data_7HYP
# 
_entry.id   7HYP 
# 
_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   7HYP         pdb_00007hyp 10.2210/pdb7hyp/pdb 
WWPDB D_1001408097 ?            ?                   
# 
_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                        7HYP 
_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-(sulfamoylmethyl)phenyl]acetyl}piperidine-3-carboxamide' 339.410   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                           65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                 78.133    1   ?         ? ? ? 
5 water       nat water                                                                18.015    181 ?         ? ? ? 
# 
_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-(sulfamoylmethyl)phenyl]acetyl}piperidine-3-carboxamide' A1BPZ 
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 
A1BPZ non-polymer         . '(3S)-1-{[2-(sulfamoylmethyl)phenyl]acetyl}piperidine-3-carboxamide' ? 'C15 H21 N3 O4 S' 339.410 
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        A1BPZ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BPZ 
_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 A1BPZ 1   201 201 A1BPZ LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 3   DMS   DMS A . 
E 5 HOH   1   301 26  HOH   HOH A . 
E 5 HOH   2   302 79  HOH   HOH A . 
E 5 HOH   3   303 181 HOH   HOH A . 
E 5 HOH   4   304 152 HOH   HOH A . 
E 5 HOH   5   305 137 HOH   HOH A . 
E 5 HOH   6   306 30  HOH   HOH A . 
E 5 HOH   7   307 169 HOH   HOH A . 
E 5 HOH   8   308 214 HOH   HOH A . 
E 5 HOH   9   309 25  HOH   HOH A . 
E 5 HOH   10  310 245 HOH   HOH A . 
E 5 HOH   11  311 24  HOH   HOH A . 
E 5 HOH   12  312 104 HOH   HOH A . 
E 5 HOH   13  313 111 HOH   HOH A . 
E 5 HOH   14  314 205 HOH   HOH A . 
E 5 HOH   15  315 34  HOH   HOH A . 
E 5 HOH   16  316 77  HOH   HOH A . 
E 5 HOH   17  317 150 HOH   HOH A . 
E 5 HOH   18  318 59  HOH   HOH A . 
E 5 HOH   19  319 36  HOH   HOH A . 
E 5 HOH   20  320 252 HOH   HOH A . 
E 5 HOH   21  321 4   HOH   HOH A . 
E 5 HOH   22  322 107 HOH   HOH A . 
E 5 HOH   23  323 9   HOH   HOH A . 
E 5 HOH   24  324 211 HOH   HOH A . 
E 5 HOH   25  325 215 HOH   HOH A . 
E 5 HOH   26  326 121 HOH   HOH A . 
E 5 HOH   27  327 253 HOH   HOH A . 
E 5 HOH   28  328 42  HOH   HOH A . 
E 5 HOH   29  329 43  HOH   HOH A . 
E 5 HOH   30  330 68  HOH   HOH A . 
E 5 HOH   31  331 75  HOH   HOH A . 
E 5 HOH   32  332 57  HOH   HOH A . 
E 5 HOH   33  333 33  HOH   HOH A . 
E 5 HOH   34  334 29  HOH   HOH A . 
E 5 HOH   35  335 186 HOH   HOH A . 
E 5 HOH   36  336 257 HOH   HOH A . 
E 5 HOH   37  337 141 HOH   HOH A . 
E 5 HOH   38  338 7   HOH   HOH A . 
E 5 HOH   39  339 218 HOH   HOH A . 
E 5 HOH   40  340 47  HOH   HOH A . 
E 5 HOH   41  341 60  HOH   HOH A . 
E 5 HOH   42  342 37  HOH   HOH A . 
E 5 HOH   43  343 28  HOH   HOH A . 
E 5 HOH   44  344 2   HOH   HOH A . 
E 5 HOH   45  345 147 HOH   HOH A . 
E 5 HOH   46  346 97  HOH   HOH A . 
E 5 HOH   47  347 254 HOH   HOH A . 
E 5 HOH   48  348 50  HOH   HOH A . 
E 5 HOH   49  349 90  HOH   HOH A . 
E 5 HOH   50  350 13  HOH   HOH A . 
E 5 HOH   51  351 21  HOH   HOH A . 
E 5 HOH   52  352 85  HOH   HOH A . 
E 5 HOH   53  353 219 HOH   HOH A . 
E 5 HOH   54  354 94  HOH   HOH A . 
E 5 HOH   55  355 82  HOH   HOH A . 
E 5 HOH   56  356 171 HOH   HOH A . 
E 5 HOH   57  357 12  HOH   HOH A . 
E 5 HOH   58  358 105 HOH   HOH A . 
E 5 HOH   59  359 119 HOH   HOH A . 
E 5 HOH   60  360 52  HOH   HOH A . 
E 5 HOH   61  361 16  HOH   HOH A . 
E 5 HOH   62  362 110 HOH   HOH A . 
E 5 HOH   63  363 18  HOH   HOH A . 
E 5 HOH   64  364 53  HOH   HOH A . 
E 5 HOH   65  365 100 HOH   HOH A . 
E 5 HOH   66  366 19  HOH   HOH A . 
E 5 HOH   67  367 167 HOH   HOH A . 
E 5 HOH   68  368 95  HOH   HOH A . 
E 5 HOH   69  369 174 HOH   HOH A . 
E 5 HOH   70  370 84  HOH   HOH A . 
E 5 HOH   71  371 255 HOH   HOH A . 
E 5 HOH   72  372 182 HOH   HOH A . 
E 5 HOH   73  373 11  HOH   HOH A . 
E 5 HOH   74  374 192 HOH   HOH A . 
E 5 HOH   75  375 62  HOH   HOH A . 
E 5 HOH   76  376 103 HOH   HOH A . 
E 5 HOH   77  377 20  HOH   HOH A . 
E 5 HOH   78  378 177 HOH   HOH A . 
E 5 HOH   79  379 8   HOH   HOH A . 
E 5 HOH   80  380 89  HOH   HOH A . 
E 5 HOH   81  381 10  HOH   HOH A . 
E 5 HOH   82  382 51  HOH   HOH A . 
E 5 HOH   83  383 96  HOH   HOH A . 
E 5 HOH   84  384 161 HOH   HOH A . 
E 5 HOH   85  385 98  HOH   HOH A . 
E 5 HOH   86  386 39  HOH   HOH A . 
E 5 HOH   87  387 83  HOH   HOH A . 
E 5 HOH   88  388 106 HOH   HOH A . 
E 5 HOH   89  389 168 HOH   HOH A . 
E 5 HOH   90  390 38  HOH   HOH A . 
E 5 HOH   91  391 108 HOH   HOH A . 
E 5 HOH   92  392 15  HOH   HOH A . 
E 5 HOH   93  393 40  HOH   HOH A . 
E 5 HOH   94  394 132 HOH   HOH A . 
E 5 HOH   95  395 46  HOH   HOH A . 
E 5 HOH   96  396 27  HOH   HOH A . 
E 5 HOH   97  397 80  HOH   HOH A . 
E 5 HOH   98  398 81  HOH   HOH A . 
E 5 HOH   99  399 251 HOH   HOH A . 
E 5 HOH   100 400 35  HOH   HOH A . 
E 5 HOH   101 401 131 HOH   HOH A . 
E 5 HOH   102 402 176 HOH   HOH A . 
E 5 HOH   103 403 138 HOH   HOH A . 
E 5 HOH   104 404 76  HOH   HOH A . 
E 5 HOH   105 405 201 HOH   HOH A . 
E 5 HOH   106 406 133 HOH   HOH A . 
E 5 HOH   107 407 72  HOH   HOH A . 
E 5 HOH   108 408 140 HOH   HOH A . 
E 5 HOH   109 409 70  HOH   HOH A . 
E 5 HOH   110 410 23  HOH   HOH A . 
E 5 HOH   111 411 48  HOH   HOH A . 
E 5 HOH   112 412 124 HOH   HOH A . 
E 5 HOH   113 413 159 HOH   HOH A . 
E 5 HOH   114 414 65  HOH   HOH A . 
E 5 HOH   115 415 114 HOH   HOH A . 
E 5 HOH   116 416 237 HOH   HOH A . 
E 5 HOH   117 417 144 HOH   HOH A . 
E 5 HOH   118 418 123 HOH   HOH A . 
E 5 HOH   119 419 175 HOH   HOH A . 
E 5 HOH   120 420 126 HOH   HOH A . 
E 5 HOH   121 421 228 HOH   HOH A . 
E 5 HOH   122 422 58  HOH   HOH A . 
E 5 HOH   123 423 128 HOH   HOH A . 
E 5 HOH   124 424 156 HOH   HOH A . 
E 5 HOH   125 425 216 HOH   HOH A . 
E 5 HOH   126 426 248 HOH   HOH A . 
E 5 HOH   127 427 155 HOH   HOH A . 
E 5 HOH   128 428 69  HOH   HOH A . 
E 5 HOH   129 429 233 HOH   HOH A . 
E 5 HOH   130 430 91  HOH   HOH A . 
E 5 HOH   131 431 258 HOH   HOH A . 
E 5 HOH   132 432 14  HOH   HOH A . 
E 5 HOH   133 433 239 HOH   HOH A . 
E 5 HOH   134 434 213 HOH   HOH A . 
E 5 HOH   135 435 256 HOH   HOH A . 
E 5 HOH   136 436 158 HOH   HOH A . 
E 5 HOH   137 437 193 HOH   HOH A . 
E 5 HOH   138 438 154 HOH   HOH A . 
E 5 HOH   139 439 135 HOH   HOH A . 
E 5 HOH   140 440 198 HOH   HOH A . 
E 5 HOH   141 441 78  HOH   HOH A . 
E 5 HOH   142 442 49  HOH   HOH A . 
E 5 HOH   143 443 142 HOH   HOH A . 
E 5 HOH   144 444 117 HOH   HOH A . 
E 5 HOH   145 445 112 HOH   HOH A . 
E 5 HOH   146 446 224 HOH   HOH A . 
E 5 HOH   147 447 206 HOH   HOH A . 
E 5 HOH   148 448 240 HOH   HOH A . 
E 5 HOH   149 449 243 HOH   HOH A . 
E 5 HOH   150 450 99  HOH   HOH A . 
E 5 HOH   151 451 67  HOH   HOH A . 
E 5 HOH   152 452 127 HOH   HOH A . 
E 5 HOH   153 453 241 HOH   HOH A . 
E 5 HOH   154 454 122 HOH   HOH A . 
E 5 HOH   155 455 73  HOH   HOH A . 
E 5 HOH   156 456 207 HOH   HOH A . 
E 5 HOH   157 457 200 HOH   HOH A . 
E 5 HOH   158 458 189 HOH   HOH A . 
E 5 HOH   159 459 86  HOH   HOH A . 
E 5 HOH   160 460 221 HOH   HOH A . 
E 5 HOH   161 461 41  HOH   HOH A . 
E 5 HOH   162 462 56  HOH   HOH A . 
E 5 HOH   163 463 229 HOH   HOH A . 
E 5 HOH   164 464 202 HOH   HOH A . 
E 5 HOH   165 465 61  HOH   HOH A . 
E 5 HOH   166 466 234 HOH   HOH A . 
E 5 HOH   167 467 238 HOH   HOH A . 
E 5 HOH   168 468 102 HOH   HOH A . 
E 5 HOH   169 469 222 HOH   HOH A . 
E 5 HOH   170 470 208 HOH   HOH A . 
E 5 HOH   171 471 223 HOH   HOH A . 
E 5 HOH   172 472 125 HOH   HOH A . 
E 5 HOH   173 473 165 HOH   HOH A . 
E 5 HOH   174 474 92  HOH   HOH A . 
E 5 HOH   175 475 118 HOH   HOH A . 
E 5 HOH   176 476 71  HOH   HOH A . 
E 5 HOH   177 477 209 HOH   HOH A . 
E 5 HOH   178 478 113 HOH   HOH A . 
E 5 HOH   179 479 230 HOH   HOH A . 
E 5 HOH   180 480 242 HOH   HOH A . 
E 5 HOH   181 481 244 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           7HYP 
_cell.length_a           87.783 
_cell.length_b           58.213 
_cell.length_c           32.764 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.46 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HYP 
_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          7HYP 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.63 
_exptl_crystal.density_percent_sol   53.25 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-09 
_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   0.92199 
_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        0.92199 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HYP 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.49 
_reflns.d_resolution_high            1.57 
_reflns.number_obs                   23030 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            0.049 
_reflns.pdbx_netI_over_sigmaI        16.7 
_reflns.pdbx_redundancy              6.8 
_reflns.pdbx_Rrim_I_all              0.053 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     156969 
_reflns.pdbx_chi_squared             0.52 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.57 
_reflns_shell.d_res_low                   1.59 
_reflns_shell.number_measured_all         6356 
_reflns_shell.number_unique_obs           1078 
_reflns_shell.Rmerge_I_obs                1.956 
_reflns_shell.pdbx_chi_squared            0.12 
_reflns_shell.pdbx_redundancy             5.9 
_reflns_shell.percent_possible_obs        94.5 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.4 
_reflns_shell.pdbx_Rrim_I_all             2.153 
_reflns_shell.pdbx_Rpim_I_all             0.883 
_reflns_shell.pdbx_CC_half                0.312 
_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                                 7HYP 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     22929 
_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                             48.50 
_refine.ls_d_res_high                            1.569 
_refine.ls_percent_reflns_obs                    99.1 
_refine.ls_R_factor_obs                          0.2046 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2029 
_refine.ls_R_factor_R_free                       0.2354 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.130 
_refine.ls_number_reflns_R_free                  1177 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_refine.B_iso_mean                               42.32 
_refine.aniso_B[1][1]                            0.96600 
_refine.aniso_B[2][2]                            -4.68940 
_refine.aniso_B[3][3]                            3.72350 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -5.97430 
_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             0.087 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.088 
_refine.pdbx_overall_SU_R_Blow_DPI               0.093 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.093 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HYP 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_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         28 
_refine_hist.number_atoms_solvent             181 
_refine_hist.number_atoms_total               1292 
_refine_hist.d_res_high                       1.569 
_refine_hist.d_res_low                        48.50 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1156 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.96  ? 2.00  1577 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  389  '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 1156 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.58  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.43 ? ?     ?    '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  1009 '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                       1.57 
_refine_ls_shell.d_res_low                        1.58 
_refine_ls_shell.number_reflns_R_work             430 
_refine_ls_shell.R_factor_R_work                  0.4082 
_refine_ls_shell.percent_reflns_obs               86.45 
_refine_ls_shell.R_factor_R_free                  0.4156 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.32 
_refine_ls_shell.number_reflns_R_free             29 
_refine_ls_shell.number_reflns_all                459 
_refine_ls_shell.R_factor_all                     0.4087 
# 
_struct.entry_id                  7HYP 
_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-0036225-001 (A71EV2A-x4403)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HYP 
_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 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              7HYP 
_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 
# 
_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 ? ? ? ? ? ? ? 2.310 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.366 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.381 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.191 ? ? 
# 
_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_555 111.6 ? 
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_555 106.3 ? 
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_555 115.7 ? 
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_555 111.0 ? 
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 98.8  ? 
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_555 113.5 ? 
# 
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 ? THR A 120 ? GLY A 119 THR A 126 
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 ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HYP 
_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_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     14 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -97.54 
_pdbx_validate_torsion.psi             37.42 
# 
_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         15.1689 
_pdbx_refine_tls.origin_y         7.6809 
_pdbx_refine_tls.origin_z         13.8557 
_pdbx_refine_tls.T[1][1]          -0.0163 
_pdbx_refine_tls.T[2][2]          -0.0637 
_pdbx_refine_tls.T[3][3]          0.0306 
_pdbx_refine_tls.T[1][2]          -0.0001 
_pdbx_refine_tls.T[1][3]          -0.0493 
_pdbx_refine_tls.T[2][3]          0.0143 
_pdbx_refine_tls.L[1][1]          2.2481 
_pdbx_refine_tls.L[2][2]          4.8707 
_pdbx_refine_tls.L[3][3]          0.6547 
_pdbx_refine_tls.L[1][2]          -0.8572 
_pdbx_refine_tls.L[1][3]          -0.2026 
_pdbx_refine_tls.L[2][3]          -0.1061 
_pdbx_refine_tls.S[1][1]          -0.0801 
_pdbx_refine_tls.S[1][2]          0.0593 
_pdbx_refine_tls.S[1][3]          0.3368 
_pdbx_refine_tls.S[2][1]          0.0955 
_pdbx_refine_tls.S[2][2]          0.0563 
_pdbx_refine_tls.S[2][3]          -0.4575 
_pdbx_refine_tls.S[3][1]          0.0088 
_pdbx_refine_tls.S[3][2]          -0.0916 
_pdbx_refine_tls.S[3][3]          0.0237 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       481 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   8.26 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A 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 
A1BPZ N1   N  N N 1   
A1BPZ C4   C  N N 2   
A1BPZ C5   C  N N 3   
A1BPZ C6   C  N N 4   
A1BPZ C7   C  Y N 5   
A1BPZ C8   C  Y N 6   
A1BPZ C10  C  Y N 7   
A1BPZ C13  C  N N 8   
A1BPZ O3   O  N N 9   
A1BPZ S    S  N N 10  
A1BPZ O2   O  N N 11  
A1BPZ N2   N  N N 12  
A1BPZ C12  C  Y N 13  
A1BPZ C11  C  Y N 14  
A1BPZ C9   C  Y N 15  
A1BPZ O1   O  N N 16  
A1BPZ C3   C  N N 17  
A1BPZ C2   C  N N 18  
A1BPZ C14  C  N N 19  
A1BPZ C1   C  N S 20  
A1BPZ C    C  N N 21  
A1BPZ O    O  N N 22  
A1BPZ N    N  N N 23  
A1BPZ H8   H  N N 24  
A1BPZ H7   H  N N 25  
A1BPZ H10  H  N N 26  
A1BPZ H9   H  N N 27  
A1BPZ H11  H  N N 28  
A1BPZ H13  H  N N 29  
A1BPZ H16  H  N N 30  
A1BPZ H15  H  N N 31  
A1BPZ H18  H  N N 32  
A1BPZ H17  H  N N 33  
A1BPZ H14  H  N N 34  
A1BPZ H12  H  N N 35  
A1BPZ H6   H  N N 36  
A1BPZ H5   H  N N 37  
A1BPZ H4   H  N N 38  
A1BPZ H3   H  N N 39  
A1BPZ H20  H  N N 40  
A1BPZ H19  H  N N 41  
A1BPZ H    H  N N 42  
A1BPZ H1   H  N N 43  
A1BPZ H2   H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
DMS   S    S  N N 132 
DMS   O    O  N N 133 
DMS   C1   C  N N 134 
DMS   C2   C  N N 135 
DMS   H11  H  N N 136 
DMS   H12  H  N N 137 
DMS   H13  H  N N 138 
DMS   H21  H  N N 139 
DMS   H22  H  N N 140 
DMS   H23  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
HOH   O    O  N N 212 
HOH   H1   H  N N 213 
HOH   H2   H  N N 214 
ILE   N    N  N N 215 
ILE   CA   C  N S 216 
ILE   C    C  N N 217 
ILE   O    O  N N 218 
ILE   CB   C  N S 219 
ILE   CG1  C  N N 220 
ILE   CG2  C  N N 221 
ILE   CD1  C  N N 222 
ILE   OXT  O  N N 223 
ILE   H    H  N N 224 
ILE   H2   H  N N 225 
ILE   HA   H  N N 226 
ILE   HB   H  N N 227 
ILE   HG12 H  N N 228 
ILE   HG13 H  N N 229 
ILE   HG21 H  N N 230 
ILE   HG22 H  N N 231 
ILE   HG23 H  N N 232 
ILE   HD11 H  N N 233 
ILE   HD12 H  N N 234 
ILE   HD13 H  N N 235 
ILE   HXT  H  N N 236 
LEU   N    N  N N 237 
LEU   CA   C  N S 238 
LEU   C    C  N N 239 
LEU   O    O  N N 240 
LEU   CB   C  N N 241 
LEU   CG   C  N N 242 
LEU   CD1  C  N N 243 
LEU   CD2  C  N N 244 
LEU   OXT  O  N N 245 
LEU   H    H  N N 246 
LEU   H2   H  N N 247 
LEU   HA   H  N N 248 
LEU   HB2  H  N N 249 
LEU   HB3  H  N N 250 
LEU   HG   H  N N 251 
LEU   HD11 H  N N 252 
LEU   HD12 H  N N 253 
LEU   HD13 H  N N 254 
LEU   HD21 H  N N 255 
LEU   HD22 H  N N 256 
LEU   HD23 H  N N 257 
LEU   HXT  H  N N 258 
LYS   N    N  N N 259 
LYS   CA   C  N S 260 
LYS   C    C  N N 261 
LYS   O    O  N N 262 
LYS   CB   C  N N 263 
LYS   CG   C  N N 264 
LYS   CD   C  N N 265 
LYS   CE   C  N N 266 
LYS   NZ   N  N N 267 
LYS   OXT  O  N N 268 
LYS   H    H  N N 269 
LYS   H2   H  N N 270 
LYS   HA   H  N N 271 
LYS   HB2  H  N N 272 
LYS   HB3  H  N N 273 
LYS   HG2  H  N N 274 
LYS   HG3  H  N N 275 
LYS   HD2  H  N N 276 
LYS   HD3  H  N N 277 
LYS   HE2  H  N N 278 
LYS   HE3  H  N N 279 
LYS   HZ1  H  N N 280 
LYS   HZ2  H  N N 281 
LYS   HZ3  H  N N 282 
LYS   HXT  H  N N 283 
MET   N    N  N N 284 
MET   CA   C  N S 285 
MET   C    C  N N 286 
MET   O    O  N N 287 
MET   CB   C  N N 288 
MET   CG   C  N N 289 
MET   SD   S  N N 290 
MET   CE   C  N N 291 
MET   OXT  O  N N 292 
MET   H    H  N N 293 
MET   H2   H  N N 294 
MET   HA   H  N N 295 
MET   HB2  H  N N 296 
MET   HB3  H  N N 297 
MET   HG2  H  N N 298 
MET   HG3  H  N N 299 
MET   HE1  H  N N 300 
MET   HE2  H  N N 301 
MET   HE3  H  N N 302 
MET   HXT  H  N N 303 
PHE   N    N  N N 304 
PHE   CA   C  N S 305 
PHE   C    C  N N 306 
PHE   O    O  N N 307 
PHE   CB   C  N N 308 
PHE   CG   C  Y N 309 
PHE   CD1  C  Y N 310 
PHE   CD2  C  Y N 311 
PHE   CE1  C  Y N 312 
PHE   CE2  C  Y N 313 
PHE   CZ   C  Y N 314 
PHE   OXT  O  N N 315 
PHE   H    H  N N 316 
PHE   H2   H  N N 317 
PHE   HA   H  N N 318 
PHE   HB2  H  N N 319 
PHE   HB3  H  N N 320 
PHE   HD1  H  N N 321 
PHE   HD2  H  N N 322 
PHE   HE1  H  N N 323 
PHE   HE2  H  N N 324 
PHE   HZ   H  N N 325 
PHE   HXT  H  N N 326 
PRO   N    N  N N 327 
PRO   CA   C  N S 328 
PRO   C    C  N N 329 
PRO   O    O  N N 330 
PRO   CB   C  N N 331 
PRO   CG   C  N N 332 
PRO   CD   C  N N 333 
PRO   OXT  O  N N 334 
PRO   H    H  N N 335 
PRO   HA   H  N N 336 
PRO   HB2  H  N N 337 
PRO   HB3  H  N N 338 
PRO   HG2  H  N N 339 
PRO   HG3  H  N N 340 
PRO   HD2  H  N N 341 
PRO   HD3  H  N N 342 
PRO   HXT  H  N N 343 
SER   N    N  N N 344 
SER   CA   C  N S 345 
SER   C    C  N N 346 
SER   O    O  N N 347 
SER   CB   C  N N 348 
SER   OG   O  N N 349 
SER   OXT  O  N N 350 
SER   H    H  N N 351 
SER   H2   H  N N 352 
SER   HA   H  N N 353 
SER   HB2  H  N N 354 
SER   HB3  H  N N 355 
SER   HG   H  N N 356 
SER   HXT  H  N N 357 
THR   N    N  N N 358 
THR   CA   C  N S 359 
THR   C    C  N N 360 
THR   O    O  N N 361 
THR   CB   C  N R 362 
THR   OG1  O  N N 363 
THR   CG2  C  N N 364 
THR   OXT  O  N N 365 
THR   H    H  N N 366 
THR   H2   H  N N 367 
THR   HA   H  N N 368 
THR   HB   H  N N 369 
THR   HG1  H  N N 370 
THR   HG21 H  N N 371 
THR   HG22 H  N N 372 
THR   HG23 H  N N 373 
THR   HXT  H  N N 374 
TRP   N    N  N N 375 
TRP   CA   C  N S 376 
TRP   C    C  N N 377 
TRP   O    O  N N 378 
TRP   CB   C  N N 379 
TRP   CG   C  Y N 380 
TRP   CD1  C  Y N 381 
TRP   CD2  C  Y N 382 
TRP   NE1  N  Y N 383 
TRP   CE2  C  Y N 384 
TRP   CE3  C  Y N 385 
TRP   CZ2  C  Y N 386 
TRP   CZ3  C  Y N 387 
TRP   CH2  C  Y N 388 
TRP   OXT  O  N N 389 
TRP   H    H  N N 390 
TRP   H2   H  N N 391 
TRP   HA   H  N N 392 
TRP   HB2  H  N N 393 
TRP   HB3  H  N N 394 
TRP   HD1  H  N N 395 
TRP   HE1  H  N N 396 
TRP   HE3  H  N N 397 
TRP   HZ2  H  N N 398 
TRP   HZ3  H  N N 399 
TRP   HH2  H  N N 400 
TRP   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
ZN    ZN   ZN N N 445 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1BPZ N   C    sing N N 1   
A1BPZ O   C    doub N N 2   
A1BPZ C   C1   sing N N 3   
A1BPZ C1  C2   sing N N 4   
A1BPZ C2  C3   sing N N 5   
A1BPZ C3  C4   sing N N 6   
A1BPZ C4  N1   sing N N 7   
A1BPZ N1  C5   sing N N 8   
A1BPZ O1  C5   doub N N 9   
A1BPZ C5  C6   sing N N 10  
A1BPZ C6  C7   sing N N 11  
A1BPZ C7  C8   doub Y N 12  
A1BPZ C8  C9   sing Y N 13  
A1BPZ C9  C10  doub Y N 14  
A1BPZ C10 C11  sing Y N 15  
A1BPZ C11 C12  doub Y N 16  
A1BPZ C7  C12  sing Y N 17  
A1BPZ C12 C13  sing N N 18  
A1BPZ C13 S    sing N N 19  
A1BPZ N2  S    sing N N 20  
A1BPZ O2  S    doub N N 21  
A1BPZ S   O3   doub N N 22  
A1BPZ C14 N1   sing N N 23  
A1BPZ C1  C14  sing N N 24  
A1BPZ C4  H8   sing N N 25  
A1BPZ C4  H7   sing N N 26  
A1BPZ C6  H10  sing N N 27  
A1BPZ C6  H9   sing N N 28  
A1BPZ C8  H11  sing N N 29  
A1BPZ C10 H13  sing N N 30  
A1BPZ C13 H16  sing N N 31  
A1BPZ C13 H15  sing N N 32  
A1BPZ N2  H18  sing N N 33  
A1BPZ N2  H17  sing N N 34  
A1BPZ C11 H14  sing N N 35  
A1BPZ C9  H12  sing N N 36  
A1BPZ C3  H6   sing N N 37  
A1BPZ C3  H5   sing N N 38  
A1BPZ C2  H4   sing N N 39  
A1BPZ C2  H3   sing N N 40  
A1BPZ C14 H20  sing N N 41  
A1BPZ C14 H19  sing N N 42  
A1BPZ C1  H    sing N N 43  
A1BPZ N   H1   sing N N 44  
A1BPZ N   H2   sing N N 45  
ALA   N   CA   sing N N 46  
ALA   N   H    sing N N 47  
ALA   N   H2   sing N N 48  
ALA   CA  C    sing N N 49  
ALA   CA  CB   sing N N 50  
ALA   CA  HA   sing N N 51  
ALA   C   O    doub N N 52  
ALA   C   OXT  sing N N 53  
ALA   CB  HB1  sing N N 54  
ALA   CB  HB2  sing N N 55  
ALA   CB  HB3  sing N N 56  
ALA   OXT HXT  sing N N 57  
ARG   N   CA   sing N N 58  
ARG   N   H    sing N N 59  
ARG   N   H2   sing N N 60  
ARG   CA  C    sing N N 61  
ARG   CA  CB   sing N N 62  
ARG   CA  HA   sing N N 63  
ARG   C   O    doub N N 64  
ARG   C   OXT  sing N N 65  
ARG   CB  CG   sing N N 66  
ARG   CB  HB2  sing N N 67  
ARG   CB  HB3  sing N N 68  
ARG   CG  CD   sing N N 69  
ARG   CG  HG2  sing N N 70  
ARG   CG  HG3  sing N N 71  
ARG   CD  NE   sing N N 72  
ARG   CD  HD2  sing N N 73  
ARG   CD  HD3  sing N N 74  
ARG   NE  CZ   sing N N 75  
ARG   NE  HE   sing N N 76  
ARG   CZ  NH1  sing N N 77  
ARG   CZ  NH2  doub N N 78  
ARG   NH1 HH11 sing N N 79  
ARG   NH1 HH12 sing N N 80  
ARG   NH2 HH21 sing N N 81  
ARG   NH2 HH22 sing N N 82  
ARG   OXT HXT  sing N N 83  
ASN   N   CA   sing N N 84  
ASN   N   H    sing N N 85  
ASN   N   H2   sing N N 86  
ASN   CA  C    sing N N 87  
ASN   CA  CB   sing N N 88  
ASN   CA  HA   sing N N 89  
ASN   C   O    doub N N 90  
ASN   C   OXT  sing N N 91  
ASN   CB  CG   sing N N 92  
ASN   CB  HB2  sing N N 93  
ASN   CB  HB3  sing N N 94  
ASN   CG  OD1  doub N N 95  
ASN   CG  ND2  sing N N 96  
ASN   ND2 HD21 sing N N 97  
ASN   ND2 HD22 sing N N 98  
ASN   OXT HXT  sing N N 99  
ASP   N   CA   sing N N 100 
ASP   N   H    sing N N 101 
ASP   N   H2   sing N N 102 
ASP   CA  C    sing N N 103 
ASP   CA  CB   sing N N 104 
ASP   CA  HA   sing N N 105 
ASP   C   O    doub N N 106 
ASP   C   OXT  sing N N 107 
ASP   CB  CG   sing N N 108 
ASP   CB  HB2  sing N N 109 
ASP   CB  HB3  sing N N 110 
ASP   CG  OD1  doub N N 111 
ASP   CG  OD2  sing N N 112 
ASP   OD2 HD2  sing N N 113 
ASP   OXT HXT  sing N N 114 
CYS   N   CA   sing N N 115 
CYS   N   H    sing N N 116 
CYS   N   H2   sing N N 117 
CYS   CA  C    sing N N 118 
CYS   CA  CB   sing N N 119 
CYS   CA  HA   sing N N 120 
CYS   C   O    doub N N 121 
CYS   C   OXT  sing N N 122 
CYS   CB  SG   sing N N 123 
CYS   CB  HB2  sing N N 124 
CYS   CB  HB3  sing N N 125 
CYS   SG  HG   sing N N 126 
CYS   OXT HXT  sing N N 127 
DMS   S   O    doub N N 128 
DMS   S   C1   sing N N 129 
DMS   S   C2   sing N N 130 
DMS   C1  H11  sing N N 131 
DMS   C1  H12  sing N N 132 
DMS   C1  H13  sing N N 133 
DMS   C2  H21  sing N N 134 
DMS   C2  H22  sing N N 135 
DMS   C2  H23  sing N N 136 
GLN   N   CA   sing N N 137 
GLN   N   H    sing N N 138 
GLN   N   H2   sing N N 139 
GLN   CA  C    sing N N 140 
GLN   CA  CB   sing N N 141 
GLN   CA  HA   sing N N 142 
GLN   C   O    doub N N 143 
GLN   C   OXT  sing N N 144 
GLN   CB  CG   sing N N 145 
GLN   CB  HB2  sing N N 146 
GLN   CB  HB3  sing N N 147 
GLN   CG  CD   sing N N 148 
GLN   CG  HG2  sing N N 149 
GLN   CG  HG3  sing N N 150 
GLN   CD  OE1  doub N N 151 
GLN   CD  NE2  sing N N 152 
GLN   NE2 HE21 sing N N 153 
GLN   NE2 HE22 sing N N 154 
GLN   OXT HXT  sing N N 155 
GLU   N   CA   sing N N 156 
GLU   N   H    sing N N 157 
GLU   N   H2   sing N N 158 
GLU   CA  C    sing N N 159 
GLU   CA  CB   sing N N 160 
GLU   CA  HA   sing N N 161 
GLU   C   O    doub N N 162 
GLU   C   OXT  sing N N 163 
GLU   CB  CG   sing N N 164 
GLU   CB  HB2  sing N N 165 
GLU   CB  HB3  sing N N 166 
GLU   CG  CD   sing N N 167 
GLU   CG  HG2  sing N N 168 
GLU   CG  HG3  sing N N 169 
GLU   CD  OE1  doub N N 170 
GLU   CD  OE2  sing N N 171 
GLU   OE2 HE2  sing N N 172 
GLU   OXT HXT  sing N N 173 
GLY   N   CA   sing N N 174 
GLY   N   H    sing N N 175 
GLY   N   H2   sing N N 176 
GLY   CA  C    sing N N 177 
GLY   CA  HA2  sing N N 178 
GLY   CA  HA3  sing N N 179 
GLY   C   O    doub N N 180 
GLY   C   OXT  sing N N 181 
GLY   OXT HXT  sing N N 182 
HIS   N   CA   sing N N 183 
HIS   N   H    sing N N 184 
HIS   N   H2   sing N N 185 
HIS   CA  C    sing N N 186 
HIS   CA  CB   sing N N 187 
HIS   CA  HA   sing N N 188 
HIS   C   O    doub N N 189 
HIS   C   OXT  sing N N 190 
HIS   CB  CG   sing N N 191 
HIS   CB  HB2  sing N N 192 
HIS   CB  HB3  sing N N 193 
HIS   CG  ND1  sing Y N 194 
HIS   CG  CD2  doub Y N 195 
HIS   ND1 CE1  doub Y N 196 
HIS   ND1 HD1  sing N N 197 
HIS   CD2 NE2  sing Y N 198 
HIS   CD2 HD2  sing N N 199 
HIS   CE1 NE2  sing Y N 200 
HIS   CE1 HE1  sing N N 201 
HIS   NE2 HE2  sing N N 202 
HIS   OXT HXT  sing N N 203 
HOH   O   H1   sing N N 204 
HOH   O   H2   sing N N 205 
ILE   N   CA   sing N N 206 
ILE   N   H    sing N N 207 
ILE   N   H2   sing N N 208 
ILE   CA  C    sing N N 209 
ILE   CA  CB   sing N N 210 
ILE   CA  HA   sing N N 211 
ILE   C   O    doub N N 212 
ILE   C   OXT  sing N N 213 
ILE   CB  CG1  sing N N 214 
ILE   CB  CG2  sing N N 215 
ILE   CB  HB   sing N N 216 
ILE   CG1 CD1  sing N N 217 
ILE   CG1 HG12 sing N N 218 
ILE   CG1 HG13 sing N N 219 
ILE   CG2 HG21 sing N N 220 
ILE   CG2 HG22 sing N N 221 
ILE   CG2 HG23 sing N N 222 
ILE   CD1 HD11 sing N N 223 
ILE   CD1 HD12 sing N N 224 
ILE   CD1 HD13 sing N N 225 
ILE   OXT HXT  sing N N 226 
LEU   N   CA   sing N N 227 
LEU   N   H    sing N N 228 
LEU   N   H2   sing N N 229 
LEU   CA  C    sing N N 230 
LEU   CA  CB   sing N N 231 
LEU   CA  HA   sing N N 232 
LEU   C   O    doub N N 233 
LEU   C   OXT  sing N N 234 
LEU   CB  CG   sing N N 235 
LEU   CB  HB2  sing N N 236 
LEU   CB  HB3  sing N N 237 
LEU   CG  CD1  sing N N 238 
LEU   CG  CD2  sing N N 239 
LEU   CG  HG   sing N N 240 
LEU   CD1 HD11 sing N N 241 
LEU   CD1 HD12 sing N N 242 
LEU   CD1 HD13 sing N N 243 
LEU   CD2 HD21 sing N N 244 
LEU   CD2 HD22 sing N N 245 
LEU   CD2 HD23 sing N N 246 
LEU   OXT HXT  sing N N 247 
LYS   N   CA   sing N N 248 
LYS   N   H    sing N N 249 
LYS   N   H2   sing N N 250 
LYS   CA  C    sing N N 251 
LYS   CA  CB   sing N N 252 
LYS   CA  HA   sing N N 253 
LYS   C   O    doub N N 254 
LYS   C   OXT  sing N N 255 
LYS   CB  CG   sing N N 256 
LYS   CB  HB2  sing N N 257 
LYS   CB  HB3  sing N N 258 
LYS   CG  CD   sing N N 259 
LYS   CG  HG2  sing N N 260 
LYS   CG  HG3  sing N N 261 
LYS   CD  CE   sing N N 262 
LYS   CD  HD2  sing N N 263 
LYS   CD  HD3  sing N N 264 
LYS   CE  NZ   sing N N 265 
LYS   CE  HE2  sing N N 266 
LYS   CE  HE3  sing N N 267 
LYS   NZ  HZ1  sing N N 268 
LYS   NZ  HZ2  sing N N 269 
LYS   NZ  HZ3  sing N N 270 
LYS   OXT HXT  sing N N 271 
MET   N   CA   sing N N 272 
MET   N   H    sing N N 273 
MET   N   H2   sing N N 274 
MET   CA  C    sing N N 275 
MET   CA  CB   sing N N 276 
MET   CA  HA   sing N N 277 
MET   C   O    doub N N 278 
MET   C   OXT  sing N N 279 
MET   CB  CG   sing N N 280 
MET   CB  HB2  sing N N 281 
MET   CB  HB3  sing N N 282 
MET   CG  SD   sing N N 283 
MET   CG  HG2  sing N N 284 
MET   CG  HG3  sing N N 285 
MET   SD  CE   sing N N 286 
MET   CE  HE1  sing N N 287 
MET   CE  HE2  sing N N 288 
MET   CE  HE3  sing N N 289 
MET   OXT HXT  sing N N 290 
PHE   N   CA   sing N N 291 
PHE   N   H    sing N N 292 
PHE   N   H2   sing N N 293 
PHE   CA  C    sing N N 294 
PHE   CA  CB   sing N N 295 
PHE   CA  HA   sing N N 296 
PHE   C   O    doub N N 297 
PHE   C   OXT  sing N N 298 
PHE   CB  CG   sing N N 299 
PHE   CB  HB2  sing N N 300 
PHE   CB  HB3  sing N N 301 
PHE   CG  CD1  doub Y N 302 
PHE   CG  CD2  sing Y N 303 
PHE   CD1 CE1  sing Y N 304 
PHE   CD1 HD1  sing N N 305 
PHE   CD2 CE2  doub Y N 306 
PHE   CD2 HD2  sing N N 307 
PHE   CE1 CZ   doub Y N 308 
PHE   CE1 HE1  sing N N 309 
PHE   CE2 CZ   sing Y N 310 
PHE   CE2 HE2  sing N N 311 
PHE   CZ  HZ   sing N N 312 
PHE   OXT HXT  sing N N 313 
PRO   N   CA   sing N N 314 
PRO   N   CD   sing N N 315 
PRO   N   H    sing N N 316 
PRO   CA  C    sing N N 317 
PRO   CA  CB   sing N N 318 
PRO   CA  HA   sing N N 319 
PRO   C   O    doub N N 320 
PRO   C   OXT  sing N N 321 
PRO   CB  CG   sing N N 322 
PRO   CB  HB2  sing N N 323 
PRO   CB  HB3  sing N N 324 
PRO   CG  CD   sing N N 325 
PRO   CG  HG2  sing N N 326 
PRO   CG  HG3  sing N N 327 
PRO   CD  HD2  sing N N 328 
PRO   CD  HD3  sing N N 329 
PRO   OXT HXT  sing N N 330 
SER   N   CA   sing N N 331 
SER   N   H    sing N N 332 
SER   N   H2   sing N N 333 
SER   CA  C    sing N N 334 
SER   CA  CB   sing N N 335 
SER   CA  HA   sing N N 336 
SER   C   O    doub N N 337 
SER   C   OXT  sing N N 338 
SER   CB  OG   sing N N 339 
SER   CB  HB2  sing N N 340 
SER   CB  HB3  sing N N 341 
SER   OG  HG   sing N N 342 
SER   OXT HXT  sing N N 343 
THR   N   CA   sing N N 344 
THR   N   H    sing N N 345 
THR   N   H2   sing N N 346 
THR   CA  C    sing N N 347 
THR   CA  CB   sing N N 348 
THR   CA  HA   sing N N 349 
THR   C   O    doub N N 350 
THR   C   OXT  sing N N 351 
THR   CB  OG1  sing N N 352 
THR   CB  CG2  sing N N 353 
THR   CB  HB   sing N N 354 
THR   OG1 HG1  sing N N 355 
THR   CG2 HG21 sing N N 356 
THR   CG2 HG22 sing N N 357 
THR   CG2 HG23 sing N N 358 
THR   OXT HXT  sing N N 359 
TRP   N   CA   sing N N 360 
TRP   N   H    sing N N 361 
TRP   N   H2   sing N N 362 
TRP   CA  C    sing N N 363 
TRP   CA  CB   sing N N 364 
TRP   CA  HA   sing N N 365 
TRP   C   O    doub N N 366 
TRP   C   OXT  sing N N 367 
TRP   CB  CG   sing N N 368 
TRP   CB  HB2  sing N N 369 
TRP   CB  HB3  sing N N 370 
TRP   CG  CD1  doub Y N 371 
TRP   CG  CD2  sing Y N 372 
TRP   CD1 NE1  sing Y N 373 
TRP   CD1 HD1  sing N N 374 
TRP   CD2 CE2  doub Y N 375 
TRP   CD2 CE3  sing Y N 376 
TRP   NE1 CE2  sing Y N 377 
TRP   NE1 HE1  sing N N 378 
TRP   CE2 CZ2  sing Y N 379 
TRP   CE3 CZ3  doub Y N 380 
TRP   CE3 HE3  sing N N 381 
TRP   CZ2 CH2  doub Y N 382 
TRP   CZ2 HZ2  sing N N 383 
TRP   CZ3 CH2  sing Y N 384 
TRP   CZ3 HZ3  sing N N 385 
TRP   CH2 HH2  sing N N 386 
TRP   OXT HXT  sing N N 387 
TYR   N   CA   sing N N 388 
TYR   N   H    sing N N 389 
TYR   N   H2   sing N N 390 
TYR   CA  C    sing N N 391 
TYR   CA  CB   sing N N 392 
TYR   CA  HA   sing N N 393 
TYR   C   O    doub N N 394 
TYR   C   OXT  sing N N 395 
TYR   CB  CG   sing N N 396 
TYR   CB  HB2  sing N N 397 
TYR   CB  HB3  sing N N 398 
TYR   CG  CD1  doub Y N 399 
TYR   CG  CD2  sing Y N 400 
TYR   CD1 CE1  sing Y N 401 
TYR   CD1 HD1  sing N N 402 
TYR   CD2 CE2  doub Y N 403 
TYR   CD2 HD2  sing N N 404 
TYR   CE1 CZ   doub Y N 405 
TYR   CE1 HE1  sing N N 406 
TYR   CE2 CZ   sing Y N 407 
TYR   CE2 HE2  sing N N 408 
TYR   CZ  OH   sing N N 409 
TYR   OH  HH   sing N N 410 
TYR   OXT HXT  sing N N 411 
VAL   N   CA   sing N N 412 
VAL   N   H    sing N N 413 
VAL   N   H2   sing N N 414 
VAL   CA  C    sing N N 415 
VAL   CA  CB   sing N N 416 
VAL   CA  HA   sing N N 417 
VAL   C   O    doub N N 418 
VAL   C   OXT  sing N N 419 
VAL   CB  CG1  sing N N 420 
VAL   CB  CG2  sing N N 421 
VAL   CB  HB   sing N N 422 
VAL   CG1 HG11 sing N N 423 
VAL   CG1 HG12 sing N N 424 
VAL   CG1 HG13 sing N N 425 
VAL   CG2 HG21 sing N N 426 
VAL   CG2 HG22 sing N N 427 
VAL   CG2 HG23 sing N N 428 
VAL   OXT HXT  sing N N 429 
# 
_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                    7HYP 
_atom_sites.fract_transf_matrix[1][1]   0.011392 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000489 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017178 
_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]   0.030549 
_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   ? 19.047 6.965   24.098 1.00 40.92 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.228 7.110   23.260 1.00 41.66 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.338 5.981   22.207 1.00 40.58 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.652 4.962   22.312 1.00 40.81 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.486 7.194   24.128 1.00 44.92 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.873 5.906   24.575 1.00 49.70 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.170 6.183   21.194 1.00 39.10 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.381 5.170   20.173 1.00 37.62 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.669 5.712   18.790 1.00 36.12 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.234 6.815   18.443 1.00 35.29 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.302 4.879   17.946 1.00 34.95 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.652 5.307   16.603 1.00 34.56 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.639 4.165   15.599 1.00 33.79 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.760 2.994   15.975 1.00 35.07 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.052 5.946   16.644 1.00 34.99 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.531 4.493   14.312 1.00 32.05 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.660 3.516   13.229 1.00 31.70 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.084 3.698   12.671 1.00 33.90 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.515 4.848   12.464 1.00 34.68 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.633 3.781   12.084 1.00 30.60 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.172 3.856   12.590 1.00 29.08 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.759 2.731   10.967 1.00 31.01 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.169 4.522   11.516 1.00 28.53 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.802 2.583   12.390 1.00 35.07 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.150 2.643   11.798 1.00 36.93 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.147 1.912   10.444 1.00 38.17 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.110 0.686   10.401 1.00 39.08 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.217 2.072   12.753 1.00 37.35 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.356 2.885   14.019 1.00 39.85 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.144 4.032   14.052 1.00 41.22 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.680 2.527   15.176 1.00 41.64 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.212 4.827   15.189 1.00 42.67 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.759 3.302   16.326 1.00 43.22 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.542 4.442   16.334 1.00 44.27 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.619 5.196   17.473 1.00 47.12 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.069 2.668   9.338  1.00 38.34 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.050 2.100   7.993  1.00 38.68 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.202 2.687   7.182  1.00 40.50 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.281 3.904   7.010  1.00 41.46 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.670 2.273   7.283  1.00 39.21 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.215 3.753   7.257  1.00 38.12 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.696 1.654   5.879  1.00 39.81 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.130 1.833   6.741  1.00 41.06 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.312 2.273   6.003  1.00 42.56 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.128 3.258   6.817  1.00 44.69 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.324 3.043   8.017  1.00 45.13 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.504 4.403   6.212  1.00 45.46 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.211 5.429   6.944  1.00 46.63 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.242 6.524   7.427  1.00 45.83 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.594 7.705   7.458  1.00 46.04 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.378 5.963   6.124  1.00 50.16 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.444 4.904   5.982  1.00 57.63 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.332 4.778   6.829  1.00 60.78 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.350 4.075   4.941  1.00 58.85 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.018 6.126   7.838  1.00 44.56 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.018 7.085   8.327  1.00 43.68 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.493 6.702   9.724  1.00 42.04 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.405 5.527   10.069 1.00 41.03 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.827 7.226   7.344  1.00 44.46 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.168 7.697   5.942  1.00 46.02 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.769 8.933   5.726  1.00 47.45 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.787 6.960   4.829  1.00 46.96 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.059 9.379   4.440  1.00 48.86 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.055 7.404   3.538  1.00 48.70 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.714 8.605   3.347  1.00 49.95 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 27.973 9.063   2.070  1.00 51.88 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.171 7.705   10.532 1.00 41.91 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.594 7.527   11.861 1.00 41.08 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.297 8.348   11.847 1.00 39.71 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.331 9.560   11.650 1.00 39.50 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.540 8.034   12.962 1.00 42.48 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.892 8.258   14.328 1.00 45.41 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.943 8.560   15.392 1.00 48.53 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.479 9.552   16.368 1.00 50.08 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.969 9.255   17.560 1.00 51.15 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.821 7.988   17.932 1.00 51.05 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.581 10.221  18.380 1.00 50.61 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.164 7.681   12.004 1.00 37.54 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.866 8.345   11.974 1.00 36.23 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.351 8.427   13.401 1.00 36.01 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.194 7.388   14.060 1.00 35.70 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.845 7.585   11.081 1.00 35.41 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.596 8.436   10.852 1.00 34.83 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.463 7.157   9.745  1.00 35.11 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.102 9.642   13.887 1.00 34.44 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.594 9.856   15.239 1.00 34.56 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.400 10.846  15.205 1.00 33.18 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.169 11.550  14.192 1.00 33.28 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.701 10.429  16.187 1.00 36.56 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.785 9.406   16.477 1.00 37.78 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.279 11.726  15.621 1.00 37.29 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.674 10.962  16.344 1.00 31.63 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.649 11.998  16.494 1.00 30.95 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.418 13.347  16.522 1.00 32.83 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.414 13.484  17.250 1.00 33.53 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.924 11.866  17.838 1.00 30.69 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.070 10.606  17.981 1.00 30.89 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.512 9.605   18.562 1.00 30.96 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.856 10.634  17.444 1.00 29.49 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.950 14.332  15.767 1.00 32.92 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.613 15.631  15.700 1.00 34.57 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.695 16.280  17.081 1.00 36.84 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.767 16.744  17.452 1.00 38.23 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.896 16.530  14.707 1.00 34.17 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.697 17.790  14.318 1.00 37.20 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.779 18.672  13.512 1.00 40.30 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.396 19.915  13.040 1.00 44.23 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.365 21.069  13.701 1.00 48.03 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.825 21.136  14.912 1.00 45.72 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.878 22.166  13.158 1.00 49.84 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.605 16.193  17.888 1.00 37.41 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.574 16.771  19.240 1.00 38.65 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.578 16.103  20.220 1.00 41.14 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.834 16.655  21.285 1.00 41.48 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.135 16.824  19.816 1.00 38.68 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.585 15.511  20.293 1.00 39.58 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.963 14.629  19.419 1.00 39.94 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.566 14.978  21.540 1.00 40.13 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.583 13.594  20.156 1.00 40.42 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.923 13.754  21.439 1.00 40.97 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.179 14.967  19.837 1.00 42.42 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.177 14.261  20.646 1.00 44.26 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.585 14.265  20.016 1.00 45.81 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.457 13.580  20.528 1.00 46.69 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.734 12.798  20.920 1.00 44.20 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.444 12.628  21.717 1.00 45.12 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.106 11.145  21.911 1.00 44.90 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.533 13.327  23.079 1.00 45.98 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.800 14.961  18.887 1.00 46.60 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.111 14.966  18.231 1.00 48.19 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.195 15.587  19.133 1.00 50.88 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.880 16.485  19.916 1.00 50.77 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.034 15.720  16.916 1.00 48.17 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.447 15.070  19.052 1.00 53.40 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.601 15.562  19.835 1.00 56.07 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.496 16.540  19.008 1.00 57.92 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.222 16.790  17.826 1.00 57.43 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.402 14.380  20.458 1.00 58.66 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.158 13.696  19.460 1.00 60.70 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.551 13.420  21.245 1.00 59.42 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.559 17.121  19.648 1.00 59.64 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.519 18.017  19.022 1.00 61.67 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.127 17.364  17.767 1.00 61.65 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.109 17.960  16.679 1.00 61.30 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.609 18.361  20.075 1.00 64.79 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 32.870 18.982  19.556 1.00 68.91 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 33.060 20.359  19.584 1.00 71.14 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 34.004 18.390  19.109 1.00 70.79 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 34.285 20.556  19.120 1.00 72.40 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 34.893 19.397  18.824 1.00 72.38 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.621 16.123  17.927 1.00 62.44 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.264 15.323  16.895 1.00 63.18 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.355 15.191  15.674 1.00 62.10 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.826 15.374  14.547 1.00 62.91 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.659 13.947  17.455 1.00 66.93 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.448 14.002  18.755 1.00 73.57 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.641 13.677  18.804 1.00 75.25 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.800 14.417  19.846 1.00 75.49 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.043 14.941  15.901 1.00 59.91 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.033 14.835  14.846 1.00 57.50 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.903 16.115  13.982 1.00 55.73 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.949 16.007  12.761 1.00 54.62 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.647 14.449  15.427 1.00 56.33 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.571 13.085  16.083 1.00 55.22 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.167 12.142  15.552 1.00 54.22 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.902 12.969  17.126 1.00 55.69 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.673 17.297  14.592 1.00 56.03 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.523 18.572  13.856 1.00 56.92 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.794 18.988  13.076 1.00 58.62 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.695 19.505  11.966 1.00 58.26 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.138 19.712  14.807 1.00 56.36 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.706 19.683  15.239 1.00 55.58 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.223 19.306  16.455 1.00 56.03 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.579 20.104  14.470 1.00 55.55 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.855 19.444  16.485 1.00 56.30 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.432 19.936  15.277 1.00 56.06 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.422 20.596  13.169 1.00 56.03 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.148 20.239  14.824 1.00 56.14 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.151 20.919  12.730 1.00 56.77 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.026 20.701  13.540 1.00 56.53 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.970 18.736  13.648 1.00 59.98 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.253 19.028  12.986 1.00 61.98 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.454 18.116  11.740 1.00 63.02 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.136 18.504  10.782 1.00 64.33 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.402 18.780  13.968 1.00 62.50 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.903 16.894  11.781 1.00 61.49 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.044 15.919  10.693 1.00 60.54 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.674 15.668  10.027 1.00 57.38 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.364 14.545  9.635  1.00 57.26 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.603 14.605  11.254 1.00 63.51 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.072 14.647  11.598 1.00 69.14 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.939 14.729  10.717 1.00 71.20 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.391 14.546  12.889 1.00 70.32 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.884 16.731  9.880  1.00 54.09 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.533 16.694  9.352  1.00 52.33 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.452 16.338  7.874  1.00 51.23 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.199 16.885  7.053  1.00 51.16 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.849 18.044  9.620  1.00 51.11 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.452 18.264  9.037  1.00 51.25 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.426 17.325  9.716  1.00 51.62 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.025 19.709  9.212  1.00 50.97 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.561 15.396  7.544  1.00 48.57 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.290 15.033  6.168  1.00 47.98 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.948 15.701  5.754  1.00 47.54 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.863 16.405  4.745  1.00 47.75 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.254 13.490  5.977  1.00 48.31 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.722 13.121  4.596  1.00 48.90 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.622 12.864  6.215  1.00 48.95 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.894 15.484  6.567  1.00 46.06 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.562 15.997  6.291  1.00 45.25 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.758 16.075  7.584  1.00 43.67 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.947 15.256  8.474  1.00 43.99 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.868 15.056  5.283  1.00 44.99 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.410 15.304  5.040  1.00 45.12 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.858 16.151  4.121  1.00 46.28 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.317 14.664  5.709  1.00 44.71 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.482 16.059  4.163  1.00 46.38 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.125 15.160  5.139  1.00 45.47 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.230 13.689  6.712  1.00 44.85 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.868 14.732  5.554  1.00 45.34 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 18.979 13.246  7.105  1.00 44.77 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.817 13.784  6.548  1.00 45.14 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.892 17.080  7.709  1.00 42.01 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.011 17.205  8.865  1.00 41.43 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.702 17.875  8.443  1.00 40.89 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.687 18.738  7.549  1.00 41.15 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.687 17.923  10.054 1.00 43.11 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.223 19.329  9.746  1.00 47.40 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.252 20.502  9.802  1.00 50.29 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.575 21.558  9.210  1.00 50.00 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.166 20.367  10.409 1.00 49.70 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.592 17.443  9.040  1.00 39.01 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.296 18.028  8.756  1.00 37.93 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.575 18.166  10.088 1.00 37.22 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.195 17.159  10.700 1.00 36.53 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.512 17.190  7.718  1.00 39.43 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.228 17.786  7.164  1.00 44.87 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.573 18.562  7.882  1.00 46.09 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.864 17.452  6.010  1.00 47.84 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.412 19.417  10.552 1.00 36.15 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.740 19.720  11.813 0.50 35.85 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.740 19.711  11.818 0.50 36.22 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.290 19.216  11.778 1.00 35.44 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.802 18.644  12.766 1.00 35.08 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.760 21.228  12.068 0.50 36.58 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.752 21.216  12.084 0.50 38.05 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.050 21.557  13.249 0.50 37.35 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.042 21.884  11.054 0.50 40.65 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.602 19.406  10.629 1.00 34.18 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.213 18.964  10.501 1.00 34.45 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.042 17.435  10.594 1.00 32.32 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.933 16.985  10.795 1.00 33.02 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.552 19.513  9.239  1.00 38.00 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.968 18.780  8.098  1.00 43.01 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.101 16.662  10.393 1.00 31.52 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.061 15.201  10.537 1.00 31.14 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.691 14.687  11.849 1.00 30.06 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.687 13.466  12.084 1.00 28.14 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.817 14.537  9.386  1.00 32.22 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.136 14.696  8.064  1.00 33.40 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.036 14.128  6.986  1.00 33.79 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.997 12.664  7.011  1.00 31.46 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.003 11.906  5.919  1.00 33.36 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.081 12.464  4.707  1.00 33.18 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.931 10.588  6.024  1.00 32.22 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.305 15.584  12.656 1.00 29.75 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.065 15.214  13.863 1.00 29.23 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.225 14.246  13.511 1.00 30.02 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.545 13.362  14.314 1.00 29.57 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.181 14.620  14.995 1.00 30.18 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.923 14.378  16.325 1.00 31.11 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.796 15.212  16.696 1.00 29.37 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.695 13.319  16.953 1.00 32.25 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.852 14.401  12.319 1.00 29.88 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.979 13.524  11.927 1.00 30.23 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.281 14.279  11.704 1.00 31.85 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.254 15.393  11.199 1.00 32.72 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.663 12.763  10.626 1.00 30.39 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.606 11.639  10.739 1.00 31.75 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.394 10.963  9.386  1.00 31.69 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.029 10.612  11.813 1.00 32.13 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.403 13.610  11.969 1.00 31.81 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.725 14.122  11.675 1.00 34.64 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.579 12.926  11.308 1.00 36.40 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.515 11.877  11.970 1.00 36.69 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.304 14.923  12.865 1.00 35.41 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.705 15.577  12.673 1.00 37.63 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.796 16.863  13.483 1.00 38.75 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.816 14.626  13.122 1.00 39.08 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.366 13.069  10.227 1.00 37.25 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.278 12.021  9.776  1.00 38.76 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.676 12.611  9.799  1.00 41.87 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.893 13.714  9.275  1.00 41.52 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.923 11.485  8.363  1.00 39.34 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.981 10.499  7.858  1.00 40.17 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.525 10.833  8.344  1.00 38.96 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.610 11.913  10.432 1.00 43.57 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.006 12.366  10.457 1.00 45.47 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.928 11.266  9.912  1.00 47.44 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.547 10.097  9.881  1.00 46.52 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.419 12.783  11.865 1.00 45.43 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.322 11.697  12.772 1.00 46.44 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.148 11.640  9.458  1.00 49.22 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.115 10.682  8.919  1.00 51.18 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.849 9.921   10.034 1.00 52.83 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.995 10.439  11.138 1.00 53.57 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.140 11.401  8.043  1.00 53.66 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.747 12.466  8.755  1.00 57.15 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.286 8.685   9.759  1.00 53.72 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.004 7.861   10.749 1.00 55.54 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.324 7.339   10.181 1.00 58.71 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.434 7.177   8.963  1.00 59.60 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.152 6.652   11.219 1.00 55.78 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.096 5.658   10.201 1.00 55.78 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.752 7.040   11.656 1.00 55.61 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.285 6.972   11.054 1.00 60.06 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.549 6.422   10.571 1.00 61.65 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.415 4.946   10.261 1.00 61.01 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.904 4.490   9.229  1.00 62.07 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.731 6.750   11.519 1.00 64.92 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.570 6.047   12.754 1.00 67.63 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.850 8.216   11.790 1.00 65.70 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.757 4.188   11.144 1.00 59.53 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.578 2.759   10.940 1.00 58.19 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.259 2.434   10.243 1.00 56.54 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.285 3.180   10.379 1.00 56.35 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.667 2.022   12.270 1.00 58.32 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.221 1.317   9.506  1.00 54.47 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.997 0.909   8.812  1.00 53.03 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.952 0.279   9.734  1.00 49.47 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.290 -0.470  10.641 1.00 48.84 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.315 -0.063  7.676  1.00 55.81 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.447 0.613   6.329  1.00 61.86 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.146 -0.370  5.237  1.00 68.16 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.019 -0.726  4.438  1.00 69.92 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.904 -0.852  5.198  1.00 69.15 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.689 0.617   9.486  1.00 46.91 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.543 0.101   10.218 1.00 45.08 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.947 -1.113  9.549  1.00 42.59 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.256 -1.406  8.395  1.00 43.39 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.102 -1.851  10.276 1.00 39.97 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.552 -3.115  9.805  1.00 39.03 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.032 -3.165  9.657  1.00 37.37 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.496 -4.244  9.387  1.00 37.73 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.031 -4.225  10.732 1.00 40.81 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.831 -4.338  10.843 1.00 46.90 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.335 -2.052  9.919  1.00 35.84 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.874 -2.051  9.840  1.00 35.56 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.476 -1.973  8.345  1.00 36.23 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.195 -1.376  7.527  1.00 36.84 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.279 -0.849  10.652 1.00 35.40 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.461 -0.996  12.167 1.00 38.74 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.451 -2.149  12.658 1.00 39.66 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.619 0.045   12.862 1.00 38.93 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.386 -2.643  7.984  1.00 35.47 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.841 -2.579  6.621  1.00 36.41 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.543 -1.726  6.683  1.00 35.43 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.723 -2.014  7.523  1.00 35.51 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.513 -4.013  6.148  1.00 39.51 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.743 -4.612  5.739  1.00 41.46 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.539 -4.054  4.954  1.00 40.43 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.375 -0.705  5.826  1.00 34.78 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.141 0.073   5.793  1.00 33.97 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.097 -0.700  4.947  1.00 34.16 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.418 -1.190  3.841  1.00 34.45 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.332 1.520   5.262  1.00 34.97 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.451 2.298   6.022  1.00 35.07 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 17.995 2.293   5.333  1.00 35.29 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.305 2.303   7.555  1.00 34.95 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.866 -0.816  5.464  1.00 32.88 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.772 -1.459  4.752  1.00 32.05 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.369 -0.598  3.563  1.00 31.66 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.321 0.627   3.689  1.00 31.53 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.578 -1.580  5.678  1.00 30.87 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.042 -1.225  2.433  1.00 32.02 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.551 -0.523  1.245  1.00 33.75 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.248 -1.229  0.902  1.00 34.41 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.245 -2.191  0.148  1.00 35.14 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.551 -0.612  0.086  1.00 35.08 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.933 0.000   0.362  1.00 38.78 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.904 1.448   0.853  1.00 41.86 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.256 1.912   1.191  1.00 44.70 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.524 3.046   1.828  1.00 45.56 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.543 3.866   2.183  1.00 44.66 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.776 3.378   2.101  1.00 46.11 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.164 -0.797  1.539  1.00 34.68 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.884 -1.501  1.516  1.00 33.93 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.741  -0.561  1.946  1.00 33.90 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.984  0.591   2.311  1.00 32.92 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.004 -2.660  2.503  1.00 33.50 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.133 -2.090  4.226  1.00 33.41 ? 56  CYS   A SG  1 
ATOM   392  N  N   A ASP   A 1 51  ? 8.485  -1.066  1.985  0.50 33.85 ? 57  ASP   A N   1 
ATOM   393  N  N   B ASP   A 1 51  ? 8.511  -1.129  1.968  0.50 34.73 ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.364  -0.275  2.503  0.50 33.82 ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.251  -0.507  2.349  0.50 35.63 ? 57  ASP   A CA  1 
ATOM   396  C  C   A ASP   A 1 51  ? 6.712  -0.964  3.718  0.50 34.24 ? 57  ASP   A C   1 
ATOM   397  C  C   B ASP   A 1 51  ? 6.623  -1.260  3.553  0.50 35.18 ? 57  ASP   A C   1 
ATOM   398  O  O   A ASP   A 1 51  ? 5.558  -0.648  4.034  0.50 34.48 ? 57  ASP   A O   1 
ATOM   399  O  O   B ASP   A 1 51  ? 5.395  -1.292  3.665  0.50 35.47 ? 57  ASP   A O   1 
ATOM   400  C  CB  A ASP   A 1 51  ? 6.303  0.027   1.418  0.50 35.10 ? 57  ASP   A CB  1 
ATOM   401  C  CB  B ASP   A 1 51  ? 6.290  -0.628  1.155  0.50 38.76 ? 57  ASP   A CB  1 
ATOM   402  C  CG  A ASP   A 1 51  ? 5.585  -1.177  0.824  0.50 38.50 ? 57  ASP   A CG  1 
ATOM   403  C  CG  B ASP   A 1 51  ? 5.360  0.543   0.988  0.50 46.40 ? 57  ASP   A CG  1 
ATOM   404  O  OD1 A ASP   A 1 51  ? 6.073  -2.308  1.002  0.50 38.67 ? 57  ASP   A OD1 1 
ATOM   405  O  OD1 B ASP   A 1 51  ? 5.805  1.685   1.209  0.50 47.92 ? 57  ASP   A OD1 1 
ATOM   406  O  OD2 A ASP   A 1 51  ? 4.540  -0.979  0.159  0.50 40.90 ? 57  ASP   A OD2 1 
ATOM   407  O  OD2 B ASP   A 1 51  ? 4.201  0.323   0.565  0.50 50.08 ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 7.445  -1.894  4.414  1.00 34.11 ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 6.954  -2.642  5.603  1.00 33.42 ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.285  -1.693  6.584  1.00 32.52 ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 6.736  -0.557  6.750  1.00 32.13 ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.081  -3.385  6.325  1.00 33.62 ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 8.725  -4.847  5.475  1.00 34.62 ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.205  -2.145  7.199  1.00 31.05 ? 59  GLN   A N   1 
ATOM   415  C  CA  . GLN   A 1 53  ? 4.549  -1.380  8.247  1.00 31.13 ? 59  GLN   A CA  1 
ATOM   416  C  C   . GLN   A 1 53  ? 4.475  -2.226  9.543  1.00 30.62 ? 59  GLN   A C   1 
ATOM   417  O  O   . GLN   A 1 53  ? 3.632  -1.933  10.387 1.00 30.01 ? 59  GLN   A O   1 
ATOM   418  C  CB  . GLN   A 1 53  ? 3.123  -0.967  7.823  1.00 34.21 ? 59  GLN   A CB  1 
ATOM   419  C  CG  . GLN   A 1 53  ? 3.039  0.239   6.915  1.00 38.56 ? 59  GLN   A CG  1 
ATOM   420  C  CD  . GLN   A 1 53  ? 1.573  0.612   6.721  1.00 42.49 ? 59  GLN   A CD  1 
ATOM   421  O  OE1 . GLN   A 1 53  ? 0.981  0.399   5.642  1.00 42.92 ? 59  GLN   A OE1 1 
ATOM   422  N  NE2 . GLN   A 1 53  ? 0.957  1.175   7.772  1.00 41.52 ? 59  GLN   A NE2 1 
ATOM   423  N  N   . THR   A 1 54  ? 5.274  -3.339  9.655  1.00 29.00 ? 60  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 54  ? 5.379  -4.149  10.875 1.00 28.54 ? 60  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 54  ? 6.874  -4.395  11.096 1.00 27.41 ? 60  THR   A C   1 
ATOM   426  O  O   . THR   A 1 54  ? 7.659  -4.476  10.147 1.00 26.99 ? 60  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 54  ? 4.573  -5.476  10.845 1.00 30.62 ? 60  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 54  ? 5.165  -6.328  9.878  1.00 32.92 ? 60  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 54  ? 3.091  -5.275  10.487 1.00 31.46 ? 60  THR   A CG2 1 
ATOM   430  N  N   . GLY   A 1 55  ? 7.288  -4.386  12.352 1.00 26.39 ? 61  GLY   A N   1 
ATOM   431  C  CA  . GLY   A 1 55  ? 8.709  -4.525  12.682 1.00 25.19 ? 61  GLY   A CA  1 
ATOM   432  C  C   . GLY   A 1 55  ? 8.861  -4.676  14.192 1.00 26.27 ? 61  GLY   A C   1 
ATOM   433  O  O   . GLY   A 1 55  ? 7.893  -4.963  14.882 1.00 27.78 ? 61  GLY   A O   1 
ATOM   434  N  N   . VAL   A 1 56  ? 10.072 -4.545  14.684 1.00 25.13 ? 62  VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 56  ? 10.354 -4.681  16.128 1.00 25.21 ? 62  VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 56  ? 11.228 -3.512  16.512 1.00 25.67 ? 62  VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 56  ? 12.172 -3.200  15.798 1.00 25.54 ? 62  VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 56  ? 11.077 -6.034  16.404 1.00 27.05 ? 62  VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 56  ? 11.514 -6.123  17.868 1.00 27.48 ? 62  VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 56  ? 10.186 -7.218  16.055 1.00 27.36 ? 62  VAL   A CG2 1 
ATOM   441  N  N   . TYR   A 1 57  ? 10.955 -2.864  17.644 1.00 26.02 ? 63  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 57  ? 11.817 -1.756  18.096 1.00 25.21 ? 63  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 57  ? 12.377 -2.019  19.496 1.00 25.98 ? 63  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 57  ? 11.751 -2.704  20.286 1.00 27.76 ? 63  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 57  ? 11.118 -0.368  18.027 1.00 25.62 ? 63  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 57  ? 10.204 -0.060  19.194 1.00 27.76 ? 63  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 57  ? 8.936  -0.628  19.282 1.00 29.23 ? 63  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 57  ? 10.621 0.761   20.233 1.00 28.47 ? 63  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 57  ? 8.069  -0.302  20.323 1.00 30.09 ? 63  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 57  ? 9.762  1.090   21.284 1.00 30.25 ? 63  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 57  ? 8.503  0.516   21.350 1.00 31.02 ? 63  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 57  ? 7.638  0.834   22.373 1.00 33.27 ? 63  TYR   A OH  1 
ATOM   453  N  N   . TYR   A 1 58  ? 13.521 -1.406  19.803 1.00 25.97 ? 64  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 58  ? 14.116 -1.536  21.122 1.00 26.68 ? 64  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 58  ? 13.656 -0.372  21.992 1.00 28.17 ? 64  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 58  ? 13.861 0.788   21.630 1.00 27.60 ? 64  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 58  ? 15.645 -1.582  21.048 1.00 26.90 ? 64  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 58  ? 16.228 -1.728  22.434 1.00 28.62 ? 64  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 58  ? 15.925 -2.832  23.223 1.00 30.55 ? 64  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 58  ? 16.995 -0.717  22.997 1.00 30.43 ? 64  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 58  ? 16.420 -2.951  24.524 1.00 31.86 ? 64  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 58  ? 17.520 -0.837  24.285 1.00 32.29 ? 64  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 58  ? 17.218 -1.947  25.049 1.00 34.08 ? 64  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 58  ? 17.709 -2.049  26.331 1.00 36.98 ? 64  TYR   A OH  1 
ATOM   465  N  N   . CYS   A 1 59  ? 13.146 -0.694  23.202 1.00 28.94 ? 65  CYS   A N   1 
ATOM   466  C  CA  . CYS   A 1 59  ? 12.679 0.291   24.179 1.00 30.49 ? 65  CYS   A CA  1 
ATOM   467  C  C   . CYS   A 1 59  ? 13.592 0.243   25.397 1.00 32.26 ? 65  CYS   A C   1 
ATOM   468  O  O   . CYS   A 1 59  ? 13.429 -0.640  26.245 1.00 33.82 ? 65  CYS   A O   1 
ATOM   469  C  CB  . CYS   A 1 59  ? 11.227 0.011   24.570 1.00 33.00 ? 65  CYS   A CB  1 
ATOM   470  S  SG  . CYS   A 1 59  ? 10.591 1.061   25.930 1.00 35.51 ? 65  CYS   A SG  1 
ATOM   471  N  N   . SER   A 1 60  ? 14.548 1.173   25.501 1.00 32.11 ? 66  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 60  ? 15.503 1.164   26.604 1.00 34.32 ? 66  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 60  ? 14.858 1.325   27.980 1.00 35.17 ? 66  SER   A C   1 
ATOM   474  O  O   . SER   A 1 60  ? 15.349 0.716   28.940 1.00 36.42 ? 66  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 60  ? 16.587 2.217   26.400 1.00 38.07 ? 66  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 60  ? 16.091 3.528   26.608 1.00 43.19 ? 66  SER   A OG  1 
ATOM   477  N  N   . SER   A 1 61  ? 13.737 2.101   28.088 1.00 34.58 ? 67  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 61  ? 13.028 2.321   29.376 1.00 35.08 ? 67  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 61  ? 12.343 1.067   29.958 1.00 37.21 ? 67  SER   A C   1 
ATOM   480  O  O   . SER   A 1 61  ? 11.921 1.080   31.132 1.00 39.53 ? 67  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 61  ? 12.022 3.474   29.274 1.00 35.07 ? 67  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 61  ? 10.976 3.215   28.353 1.00 35.75 ? 67  SER   A OG  1 
ATOM   483  N  N   . ARG   A 1 62  ? 12.262 -0.002  29.154 1.00 37.03 ? 68  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 62  ? 11.720 -1.298  29.570 1.00 37.26 ? 68  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 62  ? 12.723 -2.441  29.341 1.00 37.26 ? 68  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 62  ? 12.401 -3.593  29.667 1.00 37.85 ? 68  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 62  ? 10.446 -1.605  28.776 1.00 38.73 ? 68  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 62  ? 9.283  -0.677  29.083 1.00 40.49 ? 68  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 62  ? 8.619  -1.047  30.404 1.00 41.93 ? 68  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 62  ? 7.457  -0.197  30.670 1.00 45.27 ? 68  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 62  ? 7.520  0.988   31.267 1.00 48.05 ? 68  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 62  ? 8.689  1.475   31.671 1.00 48.75 ? 68  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 62  ? 6.414  1.691   31.479 1.00 46.71 ? 68  ARG   A NH2 1 
ATOM   494  N  N   . ARG   A 1 63  ? 13.904 -2.167  28.731 1.00 36.45 ? 69  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 63  ? 14.900 -3.204  28.376 1.00 37.20 ? 69  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 63  ? 14.221 -4.331  27.563 1.00 36.91 ? 69  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 63  ? 14.382 -5.511  27.878 1.00 38.17 ? 69  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 63  ? 15.580 -3.788  29.631 1.00 39.06 ? 69  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 63  ? 16.591 -2.861  30.261 1.00 43.90 ? 69  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 63  ? 17.248 -3.518  31.454 1.00 47.42 ? 69  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 63  ? 17.990 -2.531  32.227 1.00 51.48 ? 69  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 63  ? 17.924 -2.402  33.550 1.00 53.79 ? 69  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 63  ? 17.121 -3.184  34.262 1.00 53.84 ? 69  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 63  ? 18.617 -1.451  34.165 1.00 54.52 ? 69  ARG   A NH2 1 
ATOM   505  N  N   . LYS   A 1 64  ? 13.385 -3.957  26.588 1.00 35.70 ? 70  LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 64  ? 12.611 -4.933  25.834 1.00 35.28 ? 70  LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 64  ? 12.466 -4.527  24.392 1.00 32.87 ? 70  LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 64  ? 12.378 -3.339  24.098 1.00 32.61 ? 70  LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 64  ? 11.190 -5.060  26.416 1.00 39.46 ? 70  LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 64  ? 11.055 -6.159  27.451 1.00 48.24 ? 70  LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 64  ? 9.614  -6.633  27.586 1.00 56.27 ? 70  LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 64  ? 9.401  -7.319  28.919 1.00 63.70 ? 70  LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 64  ? 9.696  -6.415  30.078 1.00 67.41 ? 70  LYS   A NZ  1 
ATOM   514  N  N   . HIS   A 1 65  ? 12.389 -5.519  23.519 1.00 31.25 ? 71  HIS   A N   1 
ATOM   515  C  CA  . HIS   A 1 65  ? 12.155 -5.343  22.083 1.00 30.34 ? 71  HIS   A CA  1 
ATOM   516  C  C   . HIS   A 1 65  ? 10.658 -5.640  21.898 1.00 32.28 ? 71  HIS   A C   1 
ATOM   517  O  O   . HIS   A 1 65  ? 10.158 -6.664  22.431 1.00 33.93 ? 71  HIS   A O   1 
ATOM   518  C  CB  . HIS   A 1 65  ? 13.032 -6.311  21.262 1.00 29.58 ? 71  HIS   A CB  1 
ATOM   519  C  CG  . HIS   A 1 65  ? 14.505 -6.073  21.429 1.00 29.67 ? 71  HIS   A CG  1 
ATOM   520  N  ND1 . HIS   A 1 65  ? 15.238 -5.379  20.483 1.00 31.45 ? 71  HIS   A ND1 1 
ATOM   521  C  CD2 . HIS   A 1 65  ? 15.320 -6.391  22.465 1.00 30.28 ? 71  HIS   A CD2 1 
ATOM   522  C  CE1 . HIS   A 1 65  ? 16.475 -5.331  20.942 1.00 31.55 ? 71  HIS   A CE1 1 
ATOM   523  N  NE2 . HIS   A 1 65  ? 16.564 -5.887  22.156 1.00 31.94 ? 71  HIS   A NE2 1 
ATOM   524  N  N   . TYR   A 1 66  ? 9.915  -4.718  21.256 1.00 29.82 ? 72  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 66  ? 8.478  -4.920  21.102 1.00 29.55 ? 72  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 66  ? 8.123  -5.036  19.625 1.00 29.52 ? 72  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 66  ? 8.502  -4.164  18.846 1.00 28.54 ? 72  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 66  ? 7.700  -3.707  21.631 1.00 29.70 ? 72  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 66  ? 7.711  -3.576  23.141 1.00 31.45 ? 72  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 66  ? 6.942  -4.414  23.940 1.00 33.73 ? 72  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 66  ? 8.465  -2.599  23.761 1.00 32.19 ? 72  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 66  ? 6.943  -4.290  25.331 1.00 35.29 ? 72  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 66  ? 8.468  -2.455  25.145 1.00 32.99 ? 72  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 66  ? 7.698  -3.294  25.928 1.00 35.83 ? 72  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 66  ? 7.730  -3.175  27.305 1.00 38.27 ? 72  TYR   A OH  1 
ATOM   536  N  N   . PRO   A 1 67  ? 7.305  -6.020  19.270 1.00 29.96 ? 73  PRO   A N   1 
ATOM   537  C  CA  . PRO   A 1 67  ? 6.820  -6.087  17.872 1.00 30.65 ? 73  PRO   A CA  1 
ATOM   538  C  C   . PRO   A 1 67  ? 5.714  -5.004  17.715 1.00 31.49 ? 73  PRO   A C   1 
ATOM   539  O  O   . PRO   A 1 67  ? 4.863  -4.851  18.606 1.00 32.26 ? 73  PRO   A O   1 
ATOM   540  C  CB  . PRO   A 1 67  ? 6.249  -7.522  17.770 1.00 32.22 ? 73  PRO   A CB  1 
ATOM   541  C  CG  . PRO   A 1 67  ? 5.818  -7.853  19.189 1.00 33.55 ? 73  PRO   A CG  1 
ATOM   542  C  CD  . PRO   A 1 67  ? 6.806  -7.145  20.101 1.00 30.94 ? 73  PRO   A CD  1 
ATOM   543  N  N   . VAL   A 1 68  ? 5.722  -4.249  16.611 1.00 29.86 ? 74  VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 68  ? 4.734  -3.193  16.397 1.00 29.99 ? 74  VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 68  ? 4.287  -3.105  14.930 1.00 30.00 ? 74  VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 68  ? 5.033  -3.485  14.015 1.00 30.19 ? 74  VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 68  ? 5.295  -1.791  16.816 1.00 31.06 ? 74  VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 68  ? 5.290  -1.591  18.324 1.00 31.92 ? 74  VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 68  ? 6.664  -1.513  16.195 1.00 30.38 ? 74  VAL   A CG2 1 
ATOM   550  N  N   . SER   A 1 69  ? 3.078  -2.523  14.738 1.00 29.70 ? 75  SER   A N   1 
ATOM   551  C  CA  . SER   A 1 69  ? 2.533  -2.085  13.447 1.00 30.41 ? 75  SER   A CA  1 
ATOM   552  C  C   . SER   A 1 69  ? 2.754  -0.565  13.471 1.00 30.14 ? 75  SER   A C   1 
ATOM   553  O  O   . SER   A 1 69  ? 2.512  0.064   14.509 1.00 30.93 ? 75  SER   A O   1 
ATOM   554  C  CB  . SER   A 1 69  ? 1.036  -2.344  13.366 1.00 33.86 ? 75  SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 69  ? 0.818  -3.741  13.366 1.00 40.28 ? 75  SER   A OG  1 
ATOM   556  N  N   . PHE   A 1 70  ? 3.191  0.035   12.367 1.00 29.00 ? 76  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 70  ? 3.446  1.476   12.348 1.00 28.19 ? 76  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 70  ? 2.927  2.131   11.078 1.00 29.63 ? 76  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 70  ? 2.823  1.475   10.041 1.00 30.10 ? 76  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 70  ? 4.957  1.779   12.607 1.00 27.34 ? 76  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 70  ? 5.923  1.059   11.695 1.00 27.71 ? 76  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 70  ? 6.399  -0.208  12.019 1.00 28.18 ? 76  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 70  ? 6.338  1.638   10.499 1.00 28.29 ? 76  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 70  ? 7.330  -0.847  11.199 1.00 28.23 ? 76  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 70  ? 7.256  0.992   9.672  1.00 28.40 ? 76  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 70  ? 7.723  -0.258  10.004 1.00 27.30 ? 76  PHE   A CZ  1 
ATOM   567  N  N   . SER   A 1 71  ? 2.569  3.430   11.168 1.00 29.55 ? 77  SER   A N   1 
ATOM   568  C  CA  . SER   A 1 71  ? 2.023  4.158   10.048 1.00 30.31 ? 77  SER   A CA  1 
ATOM   569  C  C   . SER   A 1 71  ? 3.074  4.497   9.003  1.00 30.75 ? 77  SER   A C   1 
ATOM   570  O  O   . SER   A 1 71  ? 4.267  4.371   9.267  1.00 31.26 ? 77  SER   A O   1 
ATOM   571  C  CB  . SER   A 1 71  ? 1.317  5.425   10.551 1.00 31.37 ? 77  SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 71  ? 2.253  6.230   11.243 1.00 34.03 ? 77  SER   A OG  1 
ATOM   573  N  N   . LYS   A 1 72  ? 2.636  4.881   7.784  1.00 31.01 ? 78  LYS   A N   1 
ATOM   574  C  CA  . LYS   A 1 72  ? 3.600  5.269   6.764  1.00 32.26 ? 78  LYS   A CA  1 
ATOM   575  C  C   . LYS   A 1 72  ? 4.239  6.636   7.104  1.00 32.22 ? 78  LYS   A C   1 
ATOM   576  O  O   . LYS   A 1 72  ? 3.631  7.425   7.830  1.00 33.11 ? 78  LYS   A O   1 
ATOM   577  C  CB  . LYS   A 1 72  ? 2.961  5.227   5.340  1.00 35.43 ? 78  LYS   A CB  1 
ATOM   578  C  CG  . LYS   A 1 72  ? 2.907  3.770   4.804  1.00 40.65 ? 78  LYS   A CG  1 
ATOM   579  C  CD  . LYS   A 1 72  ? 2.439  3.631   3.340  1.00 48.02 ? 78  LYS   A CD  1 
ATOM   580  C  CE  . LYS   A 1 72  ? 2.545  2.183   2.905  1.00 53.47 ? 78  LYS   A CE  1 
ATOM   581  N  NZ  . LYS   A 1 72  ? 1.974  1.937   1.548  1.00 56.99 ? 78  LYS   A NZ  1 
ATOM   582  N  N   . PRO   A 1 73  ? 5.481  6.917   6.666  1.00 32.32 ? 79  PRO   A N   1 
ATOM   583  C  CA  . PRO   A 1 73  ? 6.099  8.234   6.990  1.00 32.38 ? 79  PRO   A CA  1 
ATOM   584  C  C   . PRO   A 1 73  ? 5.224  9.436   6.588  1.00 32.05 ? 79  PRO   A C   1 
ATOM   585  O  O   . PRO   A 1 73  ? 4.739  9.507   5.444  1.00 32.22 ? 79  PRO   A O   1 
ATOM   586  C  CB  . PRO   A 1 73  ? 7.418  8.221   6.203  1.00 34.09 ? 79  PRO   A CB  1 
ATOM   587  C  CG  . PRO   A 1 73  ? 7.730  6.749   5.985  1.00 35.69 ? 79  PRO   A CG  1 
ATOM   588  C  CD  . PRO   A 1 73  ? 6.364  6.095   5.807  1.00 32.87 ? 79  PRO   A CD  1 
ATOM   589  N  N   A SER   A 1 74  ? 5.026  10.379  7.511  0.50 31.49 ? 80  SER   A N   1 
ATOM   590  N  N   B SER   A 1 74  ? 4.994  10.359  7.525  0.50 31.88 ? 80  SER   A N   1 
ATOM   591  C  CA  A SER   A 1 74  ? 4.148  11.518  7.242  0.50 32.07 ? 80  SER   A CA  1 
ATOM   592  C  CA  B SER   A 1 74  ? 4.095  11.489  7.278  0.50 32.80 ? 80  SER   A CA  1 
ATOM   593  C  C   A SER   A 1 74  ? 4.505  12.764  8.082  0.50 32.83 ? 80  SER   A C   1 
ATOM   594  C  C   B SER   A 1 74  ? 4.502  12.755  8.077  0.50 33.15 ? 80  SER   A C   1 
ATOM   595  O  O   A SER   A 1 74  ? 5.406  12.714  8.927  0.50 32.63 ? 80  SER   A O   1 
ATOM   596  O  O   B SER   A 1 74  ? 5.419  12.704  8.905  0.50 32.94 ? 80  SER   A O   1 
ATOM   597  C  CB  A SER   A 1 74  ? 2.684  11.103  7.438  0.50 33.18 ? 80  SER   A CB  1 
ATOM   598  C  CB  B SER   A 1 74  ? 2.657  11.086  7.640  0.50 34.93 ? 80  SER   A CB  1 
ATOM   599  O  OG  A SER   A 1 74  ? 2.435  10.681  8.769  0.50 33.56 ? 80  SER   A OG  1 
ATOM   600  O  OG  B SER   A 1 74  ? 2.229  9.880   7.028  0.50 37.09 ? 80  SER   A OG  1 
ATOM   601  N  N   . LEU   A 1 75  ? 3.800  13.883  7.838  1.00 33.17 ? 81  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 75  ? 4.007  15.151  8.536  1.00 34.18 ? 81  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 75  ? 3.039  15.087  9.717  1.00 35.04 ? 81  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 75  ? 1.813  15.030  9.508  1.00 34.87 ? 81  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 75  ? 3.619  16.312  7.554  1.00 34.99 ? 81  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 75  ? 4.211  17.711  7.779  1.00 38.20 ? 81  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 75  ? 5.683  17.687  7.770  1.00 37.97 ? 81  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 75  ? 3.726  18.727  6.685  1.00 39.57 ? 81  LEU   A CD2 1 
ATOM   609  N  N   . ILE   A 1 76  ? 3.579  15.028  10.945 1.00 35.12 ? 82  ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 76  ? 2.814  14.851  12.181 1.00 36.04 ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 3.151  15.984  13.144 1.00 36.63 ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.330  16.342  13.286 1.00 36.00 ? 82  ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 76  ? 3.186  13.486  12.816 1.00 37.23 ? 82  ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 76  ? 2.748  12.295  11.939 1.00 39.18 ? 82  ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 76  ? 2.683  13.347  14.271 1.00 37.81 ? 82  ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 76  ? 1.288  12.050  11.902 1.00 41.72 ? 82  ILE   A CD1 1 
ATOM   617  N  N   . PHE   A 1 77  ? 2.121  16.579  13.770 1.00 36.80 ? 83  PHE   A N   1 
ATOM   618  C  CA  . PHE   A 1 77  ? 2.352  17.662  14.702 1.00 37.74 ? 83  PHE   A CA  1 
ATOM   619  C  C   . PHE   A 1 77  ? 2.981  17.100  15.977 1.00 37.25 ? 83  PHE   A C   1 
ATOM   620  O  O   . PHE   A 1 77  ? 2.500  16.109  16.538 1.00 38.36 ? 83  PHE   A O   1 
ATOM   621  C  CB  . PHE   A 1 77  ? 1.062  18.450  15.004 1.00 38.70 ? 83  PHE   A CB  1 
ATOM   622  C  CG  . PHE   A 1 77  ? 1.349  19.789  15.640 1.00 40.66 ? 83  PHE   A CG  1 
ATOM   623  C  CD1 . PHE   A 1 77  ? 1.917  20.814  14.905 1.00 42.25 ? 83  PHE   A CD1 1 
ATOM   624  C  CD2 . PHE   A 1 77  ? 1.075  20.012  16.976 1.00 41.88 ? 83  PHE   A CD2 1 
ATOM   625  C  CE1 . PHE   A 1 77  ? 2.225  22.026  15.499 1.00 43.66 ? 83  PHE   A CE1 1 
ATOM   626  C  CE2 . PHE   A 1 77  ? 1.345  21.239  17.560 1.00 42.80 ? 83  PHE   A CE2 1 
ATOM   627  C  CZ  . PHE   A 1 77  ? 1.911  22.238  16.819 1.00 43.43 ? 83  PHE   A CZ  1 
ATOM   628  N  N   . VAL   A 1 78  ? 4.102  17.694  16.402 1.00 35.15 ? 84  VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 78  ? 4.786  17.259  17.613 1.00 34.83 ? 84  VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 78  ? 4.831  18.419  18.590 1.00 36.52 ? 84  VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 78  ? 5.310  19.507  18.251 1.00 35.79 ? 84  VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 78  ? 6.210  16.725  17.298 1.00 34.53 ? 84  VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 78  ? 6.940  16.327  18.586 1.00 35.52 ? 84  VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 78  ? 6.159  15.550  16.327 1.00 33.82 ? 84  VAL   A CG2 1 
ATOM   635  N  N   . GLU   A 1 79  ? 4.330  18.191  19.803 1.00 38.10 ? 85  GLU   A N   1 
ATOM   636  C  CA  . GLU   A 1 79  ? 4.266  19.209  20.845 1.00 40.44 ? 85  GLU   A CA  1 
ATOM   637  C  C   . GLU   A 1 79  ? 5.618  19.836  21.137 1.00 40.42 ? 85  GLU   A C   1 
ATOM   638  O  O   . GLU   A 1 79  ? 6.646  19.221  20.881 1.00 39.09 ? 85  GLU   A O   1 
ATOM   639  C  CB  . GLU   A 1 79  ? 3.669  18.610  22.141 1.00 45.29 ? 85  GLU   A CB  1 
ATOM   640  C  CG  . GLU   A 1 79  ? 2.197  18.256  22.004 1.00 54.57 ? 85  GLU   A CG  1 
ATOM   641  C  CD  . GLU   A 1 79  ? 1.343  19.441  21.587 1.00 66.20 ? 85  GLU   A CD  1 
ATOM   642  O  OE1 . GLU   A 1 79  ? 1.154  20.352  22.426 1.00 67.89 ? 85  GLU   A OE1 1 
ATOM   643  O  OE2 . GLU   A 1 79  ? 0.900  19.482  20.414 1.00 70.20 ? 85  GLU   A OE2 1 
ATOM   644  N  N   . ALA   A 1 80  ? 5.615  21.060  21.682 1.00 41.71 ? 86  ALA   A N   1 
ATOM   645  C  CA  . ALA   A 1 80  ? 6.854  21.733  22.052 1.00 44.02 ? 86  ALA   A CA  1 
ATOM   646  C  C   . ALA   A 1 80  ? 7.533  20.946  23.169 1.00 45.73 ? 86  ALA   A C   1 
ATOM   647  O  O   . ALA   A 1 80  ? 6.853  20.376  24.024 1.00 46.78 ? 86  ALA   A O   1 
ATOM   648  C  CB  . ALA   A 1 80  ? 6.568  23.153  22.523 1.00 44.22 ? 86  ALA   A CB  1 
ATOM   649  N  N   . SER   A 1 81  ? 8.858  20.854  23.111 1.00 45.47 ? 87  SER   A N   1 
ATOM   650  C  CA  . SER   A 1 81  ? 9.691  20.182  24.112 1.00 46.09 ? 87  SER   A CA  1 
ATOM   651  C  C   . SER   A 1 81  ? 10.910 21.093  24.427 1.00 47.05 ? 87  SER   A C   1 
ATOM   652  O  O   . SER   A 1 81  ? 10.987 22.206  23.902 1.00 47.26 ? 87  SER   A O   1 
ATOM   653  C  CB  . SER   A 1 81  ? 10.188 18.851  23.553 1.00 46.44 ? 87  SER   A CB  1 
ATOM   654  O  OG  . SER   A 1 81  ? 11.099 19.103  22.494 1.00 47.55 ? 87  SER   A OG  1 
ATOM   655  N  N   . GLU   A 1 82  ? 11.881 20.616  25.243 1.00 47.81 ? 88  GLU   A N   1 
ATOM   656  C  CA  . GLU   A 1 82  ? 13.086 21.415  25.516 1.00 49.03 ? 88  GLU   A CA  1 
ATOM   657  C  C   . GLU   A 1 82  ? 14.016 21.491  24.274 1.00 48.25 ? 88  GLU   A C   1 
ATOM   658  O  O   . GLU   A 1 82  ? 14.866 22.377  24.221 1.00 48.09 ? 88  GLU   A O   1 
ATOM   659  C  CB  . GLU   A 1 82  ? 13.857 20.880  26.743 1.00 52.98 ? 88  GLU   A CB  1 
ATOM   660  C  CG  . GLU   A 1 82  ? 14.340 19.447  26.561 1.00 61.89 ? 88  GLU   A CG  1 
ATOM   661  C  CD  . GLU   A 1 82  ? 15.097 18.849  27.734 1.00 73.33 ? 88  GLU   A CD  1 
ATOM   662  O  OE1 . GLU   A 1 82  ? 16.344 18.979  27.779 1.00 74.60 ? 88  GLU   A OE1 1 
ATOM   663  O  OE2 . GLU   A 1 82  ? 14.439 18.237  28.607 1.00 77.71 ? 88  GLU   A OE2 1 
ATOM   664  N  N   . TYR   A 1 83  ? 13.830 20.590  23.266 1.00 47.28 ? 89  TYR   A N   1 
ATOM   665  C  CA  . TYR   A 1 83  ? 14.651 20.541  22.049 1.00 46.34 ? 89  TYR   A CA  1 
ATOM   666  C  C   . TYR   A 1 83  ? 14.073 21.275  20.835 1.00 44.69 ? 89  TYR   A C   1 
ATOM   667  O  O   . TYR   A 1 83  ? 14.839 21.777  20.021 1.00 45.39 ? 89  TYR   A O   1 
ATOM   668  C  CB  . TYR   A 1 83  ? 14.952 19.092  21.671 1.00 47.12 ? 89  TYR   A CB  1 
ATOM   669  C  CG  . TYR   A 1 83  ? 15.570 18.314  22.806 1.00 48.96 ? 89  TYR   A CG  1 
ATOM   670  C  CD1 . TYR   A 1 83  ? 16.872 18.566  23.222 1.00 50.16 ? 89  TYR   A CD1 1 
ATOM   671  C  CD2 . TYR   A 1 83  ? 14.831 17.378  23.512 1.00 50.47 ? 89  TYR   A CD2 1 
ATOM   672  C  CE1 . TYR   A 1 83  ? 17.441 17.856  24.272 1.00 51.36 ? 89  TYR   A CE1 1 
ATOM   673  C  CE2 . TYR   A 1 83  ? 15.391 16.657  24.554 1.00 51.60 ? 89  TYR   A CE2 1 
ATOM   674  C  CZ  . TYR   A 1 83  ? 16.694 16.903  24.938 1.00 52.64 ? 89  TYR   A CZ  1 
ATOM   675  O  OH  . TYR   A 1 83  ? 17.243 16.173  25.961 1.00 54.81 ? 89  TYR   A OH  1 
ATOM   676  N  N   . TYR   A 1 84  ? 12.748 21.320  20.687 1.00 42.19 ? 90  TYR   A N   1 
ATOM   677  C  CA  . TYR   A 1 84  ? 12.118 22.001  19.550 1.00 40.70 ? 90  TYR   A CA  1 
ATOM   678  C  C   . TYR   A 1 84  ? 10.866 22.719  19.997 1.00 42.01 ? 90  TYR   A C   1 
ATOM   679  O  O   . TYR   A 1 84  ? 10.109 22.166  20.796 1.00 43.05 ? 90  TYR   A O   1 
ATOM   680  C  CB  . TYR   A 1 84  ? 11.678 20.993  18.450 1.00 38.66 ? 90  TYR   A CB  1 
ATOM   681  C  CG  . TYR   A 1 84  ? 12.776 20.143  17.841 1.00 36.93 ? 90  TYR   A CG  1 
ATOM   682  C  CD1 . TYR   A 1 84  ? 13.675 20.680  16.922 1.00 36.52 ? 90  TYR   A CD1 1 
ATOM   683  C  CD2 . TYR   A 1 84  ? 12.922 18.807  18.188 1.00 36.43 ? 90  TYR   A CD2 1 
ATOM   684  C  CE1 . TYR   A 1 84  ? 14.674 19.899  16.351 1.00 35.51 ? 90  TYR   A CE1 1 
ATOM   685  C  CE2 . TYR   A 1 84  ? 13.924 18.018  17.632 1.00 35.72 ? 90  TYR   A CE2 1 
ATOM   686  C  CZ  . TYR   A 1 84  ? 14.790 18.564  16.704 1.00 35.44 ? 90  TYR   A CZ  1 
ATOM   687  O  OH  . TYR   A 1 84  ? 15.787 17.781  16.164 1.00 34.35 ? 90  TYR   A OH  1 
ATOM   688  N  N   . PRO   A 1 85  ? 10.523 23.860  19.371 1.00 42.02 ? 91  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? 9.182  24.437  19.602 1.00 41.42 ? 91  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? 8.111  23.520  18.947 1.00 40.52 ? 91  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? 8.464  22.558  18.234 1.00 40.55 ? 91  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? 9.259  25.785  18.875 1.00 42.77 ? 91  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? 10.219 25.553  17.755 1.00 43.46 ? 91  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? 11.263 24.597  18.320 1.00 41.97 ? 91  PRO   A CD  1 
ATOM   695  N  N   . ALA   A 1 86  ? 6.807  23.803  19.167 1.00 39.83 ? 92  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 86  ? 5.717  22.992  18.592 1.00 40.02 ? 92  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 86  ? 5.800  23.109  17.076 1.00 39.33 ? 92  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 86  ? 5.903  24.232  16.569 1.00 40.16 ? 92  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 86  ? 4.358  23.504  19.088 1.00 40.45 ? 92  ALA   A CB  1 
ATOM   700  N  N   . ARG   A 1 87  ? 5.886  21.977  16.359 1.00 37.25 ? 93  ARG   A N   1 
ATOM   701  C  CA  . ARG   A 1 87  ? 6.077  22.043  14.906 1.00 36.87 ? 93  ARG   A CA  1 
ATOM   702  C  C   . ARG   A 1 87  ? 5.606  20.752  14.214 1.00 37.45 ? 93  ARG   A C   1 
ATOM   703  O  O   . ARG   A 1 87  ? 5.356  19.768  14.911 1.00 37.74 ? 93  ARG   A O   1 
ATOM   704  C  CB  . ARG   A 1 87  ? 7.598  22.254  14.629 1.00 37.06 ? 93  ARG   A CB  1 
ATOM   705  C  CG  . ARG   A 1 87  ? 8.429  20.933  14.647 1.00 38.25 ? 93  ARG   A CG  1 
ATOM   706  C  CD  . ARG   A 1 87  ? 9.830  21.045  15.192 1.00 38.07 ? 93  ARG   A CD  1 
ATOM   707  N  NE  . ARG   A 1 87  ? 10.721 19.975  14.723 1.00 36.70 ? 93  ARG   A NE  1 
ATOM   708  C  CZ  . ARG   A 1 87  ? 10.754 18.736  15.222 1.00 37.27 ? 93  ARG   A CZ  1 
ATOM   709  N  NH1 . ARG   A 1 87  ? 9.899  18.372  16.183 1.00 34.73 ? 93  ARG   A NH1 1 
ATOM   710  N  NH2 . ARG   A 1 87  ? 11.651 17.854  14.775 1.00 32.82 ? 93  ARG   A NH2 1 
ATOM   711  N  N   . TYR   A 1 88  ? 5.571  20.722  12.850 1.00 36.58 ? 94  TYR   A N   1 
ATOM   712  C  CA  . TYR   A 1 88  ? 5.277  19.468  12.168 1.00 37.60 ? 94  TYR   A CA  1 
ATOM   713  C  C   . TYR   A 1 88  ? 6.607  18.797  11.894 1.00 35.02 ? 94  TYR   A C   1 
ATOM   714  O  O   . TYR   A 1 88  ? 7.535  19.429  11.377 1.00 34.90 ? 94  TYR   A O   1 
ATOM   715  C  CB  . TYR   A 1 88  ? 4.562  19.662  10.826 1.00 39.88 ? 94  TYR   A CB  1 
ATOM   716  C  CG  . TYR   A 1 88  ? 3.177  20.232  10.977 1.00 43.73 ? 94  TYR   A CG  1 
ATOM   717  C  CD1 . TYR   A 1 88  ? 2.084  19.404  11.171 1.00 45.57 ? 94  TYR   A CD1 1 
ATOM   718  C  CD2 . TYR   A 1 88  ? 2.965  21.601  10.954 1.00 46.57 ? 94  TYR   A CD2 1 
ATOM   719  C  CE1 . TYR   A 1 88  ? 0.803  19.924  11.317 1.00 47.90 ? 94  TYR   A CE1 1 
ATOM   720  C  CE2 . TYR   A 1 88  ? 1.686  22.135  11.074 1.00 48.34 ? 94  TYR   A CE2 1 
ATOM   721  C  CZ  . TYR   A 1 88  ? 0.607  21.290  11.262 1.00 49.81 ? 94  TYR   A CZ  1 
ATOM   722  O  OH  . TYR   A 1 88  ? -0.654 21.823  11.381 1.00 53.17 ? 94  TYR   A OH  1 
ATOM   723  N  N   . GLN   A 1 89  ? 6.711  17.536  12.261 1.00 32.85 ? 95  GLN   A N   1 
ATOM   724  C  CA  . GLN   A 1 89  ? 7.922  16.758  11.980 1.00 31.68 ? 95  GLN   A CA  1 
ATOM   725  C  C   . GLN   A 1 89  ? 7.589  15.914  10.754 1.00 31.26 ? 95  GLN   A C   1 
ATOM   726  O  O   . GLN   A 1 89  ? 6.551  15.244  10.750 1.00 32.08 ? 95  GLN   A O   1 
ATOM   727  C  CB  . GLN   A 1 89  ? 8.294  15.857  13.173 1.00 31.58 ? 95  GLN   A CB  1 
ATOM   728  C  CG  . GLN   A 1 89  ? 9.576  15.022  12.903 1.00 32.86 ? 95  GLN   A CG  1 
ATOM   729  C  CD  . GLN   A 1 89  ? 10.260 14.512  14.160 1.00 33.01 ? 95  GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A 1 89  ? 10.287 15.174  15.195 1.00 33.14 ? 95  GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A 1 89  ? 10.849 13.335  14.085 1.00 31.80 ? 95  GLN   A NE2 1 
ATOM   732  N  N   . SER   A 1 90  ? 8.428  15.955  9.721  1.00 30.75 ? 96  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 90  ? 8.197  15.160  8.517  1.00 31.17 ? 96  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 90  ? 8.858  13.756  8.615  1.00 30.22 ? 96  SER   A C   1 
ATOM   735  O  O   . SER   A 1 90  ? 9.717  13.534  9.479  1.00 29.96 ? 96  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 90  ? 8.707  15.905  7.280  1.00 32.59 ? 96  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 90  ? 10.110 16.087  7.387  1.00 34.42 ? 96  SER   A OG  1 
ATOM   738  N  N   . HIS   A 1 91  ? 8.418  12.815  7.743  1.00 29.36 ? 97  HIS   A N   1 
ATOM   739  C  CA  . HIS   A 1 91  ? 8.944  11.450  7.644  1.00 29.37 ? 97  HIS   A CA  1 
ATOM   740  C  C   . HIS   A 1 91  ? 8.832  10.668  9.000  1.00 29.48 ? 97  HIS   A C   1 
ATOM   741  O  O   . HIS   A 1 91  ? 9.675  9.811   9.286  1.00 29.71 ? 97  HIS   A O   1 
ATOM   742  C  CB  . HIS   A 1 91  ? 10.394 11.502  7.130  1.00 29.04 ? 97  HIS   A CB  1 
ATOM   743  C  CG  . HIS   A 1 91  ? 10.528 12.153  5.772  1.00 33.49 ? 97  HIS   A CG  1 
ATOM   744  N  ND1 . HIS   A 1 91  ? 10.611 11.398  4.621  1.00 36.69 ? 97  HIS   A ND1 1 
ATOM   745  C  CD2 . HIS   A 1 91  ? 10.620 13.465  5.438  1.00 34.91 ? 97  HIS   A CD2 1 
ATOM   746  C  CE1 . HIS   A 1 91  ? 10.742 12.265  3.621  1.00 36.93 ? 97  HIS   A CE1 1 
ATOM   747  N  NE2 . HIS   A 1 91  ? 10.733 13.522  4.057  1.00 36.01 ? 97  HIS   A NE2 1 
ATOM   748  N  N   . LEU   A 1 92  ? 7.793  10.977  9.784  1.00 28.86 ? 98  LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 7.566  10.351  11.088 1.00 29.02 ? 98  LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 6.510  9.232   10.970 1.00 28.48 ? 98  LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 5.457  9.418   10.334 1.00 28.37 ? 98  LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 7.088  11.414  12.104 1.00 29.04 ? 98  LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 6.998  10.977  13.588 1.00 29.65 ? 98  LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 8.384  10.682  14.134 1.00 30.40 ? 98  LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 6.322  12.094  14.449 1.00 30.24 ? 98  LEU   A CD2 1 
ATOM   756  N  N   . MET   A 1 93  ? 6.767  8.110   11.655 1.00 26.79 ? 99  MET   A N   1 
ATOM   757  C  CA  . MET   A 1 93  ? 5.858  6.972   11.666 1.00 26.87 ? 99  MET   A CA  1 
ATOM   758  C  C   . MET   A 1 93  ? 5.453  6.702   13.105 1.00 27.87 ? 99  MET   A C   1 
ATOM   759  O  O   . MET   A 1 93  ? 6.328  6.755   13.959 1.00 28.23 ? 99  MET   A O   1 
ATOM   760  C  CB  . MET   A 1 93  ? 6.623  5.750   11.118 1.00 27.28 ? 99  MET   A CB  1 
ATOM   761  C  CG  . MET   A 1 93  ? 7.123  5.969   9.668  1.00 30.16 ? 99  MET   A CG  1 
ATOM   762  S  SD  . MET   A 1 93  ? 8.186  4.613   9.103  1.00 31.17 ? 99  MET   A SD  1 
ATOM   763  C  CE  . MET   A 1 93  ? 9.539  4.802   10.155 1.00 32.07 ? 99  MET   A CE  1 
ATOM   764  N  N   . LEU   A 1 94  ? 4.144  6.486   13.404 1.00 27.28 ? 100 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 94  ? 3.724  6.215   14.784 1.00 27.35 ? 100 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 94  ? 3.295  4.749   14.930 1.00 27.86 ? 100 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 94  ? 2.814  4.119   13.979 1.00 28.26 ? 100 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 94  ? 2.471  7.079   15.191 1.00 27.87 ? 100 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 94  ? 2.614  8.593   15.120 1.00 30.40 ? 100 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 94  ? 1.365  9.283   15.708 1.00 31.89 ? 100 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 94  ? 3.859  9.069   15.864 1.00 31.57 ? 100 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 95  ? 3.409  4.268   16.149 1.00 27.28 ? 101 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 95  ? 2.958  2.940   16.609 1.00 28.82 ? 101 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 95  ? 2.419  3.104   18.034 1.00 30.18 ? 101 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 95  ? 2.749  4.066   18.740 1.00 30.96 ? 101 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 95  ? 4.147  1.969   16.643 1.00 28.53 ? 101 ALA   A CB  1 
ATOM   777  N  N   . VAL   A 1 96  ? 1.571  2.171   18.437 1.00 30.38 ? 102 VAL   A N   1 
ATOM   778  C  CA  . VAL   A 1 96  ? 1.090  2.135   19.804 1.00 31.69 ? 102 VAL   A CA  1 
ATOM   779  C  C   . VAL   A 1 96  ? 2.178  1.422   20.613 1.00 33.79 ? 102 VAL   A C   1 
ATOM   780  O  O   . VAL   A 1 96  ? 2.513  0.269   20.324 1.00 34.18 ? 102 VAL   A O   1 
ATOM   781  C  CB  . VAL   A 1 96  ? -0.270 1.424   19.915 1.00 33.02 ? 102 VAL   A CB  1 
ATOM   782  C  CG1 . VAL   A 1 96  ? -0.643 1.259   21.378 1.00 34.42 ? 102 VAL   A CG1 1 
ATOM   783  C  CG2 . VAL   A 1 96  ? -1.344 2.209   19.169 1.00 32.78 ? 102 VAL   A CG2 1 
ATOM   784  N  N   . GLY   A 1 97  ? 2.779  2.132   21.549 1.00 35.71 ? 103 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 97  ? 3.830  1.554   22.376 1.00 37.25 ? 103 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 97  ? 4.422  2.514   23.386 1.00 37.81 ? 103 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 97  ? 4.100  3.703   23.409 1.00 37.02 ? 103 GLY   A O   1 
ATOM   788  N  N   . HIS   A 1 98  ? 5.306  1.990   24.232 1.00 38.09 ? 104 HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 98  ? 5.942  2.787   25.261 1.00 37.87 ? 104 HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 98  ? 7.199  3.521   24.753 1.00 36.94 ? 104 HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 98  ? 8.091  2.916   24.155 1.00 37.22 ? 104 HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 98  ? 6.292  1.901   26.452 1.00 38.81 ? 104 HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 98  ? 6.727  2.707   27.623 1.00 42.38 ? 104 HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 98  ? 5.868  3.600   28.236 1.00 44.73 ? 104 HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 98  ? 7.944  2.803   28.195 1.00 43.67 ? 104 HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 98  ? 6.588  4.206   29.166 1.00 45.46 ? 104 HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 98  ? 7.844  3.748   29.181 1.00 45.02 ? 104 HIS   A NE2 1 
ATOM   798  N  N   . SER   A 1 99  ? 7.290  4.819   25.037 1.00 36.14 ? 105 SER   A N   1 
ATOM   799  C  CA  . SER   A 1 99  ? 8.430  5.624   24.629 1.00 37.42 ? 105 SER   A CA  1 
ATOM   800  C  C   . SER   A 1 99  ? 8.593  6.793   25.587 1.00 39.78 ? 105 SER   A C   1 
ATOM   801  O  O   . SER   A 1 99  ? 7.681  7.615   25.686 1.00 41.42 ? 105 SER   A O   1 
ATOM   802  C  CB  . SER   A 1 99  ? 8.205  6.159   23.212 1.00 38.55 ? 105 SER   A CB  1 
ATOM   803  O  OG  . SER   A 1 99  ? 9.250  7.015   22.759 1.00 41.76 ? 105 SER   A OG  1 
ATOM   804  N  N   . GLU   A 1 100 ? 9.737  6.884   26.285 1.00 39.75 ? 106 GLU   A N   1 
ATOM   805  C  CA  . GLU   A 1 100 ? 10.092 7.994   27.179 1.00 40.74 ? 106 GLU   A CA  1 
ATOM   806  C  C   . GLU   A 1 100 ? 11.243 8.813   26.531 1.00 42.47 ? 106 GLU   A C   1 
ATOM   807  O  O   . GLU   A 1 100 ? 11.886 8.283   25.615 1.00 42.91 ? 106 GLU   A O   1 
ATOM   808  C  CB  . GLU   A 1 100 ? 10.482 7.437   28.563 1.00 41.61 ? 106 GLU   A CB  1 
ATOM   809  C  CG  . GLU   A 1 100 ? 9.337  6.697   29.228 1.00 45.52 ? 106 GLU   A CG  1 
ATOM   810  C  CD  . GLU   A 1 100 ? 9.626  6.093   30.597 1.00 52.43 ? 106 GLU   A CD  1 
ATOM   811  O  OE1 . GLU   A 1 100 ? 10.238 6.788   31.436 1.00 52.37 ? 106 GLU   A OE1 1 
ATOM   812  O  OE2 . GLU   A 1 100 ? 9.243  4.923   30.831 1.00 53.69 ? 106 GLU   A OE2 1 
ATOM   813  N  N   . PRO   A 1 101 ? 11.544 10.084  26.924 1.00 43.42 ? 107 PRO   A N   1 
ATOM   814  C  CA  . PRO   A 1 101 ? 12.607 10.842  26.206 1.00 43.47 ? 107 PRO   A CA  1 
ATOM   815  C  C   . PRO   A 1 101 ? 13.950 10.097  25.953 1.00 41.90 ? 107 PRO   A C   1 
ATOM   816  O  O   . PRO   A 1 101 ? 14.454 10.084  24.803 1.00 42.15 ? 107 PRO   A O   1 
ATOM   817  C  CB  . PRO   A 1 101 ? 12.785 12.097  27.060 1.00 44.90 ? 107 PRO   A CB  1 
ATOM   818  C  CG  . PRO   A 1 101 ? 11.426 12.300  27.679 1.00 45.73 ? 107 PRO   A CG  1 
ATOM   819  C  CD  . PRO   A 1 101 ? 10.902 10.917  27.969 1.00 43.49 ? 107 PRO   A CD  1 
ATOM   820  N  N   . GLY   A 1 102 ? 14.477 9.426   26.976 1.00 39.09 ? 108 GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 102 ? 15.694 8.628   26.862 1.00 38.00 ? 108 GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 102 ? 15.605 7.417   25.927 1.00 36.29 ? 108 GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 102 ? 16.619 6.770   25.668 1.00 36.47 ? 108 GLY   A O   1 
ATOM   824  N  N   . ASP   A 1 103 ? 14.405 7.095   25.389 1.00 33.68 ? 109 ASP   A N   1 
ATOM   825  C  CA  . ASP   A 1 103 ? 14.247 6.013   24.412 1.00 32.82 ? 109 ASP   A CA  1 
ATOM   826  C  C   . ASP   A 1 103 ? 14.624 6.422   22.985 1.00 31.41 ? 109 ASP   A C   1 
ATOM   827  O  O   . ASP   A 1 103 ? 14.839 5.552   22.140 1.00 29.90 ? 109 ASP   A O   1 
ATOM   828  C  CB  . ASP   A 1 103 ? 12.830 5.430   24.402 1.00 33.29 ? 109 ASP   A CB  1 
ATOM   829  C  CG  . ASP   A 1 103 ? 12.571 4.625   25.652 1.00 35.21 ? 109 ASP   A CG  1 
ATOM   830  O  OD1 . ASP   A 1 103 ? 13.503 3.938   26.112 1.00 34.28 ? 109 ASP   A OD1 1 
ATOM   831  O  OD2 . ASP   A 1 103 ? 11.428 4.677   26.168 1.00 35.36 ? 109 ASP   A OD2 1 
ATOM   832  N  N   . CYS   A 1 104 ? 14.807 7.738   22.721 1.00 31.75 ? 110 CYS   A N   1 
ATOM   833  C  CA  . CYS   A 1 104 ? 15.194 8.181   21.365 1.00 31.39 ? 110 CYS   A CA  1 
ATOM   834  C  C   . CYS   A 1 104 ? 16.526 7.509   20.974 1.00 31.24 ? 110 CYS   A C   1 
ATOM   835  O  O   . CYS   A 1 104 ? 17.403 7.369   21.821 1.00 32.30 ? 110 CYS   A O   1 
ATOM   836  C  CB  . CYS   A 1 104 ? 15.299 9.707   21.299 1.00 33.11 ? 110 CYS   A CB  1 
ATOM   837  S  SG  . CYS   A 1 104 ? 13.708 10.562  21.413 1.00 35.75 ? 110 CYS   A SG  1 
ATOM   838  N  N   . GLY   A 1 105 ? 16.647 7.071   19.736 1.00 29.30 ? 111 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 105 ? 17.841 6.379   19.279 1.00 30.00 ? 111 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 105 ? 17.648 4.873   19.180 1.00 30.46 ? 111 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 105 ? 18.427 4.203   18.501 1.00 30.82 ? 111 GLY   A O   1 
ATOM   842  N  N   . GLY   A 1 106 ? 16.606 4.326   19.843 1.00 29.46 ? 112 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 106 ? 16.299 2.901   19.731 1.00 27.79 ? 112 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 106 ? 15.947 2.533   18.285 1.00 26.99 ? 112 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 106 ? 15.202 3.250   17.603 1.00 26.30 ? 112 GLY   A O   1 
ATOM   846  N  N   . ILE   A 1 107 ? 16.519 1.428   17.784 1.00 25.87 ? 113 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 107 ? 16.270 1.039   16.401 1.00 25.38 ? 113 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 107 ? 14.942 0.338   16.197 1.00 25.27 ? 113 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 107 ? 14.522 -0.490  17.029 1.00 26.23 ? 113 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 107 ? 17.466 0.197   15.857 1.00 27.26 ? 113 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 107 ? 18.650 1.168   15.565 1.00 28.78 ? 113 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 107 ? 17.096 -0.536  14.534 1.00 28.33 ? 113 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 107 ? 19.961 0.448   15.251 1.00 31.81 ? 113 ILE   A CD1 1 
ATOM   854  N  N   . LEU   A 1 108 ? 14.308 0.653   15.059 1.00 24.47 ? 114 LEU   A N   1 
ATOM   855  C  CA  . LEU   A 1 108 ? 13.113 -0.037  14.595 1.00 25.18 ? 114 LEU   A CA  1 
ATOM   856  C  C   . LEU   A 1 108 ? 13.597 -0.851  13.367 1.00 25.65 ? 114 LEU   A C   1 
ATOM   857  O  O   . LEU   A 1 108 ? 14.183 -0.280  12.447 1.00 24.94 ? 114 LEU   A O   1 
ATOM   858  C  CB  . LEU   A 1 108 ? 11.989 0.948   14.192 1.00 25.63 ? 114 LEU   A CB  1 
ATOM   859  C  CG  . LEU   A 1 108 ? 10.825 0.317   13.359 1.00 26.71 ? 114 LEU   A CG  1 
ATOM   860  C  CD1 . LEU   A 1 108 ? 10.049 -0.719  14.188 1.00 27.00 ? 114 LEU   A CD1 1 
ATOM   861  C  CD2 . LEU   A 1 108 ? 9.870  1.422   12.804 1.00 27.64 ? 114 LEU   A CD2 1 
ATOM   862  N  N   . ARG   A 1 109 ? 13.367 -2.169  13.384 1.00 25.81 ? 115 ARG   A N   1 
ATOM   863  C  CA  . ARG   A 1 109 ? 13.792 -3.012  12.275 1.00 27.71 ? 115 ARG   A CA  1 
ATOM   864  C  C   . ARG   A 1 109 ? 12.709 -3.917  11.719 1.00 27.73 ? 115 ARG   A C   1 
ATOM   865  O  O   . ARG   A 1 109 ? 11.810 -4.304  12.438 1.00 27.18 ? 115 ARG   A O   1 
ATOM   866  C  CB  . ARG   A 1 109 ? 15.033 -3.835  12.631 1.00 31.45 ? 115 ARG   A CB  1 
ATOM   867  C  CG  . ARG   A 1 109 ? 14.925 -4.718  13.843 1.00 39.91 ? 115 ARG   A CG  1 
ATOM   868  C  CD  . ARG   A 1 109 ? 16.224 -5.561  13.967 1.00 47.72 ? 115 ARG   A CD  1 
ATOM   869  N  NE  . ARG   A 1 109 ? 17.413 -4.725  14.207 1.00 53.02 ? 115 ARG   A NE  1 
ATOM   870  C  CZ  . ARG   A 1 109 ? 18.360 -4.478  13.301 1.00 56.78 ? 115 ARG   A CZ  1 
ATOM   871  N  NH1 . ARG   A 1 109 ? 18.279 -5.005  12.081 1.00 57.45 ? 115 ARG   A NH1 1 
ATOM   872  N  NH2 . ARG   A 1 109 ? 19.394 -3.700  13.606 1.00 56.28 ? 115 ARG   A NH2 1 
ATOM   873  N  N   . CYS   A 1 110 ? 12.781 -4.210  10.418 1.00 28.62 ? 116 CYS   A N   1 
ATOM   874  C  CA  . CYS   A 1 110 ? 11.854 -5.154  9.802  1.00 29.80 ? 116 CYS   A CA  1 
ATOM   875  C  C   . CYS   A 1 110 ? 12.743 -6.299  9.212  1.00 31.24 ? 116 CYS   A C   1 
ATOM   876  O  O   . CYS   A 1 110 ? 13.970 -6.287  9.378  1.00 32.05 ? 116 CYS   A O   1 
ATOM   877  C  CB  . CYS   A 1 110 ? 11.080 -4.447  8.698  1.00 30.68 ? 116 CYS   A CB  1 
ATOM   878  S  SG  . CYS   A 1 110 ? 12.153 -3.905  7.350  1.00 29.38 ? 116 CYS   A SG  1 
ATOM   879  N  N   . GLN   A 1 111 ? 12.138 -7.223  8.445  1.00 32.24 ? 117 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 111 ? 12.921 -8.293  7.828  1.00 34.31 ? 117 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 111 ? 13.997 -7.791  6.870  1.00 35.60 ? 117 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 111 ? 14.947 -8.530  6.598  1.00 37.52 ? 117 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 111 ? 11.998 -9.260  7.102  1.00 36.77 ? 117 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 111 ? 11.268 -8.646  5.939  1.00 40.74 ? 117 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 111 ? 10.322 -9.646  5.340  1.00 47.38 ? 117 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 111 ? 9.092  -9.464  5.368  1.00 49.66 ? 117 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 111 ? 10.880 -10.738 4.819  1.00 47.50 ? 117 GLN   A NE2 1 
ATOM   888  N  N   . HIS   A 1 112 ? 13.883 -6.546  6.361  1.00 34.84 ? 118 HIS   A N   1 
ATOM   889  C  CA  . HIS   A 1 112 ? 14.867 -6.054  5.385  1.00 35.05 ? 118 HIS   A CA  1 
ATOM   890  C  C   . HIS   A 1 112 ? 16.032 -5.245  5.970  1.00 34.82 ? 118 HIS   A C   1 
ATOM   891  O  O   . HIS   A 1 112 ? 16.990 -4.931  5.251  1.00 36.41 ? 118 HIS   A O   1 
ATOM   892  C  CB  . HIS   A 1 112 ? 14.172 -5.261  4.276  1.00 35.06 ? 118 HIS   A CB  1 
ATOM   893  C  CG  . HIS   A 1 112 ? 13.030 -6.004  3.654  1.00 35.16 ? 118 HIS   A CG  1 
ATOM   894  N  ND1 . HIS   A 1 112 ? 11.736 -5.746  4.025  1.00 36.39 ? 118 HIS   A ND1 1 
ATOM   895  C  CD2 . HIS   A 1 112 ? 13.030 -6.961  2.688  1.00 35.37 ? 118 HIS   A CD2 1 
ATOM   896  C  CE1 . HIS   A 1 112 ? 10.975 -6.522  3.274  1.00 36.89 ? 118 HIS   A CE1 1 
ATOM   897  N  NE2 . HIS   A 1 112 ? 11.714 -7.306  2.482  1.00 36.54 ? 118 HIS   A NE2 1 
ATOM   898  N  N   . GLY   A 1 113 ? 15.950 -4.907  7.256  1.00 32.71 ? 119 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 113 ? 17.006 -4.140  7.890  1.00 31.92 ? 119 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 113 ? 16.460 -3.051  8.783  1.00 29.59 ? 119 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 113 ? 15.333 -3.151  9.283  1.00 28.51 ? 119 GLY   A O   1 
ATOM   902  N  N   . VAL   A 1 114 ? 17.255 -1.992  8.954  1.00 28.85 ? 120 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 114 ? 16.887 -0.838  9.773  1.00 29.09 ? 120 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 114 ? 15.890 0.040   9.048  1.00 27.96 ? 120 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 114 ? 16.116 0.437   7.889  1.00 29.98 ? 120 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 114 ? 18.152 -0.018  10.179 1.00 30.50 ? 120 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 114 ? 17.751 1.231   10.967 1.00 30.78 ? 120 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 114 ? 19.086 -0.884  11.016 1.00 31.52 ? 120 VAL   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? 14.784 0.356   9.726  1.00 25.97 ? 121 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? 13.738 1.208   9.172  1.00 24.91 ? 121 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? 13.889 2.654   9.672  1.00 25.06 ? 121 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? 13.631 3.612   8.953  1.00 26.05 ? 121 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? 12.357 0.634   9.582  1.00 25.06 ? 121 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? 11.203 1.574   9.202  1.00 25.99 ? 121 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? 12.159 -0.766  9.042  1.00 25.43 ? 121 VAL   A CG2 1 
ATOM   916  N  N   . GLY   A 1 116 ? 14.195 2.785   10.963 1.00 24.05 ? 122 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 116 ? 14.342 4.096   11.559 1.00 24.58 ? 122 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 116 ? 14.754 4.049   13.007 1.00 24.44 ? 122 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 116 ? 15.158 3.003   13.511 1.00 25.93 ? 122 GLY   A O   1 
ATOM   920  N  N   . ILE   A 1 117 ? 14.652 5.190   13.668 1.00 24.27 ? 123 ILE   A N   1 
ATOM   921  C  CA  . ILE   A 1 117 ? 15.030 5.274   15.086 1.00 23.79 ? 123 ILE   A CA  1 
ATOM   922  C  C   . ILE   A 1 117 ? 13.936 6.013   15.838 1.00 25.18 ? 123 ILE   A C   1 
ATOM   923  O  O   . ILE   A 1 117 ? 13.304 6.934   15.294 1.00 25.41 ? 123 ILE   A O   1 
ATOM   924  C  CB  . ILE   A 1 117 ? 16.391 5.987   15.312 1.00 24.89 ? 123 ILE   A CB  1 
ATOM   925  C  CG1 . ILE   A 1 117 ? 16.418 7.360   14.643 1.00 27.72 ? 123 ILE   A CG1 1 
ATOM   926  C  CG2 . ILE   A 1 117 ? 17.610 5.111   14.913 1.00 26.05 ? 123 ILE   A CG2 1 
ATOM   927  C  CD1 . ILE   A 1 117 ? 17.771 8.205   14.922 1.00 30.13 ? 123 ILE   A CD1 1 
ATOM   928  N  N   . VAL   A 1 118 ? 13.736 5.684   17.157 1.00 24.87 ? 124 VAL   A N   1 
ATOM   929  C  CA  . VAL   A 1 118 ? 12.749 6.405   17.972 1.00 25.12 ? 124 VAL   A CA  1 
ATOM   930  C  C   . VAL   A 1 118 ? 13.124 7.891   18.002 1.00 25.56 ? 124 VAL   A C   1 
ATOM   931  O  O   . VAL   A 1 118 ? 14.299 8.243   18.183 1.00 25.81 ? 124 VAL   A O   1 
ATOM   932  C  CB  . VAL   A 1 118 ? 12.721 5.863   19.421 1.00 25.69 ? 124 VAL   A CB  1 
ATOM   933  C  CG1 . VAL   A 1 118 ? 11.749 6.668   20.293 1.00 26.76 ? 124 VAL   A CG1 1 
ATOM   934  C  CG2 . VAL   A 1 118 ? 12.339 4.378   19.423 1.00 25.32 ? 124 VAL   A CG2 1 
ATOM   935  N  N   . SER   A 1 119 ? 12.120 8.737   17.837 1.00 25.96 ? 125 SER   A N   1 
ATOM   936  C  CA  . SER   A 1 119 ? 12.291 10.184  17.826 1.00 27.13 ? 125 SER   A CA  1 
ATOM   937  C  C   . SER   A 1 119 ? 11.238 10.877  18.731 1.00 28.93 ? 125 SER   A C   1 
ATOM   938  O  O   . SER   A 1 119 ? 11.535 11.945  19.247 1.00 29.36 ? 125 SER   A O   1 
ATOM   939  C  CB  . SER   A 1 119 ? 12.186 10.707  16.385 1.00 28.96 ? 125 SER   A CB  1 
ATOM   940  O  OG  . SER   A 1 119 ? 12.391 12.113  16.287 1.00 31.15 ? 125 SER   A OG  1 
ATOM   941  N  N   . THR   A 1 120 ? 10.015 10.296  18.906 1.00 29.70 ? 126 THR   A N   1 
ATOM   942  C  CA  . THR   A 1 120 ? 8.959  10.908  19.747 1.00 31.35 ? 126 THR   A CA  1 
ATOM   943  C  C   . THR   A 1 120 ? 8.285  9.871   20.700 1.00 32.25 ? 126 THR   A C   1 
ATOM   944  O  O   . THR   A 1 120 ? 8.420  8.663   20.493 1.00 30.57 ? 126 THR   A O   1 
ATOM   945  C  CB  . THR   A 1 120 ? 7.892  11.627  18.864 1.00 31.72 ? 126 THR   A CB  1 
ATOM   946  O  OG1 . THR   A 1 120 ? 6.988  10.679  18.318 1.00 32.70 ? 126 THR   A OG1 1 
ATOM   947  C  CG2 . THR   A 1 120 ? 8.479  12.455  17.744 1.00 31.62 ? 126 THR   A CG2 1 
ATOM   948  N  N   . GLY   A 1 121 ? 7.545  10.360  21.700 1.00 34.76 ? 127 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 121 ? 6.884  9.460   22.644 1.00 37.23 ? 127 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 121 ? 5.690  10.059  23.363 1.00 40.13 ? 127 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 121 ? 5.144  11.058  22.924 1.00 40.07 ? 127 GLY   A O   1 
ATOM   952  N  N   . GLY   A 1 122 ? 5.270  9.419   24.452 1.00 42.60 ? 128 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 122 ? 4.156  9.915   25.263 1.00 44.72 ? 128 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 122 ? 2.765  9.574   24.763 1.00 46.00 ? 128 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 122 ? 2.575  9.329   23.570 1.00 45.80 ? 128 GLY   A O   1 
ATOM   956  N  N   . ASN   A 1 123 ? 1.777  9.580   25.688 1.00 47.06 ? 129 ASN   A N   1 
ATOM   957  C  CA  . ASN   A 1 123 ? 0.359  9.251   25.436 1.00 47.54 ? 129 ASN   A CA  1 
ATOM   958  C  C   . ASN   A 1 123 ? 0.155  7.814   24.912 1.00 46.16 ? 129 ASN   A C   1 
ATOM   959  O  O   . ASN   A 1 123 ? -0.846 7.533   24.250 1.00 46.58 ? 129 ASN   A O   1 
ATOM   960  C  CB  . ASN   A 1 123 ? -0.292 10.263  24.490 1.00 50.47 ? 129 ASN   A CB  1 
ATOM   961  C  CG  . ASN   A 1 123 ? -0.379 11.657  25.062 1.00 56.41 ? 129 ASN   A CG  1 
ATOM   962  O  OD1 . ASN   A 1 123 ? -0.484 11.845  26.283 1.00 58.27 ? 129 ASN   A OD1 1 
ATOM   963  N  ND2 . ASN   A 1 123 ? -0.340 12.661  24.188 1.00 57.51 ? 129 ASN   A ND2 1 
ATOM   964  N  N   . GLY   A 1 124 ? 1.086  6.914   25.230 1.00 43.37 ? 130 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 124 ? 0.994  5.537   24.782 1.00 41.24 ? 130 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 124 ? 1.356  5.313   23.324 1.00 38.32 ? 130 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 124 ? 1.106  4.233   22.778 1.00 38.16 ? 130 GLY   A O   1 
ATOM   968  N  N   . LEU   A 1 125 ? 2.038  6.286   22.720 1.00 36.49 ? 131 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 125 ? 2.504  6.201   21.343 1.00 34.61 ? 131 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 125 ? 4.040  6.330   21.270 1.00 34.07 ? 131 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 125 ? 4.680  6.858   22.177 1.00 36.20 ? 131 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 125 ? 1.871  7.320   20.511 1.00 34.20 ? 131 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 125 ? 0.334  7.275   20.413 1.00 36.14 ? 131 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 125 ? -0.229 8.645   20.106 1.00 37.94 ? 131 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 125 ? -0.121 6.243   19.412 1.00 35.80 ? 131 LEU   A CD2 1 
ATOM   976  N  N   . VAL   A 1 126 ? 4.614  5.854   20.178 1.00 30.73 ? 132 VAL   A N   1 
ATOM   977  C  CA  . VAL   A 1 126 ? 6.047  5.983   19.894 1.00 28.86 ? 132 VAL   A CA  1 
ATOM   978  C  C   . VAL   A 1 126 ? 6.177  6.386   18.429 1.00 27.34 ? 132 VAL   A C   1 
ATOM   979  O  O   . VAL   A 1 126 ? 5.503  5.825   17.585 1.00 28.07 ? 132 VAL   A O   1 
ATOM   980  C  CB  . VAL   A 1 126 ? 6.840  4.682   20.207 1.00 29.02 ? 132 VAL   A CB  1 
ATOM   981  C  CG1 . VAL   A 1 126 ? 6.148  3.437   19.647 1.00 30.82 ? 132 VAL   A CG1 1 
ATOM   982  C  CG2 . VAL   A 1 126 ? 8.281  4.770   19.706 1.00 27.51 ? 132 VAL   A CG2 1 
ATOM   983  N  N   . GLY   A 1 127 ? 6.979  7.402   18.151 1.00 25.54 ? 133 GLY   A N   1 
ATOM   984  C  CA  . GLY   A 1 127 ? 7.213  7.844   16.781 1.00 25.53 ? 133 GLY   A CA  1 
ATOM   985  C  C   . GLY   A 1 127 ? 8.650  7.532   16.401 1.00 25.86 ? 133 GLY   A C   1 
ATOM   986  O  O   . GLY   A 1 127 ? 9.562  7.706   17.217 1.00 26.41 ? 133 GLY   A O   1 
ATOM   987  N  N   . PHE   A 1 128 ? 8.833  7.120   15.146 1.00 24.97 ? 134 PHE   A N   1 
ATOM   988  C  CA  . PHE   A 1 128 ? 10.128 6.719   14.568 1.00 24.59 ? 134 PHE   A CA  1 
ATOM   989  C  C   . PHE   A 1 128 ? 10.443 7.610   13.376 1.00 24.63 ? 134 PHE   A C   1 
ATOM   990  O  O   . PHE   A 1 128 ? 9.585  7.822   12.519 1.00 24.48 ? 134 PHE   A O   1 
ATOM   991  C  CB  . PHE   A 1 128 ? 10.049 5.271   14.066 1.00 24.86 ? 134 PHE   A CB  1 
ATOM   992  C  CG  . PHE   A 1 128 ? 9.547  4.279   15.111 1.00 25.24 ? 134 PHE   A CG  1 
ATOM   993  C  CD1 . PHE   A 1 128 ? 10.407 3.784   16.090 1.00 26.04 ? 134 PHE   A CD1 1 
ATOM   994  C  CD2 . PHE   A 1 128 ? 8.224  3.840   15.106 1.00 25.84 ? 134 PHE   A CD2 1 
ATOM   995  C  CE1 . PHE   A 1 128 ? 9.966  2.841   17.043 1.00 25.87 ? 134 PHE   A CE1 1 
ATOM   996  C  CE2 . PHE   A 1 128 ? 7.783  2.888   16.035 1.00 26.11 ? 134 PHE   A CE2 1 
ATOM   997  C  CZ  . PHE   A 1 128 ? 8.650  2.405   17.016 1.00 26.02 ? 134 PHE   A CZ  1 
ATOM   998  N  N   . ALA   A 1 129 ? 11.666 8.140   13.340 1.00 24.37 ? 135 ALA   A N   1 
ATOM   999  C  CA  . ALA   A 1 129 ? 12.115 8.937   12.208 1.00 25.42 ? 135 ALA   A CA  1 
ATOM   1000 C  C   . ALA   A 1 129 ? 12.532 7.931   11.099 1.00 26.13 ? 135 ALA   A C   1 
ATOM   1001 O  O   . ALA   A 1 129 ? 13.467 7.145   11.297 1.00 25.92 ? 135 ALA   A O   1 
ATOM   1002 C  CB  . ALA   A 1 129 ? 13.321 9.786   12.631 1.00 25.50 ? 135 ALA   A CB  1 
ATOM   1003 N  N   . ASP   A 1 130 ? 11.840 7.932   9.959  1.00 27.23 ? 136 ASP   A N   1 
ATOM   1004 C  CA  . ASP   A 1 130 ? 12.163 7.017   8.857  1.00 28.19 ? 136 ASP   A CA  1 
ATOM   1005 C  C   . ASP   A 1 130 ? 13.550 7.350   8.242  1.00 28.06 ? 136 ASP   A C   1 
ATOM   1006 O  O   . ASP   A 1 130 ? 13.911 8.525   8.113  1.00 28.23 ? 136 ASP   A O   1 
ATOM   1007 C  CB  . ASP   A 1 130 ? 11.095 7.109   7.743  1.00 30.01 ? 136 ASP   A CB  1 
ATOM   1008 C  CG  . ASP   A 1 130 ? 11.285 6.068   6.656  1.00 34.56 ? 136 ASP   A CG  1 
ATOM   1009 O  OD1 . ASP   A 1 130 ? 11.412 4.880   6.990  1.00 34.55 ? 136 ASP   A OD1 1 
ATOM   1010 O  OD2 . ASP   A 1 130 ? 11.340 6.446   5.473  1.00 38.06 ? 136 ASP   A OD2 1 
ATOM   1011 N  N   . VAL   A 1 131 ? 14.325 6.320   7.855  1.00 27.26 ? 137 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? 15.595 6.537   7.144  1.00 28.96 ? 137 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? 15.572 5.791   5.776  1.00 29.81 ? 137 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? 16.552 5.868   5.054  1.00 31.01 ? 137 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? 16.859 6.138   7.959  1.00 29.31 ? 137 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? 16.891 6.884   9.293  1.00 29.22 ? 137 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? 16.907 4.624   8.193  1.00 29.88 ? 137 VAL   A CG2 1 
ATOM   1018 N  N   . ARG   A 1 132 ? 14.498 5.026   5.440  1.00 29.33 ? 138 ARG   A N   1 
ATOM   1019 C  CA  . ARG   A 1 132 ? 14.448 4.203   4.223  1.00 29.91 ? 138 ARG   A CA  1 
ATOM   1020 C  C   . ARG   A 1 132 ? 14.474 4.983   2.899  1.00 32.61 ? 138 ARG   A C   1 
ATOM   1021 O  O   . ARG   A 1 132 ? 14.834 4.402   1.879  1.00 34.10 ? 138 ARG   A O   1 
ATOM   1022 C  CB  . ARG   A 1 132 ? 13.255 3.249   4.244  1.00 28.74 ? 138 ARG   A CB  1 
ATOM   1023 C  CG  . ARG   A 1 132 ? 13.259 2.252   5.412  1.00 28.23 ? 138 ARG   A CG  1 
ATOM   1024 C  CD  . ARG   A 1 132 ? 11.951 1.455   5.372  1.00 27.47 ? 138 ARG   A CD  1 
ATOM   1025 N  NE  . ARG   A 1 132 ? 10.832 2.319   5.752  1.00 28.01 ? 138 ARG   A NE  1 
ATOM   1026 C  CZ  . ARG   A 1 132 ? 9.586  1.895   5.920  1.00 29.35 ? 138 ARG   A CZ  1 
ATOM   1027 N  NH1 . ARG   A 1 132 ? 9.253  0.643   5.605  1.00 29.84 ? 138 ARG   A NH1 1 
ATOM   1028 N  NH2 . ARG   A 1 132 ? 8.657  2.720   6.382  1.00 29.12 ? 138 ARG   A NH2 1 
ATOM   1029 N  N   . ASP   A 1 133 ? 14.147 6.273   2.912  1.00 33.51 ? 139 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 133 ? 14.213 7.090   1.695  1.00 35.21 ? 139 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 133 ? 15.647 7.643   1.430  1.00 36.62 ? 139 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 133 ? 15.926 8.137   0.335  1.00 38.11 ? 139 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 133 ? 13.217 8.251   1.778  1.00 36.45 ? 139 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 133 ? 13.561 9.262   2.859  1.00 38.80 ? 139 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 133 ? 13.894 8.835   3.993  1.00 37.68 ? 139 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 133 ? 13.499 10.470  2.575  1.00 41.69 ? 139 ASP   A OD2 1 
ATOM   1037 N  N   . LEU   A 1 134 ? 16.549 7.580   2.450  1.00 36.30 ? 140 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 134 ? 17.913 8.130   2.329  1.00 37.31 ? 140 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 134 ? 18.808 7.132   1.594  1.00 39.21 ? 140 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 134 ? 19.667 6.483   2.188  1.00 39.09 ? 140 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 134 ? 18.441 8.433   3.751  1.00 37.45 ? 140 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 134 ? 17.568 9.373   4.589  1.00 38.15 ? 140 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 134 ? 18.126 9.518   6.005  1.00 37.76 ? 140 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 134 ? 17.414 10.750  3.913  1.00 39.58 ? 140 LEU   A CD2 1 
ATOM   1045 N  N   . LEU   A 1 135 ? 18.587 7.006   0.262  1.00 39.91 ? 141 LEU   A N   1 
ATOM   1046 C  CA  . LEU   A 1 135 ? 19.262 6.025   -0.552 1.00 41.81 ? 141 LEU   A CA  1 
ATOM   1047 C  C   . LEU   A 1 135 ? 20.763 6.181   -0.586 1.00 43.93 ? 141 LEU   A C   1 
ATOM   1048 O  O   . LEU   A 1 135 ? 21.477 5.196   -0.764 1.00 44.28 ? 141 LEU   A O   1 
ATOM   1049 C  CB  . LEU   A 1 135 ? 18.675 6.018   -1.978 1.00 42.35 ? 141 LEU   A CB  1 
ATOM   1050 C  CG  . LEU   A 1 135 ? 17.175 5.785   -2.068 1.00 44.24 ? 141 LEU   A CG  1 
ATOM   1051 C  CD1 . LEU   A 1 135 ? 16.742 5.673   -3.519 1.00 46.34 ? 141 LEU   A CD1 1 
ATOM   1052 C  CD2 . LEU   A 1 135 ? 16.751 4.515   -1.331 1.00 44.57 ? 141 LEU   A CD2 1 
ATOM   1053 N  N   . TRP   A 1 136 ? 21.245 7.425   -0.442 1.00 44.86 ? 142 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A 1 136 ? 22.675 7.703   -0.472 1.00 44.86 ? 142 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A 1 136 ? 23.420 7.054   0.701  1.00 45.84 ? 142 TRP   A C   1 
ATOM   1056 O  O   . TRP   A 1 136 ? 24.632 6.927   0.617  1.00 46.02 ? 142 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A 1 136 ? 22.938 9.215   -0.535 1.00 44.16 ? 142 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A 1 136 ? 22.240 9.995   0.533  1.00 43.77 ? 142 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A 1 136 ? 21.034 10.620  0.439  1.00 44.26 ? 142 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A 1 136 ? 22.708 10.217  1.871  1.00 43.34 ? 142 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A 1 136 ? 20.747 11.267  1.617  1.00 44.18 ? 142 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A 1 136 ? 21.753 11.024  2.518  1.00 43.67 ? 142 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A 1 136 ? 23.887 9.883   2.558  1.00 43.94 ? 142 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A 1 136 ? 21.926 11.476  3.824  1.00 43.99 ? 142 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A 1 136 ? 24.043 10.311  3.860  1.00 44.48 ? 142 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A 1 136 ? 23.069 11.089  4.483  1.00 44.19 ? 142 TRP   A CH2 1 
ATOM   1067 N  N   . LEU   A 1 137 ? 22.715 6.633   1.783  1.00 45.99 ? 143 LEU   A N   1 
ATOM   1068 C  CA  . LEU   A 1 137 ? 23.366 5.987   2.927  1.00 47.25 ? 143 LEU   A CA  1 
ATOM   1069 C  C   . LEU   A 1 137 ? 24.121 4.717   2.524  1.00 50.20 ? 143 LEU   A C   1 
ATOM   1070 O  O   . LEU   A 1 137 ? 25.026 4.321   3.249  1.00 49.87 ? 143 LEU   A O   1 
ATOM   1071 C  CB  . LEU   A 1 137 ? 22.365 5.655   4.057  1.00 46.37 ? 143 LEU   A CB  1 
ATOM   1072 C  CG  . LEU   A 1 137 ? 21.877 6.827   4.911  1.00 45.61 ? 143 LEU   A CG  1 
ATOM   1073 C  CD1 . LEU   A 1 137 ? 20.738 6.400   5.827  1.00 45.52 ? 143 LEU   A CD1 1 
ATOM   1074 C  CD2 . LEU   A 1 137 ? 22.988 7.379   5.778  1.00 45.95 ? 143 LEU   A CD2 1 
ATOM   1075 N  N   . ASP   A 1 138 ? 23.727 4.075   1.393  1.00 53.11 ? 144 ASP   A N   1 
ATOM   1076 C  CA  . ASP   A 1 138 ? 24.298 2.841   0.831  1.00 56.70 ? 144 ASP   A CA  1 
ATOM   1077 C  C   . ASP   A 1 138 ? 25.524 3.070   -0.044 1.00 60.89 ? 144 ASP   A C   1 
ATOM   1078 O  O   . ASP   A 1 138 ? 26.099 2.086   -0.510 1.00 61.42 ? 144 ASP   A O   1 
ATOM   1079 C  CB  . ASP   A 1 138 ? 23.273 2.133   -0.067 1.00 58.51 ? 144 ASP   A CB  1 
ATOM   1080 C  CG  . ASP   A 1 138 ? 22.019 1.638   0.611  1.00 63.40 ? 144 ASP   A CG  1 
ATOM   1081 O  OD1 . ASP   A 1 138 ? 22.036 1.481   1.851  1.00 64.23 ? 144 ASP   A OD1 1 
ATOM   1082 O  OD2 . ASP   A 1 138 ? 21.012 1.407   -0.101 1.00 65.55 ? 144 ASP   A OD2 1 
ATOM   1083 N  N   . GLU   A 1 139 ? 25.900 4.333   -0.327 1.00 63.57 ? 145 GLU   A N   1 
ATOM   1084 C  CA  . GLU   A 1 139 ? 27.049 4.596   -1.191 1.00 67.06 ? 145 GLU   A CA  1 
ATOM   1085 C  C   . GLU   A 1 139 ? 27.869 5.825   -0.759 1.00 69.96 ? 145 GLU   A C   1 
ATOM   1086 O  O   . GLU   A 1 139 ? 27.368 6.662   0.001  1.00 70.58 ? 145 GLU   A O   1 
ATOM   1087 C  CB  . GLU   A 1 139 ? 26.579 4.744   -2.651 1.00 70.65 ? 145 GLU   A CB  1 
ATOM   1088 C  CG  . GLU   A 1 139 ? 25.785 6.013   -2.920 1.00 77.00 ? 145 GLU   A CG  1 
ATOM   1089 C  CD  . GLU   A 1 139 ? 24.494 5.794   -3.684 1.00 85.40 ? 145 GLU   A CD  1 
ATOM   1090 O  OE1 . GLU   A 1 139 ? 24.184 6.613   -4.581 1.00 87.06 ? 145 GLU   A OE1 1 
ATOM   1091 O  OE2 . GLU   A 1 139 ? 23.792 4.800   -3.385 1.00 88.01 ? 145 GLU   A OE2 1 
ATOM   1092 N  N   . GLU   A 1 140 ? 29.122 5.942   -1.270 1.00 71.54 ? 146 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 140 ? 30.020 7.077   -1.008 1.00 73.24 ? 146 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 140 ? 30.201 7.329   0.502  1.00 74.26 ? 146 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 140 ? 31.276 7.714   0.963  1.00 74.85 ? 146 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 140 ? 29.538 8.330   -1.793 1.00 75.88 ? 146 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 140 ? 29.774 9.693   -1.154 1.00 81.39 ? 146 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 140 ? 30.957 10.472  -1.694 1.00 88.46 ? 146 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 140 ? 30.979 11.712  -1.518 1.00 90.27 ? 146 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 140 ? 31.860 9.847   -2.296 1.00 90.68 ? 146 GLU   A OE2 1 
HETATM 1101 N  N1  . A1BPZ B 2 .   ? 10.137 14.622  22.323 1.00 47.88 ? 201 A1BPZ A N1  1 
HETATM 1102 C  C4  . A1BPZ B 2 .   ? 11.280 15.212  23.036 1.00 47.14 ? 201 A1BPZ A C4  1 
HETATM 1103 C  C5  . A1BPZ B 2 .   ? 9.396  13.581  22.761 1.00 49.52 ? 201 A1BPZ A C5  1 
HETATM 1104 C  C6  . A1BPZ B 2 .   ? 9.876  12.889  24.025 1.00 52.82 ? 201 A1BPZ A C6  1 
HETATM 1105 C  C7  . A1BPZ B 2 .   ? 8.755  12.593  24.998 1.00 56.10 ? 201 A1BPZ A C7  1 
HETATM 1106 C  C8  . A1BPZ B 2 .   ? 8.507  11.267  25.349 1.00 56.41 ? 201 A1BPZ A C8  1 
HETATM 1107 C  C10 . A1BPZ B 2 .   ? 6.801  11.948  26.883 1.00 57.69 ? 201 A1BPZ A C10 1 
HETATM 1108 C  C13 . A1BPZ B 2 .   ? 8.239  15.074  25.330 1.00 62.47 ? 201 A1BPZ A C13 1 
HETATM 1109 O  O3  . A1BPZ B 2 .   ? 10.642 15.398  26.307 1.00 66.19 ? 201 A1BPZ A O3  1 
HETATM 1110 S  S   . A1BPZ B 2 .   ? 9.302  15.833  26.551 1.00 65.87 ? 201 A1BPZ A S   1 
HETATM 1111 O  O2  . A1BPZ B 2 .   ? 8.705  15.632  27.834 1.00 66.80 ? 201 A1BPZ A O2  1 
HETATM 1112 N  N2  . A1BPZ B 2 .   ? 9.203  17.397  26.197 1.00 65.94 ? 201 A1BPZ A N2  1 
HETATM 1113 C  C12 . A1BPZ B 2 .   ? 7.997  13.611  25.605 1.00 59.05 ? 201 A1BPZ A C12 1 
HETATM 1114 C  C11 . A1BPZ B 2 .   ? 7.018  13.269  26.538 1.00 58.42 ? 201 A1BPZ A C11 1 
HETATM 1115 C  C9  . A1BPZ B 2 .   ? 7.546  10.951  26.294 1.00 57.07 ? 201 A1BPZ A C9  1 
HETATM 1116 O  O1  . A1BPZ B 2 .   ? 8.388  13.213  22.176 1.00 48.29 ? 201 A1BPZ A O1  1 
HETATM 1117 C  C3  . A1BPZ B 2 .   ? 12.560 15.037  22.229 1.00 46.35 ? 201 A1BPZ A C3  1 
HETATM 1118 C  C2  . A1BPZ B 2 .   ? 12.387 15.579  20.807 1.00 45.99 ? 201 A1BPZ A C2  1 
HETATM 1119 C  C14 . A1BPZ B 2 .   ? 9.909  15.220  21.004 1.00 46.42 ? 201 A1BPZ A C14 1 
HETATM 1120 C  C1  . A1BPZ B 2 .   ? 11.141 14.988  20.125 1.00 45.39 ? 201 A1BPZ A C1  1 
HETATM 1121 C  C   . A1BPZ B 2 .   ? 10.973 15.524  18.714 1.00 44.12 ? 201 A1BPZ A C   1 
HETATM 1122 O  O   . A1BPZ B 2 .   ? 10.466 16.630  18.510 1.00 43.01 ? 201 A1BPZ A O   1 
HETATM 1123 N  N   . A1BPZ B 2 .   ? 11.393 14.729  17.738 1.00 43.34 ? 201 A1BPZ A N   1 
HETATM 1124 ZN ZN  . ZN    C 3 .   ? 10.973 -4.132  5.295  1.00 32.15 2 202 ZN    A ZN  1 
HETATM 1125 S  S   . DMS   D 4 .   ? 0.838  -1.657  23.807 1.00 90.98 ? 203 DMS   A S   1 
HETATM 1126 O  O   . DMS   D 4 .   ? 0.911  -0.187  24.118 1.00 90.96 ? 203 DMS   A O   1 
HETATM 1127 C  C1  . DMS   D 4 .   ? 1.016  -2.546  25.384 1.00 91.04 ? 203 DMS   A C1  1 
HETATM 1128 C  C2  . DMS   D 4 .   ? -0.907 -2.099  23.528 1.00 90.86 ? 203 DMS   A C2  1 
HETATM 1129 O  O   . HOH   E 5 .   ? 29.219 3.527   10.115 1.00 41.11 ? 301 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 11.259 -4.590  31.638 1.00 58.19 ? 302 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 23.844 22.448  8.569  1.00 50.32 ? 303 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 6.216  3.338   3.085  1.00 52.36 ? 304 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 12.676 7.353   30.925 1.00 46.36 ? 305 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 2.828  8.564   10.206 1.00 56.71 ? 306 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 8.261  -3.562  0.348  1.00 39.78 ? 307 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 18.449 5.067   26.439 1.00 47.85 ? 308 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 0.237  2.407   24.450 1.00 51.73 ? 309 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 31.487 8.221   3.543  1.00 57.22 ? 310 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 10.274 5.341   3.307  1.00 36.11 ? 311 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 4.164  -4.315  21.114 1.00 41.48 ? 312 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 14.902 11.762  0.720  1.00 50.32 ? 313 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 19.456 -0.864  30.760 1.00 51.60 ? 314 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 19.234 -0.078  27.291 1.00 46.53 ? 315 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 23.430 0.265   15.520 1.00 39.39 ? 316 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 9.697  24.538  24.205 1.00 52.20 ? 317 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 10.249 8.712   4.496  1.00 40.36 ? 318 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 22.340 -0.446  3.716  1.00 41.96 ? 319 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 9.660  18.578  20.270 1.00 35.12 ? 320 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 20.182 9.264   18.877 1.00 33.00 ? 321 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 25.988 4.626   19.552 1.00 65.52 ? 322 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 11.633 2.583   33.371 1.00 36.84 ? 323 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 17.934 0.970   29.733 1.00 56.96 ? 324 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 18.439 -4.374  27.546 1.00 64.82 ? 325 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 27.648 3.914   2.609  1.00 53.86 ? 326 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 8.172  19.844  18.228 1.00 33.79 ? 327 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 8.129  -8.297  23.262 1.00 46.36 ? 328 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 4.658  6.190   24.829 1.00 38.55 ? 329 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 6.542  -5.083  28.871 1.00 57.07 ? 330 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 3.145  22.237  22.432 1.00 52.47 ? 331 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 17.617 -6.248  2.926  1.00 54.74 ? 332 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 0.650  0.165   16.527 1.00 29.70 ? 333 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 18.007 2.821   22.857 1.00 35.06 ? 334 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 16.348 23.533  14.669 1.00 66.31 ? 335 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 12.318 21.701  12.784 1.00 43.14 ? 336 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 23.665 4.382   23.102 1.00 64.94 ? 337 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 8.811  3.079   2.721  1.00 34.62 ? 338 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? -0.199 16.573  8.363  1.00 66.38 ? 339 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 31.335 3.178   12.366 1.00 56.88 ? 340 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 23.698 -5.951  7.989  1.00 62.01 ? 341 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 1.078  -2.093  19.962 1.00 40.23 ? 342 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 11.324 12.178  11.351 1.00 29.26 ? 343 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 15.020 2.881   23.074 1.00 29.26 ? 344 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 11.087 17.851  5.451  1.00 63.12 ? 345 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 30.541 21.539  19.970 1.00 48.80 ? 346 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 10.899 9.266   23.146 1.00 45.52 ? 347 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 18.110 19.291  16.920 1.00 36.07 ? 348 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 20.425 2.222   18.300 1.00 46.76 ? 349 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 0.208  14.578  17.138 1.00 46.08 ? 350 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 15.259 12.674  23.995 1.00 45.75 ? 351 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 17.335 20.593  19.379 1.00 47.56 ? 352 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 4.353  7.892   3.138  1.00 52.70 ? 353 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 28.276 11.786  1.304  1.00 76.84 ? 354 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 13.910 9.715   29.759 1.00 47.63 ? 355 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 6.355  17.778  25.100 1.00 57.82 ? 356 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 13.070 11.005  9.259  1.00 29.69 ? 357 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 14.489 15.043  3.536  1.00 42.66 ? 358 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 21.781 -4.617  12.313 1.00 48.69 ? 359 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 27.507 16.773  2.425  1.00 55.86 ? 360 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 17.773 21.499  9.122  1.00 43.44 ? 361 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 8.963  -5.010  32.478 1.00 58.75 ? 362 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 4.398  11.038  19.516 1.00 70.39 ? 363 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 7.089  16.756  22.338 1.00 48.69 ? 364 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 18.648 13.265  1.611  1.00 54.79 ? 365 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 5.833  2.139   6.084  1.00 42.29 ? 366 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 5.851  14.613  22.278 1.00 55.74 ? 367 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 20.995 -4.407  9.823  1.00 46.32 ? 368 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 7.307  4.042   32.930 1.00 47.27 ? 369 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 19.247 9.412   25.668 1.00 44.90 ? 370 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 14.566 21.463  8.198  1.00 56.34 ? 371 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 30.058 5.105   3.412  1.00 55.46 ? 372 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 5.588  -0.915  24.096 1.00 37.31 ? 373 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 34.537 7.041   13.878 1.00 66.37 ? 374 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 13.069 -8.228  24.440 1.00 37.78 ? 375 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 26.931 -1.287  6.446  1.00 60.87 ? 376 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 10.033 4.917   33.709 1.00 39.46 ? 377 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 0.065  4.130   6.537  1.00 55.85 ? 378 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 6.629  13.345  5.452  1.00 38.79 ? 379 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 23.869 2.675   19.152 1.00 47.98 ? 380 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 21.996 9.035   21.079 1.00 41.96 ? 381 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 18.744 0.147   19.297 1.00 42.53 ? 382 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 1.833  13.807  5.596  1.00 44.70 ? 383 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 3.726  0.866   30.476 1.00 61.16 ? 384 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 8.205  8.580   32.690 1.00 60.19 ? 385 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 36.750 -0.243  9.180  1.00 54.24 ? 386 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 31.672 0.250   13.477 1.00 62.15 ? 387 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 4.044  -4.663  6.075  1.00 46.63 ? 388 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? -0.676 15.672  13.183 1.00 38.64 ? 389 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 4.293  -1.790  21.638 1.00 46.37 ? 390 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 0.964  9.021   4.417  1.00 62.52 ? 391 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 15.445 -3.365  17.299 1.00 38.53 ? 392 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 15.468 -3.978  1.230  1.00 43.57 ? 393 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 20.792 3.207   -2.960 1.00 59.03 ? 394 HOH   A O   1 
HETATM 1223 O  O   . HOH   E 5 .   ? 30.852 11.024  14.342 1.00 69.27 ? 395 HOH   A O   1 
HETATM 1224 O  O   . HOH   E 5 .   ? 21.762 19.574  18.048 1.00 63.80 ? 396 HOH   A O   1 
HETATM 1225 O  O   . HOH   E 5 .   ? 1.480  -2.329  17.346 1.00 38.18 ? 397 HOH   A O   1 
HETATM 1226 O  O   . HOH   E 5 .   ? 31.138 19.182  8.533  1.00 58.15 ? 398 HOH   A O   1 
HETATM 1227 O  O   . HOH   E 5 .   ? 3.474  15.332  20.535 1.00 41.55 ? 399 HOH   A O   1 
HETATM 1228 O  O   . HOH   E 5 .   ? 18.613 20.078  4.965  1.00 54.99 ? 400 HOH   A O   1 
HETATM 1229 O  O   . HOH   E 5 .   ? 30.825 -3.583  6.830  1.00 58.20 ? 401 HOH   A O   1 
HETATM 1230 O  O   . HOH   E 5 .   ? 6.206  23.280  11.179 1.00 48.30 ? 402 HOH   A O   1 
HETATM 1231 O  O   . HOH   E 5 .   ? 2.150  -6.268  17.968 1.00 55.30 ? 403 HOH   A O   1 
HETATM 1232 O  O   . HOH   E 5 .   ? 6.516  -3.685  -1.775 1.00 61.59 ? 404 HOH   A O   1 
HETATM 1233 O  O   . HOH   E 5 .   ? 3.929  -4.032  3.215  1.00 60.99 ? 405 HOH   A O   1 
HETATM 1234 O  O   . HOH   E 5 .   ? 30.471 11.324  17.863 1.00 48.74 ? 406 HOH   A O   1 
HETATM 1235 O  O   . HOH   E 5 .   ? 2.356  -1.993  4.102  1.00 74.42 ? 407 HOH   A O   1 
HETATM 1236 O  O   . HOH   E 5 .   ? 17.810 21.053  25.915 1.00 73.41 ? 408 HOH   A O   1 
HETATM 1237 O  O   . HOH   E 5 .   ? 31.441 9.718   5.187  1.00 59.86 ? 409 HOH   A O   1 
HETATM 1238 O  O   . HOH   E 5 .   ? 22.373 19.338  5.562  1.00 48.44 ? 410 HOH   A O   1 
HETATM 1239 O  O   . HOH   E 5 .   ? 3.111  10.287  28.456 1.00 58.72 ? 411 HOH   A O   1 
HETATM 1240 O  O   . HOH   E 5 .   ? 2.839  3.476   27.287 1.00 54.72 ? 412 HOH   A O   1 
HETATM 1241 O  O   . HOH   E 5 .   ? 17.877 9.550   -1.742 1.00 60.15 ? 413 HOH   A O   1 
HETATM 1242 O  O   . HOH   E 5 .   ? 2.461  1.051   26.607 1.00 58.65 ? 414 HOH   A O   1 
HETATM 1243 O  O   . HOH   E 5 .   ? 32.719 14.376  6.159  1.00 62.17 ? 415 HOH   A O   1 
HETATM 1244 O  O   . HOH   E 5 .   ? 36.486 2.513   5.764  1.00 73.30 ? 416 HOH   A O   1 
HETATM 1245 O  O   . HOH   E 5 .   ? 5.378  8.018   28.039 1.00 69.12 ? 417 HOH   A O   1 
HETATM 1246 O  O   . HOH   E 5 .   ? 8.563  -7.043  8.250  1.00 57.24 ? 418 HOH   A O   1 
HETATM 1247 O  O   . HOH   E 5 .   ? 7.393  -4.960  2.529  1.00 50.03 ? 419 HOH   A O   1 
HETATM 1248 O  O   . HOH   E 5 .   ? 5.351  -6.980  14.090 1.00 60.05 ? 420 HOH   A O   1 
HETATM 1249 O  O   . HOH   E 5 .   ? 30.195 10.660  20.404 1.00 70.72 ? 421 HOH   A O   1 
HETATM 1250 O  O   . HOH   E 5 .   ? 2.421  6.031   28.218 1.00 52.78 ? 422 HOH   A O   1 
HETATM 1251 O  O   . HOH   E 5 .   ? 7.129  11.436  4.003  1.00 56.65 ? 423 HOH   A O   1 
HETATM 1252 O  O   . HOH   E 5 .   ? 28.367 -1.485  13.646 1.00 60.85 ? 424 HOH   A O   1 
HETATM 1253 O  O   . HOH   E 5 .   ? 10.069 10.137  32.118 1.00 61.69 ? 425 HOH   A O   1 
HETATM 1254 O  O   . HOH   E 5 .   ? 26.046 -2.114  14.956 1.00 54.35 ? 426 HOH   A O   1 
HETATM 1255 O  O   . HOH   E 5 .   ? 4.515  -1.212  29.071 1.00 59.46 ? 427 HOH   A O   1 
HETATM 1256 O  O   . HOH   E 5 .   ? 24.638 6.889   21.112 1.00 65.47 ? 428 HOH   A O   1 
HETATM 1257 O  O   . HOH   E 5 .   ? 20.770 7.539   -4.747 1.00 52.77 ? 429 HOH   A O   1 
HETATM 1258 O  O   . HOH   E 5 .   ? 20.707 -6.543  15.319 1.00 70.93 ? 430 HOH   A O   1 
HETATM 1259 O  O   . HOH   E 5 .   ? -0.852 24.089  14.141 1.00 58.88 ? 431 HOH   A O   1 
HETATM 1260 O  O   . HOH   E 5 .   ? 3.544  13.141  18.286 1.00 52.35 ? 432 HOH   A O   1 
HETATM 1261 O  O   . HOH   E 5 .   ? -0.678 6.565   28.412 1.00 67.35 ? 433 HOH   A O   1 
HETATM 1262 O  O   . HOH   E 5 .   ? 2.937  -6.315  15.075 1.00 62.51 ? 434 HOH   A O   1 
HETATM 1263 O  O   . HOH   E 5 .   ? 19.622 -3.869  22.605 1.00 61.48 ? 435 HOH   A O   1 
HETATM 1264 O  O   . HOH   E 5 .   ? 17.247 11.573  0.039  1.00 53.22 ? 436 HOH   A O   1 
HETATM 1265 O  O   . HOH   E 5 .   ? 12.539 14.742  1.051  1.00 62.07 ? 437 HOH   A O   1 
HETATM 1266 O  O   . HOH   E 5 .   ? 14.659 -9.169  27.299 1.00 77.62 ? 438 HOH   A O   1 
HETATM 1267 O  O   . HOH   E 5 .   ? 23.506 16.346  1.867  1.00 74.67 ? 439 HOH   A O   1 
HETATM 1268 O  O   . HOH   E 5 .   ? 7.970  -7.763  1.631  1.00 63.96 ? 440 HOH   A O   1 
HETATM 1269 O  O   . HOH   E 5 .   ? 14.982 -8.730  12.218 1.00 67.07 ? 441 HOH   A O   1 
HETATM 1270 O  O   . HOH   E 5 .   ? 22.972 24.537  13.195 1.00 52.26 ? 442 HOH   A O   1 
HETATM 1271 O  O   . HOH   E 5 .   ? 13.554 -13.564 5.146  1.00 73.15 ? 443 HOH   A O   1 
HETATM 1272 O  O   . HOH   E 5 .   ? 11.987 23.704  14.867 1.00 46.51 ? 444 HOH   A O   1 
HETATM 1273 O  O   . HOH   E 5 .   ? 36.989 17.472  13.550 1.00 53.66 ? 445 HOH   A O   1 
HETATM 1274 O  O   . HOH   E 5 .   ? 22.341 -2.839  34.290 1.00 61.97 ? 446 HOH   A O   1 
HETATM 1275 O  O   . HOH   E 5 .   ? 37.629 18.485  16.087 1.00 62.41 ? 447 HOH   A O   1 
HETATM 1276 O  O   . HOH   E 5 .   ? 20.288 15.017  0.321  1.00 60.96 ? 448 HOH   A O   1 
HETATM 1277 O  O   . HOH   E 5 .   ? -1.582 19.030  25.137 1.00 70.93 ? 449 HOH   A O   1 
HETATM 1278 O  O   . HOH   E 5 .   ? 4.169  -1.320  26.461 1.00 58.70 ? 450 HOH   A O   1 
HETATM 1279 O  O   . HOH   E 5 .   ? 14.523 -12.140 8.510  1.00 73.55 ? 451 HOH   A O   1 
HETATM 1280 O  O   . HOH   E 5 .   ? 16.511 14.447  1.821  1.00 59.26 ? 452 HOH   A O   1 
HETATM 1281 O  O   . HOH   E 5 .   ? 23.871 13.897  0.681  1.00 63.33 ? 453 HOH   A O   1 
HETATM 1282 O  O   . HOH   E 5 .   ? 31.258 6.804   15.983 1.00 56.26 ? 454 HOH   A O   1 
HETATM 1283 O  O   . HOH   E 5 .   ? 32.069 5.026   14.406 1.00 60.45 ? 455 HOH   A O   1 
HETATM 1284 O  O   . HOH   E 5 .   ? 19.626 9.952   -3.491 1.00 58.87 ? 456 HOH   A O   1 
HETATM 1285 O  O   . HOH   E 5 .   ? 36.293 18.452  22.766 1.00 61.07 ? 457 HOH   A O   1 
HETATM 1286 O  O   . HOH   E 5 .   ? 5.659  -8.593  2.865  1.00 62.32 ? 458 HOH   A O   1 
HETATM 1287 O  O   . HOH   E 5 .   ? 8.561  7.739   2.355  1.00 50.23 ? 459 HOH   A O   1 
HETATM 1288 O  O   . HOH   E 5 .   ? 5.991  5.941   2.242  1.00 69.70 ? 460 HOH   A O   1 
HETATM 1289 O  O   . HOH   E 5 .   ? 0.601  4.208   28.700 1.00 73.55 ? 461 HOH   A O   1 
HETATM 1290 O  O   . HOH   E 5 .   ? 22.923 10.062  23.388 1.00 54.47 ? 462 HOH   A O   1 
HETATM 1291 O  O   . HOH   E 5 .   ? 25.866 11.349  -1.180 1.00 64.83 ? 463 HOH   A O   1 
HETATM 1292 O  O   . HOH   E 5 .   ? 0.969  12.199  18.173 1.00 69.72 ? 464 HOH   A O   1 
HETATM 1293 O  O   . HOH   E 5 .   ? 18.481 -2.638  18.213 1.00 52.65 ? 465 HOH   A O   1 
HETATM 1294 O  O   . HOH   E 5 .   ? 24.233 11.026  -3.429 1.00 79.58 ? 466 HOH   A O   1 
HETATM 1295 O  O   . HOH   E 5 .   ? 38.384 6.834   5.590  1.00 67.20 ? 467 HOH   A O   1 
HETATM 1296 O  O   . HOH   E 5 .   ? 12.367 -13.452 8.245  1.00 68.69 ? 468 HOH   A O   1 
HETATM 1297 O  O   . HOH   E 5 .   ? 21.463 12.369  -2.825 1.00 80.27 ? 469 HOH   A O   1 
HETATM 1298 O  O   . HOH   E 5 .   ? 3.801  -6.292  22.899 1.00 50.29 ? 470 HOH   A O   1 
HETATM 1299 O  O   . HOH   E 5 .   ? 18.027 15.129  30.443 1.00 74.62 ? 471 HOH   A O   1 
HETATM 1300 O  O   . HOH   E 5 .   ? 5.166  -7.096  27.082 1.00 80.45 ? 472 HOH   A O   1 
HETATM 1301 O  O   . HOH   E 5 .   ? 17.648 -7.144  31.299 1.00 74.11 ? 473 HOH   A O   1 
HETATM 1302 O  O   . HOH   E 5 .   ? 5.708  -7.891  23.656 1.00 55.44 ? 474 HOH   A O   1 
HETATM 1303 O  O   . HOH   E 5 .   ? 14.607 12.187  -1.830 1.00 63.22 ? 475 HOH   A O   1 
HETATM 1304 O  O   . HOH   E 5 .   ? 36.257 18.352  7.084  1.00 65.79 ? 476 HOH   A O   1 
HETATM 1305 O  O   . HOH   E 5 .   ? 3.464  -5.311  25.588 1.00 70.05 ? 477 HOH   A O   1 
HETATM 1306 O  O   . HOH   E 5 .   ? 10.086 25.243  13.485 1.00 55.44 ? 478 HOH   A O   1 
HETATM 1307 O  O   . HOH   E 5 .   ? 2.648  -9.114  16.236 1.00 72.16 ? 479 HOH   A O   1 
HETATM 1308 O  O   . HOH   E 5 .   ? 5.022  23.368  8.224  1.00 65.40 ? 480 HOH   A O   1 
HETATM 1309 O  O   . HOH   E 5 .   ? 4.476  24.782  5.627  1.00 87.67 ? 481 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   ? 0.6046 0.4137 0.5365 0.0508  -0.1931 -0.0535 7   SER   A N   
2    C CA  . SER   A 1   ? 0.5873 0.4133 0.5824 0.0446  -0.2008 -0.0521 7   SER   A CA  
3    C C   . SER   A 1   ? 0.5604 0.4061 0.5753 0.0373  -0.1814 -0.0396 7   SER   A C   
4    O O   . SER   A 1   ? 0.5758 0.4191 0.5557 0.0376  -0.1688 -0.0335 7   SER   A O   
5    C CB  . SER   A 1   ? 0.6296 0.4384 0.6388 0.0509  -0.2357 -0.0622 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.6999 0.4992 0.6893 0.0548  -0.2438 -0.0578 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.5172 0.3804 0.5880 0.0310  -0.1772 -0.0360 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4874 0.3657 0.5761 0.0251  -0.1587 -0.0261 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.4474 0.3447 0.5803 0.0179  -0.1404 -0.0200 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.4331 0.3354 0.5725 0.0162  -0.1345 -0.0200 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.4212 0.3276 0.5792 0.0143  -0.1279 -0.0135 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3996 0.3197 0.5938 0.0090  -0.1073 -0.0065 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3895 0.3160 0.5783 0.0055  -0.0854 0.0004  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.4117 0.3333 0.5875 0.0069  -0.0891 -0.0006 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3837 0.3046 0.6413 0.0097  -0.1180 -0.0086 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.3619 0.2967 0.5592 0.0017  -0.0626 0.0075  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.3581 0.2955 0.5510 -0.0008 -0.0409 0.0126  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3663 0.3056 0.6161 -0.0005 -0.0309 0.0164  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3643 0.3061 0.6473 -0.0006 -0.0289 0.0194  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.3538 0.2950 0.5138 -0.0038 -0.0219 0.0182  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.3488 0.2908 0.4652 -0.0043 -0.0309 0.0153  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3635 0.3030 0.5116 -0.0055 -0.0012 0.0210  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.3479 0.2946 0.4417 -0.0063 -0.0186 0.0212  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3766 0.3141 0.6416 0.0001  -0.0223 0.0168  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3801 0.3193 0.7037 0.0008  -0.0079 0.0211  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.4022 0.3386 0.7095 -0.0001 0.0246  0.0263  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.4204 0.3529 0.7113 0.0003  0.0279  0.0231  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.3709 0.3089 0.7393 0.0040  -0.0282 0.0163  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3977 0.3344 0.7818 0.0061  -0.0616 0.0099  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3951 0.3353 0.8359 0.0059  -0.0671 0.0102  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.4375 0.3666 0.7779 0.0088  -0.0869 0.0033  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.4115 0.3476 0.8623 0.0080  -0.0996 0.0020  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.4582 0.3813 0.8028 0.0120  -0.1172 -0.0039 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.4519 0.3784 0.8517 0.0116  -0.1253 -0.0057 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.4904 0.4082 0.8919 0.0151  -0.1575 -0.0153 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.4058 0.3413 0.7095 -0.0008 0.0481  0.0341  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.4210 0.3488 0.6998 -0.0002 0.0795  0.0387  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.4284 0.3534 0.7568 0.0020  0.1069  0.0481  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.4338 0.3607 0.7810 0.0018  0.1106  0.0553  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4520 0.3758 0.6622 -0.0016 0.0840  0.0400  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4369 0.3645 0.6470 -0.0020 0.0793  0.0466  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4746 0.3856 0.6523 0.0003  0.1137  0.0430  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.4282 0.3482 0.7837 0.0043  0.1270  0.0484  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4300 0.3465 0.8405 0.0070  0.1576  0.0580  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.4276 0.3553 0.9150 0.0059  0.1414  0.0601  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.4213 0.3573 0.9360 0.0050  0.1083  0.0515  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.4279 0.3538 0.9454 0.0063  0.1617  0.0713  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.4145 0.3500 1.0073 0.0046  0.1450  0.0723  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.4136 0.3521 0.9757 0.0020  0.1214  0.0709  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.4005 0.3410 1.0079 0.0009  0.1224  0.0767  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.4369 0.3693 1.0999 0.0063  0.1817  0.0852  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.5156 0.4478 1.2262 0.0091  0.1982  0.0839  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.5272 0.4698 1.3122 0.0086  0.1766  0.0780  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5502 0.4693 1.2167 0.0128  0.2342  0.0881  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.4217 0.3601 0.9113 0.0010  0.1004  0.0631  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.4201 0.3608 0.8789 -0.0007 0.0792  0.0610  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.4042 0.3493 0.8436 -0.0014 0.0398  0.0468  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3989 0.3434 0.8166 -0.0007 0.0321  0.0403  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.4567 0.3907 0.8418 -0.0002 0.0961  0.0680  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4796 0.4036 0.8654 0.0023  0.1348  0.0836  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4807 0.4039 0.9181 0.0025  0.1466  0.0941  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.5144 0.4268 0.8430 0.0049  0.1589  0.0878  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.5042 0.4148 0.9376 0.0058  0.1850  0.1108  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.5449 0.4430 0.8625 0.0089  0.1951  0.1028  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.5437 0.4406 0.9137 0.0096  0.2098  0.1154  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5787 0.4583 0.9342 0.0146  0.2487  0.1325  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.3993 0.3465 0.8466 -0.0020 0.0164  0.0422  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.3978 0.3446 0.8187 -0.0013 -0.0184 0.0295  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.3964 0.3424 0.7697 -0.0018 -0.0210 0.0302  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.3859 0.3320 0.7829 -0.0024 -0.0181 0.0343  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3958 0.3423 0.8757 -0.0001 -0.0471 0.0207  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.4460 0.3866 0.8927 0.0022  -0.0821 0.0079  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.4688 0.4054 0.9698 0.0045  -0.1142 -0.0025 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.4960 0.4243 0.9825 0.0065  -0.1409 -0.0133 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.5294 0.4461 0.9681 0.0111  -0.1682 -0.0246 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.5417 0.4547 0.9433 0.0139  -0.1727 -0.0250 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.5305 0.4369 0.9554 0.0136  -0.1892 -0.0350 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.3899 0.3351 0.7015 -0.0017 -0.0248 0.0271  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.3871 0.3326 0.6567 -0.0019 -0.0266 0.0279  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.3916 0.3336 0.6430 0.0002  -0.0542 0.0161  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.3969 0.3358 0.6238 0.0013  -0.0641 0.0102  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.3943 0.3410 0.6102 -0.0031 -0.0107 0.0329  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.3965 0.3449 0.5819 -0.0030 -0.0111 0.0361  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.3889 0.3335 0.6115 -0.0036 0.0164  0.0421  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.3692 0.3089 0.6306 0.0014  -0.0651 0.0129  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.3808 0.3128 0.6197 0.0049  -0.0890 0.0009  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.3711 0.3033 0.5863 0.0056  -0.0860 0.0018  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.3666 0.3047 0.5931 0.0036  -0.0698 0.0118  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3941 0.3181 0.6768 0.0073  -0.1133 -0.0092 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.4025 0.3251 0.7079 0.0080  -0.1226 -0.0117 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3843 0.3114 0.7211 0.0051  -0.1073 -0.0049 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.3650 0.2886 0.5484 0.0095  -0.1011 -0.0082 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.3614 0.2835 0.5309 0.0114  -0.0999 -0.0094 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3706 0.2889 0.5881 0.0117  -0.1074 -0.0121 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3735 0.2833 0.6173 0.0132  -0.1261 -0.0218 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3759 0.2851 0.5051 0.0169  -0.1131 -0.0210 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3926 0.3034 0.4777 0.0170  -0.1051 -0.0185 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.4007 0.3044 0.4712 0.0185  -0.1129 -0.0219 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3777 0.2973 0.4453 0.0155  -0.0904 -0.0121 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.3656 0.2890 0.5962 0.0105  -0.0950 -0.0038 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.3714 0.2909 0.6513 0.0103  -0.0990 -0.0045 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.4047 0.3091 0.6860 0.0148  -0.1237 -0.0228 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.4099 0.3079 0.7349 0.0144  -0.1386 -0.0303 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3629 0.2882 0.6473 0.0096  -0.0812 0.0088  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3829 0.3051 0.7256 0.0084  -0.0783 0.0136  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.4232 0.3480 0.7602 0.0096  -0.0634 0.0266  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.4565 0.3771 0.8469 0.0087  -0.0567 0.0345  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.4982 0.4101 0.9166 0.0105  -0.0685 0.0254  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.4793 0.3839 0.8741 0.0139  -0.0880 0.0066  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.5054 0.4136 0.9748 0.0093  -0.0595 0.0350  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.4307 0.3275 0.6631 0.0194  -0.1286 -0.0310 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4571 0.3342 0.6772 0.0255  -0.1503 -0.0497 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.4942 0.3583 0.7108 0.0281  -0.1751 -0.0626 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5067 0.3511 0.7183 0.0335  -0.1978 -0.0793 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.4770 0.3476 0.6451 0.0309  -0.1437 -0.0537 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.5063 0.3749 0.6224 0.0331  -0.1404 -0.0537 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.5093 0.3953 0.6129 0.0288  -0.1214 -0.0396 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5338 0.3830 0.6081 0.0396  -0.1537 -0.0658 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.5322 0.4105 0.5932 0.0319  -0.1225 -0.0431 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5538 0.4094 0.5934 0.0388  -0.1404 -0.0577 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.5059 0.3791 0.7269 0.0249  -0.1723 -0.0552 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.5319 0.3946 0.7554 0.0275  -0.1962 -0.0647 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.5248 0.3975 0.8182 0.0224  -0.1999 -0.0602 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.5342 0.4017 0.8382 0.0241  -0.2186 -0.0656 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.5488 0.4107 0.7199 0.0295  -0.1912 -0.0608 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5870 0.4360 0.6914 0.0356  -0.1874 -0.0654 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5983 0.4468 0.6609 0.0367  -0.1805 -0.0594 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.6149 0.4364 0.6959 0.0443  -0.2128 -0.0837 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.5143 0.4008 0.8553 0.0167  -0.1803 -0.0487 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.5082 0.4036 0.9191 0.0121  -0.1774 -0.0424 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.5294 0.4130 0.9910 0.0138  -0.2105 -0.0582 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.5358 0.4052 0.9879 0.0172  -0.2290 -0.0718 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.4926 0.3999 0.9375 0.0072  -0.1480 -0.0261 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.5418 0.4303 1.0568 0.0119  -0.2192 -0.0576 24  THR   A N   
135  C CA  . THR   A 18  ? 0.5588 0.4378 1.1337 0.0131  -0.2539 -0.0724 24  THR   A CA  
136  C C   . THR   A 18  ? 0.5472 0.4361 1.2175 0.0067  -0.2415 -0.0651 24  THR   A C   
137  O O   . THR   A 18  ? 0.5332 0.4343 1.2147 0.0024  -0.2044 -0.0472 24  THR   A O   
138  C CB  . THR   A 18  ? 0.5919 0.4677 1.1691 0.0165  -0.2774 -0.0780 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5951 0.4888 1.2226 0.0118  -0.2540 -0.0628 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.6360 0.4999 1.1219 0.0230  -0.2862 -0.0825 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5484 0.4301 1.2877 0.0066  -0.2735 -0.0791 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5377 0.4271 1.3783 0.0005  -0.2651 -0.0736 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.5165 0.4251 1.4010 -0.0041 -0.2265 -0.0513 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4988 0.4153 1.4150 -0.0084 -0.1903 -0.0343 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.5599 0.4382 1.4635 0.0020  -0.3135 -0.0949 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.5682 0.4562 1.5938 -0.0044 -0.3101 -0.0903 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.5791 0.4608 1.6631 -0.0079 -0.3165 -0.0967 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.5621 0.4637 1.6641 -0.0073 -0.3033 -0.0817 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5544 0.4470 1.7496 -0.0133 -0.3116 -0.0904 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5448 0.4498 1.7554 -0.0129 -0.3030 -0.0813 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.5264 0.4396 1.4062 -0.0021 -0.2330 -0.0511 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.5185 0.4465 1.4354 -0.0048 -0.1996 -0.0334 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.5205 0.4550 1.3841 -0.0065 -0.1520 -0.0138 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.5129 0.4551 1.4222 -0.0098 -0.1154 0.0032  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.5717 0.5001 1.4712 -0.0008 -0.2187 -0.0389 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.6469 0.5651 1.5831 0.0029  -0.2724 -0.0592 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.6396 0.5639 1.6558 0.0024  -0.2843 -0.0600 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.6965 0.5972 1.5746 0.0074  -0.3066 -0.0763 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.5262 0.4555 1.2945 -0.0037 -0.1529 -0.0163 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.5133 0.4469 1.2245 -0.0046 -0.1156 -0.0004 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.4804 0.4145 1.2227 -0.0075 -0.0908 0.0122  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.4638 0.4026 1.2089 -0.0088 -0.0534 0.0307  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.5323 0.4603 1.1478 -0.0011 -0.1267 -0.0076 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.5334 0.4595 1.1052 0.0020  -0.1420 -0.0148 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.5130 0.4459 1.1012 0.0010  -0.1278 -0.0074 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.5599 0.4759 1.0802 0.0060  -0.1663 -0.0273 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.4814 0.4080 1.2394 -0.0074 -0.1103 0.0026  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.4827 0.4078 1.2723 -0.0097 -0.0888 0.0147  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.4710 0.4004 1.3559 -0.0136 -0.0663 0.0280  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.4632 0.3925 1.3578 -0.0146 -0.0303 0.0480  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.4772 0.3916 1.2724 -0.0086 -0.1177 -0.0015 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.4985 0.4076 1.2056 -0.0045 -0.1249 -0.0077 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.5238 0.4241 1.1809 -0.0003 -0.1559 -0.0274 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.5124 0.4230 1.1754 -0.0036 -0.1002 0.0063  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.5510 0.4487 1.1393 0.0028  -0.1488 -0.0263 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.5439 0.4491 1.1371 0.0006  -0.1167 -0.0062 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.5133 0.4279 1.1878 -0.0051 -0.0654 0.0291  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.5611 0.4675 1.1047 0.0027  -0.1012 0.0026  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.5412 0.4551 1.1606 -0.0024 -0.0533 0.0377  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.5595 0.4712 1.1171 0.0011  -0.0714 0.0244  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.4644 0.3961 1.4186 -0.0151 -0.0866 0.0177  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.4542 0.3911 1.5098 -0.0188 -0.0650 0.0296  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.4704 0.4135 1.5106 -0.0181 -0.0190 0.0510  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.4673 0.4111 1.5657 -0.0198 0.0177  0.0693  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.4353 0.3744 1.5651 -0.0198 -0.1027 0.0118  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.4755 0.4210 1.4396 -0.0151 -0.0206 0.0482  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.4702 0.4188 1.4112 -0.0137 0.0186  0.0642  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.4667 0.4110 1.3026 -0.0112 0.0369  0.0728  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.4829 0.4282 1.2646 -0.0092 0.0490  0.0753  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.5045 0.4588 1.4500 -0.0123 0.0009  0.0534  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.5372 0.4970 1.5929 -0.0140 -0.0092 0.0494  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.5407 0.5032 1.6615 -0.0151 0.0265  0.0642  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.5443 0.5045 1.6228 -0.0136 -0.0581 0.0294  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.4342 0.3733 1.2478 -0.0112 0.0384  0.0773  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.4430 0.3784 1.1667 -0.0087 0.0490  0.0844  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.4414 0.3718 1.1332 -0.0063 0.0929  0.1057  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.4260 0.3511 1.1667 -0.0062 0.1239  0.1220  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.4292 0.3599 1.1530 -0.0088 0.0381  0.0839  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.4584 0.3853 1.1035 -0.0058 0.0483  0.0931  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.4865 0.4177 1.0571 -0.0044 0.0252  0.0786  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.4498 0.3713 1.1154 -0.0056 0.0420  0.0951  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.4353 0.3653 1.0449 -0.0041 0.0958  0.1052  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.4468 0.3680 1.0084 -0.0007 0.1320  0.1225  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.4640 0.3798 0.9625 0.0018  0.1306  0.1298  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.4729 0.3776 0.9637 0.0049  0.1568  0.1486  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.4655 0.3879 0.9822 0.0004  0.1359  0.1163  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.4998 0.4096 0.9488 0.0047  0.1670  0.1306  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.4500 0.3765 1.0335 -0.0009 0.1422  0.1125  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.4575 0.3801 0.9124 0.0010  0.0999  0.1156  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.4664 0.3864 0.8665 0.0034  0.0948  0.1203  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.4475 0.3759 0.8357 0.0019  0.0596  0.1020  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.4496 0.3837 0.8381 0.0000  0.0414  0.0865  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.4895 0.4043 0.8158 0.0063  0.1090  0.1269  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.5108 0.4251 0.7785 0.0088  0.0982  0.1292  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.5363 0.4408 0.7813 0.0131  0.1102  0.1461  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.5160 0.4394 0.7434 0.0075  0.0735  0.1151  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.5528 0.4613 0.7482 0.0145  0.0922  0.1424  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.5401 0.4607 0.7267 0.0108  0.0709  0.1234  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.5164 0.4487 0.7388 0.0043  0.0546  0.0975  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.5484 0.4769 0.6974 0.0103  0.0507  0.1139  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.5276 0.4658 0.7074 0.0041  0.0374  0.0892  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.5433 0.4807 0.6911 0.0067  0.0357  0.0969  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.4302 0.3573 0.8088 0.0035  0.0514  0.1043  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.4268 0.3590 0.7882 0.0034  0.0231  0.0881  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.4325 0.3635 0.7577 0.0066  0.0237  0.0962  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.4349 0.3594 0.7693 0.0089  0.0400  0.1131  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.4301 0.3610 0.8469 0.0019  0.0030  0.0740  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.4673 0.3921 0.9415 0.0017  0.0120  0.0835  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.5078 0.4286 0.9742 0.0044  0.0075  0.0864  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4934 0.4080 0.9982 0.0048  0.0220  0.1001  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.5135 0.4368 0.9380 0.0064  -0.0082 0.0762  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.4202 0.3567 0.7052 0.0074  0.0074  0.0856  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.4155 0.3529 0.6730 0.0106  0.0049  0.0916  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.4066 0.3473 0.6604 0.0112  -0.0160 0.0741  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.4058 0.3510 0.6313 0.0103  -0.0251 0.0629  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.4514 0.3908 0.6559 0.0118  0.0130  0.1009  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.5284 0.4683 0.7082 0.0159  0.0103  0.1104  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.5380 0.4807 0.7324 0.0174  -0.0011 0.1050  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.5791 0.5152 0.7236 0.0181  0.0186  0.1228  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.3850 0.3212 0.6673 0.0134  -0.0219 0.0720  36  SER   A N   
241  C CA  A SER   A 30  ? 0.3832 0.3180 0.6610 0.0156  -0.0388 0.0552  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.3880 0.3228 0.6656 0.0156  -0.0389 0.0551  36  SER   A CA  
243  C C   . SER   A 30  ? 0.3900 0.3321 0.6244 0.0178  -0.0400 0.0556  36  SER   A C   
244  O O   . SER   A 30  ? 0.3924 0.3350 0.6056 0.0186  -0.0493 0.0416  36  SER   A O   
245  C CB  A SER   A 30  ? 0.3823 0.3092 0.6985 0.0181  -0.0415 0.0549  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.4010 0.3279 0.7167 0.0181  -0.0417 0.0547  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3966 0.3190 0.7035 0.0215  -0.0553 0.0383  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4343 0.3629 0.7475 0.0207  -0.0301 0.0728  36  SER   A OG  
249  N N   . SER   A 31  ? 0.3768 0.3233 0.5986 0.0192  -0.0307 0.0721  37  SER   A N   
250  C CA  . SER   A 31  ? 0.3881 0.3428 0.5781 0.0211  -0.0339 0.0731  37  SER   A CA  
251  C C   . SER   A 31  ? 0.3702 0.3312 0.5267 0.0177  -0.0356 0.0667  37  SER   A C   
252  O O   . SER   A 31  ? 0.3830 0.3508 0.5207 0.0184  -0.0398 0.0635  37  SER   A O   
253  C CB  . SER   A 31  ? 0.4346 0.3906 0.6187 0.0242  -0.0283 0.0919  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.5064 0.4612 0.6665 0.0225  -0.0200 0.1030  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.3617 0.3205 0.5154 0.0142  -0.0313 0.0659  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.3647 0.3276 0.4907 0.0110  -0.0327 0.0592  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.3507 0.3097 0.4817 0.0100  -0.0408 0.0438  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.3328 0.2937 0.4427 0.0077  -0.0420 0.0385  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.3825 0.3435 0.4983 0.0087  -0.0215 0.0685  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.4049 0.3657 0.4986 0.0107  -0.0157 0.0826  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.4166 0.3700 0.4972 0.0099  -0.0014 0.0908  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.3948 0.3508 0.4496 0.0066  -0.0029 0.0821  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.4317 0.3819 0.4541 0.0067  0.0047  0.0869  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.4382 0.3780 0.4446 0.0108  0.0152  0.1014  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.4230 0.3750 0.4261 0.0035  0.0023  0.0774  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.3400 0.2916 0.4987 0.0118  -0.0475 0.0367  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.3346 0.2784 0.4977 0.0121  -0.0593 0.0222  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.3419 0.2866 0.5121 0.0085  -0.0566 0.0238  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.3415 0.2827 0.4994 0.0086  -0.0654 0.0144  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.3588 0.2994 0.4885 0.0148  -0.0665 0.0107  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3762 0.3034 0.5025 0.0173  -0.0813 -0.0042 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3473 0.2660 0.5027 0.0186  -0.0915 -0.0103 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.4019 0.3257 0.4978 0.0182  -0.0837 -0.0092 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.3329 0.2805 0.5219 0.0063  -0.0430 0.0365  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.3334 0.2811 0.5341 0.0036  -0.0366 0.0385  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.3375 0.2814 0.5912 0.0029  -0.0323 0.0424  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.3421 0.2842 0.6170 0.0037  -0.0247 0.0511  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.3435 0.2949 0.5162 0.0022  -0.0194 0.0499  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.3742 0.3300 0.5021 0.0013  -0.0233 0.0453  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3820 0.3383 0.4837 0.0002  -0.0091 0.0546  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.3805 0.3347 0.5055 0.0005  -0.0339 0.0332  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.3293 0.2723 0.6069 0.0014  -0.0350 0.0378  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.3462 0.2873 0.6825 0.0001  -0.0284 0.0422  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.3656 0.3087 0.7088 -0.0013 -0.0188 0.0440  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.3764 0.3202 0.6973 -0.0011 -0.0314 0.0344  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.3437 0.2796 0.7221 0.0008  -0.0524 0.0288  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.3469 0.2814 0.8013 -0.0012 -0.0493 0.0318  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.3518 0.2795 0.8412 -0.0005 -0.0690 0.0218  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3553 0.2912 0.8383 -0.0020 -0.0595 0.0245  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.3665 0.3089 0.7399 -0.0021 0.0059  0.0572  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.3807 0.3236 0.7683 -0.0028 0.0200  0.0597  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.3938 0.3363 0.8609 -0.0037 0.0251  0.0626  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.3797 0.3192 0.8786 -0.0039 0.0389  0.0730  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.4034 0.3426 0.7488 -0.0017 0.0497  0.0729  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.4076 0.3448 0.7738 -0.0016 0.0685  0.0753  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.4219 0.3624 0.6958 -0.0014 0.0412  0.0685  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.4022 0.3473 0.9060 -0.0042 0.0129  0.0538  43  SER   A N   
298  C CA  . SER   A 37  ? 0.3971 0.3434 0.9873 -0.0054 0.0164  0.0558  43  SER   A CA  
299  C C   . SER   A 37  ? 0.4137 0.3617 1.0273 -0.0048 0.0362  0.0604  43  SER   A C   
300  O O   . SER   A 37  ? 0.4182 0.3662 0.9832 -0.0037 0.0366  0.0569  43  SER   A O   
301  C CB  . SER   A 37  ? 0.3833 0.3299 1.0131 -0.0057 -0.0234 0.0392  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.4062 0.3527 1.0057 -0.0038 -0.0482 0.0265  43  SER   A OG  
303  N N   . SER   A 38  ? 0.4097 0.3586 1.1020 -0.0055 0.0551  0.0685  44  SER   A N   
304  C CA  . SER   A 38  ? 0.4231 0.3730 1.1485 -0.0044 0.0779  0.0734  44  SER   A CA  
305  C C   . SER   A 38  ? 0.4282 0.3843 1.1948 -0.0041 0.0454  0.0588  44  SER   A C   
306  O O   . SER   A 38  ? 0.4272 0.3854 1.2227 -0.0050 0.0083  0.0470  44  SER   A O   
307  C CB  . SER   A 38  ? 0.4303 0.3781 1.2305 -0.0047 0.1130  0.0887  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.4470 0.3992 1.3254 -0.0075 0.0916  0.0842  44  SER   A OG  
309  N N   . THR   A 39  ? 0.4396 0.3963 1.2051 -0.0022 0.0577  0.0593  45  THR   A N   
310  C CA  . THR   A 39  ? 0.4484 0.4097 1.2522 -0.0008 0.0277  0.0476  45  THR   A CA  
311  C C   . THR   A 39  ? 0.4613 0.4261 1.3433 0.0005  0.0530  0.0545  45  THR   A C   
312  O O   . THR   A 39  ? 0.4766 0.4370 1.3511 0.0015  0.0981  0.0671  45  THR   A O   
313  C CB  . THR   A 39  ? 0.4791 0.4375 1.2027 0.0011  0.0115  0.0393  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.4900 0.4452 1.1840 0.0024  0.0464  0.0465  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.5049 0.4596 1.1485 0.0003  -0.0059 0.0341  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.4536 0.4241 1.4042 0.0017  0.0244  0.0459  46  THR   A N   
317  C CA  . THR   A 40  ? 0.4449 0.4199 1.4778 0.0035  0.0476  0.0521  46  THR   A CA  
318  C C   . THR   A 40  ? 0.4527 0.4242 1.4412 0.0070  0.0619  0.0519  46  THR   A C   
319  O O   . THR   A 40  ? 0.4604 0.4293 1.4687 0.0089  0.1053  0.0615  46  THR   A O   
320  C CB  . THR   A 40  ? 0.4477 0.4309 1.5881 0.0035  0.0117  0.0443  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4914 0.4732 1.6049 0.0064  -0.0375 0.0300  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4417 0.4265 1.6280 -0.0004 -0.0023 0.0430  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.4548 0.4239 1.3833 0.0085  0.0278  0.0412  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.4531 0.4179 1.3402 0.0115  0.0381  0.0401  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4700 0.4265 1.2518 0.0103  0.0595  0.0423  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4856 0.4407 1.2146 0.0077  0.0496  0.0412  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.4552 0.4199 1.3406 0.0145  -0.0091 0.0292  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4551 0.4055 1.2091 0.0124  0.0873  0.0444  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4719 0.4133 1.1296 0.0113  0.1046  0.0446  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4492 0.3893 1.0410 0.0104  0.0711  0.0353  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4349 0.3761 1.0448 0.0125  0.0459  0.0296  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.5134 0.4454 1.1618 0.0142  0.1458  0.0481  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5944 0.5181 1.2378 0.0152  0.1904  0.0591  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6986 0.6065 1.2849 0.0182  0.2244  0.0587  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.7124 0.6120 1.3323 0.0225  0.2618  0.0637  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7415 0.6436 1.2421 0.0164  0.2120  0.0519  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4425 0.3794 0.9606 0.0077  0.0717  0.0350  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4415 0.3765 0.8947 0.0065  0.0471  0.0279  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4301 0.3571 0.8312 0.0063  0.0650  0.0259  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4424 0.3632 0.8430 0.0072  0.0978  0.0295  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4122 0.3370 0.7693 0.0054  0.0445  0.0199  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4170 0.3338 0.7320 0.0047  0.0565  0.0163  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4200 0.3347 0.6651 0.0010  0.0527  0.0134  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4377 0.3456 0.6504 -0.0003 0.0582  0.0090  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4333 0.3476 0.7698 0.0075  0.0393  0.0129  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4791 0.3964 0.9065 0.0124  0.0428  0.0158  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4048 0.3251 0.6319 -0.0008 0.0413  0.0153  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4205 0.3405 0.5900 -0.0041 0.0362  0.0130  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4411 0.3558 0.5798 -0.0053 0.0608  0.0147  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4432 0.3555 0.6010 -0.0032 0.0802  0.0204  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4181 0.3450 0.5821 -0.0045 0.0164  0.0142  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4566 0.3829 0.6326 -0.0021 -0.0100 0.0109  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4727 0.3936 0.6406 -0.0012 -0.0155 0.0083  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4530 0.3819 0.6443 -0.0005 -0.0254 0.0108  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4483 0.3589 0.5405 -0.0080 0.0603  0.0099  52  THR   A N   
356  C CA  . THR   A 46  ? 0.4760 0.3786 0.5287 -0.0084 0.0769  0.0099  52  THR   A CA  
357  C C   . THR   A 46  ? 0.4718 0.3810 0.4936 -0.0108 0.0628  0.0116  52  THR   A C   
358  O O   . THR   A 46  ? 0.4735 0.3886 0.4871 -0.0136 0.0453  0.0078  52  THR   A O   
359  C CB  . THR   A 46  ? 0.5278 0.4196 0.5539 -0.0099 0.0826  0.0009  52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5467 0.4299 0.5988 -0.0064 0.1026  0.0003  52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5602 0.4426 0.5333 -0.0109 0.0881  -0.0028 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4691 0.3762 0.4761 -0.0091 0.0716  0.0183  53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4658 0.3787 0.4464 -0.0106 0.0583  0.0203  53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.4865 0.3915 0.4201 -0.0124 0.0565  0.0138  53  ILE   A C   
365  O O   . ILE   A 47  ? 0.5032 0.3933 0.4125 -0.0101 0.0722  0.0120  53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4768 0.3897 0.4621 -0.0075 0.0660  0.0313  53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4580 0.3773 0.4971 -0.0061 0.0674  0.0364  53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4861 0.4060 0.4488 -0.0087 0.0498  0.0333  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4450 0.3752 0.5076 -0.0081 0.0441  0.0307  53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4712 0.3847 0.3934 -0.0161 0.0377  0.0098  54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.4743 0.3826 0.3608 -0.0185 0.0307  0.0029  54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.4825 0.3835 0.3368 -0.0150 0.0327  0.0085  54  ALA   A C   
373  O O   . ALA   A 48  ? 0.4756 0.3832 0.3393 -0.0128 0.0311  0.0181  54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4526 0.3737 0.3465 -0.0230 0.0119  -0.0003 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.5055 0.3911 0.3200 -0.0141 0.0344  0.0022  55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.5449 0.4190 0.3183 -0.0095 0.0327  0.0071  55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5621 0.4346 0.3106 -0.0130 0.0108  -0.0041 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5871 0.4427 0.3052 -0.0128 0.0122  -0.0148 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5802 0.4303 0.3224 -0.0029 0.0574  0.0099  55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.6151 0.4665 0.3919 0.0003  0.0817  0.0209  55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.6404 0.5056 0.4447 0.0013  0.0780  0.0345  55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.6614 0.5284 0.5085 0.0032  0.0987  0.0426  55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.6555 0.5347 0.5408 0.0031  0.0967  0.0520  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.6413 0.5312 0.5245 0.0019  0.0776  0.0551  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.6474 0.5277 0.5770 0.0044  0.1136  0.0578  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.5533 0.4436 0.3208 -0.0166 -0.0091 -0.0028 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.5434 0.4380 0.3077 -0.0216 -0.0311 -0.0134 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.5306 0.4430 0.3143 -0.0225 -0.0490 -0.0070 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.5110 0.4314 0.3085 -0.0193 -0.0439 0.0047  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.5255 0.4270 0.3203 -0.0280 -0.0286 -0.0221 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.5007 0.4241 0.3447 -0.0300 -0.0256 -0.0133 56  CYS   A SG  
392  N N   A ASP   A 51  ? 0.5247 0.4444 0.3172 -0.0272 -0.0695 -0.0151 57  ASP   A N   
393  N N   B ASP   A 51  ? 0.5363 0.4553 0.3279 -0.0274 -0.0692 -0.0157 57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.5088 0.4469 0.3294 -0.0282 -0.0843 -0.0096 57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.5336 0.4697 0.3506 -0.0289 -0.0871 -0.0123 57  ASP   A CA  
396  C C   A ASP   A 51  ? 0.4944 0.4484 0.3582 -0.0353 -0.0864 -0.0148 57  ASP   A C   
397  C C   B ASP   A 51  ? 0.5082 0.4598 0.3687 -0.0363 -0.0888 -0.0179 57  ASP   A C   
398  O O   A ASP   A 51  ? 0.4841 0.4519 0.3739 -0.0372 -0.0994 -0.0136 57  ASP   A O   
399  O O   B ASP   A 51  ? 0.5007 0.4633 0.3838 -0.0395 -0.1048 -0.0204 57  ASP   A O   
400  C CB  A ASP   A 51  ? 0.5335 0.4672 0.3329 -0.0259 -0.1083 -0.0110 57  ASP   A CB  
401  C CB  B ASP   A 51  ? 0.5851 0.5124 0.3752 -0.0278 -0.1110 -0.0182 57  ASP   A CB  
402  C CG  A ASP   A 51  ? 0.5824 0.5083 0.3721 -0.0305 -0.1265 -0.0267 57  ASP   A CG  
403  C CG  B ASP   A 51  ? 0.6753 0.6130 0.4748 -0.0241 -0.1276 -0.0089 57  ASP   A CG  
404  O OD1 A ASP   A 51  ? 0.5871 0.5060 0.3763 -0.0348 -0.1171 -0.0366 57  ASP   A OD1 
405  O OD1 B ASP   A 51  ? 0.6926 0.6339 0.4944 -0.0192 -0.1169 0.0044  57  ASP   A OD1 
406  O OD2 A ASP   A 51  ? 0.6145 0.5405 0.3989 -0.0296 -0.1518 -0.0293 57  ASP   A OD2 
407  O OD2 B ASP   A 51  ? 0.7186 0.6597 0.5245 -0.0259 -0.1526 -0.0150 57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.4906 0.4416 0.3637 -0.0385 -0.0722 -0.0193 58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.4669 0.4279 0.3752 -0.0441 -0.0700 -0.0223 58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.4407 0.4177 0.3772 -0.0429 -0.0703 -0.0137 58  CYS   A C   
411  O O   . CYS   A 52  ? 0.4364 0.4157 0.3689 -0.0377 -0.0658 -0.0053 58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.4708 0.4249 0.3816 -0.0446 -0.0532 -0.0230 58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.4968 0.4322 0.3865 -0.0471 -0.0494 -0.0353 58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.4088 0.3953 0.3755 -0.0473 -0.0744 -0.0160 59  GLN   A N   
415  C CA  . GLN   A 53  ? 0.3965 0.3957 0.3906 -0.0456 -0.0700 -0.0086 59  GLN   A CA  
416  C C   . GLN   A 53  ? 0.3840 0.3824 0.3972 -0.0483 -0.0560 -0.0086 59  GLN   A C   
417  O O   . GLN   A 53  ? 0.3650 0.3716 0.4035 -0.0479 -0.0509 -0.0045 59  GLN   A O   
418  C CB  . GLN   A 53  ? 0.4230 0.4347 0.4419 -0.0470 -0.0855 -0.0087 59  GLN   A CB  
419  C CG  . GLN   A 53  ? 0.4825 0.4960 0.4865 -0.0417 -0.0980 -0.0038 59  GLN   A CG  
420  C CD  . GLN   A 53  ? 0.5163 0.5437 0.5545 -0.0426 -0.1139 -0.0031 59  GLN   A CD  
421  O OE1 . GLN   A 53  ? 0.5235 0.5498 0.5577 -0.0439 -0.1354 -0.0081 59  GLN   A OE1 
422  N NE2 . GLN   A 53  ? 0.4885 0.5278 0.5613 -0.0412 -0.1042 0.0026  59  GLN   A NE2 
423  N N   . THR   A 54  ? 0.3710 0.3579 0.3729 -0.0506 -0.0490 -0.0129 60  THR   A N   
424  C CA  . THR   A 54  ? 0.3632 0.3450 0.3761 -0.0515 -0.0353 -0.0106 60  THR   A CA  
425  C C   . THR   A 54  ? 0.3608 0.3303 0.3504 -0.0481 -0.0284 -0.0100 60  THR   A C   
426  O O   . THR   A 54  ? 0.3630 0.3272 0.3354 -0.0478 -0.0320 -0.0141 60  THR   A O   
427  C CB  . THR   A 54  ? 0.3821 0.3628 0.4184 -0.0589 -0.0352 -0.0160 60  THR   A CB  
428  O OG1 . THR   A 54  ? 0.4195 0.3907 0.4407 -0.0621 -0.0414 -0.0251 60  THR   A OG1 
429  C CG2 . THR   A 54  ? 0.3775 0.3717 0.4464 -0.0630 -0.0452 -0.0178 60  THR   A CG2 
430  N N   . GLY   A 55  ? 0.3501 0.3142 0.3385 -0.0441 -0.0187 -0.0042 61  GLY   A N   
431  C CA  . GLY   A 55  ? 0.3437 0.2970 0.3164 -0.0399 -0.0153 -0.0030 61  GLY   A CA  
432  C C   . GLY   A 55  ? 0.3612 0.3058 0.3311 -0.0352 -0.0079 0.0030  61  GLY   A C   
433  O O   . GLY   A 55  ? 0.3778 0.3220 0.3559 -0.0360 -0.0011 0.0062  61  GLY   A O   
434  N N   . VAL   A 56  ? 0.3535 0.2892 0.3120 -0.0300 -0.0091 0.0048  62  VAL   A N   
435  C CA  . VAL   A 56  ? 0.3628 0.2852 0.3098 -0.0237 -0.0059 0.0101  62  VAL   A CA  
436  C C   . VAL   A 56  ? 0.3722 0.2927 0.3106 -0.0171 -0.0140 0.0103  62  VAL   A C   
437  O O   . VAL   A 56  ? 0.3671 0.2913 0.3120 -0.0174 -0.0197 0.0076  62  VAL   A O   
438  C CB  . VAL   A 56  ? 0.3909 0.3002 0.3365 -0.0236 -0.0035 0.0112  62  VAL   A CB  
439  C CG1 . VAL   A 56  ? 0.4084 0.3004 0.3353 -0.0152 -0.0038 0.0176  62  VAL   A CG1 
440  C CG2 . VAL   A 56  ? 0.3905 0.3001 0.3490 -0.0306 0.0046  0.0103  62  VAL   A CG2 
441  N N   . TYR   A 57  ? 0.3838 0.2967 0.3083 -0.0107 -0.0138 0.0129  63  TYR   A N   
442  C CA  . TYR   A 57  ? 0.3773 0.2857 0.2949 -0.0043 -0.0244 0.0111  63  TYR   A CA  
443  C C   . TYR   A 57  ? 0.4019 0.2890 0.2961 0.0042  -0.0295 0.0129  63  TYR   A C   
444  O O   . TYR   A 57  ? 0.4343 0.3093 0.3110 0.0066  -0.0205 0.0174  63  TYR   A O   
445  C CB  . TYR   A 57  ? 0.3786 0.2957 0.2989 -0.0030 -0.0245 0.0097  63  TYR   A CB  
446  C CG  . TYR   A 57  ? 0.4151 0.3220 0.3176 0.0026  -0.0170 0.0114  63  TYR   A CG  
447  C CD1 . TYR   A 57  ? 0.4315 0.3413 0.3379 -0.0002 -0.0026 0.0152  63  TYR   A CD1 
448  C CD2 . TYR   A 57  ? 0.4358 0.3278 0.3182 0.0113  -0.0236 0.0088  63  TYR   A CD2 
449  C CE1 . TYR   A 57  ? 0.4505 0.3500 0.3427 0.0057  0.0091  0.0176  63  TYR   A CE1 
450  C CE2 . TYR   A 57  ? 0.4699 0.3489 0.3304 0.0178  -0.0137 0.0097  63  TYR   A CE2 
451  C CZ  . TYR   A 57  ? 0.4771 0.3594 0.3420 0.0153  0.0048  0.0150  63  TYR   A CZ  
452  O OH  . TYR   A 57  ? 0.5167 0.3851 0.3623 0.0224  0.0193  0.0168  63  TYR   A OH  
453  N N   . TYR   A 58  ? 0.4039 0.2850 0.2979 0.0092  -0.0443 0.0096  64  TYR   A N   
454  C CA  . TYR   A 58  ? 0.4289 0.2873 0.2975 0.0185  -0.0551 0.0100  64  TYR   A CA  
455  C C   . TYR   A 58  ? 0.4588 0.3071 0.3044 0.0254  -0.0581 0.0065  64  TYR   A C   
456  O O   . TYR   A 58  ? 0.4435 0.3009 0.3044 0.0248  -0.0649 0.0011  64  TYR   A O   
457  C CB  . TYR   A 58  ? 0.4268 0.2825 0.3127 0.0206  -0.0729 0.0072  64  TYR   A CB  
458  C CG  . TYR   A 58  ? 0.4668 0.2969 0.3239 0.0313  -0.0891 0.0071  64  TYR   A CG  
459  C CD1 . TYR   A 58  ? 0.5073 0.3189 0.3347 0.0358  -0.0840 0.0141  64  TYR   A CD1 
460  C CD2 . TYR   A 58  ? 0.4927 0.3143 0.3490 0.0376  -0.1100 0.0001  64  TYR   A CD2 
461  C CE1 . TYR   A 58  ? 0.5451 0.3287 0.3369 0.0474  -0.1001 0.0150  64  TYR   A CE1 
462  C CE2 . TYR   A 58  ? 0.5360 0.3307 0.3602 0.0485  -0.1291 -0.0013 64  TYR   A CE2 
463  C CZ  . TYR   A 58  ? 0.5773 0.3520 0.3654 0.0540  -0.1242 0.0066  64  TYR   A CZ  
464  O OH  . TYR   A 58  ? 0.6377 0.3817 0.3857 0.0664  -0.1442 0.0061  64  TYR   A OH  
465  N N   . CYS   A 59  ? 0.4891 0.3148 0.2957 0.0333  -0.0531 0.0095  65  CYS   A N   
466  C CA  . CYS   A 59  ? 0.5245 0.3340 0.3001 0.0419  -0.0533 0.0055  65  CYS   A CA  
467  C C   . CYS   A 59  ? 0.5694 0.3488 0.3075 0.0535  -0.0728 0.0026  65  CYS   A C   
468  O O   . CYS   A 59  ? 0.6088 0.3656 0.3107 0.0600  -0.0675 0.0093  65  CYS   A O   
469  C CB  . CYS   A 59  ? 0.5638 0.3684 0.3217 0.0429  -0.0276 0.0116  65  CYS   A CB  
470  S SG  . CYS   A 59  ? 0.6205 0.3977 0.3311 0.0561  -0.0214 0.0071  65  CYS   A SG  
471  N N   . SER   A 60  ? 0.5656 0.3425 0.3121 0.0566  -0.0964 -0.0069 66  SER   A N   
472  C CA  . SER   A 60  ? 0.6136 0.3618 0.3285 0.0677  -0.1217 -0.0116 66  SER   A CA  
473  C C   . SER   A 60  ? 0.6581 0.3713 0.3068 0.0807  -0.1176 -0.0126 66  SER   A C   
474  O O   . SER   A 60  ? 0.6974 0.3814 0.3049 0.0907  -0.1309 -0.0103 66  SER   A O   
475  C CB  . SER   A 60  ? 0.6488 0.4028 0.3949 0.0675  -0.1483 -0.0230 66  SER   A CB  
476  O OG  . SER   A 60  ? 0.7171 0.4682 0.4557 0.0699  -0.1475 -0.0320 66  SER   A OG  
477  N N   . SER   A 61  ? 0.6547 0.3683 0.2909 0.0815  -0.0978 -0.0150 67  SER   A N   
478  C CA  . SER   A 61  ? 0.6947 0.3727 0.2656 0.0947  -0.0875 -0.0162 67  SER   A CA  
479  C C   . SER   A 61  ? 0.7403 0.3999 0.2736 0.0992  -0.0637 -0.0016 67  SER   A C   
480  O O   . SER   A 61  ? 0.8029 0.4260 0.2732 0.1124  -0.0547 -0.0004 67  SER   A O   
481  C CB  . SER   A 61  ? 0.6905 0.3754 0.2667 0.0944  -0.0699 -0.0223 67  SER   A CB  
482  O OG  . SER   A 61  ? 0.6761 0.3907 0.2917 0.0837  -0.0422 -0.0135 67  SER   A OG  
483  N N   . ARG   A 62  ? 0.7184 0.4003 0.2883 0.0889  -0.0531 0.0091  68  ARG   A N   
484  C CA  . ARG   A 62  ? 0.7338 0.4013 0.2807 0.0911  -0.0315 0.0239  68  ARG   A CA  
485  C C   . ARG   A 62  ? 0.7292 0.3975 0.2891 0.0887  -0.0478 0.0301  68  ARG   A C   
486  O O   . ARG   A 62  ? 0.7465 0.4016 0.2902 0.0905  -0.0321 0.0431  68  ARG   A O   
487  C CB  . ARG   A 62  ? 0.7304 0.4245 0.3168 0.0800  0.0009  0.0310  68  ARG   A CB  
488  C CG  . ARG   A 62  ? 0.7568 0.4483 0.3333 0.0833  0.0231  0.0282  68  ARG   A CG  
489  C CD  . ARG   A 62  ? 0.8086 0.4607 0.3240 0.0968  0.0467  0.0368  68  ARG   A CD  
490  N NE  . ARG   A 62  ? 0.8527 0.5029 0.3645 0.1002  0.0725  0.0345  68  ARG   A NE  
491  C CZ  . ARG   A 62  ? 0.9047 0.5372 0.3836 0.1099  0.0657  0.0227  68  ARG   A CZ  
492  N NH1 . ARG   A 62  ? 0.9299 0.5451 0.3772 0.1168  0.0318  0.0116  68  ARG   A NH1 
493  N NH2 . ARG   A 62  ? 0.8877 0.5189 0.3682 0.1130  0.0925  0.0214  68  ARG   A NH2 
494  N N   . ARG   A 63  ? 0.7017 0.3863 0.2970 0.0843  -0.0763 0.0219  69  ARG   A N   
495  C CA  . ARG   A 63  ? 0.7016 0.3910 0.3209 0.0813  -0.0907 0.0270  69  ARG   A CA  
496  C C   . ARG   A 63  ? 0.6813 0.3895 0.3315 0.0705  -0.0645 0.0374  69  ARG   A C   
497  O O   . ARG   A 63  ? 0.7057 0.3998 0.3449 0.0731  -0.0609 0.0477  69  ARG   A O   
498  C CB  . ARG   A 63  ? 0.7560 0.4059 0.3223 0.0960  -0.1092 0.0320  69  ARG   A CB  
499  C CG  . ARG   A 63  ? 0.8288 0.4621 0.3771 0.1055  -0.1455 0.0195  69  ARG   A CG  
500  C CD  . ARG   A 63  ? 0.9046 0.4978 0.3993 0.1207  -0.1673 0.0251  69  ARG   A CD  
501  N NE  . ARG   A 63  ? 0.9730 0.5439 0.4392 0.1315  -0.2027 0.0112  69  ARG   A NE  
502  C CZ  . ARG   A 63  ? 1.0439 0.5691 0.4309 0.1484  -0.2143 0.0104  69  ARG   A CZ  
503  N NH1 . ARG   A 63  ? 1.0740 0.5705 0.4012 0.1567  -0.1890 0.0249  69  ARG   A NH1 
504  N NH2 . ARG   A 63  ? 1.0666 0.5725 0.4323 0.1573  -0.2499 -0.0054 69  ARG   A NH2 
505  N N   . LYS   A 64  ? 0.6446 0.3814 0.3304 0.0594  -0.0468 0.0347  70  LYS   A N   
506  C CA  . LYS   A 64  ? 0.6243 0.3774 0.3388 0.0492  -0.0241 0.0420  70  LYS   A CA  
507  C C   . LYS   A 64  ? 0.5651 0.3535 0.3304 0.0363  -0.0228 0.0350  70  LYS   A C   
508  O O   . LYS   A 64  ? 0.5552 0.3552 0.3285 0.0354  -0.0281 0.0274  70  LYS   A O   
509  C CB  . LYS   A 64  ? 0.6881 0.4305 0.3808 0.0514  0.0045  0.0496  70  LYS   A CB  
510  C CG  . LYS   A 64  ? 0.8227 0.5333 0.4769 0.0599  0.0161  0.0629  70  LYS   A CG  
511  C CD  . LYS   A 64  ? 0.9229 0.6326 0.5823 0.0568  0.0507  0.0726  70  LYS   A CD  
512  C CE  . LYS   A 64  ? 1.0485 0.7179 0.6538 0.0696  0.0661  0.0867  70  LYS   A CE  
513  N NZ  . LYS   A 64  ? 1.1275 0.7656 0.6683 0.0854  0.0568  0.0834  70  LYS   A NZ  
514  N N   . HIS   A 65  ? 0.5298 0.3321 0.3256 0.0272  -0.0151 0.0378  71  HIS   A N   
515  C CA  . HIS   A 65  ? 0.4948 0.3263 0.3317 0.0154  -0.0124 0.0319  71  HIS   A CA  
516  C C   . HIS   A 65  ? 0.5139 0.3528 0.3599 0.0097  0.0090  0.0356  71  HIS   A C   
517  O O   . HIS   A 65  ? 0.5416 0.3674 0.3803 0.0104  0.0229  0.0438  71  HIS   A O   
518  C CB  . HIS   A 65  ? 0.4746 0.3125 0.3366 0.0101  -0.0179 0.0309  71  HIS   A CB  
519  C CG  . HIS   A 65  ? 0.4771 0.3093 0.3410 0.0156  -0.0377 0.0281  71  HIS   A CG  
520  N ND1 . HIS   A 65  ? 0.4850 0.3341 0.3760 0.0118  -0.0462 0.0210  71  HIS   A ND1 
521  C CD2 . HIS   A 65  ? 0.4988 0.3093 0.3424 0.0251  -0.0508 0.0319  71  HIS   A CD2 
522  C CE1 . HIS   A 65  ? 0.4883 0.3280 0.3826 0.0181  -0.0632 0.0203  71  HIS   A CE1 
523  N NE2 . HIS   A 65  ? 0.5106 0.3271 0.3757 0.0265  -0.0691 0.0260  71  HIS   A NE2 
524  N N   . TYR   A 66  ? 0.4707 0.3286 0.3337 0.0051  0.0119  0.0309  72  TYR   A N   
525  C CA  . TYR   A 66  ? 0.4591 0.3253 0.3385 0.0000  0.0297  0.0340  72  TYR   A CA  
526  C C   . TYR   A 66  ? 0.4382 0.3290 0.3542 -0.0111 0.0260  0.0282  72  TYR   A C   
527  O O   . TYR   A 66  ? 0.4191 0.3231 0.3421 -0.0127 0.0144  0.0223  72  TYR   A O   
528  C CB  . TYR   A 66  ? 0.4639 0.3303 0.3343 0.0052  0.0363  0.0335  72  TYR   A CB  
529  C CG  . TYR   A 66  ? 0.5097 0.3477 0.3374 0.0173  0.0446  0.0386  72  TYR   A CG  
530  C CD1 . TYR   A 66  ? 0.5479 0.3693 0.3642 0.0202  0.0666  0.0485  72  TYR   A CD1 
531  C CD2 . TYR   A 66  ? 0.5334 0.3586 0.3311 0.0263  0.0309  0.0336  72  TYR   A CD2 
532  C CE1 . TYR   A 66  ? 0.5943 0.3845 0.3620 0.0331  0.0761  0.0540  72  TYR   A CE1 
533  C CE2 . TYR   A 66  ? 0.5696 0.3642 0.3198 0.0388  0.0364  0.0367  72  TYR   A CE2 
534  C CZ  . TYR   A 66  ? 0.6180 0.3940 0.3493 0.0427  0.0599  0.0473  72  TYR   A CZ  
535  O OH  . TYR   A 66  ? 0.6796 0.4201 0.3544 0.0568  0.0667  0.0512  72  TYR   A OH  
536  N N   . PRO   A 67  ? 0.4348 0.3302 0.3732 -0.0182 0.0361  0.0301  73  PRO   A N   
537  C CA  . PRO   A 67  ? 0.4264 0.3425 0.3956 -0.0281 0.0297  0.0230  73  PRO   A CA  
538  C C   . PRO   A 67  ? 0.4272 0.3578 0.4117 -0.0285 0.0317  0.0224  73  PRO   A C   
539  O O   . PRO   A 67  ? 0.4376 0.3633 0.4246 -0.0251 0.0464  0.0283  73  PRO   A O   
540  C CB  . PRO   A 67  ? 0.4406 0.3530 0.4307 -0.0347 0.0391  0.0247  73  PRO   A CB  
541  C CG  . PRO   A 67  ? 0.4672 0.3620 0.4455 -0.0285 0.0577  0.0358  73  PRO   A CG  
542  C CD  . PRO   A 67  ? 0.4530 0.3326 0.3900 -0.0174 0.0529  0.0387  73  PRO   A CD  
543  N N   . VAL   A 68  ? 0.3980 0.3445 0.3921 -0.0317 0.0185  0.0164  74  VAL   A N   
544  C CA  . VAL   A 68  ? 0.3893 0.3497 0.4003 -0.0314 0.0178  0.0165  74  VAL   A CA  
545  C C   . VAL   A 68  ? 0.3770 0.3541 0.4089 -0.0385 0.0036  0.0106  74  VAL   A C   
546  O O   . VAL   A 68  ? 0.3830 0.3593 0.4049 -0.0416 -0.0065 0.0056  74  VAL   A O   
547  C CB  . VAL   A 68  ? 0.4104 0.3685 0.4013 -0.0234 0.0140  0.0170  74  VAL   A CB  
548  C CG1 . VAL   A 68  ? 0.4342 0.3749 0.4039 -0.0149 0.0270  0.0215  74  VAL   A CG1 
549  C CG2 . VAL   A 68  ? 0.4077 0.3642 0.3825 -0.0228 0.0007  0.0134  74  VAL   A CG2 
550  N N   . SER   A 69  ? 0.3596 0.3500 0.4187 -0.0397 0.0030  0.0115  75  SER   A N   
551  C CA  . SER   A 69  ? 0.3581 0.3633 0.4339 -0.0436 -0.0140 0.0073  75  SER   A CA  
552  C C   . SER   A 69  ? 0.3570 0.3663 0.4221 -0.0369 -0.0175 0.0104  75  SER   A C   
553  O O   . SER   A 69  ? 0.3674 0.3739 0.4339 -0.0312 -0.0055 0.0146  75  SER   A O   
554  C CB  . SER   A 69  ? 0.3828 0.4003 0.5032 -0.0482 -0.0135 0.0074  75  SER   A CB  
555  O OG  . SER   A 69  ? 0.4607 0.4737 0.5961 -0.0549 -0.0097 0.0045  75  SER   A OG  
556  N N   . PHE   A 70  ? 0.3451 0.3583 0.3985 -0.0367 -0.0323 0.0085  76  PHE   A N   
557  C CA  . PHE   A 70  ? 0.3363 0.3521 0.3827 -0.0305 -0.0351 0.0124  76  PHE   A CA  
558  C C   . PHE   A 70  ? 0.3486 0.3745 0.4026 -0.0311 -0.0514 0.0131  76  PHE   A C   
559  O O   . PHE   A 70  ? 0.3561 0.3823 0.4054 -0.0355 -0.0631 0.0091  76  PHE   A O   
560  C CB  . PHE   A 70  ? 0.3393 0.3432 0.3563 -0.0266 -0.0322 0.0127  76  PHE   A CB  
561  C CG  . PHE   A 70  ? 0.3520 0.3500 0.3508 -0.0298 -0.0372 0.0094  76  PHE   A CG  
562  C CD1 . PHE   A 70  ? 0.3630 0.3525 0.3553 -0.0328 -0.0318 0.0060  76  PHE   A CD1 
563  C CD2 . PHE   A 70  ? 0.3629 0.3617 0.3503 -0.0290 -0.0455 0.0104  76  PHE   A CD2 
564  C CE1 . PHE   A 70  ? 0.3710 0.3536 0.3481 -0.0349 -0.0340 0.0025  76  PHE   A CE1 
565  C CE2 . PHE   A 70  ? 0.3736 0.3639 0.3418 -0.0308 -0.0459 0.0075  76  PHE   A CE2 
566  C CZ  . PHE   A 70  ? 0.3632 0.3462 0.3280 -0.0339 -0.0403 0.0027  76  PHE   A CZ  
567  N N   . SER   A 71  ? 0.3423 0.3741 0.4064 -0.0259 -0.0529 0.0181  77  SER   A N   
568  C CA  . SER   A 71  ? 0.3469 0.3867 0.4182 -0.0247 -0.0690 0.0210  77  SER   A CA  
569  C C   . SER   A 71  ? 0.3666 0.3977 0.4042 -0.0230 -0.0763 0.0229  77  SER   A C   
570  O O   . SER   A 71  ? 0.3834 0.4046 0.3998 -0.0223 -0.0671 0.0222  77  SER   A O   
571  C CB  . SER   A 71  ? 0.3493 0.3970 0.4455 -0.0191 -0.0662 0.0265  77  SER   A CB  
572  O OG  . SER   A 71  ? 0.3914 0.4303 0.4712 -0.0139 -0.0557 0.0284  77  SER   A OG  
573  N N   . LYS   A 72  ? 0.3708 0.4040 0.4033 -0.0219 -0.0928 0.0257  78  LYS   A N   
574  C CA  . LYS   A 72  ? 0.4025 0.4240 0.3993 -0.0188 -0.0957 0.0296  78  LYS   A CA  
575  C C   . LYS   A 72  ? 0.4022 0.4218 0.4001 -0.0128 -0.0868 0.0382  78  LYS   A C   
576  O O   . LYS   A 72  ? 0.4018 0.4298 0.4265 -0.0101 -0.0851 0.0410  78  LYS   A O   
577  C CB  . LYS   A 72  ? 0.4486 0.4675 0.4300 -0.0179 -0.1167 0.0303  78  LYS   A CB  
578  C CG  . LYS   A 72  ? 0.5222 0.5345 0.4877 -0.0237 -0.1240 0.0192  78  LYS   A CG  
579  C CD  . LYS   A 72  ? 0.6277 0.6311 0.5660 -0.0219 -0.1472 0.0172  78  LYS   A CD  
580  C CE  . LYS   A 72  ? 0.7058 0.6993 0.6265 -0.0276 -0.1521 0.0039  78  LYS   A CE  
581  N NZ  . LYS   A 72  ? 0.7637 0.7458 0.6559 -0.0257 -0.1785 -0.0015 78  LYS   A NZ  
582  N N   . PRO   A 73  ? 0.4156 0.4234 0.3889 -0.0105 -0.0793 0.0419  79  PRO   A N   
583  C CA  . PRO   A 73  ? 0.4144 0.4199 0.3958 -0.0055 -0.0715 0.0497  79  PRO   A CA  
584  C C   . PRO   A 73  ? 0.4040 0.4149 0.3990 -0.0004 -0.0810 0.0587  79  PRO   A C   
585  O O   . PRO   A 73  ? 0.4122 0.4205 0.3916 0.0015  -0.0934 0.0639  79  PRO   A O   
586  C CB  . PRO   A 73  ? 0.4494 0.4410 0.4049 -0.0042 -0.0630 0.0538  79  PRO   A CB  
587  C CG  . PRO   A 73  ? 0.4774 0.4642 0.4143 -0.0091 -0.0613 0.0449  79  PRO   A CG  
588  C CD  . PRO   A 73  ? 0.4378 0.4327 0.3783 -0.0121 -0.0762 0.0394  79  PRO   A CD  
589  N N   A SER   A 74  ? 0.3862 0.4023 0.4080 0.0025  -0.0762 0.0601  80  SER   A N   
590  N N   B SER   A 74  ? 0.3908 0.4072 0.4131 0.0024  -0.0764 0.0599  80  SER   A N   
591  C CA  A SER   A 74  ? 0.3852 0.4069 0.4264 0.0076  -0.0843 0.0683  80  SER   A CA  
592  C CA  B SER   A 74  ? 0.3939 0.4162 0.4362 0.0075  -0.0844 0.0679  80  SER   A CA  
593  C C   A SER   A 74  ? 0.3883 0.4082 0.4508 0.0119  -0.0749 0.0706  80  SER   A C   
594  C C   B SER   A 74  ? 0.3925 0.4124 0.4548 0.0119  -0.0750 0.0706  80  SER   A C   
595  O O   A SER   A 74  ? 0.3880 0.4021 0.4497 0.0108  -0.0645 0.0646  80  SER   A O   
596  O O   B SER   A 74  ? 0.3922 0.4061 0.4534 0.0108  -0.0645 0.0647  80  SER   A O   
597  C CB  A SER   A 74  ? 0.3868 0.4222 0.4518 0.0062  -0.0944 0.0645  80  SER   A CB  
598  C CB  B SER   A 74  ? 0.4074 0.4437 0.4760 0.0060  -0.0927 0.0634  80  SER   A CB  
599  O OG  A SER   A 74  ? 0.3835 0.4240 0.4677 0.0038  -0.0831 0.0557  80  SER   A OG  
600  O OG  B SER   A 74  ? 0.4378 0.4764 0.4950 0.0010  -0.1030 0.0585  80  SER   A OG  
601  N N   . LEU   A 75  ? 0.3849 0.4083 0.4673 0.0173  -0.0806 0.0788  81  LEU   A N   
602  C CA  . LEU   A 75  ? 0.3909 0.4113 0.4963 0.0220  -0.0733 0.0806  81  LEU   A CA  
603  C C   . LEU   A 75  ? 0.3905 0.4195 0.5214 0.0226  -0.0696 0.0714  81  LEU   A C   
604  O O   . LEU   A 75  ? 0.3782 0.4182 0.5286 0.0238  -0.0769 0.0736  81  LEU   A O   
605  C CB  . LEU   A 75  ? 0.3989 0.4177 0.5130 0.0281  -0.0813 0.0956  81  LEU   A CB  
606  C CG  . LEU   A 75  ? 0.4366 0.4466 0.5681 0.0329  -0.0738 0.1018  81  LEU   A CG  
607  C CD1 . LEU   A 75  ? 0.4423 0.4406 0.5598 0.0304  -0.0635 0.1014  81  LEU   A CD1 
608  C CD2 . LEU   A 75  ? 0.4530 0.4602 0.5901 0.0396  -0.0824 0.1194  81  LEU   A CD2 
609  N N   . ILE   A 76  ? 0.3940 0.4164 0.5239 0.0223  -0.0584 0.0611  82  ILE   A N   
610  C CA  . ILE   A 76  ? 0.4004 0.4250 0.5438 0.0239  -0.0498 0.0519  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.4085 0.4221 0.5613 0.0297  -0.0423 0.0466  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.4079 0.4102 0.5496 0.0296  -0.0425 0.0442  82  ILE   A O   
613  C CB  . ILE   A 76  ? 0.4242 0.4455 0.5450 0.0189  -0.0441 0.0431  82  ILE   A CB  
614  C CG1 . ILE   A 76  ? 0.4475 0.4787 0.5625 0.0129  -0.0515 0.0458  82  ILE   A CG1 
615  C CG2 . ILE   A 76  ? 0.4323 0.4481 0.5563 0.0222  -0.0307 0.0340  82  ILE   A CG2 
616  C CD1 . ILE   A 76  ? 0.4659 0.5103 0.6088 0.0128  -0.0533 0.0470  82  ILE   A CD1 
617  N N   . PHE   A 77  ? 0.4020 0.4179 0.5785 0.0350  -0.0358 0.0444  83  PHE   A N   
618  C CA  . PHE   A 77  ? 0.4161 0.4186 0.5994 0.0414  -0.0285 0.0372  83  PHE   A CA  
619  C C   . PHE   A 77  ? 0.4248 0.4116 0.5790 0.0418  -0.0206 0.0235  83  PHE   A C   
620  O O   . PHE   A 77  ? 0.4427 0.4302 0.5845 0.0407  -0.0124 0.0196  83  PHE   A O   
621  C CB  . PHE   A 77  ? 0.4153 0.4228 0.6324 0.0480  -0.0215 0.0383  83  PHE   A CB  
622  C CG  . PHE   A 77  ? 0.4417 0.4344 0.6690 0.0550  -0.0170 0.0324  83  PHE   A CG  
623  C CD1 . PHE   A 77  ? 0.4580 0.4484 0.6990 0.0559  -0.0260 0.0399  83  PHE   A CD1 
624  C CD2 . PHE   A 77  ? 0.4640 0.4422 0.6850 0.0611  -0.0028 0.0191  83  PHE   A CD2 
625  C CE1 . PHE   A 77  ? 0.4765 0.4520 0.7302 0.0617  -0.0227 0.0332  83  PHE   A CE1 
626  C CE2 . PHE   A 77  ? 0.4786 0.4405 0.7072 0.0678  -0.0001 0.0112  83  PHE   A CE2 
627  C CZ  . PHE   A 77  ? 0.4802 0.4418 0.7282 0.0676  -0.0108 0.0179  83  PHE   A CZ  
628  N N   . VAL   A 78  ? 0.4069 0.3783 0.5505 0.0434  -0.0243 0.0167  84  VAL   A N   
629  C CA  . VAL   A 78  ? 0.4190 0.3722 0.5323 0.0451  -0.0219 0.0032  84  VAL   A CA  
630  C C   . VAL   A 78  ? 0.4459 0.3803 0.5614 0.0532  -0.0192 -0.0082 84  VAL   A C   
631  O O   . VAL   A 78  ? 0.4307 0.3620 0.5672 0.0542  -0.0262 -0.0076 84  VAL   A O   
632  C CB  . VAL   A 78  ? 0.4213 0.3712 0.5196 0.0395  -0.0329 0.0029  84  VAL   A CB  
633  C CG1 . VAL   A 78  ? 0.4509 0.3802 0.5186 0.0425  -0.0350 -0.0111 84  VAL   A CG1 
634  C CG2 . VAL   A 78  ? 0.4089 0.3743 0.5016 0.0322  -0.0341 0.0125  84  VAL   A CG2 
635  N N   . GLU   A 79  ? 0.4786 0.3980 0.5712 0.0594  -0.0078 -0.0187 85  GLU   A N   
636  C CA  . GLU   A 79  ? 0.5179 0.4147 0.6039 0.0686  -0.0034 -0.0323 85  GLU   A CA  
637  C C   . GLU   A 79  ? 0.5258 0.4053 0.6044 0.0690  -0.0205 -0.0428 85  GLU   A C   
638  O O   . GLU   A 79  ? 0.5117 0.3930 0.5807 0.0632  -0.0329 -0.0417 85  GLU   A O   
639  C CB  . GLU   A 79  ? 0.5982 0.4763 0.6465 0.0758  0.0132  -0.0416 85  GLU   A CB  
640  C CG  . GLU   A 79  ? 0.7041 0.5970 0.7724 0.0770  0.0339  -0.0327 85  GLU   A CG  
641  C CD  . GLU   A 79  ? 0.8332 0.7355 0.9466 0.0808  0.0395  -0.0292 85  GLU   A CD  
642  O OE1 . GLU   A 79  ? 0.8634 0.7449 0.9713 0.0902  0.0483  -0.0406 85  GLU   A OE1 
643  O OE2 . GLU   A 79  ? 0.8621 0.7904 1.0146 0.0752  0.0336  -0.0155 85  GLU   A OE2 
644  N N   . ALA   A 80  ? 0.5449 0.4074 0.6323 0.0759  -0.0212 -0.0537 86  ALA   A N   
645  C CA  . ALA   A 80  ? 0.5807 0.4247 0.6671 0.0765  -0.0392 -0.0662 86  ALA   A CA  
646  C C   . ALA   A 80  ? 0.6267 0.4479 0.6628 0.0796  -0.0475 -0.0802 86  ALA   A C   
647  O O   . ALA   A 80  ? 0.6573 0.4657 0.6544 0.0859  -0.0344 -0.0851 86  ALA   A O   
648  C CB  . ALA   A 80  ? 0.5832 0.4103 0.6866 0.0842  -0.0374 -0.0775 86  ALA   A CB  
649  N N   . SER   A 81  ? 0.6241 0.4407 0.6630 0.0753  -0.0682 -0.0847 87  SER   A N   
650  C CA  . SER   A 81  ? 0.6537 0.4477 0.6498 0.0785  -0.0829 -0.0978 87  SER   A CA  
651  C C   . SER   A 81  ? 0.6654 0.4423 0.6801 0.0791  -0.1081 -0.1127 87  SER   A C   
652  O O   . SER   A 81  ? 0.6513 0.4337 0.7106 0.0771  -0.1096 -0.1118 87  SER   A O   
653  C CB  . SER   A 81  ? 0.6538 0.4653 0.6452 0.0706  -0.0857 -0.0856 87  SER   A CB  
654  O OG  . SER   A 81  ? 0.6467 0.4760 0.6840 0.0619  -0.0961 -0.0773 87  SER   A OG  
655  N N   . GLU   A 82  ? 0.6915 0.4480 0.6769 0.0816  -0.1293 -0.1255 88  GLU   A N   
656  C CA  . GLU   A 82  ? 0.7032 0.4450 0.7146 0.0814  -0.1570 -0.1402 88  GLU   A CA  
657  C C   . GLU   A 82  ? 0.6627 0.4317 0.7388 0.0696  -0.1629 -0.1263 88  GLU   A C   
658  O O   . GLU   A 82  ? 0.6486 0.4117 0.7668 0.0676  -0.1797 -0.1344 88  GLU   A O   
659  C CB  . GLU   A 82  ? 0.7797 0.4908 0.7426 0.0883  -0.1819 -0.1580 88  GLU   A CB  
660  C CG  . GLU   A 82  ? 0.8938 0.6166 0.8412 0.0840  -0.1853 -0.1467 88  GLU   A CG  
661  C CD  . GLU   A 82  ? 1.0652 0.7575 0.9636 0.0917  -0.2115 -0.1615 88  GLU   A CD  
662  O OE1 . GLU   A 82  ? 1.0724 0.7614 1.0008 0.0890  -0.2407 -0.1691 88  GLU   A OE1 
663  O OE2 . GLU   A 82  ? 1.1502 0.8211 0.9814 0.1009  -0.2025 -0.1645 88  GLU   A OE2 
664  N N   . TYR   A 83  ? 0.6382 0.4351 0.7231 0.0622  -0.1477 -0.1056 89  TYR   A N   
665  C CA  . TYR   A 83  ? 0.6012 0.4212 0.7382 0.0523  -0.1479 -0.0908 89  TYR   A CA  
666  C C   . TYR   A 83  ? 0.5610 0.4009 0.7362 0.0481  -0.1293 -0.0740 89  TYR   A C   
667  O O   . TYR   A 83  ? 0.5508 0.3997 0.7739 0.0426  -0.1307 -0.0658 89  TYR   A O   
668  C CB  . TYR   A 83  ? 0.6120 0.4458 0.7325 0.0477  -0.1446 -0.0802 89  TYR   A CB  
669  C CG  . TYR   A 83  ? 0.6541 0.4681 0.7381 0.0523  -0.1640 -0.0939 89  TYR   A CG  
670  C CD1 . TYR   A 83  ? 0.6649 0.4670 0.7737 0.0522  -0.1902 -0.1055 89  TYR   A CD1 
671  C CD2 . TYR   A 83  ? 0.6956 0.5004 0.7215 0.0576  -0.1571 -0.0953 89  TYR   A CD2 
672  C CE1 . TYR   A 83  ? 0.6987 0.4807 0.7720 0.0577  -0.2118 -0.1177 89  TYR   A CE1 
673  C CE2 . TYR   A 83  ? 0.7300 0.5134 0.7171 0.0632  -0.1750 -0.1059 89  TYR   A CE2 
674  C CZ  . TYR   A 83  ? 0.7399 0.5115 0.7486 0.0636  -0.2040 -0.1173 89  TYR   A CZ  
675  O OH  . TYR   A 83  ? 0.7884 0.5374 0.7568 0.0702  -0.2249 -0.1271 89  TYR   A OH  
676  N N   . TYR   A 84  ? 0.5335 0.3798 0.6899 0.0511  -0.1117 -0.0676 90  TYR   A N   
677  C CA  . TYR   A 84  ? 0.4979 0.3615 0.6870 0.0485  -0.0970 -0.0509 90  TYR   A CA  
678  C C   . TYR   A 84  ? 0.5195 0.3765 0.7002 0.0558  -0.0872 -0.0555 90  TYR   A C   
679  O O   . TYR   A 84  ? 0.5482 0.3979 0.6895 0.0609  -0.0813 -0.0629 90  TYR   A O   
680  C CB  . TYR   A 84  ? 0.4668 0.3542 0.6477 0.0431  -0.0840 -0.0313 90  TYR   A CB  
681  C CG  . TYR   A 84  ? 0.4402 0.3358 0.6273 0.0362  -0.0879 -0.0243 90  TYR   A CG  
682  C CD1 . TYR   A 84  ? 0.4195 0.3204 0.6477 0.0317  -0.0873 -0.0142 90  TYR   A CD1 
683  C CD2 . TYR   A 84  ? 0.4443 0.3411 0.5986 0.0348  -0.0899 -0.0271 90  TYR   A CD2 
684  C CE1 . TYR   A 84  ? 0.4017 0.3094 0.6382 0.0262  -0.0872 -0.0076 90  TYR   A CE1 
685  C CE2 . TYR   A 84  ? 0.4302 0.3340 0.5930 0.0292  -0.0923 -0.0211 90  TYR   A CE2 
686  C CZ  . TYR   A 84  ? 0.4109 0.3205 0.6150 0.0250  -0.0901 -0.0116 90  TYR   A CZ  
687  O OH  . TYR   A 84  ? 0.3917 0.3071 0.6065 0.0202  -0.0891 -0.0058 90  TYR   A OH  
688  N N   . PRO   A 85  ? 0.5056 0.3671 0.7240 0.0564  -0.0816 -0.0478 91  PRO   A N   
689  C CA  . PRO   A 85  ? 0.4991 0.3593 0.7153 0.0632  -0.0690 -0.0483 91  PRO   A CA  
690  C C   . PRO   A 85  ? 0.4852 0.3673 0.6871 0.0614  -0.0555 -0.0325 91  PRO   A C   
691  O O   . PRO   A 85  ? 0.4834 0.3800 0.6774 0.0548  -0.0566 -0.0215 91  PRO   A O   
692  C CB  . PRO   A 85  ? 0.4991 0.3610 0.7650 0.0631  -0.0683 -0.0398 91  PRO   A CB  
693  C CG  . PRO   A 85  ? 0.4959 0.3709 0.7846 0.0549  -0.0715 -0.0237 91  PRO   A CG  
694  C CD  . PRO   A 85  ? 0.4865 0.3556 0.7528 0.0512  -0.0831 -0.0348 91  PRO   A CD  
695  N N   . ALA   A 86  ? 0.4757 0.3599 0.6779 0.0674  -0.0430 -0.0319 92  ALA   A N   
696  C CA  . ALA   A 86  ? 0.4727 0.3776 0.6704 0.0658  -0.0324 -0.0184 92  ALA   A CA  
697  C C   . ALA   A 86  ? 0.4484 0.3731 0.6727 0.0602  -0.0361 0.0023  92  ALA   A C   
698  O O   . ALA   A 86  ? 0.4490 0.3722 0.7049 0.0619  -0.0380 0.0088  92  ALA   A O   
699  C CB  . ALA   A 86  ? 0.4755 0.3784 0.6828 0.0739  -0.0184 -0.0215 92  ALA   A CB  
700  N N   . ARG   A 87  ? 0.4224 0.3618 0.6312 0.0539  -0.0376 0.0122  93  ARG   A N   
701  C CA  . ARG   A 87  ? 0.4083 0.3610 0.6317 0.0496  -0.0413 0.0311  93  ARG   A CA  
702  C C   . ARG   A 87  ? 0.4170 0.3856 0.6205 0.0449  -0.0414 0.0396  93  ARG   A C   
703  O O   . ARG   A 87  ? 0.4277 0.3968 0.6095 0.0437  -0.0383 0.0306  93  ARG   A O   
704  C CB  . ARG   A 87  ? 0.4119 0.3562 0.6400 0.0455  -0.0468 0.0317  93  ARG   A CB  
705  C CG  . ARG   A 87  ? 0.4354 0.3815 0.6362 0.0394  -0.0494 0.0284  93  ARG   A CG  
706  C CD  . ARG   A 87  ? 0.4357 0.3688 0.6419 0.0374  -0.0560 0.0183  93  ARG   A CD  
707  N NE  . ARG   A 87  ? 0.4209 0.3589 0.6145 0.0315  -0.0570 0.0222  93  ARG   A NE  
708  C CZ  . ARG   A 87  ? 0.4376 0.3767 0.6018 0.0296  -0.0587 0.0151  93  ARG   A CZ  
709  N NH1 . ARG   A 87  ? 0.4142 0.3496 0.5556 0.0332  -0.0578 0.0053  93  ARG   A NH1 
710  N NH2 . ARG   A 87  ? 0.3822 0.3243 0.5405 0.0247  -0.0593 0.0185  93  ARG   A NH2 
711  N N   . TYR   A 88  ? 0.4014 0.3798 0.6088 0.0426  -0.0452 0.0564  94  TYR   A N   
712  C CA  . TYR   A 88  ? 0.4178 0.4077 0.6033 0.0378  -0.0479 0.0617  94  TYR   A CA  
713  C C   . TYR   A 88  ? 0.3936 0.3780 0.5591 0.0324  -0.0480 0.0610  94  TYR   A C   
714  O O   . TYR   A 88  ? 0.3915 0.3689 0.5658 0.0322  -0.0471 0.0678  94  TYR   A O   
715  C CB  . TYR   A 88  ? 0.4416 0.4410 0.6326 0.0391  -0.0543 0.0785  94  TYR   A CB  
716  C CG  . TYR   A 88  ? 0.4788 0.4864 0.6964 0.0445  -0.0562 0.0807  94  TYR   A CG  
717  C CD1 . TYR   A 88  ? 0.4971 0.5170 0.7173 0.0435  -0.0577 0.0771  94  TYR   A CD1 
718  C CD2 . TYR   A 88  ? 0.5068 0.5097 0.7528 0.0508  -0.0555 0.0864  94  TYR   A CD2 
719  C CE1 . TYR   A 88  ? 0.5127 0.5414 0.7658 0.0487  -0.0582 0.0794  94  TYR   A CE1 
720  C CE2 . TYR   A 88  ? 0.5168 0.5276 0.7925 0.0564  -0.0566 0.0889  94  TYR   A CE2 
721  C CZ  . TYR   A 88  ? 0.5293 0.5535 0.8097 0.0554  -0.0578 0.0853  94  TYR   A CZ  
722  O OH  . TYR   A 88  ? 0.5564 0.5895 0.8742 0.0613  -0.0580 0.0880  94  TYR   A OH  
723  N N   . GLN   A 89  ? 0.3728 0.3596 0.5157 0.0283  -0.0475 0.0534  95  GLN   A N   
724  C CA  . GLN   A 89  ? 0.3649 0.3476 0.4911 0.0234  -0.0471 0.0528  95  GLN   A CA  
725  C C   . GLN   A 89  ? 0.3628 0.3537 0.4711 0.0202  -0.0488 0.0625  95  GLN   A C   
726  O O   . GLN   A 89  ? 0.3724 0.3722 0.4743 0.0193  -0.0517 0.0608  95  GLN   A O   
727  C CB  . GLN   A 89  ? 0.3705 0.3480 0.4814 0.0218  -0.0467 0.0383  95  GLN   A CB  
728  C CG  . GLN   A 89  ? 0.3918 0.3656 0.4912 0.0171  -0.0470 0.0377  95  GLN   A CG  
729  C CD  . GLN   A 89  ? 0.3999 0.3638 0.4903 0.0174  -0.0502 0.0242  95  GLN   A CD  
730  O OE1 . GLN   A 89  ? 0.4034 0.3573 0.4983 0.0216  -0.0536 0.0149  95  GLN   A OE1 
731  N NE2 . GLN   A 89  ? 0.3896 0.3536 0.4651 0.0136  -0.0502 0.0228  95  GLN   A NE2 
732  N N   . SER   A 90  ? 0.3602 0.3466 0.4613 0.0190  -0.0464 0.0721  96  SER   A N   
733  C CA  . SER   A 90  ? 0.3732 0.3622 0.4490 0.0171  -0.0482 0.0798  96  SER   A CA  
734  C C   . SER   A 90  ? 0.3684 0.3562 0.4235 0.0118  -0.0451 0.0718  96  SER   A C   
735  O O   . SER   A 90  ? 0.3640 0.3479 0.4263 0.0101  -0.0414 0.0635  96  SER   A O   
736  C CB  . SER   A 90  ? 0.3956 0.3760 0.4667 0.0202  -0.0439 0.0957  96  SER   A CB  
737  O OG  . SER   A 90  ? 0.4186 0.3901 0.4990 0.0188  -0.0330 0.0961  96  SER   A OG  
738  N N   . HIS   A 91  ? 0.3651 0.3550 0.3953 0.0098  -0.0488 0.0737  97  HIS   A N   
739  C CA  . HIS   A 91  ? 0.3727 0.3603 0.3827 0.0051  -0.0457 0.0669  97  HIS   A CA  
740  C C   . HIS   A 91  ? 0.3700 0.3622 0.3879 0.0019  -0.0460 0.0539  97  HIS   A C   
741  O O   . HIS   A 91  ? 0.3768 0.3645 0.3874 -0.0009 -0.0415 0.0483  97  HIS   A O   
742  C CB  . HIS   A 91  ? 0.3739 0.3504 0.3790 0.0052  -0.0340 0.0716  97  HIS   A CB  
743  C CG  . HIS   A 91  ? 0.4383 0.4059 0.4281 0.0093  -0.0294 0.0861  97  HIS   A CG  
744  N ND1 . HIS   A 91  ? 0.4937 0.4526 0.4478 0.0095  -0.0268 0.0893  97  HIS   A ND1 
745  C CD2 . HIS   A 91  ? 0.4533 0.4164 0.4565 0.0139  -0.0261 0.0981  97  HIS   A CD2 
746  C CE1 . HIS   A 91  ? 0.5044 0.4526 0.4462 0.0150  -0.0215 0.1039  97  HIS   A CE1 
747  N NE2 . HIS   A 91  ? 0.4816 0.4326 0.4541 0.0176  -0.0208 0.1106  97  HIS   A NE2 
748  N N   . LEU   A 92  ? 0.3552 0.3544 0.3871 0.0033  -0.0500 0.0505  98  LEU   A N   
749  C CA  . LEU   A 92  ? 0.3561 0.3559 0.3907 0.0022  -0.0475 0.0404  98  LEU   A CA  
750  C C   . LEU   A 92  ? 0.3481 0.3556 0.3783 -0.0015 -0.0499 0.0376  98  LEU   A C   
751  O O   . LEU   A 92  ? 0.3409 0.3571 0.3799 -0.0014 -0.0565 0.0417  98  LEU   A O   
752  C CB  . LEU   A 92  ? 0.3507 0.3497 0.4031 0.0072  -0.0460 0.0378  98  LEU   A CB  
753  C CG  . LEU   A 92  ? 0.3622 0.3548 0.4094 0.0086  -0.0409 0.0278  98  LEU   A CG  
754  C CD1 . LEU   A 92  ? 0.3795 0.3602 0.4152 0.0084  -0.0418 0.0223  98  LEU   A CD1 
755  C CD2 . LEU   A 92  ? 0.3660 0.3557 0.4274 0.0149  -0.0377 0.0250  98  LEU   A CD2 
756  N N   . MET   A 93  ? 0.3310 0.3350 0.3520 -0.0045 -0.0455 0.0308  99  MET   A N   
757  C CA  . MET   A 93  ? 0.3297 0.3395 0.3518 -0.0087 -0.0458 0.0278  99  MET   A CA  
758  C C   . MET   A 93  ? 0.3418 0.3483 0.3688 -0.0070 -0.0365 0.0233  99  MET   A C   
759  O O   . MET   A 93  ? 0.3542 0.3496 0.3690 -0.0043 -0.0325 0.0201  99  MET   A O   
760  C CB  . MET   A 93  ? 0.3428 0.3473 0.3463 -0.0135 -0.0460 0.0249  99  MET   A CB  
761  C CG  . MET   A 93  ? 0.3845 0.3870 0.3744 -0.0138 -0.0514 0.0293  99  MET   A CG  
762  S SD  . MET   A 93  ? 0.4080 0.4006 0.3758 -0.0178 -0.0473 0.0247  99  MET   A SD  
763  C CE  . MET   A 93  ? 0.4201 0.4054 0.3931 -0.0154 -0.0388 0.0236  99  MET   A CE  
764  N N   . LEU   A 94  ? 0.3256 0.3398 0.3710 -0.0076 -0.0330 0.0235  100 LEU   A N   
765  C CA  . LEU   A 94  ? 0.3285 0.3360 0.3747 -0.0047 -0.0192 0.0208  100 LEU   A CA  
766  C C   . LEU   A 94  ? 0.3341 0.3420 0.3824 -0.0101 -0.0136 0.0196  100 LEU   A C   
767  O O   . LEU   A 94  ? 0.3313 0.3494 0.3931 -0.0161 -0.0215 0.0199  100 LEU   A O   
768  C CB  . LEU   A 94  ? 0.3238 0.3382 0.3969 -0.0003 -0.0125 0.0228  100 LEU   A CB  
769  C CG  . LEU   A 94  ? 0.3539 0.3681 0.4329 0.0055  -0.0164 0.0242  100 LEU   A CG  
770  C CD1 . LEU   A 94  ? 0.3621 0.3808 0.4689 0.0107  -0.0059 0.0251  100 LEU   A CD1 
771  C CD2 . LEU   A 94  ? 0.3832 0.3805 0.4359 0.0099  -0.0154 0.0196  100 LEU   A CD2 
772  N N   . ALA   A 95  ? 0.3357 0.3306 0.3704 -0.0072 -0.0003 0.0184  101 ALA   A N   
773  C CA  . ALA   A 95  ? 0.3555 0.3467 0.3930 -0.0107 0.0105  0.0192  101 ALA   A CA  
774  C C   . ALA   A 95  ? 0.3790 0.3574 0.4103 -0.0036 0.0304  0.0210  101 ALA   A C   
775  O O   . ALA   A 95  ? 0.3986 0.3662 0.4116 0.0041  0.0330  0.0191  101 ALA   A O   
776  C CB  . ALA   A 95  ? 0.3644 0.3441 0.3755 -0.0129 0.0070  0.0173  101 ALA   A CB  
777  N N   . VAL   A 96  ? 0.3767 0.3543 0.4233 -0.0060 0.0453  0.0244  102 VAL   A N   
778  C CA  . VAL   A 96  ? 0.4029 0.3636 0.4376 0.0014  0.0690  0.0277  102 VAL   A CA  
779  C C   . VAL   A 96  ? 0.4529 0.3899 0.4412 0.0051  0.0709  0.0279  102 VAL   A C   
780  O O   . VAL   A 96  ? 0.4580 0.3944 0.4462 -0.0007 0.0679  0.0294  102 VAL   A O   
781  C CB  . VAL   A 96  ? 0.4035 0.3721 0.4792 -0.0024 0.0874  0.0332  102 VAL   A CB  
782  C CG1 . VAL   A 96  ? 0.4358 0.3812 0.4908 0.0064  0.1170  0.0384  102 VAL   A CG1 
783  C CG2 . VAL   A 96  ? 0.3760 0.3679 0.5017 -0.0048 0.0825  0.0329  102 VAL   A CG2 
784  N N   . GLY   A 97  ? 0.4966 0.4137 0.4466 0.0149  0.0723  0.0253  103 GLY   A N   
785  C CA  . GLY   A 97  ? 0.5395 0.4320 0.4439 0.0201  0.0698  0.0252  103 GLY   A CA  
786  C C   . GLY   A 97  ? 0.5681 0.4377 0.4310 0.0316  0.0666  0.0199  103 GLY   A C   
787  O O   . GLY   A 97  ? 0.5547 0.4276 0.4244 0.0354  0.0665  0.0153  103 GLY   A O   
788  N N   . HIS   A 98  ? 0.5944 0.4388 0.4139 0.0378  0.0621  0.0199  104 HIS   A N   
789  C CA  . HIS   A 98  ? 0.6155 0.4334 0.3901 0.0496  0.0547  0.0132  104 HIS   A CA  
790  C C   . HIS   A 98  ? 0.5998 0.4243 0.3795 0.0479  0.0252  0.0043  104 HIS   A C   
791  O O   . HIS   A 98  ? 0.5968 0.4299 0.3876 0.0420  0.0102  0.0051  104 HIS   A O   
792  C CB  . HIS   A 98  ? 0.6560 0.4403 0.3785 0.0586  0.0608  0.0178  104 HIS   A CB  
793  C CG  . HIS   A 98  ? 0.7299 0.4814 0.3988 0.0725  0.0544  0.0100  104 HIS   A CG  
794  N ND1 . HIS   A 98  ? 0.7686 0.5079 0.4229 0.0805  0.0724  0.0065  104 HIS   A ND1 
795  C CD2 . HIS   A 98  ? 0.7658 0.4957 0.3975 0.0794  0.0294  0.0036  104 HIS   A CD2 
796  C CE1 . HIS   A 98  ? 0.8052 0.5136 0.4084 0.0922  0.0577  -0.0031 104 HIS   A CE1 
797  N NE2 . HIS   A 98  ? 0.8065 0.5085 0.3955 0.0919  0.0300  -0.0051 104 HIS   A NE2 
798  N N   . SER   A 99  ? 0.5937 0.4122 0.3673 0.0537  0.0187  -0.0043 105 SER   A N   
799  C CA  . SER   A 99  ? 0.6047 0.4280 0.3891 0.0525  -0.0070 -0.0125 105 SER   A CA  
800  C C   . SER   A 99  ? 0.6519 0.4515 0.4079 0.0633  -0.0133 -0.0235 105 SER   A C   
801  O O   . SER   A 99  ? 0.6700 0.4710 0.4328 0.0661  0.0006  -0.0255 105 SER   A O   
802  C CB  . SER   A 99  ? 0.5910 0.4470 0.4267 0.0424  -0.0094 -0.0106 105 SER   A CB  
803  O OG  . SER   A 99  ? 0.6249 0.4855 0.4764 0.0411  -0.0296 -0.0166 105 SER   A OG  
804  N N   . GLU   A 100 ? 0.6688 0.4459 0.3955 0.0696  -0.0353 -0.0313 106 GLU   A N   
805  C CA  . GLU   A 100 ? 0.6992 0.4508 0.3980 0.0799  -0.0484 -0.0450 106 GLU   A CA  
806  C C   . GLU   A 100 ? 0.7041 0.4684 0.4414 0.0748  -0.0757 -0.0528 106 GLU   A C   
807  O O   . GLU   A 100 ? 0.6909 0.4768 0.4626 0.0657  -0.0833 -0.0466 106 GLU   A O   
808  C CB  . GLU   A 100 ? 0.7457 0.4570 0.3781 0.0925  -0.0552 -0.0486 106 GLU   A CB  
809  C CG  . GLU   A 100 ? 0.8131 0.5087 0.4079 0.0984  -0.0236 -0.0392 106 GLU   A CG  
810  C CD  . GLU   A 100 ? 0.9400 0.5914 0.4606 0.1124  -0.0262 -0.0396 106 GLU   A CD  
811  O OE1 . GLU   A 100 ? 0.9630 0.5842 0.4428 0.1231  -0.0471 -0.0531 106 GLU   A OE1 
812  O OE2 . GLU   A 100 ? 0.9644 0.6092 0.4664 0.1131  -0.0083 -0.0264 106 GLU   A OE2 
813  N N   . PRO   A 101 ? 0.7206 0.4721 0.4573 0.0802  -0.0892 -0.0661 107 PRO   A N   
814  C CA  . PRO   A 101 ? 0.7004 0.4664 0.4848 0.0740  -0.1117 -0.0713 107 PRO   A CA  
815  C C   . PRO   A 101 ? 0.6737 0.4440 0.4743 0.0698  -0.1335 -0.0695 107 PRO   A C   
816  O O   . PRO   A 101 ? 0.6512 0.4482 0.5023 0.0599  -0.1347 -0.0630 107 PRO   A O   
817  C CB  . PRO   A 101 ? 0.7324 0.4731 0.5005 0.0830  -0.1256 -0.0882 107 PRO   A CB  
818  C CG  . PRO   A 101 ? 0.7599 0.4866 0.4912 0.0906  -0.0997 -0.0887 107 PRO   A CG  
819  C CD  . PRO   A 101 ? 0.7441 0.4672 0.4413 0.0918  -0.0821 -0.0769 107 PRO   A CD  
820  N N   . GLY   A 102 ? 0.6612 0.4050 0.4190 0.0779  -0.1483 -0.0738 108 GLY   A N   
821  C CA  . GLY   A 102 ? 0.6419 0.3875 0.4144 0.0755  -0.1690 -0.0717 108 GLY   A CA  
822  C C   . GLY   A 102 ? 0.6046 0.3750 0.3992 0.0664  -0.1528 -0.0563 108 GLY   A C   
823  O O   . GLY   A 102 ? 0.5981 0.3736 0.4142 0.0636  -0.1668 -0.0538 108 GLY   A O   
824  N N   . ASP   A 103 ? 0.5669 0.3525 0.3602 0.0616  -0.1241 -0.0467 109 ASP   A N   
825  C CA  . ASP   A 103 ? 0.5409 0.3494 0.3568 0.0524  -0.1098 -0.0344 109 ASP   A CA  
826  C C   . ASP   A 103 ? 0.4948 0.3327 0.3659 0.0420  -0.1085 -0.0312 109 ASP   A C   
827  O O   . ASP   A 103 ? 0.4642 0.3175 0.3544 0.0351  -0.1021 -0.0236 109 ASP   A O   
828  C CB  . ASP   A 103 ? 0.5519 0.3640 0.3488 0.0513  -0.0825 -0.0261 109 ASP   A CB  
829  C CG  . ASP   A 103 ? 0.6038 0.3868 0.3474 0.0606  -0.0783 -0.0243 109 ASP   A CG  
830  O OD1 . ASP   A 103 ? 0.6018 0.3705 0.3302 0.0643  -0.0945 -0.0241 109 ASP   A OD1 
831  O OD2 . ASP   A 103 ? 0.6173 0.3909 0.3355 0.0649  -0.0576 -0.0219 109 ASP   A OD2 
832  N N   . CYS   A 104 ? 0.4894 0.3320 0.3850 0.0416  -0.1149 -0.0370 110 CYS   A N   
833  C CA  . CYS   A 104 ? 0.4605 0.3273 0.4049 0.0330  -0.1114 -0.0319 110 CYS   A CA  
834  C C   . CYS   A 104 ? 0.4486 0.3195 0.4188 0.0298  -0.1221 -0.0301 110 CYS   A C   
835  O O   . CYS   A 104 ? 0.4691 0.3240 0.4343 0.0350  -0.1418 -0.0368 110 CYS   A O   
836  C CB  . CYS   A 104 ? 0.4746 0.3412 0.4420 0.0343  -0.1177 -0.0380 110 CYS   A CB  
837  S SG  . CYS   A 104 ? 0.5129 0.3806 0.4649 0.0370  -0.1010 -0.0380 110 CYS   A SG  
838  N N   . GLY   A 105 ? 0.4094 0.2993 0.4047 0.0223  -0.1095 -0.0214 111 GLY   A N   
839  C CA  . GLY   A 105 ? 0.4079 0.3021 0.4300 0.0195  -0.1141 -0.0189 111 GLY   A CA  
840  C C   . GLY   A 105 ? 0.4198 0.3145 0.4229 0.0177  -0.1058 -0.0139 111 GLY   A C   
841  O O   . GLY   A 105 ? 0.4145 0.3159 0.4406 0.0143  -0.1026 -0.0103 111 GLY   A O   
842  N N   . GLY   A 106 ? 0.4232 0.3097 0.3866 0.0203  -0.1001 -0.0133 112 GLY   A N   
843  C CA  . GLY   A 106 ? 0.4070 0.2935 0.3553 0.0180  -0.0903 -0.0079 112 GLY   A CA  
844  C C   . GLY   A 106 ? 0.3844 0.2901 0.3508 0.0095  -0.0740 -0.0025 112 GLY   A C   
845  O O   . GLY   A 106 ? 0.3705 0.2873 0.3416 0.0064  -0.0658 -0.0009 112 GLY   A O   
846  N N   . ILE   A 107 ? 0.3666 0.2742 0.3424 0.0065  -0.0703 0.0000  113 ILE   A N   
847  C CA  . ILE   A 107 ? 0.3522 0.2732 0.3388 -0.0004 -0.0562 0.0032  113 ILE   A CA  
848  C C   . ILE   A 107 ? 0.3563 0.2807 0.3232 -0.0041 -0.0457 0.0049  113 ILE   A C   
849  O O   . ILE   A 107 ? 0.3772 0.2923 0.3270 -0.0025 -0.0449 0.0056  113 ILE   A O   
850  C CB  . ILE   A 107 ? 0.3693 0.2897 0.3769 -0.0017 -0.0544 0.0038  113 ILE   A CB  
851  C CG1 . ILE   A 107 ? 0.3763 0.2996 0.4175 -0.0002 -0.0595 0.0034  113 ILE   A CG1 
852  C CG2 . ILE   A 107 ? 0.3810 0.3087 0.3868 -0.0078 -0.0388 0.0053  113 ILE   A CG2 
853  C CD1 . ILE   A 107 ? 0.4055 0.3271 0.4760 0.0002  -0.0582 0.0040  113 ILE   A CD1 
854  N N   . LEU   A 108 ? 0.3409 0.2772 0.3118 -0.0089 -0.0381 0.0062  114 LEU   A N   
855  C CA  . LEU   A 108 ? 0.3513 0.2928 0.3127 -0.0136 -0.0308 0.0066  114 LEU   A CA  
856  C C   . LEU   A 108 ? 0.3552 0.2984 0.3210 -0.0181 -0.0254 0.0055  114 LEU   A C   
857  O O   . LEU   A 108 ? 0.3429 0.2893 0.3153 -0.0181 -0.0233 0.0064  114 LEU   A O   
858  C CB  . LEU   A 108 ? 0.3534 0.3052 0.3152 -0.0147 -0.0302 0.0080  114 LEU   A CB  
859  C CG  . LEU   A 108 ? 0.3648 0.3244 0.3255 -0.0204 -0.0265 0.0077  114 LEU   A CG  
860  C CD1 . LEU   A 108 ? 0.3707 0.3263 0.3289 -0.0219 -0.0219 0.0072  114 LEU   A CD1 
861  C CD2 . LEU   A 108 ? 0.3713 0.3417 0.3374 -0.0204 -0.0293 0.0099  114 LEU   A CD2 
862  N N   . ARG   A 109 ? 0.3602 0.2990 0.3215 -0.0211 -0.0217 0.0036  115 ARG   A N   
863  C CA  . ARG   A 109 ? 0.3845 0.3216 0.3468 -0.0246 -0.0160 0.0004  115 ARG   A CA  
864  C C   . ARG   A 109 ? 0.3866 0.3249 0.3422 -0.0303 -0.0140 -0.0036 115 ARG   A C   
865  O O   . ARG   A 109 ? 0.3790 0.3178 0.3357 -0.0319 -0.0146 -0.0028 115 ARG   A O   
866  C CB  . ARG   A 109 ? 0.4318 0.3594 0.4036 -0.0223 -0.0142 -0.0001 115 ARG   A CB  
867  C CG  . ARG   A 109 ? 0.5426 0.4615 0.5122 -0.0206 -0.0170 0.0014  115 ARG   A CG  
868  C CD  . ARG   A 109 ? 0.6400 0.5499 0.6231 -0.0180 -0.0165 0.0013  115 ARG   A CD  
869  N NE  . ARG   A 109 ? 0.7016 0.6119 0.7011 -0.0130 -0.0230 0.0028  115 ARG   A NE  
870  C CZ  . ARG   A 109 ? 0.7418 0.6551 0.7605 -0.0129 -0.0169 0.0018  115 ARG   A CZ  
871  N NH1 . ARG   A 109 ? 0.7513 0.6649 0.7664 -0.0167 -0.0038 -0.0014 115 ARG   A NH1 
872  N NH2 . ARG   A 109 ? 0.7274 0.6418 0.7692 -0.0088 -0.0233 0.0035  115 ARG   A NH2 
873  N N   . CYS   A 110 ? 0.4006 0.3377 0.3491 -0.0331 -0.0113 -0.0081 116 CYS   A N   
874  C CA  . CYS   A 110 ? 0.4177 0.3534 0.3610 -0.0387 -0.0129 -0.0146 116 CYS   A CA  
875  C C   . CYS   A 110 ? 0.4412 0.3646 0.3813 -0.0394 -0.0055 -0.0207 116 CYS   A C   
876  O O   . CYS   A 110 ? 0.4512 0.3696 0.3971 -0.0354 0.0010  -0.0183 116 CYS   A O   
877  C CB  . CYS   A 110 ? 0.4311 0.3723 0.3621 -0.0399 -0.0195 -0.0164 116 CYS   A CB  
878  S SG  . CYS   A 110 ? 0.4246 0.3573 0.3345 -0.0358 -0.0129 -0.0163 116 CYS   A SG  
879  N N   . GLN   A 111 ? 0.4579 0.3759 0.3910 -0.0442 -0.0072 -0.0295 117 GLN   A N   
880  C CA  . GLN   A 111 ? 0.4904 0.3944 0.4188 -0.0444 0.0009  -0.0370 117 GLN   A CA  
881  C C   . GLN   A 111 ? 0.5142 0.4111 0.4273 -0.0395 0.0103  -0.0372 117 GLN   A C   
882  O O   . GLN   A 111 ? 0.5414 0.4271 0.4571 -0.0376 0.0214  -0.0408 117 GLN   A O   
883  C CB  . GLN   A 111 ? 0.5260 0.4236 0.4476 -0.0503 -0.0050 -0.0486 117 GLN   A CB  
884  C CG  . GLN   A 111 ? 0.5839 0.4821 0.4820 -0.0510 -0.0152 -0.0538 117 GLN   A CG  
885  C CD  . GLN   A 111 ? 0.6708 0.5622 0.5673 -0.0571 -0.0258 -0.0670 117 GLN   A CD  
886  O OE1 . GLN   A 111 ? 0.6929 0.5938 0.6002 -0.0613 -0.0400 -0.0684 117 GLN   A OE1 
887  N NE2 . GLN   A 111 ? 0.6808 0.5553 0.5688 -0.0577 -0.0192 -0.0775 117 GLN   A NE2 
888  N N   . HIS   A 112 ? 0.5073 0.4095 0.4070 -0.0368 0.0082  -0.0322 118 HIS   A N   
889  C CA  . HIS   A 112 ? 0.5181 0.4111 0.4026 -0.0317 0.0211  -0.0305 118 HIS   A CA  
890  C C   . HIS   A 112 ? 0.5054 0.4036 0.4139 -0.0271 0.0298  -0.0205 118 HIS   A C   
891  O O   . HIS   A 112 ? 0.5291 0.4193 0.4348 -0.0228 0.0447  -0.0179 118 HIS   A O   
892  C CB  . HIS   A 112 ? 0.5299 0.4201 0.3820 -0.0304 0.0157  -0.0303 118 HIS   A CB  
893  C CG  . HIS   A 112 ? 0.5400 0.4245 0.3713 -0.0346 0.0023  -0.0416 118 HIS   A CG  
894  N ND1 . HIS   A 112 ? 0.5484 0.4458 0.3884 -0.0387 -0.0156 -0.0415 118 HIS   A ND1 
895  C CD2 . HIS   A 112 ? 0.5576 0.4238 0.3625 -0.0350 0.0041  -0.0539 118 HIS   A CD2 
896  C CE1 . HIS   A 112 ? 0.5633 0.4518 0.3865 -0.0420 -0.0266 -0.0534 118 HIS   A CE1 
897  N NE2 . HIS   A 112 ? 0.5734 0.4420 0.3731 -0.0400 -0.0162 -0.0621 118 HIS   A NE2 
898  N N   . GLY   A 113 ? 0.4670 0.3766 0.3992 -0.0275 0.0210  -0.0153 119 GLY   A N   
899  C CA  . GLY   A 113 ? 0.4472 0.3610 0.4048 -0.0233 0.0239  -0.0079 119 GLY   A CA  
900  C C   . GLY   A 113 ? 0.4116 0.3366 0.3759 -0.0228 0.0116  -0.0023 119 GLY   A C   
901  O O   . GLY   A 113 ? 0.3991 0.3292 0.3550 -0.0255 0.0021  -0.0037 119 GLY   A O   
902  N N   . VAL   A 114 ? 0.3952 0.3234 0.3777 -0.0192 0.0131  0.0036  120 VAL   A N   
903  C CA  . VAL   A 114 ? 0.3930 0.3292 0.3831 -0.0179 0.0022  0.0076  120 VAL   A CA  
904  C C   . VAL   A 114 ? 0.3832 0.3243 0.3549 -0.0187 0.0011  0.0104  120 VAL   A C   
905  O O   . VAL   A 114 ? 0.4132 0.3506 0.3753 -0.0176 0.0105  0.0137  120 VAL   A O   
906  C CB  . VAL   A 114 ? 0.4001 0.3366 0.4221 -0.0140 0.0024  0.0115  120 VAL   A CB  
907  C CG1 . VAL   A 114 ? 0.3999 0.3421 0.4276 -0.0123 -0.0095 0.0136  120 VAL   A CG1 
908  C CG2 . VAL   A 114 ? 0.4076 0.3395 0.4505 -0.0123 -0.0019 0.0088  120 VAL   A CG2 
909  N N   . VAL   A 115 ? 0.3574 0.3053 0.3240 -0.0198 -0.0094 0.0100  121 VAL   A N   
910  C CA  . VAL   A 115 ? 0.3457 0.2996 0.3010 -0.0201 -0.0133 0.0130  121 VAL   A CA  
911  C C   . VAL   A 115 ? 0.3412 0.2995 0.3116 -0.0165 -0.0167 0.0183  121 VAL   A C   
912  O O   . VAL   A 115 ? 0.3540 0.3144 0.3214 -0.0150 -0.0158 0.0239  121 VAL   A O   
913  C CB  . VAL   A 115 ? 0.3483 0.3074 0.2966 -0.0234 -0.0209 0.0090  121 VAL   A CB  
914  C CG1 . VAL   A 115 ? 0.3582 0.3256 0.3037 -0.0231 -0.0277 0.0124  121 VAL   A CG1 
915  C CG2 . VAL   A 115 ? 0.3583 0.3122 0.2956 -0.0275 -0.0190 0.0027  121 VAL   A CG2 
916  N N   . GLY   A 116 ? 0.3240 0.2820 0.3080 -0.0147 -0.0222 0.0161  122 GLY   A N   
917  C CA  . GLY   A 116 ? 0.3253 0.2850 0.3238 -0.0112 -0.0273 0.0183  122 GLY   A CA  
918  C C   . GLY   A 116 ? 0.3231 0.2772 0.3285 -0.0083 -0.0358 0.0135  122 GLY   A C   
919  O O   . GLY   A 116 ? 0.3450 0.2935 0.3467 -0.0085 -0.0371 0.0104  122 GLY   A O   
920  N N   . ILE   A 117 ? 0.3186 0.2719 0.3318 -0.0049 -0.0423 0.0127  123 ILE   A N   
921  C CA  . ILE   A 117 ? 0.3160 0.2595 0.3284 -0.0006 -0.0531 0.0068  123 ILE   A CA  
922  C C   . ILE   A 117 ? 0.3384 0.2803 0.3379 0.0026  -0.0554 0.0045  123 ILE   A C   
923  O O   . ILE   A 117 ? 0.3366 0.2859 0.3430 0.0022  -0.0520 0.0076  123 ILE   A O   
924  C CB  . ILE   A 117 ? 0.3222 0.2609 0.3628 0.0019  -0.0616 0.0047  123 ILE   A CB  
925  C CG1 . ILE   A 117 ? 0.3492 0.2934 0.4107 0.0016  -0.0584 0.0087  123 ILE   A CG1 
926  C CG2 . ILE   A 117 ? 0.3311 0.2689 0.3897 0.0003  -0.0596 0.0059  123 ILE   A CG2 
927  C CD1 . ILE   A 117 ? 0.3684 0.3078 0.4687 0.0035  -0.0673 0.0062  123 ILE   A CD1 
928  N N   . VAL   A 118 ? 0.3453 0.2748 0.3249 0.0071  -0.0607 -0.0007 124 VAL   A N   
929  C CA  . VAL   A 118 ? 0.3551 0.2792 0.3204 0.0117  -0.0596 -0.0036 124 VAL   A CA  
930  C C   . VAL   A 118 ? 0.3550 0.2778 0.3383 0.0145  -0.0670 -0.0069 124 VAL   A C   
931  O O   . VAL   A 118 ? 0.3552 0.2719 0.3536 0.0159  -0.0784 -0.0106 124 VAL   A O   
932  C CB  . VAL   A 118 ? 0.3790 0.2835 0.3137 0.0181  -0.0634 -0.0085 124 VAL   A CB  
933  C CG1 . VAL   A 118 ? 0.4015 0.2967 0.3186 0.0243  -0.0588 -0.0122 124 VAL   A CG1 
934  C CG2 . VAL   A 118 ? 0.3791 0.2835 0.2996 0.0153  -0.0545 -0.0038 124 VAL   A CG2 
935  N N   . SER   A 119 ? 0.3572 0.2856 0.3437 0.0155  -0.0608 -0.0054 125 SER   A N   
936  C CA  . SER   A 119 ? 0.3662 0.2931 0.3716 0.0182  -0.0657 -0.0079 125 SER   A CA  
937  C C   . SER   A 119 ? 0.3965 0.3150 0.3879 0.0244  -0.0620 -0.0132 125 SER   A C   
938  O O   . SER   A 119 ? 0.4030 0.3113 0.4010 0.0289  -0.0693 -0.0201 125 SER   A O   
939  C CB  . SER   A 119 ? 0.3758 0.3186 0.4060 0.0135  -0.0599 0.0019  125 SER   A CB  
940  O OG  . SER   A 119 ? 0.3965 0.3376 0.4494 0.0159  -0.0632 0.0016  125 SER   A OG  
941  N N   . THR   A 120 ? 0.4101 0.3322 0.3863 0.0247  -0.0497 -0.0103 126 THR   A N   
942  C CA  . THR   A 120 ? 0.4372 0.3509 0.4032 0.0312  -0.0412 -0.0144 126 THR   A CA  
943  C C   . THR   A 120 ? 0.4627 0.3652 0.3975 0.0345  -0.0296 -0.0152 126 THR   A C   
944  O O   . THR   A 120 ? 0.4425 0.3488 0.3701 0.0301  -0.0277 -0.0107 126 THR   A O   
945  C CB  . THR   A 120 ? 0.4266 0.3582 0.4207 0.0292  -0.0334 -0.0074 126 THR   A CB  
946  O OG1 . THR   A 120 ? 0.4330 0.3788 0.4308 0.0245  -0.0246 -0.0001 126 THR   A OG1 
947  C CG2 . THR   A 120 ? 0.4124 0.3548 0.4341 0.0257  -0.0416 -0.0023 126 THR   A CG2 
948  N N   . GLY   A 121 ? 0.5051 0.3927 0.4227 0.0424  -0.0197 -0.0203 127 GLY   A N   
949  C CA  . GLY   A 121 ? 0.5515 0.4249 0.4381 0.0469  -0.0042 -0.0194 127 GLY   A CA  
950  C C   . GLY   A 121 ? 0.5932 0.4574 0.4742 0.0545  0.0152  -0.0214 127 GLY   A C   
951  O O   . GLY   A 121 ? 0.5789 0.4545 0.4891 0.0546  0.0176  -0.0217 127 GLY   A O   
952  N N   . GLY   A 122 ? 0.6439 0.4865 0.4883 0.0614  0.0311  -0.0215 128 GLY   A N   
953  C CA  . GLY   A 122 ? 0.6786 0.5075 0.5132 0.0703  0.0548  -0.0234 128 GLY   A CA  
954  C C   . GLY   A 122 ? 0.6740 0.5248 0.5491 0.0658  0.0772  -0.0132 128 GLY   A C   
955  O O   . GLY   A 122 ? 0.6473 0.5277 0.5652 0.0554  0.0694  -0.0065 128 GLY   A O   
956  N N   . ASN   A 123 ? 0.6973 0.5315 0.5591 0.0744  0.1055  -0.0123 129 ASN   A N   
957  C CA  . ASN   A 123 ? 0.6832 0.5348 0.5882 0.0717  0.1307  -0.0028 129 ASN   A CA  
958  C C   . ASN   A 123 ? 0.6542 0.5218 0.5780 0.0617  0.1331  0.0078  129 ASN   A C   
959  O O   . ASN   A 123 ? 0.6338 0.5259 0.6101 0.0551  0.1418  0.0148  129 ASN   A O   
960  C CB  . ASN   A 123 ? 0.6918 0.5710 0.6549 0.0681  0.1254  -0.0024 129 ASN   A CB  
961  C CG  . ASN   A 123 ? 0.7754 0.6386 0.7293 0.0785  0.1300  -0.0120 129 ASN   A CG  
962  O OD1 . ASN   A 123 ? 0.8240 0.6553 0.7348 0.0902  0.1484  -0.0182 129 ASN   A OD1 
963  N ND2 . ASN   A 123 ? 0.7704 0.6528 0.7621 0.0754  0.1137  -0.0133 129 ASN   A ND2 
964  N N   . GLY   A 124 ? 0.6372 0.4899 0.5207 0.0609  0.1244  0.0082  130 GLY   A N   
965  C CA  . GLY   A 124 ? 0.6013 0.4656 0.5000 0.0518  0.1262  0.0171  130 GLY   A CA  
966  C C   . GLY   A 124 ? 0.5410 0.4365 0.4785 0.0390  0.1017  0.0178  130 GLY   A C   
967  O O   . GLY   A 124 ? 0.5274 0.4357 0.4868 0.0305  0.1026  0.0236  130 GLY   A O   
968  N N   . LEU   A 125 ? 0.5137 0.4176 0.4551 0.0381  0.0799  0.0116  131 LEU   A N   
969  C CA  . LEU   A 125 ? 0.4729 0.4009 0.4412 0.0280  0.0579  0.0124  131 LEU   A CA  
970  C C   . LEU   A 125 ? 0.4787 0.3974 0.4185 0.0282  0.0373  0.0072  131 LEU   A C   
971  O O   . LEU   A 125 ? 0.5236 0.4208 0.4312 0.0363  0.0344  0.0011  131 LEU   A O   
972  C CB  . LEU   A 125 ? 0.4480 0.3961 0.4553 0.0267  0.0522  0.0126  131 LEU   A CB  
973  C CG  . LEU   A 125 ? 0.4539 0.4160 0.5032 0.0259  0.0687  0.0178  131 LEU   A CG  
974  C CD1 . LEU   A 125 ? 0.4638 0.4359 0.5417 0.0298  0.0664  0.0169  131 LEU   A CD1 
975  C CD2 . LEU   A 125 ? 0.4323 0.4148 0.5131 0.0154  0.0622  0.0227  131 LEU   A CD2 
976  N N   . VAL   A 126 ? 0.4267 0.3606 0.3805 0.0198  0.0228  0.0091  132 VAL   A N   
977  C CA  . VAL   A 126 ? 0.4090 0.3384 0.3492 0.0189  0.0049  0.0054  132 VAL   A CA  
978  C C   . VAL   A 126 ? 0.3732 0.3239 0.3419 0.0121  -0.0061 0.0079  132 VAL   A C   
979  O O   . VAL   A 126 ? 0.3713 0.3369 0.3585 0.0059  -0.0046 0.0121  132 VAL   A O   
980  C CB  . VAL   A 126 ? 0.4219 0.3404 0.3401 0.0173  0.0026  0.0062  132 VAL   A CB  
981  C CG1 . VAL   A 126 ? 0.4358 0.3657 0.3695 0.0098  0.0110  0.0118  132 VAL   A CG1 
982  C CG2 . VAL   A 126 ? 0.4030 0.3217 0.3205 0.0154  -0.0151 0.0033  132 VAL   A CG2 
983  N N   . GLY   A 127 ? 0.3496 0.2994 0.3214 0.0139  -0.0169 0.0055  133 GLY   A N   
984  C CA  . GLY   A 127 ? 0.3375 0.3026 0.3300 0.0091  -0.0252 0.0097  133 GLY   A CA  
985  C C   . GLY   A 127 ? 0.3451 0.3060 0.3315 0.0067  -0.0337 0.0088  133 GLY   A C   
986  O O   . GLY   A 127 ? 0.3600 0.3073 0.3362 0.0106  -0.0388 0.0037  133 GLY   A O   
987  N N   . PHE   A 128 ? 0.3279 0.2992 0.3216 0.0011  -0.0358 0.0135  134 PHE   A N   
988  C CA  . PHE   A 128 ? 0.3244 0.2931 0.3168 -0.0014 -0.0394 0.0140  134 PHE   A CA  
989  C C   . PHE   A 128 ? 0.3186 0.2934 0.3237 -0.0022 -0.0408 0.0199  134 PHE   A C   
990  O O   . PHE   A 128 ? 0.3133 0.2967 0.3203 -0.0036 -0.0405 0.0247  134 PHE   A O   
991  C CB  . PHE   A 128 ? 0.3301 0.3011 0.3135 -0.0067 -0.0363 0.0142  134 PHE   A CB  
992  C CG  . PHE   A 128 ? 0.3406 0.3055 0.3128 -0.0064 -0.0321 0.0112  134 PHE   A CG  
993  C CD1 . PHE   A 128 ? 0.3593 0.3106 0.3194 -0.0033 -0.0337 0.0082  134 PHE   A CD1 
994  C CD2 . PHE   A 128 ? 0.3447 0.3162 0.3207 -0.0087 -0.0265 0.0124  134 PHE   A CD2 
995  C CE1 . PHE   A 128 ? 0.3652 0.3073 0.3105 -0.0020 -0.0280 0.0078  134 PHE   A CE1 
996  C CE2 . PHE   A 128 ? 0.3532 0.3174 0.3213 -0.0084 -0.0188 0.0117  134 PHE   A CE2 
997  C CZ  . PHE   A 128 ? 0.3637 0.3120 0.3131 -0.0046 -0.0185 0.0101  134 PHE   A CZ  
998  N N   . ALA   A 129 ? 0.3139 0.2830 0.3291 -0.0008 -0.0427 0.0200  135 ALA   A N   
999  C CA  . ALA   A 129 ? 0.3221 0.2939 0.3496 -0.0011 -0.0400 0.0277  135 ALA   A CA  
1000 C C   . ALA   A 129 ? 0.3350 0.3072 0.3506 -0.0048 -0.0339 0.0311  135 ALA   A C   
1001 O O   . ALA   A 129 ? 0.3335 0.3010 0.3503 -0.0060 -0.0318 0.0278  135 ALA   A O   
1002 C CB  . ALA   A 129 ? 0.3180 0.2829 0.3679 0.0013  -0.0425 0.0263  135 ALA   A CB  
1003 N N   . ASP   A 130 ? 0.3518 0.3279 0.3550 -0.0058 -0.0320 0.0371  136 ASP   A N   
1004 C CA  . ASP   A 130 ? 0.3713 0.3437 0.3562 -0.0081 -0.0263 0.0387  136 ASP   A CA  
1005 C C   . ASP   A 130 ? 0.3696 0.3340 0.3627 -0.0066 -0.0151 0.0443  136 ASP   A C   
1006 O O   . ASP   A 130 ? 0.3667 0.3297 0.3763 -0.0038 -0.0122 0.0512  136 ASP   A O   
1007 C CB  . ASP   A 130 ? 0.3999 0.3746 0.3655 -0.0080 -0.0305 0.0435  136 ASP   A CB  
1008 C CG  . ASP   A 130 ? 0.4691 0.4363 0.4077 -0.0098 -0.0269 0.0420  136 ASP   A CG  
1009 O OD1 . ASP   A 130 ? 0.4704 0.4368 0.4054 -0.0133 -0.0262 0.0338  136 ASP   A OD1 
1010 O OD2 . ASP   A 130 ? 0.5225 0.4821 0.4413 -0.0069 -0.0241 0.0492  136 ASP   A OD2 
1011 N N   . VAL   A 131 ? 0.3639 0.3223 0.3495 -0.0082 -0.0070 0.0417  137 VAL   A N   
1012 C CA  . VAL   A 131 ? 0.3849 0.3351 0.3805 -0.0064 0.0080  0.0479  137 VAL   A CA  
1013 C C   . VAL   A 131 ? 0.4104 0.3506 0.3716 -0.0060 0.0191  0.0501  137 VAL   A C   
1014 O O   . VAL   A 131 ? 0.4281 0.3586 0.3916 -0.0036 0.0362  0.0559  137 VAL   A O   
1015 C CB  . VAL   A 131 ? 0.3793 0.3284 0.4061 -0.0070 0.0104  0.0431  137 VAL   A CB  
1016 C CG1 . VAL   A 131 ? 0.3677 0.3219 0.4205 -0.0063 -0.0035 0.0391  137 VAL   A CG1 
1017 C CG2 . VAL   A 131 ? 0.3912 0.3387 0.4054 -0.0095 0.0094  0.0346  137 VAL   A CG2 
1018 N N   . ARG   A 132 ? 0.4143 0.3551 0.3451 -0.0079 0.0100  0.0446  138 ARG   A N   
1019 C CA  . ARG   A 132 ? 0.4382 0.3664 0.3319 -0.0073 0.0168  0.0429  138 ARG   A CA  
1020 C C   . ARG   A 132 ? 0.4863 0.4013 0.3513 -0.0017 0.0257  0.0540  138 ARG   A C   
1021 O O   . ARG   A 132 ? 0.5215 0.4201 0.3540 0.0007  0.0373  0.0535  138 ARG   A O   
1022 C CB  . ARG   A 132 ? 0.4285 0.3604 0.3030 -0.0112 0.0012  0.0330  138 ARG   A CB  
1023 C CG  . ARG   A 132 ? 0.4125 0.3521 0.3079 -0.0160 -0.0032 0.0233  138 ARG   A CG  
1024 C CD  . ARG   A 132 ? 0.4056 0.3493 0.2887 -0.0201 -0.0174 0.0154  138 ARG   A CD  
1025 N NE  . ARG   A 132 ? 0.4050 0.3607 0.2987 -0.0200 -0.0301 0.0191  138 ARG   A NE  
1026 C CZ  . ARG   A 132 ? 0.4183 0.3815 0.3155 -0.0234 -0.0428 0.0142  138 ARG   A CZ  
1027 N NH1 . ARG   A 132 ? 0.4290 0.3879 0.3169 -0.0276 -0.0466 0.0050  138 ARG   A NH1 
1028 N NH2 . ARG   A 132 ? 0.4058 0.3806 0.3202 -0.0226 -0.0512 0.0181  138 ARG   A NH2 
1029 N N   . ASP   A 133 ? 0.4932 0.4123 0.3678 0.0011  0.0218  0.0642  139 ASP   A N   
1030 C CA  . ASP   A 133 ? 0.5289 0.4330 0.3758 0.0075  0.0314  0.0778  139 ASP   A CA  
1031 C C   . ASP   A 133 ? 0.5435 0.4377 0.4102 0.0108  0.0579  0.0883  139 ASP   A C   
1032 O O   . ASP   A 133 ? 0.5772 0.4537 0.4170 0.0169  0.0734  0.1007  139 ASP   A O   
1033 C CB  . ASP   A 133 ? 0.5403 0.4522 0.3924 0.0097  0.0163  0.0858  139 ASP   A CB  
1034 C CG  . ASP   A 133 ? 0.5492 0.4736 0.4516 0.0085  0.0169  0.0890  139 ASP   A CG  
1035 O OD1 . ASP   A 133 ? 0.5215 0.4565 0.4535 0.0040  0.0139  0.0789  139 ASP   A OD1 
1036 O OD2 . ASP   A 133 ? 0.5841 0.5056 0.4943 0.0127  0.0194  0.1015  139 ASP   A OD2 
1037 N N   . LEU   A 134 ? 0.5199 0.4242 0.4353 0.0072  0.0627  0.0839  140 LEU   A N   
1038 C CA  . LEU   A 134 ? 0.5234 0.4214 0.4730 0.0094  0.0856  0.0930  140 LEU   A CA  
1039 C C   . LEU   A 134 ? 0.5572 0.4409 0.4918 0.0110  0.1081  0.0913  140 LEU   A C   
1040 O O   . LEU   A 134 ? 0.5428 0.4314 0.5111 0.0083  0.1130  0.0842  140 LEU   A O   
1041 C CB  . LEU   A 134 ? 0.5002 0.4141 0.5085 0.0052  0.0756  0.0867  140 LEU   A CB  
1042 C CG  . LEU   A 134 ? 0.5006 0.4264 0.5227 0.0042  0.0547  0.0857  140 LEU   A CG  
1043 C CD1 . LEU   A 134 ? 0.4765 0.4125 0.5457 0.0012  0.0433  0.0766  140 LEU   A CD1 
1044 C CD2 . LEU   A 134 ? 0.5201 0.4396 0.5439 0.0085  0.0622  0.1011  140 LEU   A CD2 
1045 N N   . LEU   A 135 ? 0.5909 0.4542 0.4712 0.0166  0.1214  0.0979  141 LEU   A N   
1046 C CA  . LEU   A 135 ? 0.6300 0.4750 0.4835 0.0195  0.1436  0.0950  141 LEU   A CA  
1047 C C   . LEU   A 135 ? 0.6435 0.4836 0.5420 0.0214  0.1741  0.1023  141 LEU   A C   
1048 O O   . LEU   A 135 ? 0.6497 0.4825 0.5502 0.0218  0.1897  0.0956  141 LEU   A O   
1049 C CB  . LEU   A 135 ? 0.6703 0.4899 0.4488 0.0268  0.1501  0.1009  141 LEU   A CB  
1050 C CG  . LEU   A 135 ? 0.7069 0.5302 0.4437 0.0254  0.1178  0.0929  141 LEU   A CG  
1051 C CD1 . LEU   A 135 ? 0.7691 0.5629 0.4287 0.0337  0.1222  0.0970  141 LEU   A CD1 
1052 C CD2 . LEU   A 135 ? 0.7038 0.5407 0.4491 0.0179  0.0989  0.0732  141 LEU   A CD2 
1053 N N   . TRP   A 136 ? 0.6407 0.4842 0.5797 0.0226  0.1832  0.1161  142 TRP   A N   
1054 C CA  . TRP   A 136 ? 0.6235 0.4635 0.6174 0.0240  0.2123  0.1244  142 TRP   A CA  
1055 C C   . TRP   A 136 ? 0.6090 0.4675 0.6651 0.0180  0.2023  0.1115  142 TRP   A C   
1056 O O   . TRP   A 136 ? 0.5973 0.4525 0.6988 0.0192  0.2257  0.1152  142 TRP   A O   
1057 C CB  . TRP   A 136 ? 0.6032 0.4429 0.6316 0.0259  0.2213  0.1416  142 TRP   A CB  
1058 C CG  . TRP   A 136 ? 0.5822 0.4424 0.6383 0.0210  0.1887  0.1373  142 TRP   A CG  
1059 C CD1 . TRP   A 136 ? 0.6000 0.4614 0.6204 0.0221  0.1698  0.1405  142 TRP   A CD1 
1060 C CD2 . TRP   A 136 ? 0.5475 0.4277 0.6715 0.0150  0.1710  0.1282  142 TRP   A CD2 
1061 N NE1 . TRP   A 136 ? 0.5783 0.4587 0.6417 0.0174  0.1456  0.1345  142 TRP   A NE1 
1062 C CE2 . TRP   A 136 ? 0.5484 0.4393 0.6715 0.0132  0.1449  0.1262  142 TRP   A CE2 
1063 C CE3 . TRP   A 136 ? 0.5312 0.4193 0.7189 0.0121  0.1747  0.1221  142 TRP   A CE3 
1064 C CZ2 . TRP   A 136 ? 0.5299 0.4362 0.7052 0.0088  0.1233  0.1170  142 TRP   A CZ2 
1065 C CZ3 . TRP   A 136 ? 0.5155 0.4198 0.7549 0.0076  0.1491  0.1130  142 TRP   A CZ3 
1066 C CH2 . TRP   A 136 ? 0.5126 0.4245 0.7419 0.0062  0.1243  0.1100  142 TRP   A CH2 
1067 N N   . LEU   A 137 ? 0.6042 0.4802 0.6630 0.0124  0.1686  0.0974  143 LEU   A N   
1068 C CA  . LEU   A 137 ? 0.5986 0.4887 0.7079 0.0081  0.1561  0.0859  143 LEU   A CA  
1069 C C   . LEU   A 137 ? 0.6392 0.5205 0.7476 0.0096  0.1748  0.0805  143 LEU   A C   
1070 O O   . LEU   A 137 ? 0.6144 0.5039 0.7764 0.0079  0.1725  0.0756  143 LEU   A O   
1071 C CB  . LEU   A 137 ? 0.5865 0.4913 0.6840 0.0034  0.1208  0.0731  143 LEU   A CB  
1072 C CG  . LEU   A 137 ? 0.5661 0.4823 0.6844 0.0017  0.0998  0.0745  143 LEU   A CG  
1073 C CD1 . LEU   A 137 ? 0.5700 0.4959 0.6638 -0.0014 0.0719  0.0631  143 LEU   A CD1 
1074 C CD2 . LEU   A 137 ? 0.5451 0.4683 0.7326 0.0008  0.0959  0.0740  143 LEU   A CD2 
1075 N N   . ASP   A 138 ? 0.7025 0.5659 0.7496 0.0132  0.1909  0.0804  144 ASP   A N   
1076 C CA  . ASP   A 138 ? 0.7568 0.6067 0.7907 0.0156  0.2112  0.0740  144 ASP   A CA  
1077 C C   . ASP   A 138 ? 0.8076 0.6416 0.8642 0.0217  0.2526  0.0855  144 ASP   A C   
1078 O O   . ASP   A 138 ? 0.8204 0.6421 0.8714 0.0246  0.2733  0.0804  144 ASP   A O   
1079 C CB  . ASP   A 138 ? 0.8125 0.6459 0.7647 0.0176  0.2091  0.0673  144 ASP   A CB  
1080 C CG  . ASP   A 138 ? 0.8783 0.7243 0.8062 0.0118  0.1733  0.0550  144 ASP   A CG  
1081 O OD1 . ASP   A 138 ? 0.8685 0.7338 0.8382 0.0066  0.1530  0.0493  144 ASP   A OD1 
1082 O OD2 . ASP   A 138 ? 0.9295 0.7646 0.7966 0.0129  0.1655  0.0513  144 ASP   A OD2 
1083 N N   . GLU   A 139 ? 0.8341 0.6661 0.9150 0.0241  0.2676  0.1013  145 GLU   A N   
1084 C CA  . GLU   A 139 ? 0.8758 0.6910 0.9811 0.0303  0.3117  0.1146  145 GLU   A CA  
1085 C C   . GLU   A 139 ? 0.8819 0.7084 1.0677 0.0289  0.3191  0.1277  145 GLU   A C   
1086 O O   . GLU   A 139 ? 0.8783 0.7207 1.0827 0.0244  0.2906  0.1279  145 GLU   A O   
1087 C CB  . GLU   A 139 ? 0.9596 0.7441 0.9806 0.0386  0.3374  0.1241  145 GLU   A CB  
1088 C CG  . GLU   A 139 ? 1.0505 0.8326 1.0426 0.0400  0.3277  0.1373  145 GLU   A CG  
1089 C CD  . GLU   A 139 ? 1.1950 0.9605 1.0894 0.0436  0.3135  0.1341  145 GLU   A CD  
1090 O OE1 . GLU   A 139 ? 1.2374 0.9831 1.0873 0.0505  0.3267  0.1496  145 GLU   A OE1 
1091 O OE2 . GLU   A 139 ? 1.2361 1.0076 1.1005 0.0399  0.2882  0.1165  145 GLU   A OE2 
1092 N N   . GLU   A 140 ? 0.8887 0.7054 1.1241 0.0330  0.3588  0.1385  146 GLU   A N   
1093 C CA  . GLU   A 140 ? 0.8792 0.7040 1.1996 0.0319  0.3714  0.1519  146 GLU   A CA  
1094 C C   . GLU   A 140 ? 0.8576 0.7117 1.2524 0.0237  0.3299  0.1408  146 GLU   A C   
1095 O O   . GLU   A 140 ? 0.8312 0.6953 1.3173 0.0218  0.3352  0.1439  146 GLU   A O   
1096 C CB  . GLU   A 140 ? 0.9295 0.7393 1.2142 0.0359  0.3865  0.1706  146 GLU   A CB  
1097 C CG  . GLU   A 140 ? 0.9709 0.7951 1.3265 0.0315  0.3750  0.1794  146 GLU   A CG  
1098 C CD  . GLU   A 140 ? 1.0405 0.8550 1.4656 0.0347  0.4181  0.1988  146 GLU   A CD  
1099 O OE1 . GLU   A 140 ? 1.0489 0.8672 1.5137 0.0328  0.4154  0.2099  146 GLU   A OE1 
1100 O OE2 . GLU   A 140 ? 1.0667 0.8691 1.5097 0.0392  0.4562  0.2032  146 GLU   A OE2 
1101 N N1  . A1BPZ B .   ? 0.6702 0.5243 0.6247 0.0538  -0.0691 -0.0515 201 A1BPZ A N1  
1102 C C4  . A1BPZ B .   ? 0.6692 0.5024 0.6193 0.0579  -0.0904 -0.0653 201 A1BPZ A C4  
1103 C C5  . A1BPZ B .   ? 0.7022 0.5535 0.6258 0.0555  -0.0556 -0.0480 201 A1BPZ A C5  
1104 C C6  . A1BPZ B .   ? 0.7695 0.5932 0.6442 0.0626  -0.0625 -0.0566 201 A1BPZ A C6  
1105 C C7  . A1BPZ B .   ? 0.8301 0.6363 0.6651 0.0709  -0.0422 -0.0579 201 A1BPZ A C7  
1106 C C8  . A1BPZ B .   ? 0.8452 0.6467 0.6515 0.0711  -0.0320 -0.0510 201 A1BPZ A C8  
1107 C C10 . A1BPZ B .   ? 0.8880 0.6561 0.6481 0.0879  0.0025  -0.0582 201 A1BPZ A C10 
1108 C C13 . A1BPZ B .   ? 0.9077 0.7010 0.7651 0.0798  -0.0418 -0.0741 201 A1BPZ A C13 
1109 O O3  . A1BPZ B .   ? 0.9757 0.7328 0.8063 0.0846  -0.0917 -0.0967 201 A1BPZ A O3  
1110 S S   . A1BPZ B .   ? 0.9756 0.7298 0.7973 0.0899  -0.0663 -0.0959 201 A1BPZ A S   
1111 O O2  . A1BPZ B .   ? 1.0182 0.7397 0.7801 0.1022  -0.0536 -0.1040 201 A1BPZ A O2  
1112 N N2  . A1BPZ B .   ? 0.9615 0.7195 0.8243 0.0901  -0.0696 -0.1028 201 A1BPZ A N2  
1113 C C12 . A1BPZ B .   ? 0.8750 0.6670 0.7016 0.0792  -0.0315 -0.0659 201 A1BPZ A C12 
1114 C C11 . A1BPZ B .   ? 0.8859 0.6590 0.6746 0.0878  -0.0087 -0.0663 201 A1BPZ A C11 
1115 C C9  . A1BPZ B .   ? 0.8722 0.6545 0.6415 0.0794  -0.0102 -0.0507 201 A1BPZ A C9  
1116 O O1  . A1BPZ B .   ? 0.6769 0.5458 0.6122 0.0520  -0.0396 -0.0380 201 A1BPZ A O1  
1117 C C3  . A1BPZ B .   ? 0.6437 0.4895 0.6280 0.0502  -0.1048 -0.0608 201 A1BPZ A C3  
1118 C C2  . A1BPZ B .   ? 0.6157 0.4866 0.6452 0.0428  -0.0955 -0.0477 201 A1BPZ A C2  
1119 C C14 . A1BPZ B .   ? 0.6289 0.5073 0.6275 0.0473  -0.0647 -0.0406 201 A1BPZ A C14 
1120 C C1  . A1BPZ B .   ? 0.6042 0.4931 0.6273 0.0400  -0.0761 -0.0351 201 A1BPZ A C1  
1121 C C   . A1BPZ B .   ? 0.5691 0.4787 0.6287 0.0344  -0.0701 -0.0219 201 A1BPZ A C   
1122 O O   . A1BPZ B .   ? 0.5480 0.4590 0.6271 0.0367  -0.0669 -0.0206 201 A1BPZ A O   
1123 N N   . A1BPZ B .   ? 0.5525 0.4757 0.6183 0.0278  -0.0682 -0.0118 201 A1BPZ A N   
# 
