data_7HWN
# 
_entry.id   7HWN 
# 
_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   7HWN         pdb_00007hwn 10.2210/pdb7hwn/pdb 
WWPDB D_1001408023 ?            ?                   
# 
_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                        7HWN 
_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-[(2R)-2-(cyclopentylmethoxy)-2-phenylacetyl]piperidine-3-carboxamide' 344.448   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    62 ?         ? ? ? 
# 
_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-[(2R)-2-(cyclopentylmethoxy)-2-phenylacetyl]piperidine-3-carboxamide' A1BR5 
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 
A1BR5 non-polymer         . '(3S)-1-[(2R)-2-(cyclopentylmethoxy)-2-phenylacetyl]piperidine-3-carboxamide' ? 'C20 H28 N2 O3'  
344.448 
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        A1BR5 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BR5 
_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 A1BR5 1  201 201 A1BR5 LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 6   DMS   DMS A . 
E 5 HOH   1  301 52  HOH   HOH A . 
E 5 HOH   2  302 65  HOH   HOH A . 
E 5 HOH   3  303 15  HOH   HOH A . 
E 5 HOH   4  304 9   HOH   HOH A . 
E 5 HOH   5  305 11  HOH   HOH A . 
E 5 HOH   6  306 1   HOH   HOH A . 
E 5 HOH   7  307 56  HOH   HOH A . 
E 5 HOH   8  308 55  HOH   HOH A . 
E 5 HOH   9  309 59  HOH   HOH A . 
E 5 HOH   10 310 4   HOH   HOH A . 
E 5 HOH   11 311 38  HOH   HOH A . 
E 5 HOH   12 312 37  HOH   HOH A . 
E 5 HOH   13 313 29  HOH   HOH A . 
E 5 HOH   14 314 43  HOH   HOH A . 
E 5 HOH   15 315 24  HOH   HOH A . 
E 5 HOH   16 316 12  HOH   HOH A . 
E 5 HOH   17 317 40  HOH   HOH A . 
E 5 HOH   18 318 27  HOH   HOH A . 
E 5 HOH   19 319 26  HOH   HOH A . 
E 5 HOH   20 320 31  HOH   HOH A . 
E 5 HOH   21 321 3   HOH   HOH A . 
E 5 HOH   22 322 16  HOH   HOH A . 
E 5 HOH   23 323 45  HOH   HOH A . 
E 5 HOH   24 324 44  HOH   HOH A . 
E 5 HOH   25 325 18  HOH   HOH A . 
E 5 HOH   26 326 5   HOH   HOH A . 
E 5 HOH   27 327 41  HOH   HOH A . 
E 5 HOH   28 328 8   HOH   HOH A . 
E 5 HOH   29 329 25  HOH   HOH A . 
E 5 HOH   30 330 10  HOH   HOH A . 
E 5 HOH   31 331 54  HOH   HOH A . 
E 5 HOH   32 332 50  HOH   HOH A . 
E 5 HOH   33 333 14  HOH   HOH A . 
E 5 HOH   34 334 42  HOH   HOH A . 
E 5 HOH   35 335 17  HOH   HOH A . 
E 5 HOH   36 336 61  HOH   HOH A . 
E 5 HOH   37 337 13  HOH   HOH A . 
E 5 HOH   38 338 57  HOH   HOH A . 
E 5 HOH   39 339 28  HOH   HOH A . 
E 5 HOH   40 340 39  HOH   HOH A . 
E 5 HOH   41 341 6   HOH   HOH A . 
E 5 HOH   42 342 48  HOH   HOH A . 
E 5 HOH   43 343 64  HOH   HOH A . 
E 5 HOH   44 344 34  HOH   HOH A . 
E 5 HOH   45 345 19  HOH   HOH A . 
E 5 HOH   46 346 22  HOH   HOH A . 
E 5 HOH   47 347 30  HOH   HOH A . 
E 5 HOH   48 348 33  HOH   HOH A . 
E 5 HOH   49 349 63  HOH   HOH A . 
E 5 HOH   50 350 35  HOH   HOH A . 
E 5 HOH   51 351 62  HOH   HOH A . 
E 5 HOH   52 352 32  HOH   HOH A . 
E 5 HOH   53 353 60  HOH   HOH A . 
E 5 HOH   54 354 7   HOH   HOH A . 
E 5 HOH   55 355 23  HOH   HOH A . 
E 5 HOH   56 356 20  HOH   HOH A . 
E 5 HOH   57 357 51  HOH   HOH A . 
E 5 HOH   58 358 58  HOH   HOH A . 
E 5 HOH   59 359 21  HOH   HOH A . 
E 5 HOH   60 360 53  HOH   HOH A . 
E 5 HOH   61 361 2   HOH   HOH A . 
E 5 HOH   62 362 47  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           7HWN 
_cell.length_a           72.773 
_cell.length_b           61.330 
_cell.length_c           32.597 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.69 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HWN 
_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          7HWN 
_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   46.20 
_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                     7HWN 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             27.13 
_reflns.d_resolution_high            1.38 
_reflns.number_obs                   29277 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_netI_over_sigmaI        17.0 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.058 
_reflns.pdbx_Rpim_I_all              0.022 
_reflns.pdbx_CC_half                 1.000 
_reflns.pdbx_number_measured_all     181135 
_reflns.pdbx_chi_squared             0.61 
_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                  1.38 
_reflns_shell.d_res_low                   1.40 
_reflns_shell.number_measured_all         5545 
_reflns_shell.number_unique_obs           1363 
_reflns_shell.Rmerge_I_obs                1.374 
_reflns_shell.pdbx_chi_squared            0.15 
_reflns_shell.pdbx_redundancy             4.1 
_reflns_shell.percent_possible_obs        93.8 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             1.579 
_reflns_shell.pdbx_Rpim_I_all             0.764 
_reflns_shell.pdbx_CC_half                0.388 
_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                                 7HWN 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     29230 
_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                             16.94 
_refine.ls_d_res_high                            1.380 
_refine.ls_percent_reflns_obs                    99.2 
_refine.ls_R_factor_obs                          0.2124 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2114 
_refine.ls_R_factor_R_free                       0.2341 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.630 
_refine.ls_number_reflns_R_free                  1352 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.950 
_refine.B_iso_mean                               31.39 
_refine.aniso_B[1][1]                            -2.80160 
_refine.aniso_B[2][2]                            -0.37090 
_refine.aniso_B[3][3]                            3.17250 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.45260 
_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             0.064 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.064 
_refine.pdbx_overall_SU_R_Blow_DPI               0.063 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.064 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HWN 
_refine_analyze.Luzzati_coordinate_error_obs    0.20 
_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         30 
_refine_hist.number_atoms_solvent             60 
_refine_hist.number_atoms_total               1164 
_refine_hist.d_res_high                       1.380 
_refine_hist.d_res_low                        16.94 
# 
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                  0.012 ? 2.00  1134 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.05  ? 2.00  1542 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  384  '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  202  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1134 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.30  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.90 ? ?     ?    '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  900  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.38 
_refine_ls_shell.d_res_low                        1.39 
_refine_ls_shell.number_reflns_R_work             557 
_refine_ls_shell.R_factor_R_work                  0.3408 
_refine_ls_shell.percent_reflns_obs               87.42 
_refine_ls_shell.R_factor_R_free                  0.3794 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.79 
_refine_ls_shell.number_reflns_R_free             28 
_refine_ls_shell.number_reflns_all                585 
_refine_ls_shell.R_factor_all                     0.3426 
# 
_struct.entry_id                  7HWN 
_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-0034451-001 (A71EV2A-x3968)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HWN 
_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              7HWN 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.245 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.353 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.167 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 114.3 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 107.4 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.9 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 108.1 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 98.6  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 111.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? THR A 120 ? GLY A 119 THR A 126 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HWN 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    344 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    353 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.11 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     14 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -97.21 
_pdbx_validate_torsion.psi             33.45 
# 
_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         15.2158 
_pdbx_refine_tls.origin_y         7.1380 
_pdbx_refine_tls.origin_z         14.2251 
_pdbx_refine_tls.T[1][1]          -0.0494 
_pdbx_refine_tls.T[2][2]          -0.0376 
_pdbx_refine_tls.T[3][3]          0.0183 
_pdbx_refine_tls.T[1][2]          -0.0047 
_pdbx_refine_tls.T[1][3]          -0.0108 
_pdbx_refine_tls.T[2][3]          -0.0091 
_pdbx_refine_tls.L[1][1]          2.1441 
_pdbx_refine_tls.L[2][2]          4.9303 
_pdbx_refine_tls.L[3][3]          0.9799 
_pdbx_refine_tls.L[1][2]          2.2683 
_pdbx_refine_tls.L[1][3]          -0.5771 
_pdbx_refine_tls.L[2][3]          -1.5809 
_pdbx_refine_tls.S[1][1]          -0.1009 
_pdbx_refine_tls.S[1][2]          0.0549 
_pdbx_refine_tls.S[1][3]          0.1720 
_pdbx_refine_tls.S[2][1]          0.1573 
_pdbx_refine_tls.S[2][2]          0.1403 
_pdbx_refine_tls.S[2][3]          -0.0304 
_pdbx_refine_tls.S[3][1]          -0.0349 
_pdbx_refine_tls.S[3][2]          -0.0695 
_pdbx_refine_tls.S[3][3]          -0.0395 
# 
_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 
# 
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 
A1BR5 N1   N  N N 1   
A1BR5 C4   C  N N 2   
A1BR5 C5   C  N N 3   
A1BR5 C6   C  N R 4   
A1BR5 C7   C  N N 5   
A1BR5 C8   C  N N 6   
A1BR5 C10  C  N N 7   
A1BR5 C13  C  Y N 8   
A1BR5 C15  C  Y N 9   
A1BR5 C17  C  Y N 10  
A1BR5 O1   O  N N 11  
A1BR5 C3   C  N N 12  
A1BR5 C2   C  N N 13  
A1BR5 C19  C  N N 14  
A1BR5 C1   C  N S 15  
A1BR5 C    C  N N 16  
A1BR5 O    O  N N 17  
A1BR5 N    N  N N 18  
A1BR5 C18  C  Y N 19  
A1BR5 C16  C  Y N 20  
A1BR5 C14  C  Y N 21  
A1BR5 O2   O  N N 22  
A1BR5 C12  C  N N 23  
A1BR5 C11  C  N N 24  
A1BR5 C9   C  N N 25  
A1BR5 H9   H  N N 26  
A1BR5 H8   H  N N 27  
A1BR5 H1   H  N N 28  
A1BR5 H10  H  N N 29  
A1BR5 H11  H  N N 30  
A1BR5 H12  H  N N 31  
A1BR5 H16  H  N N 32  
A1BR5 H15  H  N N 33  
A1BR5 H22  H  N N 34  
A1BR5 H24  H  N N 35  
A1BR5 H7   H  N N 36  
A1BR5 H6   H  N N 37  
A1BR5 H5   H  N N 38  
A1BR5 H4   H  N N 39  
A1BR5 H27  H  N N 40  
A1BR5 H26  H  N N 41  
A1BR5 H    H  N N 42  
A1BR5 H2   H  N N 43  
A1BR5 H3   H  N N 44  
A1BR5 H25  H  N N 45  
A1BR5 H23  H  N N 46  
A1BR5 H21  H  N N 47  
A1BR5 H20  H  N N 48  
A1BR5 H19  H  N N 49  
A1BR5 H18  H  N N 50  
A1BR5 H17  H  N N 51  
A1BR5 H14  H  N N 52  
A1BR5 H13  H  N N 53  
ALA   N    N  N N 54  
ALA   CA   C  N S 55  
ALA   C    C  N N 56  
ALA   O    O  N N 57  
ALA   CB   C  N N 58  
ALA   OXT  O  N N 59  
ALA   H    H  N N 60  
ALA   H2   H  N N 61  
ALA   HA   H  N N 62  
ALA   HB1  H  N N 63  
ALA   HB2  H  N N 64  
ALA   HB3  H  N N 65  
ALA   HXT  H  N N 66  
ARG   N    N  N N 67  
ARG   CA   C  N S 68  
ARG   C    C  N N 69  
ARG   O    O  N N 70  
ARG   CB   C  N N 71  
ARG   CG   C  N N 72  
ARG   CD   C  N N 73  
ARG   NE   N  N N 74  
ARG   CZ   C  N N 75  
ARG   NH1  N  N N 76  
ARG   NH2  N  N N 77  
ARG   OXT  O  N N 78  
ARG   H    H  N N 79  
ARG   H2   H  N N 80  
ARG   HA   H  N N 81  
ARG   HB2  H  N N 82  
ARG   HB3  H  N N 83  
ARG   HG2  H  N N 84  
ARG   HG3  H  N N 85  
ARG   HD2  H  N N 86  
ARG   HD3  H  N N 87  
ARG   HE   H  N N 88  
ARG   HH11 H  N N 89  
ARG   HH12 H  N N 90  
ARG   HH21 H  N N 91  
ARG   HH22 H  N N 92  
ARG   HXT  H  N N 93  
ASN   N    N  N N 94  
ASN   CA   C  N S 95  
ASN   C    C  N N 96  
ASN   O    O  N N 97  
ASN   CB   C  N N 98  
ASN   CG   C  N N 99  
ASN   OD1  O  N N 100 
ASN   ND2  N  N N 101 
ASN   OXT  O  N N 102 
ASN   H    H  N N 103 
ASN   H2   H  N N 104 
ASN   HA   H  N N 105 
ASN   HB2  H  N N 106 
ASN   HB3  H  N N 107 
ASN   HD21 H  N N 108 
ASN   HD22 H  N N 109 
ASN   HXT  H  N N 110 
ASP   N    N  N N 111 
ASP   CA   C  N S 112 
ASP   C    C  N N 113 
ASP   O    O  N N 114 
ASP   CB   C  N N 115 
ASP   CG   C  N N 116 
ASP   OD1  O  N N 117 
ASP   OD2  O  N N 118 
ASP   OXT  O  N N 119 
ASP   H    H  N N 120 
ASP   H2   H  N N 121 
ASP   HA   H  N N 122 
ASP   HB2  H  N N 123 
ASP   HB3  H  N N 124 
ASP   HD2  H  N N 125 
ASP   HXT  H  N N 126 
CYS   N    N  N N 127 
CYS   CA   C  N R 128 
CYS   C    C  N N 129 
CYS   O    O  N N 130 
CYS   CB   C  N N 131 
CYS   SG   S  N N 132 
CYS   OXT  O  N N 133 
CYS   H    H  N N 134 
CYS   H2   H  N N 135 
CYS   HA   H  N N 136 
CYS   HB2  H  N N 137 
CYS   HB3  H  N N 138 
CYS   HG   H  N N 139 
CYS   HXT  H  N N 140 
DMS   S    S  N N 141 
DMS   O    O  N N 142 
DMS   C1   C  N N 143 
DMS   C2   C  N N 144 
DMS   H11  H  N N 145 
DMS   H12  H  N N 146 
DMS   H13  H  N N 147 
DMS   H21  H  N N 148 
DMS   H22  H  N N 149 
DMS   H23  H  N N 150 
GLN   N    N  N N 151 
GLN   CA   C  N S 152 
GLN   C    C  N N 153 
GLN   O    O  N N 154 
GLN   CB   C  N N 155 
GLN   CG   C  N N 156 
GLN   CD   C  N N 157 
GLN   OE1  O  N N 158 
GLN   NE2  N  N N 159 
GLN   OXT  O  N N 160 
GLN   H    H  N N 161 
GLN   H2   H  N N 162 
GLN   HA   H  N N 163 
GLN   HB2  H  N N 164 
GLN   HB3  H  N N 165 
GLN   HG2  H  N N 166 
GLN   HG3  H  N N 167 
GLN   HE21 H  N N 168 
GLN   HE22 H  N N 169 
GLN   HXT  H  N N 170 
GLU   N    N  N N 171 
GLU   CA   C  N S 172 
GLU   C    C  N N 173 
GLU   O    O  N N 174 
GLU   CB   C  N N 175 
GLU   CG   C  N N 176 
GLU   CD   C  N N 177 
GLU   OE1  O  N N 178 
GLU   OE2  O  N N 179 
GLU   OXT  O  N N 180 
GLU   H    H  N N 181 
GLU   H2   H  N N 182 
GLU   HA   H  N N 183 
GLU   HB2  H  N N 184 
GLU   HB3  H  N N 185 
GLU   HG2  H  N N 186 
GLU   HG3  H  N N 187 
GLU   HE2  H  N N 188 
GLU   HXT  H  N N 189 
GLY   N    N  N N 190 
GLY   CA   C  N N 191 
GLY   C    C  N N 192 
GLY   O    O  N N 193 
GLY   OXT  O  N N 194 
GLY   H    H  N N 195 
GLY   H2   H  N N 196 
GLY   HA2  H  N N 197 
GLY   HA3  H  N N 198 
GLY   HXT  H  N N 199 
HIS   N    N  N N 200 
HIS   CA   C  N S 201 
HIS   C    C  N N 202 
HIS   O    O  N N 203 
HIS   CB   C  N N 204 
HIS   CG   C  Y N 205 
HIS   ND1  N  Y N 206 
HIS   CD2  C  Y N 207 
HIS   CE1  C  Y N 208 
HIS   NE2  N  Y N 209 
HIS   OXT  O  N N 210 
HIS   H    H  N N 211 
HIS   H2   H  N N 212 
HIS   HA   H  N N 213 
HIS   HB2  H  N N 214 
HIS   HB3  H  N N 215 
HIS   HD1  H  N N 216 
HIS   HD2  H  N N 217 
HIS   HE1  H  N N 218 
HIS   HE2  H  N N 219 
HIS   HXT  H  N N 220 
HOH   O    O  N N 221 
HOH   H1   H  N N 222 
HOH   H2   H  N N 223 
ILE   N    N  N N 224 
ILE   CA   C  N S 225 
ILE   C    C  N N 226 
ILE   O    O  N N 227 
ILE   CB   C  N S 228 
ILE   CG1  C  N N 229 
ILE   CG2  C  N N 230 
ILE   CD1  C  N N 231 
ILE   OXT  O  N N 232 
ILE   H    H  N N 233 
ILE   H2   H  N N 234 
ILE   HA   H  N N 235 
ILE   HB   H  N N 236 
ILE   HG12 H  N N 237 
ILE   HG13 H  N N 238 
ILE   HG21 H  N N 239 
ILE   HG22 H  N N 240 
ILE   HG23 H  N N 241 
ILE   HD11 H  N N 242 
ILE   HD12 H  N N 243 
ILE   HD13 H  N N 244 
ILE   HXT  H  N N 245 
LEU   N    N  N N 246 
LEU   CA   C  N S 247 
LEU   C    C  N N 248 
LEU   O    O  N N 249 
LEU   CB   C  N N 250 
LEU   CG   C  N N 251 
LEU   CD1  C  N N 252 
LEU   CD2  C  N N 253 
LEU   OXT  O  N N 254 
LEU   H    H  N N 255 
LEU   H2   H  N N 256 
LEU   HA   H  N N 257 
LEU   HB2  H  N N 258 
LEU   HB3  H  N N 259 
LEU   HG   H  N N 260 
LEU   HD11 H  N N 261 
LEU   HD12 H  N N 262 
LEU   HD13 H  N N 263 
LEU   HD21 H  N N 264 
LEU   HD22 H  N N 265 
LEU   HD23 H  N N 266 
LEU   HXT  H  N N 267 
LYS   N    N  N N 268 
LYS   CA   C  N S 269 
LYS   C    C  N N 270 
LYS   O    O  N N 271 
LYS   CB   C  N N 272 
LYS   CG   C  N N 273 
LYS   CD   C  N N 274 
LYS   CE   C  N N 275 
LYS   NZ   N  N N 276 
LYS   OXT  O  N N 277 
LYS   H    H  N N 278 
LYS   H2   H  N N 279 
LYS   HA   H  N N 280 
LYS   HB2  H  N N 281 
LYS   HB3  H  N N 282 
LYS   HG2  H  N N 283 
LYS   HG3  H  N N 284 
LYS   HD2  H  N N 285 
LYS   HD3  H  N N 286 
LYS   HE2  H  N N 287 
LYS   HE3  H  N N 288 
LYS   HZ1  H  N N 289 
LYS   HZ2  H  N N 290 
LYS   HZ3  H  N N 291 
LYS   HXT  H  N N 292 
MET   N    N  N N 293 
MET   CA   C  N S 294 
MET   C    C  N N 295 
MET   O    O  N N 296 
MET   CB   C  N N 297 
MET   CG   C  N N 298 
MET   SD   S  N N 299 
MET   CE   C  N N 300 
MET   OXT  O  N N 301 
MET   H    H  N N 302 
MET   H2   H  N N 303 
MET   HA   H  N N 304 
MET   HB2  H  N N 305 
MET   HB3  H  N N 306 
MET   HG2  H  N N 307 
MET   HG3  H  N N 308 
MET   HE1  H  N N 309 
MET   HE2  H  N N 310 
MET   HE3  H  N N 311 
MET   HXT  H  N N 312 
PHE   N    N  N N 313 
PHE   CA   C  N S 314 
PHE   C    C  N N 315 
PHE   O    O  N N 316 
PHE   CB   C  N N 317 
PHE   CG   C  Y N 318 
PHE   CD1  C  Y N 319 
PHE   CD2  C  Y N 320 
PHE   CE1  C  Y N 321 
PHE   CE2  C  Y N 322 
PHE   CZ   C  Y N 323 
PHE   OXT  O  N N 324 
PHE   H    H  N N 325 
PHE   H2   H  N N 326 
PHE   HA   H  N N 327 
PHE   HB2  H  N N 328 
PHE   HB3  H  N N 329 
PHE   HD1  H  N N 330 
PHE   HD2  H  N N 331 
PHE   HE1  H  N N 332 
PHE   HE2  H  N N 333 
PHE   HZ   H  N N 334 
PHE   HXT  H  N N 335 
PRO   N    N  N N 336 
PRO   CA   C  N S 337 
PRO   C    C  N N 338 
PRO   O    O  N N 339 
PRO   CB   C  N N 340 
PRO   CG   C  N N 341 
PRO   CD   C  N N 342 
PRO   OXT  O  N N 343 
PRO   H    H  N N 344 
PRO   HA   H  N N 345 
PRO   HB2  H  N N 346 
PRO   HB3  H  N N 347 
PRO   HG2  H  N N 348 
PRO   HG3  H  N N 349 
PRO   HD2  H  N N 350 
PRO   HD3  H  N N 351 
PRO   HXT  H  N N 352 
SER   N    N  N N 353 
SER   CA   C  N S 354 
SER   C    C  N N 355 
SER   O    O  N N 356 
SER   CB   C  N N 357 
SER   OG   O  N N 358 
SER   OXT  O  N N 359 
SER   H    H  N N 360 
SER   H2   H  N N 361 
SER   HA   H  N N 362 
SER   HB2  H  N N 363 
SER   HB3  H  N N 364 
SER   HG   H  N N 365 
SER   HXT  H  N N 366 
THR   N    N  N N 367 
THR   CA   C  N S 368 
THR   C    C  N N 369 
THR   O    O  N N 370 
THR   CB   C  N R 371 
THR   OG1  O  N N 372 
THR   CG2  C  N N 373 
THR   OXT  O  N N 374 
THR   H    H  N N 375 
THR   H2   H  N N 376 
THR   HA   H  N N 377 
THR   HB   H  N N 378 
THR   HG1  H  N N 379 
THR   HG21 H  N N 380 
THR   HG22 H  N N 381 
THR   HG23 H  N N 382 
THR   HXT  H  N N 383 
TRP   N    N  N N 384 
TRP   CA   C  N S 385 
TRP   C    C  N N 386 
TRP   O    O  N N 387 
TRP   CB   C  N N 388 
TRP   CG   C  Y N 389 
TRP   CD1  C  Y N 390 
TRP   CD2  C  Y N 391 
TRP   NE1  N  Y N 392 
TRP   CE2  C  Y N 393 
TRP   CE3  C  Y N 394 
TRP   CZ2  C  Y N 395 
TRP   CZ3  C  Y N 396 
TRP   CH2  C  Y N 397 
TRP   OXT  O  N N 398 
TRP   H    H  N N 399 
TRP   H2   H  N N 400 
TRP   HA   H  N N 401 
TRP   HB2  H  N N 402 
TRP   HB3  H  N N 403 
TRP   HD1  H  N N 404 
TRP   HE1  H  N N 405 
TRP   HE3  H  N N 406 
TRP   HZ2  H  N N 407 
TRP   HZ3  H  N N 408 
TRP   HH2  H  N N 409 
TRP   HXT  H  N N 410 
TYR   N    N  N N 411 
TYR   CA   C  N S 412 
TYR   C    C  N N 413 
TYR   O    O  N N 414 
TYR   CB   C  N N 415 
TYR   CG   C  Y N 416 
TYR   CD1  C  Y N 417 
TYR   CD2  C  Y N 418 
TYR   CE1  C  Y N 419 
TYR   CE2  C  Y N 420 
TYR   CZ   C  Y N 421 
TYR   OH   O  N N 422 
TYR   OXT  O  N N 423 
TYR   H    H  N N 424 
TYR   H2   H  N N 425 
TYR   HA   H  N N 426 
TYR   HB2  H  N N 427 
TYR   HB3  H  N N 428 
TYR   HD1  H  N N 429 
TYR   HD2  H  N N 430 
TYR   HE1  H  N N 431 
TYR   HE2  H  N N 432 
TYR   HH   H  N N 433 
TYR   HXT  H  N N 434 
VAL   N    N  N N 435 
VAL   CA   C  N S 436 
VAL   C    C  N N 437 
VAL   O    O  N N 438 
VAL   CB   C  N N 439 
VAL   CG1  C  N N 440 
VAL   CG2  C  N N 441 
VAL   OXT  O  N N 442 
VAL   H    H  N N 443 
VAL   H2   H  N N 444 
VAL   HA   H  N N 445 
VAL   HB   H  N N 446 
VAL   HG11 H  N N 447 
VAL   HG12 H  N N 448 
VAL   HG13 H  N N 449 
VAL   HG21 H  N N 450 
VAL   HG22 H  N N 451 
VAL   HG23 H  N N 452 
VAL   HXT  H  N N 453 
ZN    ZN   ZN N N 454 
# 
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 
A1BR5 N   C    sing N N 1   
A1BR5 O   C    doub N N 2   
A1BR5 C   C1   sing N N 3   
A1BR5 C1  C2   sing N N 4   
A1BR5 C2  C3   sing N N 5   
A1BR5 C3  C4   sing N N 6   
A1BR5 C4  N1   sing N N 7   
A1BR5 N1  C5   sing N N 8   
A1BR5 C5  O1   doub N N 9   
A1BR5 C6  C5   sing N N 10  
A1BR5 O2  C6   sing N N 11  
A1BR5 C7  O2   sing N N 12  
A1BR5 C8  C7   sing N N 13  
A1BR5 C8  C9   sing N N 14  
A1BR5 C9  C10  sing N N 15  
A1BR5 C10 C11  sing N N 16  
A1BR5 C11 C12  sing N N 17  
A1BR5 C12 C8   sing N N 18  
A1BR5 C13 C6   sing N N 19  
A1BR5 C13 C14  doub Y N 20  
A1BR5 C14 C15  sing Y N 21  
A1BR5 C15 C16  doub Y N 22  
A1BR5 C16 C17  sing Y N 23  
A1BR5 C17 C18  doub Y N 24  
A1BR5 C18 C13  sing Y N 25  
A1BR5 C19 N1   sing N N 26  
A1BR5 C1  C19  sing N N 27  
A1BR5 C4  H9   sing N N 28  
A1BR5 C4  H8   sing N N 29  
A1BR5 C6  H1   sing N N 30  
A1BR5 C7  H10  sing N N 31  
A1BR5 C7  H11  sing N N 32  
A1BR5 C8  H12  sing N N 33  
A1BR5 C10 H16  sing N N 34  
A1BR5 C10 H15  sing N N 35  
A1BR5 C15 H22  sing N N 36  
A1BR5 C17 H24  sing N N 37  
A1BR5 C3  H7   sing N N 38  
A1BR5 C3  H6   sing N N 39  
A1BR5 C2  H5   sing N N 40  
A1BR5 C2  H4   sing N N 41  
A1BR5 C19 H27  sing N N 42  
A1BR5 C19 H26  sing N N 43  
A1BR5 C1  H    sing N N 44  
A1BR5 N   H2   sing N N 45  
A1BR5 N   H3   sing N N 46  
A1BR5 C18 H25  sing N N 47  
A1BR5 C16 H23  sing N N 48  
A1BR5 C14 H21  sing N N 49  
A1BR5 C12 H20  sing N N 50  
A1BR5 C12 H19  sing N N 51  
A1BR5 C11 H18  sing N N 52  
A1BR5 C11 H17  sing N N 53  
A1BR5 C9  H14  sing N N 54  
A1BR5 C9  H13  sing N N 55  
ALA   N   CA   sing N N 56  
ALA   N   H    sing N N 57  
ALA   N   H2   sing N N 58  
ALA   CA  C    sing N N 59  
ALA   CA  CB   sing N N 60  
ALA   CA  HA   sing N N 61  
ALA   C   O    doub N N 62  
ALA   C   OXT  sing N N 63  
ALA   CB  HB1  sing N N 64  
ALA   CB  HB2  sing N N 65  
ALA   CB  HB3  sing N N 66  
ALA   OXT HXT  sing N N 67  
ARG   N   CA   sing N N 68  
ARG   N   H    sing N N 69  
ARG   N   H2   sing N N 70  
ARG   CA  C    sing N N 71  
ARG   CA  CB   sing N N 72  
ARG   CA  HA   sing N N 73  
ARG   C   O    doub N N 74  
ARG   C   OXT  sing N N 75  
ARG   CB  CG   sing N N 76  
ARG   CB  HB2  sing N N 77  
ARG   CB  HB3  sing N N 78  
ARG   CG  CD   sing N N 79  
ARG   CG  HG2  sing N N 80  
ARG   CG  HG3  sing N N 81  
ARG   CD  NE   sing N N 82  
ARG   CD  HD2  sing N N 83  
ARG   CD  HD3  sing N N 84  
ARG   NE  CZ   sing N N 85  
ARG   NE  HE   sing N N 86  
ARG   CZ  NH1  sing N N 87  
ARG   CZ  NH2  doub N N 88  
ARG   NH1 HH11 sing N N 89  
ARG   NH1 HH12 sing N N 90  
ARG   NH2 HH21 sing N N 91  
ARG   NH2 HH22 sing N N 92  
ARG   OXT HXT  sing N N 93  
ASN   N   CA   sing N N 94  
ASN   N   H    sing N N 95  
ASN   N   H2   sing N N 96  
ASN   CA  C    sing N N 97  
ASN   CA  CB   sing N N 98  
ASN   CA  HA   sing N N 99  
ASN   C   O    doub N N 100 
ASN   C   OXT  sing N N 101 
ASN   CB  CG   sing N N 102 
ASN   CB  HB2  sing N N 103 
ASN   CB  HB3  sing N N 104 
ASN   CG  OD1  doub N N 105 
ASN   CG  ND2  sing N N 106 
ASN   ND2 HD21 sing N N 107 
ASN   ND2 HD22 sing N N 108 
ASN   OXT HXT  sing N N 109 
ASP   N   CA   sing N N 110 
ASP   N   H    sing N N 111 
ASP   N   H2   sing N N 112 
ASP   CA  C    sing N N 113 
ASP   CA  CB   sing N N 114 
ASP   CA  HA   sing N N 115 
ASP   C   O    doub N N 116 
ASP   C   OXT  sing N N 117 
ASP   CB  CG   sing N N 118 
ASP   CB  HB2  sing N N 119 
ASP   CB  HB3  sing N N 120 
ASP   CG  OD1  doub N N 121 
ASP   CG  OD2  sing N N 122 
ASP   OD2 HD2  sing N N 123 
ASP   OXT HXT  sing N N 124 
CYS   N   CA   sing N N 125 
CYS   N   H    sing N N 126 
CYS   N   H2   sing N N 127 
CYS   CA  C    sing N N 128 
CYS   CA  CB   sing N N 129 
CYS   CA  HA   sing N N 130 
CYS   C   O    doub N N 131 
CYS   C   OXT  sing N N 132 
CYS   CB  SG   sing N N 133 
CYS   CB  HB2  sing N N 134 
CYS   CB  HB3  sing N N 135 
CYS   SG  HG   sing N N 136 
CYS   OXT HXT  sing N N 137 
DMS   S   O    doub N N 138 
DMS   S   C1   sing N N 139 
DMS   S   C2   sing N N 140 
DMS   C1  H11  sing N N 141 
DMS   C1  H12  sing N N 142 
DMS   C1  H13  sing N N 143 
DMS   C2  H21  sing N N 144 
DMS   C2  H22  sing N N 145 
DMS   C2  H23  sing N N 146 
GLN   N   CA   sing N N 147 
GLN   N   H    sing N N 148 
GLN   N   H2   sing N N 149 
GLN   CA  C    sing N N 150 
GLN   CA  CB   sing N N 151 
GLN   CA  HA   sing N N 152 
GLN   C   O    doub N N 153 
GLN   C   OXT  sing N N 154 
GLN   CB  CG   sing N N 155 
GLN   CB  HB2  sing N N 156 
GLN   CB  HB3  sing N N 157 
GLN   CG  CD   sing N N 158 
GLN   CG  HG2  sing N N 159 
GLN   CG  HG3  sing N N 160 
GLN   CD  OE1  doub N N 161 
GLN   CD  NE2  sing N N 162 
GLN   NE2 HE21 sing N N 163 
GLN   NE2 HE22 sing N N 164 
GLN   OXT HXT  sing N N 165 
GLU   N   CA   sing N N 166 
GLU   N   H    sing N N 167 
GLU   N   H2   sing N N 168 
GLU   CA  C    sing N N 169 
GLU   CA  CB   sing N N 170 
GLU   CA  HA   sing N N 171 
GLU   C   O    doub N N 172 
GLU   C   OXT  sing N N 173 
GLU   CB  CG   sing N N 174 
GLU   CB  HB2  sing N N 175 
GLU   CB  HB3  sing N N 176 
GLU   CG  CD   sing N N 177 
GLU   CG  HG2  sing N N 178 
GLU   CG  HG3  sing N N 179 
GLU   CD  OE1  doub N N 180 
GLU   CD  OE2  sing N N 181 
GLU   OE2 HE2  sing N N 182 
GLU   OXT HXT  sing N N 183 
GLY   N   CA   sing N N 184 
GLY   N   H    sing N N 185 
GLY   N   H2   sing N N 186 
GLY   CA  C    sing N N 187 
GLY   CA  HA2  sing N N 188 
GLY   CA  HA3  sing N N 189 
GLY   C   O    doub N N 190 
GLY   C   OXT  sing N N 191 
GLY   OXT HXT  sing N N 192 
HIS   N   CA   sing N N 193 
HIS   N   H    sing N N 194 
HIS   N   H2   sing N N 195 
HIS   CA  C    sing N N 196 
HIS   CA  CB   sing N N 197 
HIS   CA  HA   sing N N 198 
HIS   C   O    doub N N 199 
HIS   C   OXT  sing N N 200 
HIS   CB  CG   sing N N 201 
HIS   CB  HB2  sing N N 202 
HIS   CB  HB3  sing N N 203 
HIS   CG  ND1  sing Y N 204 
HIS   CG  CD2  doub Y N 205 
HIS   ND1 CE1  doub Y N 206 
HIS   ND1 HD1  sing N N 207 
HIS   CD2 NE2  sing Y N 208 
HIS   CD2 HD2  sing N N 209 
HIS   CE1 NE2  sing Y N 210 
HIS   CE1 HE1  sing N N 211 
HIS   NE2 HE2  sing N N 212 
HIS   OXT HXT  sing N N 213 
HOH   O   H1   sing N N 214 
HOH   O   H2   sing N N 215 
ILE   N   CA   sing N N 216 
ILE   N   H    sing N N 217 
ILE   N   H2   sing N N 218 
ILE   CA  C    sing N N 219 
ILE   CA  CB   sing N N 220 
ILE   CA  HA   sing N N 221 
ILE   C   O    doub N N 222 
ILE   C   OXT  sing N N 223 
ILE   CB  CG1  sing N N 224 
ILE   CB  CG2  sing N N 225 
ILE   CB  HB   sing N N 226 
ILE   CG1 CD1  sing N N 227 
ILE   CG1 HG12 sing N N 228 
ILE   CG1 HG13 sing N N 229 
ILE   CG2 HG21 sing N N 230 
ILE   CG2 HG22 sing N N 231 
ILE   CG2 HG23 sing N N 232 
ILE   CD1 HD11 sing N N 233 
ILE   CD1 HD12 sing N N 234 
ILE   CD1 HD13 sing N N 235 
ILE   OXT HXT  sing N N 236 
LEU   N   CA   sing N N 237 
LEU   N   H    sing N N 238 
LEU   N   H2   sing N N 239 
LEU   CA  C    sing N N 240 
LEU   CA  CB   sing N N 241 
LEU   CA  HA   sing N N 242 
LEU   C   O    doub N N 243 
LEU   C   OXT  sing N N 244 
LEU   CB  CG   sing N N 245 
LEU   CB  HB2  sing N N 246 
LEU   CB  HB3  sing N N 247 
LEU   CG  CD1  sing N N 248 
LEU   CG  CD2  sing N N 249 
LEU   CG  HG   sing N N 250 
LEU   CD1 HD11 sing N N 251 
LEU   CD1 HD12 sing N N 252 
LEU   CD1 HD13 sing N N 253 
LEU   CD2 HD21 sing N N 254 
LEU   CD2 HD22 sing N N 255 
LEU   CD2 HD23 sing N N 256 
LEU   OXT HXT  sing N N 257 
LYS   N   CA   sing N N 258 
LYS   N   H    sing N N 259 
LYS   N   H2   sing N N 260 
LYS   CA  C    sing N N 261 
LYS   CA  CB   sing N N 262 
LYS   CA  HA   sing N N 263 
LYS   C   O    doub N N 264 
LYS   C   OXT  sing N N 265 
LYS   CB  CG   sing N N 266 
LYS   CB  HB2  sing N N 267 
LYS   CB  HB3  sing N N 268 
LYS   CG  CD   sing N N 269 
LYS   CG  HG2  sing N N 270 
LYS   CG  HG3  sing N N 271 
LYS   CD  CE   sing N N 272 
LYS   CD  HD2  sing N N 273 
LYS   CD  HD3  sing N N 274 
LYS   CE  NZ   sing N N 275 
LYS   CE  HE2  sing N N 276 
LYS   CE  HE3  sing N N 277 
LYS   NZ  HZ1  sing N N 278 
LYS   NZ  HZ2  sing N N 279 
LYS   NZ  HZ3  sing N N 280 
LYS   OXT HXT  sing N N 281 
MET   N   CA   sing N N 282 
MET   N   H    sing N N 283 
MET   N   H2   sing N N 284 
MET   CA  C    sing N N 285 
MET   CA  CB   sing N N 286 
MET   CA  HA   sing N N 287 
MET   C   O    doub N N 288 
MET   C   OXT  sing N N 289 
MET   CB  CG   sing N N 290 
MET   CB  HB2  sing N N 291 
MET   CB  HB3  sing N N 292 
MET   CG  SD   sing N N 293 
MET   CG  HG2  sing N N 294 
MET   CG  HG3  sing N N 295 
MET   SD  CE   sing N N 296 
MET   CE  HE1  sing N N 297 
MET   CE  HE2  sing N N 298 
MET   CE  HE3  sing N N 299 
MET   OXT HXT  sing N N 300 
PHE   N   CA   sing N N 301 
PHE   N   H    sing N N 302 
PHE   N   H2   sing N N 303 
PHE   CA  C    sing N N 304 
PHE   CA  CB   sing N N 305 
PHE   CA  HA   sing N N 306 
PHE   C   O    doub N N 307 
PHE   C   OXT  sing N N 308 
PHE   CB  CG   sing N N 309 
PHE   CB  HB2  sing N N 310 
PHE   CB  HB3  sing N N 311 
PHE   CG  CD1  doub Y N 312 
PHE   CG  CD2  sing Y N 313 
PHE   CD1 CE1  sing Y N 314 
PHE   CD1 HD1  sing N N 315 
PHE   CD2 CE2  doub Y N 316 
PHE   CD2 HD2  sing N N 317 
PHE   CE1 CZ   doub Y N 318 
PHE   CE1 HE1  sing N N 319 
PHE   CE2 CZ   sing Y N 320 
PHE   CE2 HE2  sing N N 321 
PHE   CZ  HZ   sing N N 322 
PHE   OXT HXT  sing N N 323 
PRO   N   CA   sing N N 324 
PRO   N   CD   sing N N 325 
PRO   N   H    sing N N 326 
PRO   CA  C    sing N N 327 
PRO   CA  CB   sing N N 328 
PRO   CA  HA   sing N N 329 
PRO   C   O    doub N N 330 
PRO   C   OXT  sing N N 331 
PRO   CB  CG   sing N N 332 
PRO   CB  HB2  sing N N 333 
PRO   CB  HB3  sing N N 334 
PRO   CG  CD   sing N N 335 
PRO   CG  HG2  sing N N 336 
PRO   CG  HG3  sing N N 337 
PRO   CD  HD2  sing N N 338 
PRO   CD  HD3  sing N N 339 
PRO   OXT HXT  sing N N 340 
SER   N   CA   sing N N 341 
SER   N   H    sing N N 342 
SER   N   H2   sing N N 343 
SER   CA  C    sing N N 344 
SER   CA  CB   sing N N 345 
SER   CA  HA   sing N N 346 
SER   C   O    doub N N 347 
SER   C   OXT  sing N N 348 
SER   CB  OG   sing N N 349 
SER   CB  HB2  sing N N 350 
SER   CB  HB3  sing N N 351 
SER   OG  HG   sing N N 352 
SER   OXT HXT  sing N N 353 
THR   N   CA   sing N N 354 
THR   N   H    sing N N 355 
THR   N   H2   sing N N 356 
THR   CA  C    sing N N 357 
THR   CA  CB   sing N N 358 
THR   CA  HA   sing N N 359 
THR   C   O    doub N N 360 
THR   C   OXT  sing N N 361 
THR   CB  OG1  sing N N 362 
THR   CB  CG2  sing N N 363 
THR   CB  HB   sing N N 364 
THR   OG1 HG1  sing N N 365 
THR   CG2 HG21 sing N N 366 
THR   CG2 HG22 sing N N 367 
THR   CG2 HG23 sing N N 368 
THR   OXT HXT  sing N N 369 
TRP   N   CA   sing N N 370 
TRP   N   H    sing N N 371 
TRP   N   H2   sing N N 372 
TRP   CA  C    sing N N 373 
TRP   CA  CB   sing N N 374 
TRP   CA  HA   sing N N 375 
TRP   C   O    doub N N 376 
TRP   C   OXT  sing N N 377 
TRP   CB  CG   sing N N 378 
TRP   CB  HB2  sing N N 379 
TRP   CB  HB3  sing N N 380 
TRP   CG  CD1  doub Y N 381 
TRP   CG  CD2  sing Y N 382 
TRP   CD1 NE1  sing Y N 383 
TRP   CD1 HD1  sing N N 384 
TRP   CD2 CE2  doub Y N 385 
TRP   CD2 CE3  sing Y N 386 
TRP   NE1 CE2  sing Y N 387 
TRP   NE1 HE1  sing N N 388 
TRP   CE2 CZ2  sing Y N 389 
TRP   CE3 CZ3  doub Y N 390 
TRP   CE3 HE3  sing N N 391 
TRP   CZ2 CH2  doub Y N 392 
TRP   CZ2 HZ2  sing N N 393 
TRP   CZ3 CH2  sing Y N 394 
TRP   CZ3 HZ3  sing N N 395 
TRP   CH2 HH2  sing N N 396 
TRP   OXT HXT  sing N N 397 
TYR   N   CA   sing N N 398 
TYR   N   H    sing N N 399 
TYR   N   H2   sing N N 400 
TYR   CA  C    sing N N 401 
TYR   CA  CB   sing N N 402 
TYR   CA  HA   sing N N 403 
TYR   C   O    doub N N 404 
TYR   C   OXT  sing N N 405 
TYR   CB  CG   sing N N 406 
TYR   CB  HB2  sing N N 407 
TYR   CB  HB3  sing N N 408 
TYR   CG  CD1  doub Y N 409 
TYR   CG  CD2  sing Y N 410 
TYR   CD1 CE1  sing Y N 411 
TYR   CD1 HD1  sing N N 412 
TYR   CD2 CE2  doub Y N 413 
TYR   CD2 HD2  sing N N 414 
TYR   CE1 CZ   doub Y N 415 
TYR   CE1 HE1  sing N N 416 
TYR   CE2 CZ   sing Y N 417 
TYR   CE2 HE2  sing N N 418 
TYR   CZ  OH   sing N N 419 
TYR   OH  HH   sing N N 420 
TYR   OXT HXT  sing N N 421 
VAL   N   CA   sing N N 422 
VAL   N   H    sing N N 423 
VAL   N   H2   sing N N 424 
VAL   CA  C    sing N N 425 
VAL   CA  CB   sing N N 426 
VAL   CA  HA   sing N N 427 
VAL   C   O    doub N N 428 
VAL   C   OXT  sing N N 429 
VAL   CB  CG1  sing N N 430 
VAL   CB  CG2  sing N N 431 
VAL   CB  HB   sing N N 432 
VAL   CG1 HG11 sing N N 433 
VAL   CG1 HG12 sing N N 434 
VAL   CG1 HG13 sing N N 435 
VAL   CG2 HG21 sing N N 436 
VAL   CG2 HG22 sing N N 437 
VAL   CG2 HG23 sing N N 438 
VAL   OXT HXT  sing N N 439 
# 
_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                    7HWN 
_atom_sites.fract_transf_matrix[1][1]   0.013741 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000646 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016305 
_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]   0.030712 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.113 6.430   24.150 1.00 31.91 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.265 6.568   23.266 1.00 32.15 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.345 5.392   22.296 1.00 30.93 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.667 4.378   22.501 1.00 31.89 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.552 6.675   24.087 1.00 36.48 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.712 5.524   24.901 1.00 41.81 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.137 5.559   21.236 1.00 27.91 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.370 4.528   20.240 1.00 26.63 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.670 5.093   18.869 1.00 25.12 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.280 6.223   18.555 1.00 25.86 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.355 4.315   18.037 1.00 23.47 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.703 4.738   16.692 1.00 23.75 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.708 3.572   15.703 1.00 22.37 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.779 2.400   16.115 1.00 23.48 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.089 5.401   16.725 1.00 25.31 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.670 3.872   14.400 1.00 21.53 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.824 2.923   13.310 1.00 21.59 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.199 3.139   12.677 1.00 24.29 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.607 4.265   12.432 1.00 24.54 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.751 3.148   12.224 1.00 21.92 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.351 3.082   12.836 1.00 20.89 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.947 2.133   11.089 1.00 23.62 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.317 3.699   11.873 1.00 21.05 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.943 2.049   12.448 1.00 26.82 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.264 2.137   11.843 1.00 28.28 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.243 1.390   10.527 1.00 29.96 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.123 0.164   10.530 1.00 31.20 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.318 1.519   12.784 1.00 29.04 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.478 2.279   14.078 1.00 29.48 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.304 3.394   14.154 1.00 31.04 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.704 1.972   15.185 1.00 30.75 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.422 4.124   15.329 1.00 32.00 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.788 2.715   16.352 1.00 31.80 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.659 3.782   16.424 1.00 32.72 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.744 4.514   17.580 1.00 34.04 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.311 2.104   9.408  1.00 29.91 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.255 1.520   8.065  1.00 31.72 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.358 2.142   7.211  1.00 33.48 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.458 3.364   7.098  1.00 33.62 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.842 1.708   7.424  1.00 33.70 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.359 3.161   7.559  1.00 33.97 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.856 1.271   5.961  1.00 35.28 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.260 1.306   6.679  1.00 35.02 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.391 1.793   5.907  1.00 36.38 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.238 2.758   6.725  1.00 37.64 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.453 2.506   7.912  1.00 39.32 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.588 3.908   6.172  1.00 36.82 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.352 4.924   6.908  1.00 37.28 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.405 6.015   7.499  1.00 33.98 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.798 7.176   7.628  1.00 33.17 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.400 5.561   6.007  1.00 41.68 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.566 4.668   5.661  1.00 48.92 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.958 3.777   6.423  1.00 51.08 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.179 4.913   4.510  1.00 51.49 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.181 5.622   7.895  1.00 31.89 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.195 6.557   8.457  1.00 30.23 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.658 6.087   9.816  1.00 27.39 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.549 4.869   10.080 1.00 27.67 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.974 6.700   7.505  1.00 30.11 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.310 7.269   6.144  1.00 31.51 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.924 8.515   6.019  1.00 33.44 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.961 6.594   4.977  1.00 32.93 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.247 9.039   4.770  1.00 34.59 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.263 7.121   3.720  1.00 34.62 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.879 8.360   3.623  1.00 35.89 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.152 8.912   2.390  1.00 38.54 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.269 7.071   10.649 1.00 24.92 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.622 6.883   11.942 1.00 23.98 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.340 7.721   11.901 1.00 22.78 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.390 8.929   11.654 1.00 22.44 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.541 7.315   13.093 1.00 25.53 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.866 7.571   14.438 1.00 27.28 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.880 7.824   15.554 1.00 30.64 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.434 8.833   16.509 1.00 31.63 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.969 8.576   17.727 1.00 32.98 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.906 7.321   18.174 1.00 32.92 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.600 9.570   18.525 1.00 31.72 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.189 7.059   12.084 1.00 21.09 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.887 7.737   12.084 1.00 20.40 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.383 7.863   13.508 1.00 20.46 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.224 6.827   14.197 1.00 21.62 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.842 6.939   11.277 1.00 21.18 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.515 7.757   11.185 1.00 20.81 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.389 6.563   9.901  1.00 22.65 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.106 9.085   13.963 1.00 19.37 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.647 9.270   15.350 1.00 19.75 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.427 10.214  15.362 1.00 19.21 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.175 10.935  14.381 1.00 19.92 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.779 9.877   16.238 1.00 22.25 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.912 8.883   16.407 1.00 25.71 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.288 11.188  15.630 1.00 22.90 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.708 10.289  16.502 1.00 18.32 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.654 11.303  16.657 1.00 18.39 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.378 12.666  16.652 1.00 19.47 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.392 12.840  17.388 1.00 20.49 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.950 11.178  18.021 1.00 18.84 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.088 9.941   18.109 1.00 20.73 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.560 8.863   18.529 1.00 20.22 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.822 10.057  17.669 1.00 19.44 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.868 13.610  15.862 1.00 18.48 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.548 14.937  15.801 1.00 19.18 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.651 15.601  17.176 1.00 21.77 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.696 16.218  17.502 1.00 22.81 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.817 15.820  14.783 1.00 18.75 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.607 17.110  14.421 1.00 19.03 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.636 17.991  13.609 1.00 19.34 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.251 19.246  13.112 1.00 20.34 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.283 20.368  13.802 1.00 22.98 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.828 20.402  15.055 1.00 24.12 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.803 21.480  13.259 1.00 23.51 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.609 15.423  18.022 1.00 21.72 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.622 16.075  19.335 1.00 23.68 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.631 15.442  20.340 1.00 26.49 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.949 16.068  21.371 1.00 28.62 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.217 16.200  19.921 1.00 24.97 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.609 14.930  20.414 1.00 25.83 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.003 14.028  19.541 1.00 25.71 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.472 14.475  21.681 1.00 26.89 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.532 13.048  20.311 1.00 25.80 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.802 13.263  21.604 1.00 27.59 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.148 14.253  20.025 1.00 25.61 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.132 13.570  20.851 1.00 26.18 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.558 13.578  20.226 1.00 26.89 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.492 12.970  20.798 1.00 28.44 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.641 12.128  21.133 1.00 26.31 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.276 12.062  21.838 1.00 28.13 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.833 10.605  22.073 1.00 28.21 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.278 12.835  23.152 1.00 28.55 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.734 14.242  19.033 1.00 25.11 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.037 14.262  18.387 1.00 25.87 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.093 14.923  19.288 1.00 26.39 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.777 15.887  19.973 1.00 27.72 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.963 15.042  17.082 1.00 25.64 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.305 14.381  19.287 1.00 27.84 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.411 14.883  20.127 1.00 29.41 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.239 15.968  19.380 1.00 30.39 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.042 16.188  18.182 1.00 29.39 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.302 13.691  20.531 1.00 31.41 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.995 13.241  19.366 1.00 34.05 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.531 12.564  21.166 1.00 31.05 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.244 16.598  20.063 1.00 32.13 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.113 17.551  19.378 1.00 33.34 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.874 16.857  18.246 1.00 32.12 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.006 17.433  17.172 1.00 32.62 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.097 18.229  20.360 1.00 37.88 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.499 19.340  21.174 1.00 46.30 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.813 20.668  20.929 1.00 50.75 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 29.642 19.282  22.222 1.00 49.39 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 30.143 21.371  21.831 1.00 51.46 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.428 20.578  22.636 1.00 51.59 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.285 15.574  18.453 1.00 31.79 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.997 14.831  17.410 1.00 32.86 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.103 14.571  16.216 1.00 30.09 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.542 14.679  15.066 1.00 30.21 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.529 13.528  17.958 1.00 36.53 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.438 12.802  16.989 1.00 46.62 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.594 13.192  16.793 1.00 50.27 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.942 11.730  16.363 1.00 49.55 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.810 14.277  16.469 1.00 28.14 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.872 14.132  15.362 1.00 26.89 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.779 15.409  14.529 1.00 26.28 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.840 15.336  13.313 1.00 26.92 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.468 13.771  15.868 1.00 26.08 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.342 12.329  16.324 1.00 28.01 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.912 11.442  15.647 1.00 30.60 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.696 12.094  17.375 1.00 27.38 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.614 16.585  15.168 1.00 26.57 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.477 17.842  14.437 1.00 26.93 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.812 18.262  13.745 1.00 29.04 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.780 18.880  12.682 1.00 29.47 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.011 18.938  15.410 1.00 26.42 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.530 18.977  15.593 1.00 24.92 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.825 18.497  16.655 1.00 26.15 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.569 19.499  14.668 1.00 23.82 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.473 18.758  16.478 1.00 25.17 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.291 19.340  15.251 1.00 24.85 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.664 20.071  13.399 1.00 24.61 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.109 19.760  14.610 1.00 24.78 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.488 20.491  12.763 1.00 24.34 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.239 20.323  13.370 1.00 24.73 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.957 17.866  14.313 1.00 30.25 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.258 18.178  13.690 1.00 32.77 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.547 17.279  12.479 1.00 33.46 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.473 17.567  11.722 1.00 34.52 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.381 18.024  14.702 1.00 33.74 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.852 16.122  12.368 1.00 30.96 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.000 15.222  11.226 1.00 29.91 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.626 15.095  10.535 1.00 28.51 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.288 14.031  10.047 1.00 27.80 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.478 13.850  11.706 1.00 31.03 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.892 13.914  12.246 1.00 37.66 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.846 14.004  11.474 1.00 39.57 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.043 13.831  13.573 1.00 39.09 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.866 16.200  10.474 1.00 27.26 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.546 16.218  9.870  1.00 26.48 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.560 15.849  8.385  1.00 28.13 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.356 16.399  7.629  1.00 30.84 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.956 17.627  10.053 1.00 26.36 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.574 17.839  9.442  1.00 26.46 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.541 16.968  10.166 1.00 26.16 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.173 19.298  9.546  1.00 26.27 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.634 14.952  7.938  1.00 26.32 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.424 14.633  6.524  1.00 27.32 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.055 15.256  6.076  1.00 27.92 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.932 15.907  5.024  1.00 29.16 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.389 13.096  6.346  1.00 29.36 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.873 12.710  4.956  1.00 30.20 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.774 12.507  6.615  1.00 30.25 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.022 15.068  6.920  1.00 25.79 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.678 15.536  6.610  1.00 24.77 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.840 15.607  7.893  1.00 23.27 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.996 14.767  8.774  1.00 23.10 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.031 14.559  5.602  1.00 25.33 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.565 14.760  5.329  1.00 25.25 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.987 15.633  4.448  1.00 26.55 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.491 14.043  5.947  1.00 24.16 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.613 15.473  4.456  1.00 26.61 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.285 14.494  5.366  1.00 25.43 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.439 13.023  6.907  1.00 24.43 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.042 13.959  5.721  1.00 25.42 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.214 12.501  7.256  1.00 25.25 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.030 12.988  6.691  1.00 24.89 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.971 16.590  7.981  1.00 22.08 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.034 16.671  9.099  1.00 22.45 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.713 17.273  8.623  1.00 21.65 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.703 18.107  7.713  1.00 22.52 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.600 17.419  10.295 1.00 23.46 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.138 18.823  10.002 1.00 24.16 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.123 19.946  9.921  1.00 25.42 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.381 20.935  9.191  1.00 29.86 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.062 19.853  10.571 1.00 24.27 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.610 16.862  9.255  1.00 20.83 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.309 17.379  8.921  1.00 20.92 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.540 17.566  10.210 1.00 21.00 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.159 16.587  10.823 1.00 21.19 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.609 16.471  7.905  1.00 22.45 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.319 17.039  7.388  1.00 29.33 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.638 17.744  8.153  1.00 31.65 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.951 16.724  6.217  1.00 29.89 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.365 18.826  10.654 1.00 21.80 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.666 19.102  11.891 0.50 23.37 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.668 19.104  11.892 0.50 23.26 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.212 18.605  11.822 1.00 24.89 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.688 18.095  12.813 1.00 26.62 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.701 20.596  12.201 0.50 26.12 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.710 20.598  12.204 0.50 25.69 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.953 20.875  13.373 0.50 29.19 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.986 21.350  11.244 0.50 28.23 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.575 18.739  10.648 1.00 24.58 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.198 18.305  10.488 1.00 25.31 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.049 16.785  10.639 1.00 24.25 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.952 16.341  10.925 1.00 26.34 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.642 18.764  9.142  1.00 30.42 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.002 17.888  8.083  1.00 34.53 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.140 16.023  10.517 1.00 20.51 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.076 14.540  10.690 1.00 19.43 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.675 14.061  12.000 1.00 19.40 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.621 12.852  12.284 1.00 18.84 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.816 13.832  9.518  1.00 20.08 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.163 14.082  8.161  1.00 21.51 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.955 13.454  7.019  1.00 22.70 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.935 11.971  7.098  1.00 20.29 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.084 11.177  6.042  1.00 22.15 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.207 11.697  4.818  1.00 24.98 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.052 9.850   6.189  1.00 22.60 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.328 14.937  12.751 1.00 19.66 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.087 14.566  13.948 1.00 18.42 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.198 13.585  13.603 1.00 17.42 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.531 12.726  14.434 1.00 18.41 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.209 14.001  15.095 1.00 19.84 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.954 13.731  16.399 1.00 21.79 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.813 14.567  16.783 1.00 22.86 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.675 12.664  17.053 1.00 20.68 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.851 13.733  12.415 1.00 17.41 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.982 12.854  12.065 1.00 17.02 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.268 13.635  11.831 1.00 18.10 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.229 14.731  11.265 1.00 18.86 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.725 12.066  10.773 1.00 17.28 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.659 10.964  10.878 1.00 17.35 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.542 10.268  9.527  1.00 18.22 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.047 9.904   11.932 1.00 17.55 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.388 13.000  12.156 1.00 17.25 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.705 13.550  11.851 1.00 18.85 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.589 12.367  11.468 1.00 19.01 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.501 11.307  12.117 1.00 19.85 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.298 14.305  13.051 1.00 19.24 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.686 14.964  12.734 1.00 20.50 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.854 16.290  13.485 1.00 21.41 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.870 14.060  13.137 1.00 23.43 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.407 12.511  10.406 1.00 18.85 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.335 11.473  9.961  1.00 19.70 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.744 12.074  10.021 1.00 21.68 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.962 13.198  9.522  1.00 22.54 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.015 10.952  8.552  1.00 21.29 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.048 9.903   8.104  1.00 22.34 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.586 10.370  8.516  1.00 20.79 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.639 11.377  10.700 1.00 22.27 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.039 11.819  10.780 1.00 24.51 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.941 10.751  10.159 1.00 27.04 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.538 9.607   9.990  1.00 26.68 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.443 12.108  12.218 1.00 25.33 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.302 10.969  13.051 1.00 27.13 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.196 11.129  9.825  1.00 29.11 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.106 10.168  9.219  1.00 32.63 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.918 9.446   10.295 1.00 35.92 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.166 9.990   11.379 1.00 36.42 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.032 10.865  8.232  1.00 34.89 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.720 11.879  8.946  1.00 37.52 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.315 8.213   9.994  1.00 37.79 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.104 7.373   10.890 1.00 40.64 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.353 6.905   10.129 1.00 45.23 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.396 6.936   8.887  1.00 45.94 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.290 6.143   11.364 1.00 41.29 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.155 5.236   10.274 1.00 42.83 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.911 6.509   11.905 1.00 40.71 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.353 6.460   10.868 1.00 47.78 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.552 5.900   10.251 1.00 50.97 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.436 4.370   10.184 1.00 53.67 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.973 3.749   9.258  1.00 55.60 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.815 6.431   10.933 1.00 52.94 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.669 6.283   12.345 1.00 55.05 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.075 7.889   10.600 1.00 53.37 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.773 3.751   11.174 1.00 53.73 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.588 2.305   11.187 1.00 54.42 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.360 1.971   10.348 1.00 54.78 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.407 2.752   10.303 1.00 54.40 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.396 1.814   12.615 1.00 54.63 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.393 0.837   9.653  1.00 55.07 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.291 0.436   8.796  1.00 55.72 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.167 -0.180  9.618  1.00 54.35 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.414 -1.000  10.504 1.00 55.21 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.784 -0.548  7.722  1.00 59.24 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.964 -0.507  6.436  1.00 65.08 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.547 0.479   5.450  1.00 71.13 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.774 0.606   5.311  1.00 73.45 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.685 1.204   4.738  1.00 70.96 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.945 0.230   9.310  1.00 51.93 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.711 -0.236  9.926  1.00 50.70 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.111 -1.368  9.117  1.00 48.52 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.276 -1.417  7.890  1.00 48.29 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.425 -2.280  9.792  1.00 46.68 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.881 -3.442  9.112  1.00 46.00 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.376 -3.624  9.319  1.00 41.59 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.874 -4.733  9.127  1.00 41.93 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.672 -4.693  9.481  1.00 51.04 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 28.828 -4.971  11.271 1.00 65.14 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.646 -2.545  9.682  1.00 37.14 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.185 -2.646  9.798  1.00 35.33 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.655 -2.631  8.350  1.00 34.71 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.254 -2.025  7.447  1.00 35.79 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.562 -1.438  10.577 1.00 36.92 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.447 -1.545  12.098 1.00 42.02 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.888 -2.556  12.584 1.00 45.03 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.839 -0.569  12.808 1.00 39.69 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.580 -3.323  8.120  1.00 32.90 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.925 -3.388  6.820  1.00 33.36 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.644 -2.557  6.917  1.00 30.55 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.868 -2.774  7.837  1.00 30.12 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.583 -4.864  6.526  1.00 38.21 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.798 -5.486  6.099  1.00 41.55 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.524 -5.026  5.424  1.00 38.17 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.452 -1.587  6.017  1.00 28.27 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.230 -0.793  6.014  1.00 26.01 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.174 -1.502  5.174  1.00 26.19 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.475 -1.953  4.053  1.00 26.90 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.483 0.602   5.439  1.00 26.59 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.703 1.299   6.097  1.00 27.98 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.219 1.463   5.494  1.00 26.33 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.472 1.566   7.661  1.00 28.75 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.957 -1.596  5.677  1.00 24.79 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.841 -2.183  4.944  1.00 23.99 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.419 -1.297  3.768  1.00 24.87 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.441 -0.071  3.884  1.00 23.91 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.645 -2.332  5.928  1.00 23.03 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.080 -1.926  2.590  1.00 26.64 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.615 -1.156  1.423  1.00 28.24 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.289 -1.844  1.112  1.00 29.71 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.254 -2.847  0.372  1.00 31.46 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.618 -1.218  0.267  1.00 29.77 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.018 -0.700  0.650  1.00 29.61 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.097 0.778   1.095  1.00 30.67 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.477 1.179   1.420  1.00 29.03 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.793 2.316   2.050  1.00 30.24 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.846 3.173   2.405  1.00 27.35 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.056 2.587   2.359  1.00 29.69 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.209 -1.313  1.690  1.00 27.93 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.905 -1.968  1.666  1.00 28.63 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.746  -1.055  2.077  1.00 29.57 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.955  0.098   2.449  1.00 29.20 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.960 -3.186  2.591  1.00 28.62 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.070 -2.743  4.368  1.00 25.98 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.499  -1.646  2.111  1.00 30.63 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.322  -0.949  2.600  1.00 31.53 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.696  -1.719  3.759  1.00 30.73 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.494  -1.638  3.963  1.00 31.85 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.273  -0.704  1.475  1.00 35.26 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.781  -1.953  0.778  1.00 43.41 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.186  -3.075  1.189  1.00 44.65 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.962  -1.823  -0.183 1.00 49.04 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.504  -2.468  4.551  1.00 28.40 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.975  -3.204  5.707  1.00 25.89 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.257  -2.234  6.657  1.00 25.52 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.693  -1.087  6.826  1.00 25.33 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.103  -3.926  6.459  1.00 25.52 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.733  -5.436  5.666  1.00 27.44 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.188  -2.706  7.281  1.00 24.42 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.490  -1.997  8.338  1.00 23.98 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.449  -2.839  9.600  1.00 21.13 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.619  -2.600  10.473 1.00 21.78 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.066  -1.560  7.951  1.00 26.29 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.073  -0.340  7.028  1.00 31.32 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.658  0.135   6.729  1.00 36.02 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.163  0.036   5.584  1.00 38.96 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.958  0.608   7.770  1.00 33.65 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.297  -3.913  9.701  1.00 20.60 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.438  -4.705  10.922 1.00 19.67 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.949  -4.909  11.157 1.00 18.49 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.763  -4.997  10.214 1.00 20.61 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.728  -6.073  10.874 1.00 23.73 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.329  -6.861  9.838  1.00 27.66 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.229  -5.940  10.581 1.00 24.77 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.302  -4.952  12.440 1.00 17.87 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.706  -5.114  12.819 1.00 17.48 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.830  -5.250  14.331 1.00 15.82 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.839  -5.496  15.011 1.00 17.09 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.059 -5.149  14.826 1.00 15.65 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.369 -5.289  16.255 1.00 16.03 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.267 -4.106  16.623 1.00 15.51 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.256 -3.840  15.932 1.00 15.76 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.107 -6.637  16.498 1.00 18.16 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.555 -6.752  17.970 1.00 19.78 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.167 -7.784  16.137 1.00 18.18 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.980 -3.471  17.768 1.00 15.32 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.858 -2.402  18.250 1.00 14.55 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.403 -2.685  19.634 1.00 16.22 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.792 -3.395  20.425 1.00 16.17 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.203 -0.980  18.197 1.00 14.48 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.249 -0.669  19.344 1.00 14.88 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.967  -1.225  19.383 1.00 16.55 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.625 0.177   20.387 1.00 15.44 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.066  -0.902  20.399 1.00 17.76 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.727  0.505   21.405 1.00 18.04 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.466  -0.076  21.429 1.00 18.34 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.575  0.251   22.432 1.00 21.48 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.562 -2.085  19.938 1.00 16.05 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.157 -2.213  21.253 1.00 16.58 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.707 -1.046  22.121 1.00 17.41 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.832 0.122   21.718 1.00 17.37 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.702 -2.218  21.201 1.00 17.39 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.280 -2.396  22.588 1.00 19.62 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.049 -3.556  23.307 1.00 20.95 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.986 -1.373  23.207 1.00 22.79 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.563 -3.730  24.599 1.00 22.32 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.518 -1.531  24.485 1.00 23.72 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.303 -2.710  25.179 1.00 24.51 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.792 -2.857  26.473 1.00 29.26 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.177 -1.368  23.318 1.00 18.30 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.689 -0.361  24.286 1.00 19.58 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.583 -0.388  25.552 1.00 20.81 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.430 -1.280  26.400 1.00 22.16 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.232 -0.654  24.623 1.00 20.88 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.536 0.411   25.932 1.00 23.38 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.513 0.574   25.664 1.00 21.60 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.463 0.586   26.756 1.00 24.35 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.798 0.740   28.114 1.00 24.30 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.244 0.094   29.070 1.00 25.66 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.526 1.659   26.559 1.00 30.66 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.951 2.947   26.645 1.00 37.62 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.680 1.497   28.196 1.00 23.36 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.956 1.652   29.490 1.00 24.62 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.238 0.406   29.969 1.00 24.51 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.745 0.408   31.109 1.00 26.23 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.980 2.817   29.478 1.00 25.63 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.962 2.578   28.511 1.00 25.19 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.293 -0.681  29.190 1.00 24.63 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.745 -1.961  29.623 1.00 25.22 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.792 -3.085  29.445 1.00 26.68 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.471 -4.251  29.754 1.00 28.22 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.490 -2.301  28.769 1.00 24.61 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.292  -1.384  28.993 1.00 26.87 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.678  -1.651  30.353 1.00 27.84 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.506  -0.808  30.621 1.00 30.92 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.547  0.386   31.196 1.00 33.43 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.709  0.902   31.596 1.00 32.07 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.423  1.070   31.400 1.00 33.72 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.027 -2.786  28.911 1.00 26.32 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.060 -3.799  28.566 1.00 27.57 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.429 -4.928  27.756 1.00 27.51 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.632 -6.124  28.046 1.00 29.59 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.836 -4.339  29.792 1.00 30.13 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.767 -3.292  30.370 1.00 35.43 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.590 -3.940  31.468 1.00 40.87 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.247 -2.969  32.341 1.00 45.19 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.024 -2.866  33.649 1.00 49.10 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.144 -3.669  34.247 1.00 49.02 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.664 -1.949  34.369 1.00 50.20 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.584 -4.541  26.770 1.00 24.68 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.840 -5.559  26.014 1.00 24.32 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.626 -5.162  24.578 1.00 21.82 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.541 -3.987  24.289 1.00 20.76 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.409 -5.675  26.615 1.00 28.44 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.215 -6.704  27.731 1.00 37.08 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.724  -6.729  28.150 1.00 42.58 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.371  -7.888  29.071 1.00 48.64 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.141  -7.472  30.483 1.00 51.34 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.477 -6.138  23.721 1.00 20.15 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.071 -5.895  22.343 1.00 18.77 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.576 -6.178  22.216 1.00 19.48 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.024 -7.134  22.816 1.00 21.14 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.825 -6.798  21.337 1.00 18.63 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.313 -6.626  21.364 1.00 19.71 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.010 -5.898  20.377 1.00 21.57 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.211 -7.154  22.225 1.00 20.70 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.295 -5.991  20.709 1.00 19.99 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.466 -6.706  21.810 1.00 23.63 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.879  -5.325  21.443 1.00 17.59 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.445  -5.502  21.242 1.00 17.20 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.106  -5.551  19.750 1.00 17.39 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.570  -4.743  18.951 1.00 17.07 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.655  -4.288  21.787 1.00 18.20 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.652  -4.175  23.296 1.00 20.32 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.833  -4.989  24.075 1.00 22.39 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.407  -3.206  23.943 1.00 22.28 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.803  -4.865  25.471 1.00 24.29 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.399  -3.087  25.339 1.00 23.00 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.612  -3.932  26.098 1.00 25.22 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.541  -3.744  27.479 1.00 28.60 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.234  -6.498  19.365 1.00 17.13 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.743  -6.532  17.978 1.00 17.70 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.638  -5.471  17.807 1.00 19.50 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.809  -5.311  18.736 1.00 22.71 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.146  -7.955  17.843 1.00 18.14 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.770  -8.307  19.217 1.00 19.26 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.632  -7.566  20.210 1.00 17.69 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.652  -4.751  16.691 1.00 18.41 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.660  -3.701  16.454 1.00 19.25 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.205  -3.639  15.027 1.00 18.57 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.945  -3.960  14.091 1.00 19.53 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.254  -2.286  16.782 1.00 21.69 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.289  -2.002  18.287 1.00 24.49 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.611  -2.081  16.153 1.00 21.27 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.960  -3.112  14.834 1.00 18.48 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.478  -2.655  13.542 1.00 20.07 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.657  -1.115  13.528 1.00 20.38 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.489  -0.483  14.591 1.00 23.10 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.986  -2.933  13.391 1.00 23.76 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.750  -4.326  13.435 1.00 31.38 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.172  -0.551  12.429 1.00 18.78 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.451  0.897   12.413 1.00 19.32 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.947  1.539   11.149 1.00 21.83 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.797  0.890   10.110 1.00 23.62 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.961  1.212   12.655 1.00 19.06 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.926  0.450   11.748 1.00 16.91 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.405  -0.793  12.119 1.00 17.01 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.378  1.010   10.551 1.00 18.68 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.303  -1.484  11.301 1.00 17.52 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.299  0.335   9.752  1.00 18.66 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.721  -0.932  10.110 1.00 18.30 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.650  2.857   11.232 1.00 21.94 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.076  3.550   10.090 1.00 24.30 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.135  3.865   9.006  1.00 24.39 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.329  3.729   9.244  1.00 23.83 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.377  4.833   10.552 1.00 27.29 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.326  5.734   11.108 1.00 27.32 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.708  4.266   7.779  1.00 25.99 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.671  4.665   6.747  1.00 27.39 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.286  6.022   7.127  1.00 28.17 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.664  6.819   7.815  1.00 29.31 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.993  4.736   5.344  1.00 32.50 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.671  3.337   4.813  1.00 38.41 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.188  3.303   3.348  1.00 44.20 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 1.919  1.859   2.973  1.00 49.96 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.754  1.654   1.511  1.00 54.94 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.515  6.292   6.672  1.00 26.79 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.161  7.584   7.016  1.00 27.98 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.309  8.783   6.628  1.00 29.76 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.819  8.838   5.484  1.00 30.70 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.467  7.571   6.218  1.00 29.32 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.729  6.129   5.896  1.00 30.33 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.364  5.447   5.819  1.00 26.87 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.088  9.708   7.579  1.00 28.92 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.224  10.848  7.265  1.00 31.09 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.529  12.063  8.158  1.00 30.71 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.474  12.008  8.980  1.00 28.74 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.753  10.430  7.285  1.00 35.92 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.308  9.962   8.539  1.00 41.06 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.851  13.214  7.875  1.00 31.16 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.006  14.486  8.588  1.00 33.97 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.062  14.428  9.761  1.00 36.48 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.831  14.394  9.562  1.00 37.38 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.558  15.666  7.696  1.00 35.80 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.600  16.383  6.927  1.00 39.40 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.963  17.437  5.977  1.00 41.45 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.614  17.082  7.851  1.00 39.82 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.602  14.429  10.982 1.00 35.73 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.797  14.295  12.220 1.00 37.16 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.215  15.382  13.232 1.00 39.75 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.382  15.728  13.249 1.00 38.03 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.985  12.851  12.746 1.00 37.41 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.260  11.801  11.903 1.00 38.68 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.624  12.749  14.221 1.00 38.27 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.728  10.395  12.176 1.00 39.88 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.296  15.911  14.060 1.00 42.34 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.606  17.063  14.962 1.00 46.39 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.378  16.678  16.235 1.00 49.23 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 3.054  15.670  16.863 1.00 50.24 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.342  17.869  15.325 1.00 47.35 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.590  19.092  16.167 1.00 49.06 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 1.972  20.289  15.586 1.00 51.01 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.457  19.045  17.542 1.00 50.55 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.216  21.410  16.362 1.00 52.59 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.698  20.167  18.318 1.00 52.00 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 2.083  21.346  17.728 1.00 52.50 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.342  17.518  16.634 1.00 50.87 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.154  17.218  17.846 1.00 53.20 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.341  18.463  18.733 1.00 55.55 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.722  19.510  18.203 1.00 55.91 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.484  16.527  17.459 1.00 53.97 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.276  16.150  18.695 1.00 54.34 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.262  15.305  16.589 1.00 54.94 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 5.185  18.318  20.053 1.00 57.14 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 5.181  19.499  20.963 1.00 59.25 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.597  19.965  21.261 1.00 60.70 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.527  19.312  20.809 1.00 61.11 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.443  19.108  22.239 1.00 62.34 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 4.184  20.224  23.241 1.00 68.78 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 2.879  20.098  24.017 1.00 77.73 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.819  20.556  25.182 1.00 81.17 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.921  19.551  23.455 1.00 79.62 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.729  21.019  22.046 1.00 61.02 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 8.038  21.638  22.304 1.00 61.95 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.945  20.806  23.184 1.00 63.05 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 8.498  19.832  23.737 1.00 64.17 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.796  22.962  22.998 1.00 62.27 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 10.161 21.308  23.367 1.00 62.59 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 11.153 20.551  24.144 1.00 62.33 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 12.450 21.363  24.244 1.00 61.72 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 12.544 22.372  23.525 1.00 62.21 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 11.420 19.229  23.476 1.00 63.83 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 12.176 19.389  22.285 1.00 65.87 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 13.391 20.962  25.094 1.00 60.47 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 14.738 21.591  25.211 1.00 59.74 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 15.325 21.544  23.798 1.00 57.67 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 16.224 22.334  23.503 1.00 58.32 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 15.488 20.787  26.267 1.00 63.27 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 16.966 20.549  26.023 1.00 69.51 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 17.524 19.507  26.981 1.00 77.21 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 18.606 19.735  27.554 1.00 79.36 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 16.861 18.468  27.164 1.00 78.78 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.707 20.731  22.916 1.00 55.10 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.263 20.479  21.566 1.00 52.47 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.481 21.173  20.427 1.00 50.24 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.160 21.703  19.542 1.00 50.52 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.277 18.959  21.400 1.00 51.57 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.777 18.183  22.589 1.00 51.16 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.125 18.126  22.891 1.00 51.69 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.905 17.471  23.391 1.00 51.43 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.592 17.401  23.974 1.00 52.24 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.352 16.745  24.482 1.00 52.13 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.702 16.707  24.771 1.00 53.17 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.157 15.979  25.831 1.00 54.44 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.150 21.140  20.417 1.00 48.17 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.397 21.693  19.257 1.00 46.60 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.195 22.533  19.651 1.00 48.82 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.714 22.426  20.779 1.00 49.44 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.853 20.593  18.338 1.00 43.37 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.886 19.685  17.721 1.00 39.28 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.644 20.092  16.636 1.00 37.82 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.106 18.411  18.216 1.00 37.98 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.592 19.262  16.062 1.00 36.26 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.049 17.569  17.654 1.00 36.08 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.795 17.992  16.571 1.00 34.75 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.729 17.171  16.012 1.00 29.41 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.689 23.370  18.730 1.00 50.06 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.466  24.086  18.954 1.00 51.07 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.327  23.182  18.481 1.00 52.02 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.577  22.272  17.708 1.00 52.67 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.630  25.255  17.959 1.00 51.63 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.327 24.629  16.789 1.00 51.76 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.326 23.706  17.449 1.00 49.95 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 7.108  23.418  18.944 1.00 52.18 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.970  22.651  18.414 1.00 51.97 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 6.021  22.737  16.894 1.00 50.58 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.138  23.848  16.356 1.00 51.28 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.651  23.124  18.961 1.00 52.72 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 6.024  21.576  16.251 1.00 48.68 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.132  21.572  14.794 1.00 46.54 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.707  20.225  14.227 1.00 44.08 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.391  19.313  15.007 1.00 44.56 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.574  21.897  14.395 1.00 46.39 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.431  20.661  14.135 1.00 45.96 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.643  20.479  15.028 1.00 45.75 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.545 19.430  14.567 1.00 45.05 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.651 18.224  15.106 1.00 43.62 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.501 17.345  14.605 1.00 39.42 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.907  17.898  16.145 1.00 44.00 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.650  20.142  12.909 1.00 42.13 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.349  18.860  12.253 1.00 41.00 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.667  18.147  11.967 1.00 36.62 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.525  18.746  11.304 1.00 36.56 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.762  19.106  10.879 1.00 43.00 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.311  19.511  10.861 1.00 46.26 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.336  18.649  10.394 1.00 48.33 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.915  20.760  11.304 1.00 48.42 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.002  19.019  10.366 1.00 50.70 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.585  21.143  11.288 1.00 50.27 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.626  20.270  10.815 1.00 51.97 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.687 20.640  10.801 1.00 55.55 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.791  16.903  12.406 1.00 32.64 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.986  16.112  12.116 1.00 29.01 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.633  15.261  10.891 1.00 27.16 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.547  14.640  10.820 1.00 29.17 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.402  15.263  13.326 1.00 26.98 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.580  14.305  13.016 1.00 25.94 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.243 13.812  14.291 1.00 26.27 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.344 14.526  15.285 1.00 27.65 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.751 12.584  14.271 1.00 22.79 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.524  15.241  9.919  1.00 25.01 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.295  14.501  8.686  1.00 23.88 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.957  13.114  8.769  1.00 23.41 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.829  12.862  9.633  1.00 22.17 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.843  15.285  7.487  1.00 25.89 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.249 15.446  7.566  1.00 26.76 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.507  12.227  7.871  1.00 23.40 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.023  10.871  7.740  1.00 22.89 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.909  10.100  9.044  1.00 21.28 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.790  9.294   9.353  1.00 20.57 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.463 10.908  7.237  1.00 23.42 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.597 11.567  5.895  1.00 27.01 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.611 10.819  4.727  1.00 29.66 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.703 12.885  5.573  1.00 29.47 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.733 11.703  3.731  1.00 30.53 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.782 12.953  4.192  1.00 30.92 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.834  10.348  9.783  1.00 21.16 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.631  9.716   11.077 1.00 21.35 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.580  8.584   10.978 1.00 20.75 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.544  8.728   10.325 1.00 22.59 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.176  10.777  12.096 1.00 22.80 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.032  10.329  13.574 1.00 24.85 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.388  9.981   14.163 1.00 25.01 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.420  11.477  14.431 1.00 27.30 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.846  7.479   11.687 1.00 18.93 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.881  6.354   11.697 1.00 19.06 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.415  6.109   13.140 1.00 20.35 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.285  6.024   14.033 1.00 20.26 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.631  5.085   11.221 1.00 19.18 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.127  5.250   9.765  1.00 22.52 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.210  3.973   9.167  1.00 25.12 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.648  4.180   10.341 1.00 23.39 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.117  5.931   13.397 1.00 20.39 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.661  5.677   14.776 1.00 21.01 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.221  4.223   14.958 1.00 20.40 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.735  3.589   14.013 1.00 20.94 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.417  6.562   15.166 1.00 24.17 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.666  8.053   15.210 1.00 27.87 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.357  8.787   15.634 1.00 29.23 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.774  8.397   16.172 1.00 28.71 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.370  3.748   16.162 1.00 19.55 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.881  2.438   16.587 1.00 20.39 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.337  2.556   18.012 1.00 21.16 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.633  3.541   18.698 1.00 22.29 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.049  1.442   16.601 1.00 20.34 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.510  1.587   18.445 1.00 21.70 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.048  1.561   19.807 1.00 22.86 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.133  0.815   20.600 1.00 24.35 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.430  -0.352  20.327 1.00 24.95 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.321 0.843   19.873 1.00 24.92 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.785 0.702   21.319 1.00 26.58 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.335 1.654   19.063 1.00 25.33 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.708  1.495   21.566 1.00 25.75 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.754  0.875   22.387 1.00 26.01 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.349  1.848   23.361 1.00 27.10 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.046  3.041   23.325 1.00 29.06 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.183  1.330   24.269 1.00 25.94 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.819  2.166   25.265 1.00 26.33 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.065  2.891   24.756 1.00 25.70 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.913  2.268   24.122 1.00 24.52 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.192  1.288   26.450 1.00 25.81 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.713  2.095   27.580 1.00 29.02 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.911  3.020   28.218 1.00 31.02 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.974  2.209   28.057 1.00 30.00 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.683  3.613   29.120 1.00 31.82 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.935  3.152   29.059 1.00 31.25 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.208  4.188   25.041 1.00 26.95 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.368  4.977   24.674 1.00 28.94 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.417  6.107   25.678 1.00 33.34 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.419  6.820   25.845 1.00 35.56 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.181  5.566   23.274 1.00 30.40 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 9.246  6.423   22.859 1.00 34.31 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.546  6.262   26.354 1.00 32.48 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.716  7.388   27.257 1.00 34.45 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.079 8.013   26.998 1.00 37.57 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.892 7.455   26.243 1.00 38.42 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.471  6.959   28.717 1.00 37.46 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 10.401 5.903   29.247 1.00 39.95 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 10.028 5.549   30.674 1.00 42.46 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 10.514 6.249   31.583 1.00 45.34 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.240  4.600   30.888 1.00 40.97 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.329 9.251   27.476 1.00 40.06 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.649 9.846   27.264 1.00 41.61 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.706 8.954   27.922 1.00 39.89 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.637 8.591   29.128 1.00 43.16 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.550 11.214  27.945 1.00 42.53 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 11.097 11.471  28.092 1.00 43.34 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 10.471 10.124  28.285 1.00 40.48 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.646 8.628   27.066 1.00 33.80 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.750 7.711   27.221 1.00 31.25 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.645 6.643   26.135 1.00 27.69 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.643 6.012   25.803 1.00 27.33 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.423 6.415   25.584 1.00 25.49 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.204 5.400   24.557 1.00 23.27 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.585 5.814   23.156 1.00 21.82 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.752 4.934   22.309 1.00 19.61 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.756 4.874   24.547 1.00 23.59 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.471 4.026   25.780 1.00 25.34 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.390 3.315   26.223 1.00 25.10 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.311 4.082   26.308 1.00 25.45 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.820 7.117   22.917 1.00 21.77 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.243 7.547   21.570 1.00 21.46 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.519 6.872   21.179 1.00 20.50 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.420 6.711   22.014 1.00 21.37 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.384 9.059   21.469 1.00 22.24 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.804 9.932   21.463 1.00 25.76 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.581 6.469   19.927 1.00 18.30 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.746 5.758   19.436 1.00 18.49 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.566 4.245   19.370 1.00 19.30 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.366 3.562   18.724 1.00 19.67 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.535 3.716   20.031 1.00 17.96 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.243 2.282   19.892 1.00 16.88 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.914 1.930   18.437 1.00 17.04 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.166 2.651   17.803 1.00 17.17 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.453 0.840   17.926 1.00 15.95 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.236 0.465   16.531 1.00 15.49 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.971 -0.302  16.315 1.00 15.01 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.647 -1.221  17.102 1.00 16.86 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.477 -0.290  16.030 1.00 18.21 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.648 0.716   15.897 1.00 20.40 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.223 -1.018  14.701 1.00 19.99 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.044 -0.028  15.480 1.00 22.98 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.289 0.036   15.210 1.00 13.96 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.123 -0.736  14.708 1.00 14.52 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.643 -1.516  13.485 1.00 15.49 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.301 -0.921  12.598 1.00 15.56 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.033 0.280   14.246 1.00 14.98 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.855 -0.354  13.472 1.00 17.06 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.032 -1.278  14.392 1.00 17.59 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.941  0.774   12.900 1.00 16.69 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.433 -2.863  13.491 1.00 15.30 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.905 -3.715  12.407 1.00 16.19 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.766 -4.548  11.874 1.00 17.38 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.919 -5.022  12.620 1.00 18.19 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.929 -4.731  12.995 1.00 20.77 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.231 -4.132  13.466 1.00 27.98 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.135 -5.220  14.078 1.00 32.24 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.425 -5.228  13.383 1.00 42.46 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.480 -4.520  13.768 1.00 46.01 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.437 -3.805  14.890 1.00 46.72 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 20.606 -4.569  13.071 1.00 48.71 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.820 -4.821  10.582 1.00 18.76 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.919 -5.818  9.951  1.00 20.54 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.818 -6.978  9.418  1.00 23.59 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.032 -6.966  9.634  1.00 23.71 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.104 -5.166  8.839  1.00 20.49 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.123 -4.583  7.435  1.00 22.09 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.243 -7.961  8.635  1.00 26.72 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.073 -9.036  8.091  1.00 29.55 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.153 -8.526  7.102  1.00 30.56 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.154 -9.230  6.876  1.00 33.99 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.181 -10.079 7.364  1.00 34.18 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.384 -9.436  6.211  1.00 40.30 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.365 -10.385 5.601  1.00 48.52 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.144  -10.144 5.644  1.00 50.62 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.852 -11.476 5.021  1.00 49.22 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.973 -7.312  6.529  1.00 28.14 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.885 -6.732  5.541  1.00 28.53 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.079 -5.972  6.181  1.00 28.52 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.076 -5.691  5.495  1.00 31.02 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.084 -5.846  4.548  1.00 28.58 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.930 -6.592  3.900  1.00 29.77 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.596 -6.292  4.162  1.00 30.54 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.959 -7.572  2.960  1.00 32.54 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.870 -7.133  3.445  1.00 33.48 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.641 -7.940  2.725  1.00 34.63 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.979 -5.657  7.495  1.00 25.39 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.054 -4.905  8.136  1.00 23.57 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.534 -3.746  8.969  1.00 20.66 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.393 -3.774  9.425  1.00 21.16 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.357 -2.700  9.134  1.00 19.51 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 16.972 -1.527  9.944  1.00 19.19 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 15.964 -0.660  9.227  1.00 18.10 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.225 -0.198  8.086  1.00 19.32 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.229 -0.725  10.344 1.00 19.96 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.818 0.546   11.062 1.00 18.75 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.150 -1.579  11.232 1.00 20.91 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.846 -0.347  9.906  1.00 18.06 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.807 0.506   9.333  1.00 17.93 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.931 1.961   9.832  1.00 17.22 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.726 2.913   9.074  1.00 17.89 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.432 -0.061  9.783  1.00 19.06 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.292 0.908   9.420  1.00 20.48 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.223 -1.432  9.157  1.00 19.48 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.235 2.125   11.120 1.00 15.90 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.315 3.477   11.689 1.00 17.26 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.713 3.451   13.155 1.00 15.09 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.098 2.408   13.687 1.00 15.64 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.616 4.623   13.819 1.00 14.83 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.008 4.751   15.215 1.00 15.65 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.945 5.459   16.000 1.00 15.93 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.276 6.359   15.472 1.00 15.63 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.360 5.445   15.395 1.00 16.50 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.385 6.808   14.664 1.00 17.88 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.543 4.514   15.023 1.00 19.29 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.751 7.577   15.100 1.00 20.89 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.730 5.051   17.283 1.00 15.05 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.751 5.755   18.126 1.00 15.38 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.071 7.252   18.197 1.00 16.21 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.238 7.607   18.409 1.00 16.50 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.747 5.169   19.553 1.00 16.57 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.832 6.014   20.456 1.00 17.75 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.331 3.682   19.544 1.00 17.96 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.040 8.107   17.977 1.00 16.70 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.223 9.539   17.984 1.00 18.66 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.186 10.284  18.851 1.00 22.17 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 11.496 11.374  19.392 1.00 23.78 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.192 10.040  16.545 1.00 20.15 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.286 11.461  16.465 1.00 21.23 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.987  9.712   19.008 1.00 22.21 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.942  10.374  19.826 1.00 23.54 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.241  9.361   20.721 1.00 25.60 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.327  8.138   20.487 1.00 24.14 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.927  11.117  18.912 1.00 25.78 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.103  10.152  18.244 1.00 27.65 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.586  12.065  17.913 1.00 25.82 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.474  9.853   21.716 1.00 27.68 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.738  8.932   22.583 1.00 30.95 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.546  9.569   23.267 1.00 34.62 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.044  10.569  22.792 1.00 36.26 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 5.097  8.971   24.347 1.00 36.92 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.963  9.487   25.105 1.00 38.70 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.588  8.984   24.680 1.00 39.96 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 2.387  8.541   23.550 1.00 39.43 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.597  9.140   25.574 1.00 40.15 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.213  8.736   25.298 1.00 41.74 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 0.050  7.285   24.807 1.00 39.67 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -0.907 6.987   24.097 1.00 40.78 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.450 9.710   24.318 1.00 45.37 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.761 11.036  24.937 1.00 52.16 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -1.056 11.120  26.133 1.00 54.32 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.749 12.094  24.136 1.00 53.92 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.973  6.392   25.169 1.00 36.97 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.900  5.009   24.735 1.00 33.70 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.293  4.789   23.278 1.00 30.75 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 1.008  3.730   22.724 1.00 31.27 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.977  5.760   22.670 1.00 27.68 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.411  5.622   21.290 1.00 25.65 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.944  5.688   21.259 1.00 24.63 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.554  6.338   22.108 1.00 26.41 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.837  6.758   20.434 1.00 27.05 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.303  6.804   20.351 1.00 30.63 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.180 8.210   19.983 1.00 33.03 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.212 5.727   19.395 1.00 30.92 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.519  5.162   20.190 1.00 21.60 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.954  5.309   19.967 1.00 19.75 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.120  5.752   18.503 1.00 19.12 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.443  5.195   17.632 1.00 19.71 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.736  4.002   20.294 1.00 19.90 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.156  2.781   19.600 1.00 21.35 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.221  4.167   19.935 1.00 19.83 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.975  6.744   18.257 1.00 19.02 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.173  7.220   16.897 1.00 19.19 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.604  6.961   16.442 1.00 18.82 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.539  7.130   17.227 1.00 19.22 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.761  6.502   15.223 1.00 16.59 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.095 6.142   14.684 1.00 16.22 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.425 7.016   13.475 1.00 16.85 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.589  7.163   12.588 1.00 17.42 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.064 4.681   14.177 1.00 15.44 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.579  3.693   15.195 1.00 16.27 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.442 3.154   16.117 1.00 15.09 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.254  3.248   15.186 1.00 17.56 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.982  2.229   17.066 1.00 15.77 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.807  2.296   16.095 1.00 17.65 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.668  1.813   17.048 1.00 16.99 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.627 7.561   13.463 1.00 16.35 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.138 8.264   12.318 1.00 16.06 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.570 7.241   11.271 1.00 16.53 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.491 6.444   11.510 1.00 17.09 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.333 9.149   12.739 1.00 16.16 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.941 7.278   10.088 1.00 16.93 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.277 6.337   9.039  1.00 17.38 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.645 6.666   8.432  1.00 18.33 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.978 7.847   8.265  1.00 18.92 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.227 6.441   7.916  1.00 19.82 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.412 5.420   6.806  1.00 24.71 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.523 4.262   7.105  1.00 22.93 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.519 5.834   5.617  1.00 30.42 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.402 5.605   8.018  1.00 17.68 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.677 5.826   7.297  1.00 17.93 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.697 5.040   5.958  1.00 19.71 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.708 5.094   5.235  1.00 20.65 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.922 5.427   8.125  1.00 18.23 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.053 6.255   9.421  1.00 18.55 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.908 3.921   8.439  1.00 19.09 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.584 4.354   5.606  1.00 19.44 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.556 3.525   4.425  1.00 20.10 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.660 4.294   3.118  1.00 24.22 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.041 3.690   2.105  1.00 26.82 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.287 2.675   4.438  1.00 20.90 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.282 1.673   5.547  1.00 20.90 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.943 0.915   5.526  1.00 21.03 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.823 1.778   5.895  1.00 22.95 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.579  1.342   6.073  1.00 24.06 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.251  0.094   5.740  1.00 23.42 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.638  2.162   6.542  1.00 24.26 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.321 5.588   3.117  1.00 23.77 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.394 6.356   1.870  1.00 26.04 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.821 6.908   1.646  1.00 26.93 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.107 7.449   0.563  1.00 28.51 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.382 7.527   1.890  1.00 28.98 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.647 8.541   2.990  1.00 31.91 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.938 8.117   4.142  1.00 29.79 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.569 9.756   2.710  1.00 31.66 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.736 6.810   2.634  1.00 25.30 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.086 7.397   2.507  1.00 25.32 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.988 6.420   1.780  1.00 26.40 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.827 5.738   2.386  1.00 26.19 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.618 7.723   3.919  1.00 23.97 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.700 8.670   4.735  1.00 24.13 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.253 8.881   6.179  1.00 23.44 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.573 10.054  4.033  1.00 25.66 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.779 6.318   0.451  1.00 26.69 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.456 5.300   -0.341 1.00 29.01 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.962 5.491   -0.360 1.00 31.34 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.702 4.509   -0.496 1.00 33.65 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.900 5.204   -1.791 1.00 29.64 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.391 5.055   -1.965 1.00 32.79 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.087 4.744   -3.419 1.00 35.67 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.782 3.951   -1.051 1.00 32.87 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.427 6.748   -0.212 1.00 30.42 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.840 7.065   -0.213 1.00 31.12 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.599 6.465   0.979  1.00 31.96 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.816 6.378   0.919  1.00 34.20 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.059 8.581   -0.317 1.00 30.11 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.339 9.368   0.743  1.00 29.10 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.078 9.888   0.671  1.00 29.15 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.813 9.646   2.074  1.00 28.05 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.777 10.554  1.841  1.00 28.64 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.845 10.452  2.702  1.00 28.00 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.021 9.394   2.748  1.00 28.83 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.000 10.917  4.006  1.00 28.46 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.199 9.908   4.017  1.00 29.44 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.195 10.656  4.637  1.00 28.53 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.908 6.027   2.058  1.00 31.17 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.604 5.401   3.193  1.00 31.87 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.374 4.146   2.762  1.00 36.61 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.357 3.808   3.413  1.00 36.90 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.599 5.003   4.306  1.00 29.83 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.030 6.155   5.089  1.00 27.74 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.943 5.671   6.018  1.00 27.58 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.117 6.853   5.913  1.00 27.75 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 23.903 3.452   1.689  1.00 40.15 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.441 2.202   1.139  1.00 44.90 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.565 2.342   0.155  1.00 48.88 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.002 1.314   -0.366 1.00 50.30 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.350 1.475   0.354  1.00 47.05 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.263 0.835   1.168  1.00 51.96 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.411 0.764   2.403  1.00 53.61 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.260 0.409   0.572  1.00 54.90 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.945 3.566   -0.219 1.00 50.52 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.997 3.767   -1.209 1.00 53.05 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.962 4.861   -0.759 1.00 54.46 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.881 5.216   -1.505 1.00 55.74 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.374 4.140   -2.561 1.00 56.55 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.613 5.457   -2.530 1.00 62.36 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.457 5.526   -3.508 1.00 69.61 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 24.367 6.524   -4.261 1.00 71.43 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.643 4.575   -3.527 1.00 71.57 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BR5 B 2 .   ? 9.696  14.258  22.263 1.00 48.19 ? 201 A1BR5 A N1  1 
HETATM 1079 C  C4  . A1BR5 B 2 .   ? 10.773 14.826  23.081 1.00 47.95 ? 201 A1BR5 A C4  1 
HETATM 1080 C  C5  . A1BR5 B 2 .   ? 8.737  13.360  22.585 1.00 49.33 ? 201 A1BR5 A C5  1 
HETATM 1081 C  C6  . A1BR5 B 2 .   ? 8.628  12.772  24.004 1.00 52.27 ? 201 A1BR5 A C6  1 
HETATM 1082 C  C7  . A1BR5 B 2 .   ? 8.454  14.481  25.666 1.00 55.83 ? 201 A1BR5 A C7  1 
HETATM 1083 C  C8  . A1BR5 B 2 .   ? 7.373  13.824  26.486 1.00 57.21 ? 201 A1BR5 A C8  1 
HETATM 1084 C  C10 . A1BR5 B 2 .   ? 6.628  13.143  28.670 1.00 58.14 ? 201 A1BR5 A C10 1 
HETATM 1085 C  C13 . A1BR5 B 2 .   ? 9.347  11.445  23.996 1.00 52.82 ? 201 A1BR5 A C13 1 
HETATM 1086 C  C15 . A1BR5 B 2 .   ? 11.160 10.064  23.232 1.00 53.32 ? 201 A1BR5 A C15 1 
HETATM 1087 C  C17 . A1BR5 B 2 .   ? 9.360  9.082   24.422 1.00 52.95 ? 201 A1BR5 A C17 1 
HETATM 1088 O  O1  . A1BR5 B 2 .   ? 7.925  13.001  21.766 1.00 47.70 ? 201 A1BR5 A O1  1 
HETATM 1089 C  C3  . A1BR5 B 2 .   ? 12.129 14.668  22.428 1.00 47.10 ? 201 A1BR5 A C3  1 
HETATM 1090 C  C2  . A1BR5 B 2 .   ? 12.108 15.180  20.991 1.00 46.25 ? 201 A1BR5 A C2  1 
HETATM 1091 C  C19 . A1BR5 B 2 .   ? 9.676  14.824  20.914 1.00 46.91 ? 201 A1BR5 A C19 1 
HETATM 1092 C  C1  . A1BR5 B 2 .   ? 10.986 14.517  20.193 1.00 45.92 ? 201 A1BR5 A C1  1 
HETATM 1093 C  C   . A1BR5 B 2 .   ? 10.962 15.015  18.758 1.00 44.29 ? 201 A1BR5 A C   1 
HETATM 1094 O  O   . A1BR5 B 2 .   ? 10.568 16.152  18.484 1.00 44.08 ? 201 A1BR5 A O   1 
HETATM 1095 N  N   . A1BR5 B 2 .   ? 11.415 14.173  17.843 1.00 41.64 ? 201 A1BR5 A N   1 
HETATM 1096 C  C18 . A1BR5 B 2 .   ? 8.759  10.321  24.546 1.00 52.96 ? 201 A1BR5 A C18 1 
HETATM 1097 C  C16 . A1BR5 B 2 .   ? 10.555 8.955   23.761 1.00 52.98 ? 201 A1BR5 A C16 1 
HETATM 1098 C  C14 . A1BR5 B 2 .   ? 10.563 11.305  23.349 1.00 53.26 ? 201 A1BR5 A C14 1 
HETATM 1099 O  O2  . A1BR5 B 2 .   ? 9.288  13.505  25.038 1.00 54.43 ? 201 A1BR5 A O2  1 
HETATM 1100 C  C12 . A1BR5 B 2 .   ? 6.251  14.778  26.893 1.00 57.87 ? 201 A1BR5 A C12 1 
HETATM 1101 C  C11 . A1BR5 B 2 .   ? 5.601  14.121  28.106 1.00 58.23 ? 201 A1BR5 A C11 1 
HETATM 1102 C  C9  . A1BR5 B 2 .   ? 7.881  13.317  27.836 1.00 57.87 ? 201 A1BR5 A C9  1 
HETATM 1103 ZN ZN  . ZN    C 3 .   ? 10.852 -4.724  5.460  1.00 24.56 2 202 ZN    A ZN  1 
HETATM 1104 S  S   . DMS   D 4 .   ? 19.702 -0.432  19.735 1.00 45.04 ? 203 DMS   A S   1 
HETATM 1105 O  O   . DMS   D 4 .   ? 18.295 -0.726  19.399 1.00 40.92 ? 203 DMS   A O   1 
HETATM 1106 C  C1  . DMS   D 4 .   ? 19.903 -0.008  21.485 1.00 45.10 ? 203 DMS   A C1  1 
HETATM 1107 C  C2  . DMS   D 4 .   ? 20.422 1.104   19.039 1.00 44.60 ? 203 DMS   A C2  1 
HETATM 1108 O  O   . HOH   E 5 .   ? 9.226  18.007  19.841 1.00 50.02 ? 301 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 7.998  19.546  17.518 1.00 30.00 ? 302 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 2.773  8.058   10.128 1.00 47.22 ? 303 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 23.664 -0.259  15.369 1.00 43.14 ? 304 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 10.591 8.077   4.703  1.00 32.03 ? 305 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 20.298 8.615   18.874 1.00 22.01 ? 306 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 15.031 9.516   24.641 1.00 33.25 ? 307 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 23.627 21.581  8.014  1.00 31.57 ? 308 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 22.563 -1.311  4.023  1.00 39.38 ? 309 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 0.590  -0.398  16.428 1.00 22.09 ? 310 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 3.831  -4.879  21.163 1.00 32.67 ? 311 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 1.039  -2.588  19.957 1.00 35.45 ? 312 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 6.044  1.406   5.956  1.00 39.28 ? 313 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 23.014 17.862  19.307 1.00 44.17 ? 314 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 8.737  2.516   2.799  1.00 32.72 ? 315 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 11.309 11.412  11.414 1.00 21.04 ? 316 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 4.434  5.614   24.763 1.00 35.28 ? 317 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 11.534 2.014   33.340 1.00 28.06 ? 318 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 10.196 4.782   3.421  1.00 29.27 ? 319 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 30.141 10.711  19.540 1.00 46.31 ? 320 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 14.963 2.246   23.117 1.00 20.21 ? 321 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 17.809 20.951  9.355  1.00 23.87 ? 322 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 0.405  1.526   24.334 1.00 40.72 ? 323 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? -0.846 -4.725  15.698 0.50 32.51 ? 324 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 17.983 18.620  17.055 1.00 24.91 ? 325 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 13.108 10.314  9.326  1.00 18.03 ? 326 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 15.231 12.030  24.099 1.00 32.73 ? 327 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 8.116  -7.345  8.645  1.00 42.95 ? 328 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 7.042  3.477   32.800 1.00 36.79 ? 329 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 17.886 2.226   23.097 1.00 27.89 ? 330 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 14.744 -4.682  17.070 1.00 28.41 ? 331 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 18.686 12.519  1.634  1.00 40.04 ? 332 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 3.162  3.418   27.435 1.00 37.07 ? 333 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 19.232 8.950   25.562 1.00 45.25 ? 334 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 4.060  -5.249  6.462  1.00 39.39 ? 335 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 14.293 14.314  3.570  1.00 37.75 ? 336 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 5.442  -1.569  24.130 1.00 27.67 ? 337 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 15.443 -4.617  1.513  1.00 33.37 ? 338 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 10.193 4.180   33.669 1.00 40.50 ? 339 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 4.262  -2.257  21.677 1.00 32.66 ? 340 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 19.649 23.406  15.520 1.00 28.57 ? 341 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 4.495  10.272  19.687 1.00 47.72 ? 342 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 6.464  17.703  24.251 1.00 30.00 ? 343 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 6.673  12.725  5.563  1.00 33.77 ? 344 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 1.520  -2.716  17.465 1.00 30.71 ? 345 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 22.394 18.726  5.852  1.00 34.85 ? 346 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 28.774 16.504  23.097 1.00 46.82 ? 347 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 23.944 2.023   19.364 1.00 45.04 ? 348 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 12.063 21.286  12.347 1.00 47.75 ? 349 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 0.625  -3.273  9.868  1.00 49.24 ? 350 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 6.158  22.828  11.301 1.00 57.12 ? 351 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 22.082 8.606   21.122 1.00 31.71 ? 352 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 7.114  11.118  4.270  1.00 47.48 ? 353 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 20.964 21.687  17.724 1.00 37.60 ? 354 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 8.694  22.336  26.628 1.00 46.35 ? 355 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 2.222  1.205   26.560 1.00 41.94 ? 356 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 8.539  19.526  7.118  1.00 60.98 ? 357 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 6.407  2.421   3.292  1.00 43.83 ? 358 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 1.089  -1.664  23.857 1.00 48.56 ? 359 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 11.016 17.678  26.633 1.00 53.11 ? 360 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 20.096 -4.043  22.244 1.00 71.88 ? 361 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 0.632  11.443  17.911 1.00 64.66 ? 362 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   ? 0.4807 0.3515 0.3802 -0.0508 -0.0875 -0.0127 7   SER   A N   
2    C CA  . SER   A 1   ? 0.4613 0.3537 0.4066 -0.0472 -0.0996 -0.0049 7   SER   A CA  
3    C C   . SER   A 1   ? 0.4215 0.3430 0.4106 -0.0358 -0.0943 0.0009  7   SER   A C   
4    O O   . SER   A 1   ? 0.4354 0.3588 0.4176 -0.0334 -0.0882 0.0015  7   SER   A O   
5    C CB  . SER   A 1   ? 0.5219 0.4015 0.4626 -0.0633 -0.1285 0.0070  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.5934 0.4687 0.5265 -0.0716 -0.1432 0.0184  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3629 0.3036 0.3941 -0.0300 -0.0941 0.0042  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3262 0.2884 0.3972 -0.0216 -0.0856 0.0079  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2932 0.2700 0.3915 -0.0153 -0.0732 0.0040  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3080 0.2820 0.3928 -0.0146 -0.0681 -0.0026 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2550 0.2451 0.3916 -0.0117 -0.0665 0.0083  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2479 0.2483 0.4061 -0.0085 -0.0522 0.0045  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2217 0.2288 0.3996 -0.0054 -0.0335 0.0024  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2323 0.2385 0.4216 -0.0042 -0.0339 0.0065  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2560 0.2591 0.4465 -0.0114 -0.0629 0.0127  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2090 0.2198 0.3893 -0.0058 -0.0166 -0.0038 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2057 0.2160 0.3988 -0.0067 0.0050  -0.0081 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2255 0.2383 0.4590 -0.0069 0.0149  -0.0049 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2266 0.2427 0.4632 -0.0085 0.0107  -0.0037 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2221 0.2301 0.3807 -0.0121 0.0171  -0.0165 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2195 0.2275 0.3467 -0.0113 0.0077  -0.0172 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2454 0.2453 0.4070 -0.0174 0.0409  -0.0227 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2299 0.2389 0.3312 -0.0177 0.0119  -0.0196 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2463 0.2570 0.5159 -0.0050 0.0294  -0.0027 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2485 0.2606 0.5655 -0.0044 0.0442  0.0011  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2752 0.2747 0.5883 -0.0086 0.0792  -0.0104 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2907 0.2823 0.6126 -0.0072 0.0921  -0.0129 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2365 0.2550 0.6120 0.0008  0.0327  0.0170  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2402 0.2658 0.6141 -0.0002 -0.0032 0.0294  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2515 0.2830 0.6451 -0.0025 -0.0151 0.0368  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2677 0.2901 0.6104 -0.0013 -0.0241 0.0319  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2672 0.2990 0.6498 -0.0072 -0.0479 0.0465  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2864 0.3077 0.6143 -0.0063 -0.0544 0.0406  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2906 0.3154 0.6373 -0.0099 -0.0668 0.0477  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3167 0.3349 0.6418 -0.0181 -0.0964 0.0552  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2825 0.2767 0.5772 -0.0157 0.0949  -0.0179 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3180 0.2932 0.5941 -0.0252 0.1295  -0.0305 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3328 0.3045 0.6348 -0.0286 0.1505  -0.0309 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3345 0.3148 0.6282 -0.0308 0.1379  -0.0273 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3692 0.3358 0.5754 -0.0371 0.1264  -0.0396 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3757 0.3552 0.5599 -0.0383 0.1020  -0.0343 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4075 0.3492 0.5838 -0.0529 0.1599  -0.0521 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3436 0.3025 0.6844 -0.0282 0.1841  -0.0342 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3514 0.3057 0.7252 -0.0308 0.2094  -0.0339 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3420 0.3211 0.7672 -0.0213 0.1832  -0.0167 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3455 0.3401 0.8083 -0.0113 0.1576  -0.0035 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3330 0.3151 0.7509 -0.0267 0.1841  -0.0161 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3175 0.3208 0.7780 -0.0203 0.1576  -0.0003 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2891 0.3022 0.6997 -0.0220 0.1193  0.0009  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2730 0.2954 0.6921 -0.0227 0.1038  0.0078  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3641 0.3649 0.8549 -0.0246 0.1826  0.0010  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4339 0.4287 0.9963 -0.0201 0.2192  0.0045  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4408 0.4426 1.0575 -0.0104 0.2148  0.0147  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4692 0.4500 1.0372 -0.0276 0.2573  -0.0023 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2794 0.2893 0.6429 -0.0222 0.1058  -0.0051 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2705 0.2867 0.5913 -0.0229 0.0756  -0.0045 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2340 0.2552 0.5515 -0.0161 0.0505  0.0000  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2357 0.2533 0.5625 -0.0130 0.0576  -0.0008 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2929 0.2989 0.5521 -0.0328 0.0841  -0.0152 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3180 0.3151 0.5640 -0.0443 0.1053  -0.0193 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3347 0.3396 0.5963 -0.0449 0.0978  -0.0130 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3540 0.3320 0.5652 -0.0572 0.1321  -0.0295 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3569 0.3526 0.6046 -0.0568 0.1177  -0.0157 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3865 0.3520 0.5770 -0.0716 0.1520  -0.0330 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3931 0.3685 0.6019 -0.0709 0.1442  -0.0256 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.4388 0.4013 0.6243 -0.0865 0.1629  -0.0280 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2069 0.2332 0.5066 -0.0151 0.0233  0.0039  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2011 0.2271 0.4831 -0.0119 0.0003  0.0065  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2032 0.2259 0.4362 -0.0139 -0.0064 -0.0004 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2007 0.2242 0.4278 -0.0162 -0.0114 0.0000  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2098 0.2394 0.5209 -0.0116 -0.0245 0.0191  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2454 0.2681 0.5231 -0.0132 -0.0494 0.0202  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2799 0.3016 0.5825 -0.0181 -0.0757 0.0346  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3106 0.3192 0.5719 -0.0244 -0.0961 0.0324  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.3427 0.3382 0.5722 -0.0297 -0.1126 0.0336  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3386 0.3357 0.5763 -0.0288 -0.1151 0.0395  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.3463 0.3240 0.5348 -0.0371 -0.1256 0.0292  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1929 0.2122 0.3964 -0.0131 -0.0049 -0.0054 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1969 0.2142 0.3638 -0.0141 -0.0097 -0.0091 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2042 0.2164 0.3567 -0.0106 -0.0259 -0.0081 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2203 0.2303 0.3709 -0.0088 -0.0283 -0.0074 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2148 0.2309 0.3589 -0.0177 0.0032  -0.0137 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2183 0.2356 0.3370 -0.0193 -0.0030 -0.0130 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2328 0.2461 0.3818 -0.0252 0.0228  -0.0167 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1961 0.2036 0.3363 -0.0108 -0.0351 -0.0085 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2120 0.2074 0.3311 -0.0102 -0.0463 -0.0097 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2139 0.2038 0.3123 -0.0085 -0.0415 -0.0139 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2181 0.2148 0.3238 -0.0086 -0.0358 -0.0128 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2442 0.2308 0.3704 -0.0148 -0.0632 -0.0054 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2760 0.2689 0.4319 -0.0164 -0.0704 0.0031  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2479 0.2362 0.3859 -0.0164 -0.0639 -0.0050 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2154 0.1909 0.2899 -0.0081 -0.0432 -0.0174 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2228 0.1897 0.2862 -0.0057 -0.0354 -0.0209 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2375 0.1962 0.3060 -0.0085 -0.0410 -0.0216 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2566 0.2036 0.3183 -0.0145 -0.0534 -0.0221 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2452 0.1913 0.2796 -0.0065 -0.0321 -0.0264 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2684 0.2214 0.2978 -0.0035 -0.0255 -0.0253 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2637 0.2173 0.2873 -0.0061 -0.0328 -0.0237 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2473 0.2071 0.2843 0.0014  -0.0129 -0.0238 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2189 0.1829 0.3004 -0.0059 -0.0343 -0.0198 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2281 0.1841 0.3165 -0.0085 -0.0392 -0.0202 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2793 0.2058 0.3419 -0.0127 -0.0415 -0.0282 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2970 0.2131 0.3567 -0.0194 -0.0532 -0.0288 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2130 0.1785 0.3209 -0.0054 -0.0317 -0.0148 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2134 0.1754 0.3342 -0.0084 -0.0372 -0.0130 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2086 0.1771 0.3491 -0.0054 -0.0301 -0.0056 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2166 0.1836 0.3727 -0.0081 -0.0345 -0.0019 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2572 0.2035 0.4125 -0.0073 -0.0323 -0.0069 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2866 0.2086 0.4212 -0.0055 -0.0244 -0.0175 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2583 0.2046 0.4304 -0.0099 -0.0366 -0.0023 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2914 0.2017 0.3323 -0.0109 -0.0300 -0.0343 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3397 0.2141 0.3462 -0.0180 -0.0276 -0.0441 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3901 0.2499 0.3666 -0.0303 -0.0460 -0.0449 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.4398 0.2663 0.3814 -0.0421 -0.0502 -0.0518 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3661 0.2232 0.3596 -0.0134 -0.0047 -0.0509 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.3813 0.2409 0.3592 -0.0124 -0.0004 -0.0511 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3606 0.2509 0.3654 -0.0041 0.0016  -0.0426 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.4178 0.2502 0.3535 -0.0205 0.0027  -0.0585 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3716 0.2546 0.3542 -0.0055 0.0061  -0.0451 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.4196 0.2685 0.3603 -0.0153 0.0068  -0.0542 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3668 0.2488 0.3575 -0.0295 -0.0574 -0.0368 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3817 0.2557 0.3575 -0.0407 -0.0779 -0.0320 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3721 0.2652 0.3844 -0.0432 -0.0959 -0.0212 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3914 0.2832 0.4061 -0.0522 -0.1157 -0.0122 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3826 0.2646 0.3525 -0.0381 -0.0757 -0.0293 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.4234 0.2861 0.3595 -0.0367 -0.0570 -0.0388 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.4223 0.2947 0.3550 -0.0345 -0.0562 -0.0348 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4596 0.2798 0.3454 -0.0510 -0.0572 -0.0476 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3328 0.2440 0.3773 -0.0358 -0.0891 -0.0198 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3242 0.2528 0.4059 -0.0376 -0.1008 -0.0100 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3400 0.2497 0.4128 -0.0517 -0.1231 -0.0056 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.3773 0.2599 0.4161 -0.0589 -0.1241 -0.0135 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3078 0.2519 0.4144 -0.0308 -0.0890 -0.0104 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3436 0.2659 0.4483 -0.0566 -0.1401 0.0078  24  THR   A N   
135  C CA  . THR   A 18  ? 0.3692 0.2764 0.4720 -0.0729 -0.1671 0.0172  24  THR   A CA  
136  C C   . THR   A 18  ? 0.3681 0.2837 0.5029 -0.0733 -0.1698 0.0211  24  THR   A C   
137  O O   . THR   A 18  ? 0.3404 0.2754 0.5009 -0.0611 -0.1508 0.0179  24  THR   A O   
138  C CB  . THR   A 18  ? 0.3806 0.2997 0.5132 -0.0783 -0.1862 0.0346  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.3826 0.3332 0.5780 -0.0671 -0.1765 0.0431  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.3869 0.3002 0.4928 -0.0775 -0.1835 0.0324  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.3948 0.2963 0.5296 -0.0896 -0.1955 0.0303  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.3951 0.3063 0.5654 -0.0906 -0.1994 0.0361  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3449 0.2927 0.5827 -0.0794 -0.1907 0.0483  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3386 0.3001 0.6009 -0.0718 -0.1754 0.0462  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4636 0.3526 0.6232 -0.1127 -0.2319 0.0463  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6055 0.4533 0.7003 -0.1250 -0.2336 0.0310  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.6653 0.5023 0.7606 -0.1291 -0.2339 0.0270  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.6784 0.4908 0.7074 -0.1350 -0.2330 0.0189  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.7098 0.5043 0.7412 -0.1409 -0.2321 0.0118  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.7316 0.5088 0.7199 -0.1454 -0.2303 0.0061  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3269 0.2881 0.5928 -0.0784 -0.1965 0.0600  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3088 0.2998 0.6399 -0.0679 -0.1820 0.0699  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2725 0.2742 0.5967 -0.0529 -0.1480 0.0552  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2569 0.2743 0.6164 -0.0470 -0.1298 0.0564  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3416 0.3410 0.7052 -0.0699 -0.1940 0.0854  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4352 0.4609 0.8752 -0.0608 -0.1781 0.0975  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4606 0.4965 0.9529 -0.0654 -0.1874 0.1130  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4662 0.5013 0.9153 -0.0487 -0.1517 0.0906  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.2674 0.2586 0.5432 -0.0487 -0.1391 0.0416  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2524 0.2518 0.5175 -0.0381 -0.1117 0.0299  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2452 0.2451 0.5081 -0.0377 -0.1036 0.0255  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2431 0.2561 0.5237 -0.0336 -0.0850 0.0248  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.2619 0.2497 0.4794 -0.0350 -0.1065 0.0187  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2843 0.2754 0.5044 -0.0330 -0.1070 0.0217  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2994 0.3059 0.5574 -0.0287 -0.0969 0.0274  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2935 0.2693 0.4777 -0.0365 -0.1159 0.0184  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2629 0.2457 0.5011 -0.0435 -0.1163 0.0222  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2677 0.2498 0.5057 -0.0431 -0.1096 0.0191  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2749 0.2704 0.5581 -0.0465 -0.1122 0.0299  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2745 0.2778 0.5673 -0.0446 -0.0994 0.0295  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2820 0.2376 0.4842 -0.0491 -0.1206 0.0121  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2785 0.2228 0.4456 -0.0431 -0.1072 0.0008  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3114 0.2381 0.4441 -0.0445 -0.1084 -0.0060 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2620 0.2129 0.4301 -0.0357 -0.0906 -0.0024 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3063 0.2278 0.4220 -0.0371 -0.0912 -0.0141 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2889 0.2266 0.4287 -0.0316 -0.0818 -0.0105 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2594 0.2255 0.4503 -0.0337 -0.0830 0.0028  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2861 0.2277 0.4278 -0.0248 -0.0674 -0.0115 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2567 0.2252 0.4430 -0.0288 -0.0712 0.0020  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2721 0.2298 0.4379 -0.0240 -0.0644 -0.0041 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2789 0.2779 0.5927 -0.0522 -0.1281 0.0415  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2886 0.3021 0.6546 -0.0549 -0.1288 0.0539  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2790 0.3120 0.6801 -0.0472 -0.1018 0.0559  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2751 0.3192 0.7174 -0.0483 -0.0929 0.0636  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2916 0.3035 0.6869 -0.0649 -0.1565 0.0696  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2514 0.2864 0.6385 -0.0410 -0.0881 0.0494  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2271 0.2732 0.6363 -0.0360 -0.0590 0.0478  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2276 0.2684 0.5874 -0.0335 -0.0425 0.0339  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2195 0.2617 0.5751 -0.0308 -0.0244 0.0292  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2284 0.2800 0.6705 -0.0328 -0.0583 0.0549  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2893 0.3493 0.7925 -0.0366 -0.0749 0.0737  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2936 0.3636 0.8462 -0.0361 -0.0591 0.0810  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3098 0.3646 0.8110 -0.0421 -0.1066 0.0832  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2250 0.2590 0.5517 -0.0354 -0.0492 0.0291  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2293 0.2600 0.5169 -0.0345 -0.0388 0.0209  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2488 0.2840 0.5358 -0.0387 -0.0144 0.0196  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2757 0.3140 0.5822 -0.0434 -0.0062 0.0239  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2366 0.2599 0.5050 -0.0360 -0.0502 0.0200  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2484 0.2701 0.4870 -0.0357 -0.0431 0.0165  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2536 0.2711 0.4693 -0.0307 -0.0440 0.0107  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2498 0.2648 0.4835 -0.0366 -0.0519 0.0183  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2358 0.2687 0.4957 -0.0393 -0.0026 0.0136  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2551 0.2851 0.4978 -0.0484 0.0189  0.0113  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2760 0.3037 0.4811 -0.0538 0.0112  0.0124  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2967 0.3225 0.4887 -0.0643 0.0159  0.0167  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2835 0.3093 0.5229 -0.0482 0.0365  0.0051  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3093 0.3249 0.5131 -0.0617 0.0569  0.0006  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2775 0.3065 0.5653 -0.0434 0.0470  0.0075  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2537 0.2814 0.4448 -0.0472 -0.0012 0.0106  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2486 0.2761 0.4162 -0.0508 -0.0082 0.0145  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2305 0.2570 0.3965 -0.0401 -0.0205 0.0124  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2285 0.2531 0.3959 -0.0337 -0.0209 0.0067  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2660 0.2904 0.4060 -0.0617 0.0031  0.0138  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2710 0.2970 0.3915 -0.0668 -0.0068 0.0211  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2896 0.3169 0.4021 -0.0780 -0.0141 0.0329  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2594 0.2869 0.3717 -0.0616 -0.0114 0.0200  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2920 0.3228 0.3961 -0.0803 -0.0238 0.0408  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2772 0.3081 0.3807 -0.0699 -0.0209 0.0321  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2628 0.2894 0.3762 -0.0518 -0.0086 0.0116  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2776 0.3117 0.3767 -0.0680 -0.0264 0.0359  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2758 0.3042 0.3793 -0.0500 -0.0131 0.0135  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2715 0.3042 0.3701 -0.0573 -0.0213 0.0254  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2161 0.2421 0.3808 -0.0390 -0.0286 0.0177  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2233 0.2446 0.3849 -0.0300 -0.0340 0.0150  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2117 0.2363 0.3748 -0.0319 -0.0363 0.0247  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2188 0.2472 0.3895 -0.0389 -0.0394 0.0344  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2374 0.2479 0.4063 -0.0238 -0.0405 0.0096  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2422 0.2499 0.4257 -0.0263 -0.0452 0.0139  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2574 0.2610 0.4476 -0.0244 -0.0459 0.0195  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3082 0.3145 0.5120 -0.0287 -0.0487 0.0271  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2463 0.2438 0.4321 -0.0186 -0.0425 0.0174  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2027 0.2261 0.3625 -0.0262 -0.0352 0.0241  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1981 0.2262 0.3704 -0.0269 -0.0374 0.0362  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2000 0.2185 0.3793 -0.0152 -0.0319 0.0309  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2071 0.2239 0.3739 -0.0117 -0.0277 0.0249  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2178 0.2561 0.3791 -0.0377 -0.0397 0.0455  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2957 0.3419 0.4768 -0.0420 -0.0470 0.0641  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3173 0.3611 0.5241 -0.0311 -0.0444 0.0669  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3039 0.3568 0.4749 -0.0578 -0.0549 0.0770  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2073 0.2161 0.4047 -0.0098 -0.0297 0.0319  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2316 0.2243 0.4322 -0.0003 -0.0187 0.0246  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2302 0.2229 0.4308 -0.0003 -0.0187 0.0246  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2424 0.2440 0.4591 0.0028  -0.0130 0.0344  36  SER   A C   
244  O O   . SER   A 30  ? 0.2709 0.2623 0.4782 0.0088  -0.0023 0.0261  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2651 0.2428 0.4846 0.0032  -0.0141 0.0245  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2598 0.2374 0.4790 0.0032  -0.0142 0.0244  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3109 0.2674 0.5309 0.0110  0.0021  0.0159  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2756 0.2659 0.5312 0.0021  -0.0170 0.0429  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2247 0.2446 0.4647 -0.0034 -0.0214 0.0537  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2229 0.2539 0.4851 -0.0028 -0.0201 0.0676  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2170 0.2529 0.4515 -0.0054 -0.0204 0.0615  37  SER   A C   
252  O O   . SER   A 31  ? 0.2368 0.2773 0.4866 -0.0022 -0.0156 0.0683  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2723 0.3210 0.5625 -0.0136 -0.0350 0.0931  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3307 0.3898 0.5914 -0.0292 -0.0485 0.0975  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1819 0.2159 0.3814 -0.0102 -0.0242 0.0492  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1757 0.2121 0.3506 -0.0123 -0.0231 0.0426  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1871 0.2089 0.3412 -0.0040 -0.0150 0.0245  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1853 0.2080 0.3223 -0.0044 -0.0137 0.0194  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1891 0.2320 0.3420 -0.0257 -0.0309 0.0436  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2009 0.2548 0.3615 -0.0404 -0.0418 0.0629  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2270 0.2791 0.3565 -0.0565 -0.0445 0.0607  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2058 0.2544 0.3106 -0.0597 -0.0391 0.0516  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2405 0.2846 0.3166 -0.0772 -0.0393 0.0523  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2811 0.3231 0.3449 -0.0950 -0.0459 0.0625  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2546 0.2931 0.3111 -0.0790 -0.0325 0.0432  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1958 0.2030 0.3481 0.0010  -0.0118 0.0156  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1940 0.1846 0.3214 0.0037  -0.0095 0.0008  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1836 0.1810 0.2974 -0.0013 -0.0176 -0.0026 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2040 0.1944 0.3010 -0.0004 -0.0181 -0.0095 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2198 0.1987 0.3353 0.0088  0.0012  -0.0048 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2622 0.2195 0.3462 0.0076  0.0010  -0.0179 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2834 0.2261 0.3591 0.0047  -0.0033 -0.0235 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2551 0.2091 0.3215 0.0075  0.0032  -0.0212 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1769 0.1856 0.2990 -0.0073 -0.0227 0.0027  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1728 0.1853 0.2888 -0.0115 -0.0248 -0.0010 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1837 0.1945 0.3095 -0.0138 -0.0290 -0.0017 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1896 0.2020 0.3252 -0.0159 -0.0306 0.0033  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1737 0.1968 0.2860 -0.0196 -0.0215 0.0041  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1771 0.2029 0.2792 -0.0199 -0.0187 0.0052  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1902 0.2206 0.2815 -0.0324 -0.0163 0.0092  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1842 0.2041 0.2786 -0.0142 -0.0167 -0.0033 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1725 0.1820 0.3008 -0.0142 -0.0310 -0.0054 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1870 0.1976 0.3318 -0.0171 -0.0344 -0.0039 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1832 0.1995 0.3394 -0.0189 -0.0284 -0.0042 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1957 0.2103 0.3483 -0.0162 -0.0287 -0.0063 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1958 0.1941 0.3412 -0.0159 -0.0460 -0.0059 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2033 0.2041 0.3714 -0.0199 -0.0519 -0.0019 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2215 0.2078 0.3844 -0.0217 -0.0623 -0.0032 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2329 0.2371 0.4201 -0.0212 -0.0573 0.0013  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1745 0.1960 0.3456 -0.0238 -0.0203 -0.0018 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1786 0.2025 0.3675 -0.0254 -0.0083 -0.0025 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1916 0.2182 0.4138 -0.0256 -0.0114 0.0024  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2014 0.2291 0.4260 -0.0291 -0.0130 0.0050  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2041 0.2267 0.3782 -0.0338 0.0104  -0.0050 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2112 0.2311 0.4067 -0.0351 0.0294  -0.0077 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2086 0.2293 0.3521 -0.0355 0.0094  -0.0070 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1891 0.2174 0.4397 -0.0224 -0.0149 0.0060  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2020 0.2350 0.4942 -0.0234 -0.0191 0.0141  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2200 0.2571 0.5502 -0.0226 0.0019  0.0166  43  SER   A C   
300  O O   . SER   A 37  ? 0.2188 0.2529 0.5422 -0.0209 0.0149  0.0118  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2105 0.2408 0.5113 -0.0231 -0.0457 0.0211  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2335 0.2621 0.5353 -0.0207 -0.0518 0.0230  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2295 0.2723 0.6043 -0.0239 0.0070  0.0244  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2585 0.3032 0.6780 -0.0225 0.0324  0.0270  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2805 0.3324 0.7517 -0.0176 0.0176  0.0407  44  SER   A C   
306  O O   . SER   A 38  ? 0.2833 0.3389 0.7614 -0.0190 -0.0139 0.0508  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2773 0.3240 0.7242 -0.0268 0.0505  0.0298  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2988 0.3542 0.7726 -0.0270 0.0245  0.0418  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2930 0.3440 0.7988 -0.0139 0.0402  0.0415  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3069 0.3655 0.8718 -0.0095 0.0287  0.0576  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3389 0.4015 0.9782 -0.0066 0.0600  0.0651  45  THR   A C   
312  O O   . THR   A 39  ? 0.3541 0.4076 0.9838 -0.0086 0.0962  0.0527  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3243 0.3769 0.8677 -0.0059 0.0286  0.0527  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3468 0.3896 0.8911 -0.0043 0.0687  0.0405  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3441 0.3904 0.8123 -0.0083 0.0087  0.0422  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3428 0.4167 1.0559 -0.0035 0.0468  0.0864  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3535 0.4317 1.1516 0.0010  0.0788  0.0964  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3816 0.4523 1.2053 0.0075  0.1035  0.0939  46  THR   A C   
319  O O   . THR   A 40  ? 0.3951 0.4574 1.2602 0.0110  0.1485  0.0890  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3459 0.4426 1.2231 -0.0004 0.0521  0.1246  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3711 0.4742 1.2464 -0.0039 0.0047  0.1409  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3558 0.4561 1.2159 -0.0067 0.0434  0.1236  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3898 0.4609 1.1909 0.0086  0.0764  0.0975  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3939 0.4575 1.2165 0.0145  0.0962  0.0958  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4332 0.4764 1.1719 0.0123  0.1229  0.0666  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4550 0.4952 1.1166 0.0068  0.1075  0.0540  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3906 0.4629 1.2222 0.0143  0.0534  0.1139  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4362 0.4641 1.1922 0.0154  0.1635  0.0567  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4781 0.4836 1.1555 0.0097  0.1888  0.0306  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4754 0.4807 1.1090 0.0107  0.1634  0.0285  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4687 0.4802 1.1487 0.0171  0.1518  0.0427  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.5206 0.5029 1.2275 0.0095  0.2457  0.0188  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.6322 0.5868 1.2537 -0.0037 0.2773  -0.0083 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.7119 0.6625 1.3283 -0.0110 0.2965  -0.0126 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.7128 0.6723 1.4055 -0.0053 0.3099  0.0001  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7429 0.6804 1.2727 -0.0249 0.2975  -0.0282 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4755 0.4739 1.0237 0.0038  0.1548  0.0129  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4774 0.4739 0.9750 0.0034  0.1348  0.0083  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4668 0.4409 0.9357 -0.0009 0.1680  -0.0086 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4752 0.4307 0.9289 -0.0085 0.2037  -0.0224 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4477 0.4202 0.9057 0.0018  0.1571  -0.0076 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4553 0.4045 0.8881 -0.0032 0.1873  -0.0229 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4238 0.3702 0.7862 -0.0088 0.1693  -0.0307 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4379 0.3687 0.7865 -0.0116 0.1841  -0.0385 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4974 0.4410 1.0011 0.0051  0.2062  -0.0153 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.6464 0.6169 1.2118 0.0168  0.1625  0.0135  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3770 0.3369 0.6972 -0.0110 0.1400  -0.0288 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3750 0.3329 0.6346 -0.0165 0.1260  -0.0348 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3904 0.3280 0.6003 -0.0319 0.1502  -0.0502 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4068 0.3370 0.6159 -0.0383 0.1675  -0.0549 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3974 0.3731 0.6323 -0.0142 0.0921  -0.0279 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4532 0.4413 0.7022 -0.0058 0.0636  -0.0158 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4943 0.4790 0.7378 -0.0044 0.0614  -0.0151 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4169 0.4157 0.6755 -0.0029 0.0428  -0.0074 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3852 0.3117 0.5534 -0.0399 0.1514  -0.0570 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4169 0.3214 0.5291 -0.0593 0.1680  -0.0691 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3912 0.3091 0.4603 -0.0651 0.1390  -0.0637 52  THR   A C   
358  O O   . THR   A 46  ? 0.3814 0.3124 0.4505 -0.0577 0.1183  -0.0574 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4908 0.3714 0.5897 -0.0663 0.1883  -0.0787 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.5267 0.3886 0.6635 -0.0644 0.2239  -0.0857 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.5213 0.3794 0.5495 -0.0902 0.1934  -0.0882 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3739 0.2887 0.4117 -0.0778 0.1379  -0.0645 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3519 0.2789 0.3575 -0.0840 0.1119  -0.0566 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3770 0.2852 0.3328 -0.1049 0.1148  -0.0603 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4054 0.2858 0.3307 -0.1235 0.1379  -0.0705 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3593 0.2925 0.3583 -0.0893 0.1061  -0.0521 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3563 0.3035 0.4032 -0.0723 0.1059  -0.0492 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3583 0.3058 0.3363 -0.0939 0.0792  -0.0409 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3491 0.3186 0.4246 -0.0532 0.0808  -0.0405 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3586 0.2791 0.3043 -0.1043 0.0930  -0.0522 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3680 0.2741 0.2695 -0.1257 0.0890  -0.0514 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3941 0.2934 0.2576 -0.1486 0.0807  -0.0452 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3707 0.2885 0.2493 -0.1425 0.0667  -0.0356 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3450 0.2721 0.2581 -0.1160 0.0657  -0.0403 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4443 0.3132 0.2549 -0.1779 0.0899  -0.0504 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4822 0.3412 0.2494 -0.2054 0.0781  -0.0415 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.5149 0.3659 0.2481 -0.2265 0.0604  -0.0330 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5643 0.3804 0.2508 -0.2498 0.0756  -0.0441 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5260 0.3499 0.2554 -0.2253 0.1075  -0.0559 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5062 0.3389 0.2799 -0.2025 0.1278  -0.0639 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.4970 0.3629 0.3053 -0.1871 0.1055  -0.0495 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.4609 0.3323 0.3097 -0.1686 0.1245  -0.0567 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.4542 0.3528 0.3418 -0.1505 0.1093  -0.0476 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4088 0.3294 0.3007 -0.1476 0.0793  -0.0326 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4332 0.3359 0.3590 -0.1356 0.1248  -0.0528 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4737 0.3552 0.2324 -0.2189 0.0301  -0.0134 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4870 0.3692 0.2316 -0.2329 0.0108  -0.0018 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4762 0.3924 0.2550 -0.2273 -0.0213 0.0241  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4527 0.3909 0.2657 -0.2109 -0.0274 0.0315  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4810 0.3623 0.2440 -0.2152 0.0243  -0.0139 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.4107 0.3317 0.2449 -0.1718 0.0198  -0.0102 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.4892 0.4097 0.2649 -0.2392 -0.0400 0.0380  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4752 0.4281 0.2945 -0.2320 -0.0664 0.0636  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4490 0.4171 0.3014 -0.2118 -0.0648 0.0633  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4485 0.4348 0.3267 -0.2147 -0.0843 0.0844  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5323 0.4806 0.3266 -0.2686 -0.0960 0.0892  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6625 0.5824 0.4047 -0.2999 -0.1003 0.0872  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6873 0.5921 0.4170 -0.2910 -0.0785 0.0656  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.7460 0.6575 0.4598 -0.3353 -0.1272 0.1088  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.4205 0.3819 0.2768 -0.1915 -0.0415 0.0414  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3751 0.3491 0.2596 -0.1730 -0.0393 0.0411  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3426 0.3482 0.2788 -0.1523 -0.0500 0.0572  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3304 0.3463 0.2857 -0.1405 -0.0492 0.0585  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3729 0.3369 0.2600 -0.1534 -0.0152 0.0185  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4256 0.3509 0.2661 -0.1726 0.0046  -0.0012 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3168 0.3352 0.2757 -0.1481 -0.0569 0.0683  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2867 0.3297 0.2948 -0.1271 -0.0586 0.0802  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2468 0.2909 0.2651 -0.1087 -0.0452 0.0703  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2385 0.2980 0.2910 -0.0961 -0.0443 0.0804  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2999 0.3606 0.3384 -0.1393 -0.0791 0.1091  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3597 0.4257 0.4047 -0.1510 -0.0935 0.1237  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3979 0.4844 0.4862 -0.1618 -0.1155 0.1570  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4421 0.5247 0.5135 -0.1918 -0.1391 0.1754  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3422 0.4487 0.4876 -0.1395 -0.1076 0.1664  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2557 0.2817 0.2455 -0.1084 -0.0335 0.0515  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2413 0.2667 0.2392 -0.0916 -0.0221 0.0426  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2354 0.2470 0.2202 -0.0822 -0.0085 0.0233  60  THR   A C   
418  O O   . THR   A 54  ? 0.2743 0.2712 0.2376 -0.0929 -0.0041 0.0144  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2983 0.3173 0.2861 -0.1023 -0.0243 0.0452  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3680 0.3638 0.3193 -0.1205 -0.0212 0.0343  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3003 0.3341 0.3067 -0.1140 -0.0400 0.0677  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2214 0.2369 0.2207 -0.0635 -0.0018 0.0185  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2205 0.2262 0.2174 -0.0542 0.0071  0.0053  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1945 0.2034 0.2031 -0.0385 0.0090  0.0049  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2071 0.2219 0.2203 -0.0360 0.0076  0.0119  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1929 0.1963 0.2055 -0.0303 0.0118  -0.0021 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1968 0.1987 0.2136 -0.0200 0.0103  -0.0015 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1889 0.1909 0.2096 -0.0138 0.0073  -0.0039 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1905 0.1906 0.2177 -0.0151 0.0084  -0.0082 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2253 0.2178 0.2470 -0.0198 0.0126  -0.0040 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2460 0.2356 0.2700 -0.0127 0.0063  -0.0001 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2283 0.2185 0.2438 -0.0271 0.0157  -0.0023 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1888 0.1896 0.2038 -0.0084 0.0051  -0.0017 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1809 0.1773 0.1948 -0.0048 0.0009  -0.0042 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2093 0.1944 0.2124 -0.0040 -0.0056 -0.0028 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2141 0.1943 0.2060 -0.0050 -0.0045 0.0002  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.1794 0.1786 0.1921 -0.0027 0.0044  -0.0041 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.1908 0.1827 0.1919 0.0000  0.0112  -0.0028 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2087 0.2060 0.2142 -0.0002 0.0184  0.0025  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2084 0.1851 0.1930 0.0009  0.0120  -0.0069 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2291 0.2182 0.2276 0.0023  0.0299  0.0035  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.2505 0.2146 0.2202 0.0016  0.0241  -0.0078 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.2493 0.2199 0.2275 0.0031  0.0345  -0.0027 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.2978 0.2542 0.2644 0.0040  0.0514  -0.0039 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2083 0.1881 0.2136 -0.0042 -0.0140 -0.0034 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2241 0.1907 0.2153 -0.0078 -0.0252 0.0007  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.2488 0.2015 0.2110 -0.0102 -0.0230 -0.0030 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.2473 0.2006 0.2119 -0.0083 -0.0202 -0.0076 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2271 0.1941 0.2396 -0.0094 -0.0384 0.0053  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.2653 0.2179 0.2622 -0.0173 -0.0555 0.0139  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.2857 0.2335 0.2768 -0.0209 -0.0605 0.0213  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3139 0.2552 0.2969 -0.0238 -0.0680 0.0153  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.3147 0.2470 0.2865 -0.0320 -0.0794 0.0318  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.3382 0.2627 0.3002 -0.0360 -0.0874 0.0251  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.3518 0.2718 0.3074 -0.0407 -0.0937 0.0340  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.4274 0.3282 0.3562 -0.0565 -0.1156 0.0459  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.2751 0.2122 0.2082 -0.0153 -0.0221 -0.0015 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.3102 0.2257 0.2081 -0.0200 -0.0143 -0.0071 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.3450 0.2365 0.2092 -0.0336 -0.0313 -0.0032 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.3723 0.2535 0.2161 -0.0410 -0.0362 0.0027  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.3314 0.2435 0.2185 -0.0178 0.0050  -0.0088 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.3896 0.2674 0.2312 -0.0246 0.0238  -0.0174 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.3601 0.2425 0.2181 -0.0389 -0.0423 -0.0046 66  SER   A N   
464  C CA  . SER   A 60  ? 0.4121 0.2725 0.2405 -0.0552 -0.0641 0.0023  66  SER   A CA  
465  C C   . SER   A 60  ? 0.4436 0.2689 0.2109 -0.0694 -0.0569 -0.0020 66  SER   A C   
466  O O   . SER   A 60  ? 0.4753 0.2846 0.2153 -0.0849 -0.0752 0.0081  66  SER   A O   
467  C CB  . SER   A 60  ? 0.4911 0.3480 0.3257 -0.0592 -0.0772 0.0019  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.5931 0.4334 0.4028 -0.0589 -0.0599 -0.0116 66  SER   A OG  
469  N N   . SER   A 61  ? 0.4423 0.2551 0.1902 -0.0651 -0.0287 -0.0154 67  SER   A N   
470  C CA  . SER   A 61  ? 0.4914 0.2655 0.1784 -0.0791 -0.0135 -0.0220 67  SER   A CA  
471  C C   . SER   A 61  ? 0.4930 0.2679 0.1704 -0.0808 -0.0082 -0.0159 67  SER   A C   
472  O O   . SER   A 61  ? 0.5447 0.2849 0.1669 -0.0955 0.0032  -0.0199 67  SER   A O   
473  C CB  . SER   A 61  ? 0.5130 0.2710 0.1898 -0.0734 0.0199  -0.0374 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.4804 0.2696 0.2073 -0.0536 0.0388  -0.0372 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.4675 0.2766 0.1918 -0.0693 -0.0177 -0.0061 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.4762 0.2872 0.1947 -0.0717 -0.0168 0.0017  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.4798 0.3079 0.2259 -0.0739 -0.0469 0.0176  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.4979 0.3294 0.2451 -0.0758 -0.0496 0.0262  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.4479 0.2835 0.2035 -0.0543 0.0072  -0.0019 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.4859 0.3072 0.2278 -0.0508 0.0397  -0.0132 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.5274 0.3147 0.2156 -0.0647 0.0544  -0.0152 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.5748 0.3451 0.2548 -0.0610 0.0917  -0.0261 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.6295 0.3664 0.2742 -0.0685 0.1079  -0.0383 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.6315 0.3474 0.2394 -0.0824 0.0867  -0.0409 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.6371 0.3593 0.2847 -0.0632 0.1463  -0.0473 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.4615 0.3016 0.2369 -0.0728 -0.0675 0.0227  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.4566 0.3159 0.2752 -0.0715 -0.0910 0.0385  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.4353 0.3182 0.2917 -0.0575 -0.0786 0.0391  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.4562 0.3423 0.3257 -0.0605 -0.0896 0.0514  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.5040 0.3436 0.2973 -0.0920 -0.1198 0.0561  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.5867 0.4061 0.3532 -0.1080 -0.1396 0.0590  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.6672 0.4701 0.4156 -0.1307 -0.1738 0.0815  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.7487 0.5207 0.4477 -0.1544 -0.1941 0.0846  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.8368 0.5688 0.4598 -0.1812 -0.2031 0.0875  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.8506 0.5707 0.4412 -0.1861 -0.1924 0.0881  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.8773 0.5779 0.4521 -0.2052 -0.2223 0.0896  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.3895 0.2870 0.2614 -0.0439 -0.0561 0.0266  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.3698 0.2854 0.2687 -0.0343 -0.0444 0.0266  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.3211 0.2565 0.2515 -0.0228 -0.0324 0.0184  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.3095 0.2444 0.2350 -0.0205 -0.0263 0.0111  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.4352 0.3413 0.3042 -0.0358 -0.0264 0.0227  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.5572 0.4496 0.4019 -0.0457 -0.0324 0.0321  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.6361 0.5221 0.4597 -0.0448 -0.0085 0.0270  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.7217 0.5987 0.5275 -0.0526 -0.0102 0.0361  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.7864 0.6301 0.5341 -0.0697 -0.0119 0.0379  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.2859 0.2354 0.2444 -0.0177 -0.0286 0.0199  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.2567 0.2210 0.2354 -0.0113 -0.0171 0.0129  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.2666 0.2354 0.2381 -0.0104 -0.0044 0.0121  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.2913 0.2564 0.2555 -0.0128 -0.0034 0.0170  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2418 0.2139 0.2520 -0.0095 -0.0179 0.0136  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.2491 0.2197 0.2800 -0.0094 -0.0282 0.0171  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.2649 0.2414 0.3132 -0.0068 -0.0244 0.0116  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.2601 0.2248 0.3017 -0.0125 -0.0428 0.0279  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.2376 0.2124 0.3093 -0.0073 -0.0353 0.0190  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.2865 0.2548 0.3566 -0.0111 -0.0482 0.0299  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2380 0.2154 0.2150 -0.0077 0.0044  0.0082  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2297 0.2142 0.2098 -0.0075 0.0146  0.0111  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2211 0.2194 0.2201 -0.0093 0.0148  0.0116  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2135 0.2160 0.2191 -0.0092 0.0129  0.0086  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2458 0.2265 0.2193 -0.0047 0.0258  0.0103  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.2892 0.2497 0.2332 -0.0070 0.0308  0.0087  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3210 0.2756 0.2541 -0.0095 0.0384  0.0130  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3266 0.2707 0.2493 -0.0090 0.0287  0.0031  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.3649 0.2959 0.2623 -0.0151 0.0448  0.0112  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.3566 0.2757 0.2415 -0.0159 0.0331  0.0011  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.3922 0.3037 0.2624 -0.0195 0.0415  0.0050  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.4601 0.3418 0.2848 -0.0295 0.0487  0.0024  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2141 0.2179 0.2188 -0.0134 0.0165  0.0164  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2148 0.2279 0.2298 -0.0203 0.0145  0.0189  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2292 0.2535 0.2582 -0.0196 0.0173  0.0269  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2677 0.2929 0.3021 -0.0148 0.0253  0.0317  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2211 0.2330 0.2352 -0.0268 0.0141  0.0226  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2377 0.2462 0.2479 -0.0212 0.0183  0.0259  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2244 0.2243 0.2236 -0.0144 0.0190  0.0211  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2106 0.2417 0.2472 -0.0246 0.0122  0.0290  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2097 0.2528 0.2688 -0.0241 0.0129  0.0400  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1957 0.2475 0.2623 -0.0378 0.0012  0.0498  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2166 0.2615 0.2641 -0.0475 -0.0049 0.0436  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2405 0.2808 0.3027 -0.0154 0.0174  0.0349  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2824 0.3114 0.3368 -0.0052 0.0301  0.0290  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2422 0.2766 0.2893 -0.0177 0.0111  0.0252  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1797 0.2457 0.2767 -0.0402 -0.0016 0.0669  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1925 0.2682 0.3017 -0.0547 -0.0166 0.0814  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1875 0.2689 0.3178 -0.0465 -0.0142 0.0846  75  SER   A C   
545  O O   . SER   A 69  ? 0.2161 0.2973 0.3642 -0.0310 0.0008  0.0820  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2234 0.3139 0.3654 -0.0623 -0.0237 0.1035  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3279 0.4126 0.4518 -0.0702 -0.0260 0.1013  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1707 0.2516 0.2914 -0.0570 -0.0257 0.0862  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1698 0.2547 0.3096 -0.0492 -0.0235 0.0884  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1926 0.2880 0.3489 -0.0652 -0.0418 0.1085  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2230 0.3162 0.3583 -0.0860 -0.0573 0.1154  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1808 0.2518 0.2916 -0.0415 -0.0163 0.0671  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1695 0.2297 0.2434 -0.0544 -0.0220 0.0568  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1818 0.2313 0.2333 -0.0536 -0.0159 0.0443  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1962 0.2545 0.2592 -0.0674 -0.0307 0.0596  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2021 0.2384 0.2252 -0.0645 -0.0154 0.0339  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2125 0.2560 0.2406 -0.0793 -0.0293 0.0480  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2176 0.2497 0.2278 -0.0778 -0.0204 0.0351  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1784 0.2830 0.3723 -0.0575 -0.0404 0.1194  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1961 0.3128 0.4143 -0.0731 -0.0604 0.1438  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2136 0.3204 0.3926 -0.0873 -0.0713 0.1371  77  SER   A C   
562  O O   . SER   A 71  ? 0.2227 0.3155 0.3672 -0.0805 -0.0601 0.1137  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2095 0.3387 0.4887 -0.0593 -0.0532 0.1593  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2163 0.3348 0.4870 -0.0440 -0.0379 0.1411  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2301 0.3430 0.4143 -0.1092 -0.0941 0.1594  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2645 0.3658 0.4105 -0.1241 -0.1020 0.1540  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2655 0.3699 0.4351 -0.1065 -0.0925 0.1493  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2586 0.3753 0.4796 -0.0905 -0.0868 0.1596  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3306 0.4345 0.4699 -0.1568 -0.1314 0.1816  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4237 0.5151 0.5204 -0.1798 -0.1404 0.1808  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5087 0.5930 0.5776 -0.2195 -0.1707 0.2046  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6034 0.6698 0.6250 -0.2411 -0.1751 0.1988  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.6909 0.7374 0.6592 -0.2849 -0.2003 0.2131  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.2644 0.3558 0.3977 -0.1099 -0.0887 0.1336  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.2721 0.3651 0.4258 -0.0946 -0.0808 0.1288  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2732 0.3813 0.4762 -0.0977 -0.0946 0.1566  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2846 0.3971 0.4847 -0.1218 -0.1171 0.1790  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3095 0.3875 0.4170 -0.1058 -0.0796 0.1143  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3420 0.4063 0.4043 -0.1185 -0.0763 0.1020  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.2912 0.3638 0.3658 -0.1284 -0.0889 0.1196  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2456 0.3594 0.4938 -0.0756 -0.0814 0.1567  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2488 0.3769 0.5556 -0.0765 -0.0915 0.1849  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2345 0.3583 0.5741 -0.0535 -0.0719 0.1759  80  SER   A C   
584  O O   . SER   A 74  ? 0.2247 0.3334 0.5339 -0.0400 -0.0538 0.1479  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2896 0.4337 0.6414 -0.0811 -0.1005 0.2107  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3494 0.4924 0.7183 -0.0615 -0.0779 0.1991  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2167 0.3515 0.6155 -0.0523 -0.0779 0.2008  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2421 0.3704 0.6780 -0.0332 -0.0591 0.1957  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2600 0.3871 0.7389 -0.0149 -0.0346 0.1948  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2469 0.3906 0.7829 -0.0174 -0.0402 0.2223  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2434 0.3844 0.7323 -0.0414 -0.0765 0.2271  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.3003 0.4359 0.7607 -0.0510 -0.0885 0.2241  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.3027 0.4533 0.8190 -0.0631 -0.1109 0.2620  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3170 0.4334 0.7625 -0.0318 -0.0644 0.1948  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2659 0.3724 0.7194 0.0016  -0.0077 0.1653  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2785 0.3763 0.7572 0.0170  0.0207  0.1589  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3163 0.3898 0.8043 0.0328  0.0495  0.1418  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3142 0.3718 0.7589 0.0330  0.0491  0.1218  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3035 0.3936 0.7242 0.0161  0.0247  0.1377  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3151 0.4254 0.7289 -0.0004 -0.0005 0.1545  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3182 0.3913 0.7446 0.0307  0.0570  0.1240  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3500 0.4534 0.7117 -0.0026 0.0010  0.1363  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3313 0.3996 0.8778 0.0451  0.0760  0.1501  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3918 0.4292 0.9415 0.0582  0.1086  0.1312  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.4620 0.4689 0.9396 0.0613  0.1286  0.0968  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4798 0.4884 0.9408 0.0610  0.1341  0.0933  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3757 0.4118 1.0116 0.0702  0.1373  0.1490  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4054 0.4079 1.0508 0.0809  0.1693  0.1327  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4239 0.4273 1.0868 0.0794  0.1568  0.1393  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4421 0.4079 1.0708 0.0901  0.2124  0.1090  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4539 0.4228 1.1215 0.0879  0.1865  0.1226  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.4717 0.4003 1.1037 0.0972  0.2440  0.0924  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.4707 0.4012 1.1227 0.0964  0.2306  0.0990  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.5066 0.4858 0.9406 0.0622  0.1361  0.0736  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.5706 0.5167 0.9342 0.0614  0.1512  0.0433  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.6144 0.5211 0.9750 0.0665  0.1808  0.0268  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.6135 0.5193 0.9916 0.0667  0.1736  0.0301  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.5998 0.5511 0.8999 0.0513  0.1215  0.0317  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.5996 0.5763 0.8888 0.0460  0.1031  0.0400  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.6046 0.5684 0.9144 0.0472  0.0993  0.0390  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6554 0.5262 0.9896 0.0688  0.2147  0.0085  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.7012 0.5253 1.0248 0.0709  0.2493  -0.0100 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.7505 0.5481 1.0076 0.0607  0.2355  -0.0308 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.7634 0.5776 0.9808 0.0528  0.2018  -0.0322 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.7589 0.5477 1.0620 0.0722  0.2909  -0.0247 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.8436 0.5920 1.1779 0.0789  0.3392  -0.0333 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.9777 0.6869 1.2888 0.0785  0.3854  -0.0488 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.0531 0.7058 1.3253 0.0735  0.4222  -0.0727 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.9882 0.7204 1.3167 0.0816  0.3859  -0.0376 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.7713 0.5267 1.0207 0.0604  0.2623  -0.0458 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.8127 0.5373 1.0038 0.0493  0.2521  -0.0646 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.8652 0.5664 0.9641 0.0334  0.2383  -0.0838 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.8893 0.5866 0.9623 0.0311  0.2465  -0.0874 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.8299 0.5062 1.0298 0.0509  0.2916  -0.0782 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.8793 0.5658 0.9331 0.0217  0.2159  -0.0936 87  SER   A N   
636  C CA  . SER   A 81  ? 0.9101 0.5743 0.8838 0.0042  0.1969  -0.1075 87  SER   A CA  
637  C C   . SER   A 81  ? 0.9195 0.5618 0.8638 -0.0075 0.1798  -0.1159 87  SER   A C   
638  O O   . SER   A 81  ? 0.9066 0.5610 0.8962 0.0000  0.1782  -0.1090 87  SER   A O   
639  C CB  . SER   A 81  ? 0.9133 0.6232 0.8886 0.0048  0.1625  -0.0941 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.9145 0.6635 0.9246 0.0088  0.1326  -0.0804 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.9384 0.5498 0.8093 -0.0273 0.1641  -0.1282 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.9433 0.5376 0.7889 -0.0403 0.1425  -0.1331 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.8833 0.5323 0.7755 -0.0327 0.1059  -0.1147 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.8965 0.5398 0.7797 -0.0415 0.0860  -0.1151 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.0315 0.5820 0.7902 -0.0665 0.1286  -0.1458 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.1040 0.6869 0.8503 -0.0720 0.0914  -0.1334 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.2403 0.7846 0.9088 -0.0999 0.0700  -0.1396 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.2609 0.8299 0.9243 -0.1044 0.0414  -0.1277 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.2977 0.7853 0.9104 -0.1189 0.0813  -0.1552 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.8185 0.5173 0.7577 -0.0182 0.0987  -0.0989 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.7557 0.5031 0.7347 -0.0121 0.0705  -0.0825 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.6965 0.4711 0.7411 0.0026  0.0799  -0.0696 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.6848 0.4794 0.7552 0.0034  0.0634  -0.0608 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7351 0.5129 0.7114 -0.0106 0.0557  -0.0745 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.7580 0.5101 0.6757 -0.0243 0.0487  -0.0835 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.7788 0.5199 0.6654 -0.0390 0.0230  -0.0847 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.7725 0.5126 0.6690 -0.0240 0.0660  -0.0880 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.8105 0.5289 0.6454 -0.0543 0.0118  -0.0885 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.8079 0.5243 0.6487 -0.0387 0.0573  -0.0939 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.8349 0.5404 0.6447 -0.0545 0.0289  -0.0933 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.8766 0.5588 0.6331 -0.0717 0.0164  -0.0953 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.6600 0.4359 0.7343 0.0130  0.1054  -0.0660 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.6084 0.4115 0.7508 0.0249  0.1106  -0.0487 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.6329 0.4133 0.8086 0.0336  0.1469  -0.0501 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.6544 0.4126 0.8113 0.0343  0.1709  -0.0598 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.5422 0.3910 0.7145 0.0301  0.0962  -0.0304 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.4903 0.3633 0.6389 0.0232  0.0665  -0.0277 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.4605 0.3530 0.6237 0.0202  0.0462  -0.0192 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4835 0.3599 0.5999 0.0200  0.0610  -0.0325 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.4395 0.3519 0.5861 0.0144  0.0247  -0.0171 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.4568 0.3544 0.5598 0.0148  0.0376  -0.0292 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.4284 0.3437 0.5480 0.0124  0.0212  -0.0218 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3590 0.2907 0.4677 0.0073  0.0036  -0.0202 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.6255 0.4160 0.8604 0.0412  0.1519  -0.0367 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.6253 0.4028 0.9124 0.0522  0.1872  -0.0317 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.6096 0.4259 0.9411 0.0597  0.1845  -0.0109 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.6106 0.4611 0.9297 0.0555  0.1549  -0.0014 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.6120 0.3959 0.9537 0.0566  0.1844  -0.0185 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.6022 0.4248 0.9395 0.0505  0.1426  -0.0053 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.6054 0.4231 0.8692 0.0403  0.1257  -0.0219 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.5953 0.4060 0.9812 0.0700  0.2157  -0.0027 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5640 0.4116 0.9990 0.0758  0.2118  0.0202  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.5153 0.4103 0.9961 0.0737  0.1743  0.0496  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.5097 0.4071 1.0316 0.0756  0.1709  0.0610  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5571 0.3896 1.0565 0.0876  0.2536  0.0269  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.4868 0.4141 0.9487 0.0670  0.1453  0.0591  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.4380 0.4033 0.9270 0.0599  0.1100  0.0844  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3963 0.3931 0.8853 0.0536  0.0901  0.0998  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.4115 0.4028 0.8789 0.0560  0.1022  0.0899  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.4544 0.4159 0.8924 0.0513  0.0885  0.0719  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.4696 0.4360 0.8408 0.0433  0.0723  0.0573  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.4932 0.4372 0.8077 0.0392  0.0692  0.0337  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.4932 0.4524 0.7659 0.0308  0.0472  0.0297  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.4873 0.4443 0.7259 0.0297  0.0486  0.0197  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.4397 0.4095 0.6487 0.0228  0.0307  0.0172  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4991 0.4388 0.7339 0.0353  0.0700  0.0122  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.3546 0.3817 0.8645 0.0435  0.0595  0.1242  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.3364 0.3882 0.8333 0.0329  0.0376  0.1366  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.3068 0.3549 0.7298 0.0238  0.0223  0.1166  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.3114 0.3580 0.7198 0.0184  0.0105  0.1146  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.3364 0.4167 0.8807 0.0210  0.0103  0.1723  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.3455 0.4374 0.9749 0.0277  0.0195  0.2001  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3583 0.4668 1.0111 0.0248  0.0160  0.2159  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3541 0.4398 1.0460 0.0372  0.0331  0.2116  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3548 0.4759 1.0958 0.0313  0.0250  0.2443  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3436 0.4407 1.1255 0.0444  0.0439  0.2396  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3504 0.4658 1.1584 0.0418  0.0402  0.2563  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3585 0.4872 1.2649 0.0490  0.0509  0.2871  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2707 0.3169 0.6524 0.0226  0.0240  0.1030  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2447 0.2901 0.5675 0.0139  0.0100  0.0880  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2143 0.2823 0.5354 -0.0010 -0.0123 0.1061  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2286 0.3083 0.5715 -0.0030 -0.0139 0.1202  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2393 0.2670 0.5190 0.0198  0.0238  0.0638  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2419 0.2713 0.4725 0.0116  0.0099  0.0518  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2656 0.2744 0.4580 0.0166  0.0203  0.0300  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2919 0.2791 0.4795 0.0227  0.0342  0.0192  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2303 0.2428 0.3930 0.0121  0.0130  0.0236  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1948 0.2666 0.4890 -0.0133 -0.0285 0.1064  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1804 0.2659 0.4612 -0.0322 -0.0484 0.1215  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1935 0.2728 0.4231 -0.0368 -0.0466 0.1030  96  SER   A C   
721  O O   . SER   A 90  ? 0.1898 0.2567 0.3958 -0.0265 -0.0343 0.0807  96  SER   A O   
722  C CB  . SER   A 90  ? 0.2056 0.2946 0.4835 -0.0463 -0.0642 0.1332  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2319 0.3090 0.4759 -0.0442 -0.0584 0.1126  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1960 0.2826 0.4105 -0.0538 -0.0598 0.1142  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2070 0.2864 0.3764 -0.0610 -0.0578 0.0995  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1891 0.2637 0.3559 -0.0451 -0.0430 0.0841  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1936 0.2587 0.3291 -0.0431 -0.0361 0.0660  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2288 0.2974 0.3637 -0.0664 -0.0550 0.0846  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2759 0.3459 0.4044 -0.0855 -0.0684 0.0993  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3240 0.3877 0.4151 -0.1096 -0.0764 0.1038  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2980 0.3721 0.4495 -0.0855 -0.0746 0.1103  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3356 0.3995 0.4248 -0.1248 -0.0881 0.1180  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3250 0.3969 0.4530 -0.1102 -0.0882 0.1233  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1739 0.2543 0.3759 -0.0349 -0.0375 0.0929  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1800 0.2533 0.3780 -0.0213 -0.0219 0.0796  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1681 0.2502 0.3701 -0.0276 -0.0258 0.0897  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1767 0.2724 0.4090 -0.0363 -0.0369 0.1124  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1891 0.2568 0.4203 -0.0057 -0.0061 0.0792  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2238 0.2769 0.4434 0.0067  0.0136  0.0635  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2462 0.2834 0.4205 0.0082  0.0150  0.0415  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2474 0.2897 0.5002 0.0188  0.0337  0.0642  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1567 0.2309 0.3315 -0.0236 -0.0179 0.0746  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1553 0.2363 0.3328 -0.0290 -0.0204 0.0827  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1708 0.2456 0.3570 -0.0137 -0.0020 0.0750  99  MET   A C   
745  O O   . MET   A 93  ? 0.1832 0.2433 0.3434 -0.0053 0.0080  0.0561  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1739 0.2474 0.3075 -0.0396 -0.0256 0.0711  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2226 0.2955 0.3376 -0.0580 -0.0392 0.0761  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2772 0.3343 0.3429 -0.0698 -0.0365 0.0588  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2595 0.3075 0.3217 -0.0490 -0.0212 0.0366  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1569 0.2412 0.3767 -0.0120 0.0022  0.0897  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1665 0.2415 0.3901 0.0008  0.0235  0.0815  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1628 0.2407 0.3718 -0.0041 0.0213  0.0820  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1633 0.2541 0.3783 -0.0170 0.0048  0.0959  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1854 0.2663 0.4667 0.0094  0.0388  0.0973  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2269 0.3014 0.5305 0.0167  0.0470  0.0969  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2209 0.2998 0.5899 0.0260  0.0670  0.1134  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2607 0.3095 0.5207 0.0239  0.0607  0.0708  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1636 0.2274 0.3518 0.0041  0.0370  0.0680  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.1775 0.2420 0.3552 0.0018  0.0389  0.0682  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.1905 0.2417 0.3719 0.0125  0.0640  0.0627  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2111 0.2468 0.3889 0.0200  0.0791  0.0534  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.1958 0.2504 0.3267 -0.0026 0.0303  0.0527  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.1943 0.2488 0.3815 0.0116  0.0701  0.0684  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2163 0.2543 0.3981 0.0191  0.0959  0.0617  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.2613 0.2794 0.3845 0.0169  0.0932  0.0433  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.2728 0.2965 0.3787 0.0109  0.0785  0.0434  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2258 0.2775 0.4436 0.0181  0.1028  0.0783  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.2575 0.2887 0.4638 0.0243  0.1331  0.0702  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2016 0.2747 0.4860 0.0190  0.1015  0.1010  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.2967 0.2903 0.3914 0.0201  0.1067  0.0292  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.3241 0.2981 0.3660 0.0156  0.1006  0.0158  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.3585 0.3031 0.3682 0.0154  0.1128  0.0022  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.3793 0.3178 0.4072 0.0200  0.1273  0.0009  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.3668 0.2907 0.3281 0.0083  0.1066  -0.0066 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.3965 0.2873 0.3165 0.0029  0.1142  -0.0190 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.3896 0.2815 0.3053 0.0016  0.0951  -0.0234 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.3673 0.2761 0.2882 0.0004  0.0716  -0.0196 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.4147 0.2823 0.2836 -0.0082 0.1106  -0.0227 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.4863 0.3135 0.3029 -0.0190 0.1188  -0.0345 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.5242 0.3243 0.3301 -0.0190 0.1521  -0.0432 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.5179 0.3273 0.2948 -0.0307 0.0976  -0.0383 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.5657 0.3278 0.3154 -0.0329 0.1510  -0.0542 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.5628 0.3305 0.2939 -0.0410 0.1160  -0.0502 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.4148 0.2870 0.3223 0.0015  0.1068  -0.0316 105 SER   A N   
785  C CA  . SER   A 99  ? 0.4425 0.3125 0.3445 -0.0007 0.0904  -0.0358 105 SER   A CA  
786  C C   . SER   A 99  ? 0.5230 0.3537 0.3899 -0.0068 0.1085  -0.0482 105 SER   A C   
787  O O   . SER   A 99  ? 0.5495 0.3697 0.4321 -0.0013 0.1371  -0.0512 105 SER   A O   
788  C CB  . SER   A 99  ? 0.4341 0.3335 0.3876 0.0090  0.0864  -0.0286 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.4845 0.3827 0.4367 0.0075  0.0729  -0.0322 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.5351 0.3423 0.3567 -0.0195 0.0930  -0.0545 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.5879 0.3526 0.3683 -0.0293 0.1076  -0.0676 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.6304 0.3938 0.4032 -0.0355 0.0817  -0.0685 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.6229 0.4166 0.4205 -0.0325 0.0547  -0.0590 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.6614 0.3847 0.3773 -0.0455 0.1198  -0.0749 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.7056 0.4267 0.3856 -0.0598 0.0886  -0.0679 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.7745 0.4517 0.3873 -0.0781 0.1028  -0.0741 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.8458 0.4783 0.3987 -0.0974 0.1036  -0.0836 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.7518 0.4366 0.3682 -0.0750 0.1137  -0.0695 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.6819 0.4119 0.4283 -0.0429 0.0918  -0.0797 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.7041 0.4327 0.4442 -0.0502 0.0655  -0.0792 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.6975 0.4184 0.3998 -0.0672 0.0343  -0.0727 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.7704 0.4554 0.4141 -0.0848 0.0362  -0.0766 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.7420 0.4258 0.4483 -0.0588 0.0863  -0.0942 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.7513 0.4245 0.4710 -0.0488 0.1274  -0.1008 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.7101 0.3984 0.4296 -0.0466 0.1288  -0.0936 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.5965 0.3512 0.3365 -0.0621 0.0074  -0.0617 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.5610 0.3264 0.2998 -0.0712 -0.0252 -0.0492 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.4829 0.2930 0.2764 -0.0549 -0.0294 -0.0392 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.4642 0.2929 0.2813 -0.0561 -0.0525 -0.0282 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.4425 0.2681 0.2578 -0.0409 -0.0062 -0.0421 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.3878 0.2499 0.2464 -0.0289 -0.0086 -0.0339 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.3453 0.2353 0.2485 -0.0189 -0.0121 -0.0313 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.2995 0.2142 0.2314 -0.0136 -0.0177 -0.0251 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.3886 0.2560 0.2518 -0.0215 0.0132  -0.0349 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.4310 0.2772 0.2545 -0.0314 0.0144  -0.0345 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.4336 0.2765 0.2437 -0.0407 -0.0075 -0.0279 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.4421 0.2743 0.2506 -0.0304 0.0381  -0.0393 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.3459 0.2291 0.2522 -0.0185 -0.0092 -0.0362 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.3206 0.2287 0.2660 -0.0113 -0.0134 -0.0327 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.2984 0.2202 0.2602 -0.0139 -0.0324 -0.0260 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.3192 0.2276 0.2651 -0.0231 -0.0481 -0.0233 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.3341 0.2309 0.2801 -0.0114 -0.0089 -0.0378 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.3790 0.2679 0.3318 -0.0037 0.0189  -0.0423 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.2517 0.1980 0.2454 -0.0076 -0.0306 -0.0222 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.2426 0.2011 0.2589 -0.0088 -0.0417 -0.0165 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.2477 0.2145 0.2710 -0.0075 -0.0405 -0.0128 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.2401 0.2177 0.2894 -0.0067 -0.0427 -0.0089 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.2400 0.2000 0.2423 -0.0074 -0.0348 -0.0141 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.2213 0.1891 0.2308 -0.0061 -0.0326 -0.0106 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2109 0.1953 0.2411 -0.0025 -0.0224 -0.0117 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2112 0.2006 0.2408 -0.0011 -0.0151 -0.0137 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.1894 0.1795 0.2369 -0.0028 -0.0216 -0.0096 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1775 0.1760 0.2352 -0.0038 -0.0107 -0.0122 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1746 0.1752 0.2205 -0.0054 -0.0044 -0.0122 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2010 0.1978 0.2417 -0.0045 -0.0059 -0.0101 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2033 0.2020 0.2864 -0.0044 -0.0076 -0.0117 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2250 0.2251 0.3252 -0.0038 -0.0124 -0.0105 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2258 0.2243 0.3095 -0.0089 0.0077  -0.0166 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2446 0.2451 0.3835 -0.0032 -0.0066 -0.0075 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1605 0.1667 0.2032 -0.0096 0.0011  -0.0128 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1696 0.1784 0.2038 -0.0149 0.0050  -0.0105 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1839 0.1877 0.2170 -0.0235 0.0125  -0.0148 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1847 0.1871 0.2193 -0.0279 0.0159  -0.0175 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1731 0.1899 0.2063 -0.0175 0.0031  -0.0046 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1996 0.2208 0.2279 -0.0271 0.0027  0.0017  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2065 0.2278 0.2340 -0.0235 0.0042  0.0042  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1884 0.2196 0.2263 -0.0309 -0.0025 0.0122  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1847 0.1824 0.2144 -0.0265 0.0173  -0.0164 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2013 0.1874 0.2264 -0.0359 0.0293  -0.0228 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2246 0.2059 0.2298 -0.0473 0.0303  -0.0217 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.2330 0.2195 0.2385 -0.0440 0.0244  -0.0165 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.2546 0.2334 0.3010 -0.0289 0.0360  -0.0257 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3362 0.3183 0.4085 -0.0203 0.0338  -0.0244 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.3820 0.3589 0.4841 -0.0146 0.0372  -0.0219 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.5040 0.4752 0.6340 -0.0144 0.0514  -0.0252 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.5375 0.5154 0.6952 -0.0087 0.0447  -0.0196 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.5442 0.5313 0.6998 -0.0044 0.0230  -0.0114 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.5632 0.5362 0.7513 -0.0086 0.0607  -0.0218 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2530 0.2210 0.2388 -0.0627 0.0389  -0.0268 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2874 0.2439 0.2491 -0.0784 0.0405  -0.0270 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3361 0.2678 0.2924 -0.0842 0.0618  -0.0402 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3309 0.2594 0.3105 -0.0740 0.0735  -0.0459 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.2957 0.2516 0.2315 -0.0973 0.0313  -0.0205 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3298 0.2671 0.2425 -0.1124 0.0440  -0.0295 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.3924 0.3038 0.3192 -0.1026 0.0684  -0.0447 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4396 0.3221 0.3610 -0.1089 0.0938  -0.0591 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.4610 0.3265 0.3738 -0.1163 0.1135  -0.0694 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5067 0.3516 0.4331 -0.1144 0.1399  -0.0809 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5192 0.3779 0.4015 -0.1315 0.0972  -0.0631 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6151 0.4656 0.4504 -0.1579 0.0860  -0.0590 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.7395 0.5691 0.5349 -0.1829 0.0812  -0.0586 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.7629 0.6086 0.5518 -0.1911 0.0557  -0.0427 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.7692 0.5610 0.5399 -0.1960 0.1065  -0.0752 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.4335 0.3071 0.3285 -0.1243 0.1027  -0.0644 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.4484 0.3058 0.3298 -0.1340 0.1201  -0.0727 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.4265 0.3017 0.3554 -0.1116 0.1241  -0.0715 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.4624 0.3236 0.3928 -0.1156 0.1447  -0.0795 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.4644 0.3199 0.3016 -0.1570 0.1043  -0.0654 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.5010 0.3382 0.2920 -0.1828 0.0962  -0.0634 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.5045 0.3627 0.2933 -0.1871 0.0658  -0.0457 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.5646 0.3619 0.3099 -0.2075 0.1155  -0.0763 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.5639 0.3981 0.3101 -0.2132 0.0640  -0.0467 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.6019 0.3971 0.3166 -0.2269 0.0934  -0.0660 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.3652 0.2687 0.3308 -0.0901 0.1051  -0.0613 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3235 0.2423 0.3296 -0.0726 0.1039  -0.0582 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2754 0.2204 0.2890 -0.0624 0.0777  -0.0467 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2826 0.2370 0.2844 -0.0624 0.0623  -0.0401 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2509 0.2056 0.2848 -0.0546 0.0747  -0.0443 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2380 0.2124 0.2786 -0.0454 0.0534  -0.0353 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2317 0.2102 0.2457 -0.0563 0.0442  -0.0306 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2551 0.2256 0.2533 -0.0689 0.0510  -0.0328 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2356 0.2163 0.3064 -0.0355 0.0524  -0.0339 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2158 0.2103 0.2862 -0.0292 0.0335  -0.0271 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2363 0.2164 0.3419 -0.0252 0.0549  -0.0325 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2277 0.2184 0.2400 -0.0519 0.0290  -0.0226 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2278 0.2257 0.2276 -0.0609 0.0181  -0.0135 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2089 0.2189 0.2265 -0.0508 0.0094  -0.0082 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2174 0.2307 0.2317 -0.0584 0.0042  -0.0019 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2412 0.2451 0.2378 -0.0617 0.0099  -0.0060 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2543 0.2700 0.2540 -0.0677 -0.0034 0.0083  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2586 0.2481 0.2335 -0.0750 0.0171  -0.0108 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1855 0.1994 0.2193 -0.0356 0.0072  -0.0100 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1966 0.2165 0.2426 -0.0275 0.0007  -0.0068 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1680 0.1849 0.2205 -0.0157 -0.0015 -0.0102 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1765 0.1890 0.2287 -0.0135 0.0002  -0.0134 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1635 0.1800 0.2202 -0.0100 -0.0055 -0.0090 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1781 0.1857 0.2309 -0.0037 -0.0087 -0.0124 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1851 0.1879 0.2322 0.0003  -0.0056 -0.0113 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1762 0.1841 0.2336 0.0006  -0.0029 -0.0070 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1879 0.1911 0.2478 -0.0032 -0.0147 -0.0146 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2017 0.2084 0.2691 -0.0042 -0.0145 -0.0132 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2182 0.2233 0.2915 -0.0051 -0.0149 -0.0150 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2397 0.2400 0.3140 -0.0041 -0.0222 -0.0151 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.1829 0.1741 0.2149 0.0024  -0.0044 -0.0141 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.1930 0.1737 0.2175 0.0055  0.0048  -0.0152 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2055 0.1775 0.2328 0.0066  0.0061  -0.0181 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2141 0.1787 0.2340 0.0037  -0.0030 -0.0217 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2231 0.1858 0.2207 0.0039  0.0061  -0.0194 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.2481 0.1928 0.2335 0.0056  0.0216  -0.0234 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2382 0.2090 0.2352 0.0033  0.0057  -0.0157 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2059 0.1795 0.2493 0.0105  0.0170  -0.0147 125 SER   A N   
922  C CA  . SER   A 119 ? 0.2312 0.1958 0.2821 0.0120  0.0205  -0.0168 125 SER   A CA  
923  C C   . SER   A 119 ? 0.2811 0.2277 0.3335 0.0164  0.0404  -0.0197 125 SER   A C   
924  O O   . SER   A 119 ? 0.3114 0.2371 0.3549 0.0161  0.0469  -0.0270 125 SER   A O   
925  C CB  . SER   A 119 ? 0.2335 0.2186 0.3134 0.0115  0.0141  -0.0071 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.2451 0.2233 0.3383 0.0135  0.0174  -0.0070 125 SER   A OG  
927  N N   . THR   A 120 ? 0.2761 0.2280 0.3400 0.0198  0.0520  -0.0144 126 THR   A N   
928  C CA  . THR   A 120 ? 0.2963 0.2300 0.3683 0.0247  0.0770  -0.0167 126 THR   A CA  
929  C C   . THR   A 120 ? 0.3311 0.2564 0.3853 0.0243  0.0889  -0.0192 126 THR   A C   
930  O O   . THR   A 120 ? 0.3100 0.2503 0.3570 0.0217  0.0764  -0.0151 126 THR   A O   
931  C CB  . THR   A 120 ? 0.2998 0.2521 0.4275 0.0309  0.0835  -0.0016 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3070 0.2852 0.4584 0.0305  0.0769  0.0127  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.2908 0.2535 0.4365 0.0297  0.0695  0.0035  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.3675 0.2674 0.4167 0.0267  0.1162  -0.0255 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.4179 0.3081 0.4501 0.0255  0.1308  -0.0273 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.4650 0.3351 0.5153 0.0309  0.1673  -0.0292 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.4690 0.3441 0.5647 0.0382  0.1790  -0.0229 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.5122 0.3599 0.5308 0.0270  0.1858  -0.0364 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.5379 0.3614 0.5710 0.0313  0.2271  -0.0399 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.5238 0.3751 0.6192 0.0407  0.2399  -0.0221 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.4891 0.3811 0.6280 0.0446  0.2159  -0.0044 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.5321 0.3588 0.6346 0.0433  0.2802  -0.0262 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.5219 0.3728 0.6911 0.0522  0.2966  -0.0075 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.4830 0.3686 0.6558 0.0495  0.2683  0.0060  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.4646 0.3827 0.7021 0.0553  0.2654  0.0274  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.5305 0.4065 0.7869 0.0636  0.3001  0.0112  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.6229 0.4632 0.8957 0.0692  0.3418  0.0009  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.6759 0.4741 0.9139 0.0664  0.3810  -0.0160 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.6228 0.4765 0.9494 0.0761  0.3366  0.0114  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.4733 0.3512 0.5802 0.0396  0.2467  -0.0046 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.4224 0.3283 0.5298 0.0366  0.2219  0.0062  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.3623 0.3064 0.4995 0.0370  0.1850  0.0196  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.3568 0.3251 0.5062 0.0344  0.1675  0.0309  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.3206 0.2668 0.4642 0.0384  0.1740  0.0174  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.2779 0.2548 0.4418 0.0361  0.1418  0.0286  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.2849 0.2511 0.3997 0.0309  0.1225  0.0140  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.3281 0.2660 0.4095 0.0301  0.1331  -0.0007 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.2705 0.2630 0.4944 0.0413  0.1438  0.0434  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.2889 0.2963 0.5785 0.0467  0.1607  0.0635  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.2988 0.3089 0.6471 0.0538  0.1731  0.0746  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.2746 0.3141 0.5860 0.0394  0.1349  0.0830  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.2389 0.2266 0.3550 0.0264  0.0957  0.0197  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.2279 0.2099 0.3127 0.0225  0.0786  0.0094  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2028 0.2073 0.3165 0.0205  0.0620  0.0199  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.1958 0.2206 0.3326 0.0167  0.0533  0.0335  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.2431 0.2219 0.2912 0.0169  0.0657  0.0031  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.2500 0.2490 0.3124 0.0139  0.0572  0.0133  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.2490 0.2257 0.2789 0.0134  0.0484  -0.0037 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2047 0.2034 0.3144 0.0208  0.0574  0.0145  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.1934 0.2103 0.3255 0.0171  0.0426  0.0245  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.1982 0.2139 0.3029 0.0118  0.0276  0.0158  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2169 0.2163 0.2969 0.0133  0.0288  0.0035  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1637 0.1944 0.2722 0.0039  0.0145  0.0229  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1665 0.1955 0.2542 -0.0014 0.0051  0.0150  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1683 0.2049 0.2671 -0.0074 -0.0027 0.0214  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1664 0.2144 0.2810 -0.0144 -0.0083 0.0352  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1593 0.1930 0.2344 -0.0087 0.0007  0.0155  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1742 0.2031 0.2410 -0.0046 0.0065  0.0127  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1692 0.1865 0.2178 -0.0012 0.0076  0.0027  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1838 0.2205 0.2631 -0.0060 0.0091  0.0225  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.1829 0.1947 0.2215 0.0008  0.0119  0.0016  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1892 0.2212 0.2602 -0.0031 0.0152  0.0204  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.1928 0.2116 0.2413 0.0003  0.0170  0.0094  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1667 0.1969 0.2577 -0.0065 -0.0045 0.0134  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1594 0.1949 0.2557 -0.0135 -0.0109 0.0180  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1702 0.2079 0.2499 -0.0251 -0.0139 0.0172  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1835 0.2148 0.2511 -0.0240 -0.0101 0.0070  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1641 0.1909 0.2592 -0.0086 -0.0107 0.0095  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1733 0.2175 0.2525 -0.0381 -0.0203 0.0287  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1888 0.2281 0.2436 -0.0531 -0.0201 0.0265  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2064 0.2382 0.2517 -0.0570 -0.0150 0.0183  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2090 0.2439 0.2659 -0.0553 -0.0185 0.0221  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2192 0.2636 0.2701 -0.0710 -0.0317 0.0434  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.2972 0.3296 0.3121 -0.0915 -0.0307 0.0404  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.2814 0.3065 0.2834 -0.0904 -0.0228 0.0306  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.3772 0.4043 0.3743 -0.1102 -0.0367 0.0474  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2080 0.2291 0.2347 -0.0634 -0.0048 0.0080  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2159 0.2285 0.2368 -0.0688 0.0047  0.0011  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.2548 0.2519 0.2423 -0.0904 0.0138  -0.0016 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.2733 0.2590 0.2522 -0.0977 0.0272  -0.0084 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2150 0.2246 0.2533 -0.0552 0.0144  -0.0099 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2087 0.2267 0.2693 -0.0391 0.0048  -0.0082 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2300 0.2324 0.2631 -0.0541 0.0231  -0.0167 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.2590 0.2532 0.2263 -0.1027 0.0074  0.0041  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.2877 0.2610 0.2149 -0.1263 0.0160  0.0000  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.3522 0.3158 0.2521 -0.1488 0.0130  0.0067  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.4068 0.3453 0.2670 -0.1698 0.0274  -0.0014 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3028 0.2757 0.2157 -0.1357 0.0057  0.0068  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.2960 0.2720 0.2261 -0.1183 0.0127  -0.0016 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3012 0.2783 0.2194 -0.1285 0.0011  0.0072  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3102 0.3091 0.2527 -0.1241 -0.0190 0.0259  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3199 0.3265 0.2678 -0.1288 -0.0310 0.0380  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3252 0.3179 0.2468 -0.1425 -0.0286 0.0340  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3042 0.3313 0.2864 -0.1207 -0.0442 0.0549  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.3348 0.3147 0.2534 -0.1463 -0.0040 0.0213  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.3752 0.3462 0.2680 -0.1694 -0.0099 0.0307  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.3875 0.3516 0.2842 -0.1644 0.0080  0.0196  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.4204 0.3725 0.2902 -0.1848 0.0089  0.0241  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.3973 0.3889 0.3149 -0.1700 -0.0365 0.0546  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4111 0.4226 0.3786 -0.1416 -0.0380 0.0550  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.3759 0.3923 0.3637 -0.1195 -0.0284 0.0425  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.3997 0.4196 0.3839 -0.1432 -0.0490 0.0681  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.3533 0.3244 0.2834 -0.1397 0.0210  0.0071  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.3497 0.3181 0.2942 -0.1339 0.0354  -0.0001 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.3796 0.3229 0.3004 -0.1454 0.0643  -0.0152 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.3691 0.3108 0.3151 -0.1306 0.0812  -0.0265 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3110 0.2969 0.3027 -0.1055 0.0323  -0.0033 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.2996 0.3042 0.3129 -0.0938 0.0097  0.0086  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.2765 0.2902 0.3239 -0.0704 0.0083  0.0030  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3170 0.3262 0.3317 -0.1025 -0.0012 0.0211  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.4076 0.3283 0.2784 -0.1744 0.0706  -0.0143 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.4586 0.3471 0.2965 -0.1901 0.1028  -0.0305 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.4800 0.3638 0.3470 -0.1797 0.1304  -0.0410 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.5151 0.3791 0.3843 -0.1793 0.1616  -0.0558 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.5003 0.3589 0.2671 -0.2289 0.1037  -0.0276 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.5488 0.4106 0.2864 -0.2455 0.0731  -0.0126 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.6238 0.4473 0.2841 -0.2883 0.0782  -0.0124 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.5414 0.4110 0.2963 -0.2306 0.0700  -0.0174 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.4531 0.3549 0.3477 -0.1709 0.1200  -0.0323 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.4509 0.3520 0.3796 -0.1613 0.1423  -0.0384 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.4374 0.3521 0.4249 -0.1341 0.1497  -0.0440 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.4562 0.3667 0.4766 -0.1279 0.1732  -0.0492 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.4280 0.3452 0.3709 -0.1599 0.1255  -0.0261 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.3958 0.3421 0.3678 -0.1419 0.0910  -0.0139 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.3997 0.3544 0.3533 -0.1489 0.0644  -0.0010 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.3579 0.3253 0.3827 -0.1153 0.0816  -0.0135 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.3724 0.3505 0.3652 -0.1271 0.0439  0.0055  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.3496 0.3338 0.3805 -0.1080 0.0533  -0.0027 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.3515 0.3235 0.4203 -0.0994 0.0939  -0.0192 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.3377 0.3378 0.4060 -0.0869 0.0395  -0.0011 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3404 0.3310 0.4472 -0.0801 0.0745  -0.0144 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3269 0.3290 0.4283 -0.0748 0.0489  -0.0071 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.4170 0.3473 0.4201 -0.1190 0.1300  -0.0413 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.4051 0.3462 0.4596 -0.0969 0.1337  -0.0440 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.4697 0.3888 0.5325 -0.1002 0.1694  -0.0560 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.4529 0.3794 0.5698 -0.0846 0.1783  -0.0554 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.3737 0.3290 0.4307 -0.0853 0.1095  -0.0399 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.3373 0.3137 0.4031 -0.0758 0.0795  -0.0293 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.3343 0.3186 0.3950 -0.0680 0.0628  -0.0269 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.3179 0.3072 0.4293 -0.0606 0.0736  -0.0257 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.5415 0.4320 0.5518 -0.1219 0.1892  -0.0657 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.6131 0.4738 0.6193 -0.1292 0.2282  -0.0801 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.6703 0.5081 0.6788 -0.1397 0.2665  -0.0883 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.7000 0.5077 0.7037 -0.1471 0.3047  -0.1018 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.6727 0.5063 0.6087 -0.1533 0.2318  -0.0877 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.7319 0.5782 0.6641 -0.1460 0.2066  -0.0835 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.7270 0.5997 0.7102 -0.1215 0.1908  -0.0770 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.7937 0.6222 0.6701 -0.1667 0.2020  -0.0858 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.6882 0.5347 0.6966 -0.1436 0.2602  -0.0814 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.7282 0.5516 0.7359 -0.1554 0.2986  -0.0888 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.7169 0.5679 0.7846 -0.1390 0.2897  -0.0772 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.7349 0.5722 0.8110 -0.1467 0.3191  -0.0804 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.8112 0.6049 0.7326 -0.1893 0.3041  -0.0930 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 0.8837 0.7013 0.7845 -0.1936 0.2609  -0.0766 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.0112 0.8063 0.8275 -0.2262 0.2484  -0.0746 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.0466 0.8369 0.8305 -0.2446 0.2406  -0.0664 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.0515 0.8334 0.8345 -0.2350 0.2447  -0.0794 145 GLU   A OE2 
1078 N N1  . A1BR5 B .   ? 0.6652 0.4873 0.6784 0.0184  0.1254  -0.0570 201 A1BR5 A N1  
1079 C C4  . A1BR5 B .   ? 0.6908 0.4775 0.6538 0.0066  0.1205  -0.0718 201 A1BR5 A C4  
1080 C C5  . A1BR5 B .   ? 0.6791 0.5042 0.6912 0.0206  0.1378  -0.0547 201 A1BR5 A C5  
1081 C C6  . A1BR5 B .   ? 0.7494 0.5354 0.7013 0.0106  0.1531  -0.0692 201 A1BR5 A C6  
1082 C C7  . A1BR5 B .   ? 0.8324 0.5405 0.7484 0.0042  0.2070  -0.0941 201 A1BR5 A C7  
1083 C C8  . A1BR5 B .   ? 0.8610 0.5491 0.7635 0.0039  0.2392  -0.0986 201 A1BR5 A C8  
1084 C C10 . A1BR5 B .   ? 0.9296 0.5464 0.7330 -0.0164 0.2815  -0.1205 201 A1BR5 A C10 
1085 C C13 . A1BR5 B .   ? 0.7614 0.5619 0.6836 0.0031  0.1241  -0.0662 201 A1BR5 A C13 
1086 C C15 . A1BR5 B .   ? 0.7550 0.5964 0.6745 -0.0023 0.0698  -0.0550 201 A1BR5 A C15 
1087 C C17 . A1BR5 B .   ? 0.7588 0.5874 0.6657 0.0000  0.1026  -0.0558 201 A1BR5 A C17 
1088 O O1  . A1BR5 B .   ? 0.6332 0.4910 0.6881 0.0282  0.1351  -0.0401 201 A1BR5 A O1  
1089 C C3  . A1BR5 B .   ? 0.6747 0.4820 0.6329 0.0014  0.0854  -0.0669 201 A1BR5 A C3  
1090 C C2  . A1BR5 B .   ? 0.6332 0.4771 0.6470 0.0108  0.0755  -0.0534 201 A1BR5 A C2  
1091 C C19 . A1BR5 B .   ? 0.6195 0.4755 0.6872 0.0260  0.1133  -0.0423 201 A1BR5 A C19 
1092 C C1  . A1BR5 B .   ? 0.6046 0.4797 0.6605 0.0202  0.0813  -0.0397 201 A1BR5 A C1  
1093 C C   . A1BR5 B .   ? 0.5576 0.4642 0.6609 0.0247  0.0694  -0.0246 201 A1BR5 A C   
1094 O O   . A1BR5 B .   ? 0.5454 0.4489 0.6805 0.0292  0.0793  -0.0201 201 A1BR5 A O   
1095 N N   . A1BR5 B .   ? 0.5137 0.4480 0.6206 0.0220  0.0493  -0.0164 201 A1BR5 A N   
1096 C C18 . A1BR5 B .   ? 0.7651 0.5700 0.6769 0.0026  0.1287  -0.0632 201 A1BR5 A C18 
1097 C C16 . A1BR5 B .   ? 0.7514 0.5978 0.6639 -0.0020 0.0744  -0.0519 201 A1BR5 A C16 
1098 C C14 . A1BR5 B .   ? 0.7608 0.5793 0.6834 -0.0001 0.0930  -0.0622 201 A1BR5 A C14 
1099 O O2  . A1BR5 B .   ? 0.8100 0.5469 0.7113 -0.0007 0.1667  -0.0865 201 A1BR5 A O2  
1100 C C12 . A1BR5 B .   ? 0.8772 0.5272 0.7944 0.0081  0.2883  -0.1089 201 A1BR5 A C12 
1101 C C11 . A1BR5 B .   ? 0.9136 0.5230 0.7760 -0.0024 0.3186  -0.1217 201 A1BR5 A C11 
1102 C C9  . A1BR5 B .   ? 0.9108 0.5609 0.7270 -0.0158 0.2358  -0.1119 201 A1BR5 A C9  
# 
