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data_1K1A
# 
_entry.id   1K1A 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.376 
_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   1K1A         pdb_00001k1a 10.2210/pdb1k1a/pdb 
RCSB  RCSB014434   ?            ?                   
WWPDB D_1000014434 ?            ?                   
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1K1B 
_pdbx_database_related.details        'Closely related crystal form of BCL3.' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1K1A 
_pdbx_database_status.recvd_initial_deposition_date   2001-09-24 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Michel, F.'      1 
'Soler-Lopez, M.' 2 
'Petosa, C.'      3 
'Cramer, P.'      4 
'Siebenlist, U.'  5 
'Mueller, C.W.'   6 
# 
_citation.id                        primary 
_citation.title                     
'Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family.' 
_citation.journal_abbrev            'EMBO J.' 
_citation.journal_volume            20 
_citation.page_first                6180 
_citation.page_last                 6190 
_citation.year                      2001 
_citation.journal_id_ASTM           EMJODG 
_citation.country                   UK 
_citation.journal_id_ISSN           0261-4189 
_citation.journal_id_CSD            0897 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   11707390 
_citation.pdbx_database_id_DOI      10.1093/emboj/20.22.6180 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Michel, F.'      1 ? 
primary 'Soler-Lopez, M.' 2 ? 
primary 'Petosa, C.'      3 ? 
primary 'Cramer, P.'      4 ? 
primary 'Siebenlist, U.'  5 ? 
primary 'Muller, C.W.'    6 ? 
# 
_cell.entry_id           1K1A 
_cell.length_a           31.703 
_cell.length_b           51.218 
_cell.length_c           64.680 
_cell.angle_alpha        90.00 
_cell.angle_beta         102.01 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1K1A 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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 'B-cell lymphoma 3-encoded protein' 25829.451 1   ? ? 'ankyrin repeat domain' ? 
2 water   nat water                               18.015    195 ? ? ?                       ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'BCL3, BCL-3 protein' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQ
TAAHLACEHRSPTCLRALLDSAAPGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVEN
NSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPA
S
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQ
TAAHLACEHRSPTCLRALLDSAAPGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVEN
NSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPA
S
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   THR n 
1 4   ARG n 
1 5   ALA n 
1 6   ASP n 
1 7   GLU n 
1 8   ASP n 
1 9   GLY n 
1 10  ASP n 
1 11  THR n 
1 12  PRO n 
1 13  LEU n 
1 14  HIS n 
1 15  ILE n 
1 16  ALA n 
1 17  VAL n 
1 18  VAL n 
1 19  GLN n 
1 20  GLY n 
1 21  ASN n 
1 22  LEU n 
1 23  PRO n 
1 24  ALA n 
1 25  VAL n 
1 26  HIS n 
1 27  ARG n 
1 28  LEU n 
1 29  VAL n 
1 30  ASN n 
1 31  LEU n 
1 32  PHE n 
1 33  GLN n 
1 34  GLN n 
1 35  GLY n 
1 36  GLY n 
1 37  ARG n 
1 38  GLU n 
1 39  LEU n 
1 40  ASP n 
1 41  ILE n 
1 42  TYR n 
1 43  ASN n 
1 44  ASN n 
1 45  LEU n 
1 46  ARG n 
1 47  GLN n 
1 48  THR n 
1 49  PRO n 
1 50  LEU n 
1 51  HIS n 
1 52  LEU n 
1 53  ALA n 
1 54  VAL n 
1 55  ILE n 
1 56  THR n 
1 57  THR n 
1 58  LEU n 
1 59  PRO n 
1 60  SER n 
1 61  VAL n 
1 62  VAL n 
1 63  ARG n 
1 64  LEU n 
1 65  LEU n 
1 66  VAL n 
1 67  THR n 
1 68  ALA n 
1 69  GLY n 
1 70  ALA n 
1 71  SER n 
1 72  PRO n 
1 73  MET n 
1 74  ALA n 
1 75  LEU n 
1 76  ASP n 
1 77  ARG n 
1 78  HIS n 
1 79  GLY n 
1 80  GLN n 
1 81  THR n 
1 82  ALA n 
1 83  ALA n 
1 84  HIS n 
1 85  LEU n 
1 86  ALA n 
1 87  CYS n 
1 88  GLU n 
1 89  HIS n 
1 90  ARG n 
1 91  SER n 
1 92  PRO n 
1 93  THR n 
1 94  CYS n 
1 95  LEU n 
1 96  ARG n 
1 97  ALA n 
1 98  LEU n 
1 99  LEU n 
1 100 ASP n 
1 101 SER n 
1 102 ALA n 
1 103 ALA n 
1 104 PRO n 
1 105 GLY n 
1 106 THR n 
1 107 LEU n 
1 108 ASP n 
1 109 LEU n 
1 110 GLU n 
1 111 ALA n 
1 112 ARG n 
1 113 ASN n 
1 114 TYR n 
1 115 ASP n 
1 116 GLY n 
1 117 LEU n 
1 118 THR n 
1 119 ALA n 
1 120 LEU n 
1 121 HIS n 
1 122 VAL n 
1 123 ALA n 
1 124 VAL n 
1 125 ASN n 
1 126 THR n 
1 127 GLU n 
1 128 CYS n 
1 129 GLN n 
1 130 GLU n 
1 131 THR n 
1 132 VAL n 
1 133 GLN n 
1 134 LEU n 
1 135 LEU n 
1 136 LEU n 
1 137 GLU n 
1 138 ARG n 
1 139 GLY n 
1 140 ALA n 
1 141 ASP n 
1 142 ILE n 
1 143 ASP n 
1 144 ALA n 
1 145 VAL n 
1 146 ASP n 
1 147 ILE n 
1 148 LYS n 
1 149 SER n 
1 150 GLY n 
1 151 ARG n 
1 152 SER n 
1 153 PRO n 
1 154 LEU n 
1 155 ILE n 
1 156 HIS n 
1 157 ALA n 
1 158 VAL n 
1 159 GLU n 
1 160 ASN n 
1 161 ASN n 
1 162 SER n 
1 163 LEU n 
1 164 SER n 
1 165 MET n 
1 166 VAL n 
1 167 GLN n 
1 168 LEU n 
1 169 LEU n 
1 170 LEU n 
1 171 GLN n 
1 172 HIS n 
1 173 GLY n 
1 174 ALA n 
1 175 ASN n 
1 176 VAL n 
1 177 ASN n 
1 178 ALA n 
1 179 GLN n 
1 180 MET n 
1 181 TYR n 
1 182 SER n 
1 183 GLY n 
1 184 SER n 
1 185 SER n 
1 186 ALA n 
1 187 LEU n 
1 188 HIS n 
1 189 SER n 
1 190 ALA n 
1 191 SER n 
1 192 GLY n 
1 193 ARG n 
1 194 GLY n 
1 195 LEU n 
1 196 LEU n 
1 197 PRO n 
1 198 LEU n 
1 199 VAL n 
1 200 ARG n 
1 201 THR n 
1 202 LEU n 
1 203 VAL n 
1 204 ARG n 
1 205 SER n 
1 206 GLY n 
1 207 ALA n 
1 208 ASP n 
1 209 SER n 
1 210 SER n 
1 211 LEU n 
1 212 LYS n 
1 213 ASN n 
1 214 CYS n 
1 215 HIS n 
1 216 ASN n 
1 217 ASP n 
1 218 THR n 
1 219 PRO n 
1 220 LEU n 
1 221 MET n 
1 222 VAL n 
1 223 ALA n 
1 224 ARG n 
1 225 SER n 
1 226 ARG n 
1 227 ARG n 
1 228 VAL n 
1 229 ILE n 
1 230 ASP n 
1 231 ILE n 
1 232 LEU n 
1 233 ARG n 
1 234 GLY n 
1 235 LYS n 
1 236 ALA n 
1 237 THR n 
1 238 ARG n 
1 239 PRO n 
1 240 ALA n 
1 241 SER n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_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               human 
_entity_src_gen.gene_src_genus                     Homo 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_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                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    BCL3_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MATRADEDGDTPLHIAVVQGNLPAVHRLVNLFQQGGRELDIYNNLRQTPLHLAVITTLPSVVRLLVTAGASPMALDRHGQ
TAAHLACEHRSPTCLRALLDSAAPGTLDLEARNYDGLTALHVAVNTECQETVQLLLERGADIDAVDIKSGRSPLIHAVEN
NSLSMVQLLLQHGANVNAQMYSGSSALHSASGRGLLPLVRTLVRSGADSSLKNCHNDTPLMVARSRRVIDILRGKATRPA
S
;
_struct_ref.pdbx_align_begin           119 
_struct_ref.pdbx_db_accession          P20749 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1K1A 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 241 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P20749 
_struct_ref_seq.db_align_beg                  119 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  359 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       119 
_struct_ref_seq.pdbx_auth_seq_align_end       359 
# 
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 
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 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          1K1A 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.99 
_exptl_crystal.density_percent_sol   38.12 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6.0 
_exptl_crystal_grow.pdbx_details    'PEG 6000, MES, pH 6.0, VAPOR DIFFUSION, HANGING DROP, temperature 293K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_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                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2000-10-28 
_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                    ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.934 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ESRF BEAMLINE ID14-1' 
_diffrn_source.pdbx_synchrotron_site       ESRF 
_diffrn_source.pdbx_synchrotron_beamline   ID14-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        0.934 
# 
_reflns.entry_id                     1K1A 
_reflns.observed_criterion_sigma_I   0 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             40 
_reflns.d_resolution_high            1.80 
_reflns.number_obs                   17021 
_reflns.number_all                   17021 
_reflns.percent_possible_obs         89.8 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.0720000 
_reflns.pdbx_netI_over_sigmaI        10.5 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              2.7 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.80 
_reflns_shell.d_res_low              1.86 
_reflns_shell.percent_possible_all   77.8 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.6970000 
_reflns_shell.meanI_over_sigI_obs    1.65 
_reflns_shell.pdbx_redundancy        1.73 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      1479 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1K1A 
_refine.ls_number_reflns_obs                     16328 
_refine.ls_number_reflns_all                     16328 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             20.00 
_refine.ls_d_res_high                            1.86 
_refine.ls_percent_reflns_obs                    89.8 
_refine.ls_R_factor_obs                          0.2004000 
_refine.ls_R_factor_all                          0.2004000 
_refine.ls_R_factor_R_work                       0.1989900 
_refine.ls_R_factor_R_free                       0.2285900 
_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                  828 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               21.105 
_refine.aniso_B[1][1]                            -0.09 
_refine.aniso_B[2][2]                            -1.27 
_refine.aniso_B[3][3]                            1.35 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.04 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
;RESIDUES SER178,VAL179,LEU182,GLN251,ARG269,SER307
PRESENT DOUBLE CONFORMATIONS.
;
_refine.pdbx_starting_model                      1ikn 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  0.15154 
_refine.overall_SU_B                             3.68115 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            0.11055 
_refine.pdbx_overall_ESU_R                       0.18488 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_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        1729 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             195 
_refine_hist.number_atoms_total               1924 
_refine_hist.d_res_high                       1.86 
_refine_hist.d_res_low                        20.00 
# 
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 
p_bond_d       0.007 0.021 ? ? 'X-RAY DIFFRACTION' ? 
p_mcbond_it    0.578 1.500 ? ? 'X-RAY DIFFRACTION' ? 
p_mcangle_it   1.104 2.000 ? ? 'X-RAY DIFFRACTION' ? 
p_scbond_it    1.789 3.000 ? ? 'X-RAY DIFFRACTION' ? 
p_scangle_it   3.103 4.500 ? ? 'X-RAY DIFFRACTION' ? 
p_plane_restr  0.004 0.020 ? ? 'X-RAY DIFFRACTION' ? 
p_chiral_restr 0.070 0.200 ? ? 'X-RAY DIFFRACTION' ? 
# 
_struct.entry_id                  1K1A 
_struct.title                     
'Crystal structure of the ankyrin repeat domain of Bcl-3: a unique member of the IkappaB protein family' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1K1A 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
_struct_keywords.text            'Bcl-3, NF-kappaB transcription factors, IkappaB proteins, TRANSCRIPTION' 
# 
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 2 ? 
# 
_struct_biol.id                    1 
_struct_biol.pdbx_parent_biol_id   ? 
_struct_biol.details               ? 
# 
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  THR A 11  ? GLN A 19  ? THR A 129 GLN A 137 1 ? 9  
HELX_P HELX_P2  2  ASN A 21  ? GLY A 35  ? ASN A 139 GLY A 153 1 ? 15 
HELX_P HELX_P3  3  THR A 48  ? THR A 56  ? THR A 166 THR A 174 1 ? 9  
HELX_P HELX_P4  4  LEU A 58  ? ALA A 68  ? LEU A 176 ALA A 186 1 ? 11 
HELX_P HELX_P5  5  THR A 81  ? HIS A 89  ? THR A 199 HIS A 207 1 ? 9  
HELX_P HELX_P6  6  SER A 91  ? ALA A 102 ? SER A 209 ALA A 220 1 ? 12 
HELX_P HELX_P7  7  THR A 118 ? GLU A 127 ? THR A 236 GLU A 245 1 ? 10 
HELX_P HELX_P8  8  CYS A 128 ? ARG A 138 ? CYS A 246 ARG A 256 1 ? 11 
HELX_P HELX_P9  9  SER A 152 ? ASN A 160 ? SER A 270 ASN A 278 1 ? 9  
HELX_P HELX_P10 10 SER A 162 ? HIS A 172 ? SER A 280 HIS A 290 1 ? 11 
HELX_P HELX_P11 11 SER A 185 ? GLY A 194 ? SER A 303 GLY A 312 1 ? 10 
HELX_P HELX_P12 12 LEU A 195 ? SER A 205 ? LEU A 313 SER A 323 1 ? 11 
HELX_P HELX_P13 13 SER A 225 ? ARG A 233 ? SER A 343 ARG A 351 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_database_PDB_matrix.entry_id          1K1A 
_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 
# 
_atom_sites.entry_id                    1K1A 
_atom_sites.fract_transf_matrix[1][1]   0.031543 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006710 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.019524 
_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]   0.015807 
_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   . GLU A 1 7   ? 14.581 13.195  3.479  1.00 22.25 ? 125 GLU A N   1 
ATOM   2    C CA  . GLU A 1 7   ? 14.496 14.621  3.901  1.00 20.31 ? 125 GLU A CA  1 
ATOM   3    C C   . GLU A 1 7   ? 14.969 14.841  5.327  1.00 19.84 ? 125 GLU A C   1 
ATOM   4    O O   . GLU A 1 7   ? 14.624 14.071  6.225  1.00 23.21 ? 125 GLU A O   1 
ATOM   5    C CB  . GLU A 1 7   ? 13.765 15.508  2.985  1.00 21.39 ? 125 GLU A CB  1 
ATOM   6    C CG  . GLU A 1 7   ? 14.084 15.489  1.490  1.00 20.87 ? 125 GLU A CG  1 
ATOM   7    C CD  . GLU A 1 7   ? 14.884 16.707  1.033  1.00 20.86 ? 125 GLU A CD  1 
ATOM   8    O OE1 . GLU A 1 7   ? 14.534 17.888  1.416  1.00 25.80 ? 125 GLU A OE1 1 
ATOM   9    O OE2 . GLU A 1 7   ? 15.906 16.556  0.268  1.00 25.92 ? 125 GLU A OE2 1 
ATOM   10   N N   . ASP A 1 8   ? 15.801 16.049  5.369  1.00 20.77 ? 126 ASP A N   1 
ATOM   11   C CA  . ASP A 1 8   ? 16.385 16.475  6.632  1.00 20.90 ? 126 ASP A CA  1 
ATOM   12   C C   . ASP A 1 8   ? 15.350 16.558  7.738  1.00 23.20 ? 126 ASP A C   1 
ATOM   13   O O   . ASP A 1 8   ? 14.313 17.195  7.581  1.00 22.64 ? 126 ASP A O   1 
ATOM   14   C CB  . ASP A 1 8   ? 17.134 17.790  6.480  1.00 20.72 ? 126 ASP A CB  1 
ATOM   15   C CG  . ASP A 1 8   ? 18.140 18.064  7.599  1.00 20.54 ? 126 ASP A CG  1 
ATOM   16   O OD1 . ASP A 1 8   ? 19.000 17.162  7.926  1.00 25.18 ? 126 ASP A OD1 1 
ATOM   17   O OD2 . ASP A 1 8   ? 18.125 19.196  8.214  1.00 24.39 ? 126 ASP A OD2 1 
ATOM   18   N N   . GLY A 1 9   ? 15.629 15.909  8.864  1.00 30.89 ? 127 GLY A N   1 
ATOM   19   C CA  . GLY A 1 9   ? 14.683 15.881  9.965  1.00 29.68 ? 127 GLY A CA  1 
ATOM   20   C C   . GLY A 1 9   ? 13.710 14.732  9.800  1.00 28.95 ? 127 GLY A C   1 
ATOM   21   O O   . GLY A 1 9   ? 12.809 14.541  10.617 1.00 29.06 ? 127 GLY A O   1 
ATOM   22   N N   . ASP A 1 10  ? 13.882 13.981  8.718  1.00 28.10 ? 128 ASP A N   1 
ATOM   23   C CA  . ASP A 1 10  ? 13.082 12.790  8.460  1.00 27.57 ? 128 ASP A CA  1 
ATOM   24   C C   . ASP A 1 10  ? 13.852 11.549  8.881  1.00 26.16 ? 128 ASP A C   1 
ATOM   25   O O   . ASP A 1 10  ? 14.836 11.177  8.244  1.00 26.12 ? 128 ASP A O   1 
ATOM   26   C CB  . ASP A 1 10  ? 12.759 12.666  6.970  1.00 28.21 ? 128 ASP A CB  1 
ATOM   27   C CG  . ASP A 1 10  ? 11.528 13.439  6.574  1.00 30.26 ? 128 ASP A CG  1 
ATOM   28   O OD1 . ASP A 1 10  ? 10.646 13.585  7.446  0.00 36.17 ? 128 ASP A OD1 1 
ATOM   29   O OD2 . ASP A 1 10  ? 11.277 13.733  5.379  1.00 34.30 ? 128 ASP A OD2 1 
ATOM   30   N N   . THR A 1 11  ? 13.406 10.905  9.950  1.00 22.61 ? 129 THR A N   1 
ATOM   31   C CA  . THR A 1 11  ? 14.029 9.663   10.384 1.00 18.72 ? 129 THR A CA  1 
ATOM   32   C C   . THR A 1 11  ? 12.964 8.649   10.777 1.00 18.31 ? 129 THR A C   1 
ATOM   33   O O   . THR A 1 11  ? 12.716 8.413   11.957 1.00 18.02 ? 129 THR A O   1 
ATOM   34   C CB  . THR A 1 11  ? 14.937 9.920   11.591 1.00 18.43 ? 129 THR A CB  1 
ATOM   35   O OG1 . THR A 1 11  ? 14.328 10.867  12.456 1.00 20.73 ? 129 THR A OG1 1 
ATOM   36   C CG2 . THR A 1 11  ? 16.308 10.471  11.200 1.00 21.48 ? 129 THR A CG2 1 
ATOM   37   N N   . PRO A 1 12  ? 12.337 8.051   9.772  1.00 20.18 ? 130 PRO A N   1 
ATOM   38   C CA  . PRO A 1 12  ? 11.236 7.107   9.988  1.00 19.20 ? 130 PRO A CA  1 
ATOM   39   C C   . PRO A 1 12  ? 11.675 5.851   10.729 1.00 18.09 ? 130 PRO A C   1 
ATOM   40   O O   . PRO A 1 12  ? 10.923 5.343   11.570 1.00 18.15 ? 130 PRO A O   1 
ATOM   41   C CB  . PRO A 1 12  ? 10.797 6.763   8.564  1.00 19.45 ? 130 PRO A CB  1 
ATOM   42   C CG  . PRO A 1 12  ? 12.017 7.022   7.741  1.00 19.45 ? 130 PRO A CG  1 
ATOM   43   C CD  . PRO A 1 12  ? 12.617 8.256   8.339  1.00 20.26 ? 130 PRO A CD  1 
ATOM   44   N N   . LEU A 1 13  ? 12.876 5.360   10.440 1.00 16.95 ? 131 LEU A N   1 
ATOM   45   C CA  . LEU A 1 13  ? 13.362 4.159   11.101 1.00 15.73 ? 131 LEU A CA  1 
ATOM   46   C C   . LEU A 1 13  ? 13.678 4.461   12.559 1.00 14.83 ? 131 LEU A C   1 
ATOM   47   O O   . LEU A 1 13  ? 13.407 3.649   13.442 1.00 14.05 ? 131 LEU A O   1 
ATOM   48   C CB  . LEU A 1 13  ? 14.589 3.600   10.377 1.00 15.87 ? 131 LEU A CB  1 
ATOM   49   C CG  . LEU A 1 13  ? 15.085 2.218   10.806 1.00 16.17 ? 131 LEU A CG  1 
ATOM   50   C CD1 . LEU A 1 13  ? 13.952 1.200   10.865 1.00 14.80 ? 131 LEU A CD1 1 
ATOM   51   C CD2 . LEU A 1 13  ? 16.196 1.735   9.856  1.00 16.50 ? 131 LEU A CD2 1 
ATOM   52   N N   . HIS A 1 14  ? 14.249 5.632   12.813 1.00 14.56 ? 132 HIS A N   1 
ATOM   53   C CA  . HIS A 1 14  ? 14.533 6.036   14.184 1.00 14.42 ? 132 HIS A CA  1 
ATOM   54   C C   . HIS A 1 14  ? 13.237 6.056   14.979 1.00 14.37 ? 132 HIS A C   1 
ATOM   55   O O   . HIS A 1 14  ? 13.176 5.539   16.088 1.00 14.36 ? 132 HIS A O   1 
ATOM   56   C CB  . HIS A 1 14  ? 15.196 7.414   14.226 1.00 14.52 ? 132 HIS A CB  1 
ATOM   57   C CG  . HIS A 1 14  ? 16.567 7.440   13.622 1.00 14.84 ? 132 HIS A CG  1 
ATOM   58   N ND1 . HIS A 1 14  ? 17.715 7.526   14.381 1.00 16.82 ? 132 HIS A ND1 1 
ATOM   59   C CD2 . HIS A 1 14  ? 16.972 7.397   12.332 1.00 14.27 ? 132 HIS A CD2 1 
ATOM   60   C CE1 . HIS A 1 14  ? 18.769 7.525   13.586 1.00 14.24 ? 132 HIS A CE1 1 
ATOM   61   N NE2 . HIS A 1 14  ? 18.347 7.458   12.337 1.00 15.75 ? 132 HIS A NE2 1 
ATOM   62   N N   . ILE A 1 15  ? 12.203 6.651   14.394 1.00 13.76 ? 133 ILE A N   1 
ATOM   63   C CA  . ILE A 1 15  ? 10.891 6.751   15.040 1.00 14.17 ? 133 ILE A CA  1 
ATOM   64   C C   . ILE A 1 15  ? 10.277 5.383   15.331 1.00 13.36 ? 133 ILE A C   1 
ATOM   65   O O   . ILE A 1 15  ? 9.792  5.138   16.436 1.00 13.41 ? 133 ILE A O   1 
ATOM   66   C CB  . ILE A 1 15  ? 9.928  7.564   14.161 1.00 14.70 ? 133 ILE A CB  1 
ATOM   67   C CG1 . ILE A 1 15  ? 10.469 8.970   13.909 1.00 17.09 ? 133 ILE A CG1 1 
ATOM   68   C CG2 . ILE A 1 15  ? 8.534  7.584   14.771 1.00 15.13 ? 133 ILE A CG2 1 
ATOM   69   C CD1 . ILE A 1 15  ? 10.678 9.792   15.150 1.00 19.85 ? 133 ILE A CD1 1 
ATOM   70   N N   . ALA A 1 16  ? 10.297 4.499   14.337 1.00 13.23 ? 134 ALA A N   1 
ATOM   71   C CA  . ALA A 1 16  ? 9.753  3.154   14.490 1.00 12.92 ? 134 ALA A CA  1 
ATOM   72   C C   . ALA A 1 16  ? 10.407 2.429   15.665 1.00 13.02 ? 134 ALA A C   1 
ATOM   73   O O   . ALA A 1 16  ? 9.750  1.674   16.385 1.00 13.22 ? 134 ALA A O   1 
ATOM   74   C CB  . ALA A 1 16  ? 9.928  2.345   13.198 1.00 13.38 ? 134 ALA A CB  1 
ATOM   75   N N   . VAL A 1 17  ? 11.701 2.681   15.872 1.00 12.50 ? 135 VAL A N   1 
ATOM   76   C CA  . VAL A 1 17  ? 12.429 2.030   16.954 1.00 11.94 ? 135 VAL A CA  1 
ATOM   77   C C   . VAL A 1 17  ? 11.992 2.540   18.313 1.00 12.41 ? 135 VAL A C   1 
ATOM   78   O O   . VAL A 1 17  ? 11.641 1.758   19.188 1.00 13.18 ? 135 VAL A O   1 
ATOM   79   C CB  . VAL A 1 17  ? 13.951 2.199   16.810 1.00 11.49 ? 135 VAL A CB  1 
ATOM   80   C CG1 . VAL A 1 17  ? 14.658 1.722   18.084 1.00 10.51 ? 135 VAL A CG1 1 
ATOM   81   C CG2 . VAL A 1 17  ? 14.443 1.431   15.618 1.00 10.56 ? 135 VAL A CG2 1 
ATOM   82   N N   . VAL A 1 18  ? 11.991 3.856   18.476 1.00 12.69 ? 136 VAL A N   1 
ATOM   83   C CA  . VAL A 1 18  ? 11.613 4.481   19.734 1.00 13.38 ? 136 VAL A CA  1 
ATOM   84   C C   . VAL A 1 18  ? 10.152 4.185   20.125 1.00 13.13 ? 136 VAL A C   1 
ATOM   85   O O   . VAL A 1 18  ? 9.835  4.053   21.316 1.00 12.30 ? 136 VAL A O   1 
ATOM   86   C CB  . VAL A 1 18  ? 11.880 5.991   19.685 1.00 13.59 ? 136 VAL A CB  1 
ATOM   87   C CG1 . VAL A 1 18  ? 11.173 6.726   20.818 1.00 15.64 ? 136 VAL A CG1 1 
ATOM   88   C CG2 . VAL A 1 18  ? 13.374 6.247   19.731 1.00 15.12 ? 136 VAL A CG2 1 
ATOM   89   N N   . GLN A 1 19  ? 9.291  4.016   19.123 1.00 12.73 ? 137 GLN A N   1 
ATOM   90   C CA  . GLN A 1 19  ? 7.873  3.710   19.368 1.00 13.06 ? 137 GLN A CA  1 
ATOM   91   C C   . GLN A 1 19  ? 7.630  2.224   19.619 1.00 13.19 ? 137 GLN A C   1 
ATOM   92   O O   . GLN A 1 19  ? 6.487  1.792   19.855 1.00 13.00 ? 137 GLN A O   1 
ATOM   93   C CB  . GLN A 1 19  ? 7.004  4.210   18.208 1.00 12.98 ? 137 GLN A CB  1 
ATOM   94   C CG  . GLN A 1 19  ? 7.035  5.725   18.044 1.00 14.07 ? 137 GLN A CG  1 
ATOM   95   C CD  . GLN A 1 19  ? 6.055  6.225   16.991 1.00 15.26 ? 137 GLN A CD  1 
ATOM   96   O OE1 . GLN A 1 19  ? 5.588  5.459   16.154 1.00 14.86 ? 137 GLN A OE1 1 
ATOM   97   N NE2 . GLN A 1 19  ? 5.742  7.510   17.041 1.00 16.79 ? 137 GLN A NE2 1 
ATOM   98   N N   . GLY A 1 20  ? 8.700  1.435   19.555 1.00 13.60 ? 138 GLY A N   1 
ATOM   99   C CA  . GLY A 1 20  ? 8.629  0.015   19.843 1.00 14.58 ? 138 GLY A CA  1 
ATOM   100  C C   . GLY A 1 20  ? 7.747  -0.752  18.881 1.00 14.83 ? 138 GLY A C   1 
ATOM   101  O O   . GLY A 1 20  ? 7.079  -1.698  19.257 1.00 15.75 ? 138 GLY A O   1 
ATOM   102  N N   . ASN A 1 21  ? 7.765  -0.354  17.624 1.00 14.88 ? 139 ASN A N   1 
ATOM   103  C CA  . ASN A 1 21  ? 6.940  -0.992  16.618 1.00 14.60 ? 139 ASN A CA  1 
ATOM   104  C C   . ASN A 1 21  ? 7.786  -1.900  15.731 1.00 14.68 ? 139 ASN A C   1 
ATOM   105  O O   . ASN A 1 21  ? 8.239  -1.484  14.661 1.00 14.09 ? 139 ASN A O   1 
ATOM   106  C CB  . ASN A 1 21  ? 6.250  0.090   15.785 1.00 14.22 ? 139 ASN A CB  1 
ATOM   107  C CG  . ASN A 1 21  ? 5.149  -0.458  14.896 1.00 14.40 ? 139 ASN A CG  1 
ATOM   108  O OD1 . ASN A 1 21  ? 5.148  -1.629  14.534 1.00 13.63 ? 139 ASN A OD1 1 
ATOM   109  N ND2 . ASN A 1 21  ? 4.218  0.409   14.516 1.00 13.39 ? 139 ASN A ND2 1 
ATOM   110  N N   . LEU A 1 22  ? 7.981  -3.146  16.176 1.00 14.99 ? 140 LEU A N   1 
ATOM   111  C CA  . LEU A 1 22  ? 8.816  -4.114  15.458 1.00 15.78 ? 140 LEU A CA  1 
ATOM   112  C C   . LEU A 1 22  ? 8.377  -4.359  14.004 1.00 15.73 ? 140 LEU A C   1 
ATOM   113  O O   . LEU A 1 22  ? 9.210  -4.380  13.106 1.00 15.26 ? 140 LEU A O   1 
ATOM   114  C CB  . LEU A 1 22  ? 8.918  -5.437  16.238 1.00 16.94 ? 140 LEU A CB  1 
ATOM   115  C CG  . LEU A 1 22  ? 9.855  -6.534  15.715 1.00 18.13 ? 140 LEU A CG  1 
ATOM   116  C CD1 . LEU A 1 22  ? 11.295 -6.108  15.779 1.00 20.05 ? 140 LEU A CD1 1 
ATOM   117  C CD2 . LEU A 1 22  ? 9.666  -7.819  16.505 1.00 20.81 ? 140 LEU A CD2 1 
ATOM   118  N N   . PRO A 1 23  ? 7.079  -4.560  13.772 1.00 15.34 ? 141 PRO A N   1 
ATOM   119  C CA  . PRO A 1 23  ? 6.576  -4.745  12.405 1.00 15.34 ? 141 PRO A CA  1 
ATOM   120  C C   . PRO A 1 23  ? 6.957  -3.587  11.475 1.00 15.24 ? 141 PRO A C   1 
ATOM   121  O O   . PRO A 1 23  ? 7.347  -3.840  10.331 1.00 15.77 ? 141 PRO A O   1 
ATOM   122  C CB  . PRO A 1 23  ? 5.051  -4.805  12.595 1.00 15.71 ? 141 PRO A CB  1 
ATOM   123  C CG  . PRO A 1 23  ? 4.867  -5.287  13.988 1.00 15.61 ? 141 PRO A CG  1 
ATOM   124  C CD  . PRO A 1 23  ? 6.013  -4.684  14.778 1.00 15.53 ? 141 PRO A CD  1 
ATOM   125  N N   . ALA A 1 24  ? 6.850  -2.345  11.950 1.00 14.96 ? 142 ALA A N   1 
ATOM   126  C CA  . ALA A 1 24  ? 7.221  -1.188  11.129 1.00 14.29 ? 142 ALA A CA  1 
ATOM   127  C C   . ALA A 1 24  ? 8.723  -1.188  10.841 1.00 14.83 ? 142 ALA A C   1 
ATOM   128  O O   . ALA A 1 24  ? 9.158  -0.861  9.726  1.00 14.51 ? 142 ALA A O   1 
ATOM   129  C CB  . ALA A 1 24  ? 6.795  0.120   11.792 1.00 14.11 ? 142 ALA A CB  1 
ATOM   130  N N   . VAL A 1 25  ? 9.507  -1.578  11.839 1.00 14.04 ? 143 VAL A N   1 
ATOM   131  C CA  . VAL A 1 25  ? 10.956 -1.656  11.678 1.00 14.85 ? 143 VAL A CA  1 
ATOM   132  C C   . VAL A 1 25  ? 11.302 -2.635  10.570 1.00 15.47 ? 143 VAL A C   1 
ATOM   133  O O   . VAL A 1 25  ? 12.101 -2.328  9.682  1.00 15.51 ? 143 VAL A O   1 
ATOM   134  C CB  . VAL A 1 25  ? 11.637 -2.099  12.977 1.00 14.70 ? 143 VAL A CB  1 
ATOM   135  C CG1 . VAL A 1 25  ? 13.116 -2.441  12.731 1.00 13.78 ? 143 VAL A CG1 1 
ATOM   136  C CG2 . VAL A 1 25  ? 11.496 -1.009  14.028 1.00 14.53 ? 143 VAL A CG2 1 
ATOM   137  N N   . HIS A 1 26  ? 10.691 -3.813  10.621 1.00 15.97 ? 144 HIS A N   1 
ATOM   138  C CA  . HIS A 1 26  ? 10.917 -4.833  9.612  1.00 17.43 ? 144 HIS A CA  1 
ATOM   139  C C   . HIS A 1 26  ? 10.580 -4.292  8.220  1.00 17.64 ? 144 HIS A C   1 
ATOM   140  O O   . HIS A 1 26  ? 11.369 -4.417  7.279  1.00 17.01 ? 144 HIS A O   1 
ATOM   141  C CB  . HIS A 1 26  ? 10.068 -6.066  9.921  1.00 18.15 ? 144 HIS A CB  1 
ATOM   142  C CG  . HIS A 1 26  ? 10.567 -7.324  9.282  1.00 21.56 ? 144 HIS A CG  1 
ATOM   143  N ND1 . HIS A 1 26  ? 11.433 -8.188  9.918  1.00 23.75 ? 144 HIS A ND1 1 
ATOM   144  C CD2 . HIS A 1 26  ? 10.300 -7.879  8.075  1.00 24.66 ? 144 HIS A CD2 1 
ATOM   145  C CE1 . HIS A 1 26  ? 11.692 -9.212  9.124  1.00 26.41 ? 144 HIS A CE1 1 
ATOM   146  N NE2 . HIS A 1 26  ? 11.014 -9.051  8.000  1.00 26.66 ? 144 HIS A NE2 1 
ATOM   147  N N   . ARG A 1 27  ? 9.404  -3.691  8.092  1.00 17.43 ? 145 ARG A N   1 
ATOM   148  C CA  . ARG A 1 27  ? 8.979  -3.137  6.810  1.00 18.36 ? 145 ARG A CA  1 
ATOM   149  C C   . ARG A 1 27  ? 9.993  -2.121  6.278  1.00 17.91 ? 145 ARG A C   1 
ATOM   150  O O   . ARG A 1 27  ? 10.398 -2.177  5.107  1.00 17.66 ? 145 ARG A O   1 
ATOM   151  C CB  . ARG A 1 27  ? 7.597  -2.496  6.947  1.00 18.42 ? 145 ARG A CB  1 
ATOM   152  C CG  . ARG A 1 27  ? 7.263  -1.461  5.876  1.00 22.14 ? 145 ARG A CG  1 
ATOM   153  C CD  . ARG A 1 27  ? 5.793  -1.007  5.892  1.00 27.00 ? 145 ARG A CD  1 
ATOM   154  N NE  . ARG A 1 27  ? 5.532  0.231   6.641  1.00 31.37 ? 145 ARG A NE  1 
ATOM   155  C CZ  . ARG A 1 27  ? 6.197  0.646   7.723  1.00 33.21 ? 145 ARG A CZ  1 
ATOM   156  N NH1 . ARG A 1 27  ? 5.850  1.784   8.310  1.00 34.62 ? 145 ARG A NH1 1 
ATOM   157  N NH2 . ARG A 1 27  ? 7.201  -0.062  8.219  1.00 33.52 ? 145 ARG A NH2 1 
ATOM   158  N N   . LEU A 1 28  ? 10.415 -1.212  7.149  1.00 17.50 ? 146 LEU A N   1 
ATOM   159  C CA  . LEU A 1 28  ? 11.380 -0.176  6.795  1.00 18.10 ? 146 LEU A CA  1 
ATOM   160  C C   . LEU A 1 28  ? 12.772 -0.732  6.459  1.00 18.34 ? 146 LEU A C   1 
ATOM   161  O O   . LEU A 1 28  ? 13.468 -0.208  5.582  1.00 18.02 ? 146 LEU A O   1 
ATOM   162  C CB  . LEU A 1 28  ? 11.490 0.845   7.926  1.00 18.09 ? 146 LEU A CB  1 
ATOM   163  C CG  . LEU A 1 28  ? 10.324 1.820   8.044  1.00 18.77 ? 146 LEU A CG  1 
ATOM   164  C CD1 . LEU A 1 28  ? 10.438 2.620   9.330  1.00 19.60 ? 146 LEU A CD1 1 
ATOM   165  C CD2 . LEU A 1 28  ? 10.298 2.746   6.842  1.00 18.96 ? 146 LEU A CD2 1 
ATOM   166  N N   . VAL A 1 29  ? 13.186 -1.770  7.174  1.00 18.63 ? 147 VAL A N   1 
ATOM   167  C CA  . VAL A 1 29  ? 14.468 -2.406  6.887  1.00 19.42 ? 147 VAL A CA  1 
ATOM   168  C C   . VAL A 1 29  ? 14.457 -3.008  5.472  1.00 20.61 ? 147 VAL A C   1 
ATOM   169  O O   . VAL A 1 29  ? 15.413 -2.841  4.708  1.00 20.26 ? 147 VAL A O   1 
ATOM   170  C CB  . VAL A 1 29  ? 14.834 -3.459  7.944  1.00 19.27 ? 147 VAL A CB  1 
ATOM   171  C CG1 . VAL A 1 29  ? 15.922 -4.400  7.418  1.00 18.58 ? 147 VAL A CG1 1 
ATOM   172  C CG2 . VAL A 1 29  ? 15.283 -2.762  9.244  1.00 18.05 ? 147 VAL A CG2 1 
ATOM   173  N N   . ASN A 1 30  ? 13.357 -3.670  5.122  1.00 21.91 ? 148 ASN A N   1 
ATOM   174  C CA  . ASN A 1 30  ? 13.181 -4.208  3.775  1.00 23.66 ? 148 ASN A CA  1 
ATOM   175  C C   . ASN A 1 30  ? 13.218 -3.103  2.719  1.00 24.03 ? 148 ASN A C   1 
ATOM   176  O O   . ASN A 1 30  ? 13.863 -3.246  1.682  1.00 24.04 ? 148 ASN A O   1 
ATOM   177  C CB  . ASN A 1 30  ? 11.870 -5.003  3.674  1.00 24.29 ? 148 ASN A CB  1 
ATOM   178  C CG  . ASN A 1 30  ? 11.910 -6.297  4.467  1.00 26.38 ? 148 ASN A CG  1 
ATOM   179  O OD1 . ASN A 1 30  ? 12.981 -6.875  4.685  1.00 30.20 ? 148 ASN A OD1 1 
ATOM   180  N ND2 . ASN A 1 30  ? 10.745 -6.755  4.916  1.00 28.18 ? 148 ASN A ND2 1 
ATOM   181  N N   . LEU A 1 31  ? 12.536 -1.997  2.997  1.00 24.62 ? 149 LEU A N   1 
ATOM   182  C CA  . LEU A 1 31  ? 12.507 -0.849  2.093  1.00 25.56 ? 149 LEU A CA  1 
ATOM   183  C C   . LEU A 1 31  ? 13.896 -0.238  1.889  1.00 25.68 ? 149 LEU A C   1 
ATOM   184  O O   . LEU A 1 31  ? 14.268 0.113   0.772  1.00 25.52 ? 149 LEU A O   1 
ATOM   185  C CB  . LEU A 1 31  ? 11.555 0.219   2.629  1.00 25.86 ? 149 LEU A CB  1 
ATOM   186  C CG  . LEU A 1 31  ? 10.275 0.492   1.841  1.00 28.50 ? 149 LEU A CG  1 
ATOM   187  C CD1 . LEU A 1 31  ? 9.052  0.324   2.730  1.00 29.31 ? 149 LEU A CD1 1 
ATOM   188  C CD2 . LEU A 1 31  ? 10.321 1.915   1.260  1.00 30.13 ? 149 LEU A CD2 1 
ATOM   189  N N   . PHE A 1 32  ? 14.651 -0.111  2.976  1.00 25.74 ? 150 PHE A N   1 
ATOM   190  C CA  . PHE A 1 32  ? 15.996 0.458   2.920  1.00 26.49 ? 150 PHE A CA  1 
ATOM   191  C C   . PHE A 1 32  ? 16.923 -0.390  2.064  1.00 27.15 ? 150 PHE A C   1 
ATOM   192  O O   . PHE A 1 32  ? 17.673 0.137   1.237  1.00 27.06 ? 150 PHE A O   1 
ATOM   193  C CB  . PHE A 1 32  ? 16.593 0.588   4.328  1.00 26.11 ? 150 PHE A CB  1 
ATOM   194  C CG  . PHE A 1 32  ? 16.256 1.880   5.016  1.00 25.88 ? 150 PHE A CG  1 
ATOM   195  C CD1 . PHE A 1 32  ? 14.974 2.401   4.954  1.00 25.42 ? 150 PHE A CD1 1 
ATOM   196  C CD2 . PHE A 1 32  ? 17.223 2.574   5.727  1.00 25.18 ? 150 PHE A CD2 1 
ATOM   197  C CE1 . PHE A 1 32  ? 14.659 3.592   5.592  1.00 26.11 ? 150 PHE A CE1 1 
ATOM   198  C CE2 . PHE A 1 32  ? 16.916 3.766   6.363  1.00 26.35 ? 150 PHE A CE2 1 
ATOM   199  C CZ  . PHE A 1 32  ? 15.634 4.278   6.294  1.00 25.97 ? 150 PHE A CZ  1 
ATOM   200  N N   . GLN A 1 33  ? 16.870 -1.697  2.283  1.00 27.96 ? 151 GLN A N   1 
ATOM   201  C CA  . GLN A 1 33  ? 17.723 -2.651  1.581  1.00 29.27 ? 151 GLN A CA  1 
ATOM   202  C C   . GLN A 1 33  ? 17.431 -2.708  0.085  1.00 29.90 ? 151 GLN A C   1 
ATOM   203  O O   . GLN A 1 33  ? 18.328 -2.946  -0.718 1.00 30.15 ? 151 GLN A O   1 
ATOM   204  C CB  . GLN A 1 33  ? 17.592 -4.041  2.201  1.00 29.20 ? 151 GLN A CB  1 
ATOM   205  C CG  . GLN A 1 33  ? 18.166 -4.152  3.607  1.00 30.72 ? 151 GLN A CG  1 
ATOM   206  C CD  . GLN A 1 33  ? 18.070 -5.557  4.169  1.00 31.93 ? 151 GLN A CD  1 
ATOM   207  O OE1 . GLN A 1 33  ? 18.974 -6.010  4.876  1.00 33.15 ? 151 GLN A OE1 1 
ATOM   208  N NE2 . GLN A 1 33  ? 16.979 -6.252  3.856  1.00 32.13 ? 151 GLN A NE2 1 
ATOM   209  N N   . GLN A 1 34  ? 16.178 -2.473  -0.286 1.00 30.37 ? 152 GLN A N   1 
ATOM   210  C CA  . GLN A 1 34  ? 15.790 -2.471  -1.690 1.00 30.93 ? 152 GLN A CA  1 
ATOM   211  C C   . GLN A 1 34  ? 16.376 -1.271  -2.423 1.00 31.15 ? 152 GLN A C   1 
ATOM   212  O O   . GLN A 1 34  ? 16.602 -1.323  -3.633 1.00 31.44 ? 152 GLN A O   1 
ATOM   213  C CB  . GLN A 1 34  ? 14.269 -2.457  -1.826 1.00 31.08 ? 152 GLN A CB  1 
ATOM   214  C CG  . GLN A 1 34  ? 13.594 -3.742  -1.404 1.00 31.87 ? 152 GLN A CG  1 
ATOM   215  C CD  . GLN A 1 34  ? 12.090 -3.698  -1.617 1.00 33.49 ? 152 GLN A CD  1 
ATOM   216  O OE1 . GLN A 1 34  ? 11.265 -4.331  -0.761 0.00 35.08 ? 152 GLN A OE1 1 
ATOM   217  N NE2 . GLN A 1 34  ? 11.649 -2.819  -2.514 1.00 33.82 ? 152 GLN A NE2 1 
ATOM   218  N N   . GLY A 1 35  ? 16.626 -0.190  -1.689 1.00 31.08 ? 153 GLY A N   1 
ATOM   219  C CA  . GLY A 1 35  ? 17.141 1.027   -2.287 1.00 31.13 ? 153 GLY A CA  1 
ATOM   220  C C   . GLY A 1 35  ? 18.617 1.273   -2.034 1.00 31.26 ? 153 GLY A C   1 
ATOM   221  O O   . GLY A 1 35  ? 19.126 2.366   -2.295 1.00 31.27 ? 153 GLY A O   1 
ATOM   222  N N   . GLY A 1 36  ? 19.303 0.263   -1.519 1.00 31.01 ? 154 GLY A N   1 
ATOM   223  C CA  . GLY A 1 36  ? 20.720 0.374   -1.226 1.00 31.13 ? 154 GLY A CA  1 
ATOM   224  C C   . GLY A 1 36  ? 21.060 1.340   -0.101 1.00 30.84 ? 154 GLY A C   1 
ATOM   225  O O   . GLY A 1 36  ? 22.220 1.711   0.069  1.00 31.27 ? 154 GLY A O   1 
ATOM   226  N N   . ARG A 1 37  ? 20.057 1.739   0.675  1.00 30.41 ? 155 ARG A N   1 
ATOM   227  C CA  . ARG A 1 37  ? 20.274 2.678   1.774  1.00 29.90 ? 155 ARG A CA  1 
ATOM   228  C C   . ARG A 1 37  ? 20.903 1.993   2.981  1.00 29.15 ? 155 ARG A C   1 
ATOM   229  O O   . ARG A 1 37  ? 20.572 0.852   3.299  1.00 28.95 ? 155 ARG A O   1 
ATOM   230  C CB  . ARG A 1 37  ? 18.959 3.335   2.193  1.00 30.33 ? 155 ARG A CB  1 
ATOM   231  C CG  . ARG A 1 37  ? 18.149 3.901   1.050  1.00 32.20 ? 155 ARG A CG  1 
ATOM   232  C CD  . ARG A 1 37  ? 16.758 4.347   1.453  1.00 35.15 ? 155 ARG A CD  1 
ATOM   233  N NE  . ARG A 1 37  ? 16.786 5.323   2.538  1.00 37.40 ? 155 ARG A NE  1 
ATOM   234  C CZ  . ARG A 1 37  ? 15.715 5.964   2.983  1.00 38.95 ? 155 ARG A CZ  1 
ATOM   235  N NH1 . ARG A 1 37  ? 14.525 5.725   2.436  1.00 39.28 ? 155 ARG A NH1 1 
ATOM   236  N NH2 . ARG A 1 37  ? 15.827 6.842   3.974  1.00 39.32 ? 155 ARG A NH2 1 
ATOM   237  N N   . GLU A 1 38  ? 21.814 2.700   3.644  1.00 28.27 ? 156 GLU A N   1 
ATOM   238  C CA  . GLU A 1 38  ? 22.452 2.211   4.857  1.00 27.47 ? 156 GLU A CA  1 
ATOM   239  C C   . GLU A 1 38  ? 21.452 2.181   6.005  1.00 26.28 ? 156 GLU A C   1 
ATOM   240  O O   . GLU A 1 38  ? 20.561 3.025   6.079  1.00 26.02 ? 156 GLU A O   1 
ATOM   241  C CB  . GLU A 1 38  ? 23.617 3.126   5.245  1.00 27.95 ? 156 GLU A CB  1 
ATOM   242  C CG  . GLU A 1 38  ? 24.790 3.101   4.284  1.00 30.01 ? 156 GLU A CG  1 
ATOM   243  C CD  . GLU A 1 38  ? 25.543 1.784   4.325  1.00 32.83 ? 156 GLU A CD  1 
ATOM   244  O OE1 . GLU A 1 38  ? 26.203 1.500   5.349  1.00 34.01 ? 156 GLU A OE1 1 
ATOM   245  O OE2 . GLU A 1 38  ? 25.466 1.025   3.338  1.00 34.86 ? 156 GLU A OE2 1 
ATOM   246  N N   . LEU A 1 39  ? 21.607 1.215   6.905  1.00 25.02 ? 157 LEU A N   1 
ATOM   247  C CA  . LEU A 1 39  ? 20.780 1.144   8.103  1.00 23.74 ? 157 LEU A CA  1 
ATOM   248  C C   . LEU A 1 39  ? 21.403 1.991   9.200  1.00 23.30 ? 157 LEU A C   1 
ATOM   249  O O   . LEU A 1 39  ? 20.738 2.377   10.156 1.00 22.92 ? 157 LEU A O   1 
ATOM   250  C CB  . LEU A 1 39  ? 20.658 -0.295  8.592  1.00 23.79 ? 157 LEU A CB  1 
ATOM   251  C CG  . LEU A 1 39  ? 19.878 -1.264  7.716  1.00 22.90 ? 157 LEU A CG  1 
ATOM   252  C CD1 . LEU A 1 39  ? 19.731 -2.592  8.446  1.00 24.16 ? 157 LEU A CD1 1 
ATOM   253  C CD2 . LEU A 1 39  ? 18.523 -0.683  7.382  1.00 23.61 ? 157 LEU A CD2 1 
ATOM   254  N N   . ASP A 1 40  ? 22.696 2.262   9.065  1.00 22.79 ? 158 ASP A N   1 
ATOM   255  C CA  . ASP A 1 40  ? 23.409 3.066   10.047 1.00 22.10 ? 158 ASP A CA  1 
ATOM   256  C C   . ASP A 1 40  ? 23.363 4.537   9.678  1.00 21.41 ? 158 ASP A C   1 
ATOM   257  O O   . ASP A 1 40  ? 24.391 5.147   9.379  1.00 21.76 ? 158 ASP A O   1 
ATOM   258  C CB  . ASP A 1 40  ? 24.854 2.592   10.186 1.00 22.64 ? 158 ASP A CB  1 
ATOM   259  C CG  . ASP A 1 40  ? 24.960 1.259   10.911 1.00 24.08 ? 158 ASP A CG  1 
ATOM   260  O OD1 . ASP A 1 40  ? 24.155 1.017   11.844 1.00 25.87 ? 158 ASP A OD1 1 
ATOM   261  O OD2 . ASP A 1 40  ? 25.817 0.395   10.624 1.00 26.00 ? 158 ASP A OD2 1 
ATOM   262  N N   . ILE A 1 41  ? 22.155 5.091   9.682  1.00 20.09 ? 159 ILE A N   1 
ATOM   263  C CA  . ILE A 1 41  ? 21.938 6.494   9.380  1.00 19.28 ? 159 ILE A CA  1 
ATOM   264  C C   . ILE A 1 41  ? 21.795 7.275   10.674 1.00 18.08 ? 159 ILE A C   1 
ATOM   265  O O   . ILE A 1 41  ? 21.073 6.876   11.580 1.00 17.49 ? 159 ILE A O   1 
ATOM   266  C CB  . ILE A 1 41  ? 20.688 6.682   8.504  1.00 19.93 ? 159 ILE A CB  1 
ATOM   267  C CG1 . ILE A 1 41  ? 19.521 5.844   9.028  1.00 20.91 ? 159 ILE A CG1 1 
ATOM   268  C CG2 . ILE A 1 41  ? 20.996 6.303   7.060  1.00 21.06 ? 159 ILE A CG2 1 
ATOM   269  C CD1 . ILE A 1 41  ? 19.319 4.556   8.278  1.00 25.27 ? 159 ILE A CD1 1 
ATOM   270  N N   . TYR A 1 42  ? 22.500 8.384   10.757 1.00 16.86 ? 160 TYR A N   1 
ATOM   271  C CA  . TYR A 1 42  ? 22.495 9.205   11.958 1.00 16.84 ? 160 TYR A CA  1 
ATOM   272  C C   . TYR A 1 42  ? 21.377 10.249  11.979 1.00 16.50 ? 160 TYR A C   1 
ATOM   273  O O   . TYR A 1 42  ? 21.040 10.821  10.946 1.00 16.48 ? 160 TYR A O   1 
ATOM   274  C CB  . TYR A 1 42  ? 23.831 9.935   12.068 1.00 16.89 ? 160 TYR A CB  1 
ATOM   275  C CG  . TYR A 1 42  ? 25.010 9.064   12.450 1.00 17.94 ? 160 TYR A CG  1 
ATOM   276  C CD1 . TYR A 1 42  ? 25.109 8.522   13.722 1.00 19.18 ? 160 TYR A CD1 1 
ATOM   277  C CD2 . TYR A 1 42  ? 26.042 8.816   11.547 1.00 21.22 ? 160 TYR A CD2 1 
ATOM   278  C CE1 . TYR A 1 42  ? 26.198 7.740   14.093 1.00 19.71 ? 160 TYR A CE1 1 
ATOM   279  C CE2 . TYR A 1 42  ? 27.142 8.037   11.909 1.00 22.80 ? 160 TYR A CE2 1 
ATOM   280  C CZ  . TYR A 1 42  ? 27.209 7.507   13.192 1.00 22.08 ? 160 TYR A CZ  1 
ATOM   281  O OH  . TYR A 1 42  ? 28.286 6.735   13.574 1.00 23.30 ? 160 TYR A OH  1 
ATOM   282  N N   . ASN A 1 43  ? 20.799 10.483  13.158 1.00 16.23 ? 161 ASN A N   1 
ATOM   283  C CA  . ASN A 1 43  ? 19.926 11.640  13.362 1.00 16.31 ? 161 ASN A CA  1 
ATOM   284  C C   . ASN A 1 43  ? 20.830 12.791  13.831 1.00 16.96 ? 161 ASN A C   1 
ATOM   285  O O   . ASN A 1 43  ? 22.054 12.661  13.799 1.00 16.32 ? 161 ASN A O   1 
ATOM   286  C CB  . ASN A 1 43  ? 18.797 11.339  14.373 1.00 16.19 ? 161 ASN A CB  1 
ATOM   287  C CG  . ASN A 1 43  ? 19.325 10.999  15.763 1.00 15.06 ? 161 ASN A CG  1 
ATOM   288  O OD1 . ASN A 1 43  ? 20.495 11.196  16.045 1.00 13.15 ? 161 ASN A OD1 1 
ATOM   289  N ND2 . ASN A 1 43  ? 18.452 10.487  16.634 1.00 14.28 ? 161 ASN A ND2 1 
ATOM   290  N N   . ASN A 1 44  ? 20.260 13.911  14.270 1.00 17.48 ? 162 ASN A N   1 
ATOM   291  C CA  . ASN A 1 44  ? 21.104 15.045  14.655 1.00 18.53 ? 162 ASN A CA  1 
ATOM   292  C C   . ASN A 1 44  ? 21.778 14.902  15.999 1.00 18.49 ? 162 ASN A C   1 
ATOM   293  O O   . ASN A 1 44  ? 22.580 15.750  16.397 1.00 19.37 ? 162 ASN A O   1 
ATOM   294  C CB  . ASN A 1 44  ? 20.341 16.359  14.577 1.00 18.99 ? 162 ASN A CB  1 
ATOM   295  C CG  . ASN A 1 44  ? 20.234 16.851  13.183 1.00 20.84 ? 162 ASN A CG  1 
ATOM   296  O OD1 . ASN A 1 44  ? 19.534 16.260  12.362 1.00 24.15 ? 162 ASN A OD1 1 
ATOM   297  N ND2 . ASN A 1 44  ? 20.955 17.912  12.876 1.00 22.03 ? 162 ASN A ND2 1 
ATOM   298  N N   . LEU A 1 45  ? 21.467 13.811  16.679 1.00 18.08 ? 163 LEU A N   1 
ATOM   299  C CA  . LEU A 1 45  ? 22.081 13.491  17.962 1.00 17.73 ? 163 LEU A CA  1 
ATOM   300  C C   . LEU A 1 45  ? 23.191 12.482  17.763 1.00 16.98 ? 163 LEU A C   1 
ATOM   301  O O   . LEU A 1 45  ? 23.794 12.004  18.722 1.00 17.30 ? 163 LEU A O   1 
ATOM   302  C CB  . LEU A 1 45  ? 21.024 12.932  18.914 1.00 17.68 ? 163 LEU A CB  1 
ATOM   303  C CG  . LEU A 1 45  ? 20.010 13.984  19.354 1.00 18.06 ? 163 LEU A CG  1 
ATOM   304  C CD1 . LEU A 1 45  ? 18.869 13.350  20.142 1.00 18.34 ? 163 LEU A CD1 1 
ATOM   305  C CD2 . LEU A 1 45  ? 20.717 15.049  20.183 1.00 17.95 ? 163 LEU A CD2 1 
ATOM   306  N N   . ARG A 1 46  ? 23.473 12.181  16.504 1.00 16.65 ? 164 ARG A N   1 
ATOM   307  C CA  . ARG A 1 46  ? 24.469 11.176  16.138 1.00 15.93 ? 164 ARG A CA  1 
ATOM   308  C C   . ARG A 1 46  ? 24.139 9.782   16.682 1.00 15.28 ? 164 ARG A C   1 
ATOM   309  O O   . ARG A 1 46  ? 25.025 9.052   17.155 1.00 15.08 ? 164 ARG A O   1 
ATOM   310  C CB  . ARG A 1 46  ? 25.889 11.602  16.532 1.00 16.41 ? 164 ARG A CB  1 
ATOM   311  C CG  . ARG A 1 46  ? 26.935 10.771  15.830 1.00 17.84 ? 164 ARG A CG  1 
ATOM   312  C CD  . ARG A 1 46  ? 28.353 11.182  16.078 1.00 22.08 ? 164 ARG A CD  1 
ATOM   313  N NE  . ARG A 1 46  ? 28.687 12.439  15.422 1.00 23.71 ? 164 ARG A NE  1 
ATOM   314  C CZ  . ARG A 1 46  ? 29.739 13.167  15.742 1.00 24.53 ? 164 ARG A CZ  1 
ATOM   315  N NH1 . ARG A 1 46  ? 30.550 12.749  16.702 1.00 25.25 ? 164 ARG A NH1 1 
ATOM   316  N NH2 . ARG A 1 46  ? 29.988 14.304  15.109 1.00 25.82 ? 164 ARG A NH2 1 
ATOM   317  N N   . GLN A 1 47  ? 22.860 9.424   16.607 1.00 13.96 ? 165 GLN A N   1 
ATOM   318  C CA  . GLN A 1 47  ? 22.394 8.092   16.963 1.00 13.49 ? 165 GLN A CA  1 
ATOM   319  C C   . GLN A 1 47  ? 21.904 7.374   15.716 1.00 12.98 ? 165 GLN A C   1 
ATOM   320  O O   . GLN A 1 47  ? 21.183 7.953   14.904 1.00 12.99 ? 165 GLN A O   1 
ATOM   321  C CB  . GLN A 1 47  ? 21.210 8.174   17.938 1.00 13.71 ? 165 GLN A CB  1 
ATOM   322  C CG  . GLN A 1 47  ? 21.439 9.048   19.154 1.00 13.58 ? 165 GLN A CG  1 
ATOM   323  C CD  . GLN A 1 47  ? 20.169 9.272   19.949 1.00 13.58 ? 165 GLN A CD  1 
ATOM   324  O OE1 . GLN A 1 47  ? 19.118 9.567   19.380 1.00 15.18 ? 165 GLN A OE1 1 
ATOM   325  N NE2 . GLN A 1 47  ? 20.259 9.127   21.263 1.00 14.74 ? 165 GLN A NE2 1 
ATOM   326  N N   . THR A 1 48  ? 22.290 6.115   15.565 1.00 12.27 ? 166 THR A N   1 
ATOM   327  C CA  . THR A 1 48  ? 21.708 5.267   14.540 1.00 11.74 ? 166 THR A CA  1 
ATOM   328  C C   . THR A 1 48  ? 20.495 4.602   15.157 1.00 11.33 ? 166 THR A C   1 
ATOM   329  O O   . THR A 1 48  ? 20.302 4.660   16.374 1.00 11.34 ? 166 THR A O   1 
ATOM   330  C CB  . THR A 1 48  ? 22.689 4.174   14.103 1.00 11.75 ? 166 THR A CB  1 
ATOM   331  O OG1 . THR A 1 48  ? 22.977 3.311   15.216 1.00 12.05 ? 166 THR A OG1 1 
ATOM   332  C CG2 . THR A 1 48  ? 24.054 4.766   13.726 1.00 12.04 ? 166 THR A CG2 1 
ATOM   333  N N   . PRO A 1 49  ? 19.660 3.989   14.329 1.00 10.65 ? 167 PRO A N   1 
ATOM   334  C CA  . PRO A 1 49  ? 18.538 3.191   14.836 1.00 10.32 ? 167 PRO A CA  1 
ATOM   335  C C   . PRO A 1 49  ? 18.974 2.101   15.830 1.00 10.25 ? 167 PRO A C   1 
ATOM   336  O O   . PRO A 1 49  ? 18.247 1.853   16.794 1.00 9.36  ? 167 PRO A O   1 
ATOM   337  C CB  . PRO A 1 49  ? 17.948 2.583   13.567 1.00 10.89 ? 167 PRO A CB  1 
ATOM   338  C CG  . PRO A 1 49  ? 18.218 3.620   12.528 1.00 10.71 ? 167 PRO A CG  1 
ATOM   339  C CD  . PRO A 1 49  ? 19.642 4.102   12.858 1.00 10.72 ? 167 PRO A CD  1 
ATOM   340  N N   . LEU A 1 50  ? 20.156 1.500   15.635 1.00 9.34  ? 168 LEU A N   1 
ATOM   341  C CA  . LEU A 1 50  ? 20.632 0.470   16.554 1.00 9.46  ? 168 LEU A CA  1 
ATOM   342  C C   . LEU A 1 50  ? 20.935 1.055   17.938 1.00 9.67  ? 168 LEU A C   1 
ATOM   343  O O   . LEU A 1 50  ? 20.592 0.452   18.962 1.00 9.47  ? 168 LEU A O   1 
ATOM   344  C CB  . LEU A 1 50  ? 21.863 -0.264  15.989 1.00 9.47  ? 168 LEU A CB  1 
ATOM   345  C CG  . LEU A 1 50  ? 22.484 -1.387  16.841 1.00 9.85  ? 168 LEU A CG  1 
ATOM   346  C CD1 . LEU A 1 50  ? 21.452 -2.485  17.161 1.00 10.96 ? 168 LEU A CD1 1 
ATOM   347  C CD2 . LEU A 1 50  ? 23.678 -1.973  16.139 1.00 9.52  ? 168 LEU A CD2 1 
ATOM   348  N N   . HIS A 1 51  ? 21.584 2.216   17.967 1.00 9.81  ? 169 HIS A N   1 
ATOM   349  C CA  . HIS A 1 51  ? 21.850 2.894   19.228 1.00 10.69 ? 169 HIS A CA  1 
ATOM   350  C C   . HIS A 1 51  ? 20.525 3.059   19.956 1.00 10.73 ? 169 HIS A C   1 
ATOM   351  O O   . HIS A 1 51  ? 20.433 2.827   21.156 1.00 10.57 ? 169 HIS A O   1 
ATOM   352  C CB  . HIS A 1 51  ? 22.436 4.293   19.000 1.00 10.78 ? 169 HIS A CB  1 
ATOM   353  C CG  . HIS A 1 51  ? 23.822 4.303   18.421 1.00 12.30 ? 169 HIS A CG  1 
ATOM   354  N ND1 . HIS A 1 51  ? 24.834 3.479   18.868 1.00 16.39 ? 169 HIS A ND1 1 
ATOM   355  C CD2 . HIS A 1 51  ? 24.369 5.076   17.453 1.00 13.01 ? 169 HIS A CD2 1 
ATOM   356  C CE1 . HIS A 1 51  ? 25.937 3.729   18.185 1.00 13.62 ? 169 HIS A CE1 1 
ATOM   357  N NE2 . HIS A 1 51  ? 25.681 4.690   17.317 1.00 15.57 ? 169 HIS A NE2 1 
ATOM   358  N N   . LEU A 1 52  ? 19.506 3.503   19.220 1.00 10.93 ? 170 LEU A N   1 
ATOM   359  C CA  . LEU A 1 52  ? 18.191 3.751   19.804 1.00 11.11 ? 170 LEU A CA  1 
ATOM   360  C C   . LEU A 1 52  ? 17.516 2.481   20.317 1.00 11.15 ? 170 LEU A C   1 
ATOM   361  O O   . LEU A 1 52  ? 16.811 2.505   21.333 1.00 11.05 ? 170 LEU A O   1 
ATOM   362  C CB  . LEU A 1 52  ? 17.290 4.484   18.809 1.00 11.71 ? 170 LEU A CB  1 
ATOM   363  C CG  . LEU A 1 52  ? 17.631 5.969   18.665 1.00 12.43 ? 170 LEU A CG  1 
ATOM   364  C CD1 . LEU A 1 52  ? 16.716 6.656   17.634 1.00 14.28 ? 170 LEU A CD1 1 
ATOM   365  C CD2 . LEU A 1 52  ? 17.545 6.655   20.018 1.00 14.70 ? 170 LEU A CD2 1 
ATOM   366  N N   . ALA A 1 53  ? 17.737 1.374   19.621 1.00 10.87 ? 171 ALA A N   1 
ATOM   367  C CA  . ALA A 1 53  ? 17.175 0.097   20.039 1.00 11.54 ? 171 ALA A CA  1 
ATOM   368  C C   . ALA A 1 53  ? 17.744 -0.327  21.386 1.00 12.29 ? 171 ALA A C   1 
ATOM   369  O O   . ALA A 1 53  ? 17.029 -0.886  22.211 1.00 12.47 ? 171 ALA A O   1 
ATOM   370  C CB  . ALA A 1 53  ? 17.430 -0.965  18.998 1.00 11.41 ? 171 ALA A CB  1 
ATOM   371  N N   . VAL A 1 54  ? 19.030 -0.064  21.601 1.00 12.53 ? 172 VAL A N   1 
ATOM   372  C CA  . VAL A 1 54  ? 19.675 -0.406  22.865 1.00 13.94 ? 172 VAL A CA  1 
ATOM   373  C C   . VAL A 1 54  ? 19.220 0.551   23.965 1.00 14.79 ? 172 VAL A C   1 
ATOM   374  O O   . VAL A 1 54  ? 18.905 0.135   25.088 1.00 15.02 ? 172 VAL A O   1 
ATOM   375  C CB  . VAL A 1 54  ? 21.199 -0.335  22.748 1.00 14.08 ? 172 VAL A CB  1 
ATOM   376  C CG1 . VAL A 1 54  ? 21.848 -0.514  24.119 1.00 14.51 ? 172 VAL A CG1 1 
ATOM   377  C CG2 . VAL A 1 54  ? 21.701 -1.370  21.760 1.00 14.02 ? 172 VAL A CG2 1 
ATOM   378  N N   . ILE A 1 55  ? 19.166 1.833   23.631 1.00 15.88 ? 173 ILE A N   1 
ATOM   379  C CA  . ILE A 1 55  ? 18.738 2.853   24.578 1.00 17.35 ? 173 ILE A CA  1 
ATOM   380  C C   . ILE A 1 55  ? 17.278 2.641   25.016 1.00 17.60 ? 173 ILE A C   1 
ATOM   381  O O   . ILE A 1 55  ? 16.927 2.906   26.160 1.00 17.93 ? 173 ILE A O   1 
ATOM   382  C CB  . ILE A 1 55  ? 18.923 4.258   23.959 1.00 17.28 ? 173 ILE A CB  1 
ATOM   383  C CG1 . ILE A 1 55  ? 20.398 4.675   23.987 1.00 18.52 ? 173 ILE A CG1 1 
ATOM   384  C CG2 . ILE A 1 55  ? 18.049 5.283   24.673 1.00 18.61 ? 173 ILE A CG2 1 
ATOM   385  C CD1 . ILE A 1 55  ? 20.766 5.697   22.917 1.00 20.02 ? 173 ILE A CD1 1 
ATOM   386  N N   . THR A 1 56  ? 16.439 2.159   24.105 1.00 18.03 ? 174 THR A N   1 
ATOM   387  C CA  . THR A 1 56  ? 15.022 1.920   24.408 1.00 18.76 ? 174 THR A CA  1 
ATOM   388  C C   . THR A 1 56  ? 14.831 0.572   25.117 1.00 18.61 ? 174 THR A C   1 
ATOM   389  O O   . THR A 1 56  ? 13.763 0.294   25.653 1.00 18.39 ? 174 THR A O   1 
ATOM   390  C CB  . THR A 1 56  ? 14.158 1.937   23.112 1.00 18.31 ? 174 THR A CB  1 
ATOM   391  O OG1 . THR A 1 56  ? 14.370 3.151   22.382 1.00 20.05 ? 174 THR A OG1 1 
ATOM   392  C CG2 . THR A 1 56  ? 12.668 2.011   23.454 1.00 20.12 ? 174 THR A CG2 1 
ATOM   393  N N   . THR A 1 57  ? 15.888 -0.239  25.128 1.00 18.58 ? 175 THR A N   1 
ATOM   394  C CA  . THR A 1 57  ? 15.860 -1.619  25.642 1.00 18.91 ? 175 THR A CA  1 
ATOM   395  C C   . THR A 1 57  ? 14.914 -2.542  24.864 1.00 18.02 ? 175 THR A C   1 
ATOM   396  O O   . THR A 1 57  ? 13.974 -3.099  25.415 1.00 18.91 ? 175 THR A O   1 
ATOM   397  C CB  . THR A 1 57  ? 15.586 -1.686  27.166 1.00 19.44 ? 175 THR A CB  1 
ATOM   398  O OG1 . THR A 1 57  ? 14.238 -1.274  27.451 1.00 21.18 ? 175 THR A OG1 1 
ATOM   399  C CG2 . THR A 1 57  ? 16.445 -0.677  27.902 1.00 21.00 ? 175 THR A CG2 1 
ATOM   400  N N   . LEU A 1 58  ? 15.193 -2.708  23.580 1.00 17.03 ? 176 LEU A N   1 
ATOM   401  C CA  . LEU A 1 58  ? 14.396 -3.565  22.709 1.00 15.97 ? 176 LEU A CA  1 
ATOM   402  C C   . LEU A 1 58  ? 15.273 -4.645  22.089 1.00 15.32 ? 176 LEU A C   1 
ATOM   403  O O   . LEU A 1 58  ? 15.702 -4.519  20.938 1.00 15.01 ? 176 LEU A O   1 
ATOM   404  C CB  . LEU A 1 58  ? 13.770 -2.722  21.602 1.00 15.59 ? 176 LEU A CB  1 
ATOM   405  C CG  . LEU A 1 58  ? 12.773 -1.657  22.050 1.00 16.20 ? 176 LEU A CG  1 
ATOM   406  C CD1 . LEU A 1 58  ? 12.479 -0.681  20.907 1.00 15.65 ? 176 LEU A CD1 1 
ATOM   407  C CD2 . LEU A 1 58  ? 11.488 -2.320  22.550 1.00 16.18 ? 176 LEU A CD2 1 
ATOM   408  N N   . PRO A 1 59  ? 15.535 -5.711  22.839 1.00 15.17 ? 177 PRO A N   1 
ATOM   409  C CA  . PRO A 1 59  ? 16.418 -6.785  22.366 1.00 14.63 ? 177 PRO A CA  1 
ATOM   410  C C   . PRO A 1 59  ? 15.993 -7.385  21.014 1.00 14.33 ? 177 PRO A C   1 
ATOM   411  O O   . PRO A 1 59  ? 16.852 -7.663  20.171 1.00 14.10 ? 177 PRO A O   1 
ATOM   412  C CB  . PRO A 1 59  ? 16.337 -7.823  23.490 1.00 15.81 ? 177 PRO A CB  1 
ATOM   413  C CG  . PRO A 1 59  ? 15.076 -7.472  24.235 1.00 16.55 ? 177 PRO A CG  1 
ATOM   414  C CD  . PRO A 1 59  ? 15.005 -5.983  24.188 1.00 15.35 ? 177 PRO A CD  1 
ATOM   415  N N   . SER A 1 60  ? 14.691 -7.548  20.781 1.00 13.42 ? 178 SER A N   1 
ATOM   416  C CA  . SER A 1 60  ? 14.239 -8.102  19.504 1.00 12.99 ? 178 SER A CA  1 
ATOM   417  C C   . SER A 1 60  ? 14.579 -7.200  18.317 1.00 12.50 ? 178 SER A C   1 
ATOM   418  O O   . SER A 1 60  ? 14.858 -7.685  17.222 1.00 12.15 ? 178 SER A O   1 
ATOM   419  C CB  . SER A 1 60  ? 12.737 -8.359  19.516 1.00 13.11 ? 178 SER A CB  1 
ATOM   420  O OG  A SER A 1 60  ? 12.415 -9.420  20.390 0.72 13.35 ? 178 SER A OG  1 
ATOM   421  O OG  B SER A 1 60  ? 12.316 -8.813  18.243 0.28 13.19 ? 178 SER A OG  1 
ATOM   422  N N   . VAL A 1 61  ? 14.526 -5.889  18.534 1.00 12.11 ? 179 VAL A N   1 
ATOM   423  C CA  . VAL A 1 61  ? 14.869 -4.935  17.489 1.00 12.06 ? 179 VAL A CA  1 
ATOM   424  C C   . VAL A 1 61  ? 16.378 -4.940  17.241 1.00 12.49 ? 179 VAL A C   1 
ATOM   425  O O   . VAL A 1 61  ? 16.838 -4.865  16.091 1.00 11.22 ? 179 VAL A O   1 
ATOM   426  C CB  . VAL A 1 61  ? 14.363 -3.531  17.834 1.00 12.35 ? 179 VAL A CB  1 
ATOM   427  C CG1 A VAL A 1 61  ? 14.647 -2.555  16.699 0.50 12.35 ? 179 VAL A CG1 1 
ATOM   428  C CG1 B VAL A 1 61  ? 14.950 -2.495  16.885 0.50 12.14 ? 179 VAL A CG1 1 
ATOM   429  C CG2 A VAL A 1 61  ? 12.864 -3.579  18.143 0.50 11.95 ? 179 VAL A CG2 1 
ATOM   430  C CG2 B VAL A 1 61  ? 12.837 -3.502  17.793 0.50 12.08 ? 179 VAL A CG2 1 
ATOM   431  N N   . VAL A 1 62  ? 17.142 -5.043  18.323 1.00 12.45 ? 180 VAL A N   1 
ATOM   432  C CA  . VAL A 1 62  ? 18.592 -5.122  18.220 1.00 12.90 ? 180 VAL A CA  1 
ATOM   433  C C   . VAL A 1 62  ? 18.977 -6.293  17.309 1.00 13.14 ? 180 VAL A C   1 
ATOM   434  O O   . VAL A 1 62  ? 19.798 -6.152  16.404 1.00 13.22 ? 180 VAL A O   1 
ATOM   435  C CB  . VAL A 1 62  ? 19.238 -5.333  19.601 1.00 12.80 ? 180 VAL A CB  1 
ATOM   436  C CG1 . VAL A 1 62  ? 20.720 -5.710  19.454 1.00 12.92 ? 180 VAL A CG1 1 
ATOM   437  C CG2 . VAL A 1 62  ? 19.072 -4.084  20.488 1.00 12.78 ? 180 VAL A CG2 1 
ATOM   438  N N   . ARG A 1 63  ? 18.375 -7.449  17.560 1.00 13.74 ? 181 ARG A N   1 
ATOM   439  C CA  . ARG A 1 63  ? 18.631 -8.659  16.777 1.00 13.82 ? 181 ARG A CA  1 
ATOM   440  C C   . ARG A 1 63  ? 18.310 -8.487  15.289 1.00 13.58 ? 181 ARG A C   1 
ATOM   441  O O   . ARG A 1 63  ? 19.083 -8.902  14.422 1.00 13.39 ? 181 ARG A O   1 
ATOM   442  C CB  . ARG A 1 63  ? 17.804 -9.833  17.326 1.00 14.51 ? 181 ARG A CB  1 
ATOM   443  C CG  . ARG A 1 63  ? 18.294 -10.406 18.665 1.00 16.84 ? 181 ARG A CG  1 
ATOM   444  C CD  . ARG A 1 63  ? 17.612 -11.724 19.075 1.00 20.98 ? 181 ARG A CD  1 
ATOM   445  N NE  . ARG A 1 63  ? 17.951 -12.108 20.452 1.00 25.13 ? 181 ARG A NE  1 
ATOM   446  C CZ  . ARG A 1 63  ? 18.974 -12.891 20.779 1.00 26.84 ? 181 ARG A CZ  1 
ATOM   447  N NH1 . ARG A 1 63  ? 19.762 -13.377 19.832 1.00 27.88 ? 181 ARG A NH1 1 
ATOM   448  N NH2 . ARG A 1 63  ? 19.217 -13.184 22.054 1.00 28.14 ? 181 ARG A NH2 1 
ATOM   449  N N   . LEU A 1 64  ? 17.148 -7.912  15.002 1.00 12.74 ? 182 LEU A N   1 
ATOM   450  C CA  . LEU A 1 64  ? 16.718 -7.679  13.622 1.00 12.90 ? 182 LEU A CA  1 
ATOM   451  C C   . LEU A 1 64  ? 17.706 -6.772  12.897 1.00 12.33 ? 182 LEU A C   1 
ATOM   452  O O   . LEU A 1 64  ? 18.152 -7.081  11.791 1.00 12.11 ? 182 LEU A O   1 
ATOM   453  C CB  A LEU A 1 64  ? 15.318 -7.052  13.586 0.50 12.91 ? 182 LEU A CB  1 
ATOM   454  C CB  B LEU A 1 64  ? 15.315 -7.052  13.616 0.50 13.01 ? 182 LEU A CB  1 
ATOM   455  C CG  A LEU A 1 64  ? 14.716 -6.709  12.213 0.50 13.45 ? 182 LEU A CG  1 
ATOM   456  C CG  B LEU A 1 64  ? 14.549 -6.841  12.300 0.50 13.89 ? 182 LEU A CG  1 
ATOM   457  C CD1 A LEU A 1 64  ? 13.250 -6.322  12.353 0.50 13.18 ? 182 LEU A CD1 1 
ATOM   458  C CD1 B LEU A 1 64  ? 14.950 -5.545  11.615 0.50 14.93 ? 182 LEU A CD1 1 
ATOM   459  C CD2 A LEU A 1 64  ? 15.494 -5.597  11.517 0.50 14.52 ? 182 LEU A CD2 1 
ATOM   460  C CD2 B LEU A 1 64  ? 14.701 -8.027  11.369 0.50 14.37 ? 182 LEU A CD2 1 
ATOM   461  N N   . LEU A 1 65  ? 18.044 -5.656  13.531 1.00 11.62 ? 183 LEU A N   1 
ATOM   462  C CA  . LEU A 1 65  ? 18.928 -4.671  12.925 1.00 11.97 ? 183 LEU A CA  1 
ATOM   463  C C   . LEU A 1 65  ? 20.331 -5.214  12.686 1.00 12.24 ? 183 LEU A C   1 
ATOM   464  O O   . LEU A 1 65  ? 20.900 -5.020  11.617 1.00 12.13 ? 183 LEU A O   1 
ATOM   465  C CB  . LEU A 1 65  ? 18.993 -3.389  13.774 1.00 11.60 ? 183 LEU A CB  1 
ATOM   466  C CG  . LEU A 1 65  ? 17.733 -2.507  13.786 1.00 12.03 ? 183 LEU A CG  1 
ATOM   467  C CD1 . LEU A 1 65  ? 17.926 -1.337  14.738 1.00 12.00 ? 183 LEU A CD1 1 
ATOM   468  C CD2 . LEU A 1 65  ? 17.399 -2.003  12.392 1.00 12.89 ? 183 LEU A CD2 1 
ATOM   469  N N   . VAL A 1 66  ? 20.886 -5.893  13.683 1.00 12.38 ? 184 VAL A N   1 
ATOM   470  C CA  . VAL A 1 66  ? 22.236 -6.441  13.542 1.00 13.36 ? 184 VAL A CA  1 
ATOM   471  C C   . VAL A 1 66  ? 22.287 -7.522  12.459 1.00 14.17 ? 184 VAL A C   1 
ATOM   472  O O   . VAL A 1 66  ? 23.168 -7.508  11.597 1.00 14.76 ? 184 VAL A O   1 
ATOM   473  C CB  . VAL A 1 66  ? 22.768 -6.964  14.872 1.00 13.23 ? 184 VAL A CB  1 
ATOM   474  C CG1 . VAL A 1 66  ? 24.148 -7.625  14.675 1.00 12.92 ? 184 VAL A CG1 1 
ATOM   475  C CG2 . VAL A 1 66  ? 22.872 -5.793  15.866 1.00 12.94 ? 184 VAL A CG2 1 
ATOM   476  N N   . THR A 1 67  ? 21.307 -8.422  12.465 1.00 15.02 ? 185 THR A N   1 
ATOM   477  C CA  . THR A 1 67  ? 21.268 -9.477  11.466 1.00 15.94 ? 185 THR A CA  1 
ATOM   478  C C   . THR A 1 67  ? 21.087 -8.891  10.051 1.00 16.38 ? 185 THR A C   1 
ATOM   479  O O   . THR A 1 67  ? 21.567 -9.462  9.063  1.00 16.54 ? 185 THR A O   1 
ATOM   480  C CB  . THR A 1 67  ? 20.177 -10.531 11.806 1.00 15.80 ? 185 THR A CB  1 
ATOM   481  O OG1 . THR A 1 67  ? 18.911 -9.887  11.958 1.00 19.72 ? 185 THR A OG1 1 
ATOM   482  C CG2 . THR A 1 67  ? 20.415 -11.126 13.185 1.00 15.11 ? 185 THR A CG2 1 
ATOM   483  N N   . ALA A 1 68  ? 20.433 -7.737  9.958  1.00 16.72 ? 186 ALA A N   1 
ATOM   484  C CA  . ALA A 1 68  ? 20.230 -7.078  8.663  1.00 17.53 ? 186 ALA A CA  1 
ATOM   485  C C   . ALA A 1 68  ? 21.448 -6.287  8.154  1.00 17.70 ? 186 ALA A C   1 
ATOM   486  O O   . ALA A 1 68  ? 21.435 -5.780  7.031  1.00 18.25 ? 186 ALA A O   1 
ATOM   487  C CB  . ALA A 1 68  ? 18.984 -6.183  8.696  1.00 17.20 ? 186 ALA A CB  1 
ATOM   488  N N   . GLY A 1 69  ? 22.483 -6.154  8.983  1.00 17.86 ? 187 GLY A N   1 
ATOM   489  C CA  . GLY A 1 69  ? 23.702 -5.484  8.549  1.00 17.35 ? 187 GLY A CA  1 
ATOM   490  C C   . GLY A 1 69  ? 24.082 -4.196  9.266  1.00 17.46 ? 187 GLY A C   1 
ATOM   491  O O   . GLY A 1 69  ? 25.072 -3.540  8.895  1.00 16.68 ? 187 GLY A O   1 
ATOM   492  N N   . ALA A 1 70  ? 23.291 -3.793  10.258 1.00 17.05 ? 188 ALA A N   1 
ATOM   493  C CA  . ALA A 1 70  ? 23.652 -2.608  11.048 1.00 17.40 ? 188 ALA A CA  1 
ATOM   494  C C   . ALA A 1 70  ? 24.909 -2.922  11.857 1.00 17.80 ? 188 ALA A C   1 
ATOM   495  O O   . ALA A 1 70  ? 25.004 -3.980  12.474 1.00 18.19 ? 188 ALA A O   1 
ATOM   496  C CB  . ALA A 1 70  ? 22.517 -2.199  11.968 1.00 17.02 ? 188 ALA A CB  1 
ATOM   497  N N   . SER A 1 71  ? 25.852 -1.988  11.880 1.00 18.39 ? 189 SER A N   1 
ATOM   498  C CA  . SER A 1 71  ? 27.142 -2.218  12.531 1.00 18.66 ? 189 SER A CA  1 
ATOM   499  C C   . SER A 1 71  ? 27.134 -1.973  14.034 1.00 18.34 ? 189 SER A C   1 
ATOM   500  O O   . SER A 1 71  ? 26.750 -0.905  14.498 1.00 18.36 ? 189 SER A O   1 
ATOM   501  C CB  . SER A 1 71  ? 28.228 -1.347  11.886 1.00 19.18 ? 189 SER A CB  1 
ATOM   502  O OG  . SER A 1 71  ? 29.466 -1.481  12.580 1.00 18.97 ? 189 SER A OG  1 
ATOM   503  N N   . PRO A 1 72  ? 27.584 -2.969  14.789 1.00 18.49 ? 190 PRO A N   1 
ATOM   504  C CA  . PRO A 1 72  ? 27.736 -2.836  16.238 1.00 18.19 ? 190 PRO A CA  1 
ATOM   505  C C   . PRO A 1 72  ? 28.868 -1.868  16.596 1.00 17.60 ? 190 PRO A C   1 
ATOM   506  O O   . PRO A 1 72  ? 28.956 -1.456  17.746 1.00 17.83 ? 190 PRO A O   1 
ATOM   507  C CB  . PRO A 1 72  ? 28.111 -4.258  16.681 1.00 18.75 ? 190 PRO A CB  1 
ATOM   508  C CG  . PRO A 1 72  ? 27.725 -5.128  15.549 1.00 19.14 ? 190 PRO A CG  1 
ATOM   509  C CD  . PRO A 1 72  ? 27.962 -4.311  14.313 1.00 18.63 ? 190 PRO A CD  1 
ATOM   510  N N   . MET A 1 73  ? 29.714 -1.508  15.630 1.00 16.76 ? 191 MET A N   1 
ATOM   511  C CA  . MET A 1 73  ? 30.824 -0.593  15.911 1.00 16.15 ? 191 MET A CA  1 
ATOM   512  C C   . MET A 1 73  ? 30.565 0.887   15.558 1.00 15.44 ? 191 MET A C   1 
ATOM   513  O O   . MET A 1 73  ? 31.427 1.729   15.791 1.00 15.38 ? 191 MET A O   1 
ATOM   514  C CB  . MET A 1 73  ? 32.124 -1.070  15.244 1.00 15.98 ? 191 MET A CB  1 
ATOM   515  C CG  . MET A 1 73  ? 32.608 -2.447  15.707 1.00 16.58 ? 191 MET A CG  1 
ATOM   516  S SD  . MET A 1 73  ? 33.036 -2.499  17.458 1.00 17.78 ? 191 MET A SD  1 
ATOM   517  C CE  . MET A 1 73  ? 34.529 -1.479  17.467 1.00 16.03 ? 191 MET A CE  1 
ATOM   518  N N   . ALA A 1 74  ? 29.404 1.205   14.982 1.00 14.75 ? 192 ALA A N   1 
ATOM   519  C CA  . ALA A 1 74  ? 29.086 2.608   14.685 1.00 14.26 ? 192 ALA A CA  1 
ATOM   520  C C   . ALA A 1 74  ? 29.128 3.401   15.987 1.00 14.08 ? 192 ALA A C   1 
ATOM   521  O O   . ALA A 1 74  ? 28.599 2.953   17.010 1.00 14.31 ? 192 ALA A O   1 
ATOM   522  C CB  . ALA A 1 74  ? 27.714 2.736   14.031 1.00 14.04 ? 192 ALA A CB  1 
ATOM   523  N N   . LEU A 1 75  ? 29.752 4.573   15.957 1.00 13.72 ? 193 LEU A N   1 
ATOM   524  C CA  . LEU A 1 75  ? 29.919 5.371   17.173 1.00 14.03 ? 193 LEU A CA  1 
ATOM   525  C C   . LEU A 1 75  ? 28.838 6.423   17.351 1.00 13.80 ? 193 LEU A C   1 
ATOM   526  O O   . LEU A 1 75  ? 28.428 7.055   16.389 1.00 13.96 ? 193 LEU A O   1 
ATOM   527  C CB  . LEU A 1 75  ? 31.279 6.070   17.152 1.00 13.99 ? 193 LEU A CB  1 
ATOM   528  C CG  . LEU A 1 75  ? 32.468 5.136   16.959 1.00 14.47 ? 193 LEU A CG  1 
ATOM   529  C CD1 . LEU A 1 75  ? 33.777 5.932   17.030 1.00 18.36 ? 193 LEU A CD1 1 
ATOM   530  C CD2 . LEU A 1 75  ? 32.431 4.041   18.011 1.00 15.57 ? 193 LEU A CD2 1 
ATOM   531  N N   . ASP A 1 76  ? 28.396 6.628   18.590 1.00 13.80 ? 194 ASP A N   1 
ATOM   532  C CA  . ASP A 1 76  ? 27.478 7.731   18.878 1.00 14.46 ? 194 ASP A CA  1 
ATOM   533  C C   . ASP A 1 76  ? 28.240 9.028   19.210 1.00 14.36 ? 194 ASP A C   1 
ATOM   534  O O   . ASP A 1 76  ? 29.456 9.109   18.993 1.00 13.72 ? 194 ASP A O   1 
ATOM   535  C CB  . ASP A 1 76  ? 26.460 7.352   19.959 1.00 14.50 ? 194 ASP A CB  1 
ATOM   536  C CG  . ASP A 1 76  ? 27.032 7.387   21.355 1.00 16.59 ? 194 ASP A CG  1 
ATOM   537  O OD1 . ASP A 1 76  ? 28.219 7.757   21.537 1.00 15.80 ? 194 ASP A OD1 1 
ATOM   538  O OD2 . ASP A 1 76  ? 26.338 7.074   22.349 1.00 19.07 ? 194 ASP A OD2 1 
ATOM   539  N N   . ARG A 1 77  ? 27.527 10.033  19.717 1.00 14.44 ? 195 ARG A N   1 
ATOM   540  C CA  . ARG A 1 77  ? 28.109 11.359  19.964 1.00 15.03 ? 195 ARG A CA  1 
ATOM   541  C C   . ARG A 1 77  ? 29.311 11.329  20.919 1.00 14.38 ? 195 ARG A C   1 
ATOM   542  O O   . ARG A 1 77  ? 30.236 12.150  20.815 1.00 14.51 ? 195 ARG A O   1 
ATOM   543  C CB  . ARG A 1 77  ? 27.025 12.308  20.493 1.00 15.69 ? 195 ARG A CB  1 
ATOM   544  C CG  . ARG A 1 77  ? 27.475 13.732  20.710 1.00 19.21 ? 195 ARG A CG  1 
ATOM   545  C CD  . ARG A 1 77  ? 26.485 14.557  21.536 1.00 25.34 ? 195 ARG A CD  1 
ATOM   546  N NE  . ARG A 1 77  ? 26.893 15.952  21.661 1.00 28.74 ? 195 ARG A NE  1 
ATOM   547  C CZ  . ARG A 1 77  ? 27.018 16.767  20.630 1.00 30.61 ? 195 ARG A CZ  1 
ATOM   548  N NH1 . ARG A 1 77  ? 26.760 16.319  19.407 1.00 31.86 ? 195 ARG A NH1 1 
ATOM   549  N NH2 . ARG A 1 77  ? 27.394 18.027  20.811 1.00 31.81 ? 195 ARG A NH2 1 
ATOM   550  N N   . HIS A 1 78  ? 29.291 10.383  21.844 1.00 13.85 ? 196 HIS A N   1 
ATOM   551  C CA  . HIS A 1 78  ? 30.347 10.248  22.824 1.00 14.08 ? 196 HIS A CA  1 
ATOM   552  C C   . HIS A 1 78  ? 31.267 9.073   22.505 1.00 13.48 ? 196 HIS A C   1 
ATOM   553  O O   . HIS A 1 78  ? 32.036 8.626   23.351 1.00 13.80 ? 196 HIS A O   1 
ATOM   554  C CB  . HIS A 1 78  ? 29.744 10.123  24.217 1.00 14.87 ? 196 HIS A CB  1 
ATOM   555  C CG  . HIS A 1 78  ? 28.832 11.254  24.566 1.00 17.78 ? 196 HIS A CG  1 
ATOM   556  N ND1 . HIS A 1 78  ? 27.460 11.128  24.570 1.00 22.69 ? 196 HIS A ND1 1 
ATOM   557  C CD2 . HIS A 1 78  ? 29.093 12.548  24.864 1.00 20.79 ? 196 HIS A CD2 1 
ATOM   558  C CE1 . HIS A 1 78  ? 26.916 12.291  24.887 1.00 23.19 ? 196 HIS A CE1 1 
ATOM   559  N NE2 . HIS A 1 78  ? 27.886 13.169  25.070 1.00 22.24 ? 196 HIS A NE2 1 
ATOM   560  N N   . GLY A 1 79  ? 31.192 8.589   21.273 1.00 12.89 ? 197 GLY A N   1 
ATOM   561  C CA  . GLY A 1 79  ? 32.054 7.504   20.833 1.00 12.76 ? 197 GLY A CA  1 
ATOM   562  C C   . GLY A 1 79  ? 31.667 6.144   21.404 1.00 12.32 ? 197 GLY A C   1 
ATOM   563  O O   . GLY A 1 79  ? 32.490 5.225   21.451 1.00 11.99 ? 197 GLY A O   1 
ATOM   564  N N   . GLN A 1 80  ? 30.423 6.024   21.864 1.00 11.86 ? 198 GLN A N   1 
ATOM   565  C CA  . GLN A 1 80  ? 29.916 4.746   22.399 1.00 12.08 ? 198 GLN A CA  1 
ATOM   566  C C   . GLN A 1 80  ? 29.517 3.801   21.284 1.00 11.22 ? 198 GLN A C   1 
ATOM   567  O O   . GLN A 1 80  ? 28.852 4.211   20.336 1.00 11.07 ? 198 GLN A O   1 
ATOM   568  C CB  . GLN A 1 80  ? 28.684 4.973   23.290 1.00 11.74 ? 198 GLN A CB  1 
ATOM   569  C CG  . GLN A 1 80  ? 28.898 5.925   24.468 1.00 15.80 ? 198 GLN A CG  1 
ATOM   570  C CD  . GLN A 1 80  ? 29.473 5.234   25.690 1.00 19.55 ? 198 GLN A CD  1 
ATOM   571  O OE1 . GLN A 1 80  ? 28.775 5.039   26.688 1.00 23.36 ? 198 GLN A OE1 1 
ATOM   572  N NE2 . GLN A 1 80  ? 30.738 4.859   25.616 1.00 20.47 ? 198 GLN A NE2 1 
ATOM   573  N N   . THR A 1 81  ? 29.923 2.536   21.396 1.00 11.46 ? 199 THR A N   1 
ATOM   574  C CA  . THR A 1 81  ? 29.425 1.494   20.498 1.00 11.08 ? 199 THR A CA  1 
ATOM   575  C C   . THR A 1 81  ? 28.134 0.965   21.100 1.00 10.91 ? 199 THR A C   1 
ATOM   576  O O   . THR A 1 81  ? 27.760 1.349   22.202 1.00 10.53 ? 199 THR A O   1 
ATOM   577  C CB  . THR A 1 81  ? 30.423 0.315   20.362 1.00 11.69 ? 199 THR A CB  1 
ATOM   578  O OG1 . THR A 1 81  ? 30.636 -0.296  21.651 1.00 10.36 ? 199 THR A OG1 1 
ATOM   579  C CG2 . THR A 1 81  ? 31.832 0.809   19.934 1.00 12.97 ? 199 THR A CG2 1 
ATOM   580  N N   . ALA A 1 82  ? 27.454 0.086   20.374 1.00 10.45 ? 200 ALA A N   1 
ATOM   581  C CA  . ALA A 1 82  ? 26.245 -0.550  20.884 1.00 10.64 ? 200 ALA A CA  1 
ATOM   582  C C   . ALA A 1 82  ? 26.514 -1.229  22.234 1.00 10.73 ? 200 ALA A C   1 
ATOM   583  O O   . ALA A 1 82  ? 25.695 -1.155  23.158 1.00 10.67 ? 200 ALA A O   1 
ATOM   584  C CB  . ALA A 1 82  ? 25.738 -1.552  19.882 1.00 11.51 ? 200 ALA A CB  1 
ATOM   585  N N   . ALA A 1 83  ? 27.664 -1.886  22.342 1.00 10.58 ? 201 ALA A N   1 
ATOM   586  C CA  . ALA A 1 83  ? 28.041 -2.581  23.568 1.00 10.44 ? 201 ALA A CA  1 
ATOM   587  C C   . ALA A 1 83  ? 28.187 -1.631  24.753 1.00 10.55 ? 201 ALA A C   1 
ATOM   588  O O   . ALA A 1 83  ? 27.740 -1.949  25.859 1.00 9.64  ? 201 ALA A O   1 
ATOM   589  C CB  . ALA A 1 83  ? 29.322 -3.390  23.364 1.00 11.11 ? 201 ALA A CB  1 
ATOM   590  N N   . HIS A 1 84  ? 28.826 -0.476  24.525 1.00 10.64 ? 202 HIS A N   1 
ATOM   591  C CA  . HIS A 1 84  ? 28.991 0.533   25.570 1.00 11.33 ? 202 HIS A CA  1 
ATOM   592  C C   . HIS A 1 84  ? 27.618 0.974   26.065 1.00 11.29 ? 202 HIS A C   1 
ATOM   593  O O   . HIS A 1 84  ? 27.396 1.142   27.265 1.00 10.88 ? 202 HIS A O   1 
ATOM   594  C CB  . HIS A 1 84  ? 29.704 1.800   25.040 1.00 11.32 ? 202 HIS A CB  1 
ATOM   595  C CG  . HIS A 1 84  ? 31.172 1.638   24.758 1.00 11.91 ? 202 HIS A CG  1 
ATOM   596  N ND1 . HIS A 1 84  ? 32.143 1.748   25.737 1.00 13.04 ? 202 HIS A ND1 1 
ATOM   597  C CD2 . HIS A 1 84  ? 31.839 1.488   23.590 1.00 12.23 ? 202 HIS A CD2 1 
ATOM   598  C CE1 . HIS A 1 84  ? 33.339 1.621   25.187 1.00 9.45  ? 202 HIS A CE1 1 
ATOM   599  N NE2 . HIS A 1 84  ? 33.183 1.465   23.885 1.00 13.52 ? 202 HIS A NE2 1 
ATOM   600  N N   . LEU A 1 85  ? 26.709 1.215   25.128 1.00 10.78 ? 203 LEU A N   1 
ATOM   601  C CA  . LEU A 1 85  ? 25.378 1.714   25.482 1.00 11.19 ? 203 LEU A CA  1 
ATOM   602  C C   . LEU A 1 85  ? 24.566 0.681   26.251 1.00 10.66 ? 203 LEU A C   1 
ATOM   603  O O   . LEU A 1 85  ? 23.829 1.034   27.177 1.00 10.97 ? 203 LEU A O   1 
ATOM   604  C CB  . LEU A 1 85  ? 24.614 2.181   24.237 1.00 11.26 ? 203 LEU A CB  1 
ATOM   605  C CG  . LEU A 1 85  ? 25.153 3.444   23.559 1.00 12.36 ? 203 LEU A CG  1 
ATOM   606  C CD1 . LEU A 1 85  ? 24.376 3.723   22.283 1.00 13.63 ? 203 LEU A CD1 1 
ATOM   607  C CD2 . LEU A 1 85  ? 25.069 4.644   24.511 1.00 13.15 ? 203 LEU A CD2 1 
ATOM   608  N N   . ALA A 1 86  ? 24.697 -0.591  25.876 1.00 10.92 ? 204 ALA A N   1 
ATOM   609  C CA  . ALA A 1 86  ? 24.022 -1.663  26.611 1.00 11.09 ? 204 ALA A CA  1 
ATOM   610  C C   . ALA A 1 86  ? 24.504 -1.701  28.058 1.00 11.35 ? 204 ALA A C   1 
ATOM   611  O O   . ALA A 1 86  ? 23.707 -1.904  28.976 1.00 11.39 ? 204 ALA A O   1 
ATOM   612  C CB  . ALA A 1 86  ? 24.217 -3.014  25.936 1.00 10.96 ? 204 ALA A CB  1 
ATOM   613  N N   . CYS A 1 87  ? 25.801 -1.476  28.273 1.00 11.73 ? 205 CYS A N   1 
ATOM   614  C CA  . CYS A 1 87  ? 26.328 -1.464  29.641 1.00 12.84 ? 205 CYS A CA  1 
ATOM   615  C C   . CYS A 1 87  ? 25.945 -0.207  30.461 1.00 13.70 ? 205 CYS A C   1 
ATOM   616  O O   . CYS A 1 87  ? 25.606 -0.305  31.641 1.00 13.96 ? 205 CYS A O   1 
ATOM   617  C CB  . CYS A 1 87  ? 27.839 -1.717  29.657 1.00 12.81 ? 205 CYS A CB  1 
ATOM   618  S SG  . CYS A 1 87  ? 28.328 -3.313  28.982 1.00 13.30 ? 205 CYS A SG  1 
ATOM   619  N N   . GLU A 1 88  ? 25.976 0.976   29.861 1.00 14.97 ? 206 GLU A N   1 
ATOM   620  C CA  . GLU A 1 88  ? 25.561 2.135   30.635 1.00 16.52 ? 206 GLU A CA  1 
ATOM   621  C C   . GLU A 1 88  ? 24.058 2.077   30.952 1.00 16.69 ? 206 GLU A C   1 
ATOM   622  O O   . GLU A 1 88  ? 23.602 2.668   31.923 1.00 16.54 ? 206 GLU A O   1 
ATOM   623  C CB  . GLU A 1 88  ? 25.968 3.453   29.972 1.00 17.86 ? 206 GLU A CB  1 
ATOM   624  C CG  . GLU A 1 88  ? 25.307 3.739   28.642 1.00 21.43 ? 206 GLU A CG  1 
ATOM   625  C CD  . GLU A 1 88  ? 25.554 5.167   28.167 1.00 27.20 ? 206 GLU A CD  1 
ATOM   626  O OE1 . GLU A 1 88  ? 25.340 6.114   28.956 1.00 29.87 ? 206 GLU A OE1 1 
ATOM   627  O OE2 . GLU A 1 88  ? 25.968 5.343   27.005 1.00 30.39 ? 206 GLU A OE2 1 
ATOM   628  N N   . HIS A 1 89  ? 23.303 1.310   30.169 1.00 16.28 ? 207 HIS A N   1 
ATOM   629  C CA  . HIS A 1 89  ? 21.867 1.180   30.419 1.00 17.22 ? 207 HIS A CA  1 
ATOM   630  C C   . HIS A 1 89  ? 21.532 -0.081  31.206 1.00 17.25 ? 207 HIS A C   1 
ATOM   631  O O   . HIS A 1 89  ? 20.371 -0.483  31.283 1.00 18.17 ? 207 HIS A O   1 
ATOM   632  C CB  . HIS A 1 89  ? 21.065 1.228   29.116 1.00 17.04 ? 207 HIS A CB  1 
ATOM   633  C CG  . HIS A 1 89  ? 20.902 2.606   28.561 1.00 17.84 ? 207 HIS A CG  1 
ATOM   634  N ND1 . HIS A 1 89  ? 19.794 3.389   28.817 1.00 20.48 ? 207 HIS A ND1 1 
ATOM   635  C CD2 . HIS A 1 89  ? 21.708 3.345   27.763 1.00 18.83 ? 207 HIS A CD2 1 
ATOM   636  C CE1 . HIS A 1 89  ? 19.926 4.549   28.197 1.00 19.36 ? 207 HIS A CE1 1 
ATOM   637  N NE2 . HIS A 1 89  ? 21.082 4.549   27.557 1.00 20.23 ? 207 HIS A NE2 1 
ATOM   638  N N   . ARG A 1 90  ? 22.556 -0.698  31.788 1.00 17.50 ? 208 ARG A N   1 
ATOM   639  C CA  . ARG A 1 90  ? 22.382 -1.901  32.600 1.00 17.99 ? 208 ARG A CA  1 
ATOM   640  C C   . ARG A 1 90  ? 21.444 -2.928  31.949 1.00 18.28 ? 208 ARG A C   1 
ATOM   641  O O   . ARG A 1 90  ? 20.518 -3.421  32.595 1.00 18.35 ? 208 ARG A O   1 
ATOM   642  C CB  . ARG A 1 90  ? 21.836 -1.526  33.986 1.00 18.15 ? 208 ARG A CB  1 
ATOM   643  C CG  . ARG A 1 90  ? 22.655 -0.477  34.744 1.00 18.72 ? 208 ARG A CG  1 
ATOM   644  C CD  . ARG A 1 90  ? 22.055 -0.112  36.099 1.00 22.27 ? 208 ARG A CD  1 
ATOM   645  N NE  . ARG A 1 90  ? 22.961 0.674   36.943 1.00 24.02 ? 208 ARG A NE  1 
ATOM   646  C CZ  . ARG A 1 90  ? 22.992 1.999   36.976 1.00 26.09 ? 208 ARG A CZ  1 
ATOM   647  N NH1 . ARG A 1 90  ? 22.184 2.704   36.205 1.00 26.81 ? 208 ARG A NH1 1 
ATOM   648  N NH2 . ARG A 1 90  ? 23.848 2.627   37.773 1.00 27.59 ? 208 ARG A NH2 1 
ATOM   649  N N   . SER A 1 91  ? 21.694 -3.261  30.684 1.00 18.02 ? 209 SER A N   1 
ATOM   650  C CA  . SER A 1 91  ? 20.792 -4.130  29.933 1.00 17.92 ? 209 SER A CA  1 
ATOM   651  C C   . SER A 1 91  ? 21.488 -5.367  29.413 1.00 17.52 ? 209 SER A C   1 
ATOM   652  O O   . SER A 1 91  ? 21.944 -5.402  28.275 1.00 17.38 ? 209 SER A O   1 
ATOM   653  C CB  . SER A 1 91  ? 20.159 -3.359  28.767 1.00 18.05 ? 209 SER A CB  1 
ATOM   654  O OG  . SER A 1 91  ? 19.235 -4.169  28.062 1.00 19.60 ? 209 SER A OG  1 
ATOM   655  N N   . PRO A 1 92  ? 21.565 -6.386  30.257 1.00 17.45 ? 210 PRO A N   1 
ATOM   656  C CA  . PRO A 1 92  ? 22.164 -7.664  29.875 1.00 16.82 ? 210 PRO A CA  1 
ATOM   657  C C   . PRO A 1 92  ? 21.466 -8.320  28.678 1.00 16.54 ? 210 PRO A C   1 
ATOM   658  O O   . PRO A 1 92  ? 22.121 -9.019  27.915 1.00 15.64 ? 210 PRO A O   1 
ATOM   659  C CB  . PRO A 1 92  ? 21.956 -8.534  31.121 1.00 17.34 ? 210 PRO A CB  1 
ATOM   660  C CG  . PRO A 1 92  ? 21.749 -7.582  32.232 1.00 17.96 ? 210 PRO A CG  1 
ATOM   661  C CD  . PRO A 1 92  ? 21.108 -6.376  31.656 1.00 17.55 ? 210 PRO A CD  1 
ATOM   662  N N   . THR A 1 93  ? 20.161 -8.119  28.529 1.00 16.68 ? 211 THR A N   1 
ATOM   663  C CA  . THR A 1 93  ? 19.452 -8.747  27.415 1.00 16.85 ? 211 THR A CA  1 
ATOM   664  C C   . THR A 1 93  ? 19.817 -8.114  26.082 1.00 16.18 ? 211 THR A C   1 
ATOM   665  O O   . THR A 1 93  ? 19.936 -8.808  25.078 1.00 16.24 ? 211 THR A O   1 
ATOM   666  C CB  . THR A 1 93  ? 17.926 -8.741  27.625 1.00 17.45 ? 211 THR A CB  1 
ATOM   667  O OG1 . THR A 1 93  ? 17.474 -7.403  27.845 1.00 19.28 ? 211 THR A OG1 1 
ATOM   668  C CG2 . THR A 1 93  ? 17.574 -9.461  28.919 1.00 17.65 ? 211 THR A CG2 1 
ATOM   669  N N   . CYS A 1 94  ? 19.988 -6.795  26.065 1.00 15.25 ? 212 CYS A N   1 
ATOM   670  C CA  . CYS A 1 94  ? 20.405 -6.132  24.837 1.00 15.09 ? 212 CYS A CA  1 
ATOM   671  C C   . CYS A 1 94  ? 21.851 -6.489  24.512 1.00 14.02 ? 212 CYS A C   1 
ATOM   672  O O   . CYS A 1 94  ? 22.211 -6.658  23.348 1.00 13.62 ? 212 CYS A O   1 
ATOM   673  C CB  . CYS A 1 94  ? 20.229 -4.620  24.935 1.00 15.13 ? 212 CYS A CB  1 
ATOM   674  S SG  . CYS A 1 94  ? 18.531 -4.073  24.674 1.00 19.29 ? 212 CYS A SG  1 
ATOM   675  N N   . LEU A 1 95  ? 22.678 -6.609  25.544 1.00 12.90 ? 213 LEU A N   1 
ATOM   676  C CA  . LEU A 1 95  ? 24.070 -6.984  25.334 1.00 12.40 ? 213 LEU A CA  1 
ATOM   677  C C   . LEU A 1 95  ? 24.136 -8.391  24.757 1.00 12.45 ? 213 LEU A C   1 
ATOM   678  O O   . LEU A 1 95  ? 24.907 -8.664  23.841 1.00 11.64 ? 213 LEU A O   1 
ATOM   679  C CB  . LEU A 1 95  ? 24.863 -6.890  26.637 1.00 12.26 ? 213 LEU A CB  1 
ATOM   680  C CG  . LEU A 1 95  ? 26.348 -7.245  26.551 1.00 12.96 ? 213 LEU A CG  1 
ATOM   681  C CD1 . LEU A 1 95  ? 27.062 -6.357  25.529 1.00 12.63 ? 213 LEU A CD1 1 
ATOM   682  C CD2 . LEU A 1 95  ? 26.998 -7.113  27.932 1.00 12.16 ? 213 LEU A CD2 1 
ATOM   683  N N   . ARG A 1 96  ? 23.318 -9.286  25.302 1.00 12.85 ? 214 ARG A N   1 
ATOM   684  C CA  . ARG A 1 96  ? 23.248 -10.643 24.797 1.00 13.96 ? 214 ARG A CA  1 
ATOM   685  C C   . ARG A 1 96  ? 22.761 -10.650 23.347 1.00 14.00 ? 214 ARG A C   1 
ATOM   686  O O   . ARG A 1 96  ? 23.300 -11.359 22.510 1.00 14.16 ? 214 ARG A O   1 
ATOM   687  C CB  . ARG A 1 96  ? 22.315 -11.486 25.668 1.00 14.76 ? 214 ARG A CB  1 
ATOM   688  C CG  . ARG A 1 96  ? 22.375 -12.975 25.371 1.00 17.56 ? 214 ARG A CG  1 
ATOM   689  C CD  . ARG A 1 96  ? 21.600 -13.827 26.352 1.00 22.82 ? 214 ARG A CD  1 
ATOM   690  N NE  . ARG A 1 96  ? 22.235 -13.875 27.667 1.00 25.89 ? 214 ARG A NE  1 
ATOM   691  C CZ  . ARG A 1 96  ? 23.239 -14.686 27.975 1.00 28.40 ? 214 ARG A CZ  1 
ATOM   692  N NH1 . ARG A 1 96  ? 23.726 -15.516 27.063 1.00 30.61 ? 214 ARG A NH1 1 
ATOM   693  N NH2 . ARG A 1 96  ? 23.755 -14.674 29.195 1.00 29.04 ? 214 ARG A NH2 1 
ATOM   694  N N   . ALA A 1 97  ? 21.739 -9.856  23.049 1.00 13.47 ? 215 ALA A N   1 
ATOM   695  C CA  . ALA A 1 97  ? 21.228 -9.811  21.681 1.00 13.94 ? 215 ALA A CA  1 
ATOM   696  C C   . ALA A 1 97  ? 22.319 -9.358  20.696 1.00 13.85 ? 215 ALA A C   1 
ATOM   697  O O   . ALA A 1 97  ? 22.445 -9.905  19.602 1.00 14.17 ? 215 ALA A O   1 
ATOM   698  C CB  . ALA A 1 97  ? 20.006 -8.913  21.594 1.00 13.82 ? 215 ALA A CB  1 
ATOM   699  N N   . LEU A 1 98  ? 23.122 -8.382  21.109 1.00 13.52 ? 216 LEU A N   1 
ATOM   700  C CA  . LEU A 1 98  ? 24.190 -7.856  20.269 1.00 14.37 ? 216 LEU A CA  1 
ATOM   701  C C   . LEU A 1 98  ? 25.279 -8.898  20.030 1.00 14.15 ? 216 LEU A C   1 
ATOM   702  O O   . LEU A 1 98  ? 25.658 -9.162  18.900 1.00 14.52 ? 216 LEU A O   1 
ATOM   703  C CB  . LEU A 1 98  ? 24.818 -6.621  20.927 1.00 14.05 ? 216 LEU A CB  1 
ATOM   704  C CG  . LEU A 1 98  ? 24.166 -5.264  20.713 1.00 16.56 ? 216 LEU A CG  1 
ATOM   705  C CD1 . LEU A 1 98  ? 24.737 -4.262  21.722 1.00 17.00 ? 216 LEU A CD1 1 
ATOM   706  C CD2 . LEU A 1 98  ? 24.406 -4.792  19.287 1.00 15.59 ? 216 LEU A CD2 1 
ATOM   707  N N   . LEU A 1 99  ? 25.773 -9.488  21.112 1.00 14.99 ? 217 LEU A N   1 
ATOM   708  C CA  . LEU A 1 99  ? 26.865 -10.450 21.028 1.00 16.10 ? 217 LEU A CA  1 
ATOM   709  C C   . LEU A 1 99  ? 26.472 -11.727 20.291 1.00 16.70 ? 217 LEU A C   1 
ATOM   710  O O   . LEU A 1 99  ? 27.311 -12.339 19.638 1.00 17.44 ? 217 LEU A O   1 
ATOM   711  C CB  . LEU A 1 99  ? 27.417 -10.778 22.422 1.00 16.09 ? 217 LEU A CB  1 
ATOM   712  C CG  . LEU A 1 99  ? 27.941 -9.602  23.264 1.00 16.33 ? 217 LEU A CG  1 
ATOM   713  C CD1 . LEU A 1 99  ? 28.437 -10.108 24.592 1.00 16.80 ? 217 LEU A CD1 1 
ATOM   714  C CD2 . LEU A 1 99  ? 29.040 -8.826  22.547 1.00 19.63 ? 217 LEU A CD2 1 
ATOM   715  N N   . ASP A 1 100 ? 25.200 -12.111 20.378 1.00 17.04 ? 218 ASP A N   1 
ATOM   716  C CA  . ASP A 1 100 ? 24.714 -13.305 19.691 1.00 17.60 ? 218 ASP A CA  1 
ATOM   717  C C   . ASP A 1 100 ? 24.434 -13.041 18.201 1.00 17.42 ? 218 ASP A C   1 
ATOM   718  O O   . ASP A 1 100 ? 24.558 -13.948 17.374 1.00 17.08 ? 218 ASP A O   1 
ATOM   719  C CB  . ASP A 1 100 ? 23.434 -13.863 20.361 1.00 18.14 ? 218 ASP A CB  1 
ATOM   720  C CG  . ASP A 1 100 ? 23.714 -14.615 21.678 1.00 21.10 ? 218 ASP A CG  1 
ATOM   721  O OD1 . ASP A 1 100 ? 24.878 -14.628 22.160 1.00 22.13 ? 218 ASP A OD1 1 
ATOM   722  O OD2 . ASP A 1 100 ? 22.812 -15.225 22.300 1.00 23.67 ? 218 ASP A OD2 1 
ATOM   723  N N   . SER A 1 101 ? 24.061 -11.808 17.857 1.00 17.12 ? 219 SER A N   1 
ATOM   724  C CA  . SER A 1 101 ? 23.672 -11.500 16.480 1.00 17.55 ? 219 SER A CA  1 
ATOM   725  C C   . SER A 1 101 ? 24.803 -11.033 15.577 1.00 17.54 ? 219 SER A C   1 
ATOM   726  O O   . SER A 1 101 ? 24.725 -11.179 14.358 1.00 17.12 ? 219 SER A O   1 
ATOM   727  C CB  . SER A 1 101 ? 22.529 -10.475 16.448 1.00 17.92 ? 219 SER A CB  1 
ATOM   728  O OG  . SER A 1 101 ? 21.481 -10.857 17.317 1.00 18.68 ? 219 SER A OG  1 
ATOM   729  N N   . ALA A 1 102 ? 25.848 -10.459 16.164 1.00 17.90 ? 220 ALA A N   1 
ATOM   730  C CA  . ALA A 1 102 ? 26.946 -9.917  15.367 1.00 18.55 ? 220 ALA A CA  1 
ATOM   731  C C   . ALA A 1 102 ? 27.682 -10.996 14.587 1.00 19.30 ? 220 ALA A C   1 
ATOM   732  O O   . ALA A 1 102 ? 27.906 -12.098 15.085 1.00 19.86 ? 220 ALA A O   1 
ATOM   733  C CB  . ALA A 1 102 ? 27.917 -9.127  16.243 1.00 18.53 ? 220 ALA A CB  1 
ATOM   734  N N   . ALA A 1 103 ? 28.058 -10.673 13.356 1.00 20.33 ? 221 ALA A N   1 
ATOM   735  C CA  . ALA A 1 103 ? 28.850 -11.583 12.546 1.00 20.89 ? 221 ALA A CA  1 
ATOM   736  C C   . ALA A 1 103 ? 30.251 -11.715 13.146 1.00 21.42 ? 221 ALA A C   1 
ATOM   737  O O   . ALA A 1 103 ? 30.788 -10.764 13.708 1.00 20.93 ? 221 ALA A O   1 
ATOM   738  C CB  . ALA A 1 103 ? 28.920 -11.088 11.108 1.00 20.79 ? 221 ALA A CB  1 
ATOM   739  N N   . PRO A 1 104 ? 30.830 -12.907 13.056 1.00 22.28 ? 222 PRO A N   1 
ATOM   740  C CA  . PRO A 1 104 ? 32.166 -13.140 13.608 1.00 22.45 ? 222 PRO A CA  1 
ATOM   741  C C   . PRO A 1 104 ? 33.164 -12.137 13.044 1.00 22.94 ? 222 PRO A C   1 
ATOM   742  O O   . PRO A 1 104 ? 33.173 -11.890 11.840 1.00 23.17 ? 222 PRO A O   1 
ATOM   743  C CB  . PRO A 1 104 ? 32.494 -14.560 13.143 1.00 22.96 ? 222 PRO A CB  1 
ATOM   744  C CG  . PRO A 1 104 ? 31.137 -15.216 12.965 1.00 22.40 ? 222 PRO A CG  1 
ATOM   745  C CD  . PRO A 1 104 ? 30.249 -14.119 12.440 1.00 22.18 ? 222 PRO A CD  1 
ATOM   746  N N   . GLY A 1 105 ? 33.969 -11.544 13.917 1.00 23.15 ? 223 GLY A N   1 
ATOM   747  C CA  . GLY A 1 105 ? 34.974 -10.579 13.504 1.00 23.60 ? 223 GLY A CA  1 
ATOM   748  C C   . GLY A 1 105 ? 34.488 -9.158  13.235 1.00 23.63 ? 223 GLY A C   1 
ATOM   749  O O   . GLY A 1 105 ? 35.232 -8.346  12.682 1.00 24.49 ? 223 GLY A O   1 
ATOM   750  N N   . THR A 1 106 ? 33.253 -8.840  13.609 1.00 22.93 ? 224 THR A N   1 
ATOM   751  C CA  . THR A 1 106 ? 32.756 -7.481  13.385 1.00 22.36 ? 224 THR A CA  1 
ATOM   752  C C   . THR A 1 106 ? 32.611 -6.674  14.682 1.00 21.67 ? 224 THR A C   1 
ATOM   753  O O   . THR A 1 106 ? 32.520 -5.458  14.649 1.00 21.90 ? 224 THR A O   1 
ATOM   754  C CB  . THR A 1 106 ? 31.414 -7.490  12.618 1.00 22.52 ? 224 THR A CB  1 
ATOM   755  O OG1 . THR A 1 106 ? 30.382 -8.033  13.450 1.00 22.45 ? 224 THR A OG1 1 
ATOM   756  C CG2 . THR A 1 106 ? 31.475 -8.455  11.434 1.00 23.15 ? 224 THR A CG2 1 
ATOM   757  N N   . LEU A 1 107 ? 32.569 -7.356  15.817 1.00 20.66 ? 225 LEU A N   1 
ATOM   758  C CA  . LEU A 1 107 ? 32.387 -6.674  17.098 1.00 20.51 ? 225 LEU A CA  1 
ATOM   759  C C   . LEU A 1 107 ? 33.640 -6.803  17.960 1.00 19.73 ? 225 LEU A C   1 
ATOM   760  O O   . LEU A 1 107 ? 34.123 -7.904  18.181 1.00 20.23 ? 225 LEU A O   1 
ATOM   761  C CB  . LEU A 1 107 ? 31.172 -7.254  17.830 1.00 20.24 ? 225 LEU A CB  1 
ATOM   762  C CG  . LEU A 1 107 ? 30.503 -6.418  18.923 1.00 21.55 ? 225 LEU A CG  1 
ATOM   763  C CD1 . LEU A 1 107 ? 29.091 -6.938  19.213 1.00 22.23 ? 225 LEU A CD1 1 
ATOM   764  C CD2 . LEU A 1 107 ? 31.331 -6.402  20.190 1.00 21.81 ? 225 LEU A CD2 1 
ATOM   765  N N   . ASP A 1 108 ? 34.151 -5.676  18.453 1.00 18.84 ? 226 ASP A N   1 
ATOM   766  C CA  . ASP A 1 108 ? 35.391 -5.667  19.236 1.00 17.67 ? 226 ASP A CA  1 
ATOM   767  C C   . ASP A 1 108 ? 35.111 -5.117  20.618 1.00 16.33 ? 226 ASP A C   1 
ATOM   768  O O   . ASP A 1 108 ? 34.794 -3.938  20.769 1.00 15.37 ? 226 ASP A O   1 
ATOM   769  C CB  . ASP A 1 108 ? 36.437 -4.789  18.538 1.00 18.32 ? 226 ASP A CB  1 
ATOM   770  C CG  . ASP A 1 108 ? 37.853 -5.013  19.066 1.00 20.41 ? 226 ASP A CG  1 
ATOM   771  O OD1 . ASP A 1 108 ? 38.027 -5.514  20.212 1.00 21.62 ? 226 ASP A OD1 1 
ATOM   772  O OD2 . ASP A 1 108 ? 38.860 -4.713  18.390 1.00 22.53 ? 226 ASP A OD2 1 
ATOM   773  N N   . LEU A 1 109 ? 35.226 -5.960  21.636 1.00 14.75 ? 227 LEU A N   1 
ATOM   774  C CA  . LEU A 1 109 ? 34.919 -5.510  23.000 1.00 14.44 ? 227 LEU A CA  1 
ATOM   775  C C   . LEU A 1 109 ? 36.013 -4.645  23.600 1.00 14.10 ? 227 LEU A C   1 
ATOM   776  O O   . LEU A 1 109 ? 35.869 -4.119  24.711 1.00 14.36 ? 227 LEU A O   1 
ATOM   777  C CB  . LEU A 1 109 ? 34.600 -6.696  23.916 1.00 14.27 ? 227 LEU A CB  1 
ATOM   778  C CG  . LEU A 1 109 ? 33.311 -7.465  23.583 1.00 14.84 ? 227 LEU A CG  1 
ATOM   779  C CD1 . LEU A 1 109 ? 33.213 -8.747  24.410 1.00 15.66 ? 227 LEU A CD1 1 
ATOM   780  C CD2 . LEU A 1 109 ? 32.066 -6.600  23.776 1.00 14.84 ? 227 LEU A CD2 1 
ATOM   781  N N   . GLU A 1 110 ? 37.106 -4.475  22.873 1.00 13.89 ? 228 GLU A N   1 
ATOM   782  C CA  . GLU A 1 110 ? 38.178 -3.607  23.364 1.00 14.02 ? 228 GLU A CA  1 
ATOM   783  C C   . GLU A 1 110 ? 37.999 -2.164  22.890 1.00 13.59 ? 228 GLU A C   1 
ATOM   784  O O   . GLU A 1 110 ? 38.835 -1.300  23.161 1.00 12.36 ? 228 GLU A O   1 
ATOM   785  C CB  . GLU A 1 110 ? 39.545 -4.159  22.969 1.00 14.54 ? 228 GLU A CB  1 
ATOM   786  C CG  . GLU A 1 110 ? 39.877 -5.469  23.669 1.00 16.61 ? 228 GLU A CG  1 
ATOM   787  C CD  . GLU A 1 110 ? 39.288 -5.548  25.068 1.00 20.05 ? 228 GLU A CD  1 
ATOM   788  O OE1 . GLU A 1 110 ? 38.550 -6.517  25.345 1.00 22.06 ? 228 GLU A OE1 1 
ATOM   789  O OE2 . GLU A 1 110 ? 39.561 -4.651  25.898 1.00 21.60 ? 228 GLU A OE2 1 
ATOM   790  N N   . ALA A 1 111 ? 36.882 -1.902  22.214 1.00 13.49 ? 229 ALA A N   1 
ATOM   791  C CA  . ALA A 1 111 ? 36.561 -0.545  21.750 1.00 13.16 ? 229 ALA A CA  1 
ATOM   792  C C   . ALA A 1 111 ? 36.634 0.490   22.879 1.00 13.10 ? 229 ALA A C   1 
ATOM   793  O O   . ALA A 1 111 ? 36.130 0.259   23.980 1.00 12.67 ? 229 ALA A O   1 
ATOM   794  C CB  . ALA A 1 111 ? 35.167 -0.520  21.101 1.00 12.73 ? 229 ALA A CB  1 
ATOM   795  N N   . ARG A 1 112 ? 37.235 1.641   22.595 1.00 13.51 ? 230 ARG A N   1 
ATOM   796  C CA  . ARG A 1 112 ? 37.353 2.711   23.591 1.00 13.57 ? 230 ARG A CA  1 
ATOM   797  C C   . ARG A 1 112 ? 36.475 3.902   23.200 1.00 13.15 ? 230 ARG A C   1 
ATOM   798  O O   . ARG A 1 112 ? 36.561 4.382   22.068 1.00 13.15 ? 230 ARG A O   1 
ATOM   799  C CB  . ARG A 1 112 ? 38.813 3.175   23.732 1.00 13.53 ? 230 ARG A CB  1 
ATOM   800  C CG  . ARG A 1 112 ? 39.858 2.031   23.855 1.00 17.07 ? 230 ARG A CG  1 
ATOM   801  C CD  . ARG A 1 112 ? 39.649 1.132   25.056 1.00 19.55 ? 230 ARG A CD  1 
ATOM   802  N NE  . ARG A 1 112 ? 40.607 0.014   25.120 1.00 20.45 ? 230 ARG A NE  1 
ATOM   803  C CZ  . ARG A 1 112 ? 41.844 0.121   25.598 1.00 22.69 ? 230 ARG A CZ  1 
ATOM   804  N NH1 . ARG A 1 112 ? 42.293 1.295   26.020 1.00 23.18 ? 230 ARG A NH1 1 
ATOM   805  N NH2 . ARG A 1 112 ? 42.642 -0.943  25.638 1.00 23.87 ? 230 ARG A NH2 1 
ATOM   806  N N   . ASN A 1 113 ? 35.625 4.370   24.120 1.00 12.90 ? 231 ASN A N   1 
ATOM   807  C CA  . ASN A 1 113 ? 34.824 5.565   23.836 1.00 13.18 ? 231 ASN A CA  1 
ATOM   808  C C   . ASN A 1 113 ? 35.696 6.807   23.935 1.00 13.42 ? 231 ASN A C   1 
ATOM   809  O O   . ASN A 1 113 ? 36.878 6.710   24.280 1.00 12.41 ? 231 ASN A O   1 
ATOM   810  C CB  . ASN A 1 113 ? 33.554 5.662   24.719 1.00 12.74 ? 231 ASN A CB  1 
ATOM   811  C CG  . ASN A 1 113 ? 33.870 5.796   26.216 1.00 12.74 ? 231 ASN A CG  1 
ATOM   812  O OD1 . ASN A 1 113 ? 34.981 6.146   26.607 1.00 12.71 ? 231 ASN A OD1 1 
ATOM   813  N ND2 . ASN A 1 113 ? 32.874 5.529   27.052 1.00 10.94 ? 231 ASN A ND2 1 
ATOM   814  N N   . TYR A 1 114 ? 35.130 7.970   23.636 1.00 13.96 ? 232 TYR A N   1 
ATOM   815  C CA  . TYR A 1 114 ? 35.939 9.184   23.576 1.00 15.53 ? 232 TYR A CA  1 
ATOM   816  C C   . TYR A 1 114 ? 36.603 9.497   24.917 1.00 16.74 ? 232 TYR A C   1 
ATOM   817  O O   . TYR A 1 114 ? 37.702 10.059  24.957 1.00 17.58 ? 232 TYR A O   1 
ATOM   818  C CB  . TYR A 1 114 ? 35.126 10.376  23.046 1.00 14.71 ? 232 TYR A CB  1 
ATOM   819  C CG  . TYR A 1 114 ? 34.769 10.261  21.573 1.00 14.22 ? 232 TYR A CG  1 
ATOM   820  C CD1 . TYR A 1 114 ? 35.537 9.486   20.697 1.00 13.36 ? 232 TYR A CD1 1 
ATOM   821  C CD2 . TYR A 1 114 ? 33.669 10.927  21.059 1.00 12.00 ? 232 TYR A CD2 1 
ATOM   822  C CE1 . TYR A 1 114 ? 35.202 9.389   19.341 1.00 13.06 ? 232 TYR A CE1 1 
ATOM   823  C CE2 . TYR A 1 114 ? 33.328 10.830  19.722 1.00 11.51 ? 232 TYR A CE2 1 
ATOM   824  C CZ  . TYR A 1 114 ? 34.089 10.075  18.867 1.00 12.97 ? 232 TYR A CZ  1 
ATOM   825  O OH  . TYR A 1 114 ? 33.729 9.999   17.535 1.00 12.65 ? 232 TYR A OH  1 
ATOM   826  N N   . ASP A 1 115 ? 35.953 9.103   26.004 1.00 17.89 ? 233 ASP A N   1 
ATOM   827  C CA  . ASP A 1 115 ? 36.537 9.245   27.335 1.00 19.44 ? 233 ASP A CA  1 
ATOM   828  C C   . ASP A 1 115 ? 37.694 8.265   27.545 1.00 19.22 ? 233 ASP A C   1 
ATOM   829  O O   . ASP A 1 115 ? 38.547 8.481   28.404 1.00 20.25 ? 233 ASP A O   1 
ATOM   830  C CB  . ASP A 1 115 ? 35.478 9.030   28.410 1.00 19.86 ? 233 ASP A CB  1 
ATOM   831  C CG  . ASP A 1 115 ? 34.512 10.182  28.507 1.00 22.97 ? 233 ASP A CG  1 
ATOM   832  O OD1 . ASP A 1 115 ? 34.951 11.340  28.335 1.00 27.76 ? 233 ASP A OD1 1 
ATOM   833  O OD2 . ASP A 1 115 ? 33.292 10.034  28.750 1.00 26.70 ? 233 ASP A OD2 1 
ATOM   834  N N   . GLY A 1 116 ? 37.706 7.180   26.776 1.00 18.68 ? 234 GLY A N   1 
ATOM   835  C CA  . GLY A 1 116 ? 38.793 6.211   26.829 1.00 17.98 ? 234 GLY A CA  1 
ATOM   836  C C   . GLY A 1 116 ? 38.449 4.861   27.446 1.00 17.73 ? 234 GLY A C   1 
ATOM   837  O O   . GLY A 1 116 ? 39.299 3.958   27.492 1.00 18.78 ? 234 GLY A O   1 
ATOM   838  N N   . LEU A 1 117 ? 37.202 4.701   27.885 1.00 16.23 ? 235 LEU A N   1 
ATOM   839  C CA  . LEU A 1 117 ? 36.783 3.481   28.573 1.00 15.26 ? 235 LEU A CA  1 
ATOM   840  C C   . LEU A 1 117 ? 36.283 2.384   27.650 1.00 14.09 ? 235 LEU A C   1 
ATOM   841  O O   . LEU A 1 117 ? 35.696 2.660   26.595 1.00 13.10 ? 235 LEU A O   1 
ATOM   842  C CB  . LEU A 1 117 ? 35.669 3.802   29.584 1.00 15.18 ? 235 LEU A CB  1 
ATOM   843  C CG  . LEU A 1 117 ? 35.958 4.856   30.652 1.00 17.45 ? 235 LEU A CG  1 
ATOM   844  C CD1 . LEU A 1 117 ? 34.735 5.062   31.534 1.00 17.84 ? 235 LEU A CD1 1 
ATOM   845  C CD2 . LEU A 1 117 ? 37.158 4.454   31.488 1.00 18.74 ? 235 LEU A CD2 1 
ATOM   846  N N   . THR A 1 118 ? 36.502 1.135   28.065 1.00 12.66 ? 236 THR A N   1 
ATOM   847  C CA  . THR A 1 118 ? 35.915 -0.010  27.385 1.00 11.96 ? 236 THR A CA  1 
ATOM   848  C C   . THR A 1 118 ? 34.534 -0.239  27.963 1.00 11.28 ? 236 THR A C   1 
ATOM   849  O O   . THR A 1 118 ? 34.176 0.358   28.975 1.00 10.26 ? 236 THR A O   1 
ATOM   850  C CB  . THR A 1 118 ? 36.731 -1.284  27.636 1.00 12.12 ? 236 THR A CB  1 
ATOM   851  O OG1 . THR A 1 118 ? 36.662 -1.622  29.034 1.00 12.08 ? 236 THR A OG1 1 
ATOM   852  C CG2 . THR A 1 118 ? 38.209 -1.049  27.380 1.00 11.57 ? 236 THR A CG2 1 
ATOM   853  N N   . ALA A 1 119 ? 33.770 -1.115  27.316 1.00 10.26 ? 237 ALA A N   1 
ATOM   854  C CA  . ALA A 1 119 ? 32.468 -1.522  27.820 1.00 9.96  ? 237 ALA A CA  1 
ATOM   855  C C   . ALA A 1 119 ? 32.587 -2.112  29.229 1.00 9.65  ? 237 ALA A C   1 
ATOM   856  O O   . ALA A 1 119 ? 31.730 -1.873  30.080 1.00 9.95  ? 237 ALA A O   1 
ATOM   857  C CB  . ALA A 1 119 ? 31.835 -2.518  26.880 1.00 9.66  ? 237 ALA A CB  1 
ATOM   858  N N   . LEU A 1 120 ? 33.653 -2.871  29.471 1.00 9.46  ? 238 LEU A N   1 
ATOM   859  C CA  . LEU A 1 120 ? 33.888 -3.460  30.792 1.00 10.14 ? 238 LEU A CA  1 
ATOM   860  C C   . LEU A 1 120 ? 34.039 -2.401  31.894 1.00 10.28 ? 238 LEU A C   1 
ATOM   861  O O   . LEU A 1 120 ? 33.489 -2.552  32.993 1.00 10.93 ? 238 LEU A O   1 
ATOM   862  C CB  . LEU A 1 120 ? 35.098 -4.408  30.770 1.00 9.64  ? 238 LEU A CB  1 
ATOM   863  C CG  . LEU A 1 120 ? 35.412 -5.099  32.094 1.00 10.52 ? 238 LEU A CG  1 
ATOM   864  C CD1 . LEU A 1 120 ? 34.178 -5.861  32.573 1.00 10.52 ? 238 LEU A CD1 1 
ATOM   865  C CD2 . LEU A 1 120 ? 36.596 -6.041  31.944 1.00 9.75  ? 238 LEU A CD2 1 
ATOM   866  N N   . HIS A 1 121 ? 34.786 -1.336  31.610 1.00 11.04 ? 239 HIS A N   1 
ATOM   867  C CA  . HIS A 1 121 ? 34.927 -0.231  32.566 1.00 11.69 ? 239 HIS A CA  1 
ATOM   868  C C   . HIS A 1 121 ? 33.556 0.345   32.907 1.00 11.69 ? 239 HIS A C   1 
ATOM   869  O O   . HIS A 1 121 ? 33.230 0.545   34.069 1.00 12.14 ? 239 HIS A O   1 
ATOM   870  C CB  . HIS A 1 121 ? 35.808 0.896   32.007 1.00 12.18 ? 239 HIS A CB  1 
ATOM   871  C CG  . HIS A 1 121 ? 37.261 0.546   31.901 1.00 13.52 ? 239 HIS A CG  1 
ATOM   872  N ND1 . HIS A 1 121 ? 38.079 0.401   33.003 1.00 16.15 ? 239 HIS A ND1 1 
ATOM   873  C CD2 . HIS A 1 121 ? 38.054 0.354   30.820 1.00 14.04 ? 239 HIS A CD2 1 
ATOM   874  C CE1 . HIS A 1 121 ? 39.306 0.116   32.604 1.00 14.56 ? 239 HIS A CE1 1 
ATOM   875  N NE2 . HIS A 1 121 ? 39.315 0.071   31.285 1.00 15.98 ? 239 HIS A NE2 1 
ATOM   876  N N   . VAL A 1 122 ? 32.766 0.637   31.877 1.00 11.52 ? 240 VAL A N   1 
ATOM   877  C CA  . VAL A 1 122 ? 31.416 1.159   32.062 1.00 11.34 ? 240 VAL A CA  1 
ATOM   878  C C   . VAL A 1 122 ? 30.559 0.212   32.908 1.00 11.12 ? 240 VAL A C   1 
ATOM   879  O O   . VAL A 1 122 ? 29.904 0.639   33.860 1.00 11.03 ? 240 VAL A O   1 
ATOM   880  C CB  . VAL A 1 122 ? 30.716 1.402   30.710 1.00 11.39 ? 240 VAL A CB  1 
ATOM   881  C CG1 . VAL A 1 122 ? 29.264 1.799   30.926 1.00 10.85 ? 240 VAL A CG1 1 
ATOM   882  C CG2 . VAL A 1 122 ? 31.446 2.488   29.919 1.00 12.16 ? 240 VAL A CG2 1 
ATOM   883  N N   . ALA A 1 123 ? 30.583 -1.073  32.575 1.00 11.24 ? 241 ALA A N   1 
ATOM   884  C CA  . ALA A 1 123 ? 29.792 -2.052  33.309 1.00 11.82 ? 241 ALA A CA  1 
ATOM   885  C C   . ALA A 1 123 ? 30.174 -2.113  34.796 1.00 12.76 ? 241 ALA A C   1 
ATOM   886  O O   . ALA A 1 123 ? 29.305 -2.161  35.674 1.00 12.54 ? 241 ALA A O   1 
ATOM   887  C CB  . ALA A 1 123 ? 29.913 -3.439  32.665 1.00 11.48 ? 241 ALA A CB  1 
ATOM   888  N N   . VAL A 1 124 ? 31.472 -2.133  35.066 1.00 13.33 ? 242 VAL A N   1 
ATOM   889  C CA  . VAL A 1 124 ? 31.961 -2.204  36.444 1.00 14.47 ? 242 VAL A CA  1 
ATOM   890  C C   . VAL A 1 124 ? 31.500 -0.975  37.223 1.00 15.58 ? 242 VAL A C   1 
ATOM   891  O O   . VAL A 1 124 ? 31.065 -1.083  38.375 1.00 15.79 ? 242 VAL A O   1 
ATOM   892  C CB  . VAL A 1 124 ? 33.497 -2.345  36.482 1.00 14.48 ? 242 VAL A CB  1 
ATOM   893  C CG1 . VAL A 1 124 ? 34.045 -2.140  37.919 1.00 15.22 ? 242 VAL A CG1 1 
ATOM   894  C CG2 . VAL A 1 124 ? 33.918 -3.707  35.942 1.00 13.31 ? 242 VAL A CG2 1 
ATOM   895  N N   . ASN A 1 125 ? 31.555 0.182   36.570 1.00 16.57 ? 243 ASN A N   1 
ATOM   896  C CA  . ASN A 1 125 ? 31.102 1.434   37.163 1.00 18.20 ? 243 ASN A CA  1 
ATOM   897  C C   . ASN A 1 125 ? 29.613 1.445   37.525 1.00 19.24 ? 243 ASN A C   1 
ATOM   898  O O   . ASN A 1 125 ? 29.225 2.053   38.516 1.00 19.46 ? 243 ASN A O   1 
ATOM   899  C CB  . ASN A 1 125 ? 31.480 2.621   36.281 1.00 18.66 ? 243 ASN A CB  1 
ATOM   900  C CG  . ASN A 1 125 ? 32.968 2.931   36.339 1.00 20.32 ? 243 ASN A CG  1 
ATOM   901  O OD1 . ASN A 1 125 ? 33.666 2.486   37.254 1.00 22.98 ? 243 ASN A OD1 1 
ATOM   902  N ND2 . ASN A 1 125 ? 33.462 3.691   35.363 1.00 20.79 ? 243 ASN A ND2 1 
ATOM   903  N N   . THR A 1 126 ? 28.785 0.755   36.742 1.00 19.88 ? 244 THR A N   1 
ATOM   904  C CA  . THR A 1 126 ? 27.377 0.622   37.091 1.00 21.00 ? 244 THR A CA  1 
ATOM   905  C C   . THR A 1 126 ? 27.230 -0.457  38.156 1.00 22.06 ? 244 THR A C   1 
ATOM   906  O O   . THR A 1 126 ? 26.186 -0.569  38.792 1.00 22.13 ? 244 THR A O   1 
ATOM   907  C CB  . THR A 1 126 ? 26.512 0.231   35.876 1.00 20.90 ? 244 THR A CB  1 
ATOM   908  O OG1 . THR A 1 126 ? 26.786 -1.128  35.510 1.00 20.16 ? 244 THR A OG1 1 
ATOM   909  C CG2 . THR A 1 126 ? 26.874 1.042   34.638 1.00 19.82 ? 244 THR A CG2 1 
ATOM   910  N N   . GLU A 1 127 ? 28.277 -1.261  38.320 1.00 23.48 ? 245 GLU A N   1 
ATOM   911  C CA  . GLU A 1 127 ? 28.273 -2.380  39.264 1.00 25.16 ? 245 GLU A CA  1 
ATOM   912  C C   . GLU A 1 127 ? 27.209 -3.423  38.948 1.00 25.36 ? 245 GLU A C   1 
ATOM   913  O O   . GLU A 1 127 ? 26.770 -4.167  39.829 1.00 26.12 ? 245 GLU A O   1 
ATOM   914  C CB  . GLU A 1 127 ? 28.127 -1.880  40.696 1.00 26.10 ? 245 GLU A CB  1 
ATOM   915  C CG  . GLU A 1 127 ? 29.185 -0.863  41.080 1.00 27.81 ? 245 GLU A CG  1 
ATOM   916  C CD  . GLU A 1 127 ? 28.869 -0.172  42.375 1.00 29.67 ? 245 GLU A CD  1 
ATOM   917  O OE1 . GLU A 1 127 ? 27.667 -0.053  42.700 1.00 32.69 ? 245 GLU A OE1 1 
ATOM   918  O OE2 . GLU A 1 127 ? 29.815 0.253   43.063 1.00 30.73 ? 245 GLU A OE2 1 
ATOM   919  N N   . CYS A 1 128 ? 26.794 -3.478  37.688 1.00 25.25 ? 246 CYS A N   1 
ATOM   920  C CA  . CYS A 1 128 ? 25.843 -4.488  37.251 1.00 24.31 ? 246 CYS A CA  1 
ATOM   921  C C   . CYS A 1 128 ? 26.586 -5.801  37.055 1.00 23.83 ? 246 CYS A C   1 
ATOM   922  O O   . CYS A 1 128 ? 27.390 -5.946  36.131 1.00 23.90 ? 246 CYS A O   1 
ATOM   923  C CB  . CYS A 1 128 ? 25.156 -4.055  35.958 1.00 24.80 ? 246 CYS A CB  1 
ATOM   924  S SG  . CYS A 1 128 ? 23.977 -5.262  35.304 1.00 24.40 ? 246 CYS A SG  1 
ATOM   925  N N   . GLN A 1 129 ? 26.326 -6.759  37.936 1.00 22.71 ? 247 GLN A N   1 
ATOM   926  C CA  . GLN A 1 129 ? 27.028 -8.025  37.898 1.00 22.04 ? 247 GLN A CA  1 
ATOM   927  C C   . GLN A 1 129 ? 26.741 -8.813  36.626 1.00 20.97 ? 247 GLN A C   1 
ATOM   928  O O   . GLN A 1 129 ? 27.607 -9.529  36.124 1.00 20.16 ? 247 GLN A O   1 
ATOM   929  C CB  . GLN A 1 129 ? 26.688 -8.851  39.137 1.00 22.50 ? 247 GLN A CB  1 
ATOM   930  C CG  . GLN A 1 129 ? 27.052 -8.126  40.442 1.00 24.74 ? 247 GLN A CG  1 
ATOM   931  C CD  . GLN A 1 129 ? 26.483 -8.787  41.672 1.00 26.12 ? 247 GLN A CD  1 
ATOM   932  O OE1 . GLN A 1 129 ? 26.217 -9.987  41.674 1.00 27.35 ? 247 GLN A OE1 1 
ATOM   933  N NE2 . GLN A 1 129 ? 26.308 -8.009  42.733 1.00 26.57 ? 247 GLN A NE2 1 
ATOM   934  N N   . GLU A 1 130 ? 25.531 -8.657  36.099 1.00 19.85 ? 248 GLU A N   1 
ATOM   935  C CA  . GLU A 1 130 ? 25.100 -9.429  34.932 1.00 19.43 ? 248 GLU A CA  1 
ATOM   936  C C   . GLU A 1 130 ? 25.838 -9.043  33.642 1.00 18.37 ? 248 GLU A C   1 
ATOM   937  O O   . GLU A 1 130 ? 26.236 -9.910  32.862 1.00 18.25 ? 248 GLU A O   1 
ATOM   938  C CB  . GLU A 1 130 ? 23.586 -9.308  34.743 1.00 19.66 ? 248 GLU A CB  1 
ATOM   939  C CG  . GLU A 1 130 ? 22.757 -9.964  35.841 1.00 21.61 ? 248 GLU A CG  1 
ATOM   940  C CD  . GLU A 1 130 ? 22.844 -9.241  37.179 1.00 25.14 ? 248 GLU A CD  1 
ATOM   941  O OE1 . GLU A 1 130 ? 22.866 -7.993  37.200 1.00 27.11 ? 248 GLU A OE1 1 
ATOM   942  O OE2 . GLU A 1 130 ? 22.891 -9.927  38.218 1.00 27.97 ? 248 GLU A OE2 1 
ATOM   943  N N   . THR A 1 131 ? 26.015 -7.745  33.423 1.00 17.09 ? 249 THR A N   1 
ATOM   944  C CA  . THR A 1 131 ? 26.728 -7.273  32.236 1.00 15.84 ? 249 THR A CA  1 
ATOM   945  C C   . THR A 1 131 ? 28.226 -7.545  32.354 1.00 15.15 ? 249 THR A C   1 
ATOM   946  O O   . THR A 1 131 ? 28.866 -7.936  31.382 1.00 14.13 ? 249 THR A O   1 
ATOM   947  C CB  . THR A 1 131 ? 26.457 -5.779  31.977 1.00 15.92 ? 249 THR A CB  1 
ATOM   948  O OG1 . THR A 1 131 ? 26.778 -5.025  33.150 1.00 16.03 ? 249 THR A OG1 1 
ATOM   949  C CG2 . THR A 1 131 ? 24.967 -5.533  31.789 1.00 16.45 ? 249 THR A CG2 1 
ATOM   950  N N   . VAL A 1 132 ? 28.787 -7.360  33.551 1.00 14.23 ? 250 VAL A N   1 
ATOM   951  C CA  . VAL A 1 132 ? 30.196 -7.654  33.748 1.00 13.94 ? 250 VAL A CA  1 
ATOM   952  C C   . VAL A 1 132 ? 30.467 -9.117  33.420 1.00 14.28 ? 250 VAL A C   1 
ATOM   953  O O   . VAL A 1 132 ? 31.357 -9.430  32.633 1.00 13.56 ? 250 VAL A O   1 
ATOM   954  C CB  . VAL A 1 132 ? 30.676 -7.308  35.196 1.00 13.63 ? 250 VAL A CB  1 
ATOM   955  C CG1 . VAL A 1 132 ? 32.088 -7.804  35.436 1.00 13.79 ? 250 VAL A CG1 1 
ATOM   956  C CG2 . VAL A 1 132 ? 30.594 -5.801  35.424 1.00 13.01 ? 250 VAL A CG2 1 
ATOM   957  N N   . GLN A 1 133 ? 29.670 -10.011 33.997 1.00 14.75 ? 251 GLN A N   1 
ATOM   958  C CA  . GLN A 1 133 ? 29.855 -11.435 33.770 1.00 15.55 ? 251 GLN A CA  1 
ATOM   959  C C   . GLN A 1 133 ? 29.802 -11.799 32.295 1.00 14.90 ? 251 GLN A C   1 
ATOM   960  O O   . GLN A 1 133 ? 30.669 -12.502 31.796 1.00 15.26 ? 251 GLN A O   1 
ATOM   961  C CB  . GLN A 1 133 ? 28.821 -12.269 34.539 1.00 15.93 ? 251 GLN A CB  1 
ATOM   962  C CG  A GLN A 1 133 ? 29.135 -13.764 34.502 0.60 17.71 ? 251 GLN A CG  1 
ATOM   963  C CG  B GLN A 1 133 ? 29.000 -13.772 34.394 0.40 17.41 ? 251 GLN A CG  1 
ATOM   964  C CD  A GLN A 1 133 ? 28.202 -14.597 35.358 0.60 18.85 ? 251 GLN A CD  1 
ATOM   965  C CD  B GLN A 1 133 ? 29.919 -14.352 35.449 0.40 18.58 ? 251 GLN A CD  1 
ATOM   966  O OE1 A GLN A 1 133 ? 28.047 -14.336 36.553 0.60 20.54 ? 251 GLN A OE1 1 
ATOM   967  O OE1 B GLN A 1 133 ? 30.289 -13.666 36.398 0.40 20.34 ? 251 GLN A OE1 1 
ATOM   968  N NE2 A GLN A 1 133 ? 27.593 -15.611 34.756 0.60 19.18 ? 251 GLN A NE2 1 
ATOM   969  N NE2 B GLN A 1 133 ? 30.281 -15.620 35.293 0.40 19.24 ? 251 GLN A NE2 1 
ATOM   970  N N   . LEU A 1 134 ? 28.789 -11.313 31.597 1.00 14.41 ? 252 LEU A N   1 
ATOM   971  C CA  . LEU A 1 134 ? 28.629 -11.662 30.192 1.00 14.00 ? 252 LEU A CA  1 
ATOM   972  C C   . LEU A 1 134 ? 29.798 -11.140 29.348 1.00 13.68 ? 252 LEU A C   1 
ATOM   973  O O   . LEU A 1 134 ? 30.329 -11.865 28.519 1.00 14.19 ? 252 LEU A O   1 
ATOM   974  C CB  . LEU A 1 134 ? 27.302 -11.133 29.660 1.00 14.10 ? 252 LEU A CB  1 
ATOM   975  C CG  . LEU A 1 134 ? 26.982 -11.405 28.196 1.00 14.81 ? 252 LEU A CG  1 
ATOM   976  C CD1 . LEU A 1 134 ? 27.002 -12.914 27.927 1.00 13.39 ? 252 LEU A CD1 1 
ATOM   977  C CD2 . LEU A 1 134 ? 25.629 -10.779 27.847 1.00 15.88 ? 252 LEU A CD2 1 
ATOM   978  N N   . LEU A 1 135 ? 30.201 -9.887  29.563 1.00 12.84 ? 253 LEU A N   1 
ATOM   979  C CA  . LEU A 1 135 ? 31.351 -9.342  28.844 1.00 12.56 ? 253 LEU A CA  1 
ATOM   980  C C   . LEU A 1 135 ? 32.581 -10.249 29.022 1.00 12.86 ? 253 LEU A C   1 
ATOM   981  O O   . LEU A 1 135 ? 33.271 -10.574 28.064 1.00 12.30 ? 253 LEU A O   1 
ATOM   982  C CB  . LEU A 1 135 ? 31.676 -7.929  29.339 1.00 12.42 ? 253 LEU A CB  1 
ATOM   983  C CG  . LEU A 1 135 ? 30.684 -6.831  28.932 1.00 12.15 ? 253 LEU A CG  1 
ATOM   984  C CD1 . LEU A 1 135 ? 30.987 -5.560  29.688 1.00 12.40 ? 253 LEU A CD1 1 
ATOM   985  C CD2 . LEU A 1 135 ? 30.711 -6.586  27.418 1.00 13.20 ? 253 LEU A CD2 1 
ATOM   986  N N   . LEU A 1 136 ? 32.838 -10.651 30.260 1.00 13.17 ? 254 LEU A N   1 
ATOM   987  C CA  . LEU A 1 136 ? 33.993 -11.488 30.565 1.00 14.45 ? 254 LEU A CA  1 
ATOM   988  C C   . LEU A 1 136 ? 33.899 -12.880 29.937 1.00 14.89 ? 254 LEU A C   1 
ATOM   989  O O   . LEU A 1 136 ? 34.910 -13.459 29.535 1.00 15.52 ? 254 LEU A O   1 
ATOM   990  C CB  . LEU A 1 136 ? 34.187 -11.595 32.078 1.00 14.24 ? 254 LEU A CB  1 
ATOM   991  C CG  . LEU A 1 136 ? 34.563 -10.276 32.770 1.00 13.94 ? 254 LEU A CG  1 
ATOM   992  C CD1 . LEU A 1 136 ? 34.568 -10.450 34.271 1.00 15.06 ? 254 LEU A CD1 1 
ATOM   993  C CD2 . LEU A 1 136 ? 35.930 -9.758  32.274 1.00 13.37 ? 254 LEU A CD2 1 
ATOM   994  N N   . GLU A 1 137 ? 32.683 -13.410 29.852 1.00 15.91 ? 255 GLU A N   1 
ATOM   995  C CA  . GLU A 1 137 ? 32.466 -14.732 29.267 1.00 16.65 ? 255 GLU A CA  1 
ATOM   996  C C   . GLU A 1 137 ? 32.652 -14.682 27.753 1.00 16.82 ? 255 GLU A C   1 
ATOM   997  O O   . GLU A 1 137 ? 32.941 -15.700 27.113 1.00 17.01 ? 255 GLU A O   1 
ATOM   998  C CB  . GLU A 1 137 ? 31.062 -15.240 29.597 1.00 17.04 ? 255 GLU A CB  1 
ATOM   999  C CG  . GLU A 1 137 ? 30.883 -15.698 31.034 1.00 19.61 ? 255 GLU A CG  1 
ATOM   1000 C CD  . GLU A 1 137 ? 29.444 -16.055 31.357 1.00 23.81 ? 255 GLU A CD  1 
ATOM   1001 O OE1 . GLU A 1 137 ? 28.532 -15.556 30.665 1.00 25.96 ? 255 GLU A OE1 1 
ATOM   1002 O OE2 . GLU A 1 137 ? 29.223 -16.826 32.314 1.00 25.56 ? 255 GLU A OE2 1 
ATOM   1003 N N   . ARG A 1 138 ? 32.493 -13.496 27.174 1.00 16.88 ? 256 ARG A N   1 
ATOM   1004 C CA  . ARG A 1 138 ? 32.589 -13.370 25.721 1.00 17.03 ? 256 ARG A CA  1 
ATOM   1005 C C   . ARG A 1 138 ? 33.911 -12.793 25.209 1.00 17.29 ? 256 ARG A C   1 
ATOM   1006 O O   . ARG A 1 138 ? 34.014 -12.411 24.047 1.00 17.20 ? 256 ARG A O   1 
ATOM   1007 C CB  . ARG A 1 138 ? 31.391 -12.620 25.160 1.00 17.36 ? 256 ARG A CB  1 
ATOM   1008 C CG  . ARG A 1 138 ? 30.056 -13.287 25.476 1.00 18.80 ? 256 ARG A CG  1 
ATOM   1009 C CD  . ARG A 1 138 ? 29.912 -14.715 24.952 1.00 21.34 ? 256 ARG A CD  1 
ATOM   1010 N NE  . ARG A 1 138 ? 28.592 -15.263 25.267 1.00 22.38 ? 256 ARG A NE  1 
ATOM   1011 C CZ  . ARG A 1 138 ? 27.538 -15.200 24.461 1.00 23.58 ? 256 ARG A CZ  1 
ATOM   1012 N NH1 . ARG A 1 138 ? 27.638 -14.629 23.267 1.00 22.11 ? 256 ARG A NH1 1 
ATOM   1013 N NH2 . ARG A 1 138 ? 26.376 -15.722 24.846 1.00 24.43 ? 256 ARG A NH2 1 
ATOM   1014 N N   . GLY A 1 139 ? 34.911 -12.705 26.084 1.00 16.98 ? 257 GLY A N   1 
ATOM   1015 C CA  . GLY A 1 139 ? 36.248 -12.329 25.653 1.00 17.07 ? 257 GLY A CA  1 
ATOM   1016 C C   . GLY A 1 139 ? 36.793 -10.947 25.997 1.00 16.76 ? 257 GLY A C   1 
ATOM   1017 O O   . GLY A 1 139 ? 37.906 -10.619 25.574 1.00 17.25 ? 257 GLY A O   1 
ATOM   1018 N N   . ALA A 1 140 ? 36.042 -10.138 26.744 1.00 16.15 ? 258 ALA A N   1 
ATOM   1019 C CA  . ALA A 1 140 ? 36.535 -8.812  27.135 1.00 16.01 ? 258 ALA A CA  1 
ATOM   1020 C C   . ALA A 1 140 ? 37.814 -8.923  27.974 1.00 16.41 ? 258 ALA A C   1 
ATOM   1021 O O   . ALA A 1 140 ? 37.904 -9.763  28.871 1.00 16.64 ? 258 ALA A O   1 
ATOM   1022 C CB  . ALA A 1 140 ? 35.477 -8.046  27.895 1.00 15.95 ? 258 ALA A CB  1 
ATOM   1023 N N   . ASP A 1 141 ? 38.795 -8.073  27.668 1.00 16.28 ? 259 ASP A N   1 
ATOM   1024 C CA  . ASP A 1 141 ? 40.072 -8.067  28.370 1.00 16.28 ? 259 ASP A CA  1 
ATOM   1025 C C   . ASP A 1 141 ? 39.857 -7.511  29.779 1.00 15.89 ? 259 ASP A C   1 
ATOM   1026 O O   . ASP A 1 141 ? 39.565 -6.329  29.953 1.00 15.04 ? 259 ASP A O   1 
ATOM   1027 C CB  . ASP A 1 141 ? 41.081 -7.211  27.606 1.00 16.93 ? 259 ASP A CB  1 
ATOM   1028 C CG  . ASP A 1 141 ? 42.513 -7.424  28.078 1.00 19.73 ? 259 ASP A CG  1 
ATOM   1029 O OD1 . ASP A 1 141 ? 42.705 -7.851  29.237 1.00 19.72 ? 259 ASP A OD1 1 
ATOM   1030 O OD2 . ASP A 1 141 ? 43.507 -7.199  27.354 1.00 22.66 ? 259 ASP A OD2 1 
ATOM   1031 N N   . ILE A 1 142 ? 39.994 -8.382  30.779 1.00 15.59 ? 260 ILE A N   1 
ATOM   1032 C CA  . ILE A 1 142 ? 39.733 -8.016  32.170 1.00 15.63 ? 260 ILE A CA  1 
ATOM   1033 C C   . ILE A 1 142 ? 40.756 -7.040  32.756 1.00 16.36 ? 260 ILE A C   1 
ATOM   1034 O O   . ILE A 1 142 ? 40.486 -6.391  33.772 1.00 16.00 ? 260 ILE A O   1 
ATOM   1035 C CB  . ILE A 1 142 ? 39.642 -9.277  33.050 1.00 16.08 ? 260 ILE A CB  1 
ATOM   1036 C CG1 . ILE A 1 142 ? 39.068 -8.920  34.424 1.00 16.03 ? 260 ILE A CG1 1 
ATOM   1037 C CG2 . ILE A 1 142 ? 41.018 -9.947  33.170 1.00 15.20 ? 260 ILE A CG2 1 
ATOM   1038 C CD1 . ILE A 1 142 ? 38.598 -10.104 35.222 1.00 18.46 ? 260 ILE A CD1 1 
ATOM   1039 N N   . ASP A 1 143 ? 41.916 -6.926  32.115 1.00 16.57 ? 261 ASP A N   1 
ATOM   1040 C CA  . ASP A 1 143 ? 42.979 -6.048  32.610 1.00 17.90 ? 261 ASP A CA  1 
ATOM   1041 C C   . ASP A 1 143 ? 43.147 -4.792  31.746 1.00 18.49 ? 261 ASP A C   1 
ATOM   1042 O O   . ASP A 1 143 ? 44.090 -4.020  31.944 1.00 18.91 ? 261 ASP A O   1 
ATOM   1043 C CB  . ASP A 1 143 ? 44.321 -6.788  32.666 1.00 17.77 ? 261 ASP A CB  1 
ATOM   1044 C CG  . ASP A 1 143 ? 44.335 -7.933  33.685 1.00 19.00 ? 261 ASP A CG  1 
ATOM   1045 O OD1 . ASP A 1 143 ? 43.910 -7.737  34.849 1.00 17.18 ? 261 ASP A OD1 1 
ATOM   1046 O OD2 . ASP A 1 143 ? 44.789 -9.064  33.410 1.00 21.83 ? 261 ASP A OD2 1 
ATOM   1047 N N   . ALA A 1 144 ? 42.253 -4.584  30.790 1.00 18.81 ? 262 ALA A N   1 
ATOM   1048 C CA  . ALA A 1 144 ? 42.360 -3.408  29.917 1.00 19.39 ? 262 ALA A CA  1 
ATOM   1049 C C   . ALA A 1 144 ? 42.479 -2.088  30.696 1.00 19.90 ? 262 ALA A C   1 
ATOM   1050 O O   . ALA A 1 144 ? 41.723 -1.848  31.642 1.00 19.34 ? 262 ALA A O   1 
ATOM   1051 C CB  . ALA A 1 144 ? 41.190 -3.348  28.959 1.00 19.34 ? 262 ALA A CB  1 
ATOM   1052 N N   . VAL A 1 145 ? 43.431 -1.241  30.296 1.00 21.05 ? 263 VAL A N   1 
ATOM   1053 C CA  . VAL A 1 145 ? 43.614 0.062   30.930 1.00 22.47 ? 263 VAL A CA  1 
ATOM   1054 C C   . VAL A 1 145 ? 43.251 1.194   29.974 1.00 23.63 ? 263 VAL A C   1 
ATOM   1055 O O   . VAL A 1 145 ? 43.785 1.291   28.865 1.00 23.95 ? 263 VAL A O   1 
ATOM   1056 C CB  . VAL A 1 145 ? 45.065 0.292   31.452 1.00 22.84 ? 263 VAL A CB  1 
ATOM   1057 C CG1 . VAL A 1 145 ? 45.557 -0.910  32.270 1.00 22.05 ? 263 VAL A CG1 1 
ATOM   1058 C CG2 . VAL A 1 145 ? 46.012 0.580   30.309 1.00 22.69 ? 263 VAL A CG2 1 
ATOM   1059 N N   . ASP A 1 146 ? 42.300 2.008   30.394 1.00 24.65 ? 264 ASP A N   1 
ATOM   1060 C CA  . ASP A 1 146 ? 41.919 3.196   29.629 1.00 26.21 ? 264 ASP A CA  1 
ATOM   1061 C C   . ASP A 1 146 ? 43.016 4.273   29.712 1.00 26.52 ? 264 ASP A C   1 
ATOM   1062 O O   . ASP A 1 146 ? 43.708 4.393   30.723 1.00 26.31 ? 264 ASP A O   1 
ATOM   1063 C CB  . ASP A 1 146 ? 40.586 3.737   30.127 1.00 26.47 ? 264 ASP A CB  1 
ATOM   1064 C CG  . ASP A 1 146 ? 40.639 4.155   31.571 1.00 28.02 ? 264 ASP A CG  1 
ATOM   1065 O OD1 . ASP A 1 146 ? 40.688 3.273   32.444 1.00 29.32 ? 264 ASP A OD1 1 
ATOM   1066 O OD2 . ASP A 1 146 ? 40.652 5.355   31.930 1.00 31.33 ? 264 ASP A OD2 1 
ATOM   1067 N N   . ILE A 1 147 ? 43.165 5.054   28.650 1.00 26.67 ? 265 ILE A N   1 
ATOM   1068 C CA  . ILE A 1 147 ? 44.266 6.003   28.563 1.00 26.96 ? 265 ILE A CA  1 
ATOM   1069 C C   . ILE A 1 147 ? 44.234 7.133   29.615 1.00 26.95 ? 265 ILE A C   1 
ATOM   1070 O O   . ILE A 1 147 ? 45.285 7.542   30.100 1.00 26.81 ? 265 ILE A O   1 
ATOM   1071 C CB  . ILE A 1 147 ? 44.386 6.561   27.122 1.00 26.78 ? 265 ILE A CB  1 
ATOM   1072 C CG1 . ILE A 1 147 ? 45.291 7.796   27.079 1.00 27.23 ? 265 ILE A CG1 1 
ATOM   1073 C CG2 . ILE A 1 147 ? 43.092 6.713   26.421 0.00 29.48 ? 265 ILE A CG2 1 
ATOM   1074 C CD1 . ILE A 1 147 ? 46.666 7.551   26.471 1.00 26.50 ? 265 ILE A CD1 1 
ATOM   1075 N N   . LYS A 1 148 ? 43.040 7.591   29.997 1.00 27.09 ? 266 LYS A N   1 
ATOM   1076 C CA  . LYS A 1 148 ? 42.899 8.709   30.960 1.00 27.43 ? 266 LYS A CA  1 
ATOM   1077 C C   . LYS A 1 148 ? 43.587 8.487   32.307 1.00 27.28 ? 266 LYS A C   1 
ATOM   1078 O O   . LYS A 1 148 ? 44.399 9.302   32.749 1.00 27.14 ? 266 LYS A O   1 
ATOM   1079 C CB  . LYS A 1 148 ? 41.423 9.015   31.241 1.00 27.91 ? 266 LYS A CB  1 
ATOM   1080 C CG  . LYS A 1 148 ? 40.813 10.146  30.444 1.00 28.62 ? 266 LYS A CG  1 
ATOM   1081 C CD  . LYS A 1 148 ? 39.817 10.916  31.315 1.00 30.99 ? 266 LYS A CD  1 
ATOM   1082 C CE  . LYS A 1 148 ? 38.510 11.179  30.588 1.00 33.37 ? 266 LYS A CE  1 
ATOM   1083 N NZ  . LYS A 1 148 ? 38.620 12.305  29.625 1.00 35.60 ? 266 LYS A NZ  1 
ATOM   1084 N N   . SER A 1 149 ? 43.246 7.380   32.963 1.00 27.02 ? 267 SER A N   1 
ATOM   1085 C CA  . SER A 1 149 ? 43.700 7.126   34.323 1.00 26.46 ? 267 SER A CA  1 
ATOM   1086 C C   . SER A 1 149 ? 44.747 6.033   34.440 1.00 25.49 ? 267 SER A C   1 
ATOM   1087 O O   . SER A 1 149 ? 45.447 5.941   35.453 1.00 25.33 ? 267 SER A O   1 
ATOM   1088 C CB  . SER A 1 149 ? 42.501 6.771   35.197 1.00 27.05 ? 267 SER A CB  1 
ATOM   1089 O OG  . SER A 1 149 ? 41.753 5.704   34.619 1.00 28.99 ? 267 SER A OG  1 
ATOM   1090 N N   . GLY A 1 150 ? 44.850 5.198   33.410 1.00 24.20 ? 268 GLY A N   1 
ATOM   1091 C CA  . GLY A 1 150 ? 45.756 4.066   33.436 1.00 22.62 ? 268 GLY A CA  1 
ATOM   1092 C C   . GLY A 1 150 ? 45.307 3.000   34.428 1.00 21.57 ? 268 GLY A C   1 
ATOM   1093 O O   . GLY A 1 150 ? 46.110 2.183   34.875 1.00 21.85 ? 268 GLY A O   1 
ATOM   1094 N N   . ARG A 1 151 ? 44.021 3.006   34.767 1.00 20.21 ? 269 ARG A N   1 
ATOM   1095 C CA  . ARG A 1 151 ? 43.466 2.075   35.752 1.00 19.50 ? 269 ARG A CA  1 
ATOM   1096 C C   . ARG A 1 151 ? 42.743 0.880   35.127 1.00 18.56 ? 269 ARG A C   1 
ATOM   1097 O O   . ARG A 1 151 ? 41.976 1.041   34.185 1.00 17.36 ? 269 ARG A O   1 
ATOM   1098 C CB  . ARG A 1 151 ? 42.482 2.811   36.661 1.00 19.91 ? 269 ARG A CB  1 
ATOM   1099 C CG  . ARG A 1 151 ? 43.141 3.817   37.588 1.00 20.48 ? 269 ARG A CG  1 
ATOM   1100 C CD  A ARG A 1 151 ? 42.371 5.120   37.736 0.50 22.06 ? 269 ARG A CD  1 
ATOM   1101 C CD  B ARG A 1 151 ? 42.164 4.721   38.310 0.50 22.29 ? 269 ARG A CD  1 
ATOM   1102 N NE  A ARG A 1 151 ? 41.126 4.967   38.482 0.50 22.68 ? 269 ARG A NE  1 
ATOM   1103 N NE  B ARG A 1 151 ? 42.831 5.587   39.279 0.50 22.86 ? 269 ARG A NE  1 
ATOM   1104 C CZ  A ARG A 1 151 ? 40.110 5.810   38.407 0.50 23.20 ? 269 ARG A CZ  1 
ATOM   1105 C CZ  B ARG A 1 151 ? 42.265 6.646   39.840 0.50 23.83 ? 269 ARG A CZ  1 
ATOM   1106 N NH1 A ARG A 1 151 ? 40.179 6.866   37.609 0.50 23.82 ? 269 ARG A NH1 1 
ATOM   1107 N NH1 B ARG A 1 151 ? 41.017 6.969   39.533 0.50 24.58 ? 269 ARG A NH1 1 
ATOM   1108 N NH2 A ARG A 1 151 ? 39.018 5.600   39.129 0.50 24.05 ? 269 ARG A NH2 1 
ATOM   1109 N NH2 B ARG A 1 151 ? 42.940 7.380   40.717 0.50 23.89 ? 269 ARG A NH2 1 
ATOM   1110 N N   . SER A 1 152 ? 42.986 -0.310  35.677 1.00 17.61 ? 270 SER A N   1 
ATOM   1111 C CA  . SER A 1 152 ? 42.274 -1.522  35.259 1.00 16.50 ? 270 SER A CA  1 
ATOM   1112 C C   . SER A 1 152 ? 40.908 -1.488  35.916 1.00 15.64 ? 270 SER A C   1 
ATOM   1113 O O   . SER A 1 152 ? 40.699 -0.725  36.846 1.00 15.09 ? 270 SER A O   1 
ATOM   1114 C CB  . SER A 1 152 ? 43.035 -2.768  35.718 1.00 16.53 ? 270 SER A CB  1 
ATOM   1115 O OG  . SER A 1 152 ? 43.051 -2.857  37.136 1.00 16.99 ? 270 SER A OG  1 
ATOM   1116 N N   . PRO A 1 153 ? 39.964 -2.280  35.419 1.00 15.19 ? 271 PRO A N   1 
ATOM   1117 C CA  . PRO A 1 153 ? 38.638 -2.382  36.044 1.00 14.73 ? 271 PRO A CA  1 
ATOM   1118 C C   . PRO A 1 153 ? 38.720 -2.699  37.547 1.00 14.71 ? 271 PRO A C   1 
ATOM   1119 O O   . PRO A 1 153 ? 37.910 -2.190  38.326 1.00 13.68 ? 271 PRO A O   1 
ATOM   1120 C CB  . PRO A 1 153 ? 37.995 -3.542  35.286 1.00 15.09 ? 271 PRO A CB  1 
ATOM   1121 C CG  . PRO A 1 153 ? 38.619 -3.462  33.919 1.00 14.89 ? 271 PRO A CG  1 
ATOM   1122 C CD  . PRO A 1 153 ? 40.061 -3.093  34.194 1.00 15.14 ? 271 PRO A CD  1 
ATOM   1123 N N   . LEU A 1 154 ? 39.684 -3.521  37.946 1.00 14.47 ? 272 LEU A N   1 
ATOM   1124 C CA  . LEU A 1 154 ? 39.820 -3.875  39.360 1.00 14.87 ? 272 LEU A CA  1 
ATOM   1125 C C   . LEU A 1 154 ? 40.066 -2.642  40.230 1.00 15.24 ? 272 LEU A C   1 
ATOM   1126 O O   . LEU A 1 154 ? 39.463 -2.483  41.298 1.00 15.45 ? 272 LEU A O   1 
ATOM   1127 C CB  . LEU A 1 154 ? 40.938 -4.901  39.569 1.00 15.06 ? 272 LEU A CB  1 
ATOM   1128 C CG  . LEU A 1 154 ? 41.146 -5.339  41.029 1.00 15.05 ? 272 LEU A CG  1 
ATOM   1129 C CD1 . LEU A 1 154 ? 39.859 -5.897  41.621 1.00 14.33 ? 272 LEU A CD1 1 
ATOM   1130 C CD2 . LEU A 1 154 ? 42.278 -6.345  41.147 1.00 17.47 ? 272 LEU A CD2 1 
ATOM   1131 N N   . ILE A 1 155 ? 40.948 -1.769  39.774 1.00 15.51 ? 273 ILE A N   1 
ATOM   1132 C CA  . ILE A 1 155 ? 41.262 -0.566  40.534 1.00 16.52 ? 273 ILE A CA  1 
ATOM   1133 C C   . ILE A 1 155 ? 40.043 0.353   40.586 1.00 17.06 ? 273 ILE A C   1 
ATOM   1134 O O   . ILE A 1 155 ? 39.719 0.917   41.641 1.00 17.15 ? 273 ILE A O   1 
ATOM   1135 C CB  . ILE A 1 155 ? 42.521 0.128   39.961 1.00 16.29 ? 273 ILE A CB  1 
ATOM   1136 C CG1 . ILE A 1 155 ? 43.755 -0.740  40.239 1.00 16.99 ? 273 ILE A CG1 1 
ATOM   1137 C CG2 . ILE A 1 155 ? 42.691 1.523   40.554 1.00 16.86 ? 273 ILE A CG2 1 
ATOM   1138 C CD1 . ILE A 1 155 ? 44.993 -0.378  39.432 1.00 15.77 ? 273 ILE A CD1 1 
ATOM   1139 N N   . HIS A 1 156 ? 39.328 0.457   39.467 1.00 17.66 ? 274 HIS A N   1 
ATOM   1140 C CA  . HIS A 1 156 ? 38.097 1.232   39.437 1.00 18.45 ? 274 HIS A CA  1 
ATOM   1141 C C   . HIS A 1 156 ? 37.139 0.704   40.501 1.00 18.24 ? 274 HIS A C   1 
ATOM   1142 O O   . HIS A 1 156 ? 36.561 1.481   41.264 1.00 18.70 ? 274 HIS A O   1 
ATOM   1143 C CB  . HIS A 1 156 ? 37.432 1.161   38.050 1.00 19.24 ? 274 HIS A CB  1 
ATOM   1144 C CG  . HIS A 1 156 ? 38.069 2.050   37.022 1.00 21.04 ? 274 HIS A CG  1 
ATOM   1145 N ND1 . HIS A 1 156 ? 37.950 3.424   37.049 1.00 24.38 ? 274 HIS A ND1 1 
ATOM   1146 C CD2 . HIS A 1 156 ? 38.808 1.759   35.924 1.00 23.32 ? 274 HIS A CD2 1 
ATOM   1147 C CE1 . HIS A 1 156 ? 38.598 3.942   36.019 1.00 25.06 ? 274 HIS A CE1 1 
ATOM   1148 N NE2 . HIS A 1 156 ? 39.123 2.953   35.318 1.00 25.13 ? 274 HIS A NE2 1 
ATOM   1149 N N   . ALA A 1 157 ? 36.985 -0.619  40.559 1.00 17.68 ? 275 ALA A N   1 
ATOM   1150 C CA  . ALA A 1 157 ? 36.081 -1.253  41.520 1.00 17.26 ? 275 ALA A CA  1 
ATOM   1151 C C   . ALA A 1 157 ? 36.487 -0.962  42.966 1.00 17.36 ? 275 ALA A C   1 
ATOM   1152 O O   . ALA A 1 157 ? 35.630 -0.720  43.827 1.00 16.75 ? 275 ALA A O   1 
ATOM   1153 C CB  . ALA A 1 157 ? 36.021 -2.765  41.286 1.00 17.32 ? 275 ALA A CB  1 
ATOM   1154 N N   . VAL A 1 158 ? 37.788 -0.998  43.231 1.00 17.38 ? 276 VAL A N   1 
ATOM   1155 C CA  . VAL A 1 158 ? 38.292 -0.724  44.577 1.00 18.37 ? 276 VAL A CA  1 
ATOM   1156 C C   . VAL A 1 158 ? 38.029 0.726   44.978 1.00 19.14 ? 276 VAL A C   1 
ATOM   1157 O O   . VAL A 1 158 ? 37.604 0.998   46.102 1.00 19.75 ? 276 VAL A O   1 
ATOM   1158 C CB  . VAL A 1 158 ? 39.787 -1.053  44.712 1.00 17.96 ? 276 VAL A CB  1 
ATOM   1159 C CG1 . VAL A 1 158 ? 40.346 -0.483  46.004 1.00 18.50 ? 276 VAL A CG1 1 
ATOM   1160 C CG2 . VAL A 1 158 ? 39.997 -2.556  44.666 1.00 17.93 ? 276 VAL A CG2 1 
ATOM   1161 N N   . GLU A 1 159 ? 38.270 1.655   44.059 1.00 20.02 ? 277 GLU A N   1 
ATOM   1162 C CA  . GLU A 1 159 ? 38.009 3.073   44.328 1.00 21.18 ? 277 GLU A CA  1 
ATOM   1163 C C   . GLU A 1 159 ? 36.523 3.381   44.554 1.00 21.07 ? 277 GLU A C   1 
ATOM   1164 O O   . GLU A 1 159 ? 36.177 4.267   45.351 1.00 21.01 ? 277 GLU A O   1 
ATOM   1165 C CB  . GLU A 1 159 ? 38.590 3.947   43.221 1.00 21.57 ? 277 GLU A CB  1 
ATOM   1166 C CG  . GLU A 1 159 ? 40.099 3.835   43.124 1.00 24.97 ? 277 GLU A CG  1 
ATOM   1167 C CD  . GLU A 1 159 ? 40.710 4.820   42.154 1.00 28.96 ? 277 GLU A CD  1 
ATOM   1168 O OE1 . GLU A 1 159 ? 40.038 5.184   41.163 1.00 33.02 ? 277 GLU A OE1 1 
ATOM   1169 O OE2 . GLU A 1 159 ? 41.873 5.221   42.378 1.00 31.61 ? 277 GLU A OE2 1 
ATOM   1170 N N   . ASN A 1 160 ? 35.648 2.633   43.882 1.00 20.76 ? 278 ASN A N   1 
ATOM   1171 C CA  . ASN A 1 160 ? 34.200 2.784   44.050 1.00 20.75 ? 278 ASN A CA  1 
ATOM   1172 C C   . ASN A 1 160 ? 33.695 2.076   45.304 1.00 20.39 ? 278 ASN A C   1 
ATOM   1173 O O   . ASN A 1 160 ? 32.490 2.056   45.571 1.00 20.14 ? 278 ASN A O   1 
ATOM   1174 C CB  . ASN A 1 160 ? 33.443 2.207   42.839 1.00 21.21 ? 278 ASN A CB  1 
ATOM   1175 C CG  . ASN A 1 160 ? 33.793 2.902   41.528 1.00 22.54 ? 278 ASN A CG  1 
ATOM   1176 O OD1 . ASN A 1 160 ? 34.308 4.021   41.513 1.00 24.10 ? 278 ASN A OD1 1 
ATOM   1177 N ND2 . ASN A 1 160 ? 33.501 2.233   40.412 1.00 23.57 ? 278 ASN A ND2 1 
ATOM   1178 N N   . ASN A 1 161 ? 34.611 1.464   46.051 1.00 19.97 ? 279 ASN A N   1 
ATOM   1179 C CA  . ASN A 1 161 ? 34.251 0.700   47.244 1.00 20.09 ? 279 ASN A CA  1 
ATOM   1180 C C   . ASN A 1 161 ? 33.129 -0.315  46.991 1.00 19.52 ? 279 ASN A C   1 
ATOM   1181 O O   . ASN A 1 161 ? 32.124 -0.342  47.697 1.00 19.44 ? 279 ASN A O   1 
ATOM   1182 C CB  . ASN A 1 161 ? 33.894 1.631   48.414 1.00 20.59 ? 279 ASN A CB  1 
ATOM   1183 C CG  . ASN A 1 161 ? 33.718 0.879   49.721 1.00 21.70 ? 279 ASN A CG  1 
ATOM   1184 O OD1 . ASN A 1 161 ? 34.400 -0.113  49.972 1.00 23.47 ? 279 ASN A OD1 1 
ATOM   1185 N ND2 . ASN A 1 161 ? 32.780 1.336   50.555 1.00 23.40 ? 279 ASN A ND2 1 
ATOM   1186 N N   . SER A 1 162 ? 33.307 -1.142  45.963 1.00 19.10 ? 280 SER A N   1 
ATOM   1187 C CA  . SER A 1 162 ? 32.338 -2.182  45.647 1.00 18.42 ? 280 SER A CA  1 
ATOM   1188 C C   . SER A 1 162 ? 32.935 -3.570  45.855 1.00 18.03 ? 280 SER A C   1 
ATOM   1189 O O   . SER A 1 162 ? 33.611 -4.110  44.971 1.00 17.94 ? 280 SER A O   1 
ATOM   1190 C CB  . SER A 1 162 ? 31.844 -2.061  44.207 1.00 18.61 ? 280 SER A CB  1 
ATOM   1191 O OG  . SER A 1 162 ? 30.929 -3.117  43.923 1.00 18.78 ? 280 SER A OG  1 
ATOM   1192 N N   . LEU A 1 163 ? 32.675 -4.142  47.019 1.00 17.13 ? 281 LEU A N   1 
ATOM   1193 C CA  . LEU A 1 163 ? 33.168 -5.472  47.341 1.00 16.84 ? 281 LEU A CA  1 
ATOM   1194 C C   . LEU A 1 163 ? 32.640 -6.530  46.359 1.00 16.39 ? 281 LEU A C   1 
ATOM   1195 O O   . LEU A 1 163 ? 33.336 -7.481  46.036 1.00 15.81 ? 281 LEU A O   1 
ATOM   1196 C CB  . LEU A 1 163 ? 32.790 -5.846  48.773 1.00 16.44 ? 281 LEU A CB  1 
ATOM   1197 C CG  . LEU A 1 163 ? 33.298 -7.200  49.261 1.00 16.67 ? 281 LEU A CG  1 
ATOM   1198 C CD1 . LEU A 1 163 ? 34.823 -7.283  49.161 1.00 15.92 ? 281 LEU A CD1 1 
ATOM   1199 C CD2 . LEU A 1 163 ? 32.835 -7.453  50.689 1.00 18.01 ? 281 LEU A CD2 1 
ATOM   1200 N N   . SER A 1 164 ? 31.404 -6.369  45.905 1.00 16.11 ? 282 SER A N   1 
ATOM   1201 C CA  . SER A 1 164 ? 30.851 -7.301  44.926 1.00 16.65 ? 282 SER A CA  1 
ATOM   1202 C C   . SER A 1 164 ? 31.696 -7.325  43.642 1.00 15.96 ? 282 SER A C   1 
ATOM   1203 O O   . SER A 1 164 ? 32.098 -8.395  43.176 1.00 16.26 ? 282 SER A O   1 
ATOM   1204 C CB  . SER A 1 164 ? 29.389 -6.954  44.610 1.00 16.60 ? 282 SER A CB  1 
ATOM   1205 O OG  . SER A 1 164 ? 28.569 -7.182  45.749 1.00 19.43 ? 282 SER A OG  1 
ATOM   1206 N N   . MET A 1 165 ? 31.966 -6.153  43.072 1.00 15.91 ? 283 MET A N   1 
ATOM   1207 C CA  . MET A 1 165 ? 32.749 -6.086  41.826 1.00 15.41 ? 283 MET A CA  1 
ATOM   1208 C C   . MET A 1 165 ? 34.178 -6.591  42.023 1.00 14.99 ? 283 MET A C   1 
ATOM   1209 O O   . MET A 1 165 ? 34.739 -7.250  41.147 1.00 14.52 ? 283 MET A O   1 
ATOM   1210 C CB  . MET A 1 165 ? 32.774 -4.664  41.255 1.00 15.64 ? 283 MET A CB  1 
ATOM   1211 C CG  . MET A 1 165 ? 31.480 -4.210  40.611 1.00 16.62 ? 283 MET A CG  1 
ATOM   1212 S SD  . MET A 1 165 ? 30.939 -5.277  39.227 1.00 16.78 ? 283 MET A SD  1 
ATOM   1213 C CE  . MET A 1 165 ? 29.692 -6.198  40.000 1.00 18.75 ? 283 MET A CE  1 
ATOM   1214 N N   . VAL A 1 166 ? 34.765 -6.263  43.168 1.00 14.18 ? 284 VAL A N   1 
ATOM   1215 C CA  . VAL A 1 166 ? 36.101 -6.727  43.494 1.00 13.86 ? 284 VAL A CA  1 
ATOM   1216 C C   . VAL A 1 166 ? 36.118 -8.244  43.545 1.00 13.49 ? 284 VAL A C   1 
ATOM   1217 O O   . VAL A 1 166 ? 36.970 -8.877  42.938 1.00 12.96 ? 284 VAL A O   1 
ATOM   1218 C CB  . VAL A 1 166 ? 36.618 -6.121  44.829 1.00 14.28 ? 284 VAL A CB  1 
ATOM   1219 C CG1 . VAL A 1 166 ? 37.858 -6.861  45.310 1.00 13.62 ? 284 VAL A CG1 1 
ATOM   1220 C CG2 . VAL A 1 166 ? 36.922 -4.609  44.649 1.00 14.36 ? 284 VAL A CG2 1 
ATOM   1221 N N   . GLN A 1 167 ? 35.144 -8.832  44.231 1.00 13.36 ? 285 GLN A N   1 
ATOM   1222 C CA  . GLN A 1 167 ? 35.060 -10.286 44.304 1.00 12.91 ? 285 GLN A CA  1 
ATOM   1223 C C   . GLN A 1 167 ? 34.812 -10.925 42.929 1.00 12.79 ? 285 GLN A C   1 
ATOM   1224 O O   . GLN A 1 167 ? 35.428 -11.929 42.581 1.00 11.79 ? 285 GLN A O   1 
ATOM   1225 C CB  . GLN A 1 167 ? 33.999 -10.716 45.328 1.00 13.75 ? 285 GLN A CB  1 
ATOM   1226 C CG  . GLN A 1 167 ? 34.437 -10.457 46.786 1.00 14.84 ? 285 GLN A CG  1 
ATOM   1227 C CD  . GLN A 1 167 ? 33.408 -10.890 47.830 1.00 18.07 ? 285 GLN A CD  1 
ATOM   1228 O OE1 . GLN A 1 167 ? 32.242 -11.131 47.509 1.00 17.11 ? 285 GLN A OE1 1 
ATOM   1229 N NE2 . GLN A 1 167 ? 33.841 -10.967 49.093 1.00 18.58 ? 285 GLN A NE2 1 
ATOM   1230 N N   . LEU A 1 168 ? 33.937 -10.312 42.141 1.00 12.48 ? 286 LEU A N   1 
ATOM   1231 C CA  . LEU A 1 168 ? 33.597 -10.829 40.817 1.00 12.12 ? 286 LEU A CA  1 
ATOM   1232 C C   . LEU A 1 168 ? 34.798 -10.808 39.872 1.00 11.89 ? 286 LEU A C   1 
ATOM   1233 O O   . LEU A 1 168 ? 35.053 -11.778 39.163 1.00 11.40 ? 286 LEU A O   1 
ATOM   1234 C CB  . LEU A 1 168 ? 32.416 -10.044 40.223 1.00 11.71 ? 286 LEU A CB  1 
ATOM   1235 C CG  . LEU A 1 168 ? 31.841 -10.561 38.899 1.00 12.85 ? 286 LEU A CG  1 
ATOM   1236 C CD1 . LEU A 1 168 ? 31.505 -12.060 38.993 1.00 13.66 ? 286 LEU A CD1 1 
ATOM   1237 C CD2 . LEU A 1 168 ? 30.613 -9.754  38.483 1.00 14.94 ? 286 LEU A CD2 1 
ATOM   1238 N N   . LEU A 1 169 ? 35.543 -9.706  39.870 1.00 12.31 ? 287 LEU A N   1 
ATOM   1239 C CA  . LEU A 1 169 ? 36.705 -9.589  38.987 1.00 12.36 ? 287 LEU A CA  1 
ATOM   1240 C C   . LEU A 1 169 ? 37.846 -10.537 39.358 1.00 13.15 ? 287 LEU A C   1 
ATOM   1241 O O   . LEU A 1 169 ? 38.476 -11.138 38.481 1.00 12.71 ? 287 LEU A O   1 
ATOM   1242 C CB  . LEU A 1 169 ? 37.199 -8.139  38.923 1.00 12.64 ? 287 LEU A CB  1 
ATOM   1243 C CG  . LEU A 1 169 ? 36.278 -7.149  38.197 1.00 11.95 ? 287 LEU A CG  1 
ATOM   1244 C CD1 . LEU A 1 169 ? 36.597 -5.718  38.583 1.00 12.47 ? 287 LEU A CD1 1 
ATOM   1245 C CD2 . LEU A 1 169 ? 36.371 -7.318  36.682 1.00 15.08 ? 287 LEU A CD2 1 
ATOM   1246 N N   . LEU A 1 170 ? 38.113 -10.681 40.654 1.00 13.45 ? 288 LEU A N   1 
ATOM   1247 C CA  . LEU A 1 170 ? 39.181 -11.568 41.097 1.00 14.15 ? 288 LEU A CA  1 
ATOM   1248 C C   . LEU A 1 170 ? 38.831 -13.008 40.759 1.00 14.70 ? 288 LEU A C   1 
ATOM   1249 O O   . LEU A 1 170 ? 39.687 -13.803 40.380 1.00 14.45 ? 288 LEU A O   1 
ATOM   1250 C CB  . LEU A 1 170 ? 39.437 -11.409 42.598 1.00 14.06 ? 288 LEU A CB  1 
ATOM   1251 C CG  . LEU A 1 170 ? 40.062 -10.064 43.015 1.00 13.73 ? 288 LEU A CG  1 
ATOM   1252 C CD1 . LEU A 1 170 ? 40.052 -9.913  44.529 1.00 15.27 ? 288 LEU A CD1 1 
ATOM   1253 C CD2 . LEU A 1 170 ? 41.475 -9.890  42.465 1.00 14.73 ? 288 LEU A CD2 1 
ATOM   1254 N N   . GLN A 1 171 ? 37.549 -13.314 40.873 1.00 15.77 ? 289 GLN A N   1 
ATOM   1255 C CA  . GLN A 1 171 ? 37.007 -14.613 40.535 1.00 16.90 ? 289 GLN A CA  1 
ATOM   1256 C C   . GLN A 1 171 ? 37.291 -14.948 39.069 1.00 16.93 ? 289 GLN A C   1 
ATOM   1257 O O   . GLN A 1 171 ? 37.491 -16.118 38.708 1.00 17.07 ? 289 GLN A O   1 
ATOM   1258 C CB  . GLN A 1 171 ? 35.500 -14.541 40.767 1.00 17.86 ? 289 GLN A CB  1 
ATOM   1259 C CG  . GLN A 1 171 ? 34.778 -15.824 40.918 1.00 19.88 ? 289 GLN A CG  1 
ATOM   1260 C CD  . GLN A 1 171 ? 33.369 -15.601 41.431 1.00 20.47 ? 289 GLN A CD  1 
ATOM   1261 O OE1 . GLN A 1 171 ? 32.400 -15.735 40.686 1.00 21.82 ? 289 GLN A OE1 1 
ATOM   1262 N NE2 . GLN A 1 171 ? 33.254 -15.263 42.707 1.00 20.98 ? 289 GLN A NE2 1 
ATOM   1263 N N   . HIS A 1 172 ? 37.305 -13.922 38.220 1.00 16.48 ? 290 HIS A N   1 
ATOM   1264 C CA  . HIS A 1 172 ? 37.522 -14.131 36.787 1.00 15.97 ? 290 HIS A CA  1 
ATOM   1265 C C   . HIS A 1 172 ? 38.959 -13.932 36.290 1.00 15.64 ? 290 HIS A C   1 
ATOM   1266 O O   . HIS A 1 172 ? 39.185 -13.757 35.092 1.00 15.90 ? 290 HIS A O   1 
ATOM   1267 C CB  . HIS A 1 172 ? 36.547 -13.288 35.968 1.00 15.98 ? 290 HIS A CB  1 
ATOM   1268 C CG  . HIS A 1 172 ? 35.154 -13.826 35.965 1.00 16.20 ? 290 HIS A CG  1 
ATOM   1269 N ND1 . HIS A 1 172 ? 34.697 -14.699 35.002 1.00 16.72 ? 290 HIS A ND1 1 
ATOM   1270 C CD2 . HIS A 1 172 ? 34.122 -13.636 36.821 1.00 16.43 ? 290 HIS A CD2 1 
ATOM   1271 C CE1 . HIS A 1 172 ? 33.440 -15.016 35.259 1.00 16.61 ? 290 HIS A CE1 1 
ATOM   1272 N NE2 . HIS A 1 172 ? 33.067 -14.384 36.357 1.00 17.40 ? 290 HIS A NE2 1 
ATOM   1273 N N   . GLY A 1 173 ? 39.922 -13.932 37.205 1.00 15.43 ? 291 GLY A N   1 
ATOM   1274 C CA  . GLY A 1 173 ? 41.328 -13.891 36.824 1.00 14.51 ? 291 GLY A CA  1 
ATOM   1275 C C   . GLY A 1 173 ? 42.016 -12.533 36.724 1.00 14.23 ? 291 GLY A C   1 
ATOM   1276 O O   . GLY A 1 173 ? 43.092 -12.431 36.133 1.00 13.48 ? 291 GLY A O   1 
ATOM   1277 N N   . ALA A 1 174 ? 41.423 -11.499 37.315 1.00 13.66 ? 292 ALA A N   1 
ATOM   1278 C CA  . ALA A 1 174 ? 42.003 -10.150 37.261 1.00 14.00 ? 292 ALA A CA  1 
ATOM   1279 C C   . ALA A 1 174 ? 43.364 -10.058 37.980 1.00 14.37 ? 292 ALA A C   1 
ATOM   1280 O O   . ALA A 1 174 ? 43.565 -10.663 39.032 1.00 14.42 ? 292 ALA A O   1 
ATOM   1281 C CB  . ALA A 1 174 ? 41.036 -9.136  37.850 1.00 13.64 ? 292 ALA A CB  1 
ATOM   1282 N N   . ASN A 1 175 ? 44.281 -9.292  37.403 1.00 14.05 ? 293 ASN A N   1 
ATOM   1283 C CA  . ASN A 1 175 ? 45.590 -9.070  37.997 1.00 14.24 ? 293 ASN A CA  1 
ATOM   1284 C C   . ASN A 1 175 ? 45.458 -8.191  39.236 1.00 13.77 ? 293 ASN A C   1 
ATOM   1285 O O   . ASN A 1 175 ? 45.235 -6.996  39.134 1.00 13.84 ? 293 ASN A O   1 
ATOM   1286 C CB  . ASN A 1 175 ? 46.531 -8.428  36.977 1.00 14.36 ? 293 ASN A CB  1 
ATOM   1287 C CG  . ASN A 1 175 ? 47.891 -8.107  37.559 1.00 15.79 ? 293 ASN A CG  1 
ATOM   1288 O OD1 . ASN A 1 175 ? 48.234 -8.558  38.657 1.00 15.52 ? 293 ASN A OD1 1 
ATOM   1289 N ND2 . ASN A 1 175 ? 48.674 -7.315  36.831 1.00 15.76 ? 293 ASN A ND2 1 
ATOM   1290 N N   . VAL A 1 176 ? 45.591 -8.799  40.409 1.00 13.38 ? 294 VAL A N   1 
ATOM   1291 C CA  . VAL A 1 176 ? 45.404 -8.085  41.661 1.00 13.26 ? 294 VAL A CA  1 
ATOM   1292 C C   . VAL A 1 176 ? 46.532 -7.059  41.918 1.00 13.61 ? 294 VAL A C   1 
ATOM   1293 O O   . VAL A 1 176 ? 46.370 -6.109  42.694 1.00 13.46 ? 294 VAL A O   1 
ATOM   1294 C CB  . VAL A 1 176 ? 45.258 -9.094  42.851 1.00 13.32 ? 294 VAL A CB  1 
ATOM   1295 C CG1 . VAL A 1 176 ? 46.586 -9.788  43.150 1.00 13.19 ? 294 VAL A CG1 1 
ATOM   1296 C CG2 . VAL A 1 176 ? 44.710 -8.405  44.079 1.00 13.60 ? 294 VAL A CG2 1 
ATOM   1297 N N   . ASN A 1 177 ? 47.656 -7.229  41.235 1.00 13.60 ? 295 ASN A N   1 
ATOM   1298 C CA  . ASN A 1 177 ? 48.785 -6.320  41.411 1.00 14.41 ? 295 ASN A CA  1 
ATOM   1299 C C   . ASN A 1 177 ? 49.014 -5.311  40.273 1.00 14.47 ? 295 ASN A C   1 
ATOM   1300 O O   . ASN A 1 177 ? 50.096 -4.738  40.146 1.00 14.45 ? 295 ASN A O   1 
ATOM   1301 C CB  . ASN A 1 177 ? 50.052 -7.104  41.710 1.00 14.38 ? 295 ASN A CB  1 
ATOM   1302 C CG  . ASN A 1 177 ? 49.993 -7.791  43.055 1.00 14.77 ? 295 ASN A CG  1 
ATOM   1303 O OD1 . ASN A 1 177 ? 49.614 -7.184  44.056 1.00 13.89 ? 295 ASN A OD1 1 
ATOM   1304 N ND2 . ASN A 1 177 ? 50.351 -9.071  43.084 1.00 17.27 ? 295 ASN A ND2 1 
ATOM   1305 N N   . ALA A 1 178 ? 47.980 -5.069  39.479 1.00 14.43 ? 296 ALA A N   1 
ATOM   1306 C CA  . ALA A 1 178 ? 48.047 -4.040  38.446 1.00 15.37 ? 296 ALA A CA  1 
ATOM   1307 C C   . ALA A 1 178 ? 48.323 -2.670  39.078 1.00 15.44 ? 296 ALA A C   1 
ATOM   1308 O O   . ALA A 1 178 ? 47.846 -2.379  40.180 1.00 15.12 ? 296 ALA A O   1 
ATOM   1309 C CB  . ALA A 1 178 ? 46.752 -4.007  37.656 1.00 15.02 ? 296 ALA A CB  1 
ATOM   1310 N N   . GLN A 1 179 ? 49.092 -1.831  38.386 1.00 16.05 ? 297 GLN A N   1 
ATOM   1311 C CA  . GLN A 1 179 ? 49.424 -0.494  38.906 1.00 16.56 ? 297 GLN A CA  1 
ATOM   1312 C C   . GLN A 1 179 ? 48.957 0.639   37.992 1.00 17.39 ? 297 GLN A C   1 
ATOM   1313 O O   . GLN A 1 179 ? 48.942 0.502   36.761 1.00 17.52 ? 297 GLN A O   1 
ATOM   1314 C CB  . GLN A 1 179 ? 50.936 -0.357  39.113 1.00 16.68 ? 297 GLN A CB  1 
ATOM   1315 C CG  . GLN A 1 179 ? 51.514 -1.198  40.238 1.00 17.71 ? 297 GLN A CG  1 
ATOM   1316 C CD  . GLN A 1 179 ? 53.041 -1.205  40.218 1.00 19.58 ? 297 GLN A CD  1 
ATOM   1317 O OE1 . GLN A 1 179 ? 53.681 -0.549  41.043 1.00 21.71 ? 297 GLN A OE1 1 
ATOM   1318 N NE2 . GLN A 1 179 ? 53.617 -1.919  39.268 1.00 18.66 ? 297 GLN A NE2 1 
ATOM   1319 N N   . MET A 1 180 ? 48.606 1.766   38.599 1.00 17.82 ? 298 MET A N   1 
ATOM   1320 C CA  . MET A 1 180 ? 48.238 2.961   37.858 1.00 18.91 ? 298 MET A CA  1 
ATOM   1321 C C   . MET A 1 180 ? 49.514 3.687   37.423 1.00 18.63 ? 298 MET A C   1 
ATOM   1322 O O   . MET A 1 180 ? 50.606 3.277   37.787 1.00 18.25 ? 298 MET A O   1 
ATOM   1323 C CB  . MET A 1 180 ? 47.440 3.890   38.757 1.00 19.78 ? 298 MET A CB  1 
ATOM   1324 C CG  . MET A 1 180 ? 46.167 3.297   39.314 1.00 22.66 ? 298 MET A CG  1 
ATOM   1325 S SD  . MET A 1 180 ? 45.273 4.517   40.295 1.00 28.25 ? 298 MET A SD  1 
ATOM   1326 C CE  . MET A 1 180 ? 46.396 4.800   41.560 1.00 27.12 ? 298 MET A CE  1 
ATOM   1327 N N   . TYR A 1 181 ? 49.367 4.777   36.665 1.00 19.19 ? 299 TYR A N   1 
ATOM   1328 C CA  . TYR A 1 181 ? 50.515 5.579   36.223 1.00 19.72 ? 299 TYR A CA  1 
ATOM   1329 C C   . TYR A 1 181 ? 51.483 5.914   37.374 1.00 20.19 ? 299 TYR A C   1 
ATOM   1330 O O   . TYR A 1 181 ? 52.708 5.872   37.211 1.00 20.31 ? 299 TYR A O   1 
ATOM   1331 C CB  . TYR A 1 181 ? 50.045 6.885   35.562 1.00 19.85 ? 299 TYR A CB  1 
ATOM   1332 C CG  . TYR A 1 181 ? 49.410 6.722   34.194 1.00 20.61 ? 299 TYR A CG  1 
ATOM   1333 C CD1 . TYR A 1 181 ? 50.087 6.094   33.166 1.00 22.48 ? 299 TYR A CD1 1 
ATOM   1334 C CD2 . TYR A 1 181 ? 48.145 7.228   33.930 1.00 20.73 ? 299 TYR A CD2 1 
ATOM   1335 C CE1 . TYR A 1 181 ? 49.510 5.959   31.903 1.00 24.53 ? 299 TYR A CE1 1 
ATOM   1336 C CE2 . TYR A 1 181 ? 47.562 7.096   32.675 1.00 22.23 ? 299 TYR A CE2 1 
ATOM   1337 C CZ  . TYR A 1 181 ? 48.249 6.456   31.672 1.00 24.01 ? 299 TYR A CZ  1 
ATOM   1338 O OH  . TYR A 1 181 ? 47.683 6.307   30.426 1.00 25.11 ? 299 TYR A OH  1 
ATOM   1339 N N   . SER A 1 182 ? 50.924 6.261   38.528 1.00 20.88 ? 300 SER A N   1 
ATOM   1340 C CA  . SER A 1 182 ? 51.719 6.624   39.701 1.00 21.72 ? 300 SER A CA  1 
ATOM   1341 C C   . SER A 1 182 ? 52.402 5.419   40.343 1.00 21.89 ? 300 SER A C   1 
ATOM   1342 O O   . SER A 1 182 ? 53.243 5.567   41.238 1.00 22.06 ? 300 SER A O   1 
ATOM   1343 C CB  . SER A 1 182 ? 50.828 7.288   40.744 1.00 21.86 ? 300 SER A CB  1 
ATOM   1344 O OG  . SER A 1 182 ? 49.865 6.356   41.226 1.00 23.07 ? 300 SER A OG  1 
ATOM   1345 N N   . GLY A 1 183 ? 52.020 4.225   39.916 1.00 21.54 ? 301 GLY A N   1 
ATOM   1346 C CA  . GLY A 1 183 ? 52.593 3.023   40.480 1.00 21.68 ? 301 GLY A CA  1 
ATOM   1347 C C   . GLY A 1 183 ? 51.817 2.477   41.667 1.00 21.58 ? 301 GLY A C   1 
ATOM   1348 O O   . GLY A 1 183 ? 52.245 1.512   42.292 1.00 21.89 ? 301 GLY A O   1 
ATOM   1349 N N   . SER A 1 184 ? 50.683 3.093   41.983 1.00 21.18 ? 302 SER A N   1 
ATOM   1350 C CA  . SER A 1 184 ? 49.841 2.601   43.068 1.00 21.03 ? 302 SER A CA  1 
ATOM   1351 C C   . SER A 1 184 ? 48.949 1.440   42.607 1.00 20.53 ? 302 SER A C   1 
ATOM   1352 O O   . SER A 1 184 ? 48.491 1.408   41.458 1.00 19.88 ? 302 SER A O   1 
ATOM   1353 C CB  . SER A 1 184 ? 48.983 3.728   43.643 1.00 21.33 ? 302 SER A CB  1 
ATOM   1354 O OG  . SER A 1 184 ? 49.766 4.633   44.414 1.00 23.14 ? 302 SER A OG  1 
ATOM   1355 N N   . SER A 1 185 ? 48.697 0.501   43.517 1.00 19.66 ? 303 SER A N   1 
ATOM   1356 C CA  . SER A 1 185 ? 47.873 -0.670  43.219 1.00 18.68 ? 303 SER A CA  1 
ATOM   1357 C C   . SER A 1 185 ? 46.516 -0.598  43.916 1.00 18.01 ? 303 SER A C   1 
ATOM   1358 O O   . SER A 1 185 ? 46.239 0.337   44.666 1.00 17.98 ? 303 SER A O   1 
ATOM   1359 C CB  . SER A 1 185 ? 48.600 -1.941  43.660 1.00 18.95 ? 303 SER A CB  1 
ATOM   1360 O OG  . SER A 1 185 ? 48.745 -1.969  45.077 1.00 18.63 ? 303 SER A OG  1 
ATOM   1361 N N   . ALA A 1 186 ? 45.671 -1.593  43.667 1.00 16.88 ? 304 ALA A N   1 
ATOM   1362 C CA  . ALA A 1 186 ? 44.381 -1.689  44.328 1.00 16.26 ? 304 ALA A CA  1 
ATOM   1363 C C   . ALA A 1 186 ? 44.572 -1.656  45.842 1.00 15.94 ? 304 ALA A C   1 
ATOM   1364 O O   . ALA A 1 186 ? 43.806 -1.019  46.573 1.00 15.55 ? 304 ALA A O   1 
ATOM   1365 C CB  . ALA A 1 186 ? 43.680 -2.973  43.925 1.00 16.20 ? 304 ALA A CB  1 
ATOM   1366 N N   . LEU A 1 187 ? 45.600 -2.342  46.308 1.00 15.64 ? 305 LEU A N   1 
ATOM   1367 C CA  . LEU A 1 187 ? 45.846 -2.431  47.749 1.00 15.79 ? 305 LEU A CA  1 
ATOM   1368 C C   . LEU A 1 187 ? 46.252 -1.090  48.384 1.00 15.88 ? 305 LEU A C   1 
ATOM   1369 O O   . LEU A 1 187 ? 45.881 -0.809  49.532 1.00 14.93 ? 305 LEU A O   1 
ATOM   1370 C CB  . LEU A 1 187 ? 46.876 -3.523  48.051 1.00 15.54 ? 305 LEU A CB  1 
ATOM   1371 C CG  . LEU A 1 187 ? 47.012 -3.941  49.514 1.00 14.99 ? 305 LEU A CG  1 
ATOM   1372 C CD1 . LEU A 1 187 ? 45.686 -4.403  50.078 1.00 13.51 ? 305 LEU A CD1 1 
ATOM   1373 C CD2 . LEU A 1 187 ? 48.078 -5.024  49.659 1.00 15.52 ? 305 LEU A CD2 1 
ATOM   1374 N N   . HIS A 1 188 ? 47.003 -0.262  47.651 1.00 16.13 ? 306 HIS A N   1 
ATOM   1375 C CA  . HIS A 1 188 ? 47.332 1.074   48.165 1.00 16.57 ? 306 HIS A CA  1 
ATOM   1376 C C   . HIS A 1 188 ? 46.039 1.813   48.469 1.00 16.99 ? 306 HIS A C   1 
ATOM   1377 O O   . HIS A 1 188 ? 45.898 2.417   49.524 1.00 16.87 ? 306 HIS A O   1 
ATOM   1378 C CB  . HIS A 1 188 ? 48.114 1.909   47.150 1.00 16.70 ? 306 HIS A CB  1 
ATOM   1379 C CG  . HIS A 1 188 ? 49.520 1.455   46.930 1.00 16.39 ? 306 HIS A CG  1 
ATOM   1380 N ND1 . HIS A 1 188 ? 50.588 1.965   47.635 1.00 17.61 ? 306 HIS A ND1 1 
ATOM   1381 C CD2 . HIS A 1 188 ? 50.040 0.578   46.043 1.00 17.70 ? 306 HIS A CD2 1 
ATOM   1382 C CE1 . HIS A 1 188 ? 51.703 1.402   47.208 1.00 17.00 ? 306 HIS A CE1 1 
ATOM   1383 N NE2 . HIS A 1 188 ? 51.397 0.559   46.239 1.00 18.08 ? 306 HIS A NE2 1 
ATOM   1384 N N   . SER A 1 189 ? 45.099 1.767   47.525 1.00 17.61 ? 307 SER A N   1 
ATOM   1385 C CA  . SER A 1 189 ? 43.830 2.477   47.666 1.00 18.14 ? 307 SER A CA  1 
ATOM   1386 C C   . SER A 1 189 ? 42.997 1.982   48.838 1.00 18.59 ? 307 SER A C   1 
ATOM   1387 O O   . SER A 1 189 ? 42.520 2.788   49.660 1.00 19.08 ? 307 SER A O   1 
ATOM   1388 C CB  . SER A 1 189 ? 43.011 2.397   46.372 1.00 18.59 ? 307 SER A CB  1 
ATOM   1389 O OG  A SER A 1 189 ? 43.406 3.404   45.454 0.50 18.78 ? 307 SER A OG  1 
ATOM   1390 O OG  B SER A 1 189 ? 41.766 3.056   46.520 0.50 17.82 ? 307 SER A OG  1 
ATOM   1391 N N   . ALA A 1 190 ? 42.812 0.667   48.915 1.00 18.49 ? 308 ALA A N   1 
ATOM   1392 C CA  . ALA A 1 190 ? 42.032 0.065   49.993 1.00 18.68 ? 308 ALA A CA  1 
ATOM   1393 C C   . ALA A 1 190 ? 42.679 0.319   51.347 1.00 18.86 ? 308 ALA A C   1 
ATOM   1394 O O   . ALA A 1 190 ? 41.992 0.629   52.322 1.00 18.49 ? 308 ALA A O   1 
ATOM   1395 C CB  . ALA A 1 190 ? 41.856 -1.441  49.761 1.00 18.50 ? 308 ALA A CB  1 
ATOM   1396 N N   . SER A 1 191 ? 44.001 0.194   51.398 1.00 19.34 ? 309 SER A N   1 
ATOM   1397 C CA  . SER A 1 191 ? 44.747 0.380   52.639 1.00 20.45 ? 309 SER A CA  1 
ATOM   1398 C C   . SER A 1 191 ? 44.712 1.828   53.120 1.00 21.02 ? 309 SER A C   1 
ATOM   1399 O O   . SER A 1 191 ? 44.487 2.090   54.306 1.00 20.67 ? 309 SER A O   1 
ATOM   1400 C CB  . SER A 1 191 ? 46.201 -0.073  52.474 1.00 20.22 ? 309 SER A CB  1 
ATOM   1401 O OG  . SER A 1 191 ? 46.957 0.242   53.635 1.00 21.50 ? 309 SER A OG  1 
ATOM   1402 N N   . GLY A 1 192 ? 44.946 2.759   52.198 1.00 21.55 ? 310 GLY A N   1 
ATOM   1403 C CA  . GLY A 1 192 ? 44.969 4.176   52.523 1.00 22.96 ? 310 GLY A CA  1 
ATOM   1404 C C   . GLY A 1 192 ? 43.623 4.730   52.962 1.00 23.40 ? 310 GLY A C   1 
ATOM   1405 O O   . GLY A 1 192 ? 43.557 5.719   53.693 1.00 23.69 ? 310 GLY A O   1 
ATOM   1406 N N   . ARG A 1 193 ? 42.548 4.083   52.531 1.00 23.78 ? 311 ARG A N   1 
ATOM   1407 C CA  . ARG A 1 193 ? 41.200 4.543   52.860 1.00 24.38 ? 311 ARG A CA  1 
ATOM   1408 C C   . ARG A 1 193 ? 40.561 3.731   53.974 1.00 24.08 ? 311 ARG A C   1 
ATOM   1409 O O   . ARG A 1 193 ? 39.436 4.012   54.386 1.00 24.24 ? 311 ARG A O   1 
ATOM   1410 C CB  . ARG A 1 193 ? 40.309 4.505   51.624 1.00 24.59 ? 311 ARG A CB  1 
ATOM   1411 C CG  . ARG A 1 193 ? 40.688 5.498   50.561 1.00 26.51 ? 311 ARG A CG  1 
ATOM   1412 C CD  . ARG A 1 193 ? 39.952 5.290   49.242 1.00 29.06 ? 311 ARG A CD  1 
ATOM   1413 N NE  . ARG A 1 193 ? 38.506 5.182   49.429 1.00 32.41 ? 311 ARG A NE  1 
ATOM   1414 C CZ  . ARG A 1 193 ? 37.635 5.064   48.430 1.00 34.16 ? 311 ARG A CZ  1 
ATOM   1415 N NH1 . ARG A 1 193 ? 38.064 5.043   47.177 1.00 34.83 ? 311 ARG A NH1 1 
ATOM   1416 N NH2 . ARG A 1 193 ? 36.336 4.973   48.680 1.00 34.60 ? 311 ARG A NH2 1 
ATOM   1417 N N   . GLY A 1 194 ? 41.269 2.710   54.443 1.00 23.87 ? 312 GLY A N   1 
ATOM   1418 C CA  . GLY A 1 194 ? 40.773 1.861   55.509 1.00 23.65 ? 312 GLY A CA  1 
ATOM   1419 C C   . GLY A 1 194 ? 39.525 1.080   55.151 1.00 23.69 ? 312 GLY A C   1 
ATOM   1420 O O   . GLY A 1 194 ? 38.655 0.865   55.998 1.00 23.74 ? 312 GLY A O   1 
ATOM   1421 N N   . LEU A 1 195 ? 39.422 0.669   53.890 1.00 23.23 ? 313 LEU A N   1 
ATOM   1422 C CA  . LEU A 1 195 ? 38.306 -0.151  53.441 1.00 23.00 ? 313 LEU A CA  1 
ATOM   1423 C C   . LEU A 1 195 ? 38.582 -1.601  53.842 1.00 22.65 ? 313 LEU A C   1 
ATOM   1424 O O   . LEU A 1 195 ? 39.007 -2.409  53.017 1.00 22.44 ? 313 LEU A O   1 
ATOM   1425 C CB  . LEU A 1 195 ? 38.146 -0.040  51.919 1.00 23.00 ? 313 LEU A CB  1 
ATOM   1426 C CG  . LEU A 1 195 ? 37.378 1.160   51.352 1.00 23.96 ? 313 LEU A CG  1 
ATOM   1427 C CD1 . LEU A 1 195 ? 37.477 2.375   52.250 1.00 24.77 ? 313 LEU A CD1 1 
ATOM   1428 C CD2 . LEU A 1 195 ? 37.844 1.485   49.934 1.00 24.14 ? 313 LEU A CD2 1 
ATOM   1429 N N   . LEU A 1 196 ? 38.328 -1.917  55.114 1.00 22.08 ? 314 LEU A N   1 
ATOM   1430 C CA  . LEU A 1 196 ? 38.649 -3.228  55.686 1.00 21.76 ? 314 LEU A CA  1 
ATOM   1431 C C   . LEU A 1 196 ? 38.231 -4.475  54.881 1.00 21.08 ? 314 LEU A C   1 
ATOM   1432 O O   . LEU A 1 196 ? 39.056 -5.339  54.646 1.00 20.81 ? 314 LEU A O   1 
ATOM   1433 C CB  . LEU A 1 196 ? 38.163 -3.335  57.138 1.00 21.80 ? 314 LEU A CB  1 
ATOM   1434 C CG  . LEU A 1 196 ? 38.650 -2.240  58.102 1.00 23.13 ? 314 LEU A CG  1 
ATOM   1435 C CD1 . LEU A 1 196 ? 38.314 -2.611  59.527 1.00 23.03 ? 314 LEU A CD1 1 
ATOM   1436 C CD2 . LEU A 1 196 ? 40.151 -1.972  57.954 1.00 23.50 ? 314 LEU A CD2 1 
ATOM   1437 N N   . PRO A 1 197 ? 36.959 -4.596  54.501 1.00 20.60 ? 315 PRO A N   1 
ATOM   1438 C CA  . PRO A 1 197 ? 36.510 -5.772  53.741 1.00 20.22 ? 315 PRO A CA  1 
ATOM   1439 C C   . PRO A 1 197 ? 37.307 -5.948  52.451 1.00 19.67 ? 315 PRO A C   1 
ATOM   1440 O O   . PRO A 1 197 ? 37.618 -7.081  52.067 1.00 19.53 ? 315 PRO A O   1 
ATOM   1441 C CB  . PRO A 1 197 ? 35.046 -5.451  53.430 1.00 20.43 ? 315 PRO A CB  1 
ATOM   1442 C CG  . PRO A 1 197 ? 34.640 -4.485  54.500 1.00 20.78 ? 315 PRO A CG  1 
ATOM   1443 C CD  . PRO A 1 197 ? 35.855 -3.656  54.765 1.00 20.94 ? 315 PRO A CD  1 
ATOM   1444 N N   . LEU A 1 198 ? 37.648 -4.836  51.803 1.00 18.92 ? 316 LEU A N   1 
ATOM   1445 C CA  . LEU A 1 198 ? 38.426 -4.886  50.571 1.00 18.49 ? 316 LEU A CA  1 
ATOM   1446 C C   . LEU A 1 198 ? 39.878 -5.269  50.838 1.00 17.60 ? 316 LEU A C   1 
ATOM   1447 O O   . LEU A 1 198 ? 40.477 -6.015  50.071 1.00 17.22 ? 316 LEU A O   1 
ATOM   1448 C CB  . LEU A 1 198 ? 38.350 -3.555  49.814 1.00 18.40 ? 316 LEU A CB  1 
ATOM   1449 C CG  . LEU A 1 198 ? 37.168 -3.425  48.837 1.00 19.75 ? 316 LEU A CG  1 
ATOM   1450 C CD1 . LEU A 1 198 ? 35.843 -3.515  49.568 1.00 21.54 ? 316 LEU A CD1 1 
ATOM   1451 C CD2 . LEU A 1 198 ? 37.252 -2.142  48.015 1.00 19.33 ? 316 LEU A CD2 1 
ATOM   1452 N N   . VAL A 1 199 ? 40.450 -4.741  51.914 1.00 16.93 ? 317 VAL A N   1 
ATOM   1453 C CA  . VAL A 1 199 ? 41.818 -5.083  52.261 1.00 16.11 ? 317 VAL A CA  1 
ATOM   1454 C C   . VAL A 1 199 ? 41.904 -6.590  52.489 1.00 15.85 ? 317 VAL A C   1 
ATOM   1455 O O   . VAL A 1 199 ? 42.800 -7.258  51.968 1.00 15.90 ? 317 VAL A O   1 
ATOM   1456 C CB  . VAL A 1 199 ? 42.315 -4.314  53.514 1.00 16.18 ? 317 VAL A CB  1 
ATOM   1457 C CG1 . VAL A 1 199 ? 43.743 -4.720  53.855 1.00 16.32 ? 317 VAL A CG1 1 
ATOM   1458 C CG2 . VAL A 1 199 ? 42.239 -2.808  53.280 1.00 15.73 ? 317 VAL A CG2 1 
ATOM   1459 N N   . ARG A 1 200 ? 40.948 -7.129  53.240 1.00 15.27 ? 318 ARG A N   1 
ATOM   1460 C CA  . ARG A 1 200 ? 40.930 -8.560  53.530 1.00 15.33 ? 318 ARG A CA  1 
ATOM   1461 C C   . ARG A 1 200 ? 40.848 -9.386  52.253 1.00 14.99 ? 318 ARG A C   1 
ATOM   1462 O O   . ARG A 1 200 ? 41.578 -10.369 52.097 1.00 15.03 ? 318 ARG A O   1 
ATOM   1463 C CB  . ARG A 1 200 ? 39.755 -8.927  54.441 1.00 15.81 ? 318 ARG A CB  1 
ATOM   1464 C CG  . ARG A 1 200 ? 39.942 -8.545  55.913 1.00 17.81 ? 318 ARG A CG  1 
ATOM   1465 C CD  . ARG A 1 200 ? 38.715 -8.810  56.786 1.00 21.17 ? 318 ARG A CD  1 
ATOM   1466 N NE  . ARG A 1 200 ? 38.851 -8.211  58.111 1.00 22.96 ? 318 ARG A NE  1 
ATOM   1467 C CZ  . ARG A 1 200 ? 38.061 -7.262  58.591 1.00 23.93 ? 318 ARG A CZ  1 
ATOM   1468 N NH1 . ARG A 1 200 ? 37.048 -6.793  57.863 1.00 25.14 ? 318 ARG A NH1 1 
ATOM   1469 N NH2 . ARG A 1 200 ? 38.284 -6.774  59.804 1.00 24.19 ? 318 ARG A NH2 1 
ATOM   1470 N N   . THR A 1 201 ? 39.947 -8.994  51.358 1.00 14.24 ? 319 THR A N   1 
ATOM   1471 C CA  . THR A 1 201 ? 39.745 -9.717  50.103 1.00 14.62 ? 319 THR A CA  1 
ATOM   1472 C C   . THR A 1 201 ? 40.987 -9.681  49.199 1.00 13.33 ? 319 THR A C   1 
ATOM   1473 O O   . THR A 1 201 ? 41.423 -10.714 48.699 1.00 13.11 ? 319 THR A O   1 
ATOM   1474 C CB  . THR A 1 201 ? 38.508 -9.176  49.368 1.00 14.86 ? 319 THR A CB  1 
ATOM   1475 O OG1 . THR A 1 201 ? 37.323 -9.698  49.987 1.00 18.12 ? 319 THR A OG1 1 
ATOM   1476 C CG2 . THR A 1 201 ? 38.432 -9.730  47.956 1.00 15.91 ? 319 THR A CG2 1 
ATOM   1477 N N   . LEU A 1 202 ? 41.547 -8.493  48.991 1.00 12.67 ? 320 LEU A N   1 
ATOM   1478 C CA  . LEU A 1 202 ? 42.756 -8.356  48.169 1.00 12.73 ? 320 LEU A CA  1 
ATOM   1479 C C   . LEU A 1 202 ? 43.954 -9.158  48.717 1.00 12.65 ? 320 LEU A C   1 
ATOM   1480 O O   . LEU A 1 202 ? 44.664 -9.807  47.963 1.00 12.36 ? 320 LEU A O   1 
ATOM   1481 C CB  . LEU A 1 202 ? 43.143 -6.880  48.005 1.00 12.30 ? 320 LEU A CB  1 
ATOM   1482 C CG  . LEU A 1 202 ? 42.141 -5.973  47.279 1.00 13.46 ? 320 LEU A CG  1 
ATOM   1483 C CD1 . LEU A 1 202 ? 42.490 -4.498  47.469 1.00 12.69 ? 320 LEU A CD1 1 
ATOM   1484 C CD2 . LEU A 1 202 ? 42.060 -6.322  45.792 1.00 12.67 ? 320 LEU A CD2 1 
ATOM   1485 N N   . VAL A 1 203 ? 44.185 -9.093  50.025 1.00 12.83 ? 321 VAL A N   1 
ATOM   1486 C CA  . VAL A 1 203 ? 45.321 -9.798  50.629 1.00 13.43 ? 321 VAL A CA  1 
ATOM   1487 C C   . VAL A 1 203 ? 45.192 -11.311 50.483 1.00 13.77 ? 321 VAL A C   1 
ATOM   1488 O O   . VAL A 1 203 ? 46.151 -11.998 50.142 1.00 13.74 ? 321 VAL A O   1 
ATOM   1489 C CB  . VAL A 1 203 ? 45.497 -9.442  52.134 1.00 13.34 ? 321 VAL A CB  1 
ATOM   1490 C CG1 . VAL A 1 203 ? 46.518 -10.377 52.796 1.00 14.76 ? 321 VAL A CG1 1 
ATOM   1491 C CG2 . VAL A 1 203 ? 45.924 -7.992  52.295 1.00 13.93 ? 321 VAL A CG2 1 
ATOM   1492 N N   . ARG A 1 204 ? 44.002 -11.830 50.721 1.00 14.64 ? 322 ARG A N   1 
ATOM   1493 C CA  . ARG A 1 204 ? 43.798 -13.258 50.596 1.00 15.80 ? 322 ARG A CA  1 
ATOM   1494 C C   . ARG A 1 204 ? 43.921 -13.701 49.144 1.00 15.24 ? 322 ARG A C   1 
ATOM   1495 O O   . ARG A 1 204 ? 44.231 -14.853 48.872 1.00 15.01 ? 322 ARG A O   1 
ATOM   1496 C CB  . ARG A 1 204 ? 42.438 -13.657 51.132 1.00 16.84 ? 322 ARG A CB  1 
ATOM   1497 C CG  . ARG A 1 204 ? 42.370 -13.689 52.634 1.00 20.58 ? 322 ARG A CG  1 
ATOM   1498 C CD  . ARG A 1 204 ? 41.120 -14.344 53.146 1.00 27.12 ? 322 ARG A CD  1 
ATOM   1499 N NE  . ARG A 1 204 ? 41.100 -14.406 54.599 1.00 32.19 ? 322 ARG A NE  1 
ATOM   1500 C CZ  . ARG A 1 204 ? 40.059 -14.811 55.300 1.00 34.63 ? 322 ARG A CZ  1 
ATOM   1501 N NH1 . ARG A 1 204 ? 38.955 -15.186 54.675 1.00 35.24 ? 322 ARG A NH1 1 
ATOM   1502 N NH2 . ARG A 1 204 ? 40.117 -14.842 56.626 1.00 36.87 ? 322 ARG A NH2 1 
ATOM   1503 N N   . SER A 1 205 ? 43.679 -12.776 48.222 1.00 14.86 ? 323 SER A N   1 
ATOM   1504 C CA  . SER A 1 205 ? 43.747 -13.080 46.796 1.00 15.22 ? 323 SER A CA  1 
ATOM   1505 C C   . SER A 1 205 ? 45.135 -12.865 46.230 1.00 15.08 ? 323 SER A C   1 
ATOM   1506 O O   . SER A 1 205 ? 45.333 -12.945 45.013 1.00 15.38 ? 323 SER A O   1 
ATOM   1507 C CB  . SER A 1 205 ? 42.734 -12.246 46.020 1.00 15.35 ? 323 SER A CB  1 
ATOM   1508 O OG  . SER A 1 205 ? 41.423 -12.580 46.420 1.00 17.29 ? 323 SER A OG  1 
ATOM   1509 N N   . GLY A 1 206 ? 46.086 -12.545 47.100 1.00 14.49 ? 324 GLY A N   1 
ATOM   1510 C CA  . GLY A 1 206 ? 47.469 -12.425 46.685 1.00 14.52 ? 324 GLY A CA  1 
ATOM   1511 C C   . GLY A 1 206 ? 48.045 -11.030 46.495 1.00 15.09 ? 324 GLY A C   1 
ATOM   1512 O O   . GLY A 1 206 ? 49.132 -10.896 45.948 1.00 15.18 ? 324 GLY A O   1 
ATOM   1513 N N   . ALA A 1 207 ? 47.353 -9.995  46.958 1.00 15.27 ? 325 ALA A N   1 
ATOM   1514 C CA  . ALA A 1 207 ? 47.876 -8.631  46.796 1.00 16.15 ? 325 ALA A CA  1 
ATOM   1515 C C   . ALA A 1 207 ? 49.259 -8.469  47.445 1.00 16.85 ? 325 ALA A C   1 
ATOM   1516 O O   . ALA A 1 207 ? 49.488 -8.935  48.557 1.00 16.19 ? 325 ALA A O   1 
ATOM   1517 C CB  . ALA A 1 207 ? 46.910 -7.619  47.348 1.00 15.89 ? 325 ALA A CB  1 
ATOM   1518 N N   . ASP A 1 208 ? 50.166 -7.799  46.734 1.00 17.70 ? 326 ASP A N   1 
ATOM   1519 C CA  . ASP A 1 208 ? 51.544 -7.579  47.196 1.00 19.01 ? 326 ASP A CA  1 
ATOM   1520 C C   . ASP A 1 208 ? 51.636 -6.315  48.050 1.00 19.40 ? 326 ASP A C   1 
ATOM   1521 O O   . ASP A 1 208 ? 51.481 -5.202  47.544 1.00 19.31 ? 326 ASP A O   1 
ATOM   1522 C CB  . ASP A 1 208 ? 52.473 -7.463  45.982 1.00 19.56 ? 326 ASP A CB  1 
ATOM   1523 C CG  . ASP A 1 208 ? 53.941 -7.281  46.363 1.00 21.66 ? 326 ASP A CG  1 
ATOM   1524 O OD1 . ASP A 1 208 ? 54.254 -7.129  47.565 1.00 24.08 ? 326 ASP A OD1 1 
ATOM   1525 O OD2 . ASP A 1 208 ? 54.854 -7.283  45.507 1.00 24.34 ? 326 ASP A OD2 1 
ATOM   1526 N N   . SER A 1 209 ? 51.889 -6.485  49.344 1.00 20.03 ? 327 SER A N   1 
ATOM   1527 C CA  . SER A 1 209 ? 51.969 -5.347  50.267 1.00 21.59 ? 327 SER A CA  1 
ATOM   1528 C C   . SER A 1 209 ? 53.341 -4.654  50.316 1.00 22.14 ? 327 SER A C   1 
ATOM   1529 O O   . SER A 1 209 ? 53.531 -3.708  51.083 1.00 22.31 ? 327 SER A O   1 
ATOM   1530 C CB  . SER A 1 209 ? 51.560 -5.772  51.683 1.00 21.33 ? 327 SER A CB  1 
ATOM   1531 O OG  . SER A 1 209 ? 52.435 -6.769  52.178 1.00 22.90 ? 327 SER A OG  1 
ATOM   1532 N N   . SER A 1 210 ? 54.286 -5.123  49.510 1.00 23.30 ? 328 SER A N   1 
ATOM   1533 C CA  . SER A 1 210 ? 55.627 -4.530  49.474 1.00 24.31 ? 328 SER A CA  1 
ATOM   1534 C C   . SER A 1 210 ? 55.833 -3.696  48.212 1.00 24.35 ? 328 SER A C   1 
ATOM   1535 O O   . SER A 1 210 ? 56.900 -3.123  47.998 1.00 24.83 ? 328 SER A O   1 
ATOM   1536 C CB  . SER A 1 210 ? 56.693 -5.619  49.539 1.00 24.43 ? 328 SER A CB  1 
ATOM   1537 O OG  . SER A 1 210 ? 56.795 -6.296  48.292 1.00 26.30 ? 328 SER A OG  1 
ATOM   1538 N N   . LEU A 1 211 ? 54.806 -3.635  47.376 1.00 24.38 ? 329 LEU A N   1 
ATOM   1539 C CA  . LEU A 1 211 ? 54.887 -2.904  46.120 1.00 24.56 ? 329 LEU A CA  1 
ATOM   1540 C C   . LEU A 1 211 ? 54.974 -1.398  46.363 1.00 24.60 ? 329 LEU A C   1 
ATOM   1541 O O   . LEU A 1 211 ? 54.116 -0.820  47.025 1.00 24.15 ? 329 LEU A O   1 
ATOM   1542 C CB  . LEU A 1 211 ? 53.673 -3.228  45.258 1.00 24.54 ? 329 LEU A CB  1 
ATOM   1543 C CG  . LEU A 1 211 ? 53.695 -2.702  43.832 1.00 25.63 ? 329 LEU A CG  1 
ATOM   1544 C CD1 . LEU A 1 211 ? 54.927 -3.205  43.086 1.00 24.98 ? 329 LEU A CD1 1 
ATOM   1545 C CD2 . LEU A 1 211 ? 52.423 -3.122  43.127 1.00 26.70 ? 329 LEU A CD2 1 
ATOM   1546 N N   . LYS A 1 212 ? 56.018 -0.771  45.831 1.00 25.08 ? 330 LYS A N   1 
ATOM   1547 C CA  . LYS A 1 212 ? 56.231 0.667   46.024 1.00 25.92 ? 330 LYS A CA  1 
ATOM   1548 C C   . LYS A 1 212 ? 55.633 1.501   44.897 1.00 25.76 ? 330 LYS A C   1 
ATOM   1549 O O   . LYS A 1 212 ? 55.665 1.095   43.735 1.00 26.39 ? 330 LYS A O   1 
ATOM   1550 C CB  . LYS A 1 212 ? 57.726 0.975   46.133 1.00 26.23 ? 330 LYS A CB  1 
ATOM   1551 C CG  . LYS A 1 212 ? 58.464 0.177   47.189 1.00 27.73 ? 330 LYS A CG  1 
ATOM   1552 C CD  . LYS A 1 212 ? 59.953 0.536   47.200 1.00 30.03 ? 330 LYS A CD  1 
ATOM   1553 C CE  . LYS A 1 212 ? 60.178 1.957   47.668 1.00 31.16 ? 330 LYS A CE  1 
ATOM   1554 N NZ  . LYS A 1 212 ? 59.833 2.132   49.114 1.00 32.16 ? 330 LYS A NZ  1 
ATOM   1555 N N   . ASN A 1 213 ? 55.055 2.651   45.241 1.00 25.45 ? 331 ASN A N   1 
ATOM   1556 C CA  . ASN A 1 213 ? 54.589 3.586   44.222 1.00 25.17 ? 331 ASN A CA  1 
ATOM   1557 C C   . ASN A 1 213 ? 55.650 4.646   43.946 1.00 25.22 ? 331 ASN A C   1 
ATOM   1558 O O   . ASN A 1 213 ? 56.775 4.543   44.442 1.00 24.85 ? 331 ASN A O   1 
ATOM   1559 C CB  . ASN A 1 213 ? 53.223 4.210   44.559 1.00 24.66 ? 331 ASN A CB  1 
ATOM   1560 C CG  . ASN A 1 213 ? 53.233 5.043   45.852 1.00 23.67 ? 331 ASN A CG  1 
ATOM   1561 O OD1 . ASN A 1 213 ? 54.269 5.525   46.305 1.00 22.02 ? 331 ASN A OD1 1 
ATOM   1562 N ND2 . ASN A 1 213 ? 52.058 5.221   46.430 1.00 22.39 ? 331 ASN A ND2 1 
ATOM   1563 N N   . CYS A 1 214 ? 55.299 5.653   43.154 1.00 25.60 ? 332 CYS A N   1 
ATOM   1564 C CA  . CYS A 1 214 ? 56.272 6.681   42.765 1.00 26.23 ? 332 CYS A CA  1 
ATOM   1565 C C   . CYS A 1 214 ? 56.734 7.509   43.957 1.00 25.55 ? 332 CYS A C   1 
ATOM   1566 O O   . CYS A 1 214 ? 57.803 8.121   43.923 1.00 25.66 ? 332 CYS A O   1 
ATOM   1567 C CB  . CYS A 1 214 ? 55.695 7.597   41.688 1.00 26.40 ? 332 CYS A CB  1 
ATOM   1568 S SG  . CYS A 1 214 ? 54.195 8.469   42.172 1.00 30.29 ? 332 CYS A SG  1 
ATOM   1569 N N   . HIS A 1 215 ? 55.923 7.532   45.006 1.00 25.11 ? 333 HIS A N   1 
ATOM   1570 C CA  . HIS A 1 215 ? 56.267 8.266   46.217 1.00 24.88 ? 333 HIS A CA  1 
ATOM   1571 C C   . HIS A 1 215 ? 57.082 7.362   47.137 1.00 24.41 ? 333 HIS A C   1 
ATOM   1572 O O   . HIS A 1 215 ? 57.471 7.763   48.236 1.00 24.64 ? 333 HIS A O   1 
ATOM   1573 C CB  . HIS A 1 215 ? 54.992 8.766   46.918 1.00 24.70 ? 333 HIS A CB  1 
ATOM   1574 C CG  . HIS A 1 215 ? 55.247 9.688   48.074 1.00 25.85 ? 333 HIS A CG  1 
ATOM   1575 N ND1 . HIS A 1 215 ? 54.643 9.523   49.304 1.00 26.69 ? 333 HIS A ND1 1 
ATOM   1576 C CD2 . HIS A 1 215 ? 56.024 10.792  48.184 1.00 24.93 ? 333 HIS A CD2 1 
ATOM   1577 C CE1 . HIS A 1 215 ? 55.042 10.482  50.122 1.00 26.42 ? 333 HIS A CE1 1 
ATOM   1578 N NE2 . HIS A 1 215 ? 55.884 11.262  49.468 1.00 26.32 ? 333 HIS A NE2 1 
ATOM   1579 N N   . ASN A 1 216 ? 57.345 6.143   46.673 1.00 23.97 ? 334 ASN A N   1 
ATOM   1580 C CA  . ASN A 1 216 ? 58.108 5.156   47.443 1.00 23.95 ? 334 ASN A CA  1 
ATOM   1581 C C   . ASN A 1 216 ? 57.308 4.573   48.608 1.00 23.11 ? 334 ASN A C   1 
ATOM   1582 O O   . ASN A 1 216 ? 57.870 3.977   49.518 1.00 23.18 ? 334 ASN A O   1 
ATOM   1583 C CB  . ASN A 1 216 ? 59.433 5.747   47.953 1.00 24.37 ? 334 ASN A CB  1 
ATOM   1584 C CG  . ASN A 1 216 ? 60.358 6.194   46.824 1.00 26.38 ? 334 ASN A CG  1 
ATOM   1585 O OD1 . ASN A 1 216 ? 61.288 6.981   47.040 1.00 28.78 ? 334 ASN A OD1 1 
ATOM   1586 N ND2 . ASN A 1 216 ? 60.112 5.692   45.621 1.00 29.30 ? 334 ASN A ND2 1 
ATOM   1587 N N   . ASP A 1 217 ? 55.994 4.745   48.566 1.00 22.70 ? 335 ASP A N   1 
ATOM   1588 C CA  . ASP A 1 217 ? 55.101 4.216   49.595 1.00 22.18 ? 335 ASP A CA  1 
ATOM   1589 C C   . ASP A 1 217 ? 54.631 2.801   49.244 1.00 22.10 ? 335 ASP A C   1 
ATOM   1590 O O   . ASP A 1 217 ? 54.368 2.507   48.077 1.00 22.05 ? 335 ASP A O   1 
ATOM   1591 C CB  . ASP A 1 217 ? 53.859 5.100   49.698 1.00 22.34 ? 335 ASP A CB  1 
ATOM   1592 C CG  . ASP A 1 217 ? 54.022 6.246   50.665 1.00 22.30 ? 335 ASP A CG  1 
ATOM   1593 O OD1 . ASP A 1 217 ? 55.020 6.282   51.413 1.00 23.16 ? 335 ASP A OD1 1 
ATOM   1594 O OD2 . ASP A 1 217 ? 53.178 7.160   50.749 1.00 23.13 ? 335 ASP A OD2 1 
ATOM   1595 N N   . THR A 1 218 ? 54.531 1.929   50.249 1.00 21.72 ? 336 THR A N   1 
ATOM   1596 C CA  . THR A 1 218 ? 53.913 0.613   50.062 1.00 21.27 ? 336 THR A CA  1 
ATOM   1597 C C   . THR A 1 218 ? 52.541 0.669   50.720 1.00 21.20 ? 336 THR A C   1 
ATOM   1598 O O   . THR A 1 218 ? 52.272 1.569   51.513 1.00 20.45 ? 336 THR A O   1 
ATOM   1599 C CB  . THR A 1 218 ? 54.739 -0.505  50.734 1.00 21.16 ? 336 THR A CB  1 
ATOM   1600 O OG1 . THR A 1 218 ? 54.884 -0.221  52.135 1.00 20.46 ? 336 THR A OG1 1 
ATOM   1601 C CG2 . THR A 1 218 ? 56.162 -0.543  50.207 1.00 21.32 ? 336 THR A CG2 1 
ATOM   1602 N N   . PRO A 1 219 ? 51.670 -0.286  50.414 1.00 21.24 ? 337 PRO A N   1 
ATOM   1603 C CA  . PRO A 1 219 ? 50.351 -0.318  51.049 1.00 21.65 ? 337 PRO A CA  1 
ATOM   1604 C C   . PRO A 1 219 ? 50.494 -0.343  52.573 1.00 22.38 ? 337 PRO A C   1 
ATOM   1605 O O   . PRO A 1 219 ? 49.647 0.189   53.295 1.00 22.58 ? 337 PRO A O   1 
ATOM   1606 C CB  . PRO A 1 219 ? 49.748 -1.626  50.531 1.00 21.75 ? 337 PRO A CB  1 
ATOM   1607 C CG  . PRO A 1 219 ? 50.434 -1.849  49.222 1.00 21.29 ? 337 PRO A CG  1 
ATOM   1608 C CD  . PRO A 1 219 ? 51.851 -1.385  49.448 1.00 21.46 ? 337 PRO A CD  1 
ATOM   1609 N N   . LEU A 1 220 ? 51.569 -0.951  53.058 1.00 22.87 ? 338 LEU A N   1 
ATOM   1610 C CA  . LEU A 1 220 ? 51.813 -0.993  54.489 1.00 23.86 ? 338 LEU A CA  1 
ATOM   1611 C C   . LEU A 1 220 ? 52.041 0.426   55.026 1.00 23.86 ? 338 LEU A C   1 
ATOM   1612 O O   . LEU A 1 220 ? 51.477 0.812   56.054 1.00 24.03 ? 338 LEU A O   1 
ATOM   1613 C CB  . LEU A 1 220 ? 53.016 -1.890  54.804 1.00 24.01 ? 338 LEU A CB  1 
ATOM   1614 C CG  . LEU A 1 220 ? 52.789 -2.951  55.882 1.00 26.13 ? 338 LEU A CG  1 
ATOM   1615 C CD1 . LEU A 1 220 ? 54.124 -3.441  56.450 1.00 27.46 ? 338 LEU A CD1 1 
ATOM   1616 C CD2 . LEU A 1 220 ? 51.896 -2.420  56.991 1.00 27.34 ? 338 LEU A CD2 1 
ATOM   1617 N N   . MET A 1 221 ? 52.836 1.212   54.305 1.00 23.91 ? 339 MET A N   1 
ATOM   1618 C CA  . MET A 1 221 ? 53.181 2.566   54.740 1.00 24.42 ? 339 MET A CA  1 
ATOM   1619 C C   . MET A 1 221 ? 52.028 3.566   54.707 1.00 24.83 ? 339 MET A C   1 
ATOM   1620 O O   . MET A 1 221 ? 52.086 4.591   55.378 1.00 24.83 ? 339 MET A O   1 
ATOM   1621 C CB  . MET A 1 221 ? 54.361 3.102   53.939 1.00 24.29 ? 339 MET A CB  1 
ATOM   1622 C CG  . MET A 1 221 ? 55.625 2.301   54.131 1.00 24.23 ? 339 MET A CG  1 
ATOM   1623 S SD  . MET A 1 221 ? 56.814 2.651   52.861 1.00 23.89 ? 339 MET A SD  1 
ATOM   1624 C CE  . MET A 1 221 ? 57.006 4.414   53.078 1.00 25.43 ? 339 MET A CE  1 
ATOM   1625 N N   . VAL A 1 222 ? 50.992 3.283   53.921 1.00 25.10 ? 340 VAL A N   1 
ATOM   1626 C CA  . VAL A 1 222 ? 49.848 4.187   53.850 1.00 25.70 ? 340 VAL A CA  1 
ATOM   1627 C C   . VAL A 1 222 ? 48.660 3.678   54.668 1.00 25.98 ? 340 VAL A C   1 
ATOM   1628 O O   . VAL A 1 222 ? 47.596 4.277   54.646 1.00 26.14 ? 340 VAL A O   1 
ATOM   1629 C CB  . VAL A 1 222 ? 49.393 4.449   52.395 1.00 25.60 ? 340 VAL A CB  1 
ATOM   1630 C CG1 . VAL A 1 222 ? 50.540 5.007   51.560 1.00 25.69 ? 340 VAL A CG1 1 
ATOM   1631 C CG2 . VAL A 1 222 ? 48.813 3.178   51.765 1.00 26.16 ? 340 VAL A CG2 1 
ATOM   1632 N N   . ALA A 1 223 ? 48.854 2.580   55.389 1.00 26.61 ? 341 ALA A N   1 
ATOM   1633 C CA  . ALA A 1 223 ? 47.782 1.992   56.185 1.00 27.38 ? 341 ALA A CA  1 
ATOM   1634 C C   . ALA A 1 223 ? 47.108 3.061   57.029 1.00 28.33 ? 341 ALA A C   1 
ATOM   1635 O O   . ALA A 1 223 ? 47.771 3.797   57.762 1.00 28.36 ? 341 ALA A O   1 
ATOM   1636 C CB  . ALA A 1 223 ? 48.318 0.886   57.056 1.00 27.32 ? 341 ALA A CB  1 
ATOM   1637 N N   . ARG A 1 224 ? 45.789 3.145   56.933 1.00 28.98 ? 342 ARG A N   1 
ATOM   1638 C CA  . ARG A 1 224 ? 45.059 4.188   57.638 1.00 29.92 ? 342 ARG A CA  1 
ATOM   1639 C C   . ARG A 1 224 ? 44.973 3.980   59.153 1.00 29.81 ? 342 ARG A C   1 
ATOM   1640 O O   . ARG A 1 224 ? 44.855 4.944   59.908 1.00 30.28 ? 342 ARG A O   1 
ATOM   1641 C CB  . ARG A 1 224 ? 43.663 4.356   57.050 1.00 30.25 ? 342 ARG A CB  1 
ATOM   1642 C CG  . ARG A 1 224 ? 43.049 5.700   57.352 1.00 32.21 ? 342 ARG A CG  1 
ATOM   1643 C CD  . ARG A 1 224 ? 41.857 6.041   56.491 1.00 35.87 ? 342 ARG A CD  1 
ATOM   1644 N NE  . ARG A 1 224 ? 41.487 7.447   56.612 1.00 38.20 ? 342 ARG A NE  1 
ATOM   1645 C CZ  . ARG A 1 224 ? 40.258 7.904   56.432 1.00 39.58 ? 342 ARG A CZ  1 
ATOM   1646 N NH1 . ARG A 1 224 ? 39.280 7.065   56.122 1.00 40.57 ? 342 ARG A NH1 1 
ATOM   1647 N NH2 . ARG A 1 224 ? 40.003 9.201   56.561 1.00 40.40 ? 342 ARG A NH2 1 
ATOM   1648 N N   . SER A 1 225 ? 45.031 2.727   59.592 1.00 29.65 ? 343 SER A N   1 
ATOM   1649 C CA  . SER A 1 225 ? 44.897 2.412   61.014 1.00 29.20 ? 343 SER A CA  1 
ATOM   1650 C C   . SER A 1 225 ? 45.596 1.112   61.380 1.00 28.57 ? 343 SER A C   1 
ATOM   1651 O O   . SER A 1 225 ? 46.062 0.378   60.515 1.00 28.37 ? 343 SER A O   1 
ATOM   1652 C CB  . SER A 1 225 ? 43.421 2.301   61.389 1.00 29.58 ? 343 SER A CB  1 
ATOM   1653 O OG  . SER A 1 225 ? 42.843 1.160   60.776 1.00 30.17 ? 343 SER A OG  1 
ATOM   1654 N N   . ARG A 1 226 ? 45.639 0.819   62.673 1.00 23.95 ? 344 ARG A N   1 
ATOM   1655 C CA  . ARG A 1 226 ? 46.281 -0.393  63.161 1.00 20.35 ? 344 ARG A CA  1 
ATOM   1656 C C   . ARG A 1 226 ? 45.543 -1.668  62.722 1.00 18.61 ? 344 ARG A C   1 
ATOM   1657 O O   . ARG A 1 226 ? 46.147 -2.730  62.596 1.00 17.67 ? 344 ARG A O   1 
ATOM   1658 C CB  . ARG A 1 226 ? 46.341 -0.374  64.700 1.00 19.95 ? 344 ARG A CB  1 
ATOM   1659 C CG  . ARG A 1 226 ? 47.437 0.539   65.248 1.00 20.39 ? 344 ARG A CG  1 
ATOM   1660 C CD  . ARG A 1 226 ? 47.346 1.967   64.712 1.00 20.95 ? 344 ARG A CD  1 
ATOM   1661 N NE  . ARG A 1 226 ? 48.664 2.591   64.517 1.00 22.31 ? 344 ARG A NE  1 
ATOM   1662 C CZ  . ARG A 1 226 ? 49.078 3.113   63.355 1.00 21.58 ? 344 ARG A CZ  1 
ATOM   1663 N NH1 . ARG A 1 226 ? 48.234 3.276   62.331 1.00 22.21 ? 344 ARG A NH1 1 
ATOM   1664 N NH2 . ARG A 1 226 ? 50.338 3.509   63.123 1.00 21.90 ? 344 ARG A NH2 1 
ATOM   1665 N N   . ARG A 1 227 ? 44.237 -1.554  62.495 1.00 19.29 ? 345 ARG A N   1 
ATOM   1666 C CA  . ARG A 1 227 ? 43.443 -2.693  62.033 1.00 20.49 ? 345 ARG A CA  1 
ATOM   1667 C C   . ARG A 1 227 ? 43.878 -3.109  60.630 1.00 18.94 ? 345 ARG A C   1 
ATOM   1668 O O   . ARG A 1 227 ? 43.911 -4.290  60.308 1.00 20.31 ? 345 ARG A O   1 
ATOM   1669 C CB  . ARG A 1 227 ? 41.957 -2.320  62.001 1.00 19.70 ? 345 ARG A CB  1 
ATOM   1670 C CG  . ARG A 1 227 ? 41.039 -3.529  61.829 1.00 20.91 ? 345 ARG A CG  1 
ATOM   1671 C CD  . ARG A 1 227 ? 40.728 -4.237  63.146 1.00 21.51 ? 345 ARG A CD  1 
ATOM   1672 N NE  . ARG A 1 227 ? 39.295 -4.516  63.324 1.00 23.35 ? 345 ARG A NE  1 
ATOM   1673 C CZ  . ARG A 1 227 ? 38.810 -5.688  63.753 1.00 20.91 ? 345 ARG A CZ  1 
ATOM   1674 N NH1 . ARG A 1 227 ? 39.447 -6.395  64.693 1.00 23.33 ? 345 ARG A NH1 1 
ATOM   1675 N NH2 . ARG A 1 227 ? 37.677 -6.241  63.296 1.00 23.15 ? 345 ARG A NH2 1 
ATOM   1676 N N   . VAL A 1 228 ? 44.206 -2.129  59.798 1.00 24.57 ? 346 VAL A N   1 
ATOM   1677 C CA  . VAL A 1 228 ? 44.681 -2.404  58.444 1.00 24.17 ? 346 VAL A CA  1 
ATOM   1678 C C   . VAL A 1 228 ? 46.040 -3.083  58.489 1.00 24.21 ? 346 VAL A C   1 
ATOM   1679 O O   . VAL A 1 228 ? 46.271 -4.088  57.811 1.00 23.46 ? 346 VAL A O   1 
ATOM   1680 C CB  . VAL A 1 228 ? 44.773 -1.119  57.602 1.00 24.24 ? 346 VAL A CB  1 
ATOM   1681 C CG1 . VAL A 1 228 ? 45.505 -1.387  56.282 1.00 24.34 ? 346 VAL A CG1 1 
ATOM   1682 C CG2 . VAL A 1 228 ? 43.393 -0.565  57.338 1.00 23.95 ? 346 VAL A CG2 1 
ATOM   1683 N N   . ILE A 1 229 ? 46.941 -2.540  59.303 1.00 24.42 ? 347 ILE A N   1 
ATOM   1684 C CA  . ILE A 1 229 ? 48.272 -3.114  59.443 1.00 25.26 ? 347 ILE A CA  1 
ATOM   1685 C C   . ILE A 1 229 ? 48.164 -4.581  59.840 1.00 25.17 ? 347 ILE A C   1 
ATOM   1686 O O   . ILE A 1 229 ? 48.860 -5.443  59.298 1.00 24.70 ? 347 ILE A O   1 
ATOM   1687 C CB  . ILE A 1 229 ? 49.069 -2.354  60.510 1.00 25.48 ? 347 ILE A CB  1 
ATOM   1688 C CG1 . ILE A 1 229 ? 48.873 -0.843  60.355 1.00 26.70 ? 347 ILE A CG1 1 
ATOM   1689 C CG2 . ILE A 1 229 ? 50.539 -2.758  60.464 1.00 26.42 ? 347 ILE A CG2 1 
ATOM   1690 C CD1 . ILE A 1 229 ? 50.061 -0.122  59.786 1.00 29.22 ? 347 ILE A CD1 1 
ATOM   1691 N N   . ASP A 1 230 ? 47.270 -4.852  60.786 1.00 22.35 ? 348 ASP A N   1 
ATOM   1692 C CA  . ASP A 1 230 ? 47.053 -6.206  61.289 1.00 20.67 ? 348 ASP A CA  1 
ATOM   1693 C C   . ASP A 1 230 ? 46.678 -7.163  60.168 1.00 21.12 ? 348 ASP A C   1 
ATOM   1694 O O   . ASP A 1 230 ? 47.157 -8.294  60.120 1.00 20.80 ? 348 ASP A O   1 
ATOM   1695 C CB  . ASP A 1 230 ? 45.925 -6.199  62.334 1.00 19.06 ? 348 ASP A CB  1 
ATOM   1696 C CG  . ASP A 1 230 ? 46.407 -5.840  63.740 1.00 20.96 ? 348 ASP A CG  1 
ATOM   1697 O OD1 . ASP A 1 230 ? 47.662 -5.670  63.964 1.00 23.83 ? 348 ASP A OD1 1 
ATOM   1698 O OD2 . ASP A 1 230 ? 45.559 -5.713  64.698 1.00 25.00 ? 348 ASP A OD2 1 
ATOM   1699 N N   . ILE A 1 231 ? 45.807 -6.706  59.276 1.00 26.57 ? 349 ILE A N   1 
ATOM   1700 C CA  . ILE A 1 231 ? 45.378 -7.517  58.142 1.00 27.23 ? 349 ILE A CA  1 
ATOM   1701 C C   . ILE A 1 231 ? 46.533 -7.738  57.159 1.00 27.94 ? 349 ILE A C   1 
ATOM   1702 O O   . ILE A 1 231 ? 46.782 -8.864  56.727 1.00 28.13 ? 349 ILE A O   1 
ATOM   1703 C CB  . ILE A 1 231 ? 44.165 -6.864  57.444 1.00 27.08 ? 349 ILE A CB  1 
ATOM   1704 C CG1 . ILE A 1 231 ? 42.962 -6.864  58.391 1.00 26.88 ? 349 ILE A CG1 1 
ATOM   1705 C CG2 . ILE A 1 231 ? 43.832 -7.597  56.154 1.00 26.58 ? 349 ILE A CG2 1 
ATOM   1706 C CD1 . ILE A 1 231 ? 41.928 -5.792  58.098 1.00 28.39 ? 349 ILE A CD1 1 
ATOM   1707 N N   . LEU A 1 232 ? 47.253 -6.665  56.837 1.00 28.91 ? 350 LEU A N   1 
ATOM   1708 C CA  . LEU A 1 232 ? 48.379 -6.740  55.898 1.00 30.06 ? 350 LEU A CA  1 
ATOM   1709 C C   . LEU A 1 232 ? 49.472 -7.700  56.346 1.00 31.07 ? 350 LEU A C   1 
ATOM   1710 O O   . LEU A 1 232 ? 50.086 -8.382  55.523 1.00 31.22 ? 350 LEU A O   1 
ATOM   1711 C CB  . LEU A 1 232 ? 48.983 -5.355  55.672 1.00 29.49 ? 350 LEU A CB  1 
ATOM   1712 C CG  . LEU A 1 232 ? 48.110 -4.378  54.890 1.00 29.62 ? 350 LEU A CG  1 
ATOM   1713 C CD1 . LEU A 1 232 ? 48.811 -3.034  54.743 1.00 28.99 ? 350 LEU A CD1 1 
ATOM   1714 C CD2 . LEU A 1 232 ? 47.767 -4.961  53.528 1.00 29.30 ? 350 LEU A CD2 1 
ATOM   1715 N N   . ARG A 1 233 ? 49.707 -7.752  57.653 1.00 32.46 ? 351 ARG A N   1 
ATOM   1716 C CA  . ARG A 1 233 ? 50.772 -8.577  58.208 1.00 34.10 ? 351 ARG A CA  1 
ATOM   1717 C C   . ARG A 1 233 ? 50.328 -10.001 58.529 1.00 34.74 ? 351 ARG A C   1 
ATOM   1718 O O   . ARG A 1 233 ? 51.145 -10.842 58.900 1.00 35.21 ? 351 ARG A O   1 
ATOM   1719 C CB  . ARG A 1 233 ? 51.375 -7.908  59.446 1.00 34.31 ? 351 ARG A CB  1 
ATOM   1720 C CG  . ARG A 1 233 ? 52.302 -6.752  59.114 1.00 35.75 ? 351 ARG A CG  1 
ATOM   1721 C CD  . ARG A 1 233 ? 53.054 -6.176  60.305 1.00 38.37 ? 351 ARG A CD  1 
ATOM   1722 N NE  . ARG A 1 233 ? 54.100 -5.254  59.873 1.00 40.74 ? 351 ARG A NE  1 
ATOM   1723 C CZ  . ARG A 1 233 ? 54.458 -4.158  60.534 1.00 42.09 ? 351 ARG A CZ  1 
ATOM   1724 N NH1 . ARG A 1 233 ? 53.857 -3.837  61.674 1.00 42.74 ? 351 ARG A NH1 1 
ATOM   1725 N NH2 . ARG A 1 233 ? 55.423 -3.380  60.054 1.00 42.67 ? 351 ARG A NH2 1 
ATOM   1726 N N   . GLY A 1 234 ? 49.037 -10.270 58.372 1.00 35.34 ? 352 GLY A N   1 
ATOM   1727 C CA  . GLY A 1 234 ? 48.503 -11.592 58.642 1.00 35.94 ? 352 GLY A CA  1 
ATOM   1728 C C   . GLY A 1 234 ? 48.186 -11.803 60.111 1.00 36.55 ? 352 GLY A C   1 
ATOM   1729 O O   . GLY A 1 234 ? 47.421 -12.703 60.471 1.00 37.28 ? 352 GLY A O   1 
HETATM 1730 O O   . HOH B 2 .   ? 25.942 -2.431  33.227 1.00 14.12 ? 360 HOH A O   1 
HETATM 1731 O O   . HOH B 2 .   ? 34.458 -1.817  24.690 1.00 9.67  ? 361 HOH A O   1 
HETATM 1732 O O   . HOH B 2 .   ? 41.013 -5.607  36.276 1.00 12.91 ? 362 HOH A O   1 
HETATM 1733 O O   . HOH B 2 .   ? 46.856 -4.682  45.008 1.00 13.15 ? 363 HOH A O   1 
HETATM 1734 O O   . HOH B 2 .   ? 45.858 -3.544  41.626 1.00 13.75 ? 364 HOH A O   1 
HETATM 1735 O O   . HOH B 2 .   ? 46.282 -11.759 40.212 1.00 14.12 ? 365 HOH A O   1 
HETATM 1736 O O   . HOH B 2 .   ? 4.191  2.963   16.054 1.00 17.77 ? 366 HOH A O   1 
HETATM 1737 O O   . HOH B 2 .   ? 46.139 -16.358 47.656 1.00 20.10 ? 367 HOH A O   1 
HETATM 1738 O O   . HOH B 2 .   ? 35.239 -4.414  27.313 1.00 12.24 ? 368 HOH A O   1 
HETATM 1739 O O   . HOH B 2 .   ? 21.314 1.048   12.877 1.00 15.55 ? 369 HOH A O   1 
HETATM 1740 O O   . HOH B 2 .   ? 32.998 9.102   25.912 1.00 21.13 ? 370 HOH A O   1 
HETATM 1741 O O   . HOH B 2 .   ? 15.365 6.790   9.906  1.00 20.78 ? 371 HOH A O   1 
HETATM 1742 O O   . HOH B 2 .   ? 34.546 3.102   20.625 1.00 13.16 ? 372 HOH A O   1 
HETATM 1743 O O   . HOH B 2 .   ? 24.586 1.126   14.002 1.00 25.62 ? 373 HOH A O   1 
HETATM 1744 O O   . HOH B 2 .   ? 43.713 -5.750  37.210 1.00 16.87 ? 374 HOH A O   1 
HETATM 1745 O O   . HOH B 2 .   ? 3.990  2.148   18.686 1.00 15.24 ? 375 HOH A O   1 
HETATM 1746 O O   . HOH B 2 .   ? 18.000 -6.493  30.583 1.00 25.51 ? 376 HOH A O   1 
HETATM 1747 O O   . HOH B 2 .   ? 44.645 -12.583 42.325 1.00 17.79 ? 377 HOH A O   1 
HETATM 1748 O O   . HOH B 2 .   ? 48.695 -11.305 49.779 1.00 20.35 ? 378 HOH A O   1 
HETATM 1749 O O   . HOH B 2 .   ? 38.307 -8.491  23.726 1.00 21.78 ? 379 HOH A O   1 
HETATM 1750 O O   . HOH B 2 .   ? 31.126 5.414   13.644 1.00 24.68 ? 380 HOH A O   1 
HETATM 1751 O O   . HOH B 2 .   ? 38.261 -12.749 32.535 1.00 24.60 ? 381 HOH A O   1 
HETATM 1752 O O   . HOH B 2 .   ? 45.628 -12.682 37.489 1.00 19.05 ? 382 HOH A O   1 
HETATM 1753 O O   . HOH B 2 .   ? 25.758 -6.280  11.374 1.00 19.76 ? 383 HOH A O   1 
HETATM 1754 O O   . HOH B 2 .   ? 29.187 3.671   33.879 1.00 24.30 ? 384 HOH A O   1 
HETATM 1755 O O   . HOH B 2 .   ? 24.148 9.299   8.406  1.00 30.17 ? 385 HOH A O   1 
HETATM 1756 O O   . HOH B 2 .   ? 29.200 -2.911  20.000 1.00 18.57 ? 386 HOH A O   1 
HETATM 1757 O O   . HOH B 2 .   ? 12.486 -6.186  22.261 1.00 20.33 ? 387 HOH A O   1 
HETATM 1758 O O   . HOH B 2 .   ? 31.366 -2.548  49.320 1.00 26.58 ? 388 HOH A O   1 
HETATM 1759 O O   . HOH B 2 .   ? 37.955 -4.696  28.536 1.00 12.94 ? 389 HOH A O   1 
HETATM 1760 O O   . HOH B 2 .   ? 49.773 -4.645  45.760 1.00 25.71 ? 390 HOH A O   1 
HETATM 1761 O O   . HOH B 2 .   ? 33.704 2.922   14.428 1.00 23.96 ? 391 HOH A O   1 
HETATM 1762 O O   . HOH B 2 .   ? 14.900 2.288   28.175 1.00 28.91 ? 392 HOH A O   1 
HETATM 1763 O O   . HOH B 2 .   ? 35.124 -4.947  58.896 1.00 36.37 ? 393 HOH A O   1 
HETATM 1764 O O   . HOH B 2 .   ? 10.113 5.068   23.774 1.00 24.32 ? 394 HOH A O   1 
HETATM 1765 O O   . HOH B 2 .   ? 15.488 10.867  16.129 1.00 29.00 ? 395 HOH A O   1 
HETATM 1766 O O   . HOH B 2 .   ? 29.281 -4.097  46.591 1.00 30.17 ? 396 HOH A O   1 
HETATM 1767 O O   . HOH B 2 .   ? 41.766 3.950   26.393 1.00 21.99 ? 397 HOH A O   1 
HETATM 1768 O O   . HOH B 2 .   ? 23.443 8.042   22.152 1.00 27.52 ? 398 HOH A O   1 
HETATM 1769 O O   . HOH B 2 .   ? 31.911 -3.078  20.919 1.00 21.79 ? 399 HOH A O   1 
HETATM 1770 O O   . HOH B 2 .   ? 36.009 -0.566  56.854 1.00 25.49 ? 400 HOH A O   1 
HETATM 1771 O O   . HOH B 2 .   ? 16.145 7.825   7.493  1.00 37.24 ? 401 HOH A O   1 
HETATM 1772 O O   . HOH B 2 .   ? 30.028 -14.155 21.654 1.00 31.95 ? 402 HOH A O   1 
HETATM 1773 O O   . HOH B 2 .   ? 36.429 -8.502  21.446 1.00 30.83 ? 403 HOH A O   1 
HETATM 1774 O O   . HOH B 2 .   ? 8.316  5.472   11.287 1.00 23.44 ? 404 HOH A O   1 
HETATM 1775 O O   . HOH B 2 .   ? 45.899 10.884  31.130 1.00 28.90 ? 405 HOH A O   1 
HETATM 1776 O O   . HOH B 2 .   ? 32.455 -0.472  40.773 1.00 30.36 ? 406 HOH A O   1 
HETATM 1777 O O   . HOH B 2 .   ? 34.493 -1.556  52.038 1.00 32.00 ? 407 HOH A O   1 
HETATM 1778 O O   . HOH B 2 .   ? 50.255 -2.777  35.706 1.00 27.90 ? 408 HOH A O   1 
HETATM 1779 O O   . HOH B 2 .   ? 48.122 5.629   47.060 1.00 64.24 ? 409 HOH A O   1 
HETATM 1780 O O   . HOH B 2 .   ? 47.694 -5.921  34.587 1.00 23.56 ? 410 HOH A O   1 
HETATM 1781 O O   . HOH B 2 .   ? 41.243 -3.452  19.267 1.00 32.60 ? 411 HOH A O   1 
HETATM 1782 O O   . HOH B 2 .   ? 24.725 10.158  20.682 1.00 19.77 ? 412 HOH A O   1 
HETATM 1783 O O   . HOH B 2 .   ? 43.011 -7.500  24.604 1.00 47.37 ? 413 HOH A O   1 
HETATM 1784 O O   . HOH B 2 .   ? 58.519 -2.753  44.503 1.00 37.35 ? 414 HOH A O   1 
HETATM 1785 O O   . HOH B 2 .   ? 14.085 -10.240 16.302 1.00 20.21 ? 415 HOH A O   1 
HETATM 1786 O O   . HOH B 2 .   ? 32.677 6.920   29.514 1.00 27.60 ? 416 HOH A O   1 
HETATM 1787 O O   . HOH B 2 .   ? 2.959  -1.893  12.533 1.00 29.51 ? 417 HOH A O   1 
HETATM 1788 O O   . HOH B 2 .   ? 17.162 -8.071  32.360 1.00 32.06 ? 418 HOH A O   1 
HETATM 1789 O O   . HOH B 2 .   ? 27.843 -3.741  9.077  1.00 38.65 ? 419 HOH A O   1 
HETATM 1790 O O   . HOH B 2 .   ? 35.129 -14.217 44.815 1.00 27.12 ? 420 HOH A O   1 
HETATM 1791 O O   . HOH B 2 .   ? 8.784  -2.930  3.301  1.00 35.89 ? 421 HOH A O   1 
HETATM 1792 O O   . HOH B 2 .   ? 7.179  8.995   19.375 1.00 33.51 ? 422 HOH A O   1 
HETATM 1793 O O   . HOH B 2 .   ? 38.904 6.602   21.727 1.00 23.12 ? 423 HOH A O   1 
HETATM 1794 O O   . HOH B 2 .   ? 14.987 -8.807  6.478  1.00 45.52 ? 424 HOH A O   1 
HETATM 1795 O O   . HOH B 2 .   ? 31.325 -15.580 38.523 1.00 34.17 ? 425 HOH A O   1 
HETATM 1796 O O   . HOH B 2 .   ? 32.897 -4.064  12.405 1.00 34.28 ? 426 HOH A O   1 
HETATM 1797 O O   . HOH B 2 .   ? 17.334 -4.104  30.445 1.00 39.81 ? 427 HOH A O   1 
HETATM 1798 O O   . HOH B 2 .   ? 40.128 -7.201  20.171 1.00 38.56 ? 428 HOH A O   1 
HETATM 1799 O O   . HOH B 2 .   ? 31.239 10.100  16.812 1.00 31.00 ? 429 HOH A O   1 
HETATM 1800 O O   . HOH B 2 .   ? 26.196 8.298   24.716 1.00 28.33 ? 430 HOH A O   1 
HETATM 1801 O O   . HOH B 2 .   ? 51.581 7.242   48.599 1.00 23.65 ? 431 HOH A O   1 
HETATM 1802 O O   . HOH B 2 .   ? 28.786 16.021  13.297 1.00 28.41 ? 432 HOH A O   1 
HETATM 1803 O O   . HOH B 2 .   ? 26.806 -4.886  42.372 1.00 35.04 ? 433 HOH A O   1 
HETATM 1804 O O   . HOH B 2 .   ? 30.708 6.041   31.498 1.00 27.97 ? 434 HOH A O   1 
HETATM 1805 O O   . HOH B 2 .   ? 15.990 -11.172 14.154 1.00 26.16 ? 435 HOH A O   1 
HETATM 1806 O O   . HOH B 2 .   ? 11.544 -10.229 14.577 1.00 47.55 ? 436 HOH A O   1 
HETATM 1807 O O   . HOH B 2 .   ? 40.274 -14.607 44.637 1.00 40.34 ? 437 HOH A O   1 
HETATM 1808 O O   . HOH B 2 .   ? 23.519 -1.374  6.401  1.00 35.66 ? 438 HOH A O   1 
HETATM 1809 O O   . HOH B 2 .   ? 18.860 -11.389 24.615 1.00 21.86 ? 439 HOH A O   1 
HETATM 1810 O O   . HOH B 2 .   ? 37.284 -13.072 45.914 1.00 38.46 ? 440 HOH A O   1 
HETATM 1811 O O   . HOH B 2 .   ? 26.266 -14.715 31.300 1.00 33.07 ? 441 HOH A O   1 
HETATM 1812 O O   . HOH B 2 .   ? 19.351 -9.444  34.367 1.00 43.18 ? 442 HOH A O   1 
HETATM 1813 O O   . HOH B 2 .   ? 35.193 -10.748 21.512 1.00 33.24 ? 443 HOH A O   1 
HETATM 1814 O O   . HOH B 2 .   ? 22.602 13.102  9.104  1.00 47.11 ? 444 HOH A O   1 
HETATM 1815 O O   . HOH B 2 .   ? 19.471 -5.077  -1.347 1.00 47.58 ? 445 HOH A O   1 
HETATM 1816 O O   . HOH B 2 .   ? 46.236 -0.709  35.838 1.00 21.31 ? 446 HOH A O   1 
HETATM 1817 O O   . HOH B 2 .   ? 49.210 1.975   34.324 1.00 27.80 ? 447 HOH A O   1 
HETATM 1818 O O   . HOH B 2 .   ? 27.549 -7.832  12.529 1.00 26.48 ? 448 HOH A O   1 
HETATM 1819 O O   . HOH B 2 .   ? 16.406 -11.807 23.116 1.00 48.40 ? 449 HOH A O   1 
HETATM 1820 O O   . HOH B 2 .   ? 4.954  6.249   13.511 1.00 30.92 ? 450 HOH A O   1 
HETATM 1821 O O   . HOH B 2 .   ? 28.136 -16.747 28.234 1.00 31.38 ? 451 HOH A O   1 
HETATM 1822 O O   . HOH B 2 .   ? 42.487 -11.674 55.194 1.00 33.46 ? 452 HOH A O   1 
HETATM 1823 O O   . HOH B 2 .   ? 48.474 7.562   43.387 1.00 64.22 ? 453 HOH A O   1 
HETATM 1824 O O   . HOH B 2 .   ? 41.104 -8.946  21.903 1.00 46.31 ? 454 HOH A O   1 
HETATM 1825 O O   . HOH B 2 .   ? 39.716 -17.508 39.057 1.00 43.01 ? 455 HOH A O   1 
HETATM 1826 O O   . HOH B 2 .   ? 48.446 -2.273  33.848 1.00 33.92 ? 456 HOH A O   1 
HETATM 1827 O O   . HOH B 2 .   ? 28.127 -13.875 17.456 1.00 38.68 ? 457 HOH A O   1 
HETATM 1828 O O   . HOH B 2 .   ? 56.003 5.810   39.445 1.00 52.47 ? 458 HOH A O   1 
HETATM 1829 O O   . HOH B 2 .   ? 17.550 0.917   31.731 1.00 47.34 ? 459 HOH A O   1 
HETATM 1830 O O   . HOH B 2 .   ? 28.765 8.544   32.321 1.00 57.95 ? 460 HOH A O   1 
HETATM 1831 O O   . HOH B 2 .   ? 14.358 8.318   5.371  1.00 54.94 ? 461 HOH A O   1 
HETATM 1832 O O   . HOH B 2 .   ? 16.998 -9.121  10.256 1.00 30.42 ? 462 HOH A O   1 
HETATM 1833 O O   . HOH B 2 .   ? 10.748 -1.053  17.766 1.00 32.02 ? 463 HOH A O   1 
HETATM 1834 O O   . HOH B 2 .   ? 6.280  3.945   12.811 1.00 35.19 ? 464 HOH A O   1 
HETATM 1835 O O   . HOH B 2 .   ? 34.050 -10.289 9.233  1.00 44.42 ? 465 HOH A O   1 
HETATM 1836 O O   . HOH B 2 .   ? 27.601 6.194   31.808 1.00 60.40 ? 466 HOH A O   1 
HETATM 1837 O O   . HOH B 2 .   ? 32.581 -3.655  51.836 1.00 36.23 ? 467 HOH A O   1 
HETATM 1838 O O   . HOH B 2 .   ? 11.801 -12.124 7.945  1.00 56.86 ? 468 HOH A O   1 
HETATM 1839 O O   . HOH B 2 .   ? 30.851 -4.523  54.190 1.00 43.38 ? 469 HOH A O   1 
HETATM 1840 O O   . HOH B 2 .   ? 35.871 4.678   38.356 1.00 64.32 ? 470 HOH A O   1 
HETATM 1841 O O   . HOH B 2 .   ? 26.800 0.740   17.328 1.00 21.96 ? 471 HOH A O   1 
HETATM 1842 O O   . HOH B 2 .   ? 40.095 -11.130 29.983 1.00 41.83 ? 472 HOH A O   1 
HETATM 1843 O O   . HOH B 2 .   ? 48.096 -17.349 49.556 1.00 41.89 ? 473 HOH A O   1 
HETATM 1844 O O   . HOH B 2 .   ? 22.483 6.931   26.633 1.00 30.77 ? 474 HOH A O   1 
HETATM 1845 O O   . HOH B 2 .   ? 14.573 -11.039 21.543 1.00 47.73 ? 475 HOH A O   1 
HETATM 1846 O O   . HOH B 2 .   ? 10.531 -5.642  20.176 1.00 33.21 ? 476 HOH A O   1 
HETATM 1847 O O   . HOH B 2 .   ? 25.205 4.102   33.497 1.00 37.31 ? 477 HOH A O   1 
HETATM 1848 O O   . HOH B 2 .   ? 25.183 -12.418 32.794 1.00 34.19 ? 478 HOH A O   1 
HETATM 1849 O O   . HOH B 2 .   ? 51.755 8.631   43.750 1.00 64.99 ? 479 HOH A O   1 
HETATM 1850 O O   . HOH B 2 .   ? 28.120 1.669   10.011 1.00 40.73 ? 480 HOH A O   1 
HETATM 1851 O O   . HOH B 2 .   ? 24.616 -13.328 35.078 1.00 34.43 ? 481 HOH A O   1 
HETATM 1852 O O   . HOH B 2 .   ? 11.284 12.698  11.702 1.00 51.96 ? 482 HOH A O   1 
HETATM 1853 O O   . HOH B 2 .   ? 39.122 7.345   45.276 1.00 79.01 ? 483 HOH A O   1 
HETATM 1854 O O   . HOH B 2 .   ? 29.821 -8.100  41.724 1.00 50.96 ? 484 HOH A O   1 
HETATM 1855 O O   . HOH B 2 .   ? 17.281 2.405   29.548 1.00 32.75 ? 485 HOH A O   1 
HETATM 1856 O O   . HOH B 2 .   ? 35.627 7.724   46.721 1.00 42.99 ? 486 HOH A O   1 
HETATM 1857 O O   . HOH B 2 .   ? 42.450 -12.932 40.819 1.00 32.09 ? 487 HOH A O   1 
HETATM 1858 O O   . HOH B 2 .   ? 13.287 -11.034 11.014 1.00 54.41 ? 488 HOH A O   1 
HETATM 1859 O O   . HOH B 2 .   ? 52.663 0.763   58.382 1.00 53.28 ? 489 HOH A O   1 
HETATM 1860 O O   . HOH B 2 .   ? 17.051 5.120   27.909 1.00 35.85 ? 490 HOH A O   1 
HETATM 1861 O O   . HOH B 2 .   ? 51.252 3.422   58.721 1.00 48.80 ? 491 HOH A O   1 
HETATM 1862 O O   . HOH B 2 .   ? 48.307 -11.771 39.599 1.00 33.25 ? 492 HOH A O   1 
HETATM 1863 O O   . HOH B 2 .   ? 30.173 -11.287 18.736 1.00 44.33 ? 493 HOH A O   1 
HETATM 1864 O O   . HOH B 2 .   ? 22.409 -12.184 32.162 1.00 32.88 ? 494 HOH A O   1 
HETATM 1865 O O   . HOH B 2 .   ? 56.775 -1.797  53.643 1.00 39.39 ? 495 HOH A O   1 
HETATM 1866 O O   . HOH B 2 .   ? 25.603 16.059  13.236 1.00 48.50 ? 496 HOH A O   1 
HETATM 1867 O O   . HOH B 2 .   ? 12.724 -12.294 19.138 1.00 46.18 ? 497 HOH A O   1 
HETATM 1868 O O   . HOH B 2 .   ? 11.832 -13.630 21.993 1.00 38.71 ? 498 HOH A O   1 
HETATM 1869 O O   . HOH B 2 .   ? 22.727 11.658  22.636 1.00 78.87 ? 499 HOH A O   1 
HETATM 1870 O O   . HOH B 2 .   ? 15.765 -11.351 11.824 1.00 33.74 ? 500 HOH A O   1 
HETATM 1871 O O   . HOH B 2 .   ? 10.430 2.311   22.017 1.00 2.00  ? 501 HOH A O   1 
HETATM 1872 O O   . HOH B 2 .   ? 20.318 16.604  6.174  1.00 87.21 ? 502 HOH A O   1 
HETATM 1873 O O   . HOH B 2 .   ? 17.507 13.691  9.262  1.00 49.98 ? 503 HOH A O   1 
HETATM 1874 O O   . HOH B 2 .   ? 17.788 14.063  12.140 1.00 31.57 ? 504 HOH A O   1 
HETATM 1875 O O   . HOH B 2 .   ? 17.297 10.452  7.641  1.00 45.69 ? 505 HOH A O   1 
HETATM 1876 O O   . HOH B 2 .   ? 19.045 -15.664 24.915 1.00 47.26 ? 506 HOH A O   1 
HETATM 1877 O O   . HOH B 2 .   ? 17.651 -1.881  31.538 1.00 50.33 ? 507 HOH A O   1 
HETATM 1878 O O   . HOH B 2 .   ? 23.364 -6.406  39.485 1.00 44.77 ? 508 HOH A O   1 
HETATM 1879 O O   . HOH B 2 .   ? 25.801 -12.009 40.075 1.00 64.61 ? 509 HOH A O   1 
HETATM 1880 O O   . HOH B 2 .   ? 31.115 5.219   39.696 1.00 49.75 ? 510 HOH A O   1 
HETATM 1881 O O   . HOH B 2 .   ? 31.557 4.984   33.813 1.00 31.99 ? 511 HOH A O   1 
HETATM 1882 O O   . HOH B 2 .   ? 24.448 1.983   40.951 1.00 28.72 ? 512 HOH A O   1 
HETATM 1883 O O   . HOH B 2 .   ? 26.976 3.068   40.184 1.00 40.98 ? 513 HOH A O   1 
HETATM 1884 O O   . HOH B 2 .   ? 41.762 -3.709  25.549 1.00 33.12 ? 514 HOH A O   1 
HETATM 1885 O O   . HOH B 2 .   ? 13.809 -4.790  28.339 1.00 44.22 ? 515 HOH A O   1 
HETATM 1886 O O   . HOH B 2 .   ? 7.303  -0.983  -1.507 1.00 54.45 ? 516 HOH A O   1 
HETATM 1887 O O   . HOH B 2 .   ? 28.095 11.508  13.037 1.00 48.29 ? 517 HOH A O   1 
HETATM 1888 O O   . HOH B 2 .   ? 13.086 13.727  -1.113 1.00 45.07 ? 518 HOH A O   1 
HETATM 1889 O O   . HOH B 2 .   ? 8.355  15.064  4.387  1.00 47.06 ? 519 HOH A O   1 
HETATM 1890 O O   . HOH B 2 .   ? 16.192 10.387  1.966  1.00 63.96 ? 520 HOH A O   1 
HETATM 1891 O O   . HOH B 2 .   ? 6.226  -6.016  8.757  1.00 33.50 ? 521 HOH A O   1 
HETATM 1892 O O   . HOH B 2 .   ? 2.203  -5.383  10.188 1.00 32.44 ? 522 HOH A O   1 
HETATM 1893 O O   . HOH B 2 .   ? 8.268  -6.468  4.611  1.00 36.38 ? 523 HOH A O   1 
HETATM 1894 O O   . HOH B 2 .   ? 30.705 -3.475  11.705 1.00 42.99 ? 524 HOH A O   1 
HETATM 1895 O O   . HOH B 2 .   ? 31.868 0.671   11.259 1.00 50.60 ? 525 HOH A O   1 
HETATM 1896 O O   . HOH B 2 .   ? 26.647 8.011   26.745 1.00 39.76 ? 526 HOH A O   1 
HETATM 1897 O O   . HOH B 2 .   ? 21.667 4.422   32.498 1.00 49.56 ? 527 HOH A O   1 
HETATM 1898 O O   . HOH B 2 .   ? 23.688 -12.232 12.247 1.00 59.12 ? 528 HOH A O   1 
HETATM 1899 O O   . HOH B 2 .   ? 27.108 -14.410 10.094 1.00 31.83 ? 529 HOH A O   1 
HETATM 1900 O O   . HOH B 2 .   ? 29.302 -17.037 10.334 1.00 35.48 ? 530 HOH A O   1 
HETATM 1901 O O   . HOH B 2 .   ? 57.437 7.575   50.948 1.00 36.37 ? 531 HOH A O   1 
HETATM 1902 O O   . HOH B 2 .   ? 27.337 -4.284  6.646  1.00 63.83 ? 532 HOH A O   1 
HETATM 1903 O O   . HOH B 2 .   ? 31.160 -10.968 16.434 1.00 48.86 ? 533 HOH A O   1 
HETATM 1904 O O   . HOH B 2 .   ? 36.106 -15.001 13.776 1.00 56.33 ? 534 HOH A O   1 
HETATM 1905 O O   . HOH B 2 .   ? 37.381 -8.026  16.616 1.00 39.30 ? 535 HOH A O   1 
HETATM 1906 O O   . HOH B 2 .   ? 38.393 11.665  23.626 1.00 39.02 ? 536 HOH A O   1 
HETATM 1907 O O   . HOH B 2 .   ? 39.091 7.130   30.476 1.00 49.22 ? 537 HOH A O   1 
HETATM 1908 O O   . HOH B 2 .   ? 39.918 8.601   23.087 1.00 38.20 ? 538 HOH A O   1 
HETATM 1909 O O   . HOH B 2 .   ? 24.770 0.444   38.638 1.00 36.24 ? 539 HOH A O   1 
HETATM 1910 O O   . HOH B 2 .   ? 46.979 6.251   36.737 1.00 33.61 ? 540 HOH A O   1 
HETATM 1911 O O   . HOH B 2 .   ? 44.697 -11.297 34.364 1.00 35.67 ? 541 HOH A O   1 
HETATM 1912 O O   . HOH B 2 .   ? 48.319 -10.184 62.680 1.00 45.94 ? 542 HOH A O   1 
HETATM 1913 O O   . HOH B 2 .   ? 53.936 -11.665 58.214 1.00 35.78 ? 543 HOH A O   1 
HETATM 1914 O O   . HOH B 2 .   ? 3.814  -1.630  9.783  1.00 28.82 ? 544 HOH A O   1 
HETATM 1915 O O   . HOH B 2 .   ? 3.984  -3.652  8.768  1.00 38.94 ? 545 HOH A O   1 
HETATM 1916 O O   . HOH B 2 .   ? 39.591 -15.984 59.025 1.00 61.19 ? 546 HOH A O   1 
HETATM 1917 O O   . HOH B 2 .   ? 10.713 5.825   0.329  1.00 51.20 ? 547 HOH A O   1 
HETATM 1918 O O   . HOH B 2 .   ? 7.088  4.269   8.502  1.00 41.49 ? 548 HOH A O   1 
HETATM 1919 O O   . HOH B 2 .   ? 5.423  8.638   12.547 1.00 29.97 ? 549 HOH A O   1 
HETATM 1920 O O   . HOH B 2 .   ? 13.969 1.634   -5.284 1.00 40.44 ? 550 HOH A O   1 
HETATM 1921 O O   . HOH B 2 .   ? 19.740 8.187   26.539 1.00 33.90 ? 551 HOH A O   1 
HETATM 1922 O O   . HOH B 2 .   ? 49.721 -7.708  51.437 1.00 41.40 ? 552 HOH A O   1 
HETATM 1923 O O   . HOH B 2 .   ? 41.576 8.027   27.291 1.00 28.14 ? 553 HOH A O   1 
HETATM 1924 O O   . HOH B 2 .   ? 47.290 7.392   28.936 1.00 40.11 ? 554 HOH A O   1 
# 
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   MET 1   119 ?   ?   ?   A . n 
A 1 2   ALA 2   120 ?   ?   ?   A . n 
A 1 3   THR 3   121 ?   ?   ?   A . n 
A 1 4   ARG 4   122 ?   ?   ?   A . n 
A 1 5   ALA 5   123 ?   ?   ?   A . n 
A 1 6   ASP 6   124 ?   ?   ?   A . n 
A 1 7   GLU 7   125 125 GLU GLU A . n 
A 1 8   ASP 8   126 126 ASP ASP A . n 
A 1 9   GLY 9   127 127 GLY GLY A . n 
A 1 10  ASP 10  128 128 ASP ASP A . n 
A 1 11  THR 11  129 129 THR THR A . n 
A 1 12  PRO 12  130 130 PRO PRO A . n 
A 1 13  LEU 13  131 131 LEU LEU A . n 
A 1 14  HIS 14  132 132 HIS HIS A . n 
A 1 15  ILE 15  133 133 ILE ILE A . n 
A 1 16  ALA 16  134 134 ALA ALA A . n 
A 1 17  VAL 17  135 135 VAL VAL A . n 
A 1 18  VAL 18  136 136 VAL VAL A . n 
A 1 19  GLN 19  137 137 GLN GLN A . n 
A 1 20  GLY 20  138 138 GLY GLY A . n 
A 1 21  ASN 21  139 139 ASN ASN A . n 
A 1 22  LEU 22  140 140 LEU LEU A . n 
A 1 23  PRO 23  141 141 PRO PRO A . n 
A 1 24  ALA 24  142 142 ALA ALA A . n 
A 1 25  VAL 25  143 143 VAL VAL A . n 
A 1 26  HIS 26  144 144 HIS HIS A . n 
A 1 27  ARG 27  145 145 ARG ARG A . n 
A 1 28  LEU 28  146 146 LEU LEU A . n 
A 1 29  VAL 29  147 147 VAL VAL A . n 
A 1 30  ASN 30  148 148 ASN ASN A . n 
A 1 31  LEU 31  149 149 LEU LEU A . n 
A 1 32  PHE 32  150 150 PHE PHE A . n 
A 1 33  GLN 33  151 151 GLN GLN A . n 
A 1 34  GLN 34  152 152 GLN GLN A . n 
A 1 35  GLY 35  153 153 GLY GLY A . n 
A 1 36  GLY 36  154 154 GLY GLY A . n 
A 1 37  ARG 37  155 155 ARG ARG A . n 
A 1 38  GLU 38  156 156 GLU GLU A . n 
A 1 39  LEU 39  157 157 LEU LEU A . n 
A 1 40  ASP 40  158 158 ASP ASP A . n 
A 1 41  ILE 41  159 159 ILE ILE A . n 
A 1 42  TYR 42  160 160 TYR TYR A . n 
A 1 43  ASN 43  161 161 ASN ASN A . n 
A 1 44  ASN 44  162 162 ASN ASN A . n 
A 1 45  LEU 45  163 163 LEU LEU A . n 
A 1 46  ARG 46  164 164 ARG ARG A . n 
A 1 47  GLN 47  165 165 GLN GLN A . n 
A 1 48  THR 48  166 166 THR THR A . n 
A 1 49  PRO 49  167 167 PRO PRO A . n 
A 1 50  LEU 50  168 168 LEU LEU A . n 
A 1 51  HIS 51  169 169 HIS HIS A . n 
A 1 52  LEU 52  170 170 LEU LEU A . n 
A 1 53  ALA 53  171 171 ALA ALA A . n 
A 1 54  VAL 54  172 172 VAL VAL A . n 
A 1 55  ILE 55  173 173 ILE ILE A . n 
A 1 56  THR 56  174 174 THR THR A . n 
A 1 57  THR 57  175 175 THR THR A . n 
A 1 58  LEU 58  176 176 LEU LEU A . n 
A 1 59  PRO 59  177 177 PRO PRO A . n 
A 1 60  SER 60  178 178 SER SER A . n 
A 1 61  VAL 61  179 179 VAL VAL A . n 
A 1 62  VAL 62  180 180 VAL VAL A . n 
A 1 63  ARG 63  181 181 ARG ARG A . n 
A 1 64  LEU 64  182 182 LEU LEU A . n 
A 1 65  LEU 65  183 183 LEU LEU A . n 
A 1 66  VAL 66  184 184 VAL VAL A . n 
A 1 67  THR 67  185 185 THR THR A . n 
A 1 68  ALA 68  186 186 ALA ALA A . n 
A 1 69  GLY 69  187 187 GLY GLY A . n 
A 1 70  ALA 70  188 188 ALA ALA A . n 
A 1 71  SER 71  189 189 SER SER A . n 
A 1 72  PRO 72  190 190 PRO PRO A . n 
A 1 73  MET 73  191 191 MET MET A . n 
A 1 74  ALA 74  192 192 ALA ALA A . n 
A 1 75  LEU 75  193 193 LEU LEU A . n 
A 1 76  ASP 76  194 194 ASP ASP A . n 
A 1 77  ARG 77  195 195 ARG ARG A . n 
A 1 78  HIS 78  196 196 HIS HIS A . n 
A 1 79  GLY 79  197 197 GLY GLY A . n 
A 1 80  GLN 80  198 198 GLN GLN A . n 
A 1 81  THR 81  199 199 THR THR A . n 
A 1 82  ALA 82  200 200 ALA ALA A . n 
A 1 83  ALA 83  201 201 ALA ALA A . n 
A 1 84  HIS 84  202 202 HIS HIS A . n 
A 1 85  LEU 85  203 203 LEU LEU A . n 
A 1 86  ALA 86  204 204 ALA ALA A . n 
A 1 87  CYS 87  205 205 CYS CYS A . n 
A 1 88  GLU 88  206 206 GLU GLU A . n 
A 1 89  HIS 89  207 207 HIS HIS A . n 
A 1 90  ARG 90  208 208 ARG ARG A . n 
A 1 91  SER 91  209 209 SER SER A . n 
A 1 92  PRO 92  210 210 PRO PRO A . n 
A 1 93  THR 93  211 211 THR THR A . n 
A 1 94  CYS 94  212 212 CYS CYS A . n 
A 1 95  LEU 95  213 213 LEU LEU A . n 
A 1 96  ARG 96  214 214 ARG ARG A . n 
A 1 97  ALA 97  215 215 ALA ALA A . n 
A 1 98  LEU 98  216 216 LEU LEU A . n 
A 1 99  LEU 99  217 217 LEU LEU A . n 
A 1 100 ASP 100 218 218 ASP ASP A . n 
A 1 101 SER 101 219 219 SER SER A . n 
A 1 102 ALA 102 220 220 ALA ALA A . n 
A 1 103 ALA 103 221 221 ALA ALA A . n 
A 1 104 PRO 104 222 222 PRO PRO A . n 
A 1 105 GLY 105 223 223 GLY GLY A . n 
A 1 106 THR 106 224 224 THR THR A . n 
A 1 107 LEU 107 225 225 LEU LEU A . n 
A 1 108 ASP 108 226 226 ASP ASP A . n 
A 1 109 LEU 109 227 227 LEU LEU A . n 
A 1 110 GLU 110 228 228 GLU GLU A . n 
A 1 111 ALA 111 229 229 ALA ALA A . n 
A 1 112 ARG 112 230 230 ARG ARG A . n 
A 1 113 ASN 113 231 231 ASN ASN A . n 
A 1 114 TYR 114 232 232 TYR TYR A . n 
A 1 115 ASP 115 233 233 ASP ASP A . n 
A 1 116 GLY 116 234 234 GLY GLY A . n 
A 1 117 LEU 117 235 235 LEU LEU A . n 
A 1 118 THR 118 236 236 THR THR A . n 
A 1 119 ALA 119 237 237 ALA ALA A . n 
A 1 120 LEU 120 238 238 LEU LEU A . n 
A 1 121 HIS 121 239 239 HIS HIS A . n 
A 1 122 VAL 122 240 240 VAL VAL A . n 
A 1 123 ALA 123 241 241 ALA ALA A . n 
A 1 124 VAL 124 242 242 VAL VAL A . n 
A 1 125 ASN 125 243 243 ASN ASN A . n 
A 1 126 THR 126 244 244 THR THR A . n 
A 1 127 GLU 127 245 245 GLU GLU A . n 
A 1 128 CYS 128 246 246 CYS CYS A . n 
A 1 129 GLN 129 247 247 GLN GLN A . n 
A 1 130 GLU 130 248 248 GLU GLU A . n 
A 1 131 THR 131 249 249 THR THR A . n 
A 1 132 VAL 132 250 250 VAL VAL A . n 
A 1 133 GLN 133 251 251 GLN GLN A . n 
A 1 134 LEU 134 252 252 LEU LEU A . n 
A 1 135 LEU 135 253 253 LEU LEU A . n 
A 1 136 LEU 136 254 254 LEU LEU A . n 
A 1 137 GLU 137 255 255 GLU GLU A . n 
A 1 138 ARG 138 256 256 ARG ARG A . n 
A 1 139 GLY 139 257 257 GLY GLY A . n 
A 1 140 ALA 140 258 258 ALA ALA A . n 
A 1 141 ASP 141 259 259 ASP ASP A . n 
A 1 142 ILE 142 260 260 ILE ILE A . n 
A 1 143 ASP 143 261 261 ASP ASP A . n 
A 1 144 ALA 144 262 262 ALA ALA A . n 
A 1 145 VAL 145 263 263 VAL VAL A . n 
A 1 146 ASP 146 264 264 ASP ASP A . n 
A 1 147 ILE 147 265 265 ILE ILE A . n 
A 1 148 LYS 148 266 266 LYS LYS A . n 
A 1 149 SER 149 267 267 SER SER A . n 
A 1 150 GLY 150 268 268 GLY GLY A . n 
A 1 151 ARG 151 269 269 ARG ARG A . n 
A 1 152 SER 152 270 270 SER SER A . n 
A 1 153 PRO 153 271 271 PRO PRO A . n 
A 1 154 LEU 154 272 272 LEU LEU A . n 
A 1 155 ILE 155 273 273 ILE ILE A . n 
A 1 156 HIS 156 274 274 HIS HIS A . n 
A 1 157 ALA 157 275 275 ALA ALA A . n 
A 1 158 VAL 158 276 276 VAL VAL A . n 
A 1 159 GLU 159 277 277 GLU GLU A . n 
A 1 160 ASN 160 278 278 ASN ASN A . n 
A 1 161 ASN 161 279 279 ASN ASN A . n 
A 1 162 SER 162 280 280 SER SER A . n 
A 1 163 LEU 163 281 281 LEU LEU A . n 
A 1 164 SER 164 282 282 SER SER A . n 
A 1 165 MET 165 283 283 MET MET A . n 
A 1 166 VAL 166 284 284 VAL VAL A . n 
A 1 167 GLN 167 285 285 GLN GLN A . n 
A 1 168 LEU 168 286 286 LEU LEU A . n 
A 1 169 LEU 169 287 287 LEU LEU A . n 
A 1 170 LEU 170 288 288 LEU LEU A . n 
A 1 171 GLN 171 289 289 GLN GLN A . n 
A 1 172 HIS 172 290 290 HIS HIS A . n 
A 1 173 GLY 173 291 291 GLY GLY A . n 
A 1 174 ALA 174 292 292 ALA ALA A . n 
A 1 175 ASN 175 293 293 ASN ASN A . n 
A 1 176 VAL 176 294 294 VAL VAL A . n 
A 1 177 ASN 177 295 295 ASN ASN A . n 
A 1 178 ALA 178 296 296 ALA ALA A . n 
A 1 179 GLN 179 297 297 GLN GLN A . n 
A 1 180 MET 180 298 298 MET MET A . n 
A 1 181 TYR 181 299 299 TYR TYR A . n 
A 1 182 SER 182 300 300 SER SER A . n 
A 1 183 GLY 183 301 301 GLY GLY A . n 
A 1 184 SER 184 302 302 SER SER A . n 
A 1 185 SER 185 303 303 SER SER A . n 
A 1 186 ALA 186 304 304 ALA ALA A . n 
A 1 187 LEU 187 305 305 LEU LEU A . n 
A 1 188 HIS 188 306 306 HIS HIS A . n 
A 1 189 SER 189 307 307 SER SER A . n 
A 1 190 ALA 190 308 308 ALA ALA A . n 
A 1 191 SER 191 309 309 SER SER A . n 
A 1 192 GLY 192 310 310 GLY GLY A . n 
A 1 193 ARG 193 311 311 ARG ARG A . n 
A 1 194 GLY 194 312 312 GLY GLY A . n 
A 1 195 LEU 195 313 313 LEU LEU A . n 
A 1 196 LEU 196 314 314 LEU LEU A . n 
A 1 197 PRO 197 315 315 PRO PRO A . n 
A 1 198 LEU 198 316 316 LEU LEU A . n 
A 1 199 VAL 199 317 317 VAL VAL A . n 
A 1 200 ARG 200 318 318 ARG ARG A . n 
A 1 201 THR 201 319 319 THR THR A . n 
A 1 202 LEU 202 320 320 LEU LEU A . n 
A 1 203 VAL 203 321 321 VAL VAL A . n 
A 1 204 ARG 204 322 322 ARG ARG A . n 
A 1 205 SER 205 323 323 SER SER A . n 
A 1 206 GLY 206 324 324 GLY GLY A . n 
A 1 207 ALA 207 325 325 ALA ALA A . n 
A 1 208 ASP 208 326 326 ASP ASP A . n 
A 1 209 SER 209 327 327 SER SER A . n 
A 1 210 SER 210 328 328 SER SER A . n 
A 1 211 LEU 211 329 329 LEU LEU A . n 
A 1 212 LYS 212 330 330 LYS LYS A . n 
A 1 213 ASN 213 331 331 ASN ASN A . n 
A 1 214 CYS 214 332 332 CYS CYS A . n 
A 1 215 HIS 215 333 333 HIS HIS A . n 
A 1 216 ASN 216 334 334 ASN ASN A . n 
A 1 217 ASP 217 335 335 ASP ASP A . n 
A 1 218 THR 218 336 336 THR THR A . n 
A 1 219 PRO 219 337 337 PRO PRO A . n 
A 1 220 LEU 220 338 338 LEU LEU A . n 
A 1 221 MET 221 339 339 MET MET A . n 
A 1 222 VAL 222 340 340 VAL VAL A . n 
A 1 223 ALA 223 341 341 ALA ALA A . n 
A 1 224 ARG 224 342 342 ARG ARG A . n 
A 1 225 SER 225 343 343 SER SER A . n 
A 1 226 ARG 226 344 344 ARG ARG A . n 
A 1 227 ARG 227 345 345 ARG ARG A . n 
A 1 228 VAL 228 346 346 VAL VAL A . n 
A 1 229 ILE 229 347 347 ILE ILE A . n 
A 1 230 ASP 230 348 348 ASP ASP A . n 
A 1 231 ILE 231 349 349 ILE ILE A . n 
A 1 232 LEU 232 350 350 LEU LEU A . n 
A 1 233 ARG 233 351 351 ARG ARG A . n 
A 1 234 GLY 234 352 352 GLY GLY A . n 
A 1 235 LYS 235 353 ?   ?   ?   A . n 
A 1 236 ALA 236 354 ?   ?   ?   A . n 
A 1 237 THR 237 355 ?   ?   ?   A . n 
A 1 238 ARG 238 356 ?   ?   ?   A . n 
A 1 239 PRO 239 357 ?   ?   ?   A . n 
A 1 240 ALA 240 358 ?   ?   ?   A . n 
A 1 241 SER 241 359 ?   ?   ?   A . 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 
B 2 HOH 1   360 353 HOH HOH A . 
B 2 HOH 2   361 354 HOH HOH A . 
B 2 HOH 3   362 355 HOH HOH A . 
B 2 HOH 4   363 356 HOH HOH A . 
B 2 HOH 5   364 357 HOH HOH A . 
B 2 HOH 6   365 358 HOH HOH A . 
B 2 HOH 7   366 359 HOH HOH A . 
B 2 HOH 8   367 360 HOH HOH A . 
B 2 HOH 9   368 361 HOH HOH A . 
B 2 HOH 10  369 362 HOH HOH A . 
B 2 HOH 11  370 363 HOH HOH A . 
B 2 HOH 12  371 364 HOH HOH A . 
B 2 HOH 13  372 365 HOH HOH A . 
B 2 HOH 14  373 366 HOH HOH A . 
B 2 HOH 15  374 367 HOH HOH A . 
B 2 HOH 16  375 368 HOH HOH A . 
B 2 HOH 17  376 369 HOH HOH A . 
B 2 HOH 18  377 370 HOH HOH A . 
B 2 HOH 19  378 371 HOH HOH A . 
B 2 HOH 20  379 372 HOH HOH A . 
B 2 HOH 21  380 373 HOH HOH A . 
B 2 HOH 22  381 374 HOH HOH A . 
B 2 HOH 23  382 375 HOH HOH A . 
B 2 HOH 24  383 376 HOH HOH A . 
B 2 HOH 25  384 377 HOH HOH A . 
B 2 HOH 26  385 378 HOH HOH A . 
B 2 HOH 27  386 379 HOH HOH A . 
B 2 HOH 28  387 380 HOH HOH A . 
B 2 HOH 29  388 381 HOH HOH A . 
B 2 HOH 30  389 382 HOH HOH A . 
B 2 HOH 31  390 383 HOH HOH A . 
B 2 HOH 32  391 384 HOH HOH A . 
B 2 HOH 33  392 385 HOH HOH A . 
B 2 HOH 34  393 386 HOH HOH A . 
B 2 HOH 35  394 387 HOH HOH A . 
B 2 HOH 36  395 388 HOH HOH A . 
B 2 HOH 37  396 389 HOH HOH A . 
B 2 HOH 38  397 390 HOH HOH A . 
B 2 HOH 39  398 391 HOH HOH A . 
B 2 HOH 40  399 392 HOH HOH A . 
B 2 HOH 41  400 393 HOH HOH A . 
B 2 HOH 42  401 394 HOH HOH A . 
B 2 HOH 43  402 395 HOH HOH A . 
B 2 HOH 44  403 396 HOH HOH A . 
B 2 HOH 45  404 397 HOH HOH A . 
B 2 HOH 46  405 398 HOH HOH A . 
B 2 HOH 47  406 399 HOH HOH A . 
B 2 HOH 48  407 400 HOH HOH A . 
B 2 HOH 49  408 401 HOH HOH A . 
B 2 HOH 50  409 402 HOH HOH A . 
B 2 HOH 51  410 403 HOH HOH A . 
B 2 HOH 52  411 404 HOH HOH A . 
B 2 HOH 53  412 405 HOH HOH A . 
B 2 HOH 54  413 406 HOH HOH A . 
B 2 HOH 55  414 407 HOH HOH A . 
B 2 HOH 56  415 408 HOH HOH A . 
B 2 HOH 57  416 409 HOH HOH A . 
B 2 HOH 58  417 410 HOH HOH A . 
B 2 HOH 59  418 411 HOH HOH A . 
B 2 HOH 60  419 412 HOH HOH A . 
B 2 HOH 61  420 413 HOH HOH A . 
B 2 HOH 62  421 414 HOH HOH A . 
B 2 HOH 63  422 415 HOH HOH A . 
B 2 HOH 64  423 416 HOH HOH A . 
B 2 HOH 65  424 417 HOH HOH A . 
B 2 HOH 66  425 418 HOH HOH A . 
B 2 HOH 67  426 419 HOH HOH A . 
B 2 HOH 68  427 420 HOH HOH A . 
B 2 HOH 69  428 421 HOH HOH A . 
B 2 HOH 70  429 422 HOH HOH A . 
B 2 HOH 71  430 423 HOH HOH A . 
B 2 HOH 72  431 424 HOH HOH A . 
B 2 HOH 73  432 425 HOH HOH A . 
B 2 HOH 74  433 426 HOH HOH A . 
B 2 HOH 75  434 427 HOH HOH A . 
B 2 HOH 76  435 428 HOH HOH A . 
B 2 HOH 77  436 429 HOH HOH A . 
B 2 HOH 78  437 430 HOH HOH A . 
B 2 HOH 79  438 431 HOH HOH A . 
B 2 HOH 80  439 432 HOH HOH A . 
B 2 HOH 81  440 433 HOH HOH A . 
B 2 HOH 82  441 434 HOH HOH A . 
B 2 HOH 83  442 435 HOH HOH A . 
B 2 HOH 84  443 436 HOH HOH A . 
B 2 HOH 85  444 437 HOH HOH A . 
B 2 HOH 86  445 438 HOH HOH A . 
B 2 HOH 87  446 439 HOH HOH A . 
B 2 HOH 88  447 440 HOH HOH A . 
B 2 HOH 89  448 441 HOH HOH A . 
B 2 HOH 90  449 442 HOH HOH A . 
B 2 HOH 91  450 443 HOH HOH A . 
B 2 HOH 92  451 444 HOH HOH A . 
B 2 HOH 93  452 445 HOH HOH A . 
B 2 HOH 94  453 446 HOH HOH A . 
B 2 HOH 95  454 447 HOH HOH A . 
B 2 HOH 96  455 448 HOH HOH A . 
B 2 HOH 97  456 449 HOH HOH A . 
B 2 HOH 98  457 450 HOH HOH A . 
B 2 HOH 99  458 452 HOH HOH A . 
B 2 HOH 100 459 453 HOH HOH A . 
B 2 HOH 101 460 454 HOH HOH A . 
B 2 HOH 102 461 455 HOH HOH A . 
B 2 HOH 103 462 456 HOH HOH A . 
B 2 HOH 104 463 457 HOH HOH A . 
B 2 HOH 105 464 458 HOH HOH A . 
B 2 HOH 106 465 459 HOH HOH A . 
B 2 HOH 107 466 460 HOH HOH A . 
B 2 HOH 108 467 461 HOH HOH A . 
B 2 HOH 109 468 462 HOH HOH A . 
B 2 HOH 110 469 463 HOH HOH A . 
B 2 HOH 111 470 464 HOH HOH A . 
B 2 HOH 112 471 465 HOH HOH A . 
B 2 HOH 113 472 466 HOH HOH A . 
B 2 HOH 114 473 467 HOH HOH A . 
B 2 HOH 115 474 468 HOH HOH A . 
B 2 HOH 116 475 469 HOH HOH A . 
B 2 HOH 117 476 470 HOH HOH A . 
B 2 HOH 118 477 471 HOH HOH A . 
B 2 HOH 119 478 472 HOH HOH A . 
B 2 HOH 120 479 473 HOH HOH A . 
B 2 HOH 121 480 474 HOH HOH A . 
B 2 HOH 122 481 475 HOH HOH A . 
B 2 HOH 123 482 476 HOH HOH A . 
B 2 HOH 124 483 477 HOH HOH A . 
B 2 HOH 125 484 478 HOH HOH A . 
B 2 HOH 126 485 479 HOH HOH A . 
B 2 HOH 127 486 480 HOH HOH A . 
B 2 HOH 128 487 481 HOH HOH A . 
B 2 HOH 129 488 482 HOH HOH A . 
B 2 HOH 130 489 483 HOH HOH A . 
B 2 HOH 131 490 484 HOH HOH A . 
B 2 HOH 132 491 485 HOH HOH A . 
B 2 HOH 133 492 486 HOH HOH A . 
B 2 HOH 134 493 487 HOH HOH A . 
B 2 HOH 135 494 488 HOH HOH A . 
B 2 HOH 136 495 489 HOH HOH A . 
B 2 HOH 137 496 490 HOH HOH A . 
B 2 HOH 138 497 491 HOH HOH A . 
B 2 HOH 139 498 492 HOH HOH A . 
B 2 HOH 140 499 493 HOH HOH A . 
B 2 HOH 141 500 494 HOH HOH A . 
B 2 HOH 142 501 495 HOH HOH A . 
B 2 HOH 143 502 496 HOH HOH A . 
B 2 HOH 144 503 497 HOH HOH A . 
B 2 HOH 145 504 498 HOH HOH A . 
B 2 HOH 146 505 499 HOH HOH A . 
B 2 HOH 147 506 500 HOH HOH A . 
B 2 HOH 148 507 501 HOH HOH A . 
B 2 HOH 149 508 502 HOH HOH A . 
B 2 HOH 150 509 503 HOH HOH A . 
B 2 HOH 151 510 504 HOH HOH A . 
B 2 HOH 152 511 505 HOH HOH A . 
B 2 HOH 153 512 506 HOH HOH A . 
B 2 HOH 154 513 507 HOH HOH A . 
B 2 HOH 155 514 508 HOH HOH A . 
B 2 HOH 156 515 509 HOH HOH A . 
B 2 HOH 157 516 510 HOH HOH A . 
B 2 HOH 158 517 512 HOH HOH A . 
B 2 HOH 159 518 513 HOH HOH A . 
B 2 HOH 160 519 514 HOH HOH A . 
B 2 HOH 161 520 515 HOH HOH A . 
B 2 HOH 162 521 516 HOH HOH A . 
B 2 HOH 163 522 517 HOH HOH A . 
B 2 HOH 164 523 518 HOH HOH A . 
B 2 HOH 165 524 519 HOH HOH A . 
B 2 HOH 166 525 520 HOH HOH A . 
B 2 HOH 167 526 521 HOH HOH A . 
B 2 HOH 168 527 522 HOH HOH A . 
B 2 HOH 169 528 523 HOH HOH A . 
B 2 HOH 170 529 524 HOH HOH A . 
B 2 HOH 171 530 525 HOH HOH A . 
B 2 HOH 172 531 526 HOH HOH A . 
B 2 HOH 173 532 527 HOH HOH A . 
B 2 HOH 174 533 528 HOH HOH A . 
B 2 HOH 175 534 529 HOH HOH A . 
B 2 HOH 176 535 530 HOH HOH A . 
B 2 HOH 177 536 531 HOH HOH A . 
B 2 HOH 178 537 532 HOH HOH A . 
B 2 HOH 179 538 533 HOH HOH A . 
B 2 HOH 180 539 534 HOH HOH A . 
B 2 HOH 181 540 535 HOH HOH A . 
B 2 HOH 182 541 536 HOH HOH A . 
B 2 HOH 183 542 537 HOH HOH A . 
B 2 HOH 184 543 538 HOH HOH A . 
B 2 HOH 185 544 539 HOH HOH A . 
B 2 HOH 186 545 540 HOH HOH A . 
B 2 HOH 187 546 541 HOH HOH A . 
B 2 HOH 188 547 542 HOH HOH A . 
B 2 HOH 189 548 543 HOH HOH A . 
B 2 HOH 190 549 544 HOH HOH A . 
B 2 HOH 191 550 545 HOH HOH A . 
B 2 HOH 192 551 546 HOH HOH A . 
B 2 HOH 193 552 547 HOH HOH A . 
B 2 HOH 194 553 548 HOH HOH A . 
B 2 HOH 195 554 549 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
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 2001-11-21 
2 'Structure model' 1 1 2008-04-27 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2023-08-16 
# 
_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' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Data collection'           
4 4 'Structure model' 'Database references'       
5 4 'Structure model' 'Refinement description'    
# 
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 4 'Structure model' chem_comp_atom                
2 4 'Structure model' chem_comp_bond                
3 4 'Structure model' database_2                    
4 4 'Structure model' pdbx_initial_refinement_model 
# 
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 4 'Structure model' '_database_2.pdbx_DOI'                
2 4 'Structure model' '_database_2.pdbx_database_accession' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
AMoRE     phasing          . ? 1 
REFMAC    refinement       . ? 2 
DENZO     'data reduction' . ? 3 
SCALEPACK 'data scaling'   . ? 4 
# 
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 O   A THR 244 ? ? O A HOH 539 ? ? 1.75 
2 1 OH  A TYR 299 ? ? O A HOH 554 ? ? 1.88 
3 1 O   A VAL 136 ? ? O A HOH 501 ? ? 1.97 
4 1 O   A SER 267 ? ? O A HOH 540 ? ? 2.02 
5 1 O   A HOH 430 ? ? O A HOH 526 ? ? 2.10 
6 1 O   A HOH 365 ? ? O A HOH 492 ? ? 2.12 
7 1 CG2 A ILE 265 ? ? O A HOH 553 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 487 ? ? 1_555 O A HOH 536 ? ? 2_846 1.75 
2 1 NH2 A ARG 345 ? ? 1_555 O A HOH 445 ? ? 1_656 1.80 
3 1 NE  A ARG 345 ? ? 1_555 O A HOH 445 ? ? 1_656 2.19 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A GLU 125 ? ? CA A GLU 125 ? ? C   A GLU 125 ? ? 130.75 110.40 20.35 2.00 N 
2 1 NE A ARG 344 ? ? CZ A ARG 344 ? ? NH2 A ARG 344 ? ? 123.75 120.30 3.45  0.50 N 
3 1 NE A ARG 345 ? ? CZ A ARG 345 ? ? NH2 A ARG 345 ? ? 123.90 120.30 3.60  0.50 N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    THR 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     175 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             62.65 
_pdbx_validate_torsion.psi             61.05 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     345 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.179 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
_pdbx_validate_chiral.id              1 
_pdbx_validate_chiral.PDB_model_num   1 
_pdbx_validate_chiral.auth_atom_id    CA 
_pdbx_validate_chiral.label_alt_id    ? 
_pdbx_validate_chiral.auth_asym_id    A 
_pdbx_validate_chiral.auth_comp_id    GLU 
_pdbx_validate_chiral.auth_seq_id     125 
_pdbx_validate_chiral.PDB_ins_code    ? 
_pdbx_validate_chiral.details         PLANAR 
_pdbx_validate_chiral.omega           . 
# 
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 0 A ASP 128 ? OD1 ? A ASP 10  OD1 
2 1 Y 0 A GLN 152 ? OE1 ? A GLN 34  OE1 
3 1 Y 0 A ILE 265 ? CG2 ? A ILE 147 CG2 
# 
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 MET 119 ? A MET 1   
2  1 Y 1 A ALA 120 ? A ALA 2   
3  1 Y 1 A THR 121 ? A THR 3   
4  1 Y 1 A ARG 122 ? A ARG 4   
5  1 Y 1 A ALA 123 ? A ALA 5   
6  1 Y 1 A ASP 124 ? A ASP 6   
7  1 Y 1 A LYS 353 ? A LYS 235 
8  1 Y 1 A ALA 354 ? A ALA 236 
9  1 Y 1 A THR 355 ? A THR 237 
10 1 Y 1 A ARG 356 ? A ARG 238 
11 1 Y 1 A PRO 357 ? A PRO 239 
12 1 Y 1 A ALA 358 ? A ALA 240 
13 1 Y 1 A SER 359 ? A SER 241 
# 
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  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
THR N    N N N 304 
THR CA   C N S 305 
THR C    C N N 306 
THR O    O N N 307 
THR CB   C N R 308 
THR OG1  O N N 309 
THR CG2  C N N 310 
THR OXT  O N N 311 
THR H    H N N 312 
THR H2   H N N 313 
THR HA   H N N 314 
THR HB   H N N 315 
THR HG1  H N N 316 
THR HG21 H N N 317 
THR HG22 H N N 318 
THR HG23 H N N 319 
THR HXT  H N N 320 
TYR N    N N N 321 
TYR CA   C N S 322 
TYR C    C N N 323 
TYR O    O N N 324 
TYR CB   C N N 325 
TYR CG   C Y N 326 
TYR CD1  C Y N 327 
TYR CD2  C Y N 328 
TYR CE1  C Y N 329 
TYR CE2  C Y N 330 
TYR CZ   C Y N 331 
TYR OH   O N N 332 
TYR OXT  O N N 333 
TYR H    H N N 334 
TYR H2   H N N 335 
TYR HA   H N N 336 
TYR HB2  H N N 337 
TYR HB3  H N N 338 
TYR HD1  H N N 339 
TYR HD2  H N N 340 
TYR HE1  H N N 341 
TYR HE2  H N N 342 
TYR HH   H N N 343 
TYR HXT  H N N 344 
VAL N    N N N 345 
VAL CA   C N S 346 
VAL C    C N N 347 
VAL O    O N N 348 
VAL CB   C N N 349 
VAL CG1  C N N 350 
VAL CG2  C N N 351 
VAL OXT  O N N 352 
VAL H    H N N 353 
VAL H2   H N N 354 
VAL HA   H N N 355 
VAL HB   H N N 356 
VAL HG11 H N N 357 
VAL HG12 H N N 358 
VAL HG13 H N N 359 
VAL HG21 H N N 360 
VAL HG22 H N N 361 
VAL HG23 H N N 362 
VAL HXT  H N N 363 
# 
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  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
THR N   CA   sing N N 290 
THR N   H    sing N N 291 
THR N   H2   sing N N 292 
THR CA  C    sing N N 293 
THR CA  CB   sing N N 294 
THR CA  HA   sing N N 295 
THR C   O    doub N N 296 
THR C   OXT  sing N N 297 
THR CB  OG1  sing N N 298 
THR CB  CG2  sing N N 299 
THR CB  HB   sing N N 300 
THR OG1 HG1  sing N N 301 
THR CG2 HG21 sing N N 302 
THR CG2 HG22 sing N N 303 
THR CG2 HG23 sing N N 304 
THR OXT HXT  sing N N 305 
TYR N   CA   sing N N 306 
TYR N   H    sing N N 307 
TYR N   H2   sing N N 308 
TYR CA  C    sing N N 309 
TYR CA  CB   sing N N 310 
TYR CA  HA   sing N N 311 
TYR C   O    doub N N 312 
TYR C   OXT  sing N N 313 
TYR CB  CG   sing N N 314 
TYR CB  HB2  sing N N 315 
TYR CB  HB3  sing N N 316 
TYR CG  CD1  doub Y N 317 
TYR CG  CD2  sing Y N 318 
TYR CD1 CE1  sing Y N 319 
TYR CD1 HD1  sing N N 320 
TYR CD2 CE2  doub Y N 321 
TYR CD2 HD2  sing N N 322 
TYR CE1 CZ   doub Y N 323 
TYR CE1 HE1  sing N N 324 
TYR CE2 CZ   sing Y N 325 
TYR CE2 HE2  sing N N 326 
TYR CZ  OH   sing N N 327 
TYR OH  HH   sing N N 328 
TYR OXT HXT  sing N N 329 
VAL N   CA   sing N N 330 
VAL N   H    sing N N 331 
VAL N   H2   sing N N 332 
VAL CA  C    sing N N 333 
VAL CA  CB   sing N N 334 
VAL CA  HA   sing N N 335 
VAL C   O    doub N N 336 
VAL C   OXT  sing N N 337 
VAL CB  CG1  sing N N 338 
VAL CB  CG2  sing N N 339 
VAL CB  HB   sing N N 340 
VAL CG1 HG11 sing N N 341 
VAL CG1 HG12 sing N N 342 
VAL CG1 HG13 sing N N 343 
VAL CG2 HG21 sing N N 344 
VAL CG2 HG22 sing N N 345 
VAL CG2 HG23 sing N N 346 
VAL OXT HXT  sing N N 347 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1IKN 
_pdbx_initial_refinement_model.details          ? 
#