data_7HVS
# 
_entry.id   7HVS 
# 
_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   7HVS         pdb_00007hvs 10.2210/pdb7hvs/pdb 
WWPDB D_1001407992 ?            ?                   
# 
_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                        7HVS 
_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-methoxyphenyl)acetyl]pyrrolidine-3-carboxamide' 262.304   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                  65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                        78.133    3   ?         ? ? ? 
5 water       nat water                                                       18.015    210 ?         ? ? ? 
# 
_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-methoxyphenyl)acetyl]pyrrolidine-3-carboxamide' A1BOM 
3 'ZINC ION'                                                  ZN    
4 'DIMETHYL SULFOXIDE'                                        DMS   
5 water                                                       HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1BOM non-polymer         . '(3S)-1-[(2-methoxyphenyl)acetyl]pyrrolidine-3-carboxamide' ? 'C14 H18 N2 O3'  262.304 
ALA   'L-peptide linking' y ALANINE                                                     ? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                    ? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                  ? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                             ? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                    ? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                        ? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                   ? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                             ? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                     ? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                   ? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                       ? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                  ? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                     ? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                      ? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                  ? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                               ? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                     ? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                      ? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                   ? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                  ? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                    ? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                      ? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                  ? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BOM 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOM 
_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 A1BOM 1   201 201 A1BOM LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 0   DMS   DMS A . 
E 4 DMS   1   204 3   DMS   DMS A . 
F 4 DMS   1   205 4   DMS   DMS A . 
G 5 HOH   1   301 25  HOH   HOH A . 
G 5 HOH   2   302 137 HOH   HOH A . 
G 5 HOH   3   303 57  HOH   HOH A . 
G 5 HOH   4   304 75  HOH   HOH A . 
G 5 HOH   5   305 269 HOH   HOH A . 
G 5 HOH   6   306 104 HOH   HOH A . 
G 5 HOH   7   307 152 HOH   HOH A . 
G 5 HOH   8   308 169 HOH   HOH A . 
G 5 HOH   9   309 46  HOH   HOH A . 
G 5 HOH   10  310 271 HOH   HOH A . 
G 5 HOH   11  311 7   HOH   HOH A . 
G 5 HOH   12  312 119 HOH   HOH A . 
G 5 HOH   13  313 212 HOH   HOH A . 
G 5 HOH   14  314 111 HOH   HOH A . 
G 5 HOH   15  315 121 HOH   HOH A . 
G 5 HOH   16  316 107 HOH   HOH A . 
G 5 HOH   17  317 24  HOH   HOH A . 
G 5 HOH   18  318 55  HOH   HOH A . 
G 5 HOH   19  319 30  HOH   HOH A . 
G 5 HOH   20  320 4   HOH   HOH A . 
G 5 HOH   21  321 270 HOH   HOH A . 
G 5 HOH   22  322 26  HOH   HOH A . 
G 5 HOH   23  323 113 HOH   HOH A . 
G 5 HOH   24  324 183 HOH   HOH A . 
G 5 HOH   25  325 35  HOH   HOH A . 
G 5 HOH   26  326 61  HOH   HOH A . 
G 5 HOH   27  327 205 HOH   HOH A . 
G 5 HOH   28  328 42  HOH   HOH A . 
G 5 HOH   29  329 68  HOH   HOH A . 
G 5 HOH   30  330 36  HOH   HOH A . 
G 5 HOH   31  331 15  HOH   HOH A . 
G 5 HOH   32  332 59  HOH   HOH A . 
G 5 HOH   33  333 262 HOH   HOH A . 
G 5 HOH   34  334 253 HOH   HOH A . 
G 5 HOH   35  335 251 HOH   HOH A . 
G 5 HOH   36  336 79  HOH   HOH A . 
G 5 HOH   37  337 37  HOH   HOH A . 
G 5 HOH   38  338 214 HOH   HOH A . 
G 5 HOH   39  339 77  HOH   HOH A . 
G 5 HOH   40  340 157 HOH   HOH A . 
G 5 HOH   41  341 108 HOH   HOH A . 
G 5 HOH   42  342 34  HOH   HOH A . 
G 5 HOH   43  343 85  HOH   HOH A . 
G 5 HOH   44  344 279 HOH   HOH A . 
G 5 HOH   45  345 146 HOH   HOH A . 
G 5 HOH   46  346 215 HOH   HOH A . 
G 5 HOH   47  347 147 HOH   HOH A . 
G 5 HOH   48  348 33  HOH   HOH A . 
G 5 HOH   49  349 274 HOH   HOH A . 
G 5 HOH   50  350 174 HOH   HOH A . 
G 5 HOH   51  351 29  HOH   HOH A . 
G 5 HOH   52  352 254 HOH   HOH A . 
G 5 HOH   53  353 216 HOH   HOH A . 
G 5 HOH   54  354 150 HOH   HOH A . 
G 5 HOH   55  355 255 HOH   HOH A . 
G 5 HOH   56  356 280 HOH   HOH A . 
G 5 HOH   57  357 135 HOH   HOH A . 
G 5 HOH   58  358 19  HOH   HOH A . 
G 5 HOH   59  359 2   HOH   HOH A . 
G 5 HOH   60  360 9   HOH   HOH A . 
G 5 HOH   61  361 28  HOH   HOH A . 
G 5 HOH   62  362 282 HOH   HOH A . 
G 5 HOH   63  363 124 HOH   HOH A . 
G 5 HOH   64  364 50  HOH   HOH A . 
G 5 HOH   65  365 21  HOH   HOH A . 
G 5 HOH   66  366 249 HOH   HOH A . 
G 5 HOH   67  367 16  HOH   HOH A . 
G 5 HOH   68  368 256 HOH   HOH A . 
G 5 HOH   69  369 211 HOH   HOH A . 
G 5 HOH   70  370 275 HOH   HOH A . 
G 5 HOH   71  371 231 HOH   HOH A . 
G 5 HOH   72  372 267 HOH   HOH A . 
G 5 HOH   73  373 218 HOH   HOH A . 
G 5 HOH   74  374 167 HOH   HOH A . 
G 5 HOH   75  375 144 HOH   HOH A . 
G 5 HOH   76  376 178 HOH   HOH A . 
G 5 HOH   77  377 181 HOH   HOH A . 
G 5 HOH   78  378 82  HOH   HOH A . 
G 5 HOH   79  379 185 HOH   HOH A . 
G 5 HOH   80  380 43  HOH   HOH A . 
G 5 HOH   81  381 177 HOH   HOH A . 
G 5 HOH   82  382 14  HOH   HOH A . 
G 5 HOH   83  383 220 HOH   HOH A . 
G 5 HOH   84  384 259 HOH   HOH A . 
G 5 HOH   85  385 126 HOH   HOH A . 
G 5 HOH   86  386 12  HOH   HOH A . 
G 5 HOH   87  387 105 HOH   HOH A . 
G 5 HOH   88  388 11  HOH   HOH A . 
G 5 HOH   89  389 49  HOH   HOH A . 
G 5 HOH   90  390 8   HOH   HOH A . 
G 5 HOH   91  391 84  HOH   HOH A . 
G 5 HOH   92  392 170 HOH   HOH A . 
G 5 HOH   93  393 52  HOH   HOH A . 
G 5 HOH   94  394 161 HOH   HOH A . 
G 5 HOH   95  395 156 HOH   HOH A . 
G 5 HOH   96  396 106 HOH   HOH A . 
G 5 HOH   97  397 20  HOH   HOH A . 
G 5 HOH   98  398 5   HOH   HOH A . 
G 5 HOH   99  399 132 HOH   HOH A . 
G 5 HOH   100 400 47  HOH   HOH A . 
G 5 HOH   101 401 260 HOH   HOH A . 
G 5 HOH   102 402 62  HOH   HOH A . 
G 5 HOH   103 403 261 HOH   HOH A . 
G 5 HOH   104 404 39  HOH   HOH A . 
G 5 HOH   105 405 18  HOH   HOH A . 
G 5 HOH   106 406 168 HOH   HOH A . 
G 5 HOH   107 407 103 HOH   HOH A . 
G 5 HOH   108 408 186 HOH   HOH A . 
G 5 HOH   109 409 41  HOH   HOH A . 
G 5 HOH   110 410 252 HOH   HOH A . 
G 5 HOH   111 411 176 HOH   HOH A . 
G 5 HOH   112 412 100 HOH   HOH A . 
G 5 HOH   113 413 95  HOH   HOH A . 
G 5 HOH   114 414 120 HOH   HOH A . 
G 5 HOH   115 415 96  HOH   HOH A . 
G 5 HOH   116 416 83  HOH   HOH A . 
G 5 HOH   117 417 191 HOH   HOH A . 
G 5 HOH   118 418 40  HOH   HOH A . 
G 5 HOH   119 419 257 HOH   HOH A . 
G 5 HOH   120 420 65  HOH   HOH A . 
G 5 HOH   121 421 123 HOH   HOH A . 
G 5 HOH   122 422 131 HOH   HOH A . 
G 5 HOH   123 423 258 HOH   HOH A . 
G 5 HOH   124 424 128 HOH   HOH A . 
G 5 HOH   125 425 159 HOH   HOH A . 
G 5 HOH   126 426 80  HOH   HOH A . 
G 5 HOH   127 427 278 HOH   HOH A . 
G 5 HOH   128 428 182 HOH   HOH A . 
G 5 HOH   129 429 10  HOH   HOH A . 
G 5 HOH   130 430 38  HOH   HOH A . 
G 5 HOH   131 431 23  HOH   HOH A . 
G 5 HOH   132 432 175 HOH   HOH A . 
G 5 HOH   133 433 89  HOH   HOH A . 
G 5 HOH   134 434 58  HOH   HOH A . 
G 5 HOH   135 435 203 HOH   HOH A . 
G 5 HOH   136 436 219 HOH   HOH A . 
G 5 HOH   137 437 76  HOH   HOH A . 
G 5 HOH   138 438 237 HOH   HOH A . 
G 5 HOH   139 439 101 HOH   HOH A . 
G 5 HOH   140 440 53  HOH   HOH A . 
G 5 HOH   141 441 200 HOH   HOH A . 
G 5 HOH   142 442 69  HOH   HOH A . 
G 5 HOH   143 443 17  HOH   HOH A . 
G 5 HOH   144 444 70  HOH   HOH A . 
G 5 HOH   145 445 248 HOH   HOH A . 
G 5 HOH   146 446 155 HOH   HOH A . 
G 5 HOH   147 447 192 HOH   HOH A . 
G 5 HOH   148 448 233 HOH   HOH A . 
G 5 HOH   149 449 110 HOH   HOH A . 
G 5 HOH   150 450 273 HOH   HOH A . 
G 5 HOH   151 451 154 HOH   HOH A . 
G 5 HOH   152 452 158 HOH   HOH A . 
G 5 HOH   153 453 201 HOH   HOH A . 
G 5 HOH   154 454 247 HOH   HOH A . 
G 5 HOH   155 455 138 HOH   HOH A . 
G 5 HOH   156 456 102 HOH   HOH A . 
G 5 HOH   157 457 160 HOH   HOH A . 
G 5 HOH   158 458 91  HOH   HOH A . 
G 5 HOH   159 459 239 HOH   HOH A . 
G 5 HOH   160 460 276 HOH   HOH A . 
G 5 HOH   161 461 213 HOH   HOH A . 
G 5 HOH   162 462 129 HOH   HOH A . 
G 5 HOH   163 463 272 HOH   HOH A . 
G 5 HOH   164 464 99  HOH   HOH A . 
G 5 HOH   165 465 229 HOH   HOH A . 
G 5 HOH   166 466 240 HOH   HOH A . 
G 5 HOH   167 467 246 HOH   HOH A . 
G 5 HOH   168 468 221 HOH   HOH A . 
G 5 HOH   169 469 134 HOH   HOH A . 
G 5 HOH   170 470 117 HOH   HOH A . 
G 5 HOH   171 471 184 HOH   HOH A . 
G 5 HOH   172 472 207 HOH   HOH A . 
G 5 HOH   173 473 112 HOH   HOH A . 
G 5 HOH   174 474 277 HOH   HOH A . 
G 5 HOH   175 475 171 HOH   HOH A . 
G 5 HOH   176 476 232 HOH   HOH A . 
G 5 HOH   177 477 284 HOH   HOH A . 
G 5 HOH   178 478 127 HOH   HOH A . 
G 5 HOH   179 479 73  HOH   HOH A . 
G 5 HOH   180 480 86  HOH   HOH A . 
G 5 HOH   181 481 241 HOH   HOH A . 
G 5 HOH   182 482 190 HOH   HOH A . 
G 5 HOH   183 483 56  HOH   HOH A . 
G 5 HOH   184 484 285 HOH   HOH A . 
G 5 HOH   185 485 238 HOH   HOH A . 
G 5 HOH   186 486 268 HOH   HOH A . 
G 5 HOH   187 487 209 HOH   HOH A . 
G 5 HOH   188 488 286 HOH   HOH A . 
G 5 HOH   189 489 266 HOH   HOH A . 
G 5 HOH   190 490 242 HOH   HOH A . 
G 5 HOH   191 491 264 HOH   HOH A . 
G 5 HOH   192 492 265 HOH   HOH A . 
G 5 HOH   193 493 122 HOH   HOH A . 
G 5 HOH   194 494 173 HOH   HOH A . 
G 5 HOH   195 495 125 HOH   HOH A . 
G 5 HOH   196 496 208 HOH   HOH A . 
G 5 HOH   197 497 165 HOH   HOH A . 
G 5 HOH   198 498 118 HOH   HOH A . 
G 5 HOH   199 499 217 HOH   HOH A . 
G 5 HOH   200 500 153 HOH   HOH A . 
G 5 HOH   201 501 92  HOH   HOH A . 
G 5 HOH   202 502 202 HOH   HOH A . 
G 5 HOH   203 503 263 HOH   HOH A . 
G 5 HOH   204 504 281 HOH   HOH A . 
G 5 HOH   205 505 225 HOH   HOH A . 
G 5 HOH   206 506 98  HOH   HOH A . 
G 5 HOH   207 507 206 HOH   HOH A . 
G 5 HOH   208 508 243 HOH   HOH A . 
G 5 HOH   209 509 283 HOH   HOH A . 
G 5 HOH   210 510 244 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           7HVS 
_cell.length_a           88.624 
_cell.length_b           58.007 
_cell.length_c           32.741 
_cell.angle_alpha        90.00 
_cell.angle_beta         91.85 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVS 
_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          7HVS 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.65 
_exptl_crystal.density_percent_sol   53.52 
_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   2024-11-14 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HVS 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.52 
_reflns.d_resolution_high            1.42 
_reflns.number_obs                   31299 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_netI_over_sigmaI        15.3 
_reflns.pdbx_redundancy              6.3 
_reflns.pdbx_Rrim_I_all              0.057 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     196072 
_reflns.pdbx_chi_squared             0.50 
_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                  1.42 
_reflns_shell.d_res_low                   1.44 
_reflns_shell.number_measured_all         6752 
_reflns_shell.number_unique_obs           1498 
_reflns_shell.Rmerge_I_obs                2.262 
_reflns_shell.pdbx_chi_squared            0.07 
_reflns_shell.pdbx_redundancy             4.5 
_reflns_shell.percent_possible_obs        97.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             2.561 
_reflns_shell.pdbx_Rpim_I_all             1.181 
_reflns_shell.pdbx_CC_half                0.340 
_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                                 7HVS 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     28744 
_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                             17.60 
_refine.ls_d_res_high                            1.420 
_refine.ls_percent_reflns_obs                    91.8 
_refine.ls_R_factor_obs                          0.2071 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2057 
_refine.ls_R_factor_R_free                       0.2332 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.030 
_refine.ls_number_reflns_R_free                  1447 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_refine.B_iso_mean                               33.55 
_refine.aniso_B[1][1]                            0.19160 
_refine.aniso_B[2][2]                            1.51880 
_refine.aniso_B[3][3]                            -1.71040 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.54180 
_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             0.072 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.073 
_refine.pdbx_overall_SU_R_Blow_DPI               0.078 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.078 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVS 
_refine_analyze.Luzzati_coordinate_error_obs    0.23 
_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        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.number_atoms_solvent             210 
_refine_hist.number_atoms_total               1325 
_refine_hist.d_res_high                       1.420 
_refine_hist.d_res_low                        17.60 
# 
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                  0.011 ? 2.00  1158 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.00  ? 2.00  1576 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  387  '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  210  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1158 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.99  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.23 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  141  '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  1092 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.42 
_refine_ls_shell.d_res_low                        1.46 
_refine_ls_shell.number_reflns_R_work             559 
_refine_ls_shell.R_factor_R_work                  0.3890 
_refine_ls_shell.percent_reflns_obs               23.27 
_refine_ls_shell.R_factor_R_free                  0.3862 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            2.78 
_refine_ls_shell.number_reflns_R_free             16 
_refine_ls_shell.number_reflns_all                575 
_refine_ls_shell.R_factor_all                     0.3889 
# 
_struct.entry_id                  7HVS 
_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-0032461-001 (A71EV2A-x3581)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVS 
_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 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7HVS 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6 AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.400 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.358 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
# 
_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_555 110.1 ? 
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_555 106.8 ? 
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_555 117.4 ? 
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_555 106.5 ? 
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_555 101.6 ? 
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_555 114.0 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HVS 
_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 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     502 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     502 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              2.11 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -98.75  38.17  
2 1 SER A 125 ? ? -137.19 -30.26 
# 
_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         15.4292 
_pdbx_refine_tls.origin_y         7.5638 
_pdbx_refine_tls.origin_z         13.5465 
_pdbx_refine_tls.T[1][1]          -0.0450 
_pdbx_refine_tls.T[2][2]          -0.0211 
_pdbx_refine_tls.T[3][3]          -0.0053 
_pdbx_refine_tls.T[1][2]          -0.0125 
_pdbx_refine_tls.T[1][3]          -0.0270 
_pdbx_refine_tls.T[2][3]          0.0115 
_pdbx_refine_tls.L[1][1]          1.2233 
_pdbx_refine_tls.L[2][2]          3.7462 
_pdbx_refine_tls.L[3][3]          0.3911 
_pdbx_refine_tls.L[1][2]          0.8970 
_pdbx_refine_tls.L[1][3]          -0.6854 
_pdbx_refine_tls.L[2][3]          -1.0146 
_pdbx_refine_tls.S[1][1]          -0.0501 
_pdbx_refine_tls.S[1][2]          0.0315 
_pdbx_refine_tls.S[1][3]          0.0779 
_pdbx_refine_tls.S[2][1]          0.0204 
_pdbx_refine_tls.S[2][2]          -0.0037 
_pdbx_refine_tls.S[2][3]          -0.2040 
_pdbx_refine_tls.S[3][1]          0.0017 
_pdbx_refine_tls.S[3][2]          -0.0539 
_pdbx_refine_tls.S[3][3]          0.0538 
# 
_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|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 508 ? 5.82 . 
2 1 O ? A HOH 509 ? 5.99 . 
3 1 O ? A HOH 510 ? 9.95 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BOM N1   N  N N 1   
A1BOM C4   C  Y N 2   
A1BOM C5   C  Y N 3   
A1BOM C6   C  Y N 4   
A1BOM C7   C  N N 5   
A1BOM C8   C  N N 6   
A1BOM C10  C  N N 7   
A1BOM C13  C  N N 8   
A1BOM O2   O  N N 9   
A1BOM C12  C  N N 10  
A1BOM C11  C  N S 11  
A1BOM C9   C  N N 12  
A1BOM N    N  N N 13  
A1BOM O1   O  N N 14  
A1BOM C1   C  Y N 15  
A1BOM O    O  N N 16  
A1BOM C    C  N N 17  
A1BOM C3   C  Y N 18  
A1BOM C2   C  Y N 19  
A1BOM H15  H  N N 20  
A1BOM H14  H  N N 21  
A1BOM H6   H  N N 22  
A1BOM H7   H  N N 23  
A1BOM H9   H  N N 24  
A1BOM H8   H  N N 25  
A1BOM H12  H  N N 26  
A1BOM H13  H  N N 27  
A1BOM H16  H  N N 28  
A1BOM H17  H  N N 29  
A1BOM H    H  N N 30  
A1BOM H10  H  N N 31  
A1BOM H11  H  N N 32  
A1BOM H2   H  N N 33  
A1BOM H1   H  N N 34  
A1BOM H3   H  N N 35  
A1BOM H5   H  N N 36  
A1BOM H4   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
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 
A1BOM C   O    sing N N 1   
A1BOM O   C1   sing N N 2   
A1BOM C1  C2   doub Y N 3   
A1BOM C2  C3   sing Y N 4   
A1BOM C3  C4   doub Y N 5   
A1BOM C4  C5   sing Y N 6   
A1BOM C5  C6   doub Y N 7   
A1BOM C1  C6   sing Y N 8   
A1BOM C6  C7   sing N N 9   
A1BOM C7  C8   sing N N 10  
A1BOM O1  C8   doub N N 11  
A1BOM C8  N    sing N N 12  
A1BOM N   C9   sing N N 13  
A1BOM C9  C10  sing N N 14  
A1BOM C10 C11  sing N N 15  
A1BOM C11 C12  sing N N 16  
A1BOM N1  C12  sing N N 17  
A1BOM C12 O2   doub N N 18  
A1BOM C13 C11  sing N N 19  
A1BOM N   C13  sing N N 20  
A1BOM N1  H15  sing N N 21  
A1BOM N1  H14  sing N N 22  
A1BOM C4  H6   sing N N 23  
A1BOM C5  H7   sing N N 24  
A1BOM C7  H9   sing N N 25  
A1BOM C7  H8   sing N N 26  
A1BOM C10 H12  sing N N 27  
A1BOM C10 H13  sing N N 28  
A1BOM C13 H16  sing N N 29  
A1BOM C13 H17  sing N N 30  
A1BOM C11 H    sing N N 31  
A1BOM C9  H10  sing N N 32  
A1BOM C9  H11  sing N N 33  
A1BOM C   H2   sing N N 34  
A1BOM C   H1   sing N N 35  
A1BOM C   H3   sing N N 36  
A1BOM C3  H5   sing N N 37  
A1BOM C2  H4   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_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                    7HVS 
_atom_sites.fract_transf_matrix[1][1]   0.011284 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000364 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017239 
_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]   0.030559 
_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   ? 19.376 7.060   23.732 1.00 31.29  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.510 7.193   22.812 1.00 32.24  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.625 6.008   21.814 1.00 31.59  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.971 4.978   21.992 1.00 31.66  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.808 7.375   23.609 1.00 34.83  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.197 6.122   24.140 1.00 36.85  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.416 6.194   20.755 1.00 30.67  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.650 5.170   19.744 1.00 29.21  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.958 5.724   18.361 1.00 28.01  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.589 6.853   18.039 1.00 27.65  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.541 4.891   17.501 1.00 26.80  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.875 5.298   16.147 1.00 27.68  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.870 4.112   15.199 1.00 27.77  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.984 2.954   15.653 1.00 29.08  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.270 5.946   16.158 1.00 27.81  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.805 4.388   13.876 1.00 25.97  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.922 3.419   12.793 1.00 25.85  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.317 3.627   12.178 1.00 27.69  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.738 4.779   11.954 1.00 27.70  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.832 3.672   11.705 1.00 26.34  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.425 3.747   12.317 1.00 25.33  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.904 2.627   10.570 1.00 27.65  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.347 4.384   11.301 1.00 24.56  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.059 2.515   11.956 1.00 29.23  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.385 2.587   11.351 1.00 31.06  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.365 1.828   10.069 1.00 32.88  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.334 0.597   10.094 1.00 35.16  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.494 2.043   12.272 1.00 31.04  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.650 2.841   13.535 1.00 32.12  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.480 3.955   13.579 1.00 32.96  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.903 2.542   14.664 1.00 33.95  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.562 4.746   14.715 1.00 33.89  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.011 3.295   15.818 1.00 35.03  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.864 4.382   15.850 1.00 35.23  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.886 5.169   16.966 1.00 37.35  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.290 2.536   8.950  1.00 32.43  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.225 1.943   7.634  1.00 33.99  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.354 2.499   6.795  1.00 35.90  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.503 3.722   6.696  1.00 34.36  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.842 2.210   6.988  1.00 34.94  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.478 3.702   7.014  1.00 35.18  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.758 1.632   5.590  1.00 34.85  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.214 1.629   6.255  1.00 37.42  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.347 2.096   5.447  1.00 38.06  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.219 3.063   6.227  1.00 38.48  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.456 2.827   7.416  1.00 38.76  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.594 4.210   5.627  1.00 38.81  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.341 5.217   6.362  1.00 38.65  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.412 6.331   6.864  1.00 36.70  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.828 7.476   6.941  1.00 36.24  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.506 5.769   5.530  1.00 41.06  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.589 4.737   5.440  1.00 47.56  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.364 4.543   6.381  1.00 49.26  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.590 3.971   4.361  1.00 50.10  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.179 5.971   7.307  1.00 35.19  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.221 6.958   7.825  1.00 33.85  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.733 6.568   9.228  1.00 32.36  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.608 5.372   9.550  1.00 31.88  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.983 7.078   6.892  1.00 33.19  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.269 7.604   5.505  1.00 34.19  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.850 8.854   5.317  1.00 35.54  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.980 6.846   4.377  1.00 36.07  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.132 9.337   4.044  1.00 36.61  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.255 7.321   3.095  1.00 37.60  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.828 8.573   2.934  1.00 38.24  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.100 9.065   1.675  1.00 39.68  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.416 7.572   10.031 1.00 31.51  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.806 7.414   11.355 1.00 29.99  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.498 8.222   11.324 1.00 29.17  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.533 9.423   11.048 1.00 29.63  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.739 7.923   12.468 1.00 31.68  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.088 8.098   13.847 1.00 31.43  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.157 8.431   14.902 1.00 34.33  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.742 9.460   15.862 1.00 34.56  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.235 9.224   17.071 1.00 35.91  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.988 7.979   17.466 1.00 36.11  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.866 10.231  17.847 1.00 34.83  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.358 7.562   11.591 1.00 26.78  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.057 8.247   11.566 1.00 26.43  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.576 8.391   13.001 1.00 26.48  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.443 7.372   13.708 1.00 27.50  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.017 7.478   10.706 1.00 26.49  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.711 8.282   10.569 1.00 24.70  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.605 7.135   9.331  1.00 27.90  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.322 9.627   13.454 1.00 24.84  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.860 9.814   14.835 1.00 25.17  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.651 10.770  14.864 1.00 24.00  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.405 11.469  13.873 1.00 24.67  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.978 10.379  15.773 1.00 27.25  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.130 9.388   15.937 1.00 29.69  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.471 11.738  15.279 1.00 28.27  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.926 10.877  16.033 1.00 22.07  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.931 11.939  16.181 1.00 21.68  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.698 13.281  16.121 1.00 23.31  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.723 13.463  16.831 1.00 23.65  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.256 11.865  17.552 1.00 21.53  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.395 10.615  17.697 1.00 23.49  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.873 9.559   18.154 1.00 24.57  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.138 10.685  17.221 1.00 21.94  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.191 14.239  15.332 1.00 23.34  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.885 15.550  15.234 1.00 23.78  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.077 16.179  16.627 1.00 25.89  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.163 16.698  16.928 1.00 26.50  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.103 16.493  14.320 1.00 24.42  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.869 17.786  13.958 1.00 24.77  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.925 18.648  13.148 1.00 26.03  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.514 19.900  12.654 1.00 27.65  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.515 21.052  13.323 1.00 28.79  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.098 21.097  14.590 1.00 27.96  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.954 22.173  12.737 1.00 28.09  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.024 16.071  17.496 1.00 25.06  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.067 16.656  18.836 1.00 26.23  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.113 15.996  19.763 1.00 27.18  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.487 16.601  20.766 1.00 28.16  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.665 16.741  19.485 1.00 26.95  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.079 15.463  19.983 1.00 27.71  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.361 14.616  19.146 1.00 28.26  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 17.019 14.982  21.246 1.00 27.78  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.932 13.626  19.916 1.00 28.15  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.312 13.783  21.181 1.00 28.16  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.590 14.782  19.435 1.00 26.91  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.621 14.119  20.243 1.00 28.91  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.022 14.137  19.595 1.00 30.65  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.928 13.455  20.092 1.00 30.90  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.173 12.667  20.523 1.00 28.57  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.857 12.545  21.296 1.00 28.98  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.526 11.059  21.589 1.00 28.79  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.903 13.338  22.603 1.00 29.78  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.185 14.811  18.435 1.00 31.47  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.490 14.815  17.752 1.00 33.24  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.582 15.456  18.604 1.00 34.71  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.279 16.394  19.350 1.00 34.69  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.384 15.523  16.406 1.00 33.17  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.837 14.940  18.502 1.00 36.13  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 28.018 15.455  19.239 1.00 37.36  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.848 16.454  18.380 1.00 38.20  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.587 16.616  17.176 1.00 37.43  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.916 14.293  19.729 1.00 39.37  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.528 13.692  18.589 1.00 41.53  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 28.166 13.254  20.567 1.00 40.13  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.874 17.095  18.991 1.00 39.64  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.736 18.029  18.295 1.00 41.62  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.425 17.382  17.098 1.00 40.98  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.501 18.010  16.030 1.00 41.04  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.736 18.646  19.289 1.00 46.32  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.154 19.828  20.002 1.00 52.67  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.912 20.960  20.269 1.00 55.50  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.877 20.050  20.400 1.00 54.74  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 31.078 21.809  20.845 1.00 56.38  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.844 21.303  20.937 1.00 56.67  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.830 16.109  17.254 1.00 40.71  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.475 15.340  16.205 1.00 41.41  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.520 15.139  15.026 1.00 39.88  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.914 15.346  13.880 1.00 40.27  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.990 14.007  16.733 1.00 44.94  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.070 13.458  15.844 1.00 54.01  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.154 14.067  15.702 1.00 57.34  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.791 12.318  15.206 1.00 55.95  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.245 14.789  15.303 1.00 37.27  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.252 14.671  14.253 1.00 36.10  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.085 16.009  13.468 1.00 34.47  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.988 15.972  12.234 1.00 34.59  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.873 14.300  14.848 1.00 34.76  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.787 12.922  15.467 1.00 36.59  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.336 11.972  14.874 1.00 37.26  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.174 12.800  16.550 1.00 36.58  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.949 17.157  14.158 1.00 34.11  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.782 18.439  13.453 1.00 34.27  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.036 18.790  12.630 1.00 35.11  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.917 19.288  11.506 1.00 35.17  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.444 19.589  14.408 1.00 34.03  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.010 19.567  14.844 1.00 35.21  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.525 19.157  16.052 1.00 36.74  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.876 19.893  14.039 1.00 34.85  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.146 19.206  16.049 1.00 37.18  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.722 19.691  14.834 1.00 36.48  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.717 20.346  12.722 1.00 34.65  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.433 19.943  14.357 1.00 35.81  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.442 20.632  12.264 1.00 35.32  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.313 20.370  13.057 1.00 35.67  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.217 18.500  13.186 1.00 36.04  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.501 18.724  12.508 1.00 37.32  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.631 17.829  11.256 1.00 37.17  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.295 18.208  10.279 1.00 37.54  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.664 18.403  13.465 1.00 38.19  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.090 16.609  11.325 1.00 36.00  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.178 15.676  10.201 1.00 36.42  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.809 15.513  9.532  1.00 34.64  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.471 14.421  9.070  1.00 35.81  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.731 14.329  10.690 1.00 38.89  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.156 14.498  11.166 1.00 45.02  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.067 14.727  10.369 1.00 46.31  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.361 14.470  12.474 1.00 47.53  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.020 16.600  9.497  1.00 32.03  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.682 16.572  8.958  1.00 30.98  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.661 16.191  7.492  1.00 31.58  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.443 16.727  6.702  1.00 32.30  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.004 17.962  9.158  1.00 29.92  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.606 18.104  8.598  1.00 29.48  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.655 17.229  9.359  1.00 30.38  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.118 19.592  8.693  1.00 28.69  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.752 15.265  7.132  1.00 29.44  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.469 14.920  5.749  1.00 30.43  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.111 15.575  5.327  1.00 30.86  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.009 16.255  4.295  1.00 32.78  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.419 13.383  5.548  1.00 31.56  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.953 13.041  4.132  1.00 32.52  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.779 12.758  5.848  1.00 31.61  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.079 15.397  6.166  1.00 28.97  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.751 15.910  5.884  1.00 28.83  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.927 15.957  7.172  1.00 26.71  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.069 15.080  8.024  1.00 26.41  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.054 15.009  4.847  1.00 29.69  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.592 15.264  4.666  1.00 30.23  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.008 16.202  3.862  1.00 31.51  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.518 14.580  5.338  1.00 29.04  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.631 16.130  3.981  1.00 31.30  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.309 15.119  4.854  1.00 29.71  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.467 13.551  6.287  1.00 28.95  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.060 14.681  5.316  1.00 29.17  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.224 13.106  6.725  1.00 28.74  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.047 13.665  6.231  1.00 28.24  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.073 16.976  7.309  1.00 24.76  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.173 17.050  8.473  1.00 25.03  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.876 17.763  8.089  1.00 26.07  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.862 18.629  7.186  1.00 26.11  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.836 17.745  9.681  1.00 26.21  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.435 19.118  9.344  1.00 29.18  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.529 20.335  9.439  1.00 31.36  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.960 21.396  8.925  1.00 32.22  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.419 20.250  10.030 1.00 29.42  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.790 17.434  8.801  1.00 25.54  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.518 18.078  8.519  1.00 25.86  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.771 18.207  9.853  1.00 25.54  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.339 17.181  10.412 1.00 25.46  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.758 17.264  7.458  1.00 27.85  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.432 17.802  7.003  1.00 34.19  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.819 18.568  7.755  1.00 36.99  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.000 17.444  5.881  1.00 36.43  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.629 19.451  10.362 1.00 24.73  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.941 19.724  11.622 0.50 25.07  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.962 19.628  11.655 0.50 25.74  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.488 19.214  11.561 1.00 25.18  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.961 18.685  12.545 1.00 25.62  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.928 21.228  11.891 0.50 25.51  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.125 21.047  12.209 0.50 28.18  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.433 21.472  13.192 0.50 24.09  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.071 21.913  11.829 0.50 29.86  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.838 19.414  10.392 1.00 23.73  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.442 18.996  10.252 1.00 25.28  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.260 17.469  10.337 1.00 24.92  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.138 17.023  10.543 1.00 25.89  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.781 19.568  9.002  1.00 29.83  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.220 18.901  7.836  1.00 35.82  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.340 16.699  10.145 1.00 23.03  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.279 15.227  10.256 1.00 22.65  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.905 14.722  11.586 1.00 21.74  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.900 13.495  11.824 1.00 22.36  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.055 14.557  9.067  1.00 22.66  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.314 14.738  7.759  1.00 23.52  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.098 14.146  6.600  1.00 25.05  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.132 12.682  6.705  1.00 24.40  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.190 11.858  5.659  1.00 25.40  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.270 12.347  4.419  1.00 25.96  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.182 10.542  5.842  1.00 24.06  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.558 15.622  12.379 1.00 21.61  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.312 15.265  13.591 1.00 21.78  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.422 14.242  13.210 1.00 21.74  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.768 13.379  14.019 1.00 22.35  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.437 14.728  14.781 1.00 23.31  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.252 14.393  16.058 1.00 24.17  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.130 15.196  16.436 1.00 24.98  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 15.021 13.306  16.662 1.00 24.47  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.066 14.411  11.990 1.00 22.46  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.165 13.490  11.600 1.00 23.47  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.486 14.215  11.346 1.00 24.53  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.485 15.314  10.807 1.00 24.79  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.833 12.701  10.332 1.00 24.27  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.830 11.521  10.459 1.00 25.76  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.624 10.850  9.113  1.00 26.64  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.250 10.514  11.531 1.00 25.60  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.591 13.525  11.623 1.00 23.41  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.921 14.041  11.300 1.00 24.74  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.770 12.857  10.858 1.00 25.06  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.677 11.782  11.474 1.00 26.85  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.559 14.759  12.492 1.00 25.69  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.972 15.334  12.206 1.00 27.79  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.149 16.675  12.865 1.00 29.14  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.073 14.371  12.668 1.00 29.67  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.522 13.002  9.757  1.00 24.96  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.427 11.942  9.303  1.00 27.01  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.855 12.546  9.315  1.00 28.90  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.076 13.638  8.766  1.00 28.60  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.108 11.399  7.886  1.00 28.38  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.162 10.392  7.440  1.00 28.81  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.695 10.811  7.799  1.00 27.52  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.794 11.859  9.968  1.00 30.09  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.190 12.301  9.978  1.00 32.21  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.074 11.204  9.354  1.00 34.41  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.621 10.076  9.164  1.00 34.36  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.656 12.643  11.396 1.00 33.41  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.561 11.501  12.232 1.00 35.00  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.326 11.543  8.993  1.00 35.45  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.234 10.548  8.419  1.00 36.76  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.010 9.808   9.525  1.00 38.06  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.233 10.359  10.615 1.00 39.00  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.208 11.217  7.450  1.00 39.60  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.830 12.322  8.082  1.00 42.56  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.416 8.562   9.248  1.00 37.78  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.185 7.748   10.198 1.00 40.15  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.486 7.240   9.544  1.00 44.57  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.560 7.145   8.309  1.00 46.14  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.363 6.508   10.661 1.00 39.96  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.256 5.602   9.567  1.00 40.83  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.972 6.880   11.188 1.00 38.91  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.470 6.835   10.362 1.00 46.41  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.707 6.282   9.812  1.00 49.37  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.588 4.766   9.609  1.00 49.57  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.163 4.230   8.660  1.00 50.74  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.936 6.728   10.635 1.00 53.12  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.745 6.334   11.995 1.00 56.52  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.146 8.228   10.582 1.00 53.64  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.800 4.078   10.450 1.00 48.68  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.619 2.635   10.316 1.00 48.53  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.340 2.260   9.557  1.00 46.97  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.373 3.017   9.568  1.00 46.03  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.613 1.982   11.690 1.00 48.97  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.330 1.080   8.917  1.00 46.11  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.157 0.594   8.192  1.00 46.03  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.112 0.090   9.197  1.00 43.11  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.441 -0.720  10.071 1.00 42.85  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.522 -0.618  7.318  1.00 50.51  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 34.346 -0.291  6.078  1.00 59.62  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.538 -0.437  4.808  1.00 68.82  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.982 -1.064  3.833  1.00 72.13  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.336 0.138   4.786  1.00 69.51  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.868 0.543   9.043  1.00 40.56  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.766 0.046   9.861  1.00 39.22  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.175 -1.225  9.289  1.00 37.72  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.478 -1.599  8.151  1.00 38.86  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.331 -1.922  10.074 1.00 35.64  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.790 -3.199  9.640  1.00 35.29  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.279 -3.249  9.462  1.00 34.03  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.742 -4.337  9.223  1.00 34.55  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.252 -4.301  10.586 1.00 36.70  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.043 -4.523  10.614 1.00 41.53  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.574 -2.126  9.661  1.00 33.08  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.107 -2.127  9.547  1.00 32.88  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.717 -2.083  8.040  1.00 33.01  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.476 -1.589  7.201  1.00 33.54  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.494 -0.916  10.326 1.00 32.36  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.604 -1.068  11.847 1.00 36.70  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.507 -2.211  12.338 1.00 38.05  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.842 -0.049  12.542 1.00 35.04  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.567 -2.666  7.709  1.00 32.40  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.043 -2.617  6.334  1.00 33.63  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.738 -1.799  6.399  1.00 32.07  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.923 -2.077  7.264  1.00 31.41  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.700 -4.063  5.859  1.00 37.70  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.936 -4.696  5.496  1.00 40.31  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.751 -4.080  4.637  1.00 38.15  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.558 -0.804  5.513  1.00 30.97  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.330 -0.011  5.504  1.00 29.83  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.257 -0.777  4.701  1.00 29.97  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.539 -1.234  3.594  1.00 30.90  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.557 1.389   4.887  1.00 29.42  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.748 2.154   5.568  1.00 29.40  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.228 2.225   4.972  1.00 29.61  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.666 2.172   7.166  1.00 29.46  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.035 -0.915  5.240  1.00 27.48  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.949 -1.559  4.509  1.00 27.59  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.524 -0.689  3.321  1.00 26.72  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.482 0.552   3.430  1.00 25.72  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.748 -1.715  5.441  1.00 27.74  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.179 -1.315  2.188  1.00 27.74  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.659 -0.578  1.027  1.00 28.97  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.362 -1.296  0.718  1.00 29.07  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.356 -2.327  0.027  1.00 29.37  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.612 -0.636  -0.176 1.00 29.92  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.005 -0.088  0.109  1.00 32.30  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.017 1.395   0.461  1.00 34.63  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.359 1.846   0.851  1.00 36.18  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.604 2.990   1.491  1.00 37.04  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.609 3.793   1.837  1.00 35.78  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.843 3.319   1.822  1.00 36.48  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.270 -0.797  1.293  1.00 28.96  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.008 -1.532  1.265  1.00 29.25  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.842  -0.606  1.690  1.00 30.13  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.074 0.564   2.036  1.00 30.01  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.154 -2.679  2.259  1.00 28.89  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.248 -2.115  3.981  1.00 28.49  ? 56  CYS   A SG  1 
ATOM   392  N  N   A ASP   A 1 51  ? 8.607  -1.143  1.747  0.50 30.51  ? 57  ASP   A N   1 
ATOM   393  N  N   B ASP   A 1 51  ? 8.607  -1.193  1.717  0.50 30.64  ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.477  -0.367  2.253  0.50 30.52  ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.318  -0.611  2.103  0.50 30.83  ? 57  ASP   A CA  1 
ATOM   396  C  C   A ASP   A 1 51  ? 6.865  -1.021  3.508  0.50 30.47  ? 57  ASP   A C   1 
ATOM   397  C  C   B ASP   A 1 51  ? 6.754  -1.350  3.347  0.50 30.54  ? 57  ASP   A C   1 
ATOM   398  O  O   A ASP   A 1 51  ? 5.713  -0.703  3.841  0.50 30.14  ? 57  ASP   A O   1 
ATOM   399  O  O   B ASP   A 1 51  ? 5.536  -1.383  3.522  0.50 30.24  ? 57  ASP   A O   1 
ATOM   400  C  CB  A ASP   A 1 51  ? 6.400  -0.142  1.168  0.50 32.45  ? 57  ASP   A CB  1 
ATOM   401  C  CB  B ASP   A 1 51  ? 6.310  -0.798  0.943  0.50 32.49  ? 57  ASP   A CB  1 
ATOM   402  C  CG  A ASP   A 1 51  ? 5.567  -1.358  0.809  0.50 36.30  ? 57  ASP   A CG  1 
ATOM   403  C  CG  B ASP   A 1 51  ? 5.208  0.244   0.842  0.50 37.23  ? 57  ASP   A CG  1 
ATOM   404  O  OD1 A ASP   A 1 51  ? 6.062  -2.482  0.969  0.50 36.28  ? 57  ASP   A OD1 1 
ATOM   405  O  OD1 B ASP   A 1 51  ? 5.353  1.319   1.441  0.50 38.17  ? 57  ASP   A OD1 1 
ATOM   406  O  OD2 A ASP   A 1 51  ? 4.421  -1.178  0.356  0.50 40.31  ? 57  ASP   A OD2 1 
ATOM   407  O  OD2 B ASP   A 1 51  ? 4.224  0.000   0.102  0.50 40.70  ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 7.618  -1.944  4.197  1.00 29.43  ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 7.152  -2.659  5.420  1.00 28.97  ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.443  -1.709  6.403  1.00 28.11  ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 6.859  -0.549  6.572  1.00 26.97  ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.318  -3.357  6.126  1.00 29.66  ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 8.882  -4.898  5.348  1.00 29.73  ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.371  -2.214  7.041  1.00 26.36  ? 59  GLN   A N   1 
ATOM   415  C  CA  . GLN   A 1 53  ? 4.647  -1.493  8.087  1.00 25.99  ? 59  GLN   A CA  1 
ATOM   416  C  C   . GLN   A 1 53  ? 4.594  -2.296  9.388  1.00 25.23  ? 59  GLN   A C   1 
ATOM   417  O  O   . GLN   A 1 53  ? 3.806  -1.967  10.276 1.00 25.05  ? 59  GLN   A O   1 
ATOM   418  C  CB  . GLN   A 1 53  ? 3.231  -1.061  7.639  1.00 27.98  ? 59  GLN   A CB  1 
ATOM   419  C  CG  . GLN   A 1 53  ? 3.189  0.253   6.934  1.00 32.84  ? 59  GLN   A CG  1 
ATOM   420  C  CD  . GLN   A 1 53  ? 1.740  0.673   6.724  1.00 35.39  ? 59  GLN   A CD  1 
ATOM   421  O  OE1 . GLN   A 1 53  ? 1.186  0.499   5.629  1.00 36.22  ? 59  GLN   A OE1 1 
ATOM   422  N  NE2 . GLN   A 1 53  ? 1.099  1.208   7.784  1.00 33.61  ? 59  GLN   A NE2 1 
ATOM   423  N  N   . THR   A 1 54  ? 5.423  -3.383  9.512  1.00 23.55  ? 60  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 54  ? 5.551  -4.160  10.740 1.00 23.31  ? 60  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 54  ? 7.060  -4.361  10.934 1.00 21.85  ? 60  THR   A C   1 
ATOM   426  O  O   . THR   A 1 54  ? 7.847  -4.430  9.978  1.00 23.24  ? 60  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 54  ? 4.827  -5.527  10.716 1.00 26.35  ? 60  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 54  ? 5.454  -6.338  9.722  1.00 30.14  ? 60  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 54  ? 3.337  -5.405  10.408 1.00 27.22  ? 60  THR   A CG2 1 
ATOM   430  N  N   . GLY   A 1 55  ? 7.450  -4.384  12.190 1.00 21.25  ? 61  GLY   A N   1 
ATOM   431  C  CA  . GLY   A 1 55  ? 8.860  -4.536  12.532 1.00 20.19  ? 61  GLY   A CA  1 
ATOM   432  C  C   . GLY   A 1 55  ? 9.021  -4.701  14.027 1.00 19.62  ? 61  GLY   A C   1 
ATOM   433  O  O   . GLY   A 1 55  ? 8.064  -5.045  14.710 1.00 21.08  ? 61  GLY   A O   1 
ATOM   434  N  N   . VAL   A 1 56  ? 10.241 -4.537  14.507 1.00 18.95  ? 62  VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 56  ? 10.584 -4.686  15.921 1.00 19.21  ? 62  VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 56  ? 11.463 -3.494  16.288 1.00 20.35  ? 62  VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 56  ? 12.350 -3.130  15.521 1.00 21.21  ? 62  VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 56  ? 11.363 -6.035  16.171 1.00 21.13  ? 62  VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 56  ? 11.771 -6.168  17.641 1.00 21.87  ? 62  VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 56  ? 10.494 -7.218  15.795 1.00 22.91  ? 62  VAL   A CG2 1 
ATOM   441  N  N   . TYR   A 1 57  ? 11.221 -2.892  17.476 1.00 19.52  ? 63  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 57  ? 12.087 -1.755  17.869 1.00 19.03  ? 63  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 57  ? 12.655 -2.006  19.266 1.00 20.65  ? 63  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 57  ? 12.033 -2.704  20.058 1.00 21.20  ? 63  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 57  ? 11.349 -0.393  17.814 1.00 19.28  ? 63  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 57  ? 10.426 -0.087  18.982 1.00 20.22  ? 63  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 57  ? 9.156  -0.655  19.063 1.00 20.70  ? 63  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 57  ? 10.821 0.774   20.007 1.00 19.93  ? 63  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 57  ? 8.311  -0.385  20.136 1.00 21.46  ? 63  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 57  ? 9.961  1.078   21.073 1.00 21.00  ? 63  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 57  ? 8.710  0.482   21.147 1.00 22.05  ? 63  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 57  ? 7.834  0.751   22.201 1.00 23.70  ? 63  TYR   A OH  1 
ATOM   453  N  N   . TYR   A 1 58  ? 13.810 -1.388  19.549 1.00 20.45  ? 64  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 58  ? 14.427 -1.499  20.869 1.00 21.40  ? 64  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 58  ? 13.978 -0.339  21.739 1.00 21.50  ? 64  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 58  ? 14.182 0.814   21.360 1.00 21.32  ? 64  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 58  ? 15.957 -1.535  20.798 1.00 21.54  ? 64  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 58  ? 16.549 -1.662  22.177 1.00 22.43  ? 64  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 58  ? 16.241 -2.752  22.991 1.00 23.14  ? 64  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 58  ? 17.364 -0.667  22.699 1.00 24.07  ? 64  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 58  ? 16.792 -2.879  24.274 1.00 24.78  ? 64  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 58  ? 17.930 -0.787  23.973 1.00 25.80  ? 64  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 58  ? 17.607 -1.873  24.772 1.00 26.22  ? 64  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 58  ? 18.135 -1.958  26.048 1.00 28.56  ? 64  TYR   A OH  1 
ATOM   465  N  N   . CYS   A 1 59  ? 13.482 -0.661  22.962 1.00 21.37  ? 65  CYS   A N   1 
ATOM   466  C  CA  . CYS   A 1 59  ? 13.025 0.314   23.936 1.00 22.50  ? 65  CYS   A CA  1 
ATOM   467  C  C   . CYS   A 1 59  ? 14.002 0.218   25.138 1.00 23.57  ? 65  CYS   A C   1 
ATOM   468  O  O   . CYS   A 1 59  ? 13.897 -0.710  25.912 1.00 24.97  ? 65  CYS   A O   1 
ATOM   469  C  CB  . CYS   A 1 59  ? 11.587 -0.003  24.340 1.00 23.83  ? 65  CYS   A CB  1 
ATOM   470  S  SG  . CYS   A 1 59  ? 10.902 1.055   25.663 1.00 27.22  ? 65  CYS   A SG  1 
ATOM   471  N  N   . SER   A 1 60  ? 14.934 1.179   25.274 1.00 23.55  ? 66  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 60  ? 15.905 1.142   26.361 1.00 24.92  ? 66  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 60  ? 15.250 1.280   27.738 1.00 26.17  ? 66  SER   A C   1 
ATOM   474  O  O   . SER   A 1 60  ? 15.732 0.680   28.706 1.00 27.72  ? 66  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 60  ? 17.004 2.190   26.182 1.00 27.51  ? 66  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 60  ? 16.468 3.502   26.140 1.00 32.46  ? 66  SER   A OG  1 
ATOM   477  N  N   . SER   A 1 61  ? 14.145 2.054   27.841 1.00 25.50  ? 67  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 61  ? 13.453 2.231   29.133 1.00 25.69  ? 67  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 61  ? 12.745 0.960   29.661 1.00 26.37  ? 67  SER   A C   1 
ATOM   480  O  O   . SER   A 1 61  ? 12.268 0.965   30.808 1.00 27.25  ? 67  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 61  ? 12.469 3.399   29.087 1.00 26.31  ? 67  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 61  ? 11.376 3.107   28.233 1.00 28.94  ? 67  SER   A OG  1 
ATOM   483  N  N   . ARG   A 1 62  ? 12.693 -0.093  28.860 1.00 24.79  ? 68  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 62  ? 12.166 -1.382  29.305 1.00 25.23  ? 68  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 62  ? 13.181 -2.493  29.073 1.00 26.40  ? 68  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 62  ? 12.815 -3.647  29.262 1.00 26.81  ? 68  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 62  ? 10.886 -1.730  28.529 1.00 27.22  ? 68  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 62  ? 9.733  -0.790  28.791 1.00 27.81  ? 68  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 62  ? 9.124  -1.134  30.154 1.00 30.23  ? 68  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 62  ? 7.993  -0.253  30.460 1.00 32.84  ? 68  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 62  ? 8.106  0.929   31.050 1.00 35.91  ? 68  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 62  ? 9.295  1.364   31.463 1.00 34.63  ? 68  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 62  ? 7.027  1.673   31.270 1.00 36.57  ? 68  ARG   A NH2 1 
ATOM   494  N  N   . ARG   A 1 63  ? 14.395 -2.206  28.506 1.00 26.24  ? 69  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 63  ? 15.347 -3.267  28.112 1.00 27.88  ? 69  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 63  ? 14.628 -4.375  27.282 1.00 26.82  ? 69  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 63  ? 14.791 -5.563  27.552 1.00 28.07  ? 69  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 63  ? 16.054 -3.849  29.354 1.00 29.35  ? 69  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 63  ? 16.917 -2.812  30.067 1.00 33.28  ? 69  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 63  ? 17.710 -3.480  31.184 1.00 37.08  ? 69  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 63  ? 18.462 -2.513  31.991 1.00 40.80  ? 69  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 63  ? 18.373 -2.415  33.318 1.00 45.21  ? 69  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 63  ? 17.533 -3.191  33.993 1.00 45.91  ? 69  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 63  ? 19.091 -1.504  33.973 1.00 46.91  ? 69  ARG   A NH2 1 
ATOM   505  N  N   . LYS   A 1 64  ? 13.734 -3.956  26.334 1.00 25.39  ? 70  LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 64  ? 12.939 -4.918  25.579 1.00 25.87  ? 70  LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 64  ? 12.808 -4.535  24.118 1.00 24.69  ? 70  LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 64  ? 12.853 -3.351  23.785 1.00 24.68  ? 70  LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 64  ? 11.546 -5.081  26.204 1.00 29.88  ? 70  LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 64  ? 11.447 -6.383  26.994 1.00 38.87  ? 70  LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 64  ? 10.044 -6.673  27.480 1.00 47.49  ? 70  LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 64  ? 10.083 -7.515  28.741 1.00 54.20  ? 70  LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 64  ? 10.884 -6.864  29.826 1.00 57.80  ? 70  LYS   A NZ  1 
ATOM   514  N  N   . HIS   A 1 65  ? 12.630 -5.530  23.266 1.00 22.76  ? 71  HIS   A N   1 
ATOM   515  C  CA  . HIS   A 1 65  ? 12.426 -5.338  21.822 1.00 22.57  ? 71  HIS   A CA  1 
ATOM   516  C  C   . HIS   A 1 65  ? 10.970 -5.705  21.562 1.00 24.30  ? 71  HIS   A C   1 
ATOM   517  O  O   . HIS   A 1 65  ? 10.545 -6.839  21.878 1.00 26.06  ? 71  HIS   A O   1 
ATOM   518  C  CB  . HIS   A 1 65  ? 13.347 -6.294  21.036 1.00 22.62  ? 71  HIS   A CB  1 
ATOM   519  C  CG  . HIS   A 1 65  ? 14.794 -6.085  21.312 1.00 23.77  ? 71  HIS   A CG  1 
ATOM   520  N  ND1 . HIS   A 1 65  ? 15.639 -5.498  20.370 1.00 25.36  ? 71  HIS   A ND1 1 
ATOM   521  C  CD2 . HIS   A 1 65  ? 15.515 -6.397  22.416 1.00 24.24  ? 71  HIS   A CD2 1 
ATOM   522  C  CE1 . HIS   A 1 65  ? 16.833 -5.462  20.934 1.00 25.29  ? 71  HIS   A CE1 1 
ATOM   523  N  NE2 . HIS   A 1 65  ? 16.806 -5.980  22.175 1.00 25.02  ? 71  HIS   A NE2 1 
ATOM   524  N  N   . TYR   A 1 66  ? 10.181 -4.741  21.073 1.00 21.76  ? 72  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 66  ? 8.756  -4.934  20.886 1.00 21.39  ? 72  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 66  ? 8.375  -5.033  19.410 1.00 20.57  ? 72  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 66  ? 8.751  -4.168  18.638 1.00 21.06  ? 72  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 66  ? 7.979  -3.728  21.461 1.00 22.08  ? 72  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 66  ? 8.043  -3.604  22.958 1.00 22.13  ? 72  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 66  ? 7.343  -4.485  23.776 1.00 23.41  ? 72  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 66  ? 8.774  -2.588  23.560 1.00 22.97  ? 72  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 66  ? 7.346  -4.339  25.168 1.00 25.03  ? 72  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 66  ? 8.793  -2.435  24.945 1.00 23.59  ? 72  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 66  ? 8.068  -3.301  25.745 1.00 26.18  ? 72  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 66  ? 8.110  -3.154  27.123 1.00 28.40  ? 72  TYR   A OH  1 
ATOM   536  N  N   . PRO   A 1 67  ? 7.559  -6.025  19.065 1.00 21.14  ? 73  PRO   A N   1 
ATOM   537  C  CA  . PRO   A 1 67  ? 7.039  -6.089  17.677 1.00 21.87  ? 73  PRO   A CA  1 
ATOM   538  C  C   . PRO   A 1 67  ? 5.944  -4.994  17.575 1.00 23.89  ? 73  PRO   A C   1 
ATOM   539  O  O   . PRO   A 1 67  ? 5.134  -4.831  18.516 1.00 25.45  ? 73  PRO   A O   1 
ATOM   540  C  CB  . PRO   A 1 67  ? 6.384  -7.510  17.592 1.00 24.50  ? 73  PRO   A CB  1 
ATOM   541  C  CG  . PRO   A 1 67  ? 6.104  -7.897  19.005 1.00 25.66  ? 73  PRO   A CG  1 
ATOM   542  C  CD  . PRO   A 1 67  ? 7.047  -7.133  19.927 1.00 22.92  ? 73  PRO   A CD  1 
ATOM   543  N  N   . VAL   A 1 68  ? 5.898  -4.287  16.449 1.00 21.38  ? 74  VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 68  ? 4.924  -3.203  16.268 1.00 22.01  ? 74  VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 68  ? 4.467  -3.099  14.807 1.00 22.64  ? 74  VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 68  ? 5.204  -3.471  13.873 1.00 21.71  ? 74  VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 68  ? 5.545  -1.832  16.668 1.00 24.81  ? 74  VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 68  ? 5.579  -1.644  18.189 1.00 26.81  ? 74  VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 68  ? 6.910  -1.591  16.025 1.00 25.45  ? 74  VAL   A CG2 1 
ATOM   550  N  N   . SER   A 1 69  ? 3.246  -2.494  14.624 1.00 21.59  ? 75  SER   A N   1 
ATOM   551  C  CA  . SER   A 1 69  ? 2.707  -2.081  13.338 1.00 22.47  ? 75  SER   A CA  1 
ATOM   552  C  C   . SER   A 1 69  ? 2.909  -0.543  13.367 1.00 22.44  ? 75  SER   A C   1 
ATOM   553  O  O   . SER   A 1 69  ? 2.644  0.088   14.409 1.00 23.15  ? 75  SER   A O   1 
ATOM   554  C  CB  . SER   A 1 69  ? 1.199  -2.325  13.277 1.00 25.17  ? 75  SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 69  ? 0.959  -3.711  13.095 1.00 32.70  ? 75  SER   A OG  1 
ATOM   556  N  N   . PHE   A 1 70  ? 3.392  0.027   12.286 1.00 20.32  ? 76  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 70  ? 3.637  1.463   12.244 1.00 21.38  ? 76  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 70  ? 3.089  2.093   10.970 1.00 23.29  ? 76  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 70  ? 3.002  1.437   9.926  1.00 25.21  ? 76  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 70  ? 5.126  1.811   12.483 1.00 21.78  ? 76  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 70  ? 6.074  1.075   11.567 1.00 21.20  ? 76  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 70  ? 6.588  -0.169  11.920 1.00 21.75  ? 76  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 70  ? 6.436  1.611   10.340 1.00 22.61  ? 76  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 70  ? 7.473  -0.842  11.076 1.00 21.94  ? 76  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 70  ? 7.316  0.935   9.487  1.00 22.84  ? 76  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 70  ? 7.809  -0.309  9.850  1.00 22.16  ? 76  PHE   A CZ  1 
ATOM   567  N  N   . SER   A 1 71  ? 2.718  3.382   11.046 1.00 24.10  ? 77  SER   A N   1 
ATOM   568  C  CA  . SER   A 1 71  ? 2.173  4.085   9.899  1.00 25.51  ? 77  SER   A CA  1 
ATOM   569  C  C   . SER   A 1 71  ? 3.279  4.434   8.856  1.00 25.86  ? 77  SER   A C   1 
ATOM   570  O  O   . SER   A 1 71  ? 4.449  4.373   9.182  1.00 26.55  ? 77  SER   A O   1 
ATOM   571  C  CB  . SER   A 1 71  ? 1.465  5.361   10.372 1.00 26.44  ? 77  SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 71  ? 2.374  6.235   11.029 1.00 26.57  ? 77  SER   A OG  1 
ATOM   573  N  N   . LYS   A 1 72  ? 2.902  4.780   7.599  1.00 26.87  ? 78  LYS   A N   1 
ATOM   574  C  CA  . LYS   A 1 72  ? 3.901  5.182   6.598  1.00 28.43  ? 78  LYS   A CA  1 
ATOM   575  C  C   . LYS   A 1 72  ? 4.480  6.564   6.940  1.00 28.43  ? 78  LYS   A C   1 
ATOM   576  O  O   . LYS   A 1 72  ? 3.782  7.364   7.559  1.00 28.96  ? 78  LYS   A O   1 
ATOM   577  C  CB  . LYS   A 1 72  ? 3.308  5.150   5.158  1.00 30.41  ? 78  LYS   A CB  1 
ATOM   578  C  CG  . LYS   A 1 72  ? 3.042  3.689   4.684  1.00 32.36  ? 78  LYS   A CG  1 
ATOM   579  C  CD  . LYS   A 1 72  ? 2.439  3.585   3.266  1.00 39.07  ? 78  LYS   A CD  1 
ATOM   580  C  CE  . LYS   A 1 72  ? 2.324  2.135   2.857  1.00 42.94  ? 78  LYS   A CE  1 
ATOM   581  N  NZ  . LYS   A 1 72  ? 1.890  1.985   1.442  1.00 46.25  ? 78  LYS   A NZ  1 
ATOM   582  N  N   . PRO   A 1 73  ? 5.705  6.876   6.469  1.00 28.12  ? 79  PRO   A N   1 
ATOM   583  C  CA  . PRO   A 1 73  ? 6.325  8.190   6.807  1.00 28.22  ? 79  PRO   A CA  1 
ATOM   584  C  C   . PRO   A 1 73  ? 5.438  9.368   6.408  1.00 28.27  ? 79  PRO   A C   1 
ATOM   585  O  O   . PRO   A 1 73  ? 4.964  9.428   5.255  1.00 28.91  ? 79  PRO   A O   1 
ATOM   586  C  CB  . PRO   A 1 73  ? 7.646  8.185   6.026  1.00 30.34  ? 79  PRO   A CB  1 
ATOM   587  C  CG  . PRO   A 1 73  ? 7.992  6.698   5.852  1.00 31.92  ? 79  PRO   A CG  1 
ATOM   588  C  CD  . PRO   A 1 73  ? 6.628  6.008   5.700  1.00 28.45  ? 79  PRO   A CD  1 
ATOM   589  N  N   A SER   A 1 74  ? 5.181  10.282  7.342  0.50 27.72  ? 80  SER   A N   1 
ATOM   590  N  N   B SER   A 1 74  ? 5.170  10.277  7.346  0.50 27.66  ? 80  SER   A N   1 
ATOM   591  C  CA  A SER   A 1 74  ? 4.303  11.423  7.058  0.50 28.45  ? 80  SER   A CA  1 
ATOM   592  C  CA  B SER   A 1 74  ? 4.282  11.417  7.076  0.50 28.33  ? 80  SER   A CA  1 
ATOM   593  C  C   A SER   A 1 74  ? 4.657  12.675  7.886  0.50 28.45  ? 80  SER   A C   1 
ATOM   594  C  C   B SER   A 1 74  ? 4.682  12.681  7.863  0.50 28.39  ? 80  SER   A C   1 
ATOM   595  O  O   A SER   A 1 74  ? 5.495  12.620  8.787  0.50 28.08  ? 80  SER   A O   1 
ATOM   596  O  O   B SER   A 1 74  ? 5.551  12.635  8.735  0.50 28.03  ? 80  SER   A O   1 
ATOM   597  C  CB  A SER   A 1 74  ? 2.836  11.025  7.242  0.50 30.29  ? 80  SER   A CB  1 
ATOM   598  C  CB  B SER   A 1 74  ? 2.834  11.046  7.410  0.50 30.00  ? 80  SER   A CB  1 
ATOM   599  O  OG  A SER   A 1 74  ? 2.480  10.904  8.609  0.50 32.81  ? 80  SER   A OG  1 
ATOM   600  O  OG  B SER   A 1 74  ? 2.434  9.806   6.856  0.50 32.13  ? 80  SER   A OG  1 
ATOM   601  N  N   . LEU   A 1 75  ? 4.021  13.811  7.569  1.00 28.39  ? 81  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 75  ? 4.262  15.063  8.285  1.00 29.28  ? 81  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 75  ? 3.320  15.012  9.495  1.00 30.18  ? 81  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 75  ? 2.099  14.892  9.312  1.00 31.45  ? 81  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 75  ? 3.864  16.210  7.344  1.00 30.06  ? 81  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 75  ? 4.275  17.601  7.725  1.00 33.42  ? 81  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 75  ? 5.757  17.730  7.809  1.00 32.86  ? 81  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 75  ? 3.680  18.632  6.744  1.00 34.42  ? 81  LEU   A CD2 1 
ATOM   609  N  N   . ILE   A 1 76  ? 3.877  15.066  10.723 1.00 29.13  ? 82  ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 76  ? 3.116  14.902  11.967 1.00 29.69  ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 3.430  16.012  12.965 1.00 29.93  ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.593  16.373  13.136 1.00 28.80  ? 82  ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 76  ? 3.428  13.494  12.578 1.00 30.81  ? 82  ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 76  ? 2.758  12.365  11.761 1.00 33.65  ? 82  ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 76  ? 3.057  13.398  14.095 1.00 30.52  ? 82  ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 76  ? 3.190  10.984  12.188 1.00 36.57  ? 82  ILE   A CD1 1 
ATOM   617  N  N   . PHE   A 1 77  ? 2.386  16.552  13.630 1.00 30.51  ? 83  PHE   A N   1 
ATOM   618  C  CA  . PHE   A 1 77  ? 2.610  17.579  14.648 1.00 32.26  ? 83  PHE   A CA  1 
ATOM   619  C  C   . PHE   A 1 77  ? 3.238  16.964  15.906 1.00 30.86  ? 83  PHE   A C   1 
ATOM   620  O  O   . PHE   A 1 77  ? 2.724  15.997  16.474 1.00 32.09  ? 83  PHE   A O   1 
ATOM   621  C  CB  . PHE   A 1 77  ? 1.318  18.304  15.026 1.00 33.79  ? 83  PHE   A CB  1 
ATOM   622  C  CG  . PHE   A 1 77  ? 1.614  19.620  15.711 1.00 36.36  ? 83  PHE   A CG  1 
ATOM   623  C  CD1 . PHE   A 1 77  ? 2.205  20.660  15.021 1.00 38.33  ? 83  PHE   A CD1 1 
ATOM   624  C  CD2 . PHE   A 1 77  ? 1.326  19.801  17.055 1.00 38.60  ? 83  PHE   A CD2 1 
ATOM   625  C  CE1 . PHE   A 1 77  ? 2.488  21.869  15.655 1.00 39.89  ? 83  PHE   A CE1 1 
ATOM   626  C  CE2 . PHE   A 1 77  ? 1.559  21.024  17.673 1.00 39.30  ? 83  PHE   A CE2 1 
ATOM   627  C  CZ  . PHE   A 1 77  ? 2.134  22.046  16.974 1.00 39.78  ? 83  PHE   A CZ  1 
ATOM   628  N  N   . VAL   A 1 78  ? 4.339  17.534  16.333 1.00 29.06  ? 84  VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 78  ? 5.091  17.056  17.491 1.00 29.02  ? 84  VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 78  ? 5.145  18.153  18.553 1.00 30.38  ? 84  VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 78  ? 5.546  19.289  18.264 1.00 30.30  ? 84  VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 78  ? 6.519  16.637  17.042 1.00 28.16  ? 84  VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 78  ? 7.406  16.308  18.253 1.00 28.03  ? 84  VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 78  ? 6.447  15.469  16.068 1.00 27.95  ? 84  VAL   A CG2 1 
ATOM   635  N  N   . GLU   A 1 79  ? 4.711  17.818  19.772 1.00 31.91  ? 85  GLU   A N   1 
ATOM   636  C  CA  . GLU   A 1 79  ? 4.690  18.764  20.883 1.00 32.98  ? 85  GLU   A CA  1 
ATOM   637  C  C   . GLU   A 1 79  ? 6.069  19.357  21.224 1.00 32.97  ? 85  GLU   A C   1 
ATOM   638  O  O   . GLU   A 1 79  ? 7.102  18.742  20.948 1.00 32.25  ? 85  GLU   A O   1 
ATOM   639  C  CB  . GLU   A 1 79  ? 4.071  18.112  22.135 1.00 36.44  ? 85  GLU   A CB  1 
ATOM   640  C  CG  . GLU   A 1 79  ? 2.579  17.859  21.995 1.00 42.32  ? 85  GLU   A CG  1 
ATOM   641  C  CD  . GLU   A 1 79  ? 1.810  19.145  21.759 1.00 51.34  ? 85  GLU   A CD  1 
ATOM   642  O  OE1 . GLU   A 1 79  ? 1.807  20.001  22.673 1.00 53.74  ? 85  GLU   A OE1 1 
ATOM   643  O  OE2 . GLU   A 1 79  ? 1.266  19.326  20.643 1.00 53.23  ? 85  GLU   A OE2 1 
ATOM   644  N  N   . ALA   A 1 80  ? 6.067  20.543  21.862 1.00 33.17  ? 86  ALA   A N   1 
ATOM   645  C  CA  . ALA   A 1 80  ? 7.305  21.176  22.303 1.00 34.38  ? 86  ALA   A CA  1 
ATOM   646  C  C   . ALA   A 1 80  ? 8.035  20.275  23.312 1.00 34.71  ? 86  ALA   A C   1 
ATOM   647  O  O   . ALA   A 1 80  ? 7.406  19.510  24.066 1.00 34.62  ? 86  ALA   A O   1 
ATOM   648  C  CB  . ALA   A 1 80  ? 7.013  22.537  22.933 1.00 34.71  ? 86  ALA   A CB  1 
ATOM   649  N  N   . SER   A 1 81  ? 9.363  20.332  23.270 1.00 34.18  ? 87  SER   A N   1 
ATOM   650  C  CA  . SER   A 1 81  ? 10.263 19.602  24.168 1.00 33.60  ? 87  SER   A CA  1 
ATOM   651  C  C   . SER   A 1 81  ? 11.460 20.513  24.516 1.00 34.73  ? 87  SER   A C   1 
ATOM   652  O  O   . SER   A 1 81  ? 11.511 21.648  24.028 1.00 36.03  ? 87  SER   A O   1 
ATOM   653  C  CB  . SER   A 1 81  ? 10.771 18.326  23.495 1.00 32.49  ? 87  SER   A CB  1 
ATOM   654  O  OG  . SER   A 1 81  ? 11.714 18.618  22.468 1.00 31.84  ? 87  SER   A OG  1 
ATOM   655  N  N   . GLU   A 1 82  ? 12.444 20.023  25.311 1.00 34.81  ? 88  GLU   A N   1 
ATOM   656  C  CA  . GLU   A 1 82  ? 13.609 20.883  25.586 1.00 35.64  ? 88  GLU   A CA  1 
ATOM   657  C  C   . GLU   A 1 82  ? 14.445 21.112  24.293 1.00 33.77  ? 88  GLU   A C   1 
ATOM   658  O  O   . GLU   A 1 82  ? 15.179 22.097  24.226 1.00 33.14  ? 88  GLU   A O   1 
ATOM   659  C  CB  . GLU   A 1 82  ? 14.474 20.366  26.754 1.00 38.76  ? 88  GLU   A CB  1 
ATOM   660  C  CG  . GLU   A 1 82  ? 15.266 19.097  26.444 1.00 41.46  ? 88  GLU   A CG  1 
ATOM   661  C  CD  . GLU   A 1 82  ? 16.272 18.685  27.515 1.00 50.25  ? 88  GLU   A CD  1 
ATOM   662  O  OE1 . GLU   A 1 82  ? 16.047 17.639  28.169 1.00 52.48  ? 88  GLU   A OE1 1 
ATOM   663  O  OE2 . GLU   A 1 82  ? 17.282 19.405  27.702 1.00 50.35  ? 88  GLU   A OE2 1 
ATOM   664  N  N   . TYR   A 1 83  ? 14.262 20.280  23.229 1.00 32.05  ? 89  TYR   A N   1 
ATOM   665  C  CA  . TYR   A 1 83  ? 15.088 20.362  22.018 1.00 31.83  ? 89  TYR   A CA  1 
ATOM   666  C  C   . TYR   A 1 83  ? 14.517 21.109  20.827 1.00 31.07  ? 89  TYR   A C   1 
ATOM   667  O  O   . TYR   A 1 83  ? 15.274 21.603  19.980 1.00 30.58  ? 89  TYR   A O   1 
ATOM   668  C  CB  . TYR   A 1 83  ? 15.453 18.942  21.575 1.00 32.91  ? 89  TYR   A CB  1 
ATOM   669  C  CG  . TYR   A 1 83  ? 16.364 18.259  22.565 1.00 35.48  ? 89  TYR   A CG  1 
ATOM   670  C  CD1 . TYR   A 1 83  ? 17.706 18.608  22.660 1.00 36.88  ? 89  TYR   A CD1 1 
ATOM   671  C  CD2 . TYR   A 1 83  ? 15.877 17.298  23.440 1.00 37.57  ? 89  TYR   A CD2 1 
ATOM   672  C  CE1 . TYR   A 1 83  ? 18.550 17.984  23.567 1.00 38.86  ? 89  TYR   A CE1 1 
ATOM   673  C  CE2 . TYR   A 1 83  ? 16.706 16.684  24.371 1.00 39.31  ? 89  TYR   A CE2 1 
ATOM   674  C  CZ  . TYR   A 1 83  ? 18.040 17.036  24.438 1.00 41.03  ? 89  TYR   A CZ  1 
ATOM   675  O  OH  . TYR   A 1 83  ? 18.867 16.399  25.333 1.00 44.83  ? 89  TYR   A OH  1 
ATOM   676  N  N   . TYR   A 1 84  ? 13.195 21.162  20.727 1.00 30.02  ? 90  TYR   A N   1 
ATOM   677  C  CA  . TYR   A 1 84  ? 12.541 21.863  19.633 1.00 29.27  ? 90  TYR   A CA  1 
ATOM   678  C  C   . TYR   A 1 84  ? 11.254 22.490  20.147 1.00 30.79  ? 90  TYR   A C   1 
ATOM   679  O  O   . TYR   A 1 84  ? 10.553 21.898  20.982 1.00 30.79  ? 90  TYR   A O   1 
ATOM   680  C  CB  . TYR   A 1 84  ? 12.110 20.877  18.514 1.00 27.40  ? 90  TYR   A CB  1 
ATOM   681  C  CG  . TYR   A 1 84  ? 13.202 20.080  17.850 1.00 25.73  ? 90  TYR   A CG  1 
ATOM   682  C  CD1 . TYR   A 1 84  ? 13.941 20.612  16.796 1.00 25.49  ? 90  TYR   A CD1 1 
ATOM   683  C  CD2 . TYR   A 1 84  ? 13.422 18.749  18.190 1.00 26.06  ? 90  TYR   A CD2 1 
ATOM   684  C  CE1 . TYR   A 1 84  ? 14.937 19.881  16.179 1.00 25.34  ? 90  TYR   A CE1 1 
ATOM   685  C  CE2 . TYR   A 1 84  ? 14.394 18.000  17.553 1.00 25.43  ? 90  TYR   A CE2 1 
ATOM   686  C  CZ  . TYR   A 1 84  ? 15.108 18.547  16.503 1.00 25.31  ? 90  TYR   A CZ  1 
ATOM   687  O  OH  . TYR   A 1 84  ? 16.084 17.781  15.891 1.00 24.12  ? 90  TYR   A OH  1 
ATOM   688  N  N   . PRO   A 1 85  ? 10.844 23.629  19.555 1.00 32.17  ? 91  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? 9.485  24.120  19.842 1.00 32.52  ? 91  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? 8.447  23.211  19.143 1.00 32.50  ? 91  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? 8.814  22.355  18.292 1.00 31.26  ? 91  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? 9.481  25.541  19.245 1.00 33.75  ? 91  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? 10.455 25.476  18.096 1.00 34.17  ? 91  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? 11.512 24.412  18.489 1.00 31.78  ? 91  PRO   A CD  1 
ATOM   695  N  N   . ALA   A 1 86  ? 7.135  23.401  19.448 1.00 32.58  ? 92  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 86  ? 6.099  22.580  18.785 1.00 33.46  ? 92  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 86  ? 6.126  22.887  17.286 1.00 33.07  ? 92  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 86  ? 6.279  24.056  16.896 1.00 33.07  ? 92  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 86  ? 4.726  22.843  19.367 1.00 34.17  ? 92  ALA   A CB  1 
ATOM   700  N  N   . ARG   A 1 87  ? 6.208  21.823  16.467 1.00 31.74  ? 93  ARG   A N   1 
ATOM   701  C  CA  . ARG   A 1 87  ? 6.375  21.972  15.018 1.00 31.27  ? 93  ARG   A CA  1 
ATOM   702  C  C   . ARG   A 1 87  ? 5.865  20.724  14.274 1.00 31.99  ? 93  ARG   A C   1 
ATOM   703  O  O   . ARG   A 1 87  ? 5.516  19.723  14.929 1.00 32.61  ? 93  ARG   A O   1 
ATOM   704  C  CB  . ARG   A 1 87  ? 7.865  22.213  14.686 1.00 31.14  ? 93  ARG   A CB  1 
ATOM   705  C  CG  . ARG   A 1 87  ? 8.693  20.896  14.641 1.00 30.99  ? 93  ARG   A CG  1 
ATOM   706  C  CD  . ARG   A 1 87  ? 10.094 21.040  15.164 1.00 32.26  ? 93  ARG   A CD  1 
ATOM   707  N  NE  . ARG   A 1 87  ? 10.988 19.988  14.653 1.00 28.76  ? 93  ARG   A NE  1 
ATOM   708  C  CZ  . ARG   A 1 87  ? 11.024 18.740  15.125 1.00 29.48  ? 93  ARG   A CZ  1 
ATOM   709  N  NH1 . ARG   A 1 87  ? 10.204 18.369  16.119 1.00 26.86  ? 93  ARG   A NH1 1 
ATOM   710  N  NH2 . ARG   A 1 87  ? 11.890 17.861  14.627 1.00 27.22  ? 93  ARG   A NH2 1 
ATOM   711  N  N   . TYR   A 1 88  ? 5.864  20.751  12.915 1.00 30.97  ? 94  TYR   A N   1 
ATOM   712  C  CA  . TYR   A 1 88  ? 5.559  19.521  12.187 1.00 31.50  ? 94  TYR   A CA  1 
ATOM   713  C  C   . TYR   A 1 88  ? 6.897  18.856  11.886 1.00 29.72  ? 94  TYR   A C   1 
ATOM   714  O  O   . TYR   A 1 88  ? 7.845  19.509  11.426 1.00 30.17  ? 94  TYR   A O   1 
ATOM   715  C  CB  . TYR   A 1 88  ? 4.827  19.768  10.878 1.00 32.80  ? 94  TYR   A CB  1 
ATOM   716  C  CG  . TYR   A 1 88  ? 3.399  20.181  11.115 1.00 33.91  ? 94  TYR   A CG  1 
ATOM   717  C  CD1 . TYR   A 1 88  ? 2.385  19.238  11.178 1.00 34.90  ? 94  TYR   A CD1 1 
ATOM   718  C  CD2 . TYR   A 1 88  ? 3.066  21.512  11.336 1.00 36.30  ? 94  TYR   A CD2 1 
ATOM   719  C  CE1 . TYR   A 1 88  ? 1.065  19.611  11.406 1.00 36.50  ? 94  TYR   A CE1 1 
ATOM   720  C  CE2 . TYR   A 1 88  ? 1.752  21.897  11.569 1.00 37.14  ? 94  TYR   A CE2 1 
ATOM   721  C  CZ  . TYR   A 1 88  ? 0.754  20.938  11.628 1.00 38.25  ? 94  TYR   A CZ  1 
ATOM   722  O  OH  . TYR   A 1 88  ? -0.555 21.298  11.859 1.00 40.17  ? 94  TYR   A OH  1 
ATOM   723  N  N   . GLN   A 1 89  ? 6.977  17.557  12.172 1.00 27.07  ? 95  GLN   A N   1 
ATOM   724  C  CA  . GLN   A 1 89  ? 8.185  16.793  11.849 1.00 26.40  ? 95  GLN   A CA  1 
ATOM   725  C  C   . GLN   A 1 89  ? 7.839  15.935  10.639 1.00 26.21  ? 95  GLN   A C   1 
ATOM   726  O  O   . GLN   A 1 89  ? 6.800  15.246  10.648 1.00 26.96  ? 95  GLN   A O   1 
ATOM   727  C  CB  . GLN   A 1 89  ? 8.633  15.907  13.026 1.00 25.93  ? 95  GLN   A CB  1 
ATOM   728  C  CG  . GLN   A 1 89  ? 9.813  14.959  12.661 1.00 25.70  ? 95  GLN   A CG  1 
ATOM   729  C  CD  . GLN   A 1 89  ? 10.556 14.480  13.910 1.00 25.47  ? 95  GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A 1 89  ? 10.741 15.207  14.874 1.00 24.21  ? 95  GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A 1 89  ? 11.009 13.242  13.908 1.00 23.96  ? 95  GLN   A NE2 1 
ATOM   732  N  N   . SER   A 1 90  ? 8.725  15.915  9.628  1.00 24.86  ? 96  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 90  ? 8.453  15.162  8.406  1.00 25.41  ? 96  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 90  ? 9.089  13.743  8.436  1.00 24.28  ? 96  SER   A C   1 
ATOM   735  O  O   . SER   A 1 90  ? 9.961  13.464  9.282  1.00 22.95  ? 96  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 90  ? 8.963  15.939  7.197  1.00 28.59  ? 96  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 90  ? 10.372 16.079  7.255  1.00 30.17  ? 96  SER   A OG  1 
ATOM   738  N  N   . HIS   A 1 91  ? 8.583  12.855  7.555  1.00 23.35  ? 97  HIS   A N   1 
ATOM   739  C  CA  . HIS   A 1 91  ? 9.081  11.473  7.419  1.00 23.09  ? 97  HIS   A CA  1 
ATOM   740  C  C   . HIS   A 1 91  ? 9.007  10.709  8.763  1.00 22.55  ? 97  HIS   A C   1 
ATOM   741  O  O   . HIS   A 1 91  ? 9.895  9.893   9.072  1.00 21.51  ? 97  HIS   A O   1 
ATOM   742  C  CB  . HIS   A 1 91  ? 10.523 11.503  6.887  1.00 24.08  ? 97  HIS   A CB  1 
ATOM   743  C  CG  . HIS   A 1 91  ? 10.645 12.155  5.535  1.00 27.55  ? 97  HIS   A CG  1 
ATOM   744  N  ND1 . HIS   A 1 91  ? 10.706 11.401  4.381  1.00 30.72  ? 97  HIS   A ND1 1 
ATOM   745  C  CD2 . HIS   A 1 91  ? 10.764 13.469  5.207  1.00 28.27  ? 97  HIS   A CD2 1 
ATOM   746  C  CE1 . HIS   A 1 91  ? 10.812 12.271  3.384  1.00 31.20  ? 97  HIS   A CE1 1 
ATOM   747  N  NE2 . HIS   A 1 91  ? 10.870 13.528  3.832  1.00 29.90  ? 97  HIS   A NE2 1 
ATOM   748  N  N   . LEU   A 1 92  ? 7.934  10.962  9.539  1.00 22.94  ? 98  LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 7.767  10.334  10.858 1.00 23.17  ? 98  LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 6.704  9.189   10.764 1.00 23.06  ? 98  LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 5.647  9.375   10.113 1.00 23.72  ? 98  LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 7.312  11.387  11.872 1.00 24.41  ? 98  LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 7.156  10.964  13.332 1.00 26.21  ? 98  LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 8.494  10.540  13.901 1.00 25.68  ? 98  LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 6.601  12.142  14.188 1.00 27.69  ? 98  LEU   A CD2 1 
ATOM   756  N  N   . MET   A 1 93  ? 7.012  8.019   11.404 1.00 21.30  ? 99  MET   A N   1 
ATOM   757  C  CA  . MET   A 1 93  ? 6.099  6.865   11.417 1.00 21.51  ? 99  MET   A CA  1 
ATOM   758  C  C   . MET   A 1 93  ? 5.651  6.663   12.875 1.00 22.75  ? 99  MET   A C   1 
ATOM   759  O  O   . MET   A 1 93  ? 6.506  6.715   13.760 1.00 22.79  ? 99  MET   A O   1 
ATOM   760  C  CB  . MET   A 1 93  ? 6.875  5.628   10.927 1.00 21.24  ? 99  MET   A CB  1 
ATOM   761  C  CG  . MET   A 1 93  ? 7.376  5.778   9.469  1.00 22.37  ? 99  MET   A CG  1 
ATOM   762  S  SD  . MET   A 1 93  ? 8.508  4.503   8.960  1.00 27.49  ? 99  MET   A SD  1 
ATOM   763  C  CE  . MET   A 1 93  ? 9.828  4.765   10.004 1.00 25.44  ? 99  MET   A CE  1 
ATOM   764  N  N   . LEU   A 1 94  ? 4.346  6.438   13.146 1.00 22.82  ? 100 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 94  ? 3.907  6.256   14.534 1.00 23.52  ? 100 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 94  ? 3.462  4.811   14.755 1.00 23.25  ? 100 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 94  ? 2.966  4.150   13.831 1.00 23.68  ? 100 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 94  ? 2.700  7.165   14.906 1.00 25.32  ? 100 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 94  ? 2.945  8.658   14.928 1.00 28.44  ? 100 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 94  ? 1.648  9.394   15.293 1.00 30.95  ? 100 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 94  ? 4.068  9.034   15.884 1.00 29.25  ? 100 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 95  ? 3.601  4.379   15.995 1.00 22.38  ? 101 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 95  ? 3.135  3.056   16.443 1.00 23.07  ? 101 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 95  ? 2.616  3.178   17.889 1.00 22.91  ? 101 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 95  ? 2.948  4.142   18.600 1.00 23.06  ? 101 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 95  ? 4.307  2.052   16.425 1.00 23.10  ? 101 ALA   A CB  1 
ATOM   777  N  N   . VAL   A 1 96  ? 1.762  2.228   18.294 1.00 21.92  ? 102 VAL   A N   1 
ATOM   778  C  CA  . VAL   A 1 96  ? 1.317  2.141   19.669 1.00 22.30  ? 102 VAL   A CA  1 
ATOM   779  C  C   . VAL   A 1 96  ? 2.371  1.351   20.428 1.00 24.15  ? 102 VAL   A C   1 
ATOM   780  O  O   . VAL   A 1 96  ? 2.599  0.159   20.158 1.00 24.60  ? 102 VAL   A O   1 
ATOM   781  C  CB  . VAL   A 1 96  ? -0.088 1.488   19.752 1.00 23.37  ? 102 VAL   A CB  1 
ATOM   782  C  CG1 . VAL   A 1 96  ? -0.523 1.303   21.208 1.00 24.05  ? 102 VAL   A CG1 1 
ATOM   783  C  CG2 . VAL   A 1 96  ? -1.080 2.390   19.029 1.00 23.03  ? 102 VAL   A CG2 1 
ATOM   784  N  N   . GLY   A 1 97  ? 3.029  2.014   21.350 1.00 24.45  ? 103 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 97  ? 4.091  1.360   22.119 1.00 26.07  ? 103 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 97  ? 4.695  2.309   23.120 1.00 26.38  ? 103 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 97  ? 4.457  3.523   23.065 1.00 26.28  ? 103 GLY   A O   1 
ATOM   788  N  N   . HIS   A 1 98  ? 5.468  1.752   24.061 1.00 26.04  ? 104 HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 98  ? 6.054  2.579   25.105 1.00 25.95  ? 104 HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 98  ? 7.318  3.296   24.641 1.00 23.93  ? 104 HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 98  ? 8.130  2.751   23.924 1.00 23.86  ? 104 HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 98  ? 6.390  1.728   26.342 1.00 27.25  ? 104 HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 98  ? 6.970  2.542   27.458 1.00 30.47  ? 104 HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 98  ? 6.220  3.510   28.113 1.00 32.12  ? 104 HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 98  ? 8.231  2.562   27.951 1.00 31.81  ? 104 HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 98  ? 7.045  4.088   28.970 1.00 33.00  ? 104 HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 98  ? 8.267  3.553   28.912 1.00 32.73  ? 104 HIS   A NE2 1 
ATOM   798  N  N   . SER   A 1 99  ? 7.459  4.578   25.024 1.00 23.31  ? 105 SER   A N   1 
ATOM   799  C  CA  . SER   A 1 99  ? 8.678  5.319   24.780 1.00 23.92  ? 105 SER   A CA  1 
ATOM   800  C  C   . SER   A 1 99  ? 8.810  6.460   25.803 1.00 26.74  ? 105 SER   A C   1 
ATOM   801  O  O   . SER   A 1 99  ? 7.797  6.951   26.315 1.00 28.21  ? 105 SER   A O   1 
ATOM   802  C  CB  . SER   A 1 99  ? 8.720  5.865   23.355 1.00 24.65  ? 105 SER   A CB  1 
ATOM   803  O  OG  . SER   A 1 99  ? 7.763  6.889   23.159 1.00 26.20  ? 105 SER   A OG  1 
ATOM   804  N  N   . GLU   A 1 100 ? 10.058 6.746   26.215 1.00 26.19  ? 106 GLU   A N   1 
ATOM   805  C  CA  . GLU   A 1 100 ? 10.442 7.862   27.057 1.00 26.76  ? 106 GLU   A CA  1 
ATOM   806  C  C   . GLU   A 1 100 ? 11.521 8.671   26.317 1.00 27.68  ? 106 GLU   A C   1 
ATOM   807  O  O   . GLU   A 1 100 ? 12.101 8.199   25.311 1.00 27.47  ? 106 GLU   A O   1 
ATOM   808  C  CB  . GLU   A 1 100 ? 10.923 7.357   28.434 1.00 29.42  ? 106 GLU   A CB  1 
ATOM   809  C  CG  . GLU   A 1 100 ? 9.845  6.531   29.087 1.00 32.81  ? 106 GLU   A CG  1 
ATOM   810  C  CD  . GLU   A 1 100 ? 10.168 5.962   30.454 1.00 36.20  ? 106 GLU   A CD  1 
ATOM   811  O  OE1 . GLU   A 1 100 ? 11.002 6.561   31.158 1.00 35.19  ? 106 GLU   A OE1 1 
ATOM   812  O  OE2 . GLU   A 1 100 ? 9.595  4.910   30.814 1.00 35.90  ? 106 GLU   A OE2 1 
ATOM   813  N  N   . PRO   A 1 101 ? 11.743 9.936   26.710 1.00 28.92  ? 107 PRO   A N   1 
ATOM   814  C  CA  . PRO   A 1 101 ? 12.700 10.779  25.958 1.00 29.18  ? 107 PRO   A CA  1 
ATOM   815  C  C   . PRO   A 1 101 ? 14.053 10.121  25.618 1.00 28.10  ? 107 PRO   A C   1 
ATOM   816  O  O   . PRO   A 1 101 ? 14.470 10.140  24.449 1.00 28.28  ? 107 PRO   A O   1 
ATOM   817  C  CB  . PRO   A 1 101 ? 12.846 12.017  26.844 1.00 30.60  ? 107 PRO   A CB  1 
ATOM   818  C  CG  . PRO   A 1 101 ? 11.551 12.118  27.589 1.00 31.13  ? 107 PRO   A CG  1 
ATOM   819  C  CD  . PRO   A 1 101 ? 11.087 10.685  27.808 1.00 28.61  ? 107 PRO   A CD  1 
ATOM   820  N  N   . GLY   A 1 102 ? 14.663 9.453   26.597 1.00 26.76  ? 108 GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 102 ? 15.947 8.777   26.446 1.00 26.95  ? 108 GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 102 ? 15.906 7.527   25.569 1.00 26.48  ? 108 GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 102 ? 16.959 6.930   25.310 1.00 27.47  ? 108 GLY   A O   1 
ATOM   824  N  N   . ASP   A 1 103 ? 14.700 7.111   25.088 1.00 24.71  ? 109 ASP   A N   1 
ATOM   825  C  CA  . ASP   A 1 103 ? 14.612 5.999   24.146 1.00 24.14  ? 109 ASP   A CA  1 
ATOM   826  C  C   . ASP   A 1 103 ? 14.971 6.432   22.723 1.00 22.37  ? 109 ASP   A C   1 
ATOM   827  O  O   . ASP   A 1 103 ? 15.164 5.567   21.875 1.00 21.78  ? 109 ASP   A O   1 
ATOM   828  C  CB  . ASP   A 1 103 ? 13.222 5.336   24.107 1.00 23.94  ? 109 ASP   A CB  1 
ATOM   829  C  CG  . ASP   A 1 103 ? 12.967 4.570   25.392 1.00 25.50  ? 109 ASP   A CG  1 
ATOM   830  O  OD1 . ASP   A 1 103 ? 13.916 3.977   25.916 1.00 24.66  ? 109 ASP   A OD1 1 
ATOM   831  O  OD2 . ASP   A 1 103 ? 11.818 4.598   25.884 1.00 25.58  ? 109 ASP   A OD2 1 
ATOM   832  N  N   . CYS   A 1 104 ? 15.122 7.768   22.452 1.00 21.94  ? 110 CYS   A N   1 
ATOM   833  C  CA  . CYS   A 1 104 ? 15.490 8.206   21.094 1.00 20.92  ? 110 CYS   A CA  1 
ATOM   834  C  C   . CYS   A 1 104 ? 16.787 7.528   20.676 1.00 22.23  ? 110 CYS   A C   1 
ATOM   835  O  O   . CYS   A 1 104 ? 17.678 7.404   21.513 1.00 24.69  ? 110 CYS   A O   1 
ATOM   836  C  CB  . CYS   A 1 104 ? 15.629 9.725   21.052 1.00 21.89  ? 110 CYS   A CB  1 
ATOM   837  S  SG  . CYS   A 1 104 ? 14.032 10.586  21.102 1.00 25.09  ? 110 CYS   A SG  1 
ATOM   838  N  N   . GLY   A 1 105 ? 16.892 7.103   19.434 1.00 21.29  ? 111 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 105 ? 18.085 6.401   18.986 1.00 22.83  ? 111 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 105 ? 17.869 4.903   18.893 1.00 23.89  ? 111 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 105 ? 18.635 4.223   18.208 1.00 24.34  ? 111 GLY   A O   1 
ATOM   842  N  N   . GLY   A 1 106 ? 16.843 4.366   19.577 1.00 22.19  ? 112 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 106 ? 16.539 2.934   19.470 1.00 21.50  ? 112 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 106 ? 16.180 2.550   18.027 1.00 21.42  ? 112 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 106 ? 15.435 3.261   17.371 1.00 21.18  ? 112 GLY   A O   1 
ATOM   846  N  N   . ILE   A 1 107 ? 16.711 1.412   17.523 1.00 21.04  ? 113 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 107 ? 16.470 1.067   16.123 1.00 21.72  ? 113 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 107 ? 15.155 0.325   15.947 1.00 20.93  ? 113 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 107 ? 14.828 -0.557  16.749 1.00 22.17  ? 113 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 107 ? 17.674 0.239   15.552 1.00 23.87  ? 113 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 107 ? 18.896 1.191   15.331 1.00 24.74  ? 113 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 107 ? 17.300 -0.467  14.217 1.00 24.68  ? 113 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 107 ? 20.238 0.518   15.085 1.00 27.80  ? 113 ILE   A CD1 1 
ATOM   854  N  N   . LEU   A 1 108 ? 14.437 0.669   14.854 1.00 19.61  ? 114 LEU   A N   1 
ATOM   855  C  CA  . LEU   A 1 108 ? 13.280 -0.062  14.344 1.00 20.39  ? 114 LEU   A CA  1 
ATOM   856  C  C   . LEU   A 1 108 ? 13.794 -0.843  13.094 1.00 21.60  ? 114 LEU   A C   1 
ATOM   857  O  O   . LEU   A 1 108 ? 14.421 -0.276  12.203 1.00 21.50  ? 114 LEU   A O   1 
ATOM   858  C  CB  . LEU   A 1 108 ? 12.195 0.917   13.918 1.00 19.82  ? 114 LEU   A CB  1 
ATOM   859  C  CG  . LEU   A 1 108 ? 11.012 0.318   13.132 1.00 22.83  ? 114 LEU   A CG  1 
ATOM   860  C  CD1 . LEU   A 1 108 ? 10.105 -0.576  14.067 1.00 23.16  ? 114 LEU   A CD1 1 
ATOM   861  C  CD2 . LEU   A 1 108 ? 10.197 1.473   12.512 1.00 23.74  ? 114 LEU   A CD2 1 
ATOM   862  N  N   . ARG   A 1 109 ? 13.550 -2.166  13.092 1.00 22.05  ? 115 ARG   A N   1 
ATOM   863  C  CA  . ARG   A 1 109 ? 13.977 -2.989  11.991 1.00 23.81  ? 115 ARG   A CA  1 
ATOM   864  C  C   . ARG   A 1 109 ? 12.887 -3.913  11.488 1.00 23.23  ? 115 ARG   A C   1 
ATOM   865  O  O   . ARG   A 1 109 ? 11.981 -4.302  12.219 1.00 22.64  ? 115 ARG   A O   1 
ATOM   866  C  CB  . ARG   A 1 109 ? 15.220 -3.807  12.354 1.00 27.08  ? 115 ARG   A CB  1 
ATOM   867  C  CG  . ARG   A 1 109 ? 15.210 -4.484  13.684 1.00 35.14  ? 115 ARG   A CG  1 
ATOM   868  C  CD  . ARG   A 1 109 ? 16.585 -5.171  13.836 1.00 41.12  ? 115 ARG   A CD  1 
ATOM   869  N  NE  . ARG   A 1 109 ? 17.550 -4.355  14.582 1.00 45.65  ? 115 ARG   A NE  1 
ATOM   870  C  CZ  . ARG   A 1 109 ? 18.716 -3.915  14.102 1.00 46.06  ? 115 ARG   A CZ  1 
ATOM   871  N  NH1 . ARG   A 1 109 ? 19.076 -4.193  12.850 1.00 44.26  ? 115 ARG   A NH1 1 
ATOM   872  N  NH2 . ARG   A 1 109 ? 19.533 -3.199  14.873 1.00 43.44  ? 115 ARG   A NH2 1 
ATOM   873  N  N   . CYS   A 1 110 ? 12.978 -4.221  10.200 1.00 23.63  ? 116 CYS   A N   1 
ATOM   874  C  CA  . CYS   A 1 110 ? 12.088 -5.198  9.576  1.00 25.72  ? 116 CYS   A CA  1 
ATOM   875  C  C   . CYS   A 1 110 ? 12.983 -6.342  8.980  1.00 27.97  ? 116 CYS   A C   1 
ATOM   876  O  O   . CYS   A 1 110 ? 14.205 -6.323  9.133  1.00 27.23  ? 116 CYS   A O   1 
ATOM   877  C  CB  . CYS   A 1 110 ? 11.312 -4.493  8.471  1.00 27.75  ? 116 CYS   A CB  1 
ATOM   878  S  SG  . CYS   A 1 110 ? 12.370 -3.974  7.101  1.00 27.66  ? 116 CYS   A SG  1 
ATOM   879  N  N   . GLN   A 1 111 ? 12.377 -7.311  8.255  1.00 31.36  ? 117 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 111 ? 13.155 -8.371  7.601  1.00 34.25  ? 117 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 111 ? 14.183 -7.842  6.584  1.00 34.83  ? 117 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 111 ? 15.092 -8.588  6.242  1.00 36.92  ? 117 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 111 ? 12.209 -9.344  6.878  1.00 37.88  ? 117 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 111 ? 11.362 -8.656  5.815  1.00 43.16  ? 117 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 111 ? 10.395 -9.583  5.132  1.00 50.77  ? 117 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 111 ? 9.172  -9.419  5.230  1.00 52.56  ? 117 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 111 ? 10.918 -10.567 4.407  1.00 52.85  ? 117 GLN   A NE2 1 
ATOM   888  N  N   . HIS   A 1 112 ? 14.093 -6.565  6.123  1.00 32.97  ? 118 HIS   A N   1 
ATOM   889  C  CA  . HIS   A 1 112 ? 15.059 -6.056  5.133  1.00 32.12  ? 118 HIS   A CA  1 
ATOM   890  C  C   . HIS   A 1 112 ? 16.230 -5.247  5.712  1.00 32.00  ? 118 HIS   A C   1 
ATOM   891  O  O   . HIS   A 1 112 ? 17.181 -4.907  4.983  1.00 32.46  ? 118 HIS   A O   1 
ATOM   892  C  CB  . HIS   A 1 112 ? 14.353 -5.245  4.042  1.00 32.69  ? 118 HIS   A CB  1 
ATOM   893  C  CG  . HIS   A 1 112 ? 13.206 -5.966  3.407  1.00 34.64  ? 118 HIS   A CG  1 
ATOM   894  N  ND1 . HIS   A 1 112 ? 11.912 -5.711  3.779  1.00 35.57  ? 118 HIS   A ND1 1 
ATOM   895  C  CD2 . HIS   A 1 112 ? 13.202 -6.877  2.398  1.00 35.98  ? 118 HIS   A CD2 1 
ATOM   896  C  CE1 . HIS   A 1 112 ? 11.146 -6.480  3.022  1.00 37.29  ? 118 HIS   A CE1 1 
ATOM   897  N  NE2 . HIS   A 1 112 ? 11.885 -7.213  2.177  1.00 37.35  ? 118 HIS   A NE2 1 
ATOM   898  N  N   . GLY   A 1 113 ? 16.176 -4.967  7.011  1.00 30.03  ? 119 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 113 ? 17.224 -4.207  7.656  1.00 28.93  ? 119 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 113 ? 16.664 -3.086  8.508  1.00 27.22  ? 119 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 113 ? 15.540 -3.175  8.994  1.00 26.91  ? 119 GLY   A O   1 
ATOM   902  N  N   . VAL   A 1 114 ? 17.461 -2.037  8.697  1.00 25.74  ? 120 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 114 ? 17.069 -0.879  9.518  1.00 25.28  ? 120 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 114 ? 16.098 -0.008  8.791  1.00 24.28  ? 120 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 114 ? 16.330 0.380   7.632  1.00 24.78  ? 120 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 114 ? 18.318 -0.056  9.905  1.00 26.12  ? 120 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 114 ? 17.928 1.193   10.710 1.00 26.57  ? 120 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 114 ? 19.312 -0.927  10.654 1.00 27.74  ? 120 VAL   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? 14.997 0.301   9.461  1.00 22.78  ? 121 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? 13.921 1.144   8.932  1.00 22.15  ? 121 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? 14.057 2.605   9.429  1.00 22.42  ? 121 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? 13.770 3.544   8.707  1.00 22.86  ? 121 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? 12.559 0.563   9.356  1.00 23.25  ? 121 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? 11.394 1.522   9.047  1.00 22.96  ? 121 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? 12.319 -0.830  8.800  1.00 23.35  ? 121 VAL   A CG2 1 
ATOM   916  N  N   . GLY   A 1 116 ? 14.432 2.772   10.704 1.00 21.61  ? 122 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 116 ? 14.555 4.104   11.293 1.00 22.01  ? 122 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 116 ? 14.940 4.057   12.761 1.00 21.46  ? 122 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 116 ? 15.360 3.009   13.252 1.00 21.50  ? 122 GLY   A O   1 
ATOM   920  N  N   . ILE   A 1 117 ? 14.874 5.212   13.435 1.00 20.92  ? 123 ILE   A N   1 
ATOM   921  C  CA  . ILE   A 1 117 ? 15.238 5.299   14.854 1.00 20.73  ? 123 ILE   A CA  1 
ATOM   922  C  C   . ILE   A 1 117 ? 14.144 6.000   15.632 1.00 20.27  ? 123 ILE   A C   1 
ATOM   923  O  O   . ILE   A 1 117 ? 13.475 6.876   15.105 1.00 19.42  ? 123 ILE   A O   1 
ATOM   924  C  CB  . ILE   A 1 117 ? 16.583 6.079   15.065 1.00 22.88  ? 123 ILE   A CB  1 
ATOM   925  C  CG1 . ILE   A 1 117 ? 16.606 7.370   14.259 1.00 24.67  ? 123 ILE   A CG1 1 
ATOM   926  C  CG2 . ILE   A 1 117 ? 17.781 5.179   14.754 1.00 25.81  ? 123 ILE   A CG2 1 
ATOM   927  C  CD1 . ILE   A 1 117 ? 17.847 8.274   14.697 1.00 26.44  ? 123 ILE   A CD1 1 
ATOM   928  N  N   . VAL   A 1 118 ? 13.983 5.653   16.947 1.00 20.16  ? 124 VAL   A N   1 
ATOM   929  C  CA  . VAL   A 1 118 ? 12.965 6.352   17.765 1.00 19.01  ? 124 VAL   A CA  1 
ATOM   930  C  C   . VAL   A 1 118 ? 13.336 7.871   17.790 1.00 18.93  ? 124 VAL   A C   1 
ATOM   931  O  O   . VAL   A 1 118 ? 14.512 8.226   17.941 1.00 19.66  ? 124 VAL   A O   1 
ATOM   932  C  CB  . VAL   A 1 118 ? 13.020 5.793   19.202 1.00 19.25  ? 124 VAL   A CB  1 
ATOM   933  C  CG1 . VAL   A 1 118 ? 12.110 6.597   20.122 1.00 20.42  ? 124 VAL   A CG1 1 
ATOM   934  C  CG2 . VAL   A 1 118 ? 12.691 4.296   19.246 1.00 19.70  ? 124 VAL   A CG2 1 
ATOM   935  N  N   . SER   A 1 119 ? 12.333 8.710   17.632 1.00 18.81  ? 125 SER   A N   1 
ATOM   936  C  CA  . SER   A 1 119 ? 12.549 10.144  17.569 1.00 19.84  ? 125 SER   A CA  1 
ATOM   937  C  C   . SER   A 1 119 ? 11.499 10.898  18.388 1.00 21.15  ? 125 SER   A C   1 
ATOM   938  O  O   . SER   A 1 119 ? 11.789 12.000  18.864 1.00 23.24  ? 125 SER   A O   1 
ATOM   939  C  CB  . SER   A 1 119 ? 12.527 10.614  16.106 1.00 21.59  ? 125 SER   A CB  1 
ATOM   940  O  OG  . SER   A 1 119 ? 12.682 12.029  15.974 1.00 22.67  ? 125 SER   A OG  1 
ATOM   941  N  N   . THR   A 1 120 ? 10.252 10.347  18.511 1.00 20.57  ? 126 THR   A N   1 
ATOM   942  C  CA  . THR   A 1 120 ? 9.169  11.028  19.275 1.00 22.04  ? 126 THR   A CA  1 
ATOM   943  C  C   . THR   A 1 120 ? 8.383  10.004  20.122 1.00 24.32  ? 126 THR   A C   1 
ATOM   944  O  O   . THR   A 1 120 ? 8.570  8.788   19.976 1.00 23.73  ? 126 THR   A O   1 
ATOM   945  C  CB  . THR   A 1 120 ? 8.191  11.798  18.285 1.00 23.60  ? 126 THR   A CB  1 
ATOM   946  O  OG1 . THR   A 1 120 ? 7.277  10.849  17.703 1.00 24.73  ? 126 THR   A OG1 1 
ATOM   947  C  CG2 . THR   A 1 120 ? 8.916  12.560  17.168 1.00 22.94  ? 126 THR   A CG2 1 
ATOM   948  N  N   . GLY   A 1 121 ? 7.476  10.494  20.980 1.00 25.12  ? 127 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 121 ? 6.617  9.597   21.726 1.00 26.96  ? 127 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 121 ? 5.851  10.292  22.823 1.00 29.16  ? 127 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 121 ? 5.797  11.529  22.896 1.00 29.28  ? 127 GLY   A O   1 
ATOM   952  N  N   . GLY   A 1 122 ? 5.283  9.459   23.676 1.00 31.81  ? 128 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 122 ? 4.477  9.906   24.805 1.00 33.17  ? 128 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 122 ? 3.049  9.429   24.663 1.00 33.79  ? 128 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 122 ? 2.580  9.161   23.557 1.00 32.81  ? 128 GLY   A O   1 
ATOM   956  N  N   . ASN   A 1 123 ? 2.355  9.299   25.793 1.00 35.13  ? 129 ASN   A N   1 
ATOM   957  C  CA  . ASN   A 1 123 ? 0.957  8.894   25.817 1.00 36.63  ? 129 ASN   A CA  1 
ATOM   958  C  C   . ASN   A 1 123 ? 0.643  7.581   25.101 1.00 35.24  ? 129 ASN   A C   1 
ATOM   959  O  O   . ASN   A 1 123 ? -0.411 7.449   24.455 1.00 35.99  ? 129 ASN   A O   1 
ATOM   960  C  CB  . ASN   A 1 123 ? 0.081  10.013  25.296 1.00 40.53  ? 129 ASN   A CB  1 
ATOM   961  C  CG  . ASN   A 1 123 ? 0.038  11.188  26.231 1.00 48.59  ? 129 ASN   A CG  1 
ATOM   962  O  OD1 . ASN   A 1 123 ? 0.396  11.103  27.422 1.00 51.21  ? 129 ASN   A OD1 1 
ATOM   963  N  ND2 . ASN   A 1 123 ? -0.418 12.309  25.712 1.00 51.48  ? 129 ASN   A ND2 1 
ATOM   964  N  N   . GLY   A 1 124 ? 1.522  6.600   25.271 1.00 32.04  ? 130 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 124 ? 1.296  5.292   24.689 1.00 30.13  ? 130 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 124 ? 1.664  5.162   23.219 1.00 26.93  ? 130 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 124 ? 1.414  4.107   22.622 1.00 25.29  ? 130 GLY   A O   1 
ATOM   968  N  N   . LEU   A 1 125 ? 2.277  6.207   22.636 1.00 25.65  ? 131 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 125 ? 2.741  6.168   21.239 1.00 24.70  ? 131 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 125 ? 4.289  6.219   21.169 1.00 25.03  ? 131 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 125 ? 4.958  6.595   22.135 1.00 26.02  ? 131 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 125 ? 2.181  7.361   20.425 1.00 26.17  ? 131 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 125 ? 0.647  7.444   20.456 1.00 29.84  ? 131 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 125 ? 0.163  8.841   20.057 1.00 32.21  ? 131 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 125 ? 0.013  6.342   19.655 1.00 30.24  ? 131 LEU   A CD2 1 
ATOM   976  N  N   . VAL   A 1 126 ? 4.816  5.799   20.034 1.00 23.02  ? 132 VAL   A N   1 
ATOM   977  C  CA  . VAL   A 1 126 ? 6.237  5.902   19.781 1.00 22.33  ? 132 VAL   A CA  1 
ATOM   978  C  C   . VAL   A 1 126 ? 6.390  6.274   18.296 1.00 22.28  ? 132 VAL   A C   1 
ATOM   979  O  O   . VAL   A 1 126 ? 5.637  5.773   17.473 1.00 22.75  ? 132 VAL   A O   1 
ATOM   980  C  CB  . VAL   A 1 126 ? 7.036  4.625   20.186 1.00 22.88  ? 132 VAL   A CB  1 
ATOM   981  C  CG1 . VAL   A 1 126 ? 6.471  3.364   19.529 1.00 24.19  ? 132 VAL   A CG1 1 
ATOM   982  C  CG2 . VAL   A 1 126 ? 8.529  4.783   19.847 1.00 22.07  ? 132 VAL   A CG2 1 
ATOM   983  N  N   . GLY   A 1 127 ? 7.235  7.247   18.013 1.00 21.47  ? 133 GLY   A N   1 
ATOM   984  C  CA  . GLY   A 1 127 ? 7.424  7.706   16.647 1.00 21.12  ? 133 GLY   A CA  1 
ATOM   985  C  C   . GLY   A 1 127 ? 8.847  7.469   16.197 1.00 21.33  ? 133 GLY   A C   1 
ATOM   986  O  O   . GLY   A 1 127 ? 9.774  7.607   17.000 1.00 21.61  ? 133 GLY   A O   1 
ATOM   987  N  N   . PHE   A 1 128 ? 9.017  7.082   14.925 1.00 20.70  ? 134 PHE   A N   1 
ATOM   988  C  CA  . PHE   A 1 128 ? 10.354 6.726   14.396 1.00 21.45  ? 134 PHE   A CA  1 
ATOM   989  C  C   . PHE   A 1 128 ? 10.642 7.590   13.195 1.00 20.86  ? 134 PHE   A C   1 
ATOM   990  O  O   . PHE   A 1 128 ? 9.769  7.742   12.338 1.00 20.82  ? 134 PHE   A O   1 
ATOM   991  C  CB  . PHE   A 1 128 ? 10.328 5.250   13.893 1.00 21.31  ? 134 PHE   A CB  1 
ATOM   992  C  CG  . PHE   A 1 128 ? 9.818  4.271   14.937 1.00 21.33  ? 134 PHE   A CG  1 
ATOM   993  C  CD1 . PHE   A 1 128 ? 10.677 3.733   15.888 1.00 21.17  ? 134 PHE   A CD1 1 
ATOM   994  C  CD2 . PHE   A 1 128 ? 8.479  3.896   14.970 1.00 22.03  ? 134 PHE   A CD2 1 
ATOM   995  C  CE1 . PHE   A 1 128 ? 10.209 2.839   16.845 1.00 21.05  ? 134 PHE   A CE1 1 
ATOM   996  C  CE2 . PHE   A 1 128 ? 8.025  2.961   15.888 1.00 21.65  ? 134 PHE   A CE2 1 
ATOM   997  C  CZ  . PHE   A 1 128 ? 8.878  2.460   16.846 1.00 21.16  ? 134 PHE   A CZ  1 
ATOM   998  N  N   . ALA   A 1 129 ? 11.884 8.106   13.115 1.00 21.04  ? 135 ALA   A N   1 
ATOM   999  C  CA  . ALA   A 1 129 ? 12.331 8.882   11.976 1.00 21.88  ? 135 ALA   A CA  1 
ATOM   1000 C  C   . ALA   A 1 129 ? 12.751 7.881   10.887 1.00 21.07  ? 135 ALA   A C   1 
ATOM   1001 O  O   . ALA   A 1 129 ? 13.653 7.057   11.107 1.00 20.78  ? 135 ALA   A O   1 
ATOM   1002 C  CB  . ALA   A 1 129 ? 13.507 9.777   12.393 1.00 21.53  ? 135 ALA   A CB  1 
ATOM   1003 N  N   . ASP   A 1 130 ? 12.076 7.921   9.718  1.00 22.33  ? 136 ASP   A N   1 
ATOM   1004 C  CA  . ASP   A 1 130 ? 12.404 6.996   8.620  1.00 23.56  ? 136 ASP   A CA  1 
ATOM   1005 C  C   . ASP   A 1 130 ? 13.753 7.286   8.010  1.00 22.53  ? 136 ASP   A C   1 
ATOM   1006 O  O   . ASP   A 1 130 ? 14.117 8.466   7.901  1.00 22.46  ? 136 ASP   A O   1 
ATOM   1007 C  CB  . ASP   A 1 130 ? 11.361 7.100   7.491  1.00 24.32  ? 136 ASP   A CB  1 
ATOM   1008 C  CG  . ASP   A 1 130 ? 11.535 6.048   6.416  1.00 27.18  ? 136 ASP   A CG  1 
ATOM   1009 O  OD1 . ASP   A 1 130 ? 11.610 4.853   6.755  1.00 27.89  ? 136 ASP   A OD1 1 
ATOM   1010 O  OD2 . ASP   A 1 130 ? 11.604 6.416   5.232  1.00 30.77  ? 136 ASP   A OD2 1 
ATOM   1011 N  N   . VAL   A 1 131 ? 14.506 6.223   7.612  1.00 21.91  ? 137 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? 15.795 6.416   6.891  1.00 23.52  ? 137 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? 15.815 5.692   5.494  1.00 24.94  ? 137 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? 16.787 5.814   4.739  1.00 26.63  ? 137 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? 17.072 6.039   7.705  1.00 24.32  ? 137 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? 17.158 6.847   9.001  1.00 24.44  ? 137 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? 17.144 4.533   7.965  1.00 23.94  ? 137 VAL   A CG2 1 
ATOM   1018 N  N   . ARG   A 1 132 ? 14.770 4.897   5.189  1.00 24.36  ? 138 ARG   A N   1 
ATOM   1019 C  CA  . ARG   A 1 132 ? 14.690 4.085   3.987  1.00 24.30  ? 138 ARG   A CA  1 
ATOM   1020 C  C   . ARG   A 1 132 ? 14.703 4.858   2.694  1.00 26.93  ? 138 ARG   A C   1 
ATOM   1021 O  O   . ARG   A 1 132 ? 15.103 4.283   1.697  1.00 29.41  ? 138 ARG   A O   1 
ATOM   1022 C  CB  . ARG   A 1 132 ? 13.472 3.149   4.024  1.00 22.63  ? 138 ARG   A CB  1 
ATOM   1023 C  CG  . ARG   A 1 132 ? 13.489 2.206   5.217  1.00 23.08  ? 138 ARG   A CG  1 
ATOM   1024 C  CD  . ARG   A 1 132 ? 12.177 1.399   5.177  1.00 23.37  ? 138 ARG   A CD  1 
ATOM   1025 N  NE  . ARG   A 1 132 ? 11.051 2.256   5.555  1.00 23.70  ? 138 ARG   A NE  1 
ATOM   1026 C  CZ  . ARG   A 1 132 ? 9.804  1.826   5.750  1.00 24.81  ? 138 ARG   A CZ  1 
ATOM   1027 N  NH1 . ARG   A 1 132 ? 9.479  0.563   5.486  1.00 25.55  ? 138 ARG   A NH1 1 
ATOM   1028 N  NH2 . ARG   A 1 132 ? 8.868  2.663   6.190  1.00 25.74  ? 138 ARG   A NH2 1 
ATOM   1029 N  N   . ASP   A 1 133 ? 14.313 6.146   2.696  1.00 26.88  ? 139 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 133 ? 14.371 6.939   1.456  1.00 27.52  ? 139 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 133 ? 15.798 7.518   1.182  1.00 28.53  ? 139 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 133 ? 16.053 8.059   0.096  1.00 30.59  ? 139 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 133 ? 13.347 8.077   1.542  1.00 27.91  ? 139 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 133 ? 13.740 9.117   2.576  1.00 31.08  ? 139 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 133 ? 14.072 8.715   3.737  1.00 29.19  ? 139 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 133 ? 13.735 10.329  2.232  1.00 31.43  ? 139 ASP   A OD2 1 
ATOM   1037 N  N   . LEU   A 1 134 ? 16.715 7.441   2.163  1.00 27.31  ? 140 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 134 ? 18.081 8.000   2.022  1.00 27.58  ? 140 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 134 ? 18.970 7.019   1.263  1.00 29.30  ? 140 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 134 ? 19.785 6.306   1.845  1.00 29.66  ? 140 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 134 ? 18.638 8.327   3.417  1.00 26.98  ? 140 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 134 ? 17.784 9.328   4.203  1.00 27.62  ? 140 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 134 ? 18.277 9.474   5.639  1.00 27.35  ? 140 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 134 ? 17.706 10.677  3.512  1.00 28.68  ? 140 LEU   A CD2 1 
ATOM   1045 N  N   . LEU   A 1 135 ? 18.766 6.951   -0.070 1.00 29.99  ? 141 LEU   A N   1 
ATOM   1046 C  CA  . LEU   A 1 135 ? 19.440 5.953   -0.894 1.00 32.14  ? 141 LEU   A CA  1 
ATOM   1047 C  C   . LEU   A 1 135 ? 20.934 6.040   -0.884 1.00 33.82  ? 141 LEU   A C   1 
ATOM   1048 O  O   . LEU   A 1 135 ? 21.623 5.019   -1.010 1.00 34.76  ? 141 LEU   A O   1 
ATOM   1049 C  CB  . LEU   A 1 135 ? 18.926 6.011   -2.336 1.00 32.62  ? 141 LEU   A CB  1 
ATOM   1050 C  CG  . LEU   A 1 135 ? 17.425 5.802   -2.520 1.00 34.78  ? 141 LEU   A CG  1 
ATOM   1051 C  CD1 . LEU   A 1 135 ? 17.098 5.619   -4.017 1.00 37.37  ? 141 LEU   A CD1 1 
ATOM   1052 C  CD2 . LEU   A 1 135 ? 16.905 4.572   -1.770 1.00 34.75  ? 141 LEU   A CD2 1 
ATOM   1053 N  N   . TRP   A 1 136 ? 21.438 7.276   -0.804 1.00 33.42  ? 142 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A 1 136 ? 22.864 7.530   -0.799 1.00 34.17  ? 142 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A 1 136 ? 23.569 6.901   0.394  1.00 35.70  ? 142 TRP   A C   1 
ATOM   1056 O  O   . TRP   A 1 136 ? 24.775 6.745   0.336  1.00 36.48  ? 142 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A 1 136 ? 23.138 9.044   -0.879 1.00 33.77  ? 142 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A 1 136 ? 22.410 9.832   0.168  1.00 32.70  ? 142 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A 1 136 ? 21.195 10.448  0.046  1.00 32.70  ? 142 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A 1 136 ? 22.875 10.115  1.498  1.00 32.52  ? 142 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A 1 136 ? 20.892 11.124  1.209  1.00 32.69  ? 142 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A 1 136 ? 21.908 10.936  2.114  1.00 32.44  ? 142 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A 1 136 ? 24.048 9.804   2.206  1.00 33.34  ? 142 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A 1 136 ? 22.050 11.395  3.425  1.00 32.89  ? 142 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A 1 136 ? 24.198 10.287  3.493  1.00 33.91  ? 142 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A 1 136 ? 23.197 11.049  4.097  1.00 33.48  ? 142 TRP   A CH2 1 
ATOM   1067 N  N   . LEU   A 1 137 ? 22.840 6.508   1.474  1.00 36.03  ? 143 LEU   A N   1 
ATOM   1068 C  CA  . LEU   A 1 137 ? 23.476 5.829   2.605  1.00 37.77  ? 143 LEU   A CA  1 
ATOM   1069 C  C   . LEU   A 1 137 ? 24.157 4.519   2.165  1.00 42.12  ? 143 LEU   A C   1 
ATOM   1070 O  O   . LEU   A 1 137 ? 25.088 4.088   2.835  1.00 42.90  ? 143 LEU   A O   1 
ATOM   1071 C  CB  . LEU   A 1 137 ? 22.453 5.500   3.706  1.00 35.94  ? 143 LEU   A CB  1 
ATOM   1072 C  CG  . LEU   A 1 137 ? 21.966 6.689   4.521  1.00 35.00  ? 143 LEU   A CG  1 
ATOM   1073 C  CD1 . LEU   A 1 137 ? 20.825 6.266   5.467  1.00 34.53  ? 143 LEU   A CD1 1 
ATOM   1074 C  CD2 . LEU   A 1 137 ? 23.087 7.295   5.318  1.00 35.12  ? 143 LEU   A CD2 1 
ATOM   1075 N  N   . ASP   A 1 138 ? 23.674 3.886   1.066  1.00 45.13  ? 144 ASP   A N   1 
ATOM   1076 C  CA  . ASP   A 1 138 ? 24.195 2.623   0.508  1.00 48.74  ? 144 ASP   A CA  1 
ATOM   1077 C  C   . ASP   A 1 138 ? 25.337 2.802   -0.476 1.00 52.33  ? 144 ASP   A C   1 
ATOM   1078 O  O   . ASP   A 1 138 ? 25.750 1.804   -1.067 1.00 52.34  ? 144 ASP   A O   1 
ATOM   1079 C  CB  . ASP   A 1 138 ? 23.112 1.884   -0.293 1.00 50.37  ? 144 ASP   A CB  1 
ATOM   1080 C  CG  . ASP   A 1 138 ? 21.882 1.498   0.458  1.00 56.59  ? 144 ASP   A CG  1 
ATOM   1081 O  OD1 . ASP   A 1 138 ? 21.913 1.542   1.706  1.00 57.76  ? 144 ASP   A OD1 1 
ATOM   1082 O  OD2 . ASP   A 1 138 ? 20.872 1.152   -0.203 1.00 59.71  ? 144 ASP   A OD2 1 
ATOM   1083 N  N   . GLU   A 1 139 ? 25.779 4.042   -0.746 1.00 54.95  ? 145 GLU   A N   1 
ATOM   1084 C  CA  . GLU   A 1 139 ? 26.853 4.258   -1.710 1.00 58.50  ? 145 GLU   A CA  1 
ATOM   1085 C  C   . GLU   A 1 139 ? 27.754 5.439   -1.349 1.00 60.83  ? 145 GLU   A C   1 
ATOM   1086 O  O   . GLU   A 1 139 ? 27.301 6.389   -0.702 1.00 61.12  ? 145 GLU   A O   1 
ATOM   1087 C  CB  . GLU   A 1 139 ? 26.281 4.416   -3.130 1.00 62.39  ? 145 GLU   A CB  1 
ATOM   1088 C  CG  . GLU   A 1 139 ? 25.334 5.592   -3.294 1.00 69.21  ? 145 GLU   A CG  1 
ATOM   1089 C  CD  . GLU   A 1 139 ? 24.304 5.379   -4.385 1.00 78.37  ? 145 GLU   A CD  1 
ATOM   1090 O  OE1 . GLU   A 1 139 ? 24.149 6.275   -5.249 1.00 79.46  ? 145 GLU   A OE1 1 
ATOM   1091 O  OE2 . GLU   A 1 139 ? 23.660 4.303   -4.381 1.00 81.39  ? 145 GLU   A OE2 1 
ATOM   1092 N  N   . GLU   A 1 140 ? 29.029 5.378   -1.783 1.00 62.41  ? 146 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 140 ? 30.055 6.412   -1.560 1.00 64.58  ? 146 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 140 ? 30.128 6.868   -0.074 1.00 65.85  ? 146 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 140 ? 31.092 7.505   0.359  1.00 66.45  ? 146 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 140 ? 29.874 7.592   -2.553 1.00 67.60  ? 146 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 140 ? 29.237 8.866   -2.017 1.00 74.19  ? 146 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 140 ? 30.217 10.017  -1.901 1.00 82.22  ? 146 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 140 ? 30.047 10.855  -0.985 1.00 83.98  ? 146 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 140 ? 31.165 10.072  -2.719 1.00 84.29  ? 146 GLU   A OE2 1 
HETATM 1101 N  N1  . A1BOM B 2 .   ? 11.980 14.595  17.419 1.00 24.86  ? 201 A1BOM A N1  1 
HETATM 1102 C  C4  . A1BOM B 2 .   ? 7.783  11.816  25.932 1.00 29.70  ? 201 A1BOM A C4  1 
HETATM 1103 C  C5  . A1BOM B 2 .   ? 8.262  12.811  25.091 1.00 29.57  ? 201 A1BOM A C5  1 
HETATM 1104 C  C6  . A1BOM B 2 .   ? 9.080  12.501  24.004 1.00 29.30  ? 201 A1BOM A C6  1 
HETATM 1105 C  C7  . A1BOM B 2 .   ? 9.482  13.557  22.997 1.00 29.58  ? 201 A1BOM A C7  1 
HETATM 1106 C  C8  . A1BOM B 2 .   ? 10.892 14.095  23.187 1.00 29.58  ? 201 A1BOM A C8  1 
HETATM 1107 C  C10 . A1BOM B 2 .   ? 12.944 15.805  20.695 1.00 28.36  ? 201 A1BOM A C10 1 
HETATM 1108 C  C13 . A1BOM B 2 .   ? 10.936 14.516  20.729 1.00 27.59  ? 201 A1BOM A C13 1 
HETATM 1109 O  O2  . A1BOM B 2 .   ? 11.009 16.407  18.335 1.00 25.39  ? 201 A1BOM A O2  1 
HETATM 1110 C  C12 . A1BOM B 2 .   ? 11.671 15.365  18.449 1.00 25.98  ? 201 A1BOM A C12 1 
HETATM 1111 C  C11 . A1BOM B 2 .   ? 12.116 14.854  19.810 1.00 27.60  ? 201 A1BOM A C11 1 
HETATM 1112 C  C9  . A1BOM B 2 .   ? 12.870 15.141  22.070 1.00 27.77  ? 201 A1BOM A C9  1 
HETATM 1113 N  N   . A1BOM B 2 .   ? 11.527 14.532  22.075 1.00 27.54  ? 201 A1BOM A N   1 
HETATM 1114 O  O1  . A1BOM B 2 .   ? 11.379 14.220  24.304 1.00 31.13  ? 201 A1BOM A O1  1 
HETATM 1115 C  C1  . A1BOM B 2 .   ? 9.427  11.164  23.800 1.00 28.81  ? 201 A1BOM A C1  1 
HETATM 1116 O  O   . A1BOM B 2 .   ? 10.250 10.939  22.727 1.00 27.51  ? 201 A1BOM A O   1 
HETATM 1117 C  C   . A1BOM B 2 .   ? 10.753 9.609   22.538 1.00 26.63  ? 201 A1BOM A C   1 
HETATM 1118 C  C3  . A1BOM B 2 .   ? 8.114  10.498  25.701 1.00 29.08  ? 201 A1BOM A C3  1 
HETATM 1119 C  C2  . A1BOM B 2 .   ? 8.933  10.164  24.631 1.00 28.93  ? 201 A1BOM A C2  1 
HETATM 1120 ZN ZN  . ZN    C 3 .   ? 11.129 -4.215  5.137  1.00 28.45  2 202 ZN    A ZN  1 
HETATM 1121 S  S   . DMS   D 4 .   ? 15.181 21.394  7.033  1.00 93.92  ? 203 DMS   A S   1 
HETATM 1122 O  O   . DMS   D 4 .   ? 14.354 21.879  8.196  1.00 93.78  ? 203 DMS   A O   1 
HETATM 1123 C  C1  . DMS   D 4 .   ? 14.101 21.246  5.579  1.00 93.88  ? 203 DMS   A C1  1 
HETATM 1124 C  C2  . DMS   D 4 .   ? 16.156 22.794  6.402  1.00 93.91  ? 203 DMS   A C2  1 
HETATM 1125 S  S   . DMS   E 4 .   ? 1.127  -1.602  23.800 1.00 108.91 ? 204 DMS   A S   1 
HETATM 1126 O  O   . DMS   E 4 .   ? 1.384  -0.263  24.429 1.00 108.95 ? 204 DMS   A O   1 
HETATM 1127 C  C1  . DMS   E 4 .   ? 1.428  -2.860  25.072 1.00 108.91 ? 204 DMS   A C1  1 
HETATM 1128 C  C2  . DMS   E 4 .   ? -0.671 -1.852  23.716 1.00 108.91 ? 204 DMS   A C2  1 
HETATM 1129 S  S   . DMS   F 4 .   ? 20.026 0.524   19.341 1.00 50.18  ? 205 DMS   A S   1 
HETATM 1130 O  O   . DMS   F 4 .   ? 18.686 0.045   18.880 1.00 47.91  ? 205 DMS   A O   1 
HETATM 1131 C  C1  . DMS   F 4 .   ? 19.899 1.294   20.968 1.00 49.86  ? 205 DMS   A C1  1 
HETATM 1132 C  C2  . DMS   F 4 .   ? 20.731 1.897   18.363 1.00 49.43  ? 205 DMS   A C2  1 
HETATM 1133 O  O   . HOH   G 5 .   ? 0.693  2.074   24.282 1.00 32.17  ? 301 HOH   A O   1 
HETATM 1134 O  O   . HOH   G 5 .   ? 13.338 7.403   30.707 1.00 37.08  ? 302 HOH   A O   1 
HETATM 1135 O  O   . HOH   G 5 .   ? 17.957 -6.050  2.862  1.00 45.13  ? 303 HOH   A O   1 
HETATM 1136 O  O   . HOH   G 5 .   ? 3.603  21.792  22.773 1.00 40.00  ? 304 HOH   A O   1 
HETATM 1137 O  O   . HOH   G 5 .   ? -1.143 12.841  23.316 1.00 60.77  ? 305 HOH   A O   1 
HETATM 1138 O  O   . HOH   G 5 .   ? 4.567  -4.718  21.026 1.00 34.96  ? 306 HOH   A O   1 
HETATM 1139 O  O   . HOH   G 5 .   ? 6.366  2.789   3.316  1.00 36.62  ? 307 HOH   A O   1 
HETATM 1140 O  O   . HOH   G 5 .   ? 8.274  -3.567  0.152  1.00 34.56  ? 308 HOH   A O   1 
HETATM 1141 O  O   . HOH   G 5 .   ? 30.978 10.421  12.892 1.00 49.77  ? 309 HOH   A O   1 
HETATM 1142 O  O   . HOH   G 5 .   ? 15.786 23.668  18.442 1.00 45.29  ? 310 HOH   A O   1 
HETATM 1143 O  O   . HOH   G 5 .   ? 9.045  2.941   2.471  1.00 33.28  ? 311 HOH   A O   1 
HETATM 1144 O  O   . HOH   G 5 .   ? 22.069 -4.365  11.883 1.00 54.30  ? 312 HOH   A O   1 
HETATM 1145 O  O   . HOH   G 5 .   ? 16.606 -6.828  10.084 1.00 49.41  ? 313 HOH   A O   1 
HETATM 1146 O  O   . HOH   G 5 .   ? 15.274 11.631  0.517  1.00 42.80  ? 314 HOH   A O   1 
HETATM 1147 O  O   . HOH   G 5 .   ? 27.692 3.636   2.676  1.00 47.58  ? 315 HOH   A O   1 
HETATM 1148 O  O   . HOH   G 5 .   ? 26.633 4.375   19.162 1.00 55.74  ? 316 HOH   A O   1 
HETATM 1149 O  O   . HOH   G 5 .   ? 10.445 5.219   3.169  1.00 28.83  ? 317 HOH   A O   1 
HETATM 1150 O  O   . HOH   G 5 .   ? 8.539  19.710  18.309 1.00 27.30  ? 318 HOH   A O   1 
HETATM 1151 O  O   . HOH   G 5 .   ? 2.997  8.536   9.819  1.00 40.38  ? 319 HOH   A O   1 
HETATM 1152 O  O   . HOH   G 5 .   ? 20.583 9.289   18.460 1.00 25.71  ? 320 HOH   A O   1 
HETATM 1153 O  O   . HOH   G 5 .   ? 22.300 -2.427  14.716 1.00 38.29  ? 321 HOH   A O   1 
HETATM 1154 O  O   . HOH   G 5 .   ? 29.482 3.431   9.834  1.00 34.42  ? 322 HOH   A O   1 
HETATM 1155 O  O   . HOH   G 5 .   ? 12.605 21.720  12.872 1.00 30.45  ? 323 HOH   A O   1 
HETATM 1156 O  O   . HOH   G 5 .   ? 5.354  20.061  25.710 1.00 38.30  ? 324 HOH   A O   1 
HETATM 1157 O  O   . HOH   G 5 .   ? 18.586 19.936  5.210  1.00 43.37  ? 325 HOH   A O   1 
HETATM 1158 O  O   . HOH   G 5 .   ? 18.734 -2.476  17.937 1.00 31.97  ? 326 HOH   A O   1 
HETATM 1159 O  O   . HOH   G 5 .   ? 19.980 -0.848  30.515 1.00 50.77  ? 327 HOH   A O   1 
HETATM 1160 O  O   . HOH   G 5 .   ? 8.754  -8.439  23.101 1.00 29.22  ? 328 HOH   A O   1 
HETATM 1161 O  O   . HOH   G 5 .   ? 7.088  -5.108  28.674 1.00 37.20  ? 329 HOH   A O   1 
HETATM 1162 O  O   . HOH   G 5 .   ? 22.507 -0.457  3.415  1.00 40.52  ? 330 HOH   A O   1 
HETATM 1163 O  O   . HOH   G 5 .   ? 16.174 -2.885  16.961 1.00 35.03  ? 331 HOH   A O   1 
HETATM 1164 O  O   . HOH   G 5 .   ? 10.574 8.706   4.245  1.00 34.26  ? 332 HOH   A O   1 
HETATM 1165 O  O   . HOH   G 5 .   ? 14.267 15.705  27.558 1.00 41.70  ? 333 HOH   A O   1 
HETATM 1166 O  O   . HOH   G 5 .   ? 10.141 18.259  20.303 1.00 25.95  ? 334 HOH   A O   1 
HETATM 1167 O  O   . HOH   G 5 .   ? 24.325 22.694  8.796  1.00 30.68  ? 335 HOH   A O   1 
HETATM 1168 O  O   . HOH   G 5 .   ? 11.245 -4.530  31.279 1.00 45.26  ? 336 HOH   A O   1 
HETATM 1169 O  O   . HOH   G 5 .   ? 1.161  -2.099  19.766 1.00 33.20  ? 337 HOH   A O   1 
HETATM 1170 O  O   . HOH   G 5 .   ? 18.742 5.071   26.140 1.00 44.45  ? 338 HOH   A O   1 
HETATM 1171 O  O   . HOH   G 5 .   ? 23.632 0.286   15.220 1.00 30.95  ? 339 HOH   A O   1 
HETATM 1172 O  O   . HOH   G 5 .   ? 24.753 16.123  21.992 1.00 55.64  ? 340 HOH   A O   1 
HETATM 1173 O  O   . HOH   G 5 .   ? 1.090  8.013   5.331  1.00 70.18  ? 341 HOH   A O   1 
HETATM 1174 O  O   . HOH   G 5 .   ? 19.770 0.047   26.859 1.00 37.39  ? 342 HOH   A O   1 
HETATM 1175 O  O   . HOH   G 5 .   ? 17.568 20.681  18.861 1.00 37.20  ? 343 HOH   A O   1 
HETATM 1176 O  O   . HOH   G 5 .   ? 15.056 -4.829  17.798 1.00 41.95  ? 344 HOH   A O   1 
HETATM 1177 O  O   . HOH   G 5 .   ? 31.210 18.794  6.858  1.00 42.75  ? 345 HOH   A O   1 
HETATM 1178 O  O   . HOH   G 5 .   ? 19.321 -4.364  26.550 1.00 56.86  ? 346 HOH   A O   1 
HETATM 1179 O  O   . HOH   G 5 .   ? 11.004 18.009  5.402  1.00 52.11  ? 347 HOH   A O   1 
HETATM 1180 O  O   . HOH   G 5 .   ? 0.841  0.094   16.490 1.00 21.91  ? 348 HOH   A O   1 
HETATM 1181 O  O   . HOH   G 5 .   ? 15.264 23.987  26.234 1.00 46.57  ? 349 HOH   A O   1 
HETATM 1182 O  O   . HOH   G 5 .   ? 7.608  4.218   32.608 1.00 40.13  ? 350 HOH   A O   1 
HETATM 1183 O  O   . HOH   G 5 .   ? 18.255 2.938   22.727 1.00 28.33  ? 351 HOH   A O   1 
HETATM 1184 O  O   . HOH   G 5 .   ? 10.051 15.632  26.282 1.00 35.60  ? 352 HOH   A O   1 
HETATM 1185 O  O   . HOH   G 5 .   ? 11.971 11.116  0.246  1.00 62.38  ? 353 HOH   A O   1 
HETATM 1186 O  O   . HOH   G 5 .   ? 10.331 24.127  24.400 1.00 44.64  ? 354 HOH   A O   1 
HETATM 1187 O  O   . HOH   G 5 .   ? 7.457  16.170  21.926 1.00 32.59  ? 355 HOH   A O   1 
HETATM 1188 O  O   . HOH   G 5 .   ? 5.094  26.327  17.979 1.00 50.58  ? 356 HOH   A O   1 
HETATM 1189 O  O   . HOH   G 5 .   ? 24.169 17.657  2.745  1.00 49.17  ? 357 HOH   A O   1 
HETATM 1190 O  O   . HOH   G 5 .   ? 6.121  2.058   5.913  1.00 29.62  ? 358 HOH   A O   1 
HETATM 1191 O  O   . HOH   G 5 .   ? 15.408 2.875   22.789 1.00 23.73  ? 359 HOH   A O   1 
HETATM 1192 O  O   . HOH   G 5 .   ? 13.334 2.581   0.366  1.00 31.59  ? 360 HOH   A O   1 
HETATM 1193 O  O   . HOH   G 5 .   ? 11.564 12.081  11.112 1.00 21.68  ? 361 HOH   A O   1 
HETATM 1194 O  O   . HOH   G 5 .   ? 7.758  25.649  15.125 1.00 50.17  ? 362 HOH   A O   1 
HETATM 1195 O  O   . HOH   G 5 .   ? 3.519  3.790   27.412 1.00 36.29  ? 363 HOH   A O   1 
HETATM 1196 O  O   . HOH   G 5 .   ? 18.370 19.231  16.644 1.00 27.55  ? 364 HOH   A O   1 
HETATM 1197 O  O   . HOH   G 5 .   ? 15.843 12.653  23.713 1.00 28.36  ? 365 HOH   A O   1 
HETATM 1198 O  O   . HOH   G 5 .   ? 24.940 10.910  20.752 1.00 54.29  ? 366 HOH   A O   1 
HETATM 1199 O  O   . HOH   G 5 .   ? 18.054 21.556  9.142  1.00 29.45  ? 367 HOH   A O   1 
HETATM 1200 O  O   . HOH   G 5 .   ? 16.642 17.432  3.587  1.00 48.64  ? 368 HOH   A O   1 
HETATM 1201 O  O   . HOH   G 5 .   ? 18.394 0.872   29.640 1.00 42.14  ? 369 HOH   A O   1 
HETATM 1202 O  O   . HOH   G 5 .   ? 33.935 -3.117  9.885  1.00 42.64  ? 370 HOH   A O   1 
HETATM 1203 O  O   . HOH   G 5 .   ? 8.294  20.831  8.960  1.00 44.42  ? 371 HOH   A O   1 
HETATM 1204 O  O   . HOH   G 5 .   ? 10.066 9.199   31.602 1.00 39.26  ? 372 HOH   A O   1 
HETATM 1205 O  O   . HOH   G 5 .   ? -0.314 16.383  9.187  1.00 54.33  ? 373 HOH   A O   1 
HETATM 1206 O  O   . HOH   G 5 .   ? 6.557  13.651  21.162 1.00 26.84  ? 374 HOH   A O   1 
HETATM 1207 O  O   . HOH   G 5 .   ? 6.418  8.178   28.483 1.00 33.35  ? 375 HOH   A O   1 
HETATM 1208 O  O   . HOH   G 5 .   ? 30.775 11.208  17.964 1.00 50.05  ? 376 HOH   A O   1 
HETATM 1209 O  O   . HOH   G 5 .   ? 21.657 21.531  6.091  1.00 42.17  ? 377 HOH   A O   1 
HETATM 1210 O  O   . HOH   G 5 .   ? 14.275 9.584   29.421 1.00 32.48  ? 378 HOH   A O   1 
HETATM 1211 O  O   . HOH   G 5 .   ? 4.541  13.498  24.543 1.00 39.39  ? 379 HOH   A O   1 
HETATM 1212 O  O   . HOH   G 5 .   ? 4.723  6.371   24.985 1.00 34.16  ? 380 HOH   A O   1 
HETATM 1213 O  O   . HOH   G 5 .   ? 0.317  4.130   6.538  1.00 35.82  ? 381 HOH   A O   1 
HETATM 1214 O  O   . HOH   G 5 .   ? 3.205  13.537  17.876 1.00 40.53  ? 382 HOH   A O   1 
HETATM 1215 O  O   . HOH   G 5 .   ? 31.833 2.749   2.441  1.00 52.92  ? 383 HOH   A O   1 
HETATM 1216 O  O   . HOH   G 5 .   ? 18.110 23.194  16.293 1.00 52.44  ? 384 HOH   A O   1 
HETATM 1217 O  O   . HOH   G 5 .   ? 6.696  -7.491  14.058 1.00 41.17  ? 385 HOH   A O   1 
HETATM 1218 O  O   . HOH   G 5 .   ? 13.322 11.001  9.009  1.00 22.75  ? 386 HOH   A O   1 
HETATM 1219 O  O   . HOH   G 5 .   ? 14.618 14.975  3.287  1.00 36.28  ? 387 HOH   A O   1 
HETATM 1220 O  O   . HOH   G 5 .   ? 5.732  -1.117  23.918 1.00 27.31  ? 388 HOH   A O   1 
HETATM 1221 O  O   . HOH   G 5 .   ? 21.009 23.699  10.528 1.00 42.61  ? 389 HOH   A O   1 
HETATM 1222 O  O   . HOH   G 5 .   ? 6.728  13.354  5.400  1.00 31.94  ? 390 HOH   A O   1 
HETATM 1223 O  O   . HOH   G 5 .   ? 19.526 9.536   25.209 1.00 31.80  ? 391 HOH   A O   1 
HETATM 1224 O  O   . HOH   G 5 .   ? 7.737  16.740  24.858 1.00 40.29  ? 392 HOH   A O   1 
HETATM 1225 O  O   . HOH   G 5 .   ? 27.904 16.254  2.095  1.00 60.18  ? 393 HOH   A O   1 
HETATM 1226 O  O   . HOH   G 5 .   ? 5.313  0.978   -2.410 1.00 50.07  ? 394 HOH   A O   1 
HETATM 1227 O  O   . HOH   G 5 .   ? 28.299 -1.634  12.972 1.00 42.83  ? 395 HOH   A O   1 
HETATM 1228 O  O   . HOH   G 5 .   ? 4.207  -4.738  6.163  1.00 38.35  ? 396 HOH   A O   1 
HETATM 1229 O  O   . HOH   G 5 .   ? 10.643 4.854   33.534 1.00 37.80  ? 397 HOH   A O   1 
HETATM 1230 O  O   . HOH   G 5 .   ? 35.243 5.239   13.068 1.00 65.70  ? 398 HOH   A O   1 
HETATM 1231 O  O   . HOH   G 5 .   ? 20.832 3.101   -3.065 1.00 45.55  ? 399 HOH   A O   1 
HETATM 1232 O  O   . HOH   G 5 .   ? 31.487 2.834   11.791 1.00 41.34  ? 400 HOH   A O   1 
HETATM 1233 O  O   . HOH   G 5 .   ? 14.142 14.641  25.159 1.00 37.94  ? 401 HOH   A O   1 
HETATM 1234 O  O   . HOH   G 5 .   ? 12.994 -8.334  24.013 1.00 29.04  ? 402 HOH   A O   1 
HETATM 1235 O  O   . HOH   G 5 .   ? 11.594 17.845  27.068 1.00 38.83  ? 403 HOH   A O   1 
HETATM 1236 O  O   . HOH   G 5 .   ? 36.872 -0.322  9.276  1.00 50.70  ? 404 HOH   A O   1 
HETATM 1237 O  O   . HOH   G 5 .   ? 4.566  11.223  18.754 1.00 43.70  ? 405 HOH   A O   1 
HETATM 1238 O  O   . HOH   G 5 .   ? -0.330 15.683  12.895 1.00 35.54  ? 406 HOH   A O   1 
HETATM 1239 O  O   . HOH   G 5 .   ? 27.089 -1.437  5.845  1.00 56.51  ? 407 HOH   A O   1 
HETATM 1240 O  O   . HOH   G 5 .   ? 20.678 24.700  14.079 1.00 43.45  ? 408 HOH   A O   1 
HETATM 1241 O  O   . HOH   G 5 .   ? -1.024 2.229   4.705  1.00 49.13  ? 409 HOH   A O   1 
HETATM 1242 O  O   . HOH   G 5 .   ? 32.608 14.558  6.134  1.00 58.39  ? 410 HOH   A O   1 
HETATM 1243 O  O   . HOH   G 5 .   ? 6.445  23.355  11.579 1.00 35.12  ? 411 HOH   A O   1 
HETATM 1244 O  O   . HOH   G 5 .   ? 19.051 13.436  1.631  1.00 45.33  ? 412 HOH   A O   1 
HETATM 1245 O  O   . HOH   G 5 .   ? 21.041 -4.556  9.462  1.00 42.70  ? 413 HOH   A O   1 
HETATM 1246 O  O   . HOH   G 5 .   ? 30.535 6.513   17.389 1.00 51.54  ? 414 HOH   A O   1 
HETATM 1247 O  O   . HOH   G 5 .   ? 2.149  13.716  5.220  1.00 47.09  ? 415 HOH   A O   1 
HETATM 1248 O  O   . HOH   G 5 .   ? 31.902 0.038   12.945 1.00 56.95  ? 416 HOH   A O   1 
HETATM 1249 O  O   . HOH   G 5 .   ? 24.264 12.873  23.047 1.00 57.02  ? 417 HOH   A O   1 
HETATM 1250 O  O   . HOH   G 5 .   ? 14.656 -4.160  33.897 1.00 45.06  ? 418 HOH   A O   1 
HETATM 1251 O  O   . HOH   G 5 .   ? 15.830 -10.010 3.661  1.00 60.10  ? 419 HOH   A O   1 
HETATM 1252 O  O   . HOH   G 5 .   ? 2.478  1.761   26.423 1.00 35.79  ? 420 HOH   A O   1 
HETATM 1253 O  O   . HOH   G 5 .   ? 8.653  -7.165  8.909  1.00 41.81  ? 421 HOH   A O   1 
HETATM 1254 O  O   . HOH   G 5 .   ? 30.925 -3.838  6.674  1.00 50.15  ? 422 HOH   A O   1 
HETATM 1255 O  O   . HOH   G 5 .   ? 6.444  25.683  21.352 1.00 36.53  ? 423 HOH   A O   1 
HETATM 1256 O  O   . HOH   G 5 .   ? 6.949  11.250  3.815  1.00 47.39  ? 424 HOH   A O   1 
HETATM 1257 O  O   . HOH   G 5 .   ? 17.911 9.433   -1.905 1.00 49.26  ? 425 HOH   A O   1 
HETATM 1258 O  O   . HOH   G 5 .   ? 1.627  -2.487  17.226 1.00 31.32  ? 426 HOH   A O   1 
HETATM 1259 O  O   . HOH   G 5 .   ? 2.607  6.220   28.120 1.00 46.47  ? 427 HOH   A O   1 
HETATM 1260 O  O   . HOH   G 5 .   ? 30.007 4.736   2.654  1.00 42.30  ? 428 HOH   A O   1 
HETATM 1261 O  O   . HOH   G 5 .   ? 22.432 9.101   20.534 1.00 30.63  ? 429 HOH   A O   1 
HETATM 1262 O  O   . HOH   G 5 .   ? 4.437  -1.934  21.497 1.00 34.40  ? 430 HOH   A O   1 
HETATM 1263 O  O   . HOH   G 5 .   ? 22.651 19.198  5.224  1.00 36.48  ? 431 HOH   A O   1 
HETATM 1264 O  O   . HOH   G 5 .   ? 7.402  -4.887  2.398  1.00 37.43  ? 432 HOH   A O   1 
HETATM 1265 O  O   . HOH   G 5 .   ? 24.081 2.539   18.816 1.00 38.48  ? 433 HOH   A O   1 
HETATM 1266 O  O   . HOH   G 5 .   ? 4.123  9.796   28.295 1.00 38.54  ? 434 HOH   A O   1 
HETATM 1267 O  O   . HOH   G 5 .   ? 4.028  14.816  20.232 1.00 30.87  ? 435 HOH   A O   1 
HETATM 1268 O  O   . HOH   G 5 .   ? 4.670  7.513   2.817  1.00 50.70  ? 436 HOH   A O   1 
HETATM 1269 O  O   . HOH   G 5 .   ? 6.472  -3.457  -1.969 1.00 43.21  ? 437 HOH   A O   1 
HETATM 1270 O  O   . HOH   G 5 .   ? 36.526 2.276   5.884  1.00 59.44  ? 438 HOH   A O   1 
HETATM 1271 O  O   . HOH   G 5 .   ? 35.376 10.689  10.888 1.00 66.57  ? 439 HOH   A O   1 
HETATM 1272 O  O   . HOH   G 5 .   ? 3.179  10.918  20.979 1.00 47.79  ? 440 HOH   A O   1 
HETATM 1273 O  O   . HOH   G 5 .   ? 8.224  -10.828 7.917  1.00 59.14  ? 441 HOH   A O   1 
HETATM 1274 O  O   . HOH   G 5 .   ? 24.792 7.680   19.761 1.00 42.03  ? 442 HOH   A O   1 
HETATM 1275 O  O   . HOH   G 5 .   ? 33.267 15.339  20.025 1.00 61.25  ? 443 HOH   A O   1 
HETATM 1276 O  O   . HOH   G 5 .   ? 31.411 9.072   4.201  1.00 38.18  ? 444 HOH   A O   1 
HETATM 1277 O  O   . HOH   G 5 .   ? 26.159 -2.357  14.232 1.00 53.61  ? 445 HOH   A O   1 
HETATM 1278 O  O   . HOH   G 5 .   ? 5.253  -1.333  29.049 1.00 50.60  ? 446 HOH   A O   1 
HETATM 1279 O  O   . HOH   G 5 .   ? 34.958 7.789   13.446 1.00 67.16  ? 447 HOH   A O   1 
HETATM 1280 O  O   . HOH   G 5 .   ? 19.439 7.543   27.396 1.00 40.50  ? 448 HOH   A O   1 
HETATM 1281 O  O   . HOH   G 5 .   ? 9.066  -4.975  31.924 1.00 71.51  ? 449 HOH   A O   1 
HETATM 1282 O  O   . HOH   G 5 .   ? 24.393 -5.443  12.125 1.00 63.29  ? 450 HOH   A O   1 
HETATM 1283 O  O   . HOH   G 5 .   ? 28.157 19.360  4.953  1.00 51.52  ? 451 HOH   A O   1 
HETATM 1284 O  O   . HOH   G 5 .   ? 17.636 11.283  -0.148 1.00 42.63  ? 452 HOH   A O   1 
HETATM 1285 O  O   . HOH   G 5 .   ? 4.886  -4.967  3.255  1.00 52.95  ? 453 HOH   A O   1 
HETATM 1286 O  O   . HOH   G 5 .   ? 24.907 -0.233  2.579  1.00 51.18  ? 454 HOH   A O   1 
HETATM 1287 O  O   . HOH   G 5 .   ? 1.770  -4.699  19.852 1.00 83.75  ? 455 HOH   A O   1 
HETATM 1288 O  O   . HOH   G 5 .   ? 28.858 17.579  22.441 1.00 51.72  ? 456 HOH   A O   1 
HETATM 1289 O  O   . HOH   G 5 .   ? 37.590 -1.224  3.379  1.00 78.14  ? 457 HOH   A O   1 
HETATM 1290 O  O   . HOH   G 5 .   ? 22.676 -4.709  15.999 1.00 57.39  ? 458 HOH   A O   1 
HETATM 1291 O  O   . HOH   G 5 .   ? -0.407 6.228   28.368 1.00 56.00  ? 459 HOH   A O   1 
HETATM 1292 O  O   . HOH   G 5 .   ? 12.629 14.575  0.777  1.00 54.07  ? 460 HOH   A O   1 
HETATM 1293 O  O   . HOH   G 5 .   ? 3.434  -6.662  14.580 1.00 51.93  ? 461 HOH   A O   1 
HETATM 1294 O  O   . HOH   G 5 .   ? 13.910 -5.874  32.064 1.00 66.49  ? 462 HOH   A O   1 
HETATM 1295 O  O   . HOH   G 5 .   ? 25.203 0.365   17.318 1.00 50.56  ? 463 HOH   A O   1 
HETATM 1296 O  O   . HOH   G 5 .   ? 4.655  -1.713  26.430 1.00 43.25  ? 464 HOH   A O   1 
HETATM 1297 O  O   . HOH   G 5 .   ? 26.261 11.061  -1.585 1.00 66.44  ? 465 HOH   A O   1 
HETATM 1298 O  O   . HOH   G 5 .   ? 20.730 14.904  0.268  1.00 49.35  ? 466 HOH   A O   1 
HETATM 1299 O  O   . HOH   G 5 .   ? 16.751 12.291  28.304 1.00 50.49  ? 467 HOH   A O   1 
HETATM 1300 O  O   . HOH   G 5 .   ? 5.890  5.139   2.130  1.00 47.47  ? 468 HOH   A O   1 
HETATM 1301 O  O   . HOH   G 5 .   ? 18.031 11.564  25.257 1.00 46.83  ? 469 HOH   A O   1 
HETATM 1302 O  O   . HOH   G 5 .   ? 12.421 23.692  14.845 1.00 39.68  ? 470 HOH   A O   1 
HETATM 1303 O  O   . HOH   G 5 .   ? 8.855  23.262  26.575 1.00 57.96  ? 471 HOH   A O   1 
HETATM 1304 O  O   . HOH   G 5 .   ? 19.955 9.663   -3.708 1.00 46.26  ? 472 HOH   A O   1 
HETATM 1305 O  O   . HOH   G 5 .   ? 37.123 17.321  13.258 1.00 48.22  ? 473 HOH   A O   1 
HETATM 1306 O  O   . HOH   G 5 .   ? 7.269  15.418  3.934  1.00 50.66  ? 474 HOH   A O   1 
HETATM 1307 O  O   . HOH   G 5 .   ? 2.715  14.172  22.482 1.00 41.88  ? 475 HOH   A O   1 
HETATM 1308 O  O   . HOH   G 5 .   ? 8.521  20.072  6.538  1.00 51.28  ? 476 HOH   A O   1 
HETATM 1309 O  O   . HOH   G 5 .   ? 23.372 24.418  13.385 1.00 46.99  ? 477 HOH   A O   1 
HETATM 1310 O  O   . HOH   G 5 .   ? 16.642 14.047  1.419  1.00 44.52  ? 478 HOH   A O   1 
HETATM 1311 O  O   . HOH   G 5 .   ? 32.352 4.364   13.622 1.00 45.44  ? 479 HOH   A O   1 
HETATM 1312 O  O   . HOH   G 5 .   ? 8.727  7.638   2.281  1.00 40.89  ? 480 HOH   A O   1 
HETATM 1313 O  O   . HOH   G 5 .   ? 24.327 13.718  0.891  1.00 54.29  ? 481 HOH   A O   1 
HETATM 1314 O  O   . HOH   G 5 .   ? 5.838  25.998  13.058 1.00 59.70  ? 482 HOH   A O   1 
HETATM 1315 O  O   . HOH   G 5 .   ? 23.364 10.344  23.052 1.00 41.76  ? 483 HOH   A O   1 
HETATM 1316 O  O   . HOH   G 5 .   ? 22.804 25.433  10.299 1.00 48.06  ? 484 HOH   A O   1 
HETATM 1317 O  O   . HOH   G 5 .   ? 39.561 7.575   7.243  1.00 67.07  ? 485 HOH   A O   1 
HETATM 1318 O  O   . HOH   G 5 .   ? 13.735 14.333  29.846 1.00 50.60  ? 486 HOH   A O   1 
HETATM 1319 O  O   . HOH   G 5 .   ? 3.935  -4.471  27.032 1.00 66.78  ? 487 HOH   A O   1 
HETATM 1320 O  O   . HOH   G 5 .   ? 22.978 1.849   21.360 1.00 49.70  ? 488 HOH   A O   1 
HETATM 1321 O  O   . HOH   G 5 .   ? 5.828  7.197   30.846 1.00 53.18  ? 489 HOH   A O   1 
HETATM 1322 O  O   . HOH   G 5 .   ? 6.107  22.689  8.818  1.00 58.01  ? 490 HOH   A O   1 
HETATM 1323 O  O   . HOH   G 5 .   ? 8.266  9.996   29.581 1.00 50.24  ? 491 HOH   A O   1 
HETATM 1324 O  O   . HOH   G 5 .   ? 5.441  15.718  25.541 1.00 44.43  ? 492 HOH   A O   1 
HETATM 1325 O  O   . HOH   G 5 .   ? 31.556 6.670   14.779 1.00 67.82  ? 493 HOH   A O   1 
HETATM 1326 O  O   . HOH   G 5 .   ? 1.160  21.018  7.667  1.00 54.10  ? 494 HOH   A O   1 
HETATM 1327 O  O   . HOH   G 5 .   ? 5.853  -7.166  27.246 1.00 52.58  ? 495 HOH   A O   1 
HETATM 1328 O  O   . HOH   G 5 .   ? 4.359  -6.718  22.652 1.00 47.18  ? 496 HOH   A O   1 
HETATM 1329 O  O   . HOH   G 5 .   ? 18.353 -6.983  30.807 1.00 65.38  ? 497 HOH   A O   1 
HETATM 1330 O  O   . HOH   G 5 .   ? 14.468 11.852  -2.082 1.00 51.72  ? 498 HOH   A O   1 
HETATM 1331 O  O   . HOH   G 5 .   ? 9.063  23.979  11.630 1.00 38.80  ? 499 HOH   A O   1 
HETATM 1332 O  O   . HOH   G 5 .   ? 21.752 10.832  25.196 1.00 45.96  ? 500 HOH   A O   1 
HETATM 1333 O  O   . HOH   G 5 .   ? 36.941 20.934  9.081  1.00 47.32  ? 501 HOH   A O   1 
HETATM 1334 O  O   . HOH   G 5 .   ? -0.404 12.588  17.408 1.00 47.91  ? 502 HOH   A O   1 
HETATM 1335 O  O   . HOH   G 5 .   ? 9.201  14.646  28.634 1.00 42.47  ? 503 HOH   A O   1 
HETATM 1336 O  O   . HOH   G 5 .   ? 10.221 25.230  14.004 1.00 38.00  ? 504 HOH   A O   1 
HETATM 1337 O  O   . HOH   G 5 .   ? 2.232  26.322  18.886 1.00 57.22  ? 505 HOH   A O   1 
HETATM 1338 O  O   . HOH   G 5 .   ? 7.863  12.702  29.724 1.00 45.43  ? 506 HOH   A O   1 
HETATM 1339 O  O   . HOH   G 5 .   ? 3.452  -9.900  16.364 1.00 54.93  ? 507 HOH   A O   1 
HETATM 1340 O  O   . HOH   G 5 .   ? 3.422  22.404  7.751  1.00 57.00  ? 508 HOH   A O   1 
HETATM 1341 O  O   . HOH   G 5 .   ? 5.866  14.567  28.054 1.00 55.17  ? 509 HOH   A O   1 
HETATM 1342 O  O   . HOH   G 5 .   ? 3.877  24.224  3.442  1.00 63.01  ? 510 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   ? 0.4287 0.3687 0.3915 -0.0440 -0.1104 0.0195  7   SER   A N   
2    C CA  . SER   A 1   ? 0.4219 0.3783 0.4247 -0.0422 -0.1152 0.0263  7   SER   A CA  
3    C C   . SER   A 1   ? 0.3976 0.3730 0.4298 -0.0354 -0.1050 0.0312  7   SER   A C   
4    O O   . SER   A 1   ? 0.4013 0.3776 0.4239 -0.0333 -0.0988 0.0306  7   SER   A O   
5    C CB  . SER   A 1   ? 0.4549 0.4036 0.4650 -0.0513 -0.1382 0.0352  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.4781 0.4283 0.4939 -0.0535 -0.1471 0.0446  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3706 0.3583 0.4366 -0.0322 -0.1014 0.0352  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3392 0.3397 0.4311 -0.0271 -0.0892 0.0392  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3144 0.3227 0.4271 -0.0229 -0.0770 0.0381  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3136 0.3202 0.4167 -0.0222 -0.0749 0.0326  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2883 0.3030 0.4270 -0.0201 -0.0664 0.0431  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2933 0.3109 0.4475 -0.0169 -0.0522 0.0424  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2914 0.3098 0.4539 -0.0144 -0.0345 0.0428  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3053 0.3245 0.4750 -0.0148 -0.0344 0.0466  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2831 0.3016 0.4719 -0.0180 -0.0591 0.0510  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2698 0.2859 0.4309 -0.0127 -0.0188 0.0395  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2689 0.2797 0.4337 -0.0121 0.0010  0.0389  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2813 0.2885 0.4821 -0.0107 0.0112  0.0466  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2787 0.2863 0.4874 -0.0100 0.0081  0.0480  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2877 0.2938 0.4194 -0.0132 0.0106  0.0303  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2826 0.2937 0.3861 -0.0141 -0.0003 0.0244  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3097 0.3046 0.4362 -0.0150 0.0312  0.0283  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2823 0.2914 0.3594 -0.0158 0.0033  0.0191  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2937 0.2968 0.5200 -0.0100 0.0244  0.0522  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3053 0.3032 0.5715 -0.0083 0.0384  0.0606  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3367 0.3188 0.5937 -0.0086 0.0670  0.0563  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3655 0.3434 0.6271 -0.0091 0.0771  0.0567  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2865 0.2914 0.6016 -0.0075 0.0297  0.0744  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2946 0.3103 0.6157 -0.0096 -0.0001 0.0794  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2961 0.3142 0.6421 -0.0099 -0.0085 0.0852  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3242 0.3447 0.6209 -0.0122 -0.0191 0.0771  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3066 0.3305 0.6506 -0.0138 -0.0361 0.0880  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3376 0.3622 0.6311 -0.0159 -0.0451 0.0803  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3320 0.3578 0.6489 -0.0173 -0.0542 0.0857  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3625 0.3883 0.6684 -0.0227 -0.0797 0.0870  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3407 0.3119 0.5796 -0.0092 0.0800  0.0516  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3742 0.3242 0.5931 -0.0117 0.1076  0.0462  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3943 0.3317 0.6382 -0.0098 0.1272  0.0517  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3726 0.3147 0.6181 -0.0085 0.1190  0.0532  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4071 0.3515 0.5688 -0.0165 0.1042  0.0349  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4111 0.3645 0.5611 -0.0156 0.0883  0.0344  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4246 0.3424 0.5570 -0.0218 0.1307  0.0291  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.4105 0.3319 0.6794 -0.0093 0.1542  0.0558  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4141 0.3208 0.7114 -0.0070 0.1773  0.0620  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3963 0.3222 0.7436 -0.0023 0.1593  0.0735  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3826 0.3280 0.7620 -0.0008 0.1379  0.0810  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.4016 0.3224 0.7507 -0.0011 0.1643  0.0747  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3790 0.3175 0.7720 0.0022  0.1449  0.0845  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3610 0.3142 0.7194 0.0006  0.1162  0.0778  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3477 0.3065 0.7227 0.0021  0.1078  0.0815  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.4017 0.3268 0.8318 0.0053  0.1690  0.0924  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4688 0.3853 0.9530 0.0077  0.1923  0.1031  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4655 0.3987 1.0074 0.0097  0.1776  0.1163  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5169 0.4059 0.9810 0.0067  0.2280  0.0980  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3540 0.3136 0.6694 -0.0022 0.1011  0.0688  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3432 0.3150 0.6279 -0.0034 0.0768  0.0627  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3197 0.3069 0.6030 -0.0046 0.0516  0.0624  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3131 0.3003 0.5977 -0.0054 0.0540  0.0629  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3569 0.3189 0.5852 -0.0063 0.0838  0.0521  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3798 0.3235 0.5957 -0.0068 0.1057  0.0517  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3901 0.3357 0.6247 -0.0041 0.1046  0.0563  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4218 0.3435 0.6051 -0.0108 0.1281  0.0468  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4141 0.3409 0.6359 -0.0046 0.1259  0.0566  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4543 0.3544 0.6199 -0.0126 0.1490  0.0466  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4548 0.3580 0.6401 -0.0091 0.1481  0.0519  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4871 0.3675 0.6531 -0.0108 0.1694  0.0524  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.3074 0.3052 0.5848 -0.0053 0.0293  0.0612  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2890 0.2966 0.5538 -0.0075 0.0061  0.0593  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2924 0.3013 0.5146 -0.0083 -0.0007 0.0494  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2986 0.3074 0.5200 -0.0076 -0.0027 0.0486  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2969 0.3115 0.5954 -0.0093 -0.0145 0.0680  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3000 0.3189 0.5755 -0.0132 -0.0390 0.0647  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3248 0.3467 0.6328 -0.0176 -0.0606 0.0750  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3368 0.3561 0.6201 -0.0224 -0.0809 0.0699  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3638 0.3797 0.6209 -0.0275 -0.0982 0.0677  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3677 0.3848 0.6194 -0.0277 -0.0986 0.0701  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3610 0.3697 0.5927 -0.0324 -0.1122 0.0619  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2721 0.2820 0.4633 -0.0094 -0.0033 0.0430  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2785 0.2901 0.4358 -0.0099 -0.0086 0.0355  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2806 0.2965 0.4290 -0.0114 -0.0265 0.0336  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2940 0.3108 0.4399 -0.0125 -0.0306 0.0341  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2900 0.2976 0.4188 -0.0110 0.0025  0.0303  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2751 0.2857 0.3776 -0.0116 -0.0033 0.0256  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.3106 0.3073 0.4423 -0.0116 0.0222  0.0319  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2618 0.2780 0.4040 -0.0119 -0.0357 0.0313  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2714 0.2858 0.3992 -0.0145 -0.0501 0.0284  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2648 0.2776 0.3696 -0.0137 -0.0491 0.0220  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2719 0.2870 0.3782 -0.0115 -0.0414 0.0218  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2929 0.3040 0.4385 -0.0182 -0.0651 0.0331  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3134 0.3270 0.4878 -0.0193 -0.0687 0.0422  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3015 0.3120 0.4607 -0.0175 -0.0643 0.0336  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2489 0.2559 0.3336 -0.0158 -0.0563 0.0176  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2500 0.2534 0.3204 -0.0151 -0.0537 0.0127  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2673 0.2676 0.3506 -0.0161 -0.0573 0.0135  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2711 0.2656 0.3620 -0.0202 -0.0682 0.0153  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2596 0.2518 0.3068 -0.0180 -0.0582 0.0079  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2876 0.2821 0.3228 -0.0168 -0.0538 0.0070  19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3016 0.2956 0.3362 -0.0186 -0.0589 0.0093  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2683 0.2669 0.2984 -0.0137 -0.0445 0.0051  19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2656 0.2690 0.3521 -0.0131 -0.0497 0.0131  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2677 0.2680 0.3678 -0.0136 -0.0517 0.0138  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3029 0.2890 0.3918 -0.0191 -0.0612 0.0091  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3079 0.2897 0.4093 -0.0228 -0.0701 0.0107  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2735 0.2782 0.3763 -0.0097 -0.0421 0.0146  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2723 0.2757 0.3931 -0.0093 -0.0417 0.0166  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2865 0.2941 0.4086 -0.0056 -0.0329 0.0186  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3013 0.3084 0.4409 -0.0043 -0.0303 0.0214  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3172 0.3164 0.4605 -0.0055 -0.0310 0.0179  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3157 0.3035 0.4431 -0.0091 -0.0342 0.0108  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3022 0.3022 0.4631 -0.0037 -0.0272 0.0211  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3039 0.2805 0.3679 -0.0205 -0.0592 0.0034  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3323 0.2888 0.3757 -0.0271 -0.0654 -0.0025 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3491 0.2976 0.3861 -0.0346 -0.0824 -0.0006 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.3730 0.3031 0.3938 -0.0426 -0.0918 -0.0042 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3534 0.2982 0.3722 -0.0265 -0.0546 -0.0087 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.3691 0.3128 0.3710 -0.0265 -0.0541 -0.0091 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3672 0.3275 0.3790 -0.0205 -0.0469 -0.0057 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.3856 0.3110 0.3591 -0.0325 -0.0590 -0.0129 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3742 0.3279 0.3675 -0.0221 -0.0472 -0.0074 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.3892 0.3221 0.3588 -0.0290 -0.0541 -0.0113 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3374 0.2981 0.3871 -0.0329 -0.0866 0.0056  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3638 0.3195 0.4151 -0.0398 -0.1038 0.0106  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3689 0.3361 0.4597 -0.0396 -0.1111 0.0197  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3680 0.3353 0.4710 -0.0443 -0.1252 0.0271  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3621 0.3210 0.4026 -0.0384 -0.1028 0.0124  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3839 0.3295 0.3877 -0.0391 -0.0955 0.0046  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3830 0.3320 0.3790 -0.0380 -0.0953 0.0074  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4132 0.3326 0.3856 -0.0485 -0.1043 -0.0007 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3683 0.3457 0.4819 -0.0338 -0.1003 0.0207  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3743 0.3610 0.5277 -0.0328 -0.1029 0.0296  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3915 0.3697 0.5576 -0.0414 -0.1224 0.0335  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4037 0.3677 0.5468 -0.0471 -0.1290 0.0267  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3657 0.3604 0.5344 -0.0258 -0.0866 0.0294  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3947 0.3798 0.5983 -0.0430 -0.1313 0.0448  24  THR   A N   
135  C CA  . THR   A 18  ? 0.4052 0.3844 0.6301 -0.0523 -0.1532 0.0519  24  THR   A CA  
136  C C   . THR   A 18  ? 0.4009 0.3860 0.6645 -0.0494 -0.1477 0.0558  24  THR   A C   
137  O O   . THR   A 18  ? 0.3850 0.3785 0.6588 -0.0400 -0.1263 0.0542  24  THR   A O   
138  C CB  . THR   A 18  ? 0.4207 0.4045 0.6708 -0.0564 -0.1684 0.0649  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4282 0.4271 0.7228 -0.0479 -0.1527 0.0735  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4444 0.4222 0.6583 -0.0591 -0.1736 0.0624  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4138 0.3933 0.6989 -0.0583 -0.1680 0.0618  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4239 0.4082 0.7494 -0.0564 -0.1643 0.0665  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3949 0.3944 0.7679 -0.0469 -0.1469 0.0770  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3889 0.3923 0.7780 -0.0396 -0.1281 0.0761  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4812 0.4562 0.8225 -0.0697 -0.1930 0.0725  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.5818 0.5381 0.8813 -0.0775 -0.2002 0.0597  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.6144 0.5628 0.9314 -0.0856 -0.2137 0.0609  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.6304 0.5741 0.8754 -0.0776 -0.1921 0.0456  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.6477 0.5773 0.9171 -0.0908 -0.2128 0.0467  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.6668 0.5930 0.8935 -0.0858 -0.1991 0.0376  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3833 0.3888 0.7745 -0.0468 -0.1504 0.0863  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3745 0.3901 0.8089 -0.0385 -0.1311 0.0961  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3635 0.3802 0.7717 -0.0285 -0.1016 0.0867  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3598 0.3783 0.7919 -0.0219 -0.0808 0.0897  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4102 0.4304 0.8670 -0.0411 -0.1408 0.1077  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5021 0.5299 1.0202 -0.0351 -0.1243 0.1215  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5271 0.5573 1.0944 -0.0366 -0.1288 0.1318  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5262 0.5561 1.0434 -0.0283 -0.1029 0.1217  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3481 0.3620 0.7060 -0.0281 -0.1001 0.0759  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3421 0.3565 0.6729 -0.0207 -0.0770 0.0677  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3228 0.3354 0.6515 -0.0175 -0.0667 0.0635  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3235 0.3364 0.6543 -0.0115 -0.0456 0.0638  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3426 0.3543 0.6238 -0.0220 -0.0808 0.0575  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3671 0.3801 0.6431 -0.0239 -0.0867 0.0603  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3658 0.3830 0.6670 -0.0206 -0.0759 0.0672  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3785 0.3864 0.6249 -0.0287 -0.1007 0.0557  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3228 0.3311 0.6419 -0.0219 -0.0801 0.0590  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3252 0.3321 0.6450 -0.0186 -0.0702 0.0559  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3193 0.3286 0.6860 -0.0157 -0.0612 0.0655  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3197 0.3286 0.6881 -0.0099 -0.0428 0.0655  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3305 0.3297 0.6328 -0.0246 -0.0847 0.0489  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3621 0.3568 0.6188 -0.0247 -0.0833 0.0387  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3937 0.3804 0.6219 -0.0309 -0.0964 0.0336  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3634 0.3606 0.6000 -0.0184 -0.0671 0.0341  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.4112 0.3955 0.6058 -0.0280 -0.0870 0.0256  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3977 0.3893 0.5990 -0.0206 -0.0704 0.0264  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3563 0.3587 0.6014 -0.0118 -0.0507 0.0369  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3953 0.3888 0.5766 -0.0160 -0.0585 0.0224  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3724 0.3760 0.5936 -0.0084 -0.0415 0.0331  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3874 0.3880 0.5800 -0.0102 -0.0456 0.0266  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3176 0.3286 0.7231 -0.0200 -0.0742 0.0748  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3153 0.3285 0.7743 -0.0174 -0.0655 0.0860  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.3101 0.3232 0.7789 -0.0095 -0.0377 0.0902  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.3062 0.3165 0.8035 -0.0048 -0.0191 0.0957  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3112 0.3271 0.8127 -0.0247 -0.0880 0.0973  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.3024 0.3161 0.7494 -0.0089 -0.0342 0.0880  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.3080 0.3173 0.7584 -0.0033 -0.0075 0.0905  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.3056 0.3105 0.7002 -0.0010 0.0045  0.0794  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.3269 0.3279 0.7058 0.0003  0.0175  0.0779  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.3299 0.3421 0.8055 -0.0048 -0.0108 0.0983  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3849 0.4016 0.9241 -0.0071 -0.0215 0.1126  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3887 0.4019 0.9691 -0.0032 -0.0033 0.1207  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.4118 0.4347 0.9592 -0.0143 -0.0518 0.1165  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2815 0.2868 0.6486 -0.0011 -0.0004 0.0724  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2848 0.2879 0.6045 0.0001  0.0064  0.0642  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2993 0.2924 0.6082 0.0032  0.0316  0.0656  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.3034 0.2900 0.6338 0.0057  0.0459  0.0710  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2759 0.2811 0.5798 -0.0001 -0.0021 0.0593  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2843 0.2887 0.5470 0.0010  0.0031  0.0536  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.3034 0.3112 0.5398 -0.0013 -0.0066 0.0479  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2752 0.2812 0.5338 0.0017  -0.0016 0.0515  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2852 0.2749 0.5586 0.0022  0.0372  0.0608  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.3106 0.2868 0.5589 0.0023  0.0585  0.0603  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.3294 0.3066 0.5366 0.0010  0.0531  0.0558  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3608 0.3295 0.5553 0.0012  0.0635  0.0581  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.3311 0.2999 0.5683 0.0005  0.0688  0.0587  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3621 0.3124 0.5611 -0.0020 0.0889  0.0564  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.3165 0.2838 0.6006 0.0022  0.0768  0.0657  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.3079 0.2954 0.4973 -0.0006 0.0366  0.0506  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.3154 0.3058 0.4743 -0.0018 0.0305  0.0482  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2858 0.2879 0.4411 -0.0022 0.0130  0.0435  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2797 0.2845 0.4391 -0.0031 0.0071  0.0408  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.3413 0.3215 0.4652 -0.0057 0.0398  0.0472  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.3559 0.3410 0.4519 -0.0082 0.0299  0.0464  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3770 0.3603 0.4601 -0.0092 0.0293  0.0510  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.3425 0.3357 0.4250 -0.0101 0.0188  0.0423  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3777 0.3685 0.4432 -0.0118 0.0177  0.0510  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3560 0.3522 0.4205 -0.0123 0.0122  0.0452  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.3389 0.3367 0.4245 -0.0102 0.0142  0.0375  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3502 0.3544 0.4037 -0.0142 0.0019  0.0434  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.3393 0.3436 0.4092 -0.0120 0.0050  0.0347  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3367 0.3441 0.3922 -0.0139 -0.0005 0.0376  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2619 0.2690 0.4101 -0.0015 0.0062  0.0430  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2652 0.2791 0.4068 -0.0019 -0.0061 0.0382  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2817 0.2991 0.4098 -0.0016 -0.0075 0.0398  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2819 0.2980 0.4124 -0.0006 -0.0027 0.0451  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2735 0.2880 0.4346 -0.0018 -0.0150 0.0358  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.3052 0.3183 0.4853 0.0000  -0.0123 0.0390  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3337 0.3483 0.5096 0.0012  -0.0135 0.0382  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3399 0.3535 0.5308 0.0031  -0.0090 0.0419  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.3136 0.3298 0.4746 0.0006  -0.0174 0.0346  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2773 0.2988 0.3944 -0.0023 -0.0137 0.0364  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2815 0.3074 0.3937 -0.0018 -0.0151 0.0398  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2767 0.3038 0.3898 -0.0011 -0.0195 0.0346  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2793 0.3067 0.3815 -0.0025 -0.0220 0.0309  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.3127 0.3394 0.4062 -0.0051 -0.0147 0.0441  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3916 0.4240 0.4835 -0.0058 -0.0187 0.0510  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.4209 0.4578 0.5268 -0.0030 -0.0202 0.0511  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.4257 0.4563 0.5023 -0.0101 -0.0203 0.0570  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2630 0.2885 0.3881 0.0008  -0.0186 0.0341  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2695 0.2903 0.3926 0.0009  -0.0187 0.0286  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2784 0.2990 0.4004 0.0007  -0.0190 0.0282  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2709 0.2968 0.3889 0.0013  -0.0175 0.0314  36  SER   A C   
244  O O   . SER   A 30  ? 0.2809 0.3023 0.3902 0.0007  -0.0170 0.0262  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2720 0.2881 0.4092 0.0025  -0.0144 0.0286  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.3078 0.3214 0.4415 0.0016  -0.0158 0.0261  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2599 0.2652 0.3904 0.0013  -0.0120 0.0215  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.3241 0.3413 0.4693 0.0044  -0.0097 0.0319  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2477 0.2821 0.3718 0.0019  -0.0175 0.0407  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2648 0.3055 0.3902 0.0015  -0.0186 0.0459  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2656 0.3073 0.3739 -0.0014 -0.0225 0.0424  37  SER   A C   
252  O O   . SER   A 31  ? 0.2759 0.3214 0.3866 -0.0018 -0.0232 0.0448  37  SER   A O   
253  C CB  . SER   A 31  ? 0.3161 0.3650 0.4522 0.0009  -0.0215 0.0588  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3974 0.4469 0.5169 -0.0032 -0.0266 0.0622  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2472 0.2855 0.3423 -0.0033 -0.0240 0.0379  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2473 0.2854 0.3277 -0.0059 -0.0261 0.0343  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2394 0.2713 0.3155 -0.0051 -0.0257 0.0256  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2508 0.2822 0.3168 -0.0067 -0.0268 0.0227  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2521 0.2880 0.3209 -0.0093 -0.0257 0.0360  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2642 0.3025 0.3268 -0.0129 -0.0286 0.0446  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2927 0.3221 0.3371 -0.0174 -0.0250 0.0452  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2905 0.3160 0.3205 -0.0207 -0.0237 0.0397  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.3138 0.3298 0.3215 -0.0272 -0.0212 0.0403  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.3284 0.3361 0.3220 -0.0316 -0.0203 0.0461  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.3017 0.3138 0.2988 -0.0299 -0.0188 0.0348  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2377 0.2634 0.3199 -0.0037 -0.0252 0.0222  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2449 0.2621 0.3204 -0.0052 -0.0283 0.0156  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2438 0.2628 0.3194 -0.0067 -0.0313 0.0163  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2548 0.2702 0.3242 -0.0083 -0.0350 0.0135  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2708 0.2816 0.3332 -0.0058 -0.0273 0.0110  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2898 0.2887 0.3401 -0.0090 -0.0330 0.0054  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3014 0.2931 0.3545 -0.0111 -0.0372 0.0039  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2984 0.2948 0.3366 -0.0103 -0.0344 0.0036  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2490 0.2714 0.3331 -0.0062 -0.0282 0.0208  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2606 0.2820 0.3490 -0.0073 -0.0266 0.0220  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2686 0.2875 0.3759 -0.0066 -0.0256 0.0247  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2698 0.2890 0.3832 -0.0052 -0.0231 0.0270  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2739 0.2960 0.3523 -0.0086 -0.0197 0.0244  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2973 0.3212 0.3600 -0.0106 -0.0205 0.0221  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3142 0.3346 0.3635 -0.0141 -0.0145 0.0242  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2952 0.3179 0.3596 -0.0106 -0.0231 0.0188  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2508 0.2679 0.3707 -0.0075 -0.0267 0.0260  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2601 0.2753 0.4045 -0.0068 -0.0247 0.0303  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2608 0.2742 0.4173 -0.0070 -0.0172 0.0339  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2844 0.2986 0.4371 -0.0083 -0.0209 0.0330  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2683 0.2817 0.4260 -0.0088 -0.0374 0.0299  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2846 0.2971 0.4743 -0.0087 -0.0371 0.0357  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.3008 0.3103 0.4961 -0.0106 -0.0463 0.0338  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3006 0.3135 0.5132 -0.0107 -0.0423 0.0411  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2566 0.2656 0.4262 -0.0056 -0.0043 0.0382  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.2789 0.2829 0.4645 -0.0054 0.0073  0.0420  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2899 0.2930 0.5152 -0.0039 0.0090  0.0490  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2848 0.2860 0.5158 -0.0025 0.0131  0.0505  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.3068 0.3003 0.4713 -0.0062 0.0260  0.0411  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3086 0.2930 0.4930 -0.0059 0.0424  0.0449  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.3076 0.3022 0.4360 -0.0089 0.0224  0.0354  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2943 0.2994 0.5496 -0.0045 0.0048  0.0545  43  SER   A N   
298  C CA  . SER   A 37  ? 0.3061 0.3111 0.6067 -0.0036 0.0059  0.0634  43  SER   A CA  
299  C C   . SER   A 37  ? 0.3269 0.3256 0.6549 -0.0019 0.0250  0.0702  43  SER   A C   
300  O O   . SER   A 37  ? 0.3333 0.3284 0.6439 -0.0023 0.0334  0.0673  43  SER   A O   
301  C CB  . SER   A 37  ? 0.3122 0.3245 0.6327 -0.0072 -0.0192 0.0669  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3320 0.3472 0.6507 -0.0097 -0.0287 0.0684  43  SER   A OG  
303  N N   . SER   A 38  ? 0.3262 0.3221 0.6987 0.0001  0.0341  0.0793  44  SER   A N   
304  C CA  . SER   A 38  ? 0.3346 0.3224 0.7397 0.0021  0.0558  0.0869  44  SER   A CA  
305  C C   . SER   A 38  ? 0.3333 0.3309 0.7819 0.0005  0.0405  0.0972  44  SER   A C   
306  O O   . SER   A 38  ? 0.3369 0.3452 0.7998 -0.0027 0.0134  0.1010  44  SER   A O   
307  C CB  . SER   A 38  ? 0.3635 0.3416 0.7997 0.0053  0.0766  0.0932  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3868 0.3749 0.8554 0.0049  0.0581  0.0990  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3251 0.3172 0.7934 0.0019  0.0575  0.1023  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3367 0.3378 0.8512 0.0006  0.0449  0.1148  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3747 0.3683 0.9507 0.0042  0.0703  0.1281  45  THR   A C   
312  O O   . THR   A 39  ? 0.4028 0.3795 0.9706 0.0074  0.1030  0.1242  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3435 0.3461 0.8287 -0.0010 0.0415  0.1097  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3626 0.3502 0.8386 0.0017  0.0743  0.1059  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3490 0.3560 0.7734 -0.0038 0.0227  0.0963  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3745 0.3784 1.0105 0.0031  0.0566  0.1445  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3917 0.3891 1.0950 0.0069  0.0818  0.1594  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3958 0.3858 1.1019 0.0086  0.1025  0.1605  46  THR   A C   
319  O O   . THR   A 40  ? 0.4071 0.3810 1.1399 0.0126  0.1390  0.1642  46  THR   A O   
320  C CB  . THR   A 40  ? 0.4099 0.4216 1.1868 0.0047  0.0582  0.1793  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4485 0.4749 1.2243 -0.0013 0.0216  0.1848  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4155 0.4299 1.1927 0.0035  0.0459  0.1774  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3919 0.3906 1.0671 0.0054  0.0825  0.1561  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3919 0.3840 1.0679 0.0067  0.1008  0.1565  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4019 0.3796 1.0031 0.0064  0.1188  0.1360  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4079 0.3877 0.9535 0.0043  0.1049  0.1228  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3860 0.3951 1.0793 0.0033  0.0694  0.1666  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3959 0.3583 0.9977 0.0078  0.1492  0.1341  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4231 0.3699 0.9561 0.0056  0.1652  0.1159  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3925 0.3540 0.8915 0.0028  0.1379  0.1102  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3742 0.3464 0.9075 0.0032  0.1275  0.1208  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4835 0.4068 1.0290 0.0066  0.2058  0.1159  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6014 0.4999 1.1642 0.0085  0.2431  0.1175  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.7516 0.6202 1.2432 0.0042  0.2700  0.0995  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.8026 0.6412 1.2966 0.0036  0.3101  0.0979  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7802 0.6541 1.2066 0.0002  0.2487  0.0862  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3819 0.3429 0.8162 0.0000  0.1280  0.0948  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3734 0.3448 0.7721 -0.0024 0.1076  0.0881  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3675 0.3246 0.7410 -0.0040 0.1296  0.0800  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3899 0.3256 0.7611 -0.0045 0.1611  0.0767  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3449 0.3111 0.6980 -0.0055 0.1147  0.0765  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3512 0.3048 0.6847 -0.0075 0.1339  0.0695  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3566 0.3083 0.6280 -0.0117 0.1266  0.0543  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3719 0.3145 0.6262 -0.0143 0.1388  0.0484  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3522 0.3152 0.7270 -0.0055 0.1298  0.0810  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3860 0.3485 0.8436 -0.0012 0.1439  0.1015  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3513 0.3123 0.5934 -0.0125 0.1060  0.0492  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3657 0.3270 0.5566 -0.0163 0.0975  0.0373  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3869 0.3265 0.5409 -0.0215 0.1179  0.0277  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3955 0.3223 0.5567 -0.0214 0.1334  0.0295  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3583 0.3359 0.5352 -0.0152 0.0702  0.0365  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4016 0.3947 0.5980 -0.0129 0.0490  0.0435  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4159 0.4101 0.6197 -0.0128 0.0508  0.0455  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3752 0.3772 0.5790 -0.0118 0.0310  0.0473  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3942 0.3278 0.5092 -0.0268 0.1180  0.0184  52  THR   A N   
356  C CA  . THR   A 46  ? 0.4315 0.3430 0.5033 -0.0345 0.1317  0.0096  52  THR   A CA  
357  C C   . THR   A 46  ? 0.4191 0.3419 0.4576 -0.0372 0.1087  0.0052  52  THR   A C   
358  O O   . THR   A 46  ? 0.4061 0.3442 0.4433 -0.0360 0.0928  0.0043  52  THR   A O   
359  C CB  . THR   A 46  ? 0.4952 0.3883 0.5490 -0.0406 0.1494  0.0028  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5242 0.4006 0.6068 -0.0389 0.1770  0.0066  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5269 0.3985 0.5242 -0.0518 0.1538  -0.0073 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4158 0.3305 0.4304 -0.0405 0.1082  0.0038  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4065 0.3317 0.3952 -0.0431 0.0875  0.0018  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4269 0.3375 0.3746 -0.0536 0.0891  -0.0051 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4556 0.3399 0.3785 -0.0612 0.1071  -0.0090 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4040 0.3273 0.3864 -0.0427 0.0848  0.0050  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3861 0.3207 0.4104 -0.0337 0.0845  0.0118  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4085 0.3451 0.3716 -0.0448 0.0626  0.0050  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3693 0.3279 0.4221 -0.0272 0.0659  0.0149  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3931 0.3181 0.3329 -0.0549 0.0710  -0.0065 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4103 0.3235 0.3146 -0.0658 0.0683  -0.0116 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4145 0.3152 0.2854 -0.0743 0.0630  -0.0105 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3947 0.3078 0.2745 -0.0698 0.0521  -0.0050 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4025 0.3369 0.3147 -0.0639 0.0492  -0.0109 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4495 0.3242 0.2802 -0.0874 0.0697  -0.0154 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4826 0.3428 0.2753 -0.0981 0.0614  -0.0132 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.4941 0.3501 0.2603 -0.1103 0.0470  -0.0156 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5174 0.3466 0.2518 -0.1217 0.0584  -0.0227 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5169 0.3415 0.2783 -0.1052 0.0848  -0.0164 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5354 0.3624 0.3293 -0.0933 0.1024  -0.0136 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5500 0.3999 0.3658 -0.0848 0.0869  -0.0054 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5563 0.4102 0.4084 -0.0737 0.1018  -0.0025 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5494 0.4258 0.4323 -0.0641 0.0906  0.0038  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5267 0.4230 0.4095 -0.0632 0.0674  0.0073  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5301 0.4088 0.4472 -0.0555 0.1030  0.0068  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4786 0.3605 0.2613 -0.1079 0.0231  -0.0096 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4852 0.3692 0.2569 -0.1172 0.0082  -0.0103 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4803 0.3912 0.2732 -0.1144 -0.0173 -0.0003 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4667 0.3928 0.2807 -0.1051 -0.0211 0.0058  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4700 0.3622 0.2654 -0.1104 0.0181  -0.0164 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4347 0.3632 0.2844 -0.0909 0.0128  -0.0116 56  CYS   A SG  
392  N N   A ASP   A 51  ? 0.4831 0.4003 0.2758 -0.1218 -0.0331 0.0016  57  ASP   A N   
393  N N   B ASP   A 51  ? 0.4856 0.4017 0.2769 -0.1224 -0.0329 0.0013  57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.4650 0.4080 0.2868 -0.1181 -0.0540 0.0121  57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.4720 0.4116 0.2879 -0.1216 -0.0555 0.0115  57  ASP   A CA  
396  C C   A ASP   A 51  ? 0.4463 0.4092 0.3023 -0.1098 -0.0546 0.0106  57  ASP   A C   
397  C C   B ASP   A 51  ? 0.4510 0.4094 0.3002 -0.1133 -0.0549 0.0092  57  ASP   A C   
398  O O   A ASP   A 51  ? 0.4290 0.4088 0.3076 -0.1096 -0.0703 0.0187  57  ASP   A O   
399  O O   B ASP   A 51  ? 0.4377 0.4087 0.3027 -0.1167 -0.0709 0.0158  57  ASP   A O   
400  C CB  A ASP   A 51  ? 0.4995 0.4350 0.2986 -0.1346 -0.0764 0.0207  57  ASP   A CB  
401  C CB  B ASP   A 51  ? 0.5079 0.4336 0.2929 -0.1408 -0.0751 0.0169  57  ASP   A CB  
402  C CG  A ASP   A 51  ? 0.5578 0.4824 0.3392 -0.1488 -0.0849 0.0177  57  ASP   A CG  
403  C CG  B ASP   A 51  ? 0.5548 0.4993 0.3606 -0.1425 -0.0996 0.0320  57  ASP   A CG  
404  O OD1 A ASP   A 51  ? 0.5657 0.4773 0.3354 -0.1496 -0.0686 0.0063  57  ASP   A OD1 
405  O OD1 B ASP   A 51  ? 0.5501 0.5135 0.3867 -0.1295 -0.0989 0.0379  57  ASP   A OD1 
406  O OD2 A ASP   A 51  ? 0.6070 0.5360 0.3887 -0.1596 -0.1083 0.0277  57  ASP   A OD2 
407  O OD2 B ASP   A 51  ? 0.6058 0.5440 0.3966 -0.1581 -0.1199 0.0388  57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.4323 0.3921 0.2938 -0.1030 -0.0369 0.0014  58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.4119 0.3872 0.3017 -0.0952 -0.0350 -0.0004 58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.3815 0.3807 0.3058 -0.0848 -0.0445 0.0076  58  CYS   A C   
411  O O   . CYS   A 52  ? 0.3620 0.3677 0.2951 -0.0778 -0.0449 0.0114  58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.4196 0.3911 0.3162 -0.0865 -0.0154 -0.0079 58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.4390 0.3836 0.3071 -0.0970 0.0010  -0.0179 58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.3492 0.3593 0.2930 -0.0840 -0.0503 0.0098  59  GLN   A N   
415  C CA  . GLN   A 53  ? 0.3272 0.3559 0.3044 -0.0740 -0.0540 0.0164  59  GLN   A CA  
416  C C   . GLN   A 53  ? 0.3105 0.3443 0.3038 -0.0653 -0.0434 0.0119  59  GLN   A C   
417  O O   . GLN   A 53  ? 0.2963 0.3411 0.3143 -0.0588 -0.0441 0.0165  59  GLN   A O   
418  C CB  . GLN   A 53  ? 0.3442 0.3819 0.3371 -0.0807 -0.0713 0.0273  59  GLN   A CB  
419  C CG  . GLN   A 53  ? 0.4049 0.4451 0.3976 -0.0828 -0.0815 0.0359  59  GLN   A CG  
420  C CD  . GLN   A 53  ? 0.4240 0.4764 0.4441 -0.0875 -0.0983 0.0495  59  GLN   A CD  
421  O OE1 . GLN   A 53  ? 0.4405 0.4877 0.4479 -0.1016 -0.1150 0.0558  59  GLN   A OE1 
422  N NE2 . GLN   A 53  ? 0.3840 0.4508 0.4423 -0.0766 -0.0938 0.0549  59  GLN   A NE2 
423  N N   . THR   A 54  ? 0.2970 0.3211 0.2768 -0.0655 -0.0321 0.0036  60  THR   A N   
424  C CA  . THR   A 54  ? 0.2887 0.3160 0.2810 -0.0574 -0.0220 0.0003  60  THR   A CA  
425  C C   . THR   A 54  ? 0.2758 0.2955 0.2590 -0.0530 -0.0107 -0.0047 60  THR   A C   
426  O O   . THR   A 54  ? 0.3026 0.3113 0.2689 -0.0585 -0.0071 -0.0076 60  THR   A O   
427  C CB  . THR   A 54  ? 0.3276 0.3522 0.3213 -0.0631 -0.0207 -0.0023 60  THR   A CB  
428  O OG1 . THR   A 54  ? 0.3886 0.3980 0.3585 -0.0723 -0.0162 -0.0085 60  THR   A OG1 
429  C CG2 . THR   A 54  ? 0.3317 0.3637 0.3388 -0.0692 -0.0336 0.0042  60  THR   A CG2 
430  N N   . GLY   A 55  ? 0.2626 0.2869 0.2579 -0.0436 -0.0053 -0.0045 61  GLY   A N   
431  C CA  . GLY   A 55  ? 0.2512 0.2706 0.2453 -0.0392 0.0026  -0.0063 61  GLY   A CA  
432  C C   . GLY   A 55  ? 0.2390 0.2625 0.2440 -0.0310 0.0048  -0.0047 61  GLY   A C   
433  O O   . GLY   A 55  ? 0.2546 0.2815 0.2650 -0.0293 0.0046  -0.0039 61  GLY   A O   
434  N N   . VAL   A 56  ? 0.2301 0.2515 0.2382 -0.0270 0.0070  -0.0034 62  VAL   A N   
435  C CA  . VAL   A 56  ? 0.2316 0.2533 0.2449 -0.0212 0.0066  -0.0007 62  VAL   A CA  
436  C C   . VAL   A 56  ? 0.2460 0.2675 0.2599 -0.0183 0.0008  0.0018  62  VAL   A C   
437  O O   . VAL   A 56  ? 0.2561 0.2766 0.2732 -0.0197 0.0013  0.0021  62  VAL   A O   
438  C CB  . VAL   A 56  ? 0.2547 0.2729 0.2754 -0.0210 0.0137  0.0004  62  VAL   A CB  
439  C CG1 . VAL   A 56  ? 0.2634 0.2807 0.2871 -0.0164 0.0102  0.0053  62  VAL   A CG1 
440  C CG2 . VAL   A 56  ? 0.2779 0.2950 0.2978 -0.0244 0.0202  -0.0029 62  VAL   A CG2 
441  N N   . TYR   A 57  ? 0.2375 0.2572 0.2470 -0.0150 -0.0037 0.0033  63  TYR   A N   
442  C CA  . TYR   A 57  ? 0.2325 0.2498 0.2407 -0.0138 -0.0103 0.0052  63  TYR   A CA  
443  C C   . TYR   A 57  ? 0.2570 0.2672 0.2602 -0.0127 -0.0150 0.0086  63  TYR   A C   
444  O O   . TYR   A 57  ? 0.2677 0.2739 0.2638 -0.0119 -0.0122 0.0088  63  TYR   A O   
445  C CB  . TYR   A 57  ? 0.2374 0.2549 0.2404 -0.0130 -0.0126 0.0035  63  TYR   A CB  
446  C CG  . TYR   A 57  ? 0.2547 0.2654 0.2481 -0.0110 -0.0107 0.0027  63  TYR   A CG  
447  C CD1 . TYR   A 57  ? 0.2596 0.2717 0.2550 -0.0102 -0.0043 0.0021  63  TYR   A CD1 
448  C CD2 . TYR   A 57  ? 0.2585 0.2586 0.2402 -0.0105 -0.0141 0.0026  63  TYR   A CD2 
449  C CE1 . TYR   A 57  ? 0.2748 0.2777 0.2628 -0.0080 0.0014  0.0016  63  TYR   A CE1 
450  C CE2 . TYR   A 57  ? 0.2804 0.2686 0.2487 -0.0094 -0.0087 0.0010  63  TYR   A CE2 
451  C CZ  . TYR   A 57  ? 0.2921 0.2814 0.2644 -0.0076 0.0005  0.0007  63  TYR   A CZ  
452  O OH  . TYR   A 57  ? 0.3217 0.2965 0.2824 -0.0061 0.0098  -0.0006 63  TYR   A OH  
453  N N   . TYR   A 58  ? 0.2542 0.2620 0.2607 -0.0134 -0.0229 0.0120  64  TYR   A N   
454  C CA  . TYR   A 58  ? 0.2717 0.2708 0.2707 -0.0147 -0.0317 0.0167  64  TYR   A CA  
455  C C   . TYR   A 58  ? 0.2841 0.2717 0.2610 -0.0158 -0.0360 0.0137  64  TYR   A C   
456  O O   . TYR   A 58  ? 0.2813 0.2694 0.2595 -0.0162 -0.0385 0.0117  64  TYR   A O   
457  C CB  . TYR   A 58  ? 0.2665 0.2679 0.2842 -0.0163 -0.0402 0.0239  64  TYR   A CB  
458  C CG  . TYR   A 58  ? 0.2840 0.2756 0.2927 -0.0196 -0.0532 0.0307  64  TYR   A CG  
459  C CD1 . TYR   A 58  ? 0.2972 0.2841 0.2980 -0.0199 -0.0528 0.0342  64  TYR   A CD1 
460  C CD2 . TYR   A 58  ? 0.3081 0.2933 0.3133 -0.0235 -0.0671 0.0339  64  TYR   A CD2 
461  C CE1 . TYR   A 58  ? 0.3260 0.3015 0.3142 -0.0244 -0.0669 0.0419  64  TYR   A CE1 
462  C CE2 . TYR   A 58  ? 0.3380 0.3114 0.3309 -0.0289 -0.0824 0.0411  64  TYR   A CE2 
463  C CZ  . TYR   A 58  ? 0.3489 0.3166 0.3308 -0.0296 -0.0825 0.0452  64  TYR   A CZ  
464  O OH  . TYR   A 58  ? 0.3892 0.3425 0.3535 -0.0365 -0.0995 0.0533  64  TYR   A OH  
465  N N   . CYS   A 59  ? 0.2940 0.2685 0.2496 -0.0169 -0.0360 0.0139  65  CYS   A N   
466  C CA  . CYS   A 59  ? 0.3231 0.2799 0.2519 -0.0191 -0.0365 0.0104  65  CYS   A CA  
467  C C   . CYS   A 59  ? 0.3479 0.2894 0.2583 -0.0251 -0.0508 0.0159  65  CYS   A C   
468  O O   . CYS   A 59  ? 0.3720 0.3058 0.2708 -0.0264 -0.0515 0.0197  65  CYS   A O   
469  C CB  . CYS   A 59  ? 0.3464 0.2961 0.2630 -0.0164 -0.0224 0.0064  65  CYS   A CB  
470  S SG  . CYS   A 59  ? 0.4113 0.3318 0.2912 -0.0191 -0.0160 0.0015  65  CYS   A SG  
471  N N   . SER   A 60  ? 0.3499 0.2865 0.2582 -0.0295 -0.0633 0.0173  66  SER   A N   
472  C CA  . SER   A 60  ? 0.3777 0.2994 0.2696 -0.0373 -0.0811 0.0241  66  SER   A CA  
473  C C   . SER   A 60  ? 0.4187 0.3114 0.2642 -0.0427 -0.0797 0.0209  66  SER   A C   
474  O O   . SER   A 60  ? 0.4488 0.3284 0.2762 -0.0488 -0.0919 0.0280  66  SER   A O   
475  C CB  . SER   A 60  ? 0.4071 0.3293 0.3086 -0.0418 -0.0954 0.0262  66  SER   A CB  
476  O OG  . SER   A 60  ? 0.4786 0.3909 0.3638 -0.0422 -0.0890 0.0171  66  SER   A OG  
477  N N   . SER   A 61  ? 0.4207 0.3013 0.2469 -0.0407 -0.0639 0.0111  67  SER   A N   
478  C CA  . SER   A 61  ? 0.4495 0.2975 0.2292 -0.0457 -0.0570 0.0070  67  SER   A CA  
479  C C   . SER   A 61  ? 0.4629 0.3062 0.2328 -0.0432 -0.0475 0.0096  67  SER   A C   
480  O O   . SER   A 61  ? 0.4981 0.3110 0.2262 -0.0480 -0.0416 0.0075  67  SER   A O   
481  C CB  . SER   A 61  ? 0.4654 0.3007 0.2335 -0.0436 -0.0391 -0.0032 67  SER   A CB  
482  O OG  . SER   A 61  ? 0.4831 0.3372 0.2793 -0.0339 -0.0212 -0.0055 67  SER   A OG  
483  N N   . ARG   A 62  ? 0.4225 0.2920 0.2274 -0.0365 -0.0451 0.0139  68  ARG   A N   
484  C CA  . ARG   A 62  ? 0.4301 0.2977 0.2308 -0.0342 -0.0379 0.0176  68  ARG   A CA  
485  C C   . ARG   A 62  ? 0.4310 0.3157 0.2562 -0.0346 -0.0520 0.0281  68  ARG   A C   
486  O O   . ARG   A 62  ? 0.4339 0.3214 0.2633 -0.0319 -0.0458 0.0318  68  ARG   A O   
487  C CB  . ARG   A 62  ? 0.4430 0.3251 0.2661 -0.0255 -0.0173 0.0123  68  ARG   A CB  
488  C CG  . ARG   A 62  ? 0.4611 0.3270 0.2684 -0.0239 0.0000  0.0043  68  ARG   A CG  
489  C CD  . ARG   A 62  ? 0.5154 0.3499 0.2833 -0.0268 0.0107  0.0039  68  ARG   A CD  
490  N NE  . ARG   A 62  ? 0.5591 0.3745 0.3141 -0.0250 0.0318  -0.0034 68  ARG   A NE  
491  C CZ  . ARG   A 62  ? 0.6167 0.4063 0.3413 -0.0304 0.0340  -0.0086 68  ARG   A CZ  
492  N NH1 . ARG   A 62  ? 0.6123 0.3909 0.3125 -0.0391 0.0140  -0.0074 68  ARG   A NH1 
493  N NH2 . ARG   A 62  ? 0.6326 0.4051 0.3519 -0.0278 0.0569  -0.0145 68  ARG   A NH2 
494  N N   . ARG   A 63  ? 0.4163 0.3151 0.2657 -0.0366 -0.0677 0.0332  69  ARG   A N   
495  C CA  . ARG   A 63  ? 0.4197 0.3367 0.3029 -0.0356 -0.0768 0.0440  69  ARG   A CA  
496  C C   . ARG   A 63  ? 0.3918 0.3265 0.3005 -0.0277 -0.0595 0.0418  69  ARG   A C   
497  O O   . ARG   A 63  ? 0.4037 0.3413 0.3216 -0.0270 -0.0595 0.0491  69  ARG   A O   
498  C CB  . ARG   A 63  ? 0.4496 0.3511 0.3144 -0.0432 -0.0940 0.0559  69  ARG   A CB  
499  C CG  . ARG   A 63  ? 0.5125 0.3970 0.3549 -0.0534 -0.1152 0.0593  69  ARG   A CG  
500  C CD  . ARG   A 63  ? 0.5696 0.4408 0.3983 -0.0623 -0.1365 0.0742  69  ARG   A CD  
501  N NE  . ARG   A 63  ? 0.6335 0.4835 0.4332 -0.0747 -0.1595 0.0777  69  ARG   A NE  
502  C CZ  . ARG   A 63  ? 0.7183 0.5353 0.4642 -0.0859 -0.1708 0.0804  69  ARG   A CZ  
503  N NH1 . ARG   A 63  ? 0.7423 0.5440 0.4581 -0.0849 -0.1591 0.0797  69  ARG   A NH1 
504  N NH2 . ARG   A 63  ? 0.7559 0.5522 0.4745 -0.0989 -0.1931 0.0830  69  ARG   A NH2 
505  N N   . LYS   A 64  ? 0.3679 0.3120 0.2850 -0.0226 -0.0449 0.0319  70  LYS   A N   
506  C CA  . LYS   A 64  ? 0.3633 0.3206 0.2992 -0.0172 -0.0303 0.0290  70  LYS   A CA  
507  C C   . LYS   A 64  ? 0.3351 0.3090 0.2941 -0.0144 -0.0244 0.0235  70  LYS   A C   
508  O O   . LYS   A 64  ? 0.3362 0.3098 0.2917 -0.0150 -0.0270 0.0196  70  LYS   A O   
509  C CB  . LYS   A 64  ? 0.4250 0.3705 0.3398 -0.0152 -0.0172 0.0241  70  LYS   A CB  
510  C CG  . LYS   A 64  ? 0.5426 0.4821 0.4522 -0.0151 -0.0149 0.0302  70  LYS   A CG  
511  C CD  . LYS   A 64  ? 0.6598 0.5892 0.5553 -0.0123 0.0012  0.0257  70  LYS   A CD  
512  C CE  . LYS   A 64  ? 0.7580 0.6701 0.6312 -0.0142 0.0008  0.0324  70  LYS   A CE  
513  N NZ  . LYS   A 64  ? 0.8223 0.7127 0.6612 -0.0213 -0.0137 0.0369  70  LYS   A NZ  
514  N N   . HIS   A 65  ? 0.2997 0.2857 0.2793 -0.0122 -0.0162 0.0231  71  HIS   A N   
515  C CA  . HIS   A 65  ? 0.2879 0.2860 0.2836 -0.0113 -0.0101 0.0179  71  HIS   A CA  
516  C C   . HIS   A 65  ? 0.3103 0.3101 0.3030 -0.0099 0.0003  0.0125  71  HIS   A C   
517  O O   . HIS   A 65  ? 0.3319 0.3310 0.3271 -0.0091 0.0064  0.0137  71  HIS   A O   
518  C CB  . HIS   A 65  ? 0.2783 0.2839 0.2973 -0.0118 -0.0072 0.0214  71  HIS   A CB  
519  C CG  . HIS   A 65  ? 0.2889 0.2941 0.3203 -0.0129 -0.0168 0.0293  71  HIS   A CG  
520  N ND1 . HIS   A 65  ? 0.3023 0.3122 0.3491 -0.0134 -0.0172 0.0295  71  HIS   A ND1 
521  C CD2 . HIS   A 65  ? 0.2963 0.2963 0.3283 -0.0141 -0.0269 0.0385  71  HIS   A CD2 
522  C CE1 . HIS   A 65  ? 0.2971 0.3061 0.3578 -0.0145 -0.0273 0.0389  71  HIS   A CE1 
523  N NE2 . HIS   A 65  ? 0.2986 0.3018 0.3504 -0.0156 -0.0351 0.0450  71  HIS   A NE2 
524  N N   . TYR   A 66  ? 0.2784 0.2802 0.2682 -0.0097 0.0018  0.0080  72  TYR   A N   
525  C CA  . TYR   A 66  ? 0.2721 0.2761 0.2644 -0.0088 0.0095  0.0051  72  TYR   A CA  
526  C C   . TYR   A 66  ? 0.2538 0.2686 0.2590 -0.0115 0.0101  0.0026  72  TYR   A C   
527  O O   . TYR   A 66  ? 0.2585 0.2768 0.2647 -0.0130 0.0055  0.0019  72  TYR   A O   
528  C CB  . TYR   A 66  ? 0.2863 0.2831 0.2694 -0.0072 0.0114  0.0039  72  TYR   A CB  
529  C CG  . TYR   A 66  ? 0.2997 0.2793 0.2617 -0.0062 0.0135  0.0050  72  TYR   A CG  
530  C CD1 . TYR   A 66  ? 0.3205 0.2921 0.2768 -0.0047 0.0222  0.0061  72  TYR   A CD1 
531  C CD2 . TYR   A 66  ? 0.3196 0.2883 0.2647 -0.0077 0.0070  0.0049  72  TYR   A CD2 
532  C CE1 . TYR   A 66  ? 0.3567 0.3074 0.2867 -0.0049 0.0253  0.0071  72  TYR   A CE1 
533  C CE2 . TYR   A 66  ? 0.3436 0.2911 0.2616 -0.0091 0.0084  0.0054  72  TYR   A CE2 
534  C CZ  . TYR   A 66  ? 0.3830 0.3204 0.2915 -0.0078 0.0181  0.0065  72  TYR   A CZ  
535  O OH  . TYR   A 66  ? 0.4307 0.3426 0.3058 -0.0104 0.0201  0.0071  72  TYR   A OH  
536  N N   . PRO   A 67  ? 0.2575 0.2756 0.2701 -0.0130 0.0153  0.0016  73  PRO   A N   
537  C CA  . PRO   A 67  ? 0.2622 0.2871 0.2816 -0.0180 0.0137  -0.0006 73  PRO   A CA  
538  C C   . PRO   A 67  ? 0.2848 0.3133 0.3095 -0.0175 0.0107  0.0010  73  PRO   A C   
539  O O   . PRO   A 67  ? 0.3043 0.3298 0.3327 -0.0137 0.0156  0.0027  73  PRO   A O   
540  C CB  . PRO   A 67  ? 0.2933 0.3185 0.3193 -0.0203 0.0195  -0.0018 73  PRO   A CB  
541  C CG  . PRO   A 67  ? 0.3096 0.3301 0.3352 -0.0148 0.0253  0.0006  73  PRO   A CG  
542  C CD  . PRO   A 67  ? 0.2810 0.2952 0.2947 -0.0111 0.0223  0.0027  73  PRO   A CD  
543  N N   . VAL   A 68  ? 0.2511 0.2843 0.2771 -0.0216 0.0041  0.0013  74  VAL   A N   
544  C CA  . VAL   A 68  ? 0.2541 0.2920 0.2902 -0.0212 0.0004  0.0050  74  VAL   A CA  
545  C C   . VAL   A 68  ? 0.2590 0.3026 0.2986 -0.0291 -0.0086 0.0069  74  VAL   A C   
546  O O   . VAL   A 68  ? 0.2526 0.2932 0.2792 -0.0346 -0.0112 0.0039  74  VAL   A O   
547  C CB  . VAL   A 68  ? 0.2922 0.3273 0.3233 -0.0171 -0.0007 0.0055  74  VAL   A CB  
548  C CG1 . VAL   A 68  ? 0.3227 0.3484 0.3478 -0.0113 0.0068  0.0048  74  VAL   A CG1 
549  C CG2 . VAL   A 68  ? 0.3042 0.3383 0.3245 -0.0190 -0.0049 0.0034  74  VAL   A CG2 
550  N N   . SER   A 69  ? 0.2375 0.2878 0.2952 -0.0300 -0.0130 0.0130  75  SER   A N   
551  C CA  . SER   A 69  ? 0.2453 0.3010 0.3077 -0.0379 -0.0253 0.0181  75  SER   A CA  
552  C C   . SER   A 69  ? 0.2425 0.3006 0.3097 -0.0337 -0.0270 0.0221  75  SER   A C   
553  O O   . SER   A 69  ? 0.2477 0.3053 0.3265 -0.0260 -0.0190 0.0234  75  SER   A O   
554  C CB  . SER   A 69  ? 0.2683 0.3313 0.3566 -0.0409 -0.0298 0.0254  75  SER   A CB  
555  O OG  . SER   A 69  ? 0.3659 0.4264 0.4503 -0.0464 -0.0298 0.0220  75  SER   A OG  
556  N N   . PHE   A 70  ? 0.2192 0.2773 0.2756 -0.0388 -0.0355 0.0235  76  PHE   A N   
557  C CA  . PHE   A 70  ? 0.2302 0.2906 0.2918 -0.0350 -0.0369 0.0273  76  PHE   A CA  
558  C C   . PHE   A 70  ? 0.2510 0.3165 0.3176 -0.0427 -0.0506 0.0360  76  PHE   A C   
559  O O   . PHE   A 70  ? 0.2811 0.3434 0.3333 -0.0527 -0.0596 0.0365  76  PHE   A O   
560  C CB  . PHE   A 70  ? 0.2436 0.2971 0.2868 -0.0311 -0.0314 0.0206  76  PHE   A CB  
561  C CG  . PHE   A 70  ? 0.2458 0.2926 0.2672 -0.0371 -0.0325 0.0159  76  PHE   A CG  
562  C CD1 . PHE   A 70  ? 0.2574 0.2988 0.2700 -0.0373 -0.0257 0.0097  76  PHE   A CD1 
563  C CD2 . PHE   A 70  ? 0.2684 0.3124 0.2783 -0.0430 -0.0385 0.0182  76  PHE   A CD2 
564  C CE1 . PHE   A 70  ? 0.2686 0.3013 0.2639 -0.0426 -0.0228 0.0055  76  PHE   A CE1 
565  C CE2 . PHE   A 70  ? 0.2823 0.3155 0.2701 -0.0489 -0.0353 0.0134  76  PHE   A CE2 
566  C CZ  . PHE   A 70  ? 0.2776 0.3049 0.2594 -0.0487 -0.0267 0.0069  76  PHE   A CZ  
567  N N   . SER   A 71  ? 0.2530 0.3243 0.3385 -0.0388 -0.0522 0.0435  77  SER   A N   
568  C CA  . SER   A 71  ? 0.2663 0.3431 0.3599 -0.0458 -0.0664 0.0544  77  SER   A CA  
569  C C   . SER   A 71  ? 0.2831 0.3524 0.3469 -0.0508 -0.0710 0.0518  77  SER   A C   
570  O O   . SER   A 71  ? 0.3001 0.3623 0.3465 -0.0464 -0.0614 0.0425  77  SER   A O   
571  C CB  . SER   A 71  ? 0.2641 0.3489 0.3915 -0.0391 -0.0639 0.0639  77  SER   A CB  
572  O OG  . SER   A 71  ? 0.2696 0.3494 0.3905 -0.0308 -0.0526 0.0579  77  SER   A OG  
573  N N   . LYS   A 72  ? 0.2977 0.3672 0.3561 -0.0606 -0.0860 0.0609  78  LYS   A N   
574  C CA  . LYS   A 72  ? 0.3307 0.3900 0.3594 -0.0653 -0.0880 0.0592  78  LYS   A CA  
575  C C   . LYS   A 72  ? 0.3254 0.3886 0.3663 -0.0560 -0.0817 0.0611  78  LYS   A C   
576  O O   . LYS   A 72  ? 0.3181 0.3918 0.3905 -0.0497 -0.0812 0.0679  78  LYS   A O   
577  C CB  . LYS   A 72  ? 0.3627 0.4171 0.3757 -0.0802 -0.1068 0.0690  78  LYS   A CB  
578  C CG  . LYS   A 72  ? 0.3989 0.4427 0.3878 -0.0919 -0.1116 0.0636  78  LYS   A CG  
579  C CD  . LYS   A 72  ? 0.4948 0.5290 0.4607 -0.1098 -0.1325 0.0729  78  LYS   A CD  
580  C CE  . LYS   A 72  ? 0.5583 0.5777 0.4956 -0.1217 -0.1343 0.0648  78  LYS   A CE  
581  N NZ  . LYS   A 72  ? 0.6170 0.6201 0.5202 -0.1417 -0.1544 0.0718  78  LYS   A NZ  
582  N N   . PRO   A 73  ? 0.3325 0.3859 0.3502 -0.0559 -0.0763 0.0558  79  PRO   A N   
583  C CA  . PRO   A 73  ? 0.3286 0.3850 0.3586 -0.0474 -0.0703 0.0570  79  PRO   A CA  
584  C C   . PRO   A 73  ? 0.3184 0.3842 0.3715 -0.0480 -0.0800 0.0711  79  PRO   A C   
585  O O   . PRO   A 73  ? 0.3301 0.3944 0.3740 -0.0578 -0.0937 0.0807  79  PRO   A O   
586  C CB  . PRO   A 73  ? 0.3693 0.4125 0.3709 -0.0502 -0.0651 0.0518  79  PRO   A CB  
587  C CG  . PRO   A 73  ? 0.4008 0.4333 0.3787 -0.0557 -0.0607 0.0430  79  PRO   A CG  
588  C CD  . PRO   A 73  ? 0.3539 0.3914 0.3359 -0.0629 -0.0723 0.0479  79  PRO   A CD  
589  N N   A SER   A 74  ? 0.2991 0.3727 0.3813 -0.0386 -0.0732 0.0731  80  SER   A N   
590  N N   B SER   A 74  ? 0.2983 0.3719 0.3806 -0.0386 -0.0733 0.0732  80  SER   A N   
591  C CA  A SER   A 74  ? 0.2954 0.3784 0.4071 -0.0379 -0.0798 0.0876  80  SER   A CA  
592  C CA  B SER   A 74  ? 0.2936 0.3768 0.4059 -0.0378 -0.0798 0.0876  80  SER   A CA  
593  C C   A SER   A 74  ? 0.2885 0.3726 0.4201 -0.0276 -0.0673 0.0860  80  SER   A C   
594  C C   B SER   A 74  ? 0.2878 0.3718 0.4189 -0.0277 -0.0674 0.0860  80  SER   A C   
595  O O   A SER   A 74  ? 0.2892 0.3667 0.4112 -0.0216 -0.0554 0.0737  80  SER   A O   
596  O O   B SER   A 74  ? 0.2890 0.3662 0.4098 -0.0218 -0.0556 0.0736  80  SER   A O   
597  C CB  A SER   A 74  ? 0.3060 0.3988 0.4461 -0.0403 -0.0870 0.0973  80  SER   A CB  
598  C CB  B SER   A 74  ? 0.3015 0.3944 0.4439 -0.0390 -0.0850 0.0964  80  SER   A CB  
599  O OG  A SER   A 74  ? 0.3307 0.4249 0.4911 -0.0315 -0.0726 0.0915  80  SER   A OG  
600  O OG  B SER   A 74  ? 0.3344 0.4257 0.4606 -0.0486 -0.0959 0.0964  80  SER   A OG  
601  N N   . LEU   A 75  ? 0.2758 0.3673 0.4355 -0.0263 -0.0709 0.0993  81  LEU   A N   
602  C CA  . LEU   A 75  ? 0.2806 0.3713 0.4605 -0.0175 -0.0581 0.0984  81  LEU   A CA  
603  C C   . LEU   A 75  ? 0.2823 0.3742 0.4900 -0.0117 -0.0466 0.0978  81  LEU   A C   
604  O O   . LEU   A 75  ? 0.2858 0.3866 0.5225 -0.0136 -0.0520 0.1103  81  LEU   A O   
605  C CB  . LEU   A 75  ? 0.2810 0.3789 0.4823 -0.0193 -0.0665 0.1149  81  LEU   A CB  
606  C CG  . LEU   A 75  ? 0.3185 0.4145 0.5370 -0.0118 -0.0549 0.1151  81  LEU   A CG  
607  C CD1 . LEU   A 75  ? 0.3248 0.4106 0.5132 -0.0101 -0.0489 0.1015  81  LEU   A CD1 
608  C CD2 . LEU   A 75  ? 0.3192 0.4244 0.5642 -0.0141 -0.0647 0.1348  81  LEU   A CD2 
609  N N   . ILE   A 76  ? 0.2758 0.3568 0.4741 -0.0056 -0.0310 0.0841  82  ILE   A N   
610  C CA  . ILE   A 76  ? 0.2797 0.3550 0.4936 -0.0007 -0.0165 0.0807  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.2855 0.3478 0.5040 0.0055  0.0009  0.0743  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.2816 0.3359 0.4768 0.0059  0.0020  0.0648  82  ILE   A O   
613  C CB  . ILE   A 76  ? 0.3052 0.3744 0.4912 -0.0022 -0.0156 0.0687  82  ILE   A CB  
614  C CG1 . ILE   A 76  ? 0.3368 0.4167 0.5249 -0.0086 -0.0294 0.0756  82  ILE   A CG1 
615  C CG2 . ILE   A 76  ? 0.3053 0.3610 0.4931 0.0030  0.0029  0.0609  82  ILE   A CG2 
616  C CD1 . ILE   A 76  ? 0.3849 0.4593 0.5454 -0.0104 -0.0289 0.0643  82  ILE   A CD1 
617  N N   . PHE   A 77  ? 0.2835 0.3421 0.5335 0.0098  0.0156  0.0797  83  PHE   A N   
618  C CA  . PHE   A 77  ? 0.3116 0.3522 0.5619 0.0145  0.0352  0.0723  83  PHE   A CA  
619  C C   . PHE   A 77  ? 0.3135 0.3337 0.5254 0.0143  0.0446  0.0550  83  PHE   A C   
620  O O   . PHE   A 77  ? 0.3322 0.3485 0.5385 0.0142  0.0490  0.0523  83  PHE   A O   
621  C CB  . PHE   A 77  ? 0.3169 0.3551 0.6119 0.0190  0.0524  0.0828  83  PHE   A CB  
622  C CG  . PHE   A 77  ? 0.3547 0.3746 0.6522 0.0226  0.0714  0.0772  83  PHE   A CG  
623  C CD1 . PHE   A 77  ? 0.3755 0.4010 0.6797 0.0227  0.0656  0.0811  83  PHE   A CD1 
624  C CD2 . PHE   A 77  ? 0.3944 0.3884 0.6839 0.0250  0.0961  0.0673  83  PHE   A CD2 
625  C CE1 . PHE   A 77  ? 0.4006 0.4080 0.7068 0.0253  0.0835  0.0752  83  PHE   A CE1 
626  C CE2 . PHE   A 77  ? 0.4102 0.3835 0.6994 0.0268  0.1149  0.0615  83  PHE   A CE2 
627  C CZ  . PHE   A 77  ? 0.4105 0.3914 0.7094 0.0270  0.1081  0.0654  83  PHE   A CZ  
628  N N   . VAL   A 78  ? 0.3036 0.3107 0.4900 0.0136  0.0467  0.0444  84  VAL   A N   
629  C CA  . VAL   A 78  ? 0.3229 0.3096 0.4701 0.0116  0.0513  0.0294  84  VAL   A CA  
630  C C   . VAL   A 78  ? 0.3514 0.3119 0.4909 0.0122  0.0699  0.0218  84  VAL   A C   
631  O O   . VAL   A 78  ? 0.3478 0.3070 0.4965 0.0127  0.0713  0.0227  84  VAL   A O   
632  C CB  . VAL   A 78  ? 0.3188 0.3113 0.4399 0.0079  0.0336  0.0239  84  VAL   A CB  
633  C CG1 . VAL   A 78  ? 0.3365 0.3079 0.4205 0.0047  0.0352  0.0108  84  VAL   A CG1 
634  C CG2 . VAL   A 78  ? 0.3089 0.3211 0.4319 0.0063  0.0191  0.0296  84  VAL   A CG2 
635  N N   . GLU   A 79  ? 0.3845 0.3220 0.5061 0.0117  0.0855  0.0144  85  GLU   A N   
636  C CA  . GLU   A 79  ? 0.4139 0.3191 0.5200 0.0105  0.1061  0.0055  85  GLU   A CA  
637  C C   . GLU   A 79  ? 0.4297 0.3206 0.5024 0.0049  0.0975  -0.0051 85  GLU   A C   
638  O O   . GLU   A 79  ? 0.4232 0.3245 0.4775 0.0017  0.0771  -0.0076 85  GLU   A O   
639  C CB  . GLU   A 79  ? 0.4742 0.3532 0.5570 0.0094  0.1236  -0.0013 85  GLU   A CB  
640  C CG  . GLU   A 79  ? 0.5327 0.4193 0.6560 0.0153  0.1394  0.0094  85  GLU   A CG  
641  C CD  . GLU   A 79  ? 0.6339 0.5180 0.7990 0.0197  0.1580  0.0173  85  GLU   A CD  
642  O OE1 . GLU   A 79  ? 0.6805 0.5318 0.8296 0.0184  0.1803  0.0087  85  GLU   A OE1 
643  O OE2 . GLU   A 79  ? 0.6322 0.5457 0.8447 0.0236  0.1493  0.0323  85  GLU   A OE2 
644  N N   . ALA   A 80  ? 0.4428 0.3080 0.5095 0.0033  0.1142  -0.0111 86  ALA   A N   
645  C CA  . ALA   A 80  ? 0.4746 0.3222 0.5096 -0.0035 0.1066  -0.0214 86  ALA   A CA  
646  C C   . ALA   A 80  ? 0.5021 0.3300 0.4866 -0.0113 0.0969  -0.0317 86  ALA   A C   
647  O O   . ALA   A 80  ? 0.5119 0.3252 0.4782 -0.0119 0.1069  -0.0343 86  ALA   A O   
648  C CB  . ALA   A 80  ? 0.4891 0.3069 0.5230 -0.0050 0.1297  -0.0272 86  ALA   A CB  
649  N N   . SER   A 81  ? 0.5010 0.3305 0.4671 -0.0171 0.0766  -0.0356 87  SER   A N   
650  C CA  . SER   A 81  ? 0.5140 0.3265 0.4363 -0.0259 0.0622  -0.0429 87  SER   A CA  
651  C C   . SER   A 81  ? 0.5402 0.3360 0.4434 -0.0345 0.0512  -0.0495 87  SER   A C   
652  O O   . SER   A 81  ? 0.5486 0.3471 0.4734 -0.0324 0.0571  -0.0489 87  SER   A O   
653  C CB  . SER   A 81  ? 0.4867 0.3292 0.4185 -0.0235 0.0415  -0.0361 87  SER   A CB  
654  O OG  . SER   A 81  ? 0.4628 0.3293 0.4178 -0.0222 0.0254  -0.0312 87  SER   A OG  
655  N N   . GLU   A 82  ? 0.5589 0.3388 0.4249 -0.0445 0.0336  -0.0543 88  GLU   A N   
656  C CA  . GLU   A 82  ? 0.5786 0.3445 0.4312 -0.0537 0.0200  -0.0590 88  GLU   A CA  
657  C C   . GLU   A 82  ? 0.5283 0.3306 0.4242 -0.0482 0.0048  -0.0507 88  GLU   A C   
658  O O   . GLU   A 82  ? 0.5210 0.3170 0.4212 -0.0525 -0.0006 -0.0530 88  GLU   A O   
659  C CB  . GLU   A 82  ? 0.6429 0.3822 0.4476 -0.0674 0.0017  -0.0640 88  GLU   A CB  
660  C CG  . GLU   A 82  ? 0.6654 0.4304 0.4797 -0.0668 -0.0224 -0.0554 88  GLU   A CG  
661  C CD  . GLU   A 82  ? 0.7974 0.5394 0.5724 -0.0812 -0.0453 -0.0569 88  GLU   A CD  
662  O OE1 . GLU   A 82  ? 0.8372 0.5704 0.5865 -0.0839 -0.0483 -0.0558 88  GLU   A OE1 
663  O OE2 . GLU   A 82  ? 0.8032 0.5357 0.5741 -0.0903 -0.0612 -0.0582 88  GLU   A OE2 
664  N N   . TYR   A 83  ? 0.4843 0.3217 0.4117 -0.0388 0.0008  -0.0413 89  TYR   A N   
665  C CA  . TYR   A 83  ? 0.4602 0.3273 0.4221 -0.0344 -0.0118 -0.0335 89  TYR   A CA  
666  C C   . TYR   A 83  ? 0.4317 0.3187 0.4301 -0.0254 -0.0005 -0.0276 89  TYR   A C   
667  O O   . TYR   A 83  ? 0.4130 0.3149 0.4342 -0.0237 -0.0077 -0.0231 89  TYR   A O   
668  C CB  . TYR   A 83  ? 0.4645 0.3531 0.4329 -0.0320 -0.0246 -0.0272 89  TYR   A CB  
669  C CG  . TYR   A 83  ? 0.5107 0.3850 0.4524 -0.0412 -0.0413 -0.0294 89  TYR   A CG  
670  C CD1 . TYR   A 83  ? 0.5275 0.4000 0.4737 -0.0478 -0.0588 -0.0280 89  TYR   A CD1 
671  C CD2 . TYR   A 83  ? 0.5508 0.4124 0.4643 -0.0440 -0.0404 -0.0317 89  TYR   A CD2 
672  C CE1 . TYR   A 83  ? 0.5637 0.4238 0.4892 -0.0572 -0.0772 -0.0274 89  TYR   A CE1 
673  C CE2 . TYR   A 83  ? 0.5860 0.4335 0.4743 -0.0534 -0.0576 -0.0318 89  TYR   A CE2 
674  C CZ  . TYR   A 83  ? 0.6058 0.4526 0.5004 -0.0604 -0.0771 -0.0292 89  TYR   A CZ  
675  O OH  . TYR   A 83  ? 0.6649 0.4994 0.5389 -0.0704 -0.0971 -0.0266 89  TYR   A OH  
676  N N   . TYR   A 84  ? 0.4155 0.3033 0.4219 -0.0198 0.0165  -0.0259 90  TYR   A N   
677  C CA  . TYR   A 84  ? 0.3879 0.2941 0.4303 -0.0121 0.0257  -0.0178 90  TYR   A CA  
678  C C   . TYR   A 84  ? 0.4110 0.3014 0.4576 -0.0097 0.0480  -0.0193 90  TYR   A C   
679  O O   . TYR   A 84  ? 0.4222 0.2975 0.4502 -0.0109 0.0573  -0.0233 90  TYR   A O   
680  C CB  . TYR   A 84  ? 0.3478 0.2832 0.4099 -0.0062 0.0199  -0.0078 90  TYR   A CB  
681  C CG  . TYR   A 84  ? 0.3214 0.2729 0.3832 -0.0073 0.0027  -0.0050 90  TYR   A CG  
682  C CD1 . TYR   A 84  ? 0.3073 0.2726 0.3884 -0.0055 -0.0031 0.0004  90  TYR   A CD1 
683  C CD2 . TYR   A 84  ? 0.3308 0.2837 0.3758 -0.0094 -0.0052 -0.0066 90  TYR   A CD2 
684  C CE1 . TYR   A 84  ? 0.3011 0.2779 0.3837 -0.0063 -0.0147 0.0031  90  TYR   A CE1 
685  C CE2 . TYR   A 84  ? 0.3169 0.2834 0.3660 -0.0100 -0.0176 -0.0034 90  TYR   A CE2 
686  C CZ  . TYR   A 84  ? 0.3051 0.2833 0.3735 -0.0082 -0.0211 0.0016  90  TYR   A CZ  
687  O OH  . TYR   A 84  ? 0.2850 0.2733 0.3583 -0.0087 -0.0296 0.0048  90  TYR   A OH  
688  N N   . PRO   A 85  ? 0.4169 0.3123 0.4931 -0.0054 0.0586  -0.0140 91  PRO   A N   
689  C CA  . PRO   A 85  ? 0.4191 0.3048 0.5119 -0.0013 0.0815  -0.0115 91  PRO   A CA  
690  C C   . PRO   A 85  ? 0.4026 0.3126 0.5196 0.0048  0.0806  0.0001  91  PRO   A C   
691  O O   . PRO   A 85  ? 0.3778 0.3118 0.4979 0.0056  0.0625  0.0058  91  PRO   A O   
692  C CB  . PRO   A 85  ? 0.4232 0.3123 0.5468 0.0018  0.0895  -0.0065 91  PRO   A CB  
693  C CG  . PRO   A 85  ? 0.4161 0.3311 0.5511 0.0028  0.0687  -0.0002 91  PRO   A CG  
694  C CD  . PRO   A 85  ? 0.3977 0.3108 0.4991 -0.0029 0.0508  -0.0077 91  PRO   A CD  
695  N N   . ALA   A 86  ? 0.3993 0.3024 0.5361 0.0087  0.1006  0.0044  92  ALA   A N   
696  C CA  . ALA   A 86  ? 0.3935 0.3198 0.5579 0.0135  0.0980  0.0168  92  ALA   A CA  
697  C C   . ALA   A 86  ? 0.3670 0.3242 0.5652 0.0166  0.0836  0.0312  92  ALA   A C   
698  O O   . ALA   A 86  ? 0.3602 0.3182 0.5782 0.0183  0.0879  0.0353  92  ALA   A O   
699  C CB  . ALA   A 86  ? 0.3992 0.3125 0.5867 0.0172  0.1230  0.0207  92  ALA   A CB  
700  N N   . ARG   A 87  ? 0.3434 0.3226 0.5400 0.0160  0.0652  0.0370  93  ARG   A N   
701  C CA  . ARG   A 87  ? 0.3227 0.3265 0.5388 0.0166  0.0495  0.0494  93  ARG   A CA  
702  C C   . ARG   A 87  ? 0.3250 0.3474 0.5432 0.0152  0.0355  0.0573  93  ARG   A C   
703  O O   . ARG   A 87  ? 0.3390 0.3563 0.5438 0.0144  0.0379  0.0519  93  ARG   A O   
704  C CB  . ARG   A 87  ? 0.3286 0.3319 0.5228 0.0140  0.0385  0.0427  93  ARG   A CB  
705  C CG  . ARG   A 87  ? 0.3358 0.3424 0.4993 0.0104  0.0246  0.0359  93  ARG   A CG  
706  C CD  . ARG   A 87  ? 0.3640 0.3584 0.5033 0.0073  0.0206  0.0247  93  ARG   A CD  
707  N NE  . ARG   A 87  ? 0.3218 0.3253 0.4455 0.0049  0.0067  0.0235  93  ARG   A NE  
708  C CZ  . ARG   A 87  ? 0.3378 0.3395 0.4430 0.0028  0.0027  0.0189  93  ARG   A CZ  
709  N NH1 . ARG   A 87  ? 0.3107 0.3018 0.4082 0.0029  0.0109  0.0149  93  ARG   A NH1 
710  N NH2 . ARG   A 87  ? 0.3101 0.3188 0.4053 0.0009  -0.0075 0.0185  93  ARG   A NH2 
711  N N   . TYR   A 88  ? 0.3015 0.3429 0.5324 0.0139  0.0208  0.0694  94  TYR   A N   
712  C CA  . TYR   A 88  ? 0.3063 0.3608 0.5298 0.0102  0.0062  0.0745  94  TYR   A CA  
713  C C   . TYR   A 88  ? 0.2963 0.3488 0.4843 0.0068  -0.0034 0.0649  94  TYR   A C   
714  O O   . TYR   A 88  ? 0.3042 0.3557 0.4865 0.0067  -0.0059 0.0639  94  TYR   A O   
715  C CB  . TYR   A 88  ? 0.3087 0.3802 0.5575 0.0081  -0.0060 0.0928  94  TYR   A CB  
716  C CG  . TYR   A 88  ? 0.3068 0.3834 0.5983 0.0109  0.0014  0.1055  94  TYR   A CG  
717  C CD1 . TYR   A 88  ? 0.3131 0.3962 0.6167 0.0090  -0.0024 0.1112  94  TYR   A CD1 
718  C CD2 . TYR   A 88  ? 0.3274 0.4011 0.6508 0.0157  0.0143  0.1120  94  TYR   A CD2 
719  C CE1 . TYR   A 88  ? 0.3163 0.4043 0.6662 0.0119  0.0055  0.1246  94  TYR   A CE1 
720  C CE2 . TYR   A 88  ? 0.3214 0.3991 0.6907 0.0189  0.0238  0.1251  94  TYR   A CE2 
721  C CZ  . TYR   A 88  ? 0.3282 0.4131 0.7119 0.0172  0.0196  0.1316  94  TYR   A CZ  
722  O OH  . TYR   A 88  ? 0.3338 0.4231 0.7696 0.0205  0.0298  0.1462  94  TYR   A OH  
723  N N   . GLN   A 89  ? 0.2698 0.3212 0.4374 0.0044  -0.0073 0.0584  95  GLN   A N   
724  C CA  . GLN   A 89  ? 0.2712 0.3211 0.4106 0.0013  -0.0150 0.0510  95  GLN   A CA  
725  C C   . GLN   A 89  ? 0.2670 0.3272 0.4016 -0.0036 -0.0267 0.0586  95  GLN   A C   
726  O O   . GLN   A 89  ? 0.2724 0.3378 0.4144 -0.0053 -0.0294 0.0630  95  GLN   A O   
727  C CB  . GLN   A 89  ? 0.2758 0.3151 0.3944 0.0013  -0.0110 0.0387  95  GLN   A CB  
728  C CG  . GLN   A 89  ? 0.2802 0.3195 0.3768 -0.0018 -0.0185 0.0334  95  GLN   A CG  
729  C CD  . GLN   A 89  ? 0.2867 0.3143 0.3666 -0.0018 -0.0160 0.0229  95  GLN   A CD  
730  O OE1 . GLN   A 89  ? 0.2753 0.2915 0.3531 -0.0007 -0.0108 0.0180  95  GLN   A OE1 
731  N NE2 . GLN   A 89  ? 0.2718 0.3001 0.3383 -0.0039 -0.0202 0.0198  95  GLN   A NE2 
732  N N   . SER   A 90  ? 0.2545 0.3151 0.3748 -0.0068 -0.0329 0.0597  96  SER   A N   
733  C CA  . SER   A 90  ? 0.2644 0.3289 0.3723 -0.0135 -0.0432 0.0662  96  SER   A CA  
734  C C   . SER   A 90  ? 0.2607 0.3193 0.3427 -0.0169 -0.0433 0.0567  96  SER   A C   
735  O O   . SER   A 90  ? 0.2478 0.3008 0.3234 -0.0136 -0.0368 0.0468  96  SER   A O   
736  C CB  . SER   A 90  ? 0.3065 0.3702 0.4098 -0.0161 -0.0473 0.0735  96  SER   A CB  
737  O OG  . SER   A 90  ? 0.3333 0.3890 0.4241 -0.0140 -0.0408 0.0652  96  SER   A OG  
738  N N   . HIS   A 91  ? 0.2530 0.3123 0.3219 -0.0241 -0.0513 0.0608  97  HIS   A N   
739  C CA  . HIS   A 91  ? 0.2600 0.3123 0.3051 -0.0283 -0.0501 0.0528  97  HIS   A CA  
740  C C   . HIS   A 91  ? 0.2512 0.3043 0.3011 -0.0238 -0.0443 0.0443  97  HIS   A C   
741  O O   . HIS   A 91  ? 0.2445 0.2914 0.2814 -0.0235 -0.0393 0.0361  97  HIS   A O   
742  C CB  . HIS   A 91  ? 0.2815 0.3237 0.3095 -0.0287 -0.0440 0.0480  97  HIS   A CB  
743  C CG  . HIS   A 91  ? 0.3308 0.3681 0.3478 -0.0339 -0.0477 0.0560  97  HIS   A CG  
744  N ND1 . HIS   A 91  ? 0.3844 0.4101 0.3726 -0.0432 -0.0500 0.0570  97  HIS   A ND1 
745  C CD2 . HIS   A 91  ? 0.3353 0.3751 0.3639 -0.0313 -0.0484 0.0629  97  HIS   A CD2 
746  C CE1 . HIS   A 91  ? 0.3947 0.4156 0.3753 -0.0465 -0.0530 0.0651  97  HIS   A CE1 
747  N NE2 . HIS   A 91  ? 0.3664 0.3968 0.3728 -0.0390 -0.0522 0.0692  97  HIS   A NE2 
748  N N   . LEU   A 92  ? 0.2476 0.3069 0.3172 -0.0205 -0.0440 0.0473  98  LEU   A N   
749  C CA  . LEU   A 92  ? 0.2506 0.3076 0.3222 -0.0165 -0.0371 0.0400  98  LEU   A CA  
750  C C   . LEU   A 92  ? 0.2472 0.3084 0.3206 -0.0204 -0.0410 0.0423  98  LEU   A C   
751  O O   . LEU   A 92  ? 0.2484 0.3168 0.3360 -0.0240 -0.0485 0.0522  98  LEU   A O   
752  C CB  . LEU   A 92  ? 0.2604 0.3164 0.3507 -0.0104 -0.0297 0.0407  98  LEU   A CB  
753  C CG  . LEU   A 92  ? 0.2869 0.3348 0.3741 -0.0067 -0.0206 0.0332  98  LEU   A CG  
754  C CD1 . LEU   A 92  ? 0.2901 0.3295 0.3561 -0.0066 -0.0199 0.0238  98  LEU   A CD1 
755  C CD2 . LEU   A 92  ? 0.3024 0.3442 0.4055 -0.0021 -0.0103 0.0342  98  LEU   A CD2 
756  N N   . MET   A 93  ? 0.2306 0.2873 0.2915 -0.0202 -0.0369 0.0342  99  MET   A N   
757  C CA  . MET   A 93  ? 0.2318 0.2912 0.2944 -0.0236 -0.0390 0.0351  99  MET   A CA  
758  C C   . MET   A 93  ? 0.2453 0.3020 0.3169 -0.0175 -0.0294 0.0314  99  MET   A C   
759  O O   . MET   A 93  ? 0.2521 0.3010 0.3127 -0.0136 -0.0231 0.0244  99  MET   A O   
760  C CB  . MET   A 93  ? 0.2379 0.2917 0.2776 -0.0285 -0.0397 0.0288  99  MET   A CB  
761  C CG  . MET   A 93  ? 0.2587 0.3088 0.2825 -0.0356 -0.0457 0.0313  99  MET   A CG  
762  S SD  . MET   A 93  ? 0.3362 0.3742 0.3341 -0.0403 -0.0397 0.0230  99  MET   A SD  
763  C CE  . MET   A 93  ? 0.3092 0.3451 0.3124 -0.0316 -0.0305 0.0173  99  MET   A CE  
764  N N   . LEU   A 94  ? 0.2382 0.2995 0.3294 -0.0172 -0.0281 0.0367  100 LEU   A N   
765  C CA  . LEU   A 94  ? 0.2474 0.3020 0.3441 -0.0115 -0.0157 0.0332  100 LEU   A CA  
766  C C   . LEU   A 94  ? 0.2448 0.2999 0.3385 -0.0136 -0.0151 0.0310  100 LEU   A C   
767  O O   . LEU   A 94  ? 0.2461 0.3089 0.3448 -0.0196 -0.0244 0.0353  100 LEU   A O   
768  C CB  . LEU   A 94  ? 0.2594 0.3158 0.3868 -0.0078 -0.0085 0.0412  100 LEU   A CB  
769  C CG  . LEU   A 94  ? 0.2971 0.3509 0.4325 -0.0046 -0.0049 0.0435  100 LEU   A CG  
770  C CD1 . LEU   A 94  ? 0.3167 0.3713 0.4880 -0.0008 0.0052  0.0525  100 LEU   A CD1 
771  C CD2 . LEU   A 94  ? 0.3208 0.3597 0.4307 -0.0015 0.0029  0.0326  100 LEU   A CD2 
772  N N   . ALA   A 95  ? 0.2403 0.2854 0.3247 -0.0094 -0.0044 0.0249  101 ALA   A N   
773  C CA  . ALA   A 95  ? 0.2497 0.2936 0.3331 -0.0099 -0.0006 0.0230  101 ALA   A CA  
774  C C   . ALA   A 95  ? 0.2515 0.2827 0.3364 -0.0041 0.0150  0.0212  101 ALA   A C   
775  O O   . ALA   A 95  ? 0.2598 0.2797 0.3364 -0.0009 0.0221  0.0187  101 ALA   A O   
776  C CB  . ALA   A 95  ? 0.2594 0.2999 0.3182 -0.0120 -0.0037 0.0160  101 ALA   A CB  
777  N N   . VAL   A 96  ? 0.2358 0.2666 0.3304 -0.0036 0.0211  0.0226  102 VAL   A N   
778  C CA  . VAL   A 96  ? 0.2474 0.2622 0.3377 0.0012  0.0380  0.0204  102 VAL   A CA  
779  C C   . VAL   A 96  ? 0.2856 0.2895 0.3425 0.0010  0.0382  0.0128  102 VAL   A C   
780  O O   . VAL   A 96  ? 0.2905 0.3004 0.3437 -0.0013 0.0329  0.0117  102 VAL   A O   
781  C CB  . VAL   A 96  ? 0.2496 0.2689 0.3694 0.0023  0.0456  0.0266  102 VAL   A CB  
782  C CG1 . VAL   A 96  ? 0.2678 0.2666 0.3794 0.0072  0.0664  0.0239  102 VAL   A CG1 
783  C CG2 . VAL   A 96  ? 0.2288 0.2594 0.3869 0.0021  0.0434  0.0369  102 VAL   A CG2 
784  N N   . GLY   A 97  ? 0.3029 0.2898 0.3362 0.0024  0.0434  0.0083  103 GLY   A N   
785  C CA  . GLY   A 97  ? 0.3373 0.3132 0.3400 0.0010  0.0404  0.0034  103 GLY   A CA  
786  C C   . GLY   A 97  ? 0.3572 0.3118 0.3332 0.0005  0.0441  -0.0007 103 GLY   A C   
787  O O   . GLY   A 97  ? 0.3557 0.3057 0.3369 0.0014  0.0487  -0.0009 103 GLY   A O   
788  N N   . HIS   A 98  ? 0.3675 0.3076 0.3144 -0.0017 0.0416  -0.0032 104 HIS   A N   
789  C CA  . HIS   A 98  ? 0.3851 0.3006 0.3002 -0.0046 0.0429  -0.0071 104 HIS   A CA  
790  C C   . HIS   A 98  ? 0.3587 0.2802 0.2704 -0.0078 0.0270  -0.0079 104 HIS   A C   
791  O O   . HIS   A 98  ? 0.3485 0.2871 0.2709 -0.0086 0.0141  -0.0055 104 HIS   A O   
792  C CB  . HIS   A 98  ? 0.4193 0.3144 0.3016 -0.0076 0.0436  -0.0077 104 HIS   A CB  
793  C CG  . HIS   A 98  ? 0.4833 0.3484 0.3260 -0.0132 0.0429  -0.0115 104 HIS   A CG  
794  N ND1 . HIS   A 98  ? 0.5176 0.3578 0.3450 -0.0134 0.0606  -0.0160 104 HIS   A ND1 
795  C CD2 . HIS   A 98  ? 0.5115 0.3676 0.3294 -0.0196 0.0261  -0.0110 104 HIS   A CD2 
796  C CE1 . HIS   A 98  ? 0.5503 0.3651 0.3387 -0.0208 0.0538  -0.0195 104 HIS   A CE1 
797  N NE2 . HIS   A 98  ? 0.5458 0.3700 0.3280 -0.0251 0.0313  -0.0160 104 HIS   A NE2 
798  N N   . SER   A 99  ? 0.3601 0.2663 0.2592 -0.0096 0.0299  -0.0113 105 SER   A N   
799  C CA  . SER   A 99  ? 0.3690 0.2769 0.2630 -0.0133 0.0155  -0.0122 105 SER   A CA  
800  C C   . SER   A 99  ? 0.4246 0.3028 0.2886 -0.0178 0.0206  -0.0175 105 SER   A C   
801  O O   . SER   A 99  ? 0.4512 0.3121 0.3086 -0.0163 0.0391  -0.0205 105 SER   A O   
802  C CB  . SER   A 99  ? 0.3592 0.2917 0.2858 -0.0101 0.0112  -0.0097 105 SER   A CB  
803  O OG  . SER   A 99  ? 0.3754 0.3054 0.3147 -0.0073 0.0236  -0.0103 105 SER   A OG  
804  N N   . GLU   A 100 ? 0.4273 0.2963 0.2714 -0.0243 0.0049  -0.0183 106 GLU   A N   
805  C CA  . GLU   A 100 ? 0.4540 0.2949 0.2678 -0.0311 0.0046  -0.0236 106 GLU   A CA  
806  C C   . GLU   A 100 ? 0.4552 0.3101 0.2862 -0.0328 -0.0107 -0.0224 106 GLU   A C   
807  O O   . GLU   A 100 ? 0.4335 0.3163 0.2941 -0.0295 -0.0214 -0.0171 106 GLU   A O   
808  C CB  . GLU   A 100 ? 0.5128 0.3242 0.2808 -0.0401 -0.0026 -0.0245 106 GLU   A CB  
809  C CG  . GLU   A 100 ? 0.5653 0.3632 0.3183 -0.0375 0.0146  -0.0251 106 GLU   A CG  
810  C CD  . GLU   A 100 ? 0.6352 0.4012 0.3391 -0.0464 0.0096  -0.0250 106 GLU   A CD  
811  O OE1 . GLU   A 100 ? 0.6415 0.3840 0.3115 -0.0568 -0.0034 -0.0270 106 GLU   A OE1 
812  O OE2 . GLU   A 100 ? 0.6339 0.3977 0.3326 -0.0438 0.0175  -0.0224 106 GLU   A OE2 
813  N N   . PRO   A 101 ? 0.4827 0.3181 0.2981 -0.0375 -0.0091 -0.0276 107 PRO   A N   
814  C CA  . PRO   A 101 ? 0.4745 0.3237 0.3103 -0.0384 -0.0216 -0.0263 107 PRO   A CA  
815  C C   . PRO   A 101 ? 0.4509 0.3171 0.2996 -0.0410 -0.0443 -0.0196 107 PRO   A C   
816  O O   . PRO   A 101 ? 0.4330 0.3253 0.3163 -0.0361 -0.0484 -0.0154 107 PRO   A O   
817  C CB  . PRO   A 101 ? 0.5139 0.3304 0.3186 -0.0463 -0.0184 -0.0337 107 PRO   A CB  
818  C CG  . PRO   A 101 ? 0.5364 0.3278 0.3185 -0.0452 0.0055  -0.0393 107 PRO   A CG  
819  C CD  . PRO   A 101 ? 0.5034 0.3012 0.2824 -0.0422 0.0071  -0.0354 107 PRO   A CD  
820  N N   . GLY   A 102 ? 0.4475 0.2987 0.2705 -0.0486 -0.0573 -0.0174 108 GLY   A N   
821  C CA  . GLY   A 102 ? 0.4403 0.3051 0.2787 -0.0517 -0.0786 -0.0089 108 GLY   A CA  
822  C C   . GLY   A 102 ? 0.4145 0.3073 0.2845 -0.0439 -0.0766 -0.0026 108 GLY   A C   
823  O O   . GLY   A 102 ? 0.4159 0.3216 0.3063 -0.0452 -0.0905 0.0053  108 GLY   A O   
824  N N   . ASP   A 103 ? 0.3868 0.2886 0.2636 -0.0363 -0.0589 -0.0054 109 ASP   A N   
825  C CA  . ASP   A 103 ? 0.3621 0.2884 0.2668 -0.0301 -0.0562 -0.0008 109 ASP   A CA  
826  C C   . ASP   A 103 ? 0.3216 0.2695 0.2590 -0.0257 -0.0554 0.0006  109 ASP   A C   
827  O O   . ASP   A 103 ? 0.3015 0.2663 0.2598 -0.0225 -0.0543 0.0043  109 ASP   A O   
828  C CB  . ASP   A 103 ? 0.3600 0.2879 0.2617 -0.0250 -0.0401 -0.0034 109 ASP   A CB  
829  C CG  . ASP   A 103 ? 0.3960 0.3044 0.2683 -0.0286 -0.0397 -0.0031 109 ASP   A CG  
830  O OD1 . ASP   A 103 ? 0.3887 0.2936 0.2546 -0.0333 -0.0538 0.0022  109 ASP   A OD1 
831  O OD2 . ASP   A 103 ? 0.4064 0.3021 0.2635 -0.0268 -0.0249 -0.0072 109 ASP   A OD2 
832  N N   . CYS   A 104 ? 0.3160 0.2612 0.2563 -0.0263 -0.0553 -0.0022 110 CYS   A N   
833  C CA  . CYS   A 104 ? 0.2876 0.2511 0.2562 -0.0225 -0.0542 0.0000  110 CYS   A CA  
834  C C   . CYS   A 104 ? 0.2941 0.2679 0.2825 -0.0235 -0.0639 0.0065  110 CYS   A C   
835  O O   . CYS   A 104 ? 0.3296 0.2950 0.3136 -0.0287 -0.0766 0.0099  110 CYS   A O   
836  C CB  . CYS   A 104 ? 0.3022 0.2590 0.2706 -0.0236 -0.0542 -0.0030 110 CYS   A CB  
837  S SG  . CYS   A 104 ? 0.3478 0.2975 0.3081 -0.0201 -0.0374 -0.0084 110 CYS   A SG  
838  N N   . GLY   A 105 ? 0.2700 0.2593 0.2796 -0.0196 -0.0580 0.0089  111 GLY   A N   
839  C CA  . GLY   A 105 ? 0.2796 0.2765 0.3113 -0.0199 -0.0622 0.0153  111 GLY   A CA  
840  C C   . GLY   A 105 ? 0.2906 0.2922 0.3248 -0.0187 -0.0574 0.0173  111 GLY   A C   
841  O O   . GLY   A 105 ? 0.2871 0.2954 0.3423 -0.0178 -0.0544 0.0219  111 GLY   A O   
842  N N   . GLY   A 106 ? 0.2774 0.2741 0.2917 -0.0186 -0.0547 0.0141  112 GLY   A N   
843  C CA  . GLY   A 106 ? 0.2663 0.2674 0.2834 -0.0173 -0.0490 0.0155  112 GLY   A CA  
844  C C   . GLY   A 106 ? 0.2583 0.2693 0.2863 -0.0149 -0.0377 0.0137  112 GLY   A C   
845  O O   . GLY   A 106 ? 0.2560 0.2695 0.2793 -0.0140 -0.0335 0.0101  112 GLY   A O   
846  N N   . ILE   A 107 ? 0.2476 0.2623 0.2894 -0.0148 -0.0326 0.0167  113 ILE   A N   
847  C CA  . ILE   A 107 ? 0.2538 0.2721 0.2994 -0.0148 -0.0215 0.0142  113 ILE   A CA  
848  C C   . ILE   A 107 ? 0.2478 0.2672 0.2801 -0.0153 -0.0160 0.0099  113 ILE   A C   
849  O O   . ILE   A 107 ? 0.2649 0.2832 0.2943 -0.0149 -0.0161 0.0104  113 ILE   A O   
850  C CB  . ILE   A 107 ? 0.2742 0.2919 0.3409 -0.0151 -0.0145 0.0187  113 ILE   A CB  
851  C CG1 . ILE   A 107 ? 0.2792 0.2968 0.3641 -0.0147 -0.0179 0.0233  113 ILE   A CG1 
852  C CG2 . ILE   A 107 ? 0.2871 0.3021 0.3487 -0.0170 -0.0003 0.0147  113 ILE   A CG2 
853  C CD1 . ILE   A 107 ? 0.3084 0.3248 0.4230 -0.0143 -0.0120 0.0307  113 ILE   A CD1 
854  N N   . LEU   A 108 ? 0.2328 0.2540 0.2584 -0.0169 -0.0120 0.0069  114 LEU   A N   
855  C CA  . LEU   A 108 ? 0.2453 0.2675 0.2620 -0.0194 -0.0079 0.0039  114 LEU   A CA  
856  C C   . LEU   A 108 ? 0.2626 0.2796 0.2784 -0.0235 0.0011  0.0026  114 LEU   A C   
857  O O   . LEU   A 108 ? 0.2627 0.2760 0.2782 -0.0250 0.0041  0.0032  114 LEU   A O   
858  C CB  . LEU   A 108 ? 0.2389 0.2647 0.2496 -0.0202 -0.0119 0.0035  114 LEU   A CB  
859  C CG  . LEU   A 108 ? 0.2786 0.3060 0.2830 -0.0248 -0.0110 0.0024  114 LEU   A CG  
860  C CD1 . LEU   A 108 ? 0.2814 0.3106 0.2880 -0.0234 -0.0098 0.0015  114 LEU   A CD1 
861  C CD2 . LEU   A 108 ? 0.2887 0.3203 0.2930 -0.0263 -0.0170 0.0053  114 LEU   A CD2 
862  N N   . ARG   A 109 ? 0.2697 0.2840 0.2843 -0.0255 0.0073  0.0008  115 ARG   A N   
863  C CA  . ARG   A 109 ? 0.2965 0.3013 0.3070 -0.0303 0.0186  -0.0017 115 ARG   A CA  
864  C C   . ARG   A 109 ? 0.2951 0.2962 0.2916 -0.0362 0.0210  -0.0060 115 ARG   A C   
865  O O   . ARG   A 109 ? 0.2848 0.2924 0.2831 -0.0349 0.0163  -0.0061 115 ARG   A O   
866  C CB  . ARG   A 109 ? 0.3330 0.3340 0.3619 -0.0277 0.0276  0.0012  115 ARG   A CB  
867  C CG  . ARG   A 109 ? 0.4291 0.4361 0.4700 -0.0236 0.0235  0.0046  115 ARG   A CG  
868  C CD  . ARG   A 109 ? 0.4979 0.5015 0.5630 -0.0218 0.0316  0.0103  115 ARG   A CD  
869  N NE  . ARG   A 109 ? 0.5478 0.5565 0.6301 -0.0181 0.0217  0.0176  115 ARG   A NE  
870  C CZ  . ARG   A 109 ? 0.5478 0.5539 0.6485 -0.0175 0.0260  0.0219  115 ARG   A CZ  
871  N NH1 . ARG   A 109 ? 0.5280 0.5243 0.6295 -0.0199 0.0427  0.0190  115 ARG   A NH1 
872  N NH2 . ARG   A 109 ? 0.5073 0.5184 0.6249 -0.0153 0.0140  0.0292  115 ARG   A NH2 
873  N N   . CYS   A 110 ? 0.3095 0.2980 0.2905 -0.0436 0.0286  -0.0095 116 CYS   A N   
874  C CA  . CYS   A 110 ? 0.3440 0.3247 0.3087 -0.0518 0.0310  -0.0141 116 CYS   A CA  
875  C C   . CYS   A 110 ? 0.3796 0.3426 0.3407 -0.0558 0.0498  -0.0182 116 CYS   A C   
876  O O   . CYS   A 110 ? 0.3660 0.3260 0.3427 -0.0509 0.0599  -0.0158 116 CYS   A O   
877  C CB  . CYS   A 110 ? 0.3787 0.3546 0.3210 -0.0602 0.0223  -0.0145 116 CYS   A CB  
878  S SG  . CYS   A 110 ? 0.3909 0.3471 0.3131 -0.0658 0.0326  -0.0159 116 CYS   A SG  
879  N N   . GLN   A 111 ? 0.4334 0.3830 0.3750 -0.0653 0.0551  -0.0240 117 GLN   A N   
880  C CA  . GLN   A 111 ? 0.4793 0.4076 0.4143 -0.0703 0.0761  -0.0290 117 GLN   A CA  
881  C C   . GLN   A 111 ? 0.4970 0.4068 0.4196 -0.0732 0.0892  -0.0298 117 GLN   A C   
882  O O   . GLN   A 111 ? 0.5278 0.4205 0.4547 -0.0742 0.1106  -0.0322 117 GLN   A O   
883  C CB  . GLN   A 111 ? 0.5391 0.4524 0.4477 -0.0827 0.0777  -0.0362 117 GLN   A CB  
884  C CG  . GLN   A 111 ? 0.6201 0.5249 0.4949 -0.0942 0.0643  -0.0378 117 GLN   A CG  
885  C CD  . GLN   A 111 ? 0.7303 0.6200 0.5788 -0.1084 0.0616  -0.0439 117 GLN   A CD  
886  O OE1 . GLN   A 111 ? 0.7493 0.6507 0.5969 -0.1124 0.0422  -0.0413 117 GLN   A OE1 
887  N NE2 . GLN   A 111 ? 0.7729 0.6345 0.6004 -0.1170 0.0815  -0.0518 117 GLN   A NE2 
888  N N   . HIS   A 112 ? 0.4765 0.3889 0.3872 -0.0741 0.0787  -0.0272 118 HIS   A N   
889  C CA  . HIS   A 112 ? 0.4765 0.3695 0.3745 -0.0769 0.0927  -0.0277 118 HIS   A CA  
890  C C   . HIS   A 112 ? 0.4600 0.3646 0.3912 -0.0654 0.0958  -0.0208 118 HIS   A C   
891  O O   . HIS   A 112 ? 0.4720 0.3606 0.4007 -0.0662 0.1110  -0.0203 118 HIS   A O   
892  C CB  . HIS   A 112 ? 0.4998 0.3824 0.3600 -0.0871 0.0820  -0.0287 118 HIS   A CB  
893  C CG  . HIS   A 112 ? 0.5398 0.4098 0.3667 -0.1008 0.0751  -0.0340 118 HIS   A CG  
894  N ND1 . HIS   A 112 ? 0.5446 0.4334 0.3735 -0.1023 0.0516  -0.0308 118 HIS   A ND1 
895  C CD2 . HIS   A 112 ? 0.5791 0.4176 0.3703 -0.1142 0.0889  -0.0419 118 HIS   A CD2 
896  C CE1 . HIS   A 112 ? 0.5826 0.4538 0.3805 -0.1165 0.0490  -0.0358 118 HIS   A CE1 
897  N NE2 . HIS   A 112 ? 0.6028 0.4422 0.3740 -0.1248 0.0708  -0.0433 118 HIS   A NE2 
898  N N   . GLY   A 113 ? 0.4169 0.3463 0.3778 -0.0557 0.0823  -0.0154 119 GLY   A N   
899  C CA  . GLY   A 113 ? 0.3889 0.3294 0.3808 -0.0464 0.0811  -0.0084 119 GLY   A CA  
900  C C   . GLY   A 113 ? 0.3583 0.3197 0.3563 -0.0412 0.0593  -0.0047 119 GLY   A C   
901  O O   . GLY   A 113 ? 0.3538 0.3250 0.3437 -0.0418 0.0470  -0.0062 119 GLY   A O   
902  N N   . VAL   A 114 ? 0.3324 0.2992 0.3464 -0.0361 0.0562  0.0002  120 VAL   A N   
903  C CA  . VAL   A 114 ? 0.3192 0.3023 0.3391 -0.0314 0.0380  0.0033  120 VAL   A CA  
904  C C   . VAL   A 114 ? 0.3143 0.2974 0.3108 -0.0355 0.0304  0.0014  120 VAL   A C   
905  O O   . VAL   A 114 ? 0.3296 0.3007 0.3113 -0.0400 0.0372  0.0009  120 VAL   A O   
906  C CB  . VAL   A 114 ? 0.3199 0.3069 0.3656 -0.0260 0.0372  0.0092  120 VAL   A CB  
907  C CG1 . VAL   A 114 ? 0.3209 0.3204 0.3684 -0.0226 0.0201  0.0110  120 VAL   A CG1 
908  C CG2 . VAL   A 114 ? 0.3304 0.3186 0.4049 -0.0227 0.0420  0.0140  120 VAL   A CG2 
909  N N   . VAL   A 115 ? 0.2922 0.2872 0.2860 -0.0343 0.0170  0.0015  121 VAL   A N   
910  C CA  . VAL   A 115 ? 0.2879 0.2862 0.2674 -0.0376 0.0073  0.0023  121 VAL   A CA  
911  C C   . VAL   A 115 ? 0.2842 0.2918 0.2759 -0.0319 -0.0007 0.0061  121 VAL   A C   
912  O O   . VAL   A 115 ? 0.2921 0.2993 0.2770 -0.0339 -0.0045 0.0086  121 VAL   A O   
913  C CB  . VAL   A 115 ? 0.3010 0.3060 0.2765 -0.0395 -0.0001 0.0012  121 VAL   A CB  
914  C CG1 . VAL   A 115 ? 0.2962 0.3083 0.2681 -0.0416 -0.0118 0.0051  121 VAL   A CG1 
915  C CG2 . VAL   A 115 ? 0.3102 0.3050 0.2721 -0.0464 0.0069  -0.0030 121 VAL   A CG2 
916  N N   . GLY   A 116 ? 0.2661 0.2807 0.2741 -0.0258 -0.0041 0.0068  122 GLY   A N   
917  C CA  . GLY   A 116 ? 0.2663 0.2865 0.2834 -0.0215 -0.0110 0.0091  122 GLY   A CA  
918  C C   . GLY   A 116 ? 0.2552 0.2778 0.2822 -0.0175 -0.0153 0.0090  122 GLY   A C   
919  O O   . GLY   A 116 ? 0.2550 0.2760 0.2859 -0.0173 -0.0131 0.0088  122 GLY   A O   
920  N N   . ILE   A 117 ? 0.2468 0.2711 0.2770 -0.0150 -0.0214 0.0096  123 ILE   A N   
921  C CA  . ILE   A 117 ? 0.2447 0.2662 0.2767 -0.0134 -0.0271 0.0093  123 ILE   A CA  
922  C C   . ILE   A 117 ? 0.2424 0.2623 0.2656 -0.0122 -0.0291 0.0071  123 ILE   A C   
923  O O   . ILE   A 117 ? 0.2303 0.2529 0.2546 -0.0116 -0.0278 0.0075  123 ILE   A O   
924  C CB  . ILE   A 117 ? 0.2685 0.2877 0.3130 -0.0131 -0.0318 0.0119  123 ILE   A CB  
925  C CG1 . ILE   A 117 ? 0.2895 0.3101 0.3377 -0.0124 -0.0305 0.0124  123 ILE   A CG1 
926  C CG2 . ILE   A 117 ? 0.3005 0.3195 0.3605 -0.0137 -0.0289 0.0157  123 ILE   A CG2 
927  C CD1 . ILE   A 117 ? 0.3083 0.3259 0.3702 -0.0124 -0.0367 0.0147  123 ILE   A CD1 
928  N N   . VAL   A 118 ? 0.2461 0.2594 0.2604 -0.0122 -0.0314 0.0056  124 VAL   A N   
929  C CA  . VAL   A 118 ? 0.2372 0.2437 0.2415 -0.0112 -0.0291 0.0030  124 VAL   A CA  
930  C C   . VAL   A 118 ? 0.2368 0.2391 0.2434 -0.0112 -0.0312 0.0024  124 VAL   A C   
931  O O   . VAL   A 118 ? 0.2460 0.2454 0.2554 -0.0129 -0.0379 0.0032  124 VAL   A O   
932  C CB  . VAL   A 118 ? 0.2496 0.2439 0.2379 -0.0126 -0.0309 0.0014  124 VAL   A CB  
933  C CG1 . VAL   A 118 ? 0.2735 0.2545 0.2479 -0.0123 -0.0251 -0.0021 124 VAL   A CG1 
934  C CG2 . VAL   A 118 ? 0.2542 0.2524 0.2420 -0.0122 -0.0282 0.0024  124 VAL   A CG2 
935  N N   . SER   A 119 ? 0.2344 0.2368 0.2436 -0.0094 -0.0255 0.0020  125 SER   A N   
936  C CA  . SER   A 119 ? 0.2470 0.2458 0.2609 -0.0090 -0.0253 0.0017  125 SER   A CA  
937  C C   . SER   A 119 ? 0.2693 0.2566 0.2777 -0.0079 -0.0164 -0.0009 125 SER   A C   
938  O O   . SER   A 119 ? 0.3008 0.2771 0.3052 -0.0088 -0.0151 -0.0035 125 SER   A O   
939  C CB  . SER   A 119 ? 0.2594 0.2712 0.2896 -0.0077 -0.0254 0.0063  125 SER   A CB  
940  O OG  . SER   A 119 ? 0.2714 0.2809 0.3092 -0.0067 -0.0243 0.0070  125 SER   A OG  
941  N N   . THR   A 120 ? 0.2606 0.2495 0.2714 -0.0059 -0.0087 0.0002  126 THR   A N   
942  C CA  . THR   A 120 ? 0.2835 0.2598 0.2941 -0.0042 0.0041  -0.0012 126 THR   A CA  
943  C C   . THR   A 120 ? 0.3187 0.2868 0.3187 -0.0039 0.0115  -0.0029 126 THR   A C   
944  O O   . THR   A 120 ? 0.3100 0.2856 0.3062 -0.0046 0.0057  -0.0021 126 THR   A O   
945  C CB  . THR   A 120 ? 0.2893 0.2786 0.3289 -0.0009 0.0088  0.0059  126 THR   A CB  
946  O OG1 . THR   A 120 ? 0.2947 0.2974 0.3476 -0.0002 0.0080  0.0113  126 THR   A OG1 
947  C CG2 . THR   A 120 ? 0.2733 0.2741 0.3243 -0.0012 0.0005  0.0095  126 THR   A CG2 
948  N N   . GLY   A 121 ? 0.3355 0.2869 0.3320 -0.0025 0.0264  -0.0048 127 GLY   A N   
949  C CA  . GLY   A 121 ? 0.3640 0.3068 0.3537 -0.0015 0.0365  -0.0055 127 GLY   A CA  
950  C C   . GLY   A 121 ? 0.4040 0.3205 0.3835 -0.0009 0.0563  -0.0091 127 GLY   A C   
951  O O   . GLY   A 121 ? 0.4074 0.3142 0.3909 -0.0007 0.0639  -0.0104 127 GLY   A O   
952  N N   . GLY   A 122 ? 0.4467 0.3497 0.4122 -0.0008 0.0663  -0.0108 128 GLY   A N   
953  C CA  . GLY   A 122 ? 0.4787 0.3514 0.4302 -0.0005 0.0895  -0.0146 128 GLY   A CA  
954  C C   . GLY   A 122 ? 0.4736 0.3533 0.4569 0.0051  0.1050  -0.0081 128 GLY   A C   
955  O O   . GLY   A 122 ? 0.4388 0.3476 0.4603 0.0082  0.0970  0.0001  128 GLY   A O   
956  N N   . ASN   A 123 ? 0.5056 0.3568 0.4723 0.0055  0.1271  -0.0114 129 ASN   A N   
957  C CA  . ASN   A 123 ? 0.5128 0.3666 0.5125 0.0109  0.1454  -0.0048 129 ASN   A CA  
958  C C   . ASN   A 123 ? 0.4775 0.3604 0.5010 0.0128  0.1321  0.0019  129 ASN   A C   
959  O O   . ASN   A 123 ? 0.4657 0.3668 0.5349 0.0167  0.1362  0.0112  129 ASN   A O   
960  C CB  . ASN   A 123 ? 0.5452 0.4050 0.5897 0.0154  0.1587  0.0022  129 ASN   A CB  
961  C CG  . ASN   A 123 ? 0.6666 0.4897 0.6899 0.0142  0.1821  -0.0048 129 ASN   A CG  
962  O OD1 . ASN   A 123 ? 0.7286 0.5159 0.7014 0.0096  0.1930  -0.0148 129 ASN   A OD1 
963  N ND2 . ASN   A 123 ? 0.6887 0.5180 0.7492 0.0175  0.1906  0.0009  129 ASN   A ND2 
964  N N   . GLY   A 124 ? 0.4463 0.3312 0.4397 0.0093  0.1170  -0.0023 130 GLY   A N   
965  C CA  . GLY   A 124 ? 0.4089 0.3167 0.4194 0.0102  0.1064  0.0024  130 GLY   A CA  
966  C C   . GLY   A 124 ? 0.3490 0.2898 0.3843 0.0092  0.0844  0.0072  130 GLY   A C   
967  O O   . GLY   A 124 ? 0.3175 0.2761 0.3674 0.0088  0.0760  0.0107  130 GLY   A O   
968  N N   . LEU   A 125 ? 0.3302 0.2769 0.3674 0.0080  0.0757  0.0069  131 LEU   A N   
969  C CA  . LEU   A 125 ? 0.3039 0.2770 0.3575 0.0062  0.0560  0.0109  131 LEU   A CA  
970  C C   . LEU   A 125 ? 0.3180 0.2898 0.3431 0.0028  0.0421  0.0051  131 LEU   A C   
971  O O   . LEU   A 125 ? 0.3465 0.2984 0.3436 0.0014  0.0453  -0.0009 131 LEU   A O   
972  C CB  . LEU   A 125 ? 0.3083 0.2921 0.3939 0.0077  0.0563  0.0181  131 LEU   A CB  
973  C CG  . LEU   A 125 ? 0.3413 0.3276 0.4648 0.0111  0.0697  0.0268  131 LEU   A CG  
974  C CD1 . LEU   A 125 ? 0.3604 0.3496 0.5137 0.0133  0.0750  0.0339  131 LEU   A CD1 
975  C CD2 . LEU   A 125 ? 0.3323 0.3388 0.4779 0.0091  0.0589  0.0336  131 LEU   A CD2 
976  N N   . VAL   A 126 ? 0.2837 0.2747 0.3164 0.0008  0.0272  0.0074  132 VAL   A N   
977  C CA  . VAL   A 126 ? 0.2802 0.2723 0.2962 -0.0018 0.0155  0.0040  132 VAL   A CA  
978  C C   . VAL   A 126 ? 0.2675 0.2778 0.3012 -0.0031 0.0057  0.0087  132 VAL   A C   
979  O O   . VAL   A 126 ? 0.2641 0.2867 0.3137 -0.0042 0.0029  0.0135  132 VAL   A O   
980  C CB  . VAL   A 126 ? 0.2939 0.2837 0.2918 -0.0038 0.0101  0.0011  132 VAL   A CB  
981  C CG1 . VAL   A 126 ? 0.3021 0.3049 0.3122 -0.0043 0.0088  0.0038  132 VAL   A CG1 
982  C CG2 . VAL   A 126 ? 0.2856 0.2778 0.2753 -0.0062 -0.0015 -0.0001 132 VAL   A CG2 
983  N N   . GLY   A 127 ? 0.2585 0.2680 0.2891 -0.0035 0.0011  0.0078  133 GLY   A N   
984  C CA  . GLY   A 127 ? 0.2453 0.2683 0.2887 -0.0050 -0.0067 0.0125  133 GLY   A CA  
985  C C   . GLY   A 127 ? 0.2514 0.2755 0.2833 -0.0072 -0.0143 0.0099  133 GLY   A C   
986  O O   . GLY   A 127 ? 0.2621 0.2768 0.2821 -0.0070 -0.0150 0.0057  133 GLY   A O   
987  N N   . PHE   A 128 ? 0.2392 0.2728 0.2745 -0.0100 -0.0198 0.0128  134 PHE   A N   
988  C CA  . PHE   A 128 ? 0.2516 0.2845 0.2790 -0.0119 -0.0232 0.0110  134 PHE   A CA  
989  C C   . PHE   A 128 ? 0.2412 0.2781 0.2732 -0.0134 -0.0260 0.0148  134 PHE   A C   
990  O O   . PHE   A 128 ? 0.2375 0.2799 0.2738 -0.0158 -0.0286 0.0197  134 PHE   A O   
991  C CB  . PHE   A 128 ? 0.2510 0.2859 0.2727 -0.0152 -0.0230 0.0101  134 PHE   A CB  
992  C CG  . PHE   A 128 ? 0.2531 0.2854 0.2719 -0.0140 -0.0198 0.0076  134 PHE   A CG  
993  C CD1 . PHE   A 128 ? 0.2553 0.2813 0.2677 -0.0127 -0.0190 0.0050  134 PHE   A CD1 
994  C CD2 . PHE   A 128 ? 0.2588 0.2947 0.2833 -0.0144 -0.0182 0.0095  134 PHE   A CD2 
995  C CE1 . PHE   A 128 ? 0.2567 0.2788 0.2642 -0.0117 -0.0159 0.0036  134 PHE   A CE1 
996  C CE2 . PHE   A 128 ? 0.2559 0.2884 0.2781 -0.0131 -0.0136 0.0075  134 PHE   A CE2 
997  C CZ  . PHE   A 128 ? 0.2557 0.2807 0.2675 -0.0115 -0.0120 0.0043  134 PHE   A CZ  
998  N N   . ALA   A 129 ? 0.2447 0.2782 0.2764 -0.0127 -0.0264 0.0136  135 ALA   A N   
999  C CA  . ALA   A 129 ? 0.2540 0.2890 0.2884 -0.0138 -0.0272 0.0172  135 ALA   A CA  
1000 C C   . ALA   A 129 ? 0.2478 0.2805 0.2723 -0.0183 -0.0253 0.0173  135 ALA   A C   
1001 O O   . ALA   A 129 ? 0.2461 0.2745 0.2691 -0.0183 -0.0216 0.0143  135 ALA   A O   
1002 C CB  . ALA   A 129 ? 0.2487 0.2798 0.2895 -0.0114 -0.0271 0.0160  135 ALA   A CB  
1003 N N   . ASP   A 130 ? 0.2659 0.2994 0.2831 -0.0229 -0.0275 0.0213  136 ASP   A N   
1004 C CA  . ASP   A 130 ? 0.2899 0.3153 0.2901 -0.0291 -0.0241 0.0204  136 ASP   A CA  
1005 C C   . ASP   A 130 ? 0.2804 0.2971 0.2783 -0.0289 -0.0165 0.0200  136 ASP   A C   
1006 O O   . ASP   A 130 ? 0.2761 0.2946 0.2826 -0.0260 -0.0174 0.0231  136 ASP   A O   
1007 C CB  . ASP   A 130 ? 0.3037 0.3285 0.2918 -0.0364 -0.0311 0.0258  136 ASP   A CB  
1008 C CG  . ASP   A 130 ? 0.3529 0.3643 0.3156 -0.0452 -0.0276 0.0235  136 ASP   A CG  
1009 O OD1 . ASP   A 130 ? 0.3643 0.3724 0.3229 -0.0463 -0.0228 0.0180  136 ASP   A OD1 
1010 O OD2 . ASP   A 130 ? 0.4074 0.4093 0.3524 -0.0516 -0.0288 0.0271  136 ASP   A OD2 
1011 N N   . VAL   A 131 ? 0.2790 0.2855 0.2682 -0.0317 -0.0072 0.0165  137 VAL   A N   
1012 C CA  . VAL   A 131 ? 0.3030 0.2983 0.2923 -0.0318 0.0039  0.0169  137 VAL   A CA  
1013 C C   . VAL   A 131 ? 0.3366 0.3134 0.2977 -0.0405 0.0135  0.0156  137 VAL   A C   
1014 O O   . VAL   A 131 ? 0.3640 0.3270 0.3209 -0.0416 0.0263  0.0160  137 VAL   A O   
1015 C CB  . VAL   A 131 ? 0.3055 0.3011 0.3174 -0.0265 0.0106  0.0157  137 VAL   A CB  
1016 C CG1 . VAL   A 131 ? 0.2963 0.3042 0.3281 -0.0205 0.0002  0.0169  137 VAL   A CG1 
1017 C CG2 . VAL   A 131 ? 0.3028 0.2942 0.3127 -0.0283 0.0168  0.0123  137 VAL   A CG2 
1018 N N   . ARG   A 132 ? 0.3367 0.3108 0.2780 -0.0474 0.0085  0.0138  138 ARG   A N   
1019 C CA  . ARG   A 132 ? 0.3537 0.3068 0.2627 -0.0579 0.0163  0.0111  138 ARG   A CA  
1020 C C   . ARG   A 132 ? 0.4004 0.3390 0.2839 -0.0648 0.0167  0.0151  138 ARG   A C   
1021 O O   . ARG   A 132 ? 0.4495 0.3637 0.3041 -0.0729 0.0293  0.0119  138 ARG   A O   
1022 C CB  . ARG   A 132 ? 0.3365 0.2913 0.2319 -0.0647 0.0072  0.0089  138 ARG   A CB  
1023 C CG  . ARG   A 132 ? 0.3319 0.2971 0.2480 -0.0588 0.0096  0.0048  138 ARG   A CG  
1024 C CD  . ARG   A 132 ? 0.3389 0.3061 0.2432 -0.0658 -0.0001 0.0036  138 ARG   A CD  
1025 N NE  . ARG   A 132 ? 0.3332 0.3177 0.2498 -0.0639 -0.0170 0.0099  138 ARG   A NE  
1026 C CZ  . ARG   A 132 ? 0.3438 0.3359 0.2629 -0.0677 -0.0278 0.0117  138 ARG   A CZ  
1027 N NH1 . ARG   A 132 ? 0.3610 0.3439 0.2657 -0.0751 -0.0255 0.0070  138 ARG   A NH1 
1028 N NH2 . ARG   A 132 ? 0.3440 0.3518 0.2822 -0.0643 -0.0398 0.0186  138 ARG   A NH2 
1029 N N   . ASP   A 133 ? 0.3926 0.3432 0.2854 -0.0619 0.0049  0.0220  139 ASP   A N   
1030 C CA  . ASP   A 133 ? 0.4137 0.3498 0.2822 -0.0684 0.0049  0.0275  139 ASP   A CA  
1031 C C   . ASP   A 133 ? 0.4273 0.3532 0.3037 -0.0630 0.0223  0.0273  139 ASP   A C   
1032 O O   . ASP   A 133 ? 0.4669 0.3755 0.3199 -0.0684 0.0275  0.0309  139 ASP   A O   
1033 C CB  . ASP   A 133 ? 0.4090 0.3625 0.2888 -0.0674 -0.0143 0.0367  139 ASP   A CB  
1034 C CG  . ASP   A 133 ? 0.4300 0.4028 0.3483 -0.0547 -0.0147 0.0385  139 ASP   A CG  
1035 O OD1 . ASP   A 133 ? 0.3951 0.3781 0.3358 -0.0472 -0.0112 0.0329  139 ASP   A OD1 
1036 O OD2 . ASP   A 133 ? 0.4312 0.4073 0.3556 -0.0529 -0.0185 0.0455  139 ASP   A OD2 
1037 N N   . LEU   A 134 ? 0.3973 0.3330 0.3072 -0.0529 0.0304  0.0243  140 LEU   A N   
1038 C CA  . LEU   A 134 ? 0.3974 0.3262 0.3243 -0.0472 0.0455  0.0256  140 LEU   A CA  
1039 C C   . LEU   A 134 ? 0.4331 0.3358 0.3443 -0.0518 0.0685  0.0214  140 LEU   A C   
1040 O O   . LEU   A 134 ? 0.4295 0.3328 0.3647 -0.0471 0.0796  0.0187  140 LEU   A O   
1041 C CB  . LEU   A 134 ? 0.3684 0.3181 0.3385 -0.0365 0.0409  0.0256  140 LEU   A CB  
1042 C CG  . LEU   A 134 ? 0.3651 0.3358 0.3486 -0.0324 0.0222  0.0286  140 LEU   A CG  
1043 C CD1 . LEU   A 134 ? 0.3459 0.3313 0.3620 -0.0246 0.0173  0.0271  140 LEU   A CD1 
1044 C CD2 . LEU   A 134 ? 0.3798 0.3496 0.3604 -0.0323 0.0196  0.0347  140 LEU   A CD2 
1045 N N   . LEU   A 135 ? 0.4646 0.3415 0.3332 -0.0621 0.0762  0.0214  141 LEU   A N   
1046 C CA  . LEU   A 135 ? 0.5105 0.3558 0.3548 -0.0687 0.1008  0.0161  141 LEU   A CA  
1047 C C   . LEU   A 135 ? 0.5251 0.3613 0.3986 -0.0613 0.1249  0.0171  141 LEU   A C   
1048 O O   . LEU   A 135 ? 0.5418 0.3607 0.4182 -0.0623 0.1464  0.0129  141 LEU   A O   
1049 C CB  . LEU   A 135 ? 0.5461 0.3610 0.3321 -0.0829 0.1033  0.0163  141 LEU   A CB  
1050 C CG  . LEU   A 135 ? 0.5819 0.4019 0.3375 -0.0932 0.0787  0.0171  141 LEU   A CG  
1051 C CD1 . LEU   A 135 ? 0.6488 0.4308 0.3403 -0.1104 0.0830  0.0168  141 LEU   A CD1 
1052 C CD2 . LEU   A 135 ? 0.5755 0.4053 0.3394 -0.0938 0.0740  0.0105  141 LEU   A CD2 
1053 N N   . TRP   A 136 ? 0.5091 0.3551 0.4056 -0.0544 0.1225  0.0234  142 TRP   A N   
1054 C CA  . TRP   A 136 ? 0.5094 0.3489 0.4402 -0.0472 0.1434  0.0263  142 TRP   A CA  
1055 C C   . TRP   A 136 ? 0.5061 0.3633 0.4871 -0.0388 0.1444  0.0263  142 TRP   A C   
1056 O O   . TRP   A 136 ? 0.5088 0.3570 0.5203 -0.0345 0.1645  0.0293  142 TRP   A O   
1057 C CB  . TRP   A 136 ? 0.4957 0.3449 0.4424 -0.0419 0.1369  0.0333  142 TRP   A CB  
1058 C CG  . TRP   A 136 ? 0.4640 0.3465 0.4320 -0.0365 0.1085  0.0355  142 TRP   A CG  
1059 C CD1 . TRP   A 136 ? 0.4683 0.3605 0.4137 -0.0401 0.0885  0.0373  142 TRP   A CD1 
1060 C CD2 . TRP   A 136 ? 0.4373 0.3450 0.4535 -0.0274 0.0980  0.0369  142 TRP   A CD2 
1061 N NE1 . TRP   A 136 ? 0.4481 0.3684 0.4255 -0.0328 0.0700  0.0389  142 TRP   A NE1 
1062 C CE2 . TRP   A 136 ? 0.4290 0.3577 0.4459 -0.0257 0.0749  0.0380  142 TRP   A CE2 
1063 C CE3 . TRP   A 136 ? 0.4315 0.3442 0.4913 -0.0212 0.1059  0.0385  142 TRP   A CE3 
1064 C CZ2 . TRP   A 136 ? 0.4157 0.3665 0.4673 -0.0191 0.0608  0.0384  142 TRP   A CZ2 
1065 C CZ3 . TRP   A 136 ? 0.4190 0.3554 0.5140 -0.0153 0.0880  0.0404  142 TRP   A CZ3 
1066 C CH2 . TRP   A 136 ? 0.4105 0.3640 0.4975 -0.0147 0.0665  0.0393  142 TRP   A CH2 
1067 N N   . LEU   A 137 ? 0.4990 0.3799 0.4902 -0.0369 0.1235  0.0242  143 LEU   A N   
1068 C CA  . LEU   A 137 ? 0.5019 0.3973 0.5359 -0.0305 0.1228  0.0254  143 LEU   A CA  
1069 C C   . LEU   A 137 ? 0.5636 0.4370 0.5997 -0.0330 0.1489  0.0232  143 LEU   A C   
1070 O O   . LEU   A 137 ? 0.5564 0.4367 0.6368 -0.0272 0.1551  0.0276  143 LEU   A O   
1071 C CB  . LEU   A 137 ? 0.4715 0.3894 0.5047 -0.0297 0.0990  0.0227  143 LEU   A CB  
1072 C CG  . LEU   A 137 ? 0.4482 0.3889 0.4926 -0.0254 0.0758  0.0252  143 LEU   A CG  
1073 C CD1 . LEU   A 137 ? 0.4395 0.3962 0.4762 -0.0258 0.0573  0.0219  143 LEU   A CD1 
1074 C CD2 . LEU   A 137 ? 0.4314 0.3831 0.5201 -0.0184 0.0732  0.0308  143 LEU   A CD2 
1075 N N   . ASP   A 138 ? 0.6266 0.4728 0.6152 -0.0425 0.1633  0.0169  144 ASP   A N   
1076 C CA  . ASP   A 138 ? 0.6839 0.5027 0.6653 -0.0468 0.1918  0.0129  144 ASP   A CA  
1077 C C   . ASP   A 138 ? 0.7381 0.5271 0.7231 -0.0471 0.2241  0.0153  144 ASP   A C   
1078 O O   . ASP   A 138 ? 0.7513 0.5116 0.7258 -0.0516 0.2522  0.0114  144 ASP   A O   
1079 C CB  . ASP   A 138 ? 0.7320 0.5292 0.6527 -0.0594 0.1929  0.0040  144 ASP   A CB  
1080 C CG  . ASP   A 138 ? 0.8062 0.6259 0.7179 -0.0612 0.1661  0.0009  144 ASP   A CG  
1081 O OD1 . ASP   A 138 ? 0.7977 0.6473 0.7497 -0.0523 0.1504  0.0044  144 ASP   A OD1 
1082 O OD2 . ASP   A 138 ? 0.8665 0.6723 0.7299 -0.0722 0.1605  -0.0047 144 ASP   A OD2 
1083 N N   . GLU   A 139 ? 0.7671 0.5586 0.7620 -0.0433 0.2230  0.0210  145 GLU   A N   
1084 C CA  . GLU   A 139 ? 0.8211 0.5823 0.8193 -0.0433 0.2559  0.0237  145 GLU   A CA  
1085 C C   . GLU   A 139 ? 0.8283 0.6066 0.8763 -0.0335 0.2527  0.0334  145 GLU   A C   
1086 O O   . GLU   A 139 ? 0.8193 0.6261 0.8770 -0.0298 0.2239  0.0362  145 GLU   A O   
1087 C CB  . GLU   A 139 ? 0.9067 0.6313 0.8325 -0.0555 0.2676  0.0179  145 GLU   A CB  
1088 C CG  . GLU   A 139 ? 0.9982 0.7370 0.8944 -0.0582 0.2392  0.0197  145 GLU   A CG  
1089 C CD  . GLU   A 139 ? 1.1491 0.8596 0.9691 -0.0733 0.2369  0.0139  145 GLU   A CD  
1090 O OE1 . GLU   A 139 ? 1.1789 0.8743 0.9658 -0.0782 0.2366  0.0172  145 GLU   A OE1 
1091 O OE2 . GLU   A 139 ? 1.1988 0.9014 0.9924 -0.0810 0.2347  0.0068  145 GLU   A OE2 
1092 N N   . GLU   A 140 ? 0.8439 0.6028 0.9247 -0.0298 0.2840  0.0387  146 GLU   A N   
1093 C CA  . GLU   A 140 ? 0.8499 0.6204 0.9835 -0.0211 0.2861  0.0489  146 GLU   A CA  
1094 C C   . GLU   A 140 ? 0.8337 0.6480 1.0204 -0.0133 0.2520  0.0551  146 GLU   A C   
1095 O O   . GLU   A 140 ? 0.8186 0.6455 1.0606 -0.0065 0.2510  0.0645  146 GLU   A O   
1096 C CB  . GLU   A 140 ? 0.9059 0.6605 1.0019 -0.0240 0.2902  0.0489  146 GLU   A CB  
1097 C CG  . GLU   A 140 ? 0.9789 0.7642 1.0758 -0.0211 0.2556  0.0513  146 GLU   A CG  
1098 C CD  . GLU   A 140 ? 1.0615 0.8557 1.2068 -0.0132 0.2586  0.0605  146 GLU   A CD  
1099 O OE1 . GLU   A 140 ? 1.0644 0.8900 1.2366 -0.0085 0.2303  0.0636  146 GLU   A OE1 
1100 O OE2 . GLU   A 140 ? 1.0928 0.8605 1.2491 -0.0122 0.2908  0.0644  146 GLU   A OE2 
1101 N N1  . A1BOM B .   ? 0.3073 0.2927 0.3447 -0.0056 -0.0118 0.0016  201 A1BOM A N1  
1102 C C4  . A1BOM B .   ? 0.4759 0.3069 0.3456 -0.0184 0.0602  -0.0313 201 A1BOM A C4  
1103 C C5  . A1BOM B .   ? 0.4622 0.3075 0.3539 -0.0174 0.0533  -0.0299 201 A1BOM A C5  
1104 C C6  . A1BOM B .   ? 0.4415 0.3169 0.3548 -0.0160 0.0337  -0.0247 201 A1BOM A C6  
1105 C C7  . A1BOM B .   ? 0.4312 0.3223 0.3705 -0.0140 0.0287  -0.0221 201 A1BOM A C7  
1106 C C8  . A1BOM B .   ? 0.4386 0.3227 0.3627 -0.0202 0.0136  -0.0254 201 A1BOM A C8  
1107 C C10 . A1BOM B .   ? 0.3905 0.3161 0.3710 -0.0173 -0.0096 -0.0168 201 A1BOM A C10 
1108 C C13 . A1BOM B .   ? 0.3772 0.3096 0.3617 -0.0111 0.0066  -0.0136 201 A1BOM A C13 
1109 O O2  . A1BOM B .   ? 0.3200 0.2844 0.3605 -0.0043 0.0056  -0.0019 201 A1BOM A O2  
1110 C C12 . A1BOM B .   ? 0.3308 0.2980 0.3585 -0.0066 -0.0040 -0.0034 201 A1BOM A C12 
1111 C C11 . A1BOM B .   ? 0.3678 0.3150 0.3659 -0.0116 -0.0066 -0.0106 201 A1BOM A C11 
1112 C C9  . A1BOM B .   ? 0.4021 0.3049 0.3483 -0.0228 -0.0097 -0.0224 201 A1BOM A C9  
1113 N N   . A1BOM B .   ? 0.3969 0.3026 0.3469 -0.0179 0.0041  -0.0210 201 A1BOM A N   
1114 O O1  . A1BOM B .   ? 0.4784 0.3361 0.3684 -0.0275 0.0109  -0.0314 201 A1BOM A O1  
1115 C C1  . A1BOM B .   ? 0.4304 0.3206 0.3434 -0.0158 0.0218  -0.0214 201 A1BOM A C1  
1116 O O   . A1BOM B .   ? 0.3989 0.3141 0.3322 -0.0147 0.0065  -0.0169 201 A1BOM A O   
1117 C C   . A1BOM B .   ? 0.3837 0.3113 0.3170 -0.0152 -0.0043 -0.0139 201 A1BOM A C   
1118 C C3  . A1BOM B .   ? 0.4617 0.3102 0.3331 -0.0179 0.0466  -0.0273 201 A1BOM A C3  
1119 C C2  . A1BOM B .   ? 0.4424 0.3205 0.3362 -0.0166 0.0278  -0.0225 201 A1BOM A C2  
# 
