data_7HZL
# 
_entry.id   7HZL 
# 
_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   7HZL         pdb_00007hzl 10.2210/pdb7hzl/pdb 
WWPDB D_1001408129 ?            ?                   
# 
_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                        7HZL 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-14 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                             15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn 'ZINC ION'                                                65.409    1   ?         ? ? ? 
3 non-polymer syn 'DIMETHYL SULFOXIDE'                                      78.133    4   ?         ? ? ? 
4 non-polymer syn 'SULFATE ION'                                             96.063    1   ?         ? ? ? 
5 non-polymer syn N-cyclopropyl-5-fluoro-1-methyl-1H-indazole-3-carboxamide 233.242   1   ?         ? ? ? 
6 water       nat water                                                     18.015    137 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'                                                ZN    
3 'DIMETHYL SULFOXIDE'                                      DMS   
4 'SULFATE ION'                                             SO4   
5 N-cyclopropyl-5-fluoro-1-methyl-1H-indazole-3-carboxamide A1BQ0 
6 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 
A1BQ0 non-polymer         . N-cyclopropyl-5-fluoro-1-methyl-1H-indazole-3-carboxamide ? 'C12 H12 F N3 O' 233.242 
ALA   'L-peptide linking' y ALANINE                                                   ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                  ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                           ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                  ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                      ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                 ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                           ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                   ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                 ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                     ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                   ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                    ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                             ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                   ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                    ? 'C3 H7 N O3'     105.093 
SO4   non-polymer         . 'SULFATE ION'                                             ? 'O4 S -2'        96.063  
THR   'L-peptide linking' y THREONINE                                                 ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                  ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                    ? 'C5 H11 N O2'    117.146 
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        A1BQ0 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BQ0 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
B 2 ZN    1   201 1   ZN    ZN  A . 
C 3 DMS   1   202 -1  DMS   DMS A . 
D 3 DMS   1   203 0   DMS   DMS A . 
E 3 DMS   1   204 1   DMS   DMS A . 
F 3 DMS   1   205 3   DMS   DMS A . 
G 4 SO4   1   206 1   SO4   SO4 A . 
H 5 A1BQ0 1   207 246 A1BQ0 LIG A . 
I 6 HOH   1   301 137 HOH   HOH A . 
I 6 HOH   2   302 212 HOH   HOH A . 
I 6 HOH   3   303 60  HOH   HOH A . 
I 6 HOH   4   304 132 HOH   HOH A . 
I 6 HOH   5   305 140 HOH   HOH A . 
I 6 HOH   6   306 49  HOH   HOH A . 
I 6 HOH   7   307 30  HOH   HOH A . 
I 6 HOH   8   308 186 HOH   HOH A . 
I 6 HOH   9   309 34  HOH   HOH A . 
I 6 HOH   10  310 5   HOH   HOH A . 
I 6 HOH   11  311 169 HOH   HOH A . 
I 6 HOH   12  312 104 HOH   HOH A . 
I 6 HOH   13  313 4   HOH   HOH A . 
I 6 HOH   14  314 26  HOH   HOH A . 
I 6 HOH   15  315 121 HOH   HOH A . 
I 6 HOH   16  316 42  HOH   HOH A . 
I 6 HOH   17  317 181 HOH   HOH A . 
I 6 HOH   18  318 111 HOH   HOH A . 
I 6 HOH   19  319 211 HOH   HOH A . 
I 6 HOH   20  320 214 HOH   HOH A . 
I 6 HOH   21  321 68  HOH   HOH A . 
I 6 HOH   22  322 190 HOH   HOH A . 
I 6 HOH   23  323 152 HOH   HOH A . 
I 6 HOH   24  324 24  HOH   HOH A . 
I 6 HOH   25  325 59  HOH   HOH A . 
I 6 HOH   26  326 15  HOH   HOH A . 
I 6 HOH   27  327 41  HOH   HOH A . 
I 6 HOH   28  328 226 HOH   HOH A . 
I 6 HOH   29  329 77  HOH   HOH A . 
I 6 HOH   30  330 2   HOH   HOH A . 
I 6 HOH   31  331 114 HOH   HOH A . 
I 6 HOH   32  332 35  HOH   HOH A . 
I 6 HOH   33  333 219 HOH   HOH A . 
I 6 HOH   34  334 6   HOH   HOH A . 
I 6 HOH   35  335 25  HOH   HOH A . 
I 6 HOH   36  336 85  HOH   HOH A . 
I 6 HOH   37  337 28  HOH   HOH A . 
I 6 HOH   38  338 173 HOH   HOH A . 
I 6 HOH   39  339 37  HOH   HOH A . 
I 6 HOH   40  340 126 HOH   HOH A . 
I 6 HOH   41  341 205 HOH   HOH A . 
I 6 HOH   42  342 33  HOH   HOH A . 
I 6 HOH   43  343 7   HOH   HOH A . 
I 6 HOH   44  344 36  HOH   HOH A . 
I 6 HOH   45  345 144 HOH   HOH A . 
I 6 HOH   46  346 133 HOH   HOH A . 
I 6 HOH   47  347 82  HOH   HOH A . 
I 6 HOH   48  348 131 HOH   HOH A . 
I 6 HOH   49  349 19  HOH   HOH A . 
I 6 HOH   50  350 16  HOH   HOH A . 
I 6 HOH   51  351 20  HOH   HOH A . 
I 6 HOH   52  352 108 HOH   HOH A . 
I 6 HOH   53  353 174 HOH   HOH A . 
I 6 HOH   54  354 9   HOH   HOH A . 
I 6 HOH   55  355 29  HOH   HOH A . 
I 6 HOH   56  356 21  HOH   HOH A . 
I 6 HOH   57  357 106 HOH   HOH A . 
I 6 HOH   58  358 156 HOH   HOH A . 
I 6 HOH   59  359 105 HOH   HOH A . 
I 6 HOH   60  360 147 HOH   HOH A . 
I 6 HOH   61  361 251 HOH   HOH A . 
I 6 HOH   62  362 51  HOH   HOH A . 
I 6 HOH   63  363 55  HOH   HOH A . 
I 6 HOH   64  364 119 HOH   HOH A . 
I 6 HOH   65  365 84  HOH   HOH A . 
I 6 HOH   66  366 170 HOH   HOH A . 
I 6 HOH   67  367 100 HOH   HOH A . 
I 6 HOH   68  368 95  HOH   HOH A . 
I 6 HOH   69  369 62  HOH   HOH A . 
I 6 HOH   70  370 124 HOH   HOH A . 
I 6 HOH   71  371 89  HOH   HOH A . 
I 6 HOH   72  372 161 HOH   HOH A . 
I 6 HOH   73  373 96  HOH   HOH A . 
I 6 HOH   74  374 40  HOH   HOH A . 
I 6 HOH   75  375 203 HOH   HOH A . 
I 6 HOH   76  376 11  HOH   HOH A . 
I 6 HOH   77  377 8   HOH   HOH A . 
I 6 HOH   78  378 177 HOH   HOH A . 
I 6 HOH   79  379 168 HOH   HOH A . 
I 6 HOH   80  380 50  HOH   HOH A . 
I 6 HOH   81  381 12  HOH   HOH A . 
I 6 HOH   82  382 38  HOH   HOH A . 
I 6 HOH   83  383 80  HOH   HOH A . 
I 6 HOH   84  384 90  HOH   HOH A . 
I 6 HOH   85  385 61  HOH   HOH A . 
I 6 HOH   86  386 167 HOH   HOH A . 
I 6 HOH   87  387 204 HOH   HOH A . 
I 6 HOH   88  388 39  HOH   HOH A . 
I 6 HOH   89  389 64  HOH   HOH A . 
I 6 HOH   90  390 10  HOH   HOH A . 
I 6 HOH   91  391 18  HOH   HOH A . 
I 6 HOH   92  392 76  HOH   HOH A . 
I 6 HOH   93  393 138 HOH   HOH A . 
I 6 HOH   94  394 27  HOH   HOH A . 
I 6 HOH   95  395 47  HOH   HOH A . 
I 6 HOH   96  396 233 HOH   HOH A . 
I 6 HOH   97  397 217 HOH   HOH A . 
I 6 HOH   98  398 69  HOH   HOH A . 
I 6 HOH   99  399 23  HOH   HOH A . 
I 6 HOH   100 400 248 HOH   HOH A . 
I 6 HOH   101 401 123 HOH   HOH A . 
I 6 HOH   102 402 128 HOH   HOH A . 
I 6 HOH   103 403 159 HOH   HOH A . 
I 6 HOH   104 404 98  HOH   HOH A . 
I 6 HOH   105 405 120 HOH   HOH A . 
I 6 HOH   106 406 154 HOH   HOH A . 
I 6 HOH   107 407 213 HOH   HOH A . 
I 6 HOH   108 408 252 HOH   HOH A . 
I 6 HOH   109 409 175 HOH   HOH A . 
I 6 HOH   110 410 134 HOH   HOH A . 
I 6 HOH   111 411 158 HOH   HOH A . 
I 6 HOH   112 412 246 HOH   HOH A . 
I 6 HOH   113 413 201 HOH   HOH A . 
I 6 HOH   114 414 189 HOH   HOH A . 
I 6 HOH   115 415 65  HOH   HOH A . 
I 6 HOH   116 416 99  HOH   HOH A . 
I 6 HOH   117 417 117 HOH   HOH A . 
I 6 HOH   118 418 240 HOH   HOH A . 
I 6 HOH   119 419 223 HOH   HOH A . 
I 6 HOH   120 420 88  HOH   HOH A . 
I 6 HOH   121 421 122 HOH   HOH A . 
I 6 HOH   122 422 92  HOH   HOH A . 
I 6 HOH   123 423 171 HOH   HOH A . 
I 6 HOH   124 424 207 HOH   HOH A . 
I 6 HOH   125 425 127 HOH   HOH A . 
I 6 HOH   126 426 86  HOH   HOH A . 
I 6 HOH   127 427 56  HOH   HOH A . 
I 6 HOH   128 428 253 HOH   HOH A . 
I 6 HOH   129 429 153 HOH   HOH A . 
I 6 HOH   130 430 118 HOH   HOH A . 
I 6 HOH   131 431 75  HOH   HOH A . 
I 6 HOH   132 432 208 HOH   HOH A . 
I 6 HOH   133 433 73  HOH   HOH A . 
I 6 HOH   134 434 164 HOH   HOH A . 
I 6 HOH   135 435 243 HOH   HOH A . 
I 6 HOH   136 436 222 HOH   HOH A . 
I 6 HOH   137 437 242 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           7HZL 
_cell.length_a           88.158 
_cell.length_b           57.664 
_cell.length_c           32.736 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.26 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HZL 
_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          7HZL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.62 
_exptl_crystal.density_percent_sol   52.98 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-09-05 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92134 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92134 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HZL 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.23 
_reflns.d_resolution_high            1.66 
_reflns.number_obs                   19414 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.072 
_reflns.pdbx_netI_over_sigmaI        14.0 
_reflns.pdbx_redundancy              6.9 
_reflns.pdbx_Rrim_I_all              0.078 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     134504 
_reflns.pdbx_chi_squared             0.84 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_CC_star                 ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.66 
_reflns_shell.d_res_low                   1.69 
_reflns_shell.number_measured_all         6806 
_reflns_shell.number_unique_obs           960 
_reflns_shell.Rmerge_I_obs                2.542 
_reflns_shell.pdbx_chi_squared            0.35 
_reflns_shell.pdbx_redundancy             7.1 
_reflns_shell.percent_possible_obs        99.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             2.742 
_reflns_shell.pdbx_Rpim_I_all             1.021 
_reflns_shell.pdbx_CC_half                0.374 
_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                                 7HZL 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     18423 
_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                             48.25 
_refine.ls_d_res_high                            1.66 
_refine.ls_percent_reflns_obs                    99.73 
_refine.ls_R_factor_obs                          0.19184 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.18811 
_refine.ls_R_factor_R_free                       0.25990 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  977 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.969 
_refine.correlation_coeff_Fo_to_Fc_free          0.942 
_refine.B_iso_mean                               42.383 
_refine.aniso_B[1][1]                            -0.22 
_refine.aniso_B[2][2]                            -0.90 
_refine.aniso_B[3][3]                            0.92 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            2.49 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.167 
_refine.pdbx_overall_ESU_R_Free                  0.159 
_refine.overall_SU_ML                            0.186 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             6.420 
_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         39 
_refine_hist.number_atoms_solvent             137 
_refine_hist.number_atoms_total               1250 
_refine_hist.d_res_high                       1.66 
_refine_hist.d_res_low                        48.25 
# 
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             0.007  0.015  ? 2960 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.015  ? 1826 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.479  1.625  ? 2950 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.293  1.597  ? 4233 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.776  5.000  ? 284  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       33.589 22.252 ? 111  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       15.439 15.000 ? 303  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       20.321 15.000 ? 12   'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.072  0.200  ? 257  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.007  0.020  ? 2739 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 521  '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                  2.484  4.238  ? 1541 'X-RAY DIFFRACTION' ? 
r_mcbond_other               2.581  4.105  ? 1427 'X-RAY DIFFRACTION' ? 
r_mcangle_it                 4.045  6.042  ? 1368 'X-RAY DIFFRACTION' ? 
r_mcangle_other              4.044  6.040  ? 1369 'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.021  4.552  ? 1418 'X-RAY DIFFRACTION' ? 
r_scbond_other               2.979  4.538  ? 1416 'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_other              4.290  6.608  ? 1571 'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       11.024 48.442 ? 2406 'X-RAY DIFFRACTION' ? 
r_long_range_B_other         11.022 48.488 ? 2407 'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.660 
_refine_ls_shell.d_res_low                        1.703 
_refine_ls_shell.number_reflns_R_work             1358 
_refine_ls_shell.R_factor_R_work                  0.487 
_refine_ls_shell.percent_reflns_obs               97.94 
_refine_ls_shell.R_factor_R_free                  0.463 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             67 
_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                  7HZL 
_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-0030497-001 (A71EV2A-x2339)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HZL 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 5 ? 
I N N 6 ? 
# 
_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              7HZL 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 56  A ZN 201 1_555 ? ? ? ? ? ? ? 2.311 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 58  A ZN 201 1_555 ? ? ? ? ? ? ? 2.454 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 B ZN . ZN ? ? A CYS 116 A ZN 201 1_555 ? ? ? ? ? ? ? 2.266 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 B ZN . ZN ? ? A HIS 118 A ZN 201 1_555 ? ? ? ? ? ? ? 2.205 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.0 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.6 ? 
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_555 116.2 ? 
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_555 111.8 ? 
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 96.2  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? B ZN . ? A ZN 201 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 116.0 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N 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 LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HZL 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -103.54 45.66  
2 1 TRP A 33  ? ? -170.21 139.84 
3 1 ARG A 69  ? ? 37.77   52.45  
4 1 SER A 125 ? ? -133.58 -39.35 
# 
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 
A1BQ0 N1   N  Y N 1   
A1BQ0 C4   C  N N 2   
A1BQ0 C5   C  N N 3   
A1BQ0 C6   C  Y N 4   
A1BQ0 C7   C  Y N 5   
A1BQ0 C8   C  Y N 6   
A1BQ0 C10  C  Y N 7   
A1BQ0 N    N  Y N 8   
A1BQ0 C    C  N N 9   
A1BQ0 O    O  N N 10  
A1BQ0 C1   C  Y N 11  
A1BQ0 C11  C  Y N 12  
A1BQ0 C2   C  N N 13  
A1BQ0 C3   C  N N 14  
A1BQ0 C9   C  Y N 15  
A1BQ0 F    F  N N 16  
A1BQ0 N2   N  N N 17  
A1BQ0 H6   H  N N 18  
A1BQ0 H5   H  N N 19  
A1BQ0 H8   H  N N 20  
A1BQ0 H7   H  N N 21  
A1BQ0 H9   H  N N 22  
A1BQ0 H11  H  N N 23  
A1BQ0 H1   H  N N 24  
A1BQ0 H    H  N N 25  
A1BQ0 H2   H  N N 26  
A1BQ0 H4   H  N N 27  
A1BQ0 H10  H  N N 28  
A1BQ0 H3   H  N N 29  
ALA   N    N  N N 30  
ALA   CA   C  N S 31  
ALA   C    C  N N 32  
ALA   O    O  N N 33  
ALA   CB   C  N N 34  
ALA   OXT  O  N N 35  
ALA   H    H  N N 36  
ALA   H2   H  N N 37  
ALA   HA   H  N N 38  
ALA   HB1  H  N N 39  
ALA   HB2  H  N N 40  
ALA   HB3  H  N N 41  
ALA   HXT  H  N N 42  
ARG   N    N  N N 43  
ARG   CA   C  N S 44  
ARG   C    C  N N 45  
ARG   O    O  N N 46  
ARG   CB   C  N N 47  
ARG   CG   C  N N 48  
ARG   CD   C  N N 49  
ARG   NE   N  N N 50  
ARG   CZ   C  N N 51  
ARG   NH1  N  N N 52  
ARG   NH2  N  N N 53  
ARG   OXT  O  N N 54  
ARG   H    H  N N 55  
ARG   H2   H  N N 56  
ARG   HA   H  N N 57  
ARG   HB2  H  N N 58  
ARG   HB3  H  N N 59  
ARG   HG2  H  N N 60  
ARG   HG3  H  N N 61  
ARG   HD2  H  N N 62  
ARG   HD3  H  N N 63  
ARG   HE   H  N N 64  
ARG   HH11 H  N N 65  
ARG   HH12 H  N N 66  
ARG   HH21 H  N N 67  
ARG   HH22 H  N N 68  
ARG   HXT  H  N N 69  
ASN   N    N  N N 70  
ASN   CA   C  N S 71  
ASN   C    C  N N 72  
ASN   O    O  N N 73  
ASN   CB   C  N N 74  
ASN   CG   C  N N 75  
ASN   OD1  O  N N 76  
ASN   ND2  N  N N 77  
ASN   OXT  O  N N 78  
ASN   H    H  N N 79  
ASN   H2   H  N N 80  
ASN   HA   H  N N 81  
ASN   HB2  H  N N 82  
ASN   HB3  H  N N 83  
ASN   HD21 H  N N 84  
ASN   HD22 H  N N 85  
ASN   HXT  H  N N 86  
ASP   N    N  N N 87  
ASP   CA   C  N S 88  
ASP   C    C  N N 89  
ASP   O    O  N N 90  
ASP   CB   C  N N 91  
ASP   CG   C  N N 92  
ASP   OD1  O  N N 93  
ASP   OD2  O  N N 94  
ASP   OXT  O  N N 95  
ASP   H    H  N N 96  
ASP   H2   H  N N 97  
ASP   HA   H  N N 98  
ASP   HB2  H  N N 99  
ASP   HB3  H  N N 100 
ASP   HD2  H  N N 101 
ASP   HXT  H  N N 102 
CYS   N    N  N N 103 
CYS   CA   C  N R 104 
CYS   C    C  N N 105 
CYS   O    O  N N 106 
CYS   CB   C  N N 107 
CYS   SG   S  N N 108 
CYS   OXT  O  N N 109 
CYS   H    H  N N 110 
CYS   H2   H  N N 111 
CYS   HA   H  N N 112 
CYS   HB2  H  N N 113 
CYS   HB3  H  N N 114 
CYS   HG   H  N N 115 
CYS   HXT  H  N N 116 
DMS   S    S  N N 117 
DMS   O    O  N N 118 
DMS   C1   C  N N 119 
DMS   C2   C  N N 120 
DMS   H11  H  N N 121 
DMS   H12  H  N N 122 
DMS   H13  H  N N 123 
DMS   H21  H  N N 124 
DMS   H22  H  N N 125 
DMS   H23  H  N N 126 
GLN   N    N  N N 127 
GLN   CA   C  N S 128 
GLN   C    C  N N 129 
GLN   O    O  N N 130 
GLN   CB   C  N N 131 
GLN   CG   C  N N 132 
GLN   CD   C  N N 133 
GLN   OE1  O  N N 134 
GLN   NE2  N  N N 135 
GLN   OXT  O  N N 136 
GLN   H    H  N N 137 
GLN   H2   H  N N 138 
GLN   HA   H  N N 139 
GLN   HB2  H  N N 140 
GLN   HB3  H  N N 141 
GLN   HG2  H  N N 142 
GLN   HG3  H  N N 143 
GLN   HE21 H  N N 144 
GLN   HE22 H  N N 145 
GLN   HXT  H  N N 146 
GLU   N    N  N N 147 
GLU   CA   C  N S 148 
GLU   C    C  N N 149 
GLU   O    O  N N 150 
GLU   CB   C  N N 151 
GLU   CG   C  N N 152 
GLU   CD   C  N N 153 
GLU   OE1  O  N N 154 
GLU   OE2  O  N N 155 
GLU   OXT  O  N N 156 
GLU   H    H  N N 157 
GLU   H2   H  N N 158 
GLU   HA   H  N N 159 
GLU   HB2  H  N N 160 
GLU   HB3  H  N N 161 
GLU   HG2  H  N N 162 
GLU   HG3  H  N N 163 
GLU   HE2  H  N N 164 
GLU   HXT  H  N N 165 
GLY   N    N  N N 166 
GLY   CA   C  N N 167 
GLY   C    C  N N 168 
GLY   O    O  N N 169 
GLY   OXT  O  N N 170 
GLY   H    H  N N 171 
GLY   H2   H  N N 172 
GLY   HA2  H  N N 173 
GLY   HA3  H  N N 174 
GLY   HXT  H  N N 175 
HIS   N    N  N N 176 
HIS   CA   C  N S 177 
HIS   C    C  N N 178 
HIS   O    O  N N 179 
HIS   CB   C  N N 180 
HIS   CG   C  Y N 181 
HIS   ND1  N  Y N 182 
HIS   CD2  C  Y N 183 
HIS   CE1  C  Y N 184 
HIS   NE2  N  Y N 185 
HIS   OXT  O  N N 186 
HIS   H    H  N N 187 
HIS   H2   H  N N 188 
HIS   HA   H  N N 189 
HIS   HB2  H  N N 190 
HIS   HB3  H  N N 191 
HIS   HD1  H  N N 192 
HIS   HD2  H  N N 193 
HIS   HE1  H  N N 194 
HIS   HE2  H  N N 195 
HIS   HXT  H  N N 196 
HOH   O    O  N N 197 
HOH   H1   H  N N 198 
HOH   H2   H  N N 199 
ILE   N    N  N N 200 
ILE   CA   C  N S 201 
ILE   C    C  N N 202 
ILE   O    O  N N 203 
ILE   CB   C  N S 204 
ILE   CG1  C  N N 205 
ILE   CG2  C  N N 206 
ILE   CD1  C  N N 207 
ILE   OXT  O  N N 208 
ILE   H    H  N N 209 
ILE   H2   H  N N 210 
ILE   HA   H  N N 211 
ILE   HB   H  N N 212 
ILE   HG12 H  N N 213 
ILE   HG13 H  N N 214 
ILE   HG21 H  N N 215 
ILE   HG22 H  N N 216 
ILE   HG23 H  N N 217 
ILE   HD11 H  N N 218 
ILE   HD12 H  N N 219 
ILE   HD13 H  N N 220 
ILE   HXT  H  N N 221 
LEU   N    N  N N 222 
LEU   CA   C  N S 223 
LEU   C    C  N N 224 
LEU   O    O  N N 225 
LEU   CB   C  N N 226 
LEU   CG   C  N N 227 
LEU   CD1  C  N N 228 
LEU   CD2  C  N N 229 
LEU   OXT  O  N N 230 
LEU   H    H  N N 231 
LEU   H2   H  N N 232 
LEU   HA   H  N N 233 
LEU   HB2  H  N N 234 
LEU   HB3  H  N N 235 
LEU   HG   H  N N 236 
LEU   HD11 H  N N 237 
LEU   HD12 H  N N 238 
LEU   HD13 H  N N 239 
LEU   HD21 H  N N 240 
LEU   HD22 H  N N 241 
LEU   HD23 H  N N 242 
LEU   HXT  H  N N 243 
LYS   N    N  N N 244 
LYS   CA   C  N S 245 
LYS   C    C  N N 246 
LYS   O    O  N N 247 
LYS   CB   C  N N 248 
LYS   CG   C  N N 249 
LYS   CD   C  N N 250 
LYS   CE   C  N N 251 
LYS   NZ   N  N N 252 
LYS   OXT  O  N N 253 
LYS   H    H  N N 254 
LYS   H2   H  N N 255 
LYS   HA   H  N N 256 
LYS   HB2  H  N N 257 
LYS   HB3  H  N N 258 
LYS   HG2  H  N N 259 
LYS   HG3  H  N N 260 
LYS   HD2  H  N N 261 
LYS   HD3  H  N N 262 
LYS   HE2  H  N N 263 
LYS   HE3  H  N N 264 
LYS   HZ1  H  N N 265 
LYS   HZ2  H  N N 266 
LYS   HZ3  H  N N 267 
LYS   HXT  H  N N 268 
MET   N    N  N N 269 
MET   CA   C  N S 270 
MET   C    C  N N 271 
MET   O    O  N N 272 
MET   CB   C  N N 273 
MET   CG   C  N N 274 
MET   SD   S  N N 275 
MET   CE   C  N N 276 
MET   OXT  O  N N 277 
MET   H    H  N N 278 
MET   H2   H  N N 279 
MET   HA   H  N N 280 
MET   HB2  H  N N 281 
MET   HB3  H  N N 282 
MET   HG2  H  N N 283 
MET   HG3  H  N N 284 
MET   HE1  H  N N 285 
MET   HE2  H  N N 286 
MET   HE3  H  N N 287 
MET   HXT  H  N N 288 
PHE   N    N  N N 289 
PHE   CA   C  N S 290 
PHE   C    C  N N 291 
PHE   O    O  N N 292 
PHE   CB   C  N N 293 
PHE   CG   C  Y N 294 
PHE   CD1  C  Y N 295 
PHE   CD2  C  Y N 296 
PHE   CE1  C  Y N 297 
PHE   CE2  C  Y N 298 
PHE   CZ   C  Y N 299 
PHE   OXT  O  N N 300 
PHE   H    H  N N 301 
PHE   H2   H  N N 302 
PHE   HA   H  N N 303 
PHE   HB2  H  N N 304 
PHE   HB3  H  N N 305 
PHE   HD1  H  N N 306 
PHE   HD2  H  N N 307 
PHE   HE1  H  N N 308 
PHE   HE2  H  N N 309 
PHE   HZ   H  N N 310 
PHE   HXT  H  N N 311 
PRO   N    N  N N 312 
PRO   CA   C  N S 313 
PRO   C    C  N N 314 
PRO   O    O  N N 315 
PRO   CB   C  N N 316 
PRO   CG   C  N N 317 
PRO   CD   C  N N 318 
PRO   OXT  O  N N 319 
PRO   H    H  N N 320 
PRO   HA   H  N N 321 
PRO   HB2  H  N N 322 
PRO   HB3  H  N N 323 
PRO   HG2  H  N N 324 
PRO   HG3  H  N N 325 
PRO   HD2  H  N N 326 
PRO   HD3  H  N N 327 
PRO   HXT  H  N N 328 
SER   N    N  N N 329 
SER   CA   C  N S 330 
SER   C    C  N N 331 
SER   O    O  N N 332 
SER   CB   C  N N 333 
SER   OG   O  N N 334 
SER   OXT  O  N N 335 
SER   H    H  N N 336 
SER   H2   H  N N 337 
SER   HA   H  N N 338 
SER   HB2  H  N N 339 
SER   HB3  H  N N 340 
SER   HG   H  N N 341 
SER   HXT  H  N N 342 
SO4   S    S  N N 343 
SO4   O1   O  N N 344 
SO4   O2   O  N N 345 
SO4   O3   O  N N 346 
SO4   O4   O  N N 347 
THR   N    N  N N 348 
THR   CA   C  N S 349 
THR   C    C  N N 350 
THR   O    O  N N 351 
THR   CB   C  N R 352 
THR   OG1  O  N N 353 
THR   CG2  C  N N 354 
THR   OXT  O  N N 355 
THR   H    H  N N 356 
THR   H2   H  N N 357 
THR   HA   H  N N 358 
THR   HB   H  N N 359 
THR   HG1  H  N N 360 
THR   HG21 H  N N 361 
THR   HG22 H  N N 362 
THR   HG23 H  N N 363 
THR   HXT  H  N N 364 
TRP   N    N  N N 365 
TRP   CA   C  N S 366 
TRP   C    C  N N 367 
TRP   O    O  N N 368 
TRP   CB   C  N N 369 
TRP   CG   C  Y N 370 
TRP   CD1  C  Y N 371 
TRP   CD2  C  Y N 372 
TRP   NE1  N  Y N 373 
TRP   CE2  C  Y N 374 
TRP   CE3  C  Y N 375 
TRP   CZ2  C  Y N 376 
TRP   CZ3  C  Y N 377 
TRP   CH2  C  Y N 378 
TRP   OXT  O  N N 379 
TRP   H    H  N N 380 
TRP   H2   H  N N 381 
TRP   HA   H  N N 382 
TRP   HB2  H  N N 383 
TRP   HB3  H  N N 384 
TRP   HD1  H  N N 385 
TRP   HE1  H  N N 386 
TRP   HE3  H  N N 387 
TRP   HZ2  H  N N 388 
TRP   HZ3  H  N N 389 
TRP   HH2  H  N N 390 
TRP   HXT  H  N N 391 
TYR   N    N  N N 392 
TYR   CA   C  N S 393 
TYR   C    C  N N 394 
TYR   O    O  N N 395 
TYR   CB   C  N N 396 
TYR   CG   C  Y N 397 
TYR   CD1  C  Y N 398 
TYR   CD2  C  Y N 399 
TYR   CE1  C  Y N 400 
TYR   CE2  C  Y N 401 
TYR   CZ   C  Y N 402 
TYR   OH   O  N N 403 
TYR   OXT  O  N N 404 
TYR   H    H  N N 405 
TYR   H2   H  N N 406 
TYR   HA   H  N N 407 
TYR   HB2  H  N N 408 
TYR   HB3  H  N N 409 
TYR   HD1  H  N N 410 
TYR   HD2  H  N N 411 
TYR   HE1  H  N N 412 
TYR   HE2  H  N N 413 
TYR   HH   H  N N 414 
TYR   HXT  H  N N 415 
VAL   N    N  N N 416 
VAL   CA   C  N S 417 
VAL   C    C  N N 418 
VAL   O    O  N N 419 
VAL   CB   C  N N 420 
VAL   CG1  C  N N 421 
VAL   CG2  C  N N 422 
VAL   OXT  O  N N 423 
VAL   H    H  N N 424 
VAL   H2   H  N N 425 
VAL   HA   H  N N 426 
VAL   HB   H  N N 427 
VAL   HG11 H  N N 428 
VAL   HG12 H  N N 429 
VAL   HG13 H  N N 430 
VAL   HG21 H  N N 431 
VAL   HG22 H  N N 432 
VAL   HG23 H  N N 433 
VAL   HXT  H  N N 434 
ZN    ZN   ZN N N 435 
# 
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 
A1BQ0 C   N    sing N N 1   
A1BQ0 N   N1   sing Y N 2   
A1BQ0 N1  C1   doub Y N 3   
A1BQ0 C2  C1   sing N N 4   
A1BQ0 O   C2   doub N N 5   
A1BQ0 N2  C2   sing N N 6   
A1BQ0 C3  N2   sing N N 7   
A1BQ0 C3  C4   sing N N 8   
A1BQ0 C4  C5   sing N N 9   
A1BQ0 C5  C3   sing N N 10  
A1BQ0 C1  C6   sing Y N 11  
A1BQ0 C6  C7   doub Y N 12  
A1BQ0 C7  C8   sing Y N 13  
A1BQ0 C8  F    sing N N 14  
A1BQ0 C9  C8   doub Y N 15  
A1BQ0 C10 C9   sing Y N 16  
A1BQ0 C11 C10  doub Y N 17  
A1BQ0 C6  C11  sing Y N 18  
A1BQ0 N   C11  sing Y N 19  
A1BQ0 C4  H6   sing N N 20  
A1BQ0 C4  H5   sing N N 21  
A1BQ0 C5  H8   sing N N 22  
A1BQ0 C5  H7   sing N N 23  
A1BQ0 C7  H9   sing N N 24  
A1BQ0 C10 H11  sing N N 25  
A1BQ0 C   H1   sing N N 26  
A1BQ0 C   H    sing N N 27  
A1BQ0 C   H2   sing N N 28  
A1BQ0 C3  H4   sing N N 29  
A1BQ0 C9  H10  sing N N 30  
A1BQ0 N2  H3   sing N N 31  
ALA   N   CA   sing N N 32  
ALA   N   H    sing N N 33  
ALA   N   H2   sing N N 34  
ALA   CA  C    sing N N 35  
ALA   CA  CB   sing N N 36  
ALA   CA  HA   sing N N 37  
ALA   C   O    doub N N 38  
ALA   C   OXT  sing N N 39  
ALA   CB  HB1  sing N N 40  
ALA   CB  HB2  sing N N 41  
ALA   CB  HB3  sing N N 42  
ALA   OXT HXT  sing N N 43  
ARG   N   CA   sing N N 44  
ARG   N   H    sing N N 45  
ARG   N   H2   sing N N 46  
ARG   CA  C    sing N N 47  
ARG   CA  CB   sing N N 48  
ARG   CA  HA   sing N N 49  
ARG   C   O    doub N N 50  
ARG   C   OXT  sing N N 51  
ARG   CB  CG   sing N N 52  
ARG   CB  HB2  sing N N 53  
ARG   CB  HB3  sing N N 54  
ARG   CG  CD   sing N N 55  
ARG   CG  HG2  sing N N 56  
ARG   CG  HG3  sing N N 57  
ARG   CD  NE   sing N N 58  
ARG   CD  HD2  sing N N 59  
ARG   CD  HD3  sing N N 60  
ARG   NE  CZ   sing N N 61  
ARG   NE  HE   sing N N 62  
ARG   CZ  NH1  sing N N 63  
ARG   CZ  NH2  doub N N 64  
ARG   NH1 HH11 sing N N 65  
ARG   NH1 HH12 sing N N 66  
ARG   NH2 HH21 sing N N 67  
ARG   NH2 HH22 sing N N 68  
ARG   OXT HXT  sing N N 69  
ASN   N   CA   sing N N 70  
ASN   N   H    sing N N 71  
ASN   N   H2   sing N N 72  
ASN   CA  C    sing N N 73  
ASN   CA  CB   sing N N 74  
ASN   CA  HA   sing N N 75  
ASN   C   O    doub N N 76  
ASN   C   OXT  sing N N 77  
ASN   CB  CG   sing N N 78  
ASN   CB  HB2  sing N N 79  
ASN   CB  HB3  sing N N 80  
ASN   CG  OD1  doub N N 81  
ASN   CG  ND2  sing N N 82  
ASN   ND2 HD21 sing N N 83  
ASN   ND2 HD22 sing N N 84  
ASN   OXT HXT  sing N N 85  
ASP   N   CA   sing N N 86  
ASP   N   H    sing N N 87  
ASP   N   H2   sing N N 88  
ASP   CA  C    sing N N 89  
ASP   CA  CB   sing N N 90  
ASP   CA  HA   sing N N 91  
ASP   C   O    doub N N 92  
ASP   C   OXT  sing N N 93  
ASP   CB  CG   sing N N 94  
ASP   CB  HB2  sing N N 95  
ASP   CB  HB3  sing N N 96  
ASP   CG  OD1  doub N N 97  
ASP   CG  OD2  sing N N 98  
ASP   OD2 HD2  sing N N 99  
ASP   OXT HXT  sing N N 100 
CYS   N   CA   sing N N 101 
CYS   N   H    sing N N 102 
CYS   N   H2   sing N N 103 
CYS   CA  C    sing N N 104 
CYS   CA  CB   sing N N 105 
CYS   CA  HA   sing N N 106 
CYS   C   O    doub N N 107 
CYS   C   OXT  sing N N 108 
CYS   CB  SG   sing N N 109 
CYS   CB  HB2  sing N N 110 
CYS   CB  HB3  sing N N 111 
CYS   SG  HG   sing N N 112 
CYS   OXT HXT  sing N N 113 
DMS   S   O    doub N N 114 
DMS   S   C1   sing N N 115 
DMS   S   C2   sing N N 116 
DMS   C1  H11  sing N N 117 
DMS   C1  H12  sing N N 118 
DMS   C1  H13  sing N N 119 
DMS   C2  H21  sing N N 120 
DMS   C2  H22  sing N N 121 
DMS   C2  H23  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
SO4   S   O1   doub N N 330 
SO4   S   O2   doub N N 331 
SO4   S   O3   sing N N 332 
SO4   S   O4   sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_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                    7HZL 
_atom_sites.fract_transf_matrix[1][1]   0.011343 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000448 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017342 
_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]   0.030571 
_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  
F  
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   ? 19.204 6.820   23.886 1.00 45.02  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.425 7.012   23.068 1.00 45.81  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.588 5.878   22.041 1.00 40.42  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.901 4.846   22.178 1.00 43.53  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.621 7.112   23.959 1.00 49.05  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.019 5.824   24.392 1.00 52.70  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.457 6.043   21.043 1.00 43.65  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.755 4.986   20.049 1.00 40.71  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.921 5.527   18.639 1.00 39.48  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.499 6.663   18.390 1.00 42.68  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.494 4.738   17.728 1.00 35.28  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.819 5.158   16.347 1.00 37.30  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.780 3.976   15.401 1.00 35.38  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.915 2.817   15.866 1.00 38.64  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.198 5.800   16.303 1.00 41.42  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.674 4.284   14.104 1.00 33.73  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.856 3.340   12.971 1.00 32.34  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.274 3.543   12.416 1.00 39.49  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.732 4.738   12.332 1.00 38.84  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.778 3.567   11.899 1.00 32.41  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.358 3.661   12.470 1.00 32.53  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.879 2.513   10.810 1.00 37.10  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.349 4.309   11.501 1.00 32.59  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.983 2.443   12.139 1.00 37.25  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.336 2.455   11.522 1.00 39.52  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.242 1.720   10.199 1.00 42.32  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.164 0.455   10.169 1.00 40.11  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.390 1.897   12.484 1.00 41.90  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.528 2.691   13.748 1.00 43.74  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.260 3.875   13.785 1.00 43.28  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.890 2.293   14.905 1.00 41.87  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.352 4.625   14.942 1.00 41.72  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.976 3.028   16.069 1.00 41.72  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.730 4.193   16.094 1.00 43.25  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.780 4.942   17.235 1.00 41.15  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.145 2.492   9.116  1.00 38.60  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.139 1.954   7.742  1.00 36.21  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.320 2.546   6.945  1.00 47.52  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.420 3.798   6.800  1.00 42.19  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.767 2.147   7.064  1.00 38.07  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.260 3.595   7.042  1.00 36.09  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.741 1.519   5.708  1.00 39.62  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.212 1.679   6.454  1.00 45.16  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.423 2.085   5.709  1.00 46.47  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.241 3.058   6.519  1.00 41.82  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.507 2.796   7.715  1.00 46.40  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.561 4.206   5.927  1.00 47.27  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.330 5.251   6.638  1.00 53.36  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.357 6.358   7.050  1.00 59.46  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.729 7.523   6.897  1.00 61.85  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.520 5.721   5.788  1.00 56.22  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.558 4.625   5.617  1.00 50.55  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.301 4.309   6.543  1.00 49.58  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.576 4.011   4.456  1.00 49.57  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.187 6.004   7.611  1.00 49.71  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.142 6.970   8.054  1.00 44.83  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.663 6.584   9.440  1.00 43.08  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.559 5.360   9.733  1.00 47.46  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.974 6.994   7.061  1.00 44.39  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.268 7.566   5.697  1.00 41.48  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.926 8.783   5.536  1.00 45.55  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.893 6.887   4.556  1.00 44.97  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.190 9.296   4.273  1.00 42.69  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.143 7.393   3.290  1.00 49.62  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.796 8.606   3.148  1.00 46.92  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.044 9.057   1.878  1.00 45.83  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.411 7.573   10.287 1.00 42.21  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.766 7.378   11.605 1.00 39.51  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.463 8.194   11.612 1.00 49.99  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.531 9.458   11.501 1.00 42.64  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.720 7.738   12.756 1.00 37.17  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.059 8.043   14.077 1.00 39.11  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.030 8.300   15.233 1.00 43.13  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.601 9.321   16.192 1.00 45.38  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.096 9.105   17.419 1.00 42.83  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.922 7.881   17.896 1.00 45.37  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.764 10.124  18.182 1.00 49.14  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.313 7.529   11.774 1.00 39.68  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.991 8.225   11.852 1.00 40.33  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.527 8.309   13.291 1.00 39.92  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.393 7.234   13.953 1.00 41.11  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.950 7.515   10.981 1.00 35.57  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.696 8.349   10.824 1.00 35.08  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.552 7.105   9.662  1.00 35.82  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.289 9.527   13.773 1.00 30.47  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.779 9.781   15.145 1.00 35.30  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.589 10.732  15.060 1.00 33.37  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.375 11.335  13.992 1.00 36.41  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.820 10.379  16.116 1.00 39.43  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.700 9.345   16.777 1.00 47.78  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.656 11.460  15.441 1.00 39.88  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.827 10.793  16.137 1.00 33.50  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.899 11.914  16.448 1.00 33.23  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.728 13.221  16.413 1.00 37.00  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.779 13.297  17.107 1.00 35.04  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.239 11.776  17.825 1.00 30.05  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.360 10.536  17.945 1.00 32.35  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.819 9.492   18.397 1.00 33.86  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.154 10.598  17.416 1.00 29.25  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.276 14.212  15.660 1.00 38.39  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.928 15.542  15.582 1.00 37.73  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.077 16.077  16.991 1.00 38.45  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.170 16.577  17.291 1.00 40.98  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.155 16.493  14.684 1.00 39.83  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.875 17.815  14.406 1.00 39.06  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.033 18.570  13.396 1.00 39.95  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.506 19.870  12.922 1.00 40.58  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.566 21.000  13.634 1.00 45.33  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.321 21.020  14.932 1.00 46.07  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.918 22.136  13.038 1.00 48.77  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.038 15.940  17.821 1.00 36.93  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.981 16.525  19.185 1.00 35.52  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.995 15.848  20.097 1.00 38.08  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.128 16.353  21.198 1.00 46.01  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.560 16.642  19.755 1.00 36.17  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.977 15.354  20.250 1.00 41.43  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.315 14.473  19.402 1.00 36.78  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.941 14.811  21.489 1.00 38.20  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.912 13.422  20.101 1.00 37.65  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.271 13.604  21.409 1.00 40.06  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.645 14.758  19.682 1.00 44.61  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.619 14.020  20.544 1.00 50.74  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.006 14.025  19.888 1.00 47.66  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.909 13.422  20.451 1.00 51.63  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.126 12.580  20.810 1.00 46.01  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.823 12.469  21.590 1.00 45.27  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.356 11.008  21.714 1.00 44.96  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.940 13.098  22.970 1.00 47.25  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.169 14.625  18.702 1.00 45.59  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.470 14.687  18.000 1.00 44.22  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.561 15.332  18.893 1.00 46.07  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.218 16.195  19.736 1.00 46.91  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.293 15.415  16.697 1.00 47.06  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.821 14.891  18.755 1.00 49.63  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.989 15.449  19.508 1.00 53.07  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.851 16.374  18.624 1.00 51.94  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.586 16.529  17.388 1.00 51.46  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.872 14.343  20.100 1.00 52.92  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.562 13.777  18.997 1.00 51.96  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 28.137 13.268  20.881 1.00 55.50  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.886 16.952  19.242 1.00 62.94  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.972 17.762  18.624 1.00 52.92  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.506 17.072  17.366 1.00 57.55  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.470 17.699  16.266 1.00 51.89  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 32.060 17.956  19.697 1.00 75.69  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 33.243 18.777  19.308 1.00 80.29  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 33.489 20.011  19.896 1.00 81.80  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 34.266 18.533  18.454 1.00 76.56  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 34.603 20.504  19.397 1.00 88.41  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 35.101 19.615  18.503 1.00 86.75  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.975 15.825  17.505 1.00 50.97  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.597 15.098  16.379 1.00 56.23  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.570 14.975  15.253 1.00 59.19  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.970 15.040  14.076 1.00 62.56  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.144 13.742  16.830 1.00 71.72  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.152 13.180  15.852 1.00 77.09  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.039 13.902  15.392 1.00 73.63  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.011 11.907  15.517 1.00 80.49  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.296 14.790  15.607 1.00 56.85  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.191 14.626  14.637 1.00 48.39  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.093 15.912  13.784 1.00 41.49  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.155 15.830  12.561 1.00 46.04  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.853 14.301  15.342 1.00 50.04  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.760 12.985  16.129 1.00 48.94  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.334 11.989  15.692 1.00 46.69  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.073 12.972  17.165 1.00 53.38  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.882 17.074  14.401 0.50 45.02  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.697 18.354  13.655 0.50 46.29  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.949 18.641  12.805 0.50 45.81  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.807 18.885  11.564 0.50 42.54  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.378 19.501  14.622 0.50 47.14  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.943 19.579  15.049 0.50 44.48  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.444 19.333  16.295 0.50 46.21  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.817 19.946  14.232 0.50 45.02  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.088 19.521  16.312 0.50 46.79  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.674 19.904  15.062 0.50 45.90  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.661 20.307  12.888 0.50 45.95  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.398 20.202  14.588 0.50 43.65  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.400 20.610  12.421 0.50 46.61  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.282 20.541  13.260 0.50 46.15  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.126 18.556  13.438 0.50 43.57  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.463 18.600  12.790 0.50 46.66  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.467 17.753  11.509 0.50 46.78  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 32.907 18.262  10.461 0.50 46.23  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.524 18.125  13.758 0.50 44.62  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.014 16.498  11.591 0.50 49.54  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.131 15.504  10.490 0.50 51.31  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.786 15.380  9.768  0.50 52.08  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.596 14.394  9.011  0.50 42.62  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.637 14.160  11.012 0.50 55.03  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.104 14.214  11.380 0.50 53.64  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.967 14.173  10.503 0.50 55.48  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.391 14.319  12.667 0.50 52.33  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.917 16.371  9.982  0.50 50.44  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.559 16.462  9.391  0.50 49.43  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.616 16.119  7.902  0.50 51.52  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.487 16.651  7.174  0.50 46.86  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.998 17.873  9.614  0.50 48.95  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.624 18.135  8.993  0.50 49.64  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.585 17.176  9.558  0.50 49.69  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.186 19.575  9.219  0.50 48.13  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.705 15.246  7.481  0.50 47.26  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.413 14.916  6.062  0.50 47.37  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.080 15.569  5.678  0.50 48.13  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.982 16.119  4.563  0.50 45.72  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.376 13.387  5.859  0.50 45.81  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.990 13.017  4.439  0.50 44.75  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.698 12.740  6.244  0.50 47.03  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.080 15.484  6.561  1.00 47.59  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.702 15.900  6.245  1.00 42.66  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.890 15.901  7.515  1.00 46.41  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.172 15.061  8.390  1.00 43.63  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.098 14.983  5.201  1.00 44.12  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.643 15.227  4.942  1.00 50.20  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.070 16.060  4.017  1.00 45.88  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.564 14.548  5.600  1.00 45.77  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.700 15.939  4.053  1.00 46.62  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.364 15.017  5.015  1.00 45.94  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.507 13.557  6.583  1.00 47.99  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.122 14.532  5.414  1.00 41.22  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.272 13.076  6.962  1.00 41.77  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.105 13.545  6.367  1.00 40.66  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.036 16.916  7.651  1.00 39.51  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.121 17.055  8.799  1.00 38.77  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.864 17.778  8.331  1.00 40.30  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.917 18.637  7.390  1.00 37.25  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.859 17.703  9.958  1.00 38.10  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.438 19.103  9.625  1.00 42.10  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.503 20.308  9.714  1.00 51.51  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.948 21.406  9.253  1.00 45.04  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.354 20.187  10.295 1.00 42.11  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.741 17.357  8.893  1.00 39.55  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.424 17.961  8.629  1.00 36.87  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.763 18.111  9.997  1.00 35.33  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.390 17.065  10.623 1.00 34.56  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.727 17.159  7.523  1.00 37.73  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.392 17.696  7.112  1.00 40.35  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.830 18.417  7.921  1.00 44.57  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.921 17.389  5.965  1.00 45.48  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.614 19.356  10.463 0.51 34.55  ? 36  SER   A N   1 
ATOM   241  C  CA  . SER   A 1 30  ? 15.993 19.698  11.772 0.51 35.61  ? 36  SER   A CA  1 
ATOM   242  C  C   . SER   A 1 30  ? 14.544 19.192  11.801 0.51 35.76  ? 36  SER   A C   1 
ATOM   243  O  O   . SER   A 1 30  ? 14.101 18.698  12.856 0.51 33.78  ? 36  SER   A O   1 
ATOM   244  C  CB  . SER   A 1 30  ? 16.059 21.183  12.031 0.51 35.83  ? 36  SER   A CB  1 
ATOM   245  O  OG  . SER   A 1 30  ? 15.591 21.481  13.332 0.51 31.33  ? 36  SER   A OG  1 
ATOM   246  N  N   . SER   A 1 31  ? 13.843 19.300  10.665 1.00 33.50  ? 37  SER   A N   1 
ATOM   247  C  CA  . SER   A 1 31  ? 12.432 18.909  10.530 1.00 35.06  ? 37  SER   A CA  1 
ATOM   248  C  C   . SER   A 1 31  ? 12.307 17.380  10.602 1.00 33.82  ? 37  SER   A C   1 
ATOM   249  O  O   . SER   A 1 31  ? 11.215 16.949  10.893 1.00 37.37  ? 37  SER   A O   1 
ATOM   250  C  CB  . SER   A 1 31  ? 11.822 19.499  9.280  1.00 39.10  ? 37  SER   A CB  1 
ATOM   251  O  OG  . SER   A 1 31  ? 12.236 18.792  8.136  1.00 47.27  ? 37  SER   A OG  1 
ATOM   252  N  N   . ARG   A 1 32  ? 13.388 16.613  10.421 1.00 30.31  ? 38  ARG   A N   1 
ATOM   253  C  CA  . ARG   A 1 32  ? 13.354 15.128  10.526 1.00 29.84  ? 38  ARG   A CA  1 
ATOM   254  C  C   . ARG   A 1 32  ? 13.980 14.612  11.826 1.00 32.35  ? 38  ARG   A C   1 
ATOM   255  O  O   . ARG   A 1 32  ? 13.883 13.355  12.076 1.00 30.96  ? 38  ARG   A O   1 
ATOM   256  C  CB  . ARG   A 1 32  ? 14.130 14.492  9.370  1.00 32.80  ? 38  ARG   A CB  1 
ATOM   257  C  CG  . ARG   A 1 32  ? 13.451 14.691  8.037  1.00 32.94  ? 38  ARG   A CG  1 
ATOM   258  C  CD  . ARG   A 1 32  ? 14.224 14.061  6.903  1.00 33.45  ? 38  ARG   A CD  1 
ATOM   259  N  NE  . ARG   A 1 32  ? 14.185 12.618  6.907  1.00 31.54  ? 38  ARG   A NE  1 
ATOM   260  C  CZ  . ARG   A 1 32  ? 14.188 11.826  5.839  1.00 33.49  ? 38  ARG   A CZ  1 
ATOM   261  N  NH1 . ARG   A 1 32  ? 14.224 12.325  4.610  1.00 35.37  ? 38  ARG   A NH1 1 
ATOM   262  N  NH2 . ARG   A 1 32  ? 14.109 10.510  6.000  1.00 33.61  ? 38  ARG   A NH2 1 
ATOM   263  N  N   . ASP   A 1 33  ? 14.562 15.493  12.633 1.00 33.65  ? 39  ASP   A N   1 
ATOM   264  C  CA  . ASP   A 1 33  ? 15.390 15.145  13.831 1.00 31.57  ? 39  ASP   A CA  1 
ATOM   265  C  C   . ASP   A 1 33  ? 16.512 14.163  13.446 1.00 31.63  ? 39  ASP   A C   1 
ATOM   266  O  O   . ASP   A 1 33  ? 16.778 13.232  14.248 1.00 30.97  ? 39  ASP   A O   1 
ATOM   267  C  CB  . ASP   A 1 33  ? 14.486 14.623  14.972 1.00 35.73  ? 39  ASP   A CB  1 
ATOM   268  C  CG  . ASP   A 1 33  ? 15.223 14.314  16.286 1.00 33.93  ? 39  ASP   A CG  1 
ATOM   269  O  OD1 . ASP   A 1 33  ? 16.063 15.131  16.678 1.00 32.02  ? 39  ASP   A OD1 1 
ATOM   270  O  OD2 . ASP   A 1 33  ? 14.978 13.211  16.901 1.00 34.86  ? 39  ASP   A OD2 1 
ATOM   271  N  N   . LEU   A 1 34  ? 17.156 14.306  12.273 1.00 32.64  ? 40  LEU   A N   1 
ATOM   272  C  CA  . LEU   A 1 34  ? 18.239 13.379  11.812 1.00 33.76  ? 40  LEU   A CA  1 
ATOM   273  C  C   . LEU   A 1 34  ? 19.548 14.147  11.572 1.00 38.89  ? 40  LEU   A C   1 
ATOM   274  O  O   . LEU   A 1 34  ? 19.513 15.320  11.070 1.00 33.01  ? 40  LEU   A O   1 
ATOM   275  C  CB  . LEU   A 1 34  ? 17.841 12.631  10.535 1.00 38.63  ? 40  LEU   A CB  1 
ATOM   276  C  CG  . LEU   A 1 34  ? 16.815 11.498  10.696 1.00 38.64  ? 40  LEU   A CG  1 
ATOM   277  C  CD1 . LEU   A 1 34  ? 16.613 10.754  9.391  1.00 37.57  ? 40  LEU   A CD1 1 
ATOM   278  C  CD2 . LEU   A 1 34  ? 17.195 10.541  11.833 1.00 36.84  ? 40  LEU   A CD2 1 
ATOM   279  N  N   . LEU   A 1 35  ? 20.656 13.489  11.889 1.00 34.02  ? 41  LEU   A N   1 
ATOM   280  C  CA  . LEU   A 1 35  ? 22.022 13.966  11.547 1.00 37.27  ? 41  LEU   A CA  1 
ATOM   281  C  C   . LEU   A 1 35  ? 22.865 12.753  11.157 1.00 41.16  ? 41  LEU   A C   1 
ATOM   282  O  O   . LEU   A 1 35  ? 22.760 11.694  11.855 1.00 45.81  ? 41  LEU   A O   1 
ATOM   283  C  CB  . LEU   A 1 35  ? 22.615 14.748  12.719 1.00 38.38  ? 41  LEU   A CB  1 
ATOM   284  C  CG  . LEU   A 1 35  ? 24.004 15.352  12.447 1.00 39.93  ? 41  LEU   A CG  1 
ATOM   285  C  CD1 . LEU   A 1 35  ? 24.157 16.644  13.215 1.00 39.82  ? 41  LEU   A CD1 1 
ATOM   286  C  CD2 . LEU   A 1 35  ? 25.097 14.370  12.871 1.00 42.40  ? 41  LEU   A CD2 1 
ATOM   287  N  N   . VAL   A 1 36  ? 23.553 12.843  10.013 1.00 38.72  ? 42  VAL   A N   1 
ATOM   288  C  CA  . VAL   A 1 36  ? 24.495 11.790  9.533  1.00 38.29  ? 42  VAL   A CA  1 
ATOM   289  C  C   . VAL   A 1 36  ? 25.881 12.442  9.573  1.00 50.35  ? 42  VAL   A C   1 
ATOM   290  O  O   . VAL   A 1 36  ? 26.005 13.567  9.022  1.00 38.80  ? 42  VAL   A O   1 
ATOM   291  C  CB  . VAL   A 1 36  ? 24.126 11.229  8.154  1.00 41.77  ? 42  VAL   A CB  1 
ATOM   292  C  CG1 . VAL   A 1 36  ? 25.134 10.186  7.682  1.00 45.01  ? 42  VAL   A CG1 1 
ATOM   293  C  CG2 . VAL   A 1 36  ? 22.710 10.664  8.103  1.00 39.10  ? 42  VAL   A CG2 1 
ATOM   294  N  N   . SER   A 1 37  ? 26.810 11.814  10.307 1.00 47.71  ? 43  SER   A N   1 
ATOM   295  C  CA  . SER   A 1 37  ? 28.258 12.147  10.398 1.00 48.99  ? 43  SER   A CA  1 
ATOM   296  C  C   . SER   A 1 37  ? 29.097 11.044  9.734  1.00 57.16  ? 43  SER   A C   1 
ATOM   297  O  O   . SER   A 1 37  ? 28.605 9.889   9.650  1.00 46.88  ? 43  SER   A O   1 
ATOM   298  C  CB  . SER   A 1 37  ? 28.658 12.432  11.845 1.00 48.07  ? 43  SER   A CB  1 
ATOM   299  O  OG  . SER   A 1 37  ? 28.423 11.342  12.729 1.00 52.18  ? 43  SER   A OG  1 
ATOM   300  N  N   . SER   A 1 38  ? 30.273 11.405  9.171  1.00 52.17  ? 44  SER   A N   1 
ATOM   301  C  CA  . SER   A 1 38  ? 31.298 10.465  8.625  1.00 48.80  ? 44  SER   A CA  1 
ATOM   302  C  C   . SER   A 1 38  ? 31.972 9.704   9.776  1.00 44.68  ? 44  SER   A C   1 
ATOM   303  O  O   . SER   A 1 38  ? 32.108 10.247  10.871 1.00 48.64  ? 44  SER   A O   1 
ATOM   304  C  CB  . SER   A 1 38  ? 32.343 11.215  7.829  1.00 54.08  ? 44  SER   A CB  1 
ATOM   305  O  OG  . SER   A 1 38  ? 32.972 12.132  8.691  1.00 60.22  ? 44  SER   A OG  1 
ATOM   306  N  N   . THR   A 1 39  ? 32.379 8.461   9.502  0.50 49.94  ? 45  THR   A N   1 
ATOM   307  C  CA  . THR   A 1 39  ? 33.063 7.546   10.455 0.50 46.78  ? 45  THR   A CA  1 
ATOM   308  C  C   . THR   A 1 39  ? 34.381 7.069   9.840  0.50 49.80  ? 45  THR   A C   1 
ATOM   309  O  O   . THR   A 1 39  ? 34.465 7.000   8.598  0.50 51.22  ? 45  THR   A O   1 
ATOM   310  C  CB  . THR   A 1 39  ? 32.191 6.325   10.780 0.50 45.92  ? 45  THR   A CB  1 
ATOM   311  O  OG1 . THR   A 1 39  ? 32.215 5.483   9.629  0.50 44.62  ? 45  THR   A OG1 1 
ATOM   312  C  CG2 . THR   A 1 39  ? 30.765 6.691   11.132 0.50 43.64  ? 45  THR   A CG2 1 
ATOM   313  N  N   . THR   A 1 40  ? 35.356 6.726   10.684 0.50 54.28  ? 46  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 40  ? 36.657 6.140   10.270 0.50 59.81  ? 46  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 40  ? 36.429 4.672   9.885  0.50 59.95  ? 46  THR   A C   1 
ATOM   316  O  O   . THR   A 1 40  ? 36.765 4.305   8.739  0.50 59.93  ? 46  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 40  ? 37.719 6.353   11.360 0.50 61.63  ? 46  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 40  ? 37.139 6.078   12.635 0.50 67.03  ? 46  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 40  ? 38.265 7.764   11.374 0.50 61.85  ? 46  THR   A CG2 1 
ATOM   320  N  N   . ALA   A 1 41  ? 35.847 3.878   10.790 0.50 58.53  ? 47  ALA   A N   1 
ATOM   321  C  CA  . ALA   A 1 41  ? 35.598 2.426   10.612 0.50 57.10  ? 47  ALA   A CA  1 
ATOM   322  C  C   . ALA   A 1 41  ? 34.334 2.197   9.770  0.50 57.08  ? 47  ALA   A C   1 
ATOM   323  O  O   . ALA   A 1 41  ? 33.460 3.090   9.744  0.50 54.66  ? 47  ALA   A O   1 
ATOM   324  C  CB  . ALA   A 1 41  ? 35.486 1.763   11.965 0.50 56.84  ? 47  ALA   A CB  1 
ATOM   325  N  N   . GLN   A 1 42  ? 34.239 1.027   9.127  0.50 53.88  ? 48  GLN   A N   1 
ATOM   326  C  CA  . GLN   A 1 42  ? 33.073 0.582   8.316  0.50 51.71  ? 48  GLN   A CA  1 
ATOM   327  C  C   . GLN   A 1 42  ? 31.998 -0.011  9.240  0.50 48.39  ? 48  GLN   A C   1 
ATOM   328  O  O   . GLN   A 1 42  ? 32.349 -0.840  10.104 0.50 44.85  ? 48  GLN   A O   1 
ATOM   329  C  CB  . GLN   A 1 42  ? 33.527 -0.449  7.285  0.50 55.14  ? 48  GLN   A CB  1 
ATOM   330  C  CG  . GLN   A 1 42  ? 32.383 -1.210  6.632  0.50 57.24  ? 48  GLN   A CG  1 
ATOM   331  C  CD  . GLN   A 1 42  ? 32.062 -0.700  5.249  0.50 60.34  ? 48  GLN   A CD  1 
ATOM   332  O  OE1 . GLN   A 1 42  ? 31.033 -1.040  4.667  0.50 62.47  ? 48  GLN   A OE1 1 
ATOM   333  N  NE2 . GLN   A 1 42  ? 32.952 0.119   4.710  0.50 60.14  ? 48  GLN   A NE2 1 
ATOM   334  N  N   . GLY   A 1 43  ? 30.741 0.411   9.065  0.50 44.23  ? 49  GLY   A N   1 
ATOM   335  C  CA  . GLY   A 1 43  ? 29.575 -0.028  9.861  0.50 42.30  ? 49  GLY   A CA  1 
ATOM   336  C  C   . GLY   A 1 43  ? 28.946 -1.275  9.268  0.50 39.68  ? 49  GLY   A C   1 
ATOM   337  O  O   . GLY   A 1 43  ? 29.277 -1.611  8.112  0.50 39.31  ? 49  GLY   A O   1 
ATOM   338  N  N   . CYS   A 1 44  ? 28.083 -1.968  10.014 0.50 37.72  ? 50  CYS   A N   1 
ATOM   339  C  CA  . CYS   A 1 44  ? 27.600 -3.312  9.615  0.50 38.93  ? 50  CYS   A CA  1 
ATOM   340  C  C   . CYS   A 1 44  ? 26.070 -3.373  9.534  0.50 38.98  ? 50  CYS   A C   1 
ATOM   341  O  O   . CYS   A 1 44  ? 25.549 -4.438  9.151  0.50 39.86  ? 50  CYS   A O   1 
ATOM   342  C  CB  . CYS   A 1 44  ? 28.197 -4.362  10.545 0.50 41.02  ? 50  CYS   A CB  1 
ATOM   343  S  SG  . CYS   A 1 44  ? 29.953 -4.629  10.175 0.50 39.09  ? 50  CYS   A SG  1 
ATOM   344  N  N   . ASP   A 1 45  ? 25.377 -2.265  9.805  0.50 38.27  ? 51  ASP   A N   1 
ATOM   345  C  CA  . ASP   A 1 45  ? 23.894 -2.199  9.721  0.50 37.42  ? 51  ASP   A CA  1 
ATOM   346  C  C   . ASP   A 1 45  ? 23.505 -2.153  8.240  0.50 37.65  ? 51  ASP   A C   1 
ATOM   347  O  O   . ASP   A 1 45  ? 24.215 -1.489  7.464  0.50 39.90  ? 51  ASP   A O   1 
ATOM   348  C  CB  . ASP   A 1 45  ? 23.357 -1.019  10.541 0.50 36.42  ? 51  ASP   A CB  1 
ATOM   349  C  CG  . ASP   A 1 45  ? 23.695 -1.140  12.023 0.50 37.22  ? 51  ASP   A CG  1 
ATOM   350  O  OD1 . ASP   A 1 45  ? 23.860 -2.301  12.485 0.50 35.26  ? 51  ASP   A OD1 1 
ATOM   351  O  OD2 . ASP   A 1 45  ? 23.795 -0.091  12.706 0.50 36.62  ? 51  ASP   A OD2 1 
ATOM   352  N  N   . THR   A 1 46  ? 22.430 -2.852  7.874  1.00 36.39  ? 52  THR   A N   1 
ATOM   353  C  CA  . THR   A 1 46  ? 21.788 -2.781  6.545  1.00 39.20  ? 52  THR   A CA  1 
ATOM   354  C  C   . THR   A 1 46  ? 20.532 -1.907  6.657  1.00 40.42  ? 52  THR   A C   1 
ATOM   355  O  O   . THR   A 1 46  ? 19.748 -2.161  7.574  1.00 30.23  ? 52  THR   A O   1 
ATOM   356  C  CB  . THR   A 1 46  ? 21.451 -4.189  6.054  1.00 45.10  ? 52  THR   A CB  1 
ATOM   357  O  OG1 . THR   A 1 46  ? 22.702 -4.853  5.847  1.00 45.54  ? 52  THR   A OG1 1 
ATOM   358  C  CG2 . THR   A 1 46  ? 20.640 -4.196  4.774  1.00 46.69  ? 52  THR   A CG2 1 
ATOM   359  N  N   . ILE   A 1 47  ? 20.350 -0.940  5.754  1.00 36.29  ? 53  ILE   A N   1 
ATOM   360  C  CA  . ILE   A 1 47  ? 19.145 -0.079  5.722  1.00 35.90  ? 53  ILE   A CA  1 
ATOM   361  C  C   . ILE   A 1 47  ? 18.080 -0.829  4.914  1.00 41.78  ? 53  ILE   A C   1 
ATOM   362  O  O   . ILE   A 1 47  ? 18.399 -1.388  3.837  1.00 36.38  ? 53  ILE   A O   1 
ATOM   363  C  CB  . ILE   A 1 47  ? 19.436 1.326   5.177  1.00 39.86  ? 53  ILE   A CB  1 
ATOM   364  C  CG1 . ILE   A 1 47  ? 20.577 2.007   5.943  1.00 38.07  ? 53  ILE   A CG1 1 
ATOM   365  C  CG2 . ILE   A 1 47  ? 18.150 2.144   5.186  1.00 38.74  ? 53  ILE   A CG2 1 
ATOM   366  C  CD1 . ILE   A 1 47  ? 20.354 2.143   7.445  1.00 34.94  ? 53  ILE   A CD1 1 
ATOM   367  N  N   . ALA   A 1 48  ? 16.861 -0.893  5.433  1.00 32.71  ? 54  ALA   A N   1 
ATOM   368  C  CA  . ALA   A 1 48  ? 15.733 -1.519  4.717  1.00 32.05  ? 54  ALA   A CA  1 
ATOM   369  C  C   . ALA   A 1 48  ? 15.396 -0.655  3.504  1.00 30.19  ? 54  ALA   A C   1 
ATOM   370  O  O   . ALA   A 1 48  ? 15.422 0.591   3.601  1.00 29.19  ? 54  ALA   A O   1 
ATOM   371  C  CB  . ALA   A 1 48  ? 14.573 -1.706  5.655  1.00 30.15  ? 54  ALA   A CB  1 
ATOM   372  N  N   . ARG   A 1 49  ? 15.060 -1.299  2.390  1.00 35.56  ? 55  ARG   A N   1 
ATOM   373  C  CA  . ARG   A 1 49  ? 14.559 -0.633  1.171  1.00 35.04  ? 55  ARG   A CA  1 
ATOM   374  C  C   . ARG   A 1 49  ? 13.220 -1.293  0.828  1.00 34.63  ? 55  ARG   A C   1 
ATOM   375  O  O   . ARG   A 1 49  ? 13.202 -2.322  0.098  1.00 37.06  ? 55  ARG   A O   1 
ATOM   376  C  CB  . ARG   A 1 49  ? 15.637 -0.692  0.074  1.00 39.89  ? 55  ARG   A CB  1 
ATOM   377  C  CG  . ARG   A 1 49  ? 16.976 -0.058  0.467  1.00 39.97  ? 55  ARG   A CG  1 
ATOM   378  C  CD  . ARG   A 1 49  ? 16.950 1.437   0.789  1.00 42.27  ? 55  ARG   A CD  1 
ATOM   379  N  NE  . ARG   A 1 49  ? 18.270 1.892   1.239  1.00 41.74  ? 55  ARG   A NE  1 
ATOM   380  C  CZ  . ARG   A 1 49  ? 18.538 3.075   1.786  1.00 41.49  ? 55  ARG   A CZ  1 
ATOM   381  N  NH1 . ARG   A 1 49  ? 17.573 3.955   2.005  1.00 46.99  ? 55  ARG   A NH1 1 
ATOM   382  N  NH2 . ARG   A 1 49  ? 19.768 3.364   2.169  1.00 42.97  ? 55  ARG   A NH2 1 
ATOM   383  N  N   . CYS   A 1 50  ? 12.120 -0.764  1.373  1.00 35.28  ? 56  CYS   A N   1 
ATOM   384  C  CA  . CYS   A 1 50  ? 10.823 -1.483  1.511  1.00 34.10  ? 56  CYS   A CA  1 
ATOM   385  C  C   . CYS   A 1 50  ? 9.704  -0.516  1.934  1.00 35.97  ? 56  CYS   A C   1 
ATOM   386  O  O   . CYS   A 1 50  ? 9.982  0.676   2.257  1.00 33.70  ? 56  CYS   A O   1 
ATOM   387  C  CB  . CYS   A 1 50  ? 10.947 -2.626  2.499  1.00 34.54  ? 56  CYS   A CB  1 
ATOM   388  S  SG  . CYS   A 1 50  ? 11.112 -2.052  4.225  1.00 33.20  ? 56  CYS   A SG  1 
ATOM   389  N  N   A ASP   A 1 51  ? 8.445  -0.969  1.902  0.26 36.47  ? 57  ASP   A N   1 
ATOM   390  N  N   B ASP   A 1 51  ? 8.482  -1.066  1.937  0.25 38.70  ? 57  ASP   A N   1 
ATOM   391  C  CA  A ASP   A 1 51  ? 7.290  -0.221  2.477  0.26 35.08  ? 57  ASP   A CA  1 
ATOM   392  C  CA  B ASP   A 1 51  ? 7.204  -0.403  2.302  0.25 38.58  ? 57  ASP   A CA  1 
ATOM   393  C  C   A ASP   A 1 51  ? 6.623  -1.089  3.558  0.26 36.64  ? 57  ASP   A C   1 
ATOM   394  C  C   B ASP   A 1 51  ? 6.665  -0.973  3.628  0.25 38.96  ? 57  ASP   A C   1 
ATOM   395  O  O   A ASP   A 1 51  ? 5.377  -1.078  3.652  0.26 35.36  ? 57  ASP   A O   1 
ATOM   396  O  O   B ASP   A 1 51  ? 5.544  -0.581  3.999  0.25 38.15  ? 57  ASP   A O   1 
ATOM   397  C  CB  A ASP   A 1 51  ? 6.294  0.199   1.393  0.26 34.72  ? 57  ASP   A CB  1 
ATOM   398  C  CB  B ASP   A 1 51  ? 6.169  -0.618  1.192  0.25 40.03  ? 57  ASP   A CB  1 
ATOM   399  C  CG  A ASP   A 1 51  ? 5.517  -0.968  0.813  0.26 35.50  ? 57  ASP   A CG  1 
ATOM   400  C  CG  B ASP   A 1 51  ? 5.244  0.561   0.954  0.25 41.51  ? 57  ASP   A CG  1 
ATOM   401  O  OD1 A ASP   A 1 51  ? 6.028  -2.098  0.871  0.26 35.82  ? 57  ASP   A OD1 1 
ATOM   402  O  OD1 B ASP   A 1 51  ? 5.675  1.700   1.194  0.25 47.72  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 A ASP   A 1 51  ? 4.412  -0.735  0.313  0.26 40.72  ? 57  ASP   A OD2 1 
ATOM   404  O  OD2 B ASP   A 1 51  ? 4.101  0.334   0.504  0.25 44.73  ? 57  ASP   A OD2 1 
ATOM   405  N  N   . CYS   A 1 52  ? 7.424  -1.842  4.315  1.00 37.60  ? 58  CYS   A N   1 
ATOM   406  C  CA  . CYS   A 1 52  ? 6.954  -2.563  5.549  1.00 37.14  ? 58  CYS   A CA  1 
ATOM   407  C  C   . CYS   A 1 52  ? 6.242  -1.618  6.523  1.00 34.06  ? 58  CYS   A C   1 
ATOM   408  O  O   . CYS   A 1 52  ? 6.652  -0.425  6.681  1.00 29.27  ? 58  CYS   A O   1 
ATOM   409  C  CB  . CYS   A 1 52  ? 8.104  -3.241  6.271  1.00 35.44  ? 58  CYS   A CB  1 
ATOM   410  S  SG  . CYS   A 1 52  ? 8.598  -4.776  5.448  1.00 39.88  ? 58  CYS   A SG  1 
ATOM   411  N  N   . GLN   A 1 53  ? 5.182  -2.108  7.173  1.00 31.36  ? 59  GLN   A N   1 
ATOM   412  C  CA  . GLN   A 1 53  ? 4.475  -1.339  8.223  1.00 34.56  ? 59  GLN   A CA  1 
ATOM   413  C  C   . GLN   A 1 53  ? 4.417  -2.186  9.507  1.00 35.14  ? 59  GLN   A C   1 
ATOM   414  O  O   . GLN   A 1 53  ? 3.645  -1.854  10.405 1.00 30.53  ? 59  GLN   A O   1 
ATOM   415  C  CB  . GLN   A 1 53  ? 3.092  -0.916  7.714  1.00 37.50  ? 59  GLN   A CB  1 
ATOM   416  C  CG  . GLN   A 1 53  ? 3.072  0.392   6.962  1.00 45.11  ? 59  GLN   A CG  1 
ATOM   417  C  CD  . GLN   A 1 53  ? 1.639  0.839   6.782  1.00 47.44  ? 59  GLN   A CD  1 
ATOM   418  O  OE1 . GLN   A 1 53  ? 1.054  0.654   5.707  1.00 39.46  ? 59  GLN   A OE1 1 
ATOM   419  N  NE2 . GLN   A 1 53  ? 1.063  1.426   7.830  1.00 42.71  ? 59  GLN   A NE2 1 
ATOM   420  N  N   . THR   A 1 54  ? 5.190  -3.262  9.571  1.00 32.81  ? 60  THR   A N   1 
ATOM   421  C  CA  . THR   A 1 54  ? 5.355  -4.068  10.798 1.00 31.87  ? 60  THR   A CA  1 
ATOM   422  C  C   . THR   A 1 54  ? 6.837  -4.291  11.013 1.00 32.20  ? 60  THR   A C   1 
ATOM   423  O  O   . THR   A 1 54  ? 7.637  -4.393  10.040 1.00 29.82  ? 60  THR   A O   1 
ATOM   424  C  CB  . THR   A 1 54  ? 4.549  -5.380  10.795 1.00 30.78  ? 60  THR   A CB  1 
ATOM   425  O  OG1 . THR   A 1 54  ? 5.129  -6.139  9.761  1.00 35.29  ? 60  THR   A OG1 1 
ATOM   426  C  CG2 . THR   A 1 54  ? 3.076  -5.229  10.507 1.00 32.27  ? 60  THR   A CG2 1 
ATOM   427  N  N   . GLY   A 1 55  ? 7.226  -4.322  12.261 1.00 27.33  ? 61  GLY   A N   1 
ATOM   428  C  CA  . GLY   A 1 55  ? 8.636  -4.435  12.662 1.00 25.55  ? 61  GLY   A CA  1 
ATOM   429  C  C   . GLY   A 1 55  ? 8.744  -4.593  14.163 1.00 28.38  ? 61  GLY   A C   1 
ATOM   430  O  O   . GLY   A 1 55  ? 7.693  -4.825  14.773 1.00 29.88  ? 61  GLY   A O   1 
ATOM   431  N  N   . VAL   A 1 56  ? 9.951  -4.441  14.685 1.00 26.73  ? 62  VAL   A N   1 
ATOM   432  C  CA  . VAL   A 1 56  ? 10.340 -4.610  16.111 1.00 30.52  ? 62  VAL   A CA  1 
ATOM   433  C  C   . VAL   A 1 56  ? 11.206 -3.414  16.478 1.00 28.38  ? 62  VAL   A C   1 
ATOM   434  O  O   . VAL   A 1 56  ? 12.112 -3.080  15.743 1.00 29.73  ? 62  VAL   A O   1 
ATOM   435  C  CB  . VAL   A 1 56  ? 11.087 -5.945  16.339 1.00 31.69  ? 62  VAL   A CB  1 
ATOM   436  C  CG1 . VAL   A 1 56  ? 11.617 -6.103  17.759 1.00 35.22  ? 62  VAL   A CG1 1 
ATOM   437  C  CG2 . VAL   A 1 56  ? 10.199 -7.112  16.003 1.00 37.07  ? 62  VAL   A CG2 1 
ATOM   438  N  N   . TYR   A 1 57  ? 10.941 -2.782  17.607 1.00 27.82  ? 63  TYR   A N   1 
ATOM   439  C  CA  . TYR   A 1 57  ? 11.808 -1.689  18.082 1.00 23.27  ? 63  TYR   A CA  1 
ATOM   440  C  C   . TYR   A 1 57  ? 12.353 -2.019  19.467 1.00 28.88  ? 63  TYR   A C   1 
ATOM   441  O  O   . TYR   A 1 57  ? 11.700 -2.739  20.216 1.00 28.95  ? 63  TYR   A O   1 
ATOM   442  C  CB  . TYR   A 1 57  ? 11.083 -0.339  18.067 1.00 26.26  ? 63  TYR   A CB  1 
ATOM   443  C  CG  . TYR   A 1 57  ? 10.160 -0.055  19.233 1.00 29.54  ? 63  TYR   A CG  1 
ATOM   444  C  CD1 . TYR   A 1 57  ? 8.866  -0.570  19.272 1.00 29.96  ? 63  TYR   A CD1 1 
ATOM   445  C  CD2 . TYR   A 1 57  ? 10.564 0.769   20.269 1.00 30.81  ? 63  TYR   A CD2 1 
ATOM   446  C  CE1 . TYR   A 1 57  ? 8.000  -0.240  20.309 1.00 36.00  ? 63  TYR   A CE1 1 
ATOM   447  C  CE2 . TYR   A 1 57  ? 9.704  1.116   21.305 1.00 32.67  ? 63  TYR   A CE2 1 
ATOM   448  C  CZ  . TYR   A 1 57  ? 8.422  0.591   21.335 1.00 33.01  ? 63  TYR   A CZ  1 
ATOM   449  O  OH  . TYR   A 1 57  ? 7.540  0.865   22.346 1.00 34.47  ? 63  TYR   A OH  1 
ATOM   450  N  N   . TYR   A 1 58  ? 13.494 -1.425  19.776 1.00 30.10  ? 64  TYR   A N   1 
ATOM   451  C  CA  . TYR   A 1 58  ? 14.129 -1.546  21.102 1.00 27.26  ? 64  TYR   A CA  1 
ATOM   452  C  C   . TYR   A 1 58  ? 13.710 -0.368  21.965 1.00 29.11  ? 64  TYR   A C   1 
ATOM   453  O  O   . TYR   A 1 58  ? 13.940 0.764   21.598 1.00 28.33  ? 64  TYR   A O   1 
ATOM   454  C  CB  . TYR   A 1 58  ? 15.634 -1.616  20.985 1.00 27.20  ? 64  TYR   A CB  1 
ATOM   455  C  CG  . TYR   A 1 58  ? 16.257 -1.728  22.343 1.00 26.86  ? 64  TYR   A CG  1 
ATOM   456  C  CD1 . TYR   A 1 58  ? 15.940 -2.816  23.152 1.00 30.66  ? 64  TYR   A CD1 1 
ATOM   457  C  CD2 . TYR   A 1 58  ? 17.086 -0.741  22.832 1.00 29.65  ? 64  TYR   A CD2 1 
ATOM   458  C  CE1 . TYR   A 1 58  ? 16.462 -2.927  24.439 1.00 32.77  ? 64  TYR   A CE1 1 
ATOM   459  C  CE2 . TYR   A 1 58  ? 17.652 -0.864  24.094 1.00 34.97  ? 64  TYR   A CE2 1 
ATOM   460  C  CZ  . TYR   A 1 58  ? 17.298 -1.933  24.911 1.00 36.89  ? 64  TYR   A CZ  1 
ATOM   461  O  OH  . TYR   A 1 58  ? 17.791 -2.024  26.189 1.00 37.40  ? 64  TYR   A OH  1 
ATOM   462  N  N   . CYS   A 1 59  ? 13.214 -0.673  23.164 1.00 31.90  ? 65  CYS   A N   1 
ATOM   463  C  CA  . CYS   A 1 59  ? 12.729 0.282   24.174 1.00 29.69  ? 65  CYS   A CA  1 
ATOM   464  C  C   . CYS   A 1 59  ? 13.680 0.187   25.358 1.00 34.65  ? 65  CYS   A C   1 
ATOM   465  O  O   . CYS   A 1 59  ? 13.523 -0.770  26.102 1.00 33.86  ? 65  CYS   A O   1 
ATOM   466  C  CB  . CYS   A 1 59  ? 11.307 -0.058  24.614 1.00 36.05  ? 65  CYS   A CB  1 
ATOM   467  S  SG  . CYS   A 1 59  ? 10.624 1.029   25.916 1.00 32.91  ? 65  CYS   A SG  1 
ATOM   468  N  N   . SER   A 1 60  ? 14.622 1.118   25.493 1.00 29.75  ? 66  SER   A N   1 
ATOM   469  C  CA  . SER   A 1 60  ? 15.653 1.054   26.551 1.00 29.35  ? 66  SER   A CA  1 
ATOM   470  C  C   . SER   A 1 60  ? 15.010 1.193   27.947 1.00 33.49  ? 66  SER   A C   1 
ATOM   471  O  O   . SER   A 1 60  ? 15.550 0.556   28.899 1.00 33.82  ? 66  SER   A O   1 
ATOM   472  C  CB  . SER   A 1 60  ? 16.765 2.027   26.376 1.00 35.18  ? 66  SER   A CB  1 
ATOM   473  O  OG  . SER   A 1 60  ? 16.426 3.320   26.795 1.00 39.95  ? 66  SER   A OG  1 
ATOM   474  N  N   . SER   A 1 61  ? 13.918 1.966   28.068 1.00 33.50  ? 67  SER   A N   1 
ATOM   475  C  CA  . SER   A 1 61  ? 13.153 2.211   29.330 1.00 31.94  ? 67  SER   A CA  1 
ATOM   476  C  C   . SER   A 1 61  ? 12.394 0.958   29.836 1.00 36.85  ? 67  SER   A C   1 
ATOM   477  O  O   . SER   A 1 61  ? 11.831 1.025   30.975 1.00 35.19  ? 67  SER   A O   1 
ATOM   478  C  CB  . SER   A 1 61  ? 12.221 3.402   29.187 1.00 29.50  ? 67  SER   A CB  1 
ATOM   479  O  OG  . SER   A 1 61  ? 11.090 3.160   28.368 1.00 30.73  ? 67  SER   A OG  1 
ATOM   480  N  N   . ARG   A 1 62  ? 12.376 -0.136  29.067 1.00 32.73  ? 68  ARG   A N   1 
ATOM   481  C  CA  . ARG   A 1 62  ? 11.777 -1.439  29.457 1.00 32.26  ? 68  ARG   A CA  1 
ATOM   482  C  C   . ARG   A 1 62  ? 12.802 -2.558  29.295 1.00 33.00  ? 68  ARG   A C   1 
ATOM   483  O  O   . ARG   A 1 62  ? 12.445 -3.690  29.571 1.00 36.94  ? 68  ARG   A O   1 
ATOM   484  C  CB  . ARG   A 1 62  ? 10.513 -1.665  28.615 1.00 37.29  ? 68  ARG   A CB  1 
ATOM   485  C  CG  . ARG   A 1 62  ? 9.364  -0.719  28.951 1.00 38.89  ? 68  ARG   A CG  1 
ATOM   486  C  CD  . ARG   A 1 62  ? 8.741  -1.030  30.306 1.00 39.32  ? 68  ARG   A CD  1 
ATOM   487  N  NE  . ARG   A 1 62  ? 7.632  -0.148  30.610 1.00 36.66  ? 68  ARG   A NE  1 
ATOM   488  C  CZ  . ARG   A 1 62  ? 7.745  1.035   31.215 1.00 38.25  ? 68  ARG   A CZ  1 
ATOM   489  N  NH1 . ARG   A 1 62  ? 8.908  1.470   31.668 1.00 38.25  ? 68  ARG   A NH1 1 
ATOM   490  N  NH2 . ARG   A 1 62  ? 6.673  1.783   31.375 1.00 37.84  ? 68  ARG   A NH2 1 
ATOM   491  N  N   . ARG   A 1 63  ? 14.000 -2.258  28.802 1.00 31.91  ? 69  ARG   A N   1 
ATOM   492  C  CA  . ARG   A 1 63  ? 14.975 -3.246  28.254 1.00 35.20  ? 69  ARG   A CA  1 
ATOM   493  C  C   . ARG   A 1 63  ? 14.250 -4.354  27.475 1.00 37.38  ? 69  ARG   A C   1 
ATOM   494  O  O   . ARG   A 1 63  ? 14.477 -5.559  27.753 1.00 37.26  ? 69  ARG   A O   1 
ATOM   495  C  CB  . ARG   A 1 63  ? 15.806 -3.871  29.393 1.00 36.43  ? 69  ARG   A CB  1 
ATOM   496  C  CG  . ARG   A 1 63  ? 16.705 -2.912  30.155 1.00 39.81  ? 69  ARG   A CG  1 
ATOM   497  C  CD  . ARG   A 1 63  ? 17.408 -3.583  31.334 1.00 47.41  ? 69  ARG   A CD  1 
ATOM   498  N  NE  . ARG   A 1 63  ? 18.164 -2.661  32.197 1.00 47.09  ? 69  ARG   A NE  1 
ATOM   499  C  CZ  . ARG   A 1 63  ? 18.008 -2.532  33.530 1.00 43.27  ? 69  ARG   A CZ  1 
ATOM   500  N  NH1 . ARG   A 1 63  ? 17.069 -3.217  34.161 1.00 47.75  ? 69  ARG   A NH1 1 
ATOM   501  N  NH2 . ARG   A 1 63  ? 18.727 -1.636  34.205 1.00 43.09  ? 69  ARG   A NH2 1 
ATOM   502  N  N   . LYS   A 1 64  ? 13.395 -3.973  26.518 0.50 35.17  ? 70  LYS   A N   1 
ATOM   503  C  CA  . LYS   A 1 64  ? 12.531 -4.925  25.772 0.50 36.38  ? 70  LYS   A CA  1 
ATOM   504  C  C   . LYS   A 1 64  ? 12.421 -4.493  24.310 0.50 33.57  ? 70  LYS   A C   1 
ATOM   505  O  O   . LYS   A 1 64  ? 12.444 -3.261  24.051 0.50 33.13  ? 70  LYS   A O   1 
ATOM   506  C  CB  . LYS   A 1 64  ? 11.132 -5.000  26.385 0.50 37.66  ? 70  LYS   A CB  1 
ATOM   507  C  CG  . LYS   A 1 64  ? 10.504 -6.389  26.367 0.50 42.24  ? 70  LYS   A CG  1 
ATOM   508  C  CD  . LYS   A 1 64  ? 8.991  -6.379  26.517 0.50 43.06  ? 70  LYS   A CD  1 
ATOM   509  C  CE  . LYS   A 1 64  ? 8.410  -7.715  26.927 0.50 42.63  ? 70  LYS   A CE  1 
ATOM   510  N  NZ  . LYS   A 1 64  ? 8.763  -8.783  25.966 0.50 43.21  ? 70  LYS   A NZ  1 
ATOM   511  N  N   . HIS   A 1 65  ? 12.308 -5.483  23.421 1.00 32.31  ? 71  HIS   A N   1 
ATOM   512  C  CA  . HIS   A 1 65  ? 12.056 -5.318  21.967 1.00 30.14  ? 71  HIS   A CA  1 
ATOM   513  C  C   . HIS   A 1 65  ? 10.573 -5.625  21.752 1.00 35.88  ? 71  HIS   A C   1 
ATOM   514  O  O   . HIS   A 1 65  ? 10.106 -6.760  22.069 1.00 33.28  ? 71  HIS   A O   1 
ATOM   515  C  CB  . HIS   A 1 65  ? 12.989 -6.269  21.162 1.00 30.33  ? 71  HIS   A CB  1 
ATOM   516  C  CG  . HIS   A 1 65  ? 14.465 -6.073  21.363 1.00 30.79  ? 71  HIS   A CG  1 
ATOM   517  N  ND1 . HIS   A 1 65  ? 15.276 -5.396  20.456 1.00 32.26  ? 71  HIS   A ND1 1 
ATOM   518  C  CD2 . HIS   A 1 65  ? 15.280 -6.399  22.391 1.00 29.11  ? 71  HIS   A CD2 1 
ATOM   519  C  CE1 . HIS   A 1 65  ? 16.513 -5.332  20.910 1.00 31.11  ? 71  HIS   A CE1 1 
ATOM   520  N  NE2 . HIS   A 1 65  ? 16.525 -5.924  22.137 1.00 32.46  ? 71  HIS   A NE2 1 
ATOM   521  N  N   . TYR   A 1 66  ? 9.818  -4.681  21.209 1.00 27.85  ? 72  TYR   A N   1 
ATOM   522  C  CA  . TYR   A 1 66  ? 8.383  -4.855  21.037 1.00 28.28  ? 72  TYR   A CA  1 
ATOM   523  C  C   . TYR   A 1 66  ? 8.073  -4.957  19.556 1.00 30.47  ? 72  TYR   A C   1 
ATOM   524  O  O   . TYR   A 1 66  ? 8.470  -4.053  18.821 1.00 30.43  ? 72  TYR   A O   1 
ATOM   525  C  CB  . TYR   A 1 66  ? 7.678  -3.621  21.598 1.00 32.34  ? 72  TYR   A CB  1 
ATOM   526  C  CG  . TYR   A 1 66  ? 7.729  -3.525  23.105 1.00 32.50  ? 72  TYR   A CG  1 
ATOM   527  C  CD1 . TYR   A 1 66  ? 6.925  -4.332  23.898 1.00 39.47  ? 72  TYR   A CD1 1 
ATOM   528  C  CD2 . TYR   A 1 66  ? 8.492  -2.554  23.722 1.00 31.98  ? 72  TYR   A CD2 1 
ATOM   529  C  CE1 . TYR   A 1 66  ? 6.936  -4.216  25.285 1.00 42.09  ? 72  TYR   A CE1 1 
ATOM   530  C  CE2 . TYR   A 1 66  ? 8.498  -2.401  25.100 1.00 36.36  ? 72  TYR   A CE2 1 
ATOM   531  C  CZ  . TYR   A 1 66  ? 7.710  -3.232  25.883 1.00 40.71  ? 72  TYR   A CZ  1 
ATOM   532  O  OH  . TYR   A 1 66  ? 7.731  -3.066  27.245 1.00 42.70  ? 72  TYR   A OH  1 
ATOM   533  N  N   . PRO   A 1 67  ? 7.238  -5.925  19.156 1.00 29.68  ? 73  PRO   A N   1 
ATOM   534  C  CA  . PRO   A 1 67  ? 6.697  -5.992  17.786 1.00 32.58  ? 73  PRO   A CA  1 
ATOM   535  C  C   . PRO   A 1 67  ? 5.607  -4.924  17.670 1.00 34.89  ? 73  PRO   A C   1 
ATOM   536  O  O   . PRO   A 1 67  ? 4.867  -4.757  18.604 1.00 35.07  ? 73  PRO   A O   1 
ATOM   537  C  CB  . PRO   A 1 67  ? 6.142  -7.438  17.652 1.00 35.67  ? 73  PRO   A CB  1 
ATOM   538  C  CG  . PRO   A 1 67  ? 5.876  -7.856  19.079 1.00 37.76  ? 73  PRO   A CG  1 
ATOM   539  C  CD  . PRO   A 1 67  ? 6.812  -7.071  19.986 1.00 33.84  ? 73  PRO   A CD  1 
ATOM   540  N  N   . VAL   A 1 68  ? 5.566  -4.188  16.561 1.00 29.74  ? 74  VAL   A N   1 
ATOM   541  C  CA  . VAL   A 1 68  ? 4.641  -3.038  16.370 1.00 29.53  ? 74  VAL   A CA  1 
ATOM   542  C  C   . VAL   A 1 68  ? 4.208  -2.973  14.918 1.00 29.11  ? 74  VAL   A C   1 
ATOM   543  O  O   . VAL   A 1 68  ? 5.003  -3.390  14.000 1.00 29.68  ? 74  VAL   A O   1 
ATOM   544  C  CB  . VAL   A 1 68  ? 5.296  -1.713  16.784 1.00 31.44  ? 74  VAL   A CB  1 
ATOM   545  C  CG1 . VAL   A 1 68  ? 5.339  -1.591  18.301 1.00 35.38  ? 74  VAL   A CG1 1 
ATOM   546  C  CG2 . VAL   A 1 68  ? 6.658  -1.538  16.146 1.00 31.84  ? 74  VAL   A CG2 1 
ATOM   547  N  N   . SER   A 1 69  ? 3.006  -2.445  14.719 1.00 29.19  ? 75  SER   A N   1 
ATOM   548  C  CA  . SER   A 1 69  ? 2.518  -1.893  13.432 1.00 32.08  ? 75  SER   A CA  1 
ATOM   549  C  C   . SER   A 1 69  ? 2.817  -0.388  13.468 1.00 32.73  ? 75  SER   A C   1 
ATOM   550  O  O   . SER   A 1 69  ? 2.593  0.231   14.514 1.00 30.70  ? 75  SER   A O   1 
ATOM   551  C  CB  . SER   A 1 69  ? 1.028  -2.163  13.260 1.00 35.02  ? 75  SER   A CB  1 
ATOM   552  O  OG  . SER   A 1 69  ? 0.806  -3.560  13.174 1.00 41.78  ? 75  SER   A OG  1 
ATOM   553  N  N   . PHE   A 1 70  ? 3.259  0.214   12.363 1.00 30.82  ? 76  PHE   A N   1 
ATOM   554  C  CA  . PHE   A 1 70  ? 3.540  1.671   12.327 1.00 26.73  ? 76  PHE   A CA  1 
ATOM   555  C  C   . PHE   A 1 70  ? 2.984  2.271   11.038 1.00 31.61  ? 76  PHE   A C   1 
ATOM   556  O  O   . PHE   A 1 70  ? 2.886  1.588   10.023 1.00 30.57  ? 76  PHE   A O   1 
ATOM   557  C  CB  . PHE   A 1 70  ? 5.030  1.943   12.553 1.00 28.40  ? 76  PHE   A CB  1 
ATOM   558  C  CG  . PHE   A 1 70  ? 5.970  1.185   11.656 1.00 28.87  ? 76  PHE   A CG  1 
ATOM   559  C  CD1 . PHE   A 1 70  ? 6.400  -0.103  11.972 1.00 25.99  ? 76  PHE   A CD1 1 
ATOM   560  C  CD2 . PHE   A 1 70  ? 6.308  1.725   10.419 1.00 29.05  ? 76  PHE   A CD2 1 
ATOM   561  C  CE1 . PHE   A 1 70  ? 7.270  -0.770  11.135 1.00 30.10  ? 76  PHE   A CE1 1 
ATOM   562  C  CE2 . PHE   A 1 70  ? 7.186  1.049   9.587  1.00 30.12  ? 76  PHE   A CE2 1 
ATOM   563  C  CZ  . PHE   A 1 70  ? 7.619  -0.217  9.906  1.00 26.98  ? 76  PHE   A CZ  1 
ATOM   564  N  N   . SER   A 1 71  ? 2.641  3.560   11.097 0.51 31.79  ? 77  SER   A N   1 
ATOM   565  C  CA  . SER   A 1 71  ? 2.138  4.336   9.939  0.51 32.59  ? 77  SER   A CA  1 
ATOM   566  C  C   . SER   A 1 71  ? 3.281  4.529   8.936  0.51 32.28  ? 77  SER   A C   1 
ATOM   567  O  O   . SER   A 1 71  ? 4.462  4.361   9.318  0.51 31.74  ? 77  SER   A O   1 
ATOM   568  C  CB  . SER   A 1 71  ? 1.537  5.649   10.387 0.51 32.65  ? 77  SER   A CB  1 
ATOM   569  O  OG  . SER   A 1 71  ? 2.511  6.477   10.999 0.51 32.00  ? 77  SER   A OG  1 
ATOM   570  N  N   . LYS   A 1 72  ? 2.939  4.831   7.685  0.51 33.11  ? 78  LYS   A N   1 
ATOM   571  C  CA  . LYS   A 1 72  ? 3.917  5.247   6.650  0.51 35.34  ? 78  LYS   A CA  1 
ATOM   572  C  C   . LYS   A 1 72  ? 4.486  6.616   7.026  0.51 34.88  ? 78  LYS   A C   1 
ATOM   573  O  O   . LYS   A 1 72  ? 3.828  7.406   7.695  0.51 35.34  ? 78  LYS   A O   1 
ATOM   574  C  CB  . LYS   A 1 72  ? 3.251  5.230   5.267  0.51 36.91  ? 78  LYS   A CB  1 
ATOM   575  C  CG  . LYS   A 1 72  ? 2.907  3.827   4.780  0.51 39.73  ? 78  LYS   A CG  1 
ATOM   576  C  CD  . LYS   A 1 72  ? 2.445  3.747   3.334  0.51 44.29  ? 78  LYS   A CD  1 
ATOM   577  C  CE  . LYS   A 1 72  ? 2.471  2.327   2.807  0.51 47.18  ? 78  LYS   A CE  1 
ATOM   578  N  NZ  . LYS   A 1 72  ? 1.750  2.199   1.517  0.51 52.50  ? 78  LYS   A NZ  1 
ATOM   579  N  N   . PRO   A 1 73  ? 5.734  6.938   6.622  1.00 33.60  ? 79  PRO   A N   1 
ATOM   580  C  CA  . PRO   A 1 73  ? 6.345  8.226   6.995  1.00 36.48  ? 79  PRO   A CA  1 
ATOM   581  C  C   . PRO   A 1 73  ? 5.514  9.412   6.486  1.00 35.58  ? 79  PRO   A C   1 
ATOM   582  O  O   . PRO   A 1 73  ? 5.107  9.441   5.296  1.00 35.57  ? 79  PRO   A O   1 
ATOM   583  C  CB  . PRO   A 1 73  ? 7.737  8.189   6.336  1.00 37.90  ? 79  PRO   A CB  1 
ATOM   584  C  CG  . PRO   A 1 73  ? 7.970  6.712   6.000  1.00 42.78  ? 79  PRO   A CG  1 
ATOM   585  C  CD  . PRO   A 1 73  ? 6.606  6.074   5.816  1.00 36.16  ? 79  PRO   A CD  1 
ATOM   586  N  N   . SER   A 1 74  ? 5.252  10.376  7.366  0.51 35.41  ? 80  SER   A N   1 
ATOM   587  C  CA  . SER   A 1 74  ? 4.348  11.523  7.082  0.51 36.52  ? 80  SER   A CA  1 
ATOM   588  C  C   . SER   A 1 74  ? 4.730  12.750  7.912  0.51 36.96  ? 80  SER   A C   1 
ATOM   589  O  O   . SER   A 1 74  ? 5.550  12.625  8.852  0.51 34.93  ? 80  SER   A O   1 
ATOM   590  C  CB  . SER   A 1 74  ? 2.913  11.139  7.342  0.51 38.18  ? 80  SER   A CB  1 
ATOM   591  O  OG  . SER   A 1 74  ? 2.708  10.897  8.725  0.51 35.37  ? 80  SER   A OG  1 
ATOM   592  N  N   . LEU   A 1 75  ? 4.118  13.887  7.575  0.51 34.25  ? 81  LEU   A N   1 
ATOM   593  C  CA  . LEU   A 1 75  ? 4.190  15.149  8.347  0.51 36.02  ? 81  LEU   A CA  1 
ATOM   594  C  C   . LEU   A 1 75  ? 3.210  15.013  9.521  0.51 36.26  ? 81  LEU   A C   1 
ATOM   595  O  O   . LEU   A 1 75  ? 2.015  14.738  9.267  0.51 33.45  ? 81  LEU   A O   1 
ATOM   596  C  CB  . LEU   A 1 75  ? 3.852  16.313  7.406  0.51 37.37  ? 81  LEU   A CB  1 
ATOM   597  C  CG  . LEU   A 1 75  ? 4.371  17.689  7.821  0.51 37.69  ? 81  LEU   A CG  1 
ATOM   598  C  CD1 . LEU   A 1 75  ? 5.887  17.728  7.834  0.51 37.60  ? 81  LEU   A CD1 1 
ATOM   599  C  CD2 . LEU   A 1 75  ? 3.829  18.781  6.903  0.51 41.03  ? 81  LEU   A CD2 1 
ATOM   600  N  N   . ILE   A 1 76  ? 3.723  15.113  10.752 0.51 36.03  ? 82  ILE   A N   1 
ATOM   601  C  CA  . ILE   A 1 76  ? 2.977  14.878  12.028 0.51 39.44  ? 82  ILE   A CA  1 
ATOM   602  C  C   . ILE   A 1 76  ? 3.320  16.016  12.993 0.51 40.21  ? 82  ILE   A C   1 
ATOM   603  O  O   . ILE   A 1 76  ? 4.523  16.285  13.181 0.51 39.47  ? 82  ILE   A O   1 
ATOM   604  C  CB  . ILE   A 1 76  ? 3.344  13.514  12.653 0.51 41.04  ? 82  ILE   A CB  1 
ATOM   605  C  CG1 . ILE   A 1 76  ? 3.021  12.333  11.733 0.51 41.77  ? 82  ILE   A CG1 1 
ATOM   606  C  CG2 . ILE   A 1 76  ? 2.697  13.359  14.023 0.51 43.00  ? 82  ILE   A CG2 1 
ATOM   607  C  CD1 . ILE   A 1 76  ? 1.549  12.049  11.578 0.51 45.50  ? 82  ILE   A CD1 1 
ATOM   608  N  N   . PHE   A 1 77  ? 2.315  16.663  13.584 0.51 40.68  ? 83  PHE   A N   1 
ATOM   609  C  CA  . PHE   A 1 77  ? 2.539  17.722  14.601 0.51 41.20  ? 83  PHE   A CA  1 
ATOM   610  C  C   . PHE   A 1 77  ? 3.088  17.064  15.871 0.51 40.28  ? 83  PHE   A C   1 
ATOM   611  O  O   . PHE   A 1 77  ? 2.509  16.068  16.341 0.51 42.16  ? 83  PHE   A O   1 
ATOM   612  C  CB  . PHE   A 1 77  ? 1.278  18.548  14.871 0.51 42.90  ? 83  PHE   A CB  1 
ATOM   613  C  CG  . PHE   A 1 77  ? 1.575  19.879  15.518 0.51 42.30  ? 83  PHE   A CG  1 
ATOM   614  C  CD1 . PHE   A 1 77  ? 2.267  20.865  14.825 0.51 42.02  ? 83  PHE   A CD1 1 
ATOM   615  C  CD2 . PHE   A 1 77  ? 1.205  20.130  16.830 0.51 42.71  ? 83  PHE   A CD2 1 
ATOM   616  C  CE1 . PHE   A 1 77  ? 2.559  22.083  15.424 0.51 42.86  ? 83  PHE   A CE1 1 
ATOM   617  C  CE2 . PHE   A 1 77  ? 1.496  21.346  17.427 0.51 42.00  ? 83  PHE   A CE2 1 
ATOM   618  C  CZ  . PHE   A 1 77  ? 2.175  22.319  16.726 0.51 44.91  ? 83  PHE   A CZ  1 
ATOM   619  N  N   . VAL   A 1 78  ? 4.195  17.604  16.389 1.00 39.12  ? 84  VAL   A N   1 
ATOM   620  C  CA  . VAL   A 1 78  ? 4.891  17.076  17.594 1.00 38.26  ? 84  VAL   A CA  1 
ATOM   621  C  C   . VAL   A 1 78  ? 4.899  18.211  18.624 1.00 40.77  ? 84  VAL   A C   1 
ATOM   622  O  O   . VAL   A 1 78  ? 5.332  19.313  18.310 1.00 38.54  ? 84  VAL   A O   1 
ATOM   623  C  CB  . VAL   A 1 78  ? 6.296  16.583  17.184 1.00 36.80  ? 84  VAL   A CB  1 
ATOM   624  C  CG1 . VAL   A 1 78  ? 7.159  16.208  18.384 1.00 37.83  ? 84  VAL   A CG1 1 
ATOM   625  C  CG2 . VAL   A 1 78  ? 6.176  15.402  16.239 1.00 36.39  ? 84  VAL   A CG2 1 
ATOM   626  N  N   . GLU   A 1 79  ? 4.398  17.917  19.823 0.51 39.24  ? 85  GLU   A N   1 
ATOM   627  C  CA  . GLU   A 1 79  ? 4.367  18.847  20.981 0.51 40.43  ? 85  GLU   A CA  1 
ATOM   628  C  C   . GLU   A 1 79  ? 5.760  19.451  21.191 0.51 36.23  ? 85  GLU   A C   1 
ATOM   629  O  O   . GLU   A 1 79  ? 6.756  18.725  20.997 0.51 35.63  ? 85  GLU   A O   1 
ATOM   630  C  CB  . GLU   A 1 79  ? 3.926  18.105  22.249 0.51 43.08  ? 85  GLU   A CB  1 
ATOM   631  C  CG  . GLU   A 1 79  ? 2.421  17.944  22.385 0.51 47.22  ? 85  GLU   A CG  1 
ATOM   632  C  CD  . GLU   A 1 79  ? 1.716  19.066  23.130 0.51 50.99  ? 85  GLU   A CD  1 
ATOM   633  O  OE1 . GLU   A 1 79  ? 2.148  19.388  24.264 0.51 56.36  ? 85  GLU   A OE1 1 
ATOM   634  O  OE2 . GLU   A 1 79  ? 0.727  19.607  22.586 0.51 49.53  ? 85  GLU   A OE2 1 
ATOM   635  N  N   . ALA   A 1 80  ? 5.829  20.719  21.605 0.51 33.78  ? 86  ALA   A N   1 
ATOM   636  C  CA  . ALA   A 1 80  ? 7.068  21.354  22.112 0.51 33.15  ? 86  ALA   A CA  1 
ATOM   637  C  C   . ALA   A 1 80  ? 7.770  20.379  23.067 0.51 31.31  ? 86  ALA   A C   1 
ATOM   638  O  O   . ALA   A 1 80  ? 7.057  19.663  23.819 0.51 31.92  ? 86  ALA   A O   1 
ATOM   639  C  CB  . ALA   A 1 80  ? 6.746  22.656  22.802 0.51 33.62  ? 86  ALA   A CB  1 
ATOM   640  N  N   . SER   A 1 81  ? 9.100  20.329  23.004 0.51 29.73  ? 87  SER   A N   1 
ATOM   641  C  CA  . SER   A 1 81  ? 10.004 19.639  23.967 0.51 31.71  ? 87  SER   A CA  1 
ATOM   642  C  C   . SER   A 1 81  ? 11.123 20.589  24.402 0.51 31.29  ? 87  SER   A C   1 
ATOM   643  O  O   . SER   A 1 81  ? 11.094 21.758  23.987 0.51 30.75  ? 87  SER   A O   1 
ATOM   644  C  CB  . SER   A 1 81  ? 10.589 18.404  23.353 0.51 30.67  ? 87  SER   A CB  1 
ATOM   645  O  OG  . SER   A 1 81  ? 11.477 18.755  22.296 0.51 29.52  ? 87  SER   A OG  1 
ATOM   646  N  N   . GLU   A 1 82  ? 12.105 20.083  25.158 0.51 34.56  ? 88  GLU   A N   1 
ATOM   647  C  CA  . GLU   A 1 82  ? 13.335 20.842  25.516 0.51 35.67  ? 88  GLU   A CA  1 
ATOM   648  C  C   . GLU   A 1 82  ? 14.248 20.989  24.285 0.51 32.78  ? 88  GLU   A C   1 
ATOM   649  O  O   . GLU   A 1 82  ? 15.054 21.934  24.286 0.51 30.04  ? 88  GLU   A O   1 
ATOM   650  C  CB  . GLU   A 1 82  ? 14.048 20.220  26.723 0.51 40.22  ? 88  GLU   A CB  1 
ATOM   651  C  CG  . GLU   A 1 82  ? 14.659 18.845  26.491 0.51 41.72  ? 88  GLU   A CG  1 
ATOM   652  C  CD  . GLU   A 1 82  ? 15.695 18.441  27.537 0.51 45.43  ? 88  GLU   A CD  1 
ATOM   653  O  OE1 . GLU   A 1 82  ? 16.704 19.168  27.683 0.51 45.21  ? 88  GLU   A OE1 1 
ATOM   654  O  OE2 . GLU   A 1 82  ? 15.496 17.406  28.207 0.51 44.54  ? 88  GLU   A OE2 1 
ATOM   655  N  N   . TYR   A 1 83  ? 14.092 20.153  23.244 0.51 30.93  ? 89  TYR   A N   1 
ATOM   656  C  CA  . TYR   A 1 83  ? 14.954 20.144  22.024 0.51 29.77  ? 89  TYR   A CA  1 
ATOM   657  C  C   . TYR   A 1 83  ? 14.346 20.956  20.859 0.51 28.24  ? 89  TYR   A C   1 
ATOM   658  O  O   . TYR   A 1 83  ? 15.101 21.527  20.067 0.51 25.62  ? 89  TYR   A O   1 
ATOM   659  C  CB  . TYR   A 1 83  ? 15.237 18.694  21.617 0.51 31.56  ? 89  TYR   A CB  1 
ATOM   660  C  CG  . TYR   A 1 83  ? 15.784 17.847  22.740 0.51 33.53  ? 89  TYR   A CG  1 
ATOM   661  C  CD1 . TYR   A 1 83  ? 17.103 17.965  23.140 0.51 34.35  ? 89  TYR   A CD1 1 
ATOM   662  C  CD2 . TYR   A 1 83  ? 14.967 16.977  23.454 0.51 36.07  ? 89  TYR   A CD2 1 
ATOM   663  C  CE1 . TYR   A 1 83  ? 17.612 17.208  24.184 0.51 36.72  ? 89  TYR   A CE1 1 
ATOM   664  C  CE2 . TYR   A 1 83  ? 15.460 16.217  24.504 0.51 37.20  ? 89  TYR   A CE2 1 
ATOM   665  C  CZ  . TYR   A 1 83  ? 16.790 16.330  24.868 0.51 37.08  ? 89  TYR   A CZ  1 
ATOM   666  O  OH  . TYR   A 1 83  ? 17.294 15.599  25.906 0.51 40.72  ? 89  TYR   A OH  1 
ATOM   667  N  N   . TYR   A 1 84  ? 13.028 20.978  20.704 0.51 27.73  ? 90  TYR   A N   1 
ATOM   668  C  CA  . TYR   A 1 84  ? 12.337 21.695  19.599 0.51 27.38  ? 90  TYR   A CA  1 
ATOM   669  C  C   . TYR   A 1 84  ? 11.082 22.361  20.145 0.51 28.61  ? 90  TYR   A C   1 
ATOM   670  O  O   . TYR   A 1 84  ? 10.481 21.853  21.093 0.51 31.42  ? 90  TYR   A O   1 
ATOM   671  C  CB  . TYR   A 1 84  ? 11.943 20.767  18.444 0.51 24.85  ? 90  TYR   A CB  1 
ATOM   672  C  CG  . TYR   A 1 84  ? 13.044 19.945  17.821 0.51 24.96  ? 90  TYR   A CG  1 
ATOM   673  C  CD1 . TYR   A 1 84  ? 13.881 20.474  16.849 0.51 23.61  ? 90  TYR   A CD1 1 
ATOM   674  C  CD2 . TYR   A 1 84  ? 13.229 18.616  18.182 0.51 24.11  ? 90  TYR   A CD2 1 
ATOM   675  C  CE1 . TYR   A 1 84  ? 14.886 19.717  16.267 0.51 22.82  ? 90  TYR   A CE1 1 
ATOM   676  C  CE2 . TYR   A 1 84  ? 14.228 17.846  17.616 0.51 22.72  ? 90  TYR   A CE2 1 
ATOM   677  C  CZ  . TYR   A 1 84  ? 15.057 18.392  16.649 0.51 24.45  ? 90  TYR   A CZ  1 
ATOM   678  O  OH  . TYR   A 1 84  ? 16.043 17.633  16.086 0.51 23.08  ? 90  TYR   A OH  1 
ATOM   679  N  N   . PRO   A 1 85  ? 10.652 23.513  19.570 0.51 28.59  ? 91  PRO   A N   1 
ATOM   680  C  CA  . PRO   A 1 85  ? 9.310  24.054  19.810 0.51 27.54  ? 91  PRO   A CA  1 
ATOM   681  C  C   . PRO   A 1 85  ? 8.284  23.160  19.109 0.51 27.66  ? 91  PRO   A C   1 
ATOM   682  O  O   . PRO   A 1 85  ? 8.730  22.283  18.362 0.51 24.89  ? 91  PRO   A O   1 
ATOM   683  C  CB  . PRO   A 1 85  ? 9.340  25.446  19.163 0.51 28.13  ? 91  PRO   A CB  1 
ATOM   684  C  CG  . PRO   A 1 85  ? 10.390 25.323  18.080 0.51 28.20  ? 91  PRO   A CG  1 
ATOM   685  C  CD  . PRO   A 1 85  ? 11.419 24.352  18.638 0.51 28.88  ? 91  PRO   A CD  1 
ATOM   686  N  N   . ALA   A 1 86  ? 6.980  23.388  19.343 0.51 27.88  ? 92  ALA   A N   1 
ATOM   687  C  CA  . ALA   A 1 86  ? 5.882  22.621  18.702 0.51 29.75  ? 92  ALA   A CA  1 
ATOM   688  C  C   . ALA   A 1 86  ? 5.960  22.839  17.183 0.51 29.69  ? 92  ALA   A C   1 
ATOM   689  O  O   . ALA   A 1 86  ? 6.018  23.995  16.750 0.51 28.26  ? 92  ALA   A O   1 
ATOM   690  C  CB  . ALA   A 1 86  ? 4.538  23.024  19.260 0.51 30.56  ? 92  ALA   A CB  1 
ATOM   691  N  N   . ARG   A 1 87  ? 6.020  21.767  16.391 0.51 29.72  ? 93  ARG   A N   1 
ATOM   692  C  CA  . ARG   A 1 87  ? 6.251  21.877  14.924 0.51 29.91  ? 93  ARG   A CA  1 
ATOM   693  C  C   . ARG   A 1 87  ? 5.766  20.609  14.218 0.51 32.31  ? 93  ARG   A C   1 
ATOM   694  O  O   . ARG   A 1 87  ? 5.538  19.597  14.907 0.51 31.05  ? 93  ARG   A O   1 
ATOM   695  C  CB  . ARG   A 1 87  ? 7.744  22.063  14.633 0.51 33.24  ? 93  ARG   A CB  1 
ATOM   696  C  CG  . ARG   A 1 87  ? 8.534  20.761  14.670 0.51 32.50  ? 93  ARG   A CG  1 
ATOM   697  C  CD  . ARG   A 1 87  ? 9.998  20.939  15.018 0.51 32.16  ? 93  ARG   A CD  1 
ATOM   698  N  NE  . ARG   A 1 87  ? 10.854 19.851  14.568 0.51 29.00  ? 93  ARG   A NE  1 
ATOM   699  C  CZ  . ARG   A 1 87  ? 10.919 18.622  15.085 0.51 29.78  ? 93  ARG   A CZ  1 
ATOM   700  N  NH1 . ARG   A 1 87  ? 10.143 18.250  16.094 0.51 29.78  ? 93  ARG   A NH1 1 
ATOM   701  N  NH2 . ARG   A 1 87  ? 11.771 17.749  14.576 0.51 27.36  ? 93  ARG   A NH2 1 
ATOM   702  N  N   . TYR   A 1 88  ? 5.652  20.654  12.886 0.51 31.49  ? 94  TYR   A N   1 
ATOM   703  C  CA  . TYR   A 1 88  ? 5.407  19.459  12.046 0.51 35.17  ? 94  TYR   A CA  1 
ATOM   704  C  C   . TYR   A 1 88  ? 6.754  18.802  11.741 0.51 35.31  ? 94  TYR   A C   1 
ATOM   705  O  O   . TYR   A 1 88  ? 7.611  19.423  11.082 0.51 33.70  ? 94  TYR   A O   1 
ATOM   706  C  CB  . TYR   A 1 88  ? 4.614  19.815  10.788 0.51 37.43  ? 94  TYR   A CB  1 
ATOM   707  C  CG  . TYR   A 1 88  ? 3.199  20.219  11.105 0.51 40.76  ? 94  TYR   A CG  1 
ATOM   708  C  CD1 . TYR   A 1 88  ? 2.194  19.273  11.214 0.51 38.30  ? 94  TYR   A CD1 1 
ATOM   709  C  CD2 . TYR   A 1 88  ? 2.881  21.544  11.364 0.51 42.51  ? 94  TYR   A CD2 1 
ATOM   710  C  CE1 . TYR   A 1 88  ? 0.895  19.638  11.525 0.51 40.09  ? 94  TYR   A CE1 1 
ATOM   711  C  CE2 . TYR   A 1 88  ? 1.586  21.926  11.679 0.51 42.48  ? 94  TYR   A CE2 1 
ATOM   712  C  CZ  . TYR   A 1 88  ? 0.590  20.968  11.760 0.51 41.07  ? 94  TYR   A CZ  1 
ATOM   713  O  OH  . TYR   A 1 88  ? -0.686 21.323  12.078 0.51 43.27  ? 94  TYR   A OH  1 
ATOM   714  N  N   . GLN   A 1 89  ? 6.914  17.570  12.222 1.00 37.60  ? 95  GLN   A N   1 
ATOM   715  C  CA  . GLN   A 1 89  ? 8.118  16.747  11.975 1.00 37.56  ? 95  GLN   A CA  1 
ATOM   716  C  C   . GLN   A 1 89  ? 7.802  15.946  10.722 1.00 33.43  ? 95  GLN   A C   1 
ATOM   717  O  O   . GLN   A 1 89  ? 6.712  15.296  10.683 1.00 30.31  ? 95  GLN   A O   1 
ATOM   718  C  CB  . GLN   A 1 89  ? 8.430  15.849  13.183 1.00 37.28  ? 95  GLN   A CB  1 
ATOM   719  C  CG  . GLN   A 1 89  ? 9.805  15.168  13.060 1.00 38.48  ? 95  GLN   A CG  1 
ATOM   720  C  CD  . GLN   A 1 89  ? 10.414 14.574  14.317 1.00 33.95  ? 95  GLN   A CD  1 
ATOM   721  O  OE1 . GLN   A 1 89  ? 10.426 15.176  15.374 1.00 36.23  ? 95  GLN   A OE1 1 
ATOM   722  N  NE2 . GLN   A 1 89  ? 11.010 13.400  14.193 1.00 36.05  ? 95  GLN   A NE2 1 
ATOM   723  N  N   . SER   A 1 90  ? 8.702  15.953  9.740  1.00 33.03  ? 96  SER   A N   1 
ATOM   724  C  CA  . SER   A 1 90  ? 8.476  15.213  8.493  1.00 33.24  ? 96  SER   A CA  1 
ATOM   725  C  C   . SER   A 1 90  ? 9.079  13.802  8.612  1.00 29.74  ? 96  SER   A C   1 
ATOM   726  O  O   . SER   A 1 90  ? 9.950  13.565  9.487  1.00 29.81  ? 96  SER   A O   1 
ATOM   727  C  CB  . SER   A 1 90  ? 9.032  16.024  7.334  1.00 35.07  ? 96  SER   A CB  1 
ATOM   728  O  OG  . SER   A 1 90  ? 10.451 16.074  7.420  1.00 33.57  ? 96  SER   A OG  1 
ATOM   729  N  N   . HIS   A 1 91  ? 8.669  12.911  7.724  1.00 29.00  ? 97  HIS   A N   1 
ATOM   730  C  CA  . HIS   A 1 91  ? 9.216  11.535  7.533  1.00 29.18  ? 97  HIS   A CA  1 
ATOM   731  C  C   . HIS   A 1 91  ? 9.036  10.746  8.865  1.00 33.02  ? 97  HIS   A C   1 
ATOM   732  O  O   . HIS   A 1 91  ? 9.921  9.993   9.209  1.00 29.70  ? 97  HIS   A O   1 
ATOM   733  C  CB  . HIS   A 1 91  ? 10.662 11.649  7.022  1.00 33.29  ? 97  HIS   A CB  1 
ATOM   734  C  CG  . HIS   A 1 91  ? 10.809 12.265  5.647  1.00 33.03  ? 97  HIS   A CG  1 
ATOM   735  N  ND1 . HIS   A 1 91  ? 10.779 11.504  4.505  1.00 35.57  ? 97  HIS   A ND1 1 
ATOM   736  C  CD2 . HIS   A 1 91  ? 10.937 13.556  5.233  1.00 34.84  ? 97  HIS   A CD2 1 
ATOM   737  C  CE1 . HIS   A 1 91  ? 10.914 12.294  3.445  1.00 36.98  ? 97  HIS   A CE1 1 
ATOM   738  N  NE2 . HIS   A 1 91  ? 10.975 13.562  3.863  1.00 31.65  ? 97  HIS   A NE2 1 
ATOM   739  N  N   . LEU   A 1 92  ? 7.961  10.964  9.604  1.00 32.67  ? 98  LEU   A N   1 
ATOM   740  C  CA  . LEU   A 1 92  ? 7.773  10.371  10.950 1.00 32.56  ? 98  LEU   A CA  1 
ATOM   741  C  C   . LEU   A 1 92  ? 6.694  9.264   10.883 1.00 33.91  ? 98  LEU   A C   1 
ATOM   742  O  O   . LEU   A 1 92  ? 5.619  9.461   10.228 1.00 30.37  ? 98  LEU   A O   1 
ATOM   743  C  CB  . LEU   A 1 92  ? 7.410  11.471  11.943 1.00 33.85  ? 98  LEU   A CB  1 
ATOM   744  C  CG  . LEU   A 1 92  ? 7.296  11.035  13.403 1.00 32.31  ? 98  LEU   A CG  1 
ATOM   745  C  CD1 . LEU   A 1 92  ? 8.676  10.714  13.914 1.00 31.84  ? 98  LEU   A CD1 1 
ATOM   746  C  CD2 . LEU   A 1 92  ? 6.644  12.127  14.251 1.00 35.94  ? 98  LEU   A CD2 1 
ATOM   747  N  N   . MET   A 1 93  ? 6.986  8.132   11.531 1.00 29.14  ? 99  MET   A N   1 
ATOM   748  C  CA  . MET   A 1 93  ? 6.093  6.946   11.590 1.00 28.48  ? 99  MET   A CA  1 
ATOM   749  C  C   . MET   A 1 93  ? 5.628  6.756   13.033 1.00 30.14  ? 99  MET   A C   1 
ATOM   750  O  O   . MET   A 1 93  ? 6.534  6.851   13.875 1.00 31.82  ? 99  MET   A O   1 
ATOM   751  C  CB  . MET   A 1 93  ? 6.894  5.729   11.140 1.00 28.64  ? 99  MET   A CB  1 
ATOM   752  C  CG  . MET   A 1 93  ? 7.398  5.886   9.674  1.00 28.76  ? 99  MET   A CG  1 
ATOM   753  S  SD  . MET   A 1 93  ? 8.467  4.558   9.175  1.00 31.13  ? 99  MET   A SD  1 
ATOM   754  C  CE  . MET   A 1 93  ? 9.881  4.807   10.236 1.00 31.59  ? 99  MET   A CE  1 
ATOM   755  N  N   . LEU   A 1 94  ? 4.324  6.595   13.309 1.00 30.32  ? 100 LEU   A N   1 
ATOM   756  C  CA  . LEU   A 1 94  ? 3.797  6.362   14.706 1.00 30.54  ? 100 LEU   A CA  1 
ATOM   757  C  C   . LEU   A 1 94  ? 3.385  4.886   14.879 1.00 30.37  ? 100 LEU   A C   1 
ATOM   758  O  O   . LEU   A 1 94  ? 2.912  4.268   13.912 1.00 29.14  ? 100 LEU   A O   1 
ATOM   759  C  CB  . LEU   A 1 94  ? 2.574  7.237   14.997 1.00 33.67  ? 100 LEU   A CB  1 
ATOM   760  C  CG  . LEU   A 1 94  ? 2.817  8.743   14.987 1.00 36.40  ? 100 LEU   A CG  1 
ATOM   761  C  CD1 . LEU   A 1 94  ? 1.596  9.476   15.538 1.00 43.04  ? 100 LEU   A CD1 1 
ATOM   762  C  CD2 . LEU   A 1 94  ? 4.037  9.107   15.816 1.00 36.21  ? 100 LEU   A CD2 1 
ATOM   763  N  N   . ALA   A 1 95  ? 3.599  4.356   16.085 1.00 29.42  ? 101 ALA   A N   1 
ATOM   764  C  CA  . ALA   A 1 95  ? 3.044  3.079   16.599 1.00 28.64  ? 101 ALA   A CA  1 
ATOM   765  C  C   . ALA   A 1 95  ? 2.489  3.312   18.001 1.00 27.76  ? 101 ALA   A C   1 
ATOM   766  O  O   . ALA   A 1 95  ? 2.874  4.288   18.651 1.00 27.72  ? 101 ALA   A O   1 
ATOM   767  C  CB  . ALA   A 1 95  ? 4.081  1.985   16.681 1.00 28.83  ? 101 ALA   A CB  1 
ATOM   768  N  N   . VAL   A 1 96  ? 1.618  2.415   18.414 1.00 31.28  ? 102 VAL   A N   1 
ATOM   769  C  CA  . VAL   A 1 96  ? 1.184  2.266   19.819 1.00 28.67  ? 102 VAL   A CA  1 
ATOM   770  C  C   . VAL   A 1 96  ? 2.274  1.488   20.543 1.00 30.39  ? 102 VAL   A C   1 
ATOM   771  O  O   . VAL   A 1 96  ? 2.534  0.281   20.255 1.00 32.93  ? 102 VAL   A O   1 
ATOM   772  C  CB  . VAL   A 1 96  ? -0.192 1.585   19.874 1.00 29.59  ? 102 VAL   A CB  1 
ATOM   773  C  CG1 . VAL   A 1 96  ? -0.700 1.458   21.299 1.00 34.46  ? 102 VAL   A CG1 1 
ATOM   774  C  CG2 . VAL   A 1 96  ? -1.219 2.321   19.011 1.00 32.67  ? 102 VAL   A CG2 1 
ATOM   775  N  N   . GLY   A 1 97  ? 2.912  2.136   21.471 1.00 32.19  ? 103 GLY   A N   1 
ATOM   776  C  CA  . GLY   A 1 97  ? 3.903  1.458   22.290 1.00 34.93  ? 103 GLY   A CA  1 
ATOM   777  C  C   . GLY   A 1 97  ? 4.460  2.427   23.284 1.00 35.83  ? 103 GLY   A C   1 
ATOM   778  O  O   . GLY   A 1 97  ? 4.167  3.642   23.199 1.00 33.06  ? 103 GLY   A O   1 
ATOM   779  N  N   . HIS   A 1 98  ? 5.108  1.881   24.308 0.51 33.21  ? 104 HIS   A N   1 
ATOM   780  C  CA  . HIS   A 1 98  ? 5.689  2.684   25.405 0.51 34.06  ? 104 HIS   A CA  1 
ATOM   781  C  C   . HIS   A 1 98  ? 7.004  3.271   24.899 0.51 31.99  ? 104 HIS   A C   1 
ATOM   782  O  O   . HIS   A 1 98  ? 7.697  2.602   24.135 0.51 32.34  ? 104 HIS   A O   1 
ATOM   783  C  CB  . HIS   A 1 98  ? 5.847  1.864   26.694 0.51 35.16  ? 104 HIS   A CB  1 
ATOM   784  C  CG  . HIS   A 1 98  ? 6.570  2.635   27.744 0.51 34.95  ? 104 HIS   A CG  1 
ATOM   785  N  ND1 . HIS   A 1 98  ? 6.010  3.740   28.353 0.51 35.29  ? 104 HIS   A ND1 1 
ATOM   786  C  CD2 . HIS   A 1 98  ? 7.821  2.521   28.230 0.51 34.95  ? 104 HIS   A CD2 1 
ATOM   787  C  CE1 . HIS   A 1 98  ? 6.886  4.266   29.187 0.51 35.45  ? 104 HIS   A CE1 1 
ATOM   788  N  NE2 . HIS   A 1 98  ? 8.007  3.537   29.125 0.51 34.37  ? 104 HIS   A NE2 1 
ATOM   789  N  N   . SER   A 1 99  ? 7.292  4.510   25.281 0.51 30.09  ? 105 SER   A N   1 
ATOM   790  C  CA  . SER   A 1 99  ? 8.600  5.176   25.095 0.51 28.78  ? 105 SER   A CA  1 
ATOM   791  C  C   . SER   A 1 99  ? 8.676  6.331   26.089 0.51 29.87  ? 105 SER   A C   1 
ATOM   792  O  O   . SER   A 1 99  ? 7.584  6.793   26.516 0.51 28.37  ? 105 SER   A O   1 
ATOM   793  C  CB  . SER   A 1 99  ? 8.771  5.662   23.687 0.51 27.02  ? 105 SER   A CB  1 
ATOM   794  O  OG  . SER   A 1 99  ? 7.872  6.722   23.418 0.51 24.86  ? 105 SER   A OG  1 
ATOM   795  N  N   . GLU   A 1 100 ? 9.904  6.739   26.423 0.51 30.40  ? 106 GLU   A N   1 
ATOM   796  C  CA  . GLU   A 1 100 ? 10.250 7.959   27.194 0.51 33.61  ? 106 GLU   A CA  1 
ATOM   797  C  C   . GLU   A 1 100 ? 11.314 8.719   26.412 0.51 33.00  ? 106 GLU   A C   1 
ATOM   798  O  O   . GLU   A 1 100 ? 11.938 8.148   25.523 0.51 37.20  ? 106 GLU   A O   1 
ATOM   799  C  CB  . GLU   A 1 100 ? 10.693 7.548   28.598 0.51 34.40  ? 106 GLU   A CB  1 
ATOM   800  C  CG  . GLU   A 1 100 ? 9.580  6.863   29.373 0.51 36.47  ? 106 GLU   A CG  1 
ATOM   801  C  CD  . GLU   A 1 100 ? 10.008 6.093   30.614 0.51 36.94  ? 106 GLU   A CD  1 
ATOM   802  O  OE1 . GLU   A 1 100 ? 11.051 6.443   31.205 0.51 37.22  ? 106 GLU   A OE1 1 
ATOM   803  O  OE2 . GLU   A 1 100 ? 9.298  5.141   30.975 0.51 36.43  ? 106 GLU   A OE2 1 
ATOM   804  N  N   . PRO   A 1 101 ? 11.547 10.025  26.690 0.51 36.08  ? 107 PRO   A N   1 
ATOM   805  C  CA  . PRO   A 1 101 ? 12.530 10.799  25.932 0.51 38.11  ? 107 PRO   A CA  1 
ATOM   806  C  C   . PRO   A 1 101 ? 13.877 10.086  25.717 0.51 39.07  ? 107 PRO   A C   1 
ATOM   807  O  O   . PRO   A 1 101 ? 14.352 10.060  24.583 0.51 39.33  ? 107 PRO   A O   1 
ATOM   808  C  CB  . PRO   A 1 101 ? 12.692 12.076  26.769 0.51 36.98  ? 107 PRO   A CB  1 
ATOM   809  C  CG  . PRO   A 1 101 ? 11.344 12.245  27.439 0.51 38.31  ? 107 PRO   A CG  1 
ATOM   810  C  CD  . PRO   A 1 101 ? 10.850 10.834  27.707 0.51 35.53  ? 107 PRO   A CD  1 
ATOM   811  N  N   . GLY   A 1 102 ? 14.453 9.508   26.777 0.51 37.75  ? 108 GLY   A N   1 
ATOM   812  C  CA  . GLY   A 1 102 ? 15.801 8.906   26.739 0.51 35.71  ? 108 GLY   A CA  1 
ATOM   813  C  C   . GLY   A 1 102 ? 15.863 7.588   25.967 0.51 36.62  ? 108 GLY   A C   1 
ATOM   814  O  O   . GLY   A 1 102 ? 16.932 6.963   26.002 0.51 37.01  ? 108 GLY   A O   1 
ATOM   815  N  N   . ASP   A 1 103 ? 14.774 7.171   25.304 0.51 36.25  ? 109 ASP   A N   1 
ATOM   816  C  CA  . ASP   A 1 103 ? 14.736 5.972   24.423 0.51 35.70  ? 109 ASP   A CA  1 
ATOM   817  C  C   . ASP   A 1 103 ? 15.142 6.346   22.994 0.51 32.57  ? 109 ASP   A C   1 
ATOM   818  O  O   . ASP   A 1 103 ? 15.383 5.411   22.183 0.51 30.43  ? 109 ASP   A O   1 
ATOM   819  C  CB  . ASP   A 1 103 ? 13.360 5.306   24.447 0.51 35.36  ? 109 ASP   A CB  1 
ATOM   820  C  CG  . ASP   A 1 103 ? 13.075 4.620   25.768 0.51 34.48  ? 109 ASP   A CG  1 
ATOM   821  O  OD1 . ASP   A 1 103 ? 14.012 4.000   26.312 0.51 32.39  ? 109 ASP   A OD1 1 
ATOM   822  O  OD2 . ASP   A 1 103 ? 11.921 4.710   26.239 0.51 35.46  ? 109 ASP   A OD2 1 
ATOM   823  N  N   . CYS   A 1 104 ? 15.227 7.641   22.680 0.51 32.27  ? 110 CYS   A N   1 
ATOM   824  C  CA  . CYS   A 1 104 ? 15.571 8.112   21.308 0.51 31.41  ? 110 CYS   A CA  1 
ATOM   825  C  C   . CYS   A 1 104 ? 16.859 7.411   20.850 0.51 32.05  ? 110 CYS   A C   1 
ATOM   826  O  O   . CYS   A 1 104 ? 17.788 7.238   21.679 0.51 29.95  ? 110 CYS   A O   1 
ATOM   827  C  CB  . CYS   A 1 104 ? 15.730 9.626   21.235 0.51 32.90  ? 110 CYS   A CB  1 
ATOM   828  S  SG  . CYS   A 1 104 ? 14.154 10.518  21.239 0.51 35.95  ? 110 CYS   A SG  1 
ATOM   829  N  N   . GLY   A 1 105 ? 16.914 7.007   19.580 0.51 29.26  ? 111 GLY   A N   1 
ATOM   830  C  CA  . GLY   A 1 105 ? 18.050 6.256   19.021 0.51 30.56  ? 111 GLY   A CA  1 
ATOM   831  C  C   . GLY   A 1 105 ? 17.772 4.766   18.959 0.51 30.39  ? 111 GLY   A C   1 
ATOM   832  O  O   . GLY   A 1 105 ? 18.425 4.097   18.110 0.51 28.11  ? 111 GLY   A O   1 
ATOM   833  N  N   . GLY   A 1 106 ? 16.808 4.262   19.753 1.00 29.77  ? 112 GLY   A N   1 
ATOM   834  C  CA  . GLY   A 1 106 ? 16.435 2.842   19.681 1.00 26.81  ? 112 GLY   A CA  1 
ATOM   835  C  C   . GLY   A 1 106 ? 16.054 2.499   18.231 1.00 29.51  ? 112 GLY   A C   1 
ATOM   836  O  O   . GLY   A 1 106 ? 15.325 3.264   17.576 1.00 28.05  ? 112 GLY   A O   1 
ATOM   837  N  N   . ILE   A 1 107 ? 16.518 1.372   17.724 1.00 28.29  ? 113 ILE   A N   1 
ATOM   838  C  CA  . ILE   A 1 107 ? 16.265 0.998   16.303 1.00 28.35  ? 113 ILE   A CA  1 
ATOM   839  C  C   . ILE   A 1 107 ? 14.908 0.338   16.135 1.00 28.65  ? 113 ILE   A C   1 
ATOM   840  O  O   . ILE   A 1 107 ? 14.518 -0.568  16.949 1.00 31.70  ? 113 ILE   A O   1 
ATOM   841  C  CB  . ILE   A 1 107 ? 17.447 0.155   15.801 1.00 32.82  ? 113 ILE   A CB  1 
ATOM   842  C  CG1 . ILE   A 1 107 ? 18.628 1.079   15.464 1.00 36.49  ? 113 ILE   A CG1 1 
ATOM   843  C  CG2 . ILE   A 1 107 ? 17.052 -0.689  14.584 1.00 36.97  ? 113 ILE   A CG2 1 
ATOM   844  C  CD1 . ILE   A 1 107 ? 19.925 0.351   15.177 1.00 36.33  ? 113 ILE   A CD1 1 
ATOM   845  N  N   . LEU   A 1 108 ? 14.260 0.676   15.031 1.00 26.61  ? 114 LEU   A N   1 
ATOM   846  C  CA  . LEU   A 1 108 ? 13.119 -0.039  14.442 1.00 26.78  ? 114 LEU   A CA  1 
ATOM   847  C  C   . LEU   A 1 108 ? 13.608 -0.839  13.221 1.00 33.33  ? 114 LEU   A C   1 
ATOM   848  O  O   . LEU   A 1 108 ? 14.225 -0.245  12.334 1.00 28.69  ? 114 LEU   A O   1 
ATOM   849  C  CB  . LEU   A 1 108 ? 12.026 0.958   14.054 1.00 28.13  ? 114 LEU   A CB  1 
ATOM   850  C  CG  . LEU   A 1 108 ? 10.832 0.386   13.267 1.00 29.27  ? 114 LEU   A CG  1 
ATOM   851  C  CD1 . LEU   A 1 108 ? 9.999  -0.557  14.139 1.00 29.99  ? 114 LEU   A CD1 1 
ATOM   852  C  CD2 . LEU   A 1 108 ? 9.970  1.527   12.724 1.00 30.21  ? 114 LEU   A CD2 1 
ATOM   853  N  N   . ARG   A 1 109 ? 13.332 -2.142  13.215 1.00 31.33  ? 115 ARG   A N   1 
ATOM   854  C  CA  . ARG   A 1 109 ? 13.862 -3.102  12.219 1.00 37.44  ? 115 ARG   A CA  1 
ATOM   855  C  C   . ARG   A 1 109 ? 12.711 -3.962  11.678 1.00 32.78  ? 115 ARG   A C   1 
ATOM   856  O  O   . ARG   A 1 109 ? 11.767 -4.247  12.422 1.00 30.54  ? 115 ARG   A O   1 
ATOM   857  C  CB  . ARG   A 1 109 ? 15.061 -3.878  12.774 1.00 38.65  ? 115 ARG   A CB  1 
ATOM   858  C  CG  . ARG   A 1 109 ? 14.811 -4.809  13.946 1.00 57.44  ? 115 ARG   A CG  1 
ATOM   859  C  CD  . ARG   A 1 109 ? 16.090 -5.549  14.351 1.00 71.90  ? 115 ARG   A CD  1 
ATOM   860  N  NE  . ARG   A 1 109 ? 17.011 -4.749  15.178 1.00 79.78  ? 115 ARG   A NE  1 
ATOM   861  C  CZ  . ARG   A 1 109 ? 18.155 -4.174  14.764 1.00 88.64  ? 115 ARG   A CZ  1 
ATOM   862  N  NH1 . ARG   A 1 109 ? 18.585 -4.298  13.516 1.00 77.43  ? 115 ARG   A NH1 1 
ATOM   863  N  NH2 . ARG   A 1 109 ? 18.886 -3.474  15.619 1.00 86.46  ? 115 ARG   A NH2 1 
ATOM   864  N  N   . CYS   A 1 110 ? 12.703 -4.197  10.367 1.00 31.24  ? 116 CYS   A N   1 
ATOM   865  C  CA  . CYS   A 1 110 ? 11.807 -5.154  9.692  1.00 33.28  ? 116 CYS   A CA  1 
ATOM   866  C  C   . CYS   A 1 110 ? 12.700 -6.286  9.164  1.00 35.69  ? 116 CYS   A C   1 
ATOM   867  O  O   . CYS   A 1 110 ? 13.913 -6.273  9.416  1.00 35.03  ? 116 CYS   A O   1 
ATOM   868  C  CB  . CYS   A 1 110 ? 11.001 -4.478  8.584  1.00 32.40  ? 116 CYS   A CB  1 
ATOM   869  S  SG  . CYS   A 1 110 ? 12.074 -3.905  7.241  1.00 31.60  ? 116 CYS   A SG  1 
ATOM   870  N  N   . GLN   A 1 111 ? 12.127 -7.244  8.449  1.00 38.68  ? 117 GLN   A N   1 
ATOM   871  C  CA  . GLN   A 1 111 ? 12.913 -8.343  7.818  1.00 42.78  ? 117 GLN   A CA  1 
ATOM   872  C  C   . GLN   A 1 111 ? 13.943 -7.807  6.814  1.00 39.42  ? 117 GLN   A C   1 
ATOM   873  O  O   . GLN   A 1 111 ? 14.907 -8.528  6.528  1.00 47.09  ? 117 GLN   A O   1 
ATOM   874  C  CB  . GLN   A 1 111 ? 11.962 -9.269  7.066  1.00 43.74  ? 117 GLN   A CB  1 
ATOM   875  C  CG  . GLN   A 1 111 ? 11.237 -8.594  5.926  1.00 42.55  ? 117 GLN   A CG  1 
ATOM   876  C  CD  . GLN   A 1 111 ? 10.318 -9.572  5.250  1.00 51.45  ? 117 GLN   A CD  1 
ATOM   877  O  OE1 . GLN   A 1 111 ? 9.091  -9.446  5.299  1.00 56.54  ? 117 GLN   A OE1 1 
ATOM   878  N  NE2 . GLN   A 1 111 ? 10.924 -10.585 4.658  1.00 57.69  ? 117 GLN   A NE2 1 
ATOM   879  N  N   . HIS   A 1 112 ? 13.800 -6.575  6.315  1.00 36.82  ? 118 HIS   A N   1 
ATOM   880  C  CA  . HIS   A 1 112 ? 14.760 -6.030  5.315  1.00 35.59  ? 118 HIS   A CA  1 
ATOM   881  C  C   . HIS   A 1 112 ? 15.938 -5.274  5.952  1.00 40.72  ? 118 HIS   A C   1 
ATOM   882  O  O   . HIS   A 1 112 ? 16.848 -4.849  5.184  1.00 44.61  ? 118 HIS   A O   1 
ATOM   883  C  CB  . HIS   A 1 112 ? 14.008 -5.221  4.274  1.00 36.15  ? 118 HIS   A CB  1 
ATOM   884  C  CG  . HIS   A 1 112 ? 12.902 -5.988  3.650  1.00 38.03  ? 118 HIS   A CG  1 
ATOM   885  N  ND1 . HIS   A 1 112 ? 11.582 -5.753  3.967  1.00 38.95  ? 118 HIS   A ND1 1 
ATOM   886  C  CD2 . HIS   A 1 112 ? 12.899 -6.976  2.731  1.00 40.64  ? 118 HIS   A CD2 1 
ATOM   887  C  CE1 . HIS   A 1 112 ? 10.808 -6.532  3.251  1.00 40.86  ? 118 HIS   A CE1 1 
ATOM   888  N  NE2 . HIS   A 1 112 ? 11.591 -7.303  2.501  1.00 43.77  ? 118 HIS   A NE2 1 
ATOM   889  N  N   . GLY   A 1 113 ? 15.943 -5.072  7.270  1.00 37.90  ? 119 GLY   A N   1 
ATOM   890  C  CA  . GLY   A 1 113 ? 16.973 -4.272  7.962  1.00 39.06  ? 119 GLY   A CA  1 
ATOM   891  C  C   . GLY   A 1 113 ? 16.413 -3.081  8.730  1.00 37.87  ? 119 GLY   A C   1 
ATOM   892  O  O   . GLY   A 1 113 ? 15.258 -3.139  9.210  1.00 31.64  ? 119 GLY   A O   1 
ATOM   893  N  N   . VAL   A 1 114 ? 17.236 -2.040  8.884  1.00 36.02  ? 120 VAL   A N   1 
ATOM   894  C  CA  . VAL   A 1 114 ? 16.946 -0.847  9.734  1.00 34.83  ? 120 VAL   A CA  1 
ATOM   895  C  C   . VAL   A 1 114 ? 15.952 0.052   9.005  1.00 35.00  ? 120 VAL   A C   1 
ATOM   896  O  O   . VAL   A 1 114 ? 16.195 0.425   7.812  1.00 29.68  ? 120 VAL   A O   1 
ATOM   897  C  CB  . VAL   A 1 114 ? 18.243 -0.106  10.136 1.00 35.35  ? 120 VAL   A CB  1 
ATOM   898  C  CG1 . VAL   A 1 114 ? 17.903 1.178   10.878 1.00 35.71  ? 120 VAL   A CG1 1 
ATOM   899  C  CG2 . VAL   A 1 114 ? 19.164 -1.000  10.983 1.00 36.52  ? 120 VAL   A CG2 1 
ATOM   900  N  N   . VAL   A 1 115 ? 14.839 0.374   9.670  1.00 30.34  ? 121 VAL   A N   1 
ATOM   901  C  CA  . VAL   A 1 115 ? 13.756 1.233   9.114  1.00 28.08  ? 121 VAL   A CA  1 
ATOM   902  C  C   . VAL   A 1 115 ? 13.935 2.673   9.637  1.00 31.03  ? 121 VAL   A C   1 
ATOM   903  O  O   . VAL   A 1 115 ? 13.674 3.640   8.923  1.00 28.47  ? 121 VAL   A O   1 
ATOM   904  C  CB  . VAL   A 1 115 ? 12.378 0.667   9.501  1.00 29.29  ? 121 VAL   A CB  1 
ATOM   905  C  CG1 . VAL   A 1 115 ? 11.242 1.615   9.157  1.00 29.47  ? 121 VAL   A CG1 1 
ATOM   906  C  CG2 . VAL   A 1 115 ? 12.159 -0.731  8.959  1.00 27.76  ? 121 VAL   A CG2 1 
ATOM   907  N  N   . GLY   A 1 116 ? 14.296 2.843   10.907 1.00 26.61  ? 122 GLY   A N   1 
ATOM   908  C  CA  . GLY   A 1 116 ? 14.375 4.174   11.488 1.00 30.89  ? 122 GLY   A CA  1 
ATOM   909  C  C   . GLY   A 1 116 ? 14.793 4.099   12.945 1.00 28.88  ? 122 GLY   A C   1 
ATOM   910  O  O   . GLY   A 1 116 ? 15.146 2.990   13.379 1.00 27.53  ? 122 GLY   A O   1 
ATOM   911  N  N   . ILE   A 1 117 ? 14.811 5.256   13.611 1.00 29.06  ? 123 ILE   A N   1 
ATOM   912  C  CA  . ILE   A 1 117 ? 15.217 5.376   15.048 1.00 26.51  ? 123 ILE   A CA  1 
ATOM   913  C  C   . ILE   A 1 117 ? 14.099 6.098   15.789 1.00 28.99  ? 123 ILE   A C   1 
ATOM   914  O  O   . ILE   A 1 117 ? 13.458 7.022   15.219 1.00 28.87  ? 123 ILE   A O   1 
ATOM   915  C  CB  . ILE   A 1 117 ? 16.588 6.050   15.280 1.00 28.09  ? 123 ILE   A CB  1 
ATOM   916  C  CG1 . ILE   A 1 117 ? 16.701 7.385   14.550 1.00 33.42  ? 123 ILE   A CG1 1 
ATOM   917  C  CG2 . ILE   A 1 117 ? 17.743 5.100   14.987 1.00 30.78  ? 123 ILE   A CG2 1 
ATOM   918  C  CD1 . ILE   A 1 117 ? 17.883 8.212   14.988 1.00 34.04  ? 123 ILE   A CD1 1 
ATOM   919  N  N   . VAL   A 1 118 ? 13.869 5.681   17.045 1.00 31.29  ? 124 VAL   A N   1 
ATOM   920  C  CA  . VAL   A 1 118 ? 12.984 6.418   17.978 1.00 28.94  ? 124 VAL   A CA  1 
ATOM   921  C  C   . VAL   A 1 118 ? 13.368 7.901   18.001 1.00 27.00  ? 124 VAL   A C   1 
ATOM   922  O  O   . VAL   A 1 118 ? 14.560 8.248   18.170 1.00 26.42  ? 124 VAL   A O   1 
ATOM   923  C  CB  . VAL   A 1 118 ? 13.041 5.810   19.387 1.00 26.91  ? 124 VAL   A CB  1 
ATOM   924  C  CG1 . VAL   A 1 118 ? 12.174 6.580   20.352 1.00 28.32  ? 124 VAL   A CG1 1 
ATOM   925  C  CG2 . VAL   A 1 118 ? 12.585 4.354   19.398 1.00 27.24  ? 124 VAL   A CG2 1 
ATOM   926  N  N   . SER   A 1 119 ? 12.354 8.728   17.828 1.00 26.93  ? 125 SER   A N   1 
ATOM   927  C  CA  . SER   A 1 119 ? 12.504 10.198  17.759 1.00 27.06  ? 125 SER   A CA  1 
ATOM   928  C  C   . SER   A 1 119 ? 11.473 10.912  18.626 1.00 28.76  ? 125 SER   A C   1 
ATOM   929  O  O   . SER   A 1 119 ? 11.824 11.968  19.134 1.00 33.19  ? 125 SER   A O   1 
ATOM   930  C  CB  . SER   A 1 119 ? 12.440 10.655  16.315 1.00 27.40  ? 125 SER   A CB  1 
ATOM   931  O  OG  . SER   A 1 119 ? 12.594 12.088  16.237 1.00 31.11  ? 125 SER   A OG  1 
ATOM   932  N  N   . THR   A 1 120 ? 10.216 10.467  18.695 1.00 29.28  ? 126 THR   A N   1 
ATOM   933  C  CA  . THR   A 1 120 ? 9.125  11.191  19.404 1.00 35.44  ? 126 THR   A CA  1 
ATOM   934  C  C   . THR   A 1 120 ? 8.344  10.215  20.295 1.00 37.82  ? 126 THR   A C   1 
ATOM   935  O  O   . THR   A 1 120 ? 8.504  8.977   20.133 1.00 32.31  ? 126 THR   A O   1 
ATOM   936  C  CB  . THR   A 1 120 ? 8.190  11.947  18.448 1.00 38.59  ? 126 THR   A CB  1 
ATOM   937  O  OG1 . THR   A 1 120 ? 7.266  11.017  17.879 1.00 36.56  ? 126 THR   A OG1 1 
ATOM   938  C  CG2 . THR   A 1 120 ? 8.925  12.671  17.340 1.00 36.10  ? 126 THR   A CG2 1 
ATOM   939  N  N   . GLY   A 1 121 ? 7.565  10.730  21.262 1.00 36.44  ? 127 GLY   A N   1 
ATOM   940  C  CA  . GLY   A 1 121 ? 6.573  9.859   21.936 1.00 38.66  ? 127 GLY   A CA  1 
ATOM   941  C  C   . GLY   A 1 121 ? 5.673  10.613  22.910 1.00 35.65  ? 127 GLY   A C   1 
ATOM   942  O  O   . GLY   A 1 121 ? 5.779  11.851  23.019 1.00 37.13  ? 127 GLY   A O   1 
ATOM   943  N  N   . GLY   A 1 122 ? 4.859  9.883   23.634 1.00 46.76  ? 128 GLY   A N   1 
ATOM   944  C  CA  . GLY   A 1 122 ? 3.910  10.466  24.607 1.00 50.79  ? 128 GLY   A CA  1 
ATOM   945  C  C   . GLY   A 1 122 ? 2.536  9.898   24.381 1.00 48.55  ? 128 GLY   A C   1 
ATOM   946  O  O   . GLY   A 1 122 ? 2.226  9.512   23.226 1.00 41.01  ? 128 GLY   A O   1 
ATOM   947  N  N   . ASN   A 1 123 ? 1.725  9.839   25.440 1.00 54.89  ? 129 ASN   A N   1 
ATOM   948  C  CA  . ASN   A 1 123 ? 0.303  9.425   25.325 1.00 47.69  ? 129 ASN   A CA  1 
ATOM   949  C  C   . ASN   A 1 123 ? 0.235  7.978   24.819 1.00 39.40  ? 129 ASN   A C   1 
ATOM   950  O  O   . ASN   A 1 123 ? -0.755 7.641   24.186 1.00 42.27  ? 129 ASN   A O   1 
ATOM   951  C  CB  . ASN   A 1 123 ? -0.495 10.339  24.378 1.00 52.28  ? 129 ASN   A CB  1 
ATOM   952  C  CG  . ASN   A 1 123 ? -0.598 11.793  24.812 1.00 61.46  ? 129 ASN   A CG  1 
ATOM   953  O  OD1 . ASN   A 1 123 ? -0.344 12.131  25.980 1.00 56.19  ? 129 ASN   A OD1 1 
ATOM   954  N  ND2 . ASN   A 1 123 ? -1.005 12.652  23.876 1.00 49.27  ? 129 ASN   A ND2 1 
ATOM   955  N  N   . GLY   A 1 124 ? 1.240  7.132   25.074 1.00 38.00  ? 130 GLY   A N   1 
ATOM   956  C  CA  . GLY   A 1 124 ? 1.181  5.714   24.654 1.00 35.71  ? 130 GLY   A CA  1 
ATOM   957  C  C   . GLY   A 1 124 ? 1.525  5.526   23.166 1.00 33.47  ? 130 GLY   A C   1 
ATOM   958  O  O   . GLY   A 1 124 ? 1.304  4.409   22.624 1.00 34.11  ? 130 GLY   A O   1 
ATOM   959  N  N   . LEU   A 1 125 ? 2.126  6.541   22.550 1.00 32.34  ? 131 LEU   A N   1 
ATOM   960  C  CA  . LEU   A 1 125 ? 2.581  6.458   21.136 1.00 36.38  ? 131 LEU   A CA  1 
ATOM   961  C  C   . LEU   A 1 125 ? 4.104  6.595   21.108 1.00 39.51  ? 131 LEU   A C   1 
ATOM   962  O  O   . LEU   A 1 125 ? 4.674  7.218   22.028 1.00 50.73  ? 131 LEU   A O   1 
ATOM   963  C  CB  . LEU   A 1 125 ? 1.911  7.563   20.329 1.00 36.97  ? 131 LEU   A CB  1 
ATOM   964  C  CG  . LEU   A 1 125 ? 0.383  7.577   20.289 1.00 40.89  ? 131 LEU   A CG  1 
ATOM   965  C  CD1 . LEU   A 1 125 ? -0.079 8.741   19.425 1.00 51.21  ? 131 LEU   A CD1 1 
ATOM   966  C  CD2 . LEU   A 1 125 ? -0.177 6.286   19.751 1.00 44.13  ? 131 LEU   A CD2 1 
ATOM   967  N  N   . VAL   A 1 126 ? 4.732  5.996   20.103 1.00 32.56  ? 132 VAL   A N   1 
ATOM   968  C  CA  . VAL   A 1 126 ? 6.183  6.124   19.860 1.00 32.08  ? 132 VAL   A CA  1 
ATOM   969  C  C   . VAL   A 1 126 ? 6.338  6.479   18.373 1.00 30.04  ? 132 VAL   A C   1 
ATOM   970  O  O   . VAL   A 1 126 ? 5.590  5.953   17.546 1.00 28.37  ? 132 VAL   A O   1 
ATOM   971  C  CB  . VAL   A 1 126 ? 6.936  4.846   20.276 1.00 30.42  ? 132 VAL   A CB  1 
ATOM   972  C  CG1 . VAL   A 1 126 ? 6.317  3.587   19.718 1.00 35.27  ? 132 VAL   A CG1 1 
ATOM   973  C  CG2 . VAL   A 1 126 ? 8.386  4.951   19.910 1.00 29.74  ? 132 VAL   A CG2 1 
ATOM   974  N  N   . GLY   A 1 127 ? 7.106  7.521   18.119 1.00 29.68  ? 133 GLY   A N   1 
ATOM   975  C  CA  . GLY   A 1 127 ? 7.419  7.961   16.752 1.00 31.29  ? 133 GLY   A CA  1 
ATOM   976  C  C   . GLY   A 1 127 ? 8.832  7.587   16.374 1.00 28.02  ? 133 GLY   A C   1 
ATOM   977  O  O   . GLY   A 1 127 ? 9.774  7.803   17.168 1.00 27.95  ? 133 GLY   A O   1 
ATOM   978  N  N   . PHE   A 1 128 ? 9.008  7.236   15.117 1.00 28.55  ? 134 PHE   A N   1 
ATOM   979  C  CA  . PHE   A 1 128 ? 10.310 6.788   14.583 1.00 27.62  ? 134 PHE   A CA  1 
ATOM   980  C  C   . PHE   A 1 128 ? 10.641 7.630   13.355 1.00 28.99  ? 134 PHE   A C   1 
ATOM   981  O  O   . PHE   A 1 128 ? 9.733  7.806   12.535 1.00 27.75  ? 134 PHE   A O   1 
ATOM   982  C  CB  . PHE   A 1 128 ? 10.224 5.338   14.114 1.00 28.45  ? 134 PHE   A CB  1 
ATOM   983  C  CG  . PHE   A 1 128 ? 9.670  4.370   15.129 1.00 29.87  ? 134 PHE   A CG  1 
ATOM   984  C  CD1 . PHE   A 1 128 ? 10.501 3.781   16.073 1.00 28.99  ? 134 PHE   A CD1 1 
ATOM   985  C  CD2 . PHE   A 1 128 ? 8.334  4.018   15.115 1.00 29.24  ? 134 PHE   A CD2 1 
ATOM   986  C  CE1 . PHE   A 1 128 ? 9.988  2.893   16.993 1.00 29.23  ? 134 PHE   A CE1 1 
ATOM   987  C  CE2 . PHE   A 1 128 ? 7.833  3.081   16.006 1.00 29.75  ? 134 PHE   A CE2 1 
ATOM   988  C  CZ  . PHE   A 1 128 ? 8.651  2.544   16.962 1.00 28.83  ? 134 PHE   A CZ  1 
ATOM   989  N  N   . ALA   A 1 129 ? 11.856 8.153   13.281 1.00 31.74  ? 135 ALA   A N   1 
ATOM   990  C  CA  . ALA   A 1 129 ? 12.343 8.940   12.111 1.00 29.71  ? 135 ALA   A CA  1 
ATOM   991  C  C   . ALA   A 1 129 ? 12.739 7.943   10.999 1.00 29.24  ? 135 ALA   A C   1 
ATOM   992  O  O   . ALA   A 1 129 ? 13.632 7.125   11.209 1.00 27.80  ? 135 ALA   A O   1 
ATOM   993  C  CB  . ALA   A 1 129 ? 13.466 9.863   12.545 1.00 31.36  ? 135 ALA   A CB  1 
ATOM   994  N  N   . ASP   A 1 130 ? 12.041 7.946   9.867  1.00 32.48  ? 136 ASP   A N   1 
ATOM   995  C  CA  . ASP   A 1 130 ? 12.364 7.015   8.752  1.00 31.79  ? 136 ASP   A CA  1 
ATOM   996  C  C   . ASP   A 1 130 ? 13.780 7.291   8.215  1.00 29.04  ? 136 ASP   A C   1 
ATOM   997  O  O   . ASP   A 1 130 ? 14.159 8.424   8.144  1.00 28.72  ? 136 ASP   A O   1 
ATOM   998  C  CB  . ASP   A 1 130 ? 11.305 7.086   7.656  1.00 32.83  ? 136 ASP   A CB  1 
ATOM   999  C  CG  . ASP   A 1 130 ? 11.508 6.062   6.568  1.00 36.62  ? 136 ASP   A CG  1 
ATOM   1000 O  OD1 . ASP   A 1 130 ? 11.549 4.880   6.906  1.00 33.33  ? 136 ASP   A OD1 1 
ATOM   1001 O  OD2 . ASP   A 1 130 ? 11.557 6.458   5.356  1.00 38.59  ? 136 ASP   A OD2 1 
ATOM   1002 N  N   . VAL   A 1 131 ? 14.541 6.274   7.848  1.00 28.82  ? 137 VAL   A N   1 
ATOM   1003 C  CA  . VAL   A 1 131 ? 15.812 6.469   7.083  1.00 33.00  ? 137 VAL   A CA  1 
ATOM   1004 C  C   . VAL   A 1 131 ? 15.720 5.739   5.727  1.00 38.00  ? 137 VAL   A C   1 
ATOM   1005 O  O   . VAL   A 1 131 ? 16.689 5.840   4.945  1.00 39.17  ? 137 VAL   A O   1 
ATOM   1006 C  CB  . VAL   A 1 131 ? 17.028 6.014   7.904  1.00 26.70  ? 137 VAL   A CB  1 
ATOM   1007 C  CG1 . VAL   A 1 131 ? 17.121 6.757   9.211  1.00 28.41  ? 137 VAL   A CG1 1 
ATOM   1008 C  CG2 . VAL   A 1 131 ? 17.058 4.513   8.130  1.00 28.45  ? 137 VAL   A CG2 1 
ATOM   1009 N  N   . ARG   A 1 132 ? 14.594 5.077   5.394  1.00 33.21  ? 138 ARG   A N   1 
ATOM   1010 C  CA  . ARG   A 1 132 ? 14.558 4.187   4.213  1.00 31.81  ? 138 ARG   A CA  1 
ATOM   1011 C  C   . ARG   A 1 132 ? 14.591 4.975   2.880  1.00 35.30  ? 138 ARG   A C   1 
ATOM   1012 O  O   . ARG   A 1 132 ? 14.902 4.334   1.854  1.00 34.12  ? 138 ARG   A O   1 
ATOM   1013 C  CB  . ARG   A 1 132 ? 13.346 3.259   4.236  1.00 34.05  ? 138 ARG   A CB  1 
ATOM   1014 C  CG  . ARG   A 1 132 ? 13.334 2.314   5.426  1.00 32.93  ? 138 ARG   A CG  1 
ATOM   1015 C  CD  . ARG   A 1 132 ? 12.083 1.459   5.351  1.00 32.39  ? 138 ARG   A CD  1 
ATOM   1016 N  NE  . ARG   A 1 132 ? 10.962 2.313   5.699  1.00 31.76  ? 138 ARG   A NE  1 
ATOM   1017 C  CZ  . ARG   A 1 132 ? 9.704  1.923   5.793  1.00 32.98  ? 138 ARG   A CZ  1 
ATOM   1018 N  NH1 . ARG   A 1 132 ? 9.381  0.668   5.543  1.00 34.59  ? 138 ARG   A NH1 1 
ATOM   1019 N  NH2 . ARG   A 1 132 ? 8.797  2.763   6.254  1.00 33.66  ? 138 ARG   A NH2 1 
ATOM   1020 N  N   . ASP   A 1 133 ? 14.271 6.267   2.853  1.00 33.80  ? 139 ASP   A N   1 
ATOM   1021 C  CA  . ASP   A 1 133 ? 14.368 7.120   1.625  1.00 36.14  ? 139 ASP   A CA  1 
ATOM   1022 C  C   . ASP   A 1 133 ? 15.807 7.596   1.371  1.00 37.96  ? 139 ASP   A C   1 
ATOM   1023 O  O   . ASP   A 1 133 ? 16.067 8.066   0.271  1.00 37.69  ? 139 ASP   A O   1 
ATOM   1024 C  CB  . ASP   A 1 133 ? 13.422 8.312   1.735  1.00 36.24  ? 139 ASP   A CB  1 
ATOM   1025 C  CG  . ASP   A 1 133 ? 13.799 9.263   2.860  1.00 39.95  ? 139 ASP   A CG  1 
ATOM   1026 O  OD1 . ASP   A 1 133 ? 14.245 8.781   3.919  1.00 39.69  ? 139 ASP   A OD1 1 
ATOM   1027 O  OD2 . ASP   A 1 133 ? 13.694 10.470  2.652  1.00 39.70  ? 139 ASP   A OD2 1 
ATOM   1028 N  N   . LEU   A 1 134 ? 16.724 7.473   2.336  1.00 34.18  ? 140 LEU   A N   1 
ATOM   1029 C  CA  . LEU   A 1 134 ? 18.122 7.988   2.277  1.00 36.28  ? 140 LEU   A CA  1 
ATOM   1030 C  C   . LEU   A 1 134 ? 18.983 6.963   1.523  1.00 37.67  ? 140 LEU   A C   1 
ATOM   1031 O  O   . LEU   A 1 134 ? 19.798 6.230   2.123  1.00 32.11  ? 140 LEU   A O   1 
ATOM   1032 C  CB  . LEU   A 1 134 ? 18.609 8.274   3.703  1.00 39.86  ? 140 LEU   A CB  1 
ATOM   1033 C  CG  . LEU   A 1 134 ? 17.739 9.242   4.511  1.00 36.49  ? 140 LEU   A CG  1 
ATOM   1034 C  CD1 . LEU   A 1 134 ? 18.323 9.473   5.905  1.00 38.23  ? 140 LEU   A CD1 1 
ATOM   1035 C  CD2 . LEU   A 1 134 ? 17.555 10.577  3.799  1.00 39.58  ? 140 LEU   A CD2 1 
ATOM   1036 N  N   . LEU   A 1 135 ? 18.807 6.931   0.200  1.00 35.94  ? 141 LEU   A N   1 
ATOM   1037 C  CA  . LEU   A 1 135 ? 19.363 5.893   -0.683 1.00 40.68  ? 141 LEU   A CA  1 
ATOM   1038 C  C   . LEU   A 1 135 ? 20.879 6.019   -0.707 1.00 44.04  ? 141 LEU   A C   1 
ATOM   1039 O  O   . LEU   A 1 135 ? 21.548 4.988   -0.872 1.00 45.46  ? 141 LEU   A O   1 
ATOM   1040 C  CB  . LEU   A 1 135 ? 18.781 6.026   -2.091 1.00 40.81  ? 141 LEU   A CB  1 
ATOM   1041 C  CG  . LEU   A 1 135 ? 17.290 5.828   -2.235 1.00 44.87  ? 141 LEU   A CG  1 
ATOM   1042 C  CD1 . LEU   A 1 135 ? 16.947 5.616   -3.706 1.00 52.85  ? 141 LEU   A CD1 1 
ATOM   1043 C  CD2 . LEU   A 1 135 ? 16.789 4.670   -1.385 1.00 46.10  ? 141 LEU   A CD2 1 
ATOM   1044 N  N   . TRP   A 1 136 ? 21.389 7.225   -0.483 1.00 42.01  ? 142 TRP   A N   1 
ATOM   1045 C  CA  . TRP   A 1 136 ? 22.848 7.494   -0.527 1.00 40.15  ? 142 TRP   A CA  1 
ATOM   1046 C  C   . TRP   A 1 136 ? 23.547 6.829   0.653  1.00 41.46  ? 142 TRP   A C   1 
ATOM   1047 O  O   . TRP   A 1 136 ? 24.713 6.641   0.553  1.00 39.62  ? 142 TRP   A O   1 
ATOM   1048 C  CB  . TRP   A 1 136 ? 23.148 8.998   -0.581 1.00 40.05  ? 142 TRP   A CB  1 
ATOM   1049 C  CG  . TRP   A 1 136 ? 22.448 9.831   0.441  1.00 37.49  ? 142 TRP   A CG  1 
ATOM   1050 C  CD1 . TRP   A 1 136 ? 21.252 10.474  0.312  1.00 37.75  ? 142 TRP   A CD1 1 
ATOM   1051 C  CD2 . TRP   A 1 136 ? 22.916 10.126  1.761  1.00 36.66  ? 142 TRP   A CD2 1 
ATOM   1052 N  NE1 . TRP   A 1 136 ? 20.933 11.124  1.471  1.00 37.52  ? 142 TRP   A NE1 1 
ATOM   1053 C  CE2 . TRP   A 1 136 ? 21.950 10.950  2.365  1.00 35.08  ? 142 TRP   A CE2 1 
ATOM   1054 C  CE3 . TRP   A 1 136 ? 24.046 9.759   2.491  1.00 39.80  ? 142 TRP   A CE3 1 
ATOM   1055 C  CZ2 . TRP   A 1 136 ? 22.077 11.393  3.673  1.00 35.22  ? 142 TRP   A CZ2 1 
ATOM   1056 C  CZ3 . TRP   A 1 136 ? 24.192 10.242  3.766  1.00 37.62  ? 142 TRP   A CZ3 1 
ATOM   1057 C  CH2 . TRP   A 1 136 ? 23.222 11.053  4.335  1.00 34.36  ? 142 TRP   A CH2 1 
ATOM   1058 N  N   . LEU   A 1 137 ? 22.853 6.461   1.736  1.00 42.29  ? 143 LEU   A N   1 
ATOM   1059 C  CA  . LEU   A 1 137 ? 23.511 5.769   2.874  1.00 40.34  ? 143 LEU   A CA  1 
ATOM   1060 C  C   . LEU   A 1 137 ? 24.194 4.465   2.403  1.00 40.52  ? 143 LEU   A C   1 
ATOM   1061 O  O   . LEU   A 1 137 ? 25.098 4.084   3.096  1.00 42.35  ? 143 LEU   A O   1 
ATOM   1062 C  CB  . LEU   A 1 137 ? 22.510 5.445   3.978  1.00 43.37  ? 143 LEU   A CB  1 
ATOM   1063 C  CG  . LEU   A 1 137 ? 22.027 6.620   4.810  1.00 38.80  ? 143 LEU   A CG  1 
ATOM   1064 C  CD1 . LEU   A 1 137 ? 20.838 6.185   5.666  1.00 43.13  ? 143 LEU   A CD1 1 
ATOM   1065 C  CD2 . LEU   A 1 137 ? 23.141 7.158   5.711  1.00 41.08  ? 143 LEU   A CD2 1 
ATOM   1066 N  N   . ASP   A 1 138 ? 23.758 3.846   1.306  1.00 48.44  ? 144 ASP   A N   1 
ATOM   1067 C  CA  . ASP   A 1 138 ? 24.246 2.535   0.784  1.00 52.53  ? 144 ASP   A CA  1 
ATOM   1068 C  C   . ASP   A 1 138 ? 25.409 2.695   -0.210 1.00 66.84  ? 144 ASP   A C   1 
ATOM   1069 O  O   . ASP   A 1 138 ? 25.861 1.662   -0.720 1.00 67.93  ? 144 ASP   A O   1 
ATOM   1070 C  CB  . ASP   A 1 138 ? 23.227 1.826   -0.101 1.00 54.65  ? 144 ASP   A CB  1 
ATOM   1071 C  CG  . ASP   A 1 138 ? 21.871 1.504   0.490  1.00 59.76  ? 144 ASP   A CG  1 
ATOM   1072 O  OD1 . ASP   A 1 138 ? 21.787 1.375   1.728  1.00 58.88  ? 144 ASP   A OD1 1 
ATOM   1073 O  OD2 . ASP   A 1 138 ? 20.905 1.349   -0.327 1.00 61.27  ? 144 ASP   A OD2 1 
ATOM   1074 N  N   . GLU   A 1 139 ? 25.834 3.917   -0.552 1.00 77.46  ? 145 GLU   A N   1 
ATOM   1075 C  CA  . GLU   A 1 139 ? 26.919 4.132   -1.557 1.00 91.17  ? 145 GLU   A CA  1 
ATOM   1076 C  C   . GLU   A 1 139 ? 27.766 5.359   -1.190 1.00 99.08  ? 145 GLU   A C   1 
ATOM   1077 O  O   . GLU   A 1 139 ? 27.434 6.046   -0.194 1.00 97.88  ? 145 GLU   A O   1 
ATOM   1078 C  CB  . GLU   A 1 139 ? 26.328 4.241   -2.969 1.00 91.84  ? 145 GLU   A CB  1 
ATOM   1079 C  CG  . GLU   A 1 139 ? 25.386 5.417   -3.191 1.00 85.97  ? 145 GLU   A CG  1 
ATOM   1080 C  CD  . GLU   A 1 139 ? 24.273 5.136   -4.194 1.00 92.20  ? 145 GLU   A CD  1 
ATOM   1081 O  OE1 . GLU   A 1 139 ? 23.967 6.020   -5.040 1.00 75.07  ? 145 GLU   A OE1 1 
ATOM   1082 O  OE2 . GLU   A 1 139 ? 23.700 4.024   -4.124 1.00 96.82  ? 145 GLU   A OE2 1 
HETATM 1083 ZN ZN  . ZN    B 2 .   ? 10.951 -4.100  5.283  1.00 34.26  ? 201 ZN    A ZN  1 
HETATM 1084 S  S   . DMS   C 3 .   ? 18.574 -7.579  8.392  1.00 136.29 ? 202 DMS   A S   1 
HETATM 1085 O  O   . DMS   C 3 .   ? 19.263 -7.672  7.062  1.00 128.61 ? 202 DMS   A O   1 
HETATM 1086 C  C1  . DMS   C 3 .   ? 17.735 -9.123  8.633  1.00 133.10 ? 202 DMS   A C1  1 
HETATM 1087 C  C2  . DMS   C 3 .   ? 19.838 -7.791  9.618  1.00 143.62 ? 202 DMS   A C2  1 
HETATM 1088 S  S   . DMS   D 3 .   ? 15.292 21.545  7.293  1.00 101.27 ? 203 DMS   A S   1 
HETATM 1089 O  O   . DMS   D 3 .   ? 14.764 21.451  8.693  1.00 68.73  ? 203 DMS   A O   1 
HETATM 1090 C  C1  . DMS   D 3 .   ? 13.922 21.170  6.220  1.00 85.64  ? 203 DMS   A C1  1 
HETATM 1091 C  C2  . DMS   D 3 .   ? 15.450 23.282  6.938  1.00 97.39  ? 203 DMS   A C2  1 
HETATM 1092 S  S   . DMS   E 3 .   ? 20.623 -2.519  22.173 1.00 123.65 ? 204 DMS   A S   1 
HETATM 1093 O  O   . DMS   E 3 .   ? 21.131 -3.328  23.330 1.00 111.53 ? 204 DMS   A O   1 
HETATM 1094 C  C1  . DMS   E 3 .   ? 21.995 -2.299  21.058 1.00 122.16 ? 204 DMS   A C1  1 
HETATM 1095 C  C2  . DMS   E 3 .   ? 19.651 -3.628  21.186 1.00 111.55 ? 204 DMS   A C2  1 
HETATM 1096 S  S   . DMS   F 3 .   ? 0.312  -2.187  23.362 1.00 111.33 ? 205 DMS   A S   1 
HETATM 1097 O  O   . DMS   F 3 .   ? 0.650  -0.818  23.906 1.00 72.87  ? 205 DMS   A O   1 
HETATM 1098 C  C1  . DMS   F 3 .   ? 1.375  -3.313  24.219 1.00 107.50 ? 205 DMS   A C1  1 
HETATM 1099 C  C2  . DMS   F 3 .   ? -1.221 -2.715  24.104 1.00 95.80  ? 205 DMS   A C2  1 
HETATM 1100 S  S   . SO4   G 4 .   ? -0.716 24.544  14.306 1.00 154.36 ? 206 SO4   A S   1 
HETATM 1101 O  O1  . SO4   G 4 .   ? 0.487  25.212  13.885 1.00 153.80 ? 206 SO4   A O1  1 
HETATM 1102 O  O2  . SO4   G 4 .   ? -1.587 24.360  13.176 1.00 142.08 ? 206 SO4   A O2  1 
HETATM 1103 O  O3  . SO4   G 4 .   ? -0.376 23.262  14.855 1.00 139.39 ? 206 SO4   A O3  1 
HETATM 1104 O  O4  . SO4   G 4 .   ? -1.381 25.341  15.308 1.00 141.74 ? 206 SO4   A O4  1 
HETATM 1105 N  N1  . A1BQ0 H 5 .   ? 10.816 11.305  22.442 0.51 25.17  ? 207 A1BQ0 A N1  1 
HETATM 1106 C  C4  . A1BQ0 H 5 .   ? 11.412 15.550  19.621 0.51 33.59  ? 207 A1BQ0 A C4  1 
HETATM 1107 C  C5  . A1BQ0 H 5 .   ? 12.804 15.100  19.830 0.51 30.93  ? 207 A1BQ0 A C5  1 
HETATM 1108 C  C6  . A1BQ0 H 5 .   ? 9.370  11.982  24.067 0.51 27.77  ? 207 A1BQ0 A C6  1 
HETATM 1109 C  C7  . A1BQ0 H 5 .   ? 8.597  12.650  25.015 0.51 29.13  ? 207 A1BQ0 A C7  1 
HETATM 1110 C  C8  . A1BQ0 H 5 .   ? 7.814  11.883  25.847 0.51 29.24  ? 207 A1BQ0 A C8  1 
HETATM 1111 C  C10 . A1BQ0 H 5 .   ? 8.496  9.840   24.827 0.51 27.72  ? 207 A1BQ0 A C10 1 
HETATM 1112 N  N   . A1BQ0 H 5 .   ? 10.197 10.217  23.015 0.51 25.74  ? 207 A1BQ0 A N   1 
HETATM 1113 C  C   . A1BQ0 H 5 .   ? 10.561 8.875   22.590 0.51 23.08  ? 207 A1BQ0 A C   1 
HETATM 1114 O  O   . A1BQ0 H 5 .   ? 10.512 14.713  23.402 0.51 30.82  ? 207 A1BQ0 A O   1 
HETATM 1115 C  C1  . A1BQ0 H 5 .   ? 10.317 12.372  23.064 0.51 27.13  ? 207 A1BQ0 A C1  1 
HETATM 1116 C  C11 . A1BQ0 H 5 .   ? 9.316  10.586  23.990 0.51 27.31  ? 207 A1BQ0 A C11 1 
HETATM 1117 C  C2  . A1BQ0 H 5 .   ? 10.746 13.756  22.671 0.51 28.42  ? 207 A1BQ0 A C2  1 
HETATM 1118 C  C3  . A1BQ0 H 5 .   ? 11.863 15.134  20.962 0.51 33.46  ? 207 A1BQ0 A C3  1 
HETATM 1119 C  C9  . A1BQ0 H 5 .   ? 7.734  10.505  25.778 0.51 28.88  ? 207 A1BQ0 A C9  1 
HETATM 1120 F  F   . A1BQ0 H 5 .   ? 7.098  12.525  26.810 0.51 30.59  ? 207 A1BQ0 A F   1 
HETATM 1121 N  N2  . A1BQ0 H 5 .   ? 11.376 13.862  21.495 0.51 33.08  ? 207 A1BQ0 A N2  1 
HETATM 1122 O  O   . HOH   I 6 .   ? 13.005 7.419   30.833 1.00 50.06  ? 301 HOH   A O   1 
HETATM 1123 O  O   . HOH   I 6 .   ? 18.337 -4.977  11.344 1.00 55.23  ? 302 HOH   A O   1 
HETATM 1124 O  O   . HOH   I 6 .   ? 23.706 -5.933  7.802  1.00 63.55  ? 303 HOH   A O   1 
HETATM 1125 O  O   . HOH   I 6 .   ? 21.022 2.654   -2.446 1.00 63.59  ? 304 HOH   A O   1 
HETATM 1126 O  O   . HOH   I 6 .   ? 18.093 20.646  26.234 1.00 70.54  ? 305 HOH   A O   1 
HETATM 1127 O  O   . HOH   I 6 .   ? 21.881 -5.324  22.013 1.00 52.95  ? 306 HOH   A O   1 
HETATM 1128 O  O   . HOH   I 6 .   ? 3.001  8.690   9.891  1.00 47.87  ? 307 HOH   A O   1 
HETATM 1129 O  O   . HOH   I 6 .   ? 16.152 23.637  14.533 1.00 67.04  ? 308 HOH   A O   1 
HETATM 1130 O  O   . HOH   I 6 .   ? 19.339 -0.172  26.969 1.00 48.42  ? 309 HOH   A O   1 
HETATM 1131 O  O   . HOH   I 6 .   ? 34.864 5.026   13.069 1.00 56.32  ? 310 HOH   A O   1 
HETATM 1132 O  O   . HOH   I 6 .   ? 8.098  -3.426  0.220  1.00 40.37  ? 311 HOH   A O   1 
HETATM 1133 O  O   . HOH   I 6 .   ? 4.104  -4.327  21.002 1.00 43.18  ? 312 HOH   A O   1 
HETATM 1134 O  O   . HOH   I 6 .   ? 20.331 9.182   18.773 1.00 34.11  ? 313 HOH   A O   1 
HETATM 1135 O  O   . HOH   I 6 .   ? 29.432 3.367   9.973  1.00 39.95  ? 314 HOH   A O   1 
HETATM 1136 O  O   . HOH   I 6 .   ? 27.594 3.834   2.559  1.00 54.03  ? 315 HOH   A O   1 
HETATM 1137 O  O   . HOH   I 6 .   ? 8.424  -8.285  23.268 1.00 44.77  ? 316 HOH   A O   1 
HETATM 1138 O  O   . HOH   I 6 .   ? 24.196 22.551  8.756  1.00 43.92  ? 317 HOH   A O   1 
HETATM 1139 O  O   . HOH   I 6 .   ? 14.957 11.704  0.779  1.00 42.85  ? 318 HOH   A O   1 
HETATM 1140 O  O   . HOH   I 6 .   ? 18.003 0.641   29.678 1.00 57.86  ? 319 HOH   A O   1 
HETATM 1141 O  O   . HOH   I 6 .   ? 18.583 5.037   26.489 1.00 49.91  ? 320 HOH   A O   1 
HETATM 1142 O  O   . HOH   I 6 .   ? 6.673  -4.909  28.721 1.00 45.71  ? 321 HOH   A O   1 
HETATM 1143 O  O   . HOH   I 6 .   ? 7.494  25.593  15.349 1.00 56.04  ? 322 HOH   A O   1 
HETATM 1144 O  O   . HOH   I 6 .   ? 6.186  3.204   3.251  1.00 46.90  ? 323 HOH   A O   1 
HETATM 1145 O  O   . HOH   I 6 .   ? 10.383 5.303   3.320  1.00 33.16  ? 324 HOH   A O   1 
HETATM 1146 O  O   . HOH   I 6 .   ? 10.610 8.883   4.527  1.00 38.04  ? 325 HOH   A O   1 
HETATM 1147 O  O   . HOH   I 6 .   ? 15.385 -3.030  17.273 1.00 44.94  ? 326 HOH   A O   1 
HETATM 1148 O  O   . HOH   I 6 .   ? -0.842 2.325   4.897  1.00 50.36  ? 327 HOH   A O   1 
HETATM 1149 O  O   . HOH   I 6 .   ? -3.630 26.056  13.368 1.00 66.18  ? 328 HOH   A O   1 
HETATM 1150 O  O   . HOH   I 6 .   ? 23.569 0.142   15.354 1.00 35.11  ? 329 HOH   A O   1 
HETATM 1151 O  O   . HOH   I 6 .   ? 15.088 2.749   22.962 1.00 31.39  ? 330 HOH   A O   1 
HETATM 1152 O  O   . HOH   I 6 .   ? 33.561 14.043  6.917  1.00 54.96  ? 331 HOH   A O   1 
HETATM 1153 O  O   . HOH   I 6 .   ? 18.694 19.721  5.266  1.00 50.45  ? 332 HOH   A O   1 
HETATM 1154 O  O   . HOH   I 6 .   ? 4.655  7.825   3.199  1.00 55.28  ? 333 HOH   A O   1 
HETATM 1155 O  O   . HOH   I 6 .   ? 6.894  13.705  21.425 0.51 36.15  ? 334 HOH   A O   1 
HETATM 1156 O  O   . HOH   I 6 .   ? 0.479  2.478   24.302 1.00 43.46  ? 335 HOH   A O   1 
HETATM 1157 O  O   . HOH   I 6 .   ? 17.490 20.461  19.444 1.00 53.41  ? 336 HOH   A O   1 
HETATM 1158 O  O   . HOH   I 6 .   ? 11.519 12.203  11.434 1.00 30.83  ? 337 HOH   A O   1 
HETATM 1159 O  O   . HOH   I 6 .   ? 3.649  21.762  22.846 1.00 49.55  ? 338 HOH   A O   1 
HETATM 1160 O  O   . HOH   I 6 .   ? 1.004  -1.950  19.999 1.00 43.49  ? 339 HOH   A O   1 
HETATM 1161 O  O   . HOH   I 6 .   ? 36.761 21.769  18.569 1.00 54.96  ? 340 HOH   A O   1 
HETATM 1162 O  O   . HOH   I 6 .   ? 20.975 -0.827  -1.972 1.00 54.60  ? 341 HOH   A O   1 
HETATM 1163 O  O   . HOH   I 6 .   ? 0.732  0.274   16.518 1.00 29.62  ? 342 HOH   A O   1 
HETATM 1164 O  O   . HOH   I 6 .   ? 8.988  3.190   2.712  1.00 31.23  ? 343 HOH   A O   1 
HETATM 1165 O  O   . HOH   I 6 .   ? 22.355 -0.503  3.648  1.00 39.65  ? 344 HOH   A O   1 
HETATM 1166 O  O   . HOH   I 6 .   ? 6.240  8.214   28.451 1.00 44.58  ? 345 HOH   A O   1 
HETATM 1167 O  O   . HOH   I 6 .   ? 30.477 11.359  18.027 1.00 60.01  ? 346 HOH   A O   1 
HETATM 1168 O  O   . HOH   I 6 .   ? 14.060 9.643   29.510 1.00 42.22  ? 347 HOH   A O   1 
HETATM 1169 O  O   . HOH   I 6 .   ? 30.732 -3.692  7.014  1.00 56.54  ? 348 HOH   A O   1 
HETATM 1170 O  O   . HOH   I 6 .   ? 6.069  2.287   6.094  1.00 35.74  ? 349 HOH   A O   1 
HETATM 1171 O  O   . HOH   I 6 .   ? 18.152 21.428  9.146  1.00 40.94  ? 350 HOH   A O   1 
HETATM 1172 O  O   . HOH   I 6 .   ? 10.363 4.869   33.527 1.00 42.98  ? 351 HOH   A O   1 
HETATM 1173 O  O   . HOH   I 6 .   ? -2.212 7.972   26.546 1.00 61.97  ? 352 HOH   A O   1 
HETATM 1174 O  O   . HOH   I 6 .   ? 7.557  4.031   32.858 1.00 42.30  ? 353 HOH   A O   1 
HETATM 1175 O  O   . HOH   I 6 .   ? 13.141 2.528   0.649  1.00 40.18  ? 354 HOH   A O   1 
HETATM 1176 O  O   . HOH   I 6 .   ? 18.177 2.764   22.912 1.00 35.34  ? 355 HOH   A O   1 
HETATM 1177 O  O   . HOH   I 6 .   ? 16.020 12.360  23.919 1.00 42.49  ? 356 HOH   A O   1 
HETATM 1178 O  O   . HOH   I 6 .   ? 4.222  -4.663  6.452  1.00 48.12  ? 357 HOH   A O   1 
HETATM 1179 O  O   . HOH   I 6 .   ? 28.181 -1.731  12.828 1.00 52.56  ? 358 HOH   A O   1 
HETATM 1180 O  O   . HOH   I 6 .   ? 14.352 14.998  3.688  1.00 42.61  ? 359 HOH   A O   1 
HETATM 1181 O  O   . HOH   I 6 .   ? 11.868 17.888  5.472  1.00 68.35  ? 360 HOH   A O   1 
HETATM 1182 O  O   . HOH   I 6 .   ? 8.469  19.454  18.290 0.51 25.66  ? 361 HOH   A O   1 
HETATM 1183 O  O   . HOH   I 6 .   ? 18.643 0.072   19.092 1.00 44.46  ? 362 HOH   A O   1 
HETATM 1184 O  O   . HOH   I 6 .   ? 9.585  18.167  20.257 1.00 41.65  ? 363 HOH   A O   1 
HETATM 1185 O  O   . HOH   I 6 .   ? 21.942 -4.391  12.251 1.00 43.92  ? 364 HOH   A O   1 
HETATM 1186 O  O   . HOH   I 6 .   ? 19.585 9.128   25.532 1.00 46.28  ? 365 HOH   A O   1 
HETATM 1187 O  O   . HOH   I 6 .   ? 6.769  16.888  24.544 0.51 42.00  ? 366 HOH   A O   1 
HETATM 1188 O  O   . HOH   I 6 .   ? 19.065 13.312  1.693  1.00 48.22  ? 367 HOH   A O   1 
HETATM 1189 O  O   . HOH   I 6 .   ? 20.973 -4.579  9.673  1.00 46.13  ? 368 HOH   A O   1 
HETATM 1190 O  O   . HOH   I 6 .   ? 12.895 -8.183  24.263 1.00 38.22  ? 369 HOH   A O   1 
HETATM 1191 O  O   . HOH   I 6 .   ? 3.296  4.307   27.531 1.00 51.28  ? 370 HOH   A O   1 
HETATM 1192 O  O   . HOH   I 6 .   ? 23.881 2.481   18.897 1.00 44.52  ? 371 HOH   A O   1 
HETATM 1193 O  O   . HOH   I 6 .   ? 3.925  1.246   30.601 1.00 56.74  ? 372 HOH   A O   1 
HETATM 1194 O  O   . HOH   I 6 .   ? 2.346  13.752  5.272  1.00 51.51  ? 373 HOH   A O   1 
HETATM 1195 O  O   . HOH   I 6 .   ? 14.264 -4.019  33.973 1.00 40.51  ? 374 HOH   A O   1 
HETATM 1196 O  O   . HOH   I 6 .   ? 3.632  15.133  20.309 1.00 48.14  ? 375 HOH   A O   1 
HETATM 1197 O  O   . HOH   I 6 .   ? 5.480  -1.018  24.107 1.00 37.04  ? 376 HOH   A O   1 
HETATM 1198 O  O   . HOH   I 6 .   ? 6.935  13.455  5.422  1.00 40.49  ? 377 HOH   A O   1 
HETATM 1199 O  O   . HOH   I 6 .   ? 0.236  4.547   6.568  1.00 43.06  ? 378 HOH   A O   1 
HETATM 1200 O  O   . HOH   I 6 .   ? -0.285 15.558  12.752 1.00 46.72  ? 379 HOH   A O   1 
HETATM 1201 O  O   . HOH   I 6 .   ? 18.476 19.049  16.974 1.00 34.11  ? 380 HOH   A O   1 
HETATM 1202 O  O   . HOH   I 6 .   ? 13.241 11.022  9.210  1.00 31.75  ? 381 HOH   A O   1 
HETATM 1203 O  O   . HOH   I 6 .   ? 4.273  -1.677  21.623 1.00 50.21  ? 382 HOH   A O   1 
HETATM 1204 O  O   . HOH   I 6 .   ? 1.343  -2.228  17.161 1.00 35.95  ? 383 HOH   A O   1 
HETATM 1205 O  O   . HOH   I 6 .   ? 20.604 2.089   18.285 1.00 47.66  ? 384 HOH   A O   1 
HETATM 1206 O  O   . HOH   I 6 .   ? 18.327 -2.767  18.452 1.00 55.93  ? 385 HOH   A O   1 
HETATM 1207 O  O   . HOH   I 6 .   ? 8.146  15.816  21.972 0.51 39.68  ? 386 HOH   A O   1 
HETATM 1208 O  O   . HOH   I 6 .   ? 0.380  12.751  21.240 1.00 63.13  ? 387 HOH   A O   1 
HETATM 1209 O  O   . HOH   I 6 .   ? 36.873 -0.416  9.057  1.00 57.67  ? 388 HOH   A O   1 
HETATM 1210 O  O   . HOH   I 6 .   ? 6.262  25.680  21.149 1.00 51.26  ? 389 HOH   A O   1 
HETATM 1211 O  O   . HOH   I 6 .   ? 22.330 8.907   20.783 1.00 48.98  ? 390 HOH   A O   1 
HETATM 1212 O  O   . HOH   I 6 .   ? 4.506  11.623  18.941 1.00 50.38  ? 391 HOH   A O   1 
HETATM 1213 O  O   . HOH   I 6 .   ? 6.634  -3.386  -1.813 1.00 57.66  ? 392 HOH   A O   1 
HETATM 1214 O  O   . HOH   I 6 .   ? 2.247  -6.296  18.447 1.00 62.95  ? 393 HOH   A O   1 
HETATM 1215 O  O   . HOH   I 6 .   ? 22.579 18.859  18.745 1.00 71.29  ? 394 HOH   A O   1 
HETATM 1216 O  O   . HOH   I 6 .   ? 31.324 2.876   11.939 1.00 50.24  ? 395 HOH   A O   1 
HETATM 1217 O  O   . HOH   I 6 .   ? 19.559 7.368   27.636 1.00 51.86  ? 396 HOH   A O   1 
HETATM 1218 O  O   . HOH   I 6 .   ? 6.295  23.413  11.537 1.00 49.33  ? 397 HOH   A O   1 
HETATM 1219 O  O   . HOH   I 6 .   ? 24.466 6.996   20.920 1.00 72.06  ? 398 HOH   A O   1 
HETATM 1220 O  O   . HOH   I 6 .   ? 22.653 19.098  5.447  1.00 43.08  ? 399 HOH   A O   1 
HETATM 1221 O  O   . HOH   I 6 .   ? 26.423 -1.946  14.354 1.00 58.86  ? 400 HOH   A O   1 
HETATM 1222 O  O   . HOH   I 6 .   ? 8.950  -7.334  8.094  1.00 54.52  ? 401 HOH   A O   1 
HETATM 1223 O  O   . HOH   I 6 .   ? 7.387  11.331  4.070  1.00 58.64  ? 402 HOH   A O   1 
HETATM 1224 O  O   . HOH   I 6 .   ? 17.919 9.446   -1.954 1.00 46.31  ? 403 HOH   A O   1 
HETATM 1225 O  O   . HOH   I 6 .   ? 9.476  9.226   31.754 1.00 55.89  ? 404 HOH   A O   1 
HETATM 1226 O  O   . HOH   I 6 .   ? 30.651 5.670   18.621 1.00 71.77  ? 405 HOH   A O   1 
HETATM 1227 O  O   . HOH   I 6 .   ? 14.898 -8.718  26.890 1.00 69.17  ? 406 HOH   A O   1 
HETATM 1228 O  O   . HOH   I 6 .   ? 2.367  -5.875  15.044 1.00 67.00  ? 407 HOH   A O   1 
HETATM 1229 O  O   . HOH   I 6 .   ? 9.380  24.666  24.280 0.51 49.89  ? 408 HOH   A O   1 
HETATM 1230 O  O   . HOH   I 6 .   ? 7.370  -4.849  2.567  1.00 43.29  ? 409 HOH   A O   1 
HETATM 1231 O  O   . HOH   I 6 .   ? 17.582 12.126  26.020 1.00 64.29  ? 410 HOH   A O   1 
HETATM 1232 O  O   . HOH   I 6 .   ? 17.673 11.342  0.062  1.00 58.52  ? 411 HOH   A O   1 
HETATM 1233 O  O   . HOH   I 6 .   ? 16.725 11.933  28.207 1.00 65.38  ? 412 HOH   A O   1 
HETATM 1234 O  O   . HOH   I 6 .   ? 4.232  -4.539  2.891  1.00 63.20  ? 413 HOH   A O   1 
HETATM 1235 O  O   . HOH   I 6 .   ? 8.015  -7.954  2.152  1.00 57.01  ? 414 HOH   A O   1 
HETATM 1236 O  O   . HOH   I 6 .   ? 2.279  2.277   26.782 1.00 44.97  ? 415 HOH   A O   1 
HETATM 1237 O  O   . HOH   I 6 .   ? 4.329  -1.554  26.550 1.00 53.52  ? 416 HOH   A O   1 
HETATM 1238 O  O   . HOH   I 6 .   ? 12.198 23.468  14.950 1.00 43.05  ? 417 HOH   A O   1 
HETATM 1239 O  O   . HOH   I 6 .   ? 20.500 14.779  0.091  1.00 54.60  ? 418 HOH   A O   1 
HETATM 1240 O  O   . HOH   I 6 .   ? 18.669 15.695  29.809 1.00 75.98  ? 419 HOH   A O   1 
HETATM 1241 O  O   . HOH   I 6 .   ? 24.817 20.350  20.252 1.00 63.27  ? 420 HOH   A O   1 
HETATM 1242 O  O   . HOH   I 6 .   ? 31.120 6.769   15.832 1.00 59.66  ? 421 HOH   A O   1 
HETATM 1243 O  O   . HOH   I 6 .   ? 5.691  -8.014  23.425 1.00 51.10  ? 422 HOH   A O   1 
HETATM 1244 O  O   . HOH   I 6 .   ? 2.373  14.460  22.457 1.00 53.84  ? 423 HOH   A O   1 
HETATM 1245 O  O   . HOH   I 6 .   ? 19.913 9.833   -3.471 1.00 53.62  ? 424 HOH   A O   1 
HETATM 1246 O  O   . HOH   I 6 .   ? 16.845 13.853  1.641  1.00 54.96  ? 425 HOH   A O   1 
HETATM 1247 O  O   . HOH   I 6 .   ? 8.449  7.696   2.584  1.00 48.34  ? 426 HOH   A O   1 
HETATM 1248 O  O   . HOH   I 6 .   ? 23.300 9.832   23.039 1.00 56.68  ? 427 HOH   A O   1 
HETATM 1249 O  O   . HOH   I 6 .   ? 0.078  12.798  18.324 0.51 42.39  ? 428 HOH   A O   1 
HETATM 1250 O  O   . HOH   I 6 .   ? 21.586 10.530  25.107 1.00 58.63  ? 429 HOH   A O   1 
HETATM 1251 O  O   . HOH   I 6 .   ? 13.340 11.842  30.557 1.00 55.34  ? 430 HOH   A O   1 
HETATM 1252 O  O   . HOH   I 6 .   ? -5.094 25.000  10.262 1.00 62.67  ? 431 HOH   A O   1 
HETATM 1253 O  O   . HOH   I 6 .   ? 4.093  -6.127  23.021 1.00 57.22  ? 432 HOH   A O   1 
HETATM 1254 O  O   . HOH   I 6 .   ? 32.213 4.750   14.269 1.00 60.33  ? 433 HOH   A O   1 
HETATM 1255 O  O   . HOH   I 6 .   ? 20.938 12.519  26.633 1.00 62.50  ? 434 HOH   A O   1 
HETATM 1256 O  O   . HOH   I 6 .   ? -3.087 21.407  25.025 1.00 73.69  ? 435 HOH   A O   1 
HETATM 1257 O  O   . HOH   I 6 .   ? 21.591 11.885  -3.341 1.00 55.22  ? 436 HOH   A O   1 
HETATM 1258 O  O   . HOH   I 6 .   ? 5.337  23.062  8.541  1.00 58.70  ? 437 HOH   A O   1 
# 
