scripts/msa/data/mmcif/102m.cif

data_102M
# 
_entry.id   102M 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.389 
_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   102M         pdb_0000102m 10.2210/pdb102m/pdb 
WWPDB D_1000170006 ?            ?                   
# 
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 1998-04-08 
2 'Structure model' 1 1 2008-03-24 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2018-03-07 
5 'Structure model' 1 4 2021-11-03 
6 'Structure model' 1 5 2024-02-07 
7 'Structure model' 1 6 2024-04-03 
# 
_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' Other                       
5 5 'Structure model' 'Database references'       
6 5 'Structure model' 'Derived calculations'      
7 6 'Structure model' 'Data collection'           
8 7 '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' diffrn_source                 
2 4 'Structure model' pdbx_database_status          
3 5 'Structure model' database_2                    
4 5 'Structure model' struct_conn                   
5 5 'Structure model' struct_ref_seq_dif            
6 5 'Structure model' struct_site                   
7 6 'Structure model' chem_comp_atom                
8 6 'Structure model' chem_comp_bond                
9 7 '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' '_diffrn_source.source'               
2  4 'Structure model' '_pdbx_database_status.process_site'  
3  5 'Structure model' '_database_2.pdbx_DOI'                
4  5 'Structure model' '_database_2.pdbx_database_accession' 
5  5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'     
6  5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'      
7  5 'Structure model' '_struct_conn.ptnr1_label_asym_id'    
8  5 'Structure model' '_struct_conn.ptnr1_label_atom_id'    
9  5 'Structure model' '_struct_conn.ptnr1_label_comp_id'    
10 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'     
11 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'     
12 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'      
13 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'    
14 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'    
15 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'    
16 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'     
17 5 'Structure model' '_struct_ref_seq_dif.details'         
18 5 'Structure model' '_struct_site.pdbx_auth_asym_id'      
19 5 'Structure model' '_struct_site.pdbx_auth_comp_id'      
20 5 'Structure model' '_struct_site.pdbx_auth_seq_id'       
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        102M 
_pdbx_database_status.recvd_initial_deposition_date   1997-12-15 
_pdbx_database_status.deposit_site                    ? 
_pdbx_database_status.process_site                    BNL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Smith, R.D.'        1 
'Olson, J.S.'        2 
'Phillips Jr., G.N.' 3 
# 
_citation.id                        primary 
_citation.title                     
'Correlations between Bound N-Alkyl Isocyanide Orientations and Pathways for Ligand Binding in Recombinant Myoglobins' 
_citation.journal_abbrev            'Thesis, Rice' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      1999 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0806 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   -1 
_citation.pdbx_database_id_DOI      ? 
# 
_citation_author.citation_id        primary 
_citation_author.name               'Smith, R.D.' 
_citation_author.ordinal            1 
_citation_author.identifier_ORCID   ? 
# 
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 MYOGLOBIN                         17298.094 1   ? 'INS(M0), H64A, D122N' ? ? 
2 non-polymer syn 'SULFATE ION'                     96.063    1   ? ?                      ? ? 
3 non-polymer syn 'PROTOPORPHYRIN IX CONTAINING FE' 616.487   1   ? ?                      ? ? 
4 water       nat water                             18.015    155 ? ?                      ? ? 
# 
_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       
;MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKAGVTVLTALGAILKKK
GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGNFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MVLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKAGVTVLTALGAILKKK
GHHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGNFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SULFATE ION'                     SO4 
3 'PROTOPORPHYRIN IX CONTAINING FE' HEM 
4 water                             HOH 
# 
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   VAL n 
1 3   LEU n 
1 4   SER n 
1 5   GLU n 
1 6   GLY n 
1 7   GLU n 
1 8   TRP n 
1 9   GLN n 
1 10  LEU n 
1 11  VAL n 
1 12  LEU n 
1 13  HIS n 
1 14  VAL n 
1 15  TRP n 
1 16  ALA n 
1 17  LYS n 
1 18  VAL n 
1 19  GLU n 
1 20  ALA n 
1 21  ASP n 
1 22  VAL n 
1 23  ALA n 
1 24  GLY n 
1 25  HIS n 
1 26  GLY n 
1 27  GLN n 
1 28  ASP n 
1 29  ILE n 
1 30  LEU n 
1 31  ILE n 
1 32  ARG n 
1 33  LEU n 
1 34  PHE n 
1 35  LYS n 
1 36  SER n 
1 37  HIS n 
1 38  PRO n 
1 39  GLU n 
1 40  THR n 
1 41  LEU n 
1 42  GLU n 
1 43  LYS n 
1 44  PHE n 
1 45  ASP n 
1 46  ARG n 
1 47  PHE n 
1 48  LYS n 
1 49  HIS n 
1 50  LEU n 
1 51  LYS n 
1 52  THR n 
1 53  GLU n 
1 54  ALA n 
1 55  GLU n 
1 56  MET n 
1 57  LYS n 
1 58  ALA n 
1 59  SER n 
1 60  GLU n 
1 61  ASP n 
1 62  LEU n 
1 63  LYS n 
1 64  LYS n 
1 65  ALA n 
1 66  GLY n 
1 67  VAL n 
1 68  THR n 
1 69  VAL n 
1 70  LEU n 
1 71  THR n 
1 72  ALA n 
1 73  LEU n 
1 74  GLY n 
1 75  ALA n 
1 76  ILE n 
1 77  LEU n 
1 78  LYS n 
1 79  LYS n 
1 80  LYS n 
1 81  GLY n 
1 82  HIS n 
1 83  HIS n 
1 84  GLU n 
1 85  ALA n 
1 86  GLU n 
1 87  LEU n 
1 88  LYS n 
1 89  PRO n 
1 90  LEU n 
1 91  ALA n 
1 92  GLN n 
1 93  SER n 
1 94  HIS n 
1 95  ALA n 
1 96  THR n 
1 97  LYS n 
1 98  HIS n 
1 99  LYS n 
1 100 ILE n 
1 101 PRO n 
1 102 ILE n 
1 103 LYS n 
1 104 TYR n 
1 105 LEU n 
1 106 GLU n 
1 107 PHE n 
1 108 ILE n 
1 109 SER n 
1 110 GLU n 
1 111 ALA n 
1 112 ILE n 
1 113 ILE n 
1 114 HIS n 
1 115 VAL n 
1 116 LEU n 
1 117 HIS n 
1 118 SER n 
1 119 ARG n 
1 120 HIS n 
1 121 PRO n 
1 122 GLY n 
1 123 ASN n 
1 124 PHE n 
1 125 GLY n 
1 126 ALA n 
1 127 ASP n 
1 128 ALA n 
1 129 GLN n 
1 130 GLY n 
1 131 ALA n 
1 132 MET n 
1 133 ASN n 
1 134 LYS n 
1 135 ALA n 
1 136 LEU n 
1 137 GLU n 
1 138 LEU n 
1 139 PHE n 
1 140 ARG n 
1 141 LYS n 
1 142 ASP n 
1 143 ILE n 
1 144 ALA n 
1 145 ALA n 
1 146 LYS n 
1 147 TYR n 
1 148 LYS n 
1 149 GLU n 
1 150 LEU n 
1 151 GLY n 
1 152 TYR n 
1 153 GLN n 
1 154 GLY 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               'sperm whale' 
_entity_src_gen.gene_src_genus                     Physeter 
_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                    'SKELETAL MUSCLE' 
_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      'Physeter catodon' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9755 
_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                SKELETAL 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    CYTOPLASM 
_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               'PHAGE RESISTANT TB1' 
_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          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'PEMBL 19+' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
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  
HEM non-polymer         . 'PROTOPORPHYRIN IX CONTAINING FE' HEME 'C34 H32 Fe N4 O4' 616.487 
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 
SO4 non-polymer         . 'SULFATE ION'                     ?    'O4 S -2'          96.063  
THR 'L-peptide linking' y THREONINE                         ?    'C4 H9 N O3'       119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                        ?    'C11 H12 N2 O2'    204.225 
TYR 'L-peptide linking' y TYROSINE                          ?    'C9 H11 N O3'      181.189 
VAL 'L-peptide linking' y VALINE                            ?    'C5 H11 N O2'      117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   0   0   MET MET A . n 
A 1 2   VAL 2   1   1   VAL VAL A . n 
A 1 3   LEU 3   2   2   LEU LEU A . n 
A 1 4   SER 4   3   3   SER SER A . n 
A 1 5   GLU 5   4   4   GLU GLU A . n 
A 1 6   GLY 6   5   5   GLY GLY A . n 
A 1 7   GLU 7   6   6   GLU GLU A . n 
A 1 8   TRP 8   7   7   TRP TRP A . n 
A 1 9   GLN 9   8   8   GLN GLN A . n 
A 1 10  LEU 10  9   9   LEU LEU A . n 
A 1 11  VAL 11  10  10  VAL VAL A . n 
A 1 12  LEU 12  11  11  LEU LEU A . n 
A 1 13  HIS 13  12  12  HIS HIS A . n 
A 1 14  VAL 14  13  13  VAL VAL A . n 
A 1 15  TRP 15  14  14  TRP TRP A . n 
A 1 16  ALA 16  15  15  ALA ALA A . n 
A 1 17  LYS 17  16  16  LYS LYS A . n 
A 1 18  VAL 18  17  17  VAL VAL A . n 
A 1 19  GLU 19  18  18  GLU GLU A . n 
A 1 20  ALA 20  19  19  ALA ALA A . n 
A 1 21  ASP 21  20  20  ASP ASP A . n 
A 1 22  VAL 22  21  21  VAL VAL A . n 
A 1 23  ALA 23  22  22  ALA ALA A . n 
A 1 24  GLY 24  23  23  GLY GLY A . n 
A 1 25  HIS 25  24  24  HIS HIS A . n 
A 1 26  GLY 26  25  25  GLY GLY A . n 
A 1 27  GLN 27  26  26  GLN GLN A . n 
A 1 28  ASP 28  27  27  ASP ASP A . n 
A 1 29  ILE 29  28  28  ILE ILE A . n 
A 1 30  LEU 30  29  29  LEU LEU A . n 
A 1 31  ILE 31  30  30  ILE ILE A . n 
A 1 32  ARG 32  31  31  ARG ARG A . n 
A 1 33  LEU 33  32  32  LEU LEU A . n 
A 1 34  PHE 34  33  33  PHE PHE A . n 
A 1 35  LYS 35  34  34  LYS LYS A . n 
A 1 36  SER 36  35  35  SER SER A . n 
A 1 37  HIS 37  36  36  HIS HIS A . n 
A 1 38  PRO 38  37  37  PRO PRO A . n 
A 1 39  GLU 39  38  38  GLU GLU A . n 
A 1 40  THR 40  39  39  THR THR A . n 
A 1 41  LEU 41  40  40  LEU LEU A . n 
A 1 42  GLU 42  41  41  GLU GLU A . n 
A 1 43  LYS 43  42  42  LYS LYS A . n 
A 1 44  PHE 44  43  43  PHE PHE A . n 
A 1 45  ASP 45  44  44  ASP ASP A . n 
A 1 46  ARG 46  45  45  ARG ARG A . n 
A 1 47  PHE 47  46  46  PHE PHE A . n 
A 1 48  LYS 48  47  47  LYS LYS A . n 
A 1 49  HIS 49  48  48  HIS HIS A . n 
A 1 50  LEU 50  49  49  LEU LEU A . n 
A 1 51  LYS 51  50  50  LYS LYS A . n 
A 1 52  THR 52  51  51  THR THR A . n 
A 1 53  GLU 53  52  52  GLU GLU A . n 
A 1 54  ALA 54  53  53  ALA ALA A . n 
A 1 55  GLU 55  54  54  GLU GLU A . n 
A 1 56  MET 56  55  55  MET MET A . n 
A 1 57  LYS 57  56  56  LYS LYS A . n 
A 1 58  ALA 58  57  57  ALA ALA A . n 
A 1 59  SER 59  58  58  SER SER A . n 
A 1 60  GLU 60  59  59  GLU GLU A . n 
A 1 61  ASP 61  60  60  ASP ASP A . n 
A 1 62  LEU 62  61  61  LEU LEU A . n 
A 1 63  LYS 63  62  62  LYS LYS A . n 
A 1 64  LYS 64  63  63  LYS LYS A . n 
A 1 65  ALA 65  64  64  ALA ALA A . n 
A 1 66  GLY 66  65  65  GLY GLY A . n 
A 1 67  VAL 67  66  66  VAL VAL A . n 
A 1 68  THR 68  67  67  THR THR A . n 
A 1 69  VAL 69  68  68  VAL VAL A . n 
A 1 70  LEU 70  69  69  LEU LEU A . n 
A 1 71  THR 71  70  70  THR THR A . n 
A 1 72  ALA 72  71  71  ALA ALA A . n 
A 1 73  LEU 73  72  72  LEU LEU A . n 
A 1 74  GLY 74  73  73  GLY GLY A . n 
A 1 75  ALA 75  74  74  ALA ALA A . n 
A 1 76  ILE 76  75  75  ILE ILE A . n 
A 1 77  LEU 77  76  76  LEU LEU A . n 
A 1 78  LYS 78  77  77  LYS LYS A . n 
A 1 79  LYS 79  78  78  LYS LYS A . n 
A 1 80  LYS 80  79  79  LYS LYS A . n 
A 1 81  GLY 81  80  80  GLY GLY A . n 
A 1 82  HIS 82  81  81  HIS HIS A . n 
A 1 83  HIS 83  82  82  HIS HIS A . n 
A 1 84  GLU 84  83  83  GLU GLU A . n 
A 1 85  ALA 85  84  84  ALA ALA A . n 
A 1 86  GLU 86  85  85  GLU GLU A . n 
A 1 87  LEU 87  86  86  LEU LEU A . n 
A 1 88  LYS 88  87  87  LYS LYS A . n 
A 1 89  PRO 89  88  88  PRO PRO A . n 
A 1 90  LEU 90  89  89  LEU LEU A . n 
A 1 91  ALA 91  90  90  ALA ALA A . n 
A 1 92  GLN 92  91  91  GLN GLN A . n 
A 1 93  SER 93  92  92  SER SER A . n 
A 1 94  HIS 94  93  93  HIS HIS A . n 
A 1 95  ALA 95  94  94  ALA ALA A . n 
A 1 96  THR 96  95  95  THR THR A . n 
A 1 97  LYS 97  96  96  LYS LYS A . n 
A 1 98  HIS 98  97  97  HIS HIS A . n 
A 1 99  LYS 99  98  98  LYS LYS A . n 
A 1 100 ILE 100 99  99  ILE ILE A . n 
A 1 101 PRO 101 100 100 PRO PRO A . n 
A 1 102 ILE 102 101 101 ILE ILE A . n 
A 1 103 LYS 103 102 102 LYS LYS A . n 
A 1 104 TYR 104 103 103 TYR TYR A . n 
A 1 105 LEU 105 104 104 LEU LEU A . n 
A 1 106 GLU 106 105 105 GLU GLU A . n 
A 1 107 PHE 107 106 106 PHE PHE A . n 
A 1 108 ILE 108 107 107 ILE ILE A . n 
A 1 109 SER 109 108 108 SER SER A . n 
A 1 110 GLU 110 109 109 GLU GLU A . n 
A 1 111 ALA 111 110 110 ALA ALA A . n 
A 1 112 ILE 112 111 111 ILE ILE A . n 
A 1 113 ILE 113 112 112 ILE ILE A . n 
A 1 114 HIS 114 113 113 HIS HIS A . n 
A 1 115 VAL 115 114 114 VAL VAL A . n 
A 1 116 LEU 116 115 115 LEU LEU A . n 
A 1 117 HIS 117 116 116 HIS HIS A . n 
A 1 118 SER 118 117 117 SER SER A . n 
A 1 119 ARG 119 118 118 ARG ARG A . n 
A 1 120 HIS 120 119 119 HIS HIS A . n 
A 1 121 PRO 121 120 120 PRO PRO A . n 
A 1 122 GLY 122 121 121 GLY GLY A . n 
A 1 123 ASN 123 122 122 ASN ASN A . n 
A 1 124 PHE 124 123 123 PHE PHE A . n 
A 1 125 GLY 125 124 124 GLY GLY A . n 
A 1 126 ALA 126 125 125 ALA ALA A . n 
A 1 127 ASP 127 126 126 ASP ASP A . n 
A 1 128 ALA 128 127 127 ALA ALA A . n 
A 1 129 GLN 129 128 128 GLN GLN A . n 
A 1 130 GLY 130 129 129 GLY GLY A . n 
A 1 131 ALA 131 130 130 ALA ALA A . n 
A 1 132 MET 132 131 131 MET MET A . n 
A 1 133 ASN 133 132 132 ASN ASN A . n 
A 1 134 LYS 134 133 133 LYS LYS A . n 
A 1 135 ALA 135 134 134 ALA ALA A . n 
A 1 136 LEU 136 135 135 LEU LEU A . n 
A 1 137 GLU 137 136 136 GLU GLU A . n 
A 1 138 LEU 138 137 137 LEU LEU A . n 
A 1 139 PHE 139 138 138 PHE PHE A . n 
A 1 140 ARG 140 139 139 ARG ARG A . n 
A 1 141 LYS 141 140 140 LYS LYS A . n 
A 1 142 ASP 142 141 141 ASP ASP A . n 
A 1 143 ILE 143 142 142 ILE ILE A . n 
A 1 144 ALA 144 143 143 ALA ALA A . n 
A 1 145 ALA 145 144 144 ALA ALA A . n 
A 1 146 LYS 146 145 145 LYS LYS A . n 
A 1 147 TYR 147 146 146 TYR TYR A . n 
A 1 148 LYS 148 147 147 LYS LYS A . n 
A 1 149 GLU 149 148 148 GLU GLU A . n 
A 1 150 LEU 150 149 149 LEU LEU A . n 
A 1 151 GLY 151 150 150 GLY GLY A . n 
A 1 152 TYR 152 151 151 TYR TYR A . n 
A 1 153 GLN 153 152 152 GLN GLN A . n 
A 1 154 GLY 154 153 153 GLY GLY 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 SO4 1   157 157 SO4 SO4 A . 
C 3 HEM 1   155 155 HEM HEM A . 
D 4 HOH 1   156 156 HOH HOH A . 
D 4 HOH 2   201 201 HOH HOH A . 
D 4 HOH 3   202 202 HOH HOH A . 
D 4 HOH 4   203 203 HOH HOH A . 
D 4 HOH 5   204 204 HOH HOH A . 
D 4 HOH 6   205 205 HOH HOH A . 
D 4 HOH 7   206 206 HOH HOH A . 
D 4 HOH 8   207 207 HOH HOH A . 
D 4 HOH 9   208 208 HOH HOH A . 
D 4 HOH 10  209 209 HOH HOH A . 
D 4 HOH 11  210 210 HOH HOH A . 
D 4 HOH 12  211 211 HOH HOH A . 
D 4 HOH 13  212 212 HOH HOH A . 
D 4 HOH 14  213 213 HOH HOH A . 
D 4 HOH 15  214 214 HOH HOH A . 
D 4 HOH 16  215 215 HOH HOH A . 
D 4 HOH 17  216 216 HOH HOH A . 
D 4 HOH 18  217 217 HOH HOH A . 
D 4 HOH 19  218 218 HOH HOH A . 
D 4 HOH 20  219 219 HOH HOH A . 
D 4 HOH 21  220 220 HOH HOH A . 
D 4 HOH 22  221 221 HOH HOH A . 
D 4 HOH 23  222 222 HOH HOH A . 
D 4 HOH 24  223 223 HOH HOH A . 
D 4 HOH 25  224 224 HOH HOH A . 
D 4 HOH 26  225 225 HOH HOH A . 
D 4 HOH 27  226 226 HOH HOH A . 
D 4 HOH 28  227 227 HOH HOH A . 
D 4 HOH 29  228 228 HOH HOH A . 
D 4 HOH 30  229 229 HOH HOH A . 
D 4 HOH 31  230 230 HOH HOH A . 
D 4 HOH 32  231 231 HOH HOH A . 
D 4 HOH 33  232 232 HOH HOH A . 
D 4 HOH 34  233 233 HOH HOH A . 
D 4 HOH 35  234 234 HOH HOH A . 
D 4 HOH 36  235 235 HOH HOH A . 
D 4 HOH 37  236 236 HOH HOH A . 
D 4 HOH 38  237 237 HOH HOH A . 
D 4 HOH 39  238 238 HOH HOH A . 
D 4 HOH 40  239 239 HOH HOH A . 
D 4 HOH 41  240 240 HOH HOH A . 
D 4 HOH 42  241 241 HOH HOH A . 
D 4 HOH 43  242 242 HOH HOH A . 
D 4 HOH 44  243 243 HOH HOH A . 
D 4 HOH 45  244 244 HOH HOH A . 
D 4 HOH 46  245 245 HOH HOH A . 
D 4 HOH 47  246 246 HOH HOH A . 
D 4 HOH 48  247 247 HOH HOH A . 
D 4 HOH 49  248 248 HOH HOH A . 
D 4 HOH 50  249 249 HOH HOH A . 
D 4 HOH 51  250 250 HOH HOH A . 
D 4 HOH 52  251 251 HOH HOH A . 
D 4 HOH 53  252 252 HOH HOH A . 
D 4 HOH 54  253 253 HOH HOH A . 
D 4 HOH 55  254 254 HOH HOH A . 
D 4 HOH 56  255 255 HOH HOH A . 
D 4 HOH 57  256 256 HOH HOH A . 
D 4 HOH 58  257 257 HOH HOH A . 
D 4 HOH 59  258 258 HOH HOH A . 
D 4 HOH 60  259 259 HOH HOH A . 
D 4 HOH 61  260 260 HOH HOH A . 
D 4 HOH 62  261 261 HOH HOH A . 
D 4 HOH 63  262 262 HOH HOH A . 
D 4 HOH 64  263 263 HOH HOH A . 
D 4 HOH 65  264 264 HOH HOH A . 
D 4 HOH 66  265 265 HOH HOH A . 
D 4 HOH 67  266 266 HOH HOH A . 
D 4 HOH 68  267 267 HOH HOH A . 
D 4 HOH 69  268 268 HOH HOH A . 
D 4 HOH 70  269 269 HOH HOH A . 
D 4 HOH 71  270 270 HOH HOH A . 
D 4 HOH 72  271 271 HOH HOH A . 
D 4 HOH 73  272 272 HOH HOH A . 
D 4 HOH 74  273 273 HOH HOH A . 
D 4 HOH 75  274 274 HOH HOH A . 
D 4 HOH 76  275 275 HOH HOH A . 
D 4 HOH 77  276 276 HOH HOH A . 
D 4 HOH 78  277 277 HOH HOH A . 
D 4 HOH 79  278 278 HOH HOH A . 
D 4 HOH 80  279 279 HOH HOH A . 
D 4 HOH 81  280 280 HOH HOH A . 
D 4 HOH 82  281 281 HOH HOH A . 
D 4 HOH 83  282 282 HOH HOH A . 
D 4 HOH 84  283 283 HOH HOH A . 
D 4 HOH 85  284 284 HOH HOH A . 
D 4 HOH 86  285 285 HOH HOH A . 
D 4 HOH 87  286 286 HOH HOH A . 
D 4 HOH 88  287 287 HOH HOH A . 
D 4 HOH 89  288 288 HOH HOH A . 
D 4 HOH 90  289 289 HOH HOH A . 
D 4 HOH 91  290 290 HOH HOH A . 
D 4 HOH 92  291 291 HOH HOH A . 
D 4 HOH 93  292 292 HOH HOH A . 
D 4 HOH 94  293 293 HOH HOH A . 
D 4 HOH 95  294 294 HOH HOH A . 
D 4 HOH 96  295 295 HOH HOH A . 
D 4 HOH 97  296 296 HOH HOH A . 
D 4 HOH 98  297 297 HOH HOH A . 
D 4 HOH 99  298 298 HOH HOH A . 
D 4 HOH 100 299 299 HOH HOH A . 
D 4 HOH 101 300 300 HOH HOH A . 
D 4 HOH 102 301 301 HOH HOH A . 
D 4 HOH 103 302 302 HOH HOH A . 
D 4 HOH 104 303 303 HOH HOH A . 
D 4 HOH 105 304 304 HOH HOH A . 
D 4 HOH 106 305 305 HOH HOH A . 
D 4 HOH 107 306 306 HOH HOH A . 
D 4 HOH 108 307 307 HOH HOH A . 
D 4 HOH 109 308 308 HOH HOH A . 
D 4 HOH 110 309 309 HOH HOH A . 
D 4 HOH 111 310 310 HOH HOH A . 
D 4 HOH 112 311 311 HOH HOH A . 
D 4 HOH 113 312 312 HOH HOH A . 
D 4 HOH 114 313 313 HOH HOH A . 
D 4 HOH 115 314 314 HOH HOH A . 
D 4 HOH 116 315 315 HOH HOH A . 
D 4 HOH 117 316 316 HOH HOH A . 
D 4 HOH 118 317 317 HOH HOH A . 
D 4 HOH 119 318 318 HOH HOH A . 
D 4 HOH 120 319 319 HOH HOH A . 
D 4 HOH 121 320 320 HOH HOH A . 
D 4 HOH 122 321 321 HOH HOH A . 
D 4 HOH 123 322 322 HOH HOH A . 
D 4 HOH 124 323 323 HOH HOH A . 
D 4 HOH 125 324 324 HOH HOH A . 
D 4 HOH 126 325 325 HOH HOH A . 
D 4 HOH 127 326 326 HOH HOH A . 
D 4 HOH 128 327 327 HOH HOH A . 
D 4 HOH 129 328 328 HOH HOH A . 
D 4 HOH 130 329 329 HOH HOH A . 
D 4 HOH 131 330 330 HOH HOH A . 
D 4 HOH 132 331 331 HOH HOH A . 
D 4 HOH 133 332 332 HOH HOH A . 
D 4 HOH 134 333 333 HOH HOH A . 
D 4 HOH 135 334 334 HOH HOH A . 
D 4 HOH 136 335 335 HOH HOH A . 
D 4 HOH 137 336 336 HOH HOH A . 
D 4 HOH 138 337 337 HOH HOH A . 
D 4 HOH 139 338 338 HOH HOH A . 
D 4 HOH 140 339 339 HOH HOH A . 
D 4 HOH 141 340 340 HOH HOH A . 
D 4 HOH 142 341 341 HOH HOH A . 
D 4 HOH 143 342 342 HOH HOH A . 
D 4 HOH 144 343 343 HOH HOH A . 
D 4 HOH 145 344 344 HOH HOH A . 
D 4 HOH 146 345 345 HOH HOH A . 
D 4 HOH 147 346 346 HOH HOH A . 
D 4 HOH 148 347 347 HOH HOH A . 
D 4 HOH 149 348 348 HOH HOH A . 
D 4 HOH 150 349 349 HOH HOH A . 
D 4 HOH 151 350 350 HOH HOH A . 
D 4 HOH 152 351 351 HOH HOH A . 
D 4 HOH 153 352 352 HOH HOH A . 
D 4 HOH 154 353 353 HOH HOH A . 
D 4 HOH 155 354 354 HOH HOH A . 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
X-PLOR 'model building' 3.851 ? 1 
X-PLOR refinement       3.851 ? 2 
XDS    'data reduction' .     ? 3 
XSCALE 'data scaling'   .     ? 4 
X-PLOR phasing          3.851 ? 5 
# 
_cell.entry_id           102M 
_cell.length_a           91.433 
_cell.length_b           91.433 
_cell.length_c           45.949 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              6 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         102M 
_symmetry.space_group_name_H-M             'P 6' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                168 
# 
_exptl.entry_id          102M 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.09 
_exptl_crystal.density_percent_sol   60.2 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              9.0 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '3.0 M AMMONIUM SULFATE, 20 MM TRIS, 1MM EDTA, PH 9.0' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           292 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   RIGAKU 
_diffrn_detector.pdbx_collection_date   1996-10 
_diffrn_detector.details                'PINHOLE COLLIMATOR' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'GRAPHITE(002)' 
_diffrn_radiation.pdbx_diffrn_protocol             ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        SIEMENS 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             1.5418 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     102M 
_reflns.observed_criterion_sigma_I   0. 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             6.00 
_reflns.d_resolution_high            1.84 
_reflns.number_obs                   17484 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         90.9 
_reflns.pdbx_Rmerge_I_obs            0.0620000 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        12.3 
_reflns.pdbx_redundancy              5.63 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.84 
_reflns_shell.d_res_low              1.85 
_reflns_shell.percent_possible_all   98.4 
_reflns_shell.Rmerge_I_obs           0.2670000 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        4.35 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 102M 
_refine.ls_number_reflns_obs                     16364 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               10000000.00 
_refine.pdbx_data_cutoff_low_absF                0.00100 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             5.00 
_refine.ls_d_res_high                            1.84 
_refine.ls_percent_reflns_obs                    89.8 
_refine.ls_R_factor_obs                          0.1590000 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1590000 
_refine.ls_R_factor_R_free                       0.2030000 
_refine.ls_R_factor_R_free_error                 0.005 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 9.9 
_refine.ls_number_reflns_R_free                  1623 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               19.5 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'SPERM WHALE MYOGLOBIN 0M, D122N (DEOXY)' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             RESTRAINED 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        102M 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_refine_analyze.Luzzati_sigma_a_obs             0.16 
_refine_analyze.Luzzati_d_res_low_obs           5.00 
_refine_analyze.Luzzati_coordinate_error_free   0.20 
_refine_analyze.Luzzati_sigma_a_free            0.16 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1220 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         44 
_refine_hist.number_atoms_solvent             159 
_refine_hist.number_atoms_total               1423 
_refine_hist.d_res_high                       1.84 
_refine_hist.d_res_low                        5.00 
# 
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 
x_bond_d                0.009 ?    ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_na             ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_bond_d_prot           ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d               ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_na            ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_d_prot          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg             1.4   ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_na          ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_angle_deg_prot        ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d      18.7  ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_dihedral_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d      1.20  ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_na   ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_improper_angle_d_prot ?     ?    ? ? 'X-RAY DIFFRACTION' ? 
x_mcbond_it             2.01  1.50 ? ? 'X-RAY DIFFRACTION' ? 
x_mcangle_it            2.51  2.00 ? ? 'X-RAY DIFFRACTION' ? 
x_scbond_it             7.32  2.50 ? ? 'X-RAY DIFFRACTION' ? 
x_scangle_it            11.08 2.50 ? ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   8 
_refine_ls_shell.d_res_high                       1.84 
_refine_ls_shell.d_res_low                        1.92 
_refine_ls_shell.number_reflns_R_work             1941 
_refine_ls_shell.R_factor_R_work                  0.2270000 
_refine_ls_shell.percent_reflns_obs               94.5 
_refine_ls_shell.R_factor_R_free                  0.2580000 
_refine_ls_shell.R_factor_R_free_error            0.018 
_refine_ls_shell.percent_reflns_R_free            9.3 
_refine_ls_shell.number_reflns_R_free             200 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
loop_
_pdbx_xplor_file.serial_no 
_pdbx_xplor_file.param_file 
_pdbx_xplor_file.topol_file 
_pdbx_xplor_file.pdbx_refine_id 
1 PARHCSDX.PRO   TOPHCSDX.PRO  'X-RAY DIFFRACTION' 
2 PARAMETER.HEME TOPOLOGY.HEME 'X-RAY DIFFRACTION' 
3 PARAM19.SOLV   TOPH19.SOLV   'X-RAY DIFFRACTION' 
4 PARAM19.SOLV   TOPH19.SOLV   'X-RAY DIFFRACTION' 
# 
_database_PDB_matrix.entry_id          102M 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_struct.entry_id                  102M 
_struct.title                     'SPERM WHALE MYOGLOBIN H64A AQUOMET AT PH 9.0' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        102M 
_struct_keywords.pdbx_keywords   'OXYGEN TRANSPORT' 
_struct_keywords.text            'LIGAND BINDING, OXYGEN STORAGE, OXYGEN BINDING, HEME, OXYGEN TRANSPORT' 
# 
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 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    MYG_PHYCA 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P02185 
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_seq_one_letter_code   
;VLSEGEWQLVLHVWAKVEADVAGHGQDILIRLFKSHPETLEKFDRFKHLKTEAEMKASEDLKKHGVTVLTALGAILKKKG
HHEAELKPLAQSHATKHKIPIKYLEFISEAIIHVLHSRHPGDFGADAQGAMNKALELFRKDIAAKYKELGYQG
;
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              102M 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 2 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 154 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P02185 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  153 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 102M ALA A 65  ? UNP P02185 HIS 64  'engineered mutation' 64  1 
1 102M ASN A 123 ? UNP P02185 ASP 122 'engineered mutation' 122 2 
# 
_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,C,D 
# 
_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 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 SER A 4   ? GLU A 19  ? SER A 3   GLU A 18  1 ? 16 
HELX_P HELX_P2 2 ASP A 21  ? SER A 36  ? ASP A 20  SER A 35  1 ? 16 
HELX_P HELX_P3 3 HIS A 37  ? LYS A 43  ? HIS A 36  LYS A 42  1 ? 7  
HELX_P HELX_P4 4 THR A 52  ? ALA A 58  ? THR A 51  ALA A 57  1 ? 7  
HELX_P HELX_P5 5 SER A 59  ? LYS A 78  ? SER A 58  LYS A 77  1 ? 20 
HELX_P HELX_P6 6 LEU A 87  ? ALA A 95  ? LEU A 86  ALA A 94  1 ? 9  
HELX_P HELX_P7 7 PRO A 101 ? ARG A 119 ? PRO A 100 ARG A 118 1 ? 19 
HELX_P HELX_P8 8 GLY A 125 ? LEU A 150 ? GLY A 124 LEU A 149 1 ? 26 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A HIS 94 NE2 ? ? ? 1_555 C HEM . FE ? ? A HIS 93  A HEM 155 1_555 ? ? ? ? ? ? ? 2.103 ? ? 
metalc2 metalc ? ? C HEM .  FE  ? ? ? 1_555 D HOH . O  ? ? A HEM 155 A HOH 156 1_555 ? ? ? ? ? ? ? 2.100 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NA ? C HEM . ? A HEM 155 ? 1_555 88.6  ? 
2  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NB ? C HEM . ? A HEM 155 ? 1_555 89.1  ? 
3  NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NB ? C HEM . ? A HEM 155 ? 1_555 88.8  ? 
4  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NC ? C HEM . ? A HEM 155 ? 1_555 94.8  ? 
5  NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NC ? C HEM . ? A HEM 155 ? 1_555 176.5 ? 
6  NB  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 NC ? C HEM . ? A HEM 155 ? 1_555 91.1  ? 
7  NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 92.8  ? 
8  NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 91.1  ? 
9  NB  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 178.1 ? 
10 NC  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 ND ? C HEM . ? A HEM 155 ? 1_555 88.9  ? 
11 NE2 ? A HIS 94 ? A HIS 93  ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 O  ? D HOH . ? A HOH 156 ? 1_555 177.2 ? 
12 NA  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 O  ? D HOH . ? A HOH 156 ? 1_555 90.5  ? 
13 NB  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 O  ? D HOH . ? A HOH 156 ? 1_555 93.5  ? 
14 NC  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 O  ? D HOH . ? A HOH 156 ? 1_555 86.0  ? 
15 ND  ? C HEM .  ? A HEM 155 ? 1_555 FE ? C HEM . ? A HEM 155 ? 1_555 O  ? D HOH . ? A HOH 156 ? 1_555 84.5  ? 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
HEM Unknown  ? ?   ?   ? 1  'LIGAND BINDING SITE.'               
AC1 Software A SO4 157 ? 5  'BINDING SITE FOR RESIDUE SO4 A 157' 
AC2 Software A HEM 155 ? 13 'BINDING SITE FOR RESIDUE HEM A 155' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  HEM 1  HEM C .   ? HEM A 155 . ? 1_555 ? 
2  AC1 5  SER A 4   ? SER A 3   . ? 1_556 ? 
3  AC1 5  GLU A 5   ? GLU A 4   . ? 1_556 ? 
4  AC1 5  THR A 52  ? THR A 51  . ? 1_555 ? 
5  AC1 5  GLU A 53  ? GLU A 52  . ? 1_555 ? 
6  AC1 5  HOH D .   ? HOH A 297 . ? 1_555 ? 
7  AC2 13 LYS A 43  ? LYS A 42  . ? 1_555 ? 
8  AC2 13 PHE A 44  ? PHE A 43  . ? 1_555 ? 
9  AC2 13 ARG A 46  ? ARG A 45  . ? 1_555 ? 
10 AC2 13 THR A 68  ? THR A 67  . ? 1_555 ? 
11 AC2 13 LEU A 90  ? LEU A 89  . ? 1_555 ? 
12 AC2 13 SER A 93  ? SER A 92  . ? 1_555 ? 
13 AC2 13 HIS A 94  ? HIS A 93  . ? 1_555 ? 
14 AC2 13 HIS A 98  ? HIS A 97  . ? 1_555 ? 
15 AC2 13 ILE A 100 ? ILE A 99  . ? 1_555 ? 
16 AC2 13 TYR A 104 ? TYR A 103 . ? 1_555 ? 
17 AC2 13 HOH D .   ? HOH A 156 . ? 1_555 ? 
18 AC2 13 HOH D .   ? HOH A 308 . ? 1_555 ? 
19 AC2 13 HOH D .   ? HOH A 316 . ? 1_555 ? 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 20  ? ? -150.71 73.37  
2 1 TYR A 151 ? ? -120.06 -69.82 
3 1 GLN A 152 ? ? 45.28   19.32  
# 
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  
GLN N    N  N N 74  
GLN CA   C  N S 75  
GLN C    C  N N 76  
GLN O    O  N N 77  
GLN CB   C  N N 78  
GLN CG   C  N N 79  
GLN CD   C  N N 80  
GLN OE1  O  N N 81  
GLN NE2  N  N N 82  
GLN OXT  O  N N 83  
GLN H    H  N N 84  
GLN H2   H  N N 85  
GLN HA   H  N N 86  
GLN HB2  H  N N 87  
GLN HB3  H  N N 88  
GLN HG2  H  N N 89  
GLN HG3  H  N N 90  
GLN HE21 H  N N 91  
GLN HE22 H  N N 92  
GLN HXT  H  N N 93  
GLU N    N  N N 94  
GLU CA   C  N S 95  
GLU C    C  N N 96  
GLU O    O  N N 97  
GLU CB   C  N N 98  
GLU CG   C  N N 99  
GLU CD   C  N N 100 
GLU OE1  O  N N 101 
GLU OE2  O  N N 102 
GLU OXT  O  N N 103 
GLU H    H  N N 104 
GLU H2   H  N N 105 
GLU HA   H  N N 106 
GLU HB2  H  N N 107 
GLU HB3  H  N N 108 
GLU HG2  H  N N 109 
GLU HG3  H  N N 110 
GLU HE2  H  N N 111 
GLU HXT  H  N N 112 
GLY N    N  N N 113 
GLY CA   C  N N 114 
GLY C    C  N N 115 
GLY O    O  N N 116 
GLY OXT  O  N N 117 
GLY H    H  N N 118 
GLY H2   H  N N 119 
GLY HA2  H  N N 120 
GLY HA3  H  N N 121 
GLY HXT  H  N N 122 
HEM CHA  C  N N 123 
HEM CHB  C  N N 124 
HEM CHC  C  N N 125 
HEM CHD  C  N N 126 
HEM C1A  C  Y N 127 
HEM C2A  C  Y N 128 
HEM C3A  C  Y N 129 
HEM C4A  C  Y N 130 
HEM CMA  C  N N 131 
HEM CAA  C  N N 132 
HEM CBA  C  N N 133 
HEM CGA  C  N N 134 
HEM O1A  O  N N 135 
HEM O2A  O  N N 136 
HEM C1B  C  N N 137 
HEM C2B  C  N N 138 
HEM C3B  C  N N 139 
HEM C4B  C  N N 140 
HEM CMB  C  N N 141 
HEM CAB  C  N N 142 
HEM CBB  C  N N 143 
HEM C1C  C  Y N 144 
HEM C2C  C  Y N 145 
HEM C3C  C  Y N 146 
HEM C4C  C  Y N 147 
HEM CMC  C  N N 148 
HEM CAC  C  N N 149 
HEM CBC  C  N N 150 
HEM C1D  C  N N 151 
HEM C2D  C  N N 152 
HEM C3D  C  N N 153 
HEM C4D  C  N N 154 
HEM CMD  C  N N 155 
HEM CAD  C  N N 156 
HEM CBD  C  N N 157 
HEM CGD  C  N N 158 
HEM O1D  O  N N 159 
HEM O2D  O  N N 160 
HEM NA   N  Y N 161 
HEM NB   N  N N 162 
HEM NC   N  Y N 163 
HEM ND   N  N N 164 
HEM FE   FE N N 165 
HEM HHB  H  N N 166 
HEM HHC  H  N N 167 
HEM HHD  H  N N 168 
HEM HMA  H  N N 169 
HEM HMAA H  N N 170 
HEM HMAB H  N N 171 
HEM HAA  H  N N 172 
HEM HAAA H  N N 173 
HEM HBA  H  N N 174 
HEM HBAA H  N N 175 
HEM HMB  H  N N 176 
HEM HMBA H  N N 177 
HEM HMBB H  N N 178 
HEM HAB  H  N N 179 
HEM HBB  H  N N 180 
HEM HBBA H  N N 181 
HEM HMC  H  N N 182 
HEM HMCA H  N N 183 
HEM HMCB H  N N 184 
HEM HAC  H  N N 185 
HEM HBC  H  N N 186 
HEM HBCA H  N N 187 
HEM HMD  H  N N 188 
HEM HMDA H  N N 189 
HEM HMDB H  N N 190 
HEM HAD  H  N N 191 
HEM HADA H  N N 192 
HEM HBD  H  N N 193 
HEM HBDA H  N N 194 
HEM H2A  H  N N 195 
HEM H2D  H  N N 196 
HEM HHA  H  N N 197 
HIS N    N  N N 198 
HIS CA   C  N S 199 
HIS C    C  N N 200 
HIS O    O  N N 201 
HIS CB   C  N N 202 
HIS CG   C  Y N 203 
HIS ND1  N  Y N 204 
HIS CD2  C  Y N 205 
HIS CE1  C  Y N 206 
HIS NE2  N  Y N 207 
HIS OXT  O  N N 208 
HIS H    H  N N 209 
HIS H2   H  N N 210 
HIS HA   H  N N 211 
HIS HB2  H  N N 212 
HIS HB3  H  N N 213 
HIS HD1  H  N N 214 
HIS HD2  H  N N 215 
HIS HE1  H  N N 216 
HIS HE2  H  N N 217 
HIS HXT  H  N N 218 
HOH O    O  N N 219 
HOH H1   H  N N 220 
HOH H2   H  N N 221 
ILE N    N  N N 222 
ILE CA   C  N S 223 
ILE C    C  N N 224 
ILE O    O  N N 225 
ILE CB   C  N S 226 
ILE CG1  C  N N 227 
ILE CG2  C  N N 228 
ILE CD1  C  N N 229 
ILE OXT  O  N N 230 
ILE H    H  N N 231 
ILE H2   H  N N 232 
ILE HA   H  N N 233 
ILE HB   H  N N 234 
ILE HG12 H  N N 235 
ILE HG13 H  N N 236 
ILE HG21 H  N N 237 
ILE HG22 H  N N 238 
ILE HG23 H  N N 239 
ILE HD11 H  N N 240 
ILE HD12 H  N N 241 
ILE HD13 H  N N 242 
ILE HXT  H  N N 243 
LEU N    N  N N 244 
LEU CA   C  N S 245 
LEU C    C  N N 246 
LEU O    O  N N 247 
LEU CB   C  N N 248 
LEU CG   C  N N 249 
LEU CD1  C  N N 250 
LEU CD2  C  N N 251 
LEU OXT  O  N N 252 
LEU H    H  N N 253 
LEU H2   H  N N 254 
LEU HA   H  N N 255 
LEU HB2  H  N N 256 
LEU HB3  H  N N 257 
LEU HG   H  N N 258 
LEU HD11 H  N N 259 
LEU HD12 H  N N 260 
LEU HD13 H  N N 261 
LEU HD21 H  N N 262 
LEU HD22 H  N N 263 
LEU HD23 H  N N 264 
LEU HXT  H  N N 265 
LYS N    N  N N 266 
LYS CA   C  N S 267 
LYS C    C  N N 268 
LYS O    O  N N 269 
LYS CB   C  N N 270 
LYS CG   C  N N 271 
LYS CD   C  N N 272 
LYS CE   C  N N 273 
LYS NZ   N  N N 274 
LYS OXT  O  N N 275 
LYS H    H  N N 276 
LYS H2   H  N N 277 
LYS HA   H  N N 278 
LYS HB2  H  N N 279 
LYS HB3  H  N N 280 
LYS HG2  H  N N 281 
LYS HG3  H  N N 282 
LYS HD2  H  N N 283 
LYS HD3  H  N N 284 
LYS HE2  H  N N 285 
LYS HE3  H  N N 286 
LYS HZ1  H  N N 287 
LYS HZ2  H  N N 288 
LYS HZ3  H  N N 289 
LYS HXT  H  N N 290 
MET N    N  N N 291 
MET CA   C  N S 292 
MET C    C  N N 293 
MET O    O  N N 294 
MET CB   C  N N 295 
MET CG   C  N N 296 
MET SD   S  N N 297 
MET CE   C  N N 298 
MET OXT  O  N N 299 
MET H    H  N N 300 
MET H2   H  N N 301 
MET HA   H  N N 302 
MET HB2  H  N N 303 
MET HB3  H  N N 304 
MET HG2  H  N N 305 
MET HG3  H  N N 306 
MET HE1  H  N N 307 
MET HE2  H  N N 308 
MET HE3  H  N N 309 
MET HXT  H  N N 310 
PHE N    N  N N 311 
PHE CA   C  N S 312 
PHE C    C  N N 313 
PHE O    O  N N 314 
PHE CB   C  N N 315 
PHE CG   C  Y N 316 
PHE CD1  C  Y N 317 
PHE CD2  C  Y N 318 
PHE CE1  C  Y N 319 
PHE CE2  C  Y N 320 
PHE CZ   C  Y N 321 
PHE OXT  O  N N 322 
PHE H    H  N N 323 
PHE H2   H  N N 324 
PHE HA   H  N N 325 
PHE HB2  H  N N 326 
PHE HB3  H  N N 327 
PHE HD1  H  N N 328 
PHE HD2  H  N N 329 
PHE HE1  H  N N 330 
PHE HE2  H  N N 331 
PHE HZ   H  N N 332 
PHE HXT  H  N N 333 
PRO N    N  N N 334 
PRO CA   C  N S 335 
PRO C    C  N N 336 
PRO O    O  N N 337 
PRO CB   C  N N 338 
PRO CG   C  N N 339 
PRO CD   C  N N 340 
PRO OXT  O  N N 341 
PRO H    H  N N 342 
PRO HA   H  N N 343 
PRO HB2  H  N N 344 
PRO HB3  H  N N 345 
PRO HG2  H  N N 346 
PRO HG3  H  N N 347 
PRO HD2  H  N N 348 
PRO HD3  H  N N 349 
PRO HXT  H  N N 350 
SER N    N  N N 351 
SER CA   C  N S 352 
SER C    C  N N 353 
SER O    O  N N 354 
SER CB   C  N N 355 
SER OG   O  N N 356 
SER OXT  O  N N 357 
SER H    H  N N 358 
SER H2   H  N N 359 
SER HA   H  N N 360 
SER HB2  H  N N 361 
SER HB3  H  N N 362 
SER HG   H  N N 363 
SER HXT  H  N N 364 
SO4 S    S  N N 365 
SO4 O1   O  N N 366 
SO4 O2   O  N N 367 
SO4 O3   O  N N 368 
SO4 O4   O  N N 369 
THR N    N  N N 370 
THR CA   C  N S 371 
THR C    C  N N 372 
THR O    O  N N 373 
THR CB   C  N R 374 
THR OG1  O  N N 375 
THR CG2  C  N N 376 
THR OXT  O  N N 377 
THR H    H  N N 378 
THR H2   H  N N 379 
THR HA   H  N N 380 
THR HB   H  N N 381 
THR HG1  H  N N 382 
THR HG21 H  N N 383 
THR HG22 H  N N 384 
THR HG23 H  N N 385 
THR HXT  H  N N 386 
TRP N    N  N N 387 
TRP CA   C  N S 388 
TRP C    C  N N 389 
TRP O    O  N N 390 
TRP CB   C  N N 391 
TRP CG   C  Y N 392 
TRP CD1  C  Y N 393 
TRP CD2  C  Y N 394 
TRP NE1  N  Y N 395 
TRP CE2  C  Y N 396 
TRP CE3  C  Y N 397 
TRP CZ2  C  Y N 398 
TRP CZ3  C  Y N 399 
TRP CH2  C  Y N 400 
TRP OXT  O  N N 401 
TRP H    H  N N 402 
TRP H2   H  N N 403 
TRP HA   H  N N 404 
TRP HB2  H  N N 405 
TRP HB3  H  N N 406 
TRP HD1  H  N N 407 
TRP HE1  H  N N 408 
TRP HE3  H  N N 409 
TRP HZ2  H  N N 410 
TRP HZ3  H  N N 411 
TRP HH2  H  N N 412 
TRP HXT  H  N N 413 
TYR N    N  N N 414 
TYR CA   C  N S 415 
TYR C    C  N N 416 
TYR O    O  N N 417 
TYR CB   C  N N 418 
TYR CG   C  Y N 419 
TYR CD1  C  Y N 420 
TYR CD2  C  Y N 421 
TYR CE1  C  Y N 422 
TYR CE2  C  Y N 423 
TYR CZ   C  Y N 424 
TYR OH   O  N N 425 
TYR OXT  O  N N 426 
TYR H    H  N N 427 
TYR H2   H  N N 428 
TYR HA   H  N N 429 
TYR HB2  H  N N 430 
TYR HB3  H  N N 431 
TYR HD1  H  N N 432 
TYR HD2  H  N N 433 
TYR HE1  H  N N 434 
TYR HE2  H  N N 435 
TYR HH   H  N N 436 
TYR HXT  H  N N 437 
VAL N    N  N N 438 
VAL CA   C  N S 439 
VAL C    C  N N 440 
VAL O    O  N N 441 
VAL CB   C  N N 442 
VAL CG1  C  N N 443 
VAL CG2  C  N N 444 
VAL OXT  O  N N 445 
VAL H    H  N N 446 
VAL H2   H  N N 447 
VAL HA   H  N N 448 
VAL HB   H  N N 449 
VAL HG11 H  N N 450 
VAL HG12 H  N N 451 
VAL HG13 H  N N 452 
VAL HG21 H  N N 453 
VAL HG22 H  N N 454 
VAL HG23 H  N N 455 
VAL HXT  H  N N 456 
# 
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  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HEM CHA C1A  sing N N 116 
HEM CHA C4D  doub N N 117 
HEM CHA HHA  sing N N 118 
HEM CHB C4A  sing N N 119 
HEM CHB C1B  doub N N 120 
HEM CHB HHB  sing N N 121 
HEM CHC C4B  sing N N 122 
HEM CHC C1C  doub N N 123 
HEM CHC HHC  sing N N 124 
HEM CHD C4C  doub N N 125 
HEM CHD C1D  sing N N 126 
HEM CHD HHD  sing N N 127 
HEM C1A C2A  doub Y N 128 
HEM C1A NA   sing Y N 129 
HEM C2A C3A  sing Y N 130 
HEM C2A CAA  sing N N 131 
HEM C3A C4A  doub Y N 132 
HEM C3A CMA  sing N N 133 
HEM C4A NA   sing Y N 134 
HEM CMA HMA  sing N N 135 
HEM CMA HMAA sing N N 136 
HEM CMA HMAB sing N N 137 
HEM CAA CBA  sing N N 138 
HEM CAA HAA  sing N N 139 
HEM CAA HAAA sing N N 140 
HEM CBA CGA  sing N N 141 
HEM CBA HBA  sing N N 142 
HEM CBA HBAA sing N N 143 
HEM CGA O1A  doub N N 144 
HEM CGA O2A  sing N N 145 
HEM C1B C2B  sing N N 146 
HEM C1B NB   sing N N 147 
HEM C2B C3B  doub N N 148 
HEM C2B CMB  sing N N 149 
HEM C3B C4B  sing N N 150 
HEM C3B CAB  sing N N 151 
HEM C4B NB   doub N N 152 
HEM CMB HMB  sing N N 153 
HEM CMB HMBA sing N N 154 
HEM CMB HMBB sing N N 155 
HEM CAB CBB  doub N N 156 
HEM CAB HAB  sing N N 157 
HEM CBB HBB  sing N N 158 
HEM CBB HBBA sing N N 159 
HEM C1C C2C  sing Y N 160 
HEM C1C NC   sing Y N 161 
HEM C2C C3C  doub Y N 162 
HEM C2C CMC  sing N N 163 
HEM C3C C4C  sing Y N 164 
HEM C3C CAC  sing N N 165 
HEM C4C NC   sing Y N 166 
HEM CMC HMC  sing N N 167 
HEM CMC HMCA sing N N 168 
HEM CMC HMCB sing N N 169 
HEM CAC CBC  doub N N 170 
HEM CAC HAC  sing N N 171 
HEM CBC HBC  sing N N 172 
HEM CBC HBCA sing N N 173 
HEM C1D C2D  sing N N 174 
HEM C1D ND   doub N N 175 
HEM C2D C3D  doub N N 176 
HEM C2D CMD  sing N N 177 
HEM C3D C4D  sing N N 178 
HEM C3D CAD  sing N N 179 
HEM C4D ND   sing N N 180 
HEM CMD HMD  sing N N 181 
HEM CMD HMDA sing N N 182 
HEM CMD HMDB sing N N 183 
HEM CAD CBD  sing N N 184 
HEM CAD HAD  sing N N 185 
HEM CAD HADA sing N N 186 
HEM CBD CGD  sing N N 187 
HEM CBD HBD  sing N N 188 
HEM CBD HBDA sing N N 189 
HEM CGD O1D  doub N N 190 
HEM CGD O2D  sing N N 191 
HEM O2A H2A  sing N N 192 
HEM O2D H2D  sing N N 193 
HEM FE  NA   sing N N 194 
HEM FE  NB   sing N N 195 
HEM FE  NC   sing N N 196 
HEM FE  ND   sing N N 197 
HIS N   CA   sing N N 198 
HIS N   H    sing N N 199 
HIS N   H2   sing N N 200 
HIS CA  C    sing N N 201 
HIS CA  CB   sing N N 202 
HIS CA  HA   sing N N 203 
HIS C   O    doub N N 204 
HIS C   OXT  sing N N 205 
HIS CB  CG   sing N N 206 
HIS CB  HB2  sing N N 207 
HIS CB  HB3  sing N N 208 
HIS CG  ND1  sing Y N 209 
HIS CG  CD2  doub Y N 210 
HIS ND1 CE1  doub Y N 211 
HIS ND1 HD1  sing N N 212 
HIS CD2 NE2  sing Y N 213 
HIS CD2 HD2  sing N N 214 
HIS CE1 NE2  sing Y N 215 
HIS CE1 HE1  sing N N 216 
HIS NE2 HE2  sing N N 217 
HIS OXT HXT  sing N N 218 
HOH O   H1   sing N N 219 
HOH O   H2   sing N N 220 
ILE N   CA   sing N N 221 
ILE N   H    sing N N 222 
ILE N   H2   sing N N 223 
ILE CA  C    sing N N 224 
ILE CA  CB   sing N N 225 
ILE CA  HA   sing N N 226 
ILE C   O    doub N N 227 
ILE C   OXT  sing N N 228 
ILE CB  CG1  sing N N 229 
ILE CB  CG2  sing N N 230 
ILE CB  HB   sing N N 231 
ILE CG1 CD1  sing N N 232 
ILE CG1 HG12 sing N N 233 
ILE CG1 HG13 sing N N 234 
ILE CG2 HG21 sing N N 235 
ILE CG2 HG22 sing N N 236 
ILE CG2 HG23 sing N N 237 
ILE CD1 HD11 sing N N 238 
ILE CD1 HD12 sing N N 239 
ILE CD1 HD13 sing N N 240 
ILE OXT HXT  sing N N 241 
LEU N   CA   sing N N 242 
LEU N   H    sing N N 243 
LEU N   H2   sing N N 244 
LEU CA  C    sing N N 245 
LEU CA  CB   sing N N 246 
LEU CA  HA   sing N N 247 
LEU C   O    doub N N 248 
LEU C   OXT  sing N N 249 
LEU CB  CG   sing N N 250 
LEU CB  HB2  sing N N 251 
LEU CB  HB3  sing N N 252 
LEU CG  CD1  sing N N 253 
LEU CG  CD2  sing N N 254 
LEU CG  HG   sing N N 255 
LEU CD1 HD11 sing N N 256 
LEU CD1 HD12 sing N N 257 
LEU CD1 HD13 sing N N 258 
LEU CD2 HD21 sing N N 259 
LEU CD2 HD22 sing N N 260 
LEU CD2 HD23 sing N N 261 
LEU OXT HXT  sing N N 262 
LYS N   CA   sing N N 263 
LYS N   H    sing N N 264 
LYS N   H2   sing N N 265 
LYS CA  C    sing N N 266 
LYS CA  CB   sing N N 267 
LYS CA  HA   sing N N 268 
LYS C   O    doub N N 269 
LYS C   OXT  sing N N 270 
LYS CB  CG   sing N N 271 
LYS CB  HB2  sing N N 272 
LYS CB  HB3  sing N N 273 
LYS CG  CD   sing N N 274 
LYS CG  HG2  sing N N 275 
LYS CG  HG3  sing N N 276 
LYS CD  CE   sing N N 277 
LYS CD  HD2  sing N N 278 
LYS CD  HD3  sing N N 279 
LYS CE  NZ   sing N N 280 
LYS CE  HE2  sing N N 281 
LYS CE  HE3  sing N N 282 
LYS NZ  HZ1  sing N N 283 
LYS NZ  HZ2  sing N N 284 
LYS NZ  HZ3  sing N N 285 
LYS OXT HXT  sing N N 286 
MET N   CA   sing N N 287 
MET N   H    sing N N 288 
MET N   H2   sing N N 289 
MET CA  C    sing N N 290 
MET CA  CB   sing N N 291 
MET CA  HA   sing N N 292 
MET C   O    doub N N 293 
MET C   OXT  sing N N 294 
MET CB  CG   sing N N 295 
MET CB  HB2  sing N N 296 
MET CB  HB3  sing N N 297 
MET CG  SD   sing N N 298 
MET CG  HG2  sing N N 299 
MET CG  HG3  sing N N 300 
MET SD  CE   sing N N 301 
MET CE  HE1  sing N N 302 
MET CE  HE2  sing N N 303 
MET CE  HE3  sing N N 304 
MET OXT HXT  sing N N 305 
PHE N   CA   sing N N 306 
PHE N   H    sing N N 307 
PHE N   H2   sing N N 308 
PHE CA  C    sing N N 309 
PHE CA  CB   sing N N 310 
PHE CA  HA   sing N N 311 
PHE C   O    doub N N 312 
PHE C   OXT  sing N N 313 
PHE CB  CG   sing N N 314 
PHE CB  HB2  sing N N 315 
PHE CB  HB3  sing N N 316 
PHE CG  CD1  doub Y N 317 
PHE CG  CD2  sing Y N 318 
PHE CD1 CE1  sing Y N 319 
PHE CD1 HD1  sing N N 320 
PHE CD2 CE2  doub Y N 321 
PHE CD2 HD2  sing N N 322 
PHE CE1 CZ   doub Y N 323 
PHE CE1 HE1  sing N N 324 
PHE CE2 CZ   sing Y N 325 
PHE CE2 HE2  sing N N 326 
PHE CZ  HZ   sing N N 327 
PHE OXT HXT  sing N N 328 
PRO N   CA   sing N N 329 
PRO N   CD   sing N N 330 
PRO N   H    sing N N 331 
PRO CA  C    sing N N 332 
PRO CA  CB   sing N N 333 
PRO CA  HA   sing N N 334 
PRO C   O    doub N N 335 
PRO C   OXT  sing N N 336 
PRO CB  CG   sing N N 337 
PRO CB  HB2  sing N N 338 
PRO CB  HB3  sing N N 339 
PRO CG  CD   sing N N 340 
PRO CG  HG2  sing N N 341 
PRO CG  HG3  sing N N 342 
PRO CD  HD2  sing N N 343 
PRO CD  HD3  sing N N 344 
PRO OXT HXT  sing N N 345 
SER N   CA   sing N N 346 
SER N   H    sing N N 347 
SER N   H2   sing N N 348 
SER CA  C    sing N N 349 
SER CA  CB   sing N N 350 
SER CA  HA   sing N N 351 
SER C   O    doub N N 352 
SER C   OXT  sing N N 353 
SER CB  OG   sing N N 354 
SER CB  HB2  sing N N 355 
SER CB  HB3  sing N N 356 
SER OG  HG   sing N N 357 
SER OXT HXT  sing N N 358 
SO4 S   O1   doub N N 359 
SO4 S   O2   doub N N 360 
SO4 S   O3   sing N N 361 
SO4 S   O4   sing N N 362 
THR N   CA   sing N N 363 
THR N   H    sing N N 364 
THR N   H2   sing N N 365 
THR CA  C    sing N N 366 
THR CA  CB   sing N N 367 
THR CA  HA   sing N N 368 
THR C   O    doub N N 369 
THR C   OXT  sing N N 370 
THR CB  OG1  sing N N 371 
THR CB  CG2  sing N N 372 
THR CB  HB   sing N N 373 
THR OG1 HG1  sing N N 374 
THR CG2 HG21 sing N N 375 
THR CG2 HG22 sing N N 376 
THR CG2 HG23 sing N N 377 
THR OXT HXT  sing N N 378 
TRP N   CA   sing N N 379 
TRP N   H    sing N N 380 
TRP N   H2   sing N N 381 
TRP CA  C    sing N N 382 
TRP CA  CB   sing N N 383 
TRP CA  HA   sing N N 384 
TRP C   O    doub N N 385 
TRP C   OXT  sing N N 386 
TRP CB  CG   sing N N 387 
TRP CB  HB2  sing N N 388 
TRP CB  HB3  sing N N 389 
TRP CG  CD1  doub Y N 390 
TRP CG  CD2  sing Y N 391 
TRP CD1 NE1  sing Y N 392 
TRP CD1 HD1  sing N N 393 
TRP CD2 CE2  doub Y N 394 
TRP CD2 CE3  sing Y N 395 
TRP NE1 CE2  sing Y N 396 
TRP NE1 HE1  sing N N 397 
TRP CE2 CZ2  sing Y N 398 
TRP CE3 CZ3  doub Y N 399 
TRP CE3 HE3  sing N N 400 
TRP CZ2 CH2  doub Y N 401 
TRP CZ2 HZ2  sing N N 402 
TRP CZ3 CH2  sing Y N 403 
TRP CZ3 HZ3  sing N N 404 
TRP CH2 HH2  sing N N 405 
TRP OXT HXT  sing N N 406 
TYR N   CA   sing N N 407 
TYR N   H    sing N N 408 
TYR N   H2   sing N N 409 
TYR CA  C    sing N N 410 
TYR CA  CB   sing N N 411 
TYR CA  HA   sing N N 412 
TYR C   O    doub N N 413 
TYR C   OXT  sing N N 414 
TYR CB  CG   sing N N 415 
TYR CB  HB2  sing N N 416 
TYR CB  HB3  sing N N 417 
TYR CG  CD1  doub Y N 418 
TYR CG  CD2  sing Y N 419 
TYR CD1 CE1  sing Y N 420 
TYR CD1 HD1  sing N N 421 
TYR CD2 CE2  doub Y N 422 
TYR CD2 HD2  sing N N 423 
TYR CE1 CZ   doub Y N 424 
TYR CE1 HE1  sing N N 425 
TYR CE2 CZ   sing Y N 426 
TYR CE2 HE2  sing N N 427 
TYR CZ  OH   sing N N 428 
TYR OH  HH   sing N N 429 
TYR OXT HXT  sing N N 430 
VAL N   CA   sing N N 431 
VAL N   H    sing N N 432 
VAL N   H2   sing N N 433 
VAL CA  C    sing N N 434 
VAL CA  CB   sing N N 435 
VAL CA  HA   sing N N 436 
VAL C   O    doub N N 437 
VAL C   OXT  sing N N 438 
VAL CB  CG1  sing N N 439 
VAL CB  CG2  sing N N 440 
VAL CB  HB   sing N N 441 
VAL CG1 HG11 sing N N 442 
VAL CG1 HG12 sing N N 443 
VAL CG1 HG13 sing N N 444 
VAL CG2 HG21 sing N N 445 
VAL CG2 HG22 sing N N 446 
VAL CG2 HG23 sing N N 447 
VAL OXT HXT  sing N N 448 
# 
_pdbx_initial_refinement_model.accession_code   ? 
_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      Other 
_pdbx_initial_refinement_model.details          'SPERM WHALE MYOGLOBIN 0M, D122N (DEOXY)' 
# 
_atom_sites.entry_id                    102M 
_atom_sites.fract_transf_matrix[1][1]   0.010937 
_atom_sites.fract_transf_matrix[1][2]   0.006314 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012629 
_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]   0.021763 
_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  
FE 
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   . MET A 1 1   ? 24.512 8.259   -9.688  1.00 33.83 ? 0   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? 24.523 9.740   -9.865  1.00 32.90 ? 0   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? 25.889 10.228  -10.330 1.00 31.90 ? 0   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? 26.886 9.516   -10.198 1.00 32.07 ? 0   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? 24.143 10.414  -8.560  1.00 34.34 ? 0   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? 24.891 9.880   -7.378  1.00 35.66 ? 0   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? 24.111 10.428  -5.871  1.00 38.66 ? 0   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? 24.454 12.221  -5.988  1.00 36.36 ? 0   MET A CE  1 
ATOM   9    N  N   . VAL A 1 2   ? 25.922 11.435  -10.891 1.00 30.10 ? 1   VAL A N   1 
ATOM   10   C  CA  . VAL A 1 2   ? 27.161 12.020  -11.393 1.00 27.92 ? 1   VAL A CA  1 
ATOM   11   C  C   . VAL A 1 2   ? 27.260 13.522  -11.114 1.00 26.21 ? 1   VAL A C   1 
ATOM   12   O  O   . VAL A 1 2   ? 26.304 14.278  -11.304 1.00 26.54 ? 1   VAL A O   1 
ATOM   13   C  CB  . VAL A 1 2   ? 27.312 11.769  -12.919 1.00 27.99 ? 1   VAL A CB  1 
ATOM   14   C  CG1 . VAL A 1 2   ? 28.557 12.455  -13.466 1.00 27.68 ? 1   VAL A CG1 1 
ATOM   15   C  CG2 . VAL A 1 2   ? 27.395 10.282  -13.189 1.00 28.05 ? 1   VAL A CG2 1 
ATOM   16   N  N   . LEU A 1 3   ? 28.407 13.938  -10.599 1.00 23.68 ? 2   LEU A N   1 
ATOM   17   C  CA  . LEU A 1 3   ? 28.641 15.349  -10.324 1.00 20.97 ? 2   LEU A CA  1 
ATOM   18   C  C   . LEU A 1 3   ? 29.285 15.976  -11.549 1.00 19.50 ? 2   LEU A C   1 
ATOM   19   O  O   . LEU A 1 3   ? 29.976 15.300  -12.306 1.00 18.60 ? 2   LEU A O   1 
ATOM   20   C  CB  . LEU A 1 3   ? 29.602 15.516  -9.142  1.00 20.07 ? 2   LEU A CB  1 
ATOM   21   C  CG  . LEU A 1 3   ? 29.003 15.462  -7.742  1.00 19.76 ? 2   LEU A CG  1 
ATOM   22   C  CD1 . LEU A 1 3   ? 28.734 14.017  -7.356  1.00 18.96 ? 2   LEU A CD1 1 
ATOM   23   C  CD2 . LEU A 1 3   ? 29.966 16.142  -6.762  1.00 18.40 ? 2   LEU A CD2 1 
ATOM   24   N  N   . SER A 1 4   ? 29.056 17.260  -11.759 1.00 18.20 ? 3   SER A N   1 
ATOM   25   C  CA  . SER A 1 4   ? 29.690 17.929  -12.882 1.00 17.70 ? 3   SER A CA  1 
ATOM   26   C  C   . SER A 1 4   ? 31.086 18.341  -12.420 1.00 17.23 ? 3   SER A C   1 
ATOM   27   O  O   . SER A 1 4   ? 31.404 18.261  -11.230 1.00 16.47 ? 3   SER A O   1 
ATOM   28   C  CB  . SER A 1 4   ? 28.882 19.155  -13.301 1.00 17.59 ? 3   SER A CB  1 
ATOM   29   O  OG  . SER A 1 4   ? 28.766 20.060  -12.225 1.00 17.97 ? 3   SER A OG  1 
ATOM   30   N  N   . GLU A 1 5   ? 31.935 18.742  -13.356 1.00 11.50 ? 4   GLU A N   1 
ATOM   31   C  CA  . GLU A 1 5   ? 33.283 19.175  -13.008 1.00 13.15 ? 4   GLU A CA  1 
ATOM   32   C  C   . GLU A 1 5   ? 33.188 20.387  -12.086 1.00 16.93 ? 4   GLU A C   1 
ATOM   33   O  O   . GLU A 1 5   ? 33.964 20.514  -11.147 1.00 15.15 ? 4   GLU A O   1 
ATOM   34   C  CB  . GLU A 1 5   ? 34.074 19.549  -14.275 1.00 17.13 ? 4   GLU A CB  1 
ATOM   35   C  CG  . GLU A 1 5   ? 35.473 20.111  -14.013 1.00 17.78 ? 4   GLU A CG  1 
ATOM   36   C  CD  . GLU A 1 5   ? 36.414 19.122  -13.332 1.00 19.05 ? 4   GLU A CD  1 
ATOM   37   O  OE1 . GLU A 1 5   ? 36.132 17.911  -13.343 1.00 29.34 ? 4   GLU A OE1 1 
ATOM   38   O  OE2 . GLU A 1 5   ? 37.452 19.559  -12.792 1.00 24.04 ? 4   GLU A OE2 1 
ATOM   39   N  N   . GLY A 1 6   ? 32.218 21.261  -12.358 1.00 13.76 ? 5   GLY A N   1 
ATOM   40   C  CA  . GLY A 1 6   ? 32.027 22.458  -11.553 1.00 13.72 ? 5   GLY A CA  1 
ATOM   41   C  C   . GLY A 1 6   ? 31.722 22.137  -10.101 1.00 13.60 ? 5   GLY A C   1 
ATOM   42   O  O   . GLY A 1 6   ? 32.186 22.833  -9.197  1.00 13.74 ? 5   GLY A O   1 
ATOM   43   N  N   . GLU A 1 7   ? 30.937 21.085  -9.881  1.00 12.33 ? 6   GLU A N   1 
ATOM   44   C  CA  . GLU A 1 7   ? 30.587 20.649  -8.531  1.00 9.54  ? 6   GLU A CA  1 
ATOM   45   C  C   . GLU A 1 7   ? 31.812 20.053  -7.832  1.00 12.64 ? 6   GLU A C   1 
ATOM   46   O  O   . GLU A 1 7   ? 32.042 20.319  -6.653  1.00 13.25 ? 6   GLU A O   1 
ATOM   47   C  CB  . GLU A 1 7   ? 29.423 19.652  -8.566  1.00 9.98  ? 6   GLU A CB  1 
ATOM   48   C  CG  . GLU A 1 7   ? 28.072 20.337  -8.823  1.00 14.10 ? 6   GLU A CG  1 
ATOM   49   C  CD  . GLU A 1 7   ? 26.947 19.382  -9.204  1.00 17.07 ? 6   GLU A CD  1 
ATOM   50   O  OE1 . GLU A 1 7   ? 27.217 18.304  -9.766  1.00 21.59 ? 6   GLU A OE1 1 
ATOM   51   O  OE2 . GLU A 1 7   ? 25.775 19.730  -8.972  1.00 22.03 ? 6   GLU A OE2 1 
ATOM   52   N  N   . TRP A 1 8   ? 32.609 19.264  -8.558  1.00 11.31 ? 7   TRP A N   1 
ATOM   53   C  CA  . TRP A 1 8   ? 33.822 18.684  -7.971  1.00 11.54 ? 7   TRP A CA  1 
ATOM   54   C  C   . TRP A 1 8   ? 34.783 19.785  -7.573  1.00 11.41 ? 7   TRP A C   1 
ATOM   55   O  O   . TRP A 1 8   ? 35.487 19.667  -6.578  1.00 11.70 ? 7   TRP A O   1 
ATOM   56   C  CB  . TRP A 1 8   ? 34.542 17.741  -8.947  1.00 10.91 ? 7   TRP A CB  1 
ATOM   57   C  CG  . TRP A 1 8   ? 33.913 16.393  -9.007  1.00 11.38 ? 7   TRP A CG  1 
ATOM   58   C  CD1 . TRP A 1 8   ? 33.327 15.798  -10.103 1.00 10.69 ? 7   TRP A CD1 1 
ATOM   59   C  CD2 . TRP A 1 8   ? 33.743 15.480  -7.917  1.00 10.51 ? 7   TRP A CD2 1 
ATOM   60   N  NE1 . TRP A 1 8   ? 32.801 14.590  -9.747  1.00 10.13 ? 7   TRP A NE1 1 
ATOM   61   C  CE2 . TRP A 1 8   ? 33.037 14.365  -8.414  1.00 11.11 ? 7   TRP A CE2 1 
ATOM   62   C  CE3 . TRP A 1 8   ? 34.108 15.499  -6.564  1.00 11.05 ? 7   TRP A CE3 1 
ATOM   63   C  CZ2 . TRP A 1 8   ? 32.683 13.276  -7.603  1.00 10.79 ? 7   TRP A CZ2 1 
ATOM   64   C  CZ3 . TRP A 1 8   ? 33.756 14.425  -5.760  1.00 11.18 ? 7   TRP A CZ3 1 
ATOM   65   C  CH2 . TRP A 1 8   ? 33.048 13.327  -6.283  1.00 11.36 ? 7   TRP A CH2 1 
ATOM   66   N  N   . GLN A 1 9   ? 34.826 20.852  -8.365  1.00 11.12 ? 8   GLN A N   1 
ATOM   67   C  CA  . GLN A 1 9   ? 35.725 21.953  -8.069  1.00 11.48 ? 8   GLN A CA  1 
ATOM   68   C  C   . GLN A 1 9   ? 35.347 22.656  -6.772  1.00 11.14 ? 8   GLN A C   1 
ATOM   69   O  O   . GLN A 1 9   ? 36.230 23.079  -6.013  1.00 11.32 ? 8   GLN A O   1 
ATOM   70   C  CB  . GLN A 1 9   ? 35.768 22.938  -9.236  1.00 13.11 ? 8   GLN A CB  1 
ATOM   71   C  CG  . GLN A 1 9   ? 36.551 22.409  -10.426 1.00 21.08 ? 8   GLN A CG  1 
ATOM   72   C  CD  . GLN A 1 9   ? 37.947 21.946  -10.034 1.00 36.83 ? 8   GLN A CD  1 
ATOM   73   O  OE1 . GLN A 1 9   ? 38.794 22.750  -9.637  1.00 52.61 ? 8   GLN A OE1 1 
ATOM   74   N  NE2 . GLN A 1 9   ? 38.186 20.640  -10.127 1.00 45.08 ? 8   GLN A NE2 1 
ATOM   75   N  N   . LEU A 1 10  ? 34.045 22.792  -6.528  1.00 10.99 ? 9   LEU A N   1 
ATOM   76   C  CA  . LEU A 1 10  ? 33.564 23.420  -5.293  1.00 10.79 ? 9   LEU A CA  1 
ATOM   77   C  C   . LEU A 1 10  ? 33.953 22.552  -4.096  1.00 10.77 ? 9   LEU A C   1 
ATOM   78   O  O   . LEU A 1 10  ? 34.396 23.067  -3.067  1.00 11.21 ? 9   LEU A O   1 
ATOM   79   C  CB  . LEU A 1 10  ? 32.047 23.616  -5.334  1.00 11.08 ? 9   LEU A CB  1 
ATOM   80   C  CG  . LEU A 1 10  ? 31.566 24.710  -6.296  1.00 11.61 ? 9   LEU A CG  1 
ATOM   81   C  CD1 . LEU A 1 10  ? 30.043 24.816  -6.291  1.00 12.25 ? 9   LEU A CD1 1 
ATOM   82   C  CD2 . LEU A 1 10  ? 32.194 26.036  -5.900  1.00 12.75 ? 9   LEU A CD2 1 
ATOM   83   N  N   . VAL A 1 11  ? 33.799 21.237  -4.253  1.00 10.04 ? 10  VAL A N   1 
ATOM   84   C  CA  . VAL A 1 11  ? 34.137 20.255  -3.225  1.00 9.24  ? 10  VAL A CA  1 
ATOM   85   C  C   . VAL A 1 11  ? 35.638 20.262  -2.923  1.00 10.26 ? 10  VAL A C   1 
ATOM   86   O  O   . VAL A 1 11  ? 36.050 20.371  -1.768  1.00 10.31 ? 10  VAL A O   1 
ATOM   87   C  CB  . VAL A 1 11  ? 33.713 18.822  -3.689  1.00 9.55  ? 10  VAL A CB  1 
ATOM   88   C  CG1 . VAL A 1 11  ? 34.293 17.739  -2.766  1.00 8.54  ? 10  VAL A CG1 1 
ATOM   89   C  CG2 . VAL A 1 11  ? 32.178 18.716  -3.742  1.00 8.68  ? 10  VAL A CG2 1 
ATOM   90   N  N   . LEU A 1 12  ? 36.460 20.196  -3.963  1.00 10.27 ? 11  LEU A N   1 
ATOM   91   C  CA  . LEU A 1 12  ? 37.908 20.168  -3.769  1.00 11.22 ? 11  LEU A CA  1 
ATOM   92   C  C   . LEU A 1 12  ? 38.481 21.497  -3.309  1.00 11.14 ? 11  LEU A C   1 
ATOM   93   O  O   . LEU A 1 12  ? 39.513 21.524  -2.642  1.00 11.99 ? 11  LEU A O   1 
ATOM   94   C  CB  . LEU A 1 12  ? 38.622 19.660  -5.027  1.00 11.89 ? 11  LEU A CB  1 
ATOM   95   C  CG  . LEU A 1 12  ? 38.154 18.258  -5.426  1.00 12.65 ? 11  LEU A CG  1 
ATOM   96   C  CD1 . LEU A 1 12  ? 38.812 17.824  -6.713  1.00 13.69 ? 11  LEU A CD1 1 
ATOM   97   C  CD2 . LEU A 1 12  ? 38.455 17.268  -4.296  1.00 13.06 ? 11  LEU A CD2 1 
ATOM   98   N  N   . HIS A 1 13  ? 37.776 22.587  -3.588  1.00 11.31 ? 12  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 13  ? 38.240 23.898  -3.158  1.00 12.09 ? 12  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 13  ? 38.153 24.025  -1.629  1.00 12.12 ? 12  HIS A C   1 
ATOM   101  O  O   . HIS A 1 13  ? 39.102 24.468  -0.981  1.00 12.27 ? 12  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 13  ? 37.427 25.009  -3.825  1.00 13.44 ? 12  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 13  ? 37.822 26.382  -3.383  1.00 22.67 ? 12  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 13  ? 39.007 26.998  -3.730  1.00 28.37 ? 12  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 13  ? 37.183 27.251  -2.559  1.00 25.14 ? 12  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 13  ? 39.050 28.190  -3.116  1.00 30.02 ? 12  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 13  ? 37.964 28.390  -2.392  1.00 28.60 ? 12  HIS A NE2 1 
ATOM   108  N  N   . VAL A 1 14  ? 37.019 23.632  -1.054  1.00 11.87 ? 13  VAL A N   1 
ATOM   109  C  CA  . VAL A 1 14  ? 36.863 23.712  0.394   1.00 11.74 ? 13  VAL A CA  1 
ATOM   110  C  C   . VAL A 1 14  ? 37.686 22.603  1.070   1.00 11.21 ? 13  VAL A C   1 
ATOM   111  O  O   . VAL A 1 14  ? 38.228 22.789  2.162   1.00 11.07 ? 13  VAL A O   1 
ATOM   112  C  CB  . VAL A 1 14  ? 35.358 23.686  0.830   1.00 12.76 ? 13  VAL A CB  1 
ATOM   113  C  CG1 . VAL A 1 14  ? 34.722 22.349  0.528   1.00 13.30 ? 13  VAL A CG1 1 
ATOM   114  C  CG2 . VAL A 1 14  ? 35.235 23.993  2.330   1.00 13.42 ? 13  VAL A CG2 1 
ATOM   115  N  N   . TRP A 1 15  ? 37.830 21.468  0.391   1.00 10.66 ? 14  TRP A N   1 
ATOM   116  C  CA  . TRP A 1 15  ? 38.624 20.383  0.957   1.00 10.48 ? 14  TRP A CA  1 
ATOM   117  C  C   . TRP A 1 15  ? 40.093 20.791  1.108   1.00 10.37 ? 14  TRP A C   1 
ATOM   118  O  O   . TRP A 1 15  ? 40.761 20.350  2.038   1.00 10.78 ? 14  TRP A O   1 
ATOM   119  C  CB  . TRP A 1 15  ? 38.526 19.112  0.116   1.00 10.76 ? 14  TRP A CB  1 
ATOM   120  C  CG  . TRP A 1 15  ? 38.936 17.916  0.907   1.00 11.28 ? 14  TRP A CG  1 
ATOM   121  C  CD1 . TRP A 1 15  ? 40.124 17.253  0.832   1.00 11.41 ? 14  TRP A CD1 1 
ATOM   122  C  CD2 . TRP A 1 15  ? 38.194 17.299  1.973   1.00 11.67 ? 14  TRP A CD2 1 
ATOM   123  N  NE1 . TRP A 1 15  ? 40.171 16.269  1.796   1.00 11.43 ? 14  TRP A NE1 1 
ATOM   124  C  CE2 . TRP A 1 15  ? 39.001 16.274  2.505   1.00 11.41 ? 14  TRP A CE2 1 
ATOM   125  C  CE3 . TRP A 1 15  ? 36.924 17.523  2.529   1.00 12.03 ? 14  TRP A CE3 1 
ATOM   126  C  CZ2 . TRP A 1 15  ? 38.587 15.466  3.570   1.00 12.35 ? 14  TRP A CZ2 1 
ATOM   127  C  CZ3 . TRP A 1 15  ? 36.506 16.726  3.588   1.00 12.90 ? 14  TRP A CZ3 1 
ATOM   128  C  CH2 . TRP A 1 15  ? 37.337 15.704  4.099   1.00 13.02 ? 14  TRP A CH2 1 
ATOM   129  N  N   . ALA A 1 16  ? 40.592 21.637  0.207   1.00 10.07 ? 15  ALA A N   1 
ATOM   130  C  CA  . ALA A 1 16  ? 41.973 22.103  0.279   1.00 9.96  ? 15  ALA A CA  1 
ATOM   131  C  C   . ALA A 1 16  ? 42.169 22.917  1.553   1.00 10.36 ? 15  ALA A C   1 
ATOM   132  O  O   . ALA A 1 16  ? 43.260 22.923  2.123   1.00 10.38 ? 15  ALA A O   1 
ATOM   133  C  CB  . ALA A 1 16  ? 42.315 22.935  -0.939  1.00 10.26 ? 15  ALA A CB  1 
ATOM   134  N  N   . LYS A 1 17  ? 41.096 23.569  2.015   1.00 13.39 ? 16  LYS A N   1 
ATOM   135  C  CA  . LYS A 1 17  ? 41.135 24.359  3.261   1.00 13.19 ? 16  LYS A CA  1 
ATOM   136  C  C   . LYS A 1 17  ? 41.171 23.406  4.455   1.00 13.61 ? 16  LYS A C   1 
ATOM   137  O  O   . LYS A 1 17  ? 41.890 23.637  5.425   1.00 12.40 ? 16  LYS A O   1 
ATOM   138  C  CB  . LYS A 1 17  ? 39.905 25.272  3.385   1.00 11.48 ? 16  LYS A CB  1 
ATOM   139  C  CG  . LYS A 1 17  ? 39.718 26.231  2.243   1.00 12.40 ? 16  LYS A CG  1 
ATOM   140  C  CD  . LYS A 1 17  ? 40.962 27.065  2.043   1.00 19.67 ? 16  LYS A CD  1 
ATOM   141  C  CE  . LYS A 1 17  ? 40.819 27.938  0.807   1.00 40.79 ? 16  LYS A CE  1 
ATOM   142  N  NZ  . LYS A 1 17  ? 42.134 28.445  0.346   1.00 42.91 ? 16  LYS A NZ  1 
ATOM   143  N  N   . VAL A 1 18  ? 40.352 22.358  4.392   1.00 8.93  ? 17  VAL A N   1 
ATOM   144  C  CA  . VAL A 1 18  ? 40.301 21.335  5.430   1.00 8.89  ? 17  VAL A CA  1 
ATOM   145  C  C   . VAL A 1 18  ? 41.690 20.708  5.613   1.00 8.91  ? 17  VAL A C   1 
ATOM   146  O  O   . VAL A 1 18  ? 42.153 20.485  6.738   1.00 9.48  ? 17  VAL A O   1 
ATOM   147  C  CB  . VAL A 1 18  ? 39.297 20.217  5.043   1.00 9.30  ? 17  VAL A CB  1 
ATOM   148  C  CG1 . VAL A 1 18  ? 39.394 19.032  5.998   1.00 8.84  ? 17  VAL A CG1 1 
ATOM   149  C  CG2 . VAL A 1 18  ? 37.887 20.779  5.041   1.00 9.56  ? 17  VAL A CG2 1 
ATOM   150  N  N   . GLU A 1 19  ? 42.372 20.447  4.505   1.00 6.61  ? 18  GLU A N   1 
ATOM   151  C  CA  . GLU A 1 19  ? 43.700 19.838  4.568   1.00 9.04  ? 18  GLU A CA  1 
ATOM   152  C  C   . GLU A 1 19  ? 44.805 20.674  5.212   1.00 12.62 ? 18  GLU A C   1 
ATOM   153  O  O   . GLU A 1 19  ? 45.866 20.153  5.526   1.00 12.36 ? 18  GLU A O   1 
ATOM   154  C  CB  . GLU A 1 19  ? 44.130 19.345  3.195   1.00 7.67  ? 18  GLU A CB  1 
ATOM   155  C  CG  . GLU A 1 19  ? 43.394 18.101  2.819   1.00 10.10 ? 18  GLU A CG  1 
ATOM   156  C  CD  . GLU A 1 19  ? 43.770 17.577  1.460   1.00 12.28 ? 18  GLU A CD  1 
ATOM   157  O  OE1 . GLU A 1 19  ? 44.253 18.345  0.613   1.00 21.78 ? 18  GLU A OE1 1 
ATOM   158  O  OE2 . GLU A 1 19  ? 43.534 16.388  1.239   1.00 18.35 ? 18  GLU A OE2 1 
ATOM   159  N  N   . ALA A 1 20  ? 44.546 21.954  5.434   1.00 10.19 ? 19  ALA A N   1 
ATOM   160  C  CA  . ALA A 1 20  ? 45.529 22.801  6.083   1.00 10.76 ? 19  ALA A CA  1 
ATOM   161  C  C   . ALA A 1 20  ? 45.596 22.426  7.567   1.00 10.82 ? 19  ALA A C   1 
ATOM   162  O  O   . ALA A 1 20  ? 46.573 22.741  8.244   1.00 11.41 ? 19  ALA A O   1 
ATOM   163  C  CB  . ALA A 1 20  ? 45.158 24.277  5.918   1.00 10.40 ? 19  ALA A CB  1 
ATOM   164  N  N   . ASP A 1 21  ? 44.554 21.753  8.072   1.00 7.53  ? 20  ASP A N   1 
ATOM   165  C  CA  . ASP A 1 21  ? 44.520 21.330  9.477   1.00 6.29  ? 20  ASP A CA  1 
ATOM   166  C  C   . ASP A 1 21  ? 43.688 20.058  9.604   1.00 8.43  ? 20  ASP A C   1 
ATOM   167  O  O   . ASP A 1 21  ? 42.597 20.076  10.167  1.00 9.13  ? 20  ASP A O   1 
ATOM   168  C  CB  . ASP A 1 21  ? 43.926 22.443  10.351  1.00 8.02  ? 20  ASP A CB  1 
ATOM   169  C  CG  . ASP A 1 21  ? 43.806 22.045  11.815  1.00 16.51 ? 20  ASP A CG  1 
ATOM   170  O  OD1 . ASP A 1 21  ? 44.596 21.205  12.290  1.00 11.97 ? 20  ASP A OD1 1 
ATOM   171  O  OD2 . ASP A 1 21  ? 42.888 22.560  12.485  1.00 20.93 ? 20  ASP A OD2 1 
ATOM   172  N  N   . VAL A 1 22  ? 44.244 18.940  9.151   1.00 8.87  ? 21  VAL A N   1 
ATOM   173  C  CA  . VAL A 1 22  ? 43.526 17.675  9.178   1.00 9.76  ? 21  VAL A CA  1 
ATOM   174  C  C   . VAL A 1 22  ? 43.119 17.225  10.571  1.00 9.90  ? 21  VAL A C   1 
ATOM   175  O  O   . VAL A 1 22  ? 41.960 16.881  10.803  1.00 10.50 ? 21  VAL A O   1 
ATOM   176  C  CB  . VAL A 1 22  ? 44.323 16.549  8.427   1.00 10.41 ? 21  VAL A CB  1 
ATOM   177  C  CG1 . VAL A 1 22  ? 43.576 15.215  8.483   1.00 11.55 ? 21  VAL A CG1 1 
ATOM   178  C  CG2 . VAL A 1 22  ? 44.488 16.939  6.978   1.00 11.00 ? 21  VAL A CG2 1 
ATOM   179  N  N   . ALA A 1 23  ? 44.055 17.261  11.508  1.00 10.03 ? 22  ALA A N   1 
ATOM   180  C  CA  . ALA A 1 23  ? 43.773 16.826  12.872  1.00 10.36 ? 22  ALA A CA  1 
ATOM   181  C  C   . ALA A 1 23  ? 42.692 17.659  13.566  1.00 10.25 ? 22  ALA A C   1 
ATOM   182  O  O   . ALA A 1 23  ? 41.819 17.110  14.235  1.00 10.43 ? 22  ALA A O   1 
ATOM   183  C  CB  . ALA A 1 23  ? 45.061 16.813  13.681  1.00 10.62 ? 22  ALA A CB  1 
ATOM   184  N  N   . GLY A 1 24  ? 42.726 18.974  13.375  1.00 10.00 ? 23  GLY A N   1 
ATOM   185  C  CA  . GLY A 1 24  ? 41.732 19.837  13.995  1.00 9.51  ? 23  GLY A CA  1 
ATOM   186  C  C   . GLY A 1 24  ? 40.331 19.608  13.452  1.00 9.38  ? 23  GLY A C   1 
ATOM   187  O  O   . GLY A 1 24  ? 39.361 19.611  14.213  1.00 9.22  ? 23  GLY A O   1 
ATOM   188  N  N   . HIS A 1 25  ? 40.214 19.429  12.135  1.00 9.06  ? 24  HIS A N   1 
ATOM   189  C  CA  . HIS A 1 25  ? 38.914 19.171  11.524  1.00 8.95  ? 24  HIS A CA  1 
ATOM   190  C  C   . HIS A 1 25  ? 38.451 17.782  11.932  1.00 9.25  ? 24  HIS A C   1 
ATOM   191  O  O   . HIS A 1 25  ? 37.269 17.580  12.166  1.00 9.76  ? 24  HIS A O   1 
ATOM   192  C  CB  . HIS A 1 25  ? 38.985 19.258  10.001  1.00 7.95  ? 24  HIS A CB  1 
ATOM   193  C  CG  . HIS A 1 25  ? 39.063 20.658  9.479   1.00 7.25  ? 24  HIS A CG  1 
ATOM   194  N  ND1 . HIS A 1 25  ? 40.216 21.408  9.444   1.00 7.49  ? 24  HIS A ND1 1 
ATOM   195  C  CD2 . HIS A 1 25  ? 38.101 21.437  8.919   1.00 8.45  ? 24  HIS A CD2 1 
ATOM   196  C  CE1 . HIS A 1 25  ? 39.929 22.587  8.876   1.00 6.61  ? 24  HIS A CE1 1 
ATOM   197  N  NE2 . HIS A 1 25  ? 38.656 22.652  8.540   1.00 8.20  ? 24  HIS A NE2 1 
ATOM   198  N  N   . GLY A 1 26  ? 39.382 16.830  12.004  1.00 9.59  ? 25  GLY A N   1 
ATOM   199  C  CA  . GLY A 1 26  ? 39.040 15.466  12.411  1.00 9.87  ? 25  GLY A CA  1 
ATOM   200  C  C   . GLY A 1 26  ? 38.425 15.435  13.811  1.00 10.45 ? 25  GLY A C   1 
ATOM   201  O  O   . GLY A 1 26  ? 37.429 14.745  14.041  1.00 10.53 ? 25  GLY A O   1 
ATOM   202  N  N   . GLN A 1 27  ? 39.016 16.175  14.750  1.00 10.50 ? 26  GLN A N   1 
ATOM   203  C  CA  . GLN A 1 27  ? 38.485 16.243  16.111  1.00 10.95 ? 26  GLN A CA  1 
ATOM   204  C  C   . GLN A 1 27  ? 37.101 16.867  16.119  1.00 11.30 ? 26  GLN A C   1 
ATOM   205  O  O   . GLN A 1 27  ? 36.179 16.308  16.705  1.00 11.60 ? 26  GLN A O   1 
ATOM   206  C  CB  . GLN A 1 27  ? 39.377 17.086  17.033  1.00 12.96 ? 26  GLN A CB  1 
ATOM   207  C  CG  . GLN A 1 27  ? 40.637 16.404  17.504  1.00 20.05 ? 26  GLN A CG  1 
ATOM   208  C  CD  . GLN A 1 27  ? 41.507 17.328  18.329  1.00 30.35 ? 26  GLN A CD  1 
ATOM   209  O  OE1 . GLN A 1 27  ? 42.178 18.210  17.792  1.00 38.63 ? 26  GLN A OE1 1 
ATOM   210  N  NE2 . GLN A 1 27  ? 41.481 17.146  19.640  1.00 23.38 ? 26  GLN A NE2 1 
ATOM   211  N  N   . ASP A 1 28  ? 36.973 18.046  15.508  1.00 7.68  ? 27  ASP A N   1 
ATOM   212  C  CA  . ASP A 1 28  ? 35.695 18.760  15.452  1.00 7.93  ? 27  ASP A CA  1 
ATOM   213  C  C   . ASP A 1 28  ? 34.561 17.910  14.902  1.00 12.23 ? 27  ASP A C   1 
ATOM   214  O  O   . ASP A 1 28  ? 33.446 17.937  15.419  1.00 8.19  ? 27  ASP A O   1 
ATOM   215  C  CB  . ASP A 1 28  ? 35.815 20.013  14.569  1.00 7.30  ? 27  ASP A CB  1 
ATOM   216  C  CG  . ASP A 1 28  ? 36.572 21.145  15.237  1.00 19.67 ? 27  ASP A CG  1 
ATOM   217  O  OD1 . ASP A 1 28  ? 36.929 21.034  16.429  1.00 19.56 ? 27  ASP A OD1 1 
ATOM   218  O  OD2 . ASP A 1 28  ? 36.816 22.160  14.559  1.00 17.34 ? 27  ASP A OD2 1 
ATOM   219  N  N   . ILE A 1 29  ? 34.843 17.189  13.822  1.00 9.35  ? 28  ILE A N   1 
ATOM   220  C  CA  . ILE A 1 29  ? 33.845 16.342  13.178  1.00 9.60  ? 28  ILE A CA  1 
ATOM   221  C  C   . ILE A 1 29  ? 33.388 15.170  14.060  1.00 9.84  ? 28  ILE A C   1 
ATOM   222  O  O   . ILE A 1 29  ? 32.177 14.944  14.233  1.00 9.58  ? 28  ILE A O   1 
ATOM   223  C  CB  . ILE A 1 29  ? 34.372 15.855  11.789  1.00 9.45  ? 28  ILE A CB  1 
ATOM   224  C  CG1 . ILE A 1 29  ? 34.350 17.040  10.808  1.00 9.63  ? 28  ILE A CG1 1 
ATOM   225  C  CG2 . ILE A 1 29  ? 33.523 14.694  11.258  1.00 9.65  ? 28  ILE A CG2 1 
ATOM   226  C  CD1 . ILE A 1 29  ? 35.151 16.829  9.528   1.00 9.98  ? 28  ILE A CD1 1 
ATOM   227  N  N   . LEU A 1 30  ? 34.343 14.443  14.637  1.00 9.88  ? 29  LEU A N   1 
ATOM   228  C  CA  . LEU A 1 30  ? 33.990 13.316  15.493  1.00 10.76 ? 29  LEU A CA  1 
ATOM   229  C  C   . LEU A 1 30  ? 33.271 13.761  16.762  1.00 11.22 ? 29  LEU A C   1 
ATOM   230  O  O   . LEU A 1 30  ? 32.309 13.128  17.186  1.00 11.71 ? 29  LEU A O   1 
ATOM   231  C  CB  . LEU A 1 30  ? 35.211 12.449  15.819  1.00 10.95 ? 29  LEU A CB  1 
ATOM   232  C  CG  . LEU A 1 30  ? 35.723 11.506  14.714  1.00 11.87 ? 29  LEU A CG  1 
ATOM   233  C  CD1 . LEU A 1 30  ? 36.798 10.593  15.279  1.00 11.72 ? 29  LEU A CD1 1 
ATOM   234  C  CD2 . LEU A 1 30  ? 34.601 10.652  14.155  1.00 12.25 ? 29  LEU A CD2 1 
ATOM   235  N  N   . ILE A 1 31  ? 33.709 14.864  17.354  1.00 11.43 ? 30  ILE A N   1 
ATOM   236  C  CA  . ILE A 1 31  ? 33.065 15.374  18.560  1.00 11.91 ? 30  ILE A CA  1 
ATOM   237  C  C   . ILE A 1 31  ? 31.627 15.805  18.240  1.00 12.34 ? 30  ILE A C   1 
ATOM   238  O  O   . ILE A 1 31  ? 30.701 15.533  19.010  1.00 12.67 ? 30  ILE A O   1 
ATOM   239  C  CB  . ILE A 1 31  ? 33.870 16.547  19.174  1.00 12.35 ? 30  ILE A CB  1 
ATOM   240  C  CG1 . ILE A 1 31  ? 35.177 16.004  19.778  1.00 12.43 ? 30  ILE A CG1 1 
ATOM   241  C  CG2 . ILE A 1 31  ? 33.016 17.295  20.204  1.00 12.10 ? 30  ILE A CG2 1 
ATOM   242  C  CD1 . ILE A 1 31  ? 36.090 17.047  20.388  1.00 13.25 ? 30  ILE A CD1 1 
ATOM   243  N  N   . ARG A 1 32  ? 31.441 16.457  17.097  1.00 12.52 ? 31  ARG A N   1 
ATOM   244  C  CA  . ARG A 1 32  ? 30.108 16.890  16.660  1.00 13.02 ? 31  ARG A CA  1 
ATOM   245  C  C   . ARG A 1 32  ? 29.220 15.641  16.504  1.00 13.90 ? 31  ARG A C   1 
ATOM   246  O  O   . ARG A 1 32  ? 28.097 15.590  17.031  1.00 13.58 ? 31  ARG A O   1 
ATOM   247  C  CB  . ARG A 1 32  ? 30.250 17.670  15.344  1.00 13.28 ? 31  ARG A CB  1 
ATOM   248  C  CG  . ARG A 1 32  ? 29.002 17.878  14.488  1.00 19.41 ? 31  ARG A CG  1 
ATOM   249  C  CD  . ARG A 1 32  ? 27.742 18.169  15.250  1.00 27.43 ? 31  ARG A CD  1 
ATOM   250  N  NE  . ARG A 1 32  ? 27.775 19.409  15.999  1.00 35.28 ? 31  ARG A NE  1 
ATOM   251  C  CZ  . ARG A 1 32  ? 26.719 20.200  16.157  1.00 57.29 ? 31  ARG A CZ  1 
ATOM   252  N  NH1 . ARG A 1 32  ? 25.564 19.911  15.563  1.00 45.11 ? 31  ARG A NH1 1 
ATOM   253  N  NH2 . ARG A 1 32  ? 26.830 21.309  16.873  1.00 59.96 ? 31  ARG A NH2 1 
ATOM   254  N  N   . LEU A 1 33  ? 29.764 14.607  15.855  1.00 13.94 ? 32  LEU A N   1 
ATOM   255  C  CA  . LEU A 1 33  ? 29.038 13.352  15.651  1.00 14.16 ? 32  LEU A CA  1 
ATOM   256  C  C   . LEU A 1 33  ? 28.613 12.719  16.984  1.00 14.58 ? 32  LEU A C   1 
ATOM   257  O  O   . LEU A 1 33  ? 27.457 12.363  17.156  1.00 14.89 ? 32  LEU A O   1 
ATOM   258  C  CB  . LEU A 1 33  ? 29.909 12.355  14.871  1.00 13.94 ? 32  LEU A CB  1 
ATOM   259  C  CG  . LEU A 1 33  ? 29.369 10.926  14.735  1.00 14.29 ? 32  LEU A CG  1 
ATOM   260  C  CD1 . LEU A 1 33  ? 28.142 10.932  13.858  1.00 14.01 ? 32  LEU A CD1 1 
ATOM   261  C  CD2 . LEU A 1 33  ? 30.418 10.000  14.141  1.00 14.52 ? 32  LEU A CD2 1 
ATOM   262  N  N   . PHE A 1 34  ? 29.552 12.604  17.925  1.00 14.72 ? 33  PHE A N   1 
ATOM   263  C  CA  . PHE A 1 34  ? 29.281 11.985  19.227  1.00 14.83 ? 33  PHE A CA  1 
ATOM   264  C  C   . PHE A 1 34  ? 28.328 12.779  20.104  1.00 15.92 ? 33  PHE A C   1 
ATOM   265  O  O   . PHE A 1 34  ? 27.591 12.196  20.902  1.00 17.20 ? 33  PHE A O   1 
ATOM   266  C  CB  . PHE A 1 34  ? 30.582 11.728  19.983  1.00 13.93 ? 33  PHE A CB  1 
ATOM   267  C  CG  . PHE A 1 34  ? 31.542 10.831  19.257  1.00 13.76 ? 33  PHE A CG  1 
ATOM   268  C  CD1 . PHE A 1 34  ? 31.079 9.781   18.465  1.00 13.40 ? 33  PHE A CD1 1 
ATOM   269  C  CD2 . PHE A 1 34  ? 32.919 11.024  19.379  1.00 13.45 ? 33  PHE A CD2 1 
ATOM   270  C  CE1 . PHE A 1 34  ? 31.976 8.934   17.802  1.00 13.10 ? 33  PHE A CE1 1 
ATOM   271  C  CE2 . PHE A 1 34  ? 33.820 10.186  18.722  1.00 13.51 ? 33  PHE A CE2 1 
ATOM   272  C  CZ  . PHE A 1 34  ? 33.346 9.137   17.930  1.00 13.06 ? 33  PHE A CZ  1 
ATOM   273  N  N   . LYS A 1 35  ? 28.340 14.102  19.976  1.00 18.34 ? 34  LYS A N   1 
ATOM   274  C  CA  . LYS A 1 35  ? 27.444 14.928  20.777  1.00 19.64 ? 34  LYS A CA  1 
ATOM   275  C  C   . LYS A 1 35  ? 26.039 14.876  20.217  1.00 21.06 ? 34  LYS A C   1 
ATOM   276  O  O   . LYS A 1 35  ? 25.067 14.866  20.969  1.00 29.46 ? 34  LYS A O   1 
ATOM   277  C  CB  . LYS A 1 35  ? 27.928 16.379  20.847  1.00 16.26 ? 34  LYS A CB  1 
ATOM   278  C  CG  . LYS A 1 35  ? 29.202 16.549  21.658  1.00 34.93 ? 34  LYS A CG  1 
ATOM   279  C  CD  . LYS A 1 35  ? 29.371 17.972  22.177  1.00 53.53 ? 34  LYS A CD  1 
ATOM   280  C  CE  . LYS A 1 35  ? 29.393 18.972  21.046  1.00 56.86 ? 34  LYS A CE  1 
ATOM   281  N  NZ  . LYS A 1 35  ? 29.855 20.321  21.475  1.00 65.56 ? 34  LYS A NZ  1 
ATOM   282  N  N   . SER A 1 36  ? 25.937 14.833  18.892  1.00 20.96 ? 35  SER A N   1 
ATOM   283  C  CA  . SER A 1 36  ? 24.648 14.788  18.218  1.00 20.74 ? 35  SER A CA  1 
ATOM   284  C  C   . SER A 1 36  ? 24.014 13.398  18.263  1.00 20.45 ? 35  SER A C   1 
ATOM   285  O  O   . SER A 1 36  ? 22.804 13.267  18.404  1.00 20.62 ? 35  SER A O   1 
ATOM   286  C  CB  . SER A 1 36  ? 24.810 15.229  16.765  1.00 21.30 ? 35  SER A CB  1 
ATOM   287  O  OG  . SER A 1 36  ? 25.385 16.521  16.692  1.00 22.82 ? 35  SER A OG  1 
ATOM   288  N  N   . HIS A 1 37  ? 24.842 12.366  18.133  1.00 20.00 ? 36  HIS A N   1 
ATOM   289  C  CA  . HIS A 1 37  ? 24.378 10.977  18.138  1.00 19.63 ? 36  HIS A CA  1 
ATOM   290  C  C   . HIS A 1 37  ? 25.296 10.109  18.982  1.00 19.65 ? 36  HIS A C   1 
ATOM   291  O  O   . HIS A 1 37  ? 26.090 9.334   18.452  1.00 19.33 ? 36  HIS A O   1 
ATOM   292  C  CB  . HIS A 1 37  ? 24.312 10.435  16.708  1.00 18.90 ? 36  HIS A CB  1 
ATOM   293  C  CG  . HIS A 1 37  ? 23.572 11.329  15.762  1.00 18.39 ? 36  HIS A CG  1 
ATOM   294  N  ND1 . HIS A 1 37  ? 22.206 11.339  15.614  1.00 16.51 ? 36  HIS A ND1 1 
ATOM   295  C  CD2 . HIS A 1 37  ? 24.038 12.258  14.891  1.00 18.40 ? 36  HIS A CD2 1 
ATOM   296  C  CE1 . HIS A 1 37  ? 21.896 12.244  14.681  1.00 16.71 ? 36  HIS A CE1 1 
ATOM   297  N  NE2 . HIS A 1 37  ? 22.976 12.830  14.209  1.00 19.04 ? 36  HIS A NE2 1 
ATOM   298  N  N   . PRO A 1 38  ? 25.154 10.193  20.319  1.00 19.63 ? 37  PRO A N   1 
ATOM   299  C  CA  . PRO A 1 38  ? 25.939 9.451   21.311  1.00 19.68 ? 37  PRO A CA  1 
ATOM   300  C  C   . PRO A 1 38  ? 26.026 7.946   21.071  1.00 19.56 ? 37  PRO A C   1 
ATOM   301  O  O   . PRO A 1 38  ? 26.986 7.305   21.482  1.00 20.20 ? 37  PRO A O   1 
ATOM   302  C  CB  . PRO A 1 38  ? 25.207 9.760   22.615  1.00 19.69 ? 37  PRO A CB  1 
ATOM   303  C  CG  . PRO A 1 38  ? 24.661 11.130  22.382  1.00 19.80 ? 37  PRO A CG  1 
ATOM   304  C  CD  . PRO A 1 38  ? 24.124 11.017  20.985  1.00 19.86 ? 37  PRO A CD  1 
ATOM   305  N  N   . GLU A 1 39  ? 25.022 7.378   20.418  1.00 20.16 ? 38  GLU A N   1 
ATOM   306  C  CA  . GLU A 1 39  ? 25.023 5.942   20.150  1.00 21.01 ? 38  GLU A CA  1 
ATOM   307  C  C   . GLU A 1 39  ? 26.216 5.553   19.284  1.00 18.90 ? 38  GLU A C   1 
ATOM   308  O  O   . GLU A 1 39  ? 26.776 4.471   19.436  1.00 25.42 ? 38  GLU A O   1 
ATOM   309  C  CB  . GLU A 1 39  ? 23.703 5.504   19.492  1.00 21.02 ? 38  GLU A CB  1 
ATOM   310  C  CG  . GLU A 1 39  ? 23.432 6.096   18.118  1.00 23.43 ? 38  GLU A CG  1 
ATOM   311  C  CD  . GLU A 1 39  ? 22.488 7.291   18.141  1.00 39.47 ? 38  GLU A CD  1 
ATOM   312  O  OE1 . GLU A 1 39  ? 22.567 8.140   19.059  1.00 28.80 ? 38  GLU A OE1 1 
ATOM   313  O  OE2 . GLU A 1 39  ? 21.657 7.382   17.215  1.00 48.16 ? 38  GLU A OE2 1 
ATOM   314  N  N   . THR A 1 40  ? 26.641 6.466   18.416  1.00 16.62 ? 39  THR A N   1 
ATOM   315  C  CA  . THR A 1 40  ? 27.777 6.204   17.532  1.00 16.61 ? 39  THR A CA  1 
ATOM   316  C  C   . THR A 1 40  ? 29.101 6.024   18.279  1.00 16.75 ? 39  THR A C   1 
ATOM   317  O  O   . THR A 1 40  ? 29.984 5.322   17.788  1.00 17.23 ? 39  THR A O   1 
ATOM   318  C  CB  . THR A 1 40  ? 27.955 7.311   16.458  1.00 16.17 ? 39  THR A CB  1 
ATOM   319  O  OG1 . THR A 1 40  ? 28.228 8.565   17.100  1.00 15.49 ? 39  THR A OG1 1 
ATOM   320  C  CG2 . THR A 1 40  ? 26.703 7.434   15.608  1.00 15.50 ? 39  THR A CG2 1 
ATOM   321  N  N   . LEU A 1 41  ? 29.239 6.635   19.458  1.00 16.76 ? 40  LEU A N   1 
ATOM   322  C  CA  . LEU A 1 41  ? 30.477 6.512   20.235  1.00 17.15 ? 40  LEU A CA  1 
ATOM   323  C  C   . LEU A 1 41  ? 30.736 5.069   20.675  1.00 17.08 ? 40  LEU A C   1 
ATOM   324  O  O   . LEU A 1 41  ? 31.880 4.651   20.800  1.00 17.31 ? 40  LEU A O   1 
ATOM   325  C  CB  . LEU A 1 41  ? 30.434 7.422   21.471  1.00 17.88 ? 40  LEU A CB  1 
ATOM   326  C  CG  . LEU A 1 41  ? 31.620 7.370   22.448  1.00 17.91 ? 40  LEU A CG  1 
ATOM   327  C  CD1 . LEU A 1 41  ? 32.919 7.686   21.725  1.00 18.31 ? 40  LEU A CD1 1 
ATOM   328  C  CD2 . LEU A 1 41  ? 31.397 8.349   23.585  1.00 18.47 ? 40  LEU A CD2 1 
ATOM   329  N  N   . GLU A 1 42  ? 29.663 4.307   20.867  1.00 19.30 ? 41  GLU A N   1 
ATOM   330  C  CA  . GLU A 1 42  ? 29.757 2.916   21.294  1.00 19.98 ? 41  GLU A CA  1 
ATOM   331  C  C   . GLU A 1 42  ? 30.523 2.004   20.340  1.00 29.73 ? 41  GLU A C   1 
ATOM   332  O  O   . GLU A 1 42  ? 31.046 0.967   20.752  1.00 28.01 ? 41  GLU A O   1 
ATOM   333  C  CB  . GLU A 1 42  ? 28.358 2.356   21.533  1.00 24.27 ? 41  GLU A CB  1 
ATOM   334  C  CG  . GLU A 1 42  ? 27.630 3.040   22.678  1.00 47.51 ? 41  GLU A CG  1 
ATOM   335  C  CD  . GLU A 1 42  ? 26.249 2.473   22.930  1.00 53.88 ? 41  GLU A CD  1 
ATOM   336  O  OE1 . GLU A 1 42  ? 25.421 2.463   21.992  1.00 62.95 ? 41  GLU A OE1 1 
ATOM   337  O  OE2 . GLU A 1 42  ? 25.986 2.052   24.076  1.00 71.39 ? 41  GLU A OE2 1 
ATOM   338  N  N   . LYS A 1 43  ? 30.608 2.392   19.072  1.00 22.48 ? 42  LYS A N   1 
ATOM   339  C  CA  . LYS A 1 43  ? 31.309 1.567   18.097  1.00 18.14 ? 42  LYS A CA  1 
ATOM   340  C  C   . LYS A 1 43  ? 32.816 1.608   18.262  1.00 18.29 ? 42  LYS A C   1 
ATOM   341  O  O   . LYS A 1 43  ? 33.516 0.698   17.820  1.00 25.30 ? 42  LYS A O   1 
ATOM   342  C  CB  . LYS A 1 43  ? 30.914 1.974   16.674  1.00 17.13 ? 42  LYS A CB  1 
ATOM   343  C  CG  . LYS A 1 43  ? 29.463 1.728   16.363  1.00 15.46 ? 42  LYS A CG  1 
ATOM   344  C  CD  . LYS A 1 43  ? 29.202 0.241   16.224  1.00 23.35 ? 42  LYS A CD  1 
ATOM   345  C  CE  . LYS A 1 43  ? 27.737 -0.048  15.968  1.00 30.11 ? 42  LYS A CE  1 
ATOM   346  N  NZ  . LYS A 1 43  ? 27.525 -1.503  15.709  1.00 34.01 ? 42  LYS A NZ  1 
ATOM   347  N  N   . PHE A 1 44  ? 33.315 2.665   18.896  1.00 21.08 ? 43  PHE A N   1 
ATOM   348  C  CA  . PHE A 1 44  ? 34.747 2.827   19.101  1.00 21.46 ? 43  PHE A CA  1 
ATOM   349  C  C   . PHE A 1 44  ? 35.178 2.328   20.476  1.00 22.05 ? 43  PHE A C   1 
ATOM   350  O  O   . PHE A 1 44  ? 35.291 3.108   21.425  1.00 22.45 ? 43  PHE A O   1 
ATOM   351  C  CB  . PHE A 1 44  ? 35.151 4.291   18.924  1.00 20.42 ? 43  PHE A CB  1 
ATOM   352  C  CG  . PHE A 1 44  ? 34.890 4.835   17.545  1.00 20.19 ? 43  PHE A CG  1 
ATOM   353  C  CD1 . PHE A 1 44  ? 33.641 5.333   17.205  1.00 20.09 ? 43  PHE A CD1 1 
ATOM   354  C  CD2 . PHE A 1 44  ? 35.914 4.904   16.606  1.00 20.17 ? 43  PHE A CD2 1 
ATOM   355  C  CE1 . PHE A 1 44  ? 33.412 5.898   15.959  1.00 19.97 ? 43  PHE A CE1 1 
ATOM   356  C  CE2 . PHE A 1 44  ? 35.695 5.469   15.354  1.00 20.09 ? 43  PHE A CE2 1 
ATOM   357  C  CZ  . PHE A 1 44  ? 34.446 5.969   15.030  1.00 20.05 ? 43  PHE A CZ  1 
ATOM   358  N  N   . ASP A 1 45  ? 35.471 1.032   20.558  1.00 27.52 ? 44  ASP A N   1 
ATOM   359  C  CA  . ASP A 1 45  ? 35.885 0.393   21.804  1.00 31.74 ? 44  ASP A CA  1 
ATOM   360  C  C   . ASP A 1 45  ? 37.062 1.075   22.475  1.00 31.70 ? 44  ASP A C   1 
ATOM   361  O  O   . ASP A 1 45  ? 37.148 1.115   23.700  1.00 34.32 ? 44  ASP A O   1 
ATOM   362  C  CB  . ASP A 1 45  ? 36.226 -1.078  21.556  1.00 38.96 ? 44  ASP A CB  1 
ATOM   363  C  CG  . ASP A 1 45  ? 35.065 -1.850  20.977  1.00 53.66 ? 44  ASP A CG  1 
ATOM   364  O  OD1 . ASP A 1 45  ? 33.965 -1.801  21.567  1.00 59.37 ? 44  ASP A OD1 1 
ATOM   365  O  OD2 . ASP A 1 45  ? 35.246 -2.497  19.924  1.00 66.33 ? 44  ASP A OD2 1 
ATOM   366  N  N   . ARG A 1 46  ? 37.949 1.639   21.666  1.00 28.24 ? 45  ARG A N   1 
ATOM   367  C  CA  . ARG A 1 46  ? 39.128 2.303   22.179  1.00 28.34 ? 45  ARG A CA  1 
ATOM   368  C  C   . ARG A 1 46  ? 38.821 3.495   23.081  1.00 28.19 ? 45  ARG A C   1 
ATOM   369  O  O   . ARG A 1 46  ? 39.501 3.698   24.081  1.00 28.78 ? 45  ARG A O   1 
ATOM   370  C  CB  . ARG A 1 46  ? 40.037 2.737   21.029  1.00 29.69 ? 45  ARG A CB  1 
ATOM   371  C  CG  . ARG A 1 46  ? 41.460 2.234   21.171  1.00 37.74 ? 45  ARG A CG  1 
ATOM   372  C  CD  . ARG A 1 46  ? 42.428 2.973   20.256  1.00 47.49 ? 45  ARG A CD  1 
ATOM   373  N  NE  . ARG A 1 46  ? 42.306 2.586   18.854  1.00 52.74 ? 45  ARG A NE  1 
ATOM   374  C  CZ  . ARG A 1 46  ? 42.350 3.441   17.833  1.00 82.62 ? 45  ARG A CZ  1 
ATOM   375  N  NH1 . ARG A 1 46  ? 42.474 4.749   18.043  1.00 70.09 ? 45  ARG A NH1 1 
ATOM   376  N  NH2 . ARG A 1 46  ? 42.245 2.988   16.591  1.00 86.55 ? 45  ARG A NH2 1 
ATOM   377  N  N   . PHE A 1 47  ? 37.788 4.265   22.762  1.00 27.54 ? 46  PHE A N   1 
ATOM   378  C  CA  . PHE A 1 47  ? 37.467 5.434   23.576  1.00 27.01 ? 46  PHE A CA  1 
ATOM   379  C  C   . PHE A 1 47  ? 35.976 5.616   23.858  1.00 26.87 ? 46  PHE A C   1 
ATOM   380  O  O   . PHE A 1 47  ? 35.494 6.721   24.094  1.00 26.72 ? 46  PHE A O   1 
ATOM   381  C  CB  . PHE A 1 47  ? 38.087 6.702   22.962  1.00 26.34 ? 46  PHE A CB  1 
ATOM   382  C  CG  . PHE A 1 47  ? 37.809 6.876   21.489  1.00 25.48 ? 46  PHE A CG  1 
ATOM   383  C  CD1 . PHE A 1 47  ? 36.614 7.438   21.053  1.00 25.12 ? 46  PHE A CD1 1 
ATOM   384  C  CD2 . PHE A 1 47  ? 38.759 6.503   20.541  1.00 25.41 ? 46  PHE A CD2 1 
ATOM   385  C  CE1 . PHE A 1 47  ? 36.371 7.627   19.701  1.00 25.43 ? 46  PHE A CE1 1 
ATOM   386  C  CE2 . PHE A 1 47  ? 38.522 6.690   19.178  1.00 25.11 ? 46  PHE A CE2 1 
ATOM   387  C  CZ  . PHE A 1 47  ? 37.328 7.253   18.760  1.00 24.66 ? 46  PHE A CZ  1 
ATOM   388  N  N   . LYS A 1 48  ? 35.269 4.494   23.894  1.00 29.85 ? 47  LYS A N   1 
ATOM   389  C  CA  . LYS A 1 48  ? 33.839 4.446   24.167  1.00 17.53 ? 47  LYS A CA  1 
ATOM   390  C  C   . LYS A 1 48  ? 33.491 4.984   25.568  1.00 25.95 ? 47  LYS A C   1 
ATOM   391  O  O   . LYS A 1 48  ? 32.357 5.374   25.824  1.00 25.55 ? 47  LYS A O   1 
ATOM   392  C  CB  . LYS A 1 48  ? 33.397 2.986   24.021  1.00 20.85 ? 47  LYS A CB  1 
ATOM   393  C  CG  . LYS A 1 48  ? 32.116 2.595   24.700  1.00 47.91 ? 47  LYS A CG  1 
ATOM   394  C  CD  . LYS A 1 48  ? 31.765 1.152   24.372  1.00 47.69 ? 47  LYS A CD  1 
ATOM   395  C  CE  . LYS A 1 48  ? 32.885 0.201   24.751  1.00 39.50 ? 47  LYS A CE  1 
ATOM   396  N  NZ  . LYS A 1 48  ? 32.549 -1.194  24.356  1.00 66.09 ? 47  LYS A NZ  1 
ATOM   397  N  N   . HIS A 1 49  ? 34.486 5.033   26.451  1.00 20.86 ? 48  HIS A N   1 
ATOM   398  C  CA  . HIS A 1 49  ? 34.304 5.486   27.833  1.00 21.06 ? 48  HIS A CA  1 
ATOM   399  C  C   . HIS A 1 49  ? 34.320 7.009   28.073  1.00 21.22 ? 48  HIS A C   1 
ATOM   400  O  O   . HIS A 1 49  ? 34.045 7.463   29.194  1.00 21.39 ? 48  HIS A O   1 
ATOM   401  C  CB  . HIS A 1 49  ? 35.377 4.843   28.708  1.00 20.17 ? 48  HIS A CB  1 
ATOM   402  C  CG  . HIS A 1 49  ? 36.762 5.241   28.324  1.00 24.11 ? 48  HIS A CG  1 
ATOM   403  N  ND1 . HIS A 1 49  ? 37.331 4.959   27.100  1.00 27.82 ? 48  HIS A ND1 1 
ATOM   404  C  CD2 . HIS A 1 49  ? 37.674 5.995   28.988  1.00 25.21 ? 48  HIS A CD2 1 
ATOM   405  C  CE1 . HIS A 1 49  ? 38.537 5.541   27.054  1.00 28.13 ? 48  HIS A CE1 1 
ATOM   406  N  NE2 . HIS A 1 49  ? 38.793 6.183   28.177  1.00 31.30 ? 48  HIS A NE2 1 
ATOM   407  N  N   . LEU A 1 50  ? 34.688 7.792   27.059  1.00 20.97 ? 49  LEU A N   1 
ATOM   408  C  CA  . LEU A 1 50  ? 34.741 9.252   27.205  1.00 20.81 ? 49  LEU A CA  1 
ATOM   409  C  C   . LEU A 1 50  ? 33.363 9.790   27.554  1.00 20.61 ? 49  LEU A C   1 
ATOM   410  O  O   . LEU A 1 50  ? 32.373 9.462   26.904  1.00 20.40 ? 49  LEU A O   1 
ATOM   411  C  CB  . LEU A 1 50  ? 35.281 9.911   25.934  1.00 21.23 ? 49  LEU A CB  1 
ATOM   412  C  CG  . LEU A 1 50  ? 36.624 9.372   25.431  1.00 21.36 ? 49  LEU A CG  1 
ATOM   413  C  CD1 . LEU A 1 50  ? 37.025 10.087  24.158  1.00 21.66 ? 49  LEU A CD1 1 
ATOM   414  C  CD2 . LEU A 1 50  ? 37.694 9.537   26.494  1.00 22.17 ? 49  LEU A CD2 1 
ATOM   415  N  N   . LYS A 1 51  ? 33.311 10.592  28.614  1.00 23.19 ? 50  LYS A N   1 
ATOM   416  C  CA  . LYS A 1 51  ? 32.056 11.148  29.124  1.00 26.12 ? 50  LYS A CA  1 
ATOM   417  C  C   . LYS A 1 51  ? 31.734 12.582  28.729  1.00 19.75 ? 50  LYS A C   1 
ATOM   418  O  O   . LYS A 1 51  ? 30.561 12.936  28.611  1.00 27.56 ? 50  LYS A O   1 
ATOM   419  C  CB  . LYS A 1 51  ? 32.033 11.065  30.656  1.00 27.93 ? 50  LYS A CB  1 
ATOM   420  C  CG  . LYS A 1 51  ? 32.205 9.664   31.236  1.00 22.56 ? 50  LYS A CG  1 
ATOM   421  C  CD  . LYS A 1 51  ? 32.397 9.745   32.751  1.00 29.71 ? 50  LYS A CD  1 
ATOM   422  C  CE  . LYS A 1 51  ? 32.597 8.376   33.394  1.00 33.46 ? 50  LYS A CE  1 
ATOM   423  N  NZ  . LYS A 1 51  ? 31.358 7.553   33.362  1.00 31.20 ? 50  LYS A NZ  1 
ATOM   424  N  N   . THR A 1 52  ? 32.761 13.406  28.541  1.00 17.64 ? 51  THR A N   1 
ATOM   425  C  CA  . THR A 1 52  ? 32.540 14.811  28.207  1.00 17.69 ? 51  THR A CA  1 
ATOM   426  C  C   . THR A 1 52  ? 33.324 15.294  27.000  1.00 17.46 ? 51  THR A C   1 
ATOM   427  O  O   . THR A 1 52  ? 34.255 14.636  26.556  1.00 17.20 ? 51  THR A O   1 
ATOM   428  C  CB  . THR A 1 52  ? 32.941 15.708  29.386  1.00 18.05 ? 51  THR A CB  1 
ATOM   429  O  OG1 . THR A 1 52  ? 34.360 15.651  29.558  1.00 17.93 ? 51  THR A OG1 1 
ATOM   430  C  CG2 . THR A 1 52  ? 32.265 15.247  30.672  1.00 18.36 ? 51  THR A CG2 1 
ATOM   431  N  N   . GLU A 1 53  ? 32.991 16.495  26.531  1.00 17.62 ? 52  GLU A N   1 
ATOM   432  C  CA  . GLU A 1 53  ? 33.674 17.089  25.393  1.00 17.54 ? 52  GLU A CA  1 
ATOM   433  C  C   . GLU A 1 53  ? 35.108 17.400  25.743  1.00 21.52 ? 52  GLU A C   1 
ATOM   434  O  O   . GLU A 1 53  ? 35.985 17.301  24.892  1.00 20.36 ? 52  GLU A O   1 
ATOM   435  C  CB  . GLU A 1 53  ? 32.981 18.365  24.919  1.00 19.57 ? 52  GLU A CB  1 
ATOM   436  C  CG  . GLU A 1 53  ? 33.720 19.033  23.757  1.00 25.46 ? 52  GLU A CG  1 
ATOM   437  C  CD  . GLU A 1 53  ? 32.907 20.112  23.059  1.00 34.52 ? 52  GLU A CD  1 
ATOM   438  O  OE1 . GLU A 1 53  ? 31.807 20.445  23.538  1.00 34.99 ? 52  GLU A OE1 1 
ATOM   439  O  OE2 . GLU A 1 53  ? 33.367 20.617  22.013  1.00 39.37 ? 52  GLU A OE2 1 
ATOM   440  N  N   . ALA A 1 54  ? 35.343 17.787  26.996  1.00 15.37 ? 53  ALA A N   1 
ATOM   441  C  CA  . ALA A 1 54  ? 36.688 18.089  27.453  1.00 15.13 ? 53  ALA A CA  1 
ATOM   442  C  C   . ALA A 1 54  ? 37.543 16.838  27.340  1.00 15.08 ? 53  ALA A C   1 
ATOM   443  O  O   . ALA A 1 54  ? 38.692 16.903  26.918  1.00 15.49 ? 53  ALA A O   1 
ATOM   444  C  CB  . ALA A 1 54  ? 36.665 18.581  28.900  1.00 15.35 ? 53  ALA A CB  1 
ATOM   445  N  N   . GLU A 1 55  ? 37.001 15.697  27.750  1.00 14.76 ? 54  GLU A N   1 
ATOM   446  C  CA  . GLU A 1 55  ? 37.754 14.447  27.653  1.00 12.01 ? 54  GLU A CA  1 
ATOM   447  C  C   . GLU A 1 55  ? 38.007 14.084  26.193  1.00 13.92 ? 54  GLU A C   1 
ATOM   448  O  O   . GLU A 1 55  ? 39.091 13.628  25.840  1.00 16.91 ? 54  GLU A O   1 
ATOM   449  C  CB  . GLU A 1 55  ? 37.012 13.318  28.349  1.00 14.48 ? 54  GLU A CB  1 
ATOM   450  C  CG  . GLU A 1 55  ? 37.169 13.386  29.849  1.00 26.43 ? 54  GLU A CG  1 
ATOM   451  C  CD  . GLU A 1 55  ? 36.329 12.375  30.591  1.00 25.73 ? 54  GLU A CD  1 
ATOM   452  O  OE1 . GLU A 1 55  ? 35.543 11.658  29.949  1.00 31.69 ? 54  GLU A OE1 1 
ATOM   453  O  OE2 . GLU A 1 55  ? 36.450 12.312  31.831  1.00 32.06 ? 54  GLU A OE2 1 
ATOM   454  N  N   . MET A 1 56  ? 37.008 14.300  25.348  1.00 16.12 ? 55  MET A N   1 
ATOM   455  C  CA  . MET A 1 56  ? 37.144 14.011  23.920  1.00 16.52 ? 55  MET A CA  1 
ATOM   456  C  C   . MET A 1 56  ? 38.235 14.878  23.279  1.00 16.13 ? 55  MET A C   1 
ATOM   457  O  O   . MET A 1 56  ? 39.064 14.380  22.512  1.00 15.55 ? 55  MET A O   1 
ATOM   458  C  CB  . MET A 1 56  ? 35.809 14.235  23.208  1.00 17.00 ? 55  MET A CB  1 
ATOM   459  C  CG  . MET A 1 56  ? 34.780 13.162  23.508  1.00 18.13 ? 55  MET A CG  1 
ATOM   460  S  SD  . MET A 1 56  ? 33.194 13.514  22.756  1.00 20.02 ? 55  MET A SD  1 
ATOM   461  C  CE  . MET A 1 56  ? 32.134 12.411  23.734  1.00 19.47 ? 55  MET A CE  1 
ATOM   462  N  N   . LYS A 1 57  ? 38.259 16.160  23.636  1.00 14.64 ? 56  LYS A N   1 
ATOM   463  C  CA  . LYS A 1 57  ? 39.245 17.094  23.089  1.00 19.54 ? 56  LYS A CA  1 
ATOM   464  C  C   . LYS A 1 57  ? 40.662 16.723  23.470  1.00 22.06 ? 56  LYS A C   1 
ATOM   465  O  O   . LYS A 1 57  ? 41.604 16.981  22.722  1.00 23.54 ? 56  LYS A O   1 
ATOM   466  C  CB  . LYS A 1 57  ? 38.972 18.515  23.580  1.00 20.18 ? 56  LYS A CB  1 
ATOM   467  C  CG  . LYS A 1 57  ? 37.814 19.216  22.912  1.00 33.45 ? 56  LYS A CG  1 
ATOM   468  C  CD  . LYS A 1 57  ? 37.654 20.603  23.507  1.00 39.86 ? 56  LYS A CD  1 
ATOM   469  C  CE  . LYS A 1 57  ? 36.505 21.355  22.883  1.00 61.63 ? 56  LYS A CE  1 
ATOM   470  N  NZ  . LYS A 1 57  ? 36.276 22.653  23.577  1.00 74.51 ? 56  LYS A NZ  1 
ATOM   471  N  N   . ALA A 1 58  ? 40.798 16.113  24.642  1.00 18.72 ? 57  ALA A N   1 
ATOM   472  C  CA  . ALA A 1 58  ? 42.087 15.711  25.182  1.00 18.55 ? 57  ALA A CA  1 
ATOM   473  C  C   . ALA A 1 58  ? 42.570 14.350  24.715  1.00 18.49 ? 57  ALA A C   1 
ATOM   474  O  O   . ALA A 1 58  ? 43.726 14.012  24.894  1.00 19.22 ? 57  ALA A O   1 
ATOM   475  C  CB  . ALA A 1 58  ? 42.018 15.735  26.704  1.00 18.54 ? 57  ALA A CB  1 
ATOM   476  N  N   . SER A 1 59  ? 41.688 13.572  24.103  1.00 18.63 ? 58  SER A N   1 
ATOM   477  C  CA  . SER A 1 59  ? 42.033 12.232  23.658  1.00 18.19 ? 58  SER A CA  1 
ATOM   478  C  C   . SER A 1 59  ? 42.875 12.150  22.390  1.00 18.90 ? 58  SER A C   1 
ATOM   479  O  O   . SER A 1 59  ? 42.458 12.586  21.319  1.00 19.29 ? 58  SER A O   1 
ATOM   480  C  CB  . SER A 1 59  ? 40.762 11.408  23.488  1.00 17.72 ? 58  SER A CB  1 
ATOM   481  O  OG  . SER A 1 59  ? 41.088 10.108  23.053  1.00 17.54 ? 58  SER A OG  1 
ATOM   482  N  N   . GLU A 1 60  ? 44.052 11.548  22.515  1.00 20.60 ? 59  GLU A N   1 
ATOM   483  C  CA  . GLU A 1 60  ? 44.953 11.377  21.386  1.00 21.93 ? 59  GLU A CA  1 
ATOM   484  C  C   . GLU A 1 60  ? 44.398 10.305  20.448  1.00 19.73 ? 59  GLU A C   1 
ATOM   485  O  O   . GLU A 1 60  ? 44.576 10.378  19.236  1.00 21.80 ? 59  GLU A O   1 
ATOM   486  C  CB  . GLU A 1 60  ? 46.341 10.976  21.888  1.00 29.78 ? 59  GLU A CB  1 
ATOM   487  C  CG  . GLU A 1 60  ? 47.460 11.873  21.392  1.00 54.96 ? 59  GLU A CG  1 
ATOM   488  C  CD  . GLU A 1 60  ? 47.238 13.337  21.726  1.00 61.96 ? 59  GLU A CD  1 
ATOM   489  O  OE1 . GLU A 1 60  ? 46.893 13.655  22.886  1.00 67.45 ? 59  GLU A OE1 1 
ATOM   490  O  OE2 . GLU A 1 60  ? 47.419 14.173  20.820  1.00 50.71 ? 59  GLU A OE2 1 
ATOM   491  N  N   . ASP A 1 61  ? 43.723 9.310   21.020  1.00 15.00 ? 60  ASP A N   1 
ATOM   492  C  CA  . ASP A 1 61  ? 43.131 8.238   20.236  1.00 12.99 ? 60  ASP A CA  1 
ATOM   493  C  C   . ASP A 1 61  ? 42.008 8.748   19.348  1.00 15.44 ? 60  ASP A C   1 
ATOM   494  O  O   . ASP A 1 61  ? 41.856 8.285   18.221  1.00 18.84 ? 60  ASP A O   1 
ATOM   495  C  CB  . ASP A 1 61  ? 42.574 7.138   21.138  1.00 16.99 ? 60  ASP A CB  1 
ATOM   496  C  CG  . ASP A 1 61  ? 43.650 6.195   21.647  1.00 29.43 ? 60  ASP A CG  1 
ATOM   497  O  OD1 . ASP A 1 61  ? 44.687 6.025   20.969  1.00 34.12 ? 60  ASP A OD1 1 
ATOM   498  O  OD2 . ASP A 1 61  ? 43.447 5.614   22.728  1.00 38.12 ? 60  ASP A OD2 1 
ATOM   499  N  N   . LEU A 1 62  ? 41.192 9.662   19.871  1.00 13.77 ? 61  LEU A N   1 
ATOM   500  C  CA  . LEU A 1 62  ? 40.079 10.213  19.098  1.00 13.73 ? 61  LEU A CA  1 
ATOM   501  C  C   . LEU A 1 62  ? 40.640 11.089  17.978  1.00 13.86 ? 61  LEU A C   1 
ATOM   502  O  O   . LEU A 1 62  ? 40.180 11.019  16.833  1.00 13.70 ? 61  LEU A O   1 
ATOM   503  C  CB  . LEU A 1 62  ? 39.120 11.003  20.003  1.00 13.68 ? 61  LEU A CB  1 
ATOM   504  C  CG  . LEU A 1 62  ? 37.849 11.616  19.397  1.00 13.93 ? 61  LEU A CG  1 
ATOM   505  C  CD1 . LEU A 1 62  ? 36.768 11.702  20.459  1.00 14.27 ? 61  LEU A CD1 1 
ATOM   506  C  CD2 . LEU A 1 62  ? 38.141 13.005  18.842  1.00 13.83 ? 61  LEU A CD2 1 
ATOM   507  N  N   . LYS A 1 63  ? 41.663 11.882  18.296  1.00 8.72  ? 62  LYS A N   1 
ATOM   508  C  CA  . LYS A 1 63  ? 42.278 12.735  17.277  1.00 14.29 ? 62  LYS A CA  1 
ATOM   509  C  C   . LYS A 1 63  ? 42.819 11.880  16.133  1.00 15.68 ? 62  LYS A C   1 
ATOM   510  O  O   . LYS A 1 63  ? 42.600 12.195  14.969  1.00 13.87 ? 62  LYS A O   1 
ATOM   511  C  CB  . LYS A 1 63  ? 43.405 13.597  17.866  1.00 18.20 ? 62  LYS A CB  1 
ATOM   512  C  CG  . LYS A 1 63  ? 44.117 14.455  16.821  1.00 18.75 ? 62  LYS A CG  1 
ATOM   513  C  CD  . LYS A 1 63  ? 44.745 15.685  17.434  1.00 40.62 ? 62  LYS A CD  1 
ATOM   514  C  CE  . LYS A 1 63  ? 45.886 15.330  18.356  1.00 53.65 ? 62  LYS A CE  1 
ATOM   515  N  NZ  . LYS A 1 63  ? 46.316 16.500  19.177  1.00 60.51 ? 62  LYS A NZ  1 
ATOM   516  N  N   . LYS A 1 64  ? 43.477 10.772  16.471  1.00 10.66 ? 63  LYS A N   1 
ATOM   517  C  CA  . LYS A 1 64  ? 44.028 9.882   15.451  1.00 13.30 ? 63  LYS A CA  1 
ATOM   518  C  C   . LYS A 1 64  ? 42.929 9.268   14.585  1.00 10.41 ? 63  LYS A C   1 
ATOM   519  O  O   . LYS A 1 64  ? 43.103 9.082   13.388  1.00 14.16 ? 63  LYS A O   1 
ATOM   520  C  CB  . LYS A 1 64  ? 44.883 8.784   16.090  1.00 21.76 ? 63  LYS A CB  1 
ATOM   521  C  CG  . LYS A 1 64  ? 46.102 9.333   16.844  1.00 43.10 ? 63  LYS A CG  1 
ATOM   522  C  CD  . LYS A 1 64  ? 47.195 8.279   17.047  1.00 63.52 ? 63  LYS A CD  1 
ATOM   523  C  CE  . LYS A 1 64  ? 46.857 7.259   18.126  1.00 72.49 ? 63  LYS A CE  1 
ATOM   524  N  NZ  . LYS A 1 64  ? 47.059 7.801   19.497  1.00 81.47 ? 63  LYS A NZ  1 
ATOM   525  N  N   . ALA A 1 65  ? 41.795 8.953   15.196  1.00 11.10 ? 64  ALA A N   1 
ATOM   526  C  CA  . ALA A 1 65  ? 40.678 8.361   14.468  1.00 10.65 ? 64  ALA A CA  1 
ATOM   527  C  C   . ALA A 1 65  ? 40.121 9.380   13.472  1.00 10.82 ? 64  ALA A C   1 
ATOM   528  O  O   . ALA A 1 65  ? 39.698 9.019   12.376  1.00 10.68 ? 64  ALA A O   1 
ATOM   529  C  CB  . ALA A 1 65  ? 39.591 7.936   15.445  1.00 10.54 ? 64  ALA A CB  1 
ATOM   530  N  N   . GLY A 1 66  ? 40.087 10.645  13.892  1.00 10.58 ? 65  GLY A N   1 
ATOM   531  C  CA  . GLY A 1 66  ? 39.592 11.714  13.039  1.00 10.18 ? 65  GLY A CA  1 
ATOM   532  C  C   . GLY A 1 66  ? 40.507 11.907  11.839  1.00 10.33 ? 65  GLY A C   1 
ATOM   533  O  O   . GLY A 1 66  ? 40.024 12.106  10.731  1.00 10.03 ? 65  GLY A O   1 
ATOM   534  N  N   . VAL A 1 67  ? 41.822 11.849  12.057  1.00 9.96  ? 66  VAL A N   1 
ATOM   535  C  CA  . VAL A 1 67  ? 42.787 12.005  10.970  1.00 10.73 ? 66  VAL A CA  1 
ATOM   536  C  C   . VAL A 1 67  ? 42.626 10.848  9.987   1.00 10.72 ? 66  VAL A C   1 
ATOM   537  O  O   . VAL A 1 67  ? 42.689 11.038  8.777   1.00 11.43 ? 66  VAL A O   1 
ATOM   538  C  CB  . VAL A 1 67  ? 44.246 12.051  11.501  1.00 10.75 ? 66  VAL A CB  1 
ATOM   539  C  CG1 . VAL A 1 67  ? 45.249 11.916  10.336  1.00 11.02 ? 66  VAL A CG1 1 
ATOM   540  C  CG2 . VAL A 1 67  ? 44.495 13.367  12.246  1.00 10.52 ? 66  VAL A CG2 1 
ATOM   541  N  N   . THR A 1 68  ? 42.366 9.662   10.513  1.00 10.64 ? 67  THR A N   1 
ATOM   542  C  CA  . THR A 1 68  ? 42.178 8.476   9.680   1.00 10.82 ? 67  THR A CA  1 
ATOM   543  C  C   . THR A 1 68  ? 40.926 8.618   8.809   1.00 10.20 ? 67  THR A C   1 
ATOM   544  O  O   . THR A 1 68  ? 40.942 8.329   7.606   1.00 10.05 ? 67  THR A O   1 
ATOM   545  C  CB  . THR A 1 68  ? 42.088 7.232   10.571  1.00 11.70 ? 67  THR A CB  1 
ATOM   546  O  OG1 . THR A 1 68  ? 43.336 7.077   11.262  1.00 12.96 ? 67  THR A OG1 1 
ATOM   547  C  CG2 . THR A 1 68  ? 41.802 5.974   9.759   1.00 11.99 ? 67  THR A CG2 1 
ATOM   548  N  N   . VAL A 1 69  ? 39.851 9.108   9.402   1.00 10.09 ? 68  VAL A N   1 
ATOM   549  C  CA  . VAL A 1 69  ? 38.609 9.291   8.664   1.00 9.84  ? 68  VAL A CA  1 
ATOM   550  C  C   . VAL A 1 69  ? 38.788 10.296  7.525   1.00 10.25 ? 68  VAL A C   1 
ATOM   551  O  O   . VAL A 1 69  ? 38.418 10.033  6.371   1.00 9.81  ? 68  VAL A O   1 
ATOM   552  C  CB  . VAL A 1 69  ? 37.472 9.776   9.604   1.00 10.58 ? 68  VAL A CB  1 
ATOM   553  C  CG1 . VAL A 1 69  ? 36.277 10.303  8.793   1.00 10.49 ? 68  VAL A CG1 1 
ATOM   554  C  CG2 . VAL A 1 69  ? 37.018 8.631   10.474  1.00 10.64 ? 68  VAL A CG2 1 
ATOM   555  N  N   . LEU A 1 70  ? 39.375 11.444  7.838   1.00 10.19 ? 69  LEU A N   1 
ATOM   556  C  CA  . LEU A 1 70  ? 39.557 12.480  6.826   1.00 10.49 ? 69  LEU A CA  1 
ATOM   557  C  C   . LEU A 1 70  ? 40.539 12.139  5.729   1.00 10.34 ? 69  LEU A C   1 
ATOM   558  O  O   . LEU A 1 70  ? 40.320 12.505  4.579   1.00 10.71 ? 69  LEU A O   1 
ATOM   559  C  CB  . LEU A 1 70  ? 39.907 13.824  7.461   1.00 11.16 ? 69  LEU A CB  1 
ATOM   560  C  CG  . LEU A 1 70  ? 38.813 14.427  8.339   1.00 12.35 ? 69  LEU A CG  1 
ATOM   561  C  CD1 . LEU A 1 70  ? 39.243 15.834  8.732   1.00 12.65 ? 69  LEU A CD1 1 
ATOM   562  C  CD2 . LEU A 1 70  ? 37.478 14.464  7.601   1.00 13.73 ? 69  LEU A CD2 1 
ATOM   563  N  N   . THR A 1 71  ? 41.619 11.453  6.075   1.00 9.99  ? 70  THR A N   1 
ATOM   564  C  CA  . THR A 1 71  ? 42.606 11.058  5.084   1.00 10.46 ? 70  THR A CA  1 
ATOM   565  C  C   . THR A 1 71  ? 41.970 10.066  4.103   1.00 10.27 ? 70  THR A C   1 
ATOM   566  O  O   . THR A 1 71  ? 42.177 10.171  2.896   1.00 10.51 ? 70  THR A O   1 
ATOM   567  C  CB  . THR A 1 71  ? 43.842 10.427  5.765   1.00 11.25 ? 70  THR A CB  1 
ATOM   568  O  OG1 . THR A 1 71  ? 44.436 11.401  6.633   1.00 12.10 ? 70  THR A OG1 1 
ATOM   569  C  CG2 . THR A 1 71  ? 44.877 9.988   4.725   1.00 12.16 ? 70  THR A CG2 1 
ATOM   570  N  N   . ALA A 1 72  ? 41.180 9.118   4.610   1.00 9.68  ? 71  ALA A N   1 
ATOM   571  C  CA  . ALA A 1 72  ? 40.525 8.141   3.731   1.00 9.74  ? 71  ALA A CA  1 
ATOM   572  C  C   . ALA A 1 72  ? 39.451 8.811   2.860   1.00 9.86  ? 71  ALA A C   1 
ATOM   573  O  O   . ALA A 1 72  ? 39.358 8.552   1.667   1.00 10.25 ? 71  ALA A O   1 
ATOM   574  C  CB  . ALA A 1 72  ? 39.912 7.027   4.548   1.00 8.94  ? 71  ALA A CB  1 
ATOM   575  N  N   . LEU A 1 73  ? 38.650 9.689   3.458   1.00 10.05 ? 72  LEU A N   1 
ATOM   576  C  CA  . LEU A 1 73  ? 37.599 10.384  2.724   1.00 10.08 ? 72  LEU A CA  1 
ATOM   577  C  C   . LEU A 1 73  ? 38.204 11.328  1.687   1.00 9.95  ? 72  LEU A C   1 
ATOM   578  O  O   . LEU A 1 73  ? 37.706 11.435  0.569   1.00 10.46 ? 72  LEU A O   1 
ATOM   579  C  CB  . LEU A 1 73  ? 36.698 11.156  3.690   1.00 10.55 ? 72  LEU A CB  1 
ATOM   580  C  CG  . LEU A 1 73  ? 35.546 11.915  3.032   1.00 11.55 ? 72  LEU A CG  1 
ATOM   581  C  CD1 . LEU A 1 73  ? 34.687 10.941  2.228   1.00 12.61 ? 72  LEU A CD1 1 
ATOM   582  C  CD2 . LEU A 1 73  ? 34.711 12.658  4.091   1.00 12.72 ? 72  LEU A CD2 1 
ATOM   583  N  N   . GLY A 1 74  ? 39.300 11.978  2.048   1.00 9.89  ? 73  GLY A N   1 
ATOM   584  C  CA  . GLY A 1 74  ? 39.958 12.885  1.123   1.00 10.36 ? 73  GLY A CA  1 
ATOM   585  C  C   . GLY A 1 74  ? 40.455 12.148  -0.107  1.00 10.40 ? 73  GLY A C   1 
ATOM   586  O  O   . GLY A 1 74  ? 40.346 12.651  -1.222  1.00 10.37 ? 73  GLY A O   1 
ATOM   587  N  N   . ALA A 1 75  ? 40.976 10.941  0.081   1.00 10.61 ? 74  ALA A N   1 
ATOM   588  C  CA  . ALA A 1 75  ? 41.494 10.163  -1.048  1.00 11.32 ? 74  ALA A CA  1 
ATOM   589  C  C   . ALA A 1 75  ? 40.356 9.795   -2.001  1.00 11.30 ? 74  ALA A C   1 
ATOM   590  O  O   . ALA A 1 75  ? 40.520 9.801   -3.229  1.00 12.20 ? 74  ALA A O   1 
ATOM   591  C  CB  . ALA A 1 75  ? 42.214 8.917   -0.548  1.00 11.47 ? 74  ALA A CB  1 
ATOM   592  N  N   . ILE A 1 76  ? 39.193 9.526   -1.423  1.00 10.72 ? 75  ILE A N   1 
ATOM   593  C  CA  . ILE A 1 76  ? 38.004 9.168   -2.184  1.00 10.41 ? 75  ILE A CA  1 
ATOM   594  C  C   . ILE A 1 76  ? 37.489 10.375  -2.968  1.00 10.39 ? 75  ILE A C   1 
ATOM   595  O  O   . ILE A 1 76  ? 37.261 10.288  -4.171  1.00 10.65 ? 75  ILE A O   1 
ATOM   596  C  CB  . ILE A 1 76  ? 36.909 8.579   -1.229  1.00 10.59 ? 75  ILE A CB  1 
ATOM   597  C  CG1 . ILE A 1 76  ? 37.318 7.155   -0.817  1.00 10.45 ? 75  ILE A CG1 1 
ATOM   598  C  CG2 . ILE A 1 76  ? 35.523 8.568   -1.888  1.00 9.92  ? 75  ILE A CG2 1 
ATOM   599  C  CD1 . ILE A 1 76  ? 36.584 6.618   0.393   1.00 12.29 ? 75  ILE A CD1 1 
ATOM   600  N  N   . LEU A 1 77  ? 37.367 11.520  -2.309  1.00 9.93  ? 76  LEU A N   1 
ATOM   601  C  CA  . LEU A 1 77  ? 36.873 12.713  -2.989  1.00 9.64  ? 76  LEU A CA  1 
ATOM   602  C  C   . LEU A 1 77  ? 37.765 13.147  -4.150  1.00 10.08 ? 76  LEU A C   1 
ATOM   603  O  O   . LEU A 1 77  ? 37.269 13.585  -5.186  1.00 10.23 ? 76  LEU A O   1 
ATOM   604  C  CB  . LEU A 1 77  ? 36.703 13.860  -1.999  1.00 9.03  ? 76  LEU A CB  1 
ATOM   605  C  CG  . LEU A 1 77  ? 35.641 13.696  -0.916  1.00 9.98  ? 76  LEU A CG  1 
ATOM   606  C  CD1 . LEU A 1 77  ? 35.747 14.894  0.036   1.00 10.06 ? 76  LEU A CD1 1 
ATOM   607  C  CD2 . LEU A 1 77  ? 34.228 13.618  -1.528  1.00 9.33  ? 76  LEU A CD2 1 
ATOM   608  N  N   . LYS A 1 78  ? 39.081 13.023  -3.985  1.00 6.59  ? 77  LYS A N   1 
ATOM   609  C  CA  . LYS A 1 78  ? 40.007 13.419  -5.041  1.00 6.32  ? 77  LYS A CA  1 
ATOM   610  C  C   . LYS A 1 78  ? 39.931 12.539  -6.281  1.00 12.36 ? 77  LYS A C   1 
ATOM   611  O  O   . LYS A 1 78  ? 40.459 12.904  -7.320  1.00 12.12 ? 77  LYS A O   1 
ATOM   612  C  CB  . LYS A 1 78  ? 41.435 13.489  -4.508  1.00 10.42 ? 77  LYS A CB  1 
ATOM   613  C  CG  . LYS A 1 78  ? 41.635 14.621  -3.510  1.00 13.56 ? 77  LYS A CG  1 
ATOM   614  C  CD  . LYS A 1 78  ? 42.938 14.460  -2.765  1.00 12.31 ? 77  LYS A CD  1 
ATOM   615  C  CE  . LYS A 1 78  ? 43.140 15.595  -1.799  1.00 19.75 ? 77  LYS A CE  1 
ATOM   616  N  NZ  . LYS A 1 78  ? 44.455 15.492  -1.115  1.00 21.72 ? 77  LYS A NZ  1 
ATOM   617  N  N   . LYS A 1 79  ? 39.288 11.374  -6.168  1.00 12.38 ? 78  LYS A N   1 
ATOM   618  C  CA  . LYS A 1 79  ? 39.110 10.475  -7.319  1.00 13.90 ? 78  LYS A CA  1 
ATOM   619  C  C   . LYS A 1 79  ? 37.963 10.966  -8.203  1.00 14.28 ? 78  LYS A C   1 
ATOM   620  O  O   . LYS A 1 79  ? 37.730 10.435  -9.289  1.00 15.58 ? 78  LYS A O   1 
ATOM   621  C  CB  . LYS A 1 79  ? 38.811 9.032   -6.873  1.00 11.74 ? 78  LYS A CB  1 
ATOM   622  C  CG  . LYS A 1 79  ? 39.925 8.360   -6.070  1.00 20.95 ? 78  LYS A CG  1 
ATOM   623  C  CD  . LYS A 1 79  ? 41.294 8.474   -6.744  1.00 25.45 ? 78  LYS A CD  1 
ATOM   624  C  CE  . LYS A 1 79  ? 41.363 7.699   -8.048  1.00 29.25 ? 78  LYS A CE  1 
ATOM   625  N  NZ  . LYS A 1 79  ? 41.213 6.242   -7.823  1.00 51.61 ? 78  LYS A NZ  1 
ATOM   626  N  N   . LYS A 1 80  ? 37.200 11.926  -7.687  1.00 7.71  ? 79  LYS A N   1 
ATOM   627  C  CA  . LYS A 1 80  ? 36.080 12.514  -8.413  1.00 9.68  ? 79  LYS A CA  1 
ATOM   628  C  C   . LYS A 1 80  ? 35.095 11.490  -8.979  1.00 14.76 ? 79  LYS A C   1 
ATOM   629  O  O   . LYS A 1 80  ? 34.706 11.553  -10.146 1.00 13.18 ? 79  LYS A O   1 
ATOM   630  C  CB  . LYS A 1 80  ? 36.609 13.452  -9.508  1.00 9.57  ? 79  LYS A CB  1 
ATOM   631  C  CG  . LYS A 1 80  ? 37.354 14.648  -8.941  1.00 13.96 ? 79  LYS A CG  1 
ATOM   632  C  CD  . LYS A 1 80  ? 38.263 15.304  -9.945  1.00 22.47 ? 79  LYS A CD  1 
ATOM   633  C  CE  . LYS A 1 80  ? 37.497 15.907  -11.080 1.00 27.28 ? 79  LYS A CE  1 
ATOM   634  N  NZ  . LYS A 1 80  ? 38.412 16.719  -11.940 1.00 38.86 ? 79  LYS A NZ  1 
ATOM   635  N  N   . GLY A 1 81  ? 34.696 10.542  -8.138  1.00 11.55 ? 80  GLY A N   1 
ATOM   636  C  CA  . GLY A 1 81  ? 33.734 9.535   -8.554  1.00 11.69 ? 80  GLY A CA  1 
ATOM   637  C  C   . GLY A 1 81  ? 34.297 8.194   -9.002  1.00 12.40 ? 80  GLY A C   1 
ATOM   638  O  O   . GLY A 1 81  ? 33.560 7.206   -9.030  1.00 12.61 ? 80  GLY A O   1 
ATOM   639  N  N   . HIS A 1 82  ? 35.579 8.147   -9.363  1.00 12.24 ? 81  HIS A N   1 
ATOM   640  C  CA  . HIS A 1 82  ? 36.215 6.911   -9.823  1.00 12.56 ? 81  HIS A CA  1 
ATOM   641  C  C   . HIS A 1 82  ? 36.891 6.297   -8.621  1.00 12.80 ? 81  HIS A C   1 
ATOM   642  O  O   . HIS A 1 82  ? 38.101 6.113   -8.604  1.00 13.05 ? 81  HIS A O   1 
ATOM   643  C  CB  . HIS A 1 82  ? 37.251 7.260   -10.889 1.00 13.85 ? 81  HIS A CB  1 
ATOM   644  C  CG  . HIS A 1 82  ? 36.662 7.872   -12.126 1.00 17.82 ? 81  HIS A CG  1 
ATOM   645  N  ND1 . HIS A 1 82  ? 36.554 9.228   -12.348 1.00 20.01 ? 81  HIS A ND1 1 
ATOM   646  C  CD2 . HIS A 1 82  ? 36.152 7.280   -13.235 1.00 14.86 ? 81  HIS A CD2 1 
ATOM   647  C  CE1 . HIS A 1 82  ? 35.999 9.404   -13.555 1.00 18.63 ? 81  HIS A CE1 1 
ATOM   648  N  NE2 . HIS A 1 82  ? 35.736 8.247   -14.132 1.00 20.38 ? 81  HIS A NE2 1 
ATOM   649  N  N   . HIS A 1 83  ? 36.084 5.919   -7.639  1.00 13.33 ? 82  HIS A N   1 
ATOM   650  C  CA  . HIS A 1 83  ? 36.603 5.426   -6.359  1.00 13.54 ? 82  HIS A CA  1 
ATOM   651  C  C   . HIS A 1 83  ? 36.306 3.973   -6.001  1.00 13.89 ? 82  HIS A C   1 
ATOM   652  O  O   . HIS A 1 83  ? 36.385 3.590   -4.827  1.00 14.05 ? 82  HIS A O   1 
ATOM   653  C  CB  . HIS A 1 83  ? 36.043 6.330   -5.254  1.00 10.72 ? 82  HIS A CB  1 
ATOM   654  C  CG  . HIS A 1 83  ? 34.554 6.447   -5.288  1.00 10.65 ? 82  HIS A CG  1 
ATOM   655  N  ND1 . HIS A 1 83  ? 33.864 7.624   -5.108  1.00 12.53 ? 82  HIS A ND1 1 
ATOM   656  C  CD2 . HIS A 1 83  ? 33.608 5.503   -5.528  1.00 11.94 ? 82  HIS A CD2 1 
ATOM   657  C  CE1 . HIS A 1 83  ? 32.556 7.360   -5.240  1.00 14.48 ? 82  HIS A CE1 1 
ATOM   658  N  NE2 . HIS A 1 83  ? 32.350 6.084   -5.498  1.00 14.32 ? 82  HIS A NE2 1 
ATOM   659  N  N   . GLU A 1 84  ? 35.936 3.173   -6.990  1.00 16.30 ? 83  GLU A N   1 
ATOM   660  C  CA  . GLU A 1 84  ? 35.622 1.774   -6.734  1.00 17.14 ? 83  GLU A CA  1 
ATOM   661  C  C   . GLU A 1 84  ? 36.715 1.037   -5.965  1.00 21.36 ? 83  GLU A C   1 
ATOM   662  O  O   . GLU A 1 84  ? 36.423 0.370   -4.975  1.00 17.53 ? 83  GLU A O   1 
ATOM   663  C  CB  . GLU A 1 84  ? 35.260 1.039   -8.037  1.00 23.83 ? 83  GLU A CB  1 
ATOM   664  C  CG  . GLU A 1 84  ? 36.100 1.399   -9.273  1.00 53.77 ? 83  GLU A CG  1 
ATOM   665  C  CD  . GLU A 1 84  ? 35.798 2.788   -9.860  1.00 57.01 ? 83  GLU A CD  1 
ATOM   666  O  OE1 . GLU A 1 84  ? 34.656 3.285   -9.704  1.00 57.45 ? 83  GLU A OE1 1 
ATOM   667  O  OE2 . GLU A 1 84  ? 36.714 3.384   -10.472 1.00 42.54 ? 83  GLU A OE2 1 
ATOM   668  N  N   . ALA A 1 85  ? 37.976 1.227   -6.357  1.00 21.49 ? 84  ALA A N   1 
ATOM   669  C  CA  . ALA A 1 85  ? 39.091 0.564   -5.684  1.00 21.34 ? 84  ALA A CA  1 
ATOM   670  C  C   . ALA A 1 85  ? 39.243 0.969   -4.229  1.00 21.53 ? 84  ALA A C   1 
ATOM   671  O  O   . ALA A 1 85  ? 39.506 0.127   -3.376  1.00 21.57 ? 84  ALA A O   1 
ATOM   672  C  CB  . ALA A 1 85  ? 40.380 0.815   -6.422  1.00 21.47 ? 84  ALA A CB  1 
ATOM   673  N  N   . GLU A 1 86  ? 39.111 2.261   -3.948  1.00 17.24 ? 85  GLU A N   1 
ATOM   674  C  CA  . GLU A 1 86  ? 39.228 2.769   -2.577  1.00 19.87 ? 85  GLU A CA  1 
ATOM   675  C  C   . GLU A 1 86  ? 38.078 2.320   -1.680  1.00 22.45 ? 85  GLU A C   1 
ATOM   676  O  O   . GLU A 1 86  ? 38.260 2.141   -0.476  1.00 21.28 ? 85  GLU A O   1 
ATOM   677  C  CB  . GLU A 1 86  ? 39.269 4.310   -2.560  1.00 18.49 ? 85  GLU A CB  1 
ATOM   678  C  CG  . GLU A 1 86  ? 40.553 4.931   -3.088  1.00 20.74 ? 85  GLU A CG  1 
ATOM   679  C  CD  . GLU A 1 86  ? 40.709 4.778   -4.590  1.00 29.20 ? 85  GLU A CD  1 
ATOM   680  O  OE1 . GLU A 1 86  ? 39.687 4.790   -5.305  1.00 26.33 ? 85  GLU A OE1 1 
ATOM   681  O  OE2 . GLU A 1 86  ? 41.855 4.652   -5.061  1.00 43.47 ? 85  GLU A OE2 1 
ATOM   682  N  N   . LEU A 1 87  ? 36.903 2.139   -2.275  1.00 18.57 ? 86  LEU A N   1 
ATOM   683  C  CA  . LEU A 1 87  ? 35.707 1.759   -1.543  1.00 18.89 ? 86  LEU A CA  1 
ATOM   684  C  C   . LEU A 1 87  ? 35.621 0.315   -1.065  1.00 18.82 ? 86  LEU A C   1 
ATOM   685  O  O   . LEU A 1 87  ? 34.994 0.033   -0.051  1.00 18.14 ? 86  LEU A O   1 
ATOM   686  C  CB  . LEU A 1 87  ? 34.480 2.057   -2.399  1.00 20.41 ? 86  LEU A CB  1 
ATOM   687  C  CG  . LEU A 1 87  ? 33.370 2.879   -1.763  1.00 21.85 ? 86  LEU A CG  1 
ATOM   688  C  CD1 . LEU A 1 87  ? 33.883 4.279   -1.451  1.00 22.52 ? 86  LEU A CD1 1 
ATOM   689  C  CD2 . LEU A 1 87  ? 32.206 2.957   -2.741  1.00 22.72 ? 86  LEU A CD2 1 
ATOM   690  N  N   . LYS A 1 88  ? 36.228 -0.602  -1.806  1.00 16.40 ? 87  LYS A N   1 
ATOM   691  C  CA  . LYS A 1 88  ? 36.169 -2.019  -1.465  1.00 15.31 ? 87  LYS A CA  1 
ATOM   692  C  C   . LYS A 1 88  ? 36.625 -2.407  -0.054  1.00 14.49 ? 87  LYS A C   1 
ATOM   693  O  O   . LYS A 1 88  ? 35.848 -2.969  0.717   1.00 16.10 ? 87  LYS A O   1 
ATOM   694  C  CB  . LYS A 1 88  ? 36.912 -2.832  -2.526  1.00 15.87 ? 87  LYS A CB  1 
ATOM   695  C  CG  . LYS A 1 88  ? 36.326 -2.639  -3.891  1.00 32.93 ? 87  LYS A CG  1 
ATOM   696  C  CD  . LYS A 1 88  ? 37.231 -3.154  -4.987  1.00 48.07 ? 87  LYS A CD  1 
ATOM   697  C  CE  . LYS A 1 88  ? 37.152 -4.652  -5.116  1.00 45.65 ? 87  LYS A CE  1 
ATOM   698  N  NZ  . LYS A 1 88  ? 37.633 -5.076  -6.461  1.00 47.04 ? 87  LYS A NZ  1 
ATOM   699  N  N   . PRO A 1 89  ? 37.877 -2.090  0.314   1.00 13.98 ? 88  PRO A N   1 
ATOM   700  C  CA  . PRO A 1 89  ? 38.327 -2.458  1.655   1.00 13.58 ? 88  PRO A CA  1 
ATOM   701  C  C   . PRO A 1 89  ? 37.568 -1.720  2.754   1.00 13.66 ? 88  PRO A C   1 
ATOM   702  O  O   . PRO A 1 89  ? 37.344 -2.266  3.835   1.00 13.81 ? 88  PRO A O   1 
ATOM   703  C  CB  . PRO A 1 89  ? 39.812 -2.089  1.621   1.00 14.37 ? 88  PRO A CB  1 
ATOM   704  C  CG  . PRO A 1 89  ? 39.871 -0.954  0.629   1.00 14.03 ? 88  PRO A CG  1 
ATOM   705  C  CD  . PRO A 1 89  ? 38.953 -1.426  -0.448  1.00 14.51 ? 88  PRO A CD  1 
ATOM   706  N  N   . LEU A 1 90  ? 37.162 -0.485  2.467   1.00 13.19 ? 89  LEU A N   1 
ATOM   707  C  CA  . LEU A 1 90  ? 36.431 0.338   3.422   1.00 13.03 ? 89  LEU A CA  1 
ATOM   708  C  C   . LEU A 1 90  ? 35.046 -0.252  3.702   1.00 12.64 ? 89  LEU A C   1 
ATOM   709  O  O   . LEU A 1 90  ? 34.594 -0.307  4.848   1.00 12.09 ? 89  LEU A O   1 
ATOM   710  C  CB  . LEU A 1 90  ? 36.291 1.751   2.844   1.00 14.71 ? 89  LEU A CB  1 
ATOM   711  C  CG  . LEU A 1 90  ? 35.582 2.798   3.690   1.00 16.03 ? 89  LEU A CG  1 
ATOM   712  C  CD1 . LEU A 1 90  ? 36.384 3.014   4.977   1.00 17.45 ? 89  LEU A CD1 1 
ATOM   713  C  CD2 . LEU A 1 90  ? 35.472 4.095   2.894   1.00 17.33 ? 89  LEU A CD2 1 
ATOM   714  N  N   . ALA A 1 91  ? 34.366 -0.676  2.643   1.00 11.94 ? 90  ALA A N   1 
ATOM   715  C  CA  . ALA A 1 91  ? 33.038 -1.264  2.766   1.00 11.43 ? 90  ALA A CA  1 
ATOM   716  C  C   . ALA A 1 91  ? 33.174 -2.580  3.501   1.00 11.36 ? 90  ALA A C   1 
ATOM   717  O  O   . ALA A 1 91  ? 32.392 -2.881  4.394   1.00 10.87 ? 90  ALA A O   1 
ATOM   718  C  CB  . ALA A 1 91  ? 32.440 -1.489  1.395   1.00 12.18 ? 90  ALA A CB  1 
ATOM   719  N  N   . GLN A 1 92  ? 34.206 -3.351  3.176   1.00 11.20 ? 91  GLN A N   1 
ATOM   720  C  CA  . GLN A 1 92  ? 34.378 -4.627  3.869   1.00 11.15 ? 91  GLN A CA  1 
ATOM   721  C  C   . GLN A 1 92  ? 34.607 -4.487  5.370   1.00 11.16 ? 91  GLN A C   1 
ATOM   722  O  O   . GLN A 1 92  ? 33.958 -5.168  6.150   1.00 11.00 ? 91  GLN A O   1 
ATOM   723  C  CB  . GLN A 1 92  ? 35.493 -5.483  3.263   1.00 11.20 ? 91  GLN A CB  1 
ATOM   724  C  CG  . GLN A 1 92  ? 35.580 -6.851  3.948   1.00 13.56 ? 91  GLN A CG  1 
ATOM   725  C  CD  . GLN A 1 92  ? 36.645 -7.749  3.361   1.00 19.17 ? 91  GLN A CD  1 
ATOM   726  O  OE1 . GLN A 1 92  ? 37.748 -7.309  3.086   1.00 14.73 ? 91  GLN A OE1 1 
ATOM   727  N  NE2 . GLN A 1 92  ? 36.321 -9.022  3.188   1.00 11.18 ? 91  GLN A NE2 1 
ATOM   728  N  N   . SER A 1 93  ? 35.530 -3.629  5.792   1.00 11.05 ? 92  SER A N   1 
ATOM   729  C  CA  . SER A 1 93  ? 35.759 -3.488  7.229   1.00 11.24 ? 92  SER A CA  1 
ATOM   730  C  C   . SER A 1 93  ? 34.571 -2.885  7.976   1.00 11.52 ? 92  SER A C   1 
ATOM   731  O  O   . SER A 1 93  ? 34.223 -3.342  9.064   1.00 11.73 ? 92  SER A O   1 
ATOM   732  C  CB  . SER A 1 93  ? 37.018 -2.678  7.511   1.00 11.25 ? 92  SER A CB  1 
ATOM   733  O  OG  . SER A 1 93  ? 36.847 -1.334  7.112   1.00 12.35 ? 92  SER A OG  1 
ATOM   734  N  N   . HIS A 1 94  ? 33.919 -1.882  7.400   1.00 11.27 ? 93  HIS A N   1 
ATOM   735  C  CA  . HIS A 1 94  ? 32.792 -1.265  8.094   1.00 11.80 ? 93  HIS A CA  1 
ATOM   736  C  C   . HIS A 1 94  ? 31.525 -2.108  8.145   1.00 12.25 ? 93  HIS A C   1 
ATOM   737  O  O   . HIS A 1 94  ? 30.716 -1.968  9.058   1.00 12.33 ? 93  HIS A O   1 
ATOM   738  C  CB  . HIS A 1 94  ? 32.535 0.139   7.556   1.00 10.39 ? 93  HIS A CB  1 
ATOM   739  C  CG  . HIS A 1 94  ? 33.597 1.102   7.955   1.00 7.06  ? 93  HIS A CG  1 
ATOM   740  N  ND1 . HIS A 1 94  ? 34.923 0.901   7.644   1.00 14.63 ? 93  HIS A ND1 1 
ATOM   741  C  CD2 . HIS A 1 94  ? 33.558 2.192   8.753   1.00 11.89 ? 93  HIS A CD2 1 
ATOM   742  C  CE1 . HIS A 1 94  ? 35.660 1.819   8.240   1.00 13.46 ? 93  HIS A CE1 1 
ATOM   743  N  NE2 . HIS A 1 94  ? 34.856 2.619   8.919   1.00 13.00 ? 93  HIS A NE2 1 
ATOM   744  N  N   . ALA A 1 95  ? 31.363 -2.999  7.177   1.00 12.99 ? 94  ALA A N   1 
ATOM   745  C  CA  . ALA A 1 95  ? 30.203 -3.879  7.162   1.00 14.15 ? 94  ALA A CA  1 
ATOM   746  C  C   . ALA A 1 95  ? 30.443 -5.125  8.025   1.00 14.92 ? 94  ALA A C   1 
ATOM   747  O  O   . ALA A 1 95  ? 29.643 -5.446  8.899   1.00 15.88 ? 94  ALA A O   1 
ATOM   748  C  CB  . ALA A 1 95  ? 29.888 -4.316  5.729   1.00 13.95 ? 94  ALA A CB  1 
ATOM   749  N  N   . THR A 1 96  ? 31.600 -5.749  7.839   1.00 15.36 ? 95  THR A N   1 
ATOM   750  C  CA  . THR A 1 96  ? 31.942 -7.011  8.499   1.00 15.76 ? 95  THR A CA  1 
ATOM   751  C  C   . THR A 1 96  ? 32.634 -6.974  9.845   1.00 16.40 ? 95  THR A C   1 
ATOM   752  O  O   . THR A 1 96  ? 32.323 -7.792  10.712  1.00 17.41 ? 95  THR A O   1 
ATOM   753  C  CB  . THR A 1 96  ? 32.797 -7.876  7.551   1.00 16.12 ? 95  THR A CB  1 
ATOM   754  O  OG1 . THR A 1 96  ? 32.200 -7.865  6.254   1.00 16.21 ? 95  THR A OG1 1 
ATOM   755  C  CG2 . THR A 1 96  ? 32.886 -9.318  8.042   1.00 15.32 ? 95  THR A CG2 1 
ATOM   756  N  N   . LYS A 1 97  ? 33.604 -6.080  10.010  1.00 14.49 ? 96  LYS A N   1 
ATOM   757  C  CA  . LYS A 1 97  ? 34.339 -5.999  11.269  1.00 13.81 ? 96  LYS A CA  1 
ATOM   758  C  C   . LYS A 1 97  ? 33.683 -5.042  12.268  1.00 15.37 ? 96  LYS A C   1 
ATOM   759  O  O   . LYS A 1 97  ? 33.266 -5.446  13.352  1.00 23.84 ? 96  LYS A O   1 
ATOM   760  C  CB  . LYS A 1 97  ? 35.791 -5.581  11.006  1.00 15.51 ? 96  LYS A CB  1 
ATOM   761  C  CG  . LYS A 1 97  ? 36.680 -5.666  12.247  1.00 22.79 ? 96  LYS A CG  1 
ATOM   762  C  CD  . LYS A 1 97  ? 38.038 -5.009  12.041  1.00 43.86 ? 96  LYS A CD  1 
ATOM   763  C  CE  . LYS A 1 97  ? 39.128 -6.005  11.662  1.00 64.91 ? 96  LYS A CE  1 
ATOM   764  N  NZ  . LYS A 1 97  ? 38.985 -6.572  10.295  1.00 62.45 ? 96  LYS A NZ  1 
ATOM   765  N  N   . HIS A 1 98  ? 33.538 -3.784  11.866  1.00 15.38 ? 97  HIS A N   1 
ATOM   766  C  CA  . HIS A 1 98  ? 32.959 -2.738  12.713  1.00 15.66 ? 97  HIS A CA  1 
ATOM   767  C  C   . HIS A 1 98  ? 31.431 -2.718  12.815  1.00 15.94 ? 97  HIS A C   1 
ATOM   768  O  O   . HIS A 1 98  ? 30.899 -2.222  13.801  1.00 16.66 ? 97  HIS A O   1 
ATOM   769  C  CB  . HIS A 1 98  ? 33.453 -1.373  12.229  1.00 14.52 ? 97  HIS A CB  1 
ATOM   770  C  CG  . HIS A 1 98  ? 34.919 -1.339  11.938  1.00 13.89 ? 97  HIS A CG  1 
ATOM   771  N  ND1 . HIS A 1 98  ? 35.878 -1.898  12.753  1.00 14.09 ? 97  HIS A ND1 1 
ATOM   772  C  CD2 . HIS A 1 98  ? 35.592 -0.822  10.878  1.00 12.59 ? 97  HIS A CD2 1 
ATOM   773  C  CE1 . HIS A 1 98  ? 37.080 -1.708  12.180  1.00 13.26 ? 97  HIS A CE1 1 
ATOM   774  N  NE2 . HIS A 1 98  ? 36.959 -1.059  11.039  1.00 12.61 ? 97  HIS A NE2 1 
ATOM   775  N  N   . LYS A 1 99  ? 30.740 -3.225  11.788  1.00 17.77 ? 98  LYS A N   1 
ATOM   776  C  CA  . LYS A 1 99  ? 29.266 -3.269  11.724  1.00 21.81 ? 98  LYS A CA  1 
ATOM   777  C  C   . LYS A 1 99  ? 28.608 -1.896  11.868  1.00 24.76 ? 98  LYS A C   1 
ATOM   778  O  O   . LYS A 1 99  ? 27.818 -1.649  12.779  1.00 18.78 ? 98  LYS A O   1 
ATOM   779  C  CB  . LYS A 1 99  ? 28.702 -4.263  12.748  1.00 27.28 ? 98  LYS A CB  1 
ATOM   780  C  CG  . LYS A 1 99  ? 28.485 -5.660  12.177  1.00 50.07 ? 98  LYS A CG  1 
ATOM   781  C  CD  . LYS A 1 99  ? 29.123 -6.751  13.019  1.00 50.17 ? 98  LYS A CD  1 
ATOM   782  C  CE  . LYS A 1 99  ? 30.630 -6.732  12.886  1.00 63.11 ? 98  LYS A CE  1 
ATOM   783  N  NZ  . LYS A 1 99  ? 31.292 -7.959  13.425  1.00 51.62 ? 98  LYS A NZ  1 
ATOM   784  N  N   . ILE A 1 100 ? 28.911 -1.026  10.911  1.00 18.32 ? 99  ILE A N   1 
ATOM   785  C  CA  . ILE A 1 100 ? 28.413 0.337   10.882  1.00 17.72 ? 99  ILE A CA  1 
ATOM   786  C  C   . ILE A 1 100 ? 27.241 0.480   9.921   1.00 18.03 ? 99  ILE A C   1 
ATOM   787  O  O   . ILE A 1 100 ? 27.407 0.396   8.699   1.00 18.32 ? 99  ILE A O   1 
ATOM   788  C  CB  . ILE A 1 100 ? 29.532 1.313   10.411  1.00 17.43 ? 99  ILE A CB  1 
ATOM   789  C  CG1 . ILE A 1 100 ? 30.821 1.109   11.230  1.00 17.21 ? 99  ILE A CG1 1 
ATOM   790  C  CG2 . ILE A 1 100 ? 29.023 2.764   10.417  1.00 17.35 ? 99  ILE A CG2 1 
ATOM   791  C  CD1 . ILE A 1 100 ? 30.652 1.114   12.750  1.00 17.14 ? 99  ILE A CD1 1 
ATOM   792  N  N   . PRO A 1 101 ? 26.041 0.737   10.454  1.00 18.18 ? 100 PRO A N   1 
ATOM   793  C  CA  . PRO A 1 101 ? 24.892 0.889   9.554   1.00 18.77 ? 100 PRO A CA  1 
ATOM   794  C  C   . PRO A 1 101 ? 24.976 2.161   8.703   1.00 19.04 ? 100 PRO A C   1 
ATOM   795  O  O   . PRO A 1 101 ? 25.634 3.129   9.086   1.00 18.81 ? 100 PRO A O   1 
ATOM   796  C  CB  . PRO A 1 101 ? 23.693 0.900   10.520  1.00 18.76 ? 100 PRO A CB  1 
ATOM   797  C  CG  . PRO A 1 101 ? 24.274 1.377   11.810  1.00 18.52 ? 100 PRO A CG  1 
ATOM   798  C  CD  . PRO A 1 101 ? 25.624 0.718   11.868  1.00 18.47 ? 100 PRO A CD  1 
ATOM   799  N  N   . ILE A 1 102 ? 24.339 2.139   7.536   1.00 19.39 ? 101 ILE A N   1 
ATOM   800  C  CA  . ILE A 1 102 ? 24.329 3.292   6.631   1.00 20.23 ? 101 ILE A CA  1 
ATOM   801  C  C   . ILE A 1 102 ? 23.859 4.539   7.360   1.00 20.22 ? 101 ILE A C   1 
ATOM   802  O  O   . ILE A 1 102 ? 24.303 5.645   7.068   1.00 20.58 ? 101 ILE A O   1 
ATOM   803  C  CB  . ILE A 1 102 ? 23.396 3.036   5.397   1.00 20.90 ? 101 ILE A CB  1 
ATOM   804  C  CG1 . ILE A 1 102 ? 23.974 1.915   4.526   1.00 21.69 ? 101 ILE A CG1 1 
ATOM   805  C  CG2 . ILE A 1 102 ? 23.173 4.314   4.589   1.00 21.19 ? 101 ILE A CG2 1 
ATOM   806  C  CD1 . ILE A 1 102 ? 25.420 2.149   4.080   1.00 22.66 ? 101 ILE A CD1 1 
ATOM   807  N  N   . LYS A 1 103 ? 22.955 4.334   8.311   1.00 15.20 ? 102 LYS A N   1 
ATOM   808  C  CA  . LYS A 1 103 ? 22.379 5.389   9.128   1.00 21.32 ? 102 LYS A CA  1 
ATOM   809  C  C   . LYS A 1 103 ? 23.485 6.228   9.759   1.00 13.06 ? 102 LYS A C   1 
ATOM   810  O  O   . LYS A 1 103 ? 23.404 7.455   9.784   1.00 16.30 ? 102 LYS A O   1 
ATOM   811  C  CB  . LYS A 1 103 ? 21.523 4.739   10.227  1.00 30.45 ? 102 LYS A CB  1 
ATOM   812  C  CG  . LYS A 1 103 ? 20.797 5.684   11.164  1.00 48.16 ? 102 LYS A CG  1 
ATOM   813  C  CD  . LYS A 1 103 ? 19.698 6.452   10.451  1.00 61.25 ? 102 LYS A CD  1 
ATOM   814  C  CE  . LYS A 1 103 ? 18.846 7.202   11.458  1.00 72.91 ? 102 LYS A CE  1 
ATOM   815  N  NZ  . LYS A 1 103 ? 17.920 8.200   10.858  1.00 79.71 ? 102 LYS A NZ  1 
ATOM   816  N  N   . TYR A 1 104 ? 24.518 5.561   10.260  1.00 11.33 ? 103 TYR A N   1 
ATOM   817  C  CA  . TYR A 1 104 ? 25.632 6.256   10.901  1.00 11.22 ? 103 TYR A CA  1 
ATOM   818  C  C   . TYR A 1 104 ? 26.486 7.019   9.894   1.00 10.83 ? 103 TYR A C   1 
ATOM   819  O  O   . TYR A 1 104 ? 27.180 7.974   10.261  1.00 10.34 ? 103 TYR A O   1 
ATOM   820  C  CB  . TYR A 1 104 ? 26.501 5.283   11.698  1.00 12.02 ? 103 TYR A CB  1 
ATOM   821  C  CG  . TYR A 1 104 ? 25.859 4.735   12.966  1.00 13.21 ? 103 TYR A CG  1 
ATOM   822  C  CD1 . TYR A 1 104 ? 24.515 4.946   13.247  1.00 14.16 ? 103 TYR A CD1 1 
ATOM   823  C  CD2 . TYR A 1 104 ? 26.610 3.983   13.873  1.00 13.80 ? 103 TYR A CD2 1 
ATOM   824  C  CE1 . TYR A 1 104 ? 23.926 4.413   14.407  1.00 15.23 ? 103 TYR A CE1 1 
ATOM   825  C  CE2 . TYR A 1 104 ? 26.042 3.454   15.019  1.00 14.79 ? 103 TYR A CE2 1 
ATOM   826  C  CZ  . TYR A 1 104 ? 24.704 3.668   15.281  1.00 15.43 ? 103 TYR A CZ  1 
ATOM   827  O  OH  . TYR A 1 104 ? 24.141 3.121   16.412  1.00 17.32 ? 103 TYR A OH  1 
ATOM   828  N  N   . LEU A 1 105 ? 26.487 6.566   8.638   1.00 10.91 ? 104 LEU A N   1 
ATOM   829  C  CA  . LEU A 1 105 ? 27.250 7.268   7.600   1.00 10.95 ? 104 LEU A CA  1 
ATOM   830  C  C   . LEU A 1 105 ? 26.497 8.551   7.255   1.00 10.90 ? 104 LEU A C   1 
ATOM   831  O  O   . LEU A 1 105 ? 27.095 9.541   6.851   1.00 10.38 ? 104 LEU A O   1 
ATOM   832  C  CB  . LEU A 1 105 ? 27.461 6.392   6.359   1.00 11.55 ? 104 LEU A CB  1 
ATOM   833  C  CG  . LEU A 1 105 ? 28.243 5.115   6.668   1.00 12.08 ? 104 LEU A CG  1 
ATOM   834  C  CD1 . LEU A 1 105 ? 28.328 4.263   5.432   1.00 13.00 ? 104 LEU A CD1 1 
ATOM   835  C  CD2 . LEU A 1 105 ? 29.619 5.461   7.157   1.00 12.57 ? 104 LEU A CD2 1 
ATOM   836  N  N   . GLU A 1 106 ? 25.174 8.528   7.406   1.00 10.57 ? 105 GLU A N   1 
ATOM   837  C  CA  . GLU A 1 106 ? 24.389 9.728   7.169   1.00 9.30  ? 105 GLU A CA  1 
ATOM   838  C  C   . GLU A 1 106 ? 24.700 10.716  8.306   1.00 13.86 ? 105 GLU A C   1 
ATOM   839  O  O   . GLU A 1 106 ? 24.866 11.916  8.071   1.00 12.19 ? 105 GLU A O   1 
ATOM   840  C  CB  . GLU A 1 106 ? 22.898 9.397   7.136   1.00 15.20 ? 105 GLU A CB  1 
ATOM   841  C  CG  . GLU A 1 106 ? 22.482 8.739   5.831   1.00 27.76 ? 105 GLU A CG  1 
ATOM   842  C  CD  . GLU A 1 106 ? 21.056 8.226   5.838   1.00 38.89 ? 105 GLU A CD  1 
ATOM   843  O  OE1 . GLU A 1 106 ? 20.238 8.703   6.648   1.00 35.62 ? 105 GLU A OE1 1 
ATOM   844  O  OE2 . GLU A 1 106 ? 20.752 7.331   5.027   1.00 38.64 ? 105 GLU A OE2 1 
ATOM   845  N  N   . PHE A 1 107 ? 24.805 10.197  9.530   1.00 10.92 ? 106 PHE A N   1 
ATOM   846  C  CA  . PHE A 1 107 ? 25.108 11.027  10.698  1.00 11.11 ? 106 PHE A CA  1 
ATOM   847  C  C   . PHE A 1 107 ? 26.457 11.727  10.580  1.00 11.11 ? 106 PHE A C   1 
ATOM   848  O  O   . PHE A 1 107 ? 26.586 12.911  10.918  1.00 10.96 ? 106 PHE A O   1 
ATOM   849  C  CB  . PHE A 1 107 ? 25.124 10.182  11.966  1.00 11.90 ? 106 PHE A CB  1 
ATOM   850  C  CG  . PHE A 1 107 ? 23.777 9.650   12.370  1.00 13.28 ? 106 PHE A CG  1 
ATOM   851  C  CD1 . PHE A 1 107 ? 22.611 10.168  11.824  1.00 14.16 ? 106 PHE A CD1 1 
ATOM   852  C  CD2 . PHE A 1 107 ? 23.682 8.661   13.336  1.00 13.64 ? 106 PHE A CD2 1 
ATOM   853  C  CE1 . PHE A 1 107 ? 21.356 9.707   12.240  1.00 15.28 ? 106 PHE A CE1 1 
ATOM   854  C  CE2 . PHE A 1 107 ? 22.439 8.194   13.759  1.00 14.65 ? 106 PHE A CE2 1 
ATOM   855  C  CZ  . PHE A 1 107 ? 21.280 8.721   13.211  1.00 15.22 ? 106 PHE A CZ  1 
ATOM   856  N  N   . ILE A 1 108 ? 27.477 11.004  10.126  1.00 10.55 ? 107 ILE A N   1 
ATOM   857  C  CA  . ILE A 1 108 ? 28.787 11.635  10.013  1.00 10.14 ? 107 ILE A CA  1 
ATOM   858  C  C   . ILE A 1 108 ? 28.804 12.625  8.848   1.00 10.39 ? 107 ILE A C   1 
ATOM   859  O  O   . ILE A 1 108 ? 29.532 13.614  8.890   1.00 9.64  ? 107 ILE A O   1 
ATOM   860  C  CB  . ILE A 1 108 ? 29.955 10.606  9.921   1.00 10.51 ? 107 ILE A CB  1 
ATOM   861  C  CG1 . ILE A 1 108 ? 31.281 11.292  10.327  1.00 10.17 ? 107 ILE A CG1 1 
ATOM   862  C  CG2 . ILE A 1 108 ? 30.034 9.996   8.517   1.00 9.97  ? 107 ILE A CG2 1 
ATOM   863  C  CD1 . ILE A 1 108 ? 32.466 10.334  10.499  1.00 10.76 ? 107 ILE A CD1 1 
ATOM   864  N  N   . SER A 1 109 ? 27.967 12.382  7.837   1.00 10.13 ? 108 SER A N   1 
ATOM   865  C  CA  . SER A 1 109 ? 27.885 13.281  6.687   1.00 10.34 ? 108 SER A CA  1 
ATOM   866  C  C   . SER A 1 109 ? 27.352 14.630  7.142   1.00 10.73 ? 108 SER A C   1 
ATOM   867  O  O   . SER A 1 109 ? 27.819 15.671  6.686   1.00 10.50 ? 108 SER A O   1 
ATOM   868  C  CB  . SER A 1 109 ? 26.983 12.703  5.604   1.00 10.68 ? 108 SER A CB  1 
ATOM   869  O  OG  . SER A 1 109 ? 27.593 11.559  5.015   1.00 12.10 ? 108 SER A OG  1 
ATOM   870  N  N   . GLU A 1 110 ? 26.408 14.598  8.082   1.00 8.69  ? 109 GLU A N   1 
ATOM   871  C  CA  . GLU A 1 110 ? 25.804 15.806  8.628   1.00 9.14  ? 109 GLU A CA  1 
ATOM   872  C  C   . GLU A 1 110 ? 26.812 16.539  9.497   1.00 6.68  ? 109 GLU A C   1 
ATOM   873  O  O   . GLU A 1 110 ? 26.839 17.774  9.522   1.00 10.73 ? 109 GLU A O   1 
ATOM   874  C  CB  . GLU A 1 110 ? 24.565 15.451  9.460   1.00 15.27 ? 109 GLU A CB  1 
ATOM   875  C  CG  . GLU A 1 110 ? 23.978 16.629  10.235  1.00 35.60 ? 109 GLU A CG  1 
ATOM   876  C  CD  . GLU A 1 110 ? 22.837 16.222  11.158  1.00 60.12 ? 109 GLU A CD  1 
ATOM   877  O  OE1 . GLU A 1 110 ? 22.997 15.249  11.936  1.00 59.25 ? 109 GLU A OE1 1 
ATOM   878  O  OE2 . GLU A 1 110 ? 21.778 16.887  11.108  1.00 68.94 ? 109 GLU A OE2 1 
ATOM   879  N  N   . ALA A 1 111 ? 27.638 15.785  10.214  1.00 7.33  ? 110 ALA A N   1 
ATOM   880  C  CA  . ALA A 1 111 ? 28.653 16.397  11.071  1.00 7.34  ? 110 ALA A CA  1 
ATOM   881  C  C   . ALA A 1 111 ? 29.708 17.093  10.212  1.00 7.79  ? 110 ALA A C   1 
ATOM   882  O  O   . ALA A 1 111 ? 30.213 18.160  10.579  1.00 8.04  ? 110 ALA A O   1 
ATOM   883  C  CB  . ALA A 1 111 ? 29.318 15.346  11.972  1.00 7.61  ? 110 ALA A CB  1 
ATOM   884  N  N   . ILE A 1 112 ? 30.029 16.502  9.064   1.00 7.42  ? 111 ILE A N   1 
ATOM   885  C  CA  . ILE A 1 112 ? 31.027 17.096  8.174   1.00 8.01  ? 111 ILE A CA  1 
ATOM   886  C  C   . ILE A 1 112 ? 30.493 18.411  7.622   1.00 8.43  ? 111 ILE A C   1 
ATOM   887  O  O   . ILE A 1 112 ? 31.180 19.427  7.625   1.00 8.53  ? 111 ILE A O   1 
ATOM   888  C  CB  . ILE A 1 112 ? 31.382 16.130  7.014   1.00 8.16  ? 111 ILE A CB  1 
ATOM   889  C  CG1 . ILE A 1 112 ? 32.207 14.960  7.553   1.00 7.94  ? 111 ILE A CG1 1 
ATOM   890  C  CG2 . ILE A 1 112 ? 32.146 16.875  5.907   1.00 8.37  ? 111 ILE A CG2 1 
ATOM   891  C  CD1 . ILE A 1 112 ? 32.269 13.769  6.631   1.00 8.87  ? 111 ILE A CD1 1 
ATOM   892  N  N   . ILE A 1 113 ? 29.246 18.400  7.186   1.00 8.68  ? 112 ILE A N   1 
ATOM   893  C  CA  . ILE A 1 113 ? 28.643 19.614  6.646   1.00 10.12 ? 112 ILE A CA  1 
ATOM   894  C  C   . ILE A 1 113 ? 28.550 20.738  7.698   1.00 10.31 ? 112 ILE A C   1 
ATOM   895  O  O   . ILE A 1 113 ? 28.850 21.896  7.397   1.00 10.39 ? 112 ILE A O   1 
ATOM   896  C  CB  . ILE A 1 113 ? 27.271 19.299  6.011   1.00 10.61 ? 112 ILE A CB  1 
ATOM   897  C  CG1 . ILE A 1 113 ? 27.498 18.490  4.728   1.00 11.44 ? 112 ILE A CG1 1 
ATOM   898  C  CG2 . ILE A 1 113 ? 26.482 20.607  5.730   1.00 11.49 ? 112 ILE A CG2 1 
ATOM   899  C  CD1 . ILE A 1 113 ? 26.241 17.839  4.179   1.00 12.82 ? 112 ILE A CD1 1 
ATOM   900  N  N   . HIS A 1 114 ? 28.216 20.375  8.939   1.00 10.42 ? 113 HIS A N   1 
ATOM   901  C  CA  . HIS A 1 114 ? 28.103 21.344  10.020  1.00 10.49 ? 113 HIS A CA  1 
ATOM   902  C  C   . HIS A 1 114 ? 29.455 21.994  10.314  1.00 10.76 ? 113 HIS A C   1 
ATOM   903  O  O   . HIS A 1 114 ? 29.549 23.211  10.450  1.00 11.11 ? 113 HIS A O   1 
ATOM   904  C  CB  . HIS A 1 114 ? 27.554 20.662  11.282  1.00 12.95 ? 113 HIS A CB  1 
ATOM   905  C  CG  . HIS A 1 114 ? 27.553 21.539  12.500  1.00 17.44 ? 113 HIS A CG  1 
ATOM   906  N  ND1 . HIS A 1 114 ? 26.448 22.217  12.966  1.00 23.03 ? 113 HIS A ND1 1 
ATOM   907  C  CD2 . HIS A 1 114 ? 28.557 21.842  13.362  1.00 19.26 ? 113 HIS A CD2 1 
ATOM   908  C  CE1 . HIS A 1 114 ? 26.808 22.893  14.068  1.00 22.28 ? 113 HIS A CE1 1 
ATOM   909  N  NE2 . HIS A 1 114 ? 28.081 22.695  14.348  1.00 23.07 ? 113 HIS A NE2 1 
ATOM   910  N  N   . VAL A 1 115 ? 30.508 21.188  10.397  1.00 10.13 ? 114 VAL A N   1 
ATOM   911  C  CA  . VAL A 1 115 ? 31.830 21.724  10.684  1.00 10.03 ? 114 VAL A CA  1 
ATOM   912  C  C   . VAL A 1 115 ? 32.381 22.605  9.547   1.00 10.14 ? 114 VAL A C   1 
ATOM   913  O  O   . VAL A 1 115 ? 32.944 23.661  9.814   1.00 10.13 ? 114 VAL A O   1 
ATOM   914  C  CB  . VAL A 1 115 ? 32.812 20.588  11.064  1.00 10.51 ? 114 VAL A CB  1 
ATOM   915  C  CG1 . VAL A 1 115 ? 34.246 21.110  11.135  1.00 10.11 ? 114 VAL A CG1 1 
ATOM   916  C  CG2 . VAL A 1 115 ? 32.398 20.007  12.405  1.00 9.35  ? 114 VAL A CG2 1 
ATOM   917  N  N   . LEU A 1 116 ? 32.240 22.179  8.289   1.00 9.97  ? 115 LEU A N   1 
ATOM   918  C  CA  . LEU A 1 116 ? 32.713 23.011  7.173   1.00 10.17 ? 115 LEU A CA  1 
ATOM   919  C  C   . LEU A 1 116 ? 31.950 24.331  7.160   1.00 10.41 ? 115 LEU A C   1 
ATOM   920  O  O   . LEU A 1 116 ? 32.515 25.381  6.875   1.00 10.19 ? 115 LEU A O   1 
ATOM   921  C  CB  . LEU A 1 116 ? 32.532 22.315  5.822   1.00 10.42 ? 115 LEU A CB  1 
ATOM   922  C  CG  . LEU A 1 116 ? 33.339 21.030  5.615   1.00 12.07 ? 115 LEU A CG  1 
ATOM   923  C  CD1 . LEU A 1 116 ? 33.300 20.605  4.173   1.00 12.97 ? 115 LEU A CD1 1 
ATOM   924  C  CD2 . LEU A 1 116 ? 34.752 21.264  6.016   1.00 13.34 ? 115 LEU A CD2 1 
ATOM   925  N  N   . HIS A 1 117 ? 30.651 24.266  7.450   1.00 10.67 ? 116 HIS A N   1 
ATOM   926  C  CA  . HIS A 1 117 ? 29.821 25.460  7.487   1.00 11.51 ? 116 HIS A CA  1 
ATOM   927  C  C   . HIS A 1 117 ? 30.304 26.403  8.593   1.00 12.32 ? 116 HIS A C   1 
ATOM   928  O  O   . HIS A 1 117 ? 30.339 27.620  8.388   1.00 12.36 ? 116 HIS A O   1 
ATOM   929  C  CB  . HIS A 1 117 ? 28.349 25.083  7.700   1.00 13.42 ? 116 HIS A CB  1 
ATOM   930  C  CG  . HIS A 1 117 ? 27.430 26.260  7.851   1.00 16.07 ? 116 HIS A CG  1 
ATOM   931  N  ND1 . HIS A 1 117 ? 26.931 26.995  6.798   1.00 22.58 ? 116 HIS A ND1 1 
ATOM   932  C  CD2 . HIS A 1 117 ? 26.907 26.822  8.970   1.00 15.62 ? 116 HIS A CD2 1 
ATOM   933  C  CE1 . HIS A 1 117 ? 26.141 27.956  7.303   1.00 16.64 ? 116 HIS A CE1 1 
ATOM   934  N  NE2 . HIS A 1 117 ? 26.096 27.890  8.618   1.00 20.44 ? 116 HIS A NE2 1 
ATOM   935  N  N   . SER A 1 118 ? 30.689 25.852  9.746   1.00 12.40 ? 117 SER A N   1 
ATOM   936  C  CA  . SER A 1 118 ? 31.176 26.680  10.858  1.00 13.42 ? 117 SER A CA  1 
ATOM   937  C  C   . SER A 1 118 ? 32.549 27.294  10.598  1.00 13.19 ? 117 SER A C   1 
ATOM   938  O  O   . SER A 1 118 ? 32.742 28.489  10.823  1.00 13.50 ? 117 SER A O   1 
ATOM   939  C  CB  . SER A 1 118 ? 31.288 25.879  12.165  1.00 14.20 ? 117 SER A CB  1 
ATOM   940  O  OG  . SER A 1 118 ? 30.065 25.256  12.503  1.00 18.35 ? 117 SER A OG  1 
ATOM   941  N  N   . ARG A 1 119 ? 33.490 26.483  10.110  1.00 12.21 ? 118 ARG A N   1 
ATOM   942  C  CA  . ARG A 1 119 ? 34.861 26.948  9.886   1.00 11.87 ? 118 ARG A CA  1 
ATOM   943  C  C   . ARG A 1 119 ? 35.188 27.644  8.578   1.00 12.00 ? 118 ARG A C   1 
ATOM   944  O  O   . ARG A 1 119 ? 36.150 28.408  8.522   1.00 12.02 ? 118 ARG A O   1 
ATOM   945  C  CB  . ARG A 1 119 ? 35.852 25.796  10.103  1.00 11.86 ? 118 ARG A CB  1 
ATOM   946  C  CG  . ARG A 1 119 ? 35.912 25.310  11.552  1.00 16.68 ? 118 ARG A CG  1 
ATOM   947  C  CD  . ARG A 1 119 ? 36.826 24.094  11.730  1.00 13.63 ? 118 ARG A CD  1 
ATOM   948  N  NE  . ARG A 1 119 ? 38.225 24.415  11.481  1.00 20.08 ? 118 ARG A NE  1 
ATOM   949  C  CZ  . ARG A 1 119 ? 39.254 23.864  12.121  1.00 27.30 ? 118 ARG A CZ  1 
ATOM   950  N  NH1 . ARG A 1 119 ? 39.056 22.964  13.080  1.00 13.60 ? 118 ARG A NH1 1 
ATOM   951  N  NH2 . ARG A 1 119 ? 40.492 24.223  11.801  1.00 16.09 ? 118 ARG A NH2 1 
ATOM   952  N  N   . HIS A 1 120 ? 34.387 27.414  7.536   1.00 11.48 ? 119 HIS A N   1 
ATOM   953  C  CA  . HIS A 1 120 ? 34.654 28.007  6.223   1.00 11.65 ? 119 HIS A CA  1 
ATOM   954  C  C   . HIS A 1 120 ? 33.431 28.664  5.604   1.00 12.44 ? 119 HIS A C   1 
ATOM   955  O  O   . HIS A 1 120 ? 33.080 28.373  4.455   1.00 12.47 ? 119 HIS A O   1 
ATOM   956  C  CB  . HIS A 1 120 ? 35.161 26.911  5.273   1.00 9.10  ? 119 HIS A CB  1 
ATOM   957  C  CG  . HIS A 1 120 ? 36.305 26.130  5.832   1.00 11.96 ? 119 HIS A CG  1 
ATOM   958  N  ND1 . HIS A 1 120 ? 37.593 26.606  5.905   1.00 10.79 ? 119 HIS A ND1 1 
ATOM   959  C  CD2 . HIS A 1 120 ? 36.322 24.921  6.448   1.00 6.08  ? 119 HIS A CD2 1 
ATOM   960  C  CE1 . HIS A 1 120 ? 38.325 25.696  6.562   1.00 9.70  ? 119 HIS A CE1 1 
ATOM   961  N  NE2 . HIS A 1 120 ? 37.591 24.654  6.907   1.00 10.06 ? 119 HIS A NE2 1 
ATOM   962  N  N   . PRO A 1 121 ? 32.809 29.616  6.316   1.00 13.22 ? 120 PRO A N   1 
ATOM   963  C  CA  . PRO A 1 121 ? 31.619 30.265  5.760   1.00 14.02 ? 120 PRO A CA  1 
ATOM   964  C  C   . PRO A 1 121 ? 31.799 30.908  4.385   1.00 14.67 ? 120 PRO A C   1 
ATOM   965  O  O   . PRO A 1 121 ? 30.903 30.840  3.547   1.00 15.54 ? 120 PRO A O   1 
ATOM   966  C  CB  . PRO A 1 121 ? 31.239 31.275  6.848   1.00 14.34 ? 120 PRO A CB  1 
ATOM   967  C  CG  . PRO A 1 121 ? 32.537 31.559  7.540   1.00 13.87 ? 120 PRO A CG  1 
ATOM   968  C  CD  . PRO A 1 121 ? 33.169 30.202  7.620   1.00 13.24 ? 120 PRO A CD  1 
ATOM   969  N  N   . GLY A 1 122 ? 32.982 31.446  4.125   1.00 15.20 ? 121 GLY A N   1 
ATOM   970  C  CA  . GLY A 1 122 ? 33.239 32.095  2.850   1.00 15.19 ? 121 GLY A CA  1 
ATOM   971  C  C   . GLY A 1 122 ? 33.418 31.135  1.693   1.00 15.61 ? 121 GLY A C   1 
ATOM   972  O  O   . GLY A 1 122 ? 33.197 31.510  0.534   1.00 16.99 ? 121 GLY A O   1 
ATOM   973  N  N   . ASN A 1 123 ? 33.826 29.904  1.979   1.00 14.49 ? 122 ASN A N   1 
ATOM   974  C  CA  . ASN A 1 123 ? 34.021 28.929  0.911   1.00 13.76 ? 122 ASN A CA  1 
ATOM   975  C  C   . ASN A 1 123 ? 32.974 27.846  0.959   1.00 13.67 ? 122 ASN A C   1 
ATOM   976  O  O   . ASN A 1 123 ? 33.044 26.863  0.210   1.00 14.46 ? 122 ASN A O   1 
ATOM   977  C  CB  . ASN A 1 123 ? 35.413 28.300  1.002   1.00 13.02 ? 122 ASN A CB  1 
ATOM   978  C  CG  . ASN A 1 123 ? 36.510 29.292  0.687   1.00 17.64 ? 122 ASN A CG  1 
ATOM   979  O  OD1 . ASN A 1 123 ? 37.436 29.500  1.476   1.00 19.83 ? 122 ASN A OD1 1 
ATOM   980  N  ND2 . ASN A 1 123 ? 36.401 29.924  -0.466  1.00 9.15  ? 122 ASN A ND2 1 
ATOM   981  N  N   . PHE A 1 124 ? 31.995 28.017  1.834   1.00 12.60 ? 123 PHE A N   1 
ATOM   982  C  CA  . PHE A 1 124 ? 30.956 27.016  1.960   1.00 11.40 ? 123 PHE A CA  1 
ATOM   983  C  C   . PHE A 1 124 ? 29.565 27.636  1.901   1.00 11.21 ? 123 PHE A C   1 
ATOM   984  O  O   . PHE A 1 124 ? 28.774 27.498  2.829   1.00 10.94 ? 123 PHE A O   1 
ATOM   985  C  CB  . PHE A 1 124 ? 31.143 26.228  3.252   1.00 9.96  ? 123 PHE A CB  1 
ATOM   986  C  CG  . PHE A 1 124 ? 30.593 24.840  3.198   1.00 9.19  ? 123 PHE A CG  1 
ATOM   987  C  CD1 . PHE A 1 124 ? 31.156 23.889  2.352   1.00 8.23  ? 123 PHE A CD1 1 
ATOM   988  C  CD2 . PHE A 1 124 ? 29.544 24.465  4.036   1.00 9.05  ? 123 PHE A CD2 1 
ATOM   989  C  CE1 . PHE A 1 124 ? 30.680 22.572  2.345   1.00 8.36  ? 123 PHE A CE1 1 
ATOM   990  C  CE2 . PHE A 1 124 ? 29.062 23.157  4.045   1.00 9.00  ? 123 PHE A CE2 1 
ATOM   991  C  CZ  . PHE A 1 124 ? 29.633 22.203  3.194   1.00 8.45  ? 123 PHE A CZ  1 
ATOM   992  N  N   . GLY A 1 125 ? 29.302 28.337  0.804   1.00 10.84 ? 124 GLY A N   1 
ATOM   993  C  CA  . GLY A 1 125 ? 28.006 28.942  0.576   1.00 10.99 ? 124 GLY A CA  1 
ATOM   994  C  C   . GLY A 1 125 ? 27.038 27.860  0.119   1.00 11.04 ? 124 GLY A C   1 
ATOM   995  O  O   . GLY A 1 125 ? 27.392 26.682  0.083   1.00 10.84 ? 124 GLY A O   1 
ATOM   996  N  N   . ALA A 1 126 ? 25.833 28.256  -0.283  1.00 11.12 ? 125 ALA A N   1 
ATOM   997  C  CA  . ALA A 1 126 ? 24.801 27.295  -0.691  1.00 11.15 ? 125 ALA A CA  1 
ATOM   998  C  C   . ALA A 1 126 ? 25.192 26.363  -1.824  1.00 11.07 ? 125 ALA A C   1 
ATOM   999  O  O   . ALA A 1 126 ? 24.911 25.175  -1.770  1.00 11.88 ? 125 ALA A O   1 
ATOM   1000 C  CB  . ALA A 1 126 ? 23.510 28.019  -1.024  1.00 11.14 ? 125 ALA A CB  1 
ATOM   1001 N  N   . ASP A 1 127 ? 25.840 26.889  -2.855  1.00 10.80 ? 126 ASP A N   1 
ATOM   1002 C  CA  . ASP A 1 127 ? 26.241 26.044  -3.971  1.00 10.59 ? 126 ASP A CA  1 
ATOM   1003 C  C   . ASP A 1 127 ? 27.321 25.047  -3.568  1.00 8.93  ? 126 ASP A C   1 
ATOM   1004 O  O   . ASP A 1 127 ? 27.285 23.889  -3.977  1.00 10.49 ? 126 ASP A O   1 
ATOM   1005 C  CB  . ASP A 1 127 ? 26.710 26.906  -5.138  1.00 16.11 ? 126 ASP A CB  1 
ATOM   1006 C  CG  . ASP A 1 127 ? 25.582 27.735  -5.743  1.00 24.03 ? 126 ASP A CG  1 
ATOM   1007 O  OD1 . ASP A 1 127 ? 24.418 27.285  -5.725  1.00 19.13 ? 126 ASP A OD1 1 
ATOM   1008 O  OD2 . ASP A 1 127 ? 25.856 28.844  -6.226  1.00 26.52 ? 126 ASP A OD2 1 
ATOM   1009 N  N   . ALA A 1 128 ? 28.275 25.492  -2.754  1.00 8.39  ? 127 ALA A N   1 
ATOM   1010 C  CA  . ALA A 1 128 ? 29.356 24.613  -2.295  1.00 8.39  ? 127 ALA A CA  1 
ATOM   1011 C  C   . ALA A 1 128 ? 28.807 23.519  -1.373  1.00 8.76  ? 127 ALA A C   1 
ATOM   1012 O  O   . ALA A 1 128 ? 29.261 22.375  -1.423  1.00 9.07  ? 127 ALA A O   1 
ATOM   1013 C  CB  . ALA A 1 128 ? 30.429 25.421  -1.579  1.00 8.59  ? 127 ALA A CB  1 
ATOM   1014 N  N   . GLN A 1 129 ? 27.853 23.871  -0.509  1.00 8.09  ? 128 GLN A N   1 
ATOM   1015 C  CA  . GLN A 1 129 ? 27.275 22.881  0.385   1.00 8.11  ? 128 GLN A CA  1 
ATOM   1016 C  C   . GLN A 1 129 ? 26.462 21.858  -0.412  1.00 8.50  ? 128 GLN A C   1 
ATOM   1017 O  O   . GLN A 1 129 ? 26.450 20.671  -0.088  1.00 8.76  ? 128 GLN A O   1 
ATOM   1018 C  CB  . GLN A 1 129 ? 26.405 23.549  1.453   1.00 7.97  ? 128 GLN A CB  1 
ATOM   1019 C  CG  . GLN A 1 129 ? 25.795 22.540  2.429   1.00 7.62  ? 128 GLN A CG  1 
ATOM   1020 C  CD  . GLN A 1 129 ? 25.025 23.194  3.567   1.00 9.00  ? 128 GLN A CD  1 
ATOM   1021 O  OE1 . GLN A 1 129 ? 25.351 24.295  3.999   1.00 13.35 ? 128 GLN A OE1 1 
ATOM   1022 N  NE2 . GLN A 1 129 ? 24.014 22.498  4.070   1.00 12.69 ? 128 GLN A NE2 1 
ATOM   1023 N  N   . GLY A 1 130 ? 25.796 22.319  -1.469  1.00 8.76  ? 129 GLY A N   1 
ATOM   1024 C  CA  . GLY A 1 130 ? 25.018 21.421  -2.297  1.00 8.78  ? 129 GLY A CA  1 
ATOM   1025 C  C   . GLY A 1 130 ? 25.924 20.419  -2.992  1.00 9.24  ? 129 GLY A C   1 
ATOM   1026 O  O   . GLY A 1 130 ? 25.579 19.236  -3.135  1.00 9.55  ? 129 GLY A O   1 
ATOM   1027 N  N   . ALA A 1 131 ? 27.064 20.898  -3.477  1.00 9.04  ? 130 ALA A N   1 
ATOM   1028 C  CA  . ALA A 1 131 ? 28.026 20.026  -4.151  1.00 9.65  ? 130 ALA A CA  1 
ATOM   1029 C  C   . ALA A 1 131 ? 28.638 19.011  -3.165  1.00 9.41  ? 130 ALA A C   1 
ATOM   1030 O  O   . ALA A 1 131 ? 28.833 17.849  -3.508  1.00 10.14 ? 130 ALA A O   1 
ATOM   1031 C  CB  . ALA A 1 131 ? 29.120 20.863  -4.806  1.00 9.94  ? 130 ALA A CB  1 
ATOM   1032 N  N   . MET A 1 132 ? 28.955 19.453  -1.952  1.00 9.07  ? 131 MET A N   1 
ATOM   1033 C  CA  . MET A 1 132 ? 29.516 18.560  -0.924  1.00 9.60  ? 131 MET A CA  1 
ATOM   1034 C  C   . MET A 1 132 ? 28.460 17.513  -0.542  1.00 9.30  ? 131 MET A C   1 
ATOM   1035 O  O   . MET A 1 132 ? 28.756 16.327  -0.428  1.00 9.37  ? 131 MET A O   1 
ATOM   1036 C  CB  . MET A 1 132 ? 29.964 19.365  0.315   1.00 10.14 ? 131 MET A CB  1 
ATOM   1037 C  CG  . MET A 1 132 ? 30.626 18.538  1.444   1.00 11.41 ? 131 MET A CG  1 
ATOM   1038 S  SD  . MET A 1 132 ? 32.114 17.623  0.887   1.00 15.48 ? 131 MET A SD  1 
ATOM   1039 C  CE  . MET A 1 132 ? 33.312 18.844  0.963   1.00 13.44 ? 131 MET A CE  1 
ATOM   1040 N  N   . ASN A 1 133 ? 27.216 17.945  -0.374  1.00 9.64  ? 132 ASN A N   1 
ATOM   1041 C  CA  . ASN A 1 133 ? 26.156 17.000  -0.056  1.00 9.63  ? 132 ASN A CA  1 
ATOM   1042 C  C   . ASN A 1 133 ? 26.016 15.928  -1.161  1.00 10.16 ? 132 ASN A C   1 
ATOM   1043 O  O   . ASN A 1 133 ? 25.850 14.745  -0.868  1.00 10.58 ? 132 ASN A O   1 
ATOM   1044 C  CB  . ASN A 1 133 ? 24.814 17.707  0.139   1.00 9.81  ? 132 ASN A CB  1 
ATOM   1045 C  CG  . ASN A 1 133 ? 23.687 16.718  0.382   1.00 10.40 ? 132 ASN A CG  1 
ATOM   1046 O  OD1 . ASN A 1 133 ? 23.706 15.992  1.362   1.00 12.93 ? 132 ASN A OD1 1 
ATOM   1047 N  ND2 . ASN A 1 133 ? 22.737 16.648  -0.543  1.00 11.63 ? 132 ASN A ND2 1 
ATOM   1048 N  N   . LYS A 1 134 ? 26.066 16.353  -2.423  1.00 8.49  ? 133 LYS A N   1 
ATOM   1049 C  CA  . LYS A 1 134 ? 25.965 15.440  -3.566  1.00 9.93  ? 133 LYS A CA  1 
ATOM   1050 C  C   . LYS A 1 134 ? 27.126 14.429  -3.563  1.00 12.00 ? 133 LYS A C   1 
ATOM   1051 O  O   . LYS A 1 134 ? 26.935 13.240  -3.823  1.00 9.92  ? 133 LYS A O   1 
ATOM   1052 C  CB  . LYS A 1 134 ? 25.982 16.265  -4.852  1.00 8.71  ? 133 LYS A CB  1 
ATOM   1053 C  CG  . LYS A 1 134 ? 25.438 15.580  -6.078  1.00 21.83 ? 133 LYS A CG  1 
ATOM   1054 C  CD  . LYS A 1 134 ? 25.284 16.576  -7.225  1.00 25.88 ? 133 LYS A CD  1 
ATOM   1055 C  CE  . LYS A 1 134 ? 24.869 15.864  -8.499  1.00 50.65 ? 133 LYS A CE  1 
ATOM   1056 N  NZ  . LYS A 1 134 ? 24.796 16.766  -9.678  1.00 51.16 ? 133 LYS A NZ  1 
ATOM   1057 N  N   . ALA A 1 135 ? 28.327 14.902  -3.235  1.00 8.45  ? 134 ALA A N   1 
ATOM   1058 C  CA  . ALA A 1 135 ? 29.503 14.034  -3.208  1.00 8.48  ? 134 ALA A CA  1 
ATOM   1059 C  C   . ALA A 1 135 ? 29.389 13.010  -2.091  1.00 8.89  ? 134 ALA A C   1 
ATOM   1060 O  O   . ALA A 1 135 ? 29.733 11.840  -2.279  1.00 9.10  ? 134 ALA A O   1 
ATOM   1061 C  CB  . ALA A 1 135 ? 30.778 14.863  -3.056  1.00 8.24  ? 134 ALA A CB  1 
ATOM   1062 N  N   . LEU A 1 136 ? 28.864 13.429  -0.943  1.00 8.95  ? 135 LEU A N   1 
ATOM   1063 C  CA  . LEU A 1 136 ? 28.709 12.516  0.187   1.00 9.81  ? 135 LEU A CA  1 
ATOM   1064 C  C   . LEU A 1 136 ? 27.559 11.544  -0.068  1.00 9.95  ? 135 LEU A C   1 
ATOM   1065 O  O   . LEU A 1 136 ? 27.608 10.398  0.365   1.00 10.73 ? 135 LEU A O   1 
ATOM   1066 C  CB  . LEU A 1 136 ? 28.488 13.292  1.491   1.00 10.62 ? 135 LEU A CB  1 
ATOM   1067 C  CG  . LEU A 1 136 ? 29.701 14.126  1.934   1.00 11.14 ? 135 LEU A CG  1 
ATOM   1068 C  CD1 . LEU A 1 136 ? 29.360 14.933  3.188   1.00 10.79 ? 135 LEU A CD1 1 
ATOM   1069 C  CD2 . LEU A 1 136 ? 30.899 13.213  2.171   1.00 11.88 ? 135 LEU A CD2 1 
ATOM   1070 N  N   . GLU A 1 137 ? 26.526 11.995  -0.780  1.00 6.73  ? 136 GLU A N   1 
ATOM   1071 C  CA  . GLU A 1 137 ? 25.402 11.117  -1.108  1.00 6.01  ? 136 GLU A CA  1 
ATOM   1072 C  C   . GLU A 1 137 ? 25.884 10.042  -2.079  1.00 16.78 ? 136 GLU A C   1 
ATOM   1073 O  O   . GLU A 1 137 ? 25.450 8.889   -2.004  1.00 11.21 ? 136 GLU A O   1 
ATOM   1074 C  CB  . GLU A 1 137 ? 24.268 11.893  -1.764  1.00 9.27  ? 136 GLU A CB  1 
ATOM   1075 C  CG  . GLU A 1 137 ? 23.518 12.804  -0.815  1.00 24.35 ? 136 GLU A CG  1 
ATOM   1076 C  CD  . GLU A 1 137 ? 22.209 13.306  -1.403  1.00 49.44 ? 136 GLU A CD  1 
ATOM   1077 O  OE1 . GLU A 1 137 ? 21.977 13.091  -2.617  1.00 45.82 ? 136 GLU A OE1 1 
ATOM   1078 O  OE2 . GLU A 1 137 ? 21.410 13.908  -0.648  1.00 44.41 ? 136 GLU A OE2 1 
ATOM   1079 N  N   . LEU A 1 138 ? 26.756 10.434  -3.008  1.00 10.54 ? 137 LEU A N   1 
ATOM   1080 C  CA  . LEU A 1 138 ? 27.325 9.494   -3.986  1.00 11.01 ? 137 LEU A CA  1 
ATOM   1081 C  C   . LEU A 1 138 ? 28.151 8.462   -3.231  1.00 11.09 ? 137 LEU A C   1 
ATOM   1082 O  O   . LEU A 1 138 ? 28.067 7.264   -3.507  1.00 11.35 ? 137 LEU A O   1 
ATOM   1083 C  CB  . LEU A 1 138 ? 28.212 10.229  -4.990  1.00 11.94 ? 137 LEU A CB  1 
ATOM   1084 C  CG  . LEU A 1 138 ? 28.994 9.349   -5.967  1.00 12.42 ? 137 LEU A CG  1 
ATOM   1085 C  CD1 . LEU A 1 138 ? 28.035 8.596   -6.888  1.00 14.31 ? 137 LEU A CD1 1 
ATOM   1086 C  CD2 . LEU A 1 138 ? 29.942 10.212  -6.783  1.00 13.30 ? 137 LEU A CD2 1 
ATOM   1087 N  N   . PHE A 1 139 ? 28.945 8.933   -2.273  1.00 10.85 ? 138 PHE A N   1 
ATOM   1088 C  CA  . PHE A 1 139 ? 29.767 8.049   -1.438  1.00 11.17 ? 138 PHE A CA  1 
ATOM   1089 C  C   . PHE A 1 139 ? 28.878 7.040   -0.683  1.00 10.87 ? 138 PHE A C   1 
ATOM   1090 O  O   . PHE A 1 139 ? 29.132 5.835   -0.708  1.00 10.35 ? 138 PHE A O   1 
ATOM   1091 C  CB  . PHE A 1 139 ? 30.594 8.894   -0.461  1.00 12.24 ? 138 PHE A CB  1 
ATOM   1092 C  CG  . PHE A 1 139 ? 31.193 8.115   0.672   1.00 13.97 ? 138 PHE A CG  1 
ATOM   1093 C  CD1 . PHE A 1 139 ? 32.206 7.198   0.449   1.00 14.07 ? 138 PHE A CD1 1 
ATOM   1094 C  CD2 . PHE A 1 139 ? 30.742 8.310   1.973   1.00 14.33 ? 138 PHE A CD2 1 
ATOM   1095 C  CE1 . PHE A 1 139 ? 32.759 6.488   1.504   1.00 15.24 ? 138 PHE A CE1 1 
ATOM   1096 C  CE2 . PHE A 1 139 ? 31.292 7.601   3.033   1.00 15.20 ? 138 PHE A CE2 1 
ATOM   1097 C  CZ  . PHE A 1 139 ? 32.304 6.688   2.797   1.00 14.79 ? 138 PHE A CZ  1 
ATOM   1098 N  N   . ARG A 1 140 ? 27.821 7.533   -0.040  1.00 10.75 ? 139 ARG A N   1 
ATOM   1099 C  CA  . ARG A 1 140 ? 26.907 6.663   0.691   1.00 10.95 ? 139 ARG A CA  1 
ATOM   1100 C  C   . ARG A 1 140 ? 26.168 5.672   -0.196  1.00 10.97 ? 139 ARG A C   1 
ATOM   1101 O  O   . ARG A 1 140 ? 25.911 4.546   0.216   1.00 11.58 ? 139 ARG A O   1 
ATOM   1102 C  CB  . ARG A 1 140 ? 25.895 7.477   1.488   1.00 10.03 ? 139 ARG A CB  1 
ATOM   1103 C  CG  . ARG A 1 140 ? 26.542 8.326   2.563   1.00 9.95  ? 139 ARG A CG  1 
ATOM   1104 C  CD  . ARG A 1 140 ? 25.537 8.698   3.633   1.00 9.00  ? 139 ARG A CD  1 
ATOM   1105 N  NE  . ARG A 1 140 ? 24.374 9.395   3.094   1.00 14.10 ? 139 ARG A NE  1 
ATOM   1106 C  CZ  . ARG A 1 140 ? 24.331 10.698  2.830   1.00 20.09 ? 139 ARG A CZ  1 
ATOM   1107 N  NH1 . ARG A 1 140 ? 25.397 11.459  3.045   1.00 19.22 ? 139 ARG A NH1 1 
ATOM   1108 N  NH2 . ARG A 1 140 ? 23.217 11.239  2.352   1.00 13.02 ? 139 ARG A NH2 1 
ATOM   1109 N  N   . LYS A 1 141 ? 25.794 6.103   -1.393  1.00 10.58 ? 140 LYS A N   1 
ATOM   1110 C  CA  . LYS A 1 141 ? 25.085 5.238   -2.334  1.00 14.91 ? 140 LYS A CA  1 
ATOM   1111 C  C   . LYS A 1 141 ? 25.960 4.072   -2.796  1.00 16.54 ? 140 LYS A C   1 
ATOM   1112 O  O   . LYS A 1 141 ? 25.508 2.920   -2.851  1.00 13.39 ? 140 LYS A O   1 
ATOM   1113 C  CB  . LYS A 1 141 ? 24.629 6.037   -3.564  1.00 23.66 ? 140 LYS A CB  1 
ATOM   1114 C  CG  . LYS A 1 141 ? 23.809 5.214   -4.555  1.00 38.30 ? 140 LYS A CG  1 
ATOM   1115 C  CD  . LYS A 1 141 ? 23.378 6.015   -5.777  1.00 65.95 ? 140 LYS A CD  1 
ATOM   1116 C  CE  . LYS A 1 141 ? 24.414 5.956   -6.891  1.00 67.66 ? 140 LYS A CE  1 
ATOM   1117 N  NZ  . LYS A 1 141 ? 25.721 6.540   -6.486  1.00 78.69 ? 140 LYS A NZ  1 
ATOM   1118 N  N   . ASP A 1 142 ? 27.209 4.369   -3.144  1.00 11.41 ? 141 ASP A N   1 
ATOM   1119 C  CA  . ASP A 1 142 ? 28.121 3.330   -3.596  1.00 12.21 ? 141 ASP A CA  1 
ATOM   1120 C  C   . ASP A 1 142 ? 28.523 2.404   -2.455  1.00 15.59 ? 141 ASP A C   1 
ATOM   1121 O  O   . ASP A 1 142 ? 28.690 1.205   -2.654  1.00 13.95 ? 141 ASP A O   1 
ATOM   1122 C  CB  . ASP A 1 142 ? 29.342 3.942   -4.275  1.00 11.10 ? 141 ASP A CB  1 
ATOM   1123 C  CG  . ASP A 1 142 ? 29.012 4.537   -5.625  1.00 18.50 ? 141 ASP A CG  1 
ATOM   1124 O  OD1 . ASP A 1 142 ? 27.901 4.285   -6.137  1.00 17.64 ? 141 ASP A OD1 1 
ATOM   1125 O  OD2 . ASP A 1 142 ? 29.858 5.267   -6.178  1.00 19.12 ? 141 ASP A OD2 1 
ATOM   1126 N  N   . ILE A 1 143 ? 28.661 2.953   -1.256  1.00 16.17 ? 142 ILE A N   1 
ATOM   1127 C  CA  . ILE A 1 143 ? 29.003 2.133   -0.099  1.00 16.87 ? 142 ILE A CA  1 
ATOM   1128 C  C   . ILE A 1 143 ? 27.828 1.207   0.228   1.00 16.30 ? 142 ILE A C   1 
ATOM   1129 O  O   . ILE A 1 143 ? 28.035 0.037   0.563   1.00 16.25 ? 142 ILE A O   1 
ATOM   1130 C  CB  . ILE A 1 143 ? 29.337 3.007   1.134   1.00 18.09 ? 142 ILE A CB  1 
ATOM   1131 C  CG1 . ILE A 1 143 ? 30.802 3.402   1.095   1.00 19.51 ? 142 ILE A CG1 1 
ATOM   1132 C  CG2 . ILE A 1 143 ? 29.037 2.265   2.432   1.00 19.83 ? 142 ILE A CG2 1 
ATOM   1133 C  CD1 . ILE A 1 143 ? 31.730 2.254   1.434   1.00 21.45 ? 142 ILE A CD1 1 
ATOM   1134 N  N   . ALA A 1 144 ? 26.604 1.726   0.138   1.00 15.33 ? 143 ALA A N   1 
ATOM   1135 C  CA  . ALA A 1 144 ? 25.417 0.915   0.434   1.00 15.31 ? 143 ALA A CA  1 
ATOM   1136 C  C   . ALA A 1 144 ? 25.327 -0.264  -0.532  1.00 15.15 ? 143 ALA A C   1 
ATOM   1137 O  O   . ALA A 1 144 ? 25.004 -1.375  -0.120  1.00 15.20 ? 143 ALA A O   1 
ATOM   1138 C  CB  . ALA A 1 144 ? 24.148 1.759   0.351   1.00 15.88 ? 143 ALA A CB  1 
ATOM   1139 N  N   . ALA A 1 145 ? 25.654 -0.018  -1.802  1.00 14.89 ? 144 ALA A N   1 
ATOM   1140 C  CA  . ALA A 1 145 ? 25.629 -1.048  -2.836  1.00 14.96 ? 144 ALA A CA  1 
ATOM   1141 C  C   . ALA A 1 145 ? 26.637 -2.150  -2.522  1.00 15.39 ? 144 ALA A C   1 
ATOM   1142 O  O   . ALA A 1 145 ? 26.351 -3.328  -2.719  1.00 15.94 ? 144 ALA A O   1 
ATOM   1143 C  CB  . ALA A 1 145 ? 25.936 -0.437  -4.191  1.00 14.69 ? 144 ALA A CB  1 
ATOM   1144 N  N   . LYS A 1 146 ? 27.806 -1.759  -2.015  1.00 13.64 ? 145 LYS A N   1 
ATOM   1145 C  CA  . LYS A 1 146 ? 28.870 -2.705  -1.666  1.00 12.78 ? 145 LYS A CA  1 
ATOM   1146 C  C   . LYS A 1 146 ? 28.470 -3.505  -0.452  1.00 11.18 ? 145 LYS A C   1 
ATOM   1147 O  O   . LYS A 1 146 ? 28.752 -4.698  -0.374  1.00 16.11 ? 145 LYS A O   1 
ATOM   1148 C  CB  . LYS A 1 146 ? 30.183 -1.968  -1.383  1.00 11.97 ? 145 LYS A CB  1 
ATOM   1149 C  CG  . LYS A 1 146 ? 30.942 -1.512  -2.618  1.00 25.52 ? 145 LYS A CG  1 
ATOM   1150 C  CD  . LYS A 1 146 ? 29.991 -1.135  -3.738  1.00 62.02 ? 145 LYS A CD  1 
ATOM   1151 C  CE  . LYS A 1 146 ? 30.529 -0.033  -4.613  1.00 54.68 ? 145 LYS A CE  1 
ATOM   1152 N  NZ  . LYS A 1 146 ? 29.441 0.506   -5.451  1.00 21.91 ? 145 LYS A NZ  1 
ATOM   1153 N  N   . TYR A 1 147 ? 27.827 -2.840  0.503   1.00 13.94 ? 146 TYR A N   1 
ATOM   1154 C  CA  . TYR A 1 147 ? 27.357 -3.498  1.721   1.00 14.36 ? 146 TYR A CA  1 
ATOM   1155 C  C   . TYR A 1 147 ? 26.490 -4.689  1.319   1.00 14.40 ? 146 TYR A C   1 
ATOM   1156 O  O   . TYR A 1 147 ? 26.687 -5.806  1.807   1.00 15.18 ? 146 TYR A O   1 
ATOM   1157 C  CB  . TYR A 1 147 ? 26.505 -2.535  2.552   1.00 15.01 ? 146 TYR A CB  1 
ATOM   1158 C  CG  . TYR A 1 147 ? 27.233 -1.771  3.637   1.00 15.73 ? 146 TYR A CG  1 
ATOM   1159 C  CD1 . TYR A 1 147 ? 28.619 -1.581  3.605   1.00 15.32 ? 146 TYR A CD1 1 
ATOM   1160 C  CD2 . TYR A 1 147 ? 26.523 -1.242  4.711   1.00 16.48 ? 146 TYR A CD2 1 
ATOM   1161 C  CE1 . TYR A 1 147 ? 29.274 -0.877  4.629   1.00 15.63 ? 146 TYR A CE1 1 
ATOM   1162 C  CE2 . TYR A 1 147 ? 27.163 -0.542  5.730   1.00 16.64 ? 146 TYR A CE2 1 
ATOM   1163 C  CZ  . TYR A 1 147 ? 28.534 -0.363  5.688   1.00 16.33 ? 146 TYR A CZ  1 
ATOM   1164 O  OH  . TYR A 1 147 ? 29.130 0.330   6.726   1.00 16.15 ? 146 TYR A OH  1 
ATOM   1165 N  N   . LYS A 1 148 ? 25.547 -4.438  0.415   1.00 13.64 ? 147 LYS A N   1 
ATOM   1166 C  CA  . LYS A 1 148 ? 24.632 -5.465  -0.085  1.00 17.22 ? 147 LYS A CA  1 
ATOM   1167 C  C   . LYS A 1 148 ? 25.367 -6.639  -0.733  1.00 16.96 ? 147 LYS A C   1 
ATOM   1168 O  O   . LYS A 1 148 ? 25.038 -7.798  -0.474  1.00 16.14 ? 147 LYS A O   1 
ATOM   1169 C  CB  . LYS A 1 148 ? 23.629 -4.856  -1.070  1.00 18.24 ? 147 LYS A CB  1 
ATOM   1170 C  CG  . LYS A 1 148 ? 22.622 -5.862  -1.601  1.00 40.13 ? 147 LYS A CG  1 
ATOM   1171 C  CD  . LYS A 1 148 ? 21.596 -5.222  -2.524  1.00 59.10 ? 147 LYS A CD  1 
ATOM   1172 C  CE  . LYS A 1 148 ? 20.771 -6.284  -3.255  1.00 68.72 ? 147 LYS A CE  1 
ATOM   1173 N  NZ  . LYS A 1 148 ? 20.154 -7.292  -2.336  1.00 66.70 ? 147 LYS A NZ  1 
ATOM   1174 N  N   . GLU A 1 149 ? 26.371 -6.342  -1.557  1.00 13.40 ? 148 GLU A N   1 
ATOM   1175 C  CA  . GLU A 1 149 ? 27.161 -7.392  -2.212  1.00 16.09 ? 148 GLU A CA  1 
ATOM   1176 C  C   . GLU A 1 149 ? 27.928 -8.224  -1.192  1.00 16.28 ? 148 GLU A C   1 
ATOM   1177 O  O   . GLU A 1 149 ? 28.209 -9.401  -1.427  1.00 15.99 ? 148 GLU A O   1 
ATOM   1178 C  CB  . GLU A 1 149 ? 28.165 -6.787  -3.191  1.00 12.33 ? 148 GLU A CB  1 
ATOM   1179 C  CG  . GLU A 1 149 ? 27.525 -6.095  -4.375  1.00 29.74 ? 148 GLU A CG  1 
ATOM   1180 C  CD  . GLU A 1 149 ? 28.537 -5.376  -5.246  1.00 38.56 ? 148 GLU A CD  1 
ATOM   1181 O  OE1 . GLU A 1 149 ? 29.668 -5.885  -5.394  1.00 41.47 ? 148 GLU A OE1 1 
ATOM   1182 O  OE2 . GLU A 1 149 ? 28.201 -4.297  -5.781  1.00 55.89 ? 148 GLU A OE2 1 
ATOM   1183 N  N   . LEU A 1 150 ? 28.287 -7.597  -0.077  1.00 18.46 ? 149 LEU A N   1 
ATOM   1184 C  CA  . LEU A 1 150 ? 29.039 -8.263  0.971   1.00 19.99 ? 149 LEU A CA  1 
ATOM   1185 C  C   . LEU A 1 150 ? 28.157 -9.039  1.950   1.00 21.04 ? 149 LEU A C   1 
ATOM   1186 O  O   . LEU A 1 150 ? 28.671 -9.745  2.818   1.00 21.25 ? 149 LEU A O   1 
ATOM   1187 C  CB  . LEU A 1 150 ? 29.922 -7.253  1.722   1.00 19.62 ? 149 LEU A CB  1 
ATOM   1188 C  CG  . LEU A 1 150 ? 31.019 -6.537  0.915   1.00 19.69 ? 149 LEU A CG  1 
ATOM   1189 C  CD1 . LEU A 1 150 ? 31.667 -5.457  1.768   1.00 19.35 ? 149 LEU A CD1 1 
ATOM   1190 C  CD2 . LEU A 1 150 ? 32.071 -7.516  0.423   1.00 19.37 ? 149 LEU A CD2 1 
ATOM   1191 N  N   . GLY A 1 151 ? 26.840 -8.893  1.824   1.00 22.06 ? 150 GLY A N   1 
ATOM   1192 C  CA  . GLY A 1 151 ? 25.928 -9.627  2.685   1.00 24.39 ? 150 GLY A CA  1 
ATOM   1193 C  C   . GLY A 1 151 ? 25.458 -8.914  3.931   1.00 26.41 ? 150 GLY A C   1 
ATOM   1194 O  O   . GLY A 1 151 ? 24.952 -9.540  4.862   1.00 26.03 ? 150 GLY A O   1 
ATOM   1195 N  N   . TYR A 1 152 ? 25.577 -7.594  3.926   1.00 28.52 ? 151 TYR A N   1 
ATOM   1196 C  CA  . TYR A 1 152 ? 25.182 -6.783  5.061   1.00 31.04 ? 151 TYR A CA  1 
ATOM   1197 C  C   . TYR A 1 152 ? 24.092 -5.767  4.724   1.00 32.72 ? 151 TYR A C   1 
ATOM   1198 O  O   . TYR A 1 152 ? 22.961 -5.891  5.185   1.00 33.29 ? 151 TYR A O   1 
ATOM   1199 C  CB  . TYR A 1 152 ? 26.421 -6.073  5.616   1.00 31.20 ? 151 TYR A CB  1 
ATOM   1200 C  CG  . TYR A 1 152 ? 26.163 -5.166  6.795   1.00 32.08 ? 151 TYR A CG  1 
ATOM   1201 C  CD1 . TYR A 1 152 ? 25.875 -5.682  8.055   1.00 32.38 ? 151 TYR A CD1 1 
ATOM   1202 C  CD2 . TYR A 1 152 ? 26.232 -3.789  6.654   1.00 32.59 ? 151 TYR A CD2 1 
ATOM   1203 C  CE1 . TYR A 1 152 ? 25.662 -4.838  9.144   1.00 32.51 ? 151 TYR A CE1 1 
ATOM   1204 C  CE2 . TYR A 1 152 ? 26.021 -2.941  7.733   1.00 32.87 ? 151 TYR A CE2 1 
ATOM   1205 C  CZ  . TYR A 1 152 ? 25.737 -3.469  8.969   1.00 32.71 ? 151 TYR A CZ  1 
ATOM   1206 O  OH  . TYR A 1 152 ? 25.525 -2.614  10.021  1.00 33.05 ? 151 TYR A OH  1 
ATOM   1207 N  N   . GLN A 1 153 ? 24.446 -4.753  3.940   1.00 34.79 ? 152 GLN A N   1 
ATOM   1208 C  CA  . GLN A 1 153 ? 23.530 -3.665  3.569   1.00 37.20 ? 152 GLN A CA  1 
ATOM   1209 C  C   . GLN A 1 153 ? 22.709 -3.098  4.737   1.00 38.24 ? 152 GLN A C   1 
ATOM   1210 O  O   . GLN A 1 153 ? 21.671 -2.466  4.532   1.00 38.67 ? 152 GLN A O   1 
ATOM   1211 C  CB  . GLN A 1 153 ? 22.597 -4.059  2.422   1.00 38.53 ? 152 GLN A CB  1 
ATOM   1212 C  CG  . GLN A 1 153 ? 22.461 -2.974  1.348   1.00 47.32 ? 152 GLN A CG  1 
ATOM   1213 C  CD  . GLN A 1 153 ? 22.386 -1.558  1.909   1.00 53.70 ? 152 GLN A CD  1 
ATOM   1214 O  OE1 . GLN A 1 153 ? 23.408 -0.957  2.246   1.00 62.61 ? 152 GLN A OE1 1 
ATOM   1215 N  NE2 . GLN A 1 153 ? 21.174 -1.020  2.010   1.00 72.20 ? 152 GLN A NE2 1 
ATOM   1216 N  N   . GLY A 1 154 ? 23.174 -3.342  5.957   1.00 39.00 ? 153 GLY A N   1 
ATOM   1217 C  CA  . GLY A 1 154 ? 22.479 -2.839  7.122   1.00 40.00 ? 153 GLY A CA  1 
ATOM   1218 C  C   . GLY A 1 154 ? 22.703 -1.350  7.301   1.00 40.37 ? 153 GLY A C   1 
ATOM   1219 O  O   . GLY A 1 154 ? 22.020 -0.745  8.154   1.00 40.86 ? 153 GLY A O   1 
ATOM   1220 O  OXT . GLY A 1 154 ? 23.555 -0.774  6.580   1.00 40.85 ? 153 GLY A OXT 1 
HETATM 1221 S  S   . SO4 B 2 .   ? 30.496 18.509  28.824  1.00 46.32 ? 157 SO4 A S   1 
HETATM 1222 O  O1  . SO4 B 2 .   ? 30.458 19.899  28.521  1.00 46.43 ? 157 SO4 A O1  1 
HETATM 1223 O  O2  . SO4 B 2 .   ? 30.763 17.789  27.638  1.00 45.67 ? 157 SO4 A O2  1 
HETATM 1224 O  O3  . SO4 B 2 .   ? 29.246 18.025  29.362  1.00 46.00 ? 157 SO4 A O3  1 
HETATM 1225 O  O4  . SO4 B 2 .   ? 31.503 18.364  29.781  1.00 46.24 ? 157 SO4 A O4  1 
HETATM 1226 C  CHA . HEM C 3 .   ? 38.084 2.453   11.203  1.00 12.15 ? 155 HEM A CHA 1 
HETATM 1227 C  CHB . HEM C 3 .   ? 37.349 5.339   7.488   1.00 10.57 ? 155 HEM A CHB 1 
HETATM 1228 C  CHC . HEM C 3 .   ? 32.904 6.170   9.172   1.00 11.11 ? 155 HEM A CHC 1 
HETATM 1229 C  CHD . HEM C 3 .   ? 33.710 3.338   12.932  1.00 11.90 ? 155 HEM A CHD 1 
HETATM 1230 C  C1A . HEM C 3 .   ? 38.253 3.145   10.042  1.00 11.35 ? 155 HEM A C1A 1 
HETATM 1231 C  C2A . HEM C 3 .   ? 39.498 3.163   9.301   1.00 11.44 ? 155 HEM A C2A 1 
HETATM 1232 C  C3A . HEM C 3 .   ? 39.252 3.984   8.253   1.00 10.63 ? 155 HEM A C3A 1 
HETATM 1233 C  C4A . HEM C 3 .   ? 37.923 4.467   8.377   1.00 10.48 ? 155 HEM A C4A 1 
HETATM 1234 C  CMA . HEM C 3 .   ? 40.219 4.239   7.078   1.00 10.02 ? 155 HEM A CMA 1 
HETATM 1235 C  CAA . HEM C 3 .   ? 40.781 2.303   9.305   1.00 13.24 ? 155 HEM A CAA 1 
HETATM 1236 C  CBA . HEM C 3 .   ? 40.856 0.850   8.860   1.00 15.50 ? 155 HEM A CBA 1 
HETATM 1237 C  CGA . HEM C 3 .   ? 39.506 0.169   8.798   1.00 16.95 ? 155 HEM A CGA 1 
HETATM 1238 O  O1A . HEM C 3 .   ? 39.102 -0.425  9.819   1.00 18.61 ? 155 HEM A O1A 1 
HETATM 1239 O  O2A . HEM C 3 .   ? 38.852 0.225   7.733   1.00 18.06 ? 155 HEM A O2A 1 
HETATM 1240 C  C1B . HEM C 3 .   ? 36.047 5.809   7.593   1.00 10.58 ? 155 HEM A C1B 1 
HETATM 1241 C  C2B . HEM C 3 .   ? 35.436 6.764   6.681   1.00 10.41 ? 155 HEM A C2B 1 
HETATM 1242 C  C3B . HEM C 3 .   ? 34.178 7.007   7.167   1.00 10.83 ? 155 HEM A C3B 1 
HETATM 1243 C  C4B . HEM C 3 .   ? 34.035 6.172   8.359   1.00 10.71 ? 155 HEM A C4B 1 
HETATM 1244 C  CMB . HEM C 3 .   ? 36.031 7.334   5.371   1.00 9.85  ? 155 HEM A CMB 1 
HETATM 1245 C  CAB . HEM C 3 .   ? 33.216 7.991   6.823   1.00 11.28 ? 155 HEM A CAB 1 
HETATM 1246 C  CBB . HEM C 3 .   ? 33.239 9.089   5.937   1.00 12.26 ? 155 HEM A CBB 1 
HETATM 1247 C  C1C . HEM C 3 .   ? 32.727 5.463   10.352  1.00 10.60 ? 155 HEM A C1C 1 
HETATM 1248 C  C2C . HEM C 3 .   ? 31.588 5.616   11.240  1.00 10.77 ? 155 HEM A C2C 1 
HETATM 1249 C  C3C . HEM C 3 .   ? 31.836 4.815   12.309  1.00 11.44 ? 155 HEM A C3C 1 
HETATM 1250 C  C4C . HEM C 3 .   ? 33.094 4.200   12.059  1.00 11.10 ? 155 HEM A C4C 1 
HETATM 1251 C  CMC . HEM C 3 .   ? 30.394 6.567   11.017  1.00 10.73 ? 155 HEM A CMC 1 
HETATM 1252 C  CAC . HEM C 3 .   ? 31.146 4.632   13.544  1.00 12.26 ? 155 HEM A CAC 1 
HETATM 1253 C  CBC . HEM C 3 .   ? 29.977 5.269   14.051  1.00 13.23 ? 155 HEM A CBC 1 
HETATM 1254 C  C1D . HEM C 3 .   ? 34.973 2.797   12.754  1.00 12.59 ? 155 HEM A C1D 1 
HETATM 1255 C  C2D . HEM C 3 .   ? 35.625 1.961   13.741  1.00 13.55 ? 155 HEM A C2D 1 
HETATM 1256 C  C3D . HEM C 3 .   ? 36.844 1.764   13.242  1.00 14.50 ? 155 HEM A C3D 1 
HETATM 1257 C  C4D . HEM C 3 .   ? 36.945 2.429   11.972  1.00 13.25 ? 155 HEM A C4D 1 
HETATM 1258 C  CMD . HEM C 3 .   ? 35.021 1.358   14.998  1.00 13.20 ? 155 HEM A CMD 1 
HETATM 1259 C  CAD . HEM C 3 .   ? 38.057 1.152   13.864  1.00 17.74 ? 155 HEM A CAD 1 
HETATM 1260 C  CBD . HEM C 3 .   ? 38.571 1.921   15.060  1.00 22.63 ? 155 HEM A CBD 1 
HETATM 1261 C  CGD . HEM C 3 .   ? 39.919 1.414   15.491  1.00 24.88 ? 155 HEM A CGD 1 
HETATM 1262 O  O1D . HEM C 3 .   ? 40.022 0.869   16.612  1.00 27.95 ? 155 HEM A O1D 1 
HETATM 1263 O  O2D . HEM C 3 .   ? 40.875 1.547   14.692  1.00 28.34 ? 155 HEM A O2D 1 
HETATM 1264 N  NA  . HEM C 3 .   ? 37.298 3.940   9.488   1.00 10.03 ? 155 HEM A NA  1 
HETATM 1265 N  NB  . HEM C 3 .   ? 35.178 5.440   8.621   1.00 10.26 ? 155 HEM A NB  1 
HETATM 1266 N  NC  . HEM C 3 .   ? 33.637 4.608   10.860  1.00 11.11 ? 155 HEM A NC  1 
HETATM 1267 N  ND  . HEM C 3 .   ? 35.802 3.057   11.670  1.00 12.11 ? 155 HEM A ND  1 
HETATM 1268 FE FE  . HEM C 3 .   ? 35.478 4.222   10.130  1.00 10.59 ? 155 HEM A FE  1 
HETATM 1269 O  O   . HOH D 4 .   ? 36.144 5.754   11.403  1.00 15.54 ? 156 HOH A O   1 
HETATM 1270 O  O   . HOH D 4 .   ? 35.809 -2.569  15.416  0.45 9.86  ? 201 HOH A O   1 
HETATM 1271 O  O   . HOH D 4 .   ? 32.720 19.906  17.089  0.86 15.72 ? 202 HOH A O   1 
HETATM 1272 O  O   . HOH D 4 .   ? 26.078 14.335  13.232  0.90 24.12 ? 203 HOH A O   1 
HETATM 1273 O  O   . HOH D 4 .   ? 22.302 7.520   2.561   1.00 27.39 ? 204 HOH A O   1 
HETATM 1274 O  O   . HOH D 4 .   ? 30.882 6.728   -8.735  0.86 35.08 ? 205 HOH A O   1 
HETATM 1275 O  O   . HOH D 4 .   ? 24.417 30.291  6.826   0.68 25.29 ? 206 HOH A O   1 
HETATM 1276 O  O   . HOH D 4 .   ? 25.005 14.317  2.905   1.00 25.78 ? 207 HOH A O   1 
HETATM 1277 O  O   . HOH D 4 .   ? 21.980 13.814  1.988   0.74 23.77 ? 208 HOH A O   1 
HETATM 1278 O  O   . HOH D 4 .   ? 29.872 8.940   35.500  1.00 23.82 ? 209 HOH A O   1 
HETATM 1279 O  O   . HOH D 4 .   ? 30.407 11.708  35.811  1.00 16.41 ? 210 HOH A O   1 
HETATM 1280 O  O   . HOH D 4 .   ? 31.800 13.157  -12.133 1.00 16.61 ? 211 HOH A O   1 
HETATM 1281 O  O   . HOH D 4 .   ? 34.534 13.101  33.334  1.00 14.53 ? 212 HOH A O   1 
HETATM 1282 O  O   . HOH D 4 .   ? 35.696 30.766  4.647   0.78 17.31 ? 213 HOH A O   1 
HETATM 1283 O  O   . HOH D 4 .   ? 37.687 28.928  4.315   0.86 7.58  ? 214 HOH A O   1 
HETATM 1284 O  O   . HOH D 4 .   ? 38.820 28.939  7.913   0.98 12.46 ? 215 HOH A O   1 
HETATM 1285 O  O   . HOH D 4 .   ? 35.289 33.294  5.305   0.38 4.14  ? 216 HOH A O   1 
HETATM 1286 O  O   . HOH D 4 .   ? 45.089 12.815  -0.705  0.53 18.34 ? 217 HOH A O   1 
HETATM 1287 O  O   . HOH D 4 .   ? 22.099 26.458  -4.278  0.53 24.02 ? 218 HOH A O   1 
HETATM 1288 O  O   . HOH D 4 .   ? 34.105 25.790  -2.181  0.87 15.49 ? 219 HOH A O   1 
HETATM 1289 O  O   . HOH D 4 .   ? 43.386 5.547   13.683  0.89 30.33 ? 220 HOH A O   1 
HETATM 1290 O  O   . HOH D 4 .   ? 35.357 15.530  -13.815 1.00 32.50 ? 221 HOH A O   1 
HETATM 1291 O  O   . HOH D 4 .   ? 34.766 10.228  -5.348  1.00 10.94 ? 222 HOH A O   1 
HETATM 1292 O  O   . HOH D 4 .   ? 43.614 11.103  -6.806  0.81 40.08 ? 223 HOH A O   1 
HETATM 1293 O  O   . HOH D 4 .   ? 41.482 19.372  -2.355  0.62 15.76 ? 224 HOH A O   1 
HETATM 1294 O  O   . HOH D 4 .   ? 28.741 28.469  -2.840  0.75 18.19 ? 225 HOH A O   1 
HETATM 1295 O  O   . HOH D 4 .   ? 36.996 2.363   26.338  0.67 20.27 ? 226 HOH A O   1 
HETATM 1296 O  O   . HOH D 4 .   ? 37.279 29.652  10.915  0.90 17.03 ? 227 HOH A O   1 
HETATM 1297 O  O   . HOH D 4 .   ? 48.962 23.633  7.839   0.62 7.65  ? 228 HOH A O   1 
HETATM 1298 O  O   . HOH D 4 .   ? 24.789 31.130  -0.305  0.51 27.16 ? 229 HOH A O   1 
HETATM 1299 O  O   . HOH D 4 .   ? 47.146 20.109  12.013  0.85 26.81 ? 230 HOH A O   1 
HETATM 1300 O  O   . HOH D 4 .   ? 41.534 14.428  14.201  0.50 15.77 ? 231 HOH A O   1 
HETATM 1301 O  O   . HOH D 4 .   ? 25.441 17.145  13.295  0.85 30.70 ? 232 HOH A O   1 
HETATM 1302 O  O   . HOH D 4 .   ? 27.341 6.672   23.985  0.47 15.52 ? 233 HOH A O   1 
HETATM 1303 O  O   . HOH D 4 .   ? 36.084 -0.402  17.941  0.88 36.10 ? 234 HOH A O   1 
HETATM 1304 O  O   . HOH D 4 .   ? 32.699 -1.501  16.265  0.32 6.19  ? 235 HOH A O   1 
HETATM 1305 O  O   . HOH D 4 .   ? 43.108 6.708   6.390   0.35 2.00  ? 236 HOH A O   1 
HETATM 1306 O  O   . HOH D 4 .   ? 26.036 30.032  -3.403  0.97 34.00 ? 237 HOH A O   1 
HETATM 1307 O  O   . HOH D 4 .   ? 43.598 12.324  1.667   0.94 23.46 ? 238 HOH A O   1 
HETATM 1308 O  O   . HOH D 4 .   ? 23.248 31.799  4.749   0.90 26.50 ? 239 HOH A O   1 
HETATM 1309 O  O   . HOH D 4 .   ? 34.672 29.936  12.196  0.71 23.07 ? 240 HOH A O   1 
HETATM 1310 O  O   . HOH D 4 .   ? 42.690 14.618  3.419   1.00 43.46 ? 241 HOH A O   1 
HETATM 1311 O  O   . HOH D 4 .   ? 42.951 9.843   -4.248  0.90 17.12 ? 242 HOH A O   1 
HETATM 1312 O  O   . HOH D 4 .   ? 40.436 6.034   0.917   0.41 2.58  ? 243 HOH A O   1 
HETATM 1313 O  O   . HOH D 4 .   ? 39.764 10.505  -10.885 0.99 34.12 ? 244 HOH A O   1 
HETATM 1314 O  O   . HOH D 4 .   ? 40.209 3.848   -7.625  1.00 49.98 ? 245 HOH A O   1 
HETATM 1315 O  O   . HOH D 4 .   ? 39.819 3.142   1.253   0.90 30.80 ? 246 HOH A O   1 
HETATM 1316 O  O   . HOH D 4 .   ? 40.703 -2.418  -3.864  0.27 4.80  ? 247 HOH A O   1 
HETATM 1317 O  O   . HOH D 4 .   ? 27.335 25.144  11.292  1.00 30.32 ? 248 HOH A O   1 
HETATM 1318 O  O   . HOH D 4 .   ? 31.020 30.610  11.394  0.80 32.55 ? 249 HOH A O   1 
HETATM 1319 O  O   . HOH D 4 .   ? 21.046 2.065   8.757   0.73 22.07 ? 250 HOH A O   1 
HETATM 1320 O  O   . HOH D 4 .   ? 31.855 3.438   -7.885  0.35 23.02 ? 251 HOH A O   1 
HETATM 1321 O  O   . HOH D 4 .   ? 33.593 28.418  -2.964  0.98 37.30 ? 252 HOH A O   1 
HETATM 1322 O  O   . HOH D 4 .   ? 27.412 -10.611 -3.947  0.37 7.11  ? 253 HOH A O   1 
HETATM 1323 O  O   . HOH D 4 .   ? 24.483 -4.300  -4.623  0.60 20.88 ? 254 HOH A O   1 
HETATM 1324 O  O   . HOH D 4 .   ? 26.180 22.991  -6.418  0.98 26.54 ? 255 HOH A O   1 
HETATM 1325 O  O   . HOH D 4 .   ? 31.820 21.765  -1.090  0.65 20.62 ? 256 HOH A O   1 
HETATM 1326 O  O   . HOH D 4 .   ? 44.080 26.514  -1.006  1.00 40.34 ? 257 HOH A O   1 
HETATM 1327 O  O   . HOH D 4 .   ? 40.595 12.222  27.663  0.48 10.14 ? 258 HOH A O   1 
HETATM 1328 O  O   . HOH D 4 .   ? 47.385 24.358  10.900  0.82 38.78 ? 259 HOH A O   1 
HETATM 1329 O  O   . HOH D 4 .   ? 44.884 21.383  14.998  0.73 19.71 ? 260 HOH A O   1 
HETATM 1330 O  O   . HOH D 4 .   ? 39.663 26.337  9.912   1.00 15.58 ? 261 HOH A O   1 
HETATM 1331 O  O   . HOH D 4 .   ? 28.039 30.216  4.506   0.84 31.49 ? 262 HOH A O   1 
HETATM 1332 O  O   . HOH D 4 .   ? 41.077 14.580  20.403  0.90 17.99 ? 263 HOH A O   1 
HETATM 1333 O  O   . HOH D 4 .   ? 27.932 12.266  23.634  1.00 38.87 ? 264 HOH A O   1 
HETATM 1334 O  O   . HOH D 4 .   ? 40.436 19.090  27.025  0.56 18.91 ? 265 HOH A O   1 
HETATM 1335 O  O   . HOH D 4 .   ? 38.852 12.239  32.795  0.66 28.16 ? 266 HOH A O   1 
HETATM 1336 O  O   . HOH D 4 .   ? 23.460 15.577  5.090   0.97 44.35 ? 267 HOH A O   1 
HETATM 1337 O  O   . HOH D 4 .   ? 31.026 29.258  -1.449  0.63 31.10 ? 268 HOH A O   1 
HETATM 1338 O  O   . HOH D 4 .   ? 41.239 8.290   24.673  0.79 29.23 ? 269 HOH A O   1 
HETATM 1339 O  O   . HOH D 4 .   ? 25.987 2.074   18.554  0.92 35.96 ? 270 HOH A O   1 
HETATM 1340 O  O   . HOH D 4 .   ? 23.033 1.881   -3.429  0.99 26.77 ? 271 HOH A O   1 
HETATM 1341 O  O   . HOH D 4 .   ? 38.624 21.577  26.423  1.00 50.64 ? 272 HOH A O   1 
HETATM 1342 O  O   . HOH D 4 .   ? 20.347 9.621   17.104  0.83 37.90 ? 273 HOH A O   1 
HETATM 1343 O  O   . HOH D 4 .   ? 24.538 19.781  8.995   0.88 49.64 ? 274 HOH A O   1 
HETATM 1344 O  O   . HOH D 4 .   ? 39.802 21.115  17.143  0.75 34.03 ? 275 HOH A O   1 
HETATM 1345 O  O   . HOH D 4 .   ? 31.091 21.833  -14.957 0.57 13.15 ? 276 HOH A O   1 
HETATM 1346 O  O   . HOH D 4 .   ? 21.933 -0.636  -2.690  0.23 2.00  ? 277 HOH A O   1 
HETATM 1347 O  O   . HOH D 4 .   ? 25.111 20.460  -6.450  0.37 9.57  ? 278 HOH A O   1 
HETATM 1348 O  O   . HOH D 4 .   ? 41.930 15.166  -7.857  0.65 22.60 ? 279 HOH A O   1 
HETATM 1349 O  O   . HOH D 4 .   ? 32.138 10.669  -3.481  0.76 20.19 ? 280 HOH A O   1 
HETATM 1350 O  O   . HOH D 4 .   ? 48.629 20.893  14.353  0.93 44.29 ? 281 HOH A O   1 
HETATM 1351 O  O   . HOH D 4 .   ? 34.355 23.339  14.406  1.00 43.27 ? 282 HOH A O   1 
HETATM 1352 O  O   . HOH D 4 .   ? 44.901 11.015  -2.802  0.73 22.95 ? 283 HOH A O   1 
HETATM 1353 O  O   . HOH D 4 .   ? 31.872 6.422   30.631  0.79 35.09 ? 284 HOH A O   1 
HETATM 1354 O  O   . HOH D 4 .   ? 36.862 24.424  16.101  0.61 24.20 ? 285 HOH A O   1 
HETATM 1355 O  O   . HOH D 4 .   ? 21.851 13.516  9.658   0.98 46.93 ? 286 HOH A O   1 
HETATM 1356 O  O   . HOH D 4 .   ? 45.529 9.159   1.236   0.93 37.11 ? 287 HOH A O   1 
HETATM 1357 O  O   . HOH D 4 .   ? 30.235 19.920  18.482  0.91 37.96 ? 288 HOH A O   1 
HETATM 1358 O  O   . HOH D 4 .   ? 44.983 24.866  1.918   0.99 43.38 ? 289 HOH A O   1 
HETATM 1359 O  O   . HOH D 4 .   ? 40.409 5.893   -10.518 0.55 29.15 ? 290 HOH A O   1 
HETATM 1360 O  O   . HOH D 4 .   ? 32.661 25.378  -9.675  0.40 10.38 ? 291 HOH A O   1 
HETATM 1361 O  O   . HOH D 4 .   ? 23.143 1.911   -6.144  1.00 45.91 ? 292 HOH A O   1 
HETATM 1362 O  O   . HOH D 4 .   ? 45.782 8.635   11.805  0.44 14.99 ? 293 HOH A O   1 
HETATM 1363 O  O   . HOH D 4 .   ? 34.716 31.089  -2.438  1.00 48.32 ? 294 HOH A O   1 
HETATM 1364 O  O   . HOH D 4 .   ? 22.931 5.045   1.014   0.58 22.66 ? 295 HOH A O   1 
HETATM 1365 O  O   . HOH D 4 .   ? 25.363 17.701  -12.277 0.66 35.23 ? 296 HOH A O   1 
HETATM 1366 O  O   . HOH D 4 .   ? 33.227 19.662  28.351  1.00 27.38 ? 297 HOH A O   1 
HETATM 1367 O  O   . HOH D 4 .   ? 38.996 23.243  -6.890  0.71 30.52 ? 298 HOH A O   1 
HETATM 1368 O  O   . HOH D 4 .   ? 44.304 15.832  21.582  0.88 44.42 ? 299 HOH A O   1 
HETATM 1369 O  O   . HOH D 4 .   ? 30.596 7.204   27.407  0.76 31.89 ? 300 HOH A O   1 
HETATM 1370 O  O   . HOH D 4 .   ? 38.845 2.159   -8.980  0.71 43.42 ? 301 HOH A O   1 
HETATM 1371 O  O   . HOH D 4 .   ? 43.243 17.994  -5.209  0.82 40.48 ? 302 HOH A O   1 
HETATM 1372 O  O   . HOH D 4 .   ? 46.109 12.446  -4.845  0.85 51.33 ? 303 HOH A O   1 
HETATM 1373 O  O   . HOH D 4 .   ? 28.878 29.843  9.534   0.42 13.43 ? 304 HOH A O   1 
HETATM 1374 O  O   . HOH D 4 .   ? 31.326 32.630  13.400  0.51 23.94 ? 305 HOH A O   1 
HETATM 1375 O  O   . HOH D 4 .   ? 38.751 6.211   12.283  1.00 18.44 ? 306 HOH A O   1 
HETATM 1376 O  O   . HOH D 4 .   ? 34.112 26.130  14.497  0.61 27.08 ? 307 HOH A O   1 
HETATM 1377 O  O   . HOH D 4 .   ? 38.211 1.927   18.691  0.70 32.18 ? 308 HOH A O   1 
HETATM 1378 O  O   . HOH D 4 .   ? 36.250 4.525   -13.252 0.69 30.05 ? 309 HOH A O   1 
HETATM 1379 O  O   . HOH D 4 .   ? 42.503 2.208   0.192   0.86 37.62 ? 310 HOH A O   1 
HETATM 1380 O  O   . HOH D 4 .   ? 27.119 5.038   -8.658  0.89 44.53 ? 311 HOH A O   1 
HETATM 1381 O  O   . HOH D 4 .   ? 46.042 9.069   7.973   0.42 19.96 ? 312 HOH A O   1 
HETATM 1382 O  O   . HOH D 4 .   ? 40.853 23.031  15.173  0.80 34.08 ? 313 HOH A O   1 
HETATM 1383 O  O   . HOH D 4 .   ? 20.650 27.027  -0.675  0.58 30.45 ? 314 HOH A O   1 
HETATM 1384 O  O   . HOH D 4 .   ? 19.377 15.455  1.237   0.42 21.59 ? 315 HOH A O   1 
HETATM 1385 O  O   . HOH D 4 .   ? 40.691 4.414   13.725  0.57 34.06 ? 316 HOH A O   1 
HETATM 1386 O  O   . HOH D 4 .   ? 24.323 14.136  23.606  0.96 49.15 ? 317 HOH A O   1 
HETATM 1387 O  O   . HOH D 4 .   ? 30.275 11.067  25.971  0.45 24.90 ? 318 HOH A O   1 
HETATM 1388 O  O   . HOH D 4 .   ? 28.820 23.012  -14.398 0.58 34.36 ? 319 HOH A O   1 
HETATM 1389 O  O   . HOH D 4 .   ? 35.550 2.160   -14.421 0.56 30.73 ? 320 HOH A O   1 
HETATM 1390 O  O   . HOH D 4 .   ? 26.311 2.064   -6.763  0.46 26.85 ? 321 HOH A O   1 
HETATM 1391 O  O   . HOH D 4 .   ? 31.315 -8.294  -5.011  0.46 26.50 ? 322 HOH A O   1 
HETATM 1392 O  O   . HOH D 4 .   ? 19.354 25.622  -3.923  0.62 40.84 ? 323 HOH A O   1 
HETATM 1393 O  O   . HOH D 4 .   ? 39.756 -5.692  2.471   0.61 29.74 ? 324 HOH A O   1 
HETATM 1394 O  O   . HOH D 4 .   ? 27.235 31.295  6.894   0.52 29.09 ? 325 HOH A O   1 
HETATM 1395 O  O   . HOH D 4 .   ? 28.005 -8.098  9.017   0.39 20.46 ? 326 HOH A O   1 
HETATM 1396 O  O   . HOH D 4 .   ? 24.228 -3.112  12.264  0.39 22.56 ? 327 HOH A O   1 
HETATM 1397 O  O   . HOH D 4 .   ? 42.763 2.840   12.280  0.59 31.68 ? 328 HOH A O   1 
HETATM 1398 O  O   . HOH D 4 .   ? 20.961 15.301  17.295  0.60 32.67 ? 329 HOH A O   1 
HETATM 1399 O  O   . HOH D 4 .   ? 25.631 18.639  18.587  0.73 38.59 ? 330 HOH A O   1 
HETATM 1400 O  O   . HOH D 4 .   ? 41.315 5.536   24.304  0.49 35.96 ? 331 HOH A O   1 
HETATM 1401 O  O   . HOH D 4 .   ? 45.428 10.952  25.285  0.54 27.00 ? 332 HOH A O   1 
HETATM 1402 O  O   . HOH D 4 .   ? 39.198 15.023  -13.907 0.53 33.19 ? 333 HOH A O   1 
HETATM 1403 O  O   . HOH D 4 .   ? 26.997 22.284  -12.525 0.49 32.97 ? 334 HOH A O   1 
HETATM 1404 O  O   . HOH D 4 .   ? 32.342 1.648   -5.941  0.36 25.48 ? 335 HOH A O   1 
HETATM 1405 O  O   . HOH D 4 .   ? 44.481 19.681  -1.554  0.43 27.70 ? 336 HOH A O   1 
HETATM 1406 O  O   . HOH D 4 .   ? 19.791 9.220   9.182   0.56 38.23 ? 337 HOH A O   1 
HETATM 1407 O  O   . HOH D 4 .   ? 34.203 31.163  14.822  0.59 32.09 ? 338 HOH A O   1 
HETATM 1408 O  O   . HOH D 4 .   ? 18.367 9.395   15.260  0.56 33.73 ? 339 HOH A O   1 
HETATM 1409 O  O   . HOH D 4 .   ? 21.972 14.805  20.979  0.57 30.12 ? 340 HOH A O   1 
HETATM 1410 O  O   . HOH D 4 .   ? 33.470 -0.854  -4.262  0.52 28.74 ? 341 HOH A O   1 
HETATM 1411 O  O   . HOH D 4 .   ? 22.575 24.287  -2.606  0.43 29.70 ? 342 HOH A O   1 
HETATM 1412 O  O   . HOH D 4 .   ? 22.240 7.639   -3.096  0.48 32.51 ? 343 HOH A O   1 
HETATM 1413 O  O   . HOH D 4 .   ? 27.808 31.684  -2.151  0.47 30.12 ? 344 HOH A O   1 
HETATM 1414 O  O   . HOH D 4 .   ? 22.873 8.351   -0.576  0.52 25.11 ? 345 HOH A O   1 
HETATM 1415 O  O   . HOH D 4 .   ? 32.753 24.245  -0.422  0.34 33.11 ? 346 HOH A O   1 
HETATM 1416 O  O   . HOH D 4 .   ? 20.818 3.110   1.969   0.55 28.70 ? 347 HOH A O   1 
HETATM 1417 O  O   . HOH D 4 .   ? 21.687 1.047   6.500   0.44 33.04 ? 348 HOH A O   1 
HETATM 1418 O  O   . HOH D 4 .   ? 44.016 3.183   6.980   0.46 27.76 ? 349 HOH A O   1 
HETATM 1419 O  O   . HOH D 4 .   ? 31.348 29.185  13.989  0.51 29.17 ? 350 HOH A O   1 
HETATM 1420 O  O   . HOH D 4 .   ? 17.886 6.997   14.175  0.49 30.17 ? 351 HOH A O   1 
HETATM 1421 O  O   . HOH D 4 .   ? 48.947 18.764  18.533  0.44 29.43 ? 352 HOH A O   1 
HETATM 1422 O  O   . HOH D 4 .   ? 44.060 8.591   24.273  0.53 29.69 ? 353 HOH A O   1 
HETATM 1423 O  O   . HOH D 4 .   ? 39.764 23.195  24.466  0.43 29.89 ? 354 HOH A O   1 
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