data_7HYB
# 
_entry.id   7HYB 
# 
_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   7HYB         pdb_00007hyb 10.2210/pdb7hyb/pdb 
WWPDB D_1001408083 ?            ?                   
# 
_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       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_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                        7HYB 
_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   2025-01-10 
_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 '(3S)-1-[(2-methoxypyridin-3-yl)acetyl]piperidine-3-carboxamide' 277.319   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                       65.409    1   ?         ? ? ? 
4 water       nat water                                                            18.015    168 ?         ? ? ? 
# 
_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 '(3S)-1-[(2-methoxypyridin-3-yl)acetyl]piperidine-3-carboxamide' A1BOY 
3 'ZINC ION'                                                       ZN    
4 water                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BOY non-polymer         . '(3S)-1-[(2-methoxypyridin-3-yl)acetyl]piperidine-3-carboxamide' ? 'C14 H19 N3 O3'  277.319 
ALA   'L-peptide linking' y ALANINE                                                          ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                         ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                       ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                  ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                         ? 'C3 H7 N O2 S'   121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                        ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                  ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                          ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                        ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                            ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                       ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                          ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                           ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                       ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                    ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                          ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                           ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                        ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                       ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                         ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                           ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                       ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BOY 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOY 
_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 A1BOY 1   201 201 A1BOY LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 HOH   1   301 139 HOH   HOH A . 
D 4 HOH   2   302 110 HOH   HOH A . 
D 4 HOH   3   303 108 HOH   HOH A . 
D 4 HOH   4   304 131 HOH   HOH A . 
D 4 HOH   5   305 81  HOH   HOH A . 
D 4 HOH   6   306 129 HOH   HOH A . 
D 4 HOH   7   307 9   HOH   HOH A . 
D 4 HOH   8   308 18  HOH   HOH A . 
D 4 HOH   9   309 2   HOH   HOH A . 
D 4 HOH   10  310 12  HOH   HOH A . 
D 4 HOH   11  311 16  HOH   HOH A . 
D 4 HOH   12  312 113 HOH   HOH A . 
D 4 HOH   13  313 37  HOH   HOH A . 
D 4 HOH   14  314 85  HOH   HOH A . 
D 4 HOH   15  315 174 HOH   HOH A . 
D 4 HOH   16  316 149 HOH   HOH A . 
D 4 HOH   17  317 141 HOH   HOH A . 
D 4 HOH   18  318 59  HOH   HOH A . 
D 4 HOH   19  319 175 HOH   HOH A . 
D 4 HOH   20  320 82  HOH   HOH A . 
D 4 HOH   21  321 60  HOH   HOH A . 
D 4 HOH   22  322 88  HOH   HOH A . 
D 4 HOH   23  323 48  HOH   HOH A . 
D 4 HOH   24  324 27  HOH   HOH A . 
D 4 HOH   25  325 87  HOH   HOH A . 
D 4 HOH   26  326 79  HOH   HOH A . 
D 4 HOH   27  327 130 HOH   HOH A . 
D 4 HOH   28  328 50  HOH   HOH A . 
D 4 HOH   29  329 148 HOH   HOH A . 
D 4 HOH   30  330 8   HOH   HOH A . 
D 4 HOH   31  331 24  HOH   HOH A . 
D 4 HOH   32  332 32  HOH   HOH A . 
D 4 HOH   33  333 75  HOH   HOH A . 
D 4 HOH   34  334 7   HOH   HOH A . 
D 4 HOH   35  335 72  HOH   HOH A . 
D 4 HOH   36  336 17  HOH   HOH A . 
D 4 HOH   37  337 152 HOH   HOH A . 
D 4 HOH   38  338 73  HOH   HOH A . 
D 4 HOH   39  339 124 HOH   HOH A . 
D 4 HOH   40  340 150 HOH   HOH A . 
D 4 HOH   41  341 34  HOH   HOH A . 
D 4 HOH   42  342 109 HOH   HOH A . 
D 4 HOH   43  343 123 HOH   HOH A . 
D 4 HOH   44  344 96  HOH   HOH A . 
D 4 HOH   45  345 14  HOH   HOH A . 
D 4 HOH   46  346 40  HOH   HOH A . 
D 4 HOH   47  347 106 HOH   HOH A . 
D 4 HOH   48  348 36  HOH   HOH A . 
D 4 HOH   49  349 21  HOH   HOH A . 
D 4 HOH   50  350 71  HOH   HOH A . 
D 4 HOH   51  351 45  HOH   HOH A . 
D 4 HOH   52  352 51  HOH   HOH A . 
D 4 HOH   53  353 23  HOH   HOH A . 
D 4 HOH   54  354 3   HOH   HOH A . 
D 4 HOH   55  355 22  HOH   HOH A . 
D 4 HOH   56  356 84  HOH   HOH A . 
D 4 HOH   57  357 58  HOH   HOH A . 
D 4 HOH   58  358 76  HOH   HOH A . 
D 4 HOH   59  359 57  HOH   HOH A . 
D 4 HOH   60  360 42  HOH   HOH A . 
D 4 HOH   61  361 93  HOH   HOH A . 
D 4 HOH   62  362 134 HOH   HOH A . 
D 4 HOH   63  363 19  HOH   HOH A . 
D 4 HOH   64  364 77  HOH   HOH A . 
D 4 HOH   65  365 86  HOH   HOH A . 
D 4 HOH   66  366 25  HOH   HOH A . 
D 4 HOH   67  367 47  HOH   HOH A . 
D 4 HOH   68  368 132 HOH   HOH A . 
D 4 HOH   69  369 55  HOH   HOH A . 
D 4 HOH   70  370 4   HOH   HOH A . 
D 4 HOH   71  371 167 HOH   HOH A . 
D 4 HOH   72  372 10  HOH   HOH A . 
D 4 HOH   73  373 153 HOH   HOH A . 
D 4 HOH   74  374 92  HOH   HOH A . 
D 4 HOH   75  375 11  HOH   HOH A . 
D 4 HOH   76  376 137 HOH   HOH A . 
D 4 HOH   77  377 30  HOH   HOH A . 
D 4 HOH   78  378 13  HOH   HOH A . 
D 4 HOH   79  379 119 HOH   HOH A . 
D 4 HOH   80  380 56  HOH   HOH A . 
D 4 HOH   81  381 105 HOH   HOH A . 
D 4 HOH   82  382 170 HOH   HOH A . 
D 4 HOH   83  383 157 HOH   HOH A . 
D 4 HOH   84  384 46  HOH   HOH A . 
D 4 HOH   85  385 169 HOH   HOH A . 
D 4 HOH   86  386 143 HOH   HOH A . 
D 4 HOH   87  387 80  HOH   HOH A . 
D 4 HOH   88  388 162 HOH   HOH A . 
D 4 HOH   89  389 74  HOH   HOH A . 
D 4 HOH   90  390 83  HOH   HOH A . 
D 4 HOH   91  391 49  HOH   HOH A . 
D 4 HOH   92  392 142 HOH   HOH A . 
D 4 HOH   93  393 67  HOH   HOH A . 
D 4 HOH   94  394 95  HOH   HOH A . 
D 4 HOH   95  395 111 HOH   HOH A . 
D 4 HOH   96  396 53  HOH   HOH A . 
D 4 HOH   97  397 166 HOH   HOH A . 
D 4 HOH   98  398 54  HOH   HOH A . 
D 4 HOH   99  399 115 HOH   HOH A . 
D 4 HOH   100 400 28  HOH   HOH A . 
D 4 HOH   101 401 15  HOH   HOH A . 
D 4 HOH   102 402 5   HOH   HOH A . 
D 4 HOH   103 403 20  HOH   HOH A . 
D 4 HOH   104 404 70  HOH   HOH A . 
D 4 HOH   105 405 94  HOH   HOH A . 
D 4 HOH   106 406 116 HOH   HOH A . 
D 4 HOH   107 407 6   HOH   HOH A . 
D 4 HOH   108 408 29  HOH   HOH A . 
D 4 HOH   109 409 39  HOH   HOH A . 
D 4 HOH   110 410 89  HOH   HOH A . 
D 4 HOH   111 411 35  HOH   HOH A . 
D 4 HOH   112 412 99  HOH   HOH A . 
D 4 HOH   113 413 68  HOH   HOH A . 
D 4 HOH   114 414 41  HOH   HOH A . 
D 4 HOH   115 415 120 HOH   HOH A . 
D 4 HOH   116 416 38  HOH   HOH A . 
D 4 HOH   117 417 97  HOH   HOH A . 
D 4 HOH   118 418 140 HOH   HOH A . 
D 4 HOH   119 419 154 HOH   HOH A . 
D 4 HOH   120 420 136 HOH   HOH A . 
D 4 HOH   121 421 64  HOH   HOH A . 
D 4 HOH   122 422 26  HOH   HOH A . 
D 4 HOH   123 423 63  HOH   HOH A . 
D 4 HOH   124 424 114 HOH   HOH A . 
D 4 HOH   125 425 98  HOH   HOH A . 
D 4 HOH   126 426 163 HOH   HOH A . 
D 4 HOH   127 427 133 HOH   HOH A . 
D 4 HOH   128 428 146 HOH   HOH A . 
D 4 HOH   129 429 33  HOH   HOH A . 
D 4 HOH   130 430 145 HOH   HOH A . 
D 4 HOH   131 431 31  HOH   HOH A . 
D 4 HOH   132 432 161 HOH   HOH A . 
D 4 HOH   133 433 107 HOH   HOH A . 
D 4 HOH   134 434 138 HOH   HOH A . 
D 4 HOH   135 435 66  HOH   HOH A . 
D 4 HOH   136 436 125 HOH   HOH A . 
D 4 HOH   137 437 103 HOH   HOH A . 
D 4 HOH   138 438 156 HOH   HOH A . 
D 4 HOH   139 439 122 HOH   HOH A . 
D 4 HOH   140 440 78  HOH   HOH A . 
D 4 HOH   141 441 61  HOH   HOH A . 
D 4 HOH   142 442 164 HOH   HOH A . 
D 4 HOH   143 443 65  HOH   HOH A . 
D 4 HOH   144 444 168 HOH   HOH A . 
D 4 HOH   145 445 52  HOH   HOH A . 
D 4 HOH   146 446 151 HOH   HOH A . 
D 4 HOH   147 447 112 HOH   HOH A . 
D 4 HOH   148 448 172 HOH   HOH A . 
D 4 HOH   149 449 43  HOH   HOH A . 
D 4 HOH   150 450 118 HOH   HOH A . 
D 4 HOH   151 451 102 HOH   HOH A . 
D 4 HOH   152 452 44  HOH   HOH A . 
D 4 HOH   153 453 101 HOH   HOH A . 
D 4 HOH   154 454 91  HOH   HOH A . 
D 4 HOH   155 455 69  HOH   HOH A . 
D 4 HOH   156 456 155 HOH   HOH A . 
D 4 HOH   157 457 121 HOH   HOH A . 
D 4 HOH   158 458 171 HOH   HOH A . 
D 4 HOH   159 459 90  HOH   HOH A . 
D 4 HOH   160 460 128 HOH   HOH A . 
D 4 HOH   161 461 158 HOH   HOH A . 
D 4 HOH   162 462 62  HOH   HOH A . 
D 4 HOH   163 463 173 HOH   HOH A . 
D 4 HOH   164 464 127 HOH   HOH A . 
D 4 HOH   165 465 104 HOH   HOH A . 
D 4 HOH   166 466 159 HOH   HOH A . 
D 4 HOH   167 467 165 HOH   HOH A . 
D 4 HOH   168 468 160 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HYB 
_cell.length_a           73.821 
_cell.length_b           61.463 
_cell.length_c           32.876 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.50 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HYB 
_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          7HYB 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.34 
_exptl_crystal.density_percent_sol   47.53 
_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   2024-12-02 
_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   0.92203 
_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        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HYB 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.26 
_reflns.d_resolution_high            1.57 
_reflns.number_obs                   20381 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            0.218 
_reflns.pdbx_netI_over_sigmaI        3.9 
_reflns.pdbx_redundancy              6.5 
_reflns.pdbx_Rrim_I_all              0.238 
_reflns.pdbx_Rpim_I_all              0.092 
_reflns.pdbx_CC_half                 0.987 
_reflns.pdbx_number_measured_all     131628 
_reflns.pdbx_chi_squared             0.35 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.57 
_reflns_shell.d_res_low                   1.60 
_reflns_shell.number_measured_all         5067 
_reflns_shell.number_unique_obs           893 
_reflns_shell.Rmerge_I_obs                3.901 
_reflns_shell.pdbx_chi_squared            0.06 
_reflns_shell.pdbx_redundancy             5.7 
_reflns_shell.percent_possible_obs        86.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             4.312 
_reflns_shell.pdbx_Rpim_I_all             1.809 
_reflns_shell.pdbx_CC_half                0.204 
_reflns_shell.percent_possible_all        ? 
_reflns_shell.pdbx_Rsym_value             ? 
_reflns_shell.meanI_over_sigI_obs         ? 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 7HYB 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     15643 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             19.43 
_refine.ls_d_res_high                            1.574 
_refine.ls_percent_reflns_obs                    76.7 
_refine.ls_R_factor_obs                          0.2428 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2399 
_refine.ls_R_factor_R_free                       0.2979 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.900 
_refine.ls_number_reflns_R_free                  767 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.935 
_refine.correlation_coeff_Fo_to_Fc_free          0.897 
_refine.B_iso_mean                               33.45 
_refine.aniso_B[1][1]                            -2.29940 
_refine.aniso_B[2][2]                            -6.39620 
_refine.aniso_B[3][3]                            8.69560 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            8.28480 
_refine.aniso_B[2][3]                            0.00000 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             ? 
_refine.overall_SU_R_Cruickshank_DPI             0.143 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.145 
_refine.pdbx_overall_SU_R_Blow_DPI               0.154 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.152 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HYB 
_refine_analyze.Luzzati_coordinate_error_obs    0.30 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         21 
_refine_hist.number_atoms_solvent             171 
_refine_hist.number_atoms_total               1266 
_refine_hist.d_res_high                       1.574 
_refine_hist.d_res_low                        19.43 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1125 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.04  ? 2.00  1531 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  377  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1125 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.77  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.89 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1089 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   39 
_refine_ls_shell.d_res_high                       1.57 
_refine_ls_shell.d_res_low                        1.69 
_refine_ls_shell.number_reflns_R_work             395 
_refine_ls_shell.R_factor_R_work                  0.5027 
_refine_ls_shell.percent_reflns_obs               10.85 
_refine_ls_shell.R_factor_R_free                  0.5340 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.13 
_refine_ls_shell.number_reflns_R_free             17 
_refine_ls_shell.number_reflns_all                412 
_refine_ls_shell.R_factor_all                     0.5041 
# 
_struct.entry_id                  7HYB 
_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-0035376-001 (A71EV2A-x4347)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HYB 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HYB 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 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 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.410 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.316 ? ? 
# 
_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 ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 103.3 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 110.1 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 122.3 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.7 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 91.0  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 119.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? 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 GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
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 ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HYB 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 368 ? ? O A HOH 403 ? ? 1.90 
2 1 O A HOH 359 ? ? O A HOH 434 ? ? 2.05 
3 1 O A HOH 330 ? ? O A HOH 368 ? ? 2.13 
4 1 O A HOH 362 ? ? O A HOH 365 ? ? 2.14 
5 1 O A HIS 104 ? ? O A HOH 301 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 403 ? ? 1_555 O A HOH 449 ? ? 2_556 2.06 
2 1 O A HOH 329 ? ? 1_555 O A HOH 398 ? ? 2_556 2.09 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.4657 
_pdbx_refine_tls.origin_y         6.5712 
_pdbx_refine_tls.origin_z         14.3369 
_pdbx_refine_tls.T[1][1]          -0.0091 
_pdbx_refine_tls.T[2][2]          -0.0689 
_pdbx_refine_tls.T[3][3]          0.0359 
_pdbx_refine_tls.T[1][2]          -0.0179 
_pdbx_refine_tls.T[1][3]          0.1454 
_pdbx_refine_tls.T[2][3]          -0.0118 
_pdbx_refine_tls.L[1][1]          1.2792 
_pdbx_refine_tls.L[2][2]          1.6901 
_pdbx_refine_tls.L[3][3]          0.8704 
_pdbx_refine_tls.L[1][2]          0.9218 
_pdbx_refine_tls.L[1][3]          -0.3622 
_pdbx_refine_tls.L[2][3]          -0.6262 
_pdbx_refine_tls.S[1][1]          -0.0645 
_pdbx_refine_tls.S[1][2]          0.0438 
_pdbx_refine_tls.S[1][3]          0.0653 
_pdbx_refine_tls.S[2][1]          0.0104 
_pdbx_refine_tls.S[2][2]          0.0407 
_pdbx_refine_tls.S[2][3]          -0.0718 
_pdbx_refine_tls.S[3][1]          0.0362 
_pdbx_refine_tls.S[3][2]          -0.0481 
_pdbx_refine_tls.S[3][3]          0.0238 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       468 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.14 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
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 
A1BOY N1   N  N N 1   
A1BOY C4   C  Y N 2   
A1BOY C5   C  Y N 3   
A1BOY C6   C  N N 4   
A1BOY C7   C  N N 5   
A1BOY C8   C  N N 6   
A1BOY C10  C  N N 7   
A1BOY C13  C  N N 8   
A1BOY O2   O  N N 9   
A1BOY C12  C  N N 10  
A1BOY N2   N  N N 11  
A1BOY C11  C  N S 12  
A1BOY C9   C  N N 13  
A1BOY O1   O  N N 14  
A1BOY C1   C  Y N 15  
A1BOY O    O  N N 16  
A1BOY C    C  N N 17  
A1BOY C3   C  Y N 18  
A1BOY C2   C  Y N 19  
A1BOY N    N  Y N 20  
A1BOY H6   H  N N 21  
A1BOY H8   H  N N 22  
A1BOY H7   H  N N 23  
A1BOY H9   H  N N 24  
A1BOY H10  H  N N 25  
A1BOY H13  H  N N 26  
A1BOY H14  H  N N 27  
A1BOY H17  H  N N 28  
A1BOY H18  H  N N 29  
A1BOY H16  H  N N 30  
A1BOY H15  H  N N 31  
A1BOY H    H  N N 32  
A1BOY H11  H  N N 33  
A1BOY H12  H  N N 34  
A1BOY H3   H  N N 35  
A1BOY H2   H  N N 36  
A1BOY H1   H  N N 37  
A1BOY H5   H  N N 38  
A1BOY H4   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  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 
THR   N    N  N N 343 
THR   CA   C  N S 344 
THR   C    C  N N 345 
THR   O    O  N N 346 
THR   CB   C  N R 347 
THR   OG1  O  N N 348 
THR   CG2  C  N N 349 
THR   OXT  O  N N 350 
THR   H    H  N N 351 
THR   H2   H  N N 352 
THR   HA   H  N N 353 
THR   HB   H  N N 354 
THR   HG1  H  N N 355 
THR   HG21 H  N N 356 
THR   HG22 H  N N 357 
THR   HG23 H  N N 358 
THR   HXT  H  N N 359 
TRP   N    N  N N 360 
TRP   CA   C  N S 361 
TRP   C    C  N N 362 
TRP   O    O  N N 363 
TRP   CB   C  N N 364 
TRP   CG   C  Y N 365 
TRP   CD1  C  Y N 366 
TRP   CD2  C  Y N 367 
TRP   NE1  N  Y N 368 
TRP   CE2  C  Y N 369 
TRP   CE3  C  Y N 370 
TRP   CZ2  C  Y N 371 
TRP   CZ3  C  Y N 372 
TRP   CH2  C  Y N 373 
TRP   OXT  O  N N 374 
TRP   H    H  N N 375 
TRP   H2   H  N N 376 
TRP   HA   H  N N 377 
TRP   HB2  H  N N 378 
TRP   HB3  H  N N 379 
TRP   HD1  H  N N 380 
TRP   HE1  H  N N 381 
TRP   HE3  H  N N 382 
TRP   HZ2  H  N N 383 
TRP   HZ3  H  N N 384 
TRP   HH2  H  N N 385 
TRP   HXT  H  N N 386 
TYR   N    N  N N 387 
TYR   CA   C  N S 388 
TYR   C    C  N N 389 
TYR   O    O  N N 390 
TYR   CB   C  N N 391 
TYR   CG   C  Y N 392 
TYR   CD1  C  Y N 393 
TYR   CD2  C  Y N 394 
TYR   CE1  C  Y N 395 
TYR   CE2  C  Y N 396 
TYR   CZ   C  Y N 397 
TYR   OH   O  N N 398 
TYR   OXT  O  N N 399 
TYR   H    H  N N 400 
TYR   H2   H  N N 401 
TYR   HA   H  N N 402 
TYR   HB2  H  N N 403 
TYR   HB3  H  N N 404 
TYR   HD1  H  N N 405 
TYR   HD2  H  N N 406 
TYR   HE1  H  N N 407 
TYR   HE2  H  N N 408 
TYR   HH   H  N N 409 
TYR   HXT  H  N N 410 
VAL   N    N  N N 411 
VAL   CA   C  N S 412 
VAL   C    C  N N 413 
VAL   O    O  N N 414 
VAL   CB   C  N N 415 
VAL   CG1  C  N N 416 
VAL   CG2  C  N N 417 
VAL   OXT  O  N N 418 
VAL   H    H  N N 419 
VAL   H2   H  N N 420 
VAL   HA   H  N N 421 
VAL   HB   H  N N 422 
VAL   HG11 H  N N 423 
VAL   HG12 H  N N 424 
VAL   HG13 H  N N 425 
VAL   HG21 H  N N 426 
VAL   HG22 H  N N 427 
VAL   HG23 H  N N 428 
VAL   HXT  H  N N 429 
ZN    ZN   ZN N N 430 
# 
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 
A1BOY C   O    sing N N 1   
A1BOY O   C1   sing N N 2   
A1BOY C1  N    doub Y N 3   
A1BOY N   C2   sing Y N 4   
A1BOY C2  C3   doub Y N 5   
A1BOY C3  C4   sing Y N 6   
A1BOY C4  C5   doub Y N 7   
A1BOY C1  C5   sing Y N 8   
A1BOY C5  C6   sing N N 9   
A1BOY C6  C7   sing N N 10  
A1BOY O1  C7   doub N N 11  
A1BOY C7  N1   sing N N 12  
A1BOY N1  C8   sing N N 13  
A1BOY C8  C9   sing N N 14  
A1BOY C9  C10  sing N N 15  
A1BOY C10 C11  sing N N 16  
A1BOY C11 C12  sing N N 17  
A1BOY N2  C12  sing N N 18  
A1BOY C12 O2   doub N N 19  
A1BOY C13 C11  sing N N 20  
A1BOY N1  C13  sing N N 21  
A1BOY C4  H6   sing N N 22  
A1BOY C6  H8   sing N N 23  
A1BOY C6  H7   sing N N 24  
A1BOY C8  H9   sing N N 25  
A1BOY C8  H10  sing N N 26  
A1BOY C10 H13  sing N N 27  
A1BOY C10 H14  sing N N 28  
A1BOY C13 H17  sing N N 29  
A1BOY C13 H18  sing N N 30  
A1BOY N2  H16  sing N N 31  
A1BOY N2  H15  sing N N 32  
A1BOY C11 H    sing N N 33  
A1BOY C9  H11  sing N N 34  
A1BOY C9  H12  sing N N 35  
A1BOY C   H3   sing N N 36  
A1BOY C   H2   sing N N 37  
A1BOY C   H1   sing N N 38  
A1BOY C3  H5   sing N N 39  
A1BOY C2  H4   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  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 
THR   N   CA   sing N N 330 
THR   N   H    sing N N 331 
THR   N   H2   sing N N 332 
THR   CA  C    sing N N 333 
THR   CA  CB   sing N N 334 
THR   CA  HA   sing N N 335 
THR   C   O    doub N N 336 
THR   C   OXT  sing N N 337 
THR   CB  OG1  sing N N 338 
THR   CB  CG2  sing N N 339 
THR   CB  HB   sing N N 340 
THR   OG1 HG1  sing N N 341 
THR   CG2 HG21 sing N N 342 
THR   CG2 HG22 sing N N 343 
THR   CG2 HG23 sing N N 344 
THR   OXT HXT  sing N N 345 
TRP   N   CA   sing N N 346 
TRP   N   H    sing N N 347 
TRP   N   H2   sing N N 348 
TRP   CA  C    sing N N 349 
TRP   CA  CB   sing N N 350 
TRP   CA  HA   sing N N 351 
TRP   C   O    doub N N 352 
TRP   C   OXT  sing N N 353 
TRP   CB  CG   sing N N 354 
TRP   CB  HB2  sing N N 355 
TRP   CB  HB3  sing N N 356 
TRP   CG  CD1  doub Y N 357 
TRP   CG  CD2  sing Y N 358 
TRP   CD1 NE1  sing Y N 359 
TRP   CD1 HD1  sing N N 360 
TRP   CD2 CE2  doub Y N 361 
TRP   CD2 CE3  sing Y N 362 
TRP   NE1 CE2  sing Y N 363 
TRP   NE1 HE1  sing N N 364 
TRP   CE2 CZ2  sing Y N 365 
TRP   CE3 CZ3  doub Y N 366 
TRP   CE3 HE3  sing N N 367 
TRP   CZ2 CH2  doub Y N 368 
TRP   CZ2 HZ2  sing N N 369 
TRP   CZ3 CH2  sing Y N 370 
TRP   CZ3 HZ3  sing N N 371 
TRP   CH2 HH2  sing N N 372 
TRP   OXT HXT  sing N N 373 
TYR   N   CA   sing N N 374 
TYR   N   H    sing N N 375 
TYR   N   H2   sing N N 376 
TYR   CA  C    sing N N 377 
TYR   CA  CB   sing N N 378 
TYR   CA  HA   sing N N 379 
TYR   C   O    doub N N 380 
TYR   C   OXT  sing N N 381 
TYR   CB  CG   sing N N 382 
TYR   CB  HB2  sing N N 383 
TYR   CB  HB3  sing N N 384 
TYR   CG  CD1  doub Y N 385 
TYR   CG  CD2  sing Y N 386 
TYR   CD1 CE1  sing Y N 387 
TYR   CD1 HD1  sing N N 388 
TYR   CD2 CE2  doub Y N 389 
TYR   CD2 HD2  sing N N 390 
TYR   CE1 CZ   doub Y N 391 
TYR   CE1 HE1  sing N N 392 
TYR   CE2 CZ   sing Y N 393 
TYR   CE2 HE2  sing N N 394 
TYR   CZ  OH   sing N N 395 
TYR   OH  HH   sing N N 396 
TYR   OXT HXT  sing N N 397 
VAL   N   CA   sing N N 398 
VAL   N   H    sing N N 399 
VAL   N   H2   sing N N 400 
VAL   CA  C    sing N N 401 
VAL   CA  CB   sing N N 402 
VAL   CA  HA   sing N N 403 
VAL   C   O    doub N N 404 
VAL   C   OXT  sing N N 405 
VAL   CB  CG1  sing N N 406 
VAL   CB  CG2  sing N N 407 
VAL   CB  HB   sing N N 408 
VAL   CG1 HG11 sing N N 409 
VAL   CG1 HG12 sing N N 410 
VAL   CG1 HG13 sing N N 411 
VAL   CG2 HG21 sing N N 412 
VAL   CG2 HG22 sing N N 413 
VAL   CG2 HG23 sing N N 414 
VAL   OXT HXT  sing N N 415 
# 
_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_1002329 
_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.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HYB 
_atom_sites.fract_transf_matrix[1][1]   0.013546 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000591 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016270 
_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]   0.030446 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.435 5.849   24.312 1.00 30.27  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.517 6.075   23.363 1.00 31.33  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.609 4.904   22.340 1.00 30.40  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.922 3.893   22.485 1.00 29.77  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.827 6.269   24.124 1.00 34.00  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.003 5.207   25.045 1.00 37.44  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.430 5.064   21.312 1.00 29.52  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.593 4.030   20.302 1.00 28.70  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.917 4.587   18.932 1.00 27.84  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.480 5.685   18.578 1.00 27.80  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.676 3.828   18.147 1.00 27.27  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 23.051 4.257   16.799 1.00 27.85  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.971 3.107   15.788 1.00 27.28  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.935 1.954   16.193 1.00 26.50  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.482 4.806   16.823 1.00 28.29  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.968 3.417   14.475 1.00 27.62  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.046 2.393   13.425 1.00 27.59  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.437 2.554   12.791 1.00 28.16  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.821 3.655   12.390 1.00 28.55  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.926 2.494   12.356 1.00 27.72  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.510 2.479   12.953 1.00 27.85  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.078 1.381   11.313 1.00 28.47  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.547 3.435   12.213 1.00 27.61  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.200 1.464   12.724 1.00 28.58  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.532 1.467   12.159 1.00 28.82  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.520 0.756   10.796 1.00 29.52  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.250 -0.441  10.742 1.00 28.71  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.505 0.833   13.161 1.00 28.47  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.691 1.711   14.377 1.00 28.41  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.482 2.850   14.323 1.00 29.21  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 27.030 1.438   15.563 1.00 29.53  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.639 3.672   15.433 1.00 30.05  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.181 2.249   16.679 1.00 30.43  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.986 3.366   16.610 1.00 31.31  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.124 4.158   17.717 1.00 33.63  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.736 1.518   9.685  1.00 29.93  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.686 0.999   8.299  1.00 30.35  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.752 1.637   7.413  1.00 31.83  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.737 2.861   7.218  1.00 31.96  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.268 1.119   7.669  1.00 30.80  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.695 2.527   7.798  1.00 30.51  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.266 0.665   6.220  1.00 31.37  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.687 0.819   6.879  1.00 31.78  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.782 1.315   6.046  1.00 32.06  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.638 2.257   6.872  1.00 31.95  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.895 1.940   8.029  1.00 32.62  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.981 3.449   6.367  1.00 31.23  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.697 4.422   7.209  1.00 32.06  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.718 5.496   7.739  1.00 31.92  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 31.081 6.672   7.837  1.00 31.76  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.879 5.042   6.498  1.00 34.23  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.919 4.008   6.145  1.00 40.45  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.661 3.496   7.003  1.00 42.89  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.980 3.668   4.873  1.00 41.79  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.472 5.076   8.061  1.00 31.16  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.439 5.976   8.564  1.00 30.86  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.898 5.536   9.959  1.00 30.37  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.842 4.346   10.257 1.00 29.67  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.276 6.073   7.562  1.00 31.21  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.617 6.699   6.230  1.00 32.80  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.157 7.978   6.157  1.00 34.08  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.323 6.050   5.037  1.00 33.69  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.431 8.578   4.930  1.00 34.89  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.546 6.657   3.809  1.00 34.34  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.127 7.912   3.758  1.00 35.71  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.373 8.514   2.545  1.00 36.54  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.529 6.522   10.810 1.00 28.90  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.932 6.317   12.122 1.00 27.64  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.630 7.147   12.099 1.00 27.42  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.681 8.335   11.809 1.00 27.93  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.885 6.772   13.237 1.00 27.46  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.194 7.071   14.582 1.00 29.30  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.210 7.276   15.704 1.00 31.12  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.818 8.343   16.626 1.00 32.80  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.296 8.143   17.833 1.00 33.17  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.063 6.908   18.268 1.00 30.12  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.958 9.179   18.598 1.00 32.25  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.472 6.521   12.322 1.00 27.19  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.183 7.244   12.310 1.00 26.72  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.650 7.364   13.742 1.00 26.97  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.471 6.354   14.401 1.00 26.38  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.142 6.568   11.400 1.00 27.09  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.937 7.498   11.173 1.00 27.16  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.757 6.150   10.067 1.00 27.13  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.388 8.580   14.222 1.00 26.66  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.895 8.779   15.588 1.00 26.63  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.668 9.718   15.560 1.00 26.41  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.409 10.404  14.560 1.00 26.13  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.995 9.419   16.507 1.00 27.34  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.955 8.380   17.046 1.00 28.26  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.716 10.571  15.811 1.00 27.73  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.979 9.847   16.712 1.00 24.93  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.957 10.877  16.888 1.00 25.37  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.727 12.222  16.826 1.00 26.34  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.847 12.297  17.351 1.00 26.53  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.285 10.716  18.260 1.00 25.15  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.340 9.537   18.292 1.00 27.08  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.696 8.448   18.724 1.00 27.92  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.121 9.708   17.787 1.00 27.58  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.212 13.197  16.062 1.00 26.21  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.839 14.507  15.948 1.00 26.39  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.901 15.202  17.307 1.00 26.37  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.862 15.908  17.571 1.00 26.05  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.077 15.394  14.951 1.00 26.31  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.881 16.594  14.428 1.00 26.15  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.931 17.598  13.810 1.00 27.30  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.548 18.815  13.280 1.00 28.43  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.741 19.932  13.980 1.00 29.83  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.487 19.959  15.286 1.00 26.56  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.226 21.020  13.387 1.00 30.17  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.890 14.994  18.183 1.00 26.00  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.879 15.628  19.525 1.00 26.72  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.906 15.022  20.495 1.00 26.92  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.178 15.592  21.559 1.00 27.89  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.460 15.658  20.148 1.00 27.77  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.931 14.353  20.673 1.00 28.32  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.296 13.459  19.849 1.00 30.24  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.865 13.892  21.952 1.00 29.21  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.883 12.462  20.633 1.00 30.75  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.218 12.671  21.904 1.00 29.71  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.465 13.883  20.144 1.00 26.74  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.457 13.205  20.969 1.00 27.80  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.881 13.228  20.350 1.00 28.58  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.795 12.611  20.894 1.00 29.39  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.991 11.744  21.240 1.00 27.73  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.641 11.589  21.987 1.00 29.39  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.280 10.106  22.200 1.00 29.81  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.655 12.313  23.328 1.00 29.76  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.063 13.899  19.207 1.00 28.77  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.352 13.961  18.530 1.00 29.30  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.418 14.588  19.425 1.00 29.40  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.124 15.521  20.147 1.00 28.97  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.218 14.751  17.223 1.00 29.15  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.641 14.048  19.395 1.00 29.78  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.780 14.529  20.204 1.00 30.12  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.623 15.590  19.450 1.00 31.06  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.368 15.825  18.272 1.00 31.52  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.662 13.308  20.581 1.00 30.01  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.400 12.897  19.420 1.00 30.39  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.855 12.144  21.174 1.00 30.31  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.659 16.193  20.103 1.00 32.07  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.554 17.134  19.431 1.00 33.60  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.303 16.393  18.313 1.00 32.35  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.480 16.961  17.235 1.00 32.36  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.563 17.760  20.403 1.00 37.81  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.943 18.578  21.503 1.00 46.51  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.300 19.786  21.240 1.00 49.86  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.930 18.362  22.844 1.00 48.84  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.892 20.239  22.418 1.00 50.70  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.249 19.421  23.413 1.00 50.40  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.720 15.125  18.547 1.00 30.74  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.378 14.349  17.479 1.00 30.71  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.444 14.089  16.273 1.00 30.32  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.912 14.098  15.142 1.00 30.15  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.924 13.016  17.993 1.00 32.51  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.806 12.333  16.971 1.00 36.44  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.847 12.873  16.600 1.00 38.48  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.401 11.157  16.460 1.00 36.09  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.130 13.882  16.500 1.00 29.74  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.187 13.691  15.393 1.00 29.23  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.098 14.982  14.567 1.00 28.86  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.124 14.924  13.339 1.00 28.54  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.790 13.288  15.900 1.00 30.10  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.729 11.920  16.527 1.00 33.25  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.273 10.978  15.931 1.00 34.61  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.134 11.793  17.617 1.00 33.53  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.017 16.147  15.232 1.00 28.87  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.970 17.430  14.499 1.00 28.77  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.313 17.760  13.815 1.00 28.52  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.322 18.379  12.761 1.00 29.00  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.501 18.598  15.400 1.00 28.51  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.005 18.626  15.593 1.00 28.12  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.294 18.072  16.620 1.00 29.15  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.039 19.176  14.686 1.00 27.50  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.946 18.292  16.435 1.00 29.35  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.764 18.974  15.256 1.00 28.62  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.131 19.838  13.458 1.00 27.90  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.591 19.393  14.625 1.00 28.56  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.966 20.238  12.829 1.00 28.09  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.719 20.028  13.414 1.00 27.82  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.437 17.331  14.400 1.00 27.99  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.757 17.581  13.814 1.00 28.59  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.996 16.759  12.526 1.00 27.73  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.838 17.140  11.713 1.00 27.53  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.861 17.296  14.832 1.00 28.81  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.282 15.634  12.372 1.00 26.37  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.375 14.743  11.217 1.00 26.56  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.986 14.543  10.567 1.00 26.66  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.658 13.446  10.146 1.00 26.39  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.985 13.407  11.648 1.00 27.89  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.357 13.592  12.223 1.00 31.26  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.321 13.908  11.498 1.00 33.71  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.469 13.486  13.540 1.00 31.07  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.179 15.630  10.524 1.00 26.62  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.846 15.702  9.959  1.00 26.32  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.825 15.285  8.509  1.00 28.14  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.550 15.863  7.695  1.00 28.75  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.345 17.150  10.041 1.00 25.35  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.899 17.400  9.572  1.00 25.70  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.894 16.552  10.384 1.00 26.00  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.514 18.893  9.678  1.00 24.62  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.927 14.355  8.154  1.00 28.01  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.757 13.950  6.777  1.00 29.12  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.446 14.618  6.272  1.00 30.05  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.446 15.368  5.294  1.00 31.23  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.729 12.409  6.667  1.00 30.57  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.179 11.981  5.313  1.00 32.05  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.127 11.827  6.892  1.00 31.06  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.372 14.429  7.030  1.00 29.28  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.030 14.925  6.757  1.00 28.92  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.234 15.014  8.088  1.00 28.25  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.468 14.229  9.007  1.00 27.56  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.363 13.940  5.775  1.00 28.08  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.912 14.189  5.506  1.00 29.04  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.371 15.204  4.772  1.00 30.44  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.809 13.469  6.073  1.00 28.46  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.993 15.135  4.816  1.00 30.56  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.626 14.075  5.605  1.00 29.46  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.708 12.385  6.952  1.00 28.10  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.362 13.591  5.937  1.00 29.73  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.458 11.893  7.249  1.00 28.76  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.302 12.525  6.784  1.00 28.80  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.315 15.976  8.187  1.00 27.68  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.429 16.140  9.340  1.00 26.85  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.101 16.777  8.880  1.00 27.57  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.113 17.624  7.969  1.00 27.74  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.097 16.878  10.515 1.00 25.74  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.635 18.272  10.194 1.00 28.43  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.603 19.387  10.080 1.00 29.43  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.871 20.347  9.328  1.00 30.74  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.503 19.268  10.666 1.00 28.65  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.956 16.321  9.434  1.00 26.50  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.642 16.891  9.078  1.00 26.20  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.845 17.083  10.381 1.00 25.71  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.412 16.100  10.978 1.00 25.62  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.909 15.997  8.064  1.00 27.71  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.678 16.616  7.423  1.00 33.64  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.125 17.563  8.000  1.00 33.71  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.254 16.127  6.344  1.00 35.92  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.672 18.348  10.828 1.00 24.44  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.947 18.675  12.048 0.50 25.34  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.948 18.624  12.063 0.50 25.12  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.497 18.165  11.941 1.00 25.15  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.979 17.553  12.862 1.00 24.33  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.997 20.185  12.286 0.50 27.28  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.029 20.102  12.434 0.50 26.45  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.368 20.607  13.482 0.50 30.14  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.259 20.880  11.533 0.50 28.77  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.876 18.355  10.773 1.00 25.00  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.502 17.884  10.549 1.00 25.76  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.356 16.383  10.769 1.00 24.41  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.257 15.936  11.055 1.00 24.82  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 12.003 18.314  9.168  1.00 28.09  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.046 17.309  8.164  1.00 31.69  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.450 15.604  10.614 1.00 23.81  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.421 14.152  10.765 1.00 23.94  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 14.027 13.665  12.102 1.00 23.81  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.922 12.476  12.394 1.00 23.18  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.162 13.450  9.592  1.00 24.11  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.481 13.483  8.225  1.00 25.27  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.293 12.781  7.130  1.00 23.96  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.183 11.327  7.184  1.00 22.05  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.353 10.503  6.144  1.00 23.84  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.678 10.985  4.946  1.00 21.62  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.255 9.183   6.309  1.00 21.85  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.676 14.560  12.909 1.00 23.19  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.356 14.150  14.152 1.00 21.71  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.480 13.152  13.796 1.00 21.71  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.767 12.251  14.591 1.00 20.91  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.412 13.597  15.266 1.00 21.26  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.157 13.283  16.555 1.00 22.43  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.019 14.098  16.956 1.00 23.26  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.956 12.187  17.107 1.00 24.43  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.137 13.329  12.612 1.00 20.88  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.266 12.463  12.187 1.00 21.98  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.617 13.188  11.933 1.00 22.72  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.674 14.310  11.416 1.00 22.72  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.910 11.625  10.952 1.00 22.65  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.905 10.492  11.142 1.00 23.87  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.831 9.703   9.890  1.00 24.17  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.352 9.525   12.243 1.00 24.43  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.711 12.493  12.267 1.00 22.74  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 22.060 12.981  12.030 1.00 23.23  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.923 11.776  11.674 1.00 24.56  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.835 10.725  12.302 1.00 26.12  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.666 13.806  13.207 1.00 22.92  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 24.018 14.516  12.912 1.00 24.43  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.092 15.844  13.599 1.00 24.60  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.253 13.642  13.317 1.00 25.72  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.696 11.912  10.613 1.00 23.93  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.632 10.916  10.150 1.00 23.89  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 26.034 11.574  10.167 1.00 24.40  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.233 12.687  9.677  1.00 23.87  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.229 10.379  8.761  1.00 24.09  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.289 9.431   8.202  1.00 25.22  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.865 9.701   8.814  1.00 24.27  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.965 10.899  10.812 1.00 24.59  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.346 11.292  10.956 1.00 25.30  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.243 10.175  10.321 1.00 27.15  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.800 9.019   10.179 1.00 26.20  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.666 11.479  12.440 1.00 24.97  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.573 10.284  13.208 1.00 25.75  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.504 10.538  9.965  1.00 28.12  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.462 9.621   9.345  1.00 30.32  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.303 8.906   10.399 1.00 33.09  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.482 9.423   11.500 1.00 34.42  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.369 10.377  8.377  1.00 31.78  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.019 11.419  9.082  1.00 34.18  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.799 7.709   10.088 1.00 34.68  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.544 6.906   11.065 1.00 37.13  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.809 6.311   10.479 1.00 40.19  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.883 6.032   9.275  1.00 40.87  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.670 5.747   11.655 1.00 38.19  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.441 4.725   10.683 1.00 39.26  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.357 6.204   12.213 1.00 38.08  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.796 6.077   11.340 1.00 41.79  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 37.044 5.460   10.917 1.00 43.57  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.779 3.964   10.705 1.00 45.00  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.101 3.420   9.652  1.00 45.54  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.157 5.740   11.949 1.00 44.89  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.665 5.486   13.278 1.00 46.00  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.685 7.160   11.861 1.00 45.05  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 36.131 3.318   11.678 1.00 45.55  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.827 1.892   11.581 1.00 46.07  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.655 1.629   10.655 1.00 46.68  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.776 2.472   10.505 1.00 47.14  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.530 1.335   12.958 1.00 46.20  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.631 0.451   10.049 1.00 46.95  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.565 0.025   9.142  1.00 47.55  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.409 -0.634  9.924  1.00 47.05  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.654 -1.501  10.750 1.00 47.81  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 34.144 -0.976  8.118  1.00 49.51  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.157 -1.409  7.030  1.00 53.99  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.189 -0.526  5.797  1.00 58.21  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.995 0.410   5.672  1.00 59.18  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.304 -0.808  4.853  1.00 58.55  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 31.171 -0.239  9.636  1.00 45.96  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.967 -0.809  10.233 1.00 45.30  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.434 -1.984  9.435  1.00 44.29  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.755 -2.126  8.249  1.00 44.51  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.618 -2.843  10.070 1.00 43.42  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 28.118 -4.027  9.372  1.00 43.47  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.620 -4.328  9.622  1.00 41.29  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.159 -5.445  9.340  1.00 40.61  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 29.008 -5.241  9.643  1.00 47.05  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.473 -5.463  11.386 1.00 57.70  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.849 -3.291  10.051 1.00 39.24  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.392 -3.376  10.155 1.00 38.50  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.806 -3.381  8.719  1.00 37.36  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.329 -2.716  7.829  1.00 37.70  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.786 -2.174  10.933 1.00 40.07  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.768 -2.279  12.456 1.00 45.04  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.524 -3.388  12.972 1.00 47.44  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.952 -1.235  13.129 1.00 45.21  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.712 -4.101  8.505  1.00 36.24  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.041 -4.185  7.207  1.00 36.07  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.796 -3.287  7.181  1.00 34.87  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.905 -3.474  8.025  1.00 35.61  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.604 -5.644  6.977  1.00 37.81  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.779 -6.442  6.802  1.00 39.23  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.700 -5.797  5.761  1.00 38.12  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.687 -2.361  6.199  1.00 32.50  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.484 -1.521  6.134  1.00 30.45  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.371 -2.231  5.340  1.00 29.63  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.677 -2.874  4.333  1.00 30.40  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.786 -0.112  5.591  1.00 30.07  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.990 0.524   6.322  1.00 30.62  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.536 0.776   5.678  1.00 29.83  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.809 0.681   7.825  1.00 31.98  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.103 -2.135  5.780  1.00 28.17  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.014 -2.774  5.040  1.00 28.29  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.600 -1.884  3.839  1.00 28.51  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.593 -0.669  3.939  1.00 28.07  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.828 -3.031  5.960  1.00 27.11  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.308 -2.491  2.706  1.00 28.89  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.851 -1.783  1.515  1.00 29.74  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.508 -2.448  1.151  1.00 29.91  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.455 -3.347  0.282  1.00 30.99  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.878 -1.904  0.391  1.00 30.72  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.247 -1.361  0.785  1.00 33.48  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.290 0.127   1.127  1.00 35.74  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.653 0.531   1.475  1.00 36.97  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.975 1.674   2.070  1.00 37.78  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.034 2.554   2.388  1.00 36.95  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.238 1.935   2.379  1.00 35.99  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.439 -2.003  1.833  1.00 28.58  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.106 -2.612  1.774  1.00 29.60  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.004 -1.590  2.188  1.00 30.99  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.308 -0.434  2.524  1.00 30.90  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.118 -3.775  2.768  1.00 29.49  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.079 -3.228  4.513  1.00 33.83  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.742  -2.086  2.309  1.00 31.77  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.632  -1.318  2.885  1.00 33.44  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.868  -2.147  3.911  1.00 33.50  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.633  -2.078  3.959  1.00 34.67  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.696  -0.662  1.861  1.00 36.18  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.853  -1.607  1.050  1.00 42.97  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.207  -2.813  0.977  1.00 44.71  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.821  -1.155  0.507  1.00 45.59  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.602  -2.973  4.692  1.00 32.00  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.074  -3.779  5.815  1.00 29.72  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.351  -2.832  6.804  1.00 28.72  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.834  -1.732  7.062  1.00 29.04  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.196  -4.512  6.551  1.00 29.27  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.876  -5.982  5.735  1.00 31.02  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.242  -3.271  7.390  1.00 27.90  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.577  -2.504  8.447  1.00 27.48  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.538  -3.310  9.771  1.00 27.35  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.691  -3.064  10.628 1.00 27.14  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.192  -1.985  8.023  1.00 28.17  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.190  -0.929  6.926  1.00 31.83  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.782  -0.438  6.680  1.00 34.43  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.179  -0.668  5.619  1.00 34.77  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.212  0.250   7.662  1.00 33.13  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.436  -4.310  9.918  1.00 27.07  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.592  -5.119  11.123 1.00 27.24  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.079  -5.309  11.348 1.00 25.46  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.858  -5.452  10.399 1.00 24.40  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.863  -6.500  11.091 1.00 29.64  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.601  -7.414  10.265 1.00 32.76  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.428  -6.410  10.621 1.00 29.41  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.438  -5.387  12.615 1.00 24.56  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.807  -5.570  13.050 1.00 24.28  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.921  -5.736  14.550 1.00 24.76  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.925  -6.046  15.211 1.00 24.73  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.146 -5.534  15.072 1.00 24.51  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.522 -5.670  16.467 1.00 24.96  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.440 -4.534  16.880 1.00 25.47  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.421 -4.261  16.182 1.00 26.11  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.207 -7.037  16.715 1.00 25.52  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.742 -7.140  18.148 1.00 26.17  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.260 -8.205  16.387 1.00 25.61  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.153 -3.883  18.018 1.00 24.82  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 12.015 -2.792  18.481 1.00 23.78  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.625 -3.042  19.863 1.00 23.79  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 12.060 -3.786  20.647 1.00 22.85  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.266 -1.459  18.418 1.00 23.70  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.316 -1.205  19.569 1.00 24.93  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 9.018  -1.712  19.552 1.00 25.67  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.677 -0.377  20.618 1.00 25.77  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.128  -1.442  20.582 1.00 27.03  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.804  -0.114  21.662 1.00 27.36  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.534  -0.669  21.655 1.00 28.16  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.672  -0.373  22.684 1.00 29.42  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.796 -2.438  20.152 1.00 23.49  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.417 -2.622  21.445 1.00 23.76  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 14.018 -1.495  22.399 1.00 23.03  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 14.182 -0.326  22.093 1.00 20.41  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.933 -2.797  21.348 1.00 23.94  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.547 -2.906  22.725 1.00 24.61  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.245 -3.976  23.558 1.00 25.03  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.335 -1.880  23.241 1.00 25.41  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.746 -4.049  24.854 1.00 26.48  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.865 -1.954  24.522 1.00 26.05  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.577 -3.046  25.326 1.00 27.53  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 18.088 -3.137  26.605 1.00 29.08  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.553 -1.864  23.598 1.00 24.46  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 13.076 -0.905  24.595 1.00 25.27  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.986 -0.940  25.789 1.00 25.09  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.818 -1.820  26.646 1.00 25.19  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.630 -1.213  24.982 1.00 27.14  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.925 -0.051  26.174 1.00 28.73  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.956 0.007   25.859 1.00 24.28  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.910 -0.051  26.959 1.00 25.52  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 15.260 0.069   28.354 1.00 25.65  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.677 -0.671  29.240 1.00 25.67  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 17.064 0.935   26.791 1.00 28.39  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.659 2.284   26.727 1.00 32.69  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 14.158 0.878   28.498 1.00 25.19  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.400 1.119   29.730 1.00 25.91  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.686 -0.129  30.307 1.00 26.56  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.191 -0.104  31.449 1.00 27.24  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.421 2.276   29.547 1.00 25.83  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.294 1.889   28.782 1.00 26.77  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.655 -1.222  29.542 1.00 25.88  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 12.151 -2.508  29.989 1.00 25.57  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.173 -3.647  29.775 1.00 27.57  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.877 -4.796  30.123 1.00 27.97  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.872 -2.885  29.237 1.00 26.33  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.697  -1.955  29.488 1.00 28.01  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 9.016  -2.221  30.822 1.00 29.56  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.855  -1.353  30.985 1.00 30.29  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.887  -0.152  31.558 1.00 31.30  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 9.024  0.328   32.049 1.00 30.43  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.779  0.580   31.644 1.00 28.07  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.311 -3.369  29.134 1.00 28.57  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.307 -4.365  28.708 1.00 29.69  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.635 -5.456  27.861 1.00 29.37  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.945 -6.649  28.014 1.00 29.24  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 16.064 -4.973  29.879 1.00 30.59  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 17.073 -4.042  30.502 1.00 34.85  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.559 -4.685  31.793 1.00 38.43  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.292 -3.724  32.604 1.00 40.30  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.254 -3.670  33.934 1.00 39.40  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.499 -4.530  34.622 1.00 36.83  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.936 -2.728  34.587 1.00 37.10  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.663 -5.048  27.018 1.00 28.90  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.924 -6.007  26.189 1.00 29.48  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.765 -5.589  24.717 1.00 28.63  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.627 -4.414  24.392 1.00 28.57  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.505 -6.211  26.752 1.00 31.59  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.383 -7.203  27.881 1.00 38.25  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 10.031 -7.025  28.567 1.00 44.47  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.615  -8.239  29.375 1.00 49.85  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.154 -8.218  30.766 1.00 52.53  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.679 -6.580  23.849 1.00 27.61  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.323 -6.388  22.454 1.00 26.71  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.787 -6.639  22.387 1.00 26.29  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.262 -7.532  23.087 1.00 27.06  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.072 -7.402  21.556 1.00 27.77  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.555 -7.183  21.514 1.00 29.61  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.149 -6.427  20.506 1.00 31.90  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.514 -7.590  22.372 1.00 30.18  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.444 -6.411  20.779 1.00 31.49  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.714 -7.076  21.899 1.00 31.77  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 10.078 -5.836  21.580 1.00 24.39  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.621  -5.927  21.420 1.00 24.44  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.189  -6.026  19.961 1.00 23.50  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.567  -5.169  19.182 1.00 23.66  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.912  -4.671  22.012 1.00 24.21  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.940  -4.575  23.515 1.00 24.60  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.272  -5.502  24.301 1.00 25.61  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.601  -3.536  24.153 1.00 26.21  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.297  -5.432  25.686 1.00 27.40  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.611  -3.437  25.540 1.00 27.26  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.947  -4.385  26.302 1.00 28.55  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.942  -4.315  27.673 1.00 31.98  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.343  -7.009  19.576 1.00 22.96  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.836  -7.022  18.185 1.00 23.27  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.787  -5.891  18.048 1.00 24.26  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.989  -5.685  18.966 1.00 24.92  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.166  -8.400  18.064 1.00 24.13  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.759  -8.761  19.512 1.00 24.32  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.804  -8.123  20.395 1.00 22.56  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.785  -5.156  16.924 1.00 24.20  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.868  -4.030  16.689 1.00 24.64  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.381  -3.983  15.235 1.00 24.55  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.092  -4.399  14.319 1.00 23.73  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.537  -2.669  17.040 1.00 25.77  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.534  -2.404  18.552 1.00 26.74  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.946  -2.558  16.456 1.00 25.31  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.205  -3.387  15.047 1.00 24.34  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.572  -3.067  13.775 1.00 25.56  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.782  -1.554  13.697 1.00 24.71  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.517  -0.889  14.694 1.00 25.21  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.083  -3.347  13.886 1.00 27.58  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.679  -4.021  12.714 1.00 32.37  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.301  -1.009  12.600 1.00 23.70  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.540  0.428   12.544 1.00 23.58  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 3.057  1.057   11.250 1.00 25.73  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.969  0.394   10.205 1.00 25.53  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 5.008  0.790   12.854 1.00 23.35  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 6.040  0.135   11.960 1.00 25.45  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.638  -1.068  12.325 1.00 26.22  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.364  0.687   10.725 1.00 25.98  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.563  -1.679  11.486 1.00 27.22  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.296  0.078   9.889  1.00 26.86  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.904  -1.091  10.279 1.00 26.44  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.727  2.351   11.320 1.00 26.83  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.256  3.069   10.147 1.00 28.41  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.391  3.350   9.134  1.00 28.49  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.580  3.266   9.472  1.00 28.30  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.584  4.372   10.570 1.00 30.70  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.498  5.166   11.309 1.00 34.01  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 3.025  3.677   7.892  1.00 28.56  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 4.019  4.043   6.871  1.00 29.96  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.643  5.442   7.211  1.00 30.78  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.963  6.266   7.815  1.00 30.80  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.375  4.024   5.462  1.00 31.54  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 3.076  2.603   4.967  1.00 35.12  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.468  2.554   3.577  1.00 39.00  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.604  1.150   3.040  1.00 43.24  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.873  0.965   1.756  1.00 45.85  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.914  5.729   6.859  1.00 31.22  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.488  7.057   7.181  1.00 31.43  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.602  8.226   6.746  1.00 30.80  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.067  8.232   5.631  1.00 30.23  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.830  7.053   6.454  1.00 32.57  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 8.194  5.610   6.356  1.00 33.32  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.888  4.893   6.126  1.00 31.47  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.384  9.167   7.659  1.00 29.85  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.486  10.288  7.398  1.00 30.21  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.806  11.526  8.264  1.00 29.13  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.739  11.492  9.067  1.00 28.26  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 3.017  9.853   7.520  1.00 33.17  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.744  8.898   8.539  1.00 36.64  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 4.058  12.630  8.047  1.00 28.84  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.199  13.909  8.749  1.00 29.72  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.288  13.819  9.959  1.00 30.34  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 2.074  13.824  9.793  1.00 30.79  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.660  15.057  7.870  1.00 29.77  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.607  16.068  7.217  1.00 30.83  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.845  17.327  6.872  1.00 31.87  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.799  16.422  8.096  1.00 30.58  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.852  13.725  11.153 1.00 29.92  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 3.080  13.612  12.375 1.00 30.88  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.455  14.767  13.298 1.00 33.15  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.643  15.060  13.471 1.00 33.16  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.326  12.220  13.024 1.00 31.11  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.469  11.139  12.345 1.00 32.85  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 3.077  12.212  14.538 1.00 30.77  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.235  10.249  11.548 1.00 34.25  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.436  15.440  13.859 1.00 34.07  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.634  16.531  14.802 1.00 35.13  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.253  16.027  16.142 1.00 33.27  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.764  15.083  16.755 1.00 32.26  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.314  17.260  15.041 1.00 36.80  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.444  18.389  16.025 1.00 39.27  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 2.023  19.589  15.652 1.00 40.86  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.998  18.248  17.329 1.00 40.97  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.120  20.640  16.557 1.00 42.00  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.083  19.304  18.225 1.00 42.06  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.673  20.483  17.842 1.00 41.73  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.346  16.671  16.562 1.00 32.36  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.113  16.323  17.744 1.00 32.52  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.182  17.495  18.727 1.00 33.62  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.669  18.583  18.381 1.00 32.87  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.533  15.776  17.357 1.00 32.14  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.403  15.598  18.595 1.00 32.76  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.430  14.464  16.576 1.00 30.94  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.665  17.267  19.959 1.00 34.61  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.646  18.265  21.026 1.00 35.56  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.019  18.842  21.318 1.00 36.26  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.022  18.150  21.143 1.00 36.50  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.086  17.659  22.315 1.00 38.62  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.610  17.338  22.239 1.00 44.35  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.692  18.487  21.861 1.00 51.12  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.067  19.669  22.051 1.00 52.77  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.576  18.193  21.380 1.00 52.16  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.065  20.074  21.828 1.00 36.29  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.335  20.710  22.207 1.00 37.21  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.128  19.889  23.244 1.00 36.80  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.539  19.192  24.066 1.00 37.27  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.060  22.099  22.794 1.00 37.63  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.452  20.037  23.245 1.00 36.13  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.356 19.399  24.199 1.00 36.49  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.544 20.354  24.446 1.00 37.91  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.618 21.424  23.836 1.00 38.72  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.849 18.055  23.646 1.00 36.39  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.772 18.222  22.579 1.00 36.16  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.484 19.970  25.321 1.00 38.71  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.710 20.749  25.572 1.00 39.69  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.623 20.826  24.313 1.00 38.40  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.504 21.698  24.236 1.00 38.05  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.497 20.137  26.767 1.00 44.48  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 14.694 18.624  26.661 1.00 52.48  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 15.445 17.945  27.799 1.00 62.52  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 16.626 18.303  28.025 1.00 64.05  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 14.863 17.045  28.451 1.00 65.54  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.397 19.922  23.319 1.00 37.06  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.202 19.880  22.097 1.00 36.19  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.565 20.584  20.908 1.00 35.43  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.287 21.073  20.052 1.00 36.60  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.597 18.437  21.716 1.00 35.68  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 16.042 17.594  22.890 1.00 36.37  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.326 17.707  23.409 1.00 37.57  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.176 16.691  23.489 1.00 37.49  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.742 16.925  24.485 1.00 38.71  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.579 15.904  24.560 1.00 38.69  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.860 16.026  25.065 1.00 39.91  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.240 15.237  26.136 1.00 41.88  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.236 20.618  20.818 1.00 33.67  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.546 21.231  19.678 1.00 32.21  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.278 21.910  20.125 1.00 32.64  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.604 21.370  20.987 1.00 32.98  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 12.078 20.139  18.672 1.00 30.72  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 13.153 19.243  18.088 1.00 29.03  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.304 17.935  18.523 1.00 28.50  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.955 19.675  17.041 1.00 28.65  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.256 17.088  17.963 1.00 28.43  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.913 18.839  16.473 1.00 28.83  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 15.068 17.546  16.944 1.00 28.98  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 16.013 16.713  16.400 1.00 28.27  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.828 22.989  19.454 1.00 32.89  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.475  23.507  19.757 1.00 33.04  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.441  22.562  19.094 1.00 33.00  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.829  21.646  18.350 1.00 32.79  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.483  24.917  19.133 1.00 33.56  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.464 24.825  18.011 1.00 34.41  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.447 23.693  18.309 1.00 32.81  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 7.137  22.763  19.338 1.00 32.40  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 6.097  21.935  18.710 1.00 32.60  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 6.208  22.048  17.161 1.00 33.06  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.358  23.152  16.627 1.00 33.48  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.720  22.394  19.171 1.00 32.70  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 6.268  20.910  16.470 1.00 32.28  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.460  20.912  15.016 1.00 31.02  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.907  19.626  14.387 1.00 30.14  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.587  18.688  15.104 1.00 30.57  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.979  21.029  14.743 1.00 31.79  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.761  19.683  14.841 1.00 32.85  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 10.177 19.808  15.331 1.00 32.20  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 11.056 18.712  14.902 1.00 30.87  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 11.159 17.534  15.511 1.00 31.26  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 12.050 16.641  15.097 1.00 28.82  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.376 17.241  16.549 1.00 30.06  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.870  19.546  13.052 1.00 29.83  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.583  18.270  12.386 1.00 29.72  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.920  17.633  12.095 1.00 27.46  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.777  18.261  11.474 1.00 27.01  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.919  18.444  11.037 1.00 30.58  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.497  18.897  11.158 1.00 32.29  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.472  17.984  11.353 1.00 33.19  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 3.174  20.246  11.118 1.00 33.81  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.155  18.403  11.486 1.00 34.92  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.858  20.676  11.220 1.00 35.11  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.851  19.754  11.424 1.00 36.47  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.439 20.216  11.535 1.00 39.46  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 7.079  16.397  12.488 1.00 26.35  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.247  15.620  12.154 1.00 25.68  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.918  14.695  10.945 1.00 26.67  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.903  13.970  10.948 1.00 27.71  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.745  14.854  13.384 1.00 25.97  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.977  14.007  13.093 1.00 26.21  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.620 13.468  14.354 1.00 28.39  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.653 14.111  15.397 1.00 29.35  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 11.155 12.264  14.274 1.00 28.25  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.745  14.749  9.895  1.00 25.53  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.579  13.942  8.678  1.00 25.71  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.273  12.574  8.775  1.00 25.14  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 10.203 12.409  9.600  1.00 24.31  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 9.154  14.695  7.484  1.00 27.47  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.529 15.009  7.671  1.00 29.11  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.822  11.596  7.918  1.00 23.87  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.401  10.241  7.853  1.00 23.96  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.226  9.490   9.246  1.00 23.91  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 10.085 8.691   9.679  1.00 22.88  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.870 10.301  7.352  1.00 24.51  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 11.015 10.968  6.003  1.00 26.61  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.994 10.230  4.831  1.00 28.40  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 11.019 12.282  5.678  1.00 27.11  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 11.007 11.113  3.839  1.00 27.88  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 11.034 12.357  4.300  1.00 27.70  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 8.102  9.785   9.925  1.00 24.25  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.761  9.205   11.242 1.00 24.57  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.767  8.037   11.180 1.00 25.51  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.707  8.165   10.553 1.00 27.87  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.251  10.307  12.219 1.00 23.73  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.100  9.890   13.693 1.00 25.54  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.344  9.326   14.232 1.00 25.47  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.526  11.023  14.583 1.00 26.84  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 7.092  6.905   11.857 1.00 23.93  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 6.198  5.736   11.873 1.00 24.34  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.682  5.477   13.305 1.00 25.76  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.504  5.297   14.212 1.00 27.13  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.924  4.488   11.342 1.00 23.97  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.543  4.700   9.919  1.00 24.45  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.691  3.382   9.451  1.00 28.66  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.976  3.656   10.528 1.00 32.40  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.346  5.426   13.519 1.00 24.39  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.814  5.172   14.855 1.00 23.90  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.353  3.724   15.069 1.00 23.46  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.768  3.125   14.158 1.00 22.20  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.640  6.121   15.194 1.00 23.76  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.912  7.627   15.107 1.00 25.08  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.721  8.419   15.672 1.00 25.57  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 4.096  8.008   15.965 1.00 24.88  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.513  3.238   16.327 1.00 23.23  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 3.124  1.920   16.825 1.00 23.37  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.532  2.053   18.266 1.00 24.78  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.893  2.960   18.994 1.00 24.12  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.355  1.035   16.892 1.00 23.45  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.618  1.153   18.646 1.00 25.39  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.077  1.102   19.987 1.00 26.96  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.146  0.339   20.802 1.00 28.29  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.439  -0.821  20.500 1.00 28.68  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.309 0.377   20.021 1.00 27.21  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.879 0.321   21.430 1.00 26.74  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.315 1.052   19.078 1.00 28.15  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.765  1.008   21.770 1.00 28.69  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.794  0.376   22.585 1.00 28.37  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.404  1.306   23.612 1.00 27.81  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.172  2.517   23.573 1.00 29.48  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.244  0.759   24.495 1.00 25.86  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.897  1.557   25.518 1.00 25.06  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.234  2.183   25.048 1.00 24.55  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 8.024  1.577   24.310 1.00 23.76  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.122  0.720   26.784 1.00 25.14  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.780  1.478   27.887 1.00 27.19  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 6.155  2.561   28.490 1.00 29.08  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.995  1.303   28.450 1.00 29.25  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.989  2.983   29.425 1.00 29.97  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 8.113  2.258   29.437 1.00 30.97  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.481  3.375   25.538 1.00 24.97  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.699  4.124   25.326 1.00 25.30  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.814  5.198   26.446 1.00 26.05  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.832  5.647   26.991 1.00 26.06  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.723  4.756   23.938 1.00 23.86  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 8.051  6.002   23.851 1.00 25.24  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 10.023 5.606   26.732 1.00 26.18  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.390 6.641   27.682 1.00 26.03  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.486 7.489   26.961 1.00 26.79  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 12.081 6.976   26.008 1.00 27.38  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 10.892 5.973   28.960 1.00 27.02  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 9.736  5.437   29.802 1.00 31.42  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 10.136 4.731   31.078 1.00 32.53  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.939 5.298   31.849 1.00 33.21  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.659  3.602   31.305 1.00 33.30  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.758 8.771   27.324 1.00 27.50  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.709 9.575   26.510 1.00 27.11  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 14.060 8.920   26.248 1.00 27.42  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.536 8.928   25.109 1.00 28.48  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.830 10.888  27.275 1.00 27.67  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.515 11.007  28.033 1.00 28.28  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 11.131 9.587   28.394 1.00 26.77  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.602 8.262   27.255 1.00 26.84  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.872 7.547   27.165 1.00 25.99  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.905 6.345   26.241 1.00 24.97  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.974 5.771   26.047 1.00 24.21  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.741 5.912   25.689 1.00 24.58  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.688 4.801   24.727 1.00 24.17  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.998 5.232   23.274 1.00 23.35  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 15.132 4.369   22.379 1.00 23.22  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 13.309 4.151   24.706 1.00 24.67  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.960 3.353   25.925 1.00 26.38  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.832 2.665   26.429 1.00 26.50  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.803 3.423   26.358 1.00 27.53  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 15.028 6.560   23.002 1.00 23.29  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.438 7.152   21.695 1.00 24.20  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.779 6.538   21.281 1.00 25.35  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.657 6.465   22.135 1.00 26.31  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.561 8.663   21.817 1.00 24.48  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.971 9.527   21.870 1.00 26.30  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.890 6.014   20.060 1.00 24.71  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 18.108 5.349   19.622 1.00 24.35  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.961 3.839   19.483 1.00 25.40  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.775 3.191   18.807 1.00 26.09  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.944 3.256   20.143 1.00 23.86  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.660 1.833   20.035 1.00 22.36  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 16.272 1.496   18.598 1.00 21.20  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.528 2.249   17.961 1.00 20.27  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.789 0.394   18.066 1.00 20.12  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.546 0.008   16.687 1.00 21.52  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.222 -0.749  16.484 1.00 21.83  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.813 -1.533  17.360 1.00 22.15  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.774 -0.799  16.158 1.00 23.58  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.877 0.116   15.604 1.00 24.09  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.412 -1.863  15.109 1.00 25.18  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.166 -0.601  15.526 1.00 24.58  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.535 -0.448  15.352 1.00 20.67  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.358 -1.140  14.862 1.00 22.01  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.843 -2.002  13.659 1.00 22.90  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.606 -1.528  12.799 1.00 21.43  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.272 -0.151  14.427 1.00 21.85  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 11.078 -0.760  13.706 1.00 23.90  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.180 -1.522  14.667 1.00 25.07  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 10.247 0.343   13.057 1.00 24.85  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.478 -3.287  13.649 1.00 24.12  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.944 -4.196  12.615 1.00 25.82  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.835 -5.040  12.085 1.00 27.14  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.982 -5.446  12.855 1.00 28.27  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.955 -5.183  13.190 1.00 28.64  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.301 -4.643  13.570 1.00 35.24  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.177 -5.800  14.018 1.00 40.93  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.657 -6.532  12.847 1.00 45.24  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.860 -6.364  12.302 1.00 46.51  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.197 -7.031  11.206 1.00 45.18  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.745 -5.545  12.865 1.00 45.66  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.895 -5.391  10.791 1.00 27.43  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.998 -6.347  10.146 1.00 28.89  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.867 -7.537  9.660  1.00 30.25  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.083 -7.569  9.908  1.00 30.22  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.278 -5.685  8.976  1.00 29.74  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.381 -5.090  7.670  1.00 30.95  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.256 -8.500  8.949  1.00 31.82  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.007 -9.607  8.343  1.00 34.22  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.097 -9.102  7.384  1.00 34.71  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.134 -9.749  7.249  1.00 36.21  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.055 -10.539 7.569  1.00 37.15  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.279 -9.834  6.453  1.00 41.37  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.243 -10.743 5.839  1.00 47.32  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.043  -10.411 5.784  1.00 48.16  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.692 -11.912 5.364  1.00 48.47  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.879 -7.951  6.734  1.00 33.58  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.817 -7.415  5.752  1.00 32.99  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 15.998 -6.645  6.360  1.00 32.38  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.025 -6.480  5.692  1.00 33.40  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.083 -6.553  4.709  1.00 33.40  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.990 -7.269  3.968  1.00 36.27  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.656 -7.015  4.229  1.00 37.66  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.069 -8.169  2.959  1.00 38.15  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.968 -7.790  3.411  1.00 38.38  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.774 -8.507  2.626  1.00 39.21  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.856 -6.157  7.593  1.00 30.21  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.941 -5.410  8.221  1.00 29.09  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.470 -4.296  9.128  1.00 27.01  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.387 -4.365  9.697  1.00 27.03  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.312 -3.288  9.278  1.00 25.96  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.106 -2.112  10.066 1.00 25.49  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.121 -1.185  9.362  1.00 25.23  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.381 -0.736  8.242  1.00 25.90  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.478 -1.440  10.316 1.00 26.06  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.305 0.001   10.793 1.00 27.57  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.301 -2.256  11.314 1.00 25.39  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 15.005 -0.888  10.029 1.00 24.61  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.952 -0.006  9.537  1.00 24.22  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.167 1.451   9.986  1.00 25.12  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 14.031 2.387   9.198  1.00 24.56  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.578 -0.547  9.975  1.00 23.77  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.473 0.423   9.599  1.00 24.58  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.327 -1.923  9.357  1.00 23.20  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.482 1.632   11.260 1.00 25.83  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.743 2.958   11.801 1.00 26.22  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 15.102 2.923   13.275 1.00 25.99  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.435 1.860   13.821 1.00 25.92  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 15.004 4.087   13.945 1.00 24.83  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.326 4.199   15.376 1.00 23.64  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 14.219 4.918   16.157 1.00 22.81  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.609 5.867   15.646 1.00 22.44  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.670 4.950   15.600 1.00 23.53  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.745 6.241   14.770 1.00 24.13  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.895 4.064   15.376 1.00 24.04  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.938 7.208   15.178 1.00 25.38  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 14.017 4.550   17.443 1.00 21.72  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 13.064 5.268   18.291 1.00 21.46  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.394 6.759   18.343 1.00 21.52  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.559 7.136   18.569 1.00 20.85  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.936 4.689   19.706 1.00 22.35  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 12.004 5.553   20.543 1.00 22.25  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.401 3.259   19.644 1.00 22.93  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.371 7.589   18.126 1.00 22.08  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.601 9.010   18.142 1.00 22.39  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.550 9.795   18.889 1.00 22.53  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.880 10.908  19.300 1.00 22.15  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.787 9.515   16.713 1.00 23.56  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.784 10.926  16.587 1.00 24.64  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.289 9.272   19.051 1.00 22.71  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 9.211  9.947   19.832 1.00 23.71  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.349  8.916   20.626 1.00 25.84  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.443  7.696   20.386 1.00 25.37  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.273  10.861  18.965 1.00 24.17  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.378  10.043  18.215 1.00 26.17  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 9.002  11.829  18.035 1.00 23.84  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.546  9.423   21.574 1.00 27.55  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.627  8.639   22.390 1.00 29.65  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.633  9.471   23.181 1.00 30.74  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.732  10.701  23.231 1.00 30.92  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.717  8.778   23.847 1.00 31.50  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.685  9.366   24.704 1.00 32.96  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.295  8.823   24.422 1.00 33.02  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.994  8.465   23.284 1.00 32.84  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.442  8.763   25.438 1.00 33.24  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.062  8.243   25.322 1.00 34.06  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 0.027  6.797   24.803 1.00 33.14  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -0.896 6.439   24.078 1.00 34.09  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.822 9.147   24.425 1.00 36.46  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.914 10.592  24.853 1.00 40.70  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.891 10.916  26.051 1.00 42.28  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.038 11.490  23.873 1.00 40.94  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 1.044  6.001   25.126 1.00 31.58  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 1.104  4.622   24.662 1.00 31.56  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.440  4.431   23.187 1.00 30.89  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 1.211  3.360   22.636 1.00 31.05  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.967  5.456   22.525 1.00 30.36  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.360  5.379   21.128 1.00 30.44  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.852  5.677   21.038 1.00 29.62  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.293  6.678   21.601 1.00 30.16  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.625  6.439   20.286 1.00 31.55  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.102  6.370   20.227 1.00 34.63  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.427 7.442   19.322 1.00 35.70  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.348 5.056   19.662 1.00 35.51  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.612  4.838   20.315 1.00 27.26  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 6.025  5.049   20.082 1.00 26.44  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.202  5.389   18.577 1.00 25.69  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.602  4.728   17.702 1.00 25.81  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.850  3.805   20.498 1.00 26.50  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.359  2.548   19.807 1.00 26.57  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.372  4.005   20.317 1.00 27.25  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 7.024  6.413   18.307 1.00 24.49  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.371  6.873   16.972 1.00 24.51  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.816  6.575   16.608 1.00 25.58  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.740  6.809   17.395 1.00 25.46  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 9.022  6.042   15.397 1.00 25.32  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.347 5.642   14.916 1.00 25.20  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.701 6.444   13.660 1.00 24.40  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.857  6.591   12.771 1.00 23.59  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.347 4.158   14.549 1.00 24.77  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.763  3.210   15.570 1.00 24.41  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.552 2.675   16.570 1.00 23.94  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.462  2.747   15.449 1.00 24.00  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 10.030 1.747   17.471 1.00 24.24  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.949  1.829   16.360 1.00 23.79  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.737  1.332   17.359 1.00 23.47  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.942 6.972   13.596 1.00 23.83  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.409 7.730   12.447 1.00 24.60  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.850 6.731   11.369 1.00 24.94  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.813 5.970   11.577 1.00 24.09  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.596 8.613   12.859 1.00 25.04  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 12.175 6.731   10.214 1.00 26.20  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.544 5.839   9.116  1.00 26.79  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.932 6.169   8.527  1.00 26.64  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.343 7.333   8.527  1.00 26.80  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.497 5.937   8.001  1.00 29.40  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.663 4.899   6.904  1.00 30.59  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.790 3.707   7.231  1.00 30.51  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.672 5.282   5.732  1.00 32.05  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.656 5.139   8.035  1.00 25.86  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.952 5.285   7.388  1.00 25.73  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.998 4.487   6.032  1.00 26.89  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.989 4.570   5.331  1.00 27.87  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.145 4.885   8.294  1.00 24.20  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.180 5.671   9.606  1.00 23.52  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.167 3.376   8.522  1.00 23.14  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.960 3.694   5.688  1.00 26.12  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.918 2.863   4.474  1.00 25.85  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.020 3.637   3.125  1.00 27.55  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.438 3.067   2.103  1.00 28.78  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.636 1.996   4.497  1.00 24.84  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.542 1.082   5.717  1.00 22.97  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.227 0.356   5.676  1.00 24.93  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.144 1.223   6.140  1.00 27.76  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.869  0.860   6.216  1.00 29.16  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.495  -0.362  5.847  1.00 29.71  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.959  1.709   6.674  1.00 28.44  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.611 4.916   3.110  1.00 27.56  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.680 5.781   1.933  1.00 27.63  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.067 6.370   1.691  1.00 29.28  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.314 6.937   0.607  1.00 30.31  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.664 6.924   2.051  1.00 28.59  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.980 7.916   3.148  1.00 32.71  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.293 7.468   4.291  1.00 31.99  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.914 9.133   2.877  1.00 34.43  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.969 6.279   2.701  1.00 28.39  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.338 6.800   2.611  1.00 27.67  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.215 5.785   1.882  1.00 28.03  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.090 5.155   2.493  1.00 28.59  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.899 7.084   4.011  1.00 27.14  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 18.054 7.938   4.911  1.00 27.93  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.650 7.964   6.277  1.00 28.40  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.887 9.328   4.348  1.00 28.09  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.978 5.625   0.562  1.00 27.03  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.690 4.649   -0.259 1.00 28.45  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.234 4.792   -0.230 1.00 29.94  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.950 3.799   -0.395 1.00 30.50  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.195 4.673   -1.725 1.00 28.70  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.683 4.658   -2.011 1.00 29.84  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.418 4.450   -3.523 1.00 30.27  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.943 3.577   -1.204 1.00 29.57  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.738 6.022   -0.009 1.00 30.32  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.168 6.342   -0.013 1.00 30.84  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.951 5.799   1.164  1.00 32.25  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.180 5.747   1.094  1.00 31.71  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.381 7.836   -0.133 1.00 30.49  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.658 8.646   0.897  1.00 31.28  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.426 9.218   0.774  1.00 32.23  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.141 9.006   2.198  1.00 31.35  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.103 9.891   1.924  1.00 32.44  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.159 9.818   2.797  1.00 32.29  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.338 8.783   2.885  1.00 32.07  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.315 10.361  4.070  1.00 32.82  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.473 9.295   4.164  1.00 33.15  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.480 10.091  4.733  1.00 33.02  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.265 5.412   2.271  1.00 33.96  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.969 4.814   3.418  1.00 36.16  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.744 3.541   3.013  1.00 39.07  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.677 3.150   3.709  1.00 38.91  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.984 4.461   4.539  1.00 36.38  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.434 5.639   5.325  1.00 37.44  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.329 5.200   6.265  1.00 37.53  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.518 6.304   6.125  1.00 38.41  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.358 2.911   1.876  1.00 41.34  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.941 1.686   1.353  1.00 44.30  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.983 1.841   0.271  1.00 47.91  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.322 0.842   -0.350 1.00 48.68  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.819 0.815   0.790  1.00 45.37  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 23.180 -0.064  1.822  1.00 47.53  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.868 -0.408  2.819  1.00 47.70  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 22.002 -0.418  1.640  1.00 48.84  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.455 3.059   -0.012 1.00 50.19  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.437 3.270   -1.077 1.00 52.97  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.387 4.437   -0.757 1.00 54.71  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 29.150 4.898   -1.625 1.00 55.89  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.709 3.502   -2.415 1.00 56.42  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.710 4.650   -2.362 1.00 61.81  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.552 4.569   -3.342 1.00 67.77  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.027 5.641   -3.728 1.00 67.50  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 24.163 3.437   -3.716 1.00 70.78  ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BOY B 2 .   ? 10.690 13.447  22.618 1.00 27.64  ? 201 A1BOY A N1  1 
HETATM 1079 C  C4  . A1BOY B 2 .   ? 8.410  10.951  25.937 1.00 29.24  ? 201 A1BOY A C4  1 
HETATM 1080 C  C5  . A1BOY B 2 .   ? 9.341  10.796  24.916 1.00 29.05  ? 201 A1BOY A C5  1 
HETATM 1081 C  C6  . A1BOY B 2 .   ? 10.197 11.968  24.490 1.00 28.79  ? 201 A1BOY A C6  1 
HETATM 1082 C  C7  . A1BOY B 2 .   ? 9.887  12.467  23.089 1.00 27.91  ? 201 A1BOY A C7  1 
HETATM 1083 C  C8  . A1BOY B 2 .   ? 11.812 14.050  23.358 1.00 27.62  ? 201 A1BOY A C8  1 
HETATM 1084 C  C10 . A1BOY B 2 .   ? 12.911 14.567  21.158 1.00 28.07  ? 201 A1BOY A C10 1 
HETATM 1085 C  C13 . A1BOY B 2 .   ? 10.455 14.035  21.296 1.00 27.82  ? 201 A1BOY A C13 1 
HETATM 1086 O  O2  . A1BOY B 2 .   ? 11.093 15.594  18.801 1.00 27.33  ? 201 A1BOY A O2  1 
HETATM 1087 C  C12 . A1BOY B 2 .   ? 11.556 14.469  19.014 1.00 27.56  ? 201 A1BOY A C12 1 
HETATM 1088 N  N2  . A1BOY B 2 .   ? 11.869 13.634  18.042 1.00 27.12  ? 201 A1BOY A N2  1 
HETATM 1089 C  C11 . A1BOY B 2 .   ? 11.711 13.932  20.428 1.00 27.56  ? 201 A1BOY A C11 1 
HETATM 1090 C  C9  . A1BOY B 2 .   ? 13.099 13.966  22.556 1.00 27.97  ? 201 A1BOY A C9  1 
HETATM 1091 O  O1  . A1BOY B 2 .   ? 8.957  12.014  22.428 1.00 27.28  ? 201 A1BOY A O1  1 
HETATM 1092 C  C1  . A1BOY B 2 .   ? 9.463  9.491   24.384 1.00 29.29  ? 201 A1BOY A C1  1 
HETATM 1093 O  O   . A1BOY B 2 .   ? 10.477 9.336   23.504 1.00 28.67  ? 201 A1BOY A O   1 
HETATM 1094 C  C   . A1BOY B 2 .   ? 10.637 8.068   22.879 1.00 29.76  ? 201 A1BOY A C   1 
HETATM 1095 C  C3  . A1BOY B 2 .   ? 7.647  9.880   26.362 1.00 29.03  ? 201 A1BOY A C3  1 
HETATM 1096 C  C2  . A1BOY B 2 .   ? 7.828  8.669   25.748 1.00 29.25  ? 201 A1BOY A C2  1 
HETATM 1097 N  N   . A1BOY B 2 .   ? 8.719  8.458   24.767 1.00 29.45  ? 201 A1BOY A N   1 
HETATM 1098 ZN ZN  . ZN    C 3 .   ? 11.129 -5.317  5.713  1.00 34.64  2 202 ZN    A ZN  1 
HETATM 1099 O  O   . HOH   D 4 .   ? 6.911  2.100   22.509 1.00 300.00 ? 301 HOH   A O   1 
HETATM 1100 O  O   . HOH   D 4 .   ? 19.029 3.813   4.661  1.00 214.66 ? 302 HOH   A O   1 
HETATM 1101 O  O   . HOH   D 4 .   ? 13.136 1.711   22.281 1.00 300.00 ? 303 HOH   A O   1 
HETATM 1102 O  O   . HOH   D 4 .   ? 11.548 5.923   23.972 1.00 98.81  ? 304 HOH   A O   1 
HETATM 1103 O  O   . HOH   D 4 .   ? 13.123 6.135   31.244 1.00 25.37  ? 305 HOH   A O   1 
HETATM 1104 O  O   . HOH   D 4 .   ? 13.337 1.186   17.515 1.00 70.36  ? 306 HOH   A O   1 
HETATM 1105 O  O   . HOH   D 4 .   ? 20.406 7.903   18.865 1.00 29.35  ? 307 HOH   A O   1 
HETATM 1106 O  O   . HOH   D 4 .   ? 10.983 7.536   4.937  1.00 32.04  ? 308 HOH   A O   1 
HETATM 1107 O  O   . HOH   D 4 .   ? 13.419 9.474   9.415  1.00 20.64  ? 309 HOH   A O   1 
HETATM 1108 O  O   . HOH   D 4 .   ? 15.237 1.589   23.310 1.00 23.38  ? 310 HOH   A O   1 
HETATM 1109 O  O   . HOH   D 4 .   ? 11.933 11.059  11.785 1.00 23.70  ? 311 HOH   A O   1 
HETATM 1110 O  O   . HOH   D 4 .   ? 0.082  14.692  8.513  1.00 53.75  ? 312 HOH   A O   1 
HETATM 1111 O  O   . HOH   D 4 .   ? 20.365 21.809  7.927  1.00 41.18  ? 313 HOH   A O   1 
HETATM 1112 O  O   . HOH   D 4 .   ? 29.691 2.576   10.261 1.00 32.49  ? 314 HOH   A O   1 
HETATM 1113 O  O   . HOH   D 4 .   ? 35.893 14.966  17.673 1.00 59.34  ? 315 HOH   A O   1 
HETATM 1114 O  O   . HOH   D 4 .   ? 24.071 21.288  8.370  1.00 31.01  ? 316 HOH   A O   1 
HETATM 1115 O  O   . HOH   D 4 .   ? 9.257  -3.620  9.228  1.00 300.00 ? 317 HOH   A O   1 
HETATM 1116 O  O   . HOH   D 4 .   ? 22.804 -2.299  4.258  1.00 32.10  ? 318 HOH   A O   1 
HETATM 1117 O  O   . HOH   D 4 .   ? 23.675 -0.579  15.639 1.00 35.39  ? 319 HOH   A O   1 
HETATM 1118 O  O   . HOH   D 4 .   ? 31.477 9.344   13.912 1.00 41.95  ? 320 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 11.835 -6.274  32.022 1.00 57.41  ? 321 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 35.098 19.452  11.631 1.00 39.98  ? 322 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? 6.376  -5.755  29.243 1.00 37.38  ? 323 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 10.152 17.621  20.568 1.00 40.13  ? 324 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? 3.469  21.873  22.536 1.00 46.65  ? 325 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 35.174 4.815   13.995 1.00 60.56  ? 326 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 0.485  13.709  17.064 1.00 44.34  ? 327 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 18.697 19.979  28.321 1.00 60.71  ? 328 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? -0.567 2.039   8.580  1.00 142.28 ? 329 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 0.683  -0.752  16.679 1.00 19.31  ? 330 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? 10.476 3.438   33.893 1.00 33.41  ? 331 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 3.570  -5.513  21.288 1.00 22.75  ? 332 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 19.762 -1.058  27.172 1.00 35.12  ? 333 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 13.565 1.390   1.010  1.00 21.08  ? 334 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? 5.442  12.633  25.154 1.00 42.01  ? 335 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 15.776 11.331  24.257 1.00 23.23  ? 336 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? -1.039 0.900   5.073  1.00 42.60  ? 337 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 19.023 3.615   26.156 1.00 26.28  ? 338 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 16.684 9.989   7.389  1.00 75.15  ? 339 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 15.618 13.010  26.544 1.00 31.71  ? 340 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 18.060 1.982   23.312 1.00 29.23  ? 341 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? -0.388 15.677  22.151 1.00 56.18  ? 342 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 5.168  -5.166  -0.164 1.00 61.60  ? 343 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 16.678 -8.620  10.191 1.00 45.94  ? 344 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 18.204 20.474  9.579  1.00 33.99  ? 345 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 7.372  2.945   33.055 1.00 32.40  ? 346 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 9.362  11.394  12.280 1.00 282.86 ? 347 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 8.296  -4.701  0.802  1.00 34.71  ? 348 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? 4.460  -5.919  6.802  1.00 43.78  ? 349 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 21.826 -5.286  10.962 1.00 39.66  ? 350 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 31.512 19.789  17.068 1.00 31.09  ? 351 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? 23.452 17.786  19.740 1.00 32.12  ? 352 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? 18.603 18.095  17.254 1.00 25.79  ? 353 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 14.823 -5.510  34.713 1.00 28.88  ? 354 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? 9.014  2.046   3.093  1.00 24.82  ? 355 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 14.159 8.463   30.080 1.00 36.05  ? 356 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 0.376  3.339   6.848  1.00 44.27  ? 357 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 5.375  -0.015  -2.067 1.00 38.27  ? 358 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? 4.563  9.885   18.781 1.00 41.96  ? 359 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? 31.183 19.758  10.388 1.00 35.71  ? 360 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 17.429 -8.269  3.470  1.00 47.84  ? 361 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? 1.197  10.965  22.094 1.00 49.00  ? 362 HOH   A O   1 
HETATM 1161 O  O   . HOH   D 4 .   ? 15.035 -4.902  17.230 1.00 32.45  ? 363 HOH   A O   1 
HETATM 1162 O  O   . HOH   D 4 .   ? 3.500  3.525   27.867 1.00 42.06  ? 364 HOH   A O   1 
HETATM 1163 O  O   . HOH   D 4 .   ? -0.280 12.220  21.176 1.00 53.75  ? 365 HOH   A O   1 
HETATM 1164 O  O   . HOH   D 4 .   ? 10.358 4.091   3.435  1.00 22.66  ? 366 HOH   A O   1 
HETATM 1165 O  O   . HOH   D 4 .   ? 8.752  18.732  18.575 1.00 34.62  ? 367 HOH   A O   1 
HETATM 1166 O  O   . HOH   D 4 .   ? 2.306  -1.677  17.705 1.00 52.77  ? 368 HOH   A O   1 
HETATM 1167 O  O   . HOH   D 4 .   ? 9.707  20.436  11.143 1.00 33.40  ? 369 HOH   A O   1 
HETATM 1168 O  O   . HOH   D 4 .   ? 5.247  -2.157  24.222 1.00 31.18  ? 370 HOH   A O   1 
HETATM 1169 O  O   . HOH   D 4 .   ? 5.227  5.305   24.217 1.00 41.75  ? 371 HOH   A O   1 
HETATM 1170 O  O   . HOH   D 4 .   ? 6.077  1.204   6.395  1.00 30.51  ? 372 HOH   A O   1 
HETATM 1171 O  O   . HOH   D 4 .   ? 8.396  -8.737  25.012 1.00 42.22  ? 373 HOH   A O   1 
HETATM 1172 O  O   . HOH   D 4 .   ? 1.542  12.567  26.137 1.00 65.14  ? 374 HOH   A O   1 
HETATM 1173 O  O   . HOH   D 4 .   ? 6.687  7.320   29.132 1.00 26.80  ? 375 HOH   A O   1 
HETATM 1174 O  O   . HOH   D 4 .   ? 2.411  -2.819  4.013  1.00 40.49  ? 376 HOH   A O   1 
HETATM 1175 O  O   . HOH   D 4 .   ? 15.214 13.785  4.104  1.00 40.68  ? 377 HOH   A O   1 
HETATM 1176 O  O   . HOH   D 4 .   ? 11.131 16.159  4.990  1.00 50.87  ? 378 HOH   A O   1 
HETATM 1177 O  O   . HOH   D 4 .   ? 6.944  12.217  5.668  1.00 35.43  ? 379 HOH   A O   1 
HETATM 1178 O  O   . HOH   D 4 .   ? 2.033  12.618  5.837  1.00 34.74  ? 380 HOH   A O   1 
HETATM 1179 O  O   . HOH   D 4 .   ? 15.407 10.609  0.735  1.00 33.63  ? 381 HOH   A O   1 
HETATM 1180 O  O   . HOH   D 4 .   ? 18.986 -0.888  19.671 1.00 32.10  ? 382 HOH   A O   1 
HETATM 1181 O  O   . HOH   D 4 .   ? 3.933  2.253   -0.018 1.00 62.20  ? 383 HOH   A O   1 
HETATM 1182 O  O   . HOH   D 4 .   ? 7.400  25.165  14.634 1.00 47.19  ? 384 HOH   A O   1 
HETATM 1183 O  O   . HOH   D 4 .   ? 14.512 20.641  8.615  1.00 41.73  ? 385 HOH   A O   1 
HETATM 1184 O  O   . HOH   D 4 .   ? 21.487 1.737   -2.558 1.00 62.30  ? 386 HOH   A O   1 
HETATM 1185 O  O   . HOH   D 4 .   ? 6.441  13.516  21.642 1.00 38.73  ? 387 HOH   A O   1 
HETATM 1186 O  O   . HOH   D 4 .   ? 10.326 -3.317  11.451 1.00 125.11 ? 388 HOH   A O   1 
HETATM 1187 O  O   . HOH   D 4 .   ? 3.901  6.073   26.184 1.00 39.43  ? 389 HOH   A O   1 
HETATM 1188 O  O   . HOH   D 4 .   ? 32.117 13.736  21.235 1.00 33.27  ? 390 HOH   A O   1 
HETATM 1189 O  O   . HOH   D 4 .   ? 18.786 11.875  2.015  1.00 38.31  ? 391 HOH   A O   1 
HETATM 1190 O  O   . HOH   D 4 .   ? -0.481 14.848  13.149 1.00 48.05  ? 392 HOH   A O   1 
HETATM 1191 O  O   . HOH   D 4 .   ? 19.862 23.226  15.482 1.00 26.12  ? 393 HOH   A O   1 
HETATM 1192 O  O   . HOH   D 4 .   ? 2.684  9.682   20.551 1.00 44.41  ? 394 HOH   A O   1 
HETATM 1193 O  O   . HOH   D 4 .   ? 18.579 -0.325  30.208 1.00 48.25  ? 395 HOH   A O   1 
HETATM 1194 O  O   . HOH   D 4 .   ? 28.671 3.356   2.977  1.00 39.24  ? 396 HOH   A O   1 
HETATM 1195 O  O   . HOH   D 4 .   ? -0.745 2.621   1.563  1.00 48.92  ? 397 HOH   A O   1 
HETATM 1196 O  O   . HOH   D 4 .   ? 0.941  1.150   24.823 1.00 32.48  ? 398 HOH   A O   1 
HETATM 1197 O  O   . HOH   D 4 .   ? 17.964 17.552  4.734  1.00 50.91  ? 399 HOH   A O   1 
HETATM 1198 O  O   . HOH   D 4 .   ? 5.225  -2.332  29.522 1.00 46.34  ? 400 HOH   A O   1 
HETATM 1199 O  O   . HOH   D 4 .   ? 22.437 8.041   20.928 1.00 31.28  ? 401 HOH   A O   1 
HETATM 1200 O  O   . HOH   D 4 .   ? 22.832 18.410  6.196  1.00 30.97  ? 402 HOH   A O   1 
HETATM 1201 O  O   . HOH   D 4 .   ? 1.228  -3.231  17.544 1.00 24.46  ? 403 HOH   A O   1 
HETATM 1202 O  O   . HOH   D 4 .   ? 29.234 21.369  18.677 1.00 52.02  ? 404 HOH   A O   1 
HETATM 1203 O  O   . HOH   D 4 .   ? 6.136  -11.743 5.967  1.00 63.21  ? 405 HOH   A O   1 
HETATM 1204 O  O   . HOH   D 4 .   ? 10.985 2.320   23.331 1.00 57.81  ? 406 HOH   A O   1 
HETATM 1205 O  O   . HOH   D 4 .   ? 12.142 20.587  12.523 1.00 34.24  ? 407 HOH   A O   1 
HETATM 1206 O  O   . HOH   D 4 .   ? 20.534 19.427  5.337  1.00 52.05  ? 408 HOH   A O   1 
HETATM 1207 O  O   . HOH   D 4 .   ? 8.881  -8.271  9.127  1.00 45.15  ? 409 HOH   A O   1 
HETATM 1208 O  O   . HOH   D 4 .   ? 31.600 1.840   12.851 1.00 32.43  ? 410 HOH   A O   1 
HETATM 1209 O  O   . HOH   D 4 .   ? 30.747 10.208  18.109 1.00 40.49  ? 411 HOH   A O   1 
HETATM 1210 O  O   . HOH   D 4 .   ? 7.269  10.232  4.268  1.00 42.35  ? 412 HOH   A O   1 
HETATM 1211 O  O   . HOH   D 4 .   ? 3.101  12.115  18.110 1.00 44.29  ? 413 HOH   A O   1 
HETATM 1212 O  O   . HOH   D 4 .   ? 35.047 7.621   6.365  1.00 35.49  ? 414 HOH   A O   1 
HETATM 1213 O  O   . HOH   D 4 .   ? 4.124  -3.289  21.987 1.00 38.02  ? 415 HOH   A O   1 
HETATM 1214 O  O   . HOH   D 4 .   ? 11.635 17.118  26.859 1.00 40.63  ? 416 HOH   A O   1 
HETATM 1215 O  O   . HOH   D 4 .   ? 20.934 6.546   -4.693 1.00 35.86  ? 417 HOH   A O   1 
HETATM 1216 O  O   . HOH   D 4 .   ? 30.363 21.811  25.798 1.00 47.29  ? 418 HOH   A O   1 
HETATM 1217 O  O   . HOH   D 4 .   ? 27.807 17.043  23.407 1.00 30.33  ? 419 HOH   A O   1 
HETATM 1218 O  O   . HOH   D 4 .   ? -0.015 -3.183  9.479  1.00 59.79  ? 420 HOH   A O   1 
HETATM 1219 O  O   . HOH   D 4 .   ? 24.740 6.711   20.774 1.00 43.66  ? 421 HOH   A O   1 
HETATM 1220 O  O   . HOH   D 4 .   ? 12.241 -8.838  13.242 1.00 30.94  ? 422 HOH   A O   1 
HETATM 1221 O  O   . HOH   D 4 .   ? 2.772  13.991  20.003 1.00 35.03  ? 423 HOH   A O   1 
HETATM 1222 O  O   . HOH   D 4 .   ? 17.872 16.004  30.279 1.00 41.35  ? 424 HOH   A O   1 
HETATM 1223 O  O   . HOH   D 4 .   ? 14.520 -11.969 4.668  1.00 51.35  ? 425 HOH   A O   1 
HETATM 1224 O  O   . HOH   D 4 .   ? 2.528  -1.173  25.580 1.00 81.08  ? 426 HOH   A O   1 
HETATM 1225 O  O   . HOH   D 4 .   ? 1.489  5.561   28.580 1.00 83.42  ? 427 HOH   A O   1 
HETATM 1226 O  O   . HOH   D 4 .   ? 21.582 13.312  1.224  1.00 50.47  ? 428 HOH   A O   1 
HETATM 1227 O  O   . HOH   D 4 .   ? 16.740 23.330  15.313 1.00 38.86  ? 429 HOH   A O   1 
HETATM 1228 O  O   . HOH   D 4 .   ? 27.247 19.998  19.418 1.00 66.79  ? 430 HOH   A O   1 
HETATM 1229 O  O   . HOH   D 4 .   ? 21.436 21.136  18.028 1.00 37.74  ? 431 HOH   A O   1 
HETATM 1230 O  O   . HOH   D 4 .   ? 29.537 15.418  23.585 1.00 34.22  ? 432 HOH   A O   1 
HETATM 1231 O  O   . HOH   D 4 .   ? 20.241 8.190   -2.434 1.00 46.83  ? 433 HOH   A O   1 
HETATM 1232 O  O   . HOH   D 4 .   ? 4.535  11.582  19.923 1.00 52.68  ? 434 HOH   A O   1 
HETATM 1233 O  O   . HOH   D 4 .   ? 7.145  -6.027  2.773  1.00 52.34  ? 435 HOH   A O   1 
HETATM 1234 O  O   . HOH   D 4 .   ? 13.946 -7.166  32.667 1.00 47.16  ? 436 HOH   A O   1 
HETATM 1235 O  O   . HOH   D 4 .   ? 19.534 -5.080  20.620 1.00 57.51  ? 437 HOH   A O   1 
HETATM 1236 O  O   . HOH   D 4 .   ? 17.805 10.312  26.205 1.00 32.70  ? 438 HOH   A O   1 
HETATM 1237 O  O   . HOH   D 4 .   ? 17.803 10.381  0.255  1.00 36.39  ? 439 HOH   A O   1 
HETATM 1238 O  O   . HOH   D 4 .   ? 35.444 10.513  19.516 1.00 55.13  ? 440 HOH   A O   1 
HETATM 1239 O  O   . HOH   D 4 .   ? 2.329  1.469   26.788 1.00 38.20  ? 441 HOH   A O   1 
HETATM 1240 O  O   . HOH   D 4 .   ? 1.117  -2.283  23.735 1.00 39.88  ? 442 HOH   A O   1 
HETATM 1241 O  O   . HOH   D 4 .   ? 12.738 13.156  1.003  1.00 44.66  ? 443 HOH   A O   1 
HETATM 1242 O  O   . HOH   D 4 .   ? 4.202  8.131   28.026 1.00 55.11  ? 444 HOH   A O   1 
HETATM 1243 O  O   . HOH   D 4 .   ? 12.295 22.686  14.519 1.00 35.22  ? 445 HOH   A O   1 
HETATM 1244 O  O   . HOH   D 4 .   ? 1.861  8.290   29.309 1.00 53.73  ? 446 HOH   A O   1 
HETATM 1245 O  O   . HOH   D 4 .   ? 14.393 -11.131 1.339  1.00 45.03  ? 447 HOH   A O   1 
HETATM 1246 O  O   . HOH   D 4 .   ? 2.127  13.494  22.670 1.00 39.80  ? 448 HOH   A O   1 
HETATM 1247 O  O   . HOH   D 4 .   ? -1.640 -4.964  15.754 1.00 49.23  ? 449 HOH   A O   1 
HETATM 1248 O  O   . HOH   D 4 .   ? 0.571  13.750  28.424 1.00 69.79  ? 450 HOH   A O   1 
HETATM 1249 O  O   . HOH   D 4 .   ? -1.805 14.640  27.465 1.00 79.16  ? 451 HOH   A O   1 
HETATM 1250 O  O   . HOH   D 4 .   ? 8.815  5.994   2.832  1.00 32.22  ? 452 HOH   A O   1 
HETATM 1251 O  O   . HOH   D 4 .   ? 16.570 11.633  28.801 1.00 70.43  ? 453 HOH   A O   1 
HETATM 1252 O  O   . HOH   D 4 .   ? 7.203  14.633  25.350 1.00 37.48  ? 454 HOH   A O   1 
HETATM 1253 O  O   . HOH   D 4 .   ? 9.746  -9.218  12.765 1.00 38.74  ? 455 HOH   A O   1 
HETATM 1254 O  O   . HOH   D 4 .   ? -0.568 3.517   28.386 1.00 55.76  ? 456 HOH   A O   1 
HETATM 1255 O  O   . HOH   D 4 .   ? 8.346  16.860  4.175  1.00 54.06  ? 457 HOH   A O   1 
HETATM 1256 O  O   . HOH   D 4 .   ? 9.738  14.551  26.902 1.00 53.49  ? 458 HOH   A O   1 
HETATM 1257 O  O   . HOH   D 4 .   ? 32.335 3.457   15.086 1.00 26.15  ? 459 HOH   A O   1 
HETATM 1258 O  O   . HOH   D 4 .   ? 4.558  -1.534  -4.352 1.00 48.80  ? 460 HOH   A O   1 
HETATM 1259 O  O   . HOH   D 4 .   ? 6.480  14.453  4.189  1.00 42.82  ? 461 HOH   A O   1 
HETATM 1260 O  O   . HOH   D 4 .   ? 10.329 23.942  13.758 1.00 36.07  ? 462 HOH   A O   1 
HETATM 1261 O  O   . HOH   D 4 .   ? 5.088  12.638  27.865 1.00 47.56  ? 463 HOH   A O   1 
HETATM 1262 O  O   . HOH   D 4 .   ? 0.309  11.109  18.741 1.00 60.13  ? 464 HOH   A O   1 
HETATM 1263 O  O   . HOH   D 4 .   ? -0.643 5.489   2.725  1.00 68.87  ? 465 HOH   A O   1 
HETATM 1264 O  O   . HOH   D 4 .   ? 20.528 3.791   9.172  1.00 210.01 ? 466 HOH   A O   1 
HETATM 1265 O  O   . HOH   D 4 .   ? 2.427  15.089  3.557  1.00 59.01  ? 467 HOH   A O   1 
HETATM 1266 O  O   . HOH   D 4 .   ? 0.046  7.779   31.333 1.00 61.09  ? 468 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.4077 0.3245 0.4178 -0.0317 0.1114 -0.0076 7   SER   A N   
2    C CA  . SER   A 1   ? 0.4137 0.3360 0.4407 -0.0290 0.1097 -0.0042 7   SER   A CA  
3    C C   . SER   A 1   ? 0.3961 0.3229 0.4362 -0.0235 0.1140 -0.0009 7   SER   A C   
4    O O   . SER   A 1   ? 0.3900 0.3153 0.4258 -0.0224 0.1167 -0.0006 7   SER   A O   
5    C CB  . SER   A 1   ? 0.4458 0.3700 0.4760 -0.0341 0.0999 0.0015  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4903 0.4151 0.5170 -0.0369 0.0946 0.0076  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3787 0.3097 0.4334 -0.0207 0.1155 0.0009  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3640 0.2970 0.4296 -0.0164 0.1214 0.0027  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3494 0.2849 0.4236 -0.0143 0.1266 0.0008  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3506 0.2858 0.4201 -0.0152 0.1272 -0.0029 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3372 0.2746 0.4245 -0.0116 0.1311 0.0035  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3415 0.2808 0.4357 -0.0106 0.1372 0.0018  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3344 0.2707 0.4314 -0.0087 0.1468 0.0003  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3249 0.2582 0.4237 -0.0072 0.1482 0.0020  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3400 0.2847 0.4502 -0.0105 0.1340 0.0067  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.3391 0.2751 0.4354 -0.0095 0.1537 -0.0027 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.3398 0.2713 0.4370 -0.0093 0.1642 -0.0051 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3406 0.2749 0.4546 -0.0076 0.1694 -0.0027 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3432 0.2820 0.4595 -0.0090 0.1677 -0.0021 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.3481 0.2764 0.4288 -0.0135 0.1687 -0.0104 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.3544 0.2821 0.4217 -0.0151 0.1635 -0.0119 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3607 0.2819 0.4393 -0.0151 0.1802 -0.0139 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.3540 0.2842 0.4109 -0.0190 0.1621 -0.0134 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3422 0.2740 0.4697 -0.0045 0.1762 -0.0007 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3378 0.2725 0.4846 -0.0022 0.1830 0.0021  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3510 0.2774 0.4934 -0.0036 0.1985 -0.0040 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3440 0.2621 0.4847 -0.0026 0.2054 -0.0063 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.3245 0.2633 0.4941 0.0026  0.1795 0.0103  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3202 0.2672 0.4920 0.0015  0.1642 0.0162  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3248 0.2797 0.5055 0.0000  0.1596 0.0192  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3379 0.2837 0.5004 0.0006  0.1548 0.0180  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3339 0.2943 0.5137 -0.0027 0.1460 0.0235  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3480 0.2993 0.5088 -0.0021 0.1418 0.0222  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3542 0.3123 0.5232 -0.0040 0.1373 0.0247  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3839 0.3455 0.5486 -0.0081 0.1247 0.0279  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3574 0.2849 0.4950 -0.0071 0.2040 -0.0069 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3688 0.2875 0.4968 -0.0110 0.2190 -0.0136 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3829 0.3052 0.5211 -0.0119 0.2268 -0.0128 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3837 0.3128 0.5178 -0.0147 0.2202 -0.0111 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3858 0.2991 0.4852 -0.0184 0.2176 -0.0195 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3823 0.3037 0.4733 -0.0211 0.2057 -0.0170 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4007 0.3044 0.4867 -0.0247 0.2322 -0.0262 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3790 0.2966 0.5319 -0.0093 0.2418 -0.0140 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3773 0.2983 0.5425 -0.0098 0.2517 -0.0132 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3636 0.2991 0.5511 -0.0058 0.2402 -0.0040 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3650 0.3056 0.5688 -0.0004 0.2315 0.0022  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3529 0.2948 0.5391 -0.0094 0.2381 -0.0027 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3529 0.3076 0.5576 -0.0072 0.2255 0.0057  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3567 0.3135 0.5427 -0.0108 0.2094 0.0057  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3509 0.3146 0.5411 -0.0128 0.2022 0.0093  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3726 0.3340 0.5942 -0.0080 0.2332 0.0088  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4436 0.4040 0.6894 -0.0031 0.2494 0.0099  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4631 0.4301 0.7363 0.0032  0.2464 0.0174  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4666 0.4183 0.7029 -0.0063 0.2672 0.0029  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3558 0.3061 0.5222 -0.0116 0.2050 0.0016  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3570 0.3082 0.5072 -0.0142 0.1921 0.0012  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3512 0.3021 0.5007 -0.0111 0.1820 0.0026  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3426 0.2896 0.4952 -0.0082 0.1860 0.0021  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3718 0.3166 0.4974 -0.0198 0.1958 -0.0044 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3935 0.3384 0.5142 -0.0250 0.2033 -0.0053 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4052 0.3567 0.5331 -0.0262 0.1981 -0.0010 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4122 0.3497 0.5182 -0.0301 0.2151 -0.0104 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4173 0.3688 0.5395 -0.0317 0.2046 -0.0010 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4234 0.3605 0.5209 -0.0366 0.2213 -0.0109 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4353 0.3798 0.5418 -0.0370 0.2162 -0.0058 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4487 0.3929 0.5466 -0.0439 0.2224 -0.0054 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.3329 0.2870 0.4780 -0.0121 0.1697 0.0045  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.3189 0.2721 0.4591 -0.0108 0.1603 0.0052  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.3234 0.2737 0.4446 -0.0136 0.1557 0.0014  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.3296 0.2817 0.4498 -0.0158 0.1529 0.0019  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3097 0.2692 0.4644 -0.0103 0.1507 0.0114  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3374 0.2951 0.4809 -0.0118 0.1396 0.0112  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3544 0.3176 0.5106 -0.0131 0.1299 0.0179  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3805 0.3415 0.5243 -0.0176 0.1203 0.0164  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3900 0.3477 0.5227 -0.0196 0.1133 0.0161  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3516 0.3087 0.4843 -0.0173 0.1139 0.0182  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3838 0.3375 0.5039 -0.0243 0.1068 0.0133  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.3265 0.2722 0.4344 -0.0136 0.1558 -0.0018 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.3259 0.2700 0.4195 -0.0156 0.1522 -0.0043 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.3308 0.2737 0.4203 -0.0146 0.1446 -0.0044 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.3244 0.2655 0.4123 -0.0133 0.1444 -0.0044 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.3357 0.2766 0.4169 -0.0178 0.1579 -0.0074 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.3393 0.2813 0.4112 -0.0201 0.1541 -0.0076 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.3363 0.2759 0.4185 -0.0201 0.1672 -0.0084 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.3276 0.2705 0.4147 -0.0156 0.1393 -0.0047 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.3304 0.2704 0.4110 -0.0158 0.1337 -0.0059 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.3311 0.2685 0.4037 -0.0162 0.1338 -0.0086 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.3265 0.2653 0.4009 -0.0165 0.1359 -0.0080 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3372 0.2778 0.4239 -0.0176 0.1270 -0.0036 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3451 0.2887 0.4400 -0.0172 0.1246 0.0006  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3387 0.2814 0.4334 -0.0190 0.1267 -0.0023 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.3163 0.2498 0.3811 -0.0164 0.1315 -0.0111 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.3244 0.2546 0.3851 -0.0162 0.1326 -0.0135 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3356 0.2636 0.4017 -0.0176 0.1302 -0.0132 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3375 0.2649 0.4056 -0.0199 0.1260 -0.0125 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3265 0.2516 0.3774 -0.0168 0.1321 -0.0169 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3519 0.2790 0.3980 -0.0156 0.1349 -0.0170 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3633 0.2909 0.4067 -0.0162 0.1334 -0.0160 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3575 0.2864 0.4041 -0.0141 0.1386 -0.0172 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.3327 0.2605 0.4029 -0.0167 0.1323 -0.0125 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.3342 0.2587 0.4097 -0.0182 0.1306 -0.0120 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3390 0.2545 0.4083 -0.0204 0.1289 -0.0166 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3354 0.2478 0.4065 -0.0237 0.1254 -0.0168 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3310 0.2563 0.4125 -0.0167 0.1332 -0.0093 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3271 0.2506 0.4160 -0.0185 0.1317 -0.0069 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.3401 0.2622 0.4351 -0.0167 0.1338 -0.0039 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3527 0.2721 0.4553 -0.0183 0.1327 -0.0009 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3731 0.2827 0.4777 -0.0190 0.1327 -0.0038 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3369 0.2381 0.4342 -0.0191 0.1339 -0.0105 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3756 0.2826 0.4879 -0.0206 0.1318 -0.0002 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3388 0.2496 0.3996 -0.0195 0.1316 -0.0206 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3548 0.2548 0.4057 -0.0230 0.1315 -0.0263 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3603 0.2597 0.4028 -0.0283 0.1250 -0.0266 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.3789 0.2694 0.4114 -0.0338 0.1231 -0.0307 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3719 0.2665 0.4167 -0.0207 0.1382 -0.0306 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.3802 0.2786 0.4171 -0.0203 0.1387 -0.0309 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3996 0.3071 0.4422 -0.0166 0.1401 -0.0270 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.3981 0.2910 0.4208 -0.0240 0.1385 -0.0347 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4092 0.3166 0.4425 -0.0175 0.1407 -0.0284 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4028 0.3020 0.4241 -0.0219 0.1396 -0.0327 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3536 0.2621 0.4004 -0.0274 0.1218 -0.0219 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3676 0.2778 0.4109 -0.0317 0.1149 -0.0196 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3704 0.2879 0.4276 -0.0328 0.1100 -0.0138 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3785 0.3002 0.4382 -0.0358 0.1037 -0.0095 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3666 0.2809 0.4063 -0.0296 0.1156 -0.0178 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3941 0.3023 0.4204 -0.0292 0.1205 -0.0228 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3989 0.3112 0.4225 -0.0278 0.1206 -0.0202 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4072 0.3051 0.4184 -0.0357 0.1189 -0.0277 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3685 0.2886 0.4361 -0.0305 0.1129 -0.0126 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3681 0.2954 0.4497 -0.0313 0.1101 -0.0073 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3699 0.2954 0.4517 -0.0382 0.1020 -0.0060 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.3712 0.2873 0.4422 -0.0426 0.1005 -0.0106 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3633 0.2917 0.4525 -0.0290 0.1149 -0.0068 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3674 0.3019 0.4620 -0.0396 0.0972 0.0006  24  THR   A N   
135  C CA  . THR   A 18  ? 0.3703 0.3061 0.4679 -0.0473 0.0877 0.0043  24  THR   A CA  
136  C C   . THR   A 18  ? 0.3773 0.3155 0.4872 -0.0494 0.0873 0.0064  24  THR   A C   
137  O O   . THR   A 18  ? 0.3805 0.3202 0.4970 -0.0445 0.0946 0.0058  24  THR   A O   
138  C CB  . THR   A 18  ? 0.3614 0.3078 0.4709 -0.0473 0.0823 0.0127  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.3559 0.3122 0.4867 -0.0421 0.0870 0.0179  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.3692 0.3137 0.4686 -0.0446 0.0833 0.0118  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.3888 0.3280 0.5018 -0.0576 0.0784 0.0096  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4026 0.3452 0.5290 -0.0603 0.0774 0.0126  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3745 0.3310 0.5235 -0.0544 0.0819 0.0198  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3713 0.3294 0.5287 -0.0525 0.0875 0.0201  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4562 0.3985 0.5821 -0.0715 0.0659 0.0156  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.5798 0.5059 0.6813 -0.0792 0.0627 0.0074  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.6295 0.5424 0.7225 -0.0801 0.0682 -0.0001 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.6169 0.5376 0.7014 -0.0870 0.0554 0.0058  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.6520 0.5509 0.7233 -0.0877 0.0655 -0.0071 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.6494 0.5523 0.7132 -0.0927 0.0578 -0.0041 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3478 0.3134 0.5067 -0.0517 0.0803 0.0255  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3367 0.3133 0.5170 -0.0455 0.0874 0.0311  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3349 0.3076 0.5094 -0.0384 0.0999 0.0255  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3271 0.3048 0.5137 -0.0360 0.1073 0.0275  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3523 0.3375 0.5454 -0.0432 0.0845 0.0383  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3898 0.3859 0.6088 -0.0376 0.0926 0.0444  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4072 0.4112 0.6438 -0.0402 0.0915 0.0498  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3846 0.3803 0.6062 -0.0303 0.1019 0.0433  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3369 0.3007 0.4924 -0.0361 0.1022 0.0190  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3336 0.2943 0.4826 -0.0312 0.1121 0.0147  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3302 0.2880 0.4783 -0.0331 0.1144 0.0133  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3237 0.2843 0.4762 -0.0312 0.1218 0.0142  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3532 0.3063 0.4841 -0.0292 0.1129 0.0090  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3925 0.3477 0.5233 -0.0269 0.1122 0.0105  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.4037 0.3646 0.5467 -0.0236 0.1171 0.0139  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4017 0.3520 0.5203 -0.0286 0.1075 0.0083  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3345 0.2859 0.4764 -0.0376 0.1085 0.0113  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3342 0.2820 0.4770 -0.0395 0.1104 0.0109  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3226 0.2787 0.4825 -0.0421 0.1106 0.0168  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3275 0.2839 0.4905 -0.0422 0.1153 0.0181  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3384 0.2746 0.4704 -0.0436 0.1056 0.0064  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3409 0.2685 0.4591 -0.0400 0.1094 0.0008  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3595 0.2824 0.4658 -0.0394 0.1082 -0.0034 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3346 0.2589 0.4514 -0.0366 0.1150 0.0003  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3664 0.2833 0.4653 -0.0355 0.1135 -0.0071 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3544 0.2724 0.4605 -0.0337 0.1172 -0.0043 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3365 0.2630 0.4607 -0.0363 0.1181 0.0043  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3549 0.2701 0.4601 -0.0300 0.1218 -0.0044 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3409 0.2642 0.4622 -0.0333 0.1219 0.0045  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3419 0.2600 0.4552 -0.0300 0.1235 0.0006  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3092 0.2729 0.4814 -0.0446 0.1055 0.0214  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3071 0.2803 0.4988 -0.0470 0.1060 0.0279  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2904 0.2710 0.4923 -0.0419 0.1173 0.0301  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2813 0.2680 0.4967 -0.0435 0.1213 0.0342  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3031 0.2841 0.5076 -0.0512 0.0967 0.0337  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2758 0.2551 0.4709 -0.0366 0.1228 0.0273  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2754 0.2584 0.4755 -0.0326 0.1345 0.0275  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2858 0.2610 0.4660 -0.0307 0.1400 0.0216  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2836 0.2584 0.4607 -0.0276 0.1472 0.0197  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2855 0.2747 0.4995 -0.0289 0.1363 0.0307  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3173 0.3165 0.5541 -0.0312 0.1302 0.0385  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3403 0.3466 0.5940 -0.0322 0.1355 0.0427  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3143 0.3146 0.5516 -0.0333 0.1185 0.0411  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2916 0.2604 0.4596 -0.0330 0.1363 0.0195  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2951 0.2579 0.4470 -0.0321 0.1391 0.0161  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.3183 0.2832 0.4677 -0.0328 0.1487 0.0168  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.3229 0.2908 0.4788 -0.0359 0.1521 0.0200  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2862 0.2434 0.4334 -0.0346 0.1342 0.0163  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2967 0.2488 0.4310 -0.0335 0.1355 0.0147  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.3045 0.2538 0.4295 -0.0300 0.1344 0.0104  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2851 0.2311 0.4193 -0.0352 0.1314 0.0160  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.3213 0.2838 0.4591 -0.0313 0.1531 0.0136  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.3380 0.3004 0.4682 -0.0341 0.1620 0.0134  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.3557 0.3147 0.4715 -0.0367 0.1587 0.0141  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3714 0.3311 0.4843 -0.0411 0.1599 0.0176  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.3576 0.3189 0.4851 -0.0320 0.1696 0.0097  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3824 0.3406 0.4947 -0.0367 0.1780 0.0078  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.3561 0.3218 0.5023 -0.0294 0.1747 0.0111  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.3490 0.3053 0.4584 -0.0340 0.1537 0.0119  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.3482 0.3025 0.4480 -0.0352 0.1501 0.0133  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.3407 0.2920 0.4406 -0.0307 0.1443 0.0108  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.3319 0.2824 0.4329 -0.0278 0.1440 0.0072  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.3419 0.2965 0.4286 -0.0386 0.1552 0.0124  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.3569 0.3116 0.4349 -0.0403 0.1509 0.0150  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3744 0.3307 0.4513 -0.0438 0.1473 0.0213  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.3517 0.3057 0.4241 -0.0382 0.1491 0.0125  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3769 0.3346 0.4494 -0.0439 0.1433 0.0236  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3646 0.3209 0.4339 -0.0406 0.1446 0.0179  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.3481 0.3002 0.4192 -0.0346 0.1505 0.0073  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3690 0.3265 0.4343 -0.0397 0.1421 0.0178  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.3586 0.3108 0.4234 -0.0342 0.1484 0.0066  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3587 0.3140 0.4214 -0.0365 0.1443 0.0117  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.3344 0.2836 0.4338 -0.0303 0.1402 0.0130  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.3253 0.2707 0.4241 -0.0265 0.1369 0.0103  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.3345 0.2802 0.4328 -0.0264 0.1355 0.0144  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.3351 0.2821 0.4368 -0.0290 0.1346 0.0202  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.3110 0.2514 0.4155 -0.0251 0.1337 0.0076  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.3434 0.2812 0.4555 -0.0272 0.1319 0.0108  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3568 0.2901 0.4713 -0.0260 0.1311 0.0134  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3715 0.3044 0.4918 -0.0282 0.1305 0.0185  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.3486 0.2793 0.4606 -0.0229 0.1315 0.0114  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.3222 0.2676 0.4172 -0.0238 0.1352 0.0127  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.3165 0.2638 0.4151 -0.0231 0.1338 0.0179  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.3109 0.2535 0.4125 -0.0181 0.1344 0.0138  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.3116 0.2549 0.4071 -0.0169 0.1356 0.0098  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.3358 0.2900 0.4270 -0.0270 0.1337 0.0216  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.4074 0.3665 0.5045 -0.0281 0.1304 0.0302  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.4051 0.3618 0.5138 -0.0235 0.1298 0.0322  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.4365 0.4017 0.5267 -0.0340 0.1288 0.0353  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2938 0.2305 0.4044 -0.0156 0.1345 0.0146  36  SER   A N   
241  C CA  A SER   A 30  ? 0.3066 0.2366 0.4196 -0.0114 0.1373 0.0099  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.3040 0.2340 0.4165 -0.0114 0.1373 0.0097  36  SER   A CA  
243  C C   . SER   A 30  ? 0.3013 0.2373 0.4170 -0.0092 0.1386 0.0130  36  SER   A C   
244  O O   . SER   A 30  ? 0.2929 0.2273 0.4041 -0.0073 0.1413 0.0079  36  SER   A O   
245  C CB  A SER   A 30  ? 0.3308 0.2520 0.4538 -0.0097 0.1386 0.0107  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.3209 0.2415 0.4425 -0.0097 0.1389 0.0095  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3702 0.2817 0.4934 -0.0067 0.1432 0.0041  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.3449 0.2688 0.4795 -0.0082 0.1385 0.0184  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2944 0.2385 0.4171 -0.0106 0.1361 0.0223  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2998 0.2519 0.4272 -0.0098 0.1359 0.0273  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2858 0.2417 0.4000 -0.0119 0.1362 0.0227  37  SER   A C   
252  O O   . SER   A 31  ? 0.2884 0.2487 0.4057 -0.0106 0.1372 0.0241  37  SER   A O   
253  C CB  . SER   A 31  ? 0.3236 0.2847 0.4592 -0.0132 0.1311 0.0396  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3707 0.3395 0.4941 -0.0201 0.1274 0.0425  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2829 0.2372 0.3845 -0.0152 0.1356 0.0180  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2878 0.2440 0.3777 -0.0173 0.1365 0.0138  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2906 0.2397 0.3745 -0.0146 0.1389 0.0052  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2850 0.2349 0.3609 -0.0155 0.1398 0.0022  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2923 0.2512 0.3728 -0.0232 0.1355 0.0150  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.3048 0.2711 0.3841 -0.0291 0.1325 0.0231  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2926 0.2588 0.3592 -0.0360 0.1338 0.0224  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2727 0.2376 0.3277 -0.0386 0.1366 0.0172  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2998 0.2645 0.3417 -0.0462 0.1386 0.0167  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2726 0.2389 0.3098 -0.0527 0.1378 0.0213  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2788 0.2402 0.3112 -0.0481 0.1421 0.0113  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2841 0.2260 0.3711 -0.0122 0.1394 0.0018  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2698 0.2054 0.3497 -0.0116 0.1400 -0.0051 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2708 0.2086 0.3453 -0.0141 0.1385 -0.0057 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2633 0.1994 0.3318 -0.0141 0.1384 -0.0091 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2665 0.2000 0.3414 -0.0098 0.1428 -0.0090 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2866 0.2132 0.3525 -0.0108 0.1422 -0.0148 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2990 0.2197 0.3649 -0.0120 0.1406 -0.0169 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3142 0.2415 0.3726 -0.0113 0.1424 -0.0166 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2582 0.1995 0.3358 -0.0164 0.1379 -0.0021 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2724 0.2152 0.3476 -0.0183 0.1387 -0.0027 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2798 0.2220 0.3615 -0.0194 0.1377 -0.0015 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2782 0.2202 0.3649 -0.0203 0.1367 0.0013  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2810 0.2280 0.3513 -0.0214 0.1413 -0.0006 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2987 0.2464 0.3618 -0.0217 0.1425 -0.0021 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3041 0.2539 0.3603 -0.0266 0.1453 -0.0010 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.3076 0.2520 0.3685 -0.0194 0.1433 -0.0063 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2794 0.2219 0.3629 -0.0195 0.1380 -0.0029 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2823 0.2261 0.3741 -0.0208 0.1373 -0.0011 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2970 0.2439 0.3921 -0.0207 0.1412 -0.0008 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.3177 0.2639 0.4108 -0.0190 0.1415 -0.0024 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2784 0.2187 0.3739 -0.0211 0.1320 -0.0020 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2933 0.2359 0.3991 -0.0235 0.1304 0.0008  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2973 0.2341 0.4035 -0.0254 0.1260 -0.0001 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3054 0.2525 0.4192 -0.0237 0.1293 0.0025  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2865 0.2362 0.3867 -0.0226 0.1452 0.0014  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.2833 0.2351 0.3894 -0.0224 0.1514 0.0016  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2835 0.2392 0.4043 -0.0229 0.1505 0.0049  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2760 0.2325 0.3985 -0.0254 0.1492 0.0069  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2891 0.2399 0.3863 -0.0254 0.1593 0.0005  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3010 0.2520 0.4052 -0.0252 0.1685 -0.0003 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2967 0.2446 0.3806 -0.0258 0.1588 -0.0020 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2812 0.2396 0.4136 -0.0208 0.1502 0.0065  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2825 0.2466 0.4321 -0.0213 0.1488 0.0109  43  SER   A CA  
299  C C   . SER   A 37  ? 0.3006 0.2680 0.4631 -0.0191 0.1588 0.0124  43  SER   A C   
300  O O   . SER   A 37  ? 0.2914 0.2552 0.4489 -0.0169 0.1646 0.0096  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2765 0.2417 0.4308 -0.0214 0.1384 0.0130  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2861 0.2512 0.4412 -0.0186 0.1372 0.0134  43  SER   A OG  
303  N N   . SER   A 38  ? 0.3048 0.2786 0.4850 -0.0199 0.1613 0.0167  44  SER   A N   
304  C CA  . SER   A 38  ? 0.3261 0.3033 0.5226 -0.0174 0.1725 0.0186  44  SER   A CA  
305  C C   . SER   A 38  ? 0.3524 0.3355 0.5696 -0.0137 0.1681 0.0243  44  SER   A C   
306  O O   . SER   A 38  ? 0.3669 0.3535 0.5875 -0.0151 0.1555 0.0282  44  SER   A O   
307  C CB  . SER   A 38  ? 0.3396 0.3215 0.5462 -0.0203 0.1786 0.0210  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3643 0.3526 0.5819 -0.0223 0.1678 0.0263  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3680 0.3513 0.5985 -0.0095 0.1785 0.0253  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3897 0.3789 0.6422 -0.0055 0.1743 0.0325  45  THR   A CA  
311  C C   . THR   A 39  ? 0.4167 0.4120 0.6982 -0.0017 0.1864 0.0374  45  THR   A C   
312  O O   . THR   A 39  ? 0.4275 0.4181 0.7071 -0.0014 0.2020 0.0324  45  THR   A O   
313  C CB  . THR   A 39  ? 0.4092 0.3909 0.6512 -0.0024 0.1737 0.0299  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.4261 0.4000 0.6654 0.0002  0.1896 0.0245  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.4187 0.3944 0.6336 -0.0055 0.1642 0.0248  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.4246 0.4301 0.7331 0.0006  0.1795 0.0477  46  THR   A N   
317  C CA  . THR   A 40  ? 0.4334 0.4464 0.7757 0.0052  0.1907 0.0544  46  THR   A CA  
318  C C   . THR   A 40  ? 0.4531 0.4575 0.7993 0.0115  0.2035 0.0517  46  THR   A C   
319  O O   . THR   A 40  ? 0.4589 0.4586 0.8130 0.0142  0.2222 0.0478  46  THR   A O   
320  C CB  . THR   A 40  ? 0.4352 0.4637 0.8069 0.0048  0.1770 0.0681  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4521 0.4803 0.8152 0.0035  0.1607 0.0718  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4338 0.4705 0.8074 -0.0015 0.1697 0.0705  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.4639 0.4645 0.8023 0.0129  0.1944 0.0529  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.4725 0.4637 0.8142 0.0184  0.2053 0.0508  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4963 0.4720 0.8055 0.0162  0.2163 0.0369  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.5124 0.4851 0.7938 0.0107  0.2098 0.0306  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.4729 0.4658 0.8166 0.0197  0.1908 0.0579  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.5017 0.4671 0.8151 0.0200  0.2330 0.0326  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.5247 0.4745 0.8077 0.0165  0.2440 0.0198  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.5269 0.4692 0.7915 0.0164  0.2355 0.0177  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.5307 0.4732 0.8125 0.0214  0.2331 0.0242  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.5486 0.4886 0.8438 0.0195  0.2677 0.0151  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6222 0.5451 0.8840 0.0136  0.2804 0.0014  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6816 0.6036 0.9267 0.0065  0.2883 -0.0050 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6852 0.6188 0.9446 0.0065  0.2860 0.0002  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7008 0.6091 0.9146 -0.0006 0.2971 -0.0159 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.5263 0.4623 0.7578 0.0104  0.2313 0.0096  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.5267 0.4557 0.7386 0.0092  0.2246 0.0065  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.5231 0.4367 0.7229 0.0081  0.2398 -0.0019 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5292 0.4361 0.7261 0.0058  0.2552 -0.0081 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.5172 0.4240 0.7085 0.0087  0.2362 -0.0026 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.5270 0.4177 0.7071 0.0069  0.2504 -0.0106 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.5108 0.3950 0.6631 0.0017  0.2436 -0.0155 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.5092 0.3800 0.6538 0.0003  0.2528 -0.0206 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.5647 0.4500 0.7729 0.0144  0.2610 -0.0061 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.6867 0.5840 0.9216 0.0217  0.2443 0.0091  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4869 0.3800 0.6242 -0.0017 0.2289 -0.0145 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4871 0.3764 0.5992 -0.0071 0.2228 -0.0188 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4828 0.3638 0.5729 -0.0153 0.2326 -0.0278 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4866 0.3696 0.5761 -0.0177 0.2378 -0.0296 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.5055 0.4063 0.6105 -0.0081 0.2067 -0.0152 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.5638 0.4700 0.6775 -0.0039 0.1949 -0.0083 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5955 0.4957 0.7111 -0.0023 0.1963 -0.0071 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5619 0.4774 0.6786 -0.0033 0.1844 -0.0043 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4779 0.3500 0.5490 -0.0208 0.2342 -0.0329 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4865 0.3505 0.5336 -0.0309 0.2415 -0.0407 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4745 0.3470 0.5036 -0.0369 0.2287 -0.0397 52  THR   A C   
358  O O   . THR   A 46  ? 0.4840 0.3592 0.5099 -0.0362 0.2198 -0.0374 52  THR   A O   
359  C CB  . THR   A 46  ? 0.5169 0.3649 0.5549 -0.0343 0.2514 -0.0467 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5323 0.3708 0.5877 -0.0291 0.2662 -0.0482 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5333 0.3728 0.5422 -0.0473 0.2560 -0.0544 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4470 0.3232 0.4648 -0.0432 0.2284 -0.0408 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4227 0.3074 0.4269 -0.0486 0.2165 -0.0383 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4227 0.2995 0.4036 -0.0597 0.2188 -0.0429 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4402 0.3054 0.4094 -0.0665 0.2306 -0.0491 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4146 0.3085 0.4196 -0.0500 0.2121 -0.0348 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4117 0.3122 0.4395 -0.0404 0.2106 -0.0307 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4111 0.3145 0.4079 -0.0535 0.1994 -0.0305 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4226 0.3295 0.4629 -0.0326 0.2003 -0.0262 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4045 0.2871 0.3786 -0.0622 0.2084 -0.0400 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4150 0.2919 0.3679 -0.0740 0.2089 -0.0431 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4209 0.3032 0.3592 -0.0844 0.2053 -0.0412 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.4087 0.3028 0.3549 -0.0812 0.1974 -0.0351 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3978 0.2804 0.3518 -0.0730 0.1995 -0.0397 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4362 0.3087 0.3526 -0.0973 0.2115 -0.0461 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4513 0.3281 0.3504 -0.1097 0.2072 -0.0434 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.4603 0.3354 0.3406 -0.1225 0.2018 -0.0434 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.4861 0.3471 0.3442 -0.1349 0.2102 -0.0505 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.4716 0.3371 0.3586 -0.1160 0.2206 -0.0497 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.4987 0.3664 0.4070 -0.1034 0.2265 -0.0494 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5170 0.4013 0.4399 -0.0970 0.2146 -0.0402 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5258 0.4110 0.4679 -0.0867 0.2208 -0.0404 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5263 0.4233 0.4858 -0.0785 0.2126 -0.0338 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5117 0.4197 0.4726 -0.0785 0.1991 -0.0269 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4976 0.3952 0.4746 -0.0703 0.2182 -0.0339 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4357 0.3247 0.3253 -0.1198 0.1886 -0.0354 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4518 0.3425 0.3305 -0.1296 0.1819 -0.0335 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4584 0.3691 0.3501 -0.1274 0.1667 -0.0218 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4484 0.3693 0.3562 -0.1182 0.1623 -0.0162 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4513 0.3330 0.3362 -0.1229 0.1875 -0.0390 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4923 0.3865 0.4066 -0.1043 0.1808 -0.0332 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.4680 0.3835 0.3557 -0.1344 0.1598 -0.0184 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4775 0.4113 0.3818 -0.1308 0.1476 -0.0076 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4757 0.4101 0.3870 -0.1273 0.1469 -0.0084 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4852 0.4313 0.4006 -0.1324 0.1382 -0.0009 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5102 0.4564 0.4080 -0.1439 0.1364 0.0027  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6047 0.5472 0.4808 -0.1621 0.1336 0.0023  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6377 0.5633 0.4979 -0.1666 0.1430 -0.0084 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6334 0.5896 0.5092 -0.1721 0.1218 0.0133  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4602 0.3821 0.3733 -0.1192 0.1561 -0.0168 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4294 0.3501 0.3497 -0.1143 0.1567 -0.0179 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4042 0.3418 0.3453 -0.1049 0.1489 -0.0096 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4022 0.3460 0.3553 -0.0962 0.1474 -0.0068 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.4273 0.3339 0.3508 -0.1048 0.1668 -0.0257 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4639 0.3475 0.3673 -0.1139 0.1794 -0.0366 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3902 0.3340 0.3358 -0.1066 0.1452 -0.0062 59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.3738 0.3310 0.3391 -0.0972 0.1409 0.0001  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.3726 0.3244 0.3421 -0.0904 0.1454 -0.0036 59  GLN   A C   
409  O O   . GLN   A 53  ? 0.3628 0.3242 0.3442 -0.0865 0.1431 0.0009  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3744 0.3485 0.3473 -0.1042 0.1320 0.0104  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.4176 0.4001 0.3917 -0.1086 0.1259 0.0171  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.4402 0.4410 0.4270 -0.1141 0.1165 0.0293  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4461 0.4516 0.4231 -0.1284 0.1098 0.0346  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.4127 0.4241 0.4221 -0.1036 0.1161 0.0343  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.3776 0.3137 0.3375 -0.0897 0.1524 -0.0112 60  THR   A N   
416  C CA  . THR   A 54  ? 0.3809 0.3102 0.3438 -0.0836 0.1564 -0.0139 60  THR   A CA  
417  C C   . THR   A 54  ? 0.3625 0.2797 0.3253 -0.0763 0.1625 -0.0193 60  THR   A C   
418  O O   . THR   A 54  ? 0.3544 0.2633 0.3095 -0.0797 0.1665 -0.0233 60  THR   A O   
419  C CB  . THR   A 54  ? 0.4169 0.3394 0.3700 -0.0926 0.1580 -0.0156 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.4666 0.3727 0.4056 -0.0986 0.1643 -0.0224 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.4099 0.3448 0.3626 -0.1025 0.1514 -0.0096 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.3488 0.2648 0.3197 -0.0674 0.1635 -0.0190 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.3469 0.2540 0.3217 -0.0600 0.1677 -0.0217 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.3507 0.2579 0.3323 -0.0529 0.1665 -0.0196 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.3493 0.2603 0.3299 -0.0547 0.1648 -0.0174 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.3464 0.2500 0.3347 -0.0456 0.1674 -0.0196 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.3507 0.2536 0.3441 -0.0399 0.1655 -0.0169 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.3531 0.2607 0.3538 -0.0338 0.1624 -0.0157 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.3605 0.2660 0.3655 -0.0320 0.1642 -0.0169 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.3614 0.2522 0.3560 -0.0391 0.1697 -0.0168 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.3679 0.2586 0.3680 -0.0339 0.1661 -0.0121 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.3675 0.2518 0.3537 -0.0461 0.1730 -0.0184 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.3430 0.2557 0.3444 -0.0312 0.1585 -0.0136 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.3270 0.2428 0.3336 -0.0267 0.1552 -0.0128 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.3281 0.2411 0.3348 -0.0246 0.1519 -0.0098 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.3187 0.2294 0.3201 -0.0264 0.1519 -0.0081 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.3234 0.2470 0.3301 -0.0266 0.1537 -0.0137 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.3394 0.2656 0.3422 -0.0268 0.1532 -0.0132 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.3487 0.2779 0.3488 -0.0300 0.1553 -0.0127 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.3506 0.2765 0.3522 -0.0246 0.1513 -0.0136 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3657 0.2977 0.3634 -0.0301 0.1566 -0.0124 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3721 0.2990 0.3685 -0.0255 0.1528 -0.0142 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3816 0.3117 0.3767 -0.0278 0.1561 -0.0136 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3985 0.3296 0.3895 -0.0285 0.1592 -0.0144 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.3222 0.2357 0.3347 -0.0217 0.1487 -0.0083 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.3263 0.2381 0.3382 -0.0214 0.1438 -0.0041 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3188 0.2334 0.3227 -0.0228 0.1407 -0.0055 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2840 0.2015 0.2898 -0.0217 0.1401 -0.0081 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.3251 0.2358 0.3488 -0.0186 0.1414 -0.0001 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3339 0.2445 0.3567 -0.0198 0.1342 0.0059  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3419 0.2487 0.3603 -0.0217 0.1328 0.0103  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3425 0.2565 0.3665 -0.0204 0.1282 0.0074  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.3615 0.2685 0.3764 -0.0244 0.1251 0.0168  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.3519 0.2658 0.3722 -0.0237 0.1203 0.0133  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.3733 0.2840 0.3888 -0.0258 0.1186 0.0184  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.3947 0.3055 0.4049 -0.0304 0.1098 0.0255  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3408 0.2533 0.3351 -0.0256 0.1391 -0.0039 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.3545 0.2673 0.3383 -0.0281 0.1383 -0.0064 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.3553 0.2651 0.3330 -0.0312 0.1315 -0.0022 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.3599 0.2670 0.3304 -0.0344 0.1297 0.0018  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.3810 0.2939 0.3565 -0.0302 0.1435 -0.0084 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.4058 0.3172 0.3686 -0.0330 0.1464 -0.0130 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.3439 0.2545 0.3243 -0.0313 0.1270 -0.0023 66  SER   A N   
464  C CA  . SER   A 60  ? 0.3619 0.2707 0.3370 -0.0359 0.1187 0.0031  66  SER   A CA  
465  C C   . SER   A 60  ? 0.3720 0.2762 0.3265 -0.0427 0.1182 0.0019  66  SER   A C   
466  O O   . SER   A 60  ? 0.3746 0.2773 0.3234 -0.0471 0.1120 0.0087  66  SER   A O   
467  C CB  . SER   A 60  ? 0.3955 0.3063 0.3770 -0.0361 0.1134 0.0035  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.4524 0.3616 0.4281 -0.0366 0.1170 -0.0041 66  SER   A OG  
469  N N   . SER   A 61  ? 0.3702 0.2720 0.3148 -0.0434 0.1257 -0.0062 67  SER   A N   
470  C CA  . SER   A 61  ? 0.3880 0.2842 0.3124 -0.0498 0.1288 -0.0096 67  SER   A CA  
471  C C   . SER   A 61  ? 0.3989 0.2943 0.3160 -0.0523 0.1304 -0.0056 67  SER   A C   
472  O O   . SER   A 61  ? 0.4154 0.3058 0.3140 -0.0589 0.1323 -0.0070 67  SER   A O   
473  C CB  . SER   A 61  ? 0.3883 0.2827 0.3104 -0.0479 0.1386 -0.0188 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.3953 0.2945 0.3273 -0.0427 0.1460 -0.0200 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.3846 0.2837 0.3150 -0.0478 0.1301 -0.0010 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.3825 0.2804 0.3085 -0.0501 0.1305 0.0040  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.4039 0.3021 0.3414 -0.0486 0.1232 0.0134  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.4102 0.3064 0.3461 -0.0502 0.1229 0.0187  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.3894 0.2899 0.3211 -0.0467 0.1393 0.0003  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.4127 0.3140 0.3373 -0.0475 0.1479 -0.0072 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.4399 0.3370 0.3463 -0.0542 0.1512 -0.0071 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.4499 0.3477 0.3532 -0.0539 0.1617 -0.0144 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.4673 0.3607 0.3614 -0.0558 0.1655 -0.0205 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.4612 0.3492 0.3459 -0.0595 0.1583 -0.0203 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.4258 0.3197 0.3211 -0.0544 0.1768 -0.0267 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.4111 0.3118 0.3626 -0.0449 0.1185 0.0156  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.4195 0.3209 0.3878 -0.0415 0.1141 0.0240  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.4135 0.3128 0.3896 -0.0377 0.1212 0.0231  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.4107 0.3070 0.3933 -0.0373 0.1195 0.0304  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.4324 0.3327 0.3972 -0.0467 0.1044 0.0349  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.4864 0.3893 0.4482 -0.0510 0.0952 0.0378  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.5349 0.4368 0.4884 -0.0586 0.0849 0.0494  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.5618 0.4651 0.5045 -0.0663 0.0757 0.0512  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.5587 0.4590 0.4793 -0.0773 0.0686 0.0554  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.5318 0.4281 0.4395 -0.0813 0.0701 0.0586  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.5332 0.4338 0.4425 -0.0856 0.0603 0.0560  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.4075 0.3082 0.3824 -0.0356 0.1290 0.0147  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4140 0.3126 0.3934 -0.0341 0.1353 0.0131  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.3996 0.3006 0.3874 -0.0305 0.1406 0.0069  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.3977 0.3031 0.3848 -0.0295 0.1412 0.0023  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.4451 0.3437 0.4116 -0.0382 0.1393 0.0108  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.5335 0.4277 0.4920 -0.0425 0.1367 0.0175  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.6165 0.5120 0.5612 -0.0469 0.1414 0.0143  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.6884 0.5795 0.6260 -0.0515 0.1409 0.0205  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.7273 0.6158 0.6529 -0.0564 0.1342 0.0268  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3860 0.2831 0.3801 -0.0295 0.1448 0.0068  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3731 0.2713 0.3707 -0.0287 0.1501 0.0012  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3700 0.2699 0.3591 -0.0329 0.1535 -0.0015 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3825 0.2791 0.3665 -0.0357 0.1538 0.0013  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3857 0.2766 0.3927 -0.0270 0.1540 0.0018  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.4051 0.2957 0.4245 -0.0226 0.1518 0.0052  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.4310 0.3243 0.4567 -0.0203 0.1540 0.0016  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.4099 0.2993 0.4373 -0.0206 0.1472 0.0127  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.4216 0.3152 0.4598 -0.0167 0.1513 0.0067  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.4249 0.3169 0.4653 -0.0167 0.1466 0.0139  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3439 0.2499 0.3327 -0.0335 0.1555 -0.0057 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3446 0.2549 0.3291 -0.0375 0.1580 -0.0070 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.3315 0.2434 0.3179 -0.0403 0.1602 -0.0096 72  TYR   A C   
519  O O   . TYR   A 66  ? 0.3312 0.2465 0.3214 -0.0386 0.1596 -0.0113 72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3393 0.2578 0.3228 -0.0365 0.1578 -0.0080 72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3472 0.2639 0.3237 -0.0366 0.1569 -0.0065 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3629 0.2774 0.3329 -0.0402 0.1584 -0.0041 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3682 0.2849 0.3429 -0.0344 0.1548 -0.0076 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.3894 0.3015 0.3502 -0.0418 0.1578 -0.0025 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.3857 0.2997 0.3504 -0.0365 0.1541 -0.0067 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4053 0.3171 0.3625 -0.0403 0.1557 -0.0041 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.4541 0.3625 0.3986 -0.0438 0.1552 -0.0030 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.3266 0.2364 0.3093 -0.0458 0.1624 -0.0095 73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.3302 0.2421 0.3119 -0.0508 0.1635 -0.0117 73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.3369 0.2623 0.3226 -0.0515 0.1613 -0.0102 73  PRO   A C   
531  O O   . PRO   A 67  ? 0.3428 0.2739 0.3302 -0.0508 0.1615 -0.0081 73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.3452 0.2506 0.3210 -0.0575 0.1658 -0.0116 73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.3476 0.2536 0.3229 -0.0560 0.1654 -0.0082 73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.3246 0.2299 0.3028 -0.0488 0.1635 -0.0071 73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.3337 0.2641 0.3218 -0.0530 0.1598 -0.0107 74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.3324 0.2759 0.3279 -0.0530 0.1575 -0.0077 74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.3301 0.2783 0.3244 -0.0604 0.1550 -0.0062 74  VAL   A C   
538  O O   . VAL   A 68  ? 0.3248 0.2652 0.3115 -0.0639 0.1557 -0.0091 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.3436 0.2899 0.3457 -0.0455 0.1567 -0.0081 74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3560 0.3013 0.3588 -0.0405 0.1585 -0.0085 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.3410 0.2800 0.3407 -0.0434 0.1565 -0.0109 74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.3204 0.2816 0.3228 -0.0628 0.1522 -0.0011 75  SER   A N   
543  C CA  . SER   A 69  ? 0.3325 0.3022 0.3364 -0.0702 0.1476 0.0032  75  SER   A CA  
544  C C   . SER   A 69  ? 0.3152 0.2926 0.3309 -0.0635 0.1459 0.0060  75  SER   A C   
545  O O   . SER   A 69  ? 0.3168 0.2983 0.3428 -0.0562 0.1481 0.0070  75  SER   A O   
546  C CB  . SER   A 69  ? 0.3519 0.3331 0.3628 -0.0758 0.1453 0.0092  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.4159 0.3969 0.4172 -0.0880 0.1415 0.0106  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.3032 0.2808 0.3165 -0.0659 0.1430 0.0068  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2958 0.2795 0.3208 -0.0595 0.1415 0.0098  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.3185 0.3119 0.3473 -0.0660 0.1354 0.0171  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.3205 0.3125 0.3371 -0.0765 0.1324 0.0177  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2976 0.2709 0.3186 -0.0526 0.1446 0.0038  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.3321 0.2954 0.3396 -0.0573 0.1457 -0.0006 76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.3487 0.3006 0.3468 -0.0577 0.1500 -0.0063 76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.3391 0.3043 0.3439 -0.0617 0.1433 0.0014  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.3681 0.3100 0.3560 -0.0616 0.1532 -0.0106 76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.3578 0.3130 0.3497 -0.0664 0.1464 -0.0034 76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.3589 0.3023 0.3432 -0.0658 0.1520 -0.0098 76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.3238 0.3265 0.3690 -0.0606 0.1335 0.0230  77  SER   A N   
560  C CA  . SER   A 71  ? 0.3381 0.3514 0.3899 -0.0663 0.1266 0.0322  77  SER   A CA  
561  C C   . SER   A 71  ? 0.3456 0.3519 0.3850 -0.0696 0.1251 0.0299  77  SER   A C   
562  O O   . SER   A 71  ? 0.3496 0.3442 0.3813 -0.0645 0.1301 0.0217  77  SER   A O   
563  C CB  . SER   A 71  ? 0.3554 0.3797 0.4314 -0.0584 0.1261 0.0397  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.3991 0.4150 0.4780 -0.0483 0.1314 0.0339  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.3444 0.3583 0.3824 -0.0787 0.1182 0.0379  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.3680 0.3762 0.3943 -0.0828 0.1171 0.0367  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.3733 0.3821 0.4142 -0.0719 0.1183 0.0383  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.3641 0.3811 0.4251 -0.0648 0.1174 0.0440  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3877 0.4042 0.4064 -0.0973 0.1085 0.0459  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4420 0.4529 0.4395 -0.1103 0.1084 0.0416  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.4928 0.5106 0.4785 -0.1271 0.0993 0.0502  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.5600 0.5649 0.5180 -0.1401 0.1027 0.0414  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.5959 0.6070 0.5391 -0.1594 0.0931 0.0494  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3848 0.3845 0.4170 -0.0706 0.1213 0.0331  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3828 0.3827 0.4286 -0.0614 0.1220 0.0347  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3647 0.3771 0.4283 -0.0615 0.1154 0.0474  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3561 0.3763 0.4163 -0.0715 0.1085 0.0561  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.4049 0.3958 0.4369 -0.0643 0.1246 0.0297  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4233 0.4052 0.4373 -0.0696 0.1293 0.0213  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3988 0.3875 0.4095 -0.0776 0.1250 0.0257  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.3457 0.3598 0.4285 -0.0509 0.1178 0.0487  80  SER   A N   
582  C CA  . SER   A 74  ? 0.3392 0.3646 0.4441 -0.0489 0.1132 0.0611  80  SER   A CA  
583  C C   . SER   A 74  ? 0.3214 0.3421 0.4432 -0.0371 0.1183 0.0595  80  SER   A C   
584  O O   . SER   A 74  ? 0.3168 0.3259 0.4309 -0.0317 0.1242 0.0487  80  SER   A O   
585  C CB  . SER   A 74  ? 0.3687 0.4064 0.4852 -0.0514 0.1102 0.0687  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.4156 0.4496 0.5268 -0.0491 0.1158 0.0603  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.3073 0.3364 0.4520 -0.0339 0.1155 0.0709  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.3141 0.3382 0.4770 -0.0235 0.1208 0.0706  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.3170 0.3421 0.4937 -0.0162 0.1281 0.0679  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.3126 0.3502 0.5071 -0.0167 0.1260 0.0780  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.3045 0.3379 0.4886 -0.0239 0.1148 0.0861  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.3203 0.3479 0.5033 -0.0242 0.1124 0.0886  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3212 0.3564 0.5332 -0.0204 0.1095 0.1034  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3251 0.3366 0.5000 -0.0176 0.1204 0.0748  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.3186 0.3312 0.4872 -0.0105 0.1365 0.0550  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.3283 0.3396 0.5055 -0.0045 0.1450 0.0506  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3586 0.3575 0.5436 0.0038  0.1536 0.0444  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3670 0.3544 0.5385 0.0039  0.1538 0.0369  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3399 0.3468 0.4953 -0.0078 0.1468 0.0407  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3583 0.3777 0.5120 -0.0152 0.1410 0.0474  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3381 0.3371 0.4938 -0.0018 0.1571 0.0318  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3839 0.4011 0.5163 -0.0233 0.1350 0.0449  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3619 0.3631 0.5696 0.0103  0.1610 0.0479  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3774 0.3649 0.5924 0.0177  0.1714 0.0411  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3663 0.3395 0.5582 0.0177  0.1788 0.0253  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.3552 0.3310 0.5397 0.0163  0.1817 0.0218  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3861 0.3796 0.6325 0.0245  0.1793 0.0489  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4204 0.3974 0.6743 0.0318  0.1925 0.0408  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4403 0.4092 0.7029 0.0345  0.1922 0.0429  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4458 0.4144 0.6966 0.0350  0.2056 0.0307  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4585 0.4101 0.7271 0.0403  0.2052 0.0347  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.4637 0.4151 0.7192 0.0404  0.2191 0.0223  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.4599 0.4022 0.7235 0.0429  0.2187 0.0238  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.3636 0.3219 0.5440 0.0182  0.1808 0.0169  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.3779 0.3225 0.5352 0.0165  0.1852 0.0035  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.3961 0.3247 0.5566 0.0205  0.1962 -0.0043 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.3863 0.3082 0.5543 0.0222  0.1960 -0.0031 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.3808 0.3228 0.5174 0.0110  0.1758 0.0003  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.4003 0.3285 0.5159 0.0089  0.1790 -0.0116 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.3637 0.3181 0.4938 0.0065  0.1679 0.0052  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.4133 0.3347 0.5671 0.0213  0.2066 -0.0124 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.4316 0.3354 0.5842 0.0236  0.2195 -0.0218 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.4516 0.3402 0.5860 0.0195  0.2163 -0.0297 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.4597 0.3505 0.5766 0.0142  0.2058 -0.0307 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.4766 0.3747 0.6161 0.0221  0.2297 -0.0303 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.5377 0.4486 0.6989 0.0268  0.2367 -0.0235 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.6117 0.5244 0.8063 0.0348  0.2457 -0.0168 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.6359 0.5342 0.8349 0.0373  0.2518 -0.0210 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.6117 0.5406 0.8297 0.0384  0.2466 -0.0066 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.4558 0.3284 0.5946 0.0215  0.2261 -0.0356 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.4786 0.3353 0.5998 0.0163  0.2237 -0.0437 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.4864 0.3363 0.5756 0.0080  0.2204 -0.0532 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.4958 0.3454 0.5750 0.0067  0.2261 -0.0574 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.4878 0.3254 0.6165 0.0190  0.2378 -0.0505 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.4847 0.3290 0.5593 0.0021  0.2114 -0.0559 87  SER   A N   
636  C CA  . SER   A 81  ? 0.5006 0.3386 0.5472 -0.0065 0.2064 -0.0629 87  SER   A CA  
637  C C   . SER   A 81  ? 0.5267 0.3507 0.5632 -0.0124 0.2031 -0.0682 87  SER   A C   
638  O O   . SER   A 81  ? 0.5333 0.3529 0.5848 -0.0092 0.2050 -0.0663 87  SER   A O   
639  C CB  . SER   A 81  ? 0.4952 0.3496 0.5379 -0.0079 0.1937 -0.0560 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.4874 0.3485 0.5379 -0.0078 0.1836 -0.0498 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.5470 0.3646 0.5591 -0.0217 0.1972 -0.0736 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.5667 0.3730 0.5682 -0.0292 0.1916 -0.0776 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.5414 0.3598 0.5580 -0.0271 0.1800 -0.0684 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.5399 0.3504 0.5553 -0.0314 0.1765 -0.0699 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.6389 0.4393 0.6118 -0.0405 0.1856 -0.0828 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.7356 0.5528 0.7057 -0.0404 0.1759 -0.0758 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.8723 0.6859 0.8172 -0.0513 0.1685 -0.0782 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.8957 0.7055 0.8326 -0.0592 0.1595 -0.0782 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.9136 0.7290 0.8475 -0.0525 0.1711 -0.0790 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.5137 0.3506 0.5437 -0.0212 0.1748 -0.0591 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.4948 0.3432 0.5372 -0.0197 0.1655 -0.0508 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.4761 0.3293 0.5408 -0.0125 0.1687 -0.0443 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.4871 0.3432 0.5602 -0.0128 0.1634 -0.0395 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.4840 0.3476 0.5240 -0.0199 0.1572 -0.0452 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.5002 0.3609 0.5207 -0.0262 0.1537 -0.0493 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.5201 0.3768 0.5307 -0.0337 0.1460 -0.0505 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.5164 0.3789 0.5291 -0.0253 0.1576 -0.0509 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.5408 0.3960 0.5342 -0.0404 0.1413 -0.0522 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.5384 0.3985 0.5331 -0.0317 0.1537 -0.0533 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.5584 0.4148 0.5433 -0.0393 0.1452 -0.0536 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.5896 0.4445 0.5572 -0.0463 0.1401 -0.0541 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.4495 0.3048 0.5248 -0.0064 0.1767 -0.0429 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.4212 0.2830 0.5196 0.0000  0.1785 -0.0343 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.4252 0.2796 0.5353 0.0054  0.1909 -0.0364 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.4328 0.2851 0.5352 0.0056  0.1973 -0.0417 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.3935 0.2745 0.4991 0.0025  0.1728 -0.0251 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.3721 0.2621 0.4687 -0.0016 0.1627 -0.0224 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.3681 0.2630 0.4516 -0.0040 0.1599 -0.0247 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.3639 0.2578 0.4669 -0.0029 0.1568 -0.0167 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.3664 0.2690 0.4448 -0.0069 0.1524 -0.0219 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.3655 0.2675 0.4622 -0.0062 0.1497 -0.0144 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.3699 0.2759 0.4551 -0.0079 0.1479 -0.0171 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3600 0.2728 0.4413 -0.0105 0.1426 -0.0149 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.4217 0.2744 0.5534 0.0104  0.1946 -0.0306 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.4191 0.2679 0.5682 0.0172  0.2071 -0.0301 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.4075 0.2766 0.5697 0.0212  0.2043 -0.0201 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.4021 0.2852 0.5586 0.0184  0.1932 -0.0144 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.4213 0.2627 0.5911 0.0209  0.2098 -0.0250 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.4291 0.2804 0.5981 0.0175  0.1961 -0.0171 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.4156 0.2718 0.5593 0.0106  0.1875 -0.0223 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.3934 0.2640 0.5735 0.0274  0.2146 -0.0179 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.3845 0.2750 0.5790 0.0303  0.2115 -0.0073 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.3804 0.2860 0.5898 0.0303  0.1992 0.0073  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.3820 0.2834 0.6067 0.0328  0.1991 0.0128  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.3784 0.2680 0.5960 0.0375  0.2253 -0.0056 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.3680 0.2890 0.5694 0.0263  0.1889 0.0127  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3453 0.2792 0.5542 0.0239  0.1773 0.0252  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3295 0.2807 0.5349 0.0202  0.1700 0.0317  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3381 0.2903 0.5330 0.0194  0.1731 0.0256  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3636 0.2902 0.5542 0.0188  0.1709 0.0204  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3841 0.3141 0.5498 0.0129  0.1651 0.0143  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3855 0.3040 0.5338 0.0095  0.1638 0.0052  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3719 0.2966 0.5043 0.0043  0.1564 0.0044  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3813 0.3072 0.4993 0.0024  0.1562 -0.0012 93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3529 0.2827 0.4594 -0.0017 0.1507 -0.0017 93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.3681 0.2906 0.4837 0.0044  0.1624 -0.0061 93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.3195 0.2832 0.5307 0.0166  0.1601 0.0436  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.3168 0.2941 0.5183 0.0105  0.1524 0.0480  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2981 0.2708 0.4745 0.0046  0.1474 0.0412  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2940 0.2634 0.4688 0.0028  0.1438 0.0431  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.3176 0.3102 0.5340 0.0072  0.1437 0.0642  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.3267 0.3283 0.5718 0.0124  0.1469 0.0743  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3332 0.3459 0.5820 0.0112  0.1471 0.0768  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3384 0.3372 0.6091 0.0189  0.1507 0.0814  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3419 0.3643 0.6206 0.0164  0.1507 0.0869  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3416 0.3493 0.6431 0.0247  0.1547 0.0918  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3531 0.3732 0.6592 0.0235  0.1549 0.0945  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3764 0.4065 0.7166 0.0296  0.1595 0.1056  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2896 0.2627 0.4488 0.0016  0.1473 0.0343  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2889 0.2593 0.4275 -0.0037 0.1433 0.0290  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2996 0.2815 0.4324 -0.0109 0.1365 0.0361  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.3093 0.2991 0.4443 -0.0125 0.1359 0.0392  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.3004 0.2623 0.4239 -0.0028 0.1477 0.0173  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.3102 0.2693 0.4165 -0.0073 0.1442 0.0127  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.3447 0.2952 0.4389 -0.0063 0.1473 0.0030  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.3593 0.3017 0.4543 -0.0033 0.1514 -0.0020 95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.3466 0.2980 0.4287 -0.0095 0.1455 0.0005  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.2875 0.2700 0.4125 -0.0161 0.1318 0.0388  96  SER   A N   
719  C CA  . SER   A 90  ? 0.2904 0.2809 0.4055 -0.0249 0.1262 0.0443  96  SER   A CA  
720  C C   . SER   A 90  ? 0.2915 0.2774 0.3863 -0.0288 0.1281 0.0352  96  SER   A C   
721  O O   . SER   A 90  ? 0.2858 0.2628 0.3749 -0.0249 0.1322 0.0262  96  SER   A O   
722  C CB  . SER   A 90  ? 0.3122 0.3042 0.4272 -0.0294 0.1217 0.0512  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.3384 0.3209 0.4469 -0.0276 0.1247 0.0441  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.2771 0.2686 0.3614 -0.0370 0.1250 0.0381  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2861 0.2722 0.3519 -0.0414 0.1277 0.0301  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2873 0.2688 0.3526 -0.0356 0.1322 0.0223  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2800 0.2539 0.3353 -0.0349 0.1359 0.0145  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2988 0.2775 0.3551 -0.0430 0.1301 0.0256  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.3246 0.3073 0.3790 -0.0497 0.1263 0.0331  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3525 0.3359 0.3906 -0.0605 0.1254 0.0343  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.3260 0.3119 0.3921 -0.0481 0.1229 0.0405  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3440 0.3319 0.3834 -0.0655 0.1210 0.0428  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3352 0.3249 0.3924 -0.0579 0.1192 0.0472  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.2857 0.2725 0.3632 -0.0318 0.1322 0.0255  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.2910 0.2744 0.3682 -0.0272 0.1367 0.0195  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.3027 0.2914 0.3753 -0.0321 0.1359 0.0209  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.3264 0.3254 0.4070 -0.0360 0.1320 0.0292  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.2753 0.2584 0.3681 -0.0194 0.1400 0.0201  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.3013 0.2784 0.3908 -0.0152 0.1457 0.0126  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.3084 0.2758 0.3834 -0.0152 0.1466 0.0047  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.3136 0.2889 0.4173 -0.0086 0.1510 0.0125  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.2888 0.2708 0.3497 -0.0323 0.1391 0.0136  99  MET   A N   
743  C CA  . MET   A 93  ? 0.2945 0.2800 0.3503 -0.0374 0.1388 0.0143  99  MET   A CA  
744  C C   . MET   A 93  ? 0.3117 0.2957 0.3712 -0.0321 0.1433 0.0110  99  MET   A C   
745  O O   . MET   A 93  ? 0.3342 0.3092 0.3875 -0.0281 0.1466 0.0044  99  MET   A O   
746  C CB  . MET   A 93  ? 0.2981 0.2760 0.3366 -0.0434 0.1396 0.0093  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.3068 0.2841 0.3382 -0.0496 0.1371 0.0111  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.3704 0.3350 0.3834 -0.0543 0.1420 0.0029  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.4185 0.3758 0.4368 -0.0443 0.1459 -0.0025 99  MET   A CE  
750  N N   . LEU   A 94  ? 0.2881 0.2811 0.3575 -0.0328 0.1435 0.0160  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.2816 0.2730 0.3535 -0.0287 0.1490 0.0127  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.2794 0.2705 0.3415 -0.0340 0.1493 0.0113  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.2618 0.2592 0.3226 -0.0413 0.1452 0.0159  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.2699 0.2706 0.3621 -0.0244 0.1518 0.0185  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2826 0.2827 0.3878 -0.0184 0.1529 0.0203  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2792 0.2862 0.4060 -0.0131 0.1588 0.0248  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2880 0.2744 0.3828 -0.0140 0.1567 0.0111  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.2810 0.2651 0.3367 -0.0310 0.1542 0.0057  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2864 0.2683 0.3333 -0.0349 0.1556 0.0041  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.3035 0.2848 0.3534 -0.0308 0.1620 0.0022  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2958 0.2731 0.3477 -0.0254 0.1656 -0.0009 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2965 0.2664 0.3281 -0.0360 0.1550 -0.0013 101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.3101 0.2951 0.3594 -0.0345 0.1639 0.0039  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.3305 0.3142 0.3797 -0.0321 0.1708 0.0019  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3579 0.3283 0.3887 -0.0326 0.1707 -0.0038 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3670 0.3336 0.3890 -0.0369 0.1676 -0.0036 102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.3280 0.3215 0.3843 -0.0366 0.1725 0.0069  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3229 0.3148 0.3783 -0.0347 0.1811 0.0046  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.3280 0.3367 0.4049 -0.0373 0.1702 0.0149  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.3672 0.3303 0.3927 -0.0286 0.1739 -0.0082 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.3720 0.3242 0.3818 -0.0296 0.1723 -0.0116 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.3694 0.3143 0.3729 -0.0269 0.1749 -0.0160 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.3873 0.3340 0.3988 -0.0235 0.1783 -0.0175 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.3523 0.2886 0.3416 -0.0290 0.1727 -0.0176 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.3480 0.2766 0.3277 -0.0289 0.1738 -0.0216 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.3422 0.2674 0.3231 -0.0269 0.1676 -0.0224 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.3311 0.2569 0.3149 -0.0266 0.1618 -0.0197 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.3568 0.2786 0.3198 -0.0336 0.1733 -0.0214 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.3901 0.3033 0.3395 -0.0360 0.1734 -0.0252 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.4160 0.3263 0.3626 -0.0359 0.1821 -0.0307 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.4219 0.3289 0.3605 -0.0391 0.1661 -0.0240 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.4358 0.3367 0.3664 -0.0402 0.1798 -0.0337 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.4504 0.3502 0.3762 -0.0425 0.1692 -0.0291 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.3497 0.2706 0.3283 -0.0260 0.1700 -0.0264 105 SER   A N   
785  C CA  . SER   A 99  ? 0.3553 0.2723 0.3339 -0.0252 0.1649 -0.0277 105 SER   A CA  
786  C C   . SER   A 99  ? 0.3713 0.2795 0.3392 -0.0274 0.1688 -0.0334 105 SER   A C   
787  O O   . SER   A 99  ? 0.3725 0.2787 0.3388 -0.0274 0.1776 -0.0369 105 SER   A O   
788  C CB  . SER   A 99  ? 0.3297 0.2528 0.3241 -0.0209 0.1638 -0.0262 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.3444 0.2679 0.3468 -0.0181 0.1697 -0.0286 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.3768 0.2795 0.3383 -0.0297 0.1629 -0.0343 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.3823 0.2751 0.3316 -0.0336 0.1648 -0.0399 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.3892 0.2819 0.3469 -0.0319 0.1589 -0.0396 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.3907 0.2904 0.3592 -0.0292 0.1527 -0.0344 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.4037 0.2904 0.3325 -0.0415 0.1604 -0.0393 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.4636 0.3484 0.3818 -0.0441 0.1684 -0.0410 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.4871 0.3659 0.3833 -0.0529 0.1640 -0.0394 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.5033 0.3740 0.3844 -0.0597 0.1600 -0.0418 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.4965 0.3787 0.3901 -0.0540 0.1640 -0.0352 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.4024 0.2867 0.3559 -0.0337 0.1614 -0.0450 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.3937 0.2789 0.3575 -0.0318 0.1561 -0.0439 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.3955 0.2854 0.3609 -0.0338 0.1448 -0.0380 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.4018 0.2984 0.3819 -0.0297 0.1417 -0.0343 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.4082 0.2809 0.3621 -0.0358 0.1605 -0.0512 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.4204 0.2872 0.3671 -0.0359 0.1726 -0.0568 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.4013 0.2742 0.3416 -0.0373 0.1708 -0.0529 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.3938 0.2808 0.3452 -0.0401 0.1393 -0.0364 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.3801 0.2720 0.3353 -0.0420 0.1286 -0.0293 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.3595 0.2605 0.3287 -0.0364 0.1274 -0.0231 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.3461 0.2513 0.3227 -0.0366 0.1203 -0.0171 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.3522 0.2562 0.3255 -0.0320 0.1344 -0.0244 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.3410 0.2517 0.3254 -0.0279 0.1343 -0.0199 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.3241 0.2397 0.3234 -0.0234 0.1352 -0.0194 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.3185 0.2381 0.3257 -0.0211 0.1355 -0.0164 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.3479 0.2599 0.3297 -0.0268 0.1406 -0.0210 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.3753 0.2836 0.3436 -0.0311 0.1404 -0.0200 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.3782 0.2854 0.3434 -0.0338 0.1339 -0.0154 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.3922 0.2995 0.3544 -0.0318 0.1468 -0.0231 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.3228 0.2372 0.3250 -0.0227 0.1366 -0.0226 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.3287 0.2472 0.3436 -0.0196 0.1366 -0.0215 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.3400 0.2613 0.3619 -0.0196 0.1317 -0.0171 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.3538 0.2731 0.3726 -0.0225 0.1264 -0.0153 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.3333 0.2478 0.3489 -0.0200 0.1372 -0.0247 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.3569 0.2692 0.3730 -0.0176 0.1455 -0.0286 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3276 0.2533 0.3581 -0.0172 0.1339 -0.0152 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.3194 0.2471 0.3585 -0.0165 0.1319 -0.0114 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.3327 0.2601 0.3721 -0.0157 0.1342 -0.0094 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.3382 0.2665 0.3867 -0.0143 0.1358 -0.0070 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.3171 0.2424 0.3472 -0.0168 0.1353 -0.0105 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2989 0.2225 0.3283 -0.0166 0.1378 -0.0089 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2829 0.2074 0.3152 -0.0161 0.1435 -0.0108 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2709 0.1981 0.3012 -0.0168 0.1451 -0.0130 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2686 0.1902 0.3056 -0.0156 0.1467 -0.0095 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2869 0.2072 0.3235 -0.0169 0.1528 -0.0121 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2947 0.2131 0.3217 -0.0202 0.1554 -0.0140 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.3007 0.2166 0.3244 -0.0205 0.1546 -0.0127 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.3111 0.2274 0.3576 -0.0151 0.1573 -0.0109 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.3131 0.2330 0.3692 -0.0134 0.1573 -0.0101 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.3350 0.2448 0.3769 -0.0178 0.1654 -0.0142 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.3154 0.2330 0.3856 -0.0104 0.1609 -0.0072 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.2807 0.2013 0.3033 -0.0236 0.1577 -0.0161 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.3008 0.2205 0.3150 -0.0285 0.1599 -0.0173 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.3155 0.2281 0.3266 -0.0321 0.1662 -0.0201 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2961 0.2084 0.3096 -0.0322 0.1687 -0.0211 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2967 0.2246 0.3090 -0.0310 0.1571 -0.0163 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.3246 0.2538 0.3295 -0.0377 0.1579 -0.0163 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.3405 0.2693 0.3429 -0.0382 0.1577 -0.0157 114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.3327 0.2715 0.3398 -0.0400 0.1544 -0.0132 114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.3351 0.2405 0.3408 -0.0351 0.1699 -0.0216 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.3613 0.2568 0.3628 -0.0388 0.1779 -0.0254 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.3838 0.2749 0.3726 -0.0470 0.1799 -0.0279 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.3981 0.2910 0.3851 -0.0477 0.1766 -0.0260 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.3970 0.2837 0.4076 -0.0338 0.1825 -0.0250 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.4747 0.3641 0.5000 -0.0268 0.1819 -0.0221 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.5459 0.4268 0.5824 -0.0226 0.1868 -0.0202 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.6042 0.4743 0.6403 -0.0248 0.1986 -0.0252 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.6169 0.4855 0.6646 -0.0215 0.2050 -0.0255 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.6048 0.4621 0.6496 -0.0245 0.2177 -0.0313 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.5982 0.4762 0.6605 -0.0157 0.1995 -0.0201 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.3930 0.2773 0.3718 -0.0542 0.1858 -0.0322 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.4188 0.2959 0.3830 -0.0642 0.1887 -0.0355 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.4428 0.3023 0.4042 -0.0655 0.2006 -0.0415 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.4395 0.2951 0.4135 -0.0576 0.2056 -0.0416 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.4315 0.3147 0.3837 -0.0739 0.1853 -0.0354 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.4497 0.3289 0.3973 -0.0764 0.1916 -0.0388 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4715 0.3201 0.4175 -0.0758 0.2056 -0.0463 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.5098 0.3391 0.4512 -0.0783 0.2191 -0.0535 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.5172 0.3430 0.4588 -0.0779 0.2271 -0.0572 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5378 0.3510 0.4868 -0.0737 0.2390 -0.0611 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5578 0.3757 0.4779 -0.0925 0.2225 -0.0590 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6152 0.4399 0.5168 -0.1053 0.2173 -0.0596 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.7006 0.5160 0.5812 -0.1206 0.2181 -0.0636 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.7094 0.5370 0.5837 -0.1281 0.2071 -0.0586 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.7260 0.5192 0.5962 -0.1258 0.2316 -0.0725 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.5012 0.3383 0.4363 -0.0819 0.2211 -0.0554 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.4954 0.3298 0.4283 -0.0832 0.2285 -0.0586 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4775 0.3199 0.4329 -0.0701 0.2280 -0.0543 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4909 0.3286 0.4494 -0.0691 0.2373 -0.0573 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.5039 0.3461 0.4189 -0.0947 0.2221 -0.0575 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5506 0.3855 0.4420 -0.1101 0.2218 -0.0611 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.5654 0.4123 0.4531 -0.1150 0.2089 -0.0551 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.5872 0.4042 0.4579 -0.1220 0.2331 -0.0698 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.5852 0.4223 0.4509 -0.1300 0.2112 -0.0595 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.6062 0.4242 0.4592 -0.1353 0.2257 -0.0690 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4409 0.2955 0.4113 -0.0611 0.2175 -0.0475 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.4176 0.2799 0.4079 -0.0504 0.2155 -0.0430 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.3839 0.2616 0.3807 -0.0459 0.2020 -0.0365 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.3845 0.2663 0.3763 -0.0476 0.1950 -0.0345 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.3643 0.2495 0.3728 -0.0404 0.1994 -0.0334 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.3520 0.2494 0.3671 -0.0361 0.1887 -0.0283 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.3500 0.2544 0.3541 -0.0424 0.1835 -0.0275 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.3605 0.2647 0.3589 -0.0472 0.1866 -0.0287 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.3526 0.2538 0.3839 -0.0295 0.1890 -0.0257 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.3670 0.2790 0.4018 -0.0274 0.1793 -0.0218 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.3403 0.2381 0.3862 -0.0228 0.1905 -0.0233 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.3407 0.2516 0.3430 -0.0425 0.1758 -0.0247 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.3348 0.2541 0.3315 -0.0472 0.1698 -0.0218 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.3397 0.2678 0.3471 -0.0417 0.1639 -0.0178 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.3311 0.2642 0.3377 -0.0446 0.1615 -0.0153 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.3299 0.2516 0.3215 -0.0504 0.1662 -0.0206 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.3366 0.2692 0.3281 -0.0539 0.1594 -0.0156 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.3302 0.2421 0.3093 -0.0579 0.1720 -0.0248 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.3453 0.2743 0.3617 -0.0346 0.1615 -0.0172 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.3456 0.2801 0.3706 -0.0300 0.1568 -0.0147 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.3412 0.2744 0.3717 -0.0244 0.1545 -0.0148 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.3421 0.2706 0.3721 -0.0233 0.1564 -0.0157 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.3239 0.2605 0.3589 -0.0215 0.1504 -0.0135 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.3089 0.2437 0.3457 -0.0182 0.1477 -0.0138 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2983 0.2350 0.3332 -0.0175 0.1461 -0.0141 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2914 0.2318 0.3294 -0.0176 0.1459 -0.0131 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.3052 0.2395 0.3492 -0.0162 0.1454 -0.0131 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.3104 0.2478 0.3585 -0.0166 0.1449 -0.0123 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.3105 0.2429 0.3601 -0.0155 0.1473 -0.0121 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.3241 0.2611 0.3790 -0.0154 0.1417 -0.0116 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2870 0.2208 0.3175 -0.0168 0.1453 -0.0152 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2843 0.2184 0.3126 -0.0161 0.1459 -0.0165 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2838 0.2171 0.3167 -0.0146 0.1450 -0.0173 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2760 0.2065 0.3098 -0.0147 0.1421 -0.0177 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2997 0.2297 0.3199 -0.0169 0.1456 -0.0178 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.2997 0.2285 0.3172 -0.0165 0.1485 -0.0203 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3082 0.2384 0.3246 -0.0185 0.1471 -0.0165 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2885 0.2245 0.3260 -0.0135 0.1475 -0.0170 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2914 0.2251 0.3344 -0.0119 0.1476 -0.0177 125 SER   A CA  
923  C C   . SER   A 119 ? 0.2932 0.2247 0.3382 -0.0100 0.1523 -0.0198 125 SER   A C   
924  O O   . SER   A 119 ? 0.2899 0.2154 0.3363 -0.0092 0.1534 -0.0223 125 SER   A O   
925  C CB  . SER   A 119 ? 0.3017 0.2404 0.3532 -0.0118 0.1461 -0.0137 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.3133 0.2504 0.3724 -0.0101 0.1465 -0.0131 125 SER   A OG  
927  N N   . THR   A 120 ? 0.2938 0.2293 0.3399 -0.0096 0.1558 -0.0187 126 THR   A N   
928  C CA  . THR   A 120 ? 0.3057 0.2392 0.3559 -0.0073 0.1626 -0.0207 126 THR   A CA  
929  C C   . THR   A 120 ? 0.3345 0.2693 0.3780 -0.0087 0.1661 -0.0219 126 THR   A C   
930  O O   . THR   A 120 ? 0.3293 0.2675 0.3672 -0.0111 0.1627 -0.0200 126 THR   A O   
931  C CB  . THR   A 120 ? 0.3033 0.2434 0.3715 -0.0040 0.1649 -0.0155 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3231 0.2741 0.3970 -0.0052 0.1633 -0.0096 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2967 0.2366 0.3724 -0.0032 0.1611 -0.0127 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.3574 0.2882 0.4013 -0.0073 0.1738 -0.0252 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.3854 0.3173 0.4240 -0.0086 0.1789 -0.0263 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.3985 0.3268 0.4427 -0.0061 0.1899 -0.0296 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.4004 0.3230 0.4513 -0.0034 0.1940 -0.0320 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.4085 0.3388 0.4494 -0.0074 0.1955 -0.0301 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.4265 0.3535 0.4722 -0.0054 0.2083 -0.0336 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.4178 0.3576 0.4792 -0.0038 0.2126 -0.0276 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.4069 0.3591 0.4817 -0.0031 0.2057 -0.0197 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.4221 0.3591 0.4816 -0.0041 0.2240 -0.0311 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.4228 0.3727 0.4986 -0.0029 0.2293 -0.0252 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.4098 0.3691 0.4802 -0.0076 0.2192 -0.0195 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.4113 0.3845 0.4993 -0.0072 0.2177 -0.0117 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.4388 0.3999 0.5467 0.0035  0.2323 -0.0177 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.4923 0.4437 0.6104 0.0090  0.2439 -0.0224 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.5214 0.4591 0.6261 0.0081  0.2555 -0.0319 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.4855 0.4432 0.6270 0.0141  0.2412 -0.0157 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.4002 0.3519 0.4479 -0.0122 0.2121 -0.0229 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.3999 0.3574 0.4419 -0.0165 0.2038 -0.0184 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.3857 0.3510 0.4368 -0.0165 0.1935 -0.0126 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.3863 0.3573 0.4363 -0.0203 0.1884 -0.0086 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.3767 0.3413 0.4355 -0.0130 0.1909 -0.0124 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.3737 0.3444 0.4385 -0.0139 0.1818 -0.0074 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.3704 0.3313 0.4237 -0.0135 0.1770 -0.0116 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.3800 0.3336 0.4323 -0.0106 0.1804 -0.0159 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3769 0.3574 0.4644 -0.0104 0.1825 -0.0011 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.4055 0.3985 0.5118 -0.0099 0.1872 0.0054  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.4079 0.4105 0.5381 -0.0064 0.1859 0.0134  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.4149 0.4163 0.5179 -0.0164 0.1813 0.0101  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.3432 0.3037 0.3889 -0.0167 0.1698 -0.0105 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3376 0.2911 0.3760 -0.0163 0.1652 -0.0131 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.3231 0.2827 0.3701 -0.0169 0.1605 -0.0087 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.3215 0.2881 0.3710 -0.0205 0.1581 -0.0045 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3452 0.2924 0.3694 -0.0193 0.1623 -0.0151 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3450 0.2964 0.3682 -0.0231 0.1607 -0.0121 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3581 0.2992 0.3780 -0.0186 0.1579 -0.0168 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.3080 0.2645 0.3580 -0.0144 0.1590 -0.0097 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.3048 0.2655 0.3610 -0.0153 0.1547 -0.0057 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.3231 0.2779 0.3708 -0.0165 0.1515 -0.0082 133 GLY   A C   
972  O O   . GLY   A 127 ? 0.3255 0.2733 0.3686 -0.0147 0.1517 -0.0122 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.3195 0.2773 0.3653 -0.0203 0.1487 -0.0056 134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.3216 0.2744 0.3613 -0.0216 0.1476 -0.0078 134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.3090 0.2650 0.3530 -0.0232 0.1455 -0.0046 134 PHE   A C   
976  O O   . PHE   A 128 ? 0.2957 0.2583 0.3424 -0.0267 0.1438 0.0002  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.3198 0.2705 0.3509 -0.0258 0.1484 -0.0088 134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.3175 0.2661 0.3441 -0.0258 0.1501 -0.0104 134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.3151 0.2570 0.3376 -0.0236 0.1507 -0.0131 134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.3105 0.2644 0.3371 -0.0290 0.1505 -0.0081 134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.3213 0.2610 0.3386 -0.0244 0.1519 -0.0136 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.3101 0.2618 0.3322 -0.0295 0.1523 -0.0092 134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.3103 0.2545 0.3271 -0.0273 0.1532 -0.0121 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.3028 0.2547 0.3478 -0.0214 0.1452 -0.0062 135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.3108 0.2650 0.3590 -0.0233 0.1437 -0.0031 135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.3183 0.2714 0.3579 -0.0287 0.1453 -0.0038 135 ALA   A C   
987  O O   . ALA   A 129 ? 0.3105 0.2580 0.3466 -0.0280 0.1480 -0.0075 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.3162 0.2662 0.3689 -0.0199 0.1433 -0.0049 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.3339 0.2916 0.3701 -0.0346 0.1438 0.0002  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.3462 0.3008 0.3709 -0.0415 0.1464 -0.0013 136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.3456 0.2963 0.3701 -0.0415 0.1495 -0.0030 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.3442 0.2974 0.3767 -0.0388 0.1473 -0.0003 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.3787 0.3399 0.3985 -0.0498 0.1427 0.0044  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.4009 0.3572 0.4043 -0.0593 0.1459 0.0017  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.4044 0.3538 0.4011 -0.0599 0.1504 -0.0039 136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4209 0.3792 0.4175 -0.0667 0.1444 0.0052  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.3407 0.2847 0.3570 -0.0446 0.1555 -0.0075 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.3402 0.2805 0.3568 -0.0452 0.1605 -0.0093 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.3618 0.2969 0.3631 -0.0547 0.1667 -0.0119 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3758 0.3074 0.3756 -0.0565 0.1727 -0.0136 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.3190 0.2551 0.3452 -0.0381 0.1642 -0.0126 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.3057 0.2452 0.3429 -0.0311 0.1581 -0.0108 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.3097 0.2386 0.3311 -0.0384 0.1697 -0.0169 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3566 0.2904 0.3456 -0.0615 0.1661 -0.0125 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3615 0.2882 0.3323 -0.0724 0.1721 -0.0161 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.3856 0.3147 0.3464 -0.0815 0.1714 -0.0126 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4091 0.3298 0.3544 -0.0901 0.1794 -0.0171 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3524 0.2786 0.3128 -0.0788 0.1691 -0.0163 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3278 0.2499 0.2951 -0.0717 0.1711 -0.0198 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3555 0.2785 0.3132 -0.0789 0.1675 -0.0190 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3838 0.3201 0.3508 -0.0769 0.1575 -0.0114 138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.4007 0.3422 0.3650 -0.0820 0.1525 -0.0081 138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.4149 0.3488 0.3650 -0.0905 0.1556 -0.0121 138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3833 0.3372 0.3602 -0.0787 0.1450 -0.0008 138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.3795 0.3190 0.3485 -0.0802 0.1624 -0.0045 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.3815 0.3247 0.3434 -0.0882 0.1599 0.0010  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.4015 0.3419 0.3690 -0.0846 0.1660 -0.0007 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4172 0.3585 0.3759 -0.0925 0.1663 0.0028  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.3862 0.3417 0.3585 -0.0873 0.1480 0.0117  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4297 0.3892 0.4237 -0.0744 0.1453 0.0137  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4192 0.3751 0.4211 -0.0657 0.1485 0.0079  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4468 0.4122 0.4491 -0.0738 0.1401 0.0211  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3861 0.3240 0.3686 -0.0735 0.1702 -0.0049 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3745 0.3110 0.3660 -0.0695 0.1756 -0.0060 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.3856 0.3122 0.3672 -0.0740 0.1889 -0.0132 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.3907 0.3128 0.3830 -0.0670 0.1959 -0.0178 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3603 0.2989 0.3719 -0.0574 0.1733 -0.0064 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3651 0.3102 0.3858 -0.0523 0.1631 -0.0017 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3666 0.3112 0.4014 -0.0428 0.1622 -0.0038 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3642 0.3150 0.3880 -0.0546 0.1574 0.0054  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.3809 0.3038 0.3422 -0.0864 0.1927 -0.0137 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.4072 0.3183 0.3553 -0.0926 0.2074 -0.0218 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.4219 0.3308 0.3847 -0.0862 0.2182 -0.0244 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.4326 0.3316 0.3948 -0.0857 0.2319 -0.0317 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.4207 0.3283 0.3415 -0.1091 0.2089 -0.0213 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.4388 0.3507 0.3445 -0.1186 0.1972 -0.0163 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.4565 0.3621 0.3316 -0.1372 0.2008 -0.0171 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.4362 0.3447 0.3427 -0.1154 0.1960 -0.0205 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.4188 0.3367 0.3963 -0.0813 0.2123 -0.0181 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.4201 0.3385 0.4133 -0.0762 0.2205 -0.0186 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.4302 0.3488 0.4463 -0.0642 0.2233 -0.0207 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.4188 0.3371 0.4490 -0.0606 0.2324 -0.0216 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.4100 0.3377 0.4109 -0.0759 0.2122 -0.0108 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.4138 0.3492 0.4256 -0.0694 0.1973 -0.0050 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.4271 0.3667 0.4308 -0.0733 0.1865 0.0003  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4060 0.3458 0.4395 -0.0586 0.1921 -0.0038 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.4228 0.3677 0.4419 -0.0647 0.1769 0.0037  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.4156 0.3602 0.4511 -0.0564 0.1798 0.0010  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.4089 0.3491 0.4605 -0.0513 0.1966 -0.0054 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.4160 0.3637 0.4673 -0.0480 0.1730 0.0023  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.4158 0.3606 0.4831 -0.0436 0.1877 -0.0029 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.4139 0.3614 0.4792 -0.0425 0.1765 0.0002  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.4497 0.3696 0.4710 -0.0582 0.2152 -0.0205 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4708 0.3907 0.5124 -0.0480 0.2168 -0.0213 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.5101 0.4203 0.5540 -0.0477 0.2328 -0.0273 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5006 0.4119 0.5658 -0.0396 0.2363 -0.0262 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.4732 0.3943 0.5148 -0.0438 0.2069 -0.0206 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.4822 0.4120 0.5285 -0.0409 0.1930 -0.0152 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.4846 0.4144 0.5271 -0.0386 0.1858 -0.0155 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4859 0.4211 0.5523 -0.0342 0.1897 -0.0117 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.5494 0.4497 0.5717 -0.0571 0.2427 -0.0332 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.5917 0.4794 0.6121 -0.0585 0.2603 -0.0406 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.6390 0.5226 0.6589 -0.0627 0.2754 -0.0434 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.6552 0.5258 0.6687 -0.0660 0.2921 -0.0509 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.6181 0.4946 0.6112 -0.0683 0.2627 -0.0467 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.6446 0.5189 0.6423 -0.0629 0.2571 -0.0472 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.6382 0.5145 0.6596 -0.0519 0.2577 -0.0450 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.6688 0.5400 0.6468 -0.0702 0.2517 -0.0489 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.6628 0.5560 0.6880 -0.0635 0.2712 -0.0381 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.6996 0.5895 0.7233 -0.0685 0.2862 -0.0405 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.7096 0.6125 0.7568 -0.0627 0.2818 -0.0329 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.7248 0.6277 0.7711 -0.0674 0.2918 -0.0331 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.7571 0.6406 0.7461 -0.0840 0.2883 -0.0435 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.8251 0.7191 0.8044 -0.0879 0.2686 -0.0356 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 0.9135 0.8022 0.8591 -0.1027 0.2653 -0.0369 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 0.9101 0.8069 0.8477 -0.1083 0.2534 -0.0294 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 0.9618 0.8380 0.8896 -0.1091 0.2742 -0.0449 145 GLU   A OE2 
1078 N N1  . A1BOY B .   ? 0.3737 0.2694 0.4071 -0.0093 0.1731 -0.0399 201 A1BOY A N1  
1079 C C4  . A1BOY B .   ? 0.4087 0.2982 0.4040 -0.0170 0.1897 -0.0495 201 A1BOY A C4  
1080 C C5  . A1BOY B .   ? 0.4019 0.2976 0.4041 -0.0160 0.1795 -0.0444 201 A1BOY A C5  
1081 C C6  . A1BOY B .   ? 0.3986 0.2893 0.4059 -0.0153 0.1768 -0.0456 201 A1BOY A C6  
1082 C C7  . A1BOY B .   ? 0.3775 0.2769 0.4060 -0.0096 0.1760 -0.0398 201 A1BOY A C7  
1083 C C8  . A1BOY B .   ? 0.3815 0.2658 0.4021 -0.0142 0.1705 -0.0452 201 A1BOY A C8  
1084 C C10 . A1BOY B .   ? 0.3760 0.2720 0.4186 -0.0106 0.1602 -0.0353 201 A1BOY A C10 
1085 C C13 . A1BOY B .   ? 0.3671 0.2703 0.4196 -0.0048 0.1718 -0.0336 201 A1BOY A C13 
1086 O O2  . A1BOY B .   ? 0.3486 0.2604 0.4295 -0.0008 0.1645 -0.0218 201 A1BOY A O2  
1087 C C12 . A1BOY B .   ? 0.3545 0.2690 0.4236 -0.0037 0.1606 -0.0231 201 A1BOY A C12 
1088 N N2  . A1BOY B .   ? 0.3457 0.2694 0.4155 -0.0049 0.1550 -0.0182 201 A1BOY A N2  
1089 C C11 . A1BOY B .   ? 0.3625 0.2693 0.4153 -0.0066 0.1627 -0.0301 201 A1BOY A C11 
1090 C C9  . A1BOY B .   ? 0.3833 0.2723 0.4072 -0.0155 0.1605 -0.0409 201 A1BOY A C9  
1091 O O1  . A1BOY B .   ? 0.3623 0.2718 0.4024 -0.0064 0.1776 -0.0349 201 A1BOY A O1  
1092 C C1  . A1BOY B .   ? 0.4015 0.3067 0.4045 -0.0162 0.1729 -0.0388 201 A1BOY A C1  
1093 O O   . A1BOY B .   ? 0.3909 0.2999 0.3985 -0.0159 0.1647 -0.0351 201 A1BOY A O   
1094 C C   . A1BOY B .   ? 0.4017 0.3183 0.4108 -0.0161 0.1597 -0.0302 201 A1BOY A C   
1095 C C3  . A1BOY B .   ? 0.4062 0.3002 0.3966 -0.0182 0.1923 -0.0481 201 A1BOY A C3  
1096 C C2  . A1BOY B .   ? 0.4050 0.3087 0.3976 -0.0184 0.1843 -0.0418 201 A1BOY A C2  
1097 N N   . A1BOY B .   ? 0.4039 0.3125 0.4024 -0.0174 0.1752 -0.0376 201 A1BOY A N   
# 
