data_7HZQ
# 
_entry.id   7HZQ 
# 
_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   7HZQ         pdb_00007hzq 10.2210/pdb7hzq/pdb 
WWPDB D_1001408134 ?            ?                   
# 
_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                        7HZQ 
_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 '(3S)-1-[(2-methoxyphenyl)acetyl]piperidine-3-carboxamide' 276.331   1  ?         ? ? ? 
4 water       nat water                                                      18.015    62 ?         ? ? ? 
# 
_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 '(3S)-1-[(2-methoxyphenyl)acetyl]piperidine-3-carboxamide' A1BQ4 
4 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 
A1BQ4 non-polymer         . '(3S)-1-[(2-methoxyphenyl)acetyl]piperidine-3-carboxamide' ? 'C15 H20 N2 O3'  276.331 
ALA   'L-peptide linking' y ALANINE                                                    ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                   ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                 ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                            ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                   ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                  ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                            ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                    ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                  ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                      ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                 ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                    ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                     ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                 ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                              ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                    ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                     ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                  ? 'C4 H9 N O3'     119.119 
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 ?   ?   ?   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        A1BQ4 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQ4 
_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 A1BQ4 1  202 245 A1BQ4 LIG A . 
D 4 HOH   1  301 57  HOH   HOH A . 
D 4 HOH   2  302 1   HOH   HOH A . 
D 4 HOH   3  303 9   HOH   HOH A . 
D 4 HOH   4  304 63  HOH   HOH A . 
D 4 HOH   5  305 62  HOH   HOH A . 
D 4 HOH   6  306 15  HOH   HOH A . 
D 4 HOH   7  307 11  HOH   HOH A . 
D 4 HOH   8  308 27  HOH   HOH A . 
D 4 HOH   9  309 60  HOH   HOH A . 
D 4 HOH   10 310 18  HOH   HOH A . 
D 4 HOH   11 311 24  HOH   HOH A . 
D 4 HOH   12 312 38  HOH   HOH A . 
D 4 HOH   13 313 45  HOH   HOH A . 
D 4 HOH   14 314 5   HOH   HOH A . 
D 4 HOH   15 315 16  HOH   HOH A . 
D 4 HOH   16 316 33  HOH   HOH A . 
D 4 HOH   17 317 13  HOH   HOH A . 
D 4 HOH   18 318 3   HOH   HOH A . 
D 4 HOH   19 319 28  HOH   HOH A . 
D 4 HOH   20 320 48  HOH   HOH A . 
D 4 HOH   21 321 6   HOH   HOH A . 
D 4 HOH   22 322 12  HOH   HOH A . 
D 4 HOH   23 323 40  HOH   HOH A . 
D 4 HOH   24 324 54  HOH   HOH A . 
D 4 HOH   25 325 41  HOH   HOH A . 
D 4 HOH   26 326 17  HOH   HOH A . 
D 4 HOH   27 327 25  HOH   HOH A . 
D 4 HOH   28 328 39  HOH   HOH A . 
D 4 HOH   29 329 10  HOH   HOH A . 
D 4 HOH   30 330 31  HOH   HOH A . 
D 4 HOH   31 331 8   HOH   HOH A . 
D 4 HOH   32 332 4   HOH   HOH A . 
D 4 HOH   33 333 19  HOH   HOH A . 
D 4 HOH   34 334 35  HOH   HOH A . 
D 4 HOH   35 335 61  HOH   HOH A . 
D 4 HOH   36 336 43  HOH   HOH A . 
D 4 HOH   37 337 53  HOH   HOH A . 
D 4 HOH   38 338 29  HOH   HOH A . 
D 4 HOH   39 339 42  HOH   HOH A . 
D 4 HOH   40 340 23  HOH   HOH A . 
D 4 HOH   41 341 22  HOH   HOH A . 
D 4 HOH   42 342 37  HOH   HOH A . 
D 4 HOH   43 343 34  HOH   HOH A . 
D 4 HOH   44 344 32  HOH   HOH A . 
D 4 HOH   45 345 55  HOH   HOH A . 
D 4 HOH   46 346 26  HOH   HOH A . 
D 4 HOH   47 347 44  HOH   HOH A . 
D 4 HOH   48 348 51  HOH   HOH A . 
D 4 HOH   49 349 30  HOH   HOH A . 
D 4 HOH   50 350 56  HOH   HOH A . 
D 4 HOH   51 351 50  HOH   HOH A . 
D 4 HOH   52 352 20  HOH   HOH A . 
D 4 HOH   53 353 64  HOH   HOH A . 
D 4 HOH   54 354 14  HOH   HOH A . 
D 4 HOH   55 355 7   HOH   HOH A . 
D 4 HOH   56 356 52  HOH   HOH A . 
D 4 HOH   57 357 21  HOH   HOH A . 
D 4 HOH   58 358 59  HOH   HOH A . 
D 4 HOH   59 359 47  HOH   HOH A . 
D 4 HOH   60 360 2   HOH   HOH A . 
D 4 HOH   61 361 65  HOH   HOH A . 
D 4 HOH   62 362 58  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           7HZQ 
_cell.length_a           72.918 
_cell.length_b           61.719 
_cell.length_c           32.822 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.94 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZQ 
_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          7HZQ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.32 
_exptl_crystal.density_percent_sol   46.99 
_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   2024-10-08 
_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   0.92209 
_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        0.92209 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZQ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.08 
_reflns.d_resolution_high            2.06 
_reflns.number_obs                   5078 
_reflns.percent_possible_obs         55.8 
_reflns.pdbx_Rmerge_I_obs            0.039 
_reflns.pdbx_netI_over_sigmaI        30.5 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.042 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     26677 
_reflns.pdbx_chi_squared             1.00 
_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                  2.06 
_reflns_shell.d_res_low                   2.17 
_reflns_shell.number_measured_all         42 
_reflns_shell.number_unique_obs           33 
_reflns_shell.Rmerge_I_obs                0.084 
_reflns_shell.pdbx_chi_squared            0.28 
_reflns_shell.pdbx_redundancy             1.3 
_reflns_shell.percent_possible_obs        2.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   3.5 
_reflns_shell.pdbx_Rrim_I_all             0.115 
_reflns_shell.pdbx_Rpim_I_all             0.078 
_reflns_shell.pdbx_CC_half                0.988 
_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                                 7HZQ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     4787 
_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                             30.88 
_refine.ls_d_res_high                            2.06 
_refine.ls_percent_reflns_obs                    55.45 
_refine.ls_R_factor_obs                          0.21388 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.20873 
_refine.ls_R_factor_R_free                       0.33179 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.5 
_refine.ls_number_reflns_R_free                  225 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.918 
_refine.correlation_coeff_Fo_to_Fc_free          0.797 
_refine.B_iso_mean                               20.690 
_refine.aniso_B[1][1]                            0.80 
_refine.aniso_B[2][2]                            -0.61 
_refine.aniso_B[3][3]                            -0.26 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.65 
_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                       ? 
_refine.pdbx_overall_ESU_R_Free                  0.539 
_refine.overall_SU_ML                            0.226 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             8.093 
_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        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_refine_hist.number_atoms_solvent             62 
_refine_hist.number_atoms_total               1157 
_refine_hist.d_res_high                       2.06 
_refine_hist.d_res_low                        30.88 
# 
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             0.006  0.015  ? 2605 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1686 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.571  1.625  ? 2653 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.153  1.609  ? 3888 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.864  5.000  ? 261  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       35.170 22.000 ? 100  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       16.753 15.000 ? 272  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       14.813 15.000 ? 12   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.059  0.200  ? 225  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.006  0.020  ? 2478 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 486  '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                  1.128  2.000  ? 1345 'X-RAY DIFFRACTION' ? 
r_mcbond_other               1.140  1.981  ? 1317 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.176  3.002  ? 1253 'X-RAY DIFFRACTION' ? 
r_mcangle_other              2.176  3.006  ? 1254 'X-RAY DIFFRACTION' ? 
r_scbond_it                  1.094  2.248  ? 1260 'X-RAY DIFFRACTION' ? 
r_scbond_other               1.094  2.253  ? 1261 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              2.047  3.275  ? 1401 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       4.607  22.825 ? 2101 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         4.544  22.810 ? 2088 '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                       2.062 
_refine_ls_shell.d_res_low                        2.116 
_refine_ls_shell.number_reflns_R_work             10 
_refine_ls_shell.R_factor_R_work                  0.102 
_refine_ls_shell.percent_reflns_obs               1.50 
_refine_ls_shell.R_factor_R_free                  0.000 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             0 
_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                  7HZQ 
_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-0031746-001 (A71EV2A-x3186)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZQ 
_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 4 ? 
# 
_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              7HZQ 
_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 
# 
_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 ASN A 13  ? ALA A 17  ? ASN A 19  ALA A 23  5 ? 5 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P4 AA4 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 ? ? ? ? ? ? ? 2.366 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 58  A ZN 201 1_555 ? ? ? ? ? ? ? 2.182 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 116 A ZN 201 1_555 ? ? ? ? ? ? ? 2.437 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 B ZN . ZN ? ? A HIS 118 A ZN 201 1_555 ? ? ? ? ? ? ? 2.098 ? ? 
# 
_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 97.6  ? 
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_555 115.5 ? 
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_555 116.3 ? 
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_555 121.5 ? 
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_555 101.5 ? 
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_555 104.1 ? 
# 
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   ? VAL A 12  ? ILE A 10  VAL A 18  
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 TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N SER A 37  ? N SER A 43  O ARG A 10  ? O ARG A 16  
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 CYS A 110 ? N CYS A 116 O GLY A 113 ? O GLY A 119 
AA2 4 5 N THR A 120 ? N THR A 126 O GLY A 127 ? O GLY A 133 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O LEU A 92  ? O LEU A 98  N SER A 74  ? N SER A 80  
# 
_pdbx_entry_details.entry_id                   7HZQ 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A HOH 352 ? ? O  A HOH 354 ? ? 2.02 
2 1 OD1 A ASP 27  ? ? OG A SER 43  ? ? 2.13 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     361 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     361 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_656 
_pdbx_validate_symm_contact.dist              0.62 
# 
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 CYS A 58  ? ? -49.66  150.30 
2 1 GLU A 85  ? ? -48.07  153.16 
3 1 ALA A 86  ? ? -58.13  102.88 
4 1 SER A 125 ? ? -143.37 -32.62 
5 1 ASN A 129 ? ? 71.00   37.10  
# 
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 GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 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 
A1BQ4 N1   N  N N 1   
A1BQ4 C4   C  Y N 2   
A1BQ4 C5   C  Y N 3   
A1BQ4 C6   C  Y N 4   
A1BQ4 C7   C  N N 5   
A1BQ4 C8   C  N N 6   
A1BQ4 C10  C  N N 7   
A1BQ4 C13  C  N N 8   
A1BQ4 N    N  N N 9   
A1BQ4 C    C  N N 10  
A1BQ4 O    O  N N 11  
A1BQ4 C1   C  Y N 12  
A1BQ4 C11  C  N N 13  
A1BQ4 C12  C  N S 14  
A1BQ4 C14  C  N N 15  
A1BQ4 C2   C  Y N 16  
A1BQ4 C3   C  Y N 17  
A1BQ4 C9   C  N N 18  
A1BQ4 O1   O  N N 19  
A1BQ4 O2   O  N N 20  
A1BQ4 H17  H  N N 21  
A1BQ4 H16  H  N N 22  
A1BQ4 H6   H  N N 23  
A1BQ4 H7   H  N N 24  
A1BQ4 H8   H  N N 25  
A1BQ4 H9   H  N N 26  
A1BQ4 H12  H  N N 27  
A1BQ4 H13  H  N N 28  
A1BQ4 H1   H  N N 29  
A1BQ4 H2   H  N N 30  
A1BQ4 H3   H  N N 31  
A1BQ4 H14  H  N N 32  
A1BQ4 H15  H  N N 33  
A1BQ4 H    H  N N 34  
A1BQ4 H18  H  N N 35  
A1BQ4 H19  H  N N 36  
A1BQ4 H4   H  N N 37  
A1BQ4 H5   H  N N 38  
A1BQ4 H10  H  N N 39  
A1BQ4 H11  H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
GLN   N    N  N N 128 
GLN   CA   C  N S 129 
GLN   C    C  N N 130 
GLN   O    O  N N 131 
GLN   CB   C  N N 132 
GLN   CG   C  N N 133 
GLN   CD   C  N N 134 
GLN   OE1  O  N N 135 
GLN   NE2  N  N N 136 
GLN   OXT  O  N N 137 
GLN   H    H  N N 138 
GLN   H2   H  N N 139 
GLN   HA   H  N N 140 
GLN   HB2  H  N N 141 
GLN   HB3  H  N N 142 
GLN   HG2  H  N N 143 
GLN   HG3  H  N N 144 
GLN   HE21 H  N N 145 
GLN   HE22 H  N N 146 
GLN   HXT  H  N N 147 
GLU   N    N  N N 148 
GLU   CA   C  N S 149 
GLU   C    C  N N 150 
GLU   O    O  N N 151 
GLU   CB   C  N N 152 
GLU   CG   C  N N 153 
GLU   CD   C  N N 154 
GLU   OE1  O  N N 155 
GLU   OE2  O  N N 156 
GLU   OXT  O  N N 157 
GLU   H    H  N N 158 
GLU   H2   H  N N 159 
GLU   HA   H  N N 160 
GLU   HB2  H  N N 161 
GLU   HB3  H  N N 162 
GLU   HG2  H  N N 163 
GLU   HG3  H  N N 164 
GLU   HE2  H  N N 165 
GLU   HXT  H  N N 166 
GLY   N    N  N N 167 
GLY   CA   C  N N 168 
GLY   C    C  N N 169 
GLY   O    O  N N 170 
GLY   OXT  O  N N 171 
GLY   H    H  N N 172 
GLY   H2   H  N N 173 
GLY   HA2  H  N N 174 
GLY   HA3  H  N N 175 
GLY   HXT  H  N N 176 
HIS   N    N  N N 177 
HIS   CA   C  N S 178 
HIS   C    C  N N 179 
HIS   O    O  N N 180 
HIS   CB   C  N N 181 
HIS   CG   C  Y N 182 
HIS   ND1  N  Y N 183 
HIS   CD2  C  Y N 184 
HIS   CE1  C  Y N 185 
HIS   NE2  N  Y N 186 
HIS   OXT  O  N N 187 
HIS   H    H  N N 188 
HIS   H2   H  N N 189 
HIS   HA   H  N N 190 
HIS   HB2  H  N N 191 
HIS   HB3  H  N N 192 
HIS   HD1  H  N N 193 
HIS   HD2  H  N N 194 
HIS   HE1  H  N N 195 
HIS   HE2  H  N N 196 
HIS   HXT  H  N N 197 
HOH   O    O  N N 198 
HOH   H1   H  N N 199 
HOH   H2   H  N N 200 
ILE   N    N  N N 201 
ILE   CA   C  N S 202 
ILE   C    C  N N 203 
ILE   O    O  N N 204 
ILE   CB   C  N S 205 
ILE   CG1  C  N N 206 
ILE   CG2  C  N N 207 
ILE   CD1  C  N N 208 
ILE   OXT  O  N N 209 
ILE   H    H  N N 210 
ILE   H2   H  N N 211 
ILE   HA   H  N N 212 
ILE   HB   H  N N 213 
ILE   HG12 H  N N 214 
ILE   HG13 H  N N 215 
ILE   HG21 H  N N 216 
ILE   HG22 H  N N 217 
ILE   HG23 H  N N 218 
ILE   HD11 H  N N 219 
ILE   HD12 H  N N 220 
ILE   HD13 H  N N 221 
ILE   HXT  H  N N 222 
LEU   N    N  N N 223 
LEU   CA   C  N S 224 
LEU   C    C  N N 225 
LEU   O    O  N N 226 
LEU   CB   C  N N 227 
LEU   CG   C  N N 228 
LEU   CD1  C  N N 229 
LEU   CD2  C  N N 230 
LEU   OXT  O  N N 231 
LEU   H    H  N N 232 
LEU   H2   H  N N 233 
LEU   HA   H  N N 234 
LEU   HB2  H  N N 235 
LEU   HB3  H  N N 236 
LEU   HG   H  N N 237 
LEU   HD11 H  N N 238 
LEU   HD12 H  N N 239 
LEU   HD13 H  N N 240 
LEU   HD21 H  N N 241 
LEU   HD22 H  N N 242 
LEU   HD23 H  N N 243 
LEU   HXT  H  N N 244 
LYS   N    N  N N 245 
LYS   CA   C  N S 246 
LYS   C    C  N N 247 
LYS   O    O  N N 248 
LYS   CB   C  N N 249 
LYS   CG   C  N N 250 
LYS   CD   C  N N 251 
LYS   CE   C  N N 252 
LYS   NZ   N  N N 253 
LYS   OXT  O  N N 254 
LYS   H    H  N N 255 
LYS   H2   H  N N 256 
LYS   HA   H  N N 257 
LYS   HB2  H  N N 258 
LYS   HB3  H  N N 259 
LYS   HG2  H  N N 260 
LYS   HG3  H  N N 261 
LYS   HD2  H  N N 262 
LYS   HD3  H  N N 263 
LYS   HE2  H  N N 264 
LYS   HE3  H  N N 265 
LYS   HZ1  H  N N 266 
LYS   HZ2  H  N N 267 
LYS   HZ3  H  N N 268 
LYS   HXT  H  N N 269 
MET   N    N  N N 270 
MET   CA   C  N S 271 
MET   C    C  N N 272 
MET   O    O  N N 273 
MET   CB   C  N N 274 
MET   CG   C  N N 275 
MET   SD   S  N N 276 
MET   CE   C  N N 277 
MET   OXT  O  N N 278 
MET   H    H  N N 279 
MET   H2   H  N N 280 
MET   HA   H  N N 281 
MET   HB2  H  N N 282 
MET   HB3  H  N N 283 
MET   HG2  H  N N 284 
MET   HG3  H  N N 285 
MET   HE1  H  N N 286 
MET   HE2  H  N N 287 
MET   HE3  H  N N 288 
MET   HXT  H  N N 289 
PHE   N    N  N N 290 
PHE   CA   C  N S 291 
PHE   C    C  N N 292 
PHE   O    O  N N 293 
PHE   CB   C  N N 294 
PHE   CG   C  Y N 295 
PHE   CD1  C  Y N 296 
PHE   CD2  C  Y N 297 
PHE   CE1  C  Y N 298 
PHE   CE2  C  Y N 299 
PHE   CZ   C  Y N 300 
PHE   OXT  O  N N 301 
PHE   H    H  N N 302 
PHE   H2   H  N N 303 
PHE   HA   H  N N 304 
PHE   HB2  H  N N 305 
PHE   HB3  H  N N 306 
PHE   HD1  H  N N 307 
PHE   HD2  H  N N 308 
PHE   HE1  H  N N 309 
PHE   HE2  H  N N 310 
PHE   HZ   H  N N 311 
PHE   HXT  H  N N 312 
PRO   N    N  N N 313 
PRO   CA   C  N S 314 
PRO   C    C  N N 315 
PRO   O    O  N N 316 
PRO   CB   C  N N 317 
PRO   CG   C  N N 318 
PRO   CD   C  N N 319 
PRO   OXT  O  N N 320 
PRO   H    H  N N 321 
PRO   HA   H  N N 322 
PRO   HB2  H  N N 323 
PRO   HB3  H  N N 324 
PRO   HG2  H  N N 325 
PRO   HG3  H  N N 326 
PRO   HD2  H  N N 327 
PRO   HD3  H  N N 328 
PRO   HXT  H  N N 329 
SER   N    N  N N 330 
SER   CA   C  N S 331 
SER   C    C  N N 332 
SER   O    O  N N 333 
SER   CB   C  N N 334 
SER   OG   O  N N 335 
SER   OXT  O  N N 336 
SER   H    H  N N 337 
SER   H2   H  N N 338 
SER   HA   H  N N 339 
SER   HB2  H  N N 340 
SER   HB3  H  N N 341 
SER   HG   H  N N 342 
SER   HXT  H  N N 343 
THR   N    N  N N 344 
THR   CA   C  N S 345 
THR   C    C  N N 346 
THR   O    O  N N 347 
THR   CB   C  N R 348 
THR   OG1  O  N N 349 
THR   CG2  C  N N 350 
THR   OXT  O  N N 351 
THR   H    H  N N 352 
THR   H2   H  N N 353 
THR   HA   H  N N 354 
THR   HB   H  N N 355 
THR   HG1  H  N N 356 
THR   HG21 H  N N 357 
THR   HG22 H  N N 358 
THR   HG23 H  N N 359 
THR   HXT  H  N N 360 
TRP   N    N  N N 361 
TRP   CA   C  N S 362 
TRP   C    C  N N 363 
TRP   O    O  N N 364 
TRP   CB   C  N N 365 
TRP   CG   C  Y N 366 
TRP   CD1  C  Y N 367 
TRP   CD2  C  Y N 368 
TRP   NE1  N  Y N 369 
TRP   CE2  C  Y N 370 
TRP   CE3  C  Y N 371 
TRP   CZ2  C  Y N 372 
TRP   CZ3  C  Y N 373 
TRP   CH2  C  Y N 374 
TRP   OXT  O  N N 375 
TRP   H    H  N N 376 
TRP   H2   H  N N 377 
TRP   HA   H  N N 378 
TRP   HB2  H  N N 379 
TRP   HB3  H  N N 380 
TRP   HD1  H  N N 381 
TRP   HE1  H  N N 382 
TRP   HE3  H  N N 383 
TRP   HZ2  H  N N 384 
TRP   HZ3  H  N N 385 
TRP   HH2  H  N N 386 
TRP   HXT  H  N N 387 
TYR   N    N  N N 388 
TYR   CA   C  N S 389 
TYR   C    C  N N 390 
TYR   O    O  N N 391 
TYR   CB   C  N N 392 
TYR   CG   C  Y N 393 
TYR   CD1  C  Y N 394 
TYR   CD2  C  Y N 395 
TYR   CE1  C  Y N 396 
TYR   CE2  C  Y N 397 
TYR   CZ   C  Y N 398 
TYR   OH   O  N N 399 
TYR   OXT  O  N N 400 
TYR   H    H  N N 401 
TYR   H2   H  N N 402 
TYR   HA   H  N N 403 
TYR   HB2  H  N N 404 
TYR   HB3  H  N N 405 
TYR   HD1  H  N N 406 
TYR   HD2  H  N N 407 
TYR   HE1  H  N N 408 
TYR   HE2  H  N N 409 
TYR   HH   H  N N 410 
TYR   HXT  H  N N 411 
VAL   N    N  N N 412 
VAL   CA   C  N S 413 
VAL   C    C  N N 414 
VAL   O    O  N N 415 
VAL   CB   C  N N 416 
VAL   CG1  C  N N 417 
VAL   CG2  C  N N 418 
VAL   OXT  O  N N 419 
VAL   H    H  N N 420 
VAL   H2   H  N N 421 
VAL   HA   H  N N 422 
VAL   HB   H  N N 423 
VAL   HG11 H  N N 424 
VAL   HG12 H  N N 425 
VAL   HG13 H  N N 426 
VAL   HG21 H  N N 427 
VAL   HG22 H  N N 428 
VAL   HG23 H  N N 429 
VAL   HXT  H  N N 430 
ZN    ZN   ZN N N 431 
# 
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 
A1BQ4 C   O    sing N N 1   
A1BQ4 O   C1   sing N N 2   
A1BQ4 C1  C2   doub Y N 3   
A1BQ4 C2  C3   sing Y N 4   
A1BQ4 C3  C4   doub Y N 5   
A1BQ4 C4  C5   sing Y N 6   
A1BQ4 C5  C6   doub Y N 7   
A1BQ4 C1  C6   sing Y N 8   
A1BQ4 C6  C7   sing N N 9   
A1BQ4 C7  C8   sing N N 10  
A1BQ4 O1  C8   doub N N 11  
A1BQ4 C8  N    sing N N 12  
A1BQ4 N   C9   sing N N 13  
A1BQ4 C9  C10  sing N N 14  
A1BQ4 C10 C11  sing N N 15  
A1BQ4 C11 C12  sing N N 16  
A1BQ4 C12 C13  sing N N 17  
A1BQ4 N1  C13  sing N N 18  
A1BQ4 C13 O2   doub N N 19  
A1BQ4 C14 C12  sing N N 20  
A1BQ4 N   C14  sing N N 21  
A1BQ4 N1  H17  sing N N 22  
A1BQ4 N1  H16  sing N N 23  
A1BQ4 C4  H6   sing N N 24  
A1BQ4 C5  H7   sing N N 25  
A1BQ4 C7  H8   sing N N 26  
A1BQ4 C7  H9   sing N N 27  
A1BQ4 C10 H12  sing N N 28  
A1BQ4 C10 H13  sing N N 29  
A1BQ4 C   H1   sing N N 30  
A1BQ4 C   H2   sing N N 31  
A1BQ4 C   H3   sing N N 32  
A1BQ4 C11 H14  sing N N 33  
A1BQ4 C11 H15  sing N N 34  
A1BQ4 C12 H    sing N N 35  
A1BQ4 C14 H18  sing N N 36  
A1BQ4 C14 H19  sing N N 37  
A1BQ4 C2  H4   sing N N 38  
A1BQ4 C3  H5   sing N N 39  
A1BQ4 C9  H10  sing N N 40  
A1BQ4 C9  H11  sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
GLN   N   CA   sing N N 124 
GLN   N   H    sing N N 125 
GLN   N   H2   sing N N 126 
GLN   CA  C    sing N N 127 
GLN   CA  CB   sing N N 128 
GLN   CA  HA   sing N N 129 
GLN   C   O    doub N N 130 
GLN   C   OXT  sing N N 131 
GLN   CB  CG   sing N N 132 
GLN   CB  HB2  sing N N 133 
GLN   CB  HB3  sing N N 134 
GLN   CG  CD   sing N N 135 
GLN   CG  HG2  sing N N 136 
GLN   CG  HG3  sing N N 137 
GLN   CD  OE1  doub N N 138 
GLN   CD  NE2  sing N N 139 
GLN   NE2 HE21 sing N N 140 
GLN   NE2 HE22 sing N N 141 
GLN   OXT HXT  sing N N 142 
GLU   N   CA   sing N N 143 
GLU   N   H    sing N N 144 
GLU   N   H2   sing N N 145 
GLU   CA  C    sing N N 146 
GLU   CA  CB   sing N N 147 
GLU   CA  HA   sing N N 148 
GLU   C   O    doub N N 149 
GLU   C   OXT  sing N N 150 
GLU   CB  CG   sing N N 151 
GLU   CB  HB2  sing N N 152 
GLU   CB  HB3  sing N N 153 
GLU   CG  CD   sing N N 154 
GLU   CG  HG2  sing N N 155 
GLU   CG  HG3  sing N N 156 
GLU   CD  OE1  doub N N 157 
GLU   CD  OE2  sing N N 158 
GLU   OE2 HE2  sing N N 159 
GLU   OXT HXT  sing N N 160 
GLY   N   CA   sing N N 161 
GLY   N   H    sing N N 162 
GLY   N   H2   sing N N 163 
GLY   CA  C    sing N N 164 
GLY   CA  HA2  sing N N 165 
GLY   CA  HA3  sing N N 166 
GLY   C   O    doub N N 167 
GLY   C   OXT  sing N N 168 
GLY   OXT HXT  sing N N 169 
HIS   N   CA   sing N N 170 
HIS   N   H    sing N N 171 
HIS   N   H2   sing N N 172 
HIS   CA  C    sing N N 173 
HIS   CA  CB   sing N N 174 
HIS   CA  HA   sing N N 175 
HIS   C   O    doub N N 176 
HIS   C   OXT  sing N N 177 
HIS   CB  CG   sing N N 178 
HIS   CB  HB2  sing N N 179 
HIS   CB  HB3  sing N N 180 
HIS   CG  ND1  sing Y N 181 
HIS   CG  CD2  doub Y N 182 
HIS   ND1 CE1  doub Y N 183 
HIS   ND1 HD1  sing N N 184 
HIS   CD2 NE2  sing Y N 185 
HIS   CD2 HD2  sing N N 186 
HIS   CE1 NE2  sing Y N 187 
HIS   CE1 HE1  sing N N 188 
HIS   NE2 HE2  sing N N 189 
HIS   OXT HXT  sing N N 190 
HOH   O   H1   sing N N 191 
HOH   O   H2   sing N N 192 
ILE   N   CA   sing N N 193 
ILE   N   H    sing N N 194 
ILE   N   H2   sing N N 195 
ILE   CA  C    sing N N 196 
ILE   CA  CB   sing N N 197 
ILE   CA  HA   sing N N 198 
ILE   C   O    doub N N 199 
ILE   C   OXT  sing N N 200 
ILE   CB  CG1  sing N N 201 
ILE   CB  CG2  sing N N 202 
ILE   CB  HB   sing N N 203 
ILE   CG1 CD1  sing N N 204 
ILE   CG1 HG12 sing N N 205 
ILE   CG1 HG13 sing N N 206 
ILE   CG2 HG21 sing N N 207 
ILE   CG2 HG22 sing N N 208 
ILE   CG2 HG23 sing N N 209 
ILE   CD1 HD11 sing N N 210 
ILE   CD1 HD12 sing N N 211 
ILE   CD1 HD13 sing N N 212 
ILE   OXT HXT  sing N N 213 
LEU   N   CA   sing N N 214 
LEU   N   H    sing N N 215 
LEU   N   H2   sing N N 216 
LEU   CA  C    sing N N 217 
LEU   CA  CB   sing N N 218 
LEU   CA  HA   sing N N 219 
LEU   C   O    doub N N 220 
LEU   C   OXT  sing N N 221 
LEU   CB  CG   sing N N 222 
LEU   CB  HB2  sing N N 223 
LEU   CB  HB3  sing N N 224 
LEU   CG  CD1  sing N N 225 
LEU   CG  CD2  sing N N 226 
LEU   CG  HG   sing N N 227 
LEU   CD1 HD11 sing N N 228 
LEU   CD1 HD12 sing N N 229 
LEU   CD1 HD13 sing N N 230 
LEU   CD2 HD21 sing N N 231 
LEU   CD2 HD22 sing N N 232 
LEU   CD2 HD23 sing N N 233 
LEU   OXT HXT  sing N N 234 
LYS   N   CA   sing N N 235 
LYS   N   H    sing N N 236 
LYS   N   H2   sing N N 237 
LYS   CA  C    sing N N 238 
LYS   CA  CB   sing N N 239 
LYS   CA  HA   sing N N 240 
LYS   C   O    doub N N 241 
LYS   C   OXT  sing N N 242 
LYS   CB  CG   sing N N 243 
LYS   CB  HB2  sing N N 244 
LYS   CB  HB3  sing N N 245 
LYS   CG  CD   sing N N 246 
LYS   CG  HG2  sing N N 247 
LYS   CG  HG3  sing N N 248 
LYS   CD  CE   sing N N 249 
LYS   CD  HD2  sing N N 250 
LYS   CD  HD3  sing N N 251 
LYS   CE  NZ   sing N N 252 
LYS   CE  HE2  sing N N 253 
LYS   CE  HE3  sing N N 254 
LYS   NZ  HZ1  sing N N 255 
LYS   NZ  HZ2  sing N N 256 
LYS   NZ  HZ3  sing N N 257 
LYS   OXT HXT  sing N N 258 
MET   N   CA   sing N N 259 
MET   N   H    sing N N 260 
MET   N   H2   sing N N 261 
MET   CA  C    sing N N 262 
MET   CA  CB   sing N N 263 
MET   CA  HA   sing N N 264 
MET   C   O    doub N N 265 
MET   C   OXT  sing N N 266 
MET   CB  CG   sing N N 267 
MET   CB  HB2  sing N N 268 
MET   CB  HB3  sing N N 269 
MET   CG  SD   sing N N 270 
MET   CG  HG2  sing N N 271 
MET   CG  HG3  sing N N 272 
MET   SD  CE   sing N N 273 
MET   CE  HE1  sing N N 274 
MET   CE  HE2  sing N N 275 
MET   CE  HE3  sing N N 276 
MET   OXT HXT  sing N N 277 
PHE   N   CA   sing N N 278 
PHE   N   H    sing N N 279 
PHE   N   H2   sing N N 280 
PHE   CA  C    sing N N 281 
PHE   CA  CB   sing N N 282 
PHE   CA  HA   sing N N 283 
PHE   C   O    doub N N 284 
PHE   C   OXT  sing N N 285 
PHE   CB  CG   sing N N 286 
PHE   CB  HB2  sing N N 287 
PHE   CB  HB3  sing N N 288 
PHE   CG  CD1  doub Y N 289 
PHE   CG  CD2  sing Y N 290 
PHE   CD1 CE1  sing Y N 291 
PHE   CD1 HD1  sing N N 292 
PHE   CD2 CE2  doub Y N 293 
PHE   CD2 HD2  sing N N 294 
PHE   CE1 CZ   doub Y N 295 
PHE   CE1 HE1  sing N N 296 
PHE   CE2 CZ   sing Y N 297 
PHE   CE2 HE2  sing N N 298 
PHE   CZ  HZ   sing N N 299 
PHE   OXT HXT  sing N N 300 
PRO   N   CA   sing N N 301 
PRO   N   CD   sing N N 302 
PRO   N   H    sing N N 303 
PRO   CA  C    sing N N 304 
PRO   CA  CB   sing N N 305 
PRO   CA  HA   sing N N 306 
PRO   C   O    doub N N 307 
PRO   C   OXT  sing N N 308 
PRO   CB  CG   sing N N 309 
PRO   CB  HB2  sing N N 310 
PRO   CB  HB3  sing N N 311 
PRO   CG  CD   sing N N 312 
PRO   CG  HG2  sing N N 313 
PRO   CG  HG3  sing N N 314 
PRO   CD  HD2  sing N N 315 
PRO   CD  HD3  sing N N 316 
PRO   OXT HXT  sing N N 317 
SER   N   CA   sing N N 318 
SER   N   H    sing N N 319 
SER   N   H2   sing N N 320 
SER   CA  C    sing N N 321 
SER   CA  CB   sing N N 322 
SER   CA  HA   sing N N 323 
SER   C   O    doub N N 324 
SER   C   OXT  sing N N 325 
SER   CB  OG   sing N N 326 
SER   CB  HB2  sing N N 327 
SER   CB  HB3  sing N N 328 
SER   OG  HG   sing N N 329 
SER   OXT HXT  sing N N 330 
THR   N   CA   sing N N 331 
THR   N   H    sing N N 332 
THR   N   H2   sing N N 333 
THR   CA  C    sing N N 334 
THR   CA  CB   sing N N 335 
THR   CA  HA   sing N N 336 
THR   C   O    doub N N 337 
THR   C   OXT  sing N N 338 
THR   CB  OG1  sing N N 339 
THR   CB  CG2  sing N N 340 
THR   CB  HB   sing N N 341 
THR   OG1 HG1  sing N N 342 
THR   CG2 HG21 sing N N 343 
THR   CG2 HG22 sing N N 344 
THR   CG2 HG23 sing N N 345 
THR   OXT HXT  sing N N 346 
TRP   N   CA   sing N N 347 
TRP   N   H    sing N N 348 
TRP   N   H2   sing N N 349 
TRP   CA  C    sing N N 350 
TRP   CA  CB   sing N N 351 
TRP   CA  HA   sing N N 352 
TRP   C   O    doub N N 353 
TRP   C   OXT  sing N N 354 
TRP   CB  CG   sing N N 355 
TRP   CB  HB2  sing N N 356 
TRP   CB  HB3  sing N N 357 
TRP   CG  CD1  doub Y N 358 
TRP   CG  CD2  sing Y N 359 
TRP   CD1 NE1  sing Y N 360 
TRP   CD1 HD1  sing N N 361 
TRP   CD2 CE2  doub Y N 362 
TRP   CD2 CE3  sing Y N 363 
TRP   NE1 CE2  sing Y N 364 
TRP   NE1 HE1  sing N N 365 
TRP   CE2 CZ2  sing Y N 366 
TRP   CE3 CZ3  doub Y N 367 
TRP   CE3 HE3  sing N N 368 
TRP   CZ2 CH2  doub Y N 369 
TRP   CZ2 HZ2  sing N N 370 
TRP   CZ3 CH2  sing Y N 371 
TRP   CZ3 HZ3  sing N N 372 
TRP   CH2 HH2  sing N N 373 
TRP   OXT HXT  sing N N 374 
TYR   N   CA   sing N N 375 
TYR   N   H    sing N N 376 
TYR   N   H2   sing N N 377 
TYR   CA  C    sing N N 378 
TYR   CA  CB   sing N N 379 
TYR   CA  HA   sing N N 380 
TYR   C   O    doub N N 381 
TYR   C   OXT  sing N N 382 
TYR   CB  CG   sing N N 383 
TYR   CB  HB2  sing N N 384 
TYR   CB  HB3  sing N N 385 
TYR   CG  CD1  doub Y N 386 
TYR   CG  CD2  sing Y N 387 
TYR   CD1 CE1  sing Y N 388 
TYR   CD1 HD1  sing N N 389 
TYR   CD2 CE2  doub Y N 390 
TYR   CD2 HD2  sing N N 391 
TYR   CE1 CZ   doub Y N 392 
TYR   CE1 HE1  sing N N 393 
TYR   CE2 CZ   sing Y N 394 
TYR   CE2 HE2  sing N N 395 
TYR   CZ  OH   sing N N 396 
TYR   OH  HH   sing N N 397 
TYR   OXT HXT  sing N N 398 
VAL   N   CA   sing N N 399 
VAL   N   H    sing N N 400 
VAL   N   H2   sing N N 401 
VAL   CA  C    sing N N 402 
VAL   CA  CB   sing N N 403 
VAL   CA  HA   sing N N 404 
VAL   C   O    doub N N 405 
VAL   C   OXT  sing N N 406 
VAL   CB  CG1  sing N N 407 
VAL   CB  CG2  sing N N 408 
VAL   CB  HB   sing N N 409 
VAL   CG1 HG11 sing N N 410 
VAL   CG1 HG12 sing N N 411 
VAL   CG1 HG13 sing N N 412 
VAL   CG2 HG21 sing N N 413 
VAL   CG2 HG22 sing N N 414 
VAL   CG2 HG23 sing N N 415 
VAL   OXT HXT  sing N N 416 
# 
_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                    7HZQ 
_atom_sites.fract_transf_matrix[1][1]   0.013714 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000705 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016202 
_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]   0.030508 
_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   ? 19.031 6.559   24.458 1.00 25.16 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.183 6.665   23.518 1.00 26.01 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.071 5.613   22.422 1.00 22.19 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.214 4.713   22.553 1.00 22.56 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.489 6.540   24.258 1.00 29.79 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.270 5.852   25.480 1.00 31.03 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.919 5.728   21.401 1.00 18.84 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.088 4.704   20.351 1.00 17.91 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.446 5.288   18.997 1.00 16.46 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.935 6.382   18.661 1.00 14.92 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.303 4.589   18.247 1.00 16.23 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.686 4.970   16.868 1.00 16.65 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.595 3.774   15.901 1.00 16.67 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.481 2.564   16.354 1.00 16.94 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.057 5.600   16.853 1.00 16.65 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.586 4.109   14.606 1.00 15.53 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.799 3.169   13.476 1.00 16.30 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.195 3.433   12.905 1.00 17.07 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.619 4.586   12.730 1.00 16.62 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.731 3.321   12.381 1.00 16.50 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.296 3.325   12.936 1.00 15.53 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.970 2.256   11.308 1.00 17.12 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.257 3.768   11.942 1.00 15.06 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.908 2.366   12.635 1.00 18.36 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.289 2.381   12.103 1.00 17.46 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.264 1.534   10.854 1.00 18.82 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.264 0.322   11.041 1.00 19.79 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.267 1.819   13.128 1.00 15.55 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.337 2.597   14.413 1.00 13.87 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.088 3.764   14.518 1.00 13.86 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.642 2.183   15.522 1.00 12.78 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.167 4.487   15.696 1.00 12.30 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.724 2.883   16.711 1.00 12.56 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.446 4.058   16.786 1.00 11.75 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.532 4.692   17.984 1.00 11.27 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.121 2.173   9.696  1.00 21.03 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.138 1.547   8.344  1.00 22.28 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.302 2.161   7.563  1.00 25.86 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.438 3.421   7.604  1.00 30.95 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.805 1.759   7.622  1.00 24.34 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.315 3.211   7.697  1.00 26.12 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.884 1.271   6.188  1.00 24.68 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.108 1.328   6.898  1.00 24.25 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.344 1.751   6.215  1.00 25.77 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.093 2.772   7.042  1.00 26.24 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.500 2.430   8.160  1.00 26.20 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.209 4.010   6.555  1.00 30.02 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.089 5.043   7.183  1.00 35.18 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.264 6.173   7.832  1.00 33.79 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.798 7.303   7.991  1.00 36.79 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.160 5.486   6.181  1.00 36.54 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.382 4.589   6.271  1.00 39.07 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.780 4.183   7.373  1.00 38.16 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.961 4.248   5.125  1.00 39.27 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.068 5.820   8.324  1.00 31.59 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.015 6.737   8.816  1.00 24.91 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.587 6.302   10.225 1.00 23.67 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.560 5.084   10.506 1.00 20.88 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.849 6.718   7.826  1.00 23.93 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.168 7.220   6.436  1.00 22.73 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.631 8.516   6.239  1.00 21.37 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.983 6.423   5.318  1.00 20.15 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 27.918 8.995   4.974  1.00 20.44 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.233 6.899   4.042  1.00 20.43 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.699 8.194   3.869  1.00 20.92 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 27.967 8.690   2.623  1.00 19.86 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.285 7.288   11.078 1.00 21.33 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.519 7.136   12.336 1.00 20.71 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.177 7.886   12.217 1.00 19.20 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.159 9.101   12.080 1.00 19.52 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.413 7.591   13.492 1.00 21.54 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.689 7.965   14.783 1.00 21.20 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.688 8.051   15.920 1.00 21.55 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.484 9.116   16.887 1.00 20.75 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.784 9.014   18.012 1.00 21.08 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.164 7.886   18.322 1.00 21.43 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.671 10.059  18.818 1.00 21.06 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.059 7.184   12.252 1.00 18.27 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.723 7.840   12.249 1.00 17.12 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.248 7.923   13.696 1.00 16.29 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.162 6.888   14.354 1.00 17.44 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.726 7.102   11.335 1.00 17.08 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.458 7.924   11.092 1.00 15.89 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.392 6.698   10.015 1.00 17.21 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.943 9.138   14.156 0.72 16.32 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.479 9.463   15.541 0.72 16.40 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.243 10.370  15.461 0.72 16.16 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.022 10.998  14.406 0.72 15.99 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.589 10.161  16.356 0.72 16.43 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.531 9.168   17.013 0.72 16.55 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.370 11.160  15.516 0.72 16.14 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.490 10.468  16.558 0.72 16.24 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.541 11.584  16.799 0.72 16.46 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.326 12.902  16.722 0.72 16.96 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.423 12.960  17.316 0.72 18.12 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.825 11.422  18.138 0.72 16.39 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.911 10.217  18.161 0.72 16.54 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.215 9.211   18.804 0.72 16.14 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.802 10.303  17.445 0.72 16.57 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.812 13.907  16.002 1.00 17.08 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.500 15.223  15.859 1.00 16.58 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.584 15.862  17.241 1.00 18.96 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.659 16.399  17.579 1.00 23.33 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.816 16.152  14.857 1.00 15.37 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.575 17.436  14.545 1.00 14.03 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.671 18.343  13.708 1.00 14.46 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.193 19.599  13.151 1.00 13.09 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.368 20.724  13.848 1.00 12.48 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.150 20.762  15.146 1.00 12.18 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.767 21.816  13.245 1.00 12.00 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.537 15.701  18.051 1.00 21.72 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.424 16.279  19.421 1.00 23.19 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.331 15.595  20.466 1.00 24.24 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.395 16.100  21.601 1.00 22.99 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.946 16.345  19.851 1.00 22.69 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.363 15.091  20.406 1.00 22.58 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.618 14.221  19.646 1.00 21.25 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.390 14.576  21.656 1.00 23.01 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.211 13.226  20.411 1.00 21.73 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.684 13.410  21.644 1.00 20.76 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.983 14.485  20.095 0.72 25.20 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.962 13.744  20.941 0.72 26.47 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.344 13.731  20.271 0.72 27.03 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.222 13.004  20.763 0.72 28.71 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.466 12.308  21.152 0.72 26.73 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.135 12.154  21.885 0.72 27.54 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.808 10.683  22.092 0.72 27.48 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.144 12.892  23.220 0.72 27.89 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.541 14.495  19.193 1.00 27.02 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.838 14.546  18.477 1.00 26.51 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.894 15.165  19.402 1.00 27.30 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.510 16.008  20.255 1.00 28.46 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.687 15.303  17.184 1.00 26.36 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.165 14.750  19.276 1.00 27.12 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.298 15.250  20.117 1.00 28.49 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.136 16.302  19.361 1.00 32.55 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.960 16.455  18.119 1.00 35.84 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.219 14.107  20.560 1.00 23.75 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.820 13.604  19.380 1.00 20.36 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.515 12.987  21.287 1.00 25.00 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.066 16.962  20.057 1.00 33.06 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.032 17.913  19.446 1.00 34.60 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.789 17.220  18.316 1.00 34.45 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.184 17.922  17.379 1.00 34.27 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.009 18.479  20.480 1.00 36.93 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.337 19.307  21.520 1.00 38.79 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.712 20.497  21.218 1.00 41.79 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.160 19.110  22.846 1.00 42.40 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.183 21.006  22.318 1.00 42.20 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.432 20.166  23.329 1.00 43.65 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.970 15.901  18.402 1.00 35.61 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.782 15.105  17.441 1.00 37.42 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.960 14.791  16.185 1.00 30.41 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.518 14.802  15.084 1.00 30.38 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.340 13.844  18.110 1.00 45.61 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.490 13.225  17.336 1.00 53.79 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.653 13.571  17.554 1.00 57.93 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.175 12.304  16.434 1.00 56.47 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.674 14.516  16.356 1.00 26.47 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.682 14.384  15.256 1.00 22.34 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.670 15.676  14.411 1.00 20.17 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.761 15.568  13.168 1.00 18.96 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.312 13.995  15.833 1.00 21.37 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.174 12.549  16.282 1.00 20.26 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.646 11.657  15.558 1.00 18.55 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.619 12.328  17.362 1.00 19.29 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.645 16.858  15.039 1.00 20.07 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.619 18.179  14.334 1.00 21.14 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.994 18.532  13.738 1.00 21.74 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.054 19.034  12.595 1.00 20.67 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.124 19.291  15.265 1.00 21.67 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.650 19.271  15.556 1.00 21.24 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.046 18.799  16.686 1.00 21.66 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.590 19.784  14.724 1.00 19.71 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.689 18.982  16.618 1.00 21.35 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.379 19.589  15.424 1.00 20.03 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.541 20.374  13.462 1.00 18.85 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.143 19.954  14.896 1.00 17.89 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.322 20.759  12.960 1.00 17.73 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.144 20.542  13.660 1.00 17.04 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.072 18.273  14.471 1.00 22.02 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.449 18.354  13.946 1.00 23.82 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.536 17.574  12.629 1.00 25.85 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.317 17.979  11.767 1.00 25.21 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.423 17.833  14.974 1.00 24.54 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.734 16.510  12.461 1.00 27.29 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.864 15.550  11.323 1.00 26.51 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.557 15.418  10.547 1.00 25.22 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.279 14.305  10.080 1.00 28.27 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.275 14.171  11.838 1.00 26.48 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.728 14.145  12.246 1.00 24.08 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.583 14.430  11.415 1.00 25.86 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.000 13.820  13.498 1.00 22.03 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.797 16.510  10.428 1.00 23.48 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.430 16.530  9.860  1.00 19.68 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.508 15.972  8.460  1.00 18.29 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.461 16.309  7.771  1.00 22.51 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.886 17.963  9.803  1.00 20.13 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.388 18.092  9.470  1.00 19.72 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.541 17.430  10.545 1.00 20.34 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 25.984 19.551  9.312  1.00 18.92 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.540 15.153  8.078  1.00 16.99 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.292 14.729  6.678  1.00 15.68 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.946 15.274  6.190  1.00 14.29 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.843 15.750  5.036  1.00 13.32 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.314 13.204  6.626  1.00 16.76 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.051 12.724  5.213  1.00 18.24 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.629 12.664  7.167  1.00 18.33 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.933 15.178  7.053  1.00 13.38 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.535 15.549  6.749  1.00 12.30 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.760 15.610  8.068  1.00 10.69 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.987 14.776  8.926  1.00 9.62  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.957 14.580  5.726  1.00 13.08 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.490 14.776  5.477  1.00 14.67 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.889 15.662  4.629  1.00 15.07 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.422 14.028  6.078  1.00 15.17 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.527 15.523  4.668  1.00 14.83 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.211 14.526  5.542  1.00 14.53 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.380 12.987  7.010  1.00 14.34 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.976 14.022  5.923  1.00 14.75 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.162 12.500  7.394  1.00 13.76 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.983 12.995  6.843  1.00 14.64 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.036 16.697  8.293  1.00 10.17 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.067 16.770  9.420  1.00 9.84  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.731 17.257  8.837  1.00 9.66  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.736 17.950  7.793  1.00 9.68  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.606 17.579  10.622 1.00 9.59  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.084 19.009  10.326 1.00 9.71  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.077 20.137  10.111 1.00 9.92  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.432 21.103  9.354  1.00 10.42 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.965 20.114  10.725 1.00 9.97  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.625 16.880  9.478  1.00 9.59  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.273 17.404  9.152  1.00 9.58  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.462 17.550  10.446 1.00 9.40  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.952 16.556  10.955 1.00 9.67  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.571 16.529  8.117  1.00 9.40  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.407 17.220  7.437  1.00 9.72  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.818 18.164  8.021  1.00 9.23  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.077 16.783  6.325  1.00 10.70 ? 35  ASP   A OD2 1 
ATOM   240  N  N   A SER   A 1 30  ? 16.363 18.788  10.933 0.36 9.36  ? 36  SER   A N   1 
ATOM   241  N  N   B SER   A 1 30  ? 16.346 18.780  10.948 0.36 9.40  ? 36  SER   A N   1 
ATOM   242  C  CA  A SER   A 1 30  ? 15.559 19.228  12.106 0.36 9.60  ? 36  SER   A CA  1 
ATOM   243  C  CA  B SER   A 1 30  ? 15.558 19.149  12.156 0.36 9.65  ? 36  SER   A CA  1 
ATOM   244  C  C   A SER   A 1 30  ? 14.141 18.637  12.064 0.36 9.54  ? 36  SER   A C   1 
ATOM   245  C  C   B SER   A 1 30  ? 14.125 18.604  12.073 0.36 9.57  ? 36  SER   A C   1 
ATOM   246  O  O   A SER   A 1 30  ? 13.665 18.164  13.097 0.36 9.85  ? 36  SER   A O   1 
ATOM   247  O  O   B SER   A 1 30  ? 13.616 18.129  13.090 0.36 9.89  ? 36  SER   A O   1 
ATOM   248  C  CB  A SER   A 1 30  ? 15.531 20.740  12.156 0.36 9.51  ? 36  SER   A CB  1 
ATOM   249  C  CB  B SER   A 1 30  ? 15.564 20.644  12.346 0.36 9.61  ? 36  SER   A CB  1 
ATOM   250  O  OG  A SER   A 1 30  ? 14.882 21.209  13.324 0.36 9.47  ? 36  SER   A OG  1 
ATOM   251  O  OG  B SER   A 1 30  ? 15.023 21.284  11.206 0.36 9.62  ? 36  SER   A OG  1 
ATOM   252  N  N   . SER   A 1 31  ? 13.485 18.686  10.905 1.00 9.73  ? 37  SER   A N   1 
ATOM   253  C  CA  . SER   A 1 31  ? 12.074 18.264  10.725 1.00 9.67  ? 37  SER   A CA  1 
ATOM   254  C  C   . SER   A 1 31  ? 11.901 16.740  10.780 1.00 9.52  ? 37  SER   A C   1 
ATOM   255  O  O   . SER   A 1 31  ? 10.745 16.313  10.966 1.00 9.22  ? 37  SER   A O   1 
ATOM   256  C  CB  . SER   A 1 31  ? 11.550 18.792  9.447  1.00 10.16 ? 37  SER   A CB  1 
ATOM   257  O  OG  . SER   A 1 31  ? 12.119 18.068  8.392  1.00 10.65 ? 37  SER   A OG  1 
ATOM   258  N  N   . ARG   A 1 32  ? 12.966 15.971  10.578 1.00 8.90  ? 38  ARG   A N   1 
ATOM   259  C  CA  . ARG   A 1 32  ? 12.978 14.491  10.690 1.00 9.13  ? 38  ARG   A CA  1 
ATOM   260  C  C   . ARG   A 1 32  ? 13.576 14.024  12.017 1.00 9.42  ? 38  ARG   A C   1 
ATOM   261  O  O   . ARG   A 1 32  ? 13.500 12.775  12.290 1.00 10.86 ? 38  ARG   A O   1 
ATOM   262  C  CB  . ARG   A 1 32  ? 13.795 13.905  9.539  1.00 8.82  ? 38  ARG   A CB  1 
ATOM   263  C  CG  . ARG   A 1 32  ? 13.236 14.273  8.180  1.00 8.61  ? 38  ARG   A CG  1 
ATOM   264  C  CD  . ARG   A 1 32  ? 13.941 13.603  7.052  1.00 8.47  ? 38  ARG   A CD  1 
ATOM   265  N  NE  . ARG   A 1 32  ? 13.963 12.148  7.167  1.00 8.51  ? 38  ARG   A NE  1 
ATOM   266  C  CZ  . ARG   A 1 32  ? 14.074 11.324  6.140  1.00 9.37  ? 38  ARG   A CZ  1 
ATOM   267  N  NH1 . ARG   A 1 32  ? 14.150 11.795  4.911  1.00 10.10 ? 38  ARG   A NH1 1 
ATOM   268  N  NH2 . ARG   A 1 32  ? 14.116 10.017  6.311  1.00 9.69  ? 38  ARG   A NH2 1 
ATOM   269  N  N   . ASP   A 1 33  ? 14.247 14.928  12.735 1.00 9.81  ? 39  ASP   A N   1 
ATOM   270  C  CA  . ASP   A 1 33  ? 14.983 14.682  14.006 1.00 9.75  ? 39  ASP   A CA  1 
ATOM   271  C  C   . ASP   A 1 33  ? 16.079 13.678  13.712 1.00 10.39 ? 39  ASP   A C   1 
ATOM   272  O  O   . ASP   A 1 33  ? 16.116 12.656  14.442 1.00 10.60 ? 39  ASP   A O   1 
ATOM   273  C  CB  . ASP   A 1 33  ? 14.039 14.204  15.109 1.00 9.88  ? 39  ASP   A CB  1 
ATOM   274  C  CG  . ASP   A 1 33  ? 14.762 13.893  16.398 1.00 10.18 ? 39  ASP   A CG  1 
ATOM   275  O  OD1 . ASP   A 1 33  ? 15.529 14.749  16.826 1.00 10.73 ? 39  ASP   A OD1 1 
ATOM   276  O  OD2 . ASP   A 1 33  ? 14.570 12.764  16.940 1.00 10.52 ? 39  ASP   A OD2 1 
ATOM   277  N  N   . LEU   A 1 34  ? 16.834 13.912  12.615 1.00 10.14 ? 40  LEU   A N   1 
ATOM   278  C  CA  . LEU   A 1 34  ? 17.891 12.995  12.092 1.00 10.59 ? 40  LEU   A CA  1 
ATOM   279  C  C   . LEU   A 1 34  ? 19.188 13.786  11.891 1.00 10.47 ? 40  LEU   A C   1 
ATOM   280  O  O   . LEU   A 1 34  ? 19.174 14.893  11.358 1.00 8.81  ? 40  LEU   A O   1 
ATOM   281  C  CB  . LEU   A 1 34  ? 17.521 12.336  10.753 1.00 10.09 ? 40  LEU   A CB  1 
ATOM   282  C  CG  . LEU   A 1 34  ? 16.649 11.093  10.796 1.00 10.14 ? 40  LEU   A CG  1 
ATOM   283  C  CD1 . LEU   A 1 34  ? 16.737 10.348  9.458  1.00 9.84  ? 40  LEU   A CD1 1 
ATOM   284  C  CD2 . LEU   A 1 34  ? 17.027 10.184  11.974 1.00 9.93  ? 40  LEU   A CD2 1 
ATOM   285  N  N   . LEU   A 1 35  ? 20.285 13.176  12.294 1.00 12.24 ? 41  LEU   A N   1 
ATOM   286  C  CA  . LEU   A 1 35  ? 21.637 13.694  11.983 1.00 13.35 ? 41  LEU   A CA  1 
ATOM   287  C  C   . LEU   A 1 35  ? 22.500 12.484  11.650 1.00 14.61 ? 41  LEU   A C   1 
ATOM   288  O  O   . LEU   A 1 35  ? 22.352 11.485  12.361 1.00 15.37 ? 41  LEU   A O   1 
ATOM   289  C  CB  . LEU   A 1 35  ? 22.160 14.484  13.192 1.00 13.78 ? 41  LEU   A CB  1 
ATOM   290  C  CG  . LEU   A 1 35  ? 23.591 14.979  13.082 1.00 14.05 ? 41  LEU   A CG  1 
ATOM   291  C  CD1 . LEU   A 1 35  ? 23.759 16.268  13.836 1.00 14.70 ? 41  LEU   A CD1 1 
ATOM   292  C  CD2 . LEU   A 1 35  ? 24.576 13.914  13.557 1.00 14.87 ? 41  LEU   A CD2 1 
ATOM   293  N  N   . VAL   A 1 36  ? 23.313 12.585  10.592 1.00 15.56 ? 42  VAL   A N   1 
ATOM   294  C  CA  . VAL   A 1 36  ? 24.390 11.620  10.239 1.00 16.58 ? 42  VAL   A CA  1 
ATOM   295  C  C   . VAL   A 1 36  ? 25.746 12.342  10.388 1.00 16.82 ? 42  VAL   A C   1 
ATOM   296  O  O   . VAL   A 1 36  ? 25.912 13.474  9.841  1.00 16.12 ? 42  VAL   A O   1 
ATOM   297  C  CB  . VAL   A 1 36  ? 24.194 11.039  8.825  1.00 16.31 ? 42  VAL   A CB  1 
ATOM   298  C  CG1 . VAL   A 1 36  ? 25.311 10.060  8.472  1.00 17.40 ? 42  VAL   A CG1 1 
ATOM   299  C  CG2 . VAL   A 1 36  ? 22.821 10.419  8.622  1.00 16.25 ? 42  VAL   A CG2 1 
ATOM   300  N  N   . SER   A 1 37  ? 26.661 11.719  11.120 1.00 18.58 ? 43  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 37  ? 28.121 12.025  11.183 1.00 21.35 ? 43  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 37  ? 28.959 10.885  10.591 1.00 24.31 ? 43  SER   A C   1 
ATOM   303  O  O   . SER   A 1 37  ? 28.487 9.708   10.560 1.00 20.89 ? 43  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 37  ? 28.546 12.293  12.594 1.00 22.69 ? 43  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 37  ? 28.034 11.301  13.491 1.00 22.89 ? 43  SER   A OG  1 
ATOM   306  N  N   . SER   A 1 38  ? 30.185 11.221  10.166 1.00 28.71 ? 44  SER   A N   1 
ATOM   307  C  CA  . SER   A 1 38  ? 31.149 10.297  9.509  1.00 30.61 ? 44  SER   A CA  1 
ATOM   308  C  C   . SER   A 1 38  ? 31.959 9.556   10.577 1.00 32.99 ? 44  SER   A C   1 
ATOM   309  O  O   . SER   A 1 38  ? 32.359 10.218  11.559 1.00 35.17 ? 44  SER   A O   1 
ATOM   310  C  CB  . SER   A 1 38  ? 32.037 11.071  8.579  1.00 31.02 ? 44  SER   A CB  1 
ATOM   311  O  OG  . SER   A 1 38  ? 32.605 12.170  9.277  1.00 31.38 ? 44  SER   A OG  1 
ATOM   312  N  N   . THR   A 1 39  ? 32.189 8.243   10.411 1.00 35.28 ? 45  THR   A N   1 
ATOM   313  C  CA  . THR   A 1 39  ? 33.042 7.424   11.329 1.00 38.04 ? 45  THR   A CA  1 
ATOM   314  C  C   . THR   A 1 39  ? 34.368 7.022   10.658 1.00 40.99 ? 45  THR   A C   1 
ATOM   315  O  O   . THR   A 1 39  ? 34.405 6.862   9.405  1.00 45.86 ? 45  THR   A O   1 
ATOM   316  C  CB  . THR   A 1 39  ? 32.348 6.138   11.794 1.00 36.88 ? 45  THR   A CB  1 
ATOM   317  O  OG1 . THR   A 1 39  ? 31.995 5.436   10.603 1.00 38.46 ? 45  THR   A OG1 1 
ATOM   318  C  CG2 . THR   A 1 39  ? 31.143 6.379   12.678 1.00 35.85 ? 45  THR   A CG2 1 
ATOM   319  N  N   . THR   A 1 40  ? 35.405 6.802   11.473 1.00 43.13 ? 46  THR   A N   1 
ATOM   320  C  CA  . THR   A 1 40  ? 36.757 6.347   11.031 1.00 43.02 ? 46  THR   A CA  1 
ATOM   321  C  C   . THR   A 1 40  ? 36.699 4.833   10.794 1.00 47.27 ? 46  THR   A C   1 
ATOM   322  O  O   . THR   A 1 40  ? 37.158 4.380   9.724  1.00 47.81 ? 46  THR   A O   1 
ATOM   323  C  CB  . THR   A 1 40  ? 37.819 6.795   12.041 1.00 41.28 ? 46  THR   A CB  1 
ATOM   324  O  OG1 . THR   A 1 40  ? 37.253 6.770   13.347 1.00 41.10 ? 46  THR   A OG1 1 
ATOM   325  C  CG2 . THR   A 1 40  ? 38.316 8.198   11.787 1.00 40.80 ? 46  THR   A CG2 1 
ATOM   326  N  N   . ALA   A 1 41  ? 36.083 4.108   11.741 1.00 52.36 ? 47  ALA   A N   1 
ATOM   327  C  CA  . ALA   A 1 41  ? 35.730 2.668   11.681 1.00 46.95 ? 47  ALA   A CA  1 
ATOM   328  C  C   . ALA   A 1 41  ? 34.728 2.373   10.554 1.00 47.78 ? 47  ALA   A C   1 
ATOM   329  O  O   . ALA   A 1 41  ? 34.283 3.329   9.883  1.00 50.70 ? 47  ALA   A O   1 
ATOM   330  C  CB  . ALA   A 1 41  ? 35.166 2.256   13.013 1.00 43.66 ? 47  ALA   A CB  1 
ATOM   331  N  N   . GLN   A 1 42  ? 34.411 1.083   10.354 1.00 51.32 ? 48  GLN   A N   1 
ATOM   332  C  CA  . GLN   A 1 42  ? 33.386 0.564   9.395  1.00 52.19 ? 48  GLN   A CA  1 
ATOM   333  C  C   . GLN   A 1 42  ? 32.237 -0.059  10.194 1.00 48.07 ? 48  GLN   A C   1 
ATOM   334  O  O   . GLN   A 1 42  ? 32.523 -0.593  11.267 1.00 45.99 ? 48  GLN   A O   1 
ATOM   335  C  CB  . GLN   A 1 42  ? 33.990 -0.476  8.447  1.00 53.21 ? 48  GLN   A CB  1 
ATOM   336  C  CG  . GLN   A 1 42  ? 33.033 -0.956  7.359  1.00 55.31 ? 48  GLN   A CG  1 
ATOM   337  C  CD  . GLN   A 1 42  ? 32.934 0.016   6.211  1.00 57.94 ? 48  GLN   A CD  1 
ATOM   338  O  OE1 . GLN   A 1 42  ? 33.358 1.165   6.306  1.00 60.44 ? 48  GLN   A OE1 1 
ATOM   339  N  NE2 . GLN   A 1 42  ? 32.388 -0.450  5.101  1.00 57.84 ? 48  GLN   A NE2 1 
ATOM   340  N  N   . GLY   A 1 43  ? 31.003 0.019   9.672  1.00 47.91 ? 49  GLY   A N   1 
ATOM   341  C  CA  . GLY   A 1 43  ? 29.756 -0.475  10.296 1.00 45.34 ? 49  GLY   A CA  1 
ATOM   342  C  C   . GLY   A 1 43  ? 28.934 -1.326  9.340  1.00 42.33 ? 49  GLY   A C   1 
ATOM   343  O  O   . GLY   A 1 43  ? 28.909 -1.046  8.125  1.00 43.77 ? 49  GLY   A O   1 
ATOM   344  N  N   . CYS   A 1 44  ? 28.276 -2.355  9.857  1.00 42.61 ? 50  CYS   A N   1 
ATOM   345  C  CA  . CYS   A 1 44  ? 27.669 -3.427  9.027  1.00 42.36 ? 50  CYS   A CA  1 
ATOM   346  C  C   . CYS   A 1 44  ? 26.210 -3.680  9.462  1.00 39.19 ? 50  CYS   A C   1 
ATOM   347  O  O   . CYS   A 1 44  ? 25.701 -4.804  9.247  1.00 44.68 ? 50  CYS   A O   1 
ATOM   348  C  CB  . CYS   A 1 44  ? 28.577 -4.660  9.016  1.00 43.07 ? 50  CYS   A CB  1 
ATOM   349  S  SG  . CYS   A 1 44  ? 29.591 -4.918  10.505 1.00 48.58 ? 50  CYS   A SG  1 
ATOM   350  N  N   . ASP   A 1 45  ? 25.518 -2.655  9.981  1.00 35.78 ? 51  ASP   A N   1 
ATOM   351  C  CA  . ASP   A 1 45  ? 24.033 -2.671  10.134 1.00 30.76 ? 51  ASP   A CA  1 
ATOM   352  C  C   . ASP   A 1 45  ? 23.393 -2.667  8.740  1.00 26.98 ? 51  ASP   A C   1 
ATOM   353  O  O   . ASP   A 1 45  ? 23.757 -1.852  7.929  1.00 27.64 ? 51  ASP   A O   1 
ATOM   354  C  CB  . ASP   A 1 45  ? 23.506 -1.495  10.968 1.00 29.97 ? 51  ASP   A CB  1 
ATOM   355  C  CG  . ASP   A 1 45  ? 23.415 -1.769  12.456 1.00 30.48 ? 51  ASP   A CG  1 
ATOM   356  O  OD1 . ASP   A 1 45  ? 23.131 -2.944  12.829 1.00 31.17 ? 51  ASP   A OD1 1 
ATOM   357  O  OD2 . ASP   A 1 45  ? 23.627 -0.812  13.232 1.00 26.29 ? 51  ASP   A OD2 1 
ATOM   358  N  N   . THR   A 1 46  ? 22.414 -3.523  8.492  1.00 28.08 ? 52  THR   A N   1 
ATOM   359  C  CA  . THR   A 1 46  ? 21.690 -3.588  7.198  1.00 26.83 ? 52  THR   A CA  1 
ATOM   360  C  C   . THR   A 1 46  ? 20.520 -2.630  7.300  1.00 25.02 ? 52  THR   A C   1 
ATOM   361  O  O   . THR   A 1 46  ? 19.787 -2.759  8.271  1.00 25.71 ? 52  THR   A O   1 
ATOM   362  C  CB  . THR   A 1 46  ? 21.242 -5.024  6.863  1.00 27.75 ? 52  THR   A CB  1 
ATOM   363  O  OG1 . THR   A 1 46  ? 22.399 -5.866  6.818  1.00 30.95 ? 52  THR   A OG1 1 
ATOM   364  C  CG2 . THR   A 1 46  ? 20.529 -5.124  5.535  1.00 28.66 ? 52  THR   A CG2 1 
ATOM   365  N  N   . ILE   A 1 47  ? 20.396 -1.687  6.363  1.00 25.00 ? 53  ILE   A N   1 
ATOM   366  C  CA  . ILE   A 1 47  ? 19.201 -0.810  6.231  1.00 23.45 ? 53  ILE   A CA  1 
ATOM   367  C  C   . ILE   A 1 47  ? 18.228 -1.556  5.325  1.00 24.08 ? 53  ILE   A C   1 
ATOM   368  O  O   . ILE   A 1 47  ? 18.699 -2.100  4.312  1.00 24.96 ? 53  ILE   A O   1 
ATOM   369  C  CB  . ILE   A 1 47  ? 19.518 0.604   5.682  1.00 22.72 ? 53  ILE   A CB  1 
ATOM   370  C  CG1 . ILE   A 1 47  ? 20.754 1.239   6.332  1.00 21.41 ? 53  ILE   A CG1 1 
ATOM   371  C  CG2 . ILE   A 1 47  ? 18.291 1.511   5.798  1.00 21.78 ? 53  ILE   A CG2 1 
ATOM   372  C  CD1 . ILE   A 1 47  ? 20.705 1.285   7.830  1.00 21.40 ? 53  ILE   A CD1 1 
ATOM   373  N  N   . ALA   A 1 48  ? 16.948 -1.567  5.713  1.00 22.36 ? 54  ALA   A N   1 
ATOM   374  C  CA  . ALA   A 1 48  ? 15.797 -2.185  5.024  1.00 20.33 ? 54  ALA   A CA  1 
ATOM   375  C  C   . ALA   A 1 48  ? 15.374 -1.260  3.905  1.00 20.82 ? 54  ALA   A C   1 
ATOM   376  O  O   . ALA   A 1 48  ? 15.296 -0.058  4.155  1.00 21.86 ? 54  ALA   A O   1 
ATOM   377  C  CB  . ALA   A 1 48  ? 14.641 -2.366  5.977  1.00 18.94 ? 54  ALA   A CB  1 
ATOM   378  N  N   . ARG   A 1 49  ? 15.048 -1.841  2.753  1.00 21.86 ? 55  ARG   A N   1 
ATOM   379  C  CA  . ARG   A 1 49  ? 14.511 -1.148  1.561  1.00 21.29 ? 55  ARG   A CA  1 
ATOM   380  C  C   . ARG   A 1 49  ? 13.207 -1.875  1.226  1.00 22.22 ? 55  ARG   A C   1 
ATOM   381  O  O   . ARG   A 1 49  ? 13.276 -2.931  0.560  1.00 20.56 ? 55  ARG   A O   1 
ATOM   382  C  CB  . ARG   A 1 49  ? 15.574 -1.155  0.452  1.00 21.90 ? 55  ARG   A CB  1 
ATOM   383  C  CG  . ARG   A 1 49  ? 16.929 -0.583  0.861  1.00 21.84 ? 55  ARG   A CG  1 
ATOM   384  C  CD  . ARG   A 1 49  ? 16.982 0.923   1.184  1.00 22.02 ? 55  ARG   A CD  1 
ATOM   385  N  NE  . ARG   A 1 49  ? 18.341 1.329   1.592  1.00 21.77 ? 55  ARG   A NE  1 
ATOM   386  C  CZ  . ARG   A 1 49  ? 18.646 2.410   2.309  1.00 22.38 ? 55  ARG   A CZ  1 
ATOM   387  N  NH1 . ARG   A 1 49  ? 17.706 3.257   2.706  1.00 23.29 ? 55  ARG   A NH1 1 
ATOM   388  N  NH2 . ARG   A 1 49  ? 19.902 2.653   2.621  1.00 22.76 ? 55  ARG   A NH2 1 
ATOM   389  N  N   . CYS   A 1 50  ? 12.086 -1.388  1.773  1.00 21.15 ? 56  CYS   A N   1 
ATOM   390  C  CA  . CYS   A 1 50  ? 10.804 -2.134  1.856  1.00 22.01 ? 56  CYS   A CA  1 
ATOM   391  C  C   . CYS   A 1 50  ? 9.725  -1.153  2.263  1.00 22.26 ? 56  CYS   A C   1 
ATOM   392  O  O   . CYS   A 1 50  ? 10.117 -0.100  2.726  1.00 24.07 ? 56  CYS   A O   1 
ATOM   393  C  CB  . CYS   A 1 50  ? 10.853 -3.214  2.923  1.00 23.73 ? 56  CYS   A CB  1 
ATOM   394  S  SG  . CYS   A 1 50  ? 10.681 -2.596  4.625  1.00 24.83 ? 56  CYS   A SG  1 
ATOM   395  N  N   . ASP   A 1 51  ? 8.442  -1.512  2.148  1.00 22.68 ? 57  ASP   A N   1 
ATOM   396  C  CA  . ASP   A 1 51  ? 7.339  -0.756  2.802  1.00 20.90 ? 57  ASP   A CA  1 
ATOM   397  C  C   . ASP   A 1 51  ? 6.617  -1.647  3.822  1.00 18.54 ? 57  ASP   A C   1 
ATOM   398  O  O   . ASP   A 1 51  ? 5.417  -1.513  3.908  1.00 17.55 ? 57  ASP   A O   1 
ATOM   399  C  CB  . ASP   A 1 51  ? 6.374  -0.174  1.762  1.00 23.75 ? 57  ASP   A CB  1 
ATOM   400  C  CG  . ASP   A 1 51  ? 5.414  -1.188  1.137  1.00 25.20 ? 57  ASP   A CG  1 
ATOM   401  O  OD1 . ASP   A 1 51  ? 5.785  -2.389  1.080  1.00 27.19 ? 57  ASP   A OD1 1 
ATOM   402  O  OD2 . ASP   A 1 51  ? 4.286  -0.775  0.734  1.00 23.11 ? 57  ASP   A OD2 1 
ATOM   403  N  N   . CYS   A 1 52  ? 7.338  -2.499  4.568  1.00 17.62 ? 58  CYS   A N   1 
ATOM   404  C  CA  . CYS   A 1 52  ? 6.864  -3.279  5.750  1.00 17.09 ? 58  CYS   A CA  1 
ATOM   405  C  C   . CYS   A 1 52  ? 6.143  -2.363  6.732  1.00 16.51 ? 58  CYS   A C   1 
ATOM   406  O  O   . CYS   A 1 52  ? 6.549  -1.196  6.825  1.00 19.73 ? 58  CYS   A O   1 
ATOM   407  C  CB  . CYS   A 1 52  ? 7.995  -3.862  6.583  1.00 17.38 ? 58  CYS   A CB  1 
ATOM   408  S  SG  . CYS   A 1 52  ? 8.867  -5.242  5.821  1.00 18.98 ? 58  CYS   A SG  1 
ATOM   409  N  N   . GLN   A 1 53  ? 5.180  -2.884  7.479  1.00 13.43 ? 59  GLN   A N   1 
ATOM   410  C  CA  . GLN   A 1 53  ? 4.481  -2.101  8.517  1.00 13.32 ? 59  GLN   A CA  1 
ATOM   411  C  C   . GLN   A 1 53  ? 4.328  -2.931  9.787  1.00 11.89 ? 59  GLN   A C   1 
ATOM   412  O  O   . GLN   A 1 53  ? 3.398  -2.677  10.538 1.00 10.49 ? 59  GLN   A O   1 
ATOM   413  C  CB  . GLN   A 1 53  ? 3.096  -1.682  8.014  1.00 14.60 ? 59  GLN   A CB  1 
ATOM   414  C  CG  . GLN   A 1 53  ? 3.103  -0.444  7.119  1.00 15.84 ? 59  GLN   A CG  1 
ATOM   415  C  CD  . GLN   A 1 53  ? 1.699  -0.150  6.663  1.00 16.59 ? 59  GLN   A CD  1 
ATOM   416  O  OE1 . GLN   A 1 53  ? 1.353  -0.411  5.506  1.00 19.30 ? 59  GLN   A OE1 1 
ATOM   417  N  NE2 . GLN   A 1 53  ? 0.869  0.332   7.584  1.00 15.56 ? 59  GLN   A NE2 1 
ATOM   418  N  N   . THR   A 1 54  ? 5.190  -3.927  9.970  1.00 10.62 ? 60  THR   A N   1 
ATOM   419  C  CA  . THR   A 1 54  ? 5.342  -4.683  11.228 1.00 9.23  ? 60  THR   A CA  1 
ATOM   420  C  C   . THR   A 1 54  ? 6.834  -4.918  11.426 1.00 9.02  ? 60  THR   A C   1 
ATOM   421  O  O   . THR   A 1 54  ? 7.614  -5.035  10.409 1.00 8.16  ? 60  THR   A O   1 
ATOM   422  C  CB  . THR   A 1 54  ? 4.542  -5.995  11.229 1.00 9.36  ? 60  THR   A CB  1 
ATOM   423  O  OG1 . THR   A 1 54  ? 5.311  -6.925  10.466 1.00 8.70  ? 60  THR   A OG1 1 
ATOM   424  C  CG2 . THR   A 1 54  ? 3.128  -5.888  10.695 1.00 8.78  ? 60  THR   A CG2 1 
ATOM   425  N  N   . GLY   A 1 55  ? 7.228  -4.997  12.684 1.00 8.66  ? 61  GLY   A N   1 
ATOM   426  C  CA  . GLY   A 1 55  ? 8.645  -4.915  13.054 1.00 9.30  ? 61  GLY   A CA  1 
ATOM   427  C  C   . GLY   A 1 55  ? 8.827  -5.134  14.530 1.00 9.28  ? 61  GLY   A C   1 
ATOM   428  O  O   . GLY   A 1 55  ? 7.851  -5.461  15.177 1.00 9.51  ? 61  GLY   A O   1 
ATOM   429  N  N   . VAL   A 1 56  ? 10.050 -4.954  15.013 1.00 9.70  ? 62  VAL   A N   1 
ATOM   430  C  CA  . VAL   A 1 56  ? 10.443 -5.172  16.431 1.00 10.13 ? 62  VAL   A CA  1 
ATOM   431  C  C   . VAL   A 1 56  ? 11.308 -3.976  16.832 1.00 9.99  ? 62  VAL   A C   1 
ATOM   432  O  O   . VAL   A 1 56  ? 12.260 -3.697  16.094 1.00 9.61  ? 62  VAL   A O   1 
ATOM   433  C  CB  . VAL   A 1 56  ? 11.156 -6.528  16.587 1.00 10.26 ? 62  VAL   A CB  1 
ATOM   434  C  CG1 . VAL   A 1 56  ? 11.697 -6.747  17.988 1.00 10.85 ? 62  VAL   A CG1 1 
ATOM   435  C  CG2 . VAL   A 1 56  ? 10.229 -7.670  16.223 1.00 10.42 ? 62  VAL   A CG2 1 
ATOM   436  N  N   . TYR   A 1 57  ? 11.013 -3.324  17.959 1.00 10.11 ? 63  TYR   A N   1 
ATOM   437  C  CA  . TYR   A 1 57  ? 11.798 -2.167  18.445 1.00 10.42 ? 63  TYR   A CA  1 
ATOM   438  C  C   . TYR   A 1 57  ? 12.328 -2.469  19.851 1.00 11.41 ? 63  TYR   A C   1 
ATOM   439  O  O   . TYR   A 1 57  ? 11.652 -3.125  20.615 1.00 10.77 ? 63  TYR   A O   1 
ATOM   440  C  CB  . TYR   A 1 57  ? 11.006 -0.862  18.386 1.00 10.13 ? 63  TYR   A CB  1 
ATOM   441  C  CG  . TYR   A 1 57  ? 10.044 -0.619  19.516 1.00 9.92  ? 63  TYR   A CG  1 
ATOM   442  C  CD1 . TYR   A 1 57  ? 8.770  -1.178  19.515 1.00 9.64  ? 63  TYR   A CD1 1 
ATOM   443  C  CD2 . TYR   A 1 57  ? 10.403 0.180   20.591 1.00 9.93  ? 63  TYR   A CD2 1 
ATOM   444  C  CE1 . TYR   A 1 57  ? 7.882  -0.931  20.545 1.00 9.51  ? 63  TYR   A CE1 1 
ATOM   445  C  CE2 . TYR   A 1 57  ? 9.526  0.433   21.635 1.00 9.57  ? 63  TYR   A CE2 1 
ATOM   446  C  CZ  . TYR   A 1 57  ? 8.268  -0.134  21.612 1.00 9.65  ? 63  TYR   A CZ  1 
ATOM   447  O  OH  . TYR   A 1 57  ? 7.414  0.093   22.651 1.00 9.73  ? 63  TYR   A OH  1 
ATOM   448  N  N   . TYR   A 1 58  ? 13.548 -2.011  20.135 1.00 12.25 ? 64  TYR   A N   1 
ATOM   449  C  CA  . TYR   A 1 58  ? 14.187 -2.135  21.454 1.00 13.65 ? 64  TYR   A CA  1 
ATOM   450  C  C   . TYR   A 1 58  ? 13.697 -0.985  22.321 1.00 14.73 ? 64  TYR   A C   1 
ATOM   451  O  O   . TYR   A 1 58  ? 13.687 0.176   21.850 1.00 13.09 ? 64  TYR   A O   1 
ATOM   452  C  CB  . TYR   A 1 58  ? 15.710 -2.208  21.368 1.00 14.13 ? 64  TYR   A CB  1 
ATOM   453  C  CG  . TYR   A 1 58  ? 16.315 -2.355  22.730 1.00 14.93 ? 64  TYR   A CG  1 
ATOM   454  C  CD1 . TYR   A 1 58  ? 16.105 -3.487  23.502 1.00 16.10 ? 64  TYR   A CD1 1 
ATOM   455  C  CD2 . TYR   A 1 58  ? 17.060 -1.328  23.269 1.00 17.13 ? 64  TYR   A CD2 1 
ATOM   456  C  CE1 . TYR   A 1 58  ? 16.633 -3.606  24.779 1.00 16.54 ? 64  TYR   A CE1 1 
ATOM   457  C  CE2 . TYR   A 1 58  ? 17.593 -1.419  24.539 1.00 17.35 ? 64  TYR   A CE2 1 
ATOM   458  C  CZ  . TYR   A 1 58  ? 17.364 -2.552  25.294 1.00 17.56 ? 64  TYR   A CZ  1 
ATOM   459  O  OH  . TYR   A 1 58  ? 17.906 -2.568  26.539 1.00 21.20 ? 64  TYR   A OH  1 
ATOM   460  N  N   . CYS   A 1 59  ? 13.271 -1.326  23.542 1.00 16.03 ? 65  CYS   A N   1 
ATOM   461  C  CA  . CYS   A 1 59  ? 12.699 -0.372  24.525 1.00 17.95 ? 65  CYS   A CA  1 
ATOM   462  C  C   . CYS   A 1 59  ? 13.576 -0.354  25.776 1.00 18.89 ? 65  CYS   A C   1 
ATOM   463  O  O   . CYS   A 1 59  ? 13.398 -1.227  26.631 1.00 19.41 ? 65  CYS   A O   1 
ATOM   464  C  CB  . CYS   A 1 59  ? 11.274 -0.747  24.888 1.00 17.88 ? 65  CYS   A CB  1 
ATOM   465  S  SG  . CYS   A 1 59  ? 10.518 0.496   25.961 1.00 18.82 ? 65  CYS   A SG  1 
ATOM   466  N  N   . SER   A 1 60  ? 14.477 0.615   25.870 1.00 18.81 ? 66  SER   A N   1 
ATOM   467  C  CA  . SER   A 1 60  ? 15.520 0.663   26.919 1.00 21.76 ? 66  SER   A CA  1 
ATOM   468  C  C   . SER   A 1 60  ? 14.875 0.760   28.298 1.00 21.07 ? 66  SER   A C   1 
ATOM   469  O  O   . SER   A 1 60  ? 15.419 0.163   29.211 1.00 22.01 ? 66  SER   A O   1 
ATOM   470  C  CB  . SER   A 1 60  ? 16.503 1.781   26.706 1.00 22.62 ? 66  SER   A CB  1 
ATOM   471  O  OG  . SER   A 1 60  ? 15.952 2.958   27.235 1.00 25.66 ? 66  SER   A OG  1 
ATOM   472  N  N   . SER   A 1 61  ? 13.740 1.452   28.416 1.00 22.68 ? 67  SER   A N   1 
ATOM   473  C  CA  . SER   A 1 61  ? 13.019 1.745   29.679 1.00 22.20 ? 67  SER   A CA  1 
ATOM   474  C  C   . SER   A 1 61  ? 12.241 0.523   30.201 1.00 24.56 ? 67  SER   A C   1 
ATOM   475  O  O   . SER   A 1 61  ? 11.553 0.679   31.252 1.00 27.24 ? 67  SER   A O   1 
ATOM   476  C  CB  . SER   A 1 61  ? 12.086 2.925   29.487 1.00 22.29 ? 67  SER   A CB  1 
ATOM   477  O  OG  . SER   A 1 61  ? 10.834 2.542   28.920 1.00 19.32 ? 67  SER   A OG  1 
ATOM   478  N  N   . ARG   A 1 62  ? 12.239 -0.598  29.468 1.00 23.89 ? 68  ARG   A N   1 
ATOM   479  C  CA  . ARG   A 1 62  ? 11.711 -1.913  29.920 1.00 21.58 ? 68  ARG   A CA  1 
ATOM   480  C  C   . ARG   A 1 62  ? 12.770 -2.992  29.680 1.00 22.35 ? 68  ARG   A C   1 
ATOM   481  O  O   . ARG   A 1 62  ? 12.532 -4.151  30.041 1.00 22.01 ? 68  ARG   A O   1 
ATOM   482  C  CB  . ARG   A 1 62  ? 10.463 -2.291  29.123 1.00 21.85 ? 68  ARG   A CB  1 
ATOM   483  C  CG  . ARG   A 1 62  ? 9.188  -1.552  29.502 1.00 22.63 ? 68  ARG   A CG  1 
ATOM   484  C  CD  . ARG   A 1 62  ? 8.630  -1.889  30.874 1.00 21.47 ? 68  ARG   A CD  1 
ATOM   485  N  NE  . ARG   A 1 62  ? 7.487  -1.020  31.105 1.00 20.74 ? 68  ARG   A NE  1 
ATOM   486  C  CZ  . ARG   A 1 62  ? 7.553  0.221   31.568 1.00 21.45 ? 68  ARG   A CZ  1 
ATOM   487  N  NH1 . ARG   A 1 62  ? 8.710  0.771   31.916 1.00 21.58 ? 68  ARG   A NH1 1 
ATOM   488  N  NH2 . ARG   A 1 62  ? 6.440  0.921   31.666 1.00 21.62 ? 68  ARG   A NH2 1 
ATOM   489  N  N   . ARG   A 1 63  ? 13.901 -2.620  29.090 1.00 25.37 ? 69  ARG   A N   1 
ATOM   490  C  CA  . ARG   A 1 63  ? 14.956 -3.542  28.597 1.00 29.03 ? 69  ARG   A CA  1 
ATOM   491  C  C   . ARG   A 1 63  ? 14.334 -4.699  27.806 1.00 26.97 ? 69  ARG   A C   1 
ATOM   492  O  O   . ARG   A 1 63  ? 14.700 -5.836  28.087 1.00 24.82 ? 69  ARG   A O   1 
ATOM   493  C  CB  . ARG   A 1 63  ? 15.790 -4.033  29.781 1.00 35.10 ? 69  ARG   A CB  1 
ATOM   494  C  CG  . ARG   A 1 63  ? 16.548 -2.934  30.509 1.00 41.27 ? 69  ARG   A CG  1 
ATOM   495  C  CD  . ARG   A 1 63  ? 17.589 -3.536  31.426 1.00 50.28 ? 69  ARG   A CD  1 
ATOM   496  N  NE  . ARG   A 1 63  ? 17.951 -2.665  32.543 1.00 62.21 ? 69  ARG   A NE  1 
ATOM   497  C  CZ  . ARG   A 1 63  ? 17.723 -2.913  33.845 1.00 66.19 ? 69  ARG   A CZ  1 
ATOM   498  N  NH1 . ARG   A 1 63  ? 17.102 -4.018  34.240 1.00 62.46 ? 69  ARG   A NH1 1 
ATOM   499  N  NH2 . ARG   A 1 63  ? 18.130 -2.035  34.753 1.00 65.33 ? 69  ARG   A NH2 1 
ATOM   500  N  N   . LYS   A 1 64  ? 13.458 -4.400  26.832 1.00 27.75 ? 70  LYS   A N   1 
ATOM   501  C  CA  . LYS   A 1 64  ? 12.661 -5.397  26.053 1.00 26.80 ? 70  LYS   A CA  1 
ATOM   502  C  C   . LYS   A 1 64  ? 12.524 -5.002  24.577 1.00 24.20 ? 70  LYS   A C   1 
ATOM   503  O  O   . LYS   A 1 64  ? 12.341 -3.806  24.297 1.00 22.73 ? 70  LYS   A O   1 
ATOM   504  C  CB  . LYS   A 1 64  ? 11.248 -5.542  26.625 1.00 28.14 ? 70  LYS   A CB  1 
ATOM   505  C  CG  . LYS   A 1 64  ? 11.065 -6.711  27.575 1.00 29.16 ? 70  LYS   A CG  1 
ATOM   506  C  CD  . LYS   A 1 64  ? 9.790  -6.612  28.360 1.00 29.73 ? 70  LYS   A CD  1 
ATOM   507  C  CE  . LYS   A 1 64  ? 9.622  -7.733  29.360 1.00 31.89 ? 70  LYS   A CE  1 
ATOM   508  N  NZ  . LYS   A 1 64  ? 10.205 -7.388  30.682 1.00 35.41 ? 70  LYS   A NZ  1 
ATOM   509  N  N   . HIS   A 1 65  ? 12.538 -6.008  23.689 1.00 20.69 ? 71  HIS   A N   1 
ATOM   510  C  CA  . HIS   A 1 65  ? 12.117 -5.912  22.267 1.00 18.26 ? 71  HIS   A CA  1 
ATOM   511  C  C   . HIS   A 1 65  ? 10.624 -6.203  22.173 1.00 18.32 ? 71  HIS   A C   1 
ATOM   512  O  O   . HIS   A 1 65  ? 10.166 -7.209  22.757 1.00 20.37 ? 71  HIS   A O   1 
ATOM   513  C  CB  . HIS   A 1 65  ? 12.926 -6.860  21.393 1.00 17.35 ? 71  HIS   A CB  1 
ATOM   514  C  CG  . HIS   A 1 65  ? 14.399 -6.719  21.579 1.00 16.25 ? 71  HIS   A CG  1 
ATOM   515  N  ND1 . HIS   A 1 65  ? 15.183 -6.038  20.702 1.00 15.95 ? 71  HIS   A ND1 1 
ATOM   516  C  CD2 . HIS   A 1 65  ? 15.228 -7.181  22.530 1.00 17.02 ? 71  HIS   A CD2 1 
ATOM   517  C  CE1 . HIS   A 1 65  ? 16.430 -6.085  21.085 1.00 16.47 ? 71  HIS   A CE1 1 
ATOM   518  N  NE2 . HIS   A 1 65  ? 16.489 -6.770  22.209 1.00 16.90 ? 71  HIS   A NE2 1 
ATOM   519  N  N   . TYR   A 1 66  ? 9.885  -5.325  21.504 1.00 17.34 ? 72  TYR   A N   1 
ATOM   520  C  CA  . TYR   A 1 66  ? 8.410  -5.364  21.412 1.00 17.21 ? 72  TYR   A CA  1 
ATOM   521  C  C   . TYR   A 1 66  ? 8.070  -5.404  19.938 1.00 16.77 ? 72  TYR   A C   1 
ATOM   522  O  O   . TYR   A 1 66  ? 8.605  -4.617  19.165 1.00 17.28 ? 72  TYR   A O   1 
ATOM   523  C  CB  . TYR   A 1 66  ? 7.757  -4.143  22.071 1.00 17.68 ? 72  TYR   A CB  1 
ATOM   524  C  CG  . TYR   A 1 66  ? 7.752  -4.119  23.576 1.00 17.23 ? 72  TYR   A CG  1 
ATOM   525  C  CD1 . TYR   A 1 66  ? 7.010  -5.026  24.316 1.00 17.58 ? 72  TYR   A CD1 1 
ATOM   526  C  CD2 . TYR   A 1 66  ? 8.456  -3.145  24.268 1.00 18.82 ? 72  TYR   A CD2 1 
ATOM   527  C  CE1 . TYR   A 1 66  ? 6.987  -4.977  25.703 1.00 16.67 ? 72  TYR   A CE1 1 
ATOM   528  C  CE2 . TYR   A 1 66  ? 8.435  -3.065  25.653 1.00 18.27 ? 72  TYR   A CE2 1 
ATOM   529  C  CZ  . TYR   A 1 66  ? 7.695  -3.990  26.371 1.00 17.97 ? 72  TYR   A CZ  1 
ATOM   530  O  OH  . TYR   A 1 66  ? 7.697  -3.926  27.733 1.00 17.90 ? 72  TYR   A OH  1 
ATOM   531  N  N   . PRO   A 1 67  ? 7.244  -6.374  19.495 1.00 16.87 ? 73  PRO   A N   1 
ATOM   532  C  CA  . PRO   A 1 67  ? 6.755  -6.374  18.115 1.00 15.66 ? 73  PRO   A CA  1 
ATOM   533  C  C   . PRO   A 1 67  ? 5.639  -5.322  17.973 1.00 15.75 ? 73  PRO   A C   1 
ATOM   534  O  O   . PRO   A 1 67  ? 4.880  -5.192  18.913 1.00 15.55 ? 73  PRO   A O   1 
ATOM   535  C  CB  . PRO   A 1 67  ? 6.307  -7.822  17.942 1.00 15.66 ? 73  PRO   A CB  1 
ATOM   536  C  CG  . PRO   A 1 67  ? 5.886  -8.264  19.335 1.00 16.70 ? 73  PRO   A CG  1 
ATOM   537  C  CD  . PRO   A 1 67  ? 6.778  -7.521  20.297 1.00 15.98 ? 73  PRO   A CD  1 
ATOM   538  N  N   . VAL   A 1 68  ? 5.630  -4.554  16.872 1.00 15.08 ? 74  VAL   A N   1 
ATOM   539  C  CA  . VAL   A 1 68  ? 4.675  -3.441  16.576 1.00 14.64 ? 74  VAL   A CA  1 
ATOM   540  C  C   . VAL   A 1 68  ? 4.194  -3.534  15.111 1.00 14.12 ? 74  VAL   A C   1 
ATOM   541  O  O   . VAL   A 1 68  ? 4.967  -3.939  14.228 1.00 13.18 ? 74  VAL   A O   1 
ATOM   542  C  CB  . VAL   A 1 68  ? 5.292  -2.045  16.840 1.00 14.77 ? 74  VAL   A CB  1 
ATOM   543  C  CG1 . VAL   A 1 68  ? 5.454  -1.752  18.312 1.00 15.94 ? 74  VAL   A CG1 1 
ATOM   544  C  CG2 . VAL   A 1 68  ? 6.623  -1.847  16.153 1.00 15.23 ? 74  VAL   A CG2 1 
ATOM   545  N  N   . SER   A 1 69  ? 2.926  -3.214  14.877 1.00 13.74 ? 75  SER   A N   1 
ATOM   546  C  CA  . SER   A 1 69  ? 2.404  -2.660  13.609 1.00 13.49 ? 75  SER   A CA  1 
ATOM   547  C  C   . SER   A 1 69  ? 2.688  -1.175  13.691 1.00 13.35 ? 75  SER   A C   1 
ATOM   548  O  O   . SER   A 1 69  ? 2.609  -0.640  14.806 1.00 13.31 ? 75  SER   A O   1 
ATOM   549  C  CB  . SER   A 1 69  ? 0.931  -2.883  13.449 1.00 13.84 ? 75  SER   A CB  1 
ATOM   550  O  OG  . SER   A 1 69  ? 0.619  -4.245  13.538 1.00 14.90 ? 75  SER   A OG  1 
ATOM   551  N  N   . PHE   A 1 70  ? 3.044  -0.555  12.583 1.00 14.08 ? 76  PHE   A N   1 
ATOM   552  C  CA  . PHE   A 1 70  ? 3.359  0.890   12.560 1.00 15.94 ? 76  PHE   A CA  1 
ATOM   553  C  C   . PHE   A 1 70  ? 2.891  1.448   11.224 1.00 16.99 ? 76  PHE   A C   1 
ATOM   554  O  O   . PHE   A 1 70  ? 2.756  0.693   10.230 1.00 15.97 ? 76  PHE   A O   1 
ATOM   555  C  CB  . PHE   A 1 70  ? 4.832  1.149   12.876 1.00 15.26 ? 76  PHE   A CB  1 
ATOM   556  C  CG  . PHE   A 1 70  ? 5.801  0.496   11.938 1.00 15.56 ? 76  PHE   A CG  1 
ATOM   557  C  CD1 . PHE   A 1 70  ? 6.321  -0.744  12.225 1.00 15.67 ? 76  PHE   A CD1 1 
ATOM   558  C  CD2 . PHE   A 1 70  ? 6.206  1.127   10.783 1.00 15.82 ? 76  PHE   A CD2 1 
ATOM   559  C  CE1 . PHE   A 1 70  ? 7.242  -1.331  11.375 1.00 16.61 ? 76  PHE   A CE1 1 
ATOM   560  C  CE2 . PHE   A 1 70  ? 7.118  0.534   9.930  1.00 16.39 ? 76  PHE   A CE2 1 
ATOM   561  C  CZ  . PHE   A 1 70  ? 7.652  -0.685  10.232 1.00 16.55 ? 76  PHE   A CZ  1 
ATOM   562  N  N   . SER   A 1 71  ? 2.640  2.758   11.212 0.72 17.53 ? 77  SER   A N   1 
ATOM   563  C  CA  . SER   A 1 71  ? 2.042  3.492   10.070 0.72 18.39 ? 77  SER   A CA  1 
ATOM   564  C  C   . SER   A 1 71  ? 3.103  3.746   8.991  0.72 18.88 ? 77  SER   A C   1 
ATOM   565  O  O   . SER   A 1 71  ? 4.274  3.347   9.175  0.72 18.71 ? 77  SER   A O   1 
ATOM   566  C  CB  . SER   A 1 71  ? 1.382  4.764   10.540 0.72 18.59 ? 77  SER   A CB  1 
ATOM   567  O  OG  . SER   A 1 71  ? 2.303  5.596   11.222 0.72 19.28 ? 77  SER   A OG  1 
ATOM   568  N  N   . LYS   A 1 72  ? 2.685  4.348   7.879  0.72 19.76 ? 78  LYS   A N   1 
ATOM   569  C  CA  . LYS   A 1 72  ? 3.571  4.720   6.750  0.72 20.87 ? 78  LYS   A CA  1 
ATOM   570  C  C   . LYS   A 1 72  ? 4.260  6.029   7.126  0.72 20.37 ? 78  LYS   A C   1 
ATOM   571  O  O   . LYS   A 1 72  ? 3.691  6.811   7.878  0.72 21.79 ? 78  LYS   A O   1 
ATOM   572  C  CB  . LYS   A 1 72  ? 2.753  4.835   5.460  0.72 21.85 ? 78  LYS   A CB  1 
ATOM   573  C  CG  . LYS   A 1 72  ? 1.643  3.804   5.287  0.72 23.07 ? 78  LYS   A CG  1 
ATOM   574  C  CD  . LYS   A 1 72  ? 1.544  3.255   3.870  0.72 24.29 ? 78  LYS   A CD  1 
ATOM   575  C  CE  . LYS   A 1 72  ? 2.710  2.352   3.506  0.72 25.03 ? 78  LYS   A CE  1 
ATOM   576  N  NZ  . LYS   A 1 72  ? 2.495  1.658   2.211  0.72 25.82 ? 78  LYS   A NZ  1 
ATOM   577  N  N   . PRO   A 1 73  ? 5.499  6.303   6.656  1.00 19.80 ? 79  PRO   A N   1 
ATOM   578  C  CA  . PRO   A 1 73  ? 6.144  7.587   6.935  1.00 20.72 ? 79  PRO   A CA  1 
ATOM   579  C  C   . PRO   A 1 73  ? 5.217  8.753   6.566  1.00 21.73 ? 79  PRO   A C   1 
ATOM   580  O  O   . PRO   A 1 73  ? 4.661  8.737   5.498  1.00 21.82 ? 79  PRO   A O   1 
ATOM   581  C  CB  . PRO   A 1 73  ? 7.337  7.566   5.996  1.00 20.31 ? 79  PRO   A CB  1 
ATOM   582  C  CG  . PRO   A 1 73  ? 7.661  6.102   5.822  1.00 19.93 ? 79  PRO   A CG  1 
ATOM   583  C  CD  . PRO   A 1 73  ? 6.333  5.395   5.849  1.00 19.85 ? 79  PRO   A CD  1 
ATOM   584  N  N   . SER   A 1 74  ? 5.060  9.721   7.475  0.72 22.01 ? 80  SER   A N   1 
ATOM   585  C  CA  . SER   A 1 74  ? 4.127  10.866  7.319  0.72 22.27 ? 80  SER   A CA  1 
ATOM   586  C  C   . SER   A 1 74  ? 4.551  12.067  8.175  0.72 22.53 ? 80  SER   A C   1 
ATOM   587  O  O   . SER   A 1 74  ? 5.505  11.940  8.964  0.72 22.71 ? 80  SER   A O   1 
ATOM   588  C  CB  . SER   A 1 74  ? 2.726  10.434  7.669  0.72 22.89 ? 80  SER   A CB  1 
ATOM   589  O  OG  . SER   A 1 74  ? 2.594  10.252  9.072  0.72 23.10 ? 80  SER   A OG  1 
ATOM   590  N  N   . LEU   A 1 75  ? 3.844  13.190  7.996  1.00 23.05 ? 81  LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 75  ? 3.925  14.392  8.856  1.00 23.19 ? 81  LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 75  ? 2.935  14.201  10.002 1.00 22.19 ? 81  LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 75  ? 1.744  13.997  9.713  1.00 22.99 ? 81  LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 75  ? 3.484  15.644  8.086  1.00 23.95 ? 81  LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 75  ? 4.482  16.336  7.173  1.00 24.35 ? 81  LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 75  ? 3.796  17.498  6.473  1.00 25.89 ? 81  LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 75  ? 5.666  16.844  7.946  1.00 24.24 ? 81  LEU   A CD2 1 
ATOM   598  N  N   . ILE   A 1 76  ? 3.394  14.356  11.231 1.00 20.91 ? 82  ILE   A N   1 
ATOM   599  C  CA  . ILE   A 1 76  ? 2.560  14.245  12.453 1.00 22.83 ? 82  ILE   A CA  1 
ATOM   600  C  C   . ILE   A 1 76  ? 3.006  15.379  13.385 1.00 24.33 ? 82  ILE   A C   1 
ATOM   601  O  O   . ILE   A 1 76  ? 4.228  15.674  13.454 1.00 22.67 ? 82  ILE   A O   1 
ATOM   602  C  CB  . ILE   A 1 76  ? 2.728  12.828  13.055 1.00 22.67 ? 82  ILE   A CB  1 
ATOM   603  C  CG1 . ILE   A 1 76  ? 2.169  11.743  12.128 1.00 22.79 ? 82  ILE   A CG1 1 
ATOM   604  C  CG2 . ILE   A 1 76  ? 2.115  12.747  14.435 1.00 21.23 ? 82  ILE   A CG2 1 
ATOM   605  C  CD1 . ILE   A 1 76  ? 2.731  10.368  12.368 1.00 24.07 ? 82  ILE   A CD1 1 
ATOM   606  N  N   . PHE   A 1 77  ? 2.046  16.054  14.021 0.72 23.34 ? 83  PHE   A N   1 
ATOM   607  C  CA  . PHE   A 1 77  ? 2.310  17.140  15.000 0.72 23.88 ? 83  PHE   A CA  1 
ATOM   608  C  C   . PHE   A 1 77  ? 3.076  16.559  16.196 0.72 22.18 ? 83  PHE   A C   1 
ATOM   609  O  O   . PHE   A 1 77  ? 2.843  15.395  16.587 0.72 22.09 ? 83  PHE   A O   1 
ATOM   610  C  CB  . PHE   A 1 77  ? 1.008  17.830  15.424 0.72 25.48 ? 83  PHE   A CB  1 
ATOM   611  C  CG  . PHE   A 1 77  ? 1.172  18.945  16.427 0.72 25.19 ? 83  PHE   A CG  1 
ATOM   612  C  CD1 . PHE   A 1 77  ? 1.435  20.240  16.010 0.72 25.57 ? 83  PHE   A CD1 1 
ATOM   613  C  CD2 . PHE   A 1 77  ? 1.059  18.698  17.789 0.72 26.47 ? 83  PHE   A CD2 1 
ATOM   614  C  CE1 . PHE   A 1 77  ? 1.590  21.265  16.933 0.72 26.45 ? 83  PHE   A CE1 1 
ATOM   615  C  CE2 . PHE   A 1 77  ? 1.208  19.724  18.713 0.72 26.71 ? 83  PHE   A CE2 1 
ATOM   616  C  CZ  . PHE   A 1 77  ? 1.484  21.005  18.283 0.72 26.99 ? 83  PHE   A CZ  1 
ATOM   617  N  N   . VAL   A 1 78  ? 3.990  17.359  16.743 0.72 21.33 ? 84  VAL   A N   1 
ATOM   618  C  CA  . VAL   A 1 78  ? 4.830  17.016  17.927 0.72 20.94 ? 84  VAL   A CA  1 
ATOM   619  C  C   . VAL   A 1 78  ? 4.823  18.237  18.852 0.72 20.98 ? 84  VAL   A C   1 
ATOM   620  O  O   . VAL   A 1 78  ? 5.278  19.306  18.433 0.72 19.61 ? 84  VAL   A O   1 
ATOM   621  C  CB  . VAL   A 1 78  ? 6.252  16.574  17.507 0.72 19.76 ? 84  VAL   A CB  1 
ATOM   622  C  CG1 . VAL   A 1 78  ? 7.150  16.279  18.696 0.72 19.59 ? 84  VAL   A CG1 1 
ATOM   623  C  CG2 . VAL   A 1 78  ? 6.208  15.360  16.592 0.72 19.28 ? 84  VAL   A CG2 1 
ATOM   624  N  N   . GLU   A 1 79  ? 4.255  18.070  20.046 0.72 22.89 ? 85  GLU   A N   1 
ATOM   625  C  CA  . GLU   A 1 79  ? 4.219  19.071  21.145 0.72 22.80 ? 85  GLU   A CA  1 
ATOM   626  C  C   . GLU   A 1 79  ? 5.623  19.649  21.359 0.72 21.75 ? 85  GLU   A C   1 
ATOM   627  O  O   . GLU   A 1 79  ? 6.603  18.936  21.085 0.72 21.87 ? 85  GLU   A O   1 
ATOM   628  C  CB  . GLU   A 1 79  ? 3.703  18.398  22.419 0.72 24.05 ? 85  GLU   A CB  1 
ATOM   629  C  CG  . GLU   A 1 79  ? 2.196  18.477  22.594 0.72 24.93 ? 85  GLU   A CG  1 
ATOM   630  C  CD  . GLU   A 1 79  ? 1.725  19.553  23.559 0.72 26.23 ? 85  GLU   A CD  1 
ATOM   631  O  OE1 . GLU   A 1 79  ? 0.621  19.385  24.116 0.72 27.88 ? 85  GLU   A OE1 1 
ATOM   632  O  OE2 . GLU   A 1 79  ? 2.453  20.561  23.750 0.72 26.43 ? 85  GLU   A OE2 1 
ATOM   633  N  N   . ALA   A 1 80  ? 5.695  20.881  21.867 0.72 20.68 ? 86  ALA   A N   1 
ATOM   634  C  CA  . ALA   A 1 80  ? 6.933  21.664  22.079 0.72 20.37 ? 86  ALA   A CA  1 
ATOM   635  C  C   . ALA   A 1 80  ? 7.895  20.901  23.001 0.72 20.87 ? 86  ALA   A C   1 
ATOM   636  O  O   . ALA   A 1 80  ? 7.659  20.870  24.227 0.72 22.54 ? 86  ALA   A O   1 
ATOM   637  C  CB  . ALA   A 1 80  ? 6.592  23.023  22.632 0.72 19.30 ? 86  ALA   A CB  1 
ATOM   638  N  N   . SER   A 1 81  ? 8.927  20.292  22.411 0.72 20.11 ? 87  SER   A N   1 
ATOM   639  C  CA  . SER   A 1 81  ? 10.068 19.632  23.103 0.72 18.96 ? 87  SER   A CA  1 
ATOM   640  C  C   . SER   A 1 81  ? 10.908 20.706  23.801 0.72 18.52 ? 87  SER   A C   1 
ATOM   641  O  O   . SER   A 1 81  ? 10.590 21.893  23.638 0.72 16.85 ? 87  SER   A O   1 
ATOM   642  C  CB  . SER   A 1 81  ? 10.906 18.819  22.123 0.72 18.26 ? 87  SER   A CB  1 
ATOM   643  O  OG  . SER   A 1 81  ? 10.163 18.452  20.956 0.72 17.79 ? 87  SER   A OG  1 
ATOM   644  N  N   . GLU   A 1 82  ? 11.946 20.297  24.538 0.72 19.42 ? 88  GLU   A N   1 
ATOM   645  C  CA  . GLU   A 1 82  ? 13.034 21.203  25.005 0.72 19.88 ? 88  GLU   A CA  1 
ATOM   646  C  C   . GLU   A 1 82  ? 14.007 21.479  23.852 0.72 19.10 ? 88  GLU   A C   1 
ATOM   647  O  O   . GLU   A 1 82  ? 14.841 22.395  24.005 0.72 20.53 ? 88  GLU   A O   1 
ATOM   648  C  CB  . GLU   A 1 82  ? 13.797 20.682  26.236 0.72 21.47 ? 88  GLU   A CB  1 
ATOM   649  C  CG  . GLU   A 1 82  ? 13.779 19.178  26.479 0.72 22.33 ? 88  GLU   A CG  1 
ATOM   650  C  CD  . GLU   A 1 82  ? 12.656 18.712  27.396 0.72 24.23 ? 88  GLU   A CD  1 
ATOM   651  O  OE1 . GLU   A 1 82  ? 11.480 18.683  26.929 0.72 25.95 ? 88  GLU   A OE1 1 
ATOM   652  O  OE2 . GLU   A 1 82  ? 12.946 18.407  28.586 0.72 24.91 ? 88  GLU   A OE2 1 
ATOM   653  N  N   . TYR   A 1 83  ? 13.919 20.712  22.757 0.72 17.68 ? 89  TYR   A N   1 
ATOM   654  C  CA  . TYR   A 1 83  ? 14.884 20.701  21.622 0.72 15.91 ? 89  TYR   A CA  1 
ATOM   655  C  C   . TYR   A 1 83  ? 14.282 21.416  20.410 0.72 14.55 ? 89  TYR   A C   1 
ATOM   656  O  O   . TYR   A 1 83  ? 15.016 22.062  19.653 0.72 14.53 ? 89  TYR   A O   1 
ATOM   657  C  CB  . TYR   A 1 83  ? 15.283 19.261  21.285 0.72 15.80 ? 89  TYR   A CB  1 
ATOM   658  C  CG  . TYR   A 1 83  ? 15.719 18.454  22.481 0.72 16.06 ? 89  TYR   A CG  1 
ATOM   659  C  CD1 . TYR   A 1 83  ? 17.011 18.524  22.979 0.72 16.70 ? 89  TYR   A CD1 1 
ATOM   660  C  CD2 . TYR   A 1 83  ? 14.827 17.625  23.135 0.72 16.73 ? 89  TYR   A CD2 1 
ATOM   661  C  CE1 . TYR   A 1 83  ? 17.402 17.794  24.095 0.72 16.96 ? 89  TYR   A CE1 1 
ATOM   662  C  CE2 . TYR   A 1 83  ? 15.203 16.876  24.239 0.72 16.74 ? 89  TYR   A CE2 1 
ATOM   663  C  CZ  . TYR   A 1 83  ? 16.490 16.964  24.731 0.72 17.19 ? 89  TYR   A CZ  1 
ATOM   664  O  OH  . TYR   A 1 83  ? 16.843 16.202  25.818 0.72 17.72 ? 89  TYR   A OH  1 
ATOM   665  N  N   . TYR   A 1 84  ? 12.973 21.294  20.235 0.72 13.66 ? 90  TYR   A N   1 
ATOM   666  C  CA  . TYR   A 1 84  ? 12.207 21.898  19.122 0.72 13.27 ? 90  TYR   A CA  1 
ATOM   667  C  C   . TYR   A 1 84  ? 10.951 22.555  19.681 0.72 13.76 ? 90  TYR   A C   1 
ATOM   668  O  O   . TYR   A 1 84  ? 10.485 22.190  20.761 0.72 13.50 ? 90  TYR   A O   1 
ATOM   669  C  CB  . TYR   A 1 84  ? 11.796 20.827  18.113 0.72 12.62 ? 90  TYR   A CB  1 
ATOM   670  C  CG  . TYR   A 1 84  ? 12.875 19.887  17.645 0.72 11.86 ? 90  TYR   A CG  1 
ATOM   671  C  CD1 . TYR   A 1 84  ? 13.743 20.252  16.629 0.72 11.57 ? 90  TYR   A CD1 1 
ATOM   672  C  CD2 . TYR   A 1 84  ? 12.994 18.613  18.174 0.72 11.42 ? 90  TYR   A CD2 1 
ATOM   673  C  CE1 . TYR   A 1 84  ? 14.719 19.385  16.169 0.72 11.31 ? 90  TYR   A CE1 1 
ATOM   674  C  CE2 . TYR   A 1 84  ? 13.962 17.733  17.721 0.72 11.42 ? 90  TYR   A CE2 1 
ATOM   675  C  CZ  . TYR   A 1 84  ? 14.825 18.117  16.708 0.72 11.33 ? 90  TYR   A CZ  1 
ATOM   676  O  OH  . TYR   A 1 84  ? 15.787 17.266  16.242 0.72 10.94 ? 90  TYR   A OH  1 
ATOM   677  N  N   . PRO   A 1 85  ? 10.373 23.543  18.966 0.72 13.94 ? 91  PRO   A N   1 
ATOM   678  C  CA  . PRO   A 1 85  ? 9.031  24.031  19.279 0.72 13.87 ? 91  PRO   A CA  1 
ATOM   679  C  C   . PRO   A 1 85  ? 7.962  23.152  18.610 0.72 14.08 ? 91  PRO   A C   1 
ATOM   680  O  O   . PRO   A 1 85  ? 8.299  22.159  17.991 0.72 13.59 ? 91  PRO   A O   1 
ATOM   681  C  CB  . PRO   A 1 85  ? 9.062  25.461  18.711 0.72 13.83 ? 91  PRO   A CB  1 
ATOM   682  C  CG  . PRO   A 1 85  ? 9.987  25.362  17.506 0.72 13.87 ? 91  PRO   A CG  1 
ATOM   683  C  CD  . PRO   A 1 85  ? 11.000 24.285  17.860 0.72 14.00 ? 91  PRO   A CD  1 
ATOM   684  N  N   . ALA   A 1 86  ? 6.697  23.548  18.755 0.72 14.28 ? 92  ALA   A N   1 
ATOM   685  C  CA  . ALA   A 1 86  ? 5.508  22.861  18.202 0.72 14.04 ? 92  ALA   A CA  1 
ATOM   686  C  C   . ALA   A 1 86  ? 5.582  22.883  16.675 0.72 13.56 ? 92  ALA   A C   1 
ATOM   687  O  O   . ALA   A 1 86  ? 5.544  23.984  16.096 0.72 13.45 ? 92  ALA   A O   1 
ATOM   688  C  CB  . ALA   A 1 86  ? 4.256  23.542  18.694 0.72 14.23 ? 92  ALA   A CB  1 
ATOM   689  N  N   . ARG   A 1 87  ? 5.652  21.707  16.053 0.72 13.13 ? 93  ARG   A N   1 
ATOM   690  C  CA  . ARG   A 1 87  ? 5.920  21.558  14.601 0.72 12.80 ? 93  ARG   A CA  1 
ATOM   691  C  C   . ARG   A 1 87  ? 5.415  20.205  14.111 0.72 13.00 ? 93  ARG   A C   1 
ATOM   692  O  O   . ARG   A 1 87  ? 5.176  19.319  14.950 0.72 12.81 ? 93  ARG   A O   1 
ATOM   693  C  CB  . ARG   A 1 87  ? 7.425  21.668  14.336 0.72 12.54 ? 93  ARG   A CB  1 
ATOM   694  C  CG  . ARG   A 1 87  ? 8.216  20.431  14.733 0.72 12.18 ? 93  ARG   A CG  1 
ATOM   695  C  CD  . ARG   A 1 87  ? 9.704  20.672  14.839 0.72 12.10 ? 93  ARG   A CD  1 
ATOM   696  N  NE  . ARG   A 1 87  ? 10.474 19.517  14.394 0.72 12.14 ? 93  ARG   A NE  1 
ATOM   697  C  CZ  . ARG   A 1 87  ? 10.619 18.377  15.069 0.72 12.06 ? 93  ARG   A CZ  1 
ATOM   698  N  NH1 . ARG   A 1 87  ? 11.355 17.396  14.568 0.72 12.30 ? 93  ARG   A NH1 1 
ATOM   699  N  NH2 . ARG   A 1 87  ? 10.036 18.213  16.242 0.72 12.28 ? 93  ARG   A NH2 1 
ATOM   700  N  N   . TYR   A 1 88  ? 5.302  20.067  12.788 0.72 13.95 ? 94  TYR   A N   1 
ATOM   701  C  CA  . TYR   A 1 88  ? 5.075  18.788  12.066 0.72 14.03 ? 94  TYR   A CA  1 
ATOM   702  C  C   . TYR   A 1 88  ? 6.421  18.101  11.819 0.72 14.27 ? 94  TYR   A C   1 
ATOM   703  O  O   . TYR   A 1 88  ? 7.189  18.596  10.989 0.72 13.73 ? 94  TYR   A O   1 
ATOM   704  C  CB  . TYR   A 1 88  ? 4.440  19.022  10.695 0.72 14.16 ? 94  TYR   A CB  1 
ATOM   705  C  CG  . TYR   A 1 88  ? 2.990  19.433  10.659 0.72 14.26 ? 94  TYR   A CG  1 
ATOM   706  C  CD1 . TYR   A 1 88  ? 1.997  18.499  10.426 0.72 14.70 ? 94  TYR   A CD1 1 
ATOM   707  C  CD2 . TYR   A 1 88  ? 2.604  20.761  10.764 0.72 14.59 ? 94  TYR   A CD2 1 
ATOM   708  C  CE1 . TYR   A 1 88  ? 0.661  18.860  10.335 0.72 14.65 ? 94  TYR   A CE1 1 
ATOM   709  C  CE2 . TYR   A 1 88  ? 1.271  21.143  10.672 0.72 14.28 ? 94  TYR   A CE2 1 
ATOM   710  C  CZ  . TYR   A 1 88  ? 0.290  20.188  10.456 0.72 14.57 ? 94  TYR   A CZ  1 
ATOM   711  O  OH  . TYR   A 1 88  ? -1.036 20.526  10.369 0.72 13.39 ? 94  TYR   A OH  1 
ATOM   712  N  N   . GLN   A 1 89  ? 6.687  16.980  12.497 0.72 14.96 ? 95  GLN   A N   1 
ATOM   713  C  CA  . GLN   A 1 89  ? 7.846  16.107  12.188 0.72 14.83 ? 95  GLN   A CA  1 
ATOM   714  C  C   . GLN   A 1 89  ? 7.481  15.274  10.959 0.72 15.62 ? 95  GLN   A C   1 
ATOM   715  O  O   . GLN   A 1 89  ? 6.408  14.627  10.979 0.72 17.02 ? 95  GLN   A O   1 
ATOM   716  C  CB  . GLN   A 1 89  ? 8.229  15.228  13.384 0.72 14.60 ? 95  GLN   A CB  1 
ATOM   717  C  CG  . GLN   A 1 89  ? 9.349  14.238  13.063 0.72 13.89 ? 95  GLN   A CG  1 
ATOM   718  C  CD  . GLN   A 1 89  ? 10.246 13.909  14.230 0.72 13.45 ? 95  GLN   A CD  1 
ATOM   719  O  OE1 . GLN   A 1 89  ? 10.573 14.764  15.050 0.72 13.22 ? 95  GLN   A OE1 1 
ATOM   720  N  NE2 . GLN   A 1 89  ? 10.679 12.658  14.293 0.72 13.17 ? 95  GLN   A NE2 1 
ATOM   721  N  N   . SER   A 1 90  ? 8.343  15.280  9.944  1.00 16.07 ? 96  SER   A N   1 
ATOM   722  C  CA  . SER   A 1 90  ? 8.139  14.524  8.681  1.00 16.04 ? 96  SER   A CA  1 
ATOM   723  C  C   . SER   A 1 90  ? 8.896  13.193  8.725  1.00 16.02 ? 96  SER   A C   1 
ATOM   724  O  O   . SER   A 1 90  ? 9.828  13.050  9.569  1.00 15.27 ? 96  SER   A O   1 
ATOM   725  C  CB  . SER   A 1 90  ? 8.575  15.367  7.491  1.00 15.87 ? 96  SER   A CB  1 
ATOM   726  O  OG  . SER   A 1 90  ? 9.982  15.450  7.390  1.00 15.56 ? 96  SER   A OG  1 
ATOM   727  N  N   . HIS   A 1 91  ? 8.453  12.232  7.904  1.00 15.83 ? 97  HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 91  ? 8.963  10.836  7.823  1.00 15.47 ? 97  HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 91  ? 8.756  10.084  9.154  1.00 15.78 ? 97  HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 91  ? 9.554  9.170   9.470  1.00 14.34 ? 97  HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 91  ? 10.409 10.853  7.333  1.00 16.12 ? 97  HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 91  ? 10.563 11.508  6.002  1.00 16.24 ? 97  HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 91  ? 10.440 10.796  4.814  1.00 16.84 ? 97  HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 91  ? 10.822 12.787  5.658  1.00 15.25 ? 97  HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 91  ? 10.627 11.618  3.800  1.00 15.87 ? 97  HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 91  ? 10.844 12.834  4.289  1.00 15.26 ? 97  HIS   A NE2 1 
ATOM   737  N  N   . LEU   A 1 92  ? 7.670  10.386  9.873  1.00 15.42 ? 98  LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 92  ? 7.353  9.722   11.161 1.00 15.09 ? 98  LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 92  ? 6.402  8.533   10.952 1.00 14.60 ? 98  LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 92  ? 5.517  8.603   10.039 1.00 14.40 ? 98  LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 92  ? 6.774  10.773  12.110 1.00 15.51 ? 98  LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 92  ? 6.798  10.427  13.597 1.00 15.80 ? 98  LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 92  ? 8.174  9.937   14.047 1.00 15.02 ? 98  LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 92  ? 6.348  11.625  14.431 1.00 15.84 ? 98  LEU   A CD2 1 
ATOM   745  N  N   . MET   A 1 93  ? 6.601  7.474   11.766 1.00 14.41 ? 99  MET   A N   1 
ATOM   746  C  CA  . MET   A 1 93  ? 5.809  6.211   11.788 1.00 13.88 ? 99  MET   A CA  1 
ATOM   747  C  C   . MET   A 1 93  ? 5.353  5.923   13.214 1.00 13.70 ? 99  MET   A C   1 
ATOM   748  O  O   . MET   A 1 93  ? 6.225  5.715   14.030 1.00 13.28 ? 99  MET   A O   1 
ATOM   749  C  CB  . MET   A 1 93  ? 6.663  5.049   11.277 1.00 13.90 ? 99  MET   A CB  1 
ATOM   750  C  CG  . MET   A 1 93  ? 7.246  5.360   9.924  1.00 14.24 ? 99  MET   A CG  1 
ATOM   751  S  SD  . MET   A 1 93  ? 8.258  4.043   9.283  1.00 15.65 ? 99  MET   A SD  1 
ATOM   752  C  CE  . MET   A 1 93  ? 9.752  4.144   10.270 1.00 15.25 ? 99  MET   A CE  1 
ATOM   753  N  N   . LEU   A 1 94  ? 4.045  5.922   13.513 1.00 14.64 ? 100 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 94  ? 3.563  5.651   14.895 1.00 15.25 ? 100 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 94  ? 3.174  4.177   15.073 1.00 15.48 ? 100 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 94  ? 2.780  3.534   14.059 1.00 13.72 ? 100 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 94  ? 2.378  6.546   15.255 1.00 16.32 ? 100 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 94  ? 2.680  8.031   15.397 1.00 16.62 ? 100 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 94  ? 1.520  8.731   16.084 1.00 18.11 ? 100 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 94  ? 3.956  8.278   16.164 1.00 17.59 ? 100 LEU   A CD2 1 
ATOM   761  N  N   . ALA   A 1 95  ? 3.301  3.702   16.330 1.00 14.88 ? 101 ALA   A N   1 
ATOM   762  C  CA  . ALA   A 1 95  ? 2.811  2.403   16.825 1.00 15.66 ? 101 ALA   A CA  1 
ATOM   763  C  C   . ALA   A 1 95  ? 2.287  2.579   18.249 1.00 16.07 ? 101 ALA   A C   1 
ATOM   764  O  O   . ALA   A 1 95  ? 2.702  3.536   18.895 1.00 16.25 ? 101 ALA   A O   1 
ATOM   765  C  CB  . ALA   A 1 95  ? 3.899  1.357   16.773 1.00 15.53 ? 101 ALA   A CB  1 
ATOM   766  N  N   . VAL   A 1 96  ? 1.354  1.699   18.633 1.00 16.58 ? 102 VAL   A N   1 
ATOM   767  C  CA  . VAL   A 1 96  ? 0.854  1.410   20.014 1.00 17.12 ? 102 VAL   A CA  1 
ATOM   768  C  C   . VAL   A 1 96  ? 1.995  0.658   20.705 1.00 17.44 ? 102 VAL   A C   1 
ATOM   769  O  O   . VAL   A 1 96  ? 2.394  -0.442  20.204 1.00 14.50 ? 102 VAL   A O   1 
ATOM   770  C  CB  . VAL   A 1 96  ? -0.444 0.567   19.976 1.00 17.38 ? 102 VAL   A CB  1 
ATOM   771  C  CG1 . VAL   A 1 96  ? -1.084 0.367   21.332 1.00 17.27 ? 102 VAL   A CG1 1 
ATOM   772  C  CG2 . VAL   A 1 96  ? -1.468 1.151   19.011 1.00 17.66 ? 102 VAL   A CG2 1 
ATOM   773  N  N   . GLY   A 1 97  ? 2.547  1.253   21.764 1.00 17.48 ? 103 GLY   A N   1 
ATOM   774  C  CA  . GLY   A 1 97  ? 3.722  0.682   22.422 1.00 18.87 ? 103 GLY   A CA  1 
ATOM   775  C  C   . GLY   A 1 97  ? 4.298  1.624   23.445 1.00 19.12 ? 103 GLY   A C   1 
ATOM   776  O  O   . GLY   A 1 97  ? 4.125  2.830   23.289 1.00 22.81 ? 103 GLY   A O   1 
ATOM   777  N  N   . HIS   A 1 98  ? 4.991  1.067   24.437 1.00 18.20 ? 104 HIS   A N   1 
ATOM   778  C  CA  . HIS   A 1 98  ? 5.639  1.830   25.521 1.00 18.56 ? 104 HIS   A CA  1 
ATOM   779  C  C   . HIS   A 1 98  ? 6.867  2.544   24.957 1.00 18.19 ? 104 HIS   A C   1 
ATOM   780  O  O   . HIS   A 1 98  ? 7.622  1.949   24.196 1.00 18.31 ? 104 HIS   A O   1 
ATOM   781  C  CB  . HIS   A 1 98  ? 5.990  0.936   26.740 1.00 18.00 ? 104 HIS   A CB  1 
ATOM   782  C  CG  . HIS   A 1 98  ? 6.629  1.712   27.842 1.00 16.69 ? 104 HIS   A CG  1 
ATOM   783  N  ND1 . HIS   A 1 98  ? 5.965  2.712   28.507 1.00 16.75 ? 104 HIS   A ND1 1 
ATOM   784  C  CD2 . HIS   A 1 98  ? 7.888  1.701   28.331 1.00 17.35 ? 104 HIS   A CD2 1 
ATOM   785  C  CE1 . HIS   A 1 98  ? 6.776  3.265   29.382 1.00 16.92 ? 104 HIS   A CE1 1 
ATOM   786  N  NE2 . HIS   A 1 98  ? 7.974  2.679   29.281 1.00 16.51 ? 104 HIS   A NE2 1 
ATOM   787  N  N   . SER   A 1 99  ? 7.030  3.807   25.340 0.72 18.39 ? 105 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 99  ? 8.245  4.633   25.130 0.72 18.69 ? 105 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 99  ? 8.281  5.712   26.211 0.72 19.52 ? 105 SER   A C   1 
ATOM   790  O  O   . SER   A 1 99  ? 7.190  6.062   26.701 0.72 19.54 ? 105 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 99  ? 8.259  5.253   23.763 0.72 18.37 ? 105 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 99  ? 7.145  6.116   23.587 0.72 17.27 ? 105 SER   A OG  1 
ATOM   793  N  N   . GLU   A 1 100 ? 9.479  6.181   26.575 0.72 20.34 ? 106 GLU   A N   1 
ATOM   794  C  CA  . GLU   A 1 100 ? 9.689  7.443   27.334 0.72 21.55 ? 106 GLU   A CA  1 
ATOM   795  C  C   . GLU   A 1 100 ? 10.993 8.082   26.836 0.72 22.39 ? 106 GLU   A C   1 
ATOM   796  O  O   . GLU   A 1 100 ? 11.768 7.447   26.114 0.72 22.45 ? 106 GLU   A O   1 
ATOM   797  C  CB  . GLU   A 1 100 ? 9.535  7.173   28.843 0.72 22.40 ? 106 GLU   A CB  1 
ATOM   798  C  CG  . GLU   A 1 100 ? 10.411 6.059   29.423 0.72 22.76 ? 106 GLU   A CG  1 
ATOM   799  C  CD  . GLU   A 1 100 ? 9.960  5.536   30.790 0.72 21.99 ? 106 GLU   A CD  1 
ATOM   800  O  OE1 . GLU   A 1 100 ? 10.662 5.789   31.791 0.72 20.77 ? 106 GLU   A OE1 1 
ATOM   801  O  OE2 . GLU   A 1 100 ? 8.905  4.868   30.855 0.72 20.83 ? 106 GLU   A OE2 1 
ATOM   802  N  N   . PRO   A 1 101 ? 11.258 9.378   27.140 1.00 22.53 ? 107 PRO   A N   1 
ATOM   803  C  CA  . PRO   A 1 101 ? 12.308 10.150  26.442 1.00 21.78 ? 107 PRO   A CA  1 
ATOM   804  C  C   . PRO   A 1 101 ? 13.663 9.504   26.113 1.00 19.33 ? 107 PRO   A C   1 
ATOM   805  O  O   . PRO   A 1 101 ? 14.120 9.655   24.975 1.00 18.52 ? 107 PRO   A O   1 
ATOM   806  C  CB  . PRO   A 1 101 ? 12.527 11.308  27.426 1.00 22.57 ? 107 PRO   A CB  1 
ATOM   807  C  CG  . PRO   A 1 101 ? 11.138 11.559  27.962 1.00 22.77 ? 107 PRO   A CG  1 
ATOM   808  C  CD  . PRO   A 1 101 ? 10.586 10.163  28.198 1.00 23.24 ? 107 PRO   A CD  1 
ATOM   809  N  N   . GLY   A 1 102 ? 14.243 8.789   27.098 1.00 19.06 ? 108 GLY   A N   1 
ATOM   810  C  CA  . GLY   A 1 102 ? 15.503 7.994   27.012 1.00 15.78 ? 108 GLY   A CA  1 
ATOM   811  C  C   . GLY   A 1 102 ? 15.528 6.871   25.969 1.00 14.17 ? 108 GLY   A C   1 
ATOM   812  O  O   . GLY   A 1 102 ? 16.611 6.394   25.641 1.00 13.39 ? 108 GLY   A O   1 
ATOM   813  N  N   . ASP   A 1 103 ? 14.354 6.501   25.449 0.72 14.25 ? 109 ASP   A N   1 
ATOM   814  C  CA  . ASP   A 1 103 ? 14.124 5.369   24.512 0.72 14.00 ? 109 ASP   A CA  1 
ATOM   815  C  C   . ASP   A 1 103 ? 14.440 5.790   23.076 0.72 14.50 ? 109 ASP   A C   1 
ATOM   816  O  O   . ASP   A 1 103 ? 14.552 4.886   22.217 0.72 15.31 ? 109 ASP   A O   1 
ATOM   817  C  CB  . ASP   A 1 103 ? 12.692 4.850   24.651 0.72 13.86 ? 109 ASP   A CB  1 
ATOM   818  C  CG  . ASP   A 1 103 ? 12.540 3.939   25.850 0.72 13.35 ? 109 ASP   A CG  1 
ATOM   819  O  OD1 . ASP   A 1 103 ? 13.523 3.275   26.175 0.72 13.47 ? 109 ASP   A OD1 1 
ATOM   820  O  OD2 . ASP   A 1 103 ? 11.457 3.912   26.444 0.72 13.38 ? 109 ASP   A OD2 1 
ATOM   821  N  N   . CYS   A 1 104 ? 14.584 7.097   22.827 1.00 14.57 ? 110 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 104 ? 15.049 7.650   21.519 1.00 13.88 ? 110 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 104 ? 16.376 6.981   21.172 1.00 13.92 ? 110 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 104 ? 17.226 6.822   22.088 1.00 15.10 ? 110 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 104 ? 15.191 9.172   21.555 1.00 13.45 ? 110 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 104 ? 13.589 10.020  21.660 1.00 13.60 ? 110 CYS   A SG  1 
ATOM   827  N  N   . GLY   A 1 105 ? 16.520 6.522   19.931 1.00 12.93 ? 111 GLY   A N   1 
ATOM   828  C  CA  . GLY   A 1 105 ? 17.750 5.858   19.465 1.00 12.39 ? 111 GLY   A CA  1 
ATOM   829  C  C   . GLY   A 1 105 ? 17.543 4.362   19.331 1.00 11.73 ? 111 GLY   A C   1 
ATOM   830  O  O   . GLY   A 1 105 ? 18.248 3.732   18.513 1.00 12.40 ? 111 GLY   A O   1 
ATOM   831  N  N   . GLY   A 1 106 ? 16.590 3.820   20.078 1.00 10.98 ? 112 GLY   A N   1 
ATOM   832  C  CA  . GLY   A 1 106 ? 16.214 2.404   19.979 1.00 10.39 ? 112 GLY   A CA  1 
ATOM   833  C  C   . GLY   A 1 106 ? 15.906 2.056   18.549 1.00 10.04 ? 112 GLY   A C   1 
ATOM   834  O  O   . GLY   A 1 106 ? 15.166 2.795   17.926 1.00 9.60  ? 112 GLY   A O   1 
ATOM   835  N  N   . ILE   A 1 107 ? 16.383 0.904   18.093 1.00 10.43 ? 113 ILE   A N   1 
ATOM   836  C  CA  . ILE   A 1 107 ? 16.262 0.471   16.676 1.00 10.61 ? 113 ILE   A CA  1 
ATOM   837  C  C   . ILE   A 1 107 ? 14.891 -0.201  16.463 1.00 10.78 ? 113 ILE   A C   1 
ATOM   838  O  O   . ILE   A 1 107 ? 14.536 -1.087  17.276 1.00 10.58 ? 113 ILE   A O   1 
ATOM   839  C  CB  . ILE   A 1 107 ? 17.484 -0.416  16.327 1.00 10.61 ? 113 ILE   A CB  1 
ATOM   840  C  CG1 . ILE   A 1 107 ? 18.626 0.424   15.759 1.00 10.97 ? 113 ILE   A CG1 1 
ATOM   841  C  CG2 . ILE   A 1 107 ? 17.119 -1.530  15.375 1.00 10.74 ? 113 ILE   A CG2 1 
ATOM   842  C  CD1 . ILE   A 1 107 ? 19.949 -0.285  15.723 1.00 10.59 ? 113 ILE   A CD1 1 
ATOM   843  N  N   . LEU   A 1 108 ? 14.163 0.203   15.406 1.00 10.56 ? 114 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 108 ? 13.108 -0.598  14.735 1.00 11.21 ? 114 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 108 ? 13.713 -1.468  13.618 1.00 12.10 ? 114 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 108 ? 14.374 -0.951  12.726 1.00 11.60 ? 114 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 108 ? 12.032 0.352   14.190 1.00 11.22 ? 114 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 108 ? 10.800 -0.275  13.519 1.00 10.75 ? 114 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 108 ? 9.927  -1.043  14.491 1.00 10.26 ? 114 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 108 ? 9.965  0.804   12.862 1.00 10.71 ? 114 LEU   A CD2 1 
ATOM   851  N  N   . ARG   A 1 109 ? 13.467 -2.774  13.694 1.00 15.01 ? 115 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 109 ? 13.962 -3.836  12.790 1.00 16.08 ? 115 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 109 ? 12.760 -4.551  12.180 1.00 16.39 ? 115 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 109 ? 11.763 -4.732  12.871 1.00 14.47 ? 115 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 109 ? 14.779 -4.876  13.554 1.00 18.48 ? 115 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 109 ? 16.281 -4.666  13.512 1.00 20.83 ? 115 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 109 ? 17.082 -5.968  13.525 1.00 22.36 ? 115 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 109 ? 18.398 -5.686  12.935 1.00 25.86 ? 115 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 109 ? 19.424 -5.157  13.604 1.00 30.04 ? 115 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 109 ? 19.335 -4.927  14.913 1.00 30.70 ? 115 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 109 ? 20.555 -4.893  12.965 1.00 32.37 ? 115 ARG   A NH2 1 
ATOM   862  N  N   . CYS   A 1 110 ? 12.905 -4.967  10.928 1.00 18.89 ? 116 CYS   A N   1 
ATOM   863  C  CA  . CYS   A 1 110 ? 11.990 -5.871  10.189 1.00 20.69 ? 116 CYS   A CA  1 
ATOM   864  C  C   . CYS   A 1 110 ? 12.845 -6.954  9.532  1.00 22.94 ? 116 CYS   A C   1 
ATOM   865  O  O   . CYS   A 1 110 ? 14.084 -6.849  9.621  1.00 23.39 ? 116 CYS   A O   1 
ATOM   866  C  CB  . CYS   A 1 110 ? 11.206 -5.100  9.144  1.00 19.95 ? 116 CYS   A CB  1 
ATOM   867  S  SG  . CYS   A 1 110 ? 12.254 -4.695  7.728  1.00 18.66 ? 116 CYS   A SG  1 
ATOM   868  N  N   . GLN   A 1 111 ? 12.216 -7.971  8.944  1.00 27.20 ? 117 GLN   A N   1 
ATOM   869  C  CA  . GLN   A 1 111 ? 12.923 -9.158  8.361  1.00 31.53 ? 117 GLN   A CA  1 
ATOM   870  C  C   . GLN   A 1 111 ? 14.078 -8.708  7.450  1.00 29.74 ? 117 GLN   A C   1 
ATOM   871  O  O   . GLN   A 1 111 ? 15.095 -9.443  7.449  1.00 31.86 ? 117 GLN   A O   1 
ATOM   872  C  CB  . GLN   A 1 111 ? 11.956 -10.081 7.606  1.00 34.67 ? 117 GLN   A CB  1 
ATOM   873  C  CG  . GLN   A 1 111 ? 10.968 -9.325  6.729  1.00 36.69 ? 117 GLN   A CG  1 
ATOM   874  C  CD  . GLN   A 1 111 ? 9.979  -10.239 6.058  1.00 40.66 ? 117 GLN   A CD  1 
ATOM   875  O  OE1 . GLN   A 1 111 ? 8.791  -9.910  5.927  1.00 42.03 ? 117 GLN   A OE1 1 
ATOM   876  N  NE2 . GLN   A 1 111 ? 10.483 -11.382 5.613  1.00 38.99 ? 117 GLN   A NE2 1 
ATOM   877  N  N   . HIS   A 1 112 ? 13.949 -7.538  6.781  1.00 27.08 ? 118 HIS   A N   1 
ATOM   878  C  CA  . HIS   A 1 112 ? 14.929 -6.947  5.819  1.00 24.56 ? 118 HIS   A CA  1 
ATOM   879  C  C   . HIS   A 1 112 ? 15.920 -5.975  6.472  1.00 22.93 ? 118 HIS   A C   1 
ATOM   880  O  O   . HIS   A 1 112 ? 16.667 -5.331  5.695  1.00 24.18 ? 118 HIS   A O   1 
ATOM   881  C  CB  . HIS   A 1 112 ? 14.223 -6.148  4.723  1.00 24.21 ? 118 HIS   A CB  1 
ATOM   882  C  CG  . HIS   A 1 112 ? 12.981 -6.776  4.214  1.00 23.72 ? 118 HIS   A CG  1 
ATOM   883  N  ND1 . HIS   A 1 112 ? 11.740 -6.347  4.590  1.00 25.08 ? 118 HIS   A ND1 1 
ATOM   884  C  CD2 . HIS   A 1 112 ? 12.798 -7.792  3.347  1.00 24.57 ? 118 HIS   A CD2 1 
ATOM   885  C  CE1 . HIS   A 1 112 ? 10.828 -7.074  3.960  1.00 25.03 ? 118 HIS   A CE1 1 
ATOM   886  N  NE2 . HIS   A 1 112 ? 11.462 -7.960  3.181  1.00 23.75 ? 118 HIS   A NE2 1 
ATOM   887  N  N   . GLY   A 1 113 ? 15.863 -5.795  7.802  1.00 21.25 ? 119 GLY   A N   1 
ATOM   888  C  CA  . GLY   A 1 113 ? 16.855 -5.038  8.603  1.00 17.74 ? 119 GLY   A CA  1 
ATOM   889  C  C   . GLY   A 1 113 ? 16.305 -3.782  9.265  1.00 15.98 ? 119 GLY   A C   1 
ATOM   890  O  O   . GLY   A 1 113 ? 15.075 -3.713  9.565  1.00 15.98 ? 119 GLY   A O   1 
ATOM   891  N  N   . VAL   A 1 114 ? 17.183 -2.808  9.471  1.00 14.03 ? 120 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 114 ? 16.934 -1.551  10.234 1.00 13.82 ? 120 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 114 ? 15.986 -0.673  9.430  1.00 13.64 ? 120 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 114 ? 16.414 -0.207  8.341  1.00 12.45 ? 120 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 114 ? 18.226 -0.766  10.545 1.00 13.87 ? 120 VAL   A CB  1 
ATOM   896  C  CG1 . VAL   A 1 114 ? 17.896 0.616   11.102 1.00 14.00 ? 120 VAL   A CG1 1 
ATOM   897  C  CG2 . VAL   A 1 114 ? 19.169 -1.533  11.488 1.00 13.13 ? 120 VAL   A CG2 1 
ATOM   898  N  N   . VAL   A 1 115 ? 14.795 -0.435  10.004 1.00 12.72 ? 121 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 115 ? 13.722 0.458   9.478  1.00 12.78 ? 121 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 115 ? 13.985 1.929   9.893  1.00 12.66 ? 121 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 115 ? 13.821 2.819   9.053  1.00 12.02 ? 121 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 115 ? 12.332 -0.038  9.943  1.00 12.42 ? 121 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 115 ? 11.256 0.937   9.525  1.00 13.13 ? 121 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 115 ? 11.984 -1.437  9.445  1.00 11.94 ? 121 VAL   A CG2 1 
ATOM   905  N  N   . GLY   A 1 116 ? 14.338 2.177   11.159 1.00 13.16 ? 122 GLY   A N   1 
ATOM   906  C  CA  . GLY   A 1 116 ? 14.534 3.517   11.739 1.00 12.88 ? 122 GLY   A CA  1 
ATOM   907  C  C   . GLY   A 1 116 ? 14.752 3.480   13.243 1.00 12.74 ? 122 GLY   A C   1 
ATOM   908  O  O   . GLY   A 1 116 ? 15.032 2.412   13.737 1.00 13.10 ? 122 GLY   A O   1 
ATOM   909  N  N   . ILE   A 1 117 ? 14.638 4.614   13.947 1.00 12.70 ? 123 ILE   A N   1 
ATOM   910  C  CA  . ILE   A 1 117 ? 15.000 4.725   15.392 1.00 13.54 ? 123 ILE   A CA  1 
ATOM   911  C  C   . ILE   A 1 117 ? 13.894 5.434   16.188 1.00 12.87 ? 123 ILE   A C   1 
ATOM   912  O  O   . ILE   A 1 117 ? 13.368 6.424   15.732 1.00 12.67 ? 123 ILE   A O   1 
ATOM   913  C  CB  . ILE   A 1 117 ? 16.346 5.452   15.594 1.00 14.29 ? 123 ILE   A CB  1 
ATOM   914  C  CG1 . ILE   A 1 117 ? 16.453 6.723   14.764 1.00 15.25 ? 123 ILE   A CG1 1 
ATOM   915  C  CG2 . ILE   A 1 117 ? 17.535 4.527   15.344 1.00 15.60 ? 123 ILE   A CG2 1 
ATOM   916  C  CD1 . ILE   A 1 117 ? 17.594 7.622   15.172 1.00 16.10 ? 123 ILE   A CD1 1 
ATOM   917  N  N   . VAL   A 1 118 ? 13.625 5.002   17.412 1.00 13.17 ? 124 VAL   A N   1 
ATOM   918  C  CA  . VAL   A 1 118 ? 12.632 5.716   18.279 1.00 13.41 ? 124 VAL   A CA  1 
ATOM   919  C  C   . VAL   A 1 118 ? 13.002 7.199   18.228 1.00 13.45 ? 124 VAL   A C   1 
ATOM   920  O  O   . VAL   A 1 118 ? 14.205 7.519   18.185 1.00 13.45 ? 124 VAL   A O   1 
ATOM   921  C  CB  . VAL   A 1 118 ? 12.652 5.174   19.709 1.00 13.01 ? 124 VAL   A CB  1 
ATOM   922  C  CG1 . VAL   A 1 118 ? 11.918 6.098   20.660 1.00 13.82 ? 124 VAL   A CG1 1 
ATOM   923  C  CG2 . VAL   A 1 118 ? 12.097 3.766   19.750 1.00 13.27 ? 124 VAL   A CG2 1 
ATOM   924  N  N   . SER   A 1 119 ? 11.999 8.076   18.175 0.72 13.36 ? 125 SER   A N   1 
ATOM   925  C  CA  . SER   A 1 119 ? 12.176 9.547   18.040 0.72 13.38 ? 125 SER   A CA  1 
ATOM   926  C  C   . SER   A 1 119 ? 11.123 10.315  18.856 0.72 13.59 ? 125 SER   A C   1 
ATOM   927  O  O   . SER   A 1 119 ? 11.463 11.409  19.324 0.72 12.80 ? 125 SER   A O   1 
ATOM   928  C  CB  . SER   A 1 119 ? 12.171 9.967   16.590 0.72 12.94 ? 125 SER   A CB  1 
ATOM   929  O  OG  . SER   A 1 119 ? 12.282 11.374  16.482 0.72 12.58 ? 125 SER   A OG  1 
ATOM   930  N  N   . THR   A 1 120 ? 9.904  9.774   18.995 0.72 14.58 ? 126 THR   A N   1 
ATOM   931  C  CA  . THR   A 1 120 ? 8.774  10.375  19.757 0.72 15.11 ? 126 THR   A CA  1 
ATOM   932  C  C   . THR   A 1 120 ? 7.978  9.284   20.481 0.72 16.45 ? 126 THR   A C   1 
ATOM   933  O  O   . THR   A 1 120 ? 8.215  8.096   20.228 0.72 17.10 ? 126 THR   A O   1 
ATOM   934  C  CB  . THR   A 1 120 ? 7.843  11.210  18.863 0.72 14.74 ? 126 THR   A CB  1 
ATOM   935  O  OG1 . THR   A 1 120 ? 7.364  10.468  17.747 0.72 14.56 ? 126 THR   A OG1 1 
ATOM   936  C  CG2 . THR   A 1 120 ? 8.508  12.439  18.290 0.72 15.21 ? 126 THR   A CG2 1 
ATOM   937  N  N   . GLY   A 1 121 ? 7.066  9.702   21.361 0.72 18.09 ? 127 GLY   A N   1 
ATOM   938  C  CA  . GLY   A 1 121 ? 6.075  8.851   22.045 0.72 19.26 ? 127 GLY   A CA  1 
ATOM   939  C  C   . GLY   A 1 121 ? 4.996  9.706   22.684 0.72 20.25 ? 127 GLY   A C   1 
ATOM   940  O  O   . GLY   A 1 121 ? 4.717  10.782  22.145 0.72 20.13 ? 127 GLY   A O   1 
ATOM   941  N  N   . GLY   A 1 122 ? 4.419  9.244   23.797 0.72 22.71 ? 128 GLY   A N   1 
ATOM   942  C  CA  . GLY   A 1 122 ? 3.307  9.902   24.516 0.72 23.11 ? 128 GLY   A CA  1 
ATOM   943  C  C   . GLY   A 1 122 ? 2.007  9.132   24.363 0.72 23.41 ? 128 GLY   A C   1 
ATOM   944  O  O   . GLY   A 1 122 ? 1.690  8.772   23.230 0.72 24.21 ? 128 GLY   A O   1 
ATOM   945  N  N   . ASN   A 1 123 ? 1.316  8.857   25.477 0.72 24.06 ? 129 ASN   A N   1 
ATOM   946  C  CA  . ASN   A 1 123 ? -0.085 8.344   25.549 0.72 23.46 ? 129 ASN   A CA  1 
ATOM   947  C  C   . ASN   A 1 123 ? -0.169 6.883   25.085 0.72 21.49 ? 129 ASN   A C   1 
ATOM   948  O  O   . ASN   A 1 123 ? -1.193 6.514   24.475 0.72 21.48 ? 129 ASN   A O   1 
ATOM   949  C  CB  . ASN   A 1 123 ? -1.044 9.232   24.749 0.72 24.64 ? 129 ASN   A CB  1 
ATOM   950  C  CG  . ASN   A 1 123 ? -0.949 10.688  25.146 0.72 25.53 ? 129 ASN   A CG  1 
ATOM   951  O  OD1 . ASN   A 1 123 ? -0.823 11.001  26.331 0.72 27.58 ? 129 ASN   A OD1 1 
ATOM   952  N  ND2 . ASN   A 1 123 ? -1.009 11.580  24.169 0.72 25.21 ? 129 ASN   A ND2 1 
ATOM   953  N  N   . GLY   A 1 124 ? 0.836  6.065   25.402 0.72 19.19 ? 130 GLY   A N   1 
ATOM   954  C  CA  . GLY   A 1 124 ? 0.906  4.668   24.936 0.72 17.96 ? 130 GLY   A CA  1 
ATOM   955  C  C   . GLY   A 1 124 ? 1.191  4.580   23.442 0.72 17.20 ? 130 GLY   A C   1 
ATOM   956  O  O   . GLY   A 1 124 ? 0.903  3.525   22.849 0.72 17.36 ? 130 GLY   A O   1 
ATOM   957  N  N   . LEU   A 1 125 ? 1.729  5.649   22.846 0.72 16.03 ? 131 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 125 ? 2.214  5.663   21.443 0.72 15.25 ? 131 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 125 ? 3.742  5.694   21.463 0.72 14.71 ? 131 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 125 ? 4.320  5.975   22.538 0.72 14.57 ? 131 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 125 ? 1.637  6.865   20.688 0.72 14.96 ? 131 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 125 ? 0.112  6.956   20.687 0.72 14.85 ? 131 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 125 ? -0.357 8.365   20.361 0.72 14.38 ? 131 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 125 ? -0.478 5.942   19.718 0.72 14.99 ? 131 LEU   A CD2 1 
ATOM   965  N  N   . VAL   A 1 126 ? 4.346  5.356   20.322 0.72 13.77 ? 132 VAL   A N   1 
ATOM   966  C  CA  . VAL   A 1 126 ? 5.812  5.434   20.063 0.72 13.25 ? 132 VAL   A CA  1 
ATOM   967  C  C   . VAL   A 1 126 ? 6.013  5.779   18.578 0.72 12.65 ? 132 VAL   A C   1 
ATOM   968  O  O   . VAL   A 1 126 ? 5.352  5.157   17.718 0.72 12.37 ? 132 VAL   A O   1 
ATOM   969  C  CB  . VAL   A 1 126 ? 6.529  4.134   20.490 0.72 12.85 ? 132 VAL   A CB  1 
ATOM   970  C  CG1 . VAL   A 1 126 ? 5.914  2.888   19.865 0.72 13.04 ? 132 VAL   A CG1 1 
ATOM   971  C  CG2 . VAL   A 1 126 ? 8.026  4.192   20.213 0.72 12.55 ? 132 VAL   A CG2 1 
ATOM   972  N  N   . GLY   A 1 127 ? 6.883  6.752   18.305 0.72 12.34 ? 133 GLY   A N   1 
ATOM   973  C  CA  . GLY   A 1 127 ? 7.163  7.288   16.961 0.72 11.87 ? 133 GLY   A CA  1 
ATOM   974  C  C   . GLY   A 1 127 ? 8.568  6.936   16.521 0.72 11.74 ? 133 GLY   A C   1 
ATOM   975  O  O   . GLY   A 1 127 ? 9.487  7.031   17.365 0.72 11.39 ? 133 GLY   A O   1 
ATOM   976  N  N   . PHE   A 1 128 ? 8.708  6.519   15.253 1.00 11.70 ? 134 PHE   A N   1 
ATOM   977  C  CA  . PHE   A 1 128 ? 9.975  6.045   14.639 1.00 10.43 ? 134 PHE   A CA  1 
ATOM   978  C  C   . PHE   A 1 128 ? 10.336 7.021   13.509 1.00 9.98  ? 134 PHE   A C   1 
ATOM   979  O  O   . PHE   A 1 128 ? 9.490  7.330   12.660 1.00 8.96  ? 134 PHE   A O   1 
ATOM   980  C  CB  . PHE   A 1 128 ? 9.838  4.596   14.188 1.00 9.28  ? 134 PHE   A CB  1 
ATOM   981  C  CG  . PHE   A 1 128 ? 9.400  3.611   15.253 1.00 9.03  ? 134 PHE   A CG  1 
ATOM   982  C  CD1 . PHE   A 1 128 ? 10.293 3.125   16.200 1.00 8.82  ? 134 PHE   A CD1 1 
ATOM   983  C  CD2 . PHE   A 1 128 ? 8.092  3.137   15.305 1.00 8.79  ? 134 PHE   A CD2 1 
ATOM   984  C  CE1 . PHE   A 1 128 ? 9.901  2.200   17.158 1.00 8.58  ? 134 PHE   A CE1 1 
ATOM   985  C  CE2 . PHE   A 1 128 ? 7.706  2.226   16.278 1.00 8.86  ? 134 PHE   A CE2 1 
ATOM   986  C  CZ  . PHE   A 1 128 ? 8.617  1.745   17.193 1.00 8.54  ? 134 PHE   A CZ  1 
ATOM   987  N  N   . ALA   A 1 129 ? 11.541 7.582   13.575 1.00 10.20 ? 135 ALA   A N   1 
ATOM   988  C  CA  . ALA   A 1 129 ? 12.147 8.324   12.449 1.00 11.11 ? 135 ALA   A CA  1 
ATOM   989  C  C   . ALA   A 1 129 ? 12.574 7.286   11.415 1.00 11.95 ? 135 ALA   A C   1 
ATOM   990  O  O   . ALA   A 1 129 ? 13.475 6.539   11.725 1.00 11.59 ? 135 ALA   A O   1 
ATOM   991  C  CB  . ALA   A 1 129 ? 13.277 9.209   12.901 1.00 10.73 ? 135 ALA   A CB  1 
ATOM   992  N  N   . ASP   A 1 130 ? 11.833 7.185   10.299 1.00 13.72 ? 136 ASP   A N   1 
ATOM   993  C  CA  . ASP   A 1 130 ? 12.152 6.331   9.123  1.00 15.98 ? 136 ASP   A CA  1 
ATOM   994  C  C   . ASP   A 1 130 ? 13.538 6.704   8.563  1.00 16.42 ? 136 ASP   A C   1 
ATOM   995  O  O   . ASP   A 1 130 ? 13.888 7.890   8.636  1.00 17.17 ? 136 ASP   A O   1 
ATOM   996  C  CB  . ASP   A 1 130 ? 11.083 6.483   8.034  1.00 17.54 ? 136 ASP   A CB  1 
ATOM   997  C  CG  . ASP   A 1 130 ? 11.278 5.518   6.870  1.00 17.62 ? 136 ASP   A CG  1 
ATOM   998  O  OD1 . ASP   A 1 130 ? 11.480 4.359   7.138  1.00 15.98 ? 136 ASP   A OD1 1 
ATOM   999  O  OD2 . ASP   A 1 130 ? 11.270 5.971   5.705  1.00 21.01 ? 136 ASP   A OD2 1 
ATOM   1000 N  N   . VAL   A 1 131 ? 14.288 5.729   8.024  1.00 16.61 ? 137 VAL   A N   1 
ATOM   1001 C  CA  . VAL   A 1 131 ? 15.616 5.926   7.367  1.00 16.78 ? 137 VAL   A CA  1 
ATOM   1002 C  C   . VAL   A 1 131 ? 15.716 5.073   6.077  1.00 18.16 ? 137 VAL   A C   1 
ATOM   1003 O  O   . VAL   A 1 131 ? 16.793 4.989   5.489  1.00 19.54 ? 137 VAL   A O   1 
ATOM   1004 C  CB  . VAL   A 1 131 ? 16.767 5.586   8.332  1.00 15.62 ? 137 VAL   A CB  1 
ATOM   1005 C  CG1 . VAL   A 1 131 ? 16.589 6.220   9.702  1.00 15.40 ? 137 VAL   A CG1 1 
ATOM   1006 C  CG2 . VAL   A 1 131 ? 16.966 4.080   8.469  1.00 15.44 ? 137 VAL   A CG2 1 
ATOM   1007 N  N   . ARG   A 1 132 ? 14.640 4.460   5.624  1.00 17.64 ? 138 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 132 ? 14.658 3.550   4.454  1.00 18.83 ? 138 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 132 ? 14.756 4.322   3.128  1.00 19.50 ? 138 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 132 ? 15.100 3.706   2.123  1.00 18.78 ? 138 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 132 ? 13.388 2.688   4.468  1.00 18.54 ? 138 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 132 ? 13.296 1.767   5.669  1.00 16.67 ? 138 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 132 ? 12.030 0.968   5.612  1.00 15.97 ? 138 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 132 ? 10.860 1.746   6.021  1.00 14.91 ? 138 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 132 ? 9.677  1.201   6.266  1.00 13.99 ? 138 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 132 ? 9.522  -0.108  6.104  1.00 13.31 ? 138 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 132 ? 8.666  1.952   6.673  1.00 13.16 ? 138 ARG   A NH2 1 
ATOM   1018 N  N   . ASP   A 1 133 ? 14.415 5.609   3.096  1.00 23.03 ? 139 ASP   A N   1 
ATOM   1019 C  CA  . ASP   A 1 133 ? 14.407 6.400   1.845  1.00 22.57 ? 139 ASP   A CA  1 
ATOM   1020 C  C   . ASP   A 1 133 ? 15.849 6.820   1.556  1.00 24.30 ? 139 ASP   A C   1 
ATOM   1021 O  O   . ASP   A 1 133 ? 16.164 7.134   0.385  1.00 26.38 ? 139 ASP   A O   1 
ATOM   1022 C  CB  . ASP   A 1 133 ? 13.400 7.555   1.923  1.00 25.36 ? 139 ASP   A CB  1 
ATOM   1023 C  CG  . ASP   A 1 133 ? 13.619 8.604   2.998  1.00 25.34 ? 139 ASP   A CG  1 
ATOM   1024 O  OD1 . ASP   A 1 133 ? 14.000 8.243   4.109  1.00 27.46 ? 139 ASP   A OD1 1 
ATOM   1025 O  OD2 . ASP   A 1 133 ? 13.371 9.788   2.710  1.00 29.95 ? 139 ASP   A OD2 1 
ATOM   1026 N  N   . LEU   A 1 134 ? 16.715 6.785   2.572  1.00 23.36 ? 140 LEU   A N   1 
ATOM   1027 C  CA  . LEU   A 1 134 ? 18.068 7.416   2.523  1.00 21.23 ? 140 LEU   A CA  1 
ATOM   1028 C  C   . LEU   A 1 134 ? 18.995 6.466   1.785  1.00 20.15 ? 140 LEU   A C   1 
ATOM   1029 O  O   . LEU   A 1 134 ? 19.912 5.904   2.417  1.00 19.61 ? 140 LEU   A O   1 
ATOM   1030 C  CB  . LEU   A 1 134 ? 18.561 7.715   3.946  1.00 19.75 ? 140 LEU   A CB  1 
ATOM   1031 C  CG  . LEU   A 1 134 ? 17.672 8.649   4.762  1.00 18.48 ? 140 LEU   A CG  1 
ATOM   1032 C  CD1 . LEU   A 1 134 ? 18.314 8.941   6.098  1.00 17.79 ? 140 LEU   A CD1 1 
ATOM   1033 C  CD2 . LEU   A 1 134 ? 17.367 9.928   3.993  1.00 17.89 ? 140 LEU   A CD2 1 
ATOM   1034 N  N   . LEU   A 1 135 ? 18.721 6.271   0.497  1.00 21.13 ? 141 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 135 ? 19.397 5.222   -0.314 1.00 22.86 ? 141 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 135 ? 20.914 5.417   -0.214 1.00 22.99 ? 141 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 135 ? 21.589 4.409   -0.045 1.00 22.99 ? 141 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 135 ? 18.902 5.273   -1.758 1.00 22.37 ? 141 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 135 ? 17.396 5.174   -1.956 1.00 23.65 ? 141 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 135 ? 17.080 4.962   -3.427 1.00 25.16 ? 141 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 135 ? 16.772 4.054   -1.133 1.00 23.96 ? 141 LEU   A CD2 1 
ATOM   1042 N  N   . TRP   A 1 136 ? 21.370 6.675   -0.140 1.00 25.46 ? 142 TRP   A N   1 
ATOM   1043 C  CA  . TRP   A 1 136 ? 22.793 7.131   -0.119 1.00 27.95 ? 142 TRP   A CA  1 
ATOM   1044 C  C   . TRP   A 1 136 ? 23.597 6.526   1.033  1.00 30.21 ? 142 TRP   A C   1 
ATOM   1045 O  O   . TRP   A 1 136 ? 24.843 6.600   0.971  1.00 35.27 ? 142 TRP   A O   1 
ATOM   1046 C  CB  . TRP   A 1 136 ? 22.884 8.668   -0.102 1.00 27.36 ? 142 TRP   A CB  1 
ATOM   1047 C  CG  . TRP   A 1 136 ? 22.246 9.400   1.050  1.00 27.60 ? 142 TRP   A CG  1 
ATOM   1048 C  CD1 . TRP   A 1 136 ? 21.014 9.995   1.067  1.00 25.84 ? 142 TRP   A CD1 1 
ATOM   1049 C  CD2 . TRP   A 1 136 ? 22.842 9.711   2.327  1.00 25.66 ? 142 TRP   A CD2 1 
ATOM   1050 N  NE1 . TRP   A 1 136 ? 20.796 10.619  2.268  1.00 25.87 ? 142 TRP   A NE1 1 
ATOM   1051 C  CE2 . TRP   A 1 136 ? 21.891 10.446  3.064  1.00 25.21 ? 142 TRP   A CE2 1 
ATOM   1052 C  CE3 . TRP   A 1 136 ? 24.067 9.415   2.924  1.00 26.59 ? 142 TRP   A CE3 1 
ATOM   1053 C  CZ2 . TRP   A 1 136 ? 22.132 10.894  4.357  1.00 27.34 ? 142 TRP   A CZ2 1 
ATOM   1054 C  CZ3 . TRP   A 1 136 ? 24.298 9.837   4.217  1.00 28.47 ? 142 TRP   A CZ3 1 
ATOM   1055 C  CH2 . TRP   A 1 136 ? 23.356 10.590  4.915  1.00 26.57 ? 142 TRP   A CH2 1 
ATOM   1056 N  N   . LEU   A 1 137 ? 22.947 5.956   2.043  1.00 32.39 ? 143 LEU   A N   1 
ATOM   1057 C  CA  . LEU   A 1 137 ? 23.644 5.289   3.180  1.00 36.18 ? 143 LEU   A CA  1 
ATOM   1058 C  C   . LEU   A 1 137 ? 24.311 3.984   2.698  1.00 37.57 ? 143 LEU   A C   1 
ATOM   1059 O  O   . LEU   A 1 137 ? 25.262 3.536   3.358  1.00 34.19 ? 143 LEU   A O   1 
ATOM   1060 C  CB  . LEU   A 1 137 ? 22.609 5.009   4.281  1.00 37.64 ? 143 LEU   A CB  1 
ATOM   1061 C  CG  . LEU   A 1 137 ? 22.038 6.233   5.007  1.00 35.33 ? 143 LEU   A CG  1 
ATOM   1062 C  CD1 . LEU   A 1 137 ? 20.765 5.883   5.778  1.00 33.50 ? 143 LEU   A CD1 1 
ATOM   1063 C  CD2 . LEU   A 1 137 ? 23.069 6.818   5.961  1.00 36.89 ? 143 LEU   A CD2 1 
ATOM   1064 N  N   . ASP   A 1 138 ? 23.791 3.394   1.607  1.00 41.49 ? 144 ASP   A N   1 
ATOM   1065 C  CA  . ASP   A 1 138 ? 24.214 2.094   1.008  1.00 45.18 ? 144 ASP   A CA  1 
ATOM   1066 C  C   . ASP   A 1 138 ? 25.563 2.219   0.287  1.00 49.27 ? 144 ASP   A C   1 
ATOM   1067 O  O   . ASP   A 1 138 ? 26.234 1.181   0.115  1.00 49.89 ? 144 ASP   A O   1 
ATOM   1068 C  CB  . ASP   A 1 138 ? 23.236 1.612   -0.072 1.00 42.75 ? 144 ASP   A CB  1 
ATOM   1069 C  CG  . ASP   A 1 138 ? 21.959 0.914   0.383  1.00 43.90 ? 144 ASP   A CG  1 
ATOM   1070 O  OD1 . ASP   A 1 138 ? 21.881 0.530   1.581  1.00 43.78 ? 144 ASP   A OD1 1 
ATOM   1071 O  OD2 . ASP   A 1 138 ? 21.040 0.744   -0.493 1.00 42.40 ? 144 ASP   A OD2 1 
ATOM   1072 N  N   . GLU   A 1 139 ? 25.921 3.425   -0.165 1.00 55.02 ? 145 GLU   A N   1 
ATOM   1073 C  CA  . GLU   A 1 139 ? 26.901 3.635   -1.265 1.00 58.55 ? 145 GLU   A CA  1 
ATOM   1074 C  C   . GLU   A 1 139 ? 27.687 4.933   -1.049 1.00 57.90 ? 145 GLU   A C   1 
ATOM   1075 O  O   . GLU   A 1 139 ? 28.772 5.060   -1.636 1.00 56.70 ? 145 GLU   A O   1 
ATOM   1076 C  CB  . GLU   A 1 139 ? 26.146 3.639   -2.595 1.00 60.58 ? 145 GLU   A CB  1 
ATOM   1077 C  CG  . GLU   A 1 139 ? 24.718 4.146   -2.470 1.00 59.32 ? 145 GLU   A CG  1 
ATOM   1078 C  CD  . GLU   A 1 139 ? 23.965 4.355   -3.776 1.00 58.16 ? 145 GLU   A CD  1 
ATOM   1079 O  OE1 . GLU   A 1 139 ? 23.789 5.534   -4.151 1.00 56.32 ? 145 GLU   A OE1 1 
ATOM   1080 O  OE2 . GLU   A 1 139 ? 23.514 3.347   -4.387 1.00 50.89 ? 145 GLU   A OE2 1 
HETATM 1081 ZN ZN  . ZN    B 2 .   ? 10.976 -4.707  5.653  1.00 29.54 ? 201 ZN    A ZN  1 
HETATM 1082 N  N1  . A1BQ4 C 3 .   ? 11.029 14.267  17.920 0.72 10.99 ? 202 A1BQ4 A N1  1 
HETATM 1083 C  C4  . A1BQ4 C 3 .   ? 7.085  10.906  26.420 0.72 13.05 ? 202 A1BQ4 A C4  1 
HETATM 1084 C  C5  . A1BQ4 C 3 .   ? 7.965  11.871  25.970 0.72 12.99 ? 202 A1BQ4 A C5  1 
HETATM 1085 C  C6  . A1BQ4 C 3 .   ? 8.852  11.604  24.931 0.72 12.90 ? 202 A1BQ4 A C6  1 
HETATM 1086 C  C7  . A1BQ4 C 3 .   ? 9.809  12.665  24.439 0.72 12.41 ? 202 A1BQ4 A C7  1 
HETATM 1087 C  C8  . A1BQ4 C 3 .   ? 9.501  13.120  23.024 0.72 11.86 ? 202 A1BQ4 A C8  1 
HETATM 1088 C  C10 . A1BQ4 C 3 .   ? 12.640 14.655  22.331 0.72 11.42 ? 202 A1BQ4 A C10 1 
HETATM 1089 C  C13 . A1BQ4 C 3 .   ? 10.923 15.131  18.912 0.72 11.19 ? 202 A1BQ4 A C13 1 
HETATM 1090 N  N   . A1BQ4 C 3 .   ? 10.264 14.122  22.535 0.72 11.33 ? 202 A1BQ4 A N   1 
HETATM 1091 C  C   . A1BQ4 C 3 .   ? 10.512 9.001   23.289 0.72 13.64 ? 202 A1BQ4 A C   1 
HETATM 1092 O  O   . A1BQ4 C 3 .   ? 9.679  10.155  23.297 0.72 13.28 ? 202 A1BQ4 A O   1 
HETATM 1093 C  C1  . A1BQ4 C 3 .   ? 8.835  10.330  24.360 0.72 13.18 ? 202 A1BQ4 A C1  1 
HETATM 1094 C  C11 . A1BQ4 C 3 .   ? 12.333 15.295  20.981 0.72 11.55 ? 202 A1BQ4 A C11 1 
HETATM 1095 C  C12 . A1BQ4 C 3 .   ? 11.168 14.575  20.304 0.72 11.37 ? 202 A1BQ4 A C12 1 
HETATM 1096 C  C14 . A1BQ4 C 3 .   ? 9.982  14.761  21.248 0.72 11.42 ? 202 A1BQ4 A C14 1 
HETATM 1097 C  C2  . A1BQ4 C 3 .   ? 7.955  9.359   24.818 0.72 13.44 ? 202 A1BQ4 A C2  1 
HETATM 1098 C  C3  . A1BQ4 C 3 .   ? 7.074  9.662   25.845 0.72 13.17 ? 202 A1BQ4 A C3  1 
HETATM 1099 C  C9  . A1BQ4 C 3 .   ? 11.425 14.711  23.212 0.72 11.32 ? 202 A1BQ4 A C9  1 
HETATM 1100 O  O1  . A1BQ4 C 3 .   ? 8.604  12.607  22.372 0.72 11.43 ? 202 A1BQ4 A O1  1 
HETATM 1101 O  O2  . A1BQ4 C 3 .   ? 10.674 16.326  18.737 0.72 11.06 ? 202 A1BQ4 A O2  1 
HETATM 1102 O  O   . HOH   D 4 .   ? 14.814 22.508  9.375  0.72 6.39  ? 301 HOH   A O   1 
HETATM 1103 O  O   . HOH   D 4 .   ? 20.357 8.615   19.017 1.00 11.81 ? 302 HOH   A O   1 
HETATM 1104 O  O   . HOH   D 4 .   ? 23.736 -0.090  15.451 1.00 23.14 ? 303 HOH   A O   1 
HETATM 1105 O  O   . HOH   D 4 .   ? 31.899 1.439   3.511  1.00 23.42 ? 304 HOH   A O   1 
HETATM 1106 O  O   . HOH   D 4 .   ? 27.492 2.530   2.754  1.00 29.28 ? 305 HOH   A O   1 
HETATM 1107 O  O   . HOH   D 4 .   ? 2.894  7.800   10.151 1.00 37.32 ? 306 HOH   A O   1 
HETATM 1108 O  O   . HOH   D 4 .   ? 10.716 8.249   4.572  1.00 15.29 ? 307 HOH   A O   1 
HETATM 1109 O  O   . HOH   D 4 .   ? 11.178 1.776   33.556 1.00 6.50  ? 308 HOH   A O   1 
HETATM 1110 O  O   . HOH   D 4 .   ? 8.551  19.629  18.503 0.72 15.59 ? 309 HOH   A O   1 
HETATM 1111 O  O   . HOH   D 4 .   ? 17.687 18.858  17.064 1.00 17.72 ? 310 HOH   A O   1 
HETATM 1112 O  O   . HOH   D 4 .   ? 8.593  2.041   2.903  1.00 3.70  ? 311 HOH   A O   1 
HETATM 1113 O  O   . HOH   D 4 .   ? 4.764  -4.759  21.514 1.00 62.74 ? 312 HOH   A O   1 
HETATM 1114 O  O   . HOH   D 4 .   ? 0.746  1.712   24.796 1.00 24.94 ? 313 HOH   A O   1 
HETATM 1115 O  O   . HOH   D 4 .   ? 12.972 10.316  9.366  1.00 3.05  ? 314 HOH   A O   1 
HETATM 1116 O  O   . HOH   D 4 .   ? 17.046 21.222  9.405  1.00 22.87 ? 315 HOH   A O   1 
HETATM 1117 O  O   . HOH   D 4 .   ? 23.505 2.515   19.525 1.00 24.30 ? 316 HOH   A O   1 
HETATM 1118 O  O   . HOH   D 4 .   ? 5.630  -1.572  24.574 1.00 12.27 ? 317 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 14.846 2.404   23.351 1.00 14.13 ? 318 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 10.155 3.891   33.737 1.00 18.99 ? 319 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? 3.890  10.931  19.499 1.00 13.61 ? 320 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 19.533 23.491  15.628 1.00 9.54  ? 321 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? 11.214 11.374  11.358 1.00 7.01  ? 322 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 4.315  6.041   25.355 1.00 34.36 ? 323 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 12.004 21.314  12.794 0.72 5.47  ? 324 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 15.088 12.233  24.201 1.00 36.43 ? 325 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? 4.239  -5.484  6.632  1.00 19.74 ? 326 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 6.478  3.494   33.021 1.00 19.22 ? 327 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? 2.880  -2.811  21.841 1.00 27.62 ? 328 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 17.772 2.269   23.335 1.00 10.14 ? 329 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 30.232 11.040  18.896 1.00 13.69 ? 330 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 9.256  -7.654  9.173  1.00 35.08 ? 331 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? 0.325  -0.497  16.727 1.00 18.60 ? 332 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 1.370  -2.738  17.398 1.00 9.27  ? 333 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? 0.500  -3.177  9.931  1.00 32.80 ? 334 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 14.253 -4.934  34.517 1.00 17.31 ? 335 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 22.630 18.317  19.832 1.00 25.09 ? 336 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 14.350 14.310  3.272  1.00 10.72 ? 337 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 5.573  1.654   6.647  1.00 11.91 ? 338 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? 8.774  17.567  26.138 0.72 13.06 ? 339 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 6.758  23.181  26.007 1.00 27.38 ? 340 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 22.608 18.864  6.206  1.00 20.84 ? 341 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 0.980  -3.161  19.520 1.00 15.53 ? 342 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 6.856  11.996  5.173  1.00 9.02  ? 343 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 22.203 8.676   21.115 1.00 12.84 ? 344 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 5.920  22.850  11.195 0.72 6.54  ? 345 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? 10.342 4.113   3.129  1.00 12.72 ? 346 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 0.363  -4.834  16.789 1.00 50.00 ? 347 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 7.975  19.563  7.847  1.00 32.65 ? 348 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? 28.206 16.867  23.408 1.00 37.69 ? 349 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? 15.982 -8.259  25.621 0.72 44.20 ? 350 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 17.304 11.137  1.028  1.00 34.31 ? 351 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? 2.097  0.660   26.827 1.00 22.20 ? 352 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 37.077 17.163  12.219 1.00 30.04 ? 353 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 2.323  2.561   27.467 1.00 18.83 ? 354 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 12.480 -8.527  14.033 1.00 16.66 ? 355 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? 10.071 14.963  28.275 0.72 14.38 ? 356 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? 0.759  -2.401  23.681 1.00 20.73 ? 357 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 2.223  14.282  22.607 0.72 27.56 ? 358 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? 1.798  11.492  18.259 1.00 43.42 ? 359 HOH   A O   1 
HETATM 1161 O  O   . HOH   D 4 .   ? 20.577 -3.084  22.919 1.00 22.42 ? 360 HOH   A O   1 
HETATM 1162 O  O   . HOH   D 4 .   ? 35.429 20.594  16.633 1.00 43.09 ? 361 HOH   A O   1 
HETATM 1163 O  O   . HOH   D 4 .   ? 19.948 -2.810  20.506 1.00 39.32 ? 362 HOH   A O   1 
# 
