data_7HZK
# 
_entry.id   7HZK 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   7HZK         pdb_00007hzk 10.2210/pdb7hzk/pdb 
WWPDB D_1001408128 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-12 
# 
_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             ? 
# 
_pdbx_database_status.entry_id                        7HZK 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-14 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
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 'Protease 2A'                                                                            15892.732 1   3.4.22.29 
? ? ? 
2 non-polymer syn 'ZINC ION'                                                                               65.409    1   ?         
? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                     78.133    3   ?         
? ? ? 
4 non-polymer syn '1-methyl-N-{[(3S)-1,2,3,4-tetrahydroisoquinolin-3-yl]methyl}-1H-indazole-3-carboxamide' 320.388   1   ?         
? ? ? 
5 water       nat water                                                                                    18.015    199 ?         
? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_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       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_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 'ZINC ION'                                                                               ZN    
3 'DIMETHYL SULFOXIDE'                                                                     DMS   
4 '1-methyl-N-{[(3S)-1,2,3,4-tetrahydroisoquinolin-3-yl]methyl}-1H-indazole-3-carboxamide' A1BQY 
5 water                                                                                    HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1BQY non-polymer         . '1-methyl-N-{[(3S)-1,2,3,4-tetrahydroisoquinolin-3-yl]methyl}-1H-indazole-3-carboxamide' ? 
'C19 H20 N4 O'   320.388 
ALA   'L-peptide linking' y ALANINE                                                                                  ? 
'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                 ? 
'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                               ? 
'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                          ? 
'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                 ? 
'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                     ? 'C2 H6 O S' 
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                                ? 
'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                          ? 
'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                  ? 
'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                ? 
'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                    ? 'H2 O' 
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                               ? 
'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                  ? 
'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                   ? 
'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                               ? 
'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                            ? 
'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                  ? 
'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                   ? 
'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                ? 
'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                               ? 
'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                 ? 
'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                   ? 
'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                                               ? 'Zn 2' 
65.409  
# 
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   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BQY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQY 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 ZN    1   201 1   ZN    ZN  A . 
C 3 DMS   1   202 -1  DMS   DMS A . 
D 3 DMS   1   203 1   DMS   DMS A . 
E 3 DMS   1   204 3   DMS   DMS A . 
F 4 A1BQY 1   205 201 A1BQY LIG A . 
G 5 HOH   1   301 181 HOH   HOH A . 
G 5 HOH   2   302 43  HOH   HOH A . 
G 5 HOH   3   303 219 HOH   HOH A . 
G 5 HOH   4   304 251 HOH   HOH A . 
G 5 HOH   5   305 254 HOH   HOH A . 
G 5 HOH   6   306 108 HOH   HOH A . 
G 5 HOH   7   307 220 HOH   HOH A . 
G 5 HOH   8   308 101 HOH   HOH A . 
G 5 HOH   9   309 168 HOH   HOH A . 
G 5 HOH   10  310 36  HOH   HOH A . 
G 5 HOH   11  311 132 HOH   HOH A . 
G 5 HOH   12  312 16  HOH   HOH A . 
G 5 HOH   13  313 13  HOH   HOH A . 
G 5 HOH   14  314 34  HOH   HOH A . 
G 5 HOH   15  315 182 HOH   HOH A . 
G 5 HOH   16  316 46  HOH   HOH A . 
G 5 HOH   17  317 211 HOH   HOH A . 
G 5 HOH   18  318 30  HOH   HOH A . 
G 5 HOH   19  319 214 HOH   HOH A . 
G 5 HOH   20  320 68  HOH   HOH A . 
G 5 HOH   21  321 174 HOH   HOH A . 
G 5 HOH   22  322 60  HOH   HOH A . 
G 5 HOH   23  323 26  HOH   HOH A . 
G 5 HOH   24  324 148 HOH   HOH A . 
G 5 HOH   25  325 133 HOH   HOH A . 
G 5 HOH   26  326 57  HOH   HOH A . 
G 5 HOH   27  327 205 HOH   HOH A . 
G 5 HOH   28  328 104 HOH   HOH A . 
G 5 HOH   29  329 4   HOH   HOH A . 
G 5 HOH   30  330 121 HOH   HOH A . 
G 5 HOH   31  331 112 HOH   HOH A . 
G 5 HOH   32  332 79  HOH   HOH A . 
G 5 HOH   33  333 173 HOH   HOH A . 
G 5 HOH   34  334 103 HOH   HOH A . 
G 5 HOH   35  335 58  HOH   HOH A . 
G 5 HOH   36  336 59  HOH   HOH A . 
G 5 HOH   37  337 29  HOH   HOH A . 
G 5 HOH   38  338 33  HOH   HOH A . 
G 5 HOH   39  339 113 HOH   HOH A . 
G 5 HOH   40  340 49  HOH   HOH A . 
G 5 HOH   41  341 97  HOH   HOH A . 
G 5 HOH   42  342 255 HOH   HOH A . 
G 5 HOH   43  343 19  HOH   HOH A . 
G 5 HOH   44  344 81  HOH   HOH A . 
G 5 HOH   45  345 234 HOH   HOH A . 
G 5 HOH   46  346 18  HOH   HOH A . 
G 5 HOH   47  347 41  HOH   HOH A . 
G 5 HOH   48  348 25  HOH   HOH A . 
G 5 HOH   49  349 169 HOH   HOH A . 
G 5 HOH   50  350 63  HOH   HOH A . 
G 5 HOH   51  351 249 HOH   HOH A . 
G 5 HOH   52  352 140 HOH   HOH A . 
G 5 HOH   53  353 212 HOH   HOH A . 
G 5 HOH   54  354 35  HOH   HOH A . 
G 5 HOH   55  355 110 HOH   HOH A . 
G 5 HOH   56  356 24  HOH   HOH A . 
G 5 HOH   57  357 28  HOH   HOH A . 
G 5 HOH   58  358 161 HOH   HOH A . 
G 5 HOH   59  359 70  HOH   HOH A . 
G 5 HOH   60  360 126 HOH   HOH A . 
G 5 HOH   61  361 88  HOH   HOH A . 
G 5 HOH   62  362 42  HOH   HOH A . 
G 5 HOH   63  363 37  HOH   HOH A . 
G 5 HOH   64  364 77  HOH   HOH A . 
G 5 HOH   65  365 2   HOH   HOH A . 
G 5 HOH   66  366 178 HOH   HOH A . 
G 5 HOH   67  367 11  HOH   HOH A . 
G 5 HOH   68  368 146 HOH   HOH A . 
G 5 HOH   69  369 67  HOH   HOH A . 
G 5 HOH   70  370 84  HOH   HOH A . 
G 5 HOH   71  371 9   HOH   HOH A . 
G 5 HOH   72  372 170 HOH   HOH A . 
G 5 HOH   73  373 120 HOH   HOH A . 
G 5 HOH   74  374 90  HOH   HOH A . 
G 5 HOH   75  375 7   HOH   HOH A . 
G 5 HOH   76  376 137 HOH   HOH A . 
G 5 HOH   77  377 106 HOH   HOH A . 
G 5 HOH   78  378 87  HOH   HOH A . 
G 5 HOH   79  379 27  HOH   HOH A . 
G 5 HOH   80  380 12  HOH   HOH A . 
G 5 HOH   81  381 227 HOH   HOH A . 
G 5 HOH   82  382 39  HOH   HOH A . 
G 5 HOH   83  383 21  HOH   HOH A . 
G 5 HOH   84  384 217 HOH   HOH A . 
G 5 HOH   85  385 119 HOH   HOH A . 
G 5 HOH   86  386 107 HOH   HOH A . 
G 5 HOH   87  387 8   HOH   HOH A . 
G 5 HOH   88  388 98  HOH   HOH A . 
G 5 HOH   89  389 20  HOH   HOH A . 
G 5 HOH   90  390 238 HOH   HOH A . 
G 5 HOH   91  391 105 HOH   HOH A . 
G 5 HOH   92  392 256 HOH   HOH A . 
G 5 HOH   93  393 17  HOH   HOH A . 
G 5 HOH   94  394 82  HOH   HOH A . 
G 5 HOH   95  395 14  HOH   HOH A . 
G 5 HOH   96  396 177 HOH   HOH A . 
G 5 HOH   97  397 15  HOH   HOH A . 
G 5 HOH   98  398 3   HOH   HOH A . 
G 5 HOH   99  399 111 HOH   HOH A . 
G 5 HOH   100 400 51  HOH   HOH A . 
G 5 HOH   101 401 141 HOH   HOH A . 
G 5 HOH   102 402 62  HOH   HOH A . 
G 5 HOH   103 403 72  HOH   HOH A . 
G 5 HOH   104 404 89  HOH   HOH A . 
G 5 HOH   105 405 235 HOH   HOH A . 
G 5 HOH   106 406 80  HOH   HOH A . 
G 5 HOH   107 407 155 HOH   HOH A . 
G 5 HOH   108 408 71  HOH   HOH A . 
G 5 HOH   109 409 52  HOH   HOH A . 
G 5 HOH   110 410 186 HOH   HOH A . 
G 5 HOH   111 411 195 HOH   HOH A . 
G 5 HOH   112 412 48  HOH   HOH A . 
G 5 HOH   113 413 50  HOH   HOH A . 
G 5 HOH   114 414 78  HOH   HOH A . 
G 5 HOH   115 415 40  HOH   HOH A . 
G 5 HOH   116 416 76  HOH   HOH A . 
G 5 HOH   117 417 95  HOH   HOH A . 
G 5 HOH   118 418 69  HOH   HOH A . 
G 5 HOH   119 419 215 HOH   HOH A . 
G 5 HOH   120 420 109 HOH   HOH A . 
G 5 HOH   121 421 124 HOH   HOH A . 
G 5 HOH   122 422 123 HOH   HOH A . 
G 5 HOH   123 423 64  HOH   HOH A . 
G 5 HOH   124 424 252 HOH   HOH A . 
G 5 HOH   125 425 100 HOH   HOH A . 
G 5 HOH   126 426 156 HOH   HOH A . 
G 5 HOH   127 427 138 HOH   HOH A . 
G 5 HOH   128 428 74  HOH   HOH A . 
G 5 HOH   129 429 10  HOH   HOH A . 
G 5 HOH   130 430 102 HOH   HOH A . 
G 5 HOH   131 431 203 HOH   HOH A . 
G 5 HOH   132 432 38  HOH   HOH A . 
G 5 HOH   133 433 5   HOH   HOH A . 
G 5 HOH   134 434 61  HOH   HOH A . 
G 5 HOH   135 435 91  HOH   HOH A . 
G 5 HOH   136 436 47  HOH   HOH A . 
G 5 HOH   137 437 204 HOH   HOH A . 
G 5 HOH   138 438 159 HOH   HOH A . 
G 5 HOH   139 439 128 HOH   HOH A . 
G 5 HOH   140 440 230 HOH   HOH A . 
G 5 HOH   141 441 147 HOH   HOH A . 
G 5 HOH   142 442 23  HOH   HOH A . 
G 5 HOH   143 443 192 HOH   HOH A . 
G 5 HOH   144 444 93  HOH   HOH A . 
G 5 HOH   145 445 96  HOH   HOH A . 
G 5 HOH   146 446 224 HOH   HOH A . 
G 5 HOH   147 447 248 HOH   HOH A . 
G 5 HOH   148 448 175 HOH   HOH A . 
G 5 HOH   149 449 245 HOH   HOH A . 
G 5 HOH   150 450 158 HOH   HOH A . 
G 5 HOH   151 451 135 HOH   HOH A . 
G 5 HOH   152 452 213 HOH   HOH A . 
G 5 HOH   153 453 233 HOH   HOH A . 
G 5 HOH   154 454 246 HOH   HOH A . 
G 5 HOH   155 455 154 HOH   HOH A . 
G 5 HOH   156 456 99  HOH   HOH A . 
G 5 HOH   157 457 239 HOH   HOH A . 
G 5 HOH   158 458 185 HOH   HOH A . 
G 5 HOH   159 459 142 HOH   HOH A . 
G 5 HOH   160 460 144 HOH   HOH A . 
G 5 HOH   161 461 127 HOH   HOH A . 
G 5 HOH   162 462 152 HOH   HOH A . 
G 5 HOH   163 463 189 HOH   HOH A . 
G 5 HOH   164 464 171 HOH   HOH A . 
G 5 HOH   165 465 247 HOH   HOH A . 
G 5 HOH   166 466 240 HOH   HOH A . 
G 5 HOH   167 467 56  HOH   HOH A . 
G 5 HOH   168 468 122 HOH   HOH A . 
G 5 HOH   169 469 253 HOH   HOH A . 
G 5 HOH   170 470 134 HOH   HOH A . 
G 5 HOH   171 471 218 HOH   HOH A . 
G 5 HOH   172 472 207 HOH   HOH A . 
G 5 HOH   173 473 65  HOH   HOH A . 
G 5 HOH   174 474 190 HOH   HOH A . 
G 5 HOH   175 475 223 HOH   HOH A . 
G 5 HOH   176 476 129 HOH   HOH A . 
G 5 HOH   177 477 86  HOH   HOH A . 
G 5 HOH   178 478 83  HOH   HOH A . 
G 5 HOH   179 479 202 HOH   HOH A . 
G 5 HOH   180 480 32  HOH   HOH A . 
G 5 HOH   181 481 229 HOH   HOH A . 
G 5 HOH   182 482 85  HOH   HOH A . 
G 5 HOH   183 483 75  HOH   HOH A . 
G 5 HOH   184 484 73  HOH   HOH A . 
G 5 HOH   185 485 209 HOH   HOH A . 
G 5 HOH   186 486 221 HOH   HOH A . 
G 5 HOH   187 487 165 HOH   HOH A . 
G 5 HOH   188 488 199 HOH   HOH A . 
G 5 HOH   189 489 118 HOH   HOH A . 
G 5 HOH   190 490 226 HOH   HOH A . 
G 5 HOH   191 491 206 HOH   HOH A . 
G 5 HOH   192 492 187 HOH   HOH A . 
G 5 HOH   193 493 222 HOH   HOH A . 
G 5 HOH   194 494 125 HOH   HOH A . 
G 5 HOH   195 495 160 HOH   HOH A . 
G 5 HOH   196 496 241 HOH   HOH A . 
G 5 HOH   197 497 242 HOH   HOH A . 
G 5 HOH   198 498 164 HOH   HOH A . 
G 5 HOH   199 499 244 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       REFMAC  5.8.0267 ? 1 
refinement       REFMAC5 .        ? 2 
'data scaling'   Aimless .        ? 3 
phasing          PHASER  .        ? 4 
'data reduction' XDS     .        ? 5 
# 
_cell.entry_id           7HZK 
_cell.length_a           86.742 
_cell.length_b           56.733 
_cell.length_c           32.737 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.96 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZK 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
# 
_exptl.entry_id          7HZK 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.52 
_exptl_crystal.density_percent_sol   51.28 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-09-05 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92134 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZK 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.45 
_reflns.d_resolution_high            1.27 
_reflns.number_obs                   35546 
_reflns.percent_possible_obs         85.6 
_reflns.pdbx_Rmerge_I_obs            0.055 
_reflns.pdbx_netI_over_sigmaI        15.2 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.060 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     219857 
_reflns.pdbx_chi_squared             0.55 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.27 
_reflns_shell.d_res_low                   1.29 
_reflns_shell.number_measured_all         2649 
_reflns_shell.number_unique_obs           721 
_reflns_shell.Rmerge_I_obs                1.706 
_reflns_shell.pdbx_chi_squared            0.13 
_reflns_shell.pdbx_redundancy             3.7 
_reflns_shell.percent_possible_obs        34.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             1.989 
_reflns_shell.pdbx_Rpim_I_all             1.013 
_reflns_shell.pdbx_CC_half                0.327 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_all           ? 
_reflns_shell.pdbx_CC_star                ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HZK 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     33633 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             47.43 
_refine.ls_d_res_high                            1.27 
_refine.ls_percent_reflns_obs                    85.06 
_refine.ls_R_factor_obs                          0.20238 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20044 
_refine.ls_R_factor_R_free                       0.23862 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  1752 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               26.193 
_refine.aniso_B[1][1]                            0.83 
_refine.aniso_B[2][2]                            -0.31 
_refine.aniso_B[3][3]                            -0.66 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.91 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.078 
_refine.pdbx_overall_ESU_R_Free                  0.081 
_refine.overall_SU_ML                            0.089 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             2.421 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         37 
_refine_hist.number_atoms_solvent             199 
_refine_hist.number_atoms_total               1319 
_refine_hist.d_res_high                       1.27 
_refine_hist.d_res_low                        47.43 
# 
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 
r_bond_refined_d             0.010  0.014  ? 2170 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.014  ? 1545 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.593  1.627  ? 2465 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.360  1.594  ? 3558 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.253  5.000  ? 227  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       30.587 21.765 ? 102  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       14.074 15.000 ? 252  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       22.170 15.000 ? 13   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.073  0.200  ? 214  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.009  0.020  ? 2232 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.003  0.020  ? 446  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  1.662  2.600  ? 1093 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.702  2.482  ? 1036 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.933  3.567  ? 1117 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.934  3.574  ? 1118 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.861  2.941  ? 1075 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.869  2.891  ? 1065 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.768  4.038  ? 1337 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       8.631  31.937 ? 2155 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         8.629  31.975 ? 2156 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.271 
_refine_ls_shell.d_res_low                        1.305 
_refine_ls_shell.number_reflns_R_work             953 
_refine_ls_shell.R_factor_R_work                  0.440 
_refine_ls_shell.percent_reflns_obs               32.16 
_refine_ls_shell.R_factor_R_free                  0.445 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             38 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.number_reflns_obs                ? 
# 
_struct.entry_id                  7HZK 
_struct.title                     
;Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre -- Crystal structure of Coxsackievirus A16 (G-10) 2A protease in complex with ASAP-0030249-001 (A71EV2A-x2293)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZK 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
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 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HZK 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_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,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_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 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_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 CYS 50  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 56  A ZN 201 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 58  A ZN 201 1_555 ? ? ? ? ? ? ? 2.271 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 116 A ZN 201 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 B ZN . ZN ? ? A HIS 118 A ZN 201 1_555 ? ? ? ? ? ? ? 2.075 ? ? 
# 
_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 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.1 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.4 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 117.9 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.5 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.2 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 116.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N VAL A 26  ? N VAL A 32  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HZK 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
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 ALA A 86  ? ? -35.28  137.37 
2 1 SER A 125 ? ? -136.32 -32.74 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 497 ? 6.02 . 
2 1 O ? A HOH 498 ? 6.21 . 
3 1 O ? A HOH 499 ? 8.00 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
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 
A1BQY N1   N  Y N 1   
A1BQY N3   N  N N 2   
A1BQY C4   C  N S 3   
A1BQY C5   C  N N 4   
A1BQY C6   C  Y N 5   
A1BQY C7   C  Y N 6   
A1BQY C8   C  Y N 7   
A1BQY C10  C  Y N 8   
A1BQY C13  C  Y N 9   
A1BQY C15  C  Y N 10  
A1BQY C17  C  Y N 11  
A1BQY N    N  Y N 12  
A1BQY C    C  N N 13  
A1BQY O    O  N N 14  
A1BQY C1   C  Y N 15  
A1BQY C11  C  Y N 16  
A1BQY C12  C  N N 17  
A1BQY C14  C  Y N 18  
A1BQY C16  C  Y N 19  
A1BQY C18  C  Y N 20  
A1BQY C2   C  N N 21  
A1BQY C3   C  N N 22  
A1BQY C9   C  Y N 23  
A1BQY N2   N  N N 24  
A1BQY H15  H  N N 25  
A1BQY H    H  N N 26  
A1BQY H7   H  N N 27  
A1BQY H8   H  N N 28  
A1BQY H9   H  N N 29  
A1BQY H10  H  N N 30  
A1BQY H12  H  N N 31  
A1BQY H17  H  N N 32  
A1BQY H19  H  N N 33  
A1BQY H2   H  N N 34  
A1BQY H1   H  N N 35  
A1BQY H3   H  N N 36  
A1BQY H13  H  N N 37  
A1BQY H14  H  N N 38  
A1BQY H16  H  N N 39  
A1BQY H18  H  N N 40  
A1BQY H6   H  N N 41  
A1BQY H5   H  N N 42  
A1BQY H11  H  N N 43  
A1BQY H4   H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
DMS   S    S  N N 132 
DMS   O    O  N N 133 
DMS   C1   C  N N 134 
DMS   C2   C  N N 135 
DMS   H11  H  N N 136 
DMS   H12  H  N N 137 
DMS   H13  H  N N 138 
DMS   H21  H  N N 139 
DMS   H22  H  N N 140 
DMS   H23  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
HOH   O    O  N N 212 
HOH   H1   H  N N 213 
HOH   H2   H  N N 214 
ILE   N    N  N N 215 
ILE   CA   C  N S 216 
ILE   C    C  N N 217 
ILE   O    O  N N 218 
ILE   CB   C  N S 219 
ILE   CG1  C  N N 220 
ILE   CG2  C  N N 221 
ILE   CD1  C  N N 222 
ILE   OXT  O  N N 223 
ILE   H    H  N N 224 
ILE   H2   H  N N 225 
ILE   HA   H  N N 226 
ILE   HB   H  N N 227 
ILE   HG12 H  N N 228 
ILE   HG13 H  N N 229 
ILE   HG21 H  N N 230 
ILE   HG22 H  N N 231 
ILE   HG23 H  N N 232 
ILE   HD11 H  N N 233 
ILE   HD12 H  N N 234 
ILE   HD13 H  N N 235 
ILE   HXT  H  N N 236 
LEU   N    N  N N 237 
LEU   CA   C  N S 238 
LEU   C    C  N N 239 
LEU   O    O  N N 240 
LEU   CB   C  N N 241 
LEU   CG   C  N N 242 
LEU   CD1  C  N N 243 
LEU   CD2  C  N N 244 
LEU   OXT  O  N N 245 
LEU   H    H  N N 246 
LEU   H2   H  N N 247 
LEU   HA   H  N N 248 
LEU   HB2  H  N N 249 
LEU   HB3  H  N N 250 
LEU   HG   H  N N 251 
LEU   HD11 H  N N 252 
LEU   HD12 H  N N 253 
LEU   HD13 H  N N 254 
LEU   HD21 H  N N 255 
LEU   HD22 H  N N 256 
LEU   HD23 H  N N 257 
LEU   HXT  H  N N 258 
LYS   N    N  N N 259 
LYS   CA   C  N S 260 
LYS   C    C  N N 261 
LYS   O    O  N N 262 
LYS   CB   C  N N 263 
LYS   CG   C  N N 264 
LYS   CD   C  N N 265 
LYS   CE   C  N N 266 
LYS   NZ   N  N N 267 
LYS   OXT  O  N N 268 
LYS   H    H  N N 269 
LYS   H2   H  N N 270 
LYS   HA   H  N N 271 
LYS   HB2  H  N N 272 
LYS   HB3  H  N N 273 
LYS   HG2  H  N N 274 
LYS   HG3  H  N N 275 
LYS   HD2  H  N N 276 
LYS   HD3  H  N N 277 
LYS   HE2  H  N N 278 
LYS   HE3  H  N N 279 
LYS   HZ1  H  N N 280 
LYS   HZ2  H  N N 281 
LYS   HZ3  H  N N 282 
LYS   HXT  H  N N 283 
MET   N    N  N N 284 
MET   CA   C  N S 285 
MET   C    C  N N 286 
MET   O    O  N N 287 
MET   CB   C  N N 288 
MET   CG   C  N N 289 
MET   SD   S  N N 290 
MET   CE   C  N N 291 
MET   OXT  O  N N 292 
MET   H    H  N N 293 
MET   H2   H  N N 294 
MET   HA   H  N N 295 
MET   HB2  H  N N 296 
MET   HB3  H  N N 297 
MET   HG2  H  N N 298 
MET   HG3  H  N N 299 
MET   HE1  H  N N 300 
MET   HE2  H  N N 301 
MET   HE3  H  N N 302 
MET   HXT  H  N N 303 
PHE   N    N  N N 304 
PHE   CA   C  N S 305 
PHE   C    C  N N 306 
PHE   O    O  N N 307 
PHE   CB   C  N N 308 
PHE   CG   C  Y N 309 
PHE   CD1  C  Y N 310 
PHE   CD2  C  Y N 311 
PHE   CE1  C  Y N 312 
PHE   CE2  C  Y N 313 
PHE   CZ   C  Y N 314 
PHE   OXT  O  N N 315 
PHE   H    H  N N 316 
PHE   H2   H  N N 317 
PHE   HA   H  N N 318 
PHE   HB2  H  N N 319 
PHE   HB3  H  N N 320 
PHE   HD1  H  N N 321 
PHE   HD2  H  N N 322 
PHE   HE1  H  N N 323 
PHE   HE2  H  N N 324 
PHE   HZ   H  N N 325 
PHE   HXT  H  N N 326 
PRO   N    N  N N 327 
PRO   CA   C  N S 328 
PRO   C    C  N N 329 
PRO   O    O  N N 330 
PRO   CB   C  N N 331 
PRO   CG   C  N N 332 
PRO   CD   C  N N 333 
PRO   OXT  O  N N 334 
PRO   H    H  N N 335 
PRO   HA   H  N N 336 
PRO   HB2  H  N N 337 
PRO   HB3  H  N N 338 
PRO   HG2  H  N N 339 
PRO   HG3  H  N N 340 
PRO   HD2  H  N N 341 
PRO   HD3  H  N N 342 
PRO   HXT  H  N N 343 
SER   N    N  N N 344 
SER   CA   C  N S 345 
SER   C    C  N N 346 
SER   O    O  N N 347 
SER   CB   C  N N 348 
SER   OG   O  N N 349 
SER   OXT  O  N N 350 
SER   H    H  N N 351 
SER   H2   H  N N 352 
SER   HA   H  N N 353 
SER   HB2  H  N N 354 
SER   HB3  H  N N 355 
SER   HG   H  N N 356 
SER   HXT  H  N N 357 
THR   N    N  N N 358 
THR   CA   C  N S 359 
THR   C    C  N N 360 
THR   O    O  N N 361 
THR   CB   C  N R 362 
THR   OG1  O  N N 363 
THR   CG2  C  N N 364 
THR   OXT  O  N N 365 
THR   H    H  N N 366 
THR   H2   H  N N 367 
THR   HA   H  N N 368 
THR   HB   H  N N 369 
THR   HG1  H  N N 370 
THR   HG21 H  N N 371 
THR   HG22 H  N N 372 
THR   HG23 H  N N 373 
THR   HXT  H  N N 374 
TRP   N    N  N N 375 
TRP   CA   C  N S 376 
TRP   C    C  N N 377 
TRP   O    O  N N 378 
TRP   CB   C  N N 379 
TRP   CG   C  Y N 380 
TRP   CD1  C  Y N 381 
TRP   CD2  C  Y N 382 
TRP   NE1  N  Y N 383 
TRP   CE2  C  Y N 384 
TRP   CE3  C  Y N 385 
TRP   CZ2  C  Y N 386 
TRP   CZ3  C  Y N 387 
TRP   CH2  C  Y N 388 
TRP   OXT  O  N N 389 
TRP   H    H  N N 390 
TRP   H2   H  N N 391 
TRP   HA   H  N N 392 
TRP   HB2  H  N N 393 
TRP   HB3  H  N N 394 
TRP   HD1  H  N N 395 
TRP   HE1  H  N N 396 
TRP   HE3  H  N N 397 
TRP   HZ2  H  N N 398 
TRP   HZ3  H  N N 399 
TRP   HH2  H  N N 400 
TRP   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
ZN    ZN   ZN N N 445 
# 
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 
A1BQY C   N    sing N N 1   
A1BQY N   N1   sing Y N 2   
A1BQY N1  C1   doub Y N 3   
A1BQY C1  C2   sing N N 4   
A1BQY C2  O    doub N N 5   
A1BQY N2  C2   sing N N 6   
A1BQY C3  N2   sing N N 7   
A1BQY C4  C3   sing N N 8   
A1BQY C4  C5   sing N N 9   
A1BQY C5  C6   sing N N 10  
A1BQY C6  C7   doub Y N 11  
A1BQY C7  C8   sing Y N 12  
A1BQY C8  C9   doub Y N 13  
A1BQY C9  C10  sing Y N 14  
A1BQY C10 C11  doub Y N 15  
A1BQY C6  C11  sing Y N 16  
A1BQY C11 C12  sing N N 17  
A1BQY C12 N3   sing N N 18  
A1BQY N3  C4   sing N N 19  
A1BQY C13 C1   sing Y N 20  
A1BQY C13 C14  doub Y N 21  
A1BQY C14 C15  sing Y N 22  
A1BQY C15 C16  doub Y N 23  
A1BQY C16 C17  sing Y N 24  
A1BQY C17 C18  doub Y N 25  
A1BQY C18 C13  sing Y N 26  
A1BQY N   C18  sing Y N 27  
A1BQY N3  H15  sing N N 28  
A1BQY C4  H    sing N N 29  
A1BQY C5  H7   sing N N 30  
A1BQY C5  H8   sing N N 31  
A1BQY C7  H9   sing N N 32  
A1BQY C8  H10  sing N N 33  
A1BQY C10 H12  sing N N 34  
A1BQY C15 H17  sing N N 35  
A1BQY C17 H19  sing N N 36  
A1BQY C   H2   sing N N 37  
A1BQY C   H1   sing N N 38  
A1BQY C   H3   sing N N 39  
A1BQY C12 H13  sing N N 40  
A1BQY C12 H14  sing N N 41  
A1BQY C14 H16  sing N N 42  
A1BQY C16 H18  sing N N 43  
A1BQY C3  H6   sing N N 44  
A1BQY C3  H5   sing N N 45  
A1BQY C9  H11  sing N N 46  
A1BQY N2  H4   sing N N 47  
ALA   N   CA   sing N N 48  
ALA   N   H    sing N N 49  
ALA   N   H2   sing N N 50  
ALA   CA  C    sing N N 51  
ALA   CA  CB   sing N N 52  
ALA   CA  HA   sing N N 53  
ALA   C   O    doub N N 54  
ALA   C   OXT  sing N N 55  
ALA   CB  HB1  sing N N 56  
ALA   CB  HB2  sing N N 57  
ALA   CB  HB3  sing N N 58  
ALA   OXT HXT  sing N N 59  
ARG   N   CA   sing N N 60  
ARG   N   H    sing N N 61  
ARG   N   H2   sing N N 62  
ARG   CA  C    sing N N 63  
ARG   CA  CB   sing N N 64  
ARG   CA  HA   sing N N 65  
ARG   C   O    doub N N 66  
ARG   C   OXT  sing N N 67  
ARG   CB  CG   sing N N 68  
ARG   CB  HB2  sing N N 69  
ARG   CB  HB3  sing N N 70  
ARG   CG  CD   sing N N 71  
ARG   CG  HG2  sing N N 72  
ARG   CG  HG3  sing N N 73  
ARG   CD  NE   sing N N 74  
ARG   CD  HD2  sing N N 75  
ARG   CD  HD3  sing N N 76  
ARG   NE  CZ   sing N N 77  
ARG   NE  HE   sing N N 78  
ARG   CZ  NH1  sing N N 79  
ARG   CZ  NH2  doub N N 80  
ARG   NH1 HH11 sing N N 81  
ARG   NH1 HH12 sing N N 82  
ARG   NH2 HH21 sing N N 83  
ARG   NH2 HH22 sing N N 84  
ARG   OXT HXT  sing N N 85  
ASN   N   CA   sing N N 86  
ASN   N   H    sing N N 87  
ASN   N   H2   sing N N 88  
ASN   CA  C    sing N N 89  
ASN   CA  CB   sing N N 90  
ASN   CA  HA   sing N N 91  
ASN   C   O    doub N N 92  
ASN   C   OXT  sing N N 93  
ASN   CB  CG   sing N N 94  
ASN   CB  HB2  sing N N 95  
ASN   CB  HB3  sing N N 96  
ASN   CG  OD1  doub N N 97  
ASN   CG  ND2  sing N N 98  
ASN   ND2 HD21 sing N N 99  
ASN   ND2 HD22 sing N N 100 
ASN   OXT HXT  sing N N 101 
ASP   N   CA   sing N N 102 
ASP   N   H    sing N N 103 
ASP   N   H2   sing N N 104 
ASP   CA  C    sing N N 105 
ASP   CA  CB   sing N N 106 
ASP   CA  HA   sing N N 107 
ASP   C   O    doub N N 108 
ASP   C   OXT  sing N N 109 
ASP   CB  CG   sing N N 110 
ASP   CB  HB2  sing N N 111 
ASP   CB  HB3  sing N N 112 
ASP   CG  OD1  doub N N 113 
ASP   CG  OD2  sing N N 114 
ASP   OD2 HD2  sing N N 115 
ASP   OXT HXT  sing N N 116 
CYS   N   CA   sing N N 117 
CYS   N   H    sing N N 118 
CYS   N   H2   sing N N 119 
CYS   CA  C    sing N N 120 
CYS   CA  CB   sing N N 121 
CYS   CA  HA   sing N N 122 
CYS   C   O    doub N N 123 
CYS   C   OXT  sing N N 124 
CYS   CB  SG   sing N N 125 
CYS   CB  HB2  sing N N 126 
CYS   CB  HB3  sing N N 127 
CYS   SG  HG   sing N N 128 
CYS   OXT HXT  sing N N 129 
DMS   S   O    doub N N 130 
DMS   S   C1   sing N N 131 
DMS   S   C2   sing N N 132 
DMS   C1  H11  sing N N 133 
DMS   C1  H12  sing N N 134 
DMS   C1  H13  sing N N 135 
DMS   C2  H21  sing N N 136 
DMS   C2  H22  sing N N 137 
DMS   C2  H23  sing N N 138 
GLN   N   CA   sing N N 139 
GLN   N   H    sing N N 140 
GLN   N   H2   sing N N 141 
GLN   CA  C    sing N N 142 
GLN   CA  CB   sing N N 143 
GLN   CA  HA   sing N N 144 
GLN   C   O    doub N N 145 
GLN   C   OXT  sing N N 146 
GLN   CB  CG   sing N N 147 
GLN   CB  HB2  sing N N 148 
GLN   CB  HB3  sing N N 149 
GLN   CG  CD   sing N N 150 
GLN   CG  HG2  sing N N 151 
GLN   CG  HG3  sing N N 152 
GLN   CD  OE1  doub N N 153 
GLN   CD  NE2  sing N N 154 
GLN   NE2 HE21 sing N N 155 
GLN   NE2 HE22 sing N N 156 
GLN   OXT HXT  sing N N 157 
GLU   N   CA   sing N N 158 
GLU   N   H    sing N N 159 
GLU   N   H2   sing N N 160 
GLU   CA  C    sing N N 161 
GLU   CA  CB   sing N N 162 
GLU   CA  HA   sing N N 163 
GLU   C   O    doub N N 164 
GLU   C   OXT  sing N N 165 
GLU   CB  CG   sing N N 166 
GLU   CB  HB2  sing N N 167 
GLU   CB  HB3  sing N N 168 
GLU   CG  CD   sing N N 169 
GLU   CG  HG2  sing N N 170 
GLU   CG  HG3  sing N N 171 
GLU   CD  OE1  doub N N 172 
GLU   CD  OE2  sing N N 173 
GLU   OE2 HE2  sing N N 174 
GLU   OXT HXT  sing N N 175 
GLY   N   CA   sing N N 176 
GLY   N   H    sing N N 177 
GLY   N   H2   sing N N 178 
GLY   CA  C    sing N N 179 
GLY   CA  HA2  sing N N 180 
GLY   CA  HA3  sing N N 181 
GLY   C   O    doub N N 182 
GLY   C   OXT  sing N N 183 
GLY   OXT HXT  sing N N 184 
HIS   N   CA   sing N N 185 
HIS   N   H    sing N N 186 
HIS   N   H2   sing N N 187 
HIS   CA  C    sing N N 188 
HIS   CA  CB   sing N N 189 
HIS   CA  HA   sing N N 190 
HIS   C   O    doub N N 191 
HIS   C   OXT  sing N N 192 
HIS   CB  CG   sing N N 193 
HIS   CB  HB2  sing N N 194 
HIS   CB  HB3  sing N N 195 
HIS   CG  ND1  sing Y N 196 
HIS   CG  CD2  doub Y N 197 
HIS   ND1 CE1  doub Y N 198 
HIS   ND1 HD1  sing N N 199 
HIS   CD2 NE2  sing Y N 200 
HIS   CD2 HD2  sing N N 201 
HIS   CE1 NE2  sing Y N 202 
HIS   CE1 HE1  sing N N 203 
HIS   NE2 HE2  sing N N 204 
HIS   OXT HXT  sing N N 205 
HOH   O   H1   sing N N 206 
HOH   O   H2   sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MET   N   CA   sing N N 274 
MET   N   H    sing N N 275 
MET   N   H2   sing N N 276 
MET   CA  C    sing N N 277 
MET   CA  CB   sing N N 278 
MET   CA  HA   sing N N 279 
MET   C   O    doub N N 280 
MET   C   OXT  sing N N 281 
MET   CB  CG   sing N N 282 
MET   CB  HB2  sing N N 283 
MET   CB  HB3  sing N N 284 
MET   CG  SD   sing N N 285 
MET   CG  HG2  sing N N 286 
MET   CG  HG3  sing N N 287 
MET   SD  CE   sing N N 288 
MET   CE  HE1  sing N N 289 
MET   CE  HE2  sing N N 290 
MET   CE  HE3  sing N N 291 
MET   OXT HXT  sing N N 292 
PHE   N   CA   sing N N 293 
PHE   N   H    sing N N 294 
PHE   N   H2   sing N N 295 
PHE   CA  C    sing N N 296 
PHE   CA  CB   sing N N 297 
PHE   CA  HA   sing N N 298 
PHE   C   O    doub N N 299 
PHE   C   OXT  sing N N 300 
PHE   CB  CG   sing N N 301 
PHE   CB  HB2  sing N N 302 
PHE   CB  HB3  sing N N 303 
PHE   CG  CD1  doub Y N 304 
PHE   CG  CD2  sing Y N 305 
PHE   CD1 CE1  sing Y N 306 
PHE   CD1 HD1  sing N N 307 
PHE   CD2 CE2  doub Y N 308 
PHE   CD2 HD2  sing N N 309 
PHE   CE1 CZ   doub Y N 310 
PHE   CE1 HE1  sing N N 311 
PHE   CE2 CZ   sing Y N 312 
PHE   CE2 HE2  sing N N 313 
PHE   CZ  HZ   sing N N 314 
PHE   OXT HXT  sing N N 315 
PRO   N   CA   sing N N 316 
PRO   N   CD   sing N N 317 
PRO   N   H    sing N N 318 
PRO   CA  C    sing N N 319 
PRO   CA  CB   sing N N 320 
PRO   CA  HA   sing N N 321 
PRO   C   O    doub N N 322 
PRO   C   OXT  sing N N 323 
PRO   CB  CG   sing N N 324 
PRO   CB  HB2  sing N N 325 
PRO   CB  HB3  sing N N 326 
PRO   CG  CD   sing N N 327 
PRO   CG  HG2  sing N N 328 
PRO   CG  HG3  sing N N 329 
PRO   CD  HD2  sing N N 330 
PRO   CD  HD3  sing N N 331 
PRO   OXT HXT  sing N N 332 
SER   N   CA   sing N N 333 
SER   N   H    sing N N 334 
SER   N   H2   sing N N 335 
SER   CA  C    sing N N 336 
SER   CA  CB   sing N N 337 
SER   CA  HA   sing N N 338 
SER   C   O    doub N N 339 
SER   C   OXT  sing N N 340 
SER   CB  OG   sing N N 341 
SER   CB  HB2  sing N N 342 
SER   CB  HB3  sing N N 343 
SER   OG  HG   sing N N 344 
SER   OXT HXT  sing N N 345 
THR   N   CA   sing N N 346 
THR   N   H    sing N N 347 
THR   N   H2   sing N N 348 
THR   CA  C    sing N N 349 
THR   CA  CB   sing N N 350 
THR   CA  HA   sing N N 351 
THR   C   O    doub N N 352 
THR   C   OXT  sing N N 353 
THR   CB  OG1  sing N N 354 
THR   CB  CG2  sing N N 355 
THR   CB  HB   sing N N 356 
THR   OG1 HG1  sing N N 357 
THR   CG2 HG21 sing N N 358 
THR   CG2 HG22 sing N N 359 
THR   CG2 HG23 sing N N 360 
THR   OXT HXT  sing N N 361 
TRP   N   CA   sing N N 362 
TRP   N   H    sing N N 363 
TRP   N   H2   sing N N 364 
TRP   CA  C    sing N N 365 
TRP   CA  CB   sing N N 366 
TRP   CA  HA   sing N N 367 
TRP   C   O    doub N N 368 
TRP   C   OXT  sing N N 369 
TRP   CB  CG   sing N N 370 
TRP   CB  HB2  sing N N 371 
TRP   CB  HB3  sing N N 372 
TRP   CG  CD1  doub Y N 373 
TRP   CG  CD2  sing Y N 374 
TRP   CD1 NE1  sing Y N 375 
TRP   CD1 HD1  sing N N 376 
TRP   CD2 CE2  doub Y N 377 
TRP   CD2 CE3  sing Y N 378 
TRP   NE1 CE2  sing Y N 379 
TRP   NE1 HE1  sing N N 380 
TRP   CE2 CZ2  sing Y N 381 
TRP   CE3 CZ3  doub Y N 382 
TRP   CE3 HE3  sing N N 383 
TRP   CZ2 CH2  doub Y N 384 
TRP   CZ2 HZ2  sing N N 385 
TRP   CZ3 CH2  sing Y N 386 
TRP   CZ3 HZ3  sing N N 387 
TRP   CH2 HH2  sing N N 388 
TRP   OXT HXT  sing N N 389 
TYR   N   CA   sing N N 390 
TYR   N   H    sing N N 391 
TYR   N   H2   sing N N 392 
TYR   CA  C    sing N N 393 
TYR   CA  CB   sing N N 394 
TYR   CA  HA   sing N N 395 
TYR   C   O    doub N N 396 
TYR   C   OXT  sing N N 397 
TYR   CB  CG   sing N N 398 
TYR   CB  HB2  sing N N 399 
TYR   CB  HB3  sing N N 400 
TYR   CG  CD1  doub Y N 401 
TYR   CG  CD2  sing Y N 402 
TYR   CD1 CE1  sing Y N 403 
TYR   CD1 HD1  sing N N 404 
TYR   CD2 CE2  doub Y N 405 
TYR   CD2 HD2  sing N N 406 
TYR   CE1 CZ   doub Y N 407 
TYR   CE1 HE1  sing N N 408 
TYR   CE2 CZ   sing Y N 409 
TYR   CE2 HE2  sing N N 410 
TYR   CZ  OH   sing N N 411 
TYR   OH  HH   sing N N 412 
TYR   OXT HXT  sing N N 413 
VAL   N   CA   sing N N 414 
VAL   N   H    sing N N 415 
VAL   N   H2   sing N N 416 
VAL   CA  C    sing N N 417 
VAL   CA  CB   sing N N 418 
VAL   CA  HA   sing N N 419 
VAL   C   O    doub N N 420 
VAL   C   OXT  sing N N 421 
VAL   CB  CG1  sing N N 422 
VAL   CB  CG2  sing N N 423 
VAL   CB  HB   sing N N 424 
VAL   CG1 HG11 sing N N 425 
VAL   CG1 HG12 sing N N 426 
VAL   CG1 HG13 sing N N 427 
VAL   CG2 HG21 sing N N 428 
VAL   CG2 HG22 sing N N 429 
VAL   CG2 HG23 sing N N 430 
VAL   OXT HXT  sing N N 431 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002330 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.type             'experimental model' 
# 
_atom_sites.entry_id                    7HZK 
_atom_sites.fract_transf_matrix[1][1]   0.011528 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001000 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017626 
_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]   0.030661 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.323 6.702   24.839 1.00 24.05  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.551 6.752   24.033 1.00 21.63  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.581 5.617   23.001 1.00 22.19  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.784 4.677   23.113 1.00 22.64  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.793 6.731   24.920 1.00 26.14  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.850 5.528   25.648 1.00 29.74  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.442 5.765   22.008 1.00 20.68  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.739 4.735   21.013 1.00 20.10  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.026 5.317   19.646 1.00 18.03  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.669 6.456   19.325 1.00 19.16  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.667 4.501   18.818 1.00 17.45  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.098 4.902   17.476 1.00 17.45  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.033 3.726   16.528 1.00 17.81  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.969 2.553   16.975 1.00 17.70  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.517 5.446   17.515 1.00 19.79  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.073 4.057   15.248 1.00 16.71  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.239 3.093   14.128 1.00 17.48  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.666 3.210   13.639 1.00 18.33  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.105 4.347   13.364 1.00 18.81  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.253 3.351   12.970 1.00 17.13  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.822 3.489   13.477 1.00 19.84  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.374 2.237   11.929 1.00 18.01  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.883 4.042   12.439 1.00 18.44  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.333 2.068   13.407 1.00 19.95  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.727 2.021   12.909 1.00 21.81  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.728 1.259   11.583 1.00 22.30  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.579 -0.008  11.632 1.00 22.30  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.637 1.393   13.962 1.00 21.00  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.749 2.222   15.218 1.00 23.22  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.606 3.305   15.280 1.00 23.79  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.994 1.940   16.337 1.00 23.76  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.712 4.073   16.430 1.00 23.53  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.085 2.696   17.500 1.00 27.10  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.937 3.796   17.539 1.00 24.30  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.020 4.530   18.703 1.00 26.16  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.741 1.993   10.481 1.00 20.89  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.697 1.469   9.081  1.00 22.59  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 26.882 2.053   8.314  1.00 24.93  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.107 3.247   8.313  1.00 23.22  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.347 1.754   8.387  1.00 21.58  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 23.990 3.230   8.401  1.00 22.61  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.300 1.205   6.951  1.00 24.81  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 27.662 1.181   7.675  1.00 24.93  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 28.884 1.631   6.999  1.00 27.83  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 29.751 2.436   7.949  1.00 23.52  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.022 1.948   9.063  1.00 22.57  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.193 3.621   7.512  1.00 26.17  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.012 4.509   8.376  1.00 26.01  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.134 5.679   8.850  1.00 26.94  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.630 6.832   8.953  1.00 24.47  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.329 4.903   7.704  1.00 30.72  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.315 3.744   7.656  1.00 31.29  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.164 3.572   8.536  1.00 34.59  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.164 2.894   6.660  1.00 32.52  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.861 5.374   9.132  1.00 22.73  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 27.884 6.368   9.634  1.00 19.56  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.325 5.940   10.989 1.00 19.89  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.112 4.747   11.320 1.00 20.09  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.732 6.547   8.633  1.00 19.94  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.140 7.047   7.268  1.00 22.98  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.874 8.217   7.141  1.00 25.29  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.765 6.394   6.097  1.00 25.92  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.235 8.716   5.902  1.00 27.14  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.112 6.883   4.847  1.00 28.43  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.853 8.052   4.749  1.00 27.40  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.233 8.552   3.541  1.00 33.04  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.017 6.975   11.780 1.00 19.90  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.343 6.879   13.087 1.00 17.99  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.102 7.770   13.018 1.00 17.54  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.234 8.973   12.720 1.00 17.56  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.248 7.300   14.258 1.00 18.88  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.537 7.570   15.574 1.00 20.53  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.557 7.835   16.699 1.00 21.23  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.084 8.826   17.667 1.00 23.35  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.462 8.594   18.806 1.00 23.84  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.183 7.361   19.210 1.00 26.59  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.101 9.621   19.556 1.00 23.66  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.911 7.156   13.121 1.00 16.84  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.629 7.901   13.017 1.00 16.49  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.078 8.011   14.429 1.00 16.33  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.799 6.968   15.048 1.00 15.62  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.617 7.170   12.134 1.00 16.32  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.394 8.033   11.896 1.00 16.35  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.264 6.682   10.883 1.00 16.34  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.889 9.243   14.885 1.00 16.01  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.366 9.511   16.244 1.00 16.65  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.206 10.490  16.160 1.00 15.43  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.052 11.181  15.133 1.00 17.19  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.446 10.036  17.199 1.00 19.04  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.406 8.936   17.514 1.00 22.77  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.128 11.293  16.646 1.00 18.57  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.448 10.587  17.257 1.00 16.40  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.487 11.695  17.416 1.00 16.86  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.267 13.025  17.449 1.00 16.35  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.256 13.143  18.243 1.00 17.84  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.675 11.579  18.693 1.00 17.77  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.773 10.354  18.751 1.00 16.01  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.168 9.319   19.232 1.00 17.63  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.565 10.473  18.219 1.00 17.48  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.875 13.969  16.640 1.00 17.91  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.551 15.299  16.583 1.00 17.35  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.593 15.925  17.990 1.00 19.80  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.700 16.407  18.416 1.00 19.14  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.867 16.237  15.614 1.00 19.72  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.644 17.544  15.389 1.00 19.72  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.850 18.378  14.404 1.00 22.71  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.481 19.625  13.916 1.00 24.77  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.615 20.762  14.589 1.00 26.77  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.275 20.868  15.859 1.00 25.78  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.146 21.813  13.966 1.00 29.12  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.534 15.760  18.777 1.00 21.43  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.483 16.375  20.140 1.00 21.44  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.435 15.691  21.118 1.00 23.31  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.698 16.289  22.195 1.00 25.13  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.054 16.491  20.663 1.00 22.47  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.468 15.202  21.120 1.00 22.85  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.894 14.302  20.248 1.00 22.50  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.315 14.689  22.355 1.00 23.63  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.434 13.278  20.937 1.00 21.94  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.661 13.485  22.231 1.00 25.55  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.980 14.515  20.806 1.00 20.48  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.907 13.768  21.681 1.00 22.19  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.321 13.716  21.097 1.00 20.12  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.180 13.067  21.725 1.00 23.33  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.337 12.361  21.900 1.00 23.40  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.945 12.327  22.511 1.00 23.88  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.465 10.895  22.652 1.00 25.10  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.978 13.032  23.875 1.00 25.09  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.574 14.392  19.974 1.00 19.56  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.911 14.385  19.331 1.00 20.50  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.941 15.003  20.277 1.00 20.76  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.608 15.992  20.999 1.00 22.33  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.863 15.137  18.039 1.00 20.38  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.110 14.428  20.284 1.00 19.45  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.261 14.885  21.101 1.00 22.00  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.065 15.967  20.379 1.00 22.42  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.941 16.183  19.154 1.00 20.84  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.171 13.699  21.427 1.00 21.35  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.830 13.220  20.251 1.00 22.82  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.446 12.582  22.156 1.00 23.38  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.019 16.592  21.090 1.00 23.36  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.973 17.497  20.409 1.00 23.88  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.764 16.687  19.378 1.00 21.58  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.964 17.209  18.288 1.00 20.76  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.927 18.209  21.401 1.00 26.59  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 32.119 18.814  20.721 1.00 29.94  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 32.052 20.023  20.041 1.00 29.42  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 33.380 18.345  20.521 1.00 32.78  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 33.237 20.308  19.521 1.00 31.28  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 34.072 19.273  19.762 1.00 32.78  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.208 15.463  19.692 1.00 22.30  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.967 14.653  18.706 1.00 24.30  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.100 14.435  17.447 1.00 21.10  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.607 14.533  16.301 1.00 20.40  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.475 13.328  19.283 1.00 27.98  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.316 12.574  18.268 1.00 33.41  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.447 12.966  17.966 1.00 39.89  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.755 11.539  17.661 1.00 32.35  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.799 14.223  17.641 1.00 21.09  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.884 14.110  16.476 1.00 19.68  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.938 15.364  15.591 1.00 17.55  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.029 15.279  14.342 1.00 17.70  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.464 13.808  16.933 1.00 18.99  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.245 12.390  17.428 1.00 19.66  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.864 11.453  16.852 1.00 21.57  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.439 12.207  18.356 1.00 20.09  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.726 16.544  16.180 1.00 18.30  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.692 17.830  15.464 1.00 18.40  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.050 18.123  14.815 1.00 17.29  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.076 18.727  13.779 1.00 18.97  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.269 18.940  16.432 1.00 18.63  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.786 19.006  16.675 1.00 17.87  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.102 18.536  17.761 1.00 21.11  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.807 19.543  15.777 1.00 18.45  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.762 18.817  17.626 1.00 19.35  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.549 19.391  16.398 1.00 17.65  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.872 20.125  14.517 1.00 18.63  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.374 19.834  15.779 1.00 18.89  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.717 20.536  13.904 1.00 20.26  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.487 20.424  14.553 1.00 19.75  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.142 17.681  15.443 1.00 18.77  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.506 17.921  14.969 1.00 19.94  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.869 16.979  13.807 1.00 21.28  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.913 17.200  13.139 1.00 23.09  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.457 17.766  16.125 1.00 18.62  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.009 15.982  13.520 1.00 21.17  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.256 14.949  12.479 1.00 21.86  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.959 14.841  11.666 1.00 20.33  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.543 13.717  11.289 1.00 22.15  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.714 13.643  13.112 1.00 23.73  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.105 13.712  13.711 1.00 26.35  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.099 13.554  13.021 1.00 29.01  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.191 13.943  14.994 1.00 27.86  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.271 15.958  11.477 1.00 19.68  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.891 15.965  10.927 1.00 19.99  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.883 15.555  9.456  1.00 21.77  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.727 16.046  8.646  1.00 23.15  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.334 17.366  11.074 1.00 20.19  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.908 17.578  10.567 1.00 19.54  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.927 16.712  11.332 1.00 20.79  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.532 19.033  10.718 1.00 23.45  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.824 14.849  9.048  0.41 19.79  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.465 14.624  7.617  0.41 19.31  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.183 15.384  7.254  0.41 19.85  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.143 16.047  6.192  0.41 18.46  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.333 13.121  7.315  0.41 18.67  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.709 12.862  5.956  0.41 17.56  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.679 12.440  7.412  0.41 18.35  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.141 15.256  8.075  0.41 18.78  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.803 15.819  7.751  0.41 19.49  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.991 15.907  9.042  0.41 19.53  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.202 15.062  9.912  0.41 18.42  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.112 14.982  6.673  0.41 18.52  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.657 15.281  6.467  0.41 17.27  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.099 16.286  5.735  0.41 17.94  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.555 14.532  7.018  0.41 16.81  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.734 16.202  5.767  0.41 16.62  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.372 15.148  6.556  0.41 16.91  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.448 13.421  7.853  0.41 17.61  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.102 14.688  6.903  0.41 18.50  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.191 12.951  8.180  0.41 18.52  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.038 13.579  7.712  0.41 17.89  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.126 16.914  9.161  0.41 20.17  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.260 17.117  10.350 0.41 20.04  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.975 17.798  9.882  0.41 19.79  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.030 18.580  8.900  0.41 20.57  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.003 17.908  11.432 0.41 21.65  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.635 19.194  10.911 0.41 21.88  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.663 20.262  10.422 0.41 24.14  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.024 21.017  9.479  0.41 23.76  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.542 20.353  10.976 0.41 22.89  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.851 17.461  10.514 0.41 18.94  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.511 18.016  10.173 0.41 20.09  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.727 18.129  11.486 0.41 20.95  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.472 17.087  12.123 0.41 19.11  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.891 17.111  9.114  0.41 20.69  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.894 17.692  8.124  0.41 21.78  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.205 18.666  8.465  0.41 25.41  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.830 17.133  6.998  0.41 23.17  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.443 19.359  11.925 0.41 21.86  ? 36  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 30  ? 15.563 19.654  13.082 0.41 24.18  ? 36  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 30  ? 14.154 19.149  12.746 0.41 20.96  ? 36  SER   A C   1 
ATOM   243  O  O   . SER   A 1 30  ? 13.511 18.579  13.639 0.41 25.59  ? 36  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 30  ? 15.570 21.132  13.384 0.41 23.95  ? 36  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 30  ? 14.954 21.842  12.324 0.41 27.18  ? 36  SER   A OG  1 
ATOM   246  N  N   . SER   A 1 31  ? 13.779 19.247  11.468 0.41 22.84  ? 37  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 31  ? 12.458 18.829  10.925 0.41 22.29  ? 37  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 31  ? 12.249 17.326  11.141 0.41 20.08  ? 37  SER   A C   1 
ATOM   249  O  O   . SER   A 1 31  ? 11.104 16.914  10.967 0.41 19.00  ? 37  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 31  ? 12.288 19.170  9.462  0.41 24.38  ? 37  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 31  ? 11.450 20.300  9.263  0.41 28.96  ? 37  SER   A OG  1 
ATOM   252  N  N   . ARG   A 1 32  ? 13.284 16.555  11.539 0.41 18.75  ? 38  ARG   A N   1 
ATOM   253  C  CA  . ARG   A 1 32  ? 13.210 15.062  11.632 0.41 16.62  ? 38  ARG   A CA  1 
ATOM   254  C  C   . ARG   A 1 32  ? 13.825 14.519  12.933 0.41 15.46  ? 38  ARG   A C   1 
ATOM   255  O  O   . ARG   A 1 32  ? 13.750 13.299  13.147 0.41 14.96  ? 38  ARG   A O   1 
ATOM   256  C  CB  . ARG   A 1 32  ? 13.936 14.412  10.445 0.41 15.86  ? 38  ARG   A CB  1 
ATOM   257  C  CG  . ARG   A 1 32  ? 13.400 14.759  9.067  0.41 15.31  ? 38  ARG   A CG  1 
ATOM   258  C  CD  . ARG   A 1 32  ? 14.219 14.174  7.920  0.41 15.36  ? 38  ARG   A CD  1 
ATOM   259  N  NE  . ARG   A 1 32  ? 14.167 12.720  7.836  0.41 14.39  ? 38  ARG   A NE  1 
ATOM   260  C  CZ  . ARG   A 1 32  ? 14.164 11.986  6.713  0.41 14.28  ? 38  ARG   A CZ  1 
ATOM   261  N  NH1 . ARG   A 1 32  ? 14.305 12.564  5.526  0.41 14.19  ? 38  ARG   A NH1 1 
ATOM   262  N  NH2 . ARG   A 1 32  ? 14.026 10.670  6.791  0.41 14.14  ? 38  ARG   A NH2 1 
ATOM   263  N  N   . ASP   A 1 33  ? 14.468 15.364  13.742 0.41 15.31  ? 39  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 33  ? 15.288 14.923  14.895 0.41 15.09  ? 39  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 33  ? 16.331 13.914  14.361 0.41 15.92  ? 39  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 33  ? 16.554 12.944  15.108 0.41 15.51  ? 39  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 33  ? 14.381 14.359  16.023 0.41 14.11  ? 39  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 33  ? 15.012 14.020  17.376 0.41 14.02  ? 39  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 33  ? 15.990 14.683  17.774 0.41 13.30  ? 39  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 33  ? 14.536 13.068  18.055 0.41 13.54  ? 39  ASP   A OD2 1 
ATOM   271  N  N   . LEU   A 1 34  ? 16.972 14.107  13.172 1.00 17.86  ? 40  LEU   A N   1 
ATOM   272  C  CA  . LEU   A 1 34  ? 18.048 13.142  12.777 1.00 17.14  ? 40  LEU   A CA  1 
ATOM   273  C  C   . LEU   A 1 34  ? 19.375 13.898  12.636 1.00 18.39  ? 40  LEU   A C   1 
ATOM   274  O  O   . LEU   A 1 34  ? 19.406 15.052  12.100 1.00 17.33  ? 40  LEU   A O   1 
ATOM   275  C  CB  . LEU   A 1 34  ? 17.672 12.427  11.478 1.00 19.04  ? 40  LEU   A CB  1 
ATOM   276  C  CG  . LEU   A 1 34  ? 16.612 11.330  11.575 1.00 19.01  ? 40  LEU   A CG  1 
ATOM   277  C  CD1 . LEU   A 1 34  ? 16.520 10.633  10.226 1.00 19.43  ? 40  LEU   A CD1 1 
ATOM   278  C  CD2 . LEU   A 1 34  ? 16.943 10.332  12.696 1.00 18.38  ? 40  LEU   A CD2 1 
ATOM   279  N  N   . LEU   A 1 35  ? 20.430 13.251  13.107 1.00 17.17  ? 41  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 35  ? 21.810 13.688  12.793 1.00 16.86  ? 41  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 35  ? 22.650 12.453  12.455 1.00 15.16  ? 41  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 35  ? 22.491 11.419  13.100 1.00 16.35  ? 41  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 35  ? 22.384 14.484  13.968 1.00 18.80  ? 41  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 35  ? 23.768 15.107  13.724 1.00 18.08  ? 41  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 35  ? 23.887 16.467  14.418 1.00 18.84  ? 41  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 35  ? 24.866 14.175  14.202 1.00 19.29  ? 41  LEU   A CD2 1 
ATOM   287  N  N   . VAL   A 1 36  ? 23.474 12.588  11.434 1.00 15.26  ? 42  VAL   A N   1 
ATOM   288  C  CA  . VAL   A 1 36  ? 24.426 11.529  10.999 1.00 15.36  ? 42  VAL   A CA  1 
ATOM   289  C  C   . VAL   A 1 36  ? 25.847 12.076  11.083 1.00 17.66  ? 42  VAL   A C   1 
ATOM   290  O  O   . VAL   A 1 36  ? 26.116 13.143  10.517 1.00 18.37  ? 42  VAL   A O   1 
ATOM   291  C  CB  . VAL   A 1 36  ? 24.101 11.021  9.593  1.00 17.54  ? 42  VAL   A CB  1 
ATOM   292  C  CG1 . VAL   A 1 36  ? 25.035 9.893   9.166  1.00 17.75  ? 42  VAL   A CG1 1 
ATOM   293  C  CG2 . VAL   A 1 36  ? 22.664 10.541  9.488  1.00 17.44  ? 42  VAL   A CG2 1 
ATOM   294  N  N   . SER   A 1 37  ? 26.692 11.366  11.793 1.00 17.43  ? 43  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 37  ? 28.140 11.671  11.904 1.00 18.82  ? 43  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 37  ? 28.947 10.513  11.270 1.00 20.38  ? 43  SER   A C   1 
ATOM   297  O  O   . SER   A 1 37  ? 28.415 9.402   11.091 1.00 21.02  ? 43  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 37  ? 28.494 11.906  13.351 1.00 18.00  ? 43  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 37  ? 28.266 10.781  14.179 1.00 19.47  ? 43  SER   A OG  1 
ATOM   300  N  N   . SER   A 1 38  ? 30.234 10.748  11.065 1.00 21.65  ? 44  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 38  ? 31.194 9.779   10.471 1.00 23.50  ? 44  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 38  ? 31.878 8.973   11.565 1.00 27.12  ? 44  SER   A C   1 
ATOM   303  O  O   . SER   A 1 38  ? 32.116 9.516   12.638 1.00 27.91  ? 44  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 38  ? 32.197 10.504  9.624  1.00 25.91  ? 44  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 38  ? 32.986 11.351  10.432 1.00 26.31  ? 44  SER   A OG  1 
ATOM   306  N  N   . THR   A 1 39  ? 32.165 7.685   11.317 1.00 27.35  ? 45  THR   A N   1 
ATOM   307  C  CA  . THR   A 1 39  ? 32.831 6.780   12.285 1.00 28.66  ? 45  THR   A CA  1 
ATOM   308  C  C   . THR   A 1 39  ? 34.133 6.241   11.671 1.00 28.89  ? 45  THR   A C   1 
ATOM   309  O  O   . THR   A 1 39  ? 34.243 6.166   10.463 1.00 29.51  ? 45  THR   A O   1 
ATOM   310  C  CB  . THR   A 1 39  ? 31.914 5.607   12.652 1.00 31.08  ? 45  THR   A CB  1 
ATOM   311  O  OG1 . THR   A 1 39  ? 31.718 4.881   11.441 1.00 30.35  ? 45  THR   A OG1 1 
ATOM   312  C  CG2 . THR   A 1 39  ? 30.569 6.047   13.193 1.00 31.77  ? 45  THR   A CG2 1 
ATOM   313  N  N   . THR   A 1 40  ? 35.117 5.927   12.504 0.50 32.27  ? 46  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 40  ? 36.357 5.244   12.056 0.50 34.17  ? 46  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 40  ? 35.997 3.787   11.728 0.50 34.11  ? 46  THR   A C   1 
ATOM   316  O  O   . THR   A 1 40  ? 36.326 3.325   10.604 0.50 34.16  ? 46  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 40  ? 37.472 5.481   13.081 0.50 34.94  ? 46  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 40  ? 37.111 4.948   14.354 0.50 37.45  ? 46  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 40  ? 37.766 6.956   13.251 0.50 36.36  ? 46  THR   A CG2 1 
ATOM   320  N  N   . ALA   A 1 41  ? 35.266 3.131   12.634 0.50 34.73  ? 47  ALA   A N   1 
ATOM   321  C  CA  . ALA   A 1 41  ? 34.863 1.706   12.562 0.50 32.59  ? 47  ALA   A CA  1 
ATOM   322  C  C   . ALA   A 1 41  ? 33.696 1.501   11.584 0.50 31.24  ? 47  ALA   A C   1 
ATOM   323  O  O   . ALA   A 1 41  ? 32.895 2.429   11.369 0.50 26.17  ? 47  ALA   A O   1 
ATOM   324  C  CB  . ALA   A 1 41  ? 34.505 1.224   13.947 0.50 32.45  ? 47  ALA   A CB  1 
ATOM   325  N  N   . GLN   A 1 42  ? 33.598 0.298   11.016 0.50 31.78  ? 48  GLN   A N   1 
ATOM   326  C  CA  . GLN   A 1 42  ? 32.459 -0.104  10.149 0.50 30.93  ? 48  GLN   A CA  1 
ATOM   327  C  C   . GLN   A 1 42  ? 31.343 -0.619  11.056 0.50 28.45  ? 48  GLN   A C   1 
ATOM   328  O  O   . GLN   A 1 42  ? 31.653 -1.390  11.973 0.50 29.81  ? 48  GLN   A O   1 
ATOM   329  C  CB  . GLN   A 1 42  ? 32.898 -1.168  9.144  0.50 33.08  ? 48  GLN   A CB  1 
ATOM   330  C  CG  . GLN   A 1 42  ? 32.529 -0.822  7.713  0.50 36.02  ? 48  GLN   A CG  1 
ATOM   331  C  CD  . GLN   A 1 42  ? 31.470 -1.716  7.123  0.50 38.32  ? 48  GLN   A CD  1 
ATOM   332  O  OE1 . GLN   A 1 42  ? 31.583 -2.149  5.979  0.50 38.42  ? 48  GLN   A OE1 1 
ATOM   333  N  NE2 . GLN   A 1 42  ? 30.428 -1.994  7.889  0.50 38.36  ? 48  GLN   A NE2 1 
ATOM   334  N  N   . GLY   A 1 43  ? 30.097 -0.223  10.785 0.50 27.32  ? 49  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 43  ? 28.925 -0.644  11.572 0.50 26.84  ? 49  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 43  ? 28.340 -1.929  11.020 0.50 26.26  ? 49  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 43  ? 28.618 -2.227  9.858  0.50 27.75  ? 49  GLY   A O   1 
ATOM   338  N  N   . CYS   A 1 44  ? 27.527 -2.650  11.778 0.50 26.31  ? 50  CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 44  ? 27.010 -3.973  11.340 0.50 25.17  ? 50  CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 44  ? 25.512 -3.868  10.986 0.50 24.47  ? 50  CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 44  ? 24.982 -4.836  10.410 0.50 23.47  ? 50  CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 44  ? 27.317 -5.058  12.372 0.50 24.34  ? 50  CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 44  ? 29.085 -5.253  12.785 0.50 27.54  ? 50  CYS   A SG  1 
ATOM   344  N  N   . ASP   A 1 45  ? 24.862 -2.716  11.208 1.00 24.00  ? 51  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 45  ? 23.399 -2.610  10.890 1.00 21.38  ? 51  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 45  ? 23.117 -2.476  9.391  1.00 23.49  ? 51  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 45  ? 23.903 -1.841  8.665  1.00 26.47  ? 51  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 45  ? 22.763 -1.429  11.645 1.00 23.22  ? 51  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 45  ? 22.849 -1.515  13.158 1.00 26.29  ? 51  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 45  ? 22.733 -2.628  13.709 1.00 30.98  ? 51  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 45  ? 22.973 -0.452  13.818 1.00 26.70  ? 51  ASP   A OD2 1 
ATOM   352  N  N   . THR   A 1 46  ? 21.954 -2.998  8.977  1.00 22.29  ? 52  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 46  ? 21.370 -2.938  7.619  1.00 25.12  ? 52  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 46  ? 20.105 -2.086  7.678  1.00 21.89  ? 52  THR   A C   1 
ATOM   355  O  O   . THR   A 1 46  ? 19.291 -2.271  8.632  1.00 22.28  ? 52  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 46  ? 21.087 -4.343  7.070  1.00 28.93  ? 52  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 46  ? 22.357 -4.995  6.938  1.00 32.68  ? 52  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 46  ? 20.350 -4.326  5.751  1.00 31.82  ? 52  THR   A CG2 1 
ATOM   359  N  N   . ILE   A 1 47  ? 19.983 -1.164  6.733  1.00 22.05  ? 53  ILE   A N   1 
ATOM   360  C  CA  . ILE   A 1 47  ? 18.797 -0.284  6.636  1.00 20.02  ? 53  ILE   A CA  1 
ATOM   361  C  C   . ILE   A 1 47  ? 17.762 -0.981  5.755  1.00 19.72  ? 53  ILE   A C   1 
ATOM   362  O  O   . ILE   A 1 47  ? 18.125 -1.485  4.675  1.00 21.31  ? 53  ILE   A O   1 
ATOM   363  C  CB  . ILE   A 1 47  ? 19.155 1.098   6.064  1.00 19.91  ? 53  ILE   A CB  1 
ATOM   364  C  CG1 . ILE   A 1 47  ? 20.329 1.761   6.803  1.00 21.00  ? 53  ILE   A CG1 1 
ATOM   365  C  CG2 . ILE   A 1 47  ? 17.945 1.983   6.002  1.00 20.60  ? 53  ILE   A CG2 1 
ATOM   366  C  CD1 . ILE   A 1 47  ? 20.095 1.942   8.301  1.00 21.51  ? 53  ILE   A CD1 1 
ATOM   367  N  N   . ALA   A 1 48  ? 16.539 -1.102  6.250  1.00 18.13  ? 54  ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 48  ? 15.398 -1.613  5.455  1.00 18.80  ? 54  ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 48  ? 15.165 -0.684  4.248  1.00 16.45  ? 54  ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 48  ? 15.207 0.559   4.378  1.00 17.40  ? 54  ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 48  ? 14.213 -1.687  6.380  1.00 18.55  ? 54  ALA   A CB  1 
ATOM   372  N  N   . ARG   A 1 49  ? 14.836 -1.291  3.093  1.00 18.70  ? 55  ARG   A N   1 
ATOM   373  C  CA  . ARG   A 1 49  ? 14.405 -0.566  1.879  1.00 18.46  ? 55  ARG   A CA  1 
ATOM   374  C  C   . ARG   A 1 49  ? 13.067 -1.153  1.446  1.00 17.78  ? 55  ARG   A C   1 
ATOM   375  O  O   . ARG   A 1 49  ? 13.039 -2.200  0.774  1.00 21.21  ? 55  ARG   A O   1 
ATOM   376  C  CB  . ARG   A 1 49  ? 15.491 -0.642  0.798  1.00 19.72  ? 55  ARG   A CB  1 
ATOM   377  C  CG  . ARG   A 1 49  ? 16.853 -0.078  1.211  1.00 20.29  ? 55  ARG   A CG  1 
ATOM   378  C  CD  . ARG   A 1 49  ? 16.911 1.412   1.537  1.00 20.84  ? 55  ARG   A CD  1 
ATOM   379  N  NE  . ARG   A 1 49  ? 18.271 1.745   2.008  1.00 24.34  ? 55  ARG   A NE  1 
ATOM   380  C  CZ  . ARG   A 1 49  ? 18.603 2.844   2.668  1.00 23.26  ? 55  ARG   A CZ  1 
ATOM   381  N  NH1 . ARG   A 1 49  ? 17.713 3.754   2.961  1.00 24.75  ? 55  ARG   A NH1 1 
ATOM   382  N  NH2 . ARG   A 1 49  ? 19.853 3.025   3.085  1.00 26.97  ? 55  ARG   A NH2 1 
ATOM   383  N  N   . CYS   A 1 50  ? 11.995 -0.521  1.890  1.00 18.50  ? 56  CYS   A N   1 
ATOM   384  C  CA  . CYS   A 1 50  ? 10.648 -1.158  1.906  1.00 18.55  ? 56  CYS   A CA  1 
ATOM   385  C  C   . CYS   A 1 50  ? 9.569  -0.207  2.381  1.00 19.62  ? 56  CYS   A C   1 
ATOM   386  O  O   . CYS   A 1 50  ? 9.901  0.897   2.811  1.00 19.87  ? 56  CYS   A O   1 
ATOM   387  C  CB  . CYS   A 1 50  ? 10.690 -2.346  2.839  1.00 16.88  ? 56  CYS   A CB  1 
ATOM   388  S  SG  . CYS   A 1 50  ? 10.704 -1.860  4.604  1.00 18.07  ? 56  CYS   A SG  1 
ATOM   389  N  N   . ASP   A 1 51  ? 8.290  -0.616  2.279  0.50 20.29  ? 57  ASP   A N   1 
ATOM   390  C  CA  . ASP   A 1 51  ? 7.139  0.137   2.841  0.50 19.92  ? 57  ASP   A CA  1 
ATOM   391  C  C   . ASP   A 1 51  ? 6.390  -0.715  3.877  0.50 20.57  ? 57  ASP   A C   1 
ATOM   392  O  O   . ASP   A 1 51  ? 5.178  -0.563  3.960  0.50 20.81  ? 57  ASP   A O   1 
ATOM   393  C  CB  . ASP   A 1 51  ? 6.167  0.575   1.745  0.50 22.22  ? 57  ASP   A CB  1 
ATOM   394  C  CG  . ASP   A 1 51  ? 5.479  -0.569  1.021  0.50 24.16  ? 57  ASP   A CG  1 
ATOM   395  O  OD1 . ASP   A 1 51  ? 5.826  -1.736  1.265  0.50 26.07  ? 57  ASP   A OD1 1 
ATOM   396  O  OD2 . ASP   A 1 51  ? 4.568  -0.271  0.221  0.50 28.33  ? 57  ASP   A OD2 1 
ATOM   397  N  N   . CYS   A 1 52  ? 7.096  -1.547  4.644  1.00 18.21  ? 58  CYS   A N   1 
ATOM   398  C  CA  . CYS   A 1 52  ? 6.498  -2.226  5.837  1.00 17.76  ? 58  CYS   A CA  1 
ATOM   399  C  C   . CYS   A 1 52  ? 5.830  -1.209  6.777  1.00 17.34  ? 58  CYS   A C   1 
ATOM   400  O  O   . CYS   A 1 52  ? 6.343  -0.087  7.023  1.00 17.97  ? 58  CYS   A O   1 
ATOM   401  C  CB  . CYS   A 1 52  ? 7.520  -3.037  6.615  1.00 17.46  ? 58  CYS   A CB  1 
ATOM   402  S  SG  . CYS   A 1 52  ? 8.197  -4.482  5.758  1.00 20.69  ? 58  CYS   A SG  1 
ATOM   403  N  N   . GLN   A 1 53  ? 4.724  -1.687  7.345  1.00 17.24  ? 59  GLN   A N   1 
ATOM   404  C  CA  . GLN   A 1 53  ? 3.996  -1.000  8.419  1.00 17.14  ? 59  GLN   A CA  1 
ATOM   405  C  C   . GLN   A 1 53  ? 3.847  -1.957  9.620  1.00 15.82  ? 59  GLN   A C   1 
ATOM   406  O  O   . GLN   A 1 53  ? 3.059  -1.607  10.484 1.00 16.71  ? 59  GLN   A O   1 
ATOM   407  C  CB  . GLN   A 1 53  ? 2.634  -0.484  7.924  1.00 19.61  ? 59  GLN   A CB  1 
ATOM   408  C  CG  . GLN   A 1 53  ? 2.689  0.741   7.024  1.00 21.75  ? 59  GLN   A CG  1 
ATOM   409  C  CD  . GLN   A 1 53  ? 1.292  1.270   6.763  1.00 22.71  ? 59  GLN   A CD  1 
ATOM   410  O  OE1 . GLN   A 1 53  ? 0.766  1.078   5.664  1.00 25.74  ? 59  GLN   A OE1 1 
ATOM   411  N  NE2 . GLN   A 1 53  ? 0.668  1.901   7.760  1.00 23.65  ? 59  GLN   A NE2 1 
ATOM   412  N  N   . THR   A 1 54  ? 4.612  -3.042  9.721  1.00 16.96  ? 60  THR   A N   1 
ATOM   413  C  CA  . THR   A 1 54  ? 4.691  -3.849  10.984 1.00 17.14  ? 60  THR   A CA  1 
ATOM   414  C  C   . THR   A 1 54  ? 6.164  -4.092  11.291 1.00 18.13  ? 60  THR   A C   1 
ATOM   415  O  O   . THR   A 1 54  ? 6.976  -4.220  10.373 1.00 18.42  ? 60  THR   A O   1 
ATOM   416  C  CB  . THR   A 1 54  ? 3.873  -5.134  10.929 1.00 19.95  ? 60  THR   A CB  1 
ATOM   417  O  OG1 . THR   A 1 54  ? 4.498  -5.951  9.965  1.00 24.44  ? 60  THR   A OG1 1 
ATOM   418  C  CG2 . THR   A 1 54  ? 2.445  -4.889  10.540 1.00 18.45  ? 60  THR   A CG2 1 
ATOM   419  N  N   . GLY   A 1 55  ? 6.489  -4.132  12.543 1.00 14.42  ? 61  GLY   A N   1 
ATOM   420  C  CA  . GLY   A 1 55  ? 7.851  -4.349  13.024 1.00 14.52  ? 61  GLY   A CA  1 
ATOM   421  C  C   . GLY   A 1 55  ? 7.874  -4.469  14.510 1.00 15.21  ? 61  GLY   A C   1 
ATOM   422  O  O   . GLY   A 1 55  ? 6.865  -4.829  15.139 1.00 16.01  ? 61  GLY   A O   1 
ATOM   423  N  N   . VAL   A 1 56  ? 9.064  -4.318  15.070 1.00 13.57  ? 62  VAL   A N   1 
ATOM   424  C  CA  . VAL   A 1 56  ? 9.333  -4.511  16.512 1.00 15.66  ? 62  VAL   A CA  1 
ATOM   425  C  C   . VAL   A 1 56  ? 10.209 -3.345  16.968 1.00 14.85  ? 62  VAL   A C   1 
ATOM   426  O  O   . VAL   A 1 56  ? 11.164 -3.046  16.283 1.00 15.07  ? 62  VAL   A O   1 
ATOM   427  C  CB  . VAL   A 1 56  ? 10.017 -5.869  16.760 1.00 16.54  ? 62  VAL   A CB  1 
ATOM   428  C  CG1 . VAL   A 1 56  ? 10.554 -5.950  18.184 1.00 17.81  ? 62  VAL   A CG1 1 
ATOM   429  C  CG2 . VAL   A 1 56  ? 9.091  -7.023  16.414 1.00 15.66  ? 62  VAL   A CG2 1 
ATOM   430  N  N   . TYR   A 1 57  ? 9.902  -2.667  18.078 1.00 16.14  ? 63  TYR   A N   1 
ATOM   431  C  CA  . TYR   A 1 57  ? 10.755 -1.578  18.634 1.00 14.45  ? 63  TYR   A CA  1 
ATOM   432  C  C   . TYR   A 1 57  ? 11.234 -1.878  20.055 1.00 14.67  ? 63  TYR   A C   1 
ATOM   433  O  O   . TYR   A 1 57  ? 10.591 -2.639  20.756 1.00 14.06  ? 63  TYR   A O   1 
ATOM   434  C  CB  . TYR   A 1 57  ? 10.045 -0.223  18.586 1.00 15.65  ? 63  TYR   A CB  1 
ATOM   435  C  CG  . TYR   A 1 57  ? 9.085  0.085   19.725 1.00 15.31  ? 63  TYR   A CG  1 
ATOM   436  C  CD1 . TYR   A 1 57  ? 7.797  -0.445  19.751 1.00 16.53  ? 63  TYR   A CD1 1 
ATOM   437  C  CD2 . TYR   A 1 57  ? 9.449  0.933   20.760 1.00 15.31  ? 63  TYR   A CD2 1 
ATOM   438  C  CE1 . TYR   A 1 57  ? 6.902  -0.143  20.774 1.00 17.44  ? 63  TYR   A CE1 1 
ATOM   439  C  CE2 . TYR   A 1 57  ? 8.591  1.218   21.811 1.00 16.97  ? 63  TYR   A CE2 1 
ATOM   440  C  CZ  . TYR   A 1 57  ? 7.299  0.684   21.809 1.00 16.36  ? 63  TYR   A CZ  1 
ATOM   441  O  OH  . TYR   A 1 57  ? 6.405  0.969   22.824 1.00 17.98  ? 63  TYR   A OH  1 
ATOM   442  N  N   . TYR   A 1 58  ? 12.433 -1.390  20.375 1.00 14.48  ? 64  TYR   A N   1 
ATOM   443  C  CA  . TYR   A 1 58  ? 13.025 -1.532  21.713 1.00 15.75  ? 64  TYR   A CA  1 
ATOM   444  C  C   . TYR   A 1 58  ? 12.579 -0.355  22.570 1.00 14.17  ? 64  TYR   A C   1 
ATOM   445  O  O   . TYR   A 1 58  ? 12.790 0.819   22.194 1.00 14.45  ? 64  TYR   A O   1 
ATOM   446  C  CB  . TYR   A 1 58  ? 14.537 -1.570  21.685 1.00 16.90  ? 64  TYR   A CB  1 
ATOM   447  C  CG  . TYR   A 1 58  ? 15.095 -1.743  23.068 1.00 17.98  ? 64  TYR   A CG  1 
ATOM   448  C  CD1 . TYR   A 1 58  ? 14.765 -2.875  23.811 1.00 19.61  ? 64  TYR   A CD1 1 
ATOM   449  C  CD2 . TYR   A 1 58  ? 15.910 -0.790  23.636 1.00 20.28  ? 64  TYR   A CD2 1 
ATOM   450  C  CE1 . TYR   A 1 58  ? 15.255 -3.048  25.096 1.00 23.69  ? 64  TYR   A CE1 1 
ATOM   451  C  CE2 . TYR   A 1 58  ? 16.424 -0.963  24.917 1.00 22.83  ? 64  TYR   A CE2 1 
ATOM   452  C  CZ  . TYR   A 1 58  ? 16.088 -2.093  25.639 1.00 25.75  ? 64  TYR   A CZ  1 
ATOM   453  O  OH  . TYR   A 1 58  ? 16.546 -2.258  26.917 1.00 25.50  ? 64  TYR   A OH  1 
ATOM   454  N  N   . CYS   A 1 59  ? 12.038 -0.687  23.744 1.00 15.20  ? 65  CYS   A N   1 
ATOM   455  C  CA  . CYS   A 1 59  ? 11.540 0.275   24.762 1.00 15.82  ? 65  CYS   A CA  1 
ATOM   456  C  C   . CYS   A 1 59  ? 12.423 0.180   26.011 1.00 15.80  ? 65  CYS   A C   1 
ATOM   457  O  O   . CYS   A 1 59  ? 12.202 -0.762  26.826 1.00 16.76  ? 65  CYS   A O   1 
ATOM   458  C  CB  . CYS   A 1 59  ? 10.087 -0.010  25.056 1.00 17.53  ? 65  CYS   A CB  1 
ATOM   459  S  SG  . CYS   A 1 59  ? 9.404  1.078   26.337 1.00 18.36  ? 65  CYS   A SG  1 
ATOM   460  N  N   . SER   A 1 60  ? 13.370 1.104   26.143 1.00 16.54  ? 66  SER   A N   1 
ATOM   461  C  CA  . SER   A 1 60  ? 14.378 1.046   27.235 1.00 18.74  ? 66  SER   A CA  1 
ATOM   462  C  C   . SER   A 1 60  ? 13.665 1.170   28.592 1.00 19.62  ? 66  SER   A C   1 
ATOM   463  O  O   . SER   A 1 60  ? 14.189 0.562   29.579 1.00 22.07  ? 66  SER   A O   1 
ATOM   464  C  CB  . SER   A 1 60  ? 15.458 2.097   27.097 1.00 20.54  ? 66  SER   A CB  1 
ATOM   465  O  OG  . SER   A 1 60  ? 14.999 3.418   27.308 1.00 23.33  ? 66  SER   A OG  1 
ATOM   466  N  N   . SER   A 1 61  ? 12.558 1.900   28.649 1.00 17.50  ? 67  SER   A N   1 
ATOM   467  C  CA  . SER   A 1 61  ? 11.810 2.225   29.904 1.00 17.37  ? 67  SER   A CA  1 
ATOM   468  C  C   . SER   A 1 61  ? 11.005 0.982   30.368 1.00 19.57  ? 67  SER   A C   1 
ATOM   469  O  O   . SER   A 1 61  ? 10.404 1.033   31.461 1.00 20.23  ? 67  SER   A O   1 
ATOM   470  C  CB  . SER   A 1 61  ? 10.979 3.456   29.805 1.00 18.96  ? 67  SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 61  ? 9.892  3.298   28.874 1.00 18.40  ? 67  SER   A OG  1 
ATOM   472  N  N   . ARG   A 1 62  ? 11.040 -0.115  29.595 1.00 18.35  ? 68  ARG   A N   1 
ATOM   473  C  CA  . ARG   A 1 62  ? 10.440 -1.424  29.981 1.00 17.55  ? 68  ARG   A CA  1 
ATOM   474  C  C   . ARG   A 1 62  ? 11.443 -2.576  29.803 1.00 18.01  ? 68  ARG   A C   1 
ATOM   475  O  O   . ARG   A 1 62  ? 11.088 -3.725  30.100 1.00 20.74  ? 68  ARG   A O   1 
ATOM   476  C  CB  . ARG   A 1 62  ? 9.197  -1.687  29.124 1.00 17.45  ? 68  ARG   A CB  1 
ATOM   477  C  CG  . ARG   A 1 62  ? 8.052  -0.720  29.318 1.00 17.79  ? 68  ARG   A CG  1 
ATOM   478  C  CD  . ARG   A 1 62  ? 7.325  -0.969  30.641 1.00 19.52  ? 68  ARG   A CD  1 
ATOM   479  N  NE  . ARG   A 1 62  ? 6.234  -0.041  30.847 1.00 20.44  ? 68  ARG   A NE  1 
ATOM   480  C  CZ  . ARG   A 1 62  ? 6.327  1.149   31.436 1.00 18.75  ? 68  ARG   A CZ  1 
ATOM   481  N  NH1 . ARG   A 1 62  ? 7.468  1.569   31.980 1.00 20.29  ? 68  ARG   A NH1 1 
ATOM   482  N  NH2 . ARG   A 1 62  ? 5.255  1.898   31.580 1.00 21.20  ? 68  ARG   A NH2 1 
ATOM   483  N  N   . ARG   A 1 63  ? 12.680 -2.308  29.356 1.00 19.25  ? 69  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 63  ? 13.653 -3.361  28.973 1.00 22.03  ? 69  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 63  ? 12.966 -4.421  28.106 1.00 21.26  ? 69  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 63  ? 13.202 -5.629  28.299 1.00 23.57  ? 69  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 63  ? 14.311 -3.971  30.215 1.00 24.85  ? 69  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 63  ? 15.082 -2.952  31.033 1.00 25.04  ? 69  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 63  ? 15.818 -3.602  32.185 1.00 27.49  ? 69  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 63  ? 16.577 -2.685  33.041 1.00 29.40  ? 69  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 63  ? 16.355 -2.510  34.362 1.00 28.52  ? 69  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 63  ? 15.357 -3.135  34.965 1.00 28.75  ? 69  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 63  ? 17.082 -1.652  35.069 1.00 25.40  ? 69  ARG   A NH2 1 
ATOM   494  N  N   . LYS   A 1 64  ? 12.144 -3.986  27.141 1.00 21.20  ? 70  LYS   A N   1 
ATOM   495  C  CA  . LYS   A 1 64  ? 11.345 -4.934  26.319 1.00 23.10  ? 70  LYS   A CA  1 
ATOM   496  C  C   . LYS   A 1 64  ? 11.333 -4.475  24.850 1.00 19.67  ? 70  LYS   A C   1 
ATOM   497  O  O   . LYS   A 1 64  ? 11.297 -3.236  24.603 1.00 19.46  ? 70  LYS   A O   1 
ATOM   498  C  CB  . LYS   A 1 64  ? 9.904  -5.043  26.840 1.00 26.80  ? 70  LYS   A CB  1 
ATOM   499  C  CG  . LYS   A 1 64  ? 9.674  -6.156  27.865 1.00 39.08  ? 70  LYS   A CG  1 
ATOM   500  C  CD  . LYS   A 1 64  ? 8.248  -6.705  27.853 1.00 42.12  ? 70  LYS   A CD  1 
ATOM   501  C  CE  . LYS   A 1 64  ? 7.961  -7.631  29.023 1.00 53.13  ? 70  LYS   A CE  1 
ATOM   502  N  NZ  . LYS   A 1 64  ? 7.979  -6.913  30.322 1.00 54.65  ? 70  LYS   A NZ  1 
ATOM   503  N  N   . HIS   A 1 65  ? 11.282 -5.459  23.943 1.00 18.10  ? 71  HIS   A N   1 
ATOM   504  C  CA  . HIS   A 1 65  ? 10.961 -5.230  22.527 1.00 17.10  ? 71  HIS   A CA  1 
ATOM   505  C  C   . HIS   A 1 65  ? 9.483  -5.528  22.388 1.00 18.35  ? 71  HIS   A C   1 
ATOM   506  O  O   . HIS   A 1 65  ? 9.023  -6.605  22.853 1.00 20.82  ? 71  HIS   A O   1 
ATOM   507  C  CB  . HIS   A 1 65  ? 11.820 -6.099  21.594 1.00 16.78  ? 71  HIS   A CB  1 
ATOM   508  C  CG  . HIS   A 1 65  ? 13.295 -5.857  21.652 1.00 17.10  ? 71  HIS   A CG  1 
ATOM   509  N  ND1 . HIS   A 1 65  ? 14.018 -5.163  20.673 1.00 18.84  ? 71  HIS   A ND1 1 
ATOM   510  C  CD2 . HIS   A 1 65  ? 14.192 -6.209  22.592 1.00 18.66  ? 71  HIS   A CD2 1 
ATOM   511  C  CE1 . HIS   A 1 65  ? 15.293 -5.108  21.053 1.00 17.39  ? 71  HIS   A CE1 1 
ATOM   512  N  NE2 . HIS   A 1 65  ? 15.412 -5.755  22.171 1.00 21.86  ? 71  HIS   A NE2 1 
ATOM   513  N  N   . TYR   A 1 66  ? 8.779  -4.682  21.655 1.00 17.18  ? 72  TYR   A N   1 
ATOM   514  C  CA  . TYR   A 1 66  ? 7.326  -4.820  21.414 1.00 16.97  ? 72  TYR   A CA  1 
ATOM   515  C  C   . TYR   A 1 66  ? 7.035  -4.873  19.929 1.00 15.60  ? 72  TYR   A C   1 
ATOM   516  O  O   . TYR   A 1 66  ? 7.454  -3.992  19.162 1.00 16.44  ? 72  TYR   A O   1 
ATOM   517  C  CB  . TYR   A 1 66  ? 6.542  -3.642  21.982 1.00 17.16  ? 72  TYR   A CB  1 
ATOM   518  C  CG  . TYR   A 1 66  ? 6.536  -3.495  23.485 1.00 19.32  ? 72  TYR   A CG  1 
ATOM   519  C  CD1 . TYR   A 1 66  ? 5.751  -4.327  24.267 1.00 21.43  ? 72  TYR   A CD1 1 
ATOM   520  C  CD2 . TYR   A 1 66  ? 7.344  -2.568  24.123 1.00 21.40  ? 72  TYR   A CD2 1 
ATOM   521  C  CE1 . TYR   A 1 66  ? 5.709  -4.189  25.646 1.00 22.56  ? 72  TYR   A CE1 1 
ATOM   522  C  CE2 . TYR   A 1 66  ? 7.301  -2.411  25.503 1.00 20.97  ? 72  TYR   A CE2 1 
ATOM   523  C  CZ  . TYR   A 1 66  ? 6.497  -3.242  26.263 1.00 23.55  ? 72  TYR   A CZ  1 
ATOM   524  O  OH  . TYR   A 1 66  ? 6.413  -3.117  27.630 1.00 24.10  ? 72  TYR   A OH  1 
ATOM   525  N  N   . PRO   A 1 67  ? 6.149  -5.796  19.496 1.00 15.87  ? 73  PRO   A N   1 
ATOM   526  C  CA  . PRO   A 1 67  ? 5.672  -5.805  18.116 1.00 16.57  ? 73  PRO   A CA  1 
ATOM   527  C  C   . PRO   A 1 67  ? 4.584  -4.756  17.907 1.00 17.35  ? 73  PRO   A C   1 
ATOM   528  O  O   . PRO   A 1 67  ? 3.747  -4.606  18.793 1.00 18.18  ? 73  PRO   A O   1 
ATOM   529  C  CB  . PRO   A 1 67  ? 5.143  -7.240  17.895 1.00 18.15  ? 73  PRO   A CB  1 
ATOM   530  C  CG  . PRO   A 1 67  ? 4.746  -7.682  19.270 1.00 19.24  ? 73  PRO   A CG  1 
ATOM   531  C  CD  . PRO   A 1 67  ? 5.714  -7.000  20.221 1.00 17.18  ? 73  PRO   A CD  1 
ATOM   532  N  N   . VAL   A 1 68  ? 4.721  -3.953  16.819 1.00 15.75  ? 74  VAL   A N   1 
ATOM   533  C  CA  . VAL   A 1 68  ? 3.777  -2.839  16.533 1.00 17.80  ? 74  VAL   A CA  1 
ATOM   534  C  C   . VAL   A 1 68  ? 3.398  -2.763  15.069 1.00 16.88  ? 74  VAL   A C   1 
ATOM   535  O  O   . VAL   A 1 68  ? 4.178  -3.138  14.180 1.00 16.02  ? 74  VAL   A O   1 
ATOM   536  C  CB  . VAL   A 1 68  ? 4.325  -1.486  16.997 1.00 19.50  ? 74  VAL   A CB  1 
ATOM   537  C  CG1 . VAL   A 1 68  ? 4.322  -1.408  18.515 1.00 19.84  ? 74  VAL   A CG1 1 
ATOM   538  C  CG2 . VAL   A 1 68  ? 5.689  -1.181  16.405 1.00 18.92  ? 74  VAL   A CG2 1 
ATOM   539  N  N   . SER   A 1 69  ? 2.201  -2.252  14.828 1.00 17.89  ? 75  SER   A N   1 
ATOM   540  C  CA  . SER   A 1 69  ? 1.814  -1.638  13.537 1.00 17.01  ? 75  SER   A CA  1 
ATOM   541  C  C   . SER   A 1 69  ? 2.086  -0.136  13.577 1.00 16.67  ? 75  SER   A C   1 
ATOM   542  O  O   . SER   A 1 69  ? 1.858  0.498   14.635 1.00 17.03  ? 75  SER   A O   1 
ATOM   543  C  CB  . SER   A 1 69  ? 0.362  -1.886  13.230 1.00 18.84  ? 75  SER   A CB  1 
ATOM   544  O  OG  . SER   A 1 69  ? 0.100  -3.268  13.221 1.00 24.40  ? 75  SER   A OG  1 
ATOM   545  N  N   . PHE   A 1 70  ? 2.585  0.475   12.481 1.00 15.53  ? 76  PHE   A N   1 
ATOM   546  C  CA  . PHE   A 1 70  ? 2.929  1.907   12.452 1.00 15.85  ? 76  PHE   A CA  1 
ATOM   547  C  C   . PHE   A 1 70  ? 2.467  2.567   11.151 1.00 15.81  ? 76  PHE   A C   1 
ATOM   548  O  O   . PHE   A 1 70  ? 2.359  1.865   10.134 1.00 18.64  ? 76  PHE   A O   1 
ATOM   549  C  CB  . PHE   A 1 70  ? 4.427  2.105   12.762 1.00 16.48  ? 76  PHE   A CB  1 
ATOM   550  C  CG  . PHE   A 1 70  ? 5.389  1.338   11.882 1.00 15.28  ? 76  PHE   A CG  1 
ATOM   551  C  CD1 . PHE   A 1 70  ? 5.818  0.065   12.204 1.00 15.52  ? 76  PHE   A CD1 1 
ATOM   552  C  CD2 . PHE   A 1 70  ? 5.891  1.921   10.716 1.00 15.68  ? 76  PHE   A CD2 1 
ATOM   553  C  CE1 . PHE   A 1 70  ? 6.694  -0.650  11.396 1.00 15.43  ? 76  PHE   A CE1 1 
ATOM   554  C  CE2 . PHE   A 1 70  ? 6.742  1.199   9.897  1.00 15.55  ? 76  PHE   A CE2 1 
ATOM   555  C  CZ  . PHE   A 1 70  ? 7.162  -0.060  10.250 1.00 16.83  ? 76  PHE   A CZ  1 
ATOM   556  N  N   . SER   A 1 71  ? 2.199  3.866   11.231 1.00 17.31  ? 77  SER   A N   1 
ATOM   557  C  CA  . SER   A 1 71  ? 1.793  4.657   10.043 1.00 19.04  ? 77  SER   A CA  1 
ATOM   558  C  C   . SER   A 1 71  ? 2.994  4.890   9.114  1.00 18.35  ? 77  SER   A C   1 
ATOM   559  O  O   . SER   A 1 71  ? 4.169  4.807   9.525  1.00 19.55  ? 77  SER   A O   1 
ATOM   560  C  CB  . SER   A 1 71  ? 1.140  5.924   10.478 1.00 19.97  ? 77  SER   A CB  1 
ATOM   561  O  OG  . SER   A 1 71  ? 2.048  6.715   11.208 1.00 22.34  ? 77  SER   A OG  1 
ATOM   562  N  N   . LYS   A 1 72  ? 2.722  5.197   7.848  1.00 19.80  ? 78  LYS   A N   1 
ATOM   563  C  CA  . LYS   A 1 72  ? 3.794  5.566   6.874  1.00 21.24  ? 78  LYS   A CA  1 
ATOM   564  C  C   . LYS   A 1 72  ? 4.357  6.927   7.265  1.00 20.36  ? 78  LYS   A C   1 
ATOM   565  O  O   . LYS   A 1 72  ? 3.704  7.718   7.921  1.00 20.00  ? 78  LYS   A O   1 
ATOM   566  C  CB  . LYS   A 1 72  ? 3.170  5.524   5.481  1.00 23.02  ? 78  LYS   A CB  1 
ATOM   567  C  CG  . LYS   A 1 72  ? 2.836  4.144   4.982  1.00 23.73  ? 78  LYS   A CG  1 
ATOM   568  C  CD  . LYS   A 1 72  ? 2.212  4.143   3.608  1.00 30.19  ? 78  LYS   A CD  1 
ATOM   569  C  CE  . LYS   A 1 72  ? 2.141  2.768   2.998  1.00 33.32  ? 78  LYS   A CE  1 
ATOM   570  N  NZ  . LYS   A 1 72  ? 1.841  2.872   1.543  1.00 39.02  ? 78  LYS   A NZ  1 
ATOM   571  N  N   . PRO   A 1 73  ? 5.658  7.193   6.966  1.00 20.94  ? 79  PRO   A N   1 
ATOM   572  C  CA  . PRO   A 1 73  ? 6.310  8.445   7.351  1.00 22.31  ? 79  PRO   A CA  1 
ATOM   573  C  C   . PRO   A 1 73  ? 5.509  9.640   6.821  1.00 21.62  ? 79  PRO   A C   1 
ATOM   574  O  O   . PRO   A 1 73  ? 5.172  9.634   5.633  1.00 24.67  ? 79  PRO   A O   1 
ATOM   575  C  CB  . PRO   A 1 73  ? 7.683  8.381   6.655  1.00 21.08  ? 79  PRO   A CB  1 
ATOM   576  C  CG  . PRO   A 1 73  ? 7.924  6.917   6.478  1.00 22.56  ? 79  PRO   A CG  1 
ATOM   577  C  CD  . PRO   A 1 73  ? 6.550  6.298   6.231  1.00 21.34  ? 79  PRO   A CD  1 
ATOM   578  N  N   . SER   A 1 74  ? 5.296  10.636  7.716  0.41 20.47  ? 80  SER   A N   1 
ATOM   579  C  CA  . SER   A 1 74  ? 4.370  11.821  7.610  0.41 20.96  ? 80  SER   A CA  1 
ATOM   580  C  C   . SER   A 1 74  ? 4.770  13.059  8.452  0.41 19.31  ? 80  SER   A C   1 
ATOM   581  O  O   . SER   A 1 74  ? 5.742  13.004  9.257  0.41 17.17  ? 80  SER   A O   1 
ATOM   582  C  CB  . SER   A 1 74  ? 2.956  11.410  7.987  0.41 21.71  ? 80  SER   A CB  1 
ATOM   583  O  OG  . SER   A 1 74  ? 2.615  10.161  7.415  0.41 23.49  ? 80  SER   A OG  1 
ATOM   584  N  N   . LEU   A 1 75  ? 4.040  14.184  8.279  0.41 17.10  ? 81  LEU   A N   1 
ATOM   585  C  CA  . LEU   A 1 75  ? 4.214  15.453  9.048  0.41 17.35  ? 81  LEU   A CA  1 
ATOM   586  C  C   . LEU   A 1 75  ? 3.221  15.485  10.218 0.41 17.08  ? 81  LEU   A C   1 
ATOM   587  O  O   . LEU   A 1 75  ? 2.002  15.549  9.962  0.41 16.18  ? 81  LEU   A O   1 
ATOM   588  C  CB  . LEU   A 1 75  ? 4.025  16.667  8.122  0.41 19.28  ? 81  LEU   A CB  1 
ATOM   589  C  CG  . LEU   A 1 75  ? 4.219  18.038  8.776  0.41 20.11  ? 81  LEU   A CG  1 
ATOM   590  C  CD1 . LEU   A 1 75  ? 5.658  18.242  9.230  0.41 20.04  ? 81  LEU   A CD1 1 
ATOM   591  C  CD2 . LEU   A 1 75  ? 3.794  19.158  7.840  0.41 21.26  ? 81  LEU   A CD2 1 
ATOM   592  N  N   . ILE   A 1 76  ? 3.738  15.554  11.439 0.41 16.02  ? 82  ILE   A N   1 
ATOM   593  C  CA  . ILE   A 1 76  ? 2.977  15.264  12.688 0.41 17.06  ? 82  ILE   A CA  1 
ATOM   594  C  C   . ILE   A 1 76  ? 3.222  16.366  13.706 0.41 16.41  ? 82  ILE   A C   1 
ATOM   595  O  O   . ILE   A 1 76  ? 4.394  16.676  13.975 0.41 15.49  ? 82  ILE   A O   1 
ATOM   596  C  CB  . ILE   A 1 76  ? 3.378  13.875  13.225 0.41 17.95  ? 82  ILE   A CB  1 
ATOM   597  C  CG1 . ILE   A 1 76  ? 2.940  12.755  12.282 0.41 19.22  ? 82  ILE   A CG1 1 
ATOM   598  C  CG2 . ILE   A 1 76  ? 2.846  13.628  14.618 0.41 18.56  ? 82  ILE   A CG2 1 
ATOM   599  C  CD1 . ILE   A 1 76  ? 1.493  12.839  11.842 0.41 20.44  ? 82  ILE   A CD1 1 
ATOM   600  N  N   . PHE   A 1 77  ? 2.141  16.884  14.287 0.41 16.13  ? 83  PHE   A N   1 
ATOM   601  C  CA  . PHE   A 1 77  ? 2.221  17.795  15.443 0.41 16.81  ? 83  PHE   A CA  1 
ATOM   602  C  C   . PHE   A 1 77  ? 2.581  16.972  16.680 0.41 17.15  ? 83  PHE   A C   1 
ATOM   603  O  O   . PHE   A 1 77  ? 1.844  16.032  17.068 0.41 15.50  ? 83  PHE   A O   1 
ATOM   604  C  CB  . PHE   A 1 77  ? 0.929  18.584  15.655 0.41 19.36  ? 83  PHE   A CB  1 
ATOM   605  C  CG  . PHE   A 1 77  ? 1.049  19.599  16.757 0.41 20.01  ? 83  PHE   A CG  1 
ATOM   606  C  CD1 . PHE   A 1 77  ? 1.812  20.737  16.575 0.41 19.99  ? 83  PHE   A CD1 1 
ATOM   607  C  CD2 . PHE   A 1 77  ? 0.434  19.406  17.986 0.41 18.82  ? 83  PHE   A CD2 1 
ATOM   608  C  CE1 . PHE   A 1 77  ? 1.955  21.664  17.598 0.41 19.64  ? 83  PHE   A CE1 1 
ATOM   609  C  CE2 . PHE   A 1 77  ? 0.583  20.331  19.008 0.41 19.45  ? 83  PHE   A CE2 1 
ATOM   610  C  CZ  . PHE   A 1 77  ? 1.337  21.459  18.807 0.41 18.95  ? 83  PHE   A CZ  1 
ATOM   611  N  N   . VAL   A 1 78  ? 3.733  17.296  17.253 0.41 16.50  ? 84  VAL   A N   1 
ATOM   612  C  CA  . VAL   A 1 78  ? 4.189  16.765  18.564 0.41 18.25  ? 84  VAL   A CA  1 
ATOM   613  C  C   . VAL   A 1 78  ? 3.760  17.737  19.666 0.41 22.50  ? 84  VAL   A C   1 
ATOM   614  O  O   . VAL   A 1 78  ? 4.463  18.754  19.931 0.41 18.56  ? 84  VAL   A O   1 
ATOM   615  C  CB  . VAL   A 1 78  ? 5.703  16.513  18.564 0.41 17.66  ? 84  VAL   A CB  1 
ATOM   616  C  CG1 . VAL   A 1 78  ? 6.167  15.887  19.871 0.41 17.62  ? 84  VAL   A CG1 1 
ATOM   617  C  CG2 . VAL   A 1 78  ? 6.095  15.661  17.377 0.41 17.07  ? 84  VAL   A CG2 1 
ATOM   618  N  N   . GLU   A 1 79  ? 2.619  17.441  20.283 0.41 23.78  ? 85  GLU   A N   1 
ATOM   619  C  CA  . GLU   A 1 79  ? 2.115  18.254  21.410 0.41 24.57  ? 85  GLU   A CA  1 
ATOM   620  C  C   . GLU   A 1 79  ? 3.312  18.553  22.301 0.41 24.67  ? 85  GLU   A C   1 
ATOM   621  O  O   . GLU   A 1 79  ? 4.189  17.643  22.487 0.41 23.79  ? 85  GLU   A O   1 
ATOM   622  C  CB  . GLU   A 1 79  ? 1.015  17.534  22.185 0.41 25.76  ? 85  GLU   A CB  1 
ATOM   623  C  CG  . GLU   A 1 79  ? -0.233 17.288  21.374 0.41 28.70  ? 85  GLU   A CG  1 
ATOM   624  C  CD  . GLU   A 1 79  ? -1.055 18.518  21.012 0.41 26.17  ? 85  GLU   A CD  1 
ATOM   625  O  OE1 . GLU   A 1 79  ? -0.995 19.528  21.753 0.41 29.37  ? 85  GLU   A OE1 1 
ATOM   626  O  OE2 . GLU   A 1 79  ? -1.726 18.474  19.975 0.41 27.28  ? 85  GLU   A OE2 1 
ATOM   627  N  N   . ALA   A 1 80  ? 3.369  19.786  22.807 0.41 22.81  ? 86  ALA   A N   1 
ATOM   628  C  CA  . ALA   A 1 80  ? 4.294  20.155  23.891 0.41 25.18  ? 86  ALA   A CA  1 
ATOM   629  C  C   . ALA   A 1 80  ? 4.409  18.948  24.815 0.41 25.21  ? 86  ALA   A C   1 
ATOM   630  O  O   . ALA   A 1 80  ? 3.382  18.259  25.046 0.41 26.73  ? 86  ALA   A O   1 
ATOM   631  C  CB  . ALA   A 1 80  ? 3.821  21.391  24.624 0.41 25.13  ? 86  ALA   A CB  1 
ATOM   632  N  N   . SER   A 1 81  ? 5.632  18.656  25.244 0.41 27.40  ? 87  SER   A N   1 
ATOM   633  C  CA  . SER   A 1 81  ? 5.964  17.740  26.359 0.41 24.88  ? 87  SER   A CA  1 
ATOM   634  C  C   . SER   A 1 81  ? 6.475  18.598  27.515 0.41 27.17  ? 87  SER   A C   1 
ATOM   635  O  O   . SER   A 1 81  ? 6.590  19.847  27.351 0.41 24.58  ? 87  SER   A O   1 
ATOM   636  C  CB  . SER   A 1 81  ? 6.979  16.691  25.911 0.41 24.63  ? 87  SER   A CB  1 
ATOM   637  O  OG  . SER   A 1 81  ? 7.849  16.304  26.970 0.41 27.08  ? 87  SER   A OG  1 
ATOM   638  N  N   . GLU   A 1 82  ? 6.740  17.975  28.657 0.41 25.75  ? 88  GLU   A N   1 
ATOM   639  C  CA  . GLU   A 1 82  ? 7.296  18.691  29.822 0.41 26.97  ? 88  GLU   A CA  1 
ATOM   640  C  C   . GLU   A 1 82  ? 8.572  19.438  29.413 0.41 27.67  ? 88  GLU   A C   1 
ATOM   641  O  O   . GLU   A 1 82  ? 8.784  20.532  29.948 0.41 27.01  ? 88  GLU   A O   1 
ATOM   642  C  CB  . GLU   A 1 82  ? 7.558  17.719  30.969 0.41 24.96  ? 88  GLU   A CB  1 
ATOM   643  C  CG  . GLU   A 1 82  ? 7.970  18.399  32.258 0.41 26.14  ? 88  GLU   A CG  1 
ATOM   644  C  CD  . GLU   A 1 82  ? 8.254  17.421  33.385 0.41 25.38  ? 88  GLU   A CD  1 
ATOM   645  O  OE1 . GLU   A 1 82  ? 8.660  17.862  34.474 0.41 27.83  ? 88  GLU   A OE1 1 
ATOM   646  O  OE2 . GLU   A 1 82  ? 8.088  16.215  33.149 0.41 28.11  ? 88  GLU   A OE2 1 
ATOM   647  N  N   . TYR   A 1 83  ? 9.385  18.892  28.499 0.41 25.51  ? 89  TYR   A N   1 
ATOM   648  C  CA  . TYR   A 1 83  ? 10.753 19.410  28.211 0.41 26.51  ? 89  TYR   A CA  1 
ATOM   649  C  C   . TYR   A 1 83  ? 10.902 19.893  26.762 0.41 25.91  ? 89  TYR   A C   1 
ATOM   650  O  O   . TYR   A 1 83  ? 11.910 20.556  26.459 0.41 26.39  ? 89  TYR   A O   1 
ATOM   651  C  CB  . TYR   A 1 83  ? 11.807 18.358  28.548 0.41 27.69  ? 89  TYR   A CB  1 
ATOM   652  C  CG  . TYR   A 1 83  ? 11.810 17.965  30.002 0.41 29.10  ? 89  TYR   A CG  1 
ATOM   653  C  CD1 . TYR   A 1 83  ? 12.400 18.779  30.958 0.41 31.25  ? 89  TYR   A CD1 1 
ATOM   654  C  CD2 . TYR   A 1 83  ? 11.208 16.789  30.432 0.41 31.44  ? 89  TYR   A CD2 1 
ATOM   655  C  CE1 . TYR   A 1 83  ? 12.409 18.429  32.301 0.41 31.62  ? 89  TYR   A CE1 1 
ATOM   656  C  CE2 . TYR   A 1 83  ? 11.208 16.427  31.771 0.41 32.33  ? 89  TYR   A CE2 1 
ATOM   657  C  CZ  . TYR   A 1 83  ? 11.810 17.249  32.710 0.41 33.41  ? 89  TYR   A CZ  1 
ATOM   658  O  OH  . TYR   A 1 83  ? 11.816 16.902  34.030 0.41 32.58  ? 89  TYR   A OH  1 
ATOM   659  N  N   . TYR   A 1 84  ? 9.942  19.610  25.894 0.41 22.95  ? 90  TYR   A N   1 
ATOM   660  C  CA  . TYR   A 1 84  ? 10.030 19.982  24.466 0.41 24.57  ? 90  TYR   A CA  1 
ATOM   661  C  C   . TYR   A 1 84  ? 8.763  20.747  24.085 0.41 23.96  ? 90  TYR   A C   1 
ATOM   662  O  O   . TYR   A 1 84  ? 7.643  20.298  24.344 0.41 23.12  ? 90  TYR   A O   1 
ATOM   663  C  CB  . TYR   A 1 84  ? 10.375 18.725  23.658 0.41 22.93  ? 90  TYR   A CB  1 
ATOM   664  C  CG  . TYR   A 1 84  ? 11.692 18.097  24.064 0.41 23.48  ? 90  TYR   A CG  1 
ATOM   665  C  CD1 . TYR   A 1 84  ? 12.876 18.508  23.484 0.41 24.10  ? 90  TYR   A CD1 1 
ATOM   666  C  CD2 . TYR   A 1 84  ? 11.774 17.121  25.048 0.41 22.83  ? 90  TYR   A CD2 1 
ATOM   667  C  CE1 . TYR   A 1 84  ? 14.099 17.979  23.861 0.41 22.96  ? 90  TYR   A CE1 1 
ATOM   668  C  CE2 . TYR   A 1 84  ? 12.987 16.568  25.433 0.41 24.89  ? 90  TYR   A CE2 1 
ATOM   669  C  CZ  . TYR   A 1 84  ? 14.161 17.011  24.841 0.41 23.19  ? 90  TYR   A CZ  1 
ATOM   670  O  OH  . TYR   A 1 84  ? 15.381 16.492  25.174 0.41 22.17  ? 90  TYR   A OH  1 
ATOM   671  N  N   . PRO   A 1 85  ? 8.913  21.926  23.443 0.41 23.95  ? 91  PRO   A N   1 
ATOM   672  C  CA  . PRO   A 1 85  ? 7.766  22.671  22.957 0.41 24.66  ? 91  PRO   A CA  1 
ATOM   673  C  C   . PRO   A 1 85  ? 7.052  21.830  21.903 0.41 24.50  ? 91  PRO   A C   1 
ATOM   674  O  O   . PRO   A 1 85  ? 7.635  20.878  21.329 0.41 21.11  ? 91  PRO   A O   1 
ATOM   675  C  CB  . PRO   A 1 85  ? 8.352  23.951  22.334 0.41 24.77  ? 91  PRO   A CB  1 
ATOM   676  C  CG  . PRO   A 1 85  ? 9.787  23.579  22.007 0.41 25.80  ? 91  PRO   A CG  1 
ATOM   677  C  CD  . PRO   A 1 85  ? 10.183 22.560  23.052 0.41 23.13  ? 91  PRO   A CD  1 
ATOM   678  N  N   . ALA   A 1 86  ? 5.793  22.176  21.695 0.41 26.17  ? 92  ALA   A N   1 
ATOM   679  C  CA  . ALA   A 1 86  ? 5.045  21.847  20.477 0.41 26.78  ? 92  ALA   A CA  1 
ATOM   680  C  C   . ALA   A 1 86  ? 5.954  22.120  19.276 0.41 27.98  ? 92  ALA   A C   1 
ATOM   681  O  O   . ALA   A 1 86  ? 6.592  23.209  19.222 0.41 25.86  ? 92  ALA   A O   1 
ATOM   682  C  CB  . ALA   A 1 86  ? 3.785  22.667  20.429 0.41 26.73  ? 92  ALA   A CB  1 
ATOM   683  N  N   . ARG   A 1 87  ? 6.092  21.142  18.390 0.41 24.40  ? 93  ARG   A N   1 
ATOM   684  C  CA  . ARG   A 1 87  ? 6.674  21.357  17.044 0.41 25.01  ? 93  ARG   A CA  1 
ATOM   685  C  C   . ARG   A 1 87  ? 6.154  20.289  16.095 0.41 24.24  ? 93  ARG   A C   1 
ATOM   686  O  O   . ARG   A 1 87  ? 5.703  19.234  16.601 0.41 25.74  ? 93  ARG   A O   1 
ATOM   687  C  CB  . ARG   A 1 87  ? 8.205  21.330  17.084 0.41 23.57  ? 93  ARG   A CB  1 
ATOM   688  C  CG  . ARG   A 1 87  ? 8.805  19.935  16.996 0.41 25.95  ? 93  ARG   A CG  1 
ATOM   689  C  CD  . ARG   A 1 87  ? 10.289 19.997  16.674 0.41 25.41  ? 93  ARG   A CD  1 
ATOM   690  N  NE  . ARG   A 1 87  ? 10.521 20.576  15.364 0.41 27.59  ? 93  ARG   A NE  1 
ATOM   691  C  CZ  . ARG   A 1 87  ? 11.627 21.219  14.997 0.41 26.42  ? 93  ARG   A CZ  1 
ATOM   692  N  NH1 . ARG   A 1 87  ? 12.622 21.401  15.848 0.41 28.97  ? 93  ARG   A NH1 1 
ATOM   693  N  NH2 . ARG   A 1 87  ? 11.716 21.705  13.772 0.41 28.98  ? 93  ARG   A NH2 1 
ATOM   694  N  N   . TYR   A 1 88  ? 6.231  20.569  14.793 0.41 23.76  ? 94  TYR   A N   1 
ATOM   695  C  CA  . TYR   A 1 88  ? 5.955  19.638  13.669 0.41 23.43  ? 94  TYR   A CA  1 
ATOM   696  C  C   . TYR   A 1 88  ? 7.215  18.903  13.204 0.41 22.50  ? 94  TYR   A C   1 
ATOM   697  O  O   . TYR   A 1 88  ? 8.008  19.494  12.414 0.41 24.11  ? 94  TYR   A O   1 
ATOM   698  C  CB  . TYR   A 1 88  ? 5.427  20.388  12.455 0.41 22.98  ? 94  TYR   A CB  1 
ATOM   699  C  CG  . TYR   A 1 88  ? 3.946  20.586  12.520 0.41 23.89  ? 94  TYR   A CG  1 
ATOM   700  C  CD1 . TYR   A 1 88  ? 3.097  19.560  12.155 0.41 23.46  ? 94  TYR   A CD1 1 
ATOM   701  C  CD2 . TYR   A 1 88  ? 3.401  21.752  13.026 0.41 24.38  ? 94  TYR   A CD2 1 
ATOM   702  C  CE1 . TYR   A 1 88  ? 1.725  19.701  12.240 0.41 24.41  ? 94  TYR   A CE1 1 
ATOM   703  C  CE2 . TYR   A 1 88  ? 2.029  21.911  13.103 0.41 25.14  ? 94  TYR   A CE2 1 
ATOM   704  C  CZ  . TYR   A 1 88  ? 1.189  20.880  12.720 0.41 25.29  ? 94  TYR   A CZ  1 
ATOM   705  O  OH  . TYR   A 1 88  ? -0.166 21.032  12.788 0.41 26.80  ? 94  TYR   A OH  1 
ATOM   706  N  N   . GLN   A 1 89  ? 7.378  17.642  13.624 0.41 18.97  ? 95  GLN   A N   1 
ATOM   707  C  CA  . GLN   A 1 89  ? 8.443  16.753  13.084 0.41 17.56  ? 95  GLN   A CA  1 
ATOM   708  C  C   . GLN   A 1 89  ? 7.918  16.117  11.787 0.41 16.50  ? 95  GLN   A C   1 
ATOM   709  O  O   . GLN   A 1 89  ? 6.695  15.841  11.774 0.41 17.26  ? 95  GLN   A O   1 
ATOM   710  C  CB  . GLN   A 1 89  ? 8.851  15.726  14.138 0.41 16.37  ? 95  GLN   A CB  1 
ATOM   711  C  CG  . GLN   A 1 89  ? 9.933  16.249  15.071 0.41 17.31  ? 95  GLN   A CG  1 
ATOM   712  C  CD  . GLN   A 1 89  ? 10.534 15.196  15.975 0.41 16.24  ? 95  GLN   A CD  1 
ATOM   713  O  OE1 . GLN   A 1 89  ? 10.909 15.456  17.113 0.41 17.57  ? 95  GLN   A OE1 1 
ATOM   714  N  NE2 . GLN   A 1 89  ? 10.642 13.982  15.467 0.41 16.30  ? 95  GLN   A NE2 1 
ATOM   715  N  N   . SER   A 1 90  ? 8.776  15.883  10.773 0.41 17.50  ? 96  SER   A N   1 
ATOM   716  C  CA  . SER   A 1 90  ? 8.469  15.295  9.426  0.41 17.48  ? 96  SER   A CA  1 
ATOM   717  C  C   . SER   A 1 90  ? 9.040  13.856  9.243  0.41 18.42  ? 96  SER   A C   1 
ATOM   718  O  O   . SER   A 1 90  ? 9.890  13.517  10.118 0.41 17.56  ? 96  SER   A O   1 
ATOM   719  C  CB  . SER   A 1 90  ? 9.043  16.202  8.374  0.41 18.12  ? 96  SER   A CB  1 
ATOM   720  O  OG  . SER   A 1 90  ? 10.413 16.435  8.669  0.41 18.64  ? 96  SER   A OG  1 
ATOM   721  N  N   . HIS   A 1 91  ? 8.717  13.078  8.168  1.00 20.14  ? 97  HIS   A N   1 
ATOM   722  C  CA  . HIS   A 1 91  ? 9.239  11.686  8.049  1.00 19.64  ? 97  HIS   A CA  1 
ATOM   723  C  C   . HIS   A 1 91  ? 8.994  10.912  9.375  1.00 21.66  ? 97  HIS   A C   1 
ATOM   724  O  O   . HIS   A 1 91  ? 9.871  10.107  9.796  1.00 20.22  ? 97  HIS   A O   1 
ATOM   725  C  CB  . HIS   A 1 91  ? 10.710 11.734  7.644  1.00 23.29  ? 97  HIS   A CB  1 
ATOM   726  C  CG  . HIS   A 1 91  ? 10.909 12.433  6.336  1.00 22.26  ? 97  HIS   A CG  1 
ATOM   727  N  ND1 . HIS   A 1 91  ? 10.960 11.759  5.165  1.00 22.44  ? 97  HIS   A ND1 1 
ATOM   728  C  CD2 . HIS   A 1 91  ? 11.067 13.747  6.021  1.00 22.21  ? 97  HIS   A CD2 1 
ATOM   729  C  CE1 . HIS   A 1 91  ? 11.191 12.623  4.175  1.00 22.60  ? 97  HIS   A CE1 1 
ATOM   730  N  NE2 . HIS   A 1 91  ? 11.181 13.825  4.653  1.00 23.63  ? 97  HIS   A NE2 1 
ATOM   731  N  N   . LEU   A 1 92  ? 7.895  11.199  10.034 1.00 20.31  ? 98  LEU   A N   1 
ATOM   732  C  CA  . LEU   A 1 92  ? 7.560  10.572  11.337 1.00 17.16  ? 98  LEU   A CA  1 
ATOM   733  C  C   . LEU   A 1 92  ? 6.497  9.477   11.167 1.00 18.23  ? 98  LEU   A C   1 
ATOM   734  O  O   . LEU   A 1 92  ? 5.522  9.679   10.438 1.00 20.09  ? 98  LEU   A O   1 
ATOM   735  C  CB  . LEU   A 1 92  ? 7.094  11.610  12.364 1.00 19.26  ? 98  LEU   A CB  1 
ATOM   736  C  CG  . LEU   A 1 92  ? 6.913  11.137  13.799 1.00 18.87  ? 98  LEU   A CG  1 
ATOM   737  C  CD1 . LEU   A 1 92  ? 8.226  10.836  14.472 1.00 18.33  ? 98  LEU   A CD1 1 
ATOM   738  C  CD2 . LEU   A 1 92  ? 6.169  12.168  14.613 1.00 20.67  ? 98  LEU   A CD2 1 
ATOM   739  N  N   . MET   A 1 93  ? 6.709  8.356   11.846 1.00 16.47  ? 99  MET   A N   1 
ATOM   740  C  CA  . MET   A 1 93  ? 5.793  7.170   11.855 1.00 16.80  ? 99  MET   A CA  1 
ATOM   741  C  C   . MET   A 1 93  ? 5.238  7.014   13.259 1.00 15.90  ? 99  MET   A C   1 
ATOM   742  O  O   . MET   A 1 93  ? 6.020  7.091   14.236 1.00 17.63  ? 99  MET   A O   1 
ATOM   743  C  CB  . MET   A 1 93  ? 6.514  5.882   11.453 1.00 15.27  ? 99  MET   A CB  1 
ATOM   744  C  CG  . MET   A 1 93  ? 7.107  5.963   10.063 1.00 17.82  ? 99  MET   A CG  1 
ATOM   745  S  SD  . MET   A 1 93  ? 8.213  4.674   9.637  1.00 17.96  ? 99  MET   A SD  1 
ATOM   746  C  CE  . MET   A 1 93  ? 9.646  4.921   10.680 1.00 15.04  ? 99  MET   A CE  1 
ATOM   747  N  N   . LEU   A 1 94  ? 3.932  6.795   13.410 1.00 17.55  ? 100 LEU   A N   1 
ATOM   748  C  CA  . LEU   A 1 94  ? 3.330  6.610   14.770 1.00 16.90  ? 100 LEU   A CA  1 
ATOM   749  C  C   . LEU   A 1 94  ? 2.829  5.164   14.973 1.00 18.91  ? 100 LEU   A C   1 
ATOM   750  O  O   . LEU   A 1 94  ? 2.341  4.529   14.019 1.00 17.47  ? 100 LEU   A O   1 
ATOM   751  C  CB  . LEU   A 1 94  ? 2.148  7.561   14.999 1.00 21.13  ? 100 LEU   A CB  1 
ATOM   752  C  CG  . LEU   A 1 94  ? 2.489  9.043   15.081 1.00 22.28  ? 100 LEU   A CG  1 
ATOM   753  C  CD1 . LEU   A 1 94  ? 1.218  9.896   15.041 1.00 25.86  ? 100 LEU   A CD1 1 
ATOM   754  C  CD2 . LEU   A 1 94  ? 3.298  9.358   16.331 1.00 24.74  ? 100 LEU   A CD2 1 
ATOM   755  N  N   . ALA   A 1 95  ? 2.920  4.679   16.207 1.00 16.58  ? 101 ALA   A N   1 
ATOM   756  C  CA  . ALA   A 1 95  ? 2.343  3.395   16.667 1.00 16.67  ? 101 ALA   A CA  1 
ATOM   757  C  C   . ALA   A 1 95  ? 1.703  3.596   18.036 1.00 16.66  ? 101 ALA   A C   1 
ATOM   758  O  O   . ALA   A 1 95  ? 2.052  4.534   18.748 1.00 17.35  ? 101 ALA   A O   1 
ATOM   759  C  CB  . ALA   A 1 95  ? 3.389  2.296   16.783 1.00 16.70  ? 101 ALA   A CB  1 
ATOM   760  N  N   . VAL   A 1 96  ? 0.829  2.672   18.409 1.00 16.62  ? 102 VAL   A N   1 
ATOM   761  C  CA  . VAL   A 1 96  ? 0.244  2.621   19.774 1.00 16.09  ? 102 VAL   A CA  1 
ATOM   762  C  C   . VAL   A 1 96  ? 1.244  1.845   20.594 1.00 14.75  ? 102 VAL   A C   1 
ATOM   763  O  O   . VAL   A 1 96  ? 1.536  0.661   20.285 1.00 16.78  ? 102 VAL   A O   1 
ATOM   764  C  CB  . VAL   A 1 96  ? -1.134 1.971   19.787 1.00 15.45  ? 102 VAL   A CB  1 
ATOM   765  C  CG1 . VAL   A 1 96  ? -1.656 1.811   21.209 1.00 17.08  ? 102 VAL   A CG1 1 
ATOM   766  C  CG2 . VAL   A 1 96  ? -2.073 2.771   18.929 1.00 16.36  ? 102 VAL   A CG2 1 
ATOM   767  N  N   . GLY   A 1 97  ? 1.771  2.477   21.627 0.41 15.58  ? 103 GLY   A N   1 
ATOM   768  C  CA  . GLY   A 1 97  ? 2.591  1.732   22.582 0.41 15.33  ? 103 GLY   A CA  1 
ATOM   769  C  C   . GLY   A 1 97  ? 3.236  2.625   23.599 0.41 15.62  ? 103 GLY   A C   1 
ATOM   770  O  O   . GLY   A 1 97  ? 2.936  3.815   23.656 0.41 15.14  ? 103 GLY   A O   1 
ATOM   771  N  N   . HIS   A 1 98  ? 4.095  2.029   24.417 0.41 14.43  ? 104 HIS   A N   1 
ATOM   772  C  CA  . HIS   A 1 98  ? 4.708  2.738   25.554 0.41 13.80  ? 104 HIS   A CA  1 
ATOM   773  C  C   . HIS   A 1 98  ? 6.025  3.402   25.135 0.41 13.05  ? 104 HIS   A C   1 
ATOM   774  O  O   . HIS   A 1 98  ? 6.865  2.740   24.487 0.41 13.41  ? 104 HIS   A O   1 
ATOM   775  C  CB  . HIS   A 1 98  ? 4.933  1.810   26.737 0.41 14.04  ? 104 HIS   A CB  1 
ATOM   776  C  CG  . HIS   A 1 98  ? 5.559  2.567   27.849 0.41 13.67  ? 104 HIS   A CG  1 
ATOM   777  N  ND1 . HIS   A 1 98  ? 4.874  3.538   28.541 0.41 13.31  ? 104 HIS   A ND1 1 
ATOM   778  C  CD2 . HIS   A 1 98  ? 6.809  2.535   28.353 0.41 13.39  ? 104 HIS   A CD2 1 
ATOM   779  C  CE1 . HIS   A 1 98  ? 5.680  4.093   29.410 0.41 13.33  ? 104 HIS   A CE1 1 
ATOM   780  N  NE2 . HIS   A 1 98  ? 6.882  3.492   29.331 0.41 13.52  ? 104 HIS   A NE2 1 
ATOM   781  N  N   . SER   A 1 99  ? 6.219  4.654   25.537 0.41 12.35  ? 105 SER   A N   1 
ATOM   782  C  CA  . SER   A 1 99  ? 7.520  5.359   25.399 0.41 12.10  ? 105 SER   A CA  1 
ATOM   783  C  C   . SER   A 1 99  ? 7.636  6.460   26.450 0.41 13.40  ? 105 SER   A C   1 
ATOM   784  O  O   . SER   A 1 99  ? 6.599  6.977   26.913 0.41 14.85  ? 105 SER   A O   1 
ATOM   785  C  CB  . SER   A 1 99  ? 7.729  5.899   23.985 0.41 9.99   ? 105 SER   A CB  1 
ATOM   786  O  OG  . SER   A 1 99  ? 6.849  6.992   23.672 0.41 9.38   ? 105 SER   A OG  1 
ATOM   787  N  N   . GLU   A 1 100 ? 8.880  6.757   26.812 0.41 16.25  ? 106 GLU   A N   1 
ATOM   788  C  CA  . GLU   A 1 100 ? 9.314  7.857   27.698 0.41 18.12  ? 106 GLU   A CA  1 
ATOM   789  C  C   . GLU   A 1 100 ? 10.572 8.434   27.055 0.41 18.90  ? 106 GLU   A C   1 
ATOM   790  O  O   . GLU   A 1 100 ? 11.154 7.800   26.165 0.41 16.42  ? 106 GLU   A O   1 
ATOM   791  C  CB  . GLU   A 1 100 ? 9.548  7.329   29.113 0.41 19.87  ? 106 GLU   A CB  1 
ATOM   792  C  CG  . GLU   A 1 100 ? 8.279  6.818   29.782 0.41 20.41  ? 106 GLU   A CG  1 
ATOM   793  C  CD  . GLU   A 1 100 ? 8.466  6.337   31.207 0.41 19.30  ? 106 GLU   A CD  1 
ATOM   794  O  OE1 . GLU   A 1 100 ? 9.118  7.043   31.973 0.41 19.27  ? 106 GLU   A OE1 1 
ATOM   795  O  OE2 . GLU   A 1 100 ? 7.954  5.275   31.531 0.41 21.92  ? 106 GLU   A OE2 1 
ATOM   796  N  N   . PRO   A 1 101 ? 11.023 9.640   27.465 0.41 17.48  ? 107 PRO   A N   1 
ATOM   797  C  CA  . PRO   A 1 101 ? 12.100 10.321  26.745 0.41 17.44  ? 107 PRO   A CA  1 
ATOM   798  C  C   . PRO   A 1 101 ? 13.390 9.531   26.483 0.41 16.40  ? 107 PRO   A C   1 
ATOM   799  O  O   . PRO   A 1 101 ? 13.889 9.587   25.344 0.41 15.95  ? 107 PRO   A O   1 
ATOM   800  C  CB  . PRO   A 1 101 ? 12.447 11.502  27.656 0.41 17.70  ? 107 PRO   A CB  1 
ATOM   801  C  CG  . PRO   A 1 101 ? 11.148 11.780  28.392 0.41 18.20  ? 107 PRO   A CG  1 
ATOM   802  C  CD  . PRO   A 1 101 ? 10.511 10.423  28.608 0.41 18.68  ? 107 PRO   A CD  1 
ATOM   803  N  N   . GLY   A 1 102 ? 13.919 8.855   27.512 0.41 15.91  ? 108 GLY   A N   1 
ATOM   804  C  CA  . GLY   A 1 102 ? 15.168 8.074   27.411 0.41 16.74  ? 108 GLY   A CA  1 
ATOM   805  C  C   . GLY   A 1 102 ? 15.036 6.822   26.559 0.41 15.86  ? 108 GLY   A C   1 
ATOM   806  O  O   . GLY   A 1 102 ? 16.045 6.114   26.421 0.41 16.36  ? 108 GLY   A O   1 
ATOM   807  N  N   . ASP   A 1 103 ? 13.852 6.552   25.986 0.41 15.64  ? 109 ASP   A N   1 
ATOM   808  C  CA  . ASP   A 1 103 ? 13.689 5.590   24.865 0.41 15.51  ? 109 ASP   A CA  1 
ATOM   809  C  C   . ASP   A 1 103 ? 14.011 6.211   23.494 0.41 16.05  ? 109 ASP   A C   1 
ATOM   810  O  O   . ASP   A 1 103 ? 14.109 5.418   22.544 0.41 15.43  ? 109 ASP   A O   1 
ATOM   811  C  CB  . ASP   A 1 103 ? 12.263 5.038   24.807 0.41 15.96  ? 109 ASP   A CB  1 
ATOM   812  C  CG  . ASP   A 1 103 ? 11.875 4.268   26.052 0.41 16.94  ? 109 ASP   A CG  1 
ATOM   813  O  OD1 . ASP   A 1 103 ? 12.789 3.657   26.672 0.41 15.33  ? 109 ASP   A OD1 1 
ATOM   814  O  OD2 . ASP   A 1 103 ? 10.664 4.262   26.383 0.41 18.47  ? 109 ASP   A OD2 1 
ATOM   815  N  N   . CYS   A 1 104 ? 14.145 7.529   23.322 0.41 16.49  ? 110 CYS   A N   1 
ATOM   816  C  CA  . CYS   A 1 104 ? 14.605 8.075   22.011 0.41 16.62  ? 110 CYS   A CA  1 
ATOM   817  C  C   . CYS   A 1 104 ? 15.961 7.398   21.675 0.41 16.79  ? 110 CYS   A C   1 
ATOM   818  O  O   . CYS   A 1 104 ? 16.854 7.413   22.554 0.41 18.25  ? 110 CYS   A O   1 
ATOM   819  C  CB  . CYS   A 1 104 ? 14.662 9.607   22.031 0.41 17.43  ? 110 CYS   A CB  1 
ATOM   820  S  SG  . CYS   A 1 104 ? 13.085 10.484  21.769 0.41 19.68  ? 110 CYS   A SG  1 
ATOM   821  N  N   . GLY   A 1 105 ? 16.122 6.856   20.444 1.00 15.53  ? 111 GLY   A N   1 
ATOM   822  C  CA  . GLY   A 1 105 ? 17.269 6.103   19.939 1.00 14.99  ? 111 GLY   A CA  1 
ATOM   823  C  C   . GLY   A 1 105 ? 17.003 4.620   19.871 1.00 15.38  ? 111 GLY   A C   1 
ATOM   824  O  O   . GLY   A 1 105 ? 17.796 3.902   19.250 1.00 17.82  ? 111 GLY   A O   1 
ATOM   825  N  N   . GLY   A 1 106 ? 15.955 4.099   20.533 1.00 15.90  ? 112 GLY   A N   1 
ATOM   826  C  CA  . GLY   A 1 106 ? 15.592 2.682   20.386 1.00 16.49  ? 112 GLY   A CA  1 
ATOM   827  C  C   . GLY   A 1 106 ? 15.298 2.332   18.921 1.00 15.36  ? 112 GLY   A C   1 
ATOM   828  O  O   . GLY   A 1 106 ? 14.586 3.114   18.256 1.00 15.41  ? 112 GLY   A O   1 
ATOM   829  N  N   . ILE   A 1 107 ? 15.751 1.197   18.429 1.00 14.29  ? 113 ILE   A N   1 
ATOM   830  C  CA  . ILE   A 1 107 ? 15.500 0.800   17.009 1.00 14.45  ? 113 ILE   A CA  1 
ATOM   831  C  C   . ILE   A 1 107 ? 14.095 0.233   16.837 1.00 14.23  ? 113 ILE   A C   1 
ATOM   832  O  O   . ILE   A 1 107 ? 13.652 -0.660  17.630 1.00 13.64  ? 113 ILE   A O   1 
ATOM   833  C  CB  . ILE   A 1 107 ? 16.595 -0.170  16.558 1.00 17.71  ? 113 ILE   A CB  1 
ATOM   834  C  CG1 . ILE   A 1 107 ? 17.836 0.677   16.275 1.00 19.65  ? 113 ILE   A CG1 1 
ATOM   835  C  CG2 . ILE   A 1 107 ? 16.188 -0.963  15.315 1.00 17.21  ? 113 ILE   A CG2 1 
ATOM   836  C  CD1 . ILE   A 1 107 ? 19.083 -0.089  16.061 1.00 23.04  ? 113 ILE   A CD1 1 
ATOM   837  N  N   . LEU   A 1 108 ? 13.491 0.639   15.733 1.00 12.48  ? 114 LEU   A N   1 
ATOM   838  C  CA  . LEU   A 1 108 ? 12.348 -0.046  15.082 1.00 12.78  ? 114 LEU   A CA  1 
ATOM   839  C  C   . LEU   A 1 108 ? 12.907 -0.851  13.904 1.00 12.27  ? 114 LEU   A C   1 
ATOM   840  O  O   . LEU   A 1 108 ? 13.614 -0.224  13.078 1.00 13.72  ? 114 LEU   A O   1 
ATOM   841  C  CB  . LEU   A 1 108 ? 11.347 0.971   14.594 1.00 12.30  ? 114 LEU   A CB  1 
ATOM   842  C  CG  . LEU   A 1 108 ? 10.153 0.454   13.799 1.00 12.59  ? 114 LEU   A CG  1 
ATOM   843  C  CD1 . LEU   A 1 108 ? 9.249  -0.458  14.624 1.00 14.65  ? 114 LEU   A CD1 1 
ATOM   844  C  CD2 . LEU   A 1 108 ? 9.391  1.598   13.192 1.00 14.24  ? 114 LEU   A CD2 1 
ATOM   845  N  N   . ARG   A 1 109 ? 12.554 -2.134  13.817 1.00 13.01  ? 115 ARG   A N   1 
ATOM   846  C  CA  . ARG   A 1 109 ? 13.063 -3.081  12.787 1.00 13.17  ? 115 ARG   A CA  1 
ATOM   847  C  C   . ARG   A 1 109 ? 11.908 -3.864  12.153 1.00 15.19  ? 115 ARG   A C   1 
ATOM   848  O  O   . ARG   A 1 109 ? 10.948 -4.245  12.882 1.00 16.37  ? 115 ARG   A O   1 
ATOM   849  C  CB  . ARG   A 1 109 ? 14.208 -3.944  13.310 1.00 15.84  ? 115 ARG   A CB  1 
ATOM   850  C  CG  . ARG   A 1 109 ? 13.791 -4.908  14.402 1.00 17.33  ? 115 ARG   A CG  1 
ATOM   851  C  CD  . ARG   A 1 109 ? 14.970 -5.682  14.986 1.00 20.72  ? 115 ARG   A CD  1 
ATOM   852  N  NE  . ARG   A 1 109 ? 15.842 -4.921  15.853 1.00 25.93  ? 115 ARG   A NE  1 
ATOM   853  C  CZ  . ARG   A 1 109 ? 17.160 -4.734  15.683 1.00 29.86  ? 115 ARG   A CZ  1 
ATOM   854  N  NH1 . ARG   A 1 109 ? 17.791 -5.155  14.592 1.00 29.46  ? 115 ARG   A NH1 1 
ATOM   855  N  NH2 . ARG   A 1 109 ? 17.833 -4.035  16.580 1.00 31.66  ? 115 ARG   A NH2 1 
ATOM   856  N  N   . CYS   A 1 110 ? 12.065 -4.180  10.863 1.00 15.50  ? 116 CYS   A N   1 
ATOM   857  C  CA  . CYS   A 1 110 ? 11.128 -5.059  10.122 1.00 15.02  ? 116 CYS   A CA  1 
ATOM   858  C  C   . CYS   A 1 110 ? 11.924 -6.227  9.551  1.00 17.69  ? 116 CYS   A C   1 
ATOM   859  O  O   . CYS   A 1 110 ? 13.137 -6.380  9.826  1.00 19.64  ? 116 CYS   A O   1 
ATOM   860  C  CB  . CYS   A 1 110 ? 10.388 -4.295  9.040  1.00 17.06  ? 116 CYS   A CB  1 
ATOM   861  S  SG  . CYS   A 1 110 ? 11.497 -3.772  7.696  1.00 17.44  ? 116 CYS   A SG  1 
ATOM   862  N  N   . GLN   A 1 111 ? 11.256 -7.079  8.802  1.00 19.69  ? 117 GLN   A N   1 
ATOM   863  C  CA  . GLN   A 1 111 ? 11.939 -8.220  8.155  1.00 22.44  ? 117 GLN   A CA  1 
ATOM   864  C  C   . GLN   A 1 111 ? 13.138 -7.752  7.320  1.00 22.80  ? 117 GLN   A C   1 
ATOM   865  O  O   . GLN   A 1 111 ? 14.063 -8.564  7.188  1.00 27.65  ? 117 GLN   A O   1 
ATOM   866  C  CB  . GLN   A 1 111 ? 10.912 -9.033  7.366  1.00 24.29  ? 117 GLN   A CB  1 
ATOM   867  C  CG  . GLN   A 1 111 ? 10.438 -8.373  6.081  1.00 25.39  ? 117 GLN   A CG  1 
ATOM   868  C  CD  . GLN   A 1 111 ? 9.559  -9.313  5.307  1.00 32.59  ? 117 GLN   A CD  1 
ATOM   869  O  OE1 . GLN   A 1 111 ? 8.371  -9.432  5.587  1.00 37.69  ? 117 GLN   A OE1 1 
ATOM   870  N  NE2 . GLN   A 1 111 ? 10.149 -10.005 4.342  1.00 33.54  ? 117 GLN   A NE2 1 
ATOM   871  N  N   . HIS   A 1 112 ? 13.192 -6.508  6.823  1.00 20.47  ? 118 HIS   A N   1 
ATOM   872  C  CA  . HIS   A 1 112 ? 14.220 -6.022  5.851  1.00 20.44  ? 118 HIS   A CA  1 
ATOM   873  C  C   . HIS   A 1 112 ? 15.401 -5.349  6.566  1.00 23.23  ? 118 HIS   A C   1 
ATOM   874  O  O   . HIS   A 1 112 ? 16.370 -4.986  5.882  1.00 26.95  ? 118 HIS   A O   1 
ATOM   875  C  CB  . HIS   A 1 112 ? 13.561 -5.052  4.872  1.00 20.39  ? 118 HIS   A CB  1 
ATOM   876  C  CG  . HIS   A 1 112 ? 12.428 -5.644  4.094  1.00 21.34  ? 118 HIS   A CG  1 
ATOM   877  N  ND1 . HIS   A 1 112 ? 11.130 -5.323  4.351  1.00 20.96  ? 118 HIS   A ND1 1 
ATOM   878  C  CD2 . HIS   A 1 112 ? 12.408 -6.487  3.029  1.00 25.10  ? 118 HIS   A CD2 1 
ATOM   879  C  CE1 . HIS   A 1 112 ? 10.320 -6.016  3.548  1.00 24.01  ? 118 HIS   A CE1 1 
ATOM   880  N  NE2 . HIS   A 1 112 ? 11.097 -6.693  2.678  1.00 24.01  ? 118 HIS   A NE2 1 
ATOM   881  N  N   . GLY   A 1 113 ? 15.279 -5.074  7.872  1.00 19.13  ? 119 GLY   A N   1 
ATOM   882  C  CA  . GLY   A 1 113 ? 16.349 -4.395  8.631  1.00 19.54  ? 119 GLY   A CA  1 
ATOM   883  C  C   . GLY   A 1 113 ? 15.833 -3.232  9.484  1.00 19.62  ? 119 GLY   A C   1 
ATOM   884  O  O   . GLY   A 1 113 ? 14.649 -3.222  9.867  1.00 18.64  ? 119 GLY   A O   1 
ATOM   885  N  N   . VAL   A 1 114 ? 16.699 -2.250  9.742  1.00 16.25  ? 120 VAL   A N   1 
ATOM   886  C  CA  . VAL   A 1 114 ? 16.346 -1.087  10.590 1.00 15.68  ? 120 VAL   A CA  1 
ATOM   887  C  C   . VAL   A 1 114 ? 15.434 -0.136  9.815  1.00 15.77  ? 120 VAL   A C   1 
ATOM   888  O  O   . VAL   A 1 114 ? 15.797 0.349   8.688  1.00 16.75  ? 120 VAL   A O   1 
ATOM   889  C  CB  . VAL   A 1 114 ? 17.601 -0.374  11.124 1.00 16.48  ? 120 VAL   A CB  1 
ATOM   890  C  CG1 . VAL   A 1 114 ? 17.239 0.902   11.874 1.00 16.47  ? 120 VAL   A CG1 1 
ATOM   891  C  CG2 . VAL   A 1 114 ? 18.416 -1.299  11.963 1.00 17.40  ? 120 VAL   A CG2 1 
ATOM   892  N  N   . VAL   A 1 115 ? 14.292 0.214   10.400 1.00 14.79  ? 121 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 115 ? 13.313 1.133   9.782  1.00 15.74  ? 121 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 115 ? 13.547 2.563   10.297 1.00 15.98  ? 121 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 115 ? 13.409 3.540   9.573  1.00 15.12  ? 121 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 115 ? 11.900 0.648   10.116 1.00 15.78  ? 121 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 115 ? 10.841 1.640   9.653  1.00 15.66  ? 121 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 115 ? 11.657 -0.733  9.543  1.00 17.79  ? 121 VAL   A CG2 1 
ATOM   899  N  N   . GLY   A 1 116 ? 13.846 2.737   11.591 1.00 14.28  ? 122 GLY   A N   1 
ATOM   900  C  CA  . GLY   A 1 116 ? 13.923 4.080   12.182 1.00 15.24  ? 122 GLY   A CA  1 
ATOM   901  C  C   . GLY   A 1 116 ? 14.307 4.026   13.658 1.00 13.65  ? 122 GLY   A C   1 
ATOM   902  O  O   . GLY   A 1 116 ? 14.569 2.920   14.191 1.00 13.73  ? 122 GLY   A O   1 
ATOM   903  N  N   . ILE   A 1 117 ? 14.213 5.184   14.327 1.00 13.93  ? 123 ILE   A N   1 
ATOM   904  C  CA  . ILE   A 1 117 ? 14.570 5.290   15.763 1.00 15.00  ? 123 ILE   A CA  1 
ATOM   905  C  C   . ILE   A 1 117 ? 13.468 6.065   16.505 1.00 14.02  ? 123 ILE   A C   1 
ATOM   906  O  O   . ILE   A 1 117 ? 12.841 6.976   15.960 1.00 14.06  ? 123 ILE   A O   1 
ATOM   907  C  CB  . ILE   A 1 117 ? 15.978 5.886   16.039 1.00 16.32  ? 123 ILE   A CB  1 
ATOM   908  C  CG1 . ILE   A 1 117 ? 16.173 7.278   15.417 1.00 17.04  ? 123 ILE   A CG1 1 
ATOM   909  C  CG2 . ILE   A 1 117 ? 17.087 4.886   15.685 1.00 15.75  ? 123 ILE   A CG2 1 
ATOM   910  C  CD1 . ILE   A 1 117 ? 17.462 8.005   15.818 1.00 17.87  ? 123 ILE   A CD1 1 
ATOM   911  N  N   . VAL   A 1 118 ? 13.213 5.660   17.737 1.00 14.10  ? 124 VAL   A N   1 
ATOM   912  C  CA  . VAL   A 1 118 ? 12.228 6.362   18.586 1.00 14.90  ? 124 VAL   A CA  1 
ATOM   913  C  C   . VAL   A 1 118 ? 12.621 7.836   18.626 1.00 16.18  ? 124 VAL   A C   1 
ATOM   914  O  O   . VAL   A 1 118 ? 13.798 8.134   18.962 1.00 15.38  ? 124 VAL   A O   1 
ATOM   915  C  CB  . VAL   A 1 118 ? 12.150 5.718   19.962 1.00 14.57  ? 124 VAL   A CB  1 
ATOM   916  C  CG1 . VAL   A 1 118 ? 11.296 6.523   20.933 1.00 15.34  ? 124 VAL   A CG1 1 
ATOM   917  C  CG2 . VAL   A 1 118 ? 11.648 4.291   19.912 1.00 14.68  ? 124 VAL   A CG2 1 
ATOM   918  N  N   . SER   A 1 119 ? 11.645 8.710   18.451 1.00 16.12  ? 125 SER   A N   1 
ATOM   919  C  CA  . SER   A 1 119 ? 11.844 10.176  18.428 1.00 15.98  ? 125 SER   A CA  1 
ATOM   920  C  C   . SER   A 1 119 ? 10.790 10.966  19.227 1.00 18.24  ? 125 SER   A C   1 
ATOM   921  O  O   . SER   A 1 119 ? 11.137 12.064  19.747 1.00 19.30  ? 125 SER   A O   1 
ATOM   922  C  CB  . SER   A 1 119 ? 11.892 10.640  17.008 1.00 16.33  ? 125 SER   A CB  1 
ATOM   923  O  OG  . SER   A 1 119 ? 12.092 12.045  16.889 1.00 17.92  ? 125 SER   A OG  1 
ATOM   924  N  N   . THR   A 1 120 ? 9.541  10.497  19.290 1.00 17.39  ? 126 THR   A N   1 
ATOM   925  C  CA  . THR   A 1 120 ? 8.468  11.265  19.959 1.00 17.68  ? 126 THR   A CA  1 
ATOM   926  C  C   . THR   A 1 120 ? 7.598  10.307  20.771 1.00 17.94  ? 126 THR   A C   1 
ATOM   927  O  O   . THR   A 1 120 ? 7.675  9.101   20.572 1.00 16.63  ? 126 THR   A O   1 
ATOM   928  C  CB  . THR   A 1 120 ? 7.583  12.032  18.979 1.00 18.39  ? 126 THR   A CB  1 
ATOM   929  O  OG1 . THR   A 1 120 ? 6.740  11.127  18.262 1.00 21.14  ? 126 THR   A OG1 1 
ATOM   930  C  CG2 . THR   A 1 120 ? 8.369  12.876  17.999 1.00 18.01  ? 126 THR   A CG2 1 
ATOM   931  N  N   . GLY   A 1 121 ? 6.697  10.872  21.586 1.00 19.35  ? 127 GLY   A N   1 
ATOM   932  C  CA  . GLY   A 1 121 ? 5.654  10.052  22.217 1.00 22.56  ? 127 GLY   A CA  1 
ATOM   933  C  C   . GLY   A 1 121 ? 4.744  10.909  23.074 1.00 25.61  ? 127 GLY   A C   1 
ATOM   934  O  O   . GLY   A 1 121 ? 5.031  12.077  23.279 1.00 30.66  ? 127 GLY   A O   1 
ATOM   935  N  N   . GLY   A 1 122 ? 3.727  10.291  23.648 1.00 28.73  ? 128 GLY   A N   1 
ATOM   936  C  CA  . GLY   A 1 122 ? 2.717  11.011  24.428 1.00 30.72  ? 128 GLY   A CA  1 
ATOM   937  C  C   . GLY   A 1 122 ? 1.365  10.404  24.156 1.00 30.07  ? 128 GLY   A C   1 
ATOM   938  O  O   . GLY   A 1 122 ? 1.173  9.893   23.056 1.00 26.47  ? 128 GLY   A O   1 
ATOM   939  N  N   . ASN   A 1 123 ? 0.462  10.481  25.129 1.00 32.07  ? 129 ASN   A N   1 
ATOM   940  C  CA  . ASN   A 1 123 ? -0.929 9.980   25.018 1.00 29.61  ? 129 ASN   A CA  1 
ATOM   941  C  C   . ASN   A 1 123 ? -0.934 8.555   24.445 1.00 24.45  ? 129 ASN   A C   1 
ATOM   942  O  O   . ASN   A 1 123 ? -1.835 8.275   23.634 1.00 26.42  ? 129 ASN   A O   1 
ATOM   943  C  CB  . ASN   A 1 123 ? -1.809 10.932  24.204 1.00 34.41  ? 129 ASN   A CB  1 
ATOM   944  C  CG  . ASN   A 1 123 ? -2.218 12.167  24.987 1.00 39.37  ? 129 ASN   A CG  1 
ATOM   945  O  OD1 . ASN   A 1 123 ? -2.156 12.174  26.213 1.00 40.83  ? 129 ASN   A OD1 1 
ATOM   946  N  ND2 . ASN   A 1 123 ? -2.637 13.213  24.294 1.00 44.56  ? 129 ASN   A ND2 1 
ATOM   947  N  N   . GLY   A 1 124 ? 0.012  7.696   24.852 1.00 24.61  ? 130 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 124 ? -0.036 6.248   24.549 1.00 22.75  ? 130 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 124 ? 0.446  5.930   23.140 1.00 22.36  ? 130 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 124 ? 0.180  4.821   22.672 1.00 19.85  ? 130 GLY   A O   1 
ATOM   951  N  N   . LEU   A 1 125 ? 1.093  6.890   22.461 1.00 22.07  ? 131 LEU   A N   1 
ATOM   952  C  CA  . LEU   A 1 125 ? 1.651  6.691   21.102 1.00 21.44  ? 131 LEU   A CA  1 
ATOM   953  C  C   . LEU   A 1 125 ? 3.174  6.776   21.208 1.00 21.76  ? 131 LEU   A C   1 
ATOM   954  O  O   . LEU   A 1 125 ? 3.707  7.367   22.154 1.00 28.19  ? 131 LEU   A O   1 
ATOM   955  C  CB  . LEU   A 1 125 ? 1.154  7.732   20.112 1.00 24.30  ? 131 LEU   A CB  1 
ATOM   956  C  CG  . LEU   A 1 125 ? -0.353 7.871   19.939 1.00 27.40  ? 131 LEU   A CG  1 
ATOM   957  C  CD1 . LEU   A 1 125 ? -0.651 8.867   18.819 1.00 34.26  ? 131 LEU   A CD1 1 
ATOM   958  C  CD2 . LEU   A 1 125 ? -0.992 6.536   19.644 1.00 28.36  ? 131 LEU   A CD2 1 
ATOM   959  N  N   . VAL   A 1 126 ? 3.848  6.137   20.271 1.00 17.86  ? 132 VAL   A N   1 
ATOM   960  C  CA  . VAL   A 1 126 ? 5.319  6.264   20.139 1.00 17.51  ? 132 VAL   A CA  1 
ATOM   961  C  C   . VAL   A 1 126 ? 5.567  6.632   18.680 1.00 16.71  ? 132 VAL   A C   1 
ATOM   962  O  O   . VAL   A 1 126 ? 4.883  6.087   17.787 1.00 17.97  ? 132 VAL   A O   1 
ATOM   963  C  CB  . VAL   A 1 126 ? 6.018  4.978   20.594 1.00 17.81  ? 132 VAL   A CB  1 
ATOM   964  C  CG1 . VAL   A 1 126 ? 5.506  3.732   19.904 1.00 19.38  ? 132 VAL   A CG1 1 
ATOM   965  C  CG2 . VAL   A 1 126 ? 7.536  5.097   20.498 1.00 18.89  ? 132 VAL   A CG2 1 
ATOM   966  N  N   . GLY   A 1 127 ? 6.457  7.595   18.452 1.00 16.38  ? 133 GLY   A N   1 
ATOM   967  C  CA  . GLY   A 1 127 ? 6.803  8.143   17.132 1.00 17.87  ? 133 GLY   A CA  1 
ATOM   968  C  C   . GLY   A 1 127 ? 8.209  7.752   16.768 1.00 15.29  ? 133 GLY   A C   1 
ATOM   969  O  O   . GLY   A 1 127 ? 9.071  7.856   17.658 1.00 16.54  ? 133 GLY   A O   1 
ATOM   970  N  N   . PHE   A 1 128 ? 8.419  7.316   15.540 1.00 15.38  ? 134 PHE   A N   1 
ATOM   971  C  CA  . PHE   A 1 128 ? 9.750  6.880   15.041 1.00 15.05  ? 134 PHE   A CA  1 
ATOM   972  C  C   . PHE   A 1 128 ? 10.171 7.751   13.852 1.00 14.45  ? 134 PHE   A C   1 
ATOM   973  O  O   . PHE   A 1 128 ? 9.387  7.937   12.940 1.00 15.37  ? 134 PHE   A O   1 
ATOM   974  C  CB  . PHE   A 1 128 ? 9.731  5.425   14.595 1.00 14.66  ? 134 PHE   A CB  1 
ATOM   975  C  CG  . PHE   A 1 128 ? 9.089  4.479   15.573 1.00 13.60  ? 134 PHE   A CG  1 
ATOM   976  C  CD1 . PHE   A 1 128 ? 9.834  3.898   16.576 1.00 13.44  ? 134 PHE   A CD1 1 
ATOM   977  C  CD2 . PHE   A 1 128 ? 7.741  4.143   15.495 1.00 15.70  ? 134 PHE   A CD2 1 
ATOM   978  C  CE1 . PHE   A 1 128 ? 9.252  3.008   17.475 1.00 13.33  ? 134 PHE   A CE1 1 
ATOM   979  C  CE2 . PHE   A 1 128 ? 7.184  3.237   16.395 1.00 15.83  ? 134 PHE   A CE2 1 
ATOM   980  C  CZ  . PHE   A 1 128 ? 7.948  2.671   17.378 1.00 16.42  ? 134 PHE   A CZ  1 
ATOM   981  N  N   . ALA   A 1 129 ? 11.393 8.250   13.877 1.00 13.54  ? 135 ALA   A N   1 
ATOM   982  C  CA  . ALA   A 1 129 ? 12.015 8.981   12.752 1.00 13.96  ? 135 ALA   A CA  1 
ATOM   983  C  C   . ALA   A 1 129 ? 12.442 7.929   11.729 1.00 14.08  ? 135 ALA   A C   1 
ATOM   984  O  O   . ALA   A 1 129 ? 13.344 7.107   12.003 1.00 14.67  ? 135 ALA   A O   1 
ATOM   985  C  CB  . ALA   A 1 129 ? 13.207 9.787   13.256 1.00 13.78  ? 135 ALA   A CB  1 
ATOM   986  N  N   . ASP   A 1 130 ? 11.853 7.924   10.541 1.00 15.41  ? 136 ASP   A N   1 
ATOM   987  C  CA  . ASP   A 1 130 ? 12.207 6.990   9.455  1.00 15.48  ? 136 ASP   A CA  1 
ATOM   988  C  C   . ASP   A 1 130 ? 13.624 7.243   8.938  1.00 15.80  ? 136 ASP   A C   1 
ATOM   989  O  O   . ASP   A 1 130 ? 14.037 8.397   8.868  1.00 16.44  ? 136 ASP   A O   1 
ATOM   990  C  CB  . ASP   A 1 130 ? 11.221 7.141   8.296  1.00 16.61  ? 136 ASP   A CB  1 
ATOM   991  C  CG  . ASP   A 1 130 ? 11.437 6.175   7.174  1.00 19.44  ? 136 ASP   A CG  1 
ATOM   992  O  OD1 . ASP   A 1 130 ? 11.438 4.995   7.418  1.00 17.69  ? 136 ASP   A OD1 1 
ATOM   993  O  OD2 . ASP   A 1 130 ? 11.551 6.657   6.027  1.00 20.86  ? 136 ASP   A OD2 1 
ATOM   994  N  N   . VAL   A 1 131 ? 14.303 6.187   8.515  1.00 17.63  ? 137 VAL   A N   1 
ATOM   995  C  CA  . VAL   A 1 131 ? 15.615 6.325   7.822  1.00 17.28  ? 137 VAL   A CA  1 
ATOM   996  C  C   . VAL   A 1 131 ? 15.590 5.593   6.478  1.00 18.26  ? 137 VAL   A C   1 
ATOM   997  O  O   . VAL   A 1 131 ? 16.606 5.618   5.765  1.00 18.27  ? 137 VAL   A O   1 
ATOM   998  C  CB  . VAL   A 1 131 ? 16.786 5.847   8.701  1.00 16.76  ? 137 VAL   A CB  1 
ATOM   999  C  CG1 . VAL   A 1 131 ? 16.917 6.711   9.946  1.00 17.00  ? 137 VAL   A CG1 1 
ATOM   1000 C  CG2 . VAL   A 1 131 ? 16.692 4.389   9.062  1.00 15.97  ? 137 VAL   A CG2 1 
ATOM   1001 N  N   . ARG   A 1 132 ? 14.458 4.964   6.081  1.00 16.44  ? 138 ARG   A N   1 
ATOM   1002 C  CA  . ARG   A 1 132 ? 14.466 4.084   4.887  1.00 17.35  ? 138 ARG   A CA  1 
ATOM   1003 C  C   . ARG   A 1 132 ? 14.652 4.873   3.581  1.00 18.02  ? 138 ARG   A C   1 
ATOM   1004 O  O   . ARG   A 1 132 ? 15.078 4.204   2.621  1.00 20.19  ? 138 ARG   A O   1 
ATOM   1005 C  CB  . ARG   A 1 132 ? 13.144 3.311   4.842  1.00 17.23  ? 138 ARG   A CB  1 
ATOM   1006 C  CG  . ARG   A 1 132 ? 13.051 2.282   5.968  1.00 18.15  ? 138 ARG   A CG  1 
ATOM   1007 C  CD  . ARG   A 1 132 ? 11.720 1.516   5.918  1.00 16.85  ? 138 ARG   A CD  1 
ATOM   1008 N  NE  . ARG   A 1 132 ? 10.659 2.420   6.254  1.00 17.57  ? 138 ARG   A NE  1 
ATOM   1009 C  CZ  . ARG   A 1 132 ? 9.370  2.107   6.331  1.00 16.56  ? 138 ARG   A CZ  1 
ATOM   1010 N  NH1 . ARG   A 1 132 ? 8.999  0.863   6.040  1.00 17.86  ? 138 ARG   A NH1 1 
ATOM   1011 N  NH2 . ARG   A 1 132 ? 8.509  3.027   6.777  1.00 17.31  ? 138 ARG   A NH2 1 
ATOM   1012 N  N   . ASP   A 1 133 ? 14.294 6.143   3.555  1.00 18.71  ? 139 ASP   A N   1 
ATOM   1013 C  CA  . ASP   A 1 133 ? 14.481 7.021   2.354  1.00 18.71  ? 139 ASP   A CA  1 
ATOM   1014 C  C   . ASP   A 1 133 ? 15.915 7.509   2.248  1.00 22.65  ? 139 ASP   A C   1 
ATOM   1015 O  O   . ASP   A 1 133 ? 16.191 8.100   1.184  1.00 23.81  ? 139 ASP   A O   1 
ATOM   1016 C  CB  . ASP   A 1 133 ? 13.559 8.225   2.401  1.00 22.63  ? 139 ASP   A CB  1 
ATOM   1017 C  CG  . ASP   A 1 133 ? 13.867 9.211   3.501  1.00 26.85  ? 139 ASP   A CG  1 
ATOM   1018 O  OD1 . ASP   A 1 133 ? 14.219 8.748   4.638  1.00 22.68  ? 139 ASP   A OD1 1 
ATOM   1019 O  OD2 . ASP   A 1 133 ? 13.740 10.437  3.252  1.00 26.24  ? 139 ASP   A OD2 1 
ATOM   1020 N  N   . LEU   A 1 134 ? 16.768 7.316   3.263  1.00 19.74  ? 140 LEU   A N   1 
ATOM   1021 C  CA  . LEU   A 1 134 ? 18.175 7.815   3.186  1.00 20.84  ? 140 LEU   A CA  1 
ATOM   1022 C  C   . LEU   A 1 134 ? 19.035 6.779   2.435  1.00 19.81  ? 140 LEU   A C   1 
ATOM   1023 O  O   . LEU   A 1 134 ? 19.792 6.031   3.039  1.00 20.60  ? 140 LEU   A O   1 
ATOM   1024 C  CB  . LEU   A 1 134 ? 18.663 8.110   4.615  1.00 19.82  ? 140 LEU   A CB  1 
ATOM   1025 C  CG  . LEU   A 1 134 ? 17.821 9.133   5.389  1.00 21.78  ? 140 LEU   A CG  1 
ATOM   1026 C  CD1 . LEU   A 1 134 ? 18.331 9.264   6.830  1.00 23.22  ? 140 LEU   A CD1 1 
ATOM   1027 C  CD2 . LEU   A 1 134 ? 17.783 10.506  4.717  1.00 22.65  ? 140 LEU   A CD2 1 
ATOM   1028 N  N   . LEU   A 1 135 ? 18.964 6.744   1.089  1.00 23.11  ? 141 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 135 ? 19.599 5.664   0.307  1.00 24.18  ? 141 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 135 ? 21.122 5.757   0.400  1.00 25.07  ? 141 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 135 ? 21.795 4.717   0.360  1.00 27.15  ? 141 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 135 ? 19.124 5.712   -1.147 1.00 25.90  ? 141 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 135 ? 17.613 5.756   -1.350 1.00 27.85  ? 141 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 135 ? 17.293 5.704   -2.843 1.00 30.01  ? 141 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 135 ? 16.927 4.590   -0.628 1.00 26.53  ? 141 LEU   A CD2 1 
ATOM   1036 N  N   . TRP   A 1 136 ? 21.629 6.989   0.552  1.00 24.55  ? 142 TRP   A N   1 
ATOM   1037 C  CA  . TRP   A 1 136 ? 23.082 7.233   0.666  1.00 25.44  ? 142 TRP   A CA  1 
ATOM   1038 C  C   . TRP   A 1 136 ? 23.690 6.583   1.908  1.00 23.98  ? 142 TRP   A C   1 
ATOM   1039 O  O   . TRP   A 1 136 ? 24.905 6.439   1.935  1.00 26.32  ? 142 TRP   A O   1 
ATOM   1040 C  CB  . TRP   A 1 136 ? 23.336 8.742   0.606  1.00 24.87  ? 142 TRP   A CB  1 
ATOM   1041 C  CG  . TRP   A 1 136 ? 22.611 9.528   1.647  1.00 24.48  ? 142 TRP   A CG  1 
ATOM   1042 C  CD1 . TRP   A 1 136 ? 21.421 10.165  1.511  1.00 23.53  ? 142 TRP   A CD1 1 
ATOM   1043 C  CD2 . TRP   A 1 136 ? 23.070 9.784   2.978  1.00 22.84  ? 142 TRP   A CD2 1 
ATOM   1044 N  NE1 . TRP   A 1 136 ? 21.116 10.825  2.666  1.00 24.96  ? 142 TRP   A NE1 1 
ATOM   1045 C  CE2 . TRP   A 1 136 ? 22.117 10.610  3.578  1.00 22.11  ? 142 TRP   A CE2 1 
ATOM   1046 C  CE3 . TRP   A 1 136 ? 24.225 9.432   3.683  1.00 21.60  ? 142 TRP   A CE3 1 
ATOM   1047 C  CZ2 . TRP   A 1 136 ? 22.249 11.088  4.879  1.00 21.91  ? 142 TRP   A CZ2 1 
ATOM   1048 C  CZ3 . TRP   A 1 136 ? 24.359 9.906   4.978  1.00 21.84  ? 142 TRP   A CZ3 1 
ATOM   1049 C  CH2 . TRP   A 1 136 ? 23.364 10.685  5.586  1.00 21.59  ? 142 TRP   A CH2 1 
ATOM   1050 N  N   . LEU   A 1 137 ? 22.919 6.147   2.920  1.00 22.59  ? 143 LEU   A N   1 
ATOM   1051 C  CA  . LEU   A 1 137 ? 23.513 5.480   4.107  1.00 24.02  ? 143 LEU   A CA  1 
ATOM   1052 C  C   . LEU   A 1 137 ? 24.184 4.160   3.682  1.00 29.67  ? 143 LEU   A C   1 
ATOM   1053 O  O   . LEU   A 1 137 ? 25.098 3.712   4.407  1.00 28.87  ? 143 LEU   A O   1 
ATOM   1054 C  CB  . LEU   A 1 137 ? 22.470 5.201   5.199  1.00 23.34  ? 143 LEU   A CB  1 
ATOM   1055 C  CG  . LEU   A 1 137 ? 21.944 6.397   5.983  1.00 21.21  ? 143 LEU   A CG  1 
ATOM   1056 C  CD1 . LEU   A 1 137 ? 20.722 5.975   6.774  1.00 22.41  ? 143 LEU   A CD1 1 
ATOM   1057 C  CD2 . LEU   A 1 137 ? 23.019 6.987   6.900  1.00 21.87  ? 143 LEU   A CD2 1 
ATOM   1058 N  N   . ASP   A 1 138 ? 23.769 3.627   2.520  1.00 29.35  ? 144 ASP   A N   1 
ATOM   1059 C  CA  . ASP   A 1 138 ? 24.140 2.308   1.946  1.00 37.40  ? 144 ASP   A CA  1 
ATOM   1060 C  C   . ASP   A 1 138 ? 25.420 2.355   1.113  1.00 41.36  ? 144 ASP   A C   1 
ATOM   1061 O  O   . ASP   A 1 138 ? 25.844 1.264   0.698  1.00 45.80  ? 144 ASP   A O   1 
ATOM   1062 C  CB  . ASP   A 1 138 ? 23.039 1.806   1.009  1.00 35.39  ? 144 ASP   A CB  1 
ATOM   1063 C  CG  . ASP   A 1 138 ? 21.889 1.178   1.751  1.00 33.83  ? 144 ASP   A CG  1 
ATOM   1064 O  OD1 . ASP   A 1 138 ? 22.106 0.830   2.908  1.00 42.83  ? 144 ASP   A OD1 1 
ATOM   1065 O  OD2 . ASP   A 1 138 ? 20.767 1.065   1.152  1.00 38.55  ? 144 ASP   A OD2 1 
ATOM   1066 N  N   . GLU   A 1 139 ? 25.995 3.531   0.843  1.00 47.54  ? 145 GLU   A N   1 
ATOM   1067 C  CA  . GLU   A 1 139 ? 27.145 3.650   -0.101 1.00 56.33  ? 145 GLU   A CA  1 
ATOM   1068 C  C   . GLU   A 1 139 ? 28.197 4.642   0.413  1.00 62.06  ? 145 GLU   A C   1 
ATOM   1069 O  O   . GLU   A 1 139 ? 27.996 5.233   1.497  1.00 60.63  ? 145 GLU   A O   1 
ATOM   1070 C  CB  . GLU   A 1 139 ? 26.623 4.045   -1.484 1.00 59.34  ? 145 GLU   A CB  1 
ATOM   1071 C  CG  . GLU   A 1 139 ? 25.959 5.409   -1.532 1.00 58.58  ? 145 GLU   A CG  1 
ATOM   1072 C  CD  . GLU   A 1 139 ? 24.811 5.508   -2.525 1.00 63.38  ? 145 GLU   A CD  1 
ATOM   1073 O  OE1 . GLU   A 1 139 ? 24.941 6.267   -3.508 1.00 69.80  ? 145 GLU   A OE1 1 
ATOM   1074 O  OE2 . GLU   A 1 139 ? 23.781 4.828   -2.312 1.00 58.52  ? 145 GLU   A OE2 1 
ATOM   1075 N  N   . GLU   A 1 140 ? 29.284 4.800   -0.353 1.00 72.85  ? 146 GLU   A N   1 
ATOM   1076 C  CA  . GLU   A 1 140 ? 30.364 5.804   -0.137 1.00 75.43  ? 146 GLU   A CA  1 
ATOM   1077 C  C   . GLU   A 1 140 ? 31.067 5.487   1.188  1.00 78.92  ? 146 GLU   A C   1 
ATOM   1078 O  O   . GLU   A 1 140 ? 32.113 4.831   1.190  1.00 80.88  ? 146 GLU   A O   1 
ATOM   1079 C  CB  . GLU   A 1 140 ? 29.782 7.222   -0.224 1.00 74.11  ? 146 GLU   A CB  1 
ATOM   1080 C  CG  . GLU   A 1 140 ? 30.377 8.231   0.749  1.00 77.35  ? 146 GLU   A CG  1 
ATOM   1081 C  CD  . GLU   A 1 140 ? 31.774 8.743   0.430  1.00 82.14  ? 146 GLU   A CD  1 
ATOM   1082 O  OE1 . GLU   A 1 140 ? 31.968 9.977   0.462  1.00 83.23  ? 146 GLU   A OE1 1 
ATOM   1083 O  OE2 . GLU   A 1 140 ? 32.672 7.915   0.174  1.00 87.90  ? 146 GLU   A OE2 1 
HETATM 1084 ZN ZN  . ZN    B 2 .   ? 10.401 -3.936  5.712  1.00 18.48  ? 201 ZN    A ZN  1 
HETATM 1085 S  S   . DMS   C 3 .   ? 18.301 -7.426  8.367  1.00 84.86  ? 202 DMS   A S   1 
HETATM 1086 O  O   . DMS   C 3 .   ? 19.275 -7.681  7.251  1.00 90.25  ? 202 DMS   A O   1 
HETATM 1087 C  C1  . DMS   C 3 .   ? 17.282 -8.878  8.474  1.00 83.96  ? 202 DMS   A C1  1 
HETATM 1088 C  C2  . DMS   C 3 .   ? 19.210 -7.640  9.878  1.00 84.95  ? 202 DMS   A C2  1 
HETATM 1089 S  S   . DMS   D 3 .   ? 19.679 -2.963  23.817 1.00 100.10 ? 203 DMS   A S   1 
HETATM 1090 O  O   . DMS   D 3 .   ? 19.607 -3.891  25.002 1.00 94.17  ? 203 DMS   A O   1 
HETATM 1091 C  C1  . DMS   D 3 .   ? 20.995 -3.573  22.792 1.00 99.46  ? 203 DMS   A C1  1 
HETATM 1092 C  C2  . DMS   D 3 .   ? 18.316 -3.402  22.777 1.00 92.68  ? 203 DMS   A C2  1 
HETATM 1093 S  S   . DMS   E 3 .   ? -0.515 -1.353  23.291 1.00 82.69  ? 204 DMS   A S   1 
HETATM 1094 O  O   . DMS   E 3 .   ? -0.253 -0.251  24.284 1.00 64.73  ? 204 DMS   A O   1 
HETATM 1095 C  C1  . DMS   E 3 .   ? 0.388  -2.770  23.875 1.00 78.75  ? 204 DMS   A C1  1 
HETATM 1096 C  C2  . DMS   E 3 .   ? -2.163 -1.942  23.610 1.00 76.92  ? 204 DMS   A C2  1 
HETATM 1097 N  N1  . A1BQY F 4 .   ? 10.363 11.284  22.913 0.41 10.19  ? 205 A1BQY A N1  1 
HETATM 1098 N  N3  . A1BQY F 4 .   ? 11.222 14.889  19.809 0.41 11.99  ? 205 A1BQY A N3  1 
HETATM 1099 C  C4  . A1BQY F 4 .   ? 12.526 15.051  20.460 0.41 11.61  ? 205 A1BQY A C4  1 
HETATM 1100 C  C5  . A1BQY F 4 .   ? 13.188 16.361  20.049 0.41 12.21  ? 205 A1BQY A C5  1 
HETATM 1101 C  C6  . A1BQY F 4 .   ? 12.230 17.533  20.074 0.41 12.71  ? 205 A1BQY A C6  1 
HETATM 1102 C  C7  . A1BQY F 4 .   ? 12.722 18.838  20.002 0.41 13.74  ? 205 A1BQY A C7  1 
HETATM 1103 C  C8  . A1BQY F 4 .   ? 11.857 19.916  19.863 0.41 14.92  ? 205 A1BQY A C8  1 
HETATM 1104 C  C10 . A1BQY F 4 .   ? 9.988  18.424  19.888 0.41 14.12  ? 205 A1BQY A C10 1 
HETATM 1105 C  C13 . A1BQY F 4 .   ? 8.941  12.148  24.451 0.41 11.10  ? 205 A1BQY A C13 1 
HETATM 1106 C  C15 . A1BQY F 4 .   ? 7.245  12.295  26.114 0.41 11.62  ? 205 A1BQY A C15 1 
HETATM 1107 C  C17 . A1BQY F 4 .   ? 7.774  10.129  25.177 0.41 11.79  ? 205 A1BQY A C17 1 
HETATM 1108 N  N   . A1BQY F 4 .   ? 9.619  10.281  23.482 0.41 10.44  ? 205 A1BQY A N   1 
HETATM 1109 C  C   . A1BQY F 4 .   ? 9.930  8.891   23.172 0.41 9.93   ? 205 A1BQY A C   1 
HETATM 1110 O  O   . A1BQY F 4 .   ? 10.176 14.760  23.679 0.41 13.24  ? 205 A1BQY A O   1 
HETATM 1111 C  C1  . A1BQY F 4 .   ? 9.958  12.409  23.485 0.41 11.26  ? 205 A1BQY A C1  1 
HETATM 1112 C  C11 . A1BQY F 4 .   ? 10.839 17.328  20.030 0.41 12.44  ? 205 A1BQY A C11 1 
HETATM 1113 C  C12 . A1BQY F 4 .   ? 10.256 15.939  20.102 0.41 12.25  ? 205 A1BQY A C12 1 
HETATM 1114 C  C14 . A1BQY F 4 .   ? 8.203  12.922  25.338 0.41 10.86  ? 205 A1BQY A C14 1 
HETATM 1115 C  C16 . A1BQY F 4 .   ? 7.034  10.929  26.045 0.41 10.77  ? 205 A1BQY A C16 1 
HETATM 1116 C  C18 . A1BQY F 4 .   ? 8.729  10.763  24.395 0.41 10.95  ? 205 A1BQY A C18 1 
HETATM 1117 C  C2  . A1BQY F 4 .   ? 10.598 13.728  23.166 0.41 12.38  ? 205 A1BQY A C2  1 
HETATM 1118 C  C3  . A1BQY F 4 .   ? 12.375 14.914  21.988 0.41 11.86  ? 205 A1BQY A C3  1 
HETATM 1119 C  C9  . A1BQY F 4 .   ? 10.495 19.709  19.796 0.41 14.05  ? 205 A1BQY A C9  1 
HETATM 1120 N  N2  . A1BQY F 4 .   ? 11.644 13.684  22.343 0.41 11.90  ? 205 A1BQY A N2  1 
HETATM 1121 O  O   . HOH   G 5 .   ? 23.411 21.255  7.712  1.00 35.98  ? 301 HOH   A O   1 
HETATM 1122 O  O   . HOH   G 5 .   ? 4.071  6.532   24.264 1.00 34.58  ? 302 HOH   A O   1 
HETATM 1123 O  O   . HOH   G 5 .   ? 3.394  9.062   4.156  1.00 54.16  ? 303 HOH   A O   1 
HETATM 1124 O  O   . HOH   G 5 .   ? 6.792  13.660  22.990 0.41 26.17  ? 304 HOH   A O   1 
HETATM 1125 O  O   . HOH   G 5 .   ? 14.827 14.415  26.220 0.41 27.72  ? 305 HOH   A O   1 
HETATM 1126 O  O   . HOH   G 5 .   ? 0.853  8.753   6.557  1.00 49.39  ? 306 HOH   A O   1 
HETATM 1127 O  O   . HOH   G 5 .   ? 31.744 2.073   4.857  1.00 44.20  ? 307 HOH   A O   1 
HETATM 1128 O  O   . HOH   G 5 .   ? 35.002 10.184  11.236 1.00 45.67  ? 308 HOH   A O   1 
HETATM 1129 O  O   . HOH   G 5 .   ? -2.214 16.094  19.416 1.00 38.63  ? 309 HOH   A O   1 
HETATM 1130 O  O   . HOH   G 5 .   ? 22.107 -0.852  4.756  1.00 26.34  ? 310 HOH   A O   1 
HETATM 1131 O  O   . HOH   G 5 .   ? 21.239 1.753   -1.210 1.00 53.27  ? 311 HOH   A O   1 
HETATM 1132 O  O   . HOH   G 5 .   ? 18.316 21.461  10.625 1.00 34.01  ? 312 HOH   A O   1 
HETATM 1133 O  O   . HOH   G 5 .   ? -0.591 15.448  17.415 1.00 33.81  ? 313 HOH   A O   1 
HETATM 1134 O  O   . HOH   G 5 .   ? 18.101 -0.566  27.980 1.00 30.40  ? 314 HOH   A O   1 
HETATM 1135 O  O   . HOH   G 5 .   ? 29.921 4.233   5.041  1.00 33.18  ? 315 HOH   A O   1 
HETATM 1136 O  O   . HOH   G 5 .   ? 30.583 9.620   14.695 1.00 38.94  ? 316 HOH   A O   1 
HETATM 1137 O  O   . HOH   G 5 .   ? 16.527 0.595   30.695 1.00 41.61  ? 317 HOH   A O   1 
HETATM 1138 O  O   . HOH   G 5 .   ? 2.736  8.950   9.994  1.00 32.40  ? 318 HOH   A O   1 
HETATM 1139 O  O   . HOH   G 5 .   ? 17.950 4.331   26.445 1.00 40.83  ? 319 HOH   A O   1 
HETATM 1140 O  O   . HOH   G 5 .   ? 5.221  -4.829  29.201 1.00 28.00  ? 320 HOH   A O   1 
HETATM 1141 O  O   . HOH   G 5 .   ? 6.111  4.239   33.067 1.00 24.38  ? 321 HOH   A O   1 
HETATM 1142 O  O   . HOH   G 5 .   ? 22.792 -5.987  9.528  1.00 40.29  ? 322 HOH   A O   1 
HETATM 1143 O  O   . HOH   G 5 .   ? 28.865 2.802   11.552 1.00 25.64  ? 323 HOH   A O   1 
HETATM 1144 O  O   . HOH   G 5 .   ? 13.172 -7.113  30.472 1.00 43.35  ? 324 HOH   A O   1 
HETATM 1145 O  O   . HOH   G 5 .   ? 30.382 10.399  17.893 1.00 34.21  ? 325 HOH   A O   1 
HETATM 1146 O  O   . HOH   G 5 .   ? 17.413 -6.356  3.869  1.00 38.28  ? 326 HOH   A O   1 
HETATM 1147 O  O   . HOH   G 5 .   ? 18.204 -0.930  31.896 1.00 34.93  ? 327 HOH   A O   1 
HETATM 1148 O  O   . HOH   G 5 .   ? 3.040  -4.532  21.358 1.00 31.31  ? 328 HOH   A O   1 
HETATM 1149 O  O   . HOH   G 5 .   ? 19.758 8.927   19.723 1.00 19.72  ? 329 HOH   A O   1 
HETATM 1150 O  O   . HOH   G 5 .   ? 27.677 3.258   3.907  1.00 44.15  ? 330 HOH   A O   1 
HETATM 1151 O  O   . HOH   G 5 .   ? 36.557 17.012  13.493 1.00 33.87  ? 331 HOH   A O   1 
HETATM 1152 O  O   . HOH   G 5 .   ? 11.767 -4.143  -0.557 1.00 40.37  ? 332 HOH   A O   1 
HETATM 1153 O  O   . HOH   G 5 .   ? 1.268  21.449  22.735 1.00 48.27  ? 333 HOH   A O   1 
HETATM 1154 O  O   . HOH   G 5 .   ? 26.362 -1.643  7.611  1.00 31.65  ? 334 HOH   A O   1 
HETATM 1155 O  O   . HOH   G 5 .   ? 2.344  7.680   26.180 1.00 51.76  ? 335 HOH   A O   1 
HETATM 1156 O  O   . HOH   G 5 .   ? 10.724 9.036   5.075  1.00 24.32  ? 336 HOH   A O   1 
HETATM 1157 O  O   . HOH   G 5 .   ? 17.114 2.663   23.750 1.00 24.38  ? 337 HOH   A O   1 
HETATM 1158 O  O   . HOH   G 5 .   ? -0.034 0.651   16.556 1.00 16.37  ? 338 HOH   A O   1 
HETATM 1159 O  O   . HOH   G 5 .   ? 13.363 23.843  13.576 1.00 49.42  ? 339 HOH   A O   1 
HETATM 1160 O  O   . HOH   G 5 .   ? 21.155 23.424  12.039 1.00 45.15  ? 340 HOH   A O   1 
HETATM 1161 O  O   . HOH   G 5 .   ? 29.660 21.148  19.440 1.00 27.46  ? 341 HOH   A O   1 
HETATM 1162 O  O   . HOH   G 5 .   ? 37.693 14.314  13.278 1.00 46.50  ? 342 HOH   A O   1 
HETATM 1163 O  O   . HOH   G 5 .   ? 5.870  2.584   6.290  1.00 24.70  ? 343 HOH   A O   1 
HETATM 1164 O  O   . HOH   G 5 .   ? 31.636 19.148  11.589 1.00 25.76  ? 344 HOH   A O   1 
HETATM 1165 O  O   . HOH   G 5 .   ? 24.594 8.896   -2.870 1.00 50.08  ? 345 HOH   A O   1 
HETATM 1166 O  O   . HOH   G 5 .   ? 4.195  11.716  19.048 1.00 38.03  ? 346 HOH   A O   1 
HETATM 1167 O  O   . HOH   G 5 .   ? -1.056 2.785   4.557  1.00 46.29  ? 347 HOH   A O   1 
HETATM 1168 O  O   . HOH   G 5 .   ? -0.581 2.860   24.417 1.00 22.87  ? 348 HOH   A O   1 
HETATM 1169 O  O   . HOH   G 5 .   ? 8.064  -3.176  0.637  1.00 26.58  ? 349 HOH   A O   1 
HETATM 1170 O  O   . HOH   G 5 .   ? -3.124 9.376   21.487 1.00 39.34  ? 350 HOH   A O   1 
HETATM 1171 O  O   . HOH   G 5 .   ? 24.034 10.468  21.883 1.00 38.37  ? 351 HOH   A O   1 
HETATM 1172 O  O   . HOH   G 5 .   ? 13.456 22.206  24.908 0.41 28.13  ? 352 HOH   A O   1 
HETATM 1173 O  O   . HOH   G 5 .   ? 17.151 -5.636  11.968 1.00 39.66  ? 353 HOH   A O   1 
HETATM 1174 O  O   . HOH   G 5 .   ? 18.733 20.389  7.287  1.00 64.89  ? 354 HOH   A O   1 
HETATM 1175 O  O   . HOH   G 5 .   ? 6.609  -4.930  31.652 1.00 36.89  ? 355 HOH   A O   1 
HETATM 1176 O  O   . HOH   G 5 .   ? 10.407 5.559   3.775  1.00 21.02  ? 356 HOH   A O   1 
HETATM 1177 O  O   . HOH   G 5 .   ? 11.053 12.422  12.371 1.00 30.43  ? 357 HOH   A O   1 
HETATM 1178 O  O   . HOH   G 5 .   ? 5.535  1.169   -1.937 1.00 31.49  ? 358 HOH   A O   1 
HETATM 1179 O  O   . HOH   G 5 .   ? 31.684 8.400   6.923  1.00 33.66  ? 359 HOH   A O   1 
HETATM 1180 O  O   . HOH   G 5 .   ? 4.605  -6.264  14.412 1.00 37.32  ? 360 HOH   A O   1 
HETATM 1181 O  O   . HOH   G 5 .   ? 25.672 18.477  21.654 1.00 37.47  ? 361 HOH   A O   1 
HETATM 1182 O  O   . HOH   G 5 .   ? 6.758  -8.035  23.645 1.00 32.18  ? 362 HOH   A O   1 
HETATM 1183 O  O   . HOH   G 5 .   ? 0.204  -1.773  19.954 1.00 29.29  ? 363 HOH   A O   1 
HETATM 1184 O  O   . HOH   G 5 .   ? 22.815 -0.094  16.587 1.00 24.96  ? 364 HOH   A O   1 
HETATM 1185 O  O   . HOH   G 5 .   ? 14.207 2.747   23.644 1.00 17.44  ? 365 HOH   A O   1 
HETATM 1186 O  O   . HOH   G 5 .   ? 29.963 10.721  20.805 1.00 31.97  ? 366 HOH   A O   1 
HETATM 1187 O  O   . HOH   G 5 .   ? 4.298  -0.762  24.333 1.00 21.69  ? 367 HOH   A O   1 
HETATM 1188 O  O   . HOH   G 5 .   ? 30.987 18.547  8.683  1.00 34.16  ? 368 HOH   A O   1 
HETATM 1189 O  O   . HOH   G 5 .   ? 14.193 -11.128 8.308  1.00 40.84  ? 369 HOH   A O   1 
HETATM 1190 O  O   . HOH   G 5 .   ? 18.659 8.965   26.456 1.00 28.79  ? 370 HOH   A O   1 
HETATM 1191 O  O   . HOH   G 5 .   ? 10.367 2.533   33.830 1.00 21.79  ? 371 HOH   A O   1 
HETATM 1192 O  O   . HOH   G 5 .   ? 4.233  13.861  25.294 1.00 43.08  ? 372 HOH   A O   1 
HETATM 1193 O  O   . HOH   G 5 .   ? 29.497 5.528   19.570 1.00 49.79  ? 373 HOH   A O   1 
HETATM 1194 O  O   . HOH   G 5 .   ? 19.764 1.919   18.970 1.00 26.78  ? 374 HOH   A O   1 
HETATM 1195 O  O   . HOH   G 5 .   ? 8.808  3.466   3.120  1.00 22.39  ? 375 HOH   A O   1 
HETATM 1196 O  O   . HOH   G 5 .   ? 14.786 7.244   -1.097 1.00 34.38  ? 376 HOH   A O   1 
HETATM 1197 O  O   . HOH   G 5 .   ? 3.412  -3.951  6.293  1.00 34.47  ? 377 HOH   A O   1 
HETATM 1198 O  O   . HOH   G 5 .   ? 36.439 1.192   8.759  0.50 37.31  ? 378 HOH   A O   1 
HETATM 1199 O  O   . HOH   G 5 .   ? 22.292 18.595  19.222 1.00 32.35  ? 379 HOH   A O   1 
HETATM 1200 O  O   . HOH   G 5 .   ? 13.103 10.878  9.851  1.00 19.24  ? 380 HOH   A O   1 
HETATM 1201 O  O   . HOH   G 5 .   ? 0.398  17.075  8.196  0.41 23.15  ? 381 HOH   A O   1 
HETATM 1202 O  O   . HOH   G 5 .   ? 35.771 -1.421  11.604 1.00 39.62  ? 382 HOH   A O   1 
HETATM 1203 O  O   . HOH   G 5 .   ? 15.265 12.196  24.722 1.00 28.40  ? 383 HOH   A O   1 
HETATM 1204 O  O   . HOH   G 5 .   ? 9.634  21.674  11.622 1.00 48.08  ? 384 HOH   A O   1 
HETATM 1205 O  O   . HOH   G 5 .   ? 20.936 -4.823  13.731 1.00 48.58  ? 385 HOH   A O   1 
HETATM 1206 O  O   . HOH   G 5 .   ? 25.352 3.809   20.883 1.00 39.93  ? 386 HOH   A O   1 
HETATM 1207 O  O   . HOH   G 5 .   ? 7.074  13.624  5.919  1.00 31.89  ? 387 HOH   A O   1 
HETATM 1208 O  O   . HOH   G 5 .   ? 8.964  9.879   31.897 1.00 33.93  ? 388 HOH   A O   1 
HETATM 1209 O  O   . HOH   G 5 .   ? 9.082  5.166   34.138 1.00 25.09  ? 389 HOH   A O   1 
HETATM 1210 O  O   . HOH   G 5 .   ? 34.497 7.640   8.041  0.50 38.57  ? 390 HOH   A O   1 
HETATM 1211 O  O   . HOH   G 5 .   ? 14.735 15.096  4.287  1.00 34.88  ? 391 HOH   A O   1 
HETATM 1212 O  O   . HOH   G 5 .   ? 36.741 14.920  15.818 1.00 39.35  ? 392 HOH   A O   1 
HETATM 1213 O  O   . HOH   G 5 .   ? 31.518 14.521  22.377 1.00 31.20  ? 393 HOH   A O   1 
HETATM 1214 O  O   . HOH   G 5 .   ? 13.024 9.595   30.132 1.00 26.59  ? 394 HOH   A O   1 
HETATM 1215 O  O   . HOH   G 5 .   ? 1.986  13.248  17.735 1.00 33.11  ? 395 HOH   A O   1 
HETATM 1216 O  O   . HOH   G 5 .   ? 0.072  5.291   6.738  1.00 29.53  ? 396 HOH   A O   1 
HETATM 1217 O  O   . HOH   G 5 .   ? 14.089 -3.507  17.828 1.00 21.94  ? 397 HOH   A O   1 
HETATM 1218 O  O   . HOH   G 5 .   ? 3.527  12.880  20.942 1.00 53.52  ? 398 HOH   A O   1 
HETATM 1219 O  O   . HOH   G 5 .   ? 15.484 11.823  1.389  1.00 39.23  ? 399 HOH   A O   1 
HETATM 1220 O  O   . HOH   G 5 .   ? 17.568 -0.368  20.068 1.00 22.65  ? 400 HOH   A O   1 
HETATM 1221 O  O   . HOH   G 5 .   ? 22.552 3.698   24.151 1.00 57.19  ? 401 HOH   A O   1 
HETATM 1222 O  O   . HOH   G 5 .   ? 11.565 -8.263  24.699 1.00 27.70  ? 402 HOH   A O   1 
HETATM 1223 O  O   . HOH   G 5 .   ? 3.032  -2.558  4.061  1.00 46.95  ? 403 HOH   A O   1 
HETATM 1224 O  O   . HOH   G 5 .   ? 23.163 2.376   20.195 1.00 31.65  ? 404 HOH   A O   1 
HETATM 1225 O  O   . HOH   G 5 .   ? 0.693  18.345  26.244 1.00 46.35  ? 405 HOH   A O   1 
HETATM 1226 O  O   . HOH   G 5 .   ? 0.439  -2.027  17.197 1.00 22.78  ? 406 HOH   A O   1 
HETATM 1227 O  O   . HOH   G 5 .   ? 3.823  -1.022  29.434 1.00 40.05  ? 407 HOH   A O   1 
HETATM 1228 O  O   . HOH   G 5 .   ? 34.075 18.254  10.373 1.00 36.14  ? 408 HOH   A O   1 
HETATM 1229 O  O   . HOH   G 5 .   ? 28.297 15.887  4.153  1.00 39.39  ? 409 HOH   A O   1 
HETATM 1230 O  O   . HOH   G 5 .   ? 15.741 17.568  17.086 0.41 16.96  ? 410 HOH   A O   1 
HETATM 1231 O  O   . HOH   G 5 .   ? 19.798 16.319  25.179 1.00 47.14  ? 411 HOH   A O   1 
HETATM 1232 O  O   . HOH   G 5 .   ? 1.223  11.428  27.862 1.00 48.80  ? 412 HOH   A O   1 
HETATM 1233 O  O   . HOH   G 5 .   ? 17.833 19.144  17.838 1.00 27.41  ? 413 HOH   A O   1 
HETATM 1234 O  O   . HOH   G 5 .   ? 13.137 -8.229  12.182 1.00 37.11  ? 414 HOH   A O   1 
HETATM 1235 O  O   . HOH   G 5 .   ? 15.207 -3.981  1.826  1.00 26.46  ? 415 HOH   A O   1 
HETATM 1236 O  O   . HOH   G 5 .   ? 6.386  -2.974  -1.406 1.00 37.32  ? 416 HOH   A O   1 
HETATM 1237 O  O   . HOH   G 5 .   ? 20.226 -4.714  10.759 1.00 35.06  ? 417 HOH   A O   1 
HETATM 1238 O  O   . HOH   G 5 .   ? 23.951 7.060   21.232 1.00 34.61  ? 418 HOH   A O   1 
HETATM 1239 O  O   . HOH   G 5 .   ? 17.746 -5.399  26.917 1.00 44.58  ? 419 HOH   A O   1 
HETATM 1240 O  O   . HOH   G 5 .   ? 13.042 17.646  16.788 0.41 21.76  ? 420 HOH   A O   1 
HETATM 1241 O  O   . HOH   G 5 .   ? 2.228  4.907   27.738 1.00 28.77  ? 421 HOH   A O   1 
HETATM 1242 O  O   . HOH   G 5 .   ? 8.215  -6.993  9.344  1.00 36.81  ? 422 HOH   A O   1 
HETATM 1243 O  O   . HOH   G 5 .   ? 4.657  24.901  22.627 1.00 35.00  ? 423 HOH   A O   1 
HETATM 1244 O  O   . HOH   G 5 .   ? 7.353  17.642  22.745 0.41 32.83  ? 424 HOH   A O   1 
HETATM 1245 O  O   . HOH   G 5 .   ? 19.217 13.305  2.697  1.00 45.16  ? 425 HOH   A O   1 
HETATM 1246 O  O   . HOH   G 5 .   ? 27.860 -1.877  14.792 1.00 38.12  ? 426 HOH   A O   1 
HETATM 1247 O  O   . HOH   G 5 .   ? 1.093  -5.841  17.683 1.00 43.83  ? 427 HOH   A O   1 
HETATM 1248 O  O   . HOH   G 5 .   ? 26.061 9.283   22.669 1.00 48.63  ? 428 HOH   A O   1 
HETATM 1249 O  O   . HOH   G 5 .   ? 21.621 8.667   21.860 1.00 25.73  ? 429 HOH   A O   1 
HETATM 1250 O  O   . HOH   G 5 .   ? 28.648 15.988  24.151 1.00 35.76  ? 430 HOH   A O   1 
HETATM 1251 O  O   . HOH   G 5 .   ? 1.756  14.436  19.947 1.00 43.33  ? 431 HOH   A O   1 
HETATM 1252 O  O   . HOH   G 5 .   ? 3.257  -1.395  21.955 1.00 31.41  ? 432 HOH   A O   1 
HETATM 1253 O  O   . HOH   G 5 .   ? 34.113 3.901   15.476 1.00 39.11  ? 433 HOH   A O   1 
HETATM 1254 O  O   . HOH   G 5 .   ? 17.308 -3.396  19.639 1.00 32.69  ? 434 HOH   A O   1 
HETATM 1255 O  O   . HOH   G 5 .   ? 20.894 -3.284  16.241 1.00 44.17  ? 435 HOH   A O   1 
HETATM 1256 O  O   . HOH   G 5 .   ? 30.661 2.168   13.609 1.00 29.43  ? 436 HOH   A O   1 
HETATM 1257 O  O   . HOH   G 5 .   ? -1.457 13.941  21.432 1.00 44.63  ? 437 HOH   A O   1 
HETATM 1258 O  O   . HOH   G 5 .   ? 18.178 9.321   -0.991 1.00 33.98  ? 438 HOH   A O   1 
HETATM 1259 O  O   . HOH   G 5 .   ? 7.510  11.619  4.672  1.00 46.13  ? 439 HOH   A O   1 
HETATM 1260 O  O   . HOH   G 5 .   ? 36.709 19.502  17.911 1.00 35.30  ? 440 HOH   A O   1 
HETATM 1261 O  O   . HOH   G 5 .   ? 12.727 17.909  6.297  1.00 57.65  ? 441 HOH   A O   1 
HETATM 1262 O  O   . HOH   G 5 .   ? 22.869 18.760  6.539  1.00 31.24  ? 442 HOH   A O   1 
HETATM 1263 O  O   . HOH   G 5 .   ? 34.205 6.894   15.528 1.00 38.32  ? 443 HOH   A O   1 
HETATM 1264 O  O   . HOH   G 5 .   ? 4.628  25.838  18.699 1.00 49.60  ? 444 HOH   A O   1 
HETATM 1265 O  O   . HOH   G 5 .   ? 2.851  14.076  5.152  1.00 47.29  ? 445 HOH   A O   1 
HETATM 1266 O  O   . HOH   G 5 .   ? 20.141 -1.945  33.628 1.00 53.19  ? 446 HOH   A O   1 
HETATM 1267 O  O   . HOH   G 5 .   ? 25.636 -2.135  15.426 1.00 45.57  ? 447 HOH   A O   1 
HETATM 1268 O  O   . HOH   G 5 .   ? 6.927  -4.663  2.684  1.00 30.42  ? 448 HOH   A O   1 
HETATM 1269 O  O   . HOH   G 5 .   ? 31.350 6.491   4.099  1.00 47.97  ? 449 HOH   A O   1 
HETATM 1270 O  O   . HOH   G 5 .   ? 17.877 11.103  0.867  1.00 46.63  ? 450 HOH   A O   1 
HETATM 1271 O  O   . HOH   G 5 .   ? 23.953 18.083  4.366  1.00 50.73  ? 451 HOH   A O   1 
HETATM 1272 O  O   . HOH   G 5 .   ? 1.776  -5.844  14.946 1.00 46.40  ? 452 HOH   A O   1 
HETATM 1273 O  O   . HOH   G 5 .   ? 18.419 7.353   28.713 1.00 40.86  ? 453 HOH   A O   1 
HETATM 1274 O  O   . HOH   G 5 .   ? 15.629 11.564  29.085 1.00 38.47  ? 454 HOH   A O   1 
HETATM 1275 O  O   . HOH   G 5 .   ? 14.278 -7.282  25.292 1.00 34.36  ? 455 HOH   A O   1 
HETATM 1276 O  O   . HOH   G 5 .   ? 3.265  -1.532  26.816 1.00 34.93  ? 456 HOH   A O   1 
HETATM 1277 O  O   . HOH   G 5 .   ? -2.254 7.454   27.765 1.00 53.24  ? 457 HOH   A O   1 
HETATM 1278 O  O   . HOH   G 5 .   ? 0.687  14.787  25.025 1.00 44.62  ? 458 HOH   A O   1 
HETATM 1279 O  O   . HOH   G 5 .   ? 13.860 -10.444 3.389  1.00 51.39  ? 459 HOH   A O   1 
HETATM 1280 O  O   . HOH   G 5 .   ? 3.165  9.947   27.841 1.00 43.76  ? 460 HOH   A O   1 
HETATM 1281 O  O   . HOH   G 5 .   ? 14.028 14.007  35.380 1.00 49.14  ? 461 HOH   A O   1 
HETATM 1282 O  O   . HOH   G 5 .   ? 6.136  3.487   3.735  1.00 27.84  ? 462 HOH   A O   1 
HETATM 1283 O  O   . HOH   G 5 .   ? 7.284  -7.235  2.097  1.00 45.32  ? 463 HOH   A O   1 
HETATM 1284 O  O   . HOH   G 5 .   ? 0.802  13.783  22.532 1.00 45.80  ? 464 HOH   A O   1 
HETATM 1285 O  O   . HOH   G 5 .   ? 26.433 -0.456  4.175  0.50 32.14  ? 465 HOH   A O   1 
HETATM 1286 O  O   . HOH   G 5 .   ? 23.709 13.622  1.682  1.00 56.19  ? 466 HOH   A O   1 
HETATM 1287 O  O   . HOH   G 5 .   ? 24.100 -0.145  18.901 0.50 21.72  ? 467 HOH   A O   1 
HETATM 1288 O  O   . HOH   G 5 .   ? 30.408 5.937   17.251 1.00 46.53  ? 468 HOH   A O   1 
HETATM 1289 O  O   . HOH   G 5 .   ? 18.912 0.807   22.326 1.00 37.27  ? 469 HOH   A O   1 
HETATM 1290 O  O   . HOH   G 5 .   ? 17.232 11.233  26.686 1.00 32.75  ? 470 HOH   A O   1 
HETATM 1291 O  O   . HOH   G 5 .   ? -1.051 16.608  25.750 1.00 50.57  ? 471 HOH   A O   1 
HETATM 1292 O  O   . HOH   G 5 .   ? 20.415 9.644   -2.228 1.00 35.16  ? 472 HOH   A O   1 
HETATM 1293 O  O   . HOH   G 5 .   ? 0.629  2.759   26.825 1.00 32.06  ? 473 HOH   A O   1 
HETATM 1294 O  O   . HOH   G 5 .   ? 4.254  24.611  16.241 1.00 51.68  ? 474 HOH   A O   1 
HETATM 1295 O  O   . HOH   G 5 .   ? 21.450 13.446  -0.464 1.00 47.84  ? 475 HOH   A O   1 
HETATM 1296 O  O   . HOH   G 5 .   ? 12.977 -6.229  33.706 1.00 45.09  ? 476 HOH   A O   1 
HETATM 1297 O  O   . HOH   G 5 .   ? 8.839  7.725   3.020  1.00 34.76  ? 477 HOH   A O   1 
HETATM 1298 O  O   . HOH   G 5 .   ? 29.719 0.073   15.389 1.00 44.95  ? 478 HOH   A O   1 
HETATM 1299 O  O   . HOH   G 5 .   ? -0.610 12.506  17.477 1.00 41.21  ? 479 HOH   A O   1 
HETATM 1300 O  O   . HOH   G 5 .   ? -1.534 11.636  20.148 1.00 41.73  ? 480 HOH   A O   1 
HETATM 1301 O  O   . HOH   G 5 .   ? 26.177 11.296  0.849  1.00 53.18  ? 481 HOH   A O   1 
HETATM 1302 O  O   . HOH   G 5 .   ? 18.143 20.121  20.679 1.00 48.42  ? 482 HOH   A O   1 
HETATM 1303 O  O   . HOH   G 5 .   ? 1.871  24.188  22.745 1.00 46.36  ? 483 HOH   A O   1 
HETATM 1304 O  O   . HOH   G 5 .   ? 31.570 3.758   15.833 1.00 36.98  ? 484 HOH   A O   1 
HETATM 1305 O  O   . HOH   G 5 .   ? 2.077  -4.221  26.765 1.00 46.19  ? 485 HOH   A O   1 
HETATM 1306 O  O   . HOH   G 5 .   ? 5.693  6.257   2.457  1.00 44.11  ? 486 HOH   A O   1 
HETATM 1307 O  O   . HOH   G 5 .   ? 15.265 -7.677  31.919 1.00 48.05  ? 487 HOH   A O   1 
HETATM 1308 O  O   . HOH   G 5 .   ? 25.743 12.600  25.608 1.00 47.13  ? 488 HOH   A O   1 
HETATM 1309 O  O   . HOH   G 5 .   ? 11.912 11.928  31.457 1.00 44.07  ? 489 HOH   A O   1 
HETATM 1310 O  O   . HOH   G 5 .   ? -3.487 24.212  11.854 1.00 53.21  ? 490 HOH   A O   1 
HETATM 1311 O  O   . HOH   G 5 .   ? 37.814 18.363  15.490 1.00 41.07  ? 491 HOH   A O   1 
HETATM 1312 O  O   . HOH   G 5 .   ? 3.986  13.654  27.855 1.00 47.78  ? 492 HOH   A O   1 
HETATM 1313 O  O   . HOH   G 5 .   ? 22.365 11.418  -2.050 1.00 50.43  ? 493 HOH   A O   1 
HETATM 1314 O  O   . HOH   G 5 .   ? 5.669  -8.556  26.025 1.00 46.50  ? 494 HOH   A O   1 
HETATM 1315 O  O   . HOH   G 5 .   ? 2.882  24.390  25.404 1.00 57.34  ? 495 HOH   A O   1 
HETATM 1316 O  O   . HOH   G 5 .   ? 25.019 11.201  -1.507 1.00 52.96  ? 496 HOH   A O   1 
HETATM 1317 O  O   . HOH   G 5 .   ? 4.867  22.934  8.594  1.00 53.60  ? 497 HOH   A O   1 
HETATM 1318 O  O   . HOH   G 5 .   ? 19.415 12.136  27.648 1.00 43.35  ? 498 HOH   A O   1 
HETATM 1319 O  O   . HOH   G 5 .   ? 4.757  22.504  5.475  1.00 54.00  ? 499 HOH   A O   1 
# 
