1091 VAL A O +2109 C CB . VAL A 272 ? 2.4403 2.3111 2.0591 0.1483 0.0327 0.1496 1091 VAL A CB +2110 C CG1 . VAL A 272 ? 2.3229 2.1984 1.9359 0.1495 0.0322 0.1417 1091 VAL A CG1 +2111 C CG2 . VAL A 272 ? 2.1970 2.0675 1.8205 0.1452 0.0387 0.1532 1091 VAL A CG2 +2112 N N . PHE A 273 ? 3.0280 2.8947 2.6443 0.1531 0.0204 0.1523 1092 PHE A N +2113 C CA . PHE A 273 ? 2.9499 2.8155 2.5626 0.1561 0.0148 0.1502 1092 PHE A CA +2114 C C . PHE A 273 ? 2.7096 2.5789 2.3210 0.1561 0.0098 0.1507 1092 PHE A C +2115 O O . PHE A 273 ? 2.6456 2.5187 2.2520 0.1578 0.0058 0.1457 1092 PHE A O +2116 C CB . PHE A 273 ? 3.1220 2.9800 2.7375 0.1576 0.0145 0.1546 1092 PHE A CB +2117 C CG . PHE A 273 ? 3.1419 2.9984 2.7545 0.1605 0.0085 0.1534 1092 PHE A CG +2118 C CD1 . PHE A 273 ? 3.0325 2.8898 2.6401 0.1631 0.0065 0.1474 1092 PHE A CD1 +2119 C CD2 . PHE A 273 ? 3.1145 2.9687 2.7294 0.1608 0.0050 0.1584 1092 PHE A CD2 +2120 C CE1 . PHE A 273 ? 2.8098 2.6657 2.4146 0.1658 0.0010 0.1463 1092 PHE A CE1 +2121 C CE2 . PHE A 273 ? 2.9790 2.8317 2.5911 0.1635 -0.0004 0.1573 1092 PHE A CE2 +2122 C CZ . PHE A 273 ? 2.7918 2.6453 2.3989 0.1660 -0.0024 0.1513 1092 PHE A CZ +2123 N N . PHE A 274 ? 2.4994 2.3673 2.1152 0.1543 0.0100 0.1569 1093 PHE A N +2124 C CA . PHE A 274 ? 2.7539 2.6246 2.3692 0.1543 0.0053 0.1584 1093 PHE A CA +2125 C C . PHE A 274 ? 2.8786 2.7570 2.4900 0.1536 0.0039 0.1533 1093 PHE A C +2126 O O . PHE A 274 ? 2.7931 2.6744 2.4011 0.1550 -0.0012 0.1511 1093 PHE A O +2127 C CB . PHE A 274 ? 3.0500 2.9182 2.6712 0.1520 0.0068 0.1659 1093 PHE A CB +2128 C CG . PHE A 274 ? 3.1891 3.0602 2.8101 0.1517 0.0024 0.1678 1093 PHE A CG +2129 C CD1 . PHE A 274 ? 2.7962 2.6646 2.4165 0.1538 -0.0027 0.1695 1093 PHE A CD1 +2130 C CD2 . PHE A 274 ? 3.1044 2.9808 2.7258 0.1493 0.0033 0.1678 1093 PHE A CD2 +2131 C CE1 . PHE A 274 ? 2.6939 2.5649 2.3140 0.1535 -0.0069 0.1712 1093 PHE A CE1 +2132 C CE2 . PHE A 274 ? 2.5358 2.4149 2.1570 0.1490 -0.0008 0.1695 1093 PHE A CE2 +2133 C CZ . PHE A 274 ? 2.4497 2.3260 2.0702 0.1511 -0.0059 0.1712 1093 PHE A CZ +2134 N N . ARG A 275 ? 2.9036 2.7853 2.5153 0.1514 0.0084 0.1516 1094 ARG A N +2135 C CA . ARG A 275 ? 2.7791 2.6683 2.3873 0.1505 0.0075 0.1469 1094 ARG A CA +2136 C C . ARG A 275 ? 2.6265 2.5185 2.2285 0.1530 0.0048 0.1394 1094 ARG A C +2137 O O . ARG A 275 ? 2.5551 2.4520 2.1533 0.1537 0.0009 0.1359 1094 ARG A O +2138 C CB . ARG A 275 ? 2.8570 2.7488 2.4673 0.1475 0.0132 0.1470 1094 ARG A CB +2139 C CG . ARG A 275 ? 2.8737 2.7720 2.4834 0.1455 0.0124 0.1463 1094 ARG A CG +2140 C CD . ARG A 275 ? 2.8498 2.7510 2.4608 0.1429 0.0180 0.1452 1094 ARG A CD +2141 N NE . ARG A 275 ? 2.8348 2.7311 2.4498 0.1419 0.0232 0.1484 1094 ARG A NE +2142 C CZ . ARG A 275 ? 2.5669 2.4601 2.1874 0.1398 0.0262 0.1548 1094 ARG A CZ +2143 N NH1 . ARG A 275 ? 2.1755 2.0702 1.7982 0.1383 0.0245 0.1587 1094 ARG A NH1 +2144 N NH2 . ARG A 275 ? 2.1576 2.0462 1.7815 0.1391 0.0309 0.1573 1094 ARG A NH2 +2145 N N . VAL A 276 ? 2.4487 2.3376 2.0499 0.1543 0.0070 0.1371 1095 VAL A N +2146 C CA . VAL A 276 ? 2.3592 2.2500 1.9546 0.1568 0.0047 0.1302 1095 VAL A CA +2147 C C . VAL A 276 ? 2.2935 2.1829 1.8865 0.1596 -0.0016 0.1300 1095 VAL A C +2148 O O . VAL A 276 ? 2.1297 2.0230 1.7176 0.1613 -0.0053 0.1246 1095 VAL A O +2149 C CB . VAL A 276 ? 2.4188 2.3058 2.0143 0.1577 0.0084 0.1285 1095 VAL A CB +2150 C CG1 . VAL A 276 ? 2.0501 1.9380 1.6399 0.1607 0.0053 0.1221 1095 VAL A CG1 +2151 C CG2 . VAL A 276 ? 2.8201 2.7097 2.4169 0.1553 0.0143 0.1273 1095 VAL A CG2 +2152 N N . ALA A 277 ? 2.4423 2.3262 2.0390 0.1599 -0.0027 0.1359 1096 ALA A N +2153 C CA . ALA A 277 ? 2.1904 2.0726 1.7855 0.1622 -0.0085 0.1367 1096 ALA A CA +2154 C C . ALA A 277 ? 2.1110 1.9987 1.7043 0.1617 -0.0125 0.1359 1096 ALA A C +2155 O O . ALA A 277 ? 1.7324 1.6228 1.3211 0.1638 -0.0172 0.1317 1096 ALA A O +2156 C CB . ALA A 277 ? 1.8423 1.7176 1.4424 0.1623 -0.0083 0.1438 1096 ALA A CB +2157 N N . ALA A 278 ? 2.2843 2.1738 1.8811 0.1589 -0.0105 0.1398 1097 ALA A N +2158 C CA . ALA A 278 ? 2.1335 2.0281 1.7291 0.1581 -0.0138 0.1397 1097 ALA A CA +2159 C C . ALA A 278 ? 2.0439 1.9456 1.6346 0.1579 -0.0142 0.1328 1097 ALA A C +2160 O O . ALA A 278 ? 1.8665 1.7727 1.4544 0.1582 -0.0182 0.1308 1097 ALA A O +2161 C CB . ALA A 278 ? 1.7956 1.6898 1.3965 0.1551 -0.0113 0.1460 1097 ALA A CB +2162 N N . ASP A 279 ? 2.0169 1.9197 1.6066 0.1574 -0.0099 0.1292 1098 ASP A N +2163 C CA . ASP A 279 ? 2.0996 2.0090 1.6845 0.1574 -0.0102 0.1223 1098 ASP A CA +2164 C C . ASP A 279 ? 2.4244 2.3347 2.0038 0.1607 -0.0147 0.1168 1098 ASP A C +2165 O O . ASP A 279 ? 2.0464 1.9621 1.6214 0.1612 -0.0178 0.1120 1098 ASP A O +2166 C CB . ASP A 279 ? 2.0011 1.9115 1.5867 0.1558 -0.0042 0.1202 1098 ASP A CB +2167 C CG . ASP A 279 ? 2.2869 2.2046 1.8693 0.1545 -0.0035 0.1153 1098 ASP A CG +2168 O OD1 . ASP A 279 ? 2.1726 2.0936 1.7500 0.1562 -0.0052 0.1088 1098 ASP A OD1 +2169 O OD2 . ASP A 279 ? 2.3815 2.3019 1.9666 0.1518 -0.0012 0.1178 1098 ASP A OD2 +2170 N N . MET A 280 ? 2.5035 2.4081 2.0830 0.1627 -0.0151 0.1173 1099 MET A N +2171 C CA . MET A 280 ? 2.3253 2.2298 1.8998 0.1659 -0.0195 0.1126 1099 MET A CA +2172 C C . MET A 280 ? 2.0372 1.9435 1.6101 0.1671 -0.0256 0.1133 1099 MET A C +2173 O O . MET A 280 ? 1.9073 1.8164 1.4751 0.1691 -0.0297 0.1082 1099 MET A O +2174 C CB . MET A 280 ? 2.5439 2.4415 2.1197 0.1678 -0.0189 0.1143 1099 MET A CB +2175 C CG . MET A 280 ? 2.7258 2.6223 2.3009 0.1679 -0.0143 0.1110 1099 MET A CG +2176 S SD . MET A 280 ? 2.6568 2.5457 2.2322 0.1707 -0.0147 0.1119 1099 MET A SD +2177 C CE . MET A 280 ? 1.6861 1.5765 1.2563 0.1739 -0.0223 0.1083 1099 MET A CE +2178 N N . PHE A 281 ? 1.9946 1.8992 1.5717 0.1657 -0.0262 0.1195 1100 PHE A N +2179 C CA . PHE A 281 ? 2.1361 2.0412 1.7122 0.1668 -0.0320 0.1211 1100 PHE A CA +2180 C C . PHE A 281 ? 2.3398 2.2501 1.9166 0.1646 -0.0328 0.1223 1100 PHE A C +2181 O O . PHE A 281 ? 2.1807 2.0901 1.7593 0.1644 -0.0359 0.1265 1100 PHE A O +2182 C CB . PHE A 281 ? 1.9103 1.8085 1.4904 0.1675 -0.0330 0.1273 1100 PHE A CB +2183 C CG . PHE A 281 ? 2.2743 2.1676 1.8530 0.1701 -0.0335 0.1259 1100 PHE A CG +2184 C CD1 . PHE A 281 ? 2.2348 2.1301 1.8079 0.1727 -0.0368 0.1196 1100 PHE A CD1 +2185 C CD2 . PHE A 281 ? 1.9198 1.8065 1.5028 0.1700 -0.0305 0.1306 1100 PHE A CD2 +2186 C CE1 . PHE A 281 ? 2.0943 1.9850 1.6661 0.1752 -0.0373 0.1182 1100 PHE A CE1 +2187 C CE2 . PHE A 281 ? 1.8680 1.7502 1.4498 0.1724 -0.0309 0.1292 1100 PHE A CE2 +2188 C CZ . PHE A 281 ? 2.0476 1.9317 1.6237 0.1750 -0.0343 0.1230 1100 PHE A CZ +2189 N N . SER A 282 ? 2.6692 2.5848 2.2445 0.1629 -0.0301 0.1187 1101 SER A N +2190 C CA . SER A 282 ? 2.8544 2.7755 2.4297 0.1609 -0.0308 0.1190 1101 SER A CA +2191 C C . SER A 282 ? 2.8398 2.7659 2.4097 0.1627 -0.0364 0.1139 1101 SER A C +2192 O O . SER A 282 ? 2.3128 2.2425 1.8825 0.1618 -0.0390 0.1150 1101 SER A O +2193 C CB . SER A 282 ? 2.8809 2.8057 2.4569 0.1584 -0.0255 0.1171 1101 SER A CB +2194 O OG . SER A 282 ? 2.8287 2.7565 2.4000 0.1596 -0.0250 0.1100 1101 SER A OG +2195 N N . ASP A 283 ? 2.8934 2.8197 2.4589 0.1652 -0.0382 0.1085 1102 ASP A N +2196 C CA . ASP A 283 ? 2.4443 2.3744 2.0045 0.1673 -0.0438 0.1038 1102 ASP A CA +2197 C C . ASP A 283 ? 2.0450 1.9708 1.6054 0.1695 -0.0486 0.1067 1102 ASP A C +2198 O O . ASP A 283 ? 1.4538 1.3822 1.0106 0.1712 -0.0538 0.1041 1102 ASP A O +2199 C CB . ASP A 283 ? 2.3625 2.2954 1.9175 0.1689 -0.0435 0.0962 1102 ASP A CB +2200 C CG . ASP A 283 ? 2.4453 2.3727 2.0003 0.1706 -0.0418 0.0956 1102 ASP A CG +2201 O OD1 . ASP A 283 ? 2.6620 2.5840 2.2218 0.1698 -0.0387 0.1008 1102 ASP A OD1 +2202 O OD2 . ASP A 283 ? 1.9469 1.8754 1.4973 0.1728 -0.0435 0.0898 1102 ASP A OD2 +2203 N N . GLY A 284 ? 2.0098 1.9291 1.5746 0.1695 -0.0469 0.1121 1103 GLY A N +2204 C CA . GLY A 284 ? 2.1125 2.0271 1.6786 0.1711 -0.0508 0.1162 1103 GLY A CA +2205 C C . GLY A 284 ? 2.4491 2.3632 2.0104 0.1745 -0.0557 0.1120 1103 GLY A C +2206 O O . GLY A 284 ? 1.5935 1.5066 1.1542 0.1759 -0.0606 0.1136 1103 GLY A O +2207 N N . ASN A 285 ? 2.9533 2.8681 2.5113 0.1757 -0.0543 0.1065 1104 ASN A N +2208 C CA . ASN A 285 ? 2.6632 2.5772 2.2165 0.1790 -0.0582 0.1020 1104 ASN A CA +2209 C C . ASN A 285 ? 2.1207 2.0280 1.6755 0.1804 -0.0563 0.1034 1104 ASN A C +2210 O O . ASN A 285 ? 2.0289 1.9361 1.5817 0.1811 -0.0538 0.0993 1104 ASN A O +2211 C CB . ASN A 285 ? 2.4166 2.3365 1.9643 0.1796 -0.0585 0.0942 1104 ASN A CB +2212 C CG . ASN A 285 ? 2.4541 2.3810 1.9999 0.1784 -0.0608 0.0922 1104 ASN A CG +2213 O OD1 . ASN A 285 ? 2.2789 2.2061 1.8263 0.1778 -0.0635 0.0960 1104 ASN A OD1 +2214 N ND2 . ASN A 285 ? 2.0532 1.9855 1.5953 0.1780 -0.0596 0.0862 1104 ASN A ND2 +2215 N N . PHE A 286 ? 1.9918 1.8935 1.5501 0.1808 -0.0576 0.1092 1105 PHE A N +2216 C CA . PHE A 286 ? 2.2229 2.1177 1.7834 0.1821 -0.0560 0.1116 1105 PHE A CA +2217 C C . PHE A 286 ? 2.7075 2.6011 2.2632 0.1855 -0.0595 0.1069 1105 PHE A C +2218 O O . PHE A 286 ? 2.8211 2.7166 2.3737 0.1872 -0.0648 0.1050 1105 PHE A O +2219 C CB . PHE A 286 ? 2.0518 1.9413 1.6170 0.1818 -0.0571 0.1191 1105 PHE A CB +2220 C CG . PHE A 286 ? 2.6409 2.5303 2.2115 0.1786 -0.0534 0.1247 1105 PHE A CG +2221 C CD1 . PHE A 286 ? 3.0549 2.9408 2.6296 0.1771 -0.0478 0.1277 1105 PHE A CD1 +2222 C CD2 . PHE A 286 ? 2.1967 2.0893 1.7683 0.1773 -0.0557 0.1272 1105 PHE A CD2 +2223 C CE1 . PHE A 286 ? 3.0261 2.9117 2.6058 0.1742 -0.0444 0.1330 1105 PHE A CE1 +2224 C CE2 . PHE A 286 ? 1.7777 1.6702 1.3543 0.1743 -0.0524 0.1324 1105 PHE A CE2 +2225 C CZ . PHE A 286 ? 2.3928 2.2817 1.9733 0.1728 -0.0467 0.1353 1105 PHE A CZ +2226 N N . ASN A 287 ? 2.8053 2.6957 2.3607 0.1864 -0.0565 0.1051 1106 ASN A N +2227 C CA . ASN A 287 ? 2.4509 2.3385 2.0029 0.1895 -0.0592 0.1018 1106 ASN A CA +2228 C C . ASN A 287 ? 2.3833 2.2647 1.9383 0.1897 -0.0551 0.1041 1106 ASN A C +2229 O O . ASN A 287 ? 2.0908 1.9716 1.6488 0.1876 -0.0498 0.1057 1106 ASN A O +2230 C CB . ASN A 287 ? 2.2681 2.1610 1.8139 0.1909 -0.0607 0.0937 1106 ASN A CB +2231 C CG . ASN A 287 ? 2.1815 2.0789 1.7271 0.1887 -0.0559 0.0908 1106 ASN A CG +2232 O OD1 . ASN A 287 ? 2.1087 2.0036 1.6565 0.1877 -0.0510 0.0914 1106 ASN A OD1 +2233 N ND2 . ASN A 287 ? 1.8489 1.7528 1.3918 0.1878 -0.0575 0.0875 1106 ASN A ND2 +2234 N N . TRP A 288 ? 2.3393 2.2158 1.8933 0.1923 -0.0576 0.1043 1107 TRP A N +2235 C CA . TRP A 288 ? 1.7816 1.6517 1.3384 0.1928 -0.0542 0.1068 1107 TRP A CA +2236 C C . TRP A 288 ? 1.8473 1.7181 1.4035 0.1920 -0.0490 0.1033 1107 TRP A C +2237 O O . TRP A 288 ? 1.7670 1.6334 1.3269 0.1912 -0.0447 0.1064 1107 TRP A O +2238 C CB . TRP A 288 ? 1.8924 1.7583 1.4470 0.1960 -0.0582 0.1059 1107 TRP A CB +2239 C CG . TRP A 288 ? 2.3815 2.2413 1.9403 0.1962 -0.0591 0.1126 1107 TRP A CG +2240 C CD1 . TRP A 288 ? 2.7751 2.6337 2.3339 0.1974 -0.0642 0.1151 1107 TRP A CD1 +2241 C CD2 . TRP A 288 ? 2.6215 2.4755 2.1856 0.1951 -0.0548 0.1179 1107 TRP A CD2 +2242 N NE1 . TRP A 288 ? 3.0894 2.9418 2.6530 0.1972 -0.0633 0.1216 1107 TRP A NE1 +2243 C CE2 . TRP A 288 ? 2.9974 2.8469 2.5643 0.1957 -0.0576 0.1235 1107 TRP A CE2 +2244 C CE3 . TRP A 288 ? 2.4550 2.3072 2.0216 0.1936 -0.0488 0.1185 1107 TRP A CE3 +2245 C CZ2 . TRP A 288 ? 2.7159 2.5591 2.2881 0.1950 -0.0546 0.1295 1107 TRP A CZ2 +2246 C CZ3 . TRP A 288 ? 2.2134 2.0594 1.7852 0.1928 -0.0459 0.1246 1107 TRP A CZ3 +2247 C CH2 . TRP A 288 ? 2.1064 1.9480 1.6809 0.1935 -0.0488 0.1300 1107 TRP A CH2 +2248 N N . GLY A 289 ? 1.7960 1.6725 1.3476 0.1924 -0.0495 0.0967 1108 GLY A N +2249 C CA . GLY A 289 ? 1.9839 1.8619 1.5346 0.1916 -0.0446 0.0930 1108 GLY A CA +2250 C C . GLY A 289 ? 2.2744 2.1525 1.8300 0.1883 -0.0391 0.0969 1108 GLY A C +2251 O O . GLY A 289 ? 2.0225 1.8979 1.5800 0.1876 -0.0343 0.0973 1108 GLY A O +2252 N N . ARG A 290 ? 2.2891 2.1703 1.8465 0.1863 -0.0397 0.0997 1109 ARG A N +2253 C CA . ARG A 290 ? 1.8999 1.7816 1.4619 0.1831 -0.0347 0.1036 1109 ARG A CA +2254 C C . ARG A 290 ? 1.9771 1.8521 1.5450 0.1823 -0.0326 0.1110 1109 ARG A C +2255 O O . ARG A 290 ? 1.9265 1.7997 1.4981 0.1803 -0.0273 0.1136 1109 ARG A O +2256 C CB . ARG A 290 ? 1.4771 1.3645 1.0392 0.1812 -0.0363 0.1042 1109 ARG A CB +2257 C CG . ARG A 290 ? 1.8781 1.7725 1.4354 0.1811 -0.0368 0.0974 1109 ARG A CG +2258 C CD . ARG A 290 ? 2.1357 2.0352 1.6939 0.1788 -0.0374 0.0989 1109 ARG A CD +2259 N NE . ARG A 290 ? 2.2246 2.1311 1.7781 0.1787 -0.0383 0.0925 1109 ARG A NE +2260 C CZ . ARG A 290 ? 2.4507 2.3625 2.0038 0.1771 -0.0395 0.0923 1109 ARG A CZ +2261 N NH1 . ARG A 290 ? 2.6467 2.5576 2.2038 0.1755 -0.0400 0.0982 1109 ARG A NH1 +2262 N NH2 . ARG A 290 ? 2.2638 2.1819 1.8125 0.1771 -0.0403 0.0863 1109 ARG A NH2 +2263 N N . VAL A 291 ? 1.9532 1.8246 1.5218 0.1838 -0.0367 0.1142 1110 VAL A N +2264 C CA . VAL A 291 ? 1.7739 1.6386 1.3477 0.1835 -0.0353 0.1210 1110 VAL A CA +2265 C C . VAL A 291 ? 1.8130 1.6730 1.3877 0.1842 -0.0313 0.1205 1110 VAL A C +2266 O O . VAL A 291 ? 1.8567 1.7126 1.4362 0.1827 -0.0271 0.1253 1110 VAL A O +2267 C CB . VAL A 291 ? 2.0396 1.9012 1.6128 0.1857 -0.0409 0.1232 1110 VAL A CB +2268 C CG1 . VAL A 291 ? 2.0476 1.9021 1.6262 0.1854 -0.0395 0.1303 1110 VAL A CG1 +2269 C CG2 . VAL A 291 ? 1.6183 1.4846 1.1903 0.1852 -0.0451 0.1234 1110 VAL A CG2 +2270 N N . VAL A 292 ? 1.7732 1.6340 1.3431 0.1864 -0.0325 0.1145 1111 VAL A N +2271 C CA . VAL A 292 ? 1.8685 1.7252 1.4386 0.1873 -0.0291 0.1132 1111 VAL A CA +2272 C C . VAL A 292 ? 1.8960 1.7555 1.4666 0.1853 -0.0235 0.1109 1111 VAL A C +2273 O O . VAL A 292 ? 1.9684 1.8239 1.5424 0.1844 -0.0188 0.1134 1111 VAL A O +2274 C CB . VAL A 292 ? 1.6905 1.5468 1.2553 0.1906 -0.0328 0.1077 1111 VAL A CB +2275 C CG1 . VAL A 292 ? 1.2994 1.1522 0.8641 0.1915 -0.0291 0.1058 1111 VAL A CG1 +2276 C CG2 . VAL A 292 ? 1.9312 1.7838 1.4961 0.1927 -0.0378 0.1106 1111 VAL A CG2 +2277 N N . ALA A 293 ? 1.7745 1.6407 1.3419 0.1845 -0.0238 0.1062 1112 ALA A N +2278 C CA . ALA A 293 ? 1.7964 1.6656 1.3639 0.1825 -0.0186 0.1037 1112 ALA A CA +2279 C C . ALA A 293 ? 2.0911 1.9592 1.6644 0.1794 -0.0142 0.1096 1112 ALA A C +2280 O O . ALA A 293 ? 1.9185 1.7864 1.4937 0.1777 -0.0090 0.1095 1112 ALA A O +2281 C CB . ALA A 293 ? 1.5919 1.4687 1.1547 0.1824 -0.0202 0.0975 1112 ALA A CB +2282 N N . LEU A 294 ? 2.1901 2.0574 1.7664 0.1785 -0.0164 0.1149 1113 LEU A N +2283 C CA . LEU A 294 ? 2.0419 1.9075 1.6239 0.1757 -0.0125 0.1210 1113 LEU A CA +2284 C C . LEU A 294 ? 1.8562 1.7141 1.4425 0.1761 -0.0106 0.1263 1113 LEU A C +2285 O O . LEU A 294 ? 1.9588 1.8143 1.5499 0.1739 -0.0061 0.1308 1113 LEU A O +2286 C CB . LEU A 294 ? 1.6033 1.4718 1.1867 0.1744 -0.0155 0.1242 1113 LEU A CB +2287 C CG . LEU A 294 ? 1.9123 1.7798 1.5014 0.1713 -0.0119 0.1305 1113 LEU A CG +2288 C CD1 . LEU A 294 ? 1.8282 1.7019 1.4165 0.1696 -0.0134 0.1298 1113 LEU A CD1 +2289 C CD2 . LEU A 294 ? 2.3416 2.2030 1.9349 0.1717 -0.0133 0.1372 1113 LEU A CD2 +2290 N N . PHE A 295 ? 1.6364 1.4905 1.2208 0.1789 -0.0139 0.1256 1114 PHE A N +2291 C CA . PHE A 295 ? 1.9343 1.7811 1.5223 0.1796 -0.0122 0.1300 1114 PHE A CA +2292 C C . PHE A 295 ? 2.0897 1.9345 1.6768 0.1801 -0.0082 0.1268 1114 PHE A C +2293 O O . PHE A 295 ? 2.3134 2.1522 1.9034 0.1805 -0.0059 0.1300 1114 PHE A O +2294 C CB . PHE A 295 ? 1.9973 1.8406 1.5841 0.1823 -0.0176 0.1311 1114 PHE A CB +2295 C CG . PHE A 295 ? 2.3354 2.1711 1.9267 0.1826 -0.0164 0.1372 1114 PHE A CG +2296 C CD1 . PHE A 295 ? 2.4115 2.2450 2.0079 0.1808 -0.0159 0.1440 1114 PHE A CD1 +2297 C CD2 . PHE A 295 ? 2.0851 1.9160 1.6756 0.1846 -0.0158 0.1360 1114 PHE A CD2 +2298 C CE1 . PHE A 295 ? 2.4506 2.2773 2.0512 0.1811 -0.0148 0.1496 1114 PHE A CE1 +2299 C CE2 . PHE A 295 ? 2.2207 2.0447 1.8154 0.1849 -0.0147 0.1416 1114 PHE A CE2 +2300 C CZ . PHE A 295 ? 2.5121 2.3340 2.1118 0.1831 -0.0143 0.1484 1114 PHE A CZ +2301 N N . TYR A 296 ? 2.0877 1.9375 1.6707 0.1803 -0.0074 0.1204 1115 TYR A N +2302 C CA . TYR A 296 ? 2.1521 2.0010 1.7344 0.1803 -0.0029 0.1171 1115 TYR A CA +2303 C C . TYR A 296 ? 2.3472 2.1978 1.9332 0.1770 0.0025 0.1195 1115 TYR A C +2304 O O . TYR A 296 ? 1.9983 1.8461 1.5865 0.1762 0.0074 0.1204 1115 TYR A O +2305 C CB . TYR A 296 ? 2.1605 2.0142 1.7363 0.1821 -0.0050 0.1090 1115 TYR A CB +2306 C CG . TYR A 296 ? 2.3317 2.1858 1.9057 0.1822 -0.0008 0.1044 1115 TYR A CG +2307 C CD1 . TYR A 296 ? 2.6652 2.5143 2.2385 0.1842 0.0000 0.1033 1115 TYR A CD1 +2308 C CD2 . TYR A 296 ? 2.2542 2.1136 1.8271 0.1803 0.0023 0.1010 1115 TYR A CD2 +2309 C CE1 . TYR A 296 ? 2.7576 2.6072 2.3292 0.1843 0.0038 0.0991 1115 TYR A CE1 +2310 C CE2 . TYR A 296 ? 2.2047 2.0647 1.7760 0.1804 0.0061 0.0968 1115 TYR A CE2 +2311 C CZ . TYR A 296 ? 2.2247 2.0798 1.7954 0.1824 0.0068 0.0958 1115 TYR A CZ +2312 O OH . TYR A 296 ? 1.9384 1.7940 1.5074 0.1825 0.0106 0.0916 1115 TYR A OH +2313 N N . PHE A 297 ? 2.4182 2.2733 2.0048 0.1752 0.0017 0.1207 1116 PHE A N +2314 C CA . PHE A 297 ? 2.2154 2.0723 1.8057 0.1719 0.0065 0.1233 1116 PHE A CA +2315 C C . PHE A 297 ? 2.0034 1.8543 1.6000 0.1706 0.0091 0.1310 1116 PHE A C +2316 O O . PHE A 297 ? 1.7151 1.5629 1.3144 0.1696 0.0141 0.1325 1116 PHE A O +2317 C CB . PHE A 297 ? 2.2035 2.0669 1.7928 0.1704 0.0046 0.1225 1116 PHE A CB +2318 C CG . PHE A 297 ? 2.5492 2.4157 2.1408 0.1672 0.0096 0.1232 1116 PHE A CG +2319 C CD1 . PHE A 297 ? 2.3411 2.2113 1.9300 0.1668 0.0126 0.1178 1116 PHE A CD1 +2320 C CD2 . PHE A 297 ? 2.9734 2.8392 2.5700 0.1648 0.0113 0.1293 1116 PHE A CD2 +2321 C CE1 . PHE A 297 ? 2.6376 2.5108 2.2287 0.1639 0.0172 0.1184 1116 PHE A CE1 +2322 C CE2 . PHE A 297 ? 2.9552 2.8239 2.5540 0.1619 0.0159 0.1300 1116 PHE A CE2 +2323 C CZ . PHE A 297 ? 2.8793 2.7517 2.4754 0.1614 0.0188 0.1245 1116 PHE A CZ +2324 N N . ALA A 298 ? 1.8420 1.6912 1.4408 0.1707 0.0058 0.1357 1117 ALA A N +2325 C CA . ALA A 298 ? 2.0650 1.9082 1.6695 0.1697 0.0076 0.1431 1117 ALA A CA +2326 C C . ALA A 298 ? 2.5409 2.3778 2.1465 0.1712 0.0098 0.1438 1117 ALA A C +2327 O O . ALA A 298 ? 2.4669 2.2991 2.0774 0.1699 0.0134 0.1489 1117 ALA A O +2328 C CB . ALA A 298 ? 2.0448 1.8867 1.6503 0.1704 0.0026 0.1470 1117 ALA A CB +2329 N N . SER A 299 ? 2.7068 2.5436 2.3078 0.1739 0.0075 0.1385 1118 SER A N +2330 C CA . SER A 299 ? 2.5001 2.3318 2.1012 0.1753 0.0098 0.1378 1118 SER A CA +2331 C C . SER A 299 ? 2.3571 2.1896 1.9600 0.1733 0.0161 0.1370 1118 SER A C +2332 O O . SER A 299 ? 2.4921 2.3200 2.0996 0.1720 0.0201 0.1417 1118 SER A O +2333 C CB . SER A 299 ? 2.3963 2.2291 1.9916 0.1784 0.0062 0.1314 1118 SER A CB +2334 O OG . SER A 299 ? 2.4374 2.2647 2.0327 0.1802 0.0074 0.1312 1118 SER A OG +2335 N N . LYS A 300 ? 2.0171 1.8552 1.6163 0.1729 0.0171 0.1312 1119 LYS A N +2336 C CA . LYS A 300 ? 2.0948 1.9342 1.6951 0.1710 0.0230 0.1296 1119 LYS A CA +2337 C C . LYS A 300 ? 2.6539 2.4925 2.2598 0.1678 0.0274 0.1353 1119 LYS A C +2338 O O . LYS A 300 ? 2.6588 2.4970 2.2665 0.1662 0.0326 0.1352 1119 LYS A O +2339 C CB . LYS A 300 ? 2.0673 1.9137 1.6626 0.1710 0.0227 0.1226 1119 LYS A CB +2340 C CG . LYS A 300 ? 1.9834 1.8304 1.5731 0.1739 0.0202 0.1161 1119 LYS A CG +2341 C CD . LYS A 300 ? 1.6078 1.4519 1.1976 0.1742 0.0247 0.1140 1119 LYS A CD +2342 C CE . LYS A 300 ? 1.9165 1.7634 1.5003 0.1765 0.0230 0.1064 1119 LYS A CE +2343 N NZ . LYS A 300 ? 1.9761 1.8186 1.5598 0.1777 0.0260 0.1049 1119 LYS A NZ +2344 N N . LEU A 301 ? 2.8837 2.7222 2.4925 0.1667 0.0253 0.1403 1120 LEU A N +2345 C CA . LEU A 301 ? 2.5202 2.3574 2.1346 0.1638 0.0292 0.1463 1120 LEU A CA +2346 C C . LEU A 301 ? 2.4604 2.2900 2.0793 0.1640 0.0312 0.1520 1120 LEU A C +2347 O O . LEU A 301 ? 2.0468 1.8735 1.6695 0.1634 0.0300 0.1579 1120 LEU A O +2348 C CB . LEU A 301 ? 2.1749 2.0151 1.7904 0.1626 0.0261 0.1493 1120 LEU A CB +2349 C CG . LEU A 301 ? 2.4272 2.2751 2.0386 0.1621 0.0243 0.1440 1120 LEU A CG +2350 C CD1 . LEU A 301 ? 2.3291 2.1798 1.9417 0.1608 0.0213 0.1472 1120 LEU A CD1 +2351 C CD2 . LEU A 301 ? 2.2025 2.0538 1.8139 0.1600 0.0296 0.1413 1120 LEU A CD2 +2352 N N . VAL A 302 ? 2.7395 2.5659 2.3580 0.1650 0.0341 0.1501 1121 VAL A N +2353 C CA . VAL A 302 ? 2.9966 2.8158 2.6190 0.1655 0.0360 0.1546 1121 VAL A CA +2354 C C . VAL A 302 ? 3.0140 2.8314 2.6375 0.1647 0.0418 0.1534 1121 VAL A C +2355 O O . VAL A 302 ? 3.1631 2.9777 2.7915 0.1627 0.0462 0.1581 1121 VAL A O +2356 C CB . VAL A 302 ? 2.4097 2.2252 2.0295 0.1688 0.0313 0.1536 1121 VAL A CB +2357 C CG1 . VAL A 302 ? 2.1558 1.9641 1.7784 0.1697 0.0339 0.1564 1121 VAL A CG1 +2358 C CG2 . VAL A 302 ? 2.1350 1.9503 1.7553 0.1694 0.0262 0.1569 1121 VAL A CG2 +2359 N N . LEU A 303 ? 2.7087 2.5279 2.3276 0.1663 0.0419 0.1470 1122 LEU A N +2360 C CA . LEU A 303 ? 2.8135 2.6307 2.4329 0.1661 0.0469 0.1452 1122 LEU A CA +2361 C C . LEU A 303 ? 2.8532 2.6720 2.4761 0.1629 0.0527 0.1471 1122 LEU A C +2362 O O . LEU A 303 ? 2.6502 2.4651 2.2762 0.1621 0.0573 0.1493 1122 LEU A O +2363 C CB . LEU A 303 ? 2.6643 2.4845 2.2777 0.1681 0.0457 0.1374 1122 LEU A CB +2364 C CG . LEU A 303 ? 2.4445 2.2603 2.0556 0.1712 0.0436 0.1354 1122 LEU A CG +2365 C CD1 . LEU A 303 ? 1.9501 1.7698 1.5551 0.1730 0.0422 0.1275 1122 LEU A CD1 +2366 C CD2 . LEU A 303 ? 1.9009 1.7102 1.5158 0.1710 0.0481 0.1389 1122 LEU A CD2 +2367 N N . SER B 5 ? 1.3921 1.5088 1.1742 0.4114 -0.0928 -0.0457 2 SER B N +2368 C CA . SER B 5 ? 1.9628 2.0791 1.7408 0.4125 -0.0901 -0.0423 2 SER B CA +2369 C C . SER B 5 ? 1.9213 2.0325 1.7019 0.4100 -0.0899 -0.0405 2 SER B C +2370 O O . SER B 5 ? 1.4656 1.5709 1.2489 0.4074 -0.0911 -0.0417 2 SER B O +2371 C CB . SER B 5 ? 1.8992 2.0119 1.6686 0.4144 -0.0871 -0.0414 2 SER B CB +2372 O OG . SER B 5 ? 1.9900 2.0934 1.7569 0.4125 -0.0861 -0.0413 2 SER B OG +2373 N N . LYS B 6 ? 1.8876 2.0010 1.6672 0.4108 -0.0885 -0.0377 3 LYS B N +2374 C CA . LYS B 6 ? 1.8192 1.9280 1.6005 0.4087 -0.0879 -0.0357 3 LYS B CA +2375 C C . LYS B 6 ? 1.8941 1.9949 1.6686 0.4086 -0.0850 -0.0342 3 LYS B C +2376 O O . LYS B 6 ? 1.7119 1.8065 1.4872 0.4064 -0.0846 -0.0332 3 LYS B O +2377 C CB . LYS B 6 ? 2.0794 2.1940 1.8626 0.4095 -0.0876 -0.0333 3 LYS B CB +2378 C CG . LYS B 6 ? 2.3645 2.4890 2.1511 0.4112 -0.0893 -0.0340 3 LYS B CG +2379 C CD . LYS B 6 ? 2.5141 2.6410 2.3082 0.4095 -0.0928 -0.0368 3 LYS B CD +2380 C CE . LYS B 6 ? 2.1997 2.3346 1.9946 0.4115 -0.0941 -0.0387 3 LYS B CE +2381 N NZ . LYS B 6 ? 1.8222 1.9587 1.6236 0.4100 -0.0975 -0.0418 3 LYS B NZ +2382 N N . GLY B 7 ? 1.9138 2.0149 1.6818 0.4109 -0.0831 -0.0341 4 GLY B N +2383 C CA . GLY B 7 ? 1.7183 1.8122 1.4795 0.4110 -0.0804 -0.0330 4 GLY B CA +2384 C C . GLY B 7 ? 1.6812 1.7675 1.4431 0.4086 -0.0812 -0.0348 4 GLY B C +2385 O O . GLY B 7 ? 1.5470 1.6261 1.3066 0.4070 -0.0798 -0.0337 4 GLY B O +2386 N N . GLU B 8 ? 1.3889 1.4768 1.1542 0.4081 -0.0835 -0.0377 5 GLU B N +2387 C CA . GLU B 8 ? 1.1251 1.2064 0.8916 0.4058 -0.0846 -0.0397 5 GLU B CA +2388 C C . GLU B 8 ? 1.2095 1.2847 0.9796 0.4026 -0.0851 -0.0390 5 GLU B C +2389 O O . GLU B 8 ? 1.6522 1.7200 1.4208 0.4009 -0.0846 -0.0396 5 GLU B O +2390 C CB . GLU B 8 ? 1.4765 1.5619 1.2476 0.4058 -0.0874 -0.0429 5 GLU B CB +2391 C CG . GLU B 8 ? 2.0641 2.1433 1.8370 0.4034 -0.0888 -0.0453 5 GLU B CG +2392 C CD . GLU B 8 ? 2.3894 2.4662 2.1568 0.4046 -0.0878 -0.0466 5 GLU B CD +2393 O OE1 . GLU B 8 ? 2.4525 2.5349 2.2195 0.4066 -0.0886 -0.0482 5 GLU B OE1 +2394 O OE2 . GLU B 8 ? 2.1617 2.2310 1.9252 0.4035 -0.0863 -0.0461 5 GLU B OE2 +2395 N N . GLU B 9 ? 1.3501 1.4284 1.1250 0.4019 -0.0860 -0.0378 6 GLU B N +2396 C CA . GLU B 9 ? 1.3106 1.3839 1.0897 0.3989 -0.0868 -0.0373 6 GLU B CA +2397 C C . GLU B 9 ? 1.4093 1.4762 1.1837 0.3983 -0.0841 -0.0347 6 GLU B C +2398 O O . GLU B 9 ? 1.4171 1.4787 1.1940 0.3957 -0.0844 -0.0343 6 GLU B O +2399 C CB . GLU B 9 ? 1.8564 1.9353 1.6421 0.3984 -0.0887 -0.0367 6 GLU B CB +2400 C CG . GLU B 9 ? 2.2350 2.3194 2.0268 0.3982 -0.0918 -0.0394 6 GLU B CG +2401 C CD . GLU B 9 ? 2.3946 2.4850 2.1928 0.3977 -0.0936 -0.0386 6 GLU B CD +2402 O OE1 . GLU B 9 ? 2.2138 2.3049 2.0111 0.3980 -0.0922 -0.0359 6 GLU B OE1 +2403 O OE2 . GLU B 9 ? 2.5417 2.6361 2.3457 0.3971 -0.0964 -0.0408 6 GLU B OE2 +2404 N N . LEU B 10 ? 1.2911 1.3587 1.0587 0.4007 -0.0815 -0.0331 7 LEU B N +2405 C CA . LEU B 10 ? 1.2205 1.2824 0.9829 0.4004 -0.0787 -0.0308 7 LEU B CA +2406 C C . LEU B 10 ? 1.4366 1.4910 1.1946 0.3995 -0.0776 -0.0317 7 LEU B C +2407 O O . LEU B 10 ? 1.1816 1.2301 0.9359 0.3987 -0.0756 -0.0301 7 LEU B O +2408 C CB . LEU B 10 ? 1.1392 1.2055 0.8965 0.4034 -0.0763 -0.0286 7 LEU B CB +2409 C CG . LEU B 10 ? 1.4073 1.4812 1.1683 0.4045 -0.0771 -0.0273 7 LEU B CG +2410 C CD1 . LEU B 10 ? 1.3762 1.4557 1.1322 0.4078 -0.0751 -0.0260 7 LEU B CD1 +2411 C CD2 . LEU B 10 ? 1.3879 1.4591 1.1512 0.4027 -0.0767 -0.0252 7 LEU B CD2 +2412 N N . PHE B 11 ? 1.5169 1.5718 1.2752 0.3997 -0.0789 -0.0342 8 PHE B N +2413 C CA . PHE B 11 ? 1.3134 1.3622 1.0669 0.3994 -0.0777 -0.0351 8 PHE B CA +2414 C C . PHE B 11 ? 1.2615 1.3051 1.0189 0.3965 -0.0797 -0.0373 8 PHE B C +2415 O O . PHE B 11 ? 1.2252 1.2640 0.9792 0.3961 -0.0790 -0.0383 8 PHE B O +2416 C CB . PHE B 11 ? 1.3378 1.3906 1.0866 0.4024 -0.0769 -0.0358 8 PHE B CB +2417 C CG . PHE B 11 ? 1.4544 1.5094 1.1971 0.4050 -0.0741 -0.0334 8 PHE B CG +2418 C CD1 . PHE B 11 ? 1.2258 1.2753 0.9618 0.4054 -0.0715 -0.0320 8 PHE B CD1 +2419 C CD2 . PHE B 11 ? 1.2353 1.2980 0.9791 0.4071 -0.0742 -0.0324 8 PHE B CD2 +2420 C CE1 . PHE B 11 ? 1.3249 1.3764 1.0554 0.4078 -0.0689 -0.0299 8 PHE B CE1 +2421 C CE2 . PHE B 11 ? 1.3500 1.4148 1.0883 0.4095 -0.0716 -0.0301 8 PHE B CE2 +2422 C CZ . PHE B 11 ? 1.3817 1.4408 1.1132 0.4099 -0.0690 -0.0289 8 PHE B CZ +2423 N N . THR B 12 ? 1.4125 1.4573 1.1770 0.3946 -0.0820 -0.0382 9 THR B N +2424 C CA . THR B 12 ? 1.4481 1.4870 1.2166 0.3914 -0.0835 -0.0396 9 THR B CA +2425 C C . THR B 12 ? 1.6129 1.6446 1.3785 0.3897 -0.0815 -0.0375 9 THR B C +2426 O O . THR B 12 ? 1.7354 1.7681 1.4992 0.3905 -0.0799 -0.0350 9 THR B O +2427 C CB . THR B 12 ? 0.8208 0.8626 0.5976 0.3897 -0.0864 -0.0407 9 THR B CB +2428 O OG1 . THR B 12 ? 1.3900 1.4316 1.1684 0.3889 -0.0858 -0.0382 9 THR B OG1 +2429 C CG2 . THR B 12 ? 0.8989 0.9493 0.6785 0.3917 -0.0881 -0.0420 9 THR B CG2 +2430 N N . GLY B 13 ? 1.0412 1.0658 0.8063 0.3875 -0.0815 -0.0385 10 GLY B N +2431 C CA . GLY B 13 ? 1.7327 1.7504 1.4954 0.3857 -0.0797 -0.0366 10 GLY B CA +2432 C C . GLY B 13 ? 1.0515 1.0675 0.8064 0.3875 -0.0765 -0.0346 10 GLY B C +2433 O O . GLY B 13 ? 1.1718 1.1926 0.9230 0.3904 -0.0756 -0.0341 10 GLY B O +2434 N N . VAL B 14 ? 1.1030 1.1120 0.8553 0.3858 -0.0750 -0.0334 11 VAL B N +2435 C CA . VAL B 14 ? 1.0165 1.0228 0.7613 0.3871 -0.0720 -0.0316 11 VAL B CA +2436 C C . VAL B 14 ? 1.0062 1.0162 0.7486 0.3891 -0.0703 -0.0289 11 VAL B C +2437 O O . VAL B 14 ? 1.1789 1.1885 0.9242 0.3879 -0.0704 -0.0276 11 VAL B O +2438 C CB . VAL B 14 ? 0.8940 0.8915 0.6370 0.3844 -0.0710 -0.0312 11 VAL B CB +2439 C CG1 . VAL B 14 ? 1.4303 1.4251 1.1657 0.3858 -0.0680 -0.0294 11 VAL B CG1 +2440 C CG2 . VAL B 14 ? 1.0144 1.0084 0.7596 0.3825 -0.0726 -0.0337 11 VAL B CG2 +2441 N N . VAL B 15 ? 1.0514 1.0648 0.7883 0.3921 -0.0686 -0.0283 12 VAL B N +2442 C CA . VAL B 15 ? 1.2248 1.2422 0.9588 0.3944 -0.0668 -0.0259 12 VAL B CA +2443 C C . VAL B 15 ? 1.2803 1.2932 1.0071 0.3950 -0.0638 -0.0241 12 VAL B C +2444 O O . VAL B 15 ? 1.2099 1.2202 0.9320 0.3957 -0.0628 -0.0248 12 VAL B O +2445 C CB . VAL B 15 ? 1.0546 1.0799 0.7874 0.3976 -0.0670 -0.0264 12 VAL B CB +2446 C CG1 . VAL B 15 ? 1.0198 1.0490 0.7494 0.3999 -0.0650 -0.0238 12 VAL B CG1 +2447 C CG2 . VAL B 15 ? 1.0845 1.1150 0.8243 0.3973 -0.0700 -0.0283 12 VAL B CG2 +2448 N N . PRO B 16 ? 1.0740 1.0858 0.7997 0.3948 -0.0623 -0.0218 13 PRO B N +2449 C CA . PRO B 16 ? 1.3818 1.3900 1.1005 0.3957 -0.0593 -0.0200 13 PRO B CA +2450 C C . PRO B 16 ? 0.9549 0.9681 0.6680 0.3994 -0.0576 -0.0192 13 PRO B C +2451 O O . PRO B 16 ? 1.2396 1.2597 0.9544 0.4014 -0.0581 -0.0190 13 PRO B O +2452 C CB . PRO B 16 ? 0.9066 0.9129 0.6267 0.3944 -0.0585 -0.0179 13 PRO B CB +2453 C CG . PRO B 16 ? 1.1653 1.1770 0.8919 0.3942 -0.0607 -0.0181 13 PRO B CG +2454 C CD . PRO B 16 ? 1.0677 1.0814 0.7987 0.3936 -0.0633 -0.0207 13 PRO B CD +2455 N N . ILE B 17 ? 1.2263 1.2360 0.9330 0.4003 -0.0556 -0.0189 14 ILE B N +2456 C CA . ILE B 17 ? 1.1683 1.1819 0.8691 0.4038 -0.0538 -0.0183 14 ILE B CA +2457 C C . ILE B 17 ? 1.0794 1.0899 0.7739 0.4047 -0.0507 -0.0161 14 ILE B C +2458 O O . ILE B 17 ? 1.0726 1.0763 0.7651 0.4028 -0.0498 -0.0156 14 ILE B O +2459 C CB . ILE B 17 ? 1.0247 1.0376 0.7228 0.4046 -0.0541 -0.0202 14 ILE B CB +2460 C CG1 . ILE B 17 ? 1.0590 1.0752 0.7631 0.4039 -0.0570 -0.0226 14 ILE B CG1 +2461 C CG2 . ILE B 17 ? 0.9061 0.9232 0.5982 0.4082 -0.0522 -0.0195 14 ILE B CG2 +2462 C CD1 . ILE B 17 ? 1.3950 1.4102 1.0966 0.4045 -0.0574 -0.0245 14 ILE B CD1 +2463 N N . LEU B 18 ? 1.0292 1.0449 0.7205 0.4076 -0.0492 -0.0147 15 LEU B N +2464 C CA . LEU B 18 ? 1.2934 1.3071 0.9785 0.4089 -0.0462 -0.0125 15 LEU B CA +2465 C C . LEU B 18 ? 1.2116 1.2295 0.8911 0.4124 -0.0446 -0.0123 15 LEU B C +2466 O O . LEU B 18 ? 1.0811 1.1059 0.7623 0.4144 -0.0455 -0.0128 15 LEU B O +2467 C CB . LEU B 18 ? 1.0025 1.0184 0.6898 0.4088 -0.0458 -0.0106 15 LEU B CB +2468 C CG . LEU B 18 ? 1.5508 1.5656 1.2325 0.4102 -0.0428 -0.0083 15 LEU B CG +2469 C CD1 . LEU B 18 ? 1.5295 1.5360 1.2078 0.4083 -0.0414 -0.0079 15 LEU B CD1 +2470 C CD2 . LEU B 18 ? 1.6440 1.6623 1.3292 0.4102 -0.0429 -0.0067 15 LEU B CD2 +2471 N N . VAL B 19 ? 1.1630 1.1769 0.8359 0.4132 -0.0424 -0.0117 16 VAL B N +2472 C CA . VAL B 19 ? 1.1629 1.1802 0.8301 0.4165 -0.0408 -0.0116 16 VAL B CA +2473 C C . VAL B 19 ? 1.2775 1.2933 0.9380 0.4182 -0.0375 -0.0094 16 VAL B C +2474 O O . VAL B 19 ? 1.1845 1.1938 0.8419 0.4168 -0.0362 -0.0087 16 VAL B O +2475 C CB . VAL B 19 ? 1.0437 1.0584 0.7089 0.4164 -0.0413 -0.0134 16 VAL B CB +2476 C CG1 . VAL B 19 ? 0.9998 1.0172 0.6585 0.4197 -0.0394 -0.0130 16 VAL B CG1 +2477 C CG2 . VAL B 19 ? 1.2149 1.2328 0.8863 0.4155 -0.0444 -0.0157 16 VAL B CG2 +2478 N N . GLU B 20 ? 1.1668 1.1888 0.8251 0.4213 -0.0363 -0.0083 17 GLU B N +2479 C CA . GLU B 20 ? 0.8897 0.9114 0.5415 0.4234 -0.0332 -0.0063 17 GLU B CA +2480 C C . GLU B 20 ? 1.3043 1.3298 0.9506 0.4268 -0.0318 -0.0064 17 GLU B C +2481 O O . GLU B 20 ? 1.2752 1.3075 0.9231 0.4288 -0.0326 -0.0069 17 GLU B O +2482 C CB . GLU B 20 ? 1.2458 1.2714 0.8995 0.4241 -0.0326 -0.0045 17 GLU B CB +2483 C CG . GLU B 20 ? 1.5015 1.5238 1.1600 0.4211 -0.0337 -0.0040 17 GLU B CG +2484 C CD . GLU B 20 ? 1.7531 1.7673 1.4085 0.4191 -0.0322 -0.0032 17 GLU B CD +2485 O OE1 . GLU B 20 ? 1.8314 1.8429 1.4804 0.4204 -0.0300 -0.0027 17 GLU B OE1 +2486 O OE2 . GLU B 20 ? 1.7578 1.7684 1.4172 0.4163 -0.0332 -0.0031 17 GLU B OE2 +2487 N N . LEU B 21 ? 1.0777 1.0988 0.7176 0.4275 -0.0296 -0.0059 18 LEU B N +2488 C CA . LEU B 21 ? 1.0291 1.0533 0.6633 0.4307 -0.0280 -0.0058 18 LEU B CA +2489 C C . LEU B 21 ? 1.2137 1.2366 0.8412 0.4327 -0.0247 -0.0038 18 LEU B C +2490 O O . LEU B 21 ? 1.4757 1.4923 1.1007 0.4312 -0.0234 -0.0029 18 LEU B O +2491 C CB . LEU B 21 ? 1.3320 1.3530 0.9646 0.4302 -0.0287 -0.0076 18 LEU B CB +2492 C CG . LEU B 21 ? 0.9687 0.9919 0.5952 0.4333 -0.0272 -0.0077 18 LEU B CG +2493 C CD1 . LEU B 21 ? 1.7000 1.7317 1.3280 0.4359 -0.0278 -0.0081 18 LEU B CD1 +2494 C CD2 . LEU B 21 ? 1.3681 1.3870 0.9931 0.4323 -0.0279 -0.0093 18 LEU B CD2 +2495 N N . ASP B 22 ? 1.1857 1.2146 0.8102 0.4360 -0.0234 -0.0031 19 ASP B N +2496 C CA . ASP B 22 ? 1.4413 1.4698 1.0589 0.4384 -0.0202 -0.0014 19 ASP B CA +2497 C C . ASP B 22 ? 1.4500 1.4804 1.0624 0.4411 -0.0191 -0.0020 19 ASP B C +2498 O O . ASP B 22 ? 1.3371 1.3740 0.9505 0.4432 -0.0198 -0.0027 19 ASP B O +2499 C CB . ASP B 22 ? 1.3195 1.3539 0.9380 0.4403 -0.0192 0.0002 19 ASP B CB +2500 C CG . ASP B 22 ? 1.7173 1.7489 1.3385 0.4381 -0.0191 0.0015 19 ASP B CG +2501 O OD1 . ASP B 22 ? 1.8298 1.8542 1.4497 0.4359 -0.0186 0.0017 19 ASP B OD1 +2502 O OD2 . ASP B 22 ? 2.1296 2.1662 1.7541 0.4387 -0.0195 0.0023 19 ASP B OD2 +2503 N N . GLY B 23 ? 1.4066 1.4315 1.0134 0.4412 -0.0173 -0.0017 20 GLY B N +2504 C CA . GLY B 23 ? 0.8331 0.8589 0.4351 0.4433 -0.0165 -0.0024 20 GLY B CA +2505 C C . GLY B 23 ? 1.4587 1.4842 1.0532 0.4460 -0.0133 -0.0009 20 GLY B C +2506 O O . GLY B 23 ? 1.4929 1.5152 1.0850 0.4457 -0.0114 0.0006 20 GLY B O +2507 N N . ASP B 24 ? 1.6189 1.6479 1.2100 0.4487 -0.0126 -0.0014 21 ASP B N +2508 C CA . ASP B 24 ? 1.1369 1.1661 0.7207 0.4516 -0.0096 -0.0002 21 ASP B CA +2509 C C . ASP B 24 ? 1.3190 1.3484 0.8994 0.4530 -0.0097 -0.0015 21 ASP B C +2510 O O . ASP B 24 ? 1.3889 1.4245 0.9706 0.4548 -0.0107 -0.0024 21 ASP B O +2511 C CB . ASP B 24 ? 2.0053 2.0416 1.5888 0.4544 -0.0084 0.0009 21 ASP B CB +2512 C CG . ASP B 24 ? 2.1573 2.1929 1.7337 0.4569 -0.0050 0.0026 21 ASP B CG +2513 O OD1 . ASP B 24 ? 1.9274 1.9583 1.4986 0.4571 -0.0036 0.0027 21 ASP B OD1 +2514 O OD2 . ASP B 24 ? 1.5553 1.5952 1.1314 0.4587 -0.0037 0.0040 21 ASP B OD2 +2515 N N . VAL B 25 ? 1.3308 1.3538 0.9071 0.4521 -0.0088 -0.0015 22 VAL B N +2516 C CA . VAL B 25 ? 1.4007 1.4232 0.9737 0.4532 -0.0089 -0.0026 22 VAL B CA +2517 C C . VAL B 25 ? 1.4013 1.4210 0.9665 0.4551 -0.0058 -0.0014 22 VAL B C +2518 O O . VAL B 25 ? 1.0978 1.1106 0.6602 0.4535 -0.0048 -0.0008 22 VAL B O +2519 C CB . VAL B 25 ? 1.0732 1.0908 0.6495 0.4500 -0.0113 -0.0043 22 VAL B CB +2520 C CG1 . VAL B 25 ? 1.1546 1.1701 0.7265 0.4509 -0.0109 -0.0051 22 VAL B CG1 +2521 C CG2 . VAL B 25 ? 1.4290 1.4511 1.0125 0.4490 -0.0143 -0.0059 22 VAL B CG2 +2522 N N . ASN B 26 ? 1.2948 1.3200 0.8564 0.4586 -0.0044 -0.0010 23 ASN B N +2523 C CA . ASN B 26 ? 1.2554 1.2792 0.8096 0.4610 -0.0013 0.0002 23 ASN B CA +2524 C C . ASN B 26 ? 1.6278 1.6487 1.1801 0.4607 0.0008 0.0021 23 ASN B C +2525 O O . ASN B 26 ? 1.1867 1.2018 0.7345 0.4603 0.0026 0.0029 23 ASN B O +2526 C CB . ASN B 26 ? 1.1778 1.1959 0.7280 0.4604 -0.0010 -0.0003 23 ASN B CB +2527 C CG . ASN B 26 ? 1.6401 1.6620 1.1895 0.4621 -0.0020 -0.0018 23 ASN B CG +2528 O OD1 . ASN B 26 ? 1.2771 1.3055 0.8299 0.4633 -0.0034 -0.0026 23 ASN B OD1 +2529 N ND2 . ASN B 26 ? 1.3724 1.3900 0.9194 0.4614 -0.0015 -0.0017 23 ASN B ND2 +2530 N N . GLY B 27 ? 1.3791 1.4041 0.9353 0.4608 0.0005 0.0027 24 GLY B N +2531 C CA . GLY B 27 ? 1.3121 1.3350 0.8675 0.4604 0.0022 0.0043 24 GLY B CA +2532 C C . GLY B 27 ? 1.4998 1.5152 1.0570 0.4567 0.0015 0.0044 24 GLY B C +2533 O O . GLY B 27 ? 1.4587 1.4713 1.0144 0.4563 0.0031 0.0058 24 GLY B O +2534 N N . HIS B 28 ? 1.4575 1.4696 1.0178 0.4541 -0.0008 0.0030 25 HIS B N +2535 C CA . HIS B 28 ? 1.5163 1.5220 1.0798 0.4504 -0.0020 0.0028 25 HIS B CA +2536 C C . HIS B 28 ? 1.5393 1.5481 1.1101 0.4487 -0.0044 0.0023 25 HIS B C +2537 O O . HIS B 28 ? 1.0814 1.0938 0.6563 0.4485 -0.0066 0.0009 25 HIS B O +2538 C CB . HIS B 28 ? 1.0197 1.0202 0.5832 0.4482 -0.0034 0.0015 25 HIS B CB +2539 C CG . HIS B 28 ? 1.8375 1.8336 1.3942 0.4492 -0.0013 0.0020 25 HIS B CG +2540 N ND1 . HIS B 28 ? 1.6403 1.6395 1.1924 0.4522 -0.0001 0.0019 25 HIS B ND1 +2541 C CD2 . HIS B 28 ? 1.7717 1.7607 1.3255 0.4474 -0.0001 0.0026 25 HIS B CD2 +2542 C CE1 . HIS B 28 ? 1.4440 1.4380 0.9906 0.4523 0.0017 0.0024 25 HIS B CE1 +2543 N NE2 . HIS B 28 ? 1.9120 1.8998 1.4595 0.4494 0.0017 0.0029 25 HIS B NE2 +2544 N N . LYS B 29 ? 1.1825 1.1898 0.7549 0.4475 -0.0038 0.0034 26 LYS B N +2545 C CA . LYS B 29 ? 1.2194 1.2295 0.7987 0.4459 -0.0059 0.0032 26 LYS B CA +2546 C C . LYS B 29 ? 1.4126 1.4163 0.9956 0.4420 -0.0077 0.0024 26 LYS B C +2547 O O . LYS B 29 ? 1.4501 1.4474 1.0298 0.4407 -0.0068 0.0025 26 LYS B O +2548 C CB . LYS B 29 ? 1.3549 1.3676 0.9341 0.4470 -0.0044 0.0049 26 LYS B CB +2549 C CG . LYS B 29 ? 1.0282 1.0476 0.6041 0.4510 -0.0026 0.0057 26 LYS B CG +2550 C CD . LYS B 29 ? 1.5710 1.5927 1.1470 0.4518 -0.0011 0.0075 26 LYS B CD +2551 C CE . LYS B 29 ? 1.4907 1.5199 1.0646 0.4556 0.0004 0.0082 26 LYS B CE +2552 N NZ . LYS B 29 ? 1.8037 1.8401 1.3827 0.4563 -0.0018 0.0072 26 LYS B NZ +2553 N N . PHE B 30 ? 1.2535 1.2589 0.8432 0.4401 -0.0102 0.0016 27 PHE B N +2554 C CA . PHE B 30 ? 1.2309 1.2308 0.8249 0.4363 -0.0121 0.0008 27 PHE B CA +2555 C C . PHE B 30 ? 1.2679 1.2714 0.8695 0.4349 -0.0147 0.0001 27 PHE B C +2556 O O . PHE B 30 ? 1.2740 1.2844 0.8777 0.4367 -0.0155 -0.0002 27 PHE B O +2557 C CB . PHE B 30 ? 1.4078 1.4036 1.0011 0.4349 -0.0132 -0.0008 27 PHE B CB +2558 C CG . PHE B 30 ? 1.3724 1.3732 0.9676 0.4362 -0.0150 -0.0024 27 PHE B CG +2559 C CD1 . PHE B 30 ? 1.3616 1.3658 0.9521 0.4394 -0.0136 -0.0024 27 PHE B CD1 +2560 C CD2 . PHE B 30 ? 1.2495 1.2516 0.8514 0.4343 -0.0179 -0.0039 27 PHE B CD2 +2561 C CE1 . PHE B 30 ? 1.3695 1.3784 0.9617 0.4406 -0.0152 -0.0039 27 PHE B CE1 +2562 C CE2 . PHE B 30 ? 1.2457 1.2525 0.8493 0.4355 -0.0195 -0.0055 27 PHE B CE2 +2563 C CZ . PHE B 30 ? 1.2107 1.2209 0.8094 0.4386 -0.0182 -0.0054 27 PHE B CZ +2564 N N . SER B 31 ? 1.1952 1.1942 0.8008 0.4315 -0.0160 -0.0001 28 SER B N +2565 C CA . SER B 31 ? 1.1445 1.1462 0.7576 0.4298 -0.0185 -0.0008 28 SER B CA +2566 C C . SER B 31 ? 1.2894 1.2859 0.9066 0.4263 -0.0208 -0.0023 28 SER B C +2567 O O . SER B 31 ? 1.1983 1.1880 0.8132 0.4245 -0.0201 -0.0022 28 SER B O +2568 C CB . SER B 31 ? 1.1901 1.1930 0.8049 0.4296 -0.0178 0.0008 28 SER B CB +2569 O OG . SER B 31 ? 1.5978 1.6065 1.2098 0.4329 -0.0161 0.0020 28 SER B OG +2570 N N . VAL B 32 ? 1.1896 1.1894 0.8130 0.4253 -0.0235 -0.0037 29 VAL B N +2571 C CA . VAL B 32 ? 1.1655 1.1614 0.7937 0.4221 -0.0259 -0.0053 29 VAL B CA +2572 C C . VAL B 32 ? 1.0514 1.0498 0.6871 0.4204 -0.0282 -0.0057 29 VAL B C +2573 O O . VAL B 32 ? 1.0157 1.0208 0.6541 0.4220 -0.0291 -0.0058 29 VAL B O +2574 C CB . VAL B 32 ? 1.2570 1.2538 0.8851 0.4226 -0.0272 -0.0072 29 VAL B CB +2575 C CG1 . VAL B 32 ? 1.2247 1.2166 0.8573 0.4191 -0.0295 -0.0088 29 VAL B CG1 +2576 C CG2 . VAL B 32 ? 0.7923 0.7871 0.4130 0.4245 -0.0250 -0.0068 29 VAL B CG2 +2577 N N . SER B 33 ? 1.1158 1.1089 0.7548 0.4171 -0.0291 -0.0057 30 SER B N +2578 C CA . SER B 33 ? 1.3514 1.3459 0.9979 0.4149 -0.0315 -0.0064 30 SER B CA +2579 C C . SER B 33 ? 1.4017 1.3924 1.0520 0.4122 -0.0339 -0.0084 30 SER B C +2580 O O . SER B 33 ? 1.1172 1.1015 0.7655 0.4104 -0.0334 -0.0087 30 SER B O +2581 C CB . SER B 33 ? 1.0664 1.0583 0.7143 0.4133 -0.0309 -0.0048 30 SER B CB +2582 O OG . SER B 33 ? 1.6161 1.6125 1.2618 0.4158 -0.0292 -0.0031 30 SER B OG +2583 N N . GLY B 34 ? 1.3829 1.3778 1.0391 0.4118 -0.0364 -0.0098 31 GLY B N +2584 C CA . GLY B 34 ? 0.8777 0.8697 0.5382 0.4092 -0.0387 -0.0118 31 GLY B CA +2585 C C . GLY B 34 ? 1.1878 1.1812 0.8559 0.4071 -0.0411 -0.0123 31 GLY B C +2586 O O . GLY B 34 ? 1.1283 1.1277 0.7992 0.4085 -0.0417 -0.0120 31 GLY B O +2587 N N . GLU B 35 ? 0.9668 0.9546 0.6383 0.4038 -0.0423 -0.0131 32 GLU B N +2588 C CA . GLU B 35 ? 1.2314 1.2202 0.9104 0.4016 -0.0448 -0.0140 32 GLU B CA +2589 C C . GLU B 35 ? 1.2086 1.1944 0.8913 0.3993 -0.0470 -0.0163 32 GLU B C +2590 O O . GLU B 35 ? 1.2076 1.1880 0.8873 0.3983 -0.0465 -0.0168 32 GLU B O +2591 C CB . GLU B 35 ? 1.1089 1.0942 0.7897 0.3995 -0.0444 -0.0125 32 GLU B CB +2592 C CG . GLU B 35 ? 1.2252 1.2024 0.9042 0.3969 -0.0435 -0.0123 32 GLU B CG +2593 C CD . GLU B 35 ? 2.2482 2.2226 1.9258 0.3961 -0.0418 -0.0102 32 GLU B CD +2594 O OE1 . GLU B 35 ? 2.2748 2.2528 1.9554 0.3965 -0.0421 -0.0092 32 GLU B OE1 +2595 O OE2 . GLU B 35 ? 2.7388 2.7076 2.4124 0.3952 -0.0402 -0.0095 32 GLU B OE2 +2596 N N . GLY B 36 ? 1.4642 1.4536 1.1532 0.3986 -0.0496 -0.0177 33 GLY B N +2597 C CA . GLY B 36 ? 1.1071 1.0939 0.8006 0.3962 -0.0519 -0.0199 33 GLY B CA +2598 C C . GLY B 36 ? 1.0125 1.0042 0.7131 0.3958 -0.0545 -0.0210 33 GLY B C +2599 O O . GLY B 36 ? 1.0913 1.0862 0.7943 0.3961 -0.0546 -0.0198 33 GLY B O +2600 N N . GLU B 37 ? 1.2215 1.2139 0.9254 0.3951 -0.0566 -0.0233 34 GLU B N +2601 C CA . GLU B 37 ? 1.1707 1.1674 0.8817 0.3944 -0.0594 -0.0247 34 GLU B CA +2602 C C . GLU B 37 ? 1.0556 1.0553 0.7675 0.3954 -0.0610 -0.0271 34 GLU B C +2603 O O . GLU B 37 ? 1.2215 1.2183 0.9297 0.3956 -0.0603 -0.0279 34 GLU B O +2604 C CB . GLU B 37 ? 1.0320 1.0238 0.7484 0.3907 -0.0609 -0.0253 34 GLU B CB +2605 C CG . GLU B 37 ? 1.9008 1.8863 1.6166 0.3886 -0.0612 -0.0268 34 GLU B CG +2606 C CD . GLU B 37 ? 1.8810 1.8613 1.6018 0.3849 -0.0625 -0.0271 34 GLU B CD +2607 O OE1 . GLU B 37 ? 1.8896 1.8719 1.6154 0.3840 -0.0637 -0.0268 34 GLU B OE1 +2608 O OE2 . GLU B 37 ? 1.8632 1.8374 1.5828 0.3829 -0.0622 -0.0277 34 GLU B OE2 +2609 N N . GLY B 38 ? 1.1429 1.1486 0.8599 0.3960 -0.0631 -0.0282 35 GLY B N +2610 C CA . GLY B 38 ? 1.2314 1.2411 0.9497 0.3972 -0.0647 -0.0305 35 GLY B CA +2611 C C . GLY B 38 ? 1.2213 1.2327 0.9473 0.3954 -0.0678 -0.0325 35 GLY B C +2612 O O . GLY B 38 ? 1.2194 1.2329 0.9503 0.3945 -0.0689 -0.0320 35 GLY B O +2613 N N . ASP B 39 ? 1.2238 1.2345 0.9511 0.3949 -0.0693 -0.0349 36 ASP B N +2614 C CA . ASP B 39 ? 1.2149 1.2268 0.9493 0.3931 -0.0723 -0.0372 36 ASP B CA +2615 C C . ASP B 39 ? 0.9058 0.9237 0.6411 0.3951 -0.0737 -0.0393 36 ASP B C +2616 O O . ASP B 39 ? 1.1308 1.1467 0.8644 0.3951 -0.0740 -0.0410 36 ASP B O +2617 C CB . ASP B 39 ? 1.1228 1.1272 0.8587 0.3899 -0.0729 -0.0384 36 ASP B CB +2618 C CG . ASP B 39 ? 1.6502 1.6532 1.3934 0.3870 -0.0750 -0.0390 36 ASP B CG +2619 O OD1 . ASP B 39 ? 1.6302 1.6388 1.3781 0.3875 -0.0766 -0.0394 36 ASP B OD1 +2620 O OD2 . ASP B 39 ? 1.4386 1.4350 1.1828 0.3842 -0.0750 -0.0391 36 ASP B OD2 +2621 N N . ALA B 40 ? 1.2776 1.3028 1.0154 0.3969 -0.0746 -0.0392 37 ALA B N +2622 C CA . ALA B 40 ? 1.0166 1.0481 0.7549 0.3990 -0.0759 -0.0411 37 ALA B CA +2623 C C . ALA B 40 ? 0.8955 0.9265 0.6394 0.3972 -0.0787 -0.0441 37 ALA B C +2624 O O . ALA B 40 ? 1.2773 1.3112 1.0207 0.3985 -0.0796 -0.0460 37 ALA B O +2625 C CB . ALA B 40 ? 0.8429 0.8825 0.5831 0.4011 -0.0762 -0.0402 37 ALA B CB +2626 N N . THR B 41 ? 1.2865 1.3140 1.0357 0.3942 -0.0801 -0.0445 38 THR B N +2627 C CA . THR B 41 ? 0.8936 0.9202 0.6486 0.3922 -0.0829 -0.0472 38 THR B CA +2628 C C . THR B 41 ? 1.1710 1.1934 0.9231 0.3918 -0.0827 -0.0489 38 THR B C +2629 O O . THR B 41 ? 1.1804 1.2051 0.9351 0.3919 -0.0846 -0.0515 38 THR B O +2630 C CB . THR B 41 ? 1.1497 1.1718 0.9098 0.3889 -0.0838 -0.0470 38 THR B CB +2631 O OG1 . THR B 41 ? 1.3055 1.3312 1.0680 0.3892 -0.0838 -0.0451 38 THR B OG1 +2632 C CG2 . THR B 41 ? 0.6464 0.6683 0.4128 0.3869 -0.0868 -0.0498 38 THR B CG2 +2633 N N . TYR B 42 ? 1.0328 1.0491 0.7795 0.3913 -0.0804 -0.0475 39 TYR B N +2634 C CA . TYR B 42 ? 1.2054 1.2174 0.9486 0.3910 -0.0800 -0.0488 39 TYR B CA +2635 C C . TYR B 42 ? 0.9579 0.9702 0.6933 0.3936 -0.0773 -0.0472 39 TYR B C +2636 O O . TYR B 42 ? 1.1002 1.1071 0.8313 0.3931 -0.0760 -0.0471 39 TYR B O +2637 C CB . TYR B 42 ? 0.8853 0.8891 0.6296 0.3876 -0.0798 -0.0487 39 TYR B CB +2638 C CG . TYR B 42 ? 1.0376 1.0405 0.7891 0.3849 -0.0818 -0.0493 39 TYR B CG +2639 C CD1 . TYR B 42 ? 1.0912 1.0946 0.8485 0.3834 -0.0845 -0.0521 39 TYR B CD1 +2640 C CD2 . TYR B 42 ? 1.2096 1.2113 0.9621 0.3840 -0.0810 -0.0471 39 TYR B CD2 +2641 C CE1 . TYR B 42 ? 1.1521 1.1547 0.9160 0.3810 -0.0863 -0.0526 39 TYR B CE1 +2642 C CE2 . TYR B 42 ? 1.4491 1.4501 1.2082 0.3816 -0.0828 -0.0476 39 TYR B CE2 +2643 C CZ . TYR B 42 ? 1.3922 1.3937 1.1570 0.3801 -0.0855 -0.0503 39 TYR B CZ +2644 O OH . TYR B 42 ? 1.1481 1.1488 0.9193 0.3777 -0.0873 -0.0507 39 TYR B OH +2645 N N . GLY B 43 ? 1.0400 1.0586 0.7736 0.3964 -0.0766 -0.0461 40 GLY B N +2646 C CA . GLY B 43 ? 1.1095 1.1298 0.8358 0.3994 -0.0742 -0.0448 40 GLY B CA +2647 C C . GLY B 43 ? 1.2319 1.2456 0.9522 0.3989 -0.0715 -0.0428 40 GLY B C +2648 O O . GLY B 43 ? 0.9617 0.9736 0.6768 0.4000 -0.0703 -0.0430 40 GLY B O +2649 N N . LYS B 44 ? 1.0474 1.0577 0.7684 0.3973 -0.0707 -0.0410 41 LYS B N +2650 C CA . LYS B 44 ? 0.8118 0.8148 0.5285 0.3959 -0.0686 -0.0394 41 LYS B CA +2651 C C . LYS B 44 ? 1.2241 1.2272 0.9367 0.3971 -0.0661 -0.0365 41 LYS B C +2652 O O . LYS B 44 ? 1.2377 1.2444 0.9531 0.3975 -0.0664 -0.0355 41 LYS B O +2653 C CB . LYS B 44 ? 0.9772 0.9744 0.6987 0.3921 -0.0699 -0.0402 41 LYS B CB +2654 C CG . LYS B 44 ? 1.2474 1.2370 0.9653 0.3904 -0.0683 -0.0394 41 LYS B CG +2655 C CD . LYS B 44 ? 1.0472 1.0315 0.7700 0.3867 -0.0694 -0.0397 41 LYS B CD +2656 C CE . LYS B 44 ? 1.5010 1.4787 1.2197 0.3854 -0.0672 -0.0378 41 LYS B CE +2657 N NZ . LYS B 44 ? 1.5355 1.5067 1.2576 0.3817 -0.0681 -0.0386 41 LYS B NZ +2658 N N . LEU B 45 ? 1.4149 1.4141 1.1210 0.3978 -0.0637 -0.0352 42 LEU B N +2659 C CA . LEU B 45 ? 1.2812 1.2807 0.9825 0.3994 -0.0611 -0.0325 42 LEU B CA +2660 C C . LEU B 45 ? 0.8107 0.8027 0.5075 0.3979 -0.0591 -0.0312 42 LEU B C +2661 O O . LEU B 45 ? 1.2206 1.2091 0.9140 0.3978 -0.0585 -0.0318 42 LEU B O +2662 C CB . LEU B 45 ? 1.0053 1.0105 0.7019 0.4031 -0.0600 -0.0322 42 LEU B CB +2663 C CG . LEU B 45 ? 1.1362 1.1455 0.8296 0.4056 -0.0580 -0.0299 42 LEU B CG +2664 C CD1 . LEU B 45 ? 1.6488 1.6628 1.3479 0.4053 -0.0595 -0.0297 42 LEU B CD1 +2665 C CD2 . LEU B 45 ? 1.1932 1.2074 0.8819 0.4090 -0.0571 -0.0301 42 LEU B CD2 +2666 N N . THR B 46 ? 1.0603 1.0496 0.7572 0.3967 -0.0580 -0.0293 43 THR B N +2667 C CA . THR B 46 ? 1.2626 1.2451 0.9552 0.3954 -0.0559 -0.0278 43 THR B CA +2668 C C . THR B 46 ? 1.1042 1.0878 0.7929 0.3970 -0.0536 -0.0253 43 THR B C +2669 O O . THR B 46 ? 1.2249 1.2106 0.9168 0.3967 -0.0539 -0.0243 43 THR B O +2670 C CB . THR B 46 ? 0.9657 0.9422 0.6627 0.3916 -0.0569 -0.0282 43 THR B CB +2671 O OG1 . THR B 46 ? 1.5847 1.5629 1.2856 0.3908 -0.0574 -0.0271 43 THR B OG1 +2672 C CG2 . THR B 46 ? 1.1829 1.1584 0.8849 0.3897 -0.0595 -0.0308 43 THR B CG2 +2673 N N . LEU B 47 ? 1.1836 1.1657 0.8654 0.3987 -0.0512 -0.0241 44 LEU B N +2674 C CA . LEU B 47 ? 1.1835 1.1669 0.8609 0.4006 -0.0488 -0.0217 44 LEU B CA +2675 C C . LEU B 47 ? 1.0980 1.0754 0.7694 0.4002 -0.0464 -0.0204 44 LEU B C +2676 O O . LEU B 47 ? 0.9696 0.9439 0.6380 0.4001 -0.0460 -0.0212 44 LEU B O +2677 C CB . LEU B 47 ? 0.9608 0.9514 0.6355 0.4044 -0.0482 -0.0216 44 LEU B CB +2678 C CG . LEU B 47 ? 1.2965 1.2941 0.9768 0.4051 -0.0502 -0.0223 44 LEU B CG +2679 C CD1 . LEU B 47 ? 1.2213 1.2258 0.8987 0.4088 -0.0497 -0.0224 44 LEU B CD1 +2680 C CD2 . LEU B 47 ? 1.1054 1.1037 0.7884 0.4044 -0.0499 -0.0206 44 LEU B CD2 +2681 N N . LYS B 48 ? 0.9474 0.9232 0.6172 0.4000 -0.0447 -0.0184 45 LYS B N +2682 C CA . LYS B 48 ? 0.8247 0.7955 0.4884 0.4000 -0.0422 -0.0169 45 LYS B CA +2683 C C . LYS B 48 ? 1.2274 1.2016 0.8860 0.4031 -0.0398 -0.0149 45 LYS B C +2684 O O . LYS B 48 ? 0.9786 0.9567 0.6394 0.4038 -0.0398 -0.0140 45 LYS B O +2685 C CB . LYS B 48 ? 0.8619 0.8264 0.5274 0.3967 -0.0421 -0.0161 45 LYS B CB +2686 C CG . LYS B 48 ? 0.9829 0.9416 0.6426 0.3963 -0.0398 -0.0150 45 LYS B CG +2687 C CD . LYS B 48 ? 1.0706 1.0244 0.7315 0.3938 -0.0392 -0.0138 45 LYS B CD +2688 C CE . LYS B 48 ? 1.2498 1.1969 0.9062 0.3925 -0.0376 -0.0133 45 LYS B CE +2689 N NZ . LYS B 48 ? 1.1008 1.0440 0.7574 0.3906 -0.0366 -0.0119 45 LYS B NZ +2690 N N . PHE B 49 ? 1.3887 1.3615 1.0407 0.4048 -0.0378 -0.0143 46 PHE B N +2691 C CA . PHE B 49 ? 1.2130 1.1890 0.8596 0.4079 -0.0354 -0.0126 46 PHE B CA +2692 C C . PHE B 49 ? 0.9358 0.9063 0.5772 0.4075 -0.0329 -0.0109 46 PHE B C +2693 O O . PHE B 49 ? 1.2033 1.1684 0.8420 0.4062 -0.0324 -0.0112 46 PHE B O +2694 C CB . PHE B 49 ? 1.1361 1.1165 0.7794 0.4109 -0.0351 -0.0133 46 PHE B CB +2695 C CG . PHE B 49 ? 1.0542 1.0406 0.7025 0.4116 -0.0375 -0.0149 46 PHE B CG +2696 C CD1 . PHE B 49 ? 1.2128 1.2057 0.8632 0.4134 -0.0377 -0.0143 46 PHE B CD1 +2697 C CD2 . PHE B 49 ? 1.0985 1.0842 0.7497 0.4104 -0.0396 -0.0171 46 PHE B CD2 +2698 C CE1 . PHE B 49 ? 1.0020 1.0005 0.6571 0.4140 -0.0399 -0.0157 46 PHE B CE1 +2699 C CE2 . PHE B 49 ? 1.2189 1.2103 0.8748 0.4111 -0.0418 -0.0186 46 PHE B CE2 +2700 C CZ . PHE B 49 ? 1.0009 0.9986 0.6588 0.4128 -0.0419 -0.0179 46 PHE B CZ +2701 N N . ILE B 50 ? 1.2492 1.2211 0.8892 0.4084 -0.0314 -0.0091 47 ILE B N +2702 C CA . ILE B 50 ? 0.9883 0.9559 0.6230 0.4085 -0.0288 -0.0074 47 ILE B CA +2703 C C . ILE B 50 ? 1.3819 1.3537 1.0107 0.4123 -0.0265 -0.0062 47 ILE B C +2704 O O . ILE B 50 ? 1.1858 1.1639 0.8158 0.4144 -0.0267 -0.0059 47 ILE B O +2705 C CB . ILE B 50 ? 1.1135 1.0793 0.7509 0.4067 -0.0286 -0.0061 47 ILE B CB +2706 C CG1 . ILE B 50 ? 1.4515 1.4140 1.0955 0.4030 -0.0310 -0.0073 47 ILE B CG1 +2707 C CG2 . ILE B 50 ? 1.4854 1.4465 1.1174 0.4066 -0.0260 -0.0045 47 ILE B CG2 +2708 C CD1 . ILE B 50 ? 1.5836 1.5385 1.2263 0.4003 -0.0308 -0.0077 47 ILE B CD1 +2709 N N . CYS B 51 ? 1.4342 1.4027 1.0567 0.4132 -0.0245 -0.0056 48 CYS B N +2710 C CA . CYS B 51 ? 1.4760 1.4476 1.0927 0.4165 -0.0219 -0.0041 48 CYS B CA +2711 C C . CYS B 51 ? 1.3656 1.3356 0.9812 0.4162 -0.0203 -0.0022 48 CYS B C +2712 O O . CYS B 51 ? 1.4477 1.4117 1.0616 0.4143 -0.0193 -0.0016 48 CYS B O +2713 C CB . CYS B 51 ? 1.7778 1.7466 1.3880 0.4178 -0.0202 -0.0041 48 CYS B CB +2714 S SG . CYS B 51 ? 1.4580 1.4322 1.0617 0.4224 -0.0177 -0.0028 48 CYS B SG +2715 N N . THR B 52 ? 1.3370 1.3127 0.9539 0.4180 -0.0200 -0.0013 49 THR B N +2716 C CA . THR B 52 ? 1.3440 1.3191 0.9605 0.4178 -0.0186 0.0004 49 THR B CA +2717 C C . THR B 52 ? 1.2623 1.2367 0.8716 0.4202 -0.0154 0.0020 49 THR B C +2718 O O . THR B 52 ? 1.3084 1.2814 0.9165 0.4201 -0.0140 0.0035 49 THR B O +2719 C CB . THR B 52 ? 1.2865 1.2679 0.9077 0.4187 -0.0196 0.0008 49 THR B CB +2720 O OG1 . THR B 52 ? 1.0854 1.0734 0.7060 0.4216 -0.0198 0.0003 49 THR B OG1 +2721 C CG2 . THR B 52 ? 0.9689 0.9495 0.5975 0.4156 -0.0223 -0.0002 49 THR B CG2 +2722 N N . THR B 53 ? 1.4617 1.4369 1.0660 0.4224 -0.0144 0.0017 50 THR B N +2723 C CA . THR B 53 ? 0.9940 0.9690 0.5913 0.4249 -0.0114 0.0031 50 THR B CA +2724 C C . THR B 53 ? 1.3418 1.3105 0.9340 0.4242 -0.0101 0.0029 50 THR B C +2725 O O . THR B 53 ? 1.8595 1.8287 1.4459 0.4267 -0.0081 0.0035 50 THR B O +2726 C CB . THR B 53 ? 1.3172 1.2992 0.9119 0.4288 -0.0106 0.0031 50 THR B CB +2727 O OG1 . THR B 53 ? 1.2028 1.1856 0.7973 0.4292 -0.0117 0.0016 50 THR B OG1 +2728 C CG2 . THR B 53 ? 0.8288 0.8174 0.4283 0.4297 -0.0116 0.0034 50 THR B CG2 +2729 N N . GLY B 54 ? 1.1074 1.0701 0.7019 0.4209 -0.0113 0.0022 51 GLY B N +2730 C CA . GLY B 54 ? 1.3331 1.2901 0.9235 0.4200 -0.0105 0.0020 51 GLY B CA +2731 C C . GLY B 54 ? 0.8643 0.8218 0.4553 0.4201 -0.0120 0.0003 51 GLY B C +2732 O O . GLY B 54 ? 2.1015 2.0614 1.6980 0.4191 -0.0144 -0.0009 51 GLY B O +2733 N N . LYS B 55 ? 1.4063 1.3615 0.9918 0.4212 -0.0107 0.0003 52 LYS B N +2734 C CA . LYS B 55 ? 1.3317 1.2880 0.9172 0.4217 -0.0119 -0.0012 52 LYS B CA +2735 C C . LYS B 55 ? 1.2326 1.1963 0.8186 0.4246 -0.0124 -0.0017 52 LYS B C +2736 O O . LYS B 55 ? 1.3005 1.2688 0.8849 0.4271 -0.0111 -0.0006 52 LYS B O +2737 C CB . LYS B 55 ? 0.9539 0.9062 0.5331 0.4224 -0.0102 -0.0009 52 LYS B CB +2738 C CG . LYS B 55 ? 1.7250 1.6702 1.3053 0.4189 -0.0110 -0.0015 52 LYS B CG +2739 C CD . LYS B 55 ? 2.3124 2.2542 1.8868 0.4197 -0.0097 -0.0014 52 LYS B CD +2740 C CE . LYS B 55 ? 2.4614 2.3959 2.0343 0.4171 -0.0088 -0.0008 52 LYS B CE +2741 N NZ . LYS B 55 ? 2.2627 2.1939 1.8296 0.4179 -0.0073 -0.0006 52 LYS B NZ +2742 N N . LEU B 56 ? 1.3501 1.3151 0.9386 0.4243 -0.0144 -0.0034 53 LEU B N +2743 C CA . LEU B 56 ? 1.3025 1.2745 0.8918 0.4269 -0.0151 -0.0041 53 LEU B CA +2744 C C . LEU B 56 ? 1.1159 1.0891 0.6985 0.4299 -0.0132 -0.0038 53 LEU B C +2745 O O . LEU B 56 ? 1.2664 1.2348 0.8456 0.4292 -0.0127 -0.0040 53 LEU B O +2746 C CB . LEU B 56 ? 1.1878 1.1607 0.7831 0.4251 -0.0182 -0.0061 53 LEU B CB +2747 C CG . LEU B 56 ? 1.2911 1.2716 0.8902 0.4268 -0.0199 -0.0071 53 LEU B CG +2748 C CD1 . LEU B 56 ? 1.1139 1.0974 0.7178 0.4262 -0.0205 -0.0065 53 LEU B CD1 +2749 C CD2 . LEU B 56 ? 0.9128 0.8932 0.5160 0.4253 -0.0225 -0.0092 53 LEU B CD2 +2750 N N . PRO B 57 ? 1.3972 1.3767 0.9777 0.4333 -0.0122 -0.0032 54 PRO B N +2751 C CA . PRO B 57 ? 1.1070 1.0877 0.6811 0.4362 -0.0104 -0.0029 54 PRO B CA +2752 C C . PRO B 57 ? 1.2794 1.2619 0.8542 0.4367 -0.0120 -0.0047 54 PRO B C +2753 O O . PRO B 57 ? 1.2902 1.2716 0.8598 0.4382 -0.0108 -0.0046 54 PRO B O +2754 C CB . PRO B 57 ? 1.1406 1.1280 0.7132 0.4395 -0.0090 -0.0019 54 PRO B CB +2755 C CG . PRO B 57 ? 1.1876 1.1789 0.7670 0.4385 -0.0110 -0.0024 54 PRO B CG +2756 C CD . PRO B 57 ? 1.2527 1.2382 0.8362 0.4345 -0.0124 -0.0027 54 PRO B CD +2757 N N . VAL B 58 ? 1.2413 1.2262 0.8223 0.4354 -0.0147 -0.0062 55 VAL B N +2758 C CA . VAL B 58 ? 1.3841 1.3711 0.9665 0.4357 -0.0165 -0.0080 55 VAL B CA +2759 C C . VAL B 58 ? 1.4502 1.4319 1.0369 0.4320 -0.0188 -0.0094 55 VAL B C +2760 O O . VAL B 58 ? 1.1438 1.1212 0.7331 0.4293 -0.0190 -0.0089 55 VAL B O +2761 C CB . VAL B 58 ? 1.1545 1.1494 0.7407 0.4374 -0.0179 -0.0088 55 VAL B CB +2762 C CG1 . VAL B 58 ? 1.2843 1.2843 0.8657 0.4413 -0.0157 -0.0076 55 VAL B CG1 +2763 C CG2 . VAL B 58 ? 1.2850 1.2809 0.8772 0.4356 -0.0192 -0.0086 55 VAL B CG2 +2764 N N . PRO B 59 ? 1.3739 1.3559 0.9615 0.4319 -0.0203 -0.0110 56 PRO B N +2765 C CA . PRO B 59 ? 1.4036 1.3807 0.9956 0.4283 -0.0224 -0.0123 56 PRO B CA +2766 C C . PRO B 59 ? 1.5108 1.4911 1.1103 0.4268 -0.0249 -0.0134 56 PRO B C +2767 O O . PRO B 59 ? 1.2564 1.2434 0.8577 0.4289 -0.0255 -0.0138 56 PRO B O +2768 C CB . PRO B 59 ? 1.1588 1.1360 0.7494 0.4289 -0.0232 -0.0138 56 PRO B CB +2769 C CG . PRO B 59 ? 1.2559 1.2378 0.8411 0.4328 -0.0215 -0.0131 56 PRO B CG +2770 C CD . PRO B 59 ? 1.2032 1.1899 0.7885 0.4346 -0.0205 -0.0119 56 PRO B CD +2771 N N . TRP B 60 ? 1.3755 1.3512 0.9795 0.4233 -0.0262 -0.0139 57 TRP B N +2772 C CA . TRP B 60 ? 0.9547 0.9330 0.5660 0.4218 -0.0287 -0.0149 57 TRP B CA +2773 C C . TRP B 60 ? 1.0609 1.0447 0.6757 0.4228 -0.0309 -0.0169 57 TRP B C +2774 O O . TRP B 60 ? 0.9571 0.9467 0.5755 0.4238 -0.0319 -0.0171 57 TRP B O +2775 C CB . TRP B 60 ? 1.0377 1.0098 0.6532 0.4178 -0.0299 -0.0153 57 TRP B CB +2776 C CG . TRP B 60 ? 1.1640 1.1330 0.7789 0.4166 -0.0284 -0.0135 57 TRP B CG +2777 C CD1 . TRP B 60 ? 0.9531 0.9157 0.5646 0.4152 -0.0268 -0.0124 57 TRP B CD1 +2778 C CD2 . TRP B 60 ? 1.1825 1.1548 0.8002 0.4169 -0.0284 -0.0126 57 TRP B CD2 +2779 N NE1 . TRP B 60 ? 1.0402 1.0018 0.6522 0.4145 -0.0258 -0.0110 57 TRP B NE1 +2780 C CE2 . TRP B 60 ? 1.0969 1.0645 0.7127 0.4155 -0.0268 -0.0110 57 TRP B CE2 +2781 C CE3 . TRP B 60 ? 1.1463 1.1252 0.7680 0.4181 -0.0297 -0.0131 57 TRP B CE3 +2782 C CZ2 . TRP B 60 ? 0.9935 0.9626 0.6112 0.4154 -0.0264 -0.0098 57 TRP B CZ2 +2783 C CZ3 . TRP B 60 ? 1.1380 1.1184 0.7617 0.4179 -0.0293 -0.0118 57 TRP B CZ3 +2784 C CH2 . TRP B 60 ? 1.0295 1.0051 0.6513 0.4166 -0.0276 -0.0102 57 TRP B CH2 +2785 N N . PRO B 61 ? 1.1994 1.1817 0.8132 0.4227 -0.0316 -0.0183 58 PRO B N +2786 C CA . PRO B 61 ? 0.8725 0.8597 0.4894 0.4236 -0.0338 -0.0203 58 PRO B CA +2787 C C . PRO B 61 ? 0.9769 0.9722 0.5932 0.4270 -0.0336 -0.0202 58 PRO B C +2788 O O . PRO B 61 ? 1.2082 1.2084 0.8295 0.4271 -0.0357 -0.0217 58 PRO B O +2789 C CB . PRO B 61 ? 1.0844 1.0686 0.6974 0.4238 -0.0334 -0.0210 58 PRO B CB +2790 C CG . PRO B 61 ? 1.1075 1.0838 0.7193 0.4211 -0.0326 -0.0202 58 PRO B CG +2791 C CD . PRO B 61 ? 0.9019 0.8775 0.5120 0.4213 -0.0307 -0.0181 58 PRO B CD +2792 N N . THR B 62 ? 1.1687 1.1657 0.7791 0.4297 -0.0310 -0.0185 59 THR B N +2793 C CA . THR B 62 ? 1.2460 1.2506 0.8553 0.4330 -0.0305 -0.0183 59 THR B CA +2794 C C . THR B 62 ? 1.2421 1.2512 0.8567 0.4328 -0.0316 -0.0181 59 THR B C +2795 O O . THR B 62 ? 1.2234 1.2396 0.8390 0.4351 -0.0319 -0.0183 59 THR B O +2796 C CB . THR B 62 ? 1.3207 1.3252 0.9226 0.4356 -0.0273 -0.0162 59 THR B CB +2797 O OG1 . THR B 62 ? 1.2832 1.2825 0.8840 0.4339 -0.0259 -0.0146 59 THR B OG1 +2798 C CG2 . THR B 62 ? 1.1545 1.1567 0.7509 0.4368 -0.0264 -0.0165 59 THR B CG2 +2799 N N . LEU B 63 ? 1.1261 1.1313 0.7442 0.4300 -0.0321 -0.0176 60 LEU B N +2800 C CA . LEU B 63 ? 0.8765 0.8853 0.4992 0.4296 -0.0328 -0.0171 60 LEU B CA +2801 C C . LEU B 63 ? 1.3332 1.3431 0.9638 0.4273 -0.0360 -0.0189 60 LEU B C +2802 O O . LEU B 63 ? 1.0060 1.0199 0.6409 0.4272 -0.0369 -0.0187 60 LEU B O +2803 C CB . LEU B 63 ? 1.1567 1.1612 0.7778 0.4285 -0.0310 -0.0151 60 LEU B CB +2804 C CG . LEU B 63 ? 1.2421 1.2472 0.8562 0.4312 -0.0279 -0.0131 60 LEU B CG +2805 C CD1 . LEU B 63 ? 1.0505 1.0510 0.6638 0.4296 -0.0264 -0.0113 60 LEU B CD1 +2806 C CD2 . LEU B 63 ? 0.9371 0.9505 0.5512 0.4344 -0.0276 -0.0127 60 LEU B CD2 +2807 N N . VAL B 64 ? 1.2436 1.2500 0.8761 0.4254 -0.0376 -0.0206 61 VAL B N +2808 C CA . VAL B 64 ? 1.0575 1.0641 0.6973 0.4229 -0.0405 -0.0225 61 VAL B CA +2809 C C . VAL B 64 ? 1.0427 1.0573 0.6868 0.4244 -0.0422 -0.0234 61 VAL B C +2810 O O . VAL B 64 ? 1.1103 1.1264 0.7602 0.4229 -0.0437 -0.0236 61 VAL B O +2811 C CB . VAL B 64 ? 1.0363 1.0393 0.6769 0.4214 -0.0419 -0.0244 61 VAL B CB +2812 C CG1 . VAL B 64 ? 0.8483 0.8527 0.4965 0.4193 -0.0451 -0.0265 61 VAL B CG1 +2813 C CG2 . VAL B 64 ? 0.9771 0.9718 0.6150 0.4191 -0.0408 -0.0237 61 VAL B CG2 +2814 N N . THR B 65 ? 1.0237 1.0437 0.6652 0.4274 -0.0419 -0.0239 62 THR B N +2815 C CA . THR B 65 ? 1.1665 1.1941 0.8124 0.4287 -0.0437 -0.0250 62 THR B CA +2816 C C . THR B 65 ? 0.9975 1.0296 0.6443 0.4299 -0.0429 -0.0233 62 THR B C +2817 O O . THR B 65 ? 1.4043 1.4421 1.0560 0.4303 -0.0445 -0.0240 62 THR B O +2818 C CB . THR B 65 ? 1.1271 1.1595 0.7698 0.4317 -0.0436 -0.0260 62 THR B CB +2819 O OG1 . THR B 65 ? 1.4620 1.4968 1.0986 0.4346 -0.0409 -0.0241 62 THR B OG1 +2820 C CG2 . THR B 65 ? 1.1461 1.1735 0.7864 0.4308 -0.0438 -0.0273 62 THR B CG2 +2821 N N . THR B 66 ? 1.1469 1.1764 0.7887 0.4307 -0.0402 -0.0211 63 THR B N +2822 C CA . THR B 66 ? 1.1649 1.1989 0.8068 0.4322 -0.0391 -0.0194 63 THR B CA +2823 C C . THR B 66 ? 1.2091 1.2408 0.8565 0.4293 -0.0403 -0.0190 63 THR B C +2824 O O . THR B 66 ? 1.1098 1.1465 0.7616 0.4296 -0.0413 -0.0188 63 THR B O +2825 C CB . THR B 66 ? 1.2215 1.2536 0.8559 0.4341 -0.0357 -0.0172 63 THR B CB +2826 O OG1 . THR B 66 ? 1.1578 1.1896 0.7867 0.4360 -0.0347 -0.0177 63 THR B OG1 +2827 C CG2 . THR B 66 ? 0.9777 1.0159 0.6117 0.4364 -0.0345 -0.0156 63 THR B CG2 +2828 N N . PHE B 67 ? 1.3811 1.4051 1.0282 0.4266 -0.0402 -0.0190 64 PHE B N +2829 C CA . PHE B 67 ? 1.2373 1.2573 0.8892 0.4234 -0.0412 -0.0187 64 PHE B CA +2830 C C . PHE B 67 ? 1.0691 1.0910 0.7290 0.4214 -0.0445 -0.0208 64 PHE B C +2831 O O . PHE B 67 ? 1.3459 1.3717 1.0108 0.4210 -0.0457 -0.0204 64 PHE B O +2832 C CB . PHE B 67 ? 1.3387 1.3500 0.9884 0.4209 -0.0404 -0.0184 64 PHE B CB +2833 C CG . PHE B 67 ? 1.0276 1.0355 0.6708 0.4218 -0.0373 -0.0163 64 PHE B CG +2834 C CD1 . PHE B 67 ? 1.0822 1.0932 0.7231 0.4238 -0.0355 -0.0144 64 PHE B CD1 +2835 C CD2 . PHE B 67 ? 1.2585 1.2596 0.8978 0.4206 -0.0363 -0.0163 64 PHE B CD2 +2836 C CE1 . PHE B 67 ? 1.1416 1.1491 0.7764 0.4245 -0.0327 -0.0126 64 PHE B CE1 +2837 C CE2 . PHE B 67 ? 1.2067 1.2043 0.8400 0.4213 -0.0336 -0.0145 64 PHE B CE2 +2838 C CZ . PHE B 67 ? 1.1410 1.1418 0.7720 0.4233 -0.0318 -0.0126 64 PHE B CZ +2839 N N1 . CR2 B 68 ? 1.1827 1.2020 0.8439 0.4201 -0.0460 -0.0227 65 CR2 B N1 +2840 C CA1 . CR2 B 68 ? 1.2588 1.2818 0.9269 0.4191 -0.0493 -0.0252 65 CR2 B CA1 +2841 C C1 . CR2 B 68 ? 1.3344 1.3643 1.0021 0.4219 -0.0501 -0.0266 65 CR2 B C1 +2842 N N2 . CR2 B 68 ? 1.4977 1.5273 1.1640 0.4224 -0.0508 -0.0284 65 CR2 B N2 +2843 N N3 . CR2 B 68 ? 1.1908 1.2282 0.8597 0.4241 -0.0503 -0.0262 65 CR2 B N3 +2844 C C2 . CR2 B 68 ? 1.1028 1.1448 0.7708 0.4261 -0.0509 -0.0276 65 CR2 B C2 +2845 O O2 . CR2 B 68 ? 1.0920 1.1417 0.7607 0.4286 -0.0512 -0.0277 65 CR2 B O2 +2846 C CA2 . CR2 B 68 ? 1.2916 1.3287 0.9578 0.4251 -0.0513 -0.0291 65 CR2 B CA2 +2847 C CA3 . CR2 B 68 ? 0.6958 0.7360 0.3658 0.4246 -0.0494 -0.0243 65 CR2 B CA3 +2848 C C3 . CR2 B 68 ? 1.5248 1.5672 1.2027 0.4226 -0.0519 -0.0249 65 CR2 B C3 +2849 O O3 . CR2 B 68 ? 1.0126 1.0626 0.6928 0.4244 -0.0522 -0.0243 65 CR2 B O3 +2850 C CB2 . CR2 B 68 ? 0.9997 1.0389 0.6646 0.4265 -0.0521 -0.0311 65 CR2 B CB2 +2851 C CG2 . CR2 B 68 ? 1.3672 1.4008 1.0302 0.4252 -0.0524 -0.0324 65 CR2 B CG2 +2852 C CD1 . CR2 B 68 ? 0.9640 0.9895 0.6260 0.4226 -0.0518 -0.0318 65 CR2 B CD1 +2853 C CD2 . CR2 B 68 ? 1.4178 1.4543 1.0794 0.4269 -0.0531 -0.0341 65 CR2 B CD2 +2854 C CE1 . CR2 B 68 ? 1.4229 1.4436 1.0831 0.4216 -0.0520 -0.0329 65 CR2 B CE1 +2855 C CE2 . CR2 B 68 ? 0.9844 1.0161 0.6440 0.4259 -0.0533 -0.0352 65 CR2 B CE2 +2856 C CZ . CR2 B 68 ? 1.2830 1.3066 0.9419 0.4232 -0.0527 -0.0346 65 CR2 B CZ +2857 O OH . CR2 B 68 ? 1.5083 1.5273 1.1654 0.4222 -0.0530 -0.0358 65 CR2 B OH +2858 N N . VAL B 69 ? 1.4361 1.4750 1.1185 0.4199 -0.0540 -0.0267 68 VAL B N +2859 C CA . VAL B 69 ? 1.1858 1.2273 0.8755 0.4183 -0.0563 -0.0272 68 VAL B CA +2860 C C . VAL B 69 ? 0.8686 0.9134 0.5638 0.4177 -0.0592 -0.0298 68 VAL B C +2861 O O . VAL B 69 ? 1.5971 1.6410 1.2984 0.4153 -0.0613 -0.0307 68 VAL B O +2862 C CB . VAL B 69 ? 1.0556 1.0933 0.7478 0.4160 -0.0560 -0.0256 68 VAL B CB +2863 C CG1 . VAL B 69 ? 1.0391 1.0789 0.7273 0.4180 -0.0535 -0.0230 68 VAL B CG1 +2864 C CG2 . VAL B 69 ? 1.7444 1.7735 1.4365 0.4130 -0.0558 -0.0257 68 VAL B CG2 +2865 N N . GLN B 70 ? 1.2339 1.2833 0.9269 0.4201 -0.0593 -0.0309 69 GLN B N +2866 C CA . GLN B 70 ? 1.3248 1.3777 1.0222 0.4200 -0.0620 -0.0336 69 GLN B CA +2867 C C . GLN B 70 ? 1.1278 1.1850 0.8333 0.4187 -0.0647 -0.0346 69 GLN B C +2868 O O . GLN B 70 ? 1.5069 1.5679 1.2161 0.4188 -0.0670 -0.0369 69 GLN B O +2869 C CB . GLN B 70 ? 1.1494 1.2080 0.8430 0.4233 -0.0615 -0.0342 69 GLN B CB +2870 C CG . GLN B 70 ? 1.4479 1.5023 1.1344 0.4244 -0.0595 -0.0341 69 GLN B CG +2871 C CD . GLN B 70 ? 1.5038 1.5643 1.1858 0.4280 -0.0583 -0.0340 69 GLN B CD +2872 O OE1 . GLN B 70 ? 1.3883 1.4558 1.0718 0.4298 -0.0586 -0.0336 69 GLN B OE1 +2873 N NE2 . GLN B 70 ? 1.4653 1.5230 1.1418 0.4290 -0.0571 -0.0343 69 GLN B NE2 +2874 N N . CYS B 71 ? 1.3478 1.4043 1.0559 0.4174 -0.0645 -0.0330 70 CYS B N +2875 C CA . CYS B 71 ? 1.2364 1.2957 0.9521 0.4158 -0.0671 -0.0337 70 CYS B CA +2876 C C . CYS B 71 ? 1.3690 1.4216 1.0887 0.4122 -0.0685 -0.0348 70 CYS B C +2877 O O . CYS B 71 ? 1.3470 1.4005 1.0732 0.4103 -0.0706 -0.0355 70 CYS B O +2878 C CB . CYS B 71 ? 1.1682 1.2305 0.8848 0.4163 -0.0661 -0.0313 70 CYS B CB +2879 S SG . CYS B 71 ? 1.5413 1.5969 1.2525 0.4157 -0.0629 -0.0283 70 CYS B SG +2880 N N . PHE B 72 ? 1.2136 1.2592 0.9292 0.4112 -0.0674 -0.0350 71 PHE B N +2881 C CA . PHE B 72 ? 1.0759 1.1147 0.7946 0.4079 -0.0685 -0.0361 71 PHE B CA +2882 C C . PHE B 72 ? 1.0484 1.0862 0.7676 0.4076 -0.0700 -0.0388 71 PHE B C +2883 O O . PHE B 72 ? 1.4961 1.5277 1.2164 0.4051 -0.0706 -0.0398 71 PHE B O +2884 C CB . PHE B 72 ? 1.0468 1.0782 0.7613 0.4066 -0.0662 -0.0341 71 PHE B CB +2885 C CG . PHE B 72 ? 1.0930 1.1242 0.8088 0.4059 -0.0654 -0.0319 71 PHE B CG +2886 C CD1 . PHE B 72 ? 1.2083 1.2381 0.9305 0.4033 -0.0672 -0.0322 71 PHE B CD1 +2887 C CD2 . PHE B 72 ? 1.2913 1.3240 1.0021 0.4080 -0.0629 -0.0295 71 PHE B CD2 +2888 C CE1 . PHE B 72 ? 1.0310 1.0608 0.7545 0.4027 -0.0665 -0.0301 71 PHE B CE1 +2889 C CE2 . PHE B 72 ? 1.0358 1.0686 0.7479 0.4075 -0.0622 -0.0274 71 PHE B CE2 +2890 C CZ . PHE B 72 ? 1.4500 1.4813 1.1685 0.4048 -0.0640 -0.0277 71 PHE B CZ +2891 N N . SER B 73 ? 1.0870 1.1310 0.8055 0.4100 -0.0706 -0.0400 72 SER B N +2892 C CA . SER B 73 ? 1.3155 1.3595 1.0351 0.4099 -0.0723 -0.0427 72 SER B CA +2893 C C . SER B 73 ? 1.3038 1.3492 1.0315 0.4077 -0.0754 -0.0449 72 SER B C +2894 O O . SER B 73 ? 1.7599 1.8101 1.4923 0.4077 -0.0766 -0.0447 72 SER B O +2895 C CB . SER B 73 ? 1.1747 1.2253 0.8911 0.4132 -0.0719 -0.0433 72 SER B CB +2896 N N . ARG B 74 ? 1.1424 1.1838 0.8720 0.4058 -0.0768 -0.0470 73 ARG B N +2897 C CA . ARG B 74 ? 1.2377 1.2806 0.9747 0.4041 -0.0799 -0.0495 73 ARG B CA +2898 C C . ARG B 74 ? 1.2107 1.2612 0.9489 0.4063 -0.0814 -0.0515 73 ARG B C +2899 O O . ARG B 74 ? 1.0954 1.1462 0.8300 0.4077 -0.0810 -0.0526 73 ARG B O +2900 C CB . ARG B 74 ? 1.1918 1.2275 0.9299 0.4013 -0.0807 -0.0511 73 ARG B CB +2901 C CG . ARG B 74 ? 1.1673 1.2035 0.9131 0.3990 -0.0838 -0.0536 73 ARG B CG +2902 C CD . ARG B 74 ? 1.0039 1.0323 0.7508 0.3960 -0.0842 -0.0547 73 ARG B CD +2903 N NE . ARG B 74 ? 1.1409 1.1672 0.8842 0.3966 -0.0840 -0.0562 73 ARG B NE +2904 C CZ . ARG B 74 ? 1.4314 1.4618 1.1763 0.3976 -0.0857 -0.0587 73 ARG B CZ +2905 N NH1 . ARG B 74 ? 0.7989 0.8359 0.5491 0.3983 -0.0879 -0.0601 73 ARG B NH1 +2906 N NH2 . ARG B 74 ? 0.9995 1.0276 0.7409 0.3981 -0.0853 -0.0599 73 ARG B NH2 +2907 N N . TYR B 75 ? 1.3256 1.3824 1.0690 0.4067 -0.0831 -0.0518 74 TYR B N +2908 C CA . TYR B 75 ? 1.4182 1.4823 1.1643 0.4083 -0.0850 -0.0540 74 TYR B CA +2909 C C . TYR B 75 ? 1.3984 1.4619 1.1515 0.4059 -0.0881 -0.0569 74 TYR B C +2910 O O . TYR B 75 ? 1.6789 1.7417 1.4375 0.4039 -0.0895 -0.0567 74 TYR B O +2911 C CB . TYR B 75 ? 1.0143 1.0864 0.7617 0.4104 -0.0850 -0.0528 74 TYR B CB +2912 C CG . TYR B 75 ? 1.1923 1.2679 0.9329 0.4137 -0.0826 -0.0512 74 TYR B CG +2913 C CD1 . TYR B 75 ? 1.3655 1.4373 1.1002 0.4143 -0.0796 -0.0484 74 TYR B CD1 +2914 C CD2 . TYR B 75 ? 1.3556 1.4381 1.0955 0.4162 -0.0832 -0.0525 74 TYR B CD2 +2915 C CE1 . TYR B 75 ? 1.2561 1.3309 0.9846 0.4174 -0.0774 -0.0470 74 TYR B CE1 +2916 C CE2 . TYR B 75 ? 1.2209 1.3066 0.9546 0.4193 -0.0810 -0.0511 74 TYR B CE2 +2917 C CZ . TYR B 75 ? 1.3504 1.4322 1.0784 0.4198 -0.0781 -0.0483 74 TYR B CZ +2918 O OH . TYR B 75 ? 1.4544 1.5393 1.1762 0.4229 -0.0758 -0.0469 74 TYR B OH +2919 N N . PRO B 76 ? 1.2233 1.2867 0.9763 0.4061 -0.0893 -0.0595 75 PRO B N +2920 C CA . PRO B 76 ? 1.1653 1.2287 0.9250 0.4041 -0.0923 -0.0624 75 PRO B CA +2921 C C . PRO B 76 ? 1.7088 1.7797 1.4747 0.4044 -0.0945 -0.0632 75 PRO B C +2922 O O . PRO B 76 ? 1.5959 1.6731 1.3602 0.4068 -0.0938 -0.0620 75 PRO B O +2923 C CB . PRO B 76 ? 1.3525 1.4168 1.1097 0.4053 -0.0927 -0.0648 75 PRO B CB +2924 C CG . PRO B 76 ? 1.3105 1.3721 1.0597 0.4070 -0.0898 -0.0629 75 PRO B CG +2925 C CD . PRO B 76 ? 1.3975 1.4612 1.1441 0.4084 -0.0878 -0.0598 75 PRO B CD +2926 N N . ASP B 77 ? 1.5525 1.6227 1.3253 0.4020 -0.0971 -0.0650 76 ASP B N +2927 C CA . ASP B 77 ? 1.6987 1.7755 1.4780 0.4019 -0.0993 -0.0656 76 ASP B CA +2928 C C . ASP B 77 ? 1.7870 1.8727 1.5662 0.4048 -0.1000 -0.0667 76 ASP B C +2929 O O . ASP B 77 ? 1.3418 1.4335 1.1224 0.4060 -0.1001 -0.0654 76 ASP B O +2930 C CB . ASP B 77 ? 2.0085 2.0832 1.7949 0.3990 -0.1021 -0.0681 76 ASP B CB +2931 C CG . ASP B 77 ? 2.2325 2.3004 2.0210 0.3961 -0.1018 -0.0667 76 ASP B CG +2932 O OD1 . ASP B 77 ? 2.0910 2.1596 1.8794 0.3962 -0.1007 -0.0641 76 ASP B OD1 +2933 O OD2 . ASP B 77 ? 2.3266 2.3886 2.1168 0.3938 -0.1026 -0.0682 76 ASP B OD2 +2934 N N . HIS B 78 ? 1.6998 1.7863 1.4772 0.4057 -0.1006 -0.0690 77 HIS B N +2935 C CA . HIS B 78 ? 1.1302 1.2251 0.9077 0.4083 -0.1014 -0.0704 77 HIS B CA +2936 C C . HIS B 78 ? 1.6334 1.7319 1.4046 0.4114 -0.0989 -0.0679 77 HIS B C +2937 O O . HIS B 78 ? 1.7331 1.8390 1.5041 0.4138 -0.0993 -0.0687 77 HIS B O +2938 C CB . HIS B 78 ? 1.1110 1.2054 0.8882 0.4085 -0.1027 -0.0736 77 HIS B CB +2939 C CG . HIS B 78 ? 1.3795 1.4685 1.1495 0.4093 -0.1004 -0.0730 77 HIS B CG +2940 N ND1 . HIS B 78 ? 1.3128 1.3930 1.0814 0.4071 -0.0996 -0.0726 77 HIS B ND1 +2941 C CD2 . HIS B 78 ? 1.4609 1.5521 1.2249 0.4120 -0.0989 -0.0729 77 HIS B CD2 +2942 C CE1 . HIS B 78 ? 1.6009 1.6782 1.3629 0.4083 -0.0976 -0.0722 77 HIS B CE1 +2943 N NE2 . HIS B 78 ? 1.6842 1.7679 1.4433 0.4113 -0.0972 -0.0724 77 HIS B NE2 +2944 N N . MET B 79 ? 1.6229 1.7164 1.3892 0.4114 -0.0962 -0.0651 78 MET B N +2945 C CA . MET B 79 ? 1.3062 1.4024 1.0661 0.4143 -0.0935 -0.0626 78 MET B CA +2946 C C . MET B 79 ? 1.5555 1.6536 1.3162 0.4144 -0.0924 -0.0597 78 MET B C +2947 O O . MET B 79 ? 1.4292 1.5324 1.1867 0.4169 -0.0910 -0.0580 78 MET B O +2948 C CB . MET B 79 ? 1.1618 1.2515 0.9143 0.4147 -0.0909 -0.0616 78 MET B CB +2949 C CG . MET B 79 ? 1.4297 1.5192 1.1801 0.4156 -0.0915 -0.0642 78 MET B CG +2950 S SD . MET B 79 ? 1.3487 1.4314 1.0902 0.4165 -0.0885 -0.0630 78 MET B SD +2951 C CE . MET B 79 ? 1.1586 1.2452 0.8940 0.4196 -0.0855 -0.0597 78 MET B CE +2952 N N . LYS B 80 ? 1.1247 1.2189 0.8896 0.4117 -0.0932 -0.0591 79 LYS B N +2953 C CA . LYS B 80 ? 1.3191 1.4134 1.0843 0.4114 -0.0919 -0.0561 79 LYS B CA +2954 C C . LYS B 80 ? 1.4436 1.5465 1.2098 0.4136 -0.0919 -0.0548 79 LYS B C +2955 O O . LYS B 80 ? 1.7543 1.8575 1.5211 0.4133 -0.0910 -0.0523 79 LYS B O +2956 C CB . LYS B 80 ? 0.9934 1.0835 0.7646 0.4081 -0.0935 -0.0562 79 LYS B CB +2957 C CG . LYS B 80 ? 1.6113 1.6920 1.3808 0.4058 -0.0928 -0.0564 79 LYS B CG +2958 C CD . LYS B 80 ? 1.2796 1.3562 1.0544 0.4027 -0.0939 -0.0560 79 LYS B CD +2959 C CE . LYS B 80 ? 1.3300 1.3972 1.1031 0.4004 -0.0932 -0.0562 79 LYS B CE +2960 N NZ . LYS B 80 ? 1.4978 1.5603 1.2636 0.4011 -0.0900 -0.0536 79 LYS B NZ +2961 N N . GLN B 81 ? 1.6648 1.7747 1.4312 0.4157 -0.0928 -0.0564 80 GLN B N +2962 C CA . GLN B 81 ? 1.6849 1.8033 1.4520 0.4178 -0.0928 -0.0553 80 GLN B CA +2963 C C . GLN B 81 ? 1.6480 1.7685 1.4075 0.4210 -0.0901 -0.0539 80 GLN B C +2964 O O . GLN B 81 ? 1.9131 2.0401 1.6718 0.4230 -0.0894 -0.0525 80 GLN B O +2965 C CB . GLN B 81 ? 1.4838 1.6095 1.2573 0.4179 -0.0959 -0.0579 80 GLN B CB +2966 C CG . GLN B 81 ? 1.4043 1.5320 1.1763 0.4191 -0.0968 -0.0608 80 GLN B CG +2967 C CD . GLN B 81 ? 1.8535 1.9750 1.6276 0.4168 -0.0983 -0.0633 80 GLN B CD +2968 O OE1 . GLN B 81 ? 2.0736 2.1893 1.8505 0.4142 -0.0988 -0.0630 80 GLN B OE1 +2969 N NE2 . GLN B 81 ? 1.5742 1.6970 1.3470 0.4178 -0.0991 -0.0658 80 GLN B NE2 +2970 N N . HIS B 82 ? 1.3956 1.5105 1.1496 0.4213 -0.0886 -0.0542 81 HIS B N +2971 C CA . HIS B 82 ? 1.6460 1.7618 1.3923 0.4242 -0.0859 -0.0529 81 HIS B CA +2972 C C . HIS B 82 ? 1.6982 1.8071 1.4391 0.4238 -0.0829 -0.0501 81 HIS B C +2973 O O . HIS B 82 ? 1.4402 1.5474 1.1742 0.4257 -0.0805 -0.0489 81 HIS B O +2974 C CB . HIS B 82 ? 1.5533 1.6683 1.2966 0.4251 -0.0862 -0.0552 81 HIS B CB +2975 C CG . HIS B 82 ? 1.6405 1.7622 1.3887 0.4256 -0.0889 -0.0582 81 HIS B CG +2976 N ND1 . HIS B 82 ? 1.7512 1.8817 1.4996 0.4281 -0.0892 -0.0582 81 HIS B ND1 +2977 C CD2 . HIS B 82 ? 1.2063 1.3273 0.9594 0.4239 -0.0916 -0.0612 81 HIS B CD2 +2978 C CE1 . HIS B 82 ? 1.7516 1.8865 1.5048 0.4278 -0.0919 -0.0612 81 HIS B CE1 +2979 N NE2 . HIS B 82 ? 1.7030 1.8323 1.4591 0.4253 -0.0934 -0.0630 81 HIS B NE2 +2980 N N . ASP B 83 ? 1.4552 1.5601 1.1995 0.4214 -0.0833 -0.0490 82 ASP B N +2981 C CA . ASP B 83 ? 1.4060 1.5045 1.1462 0.4207 -0.0808 -0.0463 82 ASP B CA +2982 C C . ASP B 83 ? 1.3699 1.4731 1.1086 0.4224 -0.0792 -0.0437 82 ASP B C +2983 O O . ASP B 83 ? 1.6101 1.7156 1.3536 0.4214 -0.0802 -0.0428 82 ASP B O +2984 C CB . ASP B 83 ? 1.9015 1.9941 1.6466 0.4172 -0.0820 -0.0465 82 ASP B CB +2985 C CG . ASP B 83 ? 1.8021 1.8868 1.5429 0.4160 -0.0796 -0.0443 82 ASP B CG +2986 O OD1 . ASP B 83 ? 1.5004 1.5854 1.2358 0.4179 -0.0770 -0.0419 82 ASP B OD1 +2987 O OD2 . ASP B 83 ? 2.0113 2.0895 1.7543 0.4133 -0.0804 -0.0449 82 ASP B OD2 +2988 N N . PHE B 84 ? 1.3769 1.4814 1.1088 0.4251 -0.0767 -0.0423 83 PHE B N +2989 C CA . PHE B 84 ? 1.3197 1.4286 1.0493 0.4271 -0.0748 -0.0397 83 PHE B CA +2990 C C . PHE B 84 ? 1.2829 1.3862 1.0107 0.4259 -0.0729 -0.0371 83 PHE B C +2991 O O . PHE B 84 ? 1.6234 1.7295 1.3538 0.4257 -0.0729 -0.0354 83 PHE B O +2992 C CB . PHE B 84 ? 1.3528 1.4644 1.0754 0.4304 -0.0727 -0.0392 83 PHE B CB +2993 C CG . PHE B 84 ? 1.4517 1.5658 1.1705 0.4323 -0.0702 -0.0363 83 PHE B CG +2994 C CD1 . PHE B 84 ? 1.6945 1.8160 1.4170 0.4331 -0.0709 -0.0354 83 PHE B CD1 +2995 C CD2 . PHE B 84 ? 1.4427 1.5520 1.1543 0.4333 -0.0671 -0.0344 83 PHE B CD2 +2996 C CE1 . PHE B 84 ? 1.6634 1.7873 1.3825 0.4349 -0.0686 -0.0328 83 PHE B CE1 +2997 C CE2 . PHE B 84 ? 1.7241 1.8359 1.4323 0.4351 -0.0648 -0.0318 83 PHE B CE2 +2998 C CZ . PHE B 84 ? 1.7001 1.8192 1.4121 0.4359 -0.0655 -0.0310 83 PHE B CZ +2999 N N . PHE B 85 ? 1.3854 1.4809 1.1087 0.4250 -0.0714 -0.0367 84 PHE B N +3000 C CA . PHE B 85 ? 1.3293 1.4189 1.0498 0.4240 -0.0692 -0.0342 84 PHE B CA +3001 C C . PHE B 85 ? 1.4077 1.4962 1.1343 0.4215 -0.0705 -0.0335 84 PHE B C +3002 O O . PHE B 85 ? 1.7478 1.8376 1.4740 0.4218 -0.0693 -0.0312 84 PHE B O +3003 C CB . PHE B 85 ? 1.3567 1.4378 1.0726 0.4229 -0.0679 -0.0345 84 PHE B CB +3004 C CG . PHE B 85 ? 1.3465 1.4283 1.0565 0.4253 -0.0667 -0.0352 84 PHE B CG +3005 C CD1 . PHE B 85 ? 1.3763 1.4596 1.0798 0.4279 -0.0639 -0.0333 84 PHE B CD1 +3006 C CD2 . PHE B 85 ? 1.3088 1.3899 1.0198 0.4249 -0.0683 -0.0379 84 PHE B CD2 +3007 C CE1 . PHE B 85 ? 1.3399 1.4239 1.0380 0.4301 -0.0628 -0.0339 84 PHE B CE1 +3008 C CE2 . PHE B 85 ? 1.0854 1.1672 0.7910 0.4270 -0.0672 -0.0385 84 PHE B CE2 +3009 C CZ . PHE B 85 ? 1.2884 1.3716 0.9874 0.4296 -0.0644 -0.0365 84 PHE B CZ +3010 N N . LYS B 86 ? 1.4259 1.5122 1.1581 0.4189 -0.0731 -0.0355 85 LYS B N +3011 C CA . LYS B 86 ? 1.6731 1.7582 1.4112 0.4164 -0.0744 -0.0349 85 LYS B CA +3012 C C . LYS B 86 ? 1.6844 1.7778 1.4270 0.4174 -0.0755 -0.0342 85 LYS B C +3013 O O . LYS B 86 ? 1.5170 1.6104 1.2616 0.4166 -0.0752 -0.0323 85 LYS B O +3014 C CB . LYS B 86 ? 1.4442 1.5254 1.1876 0.4135 -0.0769 -0.0373 85 LYS B CB +3015 C CG . LYS B 86 ? 1.2486 1.3215 0.9883 0.4122 -0.0760 -0.0379 85 LYS B CG +3016 C CD . LYS B 86 ? 1.3402 1.4090 1.0856 0.4091 -0.0785 -0.0400 85 LYS B CD +3017 C CE . LYS B 86 ? 1.0390 1.0994 0.7809 0.4076 -0.0775 -0.0405 85 LYS B CE +3018 N NZ . LYS B 86 ? 1.5673 1.6281 1.3045 0.4094 -0.0769 -0.0419 85 LYS B NZ +3019 N N . SER B 87 ? 1.6269 1.7274 1.3707 0.4193 -0.0768 -0.0357 86 SER B N +3020 C CA . SER B 87 ? 1.5576 1.6664 1.3063 0.4201 -0.0783 -0.0355 86 SER B CA +3021 C C . SER B 87 ? 1.5787 1.6912 1.3243 0.4220 -0.0761 -0.0326 86 SER B C +3022 O O . SER B 87 ? 1.6002 1.7185 1.3499 0.4222 -0.0770 -0.0318 86 SER B O +3023 C CB . SER B 87 ? 1.7310 1.8464 1.4809 0.4217 -0.0799 -0.0379 86 SER B CB +3024 O OG . SER B 87 ? 1.5359 1.6540 1.2793 0.4248 -0.0777 -0.0372 86 SER B OG +3025 N N . ALA B 88 ? 1.5843 1.6932 1.3225 0.4235 -0.0731 -0.0310 87 ALA B N +3026 C CA . ALA B 88 ? 1.3476 1.4595 1.0821 0.4255 -0.0707 -0.0283 87 ALA B CA +3027 C C . ALA B 88 ? 1.2482 1.3554 0.9833 0.4237 -0.0696 -0.0260 87 ALA B C +3028 O O . ALA B 88 ? 1.4954 1.6048 1.2284 0.4250 -0.0679 -0.0237 87 ALA B O +3029 C CB . ALA B 88 ? 1.2540 1.3646 0.9803 0.4280 -0.0679 -0.0277 87 ALA B CB +3030 N N . MET B 89 ? 1.3651 1.4656 1.1029 0.4208 -0.0707 -0.0268 88 MET B N +3031 C CA . MET B 89 ? 1.5477 1.6429 1.2861 0.4188 -0.0698 -0.0249 88 MET B CA +3032 C C . MET B 89 ? 1.3575 1.4569 1.1031 0.4175 -0.0718 -0.0244 88 MET B C +3033 O O . MET B 89 ? 1.5358 1.6407 1.2864 0.4175 -0.0742 -0.0260 88 MET B O +3034 C CB . MET B 89 ? 1.3844 1.4708 1.1227 0.4162 -0.0701 -0.0260 88 MET B CB +3035 C CG . MET B 89 ? 1.5745 1.6563 1.3056 0.4172 -0.0681 -0.0264 88 MET B CG +3036 S SD . MET B 89 ? 1.4904 1.5696 1.2139 0.4188 -0.0642 -0.0232 88 MET B SD +3037 C CE . MET B 89 ? 1.6761 1.7518 1.3920 0.4205 -0.0625 -0.0241 88 MET B CE +3038 N N . PRO B 90 ? 1.2446 1.3414 0.9906 0.4164 -0.0707 -0.0221 89 PRO B N +3039 C CA . PRO B 90 ? 1.6272 1.7173 1.3677 0.4161 -0.0680 -0.0201 89 PRO B CA +3040 C C . PRO B 90 ? 1.4615 1.5548 1.1960 0.4191 -0.0652 -0.0180 89 PRO B C +3041 O O . PRO B 90 ? 1.5430 1.6314 1.2725 0.4192 -0.0627 -0.0163 89 PRO B O +3042 C CB . PRO B 90 ? 1.4875 1.5752 1.2327 0.4136 -0.0687 -0.0189 89 PRO B CB +3043 C CG . PRO B 90 ? 1.4084 1.5039 1.1601 0.4138 -0.0710 -0.0191 89 PRO B CG +3044 C CD . PRO B 90 ? 1.3630 1.4641 1.1155 0.4154 -0.0725 -0.0214 89 PRO B CD +3045 N N . GLU B 91 ? 1.2638 1.3653 0.9991 0.4214 -0.0656 -0.0181 90 GLU B N +3046 C CA . GLU B 91 ? 1.6503 1.7558 1.3806 0.4242 -0.0631 -0.0160 90 GLU B CA +3047 C C . GLU B 91 ? 1.5858 1.6878 1.3083 0.4259 -0.0607 -0.0161 90 GLU B C +3048 O O . GLU B 91 ? 1.5769 1.6770 1.2940 0.4271 -0.0580 -0.0141 90 GLU B O +3049 C CB . GLU B 91 ? 2.0423 2.1575 1.7756 0.4261 -0.0643 -0.0162 90 GLU B CB +3050 C CG . GLU B 91 ? 2.1762 2.2952 1.9174 0.4244 -0.0668 -0.0161 90 GLU B CG +3051 C CD . GLU B 91 ? 2.3753 2.5027 2.1177 0.4263 -0.0665 -0.0144 90 GLU B CD +3052 O OE1 . GLU B 91 ? 2.2720 2.3990 2.0112 0.4272 -0.0642 -0.0119 90 GLU B OE1 +3053 O OE2 . GLU B 91 ? 2.4348 2.5692 2.1814 0.4269 -0.0685 -0.0156 90 GLU B OE2 +3054 N N . GLY B 92 ? 1.3690 1.4702 1.0911 0.4260 -0.0618 -0.0185 91 GLY B N +3055 C CA . GLY B 92 ? 1.3051 1.4018 1.0202 0.4271 -0.0598 -0.0188 91 GLY B CA +3056 C C . GLY B 92 ? 1.3104 1.4124 1.0221 0.4301 -0.0593 -0.0197 91 GLY B C +3057 O O . GLY B 92 ? 1.5333 1.6428 1.2483 0.4312 -0.0608 -0.0205 91 GLY B O +3058 N N . TYR B 93 ? 1.2806 1.3785 0.9855 0.4312 -0.0572 -0.0196 92 TYR B N +3059 C CA . TYR B 93 ? 1.3613 1.4633 1.0620 0.4341 -0.0564 -0.0203 92 TYR B CA +3060 C C . TYR B 93 ? 1.5003 1.5985 1.1926 0.4358 -0.0530 -0.0187 92 TYR B C +3061 O O . TYR B 93 ? 1.5091 1.6005 1.1990 0.4344 -0.0515 -0.0175 92 TYR B O +3062 C CB . TYR B 93 ? 1.1676 1.2692 0.8701 0.4334 -0.0585 -0.0233 92 TYR B CB +3063 C CG . TYR B 93 ? 1.4387 1.5315 1.1394 0.4314 -0.0584 -0.0243 92 TYR B CG +3064 C CD1 . TYR B 93 ? 1.6388 1.7276 1.3324 0.4326 -0.0562 -0.0240 92 TYR B CD1 +3065 C CD2 . TYR B 93 ? 1.4099 1.4987 1.1161 0.4282 -0.0607 -0.0256 92 TYR B CD2 +3066 C CE1 . TYR B 93 ? 1.5643 1.6452 1.2562 0.4307 -0.0562 -0.0249 92 TYR B CE1 +3067 C CE2 . TYR B 93 ? 1.5473 1.6282 1.2519 0.4263 -0.0606 -0.0265 92 TYR B CE2 +3068 C CZ . TYR B 93 ? 1.4850 1.5621 1.1825 0.4275 -0.0584 -0.0262 92 TYR B CZ +3069 O OH . TYR B 93 ? 1.5952 1.6646 1.2911 0.4256 -0.0583 -0.0270 92 TYR B OH +3070 N N . VAL B 94 ? 1.6274 1.7302 1.3154 0.4388 -0.0518 -0.0188 93 VAL B N +3071 C CA . VAL B 94 ? 1.4842 1.5842 1.1642 0.4408 -0.0486 -0.0174 93 VAL B CA +3072 C C . VAL B 94 ? 1.4842 1.5824 1.1606 0.4416 -0.0486 -0.0192 93 VAL B C +3073 O O . VAL B 94 ? 1.5153 1.6187 1.1936 0.4427 -0.0502 -0.0210 93 VAL B O +3074 C CB . VAL B 94 ? 1.4585 1.5654 1.1356 0.4440 -0.0468 -0.0157 93 VAL B CB +3075 C CG1 . VAL B 94 ? 1.3181 1.4213 0.9872 0.4457 -0.0433 -0.0140 93 VAL B CG1 +3076 C CG2 . VAL B 94 ? 1.4972 1.6082 1.1792 0.4434 -0.0474 -0.0142 93 VAL B CG2 +3077 N N . GLN B 95 ? 1.1381 1.2290 0.8094 0.4411 -0.0468 -0.0188 94 GLN B N +3078 C CA . GLN B 95 ? 1.4034 1.4917 1.0712 0.4416 -0.0468 -0.0205 94 GLN B CA +3079 C C . GLN B 95 ? 1.5100 1.5970 1.1695 0.4442 -0.0436 -0.0191 94 GLN B C +3080 O O . GLN B 95 ? 1.2373 1.3183 0.8929 0.4435 -0.0416 -0.0176 94 GLN B O +3081 C CB . GLN B 95 ? 1.2747 1.3549 0.9441 0.4384 -0.0480 -0.0216 94 GLN B CB +3082 C CG . GLN B 95 ? 1.2277 1.3046 0.8936 0.4387 -0.0479 -0.0233 94 GLN B CG +3083 C CD . GLN B 95 ? 1.3266 1.3966 0.9954 0.4354 -0.0496 -0.0247 94 GLN B CD +3084 O OE1 . GLN B 95 ? 1.2655 1.3367 0.9409 0.4335 -0.0523 -0.0262 94 GLN B OE1 +3085 N NE2 . GLN B 95 ? 1.3999 1.4627 1.0639 0.4346 -0.0480 -0.0243 94 GLN B NE2 +3086 N N . GLU B 96 ? 1.2973 1.3901 0.9543 0.4470 -0.0432 -0.0197 95 GLU B N +3087 C CA . GLU B 96 ? 1.1088 1.2012 0.7581 0.4497 -0.0403 -0.0185 95 GLU B CA +3088 C C . GLU B 96 ? 1.2997 1.3896 0.9457 0.4502 -0.0405 -0.0202 95 GLU B C +3089 O O . GLU B 96 ? 1.3815 1.4749 1.0306 0.4503 -0.0426 -0.0223 95 GLU B O +3090 C CB . GLU B 96 ? 1.5390 1.6401 1.1874 0.4529 -0.0395 -0.0176 95 GLU B CB +3091 C CG . GLU B 96 ? 1.9425 2.0460 1.5927 0.4529 -0.0386 -0.0155 95 GLU B CG +3092 C CD . GLU B 96 ? 2.2782 2.3913 1.9298 0.4555 -0.0387 -0.0151 95 GLU B CD +3093 O OE1 . GLU B 96 ? 2.3549 2.4732 2.0126 0.4549 -0.0412 -0.0163 95 GLU B OE1 +3094 O OE2 . GLU B 96 ? 2.2567 2.3722 1.9035 0.4581 -0.0361 -0.0134 95 GLU B OE2 +3095 N N . ARG B 97 ? 1.0336 1.1174 0.6735 0.4504 -0.0383 -0.0193 96 ARG B N +3096 C CA . ARG B 97 ? 1.3382 1.4194 0.9744 0.4509 -0.0382 -0.0207 96 ARG B CA +3097 C C . ARG B 97 ? 1.5363 1.6172 1.1645 0.4537 -0.0351 -0.0193 96 ARG B C +3098 O O . ARG B 97 ? 1.4309 1.5116 1.0561 0.4547 -0.0328 -0.0172 96 ARG B O +3099 C CB . ARG B 97 ? 1.0770 1.1495 0.7138 0.4477 -0.0389 -0.0214 96 ARG B CB +3100 C CG . ARG B 97 ? 1.5897 1.6619 1.2338 0.4450 -0.0422 -0.0235 96 ARG B CG +3101 C CD . ARG B 97 ? 1.3106 1.3758 0.9540 0.4429 -0.0429 -0.0248 96 ARG B CD +3102 N NE . ARG B 97 ? 1.6296 1.6932 1.2801 0.4399 -0.0458 -0.0265 96 ARG B NE +3103 C CZ . ARG B 97 ? 1.4624 1.5197 1.1152 0.4369 -0.0461 -0.0261 96 ARG B CZ +3104 N NH1 . ARG B 97 ? 1.6060 1.6576 1.2543 0.4364 -0.0438 -0.0242 96 ARG B NH1 +3105 N NH2 . ARG B 97 ? 1.3841 1.4405 1.0434 0.4343 -0.0488 -0.0277 96 ARG B NH2 +3106 N N . THR B 98 ? 1.3252 1.4062 0.9502 0.4550 -0.0351 -0.0206 97 THR B N +3107 C CA . THR B 98 ? 1.5965 1.6753 1.2136 0.4571 -0.0323 -0.0194 97 THR B CA +3108 C C . THR B 98 ? 1.3963 1.4690 1.0118 0.4557 -0.0330 -0.0209 97 THR B C +3109 O O . THR B 98 ? 1.3713 1.4450 0.9910 0.4545 -0.0355 -0.0230 97 THR B O +3110 C CB . THR B 98 ? 1.6579 1.7444 1.2722 0.4609 -0.0313 -0.0194 97 THR B CB +3111 O OG1 . THR B 98 ? 1.3122 1.4053 0.9302 0.4617 -0.0317 -0.0187 97 THR B OG1 +3112 C CG2 . THR B 98 ? 1.0038 1.0882 0.6100 0.4632 -0.0280 -0.0178 97 THR B CG2 +3113 N N . ILE B 99 ? 1.2446 1.3112 0.8543 0.4557 -0.0307 -0.0197 98 ILE B N +3114 C CA . ILE B 99 ? 1.4784 1.5383 1.0869 0.4538 -0.0314 -0.0208 98 ILE B CA +3115 C C . ILE B 99 ? 1.5716 1.6290 1.1722 0.4558 -0.0290 -0.0201 98 ILE B C +3116 O O . ILE B 99 ? 1.3087 1.3613 0.9047 0.4558 -0.0266 -0.0183 98 ILE B O +3117 C CB . ILE B 99 ? 1.2667 1.3193 0.8780 0.4502 -0.0319 -0.0203 98 ILE B CB +3118 C CG1 . ILE B 99 ? 1.0735 1.1288 0.6929 0.4481 -0.0346 -0.0213 98 ILE B CG1 +3119 C CG2 . ILE B 99 ? 0.9948 1.0402 0.6045 0.4482 -0.0323 -0.0213 98 ILE B CG2 +3120 C CD1 . ILE B 99 ? 1.0378 1.0890 0.6596 0.4458 -0.0343 -0.0200 98 ILE B CD1 +3121 N N . PHE B 100 ? 1.2243 1.2850 0.8235 0.4576 -0.0296 -0.0214 99 PHE B N +3122 C CA . PHE B 100 ? 1.1235 1.1827 0.7154 0.4598 -0.0274 -0.0208 99 PHE B CA +3123 C C . PHE B 100 ? 1.1344 1.1860 0.7246 0.4577 -0.0278 -0.0215 99 PHE B C +3124 O O . PHE B 100 ? 1.3552 1.4069 0.9477 0.4569 -0.0298 -0.0234 99 PHE B O +3125 C CB . PHE B 100 ? 1.0942 1.1606 0.6850 0.4627 -0.0279 -0.0220 99 PHE B CB +3126 C CG . PHE B 100 ? 1.2619 1.3364 0.8552 0.4647 -0.0280 -0.0217 99 PHE B CG +3127 C CD1 . PHE B 100 ? 1.4388 1.5163 1.0274 0.4674 -0.0253 -0.0199 99 PHE B CD1 +3128 C CD2 . PHE B 100 ? 1.4293 1.5085 1.0297 0.4636 -0.0307 -0.0232 99 PHE B CD2 +3129 C CE1 . PHE B 100 ? 1.3943 1.4794 0.9854 0.4692 -0.0253 -0.0195 99 PHE B CE1 +3130 C CE2 . PHE B 100 ? 1.4712 1.5580 1.0741 0.4654 -0.0308 -0.0229 99 PHE B CE2 +3131 C CZ . PHE B 100 ? 1.2875 1.3772 0.8856 0.4681 -0.0281 -0.0210 99 PHE B CZ +3132 N N . PHE B 101 ? 1.1003 1.1453 0.6866 0.4567 -0.0258 -0.0199 100 PHE B N +3133 C CA . PHE B 101 ? 1.2866 1.3247 0.8702 0.4552 -0.0257 -0.0203 100 PHE B CA +3134 C C . PHE B 101 ? 1.3530 1.3933 0.9308 0.4582 -0.0245 -0.0204 100 PHE B C +3135 O O . PHE B 101 ? 1.3813 1.4239 0.9540 0.4609 -0.0220 -0.0189 100 PHE B O +3136 C CB . PHE B 101 ? 0.9208 0.9516 0.5016 0.4535 -0.0238 -0.0184 100 PHE B CB +3137 C CG . PHE B 101 ? 1.1805 1.2088 0.7669 0.4504 -0.0250 -0.0183 100 PHE B CG +3138 C CD1 . PHE B 101 ? 1.3831 1.4157 0.9721 0.4510 -0.0248 -0.0175 100 PHE B CD1 +3139 C CD2 . PHE B 101 ? 1.3408 1.3626 0.9299 0.4470 -0.0264 -0.0190 100 PHE B CD2 +3140 C CE1 . PHE B 101 ? 1.0302 1.0606 0.6244 0.4483 -0.0259 -0.0173 100 PHE B CE1 +3141 C CE2 . PHE B 101 ? 1.2907 1.3103 0.8851 0.4442 -0.0275 -0.0189 100 PHE B CE2 +3142 C CZ . PHE B 101 ? 1.4594 1.4832 1.0561 0.4449 -0.0273 -0.0180 100 PHE B CZ +3143 N N . LYS B 102 ? 1.2060 1.2460 0.7846 0.4578 -0.0261 -0.0222 101 LYS B N +3144 C CA . LYS B 102 ? 1.6372 1.6792 1.2104 0.4605 -0.0251 -0.0224 101 LYS B CA +3145 C C . LYS B 102 ? 1.8534 1.8902 1.4193 0.4613 -0.0222 -0.0204 101 LYS B C +3146 O O . LYS B 102 ? 1.1315 1.1611 0.6969 0.4588 -0.0218 -0.0198 101 LYS B O +3147 C CB . LYS B 102 ? 1.2159 1.2573 0.7913 0.4595 -0.0275 -0.0246 101 LYS B CB +3148 C CG . LYS B 102 ? 1.5588 1.6007 1.1281 0.4620 -0.0263 -0.0246 101 LYS B CG +3149 C CD . LYS B 102 ? 1.7785 1.8189 1.3499 0.4607 -0.0285 -0.0267 101 LYS B CD +3150 C CE . LYS B 102 ? 1.6021 1.6492 1.1722 0.4636 -0.0291 -0.0280 101 LYS B CE +3151 N NZ . LYS B 102 ? 1.8177 1.8620 1.3819 0.4648 -0.0280 -0.0278 101 LYS B NZ +3152 N N . ASP B 103 ? 1.5642 1.6047 1.1246 0.4648 -0.0201 -0.0195 102 ASP B N +3153 C CA . ASP B 103 ? 1.5830 1.6196 1.1360 0.4661 -0.0171 -0.0176 102 ASP B CA +3154 C C . ASP B 103 ? 1.4800 1.5135 1.0321 0.4653 -0.0152 -0.0157 102 ASP B C +3155 O O . ASP B 103 ? 1.5734 1.6011 1.1231 0.4640 -0.0135 -0.0140 102 ASP B O +3156 C CB . ASP B 103 ? 1.8248 1.8549 1.3758 0.4644 -0.0173 -0.0179 102 ASP B CB +3157 C CG . ASP B 103 ? 2.0038 2.0369 1.5550 0.4655 -0.0186 -0.0193 102 ASP B CG +3158 O OD1 . ASP B 103 ? 1.8032 1.8432 1.3552 0.4678 -0.0184 -0.0194 102 ASP B OD1 +3159 O OD2 . ASP B 103 ? 1.9605 1.9893 1.5114 0.4640 -0.0197 -0.0204 102 ASP B OD2 +3160 N N . ASP B 104 ? 1.3636 1.4010 0.9201 0.4650 -0.0159 -0.0156 103 ASP B N +3161 C CA . ASP B 104 ? 1.3465 1.3804 0.9034 0.4636 -0.0146 -0.0139 103 ASP B CA +3162 C C . ASP B 104 ? 1.4121 1.4517 0.9730 0.4642 -0.0149 -0.0136 103 ASP B C +3163 O O . ASP B 104 ? 1.1121 1.1589 0.6752 0.4661 -0.0159 -0.0145 103 ASP B O +3164 C CB . ASP B 104 ? 0.9040 0.9306 0.4641 0.4596 -0.0160 -0.0144 103 ASP B CB +3165 C CG . ASP B 104 ? 1.7195 1.7420 1.2796 0.4581 -0.0147 -0.0127 103 ASP B CG +3166 O OD1 . ASP B 104 ? 1.2366 1.2619 0.7941 0.4601 -0.0126 -0.0112 103 ASP B OD1 +3167 O OD2 . ASP B 104 ? 2.8386 2.8552 2.4012 0.4549 -0.0156 -0.0129 103 ASP B OD2 +3168 N N . GLY B 105 ? 1.3959 1.4324 0.9579 0.4626 -0.0141 -0.0123 104 GLY B N +3169 C CA . GLY B 105 ? 1.2195 1.2605 0.7843 0.4633 -0.0138 -0.0114 104 GLY B CA +3170 C C . GLY B 105 ? 1.3594 1.4047 0.9318 0.4620 -0.0168 -0.0129 104 GLY B C +3171 O O . GLY B 105 ? 1.3714 1.4175 0.9468 0.4611 -0.0191 -0.0148 104 GLY B O +3172 N N . ASN B 106 ? 1.1670 1.2151 0.7427 0.4618 -0.0168 -0.0121 105 ASN B N +3173 C CA . ASN B 106 ? 1.1722 1.2245 0.7554 0.4604 -0.0196 -0.0134 105 ASN B CA +3174 C C . ASN B 106 ? 1.4632 1.5146 1.0504 0.4586 -0.0198 -0.0123 105 ASN B C +3175 O O . ASN B 106 ? 1.5885 1.6390 1.1726 0.4595 -0.0175 -0.0104 105 ASN B O +3176 C CB . ASN B 106 ? 1.4240 1.4853 1.0081 0.4634 -0.0201 -0.0141 105 ASN B CB +3177 C CG . ASN B 106 ? 1.3384 1.4041 0.9189 0.4663 -0.0176 -0.0123 105 ASN B CG +3178 O OD1 . ASN B 106 ? 1.4255 1.4923 1.0081 0.4659 -0.0171 -0.0111 105 ASN B OD1 +3179 N ND2 . ASN B 106 ? 1.1313 1.1998 0.7065 0.4694 -0.0159 -0.0121 105 ASN B ND2 +3180 N N . TYR B 107 ? 1.2056 1.2571 0.7996 0.4561 -0.0225 -0.0136 106 TYR B N +3181 C CA . TYR B 107 ? 1.3008 1.3526 0.8995 0.4544 -0.0231 -0.0128 106 TYR B CA +3182 C C . TYR B 107 ? 1.3695 1.4300 0.9728 0.4558 -0.0245 -0.0132 106 TYR B C +3183 O O . TYR B 107 ? 1.1710 1.2356 0.7773 0.4562 -0.0265 -0.0150 106 TYR B O +3184 C CB . TYR B 107 ? 1.1776 1.2239 0.7813 0.4505 -0.0253 -0.0138 106 TYR B CB +3185 C CG . TYR B 107 ? 1.2404 1.2778 0.8408 0.4485 -0.0243 -0.0133 106 TYR B CG +3186 C CD1 . TYR B 107 ? 1.4458 1.4799 1.0395 0.4497 -0.0213 -0.0116 106 TYR B CD1 +3187 C CD2 . TYR B 107 ? 1.4768 1.5092 1.0811 0.4452 -0.0263 -0.0147 106 TYR B CD2 +3188 C CE1 . TYR B 107 ? 1.1636 1.1897 0.7545 0.4478 -0.0205 -0.0112 106 TYR B CE1 +3189 C CE2 . TYR B 107 ? 1.1769 1.2013 0.7784 0.4433 -0.0255 -0.0143 106 TYR B CE2 +3190 C CZ . TYR B 107 ? 1.3226 1.3439 0.9175 0.4445 -0.0226 -0.0125 106 TYR B CZ +3191 O OH . TYR B 107 ? 1.1695 1.1831 0.7619 0.4425 -0.0218 -0.0121 106 TYR B OH +3192 N N . LYS B 108 ? 1.1669 1.2301 0.7709 0.4565 -0.0234 -0.0116 107 LYS B N +3193 C CA . LYS B 108 ? 1.2423 1.3132 0.8515 0.4572 -0.0249 -0.0119 107 LYS B CA +3194 C C . LYS B 108 ? 1.3224 1.3917 0.9367 0.4547 -0.0258 -0.0112 107 LYS B C +3195 O O . LYS B 108 ? 1.5575 1.6250 1.1697 0.4548 -0.0238 -0.0092 107 LYS B O +3196 C CB . LYS B 108 ? 1.3134 1.3910 0.9191 0.4609 -0.0229 -0.0108 107 LYS B CB +3197 C CG . LYS B 108 ? 1.2933 1.3748 0.8958 0.4635 -0.0228 -0.0119 107 LYS B CG +3198 C CD . LYS B 108 ? 1.3613 1.4495 0.9603 0.4672 -0.0207 -0.0107 107 LYS B CD +3199 C CE . LYS B 108 ? 1.5143 1.6072 1.1111 0.4697 -0.0210 -0.0121 107 LYS B CE +3200 N NZ . LYS B 108 ? 1.4454 1.5438 1.0486 0.4691 -0.0241 -0.0141 107 LYS B NZ +3201 N N . THR B 109 ? 1.3016 1.3715 0.9225 0.4525 -0.0287 -0.0127 108 THR B N +3202 C CA . THR B 109 ? 1.4027 1.4705 1.0289 0.4497 -0.0299 -0.0123 108 THR B CA +3203 C C . THR B 109 ? 1.3543 1.4294 0.9865 0.4500 -0.0316 -0.0124 108 THR B C +3204 O O . THR B 109 ? 1.1605 1.2421 0.7945 0.4516 -0.0329 -0.0136 108 THR B O +3205 C CB . THR B 109 ? 1.3165 1.3781 0.9464 0.4462 -0.0321 -0.0138 108 THR B CB +3206 O OG1 . THR B 109 ? 1.1925 1.2582 0.8274 0.4459 -0.0349 -0.0160 108 THR B OG1 +3207 C CG2 . THR B 109 ? 1.4449 1.4994 1.0694 0.4457 -0.0307 -0.0139 108 THR B CG2 +3208 N N . ARG B 110 ? 1.0699 1.1441 0.7052 0.4485 -0.0317 -0.0112 109 ARG B N +3209 C CA . ARG B 110 ? 1.2468 1.3265 0.8891 0.4478 -0.0338 -0.0115 109 ARG B CA +3210 C C . ARG B 110 ? 1.3230 1.3975 0.9694 0.4445 -0.0348 -0.0110 109 ARG B C +3211 O O . ARG B 110 ? 1.2901 1.3602 0.9337 0.4439 -0.0329 -0.0093 109 ARG B O +3212 C CB . ARG B 110 ? 1.3945 1.4811 1.0359 0.4504 -0.0325 -0.0098 109 ARG B CB +3213 C CG . ARG B 110 ? 1.5798 1.6720 1.2285 0.4496 -0.0347 -0.0099 109 ARG B CG +3214 C CD . ARG B 110 ? 1.1789 1.2777 0.8268 0.4520 -0.0333 -0.0081 109 ARG B CD +3215 N NE . ARG B 110 ? 1.5407 1.6458 1.1957 0.4514 -0.0356 -0.0084 109 ARG B NE +3216 C CZ . ARG B 110 ? 1.6108 1.7149 1.2702 0.4493 -0.0364 -0.0075 109 ARG B CZ +3217 N NH1 . ARG B 110 ? 1.6600 1.7573 1.3178 0.4477 -0.0351 -0.0063 109 ARG B NH1 +3218 N NH2 . ARG B 110 ? 1.4428 1.5530 1.1086 0.4489 -0.0386 -0.0078 109 ARG B NH2 +3219 N N . ALA B 111 ? 1.4946 1.5697 1.1474 0.4423 -0.0378 -0.0127 110 ALA B N +3220 C CA . ALA B 111 ? 1.2810 1.3516 0.9387 0.4390 -0.0391 -0.0126 110 ALA B CA +3221 C C . ALA B 111 ? 1.2980 1.3743 0.9632 0.4382 -0.0416 -0.0131 110 ALA B C +3222 O O . ALA B 111 ? 1.1918 1.2739 0.8598 0.4392 -0.0433 -0.0145 110 ALA B O +3223 C CB . ALA B 111 ? 1.4298 1.4939 1.0882 0.4366 -0.0404 -0.0144 110 ALA B CB +3224 N N . GLU B 112 ? 1.0537 1.1283 0.7219 0.4365 -0.0417 -0.0118 111 GLU B N +3225 C CA . GLU B 112 ? 1.4587 1.5373 1.1344 0.4351 -0.0442 -0.0122 111 GLU B CA +3226 C C . GLU B 112 ? 1.5898 1.6622 1.2700 0.4314 -0.0461 -0.0133 111 GLU B C +3227 O O . GLU B 112 ? 1.4565 1.5226 1.1355 0.4297 -0.0450 -0.0121 111 GLU B O +3228 C CB . GLU B 112 ? 1.6912 1.7730 1.3677 0.4357 -0.0430 -0.0098 111 GLU B CB +3229 C CG . GLU B 112 ? 2.1086 2.1981 1.7824 0.4392 -0.0416 -0.0088 111 GLU B CG +3230 C CD . GLU B 112 ? 2.1073 2.1991 1.7812 0.4398 -0.0402 -0.0063 111 GLU B CD +3231 O OE1 . GLU B 112 ? 1.7676 1.8564 1.4449 0.4375 -0.0408 -0.0055 111 GLU B OE1 +3232 O OE2 . GLU B 112 ? 1.9797 2.0766 1.6503 0.4427 -0.0385 -0.0052 111 GLU B OE2 +3233 N N . VAL B 113 ? 1.3251 1.3993 1.0104 0.4303 -0.0489 -0.0155 112 VAL B N +3234 C CA . VAL B 113 ? 1.1473 1.2166 0.8376 0.4269 -0.0510 -0.0167 112 VAL B CA +3235 C C . VAL B 113 ? 1.4416 1.5154 1.1394 0.4258 -0.0533 -0.0168 112 VAL B C +3236 O O . VAL B 113 ? 1.3787 1.4595 1.0796 0.4270 -0.0548 -0.0178 112 VAL B O +3237 C CB . VAL B 113 ? 0.9547 1.0218 0.6458 0.4261 -0.0526 -0.0193 112 VAL B CB +3238 C CG1 . VAL B 113 ? 1.2203 1.2806 0.9152 0.4225 -0.0541 -0.0202 112 VAL B CG1 +3239 C CG2 . VAL B 113 ? 1.4359 1.5006 1.1198 0.4279 -0.0506 -0.0194 112 VAL B CG2 +3240 N N . LYS B 114 ? 1.2226 1.2926 0.9234 0.4234 -0.0535 -0.0158 113 LYS B N +3241 C CA . LYS B 114 ? 1.3139 1.3874 1.0218 0.4220 -0.0556 -0.0157 113 LYS B CA +3242 C C . LYS B 114 ? 1.4806 1.5475 1.1913 0.4188 -0.0560 -0.0151 113 LYS B C +3243 O O . LYS B 114 ? 1.2383 1.2982 0.9451 0.4178 -0.0545 -0.0146 113 LYS B O +3244 C CB . LYS B 114 ? 1.7045 1.7849 1.4122 0.4242 -0.0547 -0.0138 113 LYS B CB +3245 C CG . LYS B 114 ? 1.6329 1.7108 1.3351 0.4252 -0.0515 -0.0111 113 LYS B CG +3246 C CD . LYS B 114 ? 1.3756 1.4606 1.0778 0.4274 -0.0506 -0.0092 113 LYS B CD +3247 C CE . LYS B 114 ? 1.6810 1.7628 1.3783 0.4280 -0.0476 -0.0067 113 LYS B CE +3248 N NZ . LYS B 114 ? 1.5442 1.6222 1.2337 0.4296 -0.0449 -0.0064 113 LYS B NZ +3249 N N . PHE B 115 ? 1.3950 1.4643 1.1125 0.4172 -0.0581 -0.0152 114 PHE B N +3250 C CA . PHE B 115 ? 1.4138 1.4777 1.1347 0.4142 -0.0587 -0.0147 114 PHE B CA +3251 C C . PHE B 115 ? 1.4230 1.4874 1.1427 0.4146 -0.0569 -0.0119 114 PHE B C +3252 O O . PHE B 115 ? 1.4863 1.5573 1.2066 0.4165 -0.0567 -0.0108 114 PHE B O +3253 C CB . PHE B 115 ? 1.5751 1.6412 1.3042 0.4122 -0.0620 -0.0162 114 PHE B CB +3254 C CG . PHE B 115 ? 1.7218 1.7835 1.4532 0.4101 -0.0638 -0.0187 114 PHE B CG +3255 C CD1 . PHE B 115 ? 1.5486 1.6026 1.2810 0.4071 -0.0640 -0.0188 114 PHE B CD1 +3256 C CD2 . PHE B 115 ? 1.4589 1.5241 1.1914 0.4110 -0.0654 -0.0210 114 PHE B CD2 +3257 C CE1 . PHE B 115 ? 1.2917 1.3416 1.0262 0.4052 -0.0656 -0.0211 114 PHE B CE1 +3258 C CE2 . PHE B 115 ? 1.2950 1.3562 1.0296 0.4091 -0.0671 -0.0233 114 PHE B CE2 +3259 C CZ . PHE B 115 ? 1.4042 1.4576 1.1398 0.4062 -0.0672 -0.0233 114 PHE B CZ +3260 N N . GLU B 116 ? 1.3174 1.3747 1.0355 0.4127 -0.0557 -0.0109 115 GLU B N +3261 C CA . GLU B 116 ? 1.3203 1.3773 1.0380 0.4125 -0.0543 -0.0084 115 GLU B CA +3262 C C . GLU B 116 ? 1.3740 1.4262 1.0967 0.4092 -0.0557 -0.0084 115 GLU B C +3263 O O . GLU B 116 ? 1.3677 1.4128 1.0882 0.4075 -0.0546 -0.0080 115 GLU B O +3264 C CB . GLU B 116 ? 1.2775 1.3308 0.9875 0.4139 -0.0510 -0.0068 115 GLU B CB +3265 C CG . GLU B 116 ? 1.5463 1.6033 1.2508 0.4171 -0.0496 -0.0069 115 GLU B CG +3266 C CD . GLU B 116 ? 2.0702 2.1248 1.7676 0.4187 -0.0463 -0.0050 115 GLU B CD +3267 O OE1 . GLU B 116 ? 2.1045 2.1527 1.8002 0.4170 -0.0451 -0.0041 115 GLU B OE1 +3268 O OE2 . GLU B 116 ? 1.7787 1.8381 1.4722 0.4217 -0.0448 -0.0044 115 GLU B OE2 +3269 N N . GLY B 117 ? 1.3368 1.3930 1.0665 0.4081 -0.0582 -0.0090 116 GLY B N +3270 C CA . GLY B 117 ? 1.1152 1.1672 0.8503 0.4049 -0.0600 -0.0095 116 GLY B CA +3271 C C . GLY B 117 ? 1.5247 1.5732 1.2615 0.4033 -0.0617 -0.0121 116 GLY B C +3272 O O . GLY B 117 ? 1.4090 1.4617 1.1476 0.4042 -0.0633 -0.0139 116 GLY B O +3273 N N . ASP B 118 ? 1.8239 1.8645 1.5600 0.4009 -0.0614 -0.0123 117 ASP B N +3274 C CA . ASP B 118 ? 1.6773 1.7139 1.4155 0.3989 -0.0631 -0.0148 117 ASP B CA +3275 C C . ASP B 118 ? 1.5708 1.6045 1.3027 0.4001 -0.0617 -0.0157 117 ASP B C +3276 O O . ASP B 118 ? 1.5515 1.5832 1.2845 0.3992 -0.0630 -0.0178 117 ASP B O +3277 C CB . ASP B 118 ? 1.6645 1.6941 1.4056 0.3955 -0.0637 -0.0147 117 ASP B CB +3278 C CG . ASP B 118 ? 2.0899 2.1130 1.8254 0.3950 -0.0610 -0.0131 117 ASP B CG +3279 O OD1 . ASP B 118 ? 1.9549 1.9798 1.6859 0.3970 -0.0588 -0.0111 117 ASP B OD1 +3280 O OD2 . ASP B 118 ? 1.9202 1.9364 1.6558 0.3925 -0.0612 -0.0138 117 ASP B OD2 +3281 N N . THR B 119 ? 1.5311 1.5648 1.2565 0.4022 -0.0589 -0.0140 118 THR B N +3282 C CA . THR B 119 ? 1.3755 1.4059 1.0945 0.4033 -0.0573 -0.0146 118 THR B CA +3283 C C . THR B 119 ? 1.1933 1.2302 0.9099 0.4065 -0.0571 -0.0152 118 THR B C +3284 O O . THR B 119 ? 1.2960 1.3396 1.0137 0.4084 -0.0572 -0.0144 118 THR B O +3285 C CB . THR B 119 ? 1.1236 1.1487 0.8367 0.4033 -0.0544 -0.0125 118 THR B CB +3286 O OG1 . THR B 119 ? 1.3667 1.3855 1.0824 0.4001 -0.0548 -0.0123 118 THR B OG1 +3287 C CG2 . THR B 119 ? 1.3678 1.3897 1.0742 0.4045 -0.0526 -0.0130 118 THR B CG2 +3288 N N . LEU B 120 ? 1.1864 1.2213 0.8998 0.4070 -0.0570 -0.0168 119 LEU B N +3289 C CA . LEU B 120 ? 0.9931 1.0336 0.7037 0.4100 -0.0567 -0.0175 119 LEU B CA +3290 C C . LEU B 120 ? 1.3750 1.4132 1.0774 0.4120 -0.0537 -0.0162 119 LEU B C +3291 O O . LEU B 120 ? 1.2161 1.2481 0.9151 0.4110 -0.0528 -0.0167 119 LEU B O +3292 C CB . LEU B 120 ? 1.0658 1.1061 0.7787 0.4093 -0.0588 -0.0203 119 LEU B CB +3293 C CG . LEU B 120 ? 0.8599 0.9063 0.5713 0.4120 -0.0593 -0.0217 119 LEU B CG +3294 C CD1 . LEU B 120 ? 2.0144 2.0627 1.7318 0.4108 -0.0624 -0.0243 119 LEU B CD1 +3295 C CD2 . LEU B 120 ? 1.0069 1.0503 0.7111 0.4135 -0.0572 -0.0217 119 LEU B CD2 +3296 N N . VAL B 121 ? 1.1516 1.1947 0.8509 0.4147 -0.0520 -0.0146 120 VAL B N +3297 C CA . VAL B 121 ? 1.1503 1.1913 0.8419 0.4165 -0.0489 -0.0132 120 VAL B CA +3298 C C . VAL B 121 ? 1.3922 1.4377 1.0794 0.4197 -0.0481 -0.0137 120 VAL B C +3299 O O . VAL B 121 ? 1.1042 1.1570 0.7937 0.4215 -0.0491 -0.0142 120 VAL B O +3300 C CB . VAL B 121 ? 1.2449 1.2863 0.9347 0.4172 -0.0469 -0.0105 120 VAL B CB +3301 C CG1 . VAL B 121 ? 1.0932 1.1306 0.7875 0.4141 -0.0478 -0.0099 120 VAL B CG1 +3302 C CG2 . VAL B 121 ? 1.6168 1.6667 1.3077 0.4197 -0.0469 -0.0097 120 VAL B CG2 +3303 N N . ASN B 122 ? 1.2046 1.2457 0.8857 0.4203 -0.0463 -0.0137 121 ASN B N +3304 C CA . ASN B 122 ? 1.2751 1.3194 0.9510 0.4234 -0.0450 -0.0139 121 ASN B CA +3305 C C . ASN B 122 ? 1.4727 1.5155 1.1419 0.4251 -0.0417 -0.0117 121 ASN B C +3306 O O . ASN B 122 ? 1.2117 1.2477 0.8772 0.4239 -0.0402 -0.0110 121 ASN B O +3307 C CB . ASN B 122 ? 1.0267 1.0670 0.7008 0.4227 -0.0456 -0.0159 121 ASN B CB +3308 C CG . ASN B 122 ? 1.1517 1.1964 0.8217 0.4257 -0.0449 -0.0166 121 ASN B CG +3309 O OD1 . ASN B 122 ? 1.6971 1.7488 1.3672 0.4281 -0.0448 -0.0162 121 ASN B OD1 +3310 N ND2 . ASN B 122 ? 1.1858 1.2263 0.8521 0.4256 -0.0445 -0.0176 121 ASN B ND2 +3311 N N . ARG B 123 ? 1.3606 1.4098 1.0284 0.4278 -0.0406 -0.0105 122 ARG B N +3312 C CA . ARG B 123 ? 1.2218 1.2707 0.8834 0.4298 -0.0375 -0.0083 122 ARG B CA +3313 C C . ARG B 123 ? 1.4481 1.5003 1.1040 0.4331 -0.0360 -0.0085 122 ARG B C +3314 O O . ARG B 123 ? 1.0914 1.1505 0.7488 0.4350 -0.0368 -0.0091 122 ARG B O +3315 C CB . ARG B 123 ? 1.2464 1.3001 0.9104 0.4306 -0.0371 -0.0065 122 ARG B CB +3316 C CG . ARG B 123 ? 1.3233 1.3728 0.9909 0.4277 -0.0376 -0.0056 122 ARG B CG +3317 C CD . ARG B 123 ? 1.3501 1.4041 1.0188 0.4288 -0.0367 -0.0036 122 ARG B CD +3318 N NE . ARG B 123 ? 1.4038 1.4556 1.0781 0.4260 -0.0381 -0.0032 122 ARG B NE +3319 C CZ . ARG B 123 ? 1.6275 1.6726 1.3007 0.4239 -0.0372 -0.0023 122 ARG B CZ +3320 N NH1 . ARG B 123 ? 1.5027 1.5426 1.1697 0.4243 -0.0349 -0.0017 122 ARG B NH1 +3321 N NH2 . ARG B 123 ? 1.4769 1.5205 1.1554 0.4214 -0.0386 -0.0020 122 ARG B NH2 +3322 N N . ILE B 124 ? 1.4477 1.4949 1.0972 0.4336 -0.0337 -0.0079 123 ILE B N +3323 C CA . ILE B 124 ? 1.2681 1.3169 0.9122 0.4362 -0.0325 -0.0084 123 ILE B CA +3324 C C . ILE B 124 ? 1.4236 1.4720 1.0605 0.4387 -0.0291 -0.0065 123 ILE B C +3325 O O . ILE B 124 ? 1.1346 1.1776 0.7689 0.4376 -0.0275 -0.0051 123 ILE B O +3326 C CB . ILE B 124 ? 1.5931 1.6360 1.2361 0.4346 -0.0333 -0.0102 123 ILE B CB +3327 C CG1 . ILE B 124 ? 1.3025 1.3438 0.9525 0.4315 -0.0364 -0.0119 123 ILE B CG1 +3328 C CG2 . ILE B 124 ? 1.2344 1.2804 0.8737 0.4371 -0.0330 -0.0112 123 ILE B CG2 +3329 C CD1 . ILE B 124 ? 1.4518 1.4865 1.1011 0.4294 -0.0371 -0.0133 123 ILE B CD1 +3330 N N . GLU B 125 ? 1.2685 1.3228 0.9024 0.4419 -0.0282 -0.0063 124 GLU B N +3331 C CA . GLU B 125 ? 1.2171 1.2711 0.8436 0.4445 -0.0250 -0.0049 124 GLU B CA +3332 C C . GLU B 125 ? 1.1443 1.1984 0.7668 0.4461 -0.0248 -0.0062 124 GLU B C +3333 O O . GLU B 125 ? 1.4727 1.5322 1.0977 0.4471 -0.0264 -0.0076 124 GLU B O +3334 C CB . GLU B 125 ? 1.3344 1.3958 0.9604 0.4473 -0.0238 -0.0035 124 GLU B CB +3335 C CG . GLU B 125 ? 1.8582 1.9208 1.4884 0.4461 -0.0242 -0.0021 124 GLU B CG +3336 C CD . GLU B 125 ? 2.1573 2.2285 1.7888 0.4486 -0.0238 -0.0012 124 GLU B CD +3337 O OE1 . GLU B 125 ? 2.3310 2.4082 1.9632 0.4505 -0.0246 -0.0022 124 GLU B OE1 +3338 O OE2 . GLU B 125 ? 2.0078 2.0797 1.6397 0.4487 -0.0227 0.0006 124 GLU B OE2 +3339 N N . LEU B 126 ? 1.0862 1.1347 0.7028 0.4463 -0.0229 -0.0058 125 LEU B N +3340 C CA . LEU B 126 ? 1.3293 1.3772 0.9417 0.4477 -0.0225 -0.0070 125 LEU B CA +3341 C C . LEU B 126 ? 1.3196 1.3671 0.9242 0.4505 -0.0193 -0.0055 125 LEU B C +3342 O O . LEU B 126 ? 1.5035 1.5467 1.1048 0.4501 -0.0172 -0.0040 125 LEU B O +3343 C CB . LEU B 126 ? 1.2749 1.3156 0.8880 0.4448 -0.0238 -0.0083 125 LEU B CB +3344 C CG . LEU B 126 ? 1.0675 1.1049 0.6754 0.4456 -0.0230 -0.0091 125 LEU B CG +3345 C CD1 . LEU B 126 ? 1.2076 1.2421 0.8194 0.4431 -0.0256 -0.0112 125 LEU B CD1 +3346 C CD2 . LEU B 126 ? 1.3867 1.4174 0.9887 0.4453 -0.0204 -0.0076 125 LEU B CD2 +3347 N N . LYS B 127 ? 1.3833 1.4352 0.9849 0.4532 -0.0188 -0.0062 126 LYS B N +3348 C CA . LYS B 127 ? 1.1624 1.2147 0.7567 0.4562 -0.0158 -0.0049 126 LYS B CA +3349 C C . LYS B 127 ? 1.2918 1.3433 0.8814 0.4577 -0.0153 -0.0059 126 LYS B C +3350 O O . LYS B 127 ? 1.5206 1.5779 1.1105 0.4597 -0.0160 -0.0069 126 LYS B O +3351 C CB . LYS B 127 ? 1.4401 1.5003 1.0344 0.4590 -0.0148 -0.0038 126 LYS B CB +3352 C CG . LYS B 127 ? 1.7186 1.7792 1.3058 0.4620 -0.0114 -0.0022 126 LYS B CG +3353 C CD . LYS B 127 ? 1.8529 1.9212 1.4403 0.4647 -0.0104 -0.0011 126 LYS B CD +3354 C CE . LYS B 127 ? 1.7525 1.8218 1.3326 0.4679 -0.0072 0.0001 126 LYS B CE +3355 N NZ . LYS B 127 ? 1.8140 1.8751 1.3889 0.4670 -0.0055 0.0006 126 LYS B NZ +3356 N N . GLY B 128 ? 1.3727 1.4171 0.9580 0.4567 -0.0140 -0.0055 127 GLY B N +3357 C CA . GLY B 128 ? 1.2590 1.3018 0.8397 0.4579 -0.0135 -0.0064 127 GLY B CA +3358 C C . GLY B 128 ? 1.7138 1.7569 1.2869 0.4609 -0.0104 -0.0050 127 GLY B C +3359 O O . GLY B 128 ? 1.8856 1.9250 1.4552 0.4609 -0.0081 -0.0034 127 GLY B O +3360 N N . ILE B 129 ? 1.7278 1.7753 1.2984 0.4635 -0.0102 -0.0058 128 ILE B N +3361 C CA . ILE B 129 ? 1.4727 1.5212 1.0361 0.4667 -0.0073 -0.0047 128 ILE B CA +3362 C C . ILE B 129 ? 1.2665 1.3137 0.8265 0.4675 -0.0075 -0.0059 128 ILE B C +3363 O O . ILE B 129 ? 1.5208 1.5690 1.0845 0.4664 -0.0099 -0.0076 128 ILE B O +3364 C CB . ILE B 129 ? 1.3316 1.3887 0.8948 0.4700 -0.0064 -0.0041 128 ILE B CB +3365 C CG1 . ILE B 129 ? 1.9070 1.9656 1.4727 0.4697 -0.0057 -0.0027 128 ILE B CG1 +3366 C CG2 . ILE B 129 ? 2.1957 2.2543 1.7516 0.4735 -0.0036 -0.0034 128 ILE B CG2 +3367 C CD1 . ILE B 129 ? 1.7946 1.8583 1.3680 0.4685 -0.0084 -0.0035 128 ILE B CD1 +3368 N N . ASP B 130 ? 1.6639 1.7087 1.2169 0.4694 -0.0049 -0.0049 129 ASP B N +3369 C CA . ASP B 130 ? 1.6860 1.7304 1.2374 0.4698 -0.0049 -0.0053 129 ASP B CA +3370 C C . ASP B 130 ? 1.2221 1.2592 0.7726 0.4674 -0.0059 -0.0063 129 ASP B C +3371 O O . ASP B 130 ? 1.1898 1.2270 0.7401 0.4675 -0.0068 -0.0073 129 ASP B O +3372 C CB . ASP B 130 ? 1.6605 1.7126 1.2135 0.4721 -0.0064 -0.0069 129 ASP B CB +3373 C CG . ASP B 130 ? 1.7798 1.8392 1.3334 0.4747 -0.0051 -0.0057 129 ASP B CG +3374 O OD1 . ASP B 130 ? 1.6919 1.7506 1.2440 0.4751 -0.0028 -0.0036 129 ASP B OD1 +3375 O OD2 . ASP B 130 ? 1.7567 1.8227 1.3123 0.4763 -0.0063 -0.0069 129 ASP B OD2 +3376 N N . PHE B 131 ? 1.1357 1.1665 0.6857 0.4652 -0.0058 -0.0060 130 PHE B N +3377 C CA . PHE B 131 ? 1.5807 1.6047 1.1305 0.4627 -0.0068 -0.0068 130 PHE B CA +3378 C C . PHE B 131 ? 1.1024 1.1219 0.6493 0.4621 -0.0047 -0.0051 130 PHE B C +3379 O O . PHE B 131 ? 1.5204 1.5415 1.0664 0.4632 -0.0026 -0.0032 130 PHE B O +3380 C CB . PHE B 131 ? 1.5381 1.5572 1.0928 0.4588 -0.0082 -0.0069 130 PHE B CB +3381 C CG . PHE B 131 ? 1.2944 1.3171 0.8567 0.4573 -0.0113 -0.0084 130 PHE B CG +3382 C CD1 . PHE B 131 ? 1.3810 1.4095 0.9467 0.4582 -0.0116 -0.0080 130 PHE B CD1 +3383 C CD2 . PHE B 131 ? 1.2810 1.3017 0.8470 0.4551 -0.0138 -0.0102 130 PHE B CD2 +3384 C CE1 . PHE B 131 ? 0.9604 0.9925 0.5332 0.4569 -0.0144 -0.0094 130 PHE B CE1 +3385 C CE2 . PHE B 131 ? 1.1923 1.2164 0.7652 0.4538 -0.0166 -0.0117 130 PHE B CE2 +3386 C CZ . PHE B 131 ? 1.6130 1.6429 1.1893 0.4547 -0.0169 -0.0113 130 PHE B CZ +3387 N N . LYS B 132 ? 1.3113 1.3253 0.8572 0.4603 -0.0053 -0.0057 131 LYS B N +3388 C CA . LYS B 132 ? 1.3493 1.3587 0.8930 0.4595 -0.0035 -0.0041 131 LYS B CA +3389 C C . LYS B 132 ? 1.3354 1.3369 0.8779 0.4568 -0.0028 -0.0034 131 LYS B C +3390 O O . LYS B 132 ? 2.1778 2.1752 1.7207 0.4550 -0.0044 -0.0047 131 LYS B O +3391 C CB . LYS B 132 ? 1.0748 1.0835 0.6181 0.4594 -0.0046 -0.0053 131 LYS B CB +3392 C CG . LYS B 132 ? 1.2675 1.2837 0.8121 0.4618 -0.0058 -0.0065 131 LYS B CG +3393 C CD . LYS B 132 ? 1.4804 1.4952 1.0245 0.4614 -0.0068 -0.0076 131 LYS B CD +3394 C CE . LYS B 132 ? 1.6754 1.6976 1.2205 0.4639 -0.0076 -0.0085 131 LYS B CE +3395 N NZ . LYS B 132 ? 1.7552 1.7761 1.3001 0.4635 -0.0090 -0.0099 131 LYS B NZ +3396 N N . GLU B 133 ? 1.6019 1.6011 1.1430 0.4566 -0.0005 -0.0012 132 GLU B N +3397 C CA . GLU B 133 ? 1.9196 1.9114 1.4596 0.4541 0.0003 -0.0004 132 GLU B CA +3398 C C . GLU B 133 ? 1.7135 1.6988 1.2524 0.4518 -0.0005 -0.0011 132 GLU B C +3399 O O . GLU B 133 ? 1.6626 1.6417 1.2008 0.4496 -0.0002 -0.0007 132 GLU B O +3400 C CB . GLU B 133 ? 1.4349 1.4254 0.9733 0.4543 0.0030 0.0021 132 GLU B CB +3401 C CG . GLU B 133 ? 2.8096 2.8042 2.3489 0.4556 0.0040 0.0030 132 GLU B CG +3402 C CD . GLU B 133 ? 2.5411 2.5320 2.0809 0.4538 0.0037 0.0029 132 GLU B CD +3403 O OE1 . GLU B 133 ? 2.4671 2.4511 2.0057 0.4515 0.0041 0.0033 132 GLU B OE1 +3404 O OE2 . GLU B 133 ? 1.9239 1.9188 1.4652 0.4548 0.0032 0.0026 132 GLU B OE2 +3405 N N . ASP B 134 ? 1.4206 1.4074 0.9596 0.4524 -0.0016 -0.0022 133 ASP B N +3406 C CA . ASP B 134 ? 1.4497 1.4310 0.9880 0.4504 -0.0026 -0.0031 133 ASP B CA +3407 C C . ASP B 134 ? 1.7958 1.7795 1.3357 0.4507 -0.0053 -0.0056 133 ASP B C +3408 O O . ASP B 134 ? 1.7165 1.6970 1.2561 0.4496 -0.0064 -0.0065 133 ASP B O +3409 C CB . ASP B 134 ? 2.2727 2.2526 1.8092 0.4507 -0.0012 -0.0020 133 ASP B CB +3410 C CG . ASP B 134 ? 2.5530 2.5399 2.0899 0.4535 -0.0010 -0.0020 133 ASP B CG +3411 O OD1 . ASP B 134 ? 2.4405 2.4328 1.9782 0.4553 -0.0005 -0.0015 133 ASP B OD1 +3412 O OD2 . ASP B 134 ? 2.7149 2.7020 2.2512 0.4538 -0.0014 -0.0024 133 ASP B OD2 +3413 N N . GLY B 135 ? 1.9612 1.9508 1.5029 0.4523 -0.0064 -0.0065 134 GLY B N +3414 C CA . GLY B 135 ? 1.7906 1.7836 1.3341 0.4529 -0.0089 -0.0089 134 GLY B CA +3415 C C . GLY B 135 ? 1.8897 1.8782 1.4376 0.4495 -0.0112 -0.0103 134 GLY B C +3416 O O . GLY B 135 ? 1.8543 1.8362 1.4014 0.4471 -0.0107 -0.0096 134 GLY B O +3417 N N . ASN B 136 ? 1.8451 1.8371 1.3986 0.4487 -0.0139 -0.0121 135 ASN B N +3418 C CA . ASN B 136 ? 1.1018 1.0900 0.6613 0.4450 -0.0164 -0.0133 135 ASN B CA +3419 C C . ASN B 136 ? 1.5170 1.5042 1.0808 0.4430 -0.0167 -0.0128 135 ASN B C +3420 O O . ASN B 136 ? 1.3164 1.2979 0.8825 0.4398 -0.0173 -0.0127 135 ASN B O +3421 C CB . ASN B 136 ? 1.2119 1.2041 0.7760 0.4449 -0.0191 -0.0155 135 ASN B CB +3422 C CG . ASN B 136 ? 1.4371 1.4270 0.9986 0.4450 -0.0195 -0.0164 135 ASN B CG +3423 O OD1 . ASN B 136 ? 1.1439 1.1279 0.7017 0.4440 -0.0183 -0.0156 135 ASN B OD1 +3424 N ND2 . ASN B 136 ? 1.2499 1.2445 0.8135 0.4461 -0.0213 -0.0181 135 ASN B ND2 +3425 N N . ILE B 137 ? 1.3398 1.3327 0.9046 0.4448 -0.0163 -0.0123 136 ILE B N +3426 C CA . ILE B 137 ? 1.5074 1.5001 1.0759 0.4433 -0.0164 -0.0115 136 ILE B CA +3427 C C . ILE B 137 ? 1.6518 1.6395 1.2161 0.4429 -0.0139 -0.0095 136 ILE B C +3428 O O . ILE B 137 ? 1.2172 1.1988 0.7831 0.4398 -0.0142 -0.0093 136 ILE B O +3429 C CB . ILE B 137 ? 1.3220 1.3226 0.8926 0.4456 -0.0166 -0.0114 136 ILE B CB +3430 C CG1 . ILE B 137 ? 0.9830 0.9885 0.5591 0.4455 -0.0194 -0.0135 136 ILE B CG1 +3431 C CG2 . ILE B 137 ? 0.9043 0.9045 0.4779 0.4443 -0.0162 -0.0103 136 ILE B CG2 +3432 C CD1 . ILE B 137 ? 1.3375 1.3462 0.9110 0.4478 -0.0197 -0.0146 136 ILE B CD1 +3433 N N . LEU B 138 ? 1.4395 1.4296 0.9983 0.4459 -0.0113 -0.0081 137 LEU B N +3434 C CA . LEU B 138 ? 1.4548 1.4412 1.0098 0.4459 -0.0088 -0.0062 137 LEU B CA +3435 C C . LEU B 138 ? 1.5430 1.5219 1.0942 0.4442 -0.0078 -0.0057 137 LEU B C +3436 O O . LEU B 138 ? 1.1654 1.1400 0.7144 0.4433 -0.0062 -0.0043 137 LEU B O +3437 C CB . LEU B 138 ? 1.1920 1.1830 0.7418 0.4497 -0.0063 -0.0049 137 LEU B CB +3438 C CG . LEU B 138 ? 1.4463 1.4441 0.9999 0.4510 -0.0068 -0.0048 137 LEU B CG +3439 C CD1 . LEU B 138 ? 1.7159 1.7183 1.2642 0.4548 -0.0043 -0.0036 137 LEU B CD1 +3440 C CD2 . LEU B 138 ? 1.0039 0.9993 0.5611 0.4486 -0.0070 -0.0041 137 LEU B CD2 +3441 N N . GLY B 139 ? 1.2379 1.2154 0.7885 0.4439 -0.0088 -0.0068 138 GLY B N +3442 C CA . GLY B 139 ? 1.4549 1.4252 1.0026 0.4421 -0.0083 -0.0066 138 GLY B CA +3443 C C . GLY B 139 ? 1.5982 1.5637 1.1515 0.4380 -0.0105 -0.0076 138 GLY B C +3444 O O . GLY B 139 ? 1.5426 1.5018 1.0944 0.4360 -0.0100 -0.0072 138 GLY B O +3445 N N . HIS B 140 ? 1.5804 1.5493 1.1402 0.4369 -0.0128 -0.0088 139 HIS B N +3446 C CA . HIS B 140 ? 1.4859 1.4510 1.0518 0.4331 -0.0151 -0.0099 139 HIS B CA +3447 C C . HIS B 140 ? 1.2552 1.2168 0.8214 0.4316 -0.0164 -0.0112 139 HIS B C +3448 O O . HIS B 140 ? 1.2898 1.2450 0.8556 0.4291 -0.0163 -0.0110 139 HIS B O +3449 C CB . HIS B 140 ? 1.4286 1.3886 0.9953 0.4307 -0.0143 -0.0087 139 HIS B CB +3450 C CG . HIS B 140 ? 1.5089 1.4725 1.0778 0.4313 -0.0140 -0.0080 139 HIS B CG +3451 N ND1 . HIS B 140 ? 1.4725 1.4353 1.0378 0.4323 -0.0116 -0.0061 139 HIS B ND1 +3452 C CD2 . HIS B 140 ? 1.9362 1.9044 1.5108 0.4310 -0.0158 -0.0087 139 HIS B CD2 +3453 C CE1 . HIS B 140 ? 1.1890 1.1556 0.7575 0.4326 -0.0119 -0.0058 139 HIS B CE1 +3454 N NE2 . HIS B 140 ? 1.5480 1.5180 1.1222 0.4319 -0.0144 -0.0073 139 HIS B NE2 +3455 N N . LYS B 141 ? 1.5380 1.5039 1.1049 0.4332 -0.0177 -0.0126 140 LYS B N +3456 C CA . LYS B 141 ? 1.5926 1.5560 1.1602 0.4320 -0.0191 -0.0140 140 LYS B CA +3457 C C . LYS B 141 ? 1.6138 1.5799 1.1884 0.4306 -0.0222 -0.0161 140 LYS B C +3458 O O . LYS B 141 ? 1.3468 1.3125 0.9224 0.4301 -0.0236 -0.0176 140 LYS B O +3459 C CB . LYS B 141 ? 1.5800 1.5456 1.1417 0.4351 -0.0179 -0.0138 140 LYS B CB +3460 C CG . LYS B 141 ? 1.5495 1.5115 1.1040 0.4363 -0.0149 -0.0119 140 LYS B CG +3461 C CD . LYS B 141 ? 1.7951 1.7619 1.3441 0.4403 -0.0135 -0.0115 140 LYS B CD +3462 C CE . LYS B 141 ? 1.8310 1.7952 1.3729 0.4419 -0.0103 -0.0095 140 LYS B CE +3463 N NZ . LYS B 141 ? 1.8821 1.8511 1.4210 0.4451 -0.0090 -0.0088 140 LYS B NZ +3464 N N . LEU B 142 ? 1.3133 1.2821 0.8927 0.4299 -0.0232 -0.0163 141 LEU B N +3465 C CA . LEU B 142 ? 1.3601 1.3306 0.9467 0.4280 -0.0262 -0.0183 141 LEU B CA +3466 C C . LEU B 142 ? 1.4350 1.3989 1.0253 0.4239 -0.0273 -0.0187 141 LEU B C +3467 O O . LEU B 142 ? 1.2625 1.2218 0.8518 0.4224 -0.0260 -0.0174 141 LEU B O +3468 C CB . LEU B 142 ? 1.3719 1.3481 0.9624 0.4288 -0.0269 -0.0183 141 LEU B CB +3469 C CG . LEU B 142 ? 0.8925 0.8761 0.4804 0.4327 -0.0261 -0.0182 141 LEU B CG +3470 C CD1 . LEU B 142 ? 1.1071 1.0959 0.6989 0.4333 -0.0267 -0.0179 141 LEU B CD1 +3471 C CD2 . LEU B 142 ? 1.1744 1.1614 0.7631 0.4338 -0.0278 -0.0200 141 LEU B CD2 +3472 N N . GLU B 143 ? 1.2468 1.2100 0.8413 0.4222 -0.0296 -0.0207 142 GLU B N +3473 C CA . GLU B 143 ? 1.2383 1.1959 0.8374 0.4183 -0.0310 -0.0214 142 GLU B CA +3474 C C . GLU B 143 ? 1.3811 1.3405 0.9864 0.4168 -0.0325 -0.0218 142 GLU B C +3475 O O . GLU B 143 ? 1.4035 1.3691 1.0114 0.4184 -0.0335 -0.0225 142 GLU B O +3476 C CB . GLU B 143 ? 1.1985 1.1555 0.8001 0.4173 -0.0331 -0.0235 142 GLU B CB +3477 C CG . GLU B 143 ? 1.1805 1.1332 0.7773 0.4173 -0.0320 -0.0232 142 GLU B CG +3478 C CD . GLU B 143 ? 1.6543 1.6059 1.2545 0.4158 -0.0341 -0.0253 142 GLU B CD +3479 O OE1 . GLU B 143 ? 1.6438 1.5995 1.2490 0.4157 -0.0363 -0.0271 142 GLU B OE1 +3480 O OE2 . GLU B 143 ? 1.5607 1.5075 1.1586 0.4147 -0.0336 -0.0251 142 GLU B OE2 +3481 N N . TYR B 144 ? 1.1166 1.0708 0.7243 0.4137 -0.0326 -0.0213 143 TYR B N +3482 C CA . TYR B 144 ? 1.0655 1.0208 0.6792 0.4120 -0.0339 -0.0216 143 TYR B CA +3483 C C . TYR B 144 ? 1.2566 1.2137 0.8772 0.4104 -0.0369 -0.0239 143 TYR B C +3484 O O . TYR B 144 ? 1.1086 1.0618 0.7338 0.4071 -0.0383 -0.0246 143 TYR B O +3485 C CB . TYR B 144 ? 1.0046 0.9537 0.6190 0.4090 -0.0332 -0.0204 143 TYR B CB +3486 C CG . TYR B 144 ? 1.0389 0.9896 0.6578 0.4080 -0.0338 -0.0200 143 TYR B CG +3487 C CD1 . TYR B 144 ? 1.3913 1.3486 1.0110 0.4105 -0.0339 -0.0198 143 TYR B CD1 +3488 C CD2 . TYR B 144 ? 1.0945 1.0404 0.7170 0.4046 -0.0343 -0.0198 143 TYR B CD2 +3489 C CE1 . TYR B 144 ? 1.0679 1.0268 0.6917 0.4096 -0.0345 -0.0194 143 TYR B CE1 +3490 C CE2 . TYR B 144 ? 1.1675 1.1149 0.7942 0.4038 -0.0349 -0.0194 143 TYR B CE2 +3491 C CZ . TYR B 144 ? 1.2795 1.2334 0.9068 0.4063 -0.0350 -0.0192 143 TYR B CZ +3492 O OH . TYR B 144 ? 1.0904 1.0460 0.7217 0.4054 -0.0356 -0.0187 143 TYR B OH +3493 N N . ASN B 145 ? 1.0093 0.9724 0.6307 0.4126 -0.0380 -0.0251 144 ASN B N +3494 C CA . ASN B 145 ? 1.0747 1.0399 0.7025 0.4113 -0.0409 -0.0274 144 ASN B CA +3495 C C . ASN B 145 ? 0.8895 0.8626 0.5191 0.4139 -0.0419 -0.0283 144 ASN B C +3496 O O . ASN B 145 ? 1.0741 1.0514 0.7005 0.4166 -0.0405 -0.0271 144 ASN B O +3497 C CB . ASN B 145 ? 0.7058 0.6675 0.3338 0.4100 -0.0418 -0.0289 144 ASN B CB +3498 C CG . ASN B 145 ? 1.4876 1.4509 1.1095 0.4128 -0.0406 -0.0287 144 ASN B CG +3499 O OD1 . ASN B 145 ? 1.0205 0.9899 0.6414 0.4157 -0.0407 -0.0292 144 ASN B OD1 +3500 N ND2 . ASN B 145 ? 1.3722 1.3301 0.9904 0.4119 -0.0394 -0.0281 144 ASN B ND2 +3501 N N . TYR B 146 ? 0.9603 0.9356 0.5953 0.4130 -0.0445 -0.0306 145 TYR B N +3502 C CA . TYR B 146 ? 1.2883 1.2712 0.9256 0.4153 -0.0458 -0.0317 145 TYR B CA +3503 C C . TYR B 146 ? 1.1668 1.1514 0.8074 0.4149 -0.0481 -0.0343 145 TYR B C +3504 O O . TYR B 146 ? 1.1301 1.1097 0.7725 0.4124 -0.0490 -0.0353 145 TYR B O +3505 C CB . TYR B 146 ? 0.7573 0.7429 0.3997 0.4145 -0.0467 -0.0314 145 TYR B CB +3506 C CG . TYR B 146 ? 1.0830 1.0756 0.7236 0.4178 -0.0458 -0.0305 145 TYR B CG +3507 C CD1 . TYR B 146 ? 1.1202 1.1128 0.7547 0.4198 -0.0431 -0.0283 145 TYR B CD1 +3508 C CD2 . TYR B 146 ? 1.4002 1.3993 1.0453 0.4188 -0.0477 -0.0319 145 TYR B CD2 +3509 C CE1 . TYR B 146 ? 1.2527 1.2518 0.8858 0.4228 -0.0423 -0.0275 145 TYR B CE1 +3510 C CE2 . TYR B 146 ? 1.1271 1.1328 0.7708 0.4217 -0.0470 -0.0311 145 TYR B CE2 +3511 C CZ . TYR B 146 ? 1.0777 1.0834 0.7154 0.4237 -0.0442 -0.0289 145 TYR B CZ +3512 O OH . TYR B 146 ? 1.1118 1.1242 0.7485 0.4266 -0.0435 -0.0281 145 TYR B OH +3513 N N . ASN B 147 ? 1.2825 1.2740 0.9238 0.4175 -0.0490 -0.0353 146 ASN B N +3514 C CA . ASN B 147 ? 1.1533 1.1474 0.7976 0.4175 -0.0513 -0.0379 146 ASN B CA +3515 C C . ASN B 147 ? 1.2126 1.2130 0.8628 0.4179 -0.0533 -0.0391 146 ASN B C +3516 O O . ASN B 147 ? 1.2133 1.2158 0.8646 0.4183 -0.0528 -0.0378 146 ASN B O +3517 C CB . ASN B 147 ? 1.1714 1.1686 0.8104 0.4206 -0.0503 -0.0381 146 ASN B CB +3518 C CG . ASN B 147 ? 1.0686 1.0600 0.7015 0.4205 -0.0484 -0.0369 146 ASN B CG +3519 O OD1 . ASN B 147 ? 1.1869 1.1721 0.8210 0.4177 -0.0487 -0.0371 146 ASN B OD1 +3520 N ND2 . ASN B 147 ? 1.6695 1.6630 1.2960 0.4236 -0.0462 -0.0355 146 ASN B ND2 +3521 N N . SER B 148 ? 1.1583 1.1618 0.8122 0.4180 -0.0556 -0.0416 147 SER B N +3522 C CA . SER B 148 ? 0.9996 1.0086 0.6598 0.4179 -0.0578 -0.0430 147 SER B CA +3523 C C . SER B 148 ? 0.7722 0.7893 0.4311 0.4214 -0.0580 -0.0437 147 SER B C +3524 O O . SER B 148 ? 1.6073 1.6254 1.2621 0.4232 -0.0575 -0.0442 147 SER B O +3525 C CB . SER B 148 ? 0.8740 0.8807 0.5406 0.4150 -0.0605 -0.0454 147 SER B CB +3526 O OG . SER B 148 ? 1.2861 1.2865 0.9551 0.4117 -0.0604 -0.0447 147 SER B OG +3527 N N . HIS B 149 ? 0.9973 1.0201 0.6595 0.4223 -0.0587 -0.0436 148 HIS B N +3528 C CA . HIS B 149 ? 1.2888 1.3194 0.9491 0.4258 -0.0585 -0.0437 148 HIS B CA +3529 C C . HIS B 149 ? 1.2249 1.2621 0.8920 0.4259 -0.0610 -0.0453 148 HIS B C +3530 O O . HIS B 149 ? 1.3446 1.3807 1.0169 0.4236 -0.0622 -0.0455 148 HIS B O +3531 C CB . HIS B 149 ? 1.0216 1.0533 0.6765 0.4279 -0.0557 -0.0409 148 HIS B CB +3532 C CG . HIS B 149 ? 1.1160 1.1417 0.7643 0.4280 -0.0532 -0.0392 148 HIS B CG +3533 N ND1 . HIS B 149 ? 1.1935 1.2138 0.8400 0.4266 -0.0515 -0.0371 148 HIS B ND1 +3534 C CD2 . HIS B 149 ? 1.7382 1.7623 1.3811 0.4293 -0.0521 -0.0393 148 HIS B CD2 +3535 C CE1 . HIS B 149 ? 1.3647 1.3805 1.0051 0.4270 -0.0495 -0.0361 148 HIS B CE1 +3536 N NE2 . HIS B 149 ? 1.0503 1.0682 0.6884 0.4287 -0.0498 -0.0373 148 HIS B NE2 +3537 N N . ASN B 150 ? 1.1793 1.2233 0.8461 0.4284 -0.0617 -0.0466 149 ASN B N +3538 C CA . ASN B 150 ? 1.1921 1.2429 0.8649 0.4288 -0.0639 -0.0480 149 ASN B CA +3539 C C . ASN B 150 ? 1.0851 1.1421 0.7559 0.4315 -0.0625 -0.0463 149 ASN B C +3540 O O . ASN B 150 ? 1.3433 1.4031 1.0086 0.4343 -0.0608 -0.0455 149 ASN B O +3541 C CB . ASN B 150 ? 1.4589 1.5133 1.1340 0.4294 -0.0661 -0.0510 149 ASN B CB +3542 C CG . ASN B 150 ? 1.4036 1.4520 1.0813 0.4265 -0.0676 -0.0528 149 ASN B CG +3543 O OD1 . ASN B 150 ? 1.7257 1.7703 1.4081 0.4236 -0.0688 -0.0531 149 ASN B OD1 +3544 N ND2 . ASN B 150 ? 1.4710 1.5185 1.1456 0.4274 -0.0676 -0.0540 149 ASN B ND2 +3545 N N . VAL B 151 ? 1.3140 1.3733 0.9896 0.4306 -0.0633 -0.0457 150 VAL B N +3546 C CA . VAL B 151 ? 0.9340 0.9983 0.6082 0.4326 -0.0619 -0.0437 150 VAL B CA +3547 C C . VAL B 151 ? 1.3846 1.4578 1.0629 0.4343 -0.0638 -0.0452 150 VAL B C +3548 O O . VAL B 151 ? 1.5118 1.5875 1.1966 0.4328 -0.0658 -0.0460 150 VAL B O +3549 C CB . VAL B 151 ? 1.3790 1.4396 1.0557 0.4304 -0.0614 -0.0419 150 VAL B CB +3550 C CG1 . VAL B 151 ? 0.9293 0.9961 0.6076 0.4318 -0.0611 -0.0404 150 VAL B CG1 +3551 C CG2 . VAL B 151 ? 1.0940 1.1470 0.7652 0.4296 -0.0589 -0.0399 150 VAL B CG2 +3552 N N . TYR B 152 ? 1.2312 1.3095 0.9059 0.4372 -0.0632 -0.0457 151 TYR B N +3553 C CA . TYR B 152 ? 1.2045 1.2915 0.8834 0.4387 -0.0652 -0.0474 151 TYR B CA +3554 C C . TYR B 152 ? 1.3332 1.4262 1.0141 0.4398 -0.0649 -0.0459 151 TYR B C +3555 O O . TYR B 152 ? 1.2764 1.3704 0.9525 0.4417 -0.0624 -0.0436 151 TYR B O +3556 C CB . TYR B 152 ? 1.0537 1.1444 0.7290 0.4412 -0.0652 -0.0489 151 TYR B CB +3557 C CG . TYR B 152 ? 1.2963 1.3810 0.9697 0.4401 -0.0655 -0.0503 151 TYR B CG +3558 C CD1 . TYR B 152 ? 1.0994 1.1782 0.7662 0.4404 -0.0631 -0.0487 151 TYR B CD1 +3559 C CD2 . TYR B 152 ? 1.3936 1.4786 1.0719 0.4386 -0.0683 -0.0532 151 TYR B CD2 +3560 C CE1 . TYR B 152 ? 1.6158 1.6891 1.2808 0.4392 -0.0633 -0.0499 151 TYR B CE1 +3561 C CE2 . TYR B 152 ? 1.2270 1.3064 0.9036 0.4374 -0.0686 -0.0545 151 TYR B CE2 +3562 C CZ . TYR B 152 ? 1.4726 1.5462 1.1425 0.4378 -0.0660 -0.0527 151 TYR B CZ +3563 O OH . TYR B 152 ? 1.1789 1.2470 0.8470 0.4366 -0.0662 -0.0537 151 TYR B OH +3564 N N . ILE B 153 ? 1.1916 1.2885 0.8796 0.4386 -0.0674 -0.0472 152 ILE B N +3565 C CA . ILE B 153 ? 1.1594 1.2622 0.8504 0.4393 -0.0675 -0.0460 152 ILE B CA +3566 C C . ILE B 153 ? 1.5367 1.6487 1.2303 0.4414 -0.0692 -0.0477 152 ILE B C +3567 O O . ILE B 153 ? 1.5995 1.7129 1.2946 0.4414 -0.0709 -0.0502 152 ILE B O +3568 C CB . ILE B 153 ? 1.1547 1.2549 0.8522 0.4362 -0.0692 -0.0459 152 ILE B CB +3569 C CG1 . ILE B 153 ? 0.8888 0.9797 0.5837 0.4341 -0.0676 -0.0444 152 ILE B CG1 +3570 C CG2 . ILE B 153 ? 0.9733 1.0792 0.6739 0.4368 -0.0692 -0.0443 152 ILE B CG2 +3571 C CD1 . ILE B 153 ? 1.5172 1.6050 1.2178 0.4310 -0.0689 -0.0441 152 ILE B CD1 +3572 N N . MET B 154 ? 1.6401 1.7585 1.3343 0.4430 -0.0686 -0.0463 153 MET B N +3573 C CA . MET B 154 ? 1.7039 1.8315 1.4001 0.4452 -0.0698 -0.0475 153 MET B CA +3574 C C . MET B 154 ? 1.5524 1.6853 1.2514 0.4457 -0.0696 -0.0457 153 MET B C +3575 O O . MET B 154 ? 1.6985 1.8294 1.3941 0.4461 -0.0673 -0.0431 153 MET B O +3576 C CB . MET B 154 ? 1.6830 1.8126 1.3722 0.4483 -0.0679 -0.0473 153 MET B CB +3577 C CG . MET B 154 ? 1.8903 2.0288 1.5812 0.4504 -0.0693 -0.0492 153 MET B CG +3578 S SD . MET B 154 ? 2.7877 2.9275 2.4708 0.4537 -0.0674 -0.0496 153 MET B SD +3579 C CE . MET B 154 ? 1.4990 1.6278 1.1766 0.4523 -0.0656 -0.0488 153 MET B CE +3580 N N . ALA B 155 ? 1.4942 1.6338 1.1994 0.4455 -0.0721 -0.0472 154 ALA B N +3581 C CA . ALA B 155 ? 1.5705 1.7155 1.2786 0.4459 -0.0721 -0.0455 154 ALA B CA +3582 C C . ALA B 155 ? 1.8711 2.0217 1.5741 0.4493 -0.0698 -0.0438 154 ALA B C +3583 O O . ALA B 155 ? 1.5613 1.7141 1.2602 0.4515 -0.0691 -0.0447 154 ALA B O +3584 C CB . ALA B 155 ? 1.3535 1.5046 1.0698 0.4448 -0.0754 -0.0474 154 ALA B CB +3585 N N . ASP B 156 ? 1.9395 2.0921 1.6426 0.4497 -0.0685 -0.0413 155 ASP B N +3586 C CA . ASP B 156 ? 2.2352 2.3940 1.9347 0.4527 -0.0666 -0.0396 155 ASP B CA +3587 C C . ASP B 156 ? 2.4454 2.6113 2.1511 0.4524 -0.0681 -0.0391 155 ASP B C +3588 O O . ASP B 156 ? 1.9337 2.0991 1.6396 0.4520 -0.0670 -0.0367 155 ASP B O +3589 C CB . ASP B 156 ? 2.1552 2.3091 1.8479 0.4536 -0.0631 -0.0368 155 ASP B CB +3590 C CG . ASP B 156 ? 2.1706 2.3306 1.8590 0.4569 -0.0609 -0.0352 155 ASP B CG +3591 O OD1 . ASP B 156 ? 2.3040 2.4719 1.9943 0.4586 -0.0621 -0.0363 155 ASP B OD1 +3592 O OD2 . ASP B 156 ? 1.7567 1.9134 1.4397 0.4579 -0.0581 -0.0328 155 ASP B OD2 +3593 N N . LYS B 157 ? 2.6352 2.8075 2.3458 0.4525 -0.0708 -0.0414 156 LYS B N +3594 C CA . LYS B 157 ? 2.4809 2.6599 2.1985 0.4517 -0.0729 -0.0414 156 LYS B CA +3595 C C . LYS B 157 ? 2.2135 2.3983 1.9294 0.4538 -0.0711 -0.0389 156 LYS B C +3596 O O . LYS B 157 ? 1.7278 1.9158 1.4484 0.4528 -0.0720 -0.0378 156 LYS B O +3597 C CB . LYS B 157 ? 2.3788 2.5638 2.1014 0.4517 -0.0759 -0.0445 156 LYS B CB +3598 C CG . LYS B 157 ? 2.3829 2.5634 2.1107 0.4487 -0.0786 -0.0469 156 LYS B CG +3599 C CD . LYS B 157 ? 2.2308 2.4164 1.9623 0.4489 -0.0813 -0.0502 156 LYS B CD +3600 C CE . LYS B 157 ? 2.1716 2.3535 1.9093 0.4457 -0.0842 -0.0525 156 LYS B CE +3601 N NZ . LYS B 157 ? 2.0915 2.2640 1.8262 0.4444 -0.0835 -0.0531 156 LYS B NZ +3602 N N . GLN B 158 ? 2.4089 2.5949 2.1180 0.4566 -0.0685 -0.0379 157 GLN B N +3603 C CA . GLN B 158 ? 2.4096 2.6010 2.1166 0.4588 -0.0666 -0.0355 157 GLN B CA +3604 C C . GLN B 158 ? 2.1921 2.3783 1.8969 0.4580 -0.0644 -0.0326 157 GLN B C +3605 O O . GLN B 158 ? 1.9450 2.1354 1.6516 0.4584 -0.0640 -0.0307 157 GLN B O +3606 C CB . GLN B 158 ? 2.3201 2.5150 2.0208 0.4622 -0.0646 -0.0355 157 GLN B CB +3607 C CG . GLN B 158 ? 2.5848 2.7864 2.2877 0.4633 -0.0667 -0.0382 157 GLN B CG +3608 C CD . GLN B 158 ? 2.6444 2.8556 2.3533 0.4635 -0.0687 -0.0385 157 GLN B CD +3609 O OE1 . GLN B 158 ? 2.7284 2.9405 2.4436 0.4613 -0.0706 -0.0384 157 GLN B OE1 +3610 N NE2 . GLN B 158 ? 2.3888 2.6073 2.0958 0.4662 -0.0682 -0.0389 157 GLN B NE2 +3611 N N . LYS B 159 ? 2.2887 2.4659 1.9899 0.4569 -0.0632 -0.0322 158 LYS B N +3612 C CA . LYS B 159 ? 2.0931 2.2649 1.7918 0.4562 -0.0610 -0.0295 158 LYS B CA +3613 C C . LYS B 159 ? 2.0019 2.1686 1.7059 0.4527 -0.0626 -0.0295 158 LYS B C +3614 O O . LYS B 159 ? 1.5208 1.6820 1.2229 0.4517 -0.0610 -0.0275 158 LYS B O +3615 C CB . LYS B 159 ? 1.8090 1.9745 1.4995 0.4574 -0.0579 -0.0285 158 LYS B CB +3616 C CG . LYS B 159 ? 2.4361 2.6061 2.1210 0.4608 -0.0562 -0.0286 158 LYS B CG +3617 C CD . LYS B 159 ? 2.5943 2.7736 2.2806 0.4629 -0.0560 -0.0276 158 LYS B CD +3618 C CE . LYS B 159 ? 2.2720 2.4575 1.9559 0.4657 -0.0560 -0.0290 158 LYS B CE +3619 N NZ . LYS B 159 ? 2.1921 2.3874 1.8791 0.4672 -0.0567 -0.0286 158 LYS B NZ +3620 N N . ASN B 160 ? 1.9926 2.1611 1.7031 0.4509 -0.0658 -0.0318 159 ASN B N +3621 C CA . ASN B 160 ? 2.0183 2.1829 1.7347 0.4476 -0.0677 -0.0321 159 ASN B CA +3622 C C . ASN B 160 ? 1.8941 2.0485 1.6075 0.4458 -0.0666 -0.0317 159 ASN B C +3623 O O . ASN B 160 ? 1.5867 1.7367 1.3026 0.4435 -0.0668 -0.0306 159 ASN B O +3624 C CB . ASN B 160 ? 1.9660 2.1346 1.6860 0.4472 -0.0677 -0.0299 159 ASN B CB +3625 C CG . ASN B 160 ? 2.1603 2.3271 1.8878 0.4440 -0.0703 -0.0305 159 ASN B CG +3626 O OD1 . ASN B 160 ? 2.0899 2.2573 1.8221 0.4426 -0.0731 -0.0330 159 ASN B OD1 +3627 N ND2 . ASN B 160 ? 1.9665 2.1311 1.6951 0.4429 -0.0695 -0.0282 159 ASN B ND2 +3628 N N . GLY B 161 ? 1.8331 1.9836 1.5410 0.4468 -0.0653 -0.0325 160 GLY B N +3629 C CA . GLY B 161 ? 1.7690 1.9099 1.4737 0.4451 -0.0642 -0.0322 160 GLY B CA +3630 C C . GLY B 161 ? 1.5895 1.7275 1.2927 0.4450 -0.0651 -0.0347 160 GLY B C +3631 O O . GLY B 161 ? 1.6112 1.7535 1.3187 0.4448 -0.0675 -0.0371 160 GLY B O +3632 N N . ILE B 162 ? 1.5426 1.6734 1.2400 0.4449 -0.0631 -0.0343 161 ILE B N +3633 C CA . ILE B 162 ? 1.5631 1.6908 1.2586 0.4448 -0.0638 -0.0365 161 ILE B CA +3634 C C . ILE B 162 ? 1.4480 1.5728 1.1350 0.4470 -0.0608 -0.0354 161 ILE B C +3635 O O . ILE B 162 ? 1.5435 1.6652 1.2263 0.4475 -0.0582 -0.0329 161 ILE B O +3636 C CB . ILE B 162 ? 1.5962 1.7163 1.2949 0.4414 -0.0653 -0.0377 161 ILE B CB +3637 C CG1 . ILE B 162 ? 1.5359 1.6481 1.2316 0.4400 -0.0632 -0.0355 161 ILE B CG1 +3638 C CG2 . ILE B 162 ? 1.6432 1.7663 1.3506 0.4393 -0.0685 -0.0391 161 ILE B CG2 +3639 C CD1 . ILE B 162 ? 1.1375 1.2418 0.8351 0.4369 -0.0644 -0.0368 161 ILE B CD1 +3640 N N . LYS B 163 ? 1.3337 1.4596 1.0182 0.4483 -0.0610 -0.0371 162 LYS B N +3641 C CA . LYS B 163 ? 1.4165 1.5387 1.0930 0.4501 -0.0584 -0.0364 162 LYS B CA +3642 C C . LYS B 163 ? 1.5164 1.6302 1.1925 0.4477 -0.0590 -0.0375 162 LYS B C +3643 O O . LYS B 163 ? 1.6132 1.7262 1.2947 0.4456 -0.0616 -0.0396 162 LYS B O +3644 C CB . LYS B 163 ? 1.7011 1.8294 1.3749 0.4530 -0.0584 -0.0376 162 LYS B CB +3645 C CG . LYS B 163 ? 2.1715 2.3038 1.8397 0.4562 -0.0555 -0.0355 162 LYS B CG +3646 C CD . LYS B 163 ? 2.1789 2.3185 1.8455 0.4591 -0.0558 -0.0368 162 LYS B CD +3647 C CE . LYS B 163 ? 2.1296 2.2737 1.7912 0.4623 -0.0531 -0.0346 162 LYS B CE +3648 N NZ . LYS B 163 ? 2.1116 2.2599 1.7763 0.4622 -0.0529 -0.0328 162 LYS B NZ +3649 N N . VAL B 164 ? 1.3461 1.4536 1.0160 0.4479 -0.0565 -0.0361 163 VAL B N +3650 C CA . VAL B 164 ? 1.3194 1.4188 0.9887 0.4456 -0.0569 -0.0371 163 VAL B CA +3651 C C . VAL B 164 ? 1.0363 1.1324 0.6977 0.4473 -0.0546 -0.0365 163 VAL B C +3652 O O . VAL B 164 ? 1.5201 1.6164 1.1761 0.4493 -0.0519 -0.0344 163 VAL B O +3653 C CB . VAL B 164 ? 1.5430 1.6355 1.2139 0.4427 -0.0566 -0.0356 163 VAL B CB +3654 C CG1 . VAL B 164 ? 1.0791 1.1637 0.7501 0.4401 -0.0573 -0.0368 163 VAL B CG1 +3655 C CG2 . VAL B 164 ? 1.3603 1.4562 1.0386 0.4411 -0.0585 -0.0357 163 VAL B CG2 +3656 N N . ASN B 165 ? 1.2193 1.3122 0.8801 0.4466 -0.0556 -0.0384 164 ASN B N +3657 C CA . ASN B 165 ? 1.3548 1.4435 1.0083 0.4478 -0.0534 -0.0378 164 ASN B CA +3658 C C . ASN B 165 ? 1.2337 1.3152 0.8871 0.4455 -0.0542 -0.0391 164 ASN B C +3659 O O . ASN B 165 ? 1.5248 1.6064 1.1836 0.4438 -0.0569 -0.0414 164 ASN B O +3660 C CB . ASN B 165 ? 1.3356 1.4306 0.9852 0.4514 -0.0526 -0.0382 164 ASN B CB +3661 C CG . ASN B 165 ? 1.5680 1.6680 1.2218 0.4516 -0.0554 -0.0410 164 ASN B CG +3662 O OD1 . ASN B 165 ? 1.8280 1.9323 1.4883 0.4507 -0.0576 -0.0422 164 ASN B OD1 +3663 N ND2 . ASN B 165 ? 2.0959 2.1951 1.7460 0.4527 -0.0552 -0.0422 164 ASN B ND2 +3664 N N . PHE B 166 ? 1.0291 1.1044 0.6764 0.4456 -0.0520 -0.0377 165 PHE B N +3665 C CA . PHE B 166 ? 1.3203 1.3884 0.9667 0.4435 -0.0524 -0.0387 165 PHE B CA +3666 C C . PHE B 166 ? 1.1349 1.1978 0.7736 0.4444 -0.0495 -0.0369 165 PHE B C +3667 O O . PHE B 166 ? 1.4681 1.5330 1.1021 0.4467 -0.0472 -0.0349 165 PHE B O +3668 C CB . PHE B 166 ? 1.3639 1.4267 1.0157 0.4398 -0.0539 -0.0390 165 PHE B CB +3669 C CG . PHE B 166 ? 1.2374 1.2978 0.8892 0.4389 -0.0524 -0.0367 165 PHE B CG +3670 C CD1 . PHE B 166 ? 1.0943 1.1601 0.7500 0.4393 -0.0530 -0.0361 165 PHE B CD1 +3671 C CD2 . PHE B 166 ? 0.7575 0.8101 0.4057 0.4374 -0.0507 -0.0351 165 PHE B CD2 +3672 C CE1 . PHE B 166 ? 0.9374 1.0009 0.5931 0.4384 -0.0517 -0.0339 165 PHE B CE1 +3673 C CE2 . PHE B 166 ? 1.0163 1.0667 0.6646 0.4365 -0.0494 -0.0331 165 PHE B CE2 +3674 C CZ . PHE B 166 ? 1.1299 1.1858 0.7820 0.4370 -0.0499 -0.0324 165 PHE B CZ +3675 N N . LYS B 167 ? 1.1021 1.1582 0.7395 0.4426 -0.0496 -0.0374 166 LYS B N +3676 C CA . LYS B 167 ? 1.3173 1.3689 0.9473 0.4436 -0.0471 -0.0361 166 LYS B CA +3677 C C . LYS B 167 ? 1.3476 1.3901 0.9772 0.4405 -0.0469 -0.0357 166 LYS B C +3678 O O . LYS B 167 ? 1.3278 1.3672 0.9592 0.4389 -0.0485 -0.0375 166 LYS B O +3679 C CB . LYS B 167 ? 0.9934 1.0482 0.6204 0.4459 -0.0474 -0.0375 166 LYS B CB +3680 C CG . LYS B 167 ? 1.6502 1.7008 1.2695 0.4471 -0.0450 -0.0362 166 LYS B CG +3681 C CD . LYS B 167 ? 2.0335 2.0861 1.6512 0.4485 -0.0459 -0.0381 166 LYS B CD +3682 C CE . LYS B 167 ? 1.7091 1.7708 1.3284 0.4511 -0.0469 -0.0393 166 LYS B CE +3683 N NZ . LYS B 167 ? 2.1679 2.2339 1.7820 0.4545 -0.0444 -0.0374 166 LYS B NZ +3684 N N . ILE B 168 ? 1.2432 1.2815 0.8703 0.4398 -0.0449 -0.0335 167 ILE B N +3685 C CA . ILE B 168 ? 1.3146 1.3445 0.9416 0.4368 -0.0446 -0.0330 167 ILE B CA +3686 C C . ILE B 168 ? 1.2691 1.2941 0.8897 0.4373 -0.0429 -0.0324 167 ILE B C +3687 O O . ILE B 168 ? 1.2847 1.3111 0.8992 0.4399 -0.0406 -0.0310 167 ILE B O +3688 C CB . ILE B 168 ? 0.9490 0.9763 0.5754 0.4359 -0.0430 -0.0307 167 ILE B CB +3689 C CG1 . ILE B 168 ? 1.2621 1.2944 0.8943 0.4356 -0.0443 -0.0308 167 ILE B CG1 +3690 C CG2 . ILE B 168 ? 1.1737 1.1925 0.8004 0.4326 -0.0428 -0.0303 167 ILE B CG2 +3691 C CD1 . ILE B 168 ? 1.5021 1.5334 1.1419 0.4327 -0.0472 -0.0327 167 ILE B CD1 +3692 N N . ARG B 169 ? 1.0344 1.0536 0.6564 0.4347 -0.0440 -0.0334 168 ARG B N +3693 C CA . ARG B 169 ? 1.1621 1.1761 0.7786 0.4347 -0.0424 -0.0328 168 ARG B CA +3694 C C . ARG B 169 ? 1.0306 1.0370 0.6459 0.4322 -0.0411 -0.0312 168 ARG B C +3695 O O . ARG B 169 ? 1.4382 1.4408 1.0584 0.4290 -0.0426 -0.0319 168 ARG B O +3696 C CB . ARG B 169 ? 1.3173 1.3302 0.9358 0.4337 -0.0444 -0.0351 168 ARG B CB +3697 C CG . ARG B 169 ? 1.4412 1.4615 1.0607 0.4362 -0.0458 -0.0369 168 ARG B CG +3698 C CD . ARG B 169 ? 1.3948 1.4140 1.0160 0.4353 -0.0477 -0.0391 168 ARG B CD +3699 N NE . ARG B 169 ? 1.5735 1.5911 1.2021 0.4322 -0.0503 -0.0410 168 ARG B NE +3700 C CZ . ARG B 169 ? 1.8791 1.9019 1.5136 0.4321 -0.0524 -0.0425 168 ARG B CZ +3701 N NH1 . ARG B 169 ? 1.6271 1.6572 1.2611 0.4349 -0.0522 -0.0424 168 ARG B NH1 +3702 N NH2 . ARG B 169 ? 1.8054 1.8261 1.4463 0.4291 -0.0547 -0.0441 168 ARG B NH2 +3703 N N . HIS B 170 ? 1.0119 1.0163 0.6208 0.4336 -0.0383 -0.0290 169 HIS B N +3704 C CA . HIS B 170 ? 1.3323 1.3294 0.9395 0.4314 -0.0369 -0.0274 169 HIS B CA +3705 C C . HIS B 170 ? 0.9638 0.9552 0.5669 0.4307 -0.0361 -0.0274 169 HIS B C +3706 O O . HIS B 170 ? 1.4500 1.4429 1.0479 0.4332 -0.0349 -0.0271 169 HIS B O +3707 C CB . HIS B 170 ? 0.9805 0.9781 0.5834 0.4330 -0.0342 -0.0250 169 HIS B CB +3708 C CG . HIS B 170 ? 1.1876 1.1904 0.7942 0.4336 -0.0347 -0.0247 169 HIS B CG +3709 N ND1 . HIS B 170 ? 1.3753 1.3756 0.9857 0.4313 -0.0351 -0.0241 169 HIS B ND1 +3710 C CD2 . HIS B 170 ? 1.4788 1.4891 1.0857 0.4364 -0.0348 -0.0248 169 HIS B CD2 +3711 C CE1 . HIS B 170 ? 1.2213 1.2274 0.8344 0.4325 -0.0354 -0.0238 169 HIS B CE1 +3712 N NE2 . HIS B 170 ? 0.8745 0.8868 0.4856 0.4356 -0.0353 -0.0243 169 HIS B NE2 +3713 N N . ASN B 171 ? 1.5812 1.5662 1.1868 0.4273 -0.0369 -0.0277 170 ASN B N +3714 C CA . ASN B 171 ? 1.3095 1.2887 0.9114 0.4264 -0.0361 -0.0275 170 ASN B CA +3715 C C . ASN B 171 ? 1.5546 1.5301 1.1500 0.4272 -0.0331 -0.0251 170 ASN B C +3716 O O . ASN B 171 ? 1.6569 1.6313 1.2526 0.4265 -0.0321 -0.0237 170 ASN B O +3717 C CB . ASN B 171 ? 1.4215 1.3951 1.0284 0.4224 -0.0378 -0.0286 170 ASN B CB +3718 C CG . ASN B 171 ? 1.4583 1.4343 1.0704 0.4217 -0.0406 -0.0312 170 ASN B CG +3719 O OD1 . ASN B 171 ? 1.4387 1.4212 1.0522 0.4238 -0.0416 -0.0323 170 ASN B OD1 +3720 N ND2 . ASN B 171 ? 1.4842 1.4551 1.0995 0.4186 -0.0419 -0.0323 170 ASN B ND2 +3721 N N . ILE B 172 ? 1.5043 1.4779 1.0941 0.4284 -0.0317 -0.0246 171 ILE B N +3722 C CA . ILE B 172 ? 1.5359 1.5057 1.1190 0.4293 -0.0289 -0.0224 171 ILE B CA +3723 C C . ILE B 172 ? 1.7375 1.7004 1.3195 0.4270 -0.0289 -0.0225 171 ILE B C +3724 O O . ILE B 172 ? 2.0940 2.0565 1.6793 0.4257 -0.0309 -0.0243 171 ILE B O +3725 C CB . ILE B 172 ? 1.3865 1.3611 0.9636 0.4334 -0.0272 -0.0216 171 ILE B CB +3726 C CG1 . ILE B 172 ? 1.3223 1.3040 0.9010 0.4356 -0.0273 -0.0216 171 ILE B CG1 +3727 C CG2 . ILE B 172 ? 1.1198 1.0907 0.6898 0.4345 -0.0242 -0.0195 171 ILE B CG2 +3728 C CD1 . ILE B 172 ? 1.4317 1.4197 1.0072 0.4393 -0.0268 -0.0219 171 ILE B CD1 +3729 N N . GLU B 173 ? 1.1843 1.1419 0.7620 0.4263 -0.0268 -0.0208 172 GLU B N +3730 C CA . GLU B 173 ? 1.8179 1.7689 1.3955 0.4237 -0.0270 -0.0209 172 GLU B CA +3731 C C . GLU B 173 ? 1.8831 1.8340 1.4579 0.4248 -0.0273 -0.0217 172 GLU B C +3732 O O . GLU B 173 ? 2.0317 1.9795 1.6096 0.4225 -0.0288 -0.0230 172 GLU B O +3733 C CB . GLU B 173 ? 1.5894 1.5342 1.1636 0.4223 -0.0249 -0.0190 172 GLU B CB +3734 C CG . GLU B 173 ? 2.2308 2.1689 1.8073 0.4187 -0.0258 -0.0195 172 GLU B CG +3735 C CD . GLU B 173 ? 2.7238 2.6556 2.2970 0.4171 -0.0238 -0.0177 172 GLU B CD +3736 O OE1 . GLU B 173 ? 2.4765 2.4082 2.0434 0.4193 -0.0214 -0.0161 172 GLU B OE1 +3737 O OE2 . GLU B 173 ? 2.9067 2.8338 2.4837 0.4137 -0.0246 -0.0180 172 GLU B OE2 +3738 N N . ASP B 174 ? 1.4206 1.3750 0.9898 0.4283 -0.0258 -0.0210 173 ASP B N +3739 C CA . ASP B 174 ? 1.7462 1.7008 1.3126 0.4295 -0.0259 -0.0216 173 ASP B CA +3740 C C . ASP B 174 ? 2.0521 2.0105 1.6233 0.4295 -0.0286 -0.0241 173 ASP B C +3741 O O . ASP B 174 ? 2.8149 2.7741 2.3839 0.4307 -0.0289 -0.0247 173 ASP B O +3742 C CB . ASP B 174 ? 1.9971 1.9548 1.5563 0.4334 -0.0236 -0.0202 173 ASP B CB +3743 C CG . ASP B 174 ? 1.8719 1.8364 1.4313 0.4360 -0.0234 -0.0201 173 ASP B CG +3744 O OD1 . ASP B 174 ? 1.7882 1.7564 1.3533 0.4354 -0.0254 -0.0216 173 ASP B OD1 +3745 O OD2 . ASP B 174 ? 1.8605 1.8268 1.4144 0.4387 -0.0210 -0.0185 173 ASP B OD2 +3746 N N . GLY B 175 ? 1.4821 1.4429 1.0596 0.4281 -0.0306 -0.0254 174 GLY B N +3747 C CA . GLY B 175 ? 1.4365 1.4010 1.0189 0.4279 -0.0332 -0.0277 174 GLY B CA +3748 C C . GLY B 175 ? 1.5588 1.5313 1.1412 0.4312 -0.0336 -0.0284 174 GLY B C +3749 O O . GLY B 175 ? 1.6974 1.6737 1.2843 0.4311 -0.0359 -0.0304 174 GLY B O +3750 N N . SER B 176 ? 1.1208 1.0961 0.6981 0.4340 -0.0315 -0.0267 175 SER B N +3751 C CA . SER B 176 ? 1.5787 1.5619 1.1558 0.4372 -0.0317 -0.0272 175 SER B CA +3752 C C . SER B 176 ? 1.4778 1.4642 1.0604 0.4364 -0.0328 -0.0276 175 SER B C +3753 O O . SER B 176 ? 1.4571 1.4395 1.0435 0.4334 -0.0335 -0.0276 175 SER B O +3754 C CB . SER B 176 ? 1.6744 1.6596 1.2440 0.4407 -0.0289 -0.0253 175 SER B CB +3755 O OG . SER B 176 ? 1.4344 1.4157 1.0010 0.4401 -0.0267 -0.0232 175 SER B OG +3756 N N . VAL B 177 ? 1.4633 1.4570 1.0464 0.4390 -0.0331 -0.0281 176 VAL B N +3757 C CA . VAL B 177 ? 1.2333 1.2308 0.8222 0.4384 -0.0345 -0.0287 176 VAL B CA +3758 C C . VAL B 177 ? 1.4249 1.4287 1.0116 0.4415 -0.0332 -0.0277 176 VAL B C +3759 O O . VAL B 177 ? 1.9391 1.9485 1.5235 0.4445 -0.0330 -0.0281 176 VAL B O +3760 C CB . VAL B 177 ? 1.1434 1.1441 0.7387 0.4374 -0.0377 -0.0314 176 VAL B CB +3761 C CG1 . VAL B 177 ? 1.3708 1.3771 0.9714 0.4376 -0.0390 -0.0320 176 VAL B CG1 +3762 C CG2 . VAL B 177 ? 1.4077 1.4021 1.0068 0.4337 -0.0392 -0.0325 176 VAL B CG2 +3763 N N . GLN B 178 ? 1.0020 1.0052 0.5898 0.4408 -0.0323 -0.0263 177 GLN B N +3764 C CA . GLN B 178 ? 1.3953 1.4041 0.9812 0.4435 -0.0309 -0.0251 177 GLN B CA +3765 C C . GLN B 178 ? 1.3584 1.3738 0.9505 0.4438 -0.0330 -0.0265 177 GLN B C +3766 O O . GLN B 178 ? 1.3295 1.3438 0.9272 0.4414 -0.0345 -0.0270 177 GLN B O +3767 C CB . GLN B 178 ? 1.1573 1.1623 0.7410 0.4428 -0.0288 -0.0229 177 GLN B CB +3768 C CG . GLN B 178 ? 1.5093 1.5198 1.0923 0.4451 -0.0275 -0.0217 177 GLN B CG +3769 C CD . GLN B 178 ? 1.3372 1.3513 0.9136 0.4489 -0.0253 -0.0207 177 GLN B CD +3770 O OE1 . GLN B 178 ? 1.4016 1.4118 0.9721 0.4496 -0.0232 -0.0195 177 GLN B OE1 +3771 N NE2 . GLN B 178 ? 1.4689 1.4907 1.0463 0.4515 -0.0257 -0.0212 177 GLN B NE2 +3772 N N . LEU B 179 ? 1.1503 1.1726 0.7413 0.4468 -0.0332 -0.0272 178 LEU B N +3773 C CA . LEU B 179 ? 1.1556 1.1848 0.7523 0.4473 -0.0352 -0.0285 178 LEU B CA +3774 C C . LEU B 179 ? 1.0923 1.1242 0.6899 0.4479 -0.0341 -0.0270 178 LEU B C +3775 O O . LEU B 179 ? 1.3766 1.4077 0.9691 0.4494 -0.0315 -0.0249 178 LEU B O +3776 C CB . LEU B 179 ? 1.2330 1.2690 0.8285 0.4503 -0.0357 -0.0298 178 LEU B CB +3777 C CG . LEU B 179 ? 1.5120 1.5467 1.1077 0.4499 -0.0373 -0.0317 178 LEU B CG +3778 C CD1 . LEU B 179 ? 1.6730 1.7148 1.2666 0.4532 -0.0374 -0.0327 178 LEU B CD1 +3779 C CD2 . LEU B 179 ? 1.1276 1.1611 0.7308 0.4468 -0.0404 -0.0339 178 LEU B CD2 +3780 N N . ALA B 180 ? 1.1675 1.2029 0.7717 0.4468 -0.0361 -0.0279 179 ALA B N +3781 C CA . ALA B 180 ? 1.3334 1.3721 0.9393 0.4474 -0.0354 -0.0266 179 ALA B CA +3782 C C . ALA B 180 ? 1.2906 1.3374 0.9018 0.4484 -0.0374 -0.0279 179 ALA B C +3783 O O . ALA B 180 ? 1.4148 1.4623 1.0325 0.4463 -0.0395 -0.0288 179 ALA B O +3784 C CB . ALA B 180 ? 1.4478 1.4807 1.0564 0.4442 -0.0354 -0.0256 179 ALA B CB +3785 N N . ASP B 181 ? 1.1576 1.2106 0.7659 0.4517 -0.0367 -0.0280 180 ASP B N +3786 C CA . ASP B 181 ? 1.5041 1.5653 1.1168 0.4530 -0.0386 -0.0294 180 ASP B CA +3787 C C . ASP B 181 ? 1.2922 1.3570 0.9092 0.4526 -0.0389 -0.0286 180 ASP B C +3788 O O . ASP B 181 ? 1.3571 1.4247 0.9712 0.4546 -0.0369 -0.0267 180 ASP B O +3789 C CB . ASP B 181 ? 1.5154 1.5819 1.1229 0.4567 -0.0372 -0.0293 180 ASP B CB +3790 C CG . ASP B 181 ? 1.5706 1.6445 1.1818 0.4580 -0.0394 -0.0315 180 ASP B CG +3791 O OD1 . ASP B 181 ? 1.6871 1.7627 1.3052 0.4561 -0.0420 -0.0330 180 ASP B OD1 +3792 O OD2 . ASP B 181 ? 1.8060 1.8842 1.4133 0.4609 -0.0385 -0.0316 180 ASP B OD2 +3793 N N . HIS B 182 ? 1.0685 1.1334 0.6926 0.4501 -0.0415 -0.0299 181 HIS B N +3794 C CA . HIS B 182 ? 1.3572 1.4248 0.9858 0.4494 -0.0419 -0.0290 181 HIS B CA +3795 C C . HIS B 182 ? 1.1211 1.1978 0.7537 0.4511 -0.0434 -0.0299 181 HIS B C +3796 O O . HIS B 182 ? 1.1048 1.1843 0.7421 0.4504 -0.0459 -0.0321 181 HIS B O +3797 C CB . HIS B 182 ? 1.2006 1.2633 0.8350 0.4456 -0.0438 -0.0297 181 HIS B CB +3798 C CG . HIS B 182 ? 1.0266 1.0809 0.6582 0.4436 -0.0422 -0.0282 181 HIS B CG +3799 N ND1 . HIS B 182 ? 1.3217 1.3704 0.9480 0.4435 -0.0409 -0.0280 181 HIS B ND1 +3800 C CD2 . HIS B 182 ? 1.0088 1.0593 0.6423 0.4415 -0.0418 -0.0268 181 HIS B CD2 +3801 C CE1 . HIS B 182 ? 1.2990 1.3409 0.9240 0.4415 -0.0397 -0.0266 181 HIS B CE1 +3802 N NE2 . HIS B 182 ? 1.0992 1.1420 0.7285 0.4403 -0.0403 -0.0259 181 HIS B NE2 +3803 N N . TYR B 183 ? 1.3926 1.4738 1.0238 0.4530 -0.0418 -0.0281 182 TYR B N +3804 C CA . TYR B 183 ? 1.3825 1.4726 1.0176 0.4546 -0.0430 -0.0287 182 TYR B CA +3805 C C . TYR B 183 ? 1.0961 1.1875 0.7359 0.4533 -0.0435 -0.0275 182 TYR B C +3806 O O . TYR B 183 ? 1.5675 1.6588 1.2045 0.4542 -0.0413 -0.0253 182 TYR B O +3807 C CB . TYR B 183 ? 1.1390 1.2346 0.7686 0.4584 -0.0409 -0.0277 182 TYR B CB +3808 C CG . TYR B 183 ? 1.2254 1.3215 0.8513 0.4601 -0.0408 -0.0291 182 TYR B CG +3809 C CD1 . TYR B 183 ? 1.4230 1.5130 1.0425 0.4604 -0.0389 -0.0284 182 TYR B CD1 +3810 C CD2 . TYR B 183 ? 1.1360 1.2386 0.7647 0.4612 -0.0428 -0.0312 182 TYR B CD2 +3811 C CE1 . TYR B 183 ? 1.3208 1.4112 0.9368 0.4618 -0.0389 -0.0297 182 TYR B CE1 +3812 C CE2 . TYR B 183 ? 1.4694 1.5725 1.0947 0.4627 -0.0428 -0.0325 182 TYR B CE2 +3813 C CZ . TYR B 183 ? 1.4581 1.5550 1.0770 0.4630 -0.0409 -0.0318 182 TYR B CZ +3814 O OH . TYR B 183 ? 1.4819 1.5793 1.0974 0.4645 -0.0409 -0.0330 182 TYR B OH +3815 N N . GLN B 184 ? 1.0295 1.1224 0.6766 0.4511 -0.0463 -0.0291 183 GLN B N +3816 C CA . GLN B 184 ? 1.4375 1.5304 1.0895 0.4493 -0.0470 -0.0280 183 GLN B CA +3817 C C . GLN B 184 ? 1.3280 1.4295 0.9856 0.4501 -0.0488 -0.0286 183 GLN B C +3818 O O . GLN B 184 ? 1.3996 1.5066 1.0590 0.4513 -0.0503 -0.0304 183 GLN B O +3819 C CB . GLN B 184 ? 1.3789 1.4649 1.0349 0.4456 -0.0487 -0.0290 183 GLN B CB +3820 C CG . GLN B 184 ? 1.4204 1.5059 1.0822 0.4433 -0.0498 -0.0282 183 GLN B CG +3821 C CD . GLN B 184 ? 1.5609 1.6407 1.2273 0.4398 -0.0519 -0.0297 183 GLN B CD +3822 O OE1 . GLN B 184 ? 1.1699 1.2436 0.8338 0.4387 -0.0516 -0.0304 183 GLN B OE1 +3823 N NE2 . GLN B 184 ? 1.0904 1.1722 0.7638 0.4380 -0.0541 -0.0303 183 GLN B NE2 +3824 N N . GLN B 185 ? 1.0627 1.1655 0.7232 0.4493 -0.0487 -0.0270 184 GLN B N +3825 C CA . GLN B 185 ? 1.2968 1.4070 0.9637 0.4494 -0.0507 -0.0276 184 GLN B CA +3826 C C . GLN B 185 ? 1.5729 1.6818 1.2446 0.4472 -0.0514 -0.0263 184 GLN B C +3827 O O . GLN B 185 ? 1.2898 1.3954 0.9587 0.4470 -0.0493 -0.0241 184 GLN B O +3828 C CB . GLN B 185 ? 1.6484 1.7668 1.3128 0.4529 -0.0495 -0.0268 184 GLN B CB +3829 C CG . GLN B 185 ? 2.0033 2.1212 1.6623 0.4546 -0.0463 -0.0240 184 GLN B CG +3830 C CD . GLN B 185 ? 2.3110 2.4375 1.9682 0.4580 -0.0453 -0.0234 184 GLN B CD +3831 O OE1 . GLN B 185 ? 2.3678 2.4994 2.0256 0.4594 -0.0465 -0.0251 184 GLN B OE1 +3832 N NE2 . GLN B 185 ? 2.3722 2.5003 2.0273 0.4592 -0.0432 -0.0210 184 GLN B NE2 +3833 N N . ASN B 186 ? 1.2662 1.3780 0.9452 0.4455 -0.0543 -0.0278 185 ASN B N +3834 C CA . ASN B 186 ? 1.4750 1.5858 1.1594 0.4431 -0.0553 -0.0269 185 ASN B CA +3835 C C . ASN B 186 ? 1.6083 1.7276 1.2980 0.4438 -0.0567 -0.0268 185 ASN B C +3836 O O . ASN B 186 ? 1.4011 1.5264 1.0935 0.4448 -0.0585 -0.0285 185 ASN B O +3837 C CB . ASN B 186 ? 1.4108 1.5157 1.0996 0.4398 -0.0575 -0.0287 185 ASN B CB +3838 C CG . ASN B 186 ? 1.4058 1.5017 1.0899 0.4386 -0.0560 -0.0283 185 ASN B CG +3839 O OD1 . ASN B 186 ? 1.4401 1.5336 1.1212 0.4390 -0.0559 -0.0297 185 ASN B OD1 +3840 N ND2 . ASN B 186 ? 1.1538 1.2445 0.8371 0.4371 -0.0546 -0.0264 185 ASN B ND2 +3841 N N . THR B 187 ? 1.3295 1.4489 1.0204 0.4433 -0.0560 -0.0246 186 THR B N +3842 C CA . THR B 187 ? 1.4095 1.5369 1.1044 0.4442 -0.0566 -0.0237 186 THR B CA +3843 C C . THR B 187 ? 1.4786 1.6038 1.1778 0.4419 -0.0571 -0.0223 186 THR B C +3844 O O . THR B 187 ? 1.6641 1.7840 1.3600 0.4414 -0.0551 -0.0204 186 THR B O +3845 C CB . THR B 187 ? 1.3459 1.4776 1.0351 0.4475 -0.0539 -0.0218 186 THR B CB +3846 O OG1 . THR B 187 ? 1.4562 1.5917 1.1424 0.4499 -0.0538 -0.0232 186 THR B OG1 +3847 C CG2 . THR B 187 ? 1.2395 1.3783 0.9325 0.4482 -0.0543 -0.0204 186 THR B CG2 +3848 N N . PRO B 188 ? 1.4930 1.6226 1.1995 0.4406 -0.0599 -0.0231 187 PRO B N +3849 C CA . PRO B 188 ? 1.5714 1.6995 1.2829 0.4382 -0.0607 -0.0220 187 PRO B CA +3850 C C . PRO B 188 ? 1.6065 1.7376 1.3166 0.4394 -0.0588 -0.0191 187 PRO B C +3851 O O . PRO B 188 ? 1.6523 1.7907 1.3621 0.4417 -0.0584 -0.0185 187 PRO B O +3852 C CB . PRO B 188 ? 1.4588 1.5923 1.1782 0.4371 -0.0642 -0.0239 187 PRO B CB +3853 C CG . PRO B 188 ? 1.4889 1.6295 1.2071 0.4397 -0.0645 -0.0251 187 PRO B CG +3854 C CD . PRO B 188 ? 1.2997 1.4361 1.0105 0.4412 -0.0624 -0.0254 187 PRO B CD +3855 N N . ILE B 189 ? 1.5930 1.7180 1.3023 0.4378 -0.0576 -0.0174 188 ILE B N +3856 C CA . ILE B 189 ? 1.6348 1.7617 1.3434 0.4385 -0.0559 -0.0147 188 ILE B CA +3857 C C . ILE B 189 ? 1.7938 1.9270 1.5096 0.4377 -0.0582 -0.0145 188 ILE B C +3858 O O . ILE B 189 ? 1.6472 1.7859 1.3629 0.4393 -0.0573 -0.0127 188 ILE B O +3859 C CB . ILE B 189 ? 1.5118 1.6302 1.2183 0.4366 -0.0545 -0.0133 188 ILE B CB +3860 C CG1 . ILE B 189 ? 1.4753 1.5874 1.1746 0.4373 -0.0523 -0.0135 188 ILE B CG1 +3861 C CG2 . ILE B 189 ? 1.4298 1.5498 1.1357 0.4371 -0.0528 -0.0105 188 ILE B CG2 +3862 C CD1 . ILE B 189 ? 1.5905 1.6935 1.2881 0.4350 -0.0513 -0.0127 188 ILE B CD1 +3863 N N . GLY B 190 ? 1.8974 2.0299 1.6194 0.4354 -0.0611 -0.0163 189 GLY B N +3864 C CA . GLY B 190 ? 1.9458 2.0838 1.6753 0.4342 -0.0635 -0.0163 189 GLY B CA +3865 C C . GLY B 190 ? 2.0712 2.2183 1.8032 0.4360 -0.0650 -0.0175 189 GLY B C +3866 O O . GLY B 190 ? 1.7525 1.9017 1.4810 0.4379 -0.0645 -0.0187 189 GLY B O +3867 N N . ASP B 191 ? 2.1082 2.2611 1.8465 0.4353 -0.0669 -0.0171 190 ASP B N +3868 C CA . ASP B 191 ? 2.2141 2.3763 1.9558 0.4367 -0.0686 -0.0181 190 ASP B CA +3869 C C . ASP B 191 ? 2.1005 2.2637 1.8490 0.4347 -0.0721 -0.0208 190 ASP B C +3870 O O . ASP B 191 ? 1.8533 2.0234 1.6046 0.4356 -0.0739 -0.0223 190 ASP B O +3871 C CB . ASP B 191 ? 2.1580 2.3268 1.9021 0.4375 -0.0683 -0.0158 190 ASP B CB +3872 C CG . ASP B 191 ? 2.3137 2.4844 2.0512 0.4404 -0.0651 -0.0137 190 ASP B CG +3873 O OD1 . ASP B 191 ? 2.0232 2.1976 1.7570 0.4428 -0.0643 -0.0144 190 ASP B OD1 +3874 O OD2 . ASP B 191 ? 2.4931 2.6619 2.2291 0.4402 -0.0633 -0.0112 190 ASP B OD2 +3875 N N . GLY B 192 ? 2.0852 2.2416 1.8363 0.4318 -0.0732 -0.0214 191 GLY B N +3876 C CA . GLY B 192 ? 2.0847 2.2410 1.8420 0.4297 -0.0764 -0.0240 191 GLY B CA +3877 C C . GLY B 192 ? 2.1925 2.3493 1.9481 0.4307 -0.0771 -0.0267 191 GLY B C +3878 O O . GLY B 192 ? 2.1150 2.2698 1.8639 0.4326 -0.0749 -0.0266 191 GLY B O +3879 N N . PRO B 193 ? 2.3026 2.4622 2.0642 0.4295 -0.0802 -0.0293 192 PRO B N +3880 C CA . PRO B 193 ? 2.3184 2.4791 2.0789 0.4303 -0.0812 -0.0320 192 PRO B CA +3881 C C . PRO B 193 ? 2.1579 2.3096 1.9155 0.4290 -0.0807 -0.0333 192 PRO B C +3882 O O . PRO B 193 ? 1.6849 1.8304 1.4449 0.4264 -0.0813 -0.0332 192 PRO B O +3883 C CB . PRO B 193 ? 2.1869 2.3533 1.9555 0.4291 -0.0848 -0.0342 192 PRO B CB +3884 C CG . PRO B 193 ? 1.9715 2.1355 1.7454 0.4264 -0.0859 -0.0331 192 PRO B CG +3885 C CD . PRO B 193 ? 2.0892 2.2512 1.8590 0.4272 -0.0830 -0.0297 192 PRO B CD +3886 N N . VAL B 194 ? 2.0041 2.1550 1.7564 0.4308 -0.0797 -0.0345 193 VAL B N +3887 C CA . VAL B 194 ? 1.8461 1.9888 1.5952 0.4297 -0.0791 -0.0356 193 VAL B CA +3888 C C . VAL B 194 ? 1.6994 1.8439 1.4503 0.4298 -0.0812 -0.0389 193 VAL B C +3889 O O . VAL B 194 ? 1.4960 1.6481 1.2507 0.4307 -0.0831 -0.0402 193 VAL B O +3890 C CB . VAL B 194 ? 1.9865 2.1252 1.7269 0.4316 -0.0756 -0.0339 193 VAL B CB +3891 C CG1 . VAL B 194 ? 1.4871 1.6242 1.2255 0.4317 -0.0734 -0.0307 193 VAL B CG1 +3892 C CG2 . VAL B 194 ? 1.8493 1.9939 1.5855 0.4348 -0.0747 -0.0343 193 VAL B CG2 +3893 N N . LEU B 195 ? 1.5634 1.7010 1.3117 0.4289 -0.0810 -0.0403 194 LEU B N +3894 C CA . LEU B 195 ? 1.3428 1.4814 1.0924 0.4289 -0.0829 -0.0434 194 LEU B CA +3895 C C . LEU B 195 ? 1.5067 1.6458 1.2491 0.4317 -0.0808 -0.0435 194 LEU B C +3896 O O . LEU B 195 ? 1.7759 1.9095 1.5121 0.4322 -0.0782 -0.0420 194 LEU B O +3897 C CB . LEU B 195 ? 1.2250 1.3558 0.9770 0.4260 -0.0841 -0.0450 194 LEU B CB +3898 C CG . LEU B 195 ? 1.5845 1.7141 1.3436 0.4231 -0.0861 -0.0449 194 LEU B CG +3899 C CD1 . LEU B 195 ? 1.5529 1.6744 1.3138 0.4202 -0.0871 -0.0464 194 LEU B CD1 +3900 C CD2 . LEU B 195 ? 1.1797 1.3177 0.9457 0.4231 -0.0889 -0.0462 194 LEU B CD2 +3901 N N . LEU B 196 ? 1.4768 1.6225 1.2199 0.4334 -0.0820 -0.0454 195 LEU B N +3902 C CA . LEU B 196 ? 1.6952 1.8419 1.4317 0.4361 -0.0802 -0.0456 195 LEU B CA +3903 C C . LEU B 196 ? 1.6551 1.7998 1.3919 0.4356 -0.0818 -0.0487 195 LEU B C +3904 O O . LEU B 196 ? 1.6631 1.8134 1.4040 0.4358 -0.0841 -0.0511 195 LEU B O +3905 C CB . LEU B 196 ? 1.9497 2.1056 1.6853 0.4389 -0.0797 -0.0449 195 LEU B CB +3906 C CG . LEU B 196 ? 1.6537 1.8118 1.3895 0.4393 -0.0783 -0.0418 195 LEU B CG +3907 C CD1 . LEU B 196 ? 1.5127 1.6804 1.2484 0.4419 -0.0781 -0.0412 195 LEU B CD1 +3908 C CD2 . LEU B 196 ? 1.6085 1.7598 1.3378 0.4396 -0.0751 -0.0393 195 LEU B CD2 +3909 N N . PRO B 197 ? 1.5580 1.6947 1.2904 0.4349 -0.0804 -0.0488 196 PRO B N +3910 C CA . PRO B 197 ? 1.5048 1.6374 1.2376 0.4338 -0.0818 -0.0515 196 PRO B CA +3911 C C . PRO B 197 ? 1.5156 1.6525 1.2458 0.4360 -0.0821 -0.0535 196 PRO B C +3912 O O . PRO B 197 ? 1.5730 1.7137 1.2983 0.4388 -0.0802 -0.0524 196 PRO B O +3913 C CB . PRO B 197 ? 1.4155 1.5387 1.1429 0.4328 -0.0795 -0.0501 196 PRO B CB +3914 C CG . PRO B 197 ? 1.4004 1.5245 1.1221 0.4349 -0.0765 -0.0470 196 PRO B CG +3915 C CD . PRO B 197 ? 1.3170 1.4479 1.0432 0.4353 -0.0773 -0.0460 196 PRO B CD +3916 N N . ASP B 198 ? 1.5900 1.7262 1.3236 0.4348 -0.0844 -0.0565 197 ASP B N +3917 C CA . ASP B 198 ? 1.7415 1.8795 1.4721 0.4366 -0.0846 -0.0585 197 ASP B CA +3918 C C . ASP B 198 ? 1.4824 1.6124 1.2060 0.4367 -0.0822 -0.0576 197 ASP B C +3919 O O . ASP B 198 ? 1.4768 1.5997 1.1997 0.4348 -0.0813 -0.0562 197 ASP B O +3920 C CB . ASP B 198 ? 1.8220 1.9609 1.5585 0.4349 -0.0879 -0.0620 197 ASP B CB +3921 C CG . ASP B 198 ? 1.9577 2.1056 1.7004 0.4354 -0.0903 -0.0633 197 ASP B CG +3922 O OD1 . ASP B 198 ? 1.9744 2.1287 1.7158 0.4375 -0.0893 -0.0618 197 ASP B OD1 +3923 O OD2 . ASP B 198 ? 1.7613 1.9100 1.5102 0.4335 -0.0931 -0.0658 197 ASP B OD2 +3924 N N . ASN B 199 ? 1.3756 1.5069 1.0943 0.4389 -0.0813 -0.0584 198 ASN B N +3925 C CA . ASN B 199 ? 1.6252 1.7492 1.3375 0.4390 -0.0793 -0.0578 198 ASN B CA +3926 C C . ASN B 199 ? 1.5827 1.6986 1.2973 0.4357 -0.0803 -0.0589 198 ASN B C +3927 O O . ASN B 199 ? 1.4981 1.6145 1.2174 0.4344 -0.0829 -0.0616 198 ASN B O +3928 C CB . ASN B 199 ? 1.8385 1.9652 1.5467 0.4413 -0.0790 -0.0594 198 ASN B CB +3929 C CG . ASN B 199 ? 1.8358 1.9697 1.5403 0.4447 -0.0775 -0.0582 198 ASN B CG +3930 O OD1 . ASN B 199 ? 1.3394 1.4770 1.0449 0.4453 -0.0769 -0.0563 198 ASN B OD1 +3931 N ND2 . ASN B 199 ? 1.7726 1.9087 1.4730 0.4469 -0.0770 -0.0593 198 ASN B ND2 +3932 N N . HIS B 200 ? 1.5387 1.6473 1.2503 0.4345 -0.0784 -0.0567 199 HIS B N +3933 C CA . HIS B 200 ? 1.4636 1.5637 1.1758 0.4317 -0.0788 -0.0574 199 HIS B CA +3934 C C . HIS B 200 ? 1.2924 1.3857 0.9977 0.4318 -0.0758 -0.0550 199 HIS B C +3935 O O . HIS B 200 ? 1.2539 1.3492 0.9535 0.4344 -0.0735 -0.0532 199 HIS B O +3936 C CB . HIS B 200 ? 1.2870 1.3851 1.0062 0.4286 -0.0807 -0.0577 199 HIS B CB +3937 C CG . HIS B 200 ? 1.2443 1.3417 0.9634 0.4283 -0.0792 -0.0548 199 HIS B CG +3938 N ND1 . HIS B 200 ? 1.3548 1.4592 1.0759 0.4297 -0.0793 -0.0538 199 HIS B ND1 +3939 C CD2 . HIS B 200 ? 1.3971 1.4876 1.1145 0.4266 -0.0777 -0.0528 199 HIS B CD2 +3940 C CE1 . HIS B 200 ? 1.4130 1.5149 1.1335 0.4289 -0.0779 -0.0512 199 HIS B CE1 +3941 N NE2 . HIS B 200 ? 1.4834 1.5769 1.2017 0.4271 -0.0768 -0.0505 199 HIS B NE2 +3942 N N . TYR B 201 ? 1.2775 1.3628 0.9833 0.4291 -0.0758 -0.0549 200 TYR B N +3943 C CA . TYR B 201 ? 1.3218 1.4003 1.0211 0.4290 -0.0729 -0.0527 200 TYR B CA +3944 C C . TYR B 201 ? 1.2035 1.2741 0.9049 0.4257 -0.0729 -0.0519 200 TYR B C +3945 O O . TYR B 201 ? 1.2587 1.3279 0.9661 0.4232 -0.0752 -0.0536 200 TYR B O +3946 C CB . TYR B 201 ? 1.2956 1.3721 0.9895 0.4303 -0.0721 -0.0535 200 TYR B CB +3947 C CG . TYR B 201 ? 1.3156 1.3875 1.0120 0.4281 -0.0739 -0.0560 200 TYR B CG +3948 C CD1 . TYR B 201 ? 1.3390 1.4149 1.0404 0.4278 -0.0766 -0.0589 200 TYR B CD1 +3949 C CD2 . TYR B 201 ? 1.4038 1.4673 1.0973 0.4263 -0.0727 -0.0553 200 TYR B CD2 +3950 C CE1 . TYR B 201 ? 1.2914 1.3631 0.9951 0.4258 -0.0782 -0.0612 200 TYR B CE1 +3951 C CE2 . TYR B 201 ? 1.5969 1.6561 1.2927 0.4242 -0.0743 -0.0574 200 TYR B CE2 +3952 C CZ . TYR B 201 ? 1.3827 1.4461 1.0836 0.4240 -0.0770 -0.0604 200 TYR B CZ +3953 O OH . TYR B 201 ? 1.1969 1.2561 0.9001 0.4219 -0.0786 -0.0626 200 TYR B OH +3954 N N . LEU B 202 ? 1.3417 1.4075 1.0383 0.4256 -0.0704 -0.0493 201 LEU B N +3955 C CA . LEU B 202 ? 1.3788 1.4368 1.0768 0.4225 -0.0701 -0.0485 201 LEU B CA +3956 C C . LEU B 202 ? 1.1919 1.2428 0.8852 0.4217 -0.0690 -0.0486 201 LEU B C +3957 O O . LEU B 202 ? 1.1430 1.1933 0.8298 0.4237 -0.0668 -0.0474 201 LEU B O +3958 C CB . LEU B 202 ? 1.0210 1.0781 0.7176 0.4224 -0.0683 -0.0456 201 LEU B CB +3959 C CG . LEU B 202 ? 1.1986 1.2626 0.8988 0.4235 -0.0688 -0.0448 201 LEU B CG +3960 C CD1 . LEU B 202 ? 1.2000 1.2610 0.8994 0.4226 -0.0672 -0.0420 201 LEU B CD1 +3961 C CD2 . LEU B 202 ? 1.4718 1.5396 1.1801 0.4220 -0.0721 -0.0470 201 LEU B CD2 +3962 N N . SER B 203 ? 1.1038 1.1496 0.8008 0.4187 -0.0705 -0.0501 202 SER B N +3963 C CA . SER B 203 ? 1.1708 1.2097 0.8641 0.4176 -0.0696 -0.0503 202 SER B CA +3964 C C . SER B 203 ? 1.0536 1.0857 0.7453 0.4156 -0.0679 -0.0480 202 SER B C +3965 O O . SER B 203 ? 1.3782 1.4073 1.0749 0.4129 -0.0691 -0.0483 202 SER B O +3966 C CB . SER B 203 ? 1.0432 1.0801 0.7414 0.4154 -0.0722 -0.0532 202 SER B CB +3967 O OG . SER B 203 ? 1.4108 1.4414 1.1054 0.4144 -0.0714 -0.0534 202 SER B OG +3968 N N . THR B 204 ? 1.1262 1.1559 0.8110 0.4170 -0.0652 -0.0459 203 THR B N +3969 C CA . THR B 204 ? 1.2854 1.3091 0.9681 0.4155 -0.0633 -0.0436 203 THR B CA +3970 C C . THR B 204 ? 1.2756 1.2916 0.9551 0.4138 -0.0624 -0.0436 203 THR B C +3971 O O . THR B 204 ? 1.3441 1.3599 1.0196 0.4152 -0.0619 -0.0442 203 THR B O +3972 C CB . THR B 204 ? 1.1815 1.2074 0.8586 0.4180 -0.0606 -0.0410 203 THR B CB +3973 O OG1 . THR B 204 ? 1.1335 1.1669 0.8133 0.4198 -0.0613 -0.0409 203 THR B OG1 +3974 C CG2 . THR B 204 ? 1.7864 1.8064 1.4622 0.4162 -0.0589 -0.0387 203 THR B CG2 +3975 N N . GLN B 205 ? 1.0956 1.1053 0.7769 0.4108 -0.0623 -0.0429 204 GLN B N +3976 C CA . GLN B 205 ? 1.1022 1.1043 0.7801 0.4091 -0.0610 -0.0423 204 GLN B CA +3977 C C . GLN B 205 ? 1.1976 1.1951 0.8742 0.4076 -0.0593 -0.0399 204 GLN B C +3978 O O . GLN B 205 ? 1.0443 1.0427 0.7253 0.4064 -0.0601 -0.0395 204 GLN B O +3979 C CB . GLN B 205 ? 1.2487 1.2469 0.9312 0.4062 -0.0632 -0.0446 204 GLN B CB +3980 C CG . GLN B 205 ? 1.0428 1.0457 0.7284 0.4071 -0.0655 -0.0473 204 GLN B CG +3981 C CD . GLN B 205 ? 1.3606 1.3627 1.0539 0.4042 -0.0682 -0.0493 204 GLN B CD +3982 O OE1 . GLN B 205 ? 1.9848 1.9815 1.6798 0.4017 -0.0689 -0.0504 204 GLN B OE1 +3983 N NE2 . GLN B 205 ? 1.3689 1.3761 1.0671 0.4045 -0.0697 -0.0499 204 GLN B NE2 +3984 N N . SER B 206 ? 1.2283 1.2210 0.8990 0.4077 -0.0570 -0.0384 205 SER B N +3985 C CA . SER B 206 ? 1.0173 1.0063 0.6852 0.4071 -0.0549 -0.0359 205 SER B CA +3986 C C . SER B 206 ? 0.8608 0.8420 0.5249 0.4053 -0.0534 -0.0350 205 SER B C +3987 O O . SER B 206 ? 1.1505 1.1300 0.8116 0.4058 -0.0531 -0.0358 205 SER B O +3988 C CB . SER B 206 ? 1.0007 0.9945 0.6639 0.4105 -0.0529 -0.0340 205 SER B CB +3989 O OG . SER B 206 ? 1.3034 1.3041 0.9707 0.4117 -0.0542 -0.0345 205 SER B OG +3990 N N . ASN B 207 ? 1.0863 1.0629 0.7507 0.4033 -0.0525 -0.0335 206 ASN B N +3991 C CA . ASN B 207 ? 1.1097 1.0792 0.7704 0.4016 -0.0509 -0.0325 206 ASN B CA +3992 C C . ASN B 207 ? 1.1802 1.1478 0.8377 0.4019 -0.0486 -0.0299 206 ASN B C +3993 O O . ASN B 207 ? 1.0532 1.0227 0.7140 0.4014 -0.0490 -0.0293 206 ASN B O +3994 C CB . ASN B 207 ? 1.0029 0.9669 0.6684 0.3979 -0.0526 -0.0339 206 ASN B CB +3995 C CG . ASN B 207 ? 0.9342 0.8910 0.5982 0.3954 -0.0512 -0.0324 206 ASN B CG +3996 O OD1 . ASN B 207 ? 0.9906 0.9466 0.6560 0.3944 -0.0507 -0.0311 206 ASN B OD1 +3997 N ND2 . ASN B 207 ? 1.0836 1.0354 0.7452 0.3941 -0.0506 -0.0326 206 ASN B ND2 +3998 N N . LEU B 208 ? 1.0838 1.0481 0.7349 0.4027 -0.0463 -0.0285 207 LEU B N +3999 C CA . LEU B 208 ? 0.8744 0.8368 0.5216 0.4031 -0.0440 -0.0261 207 LEU B CA +4000 C C . LEU B 208 ? 0.7794 0.7340 0.4260 0.4000 -0.0432 -0.0254 207 LEU B C +4001 O O . LEU B 208 ? 1.0313 0.9820 0.6760 0.3991 -0.0431 -0.0260 207 LEU B O +4002 C CB . LEU B 208 ? 0.9417 0.9066 0.5817 0.4066 -0.0416 -0.0248 207 LEU B CB +4003 C CG . LEU B 208 ? 0.9372 0.9094 0.5765 0.4099 -0.0421 -0.0256 207 LEU B CG +4004 C CD1 . LEU B 208 ? 1.1215 1.0948 0.7533 0.4129 -0.0397 -0.0243 207 LEU B CD1 +4005 C CD2 . LEU B 208 ? 1.0467 1.0246 0.6899 0.4107 -0.0430 -0.0255 207 LEU B CD2 +4006 N N . SER B 209 ? 0.9944 0.9468 0.6426 0.3985 -0.0427 -0.0242 208 SER B N +4007 C CA . SER B 209 ? 0.9134 0.8587 0.5612 0.3955 -0.0420 -0.0235 208 SER B CA +4008 C C . SER B 209 ? 1.1239 1.0675 0.7694 0.3955 -0.0401 -0.0213 208 SER B C +4009 O O . SER B 209 ? 0.9743 0.9224 0.6191 0.3976 -0.0394 -0.0202 208 SER B O +4010 C CB . SER B 209 ? 0.9834 0.9261 0.6383 0.3921 -0.0444 -0.0250 208 SER B CB +4011 O OG . SER B 209 ? 1.3071 1.2540 0.9670 0.3920 -0.0457 -0.0252 208 SER B OG +4012 N N . LYS B 210 ? 1.1763 1.1135 0.8210 0.3929 -0.0393 -0.0206 209 LYS B N +4013 C CA . LYS B 210 ? 0.9240 0.8586 0.5672 0.3922 -0.0377 -0.0187 209 LYS B CA +4014 C C . LYS B 210 ? 0.9921 0.9235 0.6414 0.3886 -0.0391 -0.0190 209 LYS B C +4015 O O . LYS B 210 ? 1.2830 1.2125 0.9368 0.3863 -0.0410 -0.0207 209 LYS B O +4016 C CB . LYS B 210 ? 1.2673 1.1969 0.9043 0.3922 -0.0354 -0.0175 209 LYS B CB +4017 C CG . LYS B 210 ? 1.1366 1.0686 0.7671 0.3955 -0.0338 -0.0170 209 LYS B CG +4018 C CD . LYS B 210 ? 1.0260 0.9632 0.6537 0.3987 -0.0324 -0.0157 209 LYS B CD +4019 C CE . LYS B 210 ? 1.0298 0.9684 0.6503 0.4019 -0.0303 -0.0149 209 LYS B CE +4020 N NZ . LYS B 210 ? 1.0727 1.0176 0.6914 0.4052 -0.0295 -0.0141 209 LYS B NZ +4021 N N . ASP B 211 ? 1.1865 1.1175 0.8358 0.3883 -0.0381 -0.0175 210 ASP B N +4022 C CA . ASP B 211 ? 1.0146 0.9420 0.6684 0.3851 -0.0389 -0.0173 210 ASP B CA +4023 C C . ASP B 211 ? 1.3021 1.2234 0.9518 0.3837 -0.0370 -0.0160 210 ASP B C +4024 O O . ASP B 211 ? 1.3339 1.2554 0.9781 0.3857 -0.0347 -0.0144 210 ASP B O +4025 C CB . ASP B 211 ? 1.0552 0.9868 0.7110 0.3862 -0.0388 -0.0162 210 ASP B CB +4026 C CG . ASP B 211 ? 1.4425 1.3706 1.1020 0.3833 -0.0391 -0.0156 210 ASP B CG +4027 O OD1 . ASP B 211 ? 1.4618 1.3842 1.1224 0.3803 -0.0394 -0.0159 210 ASP B OD1 +4028 O OD2 . ASP B 211 ? 1.1016 1.0328 0.7628 0.3839 -0.0391 -0.0147 210 ASP B OD2 +4029 N N . PRO B 212 ? 1.6365 1.5524 1.2890 0.3804 -0.0378 -0.0166 211 PRO B N +4030 C CA . PRO B 212 ? 1.4751 1.3853 1.1233 0.3792 -0.0359 -0.0155 211 PRO B CA +4031 C C . PRO B 212 ? 1.4103 1.3184 1.0582 0.3782 -0.0347 -0.0138 211 PRO B C +4032 O O . PRO B 212 ? 1.2702 1.1737 0.9136 0.3778 -0.0331 -0.0128 211 PRO B O +4033 C CB . PRO B 212 ? 1.2822 1.1878 0.9338 0.3760 -0.0374 -0.0170 211 PRO B CB +4034 C CG . PRO B 212 ? 1.5195 1.4273 1.1784 0.3745 -0.0399 -0.0184 211 PRO B CG +4035 C CD . PRO B 212 ? 1.2567 1.1714 0.9158 0.3776 -0.0403 -0.0185 211 PRO B CD +4036 N N . ASN B 213 ? 1.7473 1.6586 1.3988 0.3783 -0.0354 -0.0135 212 ASN B N +4037 C CA . ASN B 213 ? 1.8080 1.7181 1.4588 0.3779 -0.0341 -0.0118 212 ASN B CA +4038 C C . ASN B 213 ? 1.5662 1.4812 1.2132 0.3814 -0.0326 -0.0104 212 ASN B C +4039 O O . ASN B 213 ? 1.5108 1.4266 1.1584 0.3814 -0.0319 -0.0091 212 ASN B O +4040 C CB . ASN B 213 ? 1.5578 1.4675 1.2154 0.3753 -0.0358 -0.0121 212 ASN B CB +4041 C CG . ASN B 213 ? 1.4785 1.3846 1.1409 0.3720 -0.0378 -0.0138 212 ASN B CG +4042 O OD1 . ASN B 213 ? 1.4597 1.3611 1.1193 0.3711 -0.0374 -0.0142 212 ASN B OD1 +4043 N ND2 . ASN B 213 ? 1.4048 1.3132 1.0736 0.3709 -0.0400 -0.0149 212 ASN B ND2 +4044 N N . GLU B 214 ? 1.5069 1.4255 1.1505 0.3843 -0.0321 -0.0107 213 GLU B N +4045 C CA . GLU B 214 ? 1.1355 1.0588 0.7752 0.3877 -0.0305 -0.0094 213 GLU B CA +4046 C C . GLU B 214 ? 1.3010 1.2223 0.9333 0.3894 -0.0280 -0.0084 213 GLU B C +4047 O O . GLU B 214 ? 1.3884 1.3078 1.0184 0.3895 -0.0280 -0.0092 213 GLU B O +4048 C CB . GLU B 214 ? 1.1325 1.0623 0.7740 0.3901 -0.0318 -0.0104 213 GLU B CB +4049 C CG . GLU B 214 ? 1.1674 1.1023 0.8052 0.3935 -0.0301 -0.0091 213 GLU B CG +4050 C CD . GLU B 214 ? 1.5542 1.4892 1.1929 0.3931 -0.0293 -0.0076 213 GLU B CD +4051 O OE1 . GLU B 214 ? 1.7276 1.6590 1.3622 0.3930 -0.0273 -0.0062 213 GLU B OE1 +4052 O OE2 . GLU B 214 ? 1.2652 1.2038 0.9088 0.3930 -0.0307 -0.0077 213 GLU B OE2 +4053 N N . LYS B 215 ? 1.3265 1.2480 0.9550 0.3908 -0.0259 -0.0066 214 LYS B N +4054 C CA . LYS B 215 ? 1.3935 1.3127 1.0148 0.3924 -0.0235 -0.0055 214 LYS B CA +4055 C C . LYS B 215 ? 1.2973 1.2220 0.9142 0.3964 -0.0219 -0.0047 214 LYS B C +4056 O O . LYS B 215 ? 1.4631 1.3871 1.0741 0.3982 -0.0201 -0.0041 214 LYS B O +4057 C CB . LYS B 215 ? 1.2863 1.2003 0.9035 0.3921 -0.0219 -0.0044 214 LYS B CB +4058 C CG . LYS B 215 ? 1.7950 1.7033 1.4151 0.3888 -0.0233 -0.0052 214 LYS B CG +4059 C CD . LYS B 215 ? 2.0136 1.9162 1.6280 0.3889 -0.0215 -0.0041 214 LYS B CD +4060 C CE . LYS B 215 ? 1.9784 1.8818 1.5934 0.3892 -0.0209 -0.0029 214 LYS B CE +4061 N NZ . LYS B 215 ? 1.7193 1.6200 1.3400 0.3860 -0.0227 -0.0035 214 LYS B NZ +4062 N N . ARG B 216 ? 1.0726 1.0028 0.6925 0.3977 -0.0227 -0.0047 215 ARG B N +4063 C CA . ARG B 216 ? 0.9192 0.8554 0.5359 0.4015 -0.0216 -0.0041 215 ARG B CA +4064 C C . ARG B 216 ? 1.1791 1.1186 0.7956 0.4031 -0.0227 -0.0055 215 ARG B C +4065 O O . ARG B 216 ? 1.2634 1.2013 0.8834 0.4012 -0.0246 -0.0071 215 ARG B O +4066 C CB . ARG B 216 ? 0.9971 0.9382 0.6179 0.4021 -0.0223 -0.0036 215 ARG B CB +4067 C CG . ARG B 216 ? 1.2021 1.1413 0.8226 0.4013 -0.0210 -0.0020 215 ARG B CG +4068 C CD . ARG B 216 ? 1.1812 1.1248 0.8069 0.4013 -0.0222 -0.0018 215 ARG B CD +4069 N NE . ARG B 216 ? 1.5920 1.5337 1.2245 0.3980 -0.0248 -0.0030 215 ARG B NE +4070 C CZ . ARG B 216 ? 1.6170 1.5619 1.2553 0.3973 -0.0264 -0.0031 215 ARG B CZ +4071 N NH1 . ARG B 216 ? 1.4835 1.4337 1.1218 0.3996 -0.0258 -0.0021 215 ARG B NH1 +4072 N NH2 . ARG B 216 ? 1.1416 1.0842 0.7857 0.3943 -0.0286 -0.0043 215 ARG B NH2 +4073 N N . ASP B 217 ? 1.0253 0.9694 0.6376 0.4066 -0.0214 -0.0050 216 ASP B N +4074 C CA . ASP B 217 ? 1.1705 1.1178 0.7822 0.4083 -0.0222 -0.0063 216 ASP B CA +4075 C C . ASP B 217 ? 1.3577 1.3099 0.9756 0.4082 -0.0248 -0.0077 216 ASP B C +4076 O O . ASP B 217 ? 1.1782 1.1357 0.7978 0.4098 -0.0248 -0.0072 216 ASP B O +4077 C CB . ASP B 217 ? 1.2109 1.1613 0.8159 0.4121 -0.0200 -0.0054 216 ASP B CB +4078 C CG . ASP B 217 ? 1.5189 1.4696 1.1213 0.4132 -0.0202 -0.0066 216 ASP B CG +4079 O OD1 . ASP B 217 ? 1.5319 1.4790 1.1366 0.4109 -0.0218 -0.0079 216 ASP B OD1 +4080 O OD2 . ASP B 217 ? 1.2251 1.1794 0.8229 0.4164 -0.0189 -0.0061 216 ASP B OD2 +4081 N N . HIS B 218 ? 1.2800 1.2307 0.9016 0.4063 -0.0269 -0.0095 217 HIS B N +4082 C CA . HIS B 218 ? 1.0767 1.0309 0.7050 0.4054 -0.0295 -0.0109 217 HIS B CA +4083 C C . HIS B 218 ? 1.0370 0.9923 0.6670 0.4054 -0.0313 -0.0130 217 HIS B C +4084 O O . HIS B 218 ? 1.1604 1.1123 0.7873 0.4051 -0.0309 -0.0134 217 HIS B O +4085 C CB . HIS B 218 ? 0.9841 0.9344 0.6179 0.4018 -0.0308 -0.0111 217 HIS B CB +4086 C CG . HIS B 218 ? 0.9262 0.8703 0.5611 0.3988 -0.0317 -0.0121 217 HIS B CG +4087 N ND1 . HIS B 218 ? 1.4634 1.4021 1.0935 0.3982 -0.0300 -0.0114 217 HIS B ND1 +4088 C CD2 . HIS B 218 ? 1.3164 1.2589 0.9569 0.3962 -0.0341 -0.0138 217 HIS B CD2 +4089 C CE1 . HIS B 218 ? 1.1058 1.0399 0.7384 0.3954 -0.0313 -0.0126 217 HIS B CE1 +4090 N NE2 . HIS B 218 ? 1.2306 1.1669 0.8695 0.3941 -0.0337 -0.0141 217 HIS B NE2 +4091 N N . MET B 219 ? 1.1250 1.0853 0.7601 0.4057 -0.0334 -0.0142 218 MET B N +4092 C CA . MET B 219 ? 1.0051 0.9665 0.6432 0.4053 -0.0356 -0.0163 218 MET B CA +4093 C C . MET B 219 ? 1.2033 1.1659 0.8493 0.4030 -0.0383 -0.0176 218 MET B C +4094 O O . MET B 219 ? 1.1790 1.1457 0.8279 0.4036 -0.0387 -0.0171 218 MET B O +4095 C CB . MET B 219 ? 0.8333 0.8010 0.4687 0.4088 -0.0353 -0.0167 218 MET B CB +4096 C CG . MET B 219 ? 0.7228 0.6925 0.3613 0.4087 -0.0376 -0.0190 218 MET B CG +4097 S SD . MET B 219 ? 1.1516 1.1295 0.7877 0.4129 -0.0375 -0.0195 218 MET B SD +4098 C CE . MET B 219 ? 0.9896 0.9742 0.6303 0.4138 -0.0383 -0.0191 218 MET B CE +4099 N N . VAL B 220 ? 1.0520 1.0108 0.7013 0.4003 -0.0400 -0.0192 219 VAL B N +4100 C CA . VAL B 220 ? 1.1187 1.0790 0.7756 0.3984 -0.0428 -0.0208 219 VAL B CA +4101 C C . VAL B 220 ? 0.8966 0.8615 0.5550 0.3999 -0.0444 -0.0228 219 VAL B C +4102 O O . VAL B 220 ? 1.0999 1.0626 0.7564 0.3997 -0.0446 -0.0239 219 VAL B O +4103 C CB . VAL B 220 ? 1.0842 1.0378 0.7445 0.3944 -0.0439 -0.0216 219 VAL B CB +4104 C CG1 . VAL B 220 ? 0.9774 0.9324 0.6454 0.3924 -0.0463 -0.0228 219 VAL B CG1 +4105 C CG2 . VAL B 220 ? 1.1077 1.0558 0.7651 0.3930 -0.0419 -0.0198 219 VAL B CG2 +4106 N N . LEU B 221 ? 1.0971 1.0684 0.7588 0.4013 -0.0456 -0.0232 220 LEU B N +4107 C CA . LEU B 221 ? 0.9627 0.9394 0.6259 0.4031 -0.0472 -0.0250 220 LEU B CA +4108 C C . LEU B 221 ? 1.1395 1.1175 0.8105 0.4011 -0.0502 -0.0270 220 LEU B C +4109 O O . LEU B 221 ? 1.3020 1.2817 0.9775 0.4001 -0.0512 -0.0268 220 LEU B O +4110 C CB . LEU B 221 ? 0.8942 0.8781 0.5553 0.4067 -0.0463 -0.0241 220 LEU B CB +4111 C CG . LEU B 221 ? 1.0542 1.0447 0.7174 0.4087 -0.0480 -0.0258 220 LEU B CG +4112 C CD1 . LEU B 221 ? 0.9050 0.8947 0.5643 0.4098 -0.0477 -0.0269 220 LEU B CD1 +4113 C CD2 . LEU B 221 ? 1.0051 1.0030 0.6674 0.4117 -0.0473 -0.0249 220 LEU B CD2 +4114 N N . LEU B 222 ? 1.6917 1.6689 1.3640 0.4004 -0.0517 -0.0291 221 LEU B N +4115 C CA . LEU B 222 ? 1.0956 1.0747 0.7749 0.3989 -0.0546 -0.0313 221 LEU B CA +4116 C C . LEU B 222 ? 1.2290 1.2143 0.9086 0.4014 -0.0558 -0.0330 221 LEU B C +4117 O O . LEU B 222 ? 1.1357 1.1202 0.8118 0.4023 -0.0554 -0.0338 221 LEU B O +4118 C CB . LEU B 222 ? 1.0756 1.0483 0.7574 0.3956 -0.0557 -0.0326 221 LEU B CB +4119 C CG . LEU B 222 ? 1.2071 1.1736 0.8903 0.3925 -0.0551 -0.0314 221 LEU B CG +4120 C CD1 . LEU B 222 ? 0.8379 0.7984 0.5229 0.3895 -0.0560 -0.0327 221 LEU B CD1 +4121 C CD2 . LEU B 222 ? 1.0794 1.0484 0.7685 0.3915 -0.0565 -0.0313 221 LEU B CD2 +4122 N N . GLU B 223 ? 1.0429 1.0343 0.7267 0.4023 -0.0572 -0.0335 222 GLU B N +4123 C CA . GLU B 223 ? 1.2396 1.2376 0.9244 0.4046 -0.0585 -0.0351 222 GLU B CA +4124 C C . GLU B 223 ? 1.0956 1.0954 0.7878 0.4029 -0.0616 -0.0375 222 GLU B C +4125 O O . GLU B 223 ? 1.2581 1.2577 0.9557 0.4010 -0.0629 -0.0375 222 GLU B O +4126 C CB . GLU B 223 ? 1.0812 1.0860 0.7648 0.4075 -0.0577 -0.0338 222 GLU B CB +4127 C CG . GLU B 223 ? 1.7516 1.7581 1.4278 0.4106 -0.0552 -0.0325 222 GLU B CG +4128 C CD . GLU B 223 ? 2.1846 2.1986 1.8602 0.4136 -0.0547 -0.0315 222 GLU B CD +4129 O OE1 . GLU B 223 ? 2.1537 2.1731 1.8346 0.4138 -0.0567 -0.0327 222 GLU B OE1 +4130 O OE2 . GLU B 223 ? 2.1484 2.1630 1.8181 0.4158 -0.0522 -0.0297 222 GLU B OE2 +4131 N N . PHE B 224 ? 1.1797 1.1815 0.8722 0.4037 -0.0629 -0.0396 223 PHE B N +4132 C CA . PHE B 224 ? 1.0349 1.0400 0.7339 0.4029 -0.0658 -0.0421 223 PHE B CA +4133 C C . PHE B 224 ? 0.8526 0.8660 0.5510 0.4062 -0.0662 -0.0427 223 PHE B C +4134 O O . PHE B 224 ? 1.3950 1.4098 1.0878 0.4087 -0.0648 -0.0424 223 PHE B O +4135 C CB . PHE B 224 ? 1.1038 1.1048 0.8043 0.4010 -0.0671 -0.0443 223 PHE B CB +4136 C CG . PHE B 224 ? 1.2241 1.2169 0.9244 0.3979 -0.0665 -0.0436 223 PHE B CG +4137 C CD1 . PHE B 224 ? 1.0691 1.0587 0.7707 0.3962 -0.0657 -0.0419 223 PHE B CD1 +4138 C CD2 . PHE B 224 ? 0.8940 0.8821 0.5929 0.3967 -0.0666 -0.0448 223 PHE B CD2 +4139 C CE1 . PHE B 224 ? 0.9136 0.8958 0.6150 0.3933 -0.0651 -0.0413 223 PHE B CE1 +4140 C CE2 . PHE B 224 ? 1.1876 1.1683 0.8864 0.3938 -0.0660 -0.0443 223 PHE B CE2 +4141 C CZ . PHE B 224 ? 1.2560 1.2337 0.9560 0.3921 -0.0653 -0.0425 223 PHE B CZ +4142 N N . VAL B 225 ? 1.2059 1.2247 0.9097 0.4064 -0.0681 -0.0435 224 VAL B N +4143 C CA . VAL B 225 ? 1.2086 1.2357 0.9123 0.4095 -0.0686 -0.0442 224 VAL B CA +4144 C C . VAL B 225 ? 1.3671 1.3986 1.0781 0.4087 -0.0717 -0.0467 224 VAL B C +4145 O O . VAL B 225 ? 1.1427 1.1748 0.8591 0.4071 -0.0731 -0.0467 224 VAL B O +4146 C CB . VAL B 225 ? 1.1652 1.1967 0.8671 0.4115 -0.0671 -0.0419 224 VAL B CB +4147 C CG1 . VAL B 225 ? 1.0547 1.0937 0.7543 0.4150 -0.0669 -0.0423 224 VAL B CG1 +4148 C CG2 . VAL B 225 ? 1.1541 1.1806 0.8503 0.4115 -0.0642 -0.0392 224 VAL B CG2 +4149 N N . THR B 226 ? 1.2174 1.2520 0.9283 0.4100 -0.0729 -0.0489 225 THR B N +4150 C CA . THR B 226 ? 1.2236 1.2629 0.9412 0.4095 -0.0760 -0.0515 225 THR B CA +4151 C C . THR B 226 ? 1.1061 1.1538 0.8229 0.4127 -0.0765 -0.0525 225 THR B C +4152 O O . THR B 226 ? 1.1995 1.2477 0.9114 0.4146 -0.0756 -0.0529 225 THR B O +4153 C CB . THR B 226 ? 1.1854 1.2204 0.9059 0.4072 -0.0778 -0.0541 225 THR B CB +4154 O OG1 . THR B 226 ? 0.9974 1.0241 0.7174 0.4044 -0.0769 -0.0531 225 THR B OG1 +4155 C CG2 . THR B 226 ? 1.3272 1.3658 1.0556 0.4059 -0.0809 -0.0564 225 THR B CG2 +4156 N N . ALA B 227 ? 1.1410 1.1950 0.8625 0.4133 -0.0780 -0.0528 226 ALA B N +4157 C CA . ALA B 227 ? 1.1712 1.2335 0.8932 0.4160 -0.0789 -0.0541 226 ALA B CA +4158 C C . ALA B 227 ? 1.3694 1.4327 1.0943 0.4155 -0.0813 -0.0574 226 ALA B C +4159 O O . ALA B 227 ? 1.4207 1.4795 1.1495 0.4128 -0.0828 -0.0590 226 ALA B O +4160 C CB . ALA B 227 ? 1.2306 1.2993 0.9573 0.4164 -0.0800 -0.0536 226 ALA B CB +4161 N N . ALA B 228 ? 1.3397 1.4088 1.0625 0.4182 -0.0814 -0.0586 227 ALA B N +4162 C CA . ALA B 228 ? 1.2822 1.3520 1.0062 0.4182 -0.0832 -0.0616 227 ALA B CA +4163 C C . ALA B 228 ? 1.3789 1.4569 1.1016 0.4214 -0.0836 -0.0626 227 ALA B C +4164 O O . ALA B 228 ? 1.2898 1.3735 1.0124 0.4232 -0.0830 -0.0612 227 ALA B O +4165 C CB . ALA B 228 ? 1.1341 1.1967 0.8527 0.4177 -0.0816 -0.0614 227 ALA B CB +4166 N N . GLY B 229 ? 1.4546 1.5335 1.1766 0.4221 -0.0845 -0.0649 228 GLY B N +4167 C CA . GLY B 229 ? 1.6428 1.7288 1.3623 0.4252 -0.0845 -0.0658 228 GLY B CA +4168 C C . GLY B 229 ? 1.7617 1.8565 1.4865 0.4263 -0.0867 -0.0674 228 GLY B C +4169 O O . GLY B 229 ? 1.6701 1.7713 1.3927 0.4290 -0.0864 -0.0678 228 GLY B O +4170 N N . ILE B 230 ? 1.7427 1.8380 1.4746 0.4240 -0.0888 -0.0682 229 ILE B N +4171 C CA . ILE B 230 ? 1.7842 1.8869 1.5223 0.4243 -0.0915 -0.0704 229 ILE B CA +4172 C C . ILE B 230 ? 2.7050 2.8043 2.4485 0.4216 -0.0941 -0.0733 229 ILE B C +4173 O O . ILE B 230 ? 3.1004 3.1927 2.8452 0.4189 -0.0941 -0.0729 229 ILE B O +4174 C CB . ILE B 230 ? 1.5973 1.7035 1.3395 0.4238 -0.0919 -0.0688 229 ILE B CB +4175 C CG1 . ILE B 230 ? 1.5128 1.6235 1.2503 0.4266 -0.0896 -0.0661 229 ILE B CG1 +4176 C CG2 . ILE B 230 ? 1.8655 1.9780 1.6154 0.4231 -0.0951 -0.0712 229 ILE B CG2 +4177 C CD1 . ILE B 230 ? 1.4260 1.5395 1.1668 0.4262 -0.0896 -0.0642 229 ILE B CD1 +4178 N N . THR B 231 ? 2.9260 3.0303 2.6725 0.4222 -0.0963 -0.0763 230 THR B N +4179 C CA . THR B 231 ? 3.1189 3.2207 2.8709 0.4197 -0.0990 -0.0794 230 THR B CA +4180 C C . THR B 231 ? 3.2024 3.3022 2.9612 0.4168 -0.1006 -0.0794 230 THR B C +4181 O O . THR B 231 ? 2.8497 2.9481 2.6140 0.4147 -0.1030 -0.0819 230 THR B O +4182 C CB . THR B 231 ? 2.8327 2.9416 2.5876 0.4210 -0.1013 -0.0826 230 THR B CB +4183 O OG1 . THR B 231 ? 2.7016 2.8079 2.4620 0.4186 -0.1039 -0.0856 230 THR B OG1 +4184 C CG2 . THR B 231 ? 2.6398 2.7574 2.3984 0.4223 -0.1024 -0.0825 230 THR B CG2 +4185 N N . ALA B 235 ? 2.0034 1.9294 1.6007 0.1390 0.0273 0.1206 1054 ALA B N +4186 C CA . ALA B 235 ? 2.1998 2.1234 1.7981 0.1388 0.0324 0.1194 1054 ALA B CA +4187 C C . ALA B 235 ? 2.3927 2.3176 1.9856 0.1412 0.0313 0.1124 1054 ALA B C +4188 O O . ALA B 235 ? 1.8954 1.8249 1.4836 0.1425 0.0275 0.1074 1054 ALA B O +4189 C CB . ALA B 235 ? 1.5320 1.4480 1.1351 0.1389 0.0343 0.1255 1054 ALA B CB +4190 N N . SER B 236 ? 2.6196 2.5405 2.2134 0.1418 0.0347 0.1119 1055 SER B N +4191 C CA . SER B 236 ? 2.7791 2.7001 2.3683 0.1443 0.0338 0.1058 1055 SER B CA +4192 C C . SER B 236 ? 3.0249 2.9409 2.6135 0.1471 0.0297 0.1072 1055 SER B C +4193 O O . SER B 236 ? 2.6427 2.5587 2.2272 0.1496 0.0274 0.1024 1055 SER B O +4194 C CB . SER B 236 ? 2.3884 2.3076 1.9788 0.1435 0.0396 0.1046 1055 SER B CB +4195 O OG . SER B 236 ? 2.1019 2.0222 1.6876 0.1457 0.0388 0.0982 1055 SER B OG +4196 N N . THR B 237 ? 3.2217 3.1335 2.8145 0.1466 0.0289 0.1138 1056 THR B N +4197 C CA . THR B 237 ? 2.8533 2.7604 2.4461 0.1491 0.0247 0.1159 1056 THR B CA +4198 C C . THR B 237 ? 2.4633 2.3744 2.0511 0.1511 0.0186 0.1118 1056 THR B C +4199 O O . THR B 237 ? 1.8692 1.7775 1.4549 0.1538 0.0148 0.1108 1056 THR B O +4200 C CB . THR B 237 ? 2.3831 2.2858 1.9816 0.1478 0.0249 0.1239 1056 THR B CB +4201 O OG1 . THR B 237 ? 2.1053 2.0120 1.7041 0.1465 0.0223 0.1256 1056 THR B OG1 +4202 C CG2 . THR B 237 ? 2.0596 1.9592 1.6631 0.1454 0.0312 0.1280 1056 THR B CG2 +4203 N N . LYS B 238 ? 2.8063 2.7238 2.3922 0.1498 0.0177 0.1094 1057 LYS B N +4204 C CA . LYS B 238 ? 2.5985 2.5206 2.1792 0.1514 0.0123 0.1047 1057 LYS B CA +4205 C C . LYS B 238 ? 2.2337 2.1561 1.8095 0.1540 0.0112 0.0982 1057 LYS B C +4206 O O . LYS B 238 ? 1.8964 1.8172 1.4697 0.1566 0.0067 0.0969 1057 LYS B O +4207 C CB . LYS B 238 ? 2.4018 2.3310 1.9812 0.1493 0.0127 0.1024 1057 LYS B CB +4208 C CG . LYS B 238 ? 2.3635 2.2941 1.9456 0.1477 0.0107 0.1072 1057 LYS B CG +4209 C CD . LYS B 238 ? 2.0418 1.9677 1.6303 0.1456 0.0142 0.1147 1057 LYS B CD +4210 C CE . LYS B 238 ? 1.6876 1.6156 1.2786 0.1438 0.0127 0.1190 1057 LYS B CE +4211 N NZ . LYS B 238 ? 1.7663 1.6894 1.3636 0.1419 0.0158 0.1264 1057 LYS B NZ +4212 N N . LYS B 239 ? 2.4223 2.3468 1.9970 0.1532 0.0154 0.0944 1058 LYS B N +4213 C CA . LYS B 239 ? 2.6426 2.5683 2.2125 0.1554 0.0149 0.0877 1058 LYS B CA +4214 C C . LYS B 239 ? 2.5215 2.4410 2.0910 0.1581 0.0135 0.0881 1058 LYS B C +4215 O O . LYS B 239 ? 2.3143 2.2346 1.8792 0.1605 0.0109 0.0829 1058 LYS B O +4216 C CB . LYS B 239 ? 2.7514 2.6792 2.3213 0.1537 0.0205 0.0849 1058 LYS B CB +4217 C CG . LYS B 239 ? 2.4418 2.3756 2.0121 0.1509 0.0224 0.0843 1058 LYS B CG +4218 C CD . LYS B 239 ? 2.4300 2.3661 1.9997 0.1497 0.0276 0.0806 1058 LYS B CD +4219 C CE . LYS B 239 ? 2.3943 2.3315 1.9587 0.1522 0.0264 0.0736 1058 LYS B CE +4220 N NZ . LYS B 239 ? 1.9479 1.8858 1.5120 0.1513 0.0317 0.0705 1058 LYS B NZ +4221 N N . LEU B 240 ? 2.4589 2.3724 2.0333 0.1576 0.0151 0.0944 1059 LEU B N +4222 C CA . LEU B 240 ? 2.5230 2.4301 2.0978 0.1599 0.0144 0.0956 1059 LEU B CA +4223 C C . LEU B 240 ? 2.4485 2.3543 2.0211 0.1625 0.0081 0.0958 1059 LEU B C +4224 O O . LEU B 240 ? 1.8512 1.7555 1.4205 0.1652 0.0057 0.0922 1059 LEU B O +4225 C CB . LEU B 240 ? 2.5844 2.4856 2.1654 0.1584 0.0183 0.1025 1059 LEU B CB +4226 C CG . LEU B 240 ? 2.3884 2.2825 1.9707 0.1606 0.0173 0.1051 1059 LEU B CG +4227 C CD1 . LEU B 240 ? 2.3224 2.2153 1.9013 0.1625 0.0185 0.0999 1059 LEU B CD1 +4228 C CD2 . LEU B 240 ? 2.1121 2.0009 1.7007 0.1587 0.0212 0.1123 1059 LEU B CD2 +4229 N N . SER B 241 ? 2.6955 2.6018 2.2701 0.1616 0.0055 0.1000 1060 SER B N +4230 C CA . SER B 241 ? 2.3861 2.2911 1.9594 0.1637 -0.0004 0.1010 1060 SER B CA +4231 C C . SER B 241 ? 2.0458 1.9563 1.6130 0.1654 -0.0049 0.0945 1060 SER B C +4232 O O . SER B 241 ? 1.9328 1.8423 1.4976 0.1677 -0.0100 0.0937 1060 SER B O +4233 C CB . SER B 241 ? 1.8718 1.7760 1.4491 0.1621 -0.0017 0.1074 1060 SER B CB +4234 O OG . SER B 241 ? 1.9383 1.8488 1.5144 0.1604 -0.0025 0.1060 1060 SER B OG +4235 N N . GLU B 242 ? 1.9247 1.8410 1.4894 0.1642 -0.0031 0.0899 1061 GLU B N +4236 C CA . GLU B 242 ? 2.3523 2.2740 1.9111 0.1658 -0.0069 0.0832 1061 GLU B CA +4237 C C . GLU B 242 ? 2.1452 2.0644 1.7005 0.1687 -0.0081 0.0790 1061 GLU B C +4238 O O . GLU B 242 ? 1.7869 1.7077 1.3378 0.1710 -0.0130 0.0752 1061 GLU B O +4239 C CB . GLU B 242 ? 2.4392 2.3674 1.9962 0.1638 -0.0041 0.0791 1061 GLU B CB +4240 C CG . GLU B 242 ? 2.5073 2.4378 2.0681 0.1606 -0.0018 0.0832 1061 GLU B CG +4241 C CD . GLU B 242 ? 2.5749 2.5063 2.1367 0.1604 -0.0062 0.0869 1061 GLU B CD +4242 O OE1 . GLU B 242 ? 2.6821 2.6147 2.2404 0.1626 -0.0115 0.0845 1061 GLU B OE1 +4243 O OE2 . GLU B 242 ? 2.3258 2.2568 1.8920 0.1580 -0.0042 0.0922 1061 GLU B OE2 +4244 N N . SER B 243 ? 2.3018 2.2169 1.8591 0.1686 -0.0038 0.0797 1062 SER B N +4245 C CA . SER B 243 ? 2.6767 2.5889 2.2310 0.1712 -0.0043 0.0760 1062 SER B CA +4246 C C . SER B 243 ? 2.4187 2.3248 1.9741 0.1734 -0.0076 0.0795 1062 SER B C +4247 O O . SER B 243 ? 1.7095 1.6154 1.2610 0.1761 -0.0117 0.0760 1062 SER B O +4248 C CB . SER B 243 ? 2.7941 2.7042 2.3502 0.1702 0.0018 0.0755 1062 SER B CB +4249 O OG . SER B 243 ? 2.6890 2.6049 2.2436 0.1685 0.0046 0.0715 1062 SER B OG +4250 N N . LEU B 244 ? 2.3002 2.2017 1.8611 0.1722 -0.0059 0.0864 1063 LEU B N +4251 C CA . LEU B 244 ? 2.0627 1.9583 1.6252 0.1739 -0.0090 0.0905 1063 LEU B CA +4252 C C . LEU B 244 ? 2.2173 2.1154 1.7765 0.1756 -0.0154 0.0891 1063 LEU B C +4253 O O . LEU B 244 ? 1.9303 1.8254 1.4876 0.1782 -0.0191 0.0885 1063 LEU B O +4254 C CB . LEU B 244 ? 1.6835 1.5749 1.2523 0.1719 -0.0065 0.0984 1063 LEU B CB +4255 C CG . LEU B 244 ? 2.0891 1.9750 1.6616 0.1714 -0.0013 0.1011 1063 LEU B CG +4256 C CD1 . LEU B 244 ? 2.0463 1.9280 1.6250 0.1695 0.0005 0.1090 1063 LEU B CD1 +4257 C CD2 . LEU B 244 ? 1.7925 1.6740 1.3627 0.1744 -0.0028 0.0989 1063 LEU B CD2 +4258 N N . LYS B 245 ? 2.3217 2.2255 1.8802 0.1741 -0.0167 0.0885 1064 LYS B N +4259 C CA . LYS B 245 ? 2.2245 2.1320 1.7792 0.1755 -0.0226 0.0860 1064 LYS B CA +4260 C C . LYS B 245 ? 2.2793 2.1880 1.8281 0.1784 -0.0255 0.0793 1064 LYS B C +4261 O O . LYS B 245 ? 2.3956 2.3014 1.9430 0.1809 -0.0295 0.0793 1064 LYS B O +4262 C CB . LYS B 245 ? 1.9610 1.8752 1.5150 0.1733 -0.0226 0.0848 1064 LYS B CB +4263 C CG . LYS B 245 ? 2.2693 2.1830 1.8277 0.1713 -0.0231 0.0913 1064 LYS B CG +4264 C CD . LYS B 245 ? 2.6301 2.5508 2.1876 0.1692 -0.0229 0.0897 1064 LYS B CD +4265 C CE . LYS B 245 ? 2.5049 2.4255 2.0663 0.1674 -0.0241 0.0957 1064 LYS B CE +4266 N NZ . LYS B 245 ? 1.8208 1.7482 1.3809 0.1655 -0.0245 0.0939 1064 LYS B NZ +4267 N N . ARG B 246 ? 2.1831 2.0961 1.7288 0.1781 -0.0233 0.0735 1065 ARG B N +4268 C CA . ARG B 246 ? 2.3736 2.2886 1.9134 0.1808 -0.0262 0.0666 1065 ARG B CA +4269 C C . ARG B 246 ? 2.2940 2.2031 1.8333 0.1833 -0.0266 0.0664 1065 ARG B C +4270 O O . ARG B 246 ? 2.0900 1.9990 1.6253 0.1860 -0.0310 0.0630 1065 ARG B O +4271 C CB . ARG B 246 ? 2.3070 2.2278 1.8437 0.1799 -0.0235 0.0605 1065 ARG B CB +4272 C CG . ARG B 246 ? 2.4679 2.3956 2.0034 0.1781 -0.0245 0.0590 1065 ARG B CG +4273 C CD . ARG B 246 ? 2.7548 2.6878 2.2870 0.1774 -0.0218 0.0527 1065 ARG B CD +4274 N NE . ARG B 246 ? 3.0435 2.9831 2.5747 0.1755 -0.0223 0.0513 1065 ARG B NE +4275 C CZ . ARG B 246 ? 2.7623 2.7072 2.2912 0.1744 -0.0199 0.0465 1065 ARG B CZ +4276 N NH1 . ARG B 246 ? 2.5132 2.4577 2.0404 0.1750 -0.0168 0.0426 1065 ARG B NH1 +4277 N NH2 . ARG B 246 ? 2.1742 2.1249 1.7024 0.1727 -0.0206 0.0456 1065 ARG B NH2 +4278 N N . ILE B 247 ? 2.1100 2.0140 1.6534 0.1824 -0.0221 0.0701 1066 ILE B N +4279 C CA . ILE B 247 ? 2.0951 1.9932 1.6384 0.1847 -0.0220 0.0701 1066 ILE B CA +4280 C C . ILE B 247 ? 2.1409 2.0348 1.6846 0.1867 -0.0269 0.0734 1066 ILE B C +4281 O O . ILE B 247 ? 1.5747 1.4663 1.1154 0.1894 -0.0297 0.0708 1066 ILE B O +4282 C CB . ILE B 247 ? 2.0971 1.9906 1.6450 0.1831 -0.0158 0.0736 1066 ILE B CB +4283 C CG1 . ILE B 247 ? 2.6131 2.5104 2.1596 0.1818 -0.0113 0.0691 1066 ILE B CG1 +4284 C CG2 . ILE B 247 ? 1.5572 1.4439 1.1058 0.1853 -0.0160 0.0750 1066 ILE B CG2 +4285 C CD1 . ILE B 247 ? 2.7991 2.6931 2.3503 0.1797 -0.0049 0.0726 1066 ILE B CD1 +4286 N N . GLY B 248 ? 2.2905 2.1835 1.8379 0.1853 -0.0280 0.0791 1067 GLY B N +4287 C CA . GLY B 248 ? 2.0297 1.9194 1.5776 0.1870 -0.0328 0.0824 1067 GLY B CA +4288 C C . GLY B 248 ? 2.1645 2.0592 1.7074 0.1885 -0.0385 0.0781 1067 GLY B C +4289 O O . GLY B 248 ? 1.9399 1.8325 1.4812 0.1907 -0.0433 0.0785 1067 GLY B O +4290 N N . ASP B 249 ? 2.3180 2.2192 1.8584 0.1873 -0.0379 0.0740 1068 ASP B N +4291 C CA . ASP B 249 ? 2.2026 2.1091 1.7383 0.1884 -0.0430 0.0698 1068 ASP B CA +4292 C C . ASP B 249 ? 2.1724 2.0796 1.7025 0.1913 -0.0456 0.0633 1068 ASP B C +4293 O O . ASP B 249 ? 1.8025 1.7088 1.3301 0.1937 -0.0507 0.0624 1068 ASP B O +4294 C CB . ASP B 249 ? 2.2777 2.1911 1.8128 0.1860 -0.0415 0.0679 1068 ASP B CB +4295 C CG . ASP B 249 ? 2.5305 2.4444 2.0697 0.1838 -0.0418 0.0738 1068 ASP B CG +4296 O OD1 . ASP B 249 ? 2.5894 2.4980 2.1326 0.1837 -0.0420 0.0798 1068 ASP B OD1 +4297 O OD2 . ASP B 249 ? 2.4604 2.3801 1.9988 0.1820 -0.0417 0.0724 1068 ASP B OD2 +4298 N N . GLU B 250 ? 2.5337 2.4426 2.0619 0.1912 -0.0421 0.0587 1069 GLU B N +4299 C CA . GLU B 250 ? 2.6121 2.5214 2.1352 0.1939 -0.0438 0.0524 1069 GLU B CA +4300 C C . GLU B 250 ? 2.2992 2.2019 1.8227 0.1964 -0.0460 0.0544 1069 GLU B C +4301 O O . GLU B 250 ? 1.5695 1.4724 1.0887 0.1991 -0.0501 0.0506 1069 GLU B O +4302 C CB . GLU B 250 ? 2.4587 2.3689 1.9812 0.1931 -0.0385 0.0488 1069 GLU B CB +4303 C CG . GLU B 250 ? 2.7029 2.6195 2.2249 0.1906 -0.0358 0.0463 1069 GLU B CG +4304 C CD . GLU B 250 ? 2.6945 2.6108 2.2178 0.1893 -0.0296 0.0449 1069 GLU B CD +4305 O OE1 . GLU B 250 ? 2.3611 2.2724 1.8851 0.1904 -0.0277 0.0452 1069 GLU B OE1 +4306 O OE2 . GLU B 250 ? 2.5663 2.4873 2.0898 0.1870 -0.0267 0.0435 1069 GLU B OE2 +4307 N N . LEU B 251 ? 2.1849 2.0820 1.7136 0.1954 -0.0433 0.0606 1070 LEU B N +4308 C CA . LEU B 251 ? 2.0157 1.9061 1.5457 0.1974 -0.0450 0.0637 1070 LEU B CA +4309 C C . LEU B 251 ? 2.1584 2.0486 1.6870 0.1992 -0.0513 0.0649 1070 LEU B C +4310 O O . LEU B 251 ? 1.4329 1.3214 0.9581 0.2019 -0.0549 0.0623 1070 LEU B O +4311 C CB . LEU B 251 ? 1.9563 1.8414 1.4927 0.1956 -0.0406 0.0706 1070 LEU B CB +4312 C CG . LEU B 251 ? 2.0321 1.9096 1.5710 0.1971 -0.0408 0.0747 1070 LEU B CG +4313 C CD1 . LEU B 251 ? 1.9870 1.8625 1.5217 0.2001 -0.0424 0.0698 1070 LEU B CD1 +4314 C CD2 . LEU B 251 ? 1.5573 1.4307 1.1019 0.1949 -0.0349 0.0798 1070 LEU B CD2 +4315 N N . ASP B 252 ? 2.4747 2.3666 2.0058 0.1975 -0.0526 0.0690 1071 ASP B N +4316 C CA . ASP B 252 ? 2.2017 2.0932 1.7319 0.1989 -0.0584 0.0707 1071 ASP B CA +4317 C C . ASP B 252 ? 2.1720 2.0691 1.6961 0.2006 -0.0630 0.0643 1071 ASP B C +4318 O O . ASP B 252 ? 1.9843 1.8807 1.5062 0.2027 -0.0682 0.0640 1071 ASP B O +4319 C CB . ASP B 252 ? 1.6753 1.5667 1.2100 0.1967 -0.0584 0.0771 1071 ASP B CB +4320 C CG . ASP B 252 ? 2.7526 2.6434 2.2866 0.1982 -0.0644 0.0791 1071 ASP B CG +4321 O OD1 . ASP B 252 ? 2.6473 2.5328 2.1818 0.2001 -0.0665 0.0812 1071 ASP B OD1 +4322 O OD2 . ASP B 252 ? 3.3081 3.2038 2.8409 0.1973 -0.0670 0.0785 1071 ASP B OD2 +4323 N N . SER B 253 ? 2.2056 2.1082 1.7269 0.1997 -0.0611 0.0592 1072 SER B N +4324 C CA . SER B 253 ? 2.5151 2.4235 2.0307 0.2011 -0.0651 0.0529 1072 SER B CA +4325 C C . SER B 253 ? 2.6805 2.5888 2.1914 0.2035 -0.0656 0.0466 1072 SER B C +4326 O O . SER B 253 ? 2.4855 2.3980 1.9914 0.2051 -0.0693 0.0412 1072 SER B O +4327 C CB . SER B 253 ? 2.5225 2.4377 2.0375 0.1986 -0.0634 0.0508 1072 SER B CB +4328 O OG . SER B 253 ? 2.4740 2.3910 1.9886 0.1975 -0.0585 0.0476 1072 SER B OG +4329 N N . ASN B 254 ? 2.9598 2.8634 2.4723 0.2039 -0.0619 0.0472 1073 ASN B N +4330 C CA . ASN B 254 ? 2.9405 2.8434 2.4488 0.2063 -0.0621 0.0415 1073 ASN B CA +4331 C C . ASN B 254 ? 2.8376 2.7384 2.3427 0.2094 -0.0679 0.0402 1073 ASN B C +4332 O O . ASN B 254 ? 2.3729 2.2677 1.8802 0.2106 -0.0687 0.0440 1073 ASN B O +4333 C CB . ASN B 254 ? 2.8471 2.7447 2.3583 0.2060 -0.0570 0.0433 1073 ASN B CB +4334 C CG . ASN B 254 ? 2.5877 2.4881 2.0960 0.2060 -0.0537 0.0373 1073 ASN B CG +4335 O OD1 . ASN B 254 ? 2.5369 2.4435 2.0429 0.2049 -0.0533 0.0333 1073 ASN B OD1 +4336 N ND2 . ASN B 254 ? 2.3512 2.2470 1.8597 0.2071 -0.0512 0.0366 1073 ASN B ND2 +4337 N N . MET B 255 ? 3.1040 3.0098 2.6039 0.2108 -0.0719 0.0347 1074 MET B N +4338 C CA . MET B 255 ? 3.1620 3.0668 2.6588 0.2136 -0.0779 0.0334 1074 MET B CA +4339 C C . MET B 255 ? 3.0371 2.9370 2.5321 0.2163 -0.0783 0.0315 1074 MET B C +4340 O O . MET B 255 ? 2.6939 2.5905 2.1880 0.2185 -0.0824 0.0326 1074 MET B O +4341 C CB . MET B 255 ? 3.1976 3.1093 2.6891 0.2144 -0.0819 0.0277 1074 MET B CB +4342 C CG . MET B 255 ? 3.1270 3.0428 2.6198 0.2124 -0.0836 0.0302 1074 MET B CG +4343 S SD . MET B 255 ? 3.3355 3.2466 2.8326 0.2125 -0.0868 0.0380 1074 MET B SD +4344 C CE . MET B 255 ? 1.9335 1.8426 1.4258 0.2165 -0.0933 0.0349 1074 MET B CE +4345 N N . GLU B 256 ? 3.1322 3.0315 2.6267 0.2161 -0.0740 0.0286 1075 GLU B N +4346 C CA . GLU B 256 ? 2.9747 2.8691 2.4680 0.2184 -0.0736 0.0270 1075 GLU B CA +4347 C C . GLU B 256 ? 2.6632 2.5505 2.1611 0.2186 -0.0734 0.0338 1075 GLU B C +4348 O O . GLU B 256 ? 2.2563 2.1400 1.7530 0.2210 -0.0772 0.0343 1075 GLU B O +4349 C CB . GLU B 256 ? 2.9809 2.8752 2.4745 0.2174 -0.0679 0.0245 1075 GLU B CB +4350 C CG . GLU B 256 ? 2.9297 2.8310 2.4200 0.2165 -0.0666 0.0187 1075 GLU B CG +4351 C CD . GLU B 256 ? 2.8915 2.7923 2.3830 0.2152 -0.0605 0.0173 1075 GLU B CD +4352 O OE1 . GLU B 256 ? 2.9046 2.8008 2.4010 0.2138 -0.0565 0.0223 1075 GLU B OE1 +4353 O OE2 . GLU B 256 ? 2.7389 2.6438 2.2265 0.2156 -0.0597 0.0111 1075 GLU B OE2 +4354 N N . LEU B 257 ? 2.5201 2.4055 2.0233 0.2160 -0.0689 0.0389 1076 LEU B N +4355 C CA . LEU B 257 ? 2.4256 2.3042 1.9339 0.2157 -0.0675 0.0457 1076 LEU B CA +4356 C C . LEU B 257 ? 2.3495 2.2263 1.8589 0.2165 -0.0724 0.0500 1076 LEU B C +4357 O O . LEU B 257 ? 1.6935 1.5648 1.2040 0.2182 -0.0742 0.0527 1076 LEU B O +4358 C CB . LEU B 257 ? 2.2011 2.0792 1.7144 0.2125 -0.0617 0.0499 1076 LEU B CB +4359 C CG . LEU B 257 ? 2.2117 2.0835 1.7311 0.2115 -0.0595 0.0575 1076 LEU B CG +4360 C CD1 . LEU B 257 ? 1.9609 1.8261 1.4805 0.2137 -0.0595 0.0582 1076 LEU B CD1 +4361 C CD2 . LEU B 257 ? 2.3644 2.2367 1.8880 0.2083 -0.0534 0.0602 1076 LEU B CD2 +4362 N N . GLN B 258 ? 2.4367 2.3183 1.9460 0.2152 -0.0746 0.0505 1077 GLN B N +4363 C CA . GLN B 258 ? 2.3478 2.2282 1.8583 0.2156 -0.0791 0.0547 1077 GLN B CA +4364 C C . GLN B 258 ? 2.4551 2.3340 1.9615 0.2190 -0.0846 0.0519 1077 GLN B C +4365 O O . GLN B 258 ? 2.3897 2.2637 1.8979 0.2202 -0.0871 0.0560 1077 GLN B O +4366 C CB . GLN B 258 ? 2.0271 1.9136 1.5375 0.2138 -0.0806 0.0548 1077 GLN B CB +4367 C CG . GLN B 258 ? 2.3505 2.2388 1.8650 0.2103 -0.0753 0.0577 1077 GLN B CG +4368 C CD . GLN B 258 ? 2.3240 2.2067 1.8448 0.2088 -0.0727 0.0656 1077 GLN B CD +4369 O OE1 . GLN B 258 ? 2.2580 2.1371 1.7806 0.2097 -0.0758 0.0698 1077 GLN B OE1 +4370 N NE2 . GLN B 258 ? 1.7363 1.6184 1.2607 0.2065 -0.0669 0.0675 1077 GLN B NE2 +4371 N N . ARG B 259 ? 2.3540 2.2368 1.8548 0.2206 -0.0863 0.0449 1078 ARG B N +4372 C CA . ARG B 259 ? 2.4101 2.2917 1.9066 0.2239 -0.0912 0.0414 1078 ARG B CA +4373 C C . ARG B 259 ? 2.5101 2.3846 2.0080 0.2255 -0.0899 0.0432 1078 ARG B C +4374 O O . ARG B 259 ? 2.4187 2.2893 1.9165 0.2274 -0.0936 0.0452 1078 ARG B O +4375 C CB . ARG B 259 ? 2.6768 2.5639 2.1674 0.2250 -0.0922 0.0334 1078 ARG B CB +4376 C CG . ARG B 259 ? 2.6997 2.5864 2.1852 0.2284 -0.0977 0.0292 1078 ARG B CG +4377 C CD . ARG B 259 ? 2.9186 2.8071 2.3995 0.2299 -0.0966 0.0222 1078 ARG B CD +4378 N NE . ARG B 259 ? 3.0258 2.9212 2.5043 0.2284 -0.0949 0.0176 1078 ARG B NE +4379 C CZ . ARG B 259 ? 2.7373 2.6342 2.2147 0.2279 -0.0909 0.0137 1078 ARG B CZ +4380 N NH1 . ARG B 259 ? 2.4266 2.3185 1.9048 0.2288 -0.0880 0.0138 1078 ARG B NH1 +4381 N NH2 . ARG B 259 ? 2.2350 2.1382 1.7103 0.2265 -0.0896 0.0096 1078 ARG B NH2 +4382 N N . MET B 260 ? 2.5362 2.4091 2.0355 0.2246 -0.0846 0.0425 1079 MET B N +4383 C CA . MET B 260 ? 2.5673 2.4338 2.0678 0.2259 -0.0827 0.0437 1079 MET B CA +4384 C C . MET B 260 ? 2.6786 2.5387 2.1840 0.2259 -0.0830 0.0510 1079 MET B C +4385 O O . MET B 260 ? 2.6707 2.5257 2.1757 0.2281 -0.0847 0.0517 1079 MET B O +4386 C CB . MET B 260 ? 2.4348 2.3010 1.9369 0.2244 -0.0763 0.0426 1079 MET B CB +4387 C CG . MET B 260 ? 2.1064 1.9726 1.6043 0.2263 -0.0755 0.0363 1079 MET B CG +4388 S SD . MET B 260 ? 3.3178 3.1828 2.8181 0.2244 -0.0679 0.0359 1079 MET B SD +4389 C CE . MET B 260 ? 1.3515 1.2246 0.8512 0.2216 -0.0656 0.0333 1079 MET B CE +4390 N N . ILE B 261 ? 2.5210 2.3812 2.0310 0.2233 -0.0813 0.0564 1080 ILE B N +4391 C CA . ILE B 261 ? 2.5650 2.4191 2.0799 0.2230 -0.0810 0.0636 1080 ILE B CA +4392 C C . ILE B 261 ? 2.5938 2.4472 2.1079 0.2245 -0.0870 0.0655 1080 ILE B C +4393 O O . ILE B 261 ? 2.7844 2.6321 2.3002 0.2259 -0.0886 0.0690 1080 ILE B O +4394 C CB . ILE B 261 ? 2.3220 2.1760 1.8425 0.2197 -0.0768 0.0691 1080 ILE B CB +4395 C CG1 . ILE B 261 ? 1.9964 1.8530 1.5172 0.2178 -0.0712 0.0664 1080 ILE B CG1 +4396 C CG2 . ILE B 261 ? 2.3963 2.2432 1.9220 0.2194 -0.0754 0.0760 1080 ILE B CG2 +4397 C CD1 . ILE B 261 ? 2.0322 1.8876 1.5588 0.2147 -0.0664 0.0720 1080 ILE B CD1 +4398 N N . ALA B 262 ? 2.1260 1.9851 1.6375 0.2243 -0.0904 0.0632 1081 ALA B N +4399 C CA . ALA B 262 ? 2.2962 2.1555 1.8060 0.2260 -0.0965 0.0640 1081 ALA B CA +4400 C C . ALA B 262 ? 2.6315 2.4876 2.1376 0.2293 -0.0996 0.0607 1081 ALA B C +4401 O O . ALA B 262 ? 2.5947 2.4464 2.1017 0.2308 -0.1027 0.0639 1081 ALA B O +4402 C CB . ALA B 262 ? 1.8670 1.7336 1.3735 0.2254 -0.0995 0.0605 1081 ALA B CB +4403 N N . ALA B 263 ? 2.6144 2.4727 2.1164 0.2304 -0.0986 0.0544 1082 ALA B N +4404 C CA . ALA B 263 ? 2.6908 2.5459 2.1894 0.2335 -0.1008 0.0511 1082 ALA B CA +4405 C C . ALA B 263 ? 3.0654 2.9134 2.5675 0.2337 -0.0972 0.0546 1082 ALA B C +4406 O O . ALA B 263 ? 2.9266 2.7738 2.4281 0.2336 -0.0933 0.0520 1082 ALA B O +4407 C CB . ALA B 263 ? 2.5135 2.3734 2.0066 0.2345 -0.1008 0.0432 1082 ALA B CB +4408 N N . VAL B 264 ? 3.2402 3.0830 2.7460 0.2339 -0.0985 0.0607 1083 VAL B N +4409 C CA . VAL B 264 ? 3.2933 3.1290 2.8022 0.2345 -0.0960 0.0642 1083 VAL B CA +4410 C C . VAL B 264 ? 2.9546 2.7854 2.4653 0.2359 -0.0999 0.0691 1083 VAL B C +4411 O O . VAL B 264 ? 2.2169 2.0491 1.7288 0.2351 -0.1027 0.0722 1083 VAL B O +4412 C CB . VAL B 264 ? 2.8333 2.6671 2.3474 0.2317 -0.0895 0.0681 1083 VAL B CB +4413 C CG1 . VAL B 264 ? 2.4980 2.3305 2.0173 0.2296 -0.0892 0.0752 1083 VAL B CG1 +4414 C CG2 . VAL B 264 ? 2.6254 2.4530 2.1409 0.2327 -0.0864 0.0690 1083 VAL B CG2 +4415 N N . ASP B 265 ? 3.0620 2.8870 2.5727 0.2379 -0.1001 0.0696 1084 ASP B N +4416 C CA . ASP B 265 ? 3.1909 3.0109 2.7031 0.2394 -0.1038 0.0739 1084 ASP B CA +4417 C C . ASP B 265 ? 3.1543 2.9691 2.6730 0.2376 -0.1006 0.0815 1084 ASP B C +4418 O O . ASP B 265 ? 2.6273 2.4374 2.1484 0.2375 -0.0968 0.0832 1084 ASP B O +4419 C CB . ASP B 265 ? 3.1669 2.9832 2.6757 0.2426 -0.1059 0.0707 1084 ASP B CB +4420 C CG . ASP B 265 ? 2.9450 2.7587 2.4529 0.2447 -0.1117 0.0726 1084 ASP B CG +4421 O OD1 . ASP B 265 ? 2.9343 2.7457 2.4460 0.2438 -0.1126 0.0785 1084 ASP B OD1 +4422 O OD2 . ASP B 265 ? 2.5712 2.3850 2.0743 0.2474 -0.1153 0.0680 1084 ASP B OD2 +4423 N N . THR B 266 ? 3.3836 3.1992 2.9051 0.2362 -0.1022 0.0861 1085 THR B N +4424 C CA . THR B 266 ? 3.5848 3.3967 3.1126 0.2340 -0.0989 0.0933 1085 THR B CA +4425 C C . THR B 266 ? 3.6176 3.4253 3.1479 0.2348 -0.1026 0.0988 1085 THR B C +4426 O O . THR B 266 ? 3.6538 3.4606 3.1886 0.2328 -0.1017 0.1045 1085 THR B O +4427 C CB . THR B 266 ? 3.6122 3.4292 3.1422 0.2309 -0.0962 0.0944 1085 THR B CB +4428 O OG1 . THR B 266 ? 3.5584 3.3788 3.0866 0.2300 -0.0923 0.0897 1085 THR B OG1 +4429 C CG2 . THR B 266 ? 3.5653 3.3786 3.1019 0.2285 -0.0928 0.1019 1085 THR B CG2 +4430 N N . ASP B 267 ? 3.5207 3.3258 3.0481 0.2377 -0.1068 0.0972 1086 ASP B N +4431 C CA . ASP B 267 ? 3.3517 3.1520 2.8815 0.2387 -0.1100 0.1024 1086 ASP B CA +4432 C C . ASP B 267 ? 3.2366 3.0298 2.7707 0.2385 -0.1063 0.1069 1086 ASP B C +4433 O O . ASP B 267 ? 2.8224 2.6115 2.3610 0.2378 -0.1062 0.1132 1086 ASP B O +4434 C CB . ASP B 267 ? 3.2463 3.0464 2.7712 0.2419 -0.1159 0.0988 1086 ASP B CB +4435 C CG . ASP B 267 ? 3.3101 3.1173 2.8298 0.2424 -0.1192 0.0930 1086 ASP B CG +4436 O OD1 . ASP B 267 ? 3.3472 3.1594 2.8677 0.2401 -0.1177 0.0928 1086 ASP B OD1 +4437 O OD2 . ASP B 267 ? 3.2751 3.0830 2.7901 0.2450 -0.1233 0.0886 1086 ASP B OD2 +4438 N N . SER B 268 ? 3.3289 3.1207 2.8615 0.2392 -0.1032 0.1034 1087 SER B N +4439 C CA . SER B 268 ? 3.1910 2.9768 2.7275 0.2387 -0.0987 0.1069 1087 SER B CA +4440 C C . SER B 268 ? 3.4285 3.2170 2.9664 0.2363 -0.0928 0.1057 1087 SER B C +4441 O O . SER B 268 ? 3.2151 3.0041 2.7507 0.2369 -0.0904 0.1012 1087 SER B O +4442 C CB . SER B 268 ? 2.5942 2.3761 2.1277 0.2417 -0.0998 0.1037 1087 SER B CB +4443 O OG . SER B 268 ? 2.2461 2.0219 1.7834 0.2413 -0.0957 0.1072 1087 SER B OG +4444 N N . PRO B 269 ? 3.4704 3.2607 3.0123 0.2335 -0.0905 0.1098 1088 PRO B N +4445 C CA . PRO B 269 ? 3.0585 2.8527 2.6015 0.2309 -0.0856 0.1085 1088 PRO B CA +4446 C C . PRO B 269 ? 3.0272 2.8173 2.5737 0.2298 -0.0796 0.1104 1088 PRO B C +4447 O O . PRO B 269 ? 2.8680 2.6609 2.4132 0.2289 -0.0760 0.1067 1088 PRO B O +4448 C CB . PRO B 269 ? 2.5431 2.3397 2.0897 0.2284 -0.0859 0.1132 1088 PRO B CB +4449 C CG . PRO B 269 ? 2.7822 2.5733 2.3319 0.2292 -0.0883 0.1191 1088 PRO B CG +4450 C CD . PRO B 269 ? 3.2497 3.0383 2.7955 0.2325 -0.0926 0.1162 1088 PRO B CD +4451 N N . ARG B 270 ? 3.0392 2.8228 2.5900 0.2298 -0.0786 0.1162 1089 ARG B N +4452 C CA . ARG B 270 ? 2.7745 2.5536 2.3292 0.2286 -0.0729 0.1191 1089 ARG B CA +4453 C C . ARG B 270 ? 2.8218 2.6006 2.3737 0.2297 -0.0702 0.1138 1089 ARG B C +4454 O O . ARG B 270 ? 1.9696 1.7487 1.5233 0.2280 -0.0649 0.1136 1089 ARG B O +4455 C CB . ARG B 270 ? 2.3539 2.1259 1.9128 0.2292 -0.0734 0.1255 1089 ARG B CB +4456 C CG . ARG B 270 ? 2.6088 2.3751 2.1699 0.2295 -0.0692 0.1266 1089 ARG B CG +4457 C CD . ARG B 270 ? 2.5963 2.3557 2.1619 0.2298 -0.0695 0.1333 1089 ARG B CD +4458 N NE . ARG B 270 ? 2.7202 2.4739 2.2870 0.2306 -0.0661 0.1338 1089 ARG B NE +4459 C CZ . ARG B 270 ? 2.6854 2.4374 2.2558 0.2287 -0.0604 0.1358 1089 ARG B CZ +4460 N NH1 . ARG B 270 ? 2.7497 2.5050 2.3227 0.2259 -0.0572 0.1375 1089 ARG B NH1 +4461 N NH2 . ARG B 270 ? 2.2903 2.0371 1.8616 0.2297 -0.0577 0.1361 1089 ARG B NH2 +4462 N N . GLU B 271 ? 3.1546 2.9325 2.7020 0.2327 -0.0737 0.1096 1090 GLU B N +4463 C CA . GLU B 271 ? 3.0860 2.8637 2.6301 0.2340 -0.0717 0.1042 1090 GLU B CA +4464 C C . GLU B 271 ? 3.0219 2.8066 2.5627 0.2329 -0.0702 0.0985 1090 GLU B C +4465 O O . GLU B 271 ? 2.6461 2.4312 2.1870 0.2321 -0.0657 0.0962 1090 GLU B O +4466 C CB . GLU B 271 ? 3.1324 2.9083 2.6721 0.2374 -0.0764 0.1007 1090 GLU B CB +4467 C CG . GLU B 271 ? 3.2406 3.0107 2.7824 0.2388 -0.0796 0.1057 1090 GLU B CG +4468 C CD . GLU B 271 ? 3.2694 3.0390 2.8063 0.2421 -0.0850 0.1018 1090 GLU B CD +4469 O OE1 . GLU B 271 ? 3.1247 2.8971 2.6567 0.2435 -0.0855 0.0953 1090 GLU B OE1 +4470 O OE2 . GLU B 271 ? 3.2588 3.0251 2.7965 0.2433 -0.0887 0.1051 1090 GLU B OE2 +4471 N N . VAL B 272 ? 3.2193 3.0094 2.7574 0.2329 -0.0741 0.0963 1091 VAL B N +4472 C CA . VAL B 272 ? 3.1513 2.9485 2.6858 0.2322 -0.0736 0.0906 1091 VAL B CA +4473 C C . VAL B 272 ? 3.0882 2.8873 2.6259 0.2291 -0.0677 0.0918 1091 VAL B C +4474 O O . VAL B 272 ? 3.0127 2.8148 2.5481 0.2288 -0.0649 0.0871 1091 VAL B O +4475 C CB . VAL B 272 ? 2.4913 2.2938 2.0232 0.2323 -0.0786 0.0893 1091 VAL B CB +4476 C CG1 . VAL B 272 ? 2.3953 2.2049 1.9227 0.2320 -0.0786 0.0826 1091 VAL B CG1 +4477 C CG2 . VAL B 272 ? 2.3238 2.1240 1.8530 0.2352 -0.0845 0.0888 1091 VAL B CG2 +4478 N N . PHE B 273 ? 3.1017 2.8992 2.6447 0.2269 -0.0658 0.0982 1092 PHE B N +4479 C CA . PHE B 273 ? 3.0341 2.8330 2.5807 0.2239 -0.0602 0.1002 1092 PHE B CA +4480 C C . PHE B 273 ? 2.7490 2.5438 2.2971 0.2238 -0.0552 0.0999 1092 PHE B C +4481 O O . PHE B 273 ? 2.7015 2.4992 2.2484 0.2228 -0.0515 0.0964 1092 PHE B O +4482 C CB . PHE B 273 ? 3.2331 3.0302 2.7852 0.2217 -0.0596 0.1075 1092 PHE B CB +4483 C CG . PHE B 273 ? 3.2691 3.0666 2.8257 0.2186 -0.0536 0.1104 1092 PHE B CG +4484 C CD1 . PHE B 273 ? 3.1336 2.9373 2.6892 0.2166 -0.0517 0.1079 1092 PHE B CD1 +4485 C CD2 . PHE B 273 ? 3.1916 2.9831 2.7531 0.2177 -0.0497 0.1157 1092 PHE B CD2 +4486 C CE1 . PHE B 273 ? 2.9187 2.7226 2.4783 0.2138 -0.0462 0.1105 1092 PHE B CE1 +4487 C CE2 . PHE B 273 ? 3.0282 2.8199 2.5937 0.2149 -0.0442 0.1184 1092 PHE B CE2 +4488 C CZ . PHE B 273 ? 2.8525 2.6505 2.4171 0.2129 -0.0425 0.1158 1092 PHE B CZ +4489 N N . PHE B 274 ? 2.4140 2.2021 1.9645 0.2250 -0.0551 0.1037 1093 PHE B N +4490 C CA . PHE B 274 ? 2.7716 2.5550 2.3240 0.2250 -0.0504 0.1043 1093 PHE B CA +4491 C C . PHE B 274 ? 2.9552 2.7405 2.5029 0.2264 -0.0493 0.0973 1093 PHE B C +4492 O O . PHE B 274 ? 2.8795 2.6645 2.4284 0.2252 -0.0443 0.0963 1093 PHE B O +4493 C CB . PHE B 274 ? 3.0815 2.8575 2.6365 0.2264 -0.0515 0.1089 1093 PHE B CB +4494 C CG . PHE B 274 ? 3.2415 3.0124 2.7984 0.2266 -0.0470 0.1096 1093 PHE B CG +4495 C CD1 . PHE B 274 ? 2.8744 2.6429 2.4365 0.2242 -0.0416 0.1142 1093 PHE B CD1 +4496 C CD2 . PHE B 274 ? 3.1325 2.9011 2.6859 0.2293 -0.0480 0.1055 1093 PHE B CD2 +4497 C CE1 . PHE B 274 ? 2.7483 2.5122 2.3122 0.2243 -0.0374 0.1148 1093 PHE B CE1 +4498 C CE2 . PHE B 274 ? 2.5534 2.3172 2.1084 0.2295 -0.0438 0.1061 1093 PHE B CE2 +4499 C CZ . PHE B 274 ? 2.5189 2.2805 2.0793 0.2270 -0.0386 0.1107 1093 PHE B CZ +4500 N N . ARG B 275 ? 2.9773 2.7645 2.5198 0.2290 -0.0540 0.0923 1094 ARG B N +4501 C CA . ARG B 275 ? 2.8589 2.6477 2.3967 0.2306 -0.0534 0.0855 1094 ARG B CA +4502 C C . ARG B 275 ? 2.6902 2.4857 2.2260 0.2289 -0.0511 0.0812 1094 ARG B C +4503 O O . ARG B 275 ? 2.6731 2.4692 2.2078 0.2286 -0.0474 0.0778 1094 ARG B O +4504 C CB . ARG B 275 ? 2.9650 2.7540 2.4976 0.2338 -0.0592 0.0815 1094 ARG B CB +4505 C CG . ARG B 275 ? 2.9248 2.7112 2.4541 0.2361 -0.0586 0.0770 1094 ARG B CG +4506 C CD . ARG B 275 ? 2.8932 2.6811 2.4169 0.2391 -0.0644 0.0721 1094 ARG B CD +4507 N NE . ARG B 275 ? 2.9338 2.7219 2.4577 0.2397 -0.0695 0.0750 1094 ARG B NE +4508 C CZ . ARG B 275 ? 2.6407 2.4234 2.1662 0.2412 -0.0722 0.0789 1094 ARG B CZ +4509 N NH1 . ARG B 275 ? 1.9754 1.7521 1.5022 0.2423 -0.0703 0.0803 1094 ARG B NH1 +4510 N NH2 . ARG B 275 ? 2.3413 2.1247 1.8668 0.2415 -0.0767 0.0813 1094 ARG B NH2 +4511 N N . VAL B 276 ? 2.4360 2.2365 1.9714 0.2277 -0.0534 0.0814 1095 VAL B N +4512 C CA . VAL B 276 ? 2.3913 2.1985 1.9251 0.2258 -0.0514 0.0778 1095 VAL B CA +4513 C C . VAL B 276 ? 2.4034 2.2097 1.9420 0.2229 -0.0450 0.0811 1095 VAL B C +4514 O O . VAL B 276 ? 2.2494 2.0593 1.7869 0.2218 -0.0416 0.0775 1095 VAL B O +4515 C CB . VAL B 276 ? 2.4850 2.2974 2.0179 0.2250 -0.0552 0.0780 1095 VAL B CB +4516 C CG1 . VAL B 276 ? 2.1254 1.9442 1.6581 0.2226 -0.0523 0.0757 1095 VAL B CG1 +4517 C CG2 . VAL B 276 ? 2.9134 2.7278 2.4408 0.2278 -0.0612 0.0734 1095 VAL B CG2 +4518 N N . ALA B 277 ? 2.5160 2.3175 2.0600 0.2218 -0.0436 0.0881 1096 ALA B N +4519 C CA . ALA B 277 ? 2.1754 1.9750 1.7244 0.2192 -0.0375 0.0919 1096 ALA B CA +4520 C C . ALA B 277 ? 2.1529 1.9495 1.7012 0.2200 -0.0337 0.0893 1096 ALA B C +4521 O O . ALA B 277 ? 2.0394 1.8383 1.5882 0.2183 -0.0292 0.0875 1096 ALA B O +4522 C CB . ALA B 277 ? 1.8245 1.6188 1.3791 0.2183 -0.0372 0.0998 1096 ALA B CB +4523 N N . ALA B 278 ? 2.2499 2.0415 1.7972 0.2225 -0.0355 0.0892 1097 ALA B N +4524 C CA . ALA B 278 ? 2.0746 1.8628 1.6212 0.2235 -0.0323 0.0869 1097 ALA B CA +4525 C C . ALA B 278 ? 2.0078 1.8006 1.5488 0.2246 -0.0324 0.0790 1097 ALA B C +4526 O O . ALA B 278 ? 1.9543 1.7460 1.4949 0.2247 -0.0286 0.0766 1097 ALA B O +4527 C CB . ALA B 278 ? 1.8360 1.6175 1.3830 0.2259 -0.0344 0.0891 1097 ALA B CB +4528 N N . ASP B 279 ? 1.9359 1.7340 1.4725 0.2256 -0.0368 0.0749 1098 ASP B N +4529 C CA . ASP B 279 ? 1.9858 1.7888 1.5172 0.2265 -0.0370 0.0673 1098 ASP B CA +4530 C C . ASP B 279 ? 2.3681 2.1761 1.9004 0.2237 -0.0327 0.0660 1098 ASP B C +4531 O O . ASP B 279 ? 2.0036 1.8136 1.5335 0.2237 -0.0299 0.0612 1098 ASP B O +4532 C CB . ASP B 279 ? 2.0886 1.8954 1.6149 0.2284 -0.0432 0.0633 1098 ASP B CB +4533 C CG . ASP B 279 ? 2.3706 2.1801 1.8911 0.2305 -0.0442 0.0557 1098 ASP B CG +4534 O OD1 . ASP B 279 ? 2.1859 2.0010 1.7040 0.2295 -0.0428 0.0512 1098 ASP B OD1 +4535 O OD2 . ASP B 279 ? 2.5008 2.3066 2.0191 0.2331 -0.0465 0.0541 1098 ASP B OD2 +4536 N N . MET B 280 ? 2.5589 2.3688 2.0946 0.2213 -0.0321 0.0703 1099 MET B N +4537 C CA . MET B 280 ? 2.3883 2.2025 1.9255 0.2184 -0.0278 0.0699 1099 MET B CA +4538 C C . MET B 280 ? 2.1193 1.9301 1.6598 0.2172 -0.0216 0.0714 1099 MET B C +4539 O O . MET B 280 ? 2.0383 1.8525 1.5784 0.2156 -0.0178 0.0687 1099 MET B O +4540 C CB . MET B 280 ? 2.5405 2.3563 2.0815 0.2161 -0.0283 0.0751 1099 MET B CB +4541 C CG . MET B 280 ? 2.7674 2.5891 2.3051 0.2163 -0.0330 0.0726 1099 MET B CG +4542 S SD . MET B 280 ? 2.5841 2.4082 2.1263 0.2132 -0.0325 0.0785 1099 MET B SD +4543 C CE . MET B 280 ? 1.9072 1.7328 1.4526 0.2101 -0.0251 0.0788 1099 MET B CE +4544 N N . PHE B 281 ? 2.0162 1.8201 1.5598 0.2179 -0.0207 0.0757 1100 PHE B N +4545 C CA . PHE B 281 ? 2.0478 1.8478 1.5952 0.2165 -0.0148 0.0783 1100 PHE B CA +4546 C C . PHE B 281 ? 2.2780 2.0736 1.8235 0.2188 -0.0140 0.0756 1100 PHE B C +4547 O O . PHE B 281 ? 2.0884 1.8786 1.6376 0.2185 -0.0107 0.0793 1100 PHE B O +4548 C CB . PHE B 281 ? 1.8137 1.6092 1.3673 0.2149 -0.0134 0.0863 1100 PHE B CB +4549 C CG . PHE B 281 ? 2.1648 1.9643 1.7208 0.2122 -0.0129 0.0892 1100 PHE B CG +4550 C CD1 . PHE B 281 ? 2.2893 2.0944 1.8446 0.2102 -0.0100 0.0862 1100 PHE B CD1 +4551 C CD2 . PHE B 281 ? 1.7963 1.5942 1.3554 0.2117 -0.0155 0.0948 1100 PHE B CD2 +4552 C CE1 . PHE B 281 ? 2.2281 2.0370 1.7857 0.2078 -0.0095 0.0888 1100 PHE B CE1 +4553 C CE2 . PHE B 281 ? 1.7407 1.5423 1.3021 0.2092 -0.0150 0.0974 1100 PHE B CE2 +4554 C CZ . PHE B 281 ? 2.0306 1.8378 1.5913 0.2072 -0.0120 0.0944 1100 PHE B CZ +4555 N N . SER B 282 ? 2.6175 2.4158 2.1574 0.2211 -0.0171 0.0693 1101 SER B N +4556 C CA . SER B 282 ? 2.8244 2.6192 2.3618 0.2234 -0.0165 0.0659 1101 SER B CA +4557 C C . SER B 282 ? 2.8218 2.6185 2.3588 0.2222 -0.0112 0.0625 1101 SER B C +4558 O O . SER B 282 ? 2.2933 2.0862 1.8304 0.2231 -0.0086 0.0615 1101 SER B O +4559 C CB . SER B 282 ? 2.8910 2.6879 2.4224 0.2263 -0.0220 0.0604 1101 SER B CB +4560 O OG . SER B 282 ? 2.7507 2.5548 2.2782 0.2259 -0.0229 0.0549 1101 SER B OG +4561 N N . ASP B 283 ? 2.9417 2.7444 2.4783 0.2201 -0.0096 0.0606 1102 ASP B N +4562 C CA . ASP B 283 ? 2.4898 2.2945 2.0265 0.2186 -0.0043 0.0579 1102 ASP B CA +4563 C C . ASP B 283 ? 2.1193 1.9213 1.6623 0.2158 0.0009 0.0641 1102 ASP B C +4564 O O . ASP B 283 ? 1.6889 1.4912 1.2331 0.2143 0.0059 0.0631 1102 ASP B O +4565 C CB . ASP B 283 ? 2.3660 2.1786 1.8989 0.2178 -0.0048 0.0524 1102 ASP B CB +4566 C CG . ASP B 283 ? 2.4604 2.2770 1.9949 0.2159 -0.0066 0.0552 1102 ASP B CG +4567 O OD1 . ASP B 283 ? 2.7338 2.5477 2.2707 0.2160 -0.0094 0.0600 1102 ASP B OD1 +4568 O OD2 . ASP B 283 ? 1.8533 1.6759 1.3867 0.2142 -0.0052 0.0524 1102 ASP B OD2 +4569 N N . GLY B 284 ? 2.0627 1.8620 1.6096 0.2151 -0.0006 0.0703 1103 GLY B N +4570 C CA . GLY B 284 ? 2.0762 1.8715 1.6292 0.2128 0.0037 0.0769 1103 GLY B CA +4571 C C . GLY B 284 ? 2.4239 2.2231 1.9792 0.2097 0.0084 0.0774 1103 GLY B C +4572 O O . GLY B 284 ? 1.6415 1.4376 1.2011 0.2079 0.0133 0.0810 1103 GLY B O +4573 N N . ASN B 285 ? 2.9857 2.7916 2.5381 0.2090 0.0068 0.0737 1104 ASN B N +4574 C CA . ASN B 285 ? 2.6773 2.4878 2.2315 0.2060 0.0106 0.0738 1104 ASN B CA +4575 C C . ASN B 285 ? 2.0418 1.8544 1.5986 0.2042 0.0089 0.0782 1104 ASN B C +4576 O O . ASN B 285 ? 2.0241 1.8425 1.5782 0.2039 0.0062 0.0754 1104 ASN B O +4577 C CB . ASN B 285 ? 2.4564 2.2732 2.0054 0.2063 0.0105 0.0663 1104 ASN B CB +4578 C CG . ASN B 285 ? 2.5508 2.3659 2.0971 0.2080 0.0125 0.0616 1104 ASN B CG +4579 O OD1 . ASN B 285 ? 2.2781 2.0875 1.8270 0.2082 0.0155 0.0642 1104 ASN B OD1 +4580 N ND2 . ASN B 285 ? 2.2138 2.0338 1.7547 0.2091 0.0109 0.0547 1104 ASN B ND2 +4581 N N . PHE B 286 ? 1.8916 1.6995 1.4538 0.2029 0.0105 0.0852 1105 PHE B N +4582 C CA . PHE B 286 ? 2.1659 1.9749 1.7314 0.2012 0.0091 0.0903 1105 PHE B CA +4583 C C . PHE B 286 ? 2.7205 2.5347 2.2875 0.1981 0.0125 0.0903 1105 PHE B C +4584 O O . PHE B 286 ? 2.8705 2.6844 2.4394 0.1965 0.0177 0.0903 1105 PHE B O +4585 C CB . PHE B 286 ? 2.0955 1.8978 1.6668 0.2005 0.0106 0.0978 1105 PHE B CB +4586 C CG . PHE B 286 ? 2.6689 2.4656 2.2395 0.2033 0.0072 0.0991 1105 PHE B CG +4587 C CD1 . PHE B 286 ? 3.0649 2.8615 2.6346 0.2045 0.0017 0.1007 1105 PHE B CD1 +4588 C CD2 . PHE B 286 ? 2.2690 2.0604 1.8402 0.2045 0.0095 0.0990 1105 PHE B CD2 +4589 C CE1 . PHE B 286 ? 3.0549 2.8464 2.6242 0.2070 -0.0015 0.1019 1105 PHE B CE1 +4590 C CE2 . PHE B 286 ? 1.8105 1.5967 1.3811 0.2070 0.0064 0.1003 1105 PHE B CE2 +4591 C CZ . PHE B 286 ? 2.4411 2.2273 2.0108 0.2083 0.0009 0.1018 1105 PHE B CZ +4592 N N . ASN B 287 ? 2.8425 2.6613 2.4087 0.1973 0.0094 0.0905 1106 ASN B N +4593 C CA . ASN B 287 ? 2.4447 2.2679 2.0131 0.1943 0.0121 0.0919 1106 ASN B CA +4594 C C . ASN B 287 ? 2.2775 2.1022 1.8472 0.1936 0.0082 0.0956 1106 ASN B C +4595 O O . ASN B 287 ? 2.0127 1.8375 1.5798 0.1957 0.0029 0.0946 1106 ASN B O +4596 C CB . ASN B 287 ? 2.2481 2.0780 1.8122 0.1939 0.0130 0.0851 1106 ASN B CB +4597 C CG . ASN B 287 ? 2.1861 2.0189 1.7441 0.1966 0.0081 0.0789 1106 ASN B CG +4598 O OD1 . ASN B 287 ? 2.0744 1.9092 1.6307 0.1975 0.0031 0.0789 1106 ASN B OD1 +4599 N ND2 . ASN B 287 ? 1.8979 1.7310 1.4524 0.1980 0.0094 0.0735 1106 ASN B ND2 +4600 N N . TRP B 288 ? 2.2754 2.1015 1.8493 0.1908 0.0108 0.0999 1107 TRP B N +4601 C CA . TRP B 288 ? 1.6851 1.5123 1.2608 0.1899 0.0076 0.1040 1107 TRP B CA +4602 C C . TRP B 288 ? 1.9382 1.7708 1.5091 0.1911 0.0022 0.0997 1107 TRP B C +4603 O O . TRP B 288 ? 1.7230 1.5554 1.2944 0.1916 -0.0020 0.1025 1107 TRP B O +4604 C CB . TRP B 288 ? 1.8103 1.6393 1.3904 0.1865 0.0116 0.1080 1107 TRP B CB +4605 C CG . TRP B 288 ? 2.4184 2.2419 2.0043 0.1854 0.0130 0.1156 1107 TRP B CG +4606 C CD1 . TRP B 288 ? 2.7912 2.6108 2.3817 0.1837 0.0183 0.1195 1107 TRP B CD1 +4607 C CD2 . TRP B 288 ? 2.6337 2.4550 2.2215 0.1858 0.0090 0.1203 1107 TRP B CD2 +4608 N NE1 . TRP B 288 ? 3.0738 2.8889 2.6691 0.1831 0.0178 0.1264 1107 TRP B NE1 +4609 C CE2 . TRP B 288 ? 3.0057 2.8217 2.5993 0.1844 0.0122 0.1270 1107 TRP B CE2 +4610 C CE3 . TRP B 288 ? 2.3599 2.1832 1.9450 0.1873 0.0031 0.1195 1107 TRP B CE3 +4611 C CZ2 . TRP B 288 ? 2.7228 2.5354 2.3196 0.1844 0.0096 0.1329 1107 TRP B CZ2 +4612 C CZ3 . TRP B 288 ? 2.0804 1.9003 1.6687 0.1873 0.0005 0.1253 1107 TRP B CZ3 +4613 C CH2 . TRP B 288 ? 2.0844 1.8991 1.6785 0.1859 0.0038 0.1319 1107 TRP B CH2 +4614 N N . GLY B 289 ? 1.8489 1.6865 1.4152 0.1916 0.0022 0.0930 1108 GLY B N +4615 C CA . GLY B 289 ? 1.9614 1.8043 1.5227 0.1929 -0.0028 0.0884 1108 GLY B CA +4616 C C . GLY B 289 ? 2.2490 2.0890 1.8079 0.1959 -0.0083 0.0880 1108 GLY B C +4617 O O . GLY B 289 ? 2.1137 1.9559 1.6710 0.1965 -0.0130 0.0882 1108 GLY B O +4618 N N . ARG B 290 ? 2.2427 2.0776 1.8013 0.1978 -0.0076 0.0875 1109 ARG B N +4619 C CA . ARG B 290 ? 1.9102 1.7418 1.4666 0.2008 -0.0125 0.0871 1109 ARG B CA +4620 C C . ARG B 290 ? 1.9719 1.7986 1.5326 0.2007 -0.0142 0.0942 1109 ARG B C +4621 O O . ARG B 290 ? 1.7559 1.5818 1.3149 0.2025 -0.0193 0.0946 1109 ARG B O +4622 C CB . ARG B 290 ? 1.5028 1.3303 1.0574 0.2028 -0.0110 0.0843 1109 ARG B CB +4623 C CG . ARG B 290 ? 1.9436 1.7756 1.4928 0.2039 -0.0108 0.0765 1109 ARG B CG +4624 C CD . ARG B 290 ? 2.0851 1.9127 1.6325 0.2062 -0.0102 0.0740 1109 ARG B CD +4625 N NE . ARG B 290 ? 2.1813 2.0129 1.7238 0.2072 -0.0097 0.0667 1109 ARG B NE +4626 C CZ . ARG B 290 ? 2.4175 2.2463 1.9579 0.2090 -0.0086 0.0635 1109 ARG B CZ +4627 N NH1 . ARG B 290 ? 2.5971 2.4192 2.1401 0.2100 -0.0079 0.0670 1109 ARG B NH1 +4628 N NH2 . ARG B 290 ? 2.2691 2.1019 1.8050 0.2098 -0.0082 0.0567 1109 ARG B NH2 +4629 N N . VAL B 291 ? 1.9773 1.8005 1.5434 0.1986 -0.0098 0.0998 1110 VAL B N +4630 C CA . VAL B 291 ? 1.7546 1.5733 1.3253 0.1980 -0.0108 0.1069 1110 VAL B CA +4631 C C . VAL B 291 ? 1.7169 1.5397 1.2874 0.1973 -0.0148 0.1083 1110 VAL B C +4632 O O . VAL B 291 ? 1.7773 1.5977 1.3488 0.1983 -0.0186 0.1117 1110 VAL B O +4633 C CB . VAL B 291 ? 2.1714 1.9871 1.7480 0.1954 -0.0050 0.1122 1110 VAL B CB +4634 C CG1 . VAL B 291 ? 2.0965 1.9077 1.6780 0.1947 -0.0060 0.1198 1110 VAL B CG1 +4635 C CG2 . VAL B 291 ? 1.8024 1.6144 1.3793 0.1960 -0.0008 0.1108 1110 VAL B CG2 +4636 N N . VAL B 292 ? 1.7704 1.5996 1.3394 0.1956 -0.0138 0.1054 1111 VAL B N +4637 C CA . VAL B 292 ? 1.9481 1.7817 1.5166 0.1947 -0.0172 0.1062 1111 VAL B CA +4638 C C . VAL B 292 ? 1.9323 1.7692 1.4950 0.1972 -0.0230 0.1010 1111 VAL B C +4639 O O . VAL B 292 ? 1.9386 1.7757 1.5012 0.1979 -0.0275 0.1031 1111 VAL B O +4640 C CB . VAL B 292 ? 1.8273 1.6665 1.3967 0.1918 -0.0137 0.1053 1111 VAL B CB +4641 C CG1 . VAL B 292 ? 1.2145 1.0587 0.7829 0.1910 -0.0174 0.1055 1111 VAL B CG1 +4642 C CG2 . VAL B 292 ? 2.0840 1.9200 1.6595 0.1892 -0.0084 0.1112 1111 VAL B CG2 +4643 N N . ALA B 293 ? 1.8658 1.7052 1.4239 0.1987 -0.0230 0.0944 1112 ALA B N +4644 C CA . ALA B 293 ? 1.8483 1.6907 1.4007 0.2012 -0.0285 0.0891 1112 ALA B CA +4645 C C . ALA B 293 ? 2.0240 1.8611 1.5760 0.2038 -0.0326 0.0910 1112 ALA B C +4646 O O . ALA B 293 ? 1.7283 1.5673 1.2770 0.2056 -0.0379 0.0890 1112 ALA B O +4647 C CB . ALA B 293 ? 1.5795 1.4252 1.1271 0.2022 -0.0273 0.0817 1112 ALA B CB +4648 N N . LEU B 294 ? 2.2200 2.0507 1.7754 0.2041 -0.0301 0.0949 1113 LEU B N +4649 C CA . LEU B 294 ? 2.0614 1.8868 1.6170 0.2064 -0.0338 0.0973 1113 LEU B CA +4650 C C . LEU B 294 ? 1.9146 1.7380 1.4745 0.2052 -0.0354 0.1042 1113 LEU B C +4651 O O . LEU B 294 ? 2.0162 1.8367 1.5759 0.2070 -0.0396 0.1062 1113 LEU B O +4652 C CB . LEU B 294 ? 1.8414 1.6606 1.3983 0.2075 -0.0308 0.0981 1113 LEU B CB +4653 C CG . LEU B 294 ? 2.0254 1.8387 1.5824 0.2100 -0.0341 0.1003 1113 LEU B CG +4654 C CD1 . LEU B 294 ? 1.9478 1.7584 1.5023 0.2120 -0.0329 0.0963 1113 LEU B CD1 +4655 C CD2 . LEU B 294 ? 2.3456 2.1534 1.9088 0.2087 -0.0323 0.1081 1113 LEU B CD2 +4656 N N . PHE B 295 ? 1.6832 1.5082 1.2470 0.2023 -0.0320 0.1077 1114 PHE B N +4657 C CA . PHE B 295 ? 2.0291 1.8528 1.5970 0.2009 -0.0333 0.1141 1114 PHE B CA +4658 C C . PHE B 295 ? 2.2246 2.0542 1.7900 0.2006 -0.0375 0.1124 1114 PHE B C +4659 O O . PHE B 295 ? 2.3339 2.1632 1.9019 0.1998 -0.0395 0.1171 1114 PHE B O +4660 C CB . PHE B 295 ? 2.1187 1.9411 1.6923 0.1978 -0.0277 0.1191 1114 PHE B CB +4661 C CG . PHE B 295 ? 2.3822 2.2012 1.9608 0.1967 -0.0285 0.1266 1114 PHE B CG +4662 C CD1 . PHE B 295 ? 2.4853 2.2973 2.0668 0.1977 -0.0287 0.1311 1114 PHE B CD1 +4663 C CD2 . PHE B 295 ? 2.0780 1.9009 1.6584 0.1945 -0.0290 0.1290 1114 PHE B CD2 +4664 C CE1 . PHE B 295 ? 2.5019 2.3109 2.0880 0.1967 -0.0294 0.1379 1114 PHE B CE1 +4665 C CE2 . PHE B 295 ? 2.2602 2.0800 1.8451 0.1935 -0.0297 0.1359 1114 PHE B CE2 +4666 C CZ . PHE B 295 ? 2.5445 2.3574 2.1324 0.1945 -0.0299 0.1403 1114 PHE B CZ +4667 N N . TYR B 296 ? 2.2772 2.1124 1.8375 0.2014 -0.0388 0.1057 1115 TYR B N +4668 C CA . TYR B 296 ? 2.2747 2.1156 1.8315 0.2017 -0.0435 0.1030 1115 TYR B CA +4669 C C . TYR B 296 ? 2.3408 2.1799 1.8939 0.2050 -0.0489 0.1007 1115 TYR B C +4670 O O . TYR B 296 ? 1.9281 1.7690 1.4797 0.2058 -0.0538 0.1010 1115 TYR B O +4671 C CB . TYR B 296 ? 2.2598 2.1075 1.8130 0.2008 -0.0418 0.0967 1115 TYR B CB +4672 C CG . TYR B 296 ? 2.4153 2.2697 1.9642 0.2013 -0.0463 0.0925 1115 TYR B CG +4673 C CD1 . TYR B 296 ? 2.6967 2.5548 2.2471 0.1992 -0.0471 0.0950 1115 TYR B CD1 +4674 C CD2 . TYR B 296 ? 2.2917 2.1485 1.8348 0.2038 -0.0497 0.0861 1115 TYR B CD2 +4675 C CE1 . TYR B 296 ? 2.7306 2.5948 2.2770 0.1996 -0.0511 0.0911 1115 TYR B CE1 +4676 C CE2 . TYR B 296 ? 2.2172 2.0799 1.7562 0.2042 -0.0537 0.0822 1115 TYR B CE2 +4677 C CZ . TYR B 296 ? 2.2000 2.0664 1.7407 0.2021 -0.0545 0.0848 1115 TYR B CZ +4678 O OH . TYR B 296 ? 1.8750 1.7473 1.4116 0.2027 -0.0585 0.0808 1115 TYR B OH +4679 N N . PHE B 297 ? 2.4978 2.3331 2.0495 0.2069 -0.0481 0.0986 1116 PHE B N +4680 C CA . PHE B 297 ? 2.3379 2.1706 1.8864 0.2101 -0.0529 0.0968 1116 PHE B CA +4681 C C . PHE B 297 ? 2.1246 1.9519 1.6769 0.2105 -0.0551 0.1034 1116 PHE B C +4682 O O . PHE B 297 ? 1.7490 1.5775 1.3001 0.2113 -0.0599 0.1042 1116 PHE B O +4683 C CB . PHE B 297 ? 2.3879 2.2179 1.9341 0.2119 -0.0511 0.0928 1116 PHE B CB +4684 C CG . PHE B 297 ? 2.7069 2.5361 2.2484 0.2152 -0.0562 0.0890 1116 PHE B CG +4685 C CD1 . PHE B 297 ? 2.5088 2.3437 2.0448 0.2164 -0.0595 0.0828 1116 PHE B CD1 +4686 C CD2 . PHE B 297 ? 3.0085 2.8313 2.5512 0.2171 -0.0576 0.0917 1116 PHE B CD2 +4687 C CE1 . PHE B 297 ? 2.7200 2.5540 2.2516 0.2195 -0.0642 0.0793 1116 PHE B CE1 +4688 C CE2 . PHE B 297 ? 2.9396 2.7615 2.4779 0.2202 -0.0623 0.0883 1116 PHE B CE2 +4689 C CZ . PHE B 297 ? 2.9053 2.7329 2.4381 0.2213 -0.0656 0.0820 1116 PHE B CZ +4690 N N . ALA B 298 ? 2.0252 1.8466 1.5819 0.2099 -0.0515 0.1080 1117 ALA B N +4691 C CA . ALA B 298 ? 2.1824 1.9985 1.7434 0.2099 -0.0529 0.1149 1117 ALA B CA +4692 C C . ALA B 298 ? 2.5993 2.4182 2.1625 0.2081 -0.0548 0.1187 1117 ALA B C +4693 O O . ALA B 298 ? 2.4323 2.2484 1.9971 0.2088 -0.0582 0.1228 1117 ALA B O +4694 C CB . ALA B 298 ? 2.0477 1.8581 1.6137 0.2087 -0.0476 0.1195 1117 ALA B CB +4695 N N . SER B 299 ? 2.7218 2.5462 2.2849 0.2059 -0.0527 0.1172 1118 SER B N +4696 C CA . SER B 299 ? 2.5747 2.4031 2.1387 0.2043 -0.0550 0.1193 1118 SER B CA +4697 C C . SER B 299 ? 2.4225 2.2535 1.9818 0.2067 -0.0615 0.1160 1118 SER B C +4698 O O . SER B 299 ? 2.4622 2.2910 2.0227 0.2074 -0.0652 0.1197 1118 SER B O +4699 C CB . SER B 299 ? 2.5022 2.3366 2.0660 0.2018 -0.0516 0.1170 1118 SER B CB +4700 O OG . SER B 299 ? 2.4083 2.2460 1.9741 0.1999 -0.0528 0.1201 1118 SER B OG +4701 N N . LYS B 300 ? 2.1556 1.9911 1.7095 0.2079 -0.0628 0.1090 1119 LYS B N +4702 C CA . LYS B 300 ? 2.2607 2.0994 1.8097 0.2101 -0.0689 0.1051 1119 LYS B CA +4703 C C . LYS B 300 ? 2.7103 2.5439 2.2585 0.2128 -0.0731 0.1065 1119 LYS B C +4704 O O . LYS B 300 ? 2.6396 2.4752 2.1845 0.2145 -0.0785 0.1046 1119 LYS B O +4705 C CB . LYS B 300 ? 2.1877 2.0315 1.7311 0.2111 -0.0690 0.0971 1119 LYS B CB +4706 C CG . LYS B 300 ? 2.0533 1.9037 1.5959 0.2087 -0.0668 0.0946 1119 LYS B CG +4707 C CD . LYS B 300 ? 1.6597 1.5153 1.2003 0.2085 -0.0714 0.0938 1119 LYS B CD +4708 C CE . LYS B 300 ? 1.8858 1.7486 1.4237 0.2071 -0.0700 0.0890 1119 LYS B CE +4709 N NZ . LYS B 300 ? 2.1423 2.0099 1.6801 0.2058 -0.0729 0.0900 1119 LYS B NZ +4710 N N . LEU B 301 ? 2.9583 2.7854 2.5095 0.2133 -0.0708 0.1099 1120 LEU B N +4711 C CA . LEU B 301 ? 2.5954 2.4171 2.1466 0.2158 -0.0744 0.1121 1120 LEU B CA +4712 C C . LEU B 301 ? 2.5279 2.3471 2.0836 0.2148 -0.0760 0.1190 1120 LEU B C +4713 O O . LEU B 301 ? 2.1547 1.9678 1.7143 0.2148 -0.0747 0.1242 1120 LEU B O +4714 C CB . LEU B 301 ? 2.2179 2.0337 1.7704 0.2168 -0.0712 0.1126 1120 LEU B CB +4715 C CG . LEU B 301 ? 2.4502 2.2680 1.9984 0.2180 -0.0697 0.1057 1120 LEU B CG +4716 C CD1 . LEU B 301 ? 2.3945 2.2062 1.9441 0.2189 -0.0665 0.1065 1120 LEU B CD1 +4717 C CD2 . LEU B 301 ? 2.3200 2.1410 1.8620 0.2206 -0.0753 0.1000 1120 LEU B CD2 +4718 N N . VAL B 302 ? 2.8062 2.6301 2.3610 0.2140 -0.0790 0.1191 1121 VAL B N +4719 C CA . VAL B 302 ? 3.0226 2.8451 2.5813 0.2127 -0.0806 0.1254 1121 VAL B CA +4720 C C . VAL B 302 ? 3.0421 2.8689 2.5977 0.2137 -0.0866 0.1237 1121 VAL B C +4721 O O . VAL B 302 ? 3.1682 2.9920 2.7239 0.2153 -0.0908 0.1262 1121 VAL B O +4722 C CB . VAL B 302 ? 2.4903 2.3144 2.0537 0.2093 -0.0759 0.1292 1121 VAL B CB +4723 C CG1 . VAL B 302 ? 2.1817 2.0065 1.7481 0.2079 -0.0782 0.1344 1121 VAL B CG1 +4724 C CG2 . VAL B 302 ? 2.2211 2.0396 1.7890 0.2083 -0.0704 0.1329 1121 VAL B CG2 +4725 N N . LEU B 303 ? 2.7975 2.6311 2.3501 0.2128 -0.0870 0.1195 1122 LEU B N +4726 C CA . LEU B 303 ? 2.8758 2.7140 2.4255 0.2133 -0.0922 0.1179 1122 LEU B CA +4727 C C . LEU B 303 ? 2.8538 2.6908 2.3995 0.2165 -0.0980 0.1154 1122 LEU B C +4728 O O . LEU B 303 ? 2.6749 2.5126 2.2203 0.2171 -0.1025 0.1172 1122 LEU B O +4729 C CB . LEU B 303 ? 2.6988 2.5445 2.2453 0.2121 -0.0913 0.1126 1122 LEU B CB +4730 C CG . LEU B 303 ? 2.4902 2.3397 2.0397 0.2089 -0.0892 0.1155 1122 LEU B CG +4731 C CD1 . LEU B 303 ? 2.0109 1.8675 1.5568 0.2080 -0.0881 0.1095 1122 LEU B CD1 +4732 C CD2 . LEU B 303 ? 1.9161 1.7660 1.4671 0.2087 -0.0935 0.1196 1122 LEU B CD2 +4733 N N . SER C 5 ? 1.5094 0.9970 1.3600 0.1691 0.0431 0.0029 2 SER C N +4734 C CA . SER C 5 ? 2.1302 1.6148 1.9757 0.1695 0.0428 0.0044 2 SER C CA +4735 C C . SER C 5 ? 2.1262 1.6179 1.9799 0.1696 0.0423 0.0046 2 SER C C +4736 O O . SER C 5 ? 1.6794 1.1801 1.5449 0.1698 0.0415 0.0039 2 SER C O +4737 C CB . SER C 5 ? 2.0733 1.5576 1.9178 0.1713 0.0408 0.0057 2 SER C CB +4738 O OG . SER C 5 ? 2.0767 1.5694 1.9312 0.1735 0.0392 0.0062 2 SER C OG +4739 N N . LYS C 6 ? 2.0392 1.5266 1.8865 0.1693 0.0429 0.0056 3 LYS C N +4740 C CA . LYS C 6 ? 1.9516 1.4445 1.8049 0.1696 0.0425 0.0060 3 LYS C CA +4741 C C . LYS C 6 ? 2.0529 1.5485 1.9081 0.1727 0.0410 0.0075 3 LYS C C +4742 O O . LYS C 6 ? 1.9000 1.4016 1.7618 0.1739 0.0406 0.0079 3 LYS C O +4743 C CB . LYS C 6 ? 2.2726 1.7588 2.1170 0.1683 0.0440 0.0064 3 LYS C CB +4744 C CG . LYS C 6 ? 2.5651 2.0413 2.3976 0.1665 0.0465 0.0058 3 LYS C CG +4745 C CD . LYS C 6 ? 2.7111 2.1894 2.5475 0.1651 0.0478 0.0041 3 LYS C CD +4746 C CE . LYS C 6 ? 2.4230 1.8929 2.2499 0.1641 0.0493 0.0034 3 LYS C CE +4747 N NZ . LYS C 6 ? 2.0536 1.5260 1.8850 0.1630 0.0505 0.0017 3 LYS C NZ +4748 N N . GLY C 7 ? 2.0474 1.5385 1.8967 0.1739 0.0403 0.0083 4 GLY C N +4749 C CA . GLY C 7 ? 1.8621 1.3555 1.7129 0.1767 0.0389 0.0097 4 GLY C CA +4750 C C . GLY C 7 ? 1.7881 1.2902 1.6500 0.1782 0.0378 0.0093 4 GLY C C +4751 O O . GLY C 7 ? 1.6128 1.1196 1.4795 0.1802 0.0369 0.0102 4 GLY C O +4752 N N . GLU C 8 ? 1.5116 1.0156 1.3774 0.1771 0.0379 0.0080 5 GLU C N +4753 C CA . GLU C 8 ? 1.3927 0.9047 1.2691 0.1782 0.0369 0.0074 5 GLU C CA +4754 C C . GLU C 8 ? 1.4053 0.9249 1.2905 0.1788 0.0367 0.0074 5 GLU C C +4755 O O . GLU C 8 ? 1.7194 1.2455 1.6123 0.1806 0.0356 0.0076 5 GLU C O +4756 C CB . GLU C 8 ? 1.6521 1.1646 1.5308 0.1764 0.0374 0.0057 5 GLU C CB +4757 C CG . GLU C 8 ? 2.1945 1.7153 2.0843 0.1773 0.0365 0.0049 5 GLU C CG +4758 C CD . GLU C 8 ? 2.5037 2.0246 2.3939 0.1788 0.0353 0.0052 5 GLU C CD +4759 O OE1 . GLU C 8 ? 2.5887 2.1047 2.4738 0.1778 0.0356 0.0046 5 GLU C OE1 +4760 O OE2 . GLU C 8 ? 2.2493 1.7750 2.1448 0.1810 0.0340 0.0060 5 GLU C OE2 +4761 N N . GLU C 9 ? 1.4715 0.9902 1.3554 0.1773 0.0379 0.0071 6 GLU C N +4762 C CA . GLU C 9 ? 1.3619 0.8874 1.2537 0.1776 0.0378 0.0069 6 GLU C CA +4763 C C . GLU C 9 ? 1.5252 1.0526 1.4176 0.1799 0.0370 0.0085 6 GLU C C +4764 O O . GLU C 9 ? 1.5308 1.0646 1.4305 0.1805 0.0367 0.0085 6 GLU C O +4765 C CB . GLU C 9 ? 1.9494 1.4729 1.8391 0.1753 0.0393 0.0062 6 GLU C CB +4766 C CG . GLU C 9 ? 2.3299 1.8531 2.2210 0.1729 0.0402 0.0044 6 GLU C CG +4767 C CD . GLU C 9 ? 2.5123 2.0330 2.4006 0.1705 0.0417 0.0037 6 GLU C CD +4768 O OE1 . GLU C 9 ? 2.3883 1.9064 2.2722 0.1706 0.0422 0.0047 6 GLU C OE1 +4769 O OE2 . GLU C 9 ? 2.6045 2.1259 2.4951 0.1685 0.0425 0.0021 6 GLU C OE2 +4770 N N . LEU C 10 ? 1.4400 0.9619 1.3246 0.1810 0.0366 0.0098 7 LEU C N +4771 C CA . LEU C 10 ? 1.2520 0.7750 1.1363 0.1833 0.0358 0.0113 7 LEU C CA +4772 C C . LEU C 10 ? 1.5849 1.1129 1.4752 0.1856 0.0343 0.0118 7 LEU C C +4773 O O . LEU C 10 ? 1.3259 0.8566 1.2181 0.1875 0.0335 0.0128 7 LEU C O +4774 C CB . LEU C 10 ? 1.2596 0.7742 1.1325 0.1834 0.0362 0.0124 7 LEU C CB +4775 C CG . LEU C 10 ? 1.5241 1.0331 1.3902 0.1812 0.0377 0.0121 7 LEU C CG +4776 C CD1 . LEU C 10 ? 1.4343 0.9342 1.2886 0.1810 0.0379 0.0129 7 LEU C CD1 +4777 C CD2 . LEU C 10 ? 1.5410 1.0531 1.4098 0.1814 0.0380 0.0126 7 LEU C CD2 +4778 N N . PHE C 11 ? 1.6656 1.1949 1.5588 0.1853 0.0339 0.0109 8 PHE C N +4779 C CA . PHE C 11 ? 1.4113 0.9441 1.3087 0.1875 0.0324 0.0114 8 PHE C CA +4780 C C . PHE C 11 ? 1.3911 0.9324 1.2998 0.1877 0.0317 0.0104 8 PHE C C +4781 O O . PHE C 11 ? 1.4352 0.9799 1.3482 0.1893 0.0305 0.0107 8 PHE C O +4782 C CB . PHE C 11 ? 1.4817 1.0084 1.3721 0.1875 0.0321 0.0115 8 PHE C CB +4783 C CG . PHE C 11 ? 1.5439 1.0633 1.4240 0.1883 0.0322 0.0128 8 PHE C CG +4784 C CD1 . PHE C 11 ? 1.2449 0.7573 1.1163 0.1865 0.0334 0.0128 8 PHE C CD1 +4785 C CD2 . PHE C 11 ? 1.2720 0.7917 1.1513 0.1907 0.0310 0.0141 8 PHE C CD2 +4786 C CE1 . PHE C 11 ? 1.4450 0.9507 1.3069 0.1872 0.0334 0.0140 8 PHE C CE1 +4787 C CE2 . PHE C 11 ? 1.4248 0.9379 1.2948 0.1914 0.0309 0.0152 8 PHE C CE2 +4788 C CZ . PHE C 11 ? 1.4848 0.9908 1.3460 0.1897 0.0321 0.0152 8 PHE C CZ +4789 N N . THR C 12 ? 1.4826 1.0274 1.3962 0.1861 0.0325 0.0093 9 THR C N +4790 C CA . THR C 12 ? 1.6184 1.1720 1.5432 0.1865 0.0318 0.0086 9 THR C CA +4791 C C . THR C 12 ? 1.7067 1.2641 1.6346 0.1885 0.0310 0.0098 9 THR C C +4792 O O . THR C 12 ? 1.7597 1.3136 1.6821 0.1886 0.0315 0.0108 9 THR C O +4793 C CB . THR C 12 ? 0.9754 0.5316 0.9042 0.1844 0.0328 0.0071 9 THR C CB +4794 O OG1 . THR C 12 ? 1.4311 0.9879 1.3595 0.1843 0.0333 0.0077 9 THR C OG1 +4795 C CG2 . THR C 12 ? 1.1351 0.6852 1.0576 0.1822 0.0340 0.0062 9 THR C CG2 +4796 N N . GLY C 13 ? 1.2506 0.8149 1.1869 0.1900 0.0298 0.0099 10 GLY C N +4797 C CA . GLY C 13 ? 1.8032 1.3715 1.7430 0.1917 0.0290 0.0110 10 GLY C CA +4798 C C . GLY C 13 ? 0.9727 0.5369 0.9062 0.1936 0.0285 0.0126 10 GLY C C +4799 O O . GLY C 13 ? 1.2678 0.8249 1.1926 0.1933 0.0289 0.0130 10 GLY C O +4800 N N . VAL C 14 ? 1.1757 0.7443 1.1136 0.1955 0.0276 0.0135 11 VAL C N +4801 C CA . VAL C 14 ? 1.1404 0.7062 1.0736 0.1975 0.0269 0.0150 11 VAL C CA +4802 C C . VAL C 14 ? 1.2047 0.7639 1.1286 0.1973 0.0278 0.0159 11 VAL C C +4803 O O . VAL C 14 ? 1.2289 0.7892 1.1535 0.1969 0.0284 0.0160 11 VAL C O +4804 C CB . VAL C 14 ? 0.9300 0.5028 0.8710 0.1994 0.0257 0.0156 11 VAL C CB +4805 C CG1 . VAL C 14 ? 1.3915 0.9615 1.3279 0.2015 0.0250 0.0171 11 VAL C CG1 +4806 C CG2 . VAL C 14 ? 1.0600 0.6390 1.0099 0.1996 0.0247 0.0147 11 VAL C CG2 +4807 N N . VAL C 15 ? 1.1703 0.7225 1.0854 0.1977 0.0278 0.0165 12 VAL C N +4808 C CA . VAL C 15 ? 1.3430 0.8883 1.2485 0.1976 0.0286 0.0174 12 VAL C CA +4809 C C . VAL C 15 ? 1.3959 0.9402 1.2988 0.2000 0.0276 0.0188 12 VAL C C +4810 O O . VAL C 15 ? 1.1579 0.7023 1.0611 0.2014 0.0266 0.0191 12 VAL C O +4811 C CB . VAL C 15 ? 1.1336 0.6708 1.0299 0.1963 0.0292 0.0171 12 VAL C CB +4812 C CG1 . VAL C 15 ? 1.1600 0.6901 1.0463 0.1964 0.0298 0.0180 12 VAL C CG1 +4813 C CG2 . VAL C 15 ? 1.1007 0.6380 0.9986 0.1939 0.0302 0.0156 12 VAL C CG2 +4814 N N . PRO C 16 ? 1.1945 0.7376 1.0945 0.2006 0.0280 0.0196 13 PRO C N +4815 C CA . PRO C 16 ? 1.4425 0.9840 1.3391 0.2029 0.0272 0.0210 13 PRO C CA +4816 C C . PRO C 16 ? 1.1366 0.6695 1.0224 0.2031 0.0272 0.0215 13 PRO C C +4817 O O . PRO C 16 ? 1.2804 0.8074 1.1591 0.2015 0.0282 0.0213 13 PRO C O +4818 C CB . PRO C 16 ? 0.9392 0.4821 0.8362 0.2031 0.0277 0.0215 13 PRO C CB +4819 C CG . PRO C 16 ? 1.2596 0.8013 1.1557 0.2007 0.0291 0.0207 13 PRO C CG +4820 C CD . PRO C 16 ? 1.1158 0.6598 1.0165 0.1993 0.0291 0.0194 13 PRO C CD +4821 N N . ILE C 17 ? 1.2635 0.7959 1.1482 0.2051 0.0260 0.0223 14 ILE C N +4822 C CA . ILE C 17 ? 1.2549 0.7796 1.1299 0.2056 0.0257 0.0228 14 ILE C CA +4823 C C . ILE C 17 ? 1.1380 0.6603 1.0084 0.2077 0.0252 0.0241 14 ILE C C +4824 O O . ILE C 17 ? 1.0974 0.6248 0.9735 0.2095 0.0244 0.0247 14 ILE C O +4825 C CB . ILE C 17 ? 1.1879 0.7131 1.0646 0.2061 0.0248 0.0225 14 ILE C CB +4826 C CG1 . ILE C 17 ? 1.1595 0.6860 1.0395 0.2040 0.0254 0.0212 14 ILE C CG1 +4827 C CG2 . ILE C 17 ? 0.8765 0.3940 0.7433 0.2068 0.0244 0.0231 14 ILE C CG2 +4828 C CD1 . ILE C 17 ? 1.4233 0.9507 1.3055 0.2045 0.0244 0.0208 14 ILE C CD1 +4829 N N . LEU C 18 ? 1.0871 0.6015 0.9471 0.2075 0.0255 0.0246 15 LEU C N +4830 C CA . LEU C 18 ? 1.2982 0.8091 1.1524 0.2093 0.0251 0.0257 15 LEU C CA +4831 C C . LEU C 18 ? 1.3168 0.8200 1.1614 0.2096 0.0246 0.0260 15 LEU C C +4832 O O . LEU C 18 ? 1.0790 0.5767 0.9175 0.2079 0.0253 0.0255 15 LEU C O +4833 C CB . LEU C 18 ? 0.9169 0.4259 0.7676 0.2086 0.0261 0.0260 15 LEU C CB +4834 C CG . LEU C 18 ? 1.6164 1.1213 1.4604 0.2102 0.0259 0.0271 15 LEU C CG +4835 C CD1 . LEU C 18 ? 1.6757 1.1863 1.5259 0.2126 0.0248 0.0279 15 LEU C CD1 +4836 C CD2 . LEU C 18 ? 1.7544 1.2569 1.5947 0.2090 0.0272 0.0272 15 LEU C CD2 +4837 N N . VAL C 19 ? 1.2034 0.7061 1.0468 0.2119 0.0234 0.0269 16 VAL C N +4838 C CA . VAL C 19 ? 1.3513 0.8470 1.1861 0.2124 0.0228 0.0271 16 VAL C CA +4839 C C . VAL C 19 ? 1.3711 0.8626 1.1991 0.2144 0.0221 0.0283 16 VAL C C +4840 O O . VAL C 19 ? 1.2261 0.7218 1.0585 0.2164 0.0213 0.0289 16 VAL C O +4841 C CB . VAL C 19 ? 1.2315 0.7300 1.0708 0.2131 0.0217 0.0268 16 VAL C CB +4842 C CG1 . VAL C 19 ? 1.0951 0.5870 0.9261 0.2141 0.0208 0.0273 16 VAL C CG1 +4843 C CG2 . VAL C 19 ? 1.1806 0.6811 1.0240 0.2109 0.0224 0.0256 16 VAL C CG2 +4844 N N . GLU C 20 ? 1.3263 0.8095 1.1436 0.2138 0.0225 0.0284 17 GLU C N +4845 C CA . GLU C 20 ? 1.0510 0.5290 0.8605 0.2155 0.0219 0.0294 17 GLU C CA +4846 C C . GLU C 20 ? 1.4112 0.8821 1.2121 0.2159 0.0211 0.0295 17 GLU C C +4847 O O . GLU C 20 ? 1.3121 0.7774 1.1067 0.2140 0.0217 0.0291 17 GLU C O +4848 C CB . GLU C 20 ? 1.3340 0.8078 1.1373 0.2144 0.0231 0.0296 17 GLU C CB +4849 C CG . GLU C 20 ? 1.6619 1.1417 1.4722 0.2140 0.0239 0.0295 17 GLU C CG +4850 C CD . GLU C 20 ? 1.9081 1.3929 1.7236 0.2164 0.0232 0.0303 17 GLU C CD +4851 O OE1 . GLU C 20 ? 1.9115 1.3953 1.7252 0.2185 0.0220 0.0309 17 GLU C OE1 +4852 O OE2 . GLU C 20 ? 1.8852 1.3751 1.7065 0.2163 0.0237 0.0303 17 GLU C OE2 +4853 N N . LEU C 21 ? 1.1507 0.6217 0.9512 0.2182 0.0198 0.0302 18 LEU C N +4854 C CA . LEU C 21 ? 1.1771 0.6413 0.9693 0.2188 0.0189 0.0304 18 LEU C CA +4855 C C . LEU C 21 ? 1.2979 0.7573 1.0827 0.2207 0.0182 0.0314 18 LEU C C +4856 O O . LEU C 21 ? 1.5474 1.0107 1.3362 0.2227 0.0176 0.0320 18 LEU C O +4857 C CB . LEU C 21 ? 1.3996 0.8673 1.1972 0.2195 0.0178 0.0302 18 LEU C CB +4858 C CG . LEU C 21 ? 1.1270 0.5886 0.9173 0.2203 0.0167 0.0303 18 LEU C CG +4859 C CD1 . LEU C 21 ? 1.8442 1.2985 1.6260 0.2182 0.0174 0.0298 18 LEU C CD1 +4860 C CD2 . LEU C 21 ? 1.5511 1.0173 1.3482 0.2213 0.0156 0.0301 18 LEU C CD2 +4861 N N . ASP C 22 ? 1.3465 0.7974 1.1206 0.2202 0.0182 0.0314 19 ASP C N +4862 C CA . ASP C 22 ? 1.5994 1.0448 1.3654 0.2220 0.0173 0.0322 19 ASP C CA +4863 C C . ASP C 22 ? 1.4908 0.9316 1.2517 0.2227 0.0161 0.0322 19 ASP C C +4864 O O . ASP C 22 ? 1.4854 0.9210 1.2406 0.2210 0.0164 0.0317 19 ASP C O +4865 C CB . ASP C 22 ? 1.4396 0.8783 1.1964 0.2210 0.0182 0.0324 19 ASP C CB +4866 C CG . ASP C 22 ? 1.9096 1.3520 1.6699 0.2212 0.0191 0.0327 19 ASP C CG +4867 O OD1 . ASP C 22 ? 2.0128 1.4611 1.7801 0.2231 0.0185 0.0331 19 ASP C OD1 +4868 O OD2 . ASP C 22 ? 2.2872 1.7262 2.0430 0.2195 0.0203 0.0326 19 ASP C OD2 +4869 N N . GLY C 23 ? 1.4231 0.8656 1.1858 0.2251 0.0147 0.0328 20 GLY C N +4870 C CA . GLY C 23 ? 0.9723 0.4116 0.7317 0.2259 0.0134 0.0328 20 GLY C CA +4871 C C . GLY C 23 ? 1.6807 1.1143 1.4320 0.2278 0.0123 0.0335 20 GLY C C +4872 O O . GLY C 23 ? 1.6760 1.1099 1.4265 0.2294 0.0121 0.0341 20 GLY C O +4873 N N . ASP C 24 ? 1.7601 1.1883 1.5053 0.2278 0.0114 0.0333 21 ASP C N +4874 C CA . ASP C 24 ? 1.3177 0.7399 1.0548 0.2296 0.0102 0.0339 21 ASP C CA +4875 C C . ASP C 24 ? 1.4769 0.8978 1.2134 0.2300 0.0089 0.0337 21 ASP C C +4876 O O . ASP C 24 ? 1.5586 0.9748 1.2901 0.2282 0.0092 0.0332 21 ASP C O +4877 C CB . ASP C 24 ? 2.1643 1.5778 1.8899 0.2284 0.0108 0.0340 21 ASP C CB +4878 C CG . ASP C 24 ? 2.2948 1.7026 2.0123 0.2304 0.0096 0.0347 21 ASP C CG +4879 O OD1 . ASP C 24 ? 2.0041 1.4137 1.7238 0.2326 0.0082 0.0350 21 ASP C OD1 +4880 O OD2 . ASP C 24 ? 1.7664 1.1678 1.4751 0.2298 0.0101 0.0348 21 ASP C OD2 +4881 N N . VAL C 25 ? 1.4075 0.8322 1.1489 0.2323 0.0076 0.0341 22 VAL C N +4882 C CA . VAL C 25 ? 1.4224 0.8466 1.1642 0.2328 0.0063 0.0339 22 VAL C CA +4883 C C . VAL C 25 ? 1.5410 0.9618 1.2780 0.2353 0.0047 0.0346 22 VAL C C +4884 O O . VAL C 25 ? 1.3039 0.7296 1.0466 0.2375 0.0039 0.0351 22 VAL C O +4885 C CB . VAL C 25 ? 1.2086 0.6415 0.9623 0.2328 0.0063 0.0335 22 VAL C CB +4886 C CG1 . VAL C 25 ? 1.2856 0.7188 1.0405 0.2341 0.0047 0.0336 22 VAL C CG1 +4887 C CG2 . VAL C 25 ? 1.5140 0.9484 1.2704 0.2301 0.0076 0.0327 22 VAL C CG2 +4888 N N . ASN C 26 ? 1.4575 0.8701 1.1842 0.2350 0.0041 0.0345 23 ASN C N +4889 C CA . ASN C 26 ? 1.4156 0.8235 1.1359 0.2372 0.0026 0.0351 23 ASN C CA +4890 C C . ASN C 26 ? 1.7366 1.1447 1.4558 0.2387 0.0028 0.0358 23 ASN C C +4891 O O . ASN C 26 ? 1.4039 0.8143 1.1256 0.2411 0.0017 0.0363 23 ASN C O +4892 C CB . ASN C 26 ? 1.3549 0.7665 1.0806 0.2391 0.0011 0.0352 23 ASN C CB +4893 C CG . ASN C 26 ? 1.7164 1.1248 1.4394 0.2380 0.0005 0.0347 23 ASN C CG +4894 O OD1 . ASN C 26 ? 1.4209 0.8253 1.1393 0.2358 0.0014 0.0342 23 ASN C OD1 +4895 N ND2 . ASN C 26 ? 1.3945 0.8049 1.1205 0.2397 -0.0010 0.0349 23 ASN C ND2 +4896 N N . GLY C 27 ? 1.5041 0.9097 1.2195 0.2372 0.0042 0.0357 24 GLY C N +4897 C CA . GLY C 27 ? 1.5101 0.9157 1.2242 0.2382 0.0045 0.0362 24 GLY C CA +4898 C C . GLY C 27 ? 1.6355 1.0500 1.3603 0.2394 0.0048 0.0365 24 GLY C C +4899 O O . GLY C 27 ? 1.5415 0.9564 1.2657 0.2405 0.0050 0.0370 24 GLY C O +4900 N N . HIS C 28 ? 1.5167 0.9383 1.2514 0.2391 0.0048 0.0362 25 HIS C N +4901 C CA . HIS C 28 ? 1.6036 1.0339 1.3489 0.2396 0.0054 0.0363 25 HIS C CA +4902 C C . HIS C 28 ? 1.6902 1.1223 1.4378 0.2372 0.0071 0.0358 25 HIS C C +4903 O O . HIS C 28 ? 1.2529 0.6854 1.0021 0.2352 0.0077 0.0352 25 HIS C O +4904 C CB . HIS C 28 ? 1.0751 0.5123 0.8301 0.2403 0.0046 0.0361 25 HIS C CB +4905 C CG . HIS C 28 ? 1.8929 1.3299 1.6477 0.2428 0.0029 0.0366 25 HIS C CG +4906 N ND1 . HIS C 28 ? 1.6466 1.0776 1.3943 0.2432 0.0018 0.0366 25 HIS C ND1 +4907 C CD2 . HIS C 28 ? 1.8282 1.2702 1.5889 0.2451 0.0021 0.0372 25 HIS C CD2 +4908 C CE1 . HIS C 28 ? 1.5275 0.9598 1.2769 0.2456 0.0004 0.0371 25 HIS C CE1 +4909 N NE2 . HIS C 28 ? 1.9061 1.3452 1.6634 0.2467 0.0006 0.0374 25 HIS C NE2 +4910 N N . LYS C 29 ? 1.3109 0.7441 1.0588 0.2374 0.0079 0.0361 26 LYS C N +4911 C CA . LYS C 29 ? 1.3167 0.7519 1.0670 0.2352 0.0096 0.0357 26 LYS C CA +4912 C C . LYS C 29 ? 1.5860 1.0309 1.3487 0.2356 0.0098 0.0357 26 LYS C C +4913 O O . LYS C 29 ? 1.4802 0.9293 1.2481 0.2377 0.0088 0.0361 26 LYS C O +4914 C CB . LYS C 29 ? 1.4166 0.8474 1.1601 0.2351 0.0104 0.0361 26 LYS C CB +4915 C CG . LYS C 29 ? 1.2483 0.6692 0.9792 0.2346 0.0101 0.0361 26 LYS C CG +4916 C CD . LYS C 29 ? 1.8315 1.2483 1.5560 0.2346 0.0109 0.0365 26 LYS C CD +4917 C CE . LYS C 29 ? 1.6337 1.0407 1.3458 0.2336 0.0108 0.0364 26 LYS C CE +4918 N NZ . LYS C 29 ? 1.9508 1.3551 1.6604 0.2307 0.0119 0.0357 26 LYS C NZ +4919 N N . PHE C 30 ? 1.2492 0.6974 1.0164 0.2335 0.0111 0.0351 27 PHE C N +4920 C CA . PHE C 30 ? 1.1659 0.6232 0.9448 0.2336 0.0115 0.0350 27 PHE C CA +4921 C C . PHE C 30 ? 1.3188 0.7779 1.1001 0.2310 0.0131 0.0344 27 PHE C C +4922 O O . PHE C 30 ? 1.2906 0.7443 1.0657 0.2291 0.0138 0.0339 27 PHE C O +4923 C CB . PHE C 30 ? 1.4918 0.9543 1.2782 0.2343 0.0105 0.0348 27 PHE C CB +4924 C CG . PHE C 30 ? 1.4389 0.8993 1.2240 0.2325 0.0106 0.0341 27 PHE C CG +4925 C CD1 . PHE C 30 ? 1.4929 0.9463 1.2697 0.2328 0.0098 0.0341 27 PHE C CD1 +4926 C CD2 . PHE C 30 ? 1.4104 0.8754 1.2023 0.2307 0.0114 0.0334 27 PHE C CD2 +4927 C CE1 . PHE C 30 ? 1.4454 0.8967 1.2207 0.2312 0.0098 0.0334 27 PHE C CE1 +4928 C CE2 . PHE C 30 ? 1.4492 0.9121 1.2397 0.2291 0.0115 0.0327 27 PHE C CE2 +4929 C CZ . PHE C 30 ? 1.2825 0.7385 1.0647 0.2293 0.0107 0.0327 27 PHE C CZ +4930 N N . SER C 31 ? 1.3212 0.7876 1.1115 0.2311 0.0137 0.0344 28 SER C N +4931 C CA . SER C 31 ? 1.3402 0.8092 1.1342 0.2288 0.0151 0.0338 28 SER C CA +4932 C C . SER C 31 ? 1.3746 0.8528 1.1807 0.2286 0.0151 0.0334 28 SER C C +4933 O O . SER C 31 ? 1.1171 0.6006 0.9297 0.2305 0.0143 0.0338 28 SER C O +4934 C CB . SER C 31 ? 1.3398 0.8071 1.1304 0.2285 0.0161 0.0341 28 SER C CB +4935 O OG . SER C 31 ? 1.6698 1.1284 1.4490 0.2281 0.0163 0.0343 28 SER C OG +4936 N N . VAL C 32 ? 1.2273 0.7069 1.0363 0.2264 0.0160 0.0326 29 VAL C N +4937 C CA . VAL C 32 ? 1.3952 0.8832 1.2155 0.2259 0.0161 0.0321 29 VAL C CA +4938 C C . VAL C 32 ? 1.2304 0.7206 1.0536 0.2237 0.0176 0.0315 29 VAL C C +4939 O O . VAL C 32 ? 1.0254 0.5106 0.8428 0.2217 0.0185 0.0310 29 VAL C O +4940 C CB . VAL C 32 ? 1.1936 0.6826 1.0166 0.2255 0.0154 0.0315 29 VAL C CB +4941 C CG1 . VAL C 32 ? 1.2496 0.7476 1.0846 0.2252 0.0154 0.0311 29 VAL C CG1 +4942 C CG2 . VAL C 32 ? 0.9503 0.4366 0.7699 0.2275 0.0139 0.0321 29 VAL C CG2 +4943 N N . SER C 33 ? 1.1454 0.6430 0.9776 0.2240 0.0178 0.0315 30 SER C N +4944 C CA . SER C 33 ? 1.4438 0.9451 1.2810 0.2220 0.0191 0.0309 30 SER C CA +4945 C C . SER C 33 ? 1.4743 0.9833 1.3223 0.2216 0.0188 0.0302 30 SER C C +4946 O O . SER C 33 ? 1.1023 0.6167 0.9569 0.2233 0.0178 0.0306 30 SER C O +4947 C CB . SER C 33 ? 1.2000 0.7033 1.0383 0.2225 0.0197 0.0314 30 SER C CB +4948 O OG . SER C 33 ? 1.6386 1.1347 1.4671 0.2218 0.0204 0.0316 30 SER C OG +4949 N N . GLY C 34 ? 1.4821 0.9918 1.3319 0.2194 0.0197 0.0293 31 GLY C N +4950 C CA . GLY C 34 ? 0.8841 0.4007 0.7438 0.2188 0.0195 0.0286 31 GLY C CA +4951 C C . GLY C 34 ? 1.1714 0.6916 1.0358 0.2168 0.0207 0.0279 31 GLY C C +4952 O O . GLY C 34 ? 1.1241 0.6398 0.9830 0.2151 0.0218 0.0275 31 GLY C O +4953 N N . GLU C 35 ? 1.0328 0.5610 0.9074 0.2171 0.0205 0.0276 32 GLU C N +4954 C CA . GLU C 35 ? 1.3041 0.8365 1.1845 0.2152 0.0215 0.0268 32 GLU C CA +4955 C C . GLU C 35 ? 1.1771 0.7162 1.0672 0.2148 0.0210 0.0260 32 GLU C C +4956 O O . GLU C 35 ? 1.2513 0.7942 1.1463 0.2164 0.0198 0.0263 32 GLU C O +4957 C CB . GLU C 35 ? 1.1870 0.7226 1.0702 0.2156 0.0220 0.0272 32 GLU C CB +4958 C CG . GLU C 35 ? 1.3133 0.8557 1.2042 0.2175 0.0210 0.0278 32 GLU C CG +4959 C CD . GLU C 35 ? 2.3370 1.8791 2.2260 0.2186 0.0213 0.0287 32 GLU C CD +4960 O OE1 . GLU C 35 ? 2.3358 1.8745 2.2200 0.2175 0.0224 0.0286 32 GLU C OE1 +4961 O OE2 . GLU C 35 ? 2.8263 2.3715 2.7184 0.2206 0.0204 0.0294 32 GLU C OE2 +4962 N N . GLY C 36 ? 1.4265 0.9669 1.3192 0.2127 0.0218 0.0250 33 GLY C N +4963 C CA . GLY C 36 ? 1.0585 0.6057 0.9609 0.2120 0.0215 0.0241 33 GLY C CA +4964 C C . GLY C 36 ? 1.0523 0.5997 0.9558 0.2096 0.0227 0.0229 33 GLY C C +4965 O O . GLY C 36 ? 1.2303 0.7749 1.1298 0.2085 0.0238 0.0229 33 GLY C O +4966 N N . GLU C 37 ? 1.1595 0.7100 1.0684 0.2086 0.0225 0.0219 34 GLU C N +4967 C CA . GLU C 37 ? 1.1943 0.7459 1.1055 0.2063 0.0235 0.0207 34 GLU C CA +4968 C C . GLU C 37 ? 1.1404 0.6911 1.0522 0.2054 0.0233 0.0198 34 GLU C C +4969 O O . GLU C 37 ? 1.1285 0.6806 1.0424 0.2067 0.0222 0.0200 34 GLU C O +4970 C CB . GLU C 37 ? 1.1130 0.6728 1.0345 0.2061 0.0235 0.0202 34 GLU C CB +4971 C CG . GLU C 37 ? 1.9399 1.5064 1.8702 0.2074 0.0222 0.0201 34 GLU C CG +4972 C CD . GLU C 37 ? 1.8920 1.4666 1.8322 0.2073 0.0220 0.0197 34 GLU C CD +4973 O OE1 . GLU C 37 ? 1.9568 1.5321 1.8976 0.2059 0.0229 0.0193 34 GLU C OE1 +4974 O OE2 . GLU C 37 ? 1.8848 1.4649 1.8318 0.2086 0.0209 0.0199 34 GLU C OE2 +4975 N N . GLY C 38 ? 1.1118 0.6602 1.0216 0.2032 0.0244 0.0188 35 GLY C N +4976 C CA . GLY C 38 ? 1.2676 0.8145 1.1771 0.2021 0.0244 0.0178 35 GLY C CA +4977 C C . GLY C 38 ? 1.1654 0.7163 1.0812 0.2001 0.0251 0.0164 35 GLY C C +4978 O O . GLY C 38 ? 1.1686 0.7196 1.0843 0.1988 0.0261 0.0160 35 GLY C O +4979 N N . ASP C 39 ? 1.3031 0.8571 1.2240 0.2000 0.0245 0.0156 36 ASP C N +4980 C CA . ASP C 39 ? 1.2561 0.8144 1.1837 0.1982 0.0250 0.0141 36 ASP C CA +4981 C C . ASP C 39 ? 1.0137 0.5681 0.9379 0.1969 0.0254 0.0131 36 ASP C C +4982 O O . ASP C 39 ? 1.2591 0.8155 1.1867 0.1975 0.0245 0.0128 36 ASP C O +4983 C CB . ASP C 39 ? 1.2178 0.7849 1.1565 0.1993 0.0239 0.0138 36 ASP C CB +4984 C CG . ASP C 39 ? 1.7033 1.2761 1.6493 0.1981 0.0244 0.0129 36 ASP C CG +4985 O OD1 . ASP C 39 ? 1.7454 1.3156 1.6885 0.1961 0.0256 0.0121 36 ASP C OD1 +4986 O OD2 . ASP C 39 ? 1.5030 1.0829 1.4574 0.1990 0.0235 0.0129 36 ASP C OD2 +4987 N N . ALA C 40 ? 1.3225 0.8711 1.2399 0.1950 0.0267 0.0127 37 ALA C N +4988 C CA . ALA C 40 ? 1.1400 0.6840 1.0530 0.1936 0.0271 0.0118 37 ALA C CA +4989 C C . ALA C 40 ? 1.1214 0.6708 1.0427 0.1926 0.0270 0.0103 37 ALA C C +4990 O O . ALA C 40 ? 1.3009 0.8482 1.2207 0.1921 0.0269 0.0096 37 ALA C O +4991 C CB . ALA C 40 ? 0.8911 0.4281 0.7954 0.1917 0.0286 0.0116 37 ALA C CB +4992 N N . THR C 41 ? 1.3603 0.9165 1.2900 0.1923 0.0270 0.0097 38 THR C N +4993 C CA . THR C 41 ? 0.9701 0.5318 0.9079 0.1913 0.0270 0.0082 38 THR C CA +4994 C C . THR C 41 ? 1.2514 0.8167 1.1944 0.1927 0.0256 0.0081 38 THR C C +4995 O O . THR C 41 ? 1.2946 0.8611 1.2404 0.1918 0.0256 0.0069 38 THR C O +4996 C CB . THR C 41 ? 1.2016 0.7702 1.1475 0.1911 0.0270 0.0078 38 THR C CB +4997 O OG1 . THR C 41 ? 1.4024 0.9676 1.3434 0.1901 0.0282 0.0081 38 THR C OG1 +4998 C CG2 . THR C 41 ? 0.7782 0.3514 0.7312 0.1897 0.0271 0.0060 38 THR C CG2 +4999 N N . TYR C 42 ? 1.1331 0.7002 1.0773 0.1948 0.0245 0.0094 39 TYR C N +5000 C CA . TYR C 42 ? 1.2281 0.7983 1.1767 0.1963 0.0232 0.0095 39 TYR C CA +5001 C C . TYR C 42 ? 0.9206 0.4851 0.8615 0.1977 0.0227 0.0108 39 TYR C C +5002 O O . TYR C 42 ? 1.1217 0.6887 1.0657 0.1995 0.0214 0.0115 39 TYR C O +5003 C CB . TYR C 42 ? 0.9802 0.5588 0.9387 0.1977 0.0221 0.0097 39 TYR C CB +5004 C CG . TYR C 42 ? 1.1684 0.7520 1.1331 0.1964 0.0226 0.0087 39 TYR C CG +5005 C CD1 . TYR C 42 ? 1.1760 0.7640 1.1474 0.1952 0.0226 0.0072 39 TYR C CD1 +5006 C CD2 . TYR C 42 ? 1.3742 0.9580 1.3378 0.1963 0.0232 0.0093 39 TYR C CD2 +5007 C CE1 . TYR C 42 ? 1.1919 0.7844 1.1689 0.1941 0.0230 0.0062 39 TYR C CE1 +5008 C CE2 . TYR C 42 ? 1.5397 1.1278 1.5087 0.1952 0.0236 0.0084 39 TYR C CE2 +5009 C CZ . TYR C 42 ? 1.4327 1.0253 1.4085 0.1941 0.0235 0.0068 39 TYR C CZ +5010 O OH . TYR C 42 ? 1.2291 0.8259 1.2100 0.1929 0.0239 0.0058 39 TYR C OH +5011 N N . GLY C 43 ? 1.0986 0.6554 1.0297 0.1969 0.0236 0.0112 40 GLY C N +5012 C CA . GLY C 43 ? 1.2023 0.7525 1.1246 0.1980 0.0233 0.0123 40 GLY C CA +5013 C C . GLY C 43 ? 1.4055 0.9575 1.3289 0.2005 0.0220 0.0137 40 GLY C C +5014 O O . GLY C 43 ? 0.9933 0.5443 0.9156 0.2018 0.0210 0.0142 40 GLY C O +5015 N N . LYS C 44 ? 1.2500 0.8047 1.1755 0.2011 0.0221 0.0143 41 LYS C N +5016 C CA . LYS C 44 ? 0.8413 0.3997 0.7702 0.2034 0.0209 0.0155 41 LYS C CA +5017 C C . LYS C 44 ? 1.2118 0.7658 1.1336 0.2042 0.0212 0.0167 41 LYS C C +5018 O O . LYS C 44 ? 1.1826 0.7340 1.1007 0.2030 0.0223 0.0166 41 LYS C O +5019 C CB . LYS C 44 ? 1.0428 0.6101 0.9828 0.2035 0.0206 0.0150 41 LYS C CB +5020 C CG . LYS C 44 ? 1.3368 0.9088 1.2819 0.2057 0.0192 0.0159 41 LYS C CG +5021 C CD . LYS C 44 ? 1.0551 0.6351 1.0100 0.2057 0.0190 0.0155 41 LYS C CD +5022 C CE . LYS C 44 ? 1.6091 1.1918 1.5659 0.2077 0.0182 0.0168 41 LYS C CE +5023 N NZ . LYS C 44 ? 1.5403 1.1316 1.5079 0.2082 0.0174 0.0165 41 LYS C NZ +5024 N N . LEU C 45 ? 1.4766 1.0298 1.3966 0.2063 0.0202 0.0179 42 LEU C N +5025 C CA . LEU C 45 ? 1.2253 0.7737 1.1378 0.2073 0.0203 0.0191 42 LEU C CA +5026 C C . LEU C 45 ? 0.9715 0.5240 0.8880 0.2097 0.0191 0.0202 42 LEU C C +5027 O O . LEU C 45 ? 1.1982 0.7526 1.1175 0.2110 0.0180 0.0204 42 LEU C O +5028 C CB . LEU C 45 ? 1.0026 0.5425 0.9046 0.2072 0.0204 0.0194 42 LEU C CB +5029 C CG . LEU C 45 ? 1.2279 0.7605 1.1195 0.2073 0.0209 0.0203 42 LEU C CG +5030 C CD1 . LEU C 45 ? 1.6898 1.2207 1.5793 0.2053 0.0224 0.0197 42 LEU C CD1 +5031 C CD2 . LEU C 45 ? 1.1705 0.6956 1.0533 0.2072 0.0207 0.0204 42 LEU C CD2 +5032 N N . THR C 46 ? 1.2120 0.7656 1.1286 0.2103 0.0194 0.0209 43 THR C N +5033 C CA . THR C 46 ? 1.3243 0.8811 1.2437 0.2125 0.0184 0.0219 43 THR C CA +5034 C C . THR C 46 ? 1.0888 0.6401 0.9999 0.2133 0.0187 0.0230 43 THR C C +5035 O O . THR C 46 ? 1.2361 0.7862 1.1450 0.2122 0.0198 0.0229 43 THR C O +5036 C CB . THR C 46 ? 1.0679 0.6331 0.9976 0.2127 0.0182 0.0218 43 THR C CB +5037 O OG1 . THR C 46 ? 1.7615 1.3264 1.6900 0.2117 0.0193 0.0217 43 THR C OG1 +5038 C CG2 . THR C 46 ? 1.2765 0.8475 1.2148 0.2118 0.0179 0.0206 43 THR C CG2 +5039 N N . LEU C 47 ? 1.1298 0.6781 1.0365 0.2151 0.0178 0.0239 44 LEU C N +5040 C CA . LEU C 47 ? 1.1071 0.6497 1.0052 0.2159 0.0181 0.0249 44 LEU C CA +5041 C C . LEU C 47 ? 1.1754 0.7193 1.0743 0.2184 0.0169 0.0260 44 LEU C C +5042 O O . LEU C 47 ? 0.8618 0.4076 0.7636 0.2196 0.0158 0.0261 44 LEU C O +5043 C CB . LEU C 47 ? 0.9692 0.5031 0.8568 0.2151 0.0185 0.0248 44 LEU C CB +5044 C CG . LEU C 47 ? 1.3476 0.8784 1.2320 0.2126 0.0199 0.0239 44 LEU C CG +5045 C CD1 . LEU C 47 ? 1.2656 0.7880 1.1400 0.2118 0.0201 0.0238 44 LEU C CD1 +5046 C CD2 . LEU C 47 ? 1.0835 0.6138 0.9661 0.2120 0.0209 0.0242 44 LEU C CD2 +5047 N N . LYS C 48 ? 0.9965 0.5397 0.8930 0.2193 0.0172 0.0268 45 LYS C N +5048 C CA . LYS C 48 ? 0.9178 0.4612 0.8135 0.2217 0.0162 0.0278 45 LYS C CA +5049 C C . LYS C 48 ? 1.2923 0.8279 1.1771 0.2223 0.0164 0.0286 45 LYS C C +5050 O O . LYS C 48 ? 1.0015 0.5338 0.8815 0.2213 0.0175 0.0286 45 LYS C O +5051 C CB . LYS C 48 ? 0.9970 0.5473 0.9005 0.2225 0.0161 0.0282 45 LYS C CB +5052 C CG . LYS C 48 ? 0.9376 0.4896 0.8425 0.2250 0.0149 0.0292 45 LYS C CG +5053 C CD . LYS C 48 ? 1.0957 0.6521 1.0048 0.2258 0.0151 0.0297 45 LYS C CD +5054 C CE . LYS C 48 ? 1.3546 0.9146 1.2679 0.2281 0.0139 0.0304 45 LYS C CE +5055 N NZ . LYS C 48 ? 0.9847 0.5479 0.9006 0.2289 0.0141 0.0310 45 LYS C NZ +5056 N N . PHE C 49 ? 1.3190 0.8518 1.2002 0.2241 0.0153 0.0292 46 PHE C N +5057 C CA . PHE C 49 ? 1.2280 0.7530 1.0985 0.2248 0.0153 0.0299 46 PHE C CA +5058 C C . PHE C 49 ? 1.0520 0.5780 0.9226 0.2272 0.0145 0.0309 46 PHE C C +5059 O O . PHE C 49 ? 1.0987 0.6287 0.9745 0.2287 0.0134 0.0312 46 PHE C O +5060 C CB . PHE C 49 ? 1.2317 0.7510 1.0960 0.2246 0.0148 0.0297 46 PHE C CB +5061 C CG . PHE C 49 ? 1.2055 0.7231 1.0688 0.2221 0.0157 0.0287 46 PHE C CG +5062 C CD1 . PHE C 49 ? 1.1814 0.6934 1.0375 0.2205 0.0169 0.0284 46 PHE C CD1 +5063 C CD2 . PHE C 49 ? 1.1049 0.6266 0.9748 0.2214 0.0154 0.0279 46 PHE C CD2 +5064 C CE1 . PHE C 49 ? 1.1005 0.6110 0.9558 0.2182 0.0178 0.0275 46 PHE C CE1 +5065 C CE2 . PHE C 49 ? 1.2180 0.7381 1.0869 0.2192 0.0163 0.0269 46 PHE C CE2 +5066 C CZ . PHE C 49 ? 1.1433 0.6578 1.0050 0.2176 0.0175 0.0267 46 PHE C CZ +5067 N N . ILE C 50 ? 1.3201 0.8426 1.1850 0.2275 0.0151 0.0315 47 ILE C N +5068 C CA . ILE C 50 ? 1.0970 0.6190 0.9600 0.2297 0.0144 0.0324 47 ILE C CA +5069 C C . ILE C 50 ? 1.4570 0.9703 1.3086 0.2303 0.0141 0.0329 47 ILE C C +5070 O O . ILE C 50 ? 1.2022 0.7096 1.0465 0.2289 0.0150 0.0326 47 ILE C O +5071 C CB . ILE C 50 ? 1.2245 0.7487 1.0891 0.2297 0.0153 0.0327 47 ILE C CB +5072 C CG1 . ILE C 50 ? 1.4173 0.9495 1.2922 0.2286 0.0158 0.0322 47 ILE C CG1 +5073 C CG2 . ILE C 50 ? 1.5621 1.0866 1.4258 0.2321 0.0146 0.0337 47 ILE C CG2 +5074 C CD1 . ILE C 50 ? 1.5112 1.0507 1.3953 0.2302 0.0147 0.0325 47 ILE C CD1 +5075 N N . CYS C 51 ? 1.5697 1.0819 1.4197 0.2324 0.0129 0.0335 48 CYS C N +5076 C CA . CYS C 51 ? 1.6428 1.1471 1.4822 0.2334 0.0126 0.0341 48 CYS C CA +5077 C C . CYS C 51 ? 1.4782 0.9819 1.3152 0.2342 0.0131 0.0347 48 CYS C C +5078 O O . CYS C 51 ? 1.5491 1.0573 1.3911 0.2359 0.0126 0.0352 48 CYS C O +5079 C CB . CYS C 51 ? 1.8423 1.3455 1.6805 0.2354 0.0111 0.0345 48 CYS C CB +5080 S SG . CYS C 51 ? 1.4350 0.9277 1.2596 0.2360 0.0107 0.0349 48 CYS C SG +5081 N N . THR C 52 ? 1.3966 0.8946 1.2260 0.2330 0.0142 0.0346 49 THR C N +5082 C CA . THR C 52 ? 1.3279 0.8248 1.1544 0.2335 0.0148 0.0352 49 THR C CA +5083 C C . THR C 52 ? 1.2849 0.7765 1.1038 0.2356 0.0140 0.0359 49 THR C C +5084 O O . THR C 52 ? 1.5097 1.0006 1.3265 0.2364 0.0143 0.0365 49 THR C O +5085 C CB . THR C 52 ? 1.3315 0.8245 1.1529 0.2313 0.0163 0.0348 49 THR C CB +5086 O OG1 . THR C 52 ? 1.2251 0.7116 1.0391 0.2300 0.0164 0.0343 49 THR C OG1 +5087 C CG2 . THR C 52 ? 1.1215 0.6208 0.9513 0.2296 0.0172 0.0342 49 THR C CG2 +5088 N N . THR C 53 ? 1.5564 1.0443 1.3713 0.2364 0.0129 0.0360 50 THR C N +5089 C CA . THR C 53 ? 0.9534 0.4359 0.7607 0.2383 0.0120 0.0367 50 THR C CA +5090 C C . THR C 53 ? 1.3553 0.8410 1.1670 0.2406 0.0105 0.0371 50 THR C C +5091 O O . THR C 53 ? 1.8138 1.2948 1.6195 0.2419 0.0095 0.0374 50 THR C O +5092 C CB . THR C 53 ? 1.2850 0.7585 1.0814 0.2375 0.0119 0.0365 50 THR C CB +5093 O OG1 . THR C 53 ? 1.3545 0.8283 1.1525 0.2371 0.0111 0.0360 50 THR C OG1 +5094 C CG2 . THR C 53 ? 0.9993 0.4693 0.7913 0.2351 0.0133 0.0360 50 THR C CG2 +5095 N N . GLY C 54 ? 1.1254 0.6193 0.9475 0.2412 0.0103 0.0371 51 GLY C N +5096 C CA . GLY C 54 ? 1.3474 0.8448 1.1742 0.2433 0.0090 0.0375 51 GLY C CA +5097 C C . GLY C 54 ? 1.0170 0.5165 0.8479 0.2427 0.0083 0.0370 51 GLY C C +5098 O O . GLY C 54 ? 2.1722 1.6747 2.0076 0.2408 0.0090 0.0363 51 GLY C O +5099 N N . LYS C 55 ? 1.5024 1.0005 1.3319 0.2443 0.0069 0.0373 52 LYS C N +5100 C CA . LYS C 55 ? 1.3606 0.8592 1.1922 0.2439 0.0062 0.0368 52 LYS C CA +5101 C C . LYS C 55 ? 1.3606 0.8525 1.1843 0.2421 0.0066 0.0363 52 LYS C C +5102 O O . LYS C 55 ? 1.2520 0.7371 1.0664 0.2418 0.0070 0.0364 52 LYS C O +5103 C CB . LYS C 55 ? 0.9160 0.4145 0.7478 0.2461 0.0046 0.0373 52 LYS C CB +5104 C CG . LYS C 55 ? 1.7445 1.2515 1.5874 0.2471 0.0040 0.0374 52 LYS C CG +5105 C CD . LYS C 55 ? 2.3304 1.8373 2.1739 0.2490 0.0024 0.0377 52 LYS C CD +5106 C CE . LYS C 55 ? 2.4604 1.9735 2.3114 0.2509 0.0018 0.0383 52 LYS C CE +5107 N NZ . LYS C 55 ? 2.2523 1.7653 2.1037 0.2529 0.0002 0.0386 52 LYS C NZ +5108 N N . LEU C 56 ? 1.5407 1.0343 1.3679 0.2410 0.0064 0.0357 53 LEU C N +5109 C CA . LEU C 56 ? 1.3751 0.8628 1.1956 0.2392 0.0068 0.0351 53 LEU C CA +5110 C C . LEU C 56 ? 1.1753 0.6576 0.9893 0.2405 0.0054 0.0353 53 LEU C C +5111 O O . LEU C 56 ? 1.3096 0.7949 1.1278 0.2422 0.0042 0.0356 53 LEU C O +5112 C CB . LEU C 56 ? 1.1995 0.6919 1.0271 0.2374 0.0073 0.0343 53 LEU C CB +5113 C CG . LEU C 56 ? 1.3822 0.8699 1.2045 0.2349 0.0083 0.0335 53 LEU C CG +5114 C CD1 . LEU C 56 ? 1.1115 0.5983 0.9321 0.2334 0.0098 0.0334 53 LEU C CD1 +5115 C CD2 . LEU C 56 ? 0.9144 0.4062 0.7434 0.2337 0.0082 0.0328 53 LEU C CD2 +5116 N N . PRO C 57 ? 1.4712 0.9451 1.2745 0.2398 0.0056 0.0353 54 PRO C N +5117 C CA . PRO C 57 ? 1.2149 0.6834 1.0117 0.2410 0.0043 0.0355 54 PRO C CA +5118 C C . PRO C 57 ? 1.4213 0.8903 1.2201 0.2402 0.0037 0.0349 54 PRO C C +5119 O O . PRO C 57 ? 1.3174 0.7846 1.1144 0.2415 0.0024 0.0351 54 PRO C O +5120 C CB . PRO C 57 ? 1.1817 0.6414 0.9667 0.2402 0.0048 0.0355 54 PRO C CB +5121 C CG . PRO C 57 ? 1.2934 0.7537 1.0792 0.2379 0.0064 0.0350 54 PRO C CG +5122 C CD . PRO C 57 ? 1.3499 0.8191 1.1467 0.2381 0.0069 0.0351 54 PRO C CD +5123 N N . VAL C 58 ? 1.4424 0.9138 1.2451 0.2380 0.0048 0.0342 55 VAL C N +5124 C CA . VAL C 58 ? 1.4467 0.9187 1.2516 0.2370 0.0045 0.0335 55 VAL C CA +5125 C C . VAL C 58 ? 1.5104 0.9917 1.3277 0.2370 0.0044 0.0333 55 VAL C C +5126 O O . VAL C 58 ? 1.2232 0.7100 1.0468 0.2375 0.0049 0.0335 55 VAL C O +5127 C CB . VAL C 58 ? 1.2349 0.7020 1.0340 0.2344 0.0056 0.0328 55 VAL C CB +5128 C CG1 . VAL C 58 ? 1.3980 0.8558 1.1850 0.2345 0.0052 0.0331 55 VAL C CG1 +5129 C CG2 . VAL C 58 ? 1.3823 0.8514 1.1833 0.2331 0.0072 0.0327 55 VAL C CG2 +5130 N N . PRO C 59 ? 1.4580 0.9411 1.2789 0.2366 0.0039 0.0328 56 PRO C N +5131 C CA . PRO C 59 ? 1.4663 0.9583 1.2990 0.2364 0.0040 0.0325 56 PRO C CA +5132 C C . PRO C 59 ? 1.5931 1.0873 1.4287 0.2341 0.0056 0.0317 56 PRO C C +5133 O O . PRO C 59 ? 1.2774 0.7660 1.1062 0.2324 0.0064 0.0313 56 PRO C O +5134 C CB . PRO C 59 ? 1.2558 0.7484 1.0906 0.2366 0.0030 0.0321 56 PRO C CB +5135 C CG . PRO C 59 ? 1.2656 0.7496 1.0896 0.2366 0.0025 0.0322 56 PRO C CG +5136 C CD . PRO C 59 ? 1.3752 0.8532 1.1906 0.2359 0.0034 0.0324 56 PRO C CD +5137 N N . TRP C 60 ? 1.3947 0.8966 1.2401 0.2339 0.0060 0.0316 57 TRP C N +5138 C CA . TRP C 60 ? 0.9941 0.4984 0.8427 0.2317 0.0074 0.0309 57 TRP C CA +5139 C C . TRP C 60 ? 1.1328 0.6352 0.9804 0.2297 0.0079 0.0300 57 TRP C C +5140 O O . TRP C 60 ? 0.9948 0.4935 0.8379 0.2278 0.0090 0.0295 57 TRP C O +5141 C CB . TRP C 60 ? 1.1612 0.6745 1.0211 0.2319 0.0077 0.0309 57 TRP C CB +5142 C CG . TRP C 60 ? 1.3223 0.8367 1.1821 0.2329 0.0080 0.0316 57 TRP C CG +5143 C CD1 . TRP C 60 ? 1.0425 0.5605 0.9061 0.2350 0.0072 0.0323 57 TRP C CD1 +5144 C CD2 . TRP C 60 ? 1.2711 0.7830 1.1268 0.2317 0.0093 0.0315 57 TRP C CD2 +5145 N NE1 . TRP C 60 ? 1.0998 0.6176 0.9619 0.2353 0.0079 0.0328 57 TRP C NE1 +5146 C CE2 . TRP C 60 ? 1.1197 0.6338 0.9770 0.2333 0.0091 0.0323 57 TRP C CE2 +5147 C CE3 . TRP C 60 ? 1.1960 0.7040 1.0470 0.2295 0.0105 0.0309 57 TRP C CE3 +5148 C CZ2 . TRP C 60 ? 1.0721 0.5847 0.9264 0.2327 0.0102 0.0325 57 TRP C CZ2 +5149 C CZ3 . TRP C 60 ? 1.2130 0.7195 1.0611 0.2289 0.0116 0.0311 57 TRP C CZ3 +5150 C CH2 . TRP C 60 ? 1.1867 0.6955 1.0364 0.2305 0.0114 0.0319 57 TRP C CH2 +5151 N N . PRO C 61 ? 1.3424 0.8470 1.1940 0.2301 0.0069 0.0297 58 PRO C N +5152 C CA . PRO C 61 ? 0.8637 0.3670 0.7149 0.2283 0.0073 0.0288 58 PRO C CA +5153 C C . PRO C 61 ? 1.1210 0.6155 0.9612 0.2268 0.0079 0.0285 58 PRO C C +5154 O O . PRO C 61 ? 1.3081 0.8018 1.1482 0.2247 0.0089 0.0276 58 PRO C O +5155 C CB . PRO C 61 ? 1.2447 0.7497 1.0990 0.2296 0.0059 0.0288 58 PRO C CB +5156 C CG . PRO C 61 ? 1.2073 0.7189 1.0693 0.2315 0.0052 0.0295 58 PRO C CG +5157 C CD . PRO C 61 ? 1.0318 0.5410 0.8893 0.2322 0.0055 0.0302 58 PRO C CD +5158 N N . THR C 62 ? 1.2777 0.7657 1.1089 0.2279 0.0074 0.0292 59 THR C N +5159 C CA . THR C 62 ? 1.3670 0.8464 1.1873 0.2266 0.0079 0.0290 59 THR C CA +5160 C C . THR C 62 ? 1.3586 0.8363 1.1764 0.2246 0.0096 0.0286 59 THR C C +5161 O O . THR C 62 ? 1.2824 0.7535 1.0922 0.2230 0.0102 0.0283 59 THR C O +5162 C CB . THR C 62 ? 1.4187 0.8920 1.2303 0.2284 0.0070 0.0299 59 THR C CB +5163 O OG1 . THR C 62 ? 1.3159 0.7920 1.1297 0.2296 0.0071 0.0305 59 THR C OG1 +5164 C CG2 . THR C 62 ? 1.2399 0.7133 1.0521 0.2302 0.0054 0.0302 59 THR C CG2 +5165 N N . LEU C 63 ? 1.2679 0.7514 1.0926 0.2246 0.0102 0.0287 60 LEU C N +5166 C CA . LEU C 63 ? 1.0087 0.4907 0.8309 0.2229 0.0117 0.0285 60 LEU C CA +5167 C C . LEU C 63 ? 1.4426 0.9296 1.2720 0.2209 0.0129 0.0275 60 LEU C C +5168 O O . LEU C 63 ? 1.0914 0.5765 0.9183 0.2191 0.0142 0.0272 60 LEU C O +5169 C CB . LEU C 63 ? 1.2538 0.7376 1.0767 0.2244 0.0117 0.0293 60 LEU C CB +5170 C CG . LEU C 63 ? 1.3981 0.8753 1.2117 0.2259 0.0110 0.0302 60 LEU C CG +5171 C CD1 . LEU C 63 ? 1.2702 0.7500 1.0857 0.2272 0.0112 0.0309 60 LEU C CD1 +5172 C CD2 . LEU C 63 ? 1.0491 0.5176 0.8518 0.2243 0.0118 0.0299 60 LEU C CD2 +5173 N N . VAL C 64 ? 1.3026 0.7958 1.1408 0.2211 0.0123 0.0271 61 VAL C N +5174 C CA . VAL C 64 ? 1.0758 0.5746 0.9219 0.2193 0.0133 0.0262 61 VAL C CA +5175 C C . VAL C 64 ? 1.1137 0.6077 0.9545 0.2167 0.0146 0.0253 61 VAL C C +5176 O O . VAL C 64 ? 1.1605 0.6566 1.0039 0.2152 0.0158 0.0249 61 VAL C O +5177 C CB . VAL C 64 ? 1.1357 0.6400 0.9900 0.2197 0.0124 0.0257 61 VAL C CB +5178 C CG1 . VAL C 64 ? 0.7944 0.3031 0.6554 0.2177 0.0134 0.0246 61 VAL C CG1 +5179 C CG2 . VAL C 64 ? 0.9428 0.4534 0.8044 0.2220 0.0113 0.0264 61 VAL C CG2 +5180 N N . THR C 65 ? 1.2860 0.7734 1.1191 0.2162 0.0144 0.0252 62 THR C N +5181 C CA . THR C 65 ? 1.2760 0.7591 1.1046 0.2137 0.0156 0.0243 62 THR C CA +5182 C C . THR C 65 ? 1.1188 0.5966 0.9397 0.2127 0.0166 0.0245 62 THR C C +5183 O O . THR C 65 ? 1.4475 0.9231 1.2662 0.2104 0.0179 0.0238 62 THR C O +5184 C CB . THR C 65 ? 1.3843 0.8616 1.2065 0.2134 0.0150 0.0240 62 THR C CB +5185 O OG1 . THR C 65 ? 1.6845 1.1540 1.4958 0.2140 0.0147 0.0248 62 THR C OG1 +5186 C CG2 . THR C 65 ? 1.2348 0.7163 1.0627 0.2151 0.0136 0.0242 62 THR C CG2 +5187 N N . THR C 66 ? 1.3488 0.8243 1.1655 0.2144 0.0161 0.0255 63 THR C N +5188 C CA . THR C 66 ? 1.3339 0.8036 1.1423 0.2136 0.0170 0.0259 63 THR C CA +5189 C C . THR C 66 ? 1.3493 0.8243 1.1639 0.2129 0.0180 0.0257 63 THR C C +5190 O O . THR C 66 ? 1.2594 0.7317 1.0705 0.2110 0.0193 0.0254 63 THR C O +5191 C CB . THR C 66 ? 1.3768 0.8424 1.1787 0.2158 0.0160 0.0270 63 THR C CB +5192 O OG1 . THR C 66 ? 1.2859 0.7489 1.0850 0.2170 0.0146 0.0272 63 THR C OG1 +5193 C CG2 . THR C 66 ? 1.1277 0.5856 0.9191 0.2148 0.0168 0.0272 63 THR C CG2 +5194 N N . PHE C 67 ? 1.4722 0.9548 1.2961 0.2145 0.0174 0.0260 64 PHE C N +5195 C CA . PHE C 67 ? 1.3123 0.8014 1.1439 0.2143 0.0181 0.0259 64 PHE C CA +5196 C C . PHE C 67 ? 1.1712 0.6651 1.0100 0.2122 0.0191 0.0248 64 PHE C C +5197 O O . PHE C 67 ? 1.3881 0.8815 1.2261 0.2104 0.0204 0.0244 64 PHE C O +5198 C CB . PHE C 67 ? 1.3682 0.8645 1.2082 0.2165 0.0170 0.0265 64 PHE C CB +5199 C CG . PHE C 67 ? 1.0502 0.5444 0.8862 0.2188 0.0161 0.0277 64 PHE C CG +5200 C CD1 . PHE C 67 ? 1.1313 0.6194 0.9585 0.2188 0.0166 0.0282 64 PHE C CD1 +5201 C CD2 . PHE C 67 ? 1.2977 0.7964 1.1393 0.2210 0.0148 0.0281 64 PHE C CD2 +5202 C CE1 . PHE C 67 ? 1.1945 0.6811 1.0186 0.2210 0.0157 0.0292 64 PHE C CE1 +5203 C CE2 . PHE C 67 ? 1.2601 0.7574 1.0986 0.2231 0.0140 0.0291 64 PHE C CE2 +5204 C CZ . PHE C 67 ? 1.1768 0.6679 1.0065 0.2232 0.0144 0.0296 64 PHE C CZ +5205 N N1 . CR2 C 68 ? 1.3621 0.8607 1.2079 0.2123 0.0185 0.0243 65 CR2 C N1 +5206 C CA1 . CR2 C 68 ? 1.3442 0.8452 1.1946 0.2100 0.0194 0.0230 65 CR2 C CA1 +5207 C C1 . CR2 C 68 ? 1.4556 0.9505 1.2996 0.2086 0.0195 0.0223 65 CR2 C C1 +5208 N N2 . CR2 C 68 ? 1.4893 0.9850 1.3353 0.2088 0.0187 0.0219 65 CR2 C N2 +5209 N N3 . CR2 C 68 ? 1.1411 0.6290 0.9763 0.2069 0.0205 0.0221 65 CR2 C N3 +5210 C C2 . CR2 C 68 ? 1.3135 0.7973 1.1446 0.2060 0.0204 0.0216 65 CR2 C C2 +5211 O O2 . CR2 C 68 ? 1.1980 0.6747 1.0205 0.2043 0.0212 0.0212 65 CR2 C O2 +5212 C CA2 . CR2 C 68 ? 1.3875 0.8763 1.2256 0.2073 0.0192 0.0214 65 CR2 C CA2 +5213 C CA3 . CR2 C 68 ? 0.8314 0.3157 0.6611 0.2062 0.0215 0.0225 65 CR2 C CA3 +5214 C C3 . CR2 C 68 ? 1.3678 0.8549 1.2013 0.2041 0.0229 0.0217 65 CR2 C C3 +5215 O O3 . CR2 C 68 ? 1.2092 0.6897 1.0345 0.2022 0.0242 0.0214 65 CR2 C O3 +5216 C CB2 . CR2 C 68 ? 1.2799 0.7672 1.1173 0.2071 0.0186 0.0209 65 CR2 C CB2 +5217 C CG2 . CR2 C 68 ? 1.4463 0.9391 1.2913 0.2086 0.0174 0.0209 65 CR2 C CG2 +5218 C CD1 . CR2 C 68 ? 1.1025 0.6023 0.9557 0.2104 0.0166 0.0214 65 CR2 C CD1 +5219 C CD2 . CR2 C 68 ? 1.3640 0.8543 1.2071 0.2081 0.0170 0.0203 65 CR2 C CD2 +5220 C CE1 . CR2 C 68 ? 1.4262 0.9307 1.2860 0.2117 0.0154 0.0213 65 CR2 C CE1 +5221 C CE2 . CR2 C 68 ? 1.1798 0.6747 1.0293 0.2095 0.0158 0.0203 65 CR2 C CE2 +5222 C CZ . CR2 C 68 ? 1.3958 0.8978 1.2538 0.2112 0.0150 0.0208 65 CR2 C CZ +5223 O OH . CR2 C 68 ? 1.3605 0.8671 1.2249 0.2125 0.0138 0.0207 65 CR2 C OH +5224 N N . VAL C 69 ? 1.5605 1.0551 1.4043 0.2038 0.0230 0.0209 68 VAL C N +5225 C CA . VAL C 69 ? 1.4099 0.9067 1.2568 0.2018 0.0243 0.0201 68 VAL C CA +5226 C C . VAL C 69 ? 1.0232 0.5217 0.8739 0.1999 0.0249 0.0188 68 VAL C C +5227 O O . VAL C 69 ? 1.5785 1.0822 1.4362 0.1988 0.0256 0.0181 68 VAL C O +5228 C CB . VAL C 69 ? 1.1602 0.6609 1.0109 0.2021 0.0248 0.0205 68 VAL C CB +5229 C CG1 . VAL C 69 ? 1.1628 0.6572 1.0042 0.2026 0.0250 0.0215 68 VAL C CG1 +5230 C CG2 . VAL C 69 ? 1.8419 1.3511 1.7027 0.2039 0.0239 0.0209 68 VAL C CG2 +5231 N N . GLN C 70 ? 1.4455 0.9387 1.2905 0.1993 0.0248 0.0185 69 GLN C N +5232 C CA . GLN C 70 ? 1.3984 0.8928 1.2465 0.1976 0.0252 0.0172 69 GLN C CA +5233 C C . GLN C 70 ? 1.2619 0.7576 1.1125 0.1951 0.0267 0.0161 69 GLN C C +5234 O O . GLN C 70 ? 1.7348 1.2302 1.5865 0.1935 0.0272 0.0149 69 GLN C O +5235 C CB . GLN C 70 ? 1.3157 0.8026 1.1550 0.1972 0.0250 0.0172 69 GLN C CB +5236 C CG . GLN C 70 ? 1.6528 1.1397 1.4919 0.1995 0.0233 0.0179 69 GLN C CG +5237 C CD . GLN C 70 ? 1.6783 1.1567 1.5070 0.1992 0.0231 0.0181 69 GLN C CD +5238 O OE1 . GLN C 70 ? 1.5561 1.0281 1.3768 0.1974 0.0241 0.0178 69 GLN C OE1 +5239 N NE2 . GLN C 70 ? 1.6619 1.1403 1.4907 0.2009 0.0217 0.0185 69 GLN C NE2 +5240 N N . CYS C 71 ? 1.4391 0.9363 1.2908 0.1948 0.0274 0.0163 70 CYS C N +5241 C CA . CYS C 71 ? 1.3091 0.8086 1.1643 0.1926 0.0287 0.0152 70 CYS C CA +5242 C C . CYS C 71 ? 1.4318 0.9409 1.2993 0.1932 0.0284 0.0148 70 CYS C C +5243 O O . CYS C 71 ? 1.2970 0.8094 1.1691 0.1917 0.0293 0.0139 70 CYS C O +5244 C CB . CYS C 71 ? 1.2241 0.7195 1.0732 0.1919 0.0297 0.0157 70 CYS C CB +5245 S SG . CYS C 71 ? 1.5203 1.0170 1.3689 0.1944 0.0289 0.0174 70 CYS C SG +5246 N N . PHE C 72 ? 1.2523 0.7659 1.1250 0.1954 0.0270 0.0153 71 PHE C N +5247 C CA . PHE C 72 ? 1.1588 0.6815 1.0431 0.1961 0.0265 0.0150 71 PHE C CA +5248 C C . PHE C 72 ? 1.0881 0.6138 0.9776 0.1961 0.0258 0.0141 71 PHE C C +5249 O O . PHE C 72 ? 1.6808 1.2138 1.5798 0.1969 0.0251 0.0139 71 PHE C O +5250 C CB . PHE C 72 ? 1.2643 0.7906 1.1517 0.1984 0.0255 0.0162 71 PHE C CB +5251 C CG . PHE C 72 ? 1.2057 0.7313 1.0909 0.1983 0.0262 0.0168 71 PHE C CG +5252 C CD1 . PHE C 72 ? 1.2917 0.8226 1.1836 0.1974 0.0268 0.0162 71 PHE C CD1 +5253 C CD2 . PHE C 72 ? 1.3551 0.8745 1.2314 0.1990 0.0263 0.0179 71 PHE C CD2 +5254 C CE1 . PHE C 72 ? 1.1204 0.6506 1.0102 0.1972 0.0275 0.0167 71 PHE C CE1 +5255 C CE2 . PHE C 72 ? 1.1491 0.6677 1.0232 0.1989 0.0270 0.0184 71 PHE C CE2 +5256 C CZ . PHE C 72 ? 1.5099 1.0339 1.3908 0.1979 0.0276 0.0178 71 PHE C CZ +5257 N N . SER C 73 ? 1.1833 0.7033 1.0666 0.1952 0.0260 0.0137 72 SER C N +5258 C CA . SER C 73 ? 1.4717 0.9939 1.3592 0.1948 0.0256 0.0127 72 SER C CA +5259 C C . SER C 73 ? 1.3450 0.8721 1.2398 0.1929 0.0265 0.0112 72 SER C C +5260 O O . SER C 73 ? 1.8044 1.3299 1.6973 0.1912 0.0277 0.0107 72 SER C O +5261 C CB . SER C 73 ? 1.3567 0.8709 1.2350 0.1939 0.0258 0.0126 72 SER C CB +5262 N N . ARG C 74 ? 1.1814 0.7145 1.0847 0.1933 0.0257 0.0105 73 ARG C N +5263 C CA . ARG C 74 ? 1.3514 0.8889 1.2615 0.1916 0.0264 0.0089 73 ARG C CA +5264 C C . ARG C 74 ? 1.3322 0.8646 1.2373 0.1898 0.0271 0.0078 73 ARG C C +5265 O O . ARG C 74 ? 1.2642 0.7951 1.1682 0.1904 0.0264 0.0078 73 ARG C O +5266 C CB . ARG C 74 ? 1.2391 0.7853 1.1603 0.1928 0.0253 0.0086 73 ARG C CB +5267 C CG . ARG C 74 ? 1.2154 0.7671 1.1447 0.1913 0.0258 0.0069 73 ARG C CG +5268 C CD . ARG C 74 ? 1.1315 0.6920 1.0718 0.1926 0.0245 0.0067 73 ARG C CD +5269 N NE . ARG C 74 ? 1.1666 0.7281 1.1090 0.1937 0.0234 0.0067 73 ARG C NE +5270 C CZ . ARG C 74 ? 1.5421 1.1019 1.4839 0.1926 0.0237 0.0056 73 ARG C CZ +5271 N NH1 . ARG C 74 ? 0.7841 0.3411 0.7233 0.1903 0.0250 0.0043 73 ARG C NH1 +5272 N NH2 . ARG C 74 ? 1.1190 0.6800 1.0629 0.1937 0.0226 0.0057 73 ARG C NH2 +5273 N N . TYR C 75 ? 1.3693 0.8988 1.2713 0.1876 0.0286 0.0070 74 TYR C N +5274 C CA . TYR C 75 ? 1.5124 1.0377 1.4106 0.1856 0.0294 0.0057 74 TYR C CA +5275 C C . TYR C 75 ? 1.4442 0.9757 1.3515 0.1844 0.0297 0.0040 74 TYR C C +5276 O O . TYR C 75 ? 1.7735 1.3085 1.6852 0.1834 0.0304 0.0034 74 TYR C O +5277 C CB . TYR C 75 ? 1.1841 0.7018 1.0726 0.1837 0.0308 0.0057 74 TYR C CB +5278 C CG . TYR C 75 ? 1.3366 0.8460 1.2141 0.1842 0.0306 0.0069 74 TYR C CG +5279 C CD1 . TYR C 75 ? 1.4598 0.9678 1.3341 0.1862 0.0298 0.0085 74 TYR C CD1 +5280 C CD2 . TYR C 75 ? 1.5117 1.0145 1.3821 0.1827 0.0312 0.0063 74 TYR C CD2 +5281 C CE1 . TYR C 75 ? 1.4014 0.9019 1.2657 0.1867 0.0296 0.0095 74 TYR C CE1 +5282 C CE2 . TYR C 75 ? 1.3580 0.8533 1.2183 0.1832 0.0309 0.0073 74 TYR C CE2 +5283 C CZ . TYR C 75 ? 1.4968 0.9909 1.3540 0.1852 0.0301 0.0089 74 TYR C CZ +5284 O OH . TYR C 75 ? 1.5069 0.9934 1.3540 0.1857 0.0297 0.0098 74 TYR C OH +5285 N N . PRO C 76 ? 1.2983 0.8314 1.2088 0.1845 0.0291 0.0032 75 PRO C N +5286 C CA . PRO C 76 ? 1.2033 0.7419 1.1220 0.1833 0.0294 0.0015 75 PRO C CA +5287 C C . PRO C 76 ? 1.7677 1.3030 1.6830 0.1806 0.0311 0.0002 75 PRO C C +5288 O O . PRO C 76 ? 1.5908 1.1185 1.4964 0.1796 0.0319 0.0006 75 PRO C O +5289 C CB . PRO C 76 ? 1.4069 0.9444 1.3255 0.1836 0.0288 0.0010 75 PRO C CB +5290 C CG . PRO C 76 ? 1.4191 0.9540 1.3334 0.1857 0.0277 0.0026 75 PRO C CG +5291 C CD . PRO C 76 ? 1.5610 1.0908 1.4676 0.1857 0.0282 0.0039 75 PRO C CD +5292 N N . ASP C 77 ? 1.7104 1.2512 1.6333 0.1795 0.0315 -0.0012 76 ASP C N +5293 C CA . ASP C 77 ? 1.8190 1.3576 1.7397 0.1771 0.0330 -0.0024 76 ASP C CA +5294 C C . ASP C 77 ? 1.9226 1.4533 1.8344 0.1752 0.0341 -0.0030 76 ASP C C +5295 O O . ASP C 77 ? 1.3505 0.8750 1.2542 0.1738 0.0355 -0.0028 76 ASP C O +5296 C CB . ASP C 77 ? 2.1615 1.7074 2.0921 0.1762 0.0331 -0.0041 76 ASP C CB +5297 C CG . ASP C 77 ? 2.3380 1.8905 2.2756 0.1772 0.0326 -0.0036 76 ASP C CG +5298 O OD1 . ASP C 77 ? 2.1420 1.6921 2.0756 0.1771 0.0331 -0.0027 76 ASP C OD1 +5299 O OD2 . ASP C 77 ? 2.4296 1.9895 2.3766 0.1781 0.0316 -0.0042 76 ASP C OD2 +5300 N N . HIS C 78 ? 1.8775 1.4079 1.7900 0.1753 0.0336 -0.0037 77 HIS C N +5301 C CA . HIS C 78 ? 1.3037 0.8246 1.2048 0.1744 0.0353 -0.0041 77 HIS C CA +5302 C C . HIS C 78 ? 1.7579 1.2697 1.6468 0.1747 0.0356 -0.0026 77 HIS C C +5303 O O . HIS C 78 ? 1.8848 1.3873 1.7622 0.1739 0.0373 -0.0028 77 HIS C O +5304 C CB . HIS C 78 ? 1.2775 0.7998 1.1816 0.1748 0.0349 -0.0051 77 HIS C CB +5305 C CG . HIS C 78 ? 1.4824 1.0077 1.3903 0.1764 0.0326 -0.0041 77 HIS C CG +5306 N ND1 . HIS C 78 ? 1.4611 0.9946 1.3789 0.1782 0.0310 -0.0036 77 HIS C ND1 +5307 C CD2 . HIS C 78 ? 1.5786 1.0978 1.4788 0.1772 0.0323 -0.0032 77 HIS C CD2 +5308 C CE1 . HIS C 78 ? 1.6852 1.2175 1.6013 0.1801 0.0299 -0.0026 77 HIS C CE1 +5309 N NE2 . HIS C 78 ? 1.7752 1.2996 1.6817 0.1793 0.0304 -0.0024 77 HIS C NE2 +5310 N N . MET C 79 ? 1.7016 1.2163 1.5931 0.1758 0.0340 -0.0011 78 MET C N +5311 C CA . MET C 79 ? 1.3718 0.8788 1.2528 0.1764 0.0339 0.0003 78 MET C CA +5312 C C . MET C 79 ? 1.6323 1.1363 1.5083 0.1758 0.0348 0.0012 78 MET C C +5313 O O . MET C 79 ? 1.3886 0.8838 1.2529 0.1756 0.0355 0.0020 78 MET C O +5314 C CB . MET C 79 ? 1.2536 0.7625 1.1362 0.1790 0.0321 0.0017 78 MET C CB +5315 C CG . MET C 79 ? 1.5588 1.0685 1.4436 0.1795 0.0313 0.0011 78 MET C CG +5316 S SD . MET C 79 ? 1.4643 0.9743 1.3485 0.1826 0.0294 0.0028 78 MET C SD +5317 C CE . MET C 79 ? 1.2392 0.7395 1.1100 0.1827 0.0296 0.0043 78 MET C CE +5318 N N . LYS C 80 ? 1.3405 0.8507 1.2239 0.1757 0.0348 0.0010 79 LYS C N +5319 C CA . LYS C 80 ? 1.5154 1.0239 1.3954 0.1757 0.0354 0.0019 79 LYS C CA +5320 C C . LYS C 80 ? 1.6149 1.1139 1.4828 0.1740 0.0371 0.0020 79 LYS C C +5321 O O . LYS C 80 ? 1.8381 1.3362 1.7039 0.1736 0.0375 0.0027 79 LYS C O +5322 C CB . LYS C 80 ? 1.1783 0.6943 1.0675 0.1755 0.0356 0.0013 79 LYS C CB +5323 C CG . LYS C 80 ? 1.7074 1.2315 1.6062 0.1778 0.0341 0.0017 79 LYS C CG +5324 C CD . LYS C 80 ? 1.2498 0.7804 1.1562 0.1778 0.0343 0.0014 79 LYS C CD +5325 C CE . LYS C 80 ? 1.3832 0.9217 1.2990 0.1800 0.0328 0.0019 79 LYS C CE +5326 N NZ . LYS C 80 ? 1.6702 1.2072 1.5826 0.1822 0.0318 0.0038 79 LYS C NZ +5327 N N . GLN C 81 ? 1.8426 1.3335 1.7009 0.1732 0.0385 0.0015 80 GLN C N +5328 C CA . GLN C 81 ? 1.8358 1.3159 1.6802 0.1719 0.0404 0.0017 80 GLN C CA +5329 C C . GLN C 81 ? 1.7790 1.2520 1.6137 0.1728 0.0397 0.0030 80 GLN C C +5330 O O . GLN C 81 ? 2.0712 1.5351 1.8940 0.1720 0.0409 0.0035 80 GLN C O +5331 C CB . GLN C 81 ? 1.5830 1.0581 1.4221 0.1701 0.0427 0.0002 80 GLN C CB +5332 C CG . GLN C 81 ? 1.6527 1.1253 1.4897 0.1703 0.0426 -0.0005 80 GLN C CG +5333 C CD . GLN C 81 ? 2.0441 1.5265 1.8944 0.1711 0.0414 -0.0015 80 GLN C CD +5334 O OE1 . GLN C 81 ? 2.2864 1.7776 2.1476 0.1713 0.0407 -0.0017 80 GLN C OE1 +5335 N NE2 . GLN C 81 ? 1.7202 1.2011 1.5695 0.1715 0.0411 -0.0020 80 GLN C NE2 +5336 N N . HIS C 82 ? 1.4145 0.8916 1.2544 0.1745 0.0377 0.0035 81 HIS C N +5337 C CA . HIS C 82 ? 1.8221 1.2934 1.6541 0.1755 0.0367 0.0047 81 HIS C CA +5338 C C . HIS C 82 ? 1.8638 1.3400 1.7009 0.1770 0.0348 0.0062 81 HIS C C +5339 O O . HIS C 82 ? 1.6798 1.1530 1.5124 0.1785 0.0337 0.0073 81 HIS C O +5340 C CB . HIS C 82 ? 1.7338 1.2051 1.5667 0.1763 0.0358 0.0044 81 HIS C CB +5341 C CG . HIS C 82 ? 1.7872 1.2535 1.6149 0.1749 0.0376 0.0029 81 HIS C CG +5342 N ND1 . HIS C 82 ? 1.8349 1.2900 1.6485 0.1736 0.0392 0.0028 81 HIS C ND1 +5343 C CD2 . HIS C 82 ? 1.3619 0.8328 1.1966 0.1744 0.0380 0.0015 81 HIS C CD2 +5344 C CE1 . HIS C 82 ? 1.9321 1.3852 1.7443 0.1724 0.0406 0.0014 81 HIS C CE1 +5345 N NE2 . HIS C 82 ? 1.8919 1.3544 1.7167 0.1729 0.0399 0.0006 81 HIS C NE2 +5346 N N . ASP C 83 ? 1.6107 1.0928 1.4547 0.1772 0.0350 0.0062 82 ASP C N +5347 C CA . ASP C 83 ? 1.6061 1.0902 1.4510 0.1793 0.0341 0.0077 82 ASP C CA +5348 C C . ASP C 83 ? 1.5500 1.0270 1.3849 0.1786 0.0349 0.0085 82 ASP C C +5349 O O . ASP C 83 ? 1.7463 1.2234 1.5812 0.1772 0.0360 0.0082 82 ASP C O +5350 C CB . ASP C 83 ? 2.0650 1.5577 1.9204 0.1797 0.0342 0.0073 82 ASP C CB +5351 C CG . ASP C 83 ? 1.9756 1.4721 1.8342 0.1822 0.0331 0.0087 82 ASP C CG +5352 O OD1 . ASP C 83 ? 1.6917 1.1833 1.5430 0.1832 0.0328 0.0100 82 ASP C OD1 +5353 O OD2 . ASP C 83 ? 2.2154 1.7198 2.0839 0.1833 0.0324 0.0085 82 ASP C OD2 +5354 N N . PHE C 84 ? 1.5380 1.0088 1.3644 0.1796 0.0342 0.0096 83 PHE C N +5355 C CA . PHE C 84 ? 1.4685 0.9321 1.2848 0.1791 0.0347 0.0105 83 PHE C CA +5356 C C . PHE C 84 ? 1.4789 0.9452 1.2970 0.1807 0.0344 0.0116 83 PHE C C +5357 O O . PHE C 84 ? 1.8242 1.2886 1.6394 0.1796 0.0354 0.0117 83 PHE C O +5358 C CB . PHE C 84 ? 1.5497 1.0063 1.3568 0.1799 0.0339 0.0113 83 PHE C CB +5359 C CG . PHE C 84 ? 1.6508 1.1007 1.4482 0.1802 0.0340 0.0124 83 PHE C CG +5360 C CD1 . PHE C 84 ? 1.8649 1.3095 1.6558 0.1778 0.0354 0.0121 83 PHE C CD1 +5361 C CD2 . PHE C 84 ? 1.6183 1.0674 1.4133 0.1827 0.0327 0.0138 83 PHE C CD2 +5362 C CE1 . PHE C 84 ? 1.7879 1.2264 1.5698 0.1780 0.0355 0.0132 83 PHE C CE1 +5363 C CE2 . PHE C 84 ? 1.8690 1.3120 1.6550 0.1829 0.0328 0.0148 83 PHE C CE2 +5364 C CZ . PHE C 84 ? 1.8483 1.2860 1.6278 0.1806 0.0342 0.0145 83 PHE C CZ +5365 N N . PHE C 85 ? 1.6430 1.1138 1.4659 0.1834 0.0330 0.0125 84 PHE C N +5366 C CA . PHE C 85 ? 1.5734 1.0467 1.3978 0.1853 0.0324 0.0137 84 PHE C CA +5367 C C . PHE C 85 ? 1.5378 1.0155 1.3675 0.1844 0.0334 0.0133 84 PHE C C +5368 O O . PHE C 85 ? 1.8253 1.3002 1.6505 0.1843 0.0339 0.0140 84 PHE C O +5369 C CB . PHE C 85 ? 1.5154 0.9943 1.3465 0.1880 0.0308 0.0143 84 PHE C CB +5370 C CG . PHE C 85 ? 1.4999 0.9752 1.3267 0.1889 0.0298 0.0145 84 PHE C CG +5371 C CD1 . PHE C 85 ? 1.5569 1.0258 1.3747 0.1901 0.0292 0.0157 84 PHE C CD1 +5372 C CD2 . PHE C 85 ? 1.5463 1.0243 1.3780 0.1886 0.0294 0.0136 84 PHE C CD2 +5373 C CE1 . PHE C 85 ? 1.5007 0.9663 1.3146 0.1909 0.0281 0.0159 84 PHE C CE1 +5374 C CE2 . PHE C 85 ? 1.2013 0.6760 1.0291 0.1895 0.0285 0.0139 84 PHE C CE2 +5375 C CZ . PHE C 85 ? 1.4353 0.9038 1.2542 0.1907 0.0278 0.0150 84 PHE C CZ +5376 N N . LYS C 86 ? 1.5562 1.0407 1.3954 0.1837 0.0336 0.0122 85 LYS C N +5377 C CA . LYS C 86 ? 1.7683 1.2573 1.6130 0.1829 0.0345 0.0118 85 LYS C CA +5378 C C . LYS C 86 ? 1.8203 1.3036 1.6583 0.1803 0.0361 0.0113 85 LYS C C +5379 O O . LYS C 86 ? 1.7044 1.1882 1.5422 0.1799 0.0367 0.0116 85 LYS C O +5380 C CB . LYS C 86 ? 1.5685 1.0659 1.4248 0.1827 0.0343 0.0107 85 LYS C CB +5381 C CG . LYS C 86 ? 1.3057 0.8095 1.1696 0.1852 0.0328 0.0112 85 LYS C CG +5382 C CD . LYS C 86 ? 1.3809 0.8928 1.2559 0.1848 0.0327 0.0100 85 LYS C CD +5383 C CE . LYS C 86 ? 1.0846 0.6031 0.9676 0.1872 0.0311 0.0105 85 LYS C CE +5384 N NZ . LYS C 86 ? 1.6438 1.1597 1.5239 0.1882 0.0302 0.0107 85 LYS C NZ +5385 N N . SER C 87 ? 1.7313 1.2094 1.5639 0.1785 0.0367 0.0105 86 SER C N +5386 C CA . SER C 87 ? 1.6946 1.1677 1.5216 0.1757 0.0383 0.0098 86 SER C CA +5387 C C . SER C 87 ? 1.7147 1.1806 1.5315 0.1755 0.0387 0.0109 86 SER C C +5388 O O . SER C 87 ? 1.6949 1.1575 1.5077 0.1734 0.0400 0.0105 86 SER C O +5389 C CB . SER C 87 ? 1.9252 1.3942 1.7486 0.1739 0.0388 0.0087 86 SER C CB +5390 O OG . SER C 87 ? 1.7957 1.2567 1.6086 0.1744 0.0384 0.0095 86 SER C OG +5391 N N . ALA C 88 ? 1.7575 1.2211 1.5702 0.1777 0.0376 0.0122 87 ALA C N +5392 C CA . ALA C 88 ? 1.4831 0.9399 1.2860 0.1778 0.0378 0.0133 87 ALA C CA +5393 C C . ALA C 88 ? 1.4732 0.9335 1.2791 0.1789 0.0378 0.0141 87 ALA C C +5394 O O . ALA C 88 ? 1.7179 1.1732 1.5164 0.1789 0.0381 0.0149 87 ALA C O +5395 C CB . ALA C 88 ? 1.4643 0.9167 1.2609 0.1797 0.0365 0.0143 87 ALA C CB +5396 N N . MET C 89 ? 1.4924 0.9612 1.3090 0.1797 0.0375 0.0138 88 MET C N +5397 C CA . MET C 89 ? 1.6981 1.1711 1.5187 0.1809 0.0374 0.0145 88 MET C CA +5398 C C . MET C 89 ? 1.5319 1.0049 1.3529 0.1786 0.0389 0.0138 88 MET C C +5399 O O . MET C 89 ? 1.6750 1.1468 1.4958 0.1763 0.0399 0.0126 88 MET C O +5400 C CB . MET C 89 ? 1.5602 1.0423 1.3921 0.1828 0.0364 0.0144 88 MET C CB +5401 C CG . MET C 89 ? 1.7110 1.1933 1.5427 0.1852 0.0348 0.0152 88 MET C CG +5402 S SD . MET C 89 ? 1.6429 1.1209 1.4671 0.1873 0.0341 0.0170 88 MET C SD +5403 C CE . MET C 89 ? 1.7937 1.2711 1.6172 0.1895 0.0324 0.0175 88 MET C CE +5404 N N . PRO C 90 ? 1.4580 0.9324 1.2795 0.1793 0.0391 0.0145 89 PRO C N +5405 C CA . PRO C 90 ? 1.7574 1.2335 1.5793 0.1819 0.0381 0.0159 89 PRO C CA +5406 C C . PRO C 90 ? 1.6152 1.0832 1.4258 0.1825 0.0379 0.0170 89 PRO C C +5407 O O . PRO C 90 ? 1.6362 1.1046 1.4460 0.1847 0.0370 0.0181 89 PRO C O +5408 C CB . PRO C 90 ? 1.6370 1.1172 1.4635 0.1815 0.0388 0.0159 89 PRO C CB +5409 C CG . PRO C 90 ? 1.5285 1.0079 1.3553 0.1786 0.0402 0.0146 89 PRO C CG +5410 C CD . PRO C 90 ? 1.5080 0.9819 1.3291 0.1771 0.0405 0.0139 89 PRO C CD +5411 N N . GLU C 91 ? 1.5295 0.9902 1.3317 0.1805 0.0388 0.0166 90 GLU C N +5412 C CA . GLU C 91 ? 1.8176 1.2701 1.6085 0.1807 0.0387 0.0175 90 GLU C CA +5413 C C . GLU C 91 ? 1.8220 1.2731 1.6105 0.1830 0.0372 0.0183 90 GLU C C +5414 O O . GLU C 91 ? 1.7027 1.1507 1.4860 0.1846 0.0366 0.0194 90 GLU C O +5415 C CB . GLU C 91 ? 2.1740 1.6193 1.9568 0.1778 0.0399 0.0168 90 GLU C CB +5416 C CG . GLU C 91 ? 2.3360 1.7826 2.1211 0.1755 0.0414 0.0160 90 GLU C CG +5417 C CD . GLU C 91 ? 2.5752 2.0134 2.3498 0.1733 0.0426 0.0160 90 GLU C CD +5418 O OE1 . GLU C 91 ? 2.4880 1.9235 2.2579 0.1740 0.0426 0.0169 90 GLU C OE1 +5419 O OE2 . GLU C 91 ? 2.6359 2.0702 2.4068 0.1710 0.0434 0.0151 90 GLU C OE2 +5420 N N . GLY C 92 ? 1.6503 1.1035 1.4427 0.1831 0.0367 0.0177 91 GLY C N +5421 C CA . GLY C 92 ? 1.4214 0.8749 1.2136 0.1854 0.0352 0.0183 91 GLY C CA +5422 C C . GLY C 92 ? 1.4788 0.9252 1.2627 0.1849 0.0349 0.0183 91 GLY C C +5423 O O . GLY C 92 ? 1.7177 1.1589 1.4959 0.1825 0.0359 0.0176 91 GLY C O +5424 N N . TYR C 93 ? 1.4526 0.8988 1.2357 0.1871 0.0335 0.0190 92 TYR C N +5425 C CA . TYR C 93 ? 1.5321 0.9720 1.3077 0.1870 0.0329 0.0190 92 TYR C CA +5426 C C . TYR C 93 ? 1.6616 1.0989 1.4326 0.1896 0.0315 0.0203 92 TYR C C +5427 O O . TYR C 93 ? 1.7147 1.1562 1.4898 0.1916 0.0309 0.0210 92 TYR C O +5428 C CB . TYR C 93 ? 1.4242 0.8674 1.2055 0.1865 0.0327 0.0181 92 TYR C CB +5429 C CG . TYR C 93 ? 1.5720 1.0233 1.3634 0.1887 0.0314 0.0182 92 TYR C CG +5430 C CD1 . TYR C 93 ? 1.8099 1.2606 1.6000 0.1911 0.0299 0.0190 92 TYR C CD1 +5431 C CD2 . TYR C 93 ? 1.5050 0.9644 1.3073 0.1885 0.0318 0.0175 92 TYR C CD2 +5432 C CE1 . TYR C 93 ? 1.7758 1.2338 1.5750 0.1931 0.0288 0.0192 92 TYR C CE1 +5433 C CE2 . TYR C 93 ? 1.6554 1.1221 1.4668 0.1904 0.0306 0.0176 92 TYR C CE2 +5434 C CZ . TYR C 93 ? 1.6038 1.0698 1.4137 0.1927 0.0292 0.0185 92 TYR C CZ +5435 O OH . TYR C 93 ? 1.7443 1.2175 1.5632 0.1946 0.0281 0.0186 92 TYR C OH +5436 N N . VAL C 94 ? 1.8071 1.2374 1.5694 0.1895 0.0310 0.0205 93 VAL C N +5437 C CA . VAL C 94 ? 1.6236 1.0506 1.3806 0.1918 0.0296 0.0216 93 VAL C CA +5438 C C . VAL C 94 ? 1.6146 1.0421 1.3730 0.1928 0.0285 0.0214 93 VAL C C +5439 O O . VAL C 94 ? 1.6004 1.0249 1.3562 0.1911 0.0288 0.0206 93 VAL C O +5440 C CB . VAL C 94 ? 1.6335 1.0507 1.3775 0.1910 0.0300 0.0220 93 VAL C CB +5441 C CG1 . VAL C 94 ? 1.5771 0.9913 1.3160 0.1935 0.0285 0.0232 93 VAL C CG1 +5442 C CG2 . VAL C 94 ? 1.6123 1.0282 1.3542 0.1895 0.0313 0.0220 93 VAL C CG2 +5443 N N . GLN C 95 ? 1.2921 0.7233 1.0544 0.1955 0.0271 0.0221 94 GLN C N +5444 C CA . GLN C 95 ? 1.4705 0.9032 1.2354 0.1967 0.0258 0.0220 94 GLN C CA +5445 C C . GLN C 95 ? 1.6746 1.1024 1.4324 0.1987 0.0244 0.0230 94 GLN C C +5446 O O . GLN C 95 ? 1.4416 0.8715 1.2009 0.2010 0.0236 0.0239 94 GLN C O +5447 C CB . GLN C 95 ? 1.4118 0.8543 1.1893 0.1980 0.0253 0.0218 94 GLN C CB +5448 C CG . GLN C 95 ? 1.3145 0.7594 1.0956 0.1996 0.0239 0.0219 94 GLN C CG +5449 C CD . GLN C 95 ? 1.4867 0.9411 1.2804 0.2002 0.0237 0.0214 94 GLN C CD +5450 O OE1 . GLN C 95 ? 1.4026 0.8605 1.2016 0.1984 0.0248 0.0204 94 GLN C OE1 +5451 N NE2 . GLN C 95 ? 1.5049 0.9635 1.3034 0.2026 0.0223 0.0220 94 GLN C NE2 +5452 N N . GLU C 96 ? 1.5700 0.9911 1.3200 0.1980 0.0242 0.0228 95 GLU C N +5453 C CA . GLU C 96 ? 1.3775 0.7930 1.1196 0.1997 0.0228 0.0236 95 GLU C CA +5454 C C . GLU C 96 ? 1.4977 0.9146 1.2425 0.2008 0.0216 0.0235 95 GLU C C +5455 O O . GLU C 96 ? 1.5832 0.9998 1.3290 0.1992 0.0219 0.0226 95 GLU C O +5456 C CB . GLU C 96 ? 1.7364 1.1421 1.4661 0.1979 0.0234 0.0237 95 GLU C CB +5457 C CG . GLU C 96 ? 2.1854 1.5883 1.9104 0.1973 0.0243 0.0241 95 GLU C CG +5458 C CD . GLU C 96 ? 2.5484 1.9424 2.2625 0.1949 0.0253 0.0238 95 GLU C CD +5459 O OE1 . GLU C 96 ? 2.5850 1.9790 2.3001 0.1923 0.0267 0.0229 95 GLU C OE1 +5460 O OE2 . GLU C 96 ? 2.5103 1.8973 2.2148 0.1954 0.0247 0.0244 95 GLU C OE2 +5461 N N . ARG C 97 ? 1.2188 0.6375 0.9650 0.2035 0.0201 0.0243 96 ARG C N +5462 C CA . ARG C 97 ? 1.4695 0.8896 1.2181 0.2047 0.0188 0.0242 96 ARG C CA +5463 C C . ARG C 97 ? 1.6821 1.0964 1.4227 0.2066 0.0173 0.0251 96 ARG C C +5464 O O . ARG C 97 ? 1.6199 1.0314 1.3557 0.2077 0.0171 0.0259 96 ARG C O +5465 C CB . ARG C 97 ? 1.1422 0.5718 0.9029 0.2064 0.0181 0.0243 96 ARG C CB +5466 C CG . ARG C 97 ? 1.7639 1.1999 1.5338 0.2048 0.0191 0.0233 96 ARG C CG +5467 C CD . ARG C 97 ? 1.4930 0.9368 1.2733 0.2065 0.0181 0.0232 96 ARG C CD +5468 N NE . ARG C 97 ? 1.7865 1.2374 1.5766 0.2052 0.0191 0.0224 96 ARG C NE +5469 C CZ . ARG C 97 ? 1.6026 1.0610 1.4016 0.2062 0.0191 0.0225 96 ARG C CZ +5470 N NH1 . ARG C 97 ? 1.7444 1.2045 1.5442 0.2084 0.0182 0.0236 96 ARG C NH1 +5471 N NH2 . ARG C 97 ? 1.5343 0.9986 1.3416 0.2049 0.0200 0.0217 96 ARG C NH2 +5472 N N . THR C 98 ? 1.4706 0.8832 1.2099 0.2070 0.0163 0.0249 97 THR C N +5473 C CA . THR C 98 ? 1.7951 1.2044 1.5296 0.2092 0.0147 0.0257 97 THR C CA +5474 C C . THR C 98 ? 1.5210 0.9368 1.2644 0.2107 0.0136 0.0256 97 THR C C +5475 O O . THR C 98 ? 1.4089 0.8283 1.1580 0.2095 0.0140 0.0247 97 THR C O +5476 C CB . THR C 98 ? 1.8178 1.2176 1.5405 0.2081 0.0144 0.0256 97 THR C CB +5477 O OG1 . THR C 98 ? 1.4450 0.8395 1.1607 0.2061 0.0158 0.0255 97 THR C OG1 +5478 C CG2 . THR C 98 ? 1.0606 0.4564 0.7774 0.2105 0.0127 0.0265 97 THR C CG2 +5479 N N . ILE C 99 ? 1.3295 0.7471 1.0744 0.2134 0.0121 0.0264 98 ILE C N +5480 C CA . ILE C 99 ? 1.5794 1.0040 1.3337 0.2150 0.0111 0.0263 98 ILE C CA +5481 C C . ILE C 99 ? 1.7121 1.1339 1.4626 0.2172 0.0092 0.0269 98 ILE C C +5482 O O . ILE C 99 ? 1.4539 0.8759 1.2035 0.2193 0.0084 0.0278 98 ILE C O +5483 C CB . ILE C 99 ? 1.3417 0.7750 1.1064 0.2160 0.0114 0.0265 98 ILE C CB +5484 C CG1 . ILE C 99 ? 1.1203 0.5566 0.8891 0.2137 0.0132 0.0258 98 ILE C CG1 +5485 C CG2 . ILE C 99 ? 1.0641 0.5047 0.8384 0.2177 0.0102 0.0266 98 ILE C CG2 +5486 C CD1 . ILE C 99 ? 1.1262 0.5673 0.9001 0.2142 0.0138 0.0262 98 ILE C CD1 +5487 N N . PHE C 100 ? 1.4524 0.8714 1.2004 0.2166 0.0087 0.0265 99 PHE C N +5488 C CA . PHE C 100 ? 1.3236 0.7392 1.0673 0.2185 0.0070 0.0270 99 PHE C CA +5489 C C . PHE C 100 ? 1.2296 0.6526 0.9830 0.2204 0.0058 0.0271 99 PHE C C +5490 O O . PHE C 100 ? 1.5404 0.9665 1.2989 0.2197 0.0058 0.0265 99 PHE C O +5491 C CB . PHE C 100 ? 1.2139 0.6225 0.9497 0.2170 0.0068 0.0265 99 PHE C CB +5492 C CG . PHE C 100 ? 1.4548 0.8561 1.1812 0.2148 0.0080 0.0262 99 PHE C CG +5493 C CD1 . PHE C 100 ? 1.5538 0.9559 1.2820 0.2122 0.0097 0.0254 99 PHE C CD1 +5494 C CD2 . PHE C 100 ? 1.6212 1.0148 1.3370 0.2153 0.0075 0.0269 99 PHE C CD2 +5495 C CE1 . PHE C 100 ? 1.5563 0.9517 1.2758 0.2100 0.0109 0.0252 99 PHE C CE1 +5496 C CE2 . PHE C 100 ? 1.4989 0.8857 1.2059 0.2132 0.0086 0.0267 99 PHE C CE2 +5497 C CZ . PHE C 100 ? 1.4253 0.8130 1.1342 0.2105 0.0103 0.0258 99 PHE C CZ +5498 N N . PHE C 101 ? 1.1715 0.5974 0.9277 0.2228 0.0049 0.0279 100 PHE C N +5499 C CA . PHE C 101 ? 1.3727 0.8045 1.1366 0.2248 0.0036 0.0282 100 PHE C CA +5500 C C . PHE C 101 ? 1.4953 0.9216 1.2528 0.2256 0.0021 0.0282 100 PHE C C +5501 O O . PHE C 101 ? 1.5302 0.9500 1.2789 0.2264 0.0014 0.0288 100 PHE C O +5502 C CB . PHE C 101 ? 1.1418 0.5779 0.9099 0.2271 0.0030 0.0290 100 PHE C CB +5503 C CG . PHE C 101 ? 1.4034 0.8452 1.1783 0.2264 0.0043 0.0289 100 PHE C CG +5504 C CD1 . PHE C 101 ? 1.5292 0.9673 1.2988 0.2250 0.0056 0.0289 100 PHE C CD1 +5505 C CD2 . PHE C 101 ? 1.4920 0.9427 1.2784 0.2272 0.0042 0.0289 100 PHE C CD2 +5506 C CE1 . PHE C 101 ? 1.0524 0.4957 0.8280 0.2244 0.0068 0.0288 100 PHE C CE1 +5507 C CE2 . PHE C 101 ? 1.4453 0.9012 1.2378 0.2265 0.0054 0.0288 100 PHE C CE2 +5508 C CZ . PHE C 101 ? 1.6216 1.0738 1.4087 0.2251 0.0067 0.0287 100 PHE C CZ +5509 N N . LYS C 102 ? 1.3538 0.7826 1.1157 0.2252 0.0018 0.0277 101 LYS C N +5510 C CA . LYS C 102 ? 1.8136 1.2374 1.5698 0.2258 0.0004 0.0277 101 LYS C CA +5511 C C . LYS C 102 ? 2.0060 1.4294 1.7608 0.2287 -0.0013 0.0286 101 LYS C C +5512 O O . LYS C 102 ? 1.3609 0.7909 1.1238 0.2304 -0.0018 0.0291 101 LYS C O +5513 C CB . LYS C 102 ? 1.3236 0.7516 1.0865 0.2253 0.0002 0.0270 101 LYS C CB +5514 C CG . LYS C 102 ? 1.6687 1.0924 1.4268 0.2262 -0.0013 0.0271 101 LYS C CG +5515 C CD . LYS C 102 ? 1.9120 1.3403 1.6773 0.2257 -0.0015 0.0264 101 LYS C CD +5516 C CE . LYS C 102 ? 1.7979 1.2195 1.5556 0.2248 -0.0021 0.0259 101 LYS C CE +5517 N NZ . LYS C 102 ? 1.9596 1.3813 1.7178 0.2269 -0.0040 0.0263 101 LYS C NZ +5518 N N . ASP C 103 ? 1.6571 1.0725 1.4016 0.2291 -0.0022 0.0289 102 ASP C N +5519 C CA . ASP C 103 ? 1.7566 1.1699 1.4979 0.2317 -0.0039 0.0297 102 ASP C CA +5520 C C . ASP C 103 ? 1.6526 1.0666 1.3933 0.2328 -0.0037 0.0304 102 ASP C C +5521 O O . ASP C 103 ? 1.6109 1.0268 1.3534 0.2352 -0.0048 0.0311 102 ASP C O +5522 C CB . ASP C 103 ? 1.9996 1.4189 1.7490 0.2336 -0.0053 0.0299 102 ASP C CB +5523 C CG . ASP C 103 ? 2.1724 1.5894 1.9202 0.2329 -0.0060 0.0294 102 ASP C CG +5524 O OD1 . ASP C 103 ? 2.0035 1.4127 1.7417 0.2317 -0.0060 0.0291 102 ASP C OD1 +5525 O OD2 . ASP C 103 ? 2.1086 1.5315 1.8646 0.2337 -0.0066 0.0292 102 ASP C OD2 +5526 N N . ASP C 104 ? 1.5540 0.9661 1.2919 0.2311 -0.0021 0.0303 103 ASP C N +5527 C CA . ASP C 104 ? 1.5119 0.9261 1.2511 0.2320 -0.0016 0.0308 103 ASP C CA +5528 C C . ASP C 104 ? 1.5614 0.9717 1.2951 0.2300 0.0000 0.0306 103 ASP C C +5529 O O . ASP C 104 ? 1.2748 0.6798 1.0023 0.2278 0.0007 0.0301 103 ASP C O +5530 C CB . ASP C 104 ? 1.1583 0.5826 0.9102 0.2328 -0.0014 0.0309 103 ASP C CB +5531 C CG . ASP C 104 ? 1.8609 1.2877 1.6147 0.2339 -0.0010 0.0315 103 ASP C CG +5532 O OD1 . ASP C 104 ? 1.3050 0.7257 1.0502 0.2341 -0.0009 0.0319 103 ASP C OD1 +5533 O OD2 . ASP C 104 ? 2.9554 2.3901 2.7191 0.2346 -0.0008 0.0316 103 ASP C OD2 +5534 N N . GLY C 105 ? 1.5887 1.0018 1.3248 0.2306 0.0006 0.0311 104 GLY C N +5535 C CA . GLY C 105 ? 1.3190 0.7281 1.0493 0.2292 0.0019 0.0311 104 GLY C CA +5536 C C . GLY C 105 ? 1.5509 0.9613 1.2834 0.2265 0.0036 0.0303 104 GLY C C +5537 O O . GLY C 105 ? 1.6095 1.0221 1.3460 0.2253 0.0038 0.0297 104 GLY C O +5538 N N . ASN C 106 ? 1.2926 0.7015 1.0225 0.2253 0.0049 0.0304 105 ASN C N +5539 C CA . ASN C 106 ? 1.3376 0.7481 1.0701 0.2227 0.0066 0.0296 105 ASN C CA +5540 C C . ASN C 106 ? 1.6255 1.0383 1.3599 0.2222 0.0079 0.0298 105 ASN C C +5541 O O . ASN C 106 ? 1.7135 1.1232 1.4429 0.2232 0.0077 0.0304 105 ASN C O +5542 C CB . ASN C 106 ? 1.5056 0.9082 1.2288 0.2205 0.0071 0.0291 105 ASN C CB +5543 C CG . ASN C 106 ? 1.4763 0.8703 1.1876 0.2204 0.0071 0.0296 105 ASN C CG +5544 O OD1 . ASN C 106 ? 1.7013 1.0944 1.4106 0.2200 0.0080 0.0298 105 ASN C OD1 +5545 N ND2 . ASN C 106 ? 1.3089 0.6962 1.0121 0.2208 0.0059 0.0297 105 ASN C ND2 +5546 N N . TYR C 107 ? 1.3737 0.7920 1.1156 0.2206 0.0092 0.0292 106 TYR C N +5547 C CA . TYR C 107 ? 1.3539 0.7740 1.0973 0.2197 0.0106 0.0292 106 TYR C CA +5548 C C . TYR C 107 ? 1.4071 0.8216 1.1440 0.2168 0.0120 0.0286 106 TYR C C +5549 O O . TYR C 107 ? 1.2532 0.6672 0.9906 0.2150 0.0125 0.0278 106 TYR C O +5550 C CB . TYR C 107 ? 1.2729 0.7027 1.0289 0.2196 0.0112 0.0289 106 TYR C CB +5551 C CG . TYR C 107 ? 1.2206 0.6569 0.9844 0.2222 0.0100 0.0295 106 TYR C CG +5552 C CD1 . TYR C 107 ? 1.4997 0.9338 1.2597 0.2245 0.0089 0.0303 106 TYR C CD1 +5553 C CD2 . TYR C 107 ? 1.4827 0.9275 1.2579 0.2223 0.0101 0.0291 106 TYR C CD2 +5554 C CE1 . TYR C 107 ? 1.2078 0.6481 0.9752 0.2268 0.0078 0.0309 106 TYR C CE1 +5555 C CE2 . TYR C 107 ? 1.1532 0.6041 0.9358 0.2246 0.0090 0.0296 106 TYR C CE2 +5556 C CZ . TYR C 107 ? 1.4145 0.8631 1.1931 0.2268 0.0079 0.0305 106 TYR C CZ +5557 O OH . TYR C 107 ? 1.4317 0.8864 1.2176 0.2290 0.0069 0.0310 106 TYR C OH +5558 N N . LYS C 108 ? 1.4052 0.8156 1.1359 0.2163 0.0128 0.0289 107 LYS C N +5559 C CA . LYS C 108 ? 1.3146 0.7211 1.0408 0.2135 0.0144 0.0283 107 LYS C CA +5560 C C . LYS C 108 ? 1.4450 0.8559 1.1760 0.2129 0.0156 0.0284 107 LYS C C +5561 O O . LYS C 108 ? 1.7199 1.1301 1.4488 0.2142 0.0155 0.0290 107 LYS C O +5562 C CB . LYS C 108 ? 1.4905 0.8869 1.2036 0.2128 0.0143 0.0285 107 LYS C CB +5563 C CG . LYS C 108 ? 1.5737 0.9649 1.2811 0.2123 0.0135 0.0282 107 LYS C CG +5564 C CD . LYS C 108 ? 1.5902 0.9714 1.2845 0.2118 0.0132 0.0285 107 LYS C CD +5565 C CE . LYS C 108 ? 1.6516 1.0275 1.3402 0.2109 0.0126 0.0281 107 LYS C CE +5566 N NZ . LYS C 108 ? 1.5540 0.9300 1.2440 0.2081 0.0139 0.0272 107 LYS C NZ +5567 N N . THR C 109 ? 1.4671 0.8827 1.2049 0.2111 0.0168 0.0276 108 THR C N +5568 C CA . THR C 109 ? 1.5373 0.9581 1.2813 0.2106 0.0179 0.0275 108 THR C CA +5569 C C . THR C 109 ? 1.5260 0.9435 1.2662 0.2077 0.0196 0.0269 108 THR C C +5570 O O . THR C 109 ? 1.3124 0.7257 1.0484 0.2058 0.0201 0.0262 108 THR C O +5571 C CB . THR C 109 ? 1.4459 0.8764 1.2027 0.2110 0.0179 0.0271 108 THR C CB +5572 O OG1 . THR C 109 ? 1.2457 0.6769 1.0050 0.2088 0.0187 0.0261 108 THR C OG1 +5573 C CG2 . THR C 109 ? 1.5650 0.9991 1.3263 0.2136 0.0162 0.0276 108 THR C CG2 +5574 N N . ARG C 110 ? 1.2174 0.6368 0.9592 0.2074 0.0205 0.0271 109 ARG C N +5575 C CA . ARG C 110 ? 1.3594 0.7780 1.1007 0.2048 0.0222 0.0264 109 ARG C CA +5576 C C . ARG C 110 ? 1.4265 0.8525 1.1767 0.2050 0.0229 0.0264 109 ARG C C +5577 O O . ARG C 110 ? 1.4875 0.9148 1.2380 0.2066 0.0226 0.0272 109 ARG C O +5578 C CB . ARG C 110 ? 1.4935 0.9034 1.2232 0.2036 0.0228 0.0267 109 ARG C CB +5579 C CG . ARG C 110 ? 1.8211 1.2303 1.5504 0.2008 0.0246 0.0260 109 ARG C CG +5580 C CD . ARG C 110 ? 1.4413 0.8421 1.1593 0.1997 0.0252 0.0263 109 ARG C CD +5581 N NE . ARG C 110 ? 1.7656 1.1647 1.4822 0.1968 0.0269 0.0256 109 ARG C NE +5582 C CZ . ARG C 110 ? 1.8402 1.2422 1.5600 0.1960 0.0280 0.0255 109 ARG C CZ +5583 N NH1 . ARG C 110 ? 1.9244 1.3311 1.6490 0.1979 0.0276 0.0262 109 ARG C NH1 +5584 N NH2 . ARG C 110 ? 1.5997 0.9998 1.3179 0.1932 0.0295 0.0248 109 ARG C NH2 +5585 N N . ALA C 111 ? 1.6417 1.0727 1.3992 0.2034 0.0238 0.0256 110 ALA C N +5586 C CA . ALA C 111 ? 1.3822 0.8207 1.1489 0.2033 0.0245 0.0254 110 ALA C CA +5587 C C . ALA C 111 ? 1.4683 0.9060 1.2347 0.2005 0.0262 0.0246 110 ALA C C +5588 O O . ALA C 111 ? 1.3504 0.7848 1.1138 0.1985 0.0268 0.0238 110 ALA C O +5589 C CB . ALA C 111 ? 1.5325 0.9792 1.3102 0.2043 0.0238 0.0251 110 ALA C CB +5590 N N . GLU C 112 ? 1.2400 0.6806 1.0093 0.2004 0.0269 0.0248 111 GLU C N +5591 C CA . GLU C 112 ? 1.6119 1.0535 1.3831 0.1979 0.0285 0.0240 111 GLU C CA +5592 C C . GLU C 112 ? 1.7309 1.1821 1.5145 0.1982 0.0287 0.0236 111 GLU C C +5593 O O . GLU C 112 ? 1.6028 1.0585 1.3909 0.1998 0.0283 0.0242 111 GLU C O +5594 C CB . GLU C 112 ? 1.8315 1.2685 1.5958 0.1972 0.0294 0.0245 111 GLU C CB +5595 C CG . GLU C 112 ? 2.2940 1.7212 2.0458 0.1962 0.0296 0.0247 111 GLU C CG +5596 C CD . GLU C 112 ? 2.3346 1.7575 2.0798 0.1959 0.0303 0.0253 111 GLU C CD +5597 O OE1 . GLU C 112 ? 2.0097 1.4372 1.7600 0.1963 0.0307 0.0255 111 GLU C OE1 +5598 O OE2 . GLU C 112 ? 2.2215 1.6363 1.9561 0.1954 0.0303 0.0256 111 GLU C OE2 +5599 N N . VAL C 113 ? 1.5411 0.9953 1.3300 0.1966 0.0291 0.0226 112 VAL C N +5600 C CA . VAL C 113 ? 1.3200 0.7831 1.1204 0.1966 0.0294 0.0220 112 VAL C CA +5601 C C . VAL C 113 ? 1.5919 1.0552 1.3932 0.1940 0.0309 0.0212 112 VAL C C +5602 O O . VAL C 113 ? 1.5290 0.9882 1.3262 0.1918 0.0318 0.0204 112 VAL C O +5603 C CB . VAL C 113 ? 1.1614 0.6289 0.9686 0.1967 0.0287 0.0213 112 VAL C CB +5604 C CG1 . VAL C 113 ? 1.4384 0.9154 1.2577 0.1974 0.0285 0.0211 112 VAL C CG1 +5605 C CG2 . VAL C 113 ? 1.5802 1.0454 1.3843 0.1987 0.0272 0.0220 112 VAL C CG2 +5606 N N . LYS C 114 ? 1.3888 0.8567 1.1952 0.1943 0.0314 0.0214 113 LYS C N +5607 C CA . LYS C 114 ? 1.4917 0.9604 1.2996 0.1921 0.0328 0.0207 113 LYS C CA +5608 C C . LYS C 114 ? 1.6210 1.0974 1.4378 0.1929 0.0328 0.0209 113 LYS C C +5609 O O . LYS C 114 ? 1.3927 0.8732 1.2137 0.1952 0.0318 0.0216 113 LYS C O +5610 C CB . LYS C 114 ? 1.8516 1.3122 1.6487 0.1907 0.0337 0.0210 113 LYS C CB +5611 C CG . LYS C 114 ? 1.8560 1.3136 1.6475 0.1926 0.0332 0.0223 113 LYS C CG +5612 C CD . LYS C 114 ? 1.5435 0.9933 1.3248 0.1912 0.0342 0.0225 113 LYS C CD +5613 C CE . LYS C 114 ? 1.8608 1.3085 1.6377 0.1931 0.0337 0.0238 113 LYS C CE +5614 N NZ . LYS C 114 ? 1.6660 1.1113 1.4391 0.1954 0.0322 0.0245 113 LYS C NZ +5615 N N . PHE C 115 ? 1.5028 0.9811 1.3224 0.1910 0.0340 0.0202 114 PHE C N +5616 C CA . PHE C 115 ? 1.5513 1.0368 1.3794 0.1915 0.0342 0.0202 114 PHE C CA +5617 C C . PHE C 115 ? 1.5833 1.0659 1.4063 0.1918 0.0347 0.0210 114 PHE C C +5618 O O . PHE C 115 ? 1.7355 1.2115 1.5502 0.1904 0.0356 0.0210 114 PHE C O +5619 C CB . PHE C 115 ? 1.7782 1.2674 1.6123 0.1893 0.0352 0.0189 114 PHE C CB +5620 C CG . PHE C 115 ? 1.8244 1.3210 1.6687 0.1896 0.0346 0.0181 114 PHE C CG +5621 C CD1 . PHE C 115 ? 1.6401 1.1447 1.4939 0.1910 0.0340 0.0183 114 PHE C CD1 +5622 C CD2 . PHE C 115 ? 1.5611 1.0567 1.4057 0.1886 0.0345 0.0172 114 PHE C CD2 +5623 C CE1 . PHE C 115 ? 1.4688 0.9803 1.3321 0.1913 0.0333 0.0176 114 PHE C CE1 +5624 C CE2 . PHE C 115 ? 1.4492 0.9516 1.3032 0.1889 0.0339 0.0165 114 PHE C CE2 +5625 C CZ . PHE C 115 ? 1.5704 1.0808 1.4338 0.1903 0.0333 0.0167 114 PHE C CZ +5626 N N . GLU C 116 ? 1.4361 0.9237 1.2642 0.1937 0.0341 0.0218 115 GLU C N +5627 C CA . GLU C 116 ? 1.4984 0.9844 1.3231 0.1941 0.0345 0.0225 115 GLU C CA +5628 C C . GLU C 116 ? 1.4972 0.9909 1.3313 0.1941 0.0348 0.0223 115 GLU C C +5629 O O . GLU C 116 ? 1.4965 0.9948 1.3354 0.1961 0.0341 0.0229 115 GLU C O +5630 C CB . GLU C 116 ? 1.4569 0.9407 1.2773 0.1966 0.0335 0.0238 115 GLU C CB +5631 C CG . GLU C 116 ? 1.7403 1.2173 1.5524 0.1970 0.0329 0.0240 115 GLU C CG +5632 C CD . GLU C 116 ? 2.2278 1.7011 2.0338 0.1991 0.0322 0.0252 115 GLU C CD +5633 O OE1 . GLU C 116 ? 2.2080 1.6857 2.0183 0.2009 0.0317 0.0259 115 GLU C OE1 +5634 O OE2 . GLU C 116 ? 1.9224 1.3882 1.7189 0.1990 0.0320 0.0255 115 GLU C OE2 +5635 N N . GLY C 117 ? 1.4162 0.9111 1.2528 0.1918 0.0359 0.0213 116 GLY C N +5636 C CA . GLY C 117 ? 1.2368 0.7394 1.0831 0.1916 0.0361 0.0208 116 GLY C CA +5637 C C . GLY C 117 ? 1.6690 1.1778 1.5241 0.1919 0.0354 0.0201 116 GLY C C +5638 O O . GLY C 117 ? 1.5241 1.0310 1.3782 0.1906 0.0356 0.0192 116 GLY C O +5639 N N . ASP C 118 ? 1.9795 1.4954 1.8430 0.1935 0.0345 0.0203 117 ASP C N +5640 C CA . ASP C 118 ? 1.7764 1.2991 1.6493 0.1938 0.0338 0.0196 117 ASP C CA +5641 C C . ASP C 118 ? 1.6400 1.1621 1.5123 0.1955 0.0326 0.0201 117 ASP C C +5642 O O . ASP C 118 ? 1.7111 1.2374 1.5896 0.1957 0.0319 0.0194 117 ASP C O +5643 C CB . ASP C 118 ? 1.8396 1.3706 1.7223 0.1946 0.0335 0.0196 117 ASP C CB +5644 C CG . ASP C 118 ? 2.2215 1.7546 2.1052 0.1972 0.0325 0.0209 117 ASP C CG +5645 O OD1 . ASP C 118 ? 2.0437 1.5714 1.9196 0.1980 0.0325 0.0218 117 ASP C OD1 +5646 O OD2 . ASP C 118 ? 2.0798 1.6200 1.9723 0.1984 0.0316 0.0209 117 ASP C OD2 +5647 N N . THR C 119 ? 1.6768 1.1936 1.5414 0.1969 0.0322 0.0211 118 THR C N +5648 C CA . THR C 119 ? 1.5801 1.0967 1.4443 0.1988 0.0309 0.0217 118 THR C CA +5649 C C . THR C 119 ? 1.3788 0.8880 1.2345 0.1980 0.0310 0.0215 118 THR C C +5650 O O . THR C 119 ? 1.3912 0.8940 1.2390 0.1965 0.0320 0.0214 118 THR C O +5651 C CB . THR C 119 ? 1.3184 0.8353 1.1812 0.2012 0.0302 0.0230 118 THR C CB +5652 O OG1 . THR C 119 ? 1.4426 0.9670 1.3143 0.2019 0.0300 0.0231 118 THR C OG1 +5653 C CG2 . THR C 119 ? 1.4893 1.0055 1.3511 0.2032 0.0288 0.0236 118 THR C CG2 +5654 N N . LEU C 120 ? 1.3745 0.8847 1.2321 0.1989 0.0300 0.0214 119 LEU C N +5655 C CA . LEU C 120 ? 1.1297 0.6334 0.9799 0.1983 0.0299 0.0212 119 LEU C CA +5656 C C . LEU C 120 ? 1.4487 0.9487 1.2933 0.2006 0.0288 0.0224 119 LEU C C +5657 O O . LEU C 120 ? 1.2147 0.7191 1.0645 0.2025 0.0276 0.0228 119 LEU C O +5658 C CB . LEU C 120 ? 1.1957 0.7029 1.0519 0.1978 0.0295 0.0202 119 LEU C CB +5659 C CG . LEU C 120 ? 1.0683 0.5696 0.9183 0.1968 0.0295 0.0197 119 LEU C CG +5660 C CD1 . LEU C 120 ? 2.1338 1.6387 1.9900 0.1951 0.0300 0.0184 119 LEU C CD1 +5661 C CD2 . LEU C 120 ? 1.1766 0.6765 1.0246 0.1989 0.0282 0.0205 119 LEU C CD2 +5662 N N . VAL C 121 ? 1.2767 0.7689 1.1109 0.2003 0.0292 0.0229 120 VAL C N +5663 C CA . VAL C 121 ? 1.3690 0.8575 1.1974 0.2024 0.0282 0.0240 120 VAL C CA +5664 C C . VAL C 121 ? 1.5227 1.0045 1.3433 0.2023 0.0277 0.0240 120 VAL C C +5665 O O . VAL C 121 ? 1.2816 0.7579 1.0960 0.2004 0.0285 0.0234 120 VAL C O +5666 C CB . VAL C 121 ? 1.3790 0.8640 1.2016 0.2029 0.0287 0.0248 120 VAL C CB +5667 C CG1 . VAL C 121 ? 1.1290 0.6204 0.9591 0.2028 0.0292 0.0248 120 VAL C CG1 +5668 C CG2 . VAL C 121 ? 1.7947 1.2717 1.6073 0.2009 0.0297 0.0246 120 VAL C CG2 +5669 N N . ASN C 122 ? 1.3185 0.8009 1.1396 0.2045 0.0264 0.0246 121 ASN C N +5670 C CA . ASN C 122 ? 1.3699 0.8462 1.1836 0.2049 0.0257 0.0248 121 ASN C CA +5671 C C . ASN C 122 ? 1.6020 1.0740 1.4088 0.2068 0.0250 0.0259 121 ASN C C +5672 O O . ASN C 122 ? 1.3382 0.8143 1.1492 0.2091 0.0240 0.0266 121 ASN C O +5673 C CB . ASN C 122 ? 1.1930 0.6737 1.0131 0.2059 0.0246 0.0245 121 ASN C CB +5674 C CG . ASN C 122 ? 1.2808 0.7553 1.0937 0.2058 0.0239 0.0245 121 ASN C CG +5675 O OD1 . ASN C 122 ? 1.7479 1.2152 1.5519 0.2044 0.0246 0.0243 121 ASN C OD1 +5676 N ND2 . ASN C 122 ? 1.3374 0.8147 1.1542 0.2074 0.0227 0.0246 121 ASN C ND2 +5677 N N . ARG C 123 ? 1.5277 0.9918 1.3241 0.2059 0.0255 0.0261 122 ARG C N +5678 C CA . ARG C 123 ? 1.4019 0.8608 1.1904 0.2076 0.0249 0.0272 122 ARG C CA +5679 C C . ARG C 123 ? 1.5517 1.0040 1.3322 0.2080 0.0240 0.0273 122 ARG C C +5680 O O . ARG C 123 ? 1.2758 0.7227 1.0504 0.2062 0.0246 0.0268 122 ARG C O +5681 C CB . ARG C 123 ? 1.4641 0.9184 1.2461 0.2063 0.0261 0.0273 122 ARG C CB +5682 C CG . ARG C 123 ? 1.4995 0.9595 1.2879 0.2064 0.0268 0.0274 122 ARG C CG +5683 C CD . ARG C 123 ? 1.5068 0.9616 1.2877 0.2056 0.0277 0.0278 122 ARG C CD +5684 N NE . ARG C 123 ? 1.7424 1.2023 1.5295 0.2048 0.0287 0.0276 122 ARG C NE +5685 C CZ . ARG C 123 ? 1.8174 1.2826 1.6101 0.2065 0.0284 0.0281 122 ARG C CZ +5686 N NH1 . ARG C 123 ? 1.5773 1.0435 1.3704 0.2090 0.0272 0.0289 122 ARG C NH1 +5687 N NH2 . ARG C 123 ? 1.6287 1.0983 1.4268 0.2056 0.0293 0.0279 122 ARG C NH2 +5688 N N . ILE C 124 ? 1.5560 1.0088 1.3364 0.2105 0.0227 0.0281 123 ILE C N +5689 C CA . ILE C 124 ? 1.3546 0.8027 1.1295 0.2113 0.0216 0.0282 123 ILE C CA +5690 C C . ILE C 124 ? 1.5057 0.9482 1.2723 0.2131 0.0206 0.0292 123 ILE C C +5691 O O . ILE C 124 ? 1.3049 0.7503 1.0742 0.2151 0.0201 0.0299 123 ILE C O +5692 C CB . ILE C 124 ? 1.6813 1.1357 1.4650 0.2124 0.0205 0.0280 123 ILE C CB +5693 C CG1 . ILE C 124 ? 1.4399 0.9017 1.2338 0.2111 0.0213 0.0272 123 ILE C CG1 +5694 C CG2 . ILE C 124 ? 1.3802 0.8299 1.1589 0.2124 0.0197 0.0278 123 ILE C CG2 +5695 C CD1 . ILE C 124 ? 1.5539 1.0231 1.3577 0.2125 0.0203 0.0271 123 ILE C CD1 +5696 N N . GLU C 125 ? 1.4599 0.8941 1.2164 0.2125 0.0205 0.0291 124 GLU C N +5697 C CA . GLU C 125 ? 1.4062 0.8348 1.1547 0.2143 0.0193 0.0299 124 GLU C CA +5698 C C . GLU C 125 ? 1.3947 0.8218 1.1421 0.2149 0.0181 0.0297 124 GLU C C +5699 O O . GLU C 125 ? 1.5883 1.0128 1.3337 0.2130 0.0186 0.0290 124 GLU C O +5700 C CB . GLU C 125 ? 1.4989 0.9187 1.2358 0.2130 0.0200 0.0300 124 GLU C CB +5701 C CG . GLU C 125 ? 2.0806 1.5008 1.8172 0.2120 0.0213 0.0301 124 GLU C CG +5702 C CD . GLU C 125 ? 2.3492 1.7608 2.0749 0.2100 0.0222 0.0300 124 GLU C CD +5703 O OE1 . GLU C 125 ? 2.5207 1.9275 2.2413 0.2085 0.0223 0.0295 124 GLU C OE1 +5704 O OE2 . GLU C 125 ? 2.1716 1.5814 1.8939 0.2100 0.0228 0.0304 124 GLU C OE2 +5705 N N . LEU C 126 ? 1.2899 0.7183 1.0386 0.2174 0.0167 0.0304 125 LEU C N +5706 C CA . LEU C 126 ? 1.3386 0.7660 1.0868 0.2182 0.0154 0.0303 125 LEU C CA +5707 C C . LEU C 126 ? 1.4529 0.8744 1.1929 0.2202 0.0141 0.0310 125 LEU C C +5708 O O . LEU C 126 ? 1.6384 1.0605 1.3780 0.2220 0.0136 0.0317 125 LEU C O +5709 C CB . LEU C 126 ? 1.2990 0.7353 1.0589 0.2195 0.0148 0.0302 125 LEU C CB +5710 C CG . LEU C 126 ? 1.2035 0.6404 0.9647 0.2212 0.0131 0.0303 125 LEU C CG +5711 C CD1 . LEU C 126 ? 1.3240 0.7678 1.0951 0.2207 0.0131 0.0297 125 LEU C CD1 +5712 C CD2 . LEU C 126 ? 1.4126 0.8517 1.1755 0.2241 0.0119 0.0312 125 LEU C CD2 +5713 N N . LYS C 127 ? 1.5870 1.0028 1.3205 0.2198 0.0134 0.0308 126 LYS C N +5714 C CA . LYS C 127 ? 1.4154 0.8248 1.1402 0.2215 0.0121 0.0314 126 LYS C CA +5715 C C . LYS C 127 ? 1.5140 0.9222 1.2381 0.2225 0.0107 0.0314 126 LYS C C +5716 O O . LYS C 127 ? 1.7320 1.1351 1.4506 0.2210 0.0107 0.0309 126 LYS C O +5717 C CB . LYS C 127 ? 1.6369 1.0374 1.3500 0.2200 0.0128 0.0314 126 LYS C CB +5718 C CG . LYS C 127 ? 1.8890 1.2825 1.5926 0.2216 0.0115 0.0321 126 LYS C CG +5719 C CD . LYS C 127 ? 2.0429 1.4279 1.7352 0.2203 0.0122 0.0321 126 LYS C CD +5720 C CE . LYS C 127 ? 1.9871 1.3655 1.6704 0.2220 0.0107 0.0327 126 LYS C CE +5721 N NZ . LYS C 127 ? 1.9731 1.3562 1.6620 0.2250 0.0094 0.0333 126 LYS C NZ +5722 N N . GLY C 128 ? 1.5170 0.9295 1.2462 0.2250 0.0094 0.0319 127 GLY C N +5723 C CA . GLY C 128 ? 1.4592 0.8711 1.1884 0.2261 0.0079 0.0319 127 GLY C CA +5724 C C . GLY C 128 ? 1.8024 1.2080 1.5231 0.2280 0.0065 0.0325 127 GLY C C +5725 O O . GLY C 128 ? 1.9447 1.3504 1.6644 0.2298 0.0060 0.0331 127 GLY C O +5726 N N . ILE C 129 ? 1.8964 1.2966 1.6111 0.2275 0.0057 0.0322 128 ILE C N +5727 C CA . ILE C 129 ? 1.7081 1.1018 1.4142 0.2291 0.0042 0.0327 128 ILE C CA +5728 C C . ILE C 129 ? 1.3762 0.7704 1.0839 0.2299 0.0029 0.0325 128 ILE C C +5729 O O . ILE C 129 ? 1.7489 1.1465 1.4620 0.2286 0.0033 0.0319 128 ILE C O +5730 C CB . ILE C 129 ? 1.4799 0.8638 1.1734 0.2275 0.0047 0.0326 128 ILE C CB +5731 C CG1 . ILE C 129 ? 2.0789 1.4613 1.7694 0.2269 0.0058 0.0329 128 ILE C CG1 +5732 C CG2 . ILE C 129 ? 2.4327 1.8098 2.1175 0.2290 0.0030 0.0330 128 ILE C CG2 +5733 C CD1 . ILE C 129 ? 1.9420 1.3247 1.6332 0.2240 0.0077 0.0322 128 ILE C CD1 +5734 N N . ASP C 130 ? 1.7812 1.1719 1.4842 0.2319 0.0013 0.0330 129 ASP C N +5735 C CA . ASP C 130 ? 1.8424 1.2317 1.5446 0.2327 -0.0001 0.0329 129 ASP C CA +5736 C C . ASP C 130 ? 1.3072 0.7050 1.0207 0.2341 -0.0009 0.0329 129 ASP C C +5737 O O . ASP C 130 ? 1.4282 0.8262 1.1429 0.2343 -0.0018 0.0327 129 ASP C O +5738 C CB . ASP C 130 ? 1.8247 1.2091 1.5217 0.2302 0.0004 0.0322 129 ASP C CB +5739 C CG . ASP C 130 ? 2.0304 1.4051 1.7147 0.2291 0.0006 0.0323 129 ASP C CG +5740 O OD1 . ASP C 130 ? 1.8833 1.2532 1.5609 0.2307 -0.0006 0.0328 129 ASP C OD1 +5741 O OD2 . ASP C 130 ? 1.9716 1.3434 1.6526 0.2265 0.0020 0.0318 129 ASP C OD2 +5742 N N . PHE C 131 ? 1.1944 0.5992 0.9161 0.2352 -0.0005 0.0333 130 PHE C N +5743 C CA . PHE C 131 ? 1.6823 1.0949 1.4145 0.2366 -0.0013 0.0333 130 PHE C CA +5744 C C . PHE C 131 ? 1.0595 0.4709 0.7900 0.2393 -0.0032 0.0339 130 PHE C C +5745 O O . PHE C 131 ? 1.6103 1.0152 1.3319 0.2402 -0.0038 0.0343 130 PHE C O +5746 C CB . PHE C 131 ? 1.6154 1.0363 1.3576 0.2366 -0.0003 0.0334 130 PHE C CB +5747 C CG . PHE C 131 ? 1.3067 0.7301 1.0527 0.2340 0.0014 0.0326 130 PHE C CG +5748 C CD1 . PHE C 131 ? 1.4999 0.9190 1.2400 0.2321 0.0028 0.0324 130 PHE C CD1 +5749 C CD2 . PHE C 131 ? 1.4033 0.8328 1.1581 0.2333 0.0015 0.0321 130 PHE C CD2 +5750 C CE1 . PHE C 131 ? 1.0610 0.4822 0.8043 0.2297 0.0043 0.0317 130 PHE C CE1 +5751 C CE2 . PHE C 131 ? 1.3570 0.7886 1.1150 0.2309 0.0030 0.0314 130 PHE C CE2 +5752 C CZ . PHE C 131 ? 1.6739 1.1013 1.4262 0.2291 0.0044 0.0312 130 PHE C CZ +5753 N N . LYS C 132 ? 1.2836 0.7010 1.0222 0.2407 -0.0041 0.0340 131 LYS C N +5754 C CA . LYS C 132 ? 1.3293 0.7462 1.0672 0.2433 -0.0059 0.0345 131 LYS C CA +5755 C C . LYS C 132 ? 1.3862 0.8102 1.1325 0.2452 -0.0061 0.0351 131 LYS C C +5756 O O . LYS C 132 ? 2.3504 1.7821 2.1066 0.2448 -0.0055 0.0349 131 LYS C O +5757 C CB . LYS C 132 ? 1.2297 0.6478 0.9704 0.2435 -0.0070 0.0342 131 LYS C CB +5758 C CG . LYS C 132 ? 1.3639 0.7762 1.0982 0.2414 -0.0068 0.0336 131 LYS C CG +5759 C CD . LYS C 132 ? 1.6543 1.0686 1.3923 0.2419 -0.0079 0.0333 131 LYS C CD +5760 C CE . LYS C 132 ? 1.8361 1.2437 1.5665 0.2400 -0.0078 0.0327 131 LYS C CE +5761 N NZ . LYS C 132 ? 1.9063 1.3171 1.6419 0.2401 -0.0086 0.0324 131 LYS C NZ +5762 N N . GLU C 133 ? 1.7526 1.1743 1.4951 0.2472 -0.0069 0.0357 132 GLU C N +5763 C CA . GLU C 133 ? 2.0521 1.4801 1.8019 0.2490 -0.0070 0.0363 132 GLU C CA +5764 C C . GLU C 133 ? 1.8126 1.2482 1.5727 0.2502 -0.0079 0.0363 132 GLU C C +5765 O O . GLU C 133 ? 1.6759 1.1178 1.4436 0.2515 -0.0079 0.0367 132 GLU C O +5766 C CB . GLU C 133 ? 1.6253 1.0489 1.3684 0.2510 -0.0079 0.0369 132 GLU C CB +5767 C CG . GLU C 133 ? 2.9536 2.3723 2.6894 0.2501 -0.0067 0.0370 132 GLU C CG +5768 C CD . GLU C 133 ? 2.7057 2.1303 2.4482 0.2501 -0.0054 0.0372 132 GLU C CD +5769 O OE1 . GLU C 133 ? 2.6227 2.0536 2.3729 0.2518 -0.0059 0.0376 132 GLU C OE1 +5770 O OE2 . GLU C 133 ? 2.0660 1.4890 1.8058 0.2483 -0.0040 0.0370 132 GLU C OE2 +5771 N N . ASP C 134 ? 1.5447 0.9797 1.3052 0.2498 -0.0086 0.0359 133 ASP C N +5772 C CA . ASP C 134 ? 1.5544 0.9962 1.3244 0.2508 -0.0095 0.0359 133 ASP C CA +5773 C C . ASP C 134 ? 1.8665 1.3115 1.6416 0.2487 -0.0087 0.0352 133 ASP C C +5774 O O . ASP C 134 ? 1.8217 1.2718 1.6041 0.2492 -0.0093 0.0350 133 ASP C O +5775 C CB . ASP C 134 ? 2.3591 1.7976 2.1254 0.2527 -0.0114 0.0362 133 ASP C CB +5776 C CG . ASP C 134 ? 2.6940 2.1240 2.4500 0.2516 -0.0117 0.0358 133 ASP C CG +5777 O OD1 . ASP C 134 ? 2.6377 2.0617 2.3855 0.2505 -0.0110 0.0358 133 ASP C OD1 +5778 O OD2 . ASP C 134 ? 2.8443 2.2735 2.6003 0.2519 -0.0128 0.0356 133 ASP C OD2 +5779 N N . GLY C 135 ? 2.0247 1.4666 1.7958 0.2464 -0.0073 0.0347 134 GLY C N +5780 C CA . GLY C 135 ? 1.8657 1.3093 1.6400 0.2443 -0.0065 0.0339 134 GLY C CA +5781 C C . GLY C 135 ? 1.9366 1.3895 1.7230 0.2438 -0.0057 0.0336 134 GLY C C +5782 O O . GLY C 135 ? 1.8961 1.3548 1.6894 0.2453 -0.0060 0.0341 134 GLY C O +5783 N N . ASN C 136 ? 1.9425 1.3969 1.7316 0.2416 -0.0047 0.0329 135 ASN C N +5784 C CA . ASN C 136 ? 1.2110 0.6740 1.0114 0.2409 -0.0039 0.0325 135 ASN C CA +5785 C C . ASN C 136 ? 1.6083 1.0741 1.4113 0.2402 -0.0025 0.0326 135 ASN C C +5786 O O . ASN C 136 ? 1.3957 0.8689 1.2078 0.2408 -0.0023 0.0328 135 ASN C O +5787 C CB . ASN C 136 ? 1.2935 0.7573 1.0963 0.2389 -0.0034 0.0316 135 ASN C CB +5788 C CG . ASN C 136 ? 1.5352 1.0008 1.3413 0.2398 -0.0048 0.0315 135 ASN C CG +5789 O OD1 . ASN C 136 ? 1.1888 0.6578 0.9992 0.2419 -0.0060 0.0321 135 ASN C OD1 +5790 N ND2 . ASN C 136 ? 1.3221 0.7853 1.1262 0.2383 -0.0046 0.0308 135 ASN C ND2 +5791 N N . ILE C 137 ? 1.4140 0.8738 1.2087 0.2390 -0.0016 0.0326 136 ILE C N +5792 C CA . ILE C 137 ? 1.6697 1.1310 1.4654 0.2383 -0.0003 0.0327 136 ILE C CA +5793 C C . ILE C 137 ? 1.7573 1.2195 1.5528 0.2406 -0.0009 0.0336 136 ILE C C +5794 O O . ILE C 137 ? 1.2663 0.7355 1.0704 0.2415 -0.0008 0.0338 136 ILE C O +5795 C CB . ILE C 137 ? 1.4635 0.9179 1.2502 0.2363 0.0009 0.0324 136 ILE C CB +5796 C CG1 . ILE C 137 ? 1.1241 0.5788 0.9124 0.2338 0.0019 0.0314 136 ILE C CG1 +5797 C CG2 . ILE C 137 ? 0.9308 0.3863 0.7176 0.2359 0.0021 0.0326 136 ILE C CG2 +5798 C CD1 . ILE C 137 ? 1.4489 0.9010 1.2350 0.2336 0.0009 0.0310 136 ILE C CD1 +5799 N N . LEU C 138 ? 1.4451 0.9000 1.2308 0.2414 -0.0015 0.0340 137 LEU C N +5800 C CA . LEU C 138 ? 1.5057 0.9602 1.2896 0.2434 -0.0019 0.0348 137 LEU C CA +5801 C C . LEU C 138 ? 1.6336 1.0932 1.4240 0.2458 -0.0032 0.0353 137 LEU C C +5802 O O . LEU C 138 ? 1.3042 0.7653 1.0956 0.2474 -0.0034 0.0359 137 LEU C O +5803 C CB . LEU C 138 ? 1.3265 0.7717 1.0981 0.2438 -0.0023 0.0351 137 LEU C CB +5804 C CG . LEU C 138 ? 1.5131 0.9534 1.2781 0.2417 -0.0009 0.0348 137 LEU C CG +5805 C CD1 . LEU C 138 ? 1.7846 1.2156 1.5374 0.2420 -0.0015 0.0350 137 LEU C CD1 +5806 C CD2 . LEU C 138 ? 1.1627 0.6071 0.9318 0.2416 0.0003 0.0350 137 LEU C CD2 +5807 N N . GLY C 139 ? 1.2631 0.7254 1.0581 0.2460 -0.0040 0.0350 138 GLY C N +5808 C CA . GLY C 139 ? 1.3542 0.8221 1.1565 0.2480 -0.0052 0.0355 138 GLY C CA +5809 C C . GLY C 139 ? 1.6366 1.1137 1.4509 0.2477 -0.0046 0.0353 138 GLY C C +5810 O O . GLY C 139 ? 1.6052 1.0877 1.4263 0.2494 -0.0054 0.0357 138 GLY C O +5811 N N . HIS C 140 ? 1.6038 1.0827 1.4205 0.2454 -0.0032 0.0347 139 HIS C N +5812 C CA . HIS C 140 ? 1.5216 1.0091 1.3495 0.2447 -0.0025 0.0344 139 HIS C CA +5813 C C . HIS C 140 ? 1.3259 0.8186 1.1616 0.2452 -0.0034 0.0342 139 HIS C C +5814 O O . HIS C 140 ? 1.3178 0.8167 1.1614 0.2466 -0.0040 0.0345 139 HIS C O +5815 C CB . HIS C 140 ? 1.5352 1.0273 1.3678 0.2458 -0.0021 0.0349 139 HIS C CB +5816 C CG . HIS C 140 ? 1.6507 1.1396 1.4782 0.2447 -0.0008 0.0350 139 HIS C CG +5817 N ND1 . HIS C 140 ? 1.4615 0.9466 1.2830 0.2459 -0.0009 0.0356 139 HIS C ND1 +5818 C CD2 . HIS C 140 ? 2.0292 1.5182 1.8568 0.2425 0.0007 0.0344 139 HIS C CD2 +5819 C CE1 . HIS C 140 ? 1.1747 0.6577 0.9928 0.2446 0.0005 0.0355 139 HIS C CE1 +5820 N NE2 . HIS C 140 ? 1.5983 1.0836 1.4200 0.2425 0.0014 0.0347 139 HIS C NE2 +5821 N N . LYS C 141 ? 1.6265 1.1164 1.4598 0.2440 -0.0036 0.0335 140 LYS C N +5822 C CA . LYS C 141 ? 1.6435 1.1379 1.4837 0.2442 -0.0044 0.0332 140 LYS C CA +5823 C C . LYS C 141 ? 1.6874 1.1850 1.5325 0.2419 -0.0032 0.0323 140 LYS C C +5824 O O . LYS C 141 ? 1.3740 0.8741 1.2235 0.2416 -0.0037 0.0319 140 LYS C O +5825 C CB . LYS C 141 ? 1.5603 1.0490 1.3939 0.2450 -0.0057 0.0333 140 LYS C CB +5826 C CG . LYS C 141 ? 1.6002 1.0863 1.4299 0.2475 -0.0070 0.0342 140 LYS C CG +5827 C CD . LYS C 141 ? 1.8971 1.3747 1.7163 0.2477 -0.0079 0.0341 140 LYS C CD +5828 C CE . LYS C 141 ? 1.8216 1.2962 1.6364 0.2502 -0.0093 0.0349 140 LYS C CE +5829 N NZ . LYS C 141 ? 1.9845 1.4506 1.7887 0.2504 -0.0102 0.0349 140 LYS C NZ +5830 N N . LEU C 142 ? 1.3728 0.8702 1.2173 0.2402 -0.0018 0.0320 141 LEU C N +5831 C CA . LEU C 142 ? 1.3159 0.8173 1.1661 0.2381 -0.0007 0.0312 141 LEU C CA +5832 C C . LEU C 142 ? 1.4547 0.9655 1.3169 0.2386 -0.0006 0.0312 141 LEU C C +5833 O O . LEU C 142 ? 1.3216 0.8350 1.1861 0.2398 -0.0007 0.0318 141 LEU C O +5834 C CB . LEU C 142 ? 1.3136 0.8113 1.1586 0.2362 0.0009 0.0308 141 LEU C CB +5835 C CG . LEU C 142 ? 0.9814 0.4698 0.8148 0.2353 0.0010 0.0306 141 LEU C CG +5836 C CD1 . LEU C 142 ? 1.1707 0.6556 0.9990 0.2335 0.0025 0.0304 141 LEU C CD1 +5837 C CD2 . LEU C 142 ? 1.2526 0.7397 1.0857 0.2343 0.0007 0.0299 141 LEU C CD2 +5838 N N . GLU C 143 ? 1.2479 0.7635 1.1173 0.2376 -0.0005 0.0305 142 GLU C N +5839 C CA . GLU C 143 ? 1.3066 0.8310 1.1874 0.2377 -0.0004 0.0304 142 GLU C CA +5840 C C . GLU C 143 ? 1.4162 0.9425 1.2989 0.2360 0.0012 0.0300 142 GLU C C +5841 O O . GLU C 143 ? 1.3670 0.8891 1.2446 0.2342 0.0022 0.0294 142 GLU C O +5842 C CB . GLU C 143 ? 1.2272 0.7558 1.1148 0.2371 -0.0008 0.0297 142 GLU C CB +5843 C CG . GLU C 143 ? 1.2486 0.7783 1.1382 0.2390 -0.0024 0.0302 142 GLU C CG +5844 C CD . GLU C 143 ? 1.7225 1.2574 1.6200 0.2384 -0.0027 0.0295 142 GLU C CD +5845 O OE1 . GLU C 143 ? 1.6545 1.1897 1.5532 0.2364 -0.0018 0.0286 142 GLU C OE1 +5846 O OE2 . GLU C 143 ? 1.5692 1.1077 1.4718 0.2399 -0.0039 0.0299 142 GLU C OE2 +5847 N N . TYR C 144 ? 1.0107 0.5433 0.9007 0.2365 0.0014 0.0303 143 TYR C N +5848 C CA . TYR C 144 ? 1.0914 0.6265 0.9841 0.2350 0.0028 0.0299 143 TYR C CA +5849 C C . TYR C 144 ? 1.2658 0.8046 1.1644 0.2329 0.0035 0.0288 143 TYR C C +5850 O O . TYR C 144 ? 1.0482 0.5941 0.9559 0.2326 0.0037 0.0286 143 TYR C O +5851 C CB . TYR C 144 ? 1.0364 0.5775 0.9358 0.2361 0.0027 0.0305 143 TYR C CB +5852 C CG . TYR C 144 ? 1.1127 0.6541 1.0116 0.2348 0.0041 0.0303 143 TYR C CG +5853 C CD1 . TYR C 144 ? 1.3682 0.9030 1.2583 0.2335 0.0051 0.0301 143 TYR C CD1 +5854 C CD2 . TYR C 144 ? 1.2460 0.7942 1.1529 0.2349 0.0045 0.0304 143 TYR C CD2 +5855 C CE1 . TYR C 144 ? 1.2225 0.7573 1.1119 0.2323 0.0063 0.0299 143 TYR C CE1 +5856 C CE2 . TYR C 144 ? 1.1427 0.6911 1.0490 0.2338 0.0057 0.0302 143 TYR C CE2 +5857 C CZ . TYR C 144 ? 1.2689 0.8105 1.1664 0.2325 0.0066 0.0300 143 TYR C CZ +5858 O OH . TYR C 144 ? 1.1785 0.7200 1.0751 0.2313 0.0079 0.0299 143 TYR C OH +5859 N N . ASN C 145 ? 1.0898 0.6239 0.9833 0.2316 0.0038 0.0282 144 ASN C N +5860 C CA . ASN C 145 ? 1.1001 0.6375 0.9990 0.2296 0.0046 0.0271 144 ASN C CA +5861 C C . ASN C 145 ? 0.8659 0.3972 0.7575 0.2276 0.0056 0.0264 144 ASN C C +5862 O O . ASN C 145 ? 1.1518 0.6763 1.0341 0.2274 0.0059 0.0267 144 ASN C O +5863 C CB . ASN C 145 ? 0.7717 0.3140 0.6779 0.2301 0.0036 0.0268 144 ASN C CB +5864 C CG . ASN C 145 ? 1.4282 0.9655 1.3287 0.2311 0.0025 0.0270 144 ASN C CG +5865 O OD1 . ASN C 145 ? 1.0718 0.6027 0.9645 0.2301 0.0028 0.0267 144 ASN C OD1 +5866 N ND2 . ASN C 145 ? 1.3110 0.8515 1.2157 0.2330 0.0012 0.0276 144 ASN C ND2 +5867 N N . TYR C 146 ? 1.1187 0.6525 1.0147 0.2260 0.0060 0.0254 145 TYR C N +5868 C CA . TYR C 146 ? 1.3224 0.8509 1.2123 0.2239 0.0071 0.0246 145 TYR C CA +5869 C C . TYR C 146 ? 1.1865 0.7171 1.0807 0.2227 0.0070 0.0236 145 TYR C C +5870 O O . TYR C 146 ? 1.2491 0.7864 1.1524 0.2233 0.0064 0.0234 145 TYR C O +5871 C CB . TYR C 146 ? 0.8945 0.4229 0.7838 0.2223 0.0085 0.0243 145 TYR C CB +5872 C CG . TYR C 146 ? 1.0965 0.6163 0.9745 0.2214 0.0093 0.0243 145 TYR C CG +5873 C CD1 . TYR C 146 ? 1.0537 0.5684 0.9239 0.2227 0.0089 0.0253 145 TYR C CD1 +5874 C CD2 . TYR C 146 ? 1.4326 0.9495 1.3077 0.2191 0.0104 0.0234 145 TYR C CD2 +5875 C CE1 . TYR C 146 ? 1.2358 0.7424 1.0955 0.2217 0.0095 0.0253 145 TYR C CE1 +5876 C CE2 . TYR C 146 ? 1.2895 0.7984 1.1542 0.2181 0.0111 0.0234 145 TYR C CE2 +5877 C CZ . TYR C 146 ? 1.0036 0.5073 0.8605 0.2194 0.0107 0.0244 145 TYR C CZ +5878 O OH . TYR C 146 ? 1.1027 0.5985 0.9493 0.2183 0.0113 0.0244 145 TYR C OH +5879 N N . ASN C 147 ? 1.4018 0.9265 1.2892 0.2212 0.0077 0.0229 146 ASN C N +5880 C CA . ASN C 147 ? 1.0757 0.6014 0.9660 0.2199 0.0078 0.0219 146 ASN C CA +5881 C C . ASN C 147 ? 1.2609 0.7846 1.1491 0.2174 0.0093 0.0209 146 ASN C C +5882 O O . ASN C 147 ? 1.2093 0.7304 1.0933 0.2168 0.0102 0.0211 146 ASN C O +5883 C CB . ASN C 147 ? 1.2314 0.7512 1.1149 0.2204 0.0069 0.0220 146 ASN C CB +5884 C CG . ASN C 147 ? 1.1344 0.6558 1.0196 0.2229 0.0053 0.0229 146 ASN C CG +5885 O OD1 . ASN C 147 ? 1.1854 0.7139 1.0798 0.2238 0.0047 0.0230 146 ASN C OD1 +5886 N ND2 . ASN C 147 ? 1.7278 1.2424 1.6039 0.2239 0.0045 0.0236 146 ASN C ND2 +5887 N N . SER C 148 ? 1.2688 0.7936 1.1599 0.2160 0.0097 0.0198 147 SER C N +5888 C CA . SER C 148 ? 1.1294 0.6531 1.0197 0.2136 0.0112 0.0188 147 SER C CA +5889 C C . SER C 148 ? 0.9081 0.4235 0.7885 0.2123 0.0116 0.0184 147 SER C C +5890 O O . SER C 148 ? 1.7248 1.2374 1.6022 0.2130 0.0107 0.0185 147 SER C O +5891 C CB . SER C 148 ? 0.9741 0.5053 0.8750 0.2127 0.0114 0.0177 147 SER C CB +5892 O OG . SER C 148 ? 1.3510 0.8895 1.2604 0.2134 0.0113 0.0180 147 SER C OG +5893 N N . HIS C 149 ? 1.0442 0.5556 0.9195 0.2105 0.0130 0.0179 148 HIS C N +5894 C CA . HIS C 149 ? 1.3304 0.8330 1.1950 0.2093 0.0134 0.0177 148 HIS C CA +5895 C C . HIS C 149 ? 1.3254 0.8266 1.1890 0.2066 0.0150 0.0165 148 HIS C C +5896 O O . HIS C 149 ? 1.4077 0.9135 1.2770 0.2057 0.0159 0.0160 148 HIS C O +5897 C CB . HIS C 149 ? 1.0978 0.5942 0.9530 0.2101 0.0133 0.0189 148 HIS C CB +5898 C CG . HIS C 149 ? 1.2168 0.7141 1.0722 0.2128 0.0117 0.0200 148 HIS C CG +5899 N ND1 . HIS C 149 ? 1.2778 0.7775 1.1349 0.2142 0.0114 0.0210 148 HIS C ND1 +5900 C CD2 . HIS C 149 ? 1.7901 1.2863 1.6445 0.2142 0.0103 0.0204 148 HIS C CD2 +5901 C CE1 . HIS C 149 ? 1.4832 0.9833 1.3403 0.2165 0.0100 0.0218 148 HIS C CE1 +5902 N NE2 . HIS C 149 ? 1.1185 0.6164 0.9739 0.2165 0.0093 0.0215 148 HIS C NE2 +5903 N N . ASN C 150 ? 1.2537 0.7485 1.1101 0.2052 0.0154 0.0160 149 ASN C N +5904 C CA . ASN C 150 ? 1.3732 0.8658 1.2277 0.2026 0.0170 0.0148 149 ASN C CA +5905 C C . ASN C 150 ? 1.1939 0.6779 1.0368 0.2017 0.0177 0.0153 149 ASN C C +5906 O O . ASN C 150 ? 1.4651 0.9427 1.2996 0.2022 0.0171 0.0158 149 ASN C O +5907 C CB . ASN C 150 ? 1.5408 1.0331 1.3965 0.2014 0.0171 0.0136 149 ASN C CB +5908 C CG . ASN C 150 ? 1.4618 0.9626 1.3292 0.2022 0.0164 0.0131 149 ASN C CG +5909 O OD1 . ASN C 150 ? 1.7656 1.2732 1.6415 0.2019 0.0168 0.0127 149 ASN C OD1 +5910 N ND2 . ASN C 150 ? 1.6086 1.1092 1.4764 0.2031 0.0153 0.0131 149 ASN C ND2 +5911 N N . VAL C 151 ? 1.4036 0.8878 1.2463 0.2003 0.0190 0.0150 150 VAL C N +5912 C CA . VAL C 151 ? 1.0718 0.5488 0.9045 0.1995 0.0197 0.0156 150 VAL C CA +5913 C C . VAL C 151 ? 1.5476 1.0192 1.3746 0.1967 0.0211 0.0145 150 VAL C C +5914 O O . VAL C 151 ? 1.6453 1.1191 1.4755 0.1950 0.0224 0.0137 150 VAL C O +5915 C CB . VAL C 151 ? 1.5187 0.9993 1.3547 0.1998 0.0203 0.0161 150 VAL C CB +5916 C CG1 . VAL C 151 ? 1.0263 0.5004 0.8534 0.1983 0.0215 0.0162 150 VAL C CG1 +5917 C CG2 . VAL C 151 ? 1.2371 0.7210 1.0759 0.2026 0.0190 0.0173 150 VAL C CG2 +5918 N N . TYR C 152 ? 1.3273 0.7918 1.1458 0.1963 0.0208 0.0145 151 TYR C N +5919 C CA . TYR C 152 ? 1.3785 0.8382 1.1920 0.1936 0.0221 0.0134 151 TYR C CA +5920 C C . TYR C 152 ? 1.3647 0.8184 1.1701 0.1919 0.0234 0.0135 151 TYR C C +5921 O O . TYR C 152 ? 1.4386 0.8872 1.2363 0.1927 0.0230 0.0145 151 TYR C O +5922 C CB . TYR C 152 ? 1.2856 0.7403 1.0937 0.1934 0.0215 0.0131 151 TYR C CB +5923 C CG . TYR C 152 ? 1.4030 0.8635 1.2191 0.1951 0.0202 0.0130 151 TYR C CG +5924 C CD1 . TYR C 152 ? 1.2398 0.7012 1.0562 0.1977 0.0186 0.0141 151 TYR C CD1 +5925 C CD2 . TYR C 152 ? 1.4229 0.8880 1.2463 0.1940 0.0206 0.0117 151 TYR C CD2 +5926 C CE1 . TYR C 152 ? 1.7991 1.2659 1.6228 0.1992 0.0174 0.0140 151 TYR C CE1 +5927 C CE2 . TYR C 152 ? 1.3332 0.8037 1.1640 0.1955 0.0195 0.0116 151 TYR C CE2 +5928 C CZ . TYR C 152 ? 1.6102 1.0814 1.4410 0.1981 0.0178 0.0128 151 TYR C CZ +5929 O OH . TYR C 152 ? 1.3160 0.7925 1.1540 0.1996 0.0167 0.0127 151 TYR C OH +5930 N N . ILE C 153 ? 1.3622 0.8168 1.1696 0.1895 0.0249 0.0124 152 ILE C N +5931 C CA . ILE C 153 ? 1.4723 0.9220 1.2731 0.1877 0.0263 0.0123 152 ILE C CA +5932 C C . ILE C 153 ? 1.7672 1.2108 1.5615 0.1850 0.0274 0.0113 152 ILE C C +5933 O O . ILE C 153 ? 1.7574 1.2021 1.5545 0.1845 0.0272 0.0104 152 ILE C O +5934 C CB . ILE C 153 ? 1.3460 0.8021 1.1548 0.1870 0.0273 0.0119 152 ILE C CB +5935 C CG1 . ILE C 153 ? 1.0439 0.5067 0.8600 0.1897 0.0261 0.0129 152 ILE C CG1 +5936 C CG2 . ILE C 153 ? 1.1760 0.6273 0.9782 0.1853 0.0286 0.0120 152 ILE C CG2 +5937 C CD1 . ILE C 153 ? 1.6372 1.1067 1.4615 0.1892 0.0269 0.0125 152 ILE C CD1 +5938 N N . MET C 154 ? 1.8666 1.3031 1.6515 0.1835 0.0284 0.0114 153 MET C N +5939 C CA . MET C 154 ? 1.9224 1.3486 1.6947 0.1820 0.0300 0.0108 153 MET C CA +5940 C C . MET C 154 ? 1.7283 1.1485 1.4922 0.1807 0.0315 0.0110 153 MET C C +5941 O O . MET C 154 ? 1.7671 1.1872 1.5297 0.1814 0.0308 0.0121 153 MET C O +5942 C CB . MET C 154 ? 1.9436 1.3631 1.7073 0.1830 0.0288 0.0114 153 MET C CB +5943 C CG . MET C 154 ? 2.1538 1.5639 1.9061 0.1816 0.0301 0.0105 153 MET C CG +5944 S SD . MET C 154 ? 2.9819 2.3849 2.7251 0.1829 0.0285 0.0113 153 MET C SD +5945 C CE . MET C 154 ? 1.6256 1.0398 1.3831 0.1853 0.0260 0.0119 153 MET C CE +5946 N N . ALA C 155 ? 1.6525 1.0678 1.4108 0.1787 0.0336 0.0100 154 ALA C N +5947 C CA . ALA C 155 ? 1.7449 1.1544 1.4951 0.1773 0.0352 0.0101 154 ALA C CA +5948 C C . ALA C 155 ? 2.0874 1.4861 1.8231 0.1772 0.0351 0.0110 154 ALA C C +5949 O O . ALA C 155 ? 1.8077 1.2009 1.5368 0.1774 0.0346 0.0109 154 ALA C O +5950 C CB . ALA C 155 ? 1.4925 0.8996 1.2406 0.1750 0.0375 0.0088 154 ALA C CB +5951 N N . ASP C 156 ? 2.1781 1.5738 1.9089 0.1769 0.0354 0.0117 155 ASP C N +5952 C CA . ASP C 156 ? 2.4444 1.8293 2.1608 0.1763 0.0357 0.0124 155 ASP C CA +5953 C C . ASP C 156 ? 2.6752 2.0544 2.3843 0.1740 0.0380 0.0119 155 ASP C C +5954 O O . ASP C 156 ? 2.1723 1.5517 1.8808 0.1739 0.0383 0.0125 155 ASP C O +5955 C CB . ASP C 156 ? 2.3691 1.7553 2.0857 0.1782 0.0339 0.0138 155 ASP C CB +5956 C CG . ASP C 156 ? 2.4229 1.7979 2.1246 0.1779 0.0339 0.0145 155 ASP C CG +5957 O OD1 . ASP C 156 ? 2.5429 1.9091 2.2339 0.1761 0.0352 0.0139 155 ASP C OD1 +5958 O OD2 . ASP C 156 ? 2.0306 1.4057 1.7314 0.1793 0.0325 0.0156 155 ASP C OD2 +5959 N N . LYS C 157 ? 2.8833 2.2575 2.5871 0.1721 0.0397 0.0108 156 LYS C N +5960 C CA . LYS C 157 ? 2.7314 2.1014 2.4301 0.1697 0.0421 0.0100 156 LYS C CA +5961 C C . LYS C 157 ? 2.4643 1.8250 2.1502 0.1687 0.0427 0.0108 156 LYS C C +5962 O O . LYS C 157 ? 1.9770 1.3361 1.6607 0.1672 0.0443 0.0106 156 LYS C O +5963 C CB . LYS C 157 ? 2.6231 1.9894 2.3185 0.1679 0.0438 0.0086 156 LYS C CB +5964 C CG . LYS C 157 ? 2.6373 2.0134 2.3462 0.1680 0.0441 0.0075 156 LYS C CG +5965 C CD . LYS C 157 ? 2.5083 1.8811 2.2144 0.1665 0.0454 0.0061 156 LYS C CD +5966 C CE . LYS C 157 ? 2.4352 1.8172 2.1541 0.1664 0.0461 0.0050 156 LYS C CE +5967 N NZ . LYS C 157 ? 2.3280 1.7208 2.0605 0.1687 0.0439 0.0053 156 LYS C NZ +5968 N N . GLN C 158 ? 2.6798 2.0345 2.3574 0.1696 0.0415 0.0116 157 GLN C N +5969 C CA . GLN C 158 ? 2.7061 2.0518 2.3713 0.1688 0.0418 0.0124 157 GLN C CA +5970 C C . GLN C 158 ? 2.5000 1.8502 2.1697 0.1701 0.0410 0.0135 157 GLN C C +5971 O O . GLN C 158 ? 2.2493 1.5946 1.9121 0.1690 0.0420 0.0138 157 GLN C O +5972 C CB . GLN C 158 ? 2.6451 1.9824 2.2993 0.1693 0.0408 0.0129 157 GLN C CB +5973 C CG . GLN C 158 ? 2.8916 2.2223 2.5386 0.1676 0.0419 0.0118 157 GLN C CG +5974 C CD . GLN C 158 ? 2.9510 2.2731 2.5875 0.1645 0.0444 0.0111 157 GLN C CD +5975 O OE1 . GLN C 158 ? 3.0372 2.3622 2.6778 0.1632 0.0461 0.0105 157 GLN C OE1 +5976 N NE2 . GLN C 158 ? 2.7214 2.0327 2.3442 0.1633 0.0448 0.0111 157 GLN C NE2 +5977 N N . LYS C 159 ? 2.5815 1.9411 2.2628 0.1724 0.0391 0.0140 158 LYS C N +5978 C CA . LYS C 159 ? 2.3710 1.7351 2.0568 0.1737 0.0382 0.0150 158 LYS C CA +5979 C C . LYS C 159 ? 2.2412 1.6149 1.9394 0.1736 0.0387 0.0147 158 LYS C C +5980 O O . LYS C 159 ? 1.7584 1.1373 1.4622 0.1747 0.0379 0.0154 158 LYS C O +5981 C CB . LYS C 159 ? 2.0482 1.4156 1.7375 0.1763 0.0357 0.0160 158 LYS C CB +5982 C CG . LYS C 159 ? 2.6921 2.0503 2.3695 0.1766 0.0349 0.0164 158 LYS C CG +5983 C CD . LYS C 159 ? 2.8605 2.2070 2.5227 0.1746 0.0364 0.0164 158 LYS C CD +5984 C CE . LYS C 159 ? 2.5659 1.9034 2.2172 0.1739 0.0364 0.0161 158 LYS C CE +5985 N NZ . LYS C 159 ? 2.5055 1.8320 2.1428 0.1714 0.0382 0.0157 158 LYS C NZ +5986 N N . ASN C 160 ? 2.2271 1.6031 1.9294 0.1723 0.0401 0.0135 159 ASN C N +5987 C CA . ASN C 160 ? 2.2453 1.6297 1.9585 0.1719 0.0409 0.0129 159 ASN C CA +5988 C C . ASN C 160 ? 2.0832 1.4790 1.8106 0.1741 0.0389 0.0135 159 ASN C C +5989 O O . ASN C 160 ? 1.8888 1.2912 1.6242 0.1743 0.0389 0.0136 159 ASN C O +5990 C CB . ASN C 160 ? 2.2088 1.5896 1.9168 0.1705 0.0423 0.0132 159 ASN C CB +5991 C CG . ASN C 160 ? 2.4168 1.8042 2.1338 0.1694 0.0436 0.0123 159 ASN C CG +5992 O OD1 . ASN C 160 ? 2.3460 1.7364 2.0680 0.1687 0.0444 0.0112 159 ASN C OD1 +5993 N ND2 . ASN C 160 ? 2.2395 1.6291 1.9585 0.1694 0.0438 0.0129 159 ASN C ND2 +5994 N N . GLY C 161 ? 1.9239 1.3220 1.6544 0.1757 0.0372 0.0137 160 GLY C N +5995 C CA . GLY C 161 ? 1.8865 1.2950 1.6300 0.1777 0.0353 0.0142 160 GLY C CA +5996 C C . GLY C 161 ? 1.7598 1.1721 1.5091 0.1786 0.0343 0.0137 160 GLY C C +5997 O O . GLY C 161 ? 1.8035 1.2132 1.5506 0.1774 0.0355 0.0127 160 GLY C O +5998 N N . ILE C 162 ? 1.7426 1.1610 1.4993 0.1806 0.0323 0.0144 161 ILE C N +5999 C CA . ILE C 162 ? 1.7507 1.1726 1.5129 0.1815 0.0311 0.0140 161 ILE C CA +6000 C C . ILE C 162 ? 1.6608 1.0798 1.4184 0.1837 0.0294 0.0152 161 ILE C C +6001 O O . ILE C 162 ? 1.6177 1.0349 1.3717 0.1852 0.0288 0.0163 161 ILE C O +6002 C CB . ILE C 162 ? 1.7077 1.1403 1.4837 0.1826 0.0308 0.0136 161 ILE C CB +6003 C CG1 . ILE C 162 ? 1.7832 1.2200 1.5629 0.1852 0.0298 0.0149 161 ILE C CG1 +6004 C CG2 . ILE C 162 ? 1.7831 1.2195 1.5649 0.1804 0.0323 0.0124 161 ILE C CG2 +6005 C CD1 . ILE C 162 ? 1.2912 0.7379 1.0836 0.1866 0.0292 0.0146 161 ILE C CD1 +6006 N N . LYS C 163 ? 1.5826 1.0005 1.3397 0.1840 0.0287 0.0148 162 LYS C N +6007 C CA . LYS C 163 ? 1.5860 1.0019 1.3399 0.1863 0.0270 0.0158 162 LYS C CA +6008 C C . LYS C 163 ? 1.6647 1.0892 1.4297 0.1884 0.0259 0.0157 162 LYS C C +6009 O O . LYS C 163 ? 1.8129 1.2429 1.5859 0.1874 0.0265 0.0147 162 LYS C O +6010 C CB . LYS C 163 ? 1.8976 1.3064 1.6433 0.1853 0.0267 0.0154 162 LYS C CB +6011 C CG . LYS C 163 ? 2.3620 1.7623 2.0959 0.1859 0.0260 0.0165 162 LYS C CG +6012 C CD . LYS C 163 ? 2.3654 1.7553 2.0866 0.1851 0.0265 0.0161 162 LYS C CD +6013 C CE . LYS C 163 ? 2.3577 1.7381 2.0657 0.1852 0.0261 0.0170 162 LYS C CE +6014 N NZ . LYS C 163 ? 2.3162 1.6925 2.0182 0.1839 0.0276 0.0171 162 LYS C NZ +6015 N N . VAL C 164 ? 1.4120 0.8381 1.1780 0.1911 0.0245 0.0168 163 VAL C N +6016 C CA . VAL C 164 ? 1.4592 0.8937 1.2359 0.1930 0.0235 0.0168 163 VAL C CA +6017 C C . VAL C 164 ? 1.2455 0.6783 1.0197 0.1953 0.0217 0.0176 163 VAL C C +6018 O O . VAL C 164 ? 1.7174 1.1450 1.4839 0.1964 0.0210 0.0186 163 VAL C O +6019 C CB . VAL C 164 ? 1.7448 1.1860 1.5290 0.1943 0.0235 0.0173 163 VAL C CB +6020 C CG1 . VAL C 164 ? 1.2368 0.6870 1.0327 0.1958 0.0227 0.0172 163 VAL C CG1 +6021 C CG2 . VAL C 164 ? 1.6141 1.0560 1.3993 0.1921 0.0252 0.0167 163 VAL C CG2 +6022 N N . ASN C 165 ? 1.2819 0.7190 1.0624 0.1961 0.0209 0.0172 164 ASN C N +6023 C CA . ASN C 165 ? 1.4754 0.9119 1.2547 0.1985 0.0191 0.0180 164 ASN C CA +6024 C C . ASN C 165 ? 1.3179 0.7624 1.1078 0.2001 0.0182 0.0179 164 ASN C C +6025 O O . ASN C 165 ? 1.6362 1.0854 1.4333 0.1989 0.0188 0.0168 164 ASN C O +6026 C CB . ASN C 165 ? 1.4427 0.8707 1.2117 0.1978 0.0188 0.0180 164 ASN C CB +6027 C CG . ASN C 165 ? 1.8061 1.2338 1.5764 0.1958 0.0194 0.0167 164 ASN C CG +6028 O OD1 . ASN C 165 ? 2.0431 1.4708 1.8142 0.1935 0.0209 0.0158 164 ASN C OD1 +6029 N ND2 . ASN C 165 ? 2.2606 1.6878 2.0310 0.1967 0.0183 0.0166 164 ASN C ND2 +6030 N N . PHE C 166 ? 1.0385 0.4845 0.8295 0.2027 0.0166 0.0189 165 PHE C N +6031 C CA . PHE C 166 ? 1.4117 0.8650 1.2124 0.2044 0.0155 0.0189 165 PHE C CA +6032 C C . PHE C 166 ? 1.1125 0.5652 0.9113 0.2071 0.0138 0.0200 165 PHE C C +6033 O O . PHE C 166 ? 1.5831 1.0296 1.3731 0.2077 0.0135 0.0208 165 PHE C O +6034 C CB . PHE C 166 ? 1.4848 0.9469 1.2964 0.2045 0.0161 0.0186 165 PHE C CB +6035 C CG . PHE C 166 ? 1.4851 0.9477 1.2958 0.2050 0.0165 0.0194 165 PHE C CG +6036 C CD1 . PHE C 166 ? 1.2665 0.7254 1.0724 0.2031 0.0180 0.0191 165 PHE C CD1 +6037 C CD2 . PHE C 166 ? 0.8306 0.2976 0.6458 0.2074 0.0155 0.0203 165 PHE C CD2 +6038 C CE1 . PHE C 166 ? 1.0507 0.5101 0.8559 0.2036 0.0184 0.0198 165 PHE C CE1 +6039 C CE2 . PHE C 166 ? 1.1888 0.6564 1.0035 0.2079 0.0159 0.0210 165 PHE C CE2 +6040 C CZ . PHE C 166 ? 1.3396 0.8034 1.1492 0.2060 0.0173 0.0207 165 PHE C CZ +6041 N N . LYS C 167 ? 1.1746 0.6338 0.9819 0.2088 0.0128 0.0202 166 LYS C N +6042 C CA . LYS C 167 ? 1.4595 0.9180 1.2653 0.2114 0.0111 0.0211 166 LYS C CA +6043 C C . LYS C 167 ? 1.5366 1.0037 1.3530 0.2133 0.0103 0.0216 166 LYS C C +6044 O O . LYS C 167 ? 1.4644 0.9372 1.2889 0.2136 0.0099 0.0211 166 LYS C O +6045 C CB . LYS C 167 ? 1.0968 0.5514 0.8987 0.2113 0.0102 0.0208 166 LYS C CB +6046 C CG . LYS C 167 ? 1.8011 1.2554 1.6022 0.2139 0.0084 0.0217 166 LYS C CG +6047 C CD . LYS C 167 ? 2.1225 1.5747 1.9222 0.2137 0.0076 0.0212 166 LYS C CD +6048 C CE . LYS C 167 ? 1.8143 1.2590 1.6053 0.2113 0.0085 0.0205 166 LYS C CE +6049 N NZ . LYS C 167 ? 2.2819 1.7180 2.0610 0.2114 0.0084 0.0211 166 LYS C NZ +6050 N N . ILE C 168 ? 1.3113 0.7794 1.1274 0.2148 0.0100 0.0225 167 ILE C N +6051 C CA . ILE C 168 ? 1.3933 0.8693 1.2190 0.2166 0.0093 0.0229 167 ILE C CA +6052 C C . ILE C 168 ? 1.3053 0.7822 1.1321 0.2189 0.0076 0.0236 167 ILE C C +6053 O O . ILE C 168 ? 1.2883 0.7594 1.1071 0.2200 0.0067 0.0243 167 ILE C O +6054 C CB . ILE C 168 ? 1.1625 0.6390 0.9872 0.2173 0.0097 0.0237 167 ILE C CB +6055 C CG1 . ILE C 168 ? 1.3735 0.8484 1.1962 0.2150 0.0115 0.0231 167 ILE C CG1 +6056 C CG2 . ILE C 168 ? 1.1830 0.6680 1.0180 0.2190 0.0091 0.0241 167 ILE C CG2 +6057 C CD1 . ILE C 168 ? 1.6205 1.1026 1.4530 0.2137 0.0124 0.0223 167 ILE C CD1 +6058 N N . ARG C 169 ? 1.0258 0.5102 0.8626 0.2197 0.0070 0.0234 168 ARG C N +6059 C CA . ARG C 169 ? 1.1918 0.6779 1.0308 0.2220 0.0053 0.0240 168 ARG C CA +6060 C C . ARG C 169 ? 1.1516 0.6434 0.9967 0.2239 0.0049 0.0249 168 ARG C C +6061 O O . ARG C 169 ? 1.4433 0.9423 1.2976 0.2236 0.0053 0.0246 168 ARG C O +6062 C CB . ARG C 169 ? 1.3657 0.8562 1.2116 0.2217 0.0049 0.0233 168 ARG C CB +6063 C CG . ARG C 169 ? 1.5084 0.9934 1.3485 0.2200 0.0053 0.0225 168 ARG C CG +6064 C CD . ARG C 169 ? 1.4697 0.9589 1.3166 0.2199 0.0048 0.0218 168 ARG C CD +6065 N NE . ARG C 169 ? 1.6752 1.1717 1.5320 0.2187 0.0057 0.0209 168 ARG C NE +6066 C CZ . ARG C 169 ? 1.9754 1.4713 1.8320 0.2164 0.0072 0.0200 168 ARG C CZ +6067 N NH1 . ARG C 169 ? 1.6748 1.1630 1.5218 0.2149 0.0080 0.0197 168 ARG C NH1 +6068 N NH2 . ARG C 169 ? 1.8749 1.3778 1.7410 0.2155 0.0079 0.0193 168 ARG C NH2 +6069 N N . HIS C 170 ? 1.1297 0.6183 0.9696 0.2257 0.0039 0.0258 169 HIS C N +6070 C CA . HIS C 170 ? 1.3483 0.8422 1.1940 0.2277 0.0033 0.0266 169 HIS C CA +6071 C C . HIS C 170 ? 1.0088 0.5062 0.8593 0.2296 0.0017 0.0270 169 HIS C C +6072 O O . HIS C 170 ? 1.5880 1.0807 1.4330 0.2304 0.0007 0.0272 169 HIS C O +6073 C CB . HIS C 170 ? 1.0867 0.5757 0.9248 0.2287 0.0033 0.0275 169 HIS C CB +6074 C CG . HIS C 170 ? 1.2461 0.7315 1.0790 0.2269 0.0048 0.0273 169 HIS C CG +6075 N ND1 . HIS C 170 ? 1.4149 0.9044 1.2522 0.2265 0.0057 0.0274 169 HIS C ND1 +6076 C CD2 . HIS C 170 ? 1.5129 0.9906 1.3363 0.2254 0.0054 0.0270 169 HIS C CD2 +6077 C CE1 . HIS C 170 ? 1.3601 0.8448 1.1911 0.2248 0.0070 0.0271 169 HIS C CE1 +6078 N NE2 . HIS C 170 ? 1.0158 0.4934 0.8383 0.2241 0.0068 0.0269 169 HIS C NE2 +6079 N N . ASN C 171 ? 1.6624 1.1679 1.5233 0.2304 0.0015 0.0271 170 ASN C N +6080 C CA . ASN C 171 ? 1.3043 0.8136 1.1703 0.2324 0.0000 0.0275 170 ASN C CA +6081 C C . ASN C 171 ? 1.5050 1.0123 1.3674 0.2346 -0.0010 0.0286 170 ASN C C +6082 O O . ASN C 171 ? 1.7341 1.2412 1.5950 0.2349 -0.0004 0.0291 170 ASN C O +6083 C CB . ASN C 171 ? 1.5309 1.0497 1.4093 0.2324 0.0002 0.0273 170 ASN C CB +6084 C CG . ASN C 171 ? 1.5038 1.0252 1.3870 0.2307 0.0006 0.0262 170 ASN C CG +6085 O OD1 . ASN C 171 ? 1.4727 0.9892 1.3502 0.2290 0.0013 0.0255 170 ASN C OD1 +6086 N ND2 . ASN C 171 ? 1.4599 0.9890 1.3535 0.2310 0.0003 0.0260 170 ASN C ND2 +6087 N N . ILE C 172 ? 1.4558 0.9620 1.3170 0.2363 -0.0024 0.0290 171 ILE C N +6088 C CA . ILE C 172 ? 1.4416 0.9459 1.2995 0.2386 -0.0036 0.0300 171 ILE C CA +6089 C C . ILE C 172 ? 1.6782 1.1893 1.5453 0.2402 -0.0048 0.0303 171 ILE C C +6090 O O . ILE C 172 ? 2.1162 1.6314 1.9896 0.2395 -0.0048 0.0297 171 ILE C O +6091 C CB . ILE C 172 ? 1.3998 0.8953 1.2467 0.2390 -0.0044 0.0302 171 ILE C CB +6092 C CG1 . ILE C 172 ? 1.3672 0.8561 1.2053 0.2372 -0.0031 0.0299 171 ILE C CG1 +6093 C CG2 . ILE C 172 ? 1.1800 0.6733 1.0232 0.2414 -0.0057 0.0312 171 ILE C CG2 +6094 C CD1 . ILE C 172 ? 1.5316 1.0122 1.3596 0.2368 -0.0036 0.0297 171 ILE C CD1 +6095 N N . GLU C 173 ? 1.1342 0.6467 1.0024 0.2424 -0.0057 0.0312 172 GLU C N +6096 C CA . GLU C 173 ? 1.8522 1.3718 1.7299 0.2437 -0.0067 0.0315 172 GLU C CA +6097 C C . GLU C 173 ? 1.9550 1.4739 1.8331 0.2443 -0.0079 0.0313 172 GLU C C +6098 O O . GLU C 173 ? 2.0726 1.5975 1.9592 0.2441 -0.0081 0.0309 172 GLU C O +6099 C CB . GLU C 173 ? 1.5865 1.1085 1.4663 0.2459 -0.0073 0.0324 172 GLU C CB +6100 C CG . GLU C 173 ? 2.2493 1.7801 2.1408 0.2467 -0.0079 0.0325 172 GLU C CG +6101 C CD . GLU C 173 ? 2.7527 2.2865 2.6472 0.2488 -0.0086 0.0334 172 GLU C CD +6102 O OE1 . GLU C 173 ? 2.5003 2.0292 2.3880 0.2504 -0.0094 0.0340 172 GLU C OE1 +6103 O OE2 . GLU C 173 ? 2.9314 2.4725 2.8351 0.2490 -0.0084 0.0335 172 GLU C OE2 +6104 N N . ASP C 174 ? 1.4930 1.0047 1.3619 0.2449 -0.0087 0.0314 173 ASP C N +6105 C CA . ASP C 174 ? 1.7932 1.3038 1.6618 0.2455 -0.0099 0.0313 173 ASP C CA +6106 C C . ASP C 174 ? 2.0949 1.6060 1.9655 0.2435 -0.0094 0.0303 173 ASP C C +6107 O O . ASP C 174 ? 2.8359 2.3450 2.7048 0.2437 -0.0103 0.0301 173 ASP C O +6108 C CB . ASP C 174 ? 2.0189 1.5212 1.8767 0.2466 -0.0110 0.0317 173 ASP C CB +6109 C CG . ASP C 174 ? 1.9642 1.4590 1.8120 0.2451 -0.0100 0.0315 173 ASP C CG +6110 O OD1 . ASP C 174 ? 1.9307 1.4262 1.7796 0.2430 -0.0086 0.0308 173 ASP C OD1 +6111 O OD2 . ASP C 174 ? 1.9221 1.4104 1.7610 0.2460 -0.0106 0.0319 173 ASP C OD2 +6112 N N . GLY C 175 ? 1.5258 1.0396 1.3997 0.2416 -0.0079 0.0297 174 GLY C N +6113 C CA . GLY C 175 ? 1.4409 0.9554 1.3170 0.2396 -0.0072 0.0287 174 GLY C CA +6114 C C . GLY C 175 ? 1.6264 1.1332 1.4928 0.2380 -0.0065 0.0282 174 GLY C C +6115 O O . GLY C 175 ? 1.6889 1.1962 1.5568 0.2361 -0.0057 0.0273 174 GLY C O +6116 N N . SER C 176 ? 1.1922 0.6919 1.0488 0.2386 -0.0068 0.0287 175 SER C N +6117 C CA . SER C 176 ? 1.6198 1.1116 1.4665 0.2370 -0.0061 0.0282 175 SER C CA +6118 C C . SER C 176 ? 1.5025 0.9943 1.3487 0.2351 -0.0044 0.0278 175 SER C C +6119 O O . SER C 176 ? 1.4564 0.9542 1.3097 0.2351 -0.0038 0.0279 175 SER C O +6120 C CB . SER C 176 ? 1.6668 1.1506 1.5027 0.2382 -0.0071 0.0289 175 SER C CB +6121 O OG . SER C 176 ? 1.5806 1.0649 1.4159 0.2399 -0.0075 0.0297 175 SER C OG +6122 N N . VAL C 177 ? 1.4377 0.9227 1.2754 0.2334 -0.0036 0.0274 176 VAL C N +6123 C CA . VAL C 177 ? 1.3285 0.8132 1.1655 0.2314 -0.0019 0.0269 176 VAL C CA +6124 C C . VAL C 177 ? 1.5688 1.0448 1.3940 0.2306 -0.0014 0.0270 176 VAL C C +6125 O O . VAL C 177 ? 2.0640 1.5335 1.8814 0.2299 -0.0016 0.0268 176 VAL C O +6126 C CB . VAL C 177 ? 1.1869 0.6744 1.0287 0.2293 -0.0009 0.0258 176 VAL C CB +6127 C CG1 . VAL C 177 ? 1.3997 0.8847 1.2381 0.2270 0.0008 0.0252 176 VAL C CG1 +6128 C CG2 . VAL C 177 ? 1.3451 0.8422 1.1996 0.2297 -0.0010 0.0256 176 VAL C CG2 +6129 N N . GLN C 178 ? 1.0939 0.5697 0.9177 0.2307 -0.0006 0.0275 177 GLN C N +6130 C CA . GLN C 178 ? 1.4750 0.9428 1.2879 0.2300 -0.0001 0.0277 177 GLN C CA +6131 C C . GLN C 178 ? 1.5013 0.9671 1.3120 0.2272 0.0016 0.0268 177 GLN C C +6132 O O . GLN C 178 ? 1.3799 0.8504 1.1964 0.2263 0.0028 0.0265 177 GLN C O +6133 C CB . GLN C 178 ? 1.2169 0.6854 1.0292 0.2313 -0.0001 0.0285 177 GLN C CB +6134 C CG . GLN C 178 ? 1.6092 1.0704 1.4114 0.2303 0.0008 0.0286 177 GLN C CG +6135 C CD . GLN C 178 ? 1.4496 0.9025 1.2410 0.2312 -0.0003 0.0291 177 GLN C CD +6136 O OE1 . GLN C 178 ? 1.4278 0.8807 1.2189 0.2334 -0.0017 0.0297 177 GLN C OE1 +6137 N NE2 . GLN C 178 ? 1.5981 1.0437 1.3805 0.2294 0.0004 0.0287 177 GLN C NE2 +6138 N N . LEU C 179 ? 1.3768 0.8353 1.1789 0.2259 0.0018 0.0264 178 LEU C N +6139 C CA . LEU C 179 ? 1.3289 0.7850 1.1283 0.2232 0.0034 0.0256 178 LEU C CA +6140 C C . LEU C 179 ? 1.2002 0.6525 0.9937 0.2225 0.0044 0.0259 178 LEU C C +6141 O O . LEU C 179 ? 1.5116 0.9599 1.2990 0.2239 0.0038 0.0267 178 LEU C O +6142 C CB . LEU C 179 ? 1.3608 0.8103 1.1530 0.2219 0.0033 0.0250 178 LEU C CB +6143 C CG . LEU C 179 ? 1.6168 1.0695 1.4144 0.2220 0.0026 0.0244 178 LEU C CG +6144 C CD1 . LEU C 179 ? 1.7846 1.2298 1.5735 0.2208 0.0024 0.0240 178 LEU C CD1 +6145 C CD2 . LEU C 179 ? 1.3400 0.8002 1.1479 0.2207 0.0037 0.0236 178 LEU C CD2 +6146 N N . ALA C 180 ? 1.2286 0.6822 1.0241 0.2204 0.0060 0.0252 179 ALA C N +6147 C CA . ALA C 180 ? 1.3275 0.7774 1.1173 0.2194 0.0072 0.0254 179 ALA C CA +6148 C C . ALA C 180 ? 1.3525 0.7982 1.1378 0.2165 0.0087 0.0246 179 ALA C C +6149 O O . ALA C 180 ? 1.4423 0.8918 1.2327 0.2150 0.0100 0.0240 179 ALA C O +6150 C CB . ALA C 180 ? 1.5361 0.9926 1.3333 0.2201 0.0077 0.0258 179 ALA C CB +6151 N N . ASP C 181 ? 1.2126 0.6503 0.9880 0.2158 0.0085 0.0245 180 ASP C N +6152 C CA . ASP C 181 ? 1.6491 1.0822 1.4196 0.2131 0.0097 0.0236 180 ASP C CA +6153 C C . ASP C 181 ? 1.4641 0.8953 1.2315 0.2114 0.0113 0.0235 180 ASP C C +6154 O O . ASP C 181 ? 1.4962 0.9213 1.2549 0.2115 0.0114 0.0241 180 ASP C O +6155 C CB . ASP C 181 ? 1.6772 1.1018 1.4371 0.2130 0.0089 0.0237 180 ASP C CB +6156 C CG . ASP C 181 ? 1.7662 1.1874 1.5232 0.2105 0.0098 0.0227 180 ASP C CG +6157 O OD1 . ASP C 181 ? 1.9458 1.3704 1.7078 0.2086 0.0112 0.0219 180 ASP C OD1 +6158 O OD2 . ASP C 181 ? 1.9274 1.3424 1.6770 0.2104 0.0091 0.0227 180 ASP C OD2 +6159 N N . HIS C 182 ? 1.1189 0.5553 0.8935 0.2099 0.0126 0.0228 181 HIS C N +6160 C CA . HIS C 182 ? 1.5259 0.9617 1.2991 0.2084 0.0141 0.0227 181 HIS C CA +6161 C C . HIS C 182 ? 1.2607 0.6904 1.0269 0.2056 0.0155 0.0219 181 HIS C C +6162 O O . HIS C 182 ? 1.2173 0.6489 0.9871 0.2039 0.0163 0.0209 181 HIS C O +6163 C CB . HIS C 182 ? 1.3678 0.8126 1.1524 0.2084 0.0148 0.0224 181 HIS C CB +6164 C CG . HIS C 182 ? 1.0560 0.5062 0.8464 0.2108 0.0139 0.0233 181 HIS C CG +6165 N ND1 . HIS C 182 ? 1.4604 0.9130 1.2536 0.2131 0.0123 0.0238 181 HIS C ND1 +6166 C CD2 . HIS C 182 ? 1.1294 0.5835 0.9236 0.2113 0.0144 0.0237 181 HIS C CD2 +6167 C CE1 . HIS C 182 ? 1.3755 0.8330 1.1739 0.2149 0.0119 0.0245 181 HIS C CE1 +6168 N NE2 . HIS C 182 ? 1.2434 0.7018 1.0424 0.2139 0.0131 0.0244 181 HIS C NE2 +6169 N N . TYR C 183 ? 1.5042 0.9269 1.2607 0.2050 0.0159 0.0224 182 TYR C N +6170 C CA . TYR C 183 ? 1.5912 1.0077 1.3404 0.2023 0.0173 0.0218 182 TYR C CA +6171 C C . TYR C 183 ? 1.2765 0.6937 1.0259 0.2011 0.0187 0.0218 182 TYR C C +6172 O O . TYR C 183 ? 1.7961 1.2101 1.5402 0.2019 0.0185 0.0226 182 TYR C O +6173 C CB . TYR C 183 ? 1.3931 0.8001 1.1299 0.2022 0.0166 0.0222 182 TYR C CB +6174 C CG . TYR C 183 ? 1.4389 0.8441 1.1744 0.2028 0.0155 0.0220 182 TYR C CG +6175 C CD1 . TYR C 183 ? 1.5766 0.9838 1.3141 0.2055 0.0137 0.0227 182 TYR C CD1 +6176 C CD2 . TYR C 183 ? 1.2718 0.6736 1.0042 0.2006 0.0161 0.0211 182 TYR C CD2 +6177 C CE1 . TYR C 183 ? 1.5412 0.9470 1.2778 0.2061 0.0126 0.0225 182 TYR C CE1 +6178 C CE2 . TYR C 183 ? 1.6395 1.0397 1.3708 0.2011 0.0150 0.0209 182 TYR C CE2 +6179 C CZ . TYR C 183 ? 1.6504 1.0526 1.3837 0.2039 0.0132 0.0216 182 TYR C CZ +6180 O OH . TYR C 183 ? 1.5770 0.9778 1.3093 0.2044 0.0121 0.0214 182 TYR C OH +6181 N N . GLN C 184 ? 1.2557 0.6771 1.0112 0.1993 0.0200 0.0209 183 GLN C N +6182 C CA . GLN C 184 ? 1.6059 1.0295 1.3637 0.1984 0.0213 0.0209 183 GLN C CA +6183 C C . GLN C 184 ? 1.5435 0.9624 1.2960 0.1953 0.0230 0.0200 183 GLN C C +6184 O O . GLN C 184 ? 1.5558 0.9714 1.3053 0.1936 0.0233 0.0193 183 GLN C O +6185 C CB . GLN C 184 ? 1.6127 1.0464 1.3835 0.1990 0.0214 0.0205 183 GLN C CB +6186 C CG . GLN C 184 ? 1.5504 0.9878 1.3253 0.1982 0.0226 0.0204 183 GLN C CG +6187 C CD . GLN C 184 ? 1.6770 1.1238 1.4644 0.1982 0.0229 0.0198 183 GLN C CD +6188 O OE1 . GLN C 184 ? 1.2707 0.7226 1.0648 0.1999 0.0217 0.0199 183 GLN C OE1 +6189 N NE2 . GLN C 184 ? 1.2199 0.6691 1.0107 0.1964 0.0243 0.0191 183 GLN C NE2 +6190 N N . GLN C 185 ? 1.3325 0.7511 1.0838 0.1945 0.0240 0.0202 184 GLN C N +6191 C CA . GLN C 185 ? 1.3731 0.7886 1.1212 0.1915 0.0257 0.0194 184 GLN C CA +6192 C C . GLN C 185 ? 1.7161 1.1350 1.4679 0.1909 0.0268 0.0194 184 GLN C C +6193 O O . GLN C 185 ? 1.5086 0.9278 1.2594 0.1924 0.0265 0.0204 184 GLN C O +6194 C CB . GLN C 185 ? 1.8694 1.2747 1.6046 0.1902 0.0259 0.0195 184 GLN C CB +6195 C CG . GLN C 185 ? 2.2527 1.6529 1.9799 0.1914 0.0254 0.0207 184 GLN C CG +6196 C CD . GLN C 185 ? 2.5189 1.9091 2.2334 0.1897 0.0258 0.0207 184 GLN C CD +6197 O OE1 . GLN C 185 ? 2.5771 1.9637 2.2882 0.1883 0.0259 0.0201 184 GLN C OE1 +6198 N NE2 . GLN C 185 ? 2.5972 1.9828 2.3047 0.1898 0.0260 0.0214 184 GLN C NE2 +6199 N N . ASN C 186 ? 1.4843 0.9059 1.2406 0.1887 0.0282 0.0184 185 ASN C N +6200 C CA . ASN C 186 ? 1.6320 1.0575 1.3928 0.1879 0.0293 0.0182 185 ASN C CA +6201 C C . ASN C 186 ? 1.7830 1.2034 1.5379 0.1849 0.0310 0.0176 185 ASN C C +6202 O O . ASN C 186 ? 1.5868 1.0041 1.3391 0.1829 0.0317 0.0167 185 ASN C O +6203 C CB . ASN C 186 ? 1.5585 0.9936 1.3321 0.1883 0.0294 0.0176 185 ASN C CB +6204 C CG . ASN C 186 ? 1.5114 0.9522 1.2915 0.1913 0.0278 0.0183 185 ASN C CG +6205 O OD1 . ASN C 186 ? 1.5850 1.0268 1.3668 0.1923 0.0268 0.0183 185 ASN C OD1 +6206 N ND2 . ASN C 186 ? 1.3548 0.7994 1.1385 0.1926 0.0277 0.0190 185 ASN C ND2 +6207 N N . THR C 187 ? 1.5451 0.9648 1.2981 0.1847 0.0317 0.0181 186 THR C N +6208 C CA . THR C 187 ? 1.6643 1.0783 1.4103 0.1821 0.0332 0.0177 186 THR C CA +6209 C C . THR C 187 ? 1.5925 1.0103 1.3427 0.1819 0.0340 0.0178 186 THR C C +6210 O O . THR C 187 ? 1.8255 1.2455 1.5770 0.1839 0.0334 0.0188 186 THR C O +6211 C CB . THR C 187 ? 1.6498 1.0543 1.3830 0.1822 0.0328 0.0185 186 THR C CB +6212 O OG1 . THR C 187 ? 1.7652 1.1651 1.4934 0.1817 0.0323 0.0182 186 THR C OG1 +6213 C CG2 . THR C 187 ? 1.4218 0.8210 1.1481 0.1798 0.0343 0.0184 186 THR C CG2 +6214 N N . PRO C 188 ? 1.6659 1.0847 1.4182 0.1793 0.0355 0.0168 187 PRO C N +6215 C CA . PRO C 188 ? 1.8145 1.2373 1.5714 0.1788 0.0365 0.0168 187 PRO C CA +6216 C C . PRO C 188 ? 1.7866 1.2037 1.5351 0.1785 0.0369 0.0176 187 PRO C C +6217 O O . PRO C 188 ? 1.9282 1.3376 1.6671 0.1768 0.0376 0.0176 187 PRO C O +6218 C CB . PRO C 188 ? 1.6806 1.1045 1.4406 0.1760 0.0379 0.0154 187 PRO C CB +6219 C CG . PRO C 188 ? 1.6725 1.0872 1.4213 0.1751 0.0386 0.0150 187 PRO C CG +6220 C CD . PRO C 188 ? 1.3763 0.7919 1.1261 0.1770 0.0366 0.0157 187 PRO C CD +6221 N N . ILE C 189 ? 1.7911 1.2122 1.5434 0.1802 0.0366 0.0184 188 ILE C N +6222 C CA . ILE C 189 ? 1.9100 1.3271 1.6559 0.1801 0.0371 0.0191 188 ILE C CA +6223 C C . ILE C 189 ? 2.0431 1.4585 1.7877 0.1772 0.0388 0.0184 188 ILE C C +6224 O O . ILE C 189 ? 1.8816 1.2906 1.6176 0.1761 0.0395 0.0187 188 ILE C O +6225 C CB . ILE C 189 ? 1.6542 1.0772 1.4063 0.1826 0.0364 0.0200 188 ILE C CB +6226 C CG1 . ILE C 189 ? 1.6547 1.0794 1.4083 0.1855 0.0347 0.0207 188 ILE C CG1 +6227 C CG2 . ILE C 189 ? 1.5837 1.0027 1.3294 0.1826 0.0369 0.0207 188 ILE C CG2 +6228 C CD1 . ILE C 189 ? 1.7074 1.1391 1.4688 0.1879 0.0339 0.0214 188 ILE C CD1 +6229 N N . GLY C 190 ? 2.1122 1.5335 1.8654 0.1760 0.0395 0.0173 189 GLY C N +6230 C CA . GLY C 190 ? 2.1589 1.5797 1.9123 0.1733 0.0411 0.0164 189 GLY C CA +6231 C C . GLY C 190 ? 2.2562 1.6675 1.9983 0.1714 0.0428 0.0157 189 GLY C C +6232 O O . GLY C 190 ? 1.9454 1.3526 1.6827 0.1718 0.0423 0.0157 189 GLY C O +6233 N N . ASP C 191 ? 2.2934 1.7009 2.0310 0.1694 0.0447 0.0152 190 ASP C N +6234 C CA . ASP C 191 ? 2.4295 1.8278 2.1562 0.1673 0.0466 0.0144 190 ASP C CA +6235 C C . ASP C 191 ? 2.3151 1.7171 2.0480 0.1661 0.0478 0.0130 190 ASP C C +6236 O O . ASP C 191 ? 2.0811 1.4767 1.8067 0.1645 0.0493 0.0122 190 ASP C O +6237 C CB . ASP C 191 ? 2.4025 1.7932 2.1191 0.1657 0.0482 0.0146 190 ASP C CB +6238 C CG . ASP C 191 ? 2.5990 1.9824 2.3051 0.1664 0.0474 0.0158 190 ASP C CG +6239 O OD1 . ASP C 191 ? 2.3374 1.7146 2.0358 0.1665 0.0470 0.0159 190 ASP C OD1 +6240 O OD2 . ASP C 191 ? 2.7641 2.1480 2.4698 0.1668 0.0472 0.0165 190 ASP C OD2 +6241 N N . GLY C 192 ? 2.2909 1.7033 2.0372 0.1669 0.0472 0.0127 191 GLY C N +6242 C CA . GLY C 192 ? 2.2945 1.7117 2.0482 0.1660 0.0480 0.0114 191 GLY C CA +6243 C C . GLY C 192 ? 2.4228 1.8386 2.1756 0.1663 0.0477 0.0108 191 GLY C C +6244 O O . GLY C 192 ? 2.3410 1.7549 2.0910 0.1676 0.0463 0.0116 191 GLY C O +6245 N N . PRO C 193 ? 2.5354 1.9521 2.2906 0.1649 0.0491 0.0095 192 PRO C N +6246 C CA . PRO C 193 ? 2.5464 1.9618 2.3010 0.1650 0.0489 0.0088 192 PRO C CA +6247 C C . PRO C 193 ? 2.3825 1.8080 2.1500 0.1671 0.0467 0.0089 192 PRO C C +6248 O O . PRO C 193 ? 1.9415 1.3761 1.7204 0.1678 0.0460 0.0089 192 PRO C O +6249 C CB . PRO C 193 ? 2.4262 1.8399 2.1800 0.1628 0.0511 0.0073 192 PRO C CB +6250 C CG . PRO C 193 ? 2.1541 1.5736 1.9151 0.1623 0.0518 0.0071 192 PRO C CG +6251 C CD . PRO C 193 ? 2.3138 1.7326 2.0724 0.1632 0.0509 0.0085 192 PRO C CD +6252 N N . VAL C 194 ? 2.2263 1.6501 1.9919 0.1681 0.0457 0.0090 193 VAL C N +6253 C CA . VAL C 194 ? 2.0667 1.4995 1.8438 0.1700 0.0436 0.0092 193 VAL C CA +6254 C C . VAL C 194 ? 1.8955 1.3280 1.6736 0.1697 0.0439 0.0080 193 VAL C C +6255 O O . VAL C 194 ? 1.7561 1.1812 1.5255 0.1680 0.0457 0.0073 193 VAL C O +6256 C CB . VAL C 194 ? 2.1607 1.5928 1.9358 0.1720 0.0416 0.0106 193 VAL C CB +6257 C CG1 . VAL C 194 ? 1.6586 1.0906 1.4322 0.1724 0.0413 0.0117 193 VAL C CG1 +6258 C CG2 . VAL C 194 ? 2.0815 1.5037 1.8442 0.1718 0.0418 0.0107 193 VAL C CG2 +6259 N N . LEU C 195 ? 1.7238 1.1644 1.5124 0.1712 0.0422 0.0080 194 LEU C N +6260 C CA . LEU C 195 ? 1.5659 1.0070 1.3564 0.1711 0.0423 0.0069 194 LEU C CA +6261 C C . LEU C 195 ? 1.7096 1.1462 1.4942 0.1722 0.0411 0.0076 194 LEU C C +6262 O O . LEU C 195 ? 1.9976 1.4373 1.7853 0.1740 0.0392 0.0087 194 LEU C O +6263 C CB . LEU C 195 ? 1.4690 0.9218 1.2749 0.1719 0.0413 0.0063 194 LEU C CB +6264 C CG . LEU C 195 ? 1.7571 1.2152 1.5698 0.1708 0.0423 0.0056 194 LEU C CG +6265 C CD1 . LEU C 195 ? 1.6865 1.1561 1.5143 0.1717 0.0411 0.0049 194 LEU C CD1 +6266 C CD2 . LEU C 195 ? 1.3891 0.8404 1.1940 0.1685 0.0450 0.0044 194 LEU C CD2 +6267 N N . LEU C 196 ? 1.6810 1.1100 1.4567 0.1712 0.0421 0.0069 195 LEU C N +6268 C CA . LEU C 196 ? 1.9014 1.3256 1.6709 0.1722 0.0410 0.0075 195 LEU C CA +6269 C C . LEU C 196 ? 1.8662 1.2941 1.6417 0.1727 0.0404 0.0066 195 LEU C C +6270 O O . LEU C 196 ? 1.7869 1.2110 1.5585 0.1713 0.0419 0.0054 195 LEU C O +6271 C CB . LEU C 196 ? 2.1858 1.5973 1.9391 0.1708 0.0423 0.0077 195 LEU C CB +6272 C CG . LEU C 196 ? 1.9360 1.3438 1.6834 0.1702 0.0430 0.0085 195 LEU C CG +6273 C CD1 . LEU C 196 ? 1.8530 1.2483 1.5844 0.1686 0.0444 0.0086 195 LEU C CD1 +6274 C CD2 . LEU C 196 ? 1.8155 1.2276 1.5672 0.1723 0.0409 0.0099 195 LEU C CD2 +6275 N N . PRO C 197 ? 1.7162 1.1518 1.5013 0.1747 0.0382 0.0071 196 PRO C N +6276 C CA . PRO C 197 ? 1.7213 1.1634 1.5156 0.1754 0.0374 0.0063 196 PRO C CA +6277 C C . PRO C 197 ? 1.6775 1.1132 1.4645 0.1754 0.0373 0.0060 196 PRO C C +6278 O O . PRO C 197 ? 1.7798 1.2077 1.5563 0.1757 0.0371 0.0067 196 PRO C O +6279 C CB . PRO C 197 ? 1.7183 1.1689 1.5228 0.1775 0.0349 0.0074 196 PRO C CB +6280 C CG . PRO C 197 ? 1.5852 1.0302 1.3813 0.1781 0.0344 0.0088 196 PRO C CG +6281 C CD . PRO C 197 ? 1.4349 0.8732 1.2222 0.1764 0.0365 0.0086 196 PRO C CD +6282 N N . ASP C 198 ? 1.7789 1.2182 1.5717 0.1751 0.0376 0.0047 197 ASP C N +6283 C CA . ASP C 198 ? 1.9180 1.3538 1.7070 0.1756 0.0371 0.0044 197 ASP C CA +6284 C C . ASP C 198 ? 1.6846 1.1265 1.4809 0.1778 0.0345 0.0054 197 ASP C C +6285 O O . ASP C 198 ? 1.6377 1.0877 1.4438 0.1788 0.0334 0.0060 197 ASP C O +6286 C CB . ASP C 198 ? 1.9843 1.4233 1.7788 0.1747 0.0381 0.0028 197 ASP C CB +6287 C CG . ASP C 198 ? 2.1519 1.5831 1.9371 0.1723 0.0407 0.0017 197 ASP C CG +6288 O OD1 . ASP C 198 ? 2.1817 1.6036 1.9545 0.1714 0.0417 0.0022 197 ASP C OD1 +6289 O OD2 . ASP C 198 ? 1.9177 1.3522 1.7081 0.1714 0.0419 0.0002 197 ASP C OD2 +6290 N N . ASN C 199 ? 1.5611 0.9988 1.3524 0.1785 0.0337 0.0056 198 ASN C N +6291 C CA . ASN C 199 ? 1.7186 1.1619 1.5169 0.1806 0.0313 0.0064 198 ASN C CA +6292 C C . ASN C 199 ? 1.7106 1.1661 1.5249 0.1813 0.0303 0.0060 198 ASN C C +6293 O O . ASN C 199 ? 1.7195 1.1781 1.5388 0.1807 0.0310 0.0047 198 ASN C O +6294 C CB . ASN C 199 ? 2.0350 1.4730 1.8271 0.1810 0.0308 0.0062 198 ASN C CB +6295 C CG . ASN C 199 ? 2.1028 1.5291 1.8795 0.1807 0.0311 0.0069 198 ASN C CG +6296 O OD1 . ASN C 199 ? 1.6110 1.0319 1.3801 0.1797 0.0323 0.0072 198 ASN C OD1 +6297 N ND2 . ASN C 199 ? 2.0693 1.4917 1.8413 0.1815 0.0301 0.0071 198 ASN C ND2 +6298 N N . HIS C 200 ? 1.7116 1.1740 1.5340 0.1826 0.0288 0.0070 199 HIS C N +6299 C CA . HIS C 200 ? 1.5938 1.0663 1.4290 0.1841 0.0277 0.0070 199 HIS C CA +6300 C C . HIS C 200 ? 1.4170 0.8908 1.2524 0.1870 0.0262 0.0086 199 HIS C C +6301 O O . HIS C 200 ? 1.4291 0.8965 1.2556 0.1876 0.0258 0.0096 199 HIS C O +6302 C CB . HIS C 200 ? 1.4285 0.9070 1.2715 0.1832 0.0287 0.0062 199 HIS C CB +6303 C CG . HIS C 200 ? 1.3553 0.8330 1.1958 0.1834 0.0291 0.0072 199 HIS C CG +6304 N ND1 . HIS C 200 ? 1.5070 0.9787 1.3397 0.1814 0.0305 0.0070 199 HIS C ND1 +6305 C CD2 . HIS C 200 ? 1.4788 0.9609 1.3235 0.1853 0.0284 0.0082 199 HIS C CD2 +6306 C CE1 . HIS C 200 ? 1.4739 0.9463 1.3062 0.1822 0.0305 0.0080 199 HIS C CE1 +6307 N NE2 . HIS C 200 ? 1.6130 1.0917 1.4525 0.1845 0.0293 0.0087 199 HIS C NE2 +6308 N N . TYR C 201 ? 1.3999 0.8819 1.2453 0.1887 0.0254 0.0088 200 TYR C N +6309 C CA . TYR C 201 ? 1.4592 0.9428 1.3052 0.1914 0.0240 0.0103 200 TYR C CA +6310 C C . TYR C 201 ? 1.3971 0.8889 1.2528 0.1926 0.0238 0.0106 200 TYR C C +6311 O O . TYR C 201 ? 1.3360 0.8336 1.1997 0.1916 0.0244 0.0096 200 TYR C O +6312 C CB . TYR C 201 ? 1.2997 0.7827 1.1454 0.1929 0.0226 0.0106 200 TYR C CB +6313 C CG . TYR C 201 ? 1.3528 0.8433 1.2090 0.1935 0.0220 0.0098 200 TYR C CG +6314 C CD1 . TYR C 201 ? 1.4549 0.9464 1.3140 0.1916 0.0228 0.0083 200 TYR C CD1 +6315 C CD2 . TYR C 201 ? 1.5089 1.0052 1.3718 0.1958 0.0206 0.0106 200 TYR C CD2 +6316 C CE1 . TYR C 201 ? 1.4560 0.9542 1.3246 0.1921 0.0222 0.0075 200 TYR C CE1 +6317 C CE2 . TYR C 201 ? 1.6929 1.1960 1.5654 0.1963 0.0200 0.0099 200 TYR C CE2 +6318 C CZ . TYR C 201 ? 1.4872 0.9912 1.3624 0.1945 0.0208 0.0083 200 TYR C CZ +6319 O OH . TYR C 201 ? 1.3603 0.8710 1.2449 0.1949 0.0202 0.0076 200 TYR C OH +6320 N N . LEU C 202 ? 1.3697 0.8620 1.2245 0.1947 0.0228 0.0120 201 LEU C N +6321 C CA . LEU C 202 ? 1.4670 0.9670 1.3307 0.1960 0.0224 0.0124 201 LEU C CA +6322 C C . LEU C 202 ? 1.2938 0.7983 1.1630 0.1983 0.0208 0.0130 201 LEU C C +6323 O O . LEU C 202 ? 1.1414 0.6419 1.0052 0.1997 0.0198 0.0139 201 LEU C O +6324 C CB . LEU C 202 ? 1.1508 0.6486 1.0101 0.1966 0.0227 0.0135 201 LEU C CB +6325 C CG . LEU C 202 ? 1.2847 0.7775 1.1375 0.1945 0.0243 0.0132 201 LEU C CG +6326 C CD1 . LEU C 202 ? 1.2296 0.7230 1.0816 0.1953 0.0244 0.0142 201 LEU C CD1 +6327 C CD2 . LEU C 202 ? 1.5989 1.0945 1.4565 0.1921 0.0255 0.0117 201 LEU C CD2 +6328 N N . SER C 203 ? 1.2353 0.7480 1.1154 0.1987 0.0205 0.0124 202 SER C N +6329 C CA . SER C 203 ? 1.1855 0.7030 1.0716 0.2008 0.0190 0.0129 202 SER C CA +6330 C C . SER C 203 ? 1.2372 0.7591 1.1274 0.2025 0.0185 0.0140 202 SER C C +6331 O O . SER C 203 ? 1.5331 1.0609 1.4305 0.2021 0.0189 0.0136 202 SER C O +6332 C CB . SER C 203 ? 1.0661 0.5901 0.9618 0.2002 0.0189 0.0117 202 SER C CB +6333 O OG . SER C 203 ? 1.3816 0.9097 1.2826 0.2021 0.0175 0.0121 202 SER C OG +6334 N N . THR C 204 ? 1.2616 0.7804 1.1468 0.2044 0.0175 0.0153 203 THR C N +6335 C CA . THR C 204 ? 1.2945 0.8165 1.1822 0.2061 0.0170 0.0164 203 THR C CA +6336 C C . THR C 204 ? 1.3067 0.8346 1.2018 0.2082 0.0155 0.0169 203 THR C C +6337 O O . THR C 204 ? 1.3704 0.8970 1.2645 0.2090 0.0146 0.0169 203 THR C O +6338 C CB . THR C 204 ? 1.2031 0.7178 1.0804 0.2069 0.0169 0.0175 203 THR C CB +6339 O OG1 . THR C 204 ? 1.2630 0.7716 1.1326 0.2049 0.0182 0.0171 203 THR C OG1 +6340 C CG2 . THR C 204 ? 1.8877 1.4058 1.7677 0.2084 0.0166 0.0185 203 THR C CG2 +6341 N N . GLN C 205 ? 1.2045 0.7389 1.1070 0.2091 0.0153 0.0173 204 GLN C N +6342 C CA . GLN C 205 ? 1.2311 0.7708 1.1399 0.2113 0.0139 0.0180 204 GLN C CA +6343 C C . GLN C 205 ? 1.2792 0.8209 1.1890 0.2125 0.0138 0.0190 204 GLN C C +6344 O O . GLN C 205 ? 1.1074 0.6508 1.0188 0.2115 0.0148 0.0188 204 GLN C O +6345 C CB . GLN C 205 ? 1.2295 0.7772 1.1495 0.2111 0.0136 0.0171 204 GLN C CB +6346 C CG . GLN C 205 ? 1.0567 0.6032 0.9769 0.2095 0.0139 0.0159 204 GLN C CG +6347 C CD . GLN C 205 ? 1.4395 0.9925 1.3687 0.2081 0.0145 0.0146 204 GLN C CD +6348 O OE1 . GLN C 205 ? 2.0537 1.6135 1.9919 0.2088 0.0138 0.0144 204 GLN C OE1 +6349 N NE2 . GLN C 205 ? 1.4519 1.0027 1.3786 0.2061 0.0159 0.0138 204 GLN C NE2 +6350 N N . SER C 206 ? 1.1624 0.7042 1.0716 0.2147 0.0126 0.0201 205 SER C N +6351 C CA . SER C 206 ? 0.9730 0.5153 0.8812 0.2161 0.0125 0.0212 205 SER C CA +6352 C C . SER C 206 ? 0.8982 0.4457 0.8124 0.2184 0.0111 0.0220 205 SER C C +6353 O O . SER C 206 ? 1.2828 0.8312 1.1989 0.2193 0.0100 0.0220 205 SER C O +6354 C CB . SER C 206 ? 1.0585 0.5921 0.9548 0.2163 0.0127 0.0219 205 SER C CB +6355 O OG . SER C 206 ? 1.4443 0.9736 1.3354 0.2141 0.0141 0.0212 205 SER C OG +6356 N N . ASN C 207 ? 1.0359 0.5868 0.9532 0.2192 0.0111 0.0226 206 ASN C N +6357 C CA . ASN C 207 ? 1.1394 0.6948 1.0618 0.2214 0.0099 0.0235 206 ASN C CA +6358 C C . ASN C 207 ? 1.2440 0.7975 1.1624 0.2226 0.0099 0.0245 206 ASN C C +6359 O O . ASN C 207 ? 1.1346 0.6876 1.0517 0.2216 0.0110 0.0245 206 ASN C O +6360 C CB . ASN C 207 ? 1.0943 0.6588 1.0288 0.2213 0.0095 0.0230 206 ASN C CB +6361 C CG . ASN C 207 ? 0.9994 0.5693 0.9397 0.2231 0.0087 0.0238 206 ASN C CG +6362 O OD1 . ASN C 207 ? 0.8582 0.4287 0.7982 0.2233 0.0092 0.0242 206 ASN C OD1 +6363 N ND2 . ASN C 207 ? 1.1314 0.7053 1.0774 0.2244 0.0075 0.0240 206 ASN C ND2 +6364 N N . LEU C 208 ? 1.0672 0.6196 0.9836 0.2247 0.0088 0.0255 207 LEU C N +6365 C CA . LEU C 208 ? 0.8264 0.3766 0.7385 0.2261 0.0087 0.0265 207 LEU C CA +6366 C C . LEU C 208 ? 0.9249 0.4820 0.8453 0.2277 0.0079 0.0271 207 LEU C C +6367 O O . LEU C 208 ? 1.0501 0.6107 0.9756 0.2288 0.0068 0.0272 207 LEU C O +6368 C CB . LEU C 208 ? 1.1109 0.6537 1.0134 0.2273 0.0081 0.0272 207 LEU C CB +6369 C CG . LEU C 208 ? 0.8759 0.4113 0.7698 0.2258 0.0086 0.0267 207 LEU C CG +6370 C CD1 . LEU C 208 ? 1.1441 0.6726 1.0288 0.2272 0.0078 0.0274 207 LEU C CD1 +6371 C CD2 . LEU C 208 ? 0.9939 0.5265 0.8838 0.2239 0.0101 0.0263 207 LEU C CD2 +6372 N N . SER C 209 ? 0.9501 0.5092 0.8718 0.2278 0.0085 0.0275 208 SER C N +6373 C CA . SER C 209 ? 1.0531 0.6187 0.9824 0.2293 0.0079 0.0280 208 SER C CA +6374 C C . SER C 209 ? 1.2462 0.8105 1.1722 0.2303 0.0081 0.0289 208 SER C C +6375 O O . SER C 209 ? 0.9903 0.5489 0.9083 0.2298 0.0090 0.0291 208 SER C O +6376 C CB . SER C 209 ? 1.0100 0.5832 0.9494 0.2280 0.0082 0.0272 208 SER C CB +6377 O OG . SER C 209 ? 1.2430 0.8148 1.1805 0.2261 0.0096 0.0266 208 SER C OG +6378 N N . LYS C 210 ? 1.1791 0.7489 1.1116 0.2317 0.0075 0.0294 209 LYS C N +6379 C CA . LYS C 210 ? 0.9574 0.5274 0.8886 0.2327 0.0077 0.0302 209 LYS C CA +6380 C C . LYS C 210 ? 1.0335 0.6103 0.9729 0.2319 0.0083 0.0299 209 LYS C C +6381 O O . LYS C 210 ? 1.2739 0.8565 1.2216 0.2312 0.0081 0.0293 209 LYS C O +6382 C CB . LYS C 210 ? 1.2235 0.7941 1.1550 0.2351 0.0065 0.0312 209 LYS C CB +6383 C CG . LYS C 210 ? 1.0646 0.6288 0.9884 0.2362 0.0057 0.0315 209 LYS C CG +6384 C CD . LYS C 210 ? 0.9882 0.5442 0.9008 0.2359 0.0065 0.0318 209 LYS C CD +6385 C CE . LYS C 210 ? 1.0424 0.5924 0.9474 0.2373 0.0055 0.0323 209 LYS C CE +6386 N NZ . LYS C 210 ? 1.0594 0.6012 0.9535 0.2367 0.0062 0.0324 209 LYS C NZ +6387 N N . ASP C 211 ? 1.1881 0.7638 1.1248 0.2321 0.0090 0.0304 210 ASP C N +6388 C CA . ASP C 211 ? 1.0382 0.6196 0.9814 0.2318 0.0094 0.0303 210 ASP C CA +6389 C C . ASP C 211 ? 1.3187 0.9029 1.2645 0.2341 0.0085 0.0313 210 ASP C C +6390 O O . ASP C 211 ? 1.4211 1.0006 1.3603 0.2354 0.0083 0.0321 210 ASP C O +6391 C CB . ASP C 211 ? 1.1481 0.7255 1.0852 0.2309 0.0107 0.0304 210 ASP C CB +6392 C CG . ASP C 211 ? 1.4827 1.0652 1.4252 0.2307 0.0112 0.0305 210 ASP C CG +6393 O OD1 . ASP C 211 ? 1.4533 1.0422 1.4038 0.2316 0.0105 0.0306 210 ASP C OD1 +6394 O OD2 . ASP C 211 ? 1.1116 0.6915 1.0500 0.2297 0.0123 0.0304 210 ASP C OD2 +6395 N N . PRO C 212 ? 1.5627 1.1544 1.5182 0.2344 0.0079 0.0312 211 PRO C N +6396 C CA . PRO C 212 ? 1.4464 1.0404 1.4043 0.2365 0.0070 0.0321 211 PRO C CA +6397 C C . PRO C 212 ? 1.4237 1.0182 1.3806 0.2373 0.0075 0.0327 211 PRO C C +6398 O O . PRO C 212 ? 1.3423 0.9384 1.3007 0.2391 0.0068 0.0335 211 PRO C O +6399 C CB . PRO C 212 ? 1.1791 0.7808 1.1477 0.2365 0.0061 0.0317 211 PRO C CB +6400 C CG . PRO C 212 ? 1.4344 1.0391 1.4072 0.2343 0.0070 0.0306 211 PRO C CG +6401 C CD . PRO C 212 ? 1.1441 0.7422 1.1086 0.2330 0.0080 0.0303 211 PRO C CD +6402 N N . ASN C 213 ? 1.7223 1.3153 1.6766 0.2359 0.0087 0.0325 212 ASN C N +6403 C CA . ASN C 213 ? 1.8269 1.4195 1.7791 0.2366 0.0093 0.0331 212 ASN C CA +6404 C C . ASN C 213 ? 1.6330 1.2175 1.5741 0.2368 0.0099 0.0335 212 ASN C C +6405 O O . ASN C 213 ? 1.5264 1.1095 1.4645 0.2369 0.0107 0.0339 212 ASN C O +6406 C CB . ASN C 213 ? 1.6081 1.2048 1.5651 0.2350 0.0102 0.0326 212 ASN C CB +6407 C CG . ASN C 213 ? 1.4677 1.0719 1.4351 0.2343 0.0096 0.0319 212 ASN C CG +6408 O OD1 . ASN C 213 ? 1.4092 1.0173 1.3820 0.2355 0.0086 0.0321 212 ASN C OD1 +6409 N ND2 . ASN C 213 ? 1.2766 0.8830 1.2469 0.2324 0.0104 0.0310 212 ASN C ND2 +6410 N N . GLU C 214 ? 1.5459 1.1250 1.4810 0.2367 0.0097 0.0334 213 GLU C N +6411 C CA . GLU C 214 ? 1.1366 0.7077 1.0610 0.2368 0.0102 0.0338 213 GLU C CA +6412 C C . GLU C 214 ? 1.1972 0.7653 1.1176 0.2390 0.0092 0.0346 213 GLU C C +6413 O O . GLU C 214 ? 1.3842 0.9537 1.3073 0.2397 0.0081 0.0345 213 GLU C O +6414 C CB . GLU C 214 ? 1.0658 0.6324 0.9854 0.2350 0.0107 0.0330 213 GLU C CB +6415 C CG . GLU C 214 ? 1.2236 0.7817 1.1320 0.2351 0.0112 0.0334 213 GLU C CG +6416 C CD . GLU C 214 ? 1.6455 1.2025 1.5510 0.2352 0.0121 0.0338 213 GLU C CD +6417 O OE1 . GLU C 214 ? 1.7553 1.3120 1.6594 0.2370 0.0117 0.0346 213 GLU C OE1 +6418 O OE2 . GLU C 214 ? 1.3279 0.8843 1.2325 0.2334 0.0133 0.0333 213 GLU C OE2 +6419 N N . LYS C 215 ? 1.2704 0.8345 1.1845 0.2401 0.0094 0.0353 214 LYS C N +6420 C CA . LYS C 215 ? 1.4260 0.9873 1.3363 0.2423 0.0084 0.0361 214 LYS C CA +6421 C C . LYS C 215 ? 1.3214 0.8739 1.2203 0.2424 0.0085 0.0362 214 LYS C C +6422 O O . LYS C 215 ? 1.4755 1.0247 1.3704 0.2440 0.0076 0.0367 214 LYS C O +6423 C CB . LYS C 215 ? 1.3048 0.8687 1.2171 0.2439 0.0083 0.0368 214 LYS C CB +6424 C CG . LYS C 215 ? 1.9125 1.4851 1.8358 0.2438 0.0082 0.0367 214 LYS C CG +6425 C CD . LYS C 215 ? 2.0622 1.6372 1.9875 0.2458 0.0079 0.0375 214 LYS C CD +6426 C CE . LYS C 215 ? 1.9184 1.4919 1.8403 0.2455 0.0090 0.0378 214 LYS C CE +6427 N NZ . LYS C 215 ? 1.6591 1.2391 1.5888 0.2444 0.0096 0.0374 214 LYS C NZ +6428 N N . ARG C 216 ? 1.1244 0.6730 1.0183 0.2406 0.0096 0.0358 215 ARG C N +6429 C CA . ARG C 216 ? 1.0331 0.5733 0.9163 0.2403 0.0099 0.0358 215 ARG C CA +6430 C C . ARG C 216 ? 1.1247 0.6629 1.0068 0.2395 0.0094 0.0352 215 ARG C C +6431 O O . ARG C 216 ? 1.4350 0.9784 1.3247 0.2387 0.0092 0.0347 215 ARG C O +6432 C CB . ARG C 216 ? 0.9699 0.5071 0.8487 0.2385 0.0113 0.0355 215 ARG C CB +6433 C CG . ARG C 216 ? 1.3089 0.8459 1.1859 0.2393 0.0119 0.0361 215 ARG C CG +6434 C CD . ARG C 216 ? 1.2520 0.7875 1.1268 0.2372 0.0133 0.0357 215 ARG C CD +6435 N NE . ARG C 216 ? 1.6175 1.1599 1.5015 0.2359 0.0138 0.0351 215 ARG C NE +6436 C CZ . ARG C 216 ? 1.6651 1.2081 1.5497 0.2340 0.0150 0.0346 215 ARG C CZ +6437 N NH1 . ARG C 216 ? 1.5349 1.0718 1.4112 0.2332 0.0159 0.0347 215 ARG C NH1 +6438 N NH2 . ARG C 216 ? 1.3223 0.8720 1.2158 0.2329 0.0153 0.0340 215 ARG C NH2 +6439 N N . ASP C 217 ? 1.0512 0.5819 0.9240 0.2396 0.0091 0.0353 216 ASP C N +6440 C CA . ASP C 217 ? 1.3962 0.9247 1.2675 0.2389 0.0086 0.0348 216 ASP C CA +6441 C C . ASP C 217 ? 1.4336 0.9619 1.3053 0.2363 0.0097 0.0339 216 ASP C C +6442 O O . ASP C 217 ? 1.1489 0.6723 1.0141 0.2351 0.0107 0.0337 216 ASP C O +6443 C CB . ASP C 217 ? 1.2695 0.7901 1.1307 0.2399 0.0079 0.0352 216 ASP C CB +6444 C CG . ASP C 217 ? 1.5962 1.1162 1.4579 0.2402 0.0068 0.0349 216 ASP C CG +6445 O OD1 . ASP C 217 ? 1.6063 1.1325 1.4767 0.2400 0.0065 0.0346 216 ASP C OD1 +6446 O OD2 . ASP C 217 ? 1.3340 0.8473 1.1874 0.2406 0.0063 0.0351 216 ASP C OD2 +6447 N N . HIS C 218 ? 1.2755 0.8089 1.1549 0.2356 0.0095 0.0333 217 HIS C N +6448 C CA . HIS C 218 ? 1.1364 0.6714 1.0185 0.2332 0.0105 0.0324 217 HIS C CA +6449 C C . HIS C 218 ? 0.9923 0.5288 0.8780 0.2323 0.0101 0.0316 217 HIS C C +6450 O O . HIS C 218 ? 1.1508 0.6892 1.0395 0.2336 0.0089 0.0318 217 HIS C O +6451 C CB . HIS C 218 ? 0.9840 0.5260 0.8745 0.2327 0.0111 0.0322 217 HIS C CB +6452 C CG . HIS C 218 ? 0.9440 0.4938 0.8450 0.2335 0.0103 0.0322 217 HIS C CG +6453 N ND1 . HIS C 218 ? 1.4186 0.9705 1.3219 0.2357 0.0091 0.0329 217 HIS C ND1 +6454 C CD2 . HIS C 218 ? 1.3149 0.8709 1.2246 0.2323 0.0104 0.0314 217 HIS C CD2 +6455 C CE1 . HIS C 218 ? 1.0681 0.6271 0.9811 0.2358 0.0086 0.0326 217 HIS C CE1 +6456 N NE2 . HIS C 218 ? 1.1842 0.7458 1.1012 0.2338 0.0093 0.0317 217 HIS C NE2 +6457 N N . MET C 219 ? 1.1422 0.6779 1.0276 0.2301 0.0110 0.0308 218 MET C N +6458 C CA . MET C 219 ? 1.0689 0.6067 0.9584 0.2289 0.0109 0.0299 218 MET C CA +6459 C C . MET C 219 ? 1.1260 0.6685 1.0218 0.2269 0.0119 0.0291 218 MET C C +6460 O O . MET C 219 ? 1.1507 0.6903 1.0425 0.2256 0.0131 0.0289 218 MET C O +6461 C CB . MET C 219 ? 0.9557 0.4861 0.8366 0.2283 0.0108 0.0297 218 MET C CB +6462 C CG . MET C 219 ? 0.7938 0.3258 0.6783 0.2270 0.0107 0.0288 218 MET C CG +6463 S SD . MET C 219 ? 1.1095 0.6324 0.9833 0.2260 0.0109 0.0284 218 MET C SD +6464 C CE . MET C 219 ? 1.0350 0.5531 0.9023 0.2237 0.0126 0.0280 218 MET C CE +6465 N N . VAL C 220 ? 1.0337 0.5831 0.9392 0.2268 0.0115 0.0286 219 VAL C N +6466 C CA . VAL C 220 ? 1.0743 0.6278 0.9857 0.2247 0.0124 0.0276 219 VAL C CA +6467 C C . VAL C 220 ? 0.7542 0.3054 0.6642 0.2234 0.0124 0.0267 219 VAL C C +6468 O O . VAL C 220 ? 1.1423 0.6955 1.0557 0.2241 0.0114 0.0266 219 VAL C O +6469 C CB . VAL C 220 ? 0.9767 0.5394 0.8998 0.2251 0.0119 0.0274 219 VAL C CB +6470 C CG1 . VAL C 220 ? 0.9234 0.4896 0.8513 0.2231 0.0130 0.0265 219 VAL C CG1 +6471 C CG2 . VAL C 220 ? 1.0852 0.6503 1.0100 0.2269 0.0115 0.0284 219 VAL C CG2 +6472 N N . LEU C 221 ? 1.0940 0.6408 0.9988 0.2215 0.0136 0.0261 220 LEU C N +6473 C CA . LEU C 221 ? 0.9953 0.5390 0.8976 0.2200 0.0138 0.0252 220 LEU C CA +6474 C C . LEU C 221 ? 1.1584 0.7070 1.0678 0.2180 0.0146 0.0241 220 LEU C C +6475 O O . LEU C 221 ? 1.3557 0.9056 1.2664 0.2169 0.0156 0.0238 220 LEU C O +6476 C CB . LEU C 221 ? 0.8972 0.4320 0.7879 0.2191 0.0146 0.0253 220 LEU C CB +6477 C CG . LEU C 221 ? 1.1615 0.6922 1.0485 0.2172 0.0151 0.0244 220 LEU C CG +6478 C CD1 . LEU C 221 ? 0.9922 0.5224 0.8795 0.2182 0.0139 0.0243 220 LEU C CD1 +6479 C CD2 . LEU C 221 ? 1.0812 0.6033 0.9570 0.2161 0.0160 0.0244 220 LEU C CD2 +6480 N N . LEU C 222 ? 1.7324 1.2834 1.6462 0.2176 0.0141 0.0234 221 LEU C N +6481 C CA . LEU C 222 ? 1.1280 0.6831 1.0481 0.2158 0.0147 0.0221 221 LEU C CA +6482 C C . LEU C 222 ? 1.2440 0.7944 1.1596 0.2144 0.0150 0.0213 221 LEU C C +6483 O O . LEU C 222 ? 1.1635 0.7133 1.0791 0.2152 0.0141 0.0214 221 LEU C O +6484 C CB . LEU C 222 ? 1.0926 0.6562 1.0239 0.2165 0.0138 0.0219 221 LEU C CB +6485 C CG . LEU C 222 ? 1.3597 0.9291 1.2972 0.2176 0.0135 0.0224 221 LEU C CG +6486 C CD1 . LEU C 222 ? 0.8032 0.3802 0.7509 0.2183 0.0125 0.0222 221 LEU C CD1 +6487 C CD2 . LEU C 222 ? 1.0612 0.6321 1.0001 0.2160 0.0147 0.0219 221 LEU C CD2 +6488 N N . GLU C 223 ? 1.1537 0.7010 1.0656 0.2124 0.0163 0.0206 222 GLU C N +6489 C CA . GLU C 223 ? 1.2719 0.8144 1.1792 0.2109 0.0167 0.0198 222 GLU C CA +6490 C C . GLU C 223 ? 1.1396 0.6862 1.0533 0.2090 0.0174 0.0184 222 GLU C C +6491 O O . GLU C 223 ? 1.2633 0.8132 1.1810 0.2079 0.0182 0.0179 222 GLU C O +6492 C CB . GLU C 223 ? 1.1409 0.6751 1.0372 0.2099 0.0177 0.0200 222 GLU C CB +6493 C CG . GLU C 223 ? 1.7750 1.3026 1.6624 0.2112 0.0171 0.0210 222 GLU C CG +6494 C CD . GLU C 223 ? 2.2794 1.7984 2.1557 0.2098 0.0180 0.0209 222 GLU C CD +6495 O OE1 . GLU C 223 ? 2.2423 1.7600 2.1179 0.2076 0.0192 0.0199 222 GLU C OE1 +6496 O OE2 . GLU C 223 ? 2.3019 1.8153 2.1703 0.2109 0.0176 0.0218 222 GLU C OE2 +6497 N N . PHE C 224 ? 1.2833 0.8296 1.1980 0.2085 0.0171 0.0177 223 PHE C N +6498 C CA . PHE C 224 ? 1.1165 0.6648 1.0351 0.2064 0.0179 0.0162 223 PHE C CA +6499 C C . PHE C 224 ? 0.9008 0.4412 0.8101 0.2050 0.0187 0.0158 223 PHE C C +6500 O O . PHE C 224 ? 1.4522 0.9877 1.3554 0.2059 0.0180 0.0163 223 PHE C O +6501 C CB . PHE C 224 ? 1.1372 0.6919 1.0649 0.2069 0.0170 0.0156 223 PHE C CB +6502 C CG . PHE C 224 ? 1.3118 0.8740 1.2483 0.2085 0.0160 0.0161 223 PHE C CG +6503 C CD1 . PHE C 224 ? 1.1796 0.7443 1.1180 0.2089 0.0163 0.0167 223 PHE C CD1 +6504 C CD2 . PHE C 224 ? 1.0475 0.6143 0.9906 0.2096 0.0148 0.0160 223 PHE C CD2 +6505 C CE1 . PHE C 224 ? 1.0378 0.6093 0.9842 0.2103 0.0154 0.0171 223 PHE C CE1 +6506 C CE2 . PHE C 224 ? 1.0723 0.6460 1.0234 0.2110 0.0139 0.0165 223 PHE C CE2 +6507 C CZ . PHE C 224 ? 1.3970 0.9730 1.3498 0.2113 0.0142 0.0171 223 PHE C CZ +6508 N N . VAL C 225 ? 1.3252 0.8639 1.2330 0.2028 0.0200 0.0148 224 VAL C N +6509 C CA . VAL C 225 ? 1.2452 0.7764 1.1443 0.2012 0.0208 0.0143 224 VAL C CA +6510 C C . VAL C 225 ? 1.4213 0.9542 1.3240 0.1989 0.0218 0.0127 224 VAL C C +6511 O O . VAL C 225 ? 1.2651 0.8010 1.1715 0.1978 0.0227 0.0122 224 VAL C O +6512 C CB . VAL C 225 ? 1.1846 0.7090 1.0741 0.2007 0.0217 0.0150 224 VAL C CB +6513 C CG1 . VAL C 225 ? 1.2768 0.7928 1.1563 0.1995 0.0222 0.0147 224 VAL C CG1 +6514 C CG2 . VAL C 225 ? 1.3579 0.8816 1.2449 0.2029 0.0208 0.0165 224 VAL C CG2 +6515 N N . THR C 226 ? 1.3702 0.9012 1.2718 0.1982 0.0217 0.0119 225 THR C N +6516 C CA . THR C 226 ? 1.3857 0.9172 1.2895 0.1960 0.0227 0.0103 225 THR C CA +6517 C C . THR C 226 ? 1.2032 0.7266 1.0976 0.1945 0.0235 0.0099 225 THR C C +6518 O O . THR C 226 ? 1.3589 0.8788 1.2491 0.1953 0.0227 0.0103 225 THR C O +6519 C CB . THR C 226 ? 1.2298 0.7685 1.1438 0.1961 0.0221 0.0093 225 THR C CB +6520 O OG1 . THR C 226 ? 1.0899 0.6356 1.0120 0.1980 0.0210 0.0100 225 THR C OG1 +6521 C CG2 . THR C 226 ? 1.3974 0.9386 1.3157 0.1939 0.0232 0.0077 225 THR C CG2 +6522 N N . ALA C 227 ? 1.1406 0.6610 1.0317 0.1922 0.0249 0.0090 226 ALA C N +6523 C CA . ALA C 227 ? 1.2615 0.7747 1.1447 0.1905 0.0257 0.0083 226 ALA C CA +6524 C C . ALA C 227 ? 1.4551 0.9712 1.3435 0.1898 0.0255 0.0070 226 ALA C C +6525 O O . ALA C 227 ? 1.5631 1.0868 1.4615 0.1901 0.0251 0.0063 226 ALA C O +6526 C CB . ALA C 227 ? 1.2589 0.7683 1.1373 0.1882 0.0273 0.0077 226 ALA C CB +6527 N N . ALA C 228 ? 1.3626 0.8726 1.2442 0.1889 0.0257 0.0066 227 ALA C N +6528 C CA . ALA C 228 ? 1.3946 0.9063 1.2799 0.1886 0.0254 0.0055 227 ALA C CA +6529 C C . ALA C 228 ? 1.5811 1.0847 1.4570 0.1871 0.0260 0.0050 227 ALA C C +6530 O O . ALA C 228 ? 1.5386 1.0356 1.4057 0.1860 0.0268 0.0054 227 ALA C O +6531 C CB . ALA C 228 ? 1.2736 0.7891 1.1634 0.1911 0.0236 0.0064 227 ALA C CB +6532 N N . GLY C 229 ? 1.6049 1.1088 1.4824 0.1870 0.0255 0.0043 228 GLY C N +6533 C CA . GLY C 229 ? 1.7507 1.2468 1.6191 0.1860 0.0258 0.0040 228 GLY C CA +6534 C C . GLY C 229 ? 1.9218 1.4133 1.7855 0.1831 0.0275 0.0027 228 GLY C C +6535 O O . GLY C 229 ? 1.8835 1.3664 1.7365 0.1826 0.0281 0.0026 228 GLY C O +6536 N N . ILE C 230 ? 1.8832 1.3786 1.7522 0.1817 0.0286 0.0017 229 ILE C N +6537 C CA . ILE C 230 ? 1.9455 1.4356 1.8083 0.1800 0.0308 0.0003 229 ILE C CA +6538 C C . ILE C 230 ? 2.8537 2.3521 2.7282 0.1797 0.0307 -0.0012 229 ILE C C +6539 O O . ILE C 230 ? 3.2444 2.7524 3.1309 0.1802 0.0296 -0.0012 229 ILE C O +6540 C CB . ILE C 230 ? 1.7175 1.2044 1.5755 0.1787 0.0325 0.0003 229 ILE C CB +6541 C CG1 . ILE C 230 ? 1.6618 1.1389 1.5065 0.1787 0.0329 0.0015 229 ILE C CG1 +6542 C CG2 . ILE C 230 ? 2.0179 1.5021 1.8733 0.1769 0.0347 -0.0013 229 ILE C CG2 +6543 C CD1 . ILE C 230 ? 1.6058 1.0800 1.4460 0.1775 0.0343 0.0018 229 ILE C CD1 +6544 N N . THR C 231 ? 3.0897 2.5846 2.9608 0.1790 0.0318 -0.0025 230 THR C N +6545 C CA . THR C 231 ? 3.2806 2.7827 3.1619 0.1787 0.0318 -0.0040 230 THR C CA +6546 C C . THR C 231 ? 3.3631 2.8717 3.2524 0.1779 0.0325 -0.0048 230 THR C C +6547 O O . THR C 231 ? 3.0026 2.5165 2.8995 0.1774 0.0328 -0.0062 230 THR C O +6548 C CB . THR C 231 ? 2.9958 2.4915 2.8701 0.1778 0.0334 -0.0054 230 THR C CB +6549 O OG1 . THR C 231 ? 2.8523 2.3553 2.7368 0.1775 0.0335 -0.0070 230 THR C OG1 +6550 C CG2 . THR C 231 ? 2.8157 2.3021 2.6779 0.1760 0.0359 -0.0058 230 THR C CG2 +6551 N N . ALA C 235 ? 1.9289 1.8748 1.6266 0.1648 -0.0882 0.0598 1054 ALA C N +6552 C CA . ALA C 235 ? 2.1267 2.0745 1.8276 0.1655 -0.0899 0.0550 1054 ALA C CA +6553 C C . ALA C 235 ? 2.3589 2.3023 2.0522 0.1657 -0.0836 0.0525 1054 ALA C C +6554 O O . ALA C 235 ? 1.9043 1.8433 1.5889 0.1644 -0.0777 0.0533 1054 ALA C O +6555 C CB . ALA C 235 ? 1.5010 1.4523 1.2120 0.1686 -0.0957 0.0566 1054 ALA C CB +6556 N N . SER C 236 ? 2.5707 2.5152 2.2675 0.1673 -0.0851 0.0495 1055 SER C N +6557 C CA . SER C 236 ? 2.7265 2.6671 2.4174 0.1680 -0.0797 0.0474 1055 SER C CA +6558 C C . SER C 236 ? 2.9807 2.9187 2.6726 0.1713 -0.0787 0.0518 1055 SER C C +6559 O O . SER C 236 ? 2.5912 2.5251 2.2776 0.1722 -0.0737 0.0515 1055 SER C O +6560 C CB . SER C 236 ? 2.3086 2.2517 2.0026 0.1681 -0.0817 0.0419 1055 SER C CB +6561 O OG . SER C 236 ? 2.1089 2.0480 1.7963 0.1683 -0.0762 0.0395 1055 SER C OG +6562 N N . THR C 237 ? 3.1785 3.1190 2.8777 0.1730 -0.0835 0.0559 1056 THR C N +6563 C CA . THR C 237 ? 2.8404 2.7789 2.5413 0.1760 -0.0831 0.0608 1056 THR C CA +6564 C C . THR C 237 ? 2.4318 2.3649 2.1236 0.1754 -0.0767 0.0639 1056 THR C C +6565 O O . THR C 237 ? 1.8577 1.7875 1.5476 0.1776 -0.0740 0.0669 1056 THR C O +6566 C CB . THR C 237 ? 2.3121 2.2546 2.0224 0.1775 -0.0897 0.0646 1056 THR C CB +6567 O OG1 . THR C 237 ? 2.1626 2.1050 1.8709 0.1756 -0.0897 0.0675 1056 THR C OG1 +6568 C CG2 . THR C 237 ? 2.0190 1.9671 1.7380 0.1776 -0.0962 0.0613 1056 THR C CG2 +6569 N N . LYS C 238 ? 2.7574 2.6895 2.4435 0.1724 -0.0742 0.0633 1057 LYS C N +6570 C CA . LYS C 238 ? 2.5664 2.4933 2.2429 0.1713 -0.0677 0.0654 1057 LYS C CA +6571 C C . LYS C 238 ? 2.2001 2.1227 1.8700 0.1720 -0.0619 0.0633 1057 LYS C C +6572 O O . LYS C 238 ? 1.8507 1.7696 1.5175 0.1738 -0.0585 0.0666 1057 LYS C O +6573 C CB . LYS C 238 ? 2.3754 2.3025 2.0469 0.1676 -0.0661 0.0636 1057 LYS C CB +6574 C CG . LYS C 238 ? 2.3164 2.2452 1.9902 0.1667 -0.0688 0.0676 1057 LYS C CG +6575 C CD . LYS C 238 ? 1.9981 1.9325 1.6829 0.1679 -0.0766 0.0684 1057 LYS C CD +6576 C CE . LYS C 238 ? 1.7141 1.6503 1.4007 0.1666 -0.0793 0.0717 1057 LYS C CE +6577 N NZ . LYS C 238 ? 1.6936 1.6352 1.3910 0.1679 -0.0868 0.0727 1057 LYS C NZ +6578 N N . LYS C 239 ? 2.3722 2.2956 2.0404 0.1706 -0.0611 0.0577 1058 LYS C N +6579 C CA . LYS C 239 ? 2.6101 2.5296 2.2715 0.1707 -0.0554 0.0549 1058 LYS C CA +6580 C C . LYS C 239 ? 2.5004 2.4183 2.1641 0.1742 -0.0550 0.0567 1058 LYS C C +6581 O O . LYS C 239 ? 2.2945 2.2079 1.9516 0.1748 -0.0495 0.0564 1058 LYS C O +6582 C CB . LYS C 239 ? 2.7177 2.6393 2.3790 0.1689 -0.0560 0.0486 1058 LYS C CB +6583 C CG . LYS C 239 ? 2.4159 2.3392 2.0749 0.1654 -0.0565 0.0464 1058 LYS C CG +6584 C CD . LYS C 239 ? 2.4016 2.3264 2.0594 0.1636 -0.0562 0.0400 1058 LYS C CD +6585 C CE . LYS C 239 ? 2.3701 2.2903 2.0205 0.1640 -0.0500 0.0376 1058 LYS C CE +6586 N NZ . LYS C 239 ? 1.9440 1.8659 1.5946 0.1630 -0.0502 0.0315 1058 LYS C NZ +6587 N N . LEU C 240 ? 2.4276 2.3491 2.1007 0.1766 -0.0610 0.0585 1059 LEU C N +6588 C CA . LEU C 240 ? 2.4944 2.4152 2.1711 0.1800 -0.0615 0.0600 1059 LEU C CA +6589 C C . LEU C 240 ? 2.4007 2.3176 2.0743 0.1818 -0.0584 0.0656 1059 LEU C C +6590 O O . LEU C 240 ? 1.7838 1.6970 1.4535 0.1834 -0.0543 0.0661 1059 LEU C O +6591 C CB . LEU C 240 ? 2.5546 2.4808 2.2425 0.1818 -0.0691 0.0602 1059 LEU C CB +6592 C CG . LEU C 240 ? 2.3467 2.2727 2.0397 0.1855 -0.0707 0.0627 1059 LEU C CG +6593 C CD1 . LEU C 240 ? 2.2763 2.1999 1.9658 0.1865 -0.0672 0.0592 1059 LEU C CD1 +6594 C CD2 . LEU C 240 ? 2.0523 1.9838 1.7563 0.1869 -0.0785 0.0629 1059 LEU C CD2 +6595 N N . SER C 241 ? 2.6387 2.5565 2.3143 0.1815 -0.0604 0.0699 1060 SER C N +6596 C CA . SER C 241 ? 2.3304 2.2449 2.0040 0.1832 -0.0582 0.0755 1060 SER C CA +6597 C C . SER C 241 ? 2.0586 1.9675 1.7212 0.1817 -0.0507 0.0761 1060 SER C C +6598 O O . SER C 241 ? 1.9638 1.8691 1.6231 0.1832 -0.0474 0.0801 1060 SER C O +6599 C CB . SER C 241 ? 1.8979 1.8152 1.5769 0.1831 -0.0627 0.0797 1060 SER C CB +6600 O OG . SER C 241 ? 1.9256 1.8425 1.5998 0.1799 -0.0611 0.0794 1060 SER C OG +6601 N N . GLU C 242 ? 1.9701 1.8785 1.6270 0.1787 -0.0479 0.0720 1061 GLU C N +6602 C CA . GLU C 242 ? 2.3453 2.2484 1.9915 0.1772 -0.0406 0.0719 1061 GLU C CA +6603 C C . GLU C 242 ? 2.1402 2.0398 1.7830 0.1792 -0.0365 0.0711 1061 GLU C C +6604 O O . GLU C 242 ? 1.8706 1.7653 1.5064 0.1796 -0.0310 0.0734 1061 GLU C O +6605 C CB . GLU C 242 ? 2.4065 2.3099 2.0476 0.1736 -0.0386 0.0672 1061 GLU C CB +6606 C CG . GLU C 242 ? 2.4770 2.3846 2.1222 0.1715 -0.0432 0.0670 1061 GLU C CG +6607 C CD . GLU C 242 ? 2.5614 2.4685 2.2068 0.1714 -0.0438 0.0725 1061 GLU C CD +6608 O OE1 . GLU C 242 ? 2.6674 2.5700 2.3069 0.1719 -0.0391 0.0759 1061 GLU C OE1 +6609 O OE2 . GLU C 242 ? 2.3234 2.2346 1.9748 0.1707 -0.0491 0.0733 1061 GLU C OE2 +6610 N N . SER C 243 ? 2.2497 2.1518 1.8977 0.1806 -0.0394 0.0678 1062 SER C N +6611 C CA . SER C 243 ? 2.6164 2.5156 2.2620 0.1826 -0.0361 0.0667 1062 SER C CA +6612 C C . SER C 243 ? 2.3816 2.2799 2.0311 0.1861 -0.0372 0.0715 1062 SER C C +6613 O O . SER C 243 ? 1.6547 1.5485 1.2987 0.1874 -0.0323 0.0734 1062 SER C O +6614 C CB . SER C 243 ? 2.7549 2.6572 2.4047 0.1827 -0.0389 0.0613 1062 SER C CB +6615 O OG . SER C 243 ? 2.6314 2.5340 2.2767 0.1796 -0.0371 0.0566 1062 SER C OG +6616 N N . LEU C 244 ? 2.2984 2.2009 1.9573 0.1876 -0.0437 0.0736 1063 LEU C N +6617 C CA . LEU C 244 ? 2.0625 1.9647 1.7259 0.1908 -0.0454 0.0784 1063 LEU C CA +6618 C C . LEU C 244 ? 2.1850 2.0828 1.8421 0.1908 -0.0409 0.0832 1063 LEU C C +6619 O O . LEU C 244 ? 1.8890 1.7839 1.5448 0.1931 -0.0386 0.0863 1063 LEU C O +6620 C CB . LEU C 244 ? 1.7054 1.6129 1.3793 0.1918 -0.0530 0.0802 1063 LEU C CB +6621 C CG . LEU C 244 ? 1.9798 1.8911 1.6617 0.1936 -0.0579 0.0772 1063 LEU C CG +6622 C CD1 . LEU C 244 ? 1.9828 1.8991 1.6749 0.1947 -0.0652 0.0796 1063 LEU C CD1 +6623 C CD2 . LEU C 244 ? 1.7051 1.6137 1.3861 0.1965 -0.0554 0.0777 1063 LEU C CD2 +6624 N N . LYS C 245 ? 2.2678 2.1653 1.9210 0.1880 -0.0398 0.0837 1064 LYS C N +6625 C CA . LYS C 245 ? 2.1976 2.0907 1.8435 0.1873 -0.0348 0.0875 1064 LYS C CA +6626 C C . LYS C 245 ? 2.2529 2.1407 1.8904 0.1879 -0.0278 0.0868 1064 LYS C C +6627 O O . LYS C 245 ? 2.3455 2.2304 1.9820 0.1902 -0.0258 0.0905 1064 LYS C O +6628 C CB . LYS C 245 ? 1.9319 1.8253 1.5736 0.1838 -0.0338 0.0866 1064 LYS C CB +6629 C CG . LYS C 245 ? 2.2295 2.1261 1.8768 0.1834 -0.0387 0.0901 1064 LYS C CG +6630 C CD . LYS C 245 ? 2.6016 2.4984 2.2444 0.1798 -0.0374 0.0888 1064 LYS C CD +6631 C CE . LYS C 245 ? 2.4909 2.3903 2.1384 0.1794 -0.0416 0.0927 1064 LYS C CE +6632 N NZ . LYS C 245 ? 1.8903 1.7895 1.5327 0.1760 -0.0399 0.0919 1064 LYS C NZ +6633 N N . ARG C 246 ? 2.1740 2.0604 1.8057 0.1858 -0.0243 0.0820 1065 ARG C N +6634 C CA . ARG C 246 ? 2.3889 2.2700 2.0117 0.1860 -0.0172 0.0811 1065 ARG C CA +6635 C C . ARG C 246 ? 2.2667 2.1467 1.8918 0.1893 -0.0169 0.0817 1065 ARG C C +6636 O O . ARG C 246 ? 2.0139 1.8893 1.6334 0.1905 -0.0119 0.0839 1065 ARG C O +6637 C CB . ARG C 246 ? 2.3378 2.2179 1.9542 0.1831 -0.0137 0.0756 1065 ARG C CB +6638 C CG . ARG C 246 ? 2.5056 2.3852 2.1170 0.1797 -0.0120 0.0754 1065 ARG C CG +6639 C CD . ARG C 246 ? 2.7637 2.6422 2.3687 0.1770 -0.0082 0.0698 1065 ARG C CD +6640 N NE . ARG C 246 ? 3.0317 2.9101 2.6321 0.1736 -0.0068 0.0693 1065 ARG C NE +6641 C CZ . ARG C 246 ? 2.7482 2.6261 2.3434 0.1709 -0.0042 0.0646 1065 ARG C CZ +6642 N NH1 . ARG C 246 ? 2.4886 2.3660 2.0823 0.1710 -0.0026 0.0601 1065 ARG C NH1 +6643 N NH2 . ARG C 246 ? 2.1640 2.0418 1.7553 0.1679 -0.0031 0.0645 1065 ARG C NH2 +6644 N N . ILE C 247 ? 2.0892 1.9732 1.7226 0.1909 -0.0222 0.0798 1066 ILE C N +6645 C CA . ILE C 247 ? 2.1002 1.9835 1.7364 0.1941 -0.0223 0.0800 1066 ILE C CA +6646 C C . ILE C 247 ? 2.1387 2.0204 1.7769 0.1968 -0.0224 0.0860 1066 ILE C C +6647 O O . ILE C 247 ? 1.5624 1.4407 1.1976 0.1988 -0.0189 0.0873 1066 ILE C O +6648 C CB . ILE C 247 ? 2.1000 1.9884 1.7451 0.1951 -0.0283 0.0765 1066 ILE C CB +6649 C CG1 . ILE C 247 ? 2.5752 2.4644 2.2173 0.1927 -0.0271 0.0702 1066 ILE C CG1 +6650 C CG2 . ILE C 247 ? 1.4551 1.3433 1.1045 0.1986 -0.0294 0.0776 1066 ILE C CG2 +6651 C CD1 . ILE C 247 ? 2.7669 2.6614 2.4175 0.1930 -0.0332 0.0666 1066 ILE C CD1 +6652 N N . GLY C 248 ? 2.2648 2.1489 1.9079 0.1968 -0.0265 0.0897 1067 GLY C N +6653 C CA . GLY C 248 ? 1.9864 1.8690 1.6310 0.1991 -0.0266 0.0955 1067 GLY C CA +6654 C C . GLY C 248 ? 2.1387 2.0161 1.7738 0.1979 -0.0202 0.0982 1067 GLY C C +6655 O O . GLY C 248 ? 1.9252 1.7997 1.5587 0.1998 -0.0181 0.1026 1067 GLY C O +6656 N N . ASP C 249 ? 2.2855 2.1618 1.9142 0.1947 -0.0172 0.0955 1068 ASP C N +6657 C CA . ASP C 249 ? 2.1879 2.0595 1.8073 0.1931 -0.0111 0.0976 1068 ASP C CA +6658 C C . ASP C 249 ? 2.1697 2.0362 1.7814 0.1939 -0.0045 0.0967 1068 ASP C C +6659 O O . ASP C 249 ? 1.8426 1.7055 1.4509 0.1954 -0.0012 0.1008 1068 ASP C O +6660 C CB . ASP C 249 ? 2.2639 2.1363 1.8794 0.1894 -0.0103 0.0951 1068 ASP C CB +6661 C CG . ASP C 249 ? 2.5169 2.3924 2.1372 0.1885 -0.0149 0.0980 1068 ASP C CG +6662 O OD1 . ASP C 249 ? 2.5661 2.4442 2.1942 0.1907 -0.0197 0.1013 1068 ASP C OD1 +6663 O OD2 . ASP C 249 ? 2.4649 2.3404 2.0814 0.1856 -0.0138 0.0971 1068 ASP C OD2 +6664 N N . GLU C 250 ? 2.5034 2.3698 2.1124 0.1929 -0.0026 0.0914 1069 GLU C N +6665 C CA . GLU C 250 ? 2.5945 2.4564 2.1966 0.1937 0.0033 0.0899 1069 GLU C CA +6666 C C . GLU C 250 ? 2.3040 2.1648 1.9095 0.1974 0.0028 0.0932 1069 GLU C C +6667 O O . GLU C 250 ? 1.5284 1.3846 1.1279 0.1985 0.0080 0.0949 1069 GLU C O +6668 C CB . GLU C 250 ? 2.4473 2.3104 2.0489 0.1927 0.0035 0.0836 1069 GLU C CB +6669 C CG . GLU C 250 ? 2.6997 2.5639 2.2979 0.1890 0.0041 0.0798 1069 GLU C CG +6670 C CD . GLU C 250 ? 2.6895 2.5566 2.2903 0.1883 0.0021 0.0738 1069 GLU C CD +6671 O OE1 . GLU C 250 ? 2.3685 2.2362 1.9729 0.1907 0.0008 0.0725 1069 GLU C OE1 +6672 O OE2 . GLU C 250 ? 2.5428 2.4115 2.1420 0.1854 0.0017 0.0704 1069 GLU C OE2 +6673 N N . LEU C 251 ? 2.2653 2.1305 1.8806 0.1993 -0.0036 0.0940 1070 LEU C N +6674 C CA . LEU C 251 ? 2.0668 1.9319 1.6869 0.2029 -0.0053 0.0973 1070 LEU C CA +6675 C C . LEU C 251 ? 2.1622 2.0242 1.7797 0.2040 -0.0031 0.1033 1070 LEU C C +6676 O O . LEU C 251 ? 1.4883 1.3464 1.1020 0.2059 0.0010 0.1053 1070 LEU C O +6677 C CB . LEU C 251 ? 1.9712 1.8421 1.6026 0.2043 -0.0131 0.0970 1070 LEU C CB +6678 C CG . LEU C 251 ? 2.0321 1.9043 1.6705 0.2080 -0.0164 0.0994 1070 LEU C CG +6679 C CD1 . LEU C 251 ? 1.9002 1.7685 1.5341 0.2098 -0.0116 0.0986 1070 LEU C CD1 +6680 C CD2 . LEU C 251 ? 1.5085 1.3864 1.1569 0.2086 -0.0235 0.0969 1070 LEU C CD2 +6681 N N . ASP C 252 ? 2.4199 2.2835 2.0395 0.2029 -0.0056 0.1062 1071 ASP C N +6682 C CA . ASP C 252 ? 2.1689 2.0299 1.7868 0.2039 -0.0040 0.1121 1071 ASP C CA +6683 C C . ASP C 252 ? 2.1534 2.0088 1.7602 0.2024 0.0036 0.1129 1071 ASP C C +6684 O O . ASP C 252 ? 1.8945 1.7465 1.4981 0.2037 0.0066 0.1173 1071 ASP C O +6685 C CB . ASP C 252 ? 1.6778 1.5423 1.3014 0.2033 -0.0091 0.1151 1071 ASP C CB +6686 C CG . ASP C 252 ? 2.7342 2.5961 2.3563 0.2044 -0.0076 0.1213 1071 ASP C CG +6687 O OD1 . ASP C 252 ? 2.6176 2.4788 2.2428 0.2074 -0.0082 0.1244 1071 ASP C OD1 +6688 O OD2 . ASP C 252 ? 3.2854 3.1461 2.9033 0.2023 -0.0058 0.1230 1071 ASP C OD2 +6689 N N . SER C 253 ? 2.2130 2.0674 1.8139 0.1996 0.0068 0.1085 1072 SER C N +6690 C CA . SER C 253 ? 2.5282 2.3774 2.1183 0.1979 0.0140 0.1087 1072 SER C CA +6691 C C . SER C 253 ? 2.6714 2.5168 2.2556 0.1988 0.0193 0.1062 1072 SER C C +6692 O O . SER C 253 ? 2.4862 2.3269 2.0614 0.1978 0.0256 0.1067 1072 SER C O +6693 C CB . SER C 253 ? 2.5124 2.3623 2.0986 0.1941 0.0148 0.1060 1072 SER C CB +6694 O OG . SER C 253 ? 2.4703 2.3216 2.0558 0.1927 0.0149 0.1000 1072 SER C OG +6695 N N . ASN C 254 ? 2.9613 2.8087 2.5504 0.2006 0.0169 0.1035 1073 ASN C N +6696 C CA . ASN C 254 ? 2.9585 2.8026 2.5427 0.2017 0.0216 0.1011 1073 ASN C CA +6697 C C . ASN C 254 ? 2.8611 2.7008 2.4416 0.2040 0.0256 0.1056 1073 ASN C C +6698 O O . ASN C 254 ? 2.3849 2.2255 1.9710 0.2070 0.0229 0.1084 1073 ASN C O +6699 C CB . ASN C 254 ? 2.8483 2.6958 2.4395 0.2035 0.0175 0.0978 1073 ASN C CB +6700 C CG . ASN C 254 ? 2.5881 2.4347 2.1747 0.2021 0.0206 0.0919 1073 ASN C CG +6701 O OD1 . ASN C 254 ? 2.5420 2.3873 2.1226 0.1991 0.0236 0.0894 1073 ASN C OD1 +6702 N ND2 . ASN C 254 ? 2.3559 2.2030 1.9454 0.2042 0.0198 0.0897 1073 ASN C ND2 +6703 N N . MET C 255 ? 3.1275 2.9623 2.6983 0.2026 0.0322 0.1063 1074 MET C N +6704 C CA . MET C 255 ? 3.1716 3.0020 2.7381 0.2044 0.0364 0.1110 1074 MET C CA +6705 C C . MET C 255 ? 3.0248 2.8534 2.5915 0.2074 0.0381 0.1106 1074 MET C C +6706 O O . MET C 255 ? 2.6477 2.4741 2.2144 0.2097 0.0393 0.1149 1074 MET C O +6707 C CB . MET C 255 ? 3.2071 3.0327 2.7630 0.2020 0.0431 0.1114 1074 MET C CB +6708 C CG . MET C 255 ? 3.1338 2.9604 2.6892 0.1997 0.0419 0.1138 1074 MET C CG +6709 S SD . MET C 255 ? 3.3498 3.1781 2.9123 0.2020 0.0372 0.1205 1074 MET C SD +6710 C CE . MET C 255 ? 1.9215 1.7440 1.4781 0.2045 0.0431 0.1248 1074 MET C CE +6711 N N . GLU C 256 ? 3.1371 2.9666 2.7041 0.2072 0.0381 0.1056 1075 GLU C N +6712 C CA . GLU C 256 ? 2.9784 2.8068 2.5465 0.2100 0.0392 0.1048 1075 GLU C CA +6713 C C . GLU C 256 ? 2.6648 2.4962 2.2422 0.2131 0.0336 0.1081 1075 GLU C C +6714 O O . GLU C 256 ? 2.2652 2.0943 1.8424 0.2156 0.0351 0.1119 1075 GLU C O +6715 C CB . GLU C 256 ? 2.9732 2.8037 2.5425 0.2093 0.0382 0.0987 1075 GLU C CB +6716 C CG . GLU C 256 ? 2.9166 2.7454 2.4783 0.2060 0.0423 0.0944 1075 GLU C CG +6717 C CD . GLU C 256 ? 2.8950 2.7266 2.4593 0.2054 0.0403 0.0885 1075 GLU C CD +6718 O OE1 . GLU C 256 ? 2.9301 2.7663 2.5034 0.2066 0.0341 0.0877 1075 GLU C OE1 +6719 O OE2 . GLU C 256 ? 2.7504 2.5795 2.3079 0.2038 0.0449 0.0847 1075 GLU C OE2 +6720 N N . LEU C 257 ? 2.4905 2.3272 2.0761 0.2127 0.0271 0.1067 1076 LEU C N +6721 C CA . LEU C 257 ? 2.3997 2.2402 1.9953 0.2154 0.0208 0.1090 1076 LEU C CA +6722 C C . LEU C 257 ? 2.3502 2.1899 1.9475 0.2167 0.0199 0.1153 1076 LEU C C +6723 O O . LEU C 257 ? 1.7357 1.5753 1.3369 0.2197 0.0186 0.1184 1076 LEU C O +6724 C CB . LEU C 257 ? 2.2105 2.0567 1.8136 0.2141 0.0145 0.1059 1076 LEU C CB +6725 C CG . LEU C 257 ? 2.1914 2.0424 1.8056 0.2163 0.0071 0.1079 1076 LEU C CG +6726 C CD1 . LEU C 257 ? 1.9448 1.7955 1.5625 0.2198 0.0065 0.1085 1076 LEU C CD1 +6727 C CD2 . LEU C 257 ? 2.3655 2.2216 1.9854 0.2146 0.0019 0.1038 1076 LEU C CD2 +6728 N N . GLN C 258 ? 2.4303 2.2695 2.0246 0.2144 0.0206 0.1172 1077 GLN C N +6729 C CA . GLN C 258 ? 2.3388 2.1775 1.9348 0.2154 0.0196 0.1231 1077 GLN C CA +6730 C C . GLN C 258 ? 2.4445 2.2782 2.0353 0.2175 0.0247 0.1267 1077 GLN C C +6731 O O . GLN C 258 ? 2.3385 2.1725 1.9336 0.2201 0.0227 0.1310 1077 GLN C O +6732 C CB . GLN C 258 ? 2.0526 1.8911 1.6450 0.2123 0.0203 0.1242 1077 GLN C CB +6733 C CG . GLN C 258 ? 2.3446 2.1880 1.9420 0.2101 0.0152 0.1209 1077 GLN C CG +6734 C CD . GLN C 258 ? 2.3115 2.1601 1.9200 0.2118 0.0075 0.1225 1077 GLN C CD +6735 O OE1 . GLN C 258 ? 2.2943 2.1429 1.9064 0.2138 0.0058 0.1274 1077 GLN C OE1 +6736 N NE2 . GLN C 258 ? 1.7106 1.5637 1.3247 0.2109 0.0030 0.1185 1077 GLN C NE2 +6737 N N . ARG C 259 ? 2.3700 2.1993 1.9516 0.2165 0.0313 0.1248 1078 ARG C N +6738 C CA . ARG C 259 ? 2.4255 2.2499 2.0016 0.2184 0.0366 0.1274 1078 ARG C CA +6739 C C . ARG C 259 ? 2.5186 2.3441 2.1003 0.2218 0.0344 0.1275 1078 ARG C C +6740 O O . ARG C 259 ? 2.4346 2.2587 2.0176 0.2244 0.0346 0.1318 1078 ARG C O +6741 C CB . ARG C 259 ? 2.6831 2.5031 2.2489 0.2165 0.0437 0.1243 1078 ARG C CB +6742 C CG . ARG C 259 ? 2.7181 2.5326 2.2770 0.2182 0.0498 0.1271 1078 ARG C CG +6743 C CD . ARG C 259 ? 2.9308 2.7422 2.4830 0.2178 0.0550 0.1228 1078 ARG C CD +6744 N NE . ARG C 259 ? 3.0388 2.8494 2.5849 0.2144 0.0580 0.1189 1078 ARG C NE +6745 C CZ . ARG C 259 ? 2.7590 2.5701 2.3034 0.2133 0.0590 0.1134 1078 ARG C CZ +6746 N NH1 . ARG C 259 ? 2.4731 2.2855 2.0215 0.2155 0.0574 0.1113 1078 ARG C NH1 +6747 N NH2 . ARG C 259 ? 2.2612 2.0714 1.7999 0.2101 0.0617 0.1102 1078 ARG C NH2 +6748 N N . MET C 260 ? 2.5289 2.3570 2.1138 0.2218 0.0322 0.1227 1079 MET C N +6749 C CA . MET C 260 ? 2.5461 2.3753 2.1361 0.2249 0.0302 0.1218 1079 MET C CA +6750 C C . MET C 260 ? 2.6357 2.4681 2.2349 0.2276 0.0245 0.1258 1079 MET C C +6751 O O . MET C 260 ? 2.6279 2.4592 2.2290 0.2305 0.0248 0.1279 1079 MET C O +6752 C CB . MET C 260 ? 2.3801 2.2125 1.9730 0.2240 0.0278 0.1158 1079 MET C CB +6753 C CG . MET C 260 ? 2.0188 1.8483 1.6066 0.2246 0.0324 0.1122 1079 MET C CG +6754 S SD . MET C 260 ? 3.2580 3.0917 2.8505 0.2240 0.0288 0.1054 1079 MET C SD +6755 C CE . MET C 260 ? 1.3610 1.1955 0.9490 0.2195 0.0298 0.1019 1079 MET C CE +6756 N N . ILE C 261 ? 2.4587 2.2950 2.0639 0.2265 0.0192 0.1268 1080 ILE C N +6757 C CA . ILE C 261 ? 2.5310 2.3707 2.1455 0.2290 0.0133 0.1303 1080 ILE C CA +6758 C C . ILE C 261 ? 2.5796 2.4167 2.1926 0.2302 0.0149 0.1364 1080 ILE C C +6759 O O . ILE C 261 ? 2.7634 2.6010 2.3812 0.2331 0.0128 0.1396 1080 ILE C O +6760 C CB . ILE C 261 ? 2.2783 2.1235 1.9005 0.2276 0.0067 0.1291 1080 ILE C CB +6761 C CG1 . ILE C 261 ? 1.9379 1.7853 1.5599 0.2256 0.0059 0.1229 1080 ILE C CG1 +6762 C CG2 . ILE C 261 ? 2.3456 2.1948 1.9782 0.2304 0.0003 0.1315 1080 ILE C CG2 +6763 C CD1 . ILE C 261 ? 1.9569 1.8100 1.5874 0.2247 -0.0011 0.1214 1080 ILE C CD1 +6764 N N . ALA C 262 ? 2.1980 2.0325 1.8043 0.2279 0.0185 0.1380 1081 ALA C N +6765 C CA . ALA C 262 ? 2.2873 2.1186 1.8906 0.2288 0.0210 0.1436 1081 ALA C CA +6766 C C . ALA C 262 ? 2.6281 2.4554 2.2279 0.2315 0.0253 0.1450 1081 ALA C C +6767 O O . ALA C 262 ? 2.6073 2.4341 2.2101 0.2340 0.0243 0.1494 1081 ALA C O +6768 C CB . ALA C 262 ? 1.8157 1.6440 1.4107 0.2258 0.0255 0.1442 1081 ALA C CB +6769 N N . ALA C 263 ? 2.5696 2.3945 2.1634 0.2309 0.0298 0.1411 1082 ALA C N +6770 C CA . ALA C 263 ? 2.6365 2.4579 2.2273 0.2334 0.0336 0.1416 1082 ALA C CA +6771 C C . ALA C 263 ? 3.0045 2.8294 2.6039 0.2362 0.0288 0.1404 1082 ALA C C +6772 O O . ALA C 263 ? 2.8716 2.6973 2.4712 0.2362 0.0290 0.1359 1082 ALA C O +6773 C CB . ALA C 263 ? 2.4955 2.3132 2.0770 0.2317 0.0400 0.1377 1082 ALA C CB +6774 N N . VAL C 264 ? 3.2016 3.0285 2.8080 0.2385 0.0246 0.1446 1083 VAL C N +6775 C CA . VAL C 264 ? 3.2166 3.0463 2.8309 0.2415 0.0205 0.1444 1083 VAL C CA +6776 C C . VAL C 264 ? 2.8783 2.7079 2.4969 0.2443 0.0185 0.1503 1083 VAL C C +6777 O O . VAL C 264 ? 2.1545 1.9841 1.7735 0.2436 0.0175 0.1541 1083 VAL C O +6778 C CB . VAL C 264 ? 2.8484 2.6837 2.4710 0.2410 0.0140 0.1408 1083 VAL C CB +6779 C CG1 . VAL C 264 ? 2.5118 2.3511 2.1418 0.2408 0.0080 0.1439 1083 VAL C CG1 +6780 C CG2 . VAL C 264 ? 2.5750 2.4122 2.2030 0.2436 0.0115 0.1386 1083 VAL C CG2 +6781 N N . ASP C 265 ? 2.9669 2.7962 2.5885 0.2474 0.0181 0.1510 1084 ASP C N +6782 C CA . ASP C 265 ? 3.1244 2.9534 2.7499 0.2502 0.0166 0.1564 1084 ASP C CA +6783 C C . ASP C 265 ? 3.0988 2.9333 2.7355 0.2516 0.0087 0.1574 1084 ASP C C +6784 O O . ASP C 265 ? 2.5821 2.4194 2.2247 0.2532 0.0054 0.1551 1084 ASP C O +6785 C CB . ASP C 265 ? 3.1333 2.9592 2.7562 0.2530 0.0202 0.1569 1084 ASP C CB +6786 C CG . ASP C 265 ? 2.8995 2.7228 2.5218 0.2552 0.0216 0.1629 1084 ASP C CG +6787 O OD1 . ASP C 265 ? 2.8723 2.6980 2.5005 0.2558 0.0173 0.1666 1084 ASP C OD1 +6788 O OD2 . ASP C 265 ? 2.5351 2.3539 2.1510 0.2562 0.0272 0.1640 1084 ASP C OD2 +6789 N N . THR C 266 ? 3.3375 3.1735 2.9770 0.2508 0.0059 0.1609 1085 THR C N +6790 C CA . THR C 266 ? 3.5352 3.3767 3.1851 0.2514 -0.0016 0.1615 1085 THR C CA +6791 C C . THR C 266 ? 3.5579 3.3998 3.2126 0.2537 -0.0042 0.1675 1085 THR C C +6792 O O . THR C 266 ? 3.5950 3.4403 3.2558 0.2533 -0.0092 0.1694 1085 THR C O +6793 C CB . THR C 266 ? 3.5595 3.4035 3.2098 0.2481 -0.0039 0.1595 1085 THR C CB +6794 O OG1 . THR C 266 ? 3.5082 3.3523 3.1549 0.2461 -0.0021 0.1538 1085 THR C OG1 +6795 C CG2 . THR C 266 ? 3.5069 3.3566 3.1678 0.2486 -0.0117 0.1602 1085 THR C CG2 +6796 N N . ASP C 267 ? 3.4493 3.2877 3.1011 0.2560 -0.0007 0.1704 1086 ASP C N +6797 C CA . ASP C 267 ? 3.2792 3.1181 2.9360 0.2586 -0.0032 0.1759 1086 ASP C CA +6798 C C . ASP C 267 ? 3.1642 3.0071 2.8306 0.2612 -0.0088 0.1750 1086 ASP C C +6799 O O . ASP C 267 ? 2.7408 2.5868 2.4149 0.2626 -0.0140 0.1781 1086 ASP C O +6800 C CB . ASP C 267 ? 3.1855 3.0190 2.8355 0.2601 0.0027 0.1793 1086 ASP C CB +6801 C CG . ASP C 267 ? 3.2522 3.0813 2.8917 0.2575 0.0091 0.1792 1086 ASP C CG +6802 O OD1 . ASP C 267 ? 3.2992 3.1293 2.9371 0.2546 0.0085 0.1776 1086 ASP C OD1 +6803 O OD2 . ASP C 267 ? 3.2131 3.0375 2.8458 0.2584 0.0147 0.1807 1086 ASP C OD2 +6804 N N . SER C 268 ? 3.2848 3.1277 2.9505 0.2618 -0.0077 0.1708 1087 SER C N +6805 C CA . SER C 268 ? 3.1340 2.9809 2.8082 0.2638 -0.0128 0.1687 1087 SER C CA +6806 C C . SER C 268 ? 3.3645 3.2143 3.0399 0.2615 -0.0149 0.1630 1087 SER C C +6807 O O . SER C 268 ? 3.1474 2.9964 2.8199 0.2613 -0.0125 0.1588 1087 SER C O +6808 C CB . SER C 268 ? 2.5261 2.3705 2.1985 0.2665 -0.0097 0.1684 1087 SER C CB +6809 O OG . SER C 268 ? 2.2126 2.0608 1.8934 0.2686 -0.0148 0.1667 1087 SER C OG +6810 N N . PRO C 269 ? 3.4084 3.2618 3.0881 0.2596 -0.0193 0.1628 1088 PRO C N +6811 C CA . PRO C 269 ? 2.9968 2.8527 2.6766 0.2568 -0.0208 0.1578 1088 PRO C CA +6812 C C . PRO C 269 ? 2.9667 2.8269 2.6538 0.2578 -0.0255 0.1537 1088 PRO C C +6813 O O . PRO C 269 ? 2.8201 2.6806 2.5046 0.2561 -0.0243 0.1487 1088 PRO C O +6814 C CB . PRO C 269 ? 2.4771 2.3354 2.1600 0.2551 -0.0244 0.1601 1088 PRO C CB +6815 C CG . PRO C 269 ? 2.7081 2.5678 2.3975 0.2577 -0.0279 0.1653 1088 PRO C CG +6816 C CD . PRO C 269 ? 3.1761 3.0315 2.8613 0.2602 -0.0234 0.1676 1088 PRO C CD +6817 N N . ARG C 270 ? 2.9836 2.8468 2.6794 0.2604 -0.0307 0.1557 1089 ARG C N +6818 C CA . ARG C 270 ? 2.7347 2.6025 2.4386 0.2615 -0.0360 0.1523 1089 ARG C CA +6819 C C . ARG C 270 ? 2.7629 2.6295 2.4638 0.2618 -0.0332 0.1475 1089 ARG C C +6820 O O . ARG C 270 ? 1.9259 1.7955 1.6296 0.2607 -0.0357 0.1429 1089 ARG C O +6821 C CB . ARG C 270 ? 2.3208 2.1912 2.0336 0.2647 -0.0408 0.1560 1089 ARG C CB +6822 C CG . ARG C 270 ? 2.5191 2.3922 2.2381 0.2668 -0.0440 0.1531 1089 ARG C CG +6823 C CD . ARG C 270 ? 2.4985 2.3743 2.2266 0.2698 -0.0493 0.1568 1089 ARG C CD +6824 N NE . ARG C 270 ? 2.6373 2.5150 2.3703 0.2722 -0.0514 0.1543 1089 ARG C NE +6825 C CZ . ARG C 270 ? 2.6047 2.4867 2.3439 0.2719 -0.0559 0.1503 1089 ARG C CZ +6826 N NH1 . ARG C 270 ? 2.6655 2.5504 2.4066 0.2693 -0.0589 0.1482 1089 ARG C NH1 +6827 N NH2 . ARG C 270 ? 2.1850 2.0684 1.9283 0.2742 -0.0576 0.1484 1089 ARG C NH2 +6828 N N . GLU C 271 ? 3.0710 2.9333 2.7662 0.2634 -0.0280 0.1487 1090 GLU C N +6829 C CA . GLU C 271 ? 3.0021 2.8628 2.6936 0.2638 -0.0247 0.1444 1090 GLU C CA +6830 C C . GLU C 271 ? 2.9547 2.8138 2.6388 0.2605 -0.0209 0.1402 1090 GLU C C +6831 O O . GLU C 271 ? 2.5766 2.4371 2.2611 0.2597 -0.0214 0.1352 1090 GLU C O +6832 C CB . GLU C 271 ? 3.0505 2.9066 2.7368 0.2660 -0.0195 0.1469 1090 GLU C CB +6833 C CG . GLU C 271 ? 3.1578 3.0142 2.8493 0.2691 -0.0219 0.1522 1090 GLU C CG +6834 C CD . GLU C 271 ? 3.1966 3.0478 2.8815 0.2708 -0.0160 0.1552 1090 GLU C CD +6835 O OE1 . GLU C 271 ? 3.0673 2.9150 2.7446 0.2701 -0.0105 0.1525 1090 GLU C OE1 +6836 O OE2 . GLU C 271 ? 3.1750 3.0256 2.8622 0.2728 -0.0167 0.1601 1090 GLU C OE2 +6837 N N . VAL C 272 ? 3.1502 3.0062 2.8275 0.2584 -0.0171 0.1423 1091 VAL C N +6838 C CA . VAL C 272 ? 3.0936 2.9474 2.7627 0.2552 -0.0127 0.1389 1091 VAL C CA +6839 C C . VAL C 272 ? 3.0387 2.8967 2.7116 0.2530 -0.0167 0.1343 1091 VAL C C +6840 O O . VAL C 272 ? 2.9597 2.8172 2.6287 0.2515 -0.0144 0.1296 1091 VAL C O +6841 C CB . VAL C 272 ? 2.4369 2.2874 2.0994 0.2534 -0.0090 0.1425 1091 VAL C CB +6842 C CG1 . VAL C 272 ? 2.3442 2.1918 1.9974 0.2504 -0.0036 0.1390 1091 VAL C CG1 +6843 C CG2 . VAL C 272 ? 2.2879 2.1346 1.9475 0.2558 -0.0056 0.1475 1091 VAL C CG2 +6844 N N . PHE C 273 ? 3.0427 2.9051 2.7235 0.2528 -0.0228 0.1358 1092 PHE C N +6845 C CA . PHE C 273 ? 2.9535 2.8203 2.6388 0.2509 -0.0273 0.1317 1092 PHE C CA +6846 C C . PHE C 273 ? 2.7008 2.5701 2.3907 0.2522 -0.0297 0.1274 1092 PHE C C +6847 O O . PHE C 273 ? 2.6681 2.5378 2.3555 0.2504 -0.0287 0.1225 1092 PHE C O +6848 C CB . PHE C 273 ? 3.1304 3.0013 2.8237 0.2508 -0.0335 0.1346 1092 PHE C CB +6849 C CG . PHE C 273 ? 3.1677 3.0436 2.8670 0.2493 -0.0389 0.1308 1092 PHE C CG +6850 C CD1 . PHE C 273 ? 3.0369 2.9131 2.7322 0.2459 -0.0378 0.1278 1092 PHE C CD1 +6851 C CD2 . PHE C 273 ? 3.1109 2.9914 2.8201 0.2512 -0.0451 0.1302 1092 PHE C CD2 +6852 C CE1 . PHE C 273 ? 2.8049 2.6858 2.5058 0.2445 -0.0427 0.1242 1092 PHE C CE1 +6853 C CE2 . PHE C 273 ? 2.9519 2.8370 2.6667 0.2498 -0.0501 0.1267 1092 PHE C CE2 +6854 C CZ . PHE C 273 ? 2.7545 2.6398 2.4652 0.2464 -0.0489 0.1237 1092 PHE C CZ +6855 N N . PHE C 274 ? 2.3582 2.2289 2.0545 0.2554 -0.0328 0.1294 1093 PHE C N +6856 C CA . PHE C 274 ? 2.6775 2.5510 2.3793 0.2570 -0.0358 0.1258 1093 PHE C CA +6857 C C . PHE C 274 ? 2.8635 2.7341 2.5586 0.2566 -0.0306 0.1215 1093 PHE C C +6858 O O . PHE C 274 ? 2.7764 2.6494 2.4737 0.2560 -0.0325 0.1167 1093 PHE C O +6859 C CB . PHE C 274 ? 3.0020 2.8768 2.7108 0.2606 -0.0389 0.1292 1093 PHE C CB +6860 C CG . PHE C 274 ? 3.1595 3.0369 2.8739 0.2625 -0.0418 0.1257 1093 PHE C CG +6861 C CD1 . PHE C 274 ? 2.7863 2.6691 2.5093 0.2623 -0.0483 0.1234 1093 PHE C CD1 +6862 C CD2 . PHE C 274 ? 3.0423 2.9168 2.7533 0.2644 -0.0381 0.1249 1093 PHE C CD2 +6863 C CE1 . PHE C 274 ? 2.6605 2.5457 2.3885 0.2640 -0.0510 0.1202 1093 PHE C CE1 +6864 C CE2 . PHE C 274 ? 2.4584 2.3354 2.1745 0.2662 -0.0407 0.1217 1093 PHE C CE2 +6865 C CZ . PHE C 274 ? 2.4303 2.3126 2.1549 0.2659 -0.0472 0.1194 1093 PHE C CZ +6866 N N . ARG C 275 ? 2.8935 2.7589 2.5805 0.2571 -0.0243 0.1232 1094 ARG C N +6867 C CA . ARG C 275 ? 2.7731 2.6354 2.4534 0.2569 -0.0191 0.1195 1094 ARG C CA +6868 C C . ARG C 275 ? 2.6021 2.4640 2.2768 0.2533 -0.0168 0.1152 1094 ARG C C +6869 O O . ARG C 275 ? 2.5951 2.4574 2.2686 0.2528 -0.0160 0.1103 1094 ARG C O +6870 C CB . ARG C 275 ? 2.8937 2.7505 2.5666 0.2583 -0.0128 0.1226 1094 ARG C CB +6871 C CG . ARG C 275 ? 2.8586 2.7133 2.5290 0.2601 -0.0096 0.1201 1094 ARG C CG +6872 C CD . ARG C 275 ? 2.8223 2.6712 2.4840 0.2609 -0.0026 0.1228 1094 ARG C CD +6873 N NE . ARG C 275 ? 2.8758 2.7232 2.5370 0.2613 -0.0024 0.1286 1094 ARG C NE +6874 C CZ . ARG C 275 ? 2.5934 2.4410 2.2590 0.2642 -0.0041 0.1329 1094 ARG C CZ +6875 N NH1 . ARG C 275 ? 1.9516 1.8006 1.6222 0.2670 -0.0063 0.1322 1094 ARG C NH1 +6876 N NH2 . ARG C 275 ? 2.2975 2.1438 1.9623 0.2643 -0.0038 0.1380 1094 ARG C NH2 +6877 N N . VAL C 276 ? 2.3852 2.2462 2.0565 0.2510 -0.0157 0.1170 1095 VAL C N +6878 C CA . VAL C 276 ? 2.3328 2.1936 1.9990 0.2475 -0.0138 0.1133 1095 VAL C CA +6879 C C . VAL C 276 ? 2.3200 2.1862 1.9936 0.2465 -0.0198 0.1094 1095 VAL C C +6880 O O . VAL C 276 ? 2.1511 2.0177 1.8218 0.2444 -0.0186 0.1046 1095 VAL C O +6881 C CB . VAL C 276 ? 2.4301 2.2892 2.0920 0.2453 -0.0120 0.1165 1095 VAL C CB +6882 C CG1 . VAL C 276 ? 2.0885 1.9486 1.7472 0.2417 -0.0116 0.1126 1095 VAL C CG1 +6883 C CG2 . VAL C 276 ? 2.8537 2.7070 2.5068 0.2458 -0.0052 0.1195 1095 VAL C CG2 +6884 N N . ALA C 277 ? 2.4607 2.3311 2.1437 0.2480 -0.0261 0.1115 1096 ALA C N +6885 C CA . ALA C 277 ? 2.1265 2.0022 1.8175 0.2475 -0.0324 0.1082 1096 ALA C CA +6886 C C . ALA C 277 ? 2.0610 1.9374 1.7533 0.2488 -0.0323 0.1038 1096 ALA C C +6887 O O . ALA C 277 ? 1.9065 1.7848 1.5988 0.2470 -0.0332 0.0989 1096 ALA C O +6888 C CB . ALA C 277 ? 1.7041 1.5837 1.4048 0.2494 -0.0389 0.1118 1096 ALA C CB +6889 N N . ALA C 278 ? 2.1624 2.0372 1.8555 0.2518 -0.0313 0.1055 1097 ALA C N +6890 C CA . ALA C 278 ? 2.0324 1.9077 1.7269 0.2533 -0.0311 0.1018 1097 ALA C CA +6891 C C . ALA C 278 ? 1.9255 1.7968 1.6105 0.2518 -0.0247 0.0980 1097 ALA C C +6892 O O . ALA C 278 ? 1.8252 1.6975 1.5109 0.2521 -0.0247 0.0936 1097 ALA C O +6893 C CB . ALA C 278 ? 1.7848 1.6595 1.4829 0.2570 -0.0318 0.1049 1097 ALA C CB +6894 N N . ASP C 279 ? 1.8579 1.7250 1.5343 0.2503 -0.0191 0.0997 1098 ASP C N +6895 C CA . ASP C 279 ? 1.9094 1.7728 1.5766 0.2485 -0.0129 0.0961 1098 ASP C CA +6896 C C . ASP C 279 ? 2.3176 2.1831 1.9839 0.2452 -0.0140 0.0916 1098 ASP C C +6897 O O . ASP C 279 ? 1.9806 1.8454 1.6433 0.2442 -0.0116 0.0869 1098 ASP C O +6898 C CB . ASP C 279 ? 2.0804 1.9383 1.7384 0.2480 -0.0064 0.0995 1098 ASP C CB +6899 C CG . ASP C 279 ? 2.3237 2.1772 1.9730 0.2477 0.0003 0.0967 1098 ASP C CG +6900 O OD1 . ASP C 279 ? 2.1084 1.9608 1.7519 0.2449 0.0031 0.0931 1098 ASP C OD1 +6901 O OD2 . ASP C 279 ? 2.4557 2.3068 2.1038 0.2503 0.0027 0.0981 1098 ASP C OD2 +6902 N N . MET C 280 ? 2.4866 2.3549 2.1564 0.2436 -0.0177 0.0929 1099 MET C N +6903 C CA . MET C 280 ? 2.3148 2.1857 1.9848 0.2405 -0.0196 0.0889 1099 MET C CA +6904 C C . MET C 280 ? 2.0502 1.9253 1.7270 0.2411 -0.0241 0.0844 1099 MET C C +6905 O O . MET C 280 ? 1.9931 1.8693 1.6682 0.2389 -0.0238 0.0796 1099 MET C O +6906 C CB . MET C 280 ? 2.5051 2.3787 2.1790 0.2391 -0.0236 0.0916 1099 MET C CB +6907 C CG . MET C 280 ? 2.7343 2.6043 2.4004 0.2370 -0.0191 0.0943 1099 MET C CG +6908 S SD . MET C 280 ? 2.5363 2.4100 2.2071 0.2350 -0.0241 0.0965 1099 MET C SD +6909 C CE . MET C 280 ? 1.7951 1.6734 1.4700 0.2328 -0.0282 0.0901 1099 MET C CE +6910 N N . PHE C 281 ? 1.9209 1.7983 1.6052 0.2442 -0.0281 0.0859 1100 PHE C N +6911 C CA . PHE C 281 ? 1.9490 1.8308 1.6408 0.2449 -0.0332 0.0821 1100 PHE C CA +6912 C C . PHE C 281 ? 2.1808 2.0614 1.8727 0.2475 -0.0315 0.0804 1100 PHE C C +6913 O O . PHE C 281 ? 1.9735 1.8575 1.6731 0.2494 -0.0362 0.0794 1100 PHE C O +6914 C CB . PHE C 281 ? 1.7293 1.6158 1.4314 0.2462 -0.0404 0.0848 1100 PHE C CB +6915 C CG . PHE C 281 ? 2.0448 1.9335 1.7480 0.2435 -0.0429 0.0855 1100 PHE C CG +6916 C CD1 . PHE C 281 ? 2.1933 2.0826 1.8931 0.2404 -0.0420 0.0814 1100 PHE C CD1 +6917 C CD2 . PHE C 281 ? 1.6901 1.5801 1.3977 0.2442 -0.0461 0.0905 1100 PHE C CD2 +6918 C CE1 . PHE C 281 ? 2.1465 2.0378 1.8473 0.2380 -0.0443 0.0820 1100 PHE C CE1 +6919 C CE2 . PHE C 281 ? 1.6960 1.5880 1.4046 0.2418 -0.0484 0.0911 1100 PHE C CE2 +6920 C CZ . PHE C 281 ? 1.9426 1.8352 1.6478 0.2387 -0.0475 0.0869 1100 PHE C CZ +6921 N N . SER C 282 ? 2.5319 2.4075 2.2149 0.2474 -0.0248 0.0800 1101 SER C N +6922 C CA . SER C 282 ? 2.7650 2.6389 2.4467 0.2495 -0.0224 0.0781 1101 SER C CA +6923 C C . SER C 282 ? 2.7472 2.6226 2.4282 0.2480 -0.0224 0.0718 1101 SER C C +6924 O O . SER C 282 ? 2.2026 2.0786 1.8860 0.2498 -0.0230 0.0693 1101 SER C O +6925 C CB . SER C 282 ? 2.8250 2.6930 2.4974 0.2500 -0.0151 0.0802 1101 SER C CB +6926 O OG . SER C 282 ? 2.6867 2.5517 2.3503 0.2469 -0.0102 0.0781 1101 SER C OG +6927 N N . ASP C 283 ? 2.8561 2.7318 2.5336 0.2447 -0.0216 0.0693 1102 ASP C N +6928 C CA . ASP C 283 ? 2.4108 2.2883 2.0882 0.2430 -0.0222 0.0633 1102 ASP C CA +6929 C C . ASP C 283 ? 2.0385 1.9220 1.7258 0.2428 -0.0298 0.0618 1102 ASP C C +6930 O O . ASP C 283 ? 1.5744 1.4605 1.2638 0.2419 -0.0317 0.0570 1102 ASP C O +6931 C CB . ASP C 283 ? 2.2693 2.1442 1.9378 0.2395 -0.0174 0.0609 1102 ASP C CB +6932 C CG . ASP C 283 ? 2.3941 2.2698 2.0624 0.2373 -0.0187 0.0635 1102 ASP C CG +6933 O OD1 . ASP C 283 ? 2.6587 2.5352 2.3310 0.2386 -0.0213 0.0683 1102 ASP C OD1 +6934 O OD2 . ASP C 283 ? 1.8628 1.7383 1.5268 0.2342 -0.0172 0.0607 1102 ASP C OD2 +6935 N N . GLY C 284 ? 1.9682 1.8540 1.6616 0.2438 -0.0341 0.0661 1103 GLY C N +6936 C CA . GLY C 284 ? 2.0159 1.9074 1.7197 0.2444 -0.0417 0.0657 1103 GLY C CA +6937 C C . GLY C 284 ? 2.3612 2.2560 2.0665 0.2414 -0.0445 0.0617 1103 GLY C C +6938 O O . GLY C 284 ? 1.5419 1.4412 1.2548 0.2418 -0.0499 0.0592 1103 GLY C O +6939 N N . ASN C 285 ? 2.9086 2.8011 2.6066 0.2385 -0.0406 0.0610 1104 ASN C N +6940 C CA . ASN C 285 ? 2.5867 2.4819 2.2851 0.2354 -0.0426 0.0575 1104 ASN C CA +6941 C C . ASN C 285 ? 1.9431 1.8398 1.6435 0.2340 -0.0453 0.0610 1104 ASN C C +6942 O O . ASN C 285 ? 1.9808 1.8749 1.6744 0.2317 -0.0416 0.0617 1104 ASN C O +6943 C CB . ASN C 285 ? 2.3622 2.2539 2.0508 0.2328 -0.0365 0.0538 1104 ASN C CB +6944 C CG . ASN C 285 ? 2.4608 2.3510 2.1471 0.2340 -0.0338 0.0500 1104 ASN C CG +6945 O OD1 . ASN C 285 ? 2.2224 2.1151 1.9153 0.2362 -0.0374 0.0489 1104 ASN C OD1 +6946 N ND2 . ASN C 285 ? 2.0947 1.9807 1.7716 0.2325 -0.0273 0.0479 1104 ASN C ND2 +6947 N N . PHE C 286 ? 1.7764 1.6773 1.4862 0.2354 -0.0517 0.0631 1105 PHE C N +6948 C CA . PHE C 286 ? 2.0750 1.9780 1.7883 0.2345 -0.0551 0.0666 1105 PHE C CA +6949 C C . PHE C 286 ? 2.6385 2.5439 2.3515 0.2311 -0.0568 0.0635 1105 PHE C C +6950 O O . PHE C 286 ? 2.7415 2.6500 2.4577 0.2303 -0.0595 0.0589 1105 PHE C O +6951 C CB . PHE C 286 ? 1.9351 1.8424 1.6592 0.2370 -0.0619 0.0691 1105 PHE C CB +6952 C CG . PHE C 286 ? 2.5493 2.4547 2.2749 0.2404 -0.0612 0.0729 1105 PHE C CG +6953 C CD1 . PHE C 286 ? 2.9820 2.8850 2.7057 0.2412 -0.0596 0.0784 1105 PHE C CD1 +6954 C CD2 . PHE C 286 ? 2.1677 2.0740 1.8970 0.2429 -0.0624 0.0711 1105 PHE C CD2 +6955 C CE1 . PHE C 286 ? 2.9741 2.8755 2.6994 0.2444 -0.0590 0.0820 1105 PHE C CE1 +6956 C CE2 . PHE C 286 ? 1.6926 1.5973 1.4236 0.2461 -0.0619 0.0746 1105 PHE C CE2 +6957 C CZ . PHE C 286 ? 2.3598 2.2620 2.0887 0.2468 -0.0602 0.0801 1105 PHE C CZ +6958 N N . ASN C 287 ? 2.7730 2.6772 2.4822 0.2291 -0.0553 0.0660 1106 ASN C N +6959 C CA . ASN C 287 ? 2.3642 2.2711 2.0742 0.2261 -0.0578 0.0641 1106 ASN C CA +6960 C C . ASN C 287 ? 2.1887 2.0955 1.8991 0.2255 -0.0588 0.0691 1106 ASN C C +6961 O O . ASN C 287 ? 1.9777 1.8809 1.6842 0.2266 -0.0553 0.0733 1106 ASN C O +6962 C CB . ASN C 287 ? 2.2021 2.1066 1.9036 0.2231 -0.0528 0.0598 1106 ASN C CB +6963 C CG . ASN C 287 ? 2.1298 2.0283 1.8214 0.2232 -0.0452 0.0611 1106 ASN C CG +6964 O OD1 . ASN C 287 ? 2.0551 1.9509 1.7428 0.2230 -0.0427 0.0653 1106 ASN C OD1 +6965 N ND2 . ASN C 287 ? 1.8245 1.7209 1.5118 0.2234 -0.0416 0.0575 1106 ASN C ND2 +6966 N N . TRP C 288 ? 2.1538 2.0646 1.8691 0.2239 -0.0635 0.0688 1107 TRP C N +6967 C CA . TRP C 288 ? 1.5960 1.5073 1.3127 0.2233 -0.0652 0.0735 1107 TRP C CA +6968 C C . TRP C 288 ? 1.8701 1.7764 1.5772 0.2218 -0.0590 0.0760 1107 TRP C C +6969 O O . TRP C 288 ? 1.6835 1.5888 1.3907 0.2224 -0.0590 0.0809 1107 TRP C O +6970 C CB . TRP C 288 ? 1.7281 1.6441 1.4500 0.2212 -0.0704 0.0718 1107 TRP C CB +6971 C CG . TRP C 288 ? 2.3409 2.2612 2.0730 0.2230 -0.0773 0.0744 1107 TRP C CG +6972 C CD1 . TRP C 288 ? 2.7203 2.6454 2.4609 0.2238 -0.0831 0.0719 1107 TRP C CD1 +6973 C CD2 . TRP C 288 ? 2.5498 2.4701 2.2849 0.2244 -0.0790 0.0802 1107 TRP C CD2 +6974 N NE1 . TRP C 288 ? 3.0067 2.9348 2.7555 0.2255 -0.0885 0.0757 1107 TRP C NE1 +6975 C CE2 . TRP C 288 ? 2.9259 2.8511 2.6714 0.2259 -0.0860 0.0809 1107 TRP C CE2 +6976 C CE3 . TRP C 288 ? 2.2749 2.1914 2.0048 0.2245 -0.0752 0.0849 1107 TRP C CE3 +6977 C CZ2 . TRP C 288 ? 2.6393 2.5658 2.3902 0.2275 -0.0894 0.0860 1107 TRP C CZ2 +6978 C CZ3 . TRP C 288 ? 2.0089 1.9267 1.7441 0.2260 -0.0786 0.0900 1107 TRP C CZ3 +6979 C CH2 . TRP C 288 ? 2.0100 1.9327 1.7555 0.2276 -0.0856 0.0905 1107 TRP C CH2 +6980 N N . GLY C 289 ? 1.7719 1.6751 1.4706 0.2199 -0.0536 0.0726 1108 GLY C N +6981 C CA . GLY C 289 ? 1.9159 1.8142 1.6051 0.2185 -0.0472 0.0745 1108 GLY C CA +6982 C C . GLY C 289 ? 2.2183 2.1129 1.9052 0.2211 -0.0441 0.0792 1108 GLY C C +6983 O O . GLY C 289 ? 2.0791 1.9712 1.7623 0.2206 -0.0418 0.0833 1108 GLY C O +6984 N N . ARG C 290 ? 2.1766 2.0708 1.8658 0.2237 -0.0441 0.0786 1109 ARG C N +6985 C CA . ARG C 290 ? 1.7889 1.6797 1.4762 0.2264 -0.0413 0.0828 1109 ARG C CA +6986 C C . ARG C 290 ? 1.8323 1.7253 1.5272 0.2286 -0.0461 0.0878 1109 ARG C C +6987 O O . ARG C 290 ? 1.6178 1.5079 1.3103 0.2298 -0.0438 0.0925 1109 ARG C O +6988 C CB . ARG C 290 ? 1.4372 1.3269 1.1246 0.2286 -0.0398 0.0803 1109 ARG C CB +6989 C CG . ARG C 290 ? 1.8716 1.7577 1.5501 0.2271 -0.0336 0.0764 1109 ARG C CG +6990 C CD . ARG C 290 ? 2.0199 1.9046 1.6984 0.2297 -0.0320 0.0749 1109 ARG C CD +6991 N NE . ARG C 290 ? 2.1988 2.0802 1.8691 0.2283 -0.0263 0.0709 1109 ARG C NE +6992 C CZ . ARG C 290 ? 2.3791 2.2592 2.0484 0.2300 -0.0243 0.0685 1109 ARG C CZ +6993 N NH1 . ARG C 290 ? 2.5274 2.4091 2.2033 0.2331 -0.0276 0.0699 1109 ARG C NH1 +6994 N NH2 . ARG C 290 ? 2.2126 2.0897 1.8743 0.2286 -0.0191 0.0649 1109 ARG C NH2 +6995 N N . VAL C 291 ? 1.8544 1.7527 1.5586 0.2290 -0.0528 0.0868 1110 VAL C N +6996 C CA . VAL C 291 ? 1.6761 1.5772 1.3883 0.2308 -0.0580 0.0912 1110 VAL C CA +6997 C C . VAL C 291 ? 1.6185 1.5184 1.3277 0.2291 -0.0570 0.0951 1110 VAL C C +6998 O O . VAL C 291 ? 1.7336 1.6328 1.4447 0.2307 -0.0578 0.1001 1110 VAL C O +6999 C CB . VAL C 291 ? 2.1264 2.0334 1.8482 0.2307 -0.0653 0.0888 1110 VAL C CB +7000 C CG1 . VAL C 291 ? 2.0395 1.9496 1.7698 0.2325 -0.0709 0.0934 1110 VAL C CG1 +7001 C CG2 . VAL C 291 ? 1.7425 1.6509 1.4672 0.2322 -0.0664 0.0846 1110 VAL C CG2 +7002 N N . VAL C 292 ? 1.7038 1.6034 1.4081 0.2259 -0.0552 0.0926 1111 VAL C N +7003 C CA . VAL C 292 ? 1.9112 1.8097 1.6121 0.2239 -0.0541 0.0957 1111 VAL C CA +7004 C C . VAL C 292 ? 1.9145 1.8070 1.6058 0.2238 -0.0469 0.0982 1111 VAL C C +7005 O O . VAL C 292 ? 1.9089 1.7999 1.5993 0.2242 -0.0462 0.1031 1111 VAL C O +7006 C CB . VAL C 292 ? 1.7163 1.6170 1.4161 0.2204 -0.0552 0.0920 1111 VAL C CB +7007 C CG1 . VAL C 292 ? 1.1826 1.0817 0.8781 0.2184 -0.0534 0.0951 1111 VAL C CG1 +7008 C CG2 . VAL C 292 ? 1.9773 1.8838 1.6869 0.2206 -0.0626 0.0903 1111 VAL C CG2 +7009 N N . ALA C 293 ? 1.8019 1.6911 1.4860 0.2232 -0.0416 0.0950 1112 ALA C N +7010 C CA . ALA C 293 ? 1.8220 1.7055 1.4967 0.2231 -0.0345 0.0971 1112 ALA C CA +7011 C C . ALA C 293 ? 1.9848 1.8663 1.6611 0.2265 -0.0339 0.1018 1112 ALA C C +7012 O O . ALA C 293 ? 1.7778 1.6553 1.4483 0.2266 -0.0296 0.1054 1112 ALA C O +7013 C CB . ALA C 293 ? 1.5777 1.4583 1.2450 0.2220 -0.0292 0.0925 1112 ALA C CB +7014 N N . LEU C 294 ? 2.1511 2.0354 1.8352 0.2291 -0.0383 0.1018 1113 LEU C N +7015 C CA . LEU C 294 ? 1.9774 1.8605 1.6640 0.2323 -0.0384 0.1064 1113 LEU C CA +7016 C C . LEU C 294 ? 1.8654 1.7510 1.5583 0.2328 -0.0431 0.1110 1113 LEU C C +7017 O O . LEU C 294 ? 1.9811 1.8650 1.6745 0.2349 -0.0426 0.1158 1113 LEU C O +7018 C CB . LEU C 294 ? 1.7122 1.5968 1.4041 0.2350 -0.0407 0.1044 1113 LEU C CB +7019 C CG . LEU C 294 ? 1.9350 1.8183 1.6295 0.2385 -0.0407 0.1086 1113 LEU C CG +7020 C CD1 . LEU C 294 ? 1.8356 1.7172 1.5284 0.2402 -0.0382 0.1057 1113 LEU C CD1 +7021 C CD2 . LEU C 294 ? 2.2891 2.1772 1.9945 0.2402 -0.0480 0.1108 1113 LEU C CD2 +7022 N N . PHE C 295 ? 1.5510 1.4407 1.2484 0.2310 -0.0477 0.1097 1114 PHE C N +7023 C CA . PHE C 295 ? 1.9219 1.8141 1.6249 0.2312 -0.0522 0.1139 1114 PHE C CA +7024 C C . PHE C 295 ? 2.1544 2.0437 1.8507 0.2289 -0.0486 0.1165 1114 PHE C C +7025 O O . PHE C 295 ? 2.2519 2.1424 1.9513 0.2289 -0.0512 0.1204 1114 PHE C O +7026 C CB . PHE C 295 ? 2.0363 1.9343 1.7479 0.2304 -0.0591 0.1114 1114 PHE C CB +7027 C CG . PHE C 295 ? 2.2828 2.1840 2.0023 0.2314 -0.0646 0.1158 1114 PHE C CG +7028 C CD1 . PHE C 295 ? 2.3509 2.2537 2.0775 0.2347 -0.0682 0.1183 1114 PHE C CD1 +7029 C CD2 . PHE C 295 ? 1.9969 1.8995 1.7165 0.2292 -0.0663 0.1172 1114 PHE C CD2 +7030 C CE1 . PHE C 295 ? 2.4041 2.3099 2.1380 0.2357 -0.0733 0.1223 1114 PHE C CE1 +7031 C CE2 . PHE C 295 ? 2.1794 2.0849 1.9063 0.2302 -0.0714 0.1211 1114 PHE C CE2 +7032 C CZ . PHE C 295 ? 2.4759 2.3830 2.2098 0.2334 -0.0749 0.1237 1114 PHE C CZ +7033 N N . TYR C 296 ? 2.2242 2.1097 1.9110 0.2269 -0.0425 0.1142 1115 TYR C N +7034 C CA . TYR C 296 ? 2.2521 2.1340 1.9310 0.2250 -0.0379 0.1167 1115 TYR C CA +7035 C C . TYR C 296 ? 2.3129 2.1901 1.9874 0.2272 -0.0333 0.1205 1115 TYR C C +7036 O O . TYR C 296 ? 1.9302 1.8048 1.6011 0.2270 -0.0309 0.1247 1115 TYR C O +7037 C CB . TYR C 296 ? 2.2130 2.0931 1.8841 0.2218 -0.0337 0.1120 1115 TYR C CB +7038 C CG . TYR C 296 ? 2.3873 2.2632 2.0490 0.2194 -0.0280 0.1136 1115 TYR C CG +7039 C CD1 . TYR C 296 ? 2.6756 2.5529 2.3374 0.2172 -0.0295 0.1153 1115 TYR C CD1 +7040 C CD2 . TYR C 296 ? 2.2617 2.1325 1.9145 0.2194 -0.0210 0.1135 1115 TYR C CD2 +7041 C CE1 . TYR C 296 ? 2.7166 2.5900 2.3697 0.2151 -0.0243 0.1167 1115 TYR C CE1 +7042 C CE2 . TYR C 296 ? 2.1468 2.0136 1.7909 0.2174 -0.0158 0.1149 1115 TYR C CE2 +7043 C CZ . TYR C 296 ? 2.1573 2.0255 1.8016 0.2152 -0.0174 0.1165 1115 TYR C CZ +7044 O OH . TYR C 296 ? 1.9044 1.7686 1.5400 0.2132 -0.0121 0.1179 1115 TYR C OH +7045 N N . PHE C 297 ? 2.3946 2.2708 2.0694 0.2293 -0.0321 0.1189 1116 PHE C N +7046 C CA . PHE C 297 ? 2.2218 2.0940 1.8931 0.2317 -0.0281 0.1223 1116 PHE C CA +7047 C C . PHE C 297 ? 1.9989 1.8728 1.6774 0.2343 -0.0323 0.1275 1116 PHE C C +7048 O O . PHE C 297 ? 1.6692 1.5408 1.3450 0.2343 -0.0305 0.1321 1116 PHE C O +7049 C CB . PHE C 297 ? 2.3313 2.2021 2.0013 0.2333 -0.0259 0.1190 1116 PHE C CB +7050 C CG . PHE C 297 ? 2.6708 2.5366 2.3348 0.2351 -0.0202 0.1217 1116 PHE C CG +7051 C CD1 . PHE C 297 ? 2.4644 2.3254 2.1181 0.2334 -0.0134 0.1214 1116 PHE C CD1 +7052 C CD2 . PHE C 297 ? 2.9739 2.8397 2.6423 0.2385 -0.0217 0.1245 1116 PHE C CD2 +7053 C CE1 . PHE C 297 ? 2.6719 2.5282 2.3199 0.2350 -0.0082 0.1239 1116 PHE C CE1 +7054 C CE2 . PHE C 297 ? 2.8884 2.7496 2.5512 0.2402 -0.0165 0.1270 1116 PHE C CE2 +7055 C CZ . PHE C 297 ? 2.8569 2.7132 2.5094 0.2384 -0.0097 0.1267 1116 PHE C CZ +7056 N N . ALA C 298 ? 1.9324 1.8104 1.6200 0.2363 -0.0379 0.1269 1117 ALA C N +7057 C CA . ALA C 298 ? 2.1210 2.0013 1.8165 0.2386 -0.0427 0.1315 1117 ALA C CA +7058 C C . ALA C 298 ? 2.5347 2.4160 2.2311 0.2370 -0.0447 0.1349 1117 ALA C C +7059 O O . ALA C 298 ? 2.3842 2.2655 2.0836 0.2386 -0.0462 0.1398 1117 ALA C O +7060 C CB . ALA C 298 ? 2.0469 1.9322 1.7523 0.2402 -0.0491 0.1293 1117 ALA C CB +7061 N N . SER C 299 ? 2.6854 2.5678 2.3793 0.2338 -0.0446 0.1321 1118 SER C N +7062 C CA . SER C 299 ? 2.5126 2.3952 2.2053 0.2318 -0.0451 0.1349 1118 SER C CA +7063 C C . SER C 299 ? 2.3528 2.2300 2.0374 0.2320 -0.0390 0.1388 1118 SER C C +7064 O O . SER C 299 ? 2.4003 2.2770 2.0870 0.2334 -0.0401 0.1439 1118 SER C O +7065 C CB . SER C 299 ? 2.4368 2.3207 2.1266 0.2283 -0.0449 0.1306 1118 SER C CB +7066 O OG . SER C 299 ? 2.3376 2.2227 2.0280 0.2264 -0.0467 0.1330 1118 SER C OG +7067 N N . LYS C 300 ? 2.0946 1.9676 1.7699 0.2306 -0.0327 0.1365 1119 LYS C N +7068 C CA . LYS C 300 ? 2.1788 2.0465 1.8454 0.2304 -0.0264 0.1398 1119 LYS C CA +7069 C C . LYS C 300 ? 2.6448 2.5103 2.3126 0.2337 -0.0254 0.1444 1119 LYS C C +7070 O O . LYS C 300 ? 2.5708 2.4323 2.2327 0.2337 -0.0211 0.1480 1119 LYS C O +7071 C CB . LYS C 300 ? 2.0926 1.9564 1.7496 0.2286 -0.0200 0.1360 1119 LYS C CB +7072 C CG . LYS C 300 ? 1.9869 1.8514 1.6399 0.2249 -0.0190 0.1326 1119 LYS C CG +7073 C CD . LYS C 300 ? 1.6027 1.4645 1.2499 0.2230 -0.0160 0.1360 1119 LYS C CD +7074 C CE . LYS C 300 ? 1.8693 1.7301 1.5097 0.2194 -0.0128 0.1321 1119 LYS C CE +7075 N NZ . LYS C 300 ? 2.1444 2.0046 1.7818 0.2172 -0.0121 0.1349 1119 LYS C NZ +7076 N N . LEU C 301 ? 2.8983 2.7663 2.5734 0.2364 -0.0293 0.1442 1120 LEU C N +7077 C CA . LEU C 301 ? 2.5306 2.3972 2.2080 0.2397 -0.0293 0.1486 1120 LEU C CA +7078 C C . LEU C 301 ? 2.4675 2.3366 2.1515 0.2405 -0.0340 0.1534 1120 LEU C C +7079 O O . LEU C 301 ? 2.0401 1.9122 1.7325 0.2429 -0.0389 0.1548 1120 LEU C O +7080 C CB . LEU C 301 ? 2.0929 1.9612 1.7755 0.2423 -0.0315 0.1463 1120 LEU C CB +7081 C CG . LEU C 301 ? 2.3724 2.2380 2.0486 0.2417 -0.0266 0.1418 1120 LEU C CG +7082 C CD1 . LEU C 301 ? 2.3355 2.2029 2.0170 0.2443 -0.0289 0.1396 1120 LEU C CD1 +7083 C CD2 . LEU C 301 ? 2.2587 2.1183 1.9248 0.2415 -0.0192 0.1438 1120 LEU C CD2 +7084 N N . VAL C 302 ? 2.7750 2.6427 2.4551 0.2385 -0.0325 0.1558 1121 VAL C N +7085 C CA . VAL C 302 ? 2.9926 2.8627 2.6782 0.2388 -0.0367 0.1602 1121 VAL C CA +7086 C C . VAL C 302 ? 2.9959 2.8618 2.6744 0.2378 -0.0322 0.1644 1121 VAL C C +7087 O O . VAL C 302 ? 3.1301 2.9946 2.8097 0.2398 -0.0320 0.1693 1121 VAL C O +7088 C CB . VAL C 302 ? 2.4455 2.3205 2.1367 0.2367 -0.0422 0.1578 1121 VAL C CB +7089 C CG1 . VAL C 302 ? 2.1239 2.0003 1.8181 0.2361 -0.0451 0.1623 1121 VAL C CG1 +7090 C CG2 . VAL C 302 ? 2.1801 2.0598 1.8805 0.2383 -0.0480 0.1551 1121 VAL C CG2 +7091 N N . LEU C 303 ? 2.7407 2.6048 2.4120 0.2347 -0.0286 0.1625 1122 LEU C N +7092 C CA . LEU C 303 ? 2.8301 2.6908 2.4948 0.2332 -0.0247 0.1660 1122 LEU C CA +7093 C C . LEU C 303 ? 2.8087 2.6644 2.4681 0.2352 -0.0197 0.1699 1122 LEU C C +7094 O O . LEU C 303 ? 2.6225 2.4766 2.2806 0.2353 -0.0188 0.1747 1122 LEU C O +7095 C CB . LEU C 303 ? 2.6739 2.5329 2.3308 0.2297 -0.0208 0.1625 1122 LEU C CB +7096 C CG . LEU C 303 ? 2.4448 2.3070 2.1038 0.2269 -0.0241 0.1618 1122 LEU C CG +7097 C CD1 . LEU C 303 ? 1.9592 1.8196 1.6102 0.2235 -0.0200 0.1577 1122 LEU C CD1 +7098 C CD2 . LEU C 303 ? 1.8604 1.7223 1.5204 0.2270 -0.0252 0.1674 1122 LEU C CD2 +7099 N N . SER D 5 ? 0.8465 1.4648 1.1768 0.2240 -0.0083 -0.1061 2 SER D N +7100 C CA . SER D 5 ? 1.5918 2.2134 1.9213 0.2234 -0.0095 -0.1055 2 SER D CA +7101 C C . SER D 5 ? 1.5600 2.1823 1.8890 0.2241 -0.0098 -0.1051 2 SER D C +7102 O O . SER D 5 ? 1.0665 1.6875 1.3948 0.2249 -0.0098 -0.1055 2 SER D O +7103 C CB . SER D 5 ? 1.5643 2.1878 1.8918 0.2228 -0.0107 -0.1060 2 SER D CB +7104 O OG . SER D 5 ? 1.4975 2.1212 1.8231 0.2233 -0.0115 -0.1064 2 SER D OG +7105 N N . LYS D 6 ? 1.5799 2.2044 1.9093 0.2238 -0.0102 -0.1043 3 LYS D N +7106 C CA . LYS D 6 ? 1.5103 2.1359 1.8393 0.2243 -0.0106 -0.1038 3 LYS D CA +7107 C C . LYS D 6 ? 1.5169 2.1446 1.8435 0.2242 -0.0120 -0.1042 3 LYS D C +7108 O O . LYS D 6 ? 1.3621 1.9903 1.6879 0.2248 -0.0124 -0.1041 3 LYS D O +7109 C CB . LYS D 6 ? 1.8330 2.4603 2.1633 0.2240 -0.0105 -0.1028 3 LYS D CB +7110 C CG . LYS D 6 ? 2.0781 2.7041 2.4109 0.2237 -0.0092 -0.1024 3 LYS D CG +7111 C CD . LYS D 6 ? 2.1621 2.7848 2.4963 0.2245 -0.0079 -0.1026 3 LYS D CD +7112 C CE . LYS D 6 ? 1.8640 2.4848 2.1991 0.2242 -0.0070 -0.1031 3 LYS D CE +7113 N NZ . LYS D 6 ? 1.5487 2.1661 1.8847 0.2250 -0.0058 -0.1036 3 LYS D NZ +7114 N N . GLY D 7 ? 1.4922 2.1210 1.8178 0.2234 -0.0127 -0.1046 4 GLY D N +7115 C CA . GLY D 7 ? 1.3644 1.9951 1.6878 0.2233 -0.0140 -0.1049 4 GLY D CA +7116 C C . GLY D 7 ? 1.2803 1.9092 1.6026 0.2241 -0.0140 -0.1057 4 GLY D C +7117 O O . GLY D 7 ? 1.0315 1.6615 1.3523 0.2244 -0.0148 -0.1059 4 GLY D O +7118 N N . GLU D 8 ? 0.9588 1.5849 1.2818 0.2244 -0.0131 -0.1062 5 GLU D N +7119 C CA . GLU D 8 ? 0.8395 1.4636 1.1616 0.2251 -0.0130 -0.1070 5 GLU D CA +7120 C C . GLU D 8 ? 0.9471 1.5710 1.2688 0.2260 -0.0131 -0.1070 5 GLU D C +7121 O O . GLU D 8 ? 1.2345 1.8582 1.5549 0.2264 -0.0136 -0.1076 5 GLU D O +7122 C CB . GLU D 8 ? 1.1248 1.7459 1.4483 0.2253 -0.0118 -0.1074 5 GLU D CB +7123 C CG . GLU D 8 ? 1.7259 2.3449 2.0485 0.2260 -0.0117 -0.1083 5 GLU D CG +7124 C CD . GLU D 8 ? 2.0096 2.6287 2.3310 0.2255 -0.0122 -0.1090 5 GLU D CD +7125 O OE1 . GLU D 8 ? 2.0669 2.6858 2.3890 0.2249 -0.0119 -0.1090 5 GLU D OE1 +7126 O OE2 . GLU D 8 ? 1.7029 2.3224 2.0228 0.2258 -0.0130 -0.1095 5 GLU D OE2 +7127 N N . GLU D 9 ? 1.0398 1.6640 1.3626 0.2263 -0.0127 -0.1062 6 GLU D N +7128 C CA . GLU D 9 ? 0.9381 1.5622 1.2607 0.2271 -0.0127 -0.1061 6 GLU D CA +7129 C C . GLU D 9 ? 1.0440 1.6709 1.3649 0.2270 -0.0139 -0.1060 6 GLU D C +7130 O O . GLU D 9 ? 1.1474 1.7746 1.4679 0.2277 -0.0141 -0.1060 6 GLU D O +7131 C CB . GLU D 9 ? 1.4971 2.1205 1.8217 0.2275 -0.0117 -0.1053 6 GLU D CB +7132 C CG . GLU D 9 ? 1.8166 2.4369 2.1430 0.2278 -0.0104 -0.1053 6 GLU D CG +7133 C CD . GLU D 9 ? 1.9866 2.6064 2.3152 0.2281 -0.0094 -0.1044 6 GLU D CD +7134 O OE1 . GLU D 9 ? 1.8367 2.4588 2.1653 0.2279 -0.0099 -0.1037 6 GLU D OE1 +7135 O OE2 . GLU D 9 ? 2.1351 2.7523 2.4654 0.2286 -0.0082 -0.1044 6 GLU D OE2 +7136 N N . LEU D 10 ? 0.8651 1.4943 1.1851 0.2262 -0.0148 -0.1060 7 LEU D N +7137 C CA . LEU D 10 ? 0.7287 1.3606 1.0470 0.2260 -0.0159 -0.1060 7 LEU D CA +7138 C C . LEU D 10 ? 1.0905 1.7222 1.4070 0.2262 -0.0166 -0.1069 7 LEU D C +7139 O O . LEU D 10 ? 0.7568 1.3902 1.0719 0.2263 -0.0175 -0.1071 7 LEU D O +7140 C CB . LEU D 10 ? 0.7771 1.4116 1.0954 0.2250 -0.0165 -0.1054 7 LEU D CB +7141 C CG . LEU D 10 ? 1.0371 1.6726 1.3569 0.2249 -0.0161 -0.1044 7 LEU D CG +7142 C CD1 . LEU D 10 ? 0.9864 1.6233 1.3068 0.2238 -0.0163 -0.1039 7 LEU D CD1 +7143 C CD2 . LEU D 10 ? 1.0262 1.6638 1.3452 0.2252 -0.0168 -0.1040 7 LEU D CD2 +7144 N N . PHE D 11 ? 1.1176 1.7471 1.4343 0.2262 -0.0162 -0.1075 8 PHE D N +7145 C CA . PHE D 11 ? 1.0195 1.6489 1.3347 0.2261 -0.0168 -0.1083 8 PHE D CA +7146 C C . PHE D 11 ? 1.0423 1.6692 1.3571 0.2270 -0.0164 -0.1091 8 PHE D C +7147 O O . PHE D 11 ? 1.0671 1.6938 1.3809 0.2269 -0.0169 -0.1098 8 PHE D O +7148 C CB . PHE D 11 ? 0.9176 1.5474 1.2329 0.2253 -0.0169 -0.1085 8 PHE D CB +7149 C CG . PHE D 11 ? 1.0736 1.7063 1.3884 0.2244 -0.0177 -0.1079 8 PHE D CG +7150 C CD1 . PHE D 11 ? 0.7423 1.3772 1.0555 0.2242 -0.0188 -0.1081 8 PHE D CD1 +7151 C CD2 . PHE D 11 ? 0.9485 1.5820 1.2647 0.2239 -0.0174 -0.1072 8 PHE D CD2 +7152 C CE1 . PHE D 11 ? 0.8643 1.5020 1.1773 0.2234 -0.0195 -0.1076 8 PHE D CE1 +7153 C CE2 . PHE D 11 ? 1.0040 1.6403 1.3198 0.2231 -0.0182 -0.1067 8 PHE D CE2 +7154 C CZ . PHE D 11 ? 0.8035 1.4419 1.1178 0.2228 -0.0192 -0.1069 8 PHE D CZ +7155 N N . THR D 12 ? 0.9986 1.6238 1.3145 0.2277 -0.0156 -0.1089 9 THR D N +7156 C CA . THR D 12 ? 1.0752 1.6986 1.3907 0.2286 -0.0154 -0.1095 9 THR D CA +7157 C C . THR D 12 ? 1.1394 1.7649 1.4533 0.2288 -0.0164 -0.1097 9 THR D C +7158 O O . THR D 12 ? 1.1776 1.8055 1.4913 0.2285 -0.0169 -0.1091 9 THR D O +7159 C CB . THR D 12 ? 0.3439 0.9653 0.6611 0.2293 -0.0143 -0.1092 9 THR D CB +7160 O OG1 . THR D 12 ? 0.9772 1.6003 1.2947 0.2294 -0.0144 -0.1084 9 THR D OG1 +7161 C CG2 . THR D 12 ? 0.7186 1.3383 1.0376 0.2290 -0.0133 -0.1089 9 THR D CG2 +7162 N N . GLY D 13 ? 0.8379 1.4628 1.1508 0.2293 -0.0167 -0.1104 10 GLY D N +7163 C CA . GLY D 13 ? 1.4479 2.0747 1.7593 0.2295 -0.0176 -0.1106 10 GLY D CA +7164 C C . GLY D 13 ? 0.7779 1.4076 1.0880 0.2288 -0.0186 -0.1105 10 GLY D C +7165 O O . GLY D 13 ? 0.9320 1.5629 1.2425 0.2281 -0.0187 -0.1100 10 GLY D O +7166 N N . VAL D 14 ? 0.6175 1.2484 0.9261 0.2290 -0.0194 -0.1110 11 VAL D N +7167 C CA . VAL D 14 ? 0.5904 1.2239 0.8977 0.2284 -0.0204 -0.1111 11 VAL D CA +7168 C C . VAL D 14 ? 0.7585 1.3947 1.0660 0.2279 -0.0208 -0.1102 11 VAL D C +7169 O O . VAL D 14 ? 0.8564 1.4937 1.1638 0.2283 -0.0209 -0.1098 11 VAL D O +7170 C CB . VAL D 14 ? 0.6208 1.2550 0.9266 0.2289 -0.0211 -0.1118 11 VAL D CB +7171 C CG1 . VAL D 14 ? 0.9134 1.5503 1.2180 0.2283 -0.0220 -0.1118 11 VAL D CG1 +7172 C CG2 . VAL D 14 ? 0.5764 1.2082 0.8821 0.2293 -0.0208 -0.1127 11 VAL D CG2 +7173 N N . VAL D 15 ? 0.5932 1.2305 0.9008 0.2271 -0.0210 -0.1099 12 VAL D N +7174 C CA . VAL D 15 ? 0.8146 1.4545 1.1224 0.2264 -0.0214 -0.1090 12 VAL D CA +7175 C C . VAL D 15 ? 0.9541 1.5968 1.2605 0.2260 -0.0224 -0.1091 12 VAL D C +7176 O O . VAL D 15 ? 0.7059 1.3486 1.0116 0.2257 -0.0228 -0.1097 12 VAL D O +7177 C CB . VAL D 15 ? 0.6473 1.2871 0.9563 0.2257 -0.0210 -0.1085 12 VAL D CB +7178 C CG1 . VAL D 15 ? 0.6807 1.3232 0.9899 0.2251 -0.0214 -0.1076 12 VAL D CG1 +7179 C CG2 . VAL D 15 ? 0.3859 1.0229 0.6964 0.2261 -0.0199 -0.1084 12 VAL D CG2 +7180 N N . PRO D 16 ? 0.7469 1.3918 1.0529 0.2260 -0.0229 -0.1086 13 PRO D N +7181 C CA . PRO D 16 ? 0.9362 1.5838 1.2411 0.2255 -0.0238 -0.1086 13 PRO D CA +7182 C C . PRO D 16 ? 0.7309 1.3802 1.0361 0.2245 -0.0241 -0.1081 13 PRO D C +7183 O O . PRO D 16 ? 0.8434 1.4929 1.1498 0.2241 -0.0238 -0.1073 13 PRO D O +7184 C CB . PRO D 16 ? 0.5133 1.1626 0.8177 0.2259 -0.0240 -0.1082 13 PRO D CB +7185 C CG . PRO D 16 ? 0.8042 1.4524 1.1100 0.2262 -0.0232 -0.1077 13 PRO D CG +7186 C CD . PRO D 16 ? 0.7379 1.3830 1.0445 0.2265 -0.0225 -0.1081 13 PRO D CD +7187 N N . ILE D 17 ? 0.8256 1.4760 1.1300 0.2241 -0.0248 -0.1084 14 ILE D N +7188 C CA . ILE D 17 ? 0.8039 1.4559 1.1085 0.2231 -0.0252 -0.1080 14 ILE D CA +7189 C C . ILE D 17 ? 0.7469 1.4019 1.0506 0.2227 -0.0261 -0.1077 14 ILE D C +7190 O O . ILE D 17 ? 0.6789 1.3345 0.9814 0.2231 -0.0265 -0.1082 14 ILE D O +7191 C CB . ILE D 17 ? 0.6430 1.2937 0.9475 0.2228 -0.0252 -0.1085 14 ILE D CB +7192 C CG1 . ILE D 17 ? 0.6763 1.3238 0.9816 0.2233 -0.0244 -0.1090 14 ILE D CG1 +7193 C CG2 . ILE D 17 ? 0.4463 1.0984 0.7513 0.2218 -0.0255 -0.1080 14 ILE D CG2 +7194 C CD1 . ILE D 17 ? 1.0689 1.7151 1.3740 0.2231 -0.0244 -0.1096 14 ILE D CD1 +7195 N N . LEU D 18 ? 0.7089 1.3658 1.0131 0.2219 -0.0263 -0.1069 15 LEU D N +7196 C CA . LEU D 18 ? 0.8957 1.5557 1.1994 0.2214 -0.0271 -0.1065 15 LEU D CA +7197 C C . LEU D 18 ? 0.8433 1.5045 1.1475 0.2204 -0.0275 -0.1060 15 LEU D C +7198 O O . LEU D 18 ? 0.5512 1.2118 0.8566 0.2200 -0.0270 -0.1056 15 LEU D O +7199 C CB . LEU D 18 ? 0.4587 1.1201 0.7626 0.2216 -0.0271 -0.1058 15 LEU D CB +7200 C CG . LEU D 18 ? 1.0023 1.6669 1.3059 0.2211 -0.0278 -0.1052 15 LEU D CG +7201 C CD1 . LEU D 18 ? 1.0956 1.7611 1.3977 0.2215 -0.0283 -0.1058 15 LEU D CD1 +7202 C CD2 . LEU D 18 ? 1.1109 1.7763 1.4150 0.2213 -0.0275 -0.1045 15 LEU D CD2 +7203 N N . VAL D 19 ? 0.6811 1.3438 0.9846 0.2200 -0.0282 -0.1062 16 VAL D N +7204 C CA . VAL D 19 ? 0.7338 1.3978 1.0378 0.2190 -0.0285 -0.1057 16 VAL D CA +7205 C C . VAL D 19 ? 0.7110 1.3783 1.0147 0.2184 -0.0293 -0.1051 16 VAL D C +7206 O O . VAL D 19 ? 0.6896 1.3580 0.9924 0.2187 -0.0298 -0.1054 16 VAL D O +7207 C CB . VAL D 19 ? 0.6817 1.3442 0.9854 0.2190 -0.0286 -0.1064 16 VAL D CB +7208 C CG1 . VAL D 19 ? 0.6251 1.2889 0.9294 0.2180 -0.0289 -0.1060 16 VAL D CG1 +7209 C CG2 . VAL D 19 ? 0.7048 1.3642 1.0089 0.2195 -0.0277 -0.1070 16 VAL D CG2 +7210 N N . GLU D 20 ? 0.7632 1.4320 1.0679 0.2176 -0.0295 -0.1043 17 GLU D N +7211 C CA . GLU D 20 ? 0.6123 1.2842 0.9169 0.2168 -0.0302 -0.1036 17 GLU D CA +7212 C C . GLU D 20 ? 0.8808 1.5536 1.1860 0.2158 -0.0306 -0.1033 17 GLU D C +7213 O O . GLU D 20 ? 0.5111 1.1832 0.8173 0.2154 -0.0302 -0.1030 17 GLU D O +7214 C CB . GLU D 20 ? 0.8083 1.4818 1.1135 0.2166 -0.0301 -0.1028 17 GLU D CB +7215 C CG . GLU D 20 ? 1.0206 1.6941 1.3252 0.2174 -0.0300 -0.1028 17 GLU D CG +7216 C CD . GLU D 20 ? 1.3510 2.0258 1.6544 0.2178 -0.0305 -0.1032 17 GLU D CD +7217 O OE1 . GLU D 20 ? 1.3734 2.0498 1.6765 0.2173 -0.0311 -0.1032 17 GLU D OE1 +7218 O OE2 . GLU D 20 ? 1.2160 1.8904 1.5187 0.2186 -0.0303 -0.1036 17 GLU D OE2 +7219 N N . LEU D 21 ? 0.6852 1.3596 0.9898 0.2155 -0.0312 -0.1034 18 LEU D N +7220 C CA . LEU D 21 ? 0.7702 1.4457 1.0753 0.2146 -0.0317 -0.1030 18 LEU D CA +7221 C C . LEU D 21 ? 0.7299 1.4087 1.0351 0.2139 -0.0324 -0.1022 18 LEU D C +7222 O O . LEU D 21 ? 0.8623 1.5423 1.1668 0.2142 -0.0328 -0.1023 18 LEU D O +7223 C CB . LEU D 21 ? 0.9426 1.6167 1.2473 0.2148 -0.0317 -0.1038 18 LEU D CB +7224 C CG . LEU D 21 ? 0.7935 1.4687 1.0986 0.2138 -0.0322 -0.1034 18 LEU D CG +7225 C CD1 . LEU D 21 ? 1.2526 1.9274 1.5588 0.2132 -0.0319 -0.1030 18 LEU D CD1 +7226 C CD2 . LEU D 21 ? 1.0521 1.7260 1.3567 0.2141 -0.0323 -0.1042 18 LEU D CD2 +7227 N N . ASP D 22 ? 0.7749 1.4551 1.0811 0.2129 -0.0327 -0.1015 19 ASP D N +7228 C CA . ASP D 22 ? 1.0047 1.6880 1.3112 0.2121 -0.0335 -0.1007 19 ASP D CA +7229 C C . ASP D 22 ? 1.0116 1.6954 1.3186 0.2113 -0.0338 -0.1006 19 ASP D C +7230 O O . ASP D 22 ? 0.9453 1.6289 1.2532 0.2106 -0.0337 -0.1003 19 ASP D O +7231 C CB . ASP D 22 ? 0.8165 1.5017 1.1239 0.2115 -0.0335 -0.0998 19 ASP D CB +7232 C CG . ASP D 22 ? 1.2418 1.9278 1.5486 0.2121 -0.0335 -0.0996 19 ASP D CG +7233 O OD1 . ASP D 22 ? 1.4405 2.1268 1.7463 0.2127 -0.0337 -0.1001 19 ASP D OD1 +7234 O OD2 . ASP D 22 ? 1.5888 2.2753 1.8963 0.2120 -0.0332 -0.0991 19 ASP D OD2 +7235 N N . GLY D 23 ? 0.9814 1.6659 1.2878 0.2113 -0.0343 -0.1009 20 GLY D N +7236 C CA . GLY D 23 ? 0.4160 1.1008 0.7228 0.2106 -0.0347 -0.1008 20 GLY D CA +7237 C C . GLY D 23 ? 1.0389 1.7269 1.3462 0.2097 -0.0355 -0.0999 20 GLY D C +7238 O O . GLY D 23 ? 0.8829 1.5728 1.1901 0.2098 -0.0358 -0.0995 20 GLY D O +7239 N N . ASP D 24 ? 1.2302 1.9186 1.5383 0.2089 -0.0357 -0.0997 21 ASP D N +7240 C CA . ASP D 24 ? 0.7397 1.4309 1.0484 0.2080 -0.0365 -0.0988 21 ASP D CA +7241 C C . ASP D 24 ? 0.9157 1.6065 1.2246 0.2075 -0.0367 -0.0989 21 ASP D C +7242 O O . ASP D 24 ? 0.9664 1.6567 1.2760 0.2069 -0.0366 -0.0988 21 ASP D O +7243 C CB . ASP D 24 ? 1.5631 2.2560 1.8728 0.2071 -0.0366 -0.0979 21 ASP D CB +7244 C CG . ASP D 24 ? 1.6353 2.3314 1.9457 0.2062 -0.0374 -0.0969 21 ASP D CG +7245 O OD1 . ASP D 24 ? 1.3922 2.0893 1.7025 0.2060 -0.0379 -0.0969 21 ASP D OD1 +7246 O OD2 . ASP D 24 ? 0.9442 1.6420 1.2553 0.2057 -0.0376 -0.0962 21 ASP D OD2 +7247 N N . VAL D 25 ? 0.8176 1.5088 1.1262 0.2077 -0.0371 -0.0992 22 VAL D N +7248 C CA . VAL D 25 ? 0.7992 1.4899 1.1079 0.2074 -0.0373 -0.0993 22 VAL D CA +7249 C C . VAL D 25 ? 0.8772 1.5706 1.1864 0.2067 -0.0381 -0.0986 22 VAL D C +7250 O O . VAL D 25 ? 0.7189 1.4130 1.0277 0.2072 -0.0383 -0.0988 22 VAL D O +7251 C CB . VAL D 25 ? 0.7583 1.4463 1.0661 0.2083 -0.0368 -0.1004 22 VAL D CB +7252 C CG1 . VAL D 25 ? 0.7846 1.4726 1.0927 0.2080 -0.0371 -0.1005 22 VAL D CG1 +7253 C CG2 . VAL D 25 ? 0.8390 1.5243 1.1467 0.2088 -0.0360 -0.1010 22 VAL D CG2 +7254 N N . ASN D 26 ? 0.8675 1.5626 1.1777 0.2056 -0.0385 -0.0979 23 ASN D N +7255 C CA . ASN D 26 ? 0.7194 1.4173 1.0304 0.2049 -0.0393 -0.0970 23 ASN D CA +7256 C C . ASN D 26 ? 1.0813 1.7813 1.3922 0.2049 -0.0396 -0.0965 23 ASN D C +7257 O O . ASN D 26 ? 0.7207 1.4220 1.0316 0.2051 -0.0400 -0.0964 23 ASN D O +7258 C CB . ASN D 26 ? 0.7672 1.4647 1.0779 0.2051 -0.0395 -0.0974 23 ASN D CB +7259 C CG . ASN D 26 ? 1.1681 1.8646 1.4793 0.2046 -0.0395 -0.0974 23 ASN D CG +7260 O OD1 . ASN D 26 ? 0.8227 1.5185 1.1342 0.2042 -0.0392 -0.0974 23 ASN D OD1 +7261 N ND2 . ASN D 26 ? 0.8219 1.5185 1.1331 0.2046 -0.0398 -0.0975 23 ASN D ND2 +7262 N N . GLY D 27 ? 0.9611 1.6613 1.2721 0.2049 -0.0394 -0.0963 24 GLY D N +7263 C CA . GLY D 27 ? 0.8416 1.5436 1.1526 0.2050 -0.0396 -0.0958 24 GLY D CA +7264 C C . GLY D 27 ? 0.9219 1.6231 1.2318 0.2061 -0.0393 -0.0965 24 GLY D C +7265 O O . GLY D 27 ? 0.9129 1.6158 1.2228 0.2062 -0.0395 -0.0961 24 GLY D O +7266 N N . HIS D 28 ? 0.9318 1.6304 1.2409 0.2069 -0.0389 -0.0975 25 HIS D N +7267 C CA . HIS D 28 ? 0.9870 1.6843 1.2950 0.2080 -0.0385 -0.0983 25 HIS D CA +7268 C C . HIS D 28 ? 1.0649 1.7604 1.3724 0.2085 -0.0379 -0.0987 25 HIS D C +7269 O O . HIS D 28 ? 0.6029 1.2962 0.9104 0.2087 -0.0374 -0.0992 25 HIS D O +7270 C CB . HIS D 28 ? 0.5110 1.2064 0.8183 0.2087 -0.0383 -0.0992 25 HIS D CB +7271 C CG . HIS D 28 ? 1.2879 1.9848 1.5956 0.2084 -0.0389 -0.0989 25 HIS D CG +7272 N ND1 . HIS D 28 ? 1.0542 1.7521 1.3628 0.2075 -0.0393 -0.0983 25 HIS D ND1 +7273 C CD2 . HIS D 28 ? 1.1398 1.8375 1.4472 0.2088 -0.0391 -0.0991 25 HIS D CD2 +7274 C CE1 . HIS D 28 ? 0.8475 1.5466 1.1563 0.2075 -0.0398 -0.0982 25 HIS D CE1 +7275 N NE2 . HIS D 28 ? 1.2229 1.9220 1.5311 0.2083 -0.0397 -0.0986 25 HIS D NE2 +7276 N N . LYS D 29 ? 0.8784 1.5751 1.1858 0.2088 -0.0378 -0.0984 26 LYS D N +7277 C CA . LYS D 29 ? 0.8356 1.5306 1.1425 0.2093 -0.0372 -0.0988 26 LYS D CA +7278 C C . LYS D 29 ? 1.0500 1.7432 1.3558 0.2105 -0.0369 -0.0998 26 LYS D C +7279 O O . LYS D 29 ? 0.8589 1.5525 1.1643 0.2107 -0.0371 -0.1001 26 LYS D O +7280 C CB . LYS D 29 ? 0.8183 1.5155 1.1256 0.2090 -0.0374 -0.0979 26 LYS D CB +7281 C CG . LYS D 29 ? 0.6712 1.3705 0.9798 0.2078 -0.0378 -0.0969 26 LYS D CG +7282 C CD . LYS D 29 ? 1.1407 1.8425 1.4497 0.2074 -0.0381 -0.0960 26 LYS D CD +7283 C CE . LYS D 29 ? 0.9616 1.6650 1.2719 0.2063 -0.0384 -0.0951 26 LYS D CE +7284 N NZ . LYS D 29 ? 1.2801 1.9819 1.5908 0.2062 -0.0379 -0.0951 26 LYS D NZ +7285 N N . PHE D 30 ? 0.6876 1.3787 0.9930 0.2111 -0.0362 -0.1003 27 PHE D N +7286 C CA . PHE D 30 ? 0.7738 1.4630 1.0781 0.2122 -0.0358 -0.1012 27 PHE D CA +7287 C C . PHE D 30 ? 0.8883 1.5755 1.1924 0.2127 -0.0351 -0.1015 27 PHE D C +7288 O O . PHE D 30 ? 0.6834 1.3702 0.9883 0.2123 -0.0349 -0.1011 27 PHE D O +7289 C CB . PHE D 30 ? 0.9368 1.6242 1.2407 0.2126 -0.0358 -0.1020 27 PHE D CB +7290 C CG . PHE D 30 ? 0.8408 1.5261 1.1450 0.2124 -0.0354 -0.1023 27 PHE D CG +7291 C CD1 . PHE D 30 ? 0.9886 1.6749 1.2937 0.2114 -0.0357 -0.1017 27 PHE D CD1 +7292 C CD2 . PHE D 30 ? 0.8517 1.5342 1.1555 0.2131 -0.0347 -0.1031 27 PHE D CD2 +7293 C CE1 . PHE D 30 ? 0.9577 1.6423 1.2632 0.2112 -0.0354 -0.1019 27 PHE D CE1 +7294 C CE2 . PHE D 30 ? 0.9479 1.6285 1.2521 0.2129 -0.0344 -0.1033 27 PHE D CE2 +7295 C CZ . PHE D 30 ? 0.7866 1.4682 1.0916 0.2120 -0.0347 -0.1027 27 PHE D CZ +7296 N N . SER D 31 ? 0.7969 1.4829 1.1001 0.2137 -0.0348 -0.1022 28 SER D N +7297 C CA . SER D 31 ? 0.8052 1.4892 1.1083 0.2143 -0.0341 -0.1025 28 SER D CA +7298 C C . SER D 31 ? 0.8666 1.5481 1.1688 0.2153 -0.0337 -0.1036 28 SER D C +7299 O O . SER D 31 ? 0.6390 1.3209 0.9405 0.2157 -0.0340 -0.1040 28 SER D O +7300 C CB . SER D 31 ? 0.8602 1.5458 1.1634 0.2144 -0.0341 -0.1019 28 SER D CB +7301 O OG . SER D 31 ? 1.3925 2.0801 1.6966 0.2134 -0.0344 -0.1009 28 SER D OG +7302 N N . VAL D 32 ? 0.7761 1.4551 1.0784 0.2156 -0.0331 -0.1039 29 VAL D N +7303 C CA . VAL D 32 ? 0.8326 1.5091 1.1343 0.2166 -0.0326 -0.1049 29 VAL D CA +7304 C C . VAL D 32 ? 0.7112 1.3861 1.0128 0.2172 -0.0320 -0.1050 29 VAL D C +7305 O O . VAL D 32 ? 0.4943 1.1688 0.7967 0.2168 -0.0317 -0.1045 29 VAL D O +7306 C CB . VAL D 32 ? 0.6884 1.3627 0.9902 0.2165 -0.0324 -0.1055 29 VAL D CB +7307 C CG1 . VAL D 32 ? 0.7250 1.3969 1.0260 0.2175 -0.0320 -0.1065 29 VAL D CG1 +7308 C CG2 . VAL D 32 ? 0.5291 1.2048 0.8310 0.2159 -0.0330 -0.1053 29 VAL D CG2 +7309 N N . SER D 33 ? 0.6432 1.3173 0.9440 0.2181 -0.0319 -0.1057 30 SER D N +7310 C CA . SER D 33 ? 0.9178 1.5901 1.2185 0.2188 -0.0312 -0.1059 30 SER D CA +7311 C C . SER D 33 ? 0.8660 1.5355 1.1663 0.2196 -0.0308 -0.1069 30 SER D C +7312 O O . SER D 33 ? 0.6409 1.3103 0.9404 0.2199 -0.0311 -0.1075 30 SER D O +7313 C CB . SER D 33 ? 0.7743 1.4483 1.0745 0.2192 -0.0314 -0.1057 30 SER D CB +7314 O OG . SER D 33 ? 1.1873 1.8629 1.4883 0.2187 -0.0314 -0.1047 30 SER D OG +7315 N N . GLY D 34 ? 0.8239 1.4912 1.1248 0.2198 -0.0301 -0.1070 31 GLY D N +7316 C CA . GLY D 34 ? 0.5593 1.2237 0.8598 0.2205 -0.0297 -0.1079 31 GLY D CA +7317 C C . GLY D 34 ? 0.7561 1.4189 1.0568 0.2213 -0.0290 -0.1080 31 GLY D C +7318 O O . GLY D 34 ? 0.6660 1.3289 0.9675 0.2211 -0.0287 -0.1074 31 GLY D O +7319 N N . GLU D 35 ? 0.5905 1.2517 0.8905 0.2221 -0.0289 -0.1088 32 GLU D N +7320 C CA . GLU D 35 ? 0.9173 1.5766 1.2175 0.2228 -0.0282 -0.1090 32 GLU D CA +7321 C C . GLU D 35 ? 0.7754 1.4319 1.0754 0.2235 -0.0278 -0.1099 32 GLU D C +7322 O O . GLU D 35 ? 0.6650 1.3213 0.9644 0.2236 -0.0281 -0.1105 32 GLU D O +7323 C CB . GLU D 35 ? 0.7221 1.3828 1.0217 0.2234 -0.0284 -0.1089 32 GLU D CB +7324 C CG . GLU D 35 ? 0.7333 1.3942 1.0317 0.2239 -0.0288 -0.1097 32 GLU D CG +7325 C CD . GLU D 35 ? 1.7624 2.4253 2.0602 0.2242 -0.0291 -0.1096 32 GLU D CD +7326 O OE1 . GLU D 35 ? 1.7998 2.4623 2.0978 0.2247 -0.0287 -0.1094 32 GLU D OE1 +7327 O OE2 . GLU D 35 ? 2.3291 2.9939 2.6261 0.2241 -0.0296 -0.1098 32 GLU D OE2 +7328 N N . GLY D 36 ? 0.9354 1.5898 1.2361 0.2239 -0.0271 -0.1099 33 GLY D N +7329 C CA . GLY D 36 ? 0.6560 1.3076 0.9566 0.2246 -0.0266 -0.1107 33 GLY D CA +7330 C C . GLY D 36 ? 0.6424 1.2918 0.9440 0.2249 -0.0257 -0.1105 33 GLY D C +7331 O O . GLY D 36 ? 0.6501 1.3001 0.9523 0.2249 -0.0255 -0.1099 33 GLY D O +7332 N N . GLU D 37 ? 0.7655 1.4123 1.0674 0.2252 -0.0253 -0.1111 34 GLU D N +7333 C CA . GLU D 37 ? 0.8179 1.4623 1.1209 0.2256 -0.0244 -0.1110 34 GLU D CA +7334 C C . GLU D 37 ? 0.6994 1.3415 1.0030 0.2255 -0.0239 -0.1114 34 GLU D C +7335 O O . GLU D 37 ? 0.6400 1.2817 0.9430 0.2254 -0.0242 -0.1120 34 GLU D O +7336 C CB . GLU D 37 ? 0.7319 1.3751 1.0345 0.2265 -0.0241 -0.1115 34 GLU D CB +7337 C CG . GLU D 37 ? 1.4143 2.0564 1.7160 0.2270 -0.0243 -0.1124 34 GLU D CG +7338 C CD . GLU D 37 ? 1.4355 2.0768 1.7369 0.2279 -0.0241 -0.1129 34 GLU D CD +7339 O OE1 . GLU D 37 ? 1.5790 2.2198 1.8810 0.2283 -0.0237 -0.1125 34 GLU D OE1 +7340 O OE2 . GLU D 37 ? 1.4419 2.0830 1.7424 0.2283 -0.0245 -0.1136 34 GLU D OE2 +7341 N N . GLY D 38 ? 0.6379 1.2784 0.9427 0.2255 -0.0231 -0.1111 35 GLY D N +7342 C CA . GLY D 38 ? 0.7960 1.4341 1.1014 0.2254 -0.0226 -0.1114 35 GLY D CA +7343 C C . GLY D 38 ? 0.7165 1.3519 1.0230 0.2260 -0.0216 -0.1115 35 GLY D C +7344 O O . GLY D 38 ? 0.6789 1.3143 0.9860 0.2262 -0.0212 -0.1110 35 GLY D O +7345 N N . ASP D 39 ? 0.8895 1.5225 1.1961 0.2263 -0.0212 -0.1121 36 ASP D N +7346 C CA . ASP D 39 ? 0.8654 1.4956 1.1730 0.2270 -0.0202 -0.1123 36 ASP D CA +7347 C C . ASP D 39 ? 0.5391 1.1675 0.8477 0.2266 -0.0195 -0.1123 36 ASP D C +7348 O O . ASP D 39 ? 0.5693 1.1963 0.8776 0.2266 -0.0195 -0.1129 36 ASP D O +7349 C CB . ASP D 39 ? 0.7463 1.3750 1.0531 0.2277 -0.0202 -0.1132 36 ASP D CB +7350 C CG . ASP D 39 ? 1.3020 1.9289 1.6096 0.2286 -0.0195 -0.1132 36 ASP D CG +7351 O OD1 . ASP D 39 ? 1.3103 1.9362 1.6192 0.2286 -0.0188 -0.1126 36 ASP D OD1 +7352 O OD2 . ASP D 39 ? 1.0165 1.6430 1.3233 0.2292 -0.0197 -0.1137 36 ASP D OD2 +7353 N N . ALA D 40 ? 0.8130 1.4415 1.1229 0.2262 -0.0190 -0.1116 37 ALA D N +7354 C CA . ALA D 40 ? 0.7052 1.3322 1.0160 0.2258 -0.0184 -0.1116 37 ALA D CA +7355 C C . ALA D 40 ? 0.6654 1.2892 0.9768 0.2264 -0.0175 -0.1122 37 ALA D C +7356 O O . ALA D 40 ? 0.7524 1.3751 1.0639 0.2262 -0.0173 -0.1126 37 ALA D O +7357 C CB . ALA D 40 ? 0.5323 1.1597 0.8446 0.2255 -0.0178 -0.1108 37 ALA D CB +7358 N N . THR D 41 ? 1.1037 1.7261 1.4154 0.2273 -0.0171 -0.1123 38 THR D N +7359 C CA . THR D 41 ? 0.6170 1.2364 0.9294 0.2280 -0.0162 -0.1128 38 THR D CA +7360 C C . THR D 41 ? 0.6487 1.2672 0.9601 0.2280 -0.0165 -0.1136 38 THR D C +7361 O O . THR D 41 ? 0.7845 1.4006 1.0967 0.2282 -0.0158 -0.1140 38 THR D O +7362 C CB . THR D 41 ? 0.7695 1.3882 1.0818 0.2288 -0.0161 -0.1128 38 THR D CB +7363 O OG1 . THR D 41 ? 0.9285 1.5485 1.2415 0.2288 -0.0160 -0.1120 38 THR D OG1 +7364 C CG2 . THR D 41 ? 0.3968 1.0123 0.7102 0.2295 -0.0150 -0.1132 38 THR D CG2 +7365 N N . TYR D 42 ? 0.5864 1.2067 0.8963 0.2278 -0.0175 -0.1139 39 TYR D N +7366 C CA . TYR D 42 ? 0.7619 1.3815 1.0710 0.2278 -0.0179 -0.1146 39 TYR D CA +7367 C C . TYR D 42 ? 0.6161 1.2379 0.9245 0.2269 -0.0187 -0.1145 39 TYR D C +7368 O O . TYR D 42 ? 0.6175 1.2397 0.9249 0.2269 -0.0192 -0.1151 39 TYR D O +7369 C CB . TYR D 42 ? 0.4238 1.0433 0.7320 0.2285 -0.0183 -0.1152 39 TYR D CB +7370 C CG . TYR D 42 ? 0.7141 1.3319 1.0230 0.2293 -0.0176 -0.1152 39 TYR D CG +7371 C CD1 . TYR D 42 ? 0.8340 1.4534 1.1430 0.2294 -0.0178 -0.1146 39 TYR D CD1 +7372 C CD2 . TYR D 42 ? 0.8405 1.4554 1.1502 0.2299 -0.0167 -0.1156 39 TYR D CD2 +7373 C CE1 . TYR D 42 ? 1.1279 1.7460 1.4376 0.2302 -0.0172 -0.1145 39 TYR D CE1 +7374 C CE2 . TYR D 42 ? 0.7853 1.3989 1.0958 0.2306 -0.0161 -0.1154 39 TYR D CE2 +7375 C CZ . TYR D 42 ? 0.9886 1.6037 1.2991 0.2307 -0.0163 -0.1149 39 TYR D CZ +7376 O OH . TYR D 42 ? 0.8010 1.4149 1.1123 0.2315 -0.0157 -0.1147 39 TYR D OH +7377 N N . GLY D 43 ? 0.6768 1.3001 0.9857 0.2263 -0.0187 -0.1139 40 GLY D N +7378 C CA . GLY D 43 ? 0.6095 1.2350 0.9180 0.2254 -0.0194 -0.1136 40 GLY D CA +7379 C C . GLY D 43 ? 0.8517 1.4793 1.1587 0.2253 -0.0205 -0.1138 40 GLY D C +7380 O O . GLY D 43 ? 0.6399 1.2680 0.9463 0.2249 -0.0209 -0.1141 40 GLY D O +7381 N N . LYS D 44 ? 0.6330 1.2620 0.9395 0.2256 -0.0208 -0.1136 41 LYS D N +7382 C CA . LYS D 44 ? 0.3420 0.9727 0.6472 0.2257 -0.0217 -0.1139 41 LYS D CA +7383 C C . LYS D 44 ? 0.8503 1.4841 1.1552 0.2252 -0.0224 -0.1133 41 LYS D C +7384 O O . LYS D 44 ? 0.8079 1.4422 1.1133 0.2252 -0.0222 -0.1127 41 LYS D O +7385 C CB . LYS D 44 ? 0.5713 1.2006 0.8761 0.2266 -0.0216 -0.1145 41 LYS D CB +7386 C CG . LYS D 44 ? 0.7724 1.4028 1.0759 0.2268 -0.0223 -0.1150 41 LYS D CG +7387 C CD . LYS D 44 ? 0.5385 1.1677 0.8418 0.2277 -0.0222 -0.1156 41 LYS D CD +7388 C CE . LYS D 44 ? 1.1232 1.7547 1.4254 0.2278 -0.0230 -0.1157 41 LYS D CE +7389 N NZ . LYS D 44 ? 1.0603 1.6907 1.3619 0.2286 -0.0230 -0.1164 41 LYS D NZ +7390 N N . LEU D 45 ? 0.8350 1.4708 1.1389 0.2247 -0.0233 -0.1133 42 LEU D N +7391 C CA . LEU D 45 ? 0.6704 1.3092 0.9740 0.2243 -0.0240 -0.1128 42 LEU D CA +7392 C C . LEU D 45 ? 0.3872 1.0275 0.6895 0.2245 -0.0247 -0.1132 42 LEU D C +7393 O O . LEU D 45 ? 0.7935 1.4333 1.0953 0.2245 -0.0250 -0.1137 42 LEU D O +7394 C CB . LEU D 45 ? 0.6144 1.2546 0.9184 0.2233 -0.0242 -0.1122 42 LEU D CB +7395 C CG . LEU D 45 ? 0.7754 1.4179 1.0798 0.2227 -0.0245 -0.1113 42 LEU D CG +7396 C CD1 . LEU D 45 ? 1.1252 1.7665 1.4306 0.2230 -0.0237 -0.1109 42 LEU D CD1 +7397 C CD2 . LEU D 45 ? 0.8337 1.4777 1.1384 0.2217 -0.0248 -0.1109 42 LEU D CD2 +7398 N N . THR D 46 ? 0.6450 1.2870 0.9468 0.2247 -0.0251 -0.1129 43 THR D N +7399 C CA . THR D 46 ? 0.9597 1.6035 1.2605 0.2247 -0.0259 -0.1132 43 THR D CA +7400 C C . THR D 46 ? 0.7483 1.3951 1.0488 0.2242 -0.0264 -0.1125 43 THR D C +7401 O O . THR D 46 ? 0.8100 1.4573 1.1109 0.2244 -0.0262 -0.1120 43 THR D O +7402 C CB . THR D 46 ? 0.6654 1.3083 0.9656 0.2257 -0.0258 -0.1139 43 THR D CB +7403 O OG1 . THR D 46 ? 1.3338 1.9782 1.6338 0.2259 -0.0259 -0.1135 43 THR D OG1 +7404 C CG2 . THR D 46 ? 0.7541 1.3937 1.0548 0.2263 -0.0250 -0.1143 43 THR D CG2 +7405 N N . LEU D 47 ? 0.6201 1.2689 0.9202 0.2237 -0.0271 -0.1124 44 LEU D N +7406 C CA . LEU D 47 ? 0.6218 1.2735 0.9218 0.2231 -0.0277 -0.1116 44 LEU D CA +7407 C C . LEU D 47 ? 0.5593 1.2132 0.8585 0.2230 -0.0284 -0.1118 44 LEU D C +7408 O O . LEU D 47 ? 0.4810 1.1344 0.7799 0.2230 -0.0287 -0.1123 44 LEU D O +7409 C CB . LEU D 47 ? 0.5243 1.1767 0.8252 0.2222 -0.0276 -0.1109 44 LEU D CB +7410 C CG . LEU D 47 ? 0.8033 1.4546 1.1052 0.2223 -0.0269 -0.1105 44 LEU D CG +7411 C CD1 . LEU D 47 ? 0.8533 1.5048 1.1561 0.2214 -0.0268 -0.1099 44 LEU D CD1 +7412 C CD2 . LEU D 47 ? 0.6279 1.2808 0.9297 0.2224 -0.0270 -0.1099 44 LEU D CD2 +7413 N N . LYS D 48 ? 0.6210 1.2772 0.9199 0.2229 -0.0288 -0.1114 45 LYS D N +7414 C CA . LYS D 48 ? 0.4766 1.1351 0.7748 0.2227 -0.0296 -0.1114 45 LYS D CA +7415 C C . LYS D 48 ? 0.8046 1.4659 1.1031 0.2219 -0.0300 -0.1104 45 LYS D C +7416 O O . LYS D 48 ? 0.5668 1.2289 0.8656 0.2218 -0.0299 -0.1098 45 LYS D O +7417 C CB . LYS D 48 ? 0.4946 1.1535 0.7919 0.2235 -0.0297 -0.1119 45 LYS D CB +7418 C CG . LYS D 48 ? 0.3936 1.0546 0.6903 0.2233 -0.0304 -0.1120 45 LYS D CG +7419 C CD . LYS D 48 ? 0.5152 1.1772 0.8111 0.2239 -0.0306 -0.1123 45 LYS D CD +7420 C CE . LYS D 48 ? 0.7853 1.4486 1.0806 0.2240 -0.0312 -0.1128 45 LYS D CE +7421 N NZ . LYS D 48 ? 0.7008 1.3646 0.9954 0.2247 -0.0313 -0.1133 45 LYS D NZ +7422 N N . PHE D 49 ? 0.6823 1.3450 0.9808 0.2213 -0.0305 -0.1103 46 PHE D N +7423 C CA . PHE D 49 ? 0.5970 1.2623 0.8958 0.2205 -0.0310 -0.1094 46 PHE D CA +7424 C C . PHE D 49 ? 0.5752 1.2430 0.8735 0.2205 -0.0317 -0.1094 46 PHE D C +7425 O O . PHE D 49 ? 0.6161 1.2836 0.9139 0.2207 -0.0319 -0.1100 46 PHE D O +7426 C CB . PHE D 49 ? 0.6678 1.3329 0.9673 0.2197 -0.0311 -0.1091 46 PHE D CB +7427 C CG . PHE D 49 ? 0.6988 1.3617 0.9990 0.2197 -0.0304 -0.1091 46 PHE D CG +7428 C CD1 . PHE D 49 ? 0.6710 1.3343 0.9719 0.2195 -0.0301 -0.1084 46 PHE D CD1 +7429 C CD2 . PHE D 49 ? 0.7206 1.3810 1.0208 0.2200 -0.0300 -0.1098 46 PHE D CD2 +7430 C CE1 . PHE D 49 ? 0.6272 1.2883 0.9287 0.2195 -0.0295 -0.1085 46 PHE D CE1 +7431 C CE2 . PHE D 49 ? 0.8638 1.5221 1.1646 0.2200 -0.0294 -0.1098 46 PHE D CE2 +7432 C CZ . PHE D 49 ? 0.5038 1.1625 0.8054 0.2198 -0.0291 -0.1091 46 PHE D CZ +7433 N N . ILE D 50 ? 0.7805 1.4505 1.0787 0.2202 -0.0319 -0.1087 47 ILE D N +7434 C CA . ILE D 50 ? 0.5366 1.2092 0.8344 0.2201 -0.0325 -0.1085 47 ILE D CA +7435 C C . ILE D 50 ? 0.8376 1.5124 1.1361 0.2191 -0.0329 -0.1076 47 ILE D C +7436 O O . ILE D 50 ? 0.5317 1.2070 0.8309 0.2187 -0.0328 -0.1069 47 ILE D O +7437 C CB . ILE D 50 ? 0.7120 1.3856 1.0094 0.2206 -0.0325 -0.1085 47 ILE D CB +7438 C CG1 . ILE D 50 ? 0.9144 1.5860 1.2111 0.2216 -0.0321 -0.1094 47 ILE D CG1 +7439 C CG2 . ILE D 50 ? 1.0728 1.7493 1.3699 0.2203 -0.0331 -0.1082 47 ILE D CG2 +7440 C CD1 . ILE D 50 ? 0.8953 1.5665 1.1914 0.2219 -0.0324 -0.1103 47 ILE D CD1 +7441 N N . CYS D 51 ? 0.8890 1.5653 1.1876 0.2187 -0.0335 -0.1075 48 CYS D N +7442 C CA . CYS D 51 ? 1.1285 1.8074 1.4278 0.2178 -0.0339 -0.1065 48 CYS D CA +7443 C C . CYS D 51 ? 0.7920 1.4732 1.0910 0.2178 -0.0342 -0.1061 48 CYS D C +7444 O O . CYS D 51 ? 1.0003 1.6827 1.2988 0.2181 -0.0345 -0.1064 48 CYS D O +7445 C CB . CYS D 51 ? 1.3764 2.0563 1.6759 0.2173 -0.0344 -0.1065 48 CYS D CB +7446 S SG . CYS D 51 ? 0.8285 1.5112 1.1290 0.2161 -0.0350 -0.1053 48 CYS D SG +7447 N N . THR D 52 ? 0.7549 1.4370 1.0543 0.2174 -0.0341 -0.1053 49 THR D N +7448 C CA . THR D 52 ? 0.8431 1.5273 1.1425 0.2174 -0.0343 -0.1048 49 THR D CA +7449 C C . THR D 52 ? 0.6976 1.3849 0.9974 0.2167 -0.0349 -0.1040 49 THR D C +7450 O O . THR D 52 ? 0.9089 1.5982 1.2086 0.2167 -0.0351 -0.1036 49 THR D O +7451 C CB . THR D 52 ? 0.7596 1.4433 1.0593 0.2175 -0.0338 -0.1044 49 THR D CB +7452 O OG1 . THR D 52 ? 0.6075 1.2909 0.9082 0.2167 -0.0337 -0.1038 49 THR D OG1 +7453 C CG2 . THR D 52 ? 0.6667 1.3477 0.9658 0.2184 -0.0332 -0.1051 49 THR D CG2 +7454 N N . THR D 53 ? 0.9871 1.6748 1.2874 0.2160 -0.0352 -0.1038 50 THR D N +7455 C CA . THR D 53 ? 0.4405 1.1310 0.7414 0.2152 -0.0358 -0.1030 50 THR D CA +7456 C C . THR D 53 ? 0.7773 1.4686 1.0780 0.2153 -0.0362 -0.1033 50 THR D C +7457 O O . THR D 53 ? 1.2567 1.9503 1.5580 0.2146 -0.0367 -0.1027 50 THR D O +7458 C CB . THR D 53 ? 0.6814 1.3725 0.9834 0.2142 -0.0360 -0.1022 50 THR D CB +7459 O OG1 . THR D 53 ? 0.6951 1.3844 0.9972 0.2141 -0.0359 -0.1026 50 THR D OG1 +7460 C CG2 . THR D 53 ? 0.5602 1.2510 0.8626 0.2141 -0.0356 -0.1017 50 THR D CG2 +7461 N N . GLY D 54 ? 0.6370 1.3266 0.9370 0.2161 -0.0360 -0.1043 51 GLY D N +7462 C CA . GLY D 54 ? 0.7727 1.4628 1.0726 0.2162 -0.0364 -0.1047 51 GLY D CA +7463 C C . GLY D 54 ? 0.5669 1.2547 0.8668 0.2163 -0.0362 -0.1053 51 GLY D C +7464 O O . GLY D 54 ? 1.5417 2.2270 1.8411 0.2169 -0.0357 -0.1060 51 GLY D O +7465 N N . LYS D 55 ? 1.0710 1.7597 1.3715 0.2158 -0.0366 -0.1050 52 LYS D N +7466 C CA . LYS D 55 ? 0.7897 1.4765 1.0904 0.2158 -0.0365 -0.1054 52 LYS D CA +7467 C C . LYS D 55 ? 0.6253 1.3115 0.9265 0.2151 -0.0363 -0.1049 52 LYS D C +7468 O O . LYS D 55 ? 0.7515 1.4394 1.0533 0.2145 -0.0365 -0.1041 52 LYS D O +7469 C CB . LYS D 55 ? 0.4102 1.0981 0.7113 0.2155 -0.0369 -0.1053 52 LYS D CB +7470 C CG . LYS D 55 ? 1.2479 1.9342 1.5484 0.2164 -0.0368 -0.1064 52 LYS D CG +7471 C CD . LYS D 55 ? 1.7876 2.4746 2.0887 0.2161 -0.0372 -0.1063 52 LYS D CD +7472 C CE . LYS D 55 ? 1.9113 2.5990 2.2121 0.2167 -0.0373 -0.1068 52 LYS D CE +7473 N NZ . LYS D 55 ? 1.6663 2.3544 1.9678 0.2165 -0.0376 -0.1068 52 LYS D NZ +7474 N N . LEU D 56 ? 0.8952 1.5793 1.1965 0.2152 -0.0361 -0.1053 53 LEU D N +7475 C CA . LEU D 56 ? 0.7833 1.4665 1.0852 0.2146 -0.0359 -0.1050 53 LEU D CA +7476 C C . LEU D 56 ? 0.6554 1.3400 0.9581 0.2137 -0.0364 -0.1044 53 LEU D C +7477 O O . LEU D 56 ? 0.7935 1.4781 1.0962 0.2138 -0.0366 -0.1046 53 LEU D O +7478 C CB . LEU D 56 ? 0.7125 1.3925 1.0140 0.2152 -0.0353 -0.1058 53 LEU D CB +7479 C CG . LEU D 56 ? 0.8436 1.5223 1.1454 0.2149 -0.0348 -0.1056 53 LEU D CG +7480 C CD1 . LEU D 56 ? 0.5967 1.2759 0.8985 0.2151 -0.0346 -0.1053 53 LEU D CD1 +7481 C CD2 . LEU D 56 ? 0.3390 1.0146 0.6406 0.2155 -0.0342 -0.1064 53 LEU D CD2 +7482 N N . PRO D 57 ? 0.8685 1.5545 1.1720 0.2129 -0.0366 -0.1035 54 PRO D N +7483 C CA . PRO D 57 ? 0.6987 1.3860 1.0030 0.2120 -0.0370 -0.1028 54 PRO D CA +7484 C C . PRO D 57 ? 0.9118 1.5970 1.2161 0.2120 -0.0368 -0.1033 54 PRO D C +7485 O O . PRO D 57 ? 0.7837 1.4696 1.0885 0.2117 -0.0372 -0.1032 54 PRO D O +7486 C CB . PRO D 57 ? 0.6222 1.3109 0.9273 0.2112 -0.0371 -0.1020 54 PRO D CB +7487 C CG . PRO D 57 ? 0.6329 1.3200 0.9374 0.2117 -0.0365 -0.1023 54 PRO D CG +7488 C CD . PRO D 57 ? 0.8534 1.5397 1.1570 0.2127 -0.0364 -0.1030 54 PRO D CD +7489 N N . VAL D 58 ? 0.8907 1.5733 1.1947 0.2125 -0.0362 -0.1039 55 VAL D N +7490 C CA . VAL D 58 ? 0.8570 1.5376 1.1611 0.2125 -0.0359 -0.1044 55 VAL D CA +7491 C C . VAL D 58 ? 0.9809 1.6589 1.2842 0.2135 -0.0354 -0.1054 55 VAL D C +7492 O O . VAL D 58 ? 0.7679 1.4456 1.0705 0.2142 -0.0353 -0.1058 55 VAL D O +7493 C CB . VAL D 58 ? 0.7256 1.4053 1.0301 0.2121 -0.0355 -0.1042 55 VAL D CB +7494 C CG1 . VAL D 58 ? 0.6712 1.3535 0.9765 0.2110 -0.0360 -0.1031 55 VAL D CG1 +7495 C CG2 . VAL D 58 ? 0.8274 1.5059 1.1313 0.2128 -0.0350 -0.1045 55 VAL D CG2 +7496 N N . PRO D 59 ? 0.8645 1.5406 1.1678 0.2136 -0.0352 -0.1059 56 PRO D N +7497 C CA . PRO D 59 ? 0.8454 1.5190 1.1480 0.2146 -0.0347 -0.1070 56 PRO D CA +7498 C C . PRO D 59 ? 1.0807 1.7522 1.3829 0.2151 -0.0341 -0.1074 56 PRO D C +7499 O O . PRO D 59 ? 0.8222 1.4935 1.1249 0.2147 -0.0338 -0.1070 56 PRO D O +7500 C CB . PRO D 59 ? 0.6028 1.2751 0.9057 0.2145 -0.0346 -0.1072 56 PRO D CB +7501 C CG . PRO D 59 ? 0.8415 1.5157 1.1452 0.2134 -0.0351 -0.1063 56 PRO D CG +7502 C CD . PRO D 59 ? 0.8276 1.5036 1.1316 0.2129 -0.0352 -0.1056 56 PRO D CD +7503 N N . TRP D 60 ? 0.9582 1.6282 1.2597 0.2161 -0.0337 -0.1082 57 TRP D N +7504 C CA . TRP D 60 ? 0.4474 1.1154 0.7486 0.2166 -0.0331 -0.1086 57 TRP D CA +7505 C C . TRP D 60 ? 0.5879 1.2536 0.8895 0.2165 -0.0325 -0.1088 57 TRP D C +7506 O O . TRP D 60 ? 0.5197 1.1850 0.8217 0.2163 -0.0322 -0.1085 57 TRP D O +7507 C CB . TRP D 60 ? 0.5828 1.2496 0.8832 0.2176 -0.0329 -0.1094 57 TRP D CB +7508 C CG . TRP D 60 ? 0.6624 1.3310 0.9624 0.2178 -0.0332 -0.1092 57 TRP D CG +7509 C CD1 . TRP D 60 ? 0.4666 1.1366 0.7662 0.2180 -0.0336 -0.1093 57 TRP D CD1 +7510 C CD2 . TRP D 60 ? 0.6478 1.3170 0.9478 0.2177 -0.0330 -0.1088 57 TRP D CD2 +7511 N NE1 . TRP D 60 ? 0.5939 1.2655 0.8933 0.2181 -0.0337 -0.1090 57 TRP D NE1 +7512 C CE2 . TRP D 60 ? 0.6037 1.2748 0.9033 0.2180 -0.0333 -0.1087 57 TRP D CE2 +7513 C CE3 . TRP D 60 ? 0.5771 1.2455 0.8776 0.2176 -0.0325 -0.1085 57 TRP D CE3 +7514 C CZ2 . TRP D 60 ? 0.5268 1.1990 0.8263 0.2180 -0.0333 -0.1083 57 TRP D CZ2 +7515 C CZ3 . TRP D 60 ? 0.6067 1.2761 0.9071 0.2176 -0.0325 -0.1080 57 TRP D CZ3 +7516 C CH2 . TRP D 60 ? 0.6720 1.3433 0.9719 0.2178 -0.0329 -0.1079 57 TRP D CH2 +7517 N N . PRO D 61 ? 0.7990 1.4632 1.1006 0.2166 -0.0324 -0.1093 58 PRO D N +7518 C CA . PRO D 61 ? 0.3378 0.9998 0.6398 0.2166 -0.0319 -0.1095 58 PRO D CA +7519 C C . PRO D 61 ? 0.4303 1.0931 0.7330 0.2157 -0.0318 -0.1088 58 PRO D C +7520 O O . PRO D 61 ? 0.7233 1.3842 1.0263 0.2159 -0.0312 -0.1090 58 PRO D O +7521 C CB . PRO D 61 ? 0.6258 1.2876 0.9278 0.2164 -0.0321 -0.1097 58 PRO D CB +7522 C CG . PRO D 61 ? 0.7726 1.4347 1.0740 0.2170 -0.0324 -0.1101 58 PRO D CG +7523 C CD . PRO D 61 ? 0.6124 1.2768 0.9137 0.2169 -0.0328 -0.1097 58 PRO D CD +7524 N N . THR D 62 ? 0.8186 1.4842 1.1218 0.2149 -0.0324 -0.1080 59 THR D N +7525 C CA . THR D 62 ? 0.7278 1.3943 1.0317 0.2140 -0.0325 -0.1073 59 THR D CA +7526 C C . THR D 62 ? 0.7757 1.4418 1.0798 0.2141 -0.0320 -0.1071 59 THR D C +7527 O O . THR D 62 ? 0.6837 1.3503 0.9885 0.2134 -0.0320 -0.1066 59 THR D O +7528 C CB . THR D 62 ? 0.7885 1.4582 1.0928 0.2132 -0.0333 -0.1064 59 THR D CB +7529 O OG1 . THR D 62 ? 0.8649 1.5362 1.1688 0.2135 -0.0336 -0.1062 59 THR D OG1 +7530 C CG2 . THR D 62 ? 0.8049 1.4751 1.1094 0.2129 -0.0337 -0.1064 59 THR D CG2 +7531 N N . LEU D 63 ? 0.8587 1.5240 1.1622 0.2149 -0.0318 -0.1074 60 LEU D N +7532 C CA . LEU D 63 ? 0.5186 1.1839 0.8224 0.2150 -0.0314 -0.1072 60 LEU D CA +7533 C C . LEU D 63 ? 0.8796 1.5420 1.1833 0.2158 -0.0306 -0.1078 60 LEU D C +7534 O O . LEU D 63 ? 0.5900 1.2520 0.8941 0.2158 -0.0302 -0.1076 60 LEU D O +7535 C CB . LEU D 63 ? 0.7644 1.4318 1.0678 0.2151 -0.0319 -0.1069 60 LEU D CB +7536 C CG . LEU D 63 ? 0.9646 1.6352 1.2683 0.2143 -0.0327 -0.1061 60 LEU D CG +7537 C CD1 . LEU D 63 ? 0.8803 1.5526 1.1834 0.2146 -0.0331 -0.1060 60 LEU D CD1 +7538 C CD2 . LEU D 63 ? 0.6552 1.3269 0.9598 0.2135 -0.0327 -0.1053 60 LEU D CD2 +7539 N N . VAL D 64 ? 0.8060 1.4662 1.1092 0.2164 -0.0303 -0.1086 61 VAL D N +7540 C CA . VAL D 64 ? 0.6492 1.3066 0.9524 0.2172 -0.0295 -0.1093 61 VAL D CA +7541 C C . VAL D 64 ? 0.5334 1.1896 0.8374 0.2170 -0.0289 -0.1090 61 VAL D C +7542 O O . VAL D 64 ? 0.6540 1.3091 0.9582 0.2174 -0.0284 -0.1091 61 VAL D O +7543 C CB . VAL D 64 ? 0.6147 1.2699 0.9175 0.2177 -0.0293 -0.1101 61 VAL D CB +7544 C CG1 . VAL D 64 ? 0.3800 1.0322 0.6830 0.2184 -0.0284 -0.1106 61 VAL D CG1 +7545 C CG2 . VAL D 64 ? 0.3382 0.9941 0.6402 0.2181 -0.0298 -0.1104 61 VAL D CG2 +7546 N N . THR D 65 ? 0.6576 1.3142 0.9623 0.2162 -0.0289 -0.1087 62 THR D N +7547 C CA . THR D 65 ? 0.8082 1.4636 1.1138 0.2159 -0.0283 -0.1085 62 THR D CA +7548 C C . THR D 65 ? 0.5415 1.1986 0.8477 0.2156 -0.0284 -0.1078 62 THR D C +7549 O O . THR D 65 ? 0.8944 1.5505 1.2013 0.2155 -0.0278 -0.1076 62 THR D O +7550 C CB . THR D 65 ? 0.8262 1.4820 1.1324 0.2151 -0.0284 -0.1083 62 THR D CB +7551 O OG1 . THR D 65 ? 1.1339 1.7928 1.4402 0.2143 -0.0293 -0.1076 62 THR D OG1 +7552 C CG2 . THR D 65 ? 0.8034 1.4576 1.1091 0.2154 -0.0283 -0.1090 62 THR D CG2 +7553 N N . THR D 66 ? 0.7479 1.4076 1.0537 0.2152 -0.0291 -0.1073 63 THR D N +7554 C CA . THR D 66 ? 0.9425 1.6041 1.2489 0.2148 -0.0292 -0.1065 63 THR D CA +7555 C C . THR D 66 ? 0.9280 1.5888 1.2340 0.2156 -0.0289 -0.1066 63 THR D C +7556 O O . THR D 66 ? 0.8153 1.4760 1.1220 0.2155 -0.0285 -0.1062 63 THR D O +7557 C CB . THR D 66 ? 0.9839 1.6488 1.2902 0.2140 -0.0302 -0.1058 63 THR D CB +7558 O OG1 . THR D 66 ? 0.6669 1.3323 0.9734 0.2134 -0.0305 -0.1058 63 THR D OG1 +7559 C CG2 . THR D 66 ? 0.6290 1.2957 0.9361 0.2134 -0.0303 -0.1049 63 THR D CG2 +7560 N N . PHE D 67 ? 0.9492 1.6094 1.2543 0.2163 -0.0290 -0.1072 64 PHE D N +7561 C CA . PHE D 67 ? 0.7818 1.4413 1.0863 0.2172 -0.0288 -0.1075 64 PHE D CA +7562 C C . PHE D 67 ? 0.8525 1.5089 1.1574 0.2179 -0.0278 -0.1080 64 PHE D C +7563 O O . PHE D 67 ? 0.8985 1.5544 1.2037 0.2182 -0.0274 -0.1077 64 PHE D O +7564 C CB . PHE D 67 ? 0.7392 1.3989 1.0426 0.2177 -0.0292 -0.1080 64 PHE D CB +7565 C CG . PHE D 67 ? 0.4032 1.0658 0.7062 0.2173 -0.0300 -0.1076 64 PHE D CG +7566 C CD1 . PHE D 67 ? 0.7032 1.3682 1.0066 0.2168 -0.0303 -0.1068 64 PHE D CD1 +7567 C CD2 . PHE D 67 ? 0.7908 1.4537 1.0930 0.2175 -0.0304 -0.1081 64 PHE D CD2 +7568 C CE1 . PHE D 67 ? 0.6427 1.3104 0.9457 0.2164 -0.0311 -0.1064 64 PHE D CE1 +7569 C CE2 . PHE D 67 ? 0.7542 1.4198 1.0562 0.2172 -0.0312 -0.1077 64 PHE D CE2 +7570 C CZ . PHE D 67 ? 0.6542 1.3221 0.9565 0.2166 -0.0315 -0.1068 64 PHE D CZ +7571 N N1 . CR2 D 68 ? 0.8150 1.4693 1.1197 0.2183 -0.0275 -0.1087 65 CR2 D N1 +7572 C CA1 . CR2 D 68 ? 0.6637 1.3148 0.9690 0.2187 -0.0266 -0.1091 65 CR2 D CA1 +7573 C C1 . CR2 D 68 ? 0.8495 1.4997 1.1557 0.2181 -0.0262 -0.1090 65 CR2 D C1 +7574 N N2 . CR2 D 68 ? 0.9935 1.6423 1.2996 0.2180 -0.0261 -0.1095 65 CR2 D N2 +7575 N N3 . CR2 D 68 ? 0.8976 1.5484 1.2048 0.2175 -0.0260 -0.1084 65 CR2 D N3 +7576 C C2 . CR2 D 68 ? 0.8893 1.5393 1.1971 0.2171 -0.0257 -0.1085 65 CR2 D C2 +7577 O O2 . CR2 D 68 ? 0.7188 1.3693 1.0277 0.2164 -0.0254 -0.1080 65 CR2 D O2 +7578 C CA2 . CR2 D 68 ? 0.9528 1.6016 1.2600 0.2174 -0.0258 -0.1092 65 CR2 D CA2 +7579 C CA3 . CR2 D 68 ? 0.4752 1.1277 0.7828 0.2173 -0.0261 -0.1077 65 CR2 D CA3 +7580 C C3 . CR2 D 68 ? 0.7240 1.3746 1.0321 0.2180 -0.0252 -0.1077 65 CR2 D C3 +7581 O O3 . CR2 D 68 ? 0.6630 1.3141 0.9723 0.2176 -0.0249 -0.1071 65 CR2 D O3 +7582 C CB2 . CR2 D 68 ? 0.7460 1.3935 1.0534 0.2171 -0.0255 -0.1096 65 CR2 D CB2 +7583 C CG2 . CR2 D 68 ? 0.7179 1.3642 1.0245 0.2174 -0.0257 -0.1102 65 CR2 D CG2 +7584 C CD1 . CR2 D 68 ? 0.7039 1.3502 1.0096 0.2181 -0.0260 -0.1106 65 CR2 D CD1 +7585 C CD2 . CR2 D 68 ? 0.6354 1.2811 0.9424 0.2170 -0.0255 -0.1104 65 CR2 D CD2 +7586 C CE1 . CR2 D 68 ? 0.8809 1.5263 1.1860 0.2183 -0.0262 -0.1112 65 CR2 D CE1 +7587 C CE2 . CR2 D 68 ? 0.7460 1.3907 1.0524 0.2173 -0.0257 -0.1110 65 CR2 D CE2 +7588 C CZ . CR2 D 68 ? 0.9408 1.5854 1.2463 0.2180 -0.0260 -0.1114 65 CR2 D CZ +7589 O OH . CR2 D 68 ? 0.7027 1.3464 1.0077 0.2183 -0.0261 -0.1120 65 CR2 D OH +7590 N N . VAL D 69 ? 1.1396 1.7877 1.4475 0.2189 -0.0247 -0.1085 68 VAL D N +7591 C CA . VAL D 69 ? 0.8438 1.4904 1.1523 0.2195 -0.0240 -0.1084 68 VAL D CA +7592 C C . VAL D 69 ? 0.5846 1.2281 0.8939 0.2199 -0.0230 -0.1088 68 VAL D C +7593 O O . VAL D 69 ? 1.0087 1.6504 1.3182 0.2206 -0.0224 -0.1090 68 VAL D O +7594 C CB . VAL D 69 ? 0.6627 1.3101 0.9707 0.2200 -0.0241 -0.1082 68 VAL D CB +7595 C CG1 . VAL D 69 ? 0.5649 1.2153 0.8730 0.2193 -0.0247 -0.1074 68 VAL D CG1 +7596 C CG2 . VAL D 69 ? 1.1920 1.8392 1.4987 0.2207 -0.0245 -0.1088 68 VAL D CG2 +7597 N N . GLN D 70 ? 1.0539 1.6971 1.3638 0.2192 -0.0228 -0.1087 69 GLN D N +7598 C CA . GLN D 70 ? 0.9674 1.6079 1.2781 0.2195 -0.0219 -0.1092 69 GLN D CA +7599 C C . GLN D 70 ? 0.7037 1.3420 1.0155 0.2200 -0.0209 -0.1092 69 GLN D C +7600 O O . GLN D 70 ? 1.2536 1.8894 1.5660 0.2203 -0.0201 -0.1095 69 GLN D O +7601 C CB . GLN D 70 ? 0.7496 1.3905 1.0608 0.2186 -0.0220 -0.1091 69 GLN D CB +7602 C CG . GLN D 70 ? 1.0593 1.7014 1.3695 0.2182 -0.0228 -0.1094 69 GLN D CG +7603 C CD . GLN D 70 ? 1.1739 1.8175 1.4847 0.2171 -0.0231 -0.1090 69 GLN D CD +7604 O OE1 . GLN D 70 ? 1.0612 1.7053 1.3731 0.2166 -0.0227 -0.1085 69 GLN D OE1 +7605 N NE2 . GLN D 70 ? 0.8887 1.5331 1.1988 0.2167 -0.0236 -0.1092 69 GLN D NE2 +7606 N N . CYS D 71 ? 0.7797 1.4190 1.0917 0.2203 -0.0209 -0.1086 70 CYS D N +7607 C CA . CYS D 71 ? 0.7928 1.4303 1.1058 0.2209 -0.0200 -0.1085 70 CYS D CA +7608 C C . CYS D 71 ? 1.0105 1.6461 1.3227 0.2220 -0.0198 -0.1092 70 CYS D C +7609 O O . CYS D 71 ? 0.9219 1.5558 1.2348 0.2226 -0.0191 -0.1091 70 CYS D O +7610 C CB . CYS D 71 ? 0.5049 1.1442 0.8184 0.2208 -0.0202 -0.1077 70 CYS D CB +7611 S SG . CYS D 71 ? 1.0365 1.6789 1.3484 0.2207 -0.0213 -0.1074 70 CYS D SG +7612 N N . PHE D 72 ? 0.8390 1.4750 1.1498 0.2221 -0.0205 -0.1097 71 PHE D N +7613 C CA . PHE D 72 ? 0.7434 1.3778 1.0536 0.2230 -0.0204 -0.1104 71 PHE D CA +7614 C C . PHE D 72 ? 0.8191 1.4513 1.1292 0.2231 -0.0200 -0.1111 71 PHE D C +7615 O O . PHE D 72 ? 1.3084 1.9396 1.6176 0.2237 -0.0202 -0.1117 71 PHE D O +7616 C CB . PHE D 72 ? 0.7010 1.3374 1.0098 0.2231 -0.0213 -0.1105 71 PHE D CB +7617 C CG . PHE D 72 ? 0.7360 1.3740 1.0447 0.2233 -0.0215 -0.1099 71 PHE D CG +7618 C CD1 . PHE D 72 ? 0.8879 1.5286 1.1968 0.2226 -0.0220 -0.1092 71 PHE D CD1 +7619 C CD2 . PHE D 72 ? 0.9637 1.6006 1.2723 0.2242 -0.0212 -0.1101 71 PHE D CD2 +7620 C CE1 . PHE D 72 ? 0.7588 1.4009 1.0676 0.2227 -0.0222 -0.1086 71 PHE D CE1 +7621 C CE2 . PHE D 72 ? 0.6794 1.3179 0.9880 0.2243 -0.0214 -0.1095 71 PHE D CE2 +7622 C CZ . PHE D 72 ? 1.0650 1.7060 1.3736 0.2236 -0.0219 -0.1088 71 PHE D CZ +7623 N N . SER D 73 ? 0.6938 1.3254 1.0048 0.2226 -0.0196 -0.1110 72 SER D N +7624 C CA . SER D 73 ? 0.9269 1.5562 1.2379 0.2227 -0.0192 -0.1117 72 SER D CA +7625 C C . SER D 73 ? 0.8899 1.5161 1.2018 0.2235 -0.0181 -0.1119 72 SER D C +7626 O O . SER D 73 ? 1.2643 1.8902 1.5773 0.2237 -0.0175 -0.1114 72 SER D O +7627 C CB . SER D 73 ? 0.7678 1.3975 1.0794 0.2219 -0.0191 -0.1115 72 SER D CB +7628 N N . ARG D 74 ? 0.7192 1.3434 1.0308 0.2241 -0.0178 -0.1126 73 ARG D N +7629 C CA . ARG D 74 ? 0.9159 1.5370 1.2285 0.2248 -0.0167 -0.1129 73 ARG D CA +7630 C C . ARG D 74 ? 0.8374 1.4570 1.1513 0.2245 -0.0158 -0.1129 73 ARG D C +7631 O O . ARG D 74 ? 0.7878 1.4068 1.1014 0.2242 -0.0158 -0.1133 73 ARG D O +7632 C CB . ARG D 74 ? 0.9349 1.5544 1.2468 0.2255 -0.0167 -0.1136 73 ARG D CB +7633 C CG . ARG D 74 ? 0.8653 1.4817 1.1783 0.2263 -0.0155 -0.1138 73 ARG D CG +7634 C CD . ARG D 74 ? 0.6918 1.3066 1.0040 0.2270 -0.0156 -0.1145 73 ARG D CD +7635 N NE . ARG D 74 ? 0.7182 1.3323 1.0299 0.2269 -0.0157 -0.1151 73 ARG D NE +7636 C CZ . ARG D 74 ? 1.0929 1.7050 1.4054 0.2268 -0.0150 -0.1154 73 ARG D CZ +7637 N NH1 . ARG D 74 ? 0.3412 0.9517 0.6552 0.2269 -0.0139 -0.1151 73 ARG D NH1 +7638 N NH2 . ARG D 74 ? 0.6913 1.3029 1.0032 0.2267 -0.0152 -0.1159 73 ARG D NH2 +7639 N N . TYR D 75 ? 0.8118 1.4306 1.1271 0.2245 -0.0150 -0.1124 74 TYR D N +7640 C CA . TYR D 75 ? 1.0315 1.6485 1.3482 0.2243 -0.0139 -0.1124 74 TYR D CA +7641 C C . TYR D 75 ? 1.0146 1.6282 1.3321 0.2252 -0.0128 -0.1128 74 TYR D C +7642 O O . TYR D 75 ? 1.1288 1.7417 1.4468 0.2258 -0.0124 -0.1126 74 TYR D O +7643 C CB . TYR D 75 ? 0.7397 1.3577 1.0576 0.2238 -0.0136 -0.1116 74 TYR D CB +7644 C CG . TYR D 75 ? 0.8645 1.4851 1.1822 0.2228 -0.0143 -0.1113 74 TYR D CG +7645 C CD1 . TYR D 75 ? 0.8564 1.4799 1.1729 0.2223 -0.0155 -0.1110 74 TYR D CD1 +7646 C CD2 . TYR D 75 ? 1.0821 1.7021 1.4007 0.2222 -0.0137 -0.1113 74 TYR D CD2 +7647 C CE1 . TYR D 75 ? 0.9717 1.5974 1.2879 0.2214 -0.0161 -0.1107 74 TYR D CE1 +7648 C CE2 . TYR D 75 ? 0.8775 1.4999 1.1959 0.2212 -0.0144 -0.1111 74 TYR D CE2 +7649 C CZ . TYR D 75 ? 1.0806 1.7059 1.3979 0.2208 -0.0156 -0.1107 74 TYR D CZ +7650 O OH . TYR D 75 ? 1.0418 1.6694 1.3589 0.2198 -0.0163 -0.1104 74 TYR D OH +7651 N N . PRO D 76 ? 0.9013 1.5131 1.2190 0.2253 -0.0123 -0.1134 75 PRO D N +7652 C CA . PRO D 76 ? 0.7825 1.3910 1.1011 0.2261 -0.0111 -0.1137 75 PRO D CA +7653 C C . PRO D 76 ? 1.2968 1.9042 1.6173 0.2261 -0.0100 -0.1132 75 PRO D C +7654 O O . PRO D 76 ? 1.1265 1.7353 1.4476 0.2254 -0.0100 -0.1127 75 PRO D O +7655 C CB . PRO D 76 ? 0.8659 1.4731 1.1844 0.2258 -0.0109 -0.1143 75 PRO D CB +7656 C CG . PRO D 76 ? 0.9063 1.5160 1.2234 0.2251 -0.0121 -0.1144 75 PRO D CG +7657 C CD . PRO D 76 ? 0.9726 1.5850 1.2896 0.2246 -0.0127 -0.1137 75 PRO D CD +7658 N N . ASP D 77 ? 1.2314 1.8363 1.5529 0.2269 -0.0090 -0.1132 76 ASP D N +7659 C CA . ASP D 77 ? 1.2970 1.9007 1.6204 0.2271 -0.0079 -0.1127 76 ASP D CA +7660 C C . ASP D 77 ? 1.3849 1.9880 1.7095 0.2266 -0.0070 -0.1126 76 ASP D C +7661 O O . ASP D 77 ? 0.9579 1.5616 1.2838 0.2263 -0.0065 -0.1120 76 ASP D O +7662 C CB . ASP D 77 ? 1.6643 2.2652 1.9885 0.2282 -0.0069 -0.1129 76 ASP D CB +7663 C CG . ASP D 77 ? 1.8576 2.4591 2.1807 0.2287 -0.0077 -0.1129 76 ASP D CG +7664 O OD1 . ASP D 77 ? 1.6591 2.2626 1.9822 0.2287 -0.0082 -0.1124 76 ASP D OD1 +7665 O OD2 . ASP D 77 ? 1.9690 2.5693 2.2915 0.2293 -0.0078 -0.1135 76 ASP D OD2 +7666 N N . HIS D 78 ? 1.3086 1.9106 1.6330 0.2264 -0.0068 -0.1132 77 HIS D N +7667 C CA . HIS D 78 ? 0.7917 1.3930 1.1172 0.2258 -0.0060 -0.1132 77 HIS D CA +7668 C C . HIS D 78 ? 1.2546 1.8588 1.5797 0.2248 -0.0068 -0.1129 77 HIS D C +7669 O O . HIS D 78 ? 1.3354 1.9394 1.6615 0.2242 -0.0062 -0.1128 77 HIS D O +7670 C CB . HIS D 78 ? 0.8199 1.4192 1.1453 0.2260 -0.0055 -0.1139 77 HIS D CB +7671 C CG . HIS D 78 ? 1.0597 1.6605 1.3832 0.2255 -0.0067 -0.1143 77 HIS D CG +7672 N ND1 . HIS D 78 ? 1.0206 1.6216 1.3427 0.2259 -0.0075 -0.1147 77 HIS D ND1 +7673 C CD2 . HIS D 78 ? 0.9967 1.5990 1.3197 0.2246 -0.0072 -0.1144 77 HIS D CD2 +7674 C CE1 . HIS D 78 ? 1.1990 1.8015 1.5198 0.2254 -0.0084 -0.1150 77 HIS D CE1 +7675 N NE2 . HIS D 78 ? 1.3383 1.9416 1.6596 0.2246 -0.0083 -0.1148 77 HIS D NE2 +7676 N N . MET D 79 ? 1.2730 1.8798 1.5966 0.2245 -0.0082 -0.1127 78 MET D N +7677 C CA . MET D 79 ? 1.0099 1.6198 1.3331 0.2235 -0.0091 -0.1123 78 MET D CA +7678 C C . MET D 79 ? 1.1904 1.8022 1.5140 0.2233 -0.0094 -0.1115 78 MET D C +7679 O O . MET D 79 ? 0.9491 1.5629 1.2730 0.2225 -0.0097 -0.1111 78 MET D O +7680 C CB . MET D 79 ? 0.8597 1.4712 1.1808 0.2232 -0.0104 -0.1127 78 MET D CB +7681 C CG . MET D 79 ? 1.1026 1.7128 1.4233 0.2231 -0.0102 -0.1134 78 MET D CG +7682 S SD . MET D 79 ? 1.0943 1.7069 1.4130 0.2226 -0.0118 -0.1137 78 MET D SD +7683 C CE . MET D 79 ? 0.9068 1.5229 1.2255 0.2216 -0.0126 -0.1129 78 MET D CE +7684 N N . LYS D 80 ? 1.0146 1.6258 1.3382 0.2241 -0.0093 -0.1113 79 LYS D N +7685 C CA . LYS D 80 ? 1.0976 1.7108 1.4213 0.2240 -0.0098 -0.1106 79 LYS D CA +7686 C C . LYS D 80 ? 1.0869 1.7013 1.4121 0.2234 -0.0094 -0.1099 79 LYS D C +7687 O O . LYS D 80 ? 1.4601 2.0762 1.7855 0.2234 -0.0098 -0.1093 79 LYS D O +7688 C CB . LYS D 80 ? 0.7721 1.3839 1.0961 0.2250 -0.0094 -0.1105 79 LYS D CB +7689 C CG . LYS D 80 ? 1.1213 1.7329 1.4437 0.2256 -0.0101 -0.1111 79 LYS D CG +7690 C CD . LYS D 80 ? 0.7370 1.3480 1.0596 0.2264 -0.0099 -0.1108 79 LYS D CD +7691 C CE . LYS D 80 ? 0.9253 1.5360 1.2464 0.2270 -0.0105 -0.1114 79 LYS D CE +7692 N NZ . LYS D 80 ? 1.1646 1.7782 1.4840 0.2267 -0.0119 -0.1114 79 LYS D NZ +7693 N N . GLN D 81 ? 1.2709 1.8844 1.5971 0.2229 -0.0087 -0.1100 80 GLN D N +7694 C CA . GLN D 81 ? 1.4063 2.0210 1.7339 0.2223 -0.0083 -0.1094 80 GLN D CA +7695 C C . GLN D 81 ? 1.3594 1.9766 1.6862 0.2212 -0.0093 -0.1094 80 GLN D C +7696 O O . GLN D 81 ? 1.4542 2.0725 1.7820 0.2205 -0.0090 -0.1090 80 GLN D O +7697 C CB . GLN D 81 ? 1.2247 1.8367 1.5543 0.2225 -0.0067 -0.1095 80 GLN D CB +7698 C CG . GLN D 81 ? 1.1292 1.7396 1.4589 0.2223 -0.0061 -0.1102 80 GLN D CG +7699 C CD . GLN D 81 ? 1.4416 2.0497 1.7705 0.2231 -0.0059 -0.1109 80 GLN D CD +7700 O OE1 . GLN D 81 ? 1.6583 2.2657 1.9869 0.2238 -0.0060 -0.1108 80 GLN D OE1 +7701 N NE2 . GLN D 81 ? 1.2100 1.8169 1.5388 0.2229 -0.0055 -0.1115 80 GLN D NE2 +7702 N N . HIS D 82 ? 1.2535 1.8717 1.5785 0.2211 -0.0103 -0.1099 81 HIS D N +7703 C CA . HIS D 82 ? 1.2823 1.9030 1.6063 0.2201 -0.0114 -0.1098 81 HIS D CA +7704 C C . HIS D 82 ? 1.2785 1.9018 1.6009 0.2200 -0.0128 -0.1096 81 HIS D C +7705 O O . HIS D 82 ? 1.2307 1.8560 1.5520 0.2194 -0.0138 -0.1097 81 HIS D O +7706 C CB . HIS D 82 ? 1.2577 1.8775 1.5811 0.2199 -0.0114 -0.1106 81 HIS D CB +7707 C CG . HIS D 82 ? 1.2607 1.8780 1.5855 0.2200 -0.0100 -0.1109 81 HIS D CG +7708 N ND1 . HIS D 82 ? 1.2604 1.8783 1.5866 0.2193 -0.0095 -0.1106 81 HIS D ND1 +7709 C CD2 . HIS D 82 ? 0.7961 1.4105 1.1213 0.2206 -0.0090 -0.1114 81 HIS D CD2 +7710 C CE1 . HIS D 82 ? 1.3480 1.9633 1.6752 0.2195 -0.0082 -0.1110 81 HIS D CE1 +7711 N NE2 . HIS D 82 ? 1.4084 2.0215 1.7351 0.2203 -0.0079 -0.1115 81 HIS D NE2 +7712 N N . ASP D 83 ? 1.1103 1.7336 1.4327 0.2207 -0.0128 -0.1093 82 ASP D N +7713 C CA . ASP D 83 ? 1.0938 1.7194 1.4149 0.2207 -0.0140 -0.1090 82 ASP D CA +7714 C C . ASP D 83 ? 1.0501 1.6782 1.3718 0.2200 -0.0143 -0.1082 82 ASP D C +7715 O O . ASP D 83 ? 1.2178 1.8458 1.5403 0.2204 -0.0139 -0.1077 82 ASP D O +7716 C CB . ASP D 83 ? 1.5311 2.1554 1.8518 0.2217 -0.0138 -0.1091 82 ASP D CB +7717 C CG . ASP D 83 ? 1.3772 2.0037 1.6963 0.2218 -0.0150 -0.1091 82 ASP D CG +7718 O OD1 . ASP D 83 ? 1.1349 1.7640 1.4536 0.2212 -0.0158 -0.1085 82 ASP D OD1 +7719 O OD2 . ASP D 83 ? 1.5728 2.1983 1.8909 0.2225 -0.0152 -0.1096 82 ASP D OD2 +7720 N N . PHE D 84 ? 1.0808 1.7112 1.4022 0.2191 -0.0151 -0.1080 83 PHE D N +7721 C CA . PHE D 84 ? 0.8349 1.4679 1.1568 0.2183 -0.0156 -0.1072 83 PHE D CA +7722 C C . PHE D 84 ? 0.9474 1.5823 1.2682 0.2185 -0.0165 -0.1068 83 PHE D C +7723 O O . PHE D 84 ? 1.3391 1.9750 1.6607 0.2185 -0.0164 -0.1061 83 PHE D O +7724 C CB . PHE D 84 ? 0.8560 1.4909 1.1776 0.2172 -0.0162 -0.1072 83 PHE D CB +7725 C CG . PHE D 84 ? 1.0933 1.7314 1.4149 0.2165 -0.0171 -0.1064 83 PHE D CG +7726 C CD1 . PHE D 84 ? 1.3421 1.9808 1.6653 0.2161 -0.0166 -0.1057 83 PHE D CD1 +7727 C CD2 . PHE D 84 ? 0.9846 1.6252 1.3048 0.2160 -0.0183 -0.1063 83 PHE D CD2 +7728 C CE1 . PHE D 84 ? 1.1952 1.8368 1.5184 0.2154 -0.0174 -0.1050 83 PHE D CE1 +7729 C CE2 . PHE D 84 ? 1.3376 1.9811 1.6578 0.2153 -0.0191 -0.1056 83 PHE D CE2 +7730 C CZ . PHE D 84 ? 1.3572 2.0012 1.6789 0.2150 -0.0186 -0.1049 83 PHE D CZ +7731 N N . PHE D 85 ? 0.9137 1.5493 1.2328 0.2187 -0.0173 -0.1072 84 PHE D N +7732 C CA . PHE D 85 ? 0.8771 1.5147 1.1950 0.2189 -0.0182 -0.1070 84 PHE D CA +7733 C C . PHE D 85 ? 1.0148 1.6517 1.3332 0.2197 -0.0178 -0.1066 84 PHE D C +7734 O O . PHE D 85 ? 1.4109 2.0497 1.7294 0.2194 -0.0181 -0.1060 84 PHE D O +7735 C CB . PHE D 85 ? 0.9932 1.6305 1.3094 0.2192 -0.0189 -0.1077 84 PHE D CB +7736 C CG . PHE D 85 ? 0.9841 1.6223 1.2998 0.2184 -0.0194 -0.1079 84 PHE D CG +7737 C CD1 . PHE D 85 ? 0.9715 1.6123 1.2874 0.2175 -0.0200 -0.1074 84 PHE D CD1 +7738 C CD2 . PHE D 85 ? 0.9912 1.6275 1.3064 0.2187 -0.0192 -0.1087 84 PHE D CD2 +7739 C CE1 . PHE D 85 ? 1.0439 1.6855 1.3594 0.2168 -0.0205 -0.1076 84 PHE D CE1 +7740 C CE2 . PHE D 85 ? 0.7339 1.3711 1.0487 0.2180 -0.0197 -0.1089 84 PHE D CE2 +7741 C CZ . PHE D 85 ? 0.9554 1.5953 1.2703 0.2171 -0.0203 -0.1083 84 PHE D CZ +7742 N N . LYS D 86 ? 1.0474 1.6816 1.3659 0.2205 -0.0170 -0.1071 85 LYS D N +7743 C CA . LYS D 86 ? 1.1935 1.8269 1.5125 0.2213 -0.0166 -0.1068 85 LYS D CA +7744 C C . LYS D 86 ? 1.2458 1.8792 1.5667 0.2211 -0.0158 -0.1061 85 LYS D C +7745 O O . LYS D 86 ? 1.1321 1.7667 1.4534 0.2213 -0.0159 -0.1055 85 LYS D O +7746 C CB . LYS D 86 ? 0.9712 1.6017 1.2901 0.2223 -0.0159 -0.1075 85 LYS D CB +7747 C CG . LYS D 86 ? 0.9693 1.5999 1.2865 0.2226 -0.0166 -0.1082 85 LYS D CG +7748 C CD . LYS D 86 ? 0.9034 1.5313 1.2205 0.2236 -0.0160 -0.1087 85 LYS D CD +7749 C CE . LYS D 86 ? 0.7655 1.3931 1.0811 0.2239 -0.0166 -0.1095 85 LYS D CE +7750 N NZ . LYS D 86 ? 1.2905 1.9177 1.6059 0.2233 -0.0167 -0.1099 85 LYS D NZ +7751 N N . SER D 87 ? 1.2028 1.8349 1.5249 0.2207 -0.0150 -0.1061 86 SER D N +7752 C CA . SER D 87 ? 1.1848 1.8165 1.5090 0.2206 -0.0141 -0.1055 86 SER D CA +7753 C C . SER D 87 ? 1.1723 1.8071 1.4968 0.2199 -0.0148 -0.1047 86 SER D C +7754 O O . SER D 87 ? 1.1778 1.8126 1.5037 0.2199 -0.0142 -0.1040 86 SER D O +7755 C CB . SER D 87 ? 1.3365 1.9667 1.6619 0.2202 -0.0133 -0.1058 86 SER D CB +7756 O OG . SER D 87 ? 1.1483 1.7805 1.4732 0.2192 -0.0140 -0.1058 86 SER D OG +7757 N N . ALA D 88 ? 1.2142 1.8514 1.5372 0.2193 -0.0160 -0.1047 87 ALA D N +7758 C CA . ALA D 88 ? 1.0278 1.6680 1.3510 0.2185 -0.0167 -0.1039 87 ALA D CA +7759 C C . ALA D 88 ? 1.0215 1.6630 1.3441 0.2190 -0.0171 -0.1034 87 ALA D C +7760 O O . ALA D 88 ? 1.2599 1.9037 1.5830 0.2185 -0.0175 -0.1027 87 ALA D O +7761 C CB . ALA D 88 ? 1.0125 1.6548 1.3345 0.2177 -0.0178 -0.1041 87 ALA D CB +7762 N N . MET D 89 ? 0.9674 1.6075 1.2892 0.2199 -0.0170 -0.1039 88 MET D N +7763 C CA . MET D 89 ? 1.0716 1.7128 1.3927 0.2204 -0.0174 -0.1035 88 MET D CA +7764 C C . MET D 89 ? 0.9239 1.5643 1.2467 0.2209 -0.0165 -0.1029 88 MET D C +7765 O O . MET D 89 ? 1.0632 1.7015 1.3875 0.2210 -0.0155 -0.1029 88 MET D O +7766 C CB . MET D 89 ? 0.9306 1.5707 1.2502 0.2212 -0.0176 -0.1043 88 MET D CB +7767 C CG . MET D 89 ? 1.1612 1.8022 1.4792 0.2208 -0.0185 -0.1049 88 MET D CG +7768 S SD . MET D 89 ? 0.9958 1.6406 1.3125 0.2201 -0.0199 -0.1044 88 MET D SD +7769 C CE . MET D 89 ? 1.3071 1.9524 1.6227 0.2195 -0.0206 -0.1051 88 MET D CE +7770 N N . PRO D 90 ? 0.9354 1.5773 1.2578 0.2212 -0.0169 -0.1023 89 PRO D N +7771 C CA . PRO D 90 ? 1.3148 1.9592 1.6355 0.2211 -0.0180 -0.1023 89 PRO D CA +7772 C C . PRO D 90 ? 1.1895 1.8368 1.5100 0.2201 -0.0189 -0.1018 89 PRO D C +7773 O O . PRO D 90 ? 1.1912 1.8406 1.5103 0.2199 -0.0198 -0.1018 89 PRO D O +7774 C CB . PRO D 90 ? 1.0540 1.6984 1.3749 0.2219 -0.0178 -0.1019 89 PRO D CB +7775 C CG . PRO D 90 ? 1.0593 1.7030 1.3824 0.2218 -0.0169 -0.1011 89 PRO D CG +7776 C CD . PRO D 90 ? 0.9342 1.5757 1.2583 0.2216 -0.0161 -0.1016 89 PRO D CD +7777 N N . GLU D 91 ? 0.9649 1.6125 1.2870 0.2194 -0.0184 -0.1013 90 GLU D N +7778 C CA . GLU D 91 ? 1.1944 1.8448 1.5166 0.2184 -0.0192 -0.1007 90 GLU D CA +7779 C C . GLU D 91 ? 1.1437 1.7953 1.4645 0.2178 -0.0200 -0.1012 90 GLU D C +7780 O O . GLU D 91 ? 0.9794 1.6335 1.2994 0.2173 -0.0210 -0.1009 90 GLU D O +7781 C CB . GLU D 91 ? 1.5757 2.2259 1.9000 0.2178 -0.0185 -0.1001 90 GLU D CB +7782 C CG . GLU D 91 ? 1.7629 2.4119 2.0888 0.2184 -0.0175 -0.0996 90 GLU D CG +7783 C CD . GLU D 91 ? 1.9759 2.6263 2.3036 0.2177 -0.0173 -0.0987 90 GLU D CD +7784 O OE1 . GLU D 91 ? 1.8540 2.5069 2.1814 0.2174 -0.0179 -0.0980 90 GLU D OE1 +7785 O OE2 . GLU D 91 ? 2.0486 2.6974 2.3780 0.2176 -0.0164 -0.0987 90 GLU D OE2 +7786 N N . GLY D 92 ? 1.0685 1.7180 1.3891 0.2179 -0.0197 -0.1019 91 GLY D N +7787 C CA . GLY D 92 ? 1.0306 1.6809 1.3498 0.2175 -0.0205 -0.1025 91 GLY D CA +7788 C C . GLY D 92 ? 0.9779 1.6290 1.2978 0.2165 -0.0206 -0.1024 91 GLY D C +7789 O O . GLY D 92 ? 1.1114 1.7621 1.4328 0.2160 -0.0200 -0.1020 91 GLY D O +7790 N N . TYR D 93 ? 0.9004 1.5525 1.2190 0.2161 -0.0215 -0.1028 92 TYR D N +7791 C CA . TYR D 93 ? 0.9955 1.6484 1.3145 0.2151 -0.0217 -0.1028 92 TYR D CA +7792 C C . TYR D 93 ? 1.0148 1.6707 1.3326 0.2144 -0.0229 -0.1026 92 TYR D C +7793 O O . TYR D 93 ? 1.1219 1.7791 1.4387 0.2147 -0.0235 -0.1024 92 TYR D O +7794 C CB . TYR D 93 ? 0.8718 1.5222 1.1905 0.2153 -0.0212 -0.1037 92 TYR D CB +7795 C CG . TYR D 93 ? 1.1209 1.7705 1.4381 0.2160 -0.0216 -0.1044 92 TYR D CG +7796 C CD1 . TYR D 93 ? 1.3275 1.9787 1.6434 0.2155 -0.0226 -0.1046 92 TYR D CD1 +7797 C CD2 . TYR D 93 ? 0.8349 1.4819 1.1519 0.2170 -0.0209 -0.1049 92 TYR D CD2 +7798 C CE1 . TYR D 93 ? 1.2159 1.8662 1.5303 0.2161 -0.0228 -0.1053 92 TYR D CE1 +7799 C CE2 . TYR D 93 ? 1.0375 1.6836 1.3530 0.2176 -0.0212 -0.1056 92 TYR D CE2 +7800 C CZ . TYR D 93 ? 1.0604 1.7083 1.3747 0.2171 -0.0222 -0.1058 92 TYR D CZ +7801 O OH . TYR D 93 ? 1.0251 1.6722 1.3381 0.2177 -0.0225 -0.1065 92 TYR D OH +7802 N N . VAL D 94 ? 1.1204 1.7774 1.4386 0.2134 -0.0233 -0.1025 93 VAL D N +7803 C CA . VAL D 94 ? 1.1226 1.7824 1.4399 0.2127 -0.0244 -0.1022 93 VAL D CA +7804 C C . VAL D 94 ? 1.1161 1.7751 1.4327 0.2125 -0.0246 -0.1029 93 VAL D C +7805 O O . VAL D 94 ? 1.1057 1.7634 1.4232 0.2122 -0.0241 -0.1031 93 VAL D O +7806 C CB . VAL D 94 ? 1.1612 1.8235 1.4797 0.2116 -0.0248 -0.1014 93 VAL D CB +7807 C CG1 . VAL D 94 ? 1.0240 1.6892 1.3416 0.2109 -0.0260 -0.1010 93 VAL D CG1 +7808 C CG2 . VAL D 94 ? 1.1141 1.7768 1.4336 0.2117 -0.0244 -0.1007 93 VAL D CG2 +7809 N N . GLN D 95 ? 0.7255 1.3854 1.0408 0.2126 -0.0254 -0.1032 94 GLN D N +7810 C CA . GLN D 95 ? 0.8878 1.5469 1.2024 0.2125 -0.0256 -0.1038 94 GLN D CA +7811 C C . GLN D 95 ? 1.0903 1.7523 1.4045 0.2115 -0.0266 -0.1034 94 GLN D C +7812 O O . GLN D 95 ? 0.8321 1.4959 1.1454 0.2116 -0.0273 -0.1032 94 GLN D O +7813 C CB . GLN D 95 ? 0.8142 1.4714 1.1275 0.2135 -0.0254 -0.1046 94 GLN D CB +7814 C CG . GLN D 95 ? 0.7334 1.3899 1.0461 0.2135 -0.0256 -0.1052 94 GLN D CG +7815 C CD . GLN D 95 ? 0.9769 1.6311 1.2886 0.2145 -0.0253 -0.1060 94 GLN D CD +7816 O OE1 . GLN D 95 ? 0.9407 1.5924 1.2528 0.2152 -0.0245 -0.1064 94 GLN D OE1 +7817 N NE2 . GLN D 95 ? 0.9935 1.6485 1.3041 0.2146 -0.0260 -0.1063 94 GLN D NE2 +7818 N N . GLU D 96 ? 1.0313 1.6938 1.3463 0.2107 -0.0266 -0.1032 95 GLU D N +7819 C CA . GLU D 96 ? 0.7236 1.3888 1.0385 0.2097 -0.0276 -0.1028 95 GLU D CA +7820 C C . GLU D 96 ? 0.8581 1.5225 1.1724 0.2096 -0.0277 -0.1034 95 GLU D C +7821 O O . GLU D 96 ? 0.9529 1.6153 1.2677 0.2097 -0.0271 -0.1039 95 GLU D O +7822 C CB . GLU D 96 ? 1.0461 1.7129 1.3625 0.2086 -0.0276 -0.1021 95 GLU D CB +7823 C CG . GLU D 96 ? 1.4779 2.1466 1.7947 0.2084 -0.0279 -0.1013 95 GLU D CG +7824 C CD . GLU D 96 ? 1.9348 2.6044 2.2533 0.2075 -0.0277 -0.1007 95 GLU D CD +7825 O OE1 . GLU D 96 ? 2.0182 2.6858 2.3376 0.2077 -0.0268 -0.1010 95 GLU D OE1 +7826 O OE2 . GLU D 96 ? 1.8945 2.5668 2.2134 0.2067 -0.0283 -0.0999 95 GLU D OE2 +7827 N N . ARG D 97 ? 0.4979 1.1638 0.8112 0.2095 -0.0286 -0.1034 96 ARG D N +7828 C CA . ARG D 97 ? 0.8872 1.5525 1.2000 0.2094 -0.0288 -0.1039 96 ARG D CA +7829 C C . ARG D 97 ? 1.1253 1.7936 1.4383 0.2084 -0.0298 -0.1033 96 ARG D C +7830 O O . ARG D 97 ? 0.9896 1.6603 1.3028 0.2078 -0.0303 -0.1025 96 ARG D O +7831 C CB . ARG D 97 ? 0.6411 1.3051 0.9527 0.2104 -0.0288 -0.1045 96 ARG D CB +7832 C CG . ARG D 97 ? 1.2246 1.8853 1.5361 0.2113 -0.0278 -0.1053 96 ARG D CG +7833 C CD . ARG D 97 ? 0.9591 1.6183 1.2695 0.2120 -0.0278 -0.1060 96 ARG D CD +7834 N NE . ARG D 97 ? 1.1691 1.8252 1.4793 0.2130 -0.0270 -0.1067 96 ARG D NE +7835 C CZ . ARG D 97 ? 1.0468 1.7022 1.3562 0.2139 -0.0269 -0.1070 96 ARG D CZ +7836 N NH1 . ARG D 97 ? 1.1312 1.7886 1.4399 0.2139 -0.0277 -0.1067 96 ARG D NH1 +7837 N NH2 . ARG D 97 ? 1.0641 1.7168 1.3736 0.2147 -0.0261 -0.1076 96 ARG D NH2 +7838 N N . THR D 98 ? 0.9409 1.6088 1.2537 0.2081 -0.0299 -0.1036 97 THR D N +7839 C CA . THR D 98 ? 1.2424 1.9128 1.5550 0.2073 -0.0308 -0.1032 97 THR D CA +7840 C C . THR D 98 ? 1.0016 1.6706 1.3133 0.2079 -0.0309 -0.1038 97 THR D C +7841 O O . THR D 98 ? 0.8583 1.5247 1.1699 0.2083 -0.0302 -0.1045 97 THR D O +7842 C CB . THR D 98 ? 1.2729 1.9446 1.5866 0.2062 -0.0311 -0.1027 97 THR D CB +7843 O OG1 . THR D 98 ? 0.8829 1.5556 1.1976 0.2057 -0.0309 -0.1022 97 THR D OG1 +7844 C CG2 . THR D 98 ? 0.6354 1.3099 0.9490 0.2053 -0.0321 -0.1021 97 THR D CG2 +7845 N N . ILE D 99 ? 0.7264 1.3970 1.0375 0.2079 -0.0316 -0.1037 98 ILE D N +7846 C CA . ILE D 99 ? 0.8890 1.5583 1.1992 0.2084 -0.0316 -0.1043 98 ILE D CA +7847 C C . ILE D 99 ? 1.1588 1.8302 1.4690 0.2077 -0.0325 -0.1039 98 ILE D C +7848 O O . ILE D 99 ? 0.8771 1.5506 1.1870 0.2076 -0.0332 -0.1034 98 ILE D O +7849 C CB . ILE D 99 ? 0.8332 1.5017 1.1424 0.2095 -0.0316 -0.1047 98 ILE D CB +7850 C CG1 . ILE D 99 ? 0.4573 1.1239 0.7666 0.2101 -0.0308 -0.1049 98 ILE D CG1 +7851 C CG2 . ILE D 99 ? 0.4669 1.1340 0.7753 0.2101 -0.0316 -0.1053 98 ILE D CG2 +7852 C CD1 . ILE D 99 ? 0.6463 1.3126 0.9548 0.2110 -0.0308 -0.1052 98 ILE D CD1 +7853 N N . PHE D 100 ? 0.8561 1.5270 1.1666 0.2073 -0.0324 -0.1040 99 PHE D N +7854 C CA . PHE D 100 ? 0.7180 1.3908 1.0287 0.2066 -0.0332 -0.1037 99 PHE D CA +7855 C C . PHE D 100 ? 0.6739 1.3455 0.9837 0.2074 -0.0332 -0.1042 99 PHE D C +7856 O O . PHE D 100 ? 0.8545 1.5235 1.1640 0.2080 -0.0326 -0.1050 99 PHE D O +7857 C CB . PHE D 100 ? 0.5578 1.2307 0.8693 0.2058 -0.0331 -0.1036 99 PHE D CB +7858 C CG . PHE D 100 ? 1.0116 1.6854 1.3240 0.2051 -0.0330 -0.1031 99 PHE D CG +7859 C CD1 . PHE D 100 ? 1.0327 1.7095 1.3457 0.2041 -0.0338 -0.1022 99 PHE D CD1 +7860 C CD2 . PHE D 100 ? 1.0892 1.7607 1.4019 0.2054 -0.0320 -0.1036 99 PHE D CD2 +7861 C CE1 . PHE D 100 ? 0.9572 1.6349 1.2712 0.2034 -0.0336 -0.1017 99 PHE D CE1 +7862 C CE2 . PHE D 100 ? 0.8245 1.4969 1.1383 0.2047 -0.0319 -0.1032 99 PHE D CE2 +7863 C CZ . PHE D 100 ? 0.7262 1.4017 1.0406 0.2037 -0.0327 -0.1022 99 PHE D CZ +7864 N N . PHE D 101 ? 0.5472 1.2205 0.8566 0.2074 -0.0339 -0.1039 100 PHE D N +7865 C CA . PHE D 101 ? 0.7888 1.4614 1.0977 0.2079 -0.0340 -0.1043 100 PHE D CA +7866 C C . PHE D 101 ? 0.9247 1.5988 1.2342 0.2070 -0.0345 -0.1039 100 PHE D C +7867 O O . PHE D 101 ? 0.8468 1.5234 1.1569 0.2061 -0.0352 -0.1030 100 PHE D O +7868 C CB . PHE D 101 ? 0.4775 1.1513 0.7858 0.2083 -0.0345 -0.1041 100 PHE D CB +7869 C CG . PHE D 101 ? 0.8905 1.5633 1.1983 0.2092 -0.0341 -0.1045 100 PHE D CG +7870 C CD1 . PHE D 101 ? 1.0651 1.7387 1.3732 0.2089 -0.0340 -0.1041 100 PHE D CD1 +7871 C CD2 . PHE D 101 ? 1.0492 1.7201 1.3561 0.2102 -0.0338 -0.1053 100 PHE D CD2 +7872 C CE1 . PHE D 101 ? 0.4949 1.1675 0.8025 0.2096 -0.0336 -0.1044 100 PHE D CE1 +7873 C CE2 . PHE D 101 ? 0.9072 1.5772 1.2136 0.2109 -0.0334 -0.1056 100 PHE D CE2 +7874 C CZ . PHE D 101 ? 0.9987 1.6696 1.3054 0.2106 -0.0333 -0.1052 100 PHE D CZ +7875 N N . LYS D 102 ? 0.7577 1.4301 1.0669 0.2074 -0.0343 -0.1044 101 LYS D N +7876 C CA . LYS D 102 ? 1.2275 1.9011 1.5373 0.2066 -0.0347 -0.1040 101 LYS D CA +7877 C C . LYS D 102 ? 1.3397 2.0159 1.6497 0.2062 -0.0356 -0.1033 101 LYS D C +7878 O O . LYS D 102 ? 0.8204 1.4963 1.1298 0.2069 -0.0357 -0.1036 101 LYS D O +7879 C CB . LYS D 102 ? 0.9195 1.5906 1.2290 0.2071 -0.0341 -0.1048 101 LYS D CB +7880 C CG . LYS D 102 ? 1.1174 1.7895 1.4275 0.2062 -0.0345 -0.1045 101 LYS D CG +7881 C CD . LYS D 102 ? 1.4299 2.0997 1.7396 0.2069 -0.0340 -0.1052 101 LYS D CD +7882 C CE . LYS D 102 ? 1.3134 1.9833 1.6236 0.2062 -0.0340 -0.1051 101 LYS D CE +7883 N NZ . LYS D 102 ? 1.4300 2.0999 1.7402 0.2063 -0.0343 -0.1051 101 LYS D NZ +7884 N N . ASP D 103 ? 1.0485 1.7272 1.3592 0.2051 -0.0363 -0.1025 102 ASP D N +7885 C CA . ASP D 103 ? 1.1570 1.8385 1.4681 0.2046 -0.0372 -0.1017 102 ASP D CA +7886 C C . ASP D 103 ? 1.1066 1.7896 1.4176 0.2047 -0.0375 -0.1013 102 ASP D C +7887 O O . ASP D 103 ? 1.0344 1.7186 1.3453 0.2049 -0.0380 -0.1010 102 ASP D O +7888 C CB . ASP D 103 ? 1.3585 2.0393 1.6693 0.2051 -0.0373 -0.1020 102 ASP D CB +7889 C CG . ASP D 103 ? 1.4803 2.1602 1.7914 0.2048 -0.0371 -0.1022 102 ASP D CG +7890 O OD1 . ASP D 103 ? 1.3823 2.0627 1.6939 0.2040 -0.0371 -0.1019 102 ASP D OD1 +7891 O OD2 . ASP D 103 ? 1.4178 2.0963 1.7286 0.2054 -0.0369 -0.1026 102 ASP D OD2 +7892 N N . ASP D 104 ? 0.9064 1.5892 1.2174 0.2047 -0.0372 -0.1013 103 ASP D N +7893 C CA . ASP D 104 ? 0.7496 1.4335 1.0603 0.2050 -0.0374 -0.1010 103 ASP D CA +7894 C C . ASP D 104 ? 0.9066 1.5906 1.2175 0.2048 -0.0372 -0.1009 103 ASP D C +7895 O O . ASP D 104 ? 0.6283 1.3118 0.9397 0.2043 -0.0369 -0.1009 103 ASP D O +7896 C CB . ASP D 104 ? 0.6750 1.3570 0.9848 0.2062 -0.0370 -0.1018 103 ASP D CB +7897 C CG . ASP D 104 ? 1.3341 2.0173 1.6436 0.2065 -0.0373 -0.1016 103 ASP D CG +7898 O OD1 . ASP D 104 ? 0.7572 1.4427 1.0672 0.2058 -0.0377 -0.1008 103 ASP D OD1 +7899 O OD2 . ASP D 104 ? 2.4314 3.1133 2.7401 0.2075 -0.0370 -0.1022 103 ASP D OD2 +7900 N N . GLY D 105 ? 0.8677 1.5524 1.1783 0.2051 -0.0372 -0.1007 104 GLY D N +7901 C CA . GLY D 105 ? 0.4806 1.1659 0.7915 0.2049 -0.0371 -0.1004 104 GLY D CA +7902 C C . GLY D 105 ? 0.9710 1.6536 1.2816 0.2055 -0.0362 -0.1011 104 GLY D C +7903 O O . GLY D 105 ? 0.8878 1.5678 1.1979 0.2061 -0.0356 -0.1019 104 GLY D O +7904 N N . ASN D 106 ? 0.7642 1.4473 1.0751 0.2054 -0.0360 -0.1008 105 ASN D N +7905 C CA . ASN D 106 ? 0.8653 1.5459 1.1760 0.2059 -0.0351 -0.1014 105 ASN D CA +7906 C C . ASN D 106 ? 1.1303 1.8111 1.4408 0.2064 -0.0349 -0.1013 105 ASN D C +7907 O O . ASN D 106 ? 1.0840 1.7671 1.3947 0.2059 -0.0355 -0.1006 105 ASN D O +7908 C CB . ASN D 106 ? 0.9770 1.6576 1.2887 0.2051 -0.0349 -0.1012 105 ASN D CB +7909 C CG . ASN D 106 ? 0.9771 1.6607 1.2896 0.2040 -0.0356 -0.1002 105 ASN D CG +7910 O OD1 . ASN D 106 ? 0.8298 1.5139 1.1426 0.2040 -0.0355 -0.0999 105 ASN D OD1 +7911 N ND2 . ASN D 106 ? 0.7504 1.4360 1.0635 0.2031 -0.0363 -0.0996 105 ASN D ND2 +7912 N N . TYR D 107 ? 0.8260 1.5041 1.1360 0.2073 -0.0341 -0.1020 106 TYR D N +7913 C CA . TYR D 107 ? 0.7927 1.4707 1.1026 0.2077 -0.0338 -0.1019 106 TYR D CA +7914 C C . TYR D 107 ? 0.9166 1.5940 1.2275 0.2073 -0.0333 -0.1018 106 TYR D C +7915 O O . TYR D 107 ? 0.7374 1.4130 1.0486 0.2072 -0.0328 -0.1021 106 TYR D O +7916 C CB . TYR D 107 ? 0.7391 1.4146 1.0481 0.2089 -0.0332 -0.1028 106 TYR D CB +7917 C CG . TYR D 107 ? 0.7868 1.4625 1.0948 0.2095 -0.0336 -0.1031 106 TYR D CG +7918 C CD1 . TYR D 107 ? 0.7547 1.4332 1.0628 0.2090 -0.0344 -0.1025 106 TYR D CD1 +7919 C CD2 . TYR D 107 ? 0.8997 1.5729 1.2069 0.2105 -0.0331 -0.1040 106 TYR D CD2 +7920 C CE1 . TYR D 107 ? 0.5547 1.2334 0.8620 0.2095 -0.0347 -0.1028 106 TYR D CE1 +7921 C CE2 . TYR D 107 ? 0.4261 1.0996 0.7326 0.2110 -0.0334 -0.1043 106 TYR D CE2 +7922 C CZ . TYR D 107 ? 0.8357 1.5118 1.1422 0.2105 -0.0342 -0.1038 106 TYR D CZ +7923 O OH . TYR D 107 ? 0.8139 1.4901 1.1197 0.2111 -0.0345 -0.1041 106 TYR D OH +7924 N N . LYS D 108 ? 0.7732 1.4520 1.0846 0.2070 -0.0334 -0.1012 107 LYS D N +7925 C CA . LYS D 108 ? 0.8020 1.4799 1.1142 0.2069 -0.0328 -0.1011 107 LYS D CA +7926 C C . LYS D 108 ? 1.0268 1.7042 1.3387 0.2076 -0.0324 -0.1011 107 LYS D C +7927 O O . LYS D 108 ? 1.0858 1.7652 1.3975 0.2075 -0.0329 -0.1005 107 LYS D O +7928 C CB . LYS D 108 ? 0.8693 1.5495 1.1826 0.2056 -0.0332 -0.1002 107 LYS D CB +7929 C CG . LYS D 108 ? 1.0581 1.7384 1.3719 0.2049 -0.0334 -0.1003 107 LYS D CG +7930 C CD . LYS D 108 ? 1.0355 1.7185 1.3503 0.2036 -0.0341 -0.0994 107 LYS D CD +7931 C CE . LYS D 108 ? 1.1669 1.8497 1.4824 0.2029 -0.0340 -0.0995 107 LYS D CE +7932 N NZ . LYS D 108 ? 1.1529 1.8332 1.4689 0.2032 -0.0330 -0.1001 107 LYS D NZ +7933 N N . THR D 109 ? 1.0236 1.6982 1.3354 0.2084 -0.0315 -0.1017 108 THR D N +7934 C CA . THR D 109 ? 0.9000 1.5737 1.2114 0.2093 -0.0311 -0.1018 108 THR D CA +7935 C C . THR D 109 ? 0.8894 1.5621 1.2018 0.2093 -0.0304 -0.1016 108 THR D C +7936 O O . THR D 109 ? 0.6053 1.2771 0.9186 0.2088 -0.0300 -0.1017 108 THR D O +7937 C CB . THR D 109 ? 0.8426 1.5138 1.1529 0.2104 -0.0307 -0.1028 108 THR D CB +7938 O OG1 . THR D 109 ? 0.8199 1.4884 1.1306 0.2107 -0.0299 -0.1034 108 THR D OG1 +7939 C CG2 . THR D 109 ? 0.9644 1.6364 1.2738 0.2104 -0.0314 -0.1030 108 THR D CG2 +7940 N N . ARG D 110 ? 0.8044 1.4772 1.1167 0.2098 -0.0302 -0.1014 109 ARG D N +7941 C CA . ARG D 110 ? 0.8141 1.4856 1.1273 0.2100 -0.0294 -0.1013 109 ARG D CA +7942 C C . ARG D 110 ? 0.9088 1.5795 1.2214 0.2110 -0.0291 -0.1015 109 ARG D C +7943 O O . ARG D 110 ? 0.8034 1.4759 1.1155 0.2110 -0.0296 -0.1010 109 ARG D O +7944 C CB . ARG D 110 ? 0.8612 1.5349 1.1756 0.2090 -0.0297 -0.1003 109 ARG D CB +7945 C CG . ARG D 110 ? 1.1173 1.7898 1.4328 0.2093 -0.0289 -0.1001 109 ARG D CG +7946 C CD . ARG D 110 ? 0.7903 1.4651 1.1069 0.2085 -0.0291 -0.0992 109 ARG D CD +7947 N NE . ARG D 110 ? 1.0587 1.7323 1.3765 0.2087 -0.0283 -0.0990 109 ARG D NE +7948 C CZ . ARG D 110 ? 1.2425 1.9158 1.5603 0.2093 -0.0279 -0.0988 109 ARG D CZ +7949 N NH1 . ARG D 110 ? 1.3026 1.9769 1.6193 0.2098 -0.0284 -0.0987 109 ARG D NH1 +7950 N NH2 . ARG D 110 ? 0.9965 1.6685 1.3155 0.2095 -0.0271 -0.0986 109 ARG D NH2 +7951 N N . ALA D 111 ? 1.0489 1.7166 1.3614 0.2118 -0.0283 -0.1021 110 ALA D N +7952 C CA . ALA D 111 ? 0.7708 1.4373 1.0827 0.2129 -0.0279 -0.1024 110 ALA D CA +7953 C C . ALA D 111 ? 0.9882 1.6533 1.3012 0.2131 -0.0271 -0.1022 110 ALA D C +7954 O O . ALA D 111 ? 0.8850 1.5490 1.1992 0.2128 -0.0265 -0.1022 110 ALA D O +7955 C CB . ALA D 111 ? 0.9242 1.5885 1.2351 0.2137 -0.0277 -0.1034 110 ALA D CB +7956 N N . GLU D 112 ? 0.7215 1.3868 1.0344 0.2137 -0.0269 -0.1019 111 GLU D N +7957 C CA . GLU D 112 ? 1.0090 1.6726 1.3229 0.2142 -0.0260 -0.1018 111 GLU D CA +7958 C C . GLU D 112 ? 1.2037 1.8650 1.5167 0.2154 -0.0256 -0.1025 111 GLU D C +7959 O O . GLU D 112 ? 1.1728 1.8350 1.4847 0.2159 -0.0260 -0.1026 111 GLU D O +7960 C CB . GLU D 112 ? 1.2215 1.8870 1.5361 0.2140 -0.0261 -0.1009 111 GLU D CB +7961 C CG . GLU D 112 ? 1.7202 2.3878 2.0359 0.2128 -0.0264 -0.1002 111 GLU D CG +7962 C CD . GLU D 112 ? 1.7445 2.4141 2.0609 0.2126 -0.0266 -0.0992 111 GLU D CD +7963 O OE1 . GLU D 112 ? 1.3378 2.0075 1.6537 0.2133 -0.0265 -0.0991 111 GLU D OE1 +7964 O OE2 . GLU D 112 ? 1.6978 2.3690 2.0154 0.2117 -0.0268 -0.0986 111 GLU D OE2 +7965 N N . VAL D 113 ? 1.1003 1.7588 1.4138 0.2159 -0.0248 -0.1031 112 VAL D N +7966 C CA . VAL D 113 ? 0.9605 1.6168 1.2734 0.2169 -0.0243 -0.1037 112 VAL D CA +7967 C C . VAL D 113 ? 0.9783 1.6332 1.2924 0.2175 -0.0234 -0.1034 112 VAL D C +7968 O O . VAL D 113 ? 0.8235 1.4770 1.1389 0.2173 -0.0227 -0.1032 112 VAL D O +7969 C CB . VAL D 113 ? 0.5919 1.2457 0.9044 0.2172 -0.0239 -0.1046 112 VAL D CB +7970 C CG1 . VAL D 113 ? 1.0672 1.7192 1.3790 0.2183 -0.0236 -0.1052 112 VAL D CG1 +7971 C CG2 . VAL D 113 ? 1.0158 1.6710 1.3275 0.2166 -0.0247 -0.1048 112 VAL D CG2 +7972 N N . LYS D 114 ? 0.7221 1.3773 1.0357 0.2181 -0.0234 -0.1032 113 LYS D N +7973 C CA . LYS D 114 ? 0.9457 1.5999 1.2604 0.2186 -0.0227 -0.1028 113 LYS D CA +7974 C C . LYS D 114 ? 1.1016 1.7556 1.4154 0.2196 -0.0227 -0.1030 113 LYS D C +7975 O O . LYS D 114 ? 0.8670 1.5217 1.1793 0.2198 -0.0233 -0.1034 113 LYS D O +7976 C CB . LYS D 114 ? 1.2913 1.9475 1.6071 0.2179 -0.0227 -0.1018 113 LYS D CB +7977 C CG . LYS D 114 ? 1.2978 1.9571 1.6128 0.2176 -0.0237 -0.1013 113 LYS D CG +7978 C CD . LYS D 114 ? 1.0971 1.7584 1.4136 0.2169 -0.0237 -0.1003 113 LYS D CD +7979 C CE . LYS D 114 ? 1.3678 2.0321 1.6835 0.2166 -0.0245 -0.0997 113 LYS D CE +7980 N NZ . LYS D 114 ? 1.1281 1.7943 1.4429 0.2158 -0.0254 -0.0998 113 LYS D NZ +7981 N N . PHE D 115 ? 0.8507 1.5035 1.1655 0.2201 -0.0220 -0.1027 114 PHE D N +7982 C CA . PHE D 115 ? 0.9683 1.6207 1.2824 0.2211 -0.0219 -0.1028 114 PHE D CA +7983 C C . PHE D 115 ? 0.9477 1.6027 1.2618 0.2210 -0.0223 -0.1020 114 PHE D C +7984 O O . PHE D 115 ? 1.0674 1.7233 1.3827 0.2205 -0.0221 -0.1012 114 PHE D O +7985 C CB . PHE D 115 ? 1.3012 1.9509 1.6165 0.2218 -0.0208 -0.1029 114 PHE D CB +7986 C CG . PHE D 115 ? 1.3663 2.0134 1.6809 0.2225 -0.0205 -0.1038 114 PHE D CG +7987 C CD1 . PHE D 115 ? 1.1970 1.8437 1.5106 0.2233 -0.0207 -0.1043 114 PHE D CD1 +7988 C CD2 . PHE D 115 ? 1.0559 1.7011 1.3711 0.2223 -0.0201 -0.1043 114 PHE D CD2 +7989 C CE1 . PHE D 115 ? 0.9581 1.6024 1.2711 0.2239 -0.0204 -0.1052 114 PHE D CE1 +7990 C CE2 . PHE D 115 ? 0.8860 1.5289 1.2007 0.2229 -0.0198 -0.1051 114 PHE D CE2 +7991 C CZ . PHE D 115 ? 0.9107 1.5530 1.2243 0.2237 -0.0199 -0.1056 114 PHE D CZ +7992 N N . GLU D 116 ? 0.8571 1.5133 1.1697 0.2214 -0.0229 -0.1023 115 GLU D N +7993 C CA . GLU D 116 ? 0.9515 1.6100 1.2639 0.2214 -0.0233 -0.1015 115 GLU D CA +7994 C C . GLU D 116 ? 0.8904 1.5480 1.2024 0.2224 -0.0230 -0.1018 115 GLU D C +7995 O O . GLU D 116 ? 0.8100 1.4684 1.1205 0.2228 -0.0235 -0.1022 115 GLU D O +7996 C CB . GLU D 116 ? 1.0151 1.6764 1.3263 0.2208 -0.0243 -0.1015 115 GLU D CB +7997 C CG . GLU D 116 ? 1.1457 1.8084 1.4576 0.2197 -0.0246 -0.1011 115 GLU D CG +7998 C CD . GLU D 116 ? 1.6567 2.3224 1.9677 0.2191 -0.0256 -0.1008 115 GLU D CD +7999 O OE1 . GLU D 116 ? 1.6120 2.2787 1.9218 0.2196 -0.0260 -0.1009 115 GLU D OE1 +8000 O OE2 . GLU D 116 ? 1.4402 2.1073 1.7517 0.2182 -0.0259 -0.1004 115 GLU D OE2 +8001 N N . GLY D 117 ? 0.9553 1.6111 1.2686 0.2229 -0.0221 -0.1015 116 GLY D N +8002 C CA . GLY D 117 ? 0.8908 1.5453 1.2039 0.2239 -0.0217 -0.1017 116 GLY D CA +8003 C C . GLY D 117 ? 1.1729 1.8247 1.4857 0.2244 -0.0214 -0.1027 116 GLY D C +8004 O O . GLY D 117 ? 0.8102 1.4600 1.1239 0.2242 -0.0208 -0.1028 116 GLY D O +8005 N N . ASP D 118 ? 1.4786 2.1303 1.7900 0.2251 -0.0217 -0.1033 117 ASP D N +8006 C CA . ASP D 118 ? 1.3941 2.0433 1.7050 0.2256 -0.0214 -0.1042 117 ASP D CA +8007 C C . ASP D 118 ? 1.2050 1.8546 1.5149 0.2251 -0.0220 -0.1049 117 ASP D C +8008 O O . ASP D 118 ? 1.2255 1.8731 1.5349 0.2254 -0.0219 -0.1057 117 ASP D O +8009 C CB . ASP D 118 ? 1.3861 2.0349 1.6962 0.2265 -0.0215 -0.1047 117 ASP D CB +8010 C CG . ASP D 118 ? 1.7170 2.3681 2.0253 0.2265 -0.0224 -0.1050 117 ASP D CG +8011 O OD1 . ASP D 118 ? 1.5184 2.1721 1.8265 0.2260 -0.0230 -0.1044 117 ASP D OD1 +8012 O OD2 . ASP D 118 ? 1.4905 2.1409 1.7977 0.2271 -0.0226 -0.1058 117 ASP D OD2 +8013 N N . THR D 119 ? 1.1729 1.8248 1.4824 0.2243 -0.0227 -0.1046 118 THR D N +8014 C CA . THR D 119 ? 1.0888 1.7412 1.3973 0.2238 -0.0233 -0.1051 118 THR D CA +8015 C C . THR D 119 ? 0.9436 1.5959 1.2530 0.2229 -0.0232 -0.1049 118 THR D C +8016 O O . THR D 119 ? 0.9372 1.5904 1.2477 0.2224 -0.0231 -0.1041 118 THR D O +8017 C CB . THR D 119 ? 0.8060 1.4612 1.1131 0.2236 -0.0243 -0.1051 118 THR D CB +8018 O OG1 . THR D 119 ? 0.9707 1.6257 1.2769 0.2245 -0.0243 -0.1055 118 THR D OG1 +8019 C CG2 . THR D 119 ? 0.6777 1.3335 0.9839 0.2231 -0.0249 -0.1057 118 THR D CG2 +8020 N N . LEU D 120 ? 0.8865 1.5377 1.1954 0.2228 -0.0233 -0.1056 119 LEU D N +8021 C CA . LEU D 120 ? 0.5186 1.1698 0.8280 0.2219 -0.0234 -0.1055 119 LEU D CA +8022 C C . LEU D 120 ? 0.9525 1.6063 1.2609 0.2213 -0.0244 -0.1055 119 LEU D C +8023 O O . LEU D 120 ? 0.5664 1.2204 0.8736 0.2215 -0.0249 -0.1061 119 LEU D O +8024 C CB . LEU D 120 ? 0.5102 1.1586 0.8197 0.2222 -0.0229 -0.1063 119 LEU D CB +8025 C CG . LEU D 120 ? 0.4448 1.0928 0.7550 0.2214 -0.0228 -0.1063 119 LEU D CG +8026 C CD1 . LEU D 120 ? 1.4400 2.0848 1.7510 0.2219 -0.0219 -0.1068 119 LEU D CD1 +8027 C CD2 . LEU D 120 ? 0.6545 1.3037 0.9636 0.2209 -0.0236 -0.1067 119 LEU D CD2 +8028 N N . VAL D 121 ? 0.8296 1.4855 1.1386 0.2204 -0.0247 -0.1047 120 VAL D N +8029 C CA . VAL D 121 ? 0.8010 1.4596 1.1092 0.2198 -0.0256 -0.1045 120 VAL D CA +8030 C C . VAL D 121 ? 1.0266 1.6856 1.3353 0.2188 -0.0258 -0.1044 120 VAL D C +8031 O O . VAL D 121 ? 0.7545 1.4128 1.0645 0.2184 -0.0253 -0.1040 120 VAL D O +8032 C CB . VAL D 121 ? 0.9182 1.5794 1.2265 0.2195 -0.0260 -0.1036 120 VAL D CB +8033 C CG1 . VAL D 121 ? 0.6472 1.3081 0.9550 0.2205 -0.0258 -0.1037 120 VAL D CG1 +8034 C CG2 . VAL D 121 ? 1.2242 1.8860 1.5341 0.2189 -0.0256 -0.1028 120 VAL D CG2 +8035 N N . ASN D 122 ? 0.7788 1.4387 1.0866 0.2185 -0.0264 -0.1047 121 ASN D N +8036 C CA . ASN D 122 ? 0.8566 1.5174 1.1648 0.2176 -0.0268 -0.1046 121 ASN D CA +8037 C C . ASN D 122 ? 1.1156 1.7796 1.4234 0.2169 -0.0277 -0.1039 121 ASN D C +8038 O O . ASN D 122 ? 0.7346 1.3999 1.0414 0.2171 -0.0283 -0.1042 121 ASN D O +8039 C CB . ASN D 122 ? 0.4791 1.1384 0.7866 0.2178 -0.0269 -0.1054 121 ASN D CB +8040 C CG . ASN D 122 ? 0.7369 1.3965 1.0450 0.2169 -0.0270 -0.1053 121 ASN D CG +8041 O OD1 . ASN D 122 ? 1.1945 1.8546 1.5036 0.2163 -0.0268 -0.1047 121 ASN D OD1 +8042 N ND2 . ASN D 122 ? 0.8461 1.5054 1.1535 0.2168 -0.0273 -0.1058 121 ASN D ND2 +8043 N N . ARG D 123 ? 0.9355 1.6010 1.2444 0.2161 -0.0277 -0.1031 122 ARG D N +8044 C CA . ARG D 123 ? 0.8213 1.4900 1.1301 0.2154 -0.0285 -0.1024 122 ARG D CA +8045 C C . ARG D 123 ? 0.9449 1.6147 1.2541 0.2143 -0.0290 -0.1022 122 ARG D C +8046 O O . ARG D 123 ? 0.6688 1.3382 0.9792 0.2138 -0.0287 -0.1019 122 ARG D O +8047 C CB . ARG D 123 ? 0.9220 1.5920 1.2316 0.2152 -0.0284 -0.1016 122 ARG D CB +8048 C CG . ARG D 123 ? 0.8838 1.5541 1.1928 0.2160 -0.0284 -0.1016 122 ARG D CG +8049 C CD . ARG D 123 ? 1.0387 1.7108 1.3484 0.2157 -0.0284 -0.1006 122 ARG D CD +8050 N NE . ARG D 123 ? 1.2595 1.9308 1.5692 0.2166 -0.0279 -0.1006 122 ARG D NE +8051 C CZ . ARG D 123 ? 1.3761 2.0481 1.6847 0.2172 -0.0281 -0.1008 122 ARG D CZ +8052 N NH1 . ARG D 123 ? 1.0916 1.7651 1.3991 0.2171 -0.0288 -0.1011 122 ARG D NH1 +8053 N NH2 . ARG D 123 ? 1.1828 1.8539 1.4915 0.2179 -0.0277 -0.1008 122 ARG D NH2 +8054 N N . ILE D 124 ? 0.9497 1.6210 1.2581 0.2141 -0.0297 -0.1023 123 ILE D N +8055 C CA . ILE D 124 ? 0.8072 1.4792 1.1159 0.2133 -0.0301 -0.1023 123 ILE D CA +8056 C C . ILE D 124 ? 0.9285 1.6038 1.2373 0.2124 -0.0310 -0.1015 123 ILE D C +8057 O O . ILE D 124 ? 0.6304 1.3073 0.9384 0.2126 -0.0314 -0.1014 123 ILE D O +8058 C CB . ILE D 124 ? 1.0840 1.7544 1.3917 0.2137 -0.0301 -0.1032 123 ILE D CB +8059 C CG1 . ILE D 124 ? 0.8788 1.5464 1.1860 0.2148 -0.0294 -0.1039 123 ILE D CG1 +8060 C CG2 . ILE D 124 ? 0.7971 1.4672 1.1054 0.2131 -0.0302 -0.1032 123 ILE D CG2 +8061 C CD1 . ILE D 124 ? 1.0232 1.6895 1.3294 0.2154 -0.0295 -0.1048 123 ILE D CD1 +8062 N N . GLU D 125 ? 1.0605 1.7367 1.3702 0.2114 -0.0312 -0.1010 124 GLU D N +8063 C CA . GLU D 125 ? 0.9038 1.5829 1.2137 0.2105 -0.0320 -0.1004 124 GLU D CA +8064 C C . GLU D 125 ? 0.8933 1.5720 1.2032 0.2101 -0.0322 -0.1007 124 GLU D C +8065 O O . GLU D 125 ? 0.9865 1.6637 1.2971 0.2098 -0.0318 -0.1009 124 GLU D O +8066 C CB . GLU D 125 ? 0.8855 1.5663 1.1966 0.2096 -0.0321 -0.0994 124 GLU D CB +8067 C CG . GLU D 125 ? 1.3676 2.0490 1.6790 0.2100 -0.0319 -0.0990 124 GLU D CG +8068 C CD . GLU D 125 ? 1.6572 2.3405 1.9699 0.2091 -0.0320 -0.0981 124 GLU D CD +8069 O OE1 . GLU D 125 ? 1.9222 2.6046 2.2359 0.2086 -0.0316 -0.0980 124 GLU D OE1 +8070 O OE2 . GLU D 125 ? 1.4028 2.0885 1.7156 0.2088 -0.0325 -0.0974 124 GLU D OE2 +8071 N N . LEU D 126 ? 0.7746 1.4546 1.0838 0.2100 -0.0329 -0.1007 125 LEU D N +8072 C CA . LEU D 126 ? 0.9313 1.6112 1.2406 0.2095 -0.0332 -0.1010 125 LEU D CA +8073 C C . LEU D 126 ? 0.9659 1.6488 1.2755 0.2086 -0.0341 -0.1002 125 LEU D C +8074 O O . LEU D 126 ? 0.9341 1.6190 1.2434 0.2086 -0.0345 -0.0998 125 LEU D O +8075 C CB . LEU D 126 ? 0.6665 1.3444 0.9747 0.2104 -0.0330 -0.1019 125 LEU D CB +8076 C CG . LEU D 126 ? 0.5456 1.2237 0.8535 0.2102 -0.0334 -0.1022 125 LEU D CG +8077 C CD1 . LEU D 126 ? 0.7336 1.4087 1.0408 0.2111 -0.0329 -0.1032 125 LEU D CD1 +8078 C CD2 . LEU D 126 ? 0.8950 1.5753 1.2024 0.2101 -0.0341 -0.1019 125 LEU D CD2 +8079 N N . LYS D 127 ? 0.9997 1.6831 1.3099 0.2078 -0.0343 -0.1000 126 LYS D N +8080 C CA . LYS D 127 ? 0.7416 1.4279 1.0523 0.2068 -0.0352 -0.0992 126 LYS D CA +8081 C C . LYS D 127 ? 0.8685 1.5550 1.1793 0.2064 -0.0355 -0.0994 126 LYS D C +8082 O O . LYS D 127 ? 1.1312 1.8174 1.4428 0.2057 -0.0354 -0.0993 126 LYS D O +8083 C CB . LYS D 127 ? 0.8968 1.5848 1.2087 0.2059 -0.0353 -0.0984 126 LYS D CB +8084 C CG . LYS D 127 ? 1.2201 1.9113 1.5327 0.2048 -0.0362 -0.0975 126 LYS D CG +8085 C CD . LYS D 127 ? 1.3730 2.0661 1.6865 0.2041 -0.0364 -0.0966 126 LYS D CD +8086 C CE . LYS D 127 ? 1.2597 1.9560 1.5740 0.2030 -0.0373 -0.0957 126 LYS D CE +8087 N NZ . LYS D 127 ? 1.1159 1.8128 1.4293 0.2033 -0.0378 -0.0958 126 LYS D NZ +8088 N N . GLY D 128 ? 0.9464 1.6333 1.2566 0.2067 -0.0359 -0.0996 127 GLY D N +8089 C CA . GLY D 128 ? 0.9158 1.6027 1.2260 0.2063 -0.0362 -0.0997 127 GLY D CA +8090 C C . GLY D 128 ? 1.1730 1.8631 1.4840 0.2053 -0.0371 -0.0987 127 GLY D C +8091 O O . GLY D 128 ? 1.3248 2.0169 1.6358 0.2051 -0.0376 -0.0982 127 GLY D O +8092 N N . ILE D 129 ? 1.3388 2.0290 1.6503 0.2046 -0.0373 -0.0986 128 ILE D N +8093 C CA . ILE D 129 ? 1.0753 1.7684 1.3877 0.2035 -0.0382 -0.0977 128 ILE D CA +8094 C C . ILE D 129 ? 0.7970 1.4896 1.1094 0.2032 -0.0384 -0.0979 128 ILE D C +8095 O O . ILE D 129 ? 1.1224 1.8126 1.4345 0.2037 -0.0378 -0.0986 128 ILE D O +8096 C CB . ILE D 129 ? 0.8701 1.5646 1.1836 0.2024 -0.0383 -0.0969 128 ILE D CB +8097 C CG1 . ILE D 129 ? 1.4498 2.1451 1.7634 0.2025 -0.0382 -0.0966 128 ILE D CG1 +8098 C CG2 . ILE D 129 ? 1.7924 2.4897 2.1068 0.2012 -0.0392 -0.0960 128 ILE D CG2 +8099 C CD1 . ILE D 129 ? 1.3565 2.0496 1.6700 0.2030 -0.0374 -0.0971 128 ILE D CD1 +8100 N N . ASP D 130 ? 1.1649 1.8600 1.4778 0.2026 -0.0392 -0.0972 129 ASP D N +8101 C CA . ASP D 130 ? 1.2569 1.9522 1.5702 0.2021 -0.0395 -0.0971 129 ASP D CA +8102 C C . ASP D 130 ? 0.7799 1.4734 1.0923 0.2030 -0.0393 -0.0979 129 ASP D C +8103 O O . ASP D 130 ? 0.7023 1.3950 1.0148 0.2029 -0.0393 -0.0981 129 ASP D O +8104 C CB . ASP D 130 ? 1.0191 1.7134 1.3329 0.2016 -0.0392 -0.0973 129 ASP D CB +8105 C CG . ASP D 130 ? 1.2833 1.9797 1.5981 0.2005 -0.0396 -0.0964 129 ASP D CG +8106 O OD1 . ASP D 130 ? 1.0612 1.7604 1.3767 0.1997 -0.0404 -0.0955 129 ASP D OD1 +8107 O OD2 . ASP D 130 ? 1.2538 1.9490 1.5688 0.2003 -0.0391 -0.0967 129 ASP D OD2 +8108 N N . PHE D 131 ? 0.5302 1.2232 0.8419 0.2039 -0.0391 -0.0983 130 PHE D N +8109 C CA . PHE D 131 ? 1.0630 1.7544 1.3739 0.2048 -0.0389 -0.0990 130 PHE D CA +8110 C C . PHE D 131 ? 0.5413 1.2349 0.8527 0.2043 -0.0397 -0.0983 130 PHE D C +8111 O O . PHE D 131 ? 0.8466 1.5429 1.1588 0.2036 -0.0403 -0.0974 130 PHE D O +8112 C CB . PHE D 131 ? 0.9325 1.6221 1.2424 0.2059 -0.0384 -0.0997 130 PHE D CB +8113 C CG . PHE D 131 ? 0.6936 1.3806 1.0031 0.2064 -0.0376 -0.1005 130 PHE D CG +8114 C CD1 . PHE D 131 ? 1.0381 1.7253 1.3478 0.2062 -0.0373 -0.1002 130 PHE D CD1 +8115 C CD2 . PHE D 131 ? 0.8274 1.5115 1.1362 0.2072 -0.0370 -0.1014 130 PHE D CD2 +8116 C CE1 . PHE D 131 ? 0.4887 1.1734 0.7981 0.2067 -0.0366 -0.1008 130 PHE D CE1 +8117 C CE2 . PHE D 131 ? 0.7014 1.3830 1.0099 0.2077 -0.0362 -0.1021 130 PHE D CE2 +8118 C CZ . PHE D 131 ? 1.0502 1.7321 1.3590 0.2074 -0.0360 -0.1018 130 PHE D CZ +8119 N N . LYS D 132 ? 0.6710 1.3635 0.9822 0.2048 -0.0396 -0.0988 131 LYS D N +8120 C CA . LYS D 132 ? 0.7834 1.4777 1.0951 0.2045 -0.0403 -0.0983 131 LYS D CA +8121 C C . LYS D 132 ? 0.7242 1.4185 1.0353 0.2053 -0.0403 -0.0986 131 LYS D C +8122 O O . LYS D 132 ? 1.7150 2.4070 2.0254 0.2062 -0.0398 -0.0994 131 LYS D O +8123 C CB . LYS D 132 ? 0.5536 1.2467 0.8654 0.2045 -0.0402 -0.0986 131 LYS D CB +8124 C CG . LYS D 132 ? 0.8094 1.5016 1.1214 0.2040 -0.0400 -0.0987 131 LYS D CG +8125 C CD . LYS D 132 ? 0.9715 1.6625 1.2835 0.2041 -0.0399 -0.0990 131 LYS D CD +8126 C CE . LYS D 132 ? 1.1244 1.8155 1.4370 0.2033 -0.0400 -0.0988 131 LYS D CE +8127 N NZ . LYS D 132 ? 1.1514 1.8408 1.4638 0.2036 -0.0397 -0.0993 131 LYS D NZ +8128 N N . GLU D 133 ? 1.0814 1.7782 1.3930 0.2050 -0.0408 -0.0978 132 GLU D N +8129 C CA . GLU D 133 ? 1.3916 2.0887 1.7028 0.2057 -0.0408 -0.0981 132 GLU D CA +8130 C C . GLU D 133 ? 1.1933 1.8889 1.5042 0.2065 -0.0407 -0.0987 132 GLU D C +8131 O O . GLU D 133 ? 0.9692 1.6644 1.2796 0.2073 -0.0405 -0.0992 132 GLU D O +8132 C CB . GLU D 133 ? 1.0344 1.7348 1.3465 0.2051 -0.0415 -0.0970 132 GLU D CB +8133 C CG . GLU D 133 ? 2.3917 3.0936 2.7039 0.2047 -0.0416 -0.0965 132 GLU D CG +8134 C CD . GLU D 133 ? 2.0916 2.7931 2.4030 0.2056 -0.0413 -0.0970 132 GLU D CD +8135 O OE1 . GLU D 133 ? 1.9793 2.6811 2.2905 0.2062 -0.0414 -0.0972 132 GLU D OE1 +8136 O OE2 . GLU D 133 ? 1.4889 2.1899 1.7999 0.2057 -0.0410 -0.0971 132 GLU D OE2 +8137 N N . ASP D 134 ? 0.9610 1.6558 1.2721 0.2062 -0.0407 -0.0988 133 ASP D N +8138 C CA . ASP D 134 ? 0.9582 1.6515 1.2691 0.2069 -0.0405 -0.0994 133 ASP D CA +8139 C C . ASP D 134 ? 1.2429 1.9331 1.5531 0.2075 -0.0398 -0.1004 133 ASP D C +8140 O O . ASP D 134 ? 1.2790 1.9676 1.5889 0.2080 -0.0396 -0.1010 133 ASP D O +8141 C CB . ASP D 134 ? 1.7555 2.4505 2.0675 0.2062 -0.0411 -0.0986 133 ASP D CB +8142 C CG . ASP D 134 ? 2.0658 2.7620 2.3786 0.2052 -0.0414 -0.0979 133 ASP D CG +8143 O OD1 . ASP D 134 ? 2.0112 2.7079 2.3239 0.2047 -0.0414 -0.0976 133 ASP D OD1 +8144 O OD2 . ASP D 134 ? 2.2375 2.9338 2.5508 0.2048 -0.0416 -0.0976 133 ASP D OD2 +8145 N N . GLY D 135 ? 1.4753 2.1645 1.7852 0.2073 -0.0394 -0.1005 134 GLY D N +8146 C CA . GLY D 135 ? 1.3331 2.0194 1.6423 0.2077 -0.0388 -0.1014 134 GLY D CA +8147 C C . GLY D 135 ? 1.3127 1.9963 1.6209 0.2089 -0.0381 -0.1025 134 GLY D C +8148 O O . GLY D 135 ? 1.1543 1.8381 1.4623 0.2095 -0.0382 -0.1027 134 GLY D O +8149 N N . ASN D 136 ? 1.3786 2.0596 1.6864 0.2092 -0.0375 -0.1032 135 ASN D N +8150 C CA . ASN D 136 ? 0.7801 1.4584 1.0869 0.2103 -0.0368 -0.1043 135 ASN D CA +8151 C C . ASN D 136 ? 1.1065 1.7847 1.4128 0.2108 -0.0366 -0.1045 135 ASN D C +8152 O O . ASN D 136 ? 0.9008 1.5785 1.2065 0.2115 -0.0365 -0.1050 135 ASN D O +8153 C CB . ASN D 136 ? 0.9490 1.6246 1.2557 0.2105 -0.0362 -0.1049 135 ASN D CB +8154 C CG . ASN D 136 ? 1.0016 1.6764 1.3085 0.2105 -0.0362 -0.1051 135 ASN D CG +8155 O OD1 . ASN D 136 ? 0.5012 1.1768 0.8082 0.2107 -0.0366 -0.1050 135 ASN D OD1 +8156 N ND2 . ASN D 136 ? 0.7036 1.3770 1.0106 0.2103 -0.0359 -0.1053 135 ASN D ND2 +8157 N N . ILE D 137 ? 0.8160 1.4948 1.1225 0.2103 -0.0365 -0.1041 136 ILE D N +8158 C CA . ILE D 137 ? 1.0645 1.7437 1.3706 0.2106 -0.0364 -0.1041 136 ILE D CA +8159 C C . ILE D 137 ? 1.1893 1.8709 1.4954 0.2105 -0.0370 -0.1036 136 ILE D C +8160 O O . ILE D 137 ? 0.7959 1.4770 1.1015 0.2113 -0.0369 -0.1041 136 ILE D O +8161 C CB . ILE D 137 ? 0.7820 1.4620 1.0886 0.2099 -0.0364 -0.1035 136 ILE D CB +8162 C CG1 . ILE D 137 ? 0.5047 1.1821 0.8113 0.2100 -0.0357 -0.1040 136 ILE D CG1 +8163 C CG2 . ILE D 137 ? 0.4472 1.1279 0.7535 0.2101 -0.0363 -0.1034 136 ILE D CG2 +8164 C CD1 . ILE D 137 ? 0.9498 1.6268 1.2568 0.2095 -0.0357 -0.1040 136 ILE D CD1 +8165 N N . LEU D 138 ? 0.9598 1.6442 1.2668 0.2096 -0.0376 -0.1026 137 LEU D N +8166 C CA . LEU D 138 ? 0.9746 1.6615 1.2817 0.2095 -0.0381 -0.1020 137 LEU D CA +8167 C C . LEU D 138 ? 1.1119 1.7993 1.4190 0.2099 -0.0384 -0.1022 137 LEU D C +8168 O O . LEU D 138 ? 0.8097 1.4987 1.1168 0.2100 -0.0387 -0.1019 137 LEU D O +8169 C CB . LEU D 138 ? 0.6891 1.3788 0.9973 0.2084 -0.0387 -0.1009 137 LEU D CB +8170 C CG . LEU D 138 ? 0.9273 1.6171 1.2355 0.2081 -0.0384 -0.1006 137 LEU D CG +8171 C CD1 . LEU D 138 ? 1.2858 1.9785 1.5950 0.2069 -0.0391 -0.0995 137 LEU D CD1 +8172 C CD2 . LEU D 138 ? 0.7133 1.4026 1.0207 0.2088 -0.0381 -0.1010 137 LEU D CD2 +8173 N N . GLY D 139 ? 0.6691 1.3552 0.9763 0.2100 -0.0383 -0.1025 138 GLY D N +8174 C CA . GLY D 139 ? 0.7274 1.4136 1.0346 0.2105 -0.0385 -0.1028 138 GLY D CA +8175 C C . GLY D 139 ? 1.0060 1.6897 1.3122 0.2116 -0.0379 -0.1039 138 GLY D C +8176 O O . GLY D 139 ? 0.9465 1.6302 1.2526 0.2121 -0.0380 -0.1042 138 GLY D O +8177 N N . HIS D 140 ? 1.1206 1.8022 1.4261 0.2120 -0.0374 -0.1045 139 HIS D N +8178 C CA . HIS D 140 ? 0.9910 1.6701 1.2956 0.2130 -0.0368 -0.1056 139 HIS D CA +8179 C C . HIS D 140 ? 0.8595 1.5368 1.1641 0.2135 -0.0366 -0.1062 139 HIS D C +8180 O O . HIS D 140 ? 0.8435 1.5206 1.1479 0.2140 -0.0367 -0.1066 139 HIS D O +8181 C CB . HIS D 140 ? 0.8767 1.5567 1.1808 0.2136 -0.0369 -0.1058 139 HIS D CB +8182 C CG . HIS D 140 ? 1.0802 1.7609 1.3840 0.2135 -0.0368 -0.1055 139 HIS D CG +8183 N ND1 . HIS D 140 ? 0.8682 1.5517 1.1725 0.2130 -0.0373 -0.1048 139 HIS D ND1 +8184 C CD2 . HIS D 140 ? 1.5074 2.1866 1.8107 0.2138 -0.0363 -0.1059 139 HIS D CD2 +8185 C CE1 . HIS D 140 ? 0.6613 1.3449 0.9652 0.2131 -0.0371 -0.1047 139 HIS D CE1 +8186 N NE2 . HIS D 140 ? 1.0221 1.7031 1.3256 0.2135 -0.0365 -0.1053 139 HIS D NE2 +8187 N N . LYS D 141 ? 0.9783 1.6543 1.2831 0.2132 -0.0364 -0.1062 140 LYS D N +8188 C CA . LYS D 141 ? 1.1018 1.7760 1.4066 0.2135 -0.0362 -0.1068 140 LYS D CA +8189 C C . LYS D 141 ? 1.2186 1.8896 1.5228 0.2141 -0.0354 -0.1076 140 LYS D C +8190 O O . LYS D 141 ? 0.8035 1.4727 1.1077 0.2144 -0.0352 -0.1082 140 LYS D O +8191 C CB . LYS D 141 ? 0.9904 1.6658 1.2961 0.2127 -0.0366 -0.1061 140 LYS D CB +8192 C CG . LYS D 141 ? 1.0516 1.7297 1.3580 0.2123 -0.0373 -0.1053 140 LYS D CG +8193 C CD . LYS D 141 ? 1.3398 2.0198 1.6471 0.2112 -0.0378 -0.1043 140 LYS D CD +8194 C CE . LYS D 141 ? 1.2138 1.8968 1.5220 0.2107 -0.0385 -0.1034 140 LYS D CE +8195 N NZ . LYS D 141 ? 1.4720 2.1572 1.7810 0.2096 -0.0390 -0.1024 140 LYS D NZ +8196 N N . LEU D 142 ? 0.8374 1.5078 1.1412 0.2142 -0.0351 -0.1078 141 LEU D N +8197 C CA . LEU D 142 ? 0.7067 1.3742 1.0100 0.2149 -0.0344 -0.1086 141 LEU D CA +8198 C C . LEU D 142 ? 0.8001 1.4660 1.1027 0.2159 -0.0341 -0.1095 141 LEU D C +8199 O O . LEU D 142 ? 0.5785 1.2458 0.8808 0.2161 -0.0344 -0.1094 141 LEU D O +8200 C CB . LEU D 142 ? 0.7997 1.4671 1.1029 0.2147 -0.0341 -0.1084 141 LEU D CB +8201 C CG . LEU D 142 ? 0.5098 1.1783 0.8137 0.2137 -0.0342 -0.1076 141 LEU D CG +8202 C CD1 . LEU D 142 ? 0.5988 1.2674 0.9028 0.2136 -0.0340 -0.1074 141 LEU D CD1 +8203 C CD2 . LEU D 142 ? 0.8497 1.5164 1.1539 0.2136 -0.0339 -0.1079 141 LEU D CD2 +8204 N N . GLU D 143 ? 0.7564 1.4196 1.0588 0.2164 -0.0336 -0.1102 142 GLU D N +8205 C CA . GLU D 143 ? 0.8265 1.4878 1.1282 0.2174 -0.0332 -0.1111 142 GLU D CA +8206 C C . GLU D 143 ? 0.9526 1.6128 1.2538 0.2179 -0.0328 -0.1115 142 GLU D C +8207 O O . GLU D 143 ? 0.7859 1.4455 1.0873 0.2176 -0.0325 -0.1112 142 GLU D O +8208 C CB . GLU D 143 ? 0.7883 1.4472 1.0901 0.2178 -0.0328 -0.1117 142 GLU D CB +8209 C CG . GLU D 143 ? 0.8969 1.5563 1.1989 0.2178 -0.0332 -0.1118 142 GLU D CG +8210 C CD . GLU D 143 ? 1.2916 1.9484 1.5937 0.2183 -0.0327 -0.1125 142 GLU D CD +8211 O OE1 . GLU D 143 ? 1.2247 1.8794 1.5266 0.2184 -0.0322 -0.1128 142 GLU D OE1 +8212 O OE2 . GLU D 143 ? 1.1301 1.7869 1.4323 0.2185 -0.0329 -0.1127 142 GLU D OE2 +8213 N N . TYR D 144 ? 0.5909 1.2511 0.8916 0.2186 -0.0328 -0.1119 143 TYR D N +8214 C CA . TYR D 144 ? 0.6039 1.2630 0.9041 0.2191 -0.0324 -0.1123 143 TYR D CA +8215 C C . TYR D 144 ? 0.7202 1.3761 1.0202 0.2196 -0.0317 -0.1130 143 TYR D C +8216 O O . TYR D 144 ? 0.6273 1.2816 0.9268 0.2204 -0.0314 -0.1137 143 TYR D O +8217 C CB . TYR D 144 ? 0.4790 1.1389 0.7786 0.2197 -0.0326 -0.1126 143 TYR D CB +8218 C CG . TYR D 144 ? 0.4482 1.1081 0.7474 0.2199 -0.0324 -0.1126 143 TYR D CG +8219 C CD1 . TYR D 144 ? 0.9154 1.5762 1.2149 0.2193 -0.0323 -0.1119 143 TYR D CD1 +8220 C CD2 . TYR D 144 ? 0.6888 1.3480 0.9874 0.2207 -0.0322 -0.1133 143 TYR D CD2 +8221 C CE1 . TYR D 144 ? 0.8097 1.4706 1.1090 0.2196 -0.0321 -0.1118 143 TYR D CE1 +8222 C CE2 . TYR D 144 ? 0.7037 1.3630 1.0020 0.2209 -0.0320 -0.1132 143 TYR D CE2 +8223 C CZ . TYR D 144 ? 0.8213 1.4814 1.1200 0.2204 -0.0320 -0.1124 143 TYR D CZ +8224 O OH . TYR D 144 ? 0.6111 1.2714 0.9095 0.2206 -0.0318 -0.1123 143 TYR D OH +8225 N N . ASN D 145 ? 0.3831 1.0381 0.6836 0.2192 -0.0313 -0.1127 144 ASN D N +8226 C CA . ASN D 145 ? 0.5613 1.2133 0.8617 0.2197 -0.0306 -0.1133 144 ASN D CA +8227 C C . ASN D 145 ? 0.3894 1.0408 0.6904 0.2192 -0.0302 -0.1129 144 ASN D C +8228 O O . ASN D 145 ? 0.7308 1.3842 1.0321 0.2185 -0.0305 -0.1122 144 ASN D O +8229 C CB . ASN D 145 ? 0.3397 0.9900 0.6401 0.2201 -0.0305 -0.1140 144 ASN D CB +8230 C CG . ASN D 145 ? 1.0349 1.6862 1.3359 0.2194 -0.0308 -0.1135 144 ASN D CG +8231 O OD1 . ASN D 145 ? 0.5147 1.1666 0.8161 0.2187 -0.0308 -0.1130 144 ASN D OD1 +8232 N ND2 . ASN D 145 ? 0.7432 1.3945 1.0441 0.2196 -0.0311 -0.1138 144 ASN D ND2 +8233 N N . TYR D 146 ? 0.5171 1.1658 0.8182 0.2196 -0.0295 -0.1135 145 TYR D N +8234 C CA . TYR D 146 ? 0.9107 1.5586 1.2123 0.2192 -0.0291 -0.1132 145 TYR D CA +8235 C C . TYR D 146 ? 0.6005 1.2456 0.9025 0.2195 -0.0284 -0.1137 145 TYR D C +8236 O O . TYR D 146 ? 0.7140 1.3574 1.0156 0.2202 -0.0282 -0.1144 145 TYR D O +8237 C CB . TYR D 146 ? 0.4419 1.0896 0.7435 0.2195 -0.0287 -0.1130 145 TYR D CB +8238 C CG . TYR D 146 ? 0.5655 1.2146 0.8677 0.2187 -0.0288 -0.1123 145 TYR D CG +8239 C CD1 . TYR D 146 ? 0.5240 1.1760 0.8262 0.2180 -0.0294 -0.1116 145 TYR D CD1 +8240 C CD2 . TYR D 146 ? 0.9444 1.5918 1.2472 0.2186 -0.0281 -0.1123 145 TYR D CD2 +8241 C CE1 . TYR D 146 ? 0.7969 1.4502 1.0998 0.2173 -0.0295 -0.1109 145 TYR D CE1 +8242 C CE2 . TYR D 146 ? 0.6869 1.3355 0.9903 0.2179 -0.0281 -0.1116 145 TYR D CE2 +8243 C CZ . TYR D 146 ? 0.4368 1.0884 0.7403 0.2172 -0.0288 -0.1109 145 TYR D CZ +8244 O OH . TYR D 146 ? 0.7139 1.3667 1.0180 0.2165 -0.0288 -0.1102 145 TYR D OH +8245 N N . ASN D 147 ? 0.9358 1.5804 1.2383 0.2190 -0.0280 -0.1134 146 ASN D N +8246 C CA . ASN D 147 ? 0.7025 1.3446 1.0054 0.2192 -0.0274 -0.1139 146 ASN D CA +8247 C C . ASN D 147 ? 0.8072 1.4477 1.1106 0.2193 -0.0266 -0.1139 146 ASN D C +8248 O O . ASN D 147 ? 0.7507 1.3922 1.0542 0.2193 -0.0266 -0.1135 146 ASN D O +8249 C CB . ASN D 147 ? 0.7783 1.4213 1.0816 0.2185 -0.0276 -0.1135 146 ASN D CB +8250 C CG . ASN D 147 ? 0.7236 1.3679 1.0266 0.2184 -0.0283 -0.1135 146 ASN D CG +8251 O OD1 . ASN D 147 ? 0.6436 1.2869 0.9462 0.2190 -0.0283 -0.1141 146 ASN D OD1 +8252 N ND2 . ASN D 147 ? 1.2246 1.8712 1.5279 0.2175 -0.0289 -0.1129 146 ASN D ND2 +8253 N N . SER D 148 ? 0.7486 1.3868 1.0524 0.2195 -0.0259 -0.1142 147 SER D N +8254 C CA . SER D 148 ? 0.6287 1.2651 0.9331 0.2197 -0.0250 -0.1143 147 SER D CA +8255 C C . SER D 148 ? 0.4486 1.0855 0.7538 0.2189 -0.0248 -0.1139 147 SER D C +8256 O O . SER D 148 ? 1.1170 1.7544 1.4223 0.2184 -0.0251 -0.1138 147 SER D O +8257 C CB . SER D 148 ? 0.6011 1.2343 0.9056 0.2205 -0.0243 -0.1151 147 SER D CB +8258 O OG . SER D 148 ? 0.8673 1.5000 1.1711 0.2213 -0.0244 -0.1154 147 SER D OG +8259 N N . HIS D 149 ? 0.5957 1.2325 0.9014 0.2187 -0.0244 -0.1135 148 HIS D N +8260 C CA . HIS D 149 ? 0.7896 1.4272 1.0961 0.2179 -0.0243 -0.1131 148 HIS D CA +8261 C C . HIS D 149 ? 0.7670 1.4026 1.0743 0.2181 -0.0233 -0.1132 148 HIS D C +8262 O O . HIS D 149 ? 0.8045 1.4384 1.1118 0.2188 -0.0228 -0.1134 148 HIS D O +8263 C CB . HIS D 149 ? 0.7511 1.3920 1.0575 0.2171 -0.0252 -0.1123 148 HIS D CB +8264 C CG . HIS D 149 ? 0.7075 1.3504 1.0132 0.2169 -0.0261 -0.1122 148 HIS D CG +8265 N ND1 . HIS D 149 ? 0.7276 1.3720 1.0327 0.2172 -0.0267 -0.1120 148 HIS D ND1 +8266 C CD2 . HIS D 149 ? 1.2347 1.8784 1.5403 0.2165 -0.0266 -0.1122 148 HIS D CD2 +8267 C CE1 . HIS D 149 ? 0.8979 1.5438 1.2026 0.2169 -0.0274 -0.1120 148 HIS D CE1 +8268 N NE2 . HIS D 149 ? 0.5879 1.2334 0.8928 0.2166 -0.0273 -0.1120 148 HIS D NE2 +8269 N N . ASN D 150 ? 0.7124 1.3482 1.0206 0.2174 -0.0230 -0.1129 149 ASN D N +8270 C CA . ASN D 150 ? 0.8747 1.5086 1.1838 0.2175 -0.0220 -0.1129 149 ASN D CA +8271 C C . ASN D 150 ? 0.7130 1.3491 1.0228 0.2167 -0.0222 -0.1122 149 ASN D C +8272 O O . ASN D 150 ? 1.0384 1.6765 1.3483 0.2159 -0.0228 -0.1119 149 ASN D O +8273 C CB . ASN D 150 ? 0.9684 1.6000 1.2780 0.2176 -0.0212 -0.1134 149 ASN D CB +8274 C CG . ASN D 150 ? 0.8937 1.5233 1.2027 0.2184 -0.0210 -0.1142 149 ASN D CG +8275 O OD1 . ASN D 150 ? 1.3282 1.9559 1.6371 0.2193 -0.0206 -0.1145 149 ASN D OD1 +8276 N ND2 . ASN D 150 ? 1.0399 1.6697 1.3485 0.2182 -0.0213 -0.1144 149 ASN D ND2 +8277 N N . VAL D 151 ? 0.9369 1.5726 1.2472 0.2170 -0.0218 -0.1120 150 VAL D N +8278 C CA . VAL D 151 ? 0.6584 1.2964 0.9693 0.2163 -0.0221 -0.1112 150 VAL D CA +8279 C C . VAL D 151 ? 1.0233 1.6602 1.3355 0.2159 -0.0212 -0.1111 150 VAL D C +8280 O O . VAL D 151 ? 1.0660 1.7017 1.3789 0.2163 -0.0205 -0.1110 150 VAL D O +8281 C CB . VAL D 151 ? 0.9112 1.5497 1.2218 0.2168 -0.0223 -0.1110 150 VAL D CB +8282 C CG1 . VAL D 151 ? 0.5305 1.1711 0.8417 0.2162 -0.0225 -0.1102 150 VAL D CG1 +8283 C CG2 . VAL D 151 ? 0.6101 1.2498 0.9194 0.2171 -0.0232 -0.1111 150 VAL D CG2 +8284 N N . TYR D 152 ? 0.8353 1.4728 1.1479 0.2152 -0.0212 -0.1111 151 TYR D N +8285 C CA . TYR D 152 ? 0.8701 1.5064 1.1840 0.2149 -0.0203 -0.1111 151 TYR D CA +8286 C C . TYR D 152 ? 0.8656 1.5031 1.1805 0.2145 -0.0202 -0.1105 151 TYR D C +8287 O O . TYR D 152 ? 0.8586 1.4988 1.1735 0.2137 -0.0209 -0.1099 151 TYR D O +8288 C CB . TYR D 152 ? 0.6641 1.3007 0.9782 0.2142 -0.0204 -0.1113 151 TYR D CB +8289 C CG . TYR D 152 ? 0.8073 1.4426 1.1205 0.2147 -0.0205 -0.1119 151 TYR D CG +8290 C CD1 . TYR D 152 ? 0.9040 1.5362 1.2174 0.2154 -0.0195 -0.1126 151 TYR D CD1 +8291 C CD2 . TYR D 152 ? 0.5066 1.1438 0.8187 0.2144 -0.0215 -0.1118 151 TYR D CD2 +8292 C CE1 . TYR D 152 ? 0.7480 1.3791 1.0607 0.2158 -0.0196 -0.1131 151 TYR D CE1 +8293 C CE2 . TYR D 152 ? 1.2184 1.8545 1.5297 0.2149 -0.0216 -0.1123 151 TYR D CE2 +8294 C CZ . TYR D 152 ? 1.1707 1.8037 1.4823 0.2155 -0.0206 -0.1130 151 TYR D CZ +8295 O OH . TYR D 152 ? 0.8460 1.4780 1.1569 0.2159 -0.0207 -0.1135 151 TYR D OH +8296 N N . ILE D 153 ? 0.6345 1.2699 0.9502 0.2151 -0.0192 -0.1106 152 ILE D N +8297 C CA . ILE D 153 ? 0.9812 1.6174 1.2981 0.2148 -0.0188 -0.1100 152 ILE D CA +8298 C C . ILE D 153 ? 1.1936 1.8290 1.5119 0.2143 -0.0180 -0.1100 152 ILE D C +8299 O O . ILE D 153 ? 1.1937 1.8272 1.5121 0.2144 -0.0174 -0.1106 152 ILE D O +8300 C CB . ILE D 153 ? 0.8691 1.5036 1.1861 0.2158 -0.0183 -0.1100 152 ILE D CB +8301 C CG1 . ILE D 153 ? 0.6395 1.2744 0.9551 0.2164 -0.0190 -0.1101 152 ILE D CG1 +8302 C CG2 . ILE D 153 ? 0.6694 1.3052 0.9875 0.2155 -0.0181 -0.1093 152 ILE D CG2 +8303 C CD1 . ILE D 153 ? 1.2321 1.8660 1.5477 0.2172 -0.0186 -0.1101 152 ILE D CD1 +8304 N N . MET D 154 ? 1.1438 1.7805 1.4630 0.2137 -0.0179 -0.1094 153 MET D N +8305 C CA . MET D 154 ? 1.3426 1.9792 1.6633 0.2130 -0.0172 -0.1094 153 MET D CA +8306 C C . MET D 154 ? 1.1859 1.8236 1.5077 0.2127 -0.0170 -0.1087 153 MET D C +8307 O O . MET D 154 ? 1.2089 1.8489 1.5303 0.2125 -0.0179 -0.1081 153 MET D O +8308 C CB . MET D 154 ? 1.3881 2.0269 1.7084 0.2120 -0.0180 -0.1093 153 MET D CB +8309 C CG . MET D 154 ? 1.3738 2.0127 1.6955 0.2112 -0.0175 -0.1093 153 MET D CG +8310 S SD . MET D 154 ? 2.2356 2.8748 2.5567 0.2106 -0.0178 -0.1098 153 MET D SD +8311 C CE . MET D 154 ? 1.1069 1.7488 1.4263 0.2103 -0.0194 -0.1095 153 MET D CE +8312 N N . ALA D 155 ? 1.0845 1.7205 1.4079 0.2128 -0.0158 -0.1088 154 ALA D N +8313 C CA . ALA D 155 ? 1.1092 1.7462 1.4339 0.2126 -0.0156 -0.1081 154 ALA D CA +8314 C C . ALA D 155 ? 1.5166 2.1564 1.8417 0.2113 -0.0162 -0.1076 154 ALA D C +8315 O O . ALA D 155 ? 1.2559 1.8963 1.5811 0.2106 -0.0164 -0.1079 154 ALA D O +8316 C CB . ALA D 155 ? 0.8127 1.4468 1.1389 0.2131 -0.0140 -0.1083 154 ALA D CB +8317 N N . ASP D 156 ? 1.5892 2.2308 1.9149 0.2110 -0.0166 -0.1069 155 ASP D N +8318 C CA . ASP D 156 ? 1.8436 2.4878 2.1702 0.2099 -0.0170 -0.1063 155 ASP D CA +8319 C C . ASP D 156 ? 2.0350 2.6785 2.3634 0.2099 -0.0160 -0.1059 155 ASP D C +8320 O O . ASP D 156 ? 1.4695 2.1142 1.7981 0.2100 -0.0163 -0.1053 155 ASP D O +8321 C CB . ASP D 156 ? 1.7643 2.4118 2.0899 0.2093 -0.0185 -0.1057 155 ASP D CB +8322 C CG . ASP D 156 ? 1.7874 2.4376 2.1139 0.2080 -0.0190 -0.1051 155 ASP D CG +8323 O OD1 . ASP D 156 ? 1.8955 2.5452 2.2234 0.2075 -0.0183 -0.1052 155 ASP D OD1 +8324 O OD2 . ASP D 156 ? 1.3685 2.0214 1.6943 0.2075 -0.0202 -0.1046 155 ASP D OD2 +8325 N N . LYS D 157 ? 2.2450 2.8865 2.5748 0.2100 -0.0148 -0.1063 156 LYS D N +8326 C CA . LYS D 157 ? 2.1264 2.7666 2.4580 0.2102 -0.0136 -0.1060 156 LYS D CA +8327 C C . LYS D 157 ? 1.8971 2.5399 2.2298 0.2093 -0.0140 -0.1052 156 LYS D C +8328 O O . LYS D 157 ? 1.3959 2.0384 1.7299 0.2095 -0.0134 -0.1047 156 LYS D O +8329 C CB . LYS D 157 ? 2.0555 2.6930 2.3884 0.2104 -0.0121 -0.1066 156 LYS D CB +8330 C CG . LYS D 157 ? 2.0623 2.6967 2.3945 0.2116 -0.0114 -0.1073 156 LYS D CG +8331 C CD . LYS D 157 ? 1.8985 2.5301 2.2319 0.2118 -0.0099 -0.1079 156 LYS D CD +8332 C CE . LYS D 157 ? 1.7681 2.3965 2.1010 0.2130 -0.0091 -0.1085 156 LYS D CE +8333 N NZ . LYS D 157 ? 1.7455 2.3742 2.0763 0.2133 -0.0102 -0.1089 156 LYS D NZ +8334 N N . GLN D 158 ? 2.1378 2.7834 2.4702 0.2082 -0.0151 -0.1050 157 GLN D N +8335 C CA . GLN D 158 ? 2.1438 2.7921 2.4772 0.2072 -0.0156 -0.1043 157 GLN D CA +8336 C C . GLN D 158 ? 1.9008 2.5510 2.2335 0.2073 -0.0165 -0.1035 157 GLN D C +8337 O O . GLN D 158 ? 1.5801 2.2313 1.9140 0.2071 -0.0164 -0.1029 157 GLN D O +8338 C CB . GLN D 158 ? 2.0204 2.6709 2.3536 0.2060 -0.0164 -0.1043 157 GLN D CB +8339 C CG . GLN D 158 ? 2.2157 2.8647 2.5499 0.2057 -0.0154 -0.1050 157 GLN D CG +8340 C CD . GLN D 158 ? 2.2636 2.9117 2.6000 0.2054 -0.0141 -0.1049 157 GLN D CD +8341 O OE1 . GLN D 158 ? 2.3458 2.9914 2.6831 0.2063 -0.0129 -0.1050 157 GLN D OE1 +8342 N NE2 . GLN D 158 ? 1.9477 2.5979 2.2852 0.2042 -0.0143 -0.1047 157 GLN D NE2 +8343 N N . LYS D 159 ? 1.9504 2.6010 2.2812 0.2078 -0.0174 -0.1037 158 LYS D N +8344 C CA . LYS D 159 ? 1.6808 2.3333 2.0108 0.2079 -0.0184 -0.1030 158 LYS D CA +8345 C C . LYS D 159 ? 1.6363 2.2869 1.9658 0.2092 -0.0179 -0.1031 158 LYS D C +8346 O O . LYS D 159 ? 1.2871 1.9390 1.6156 0.2094 -0.0187 -0.1027 158 LYS D O +8347 C CB . LYS D 159 ? 1.4928 2.1477 1.8212 0.2073 -0.0198 -0.1029 158 LYS D CB +8348 C CG . LYS D 159 ? 2.1169 2.7736 2.4456 0.2061 -0.0203 -0.1029 158 LYS D CG +8349 C CD . LYS D 159 ? 2.2480 2.9062 2.5787 0.2052 -0.0201 -0.1023 158 LYS D CD +8350 C CE . LYS D 159 ? 1.9181 2.5769 2.2495 0.2042 -0.0200 -0.1026 158 LYS D CE +8351 N NZ . LYS D 159 ? 1.7592 2.4186 2.0926 0.2035 -0.0194 -0.1022 158 LYS D NZ +8352 N N . ASN D 160 ? 1.6679 2.3153 1.9980 0.2099 -0.0166 -0.1036 159 ASN D N +8353 C CA . ASN D 160 ? 1.6589 2.3043 1.9889 0.2111 -0.0160 -0.1037 159 ASN D CA +8354 C C . ASN D 160 ? 1.3913 2.0368 1.7192 0.2118 -0.0168 -0.1039 159 ASN D C +8355 O O . ASN D 160 ? 1.1472 1.7923 1.4747 0.2125 -0.0168 -0.1037 159 ASN D O +8356 C CB . ASN D 160 ? 1.6210 2.2672 1.9523 0.2112 -0.0157 -0.1028 159 ASN D CB +8357 C CG . ASN D 160 ? 1.7932 2.4369 2.1250 0.2124 -0.0147 -0.1029 159 ASN D CG +8358 O OD1 . ASN D 160 ? 1.7745 2.4154 2.1066 0.2130 -0.0137 -0.1035 159 ASN D OD1 +8359 N ND2 . ASN D 160 ? 1.5586 2.2033 1.8905 0.2127 -0.0150 -0.1022 159 ASN D ND2 +8360 N N . GLY D 161 ? 1.2410 1.8870 1.5677 0.2115 -0.0175 -0.1044 160 GLY D N +8361 C CA . GLY D 161 ? 1.2793 1.9255 1.6041 0.2120 -0.0183 -0.1047 160 GLY D CA +8362 C C . GLY D 161 ? 1.2704 1.9150 1.5944 0.2122 -0.0182 -0.1055 160 GLY D C +8363 O O . GLY D 161 ? 1.3124 1.9553 1.6374 0.2121 -0.0173 -0.1059 160 GLY D O +8364 N N . ILE D 162 ? 1.2446 1.8899 1.5669 0.2123 -0.0190 -0.1058 161 ILE D N +8365 C CA . ILE D 162 ? 1.1698 1.8139 1.4914 0.2124 -0.0191 -0.1065 161 ILE D CA +8366 C C . ILE D 162 ? 1.0122 1.6590 1.3328 0.2116 -0.0203 -0.1064 161 ILE D C +8367 O O . ILE D 162 ? 1.0779 1.7273 1.3981 0.2111 -0.0212 -0.1058 161 ILE D O +8368 C CB . ILE D 162 ? 1.2109 1.8527 1.5313 0.2135 -0.0188 -0.1071 161 ILE D CB +8369 C CG1 . ILE D 162 ? 1.2150 1.8585 1.5342 0.2139 -0.0198 -0.1068 161 ILE D CG1 +8370 C CG2 . ILE D 162 ? 1.3031 1.9420 1.6246 0.2144 -0.0175 -0.1073 161 ILE D CG2 +8371 C CD1 . ILE D 162 ? 0.7255 1.3671 1.0434 0.2149 -0.0197 -0.1074 161 ILE D CD1 +8372 N N . LYS D 163 ? 0.8559 1.5020 1.1761 0.2113 -0.0203 -0.1069 162 LYS D N +8373 C CA . LYS D 163 ? 1.0730 1.7212 1.3922 0.2107 -0.0214 -0.1068 162 LYS D CA +8374 C C . LYS D 163 ? 1.1637 1.8105 1.4816 0.2114 -0.0215 -0.1075 162 LYS D C +8375 O O . LYS D 163 ? 1.3220 1.9661 1.6400 0.2120 -0.0207 -0.1081 162 LYS D O +8376 C CB . LYS D 163 ? 1.3712 2.0201 1.6912 0.2097 -0.0213 -0.1069 162 LYS D CB +8377 C CG . LYS D 163 ? 1.8190 2.4712 2.1395 0.2085 -0.0222 -0.1061 162 LYS D CG +8378 C CD . LYS D 163 ? 1.8095 2.4625 2.1306 0.2076 -0.0223 -0.1062 162 LYS D CD +8379 C CE . LYS D 163 ? 1.7269 2.3831 2.0488 0.2064 -0.0230 -0.1054 162 LYS D CE +8380 N NZ . LYS D 163 ? 1.7145 2.3707 2.0377 0.2063 -0.0224 -0.1050 162 LYS D NZ +8381 N N . VAL D 164 ? 0.9086 1.5571 1.2252 0.2114 -0.0226 -0.1073 163 VAL D N +8382 C CA . VAL D 164 ? 0.8680 1.5152 1.1834 0.2121 -0.0227 -0.1079 163 VAL D CA +8383 C C . VAL D 164 ? 0.6494 1.2985 0.9640 0.2115 -0.0237 -0.1079 163 VAL D C +8384 O O . VAL D 164 ? 1.1361 1.7880 1.4506 0.2107 -0.0245 -0.1073 163 VAL D O +8385 C CB . VAL D 164 ? 1.1943 1.8411 1.5089 0.2130 -0.0228 -0.1079 163 VAL D CB +8386 C CG1 . VAL D 164 ? 0.7089 1.3541 1.0223 0.2138 -0.0228 -0.1087 163 VAL D CG1 +8387 C CG2 . VAL D 164 ? 1.0513 1.6966 1.3668 0.2135 -0.0219 -0.1079 163 VAL D CG2 +8388 N N . ASN D 165 ? 0.7261 1.3737 1.0400 0.2119 -0.0236 -0.1085 164 ASN D N +8389 C CA . ASN D 165 ? 1.0034 1.6527 1.3165 0.2114 -0.0245 -0.1085 164 ASN D CA +8390 C C . ASN D 165 ? 0.8707 1.5183 1.1828 0.2122 -0.0244 -0.1092 164 ASN D C +8391 O O . ASN D 165 ? 1.0963 1.7410 1.4085 0.2130 -0.0236 -0.1098 164 ASN D O +8392 C CB . ASN D 165 ? 0.9939 1.6444 1.3078 0.2104 -0.0246 -0.1083 164 ASN D CB +8393 C CG . ASN D 165 ? 1.2835 1.9313 1.5977 0.2107 -0.0237 -0.1090 164 ASN D CG +8394 O OD1 . ASN D 165 ? 1.5754 2.2213 1.8905 0.2110 -0.0227 -0.1092 164 ASN D OD1 +8395 N ND2 . ASN D 165 ? 1.6591 2.3068 1.9728 0.2106 -0.0240 -0.1093 164 ASN D ND2 +8396 N N . PHE D 166 ? 0.6522 1.3014 0.9634 0.2121 -0.0254 -0.1090 165 PHE D N +8397 C CA . PHE D 166 ? 0.8070 1.4549 1.1173 0.2128 -0.0254 -0.1096 165 PHE D CA +8398 C C . PHE D 166 ? 0.5712 1.2215 0.8808 0.2123 -0.0265 -0.1093 165 PHE D C +8399 O O . PHE D 166 ? 0.9570 1.6100 1.2668 0.2116 -0.0272 -0.1086 165 PHE D O +8400 C CB . PHE D 166 ? 0.9360 1.5820 1.2457 0.2139 -0.0250 -0.1101 165 PHE D CB +8401 C CG . PHE D 166 ? 0.9571 1.6047 1.2666 0.2140 -0.0255 -0.1096 165 PHE D CG +8402 C CD1 . PHE D 166 ? 0.6741 1.3220 0.9843 0.2138 -0.0251 -0.1092 165 PHE D CD1 +8403 C CD2 . PHE D 166 ? 0.4439 1.0928 0.7525 0.2142 -0.0262 -0.1096 165 PHE D CD2 +8404 C CE1 . PHE D 166 ? 0.5394 1.1889 0.8495 0.2139 -0.0255 -0.1087 165 PHE D CE1 +8405 C CE2 . PHE D 166 ? 0.6462 1.2966 0.9545 0.2143 -0.0266 -0.1092 165 PHE D CE2 +8406 C CZ . PHE D 166 ? 0.8338 1.4845 1.1428 0.2142 -0.0262 -0.1087 165 PHE D CZ +8407 N N . LYS D 167 ? 0.6905 1.3399 0.9994 0.2128 -0.0266 -0.1098 166 LYS D N +8408 C CA . LYS D 167 ? 0.9118 1.5633 1.2202 0.2125 -0.0276 -0.1095 166 LYS D CA +8409 C C . LYS D 167 ? 0.8888 1.5395 1.1963 0.2133 -0.0277 -0.1099 166 LYS D C +8410 O O . LYS D 167 ? 0.9286 1.5770 1.2357 0.2139 -0.0273 -0.1106 166 LYS D O +8411 C CB . LYS D 167 ? 0.6250 1.2765 0.9337 0.2119 -0.0276 -0.1096 166 LYS D CB +8412 C CG . LYS D 167 ? 1.2841 1.9379 1.5925 0.2115 -0.0286 -0.1092 166 LYS D CG +8413 C CD . LYS D 167 ? 1.5704 2.2239 1.8790 0.2110 -0.0286 -0.1093 166 LYS D CD +8414 C CE . LYS D 167 ? 1.3033 1.9567 1.6128 0.2103 -0.0281 -0.1092 166 LYS D CE +8415 N NZ . LYS D 167 ? 1.6902 2.3465 2.0003 0.2093 -0.0287 -0.1084 166 LYS D NZ +8416 N N . ILE D 168 ? 0.7516 1.4042 1.0587 0.2133 -0.0284 -0.1096 167 ILE D N +8417 C CA . ILE D 168 ? 0.9458 1.5980 1.2520 0.2141 -0.0286 -0.1099 167 ILE D CA +8418 C C . ILE D 168 ? 0.7375 1.3910 1.0434 0.2139 -0.0293 -0.1099 167 ILE D C +8419 O O . ILE D 168 ? 0.7757 1.4316 1.0819 0.2130 -0.0300 -0.1092 167 ILE D O +8420 C CB . ILE D 168 ? 0.6017 1.2556 0.9076 0.2142 -0.0290 -0.1095 167 ILE D CB +8421 C CG1 . ILE D 168 ? 0.6799 1.3329 0.9862 0.2144 -0.0284 -0.1095 167 ILE D CG1 +8422 C CG2 . ILE D 168 ? 0.6679 1.3217 0.9729 0.2149 -0.0293 -0.1099 167 ILE D CG2 +8423 C CD1 . ILE D 168 ? 0.9325 1.5823 1.2386 0.2154 -0.0275 -0.1103 167 ILE D CD1 +8424 N N . ARG D 169 ? 0.5741 1.2258 0.8795 0.2146 -0.0291 -0.1105 168 ARG D N +8425 C CA . ARG D 169 ? 0.7942 1.4470 1.0993 0.2145 -0.0297 -0.1105 168 ARG D CA +8426 C C . ARG D 169 ? 0.5698 1.2235 0.8743 0.2150 -0.0302 -0.1105 168 ARG D C +8427 O O . ARG D 169 ? 0.9621 1.6140 1.2660 0.2159 -0.0298 -0.1111 168 ARG D O +8428 C CB . ARG D 169 ? 0.8800 1.5304 1.1850 0.2150 -0.0293 -0.1112 168 ARG D CB +8429 C CG . ARG D 169 ? 1.0168 1.6664 1.3224 0.2145 -0.0288 -0.1111 168 ARG D CG +8430 C CD . ARG D 169 ? 0.8840 1.5312 1.1895 0.2150 -0.0284 -0.1118 168 ARG D CD +8431 N NE . ARG D 169 ? 1.2044 1.8487 1.5096 0.2160 -0.0276 -0.1126 168 ARG D NE +8432 C CZ . ARG D 169 ? 1.4891 2.1315 1.7945 0.2162 -0.0268 -0.1128 168 ARG D CZ +8433 N NH1 . ARG D 169 ? 1.1941 1.8373 1.5002 0.2156 -0.0267 -0.1124 168 ARG D NH1 +8434 N NH2 . ARG D 169 ? 1.2475 1.8875 1.5527 0.2171 -0.0262 -0.1135 168 ARG D NH2 +8435 N N . HIS D 170 ? 0.4341 1.0906 0.7386 0.2145 -0.0310 -0.1099 169 HIS D N +8436 C CA . HIS D 170 ? 0.7616 1.4190 1.0655 0.2149 -0.0314 -0.1100 169 HIS D CA +8437 C C . HIS D 170 ? 0.4376 1.0951 0.7414 0.2151 -0.0318 -0.1102 169 HIS D C +8438 O O . HIS D 170 ? 1.1063 1.7650 1.4106 0.2144 -0.0321 -0.1097 169 HIS D O +8439 C CB . HIS D 170 ? 0.4019 1.0624 0.7060 0.2143 -0.0321 -0.1092 169 HIS D CB +8440 C CG . HIS D 170 ? 0.8778 1.5385 1.1821 0.2142 -0.0318 -0.1089 169 HIS D CG +8441 N ND1 . HIS D 170 ? 0.9618 1.6220 1.2656 0.2148 -0.0316 -0.1091 169 HIS D ND1 +8442 C CD2 . HIS D 170 ? 0.9770 1.6384 1.2819 0.2134 -0.0317 -0.1084 169 HIS D CD2 +8443 C CE1 . HIS D 170 ? 0.7720 1.4325 1.0761 0.2144 -0.0314 -0.1088 169 HIS D CE1 +8444 N NE2 . HIS D 170 ? 0.5258 1.1870 0.8306 0.2136 -0.0315 -0.1083 169 HIS D NE2 +8445 N N . ASN D 171 ? 1.0741 1.7305 1.3773 0.2159 -0.0317 -0.1108 170 ASN D N +8446 C CA . ASN D 171 ? 0.5911 1.2477 0.8944 0.2160 -0.0320 -0.1110 170 ASN D CA +8447 C C . ASN D 171 ? 0.8966 1.5561 1.2000 0.2156 -0.0328 -0.1103 170 ASN D C +8448 O O . ASN D 171 ? 1.3184 1.9794 1.6216 0.2156 -0.0330 -0.1100 170 ASN D O +8449 C CB . ASN D 171 ? 1.1043 1.7586 1.4070 0.2171 -0.0316 -0.1119 170 ASN D CB +8450 C CG . ASN D 171 ? 1.0307 1.6820 1.3335 0.2175 -0.0308 -0.1125 170 ASN D CG +8451 O OD1 . ASN D 171 ? 0.7805 1.4311 1.0835 0.2171 -0.0304 -0.1124 170 ASN D OD1 +8452 N ND2 . ASN D 171 ? 0.9629 1.6123 1.2653 0.2182 -0.0306 -0.1132 170 ASN D ND2 +8453 N N . ILE D 172 ? 0.9859 1.6465 1.2897 0.2153 -0.0332 -0.1101 171 ILE D N +8454 C CA . ILE D 172 ? 0.9182 1.5815 1.2223 0.2150 -0.0340 -0.1094 171 ILE D CA +8455 C C . ILE D 172 ? 1.1569 1.8195 1.4610 0.2155 -0.0340 -0.1099 171 ILE D C +8456 O O . ILE D 172 ? 1.5398 2.2000 1.8437 0.2160 -0.0335 -0.1105 171 ILE D O +8457 C CB . ILE D 172 ? 0.8418 1.5073 1.1467 0.2139 -0.0344 -0.1085 171 ILE D CB +8458 C CG1 . ILE D 172 ? 0.8819 1.5480 1.1868 0.2134 -0.0344 -0.1081 171 ILE D CG1 +8459 C CG2 . ILE D 172 ? 0.5566 1.2249 0.8619 0.2135 -0.0352 -0.1078 171 ILE D CG2 +8460 C CD1 . ILE D 172 ? 0.9545 1.6214 1.2601 0.2125 -0.0345 -0.1075 171 ILE D CD1 +8461 N N . GLU D 173 ? 0.6694 1.3339 0.9736 0.2155 -0.0346 -0.1096 172 GLU D N +8462 C CA . GLU D 173 ? 1.2972 1.9607 1.6014 0.2162 -0.0345 -0.1101 172 GLU D CA +8463 C C . GLU D 173 ? 1.4951 2.1584 1.7999 0.2159 -0.0346 -0.1099 172 GLU D C +8464 O O . GLU D 173 ? 1.6402 2.3017 1.9450 0.2165 -0.0343 -0.1106 172 GLU D O +8465 C CB . GLU D 173 ? 0.9675 1.6329 1.2717 0.2164 -0.0350 -0.1100 172 GLU D CB +8466 C CG . GLU D 173 ? 1.7491 2.4128 2.0531 0.2172 -0.0348 -0.1108 172 GLU D CG +8467 C CD . GLU D 173 ? 2.2136 2.8792 2.5179 0.2174 -0.0353 -0.1107 172 GLU D CD +8468 O OE1 . GLU D 173 ? 1.9214 2.5893 2.2265 0.2168 -0.0358 -0.1099 172 GLU D OE1 +8469 O OE2 . GLU D 173 ? 2.3236 2.9883 2.6273 0.2181 -0.0351 -0.1114 172 GLU D OE2 +8470 N N . ASP D 174 ? 1.1477 1.8127 1.4532 0.2150 -0.0350 -0.1091 173 ASP D N +8471 C CA . ASP D 174 ? 1.2613 1.9261 1.5674 0.2148 -0.0351 -0.1089 173 ASP D CA +8472 C C . ASP D 174 ? 1.6274 2.2895 1.9332 0.2150 -0.0344 -0.1095 173 ASP D C +8473 O O . ASP D 174 ? 2.3953 3.0570 2.7016 0.2148 -0.0344 -0.1094 173 ASP D O +8474 C CB . ASP D 174 ? 1.4716 2.1392 1.7785 0.2137 -0.0357 -0.1077 173 ASP D CB +8475 C CG . ASP D 174 ? 1.4589 2.1272 1.7657 0.2131 -0.0357 -0.1074 173 ASP D CG +8476 O OD1 . ASP D 174 ? 1.4023 2.0686 1.7086 0.2134 -0.0351 -0.1079 173 ASP D OD1 +8477 O OD2 . ASP D 174 ? 1.3941 2.0650 1.7014 0.2123 -0.0363 -0.1065 173 ASP D OD2 +8478 N N . GLY D 175 ? 0.9265 1.5867 1.2317 0.2154 -0.0338 -0.1101 174 GLY D N +8479 C CA . GLY D 175 ? 0.9448 1.6023 1.2498 0.2157 -0.0331 -0.1107 174 GLY D CA +8480 C C . GLY D 175 ? 1.1653 1.8230 1.4705 0.2150 -0.0330 -0.1103 174 GLY D C +8481 O O . GLY D 175 ? 1.1356 1.7910 1.4406 0.2152 -0.0323 -0.1108 174 GLY D O +8482 N N . SER D 176 ? 0.7289 1.3893 1.0344 0.2142 -0.0336 -0.1094 175 SER D N +8483 C CA . SER D 176 ? 1.0938 1.7547 1.3997 0.2135 -0.0335 -0.1090 175 SER D CA +8484 C C . SER D 176 ? 0.8922 1.5524 1.1976 0.2136 -0.0331 -0.1093 175 SER D C +8485 O O . SER D 176 ? 1.0735 1.7329 1.3784 0.2143 -0.0330 -0.1097 175 SER D O +8486 C CB . SER D 176 ? 1.0356 1.6997 1.3421 0.2124 -0.0343 -0.1080 175 SER D CB +8487 O OG . SER D 176 ? 1.0365 1.7027 1.3430 0.2124 -0.0348 -0.1075 175 SER D OG +8488 N N . VAL D 177 ? 0.8377 1.4982 1.1434 0.2130 -0.0330 -0.1089 176 VAL D N +8489 C CA . VAL D 177 ? 0.7466 1.4059 1.0520 0.2132 -0.0325 -0.1092 176 VAL D CA +8490 C C . VAL D 177 ? 1.0207 1.6822 1.3266 0.2124 -0.0328 -0.1085 176 VAL D C +8491 O O . VAL D 177 ? 1.3387 2.0007 1.6451 0.2117 -0.0328 -0.1081 176 VAL D O +8492 C CB . VAL D 177 ? 0.7053 1.3616 1.0106 0.2137 -0.0316 -0.1099 176 VAL D CB +8493 C CG1 . VAL D 177 ? 0.8803 1.5356 1.1856 0.2138 -0.0310 -0.1101 176 VAL D CG1 +8494 C CG2 . VAL D 177 ? 0.8289 1.4828 1.1337 0.2146 -0.0312 -0.1108 176 VAL D CG2 +8495 N N . GLN D 178 ? 0.7092 1.3719 1.0149 0.2124 -0.0330 -0.1082 177 GLN D N +8496 C CA . GLN D 178 ? 0.8586 1.5233 1.1647 0.2116 -0.0333 -0.1075 177 GLN D CA +8497 C C . GLN D 178 ? 0.8715 1.5346 1.1777 0.2116 -0.0326 -0.1077 177 GLN D C +8498 O O . GLN D 178 ? 0.9575 1.6189 1.2633 0.2123 -0.0321 -0.1082 177 GLN D O +8499 C CB . GLN D 178 ? 0.6132 1.2798 0.9191 0.2117 -0.0337 -0.1071 177 GLN D CB +8500 C CG . GLN D 178 ? 1.0199 1.6886 1.3263 0.2109 -0.0340 -0.1063 177 GLN D CG +8501 C CD . GLN D 178 ? 0.8716 1.5428 1.1787 0.2098 -0.0347 -0.1055 177 GLN D CD +8502 O OE1 . GLN D 178 ? 0.8793 1.5522 1.1866 0.2096 -0.0353 -0.1051 177 GLN D OE1 +8503 N NE2 . GLN D 178 ? 0.9322 1.6038 1.2398 0.2091 -0.0346 -0.1051 177 GLN D NE2 +8504 N N . LEU D 179 ? 0.8144 1.4780 1.1212 0.2108 -0.0326 -0.1074 178 LEU D N +8505 C CA . LEU D 179 ? 0.6870 1.3490 0.9941 0.2108 -0.0318 -0.1076 178 LEU D CA +8506 C C . LEU D 179 ? 0.6399 1.3034 0.9473 0.2105 -0.0320 -0.1071 178 LEU D C +8507 O O . LEU D 179 ? 1.0602 1.7264 1.3678 0.2098 -0.0327 -0.1063 178 LEU D O +8508 C CB . LEU D 179 ? 0.8256 1.4873 1.1333 0.2102 -0.0316 -0.1075 178 LEU D CB +8509 C CG . LEU D 179 ? 1.0949 1.7548 1.4024 0.2105 -0.0313 -0.1081 178 LEU D CG +8510 C CD1 . LEU D 179 ? 1.3477 2.0079 1.6559 0.2097 -0.0313 -0.1079 178 LEU D CD1 +8511 C CD2 . LEU D 179 ? 0.7008 1.3573 1.0079 0.2116 -0.0304 -0.1090 178 LEU D CD2 +8512 N N . ALA D 180 ? 0.6072 1.2688 0.9145 0.2109 -0.0312 -0.1075 179 ALA D N +8513 C CA . ALA D 180 ? 0.7849 1.4478 1.0925 0.2107 -0.0313 -0.1070 179 ALA D CA +8514 C C . ALA D 180 ? 0.7772 1.4387 1.0855 0.2105 -0.0306 -0.1071 179 ALA D C +8515 O O . ALA D 180 ? 0.9616 1.6214 1.2698 0.2111 -0.0299 -0.1074 179 ALA D O +8516 C CB . ALA D 180 ? 0.8769 1.5395 1.1839 0.2115 -0.0312 -0.1072 179 ALA D CB +8517 N N . ASP D 181 ? 0.6059 1.2685 0.9149 0.2096 -0.0307 -0.1067 180 ASP D N +8518 C CA . ASP D 181 ? 1.0510 1.7125 1.3608 0.2093 -0.0300 -0.1068 180 ASP D CA +8519 C C . ASP D 181 ? 0.7668 1.4286 1.0770 0.2093 -0.0298 -0.1064 180 ASP D C +8520 O O . ASP D 181 ? 0.8756 1.5400 1.1861 0.2086 -0.0304 -0.1057 180 ASP D O +8521 C CB . ASP D 181 ? 0.9746 1.6378 1.2851 0.2082 -0.0305 -0.1063 180 ASP D CB +8522 C CG . ASP D 181 ? 1.0548 1.7164 1.3660 0.2080 -0.0297 -0.1066 180 ASP D CG +8523 O OD1 . ASP D 181 ? 1.3812 2.0408 1.6926 0.2085 -0.0289 -0.1070 180 ASP D OD1 +8524 O OD2 . ASP D 181 ? 1.2734 1.9357 1.5850 0.2072 -0.0299 -0.1065 180 ASP D OD2 +8525 N N . HIS D 182 ? 0.5676 1.2269 0.8778 0.2101 -0.0289 -0.1070 181 HIS D N +8526 C CA . HIS D 182 ? 0.9611 1.6205 1.2716 0.2102 -0.0286 -0.1067 181 HIS D CA +8527 C C . HIS D 182 ? 0.7609 1.4196 1.0725 0.2098 -0.0280 -0.1066 181 HIS D C +8528 O O . HIS D 182 ? 0.6913 1.3476 1.0032 0.2101 -0.0271 -0.1072 181 HIS D O +8529 C CB . HIS D 182 ? 0.7640 1.4211 1.0739 0.2114 -0.0281 -0.1073 181 HIS D CB +8530 C CG . HIS D 182 ? 0.6181 1.2761 0.9270 0.2119 -0.0286 -0.1073 181 HIS D CG +8531 N ND1 . HIS D 182 ? 0.8122 1.4703 1.1204 0.2120 -0.0291 -0.1076 181 HIS D ND1 +8532 C CD2 . HIS D 182 ? 0.4983 1.1570 0.8068 0.2123 -0.0288 -0.1071 181 HIS D CD2 +8533 C CE1 . HIS D 182 ? 0.8396 1.4985 1.1471 0.2125 -0.0295 -0.1076 181 HIS D CE1 +8534 N NE2 . HIS D 182 ? 0.6842 1.3434 0.9917 0.2126 -0.0293 -0.1073 181 HIS D NE2 +8535 N N . TYR D 183 ? 1.0329 1.6936 1.3452 0.2091 -0.0282 -0.1059 182 TYR D N +8536 C CA . TYR D 183 ? 1.0256 1.6858 1.3392 0.2087 -0.0276 -0.1057 182 TYR D CA +8537 C C . TYR D 183 ? 0.8277 1.4879 1.1416 0.2091 -0.0273 -0.1054 182 TYR D C +8538 O O . TYR D 183 ? 1.2447 1.9072 1.5586 0.2086 -0.0279 -0.1047 182 TYR D O +8539 C CB . TYR D 183 ? 0.7551 1.4178 1.0695 0.2074 -0.0282 -0.1051 182 TYR D CB +8540 C CG . TYR D 183 ? 0.8921 1.5546 1.2063 0.2070 -0.0283 -0.1054 182 TYR D CG +8541 C CD1 . TYR D 183 ? 0.9593 1.6229 1.2727 0.2070 -0.0291 -0.1054 182 TYR D CD1 +8542 C CD2 . TYR D 183 ? 0.5393 1.2006 0.8543 0.2067 -0.0277 -0.1057 182 TYR D CD2 +8543 C CE1 . TYR D 183 ? 0.8439 1.5074 1.1572 0.2067 -0.0293 -0.1056 182 TYR D CE1 +8544 C CE2 . TYR D 183 ? 1.0066 1.6679 1.3215 0.2063 -0.0278 -0.1060 182 TYR D CE2 +8545 C CZ . TYR D 183 ? 1.0762 1.7386 1.3903 0.2063 -0.0286 -0.1059 182 TYR D CZ +8546 O OH . TYR D 183 ? 0.9708 1.6332 1.2847 0.2060 -0.0288 -0.1061 182 TYR D OH +8547 N N . GLN D 184 ? 0.7812 1.4387 1.0953 0.2099 -0.0263 -0.1059 183 GLN D N +8548 C CA . GLN D 184 ? 1.0635 1.7206 1.3777 0.2104 -0.0260 -0.1057 183 GLN D CA +8549 C C . GLN D 184 ? 0.9526 1.6088 1.2683 0.2102 -0.0251 -0.1055 183 GLN D C +8550 O O . GLN D 184 ? 0.8477 1.5024 1.1642 0.2101 -0.0245 -0.1058 183 GLN D O +8551 C CB . GLN D 184 ? 1.0127 1.6675 1.3261 0.2116 -0.0255 -0.1063 183 GLN D CB +8552 C CG . GLN D 184 ? 1.0303 1.6842 1.3439 0.2123 -0.0250 -0.1062 183 GLN D CG +8553 C CD . GLN D 184 ? 1.1207 1.7721 1.4336 0.2135 -0.0246 -0.1069 183 GLN D CD +8554 O OE1 . GLN D 184 ? 0.7019 1.3527 1.0138 0.2138 -0.0248 -0.1074 183 GLN D OE1 +8555 N NE2 . GLN D 184 ? 0.7058 1.3556 1.0191 0.2141 -0.0238 -0.1069 183 GLN D NE2 +8556 N N . GLN D 185 ? 0.7924 1.4495 1.1085 0.2103 -0.0251 -0.1049 184 GLN D N +8557 C CA . GLN D 185 ? 0.8459 1.5020 1.1634 0.2103 -0.0242 -0.1047 184 GLN D CA +8558 C C . GLN D 185 ? 1.2386 1.8944 1.5563 0.2109 -0.0239 -0.1044 184 GLN D C +8559 O O . GLN D 185 ? 0.8392 1.4970 1.1563 0.2109 -0.0246 -0.1040 184 GLN D O +8560 C CB . GLN D 185 ? 1.1631 1.8212 1.4818 0.2091 -0.0245 -0.1042 184 GLN D CB +8561 C CG . GLN D 185 ? 1.6090 2.2703 1.9276 0.2084 -0.0255 -0.1033 184 GLN D CG +8562 C CD . GLN D 185 ? 1.9316 2.5948 2.2515 0.2072 -0.0257 -0.1028 184 GLN D CD +8563 O OE1 . GLN D 185 ? 2.0086 2.6711 2.3292 0.2067 -0.0253 -0.1031 184 GLN D OE1 +8564 N NE2 . GLN D 185 ? 2.0490 2.7147 2.3693 0.2066 -0.0263 -0.1019 184 GLN D NE2 +8565 N N . ASN D 186 ? 1.0853 1.7386 1.4038 0.2115 -0.0228 -0.1047 185 ASN D N +8566 C CA . ASN D 186 ? 1.0458 1.6983 1.3645 0.2123 -0.0224 -0.1045 185 ASN D CA +8567 C C . ASN D 186 ? 1.2658 1.9180 1.5863 0.2120 -0.0216 -0.1040 185 ASN D C +8568 O O . ASN D 186 ? 0.9777 1.6289 1.2992 0.2117 -0.0210 -0.1042 185 ASN D O +8569 C CB . ASN D 186 ? 0.9493 1.5989 1.2673 0.2134 -0.0218 -0.1052 185 ASN D CB +8570 C CG . ASN D 186 ? 1.0102 1.6602 1.3265 0.2138 -0.0226 -0.1056 185 ASN D CG +8571 O OD1 . ASN D 186 ? 0.9883 1.6380 1.3041 0.2136 -0.0228 -0.1061 185 ASN D OD1 +8572 N ND2 . ASN D 186 ? 0.8228 1.4736 1.1383 0.2143 -0.0229 -0.1055 185 ASN D ND2 +8573 N N . THR D 187 ? 1.1085 1.7615 1.4292 0.2123 -0.0217 -0.1034 186 THR D N +8574 C CA . THR D 187 ? 1.1499 1.8033 1.4724 0.2120 -0.0211 -0.1028 186 THR D CA +8575 C C . THR D 187 ? 0.9682 1.6216 1.2908 0.2127 -0.0209 -0.1024 186 THR D C +8576 O O . THR D 187 ? 1.2267 1.8820 1.5484 0.2127 -0.0217 -0.1020 186 THR D O +8577 C CB . THR D 187 ? 1.1343 1.7907 1.4573 0.2107 -0.0219 -0.1021 186 THR D CB +8578 O OG1 . THR D 187 ? 1.3632 2.0194 1.6867 0.2100 -0.0217 -0.1025 186 THR D OG1 +8579 C CG2 . THR D 187 ? 0.9233 1.5805 1.2479 0.2105 -0.0215 -0.1013 186 THR D CG2 +8580 N N . PRO D 188 ? 1.1529 1.8041 1.4768 0.2132 -0.0198 -0.1023 187 PRO D N +8581 C CA . PRO D 188 ? 1.2391 1.8901 1.5634 0.2139 -0.0194 -0.1019 187 PRO D CA +8582 C C . PRO D 188 ? 1.2375 1.8912 1.5623 0.2133 -0.0199 -0.1009 187 PRO D C +8583 O O . PRO D 188 ? 1.3416 1.9963 1.6679 0.2126 -0.0198 -0.1005 187 PRO D O +8584 C CB . PRO D 188 ? 1.1672 1.8154 1.4931 0.2144 -0.0181 -0.1020 187 PRO D CB +8585 C CG . PRO D 188 ? 1.0812 1.7291 1.4081 0.2136 -0.0177 -0.1023 187 PRO D CG +8586 C CD . PRO D 188 ? 1.0505 1.6995 1.3758 0.2132 -0.0187 -0.1027 187 PRO D CD +8587 N N . ILE D 189 ? 1.2715 1.9265 1.5953 0.2137 -0.0206 -0.1007 188 ILE D N +8588 C CA . ILE D 189 ? 1.2070 1.8642 1.5312 0.2135 -0.0209 -0.0998 188 ILE D CA +8589 C C . ILE D 189 ? 1.4121 2.0679 1.7382 0.2139 -0.0198 -0.0994 188 ILE D C +8590 O O . ILE D 189 ? 1.3336 1.9909 1.6609 0.2133 -0.0198 -0.0986 188 ILE D O +8591 C CB . ILE D 189 ? 0.9530 1.6112 1.2757 0.2141 -0.0216 -0.0998 188 ILE D CB +8592 C CG1 . ILE D 189 ? 1.0654 1.7246 1.3863 0.2138 -0.0225 -0.1003 188 ILE D CG1 +8593 C CG2 . ILE D 189 ? 0.9583 1.6189 1.2814 0.2138 -0.0219 -0.0988 188 ILE D CG2 +8594 C CD1 . ILE D 189 ? 1.1402 1.7999 1.4594 0.2145 -0.0231 -0.1005 188 ILE D CD1 +8595 N N . GLY D 190 ? 1.5371 2.1901 1.8634 0.2148 -0.0189 -0.0999 189 GLY D N +8596 C CA . GLY D 190 ? 1.5693 2.2206 1.8973 0.2153 -0.0178 -0.0995 189 GLY D CA +8597 C C . GLY D 190 ? 1.6757 2.3260 2.0057 0.2148 -0.0169 -0.0994 189 GLY D C +8598 O O . GLY D 190 ? 1.3502 2.0000 1.6801 0.2143 -0.0169 -0.0999 189 GLY D O +8599 N N . ASP D 191 ? 1.6625 2.3122 1.9942 0.2150 -0.0161 -0.0988 190 ASP D N +8600 C CA . ASP D 191 ? 1.7817 2.4307 2.1155 0.2144 -0.0152 -0.0986 190 ASP D CA +8601 C C . ASP D 191 ? 1.7326 2.3781 2.0674 0.2152 -0.0139 -0.0992 190 ASP D C +8602 O O . ASP D 191 ? 1.5540 2.1985 1.8904 0.2148 -0.0130 -0.0993 190 ASP D O +8603 C CB . ASP D 191 ? 1.7677 2.4183 2.1032 0.2141 -0.0151 -0.0976 190 ASP D CB +8604 C CG . ASP D 191 ? 1.9403 2.5943 2.2751 0.2132 -0.0163 -0.0970 190 ASP D CG +8605 O OD1 . ASP D 191 ? 1.7373 2.3927 2.0714 0.2124 -0.0170 -0.0973 190 ASP D OD1 +8606 O OD2 . ASP D 191 ? 2.0183 2.6739 2.3534 0.2133 -0.0166 -0.0963 190 ASP D OD2 +8607 N N . GLY D 192 ? 1.7636 2.4074 2.0975 0.2162 -0.0137 -0.0995 191 GLY D N +8608 C CA . GLY D 192 ? 1.7559 2.3964 2.0906 0.2170 -0.0124 -0.1000 191 GLY D CA +8609 C C . GLY D 192 ? 1.9068 2.5459 2.2409 0.2168 -0.0123 -0.1010 191 GLY D C +8610 O O . GLY D 192 ? 1.8417 2.4825 2.1743 0.2162 -0.0134 -0.1013 191 GLY D O +8611 N N . PRO D 193 ? 1.9478 2.5839 2.2830 0.2173 -0.0111 -0.1014 192 PRO D N +8612 C CA . PRO D 193 ? 1.9359 2.5706 2.2707 0.2171 -0.0108 -0.1022 192 PRO D CA +8613 C C . PRO D 193 ? 1.7969 2.4308 2.1296 0.2176 -0.0115 -0.1030 192 PRO D C +8614 O O . PRO D 193 ? 1.3451 1.9787 1.6770 0.2184 -0.0116 -0.1030 192 PRO D O +8615 C CB . PRO D 193 ? 1.7975 2.4292 2.1343 0.2176 -0.0092 -0.1024 192 PRO D CB +8616 C CG . PRO D 193 ? 1.6185 2.2494 1.9560 0.2185 -0.0087 -0.1019 192 PRO D CG +8617 C CD . PRO D 193 ? 1.6746 2.3086 2.0116 0.2181 -0.0098 -0.1011 192 PRO D CD +8618 N N . VAL D 194 ? 1.6278 2.2617 1.9596 0.2172 -0.0118 -0.1036 193 VAL D N +8619 C CA . VAL D 194 ? 1.4861 2.1195 1.8159 0.2176 -0.0124 -0.1043 193 VAL D CA +8620 C C . VAL D 194 ? 1.2172 1.8483 1.5473 0.2176 -0.0117 -0.1051 193 VAL D C +8621 O O . VAL D 194 ? 1.2398 1.8703 1.5713 0.2171 -0.0109 -0.1051 193 VAL D O +8622 C CB . VAL D 194 ? 1.5813 2.2177 1.9094 0.2168 -0.0139 -0.1043 193 VAL D CB +8623 C CG1 . VAL D 194 ? 1.0742 1.7129 1.4019 0.2168 -0.0147 -0.1035 193 VAL D CG1 +8624 C CG2 . VAL D 194 ? 1.4454 2.0831 1.7739 0.2157 -0.0142 -0.1043 193 VAL D CG2 +8625 N N . LEU D 195 ? 1.0887 1.7183 1.4173 0.2182 -0.0119 -0.1058 194 LEU D N +8626 C CA . LEU D 195 ? 0.9925 1.6198 1.3212 0.2183 -0.0112 -0.1066 194 LEU D CA +8627 C C . LEU D 195 ? 1.0962 1.7252 1.4240 0.2174 -0.0120 -0.1069 194 LEU D C +8628 O O . LEU D 195 ? 1.3700 2.0011 1.6963 0.2171 -0.0132 -0.1069 194 LEU D O +8629 C CB . LEU D 195 ? 0.9947 1.6200 1.3224 0.2193 -0.0111 -0.1072 194 LEU D CB +8630 C CG . LEU D 195 ? 1.2005 1.8242 1.5289 0.2203 -0.0104 -0.1069 194 LEU D CG +8631 C CD1 . LEU D 195 ? 1.1048 1.7265 1.4321 0.2212 -0.0103 -0.1075 194 LEU D CD1 +8632 C CD2 . LEU D 195 ? 0.7688 1.3908 1.0996 0.2204 -0.0089 -0.1066 194 LEU D CD2 +8633 N N . LEU D 196 ? 0.9463 1.5745 1.2752 0.2169 -0.0113 -0.1071 195 LEU D N +8634 C CA . LEU D 196 ? 1.3268 1.9566 1.6550 0.2159 -0.0120 -0.1074 195 LEU D CA +8635 C C . LEU D 196 ? 1.1742 1.8017 1.5019 0.2163 -0.0115 -0.1082 195 LEU D C +8636 O O . LEU D 196 ? 1.2648 1.8904 1.5938 0.2163 -0.0104 -0.1085 195 LEU D O +8637 C CB . LEU D 196 ? 1.6545 2.2858 1.9841 0.2149 -0.0118 -0.1069 195 LEU D CB +8638 C CG . LEU D 196 ? 1.3911 2.0245 1.7214 0.2147 -0.0122 -0.1060 195 LEU D CG +8639 C CD1 . LEU D 196 ? 1.2068 1.8415 1.5387 0.2137 -0.0119 -0.1056 195 LEU D CD1 +8640 C CD2 . LEU D 196 ? 1.1327 1.7687 1.4612 0.2145 -0.0137 -0.1057 195 LEU D CD2 +8641 N N . PRO D 197 ? 1.1739 1.8017 1.4998 0.2165 -0.0124 -0.1086 196 PRO D N +8642 C CA . PRO D 197 ? 1.2255 1.8510 1.5508 0.2170 -0.0120 -0.1094 196 PRO D CA +8643 C C . PRO D 197 ? 1.1711 1.7961 1.4966 0.2164 -0.0117 -0.1099 196 PRO D C +8644 O O . PRO D 197 ? 1.1981 1.8252 1.5239 0.2155 -0.0121 -0.1097 196 PRO D O +8645 C CB . PRO D 197 ? 1.1368 1.7636 1.4600 0.2172 -0.0133 -0.1096 196 PRO D CB +8646 C CG . PRO D 197 ? 1.0833 1.7135 1.4062 0.2164 -0.0144 -0.1089 196 PRO D CG +8647 C CD . PRO D 197 ? 0.9826 1.6131 1.3071 0.2163 -0.0138 -0.1083 196 PRO D CD +8648 N N . ASP D 198 ? 1.3249 1.9472 1.6504 0.2170 -0.0109 -0.1106 197 ASP D N +8649 C CA . ASP D 198 ? 1.3979 2.0197 1.7231 0.2166 -0.0108 -0.1111 197 ASP D CA +8650 C C . ASP D 198 ? 1.1492 1.7726 1.4725 0.2165 -0.0121 -0.1113 197 ASP D C +8651 O O . ASP D 198 ? 1.1045 1.7285 1.4268 0.2169 -0.0129 -0.1112 197 ASP D O +8652 C CB . ASP D 198 ? 1.4457 2.0640 1.7717 0.2174 -0.0094 -0.1118 197 ASP D CB +8653 C CG . ASP D 198 ? 1.5915 2.2082 1.9195 0.2174 -0.0079 -0.1116 197 ASP D CG +8654 O OD1 . ASP D 198 ? 1.5488 2.1672 1.8777 0.2167 -0.0079 -0.1111 197 ASP D OD1 +8655 O OD2 . ASP D 198 ? 1.3760 1.9896 1.7048 0.2182 -0.0066 -0.1120 197 ASP D OD2 +8656 N N . ASN D 199 ? 1.0244 1.6484 1.3472 0.2159 -0.0124 -0.1116 198 ASN D N +8657 C CA . ASN D 199 ? 1.2510 1.8764 1.5722 0.2157 -0.0136 -0.1118 198 ASN D CA +8658 C C . ASN D 199 ? 1.1970 1.8205 1.5173 0.2167 -0.0136 -0.1123 198 ASN D C +8659 O O . ASN D 199 ? 1.1130 1.7336 1.4336 0.2173 -0.0126 -0.1128 198 ASN D O +8660 C CB . ASN D 199 ? 1.5007 2.1265 1.8218 0.2150 -0.0137 -0.1122 198 ASN D CB +8661 C CG . ASN D 199 ? 1.4894 2.1177 1.8112 0.2139 -0.0141 -0.1117 198 ASN D CG +8662 O OD1 . ASN D 199 ? 0.8121 1.4414 1.1347 0.2136 -0.0140 -0.1112 198 ASN D OD1 +8663 N ND2 . ASN D 199 ? 1.4537 2.0832 1.7752 0.2132 -0.0145 -0.1119 198 ASN D ND2 +8664 N N . HIS D 200 ? 1.1047 1.7296 1.4237 0.2169 -0.0146 -0.1121 199 HIS D N +8665 C CA . HIS D 200 ? 1.0805 1.7041 1.3984 0.2178 -0.0148 -0.1126 199 HIS D CA +8666 C C . HIS D 200 ? 0.9426 1.5687 1.2590 0.2175 -0.0163 -0.1124 199 HIS D C +8667 O O . HIS D 200 ? 1.0477 1.6766 1.3641 0.2167 -0.0170 -0.1119 199 HIS D O +8668 C CB . HIS D 200 ? 0.9003 1.5219 1.2186 0.2187 -0.0141 -0.1126 199 HIS D CB +8669 C CG . HIS D 200 ? 0.9003 1.5238 1.2186 0.2187 -0.0147 -0.1119 199 HIS D CG +8670 N ND1 . HIS D 200 ? 1.0742 1.6988 1.3936 0.2182 -0.0144 -0.1113 199 HIS D ND1 +8671 C CD2 . HIS D 200 ? 0.9700 1.5944 1.2873 0.2191 -0.0154 -0.1118 199 HIS D CD2 +8672 C CE1 . HIS D 200 ? 1.0516 1.6777 1.3707 0.2183 -0.0150 -0.1108 199 HIS D CE1 +8673 N NE2 . HIS D 200 ? 1.0859 1.7120 1.4037 0.2189 -0.0156 -0.1111 199 HIS D NE2 +8674 N N . TYR D 201 ? 0.7078 1.3332 1.0232 0.2182 -0.0166 -0.1128 200 TYR D N +8675 C CA . TYR D 201 ? 0.8747 1.5024 1.1887 0.2180 -0.0179 -0.1126 200 TYR D CA +8676 C C . TYR D 201 ? 0.8979 1.5251 1.2112 0.2189 -0.0181 -0.1127 200 TYR D C +8677 O O . TYR D 201 ? 0.8794 1.5042 1.1932 0.2197 -0.0172 -0.1130 200 TYR D O +8678 C CB . TYR D 201 ? 0.8309 1.4589 1.1442 0.2177 -0.0183 -0.1130 200 TYR D CB +8679 C CG . TYR D 201 ? 1.0260 1.6513 1.3389 0.2185 -0.0178 -0.1137 200 TYR D CG +8680 C CD1 . TYR D 201 ? 1.0312 1.6539 1.3449 0.2187 -0.0167 -0.1141 200 TYR D CD1 +8681 C CD2 . TYR D 201 ? 1.0421 1.6675 1.3539 0.2190 -0.0184 -0.1140 200 TYR D CD2 +8682 C CE1 . TYR D 201 ? 0.9793 1.5996 1.2928 0.2195 -0.0162 -0.1148 200 TYR D CE1 +8683 C CE2 . TYR D 201 ? 1.2041 1.8270 1.5156 0.2198 -0.0180 -0.1146 200 TYR D CE2 +8684 C CZ . TYR D 201 ? 1.0613 1.6817 1.3736 0.2200 -0.0169 -0.1150 200 TYR D CZ +8685 O OH . TYR D 201 ? 0.9844 1.6024 1.2965 0.2207 -0.0164 -0.1157 200 TYR D OH +8686 N N . LEU D 202 ? 0.9135 1.5429 1.2257 0.2188 -0.0191 -0.1125 201 LEU D N +8687 C CA . LEU D 202 ? 0.9608 1.5899 1.2722 0.2196 -0.0194 -0.1127 201 LEU D CA +8688 C C . LEU D 202 ? 0.7183 1.3477 1.0285 0.2197 -0.0201 -0.1131 201 LEU D C +8689 O O . LEU D 202 ? 0.5730 1.2046 0.8827 0.2190 -0.0209 -0.1129 201 LEU D O +8690 C CB . LEU D 202 ? 0.5779 1.2094 0.8891 0.2194 -0.0200 -0.1120 201 LEU D CB +8691 C CG . LEU D 202 ? 0.9089 1.5407 1.2212 0.2192 -0.0195 -0.1114 201 LEU D CG +8692 C CD1 . LEU D 202 ? 0.6977 1.3314 1.0095 0.2193 -0.0202 -0.1110 201 LEU D CD1 +8693 C CD2 . LEU D 202 ? 1.1089 1.7377 1.4222 0.2199 -0.0183 -0.1117 201 LEU D CD2 +8694 N N . SER D 203 ? 0.7224 1.3496 1.0322 0.2205 -0.0197 -0.1137 202 SER D N +8695 C CA . SER D 203 ? 0.7861 1.4135 1.0949 0.2207 -0.0203 -0.1142 202 SER D CA +8696 C C . SER D 203 ? 0.6243 1.2533 0.9322 0.2210 -0.0211 -0.1140 202 SER D C +8697 O O . SER D 203 ? 1.0497 1.6775 1.3576 0.2217 -0.0208 -0.1142 202 SER D O +8698 C CB . SER D 203 ? 0.5421 1.1664 0.8510 0.2214 -0.0196 -0.1149 202 SER D CB +8699 O OG . SER D 203 ? 1.0204 1.6448 1.3284 0.2217 -0.0201 -0.1153 202 SER D OG +8700 N N . THR D 204 ? 0.8061 1.4377 1.1133 0.2204 -0.0221 -0.1137 203 THR D N +8701 C CA . THR D 204 ? 0.9517 1.5850 1.2581 0.2206 -0.0228 -0.1136 203 THR D CA +8702 C C . THR D 204 ? 0.8726 1.5060 1.1781 0.2209 -0.0233 -0.1141 203 THR D C +8703 O O . THR D 204 ? 0.9429 1.5762 1.2482 0.2206 -0.0235 -0.1143 203 THR D O +8704 C CB . THR D 204 ? 0.8743 1.5109 1.1807 0.2198 -0.0236 -0.1129 203 THR D CB +8705 O OG1 . THR D 204 ? 0.7465 1.3831 1.0538 0.2194 -0.0231 -0.1124 203 THR D OG1 +8706 C CG2 . THR D 204 ? 1.4263 2.0643 1.7320 0.2202 -0.0241 -0.1127 203 THR D CG2 +8707 N N . GLN D 205 ? 0.8118 1.4452 1.1165 0.2216 -0.0236 -0.1144 204 GLN D N +8708 C CA . GLN D 205 ? 0.7994 1.4334 1.1032 0.2218 -0.0242 -0.1148 204 GLN D CA +8709 C C . GLN D 205 ? 0.8289 1.4649 1.1322 0.2220 -0.0248 -0.1146 204 GLN D C +8710 O O . GLN D 205 ? 0.5185 1.1542 0.8218 0.2223 -0.0245 -0.1144 204 GLN D O +8711 C CB . GLN D 205 ? 0.8090 1.4402 1.1127 0.2227 -0.0237 -0.1156 204 GLN D CB +8712 C CG . GLN D 205 ? 0.6006 1.2294 0.9050 0.2227 -0.0229 -0.1158 204 GLN D CG +8713 C CD . GLN D 205 ? 0.9634 1.5893 1.2681 0.2235 -0.0221 -0.1164 204 GLN D CD +8714 O OE1 . GLN D 205 ? 1.5434 2.1680 1.8478 0.2241 -0.0220 -0.1170 204 GLN D OE1 +8715 N NE2 . GLN D 205 ? 0.9144 1.5394 1.2200 0.2236 -0.0214 -0.1161 204 GLN D NE2 +8716 N N . SER D 206 ? 0.6353 1.2732 0.9379 0.2217 -0.0256 -0.1145 205 SER D N +8717 C CA . SER D 206 ? 0.5034 1.1436 0.8054 0.2218 -0.0263 -0.1143 205 SER D CA +8718 C C . SER D 206 ? 0.3686 1.0095 0.6698 0.2220 -0.0268 -0.1147 205 SER D C +8719 O O . SER D 206 ? 0.8652 1.5057 1.1665 0.2218 -0.0269 -0.1149 205 SER D O +8720 C CB . SER D 206 ? 0.5441 1.1871 0.8464 0.2209 -0.0267 -0.1134 205 SER D CB +8721 O OG . SER D 206 ? 1.0532 1.6956 1.3562 0.2206 -0.0262 -0.1130 205 SER D OG +8722 N N . ASN D 207 ? 0.5723 1.2142 0.8729 0.2224 -0.0272 -0.1148 206 ASN D N +8723 C CA . ASN D 207 ? 0.6176 1.2608 0.9176 0.2225 -0.0278 -0.1151 206 ASN D CA +8724 C C . ASN D 207 ? 0.8880 1.5339 1.1876 0.2224 -0.0284 -0.1146 206 ASN D C +8725 O O . ASN D 207 ? 0.5399 1.1860 0.8395 0.2226 -0.0282 -0.1144 206 ASN D O +8726 C CB . ASN D 207 ? 0.5010 1.1421 0.8006 0.2234 -0.0276 -0.1160 206 ASN D CB +8727 C CG . ASN D 207 ? 0.6225 1.2647 0.9213 0.2239 -0.0280 -0.1163 206 ASN D CG +8728 O OD1 . ASN D 207 ? 0.4816 1.1248 0.7803 0.2240 -0.0281 -0.1160 206 ASN D OD1 +8729 N ND2 . ASN D 207 ? 0.3425 0.9847 0.6411 0.2241 -0.0283 -0.1168 206 ASN D ND2 +8730 N N . LEU D 208 ? 0.5934 1.2413 0.8927 0.2220 -0.0291 -0.1145 207 LEU D N +8731 C CA . LEU D 208 ? 0.3413 0.9919 0.6402 0.2218 -0.0297 -0.1141 207 LEU D CA +8732 C C . LEU D 208 ? 0.3419 0.9930 0.6403 0.2224 -0.0300 -0.1146 207 LEU D C +8733 O O . LEU D 208 ? 0.7919 1.4424 1.0901 0.2225 -0.0302 -0.1150 207 LEU D O +8734 C CB . LEU D 208 ? 0.7018 1.3547 1.0011 0.2209 -0.0302 -0.1133 207 LEU D CB +8735 C CG . LEU D 208 ? 0.4940 1.1465 0.7941 0.2202 -0.0300 -0.1129 207 LEU D CG +8736 C CD1 . LEU D 208 ? 0.7438 1.3986 1.0442 0.2194 -0.0306 -0.1122 207 LEU D CD1 +8737 C CD2 . LEU D 208 ? 0.5103 1.1629 0.8107 0.2201 -0.0296 -0.1124 207 LEU D CD2 +8738 N N . SER D 209 ? 0.6789 1.3310 0.9768 0.2227 -0.0302 -0.1146 208 SER D N +8739 C CA . SER D 209 ? 0.4598 1.1124 0.7570 0.2233 -0.0304 -0.1152 208 SER D CA +8740 C C . SER D 209 ? 0.8007 1.4560 1.0976 0.2232 -0.0309 -0.1148 208 SER D C +8741 O O . SER D 209 ? 0.4805 1.1372 0.7776 0.2227 -0.0310 -0.1141 208 SER D O +8742 C CB . SER D 209 ? 0.4833 1.1334 0.7803 0.2242 -0.0299 -0.1160 208 SER D CB +8743 O OG . SER D 209 ? 0.7986 1.4479 1.0958 0.2242 -0.0294 -0.1157 208 SER D OG +8744 N N . LYS D 210 ? 0.7481 1.4040 1.0445 0.2236 -0.0312 -0.1153 209 LYS D N +8745 C CA . LYS D 210 ? 0.4979 1.1562 0.7938 0.2236 -0.0317 -0.1151 209 LYS D CA +8746 C C . LYS D 210 ? 0.7244 1.3819 1.0197 0.2245 -0.0314 -0.1158 209 LYS D C +8747 O O . LYS D 210 ? 0.8417 1.4974 1.1368 0.2251 -0.0313 -0.1166 209 LYS D O +8748 C CB . LYS D 210 ? 0.7830 1.4431 1.0789 0.2234 -0.0322 -0.1151 209 LYS D CB +8749 C CG . LYS D 210 ? 0.6544 1.3158 0.9510 0.2226 -0.0326 -0.1144 209 LYS D CG +8750 C CD . LYS D 210 ? 0.7744 1.4379 1.0713 0.2219 -0.0328 -0.1135 209 LYS D CD +8751 C CE . LYS D 210 ? 0.5971 1.2621 0.8945 0.2211 -0.0332 -0.1128 209 LYS D CE +8752 N NZ . LYS D 210 ? 0.6521 1.3184 0.9499 0.2204 -0.0332 -0.1119 209 LYS D NZ +8753 N N . ASP D 211 ? 0.8981 1.5569 1.1932 0.2245 -0.0315 -0.1154 210 ASP D N +8754 C CA . ASP D 211 ? 0.5827 1.2418 0.8771 0.2252 -0.0315 -0.1159 210 ASP D CA +8755 C C . ASP D 211 ? 0.7537 1.4146 1.0477 0.2253 -0.0320 -0.1162 210 ASP D C +8756 O O . ASP D 211 ? 0.8562 1.5195 1.1504 0.2248 -0.0325 -0.1157 210 ASP D O +8757 C CB . ASP D 211 ? 0.6252 1.2856 0.9196 0.2251 -0.0314 -0.1152 210 ASP D CB +8758 C CG . ASP D 211 ? 1.0234 1.6837 1.3172 0.2258 -0.0313 -0.1157 210 ASP D CG +8759 O OD1 . ASP D 211 ? 0.9579 1.6178 1.2513 0.2264 -0.0314 -0.1165 210 ASP D OD1 +8760 O OD2 . ASP D 211 ? 0.9403 1.6010 1.2342 0.2259 -0.0311 -0.1152 210 ASP D OD2 +8761 N N . PRO D 212 ? 0.9920 1.6520 1.2856 0.2260 -0.0320 -0.1171 211 PRO D N +8762 C CA . PRO D 212 ? 0.9931 1.6547 1.2864 0.2262 -0.0325 -0.1175 211 PRO D CA +8763 C C . PRO D 212 ? 1.0321 1.6959 1.3249 0.2264 -0.0327 -0.1174 211 PRO D C +8764 O O . PRO D 212 ? 0.7624 1.4276 1.0549 0.2265 -0.0331 -0.1178 211 PRO D O +8765 C CB . PRO D 212 ? 0.9409 1.6004 1.2341 0.2268 -0.0323 -0.1185 211 PRO D CB +8766 C CG . PRO D 212 ? 0.9352 1.5924 1.2283 0.2273 -0.0317 -0.1188 211 PRO D CG +8767 C CD . PRO D 212 ? 0.6995 1.3566 0.9930 0.2267 -0.0315 -0.1179 211 PRO D CD +8768 N N . ASN D 213 ? 1.3235 1.9875 1.6161 0.2264 -0.0325 -0.1170 212 ASN D N +8769 C CA . ASN D 213 ? 1.4728 2.1390 1.7649 0.2266 -0.0327 -0.1168 212 ASN D CA +8770 C C . ASN D 213 ? 1.2441 1.9122 1.5365 0.2259 -0.0328 -0.1157 212 ASN D C +8771 O O . ASN D 213 ? 1.0573 1.7266 1.3495 0.2259 -0.0328 -0.1153 212 ASN D O +8772 C CB . ASN D 213 ? 1.1920 1.8570 1.4836 0.2273 -0.0324 -0.1173 212 ASN D CB +8773 C CG . ASN D 213 ? 0.9937 1.6564 1.2851 0.2280 -0.0322 -0.1184 212 ASN D CG +8774 O OD1 . ASN D 213 ? 0.9332 1.5962 1.2245 0.2281 -0.0324 -0.1190 212 ASN D OD1 +8775 N ND2 . ASN D 213 ? 1.0879 1.7483 1.3794 0.2284 -0.0317 -0.1186 212 ASN D ND2 +8776 N N . GLU D 214 ? 0.9897 1.6580 1.2828 0.2252 -0.0330 -0.1152 213 GLU D N +8777 C CA . GLU D 214 ? 0.7159 1.3858 1.0094 0.2244 -0.0331 -0.1141 213 GLU D CA +8778 C C . GLU D 214 ? 0.7311 1.4029 1.0250 0.2238 -0.0336 -0.1137 213 GLU D C +8779 O O . GLU D 214 ? 0.8211 1.4920 1.1154 0.2236 -0.0336 -0.1139 213 GLU D O +8780 C CB . GLU D 214 ? 0.6891 1.3570 0.9831 0.2241 -0.0327 -0.1138 213 GLU D CB +8781 C CG . GLU D 214 ? 0.5993 1.2689 0.8939 0.2233 -0.0328 -0.1127 213 GLU D CG +8782 C CD . GLU D 214 ? 1.0421 1.7138 1.3364 0.2234 -0.0329 -0.1123 213 GLU D CD +8783 O OE1 . GLU D 214 ? 0.7976 1.4685 1.0919 0.2237 -0.0325 -0.1121 213 GLU D OE1 +8784 O OE2 . GLU D 214 ? 1.2573 1.9313 1.5515 0.2232 -0.0334 -0.1120 213 GLU D OE2 +8785 N N . LYS D 215 ? 0.8944 1.5689 1.1883 0.2235 -0.0340 -0.1131 214 LYS D N +8786 C CA . LYS D 215 ? 1.0437 1.7203 1.3380 0.2229 -0.0345 -0.1128 214 LYS D CA +8787 C C . LYS D 215 ? 0.8736 1.5517 1.1686 0.2220 -0.0347 -0.1117 214 LYS D C +8788 O O . LYS D 215 ? 0.8890 1.5685 1.1845 0.2215 -0.0351 -0.1113 214 LYS D O +8789 C CB . LYS D 215 ? 0.7338 1.4124 1.0277 0.2233 -0.0348 -0.1131 214 LYS D CB +8790 C CG . LYS D 215 ? 1.3900 2.0672 1.6833 0.2241 -0.0347 -0.1142 214 LYS D CG +8791 C CD . LYS D 215 ? 1.4961 2.1755 1.7891 0.2243 -0.0350 -0.1145 214 LYS D CD +8792 C CE . LYS D 215 ? 1.3692 2.0502 1.6617 0.2246 -0.0350 -0.1143 214 LYS D CE +8793 N NZ . LYS D 215 ? 1.1974 1.8766 1.4891 0.2254 -0.0347 -0.1151 214 LYS D NZ +8794 N N . ARG D 216 ? 0.4528 1.1308 0.7480 0.2218 -0.0344 -0.1111 215 ARG D N +8795 C CA . ARG D 216 ? 0.6710 1.3501 0.9669 0.2209 -0.0346 -0.1101 215 ARG D CA +8796 C C . ARG D 216 ? 0.5795 1.2567 0.8759 0.2206 -0.0344 -0.1102 215 ARG D C +8797 O O . ARG D 216 ? 0.8787 1.5534 1.1748 0.2211 -0.0341 -0.1109 215 ARG D O +8798 C CB . ARG D 216 ? 0.6051 1.2844 0.9010 0.2209 -0.0343 -0.1096 215 ARG D CB +8799 C CG . ARG D 216 ? 0.9146 1.5959 1.2100 0.2211 -0.0345 -0.1094 215 ARG D CG +8800 C CD . ARG D 216 ? 0.7764 1.4573 1.0717 0.2213 -0.0341 -0.1091 215 ARG D CD +8801 N NE . ARG D 216 ? 1.1068 1.7852 1.4016 0.2221 -0.0336 -0.1099 215 ARG D NE +8802 C CZ . ARG D 216 ? 1.0531 1.7306 1.3478 0.2225 -0.0332 -0.1098 215 ARG D CZ +8803 N NH1 . ARG D 216 ? 0.9228 1.6016 1.2179 0.2221 -0.0332 -0.1089 215 ARG D NH1 +8804 N NH2 . ARG D 216 ? 0.6926 1.3678 0.9868 0.2233 -0.0328 -0.1106 215 ARG D NH2 +8805 N N . ASP D 217 ? 0.5970 1.2754 0.8942 0.2197 -0.0346 -0.1093 216 ASP D N +8806 C CA . ASP D 217 ? 0.8380 1.5147 1.1356 0.2194 -0.0345 -0.1093 216 ASP D CA +8807 C C . ASP D 217 ? 0.9507 1.6251 1.2483 0.2196 -0.0339 -0.1095 216 ASP D C +8808 O O . ASP D 217 ? 0.7355 1.4104 1.0333 0.2194 -0.0337 -0.1089 216 ASP D O +8809 C CB . ASP D 217 ? 0.7630 1.4417 1.0614 0.2184 -0.0349 -0.1084 216 ASP D CB +8810 C CG . ASP D 217 ? 1.1068 1.7844 1.4057 0.2181 -0.0350 -0.1085 216 ASP D CG +8811 O OD1 . ASP D 217 ? 1.2251 1.9009 1.5237 0.2186 -0.0348 -0.1093 216 ASP D OD1 +8812 O OD2 . ASP D 217 ? 0.6243 1.3030 0.9239 0.2172 -0.0352 -0.1077 216 ASP D OD2 +8813 N N . HIS D 218 ? 0.8367 1.5085 1.1341 0.2201 -0.0335 -0.1102 217 HIS D N +8814 C CA . HIS D 218 ? 0.7022 1.3715 0.9996 0.2205 -0.0329 -0.1105 217 HIS D CA +8815 C C . HIS D 218 ? 0.5216 1.1883 0.8192 0.2206 -0.0325 -0.1110 217 HIS D C +8816 O O . HIS D 218 ? 0.7814 1.4478 1.0790 0.2206 -0.0327 -0.1114 217 HIS D O +8817 C CB . HIS D 218 ? 0.5165 1.1851 0.8132 0.2214 -0.0326 -0.1111 217 HIS D CB +8818 C CG . HIS D 218 ? 0.4881 1.1553 0.7843 0.2220 -0.0326 -0.1121 217 HIS D CG +8819 N ND1 . HIS D 218 ? 1.0432 1.7116 1.3392 0.2220 -0.0331 -0.1124 217 HIS D ND1 +8820 C CD2 . HIS D 218 ? 0.7009 1.3654 0.9967 0.2228 -0.0321 -0.1129 217 HIS D CD2 +8821 C CE1 . HIS D 218 ? 0.6503 1.3169 0.9459 0.2227 -0.0329 -0.1133 217 HIS D CE1 +8822 N NE2 . HIS D 218 ? 0.8376 1.5019 1.1331 0.2231 -0.0323 -0.1136 217 HIS D NE2 +8823 N N . MET D 219 ? 0.6108 1.2757 0.9087 0.2206 -0.0320 -0.1110 218 MET D N +8824 C CA . MET D 219 ? 0.5708 1.2329 0.8689 0.2209 -0.0315 -0.1115 218 MET D CA +8825 C C . MET D 219 ? 0.6475 1.3073 0.9455 0.2216 -0.0309 -0.1120 218 MET D C +8826 O O . MET D 219 ? 0.6531 1.3131 0.9513 0.2215 -0.0306 -0.1115 218 MET D O +8827 C CB . MET D 219 ? 0.6093 1.2714 0.9082 0.2200 -0.0315 -0.1110 218 MET D CB +8828 C CG . MET D 219 ? 0.3409 1.0002 0.6401 0.2202 -0.0309 -0.1114 218 MET D CG +8829 S SD . MET D 219 ? 0.6478 1.3072 0.9479 0.2193 -0.0308 -0.1108 218 MET D SD +8830 C CE . MET D 219 ? 0.5720 1.2318 0.8725 0.2191 -0.0305 -0.1101 218 MET D CE +8831 N N . VAL D 220 ? 0.6710 1.3286 0.9686 0.2223 -0.0306 -0.1129 219 VAL D N +8832 C CA . VAL D 220 ? 0.5258 1.1808 0.8235 0.2229 -0.0299 -0.1133 219 VAL D CA +8833 C C . VAL D 220 ? 0.4082 1.0611 0.7065 0.2226 -0.0294 -0.1133 219 VAL D C +8834 O O . VAL D 220 ? 0.6436 1.2956 0.9420 0.2226 -0.0294 -0.1137 219 VAL D O +8835 C CB . VAL D 220 ? 0.5576 1.2111 0.8547 0.2238 -0.0298 -0.1143 219 VAL D CB +8836 C CG1 . VAL D 220 ? 0.3540 1.0054 0.6511 0.2244 -0.0291 -0.1146 219 VAL D CG1 +8837 C CG2 . VAL D 220 ? 0.7011 1.3567 0.9975 0.2240 -0.0303 -0.1145 219 VAL D CG2 +8838 N N . LEU D 221 ? 0.6805 1.3328 0.9794 0.2225 -0.0290 -0.1129 220 LEU D N +8839 C CA . LEU D 221 ? 0.6329 1.2834 0.9326 0.2222 -0.0285 -0.1128 220 LEU D CA +8840 C C . LEU D 221 ? 0.6227 1.2702 0.9226 0.2228 -0.0277 -0.1133 220 LEU D C +8841 O O . LEU D 221 ? 0.8248 1.4721 1.1250 0.2231 -0.0273 -0.1130 220 LEU D O +8842 C CB . LEU D 221 ? 0.5255 1.1774 0.8258 0.2213 -0.0285 -0.1119 220 LEU D CB +8843 C CG . LEU D 221 ? 0.5011 1.1512 0.8023 0.2210 -0.0279 -0.1118 220 LEU D CG +8844 C CD1 . LEU D 221 ? 0.5638 1.2133 0.8650 0.2208 -0.0281 -0.1121 220 LEU D CD1 +8845 C CD2 . LEU D 221 ? 0.6207 1.2722 0.9227 0.2203 -0.0279 -0.1109 220 LEU D CD2 +8846 N N . LEU D 222 ? 1.2599 1.9053 1.5600 0.2231 -0.0273 -0.1139 221 LEU D N +8847 C CA . LEU D 222 ? 0.7261 1.3686 1.0266 0.2236 -0.0265 -0.1143 221 LEU D CA +8848 C C . LEU D 222 ? 0.8851 1.5262 1.1864 0.2232 -0.0261 -0.1141 221 LEU D C +8849 O O . LEU D 222 ? 0.7141 1.3548 1.0153 0.2230 -0.0262 -0.1144 221 LEU D O +8850 C CB . LEU D 222 ? 0.6179 1.2585 0.9179 0.2244 -0.0264 -0.1152 221 LEU D CB +8851 C CG . LEU D 222 ? 0.9174 1.5588 1.2167 0.2250 -0.0267 -0.1155 221 LEU D CG +8852 C CD1 . LEU D 222 ? 0.4120 1.0517 0.7108 0.2257 -0.0266 -0.1164 221 LEU D CD1 +8853 C CD2 . LEU D 222 ? 0.7798 1.4206 1.0793 0.2254 -0.0262 -0.1152 221 LEU D CD2 +8854 N N . GLU D 223 ? 0.6140 1.2543 0.9160 0.2231 -0.0255 -0.1137 222 GLU D N +8855 C CA . GLU D 223 ? 0.7271 1.3660 1.0300 0.2227 -0.0249 -0.1136 222 GLU D CA +8856 C C . GLU D 223 ? 0.7015 1.3373 1.0050 0.2234 -0.0240 -0.1140 222 GLU D C +8857 O O . GLU D 223 ? 0.7503 1.3854 1.0539 0.2240 -0.0237 -0.1140 222 GLU D O +8858 C CB . GLU D 223 ? 0.5894 1.2298 0.8930 0.2220 -0.0249 -0.1127 222 GLU D CB +8859 C CG . GLU D 223 ? 1.2992 1.9419 1.6028 0.2211 -0.0256 -0.1123 222 GLU D CG +8860 C CD . GLU D 223 ? 1.7093 2.3533 2.0138 0.2204 -0.0255 -0.1115 222 GLU D CD +8861 O OE1 . GLU D 223 ? 1.6499 2.2924 1.9552 0.2206 -0.0247 -0.1114 222 GLU D OE1 +8862 O OE2 . GLU D 223 ? 1.7040 2.3505 2.0084 0.2197 -0.0261 -0.1109 222 GLU D OE2 +8863 N N . PHE D 224 ? 0.9068 1.5408 1.2107 0.2233 -0.0236 -0.1143 223 PHE D N +8864 C CA . PHE D 224 ? 0.5872 1.2183 0.8919 0.2238 -0.0226 -0.1146 223 PHE D CA +8865 C C . PHE D 224 ? 0.4183 1.0492 0.7240 0.2231 -0.0222 -0.1142 223 PHE D C +8866 O O . PHE D 224 ? 0.8459 1.4779 1.1516 0.2224 -0.0225 -0.1140 223 PHE D O +8867 C CB . PHE D 224 ? 0.6271 1.2560 0.9315 0.2242 -0.0224 -0.1154 223 PHE D CB +8868 C CG . PHE D 224 ? 0.8307 1.4598 1.1343 0.2249 -0.0228 -0.1159 223 PHE D CG +8869 C CD1 . PHE D 224 ? 0.7174 1.3476 1.0205 0.2252 -0.0231 -0.1158 223 PHE D CD1 +8870 C CD2 . PHE D 224 ? 0.5618 1.1898 0.8650 0.2251 -0.0229 -0.1166 223 PHE D CD2 +8871 C CE1 . PHE D 224 ? 0.6163 1.2467 0.9186 0.2258 -0.0235 -0.1163 223 PHE D CE1 +8872 C CE2 . PHE D 224 ? 0.7576 1.3856 1.0600 0.2257 -0.0233 -0.1171 223 PHE D CE2 +8873 C CZ . PHE D 224 ? 0.9114 1.5406 1.2133 0.2260 -0.0235 -0.1170 223 PHE D CZ +8874 N N . VAL D 225 ? 0.7223 1.3520 1.0290 0.2233 -0.0214 -0.1139 224 VAL D N +8875 C CA . VAL D 225 ? 0.7200 1.3494 1.0277 0.2226 -0.0209 -0.1135 224 VAL D CA +8876 C C . VAL D 225 ? 0.8718 1.4983 1.1806 0.2231 -0.0198 -0.1137 224 VAL D C +8877 O O . VAL D 225 ? 0.8146 1.4402 1.1238 0.2236 -0.0193 -0.1136 224 VAL D O +8878 C CB . VAL D 225 ? 0.7133 1.3452 1.0214 0.2221 -0.0212 -0.1127 224 VAL D CB +8879 C CG1 . VAL D 225 ? 0.8155 1.4478 1.1243 0.2212 -0.0211 -0.1123 224 VAL D CG1 +8880 C CG2 . VAL D 225 ? 0.7945 1.4292 1.1015 0.2218 -0.0223 -0.1124 224 VAL D CG2 +8881 N N . THR D 226 ? 0.8453 1.4703 1.1546 0.2229 -0.0193 -0.1140 225 THR D N +8882 C CA . THR D 226 ? 0.9310 1.5533 1.2415 0.2233 -0.0181 -0.1141 225 THR D CA +8883 C C . THR D 226 ? 0.8598 1.4820 1.1713 0.2226 -0.0176 -0.1138 225 THR D C +8884 O O . THR D 226 ? 0.8011 1.4240 1.1123 0.2220 -0.0180 -0.1139 225 THR D O +8885 C CB . THR D 226 ? 0.7626 1.3822 1.0729 0.2239 -0.0176 -0.1149 225 THR D CB +8886 O OG1 . THR D 226 ? 0.6828 1.3025 0.9923 0.2246 -0.0181 -0.1152 225 THR D OG1 +8887 C CG2 . THR D 226 ? 1.0020 1.6187 1.3136 0.2244 -0.0163 -0.1150 225 THR D CG2 +8888 N N . ALA D 227 ? 0.7604 1.3817 1.0732 0.2226 -0.0168 -0.1135 226 ALA D N +8889 C CA . ALA D 227 ? 0.7501 1.3710 1.0640 0.2220 -0.0161 -0.1133 226 ALA D CA +8890 C C . ALA D 227 ? 0.8684 1.4863 1.1828 0.2223 -0.0152 -0.1139 226 ALA D C +8891 O O . ALA D 227 ? 0.9899 1.6055 1.3043 0.2232 -0.0147 -0.1143 226 ALA D O +8892 C CB . ALA D 227 ? 0.7489 1.3697 1.0640 0.2220 -0.0155 -0.1127 226 ALA D CB +8893 N N . ALA D 228 ? 0.8251 1.4432 1.1398 0.2217 -0.0151 -0.1139 227 ALA D N +8894 C CA . ALA D 228 ? 0.9994 1.6152 1.3145 0.2219 -0.0143 -0.1145 227 ALA D CA +8895 C C . ALA D 228 ? 1.0680 1.6841 1.3839 0.2211 -0.0140 -0.1144 227 ALA D C +8896 O O . ALA D 228 ? 0.9864 1.6040 1.3030 0.2205 -0.0140 -0.1138 227 ALA D O +8897 C CB . ALA D 228 ? 0.6954 1.3114 1.0092 0.2220 -0.0151 -0.1150 227 ALA D CB +8898 N N . GLY D 229 ? 1.0654 1.6801 1.3814 0.2210 -0.0135 -0.1149 228 GLY D N +8899 C CA . GLY D 229 ? 1.1965 1.8118 1.5131 0.2202 -0.0133 -0.1148 228 GLY D CA +8900 C C . GLY D 229 ? 1.2905 1.9041 1.6088 0.2202 -0.0120 -0.1147 228 GLY D C +8901 O O . GLY D 229 ? 1.3409 1.9546 1.6597 0.2196 -0.0116 -0.1148 228 GLY D O +8902 N N . ILE D 230 ? 1.0771 1.6892 1.3962 0.2208 -0.0112 -0.1146 229 ILE D N +8903 C CA . ILE D 230 ? 1.2284 1.8384 1.5492 0.2210 -0.0098 -0.1146 229 ILE D CA +8904 C C . ILE D 230 ? 2.2792 2.8859 2.6002 0.2219 -0.0088 -0.1152 229 ILE D C +8905 O O . ILE D 230 ? 2.7002 3.3063 3.0206 0.2226 -0.0091 -0.1153 229 ILE D O +8906 C CB . ILE D 230 ? 1.2894 1.8997 1.6112 0.2211 -0.0094 -0.1140 229 ILE D CB +8907 C CG1 . ILE D 230 ? 1.2707 1.8840 1.5927 0.2201 -0.0101 -0.1134 229 ILE D CG1 +8908 C CG2 . ILE D 230 ? 1.6379 2.2454 1.9615 0.2215 -0.0078 -0.1141 229 ILE D CG2 +8909 C CD1 . ILE D 230 ? 1.1192 1.7330 1.4422 0.2201 -0.0097 -0.1128 229 ILE D CD1 +8910 N N . THR D 231 ? 2.5246 3.1292 2.8465 0.2219 -0.0077 -0.1156 230 THR D N +8911 C CA . THR D 231 ? 2.7131 3.3145 3.0353 0.2228 -0.0068 -0.1161 230 THR D CA +8912 C C . THR D 231 ? 2.8243 3.4240 3.1471 0.2237 -0.0062 -0.1159 230 THR D C +8913 O O . THR D 231 ? 2.5338 3.1307 2.8577 0.2243 -0.0049 -0.1161 230 THR D O +8914 C CB . THR D 231 ? 2.4741 3.0734 2.7975 0.2227 -0.0054 -0.1164 230 THR D CB +8915 O OG1 . THR D 231 ? 2.3768 2.9732 2.7003 0.2235 -0.0046 -0.1169 230 THR D OG1 +8916 C CG2 . THR D 231 ? 2.3048 2.9032 2.6300 0.2228 -0.0042 -0.1160 230 THR D CG2 +8917 N N . ALA D 235 ? 1.9924 1.8196 1.6095 0.2559 0.0288 0.1166 1054 ALA D N +8918 C CA . ALA D 235 ? 2.3012 2.1253 1.9125 0.2546 0.0321 0.1205 1054 ALA D CA +8919 C C . ALA D 235 ? 2.4452 2.2683 2.0503 0.2508 0.0347 0.1178 1054 ALA D C +8920 O O . ALA D 235 ? 2.0076 1.8309 1.6102 0.2492 0.0361 0.1128 1054 ALA D O +8921 C CB . ALA D 235 ? 1.9027 1.7295 1.5211 0.2556 0.0270 0.1253 1054 ALA D CB +8922 N N . SER D 236 ? 2.6323 2.4542 2.2348 0.2492 0.0356 0.1211 1055 SER D N +8923 C CA . SER D 236 ? 2.7940 2.6155 2.3915 0.2456 0.0374 0.1190 1055 SER D CA +8924 C C . SER D 236 ? 2.9936 2.8206 2.5990 0.2443 0.0306 0.1179 1055 SER D C +8925 O O . SER D 236 ? 2.5695 2.3975 2.1728 0.2413 0.0305 0.1153 1055 SER D O +8926 C CB . SER D 236 ? 2.4470 2.2645 2.0375 0.2445 0.0419 0.1232 1055 SER D CB +8927 O OG . SER D 236 ? 2.0626 1.8791 1.6472 0.2410 0.0444 0.1208 1055 SER D OG +8928 N N . THR D 237 ? 3.1962 3.0267 2.8108 0.2467 0.0248 0.1200 1056 THR D N +8929 C CA . THR D 237 ? 2.8825 2.7187 2.5058 0.2460 0.0178 0.1189 1056 THR D CA +8930 C C . THR D 237 ? 2.4252 2.2637 2.0495 0.2446 0.0165 0.1127 1056 THR D C +8931 O O . THR D 237 ? 1.9262 1.7686 1.5548 0.2428 0.0123 0.1106 1056 THR D O +8932 C CB . THR D 237 ? 2.3486 2.1878 1.9815 0.2492 0.0122 0.1221 1056 THR D CB +8933 O OG1 . THR D 237 ? 2.1672 2.0072 1.8030 0.2515 0.0116 0.1196 1056 THR D OG1 +8934 C CG2 . THR D 237 ? 2.1006 1.9369 1.7317 0.2509 0.0142 0.1282 1056 THR D CG2 +8935 N N . LYS D 238 ? 2.7442 2.5804 2.3646 0.2454 0.0202 0.1098 1057 LYS D N +8936 C CA . LYS D 238 ? 2.5999 2.4376 2.2197 0.2440 0.0202 0.1037 1057 LYS D CA +8937 C C . LYS D 238 ? 2.2695 2.1067 1.8839 0.2402 0.0221 0.1014 1057 LYS D C +8938 O O . LYS D 238 ? 1.8305 1.6716 1.4493 0.2385 0.0180 0.0985 1057 LYS D O +8939 C CB . LYS D 238 ? 2.4456 2.2797 2.0598 0.2452 0.0254 0.1015 1057 LYS D CB +8940 C CG . LYS D 238 ? 2.3389 2.1750 1.9597 0.2484 0.0223 0.1008 1057 LYS D CG +8941 C CD . LYS D 238 ? 2.1339 1.9705 1.7600 0.2514 0.0197 0.1063 1057 LYS D CD +8942 C CE . LYS D 238 ? 1.8296 1.6674 1.4608 0.2547 0.0178 0.1056 1057 LYS D CE +8943 N NZ . LYS D 238 ? 1.8641 1.7027 1.5012 0.2576 0.0148 0.1108 1057 LYS D NZ +8944 N N . LYS D 239 ? 2.5041 2.3366 2.1094 0.2389 0.0283 0.1029 1058 LYS D N +8945 C CA . LYS D 239 ? 2.6790 2.5101 2.2777 0.2353 0.0313 0.1006 1058 LYS D CA +8946 C C . LYS D 239 ? 2.4898 2.3247 2.0930 0.2332 0.0266 0.1014 1058 LYS D C +8947 O O . LYS D 239 ? 2.2388 2.0743 1.8392 0.2302 0.0271 0.0983 1058 LYS D O +8948 C CB . LYS D 239 ? 2.8027 2.6280 2.3914 0.2346 0.0385 0.1032 1058 LYS D CB +8949 C CG . LYS D 239 ? 2.4789 2.3001 2.0625 0.2366 0.0437 0.1027 1058 LYS D CG +8950 C CD . LYS D 239 ? 2.4632 2.2788 2.0365 0.2355 0.0509 0.1048 1058 LYS D CD +8951 C CE . LYS D 239 ? 2.3914 2.2062 1.9587 0.2317 0.0533 0.1020 1058 LYS D CE +8952 N NZ . LYS D 239 ? 2.0103 1.8201 1.5683 0.2304 0.0596 0.1047 1058 LYS D NZ +8953 N N . LEU D 240 ? 2.3756 2.2127 1.9856 0.2349 0.0220 0.1057 1059 LEU D N +8954 C CA . LEU D 240 ? 2.4786 2.3191 2.0932 0.2333 0.0174 0.1072 1059 LEU D CA +8955 C C . LEU D 240 ? 2.3738 2.2199 1.9961 0.2325 0.0112 0.1033 1059 LEU D C +8956 O O . LEU D 240 ? 1.5586 1.4065 1.1807 0.2297 0.0098 0.1013 1059 LEU D O +8957 C CB . LEU D 240 ? 2.5932 2.4344 2.2129 0.2355 0.0145 0.1131 1059 LEU D CB +8958 C CG . LEU D 240 ? 2.3264 2.1718 1.9527 0.2345 0.0087 0.1149 1059 LEU D CG +8959 C CD1 . LEU D 240 ? 2.2169 2.0608 1.8370 0.2311 0.0113 0.1149 1059 LEU D CD1 +8960 C CD2 . LEU D 240 ? 2.0241 1.8700 1.6555 0.2371 0.0060 0.1207 1059 LEU D CD2 +8961 N N . SER D 241 ? 2.7303 2.5789 2.3595 0.2351 0.0076 0.1023 1060 SER D N +8962 C CA . SER D 241 ? 2.4500 2.3040 2.0874 0.2349 0.0014 0.0989 1060 SER D CA +8963 C C . SER D 241 ? 2.0519 1.9060 1.6855 0.2327 0.0033 0.0928 1060 SER D C +8964 O O . SER D 241 ? 1.9572 1.8155 1.5961 0.2317 -0.0012 0.0894 1060 SER D O +8965 C CB . SER D 241 ? 1.9017 1.7580 1.5470 0.2383 -0.0026 0.0998 1060 SER D CB +8966 O OG . SER D 241 ? 1.7536 1.6077 1.3957 0.2397 0.0008 0.0971 1060 SER D OG +8967 N N . GLU D 242 ? 1.9882 1.8376 1.6128 0.2322 0.0100 0.0913 1061 GLU D N +8968 C CA . GLU D 242 ? 2.3941 2.2431 2.0142 0.2299 0.0125 0.0857 1061 GLU D CA +8969 C C . GLU D 242 ? 2.2187 2.0690 1.8369 0.2264 0.0118 0.0845 1061 GLU D C +8970 O O . GLU D 242 ? 1.6799 1.5326 1.2991 0.2244 0.0102 0.0799 1061 GLU D O +8971 C CB . GLU D 242 ? 2.4984 2.3418 2.1086 0.2299 0.0201 0.0848 1061 GLU D CB +8972 C CG . GLU D 242 ? 2.5160 2.3573 2.1267 0.2334 0.0217 0.0868 1061 GLU D CG +8973 C CD . GLU D 242 ? 2.5893 2.4343 2.2082 0.2356 0.0170 0.0844 1061 GLU D CD +8974 O OE1 . GLU D 242 ? 2.6311 2.4794 2.2531 0.2343 0.0140 0.0799 1061 GLU D OE1 +8975 O OE2 . GLU D 242 ? 2.4238 2.2684 2.0459 0.2387 0.0162 0.0871 1061 GLU D OE2 +8976 N N . SER D 243 ? 2.4079 2.2566 2.0236 0.2256 0.0130 0.0888 1062 SER D N +8977 C CA . SER D 243 ? 2.6883 2.5379 2.3021 0.2224 0.0125 0.0884 1062 SER D CA +8978 C C . SER D 243 ? 2.4414 2.2968 2.0648 0.2222 0.0049 0.0886 1062 SER D C +8979 O O . SER D 243 ? 1.8326 1.6908 1.4572 0.2197 0.0027 0.0851 1062 SER D O +8980 C CB . SER D 243 ? 2.7505 2.5962 2.3580 0.2217 0.0167 0.0930 1062 SER D CB +8981 O OG . SER D 243 ? 2.6214 2.4617 2.2194 0.2216 0.0239 0.0924 1062 SER D OG +8982 N N . LEU D 244 ? 2.2762 2.1334 1.9065 0.2247 0.0009 0.0927 1063 LEU D N +8983 C CA . LEU D 244 ? 2.0361 1.8988 1.6763 0.2249 -0.0066 0.0932 1063 LEU D CA +8984 C C . LEU D 244 ? 2.1295 1.9960 1.7743 0.2246 -0.0100 0.0878 1063 LEU D C +8985 O O . LEU D 244 ? 1.7501 1.6206 1.3996 0.2230 -0.0146 0.0860 1063 LEU D O +8986 C CB . LEU D 244 ? 1.7458 1.6096 1.3926 0.2283 -0.0099 0.0979 1063 LEU D CB +8987 C CG . LEU D 244 ? 2.0328 1.8953 1.6788 0.2282 -0.0097 0.1036 1063 LEU D CG +8988 C CD1 . LEU D 244 ? 1.8960 1.7602 1.5496 0.2315 -0.0137 0.1079 1063 LEU D CD1 +8989 C CD2 . LEU D 244 ? 1.7248 1.5900 1.3721 0.2253 -0.0125 0.1032 1063 LEU D CD2 +8990 N N . LYS D 245 ? 2.3139 2.1789 1.9573 0.2261 -0.0078 0.0853 1064 LYS D N +8991 C CA . LYS D 245 ? 2.2326 2.1003 1.8786 0.2256 -0.0098 0.0796 1064 LYS D CA +8992 C C . LYS D 245 ? 2.3563 2.2245 1.9982 0.2219 -0.0087 0.0757 1064 LYS D C +8993 O O . LYS D 245 ? 2.3965 2.2691 2.0441 0.2207 -0.0138 0.0738 1064 LYS D O +8994 C CB . LYS D 245 ? 1.8901 1.7547 1.5321 0.2273 -0.0056 0.0775 1064 LYS D CB +8995 C CG . LYS D 245 ? 2.2165 2.0828 1.8657 0.2309 -0.0089 0.0787 1064 LYS D CG +8996 C CD . LYS D 245 ? 2.6479 2.5109 2.2924 0.2324 -0.0043 0.0766 1064 LYS D CD +8997 C CE . LYS D 245 ? 2.4608 2.3258 2.1126 0.2359 -0.0078 0.0772 1064 LYS D CE +8998 N NZ . LYS D 245 ? 1.8307 1.6929 1.4784 0.2372 -0.0036 0.0746 1064 LYS D NZ +8999 N N . ARG D 246 ? 2.2663 2.1301 1.8984 0.2201 -0.0021 0.0747 1065 ARG D N +9000 C CA . ARG D 246 ? 2.4018 2.2658 2.0294 0.2166 -0.0006 0.0705 1065 ARG D CA +9001 C C . ARG D 246 ? 2.2867 2.1535 1.9169 0.2144 -0.0041 0.0718 1065 ARG D C +9002 O O . ARG D 246 ? 2.1390 2.0087 1.7707 0.2122 -0.0064 0.0680 1065 ARG D O +9003 C CB . ARG D 246 ? 2.3259 2.1844 1.9423 0.2152 0.0073 0.0693 1065 ARG D CB +9004 C CG . ARG D 246 ? 2.5058 2.3618 2.1189 0.2167 0.0109 0.0665 1065 ARG D CG +9005 C CD . ARG D 246 ? 2.7533 2.6040 2.3551 0.2150 0.0187 0.0654 1065 ARG D CD +9006 N NE . ARG D 246 ? 2.9997 2.8477 2.5980 0.2164 0.0225 0.0629 1065 ARG D NE +9007 C CZ . ARG D 246 ? 2.7171 2.5602 2.3060 0.2156 0.0294 0.0620 1065 ARG D CZ +9008 N NH1 . ARG D 246 ? 2.5002 2.3404 2.0819 0.2133 0.0335 0.0633 1065 ARG D NH1 +9009 N NH2 . ARG D 246 ? 2.1530 1.9941 1.7395 0.2171 0.0324 0.0598 1065 ARG D NH2 +9010 N N . ILE D 247 ? 2.0097 1.8758 1.6407 0.2151 -0.0047 0.0771 1066 ILE D N +9011 C CA . ILE D 247 ? 2.0547 1.9232 1.6880 0.2131 -0.0078 0.0788 1066 ILE D CA +9012 C C . ILE D 247 ? 2.1518 2.0264 1.7954 0.2133 -0.0156 0.0774 1066 ILE D C +9013 O O . ILE D 247 ? 1.6976 1.5750 1.3426 0.2109 -0.0180 0.0755 1066 ILE D O +9014 C CB . ILE D 247 ? 2.1518 2.0180 1.7835 0.2139 -0.0065 0.0851 1066 ILE D CB +9015 C CG1 . ILE D 247 ? 2.5627 2.4230 2.1834 0.2128 0.0013 0.0860 1066 ILE D CG1 +9016 C CG2 . ILE D 247 ? 1.6351 1.5045 1.2711 0.2123 -0.0109 0.0872 1066 ILE D CG2 +9017 C CD1 . ILE D 247 ? 2.7721 2.6294 2.3906 0.2141 0.0035 0.0921 1066 ILE D CD1 +9018 N N . GLY D 248 ? 2.2725 2.1493 1.9234 0.2163 -0.0194 0.0784 1067 GLY D N +9019 C CA . GLY D 248 ? 1.9349 1.8174 1.5957 0.2168 -0.0266 0.0767 1067 GLY D CA +9020 C C . GLY D 248 ? 2.1203 2.0044 1.7812 0.2157 -0.0269 0.0705 1067 GLY D C +9021 O O . GLY D 248 ? 1.9920 1.8808 1.6594 0.2150 -0.0322 0.0680 1067 GLY D O +9022 N N . ASP D 249 ? 2.2945 2.1748 1.9481 0.2156 -0.0212 0.0681 1068 ASP D N +9023 C CA . ASP D 249 ? 2.1876 2.0689 1.8403 0.2146 -0.0207 0.0621 1068 ASP D CA +9024 C C . ASP D 249 ? 2.1822 2.0641 1.8308 0.2109 -0.0197 0.0586 1068 ASP D C +9025 O O . ASP D 249 ? 1.8600 1.7461 1.5137 0.2098 -0.0241 0.0552 1068 ASP D O +9026 C CB . ASP D 249 ? 2.2796 2.1564 1.9259 0.2159 -0.0149 0.0608 1068 ASP D CB +9027 C CG . ASP D 249 ? 2.5232 2.4010 2.1754 0.2195 -0.0173 0.0618 1068 ASP D CG +9028 O OD1 . ASP D 249 ? 2.6034 2.4846 2.2640 0.2212 -0.0228 0.0645 1068 ASP D OD1 +9029 O OD2 . ASP D 249 ? 2.3643 2.2394 2.0128 0.2207 -0.0135 0.0599 1068 ASP D OD2 +9030 N N . GLU D 250 ? 2.4610 2.3387 2.1006 0.2090 -0.0139 0.0595 1069 GLU D N +9031 C CA . GLU D 250 ? 2.5512 2.4290 2.1862 0.2053 -0.0125 0.0567 1069 GLU D CA +9032 C C . GLU D 250 ? 2.3413 2.2241 1.9836 0.2042 -0.0189 0.0574 1069 GLU D C +9033 O O . GLU D 250 ? 1.7090 1.5944 1.3520 0.2018 -0.0207 0.0536 1069 GLU D O +9034 C CB . GLU D 250 ? 2.3581 2.2309 1.9835 0.2039 -0.0061 0.0592 1069 GLU D CB +9035 C CG . GLU D 250 ? 2.6915 2.5591 2.3089 0.2047 0.0007 0.0586 1069 GLU D CG +9036 C CD . GLU D 250 ? 2.7120 2.5747 2.3213 0.2041 0.0063 0.0626 1069 GLU D CD +9037 O OE1 . GLU D 250 ? 2.4171 2.2805 2.0267 0.2027 0.0050 0.0653 1069 GLU D OE1 +9038 O OE2 . GLU D 250 ? 2.4856 2.3438 2.0885 0.2050 0.0119 0.0629 1069 GLU D OE2 +9039 N N . LEU D 251 ? 2.2121 2.0961 1.8597 0.2061 -0.0222 0.0623 1070 LEU D N +9040 C CA . LEU D 251 ? 2.0029 1.8916 1.6581 0.2055 -0.0285 0.0637 1070 LEU D CA +9041 C C . LEU D 251 ? 2.0691 1.9630 1.7326 0.2058 -0.0345 0.0598 1070 LEU D C +9042 O O . LEU D 251 ? 1.4530 1.3501 1.1184 0.2035 -0.0373 0.0571 1070 LEU D O +9043 C CB . LEU D 251 ? 2.0330 1.9217 1.6925 0.2080 -0.0306 0.0698 1070 LEU D CB +9044 C CG . LEU D 251 ? 2.1463 2.0390 1.8130 0.2077 -0.0366 0.0728 1070 LEU D CG +9045 C CD1 . LEU D 251 ? 1.9618 1.8557 1.6259 0.2042 -0.0368 0.0711 1070 LEU D CD1 +9046 C CD2 . LEU D 251 ? 1.6603 1.5510 1.3273 0.2096 -0.0360 0.0791 1070 LEU D CD2 +9047 N N . ASP D 252 ? 2.3111 2.2059 1.9793 0.2087 -0.0363 0.0595 1071 ASP D N +9048 C CA . ASP D 252 ? 2.0859 1.9857 1.7624 0.2092 -0.0421 0.0561 1071 ASP D CA +9049 C C . ASP D 252 ? 2.0579 1.9579 1.7309 0.2071 -0.0403 0.0499 1071 ASP D C +9050 O O . ASP D 252 ? 1.8552 1.7595 1.5338 0.2064 -0.0448 0.0464 1071 ASP D O +9051 C CB . ASP D 252 ? 1.5870 1.4879 1.2700 0.2129 -0.0449 0.0576 1071 ASP D CB +9052 C CG . ASP D 252 ? 2.7216 2.6277 2.4134 0.2135 -0.0510 0.0541 1071 ASP D CG +9053 O OD1 . ASP D 252 ? 2.6016 2.5119 2.2999 0.2128 -0.0566 0.0546 1071 ASP D OD1 +9054 O OD2 . ASP D 252 ? 3.2650 3.1710 2.9572 0.2147 -0.0504 0.0509 1071 ASP D OD2 +9055 N N . SER D 253 ? 2.0521 1.9473 1.7156 0.2061 -0.0335 0.0485 1072 SER D N +9056 C CA . SER D 253 ? 2.4229 2.3178 2.0823 0.2042 -0.0311 0.0426 1072 SER D CA +9057 C C . SER D 253 ? 2.6329 2.5274 2.2867 0.2004 -0.0290 0.0408 1072 SER D C +9058 O O . SER D 253 ? 2.4616 2.3564 2.1125 0.1985 -0.0277 0.0358 1072 SER D O +9059 C CB . SER D 253 ? 2.4522 2.3426 2.1049 0.2054 -0.0252 0.0414 1072 SER D CB +9060 O OG . SER D 253 ? 2.2824 2.1677 1.9259 0.2043 -0.0188 0.0437 1072 SER D OG +9061 N N . ASN D 254 ? 2.9307 2.8244 2.5827 0.1994 -0.0286 0.0447 1073 ASN D N +9062 C CA . ASN D 254 ? 2.8909 2.7842 2.5379 0.1959 -0.0269 0.0434 1073 ASN D CA +9063 C C . ASN D 254 ? 2.7926 2.6911 2.4454 0.1941 -0.0323 0.0397 1073 ASN D C +9064 O O . ASN D 254 ? 2.2626 2.1649 1.9223 0.1942 -0.0377 0.0418 1073 ASN D O +9065 C CB . ASN D 254 ? 2.7939 2.6859 2.4392 0.1954 -0.0262 0.0487 1073 ASN D CB +9066 C CG . ASN D 254 ? 2.5755 2.4627 2.2100 0.1931 -0.0194 0.0488 1073 ASN D CG +9067 O OD1 . ASN D 254 ? 2.4866 2.3703 2.1144 0.1928 -0.0141 0.0464 1073 ASN D OD1 +9068 N ND2 . ASN D 254 ? 2.3534 2.2405 1.9864 0.1913 -0.0195 0.0515 1073 ASN D ND2 +9069 N N . MET D 255 ? 3.0760 2.9747 2.7260 0.1924 -0.0307 0.0343 1074 MET D N +9070 C CA . MET D 255 ? 3.1042 3.0079 2.7598 0.1910 -0.0358 0.0302 1074 MET D CA +9071 C C . MET D 255 ? 2.9608 2.8667 2.6169 0.1883 -0.0379 0.0308 1074 MET D C +9072 O O . MET D 255 ? 2.5690 2.4796 2.2319 0.1876 -0.0436 0.0292 1074 MET D O +9073 C CB . MET D 255 ? 3.1289 3.0319 2.7806 0.1897 -0.0330 0.0242 1074 MET D CB +9074 C CG . MET D 255 ? 3.0149 2.9176 2.6691 0.1925 -0.0332 0.0227 1074 MET D CG +9075 S SD . MET D 255 ? 3.2689 3.1774 2.9363 0.1953 -0.0417 0.0237 1074 MET D SD +9076 C CE . MET D 255 ? 1.8291 1.7429 1.5011 0.1925 -0.0468 0.0191 1074 MET D CE +9077 N N . GLU D 256 ? 3.0763 2.9786 2.7250 0.1867 -0.0334 0.0332 1075 GLU D N +9078 C CA . GLU D 256 ? 2.9409 2.8448 2.5895 0.1842 -0.0350 0.0344 1075 GLU D CA +9079 C C . GLU D 256 ? 2.5910 2.4989 2.2490 0.1857 -0.0415 0.0381 1075 GLU D C +9080 O O . GLU D 256 ? 2.1550 2.0674 1.8189 0.1847 -0.0468 0.0367 1075 GLU D O +9081 C CB . GLU D 256 ? 2.9122 2.8113 2.5521 0.1830 -0.0292 0.0376 1075 GLU D CB +9082 C CG . GLU D 256 ? 2.8705 2.7647 2.5004 0.1820 -0.0219 0.0352 1075 GLU D CG +9083 C CD . GLU D 256 ? 2.8376 2.7271 2.4597 0.1812 -0.0166 0.0390 1075 GLU D CD +9084 O OE1 . GLU D 256 ? 2.8645 2.7537 2.4891 0.1829 -0.0178 0.0442 1075 GLU D OE1 +9085 O OE2 . GLU D 256 ? 2.7158 2.6021 2.3293 0.1790 -0.0111 0.0369 1075 GLU D OE2 +9086 N N . LEU D 257 ? 2.4570 2.3630 2.1159 0.1883 -0.0410 0.0429 1076 LEU D N +9087 C CA . LEU D 257 ? 2.3877 2.2966 2.0546 0.1901 -0.0463 0.0474 1076 LEU D CA +9088 C C . LEU D 257 ? 2.3153 2.2293 1.9925 0.1917 -0.0532 0.0456 1076 LEU D C +9089 O O . LEU D 257 ? 1.5824 1.5006 1.2663 0.1914 -0.0587 0.0466 1076 LEU D O +9090 C CB . LEU D 257 ? 2.2155 2.1206 1.8804 0.1926 -0.0435 0.0524 1076 LEU D CB +9091 C CG . LEU D 257 ? 2.1868 2.0940 1.8593 0.1951 -0.0482 0.0575 1076 LEU D CG +9092 C CD1 . LEU D 257 ? 1.8853 1.7955 1.5612 0.1934 -0.0521 0.0595 1076 LEU D CD1 +9093 C CD2 . LEU D 257 ? 2.3066 2.2092 1.9749 0.1971 -0.0439 0.0621 1076 LEU D CD2 +9094 N N . GLN D 258 ? 2.5019 2.4156 2.1801 0.1935 -0.0527 0.0431 1077 GLN D N +9095 C CA . GLN D 258 ? 2.3904 2.3088 2.0782 0.1953 -0.0588 0.0413 1077 GLN D CA +9096 C C . GLN D 258 ? 2.3925 2.3153 2.0840 0.1928 -0.0630 0.0374 1077 GLN D C +9097 O O . GLN D 258 ? 2.1613 2.0888 1.8616 0.1935 -0.0694 0.0380 1077 GLN D O +9098 C CB . GLN D 258 ? 2.1288 2.0457 1.8160 0.1972 -0.0569 0.0387 1077 GLN D CB +9099 C CG . GLN D 258 ? 2.3450 2.2574 2.0286 0.1998 -0.0527 0.0424 1077 GLN D CG +9100 C CD . GLN D 258 ? 2.2905 2.2045 1.9813 0.2026 -0.0568 0.0476 1077 GLN D CD +9101 O OE1 . GLN D 258 ? 2.2273 2.1459 1.9270 0.2036 -0.0631 0.0475 1077 GLN D OE1 +9102 N NE2 . GLN D 258 ? 1.6833 1.5933 1.3699 0.2038 -0.0532 0.0521 1077 GLN D NE2 +9103 N N . ARG D 259 ? 2.3805 2.3021 2.0655 0.1900 -0.0594 0.0334 1078 ARG D N +9104 C CA . ARG D 259 ? 2.4362 2.3615 2.1234 0.1874 -0.0626 0.0295 1078 ARG D CA +9105 C C . ARG D 259 ? 2.5059 2.4336 2.1962 0.1862 -0.0661 0.0328 1078 ARG D C +9106 O O . ARG D 259 ? 2.2954 2.2280 1.9934 0.1859 -0.0721 0.0319 1078 ARG D O +9107 C CB . ARG D 259 ? 2.6447 2.5673 2.3228 0.1845 -0.0572 0.0254 1078 ARG D CB +9108 C CG . ARG D 259 ? 2.6504 2.5768 2.3305 0.1817 -0.0601 0.0208 1078 ARG D CG +9109 C CD . ARG D 259 ? 2.8692 2.7930 2.5404 0.1783 -0.0553 0.0193 1078 ARG D CD +9110 N NE . ARG D 259 ? 2.9748 2.8936 2.6369 0.1780 -0.0484 0.0174 1078 ARG D NE +9111 C CZ . ARG D 259 ? 2.6715 2.5860 2.3247 0.1764 -0.0425 0.0188 1078 ARG D CZ +9112 N NH1 . ARG D 259 ? 2.3667 2.2812 2.0189 0.1750 -0.0429 0.0221 1078 ARG D NH1 +9113 N NH2 . ARG D 259 ? 2.2514 2.1616 1.8968 0.1761 -0.0364 0.0169 1078 ARG D NH2 +9114 N N . MET D 260 ? 2.5452 2.4693 2.2297 0.1856 -0.0623 0.0366 1079 MET D N +9115 C CA . MET D 260 ? 2.4935 2.4192 2.1796 0.1843 -0.0645 0.0400 1079 MET D CA +9116 C C . MET D 260 ? 2.5580 2.4878 2.2542 0.1864 -0.0713 0.0433 1079 MET D C +9117 O O . MET D 260 ? 2.5563 2.4897 2.2571 0.1851 -0.0757 0.0436 1079 MET D O +9118 C CB . MET D 260 ? 2.2711 2.1918 1.9492 0.1839 -0.0589 0.0440 1079 MET D CB +9119 C CG . MET D 260 ? 1.8570 1.7763 1.5281 0.1804 -0.0557 0.0430 1079 MET D CG +9120 S SD . MET D 260 ? 3.1497 3.0635 2.8125 0.1801 -0.0498 0.0484 1079 MET D SD +9121 C CE . MET D 260 ? 1.3827 1.2908 1.0374 0.1813 -0.0426 0.0471 1079 MET D CE +9122 N N . ILE D 261 ? 2.4175 2.3465 2.1172 0.1896 -0.0720 0.0458 1080 ILE D N +9123 C CA . ILE D 261 ? 2.4472 2.3797 2.1563 0.1918 -0.0781 0.0493 1080 ILE D CA +9124 C C . ILE D 261 ? 2.5165 2.4544 2.2344 0.1923 -0.0843 0.0459 1080 ILE D C +9125 O O . ILE D 261 ? 2.6152 2.5572 2.3405 0.1925 -0.0901 0.0473 1080 ILE D O +9126 C CB . ILE D 261 ? 2.2248 2.1549 1.9348 0.1951 -0.0769 0.0535 1080 ILE D CB +9127 C CG1 . ILE D 261 ? 2.0108 1.9350 1.7110 0.1947 -0.0698 0.0560 1080 ILE D CG1 +9128 C CG2 . ILE D 261 ? 2.2783 2.2114 1.9966 0.1969 -0.0826 0.0580 1080 ILE D CG2 +9129 C CD1 . ILE D 261 ? 1.9234 1.8452 1.6245 0.1978 -0.0689 0.0610 1080 ILE D CD1 +9130 N N . ALA D 262 ? 2.3445 2.2821 2.0615 0.1927 -0.0831 0.0415 1081 ALA D N +9131 C CA . ALA D 262 ? 2.3394 2.2818 2.0638 0.1929 -0.0885 0.0376 1081 ALA D CA +9132 C C . ALA D 262 ? 2.5750 2.5207 2.3008 0.1899 -0.0914 0.0356 1081 ALA D C +9133 O O . ALA D 262 ? 2.3397 2.2903 2.0739 0.1902 -0.0977 0.0354 1081 ALA D O +9134 C CB . ALA D 262 ? 1.7032 1.6442 1.4243 0.1930 -0.0855 0.0327 1081 ALA D CB +9135 N N . ALA D 263 ? 2.5850 2.5282 2.3026 0.1870 -0.0868 0.0341 1082 ALA D N +9136 C CA . ALA D 263 ? 2.5956 2.5414 2.3134 0.1841 -0.0888 0.0327 1082 ALA D CA +9137 C C . ALA D 263 ? 2.9490 2.8956 2.6692 0.1840 -0.0911 0.0379 1082 ALA D C +9138 O O . ALA D 263 ? 2.8210 2.7646 2.5345 0.1825 -0.0872 0.0400 1082 ALA D O +9139 C CB . ALA D 263 ? 2.4334 2.3760 2.1413 0.1811 -0.0829 0.0295 1082 ALA D CB +9140 N N . VAL D 264 ? 3.1333 3.0840 2.8630 0.1858 -0.0974 0.0400 1083 VAL D N +9141 C CA . VAL D 264 ? 3.1808 3.1332 2.9141 0.1856 -0.1006 0.0444 1083 VAL D CA +9142 C C . VAL D 264 ? 2.8477 2.8059 2.5921 0.1867 -0.1084 0.0444 1083 VAL D C +9143 O O . VAL D 264 ? 2.0917 2.0518 1.8417 0.1888 -0.1113 0.0429 1083 VAL D O +9144 C CB . VAL D 264 ? 2.7609 2.7096 2.4918 0.1876 -0.0978 0.0503 1083 VAL D CB +9145 C CG1 . VAL D 264 ? 2.4671 2.4170 2.2052 0.1912 -0.1012 0.0526 1083 VAL D CG1 +9146 C CG2 . VAL D 264 ? 2.5204 2.4695 2.2512 0.1863 -0.0989 0.0543 1083 VAL D CG2 +9147 N N . ASP D 265 ? 2.9490 2.9100 2.6964 0.1853 -0.1119 0.0460 1084 ASP D N +9148 C CA . ASP D 265 ? 3.0903 3.0569 2.8480 0.1860 -0.1194 0.0459 1084 ASP D CA +9149 C C . ASP D 265 ? 3.0356 3.0030 2.7995 0.1888 -0.1226 0.0513 1084 ASP D C +9150 O O . ASP D 265 ? 2.5588 2.5254 2.3220 0.1885 -0.1226 0.0556 1084 ASP D O +9151 C CB . ASP D 265 ? 3.0844 3.0539 2.8427 0.1830 -0.1217 0.0448 1084 ASP D CB +9152 C CG . ASP D 265 ? 2.8386 2.8140 2.6060 0.1830 -0.1286 0.0421 1084 ASP D CG +9153 O OD1 . ASP D 265 ? 2.7853 2.7632 2.5607 0.1856 -0.1331 0.0435 1084 ASP D OD1 +9154 O OD2 . ASP D 265 ? 2.4479 2.4254 2.2146 0.1803 -0.1296 0.0385 1084 ASP D OD2 +9155 N N . THR D 266 ? 3.2580 3.2269 3.0280 0.1916 -0.1254 0.0511 1085 THR D N +9156 C CA . THR D 266 ? 3.4611 3.4300 3.2361 0.1946 -0.1277 0.0561 1085 THR D CA +9157 C C . THR D 266 ? 3.4901 3.4644 3.2765 0.1963 -0.1352 0.0562 1085 THR D C +9158 O O . THR D 266 ? 3.5085 3.4832 3.3000 0.1992 -0.1373 0.0584 1085 THR D O +9159 C CB . THR D 266 ? 3.4701 3.4348 3.2414 0.1969 -0.1233 0.0568 1085 THR D CB +9160 O OG1 . THR D 266 ? 3.4317 3.3913 3.1927 0.1955 -0.1163 0.0573 1085 THR D OG1 +9161 C CG2 . THR D 266 ? 3.3990 3.3637 3.1756 0.2002 -0.1255 0.0619 1085 THR D CG2 +9162 N N . ASP D 267 ? 3.4187 3.3971 3.2090 0.1944 -0.1394 0.0537 1086 ASP D N +9163 C CA . ASP D 267 ? 3.2389 3.2227 3.0400 0.1957 -0.1468 0.0541 1086 ASP D CA +9164 C C . ASP D 267 ? 3.0876 3.0722 2.8919 0.1962 -0.1493 0.0597 1086 ASP D C +9165 O O . ASP D 267 ? 2.5969 2.5841 2.4092 0.1985 -0.1540 0.0623 1086 ASP D O +9166 C CB . ASP D 267 ? 3.1269 3.1147 2.9306 0.1934 -0.1501 0.0493 1086 ASP D CB +9167 C CG . ASP D 267 ? 3.1743 3.1608 2.9729 0.1921 -0.1466 0.0437 1086 ASP D CG +9168 O OD1 . ASP D 267 ? 3.1764 3.1596 2.9713 0.1936 -0.1427 0.0433 1086 ASP D OD1 +9169 O OD2 . ASP D 267 ? 3.1466 3.1355 2.9450 0.1896 -0.1478 0.0398 1086 ASP D OD2 +9170 N N . SER D 268 ? 3.2214 3.2037 3.0193 0.1940 -0.1460 0.0613 1087 SER D N +9171 C CA . SER D 268 ? 3.0572 3.0390 2.8560 0.1944 -0.1468 0.0668 1087 SER D CA +9172 C C . SER D 268 ? 3.2717 3.2476 3.0618 0.1948 -0.1400 0.0697 1087 SER D C +9173 O O . SER D 268 ? 3.0069 2.9802 2.7897 0.1925 -0.1359 0.0701 1087 SER D O +9174 C CB . SER D 268 ? 2.4138 2.3978 2.2121 0.1914 -0.1484 0.0664 1087 SER D CB +9175 O OG . SER D 268 ? 2.0470 2.0310 1.8468 0.1917 -0.1497 0.0717 1087 SER D OG +9176 N N . PRO D 269 ? 3.3208 3.2948 3.1119 0.1977 -0.1389 0.0717 1088 PRO D N +9177 C CA . PRO D 269 ? 2.8677 2.8360 2.6506 0.1984 -0.1323 0.0736 1088 PRO D CA +9178 C C . PRO D 269 ? 2.8080 2.7736 2.5879 0.1985 -0.1303 0.0793 1088 PRO D C +9179 O O . PRO D 269 ? 2.6456 2.6068 2.4167 0.1974 -0.1243 0.0800 1088 PRO D O +9180 C CB . PRO D 269 ? 2.3666 2.3347 2.1536 0.2017 -0.1332 0.0739 1088 PRO D CB +9181 C CG . PRO D 269 ? 2.6394 2.6126 2.4373 0.2033 -0.1406 0.0752 1088 PRO D CG +9182 C CD . PRO D 269 ? 3.1235 3.1006 2.9240 0.2006 -0.1442 0.0724 1088 PRO D CD +9183 N N . ARG D 270 ? 2.8476 2.8160 2.6348 0.1998 -0.1352 0.0831 1089 ARG D N +9184 C CA . ARG D 270 ? 2.6556 2.6220 2.4413 0.2003 -0.1341 0.0889 1089 ARG D CA +9185 C C . ARG D 270 ? 2.6911 2.6548 2.4686 0.1974 -0.1298 0.0895 1089 ARG D C +9186 O O . ARG D 270 ? 1.6037 1.5632 1.3750 0.1976 -0.1251 0.0928 1089 ARG D O +9187 C CB . ARG D 270 ? 2.2695 2.2403 2.0651 0.2017 -0.1409 0.0920 1089 ARG D CB +9188 C CG . ARG D 270 ? 2.5123 2.4825 2.3069 0.2009 -0.1410 0.0968 1089 ARG D CG +9189 C CD . ARG D 270 ? 2.4334 2.4077 2.2378 0.2025 -0.1477 0.1001 1089 ARG D CD +9190 N NE . ARG D 270 ? 2.5434 2.5176 2.3469 0.2012 -0.1480 0.1040 1089 ARG D NE +9191 C CZ . ARG D 270 ? 2.5415 2.5122 2.3413 0.2021 -0.1450 0.1088 1089 ARG D CZ +9192 N NH1 . ARG D 270 ? 2.5943 2.5613 2.3910 0.2042 -0.1413 0.1104 1089 ARG D NH1 +9193 N NH2 . ARG D 270 ? 2.2080 2.1789 2.0071 0.2008 -0.1456 0.1121 1089 ARG D NH2 +9194 N N . GLU D 271 ? 3.0587 3.0250 2.8361 0.1946 -0.1314 0.0863 1090 GLU D N +9195 C CA . GLU D 271 ? 2.9628 2.9269 2.7325 0.1916 -0.1276 0.0865 1090 GLU D CA +9196 C C . GLU D 271 ? 2.8436 2.8028 2.6032 0.1906 -0.1204 0.0841 1090 GLU D C +9197 O O . GLU D 271 ? 2.4293 2.3845 2.1815 0.1896 -0.1155 0.0865 1090 GLU D O +9198 C CB . GLU D 271 ? 2.9589 2.9270 2.7310 0.1889 -0.1310 0.0830 1090 GLU D CB +9199 C CG . GLU D 271 ? 3.0540 3.0277 2.8368 0.1899 -0.1387 0.0837 1090 GLU D CG +9200 C CD . GLU D 271 ? 3.1141 3.0918 2.8991 0.1873 -0.1418 0.0793 1090 GLU D CD +9201 O OE1 . GLU D 271 ? 3.0163 2.9923 2.7942 0.1846 -0.1381 0.0766 1090 GLU D OE1 +9202 O OE2 . GLU D 271 ? 3.0941 3.0766 2.8879 0.1881 -0.1480 0.0786 1090 GLU D OE2 +9203 N N . VAL D 272 ? 3.0230 2.9825 2.7826 0.1909 -0.1198 0.0795 1091 VAL D N +9204 C CA . VAL D 272 ? 2.9154 2.8707 2.6658 0.1898 -0.1133 0.0765 1091 VAL D CA +9205 C C . VAL D 272 ? 2.9271 2.8771 2.6716 0.1914 -0.1080 0.0802 1091 VAL D C +9206 O O . VAL D 272 ? 2.8178 2.7638 2.5533 0.1898 -0.1021 0.0801 1091 VAL D O +9207 C CB . VAL D 272 ? 2.3820 2.3387 2.1345 0.1904 -0.1142 0.0714 1091 VAL D CB +9208 C CG1 . VAL D 272 ? 2.2693 2.2220 2.0122 0.1888 -0.1076 0.0678 1091 VAL D CG1 +9209 C CG2 . VAL D 272 ? 2.1533 2.1156 1.9127 0.1892 -0.1201 0.0680 1091 VAL D CG2 +9210 N N . PHE D 273 ? 2.9553 2.9055 2.7049 0.1945 -0.1100 0.0835 1092 PHE D N +9211 C CA . PHE D 273 ? 2.8655 2.8110 2.6104 0.1963 -0.1054 0.0874 1092 PHE D CA +9212 C C . PHE D 273 ? 2.6576 2.6009 2.3984 0.1952 -0.1033 0.0918 1092 PHE D C +9213 O O . PHE D 273 ? 2.6157 2.5543 2.3477 0.1943 -0.0972 0.0927 1092 PHE D O +9214 C CB . PHE D 273 ? 3.0239 2.9706 2.7762 0.2000 -0.1088 0.0901 1092 PHE D CB +9215 C CG . PHE D 273 ? 3.0607 3.0030 2.8092 0.2019 -0.1049 0.0947 1092 PHE D CG +9216 C CD1 . PHE D 273 ? 2.9519 2.8897 2.6933 0.2025 -0.0990 0.0936 1092 PHE D CD1 +9217 C CD2 . PHE D 273 ? 3.0440 2.9866 2.7960 0.2033 -0.1070 0.1002 1092 PHE D CD2 +9218 C CE1 . PHE D 273 ? 2.7350 2.6688 2.4729 0.2043 -0.0953 0.0979 1092 PHE D CE1 +9219 C CE2 . PHE D 273 ? 2.9093 2.8479 2.6578 0.2051 -0.1034 0.1045 1092 PHE D CE2 +9220 C CZ . PHE D 273 ? 2.7133 2.6474 2.4548 0.2056 -0.0976 0.1033 1092 PHE D CZ +9221 N N . PHE D 274 ? 2.4498 2.3965 2.1969 0.1952 -0.1083 0.0946 1093 PHE D N +9222 C CA . PHE D 274 ? 2.6728 2.6178 2.4171 0.1944 -0.1071 0.0993 1093 PHE D CA +9223 C C . PHE D 274 ? 2.8235 2.7659 2.5587 0.1911 -0.1022 0.0978 1093 PHE D C +9224 O O . PHE D 274 ? 2.7546 2.6931 2.4835 0.1907 -0.0978 0.1010 1093 PHE D O +9225 C CB . PHE D 274 ? 2.9520 2.9018 2.7051 0.1947 -0.1138 0.1017 1093 PHE D CB +9226 C CG . PHE D 274 ? 3.1128 3.0613 2.8636 0.1937 -0.1130 0.1063 1093 PHE D CG +9227 C CD1 . PHE D 274 ? 2.7363 2.6823 2.4869 0.1959 -0.1117 0.1117 1093 PHE D CD1 +9228 C CD2 . PHE D 274 ? 3.0234 2.9732 2.7721 0.1907 -0.1134 0.1053 1093 PHE D CD2 +9229 C CE1 . PHE D 274 ? 2.6301 2.5749 2.3785 0.1950 -0.1109 0.1159 1093 PHE D CE1 +9230 C CE2 . PHE D 274 ? 2.4525 2.4012 2.1991 0.1898 -0.1126 0.1095 1093 PHE D CE2 +9231 C CZ . PHE D 274 ? 2.3779 2.3241 2.1244 0.1920 -0.1114 0.1148 1093 PHE D CZ +9232 N N . ARG D 275 ? 2.8534 2.7982 2.5882 0.1886 -0.1031 0.0929 1094 ARG D N +9233 C CA . ARG D 275 ? 2.7231 2.6657 2.4496 0.1853 -0.0989 0.0912 1094 ARG D CA +9234 C C . ARG D 275 ? 2.5661 2.5034 2.2830 0.1851 -0.0916 0.0898 1094 ARG D C +9235 O O . ARG D 275 ? 2.5334 2.4670 2.2425 0.1835 -0.0867 0.0913 1094 ARG D O +9236 C CB . ARG D 275 ? 2.7935 2.7400 2.5221 0.1829 -0.1019 0.0862 1094 ARG D CB +9237 C CG . ARG D 275 ? 2.8135 2.7602 2.5380 0.1796 -0.1009 0.0862 1094 ARG D CG +9238 C CD . ARG D 275 ? 2.7703 2.7202 2.4956 0.1771 -0.1028 0.0807 1094 ARG D CD +9239 N NE . ARG D 275 ? 2.7853 2.7394 2.5190 0.1786 -0.1082 0.0779 1094 ARG D NE +9240 C CZ . ARG D 275 ? 2.5355 2.4946 2.2782 0.1790 -0.1148 0.0785 1094 ARG D CZ +9241 N NH1 . ARG D 275 ? 2.1432 2.1038 1.8877 0.1781 -0.1170 0.0818 1094 ARG D NH1 +9242 N NH2 . ARG D 275 ? 2.1301 2.0928 1.8800 0.1804 -0.1192 0.0759 1094 ARG D NH2 +9243 N N . VAL D 276 ? 2.3792 2.3161 2.0969 0.1866 -0.0909 0.0869 1095 VAL D N +9244 C CA . VAL D 276 ? 2.3101 2.2419 2.0192 0.1867 -0.0842 0.0856 1095 VAL D CA +9245 C C . VAL D 276 ? 2.2482 2.1759 1.9541 0.1885 -0.0808 0.0909 1095 VAL D C +9246 O O . VAL D 276 ? 2.0688 1.9918 1.7658 0.1877 -0.0745 0.0914 1095 VAL D O +9247 C CB . VAL D 276 ? 2.3677 2.3004 2.0794 0.1882 -0.0848 0.0817 1095 VAL D CB +9248 C CG1 . VAL D 276 ? 1.9771 1.9044 1.6808 0.1890 -0.0781 0.0813 1095 VAL D CG1 +9249 C CG2 . VAL D 276 ? 2.7728 2.7086 2.4856 0.1860 -0.0868 0.0759 1095 VAL D CG2 +9250 N N . ALA D 277 ? 2.4065 2.3361 2.1197 0.1910 -0.0850 0.0949 1096 ALA D N +9251 C CA . ALA D 277 ? 2.1504 2.0767 1.8617 0.1929 -0.0826 0.1005 1096 ALA D CA +9252 C C . ALA D 277 ? 2.0813 2.0054 1.7868 0.1908 -0.0799 0.1033 1096 ALA D C +9253 O O . ALA D 277 ? 1.8080 1.7274 1.5059 0.1906 -0.0741 0.1053 1096 ALA D O +9254 C CB . ALA D 277 ? 1.7662 1.6956 1.4872 0.1958 -0.0885 0.1040 1096 ALA D CB +9255 N N . ALA D 278 ? 2.2066 2.1344 1.9160 0.1891 -0.0840 0.1034 1097 ALA D N +9256 C CA . ALA D 278 ? 2.0695 1.9960 1.7744 0.1869 -0.0822 0.1059 1097 ALA D CA +9257 C C . ALA D 278 ? 2.0249 1.9483 1.7200 0.1839 -0.0765 0.1026 1097 ALA D C +9258 O O . ALA D 278 ? 1.9338 1.8543 1.6226 0.1824 -0.0728 0.1050 1097 ALA D O +9259 C CB . ALA D 278 ? 1.7398 1.6713 1.4519 0.1860 -0.0885 0.1067 1097 ALA D CB +9260 N N . ASP D 279 ? 1.9549 1.8791 1.6488 0.1829 -0.0757 0.0972 1098 ASP D N +9261 C CA . ASP D 279 ? 2.0772 1.9984 1.7618 0.1802 -0.0701 0.0939 1098 ASP D CA +9262 C C . ASP D 279 ? 2.3895 2.3049 2.0660 0.1811 -0.0633 0.0951 1098 ASP D C +9263 O O . ASP D 279 ? 1.9643 1.8759 1.6322 0.1792 -0.0579 0.0953 1098 ASP D O +9264 C CB . ASP D 279 ? 1.9803 1.9041 1.6661 0.1788 -0.0715 0.0876 1098 ASP D CB +9265 C CG . ASP D 279 ? 2.2527 2.1753 1.9310 0.1752 -0.0679 0.0843 1098 ASP D CG +9266 O OD1 . ASP D 279 ? 2.1375 2.0558 1.8076 0.1745 -0.0618 0.0825 1098 ASP D OD1 +9267 O OD2 . ASP D 279 ? 2.3575 2.2832 2.0382 0.1732 -0.0710 0.0834 1098 ASP D OD2 +9268 N N . MET D 280 ? 2.4842 2.3988 2.1636 0.1841 -0.0636 0.0960 1099 MET D N +9269 C CA . MET D 280 ? 2.2871 2.1964 1.9597 0.1854 -0.0576 0.0976 1099 MET D CA +9270 C C . MET D 280 ? 2.0198 1.9260 1.6886 0.1855 -0.0549 0.1031 1099 MET D C +9271 O O . MET D 280 ? 1.9334 1.8347 1.5939 0.1852 -0.0488 0.1041 1099 MET D O +9272 C CB . MET D 280 ? 2.5044 2.4141 2.1822 0.1889 -0.0593 0.0981 1099 MET D CB +9273 C CG . MET D 280 ? 2.6849 2.5954 2.3630 0.1890 -0.0590 0.0927 1099 MET D CG +9274 S SD . MET D 280 ? 2.5647 2.4744 2.2469 0.1931 -0.0595 0.0938 1099 MET D SD +9275 C CE . MET D 280 ? 1.5692 1.4725 1.2430 0.1941 -0.0528 0.0987 1099 MET D CE +9276 N N . PHE D 281 ? 1.9100 1.8191 1.5848 0.1859 -0.0596 0.1066 1100 PHE D N +9277 C CA . PHE D 281 ? 2.0888 1.9954 1.7614 0.1864 -0.0579 0.1123 1100 PHE D CA +9278 C C . PHE D 281 ? 2.3112 2.2186 1.9819 0.1837 -0.0584 0.1135 1100 PHE D C +9279 O O . PHE D 281 ? 2.1430 2.0508 1.8159 0.1842 -0.0601 0.1182 1100 PHE D O +9280 C CB . PHE D 281 ? 1.8365 1.7450 1.5173 0.1896 -0.0624 0.1165 1100 PHE D CB +9281 C CG . PHE D 281 ? 2.2279 2.1346 1.9095 0.1925 -0.0610 0.1164 1100 PHE D CG +9282 C CD1 . PHE D 281 ? 2.2266 2.1280 1.8996 0.1927 -0.0543 0.1163 1100 PHE D CD1 +9283 C CD2 . PHE D 281 ? 1.8455 1.7557 1.5361 0.1950 -0.0664 0.1164 1100 PHE D CD2 +9284 C CE1 . PHE D 281 ? 2.0749 1.9747 1.7485 0.1954 -0.0530 0.1162 1100 PHE D CE1 +9285 C CE2 . PHE D 281 ? 1.7345 1.6431 1.4258 0.1977 -0.0651 0.1163 1100 PHE D CE2 +9286 C CZ . PHE D 281 ? 1.9956 1.8989 1.6783 0.1979 -0.0584 0.1162 1100 PHE D CZ +9287 N N . SER D 282 ? 2.6389 2.5468 2.3055 0.1807 -0.0569 0.1091 1101 SER D N +9288 C CA . SER D 282 ? 2.8219 2.7304 2.4857 0.1778 -0.0567 0.1096 1101 SER D CA +9289 C C . SER D 282 ? 2.8073 2.7103 2.4610 0.1767 -0.0498 0.1118 1101 SER D C +9290 O O . SER D 282 ? 2.2027 2.1052 1.8539 0.1751 -0.0492 0.1144 1101 SER D O +9291 C CB . SER D 282 ? 2.8449 2.7561 2.5085 0.1752 -0.0579 0.1039 1101 SER D CB +9292 O OG . SER D 282 ? 2.7744 2.6824 2.4305 0.1742 -0.0525 0.1000 1101 SER D OG +9293 N N . ASP D 283 ? 2.8834 2.7822 2.5311 0.1775 -0.0445 0.1108 1102 ASP D N +9294 C CA . ASP D 283 ? 2.4497 2.3430 2.0881 0.1769 -0.0378 0.1132 1102 ASP D CA +9295 C C . ASP D 283 ? 2.0445 1.9359 1.6846 0.1797 -0.0377 0.1190 1102 ASP D C +9296 O O . ASP D 283 ? 1.5090 1.3961 1.1425 0.1795 -0.0329 0.1222 1102 ASP D O +9297 C CB . ASP D 283 ? 2.3704 2.2600 2.0009 0.1762 -0.0319 0.1092 1102 ASP D CB +9298 C CG . ASP D 283 ? 2.4348 2.3244 2.0684 0.1789 -0.0323 0.1077 1102 ASP D CG +9299 O OD1 . ASP D 283 ? 2.6248 2.5184 2.2674 0.1807 -0.0381 0.1078 1102 ASP D OD1 +9300 O OD2 . ASP D 283 ? 1.9829 1.8683 1.6098 0.1792 -0.0268 0.1064 1102 ASP D OD2 +9301 N N . GLY D 284 ? 1.9387 1.8333 1.5878 0.1824 -0.0430 0.1203 1103 GLY D N +9302 C CA . GLY D 284 ? 2.0266 1.9203 1.6790 0.1851 -0.0442 0.1260 1103 GLY D CA +9303 C C . GLY D 284 ? 2.4006 2.2889 2.0467 0.1867 -0.0383 0.1282 1103 GLY D C +9304 O O . GLY D 284 ? 1.5560 1.4421 1.2011 0.1879 -0.0371 0.1332 1103 GLY D O +9305 N N . ASN D 285 ? 2.9276 2.8138 2.5693 0.1867 -0.0347 0.1243 1104 ASN D N +9306 C CA . ASN D 285 ? 2.6690 2.5502 2.3047 0.1883 -0.0290 0.1256 1104 ASN D CA +9307 C C . ASN D 285 ? 2.1224 2.0047 1.7637 0.1914 -0.0312 0.1250 1104 ASN D C +9308 O O . ASN D 285 ? 1.9081 1.7897 1.5473 0.1915 -0.0292 0.1208 1104 ASN D O +9309 C CB . ASN D 285 ? 2.4204 2.2979 2.0462 0.1860 -0.0226 0.1219 1104 ASN D CB +9310 C CG . ASN D 285 ? 2.4359 2.3119 2.0554 0.1829 -0.0198 0.1226 1104 ASN D CG +9311 O OD1 . ASN D 285 ? 2.3222 2.1988 1.9433 0.1827 -0.0214 0.1267 1104 ASN D OD1 +9312 N ND2 . ASN D 285 ? 1.9630 1.8372 1.5754 0.1804 -0.0156 0.1185 1104 ASN D ND2 +9313 N N . PHE D 286 ? 2.0065 1.8905 1.6548 0.1940 -0.0353 0.1291 1105 PHE D N +9314 C CA . PHE D 286 ? 2.1781 2.0634 1.8327 0.1972 -0.0380 0.1291 1105 PHE D CA +9315 C C . PHE D 286 ? 2.6584 2.5389 2.3073 0.1990 -0.0324 0.1300 1105 PHE D C +9316 O O . PHE D 286 ? 2.7819 2.6584 2.4251 0.1992 -0.0282 0.1337 1105 PHE D O +9317 C CB . PHE D 286 ? 2.0188 1.9069 1.6819 0.1994 -0.0435 0.1339 1105 PHE D CB +9318 C CG . PHE D 286 ? 2.5896 2.4830 2.2600 0.1982 -0.0499 0.1334 1105 PHE D CG +9319 C CD1 . PHE D 286 ? 2.9988 2.8968 2.6769 0.1988 -0.0552 0.1301 1105 PHE D CD1 +9320 C CD2 . PHE D 286 ? 2.1571 2.0510 1.8269 0.1966 -0.0507 0.1364 1105 PHE D CD2 +9321 C CE1 . PHE D 286 ? 2.9792 2.8821 2.6641 0.1978 -0.0611 0.1297 1105 PHE D CE1 +9322 C CE2 . PHE D 286 ? 1.7600 1.6587 1.4365 0.1956 -0.0565 0.1360 1105 PHE D CE2 +9323 C CZ . PHE D 286 ? 2.3654 2.2687 2.0496 0.1962 -0.0618 0.1326 1105 PHE D CZ +9324 N N . ASN D 287 ? 2.7789 2.6598 2.4294 0.2004 -0.0326 0.1267 1106 ASN D N +9325 C CA . ASN D 287 ? 2.4402 2.3173 2.0874 0.2027 -0.0286 0.1276 1106 ASN D CA +9326 C C . ASN D 287 ? 2.3504 2.2304 2.0050 0.2051 -0.0325 0.1255 1106 ASN D C +9327 O O . ASN D 287 ? 2.0493 1.9334 1.7088 0.2043 -0.0366 0.1216 1106 ASN D O +9328 C CB . ASN D 287 ? 2.2921 2.1646 1.9288 0.2010 -0.0213 0.1249 1106 ASN D CB +9329 C CG . ASN D 287 ? 2.2061 2.0803 1.8409 0.1981 -0.0214 0.1192 1106 ASN D CG +9330 O OD1 . ASN D 287 ? 2.0520 1.9293 1.6915 0.1985 -0.0245 0.1153 1106 ASN D OD1 +9331 N ND2 . ASN D 287 ? 1.9102 1.7825 1.5380 0.1952 -0.0178 0.1186 1106 ASN D ND2 +9332 N N . TRP D 288 ? 2.3192 2.1974 1.9748 0.2081 -0.0315 0.1280 1107 TRP D N +9333 C CA . TRP D 288 ? 1.7860 1.6668 1.4488 0.2107 -0.0353 0.1265 1107 TRP D CA +9334 C C . TRP D 288 ? 1.8369 1.7190 1.4993 0.2098 -0.0351 0.1203 1107 TRP D C +9335 O O . TRP D 288 ? 1.7810 1.6668 1.4509 0.2111 -0.0399 0.1182 1107 TRP D O +9336 C CB . TRP D 288 ? 1.8341 1.7116 1.4957 0.2138 -0.0326 0.1297 1107 TRP D CB +9337 C CG . TRP D 288 ? 2.3488 2.2287 2.0188 0.2165 -0.0375 0.1339 1107 TRP D CG +9338 C CD1 . TRP D 288 ? 2.7400 2.6180 2.4097 0.2177 -0.0369 0.1395 1107 TRP D CD1 +9339 C CD2 . TRP D 288 ? 2.5710 2.4557 2.2511 0.2182 -0.0441 0.1329 1107 TRP D CD2 +9340 N NE1 . TRP D 288 ? 3.0404 2.9218 2.7194 0.2202 -0.0426 0.1421 1107 TRP D NE1 +9341 C CE2 . TRP D 288 ? 2.9467 2.8322 2.6322 0.2206 -0.0471 0.1381 1107 TRP D CE2 +9342 C CE3 . TRP D 288 ? 2.3768 2.2652 2.0618 0.2181 -0.0476 0.1281 1107 TRP D CE3 +9343 C CZ2 . TRP D 288 ? 2.6613 2.5512 2.3569 0.2227 -0.0535 0.1387 1107 TRP D CZ2 +9344 C CZ3 . TRP D 288 ? 2.1260 2.0187 1.8210 0.2202 -0.0540 0.1287 1107 TRP D CZ3 +9345 C CH2 . TRP D 288 ? 2.0178 1.9112 1.7181 0.2225 -0.0569 0.1339 1107 TRP D CH2 +9346 N N . GLY D 289 ? 1.7876 1.6665 1.4412 0.2076 -0.0297 0.1173 1108 GLY D N +9347 C CA . GLY D 289 ? 1.9841 1.8640 1.6366 0.2064 -0.0291 0.1114 1108 GLY D CA +9348 C C . GLY D 289 ? 2.2411 2.1264 1.9003 0.2049 -0.0351 0.1083 1108 GLY D C +9349 O O . GLY D 289 ? 1.9840 1.8721 1.6478 0.2055 -0.0380 0.1046 1108 GLY D O +9350 N N . ARG D 290 ? 2.2539 2.1408 1.9139 0.2030 -0.0370 0.1101 1109 ARG D N +9351 C CA . ARG D 290 ? 1.8905 1.7827 1.5568 0.2014 -0.0427 0.1076 1109 ARG D CA +9352 C C . ARG D 290 ? 1.9638 1.8604 1.6410 0.2038 -0.0497 0.1094 1109 ARG D C +9353 O O . ARG D 290 ? 1.8571 1.7581 1.5407 0.2036 -0.0546 0.1062 1109 ARG D O +9354 C CB . ARG D 290 ? 1.4924 1.3846 1.1556 0.1986 -0.0423 0.1089 1109 ARG D CB +9355 C CG . ARG D 290 ? 1.8717 1.7607 1.5252 0.1956 -0.0366 0.1059 1109 ARG D CG +9356 C CD . ARG D 290 ? 2.1686 2.0587 1.8207 0.1928 -0.0374 0.1068 1109 ARG D CD +9357 N NE . ARG D 290 ? 2.2474 2.1344 1.8900 0.1899 -0.0318 0.1043 1109 ARG D NE +9358 C CZ . ARG D 290 ? 2.4487 2.3355 2.0879 0.1872 -0.0309 0.1050 1109 ARG D CZ +9359 N NH1 . ARG D 290 ? 2.6011 2.4908 2.2457 0.1872 -0.0354 0.1082 1109 ARG D NH1 +9360 N NH2 . ARG D 290 ? 2.2793 2.1632 1.9098 0.1846 -0.0256 0.1025 1109 ARG D NH2 +9361 N N . VAL D 291 ? 1.9326 1.8281 1.6120 0.2061 -0.0503 0.1147 1110 VAL D N +9362 C CA . VAL D 291 ? 1.6540 1.5532 1.3435 0.2088 -0.0564 0.1170 1110 VAL D CA +9363 C C . VAL D 291 ? 1.7553 1.6560 1.4488 0.2106 -0.0581 0.1135 1110 VAL D C +9364 O O . VAL D 291 ? 1.8126 1.7180 1.5148 0.2116 -0.0641 0.1123 1110 VAL D O +9365 C CB . VAL D 291 ? 1.9545 1.8512 1.6440 0.2111 -0.0553 0.1230 1110 VAL D CB +9366 C CG1 . VAL D 291 ? 1.9628 1.8634 1.6629 0.2139 -0.0617 0.1254 1110 VAL D CG1 +9367 C CG2 . VAL D 291 ? 1.6038 1.4987 1.2889 0.2093 -0.0533 0.1265 1110 VAL D CG2 +9368 N N . VAL D 292 ? 1.7817 1.6786 1.4687 0.2111 -0.0527 0.1117 1111 VAL D N +9369 C CA . VAL D 292 ? 1.7961 1.6938 1.4859 0.2128 -0.0535 0.1083 1111 VAL D CA +9370 C C . VAL D 292 ? 1.7871 1.6872 1.4768 0.2106 -0.0545 0.1022 1111 VAL D C +9371 O O . VAL D 292 ? 1.9053 1.8091 1.6019 0.2117 -0.0589 0.0996 1111 VAL D O +9372 C CB . VAL D 292 ? 1.6363 1.5288 1.3191 0.2143 -0.0472 0.1089 1111 VAL D CB +9373 C CG1 . VAL D 292 ? 1.1439 1.0372 0.8289 0.2158 -0.0476 0.1050 1111 VAL D CG1 +9374 C CG2 . VAL D 292 ? 1.8696 1.7603 1.5537 0.2168 -0.0469 0.1148 1111 VAL D CG2 +9375 N N . ALA D 293 ? 1.6896 1.5878 1.3718 0.2076 -0.0505 0.1000 1112 ALA D N +9376 C CA . ALA D 293 ? 1.7592 1.6595 1.4409 0.2053 -0.0512 0.0942 1112 ALA D CA +9377 C C . ALA D 293 ? 2.0288 1.9349 1.7190 0.2045 -0.0582 0.0932 1112 ALA D C +9378 O O . ALA D 293 ? 1.8675 1.7766 1.5607 0.2036 -0.0609 0.0887 1112 ALA D O +9379 C CB . ALA D 293 ? 1.6587 1.5556 1.3303 0.2022 -0.0453 0.0923 1112 ALA D CB +9380 N N . LEU D 294 ? 2.1079 2.0154 1.8019 0.2047 -0.0613 0.0976 1113 LEU D N +9381 C CA . LEU D 294 ? 2.0047 1.9178 1.7073 0.2043 -0.0682 0.0972 1113 LEU D CA +9382 C C . LEU D 294 ? 1.8217 1.7378 1.5337 0.2075 -0.0734 0.0984 1113 LEU D C +9383 O O . LEU D 294 ? 1.8853 1.8062 1.6052 0.2075 -0.0794 0.0968 1113 LEU D O +9384 C CB . LEU D 294 ? 1.5975 1.5109 1.2999 0.2029 -0.0692 0.1012 1113 LEU D CB +9385 C CG . LEU D 294 ? 1.8775 1.7963 1.5881 0.2021 -0.0760 0.1011 1113 LEU D CG +9386 C CD1 . LEU D 294 ? 1.7504 1.6689 1.4567 0.1991 -0.0748 0.1018 1113 LEU D CD1 +9387 C CD2 . LEU D 294 ? 2.2884 2.2092 2.0070 0.2049 -0.0807 0.1057 1113 LEU D CD2 +9388 N N . PHE D 295 ? 1.5229 1.4362 1.2341 0.2102 -0.0712 0.1011 1114 PHE D N +9389 C CA . PHE D 295 ? 1.8571 1.7729 1.5767 0.2133 -0.0756 0.1020 1114 PHE D CA +9390 C C . PHE D 295 ? 2.0509 1.9672 1.7709 0.2140 -0.0752 0.0971 1114 PHE D C +9391 O O . PHE D 295 ? 2.2303 2.1489 1.9572 0.2165 -0.0789 0.0969 1114 PHE D O +9392 C CB . PHE D 295 ? 1.9386 1.8514 1.6576 0.2160 -0.0738 0.1074 1114 PHE D CB +9393 C CG . PHE D 295 ? 2.2883 2.2042 2.0170 0.2192 -0.0793 0.1095 1114 PHE D CG +9394 C CD1 . PHE D 295 ? 2.3497 2.2694 2.0860 0.2195 -0.0850 0.1124 1114 PHE D CD1 +9395 C CD2 . PHE D 295 ? 1.9893 1.9044 1.7195 0.2218 -0.0787 0.1087 1114 PHE D CD2 +9396 C CE1 . PHE D 295 ? 2.3714 2.2940 2.1166 0.2224 -0.0900 0.1144 1114 PHE D CE1 +9397 C CE2 . PHE D 295 ? 2.1023 2.0203 1.8414 0.2247 -0.0837 0.1106 1114 PHE D CE2 +9398 C CZ . PHE D 295 ? 2.4128 2.3345 2.1594 0.2250 -0.0894 0.1135 1114 PHE D CZ +9399 N N . TYR D 296 ? 2.0659 1.9797 1.7782 0.2119 -0.0705 0.0931 1115 TYR D N +9400 C CA . TYR D 296 ? 2.0854 2.0000 1.7979 0.2120 -0.0701 0.0878 1115 TYR D CA +9401 C C . TYR D 296 ? 2.2671 2.1864 1.9841 0.2098 -0.0748 0.0841 1115 TYR D C +9402 O O . TYR D 296 ? 1.9979 1.9203 1.7199 0.2103 -0.0780 0.0804 1115 TYR D O +9403 C CB . TYR D 296 ? 2.0779 1.9874 1.7796 0.2106 -0.0626 0.0856 1115 TYR D CB +9404 C CG . TYR D 296 ? 2.2570 2.1665 1.9568 0.2102 -0.0610 0.0797 1115 TYR D CG +9405 C CD1 . TYR D 296 ? 2.5928 2.5016 2.2943 0.2129 -0.0606 0.0788 1115 TYR D CD1 +9406 C CD2 . TYR D 296 ? 2.1725 2.0826 1.8686 0.2072 -0.0599 0.0752 1115 TYR D CD2 +9407 C CE1 . TYR D 296 ? 2.6652 2.5740 2.3649 0.2124 -0.0592 0.0735 1115 TYR D CE1 +9408 C CE2 . TYR D 296 ? 2.1364 2.0465 1.8307 0.2067 -0.0584 0.0699 1115 TYR D CE2 +9409 C CZ . TYR D 296 ? 2.1392 2.0487 1.8354 0.2093 -0.0581 0.0691 1115 TYR D CZ +9410 O OH . TYR D 296 ? 1.7900 1.6995 1.4844 0.2089 -0.0567 0.0638 1115 TYR D OH +9411 N N . PHE D 297 ? 2.3192 2.2392 2.0347 0.2074 -0.0753 0.0852 1116 PHE D N +9412 C CA . PHE D 297 ? 2.1756 2.1002 1.8956 0.2053 -0.0799 0.0822 1116 PHE D CA +9413 C C . PHE D 297 ? 1.9713 1.9009 1.7025 0.2072 -0.0873 0.0838 1116 PHE D C +9414 O O . PHE D 297 ? 1.5558 1.4888 1.2927 0.2078 -0.0912 0.0804 1116 PHE D O +9415 C CB . PHE D 297 ? 2.2054 2.1291 1.9204 0.2023 -0.0782 0.0832 1116 PHE D CB +9416 C CG . PHE D 297 ? 2.5056 2.4331 2.2227 0.1996 -0.0813 0.0790 1116 PHE D CG +9417 C CD1 . PHE D 297 ? 2.2837 2.2106 1.9961 0.1977 -0.0785 0.0737 1116 PHE D CD1 +9418 C CD2 . PHE D 297 ? 2.9107 2.8426 2.6348 0.1991 -0.0870 0.0805 1116 PHE D CD2 +9419 C CE1 . PHE D 297 ? 2.5664 2.4968 2.2807 0.1952 -0.0813 0.0699 1116 PHE D CE1 +9420 C CE2 . PHE D 297 ? 2.8806 2.8159 2.6065 0.1966 -0.0899 0.0767 1116 PHE D CE2 +9421 C CZ . PHE D 297 ? 2.7981 2.7328 2.5192 0.1947 -0.0870 0.0714 1116 PHE D CZ +9422 N N . ALA D 298 ? 1.8744 1.8044 1.6087 0.2082 -0.0894 0.0890 1117 ALA D N +9423 C CA . ALA D 298 ? 2.0567 1.9911 1.8015 0.2103 -0.0962 0.0912 1117 ALA D CA +9424 C C . ALA D 298 ? 2.4283 2.3636 2.1780 0.2133 -0.0979 0.0899 1117 ALA D C +9425 O O . ALA D 298 ? 2.3178 2.2575 2.0765 0.2145 -0.1039 0.0893 1117 ALA D O +9426 C CB . ALA D 298 ? 2.0162 1.9496 1.7622 0.2114 -0.0968 0.0974 1117 ALA D CB +9427 N N . SER D 299 ? 2.6030 2.5341 2.3467 0.2143 -0.0926 0.0894 1118 SER D N +9428 C CA . SER D 299 ? 2.4318 2.3632 2.1785 0.2167 -0.0933 0.0872 1118 SER D CA +9429 C C . SER D 299 ? 2.2672 2.2021 2.0166 0.2153 -0.0959 0.0813 1118 SER D C +9430 O O . SER D 299 ? 2.4019 2.3411 2.1599 0.2165 -0.1017 0.0803 1118 SER D O +9431 C CB . SER D 299 ? 2.3332 2.2591 2.0714 0.2174 -0.0863 0.0873 1118 SER D CB +9432 O OG . SER D 299 ? 2.3283 2.2542 2.0696 0.2202 -0.0868 0.0864 1118 SER D OG +9433 N N . LYS D 300 ? 1.9083 1.8412 1.6503 0.2127 -0.0917 0.0775 1119 LYS D N +9434 C CA . LYS D 300 ? 1.9769 1.9126 1.7204 0.2112 -0.0935 0.0717 1119 LYS D CA +9435 C C . LYS D 300 ? 2.5778 2.5192 2.3295 0.2102 -0.1003 0.0706 1119 LYS D C +9436 O O . LYS D 300 ? 2.5929 2.5373 2.3477 0.2094 -0.1029 0.0660 1119 LYS D O +9437 C CB . LYS D 300 ? 1.9480 1.8805 1.6817 0.2082 -0.0876 0.0683 1119 LYS D CB +9438 C CG . LYS D 300 ? 1.8662 1.7937 1.5922 0.2091 -0.0812 0.0674 1119 LYS D CG +9439 C CD . LYS D 300 ? 1.4921 1.4209 1.2204 0.2100 -0.0819 0.0626 1119 LYS D CD +9440 C CE . LYS D 300 ? 1.8521 1.7760 1.5711 0.2097 -0.0749 0.0603 1119 LYS D CE +9441 N NZ . LYS D 300 ? 1.8799 1.8043 1.6014 0.2117 -0.0753 0.0572 1119 LYS D NZ +9442 N N . LEU D 301 ? 2.8099 2.7527 2.5649 0.2101 -0.1032 0.0747 1120 LEU D N +9443 C CA . LEU D 301 ? 2.4314 2.3796 2.1947 0.2094 -0.1099 0.0743 1120 LEU D CA +9444 C C . LEU D 301 ? 2.3467 2.2983 2.1199 0.2125 -0.1155 0.0755 1120 LEU D C +9445 O O . LEU D 301 ? 1.8822 1.8360 1.6614 0.2136 -0.1197 0.0794 1120 LEU D O +9446 C CB . LEU D 301 ? 2.1326 2.0810 1.8953 0.2080 -0.1107 0.0782 1120 LEU D CB +9447 C CG . LEU D 301 ? 2.3512 2.2967 2.1046 0.2048 -0.1056 0.0769 1120 LEU D CG +9448 C CD1 . LEU D 301 ? 2.2388 2.1845 1.9919 0.2035 -0.1065 0.0810 1120 LEU D CD1 +9449 C CD2 . LEU D 301 ? 2.1358 2.0833 1.8882 0.2023 -0.1061 0.0709 1120 LEU D CD2 +9450 N N . VAL D 302 ? 2.6538 2.6057 2.4284 0.2139 -0.1156 0.0722 1121 VAL D N +9451 C CA . VAL D 302 ? 2.9058 2.8604 2.6891 0.2170 -0.1202 0.0730 1121 VAL D CA +9452 C C . VAL D 302 ? 2.9168 2.8740 2.7032 0.2170 -0.1222 0.0674 1121 VAL D C +9453 O O . VAL D 302 ? 3.0831 3.0452 2.8777 0.2172 -0.1282 0.0660 1121 VAL D O +9454 C CB . VAL D 302 ? 2.2806 2.2315 2.0619 0.2199 -0.1170 0.0767 1121 VAL D CB +9455 C CG1 . VAL D 302 ? 2.0391 1.9922 1.8278 0.2229 -0.1207 0.0761 1121 VAL D CG1 +9456 C CG2 . VAL D 302 ? 2.0553 2.0049 1.8366 0.2205 -0.1170 0.0827 1121 VAL D CG2 +9457 N N . LEU D 303 ? 2.5877 2.5417 2.3676 0.2167 -0.1172 0.0643 1122 LEU D N +9458 C CA . LEU D 303 ? 2.7109 2.6667 2.4930 0.2171 -0.1184 0.0592 1122 LEU D CA +9459 C C . LEU D 303 ? 2.7599 2.7204 2.5464 0.2150 -0.1228 0.0550 1122 LEU D C +9460 O O . LEU D 303 ? 2.5741 2.5380 2.3671 0.2161 -0.1269 0.0522 1122 LEU D O +9461 C CB . LEU D 303 ? 2.5797 2.5309 2.3526 0.2166 -0.1115 0.0564 1122 LEU D CB +9462 C CG . LEU D 303 ? 2.3538 2.3022 2.1257 0.2195 -0.1089 0.0574 1122 LEU D CG +9463 C CD1 . LEU D 303 ? 1.8388 1.7825 1.6008 0.2186 -0.1018 0.0547 1122 LEU D CD1 +9464 C CD2 . LEU D 303 ? 1.8041 1.7562 1.5847 0.2218 -0.1140 0.0554 1122 LEU D CD2 +#