data_7HWK
# 
_entry.id   7HWK 
# 
_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   7HWK         pdb_00007hwk 10.2210/pdb7hwk/pdb 
WWPDB D_1001408020 ?            ?                   
# 
_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                        7HWK 
_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-[(7R)-2-methoxy-6,7-dihydro-5H-cyclopenta[b]pyridine-7-carbonyl]piperidine-3-carboxamide' 303.356   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    64 ? 
? ? ? 
# 
_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-[(7R)-2-methoxy-6,7-dihydro-5H-cyclopenta[b]pyridine-7-carbonyl]piperidine-3-carboxamide' A1BRD 
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 
A1BRD non-polymer         . '(3S)-1-[(7R)-2-methoxy-6,7-dihydro-5H-cyclopenta[b]pyridine-7-carbonyl]piperidine-3-carboxamide' ? 
'C16 H21 N3 O3'  303.356 
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 ?   ?   ?   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        A1BRD 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BRD 
_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 A1BRD 1  201 201 A1BRD LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 2   DMS   DMS A . 
E 5 HOH   1  301 15  HOH   HOH A . 
E 5 HOH   2  302 9   HOH   HOH A . 
E 5 HOH   3  303 24  HOH   HOH A . 
E 5 HOH   4  304 1   HOH   HOH A . 
E 5 HOH   5  305 11  HOH   HOH A . 
E 5 HOH   6  306 10  HOH   HOH A . 
E 5 HOH   7  307 5   HOH   HOH A . 
E 5 HOH   8  308 16  HOH   HOH A . 
E 5 HOH   9  309 4   HOH   HOH A . 
E 5 HOH   10 310 60  HOH   HOH A . 
E 5 HOH   11 311 27  HOH   HOH A . 
E 5 HOH   12 312 61  HOH   HOH A . 
E 5 HOH   13 313 63  HOH   HOH A . 
E 5 HOH   14 314 12  HOH   HOH A . 
E 5 HOH   15 315 56  HOH   HOH A . 
E 5 HOH   16 316 64  HOH   HOH A . 
E 5 HOH   17 317 25  HOH   HOH A . 
E 5 HOH   18 318 3   HOH   HOH A . 
E 5 HOH   19 319 18  HOH   HOH A . 
E 5 HOH   20 320 6   HOH   HOH A . 
E 5 HOH   21 321 28  HOH   HOH A . 
E 5 HOH   22 322 13  HOH   HOH A . 
E 5 HOH   23 323 31  HOH   HOH A . 
E 5 HOH   24 324 58  HOH   HOH A . 
E 5 HOH   25 325 66  HOH   HOH A . 
E 5 HOH   26 326 26  HOH   HOH A . 
E 5 HOH   27 327 29  HOH   HOH A . 
E 5 HOH   28 328 19  HOH   HOH A . 
E 5 HOH   29 329 41  HOH   HOH A . 
E 5 HOH   30 330 42  HOH   HOH A . 
E 5 HOH   31 331 45  HOH   HOH A . 
E 5 HOH   32 332 40  HOH   HOH A . 
E 5 HOH   33 333 57  HOH   HOH A . 
E 5 HOH   34 334 52  HOH   HOH A . 
E 5 HOH   35 335 7   HOH   HOH A . 
E 5 HOH   36 336 22  HOH   HOH A . 
E 5 HOH   37 337 65  HOH   HOH A . 
E 5 HOH   38 338 62  HOH   HOH A . 
E 5 HOH   39 339 53  HOH   HOH A . 
E 5 HOH   40 340 55  HOH   HOH A . 
E 5 HOH   41 341 54  HOH   HOH A . 
E 5 HOH   42 342 8   HOH   HOH A . 
E 5 HOH   43 343 14  HOH   HOH A . 
E 5 HOH   44 344 59  HOH   HOH A . 
E 5 HOH   45 345 44  HOH   HOH A . 
E 5 HOH   46 346 32  HOH   HOH A . 
E 5 HOH   47 347 48  HOH   HOH A . 
E 5 HOH   48 348 37  HOH   HOH A . 
E 5 HOH   49 349 50  HOH   HOH A . 
E 5 HOH   50 350 33  HOH   HOH A . 
E 5 HOH   51 351 17  HOH   HOH A . 
E 5 HOH   52 352 30  HOH   HOH A . 
E 5 HOH   53 353 39  HOH   HOH A . 
E 5 HOH   54 354 23  HOH   HOH A . 
E 5 HOH   55 355 34  HOH   HOH A . 
E 5 HOH   56 356 38  HOH   HOH A . 
E 5 HOH   57 357 43  HOH   HOH A . 
E 5 HOH   58 358 21  HOH   HOH A . 
E 5 HOH   59 359 20  HOH   HOH A . 
E 5 HOH   60 360 51  HOH   HOH A . 
E 5 HOH   61 361 2   HOH   HOH A . 
E 5 HOH   62 362 35  HOH   HOH A . 
E 5 HOH   63 363 47  HOH   HOH A . 
E 5 HOH   64 364 67  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           7HWK 
_cell.length_a           72.391 
_cell.length_b           61.741 
_cell.length_c           32.617 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.04 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWK 
_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          7HWK 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46.29 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HWK 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.14 
_reflns.d_resolution_high            1.94 
_reflns.number_obs                   9776 
_reflns.percent_possible_obs         91.7 
_reflns.pdbx_Rmerge_I_obs            0.214 
_reflns.pdbx_netI_over_sigmaI        4.5 
_reflns.pdbx_redundancy              4.9 
_reflns.pdbx_Rrim_I_all              0.240 
_reflns.pdbx_Rpim_I_all              0.104 
_reflns.pdbx_CC_half                 0.789 
_reflns.pdbx_number_measured_all     48177 
_reflns.pdbx_chi_squared             0.77 
_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                  1.94 
_reflns_shell.d_res_low                   2.05 
_reflns_shell.number_measured_all         4626 
_reflns_shell.number_unique_obs           1289 
_reflns_shell.Rmerge_I_obs                1.493 
_reflns_shell.pdbx_chi_squared            0.59 
_reflns_shell.pdbx_redundancy             3.6 
_reflns_shell.percent_possible_obs        83.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.730 
_reflns_shell.pdbx_Rpim_I_all             0.859 
_reflns_shell.pdbx_CC_half                0.043 
_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                                 7HWK 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     9699 
_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                             36.15 
_refine.ls_d_res_high                            1.943 
_refine.ls_percent_reflns_obs                    91.1 
_refine.ls_R_factor_obs                          0.2519 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2492 
_refine.ls_R_factor_R_free                       0.3117 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.460 
_refine.ls_number_reflns_R_free                  433 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.907 
_refine.correlation_coeff_Fo_to_Fc_free          0.866 
_refine.B_iso_mean                               32.40 
_refine.aniso_B[1][1]                            1.74130 
_refine.aniso_B[2][2]                            -0.21050 
_refine.aniso_B[3][3]                            -1.53090 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -3.34980 
_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             0.240 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.216 
_refine.pdbx_overall_SU_R_Blow_DPI               0.242 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.215 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWK 
_refine_analyze.Luzzati_coordinate_error_obs    0.34 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         23 
_refine_hist.number_atoms_solvent             64 
_refine_hist.number_atoms_total               1161 
_refine_hist.d_res_high                       1.943 
_refine_hist.d_res_low                        36.15 
# 
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                  0.008 ? 2.00  1131 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.92  ? 2.00  1540 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  380  '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  204  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1128 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.52  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           17.64 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  139  '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  915  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   22 
_refine_ls_shell.d_res_high                       1.94 
_refine_ls_shell.d_res_low                        1.98 
_refine_ls_shell.number_reflns_R_work             440 
_refine_ls_shell.R_factor_R_work                  0.3400 
_refine_ls_shell.percent_reflns_obs               76.34 
_refine_ls_shell.R_factor_R_free                  0.4003 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.76 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_all                462 
_refine_ls_shell.R_factor_all                     0.3429 
# 
_struct.entry_id                  7HWK 
_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-0034455-001 (A71EV2A-x3954)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWK 
_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              7HWK 
_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 LEU A 134 ? ASP A 138 ? LEU A 140 ASP A 144 5 ? 5 
# 
_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 ? ? ? ? ? ? ? 2.175 ? ? 
metalc2 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.299 ? ? 
metalc3 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 1.923 ? ? 
# 
_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 110 ? A CYS 116 ? 1_555 117.5 ? 
2 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 87.1  ? 
3 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 69.6  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
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 
AA1 3 4 ? 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
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 ILE A 117 ? N ILE A 123 O ALA A 129 ? O ALA A 135 
AA2 5 6 O VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7HWK 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -93.25  31.29  
2 1 SER A 125 ? ? -131.91 -36.28 
# 
_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         15.0249 
_pdbx_refine_tls.origin_y         7.1481 
_pdbx_refine_tls.origin_z         14.2477 
_pdbx_refine_tls.T[1][1]          -0.0198 
_pdbx_refine_tls.T[2][2]          -0.0400 
_pdbx_refine_tls.T[3][3]          -0.1207 
_pdbx_refine_tls.T[1][2]          0.0249 
_pdbx_refine_tls.T[1][3]          -0.0726 
_pdbx_refine_tls.T[2][3]          -0.0108 
_pdbx_refine_tls.L[1][1]          0.6997 
_pdbx_refine_tls.L[2][2]          9.0877 
_pdbx_refine_tls.L[3][3]          1.8823 
_pdbx_refine_tls.L[1][2]          2.6163 
_pdbx_refine_tls.L[1][3]          -0.8869 
_pdbx_refine_tls.L[2][3]          -2.9305 
_pdbx_refine_tls.S[1][1]          -0.0994 
_pdbx_refine_tls.S[1][2]          0.1241 
_pdbx_refine_tls.S[1][3]          -0.0445 
_pdbx_refine_tls.S[2][1]          0.4284 
_pdbx_refine_tls.S[2][2]          0.1790 
_pdbx_refine_tls.S[2][3]          -0.2700 
_pdbx_refine_tls.S[3][1]          -0.1143 
_pdbx_refine_tls.S[3][2]          -0.1345 
_pdbx_refine_tls.S[3][3]          -0.0796 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
6 1 N 0 A DMS 203 ? D DMS ?   
# 
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 
A1BRD N1   N  N N 1   
A1BRD C4   C  Y N 2   
A1BRD C5   C  Y N 3   
A1BRD C6   C  N S 4   
A1BRD C7   C  N N 5   
A1BRD C8   C  N N 6   
A1BRD C10  C  N N 7   
A1BRD C13  C  N N 8   
A1BRD C15  C  N N 9   
A1BRD O2   O  N N 10  
A1BRD C12  C  N N 11  
A1BRD N2   N  N N 12  
A1BRD C11  C  N S 13  
A1BRD C9   C  N N 14  
A1BRD O1   O  N N 15  
A1BRD C14  C  N N 16  
A1BRD C3   C  Y N 17  
A1BRD C2   C  Y N 18  
A1BRD N    N  Y N 19  
A1BRD C1   C  Y N 20  
A1BRD O    O  N N 21  
A1BRD C    C  N N 22  
A1BRD H    H  N N 23  
A1BRD H8   H  N N 24  
A1BRD H7   H  N N 25  
A1BRD H11  H  N N 26  
A1BRD H12  H  N N 27  
A1BRD H15  H  N N 28  
A1BRD H16  H  N N 29  
A1BRD H19  H  N N 30  
A1BRD H20  H  N N 31  
A1BRD H14  H  N N 32  
A1BRD H13  H  N N 33  
A1BRD H1   H  N N 34  
A1BRD H9   H  N N 35  
A1BRD H10  H  N N 36  
A1BRD H17  H  N N 37  
A1BRD H18  H  N N 38  
A1BRD H6   H  N N 39  
A1BRD H5   H  N N 40  
A1BRD H3   H  N N 41  
A1BRD H4   H  N N 42  
A1BRD H2   H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
DMS   S    S  N N 131 
DMS   O    O  N N 132 
DMS   C1   C  N N 133 
DMS   C2   C  N N 134 
DMS   H11  H  N N 135 
DMS   H12  H  N N 136 
DMS   H13  H  N N 137 
DMS   H21  H  N N 138 
DMS   H22  H  N N 139 
DMS   H23  H  N N 140 
GLN   N    N  N N 141 
GLN   CA   C  N S 142 
GLN   C    C  N N 143 
GLN   O    O  N N 144 
GLN   CB   C  N N 145 
GLN   CG   C  N N 146 
GLN   CD   C  N N 147 
GLN   OE1  O  N N 148 
GLN   NE2  N  N N 149 
GLN   OXT  O  N N 150 
GLN   H    H  N N 151 
GLN   H2   H  N N 152 
GLN   HA   H  N N 153 
GLN   HB2  H  N N 154 
GLN   HB3  H  N N 155 
GLN   HG2  H  N N 156 
GLN   HG3  H  N N 157 
GLN   HE21 H  N N 158 
GLN   HE22 H  N N 159 
GLN   HXT  H  N N 160 
GLU   N    N  N N 161 
GLU   CA   C  N S 162 
GLU   C    C  N N 163 
GLU   O    O  N N 164 
GLU   CB   C  N N 165 
GLU   CG   C  N N 166 
GLU   CD   C  N N 167 
GLU   OE1  O  N N 168 
GLU   OE2  O  N N 169 
GLU   OXT  O  N N 170 
GLU   H    H  N N 171 
GLU   H2   H  N N 172 
GLU   HA   H  N N 173 
GLU   HB2  H  N N 174 
GLU   HB3  H  N N 175 
GLU   HG2  H  N N 176 
GLU   HG3  H  N N 177 
GLU   HE2  H  N N 178 
GLU   HXT  H  N N 179 
GLY   N    N  N N 180 
GLY   CA   C  N N 181 
GLY   C    C  N N 182 
GLY   O    O  N N 183 
GLY   OXT  O  N N 184 
GLY   H    H  N N 185 
GLY   H2   H  N N 186 
GLY   HA2  H  N N 187 
GLY   HA3  H  N N 188 
GLY   HXT  H  N N 189 
HIS   N    N  N N 190 
HIS   CA   C  N S 191 
HIS   C    C  N N 192 
HIS   O    O  N N 193 
HIS   CB   C  N N 194 
HIS   CG   C  Y N 195 
HIS   ND1  N  Y N 196 
HIS   CD2  C  Y N 197 
HIS   CE1  C  Y N 198 
HIS   NE2  N  Y N 199 
HIS   OXT  O  N N 200 
HIS   H    H  N N 201 
HIS   H2   H  N N 202 
HIS   HA   H  N N 203 
HIS   HB2  H  N N 204 
HIS   HB3  H  N N 205 
HIS   HD1  H  N N 206 
HIS   HD2  H  N N 207 
HIS   HE1  H  N N 208 
HIS   HE2  H  N N 209 
HIS   HXT  H  N N 210 
HOH   O    O  N N 211 
HOH   H1   H  N N 212 
HOH   H2   H  N N 213 
ILE   N    N  N N 214 
ILE   CA   C  N S 215 
ILE   C    C  N N 216 
ILE   O    O  N N 217 
ILE   CB   C  N S 218 
ILE   CG1  C  N N 219 
ILE   CG2  C  N N 220 
ILE   CD1  C  N N 221 
ILE   OXT  O  N N 222 
ILE   H    H  N N 223 
ILE   H2   H  N N 224 
ILE   HA   H  N N 225 
ILE   HB   H  N N 226 
ILE   HG12 H  N N 227 
ILE   HG13 H  N N 228 
ILE   HG21 H  N N 229 
ILE   HG22 H  N N 230 
ILE   HG23 H  N N 231 
ILE   HD11 H  N N 232 
ILE   HD12 H  N N 233 
ILE   HD13 H  N N 234 
ILE   HXT  H  N N 235 
LEU   N    N  N N 236 
LEU   CA   C  N S 237 
LEU   C    C  N N 238 
LEU   O    O  N N 239 
LEU   CB   C  N N 240 
LEU   CG   C  N N 241 
LEU   CD1  C  N N 242 
LEU   CD2  C  N N 243 
LEU   OXT  O  N N 244 
LEU   H    H  N N 245 
LEU   H2   H  N N 246 
LEU   HA   H  N N 247 
LEU   HB2  H  N N 248 
LEU   HB3  H  N N 249 
LEU   HG   H  N N 250 
LEU   HD11 H  N N 251 
LEU   HD12 H  N N 252 
LEU   HD13 H  N N 253 
LEU   HD21 H  N N 254 
LEU   HD22 H  N N 255 
LEU   HD23 H  N N 256 
LEU   HXT  H  N N 257 
LYS   N    N  N N 258 
LYS   CA   C  N S 259 
LYS   C    C  N N 260 
LYS   O    O  N N 261 
LYS   CB   C  N N 262 
LYS   CG   C  N N 263 
LYS   CD   C  N N 264 
LYS   CE   C  N N 265 
LYS   NZ   N  N N 266 
LYS   OXT  O  N N 267 
LYS   H    H  N N 268 
LYS   H2   H  N N 269 
LYS   HA   H  N N 270 
LYS   HB2  H  N N 271 
LYS   HB3  H  N N 272 
LYS   HG2  H  N N 273 
LYS   HG3  H  N N 274 
LYS   HD2  H  N N 275 
LYS   HD3  H  N N 276 
LYS   HE2  H  N N 277 
LYS   HE3  H  N N 278 
LYS   HZ1  H  N N 279 
LYS   HZ2  H  N N 280 
LYS   HZ3  H  N N 281 
LYS   HXT  H  N N 282 
MET   N    N  N N 283 
MET   CA   C  N S 284 
MET   C    C  N N 285 
MET   O    O  N N 286 
MET   CB   C  N N 287 
MET   CG   C  N N 288 
MET   SD   S  N N 289 
MET   CE   C  N N 290 
MET   OXT  O  N N 291 
MET   H    H  N N 292 
MET   H2   H  N N 293 
MET   HA   H  N N 294 
MET   HB2  H  N N 295 
MET   HB3  H  N N 296 
MET   HG2  H  N N 297 
MET   HG3  H  N N 298 
MET   HE1  H  N N 299 
MET   HE2  H  N N 300 
MET   HE3  H  N N 301 
MET   HXT  H  N N 302 
PHE   N    N  N N 303 
PHE   CA   C  N S 304 
PHE   C    C  N N 305 
PHE   O    O  N N 306 
PHE   CB   C  N N 307 
PHE   CG   C  Y N 308 
PHE   CD1  C  Y N 309 
PHE   CD2  C  Y N 310 
PHE   CE1  C  Y N 311 
PHE   CE2  C  Y N 312 
PHE   CZ   C  Y N 313 
PHE   OXT  O  N N 314 
PHE   H    H  N N 315 
PHE   H2   H  N N 316 
PHE   HA   H  N N 317 
PHE   HB2  H  N N 318 
PHE   HB3  H  N N 319 
PHE   HD1  H  N N 320 
PHE   HD2  H  N N 321 
PHE   HE1  H  N N 322 
PHE   HE2  H  N N 323 
PHE   HZ   H  N N 324 
PHE   HXT  H  N N 325 
PRO   N    N  N N 326 
PRO   CA   C  N S 327 
PRO   C    C  N N 328 
PRO   O    O  N N 329 
PRO   CB   C  N N 330 
PRO   CG   C  N N 331 
PRO   CD   C  N N 332 
PRO   OXT  O  N N 333 
PRO   H    H  N N 334 
PRO   HA   H  N N 335 
PRO   HB2  H  N N 336 
PRO   HB3  H  N N 337 
PRO   HG2  H  N N 338 
PRO   HG3  H  N N 339 
PRO   HD2  H  N N 340 
PRO   HD3  H  N N 341 
PRO   HXT  H  N N 342 
SER   N    N  N N 343 
SER   CA   C  N S 344 
SER   C    C  N N 345 
SER   O    O  N N 346 
SER   CB   C  N N 347 
SER   OG   O  N N 348 
SER   OXT  O  N N 349 
SER   H    H  N N 350 
SER   H2   H  N N 351 
SER   HA   H  N N 352 
SER   HB2  H  N N 353 
SER   HB3  H  N N 354 
SER   HG   H  N N 355 
SER   HXT  H  N N 356 
THR   N    N  N N 357 
THR   CA   C  N S 358 
THR   C    C  N N 359 
THR   O    O  N N 360 
THR   CB   C  N R 361 
THR   OG1  O  N N 362 
THR   CG2  C  N N 363 
THR   OXT  O  N N 364 
THR   H    H  N N 365 
THR   H2   H  N N 366 
THR   HA   H  N N 367 
THR   HB   H  N N 368 
THR   HG1  H  N N 369 
THR   HG21 H  N N 370 
THR   HG22 H  N N 371 
THR   HG23 H  N N 372 
THR   HXT  H  N N 373 
TRP   N    N  N N 374 
TRP   CA   C  N S 375 
TRP   C    C  N N 376 
TRP   O    O  N N 377 
TRP   CB   C  N N 378 
TRP   CG   C  Y N 379 
TRP   CD1  C  Y N 380 
TRP   CD2  C  Y N 381 
TRP   NE1  N  Y N 382 
TRP   CE2  C  Y N 383 
TRP   CE3  C  Y N 384 
TRP   CZ2  C  Y N 385 
TRP   CZ3  C  Y N 386 
TRP   CH2  C  Y N 387 
TRP   OXT  O  N N 388 
TRP   H    H  N N 389 
TRP   H2   H  N N 390 
TRP   HA   H  N N 391 
TRP   HB2  H  N N 392 
TRP   HB3  H  N N 393 
TRP   HD1  H  N N 394 
TRP   HE1  H  N N 395 
TRP   HE3  H  N N 396 
TRP   HZ2  H  N N 397 
TRP   HZ3  H  N N 398 
TRP   HH2  H  N N 399 
TRP   HXT  H  N N 400 
TYR   N    N  N N 401 
TYR   CA   C  N S 402 
TYR   C    C  N N 403 
TYR   O    O  N N 404 
TYR   CB   C  N N 405 
TYR   CG   C  Y N 406 
TYR   CD1  C  Y N 407 
TYR   CD2  C  Y N 408 
TYR   CE1  C  Y N 409 
TYR   CE2  C  Y N 410 
TYR   CZ   C  Y N 411 
TYR   OH   O  N N 412 
TYR   OXT  O  N N 413 
TYR   H    H  N N 414 
TYR   H2   H  N N 415 
TYR   HA   H  N N 416 
TYR   HB2  H  N N 417 
TYR   HB3  H  N N 418 
TYR   HD1  H  N N 419 
TYR   HD2  H  N N 420 
TYR   HE1  H  N N 421 
TYR   HE2  H  N N 422 
TYR   HH   H  N N 423 
TYR   HXT  H  N N 424 
VAL   N    N  N N 425 
VAL   CA   C  N S 426 
VAL   C    C  N N 427 
VAL   O    O  N N 428 
VAL   CB   C  N N 429 
VAL   CG1  C  N N 430 
VAL   CG2  C  N N 431 
VAL   OXT  O  N N 432 
VAL   H    H  N N 433 
VAL   H2   H  N N 434 
VAL   HA   H  N N 435 
VAL   HB   H  N N 436 
VAL   HG11 H  N N 437 
VAL   HG12 H  N N 438 
VAL   HG13 H  N N 439 
VAL   HG21 H  N N 440 
VAL   HG22 H  N N 441 
VAL   HG23 H  N N 442 
VAL   HXT  H  N N 443 
ZN    ZN   ZN N N 444 
# 
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 
A1BRD C   O    sing N N 1   
A1BRD O   C1   sing N N 2   
A1BRD C1  C2   doub Y N 3   
A1BRD C2  C3   sing Y N 4   
A1BRD C3  C4   doub Y N 5   
A1BRD C4  C5   sing Y N 6   
A1BRD N   C5   doub Y N 7   
A1BRD C1  N    sing Y N 8   
A1BRD C5  C6   sing N N 9   
A1BRD C6  C7   sing N N 10  
A1BRD O1  C7   doub N N 11  
A1BRD C7  N1   sing N N 12  
A1BRD N1  C8   sing N N 13  
A1BRD C8  C9   sing N N 14  
A1BRD C9  C10  sing N N 15  
A1BRD C10 C11  sing N N 16  
A1BRD C11 C12  sing N N 17  
A1BRD N2  C12  sing N N 18  
A1BRD C12 O2   doub N N 19  
A1BRD C13 C11  sing N N 20  
A1BRD N1  C13  sing N N 21  
A1BRD C14 C6   sing N N 22  
A1BRD C15 C14  sing N N 23  
A1BRD C4  C15  sing N N 24  
A1BRD C6  H    sing N N 25  
A1BRD C8  H8   sing N N 26  
A1BRD C8  H7   sing N N 27  
A1BRD C10 H11  sing N N 28  
A1BRD C10 H12  sing N N 29  
A1BRD C13 H15  sing N N 30  
A1BRD C13 H16  sing N N 31  
A1BRD C15 H19  sing N N 32  
A1BRD C15 H20  sing N N 33  
A1BRD N2  H14  sing N N 34  
A1BRD N2  H13  sing N N 35  
A1BRD C11 H1   sing N N 36  
A1BRD C9  H9   sing N N 37  
A1BRD C9  H10  sing N N 38  
A1BRD C14 H17  sing N N 39  
A1BRD C14 H18  sing N N 40  
A1BRD C3  H6   sing N N 41  
A1BRD C2  H5   sing N N 42  
A1BRD C   H3   sing N N 43  
A1BRD C   H4   sing N N 44  
A1BRD C   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                    7HWK 
_atom_sites.fract_transf_matrix[1][1]   0.013814 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000734 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016197 
_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]   0.030702 
_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   ? 18.712 6.625   24.346 1.00 37.12  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.926 6.741   23.532 1.00 37.10  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.068 5.582   22.540 1.00 36.13  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.456 4.531   22.722 1.00 36.42  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.175 6.899   24.403 1.00 38.30  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.051 6.326   25.695 1.00 39.97  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.831 5.805   21.476 1.00 35.07  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.040 4.800   20.440 1.00 34.59  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.293 5.380   19.063 1.00 33.73  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.843 6.486   18.755 1.00 33.73  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.014 4.630   18.227 1.00 33.13  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.374 5.038   16.866 1.00 33.29  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.393 3.834   15.896 1.00 32.88  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.420 2.688   16.349 1.00 32.83  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.747 5.710   16.886 1.00 33.43  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.385 4.101   14.563 1.00 32.37  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.482 3.090   13.501 1.00 32.61  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.843 3.266   12.831 1.00 33.47  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.197 4.369   12.420 1.00 33.29  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.369 3.236   12.426 1.00 32.99  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.956 3.189   13.025 1.00 33.67  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.543 2.200   11.319 1.00 33.37  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.946 3.885   12.136 1.00 35.15  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.599 2.188   12.709 1.00 34.05  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.912 2.238   12.090 1.00 34.80  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.925 1.461   10.786 1.00 35.97  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.954 0.240   10.827 1.00 36.17  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.953 1.688   13.071 1.00 34.38  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.092 2.536   14.318 1.00 34.19  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.791 3.732   14.294 1.00 35.18  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.527 2.140   15.517 1.00 34.53  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.914 4.521   15.431 1.00 35.64  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.639 2.921   16.660 1.00 35.31  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.336 4.112   16.613 1.00 35.86  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.492 4.863   17.748 1.00 36.56  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.899 2.162   9.630  1.00 36.43  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.943 1.555   8.291  1.00 37.36  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.083 2.164   7.479  1.00 39.20  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.105 3.379   7.248  1.00 39.51  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.606 1.680   7.528  1.00 37.46  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.103 3.124   7.512  1.00 37.81  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.741 1.142   6.108  1.00 37.49  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.035 1.325   7.061  1.00 40.21  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.198 1.770   6.304  1.00 41.18  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.010 2.792   7.071  1.00 42.22  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.252 2.606   8.266  1.00 42.63  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.371 3.911   6.426  1.00 42.28  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.127 4.959   7.110  1.00 42.75  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.200 6.031   7.703  1.00 41.46  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.588 7.200   7.784  1.00 42.33  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.154 5.586   6.177  1.00 45.38  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.270 4.652   5.770  1.00 52.03  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.617 3.699   6.477  1.00 54.54  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.884 4.924   4.625  1.00 53.86  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.978 5.645   8.117  1.00 39.01  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.034 6.605   8.688  1.00 36.86  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.512 6.186   10.065 1.00 35.01  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.460 5.000   10.401 1.00 34.65  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.816 6.798   7.759  1.00 36.25  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.139 7.364   6.401  1.00 36.03  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.771 8.591   6.271  1.00 36.73  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.792 6.683   5.243  1.00 36.69  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.090 9.110   5.023  1.00 37.57  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.098 7.193   3.989  1.00 37.85  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.744 8.411   3.882  1.00 38.87  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.049 8.924   2.645  1.00 41.16  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.075 7.181   10.834 1.00 33.14  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.435 7.001   12.125 1.00 31.84  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.118 7.798   12.030 1.00 29.89  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.136 8.978   11.710 1.00 29.65  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.337 7.516   13.272 1.00 32.70  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.612 7.722   14.608 1.00 34.46  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.563 8.086   15.736 1.00 36.29  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.011 9.100   16.635 1.00 37.65  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.708 8.893   17.915 1.00 38.62  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.845 7.685   18.450 1.00 36.67  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.234 9.885   18.661 1.00 38.09  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.981 7.139   12.230 1.00 28.30  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.681 7.794   12.146 1.00 26.42  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.137 7.964   13.537 1.00 25.39  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.916 6.973   14.219 1.00 26.04  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.694 7.001   11.259 1.00 25.95  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.371 7.747   11.133 1.00 25.96  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.295 6.712   9.880  1.00 25.33  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.928 9.202   13.981 1.00 23.89  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.380 9.469   15.317 1.00 23.16  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.187 10.456  15.233 1.00 22.84  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.968 11.087  14.184 1.00 22.45  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.466 10.055  16.271 1.00 23.33  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.683 9.158   16.372 1.00 23.93  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.860 11.459  15.852 1.00 23.58  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.443 10.604  16.360 1.00 22.68  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.393 11.593  16.550 1.00 23.15  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.119 12.935  16.596 1.00 24.24  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.072 13.098  17.352 1.00 24.97  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.677 11.391  17.896 1.00 23.76  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.752 10.199  17.955 1.00 26.56  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.127 9.100   18.394 1.00 29.51  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.516 10.389  17.544 1.00 24.66  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.696 13.884  15.783 1.00 24.27  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.305 15.203  15.715 1.00 24.40  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.326 15.901  17.074 1.00 25.80  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.352 16.503  17.411 1.00 26.77  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.570 16.065  14.685 1.00 23.37  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.320 17.300  14.231 1.00 22.33  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.303 18.221  13.593 1.00 21.55  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 18.855 19.434  12.988 1.00 21.29  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.087 20.569  13.643 1.00 21.18  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.952 20.624  14.968 1.00 19.44  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.527 21.637  12.992 1.00 19.43  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.243 15.779  17.879 1.00 25.76  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.183 16.438  19.197 1.00 26.94  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.148 15.826  20.247 1.00 28.85  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.457 16.469  21.261 1.00 29.32  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.729 16.509  19.725 1.00 27.23  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.179 15.235  20.290 1.00 27.88  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.502 14.322  19.491 1.00 28.60  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.198 14.770  21.564 1.00 29.16  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.146 13.329  20.296 1.00 29.50  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.546 13.548  21.553 1.00 29.81  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.661 14.612  19.985 1.00 29.57  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.615 13.941  20.884 1.00 30.48  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.052 13.893  20.318 1.00 32.16  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.901 13.222  20.904 1.00 32.46  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.153 12.487  21.180 1.00 30.38  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.824 12.326  21.927 1.00 31.10  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.509 10.853  22.191 1.00 30.87  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.807 13.146  23.225 1.00 31.36  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.314 14.521  19.162 1.00 32.63  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.640 14.492  18.553 1.00 33.94  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.700 15.152  19.430 1.00 35.34  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.406 16.116  20.125 1.00 35.29  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.602 15.157  17.179 1.00 34.15  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.935 14.632  19.391 1.00 36.91  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.077 15.136  20.177 1.00 38.67  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.852 16.253  19.413 1.00 40.63  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.485 16.584  18.281 1.00 41.20  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.011 13.949  20.492 1.00 40.35  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.507 13.456  19.254 1.00 41.29  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.326 12.838  21.270 1.00 41.05  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.923 16.832  20.015 1.00 41.51  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.748 17.806  19.311 1.00 42.77  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.494 17.110  18.170 1.00 42.49  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.695 17.709  17.126 1.00 42.17  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.764 18.444  20.267 1.00 45.40  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.164 19.384  21.262 1.00 50.71  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.517 20.535  20.862 1.00 53.70  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.193 19.345  22.617 1.00 53.19  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.160 21.153  21.976 1.00 54.76  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.547 20.478  23.059 1.00 54.76  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.912 15.848  18.367 1.00 42.35  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.617 15.104  17.329 1.00 42.93  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.747 14.846  16.121 1.00 41.39  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.254 14.870  15.005 1.00 41.95  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.161 13.782  17.848 1.00 46.26  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.394 13.392  17.088 1.00 52.43  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.233 14.243  16.792 1.00 54.30  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.528 12.116  16.732 1.00 53.97  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.443 14.586  16.335 1.00 39.48  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.478 14.366  15.257 1.00 37.49  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.384 15.616  14.390 1.00 36.06  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.409 15.516  13.175 1.00 35.75  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.100 14.025  15.833 1.00 37.83  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.005 12.635  16.408 1.00 40.29  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.566 11.715  15.808 1.00 41.35  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.371 12.475  17.469 1.00 41.26  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.321 16.796  15.014 1.00 35.24  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.261 18.086  14.318 1.00 34.65  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.607 18.491  13.672 1.00 35.34  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.612 19.204  12.676 1.00 35.78  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.769 19.174  15.288 1.00 33.55  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.276 19.169  15.456 1.00 32.34  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.565 18.604  16.471 1.00 32.66  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.321 19.786  14.590 1.00 31.63  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.222 18.821  16.282 1.00 32.70  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.042 19.517  15.118 1.00 32.25  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.415 20.482  13.382 1.00 31.70  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.876 19.978  14.514 1.00 32.04  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.255 20.897  12.762 1.00 32.00  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.006 20.644  13.324 1.00 31.97  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.738 18.060  14.241 1.00 35.79  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.051 18.345  13.652 1.00 37.02  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.321 17.457  12.425 1.00 38.05  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.107 17.822  11.558 1.00 39.35  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.160 18.164  14.689 1.00 37.25  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.688 16.290  12.354 1.00 37.27  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.825 15.364  11.238 1.00 36.43  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.443 15.188  10.591 1.00 34.96  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.043 14.074  10.286 1.00 34.65  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.358 14.036  11.767 1.00 37.67  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.756 14.163  12.331 1.00 41.27  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.608 14.832  11.756 1.00 43.60  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.024 13.519  13.456 1.00 40.58  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.702 16.298  10.412 1.00 33.48  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.350 16.294  9.876  1.00 32.06  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.313 15.964  8.395  1.00 31.89  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.081 16.538  7.635  1.00 32.63  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.713 17.667  10.136 1.00 31.69  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.343 17.949  9.476  1.00 32.05  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.254 17.160  10.153 1.00 32.27  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.030 19.436  9.455  1.00 31.28  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.398 15.061  7.971  1.00 30.93  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.211 14.710  6.562  1.00 30.32  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.861 15.278  6.066  1.00 28.70  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.769 15.839  4.978  1.00 29.04  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.283 13.184  6.345  1.00 31.59  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.887 12.820  4.920  1.00 32.60  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.677 12.642  6.675  1.00 31.84  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.821 15.141  6.885  1.00 26.45  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.479 15.601  6.565  1.00 24.31  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.679 15.684  7.831  1.00 22.85  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.809 14.839  8.708  1.00 21.98  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.793 14.609  5.601  1.00 23.71  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.315 14.804  5.388  1.00 23.82  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.713 15.729  4.589  1.00 24.42  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.254 14.054  6.000  1.00 23.21  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.345 15.596  4.658  1.00 24.29  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.038 14.567  5.506  1.00 23.78  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.216 12.990  6.907  1.00 23.15  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.801 14.021  5.856  1.00 24.13  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 18.990 12.491  7.294  1.00 23.65  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.802 12.987  6.750  1.00 23.88  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.808 16.681  7.911  1.00 22.04  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.877 16.786  9.031  1.00 20.81  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.537 17.329  8.552  1.00 19.56  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.482 18.088  7.584  1.00 18.68  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.446 17.546  10.255 1.00 20.99  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.067 18.900  9.962  1.00 22.62  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.110 20.055  9.726  1.00 24.95  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.418 20.902  8.854  1.00 28.76  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.059 20.118  10.405 1.00 20.77  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.455 16.882  9.201  1.00 19.14  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.113 17.364  8.909  1.00 18.64  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.341 17.523  10.210 1.00 17.71  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.895 16.541  10.784 1.00 17.60  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.368 16.460  7.938  1.00 20.15  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.203 17.157  7.275  1.00 25.63  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.589 18.037  7.916  1.00 26.03  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.905 16.829  6.124  1.00 30.01  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.181 18.771  10.666 1.00 17.23  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.471 19.085  11.893 0.50 18.17  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.469 19.060  11.903 0.50 17.65  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.013 18.600  11.797 1.00 18.79  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.485 18.060  12.758 1.00 19.02  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.547 20.589  12.154 0.50 19.90  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.549 20.549  12.238 0.50 17.92  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.683 21.016  13.190 0.50 23.37  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.706 21.317  11.395 0.50 19.04  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.385 18.733  10.593 1.00 19.93  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.994 18.297  10.370 1.00 20.27  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.797 16.772  10.506 1.00 19.42  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.669 16.308  10.701 1.00 19.33  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.454 18.810  9.039  1.00 22.48  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.775 17.966  7.944  1.00 26.70  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.884 16.004  10.395 1.00 17.67  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.846 14.555  10.580 1.00 16.70  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.445 14.113  11.937 1.00 16.70  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.345 12.939  12.269 1.00 16.86  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.625 13.866  9.452  1.00 16.07  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 12.985 14.048  8.084  1.00 15.58  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.789 13.363  6.984  1.00 15.34  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.716 11.911  7.136  1.00 16.61  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.854 11.039  6.138  1.00 18.65  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.065 11.464  4.900  1.00 16.45  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.770 9.737   6.372  1.00 19.14  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.078 15.026  12.707 1.00 16.60  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.819 14.691  13.933 1.00 16.58  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 15.991 13.746  13.537 1.00 17.44  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.351 12.870  14.329 1.00 16.61  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.928 14.019  15.019 1.00 16.93  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.607 13.798  16.370 1.00 19.94  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.469 14.614  16.737 1.00 18.50  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.261 12.790  17.067 1.00 22.10  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.596 13.916  12.330 1.00 18.00  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.734 13.059  11.942 1.00 19.53  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.016 13.824  11.736 1.00 21.15  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.013 14.944  11.231 1.00 21.81  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.460 12.251  10.645 1.00 19.61  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.512 11.042  10.717 1.00 20.62  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.584 10.238  9.432  1.00 21.03  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.824 10.125  11.927 1.00 20.83  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.126 13.181  12.050 1.00 21.91  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.444 13.727  11.794 1.00 23.63  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.344 12.529  11.449 1.00 25.57  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.282 11.486  12.097 1.00 26.05  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 21.996 14.511  13.017 1.00 24.10  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.340 15.231  12.803 1.00 25.62  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.420 16.497  13.611 1.00 26.18  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.526 14.346  13.126 1.00 26.83  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.158 12.672  10.415 1.00 26.64  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.087 11.646  10.008 1.00 28.13  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.471 12.249  10.083 1.00 29.85  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.734 13.304  9.505  1.00 29.61  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.789 11.128  8.590  1.00 28.69  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.848 10.110  8.158  1.00 29.36  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.385 10.538  8.508  1.00 28.75  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.337 11.598  10.827 1.00 31.33  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.720 11.997  10.973 1.00 33.71  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.629 10.908  10.362 1.00 36.60  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.202 9.766   10.173 1.00 36.01  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.050 12.219  12.442 1.00 34.58  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.043 10.999  13.166 1.00 36.52  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 29.873 11.269  10.039 1.00 39.36  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 30.814 10.330  9.441  1.00 42.62  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.645 9.621   10.494 1.00 46.31  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.953 10.190  11.536 1.00 46.62  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.737 11.051  8.469  1.00 43.44  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.556 11.953  9.189  1.00 45.90  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.023 8.381   10.215 1.00 49.01  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.855 7.602   11.131 1.00 52.01  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.112 7.124   10.406 1.00 55.03  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.140 7.085   9.175  1.00 55.56  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.079 6.385   11.711 1.00 53.30  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.976 5.351   10.730 1.00 54.81  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.719 6.745   12.252 1.00 53.05  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.132 6.726   11.160 1.00 56.93  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.339 6.157   10.574 1.00 59.33  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.128 4.635   10.428 1.00 61.14  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.436 4.056   9.383  1.00 61.85  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.557 6.497   11.439 1.00 61.33  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.270 6.138   12.792 1.00 62.81  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.924 7.970   11.370 1.00 61.87  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.576 3.998   11.475 1.00 61.54  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.320 2.562   11.504 1.00 62.20  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.151 2.147   10.601 1.00 62.79  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.307 2.981   10.269 1.00 63.17  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.062 2.125   12.936 1.00 62.41  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.098 0.857   10.208 1.00 62.93  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.034 0.337   9.344  1.00 63.45  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.768 -0.026  10.118 1.00 63.21  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 31.835 -0.405  11.286 1.00 63.74  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.520 -0.872  8.527  1.00 65.43  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.950 -0.910  7.113  1.00 69.23  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.517 0.217   6.284  1.00 74.39  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.721 0.505   6.331  1.00 76.39  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.666 0.890   5.511  1.00 74.67  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.629 0.072   9.444  1.00 62.09  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.324 -0.219  10.016 1.00 61.23  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.720 -1.495  9.475  1.00 59.76  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 28.691 -1.726  8.267  1.00 59.91  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.203 -2.308  10.369 1.00 58.29  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.649 -3.604  10.022 1.00 57.45  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.117 -3.684  10.103 1.00 54.52  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.576 -4.775  10.306 1.00 54.96  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.309 -4.679  10.878 1.00 60.02  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 28.516 -4.223  12.623 1.00 67.32  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.419 -2.553  9.917  1.00 51.31  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.963 -2.549  9.968  1.00 49.13  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.323 -2.554  8.600  1.00 46.40  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.554 -1.653  7.792  1.00 46.94  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.417 -1.377  10.795 1.00 50.59  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.255 -1.718  12.251 1.00 55.38  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.922 -2.885  12.552 1.00 57.12  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.457 -0.825  13.091 1.00 57.14  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.483 -3.547  8.360  1.00 43.45  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.738 -3.673  7.120  1.00 41.17  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.534 -2.751  7.219  1.00 38.09  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.770 -2.862  8.178  1.00 38.06  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.267 -5.126  6.966  1.00 42.66  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.404 -5.956  6.738  1.00 44.19  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.282 -5.304  5.830  1.00 42.87  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.364 -1.837  6.259  1.00 35.04  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.194 -0.968  6.254  1.00 32.52  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.139 -1.643  5.385  1.00 31.38  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.456 -2.080  4.280  1.00 31.84  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.518 0.455   5.728  1.00 31.54  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.736 1.082   6.463  1.00 31.39  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.268 1.362   5.766  1.00 30.76  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.488 1.349   7.936  1.00 31.70  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.904 -1.749  5.875  1.00 29.88  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.803 -2.329  5.101  1.00 29.24  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.409 -1.387  3.965  1.00 28.17  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.439 -0.192  4.127  1.00 27.04  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.597 -2.548  5.994  1.00 28.82  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.036 -1.933  2.821  1.00 28.94  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.573 -1.162  1.683  1.00 28.87  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.229 -1.835  1.338  1.00 28.74  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.202 -2.817  0.603  1.00 29.58  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.613 -1.247  0.563  1.00 30.70  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.010 -0.707  0.939  1.00 32.24  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.050 0.766   1.357  1.00 32.74  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.427 1.205   1.557  1.00 32.22  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.787 2.333   2.163  1.00 32.73  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.869 3.151   2.663  1.00 30.39  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.070 2.640   2.297  1.00 32.56  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.132 -1.361  1.953  1.00 28.13  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.831 -2.016  1.878  1.00 29.11  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.685  -1.073  2.304  1.00 30.73  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.907  0.072   2.654  1.00 30.80  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.851 -3.260  2.779  1.00 29.72  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 10.952 -2.879  4.561  1.00 33.86  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.450  -1.596  2.314  1.00 32.26  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.252  -0.890  2.749  1.00 33.57  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.588  -1.644  3.923  1.00 33.70  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.371  -1.608  4.055  1.00 34.85  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.271  -0.750  1.583  1.00 36.61  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.702  -2.077  1.114  1.00 46.52  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.441  -3.099  1.161  1.00 49.09  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.510  -2.110  0.744  1.00 50.23  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.381  -2.335  4.753  1.00 32.32  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.898  -3.079  5.903  1.00 31.06  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.171  -2.239  6.883  1.00 28.96  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.573  -1.127  7.161  1.00 29.39  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.048  -3.799  6.581  1.00 31.81  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.330  -5.446  5.932  1.00 36.00  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.121  -2.781  7.427  1.00 27.16  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.357  -2.133  8.474  1.00 25.98  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.326  -2.945  9.747  1.00 24.09  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.443  -2.717  10.562 1.00 24.07  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 2.936  -1.821  8.012  1.00 27.55  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.863  -0.572  7.176  1.00 31.59  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.440  -0.225  6.833  1.00 34.55  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.069  -0.166  5.665  1.00 36.35  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.616  0.023   7.846  1.00 33.46  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.216  -3.941  9.901  1.00 22.83  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.350  -4.754  11.110 1.00 22.39  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.843  -4.887  11.369 1.00 21.34  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.641  -5.020  10.442 1.00 21.73  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.755  -6.164  10.952 1.00 24.65  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.434  -6.810  9.871  1.00 26.30  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.224  -6.159  10.714 1.00 24.90  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.201  -4.910  12.625 1.00 20.21  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.591  -5.000  13.022 1.00 20.01  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.742  -5.260  14.496 1.00 19.26  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.786  -5.659  15.161 1.00 18.93  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.962  -5.042  14.991 1.00 18.43  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.386 -5.236  16.368 1.00 17.30  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.241 -4.019  16.751 1.00 17.09  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.201 -3.710  16.042 1.00 16.37  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.225 -6.554  16.467 1.00 17.50  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.851 -6.721  17.847 1.00 17.96  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.377 -7.774  16.122 1.00 18.15  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.932 -3.361  17.866 1.00 17.57  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.757 -2.251  18.341 1.00 18.15  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.340 -2.498  19.740 1.00 18.90  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.739 -3.205  20.535 1.00 19.33  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.999 -0.915  18.289 1.00 17.93  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.011 -0.691  19.415 1.00 18.47  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.763  -1.295  19.400 1.00 19.36  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.301 0.173   20.460 1.00 19.90  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.839  -1.070  20.412 1.00 20.68  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.388  0.400   21.487 1.00 21.08  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.148  -0.217  21.450 1.00 21.85  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.207  0.014   22.422 1.00 23.24  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.494 -1.894  20.046 1.00 19.25  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.099 -2.036  21.361 1.00 21.38  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.642 -0.867  22.268 1.00 21.46  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.712 0.297   21.861 1.00 20.82  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.637 -2.133  21.273 1.00 22.30  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.249 -2.295  22.642 1.00 23.44  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.019 -3.436  23.393 1.00 23.94  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.966 -1.261  23.231 1.00 24.76  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.520 -3.564  24.676 1.00 25.58  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.459 -1.372  24.525 1.00 25.64  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.236 -2.527  25.243 1.00 26.90  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.706 -2.651  26.522 1.00 30.08  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.082 -1.196  23.450 1.00 21.73  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.562 -0.209  24.398 1.00 22.67  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.447 -0.267  25.628 1.00 24.45  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.276 -1.157  26.463 1.00 23.44  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.105 -0.531  24.731 1.00 22.97  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.398 0.471   26.060 1.00 26.60  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.428 0.654   25.727 1.00 26.38  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.362 0.622   26.839 1.00 28.45  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.722 0.909   28.178 1.00 29.74  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.264 0.460   29.176 1.00 30.93  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.576 1.515   26.601 1.00 31.62  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.291 2.897   26.676 1.00 36.16  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.550 1.563   28.226 1.00 30.29  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.838 1.783   29.497 1.00 31.57  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.266 0.490   30.090 1.00 32.16  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.034 0.406   31.304 1.00 32.49  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.753 2.845   29.353 1.00 33.92  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.834 2.577   28.304 1.00 35.83  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.094 -0.534  29.254 1.00 31.48  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.671 -1.840  29.721 1.00 31.99  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.775 -2.891  29.596 1.00 32.58  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.551 -4.030  30.000 1.00 33.61  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.456 -2.310  28.911 1.00 32.48  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.185  -1.543  29.216 1.00 34.29  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.623  -1.885  30.590 1.00 36.43  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.472  -1.042  30.883 1.00 38.69  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.544  0.170   31.427 1.00 40.22  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.718  0.670   31.802 1.00 39.31  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.442  0.887   31.613 1.00 40.31  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.922 -2.560  28.965 1.00 32.15  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.004 -3.493  28.638 1.00 32.24  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.457 -4.728  27.911 1.00 31.01  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.848 -5.867  28.196 1.00 31.53  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.847 -3.849  29.862 1.00 35.55  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.582 -2.648  30.467 1.00 40.18  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.965 -3.066  30.895 1.00 45.56  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.223 -2.763  32.300 1.00 51.55  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.904 -3.561  33.317 1.00 56.64  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.274 -4.713  33.098 1.00 58.05  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.193 -3.204  34.561 1.00 56.20  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.501 -4.480  26.993 1.00 28.80  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.786 -5.486  26.225 1.00 27.56  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.604 -5.033  24.766 1.00 25.77  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.590 -3.830  24.485 1.00 25.33  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.381 -5.700  26.825 1.00 29.69  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.191 -7.030  27.548 1.00 35.47  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.737  -7.213  27.978 1.00 40.75  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.536  -8.425  28.854 1.00 45.68  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.672  -8.100  30.308 1.00 47.10  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.405 -6.022  23.867 1.00 24.41  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.106 -5.874  22.440 1.00 23.48  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.620 -6.204  22.285 1.00 22.27  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.109 -7.170  22.889 1.00 22.99  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.920 -6.866  21.594 1.00 23.75  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.393 -6.593  21.550 1.00 24.24  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 14.961 -5.856  20.529 1.00 25.72  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.373 -7.012  22.375 1.00 24.79  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.258 -5.840  20.775 1.00 25.48  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.550 -6.513  21.879 1.00 25.37  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.920  -5.366  21.553 1.00 20.21  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.494  -5.538  21.369 1.00 20.17  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.141  -5.584  19.904 1.00 18.76  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.541  -4.703  19.155 1.00 17.19  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.726  -4.358  21.992 1.00 20.47  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.799  -4.281  23.496 1.00 22.16  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.137  -5.205  24.289 1.00 24.06  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.437  -3.225  24.124 1.00 23.54  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.159  -5.114  25.673 1.00 25.44  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.430  -3.098  25.507 1.00 25.21  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.805  -4.054  26.279 1.00 26.78  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.835  -3.970  27.649 1.00 29.41  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.315  -6.569  19.499 1.00 19.59  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.817  -6.564  18.113 1.00 19.51  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.713  -5.498  17.949 1.00 20.71  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.875  -5.366  18.845 1.00 21.77  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.281  -7.981  17.922 1.00 20.42  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.922  -8.460  19.312 1.00 21.09  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.752  -7.678  20.310 1.00 19.18  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.748  -4.695  16.869 1.00 20.61  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.766  -3.635  16.617 1.00 21.80  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.234  -3.565  15.183 1.00 22.29  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.919  -3.945  14.240 1.00 22.45  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.325  -2.231  16.985 1.00 23.07  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.356  -2.015  18.486 1.00 23.71  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.681  -1.979  16.333 1.00 23.95  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.032  -3.000  15.012 1.00 22.56  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.489  -2.667  13.695 1.00 23.16  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.659  -1.165  13.629 1.00 23.14  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.354  -0.473  14.614 1.00 24.04  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.003  -3.002  13.585 1.00 25.23  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.810  -4.402  13.471 1.00 28.78  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.161  -0.647  12.510 1.00 21.78  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.416  0.782   12.436 1.00 21.69  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.895  1.410   11.157 1.00 24.11  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.679  0.713   10.158 1.00 25.44  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.908  1.083   12.693 1.00 19.76  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.919  0.370   11.824 1.00 17.76  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.478  -0.830  12.225 1.00 17.14  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.314  0.906   10.607 1.00 17.71  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.403  -1.486  11.425 1.00 17.65  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.291  0.280   9.837  1.00 17.66  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.825  -0.916  10.245 1.00 17.28  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.601  2.714   11.213 1.00 24.53  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.020  3.378   10.060 1.00 26.25  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.077  3.713   9.006  1.00 26.92  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.264  3.485   9.230  1.00 26.60  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.227  4.607   10.498 1.00 27.71  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.050  5.491   11.240 1.00 29.47  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.641  4.208   7.840  1.00 27.27  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.546  4.630   6.771  1.00 28.85  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.220  5.961   7.155  1.00 28.99  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.630  6.722   7.918  1.00 28.91  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.757  4.763   5.453  1.00 31.63  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.170  3.434   5.026  1.00 38.72  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.309  3.210   3.523  1.00 47.18  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.503  1.739   3.216  1.00 53.06  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.990  1.535   1.824  1.00 56.76  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.451  6.258   6.691  1.00 29.77  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.090  7.531   7.082  1.00 30.94  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.255  8.725   6.643  1.00 32.24  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.833  8.791   5.476  1.00 32.49  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.445  7.486   6.371  1.00 31.64  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.682  6.041   6.092  1.00 31.73  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.326  5.476   5.801  1.00 29.55  ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.954  9.637   7.587  1.00 32.36  ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.112  10.784  7.260  1.00 33.35  ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.430  12.026  8.122  1.00 33.81  ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.352  12.000  8.940  1.00 33.44  ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.638  10.381  7.369  1.00 35.74  ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.319  9.901   8.666  1.00 38.51  ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.703  13.131  7.884  1.00 34.06  ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.834  14.378  8.620  1.00 35.32  ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.922  14.252  9.825  1.00 36.72  ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.713  14.202  9.635  1.00 37.41  ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.290  15.538  7.767  1.00 35.62  ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.236  16.249  6.845  1.00 37.45  ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.469  17.224  5.942  1.00 38.55  ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.309  16.967  7.625  1.00 38.06  ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.467  14.234  11.048 1.00 36.87  ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.660  14.167  12.264 1.00 37.78  ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.059  15.350  13.165 1.00 39.86  ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.246  15.599  13.328 1.00 39.59  ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.882  12.785  12.958 1.00 37.73  ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.085  11.668  12.265 1.00 38.10  ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.601  12.812  14.452 1.00 37.79  ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.912  10.503  11.930 1.00 38.98  ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.089  16.086  13.732 1.00 41.60  ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.409  17.201  14.629 1.00 43.57  ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.036  16.696  15.944 1.00 43.57  ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.614  15.691  16.504 1.00 43.28  ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.173  18.087  14.869 1.00 45.00  ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.225  19.052  16.033 1.00 46.90  ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.795  20.300  15.892 1.00 48.22  ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.652  18.727  17.251 1.00 48.29  ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 1.804  21.200  16.949 1.00 49.25  ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 0.656  19.634  18.304 1.00 49.26  ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.233  20.863  18.145 1.00 49.04  ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.095  17.361  16.385 1.00 43.75  ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.809  17.021  17.598 1.00 44.43  ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.829  18.262  18.484 1.00 45.92  ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.241  19.343  18.044 1.00 46.35  ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.241  16.498  17.296 1.00 44.29  ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.015  16.248  18.584 1.00 44.19  ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.199  15.229  16.449 1.00 44.48  ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.347  18.118  19.720 1.00 46.58  ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.286  19.213  20.681 1.00 47.37  ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 5.668  19.766  21.029 1.00 47.14  ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.675  19.073  20.888 1.00 47.05  ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 3.565  18.754  21.947 1.00 50.95  ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.174  18.222  21.672 1.00 58.38  ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.268  18.233  22.885 1.00 67.53  ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.201  19.286  23.560 1.00 69.46  ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.616  17.197  23.154 1.00 70.71  ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 5.707  21.003  21.505 1.00 46.75  ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 6.932  21.697  21.883 1.00 47.23  ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 7.810  20.914  22.864 1.00 47.12  ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.301  20.191  23.713 1.00 47.75  ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 6.580  23.049  22.491 1.00 47.38  ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.124  21.097  22.771 1.00 46.42  ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.092 20.471  23.670 1.00 46.40  ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.284 21.424  23.860 1.00 46.54  ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.349 22.464  23.187 1.00 46.62  ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 10.564 19.130  23.100 1.00 47.25  ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.491 19.288  22.038 1.00 48.88  ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.249 21.071  24.740 1.00 46.19  ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.435 21.918  24.897 1.00 46.19  ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.358 21.903  23.656 1.00 44.18  ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.328 22.653  23.606 1.00 44.40  ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.204 21.598  26.187 1.00 50.49  ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 15.113 20.382  26.113 1.00 58.11  ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 16.510 20.713  26.600 1.00 65.98  ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 17.129 21.627  26.007 1.00 66.83  ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 16.983 20.079  27.573 1.00 67.69  ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.031 21.087  22.639 1.00 42.37  ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 14.830 20.959  21.428 1.00 40.11  ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.125 21.557  20.222 1.00 38.47  ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.783 22.114  19.348 1.00 38.40  ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.133 19.484  21.137 1.00 39.39  ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.567 18.677  22.339 1.00 39.35  ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.883 18.698  22.777 1.00 40.01  ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.673 17.857  23.007 1.00 39.67  ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.288 17.958  23.879 1.00 40.45  ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.063 17.120  24.115 1.00 40.32  ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.373 17.170  24.548 1.00 41.26  ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.762 16.426  25.637 1.00 42.95  ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.800 21.414  20.146 1.00 37.02  ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.054 21.895  18.983 1.00 36.13  ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.800 22.671  19.356 1.00 36.58  ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.105 22.274  20.287 1.00 36.40  ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.580 20.678  18.145 1.00 34.75  ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.672 19.776  17.614 1.00 33.20  ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.823 18.480  18.086 1.00 32.53  ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.513 20.197  16.592 1.00 32.83  ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.793 17.630  17.567 1.00 32.18  ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.491 19.359  16.074 1.00 32.73  ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.617 18.071  16.552 1.00 32.39  ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.625 17.274  16.072 1.00 32.10  ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.387 23.659  18.541 1.00 36.88  ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.068  24.279  18.781 1.00 37.52  ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.913  23.359  18.291 1.00 38.38  ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.171  22.283  17.749 1.00 38.83  ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.149  25.605  18.005 1.00 37.73  ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.202 25.388  16.957 1.00 37.79  ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.047 24.197  17.331 1.00 36.19  ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.648  23.771  18.465 1.00 38.65  ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.507  22.969  17.993 1.00 39.11  ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.550  22.914  16.455 1.00 37.70  ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.417  23.953  15.817 1.00 38.36  ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.193  23.599  18.466 1.00 39.86  ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.757  21.719  15.862 1.00 35.40  ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.912  21.596  14.404 1.00 33.67  ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.365  20.259  13.849 1.00 32.65  ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.064  19.376  14.639 1.00 32.65  ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.427  21.669  14.095 1.00 33.26  ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.179  20.424  14.605 1.00 33.00  ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.664  20.615  14.842 1.00 32.12  ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.481 19.473  14.408 1.00 29.65  ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.562 18.315  15.058 1.00 28.25  ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.344 17.348  14.606 1.00 24.99  ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.851  18.115  16.164 1.00 27.41  ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.308  20.073  12.497 1.00 31.52  ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 4.946  18.756  11.954 1.00 30.90  ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.281  18.037  11.651 1.00 28.56  ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.109  18.572  10.928 1.00 28.67  ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.169  18.842  10.638 1.00 31.93  ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.762  19.404  10.686 1.00 34.71  ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.661  18.599  10.408 1.00 36.27  ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.546  20.772  10.792 1.00 36.43  ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.379  19.134  10.311 1.00 37.74  ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.272  21.314  10.709 1.00 37.91  ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.187  20.493  10.478 1.00 39.67  ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -1.068 21.073  10.367 1.00 42.76  ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.490  16.848  12.192 1.00 26.25  ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.694  16.065  11.927 1.00 23.94  ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.410  15.162  10.731 1.00 22.76  ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.422  14.437  10.727 1.00 23.25  ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.089  15.223  13.162 1.00 23.24  ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.260  14.263  12.914 1.00 21.36  ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 9.972  13.879  14.199 1.00 22.60  ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.112 14.686  15.124 1.00 24.63  ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.473 12.656  14.274 1.00 19.28  ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.246  15.221  9.713  1.00 21.57  ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.065  14.399  8.516  1.00 21.40  ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.780  13.054  8.646  1.00 21.10  ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.663  12.883  9.521  1.00 20.68  ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.542  15.151  7.271  1.00 22.29  ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 9.938  15.406  7.306  1.00 24.78  ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.379  12.093  7.792  1.00 20.53  ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 8.970  10.752  7.731  1.00 20.47  ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.837  9.981   9.044  1.00 20.13  ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.690  9.161   9.372  1.00 19.64  ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.428 10.845  7.280  1.00 20.39  ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.561 11.394  5.890  1.00 22.76  ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.584 10.557  4.785  1.00 25.12  ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.643 12.676  5.468  1.00 23.16  ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.710 11.357  3.729  1.00 25.79  ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.742 12.637  4.091  1.00 24.56  ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.759  10.246  9.792  1.00 20.25  ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.549  9.645   11.112 1.00 20.41  ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.522  8.537   11.044 1.00 19.99  ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.566  8.653   10.292 1.00 19.03  ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.087  10.748  12.086 1.00 20.53  ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.922  10.335  13.528 1.00 22.05  ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.245  9.991   14.118 1.00 21.52  ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.251  11.445  14.332 1.00 23.50  ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.721  7.441   11.814 1.00 20.31  ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.788  6.310   11.786 1.00 21.10  ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.357  5.998   13.173 1.00 22.20  ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.214  5.759   14.012 1.00 23.05  ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.459  5.065   11.207 1.00 21.22  ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.005  5.291   9.804  1.00 22.38  ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.026  3.924   9.256  1.00 24.50  ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.333  4.021   10.336 1.00 17.50  ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.046  5.935   13.422 1.00 21.96  ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.567  5.627   14.761 1.00 22.76  ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.171  4.160   14.938 1.00 23.08  ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.704  3.526   13.999 1.00 23.25  ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.376  6.541   15.128 1.00 23.26  ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.685  8.024   15.301 1.00 25.02  ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.409  8.819   15.548 1.00 25.05  ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.679  8.257   16.408 1.00 25.34  ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.302  3.656   16.170 1.00 23.03  ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.910  2.307   16.587 1.00 23.98  ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.294  2.385   17.966 1.00 24.63  ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.605  3.293   18.728 1.00 23.55  ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.132  1.392   16.648 1.00 24.13  ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.455  1.401   18.318 1.00 26.31  ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.912  1.315   19.665 1.00 28.03  ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 1.939  0.493   20.436 1.00 28.56  ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.257  -0.625  20.045 1.00 28.97  ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.496 0.680   19.722 1.00 29.33  ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.964 0.541   21.164 1.00 29.44  ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.492 1.513   18.924 1.00 30.19  ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.518  1.099   21.451 1.00 28.31  ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.556  0.475   22.251 1.00 28.92  ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.115  1.420   23.299 1.00 29.10  ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 3.904  2.631   23.226 1.00 29.93  ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.830  0.872   24.288 1.00 28.27  ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.431  1.686   25.326 1.00 28.64  ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.672  2.489   24.884 1.00 28.84  ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.587  1.956   24.274 1.00 28.13  ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.760  0.855   26.579 1.00 29.27  ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.365  1.689   27.661 1.00 31.61  ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.632  2.655   28.307 1.00 34.01  ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.648  1.759   28.080 1.00 33.22  ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.478  3.265   29.124 1.00 34.91  ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.703  2.754   29.025 1.00 34.99  ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.730  3.742   25.307 1.00 30.36  ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 7.869  4.612   25.088 1.00 32.68  ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 7.866  5.738   26.104 1.00 35.27  ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.809  6.249   26.459 1.00 36.38  ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 7.821  5.219   23.696 1.00 33.95  ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.585  5.880   23.516 1.00 36.24  ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.044  6.137   26.560 1.00 36.22  ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.209  7.282   27.446 1.00 37.77  ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.525 8.026   27.113 1.00 39.07  ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.352 7.480   26.374 1.00 38.39  ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.048  6.915   28.929 1.00 40.02  ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 10.056 5.913   29.427 1.00 43.22  ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 9.751  5.485   30.845 1.00 44.88  ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.032 6.282   31.758 1.00 48.48  ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.213  4.376   31.045 1.00 42.19  ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.737 9.291   27.573 1.00 40.22  ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 11.994 9.992   27.223 1.00 40.55  ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.165 9.177   27.758 1.00 39.96  ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.127 8.728   28.916 1.00 41.34  ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.861 11.350  27.922 1.00 41.42  ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.406 11.503  28.198 1.00 41.81  ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.884  10.126  28.439 1.00 39.91  ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.114 8.905   26.876 1.00 37.30  ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.230 8.002   27.133 1.00 35.26  ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.207 6.817   26.168 1.00 33.39  ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.209 6.112   26.007 1.00 33.41  ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.058 6.587   25.496 1.00 31.38  ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.912 5.515   24.530 1.00 29.85  ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.346 5.916   23.120 1.00 28.96  ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.645 5.019   22.326 1.00 29.00  ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.486 4.970   24.534 1.00 29.97  ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.192 4.104   25.736 1.00 31.01  ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.137 3.490   26.270 1.00 31.19  ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.020 4.054   26.155 1.00 30.75  ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.437 7.251   22.809 1.00 27.74  ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.902 7.769   21.499 1.00 27.37  ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.244 7.113   21.147 1.00 26.05  ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.107 7.047   22.006 1.00 26.12  ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.026 9.293   21.512 1.00 28.59  ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.444 10.176  21.591 1.00 34.36  ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.368 6.562   19.951 1.00 24.68  ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.583 5.851   19.566 1.00 24.06  ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.408 4.344   19.482 1.00 23.72  ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.217 3.646   18.865 1.00 24.58  ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.324 3.825   20.056 1.00 22.18  ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.017 2.401   19.968 1.00 20.41  ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.699 2.061   18.530 1.00 17.99  ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 14.897 2.738   17.897 1.00 16.19  ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.393 1.074   17.993 1.00 17.24  ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.232 0.667   16.623 1.00 17.22  ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.908 -0.108  16.414 1.00 16.63  ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.517 -0.939  17.247 1.00 16.67  ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.532 -0.151  16.244 1.00 18.68  ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.684 0.813   15.875 1.00 19.19  ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.290 -1.193  15.137 1.00 19.60  ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.142 0.158   15.737 1.00 20.04  ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.205 0.203   15.321 1.00 15.76  ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.048 -0.542  14.859 1.00 15.65  ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.562 -1.400  13.650 1.00 17.49  ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.263 -0.907  12.761 1.00 16.80  ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 11.908 0.380   14.447 1.00 14.24  ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.782 -0.210  13.571 1.00 14.23  ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 9.806  -1.054  14.389 1.00 14.19  ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.962  0.914   12.968 1.00 15.13  ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.254 -2.683  13.659 1.00 18.67  ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.733 -3.606  12.647 1.00 20.10  ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.613 -4.422  12.079 1.00 20.62  ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.693 -4.787  12.793 1.00 20.70  ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.696 -4.617  13.316 1.00 23.14  ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.173 -4.379  13.113 1.00 29.80  ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 16.976 -5.667  13.336 1.00 36.16  ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.322 -5.535  12.768 1.00 42.62  ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.380 -5.089  13.444 1.00 46.71  ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.274 -4.785  14.733 1.00 46.96  ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 20.554 -4.959  12.841 1.00 47.42  ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.761 -4.845  10.828 1.00 21.20  ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.847 -5.794  10.222 1.00 21.96  ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.740 -6.946  9.735  1.00 23.44  ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.935 -6.951  10.050 1.00 23.31  ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.098 -5.139  9.069  1.00 21.90  ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.189 -4.547  7.773  1.00 24.42  ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.193 -7.910  8.949  1.00 24.47  ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.015 -8.988  8.413  1.00 26.40  ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.095 -8.463  7.467  1.00 26.87  ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.117 -9.119  7.311  1.00 27.87  ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.153 -9.994  7.648  1.00 30.29  ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.283 -9.363  6.569  1.00 36.37  ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.366 -10.375 5.930  1.00 42.71  ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.134  -10.248 5.969  1.00 44.40  ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.953 -11.402 5.323  1.00 44.53  ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.874 -7.309  6.817  1.00 25.58  ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.841 -6.776  5.859  1.00 24.44  ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 15.984 -6.014  6.482  1.00 23.28  ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 16.932 -5.690  5.756  1.00 24.25  ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.193 -5.913  4.743  1.00 24.43  ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.710 -6.053  4.631  1.00 24.61  ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.843 -5.387  5.521  1.00 22.84  ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 11.980 -6.771  3.741  1.00 26.64  ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.661 -5.809  5.226  1.00 25.31  ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 10.666 -6.601  4.101  1.00 28.17  ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.898 -5.719  7.781  1.00 20.83  ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 16.906 -4.964  8.499  1.00 19.59  ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.363 -3.730  9.207  1.00 18.57  ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.183 -3.673  9.562  1.00 19.45  ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.225 -2.731  9.407  1.00 17.31  ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.914 -1.488  10.125 1.00 18.12  ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.875 -0.644  9.374  1.00 17.99  ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.081 -0.351  8.198  1.00 18.16  ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.206 -0.666  10.396 1.00 18.82  ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.861 0.673   11.049 1.00 19.92  ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.184 -1.454  11.279 1.00 18.38  ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.737 -0.339  10.021 1.00 16.85  ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.647 0.470   9.477  1.00 16.75  ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.849 1.944   9.918  1.00 18.12  ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.790 2.864   9.102  1.00 18.94  ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.265 -0.069  9.946  1.00 16.71  ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.131 0.854   9.526  1.00 16.83  ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.028 -1.483  9.443  1.00 16.96  ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.060 2.143   11.213 1.00 17.37  ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.244 3.475   11.749 1.00 17.71  ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.601 3.471   13.212 1.00 16.70  ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.028 2.449   13.741 1.00 16.83  ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.453 4.625   13.868 1.00 16.18  ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 14.792 4.782   15.284 1.00 15.71  ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.720 5.546   16.024 1.00 15.42  ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.140 6.495   15.484 1.00 13.88  ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.135 5.530   15.492 1.00 16.80  ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.263 6.752   14.577 1.00 17.42  ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.337 4.613   15.390 1.00 17.58  ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.143 7.789   15.102 1.00 19.07  ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.571 5.259   17.332 1.00 15.22  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.591 5.939   18.169 1.00 16.52  ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.893 7.431   18.188 1.00 18.45  ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.064 7.823   18.264 1.00 18.53  ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.556 5.348   19.599 1.00 17.28  ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.628 6.170   20.495 1.00 18.06  ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.105 3.892   19.560 1.00 18.02  ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.859 8.248   17.990 1.00 19.40  ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.030 9.675   17.922 1.00 21.10  ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.021 10.402  18.799 1.00 23.70  ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.347 11.446  19.353 1.00 23.68  ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 11.919 10.126  16.473 1.00 22.12  ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.052 11.531  16.380 1.00 24.56  ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.775  9.882   18.885 1.00 25.82  ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.703  10.459  19.710 1.00 28.21  ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.976  9.330   20.516 1.00 30.66  ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.313  8.156   20.398 1.00 30.74  ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.704  11.322  18.852 1.00 29.28  ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.877  10.452  18.092 1.00 29.94  ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.381  12.354  17.953 1.00 30.13  ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.983  9.698   21.311 1.00 32.36  ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.174  8.754   22.049 1.00 35.03  ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.247  9.446   23.021 1.00 37.63  ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.260  10.676  23.147 1.00 38.05  ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.469  8.652   23.733 1.00 39.12  ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.541  9.177   24.722 1.00 40.98  ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.121  8.709   24.498 1.00 42.56  ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.663  8.666   23.359 1.00 43.03  ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.436  8.341   25.589 1.00 43.24  ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.049  7.867   25.649 1.00 44.19  ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.176 6.528   24.956 1.00 43.00  ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.212 6.317   24.334 1.00 44.16  ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.919 8.924   25.131 1.00 47.34  ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.811 10.236  25.866 1.00 52.46  ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.925 10.281  27.097 1.00 54.55  ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.588 11.323  25.129 1.00 52.61  ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.774  5.620   25.099 1.00 40.46  ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.686  4.311   24.468 1.00 38.46  ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.113  4.306   23.013 1.00 35.99  ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.939  3.306   22.330 1.00 35.58  ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.673  5.415   22.518 1.00 34.18  ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.110  5.521   21.131 1.00 33.09  ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.606  5.712   21.069 1.00 31.19  ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.131  6.495   21.839 1.00 31.90  ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.433  6.750   20.482 1.00 33.55  ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? -0.074 6.670   20.446 1.00 35.49  ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.692 8.001   20.105 1.00 36.39  ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.513 5.584   19.498 1.00 36.77  ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.298  5.032   20.141 1.00 28.56  ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.726  5.217   19.928 1.00 26.25  ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.927  5.686   18.484 1.00 25.16  ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.302  5.143   17.576 1.00 25.28  ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.588  3.976   20.313 1.00 25.90  ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.048  2.683   19.707 1.00 25.83  ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.066  4.182   19.978 1.00 25.88  ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.726  6.737   18.292 1.00 23.71  ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.007  7.278   16.968 1.00 23.06  ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.416  6.982   16.530 1.00 21.79  ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.346  7.163   17.306 1.00 21.79  ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.587  6.553   15.269 1.00 19.96  ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 9.874  6.156   14.705 1.00 17.31  ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.286 6.998   13.489 1.00 16.19  ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.528  7.127   12.540 1.00 15.53  ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.822  4.673   14.293 1.00 15.90  ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.394  3.698   15.370 1.00 15.15  ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.321 3.142   16.232 1.00 15.09  ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.089  3.237   15.432 1.00 15.75  ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.943  2.188   17.170 1.00 15.23  ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.714  2.285   16.372 1.00 15.63  ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.643  1.775   17.245 1.00 14.87  ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.516 7.510   13.497 1.00 15.43  ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.042 8.272   12.382 1.00 16.07  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.484 7.275   11.324 1.00 17.64  ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.433 6.531   11.559 1.00 17.97  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.238 9.096   12.838 1.00 15.97  ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.807 7.242   10.177 1.00 18.37  ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.142 6.314   9.118  1.00 20.01  ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.507 6.644   8.493  1.00 21.67  ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.899 7.813   8.480  1.00 23.19  ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.031 6.334   8.066  1.00 21.97  ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.221 5.337   6.956  1.00 24.46  ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.318 4.129   7.253  1.00 20.55  ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.305 5.769   5.784  1.00 29.53  ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.257 5.618   8.037  1.00 20.89  ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.564 5.786   7.365  1.00 20.74  ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.640 5.013   6.002  1.00 20.08  ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.612 5.152   5.260  1.00 20.38  ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.756 5.381   8.288  1.00 21.57  ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.619 5.979   9.687  1.00 21.53  ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.895 3.861   8.383  1.00 22.05  ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.642 4.193   5.685  1.00 19.68  ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.654 3.349   4.486  1.00 20.15  ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.803 4.102   3.145  1.00 21.53  ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.334 3.515   2.200  1.00 21.81  ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.420 2.436   4.448  1.00 19.46  ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.376 1.419   5.581  1.00 18.81  ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.058 0.680   5.567  1.00 19.24  ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.002 1.562   6.061  1.00 20.43  ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.733  1.220   6.192  1.00 19.57  ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.319  0.021   5.798  1.00 19.56  ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.858  2.085   6.690  1.00 17.83  ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.340 5.371   3.056  1.00 22.19  ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.428 6.201   1.839  1.00 23.50  ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.818 6.809   1.632  1.00 24.47  ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.079 7.358   0.555  1.00 24.19  ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.416 7.355   1.899  1.00 25.62  ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.664 8.291   3.078  1.00 31.32  ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.804 7.790   4.217  1.00 31.52  ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.735 9.518   2.856  1.00 33.72  ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.683 6.805   2.676  1.00 25.17  ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.023 7.401   2.547  1.00 25.95  ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.930 6.383   1.897  1.00 27.42  ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.778 5.788   2.555  1.00 27.97  ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.583 7.865   3.904  1.00 25.66  ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.624 8.701   4.752  1.00 26.65  ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.180 8.967   6.110  1.00 26.67  ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.186 9.974   4.025  1.00 27.09  ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.729 6.166   0.595  1.00 28.18  ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.471 5.204   -0.211 1.00 29.51  ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.973 5.488   -0.240 1.00 31.83  ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.754 4.560   -0.472 1.00 31.74  ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.899 5.159   -1.651 1.00 29.47  ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.378 5.024   -1.795 1.00 30.82  ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.006 4.686   -3.211 1.00 31.41  ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.819 3.895   -0.922 1.00 31.27  ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.382 6.771   -0.015 1.00 33.00  ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.792 7.160   0.011  1.00 34.52  ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.565 6.605   1.208  1.00 37.48  ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.793 6.727   1.231  1.00 37.89  ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 22.968 8.673   -0.076 1.00 33.74  ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.220 9.437   0.974  1.00 33.34  ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 20.965 9.961   0.869  1.00 33.96  ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.701 9.803   2.272  1.00 32.93  ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.627 10.612  2.029  1.00 34.29  ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.671 10.520  2.914  1.00 33.73  ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 23.892 9.568   2.968  1.00 33.00  ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.803 11.010  4.208  1.00 33.80  ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.016 10.051  4.254  1.00 33.61  ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 22.984 10.769  4.857  1.00 33.60  ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.862 6.022   2.212  1.00 38.96  ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.508 5.379   3.355  1.00 40.87  ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.254 4.123   2.874  1.00 44.26  ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.334 3.823   3.367  1.00 44.37  ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.481 4.978   4.427  1.00 39.93  ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.778 6.113   5.167  1.00 39.85  ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.769 5.565   6.162  1.00 39.67  ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 22.772 7.011   5.886  1.00 39.74  ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 23.675 3.398   1.906  1.00 46.85  ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.243 2.174   1.358  1.00 49.83  ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.146 2.384   0.138  1.00 52.51  ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 25.758 1.422   -0.322 1.00 53.18  ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.117 1.183   1.020  1.00 52.08  ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.663 0.355   2.199  1.00 57.38  ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.533 -0.151  2.940  1.00 58.21  ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.439 0.204   2.379  1.00 60.29  ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.225 3.611   -0.402 1.00 54.26  ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.066 3.877   -1.570 1.00 56.43  ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 26.891 5.151   -1.423 1.00 57.21  ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 27.644 5.492   -2.337 1.00 57.79  ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 25.220 3.936   -2.852 1.00 60.51  ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 24.287 5.134   -2.911 1.00 67.17  ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 23.051 4.948   -3.772 1.00 75.30  ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 22.339 5.955   -4.001 1.00 77.21  ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 22.787 3.804   -4.213 1.00 77.13  ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BRD B 2 .   ? 9.991  14.423  22.361 1.00 35.68  ? 201 A1BRD A N1  1 
HETATM 1079 C  C4  . A1BRD B 2 .   ? 7.771  11.797  25.614 1.00 37.61  ? 201 A1BRD A C4  1 
HETATM 1080 C  C5  . A1BRD B 2 .   ? 8.809  11.803  24.677 1.00 37.04  ? 201 A1BRD A C5  1 
HETATM 1081 C  C6  . A1BRD B 2 .   ? 9.299  13.207  24.403 1.00 36.75  ? 201 A1BRD A C6  1 
HETATM 1082 C  C7  . A1BRD B 2 .   ? 9.275  13.410  22.889 1.00 36.30  ? 201 A1BRD A C7  1 
HETATM 1083 C  C8  . A1BRD B 2 .   ? 11.013 15.216  23.060 1.00 35.19  ? 201 A1BRD A C8  1 
HETATM 1084 C  C10 . A1BRD B 2 .   ? 12.169 15.497  20.840 1.00 35.23  ? 201 A1BRD A C10 1 
HETATM 1085 C  C13 . A1BRD B 2 .   ? 9.787  14.837  20.968 1.00 35.33  ? 201 A1BRD A C13 1 
HETATM 1086 C  C15 . A1BRD B 2 .   ? 7.526  13.182  26.155 1.00 37.93  ? 201 A1BRD A C15 1 
HETATM 1087 O  O2  . A1BRD B 2 .   ? 10.512 16.085  18.329 1.00 33.68  ? 201 A1BRD A O2  1 
HETATM 1088 C  C12 . A1BRD B 2 .   ? 10.934 14.984  18.695 1.00 34.22  ? 201 A1BRD A C12 1 
HETATM 1089 N  N2  . A1BRD B 2 .   ? 11.281 14.028  17.847 1.00 34.00  ? 201 A1BRD A N2  1 
HETATM 1090 C  C11 . A1BRD B 2 .   ? 11.080 14.646  20.169 1.00 34.86  ? 201 A1BRD A C11 1 
HETATM 1091 C  C9  . A1BRD B 2 .   ? 12.340 15.142  22.322 1.00 35.35  ? 201 A1BRD A C9  1 
HETATM 1092 O  O1  . A1BRD B 2 .   ? 8.602  12.679  22.186 1.00 36.50  ? 201 A1BRD A O1  1 
HETATM 1093 C  C14 . A1BRD B 2 .   ? 8.253  14.094  25.148 1.00 37.23  ? 201 A1BRD A C14 1 
HETATM 1094 C  C3  . A1BRD B 2 .   ? 7.194  10.571  25.918 1.00 37.51  ? 201 A1BRD A C3  1 
HETATM 1095 C  C2  . A1BRD B 2 .   ? 7.656  9.420   25.305 1.00 37.66  ? 201 A1BRD A C2  1 
HETATM 1096 N  N   . A1BRD B 2 .   ? 9.295  10.702  24.084 1.00 36.95  ? 201 A1BRD A N   1 
HETATM 1097 C  C1  . A1BRD B 2 .   ? 8.729  9.541   24.399 1.00 37.11  ? 201 A1BRD A C1  1 
HETATM 1098 O  O   . A1BRD B 2 .   ? 9.172  8.379   23.864 1.00 37.28  ? 201 A1BRD A O   1 
HETATM 1099 C  C   . A1BRD B 2 .   ? 10.390 8.398   23.114 1.00 36.85  ? 201 A1BRD A C   1 
HETATM 1100 ZN ZN  . ZN    C 3 .   ? 12.635 -3.644  5.706  1.00 299.35 2 202 ZN    A ZN  1 
HETATM 1101 S  S   . DMS   D 4 .   ? 17.453 21.331  5.468  0.00 30.93  ? 203 DMS   A S   1 
HETATM 1102 O  O   . DMS   D 4 .   ? 17.799 22.664  6.062  0.00 22.76  ? 203 DMS   A O   1 
HETATM 1103 C  C1  . DMS   D 4 .   ? 16.521 21.639  3.943  0.00 27.46  ? 203 DMS   A C1  1 
HETATM 1104 C  C2  . DMS   D 4 .   ? 18.941 20.697  4.648  0.00 27.40  ? 203 DMS   A C2  1 
HETATM 1105 O  O   . HOH   E 5 .   ? 3.002  7.636   9.939  1.00 70.27  ? 301 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 23.673 0.178   15.276 1.00 43.44  ? 302 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 8.862  2.285   2.995  1.00 20.48  ? 303 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 19.905 8.803   18.945 1.00 14.95  ? 304 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 10.519 7.855   4.578  1.00 41.08  ? 305 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 17.593 2.829   23.092 1.00 20.26  ? 306 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 13.055 10.104  9.278  1.00 16.70  ? 307 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 17.745 20.950  9.595  1.00 23.30  ? 308 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 0.426  -0.621  16.346 1.00 24.25  ? 309 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 19.849 22.662  7.656  1.00 27.67  ? 310 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 11.806 2.034   33.356 1.00 27.94  ? 311 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 21.572 18.836  17.898 1.00 35.20  ? 312 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 12.296 -5.005  -0.653 1.00 43.63  ? 313 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 11.160 11.398  11.312 1.00 12.45  ? 314 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 24.538 10.970  20.700 1.00 29.06  ? 315 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 28.183 21.732  18.707 1.00 37.25  ? 316 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 6.984  3.254   33.056 1.00 36.26  ? 317 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 15.102 2.380   23.290 1.00 28.33  ? 318 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 17.889 18.877  16.954 1.00 24.73  ? 319 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 19.282 23.484  15.162 1.00 28.28  ? 320 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 10.041 3.782   33.744 1.00 25.72  ? 321 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 5.324  -1.971  24.308 1.00 30.14  ? 322 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 29.954 10.945  19.253 1.00 34.48  ? 323 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 21.831 -6.022  10.466 1.00 30.39  ? 324 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 7.059  -5.493  2.694  1.00 38.05  ? 325 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 10.330 4.307   3.441  1.00 23.01  ? 326 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 5.441  1.665   7.256  1.00 25.51  ? 327 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 1.633  -2.498  17.539 1.00 24.14  ? 328 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 14.373 12.567  24.056 1.00 31.57  ? 329 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 18.057 9.306   25.381 1.00 48.36  ? 330 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? -2.317 0.372   8.263  1.00 51.64  ? 331 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 3.942  5.661   24.919 1.00 44.02  ? 332 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 11.419 16.995  5.117  1.00 39.97  ? 333 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 11.688 21.259  12.284 1.00 28.30  ? 334 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 20.388 21.448  17.505 1.00 37.52  ? 335 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 22.311 18.955  5.882  1.00 25.29  ? 336 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 13.970 21.070  7.908  1.00 37.92  ? 337 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 2.467  -6.685  14.765 1.00 36.46  ? 338 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 14.305 14.280  3.585  1.00 29.47  ? 339 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 6.013  -5.938  29.281 1.00 34.23  ? 340 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 4.753  8.042   28.081 1.00 26.28  ? 341 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 8.898  -7.780  9.301  1.00 29.74  ? 342 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 2.537  2.679   27.197 1.00 32.16  ? 343 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 9.386  20.969  10.478 1.00 31.07  ? 344 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? -2.146 -4.542  15.120 0.50 11.48  ? 345 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 21.735 9.040   20.984 1.00 33.28  ? 346 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 3.762  11.491  18.979 1.00 46.04  ? 347 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 0.778  -3.683  19.640 1.00 41.14  ? 348 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 17.860 12.817  2.004  1.00 42.86  ? 349 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 24.365 2.233   19.349 1.00 41.05  ? 350 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 3.974  -6.077  6.675  1.00 35.26  ? 351 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 27.610 17.450  23.323 1.00 32.86  ? 352 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 4.007  -3.335  21.699 1.00 54.83  ? 353 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 8.199  22.342  26.485 1.00 50.42  ? 354 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 6.863  11.496  4.112  1.00 37.85  ? 355 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 2.131  -5.185  21.275 1.00 53.52  ? 356 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 21.732 19.407  21.194 1.00 36.86  ? 357 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 1.119  -2.163  23.401 1.00 36.79  ? 358 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 1.848  0.295   26.681 1.00 32.90  ? 359 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 8.244  18.892  6.182  1.00 39.78  ? 360 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 20.214 -4.757  24.069 1.00 33.27  ? 361 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 0.113  -4.536  8.217  1.00 43.31  ? 362 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 1.163  11.019  18.118 1.00 41.65  ? 363 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 3.912  13.141  27.969 1.00 35.19  ? 364 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   ? 0.7702 0.3167 0.3237 -0.0466 -0.2530 0.0227  7   SER   A N   
2    C CA  . SER   A 1   ? 0.7194 0.3240 0.3664 -0.0478 -0.2801 0.0325  7   SER   A CA  
3    C C   . SER   A 1   ? 0.6470 0.3326 0.3931 -0.0326 -0.2672 0.0304  7   SER   A C   
4    O O   . SER   A 1   ? 0.6521 0.3411 0.3907 -0.0271 -0.2541 0.0254  7   SER   A O   
5    C CB  . SER   A 1   ? 0.7563 0.3092 0.3897 -0.0750 -0.3399 0.0533  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.8301 0.3052 0.3832 -0.0938 -0.3650 0.0599  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.5859 0.3294 0.4172 -0.0267 -0.2661 0.0334  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.5301 0.3374 0.4467 -0.0142 -0.2464 0.0306  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.4838 0.3415 0.4562 -0.0051 -0.2211 0.0247  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.4957 0.3509 0.4349 -0.0028 -0.2084 0.0178  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.4356 0.3328 0.4904 -0.0002 -0.2104 0.0280  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.4086 0.3429 0.5133 0.0058  -0.1819 0.0225  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3794 0.3403 0.5297 0.0129  -0.1477 0.0161  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3755 0.3317 0.5400 0.0139  -0.1521 0.0201  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3884 0.3258 0.5558 -0.0010 -0.2050 0.0394  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.3618 0.3415 0.5266 0.0156  -0.1129 0.0062  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.3528 0.3407 0.5456 0.0180  -0.0744 -0.0009 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3338 0.3293 0.6086 0.0191  -0.0575 0.0077  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3275 0.3278 0.6096 0.0168  -0.0577 0.0085  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.3779 0.3656 0.5101 0.0143  -0.0462 -0.0173 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.4091 0.3944 0.4756 0.0139  -0.0600 -0.0214 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3822 0.3599 0.5258 0.0109  -0.0058 -0.0248 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.4417 0.4313 0.4625 0.0086  -0.0483 -0.0280 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3194 0.3145 0.6598 0.0232  -0.0392 0.0154  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2958 0.2963 0.7301 0.0263  -0.0144 0.0271  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3172 0.2988 0.7508 0.0275  0.0484  0.0137  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3172 0.2881 0.7689 0.0313  0.0667  0.0147  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2549 0.2651 0.7861 0.0296  -0.0443 0.0547  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2549 0.2674 0.7768 0.0216  -0.1088 0.0706  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2539 0.2739 0.8087 0.0162  -0.1268 0.0821  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2807 0.2785 0.7528 0.0168  -0.1502 0.0741  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2715 0.2800 0.8025 0.0043  -0.1863 0.0967  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3057 0.2869 0.7490 0.0048  -0.2064 0.0877  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3027 0.2871 0.7727 -0.0024 -0.2253 0.0991  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3339 0.2895 0.7657 -0.0186 -0.2820 0.1138  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3371 0.3057 0.7414 0.0219  0.0822  0.0013  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3688 0.2997 0.7511 0.0171  0.1456  -0.0125 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3739 0.2957 0.8198 0.0182  0.1839  -0.0071 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3805 0.3117 0.8091 0.0135  0.1705  -0.0091 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4197 0.3258 0.6779 0.0021  0.1519  -0.0339 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4319 0.3563 0.6484 -0.0030 0.1202  -0.0364 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4524 0.3019 0.6703 -0.0099 0.2152  -0.0472 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3674 0.2692 0.8914 0.0251  0.2346  0.0010  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3581 0.2477 0.9589 0.0281  0.2813  0.0092  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3236 0.2627 1.0178 0.0339  0.2348  0.0329  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2968 0.2719 1.0511 0.0398  0.1819  0.0537  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3255 0.2612 1.0197 0.0289  0.2487  0.0302  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2907 0.2685 1.0653 0.0309  0.2026  0.0529  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3004 0.2957 0.9793 0.0224  0.1397  0.0430  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3007 0.3111 0.9965 0.0186  0.1170  0.0502  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3046 0.2711 1.1488 0.0314  0.2526  0.0595  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3525 0.3040 1.3205 0.0427  0.3168  0.0771  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3499 0.3200 1.4025 0.0524  0.3040  0.0981  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.3826 0.2960 1.3679 0.0418  0.3904  0.0709  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3032 0.2940 0.8851 0.0197  0.1149  0.0278  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3010 0.3027 0.7969 0.0138  0.0650  0.0197  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2789 0.2934 0.7578 0.0159  0.0125  0.0274  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2685 0.2804 0.7678 0.0203  0.0171  0.0309  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3400 0.3176 0.7197 0.0055  0.0872  -0.0061 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3511 0.3029 0.7151 -0.0021 0.1331  -0.0162 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3460 0.3091 0.7406 -0.0032 0.1255  -0.0099 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3931 0.3005 0.7004 -0.0114 0.1837  -0.0322 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3722 0.3063 0.7489 -0.0113 0.1698  -0.0194 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4301 0.2995 0.7084 -0.0224 0.2275  -0.0418 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4258 0.3103 0.7408 -0.0214 0.2213  -0.0357 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4798 0.3220 0.7619 -0.0332 0.2661  -0.0455 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2692 0.2895 0.7006 0.0116  -0.0334 0.0288  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2682 0.2854 0.6564 0.0104  -0.0793 0.0329  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2813 0.2899 0.5645 0.0082  -0.0830 0.0149  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2848 0.2933 0.5486 0.0051  -0.0853 0.0122  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2627 0.2804 0.6993 0.0039  -0.1313 0.0580  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3185 0.3130 0.6777 -0.0028 -0.1783 0.0596  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3339 0.3140 0.7308 -0.0161 -0.2343 0.0874  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3958 0.3383 0.6963 -0.0275 -0.2695 0.0849  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4420 0.3432 0.6824 -0.0388 -0.3087 0.0923  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4087 0.3075 0.6771 -0.0396 -0.3222 0.1024  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4828 0.3371 0.6274 -0.0502 -0.3310 0.0888  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2829 0.2853 0.5070 0.0102  -0.0805 0.0045  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2877 0.2853 0.4308 0.0094  -0.0814 -0.0071 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2935 0.2758 0.3954 0.0102  -0.1145 -0.0020 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.3052 0.2807 0.4035 0.0115  -0.1226 0.0003  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2939 0.2917 0.4002 0.0079  -0.0523 -0.0195 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.3152 0.3133 0.3580 0.0064  -0.0566 -0.0242 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2799 0.2725 0.4102 0.0027  -0.0144 -0.0255 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2913 0.2602 0.3561 0.0083  -0.1307 -0.0003 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.3118 0.2480 0.3201 0.0068  -0.1546 0.0033  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.3309 0.2575 0.2792 0.0112  -0.1407 -0.0036 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.3166 0.2640 0.2725 0.0132  -0.1231 -0.0083 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3208 0.2289 0.3370 -0.0039 -0.1928 0.0178  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2983 0.2188 0.3921 -0.0085 -0.2106 0.0321  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3236 0.2319 0.3405 -0.0072 -0.1943 0.0187  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.3610 0.2502 0.2505 0.0119  -0.1472 -0.0024 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.3906 0.2597 0.2294 0.0174  -0.1315 -0.0045 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.4149 0.2641 0.2421 0.0115  -0.1441 -0.0016 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.4379 0.2555 0.2553 0.0000  -0.1729 0.0049  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.4366 0.2535 0.2127 0.0174  -0.1307 -0.0031 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.4654 0.2975 0.2462 0.0239  -0.1149 -0.0052 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.5016 0.3301 0.2896 0.0194  -0.1289 -0.0048 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.4357 0.2845 0.2169 0.0337  -0.0874 -0.0046 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.4089 0.2750 0.2384 0.0170  -0.1267 -0.0039 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.4199 0.2693 0.2380 0.0122  -0.1355 -0.0020 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.4851 0.2640 0.2314 0.0051  -0.1481 0.0017  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.5086 0.2621 0.2463 -0.0080 -0.1747 0.0069  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3966 0.2705 0.2211 0.0202  -0.1121 -0.0041 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3832 0.2541 0.2111 0.0152  -0.1192 -0.0035 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.3738 0.2532 0.1917 0.0239  -0.0970 -0.0025 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3695 0.2495 0.1899 0.0203  -0.0997 -0.0026 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3960 0.2333 0.1754 0.0183  -0.1043 -0.0008 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.4109 0.1922 0.1356 0.0165  -0.1080 0.0009  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3706 0.2124 0.1551 0.0153  -0.1055 -0.0009 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.5155 0.2554 0.2077 0.0110  -0.1289 0.0006  21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.5894 0.2418 0.1925 0.0017  -0.1324 0.0026  21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.6402 0.2453 0.2106 -0.0192 -0.1734 0.0082  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.7009 0.2233 0.1897 -0.0364 -0.1897 0.0121  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.6200 0.2369 0.1776 0.0148  -0.0901 0.0008  21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.6319 0.2438 0.1835 0.0171  -0.0835 0.0000  21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.5954 0.2775 0.2139 0.0301  -0.0691 0.0000  21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.6966 0.2352 0.1760 0.0055  -0.0902 -0.0001 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.6241 0.2802 0.2166 0.0284  -0.0664 -0.0008 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.6846 0.2545 0.1934 0.0140  -0.0782 -0.0012 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.6132 0.2649 0.2454 -0.0203 -0.1922 0.0108  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.6400 0.2567 0.2615 -0.0402 -0.2362 0.0214  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.6179 0.2790 0.3249 -0.0494 -0.2714 0.0333  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.6192 0.2671 0.3470 -0.0646 -0.3104 0.0476  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.6306 0.2598 0.2638 -0.0349 -0.2311 0.0195  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.6825 0.2618 0.2375 -0.0283 -0.1982 0.0116  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.6685 0.2635 0.2409 -0.0250 -0.1980 0.0107  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.7621 0.2300 0.1995 -0.0471 -0.2067 0.0143  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.5873 0.3013 0.3513 -0.0402 -0.2562 0.0298  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.5605 0.3157 0.4134 -0.0468 -0.2791 0.0415  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.6018 0.3059 0.4349 -0.0722 -0.3298 0.0607  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.6539 0.2922 0.3949 -0.0835 -0.3378 0.0595  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.5311 0.3376 0.4288 -0.0342 -0.2483 0.0323  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.5838 0.3136 0.5049 -0.0826 -0.3634 0.0809  24  THR   A N   
135  C CA  . THR   A 18  ? 0.6191 0.3072 0.5430 -0.1113 -0.4222 0.1073  24  THR   A CA  
136  C C   . THR   A 18  ? 0.6185 0.3326 0.5925 -0.1143 -0.4239 0.1132  24  THR   A C   
137  O O   . THR   A 18  ? 0.6007 0.3623 0.6023 -0.0937 -0.3779 0.0954  24  THR   A O   
138  C CB  . THR   A 18  ? 0.6018 0.3124 0.6190 -0.1201 -0.4582 0.1324  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5437 0.3366 0.6886 -0.1002 -0.4257 0.1322  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.6359 0.3192 0.6048 -0.1190 -0.4600 0.1279  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.6377 0.3176 0.6220 -0.1425 -0.4794 0.1400  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.6244 0.3321 0.6687 -0.1464 -0.4831 0.1488  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.5399 0.3353 0.7392 -0.1289 -0.4581 0.1561  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.5081 0.3423 0.7518 -0.1175 -0.4253 0.1476  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.6819 0.3323 0.7107 -0.1845 -0.5550 0.1814  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.8379 0.3865 0.7022 -0.2056 -0.5730 0.1734  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.9061 0.4376 0.6966 -0.1949 -0.5343 0.1495  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.9361 0.3881 0.6968 -0.2389 -0.6246 0.1884  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 1.0028 0.4280 0.6498 -0.2194 -0.5569 0.1495  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 1.0319 0.4008 0.6480 -0.2482 -0.6114 0.1716  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.5036 0.3233 0.7821 -0.1275 -0.4700 0.1723  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4389 0.3301 0.8623 -0.1103 -0.4374 0.1798  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.4116 0.3392 0.8219 -0.0819 -0.3643 0.1448  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3778 0.3466 0.8695 -0.0709 -0.3263 0.1431  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4508 0.3535 0.9535 -0.1131 -0.4614 0.2037  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4524 0.4144 1.1254 -0.1040 -0.4418 0.2264  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4467 0.4241 1.1923 -0.1124 -0.4524 0.2456  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4389 0.4319 1.1797 -0.0861 -0.4075 0.2248  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.4284 0.3355 0.7360 -0.0723 -0.3447 0.1192  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.4027 0.3366 0.6850 -0.0507 -0.2849 0.0895  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3894 0.3298 0.6507 -0.0481 -0.2621 0.0774  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3624 0.3344 0.6616 -0.0372 -0.2191 0.0661  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.4509 0.3570 0.6296 -0.0449 -0.2783 0.0714  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.4764 0.3820 0.6726 -0.0434 -0.2872 0.0772  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.4481 0.3902 0.7330 -0.0361 -0.2696 0.0827  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.5291 0.3918 0.6470 -0.0499 -0.3087 0.0762  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.4136 0.3163 0.6092 -0.0604 -0.2908 0.0804  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.4137 0.3173 0.5854 -0.0595 -0.2745 0.0710  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3799 0.3115 0.6515 -0.0661 -0.2776 0.0873  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3782 0.3259 0.6554 -0.0606 -0.2474 0.0764  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.4552 0.2994 0.5201 -0.0711 -0.3014 0.0700  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.4774 0.3006 0.4507 -0.0582 -0.2743 0.0496  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.5154 0.3000 0.4254 -0.0594 -0.2828 0.0480  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.4743 0.3118 0.4156 -0.0433 -0.2349 0.0317  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.5380 0.3161 0.3884 -0.0441 -0.2469 0.0309  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.5129 0.3263 0.3863 -0.0342 -0.2198 0.0224  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.4558 0.3242 0.4244 -0.0376 -0.2108 0.0248  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.5175 0.3400 0.3600 -0.0199 -0.1855 0.0105  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.4711 0.3454 0.3993 -0.0252 -0.1799 0.0114  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.4958 0.3505 0.3683 -0.0163 -0.1690 0.0062  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3568 0.2925 0.7105 -0.0791 -0.3148 0.1160  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3233 0.2896 0.7937 -0.0844 -0.3148 0.1368  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2907 0.3019 0.8532 -0.0660 -0.2555 0.1300  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2740 0.3070 0.9143 -0.0646 -0.2295 0.1365  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3063 0.2622 0.8467 -0.1066 -0.3784 0.1765  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2831 0.3004 0.8326 -0.0534 -0.2316 0.1175  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2431 0.2859 0.8552 -0.0385 -0.1721 0.1085  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2630 0.2958 0.7696 -0.0282 -0.1343 0.0742  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2573 0.2939 0.7653 -0.0196 -0.1058 0.0650  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2262 0.2813 0.9239 -0.0360 -0.1822 0.1293  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2262 0.2946 1.0472 -0.0481 -0.2228 0.1703  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2274 0.3097 1.1196 -0.0512 -0.2108 0.1824  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2092 0.2720 1.0607 -0.0572 -0.2738 0.1952  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2787 0.2971 0.6963 -0.0305 -0.1371 0.0584  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2945 0.3045 0.6192 -0.0237 -0.1118 0.0332  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2875 0.3020 0.6222 -0.0204 -0.0571 0.0189  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2832 0.2990 0.6578 -0.0239 -0.0362 0.0212  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.3220 0.3144 0.5677 -0.0274 -0.1309 0.0268  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.3557 0.3425 0.5196 -0.0215 -0.1079 0.0071  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.3753 0.3563 0.4943 -0.0155 -0.1148 0.0029  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.3678 0.3401 0.4804 -0.0242 -0.1176 0.0045  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2918 0.3010 0.5824 -0.0164 -0.0337 0.0046  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2952 0.2905 0.5663 -0.0195 0.0158  -0.0099 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.3112 0.2949 0.4843 -0.0240 0.0135  -0.0238 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3319 0.2989 0.4726 -0.0324 0.0360  -0.0320 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.3048 0.2941 0.6015 -0.0165 0.0445  -0.0120 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3462 0.3024 0.5900 -0.0255 0.0933  -0.0287 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2655 0.2671 0.6771 -0.0113 0.0526  0.0063  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2950 0.2850 0.4252 -0.0194 -0.0140 -0.0238 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2938 0.2785 0.3515 -0.0218 -0.0191 -0.0300 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2804 0.2719 0.3159 -0.0130 -0.0491 -0.0246 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2619 0.2565 0.3169 -0.0082 -0.0599 -0.0208 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.3022 0.2733 0.3254 -0.0303 0.0050  -0.0379 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.3235 0.2939 0.2876 -0.0346 -0.0077 -0.0371 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3471 0.3089 0.2719 -0.0439 -0.0105 -0.0357 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.3180 0.2979 0.2659 -0.0303 -0.0207 -0.0334 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3534 0.3216 0.2479 -0.0455 -0.0261 -0.0283 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3387 0.3181 0.2469 -0.0371 -0.0304 -0.0274 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.3083 0.2962 0.2750 -0.0221 -0.0254 -0.0326 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3443 0.3335 0.2390 -0.0358 -0.0420 -0.0195 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.3205 0.3150 0.2632 -0.0203 -0.0357 -0.0283 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3334 0.3297 0.2442 -0.0270 -0.0426 -0.0213 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2853 0.2737 0.2784 -0.0114 -0.0592 -0.0234 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2805 0.2651 0.2451 -0.0026 -0.0760 -0.0187 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2754 0.2623 0.2053 -0.0014 -0.0711 -0.0159 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2671 0.2543 0.1885 -0.0078 -0.0654 -0.0160 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2903 0.2566 0.2505 0.0003  -0.0980 -0.0132 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.3141 0.2724 0.2732 -0.0039 -0.1025 -0.0118 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3602 0.3100 0.2779 0.0001  -0.0968 -0.0115 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4059 0.3595 0.3272 -0.0046 -0.0908 -0.0131 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.3220 0.2595 0.2078 0.0082  -0.0956 -0.0082 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2746 0.2625 0.1899 0.0057  -0.0733 -0.0110 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2713 0.2648 0.1723 0.0085  -0.0700 -0.0014 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2683 0.2480 0.1566 0.0223  -0.0688 0.0052  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2662 0.2470 0.1555 0.0257  -0.0670 0.0060  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2849 0.2929 0.1879 -0.0020 -0.0672 0.0024  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3524 0.3682 0.2531 -0.0056 -0.0712 0.0181  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3558 0.3706 0.2626 0.0075  -0.0696 0.0282  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.4104 0.4276 0.3022 -0.0231 -0.0758 0.0223  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2745 0.2342 0.1461 0.0295  -0.0656 0.0095  36  SER   A N   
241  C CA  A SER   A 30  ? 0.3045 0.2337 0.1523 0.0417  -0.0547 0.0151  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2978 0.2271 0.1457 0.0417  -0.0548 0.0150  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2988 0.2462 0.1688 0.0492  -0.0409 0.0286  36  SER   A C   
244  O O   . SER   A 30  ? 0.3112 0.2408 0.1705 0.0566  -0.0300 0.0305  36  SER   A O   
245  C CB  A SER   A 30  ? 0.3444 0.2437 0.1679 0.0463  -0.0482 0.0178  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.3208 0.2178 0.1424 0.0465  -0.0480 0.0175  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.4108 0.2702 0.2068 0.0584  -0.0266 0.0246  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.3206 0.2371 0.1656 0.0513  -0.0380 0.0298  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2915 0.2724 0.1934 0.0441  -0.0442 0.0402  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2768 0.2800 0.2135 0.0470  -0.0386 0.0599  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2598 0.2764 0.2015 0.0414  -0.0435 0.0567  37  SER   A C   
252  O O   . SER   A 31  ? 0.2453 0.2745 0.2147 0.0457  -0.0369 0.0729  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2869 0.3157 0.2517 0.0364  -0.0511 0.0770  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3379 0.3813 0.2953 0.0150  -0.0702 0.0720  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2452 0.2591 0.1671 0.0322  -0.0534 0.0381  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2302 0.2512 0.1530 0.0276  -0.0561 0.0330  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2463 0.2409 0.1473 0.0363  -0.0523 0.0211  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2473 0.2446 0.1488 0.0348  -0.0533 0.0180  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2208 0.2506 0.1392 0.0099  -0.0655 0.0229  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2097 0.2512 0.1311 -0.0067 -0.0740 0.0352  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2179 0.2482 0.1167 -0.0268 -0.0748 0.0228  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2363 0.2647 0.1301 -0.0317 -0.0721 0.0178  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2763 0.2881 0.1440 -0.0527 -0.0703 0.0134  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2652 0.2560 0.1037 -0.0728 -0.0711 0.0133  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2856 0.2933 0.1482 -0.0557 -0.0660 0.0090  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2635 0.2273 0.1401 0.0422  -0.0513 0.0159  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2853 0.2134 0.1314 0.0429  -0.0576 0.0072  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2838 0.2288 0.1498 0.0328  -0.0745 -0.0019 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2805 0.2111 0.1393 0.0315  -0.0827 -0.0048 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.3041 0.2088 0.1303 0.0502  -0.0444 0.0109  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3759 0.2279 0.1539 0.0466  -0.0538 0.0043  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3781 0.1975 0.1274 0.0408  -0.0665 0.0015  39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.4116 0.2510 0.1772 0.0470  -0.0514 0.0036  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2742 0.2440 0.1657 0.0255  -0.0768 -0.0050 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2815 0.2610 0.1996 0.0180  -0.0825 -0.0119 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2978 0.2727 0.2330 0.0136  -0.0903 -0.0137 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.3089 0.2834 0.2364 0.0127  -0.0877 -0.0130 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2707 0.2716 0.2026 0.0099  -0.0700 -0.0147 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2833 0.2911 0.2090 0.0092  -0.0660 -0.0126 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2868 0.2990 0.2135 -0.0047 -0.0555 -0.0168 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2886 0.2858 0.2169 0.0155  -0.0726 -0.0145 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2974 0.2710 0.2642 0.0103  -0.0995 -0.0137 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.3067 0.2812 0.3098 0.0051  -0.1065 -0.0112 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.3078 0.2956 0.3681 0.0029  -0.0987 -0.0103 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.3120 0.2977 0.3801 0.0049  -0.1056 -0.0078 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.3275 0.2733 0.3147 0.0018  -0.1360 -0.0027 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.3323 0.2796 0.3616 -0.0060 -0.1492 0.0045  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.3667 0.2786 0.3494 -0.0118 -0.1719 0.0097  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3221 0.2776 0.4199 -0.0111 -0.1648 0.0163  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.3049 0.3023 0.4050 -0.0009 -0.0797 -0.0119 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.3008 0.3047 0.4632 -0.0014 -0.0618 -0.0095 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2989 0.3074 0.5281 -0.0039 -0.0701 0.0028  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2972 0.3049 0.5228 -0.0075 -0.0635 0.0008  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.3146 0.3132 0.4622 -0.0058 -0.0205 -0.0216 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3021 0.2970 0.5164 -0.0052 0.0090  -0.0188 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.3374 0.3321 0.4230 -0.0072 -0.0194 -0.0290 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2946 0.3078 0.5879 -0.0034 -0.0879 0.0183  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2937 0.3150 0.6722 -0.0074 -0.1005 0.0374  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2948 0.3275 0.7684 -0.0025 -0.0649 0.0453  43  SER   A C   
300  O O   . SER   A 37  ? 0.2917 0.3208 0.7556 0.0028  -0.0414 0.0369  43  SER   A O   
301  C CB  . SER   A 37  ? 0.3066 0.3175 0.6896 -0.0150 -0.1580 0.0569  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3249 0.3343 0.7283 -0.0132 -0.1716 0.0652  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2948 0.3383 0.8625 -0.0042 -0.0571 0.0623  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2992 0.3494 0.9709 0.0023  -0.0145 0.0731  44  SER   A CA  
305  C C   . SER   A 38  ? 0.3070 0.3731 1.0794 0.0027  -0.0514 0.1047  44  SER   A C   
306  O O   . SER   A 38  ? 0.3062 0.3764 1.0887 -0.0072 -0.1123 0.1245  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2888 0.3403 1.0215 0.0012  0.0232  0.0773  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2944 0.3631 1.0863 -0.0062 -0.0244 0.1022  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3168 0.3851 1.1603 0.0118  -0.0154 0.1114  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3124 0.3968 1.2667 0.0127  -0.0480 0.1456  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2962 0.3925 1.4021 0.0219  0.0035  0.1679  45  THR   A C   
312  O O   . THR   A 39  ? 0.3104 0.3905 1.4101 0.0285  0.0751  0.1493  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3481 0.4229 1.2541 0.0171  -0.0564 0.1372  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3686 0.4313 1.2826 0.0287  0.0150  0.1211  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3993 0.4582 1.1584 0.0108  -0.0904 0.1134  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2677 0.3861 1.5093 0.0209  -0.0308 0.2096  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2379 0.3698 1.6465 0.0322  0.0209  0.2373  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2587 0.3775 1.6870 0.0464  0.0660  0.2321  46  THR   A C   
319  O O   . THR   A 40  ? 0.2593 0.3595 1.7311 0.0593  0.1511  0.2240  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2013 0.3659 1.7631 0.0225  -0.0411 0.2915  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.2297 0.3951 1.7616 0.0095  -0.1262 0.3086  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2061 0.3788 1.7658 0.0095  -0.0661 0.2972  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2781 0.3979 1.6621 0.0427  0.0122  0.2351  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2868 0.3944 1.6820 0.0544  0.0445  0.2312  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3554 0.4264 1.6038 0.0591  0.1043  0.1819  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4067 0.4664 1.5270 0.0509  0.0973  0.1521  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2907 0.4066 1.6741 0.0457  -0.0368 0.2498  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3583 0.4073 1.6256 0.0705  0.1613  0.1758  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4257 0.4316 1.5537 0.0701  0.2149  0.1333  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4628 0.4683 1.4707 0.0638  0.1640  0.1156  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4492 0.4759 1.4969 0.0643  0.1084  0.1366  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4443 0.4126 1.6292 0.0820  0.3040  0.1328  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5543 0.4613 1.6149 0.0753  0.3795  0.0939  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6158 0.5133 1.6971 0.0717  0.4142  0.0925  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.5853 0.5011 1.8161 0.0814  0.4357  0.1223  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6765 0.5455 1.6149 0.0567  0.4193  0.0607  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.5060 0.4836 1.3696 0.0564  0.1836  0.0795  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.5345 0.5099 1.2822 0.0503  0.1449  0.0615  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.5462 0.4854 1.2390 0.0511  0.1914  0.0435  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5733 0.4708 1.2322 0.0478  0.2565  0.0273  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.5322 0.4789 1.2037 0.0525  0.1575  0.0457  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.5481 0.4621 1.1728 0.0527  0.1936  0.0319  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.5610 0.4647 1.0458 0.0409  0.1721  0.0076  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.5852 0.4704 1.0326 0.0398  0.1816  0.0006  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.5436 0.4705 1.2664 0.0641  0.1799  0.0564  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.6045 0.5772 1.3762 0.0633  0.0835  0.0844  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.5400 0.4551 0.9544 0.0321  0.1453  -0.0030 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.5520 0.4618 0.8530 0.0215  0.1253  -0.0201 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.5597 0.4294 0.7740 0.0059  0.1657  -0.0395 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.5746 0.4341 0.7750 -0.0006 0.1820  -0.0442 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.5694 0.5107 0.8420 0.0207  0.0704  -0.0172 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.6195 0.5778 0.9071 0.0265  0.0240  -0.0055 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.6485 0.5971 0.9247 0.0276  0.0280  -0.0071 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.6317 0.6053 0.9342 0.0275  -0.0160 0.0052  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.5533 0.3960 0.7017 -0.0034 0.1769  -0.0494 52  THR   A N   
356  C CA  . THR   A 46  ? 0.5737 0.3680 0.6227 -0.0255 0.2049  -0.0648 52  THR   A CA  
357  C C   . THR   A 46  ? 0.5476 0.3666 0.5332 -0.0358 0.1604  -0.0664 52  THR   A C   
358  O O   . THR   A 46  ? 0.5372 0.3895 0.5194 -0.0302 0.1214  -0.0615 52  THR   A O   
359  C CB  . THR   A 46  ? 0.6197 0.3764 0.6247 -0.0335 0.2252  -0.0709 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.6301 0.3546 0.6941 -0.0239 0.2774  -0.0689 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6799 0.3834 0.5656 -0.0632 0.2370  -0.0831 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.5304 0.3309 0.4701 -0.0504 0.1680  -0.0715 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.5086 0.3305 0.3967 -0.0607 0.1285  -0.0691 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.5397 0.3173 0.3351 -0.0884 0.1326  -0.0733 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.5839 0.2980 0.3279 -0.1076 0.1708  -0.0818 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4933 0.3211 0.3840 -0.0630 0.1264  -0.0687 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4491 0.3112 0.4322 -0.0400 0.1246  -0.0627 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4895 0.3414 0.3380 -0.0717 0.0860  -0.0625 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4238 0.3350 0.4457 -0.0229 0.0799  -0.0530 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.5198 0.3236 0.2918 -0.0928 0.0952  -0.0658 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.5514 0.3181 0.2416 -0.1229 0.0876  -0.0636 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.5657 0.3052 0.1994 -0.1484 0.0796  -0.0599 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.5292 0.3041 0.1941 -0.1385 0.0627  -0.0547 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.5278 0.3387 0.2285 -0.1186 0.0484  -0.0514 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.6285 0.2984 0.1727 -0.1838 0.0900  -0.0617 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.6635 0.2946 0.1387 -0.2159 0.0760  -0.0552 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.6911 0.2991 0.1018 -0.2493 0.0408  -0.0401 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.7551 0.2861 0.0828 -0.2787 0.0594  -0.0461 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.7348 0.2810 0.1507 -0.2326 0.1279  -0.0716 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.7186 0.2907 0.2159 -0.1989 0.1651  -0.0827 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.6830 0.3209 0.2399 -0.1806 0.1356  -0.0750 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.6500 0.2993 0.2750 -0.1561 0.1710  -0.0836 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.6141 0.3217 0.3076 -0.1337 0.1526  -0.0787 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5649 0.3229 0.2669 -0.1299 0.1047  -0.0671 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5883 0.3022 0.3465 -0.1153 0.1832  -0.0833 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.6465 0.3202 0.1019 -0.2436 -0.0073 -0.0190 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.6693 0.3406 0.0961 -0.2691 -0.0444 0.0010  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.6466 0.3870 0.1342 -0.2639 -0.0926 0.0296  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.6149 0.3990 0.1565 -0.2408 -0.0948 0.0313  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.6634 0.3502 0.1155 -0.2513 -0.0304 -0.0070 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.6425 0.4284 0.2156 -0.1968 -0.0337 -0.0074 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.6642 0.4132 0.1484 -0.2850 -0.1287 0.0539  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.6355 0.4487 0.1913 -0.2801 -0.1695 0.0864  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.6002 0.4632 0.2170 -0.2587 -0.1719 0.0938  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.5902 0.4853 0.2487 -0.2688 -0.2053 0.1256  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.7027 0.4790 0.2093 -0.3310 -0.2166 0.1184  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.8685 0.5925 0.3065 -0.3707 -0.2339 0.1272  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.9350 0.6133 0.3171 -0.3694 -0.1975 0.0985  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.9108 0.6402 0.3574 -0.4026 -0.2842 0.1650  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.5788 0.4454 0.2037 -0.2309 -0.1371 0.0671  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.5349 0.4389 0.2065 -0.2103 -0.1348 0.0697  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4583 0.4268 0.2153 -0.1832 -0.1444 0.0880  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4458 0.4359 0.2348 -0.1617 -0.1363 0.0841  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.5501 0.4424 0.2162 -0.1852 -0.0977 0.0387  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.6539 0.4764 0.2376 -0.2133 -0.0819 0.0248  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.4153 0.4091 0.2076 -0.1840 -0.1572 0.1076  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.3553 0.4018 0.2298 -0.1566 -0.1554 0.1253  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.3219 0.3793 0.2142 -0.1326 -0.1338 0.1137  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2915 0.3806 0.2427 -0.1171 -0.1299 0.1321  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3505 0.4223 0.2738 -0.1780 -0.1890 0.1689  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3953 0.4723 0.3326 -0.1876 -0.2075 0.1856  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3998 0.5074 0.4055 -0.2070 -0.2434 0.2353  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4392 0.5248 0.4170 -0.2469 -0.2832 0.2578  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3401 0.4936 0.4377 -0.1805 -0.2295 0.2559  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.3323 0.3595 0.1756 -0.1312 -0.1184 0.0862  60  THR   A N   
416  C CA  . THR   A 54  ? 0.3230 0.3533 0.1745 -0.1099 -0.1001 0.0733  60  THR   A CA  
417  C C   . THR   A 54  ? 0.3270 0.3338 0.1501 -0.0944 -0.0800 0.0423  60  THR   A C   
418  O O   . THR   A 54  ? 0.3540 0.3322 0.1394 -0.1081 -0.0763 0.0301  60  THR   A O   
419  C CB  . THR   A 54  ? 0.3642 0.3804 0.1920 -0.1306 -0.1084 0.0790  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.4223 0.3934 0.1834 -0.1555 -0.1096 0.0651  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3454 0.3872 0.2134 -0.1495 -0.1333 0.1160  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.3048 0.3176 0.1457 -0.0685 -0.0667 0.0322  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.3116 0.3067 0.1419 -0.0538 -0.0544 0.0099  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2996 0.2925 0.1395 -0.0330 -0.0486 0.0044  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2919 0.2903 0.1369 -0.0310 -0.0478 0.0138  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2929 0.2730 0.1345 -0.0200 -0.0458 -0.0087 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2844 0.2490 0.1239 -0.0052 -0.0472 -0.0136 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2807 0.2400 0.1285 0.0052  -0.0523 -0.0161 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2656 0.2283 0.1280 0.0034  -0.0532 -0.0212 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2938 0.2411 0.1299 -0.0069 -0.0465 -0.0230 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.3074 0.2335 0.1415 0.0043  -0.0565 -0.0251 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.3081 0.2541 0.1273 -0.0190 -0.0414 -0.0211 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2965 0.2404 0.1308 0.0144  -0.0532 -0.0126 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.3105 0.2383 0.1407 0.0206  -0.0613 -0.0144 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.3439 0.2292 0.1452 0.0229  -0.0744 -0.0163 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.3649 0.2291 0.1403 0.0227  -0.0702 -0.0157 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.3069 0.2395 0.1350 0.0253  -0.0510 -0.0072 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.3321 0.2363 0.1333 0.0319  -0.0358 -0.0013 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.3352 0.2526 0.1477 0.0317  -0.0204 0.0074  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.3784 0.2364 0.1412 0.0364  -0.0337 -0.0029 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3680 0.2556 0.1623 0.0390  0.0028  0.0143  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.4186 0.2356 0.1469 0.0416  -0.0099 0.0016  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.4158 0.2497 0.1649 0.0445  0.0117  0.0102  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.4559 0.2477 0.1795 0.0511  0.0442  0.0164  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.3531 0.2217 0.1565 0.0223  -0.0927 -0.0165 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.4077 0.2272 0.1775 0.0181  -0.1146 -0.0138 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.4439 0.2161 0.1555 0.0175  -0.1103 -0.0121 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.4314 0.2114 0.1483 0.0201  -0.1056 -0.0115 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.4051 0.2271 0.2151 0.0138  -0.1425 -0.0090 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.4500 0.2166 0.2241 0.0038  -0.1751 -0.0008 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4728 0.2140 0.2230 0.0000  -0.1818 0.0004  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4861 0.2168 0.2379 -0.0051 -0.2011 0.0069  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.5293 0.2089 0.2338 -0.0137 -0.2157 0.0098  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.5353 0.2012 0.2377 -0.0209 -0.2369 0.0171  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5685 0.2075 0.2459 -0.0258 -0.2449 0.0188  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.6527 0.2185 0.2716 -0.0456 -0.2842 0.0306  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.4854 0.2033 0.1368 0.0138  -0.1059 -0.0118 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.5422 0.1958 0.1232 0.0119  -0.0912 -0.0112 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.6121 0.1892 0.1276 -0.0051 -0.1250 -0.0082 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.6270 0.1626 0.1010 -0.0126 -0.1303 -0.0080 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.5569 0.1987 0.1171 0.0192  -0.0514 -0.0116 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.6680 0.2100 0.1326 0.0171  -0.0181 -0.0112 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.6467 0.2028 0.1527 -0.0143 -0.1524 -0.0036 66  SER   A N   
464  C CA  . SER   A 60  ? 0.7176 0.1990 0.1645 -0.0365 -0.1959 0.0049  66  SER   A CA  
465  C C   . SER   A 60  ? 0.8112 0.1836 0.1352 -0.0499 -0.1827 0.0026  66  SER   A C   
466  O O   . SER   A 60  ? 0.8697 0.1723 0.1330 -0.0718 -0.2188 0.0100  66  SER   A O   
467  C CB  . SER   A 60  ? 0.7481 0.2334 0.2200 -0.0461 -0.2324 0.0142  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.8342 0.2838 0.2560 -0.0471 -0.2153 0.0107  66  SER   A OG  
469  N N   . SER   A 61  ? 0.8370 0.1892 0.1246 -0.0382 -0.1295 -0.0055 67  SER   A N   
470  C CA  . SER   A 61  ? 0.9317 0.1693 0.0985 -0.0495 -0.1021 -0.0087 67  SER   A CA  
471  C C   . SER   A 61  ? 0.9544 0.1706 0.0969 -0.0513 -0.0920 -0.0110 67  SER   A C   
472  O O   . SER   A 61  ? 1.0331 0.1385 0.0627 -0.0689 -0.0844 -0.0123 67  SER   A O   
473  C CB  . SER   A 61  ? 0.9721 0.1942 0.1225 -0.0337 -0.0407 -0.0134 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.9288 0.2512 0.1815 -0.0078 -0.0059 -0.0136 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.8816 0.1941 0.1203 -0.0364 -0.0933 -0.0114 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.8964 0.1975 0.1214 -0.0387 -0.0900 -0.0129 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.8787 0.2122 0.1469 -0.0480 -0.1451 -0.0067 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.8991 0.2218 0.1561 -0.0513 -0.1483 -0.0071 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.8529 0.2309 0.1503 -0.0160 -0.0440 -0.0161 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.8986 0.2399 0.1645 -0.0058 0.0167  -0.0169 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.9980 0.2289 0.1574 -0.0171 0.0437  -0.0198 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 1.0482 0.2373 0.1845 -0.0055 0.1105  -0.0184 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 1.1204 0.2263 0.1817 -0.0111 0.1317  -0.0198 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.1503 0.2009 0.1426 -0.0319 0.0850  -0.0223 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 1.1337 0.2071 0.1909 0.0031  0.2005  -0.0165 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.8376 0.2165 0.1674 -0.0500 -0.1837 0.0004  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.8001 0.2236 0.2014 -0.0538 -0.2277 0.0099  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.7392 0.2328 0.2062 -0.0375 -0.2046 0.0036  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.7421 0.2331 0.2228 -0.0428 -0.2267 0.0088  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.8909 0.2306 0.2291 -0.0810 -0.2805 0.0238  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.9930 0.2632 0.2703 -0.1029 -0.3143 0.0339  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 1.0578 0.3104 0.3628 -0.1255 -0.3855 0.0578  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.2201 0.3437 0.3949 -0.1618 -0.4256 0.0691  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.3392 0.3845 0.4283 -0.1793 -0.4366 0.0709  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.3301 0.4196 0.4560 -0.1612 -0.4082 0.0613  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.4213 0.3358 0.3782 -0.2177 -0.4759 0.0822  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.6803 0.2306 0.1834 -0.0198 -0.1613 -0.0057 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.6279 0.2380 0.1811 -0.0078 -0.1365 -0.0110 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.5556 0.2431 0.1804 0.0045  -0.1178 -0.0138 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.5488 0.2400 0.1736 0.0075  -0.1108 -0.0135 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.6831 0.2610 0.1840 -0.0052 -0.0992 -0.0153 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.7763 0.3242 0.2471 -0.0116 -0.1043 -0.0159 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.8623 0.3882 0.2978 -0.0070 -0.0598 -0.0187 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.9529 0.4373 0.3456 -0.0149 -0.0626 -0.0201 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 1.0439 0.4176 0.3281 -0.0310 -0.0689 -0.0201 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.5043 0.2439 0.1794 0.0092  -0.1090 -0.0163 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.4543 0.2554 0.1822 0.0149  -0.0919 -0.0184 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.4371 0.2521 0.1570 0.0168  -0.0648 -0.0175 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.4598 0.2563 0.1575 0.0146  -0.0601 -0.0178 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.4318 0.2630 0.2078 0.0136  -0.0994 -0.0203 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.4271 0.2558 0.2380 0.0131  -0.1218 -0.0162 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.4226 0.2809 0.2738 0.0155  -0.1167 -0.0168 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.4411 0.2419 0.2589 0.0092  -0.1499 -0.0084 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.4100 0.2604 0.2976 0.0146  -0.1386 -0.0091 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.4247 0.2420 0.2971 0.0101  -0.1620 -0.0020 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3942 0.2388 0.1347 0.0201  -0.0490 -0.0134 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3845 0.2470 0.1349 0.0208  -0.0267 -0.0054 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.3352 0.2490 0.1285 0.0147  -0.0275 0.0000  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.3036 0.2351 0.1143 0.0148  -0.0322 0.0003  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.4000 0.2405 0.1372 0.0287  -0.0043 0.0020  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.4660 0.2361 0.1399 0.0301  0.0041  -0.0022 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.5084 0.2502 0.1558 0.0284  0.0180  -0.0016 72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.5131 0.2363 0.1451 0.0305  0.0003  -0.0056 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.5765 0.2392 0.1508 0.0261  0.0283  -0.0055 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5872 0.2283 0.1424 0.0264  0.0091  -0.0085 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.6287 0.2368 0.1521 0.0237  0.0236  -0.0089 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.7238 0.2370 0.1564 0.0157  0.0323  -0.0125 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.3359 0.2679 0.1404 0.0066  -0.0239 0.0059  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.3134 0.2820 0.1459 -0.0059 -0.0288 0.0152  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.3099 0.3004 0.1763 -0.0032 -0.0199 0.0347  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.3238 0.3053 0.1983 0.0056  -0.0019 0.0441  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.3266 0.2968 0.1523 -0.0181 -0.0310 0.0174  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.3487 0.2944 0.1583 -0.0083 -0.0194 0.0162  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.3430 0.2566 0.1292 0.0056  -0.0171 0.0063  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2941 0.3078 0.1812 -0.0100 -0.0291 0.0418  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2870 0.3241 0.2170 -0.0077 -0.0237 0.0642  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2752 0.3415 0.2303 -0.0293 -0.0448 0.0823  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2894 0.3490 0.2146 -0.0452 -0.0601 0.0717  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.3076 0.3335 0.2354 0.0081  -0.0140 0.0586  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3374 0.3240 0.2396 0.0253  0.0090  0.0514  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.3284 0.3495 0.2320 0.0038  -0.0293 0.0407  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2514 0.3441 0.2618 -0.0312 -0.0445 0.1119  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2420 0.3587 0.2795 -0.0542 -0.0715 0.1355  75  SER   A CA  
544  C C   . SER   A 69  ? 0.2308 0.3557 0.2929 -0.0402 -0.0644 0.1401  75  SER   A C   
545  O O   . SER   A 69  ? 0.2338 0.3566 0.3231 -0.0162 -0.0365 0.1435  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2378 0.3824 0.3384 -0.0661 -0.0806 0.1732  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2947 0.4304 0.3685 -0.0839 -0.0919 0.1708  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.2189 0.3445 0.2640 -0.0557 -0.0855 0.1391  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2097 0.3410 0.2734 -0.0425 -0.0791 0.1413  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2259 0.3749 0.3154 -0.0650 -0.1081 0.1678  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2524 0.3957 0.3186 -0.0964 -0.1372 0.1767  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2121 0.3168 0.2219 -0.0303 -0.0683 0.1060  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2110 0.2963 0.1676 -0.0487 -0.0814 0.0854  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2204 0.2868 0.1442 -0.0487 -0.0751 0.0662  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2181 0.2981 0.1568 -0.0662 -0.0959 0.0859  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2489 0.2919 0.1300 -0.0637 -0.0781 0.0490  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2444 0.2953 0.1312 -0.0817 -0.0967 0.0658  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2540 0.2868 0.1158 -0.0796 -0.0855 0.0480  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2105 0.3752 0.3462 -0.0515 -0.1013 0.1838  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2154 0.3976 0.3846 -0.0731 -0.1323 0.2146  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2544 0.4120 0.3565 -0.0908 -0.1498 0.1944  77  SER   A C   
562  O O   . SER   A 71  ? 0.2778 0.4107 0.3221 -0.0821 -0.1335 0.1581  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1973 0.4051 0.4503 -0.0516 -0.1158 0.2430  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2341 0.4235 0.4620 -0.0233 -0.0832 0.2163  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2547 0.4155 0.3659 -0.1180 -0.1837 0.2204  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.3070 0.4370 0.3521 -0.1372 -0.1974 0.2041  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.3024 0.4385 0.3604 -0.1090 -0.1745 0.1900  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2702 0.4334 0.3948 -0.0839 -0.1592 0.2063  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3447 0.4676 0.3895 -0.1792 -0.2451 0.2406  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4489 0.5552 0.4672 -0.2129 -0.2717 0.2546  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.6021 0.6544 0.5361 -0.2646 -0.3112 0.2622  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.7191 0.7248 0.5721 -0.2922 -0.3147 0.2473  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.8322 0.7592 0.5652 -0.3324 -0.3246 0.2310  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3424 0.4497 0.3389 -0.1117 -0.1675 0.1604  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3516 0.4639 0.3603 -0.0868 -0.1487 0.1486  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3436 0.4767 0.4045 -0.0895 -0.1653 0.1820  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3525 0.4782 0.4036 -0.1215 -0.1993 0.2038  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3953 0.4724 0.3345 -0.0984 -0.1442 0.1182  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4200 0.4723 0.3132 -0.1165 -0.1445 0.1054  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3811 0.4452 0.2963 -0.1375 -0.1718 0.1376  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.3209 0.4733 0.4353 -0.0582 -0.1418 0.1889  80  SER   A N   
582  C CA  . SER   A 74  ? 0.3053 0.4788 0.4832 -0.0564 -0.1519 0.2238  80  SER   A CA  
583  C C   . SER   A 74  ? 0.3054 0.4767 0.5025 -0.0226 -0.1174 0.2149  80  SER   A C   
584  O O   . SER   A 74  ? 0.3224 0.4724 0.4757 -0.0047 -0.0915 0.1817  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2981 0.5023 0.5577 -0.0614 -0.1641 0.2669  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3217 0.5319 0.6096 -0.0344 -0.1277 0.2613  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2821 0.4702 0.5418 -0.0170 -0.1199 0.2464  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2942 0.4739 0.5737 0.0127  -0.0854 0.2435  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2912 0.4750 0.6289 0.0384  -0.0468 0.2590  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2616 0.4749 0.6848 0.0356  -0.0533 0.2997  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2747 0.4708 0.6079 0.0064  -0.1040 0.2773  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.3222 0.5021 0.5987 -0.0084 -0.1248 0.2608  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3097 0.5077 0.6474 -0.0196 -0.1512 0.3025  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3558 0.5078 0.5825 0.0152  -0.0907 0.2249  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.3194 0.4689 0.6127 0.0612  -0.0071 0.2300  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.3232 0.4585 0.6540 0.0851  0.0388  0.2410  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3764 0.4637 0.6744 0.1091  0.0821  0.2266  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.4100 0.4670 0.6270 0.1067  0.0765  0.1933  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3416 0.4640 0.6281 0.0821  0.0430  0.2192  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3160 0.4805 0.6513 0.0617  0.0115  0.2431  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3615 0.4395 0.6349 0.1064  0.0970  0.2123  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3516 0.5120 0.6174 0.0419  -0.0166 0.2148  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3813 0.4570 0.7424 0.1307  0.1264  0.2533  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.4412 0.4558 0.7586 0.1515  0.1736  0.2398  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.4964 0.4443 0.7147 0.1567  0.2021  0.2049  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4926 0.4369 0.7147 0.1574  0.2143  0.2054  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.4275 0.4401 0.8422 0.1737  0.2212  0.2797  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4943 0.4253 0.8622 0.1971  0.2886  0.2690  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.5332 0.4343 0.8647 0.2018  0.2947  0.2605  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.5341 0.4104 0.8904 0.2127  0.3488  0.2690  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.5927 0.4071 0.8714 0.2203  0.3586  0.2518  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5960 0.3802 0.8956 0.2308  0.4158  0.2599  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.6174 0.3696 0.8763 0.2338  0.4198  0.2513  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.5471 0.4415 0.6735 0.1563  0.2053  0.1757  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.6150 0.4364 0.6368 0.1551  0.2218  0.1451  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.6801 0.4171 0.6476 0.1683  0.2712  0.1413  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.6887 0.4225 0.6499 0.1690  0.2648  0.1408  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.6326 0.4625 0.5875 0.1350  0.1690  0.1150  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.6932 0.4430 0.5427 0.1303  0.1783  0.0891  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.5973 0.4967 0.5960 0.1216  0.1291  0.1176  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.7283 0.3898 0.6517 0.1775  0.3238  0.1390  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.7957 0.3547 0.6494 0.1876  0.3805  0.1347  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.8541 0.3512 0.5859 0.1704  0.3524  0.1049  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.8604 0.3770 0.5504 0.1515  0.2980  0.0855  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.8812 0.3594 0.6951 0.1958  0.4427  0.1355  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.9118 0.4492 0.8572 0.2133  0.4746  0.1692  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 1.0664 0.5109 0.9884 0.2284  0.5603  0.1766  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.1470 0.4909 1.0010 0.2364  0.6172  0.1720  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.0846 0.5503 1.0518 0.2314  0.5739  0.1870  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.8929 0.3121 0.5712 0.1763  0.3910  0.1038  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.9607 0.3110 0.5229 0.1583  0.3672  0.0805  86  ALA   A CA  
632  C C   . ALA   A 80  ? 1.0225 0.3021 0.4658 0.1347  0.3419  0.0567  86  ALA   A C   
633  O O   . ALA   A 80  ? 1.0583 0.2884 0.4675 0.1353  0.3725  0.0557  86  ALA   A O   
634  C CB  . ALA   A 80  ? 1.0132 0.2649 0.5223 0.1686  0.4293  0.0848  86  ALA   A CB  
635  N N   . SER   A 81  ? 1.0368 0.3077 0.4194 0.1128  0.2862  0.0405  87  SER   A N   
636  C CA  . SER   A 81  ? 1.0950 0.2980 0.3700 0.0862  0.2509  0.0233  87  SER   A CA  
637  C C   . SER   A 81  ? 1.1446 0.2893 0.3343 0.0645  0.2170  0.0135  87  SER   A C   
638  O O   . SER   A 81  ? 1.1266 0.2960 0.3486 0.0726  0.2215  0.0178  87  SER   A O   
639  C CB  . SER   A 81  ? 1.0529 0.3511 0.3913 0.0795  0.1956  0.0202  87  SER   A CB  
640  O OG  . SER   A 81  ? 1.0289 0.4077 0.4206 0.0730  0.1422  0.0178  87  SER   A OG  
641  N N   . GLU   A 82  ? 1.1998 0.2696 0.2855 0.0350  0.1777  0.0030  88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.2405 0.2601 0.2545 0.0101  0.1359  -0.0018 88  GLU   A CA  
643  C C   . GLU   A 82  ? 1.1406 0.2814 0.2566 0.0098  0.0784  0.0000  88  GLU   A C   
644  O O   . GLU   A 82  ? 1.1628 0.2802 0.2440 -0.0080 0.0441  -0.0011 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.3816 0.2801 0.2568 -0.0263 0.1037  -0.0073 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.4458 0.4030 0.3593 -0.0428 0.0350  -0.0063 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.5908 0.4870 0.4292 -0.0812 -0.0321 -0.0031 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.5848 0.5071 0.4474 -0.0843 -0.0524 -0.0006 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.6647 0.4854 0.4217 -0.1097 -0.0666 -0.0006 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 1.0363 0.2993 0.2743 0.0280  0.0714  0.0034  89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.9422 0.3106 0.2714 0.0274  0.0268  0.0041  89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.8665 0.3116 0.2835 0.0500  0.0517  0.0107  89  TYR   A C   
653  O O   . TYR   A 83  ? 0.8378 0.3289 0.2922 0.0470  0.0276  0.0104  89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.8901 0.3276 0.2789 0.0250  -0.0045 0.0029  89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.9376 0.3054 0.2521 0.0054  -0.0262 0.0002  89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.9706 0.3038 0.2460 -0.0212 -0.0792 0.0014  89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.9594 0.2981 0.2498 0.0117  0.0027  -0.0005 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 1.0214 0.2869 0.2286 -0.0429 -0.1064 0.0030  89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 1.0165 0.2844 0.2311 -0.0086 -0.0189 -0.0025 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 1.0553 0.2856 0.2267 -0.0368 -0.0758 -0.0001 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.1257 0.2833 0.2229 -0.0604 -0.1043 0.0019  89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.8303 0.2903 0.2858 0.0708  0.0975  0.0193  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.7634 0.2981 0.3111 0.0893  0.1142  0.0317  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.7830 0.2742 0.3325 0.1090  0.1756  0.0452  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.8096 0.2463 0.3271 0.1149  0.2133  0.0473  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.6845 0.3131 0.3228 0.0948  0.1001  0.0383  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.6426 0.3212 0.2975 0.0792  0.0500  0.0274  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.6358 0.3170 0.2834 0.0730  0.0368  0.0218  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.6137 0.3363 0.2974 0.0717  0.0207  0.0240  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.6078 0.3339 0.2811 0.0611  -0.0024 0.0143  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.5907 0.3549 0.2981 0.0594  -0.0151 0.0159  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.5861 0.3530 0.2917 0.0549  -0.0254 0.0117  90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.5611 0.3634 0.2950 0.0443  -0.0552 0.0055  90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.7579 0.2814 0.3618 0.1213  0.1894  0.0578  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.7635 0.2607 0.4015 0.1440  0.2513  0.0775  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.7128 0.2863 0.4593 0.1575  0.2612  0.0984  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.6850 0.3247 0.4655 0.1476  0.2196  0.0946  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.7516 0.2643 0.4178 0.1499  0.2523  0.0860  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.7210 0.3065 0.4084 0.1333  0.1882  0.0760  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.7138 0.3011 0.3600 0.1157  0.1514  0.0576  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.7005 0.2628 0.5052 0.1791  0.3166  0.1228  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.6438 0.2792 0.5629 0.1899  0.3230  0.1491  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.5609 0.3019 0.5695 0.1823  0.2681  0.1635  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.5519 0.3079 0.5976 0.1876  0.2683  0.1774  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.6453 0.2458 0.6234 0.2153  0.3963  0.1779  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.5024 0.3067 0.5359 0.1678  0.2224  0.1599  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.4345 0.3192 0.5255 0.1540  0.1698  0.1698  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3821 0.3283 0.5302 0.1436  0.1419  0.1824  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3914 0.3212 0.5279 0.1472  0.1596  0.1779  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.4579 0.3350 0.4708 0.1363  0.1307  0.1376  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.4761 0.3438 0.4340 0.1244  0.1117  0.1126  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.5019 0.3375 0.3812 0.1119  0.0887  0.0840  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.4611 0.3308 0.3348 0.0959  0.0510  0.0691  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.4527 0.3135 0.3074 0.0928  0.0485  0.0606  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.4014 0.2914 0.2568 0.0795  0.0178  0.0485  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4630 0.2808 0.2977 0.1031  0.0806  0.0647  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.3317 0.3391 0.5269 0.1268  0.0963  0.1962  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2985 0.3509 0.5244 0.1107  0.0655  0.2043  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2962 0.3452 0.4439 0.0919  0.0329  0.1683  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.3065 0.3572 0.4257 0.0812  0.0112  0.1567  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2676 0.3734 0.5721 0.0956  0.0303  0.2403  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2599 0.3857 0.6731 0.1101  0.0516  0.2871  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2386 0.4048 0.7345 0.1023  0.0374  0.3222  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2772 0.3867 0.7203 0.1277  0.0785  0.3013  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2083 0.4007 0.8250 0.1134  0.0510  0.3729  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2496 0.3817 0.8092 0.1409  0.0970  0.3496  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2263 0.4020 0.8788 0.1341  0.0831  0.3870  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2119 0.4143 0.9986 0.1471  0.0998  0.4414  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2785 0.3214 0.3974 0.0885  0.0323  0.1526  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2690 0.3101 0.3305 0.0727  0.0062  0.1233  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2325 0.3136 0.3188 0.0506  -0.0267 0.1338  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2180 0.3196 0.3457 0.0481  -0.0282 0.1538  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2860 0.2943 0.3026 0.0791  0.0211  0.1030  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2749 0.2857 0.2511 0.0644  -0.0044 0.0783  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.3227 0.2896 0.2466 0.0699  0.0047  0.0587  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.3752 0.2962 0.2643 0.0793  0.0228  0.0550  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2828 0.2555 0.1941 0.0616  -0.0094 0.0469  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.2255 0.3109 0.2832 0.0327  -0.0512 0.1219  96  SER   A N   
719  C CA  . SER   A 90  ? 0.2171 0.3208 0.2752 0.0063  -0.0804 0.1295  96  SER   A CA  
720  C C   . SER   A 90  ? 0.2300 0.3239 0.2479 -0.0022 -0.0825 0.1057  96  SER   A C   
721  O O   . SER   A 90  ? 0.2396 0.3156 0.2305 0.0105  -0.0677 0.0822  96  SER   A O   
722  C CB  . SER   A 90  ? 0.2360 0.3361 0.2750 -0.0117 -0.1002 0.1300  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2902 0.3689 0.2824 -0.0096 -0.0922 0.0995  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.2220 0.3229 0.2353 -0.0257 -0.1026 0.1144  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2382 0.3261 0.2137 -0.0365 -0.1029 0.0945  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2299 0.3198 0.2153 -0.0177 -0.0859 0.0870  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2378 0.3136 0.1946 -0.0169 -0.0797 0.0651  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2595 0.3241 0.1913 -0.0417 -0.0971 0.0671  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.3020 0.3533 0.2096 -0.0652 -0.1111 0.0723  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3548 0.3806 0.2191 -0.0956 -0.1215 0.0715  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.3051 0.3569 0.2180 -0.0644 -0.1155 0.0788  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3774 0.3852 0.2172 -0.1138 -0.1322 0.0769  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3447 0.3717 0.2169 -0.0950 -0.1302 0.0818  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.2124 0.3162 0.2408 -0.0031 -0.0763 0.1073  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.2164 0.3119 0.2472 0.0145  -0.0556 0.1013  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1967 0.3094 0.2536 0.0051  -0.0622 0.1184  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1633 0.2986 0.2611 -0.0077 -0.0785 0.1469  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.2141 0.2986 0.2673 0.0381  -0.0290 0.1106  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2475 0.3046 0.2856 0.0548  -0.0020 0.1030  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2715 0.2974 0.2489 0.0548  -0.0056 0.0730  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2666 0.3017 0.3244 0.0751  0.0321  0.1167  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.2119 0.3129 0.2470 0.0093  -0.0534 0.1038  99  MET   A N   
743  C CA  . MET   A 93  ? 0.2098 0.3254 0.2664 -0.0006 -0.0595 0.1189  99  MET   A CA  
744  C C   . MET   A 93  ? 0.2246 0.3284 0.2904 0.0195  -0.0321 0.1180  99  MET   A C   
745  O O   . MET   A 93  ? 0.2597 0.3347 0.2812 0.0293  -0.0208 0.0935  99  MET   A O   
746  C CB  . MET   A 93  ? 0.2296 0.3354 0.2413 -0.0201 -0.0753 0.1011  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2554 0.3551 0.2396 -0.0433 -0.0955 0.0981  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.3122 0.3826 0.2360 -0.0613 -0.0969 0.0720  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2304 0.2891 0.1455 -0.0356 -0.0757 0.0445  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1965 0.3183 0.3197 0.0235  -0.0219 0.1466  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.2119 0.3132 0.3396 0.0420  0.0120  0.1462  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.2146 0.3222 0.3401 0.0322  0.0057  0.1466  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1991 0.3355 0.3488 0.0113  -0.0220 0.1626  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1917 0.3008 0.3914 0.0582  0.0419  0.1778  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2215 0.3109 0.4180 0.0734  0.0611  0.1762  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.1904 0.2890 0.4726 0.0895  0.0948  0.2124  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2731 0.3041 0.3856 0.0853  0.0825  0.1427  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.2365 0.3103 0.3284 0.0450  0.0311  0.1312  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2508 0.3233 0.3369 0.0395  0.0321  0.1302  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2704 0.3079 0.3576 0.0585  0.0757  0.1336  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2801 0.2768 0.3379 0.0734  0.1023  0.1248  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2823 0.3345 0.2998 0.0315  0.0141  0.0987  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2813 0.3254 0.3929 0.0560  0.0853  0.1454  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.3215 0.3212 0.4223 0.0720  0.1317  0.1459  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3749 0.3280 0.3821 0.0686  0.1242  0.1124  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3783 0.3504 0.3722 0.0550  0.0952  0.1038  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.3023 0.3304 0.4816 0.0713  0.1485  0.1774  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3315 0.3009 0.4861 0.0872  0.2035  0.1738  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2607 0.3384 0.5481 0.0726  0.1491  0.2179  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.4153 0.3042 0.3563 0.0783  0.1466  0.0951  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4693 0.3072 0.3223 0.0726  0.1335  0.0680  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.5233 0.2820 0.3003 0.0784  0.1538  0.0550  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.5332 0.2815 0.3226 0.0873  0.1750  0.0626  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.5617 0.2577 0.2549 0.0708  0.1454  0.0369  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.6265 0.2325 0.2291 0.0685  0.1562  0.0256  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.6327 0.2443 0.2186 0.0626  0.1190  0.0167  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.6035 0.2576 0.2078 0.0547  0.0754  0.0099  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.6915 0.2178 0.2028 0.0570  0.1538  0.0134  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.7933 0.2121 0.1956 0.0476  0.1596  0.0041  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.8615 0.2083 0.2226 0.0546  0.2156  0.0084  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.8514 0.2254 0.1853 0.0302  0.1144  -0.0060 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.9408 0.1923 0.1932 0.0388  0.2024  -0.0019 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.9423 0.2092 0.1781 0.0226  0.1378  -0.0090 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.6840 0.2411 0.2286 0.0657  0.1406  0.0166  105 SER   A N   
785  C CA  . SER   A 99  ? 0.7257 0.2726 0.2436 0.0586  0.1094  0.0093  105 SER   A CA  
786  C C   . SER   A 99  ? 0.8228 0.2662 0.2511 0.0562  0.1394  0.0067  105 SER   A C   
787  O O   . SER   A 99  ? 0.8486 0.2584 0.2755 0.0683  0.1949  0.0147  105 SER   A O   
788  C CB  . SER   A 99  ? 0.6831 0.3176 0.2894 0.0673  0.1000  0.0171  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.6931 0.3390 0.3448 0.0823  0.1451  0.0327  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.8772 0.2661 0.2327 0.0392  0.1040  -0.0021 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.9659 0.2475 0.2216 0.0308  0.1238  -0.0051 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.9838 0.2718 0.2289 0.0179  0.0736  -0.0079 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.9285 0.2931 0.2370 0.0146  0.0259  -0.0080 106 GLU   A O   
794  C CB  . GLU   A 100 ? 1.0792 0.2325 0.2090 0.0142  0.1419  -0.0106 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 1.1412 0.2738 0.2270 -0.0090 0.0823  -0.0150 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.2475 0.2511 0.2066 -0.0269 0.1021  -0.0191 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.3758 0.2551 0.2112 -0.0465 0.1098  -0.0219 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.2032 0.2217 0.1782 -0.0232 0.1119  -0.0196 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 1.0481 0.2589 0.2213 0.0111  0.0866  -0.0090 107 PRO   A N   
800  C CA  . PRO   A 101 ? 1.0491 0.2712 0.2205 -0.0023 0.0363  -0.0094 107 PRO   A CA  
801  C C   . PRO   A 101 ? 1.0634 0.2586 0.1963 -0.0282 -0.0265 -0.0092 107 PRO   A C   
802  O O   . PRO   A 101 ? 1.1456 0.2445 0.1806 -0.0462 -0.0280 -0.0105 107 PRO   A O   
803  C CB  . PRO   A 101 ? 1.1287 0.2436 0.2015 -0.0092 0.0672  -0.0107 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 1.1488 0.2280 0.2118 0.0101  0.1439  -0.0094 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 1.1089 0.2115 0.1959 0.0137  0.1495  -0.0094 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.9725 0.2545 0.1902 -0.0291 -0.0739 -0.0058 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.9432 0.2283 0.1681 -0.0483 -0.1331 -0.0002 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.8448 0.2407 0.1833 -0.0322 -0.1388 -0.0005 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.8192 0.2467 0.2035 -0.0413 -0.1831 0.0060  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.7839 0.2366 0.1720 -0.0094 -0.0933 -0.0056 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.7021 0.2487 0.1834 0.0028  -0.0946 -0.0063 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.6333 0.2652 0.2017 0.0117  -0.1011 -0.0058 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.5908 0.2855 0.2254 0.0150  -0.1116 -0.0063 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.6971 0.2562 0.1854 0.0168  -0.0505 -0.0078 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.7559 0.2466 0.1757 0.0077  -0.0473 -0.0093 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.7759 0.2388 0.1703 -0.0084 -0.0885 -0.0083 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.7702 0.2329 0.1652 0.0160  -0.0033 -0.0093 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.6221 0.2481 0.1839 0.0138  -0.0939 -0.0051 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.5706 0.2660 0.2035 0.0196  -0.1000 -0.0049 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.5278 0.2534 0.2085 0.0106  -0.1377 -0.0029 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.5540 0.2338 0.2046 -0.0038 -0.1698 0.0026  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.6055 0.2718 0.2090 0.0189  -0.0942 -0.0038 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.6933 0.3392 0.2731 0.0349  -0.0402 -0.0019 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.4639 0.2579 0.2160 0.0172  -0.1324 -0.0051 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.4285 0.2494 0.2365 0.0117  -0.1560 -0.0020 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.4096 0.2498 0.2419 0.0138  -0.1523 -0.0036 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.3912 0.2613 0.2815 0.0133  -0.1578 -0.0018 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.4098 0.2318 0.2011 0.0169  -0.1377 -0.0066 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.3759 0.2150 0.1845 0.0185  -0.1322 -0.0087 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.3119 0.2051 0.1667 0.0231  -0.1113 -0.0132 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2842 0.1951 0.1358 0.0264  -0.0940 -0.0140 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2820 0.1947 0.1783 0.0213  -0.1133 -0.0144 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2617 0.2072 0.1856 0.0204  -0.0925 -0.0194 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2594 0.2127 0.1599 0.0189  -0.0778 -0.0214 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2704 0.2093 0.1538 0.0199  -0.0812 -0.0206 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2614 0.2116 0.2369 0.0193  -0.0929 -0.0187 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2528 0.2089 0.2675 0.0193  -0.0984 -0.0147 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2669 0.2276 0.2502 0.0155  -0.0665 -0.0256 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2384 0.1972 0.3258 0.0203  -0.1000 -0.0066 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.2421 0.2154 0.1414 0.0141  -0.0647 -0.0213 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.2416 0.2247 0.1282 0.0071  -0.0560 -0.0186 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.2638 0.2458 0.1551 -0.0047 -0.0456 -0.0251 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2525 0.2333 0.1527 -0.0091 -0.0386 -0.0288 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2196 0.2184 0.1029 0.0050  -0.0537 -0.0085 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2157 0.2287 0.0962 -0.0093 -0.0524 0.0008  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2160 0.2289 0.0942 -0.0067 -0.0503 0.0075  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2171 0.2478 0.1102 -0.0130 -0.0558 0.0155  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2849 0.2594 0.1652 -0.0104 -0.0409 -0.0268 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.3108 0.2690 0.1840 -0.0222 -0.0248 -0.0338 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.3311 0.2828 0.1695 -0.0393 -0.0236 -0.0301 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.3299 0.2918 0.1648 -0.0370 -0.0332 -0.0235 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.3454 0.2909 0.2429 -0.0128 -0.0198 -0.0386 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.4172 0.3569 0.3580 -0.0058 -0.0100 -0.0409 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.4934 0.4170 0.4637 -0.0013 0.0023  -0.0418 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.5605 0.4763 0.5825 0.0029  0.0233  -0.0412 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.5876 0.5152 0.6722 0.0142  0.0084  -0.0311 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.5862 0.5238 0.6741 0.0195  -0.0291 -0.0227 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.5787 0.5017 0.7213 0.0179  0.0315  -0.0274 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.3571 0.2829 0.1656 -0.0584 -0.0097 -0.0344 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3876 0.2940 0.1528 -0.0808 -0.0109 -0.0305 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.4277 0.2907 0.1724 -0.0867 0.0175  -0.0438 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.4140 0.2750 0.1965 -0.0693 0.0344  -0.0516 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.4009 0.2994 0.1319 -0.1058 -0.0228 -0.0201 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.4550 0.3146 0.1582 -0.1177 -0.0010 -0.0311 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4728 0.2967 0.1601 -0.1124 0.0239  -0.0441 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.5240 0.2946 0.1845 -0.1188 0.0594  -0.0571 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.5442 0.2791 0.1975 -0.1221 0.0915  -0.0664 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5639 0.2652 0.2297 -0.1147 0.1296  -0.0760 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.6154 0.3378 0.1977 -0.1518 0.0592  -0.0551 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.7196 0.4203 0.2420 -0.1859 0.0381  -0.0443 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.8421 0.4940 0.2866 -0.2229 0.0272  -0.0374 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.8561 0.5333 0.2976 -0.2395 -0.0128 -0.0173 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.9109 0.4880 0.2932 -0.2377 0.0639  -0.0518 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.5325 0.2709 0.1685 -0.1333 0.0796  -0.0621 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.5362 0.2346 0.1577 -0.1391 0.1122  -0.0710 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4800 0.2175 0.1872 -0.1077 0.1217  -0.0732 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.5020 0.2072 0.2121 -0.1089 0.1560  -0.0802 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.5675 0.2387 0.1219 -0.1702 0.0968  -0.0653 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5797 0.2609 0.0943 -0.1939 0.0533  -0.0490 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.5134 0.2686 0.0860 -0.1777 0.0138  -0.0333 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.6543 0.2769 0.0812 -0.2334 0.0449  -0.0433 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.5586 0.3075 0.0957 -0.2029 -0.0145 -0.0178 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.6519 0.3215 0.0970 -0.2404 -0.0030 -0.0216 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4074 0.2057 0.1782 -0.0830 0.0927  -0.0662 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3547 0.1879 0.2016 -0.0578 0.0901  -0.0642 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.3202 0.2009 0.1846 -0.0486 0.0523  -0.0559 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.3336 0.2320 0.1734 -0.0532 0.0277  -0.0495 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2835 0.1814 0.1930 -0.0358 0.0507  -0.0544 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2769 0.2098 0.2018 -0.0260 0.0204  -0.0475 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2892 0.2248 0.1696 -0.0404 0.0109  -0.0443 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.3079 0.2196 0.1623 -0.0553 0.0269  -0.0482 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2638 0.2066 0.2447 -0.0132 0.0211  -0.0455 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2699 0.2364 0.2506 -0.0066 -0.0071 -0.0396 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2383 0.1828 0.2771 -0.0004 0.0198  -0.0407 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2698 0.2288 0.1418 -0.0377 -0.0128 -0.0353 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2726 0.2417 0.1220 -0.0490 -0.0264 -0.0251 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2749 0.2645 0.1489 -0.0350 -0.0359 -0.0213 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2886 0.2775 0.1534 -0.0434 -0.0375 -0.0181 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2702 0.2529 0.1117 -0.0525 -0.0409 -0.0131 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2657 0.2659 0.1076 -0.0612 -0.0574 0.0046  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2922 0.2503 0.1017 -0.0699 -0.0342 -0.0161 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.2545 0.2545 0.1511 -0.0164 -0.0429 -0.0211 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.2524 0.2601 0.1606 -0.0051 -0.0507 -0.0178 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.2402 0.2397 0.1545 0.0090  -0.0592 -0.0184 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.2431 0.2339 0.1627 0.0106  -0.0608 -0.0218 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.2376 0.2320 0.1453 0.0169  -0.0651 -0.0141 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2450 0.2136 0.1382 0.0246  -0.0752 -0.0138 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2556 0.2089 0.1215 0.0315  -0.0677 -0.0073 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2301 0.1956 0.1015 0.0336  -0.0593 -0.0016 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2592 0.2157 0.1636 0.0241  -0.0894 -0.0152 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2598 0.2296 0.1724 0.0231  -0.0842 -0.0151 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2557 0.2153 0.1969 0.0207  -0.0971 -0.0167 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2879 0.2388 0.1977 0.0232  -0.0987 -0.0133 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2755 0.1931 0.1096 0.0348  -0.0693 -0.0071 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.3129 0.2002 0.1145 0.0419  -0.0520 -0.0015 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.3482 0.2174 0.1353 0.0442  -0.0505 -0.0002 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.3560 0.2121 0.1360 0.0382  -0.0709 -0.0045 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.3566 0.1909 0.1093 0.0407  -0.0528 -0.0036 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3974 0.1828 0.1060 0.0474  -0.0250 0.0011  124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3543 0.2081 0.1223 0.0395  -0.0511 -0.0042 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.3563 0.2303 0.1506 0.0523  -0.0274 0.0084  125 SER   A N   
922  C CA  . SER   A 119 ? 0.3870 0.2448 0.1700 0.0556  -0.0220 0.0104  125 SER   A CA  
923  C C   . SER   A 119 ? 0.4449 0.2572 0.1982 0.0659  0.0115  0.0181  125 SER   A C   
924  O O   . SER   A 119 ? 0.4755 0.2389 0.1851 0.0663  0.0179  0.0158  125 SER   A O   
925  C CB  . SER   A 119 ? 0.3650 0.2772 0.1981 0.0547  -0.0258 0.0157  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.4037 0.3015 0.2279 0.0584  -0.0202 0.0181  125 SER   A OG  
927  N N   . THR   A 120 ? 0.4586 0.2840 0.2385 0.0738  0.0362  0.0289  126 THR   A N   
928  C CA  . THR   A 120 ? 0.5085 0.2895 0.2738 0.0861  0.0794  0.0392  126 THR   A CA  
929  C C   . THR   A 120 ? 0.5496 0.3106 0.3046 0.0880  0.0983  0.0412  126 THR   A C   
930  O O   . THR   A 120 ? 0.5411 0.3264 0.3006 0.0797  0.0742  0.0347  126 THR   A O   
931  C CB  . THR   A 120 ? 0.4841 0.3077 0.3208 0.0972  0.0994  0.0601  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.4484 0.3346 0.3547 0.0956  0.0922  0.0750  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.4837 0.3298 0.3314 0.0941  0.0795  0.0584  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.5910 0.3050 0.3336 0.0992  0.1452  0.0507  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.6335 0.3260 0.3716 0.1023  0.1712  0.0549  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.6984 0.3190 0.4123 0.1155  0.2340  0.0643  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.7229 0.3054 0.4173 0.1219  0.2573  0.0666  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.7267 0.3218 0.4377 0.1191  0.2654  0.0692  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.7847 0.3010 0.4716 0.1319  0.3361  0.0783  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.7531 0.3180 0.5458 0.1462  0.3728  0.1050  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.6896 0.3526 0.5928 0.1496  0.3492  0.1253  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.7988 0.2897 0.5544 0.1515  0.4289  0.1066  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.7695 0.2884 0.6212 0.1654  0.4753  0.1337  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.7006 0.3118 0.6214 0.1566  0.4287  0.1410  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.6503 0.3335 0.6941 0.1643  0.4369  0.1722  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.7584 0.3136 0.7267 0.1859  0.5163  0.1672  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.8795 0.3347 0.7791 0.1960  0.5725  0.1611  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.9779 0.3153 0.7793 0.1970  0.6313  0.1489  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.8555 0.3471 0.7963 0.2015  0.5568  0.1693  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.6971 0.3007 0.5396 0.1391  0.3806  0.1148  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.6308 0.3096 0.5210 0.1289  0.3370  0.1177  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.5464 0.3212 0.4998 0.1205  0.2764  0.1228  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.5062 0.3422 0.5037 0.1104  0.2429  0.1288  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.5223 0.3035 0.4729 0.1224  0.2634  0.1200  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4664 0.3255 0.4655 0.1128  0.2110  0.1239  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4757 0.3135 0.3957 0.1031  0.1747  0.0948  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.5285 0.3012 0.3824 0.1072  0.1919  0.0822  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.4343 0.3258 0.5147 0.1233  0.2267  0.1511  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.4130 0.3360 0.5995 0.1328  0.2594  0.1889  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3946 0.3307 0.6575 0.1470  0.2856  0.2170  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3839 0.3810 0.6322 0.1156  0.2143  0.2049  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.4233 0.3108 0.3511 0.0890  0.1264  0.0863  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.4144 0.2920 0.2910 0.0806  0.0931  0.0639  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.3642 0.3013 0.2906 0.0744  0.0664  0.0712  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.3315 0.3187 0.3104 0.0664  0.0530  0.0859  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.4305 0.2934 0.2601 0.0699  0.0679  0.0446  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.4002 0.3104 0.2708 0.0625  0.0561  0.0515  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.4397 0.3018 0.2419 0.0618  0.0339  0.0281  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.3571 0.2817 0.2622 0.0756  0.0591  0.0629  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.3220 0.2917 0.2623 0.0685  0.0361  0.0679  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.3158 0.2874 0.2246 0.0576  0.0066  0.0471  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.3441 0.2766 0.2072 0.0592  0.0036  0.0321  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.2714 0.2825 0.2045 0.0443  -0.0147 0.0486  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.2434 0.2563 0.1579 0.0342  -0.0341 0.0312  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.2195 0.2501 0.1455 0.0262  -0.0441 0.0324  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1960 0.2497 0.1443 0.0166  -0.0496 0.0471  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.2211 0.2465 0.1367 0.0225  -0.0424 0.0279  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.2204 0.2305 0.1248 0.0280  -0.0343 0.0269  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2384 0.2205 0.1144 0.0311  -0.0383 0.0123  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.2159 0.2403 0.1425 0.0271  -0.0261 0.0430  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2517 0.2155 0.1114 0.0336  -0.0329 0.0112  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.2238 0.2322 0.1380 0.0310  -0.0170 0.0412  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2380 0.2137 0.1135 0.0342  -0.0199 0.0240  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.2198 0.2366 0.1301 0.0271  -0.0493 0.0188  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.2222 0.2499 0.1386 0.0192  -0.0556 0.0174  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.2408 0.2750 0.1543 0.0029  -0.0604 0.0106  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.2497 0.2735 0.1597 0.0029  -0.0591 -0.0019 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.2310 0.2396 0.1360 0.0251  -0.0583 0.0067  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.2468 0.2913 0.1599 -0.0129 -0.0657 0.0207  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2786 0.3117 0.1702 -0.0330 -0.0661 0.0141  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.3086 0.3246 0.1903 -0.0367 -0.0564 -0.0013 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.3237 0.3432 0.2141 -0.0301 -0.0574 -0.0015 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.3054 0.3419 0.1876 -0.0550 -0.0805 0.0327  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3611 0.3683 0.2001 -0.0821 -0.0807 0.0271  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3181 0.3159 0.1469 -0.0832 -0.0732 0.0192  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4426 0.4284 0.2508 -0.1036 -0.0865 0.0301  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.3101 0.3054 0.1784 -0.0456 -0.0431 -0.0135 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.3151 0.2898 0.1832 -0.0493 -0.0247 -0.0261 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.3357 0.2697 0.1576 -0.0750 -0.0070 -0.0318 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3511 0.2576 0.1656 -0.0812 0.0165  -0.0414 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.3106 0.2891 0.2199 -0.0318 -0.0163 -0.0341 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2959 0.2949 0.2272 -0.0136 -0.0362 -0.0282 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.3214 0.2864 0.2301 -0.0342 -0.0038 -0.0390 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3459 0.2686 0.1332 -0.0917 -0.0157 -0.0252 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3904 0.2593 0.1160 -0.1207 -0.0001 -0.0303 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.4387 0.2664 0.1127 -0.1457 0.0047  -0.0305 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4808 0.2473 0.1004 -0.1663 0.0331  -0.0414 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3932 0.2575 0.0885 -0.1379 -0.0201 -0.0185 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3662 0.2535 0.0951 -0.1188 -0.0169 -0.0219 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3785 0.2676 0.0851 -0.1358 -0.0397 -0.0069 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3653 0.3005 0.1104 -0.1280 -0.0684 0.0138  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3466 0.2981 0.0991 -0.1383 -0.0915 0.0343  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3688 0.2925 0.0819 -0.1610 -0.0957 0.0366  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.2942 0.2870 0.0961 -0.1267 -0.1086 0.0547  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.4348 0.2877 0.1206 -0.1450 -0.0196 -0.0184 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.4804 0.2953 0.1172 -0.1692 -0.0206 -0.0163 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.4922 0.2939 0.1436 -0.1575 0.0124  -0.0332 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.5197 0.2774 0.1219 -0.1788 0.0212  -0.0356 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.4883 0.3398 0.1453 -0.1700 -0.0592 0.0061  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.5164 0.4259 0.2475 -0.1330 -0.0610 0.0063  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4958 0.4339 0.2678 -0.1090 -0.0549 0.0012  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.5409 0.4593 0.2810 -0.1302 -0.0687 0.0115  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.4657 0.3043 0.1864 -0.1256 0.0265  -0.0416 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.4676 0.2998 0.2188 -0.1146 0.0541  -0.0524 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.5103 0.2888 0.2428 -0.1240 0.1005  -0.0657 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.4930 0.2854 0.2845 -0.1045 0.1203  -0.0701 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.4188 0.3056 0.2504 -0.0825 0.0433  -0.0505 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.4124 0.3421 0.2580 -0.0707 0.0060  -0.0382 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3833 0.3453 0.2846 -0.0456 -0.0033 -0.0375 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.4275 0.3540 0.2476 -0.0813 -0.0065 -0.0315 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.5714 0.2808 0.2184 -0.1561 0.1184  -0.0702 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.6265 0.2621 0.2326 -0.1707 0.1720  -0.0835 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.6364 0.2672 0.3059 -0.1525 0.2190  -0.0920 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.6461 0.2349 0.3251 -0.1509 0.2693  -0.1002 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.6974 0.2444 0.1780 -0.2153 0.1776  -0.0853 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.7339 0.2821 0.1551 -0.2405 0.1236  -0.0696 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.8215 0.2625 0.1096 -0.2906 0.1321  -0.0707 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.7185 0.3006 0.1690 -0.2290 0.1094  -0.0655 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.6215 0.2931 0.3391 -0.1391 0.2045  -0.0880 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.6150 0.2903 0.4064 -0.1225 0.2422  -0.0911 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.5974 0.3255 0.5011 -0.0920 0.2431  -0.0845 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.5765 0.3065 0.5566 -0.0794 0.2758  -0.0821 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.5919 0.2928 0.3973 -0.1199 0.2223  -0.0874 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.5535 0.3255 0.3879 -0.1049 0.1622  -0.0765 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.5766 0.3579 0.3560 -0.1164 0.1223  -0.0702 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4976 0.3322 0.4213 -0.0777 0.1383  -0.0684 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.5433 0.3870 0.3726 -0.0950 0.0835  -0.0608 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.5007 0.3726 0.4083 -0.0731 0.0910  -0.0608 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.4602 0.3177 0.4760 -0.0589 0.1508  -0.0638 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.4679 0.3868 0.4297 -0.0524 0.0608  -0.0529 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.4324 0.3408 0.5039 -0.0412 0.1107  -0.0532 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.4360 0.3690 0.4716 -0.0390 0.0684  -0.0497 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.5977 0.3669 0.5157 -0.0816 0.2058  -0.0788 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.5774 0.3870 0.5887 -0.0576 0.2009  -0.0707 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.6283 0.3924 0.6608 -0.0580 0.2579  -0.0750 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5899 0.3735 0.7224 -0.0400 0.2742  -0.0655 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.5557 0.4041 0.5571 -0.0506 0.1537  -0.0656 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.5418 0.4343 0.5380 -0.0445 0.1036  -0.0588 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.5352 0.4530 0.5190 -0.0384 0.0704  -0.0542 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.5052 0.4295 0.5752 -0.0290 0.0897  -0.0505 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.7143 0.4129 0.6530 -0.0804 0.2876  -0.0867 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.7726 0.4110 0.7097 -0.0839 0.3490  -0.0928 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.8363 0.4024 0.7565 -0.0951 0.4185  -0.1008 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.8603 0.3699 0.7904 -0.0951 0.4814  -0.1048 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.8515 0.4443 0.6829 -0.1059 0.3449  -0.1010 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.8884 0.5327 0.7590 -0.0902 0.3085  -0.0939 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.8563 0.5299 0.8256 -0.0663 0.3205  -0.0864 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.9439 0.5971 0.7496 -0.1030 0.2677  -0.0936 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.8699 0.4303 0.7614 -0.1052 0.4125  -0.1032 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.9306 0.4155 0.7979 -0.1177 0.4809  -0.1114 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.8978 0.4278 0.8482 -0.1034 0.4757  -0.1033 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.9277 0.4004 0.8677 -0.1121 0.5325  -0.1089 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.0694 0.4597 0.7700 -0.1587 0.4915  -0.1259 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.1603 0.5848 0.8070 -0.1721 0.4247  -0.1225 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.3368 0.6927 0.8314 -0.2132 0.4021  -0.1271 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.3689 0.7429 0.8217 -0.2269 0.3531  -0.1212 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.4098 0.6919 0.8288 -0.2332 0.4311  -0.1341 145 GLU   A OE2 
1078 N N1  . A1BRD B .   ? 0.7790 0.2859 0.2909 0.0804  0.1309  0.0213  201 A1BRD A N1  
1079 C C4  . A1BRD B .   ? 0.9097 0.2347 0.2845 0.0813  0.2329  0.0200  201 A1BRD A C4  
1080 C C5  . A1BRD B .   ? 0.8645 0.2631 0.2798 0.0734  0.1728  0.0156  201 A1BRD A C5  
1081 C C6  . A1BRD B .   ? 0.8732 0.2529 0.2704 0.0729  0.1711  0.0152  201 A1BRD A C6  
1082 C C7  . A1BRD B .   ? 0.7897 0.2874 0.3023 0.0839  0.1507  0.0235  201 A1BRD A C7  
1083 C C8  . A1BRD B .   ? 0.8321 0.2569 0.2479 0.0634  0.1129  0.0113  201 A1BRD A C8  
1084 C C10 . A1BRD B .   ? 0.7382 0.3173 0.2830 0.0629  0.0498  0.0121  201 A1BRD A C10 
1085 C C13 . A1BRD B .   ? 0.7117 0.3108 0.3197 0.0906  0.1227  0.0310  201 A1BRD A C13 
1086 C C15 . A1BRD B .   ? 0.9646 0.1996 0.2770 0.0855  0.2804  0.0215  201 A1BRD A C15 
1087 O O2  . A1BRD B .   ? 0.6062 0.3408 0.3326 0.0912  0.0766  0.0387  201 A1BRD A O2  
1088 C C12 . A1BRD B .   ? 0.6191 0.3530 0.3281 0.0825  0.0577  0.0298  201 A1BRD A C12 
1089 N N2  . A1BRD B .   ? 0.5800 0.3770 0.3347 0.0758  0.0288  0.0272  201 A1BRD A N2  
1090 C C11 . A1BRD B .   ? 0.6829 0.3328 0.3087 0.0770  0.0680  0.0217  201 A1BRD A C11 
1091 C C9  . A1BRD B .   ? 0.8059 0.2862 0.2511 0.0503  0.0533  0.0060  201 A1BRD A C9  
1092 O O1  . A1BRD B .   ? 0.7387 0.3129 0.3352 0.0931  0.1523  0.0328  201 A1BRD A O1  
1093 C C14 . A1BRD B .   ? 0.9220 0.2161 0.2766 0.0854  0.2439  0.0220  201 A1BRD A C14 
1094 C C3  . A1BRD B .   ? 0.8984 0.2362 0.2904 0.0830  0.2418  0.0217  201 A1BRD A C3  
1095 C C2  . A1BRD B .   ? 0.8563 0.2750 0.2996 0.0767  0.1916  0.0187  201 A1BRD A C2  
1096 N N   . A1BRD B .   ? 0.8218 0.2949 0.2871 0.0676  0.1279  0.0127  201 A1BRD A N   
1097 C C1  . A1BRD B .   ? 0.8174 0.2988 0.2941 0.0693  0.1370  0.0139  201 A1BRD A C1  
1098 O O   . A1BRD B .   ? 0.7826 0.3299 0.3039 0.0636  0.0975  0.0108  201 A1BRD A O   
1099 C C   . A1BRD B .   ? 0.7518 0.3477 0.3004 0.0549  0.0484  0.0055  201 A1BRD A C   
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