data_7HY1
# 
_entry.id   7HY1 
# 
_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   7HY1         pdb_00007hy1 10.2210/pdb7hy1/pdb 
WWPDB D_1001408073 ?            ?                   
# 
_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                        7HY1 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                  15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2,3-dihydro-1-benzofuran-7-yl)methyl]-6-oxopiperidine-3-carboxamide' 274.315   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                     65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                           78.133    2   ?         ? ? ? 
5 water       nat water                                                                          18.015    213 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-1-[(2,3-dihydro-1-benzofuran-7-yl)methyl]-6-oxopiperidine-3-carboxamide' A1BSG 
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 
A1BSG non-polymer         . '(3S)-1-[(2,3-dihydro-1-benzofuran-7-yl)methyl]-6-oxopiperidine-3-carboxamide' ? 'C15 H18 N2 O3'  
274.315 
ALA   'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                           ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                          ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                     ? 'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                  ? 'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                                                                        ? 'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                                                                         ? 'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                                                                      ? 'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                     ? 'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                       ? 'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                                                                         ? 'C5 H11 N O2'    
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                     ? 'Zn 2'           
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1BSG 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BSG 
_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 A1BSG 1   201 201 A1BSG LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 0   DMS   DMS A . 
E 4 DMS   1   204 4   DMS   DMS A . 
F 5 HOH   1   301 137 HOH   HOH A . 
F 5 HOH   2   302 229 HOH   HOH A . 
F 5 HOH   3   303 75  HOH   HOH A . 
F 5 HOH   4   304 30  HOH   HOH A . 
F 5 HOH   5   305 152 HOH   HOH A . 
F 5 HOH   6   306 249 HOH   HOH A . 
F 5 HOH   7   307 41  HOH   HOH A . 
F 5 HOH   8   308 72  HOH   HOH A . 
F 5 HOH   9   309 279 HOH   HOH A . 
F 5 HOH   10  310 13  HOH   HOH A . 
F 5 HOH   11  311 119 HOH   HOH A . 
F 5 HOH   12  312 34  HOH   HOH A . 
F 5 HOH   13  313 68  HOH   HOH A . 
F 5 HOH   14  314 37  HOH   HOH A . 
F 5 HOH   15  315 136 HOH   HOH A . 
F 5 HOH   16  316 59  HOH   HOH A . 
F 5 HOH   17  317 278 HOH   HOH A . 
F 5 HOH   18  318 219 HOH   HOH A . 
F 5 HOH   19  319 167 HOH   HOH A . 
F 5 HOH   20  320 67  HOH   HOH A . 
F 5 HOH   21  321 108 HOH   HOH A . 
F 5 HOH   22  322 60  HOH   HOH A . 
F 5 HOH   23  323 262 HOH   HOH A . 
F 5 HOH   24  324 169 HOH   HOH A . 
F 5 HOH   25  325 55  HOH   HOH A . 
F 5 HOH   26  326 252 HOH   HOH A . 
F 5 HOH   27  327 4   HOH   HOH A . 
F 5 HOH   28  328 261 HOH   HOH A . 
F 5 HOH   29  329 42  HOH   HOH A . 
F 5 HOH   30  330 104 HOH   HOH A . 
F 5 HOH   31  331 254 HOH   HOH A . 
F 5 HOH   32  332 133 HOH   HOH A . 
F 5 HOH   33  333 181 HOH   HOH A . 
F 5 HOH   34  334 77  HOH   HOH A . 
F 5 HOH   35  335 147 HOH   HOH A . 
F 5 HOH   36  336 273 HOH   HOH A . 
F 5 HOH   37  337 267 HOH   HOH A . 
F 5 HOH   38  338 25  HOH   HOH A . 
F 5 HOH   39  339 251 HOH   HOH A . 
F 5 HOH   40  340 26  HOH   HOH A . 
F 5 HOH   41  341 272 HOH   HOH A . 
F 5 HOH   42  342 57  HOH   HOH A . 
F 5 HOH   43  343 135 HOH   HOH A . 
F 5 HOH   44  344 210 HOH   HOH A . 
F 5 HOH   45  345 93  HOH   HOH A . 
F 5 HOH   46  346 146 HOH   HOH A . 
F 5 HOH   47  347 24  HOH   HOH A . 
F 5 HOH   48  348 43  HOH   HOH A . 
F 5 HOH   49  349 121 HOH   HOH A . 
F 5 HOH   50  350 7   HOH   HOH A . 
F 5 HOH   51  351 33  HOH   HOH A . 
F 5 HOH   52  352 2   HOH   HOH A . 
F 5 HOH   53  353 15  HOH   HOH A . 
F 5 HOH   54  354 124 HOH   HOH A . 
F 5 HOH   55  355 19  HOH   HOH A . 
F 5 HOH   56  356 216 HOH   HOH A . 
F 5 HOH   57  357 215 HOH   HOH A . 
F 5 HOH   58  358 16  HOH   HOH A . 
F 5 HOH   59  359 280 HOH   HOH A . 
F 5 HOH   60  360 110 HOH   HOH A . 
F 5 HOH   61  361 253 HOH   HOH A . 
F 5 HOH   62  362 170 HOH   HOH A . 
F 5 HOH   63  363 205 HOH   HOH A . 
F 5 HOH   64  364 264 HOH   HOH A . 
F 5 HOH   65  365 211 HOH   HOH A . 
F 5 HOH   66  366 212 HOH   HOH A . 
F 5 HOH   67  367 28  HOH   HOH A . 
F 5 HOH   68  368 9   HOH   HOH A . 
F 5 HOH   69  369 271 HOH   HOH A . 
F 5 HOH   70  370 52  HOH   HOH A . 
F 5 HOH   71  371 144 HOH   HOH A . 
F 5 HOH   72  372 191 HOH   HOH A . 
F 5 HOH   73  373 63  HOH   HOH A . 
F 5 HOH   74  374 270 HOH   HOH A . 
F 5 HOH   75  375 49  HOH   HOH A . 
F 5 HOH   76  376 84  HOH   HOH A . 
F 5 HOH   77  377 263 HOH   HOH A . 
F 5 HOH   78  378 79  HOH   HOH A . 
F 5 HOH   79  379 90  HOH   HOH A . 
F 5 HOH   80  380 50  HOH   HOH A . 
F 5 HOH   81  381 182 HOH   HOH A . 
F 5 HOH   82  382 85  HOH   HOH A . 
F 5 HOH   83  383 36  HOH   HOH A . 
F 5 HOH   84  384 156 HOH   HOH A . 
F 5 HOH   85  385 161 HOH   HOH A . 
F 5 HOH   86  386 47  HOH   HOH A . 
F 5 HOH   87  387 265 HOH   HOH A . 
F 5 HOH   88  388 174 HOH   HOH A . 
F 5 HOH   89  389 126 HOH   HOH A . 
F 5 HOH   90  390 12  HOH   HOH A . 
F 5 HOH   91  391 277 HOH   HOH A . 
F 5 HOH   92  392 35  HOH   HOH A . 
F 5 HOH   93  393 255 HOH   HOH A . 
F 5 HOH   94  394 29  HOH   HOH A . 
F 5 HOH   95  395 103 HOH   HOH A . 
F 5 HOH   96  396 20  HOH   HOH A . 
F 5 HOH   97  397 82  HOH   HOH A . 
F 5 HOH   98  398 220 HOH   HOH A . 
F 5 HOH   99  399 74  HOH   HOH A . 
F 5 HOH   100 400 106 HOH   HOH A . 
F 5 HOH   101 401 40  HOH   HOH A . 
F 5 HOH   102 402 111 HOH   HOH A . 
F 5 HOH   103 403 257 HOH   HOH A . 
F 5 HOH   104 404 70  HOH   HOH A . 
F 5 HOH   105 405 214 HOH   HOH A . 
F 5 HOH   106 406 132 HOH   HOH A . 
F 5 HOH   107 407 88  HOH   HOH A . 
F 5 HOH   108 408 11  HOH   HOH A . 
F 5 HOH   109 409 269 HOH   HOH A . 
F 5 HOH   110 410 105 HOH   HOH A . 
F 5 HOH   111 411 203 HOH   HOH A . 
F 5 HOH   112 412 231 HOH   HOH A . 
F 5 HOH   113 413 177 HOH   HOH A . 
F 5 HOH   114 414 62  HOH   HOH A . 
F 5 HOH   115 415 168 HOH   HOH A . 
F 5 HOH   116 416 27  HOH   HOH A . 
F 5 HOH   117 417 39  HOH   HOH A . 
F 5 HOH   118 418 5   HOH   HOH A . 
F 5 HOH   119 419 51  HOH   HOH A . 
F 5 HOH   120 420 281 HOH   HOH A . 
F 5 HOH   121 421 48  HOH   HOH A . 
F 5 HOH   122 422 286 HOH   HOH A . 
F 5 HOH   123 423 95  HOH   HOH A . 
F 5 HOH   124 424 176 HOH   HOH A . 
F 5 HOH   125 425 8   HOH   HOH A . 
F 5 HOH   126 426 96  HOH   HOH A . 
F 5 HOH   127 427 38  HOH   HOH A . 
F 5 HOH   128 428 192 HOH   HOH A . 
F 5 HOH   129 429 61  HOH   HOH A . 
F 5 HOH   130 430 248 HOH   HOH A . 
F 5 HOH   131 431 94  HOH   HOH A . 
F 5 HOH   132 432 100 HOH   HOH A . 
F 5 HOH   133 433 259 HOH   HOH A . 
F 5 HOH   134 434 256 HOH   HOH A . 
F 5 HOH   135 435 10  HOH   HOH A . 
F 5 HOH   136 436 80  HOH   HOH A . 
F 5 HOH   137 437 89  HOH   HOH A . 
F 5 HOH   138 438 123 HOH   HOH A . 
F 5 HOH   139 439 234 HOH   HOH A . 
F 5 HOH   140 440 282 HOH   HOH A . 
F 5 HOH   141 441 283 HOH   HOH A . 
F 5 HOH   142 442 23  HOH   HOH A . 
F 5 HOH   143 443 98  HOH   HOH A . 
F 5 HOH   144 444 186 HOH   HOH A . 
F 5 HOH   145 445 122 HOH   HOH A . 
F 5 HOH   146 446 276 HOH   HOH A . 
F 5 HOH   147 447 258 HOH   HOH A . 
F 5 HOH   148 448 159 HOH   HOH A . 
F 5 HOH   149 449 138 HOH   HOH A . 
F 5 HOH   150 450 128 HOH   HOH A . 
F 5 HOH   151 451 69  HOH   HOH A . 
F 5 HOH   152 452 224 HOH   HOH A . 
F 5 HOH   153 453 76  HOH   HOH A . 
F 5 HOH   154 454 288 HOH   HOH A . 
F 5 HOH   155 455 97  HOH   HOH A . 
F 5 HOH   156 456 155 HOH   HOH A . 
F 5 HOH   157 457 233 HOH   HOH A . 
F 5 HOH   158 458 175 HOH   HOH A . 
F 5 HOH   159 459 158 HOH   HOH A . 
F 5 HOH   160 460 246 HOH   HOH A . 
F 5 HOH   161 461 151 HOH   HOH A . 
F 5 HOH   162 462 201 HOH   HOH A . 
F 5 HOH   163 463 289 HOH   HOH A . 
F 5 HOH   164 464 101 HOH   HOH A . 
F 5 HOH   165 465 239 HOH   HOH A . 
F 5 HOH   166 466 58  HOH   HOH A . 
F 5 HOH   167 467 91  HOH   HOH A . 
F 5 HOH   168 468 112 HOH   HOH A . 
F 5 HOH   169 469 207 HOH   HOH A . 
F 5 HOH   170 470 266 HOH   HOH A . 
F 5 HOH   171 471 71  HOH   HOH A . 
F 5 HOH   172 472 171 HOH   HOH A . 
F 5 HOH   173 473 240 HOH   HOH A . 
F 5 HOH   174 474 65  HOH   HOH A . 
F 5 HOH   175 475 213 HOH   HOH A . 
F 5 HOH   176 476 134 HOH   HOH A . 
F 5 HOH   177 477 189 HOH   HOH A . 
F 5 HOH   178 478 99  HOH   HOH A . 
F 5 HOH   179 479 274 HOH   HOH A . 
F 5 HOH   180 480 232 HOH   HOH A . 
F 5 HOH   181 481 268 HOH   HOH A . 
F 5 HOH   182 482 221 HOH   HOH A . 
F 5 HOH   183 483 78  HOH   HOH A . 
F 5 HOH   184 484 127 HOH   HOH A . 
F 5 HOH   185 485 247 HOH   HOH A . 
F 5 HOH   186 486 86  HOH   HOH A . 
F 5 HOH   187 487 275 HOH   HOH A . 
F 5 HOH   188 488 223 HOH   HOH A . 
F 5 HOH   189 489 73  HOH   HOH A . 
F 5 HOH   190 490 290 HOH   HOH A . 
F 5 HOH   191 491 56  HOH   HOH A . 
F 5 HOH   192 492 46  HOH   HOH A . 
F 5 HOH   193 493 287 HOH   HOH A . 
F 5 HOH   194 494 209 HOH   HOH A . 
F 5 HOH   195 495 129 HOH   HOH A . 
F 5 HOH   196 496 202 HOH   HOH A . 
F 5 HOH   197 497 118 HOH   HOH A . 
F 5 HOH   198 498 243 HOH   HOH A . 
F 5 HOH   199 499 238 HOH   HOH A . 
F 5 HOH   200 500 153 HOH   HOH A . 
F 5 HOH   201 501 92  HOH   HOH A . 
F 5 HOH   202 502 208 HOH   HOH A . 
F 5 HOH   203 503 165 HOH   HOH A . 
F 5 HOH   204 504 206 HOH   HOH A . 
F 5 HOH   205 505 284 HOH   HOH A . 
F 5 HOH   206 506 83  HOH   HOH A . 
F 5 HOH   207 507 285 HOH   HOH A . 
F 5 HOH   208 508 114 HOH   HOH A . 
F 5 HOH   209 509 222 HOH   HOH A . 
F 5 HOH   210 510 242 HOH   HOH A . 
F 5 HOH   211 511 241 HOH   HOH A . 
F 5 HOH   212 512 225 HOH   HOH A . 
F 5 HOH   213 513 244 HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7HY1 
_cell.length_a           88.933 
_cell.length_b           57.936 
_cell.length_c           32.747 
_cell.angle_alpha        90.00 
_cell.angle_beta         91.20 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HY1 
_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          7HY1 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.65 
_exptl_crystal.density_percent_sol   53.65 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-12-02 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92203 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92203 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HY1 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             44.46 
_reflns.d_resolution_high            1.44 
_reflns.number_obs                   30126 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.078 
_reflns.pdbx_netI_over_sigmaI        9.7 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.086 
_reflns.pdbx_Rpim_I_all              0.035 
_reflns.pdbx_CC_half                 0.997 
_reflns.pdbx_number_measured_all     172290 
_reflns.pdbx_chi_squared             0.82 
_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                  1.44 
_reflns_shell.d_res_low                   1.52 
_reflns_shell.number_measured_all         18897 
_reflns_shell.number_unique_obs           4371 
_reflns_shell.Rmerge_I_obs                1.303 
_reflns_shell.pdbx_chi_squared            0.66 
_reflns_shell.pdbx_redundancy             4.3 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.2 
_reflns_shell.pdbx_Rrim_I_all             1.488 
_reflns_shell.pdbx_Rpim_I_all             0.703 
_reflns_shell.pdbx_CC_half                0.438 
_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                                 7HY1 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     29973 
_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                             18.21 
_refine.ls_d_res_high                            1.440 
_refine.ls_percent_reflns_obs                    99.5 
_refine.ls_R_factor_obs                          0.1852 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1834 
_refine.ls_R_factor_R_free                       0.2194 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.080 
_refine.ls_number_reflns_R_free                  1524 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.951 
_refine.B_iso_mean                               26.76 
_refine.aniso_B[1][1]                            -3.76410 
_refine.aniso_B[2][2]                            0.40890 
_refine.aniso_B[3][3]                            3.35530 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.43590 
_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             0.062 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.067 
_refine.pdbx_overall_SU_R_Blow_DPI               0.067 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.071 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HY1 
_refine_analyze.Luzzati_coordinate_error_obs    0.18 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         29 
_refine_hist.number_atoms_solvent             213 
_refine_hist.number_atoms_total               1325 
_refine_hist.d_res_high                       1.440 
_refine_hist.d_res_low                        18.21 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  1157 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 2.00  1577 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  390  '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  211  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1157 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.31  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           16.05 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  141  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1043 '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                       1.44 
_refine_ls_shell.d_res_low                        1.45 
_refine_ls_shell.number_reflns_R_work             564 
_refine_ls_shell.R_factor_R_work                  0.3130 
_refine_ls_shell.percent_reflns_obs               93.79 
_refine_ls_shell.R_factor_R_free                  0.2929 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            6.00 
_refine_ls_shell.number_reflns_R_free             36 
_refine_ls_shell.number_reflns_all                600 
_refine_ls_shell.R_factor_all                     0.3118 
# 
_struct.entry_id                  7HY1 
_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-0035387-001 (A71EV2A-x4324)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HY1 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 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              7HY1 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
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 ? ? ? ? ? ? ? 2.347 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.246 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.308 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.070 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.2 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.2 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 117.5 ? 
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_555 107.5 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 99.1  ? 
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_555 116.0 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N VAL A 26  ? N VAL A 32  
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 GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7HY1 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     304 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    A 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     373 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_556 
_pdbx_validate_symm_contact.dist              1.78 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     125 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -136.67 
_pdbx_validate_torsion.psi             -30.76 
# 
_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         15.6531 
_pdbx_refine_tls.origin_y         7.6156 
_pdbx_refine_tls.origin_z         13.4292 
_pdbx_refine_tls.T[1][1]          -0.0497 
_pdbx_refine_tls.T[2][2]          -0.0115 
_pdbx_refine_tls.T[3][3]          0.0078 
_pdbx_refine_tls.T[1][2]          -0.0131 
_pdbx_refine_tls.T[1][3]          -0.0198 
_pdbx_refine_tls.T[2][3]          0.0032 
_pdbx_refine_tls.L[1][1]          0.8952 
_pdbx_refine_tls.L[2][2]          2.3202 
_pdbx_refine_tls.L[3][3]          0.3000 
_pdbx_refine_tls.L[1][2]          0.6368 
_pdbx_refine_tls.L[1][3]          -0.3889 
_pdbx_refine_tls.L[2][3]          -0.6681 
_pdbx_refine_tls.S[1][1]          -0.0734 
_pdbx_refine_tls.S[1][2]          0.0308 
_pdbx_refine_tls.S[1][3]          0.0511 
_pdbx_refine_tls.S[2][1]          -0.0072 
_pdbx_refine_tls.S[2][2]          0.0364 
_pdbx_refine_tls.S[2][3]          -0.0875 
_pdbx_refine_tls.S[3][1]          -0.0052 
_pdbx_refine_tls.S[3][2]          -0.0380 
_pdbx_refine_tls.S[3][3]          0.0370 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 512 ? 6.98 . 
2 1 O ? A HOH 513 ? 7.37 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BSG N1   N  N N 1   
A1BSG C4   C  N N 2   
A1BSG C5   C  N N 3   
A1BSG C6   C  Y N 4   
A1BSG C7   C  Y N 5   
A1BSG C8   C  Y N 6   
A1BSG C10  C  Y N 7   
A1BSG C13  C  N N 8   
A1BSG O1   O  N N 9   
A1BSG C3   C  N N 10  
A1BSG C2   C  N N 11  
A1BSG C14  C  N N 12  
A1BSG C1   C  N S 13  
A1BSG C    C  N N 14  
A1BSG O    O  N N 15  
A1BSG N    N  N N 16  
A1BSG C11  C  Y N 17  
A1BSG O2   O  N N 18  
A1BSG C12  C  N N 19  
A1BSG C9   C  Y N 20  
A1BSG H7   H  N N 21  
A1BSG H8   H  N N 22  
A1BSG H9   H  N N 23  
A1BSG H10  H  N N 24  
A1BSG H14  H  N N 25  
A1BSG H15  H  N N 26  
A1BSG H6   H  N N 27  
A1BSG H5   H  N N 28  
A1BSG H4   H  N N 29  
A1BSG H3   H  N N 30  
A1BSG H17  H  N N 31  
A1BSG H16  H  N N 32  
A1BSG H    H  N N 33  
A1BSG H1   H  N N 34  
A1BSG H2   H  N N 35  
A1BSG H12  H  N N 36  
A1BSG H13  H  N N 37  
A1BSG H11  H  N N 38  
ALA   N    N  N N 39  
ALA   CA   C  N S 40  
ALA   C    C  N N 41  
ALA   O    O  N N 42  
ALA   CB   C  N N 43  
ALA   OXT  O  N N 44  
ALA   H    H  N N 45  
ALA   H2   H  N N 46  
ALA   HA   H  N N 47  
ALA   HB1  H  N N 48  
ALA   HB2  H  N N 49  
ALA   HB3  H  N N 50  
ALA   HXT  H  N N 51  
ARG   N    N  N N 52  
ARG   CA   C  N S 53  
ARG   C    C  N N 54  
ARG   O    O  N N 55  
ARG   CB   C  N N 56  
ARG   CG   C  N N 57  
ARG   CD   C  N N 58  
ARG   NE   N  N N 59  
ARG   CZ   C  N N 60  
ARG   NH1  N  N N 61  
ARG   NH2  N  N N 62  
ARG   OXT  O  N N 63  
ARG   H    H  N N 64  
ARG   H2   H  N N 65  
ARG   HA   H  N N 66  
ARG   HB2  H  N N 67  
ARG   HB3  H  N N 68  
ARG   HG2  H  N N 69  
ARG   HG3  H  N N 70  
ARG   HD2  H  N N 71  
ARG   HD3  H  N N 72  
ARG   HE   H  N N 73  
ARG   HH11 H  N N 74  
ARG   HH12 H  N N 75  
ARG   HH21 H  N N 76  
ARG   HH22 H  N N 77  
ARG   HXT  H  N N 78  
ASN   N    N  N N 79  
ASN   CA   C  N S 80  
ASN   C    C  N N 81  
ASN   O    O  N N 82  
ASN   CB   C  N N 83  
ASN   CG   C  N N 84  
ASN   OD1  O  N N 85  
ASN   ND2  N  N N 86  
ASN   OXT  O  N N 87  
ASN   H    H  N N 88  
ASN   H2   H  N N 89  
ASN   HA   H  N N 90  
ASN   HB2  H  N N 91  
ASN   HB3  H  N N 92  
ASN   HD21 H  N N 93  
ASN   HD22 H  N N 94  
ASN   HXT  H  N N 95  
ASP   N    N  N N 96  
ASP   CA   C  N S 97  
ASP   C    C  N N 98  
ASP   O    O  N N 99  
ASP   CB   C  N N 100 
ASP   CG   C  N N 101 
ASP   OD1  O  N N 102 
ASP   OD2  O  N N 103 
ASP   OXT  O  N N 104 
ASP   H    H  N N 105 
ASP   H2   H  N N 106 
ASP   HA   H  N N 107 
ASP   HB2  H  N N 108 
ASP   HB3  H  N N 109 
ASP   HD2  H  N N 110 
ASP   HXT  H  N N 111 
CYS   N    N  N N 112 
CYS   CA   C  N R 113 
CYS   C    C  N N 114 
CYS   O    O  N N 115 
CYS   CB   C  N N 116 
CYS   SG   S  N N 117 
CYS   OXT  O  N N 118 
CYS   H    H  N N 119 
CYS   H2   H  N N 120 
CYS   HA   H  N N 121 
CYS   HB2  H  N N 122 
CYS   HB3  H  N N 123 
CYS   HG   H  N N 124 
CYS   HXT  H  N N 125 
DMS   S    S  N N 126 
DMS   O    O  N N 127 
DMS   C1   C  N N 128 
DMS   C2   C  N N 129 
DMS   H11  H  N N 130 
DMS   H12  H  N N 131 
DMS   H13  H  N N 132 
DMS   H21  H  N N 133 
DMS   H22  H  N N 134 
DMS   H23  H  N N 135 
GLN   N    N  N N 136 
GLN   CA   C  N S 137 
GLN   C    C  N N 138 
GLN   O    O  N N 139 
GLN   CB   C  N N 140 
GLN   CG   C  N N 141 
GLN   CD   C  N N 142 
GLN   OE1  O  N N 143 
GLN   NE2  N  N N 144 
GLN   OXT  O  N N 145 
GLN   H    H  N N 146 
GLN   H2   H  N N 147 
GLN   HA   H  N N 148 
GLN   HB2  H  N N 149 
GLN   HB3  H  N N 150 
GLN   HG2  H  N N 151 
GLN   HG3  H  N N 152 
GLN   HE21 H  N N 153 
GLN   HE22 H  N N 154 
GLN   HXT  H  N N 155 
GLU   N    N  N N 156 
GLU   CA   C  N S 157 
GLU   C    C  N N 158 
GLU   O    O  N N 159 
GLU   CB   C  N N 160 
GLU   CG   C  N N 161 
GLU   CD   C  N N 162 
GLU   OE1  O  N N 163 
GLU   OE2  O  N N 164 
GLU   OXT  O  N N 165 
GLU   H    H  N N 166 
GLU   H2   H  N N 167 
GLU   HA   H  N N 168 
GLU   HB2  H  N N 169 
GLU   HB3  H  N N 170 
GLU   HG2  H  N N 171 
GLU   HG3  H  N N 172 
GLU   HE2  H  N N 173 
GLU   HXT  H  N N 174 
GLY   N    N  N N 175 
GLY   CA   C  N N 176 
GLY   C    C  N N 177 
GLY   O    O  N N 178 
GLY   OXT  O  N N 179 
GLY   H    H  N N 180 
GLY   H2   H  N N 181 
GLY   HA2  H  N N 182 
GLY   HA3  H  N N 183 
GLY   HXT  H  N N 184 
HIS   N    N  N N 185 
HIS   CA   C  N S 186 
HIS   C    C  N N 187 
HIS   O    O  N N 188 
HIS   CB   C  N N 189 
HIS   CG   C  Y N 190 
HIS   ND1  N  Y N 191 
HIS   CD2  C  Y N 192 
HIS   CE1  C  Y N 193 
HIS   NE2  N  Y N 194 
HIS   OXT  O  N N 195 
HIS   H    H  N N 196 
HIS   H2   H  N N 197 
HIS   HA   H  N N 198 
HIS   HB2  H  N N 199 
HIS   HB3  H  N N 200 
HIS   HD1  H  N N 201 
HIS   HD2  H  N N 202 
HIS   HE1  H  N N 203 
HIS   HE2  H  N N 204 
HIS   HXT  H  N N 205 
HOH   O    O  N N 206 
HOH   H1   H  N N 207 
HOH   H2   H  N N 208 
ILE   N    N  N N 209 
ILE   CA   C  N S 210 
ILE   C    C  N N 211 
ILE   O    O  N N 212 
ILE   CB   C  N S 213 
ILE   CG1  C  N N 214 
ILE   CG2  C  N N 215 
ILE   CD1  C  N N 216 
ILE   OXT  O  N N 217 
ILE   H    H  N N 218 
ILE   H2   H  N N 219 
ILE   HA   H  N N 220 
ILE   HB   H  N N 221 
ILE   HG12 H  N N 222 
ILE   HG13 H  N N 223 
ILE   HG21 H  N N 224 
ILE   HG22 H  N N 225 
ILE   HG23 H  N N 226 
ILE   HD11 H  N N 227 
ILE   HD12 H  N N 228 
ILE   HD13 H  N N 229 
ILE   HXT  H  N N 230 
LEU   N    N  N N 231 
LEU   CA   C  N S 232 
LEU   C    C  N N 233 
LEU   O    O  N N 234 
LEU   CB   C  N N 235 
LEU   CG   C  N N 236 
LEU   CD1  C  N N 237 
LEU   CD2  C  N N 238 
LEU   OXT  O  N N 239 
LEU   H    H  N N 240 
LEU   H2   H  N N 241 
LEU   HA   H  N N 242 
LEU   HB2  H  N N 243 
LEU   HB3  H  N N 244 
LEU   HG   H  N N 245 
LEU   HD11 H  N N 246 
LEU   HD12 H  N N 247 
LEU   HD13 H  N N 248 
LEU   HD21 H  N N 249 
LEU   HD22 H  N N 250 
LEU   HD23 H  N N 251 
LEU   HXT  H  N N 252 
LYS   N    N  N N 253 
LYS   CA   C  N S 254 
LYS   C    C  N N 255 
LYS   O    O  N N 256 
LYS   CB   C  N N 257 
LYS   CG   C  N N 258 
LYS   CD   C  N N 259 
LYS   CE   C  N N 260 
LYS   NZ   N  N N 261 
LYS   OXT  O  N N 262 
LYS   H    H  N N 263 
LYS   H2   H  N N 264 
LYS   HA   H  N N 265 
LYS   HB2  H  N N 266 
LYS   HB3  H  N N 267 
LYS   HG2  H  N N 268 
LYS   HG3  H  N N 269 
LYS   HD2  H  N N 270 
LYS   HD3  H  N N 271 
LYS   HE2  H  N N 272 
LYS   HE3  H  N N 273 
LYS   HZ1  H  N N 274 
LYS   HZ2  H  N N 275 
LYS   HZ3  H  N N 276 
LYS   HXT  H  N N 277 
MET   N    N  N N 278 
MET   CA   C  N S 279 
MET   C    C  N N 280 
MET   O    O  N N 281 
MET   CB   C  N N 282 
MET   CG   C  N N 283 
MET   SD   S  N N 284 
MET   CE   C  N N 285 
MET   OXT  O  N N 286 
MET   H    H  N N 287 
MET   H2   H  N N 288 
MET   HA   H  N N 289 
MET   HB2  H  N N 290 
MET   HB3  H  N N 291 
MET   HG2  H  N N 292 
MET   HG3  H  N N 293 
MET   HE1  H  N N 294 
MET   HE2  H  N N 295 
MET   HE3  H  N N 296 
MET   HXT  H  N N 297 
PHE   N    N  N N 298 
PHE   CA   C  N S 299 
PHE   C    C  N N 300 
PHE   O    O  N N 301 
PHE   CB   C  N N 302 
PHE   CG   C  Y N 303 
PHE   CD1  C  Y N 304 
PHE   CD2  C  Y N 305 
PHE   CE1  C  Y N 306 
PHE   CE2  C  Y N 307 
PHE   CZ   C  Y N 308 
PHE   OXT  O  N N 309 
PHE   H    H  N N 310 
PHE   H2   H  N N 311 
PHE   HA   H  N N 312 
PHE   HB2  H  N N 313 
PHE   HB3  H  N N 314 
PHE   HD1  H  N N 315 
PHE   HD2  H  N N 316 
PHE   HE1  H  N N 317 
PHE   HE2  H  N N 318 
PHE   HZ   H  N N 319 
PHE   HXT  H  N N 320 
PRO   N    N  N N 321 
PRO   CA   C  N S 322 
PRO   C    C  N N 323 
PRO   O    O  N N 324 
PRO   CB   C  N N 325 
PRO   CG   C  N N 326 
PRO   CD   C  N N 327 
PRO   OXT  O  N N 328 
PRO   H    H  N N 329 
PRO   HA   H  N N 330 
PRO   HB2  H  N N 331 
PRO   HB3  H  N N 332 
PRO   HG2  H  N N 333 
PRO   HG3  H  N N 334 
PRO   HD2  H  N N 335 
PRO   HD3  H  N N 336 
PRO   HXT  H  N N 337 
SER   N    N  N N 338 
SER   CA   C  N S 339 
SER   C    C  N N 340 
SER   O    O  N N 341 
SER   CB   C  N N 342 
SER   OG   O  N N 343 
SER   OXT  O  N N 344 
SER   H    H  N N 345 
SER   H2   H  N N 346 
SER   HA   H  N N 347 
SER   HB2  H  N N 348 
SER   HB3  H  N N 349 
SER   HG   H  N N 350 
SER   HXT  H  N N 351 
THR   N    N  N N 352 
THR   CA   C  N S 353 
THR   C    C  N N 354 
THR   O    O  N N 355 
THR   CB   C  N R 356 
THR   OG1  O  N N 357 
THR   CG2  C  N N 358 
THR   OXT  O  N N 359 
THR   H    H  N N 360 
THR   H2   H  N N 361 
THR   HA   H  N N 362 
THR   HB   H  N N 363 
THR   HG1  H  N N 364 
THR   HG21 H  N N 365 
THR   HG22 H  N N 366 
THR   HG23 H  N N 367 
THR   HXT  H  N N 368 
TRP   N    N  N N 369 
TRP   CA   C  N S 370 
TRP   C    C  N N 371 
TRP   O    O  N N 372 
TRP   CB   C  N N 373 
TRP   CG   C  Y N 374 
TRP   CD1  C  Y N 375 
TRP   CD2  C  Y N 376 
TRP   NE1  N  Y N 377 
TRP   CE2  C  Y N 378 
TRP   CE3  C  Y N 379 
TRP   CZ2  C  Y N 380 
TRP   CZ3  C  Y N 381 
TRP   CH2  C  Y N 382 
TRP   OXT  O  N N 383 
TRP   H    H  N N 384 
TRP   H2   H  N N 385 
TRP   HA   H  N N 386 
TRP   HB2  H  N N 387 
TRP   HB3  H  N N 388 
TRP   HD1  H  N N 389 
TRP   HE1  H  N N 390 
TRP   HE3  H  N N 391 
TRP   HZ2  H  N N 392 
TRP   HZ3  H  N N 393 
TRP   HH2  H  N N 394 
TRP   HXT  H  N N 395 
TYR   N    N  N N 396 
TYR   CA   C  N S 397 
TYR   C    C  N N 398 
TYR   O    O  N N 399 
TYR   CB   C  N N 400 
TYR   CG   C  Y N 401 
TYR   CD1  C  Y N 402 
TYR   CD2  C  Y N 403 
TYR   CE1  C  Y N 404 
TYR   CE2  C  Y N 405 
TYR   CZ   C  Y N 406 
TYR   OH   O  N N 407 
TYR   OXT  O  N N 408 
TYR   H    H  N N 409 
TYR   H2   H  N N 410 
TYR   HA   H  N N 411 
TYR   HB2  H  N N 412 
TYR   HB3  H  N N 413 
TYR   HD1  H  N N 414 
TYR   HD2  H  N N 415 
TYR   HE1  H  N N 416 
TYR   HE2  H  N N 417 
TYR   HH   H  N N 418 
TYR   HXT  H  N N 419 
VAL   N    N  N N 420 
VAL   CA   C  N S 421 
VAL   C    C  N N 422 
VAL   O    O  N N 423 
VAL   CB   C  N N 424 
VAL   CG1  C  N N 425 
VAL   CG2  C  N N 426 
VAL   OXT  O  N N 427 
VAL   H    H  N N 428 
VAL   H2   H  N N 429 
VAL   HA   H  N N 430 
VAL   HB   H  N N 431 
VAL   HG11 H  N N 432 
VAL   HG12 H  N N 433 
VAL   HG13 H  N N 434 
VAL   HG21 H  N N 435 
VAL   HG22 H  N N 436 
VAL   HG23 H  N N 437 
VAL   HXT  H  N N 438 
ZN    ZN   ZN N N 439 
# 
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 
A1BSG N   C    sing N N 1   
A1BSG O   C    doub N N 2   
A1BSG C   C1   sing N N 3   
A1BSG C1  C2   sing N N 4   
A1BSG C2  C3   sing N N 5   
A1BSG C3  C4   sing N N 6   
A1BSG C4  O1   doub N N 7   
A1BSG N1  C4   sing N N 8   
A1BSG C5  N1   sing N N 9   
A1BSG C6  C5   sing N N 10  
A1BSG C6  C7   doub Y N 11  
A1BSG C7  C8   sing Y N 12  
A1BSG C8  C9   doub Y N 13  
A1BSG C9  C10  sing Y N 14  
A1BSG C10 C11  doub Y N 15  
A1BSG C11 C6   sing Y N 16  
A1BSG O2  C11  sing N N 17  
A1BSG C12 O2   sing N N 18  
A1BSG C13 C12  sing N N 19  
A1BSG C10 C13  sing N N 20  
A1BSG C14 N1   sing N N 21  
A1BSG C1  C14  sing N N 22  
A1BSG C5  H7   sing N N 23  
A1BSG C5  H8   sing N N 24  
A1BSG C7  H9   sing N N 25  
A1BSG C8  H10  sing N N 26  
A1BSG C13 H14  sing N N 27  
A1BSG C13 H15  sing N N 28  
A1BSG C3  H6   sing N N 29  
A1BSG C3  H5   sing N N 30  
A1BSG C2  H4   sing N N 31  
A1BSG C2  H3   sing N N 32  
A1BSG C14 H17  sing N N 33  
A1BSG C14 H16  sing N N 34  
A1BSG C1  H    sing N N 35  
A1BSG N   H1   sing N N 36  
A1BSG N   H2   sing N N 37  
A1BSG C12 H12  sing N N 38  
A1BSG C12 H13  sing N N 39  
A1BSG C9  H11  sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
DMS   S   O    doub N N 123 
DMS   S   C1   sing N N 124 
DMS   S   C2   sing N N 125 
DMS   C1  H11  sing N N 126 
DMS   C1  H12  sing N N 127 
DMS   C1  H13  sing N N 128 
DMS   C2  H21  sing N N 129 
DMS   C2  H22  sing N N 130 
DMS   C2  H23  sing N N 131 
GLN   N   CA   sing N N 132 
GLN   N   H    sing N N 133 
GLN   N   H2   sing N N 134 
GLN   CA  C    sing N N 135 
GLN   CA  CB   sing N N 136 
GLN   CA  HA   sing N N 137 
GLN   C   O    doub N N 138 
GLN   C   OXT  sing N N 139 
GLN   CB  CG   sing N N 140 
GLN   CB  HB2  sing N N 141 
GLN   CB  HB3  sing N N 142 
GLN   CG  CD   sing N N 143 
GLN   CG  HG2  sing N N 144 
GLN   CG  HG3  sing N N 145 
GLN   CD  OE1  doub N N 146 
GLN   CD  NE2  sing N N 147 
GLN   NE2 HE21 sing N N 148 
GLN   NE2 HE22 sing N N 149 
GLN   OXT HXT  sing N N 150 
GLU   N   CA   sing N N 151 
GLU   N   H    sing N N 152 
GLU   N   H2   sing N N 153 
GLU   CA  C    sing N N 154 
GLU   CA  CB   sing N N 155 
GLU   CA  HA   sing N N 156 
GLU   C   O    doub N N 157 
GLU   C   OXT  sing N N 158 
GLU   CB  CG   sing N N 159 
GLU   CB  HB2  sing N N 160 
GLU   CB  HB3  sing N N 161 
GLU   CG  CD   sing N N 162 
GLU   CG  HG2  sing N N 163 
GLU   CG  HG3  sing N N 164 
GLU   CD  OE1  doub N N 165 
GLU   CD  OE2  sing N N 166 
GLU   OE2 HE2  sing N N 167 
GLU   OXT HXT  sing N N 168 
GLY   N   CA   sing N N 169 
GLY   N   H    sing N N 170 
GLY   N   H2   sing N N 171 
GLY   CA  C    sing N N 172 
GLY   CA  HA2  sing N N 173 
GLY   CA  HA3  sing N N 174 
GLY   C   O    doub N N 175 
GLY   C   OXT  sing N N 176 
GLY   OXT HXT  sing N N 177 
HIS   N   CA   sing N N 178 
HIS   N   H    sing N N 179 
HIS   N   H2   sing N N 180 
HIS   CA  C    sing N N 181 
HIS   CA  CB   sing N N 182 
HIS   CA  HA   sing N N 183 
HIS   C   O    doub N N 184 
HIS   C   OXT  sing N N 185 
HIS   CB  CG   sing N N 186 
HIS   CB  HB2  sing N N 187 
HIS   CB  HB3  sing N N 188 
HIS   CG  ND1  sing Y N 189 
HIS   CG  CD2  doub Y N 190 
HIS   ND1 CE1  doub Y N 191 
HIS   ND1 HD1  sing N N 192 
HIS   CD2 NE2  sing Y N 193 
HIS   CD2 HD2  sing N N 194 
HIS   CE1 NE2  sing Y N 195 
HIS   CE1 HE1  sing N N 196 
HIS   NE2 HE2  sing N N 197 
HIS   OXT HXT  sing N N 198 
HOH   O   H1   sing N N 199 
HOH   O   H2   sing N N 200 
ILE   N   CA   sing N N 201 
ILE   N   H    sing N N 202 
ILE   N   H2   sing N N 203 
ILE   CA  C    sing N N 204 
ILE   CA  CB   sing N N 205 
ILE   CA  HA   sing N N 206 
ILE   C   O    doub N N 207 
ILE   C   OXT  sing N N 208 
ILE   CB  CG1  sing N N 209 
ILE   CB  CG2  sing N N 210 
ILE   CB  HB   sing N N 211 
ILE   CG1 CD1  sing N N 212 
ILE   CG1 HG12 sing N N 213 
ILE   CG1 HG13 sing N N 214 
ILE   CG2 HG21 sing N N 215 
ILE   CG2 HG22 sing N N 216 
ILE   CG2 HG23 sing N N 217 
ILE   CD1 HD11 sing N N 218 
ILE   CD1 HD12 sing N N 219 
ILE   CD1 HD13 sing N N 220 
ILE   OXT HXT  sing N N 221 
LEU   N   CA   sing N N 222 
LEU   N   H    sing N N 223 
LEU   N   H2   sing N N 224 
LEU   CA  C    sing N N 225 
LEU   CA  CB   sing N N 226 
LEU   CA  HA   sing N N 227 
LEU   C   O    doub N N 228 
LEU   C   OXT  sing N N 229 
LEU   CB  CG   sing N N 230 
LEU   CB  HB2  sing N N 231 
LEU   CB  HB3  sing N N 232 
LEU   CG  CD1  sing N N 233 
LEU   CG  CD2  sing N N 234 
LEU   CG  HG   sing N N 235 
LEU   CD1 HD11 sing N N 236 
LEU   CD1 HD12 sing N N 237 
LEU   CD1 HD13 sing N N 238 
LEU   CD2 HD21 sing N N 239 
LEU   CD2 HD22 sing N N 240 
LEU   CD2 HD23 sing N N 241 
LEU   OXT HXT  sing N N 242 
LYS   N   CA   sing N N 243 
LYS   N   H    sing N N 244 
LYS   N   H2   sing N N 245 
LYS   CA  C    sing N N 246 
LYS   CA  CB   sing N N 247 
LYS   CA  HA   sing N N 248 
LYS   C   O    doub N N 249 
LYS   C   OXT  sing N N 250 
LYS   CB  CG   sing N N 251 
LYS   CB  HB2  sing N N 252 
LYS   CB  HB3  sing N N 253 
LYS   CG  CD   sing N N 254 
LYS   CG  HG2  sing N N 255 
LYS   CG  HG3  sing N N 256 
LYS   CD  CE   sing N N 257 
LYS   CD  HD2  sing N N 258 
LYS   CD  HD3  sing N N 259 
LYS   CE  NZ   sing N N 260 
LYS   CE  HE2  sing N N 261 
LYS   CE  HE3  sing N N 262 
LYS   NZ  HZ1  sing N N 263 
LYS   NZ  HZ2  sing N N 264 
LYS   NZ  HZ3  sing N N 265 
LYS   OXT HXT  sing N N 266 
MET   N   CA   sing N N 267 
MET   N   H    sing N N 268 
MET   N   H2   sing N N 269 
MET   CA  C    sing N N 270 
MET   CA  CB   sing N N 271 
MET   CA  HA   sing N N 272 
MET   C   O    doub N N 273 
MET   C   OXT  sing N N 274 
MET   CB  CG   sing N N 275 
MET   CB  HB2  sing N N 276 
MET   CB  HB3  sing N N 277 
MET   CG  SD   sing N N 278 
MET   CG  HG2  sing N N 279 
MET   CG  HG3  sing N N 280 
MET   SD  CE   sing N N 281 
MET   CE  HE1  sing N N 282 
MET   CE  HE2  sing N N 283 
MET   CE  HE3  sing N N 284 
MET   OXT HXT  sing N N 285 
PHE   N   CA   sing N N 286 
PHE   N   H    sing N N 287 
PHE   N   H2   sing N N 288 
PHE   CA  C    sing N N 289 
PHE   CA  CB   sing N N 290 
PHE   CA  HA   sing N N 291 
PHE   C   O    doub N N 292 
PHE   C   OXT  sing N N 293 
PHE   CB  CG   sing N N 294 
PHE   CB  HB2  sing N N 295 
PHE   CB  HB3  sing N N 296 
PHE   CG  CD1  doub Y N 297 
PHE   CG  CD2  sing Y N 298 
PHE   CD1 CE1  sing Y N 299 
PHE   CD1 HD1  sing N N 300 
PHE   CD2 CE2  doub Y N 301 
PHE   CD2 HD2  sing N N 302 
PHE   CE1 CZ   doub Y N 303 
PHE   CE1 HE1  sing N N 304 
PHE   CE2 CZ   sing Y N 305 
PHE   CE2 HE2  sing N N 306 
PHE   CZ  HZ   sing N N 307 
PHE   OXT HXT  sing N N 308 
PRO   N   CA   sing N N 309 
PRO   N   CD   sing N N 310 
PRO   N   H    sing N N 311 
PRO   CA  C    sing N N 312 
PRO   CA  CB   sing N N 313 
PRO   CA  HA   sing N N 314 
PRO   C   O    doub N N 315 
PRO   C   OXT  sing N N 316 
PRO   CB  CG   sing N N 317 
PRO   CB  HB2  sing N N 318 
PRO   CB  HB3  sing N N 319 
PRO   CG  CD   sing N N 320 
PRO   CG  HG2  sing N N 321 
PRO   CG  HG3  sing N N 322 
PRO   CD  HD2  sing N N 323 
PRO   CD  HD3  sing N N 324 
PRO   OXT HXT  sing N N 325 
SER   N   CA   sing N N 326 
SER   N   H    sing N N 327 
SER   N   H2   sing N N 328 
SER   CA  C    sing N N 329 
SER   CA  CB   sing N N 330 
SER   CA  HA   sing N N 331 
SER   C   O    doub N N 332 
SER   C   OXT  sing N N 333 
SER   CB  OG   sing N N 334 
SER   CB  HB2  sing N N 335 
SER   CB  HB3  sing N N 336 
SER   OG  HG   sing N N 337 
SER   OXT HXT  sing N N 338 
THR   N   CA   sing N N 339 
THR   N   H    sing N N 340 
THR   N   H2   sing N N 341 
THR   CA  C    sing N N 342 
THR   CA  CB   sing N N 343 
THR   CA  HA   sing N N 344 
THR   C   O    doub N N 345 
THR   C   OXT  sing N N 346 
THR   CB  OG1  sing N N 347 
THR   CB  CG2  sing N N 348 
THR   CB  HB   sing N N 349 
THR   OG1 HG1  sing N N 350 
THR   CG2 HG21 sing N N 351 
THR   CG2 HG22 sing N N 352 
THR   CG2 HG23 sing N N 353 
THR   OXT HXT  sing N N 354 
TRP   N   CA   sing N N 355 
TRP   N   H    sing N N 356 
TRP   N   H2   sing N N 357 
TRP   CA  C    sing N N 358 
TRP   CA  CB   sing N N 359 
TRP   CA  HA   sing N N 360 
TRP   C   O    doub N N 361 
TRP   C   OXT  sing N N 362 
TRP   CB  CG   sing N N 363 
TRP   CB  HB2  sing N N 364 
TRP   CB  HB3  sing N N 365 
TRP   CG  CD1  doub Y N 366 
TRP   CG  CD2  sing Y N 367 
TRP   CD1 NE1  sing Y N 368 
TRP   CD1 HD1  sing N N 369 
TRP   CD2 CE2  doub Y N 370 
TRP   CD2 CE3  sing Y N 371 
TRP   NE1 CE2  sing Y N 372 
TRP   NE1 HE1  sing N N 373 
TRP   CE2 CZ2  sing Y N 374 
TRP   CE3 CZ3  doub Y N 375 
TRP   CE3 HE3  sing N N 376 
TRP   CZ2 CH2  doub Y N 377 
TRP   CZ2 HZ2  sing N N 378 
TRP   CZ3 CH2  sing Y N 379 
TRP   CZ3 HZ3  sing N N 380 
TRP   CH2 HH2  sing N N 381 
TRP   OXT HXT  sing N N 382 
TYR   N   CA   sing N N 383 
TYR   N   H    sing N N 384 
TYR   N   H2   sing N N 385 
TYR   CA  C    sing N N 386 
TYR   CA  CB   sing N N 387 
TYR   CA  HA   sing N N 388 
TYR   C   O    doub N N 389 
TYR   C   OXT  sing N N 390 
TYR   CB  CG   sing N N 391 
TYR   CB  HB2  sing N N 392 
TYR   CB  HB3  sing N N 393 
TYR   CG  CD1  doub Y N 394 
TYR   CG  CD2  sing Y N 395 
TYR   CD1 CE1  sing Y N 396 
TYR   CD1 HD1  sing N N 397 
TYR   CD2 CE2  doub Y N 398 
TYR   CD2 HD2  sing N N 399 
TYR   CE1 CZ   doub Y N 400 
TYR   CE1 HE1  sing N N 401 
TYR   CE2 CZ   sing Y N 402 
TYR   CE2 HE2  sing N N 403 
TYR   CZ  OH   sing N N 404 
TYR   OH  HH   sing N N 405 
TYR   OXT HXT  sing N N 406 
VAL   N   CA   sing N N 407 
VAL   N   H    sing N N 408 
VAL   N   H2   sing N N 409 
VAL   CA  C    sing N N 410 
VAL   CA  CB   sing N N 411 
VAL   CA  HA   sing N N 412 
VAL   C   O    doub N N 413 
VAL   C   OXT  sing N N 414 
VAL   CB  CG1  sing N N 415 
VAL   CB  CG2  sing N N 416 
VAL   CB  HB   sing N N 417 
VAL   CG1 HG11 sing N N 418 
VAL   CG1 HG12 sing N N 419 
VAL   CG1 HG13 sing N N 420 
VAL   CG2 HG21 sing N N 421 
VAL   CG2 HG22 sing N N 422 
VAL   CG2 HG23 sing N N 423 
VAL   OXT HXT  sing N N 424 
# 
_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                    7HY1 
_atom_sites.fract_transf_matrix[1][1]   0.011244 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000236 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017260 
_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]   0.030544 
_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   ? 19.972 6.954   23.457 1.00 23.51  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 21.105 7.008   22.530 1.00 24.75  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 21.068 5.859   21.514 1.00 23.78  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 20.316 4.885   21.688 1.00 23.68  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 22.435 7.021   23.296 1.00 27.64  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.680 5.768   23.907 1.00 32.88  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.824 6.018   20.431 1.00 22.16  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.950 5.008   19.392 1.00 21.40  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 22.270 5.575   18.030 1.00 20.74  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.912 6.716   17.725 1.00 22.13  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.893 4.777   17.187 1.00 19.19  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 23.213 5.190   15.816 1.00 19.87  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 23.141 4.035   14.848 1.00 19.68  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 23.203 2.855   15.270 1.00 21.03  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.645 5.766   15.791 1.00 20.70  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 23.052 4.334   13.534 1.00 18.21  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.124 3.369   12.457 1.00 19.49  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.509 3.550   11.790 1.00 20.09  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.933 4.678   11.518 1.00 20.93  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 22.026 3.619   11.410 1.00 19.91  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.638 3.683   12.061 1.00 19.41  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.069 2.557   10.311 1.00 21.64  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.593 4.378   11.134 1.00 20.16  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.218 2.431   11.524 1.00 20.46  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.527 2.475   10.852 1.00 21.91  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.451 1.738   9.525  1.00 23.18  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.348 0.513   9.539  1.00 24.22  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.602 1.845   11.754 1.00 23.04  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.845 2.644   13.013 1.00 23.54  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.635 3.792   12.991 1.00 24.21  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 27.208 2.318   14.198 1.00 25.11  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.818 4.563   14.135 1.00 25.31  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.353 3.098   15.335 1.00 25.41  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 28.184 4.204   15.310 1.00 26.82  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.289 4.977   16.443 1.00 28.38  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.428 2.440   8.398  1.00 22.25  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.295 1.853   7.067  1.00 24.59  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.378 2.421   6.174  1.00 25.95  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.570 3.646   6.125  1.00 25.17  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.870 2.062   6.481  1.00 25.39  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.443 3.546   6.536  1.00 26.23  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.765 1.491   5.072  1.00 27.01  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.187 1.555   5.542  1.00 26.95  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.308 2.020   4.731  1.00 27.55  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.224 2.931   5.529  1.00 27.85  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.525 2.623   6.681  1.00 28.51  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.557 4.111   4.992  1.00 27.81  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.345 5.074   5.760  1.00 27.12  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.488 6.200   6.313  1.00 25.42  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.953 7.344   6.404  1.00 25.42  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.529 5.612   4.969  1.00 29.81  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.644 4.602   4.871  1.00 37.93  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.467 4.432   5.792  1.00 40.53  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.672 3.881   3.765  1.00 39.97  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.271 5.864   6.738  1.00 24.86  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.344 6.843   7.308  1.00 24.45  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.861 6.429   8.711  1.00 22.95  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.726 5.231   9.011  1.00 21.73  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.104 6.991   6.421  1.00 24.31  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.381 7.537   5.041  1.00 24.76  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.992 8.776   4.872  1.00 26.53  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.047 6.815   3.905  1.00 26.29  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.273 9.271   3.609  1.00 28.00  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.297 7.320   2.631  1.00 27.41  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.897 8.558   2.492  1.00 29.28  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.149 9.096   1.252  1.00 31.87  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.615 7.435   9.552  1.00 21.62  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 27.035 7.302   10.899 1.00 21.35  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.743 8.129   10.926 1.00 20.69  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.799 9.344   10.714 1.00 21.50  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 28.015 7.820   11.950 1.00 23.30  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.473 7.951   13.379 1.00 24.13  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.586 8.284   14.403 1.00 26.68  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 28.180 9.289   15.406 1.00 26.01  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.670 9.007   16.605 1.00 28.24  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.438 7.743   16.957 1.00 27.59  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 27.320 9.987   17.432 1.00 24.68  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.596 7.491   11.212 1.00 19.86  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.310 8.211   11.248 1.00 19.96  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.870 8.314   12.717 1.00 20.31  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.710 7.267   13.386 1.00 20.49  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.226 7.462   10.450 1.00 20.70  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.917 8.258   10.424 1.00 20.37  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.687 7.116   9.039  1.00 21.69  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.607 9.538   13.194 1.00 19.29  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 22.190 9.756   14.579 1.00 19.36  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.982 10.728  14.647 1.00 18.87  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.693 11.429  13.669 1.00 18.95  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 23.352 10.300  15.448 1.00 22.02  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.414 9.239   15.663 1.00 24.89  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.946 11.584  14.841 1.00 22.23  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 20.323 10.851  15.834 1.00 16.59  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 19.309 11.899  16.012 1.00 16.72  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 20.106 13.215  15.985 1.00 18.68  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 21.176 13.341  16.649 1.00 19.69  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.634 11.801  17.403 1.00 17.18  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.765 10.553  17.568 1.00 18.71  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 18.216 9.507   18.048 1.00 20.01  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.515 10.635  17.176 1.00 17.55  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.594 14.198  15.233 1.00 17.61  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 20.324 15.497  15.110 1.00 17.50  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.557 16.118  16.497 1.00 19.17  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.655 16.635  16.766 1.00 19.43  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.527 16.451  14.192 1.00 18.13  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 20.281 17.747  13.814 1.00 17.80  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.301 18.652  13.059 1.00 18.70  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.890 19.907  12.570 1.00 22.14  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.923 21.049  13.251 1.00 24.14  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.620 21.070  14.549 1.00 23.74  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.376 22.164  12.672 1.00 23.74  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.561 16.016  17.395 1.00 19.09  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.687 16.590  18.737 1.00 19.62  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.707 15.889  19.605 1.00 20.64  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 21.163 16.496  20.571 1.00 22.41  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.323 16.702  19.437 1.00 19.77  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.731 15.406  19.928 1.00 19.86  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.999 14.568  19.093 1.00 20.02  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 17.723 14.886  21.183 1.00 20.36  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.583 13.562  19.855 1.00 19.62  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.998 13.701  21.123 1.00 20.58  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 21.160 14.661  19.238 1.00 20.04  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 22.206 13.960  20.003 1.00 21.69  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.583 13.965  19.313 1.00 23.12  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 24.515 13.315  19.805 1.00 23.57  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.748 12.530  20.304 1.00 22.36  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 20.442 12.450  21.110 1.00 22.97  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 20.025 10.975  21.335 1.00 23.04  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 20.537 13.193  22.452 1.00 23.50  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.719 14.669  18.151 1.00 22.33  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 25.021 14.680  17.465 1.00 23.36  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 26.137 15.304  18.293 1.00 24.68  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.900 16.249  19.040 1.00 24.54  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.890 15.374  16.113 1.00 23.65  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 27.357 14.756  18.168 1.00 24.01  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 28.538 15.254  18.886 1.00 24.20  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 29.300 16.329  18.083 1.00 24.85  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 29.043 16.520  16.882 1.00 23.76  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 29.489 14.078  19.197 1.00 26.96  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 30.069 13.666  17.951 1.00 30.20  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 28.779 12.892  19.851 1.00 26.93  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 30.302 16.946  18.711 1.00 26.24  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 31.210 17.901  18.095 1.00 27.97  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.858 17.268  16.833 1.00 27.05  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.906 17.925  15.781 1.00 26.93  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 32.260 18.319  19.154 1.00 32.25  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 33.616 18.706  18.637 1.00 39.61  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 34.025 20.020  18.621 1.00 42.88  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 34.647 17.927  18.224 1.00 41.45  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 35.247 20.010  18.109 1.00 43.70  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 35.645 18.772  17.823 1.00 42.84  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 32.283 16.009  16.942 1.00 27.00  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.909 15.266  15.843 1.00 27.65  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.924 15.060  14.700 1.00 26.07  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.304 15.211  13.542 1.00 26.89  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.451 13.906  16.319 1.00 30.93  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 34.310 13.217  15.281 1.00 38.57  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.478 13.585  15.072 1.00 41.97  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.765 12.205  14.612 1.00 40.25  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.642 14.722  14.998 1.00 23.86  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.667 14.544  13.936 1.00 23.22  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.485 15.860  13.140 1.00 22.99  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.404 15.807  11.917 1.00 23.27  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 28.279 14.184  14.509 1.00 22.72  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 28.187 12.797  15.069 1.00 25.40  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.747 11.863  14.438 1.00 27.40  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.602 12.643  16.166 1.00 23.88  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.382 17.006  13.815 1.00 23.23  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 29.203 18.292  13.113 1.00 23.74  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.475 18.666  12.295 1.00 23.96  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.309 19.170  11.176 1.00 23.35  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.835 19.440  14.083 1.00 22.81  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.424 19.372  14.577 1.00 22.63  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 27.003 18.949  15.809 1.00 23.41  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.261 19.774  13.865 1.00 21.64  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.629 19.048  15.893 1.00 23.47  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 25.140 19.484  14.682 1.00 22.88  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.034 20.257  12.563 1.00 21.47  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.825 19.773  14.279 1.00 23.04  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.738 20.538  12.167 1.00 21.87  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.644 20.262  13.004 1.00 22.28  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.677 18.359  12.811 1.00 25.36  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.935 18.619  12.093 1.00 25.28  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 33.064 17.720  10.850 1.00 25.97  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.678 18.120  9.857  1.00 26.70  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 34.134 18.398  13.019 1.00 25.14  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.465 16.511  10.898 1.00 24.85  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.514 15.565  9.777  1.00 25.66  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 31.119 15.387  9.165  1.00 24.55  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.773 14.295  8.686  1.00 23.89  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 33.080 14.231  10.278 1.00 27.93  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.528 14.437  10.636 1.00 32.81  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.380 14.538  9.762  1.00 34.73  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.814 14.639  11.913 1.00 33.60  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.332 16.481  9.141  1.00 23.16  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.945 16.476  8.663  1.00 21.63  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.852 16.132  7.179  1.00 23.05  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.583 16.701  6.365  1.00 24.81  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.294 17.865  8.912  1.00 21.45  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.893 18.084  8.372  1.00 21.41  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.866 17.229  9.121  1.00 22.24  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.462 19.564  8.532  1.00 22.32  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.917 15.227  6.837  1.00 21.34  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.596 14.923  5.444  1.00 22.25  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.250 15.607  5.088  1.00 23.38  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.131 16.278  4.060  1.00 25.62  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.520 13.383  5.224  1.00 23.24  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.980 13.065  3.825  1.00 24.04  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.904 12.756  5.431  1.00 24.07  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.211 15.403  5.922  1.00 21.99  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.872 15.936  5.670  1.00 21.78  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.095 16.001  7.009  1.00 20.74  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.276 15.150  7.874  1.00 20.52  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.128 15.010  4.665  1.00 22.57  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.666 15.291  4.521  1.00 22.26  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.075 16.212  3.705  1.00 23.27  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.600 14.613  5.210  1.00 21.58  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.699 16.164  3.864  1.00 23.83  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.389 15.201  4.791  1.00 22.37  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.564 13.623  6.200  1.00 22.53  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.143 14.750  5.249  1.00 23.27  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.324 13.175  6.650  1.00 22.88  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.140 13.733  6.162  1.00 22.48  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.253 17.032  7.192  1.00 19.21  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.399 17.119  8.382  1.00 18.94  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.102 17.856  8.028  1.00 19.55  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.063 18.685  7.110  1.00 19.80  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.103 17.777  9.585  1.00 18.54  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.716 19.166  9.291  1.00 20.33  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.787 20.367  9.346  1.00 24.24  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.198 21.444  8.850  1.00 24.23  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.680 20.262  9.924  1.00 23.45  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.021 17.509  8.740  1.00 19.61  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.728 18.148  8.504  1.00 19.87  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 17.016 18.245  9.870  1.00 18.92  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.596 17.228  10.439 1.00 18.75  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.930 17.353  7.444  1.00 22.16  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.575 17.927  7.074  1.00 27.36  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.027 18.680  7.872  1.00 28.91  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.100 17.662  5.930  1.00 28.56  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.878 19.470  10.398 1.00 18.65  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 16.225 19.770  11.669 0.50 18.83  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 16.252 19.665  11.707 0.50 19.26  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.768 19.278  11.660 1.00 19.31  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 14.287 18.729  12.659 1.00 19.92  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.230 21.286  11.893 0.50 19.93  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.439 21.096  12.221 0.50 22.01  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.841 21.575  13.222 0.50 21.30  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.537 21.985  11.595 0.50 24.26  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 14.069 19.488  10.504 1.00 18.48  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.659 19.070  10.413 1.00 18.70  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.510 17.546  10.474 1.00 18.74  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.430 17.086  10.775 1.00 20.05  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.982 19.630  9.168  1.00 23.27  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.374 18.933  8.001  1.00 29.98  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.578 16.772  10.256 1.00 17.28  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.523 15.297  10.362 1.00 16.16  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 14.159 14.779  11.665 1.00 16.63  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 14.135 13.565  11.927 1.00 17.00  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.264 14.628  9.178  1.00 16.62  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.521 14.836  7.861  1.00 18.11  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.243 14.239  6.643  1.00 19.72  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.256 12.771  6.701  1.00 18.89  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.321 11.974  5.640  1.00 18.95  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.336 12.490  4.410  1.00 19.72  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.255 10.651  5.790  1.00 18.78  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.858 15.652  12.420 1.00 17.92  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.630 15.246  13.599 1.00 17.52  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.750 14.229  13.207 1.00 16.88  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 17.083 13.353  14.012 1.00 16.87  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.751 14.714  14.767 1.00 17.85  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.545 14.412  16.049 1.00 19.31  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.455 15.194  16.386 1.00 19.38  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 15.333 13.326  16.655 1.00 19.28  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.356 14.362  11.976 1.00 17.38  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.441 13.468  11.553 1.00 16.66  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.730 14.229  11.226 1.00 17.05  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.694 15.351  10.685 1.00 18.13  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 18.060 12.681  10.279 1.00 17.95  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 17.025 11.564  10.427 1.00 18.65  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.773 10.902  9.083  1.00 19.43  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.446 10.551  11.489 1.00 18.10  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.855 13.526  11.412 1.00 17.20  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 22.190 13.998  11.053 1.00 18.05  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 23.025 12.797  10.617 1.00 18.70  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.942 11.701  11.235 1.00 19.59  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.844 14.705  12.222 1.00 18.69  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 24.240 15.306  11.902 1.00 19.67  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.454 16.598  12.659 1.00 21.99  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.355 14.312  12.214 1.00 21.74  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.779 12.945  9.502  1.00 18.90  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.675 11.893  9.023  1.00 18.41  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 26.087 12.495  8.982  1.00 19.41  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.286 13.600  8.453  1.00 20.61  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.299 11.372  7.608  1.00 19.64  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.317 10.337  7.135  1.00 20.83  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.872 10.795  7.586  1.00 18.94  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 27.052 11.754  9.522  1.00 20.04  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.455 12.154  9.532  1.00 21.37  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.301 11.047  8.912  1.00 23.70  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.871 9.900   8.815  1.00 24.11  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.909 12.449  10.964 1.00 21.60  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.853 11.303  11.797 1.00 23.00  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.521 11.393  8.464  1.00 24.03  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.403 10.411  7.834  1.00 25.89  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.224 9.645   8.873  1.00 26.91  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.468 10.158  9.960  1.00 28.70  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.315 11.102  6.828  1.00 28.49  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.072 12.095  7.498  1.00 32.30  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.613 8.405   8.571  1.00 26.76  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.402 7.572   9.482  1.00 28.64  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.669 7.071   8.775  1.00 31.70  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.716 7.020   7.537  1.00 31.65  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.591 6.347   9.999  1.00 29.02  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.399 5.430   8.927  1.00 30.19  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.259 6.737   10.638 1.00 29.41  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.664 6.652   9.558  1.00 33.86  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.899 6.103   9.001  1.00 36.85  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.771 4.597   8.777  1.00 37.11  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.330 4.065   7.822  1.00 38.25  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.071 6.429   9.930  1.00 40.74  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.865 5.732   11.163 1.00 44.51  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.197 7.917   10.200 1.00 40.78  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 36.029 3.909   9.643  1.00 36.32  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.843 2.475   9.536  1.00 36.31  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.517 2.133   8.879  1.00 35.39  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.560 2.909   8.955  1.00 34.93  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.911 1.838   10.916 1.00 37.01  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.450 0.959   8.249  1.00 34.51  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.246 0.486   7.592  1.00 33.96  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.222 -0.018  8.601  1.00 31.30  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.584 -0.725  9.545  1.00 31.11  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.595 -0.651  6.626  1.00 38.57  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 34.242 -0.189  5.332  1.00 46.30  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.322 -0.449  4.171  1.00 55.23  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.343 -1.527  3.567  1.00 59.40  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.487 0.528   3.836  1.00 55.73  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.958 0.359   8.400  1.00 28.43  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.858 -0.129  9.230  1.00 27.86  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.263 -1.417  8.711  1.00 27.46  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.506 -1.799  7.556  1.00 29.19  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.440 -2.073  9.540  1.00 25.19  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.871 -3.373  9.196  1.00 25.49  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.371 -3.391  9.073  1.00 24.98  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.811 -4.483  8.876  1.00 26.63  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.326 -4.435  10.195 1.00 26.34  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.114 -4.598  10.312 1.00 31.86  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.689 -2.249  9.251  1.00 24.24  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.218 -2.252  9.185  1.00 23.78  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.758 -2.187  7.702  1.00 24.36  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.491 -1.699  6.826  1.00 25.78  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.638 -1.062  10.004 1.00 23.72  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.845 -1.156  11.522 1.00 28.46  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.845 -2.287  12.055 1.00 30.89  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 24.009 -0.095  12.176 1.00 25.49  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.567 -2.725  7.415  1.00 24.01  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.984 -2.650  6.060  1.00 24.96  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.689 -1.824  6.196  1.00 24.05  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.920 -2.085  7.103  1.00 24.22  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.599 -4.069  5.559  1.00 27.76  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.817 -4.774  5.271  1.00 30.81  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.752 -4.037  4.263  1.00 29.04  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.465 -0.847  5.311  1.00 23.16  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.248 -0.044  5.352  1.00 22.37  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.176 -0.783  4.553  1.00 22.65  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.426 -1.221  3.413  1.00 23.76  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.488 1.380   4.773  1.00 22.47  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.713 2.085   5.381  1.00 23.49  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.230 2.265   4.907  1.00 23.21  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.586 2.338   6.909  1.00 24.95  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.964 -0.882  5.103  1.00 20.42  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.845 -1.481  4.390  1.00 21.27  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.466 -0.568  3.199  1.00 21.33  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.508 0.658   3.314  1.00 21.34  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.658 -1.574  5.337  1.00 21.14  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.062 -1.165  2.069  1.00 22.15  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.575 -0.426  0.896  1.00 22.73  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.253 -1.133  0.601  1.00 23.19  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.212 -2.140  -0.110 1.00 24.73  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.553 -0.527  -0.274 1.00 23.11  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.935 0.068   0.021  1.00 24.84  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.942 1.541   0.462  1.00 26.26  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.304 1.992   0.779  1.00 26.70  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.590 3.132   1.412  1.00 27.19  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.625 3.977   1.743  1.00 25.05  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.848 3.445   1.692  1.00 27.46  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.171 -0.595  1.153  1.00 22.57  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.882 -1.280  1.183  1.00 22.63  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.769  -0.338  1.686  1.00 23.00  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.048 0.809   2.071  1.00 22.85  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.032 -2.464  2.147  1.00 20.58  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.165 -1.974  3.894  1.00 21.56  ? 56  CYS   A SG  1 
ATOM   392  N  N   A ASP   A 1 51  ? 8.521  -0.832  1.738  0.50 23.41  ? 57  ASP   A N   1 
ATOM   393  N  N   B ASP   A 1 51  ? 8.520  -0.892  1.722  0.50 24.23  ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.423  -0.060  2.302  0.50 23.81  ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.248  -0.316  2.169  0.50 25.51  ? 57  ASP   A CA  1 
ATOM   396  C  C   A ASP   A 1 51  ? 6.790  -0.795  3.507  0.50 24.27  ? 57  ASP   A C   1 
ATOM   397  C  C   B ASP   A 1 51  ? 6.696  -1.058  3.409  0.50 24.85  ? 57  ASP   A C   1 
ATOM   398  O  O   A ASP   A 1 51  ? 5.616  -0.551  3.799  0.50 24.32  ? 57  ASP   A O   1 
ATOM   399  O  O   B ASP   A 1 51  ? 5.486  -1.054  3.631  0.50 24.55  ? 57  ASP   A O   1 
ATOM   400  C  CB  A ASP   A 1 51  ? 6.359  0.301   1.235  0.50 24.78  ? 57  ASP   A CB  1 
ATOM   401  C  CB  B ASP   A 1 51  ? 6.210  -0.479  1.037  0.50 28.90  ? 57  ASP   A CB  1 
ATOM   402  C  CG  A ASP   A 1 51  ? 5.614  -0.880  0.625  0.50 27.60  ? 57  ASP   A CG  1 
ATOM   403  C  CG  B ASP   A 1 51  ? 5.078  0.524   1.061  0.50 37.17  ? 57  ASP   A CG  1 
ATOM   404  O  OD1 A ASP   A 1 51  ? 5.937  -2.022  0.964  0.50 26.25  ? 57  ASP   A OD1 1 
ATOM   405  O  OD1 B ASP   A 1 51  ? 5.192  1.531   1.788  0.50 39.14  ? 57  ASP   A OD1 1 
ATOM   406  O  OD2 A ASP   A 1 51  ? 4.735  -0.651  -0.239 0.50 32.26  ? 57  ASP   A OD2 1 
ATOM   407  O  OD2 B ASP   A 1 51  ? 4.084  0.310   0.339  0.50 41.40  ? 57  ASP   A OD2 1 
ATOM   408  N  N   . CYS   A 1 52  ? 7.552  -1.706  4.196  1.00 23.62  ? 58  CYS   A N   1 
ATOM   409  C  CA  . CYS   A 1 52  ? 7.089  -2.456  5.399  1.00 22.57  ? 58  CYS   A CA  1 
ATOM   410  C  C   . CYS   A 1 52  ? 6.408  -1.522  6.399  1.00 21.56  ? 58  CYS   A C   1 
ATOM   411  O  O   . CYS   A 1 52  ? 6.801  -0.350  6.547  1.00 21.04  ? 58  CYS   A O   1 
ATOM   412  C  CB  . CYS   A 1 52  ? 8.232  -3.205  6.089  1.00 22.70  ? 58  CYS   A CB  1 
ATOM   413  S  SG  . CYS   A 1 52  ? 8.862  -4.657  5.194  1.00 22.88  ? 58  CYS   A SG  1 
ATOM   414  N  N   . GLN   A 1 53  ? 5.375  -2.051  7.053  1.00 20.49  ? 59  GLN   A N   1 
ATOM   415  C  CA  . GLN   A 1 53  ? 4.674  -1.370  8.131  1.00 19.56  ? 59  GLN   A CA  1 
ATOM   416  C  C   . GLN   A 1 53  ? 4.655  -2.226  9.407  1.00 19.24  ? 59  GLN   A C   1 
ATOM   417  O  O   . GLN   A 1 53  ? 3.875  -1.943  10.310 1.00 18.98  ? 59  GLN   A O   1 
ATOM   418  C  CB  . GLN   A 1 53  ? 3.250  -0.919  7.743  1.00 21.82  ? 59  GLN   A CB  1 
ATOM   419  C  CG  . GLN   A 1 53  ? 3.189  0.369   6.943  1.00 23.53  ? 59  GLN   A CG  1 
ATOM   420  C  CD  . GLN   A 1 53  ? 1.743  0.832   6.749  1.00 28.79  ? 59  GLN   A CD  1 
ATOM   421  O  OE1 . GLN   A 1 53  ? 1.144  0.646   5.676  1.00 32.51  ? 59  GLN   A OE1 1 
ATOM   422  N  NE2 . GLN   A 1 53  ? 1.141  1.404   7.795  1.00 28.18  ? 59  GLN   A NE2 1 
ATOM   423  N  N   . THR   A 1 54  ? 5.476  -3.322  9.471  1.00 17.89  ? 60  THR   A N   1 
ATOM   424  C  CA  . THR   A 1 54  ? 5.657  -4.111  10.680 1.00 18.20  ? 60  THR   A CA  1 
ATOM   425  C  C   . THR   A 1 54  ? 7.169  -4.329  10.876 1.00 17.03  ? 60  THR   A C   1 
ATOM   426  O  O   . THR   A 1 54  ? 7.923  -4.398  9.914  1.00 19.27  ? 60  THR   A O   1 
ATOM   427  C  CB  . THR   A 1 54  ? 4.912  -5.464  10.653 1.00 20.85  ? 60  THR   A CB  1 
ATOM   428  O  OG1 . THR   A 1 54  ? 5.457  -6.269  9.633  1.00 24.10  ? 60  THR   A OG1 1 
ATOM   429  C  CG2 . THR   A 1 54  ? 3.422  -5.316  10.432 1.00 20.58  ? 60  THR   A CG2 1 
ATOM   430  N  N   . GLY   A 1 55  ? 7.574  -4.373  12.150 1.00 16.30  ? 61  GLY   A N   1 
ATOM   431  C  CA  . GLY   A 1 55  ? 8.979  -4.557  12.520 1.00 16.19  ? 61  GLY   A CA  1 
ATOM   432  C  C   . GLY   A 1 55  ? 9.136  -4.700  14.021 1.00 15.79  ? 61  GLY   A C   1 
ATOM   433  O  O   . GLY   A 1 55  ? 8.182  -5.024  14.717 1.00 17.66  ? 61  GLY   A O   1 
ATOM   434  N  N   . VAL   A 1 56  ? 10.368 -4.564  14.477 1.00 14.18  ? 62  VAL   A N   1 
ATOM   435  C  CA  . VAL   A 1 56  ? 10.715 -4.667  15.895 1.00 13.64  ? 62  VAL   A CA  1 
ATOM   436  C  C   . VAL   A 1 56  ? 11.590 -3.462  16.256 1.00 14.78  ? 62  VAL   A C   1 
ATOM   437  O  O   . VAL   A 1 56  ? 12.464 -3.092  15.482 1.00 16.73  ? 62  VAL   A O   1 
ATOM   438  C  CB  . VAL   A 1 56  ? 11.487 -6.018  16.164 1.00 15.59  ? 62  VAL   A CB  1 
ATOM   439  C  CG1 . VAL   A 1 56  ? 11.893 -6.137  17.648 1.00 16.81  ? 62  VAL   A CG1 1 
ATOM   440  C  CG2 . VAL   A 1 56  ? 10.623 -7.191  15.822 1.00 18.33  ? 62  VAL   A CG2 1 
ATOM   441  N  N   . TYR   A 1 57  ? 11.369 -2.868  17.459 1.00 14.86  ? 63  TYR   A N   1 
ATOM   442  C  CA  . TYR   A 1 57  ? 12.250 -1.757  17.880 1.00 13.49  ? 63  TYR   A CA  1 
ATOM   443  C  C   . TYR   A 1 57  ? 12.805 -1.991  19.254 1.00 14.83  ? 63  TYR   A C   1 
ATOM   444  O  O   . TYR   A 1 57  ? 12.188 -2.668  20.047 1.00 15.94  ? 63  TYR   A O   1 
ATOM   445  C  CB  . TYR   A 1 57  ? 11.548 -0.368  17.814 1.00 13.95  ? 63  TYR   A CB  1 
ATOM   446  C  CG  . TYR   A 1 57  ? 10.646 -0.001  18.977 1.00 14.76  ? 63  TYR   A CG  1 
ATOM   447  C  CD1 . TYR   A 1 57  ? 9.356  -0.520  19.071 1.00 15.74  ? 63  TYR   A CD1 1 
ATOM   448  C  CD2 . TYR   A 1 57  ? 11.093 0.838   20.003 1.00 16.40  ? 63  TYR   A CD2 1 
ATOM   449  C  CE1 . TYR   A 1 57  ? 8.524  -0.200  20.141 1.00 17.09  ? 63  TYR   A CE1 1 
ATOM   450  C  CE2 . TYR   A 1 57  ? 10.247 1.205   21.055 1.00 16.27  ? 63  TYR   A CE2 1 
ATOM   451  C  CZ  . TYR   A 1 57  ? 8.966  0.665   21.132 1.00 16.97  ? 63  TYR   A CZ  1 
ATOM   452  O  OH  . TYR   A 1 57  ? 8.132  0.973   22.192 1.00 17.49  ? 63  TYR   A OH  1 
ATOM   453  N  N   . TYR   A 1 58  ? 13.985 -1.408  19.511 1.00 14.11  ? 64  TYR   A N   1 
ATOM   454  C  CA  . TYR   A 1 58  ? 14.597 -1.514  20.843 1.00 15.52  ? 64  TYR   A CA  1 
ATOM   455  C  C   . TYR   A 1 58  ? 14.168 -0.326  21.689 1.00 16.04  ? 64  TYR   A C   1 
ATOM   456  O  O   . TYR   A 1 58  ? 14.443 0.829   21.327 1.00 16.34  ? 64  TYR   A O   1 
ATOM   457  C  CB  . TYR   A 1 58  ? 16.141 -1.556  20.765 1.00 16.05  ? 64  TYR   A CB  1 
ATOM   458  C  CG  . TYR   A 1 58  ? 16.727 -1.646  22.158 1.00 17.12  ? 64  TYR   A CG  1 
ATOM   459  C  CD1 . TYR   A 1 58  ? 16.470 -2.738  22.969 1.00 17.86  ? 64  TYR   A CD1 1 
ATOM   460  C  CD2 . TYR   A 1 58  ? 17.588 -0.668  22.635 1.00 18.72  ? 64  TYR   A CD2 1 
ATOM   461  C  CE1 . TYR   A 1 58  ? 17.010 -2.831  24.261 1.00 18.77  ? 64  TYR   A CE1 1 
ATOM   462  C  CE2 . TYR   A 1 58  ? 18.133 -0.745  23.920 1.00 19.98  ? 64  TYR   A CE2 1 
ATOM   463  C  CZ  . TYR   A 1 58  ? 17.869 -1.846  24.713 1.00 20.73  ? 64  TYR   A CZ  1 
ATOM   464  O  OH  . TYR   A 1 58  ? 18.355 -1.919  26.006 1.00 24.75  ? 64  TYR   A OH  1 
ATOM   465  N  N   . CYS   A 1 59  ? 13.671 -0.637  22.921 1.00 16.35  ? 65  CYS   A N   1 
ATOM   466  C  CA  . CYS   A 1 59  ? 13.240 0.337   23.914 1.00 17.16  ? 65  CYS   A CA  1 
ATOM   467  C  C   . CYS   A 1 59  ? 14.187 0.231   25.139 1.00 18.38  ? 65  CYS   A C   1 
ATOM   468  O  O   . CYS   A 1 59  ? 14.052 -0.671  25.959 1.00 18.87  ? 65  CYS   A O   1 
ATOM   469  C  CB  . CYS   A 1 59  ? 11.779 0.091   24.302 1.00 18.09  ? 65  CYS   A CB  1 
ATOM   470  S  SG  . CYS   A 1 59  ? 11.165 1.181   25.627 1.00 19.78  ? 65  CYS   A SG  1 
ATOM   471  N  N   . SER   A 1 60  ? 15.166 1.141   25.239 1.00 17.50  ? 66  SER   A N   1 
ATOM   472  C  CA  . SER   A 1 60  ? 16.130 1.119   26.347 1.00 18.20  ? 66  SER   A CA  1 
ATOM   473  C  C   . SER   A 1 60  ? 15.491 1.285   27.725 1.00 19.35  ? 66  SER   A C   1 
ATOM   474  O  O   . SER   A 1 60  ? 15.996 0.721   28.708 1.00 20.78  ? 66  SER   A O   1 
ATOM   475  C  CB  . SER   A 1 60  ? 17.246 2.148   26.144 1.00 20.41  ? 66  SER   A CB  1 
ATOM   476  O  OG  . SER   A 1 60  ? 16.792 3.483   26.321 1.00 25.31  ? 66  SER   A OG  1 
ATOM   477  N  N   . SER   A 1 61  ? 14.388 2.075   27.822 1.00 18.71  ? 67  SER   A N   1 
ATOM   478  C  CA  . SER   A 1 61  ? 13.722 2.294   29.125 1.00 19.29  ? 67  SER   A CA  1 
ATOM   479  C  C   . SER   A 1 61  ? 12.955 1.049   29.617 1.00 19.98  ? 67  SER   A C   1 
ATOM   480  O  O   . SER   A 1 61  ? 12.456 1.050   30.747 1.00 20.79  ? 67  SER   A O   1 
ATOM   481  C  CB  . SER   A 1 61  ? 12.807 3.517   29.078 1.00 19.32  ? 67  SER   A CB  1 
ATOM   482  O  OG  . SER   A 1 61  ? 11.746 3.329   28.158 1.00 22.30  ? 67  SER   A OG  1 
ATOM   483  N  N   . ARG   A 1 62  ? 12.878 -0.012  28.802 1.00 19.48  ? 68  ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 62  ? 12.289 -1.288  29.221 1.00 19.78  ? 68  ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 62  ? 13.271 -2.456  29.037 1.00 19.82  ? 68  ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 62  ? 12.926 -3.611  29.352 1.00 20.41  ? 68  ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 62  ? 11.003 -1.575  28.433 1.00 20.32  ? 68  ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 62  ? 9.862  -0.600  28.716 1.00 20.57  ? 68  ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 62  ? 9.235  -0.879  30.085 1.00 22.16  ? 68  ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 62  ? 8.123  0.045   30.360 1.00 24.86  ? 68  ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 62  ? 8.259  1.207   30.990 1.00 26.61  ? 68  ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 62  ? 9.456  1.604   31.418 1.00 25.09  ? 68  ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 62  ? 7.193  1.972   31.228 1.00 26.97  ? 68  ARG   A NH2 1 
ATOM   494  N  N   . ARG   A 1 63  ? 14.494 -2.202  28.477 1.00 19.82  ? 69  ARG   A N   1 
ATOM   495  C  CA  . ARG   A 1 63  ? 15.463 -3.255  28.082 1.00 20.47  ? 69  ARG   A CA  1 
ATOM   496  C  C   . ARG   A 1 63  ? 14.729 -4.349  27.278 1.00 20.86  ? 69  ARG   A C   1 
ATOM   497  O  O   . ARG   A 1 63  ? 14.891 -5.542  27.545 1.00 22.30  ? 69  ARG   A O   1 
ATOM   498  C  CB  . ARG   A 1 63  ? 16.184 -3.861  29.307 1.00 21.26  ? 69  ARG   A CB  1 
ATOM   499  C  CG  . ARG   A 1 63  ? 17.116 -2.871  29.983 1.00 23.00  ? 69  ARG   A CG  1 
ATOM   500  C  CD  . ARG   A 1 63  ? 17.877 -3.531  31.117 1.00 28.65  ? 69  ARG   A CD  1 
ATOM   501  N  NE  . ARG   A 1 63  ? 18.695 -2.568  31.855 1.00 31.56  ? 69  ARG   A NE  1 
ATOM   502  C  CZ  . ARG   A 1 63  ? 18.630 -2.393  33.177 1.00 35.29  ? 69  ARG   A CZ  1 
ATOM   503  N  NH1 . ARG   A 1 63  ? 17.761 -3.085  33.903 1.00 35.81  ? 69  ARG   A NH1 1 
ATOM   504  N  NH2 . ARG   A 1 63  ? 19.401 -1.488  33.773 1.00 35.20  ? 69  ARG   A NH2 1 
ATOM   505  N  N   . LYS   A 1 64  ? 13.890 -3.942  26.307 1.00 18.94  ? 70  LYS   A N   1 
ATOM   506  C  CA  . LYS   A 1 64  ? 13.052 -4.896  25.568 1.00 17.41  ? 70  LYS   A CA  1 
ATOM   507  C  C   . LYS   A 1 64  ? 12.955 -4.522  24.110 1.00 17.18  ? 70  LYS   A C   1 
ATOM   508  O  O   . LYS   A 1 64  ? 12.984 -3.330  23.776 1.00 19.12  ? 70  LYS   A O   1 
ATOM   509  C  CB  . LYS   A 1 64  ? 11.614 -4.929  26.159 1.00 21.88  ? 70  LYS   A CB  1 
ATOM   510  C  CG  . LYS   A 1 64  ? 11.526 -5.812  27.405 1.00 33.18  ? 70  LYS   A CG  1 
ATOM   511  C  CD  . LYS   A 1 64  ? 10.117 -6.324  27.661 1.00 41.85  ? 70  LYS   A CD  1 
ATOM   512  C  CE  . LYS   A 1 64  ? 10.072 -7.249  28.860 1.00 48.85  ? 70  LYS   A CE  1 
ATOM   513  N  NZ  . LYS   A 1 64  ? 10.484 -6.572  30.121 1.00 52.77  ? 70  LYS   A NZ  1 
ATOM   514  N  N   . HIS   A 1 65  ? 12.769 -5.510  23.262 1.00 15.73  ? 71  HIS   A N   1 
ATOM   515  C  CA  . HIS   A 1 65  ? 12.583 -5.333  21.802 1.00 15.47  ? 71  HIS   A CA  1 
ATOM   516  C  C   . HIS   A 1 65  ? 11.105 -5.671  21.539 1.00 18.12  ? 71  HIS   A C   1 
ATOM   517  O  O   . HIS   A 1 65  ? 10.652 -6.805  21.786 1.00 20.29  ? 71  HIS   A O   1 
ATOM   518  C  CB  . HIS   A 1 65  ? 13.484 -6.356  21.083 1.00 16.54  ? 71  HIS   A CB  1 
ATOM   519  C  CG  . HIS   A 1 65  ? 14.949 -6.133  21.348 1.00 18.19  ? 71  HIS   A CG  1 
ATOM   520  N  ND1 . HIS   A 1 65  ? 15.767 -5.466  20.442 1.00 20.10  ? 71  HIS   A ND1 1 
ATOM   521  C  CD2 . HIS   A 1 65  ? 15.682 -6.465  22.436 1.00 18.21  ? 71  HIS   A CD2 1 
ATOM   522  C  CE1 . HIS   A 1 65  ? 16.970 -5.441  20.982 1.00 19.57  ? 71  HIS   A CE1 1 
ATOM   523  N  NE2 . HIS   A 1 65  ? 16.971 -5.998  22.202 1.00 19.70  ? 71  HIS   A NE2 1 
ATOM   524  N  N   . TYR   A 1 66  ? 10.353 -4.682  21.071 1.00 15.93  ? 72  TYR   A N   1 
ATOM   525  C  CA  . TYR   A 1 66  ? 8.923  -4.857  20.873 1.00 15.16  ? 72  TYR   A CA  1 
ATOM   526  C  C   . TYR   A 1 66  ? 8.514  -4.982  19.388 1.00 14.81  ? 72  TYR   A C   1 
ATOM   527  O  O   . TYR   A 1 66  ? 8.862  -4.126  18.579 1.00 16.05  ? 72  TYR   A O   1 
ATOM   528  C  CB  . TYR   A 1 66  ? 8.162  -3.627  21.432 1.00 15.72  ? 72  TYR   A CB  1 
ATOM   529  C  CG  . TYR   A 1 66  ? 8.210  -3.486  22.937 1.00 16.57  ? 72  TYR   A CG  1 
ATOM   530  C  CD1 . TYR   A 1 66  ? 7.375  -4.246  23.751 1.00 18.52  ? 72  TYR   A CD1 1 
ATOM   531  C  CD2 . TYR   A 1 66  ? 8.996  -2.513  23.539 1.00 17.38  ? 72  TYR   A CD2 1 
ATOM   532  C  CE1 . TYR   A 1 66  ? 7.373  -4.081  25.136 1.00 19.58  ? 72  TYR   A CE1 1 
ATOM   533  C  CE2 . TYR   A 1 66  ? 8.990  -2.327  24.920 1.00 18.03  ? 72  TYR   A CE2 1 
ATOM   534  C  CZ  . TYR   A 1 66  ? 8.135  -3.075  25.704 1.00 19.64  ? 72  TYR   A CZ  1 
ATOM   535  O  OH  . TYR   A 1 66  ? 8.143  -2.934  27.087 1.00 21.86  ? 72  TYR   A OH  1 
ATOM   536  N  N   . PRO   A 1 67  ? 7.685  -5.979  19.076 1.00 15.51  ? 73  PRO   A N   1 
ATOM   537  C  CA  . PRO   A 1 67  ? 7.146  -6.086  17.701 1.00 15.15  ? 73  PRO   A CA  1 
ATOM   538  C  C   . PRO   A 1 67  ? 6.045  -5.024  17.551 1.00 17.20  ? 73  PRO   A C   1 
ATOM   539  O  O   . PRO   A 1 67  ? 5.187  -4.926  18.446 1.00 19.40  ? 73  PRO   A O   1 
ATOM   540  C  CB  . PRO   A 1 67  ? 6.485  -7.498  17.678 1.00 18.04  ? 73  PRO   A CB  1 
ATOM   541  C  CG  . PRO   A 1 67  ? 6.387  -7.917  19.081 1.00 20.64  ? 73  PRO   A CG  1 
ATOM   542  C  CD  . PRO   A 1 67  ? 7.261  -7.095  19.954 1.00 17.68  ? 73  PRO   A CD  1 
ATOM   543  N  N   . VAL   A 1 68  ? 6.037  -4.279  16.438 1.00 15.86  ? 74  VAL   A N   1 
ATOM   544  C  CA  . VAL   A 1 68  ? 5.061  -3.204  16.263 1.00 16.54  ? 74  VAL   A CA  1 
ATOM   545  C  C   . VAL   A 1 68  ? 4.572  -3.112  14.831 1.00 17.63  ? 74  VAL   A C   1 
ATOM   546  O  O   . VAL   A 1 68  ? 5.275  -3.457  13.887 1.00 18.99  ? 74  VAL   A O   1 
ATOM   547  C  CB  . VAL   A 1 68  ? 5.638  -1.804  16.659 1.00 18.58  ? 74  VAL   A CB  1 
ATOM   548  C  CG1 . VAL   A 1 68  ? 5.736  -1.640  18.193 1.00 20.51  ? 74  VAL   A CG1 1 
ATOM   549  C  CG2 . VAL   A 1 68  ? 6.978  -1.508  15.972 1.00 20.15  ? 74  VAL   A CG2 1 
ATOM   550  N  N   . SER   A 1 69  ? 3.355  -2.537  14.672 1.00 16.86  ? 75  SER   A N   1 
ATOM   551  C  CA  . SER   A 1 69  ? 2.821  -2.048  13.401 1.00 16.71  ? 75  SER   A CA  1 
ATOM   552  C  C   . SER   A 1 69  ? 3.044  -0.526  13.436 1.00 17.29  ? 75  SER   A C   1 
ATOM   553  O  O   . SER   A 1 69  ? 2.893  0.084   14.487 1.00 17.70  ? 75  SER   A O   1 
ATOM   554  C  CB  . SER   A 1 69  ? 1.321  -2.305  13.314 1.00 20.77  ? 75  SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 69  ? 1.092  -3.705  13.271 1.00 27.75  ? 75  SER   A OG  1 
ATOM   556  N  N   . PHE   A 1 70  ? 3.483  0.067   12.337 1.00 15.65  ? 76  PHE   A N   1 
ATOM   557  C  CA  . PHE   A 1 70  ? 3.773  1.513   12.322 1.00 16.00  ? 76  PHE   A CA  1 
ATOM   558  C  C   . PHE   A 1 70  ? 3.227  2.165   11.093 1.00 17.23  ? 76  PHE   A C   1 
ATOM   559  O  O   . PHE   A 1 70  ? 3.051  1.525   10.063 1.00 19.12  ? 76  PHE   A O   1 
ATOM   560  C  CB  . PHE   A 1 70  ? 5.300  1.795   12.507 1.00 16.79  ? 76  PHE   A CB  1 
ATOM   561  C  CG  . PHE   A 1 70  ? 6.245  1.069   11.570 1.00 16.84  ? 76  PHE   A CG  1 
ATOM   562  C  CD1 . PHE   A 1 70  ? 6.743  -0.190  11.894 1.00 17.13  ? 76  PHE   A CD1 1 
ATOM   563  C  CD2 . PHE   A 1 70  ? 6.631  1.642   10.360 1.00 17.64  ? 76  PHE   A CD2 1 
ATOM   564  C  CE1 . PHE   A 1 70  ? 7.587  -0.866  11.014 1.00 17.84  ? 76  PHE   A CE1 1 
ATOM   565  C  CE2 . PHE   A 1 70  ? 7.520  0.984   9.511  1.00 18.10  ? 76  PHE   A CE2 1 
ATOM   566  C  CZ  . PHE   A 1 70  ? 7.950  -0.291  9.811  1.00 17.16  ? 76  PHE   A CZ  1 
ATOM   567  N  N   . SER   A 1 71  ? 2.990  3.491   11.179 1.00 17.49  ? 77  SER   A N   1 
ATOM   568  C  CA  . SER   A 1 71  ? 2.412  4.223   10.072 1.00 19.67  ? 77  SER   A CA  1 
ATOM   569  C  C   . SER   A 1 71  ? 3.431  4.575   8.966  1.00 20.23  ? 77  SER   A C   1 
ATOM   570  O  O   . SER   A 1 71  ? 4.626  4.407   9.188  1.00 21.24  ? 77  SER   A O   1 
ATOM   571  C  CB  . SER   A 1 71  ? 1.708  5.468   10.619 1.00 21.45  ? 77  SER   A CB  1 
ATOM   572  O  OG  . SER   A 1 71  ? 2.645  6.391   11.147 1.00 22.62  ? 77  SER   A OG  1 
ATOM   573  N  N   . LYS   A 1 72  ? 2.997  5.013   7.751  1.00 22.08  ? 78  LYS   A N   1 
ATOM   574  C  CA  . LYS   A 1 72  ? 3.957  5.403   6.708  1.00 23.35  ? 78  LYS   A CA  1 
ATOM   575  C  C   . LYS   A 1 72  ? 4.548  6.779   7.049  1.00 23.14  ? 78  LYS   A C   1 
ATOM   576  O  O   . LYS   A 1 72  ? 3.869  7.603   7.669  1.00 24.12  ? 78  LYS   A O   1 
ATOM   577  C  CB  . LYS   A 1 72  ? 3.268  5.412   5.299  1.00 25.90  ? 78  LYS   A CB  1 
ATOM   578  C  CG  . LYS   A 1 72  ? 3.020  3.994   4.753  1.00 31.10  ? 78  LYS   A CG  1 
ATOM   579  C  CD  . LYS   A 1 72  ? 2.534  3.999   3.291  1.00 35.97  ? 78  LYS   A CD  1 
ATOM   580  C  CE  . LYS   A 1 72  ? 2.148  2.591   2.902  1.00 39.98  ? 78  LYS   A CE  1 
ATOM   581  N  NZ  . LYS   A 1 72  ? 1.910  2.460   1.433  1.00 43.51  ? 78  LYS   A NZ  1 
ATOM   582  N  N   . PRO   A 1 73  ? 5.765  7.074   6.558  1.00 22.08  ? 79  PRO   A N   1 
ATOM   583  C  CA  . PRO   A 1 73  ? 6.406  8.367   6.897  1.00 21.74  ? 79  PRO   A CA  1 
ATOM   584  C  C   . PRO   A 1 73  ? 5.542  9.561   6.526  1.00 21.64  ? 79  PRO   A C   1 
ATOM   585  O  O   . PRO   A 1 73  ? 5.055  9.646   5.385  1.00 22.41  ? 79  PRO   A O   1 
ATOM   586  C  CB  . PRO   A 1 73  ? 7.742  8.319   6.154  1.00 23.42  ? 79  PRO   A CB  1 
ATOM   587  C  CG  . PRO   A 1 73  ? 8.015  6.874   5.932  1.00 24.92  ? 79  PRO   A CG  1 
ATOM   588  C  CD  . PRO   A 1 73  ? 6.674  6.190   5.811  1.00 22.19  ? 79  PRO   A CD  1 
ATOM   589  N  N   A SER   A 1 74  ? 5.326  10.474  7.481  0.50 20.69  ? 80  SER   A N   1 
ATOM   590  N  N   B SER   A 1 74  ? 5.322  10.473  7.482  0.50 20.85  ? 80  SER   A N   1 
ATOM   591  C  CA  A SER   A 1 74  ? 4.425  11.601  7.283  0.50 21.50  ? 80  SER   A CA  1 
ATOM   592  C  CA  B SER   A 1 74  ? 4.436  11.609  7.279  0.50 21.81  ? 80  SER   A CA  1 
ATOM   593  C  C   A SER   A 1 74  ? 4.887  12.875  8.020  0.50 21.84  ? 80  SER   A C   1 
ATOM   594  C  C   B SER   A 1 74  ? 4.844  12.860  8.078  0.50 21.96  ? 80  SER   A C   1 
ATOM   595  O  O   A SER   A 1 74  ? 5.861  12.849  8.777  0.50 21.65  ? 80  SER   A O   1 
ATOM   596  O  O   B SER   A 1 74  ? 5.732  12.802  8.936  0.50 21.62  ? 80  SER   A O   1 
ATOM   597  C  CB  A SER   A 1 74  ? 3.018  11.218  7.762  0.50 22.91  ? 80  SER   A CB  1 
ATOM   598  C  CB  B SER   A 1 74  ? 3.004  11.201  7.629  0.50 23.73  ? 80  SER   A CB  1 
ATOM   599  O  OG  A SER   A 1 74  ? 2.650  9.876   7.485  0.50 26.71  ? 80  SER   A OG  1 
ATOM   600  O  OG  B SER   A 1 74  ? 2.486  10.265  6.699  0.50 28.28  ? 80  SER   A OG  1 
ATOM   601  N  N   . LEU   A 1 75  ? 4.159  13.981  7.813  1.00 22.12  ? 81  LEU   A N   1 
ATOM   602  C  CA  . LEU   A 1 75  ? 4.409  15.252  8.464  1.00 22.96  ? 81  LEU   A CA  1 
ATOM   603  C  C   . LEU   A 1 75  ? 3.471  15.271  9.678  1.00 24.21  ? 81  LEU   A C   1 
ATOM   604  O  O   . LEU   A 1 75  ? 2.226  15.208  9.522  1.00 24.99  ? 81  LEU   A O   1 
ATOM   605  C  CB  . LEU   A 1 75  ? 4.034  16.363  7.473  1.00 23.45  ? 81  LEU   A CB  1 
ATOM   606  C  CG  . LEU   A 1 75  ? 4.494  17.775  7.828  1.00 25.86  ? 81  LEU   A CG  1 
ATOM   607  C  CD1 . LEU   A 1 75  ? 5.992  17.876  7.989  1.00 24.95  ? 81  LEU   A CD1 1 
ATOM   608  C  CD2 . LEU   A 1 75  ? 4.006  18.797  6.803  1.00 28.14  ? 81  LEU   A CD2 1 
ATOM   609  N  N   . ILE   A 1 76  ? 4.050  15.276  10.876 1.00 23.86  ? 82  ILE   A N   1 
ATOM   610  C  CA  . ILE   A 1 76  ? 3.305  15.142  12.133 1.00 25.12  ? 82  ILE   A CA  1 
ATOM   611  C  C   . ILE   A 1 76  ? 3.656  16.240  13.130 1.00 24.97  ? 82  ILE   A C   1 
ATOM   612  O  O   . ILE   A 1 76  ? 4.825  16.602  13.242 1.00 23.37  ? 82  ILE   A O   1 
ATOM   613  C  CB  . ILE   A 1 76  ? 3.601  13.730  12.723 1.00 27.59  ? 82  ILE   A CB  1 
ATOM   614  C  CG1 . ILE   A 1 76  ? 2.972  12.622  11.856 1.00 30.11  ? 82  ILE   A CG1 1 
ATOM   615  C  CG2 . ILE   A 1 76  ? 3.151  13.603  14.201 1.00 28.42  ? 82  ILE   A CG2 1 
ATOM   616  C  CD1 . ILE   A 1 76  ? 3.386  11.237  12.286 1.00 31.73  ? 82  ILE   A CD1 1 
ATOM   617  N  N   . PHE   A 1 77  ? 2.644  16.819  13.812 1.00 25.31  ? 83  PHE   A N   1 
ATOM   618  C  CA  . PHE   A 1 77  ? 2.925  17.856  14.799 1.00 25.62  ? 83  PHE   A CA  1 
ATOM   619  C  C   . PHE   A 1 77  ? 3.550  17.213  16.055 1.00 24.90  ? 83  PHE   A C   1 
ATOM   620  O  O   . PHE   A 1 77  ? 3.055  16.185  16.558 1.00 25.80  ? 83  PHE   A O   1 
ATOM   621  C  CB  . PHE   A 1 77  ? 1.653  18.657  15.145 1.00 27.41  ? 83  PHE   A CB  1 
ATOM   622  C  CG  . PHE   A 1 77  ? 2.001  19.953  15.830 1.00 30.93  ? 83  PHE   A CG  1 
ATOM   623  C  CD1 . PHE   A 1 77  ? 2.587  20.993  15.124 1.00 32.94  ? 83  PHE   A CD1 1 
ATOM   624  C  CD2 . PHE   A 1 77  ? 1.811  20.108  17.193 1.00 33.46  ? 83  PHE   A CD2 1 
ATOM   625  C  CE1 . PHE   A 1 77  ? 2.910  22.186  15.752 1.00 34.48  ? 83  PHE   A CE1 1 
ATOM   626  C  CE2 . PHE   A 1 77  ? 2.173  21.295  17.827 1.00 34.70  ? 83  PHE   A CE2 1 
ATOM   627  C  CZ  . PHE   A 1 77  ? 2.692  22.330  17.099 1.00 34.85  ? 83  PHE   A CZ  1 
ATOM   628  N  N   . VAL   A 1 78  ? 4.704  17.781  16.497 1.00 23.08  ? 84  VAL   A N   1 
ATOM   629  C  CA  . VAL   A 1 78  ? 5.429  17.296  17.664 1.00 23.28  ? 84  VAL   A CA  1 
ATOM   630  C  C   . VAL   A 1 78  ? 5.506  18.413  18.700 1.00 24.30  ? 84  VAL   A C   1 
ATOM   631  O  O   . VAL   A 1 78  ? 6.003  19.502  18.393 1.00 24.28  ? 84  VAL   A O   1 
ATOM   632  C  CB  . VAL   A 1 78  ? 6.858  16.810  17.252 1.00 23.01  ? 84  VAL   A CB  1 
ATOM   633  C  CG1 . VAL   A 1 78  ? 7.676  16.445  18.486 1.00 22.99  ? 84  VAL   A CG1 1 
ATOM   634  C  CG2 . VAL   A 1 78  ? 6.777  15.618  16.311 1.00 23.53  ? 84  VAL   A CG2 1 
ATOM   635  N  N   . GLU   A 1 79  ? 5.054  18.138  19.937 1.00 24.94  ? 85  GLU   A N   1 
ATOM   636  C  CA  . GLU   A 1 79  ? 5.087  19.134  21.010 1.00 25.71  ? 85  GLU   A CA  1 
ATOM   637  C  C   . GLU   A 1 79  ? 6.495  19.635  21.378 1.00 26.19  ? 85  GLU   A C   1 
ATOM   638  O  O   . GLU   A 1 79  ? 7.482  18.934  21.161 1.00 24.59  ? 85  GLU   A O   1 
ATOM   639  C  CB  . GLU   A 1 79  ? 4.407  18.557  22.268 1.00 28.86  ? 85  GLU   A CB  1 
ATOM   640  C  CG  . GLU   A 1 79  ? 2.929  18.290  22.065 1.00 33.43  ? 85  GLU   A CG  1 
ATOM   641  C  CD  . GLU   A 1 79  ? 2.094  19.528  21.784 1.00 41.96  ? 85  GLU   A CD  1 
ATOM   642  O  OE1 . GLU   A 1 79  ? 2.425  20.617  22.307 1.00 43.93  ? 85  GLU   A OE1 1 
ATOM   643  O  OE2 . GLU   A 1 79  ? 1.109  19.410  21.021 1.00 43.60  ? 85  GLU   A OE2 1 
ATOM   644  N  N   . ALA   A 1 80  ? 6.581  20.821  22.025 1.00 26.85  ? 86  ALA   A N   1 
ATOM   645  C  CA  . ALA   A 1 80  ? 7.870  21.353  22.466 1.00 28.34  ? 86  ALA   A CA  1 
ATOM   646  C  C   . ALA   A 1 80  ? 8.569  20.388  23.434 1.00 28.37  ? 86  ALA   A C   1 
ATOM   647  O  O   . ALA   A 1 80  ? 7.913  19.692  24.215 1.00 28.90  ? 86  ALA   A O   1 
ATOM   648  C  CB  . ALA   A 1 80  ? 7.671  22.700  23.142 1.00 28.61  ? 86  ALA   A CB  1 
ATOM   649  N  N   . SER   A 1 81  ? 9.892  20.333  23.329 1.00 27.62  ? 87  SER   A N   1 
ATOM   650  C  CA  . SER   A 1 81  ? 10.734 19.485  24.155 1.00 27.03  ? 87  SER   A CA  1 
ATOM   651  C  C   . SER   A 1 81  ? 11.967 20.287  24.630 1.00 28.16  ? 87  SER   A C   1 
ATOM   652  O  O   . SER   A 1 81  ? 12.066 21.485  24.364 1.00 29.21  ? 87  SER   A O   1 
ATOM   653  C  CB  . SER   A 1 81  ? 11.178 18.268  23.339 1.00 26.71  ? 87  SER   A CB  1 
ATOM   654  O  OG  . SER   A 1 81  ? 12.151 18.640  22.366 1.00 26.77  ? 87  SER   A OG  1 
ATOM   655  N  N   . GLU   A 1 82  ? 12.943 19.611  25.253 1.00 28.47  ? 88  GLU   A N   1 
ATOM   656  C  CA  . GLU   A 1 82  ? 14.190 20.249  25.649 1.00 29.35  ? 88  GLU   A CA  1 
ATOM   657  C  C   . GLU   A 1 82  ? 15.020 20.697  24.441 1.00 28.76  ? 88  GLU   A C   1 
ATOM   658  O  O   . GLU   A 1 82  ? 15.805 21.637  24.570 1.00 29.28  ? 88  GLU   A O   1 
ATOM   659  C  CB  . GLU   A 1 82  ? 15.019 19.269  26.505 1.00 33.60  ? 88  GLU   A CB  1 
ATOM   660  C  CG  . GLU   A 1 82  ? 14.519 19.185  27.940 1.00 41.75  ? 88  GLU   A CG  1 
ATOM   661  C  CD  . GLU   A 1 82  ? 15.387 18.371  28.882 1.00 52.62  ? 88  GLU   A CD  1 
ATOM   662  O  OE1 . GLU   A 1 82  ? 15.003 18.245  30.068 1.00 56.23  ? 88  GLU   A OE1 1 
ATOM   663  O  OE2 . GLU   A 1 82  ? 16.443 17.856  28.442 1.00 54.30  ? 88  GLU   A OE2 1 
ATOM   664  N  N   . TYR   A 1 83  ? 14.842 20.061  23.259 1.00 26.95  ? 89  TYR   A N   1 
ATOM   665  C  CA  . TYR   A 1 83  ? 15.691 20.337  22.099 1.00 26.73  ? 89  TYR   A CA  1 
ATOM   666  C  C   . TYR   A 1 83  ? 15.060 21.064  20.898 1.00 26.00  ? 89  TYR   A C   1 
ATOM   667  O  O   . TYR   A 1 83  ? 15.801 21.553  20.050 1.00 27.01  ? 89  TYR   A O   1 
ATOM   668  C  CB  . TYR   A 1 83  ? 16.305 19.012  21.620 1.00 27.32  ? 89  TYR   A CB  1 
ATOM   669  C  CG  . TYR   A 1 83  ? 17.347 18.475  22.577 1.00 29.89  ? 89  TYR   A CG  1 
ATOM   670  C  CD1 . TYR   A 1 83  ? 18.682 18.827  22.451 1.00 31.12  ? 89  TYR   A CD1 1 
ATOM   671  C  CD2 . TYR   A 1 83  ? 16.999 17.596  23.595 1.00 32.01  ? 89  TYR   A CD2 1 
ATOM   672  C  CE1 . TYR   A 1 83  ? 19.644 18.330  23.320 1.00 33.18  ? 89  TYR   A CE1 1 
ATOM   673  C  CE2 . TYR   A 1 83  ? 17.952 17.112  24.489 1.00 33.38  ? 89  TYR   A CE2 1 
ATOM   674  C  CZ  . TYR   A 1 83  ? 19.277 17.472  24.337 1.00 35.31  ? 89  TYR   A CZ  1 
ATOM   675  O  OH  . TYR   A 1 83  ? 20.227 17.001  25.222 1.00 38.99  ? 89  TYR   A OH  1 
ATOM   676  N  N   . TYR   A 1 84  ? 13.737 21.135  20.806 1.00 24.36  ? 90  TYR   A N   1 
ATOM   677  C  CA  . TYR   A 1 84  ? 13.066 21.869  19.726 1.00 24.16  ? 90  TYR   A CA  1 
ATOM   678  C  C   . TYR   A 1 84  ? 11.811 22.529  20.270 1.00 25.40  ? 90  TYR   A C   1 
ATOM   679  O  O   . TYR   A 1 84  ? 11.107 21.933  21.093 1.00 26.46  ? 90  TYR   A O   1 
ATOM   680  C  CB  . TYR   A 1 84  ? 12.590 20.942  18.558 1.00 22.81  ? 90  TYR   A CB  1 
ATOM   681  C  CG  . TYR   A 1 84  ? 13.662 20.122  17.874 1.00 21.79  ? 90  TYR   A CG  1 
ATOM   682  C  CD1 . TYR   A 1 84  ? 14.439 20.662  16.851 1.00 21.74  ? 90  TYR   A CD1 1 
ATOM   683  C  CD2 . TYR   A 1 84  ? 13.834 18.779  18.177 1.00 21.88  ? 90  TYR   A CD2 1 
ATOM   684  C  CE1 . TYR   A 1 84  ? 15.409 19.906  16.205 1.00 21.59  ? 90  TYR   A CE1 1 
ATOM   685  C  CE2 . TYR   A 1 84  ? 14.799 18.017  17.543 1.00 21.62  ? 90  TYR   A CE2 1 
ATOM   686  C  CZ  . TYR   A 1 84  ? 15.565 18.571  16.531 1.00 22.02  ? 90  TYR   A CZ  1 
ATOM   687  O  OH  . TYR   A 1 84  ? 16.525 17.810  15.898 1.00 21.08  ? 90  TYR   A OH  1 
ATOM   688  N  N   . PRO   A 1 85  ? 11.431 23.706  19.739 1.00 26.07  ? 91  PRO   A N   1 
ATOM   689  C  CA  . PRO   A 1 85  ? 10.087 24.222  20.046 1.00 26.35  ? 91  PRO   A CA  1 
ATOM   690  C  C   . PRO   A 1 85  ? 9.011  23.367  19.337 1.00 25.87  ? 91  PRO   A C   1 
ATOM   691  O  O   . PRO   A 1 85  ? 9.328  22.511  18.493 1.00 25.33  ? 91  PRO   A O   1 
ATOM   692  C  CB  . PRO   A 1 85  ? 10.121 25.650  19.456 1.00 27.57  ? 91  PRO   A CB  1 
ATOM   693  C  CG  . PRO   A 1 85  ? 11.030 25.536  18.285 1.00 28.08  ? 91  PRO   A CG  1 
ATOM   694  C  CD  . PRO   A 1 85  ? 12.106 24.515  18.701 1.00 25.86  ? 91  PRO   A CD  1 
ATOM   695  N  N   . ALA   A 1 86  ? 7.721  23.606  19.622 1.00 25.38  ? 92  ALA   A N   1 
ATOM   696  C  CA  . ALA   A 1 86  ? 6.639  22.870  18.948 1.00 25.70  ? 92  ALA   A CA  1 
ATOM   697  C  C   . ALA   A 1 86  ? 6.711  23.120  17.446 1.00 25.57  ? 92  ALA   A C   1 
ATOM   698  O  O   . ALA   A 1 86  ? 6.894  24.269  17.021 1.00 26.82  ? 92  ALA   A O   1 
ATOM   699  C  CB  . ALA   A 1 86  ? 5.285  23.302  19.491 1.00 26.39  ? 92  ALA   A CB  1 
ATOM   700  N  N   . ARG   A 1 87  ? 6.670  22.051  16.647 1.00 23.90  ? 93  ARG   A N   1 
ATOM   701  C  CA  . ARG   A 1 87  ? 6.816  22.191  15.189 1.00 22.80  ? 93  ARG   A CA  1 
ATOM   702  C  C   . ARG   A 1 87  ? 6.296  20.931  14.505 1.00 23.39  ? 93  ARG   A C   1 
ATOM   703  O  O   . ARG   A 1 87  ? 6.060  19.913  15.174 1.00 24.90  ? 93  ARG   A O   1 
ATOM   704  C  CB  . ARG   A 1 87  ? 8.334  22.343  14.850 1.00 22.71  ? 93  ARG   A CB  1 
ATOM   705  C  CG  . ARG   A 1 87  ? 9.110  21.000  14.919 1.00 23.94  ? 93  ARG   A CG  1 
ATOM   706  C  CD  . ARG   A 1 87  ? 10.545 21.138  15.331 1.00 23.10  ? 93  ARG   A CD  1 
ATOM   707  N  NE  . ARG   A 1 87  ? 11.408 20.059  14.816 1.00 21.89  ? 93  ARG   A NE  1 
ATOM   708  C  CZ  . ARG   A 1 87  ? 11.401 18.794  15.241 1.00 22.92  ? 93  ARG   A CZ  1 
ATOM   709  N  NH1 . ARG   A 1 87  ? 12.269 17.920  14.742 1.00 22.10  ? 93  ARG   A NH1 1 
ATOM   710  N  NH2 . ARG   A 1 87  ? 10.576 18.414  16.225 1.00 21.06  ? 93  ARG   A NH2 1 
ATOM   711  N  N   . TYR   A 1 88  ? 6.215  20.948  13.165 1.00 22.54  ? 94  TYR   A N   1 
ATOM   712  C  CA  . TYR   A 1 88  ? 5.924  19.740  12.424 1.00 23.26  ? 94  TYR   A CA  1 
ATOM   713  C  C   . TYR   A 1 88  ? 7.242  19.045  12.089 1.00 21.87  ? 94  TYR   A C   1 
ATOM   714  O  O   . TYR   A 1 88  ? 8.185  19.663  11.577 1.00 22.71  ? 94  TYR   A O   1 
ATOM   715  C  CB  . TYR   A 1 88  ? 5.222  20.080  11.115 1.00 24.59  ? 94  TYR   A CB  1 
ATOM   716  C  CG  . TYR   A 1 88  ? 3.778  20.466  11.333 1.00 26.24  ? 94  TYR   A CG  1 
ATOM   717  C  CD1 . TYR   A 1 88  ? 2.787  19.504  11.394 1.00 27.81  ? 94  TYR   A CD1 1 
ATOM   718  C  CD2 . TYR   A 1 88  ? 3.417  21.790  11.544 1.00 28.48  ? 94  TYR   A CD2 1 
ATOM   719  C  CE1 . TYR   A 1 88  ? 1.456  19.850  11.596 1.00 30.15  ? 94  TYR   A CE1 1 
ATOM   720  C  CE2 . TYR   A 1 88  ? 2.086  22.154  11.738 1.00 30.04  ? 94  TYR   A CE2 1 
ATOM   721  C  CZ  . TYR   A 1 88  ? 1.113  21.174  11.794 1.00 31.44  ? 94  TYR   A CZ  1 
ATOM   722  O  OH  . TYR   A 1 88  ? -0.209 21.505  12.005 1.00 34.42  ? 94  TYR   A OH  1 
ATOM   723  N  N   . GLN   A 1 89  ? 7.282  17.718  12.341 1.00 19.94  ? 95  GLN   A N   1 
ATOM   724  C  CA  . GLN   A 1 89  ? 8.446  16.894  12.002 1.00 19.77  ? 95  GLN   A CA  1 
ATOM   725  C  C   . GLN   A 1 89  ? 8.048  16.045  10.785 1.00 19.65  ? 95  GLN   A C   1 
ATOM   726  O  O   . GLN   A 1 89  ? 6.959  15.437  10.780 1.00 20.50  ? 95  GLN   A O   1 
ATOM   727  C  CB  . GLN   A 1 89  ? 8.858  15.997  13.191 1.00 19.50  ? 95  GLN   A CB  1 
ATOM   728  C  CG  . GLN   A 1 89  ? 10.086 15.099  12.848 1.00 20.20  ? 95  GLN   A CG  1 
ATOM   729  C  CD  . GLN   A 1 89  ? 10.831 14.550  14.053 1.00 18.85  ? 95  GLN   A CD  1 
ATOM   730  O  OE1 . GLN   A 1 89  ? 10.991 15.217  15.066 1.00 20.22  ? 95  GLN   A OE1 1 
ATOM   731  N  NE2 . GLN   A 1 89  ? 11.314 13.291  13.943 1.00 19.17  ? 95  GLN   A NE2 1 
ATOM   732  N  N   . SER   A 1 90  ? 8.893  16.033  9.748  1.00 19.38  ? 96  SER   A N   1 
ATOM   733  C  CA  . SER   A 1 90  ? 8.641  15.292  8.521  1.00 19.43  ? 96  SER   A CA  1 
ATOM   734  C  C   . SER   A 1 90  ? 9.290  13.884  8.549  1.00 18.51  ? 96  SER   A C   1 
ATOM   735  O  O   . SER   A 1 90  ? 10.165 13.601  9.391  1.00 19.15  ? 96  SER   A O   1 
ATOM   736  C  CB  . SER   A 1 90  ? 9.150  16.073  7.318  1.00 20.07  ? 96  SER   A CB  1 
ATOM   737  O  OG  . SER   A 1 90  ? 10.569 16.199  7.380  1.00 21.87  ? 96  SER   A OG  1 
ATOM   738  N  N   . HIS   A 1 91  ? 8.795  12.995  7.652  1.00 17.60  ? 97  HIS   A N   1 
ATOM   739  C  CA  . HIS   A 1 91  ? 9.298  11.625  7.512  1.00 17.29  ? 97  HIS   A CA  1 
ATOM   740  C  C   . HIS   A 1 91  ? 9.187  10.859  8.843  1.00 17.19  ? 97  HIS   A C   1 
ATOM   741  O  O   . HIS   A 1 91  ? 10.029 10.015  9.100  1.00 17.10  ? 97  HIS   A O   1 
ATOM   742  C  CB  . HIS   A 1 91  ? 10.760 11.651  6.967  1.00 18.41  ? 97  HIS   A CB  1 
ATOM   743  C  CG  . HIS   A 1 91  ? 10.870 12.327  5.620  1.00 21.67  ? 97  HIS   A CG  1 
ATOM   744  N  ND1 . HIS   A 1 91  ? 10.820 11.602  4.441  1.00 25.04  ? 97  HIS   A ND1 1 
ATOM   745  C  CD2 . HIS   A 1 91  ? 10.983 13.648  5.316  1.00 22.40  ? 97  HIS   A CD2 1 
ATOM   746  C  CE1 . HIS   A 1 91  ? 10.922 12.497  3.459  1.00 25.31  ? 97  HIS   A CE1 1 
ATOM   747  N  NE2 . HIS   A 1 91  ? 10.999 13.743  3.932  1.00 23.91  ? 97  HIS   A NE2 1 
ATOM   748  N  N   . LEU   A 1 92  ? 8.106  11.100  9.622  1.00 17.87  ? 98  LEU   A N   1 
ATOM   749  C  CA  . LEU   A 1 92  ? 7.942  10.462  10.946 1.00 18.29  ? 98  LEU   A CA  1 
ATOM   750  C  C   . LEU   A 1 92  ? 6.889  9.330   10.873 1.00 18.61  ? 98  LEU   A C   1 
ATOM   751  O  O   . LEU   A 1 92  ? 5.855  9.497   10.214 1.00 19.68  ? 98  LEU   A O   1 
ATOM   752  C  CB  . LEU   A 1 92  ? 7.498  11.536  11.968 1.00 18.94  ? 98  LEU   A CB  1 
ATOM   753  C  CG  . LEU   A 1 92  ? 7.422  11.090  13.466 1.00 20.12  ? 98  LEU   A CG  1 
ATOM   754  C  CD1 . LEU   A 1 92  ? 8.784  10.715  13.972 1.00 20.10  ? 98  LEU   A CD1 1 
ATOM   755  C  CD2 . LEU   A 1 92  ? 6.867  12.230  14.334 1.00 21.92  ? 98  LEU   A CD2 1 
ATOM   756  N  N   . MET   A 1 93  ? 7.165  8.189   11.549 1.00 16.94  ? 99  MET   A N   1 
ATOM   757  C  CA  . MET   A 1 93  ? 6.226  7.064   11.565 1.00 16.41  ? 99  MET   A CA  1 
ATOM   758  C  C   . MET   A 1 93  ? 5.829  6.820   13.022 1.00 17.20  ? 99  MET   A C   1 
ATOM   759  O  O   . MET   A 1 93  ? 6.710  6.850   13.881 1.00 18.01  ? 99  MET   A O   1 
ATOM   760  C  CB  . MET   A 1 93  ? 6.967  5.815   11.030 1.00 16.90  ? 99  MET   A CB  1 
ATOM   761  C  CG  . MET   A 1 93  ? 7.430  5.982   9.546  1.00 18.56  ? 99  MET   A CG  1 
ATOM   762  S  SD  . MET   A 1 93  ? 8.514  4.674   9.020  1.00 21.88  ? 99  MET   A SD  1 
ATOM   763  C  CE  . MET   A 1 93  ? 9.860  4.920   10.075 1.00 23.51  ? 99  MET   A CE  1 
ATOM   764  N  N   . LEU   A 1 94  ? 4.537  6.557   13.312 1.00 17.00  ? 100 LEU   A N   1 
ATOM   765  C  CA  . LEU   A 1 94  ? 4.124  6.309   14.700 1.00 16.90  ? 100 LEU   A CA  1 
ATOM   766  C  C   . LEU   A 1 94  ? 3.682  4.839   14.882 1.00 16.54  ? 100 LEU   A C   1 
ATOM   767  O  O   . LEU   A 1 94  ? 3.168  4.217   13.953 1.00 18.41  ? 100 LEU   A O   1 
ATOM   768  C  CB  . LEU   A 1 94  ? 2.897  7.175   15.139 1.00 17.98  ? 100 LEU   A CB  1 
ATOM   769  C  CG  . LEU   A 1 94  ? 3.090  8.686   15.080 1.00 20.25  ? 100 LEU   A CG  1 
ATOM   770  C  CD1 . LEU   A 1 94  ? 1.846  9.415   15.629 1.00 22.76  ? 100 LEU   A CD1 1 
ATOM   771  C  CD2 . LEU   A 1 94  ? 4.351  9.134   15.804 1.00 21.36  ? 100 LEU   A CD2 1 
ATOM   772  N  N   . ALA   A 1 95  ? 3.829  4.371   16.091 1.00 16.87  ? 101 ALA   A N   1 
ATOM   773  C  CA  . ALA   A 1 95  ? 3.334  3.056   16.532 1.00 16.49  ? 101 ALA   A CA  1 
ATOM   774  C  C   . ALA   A 1 95  ? 2.832  3.182   17.976 1.00 16.71  ? 101 ALA   A C   1 
ATOM   775  O  O   . ALA   A 1 95  ? 3.163  4.158   18.682 1.00 17.23  ? 101 ALA   A O   1 
ATOM   776  C  CB  . ALA   A 1 95  ? 4.476  2.027   16.500 1.00 16.14  ? 101 ALA   A CB  1 
ATOM   777  N  N   . VAL   A 1 96  ? 1.962  2.254   18.375 1.00 16.28  ? 102 VAL   A N   1 
ATOM   778  C  CA  . VAL   A 1 96  ? 1.535  2.168   19.748 1.00 16.34  ? 102 VAL   A CA  1 
ATOM   779  C  C   . VAL   A 1 96  ? 2.616  1.428   20.515 1.00 18.35  ? 102 VAL   A C   1 
ATOM   780  O  O   . VAL   A 1 96  ? 2.880  0.231   20.290 1.00 19.98  ? 102 VAL   A O   1 
ATOM   781  C  CB  . VAL   A 1 96  ? 0.141  1.495   19.855 1.00 17.18  ? 102 VAL   A CB  1 
ATOM   782  C  CG1 . VAL   A 1 96  ? -0.292 1.360   21.316 1.00 18.12  ? 102 VAL   A CG1 1 
ATOM   783  C  CG2 . VAL   A 1 96  ? -0.879 2.337   19.097 1.00 18.11  ? 102 VAL   A CG2 1 
ATOM   784  N  N   . GLY   A 1 97  ? 3.257  2.153   21.417 1.00 18.83  ? 103 GLY   A N   1 
ATOM   785  C  CA  . GLY   A 1 97  ? 4.341  1.561   22.206 1.00 20.17  ? 103 GLY   A CA  1 
ATOM   786  C  C   . GLY   A 1 97  ? 4.957  2.557   23.158 1.00 20.26  ? 103 GLY   A C   1 
ATOM   787  O  O   . GLY   A 1 97  ? 4.588  3.736   23.167 1.00 20.78  ? 103 GLY   A O   1 
ATOM   788  N  N   . HIS   A 1 98  ? 5.915  2.069   23.979 1.00 19.50  ? 104 HIS   A N   1 
ATOM   789  C  CA  . HIS   A 1 98  ? 6.531  2.913   24.992 1.00 19.61  ? 104 HIS   A CA  1 
ATOM   790  C  C   . HIS   A 1 98  ? 7.786  3.646   24.512 1.00 19.22  ? 104 HIS   A C   1 
ATOM   791  O  O   . HIS   A 1 98  ? 8.612  3.053   23.865 1.00 18.76  ? 104 HIS   A O   1 
ATOM   792  C  CB  . HIS   A 1 98  ? 6.865  2.069   26.250 1.00 20.59  ? 104 HIS   A CB  1 
ATOM   793  C  CG  . HIS   A 1 98  ? 7.363  2.916   27.384 1.00 23.42  ? 104 HIS   A CG  1 
ATOM   794  N  ND1 . HIS   A 1 98  ? 6.518  3.794   28.042 1.00 26.22  ? 104 HIS   A ND1 1 
ATOM   795  C  CD2 . HIS   A 1 98  ? 8.623  3.086   27.859 1.00 24.45  ? 104 HIS   A CD2 1 
ATOM   796  C  CE1 . HIS   A 1 98  ? 7.276  4.431   28.927 1.00 26.18  ? 104 HIS   A CE1 1 
ATOM   797  N  NE2 . HIS   A 1 98  ? 8.552  4.028   28.852 1.00 25.43  ? 104 HIS   A NE2 1 
ATOM   798  N  N   . SER   A 1 99  ? 7.951  4.922   24.861 1.00 19.62  ? 105 SER   A N   1 
ATOM   799  C  CA  . SER   A 1 99  ? 9.089  5.748   24.476 1.00 20.23  ? 105 SER   A CA  1 
ATOM   800  C  C   . SER   A 1 99  ? 9.327  6.836   25.529 1.00 21.53  ? 105 SER   A C   1 
ATOM   801  O  O   . SER   A 1 99  ? 8.370  7.504   25.904 1.00 23.57  ? 105 SER   A O   1 
ATOM   802  C  CB  . SER   A 1 99  ? 8.788  6.429   23.121 1.00 23.84  ? 105 SER   A CB  1 
ATOM   803  O  OG  . SER   A 1 99  ? 9.877  7.189   22.626 1.00 30.63  ? 105 SER   A OG  1 
ATOM   804  N  N   . GLU   A 1 100 ? 10.595 7.044   25.956 1.00 20.52  ? 106 GLU   A N   1 
ATOM   805  C  CA  . GLU   A 1 100 ? 11.040 8.153   26.818 1.00 21.33  ? 106 GLU   A CA  1 
ATOM   806  C  C   . GLU   A 1 100 ? 12.170 8.860   26.087 1.00 21.67  ? 106 GLU   A C   1 
ATOM   807  O  O   . GLU   A 1 100 ? 12.763 8.284   25.165 1.00 20.80  ? 106 GLU   A O   1 
ATOM   808  C  CB  . GLU   A 1 100 ? 11.492 7.630   28.208 1.00 23.01  ? 106 GLU   A CB  1 
ATOM   809  C  CG  . GLU   A 1 100 ? 10.382 6.885   28.922 1.00 25.12  ? 106 GLU   A CG  1 
ATOM   810  C  CD  . GLU   A 1 100 ? 10.716 6.302   30.288 1.00 31.01  ? 106 GLU   A CD  1 
ATOM   811  O  OE1 . GLU   A 1 100 ? 11.658 6.813   30.930 1.00 32.45  ? 106 GLU   A OE1 1 
ATOM   812  O  OE2 . GLU   A 1 100 ? 10.056 5.325   30.702 1.00 29.41  ? 106 GLU   A OE2 1 
ATOM   813  N  N   . PRO   A 1 101 ? 12.463 10.145  26.391 1.00 22.15  ? 107 PRO   A N   1 
ATOM   814  C  CA  . PRO   A 1 101 ? 13.493 10.861  25.619 1.00 21.88  ? 107 PRO   A CA  1 
ATOM   815  C  C   . PRO   A 1 101 ? 14.811 10.115  25.396 1.00 21.56  ? 107 PRO   A C   1 
ATOM   816  O  O   . PRO   A 1 101 ? 15.336 10.121  24.285 1.00 21.05  ? 107 PRO   A O   1 
ATOM   817  C  CB  . PRO   A 1 101 ? 13.694 12.166  26.408 1.00 23.27  ? 107 PRO   A CB  1 
ATOM   818  C  CG  . PRO   A 1 101 ? 12.335 12.419  27.033 1.00 23.43  ? 107 PRO   A CG  1 
ATOM   819  C  CD  . PRO   A 1 101 ? 11.821 11.021  27.406 1.00 22.44  ? 107 PRO   A CD  1 
ATOM   820  N  N   . GLY   A 1 102 ? 15.339 9.461   26.433 1.00 20.61  ? 108 GLY   A N   1 
ATOM   821  C  CA  . GLY   A 1 102 ? 16.599 8.731   26.320 1.00 21.01  ? 108 GLY   A CA  1 
ATOM   822  C  C   . GLY   A 1 102 ? 16.518 7.474   25.466 1.00 20.17  ? 108 GLY   A C   1 
ATOM   823  O  O   . GLY   A 1 102 ? 17.545 6.866   25.174 1.00 20.85  ? 108 GLY   A O   1 
ATOM   824  N  N   . ASP   A 1 103 ? 15.307 7.077   25.041 1.00 18.94  ? 109 ASP   A N   1 
ATOM   825  C  CA  . ASP   A 1 103 ? 15.132 5.975   24.090 1.00 17.41  ? 109 ASP   A CA  1 
ATOM   826  C  C   . ASP   A 1 103 ? 15.454 6.393   22.657 1.00 17.50  ? 109 ASP   A C   1 
ATOM   827  O  O   . ASP   A 1 103 ? 15.592 5.521   21.791 1.00 17.62  ? 109 ASP   A O   1 
ATOM   828  C  CB  . ASP   A 1 103 ? 13.690 5.415   24.106 1.00 16.88  ? 109 ASP   A CB  1 
ATOM   829  C  CG  . ASP   A 1 103 ? 13.366 4.672   25.384 1.00 20.78  ? 109 ASP   A CG  1 
ATOM   830  O  OD1 . ASP   A 1 103 ? 14.241 4.009   25.900 1.00 19.96  ? 109 ASP   A OD1 1 
ATOM   831  O  OD2 . ASP   A 1 103 ? 12.207 4.755   25.845 1.00 19.83  ? 109 ASP   A OD2 1 
ATOM   832  N  N   . CYS   A 1 104 ? 15.606 7.723   22.369 1.00 16.71  ? 110 CYS   A N   1 
ATOM   833  C  CA  . CYS   A 1 104 ? 15.937 8.160   21.007 1.00 16.14  ? 110 CYS   A CA  1 
ATOM   834  C  C   . CYS   A 1 104 ? 17.228 7.498   20.548 1.00 17.09  ? 110 CYS   A C   1 
ATOM   835  O  O   . CYS   A 1 104 ? 18.201 7.472   21.306 1.00 18.69  ? 110 CYS   A O   1 
ATOM   836  C  CB  . CYS   A 1 104 ? 16.071 9.686   20.939 1.00 16.60  ? 110 CYS   A CB  1 
ATOM   837  S  SG  . CYS   A 1 104 ? 14.484 10.574  21.045 1.00 19.32  ? 110 CYS   A SG  1 
ATOM   838  N  N   . GLY   A 1 105 ? 17.260 7.052   19.292 1.00 15.74  ? 111 GLY   A N   1 
ATOM   839  C  CA  . GLY   A 1 105 ? 18.430 6.343   18.785 1.00 16.83  ? 111 GLY   A CA  1 
ATOM   840  C  C   . GLY   A 1 105 ? 18.190 4.844   18.674 1.00 16.81  ? 111 GLY   A C   1 
ATOM   841  O  O   . GLY   A 1 105 ? 18.947 4.128   17.984 1.00 18.03  ? 111 GLY   A O   1 
ATOM   842  N  N   . GLY   A 1 106 ? 17.186 4.319   19.417 1.00 16.48  ? 112 GLY   A N   1 
ATOM   843  C  CA  . GLY   A 1 106 ? 16.861 2.888   19.332 1.00 15.73  ? 112 GLY   A CA  1 
ATOM   844  C  C   . GLY   A 1 106 ? 16.439 2.535   17.905 1.00 16.30  ? 112 GLY   A C   1 
ATOM   845  O  O   . GLY   A 1 106 ? 15.667 3.266   17.291 1.00 16.86  ? 112 GLY   A O   1 
ATOM   846  N  N   . ILE   A 1 107 ? 16.958 1.409   17.371 1.00 16.02  ? 113 ILE   A N   1 
ATOM   847  C  CA  . ILE   A 1 107 ? 16.644 1.058   15.994 1.00 15.76  ? 113 ILE   A CA  1 
ATOM   848  C  C   . ILE   A 1 107 ? 15.288 0.368   15.847 1.00 15.23  ? 113 ILE   A C   1 
ATOM   849  O  O   . ILE   A 1 107 ? 14.954 -0.506  16.664 1.00 16.74  ? 113 ILE   A O   1 
ATOM   850  C  CB  . ILE   A 1 107 ? 17.809 0.213   15.411 1.00 18.67  ? 113 ILE   A CB  1 
ATOM   851  C  CG1 . ILE   A 1 107 ? 18.964 1.174   15.028 1.00 20.18  ? 113 ILE   A CG1 1 
ATOM   852  C  CG2 . ILE   A 1 107 ? 17.402 -0.572  14.147 1.00 20.32  ? 113 ILE   A CG2 1 
ATOM   853  C  CD1 . ILE   A 1 107 ? 20.323 0.497   14.690 1.00 22.76  ? 113 ILE   A CD1 1 
ATOM   854  N  N   . LEU   A 1 108 ? 14.589 0.694   14.722 1.00 14.90  ? 114 LEU   A N   1 
ATOM   855  C  CA  . LEU   A 1 108 ? 13.403 -0.049  14.265 1.00 15.44  ? 114 LEU   A CA  1 
ATOM   856  C  C   . LEU   A 1 108 ? 13.900 -0.808  13.020 1.00 17.06  ? 114 LEU   A C   1 
ATOM   857  O  O   . LEU   A 1 108 ? 14.508 -0.219  12.110 1.00 16.47  ? 114 LEU   A O   1 
ATOM   858  C  CB  . LEU   A 1 108 ? 12.309 0.954   13.853 1.00 14.89  ? 114 LEU   A CB  1 
ATOM   859  C  CG  . LEU   A 1 108 ? 11.110 0.367   13.085 1.00 16.02  ? 114 LEU   A CG  1 
ATOM   860  C  CD1 . LEU   A 1 108 ? 10.270 -0.528  14.014 1.00 16.49  ? 114 LEU   A CD1 1 
ATOM   861  C  CD2 . LEU   A 1 108 ? 10.219 1.552   12.518 1.00 16.43  ? 114 LEU   A CD2 1 
ATOM   862  N  N   . ARG   A 1 109 ? 13.645 -2.133  13.013 1.00 17.57  ? 115 ARG   A N   1 
ATOM   863  C  CA  . ARG   A 1 109 ? 14.043 -2.944  11.877 1.00 19.25  ? 115 ARG   A CA  1 
ATOM   864  C  C   . ARG   A 1 109 ? 12.971 -3.875  11.396 1.00 18.35  ? 115 ARG   A C   1 
ATOM   865  O  O   . ARG   A 1 109 ? 12.073 -4.282  12.127 1.00 17.84  ? 115 ARG   A O   1 
ATOM   866  C  CB  . ARG   A 1 109 ? 15.315 -3.739  12.151 1.00 23.29  ? 115 ARG   A CB  1 
ATOM   867  C  CG  . ARG   A 1 109 ? 15.498 -4.311  13.521 1.00 31.09  ? 115 ARG   A CG  1 
ATOM   868  C  CD  . ARG   A 1 109 ? 16.925 -4.889  13.610 1.00 36.43  ? 115 ARG   A CD  1 
ATOM   869  N  NE  . ARG   A 1 109 ? 17.807 -4.139  14.510 1.00 39.39  ? 115 ARG   A NE  1 
ATOM   870  C  CZ  . ARG   A 1 109 ? 19.056 -3.771  14.207 1.00 39.30  ? 115 ARG   A CZ  1 
ATOM   871  N  NH1 . ARG   A 1 109 ? 19.564 -4.035  13.005 1.00 36.92  ? 115 ARG   A NH1 1 
ATOM   872  N  NH2 . ARG   A 1 109 ? 19.800 -3.121  15.101 1.00 36.95  ? 115 ARG   A NH2 1 
ATOM   873  N  N   . CYS   A 1 110 ? 13.012 -4.113  10.095 1.00 18.67  ? 116 CYS   A N   1 
ATOM   874  C  CA  . CYS   A 1 110 ? 12.101 -5.076  9.453  1.00 20.32  ? 116 CYS   A CA  1 
ATOM   875  C  C   . CYS   A 1 110 ? 12.946 -6.231  8.847  1.00 22.58  ? 116 CYS   A C   1 
ATOM   876  O  O   . CYS   A 1 110 ? 14.187 -6.226  8.965  1.00 23.57  ? 116 CYS   A O   1 
ATOM   877  C  CB  . CYS   A 1 110 ? 11.276 -4.371  8.373  1.00 20.08  ? 116 CYS   A CB  1 
ATOM   878  S  SG  . CYS   A 1 110 ? 12.251 -3.839  6.927  1.00 20.52  ? 116 CYS   A SG  1 
ATOM   879  N  N   . GLN   A 1 111 ? 12.289 -7.160  8.110  1.00 24.54  ? 117 GLN   A N   1 
ATOM   880  C  CA  . GLN   A 1 111 ? 13.024 -8.234  7.449  1.00 26.79  ? 117 GLN   A CA  1 
ATOM   881  C  C   . GLN   A 1 111 ? 14.067 -7.744  6.440  1.00 27.52  ? 117 GLN   A C   1 
ATOM   882  O  O   . GLN   A 1 111 ? 14.993 -8.493  6.127  1.00 29.88  ? 117 GLN   A O   1 
ATOM   883  C  CB  . GLN   A 1 111 ? 12.036 -9.214  6.774  1.00 29.82  ? 117 GLN   A CB  1 
ATOM   884  C  CG  . GLN   A 1 111 ? 11.336 -8.641  5.542  1.00 33.35  ? 117 GLN   A CG  1 
ATOM   885  C  CD  . GLN   A 1 111 ? 10.334 -9.600  4.942  1.00 38.36  ? 117 GLN   A CD  1 
ATOM   886  O  OE1 . GLN   A 1 111 ? 9.129  -9.497  5.189  1.00 38.58  ? 117 GLN   A OE1 1 
ATOM   887  N  NE2 . GLN   A 1 111 ? 10.808 -10.528 4.112  1.00 39.28  ? 117 GLN   A NE2 1 
ATOM   888  N  N   . HIS   A 1 112 ? 13.973 -6.479  5.961  1.00 25.77  ? 118 HIS   A N   1 
ATOM   889  C  CA  . HIS   A 1 112 ? 14.895 -5.941  4.941  1.00 26.08  ? 118 HIS   A CA  1 
ATOM   890  C  C   . HIS   A 1 112 ? 16.089 -5.157  5.506  1.00 26.34  ? 118 HIS   A C   1 
ATOM   891  O  O   . HIS   A 1 112 ? 17.046 -4.846  4.773  1.00 28.11  ? 118 HIS   A O   1 
ATOM   892  C  CB  . HIS   A 1 112 ? 14.117 -5.082  3.902  1.00 25.98  ? 118 HIS   A CB  1 
ATOM   893  C  CG  . HIS   A 1 112 ? 12.935 -5.800  3.293  1.00 25.55  ? 118 HIS   A CG  1 
ATOM   894  N  ND1 . HIS   A 1 112 ? 11.644 -5.500  3.661  1.00 25.83  ? 118 HIS   A ND1 1 
ATOM   895  C  CD2 . HIS   A 1 112 ? 12.900 -6.754  2.323  1.00 27.08  ? 118 HIS   A CD2 1 
ATOM   896  C  CE1 . HIS   A 1 112 ? 10.856 -6.307  2.961  1.00 27.53  ? 118 HIS   A CE1 1 
ATOM   897  N  NE2 . HIS   A 1 112 ? 11.571 -7.095  2.151  1.00 28.37  ? 118 HIS   A NE2 1 
ATOM   898  N  N   . GLY   A 1 113 ? 16.040 -4.848  6.801  1.00 23.94  ? 119 GLY   A N   1 
ATOM   899  C  CA  . GLY   A 1 113 ? 17.112 -4.092  7.420  1.00 22.26  ? 119 GLY   A CA  1 
ATOM   900  C  C   . GLY   A 1 113 ? 16.594 -2.994  8.317  1.00 20.45  ? 119 GLY   A C   1 
ATOM   901  O  O   . GLY   A 1 113 ? 15.467 -3.073  8.819  1.00 20.25  ? 119 GLY   A O   1 
ATOM   902  N  N   . VAL   A 1 114 ? 17.432 -1.972  8.533  1.00 19.16  ? 120 VAL   A N   1 
ATOM   903  C  CA  . VAL   A 1 114 ? 17.088 -0.818  9.383  1.00 18.98  ? 120 VAL   A CA  1 
ATOM   904  C  C   . VAL   A 1 114 ? 16.113 0.081   8.698  1.00 18.72  ? 120 VAL   A C   1 
ATOM   905  O  O   . VAL   A 1 114 ? 16.334 0.490   7.548  1.00 19.22  ? 120 VAL   A O   1 
ATOM   906  C  CB  . VAL   A 1 114 ? 18.360 -0.028  9.759  1.00 18.87  ? 120 VAL   A CB  1 
ATOM   907  C  CG1 . VAL   A 1 114 ? 17.984 1.206   10.585 1.00 19.65  ? 120 VAL   A CG1 1 
ATOM   908  C  CG2 . VAL   A 1 114 ? 19.325 -0.920  10.531 1.00 20.73  ? 120 VAL   A CG2 1 
ATOM   909  N  N   . VAL   A 1 115 ? 14.972 0.350   9.376  1.00 16.50  ? 121 VAL   A N   1 
ATOM   910  C  CA  . VAL   A 1 115 ? 13.928 1.254   8.877  1.00 16.13  ? 121 VAL   A CA  1 
ATOM   911  C  C   . VAL   A 1 115 ? 14.129 2.699   9.362  1.00 16.45  ? 121 VAL   A C   1 
ATOM   912  O  O   . VAL   A 1 115 ? 13.868 3.645   8.644  1.00 18.03  ? 121 VAL   A O   1 
ATOM   913  C  CB  . VAL   A 1 115 ? 12.549 0.697   9.325  1.00 16.99  ? 121 VAL   A CB  1 
ATOM   914  C  CG1 . VAL   A 1 115 ? 11.379 1.615   8.938  1.00 17.11  ? 121 VAL   A CG1 1 
ATOM   915  C  CG2 . VAL   A 1 115 ? 12.340 -0.705  8.813  1.00 17.71  ? 121 VAL   A CG2 1 
ATOM   916  N  N   . GLY   A 1 116 ? 14.485 2.855   10.648 1.00 16.46  ? 122 GLY   A N   1 
ATOM   917  C  CA  . GLY   A 1 116 ? 14.647 4.180   11.240 1.00 16.54  ? 122 GLY   A CA  1 
ATOM   918  C  C   . GLY   A 1 116 ? 15.071 4.112   12.689 1.00 16.06  ? 122 GLY   A C   1 
ATOM   919  O  O   . GLY   A 1 116 ? 15.443 3.042   13.170 1.00 16.76  ? 122 GLY   A O   1 
ATOM   920  N  N   . ILE   A 1 117 ? 15.063 5.251   13.351 1.00 14.52  ? 123 ILE   A N   1 
ATOM   921  C  CA  . ILE   A 1 117 ? 15.432 5.321   14.773 1.00 14.29  ? 123 ILE   A CA  1 
ATOM   922  C  C   . ILE   A 1 117 ? 14.374 6.040   15.577 1.00 15.08  ? 123 ILE   A C   1 
ATOM   923  O  O   . ILE   A 1 117 ? 13.730 6.963   15.097 1.00 14.92  ? 123 ILE   A O   1 
ATOM   924  C  CB  . ILE   A 1 117 ? 16.816 6.025   14.970 1.00 15.96  ? 123 ILE   A CB  1 
ATOM   925  C  CG1 . ILE   A 1 117 ? 16.837 7.422   14.281 1.00 17.24  ? 123 ILE   A CG1 1 
ATOM   926  C  CG2 . ILE   A 1 117 ? 17.991 5.090   14.555 1.00 18.53  ? 123 ILE   A CG2 1 
ATOM   927  C  CD1 . ILE   A 1 117 ? 18.208 8.190   14.546 1.00 18.82  ? 123 ILE   A CD1 1 
ATOM   928  N  N   . VAL   A 1 118 ? 14.252 5.681   16.885 1.00 15.53  ? 124 VAL   A N   1 
ATOM   929  C  CA  . VAL   A 1 118 ? 13.281 6.350   17.760 1.00 15.08  ? 124 VAL   A CA  1 
ATOM   930  C  C   . VAL   A 1 118 ? 13.637 7.858   17.823 1.00 14.77  ? 124 VAL   A C   1 
ATOM   931  O  O   . VAL   A 1 118 ? 14.820 8.226   17.924 1.00 15.30  ? 124 VAL   A O   1 
ATOM   932  C  CB  . VAL   A 1 118 ? 13.359 5.757   19.182 1.00 15.65  ? 124 VAL   A CB  1 
ATOM   933  C  CG1 . VAL   A 1 118 ? 12.504 6.565   20.145 1.00 17.84  ? 124 VAL   A CG1 1 
ATOM   934  C  CG2 . VAL   A 1 118 ? 12.936 4.263   19.205 1.00 15.95  ? 124 VAL   A CG2 1 
ATOM   935  N  N   . SER   A 1 119 ? 12.615 8.694   17.716 1.00 13.61  ? 125 SER   A N   1 
ATOM   936  C  CA  . SER   A 1 119 ? 12.810 10.167  17.685 1.00 14.02  ? 125 SER   A CA  1 
ATOM   937  C  C   . SER   A 1 119 ? 11.807 10.900  18.544 1.00 16.50  ? 125 SER   A C   1 
ATOM   938  O  O   . SER   A 1 119 ? 12.132 11.997  19.045 1.00 17.99  ? 125 SER   A O   1 
ATOM   939  C  CB  . SER   A 1 119 ? 12.743 10.662  16.232 1.00 15.06  ? 125 SER   A CB  1 
ATOM   940  O  OG  . SER   A 1 119 ? 12.937 12.080  16.120 1.00 17.24  ? 125 SER   A OG  1 
ATOM   941  N  N   . THR   A 1 120 ? 10.565 10.357  18.700 1.00 16.92  ? 126 THR   A N   1 
ATOM   942  C  CA  . THR   A 1 120 ? 9.501  11.023  19.478 1.00 18.72  ? 126 THR   A CA  1 
ATOM   943  C  C   . THR   A 1 120 ? 8.745  10.041  20.397 1.00 18.56  ? 126 THR   A C   1 
ATOM   944  O  O   . THR   A 1 120 ? 8.925  8.812   20.303 1.00 17.63  ? 126 THR   A O   1 
ATOM   945  C  CB  . THR   A 1 120 ? 8.492  11.793  18.536 1.00 20.35  ? 126 THR   A CB  1 
ATOM   946  O  OG1 . THR   A 1 120 ? 7.657  10.838  17.887 1.00 21.22  ? 126 THR   A OG1 1 
ATOM   947  C  CG2 . THR   A 1 120 ? 9.155  12.711  17.535 1.00 19.87  ? 126 THR   A CG2 1 
ATOM   948  N  N   . GLY   A 1 121 ? 7.887  10.575  21.260 1.00 20.50  ? 127 GLY   A N   1 
ATOM   949  C  CA  . GLY   A 1 121 ? 7.068  9.751   22.123 1.00 21.94  ? 127 GLY   A CA  1 
ATOM   950  C  C   . GLY   A 1 121 ? 6.079  10.580  22.907 1.00 24.06  ? 127 GLY   A C   1 
ATOM   951  O  O   . GLY   A 1 121 ? 6.147  11.814  22.956 1.00 24.85  ? 127 GLY   A O   1 
ATOM   952  N  N   . GLY   A 1 122 ? 5.223  9.869   23.592 1.00 26.48  ? 128 GLY   A N   1 
ATOM   953  C  CA  . GLY   A 1 122 ? 4.245  10.480  24.479 1.00 27.76  ? 128 GLY   A CA  1 
ATOM   954  C  C   . GLY   A 1 122 ? 2.884  9.893   24.239 1.00 28.71  ? 128 GLY   A C   1 
ATOM   955  O  O   . GLY   A 1 122 ? 2.589  9.472   23.125 1.00 27.51  ? 128 GLY   A O   1 
ATOM   956  N  N   . ASN   A 1 123 ? 2.039  9.888   25.276 1.00 29.75  ? 129 ASN   A N   1 
ATOM   957  C  CA  . ASN   A 1 123 ? 0.655  9.427   25.147 1.00 30.58  ? 129 ASN   A CA  1 
ATOM   958  C  C   . ASN   A 1 123 ? 0.519  7.953   24.714 1.00 29.78  ? 129 ASN   A C   1 
ATOM   959  O  O   . ASN   A 1 123 ? -0.479 7.585   24.086 1.00 30.82  ? 129 ASN   A O   1 
ATOM   960  C  CB  . ASN   A 1 123 ? -0.109 10.360  24.190 1.00 32.82  ? 129 ASN   A CB  1 
ATOM   961  C  CG  . ASN   A 1 123 ? -0.240 11.784  24.696 1.00 38.31  ? 129 ASN   A CG  1 
ATOM   962  O  OD1 . ASN   A 1 123 ? -0.303 12.027  25.908 1.00 40.26  ? 129 ASN   A OD1 1 
ATOM   963  N  ND2 . ASN   A 1 123 ? -0.337 12.749  23.787 1.00 38.94  ? 129 ASN   A ND2 1 
ATOM   964  N  N   . GLY   A 1 124 ? 1.506  7.119   25.032 1.00 27.86  ? 130 GLY   A N   1 
ATOM   965  C  CA  . GLY   A 1 124 ? 1.465  5.715   24.638 1.00 25.39  ? 130 GLY   A CA  1 
ATOM   966  C  C   . GLY   A 1 124 ? 1.812  5.462   23.170 1.00 21.89  ? 130 GLY   A C   1 
ATOM   967  O  O   . GLY   A 1 124 ? 1.579  4.367   22.648 1.00 20.66  ? 130 GLY   A O   1 
ATOM   968  N  N   . LEU   A 1 125 ? 2.430  6.440   22.538 1.00 20.56  ? 131 LEU   A N   1 
ATOM   969  C  CA  . LEU   A 1 125 ? 2.861  6.350   21.168 1.00 19.87  ? 131 LEU   A CA  1 
ATOM   970  C  C   . LEU   A 1 125 ? 4.395  6.465   21.132 1.00 20.97  ? 131 LEU   A C   1 
ATOM   971  O  O   . LEU   A 1 125 ? 4.996  7.097   22.019 1.00 23.32  ? 131 LEU   A O   1 
ATOM   972  C  CB  . LEU   A 1 125 ? 2.248  7.507   20.348 1.00 20.51  ? 131 LEU   A CB  1 
ATOM   973  C  CG  . LEU   A 1 125 ? 0.714  7.454   20.222 1.00 21.98  ? 131 LEU   A CG  1 
ATOM   974  C  CD1 . LEU   A 1 125 ? 0.168  8.819   19.783 1.00 25.63  ? 131 LEU   A CD1 1 
ATOM   975  C  CD2 . LEU   A 1 125 ? 0.261  6.318   19.297 1.00 21.65  ? 131 LEU   A CD2 1 
ATOM   976  N  N   . VAL   A 1 126 ? 4.996  5.880   20.103 1.00 16.85  ? 132 VAL   A N   1 
ATOM   977  C  CA  . VAL   A 1 126 ? 6.439  6.014   19.862 1.00 14.66  ? 132 VAL   A CA  1 
ATOM   978  C  C   . VAL   A 1 126 ? 6.599  6.436   18.399 1.00 15.03  ? 132 VAL   A C   1 
ATOM   979  O  O   . VAL   A 1 126 ? 5.895  5.909   17.529 1.00 16.26  ? 132 VAL   A O   1 
ATOM   980  C  CB  . VAL   A 1 126 ? 7.226  4.710   20.182 1.00 15.66  ? 132 VAL   A CB  1 
ATOM   981  C  CG1 . VAL   A 1 126 ? 6.625  3.478   19.546 1.00 17.28  ? 132 VAL   A CG1 1 
ATOM   982  C  CG2 . VAL   A 1 126 ? 8.727  4.848   19.849 1.00 15.46  ? 132 VAL   A CG2 1 
ATOM   983  N  N   . GLY   A 1 127 ? 7.488  7.400   18.142 1.00 15.21  ? 133 GLY   A N   1 
ATOM   984  C  CA  . GLY   A 1 127 ? 7.696  7.838   16.769 1.00 15.14  ? 133 GLY   A CA  1 
ATOM   985  C  C   . GLY   A 1 127 ? 9.112  7.548   16.302 1.00 14.77  ? 133 GLY   A C   1 
ATOM   986  O  O   . GLY   A 1 127 ? 10.055 7.686   17.058 1.00 17.33  ? 133 GLY   A O   1 
ATOM   987  N  N   . PHE   A 1 128 ? 9.243  7.198   15.025 1.00 14.60  ? 134 PHE   A N   1 
ATOM   988  C  CA  . PHE   A 1 128 ? 10.541 6.851   14.429 1.00 15.63  ? 134 PHE   A CA  1 
ATOM   989  C  C   . PHE   A 1 128 ? 10.814 7.727   13.228 1.00 15.42  ? 134 PHE   A C   1 
ATOM   990  O  O   . PHE   A 1 128 ? 9.947  7.886   12.351 1.00 17.01  ? 134 PHE   A O   1 
ATOM   991  C  CB  . PHE   A 1 128 ? 10.510 5.371   13.940 1.00 16.10  ? 134 PHE   A CB  1 
ATOM   992  C  CG  . PHE   A 1 128 ? 9.996  4.390   14.973 1.00 16.18  ? 134 PHE   A CG  1 
ATOM   993  C  CD1 . PHE   A 1 128 ? 10.856 3.807   15.881 1.00 17.06  ? 134 PHE   A CD1 1 
ATOM   994  C  CD2 . PHE   A 1 128 ? 8.650  4.018   15.000 1.00 16.64  ? 134 PHE   A CD2 1 
ATOM   995  C  CE1 . PHE   A 1 128 ? 10.391 2.899   16.827 1.00 17.27  ? 134 PHE   A CE1 1 
ATOM   996  C  CE2 . PHE   A 1 128 ? 8.188  3.076   15.924 1.00 17.51  ? 134 PHE   A CE2 1 
ATOM   997  C  CZ  . PHE   A 1 128 ? 9.062  2.531   16.838 1.00 16.72  ? 134 PHE   A CZ  1 
ATOM   998  N  N   . ALA   A 1 129 ? 12.083 8.260   13.163 1.00 14.99  ? 135 ALA   A N   1 
ATOM   999  C  CA  . ALA   A 1 129 ? 12.504 8.993   11.984 1.00 16.33  ? 135 ALA   A CA  1 
ATOM   1000 C  C   . ALA   A 1 129 ? 12.878 7.967   10.908 1.00 16.53  ? 135 ALA   A C   1 
ATOM   1001 O  O   . ALA   A 1 129 ? 13.791 7.152   11.117 1.00 16.14  ? 135 ALA   A O   1 
ATOM   1002 C  CB  . ALA   A 1 129 ? 13.733 9.851   12.338 1.00 15.89  ? 135 ALA   A CB  1 
ATOM   1003 N  N   . ASP   A 1 130 ? 12.235 8.022   9.716  1.00 17.28  ? 136 ASP   A N   1 
ATOM   1004 C  CA  . ASP   A 1 130 ? 12.539 7.088   8.622  1.00 17.58  ? 136 ASP   A CA  1 
ATOM   1005 C  C   . ASP   A 1 130 ? 13.878 7.416   7.996  1.00 17.16  ? 136 ASP   A C   1 
ATOM   1006 O  O   . ASP   A 1 130 ? 14.208 8.601   7.847  1.00 17.49  ? 136 ASP   A O   1 
ATOM   1007 C  CB  . ASP   A 1 130 ? 11.457 7.193   7.507  1.00 19.39  ? 136 ASP   A CB  1 
ATOM   1008 C  CG  . ASP   A 1 130 ? 11.630 6.179   6.392  1.00 23.01  ? 136 ASP   A CG  1 
ATOM   1009 O  OD1 . ASP   A 1 130 ? 11.688 4.986   6.683  1.00 22.52  ? 136 ASP   A OD1 1 
ATOM   1010 O  OD2 . ASP   A 1 130 ? 11.704 6.593   5.203  1.00 26.04  ? 136 ASP   A OD2 1 
ATOM   1011 N  N   . VAL   A 1 131 ? 14.612 6.374   7.551  1.00 17.51  ? 137 VAL   A N   1 
ATOM   1012 C  CA  . VAL   A 1 131 ? 15.869 6.534   6.779  1.00 18.59  ? 137 VAL   A CA  1 
ATOM   1013 C  C   . VAL   A 1 131 ? 15.819 5.781   5.416  1.00 19.82  ? 137 VAL   A C   1 
ATOM   1014 O  O   . VAL   A 1 131 ? 16.781 5.859   4.655  1.00 20.32  ? 137 VAL   A O   1 
ATOM   1015 C  CB  . VAL   A 1 131 ? 17.138 6.116   7.572  1.00 19.09  ? 137 VAL   A CB  1 
ATOM   1016 C  CG1 . VAL   A 1 131 ? 17.256 6.927   8.872  1.00 19.25  ? 137 VAL   A CG1 1 
ATOM   1017 C  CG2 . VAL   A 1 131 ? 17.148 4.610   7.839  1.00 19.04  ? 137 VAL   A CG2 1 
ATOM   1018 N  N   . ARG   A 1 132 ? 14.727 5.018   5.130  1.00 19.12  ? 138 ARG   A N   1 
ATOM   1019 C  CA  . ARG   A 1 132 ? 14.624 4.219   3.906  1.00 19.25  ? 138 ARG   A CA  1 
ATOM   1020 C  C   . ARG   A 1 132 ? 14.654 5.011   2.612  1.00 22.14  ? 138 ARG   A C   1 
ATOM   1021 O  O   . ARG   A 1 132 ? 14.927 4.413   1.563  1.00 24.27  ? 138 ARG   A O   1 
ATOM   1022 C  CB  . ARG   A 1 132 ? 13.370 3.325   3.943  1.00 18.20  ? 138 ARG   A CB  1 
ATOM   1023 C  CG  . ARG   A 1 132 ? 13.386 2.333   5.135  1.00 17.11  ? 138 ARG   A CG  1 
ATOM   1024 C  CD  . ARG   A 1 132 ? 12.087 1.580   5.145  1.00 17.88  ? 138 ARG   A CD  1 
ATOM   1025 N  NE  . ARG   A 1 132 ? 10.981 2.463   5.534  1.00 18.38  ? 138 ARG   A NE  1 
ATOM   1026 C  CZ  . ARG   A 1 132 ? 9.740  2.045   5.733  1.00 19.26  ? 138 ARG   A CZ  1 
ATOM   1027 N  NH1 . ARG   A 1 132 ? 9.392  0.790   5.424  1.00 21.63  ? 138 ARG   A NH1 1 
ATOM   1028 N  NH2 . ARG   A 1 132 ? 8.812  2.888   6.185  1.00 20.14  ? 138 ARG   A NH2 1 
ATOM   1029 N  N   . ASP   A 1 133 ? 14.364 6.322   2.650  1.00 20.64  ? 139 ASP   A N   1 
ATOM   1030 C  CA  . ASP   A 1 133 ? 14.392 7.121   1.420  1.00 20.93  ? 139 ASP   A CA  1 
ATOM   1031 C  C   . ASP   A 1 133 ? 15.807 7.710   1.139  1.00 21.69  ? 139 ASP   A C   1 
ATOM   1032 O  O   . ASP   A 1 133 ? 16.027 8.301   0.064  1.00 23.17  ? 139 ASP   A O   1 
ATOM   1033 C  CB  . ASP   A 1 133 ? 13.390 8.273   1.522  1.00 22.24  ? 139 ASP   A CB  1 
ATOM   1034 C  CG  . ASP   A 1 133 ? 13.735 9.287   2.576  1.00 24.39  ? 139 ASP   A CG  1 
ATOM   1035 O  OD1 . ASP   A 1 133 ? 14.094 8.869   3.717  1.00 23.38  ? 139 ASP   A OD1 1 
ATOM   1036 O  OD2 . ASP   A 1 133 ? 13.670 10.515  2.273  1.00 25.70  ? 139 ASP   A OD2 1 
ATOM   1037 N  N   . LEU   A 1 134 ? 16.759 7.570   2.070  1.00 20.53  ? 140 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 134 ? 18.107 8.149   1.908  1.00 20.78  ? 140 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 134 ? 18.948 7.138   1.132  1.00 21.68  ? 140 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 134 ? 19.772 6.388   1.685  1.00 22.31  ? 140 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 134 ? 18.676 8.433   3.311  1.00 19.85  ? 140 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 134 ? 17.839 9.410   4.148  1.00 21.17  ? 140 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 134 ? 18.401 9.563   5.576  1.00 21.28  ? 140 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 134 ? 17.763 10.751  3.500  1.00 22.81  ? 140 LEU   A CD2 1 
ATOM   1045 N  N   . LEU   A 1 135 ? 18.676 7.063   -0.188 1.00 21.87  ? 141 LEU   A N   1 
ATOM   1046 C  CA  . LEU   A 1 135 ? 19.270 6.033   -1.034 1.00 23.61  ? 141 LEU   A CA  1 
ATOM   1047 C  C   . LEU   A 1 135 ? 20.766 6.138   -1.146 1.00 25.28  ? 141 LEU   A C   1 
ATOM   1048 O  O   . LEU   A 1 135 ? 21.440 5.119   -1.325 1.00 26.20  ? 141 LEU   A O   1 
ATOM   1049 C  CB  . LEU   A 1 135 ? 18.619 6.036   -2.437 1.00 23.44  ? 141 LEU   A CB  1 
ATOM   1050 C  CG  . LEU   A 1 135 ? 17.093 5.989   -2.474 1.00 25.10  ? 141 LEU   A CG  1 
ATOM   1051 C  CD1 . LEU   A 1 135 ? 16.579 6.008   -3.961 1.00 27.08  ? 141 LEU   A CD1 1 
ATOM   1052 C  CD2 . LEU   A 1 135 ? 16.557 4.735   -1.789 1.00 25.87  ? 141 LEU   A CD2 1 
ATOM   1053 N  N   . TRP   A 1 136 ? 21.293 7.357   -1.025 1.00 24.85  ? 142 TRP   A N   1 
ATOM   1054 C  CA  . TRP   A 1 136 ? 22.719 7.597   -1.109 1.00 25.73  ? 142 TRP   A CA  1 
ATOM   1055 C  C   . TRP   A 1 136 ? 23.498 6.940   0.042  1.00 27.00  ? 142 TRP   A C   1 
ATOM   1056 O  O   . TRP   A 1 136 ? 24.715 6.809   -0.063 1.00 28.29  ? 142 TRP   A O   1 
ATOM   1057 C  CB  . TRP   A 1 136 ? 23.005 9.101   -1.196 1.00 25.61  ? 142 TRP   A CB  1 
ATOM   1058 C  CG  . TRP   A 1 136 ? 22.361 9.904   -0.105 1.00 24.26  ? 142 TRP   A CG  1 
ATOM   1059 C  CD1 . TRP   A 1 136 ? 21.151 10.540  -0.151 1.00 24.63  ? 142 TRP   A CD1 1 
ATOM   1060 C  CD2 . TRP   A 1 136 ? 22.897 10.155  1.207  1.00 23.72  ? 142 TRP   A CD2 1 
ATOM   1061 N  NE1 . TRP   A 1 136 ? 20.894 11.148  1.055  1.00 24.99  ? 142 TRP   A NE1 1 
ATOM   1062 C  CE2 . TRP   A 1 136 ? 21.985 10.993  1.877  1.00 24.45  ? 142 TRP   A CE2 1 
ATOM   1063 C  CE3 . TRP   A 1 136 ? 24.098 9.811   1.847  1.00 24.43  ? 142 TRP   A CE3 1 
ATOM   1064 C  CZ2 . TRP   A 1 136 ? 22.192 11.418  3.194  1.00 24.68  ? 142 TRP   A CZ2 1 
ATOM   1065 C  CZ3 . TRP   A 1 136 ? 24.316 10.263  3.140  1.00 24.66  ? 142 TRP   A CZ3 1 
ATOM   1066 C  CH2 . TRP   A 1 136 ? 23.357 11.027  3.807  1.00 24.89  ? 142 TRP   A CH2 1 
ATOM   1067 N  N   . LEU   A 1 137 ? 22.818 6.529   1.143  1.00 27.11  ? 143 LEU   A N   1 
ATOM   1068 C  CA  . LEU   A 1 137 ? 23.511 5.830   2.225  1.00 28.31  ? 143 LEU   A CA  1 
ATOM   1069 C  C   . LEU   A 1 137 ? 24.086 4.484   1.696  1.00 31.70  ? 143 LEU   A C   1 
ATOM   1070 O  O   . LEU   A 1 137 ? 25.035 3.980   2.275  1.00 33.06  ? 143 LEU   A O   1 
ATOM   1071 C  CB  . LEU   A 1 137 ? 22.565 5.534   3.418  1.00 27.28  ? 143 LEU   A CB  1 
ATOM   1072 C  CG  . LEU   A 1 137 ? 22.131 6.716   4.296  1.00 26.51  ? 143 LEU   A CG  1 
ATOM   1073 C  CD1 . LEU   A 1 137 ? 21.028 6.294   5.250  1.00 25.80  ? 143 LEU   A CD1 1 
ATOM   1074 C  CD2 . LEU   A 1 137 ? 23.293 7.272   5.107  1.00 26.63  ? 143 LEU   A CD2 1 
ATOM   1075 N  N   . ASP   A 1 138 ? 23.526 3.917   0.592  1.00 33.49  ? 144 ASP   A N   1 
ATOM   1076 C  CA  . ASP   A 1 138 ? 23.974 2.631   0.024  1.00 35.50  ? 144 ASP   A CA  1 
ATOM   1077 C  C   . ASP   A 1 138 ? 25.177 2.763   -0.902 1.00 38.55  ? 144 ASP   A C   1 
ATOM   1078 O  O   . ASP   A 1 138 ? 25.625 1.743   -1.417 1.00 38.92  ? 144 ASP   A O   1 
ATOM   1079 C  CB  . ASP   A 1 138 ? 22.850 1.969   -0.787 1.00 35.92  ? 144 ASP   A CB  1 
ATOM   1080 C  CG  . ASP   A 1 138 ? 21.612 1.581   -0.028 1.00 39.18  ? 144 ASP   A CG  1 
ATOM   1081 O  OD1 . ASP   A 1 138 ? 21.655 1.587   1.220  1.00 40.27  ? 144 ASP   A OD1 1 
ATOM   1082 O  OD2 . ASP   A 1 138 ? 20.589 1.272   -0.681 1.00 40.85  ? 144 ASP   A OD2 1 
ATOM   1083 N  N   . GLU   A 1 139 ? 25.678 3.993   -1.173 1.00 40.58  ? 145 GLU   A N   1 
ATOM   1084 C  CA  . GLU   A 1 139 ? 26.810 4.157   -2.081 1.00 44.21  ? 145 GLU   A CA  1 
ATOM   1085 C  C   . GLU   A 1 139 ? 27.788 5.266   -1.659 1.00 47.54  ? 145 GLU   A C   1 
ATOM   1086 O  O   . GLU   A 1 139 ? 27.408 6.164   -0.909 1.00 48.39  ? 145 GLU   A O   1 
ATOM   1087 C  CB  . GLU   A 1 139 ? 26.295 4.414   -3.505 1.00 47.27  ? 145 GLU   A CB  1 
ATOM   1088 C  CG  . GLU   A 1 139 ? 25.382 5.620   -3.620 1.00 52.32  ? 145 GLU   A CG  1 
ATOM   1089 C  CD  . GLU   A 1 139 ? 24.141 5.352   -4.447 1.00 60.69  ? 145 GLU   A CD  1 
ATOM   1090 O  OE1 . GLU   A 1 139 ? 23.958 6.022   -5.491 1.00 60.81  ? 145 GLU   A OE1 1 
ATOM   1091 O  OE2 . GLU   A 1 139 ? 23.357 4.455   -4.057 1.00 64.64  ? 145 GLU   A OE2 1 
ATOM   1092 N  N   . GLU   A 1 140 ? 29.028 5.230   -2.186 1.00 49.40  ? 146 GLU   A N   1 
ATOM   1093 C  CA  . GLU   A 1 140 ? 30.115 6.204   -1.952 1.00 51.64  ? 146 GLU   A CA  1 
ATOM   1094 C  C   . GLU   A 1 140 ? 30.125 6.817   -0.533 1.00 53.35  ? 146 GLU   A C   1 
ATOM   1095 O  O   . GLU   A 1 140 ? 31.040 7.560   -0.172 1.00 54.16  ? 146 GLU   A O   1 
ATOM   1096 C  CB  . GLU   A 1 140 ? 30.132 7.299   -3.046 1.00 54.13  ? 146 GLU   A CB  1 
ATOM   1097 C  CG  . GLU   A 1 140 ? 29.423 8.613   -2.746 1.00 59.91  ? 146 GLU   A CG  1 
ATOM   1098 C  CD  . GLU   A 1 140 ? 30.318 9.841   -2.727 1.00 68.16  ? 146 GLU   A CD  1 
ATOM   1099 O  OE1 . GLU   A 1 140 ? 29.815 10.936  -2.383 1.00 70.03  ? 146 GLU   A OE1 1 
ATOM   1100 O  OE2 . GLU   A 1 140 ? 31.521 9.711   -3.051 1.00 70.73  ? 146 GLU   A OE2 1 
HETATM 1101 N  N1  . A1BSG B 2 .   ? 11.699 14.786  22.323 1.00 20.99  ? 201 A1BSG A N1  1 
HETATM 1102 C  C4  . A1BSG B 2 .   ? 12.944 14.968  22.833 1.00 21.75  ? 201 A1BSG A C4  1 
HETATM 1103 C  C5  . A1BSG B 2 .   ? 10.601 14.440  23.228 1.00 22.27  ? 201 A1BSG A C5  1 
HETATM 1104 C  C6  . A1BSG B 2 .   ? 10.403 12.957  23.440 1.00 22.23  ? 201 A1BSG A C6  1 
HETATM 1105 C  C7  . A1BSG B 2 .   ? 11.138 11.991  22.749 1.00 21.53  ? 201 A1BSG A C7  1 
HETATM 1106 C  C8  . A1BSG B 2 .   ? 10.955 10.639  23.001 1.00 21.59  ? 201 A1BSG A C8  1 
HETATM 1107 C  C10 . A1BSG B 2 .   ? 9.295  11.180  24.647 1.00 23.62  ? 201 A1BSG A C10 1 
HETATM 1108 C  C13 . A1BSG B 2 .   ? 8.264  11.032  25.737 1.00 24.71  ? 201 A1BSG A C13 1 
HETATM 1109 O  O1  . A1BSG B 2 .   ? 13.177 14.894  24.038 1.00 23.15  ? 201 A1BSG A O1  1 
HETATM 1110 C  C3  . A1BSG B 2 .   ? 14.030 15.386  21.875 1.00 22.39  ? 201 A1BSG A C3  1 
HETATM 1111 C  C2  . A1BSG B 2 .   ? 13.568 15.881  20.498 1.00 22.56  ? 201 A1BSG A C2  1 
HETATM 1112 C  C14 . A1BSG B 2 .   ? 11.253 15.020  20.942 1.00 20.56  ? 201 A1BSG A C14 1 
HETATM 1113 C  C1  . A1BSG B 2 .   ? 12.426 15.012  19.959 1.00 21.41  ? 201 A1BSG A C1  1 
HETATM 1114 C  C   . A1BSG B 2 .   ? 11.974 15.448  18.574 1.00 21.17  ? 201 A1BSG A C   1 
HETATM 1115 O  O   . A1BSG B 2 .   ? 11.355 16.510  18.405 1.00 21.21  ? 201 A1BSG A O   1 
HETATM 1116 N  N   . A1BSG B 2 .   ? 12.210 14.588  17.594 1.00 20.26  ? 201 A1BSG A N   1 
HETATM 1117 C  C11 . A1BSG B 2 .   ? 9.460  12.526  24.376 1.00 23.15  ? 201 A1BSG A C11 1 
HETATM 1118 O  O2  . A1BSG B 2 .   ? 8.634  13.349  25.107 1.00 24.54  ? 201 A1BSG A O2  1 
HETATM 1119 C  C12 . A1BSG B 2 .   ? 7.783  12.480  25.927 1.00 25.03  ? 201 A1BSG A C12 1 
HETATM 1120 C  C9  . A1BSG B 2 .   ? 10.056 10.235  23.967 1.00 22.02  ? 201 A1BSG A C9  1 
HETATM 1121 ZN ZN  . ZN    C 3 .   ? 11.013 -4.044  4.990  1.00 22.03  2 202 ZN    A ZN  1 
HETATM 1122 S  S   . DMS   D 4 .   ? 15.454 21.649  7.197  1.00 87.40  ? 203 DMS   A S   1 
HETATM 1123 O  O   . DMS   D 4 .   ? 14.716 21.723  8.503  1.00 87.23  ? 203 DMS   A O   1 
HETATM 1124 C  C1  . DMS   D 4 .   ? 14.229 21.464  5.870  1.00 87.31  ? 203 DMS   A C1  1 
HETATM 1125 C  C2  . DMS   D 4 .   ? 15.969 23.334  6.758  1.00 87.44  ? 203 DMS   A C2  1 
HETATM 1126 S  S   . DMS   E 4 .   ? 4.269  11.346  18.995 1.00 56.53  ? 204 DMS   A S   1 
HETATM 1127 O  O   . DMS   E 4 .   ? 5.306  12.412  19.158 1.00 56.70  ? 204 DMS   A O   1 
HETATM 1128 C  C1  . DMS   E 4 .   ? 3.278  11.394  20.512 1.00 56.17  ? 204 DMS   A C1  1 
HETATM 1129 C  C2  . DMS   E 4 .   ? 5.010  9.732   19.287 1.00 56.31  ? 204 DMS   A C2  1 
HETATM 1130 O  O   . HOH   F 5 .   ? 13.624 7.863   30.744 1.00 40.26  ? 301 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 26.643 8.305   -1.034 1.00 38.76  ? 302 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 4.215  22.296  22.888 1.00 31.86  ? 303 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 2.992  8.664   9.985  1.00 32.80  ? 304 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 6.472  3.206   3.275  1.00 36.66  ? 305 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 25.214 10.811  19.913 1.00 46.78  ? 306 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? -0.994 1.627   4.550  1.00 51.94  ? 307 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 2.884  -0.745  3.504  1.00 51.26  ? 308 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 35.178 8.471   5.369  1.00 50.61  ? 309 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 0.595  15.398  17.172 1.00 35.44  ? 310 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 22.256 -4.411  11.899 1.00 33.93  ? 311 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 20.003 -0.036  26.917 1.00 36.04  ? 312 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 6.898  -4.756  28.579 1.00 36.76  ? 313 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 1.470  -1.997  19.894 1.00 32.35  ? 314 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? 18.588 19.326  27.819 1.00 50.99  ? 315 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 10.678 8.887   4.286  1.00 25.54  ? 316 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 0.209  16.171  8.050  1.00 45.14  ? 317 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 4.404  8.186   3.235  1.00 41.33  ? 318 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 7.035  13.773  21.345 1.00 27.62  ? 319 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 15.713 -10.799 7.320  1.00 54.64  ? 320 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 1.039  9.500   4.558  1.00 55.48  ? 321 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 23.716 -5.917  7.542  1.00 44.50  ? 322 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 12.718 16.562  26.108 1.00 33.83  ? 323 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 8.164  -3.252  0.064  1.00 33.67  ? 324 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 10.557 18.418  20.199 1.00 23.31  ? 325 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 8.920  19.841  18.292 1.00 21.89  ? 326 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 20.954 9.208   18.218 1.00 19.96  ? 327 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 32.334 0.234   12.074 1.00 49.05  ? 328 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 8.897  -8.351  23.172 1.00 23.72  ? 329 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 4.543  -4.396  21.038 1.00 26.90  ? 330 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 15.252 -4.999  17.806 1.00 34.99  ? 331 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 31.330 11.249  17.876 1.00 43.57  ? 332 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 24.636 22.644  8.618  1.00 26.53  ? 333 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 23.922 0.243   14.883 1.00 26.89  ? 334 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 11.877 17.960  5.499  1.00 57.56  ? 335 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 15.650 23.524  26.541 1.00 43.69  ? 336 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 10.879 23.924  24.701 1.00 36.04  ? 337 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 0.963  2.346   24.386 1.00 31.81  ? 338 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 16.866 12.422  23.540 1.00 23.52  ? 339 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 29.651 3.307   9.310  1.00 28.07  ? 340 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 16.140 23.828  18.562 1.00 37.52  ? 341 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 18.021 -6.473  2.794  1.00 40.18  ? 342 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 24.508 17.280  2.091  1.00 47.29  ? 343 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 15.763 14.576  24.897 1.00 32.56  ? 344 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 5.801  26.606  17.954 1.00 46.70  ? 345 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 31.273 18.860  6.477  1.00 37.21  ? 346 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 10.411 5.462   3.062  1.00 22.69  ? 347 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 5.199  6.328   24.654 1.00 30.78  ? 348 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 27.733 3.593   1.877  1.00 45.67  ? 349 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 8.940  3.287   2.550  1.00 28.75  ? 350 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 1.021  0.190   16.511 1.00 17.29  ? 351 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 15.746 2.843   22.703 1.00 17.50  ? 352 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 16.433 -2.813  17.054 1.00 27.46  ? 353 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 3.825  3.934   27.384 1.00 37.53  ? 354 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 6.038  2.306   6.280  1.00 36.52  ? 355 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 11.712 11.295  0.459  1.00 51.08  ? 356 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? 19.308 -4.361  26.940 1.00 48.67  ? 357 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? 18.365 21.578  9.116  1.00 24.96  ? 358 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 8.376  25.980  15.402 1.00 37.21  ? 359 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 8.265  -5.229  31.135 1.00 65.59  ? 360 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 16.684 17.547  3.639  1.00 42.47  ? 361 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? 7.861  16.344  22.122 1.00 27.68  ? 362 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 20.377 -0.932  30.348 1.00 49.10  ? 363 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 27.042 4.130   18.791 1.00 39.69  ? 364 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 18.640 0.797   29.598 1.00 38.01  ? 365 HOH   A O   1 
HETATM 1195 O  O   . HOH   F 5 .   ? 18.655 -5.006  10.549 1.00 47.33  ? 366 HOH   A O   1 
HETATM 1196 O  O   . HOH   F 5 .   ? 11.790 12.124  11.130 1.00 15.85  ? 367 HOH   A O   1 
HETATM 1197 O  O   . HOH   F 5 .   ? 13.076 2.677   0.376  1.00 24.44  ? 368 HOH   A O   1 
HETATM 1198 O  O   . HOH   F 5 .   ? 34.123 -3.069  9.535  1.00 33.57  ? 369 HOH   A O   1 
HETATM 1199 O  O   . HOH   F 5 .   ? 27.865 16.338  1.857  1.00 45.21  ? 370 HOH   A O   1 
HETATM 1200 O  O   . HOH   F 5 .   ? 7.013  8.497   28.153 1.00 39.20  ? 371 HOH   A O   1 
HETATM 1201 O  O   . HOH   F 5 .   ? 25.639 12.098  22.079 1.00 49.61  ? 372 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 5 .   ? -2.030 8.878   22.114 1.00 107.08 ? 373 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 5 .   ? 5.741  20.243  25.943 1.00 42.20  ? 374 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 5 .   ? 21.275 23.652  10.370 1.00 36.04  ? 375 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 5 .   ? 20.263 9.236   25.120 1.00 25.24  ? 376 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 5 .   ? 21.838 21.637  6.040  1.00 37.35  ? 377 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 5 .   ? 10.429 -4.147  31.599 1.00 45.65  ? 378 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 5 .   ? 21.003 2.209   17.578 1.00 35.41  ? 379 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 5 .   ? 18.918 19.205  16.580 1.00 22.92  ? 380 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 5 .   ? 30.075 4.777   2.264  1.00 34.00  ? 381 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 5 .   ? 18.230 20.630  18.872 1.00 40.52  ? 382 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 5 .   ? 22.241 -0.499  3.104  1.00 31.69  ? 383 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 5 .   ? 28.581 -1.641  12.358 1.00 35.86  ? 384 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 5 .   ? 5.093  1.385   -2.213 1.00 49.78  ? 385 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 5 .   ? 31.667 2.715   11.097 1.00 33.34  ? 386 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 5 .   ? 22.523 -2.285  14.786 1.00 33.26  ? 387 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 5 .   ? 7.929  4.339   32.671 1.00 31.18  ? 388 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 5 .   ? 6.108  -6.876  14.009 1.00 36.88  ? 389 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 5 .   ? 13.466 11.116  9.013  1.00 17.07  ? 390 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 5 .   ? 11.158 16.528  3.258  1.00 44.58  ? 391 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 5 .   ? 18.553 19.966  5.029  1.00 43.42  ? 392 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 5 .   ? 7.912  16.905  24.912 1.00 36.69  ? 393 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 5 .   ? 18.600 2.783   22.632 1.00 22.19  ? 394 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 5 .   ? 27.839 -1.338  5.261  1.00 42.87  ? 395 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 5 .   ? 10.996 5.082   33.408 1.00 30.55  ? 396 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 5 .   ? 14.835 9.743   29.260 1.00 26.92  ? 397 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 5 .   ? 31.983 2.600   1.798  1.00 51.32  ? 398 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 5 .   ? 27.321 9.642   20.310 1.00 43.63  ? 399 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 5 .   ? 4.083  -4.525  6.270  1.00 32.62  ? 400 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 5 .   ? 15.347 -3.917  0.727  1.00 31.91  ? 401 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 5 .   ? 15.372 11.850  0.338  1.00 36.52  ? 402 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 5 .   ? 30.981 -4.022  6.412  1.00 36.75  ? 403 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 5 .   ? 31.724 8.928   4.095  1.00 34.27  ? 404 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 5 .   ? 19.712 4.465   24.934 1.00 39.46  ? 405 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 5 .   ? 20.763 3.241   -3.495 1.00 42.05  ? 406 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 5 .   ? 26.910 18.902  19.723 1.00 60.52  ? 407 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 5 .   ? 6.025  -0.851  23.921 1.00 21.23  ? 408 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 5 .   ? 12.933 21.851  13.068 1.00 27.22  ? 409 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 5 .   ? 14.657 15.179  3.302  1.00 30.78  ? 410 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 5 .   ? 4.294  15.376  20.539 1.00 32.74  ? 411 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 5 .   ? 8.483  20.997  8.988  1.00 44.64  ? 412 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 5 .   ? 0.361  4.167   6.798  1.00 33.59  ? 413 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 5 .   ? 30.642 20.654  8.672  1.00 23.15  ? 414 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 5 .   ? -0.063 15.855  13.221 1.00 38.60  ? 415 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 5 .   ? 23.812 18.279  18.065 1.00 31.72  ? 416 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 5 .   ? 37.014 -0.466  8.172  1.00 43.95  ? 417 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 5 .   ? 35.243 4.834   12.317 1.00 44.48  ? 418 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 5 .   ? 19.131 0.065   18.823 1.00 27.76  ? 419 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 5 .   ? 16.970 -6.953  9.626  1.00 42.83  ? 420 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 5 .   ? 2.344  10.750  28.086 1.00 57.37  ? 421 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 5 .   ? 15.565 15.107  27.791 1.00 50.21  ? 422 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 5 .   ? 21.038 -4.506  9.237  1.00 33.94  ? 423 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 5 .   ? 6.752  23.451  11.642 1.00 32.31  ? 424 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 5 .   ? 6.874  13.640  5.452  1.00 25.48  ? 425 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 5 .   ? 2.212  13.891  5.534  1.00 33.92  ? 426 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 5 .   ? 4.757  -1.673  21.653 1.00 25.73  ? 427 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 5 .   ? 35.300 7.508   12.415 1.00 51.87  ? 428 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 5 .   ? 18.938 -2.385  17.903 1.00 29.82  ? 429 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 5 .   ? 26.541 -2.048  13.412 1.00 50.32  ? 430 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 5 .   ? 28.044 12.004  0.409  1.00 60.54  ? 431 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 5 .   ? 19.062 13.491  1.649  1.00 37.48  ? 432 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 5 .   ? 7.019  25.811  21.588 1.00 30.39  ? 433 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 5 .   ? 33.018 14.701  5.940  1.00 58.04  ? 434 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 5 .   ? 22.993 8.809   20.134 1.00 23.26  ? 435 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 5 .   ? 1.713  -2.453  17.233 1.00 25.57  ? 436 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 5 .   ? 24.502 2.549   18.525 1.00 32.69  ? 437 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 5 .   ? 9.025  -7.049  8.848  1.00 41.33  ? 438 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 5 .   ? 23.884 9.027   -4.884 1.00 64.24  ? 439 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 5 .   ? 35.750 11.051  8.587  1.00 53.47  ? 440 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 5 .   ? 18.304 -5.781  17.062 1.00 48.05  ? 441 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 5 .   ? 22.772 19.347  5.232  1.00 28.72  ? 442 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 5 .   ? 10.511 9.629   31.435 1.00 41.01  ? 443 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 5 .   ? 16.924 24.409  13.944 1.00 54.80  ? 444 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 5 .   ? 31.098 6.158   17.130 1.00 55.31  ? 445 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 5 .   ? 18.595 23.017  16.775 1.00 45.03  ? 446 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 5 .   ? 33.029 14.723  19.713 1.00 43.02  ? 447 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 5 .   ? 17.913 9.522   -2.146 1.00 30.45  ? 448 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 5 .   ? 2.340  -6.264  17.843 1.00 48.37  ? 449 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 5 .   ? 7.188  11.485  3.818  1.00 52.06  ? 450 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 5 .   ? 25.337 7.559   19.408 1.00 36.16  ? 451 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 5 .   ? 22.387 -2.024  32.618 1.00 72.12  ? 452 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 5 .   ? 6.428  -3.507  -1.934 1.00 45.56  ? 453 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 5 .   ? 4.736  14.507  24.309 1.00 60.65  ? 454 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 5 .   ? 12.397 -7.604  12.266 1.00 46.17  ? 455 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 5 .   ? 5.197  -0.651  28.842 1.00 48.08  ? 456 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 5 .   ? 20.027 7.511   27.372 1.00 32.75  ? 457 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 5 .   ? 7.210  -4.867  2.319  1.00 35.57  ? 458 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 5 .   ? 17.754 11.419  -0.218 1.00 36.69  ? 459 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 5 .   ? 17.295 11.875  27.950 1.00 44.47  ? 460 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 5 .   ? 19.261 -6.237  33.772 1.00 48.58  ? 461 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 5 .   ? 4.527  -4.609  2.893  1.00 54.13  ? 462 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 5 .   ? 2.896  6.210   28.163 1.00 44.30  ? 463 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 5 .   ? 35.606 10.586  11.601 1.00 68.33  ? 464 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 5 .   ? -0.234 6.893   28.154 1.00 51.37  ? 465 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 5 .   ? 4.560  8.101   27.114 1.00 82.25  ? 466 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 5 .   ? 23.001 -4.651  15.810 1.00 54.55  ? 467 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 5 .   ? 37.478 16.815  13.062 1.00 49.38  ? 468 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 5 .   ? 20.083 9.636   -3.666 1.00 29.08  ? 469 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 5 .   ? 10.129 16.356  26.691 1.00 40.97  ? 470 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 5 .   ? 36.307 18.181  7.222  1.00 59.00  ? 471 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 5 .   ? 2.828  14.404  22.431 1.00 46.58  ? 472 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 5 .   ? 20.628 15.203  0.277  1.00 43.24  ? 473 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 5 .   ? 2.858  1.999   26.321 1.00 38.04  ? 474 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 5 .   ? 3.513  -6.857  14.569 1.00 47.52  ? 475 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 5 .   ? 18.852 11.594  25.250 1.00 30.62  ? 476 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 5 .   ? 7.688  -7.463  1.539  1.00 53.39  ? 477 HOH   A O   1 
HETATM 1307 O  O   . HOH   F 5 .   ? 4.636  -1.299  26.275 1.00 40.66  ? 478 HOH   A O   1 
HETATM 1308 O  O   . HOH   F 5 .   ? 12.818 23.766  15.068 1.00 33.28  ? 479 HOH   A O   1 
HETATM 1309 O  O   . HOH   F 5 .   ? 8.835  20.188  6.618  1.00 48.48  ? 480 HOH   A O   1 
HETATM 1310 O  O   . HOH   F 5 .   ? 1.496  -1.303  23.744 1.00 47.26  ? 481 HOH   A O   1 
HETATM 1311 O  O   . HOH   F 5 .   ? 5.903  5.515   1.940  1.00 57.29  ? 482 HOH   A O   1 
HETATM 1312 O  O   . HOH   F 5 .   ? 14.875 -8.365  12.372 1.00 66.57  ? 483 HOH   A O   1 
HETATM 1313 O  O   . HOH   F 5 .   ? 16.679 14.261  1.466  1.00 36.53  ? 484 HOH   A O   1 
HETATM 1314 O  O   . HOH   F 5 .   ? 24.859 -1.218  2.672  1.00 58.92  ? 485 HOH   A O   1 
HETATM 1315 O  O   . HOH   F 5 .   ? 8.816  7.876   2.437  1.00 37.26  ? 486 HOH   A O   1 
HETATM 1316 O  O   . HOH   F 5 .   ? 15.026 24.535  16.247 1.00 36.24  ? 487 HOH   A O   1 
HETATM 1317 O  O   . HOH   F 5 .   ? 24.678 13.789  0.852  1.00 47.20  ? 488 HOH   A O   1 
HETATM 1318 O  O   . HOH   F 5 .   ? 32.684 4.339   13.129 1.00 37.71  ? 489 HOH   A O   1 
HETATM 1319 O  O   . HOH   F 5 .   ? 6.819  27.923  20.021 1.00 40.14  ? 490 HOH   A O   1 
HETATM 1320 O  O   . HOH   F 5 .   ? 23.775 10.101  22.780 1.00 39.89  ? 491 HOH   A O   1 
HETATM 1321 O  O   . HOH   F 5 .   ? 31.878 6.806   14.496 1.00 48.18  ? 492 HOH   A O   1 
HETATM 1322 O  O   . HOH   F 5 .   ? 9.030  10.504  29.254 1.00 35.39  ? 493 HOH   A O   1 
HETATM 1323 O  O   . HOH   F 5 .   ? 3.688  -3.834  26.901 1.00 50.22  ? 494 HOH   A O   1 
HETATM 1324 O  O   . HOH   F 5 .   ? 15.025 -6.404  32.350 1.00 47.90  ? 495 HOH   A O   1 
HETATM 1325 O  O   . HOH   F 5 .   ? 0.240  12.664  17.471 1.00 45.70  ? 496 HOH   A O   1 
HETATM 1326 O  O   . HOH   F 5 .   ? 14.668 12.025  -2.314 1.00 41.70  ? 497 HOH   A O   1 
HETATM 1327 O  O   . HOH   F 5 .   ? 1.553  21.551  7.726  1.00 62.30  ? 498 HOH   A O   1 
HETATM 1328 O  O   . HOH   F 5 .   ? 41.962 4.821   9.193  1.00 62.19  ? 499 HOH   A O   1 
HETATM 1329 O  O   . HOH   F 5 .   ? 22.572 10.499  25.019 1.00 39.89  ? 500 HOH   A O   1 
HETATM 1330 O  O   . HOH   F 5 .   ? 37.495 20.803  9.438  1.00 42.34  ? 501 HOH   A O   1 
HETATM 1331 O  O   . HOH   F 5 .   ? 4.453  -6.516  22.800 1.00 33.73  ? 502 HOH   A O   1 
HETATM 1332 O  O   . HOH   F 5 .   ? 17.772 -7.116  31.114 1.00 51.26  ? 503 HOH   A O   1 
HETATM 1333 O  O   . HOH   F 5 .   ? 39.788 18.717  15.557 1.00 49.03  ? 504 HOH   A O   1 
HETATM 1334 O  O   . HOH   F 5 .   ? 10.601 25.352  14.114 1.00 35.76  ? 505 HOH   A O   1 
HETATM 1335 O  O   . HOH   F 5 .   ? 30.183 -0.840  13.924 1.00 56.94  ? 506 HOH   A O   1 
HETATM 1336 O  O   . HOH   F 5 .   ? 9.543  28.332  16.462 1.00 47.77  ? 507 HOH   A O   1 
HETATM 1337 O  O   . HOH   F 5 .   ? 34.694 11.652  2.885  1.00 59.89  ? 508 HOH   A O   1 
HETATM 1338 O  O   . HOH   F 5 .   ? 21.748 11.772  -3.760 1.00 37.68  ? 509 HOH   A O   1 
HETATM 1339 O  O   . HOH   F 5 .   ? 5.560  22.427  8.012  1.00 68.76  ? 510 HOH   A O   1 
HETATM 1340 O  O   . HOH   F 5 .   ? 24.295 12.021  -3.193 1.00 44.27  ? 511 HOH   A O   1 
HETATM 1341 O  O   . HOH   F 5 .   ? 3.656  30.453  17.202 1.00 57.75  ? 512 HOH   A O   1 
HETATM 1342 O  O   . HOH   F 5 .   ? 1.617  20.739  4.686  1.00 67.05  ? 513 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   ? 0.2933 0.2886 0.3114 -0.0220 -0.0646 0.0083  7   SER   A N   
2    C CA  . SER   A 1   ? 0.2982 0.3026 0.3397 -0.0217 -0.0673 0.0124  7   SER   A CA  
3    C C   . SER   A 1   ? 0.2770 0.2919 0.3348 -0.0183 -0.0595 0.0146  7   SER   A C   
4    O O   . SER   A 1   ? 0.2773 0.2931 0.3294 -0.0167 -0.0547 0.0140  7   SER   A O   
5    C CB  . SER   A 1   ? 0.3338 0.3351 0.3812 -0.0266 -0.0804 0.0186  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3993 0.4016 0.4486 -0.0277 -0.0842 0.0241  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2480 0.2693 0.3246 -0.0173 -0.0571 0.0165  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.2313 0.2595 0.3222 -0.0151 -0.0485 0.0181  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.2183 0.2498 0.3197 -0.0142 -0.0422 0.0171  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2386 0.2686 0.3334 -0.0141 -0.0424 0.0139  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1925 0.2272 0.3093 -0.0135 -0.0353 0.0197  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1984 0.2339 0.3226 -0.0132 -0.0273 0.0188  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1948 0.2303 0.3228 -0.0129 -0.0157 0.0181  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2100 0.2461 0.3430 -0.0125 -0.0140 0.0201  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2019 0.2381 0.3465 -0.0140 -0.0308 0.0240  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1778 0.2111 0.3029 -0.0136 -0.0071 0.0157  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1950 0.2245 0.3209 -0.0147 0.0053  0.0145  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1969 0.2239 0.3423 -0.0148 0.0125  0.0182  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2064 0.2335 0.3552 -0.0148 0.0101  0.0192  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2083 0.2346 0.3137 -0.0170 0.0095  0.0095  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2058 0.2355 0.2963 -0.0166 0.0022  0.0070  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2339 0.2531 0.3351 -0.0197 0.0223  0.0074  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2209 0.2494 0.2957 -0.0189 0.0021  0.0045  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1978 0.2218 0.3579 -0.0147 0.0224  0.0205  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2102 0.2305 0.3920 -0.0144 0.0323  0.0245  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2325 0.2423 0.4058 -0.0167 0.0500  0.0205  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2460 0.2528 0.4215 -0.0170 0.0573  0.0197  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2128 0.2378 0.4249 -0.0125 0.0293  0.0325  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2143 0.2469 0.4331 -0.0120 0.0112  0.0369  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2183 0.2523 0.4494 -0.0122 0.0060  0.0403  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2363 0.2726 0.4452 -0.0120 -0.0006 0.0371  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2299 0.2684 0.4632 -0.0130 -0.0111 0.0435  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2392 0.2790 0.4475 -0.0129 -0.0168 0.0400  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2526 0.2932 0.4731 -0.0137 -0.0224 0.0432  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2733 0.3151 0.4899 -0.0157 -0.0386 0.0453  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2272 0.2299 0.3881 -0.0190 0.0571  0.0177  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2665 0.2557 0.4120 -0.0229 0.0737  0.0131  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2828 0.2641 0.4392 -0.0233 0.0858  0.0155  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2711 0.2563 0.4290 -0.0225 0.0791  0.0175  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2894 0.2753 0.4001 -0.0271 0.0694  0.0069  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3006 0.2928 0.4032 -0.0267 0.0571  0.0078  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3222 0.2914 0.4126 -0.0330 0.0854  0.0023  12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2953 0.2656 0.4631 -0.0240 0.1044  0.0159  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3010 0.2627 0.4829 -0.0240 0.1186  0.0188  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2900 0.2643 0.5039 -0.0195 0.1081  0.0268  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2869 0.2725 0.5240 -0.0163 0.0976  0.0319  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.2906 0.2631 0.5030 -0.0199 0.1084  0.0280  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2686 0.2527 0.5092 -0.0165 0.0965  0.0350  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2498 0.2433 0.4727 -0.0166 0.0767  0.0330  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2449 0.2424 0.4784 -0.0156 0.0706  0.0363  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2982 0.2752 0.5594 -0.0159 0.1107  0.0395  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3916 0.3634 0.6860 -0.0141 0.1274  0.0448  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4087 0.3908 0.7404 -0.0110 0.1203  0.0530  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4276 0.3823 0.7087 -0.0166 0.1500  0.0404  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2495 0.2464 0.4486 -0.0176 0.0674  0.0281  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2471 0.2518 0.4300 -0.0176 0.0505  0.0260  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2243 0.2383 0.4092 -0.0159 0.0361  0.0263  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2085 0.2222 0.3951 -0.0158 0.0393  0.0259  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2587 0.2575 0.4075 -0.0210 0.0526  0.0200  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2714 0.2594 0.4100 -0.0239 0.0645  0.0196  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2896 0.2793 0.4390 -0.0227 0.0625  0.0231  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3024 0.2772 0.4192 -0.0285 0.0778  0.0158  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3152 0.2941 0.4548 -0.0254 0.0741  0.0233  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.3252 0.2877 0.4286 -0.0321 0.0889  0.0156  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.3442 0.3092 0.4592 -0.0303 0.0870  0.0196  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3859 0.3383 0.4869 -0.0339 0.0980  0.0200  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2057 0.2265 0.3894 -0.0151 0.0213  0.0269  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2016 0.2288 0.3809 -0.0143 0.0073  0.0264  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2012 0.2291 0.3558 -0.0148 0.0009  0.0214  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2118 0.2397 0.3655 -0.0149 -0.0023 0.0215  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2176 0.2494 0.4184 -0.0138 -0.0041 0.0321  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2301 0.2653 0.4215 -0.0143 -0.0193 0.0314  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2546 0.2923 0.4669 -0.0155 -0.0314 0.0381  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2512 0.2878 0.4494 -0.0174 -0.0453 0.0359  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2845 0.3198 0.4687 -0.0189 -0.0551 0.0349  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2762 0.3128 0.4593 -0.0184 -0.0535 0.0363  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2457 0.2769 0.4150 -0.0212 -0.0652 0.0320  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1963 0.2248 0.3337 -0.0151 -0.0008 0.0177  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2035 0.2331 0.3217 -0.0153 -0.0060 0.0141  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2080 0.2406 0.3232 -0.0141 -0.0166 0.0135  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2102 0.2436 0.3248 -0.0137 -0.0175 0.0135  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2194 0.2466 0.3204 -0.0172 0.0000  0.0109  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2193 0.2485 0.3059 -0.0175 -0.0056 0.0090  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2349 0.2554 0.3338 -0.0198 0.0117  0.0108  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1963 0.2290 0.3078 -0.0137 -0.0235 0.0126  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1997 0.2316 0.3045 -0.0134 -0.0320 0.0113  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1981 0.2287 0.2900 -0.0127 -0.0331 0.0079  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1989 0.2304 0.2907 -0.0127 -0.0298 0.0080  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2301 0.2604 0.3460 -0.0146 -0.0404 0.0141  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2606 0.2928 0.3923 -0.0152 -0.0410 0.0190  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2301 0.2599 0.3546 -0.0149 -0.0406 0.0150  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1737 0.2012 0.2554 -0.0124 -0.0374 0.0056  19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1790 0.2038 0.2526 -0.0116 -0.0371 0.0029  19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2024 0.2246 0.2827 -0.0124 -0.0406 0.0034  19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2147 0.2339 0.2995 -0.0143 -0.0466 0.0044  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1911 0.2097 0.2520 -0.0115 -0.0392 0.0001  19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2117 0.2325 0.2666 -0.0105 -0.0356 -0.0003 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2284 0.2493 0.2826 -0.0112 -0.0374 0.0008  19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1972 0.2200 0.2497 -0.0089 -0.0308 -0.0011 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1880 0.2112 0.2701 -0.0115 -0.0376 0.0034  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1849 0.2056 0.2746 -0.0121 -0.0401 0.0040  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2110 0.2231 0.2945 -0.0138 -0.0458 0.0009  20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2129 0.2223 0.3031 -0.0160 -0.0512 0.0018  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1914 0.2142 0.2834 -0.0107 -0.0360 0.0051  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1844 0.2056 0.2862 -0.0112 -0.0372 0.0065  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1947 0.2177 0.2983 -0.0097 -0.0337 0.0083  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2352 0.2572 0.3487 -0.0099 -0.0338 0.0103  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2615 0.2777 0.3778 -0.0097 -0.0351 0.0081  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2619 0.2707 0.3695 -0.0102 -0.0366 0.0031  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2531 0.2691 0.3797 -0.0097 -0.0346 0.0105  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2162 0.2227 0.2863 -0.0134 -0.0444 -0.0026 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2309 0.2254 0.2892 -0.0161 -0.0484 -0.0065 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2463 0.2373 0.3005 -0.0198 -0.0571 -0.0054 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.2754 0.2557 0.3206 -0.0239 -0.0633 -0.0076 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2398 0.2269 0.2844 -0.0147 -0.0421 -0.0104 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2439 0.2316 0.2791 -0.0140 -0.0403 -0.0106 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2402 0.2383 0.2821 -0.0110 -0.0356 -0.0081 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.2590 0.2371 0.2777 -0.0166 -0.0426 -0.0129 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.2394 0.2348 0.2711 -0.0111 -0.0347 -0.0090 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.2604 0.2439 0.2776 -0.0143 -0.0386 -0.0117 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2334 0.2328 0.2953 -0.0192 -0.0583 -0.0015 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.2543 0.2520 0.3176 -0.0227 -0.0673 0.0016  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.2627 0.2673 0.3486 -0.0235 -0.0712 0.0072  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.2655 0.2708 0.3590 -0.0262 -0.0787 0.0117  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.2639 0.2643 0.3215 -0.0216 -0.0653 0.0027  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.2813 0.2739 0.3177 -0.0210 -0.0610 -0.0020 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.2821 0.2783 0.3151 -0.0197 -0.0587 -0.0004 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2994 0.2766 0.3169 -0.0258 -0.0670 -0.0053 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.2469 0.2565 0.3451 -0.0213 -0.0657 0.0077  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.2507 0.2656 0.3714 -0.0218 -0.0672 0.0131  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.2665 0.2766 0.3947 -0.0264 -0.0789 0.0156  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.2718 0.2732 0.3873 -0.0292 -0.0841 0.0118  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.2504 0.2693 0.3790 -0.0191 -0.0586 0.0131  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.2492 0.2642 0.3990 -0.0276 -0.0829 0.0225  24  THR   A N   
135  C CA  . THR   A 18  ? 0.2486 0.2604 0.4107 -0.0327 -0.0960 0.0270  24  THR   A CA  
136  C C   . THR   A 18  ? 0.2495 0.2635 0.4313 -0.0324 -0.0942 0.0290  24  THR   A C   
137  O O   . THR   A 18  ? 0.2323 0.2507 0.4198 -0.0280 -0.0821 0.0280  24  THR   A O   
138  C CB  . THR   A 18  ? 0.2755 0.2924 0.4566 -0.0343 -0.1017 0.0354  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.3053 0.3306 0.5117 -0.0301 -0.0907 0.0398  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2808 0.2969 0.4455 -0.0340 -0.1019 0.0345  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.2644 0.2750 0.4576 -0.0376 -0.1066 0.0328  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.2781 0.2907 0.4941 -0.0380 -0.1068 0.0361  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.2540 0.2763 0.4975 -0.0333 -0.0950 0.0422  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.2492 0.2733 0.5006 -0.0302 -0.0851 0.0416  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3307 0.3383 0.5562 -0.0457 -0.1250 0.0409  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4100 0.4232 0.6719 -0.0467 -0.1278 0.0492  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4510 0.4597 0.7185 -0.0497 -0.1325 0.0481  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4193 0.4412 0.7145 -0.0455 -0.1266 0.0591  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4468 0.4625 0.7510 -0.0497 -0.1332 0.0572  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4272 0.4508 0.7496 -0.0469 -0.1287 0.0641  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.2476 0.2747 0.5036 -0.0328 -0.0949 0.0478  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.2452 0.2789 0.5265 -0.0288 -0.0819 0.0534  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.2308 0.2645 0.4954 -0.0239 -0.0649 0.0472  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.2365 0.2713 0.5140 -0.0214 -0.0526 0.0490  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.2803 0.3179 0.5772 -0.0294 -0.0850 0.0604  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.3650 0.4073 0.6933 -0.0260 -0.0710 0.0671  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3966 0.4412 0.7569 -0.0269 -0.0723 0.0748  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3887 0.4314 0.7093 -0.0223 -0.0567 0.0644  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.2132 0.2448 0.4486 -0.0230 -0.0642 0.0404  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.2103 0.2420 0.4301 -0.0196 -0.0506 0.0355  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.2088 0.2387 0.4259 -0.0187 -0.0463 0.0334  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2121 0.2421 0.4298 -0.0168 -0.0342 0.0336  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.2140 0.2438 0.4054 -0.0192 -0.0525 0.0292  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.2480 0.2794 0.4378 -0.0193 -0.0536 0.0306  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.2673 0.3015 0.4723 -0.0180 -0.0456 0.0345  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.2348 0.2636 0.4087 -0.0208 -0.0618 0.0281  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.2145 0.2414 0.4267 -0.0207 -0.0556 0.0312  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.2218 0.2470 0.4333 -0.0198 -0.0518 0.0297  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.2151 0.2420 0.4533 -0.0196 -0.0470 0.0358  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.2077 0.2342 0.4452 -0.0177 -0.0372 0.0360  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.2152 0.2351 0.4163 -0.0222 -0.0617 0.0256  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.2226 0.2392 0.3980 -0.0214 -0.0615 0.0194  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.2390 0.2512 0.3994 -0.0236 -0.0687 0.0162  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.2139 0.2311 0.3774 -0.0185 -0.0535 0.0166  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.2471 0.2568 0.3880 -0.0216 -0.0640 0.0111  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.2372 0.2510 0.3812 -0.0184 -0.0551 0.0118  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.2094 0.2295 0.3768 -0.0163 -0.0451 0.0185  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.2428 0.2570 0.3757 -0.0160 -0.0491 0.0095  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.2188 0.2391 0.3730 -0.0145 -0.0408 0.0165  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.2297 0.2479 0.3688 -0.0142 -0.0428 0.0123  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.2245 0.2531 0.4860 -0.0216 -0.0532 0.0415  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2129 0.2433 0.5045 -0.0212 -0.0477 0.0483  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2198 0.2506 0.5163 -0.0180 -0.0302 0.0504  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2248 0.2542 0.5355 -0.0168 -0.0196 0.0537  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2016 0.2342 0.5195 -0.0246 -0.0599 0.0552  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2099 0.2412 0.4930 -0.0171 -0.0264 0.0481  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2207 0.2498 0.5043 -0.0152 -0.0094 0.0489  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2188 0.2450 0.4690 -0.0147 -0.0035 0.0421  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2143 0.2381 0.4551 -0.0143 0.0057  0.0405  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2433 0.2747 0.5431 -0.0151 -0.0091 0.0530  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2914 0.3259 0.6293 -0.0159 -0.0135 0.0618  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3092 0.3416 0.6687 -0.0147 -0.0010 0.0663  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2976 0.3359 0.6434 -0.0186 -0.0318 0.0646  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2068 0.2326 0.4407 -0.0149 -0.0086 0.0386  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1973 0.2215 0.4029 -0.0148 -0.0060 0.0336  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2201 0.2389 0.4167 -0.0153 0.0087  0.0342  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2403 0.2555 0.4469 -0.0155 0.0164  0.0375  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1975 0.2223 0.3950 -0.0148 -0.0137 0.0316  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2050 0.2291 0.3793 -0.0147 -0.0119 0.0287  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2200 0.2460 0.3791 -0.0146 -0.0165 0.0247  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2167 0.2409 0.3904 -0.0143 -0.0173 0.0283  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2060 0.2229 0.3818 -0.0163 0.0124  0.0309  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2257 0.2349 0.3846 -0.0186 0.0244  0.0305  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2473 0.2573 0.3838 -0.0201 0.0187  0.0289  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2800 0.2853 0.4079 -0.0220 0.0232  0.0310  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2421 0.2471 0.3937 -0.0199 0.0327  0.0283  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2640 0.2586 0.3907 -0.0241 0.0435  0.0268  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2441 0.2480 0.4224 -0.0184 0.0403  0.0316  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2308 0.2462 0.3587 -0.0194 0.0092  0.0260  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2330 0.2501 0.3445 -0.0205 0.0039  0.0256  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2174 0.2408 0.3299 -0.0181 -0.0063 0.0228  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2130 0.2380 0.3288 -0.0171 -0.0080 0.0205  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2519 0.2637 0.3419 -0.0246 0.0092  0.0249  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2517 0.2665 0.3277 -0.0262 0.0019  0.0255  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2673 0.2812 0.3359 -0.0285 -0.0005 0.0296  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2435 0.2629 0.3136 -0.0258 -0.0038 0.0231  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2753 0.2937 0.3364 -0.0294 -0.0080 0.0304  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2554 0.2770 0.3175 -0.0277 -0.0096 0.0261  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2537 0.2757 0.3268 -0.0238 -0.0048 0.0193  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2668 0.2930 0.3244 -0.0278 -0.0153 0.0255  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2592 0.2850 0.3251 -0.0240 -0.0099 0.0181  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2558 0.2836 0.3148 -0.0259 -0.0147 0.0211  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1978 0.2238 0.3082 -0.0173 -0.0121 0.0235  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1938 0.2231 0.3028 -0.0153 -0.0189 0.0206  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2028 0.2341 0.3061 -0.0154 -0.0213 0.0227  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2058 0.2365 0.3102 -0.0165 -0.0202 0.0267  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1850 0.2139 0.3056 -0.0135 -0.0239 0.0187  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2043 0.2320 0.3360 -0.0131 -0.0243 0.0211  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2542 0.2820 0.3850 -0.0121 -0.0264 0.0215  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2515 0.2784 0.3908 -0.0120 -0.0255 0.0243  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2463 0.2747 0.3701 -0.0112 -0.0283 0.0195  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2043 0.2378 0.3029 -0.0144 -0.0243 0.0207  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2069 0.2429 0.3050 -0.0142 -0.0265 0.0238  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1942 0.2302 0.2946 -0.0113 -0.0282 0.0202  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1939 0.2304 0.2881 -0.0111 -0.0281 0.0175  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2390 0.2765 0.3264 -0.0178 -0.0265 0.0271  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3028 0.3440 0.3927 -0.0185 -0.0303 0.0325  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.3184 0.3614 0.4187 -0.0151 -0.0312 0.0325  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3207 0.3621 0.4023 -0.0230 -0.0322 0.0374  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1887 0.2227 0.2972 -0.0092 -0.0285 0.0200  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1920 0.2223 0.3010 -0.0069 -0.0278 0.0162  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1977 0.2280 0.3059 -0.0070 -0.0279 0.0159  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1972 0.2309 0.3055 -0.0062 -0.0266 0.0184  36  SER   A C   
244  O O   . SER   A 30  ? 0.2074 0.2384 0.3110 -0.0050 -0.0249 0.0146  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2041 0.2305 0.3227 -0.0055 -0.0266 0.0166  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2318 0.2567 0.3478 -0.0056 -0.0270 0.0146  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2249 0.2438 0.3407 -0.0041 -0.0243 0.0114  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2561 0.2837 0.3821 -0.0045 -0.0252 0.0200  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1830 0.2224 0.2966 -0.0074 -0.0279 0.0253  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1833 0.2270 0.3003 -0.0073 -0.0282 0.0291  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1870 0.2323 0.2928 -0.0091 -0.0290 0.0267  37  SER   A C   
252  O O   . SER   A 31  ? 0.2019 0.2494 0.3106 -0.0085 -0.0285 0.0280  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2366 0.2857 0.3619 -0.0095 -0.0318 0.0384  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.3249 0.3756 0.4386 -0.0143 -0.0355 0.0409  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1725 0.2162 0.2679 -0.0110 -0.0294 0.0233  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1613 0.2056 0.2470 -0.0125 -0.0291 0.0206  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1699 0.2102 0.2519 -0.0102 -0.0272 0.0143  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1767 0.2172 0.2522 -0.0109 -0.0265 0.0122  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1704 0.2140 0.2472 -0.0167 -0.0291 0.0216  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1894 0.2351 0.2636 -0.0210 -0.0324 0.0281  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2157 0.2570 0.2766 -0.0262 -0.0308 0.0284  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2092 0.2483 0.2601 -0.0283 -0.0284 0.0245  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2166 0.2506 0.2529 -0.0343 -0.0270 0.0248  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2307 0.2606 0.2581 -0.0394 -0.0284 0.0293  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2176 0.2494 0.2467 -0.0359 -0.0243 0.0209  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1867 0.2226 0.2716 -0.0084 -0.0270 0.0117  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1850 0.2158 0.2647 -0.0078 -0.0276 0.0068  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1770 0.2094 0.2549 -0.0096 -0.0285 0.0067  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1788 0.2095 0.2526 -0.0096 -0.0293 0.0045  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1924 0.2200 0.2659 -0.0063 -0.0257 0.0039  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2161 0.2365 0.2813 -0.0068 -0.0276 -0.0003 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2181 0.2339 0.2841 -0.0078 -0.0306 -0.0016 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2182 0.2379 0.2765 -0.0069 -0.0272 -0.0016 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1815 0.2160 0.2629 -0.0113 -0.0275 0.0096  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1722 0.2065 0.2545 -0.0128 -0.0256 0.0097  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1745 0.2071 0.2662 -0.0131 -0.0255 0.0112  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1871 0.2196 0.2823 -0.0131 -0.0256 0.0131  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1904 0.2257 0.2661 -0.0156 -0.0216 0.0114  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2014 0.2382 0.2691 -0.0163 -0.0213 0.0102  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2147 0.2500 0.2737 -0.0206 -0.0182 0.0116  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1943 0.2306 0.2629 -0.0148 -0.0210 0.0075  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1746 0.2064 0.2724 -0.0135 -0.0245 0.0113  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1816 0.2121 0.2922 -0.0139 -0.0233 0.0137  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1880 0.2179 0.3044 -0.0148 -0.0173 0.0151  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1995 0.2302 0.3145 -0.0146 -0.0179 0.0141  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1873 0.2166 0.3061 -0.0135 -0.0307 0.0133  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1942 0.2229 0.3302 -0.0141 -0.0307 0.0167  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2232 0.2494 0.3628 -0.0145 -0.0379 0.0158  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2158 0.2453 0.3650 -0.0147 -0.0308 0.0194  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1894 0.2168 0.3119 -0.0158 -0.0100 0.0175  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1814 0.2061 0.3120 -0.0165 -0.0014 0.0190  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1869 0.2111 0.3393 -0.0158 -0.0001 0.0230  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2018 0.2249 0.3565 -0.0159 0.0005  0.0243  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2037 0.2224 0.3199 -0.0192 0.0093  0.0181  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2174 0.2308 0.3433 -0.0199 0.0210  0.0192  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2012 0.2207 0.2976 -0.0207 0.0066  0.0150  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1885 0.2138 0.3589 -0.0151 0.0004  0.0257  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1967 0.2222 0.3931 -0.0147 0.0014  0.0309  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2225 0.2445 0.4336 -0.0145 0.0146  0.0339  43  SER   A C   
300  O O   . SER   A 37  ? 0.2311 0.2513 0.4335 -0.0148 0.0200  0.0317  43  SER   A O   
301  C CB  . SER   A 37  ? 0.1938 0.2239 0.4029 -0.0148 -0.0132 0.0332  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2104 0.2427 0.4210 -0.0148 -0.0170 0.0340  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2193 0.2396 0.4543 -0.0141 0.0211  0.0390  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2386 0.2539 0.4912 -0.0137 0.0365  0.0423  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2400 0.2613 0.5211 -0.0126 0.0305  0.0483  44  SER   A C   
306  O O   . SER   A 38  ? 0.2570 0.2851 0.5486 -0.0129 0.0142  0.0514  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2687 0.2782 0.5354 -0.0136 0.0485  0.0457  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3070 0.3232 0.5971 -0.0128 0.0372  0.0508  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2355 0.2531 0.5280 -0.0120 0.0430  0.0502  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2474 0.2707 0.5700 -0.0110 0.0382  0.0575  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2764 0.2949 0.6333 -0.0096 0.0559  0.0643  45  THR   A C   
312  O O   . THR   A 39  ? 0.2820 0.2900 0.6307 -0.0097 0.0752  0.0609  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2569 0.2811 0.5646 -0.0110 0.0365  0.0543  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2778 0.2924 0.5767 -0.0111 0.0566  0.0503  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2719 0.2994 0.5461 -0.0121 0.0222  0.0475  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2889 0.3140 0.6836 -0.0088 0.0500  0.0741  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3148 0.3363 0.7490 -0.0070 0.0672  0.0822  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3192 0.3352 0.7556 -0.0060 0.0820  0.0814  46  THR   A C   
319  O O   . THR   A 40  ? 0.3323 0.3382 0.7827 -0.0048 0.1053  0.0823  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3458 0.3776 0.8244 -0.0071 0.0524  0.0950  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3900 0.4298 0.8714 -0.0081 0.0353  0.0988  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3458 0.3818 0.8217 -0.0088 0.0373  0.0953  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3122 0.3336 0.7343 -0.0065 0.0700  0.0794  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3129 0.3298 0.7371 -0.0056 0.0824  0.0787  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3197 0.3279 0.6971 -0.0072 0.0903  0.0657  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.3243 0.3343 0.6685 -0.0088 0.0788  0.0588  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3125 0.3406 0.7533 -0.0054 0.0646  0.0861  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3124 0.3105 0.6884 -0.0072 0.1097  0.0628  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.3228 0.3113 0.6564 -0.0098 0.1173  0.0513  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2918 0.2891 0.6085 -0.0099 0.1007  0.0489  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2787 0.2836 0.6196 -0.0081 0.0941  0.0558  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.3848 0.3575 0.7231 -0.0105 0.1442  0.0489  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.4861 0.4444 0.8286 -0.0115 0.1654  0.0483  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6202 0.5594 0.9190 -0.0165 0.1816  0.0367  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6782 0.6001 0.9785 -0.0182 0.2062  0.0342  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6392 0.5802 0.8981 -0.0197 0.1682  0.0297  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.2692 0.2651 0.5459 -0.0123 0.0940  0.0399  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.2661 0.2684 0.5240 -0.0126 0.0812  0.0366  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.2689 0.2619 0.5126 -0.0144 0.0948  0.0309  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.2972 0.2763 0.5358 -0.0166 0.1142  0.0272  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.2411 0.2400 0.4758 -0.0141 0.0852  0.0297  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.2511 0.2422 0.4751 -0.0158 0.0966  0.0248  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2571 0.2474 0.4447 -0.0188 0.0900  0.0165  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2831 0.2675 0.4612 -0.0206 0.0974  0.0125  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2505 0.2480 0.5024 -0.0128 0.0948  0.0319  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3031 0.3020 0.6054 -0.0095 0.1032  0.0439  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2518 0.2480 0.4213 -0.0192 0.0761  0.0146  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.2559 0.2524 0.3952 -0.0219 0.0693  0.0083  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.2762 0.2593 0.3899 -0.0276 0.0801  0.0016  51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2965 0.2716 0.4115 -0.0290 0.0895  0.0018  51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.2539 0.2613 0.3862 -0.0200 0.0513  0.0095  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3053 0.3228 0.4531 -0.0162 0.0391  0.0149  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3331 0.3515 0.4892 -0.0153 0.0411  0.0166  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.2649 0.2883 0.4154 -0.0148 0.0275  0.0175  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.2807 0.2603 0.3713 -0.0315 0.0788  -0.0037 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3066 0.2730 0.3687 -0.0386 0.0854  -0.0095 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2986 0.2729 0.3423 -0.0401 0.0693  -0.0102 52  THR   A C   
358  O O   . THR   A 46  ? 0.2967 0.2806 0.3428 -0.0378 0.0596  -0.0097 52  THR   A O   
359  C CB  . THR   A 46  ? 0.3500 0.3042 0.4004 -0.0435 0.0967  -0.0147 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3861 0.3306 0.4540 -0.0424 0.1146  -0.0140 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3826 0.3227 0.3980 -0.0528 0.0993  -0.0207 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.2943 0.2641 0.3215 -0.0439 0.0672  -0.0108 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.2865 0.2635 0.2999 -0.0455 0.0528  -0.0103 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3012 0.2692 0.2902 -0.0535 0.0532  -0.0142 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.3265 0.2784 0.2980 -0.0604 0.0639  -0.0176 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.2893 0.2662 0.2982 -0.0461 0.0493  -0.0077 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.2924 0.2752 0.3251 -0.0396 0.0505  -0.0040 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.2988 0.2843 0.2989 -0.0469 0.0344  -0.0057 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.2999 0.2975 0.3506 -0.0329 0.0389  -0.0013 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.2707 0.2477 0.2573 -0.0534 0.0417  -0.0137 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.2908 0.2610 0.2565 -0.0615 0.0389  -0.0162 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3008 0.2640 0.2455 -0.0688 0.0341  -0.0147 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.2964 0.2672 0.2472 -0.0656 0.0272  -0.0105 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.2821 0.2655 0.2557 -0.0586 0.0270  -0.0141 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3249 0.2728 0.2440 -0.0793 0.0371  -0.0178 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.3430 0.2826 0.2383 -0.0883 0.0306  -0.0156 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.3544 0.2917 0.2351 -0.0966 0.0212  -0.0160 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.3864 0.3071 0.2463 -0.1054 0.0281  -0.0212 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.3617 0.2802 0.2360 -0.0947 0.0451  -0.0192 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.3767 0.2973 0.2696 -0.0864 0.0558  -0.0183 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.3844 0.3205 0.2928 -0.0799 0.0449  -0.0119 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.3830 0.3206 0.3109 -0.0725 0.0549  -0.0112 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.3784 0.3294 0.3255 -0.0653 0.0480  -0.0067 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.3466 0.3096 0.2954 -0.0642 0.0329  -0.0027 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.3753 0.3270 0.3411 -0.0596 0.0566  -0.0058 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.3373 0.2904 0.2301 -0.0942 0.0058  -0.0104 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.3383 0.2939 0.2276 -0.0998 -0.0040 -0.0095 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.3315 0.3046 0.2377 -0.0964 -0.0200 -0.0012 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.3220 0.3045 0.2418 -0.0894 -0.0223 0.0028  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.3065 0.2654 0.2101 -0.0940 0.0040  -0.0143 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2999 0.2806 0.2387 -0.0784 0.0023  -0.0111 56  CYS   A SG  
392  N N   A ASP   A 51  ? 0.3348 0.3120 0.2428 -0.1011 -0.0301 0.0015  57  ASP   A N   
393  N N   B ASP   A 51  ? 0.3455 0.3222 0.2528 -0.1014 -0.0299 0.0012  57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.3273 0.3210 0.2564 -0.0972 -0.0431 0.0097  57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.3506 0.3424 0.2764 -0.0997 -0.0441 0.0094  57  ASP   A CA  
396  C C   A ASP   A 51  ? 0.3224 0.3269 0.2727 -0.0905 -0.0423 0.0089  57  ASP   A C   
397  C C   B ASP   A 51  ? 0.3313 0.3341 0.2790 -0.0923 -0.0424 0.0082  57  ASP   A C   
398  O O   A ASP   A 51  ? 0.3147 0.3295 0.2800 -0.0904 -0.0524 0.0154  57  ASP   A O   
399  O O   B ASP   A 51  ? 0.3204 0.3318 0.2807 -0.0936 -0.0524 0.0139  57  ASP   A O   
400  C CB  A ASP   A 51  ? 0.3443 0.3353 0.2618 -0.1090 -0.0585 0.0173  57  ASP   A CB  
401  C CB  B ASP   A 51  ? 0.4016 0.3864 0.3100 -0.1138 -0.0575 0.0142  57  ASP   A CB  
402  C CG  A ASP   A 51  ? 0.3889 0.3700 0.2897 -0.1210 -0.0637 0.0157  57  ASP   A CG  
403  C CG  B ASP   A 51  ? 0.4958 0.4942 0.4222 -0.1139 -0.0732 0.0255  57  ASP   A CG  
404  O OD1 A ASP   A 51  ? 0.3745 0.3503 0.2725 -0.1200 -0.0540 0.0081  57  ASP   A OD1 
405  O OD1 B ASP   A 51  ? 0.5104 0.5202 0.4563 -0.1044 -0.0727 0.0293  57  ASP   A OD1 
406  O OD2 A ASP   A 51  ? 0.4529 0.4305 0.3425 -0.1323 -0.0780 0.0224  57  ASP   A OD2 
407  O OD2 B ASP   A 51  ? 0.5513 0.5484 0.4732 -0.1240 -0.0861 0.0310  57  ASP   A OD2 
408  N N   . CYS   A 52  ? 0.3142 0.3162 0.2672 -0.0851 -0.0300 0.0018  58  CYS   A N   
409  C CA  . CYS   A 52  ? 0.2917 0.3026 0.2632 -0.0783 -0.0277 0.0009  58  CYS   A CA  
410  C C   . CYS   A 52  ? 0.2663 0.2922 0.2608 -0.0699 -0.0334 0.0070  58  CYS   A C   
411  O O   . CYS   A 52  ? 0.2566 0.2866 0.2563 -0.0652 -0.0343 0.0095  58  CYS   A O   
412  C CB  . CYS   A 52  ? 0.2935 0.3011 0.2678 -0.0719 -0.0142 -0.0055 58  CYS   A CB  
413  S SG  . CYS   A 52  ? 0.3088 0.2982 0.2623 -0.0805 -0.0035 -0.0133 58  CYS   A SG  
414  N N   . GLN   A 53  ? 0.2459 0.2787 0.2541 -0.0683 -0.0362 0.0092  59  GLN   A N   
415  C CA  . GLN   A 53  ? 0.2227 0.2674 0.2533 -0.0601 -0.0382 0.0141  59  GLN   A CA  
416  C C   . GLN   A 53  ? 0.2143 0.2618 0.2550 -0.0530 -0.0302 0.0110  59  GLN   A C   
417  O O   . GLN   A 53  ? 0.2030 0.2578 0.2604 -0.0475 -0.0304 0.0146  59  GLN   A O   
418  C CB  . GLN   A 53  ? 0.2450 0.2963 0.2878 -0.0645 -0.0496 0.0228  59  GLN   A CB  
419  C CG  . GLN   A 53  ? 0.2665 0.3192 0.3082 -0.0675 -0.0577 0.0288  59  GLN   A CG  
420  C CD  . GLN   A 53  ? 0.3239 0.3850 0.3849 -0.0706 -0.0689 0.0393  59  GLN   A CD  
421  O OE1 . GLN   A 53  ? 0.3742 0.4327 0.4282 -0.0814 -0.0802 0.0442  59  GLN   A OE1 
422  N NE2 . GLN   A 53  ? 0.3047 0.3751 0.3908 -0.0618 -0.0658 0.0433  59  GLN   A NE2 
423  N N   . THR   A 54  ? 0.2027 0.2433 0.2336 -0.0535 -0.0225 0.0047  60  THR   A N   
424  C CA  . THR   A 54  ? 0.2033 0.2459 0.2425 -0.0468 -0.0150 0.0023  60  THR   A CA  
425  C C   . THR   A 54  ? 0.1925 0.2297 0.2247 -0.0436 -0.0071 -0.0025 60  THR   A C   
426  O O   . THR   A 54  ? 0.2274 0.2571 0.2476 -0.0485 -0.0051 -0.0053 60  THR   A O   
427  C CB  . THR   A 54  ? 0.2368 0.2778 0.2777 -0.0508 -0.0141 0.0013  60  THR   A CB  
428  O OG1 . THR   A 54  ? 0.2866 0.3174 0.3116 -0.0585 -0.0117 -0.0034 60  THR   A OG1 
429  C CG2 . THR   A 54  ? 0.2280 0.2747 0.2793 -0.0545 -0.0226 0.0071  60  THR   A CG2 
430  N N   . GLY   A 55  ? 0.1795 0.2200 0.2200 -0.0358 -0.0028 -0.0025 61  GLY   A N   
431  C CA  . GLY   A 55  ? 0.1796 0.2168 0.2187 -0.0324 0.0031  -0.0050 61  GLY   A CA  
432  C C   . GLY   A 55  ? 0.1708 0.2114 0.2179 -0.0253 0.0051  -0.0036 61  GLY   A C   
433  O O   . GLY   A 55  ? 0.1918 0.2354 0.2438 -0.0234 0.0050  -0.0021 61  GLY   A O   
434  N N   . VAL   A 56  ? 0.1505 0.1895 0.1987 -0.0221 0.0073  -0.0038 62  VAL   A N   
435  C CA  . VAL   A 56  ? 0.1419 0.1822 0.1944 -0.0167 0.0077  -0.0019 62  VAL   A CA  
436  C C   . VAL   A 56  ? 0.1566 0.1968 0.2082 -0.0142 0.0041  -0.0010 62  VAL   A C   
437  O O   . VAL   A 56  ? 0.1816 0.2204 0.2335 -0.0159 0.0043  -0.0016 62  VAL   A O   
438  C CB  . VAL   A 56  ? 0.1657 0.2035 0.2231 -0.0164 0.0130  -0.0018 62  VAL   A CB  
439  C CG1 . VAL   A 56  ? 0.1800 0.2184 0.2403 -0.0118 0.0116  0.0015  62  VAL   A CG1 
440  C CG2 . VAL   A 56  ? 0.2004 0.2374 0.2586 -0.0191 0.0169  -0.0033 62  VAL   A CG2 
441  N N   . TYR   A 57  ? 0.1582 0.1984 0.2080 -0.0106 0.0016  0.0005  63  TYR   A N   
442  C CA  . TYR   A 57  ? 0.1420 0.1806 0.1899 -0.0092 -0.0025 0.0012  63  TYR   A CA  
443  C C   . TYR   A 57  ? 0.1609 0.1963 0.2064 -0.0071 -0.0043 0.0033  63  TYR   A C   
444  O O   . TYR   A 57  ? 0.1763 0.2102 0.2190 -0.0059 -0.0023 0.0041  63  TYR   A O   
445  C CB  . TYR   A 57  ? 0.1489 0.1877 0.1936 -0.0085 -0.0048 0.0006  63  TYR   A CB  
446  C CG  . TYR   A 57  ? 0.1615 0.1974 0.2018 -0.0058 -0.0037 0.0009  63  TYR   A CG  
447  C CD1 . TYR   A 57  ? 0.1725 0.2099 0.2155 -0.0053 0.0001  0.0014  63  TYR   A CD1 
448  C CD2 . TYR   A 57  ? 0.1867 0.2168 0.2197 -0.0044 -0.0057 0.0006  63  TYR   A CD2 
449  C CE1 . TYR   A 57  ? 0.1922 0.2253 0.2320 -0.0026 0.0036  0.0017  63  TYR   A CE1 
450  C CE2 . TYR   A 57  ? 0.1893 0.2134 0.2154 -0.0025 -0.0023 0.0001  63  TYR   A CE2 
451  C CZ  . TYR   A 57  ? 0.1963 0.2219 0.2264 -0.0012 0.0033  0.0008  63  TYR   A CZ  
452  O OH  . TYR   A 57  ? 0.2074 0.2255 0.2315 0.0009  0.0090  0.0004  63  TYR   A OH  
453  N N   . TYR   A 58  ? 0.1519 0.1857 0.1985 -0.0072 -0.0088 0.0047  64  TYR   A N   
454  C CA  . TYR   A 58  ? 0.1726 0.2021 0.2150 -0.0068 -0.0134 0.0077  64  TYR   A CA  
455  C C   . TYR   A 58  ? 0.1855 0.2090 0.2147 -0.0064 -0.0163 0.0061  64  TYR   A C   
456  O O   . TYR   A 58  ? 0.1896 0.2126 0.2185 -0.0069 -0.0188 0.0046  64  TYR   A O   
457  C CB  . TYR   A 58  ? 0.1755 0.2059 0.2282 -0.0079 -0.0180 0.0114  64  TYR   A CB  
458  C CG  . TYR   A 58  ? 0.1924 0.2181 0.2399 -0.0088 -0.0253 0.0158  64  TYR   A CG  
459  C CD1 . TYR   A 58  ? 0.2033 0.2273 0.2481 -0.0085 -0.0246 0.0188  64  TYR   A CD1 
460  C CD2 . TYR   A 58  ? 0.2147 0.2368 0.2596 -0.0107 -0.0337 0.0175  64  TYR   A CD2 
461  C CE1 . TYR   A 58  ? 0.2192 0.2374 0.2565 -0.0104 -0.0326 0.0237  64  TYR   A CE1 
462  C CE2 . TYR   A 58  ? 0.2353 0.2513 0.2725 -0.0131 -0.0423 0.0221  64  TYR   A CE2 
463  C CZ  . TYR   A 58  ? 0.2468 0.2609 0.2800 -0.0131 -0.0420 0.0255  64  TYR   A CZ  
464  O OH  . TYR   A 58  ? 0.3038 0.3104 0.3261 -0.0166 -0.0516 0.0307  64  TYR   A OH  
465  N N   . CYS   A 59  ? 0.1956 0.2125 0.2131 -0.0060 -0.0158 0.0069  65  CYS   A N   
466  C CA  . CYS   A 59  ? 0.2145 0.2216 0.2158 -0.0063 -0.0163 0.0050  65  CYS   A CA  
467  C C   . CYS   A 59  ? 0.2367 0.2353 0.2263 -0.0092 -0.0240 0.0082  65  CYS   A C   
468  O O   . CYS   A 59  ? 0.2465 0.2413 0.2293 -0.0097 -0.0237 0.0110  65  CYS   A O   
469  C CB  . CYS   A 59  ? 0.2293 0.2332 0.2249 -0.0042 -0.0077 0.0032  65  CYS   A CB  
470  S SG  . CYS   A 59  ? 0.2633 0.2510 0.2372 -0.0046 -0.0041 0.0003  65  CYS   A SG  
471  N N   . SER   A 60  ? 0.2272 0.2229 0.2148 -0.0118 -0.0319 0.0086  66  SER   A N   
472  C CA  . SER   A 60  ? 0.2423 0.2298 0.2194 -0.0161 -0.0420 0.0127  66  SER   A CA  
473  C C   . SER   A 60  ? 0.2713 0.2430 0.2210 -0.0184 -0.0409 0.0112  66  SER   A C   
474  O O   . SER   A 60  ? 0.2952 0.2601 0.2341 -0.0220 -0.0478 0.0160  66  SER   A O   
475  C CB  . SER   A 60  ? 0.2690 0.2560 0.2504 -0.0189 -0.0510 0.0134  66  SER   A CB  
476  O OG  . SER   A 60  ? 0.3386 0.3170 0.3062 -0.0197 -0.0491 0.0077  66  SER   A OG  
477  N N   . SER   A 61  ? 0.2693 0.2339 0.2077 -0.0167 -0.0317 0.0051  67  SER   A N   
478  C CA  . SER   A 61  ? 0.2919 0.2383 0.2025 -0.0190 -0.0273 0.0028  67  SER   A CA  
479  C C   . SER   A 61  ? 0.3023 0.2478 0.2092 -0.0171 -0.0205 0.0051  67  SER   A C   
480  O O   . SER   A 61  ? 0.3260 0.2553 0.2087 -0.0193 -0.0161 0.0041  67  SER   A O   
481  C CB  . SER   A 61  ? 0.2974 0.2357 0.2008 -0.0174 -0.0175 -0.0038 67  SER   A CB  
482  O OG  . SER   A 61  ? 0.3251 0.2747 0.2474 -0.0118 -0.0073 -0.0051 67  SER   A OG  
483  N N   . ARG   A 62  ? 0.2833 0.2443 0.2124 -0.0136 -0.0190 0.0082  68  ARG   A N   
484  C CA  . ARG   A 62  ? 0.2871 0.2486 0.2158 -0.0121 -0.0137 0.0111  68  ARG   A CA  
485  C C   . ARG   A 62  ? 0.2797 0.2507 0.2226 -0.0129 -0.0216 0.0178  68  ARG   A C   
486  O O   . ARG   A 62  ? 0.2860 0.2584 0.2310 -0.0117 -0.0181 0.0212  68  ARG   A O   
487  C CB  . ARG   A 62  ? 0.2863 0.2561 0.2296 -0.0070 -0.0017 0.0083  68  ARG   A CB  
488  C CG  . ARG   A 62  ? 0.2957 0.2561 0.2296 -0.0055 0.0085  0.0034  68  ARG   A CG  
489  C CD  . ARG   A 62  ? 0.3291 0.2727 0.2401 -0.0065 0.0159  0.0035  68  ARG   A CD  
490  N NE  . ARG   A 62  ? 0.3690 0.3021 0.2735 -0.0046 0.0284  -0.0010 68  ARG   A NE  
491  C CZ  . ARG   A 62  ? 0.4031 0.3202 0.2877 -0.0074 0.0299  -0.0049 68  ARG   A CZ  
492  N NH1 . ARG   A 62  ? 0.3918 0.3018 0.2597 -0.0127 0.0180  -0.0048 68  ARG   A NH1 
493  N NH2 . ARG   A 62  ? 0.4120 0.3191 0.2938 -0.0052 0.0438  -0.0087 68  ARG   A NH2 
494  N N   . ARG   A 63  ? 0.2729 0.2511 0.2290 -0.0146 -0.0313 0.0204  69  ARG   A N   
495  C CA  . ARG   A 63  ? 0.2708 0.2593 0.2477 -0.0146 -0.0366 0.0270  69  ARG   A CA  
496  C C   . ARG   A 63  ? 0.2670 0.2654 0.2601 -0.0104 -0.0264 0.0260  69  ARG   A C   
497  O O   . ARG   A 63  ? 0.2821 0.2829 0.2825 -0.0101 -0.0261 0.0311  69  ARG   A O   
498  C CB  . ARG   A 63  ? 0.2865 0.2677 0.2537 -0.0188 -0.0464 0.0350  69  ARG   A CB  
499  C CG  . ARG   A 63  ? 0.3161 0.2882 0.2697 -0.0246 -0.0593 0.0371  69  ARG   A CG  
500  C CD  . ARG   A 63  ? 0.3925 0.3580 0.3380 -0.0299 -0.0713 0.0468  69  ARG   A CD  
501  N NE  . ARG   A 63  ? 0.4386 0.3930 0.3673 -0.0370 -0.0854 0.0489  69  ARG   A NE  
502  C CZ  . ARG   A 63  ? 0.5027 0.4392 0.3989 -0.0436 -0.0923 0.0509  69  ARG   A CZ  
503  N NH1 . ARG   A 63  ? 0.5184 0.4463 0.3959 -0.0433 -0.0851 0.0510  69  ARG   A NH1 
504  N NH2 . ARG   A 63  ? 0.5105 0.4361 0.3909 -0.0512 -0.1060 0.0524  69  ARG   A NH2 
505  N N   . LYS   A 64  ? 0.2392 0.2425 0.2379 -0.0077 -0.0186 0.0199  70  LYS   A N   
506  C CA  . LYS   A 64  ? 0.2134 0.2240 0.2242 -0.0050 -0.0098 0.0185  70  LYS   A CA  
507  C C   . LYS   A 64  ? 0.2034 0.2223 0.2272 -0.0043 -0.0071 0.0145  70  LYS   A C   
508  O O   . LYS   A 64  ? 0.2294 0.2474 0.2497 -0.0047 -0.0091 0.0116  70  LYS   A O   
509  C CB  . LYS   A 64  ? 0.2758 0.2807 0.2749 -0.0033 -0.0019 0.0160  70  LYS   A CB  
510  C CG  . LYS   A 64  ? 0.4248 0.4225 0.4134 -0.0038 -0.0015 0.0205  70  LYS   A CG  
511  C CD  . LYS   A 64  ? 0.5360 0.5316 0.5224 -0.0014 0.0089  0.0191  70  LYS   A CD  
512  C CE  . LYS   A 64  ? 0.6316 0.6188 0.6058 -0.0022 0.0096  0.0240  70  LYS   A CE  
513  N NZ  . LYS   A 64  ? 0.6944 0.6672 0.6434 -0.0056 0.0039  0.0254  70  LYS   A NZ  
514  N N   . HIS   A 65  ? 0.1786 0.2038 0.2153 -0.0038 -0.0022 0.0143  71  HIS   A N   
515  C CA  . HIS   A 65  ? 0.1704 0.2013 0.2161 -0.0045 0.0009  0.0106  71  HIS   A CA  
516  C C   . HIS   A 65  ? 0.2037 0.2360 0.2486 -0.0039 0.0066  0.0081  71  HIS   A C   
517  O O   . HIS   A 65  ? 0.2299 0.2626 0.2782 -0.0035 0.0107  0.0093  71  HIS   A O   
518  C CB  . HIS   A 65  ? 0.1782 0.2123 0.2377 -0.0056 0.0031  0.0122  71  HIS   A CB  
519  C CG  . HIS   A 65  ? 0.1971 0.2308 0.2633 -0.0060 -0.0023 0.0163  71  HIS   A CG  
520  N ND1 . HIS   A 65  ? 0.2185 0.2537 0.2913 -0.0070 -0.0031 0.0153  71  HIS   A ND1 
521  C CD2 . HIS   A 65  ? 0.1975 0.2292 0.2652 -0.0059 -0.0077 0.0223  71  HIS   A CD2 
522  C CE1 . HIS   A 65  ? 0.2092 0.2442 0.2903 -0.0072 -0.0085 0.0207  71  HIS   A CE1 
523  N NE2 . HIS   A 65  ? 0.2126 0.2455 0.2905 -0.0069 -0.0126 0.0254  71  HIS   A NE2 
524  N N   . TYR   A 66  ? 0.1766 0.2098 0.2191 -0.0040 0.0066  0.0055  72  TYR   A N   
525  C CA  . TYR   A 66  ? 0.1653 0.2004 0.2104 -0.0037 0.0108  0.0047  72  TYR   A CA  
526  C C   . TYR   A 66  ? 0.1566 0.1969 0.2090 -0.0069 0.0105  0.0030  72  TYR   A C   
527  O O   . TYR   A 66  ? 0.1722 0.2138 0.2240 -0.0085 0.0072  0.0019  72  TYR   A O   
528  C CB  . TYR   A 66  ? 0.1752 0.2070 0.2151 -0.0018 0.0114  0.0043  72  TYR   A CB  
529  C CG  . TYR   A 66  ? 0.1928 0.2159 0.2207 0.0003  0.0134  0.0052  72  TYR   A CG  
530  C CD1 . TYR   A 66  ? 0.2193 0.2389 0.2455 0.0018  0.0196  0.0067  72  TYR   A CD1 
531  C CD2 . TYR   A 66  ? 0.2090 0.2256 0.2257 0.0000  0.0096  0.0046  72  TYR   A CD2 
532  C CE1 . TYR   A 66  ? 0.2414 0.2501 0.2524 0.0029  0.0222  0.0074  72  TYR   A CE1 
533  C CE2 . TYR   A 66  ? 0.2263 0.2318 0.2272 0.0004  0.0111  0.0051  72  TYR   A CE2 
534  C CZ  . TYR   A 66  ? 0.2495 0.2504 0.2464 0.0018  0.0180  0.0063  72  TYR   A CZ  
535  O OH  . TYR   A 66  ? 0.2887 0.2759 0.2659 0.0013  0.0203  0.0068  72  TYR   A OH  
536  N N   . PRO   A 67  ? 0.1630 0.2053 0.2209 -0.0084 0.0135  0.0031  73  PRO   A N   
537  C CA  . PRO   A 67  ? 0.1563 0.2015 0.2178 -0.0130 0.0118  0.0018  73  PRO   A CA  
538  C C   . PRO   A 67  ? 0.1800 0.2282 0.2452 -0.0128 0.0091  0.0036  73  PRO   A C   
539  O O   . PRO   A 67  ? 0.2065 0.2547 0.2761 -0.0096 0.0122  0.0056  73  PRO   A O   
540  C CB  . PRO   A 67  ? 0.1910 0.2365 0.2578 -0.0147 0.0156  0.0019  73  PRO   A CB  
541  C CG  . PRO   A 67  ? 0.2243 0.2683 0.2918 -0.0100 0.0196  0.0040  73  PRO   A CG  
542  C CD  . PRO   A 67  ? 0.1902 0.2312 0.2503 -0.0066 0.0181  0.0047  73  PRO   A CD  
543  N N   . VAL   A 68  ? 0.1626 0.2126 0.2272 -0.0164 0.0043  0.0035  74  VAL   A N   
544  C CA  . VAL   A 68  ? 0.1679 0.2213 0.2393 -0.0161 0.0012  0.0066  74  VAL   A CA  
545  C C   . VAL   A 68  ? 0.1802 0.2362 0.2533 -0.0228 -0.0052 0.0081  74  VAL   A C   
546  O O   . VAL   A 68  ? 0.2015 0.2546 0.2653 -0.0275 -0.0070 0.0055  74  VAL   A O   
547  C CB  . VAL   A 68  ? 0.1954 0.2472 0.2634 -0.0127 0.0004  0.0064  74  VAL   A CB  
548  C CG1 . VAL   A 68  ? 0.2224 0.2696 0.2872 -0.0071 0.0058  0.0059  74  VAL   A CG1 
549  C CG2 . VAL   A 68  ? 0.2188 0.2688 0.2782 -0.0147 -0.0024 0.0039  74  VAL   A CG2 
550  N N   . SER   A 69  ? 0.1649 0.2255 0.2501 -0.0234 -0.0085 0.0130  75  SER   A N   
551  C CA  . SER   A 69  ? 0.1612 0.2247 0.2491 -0.0298 -0.0171 0.0167  75  SER   A CA  
552  C C   . SER   A 69  ? 0.1672 0.2321 0.2577 -0.0267 -0.0187 0.0189  75  SER   A C   
553  O O   . SER   A 69  ? 0.1701 0.2350 0.2674 -0.0202 -0.0134 0.0194  75  SER   A O   
554  C CB  . SER   A 69  ? 0.2051 0.2739 0.3102 -0.0321 -0.0206 0.0228  75  SER   A CB  
555  O OG  . SER   A 69  ? 0.2946 0.3618 0.3979 -0.0353 -0.0193 0.0207  75  SER   A OG  
556  N N   . PHE   A 70  ? 0.1491 0.2134 0.2323 -0.0314 -0.0249 0.0196  76  PHE   A N   
557  C CA  . PHE   A 70  ? 0.1522 0.2176 0.2382 -0.0285 -0.0262 0.0216  76  PHE   A CA  
558  C C   . PHE   A 70  ? 0.1657 0.2340 0.2551 -0.0347 -0.0356 0.0278  76  PHE   A C   
559  O O   . PHE   A 70  ? 0.1929 0.2596 0.2741 -0.0427 -0.0418 0.0287  76  PHE   A O   
560  C CB  . PHE   A 70  ? 0.1685 0.2287 0.2406 -0.0260 -0.0224 0.0159  76  PHE   A CB  
561  C CG  . PHE   A 70  ? 0.1759 0.2312 0.2328 -0.0314 -0.0230 0.0121  76  PHE   A CG  
562  C CD1 . PHE   A 70  ? 0.1826 0.2344 0.2337 -0.0314 -0.0178 0.0076  76  PHE   A CD1 
563  C CD2 . PHE   A 70  ? 0.1895 0.2426 0.2381 -0.0366 -0.0275 0.0132  76  PHE   A CD2 
564  C CE1 . PHE   A 70  ? 0.1979 0.2435 0.2366 -0.0363 -0.0160 0.0041  76  PHE   A CE1 
565  C CE2 . PHE   A 70  ? 0.2028 0.2486 0.2363 -0.0417 -0.0253 0.0092  76  PHE   A CE2 
566  C CZ  . PHE   A 70  ? 0.1936 0.2355 0.2228 -0.0417 -0.0192 0.0046  76  PHE   A CZ  
567  N N   . SER   A 71  ? 0.1641 0.2356 0.2646 -0.0316 -0.0370 0.0323  77  SER   A N   
568  C CA  . SER   A 71  ? 0.1884 0.2636 0.2952 -0.0372 -0.0468 0.0401  77  SER   A CA  
569  C C   . SER   A 71  ? 0.2037 0.2739 0.2911 -0.0425 -0.0511 0.0383  77  SER   A C   
570  O O   . SER   A 71  ? 0.2229 0.2877 0.2963 -0.0402 -0.0449 0.0311  77  SER   A O   
571  C CB  . SER   A 71  ? 0.2018 0.2820 0.3312 -0.0316 -0.0452 0.0464  77  SER   A CB  
572  O OG  . SER   A 71  ? 0.2197 0.2962 0.3437 -0.0259 -0.0391 0.0420  77  SER   A OG  
573  N N   . LYS   A 72  ? 0.2273 0.2985 0.3133 -0.0502 -0.0615 0.0454  78  LYS   A N   
574  C CA  . LYS   A 72  ? 0.2521 0.3168 0.3181 -0.0552 -0.0641 0.0439  78  LYS   A CA  
575  C C   . LYS   A 72  ? 0.2464 0.3129 0.3198 -0.0486 -0.0607 0.0446  78  LYS   A C   
576  O O   . LYS   A 72  ? 0.2496 0.3225 0.3443 -0.0433 -0.0605 0.0496  78  LYS   A O   
577  C CB  . LYS   A 72  ? 0.2874 0.3506 0.3461 -0.0669 -0.0773 0.0517  78  LYS   A CB  
578  C CG  . LYS   A 72  ? 0.3609 0.4175 0.4032 -0.0757 -0.0803 0.0486  78  LYS   A CG  
579  C CD  . LYS   A 72  ? 0.4296 0.4807 0.4565 -0.0894 -0.0939 0.0553  78  LYS   A CD  
580  C CE  . LYS   A 72  ? 0.4875 0.5315 0.5000 -0.0982 -0.0965 0.0517  78  LYS   A CE  
581  N NZ  . LYS   A 72  ? 0.5438 0.5773 0.5321 -0.1135 -0.1090 0.0561  78  LYS   A NZ  
582  N N   . PRO   A 73  ? 0.2406 0.3007 0.2975 -0.0496 -0.0579 0.0404  79  PRO   A N   
583  C CA  . PRO   A 73  ? 0.2336 0.2950 0.2976 -0.0436 -0.0546 0.0406  79  PRO   A CA  
584  C C   . PRO   A 73  ? 0.2248 0.2921 0.3052 -0.0441 -0.0618 0.0507  79  PRO   A C   
585  O O   . PRO   A 73  ? 0.2362 0.3034 0.3120 -0.0522 -0.0713 0.0578  79  PRO   A O   
586  C CB  . PRO   A 73  ? 0.2643 0.3174 0.3082 -0.0467 -0.0515 0.0359  79  PRO   A CB  
587  C CG  . PRO   A 73  ? 0.2906 0.3375 0.3189 -0.0509 -0.0484 0.0302  79  PRO   A CG  
588  C CD  . PRO   A 73  ? 0.2533 0.3038 0.2862 -0.0554 -0.0552 0.0344  79  PRO   A CD  
589  N N   A SER   A 74  ? 0.2051 0.2765 0.3043 -0.0363 -0.0573 0.0517  80  SER   A N   
590  N N   B SER   A 74  ? 0.2072 0.2786 0.3065 -0.0363 -0.0573 0.0517  80  SER   A N   
591  C CA  A SER   A 74  ? 0.2063 0.2838 0.3269 -0.0356 -0.0621 0.0618  80  SER   A CA  
592  C CA  B SER   A 74  ? 0.2103 0.2877 0.3309 -0.0355 -0.0620 0.0617  80  SER   A CA  
593  C C   A SER   A 74  ? 0.2072 0.2840 0.3386 -0.0279 -0.0549 0.0601  80  SER   A C   
594  C C   B SER   A 74  ? 0.2084 0.2853 0.3407 -0.0276 -0.0546 0.0601  80  SER   A C   
595  O O   A SER   A 74  ? 0.2097 0.2813 0.3315 -0.0236 -0.0473 0.0512  80  SER   A O   
596  O O   B SER   A 74  ? 0.2084 0.2804 0.3325 -0.0228 -0.0465 0.0510  80  SER   A O   
597  C CB  A SER   A 74  ? 0.2150 0.2988 0.3567 -0.0346 -0.0634 0.0674  80  SER   A CB  
598  C CB  B SER   A 74  ? 0.2256 0.3094 0.3665 -0.0355 -0.0647 0.0681  80  SER   A CB  
599  O OG  A SER   A 74  ? 0.2664 0.3498 0.3986 -0.0401 -0.0674 0.0662  80  SER   A OG  
600  O OG  B SER   A 74  ? 0.2859 0.3705 0.4182 -0.0446 -0.0745 0.0720  80  SER   A OG  
601  N N   . LEU   A 75  ? 0.2021 0.2836 0.3547 -0.0269 -0.0578 0.0693  81  LEU   A N   
602  C CA  . LEU   A 75  ? 0.2090 0.2891 0.3744 -0.0203 -0.0507 0.0687  81  LEU   A CA  
603  C C   . LEU   A 75  ? 0.2181 0.2988 0.4031 -0.0141 -0.0423 0.0685  81  LEU   A C   
604  O O   . LEU   A 75  ? 0.2187 0.3057 0.4251 -0.0151 -0.0454 0.0777  81  LEU   A O   
605  C CB  . LEU   A 75  ? 0.2091 0.2936 0.3884 -0.0231 -0.0583 0.0802  81  LEU   A CB  
606  C CG  . LEU   A 75  ? 0.2369 0.3190 0.4269 -0.0177 -0.0521 0.0800  81  LEU   A CG  
607  C CD1 . LEU   A 75  ? 0.2349 0.3098 0.4034 -0.0165 -0.0477 0.0696  81  LEU   A CD1 
608  C CD2 . LEU   A 75  ? 0.2585 0.3459 0.4647 -0.0208 -0.0603 0.0932  81  LEU   A CD2 
609  N N   . ILE   A 76  ? 0.2187 0.2921 0.3960 -0.0086 -0.0318 0.0585  82  ILE   A N   
610  C CA  . ILE   A 76  ? 0.2320 0.3021 0.4204 -0.0033 -0.0214 0.0561  82  ILE   A CA  
611  C C   . ILE   A 76  ? 0.2323 0.2933 0.4232 0.0022  -0.0106 0.0509  82  ILE   A C   
612  O O   . ILE   A 76  ? 0.2193 0.2749 0.3939 0.0022  -0.0106 0.0443  82  ILE   A O   
613  C CB  . ILE   A 76  ? 0.2704 0.3375 0.4402 -0.0038 -0.0194 0.0481  82  ILE   A CB  
614  C CG1 . ILE   A 76  ? 0.2996 0.3743 0.4702 -0.0094 -0.0284 0.0534  82  ILE   A CG1 
615  C CG2 . ILE   A 76  ? 0.2824 0.3421 0.4554 0.0017  -0.0069 0.0432  82  ILE   A CG2 
616  C CD1 . ILE   A 76  ? 0.3273 0.3990 0.4795 -0.0103 -0.0267 0.0458  82  ILE   A CD1 
617  N N   . PHE   A 77  ? 0.2302 0.2887 0.4427 0.0065  -0.0011 0.0544  83  PHE   A N   
618  C CA  . PHE   A 77  ? 0.2381 0.2848 0.4505 0.0110  0.0108  0.0486  83  PHE   A CA  
619  C C   . PHE   A 77  ? 0.2416 0.2761 0.4283 0.0122  0.0181  0.0365  83  PHE   A C   
620  O O   . PHE   A 77  ? 0.2544 0.2884 0.4375 0.0126  0.0211  0.0351  83  PHE   A O   
621  C CB  . PHE   A 77  ? 0.2508 0.2963 0.4945 0.0150  0.0211  0.0558  83  PHE   A CB  
622  C CG  . PHE   A 77  ? 0.2992 0.3321 0.5439 0.0184  0.0323  0.0510  83  PHE   A CG  
623  C CD1 . PHE   A 77  ? 0.3224 0.3576 0.5714 0.0175  0.0270  0.0537  83  PHE   A CD1 
624  C CD2 . PHE   A 77  ? 0.3389 0.3557 0.5767 0.0218  0.0483  0.0430  83  PHE   A CD2 
625  C CE1 . PHE   A 77  ? 0.3457 0.3686 0.5958 0.0201  0.0374  0.0489  83  PHE   A CE1 
626  C CE2 . PHE   A 77  ? 0.3602 0.3628 0.5953 0.0237  0.0587  0.0374  83  PHE   A CE2 
627  C CZ  . PHE   A 77  ? 0.3583 0.3645 0.6012 0.0230  0.0531  0.0405  83  PHE   A CZ  
628  N N   . VAL   A 78  ? 0.2278 0.2529 0.3962 0.0120  0.0192  0.0284  84  VAL   A N   
629  C CA  . VAL   A 78  ? 0.2430 0.2557 0.3857 0.0119  0.0236  0.0180  84  VAL   A CA  
630  C C   . VAL   A 78  ? 0.2628 0.2590 0.4015 0.0139  0.0350  0.0123  84  VAL   A C   
631  O O   . VAL   A 78  ? 0.2618 0.2561 0.4046 0.0137  0.0339  0.0123  84  VAL   A O   
632  C CB  . VAL   A 78  ? 0.2452 0.2609 0.3682 0.0084  0.0126  0.0139  84  VAL   A CB  
633  C CG1 . VAL   A 78  ? 0.2574 0.2603 0.3561 0.0076  0.0152  0.0047  84  VAL   A CG1 
634  C CG2 . VAL   A 78  ? 0.2473 0.2758 0.3709 0.0059  0.0039  0.0181  84  VAL   A CG2 
635  N N   . GLU   A 79  ? 0.2788 0.2613 0.4074 0.0153  0.0465  0.0070  85  GLU   A N   
636  C CA  . GLU   A 79  ? 0.2983 0.2608 0.4179 0.0160  0.0592  0.0003  85  GLU   A CA  
637  C C   . GLU   A 79  ? 0.3158 0.2683 0.4112 0.0123  0.0533  -0.0076 85  GLU   A C   
638  O O   . GLU   A 79  ? 0.2983 0.2568 0.3793 0.0094  0.0412  -0.0092 85  GLU   A O   
639  C CB  . GLU   A 79  ? 0.3473 0.2949 0.4544 0.0170  0.0725  -0.0043 85  GLU   A CB  
640  C CG  . GLU   A 79  ? 0.3935 0.3479 0.5288 0.0211  0.0816  0.0037  85  GLU   A CG  
641  C CD  . GLU   A 79  ? 0.4918 0.4450 0.6574 0.0246  0.0919  0.0094  85  GLU   A CD  
642  O OE1 . GLU   A 79  ? 0.5244 0.4620 0.6828 0.0244  0.1003  0.0039  85  GLU   A OE1 
643  O OE2 . GLU   A 79  ? 0.4970 0.4649 0.6948 0.0270  0.0910  0.0201  85  GLU   A OE2 
644  N N   . ALA   A 80  ? 0.3312 0.2668 0.4221 0.0120  0.0627  -0.0126 86  ALA   A N   
645  C CA  . ALA   A 80  ? 0.3614 0.2857 0.4297 0.0076  0.0568  -0.0200 86  ALA   A CA  
646  C C   . ALA   A 80  ? 0.3758 0.2903 0.4120 0.0034  0.0520  -0.0266 86  ALA   A C   
647  O O   . ALA   A 80  ? 0.3887 0.2950 0.4144 0.0039  0.0600  -0.0284 86  ALA   A O   
648  C CB  . ALA   A 80  ? 0.3722 0.2763 0.4386 0.0074  0.0699  -0.0252 86  ALA   A CB  
649  N N   . SER   A 81  ? 0.3699 0.2863 0.3933 -0.0008 0.0387  -0.0288 87  SER   A N   
650  C CA  . SER   A 81  ? 0.3740 0.2828 0.3703 -0.0055 0.0309  -0.0331 87  SER   A CA  
651  C C   . SER   A 81  ? 0.3980 0.2941 0.3777 -0.0113 0.0234  -0.0384 87  SER   A C   
652  O O   . SER   A 81  ? 0.4098 0.3019 0.3983 -0.0112 0.0264  -0.0396 87  SER   A O   
653  C CB  . SER   A 81  ? 0.3605 0.2898 0.3646 -0.0048 0.0190  -0.0276 87  SER   A CB  
654  O OG  . SER   A 81  ? 0.3533 0.2946 0.3691 -0.0056 0.0084  -0.0247 87  SER   A OG  
655  N N   . GLU   A 82  ? 0.4106 0.3019 0.3692 -0.0166 0.0125  -0.0405 88  GLU   A N   
656  C CA  . GLU   A 82  ? 0.4294 0.3108 0.3748 -0.0231 0.0023  -0.0438 88  GLU   A CA  
657  C C   . GLU   A 82  ? 0.4081 0.3071 0.3775 -0.0216 -0.0071 -0.0391 88  GLU   A C   
658  O O   . GLU   A 82  ? 0.4182 0.3094 0.3849 -0.0255 -0.0118 -0.0417 88  GLU   A O   
659  C CB  . GLU   A 82  ? 0.4929 0.3685 0.4153 -0.0291 -0.0094 -0.0444 88  GLU   A CB  
660  C CG  . GLU   A 82  ? 0.6157 0.4656 0.5049 -0.0337 -0.0019 -0.0506 88  GLU   A CG  
661  C CD  . GLU   A 82  ? 0.7649 0.6060 0.6284 -0.0414 -0.0152 -0.0505 88  GLU   A CD  
662  O OE1 . GLU   A 82  ? 0.8287 0.6469 0.6609 -0.0462 -0.0097 -0.0554 88  GLU   A OE1 
663  O OE2 . GLU   A 82  ? 0.7774 0.6334 0.6522 -0.0427 -0.0305 -0.0450 88  GLU   A OE2 
664  N N   . TYR   A 83  ? 0.3703 0.2915 0.3621 -0.0166 -0.0091 -0.0324 89  TYR   A N   
665  C CA  . TYR   A 83  ? 0.3560 0.2924 0.3672 -0.0158 -0.0173 -0.0277 89  TYR   A CA  
666  C C   . TYR   A 83  ? 0.3351 0.2828 0.3699 -0.0109 -0.0115 -0.0235 89  TYR   A C   
667  O O   . TYR   A 83  ? 0.3409 0.2967 0.3886 -0.0110 -0.0170 -0.0204 89  TYR   A O   
668  C CB  . TYR   A 83  ? 0.3573 0.3081 0.3726 -0.0157 -0.0260 -0.0232 89  TYR   A CB  
669  C CG  . TYR   A 83  ? 0.3979 0.3408 0.3970 -0.0213 -0.0360 -0.0247 89  TYR   A CG  
670  C CD1 . TYR   A 83  ? 0.4113 0.3554 0.4157 -0.0250 -0.0465 -0.0232 89  TYR   A CD1 
671  C CD2 . TYR   A 83  ? 0.4340 0.3683 0.4139 -0.0232 -0.0353 -0.0267 89  TYR   A CD2 
672  C CE1 . TYR   A 83  ? 0.4435 0.3811 0.4360 -0.0308 -0.0575 -0.0229 89  TYR   A CE1 
673  C CE2 . TYR   A 83  ? 0.4590 0.3856 0.4238 -0.0291 -0.0461 -0.0267 89  TYR   A CE2 
674  C CZ  . TYR   A 83  ? 0.4802 0.4090 0.4524 -0.0331 -0.0579 -0.0244 89  TYR   A CZ  
675  O OH  . TYR   A 83  ? 0.5331 0.4550 0.4933 -0.0397 -0.0703 -0.0227 89  TYR   A OH  
676  N N   . TYR   A 84  ? 0.3118 0.2601 0.3537 -0.0069 -0.0011 -0.0222 90  TYR   A N   
677  C CA  . TYR   A 84  ? 0.2981 0.2564 0.3634 -0.0029 0.0033  -0.0167 90  TYR   A CA  
678  C C   . TYR   A 84  ? 0.3159 0.2638 0.3856 -0.0003 0.0169  -0.0180 90  TYR   A C   
679  O O   . TYR   A 84  ? 0.3354 0.2754 0.3947 0.0002  0.0238  -0.0207 90  TYR   A O   
680  C CB  . TYR   A 84  ? 0.2701 0.2474 0.3491 -0.0004 0.0000  -0.0092 90  TYR   A CB  
681  C CG  . TYR   A 84  ? 0.2545 0.2421 0.3312 -0.0024 -0.0103 -0.0072 90  TYR   A CG  
682  C CD1 . TYR   A 84  ? 0.2480 0.2430 0.3351 -0.0030 -0.0153 -0.0036 90  TYR   A CD1 
683  C CD2 . TYR   A 84  ? 0.2583 0.2484 0.3245 -0.0034 -0.0135 -0.0081 90  TYR   A CD2 
684  C CE1 . TYR   A 84  ? 0.2437 0.2466 0.3301 -0.0047 -0.0222 -0.0017 90  TYR   A CE1 
685  C CE2 . TYR   A 84  ? 0.2521 0.2507 0.3188 -0.0050 -0.0208 -0.0060 90  TYR   A CE2 
686  C CZ  . TYR   A 84  ? 0.2516 0.2564 0.3287 -0.0056 -0.0245 -0.0029 90  TYR   A CZ  
687  O OH  . TYR   A 84  ? 0.2370 0.2483 0.3154 -0.0071 -0.0293 -0.0008 90  TYR   A OH  
688  N N   . PRO   A 85  ? 0.3178 0.2665 0.4062 0.0020  0.0221  -0.0150 91  PRO   A N   
689  C CA  . PRO   A 85  ? 0.3193 0.2616 0.4201 0.0056  0.0362  -0.0136 91  PRO   A CA  
690  C C   . PRO   A 85  ? 0.3022 0.2605 0.4203 0.0091  0.0365  -0.0052 91  PRO   A C   
691  O O   . PRO   A 85  ? 0.2898 0.2635 0.4093 0.0083  0.0257  -0.0008 91  PRO   A O   
692  C CB  . PRO   A 85  ? 0.3282 0.2707 0.4486 0.0070  0.0391  -0.0105 91  PRO   A CB  
693  C CG  . PRO   A 85  ? 0.3271 0.2859 0.4538 0.0058  0.0253  -0.0054 91  PRO   A CG  
694  C CD  . PRO   A 85  ? 0.3073 0.2651 0.4103 0.0019  0.0157  -0.0107 91  PRO   A CD  
695  N N   . ALA   A 86  ? 0.2923 0.2468 0.4254 0.0126  0.0490  -0.0025 92  ALA   A N   
696  C CA  . ALA   A 86  ? 0.2845 0.2543 0.4375 0.0153  0.0483  0.0067  92  ALA   A CA  
697  C C   . ALA   A 86  ? 0.2700 0.2584 0.4432 0.0152  0.0372  0.0166  92  ALA   A C   
698  O O   . ALA   A 86  ? 0.2817 0.2697 0.4675 0.0158  0.0379  0.0193  92  ALA   A O   
699  C CB  . ALA   A 86  ? 0.2897 0.2517 0.4613 0.0192  0.0645  0.0092  92  ALA   A CB  
700  N N   . ARG   A 87  ? 0.2441 0.2470 0.4170 0.0137  0.0268  0.0215  93  ARG   A N   
701  C CA  . ARG   A 87  ? 0.2210 0.2391 0.4063 0.0121  0.0157  0.0305  93  ARG   A CA  
702  C C   . ARG   A 87  ? 0.2240 0.2544 0.4102 0.0102  0.0080  0.0361  93  ARG   A C   
703  O O   . ARG   A 87  ? 0.2475 0.2753 0.4231 0.0104  0.0105  0.0318  93  ARG   A O   
704  C CB  . ARG   A 87  ? 0.2259 0.2432 0.3940 0.0092  0.0078  0.0257  93  ARG   A CB  
705  C CG  . ARG   A 87  ? 0.2479 0.2673 0.3942 0.0065  0.0011  0.0208  93  ARG   A CG  
706  C CD  . ARG   A 87  ? 0.2454 0.2577 0.3747 0.0046  -0.0018 0.0133  93  ARG   A CD  
707  N NE  . ARG   A 87  ? 0.2318 0.2504 0.3494 0.0018  -0.0098 0.0127  93  ARG   A NE  
708  C CZ  . ARG   A 87  ? 0.2485 0.2676 0.3547 0.0011  -0.0108 0.0099  93  ARG   A CZ  
709  N NH1 . ARG   A 87  ? 0.2393 0.2630 0.3374 -0.0012 -0.0167 0.0095  93  ARG   A NH1 
710  N NH2 . ARG   A 87  ? 0.2280 0.2414 0.3308 0.0027  -0.0047 0.0072  93  ARG   A NH2 
711  N N   . TYR   A 88  ? 0.2062 0.2487 0.4016 0.0075  -0.0021 0.0450  94  TYR   A N   
712  C CA  . TYR   A 88  ? 0.2138 0.2656 0.4043 0.0040  -0.0107 0.0490  94  TYR   A CA  
713  C C   . TYR   A 88  ? 0.2047 0.2557 0.3704 0.0007  -0.0167 0.0426  94  TYR   A C   
714  O O   . TYR   A 88  ? 0.2173 0.2675 0.3781 -0.0006 -0.0197 0.0421  94  TYR   A O   
715  C CB  . TYR   A 88  ? 0.2211 0.2837 0.4296 0.0011  -0.0194 0.0620  94  TYR   A CB  
716  C CG  . TYR   A 88  ? 0.2310 0.2971 0.4689 0.0038  -0.0151 0.0708  94  TYR   A CG  
717  C CD1 . TYR   A 88  ? 0.2466 0.3179 0.4922 0.0028  -0.0166 0.0748  94  TYR   A CD1 
718  C CD2 . TYR   A 88  ? 0.2528 0.3163 0.5131 0.0075  -0.0082 0.0752  94  TYR   A CD2 
719  C CE1 . TYR   A 88  ? 0.2646 0.3395 0.5416 0.0054  -0.0121 0.0841  94  TYR   A CE1 
720  C CE2 . TYR   A 88  ? 0.2610 0.3277 0.5528 0.0103  -0.0028 0.0844  94  TYR   A CE2 
721  C CZ  . TYR   A 88  ? 0.2738 0.3462 0.5746 0.0094  -0.0045 0.0889  94  TYR   A CZ  
722  O OH  . TYR   A 88  ? 0.2987 0.3746 0.6346 0.0123  0.0014  0.0990  94  TYR   A OH  
723  N N   . GLN   A 89  ? 0.1845 0.2361 0.3368 -0.0007 -0.0179 0.0386  95  GLN   A N   
724  C CA  . GLN   A 89  ? 0.1893 0.2404 0.3215 -0.0038 -0.0224 0.0335  95  GLN   A CA  
725  C C   . GLN   A 89  ? 0.1861 0.2447 0.3159 -0.0088 -0.0300 0.0394  95  GLN   A C   
726  O O   . GLN   A 89  ? 0.1931 0.2558 0.3302 -0.0095 -0.0311 0.0433  95  GLN   A O   
727  C CB  . GLN   A 89  ? 0.1925 0.2374 0.3108 -0.0022 -0.0181 0.0249  95  GLN   A CB  
728  C CG  . GLN   A 89  ? 0.2069 0.2517 0.3090 -0.0051 -0.0221 0.0208  95  GLN   A CG  
729  C CD  . GLN   A 89  ? 0.1961 0.2340 0.2862 -0.0037 -0.0193 0.0133  95  GLN   A CD  
730  O OE1 . GLN   A 89  ? 0.2165 0.2468 0.3049 -0.0017 -0.0157 0.0095  95  GLN   A OE1 
731  N NE2 . GLN   A 89  ? 0.2028 0.2422 0.2835 -0.0056 -0.0211 0.0113  95  GLN   A NE2 
732  N N   . SER   A 90  ? 0.1859 0.2449 0.3055 -0.0127 -0.0349 0.0403  96  SER   A N   
733  C CA  . SER   A 90  ? 0.1881 0.2504 0.2999 -0.0190 -0.0417 0.0450  96  SER   A CA  
734  C C   . SER   A 90  ? 0.1835 0.2426 0.2772 -0.0213 -0.0403 0.0382  96  SER   A C   
735  O O   . SER   A 90  ? 0.1947 0.2499 0.2828 -0.0181 -0.0353 0.0309  96  SER   A O   
736  C CB  . SER   A 90  ? 0.1974 0.2594 0.3059 -0.0227 -0.0460 0.0501  96  SER   A CB  
737  O OG  . SER   A 90  ? 0.2254 0.2820 0.3234 -0.0217 -0.0419 0.0437  96  SER   A OG  
738  N N   . HIS   A 91  ? 0.1742 0.2346 0.2598 -0.0274 -0.0453 0.0413  97  HIS   A N   
739  C CA  . HIS   A 91  ? 0.1771 0.2335 0.2463 -0.0305 -0.0434 0.0356  97  HIS   A CA  
740  C C   . HIS   A 91  ? 0.1746 0.2314 0.2472 -0.0255 -0.0382 0.0298  97  HIS   A C   
741  O O   . HIS   A 91  ? 0.1780 0.2310 0.2407 -0.0254 -0.0343 0.0239  97  HIS   A O   
742  C CB  . HIS   A 91  ? 0.1978 0.2478 0.2538 -0.0320 -0.0398 0.0315  97  HIS   A CB  
743  C CG  . HIS   A 91  ? 0.2421 0.2897 0.2914 -0.0375 -0.0439 0.0373  97  HIS   A CG  
744  N ND1 . HIS   A 91  ? 0.2928 0.3346 0.3240 -0.0457 -0.0462 0.0386  97  HIS   A ND1 
745  C CD2 . HIS   A 91  ? 0.2482 0.2972 0.3054 -0.0363 -0.0459 0.0421  97  HIS   A CD2 
746  C CE1 . HIS   A 91  ? 0.2984 0.3379 0.3254 -0.0495 -0.0498 0.0444  97  HIS   A CE1 
747  N NE2 . HIS   A 91  ? 0.2734 0.3180 0.3172 -0.0437 -0.0500 0.0472  97  HIS   A NE2 
748  N N   . LEU   A 92  ? 0.1771 0.2379 0.2640 -0.0220 -0.0377 0.0323  98  LEU   A N   
749  C CA  . LEU   A 92  ? 0.1824 0.2418 0.2708 -0.0175 -0.0319 0.0272  98  LEU   A CA  
750  C C   . LEU   A 92  ? 0.1847 0.2473 0.2753 -0.0199 -0.0336 0.0293  98  LEU   A C   
751  O O   . LEU   A 92  ? 0.1932 0.2606 0.2938 -0.0231 -0.0390 0.0365  98  LEU   A O   
752  C CB  . LEU   A 92  ? 0.1866 0.2450 0.2881 -0.0117 -0.0274 0.0278  98  LEU   A CB  
753  C CG  . LEU   A 92  ? 0.2040 0.2575 0.3030 -0.0073 -0.0201 0.0221  98  LEU   A CG  
754  C CD1 . LEU   A 92  ? 0.2106 0.2587 0.2946 -0.0069 -0.0191 0.0153  98  LEU   A CD1 
755  C CD2 . LEU   A 92  ? 0.2244 0.2739 0.3345 -0.0028 -0.0140 0.0226  98  LEU   A CD2 
756  N N   . MET   A 93  ? 0.1669 0.2271 0.2497 -0.0189 -0.0296 0.0237  99  MET   A N   
757  C CA  . MET   A 93  ? 0.1585 0.2212 0.2438 -0.0210 -0.0303 0.0251  99  MET   A CA  
758  C C   . MET   A 93  ? 0.1670 0.2283 0.2582 -0.0151 -0.0232 0.0225  99  MET   A C   
759  O O   . MET   A 93  ? 0.1817 0.2379 0.2647 -0.0117 -0.0187 0.0171  99  MET   A O   
760  C CB  . MET   A 93  ? 0.1711 0.2305 0.2406 -0.0253 -0.0305 0.0207  99  MET   A CB  
761  C CG  . MET   A 93  ? 0.1965 0.2536 0.2552 -0.0322 -0.0355 0.0224  99  MET   A CG  
762  S SD  . MET   A 93  ? 0.2472 0.2967 0.2875 -0.0364 -0.0313 0.0160  99  MET   A SD  
763  C CE  . MET   A 93  ? 0.2679 0.3155 0.3099 -0.0294 -0.0245 0.0110  99  MET   A CE  
764  N N   . LEU   A 94  ? 0.1588 0.2235 0.2636 -0.0143 -0.0221 0.0266  100 LEU   A N   
765  C CA  . LEU   A 94  ? 0.1575 0.2187 0.2660 -0.0090 -0.0135 0.0242  100 LEU   A CA  
766  C C   . LEU   A 94  ? 0.1531 0.2155 0.2599 -0.0105 -0.0125 0.0233  100 LEU   A C   
767  O O   . LEU   A 94  ? 0.1740 0.2412 0.2844 -0.0156 -0.0186 0.0267  100 LEU   A O   
768  C CB  . LEU   A 94  ? 0.1638 0.2263 0.2931 -0.0055 -0.0090 0.0298  100 LEU   A CB  
769  C CG  . LEU   A 94  ? 0.1910 0.2518 0.3265 -0.0033 -0.0081 0.0314  100 LEU   A CG  
770  C CD1 . LEU   A 94  ? 0.2152 0.2758 0.3738 0.0006  -0.0007 0.0368  100 LEU   A CD1 
771  C CD2 . LEU   A 94  ? 0.2139 0.2660 0.3317 -0.0010 -0.0043 0.0236  100 LEU   A CD2 
772  N N   . ALA   A 95  ? 0.1609 0.2180 0.2621 -0.0065 -0.0051 0.0191  101 ALA   A N   
773  C CA  . ALA   A 95  ? 0.1558 0.2132 0.2574 -0.0066 -0.0020 0.0186  101 ALA   A CA  
774  C C   . ALA   A 95  ? 0.1600 0.2110 0.2637 -0.0011 0.0082  0.0176  101 ALA   A C   
775  O O   . ALA   A 95  ? 0.1707 0.2148 0.2693 0.0021  0.0127  0.0154  101 ALA   A O   
776  C CB  . ALA   A 95  ? 0.1577 0.2126 0.2429 -0.0084 -0.0032 0.0134  101 ALA   A CB  
777  N N   . VAL   A 96  ? 0.1519 0.2038 0.2630 -0.0004 0.0124  0.0193  102 VAL   A N   
778  C CA  . VAL   A 96  ? 0.1559 0.1997 0.2653 0.0042  0.0235  0.0180  102 VAL   A CA  
779  C C   . VAL   A 96  ? 0.1908 0.2278 0.2785 0.0045  0.0246  0.0125  102 VAL   A C   
780  O O   . VAL   A 96  ? 0.2115 0.2517 0.2958 0.0024  0.0217  0.0118  102 VAL   A O   
781  C CB  . VAL   A 96  ? 0.1588 0.2064 0.2875 0.0049  0.0282  0.0231  102 VAL   A CB  
782  C CG1 . VAL   A 96  ? 0.1755 0.2125 0.3005 0.0096  0.0418  0.0216  102 VAL   A CG1 
783  C CG2 . VAL   A 96  ? 0.1598 0.2147 0.3136 0.0042  0.0256  0.0304  102 VAL   A CG2 
784  N N   . GLY   A 97  ? 0.2050 0.2320 0.2783 0.0065  0.0282  0.0090  103 GLY   A N   
785  C CA  . GLY   A 97  ? 0.2310 0.2511 0.2841 0.0061  0.0273  0.0052  103 GLY   A CA  
786  C C   . GLY   A 97  ? 0.2418 0.2495 0.2786 0.0069  0.0298  0.0018  103 GLY   A C   
787  O O   . GLY   A 97  ? 0.2482 0.2522 0.2890 0.0081  0.0333  0.0016  103 GLY   A O   
788  N N   . HIS   A 98  ? 0.2407 0.2412 0.2590 0.0057  0.0274  -0.0003 104 HIS   A N   
789  C CA  . HIS   A 98  ? 0.2534 0.2397 0.2522 0.0048  0.0283  -0.0035 104 HIS   A CA  
790  C C   . HIS   A 98  ? 0.2489 0.2372 0.2443 0.0025  0.0185  -0.0049 104 HIS   A C   
791  O O   . HIS   A 98  ? 0.2386 0.2357 0.2386 0.0011  0.0108  -0.0036 104 HIS   A O   
792  C CB  . HIS   A 98  ? 0.2759 0.2514 0.2549 0.0036  0.0297  -0.0038 104 HIS   A CB  
793  C CG  . HIS   A 98  ? 0.3259 0.2835 0.2806 0.0013  0.0306  -0.0070 104 HIS   A CG  
794  N ND1 . HIS   A 98  ? 0.3685 0.3122 0.3155 0.0024  0.0422  -0.0098 104 HIS   A ND1 
795  C CD2 . HIS   A 98  ? 0.3465 0.2978 0.2846 -0.0027 0.0210  -0.0077 104 HIS   A CD2 
796  C CE1 . HIS   A 98  ? 0.3816 0.3093 0.3037 -0.0015 0.0395  -0.0130 104 HIS   A CE1 
797  N NE2 . HIS   A 98  ? 0.3725 0.3048 0.2889 -0.0049 0.0257  -0.0114 104 HIS   A NE2 
798  N N   . SER   A 99  ? 0.2595 0.2387 0.2473 0.0021  0.0199  -0.0076 105 SER   A N   
799  C CA  . SER   A 99  ? 0.2677 0.2477 0.2533 -0.0001 0.0113  -0.0088 105 SER   A CA  
800  C C   . SER   A 99  ? 0.2962 0.2588 0.2630 -0.0020 0.0137  -0.0128 105 SER   A C   
801  O O   . SER   A 99  ? 0.3252 0.2792 0.2911 -0.0002 0.0242  -0.0146 105 SER   A O   
802  C CB  . SER   A 99  ? 0.3027 0.2945 0.3084 0.0013  0.0101  -0.0073 105 SER   A CB  
803  O OG  . SER   A 99  ? 0.3880 0.3817 0.3940 -0.0006 0.0025  -0.0080 105 SER   A OG  
804  N N   . GLU   A 100 ? 0.2898 0.2467 0.2431 -0.0060 0.0043  -0.0138 106 GLU   A N   
805  C CA  . GLU   A 100 ? 0.3122 0.2520 0.2462 -0.0095 0.0037  -0.0178 106 GLU   A CA  
806  C C   . GLU   A 100 ? 0.3113 0.2580 0.2542 -0.0113 -0.0067 -0.0173 106 GLU   A C   
807  O O   . GLU   A 100 ? 0.2898 0.2518 0.2487 -0.0104 -0.0135 -0.0137 106 GLU   A O   
808  C CB  . GLU   A 100 ? 0.3481 0.2717 0.2544 -0.0142 0.0006  -0.0185 106 GLU   A CB  
809  C CG  . GLU   A 100 ? 0.3803 0.2965 0.2776 -0.0123 0.0120  -0.0186 106 GLU   A CG  
810  C CD  . GLU   A 100 ? 0.4705 0.3697 0.3382 -0.0173 0.0098  -0.0185 106 GLU   A CD  
811  O OE1 . GLU   A 100 ? 0.4994 0.3863 0.3472 -0.0235 0.0006  -0.0197 106 GLU   A OE1 
812  O OE2 . GLU   A 100 ? 0.4517 0.3496 0.3162 -0.0156 0.0162  -0.0166 106 GLU   A OE2 
813  N N   . PRO   A 101 ? 0.3239 0.2595 0.2583 -0.0136 -0.0069 -0.0209 107 PRO   A N   
814  C CA  . PRO   A 101 ? 0.3141 0.2572 0.2601 -0.0149 -0.0160 -0.0200 107 PRO   A CA  
815  C C   . PRO   A 101 ? 0.3054 0.2572 0.2564 -0.0175 -0.0290 -0.0158 107 PRO   A C   
816  O O   . PRO   A 101 ? 0.2879 0.2536 0.2584 -0.0159 -0.0327 -0.0131 107 PRO   A O   
817  C CB  . PRO   A 101 ? 0.3435 0.2681 0.2724 -0.0187 -0.0150 -0.0251 107 PRO   A CB  
818  C CG  . PRO   A 101 ? 0.3530 0.2648 0.2722 -0.0165 0.0003  -0.0288 107 PRO   A CG  
819  C CD  . PRO   A 101 ? 0.3411 0.2556 0.2558 -0.0151 0.0029  -0.0263 107 PRO   A CD  
820  N N   . GLY   A 102 ? 0.3019 0.2450 0.2362 -0.0217 -0.0352 -0.0146 108 GLY   A N   
821  C CA  . GLY   A 102 ? 0.3016 0.2526 0.2441 -0.0242 -0.0474 -0.0091 108 GLY   A CA  
822  C C   . GLY   A 102 ? 0.2791 0.2466 0.2408 -0.0202 -0.0455 -0.0049 108 GLY   A C   
823  O O   . GLY   A 102 ? 0.2809 0.2562 0.2551 -0.0213 -0.0531 0.0000  108 GLY   A O   
824  N N   . ASP   A 103 ? 0.2606 0.2328 0.2264 -0.0158 -0.0349 -0.0065 109 ASP   A N   
825  C CA  . ASP   A 103 ? 0.2306 0.2173 0.2137 -0.0126 -0.0323 -0.0035 109 ASP   A CA  
826  C C   . ASP   A 103 ? 0.2216 0.2197 0.2234 -0.0110 -0.0323 -0.0030 109 ASP   A C   
827  O O   . ASP   A 103 ? 0.2156 0.2237 0.2301 -0.0098 -0.0311 -0.0007 109 ASP   A O   
828  C CB  . ASP   A 103 ? 0.2241 0.2116 0.2057 -0.0094 -0.0222 -0.0049 109 ASP   A CB  
829  C CG  . ASP   A 103 ? 0.2825 0.2599 0.2472 -0.0105 -0.0206 -0.0045 109 ASP   A CG  
830  O OD1 . ASP   A 103 ? 0.2738 0.2499 0.2346 -0.0132 -0.0279 -0.0012 109 ASP   A OD1 
831  O OD2 . ASP   A 103 ? 0.2753 0.2460 0.2323 -0.0088 -0.0114 -0.0068 109 ASP   A OD2 
832  N N   . CYS   A 104 ? 0.2121 0.2078 0.2149 -0.0114 -0.0332 -0.0050 110 CYS   A N   
833  C CA  . CYS   A 104 ? 0.1963 0.2017 0.2152 -0.0103 -0.0331 -0.0039 110 CYS   A CA  
834  C C   . CYS   A 104 ? 0.2025 0.2140 0.2327 -0.0116 -0.0383 -0.0002 110 CYS   A C   
835  O O   . CYS   A 104 ? 0.2249 0.2321 0.2532 -0.0143 -0.0456 0.0017  110 CYS   A O   
836  C CB  . CYS   A 104 ? 0.2039 0.2046 0.2223 -0.0108 -0.0341 -0.0060 110 CYS   A CB  
837  S SG  . CYS   A 104 ? 0.2413 0.2372 0.2556 -0.0082 -0.0249 -0.0092 110 CYS   A SG  
838  N N   . GLY   A 105 ? 0.1786 0.1988 0.2208 -0.0105 -0.0346 0.0011  111 GLY   A N   
839  C CA  . GLY   A 105 ? 0.1866 0.2114 0.2415 -0.0114 -0.0361 0.0045  111 GLY   A CA  
840  C C   . GLY   A 105 ? 0.1845 0.2125 0.2417 -0.0108 -0.0321 0.0058  111 GLY   A C   
841  O O   . GLY   A 105 ? 0.1948 0.2264 0.2640 -0.0111 -0.0295 0.0081  111 GLY   A O   
842  N N   . GLY   A 106 ? 0.1846 0.2103 0.2313 -0.0099 -0.0304 0.0044  112 GLY   A N   
843  C CA  . GLY   A 106 ? 0.1734 0.2020 0.2225 -0.0094 -0.0262 0.0054  112 GLY   A CA  
844  C C   . GLY   A 106 ? 0.1770 0.2105 0.2316 -0.0095 -0.0198 0.0040  112 GLY   A C   
845  O O   . GLY   A 106 ? 0.1849 0.2194 0.2362 -0.0095 -0.0184 0.0020  112 GLY   A O   
846  N N   . ILE   A 107 ? 0.1701 0.2055 0.2329 -0.0102 -0.0159 0.0054  113 ILE   A N   
847  C CA  . ILE   A 107 ? 0.1660 0.2028 0.2299 -0.0118 -0.0096 0.0035  113 ILE   A CA  
848  C C   . ILE   A 107 ? 0.1614 0.1990 0.2184 -0.0123 -0.0067 0.0015  113 ILE   A C   
849  O O   . ILE   A 107 ? 0.1807 0.2183 0.2372 -0.0112 -0.0060 0.0021  113 ILE   A O   
850  C CB  . ILE   A 107 ? 0.1995 0.2352 0.2748 -0.0128 -0.0044 0.0052  113 ILE   A CB  
851  C CG1 . ILE   A 107 ? 0.2160 0.2512 0.2996 -0.0130 -0.0059 0.0070  113 ILE   A CG1 
852  C CG2 . ILE   A 107 ? 0.2222 0.2557 0.2940 -0.0156 0.0039  0.0024  113 ILE   A CG2 
853  C CD1 . ILE   A 107 ? 0.2434 0.2774 0.3441 -0.0132 -0.0005 0.0103  113 ILE   A CD1 
854  N N   . LEU   A 108 ? 0.1585 0.1967 0.2111 -0.0147 -0.0052 -0.0001 114 LEU   A N   
855  C CA  . LEU   A 108 ? 0.1665 0.2054 0.2147 -0.0169 -0.0031 -0.0013 114 LEU   A CA  
856  C C   . LEU   A 108 ? 0.1890 0.2239 0.2353 -0.0212 0.0024  -0.0029 114 LEU   A C   
857  O O   . LEU   A 108 ? 0.1831 0.2153 0.2274 -0.0234 0.0035  -0.0031 114 LEU   A O   
858  C CB  . LEU   A 108 ? 0.1599 0.2011 0.2049 -0.0178 -0.0069 -0.0006 114 LEU   A CB  
859  C CG  . LEU   A 108 ? 0.1748 0.2170 0.2169 -0.0217 -0.0070 -0.0005 114 LEU   A CG  
860  C CD1 . LEU   A 108 ? 0.1790 0.2230 0.2244 -0.0197 -0.0055 -0.0003 114 LEU   A CD1 
861  C CD2 . LEU   A 108 ? 0.1787 0.2239 0.2216 -0.0231 -0.0122 0.0023  114 LEU   A CD2 
862  N N   . ARG   A 109 ? 0.1961 0.2292 0.2424 -0.0226 0.0068  -0.0041 115 ARG   A N   
863  C CA  . ARG   A 109 ? 0.2209 0.2473 0.2632 -0.0274 0.0139  -0.0066 115 ARG   A CA  
864  C C   . ARG   A 109 ? 0.2127 0.2368 0.2477 -0.0318 0.0151  -0.0087 115 ARG   A C   
865  O O   . ARG   A 109 ? 0.2037 0.2323 0.2416 -0.0301 0.0125  -0.0078 115 ARG   A O   
866  C CB  . ARG   A 109 ? 0.2695 0.2930 0.3223 -0.0255 0.0210  -0.0060 115 ARG   A CB  
867  C CG  . ARG   A 109 ? 0.3633 0.3913 0.4268 -0.0208 0.0193  -0.0032 115 ARG   A CG  
868  C CD  . ARG   A 109 ? 0.4269 0.4524 0.5048 -0.0195 0.0253  -0.0008 115 ARG   A CD  
869  N NE  . ARG   A 109 ? 0.4596 0.4893 0.5477 -0.0159 0.0189  0.0038  115 ARG   A NE  
870  C CZ  . ARG   A 109 ? 0.4550 0.4833 0.5548 -0.0155 0.0210  0.0063  115 ARG   A CZ  
871  N NH1 . ARG   A 109 ? 0.4264 0.4485 0.5281 -0.0181 0.0312  0.0042  115 ARG   A NH1 
872  N NH2 . ARG   A 109 ? 0.4209 0.4530 0.5300 -0.0131 0.0132  0.0110  115 ARG   A NH2 
873  N N   . CYS   A 110 ? 0.2231 0.2392 0.2470 -0.0384 0.0189  -0.0113 116 CYS   A N   
874  C CA  . CYS   A 110 ? 0.2489 0.2599 0.2632 -0.0448 0.0200  -0.0139 116 CYS   A CA  
875  C C   . CYS   A 110 ? 0.2827 0.2820 0.2933 -0.0483 0.0321  -0.0180 116 CYS   A C   
876  O O   . CYS   A 110 ? 0.2933 0.2901 0.3122 -0.0450 0.0394  -0.0178 116 CYS   A O   
877  C CB  . CYS   A 110 ? 0.2514 0.2599 0.2516 -0.0517 0.0129  -0.0133 116 CYS   A CB  
878  S SG  . CYS   A 110 ? 0.2667 0.2625 0.2505 -0.0579 0.0182  -0.0154 116 CYS   A SG  
879  N N   . GLN   A 111 ? 0.3143 0.3051 0.3128 -0.0557 0.0347  -0.0216 117 GLN   A N   
880  C CA  . GLN   A 111 ? 0.3493 0.3262 0.3423 -0.0600 0.0481  -0.0263 117 GLN   A CA  
881  C C   . GLN   A 111 ? 0.3658 0.3311 0.3490 -0.0632 0.0562  -0.0283 117 GLN   A C   
882  O O   . GLN   A 111 ? 0.3984 0.3529 0.3839 -0.0639 0.0703  -0.0312 117 GLN   A O   
883  C CB  . GLN   A 111 ? 0.3957 0.3635 0.3737 -0.0689 0.0482  -0.0303 117 GLN   A CB  
884  C CG  . GLN   A 111 ? 0.4509 0.4111 0.4052 -0.0791 0.0406  -0.0313 117 GLN   A CG  
885  C CD  . GLN   A 111 ? 0.5222 0.4733 0.4619 -0.0890 0.0385  -0.0347 117 GLN   A CD  
886  O OE1 . GLN   A 111 ? 0.5212 0.4810 0.4637 -0.0907 0.0262  -0.0313 117 GLN   A OE1 
887  N NE2 . GLN   A 111 ? 0.5453 0.4776 0.4694 -0.0963 0.0509  -0.0412 117 GLN   A NE2 
888  N N   . HIS   A 112 ? 0.3458 0.3130 0.3203 -0.0646 0.0488  -0.0262 118 HIS   A N   
889  C CA  . HIS   A 112 ? 0.3574 0.3128 0.3207 -0.0681 0.0566  -0.0277 118 HIS   A CA  
890  C C   . HIS   A 112 ? 0.3519 0.3142 0.3345 -0.0597 0.0595  -0.0241 118 HIS   A C   
891  O O   . HIS   A 112 ? 0.3789 0.3314 0.3579 -0.0613 0.0689  -0.0250 118 HIS   A O   
892  C CB  . HIS   A 112 ? 0.3655 0.3162 0.3054 -0.0763 0.0473  -0.0271 118 HIS   A CB  
893  C CG  . HIS   A 112 ? 0.3688 0.3122 0.2897 -0.0861 0.0420  -0.0295 118 HIS   A CG  
894  N ND1 . HIS   A 112 ? 0.3672 0.3227 0.2916 -0.0866 0.0267  -0.0255 118 HIS   A ND1 
895  C CD2 . HIS   A 112 ? 0.4021 0.3263 0.3006 -0.0963 0.0502  -0.0354 118 HIS   A CD2 
896  C CE1 . HIS   A 112 ? 0.3980 0.3432 0.3048 -0.0967 0.0246  -0.0282 118 HIS   A CE1 
897  N NE2 . HIS   A 112 ? 0.4211 0.3467 0.3101 -0.1032 0.0383  -0.0347 118 HIS   A NE2 
898  N N   . GLY   A 113 ? 0.3098 0.2877 0.3123 -0.0514 0.0516  -0.0200 119 GLY   A N   
899  C CA  . GLY   A 113 ? 0.2801 0.2648 0.3007 -0.0445 0.0516  -0.0161 119 GLY   A CA  
900  C C   . GLY   A 113 ? 0.2507 0.2491 0.2772 -0.0396 0.0378  -0.0123 119 GLY   A C   
901  O O   . GLY   A 113 ? 0.2470 0.2518 0.2706 -0.0393 0.0299  -0.0119 119 GLY   A O   
902  N N   . VAL   A 114 ? 0.2300 0.2320 0.2659 -0.0358 0.0360  -0.0094 120 VAL   A N   
903  C CA  . VAL   A 114 ? 0.2225 0.2351 0.2635 -0.0315 0.0244  -0.0063 120 VAL   A CA  
904  C C   . VAL   A 114 ? 0.2237 0.2367 0.2508 -0.0350 0.0179  -0.0063 120 VAL   A C   
905  O O   . VAL   A 114 ? 0.2360 0.2418 0.2526 -0.0395 0.0209  -0.0069 120 VAL   A O   
906  C CB  . VAL   A 114 ? 0.2156 0.2304 0.2711 -0.0274 0.0244  -0.0032 120 VAL   A CB  
907  C CG1 . VAL   A 114 ? 0.2220 0.2449 0.2796 -0.0240 0.0133  -0.0010 120 VAL   A CG1 
908  C CG2 . VAL   A 114 ? 0.2329 0.2486 0.3061 -0.0241 0.0288  -0.0011 120 VAL   A CG2 
909  N N   . VAL   A 115 ? 0.1931 0.2136 0.2202 -0.0333 0.0093  -0.0051 121 VAL   A N   
910  C CA  . VAL   A 115 ? 0.1901 0.2132 0.2097 -0.0359 0.0018  -0.0032 121 VAL   A CA  
911  C C   . VAL   A 115 ? 0.1898 0.2184 0.2170 -0.0315 -0.0035 -0.0005 121 VAL   A C   
912  O O   . VAL   A 115 ? 0.2112 0.2396 0.2341 -0.0338 -0.0070 0.0016  121 VAL   A O   
913  C CB  . VAL   A 115 ? 0.1995 0.2271 0.2191 -0.0364 -0.0028 -0.0027 121 VAL   A CB  
914  C CG1 . VAL   A 115 ? 0.2001 0.2320 0.2181 -0.0386 -0.0112 0.0010  121 VAL   A CG1 
915  C CG2 . VAL   A 115 ? 0.2133 0.2346 0.2251 -0.0414 0.0021  -0.0057 121 VAL   A CG2 
916  N N   . GLY   A 116 ? 0.1849 0.2179 0.2226 -0.0257 -0.0047 -0.0002 122 GLY   A N   
917  C CA  . GLY   A 116 ? 0.1828 0.2192 0.2262 -0.0220 -0.0094 0.0015  122 GLY   A CA  
918  C C   . GLY   A 116 ? 0.1740 0.2120 0.2242 -0.0174 -0.0108 0.0012  122 GLY   A C   
919  O O   . GLY   A 116 ? 0.1825 0.2196 0.2348 -0.0168 -0.0082 0.0006  122 GLY   A O   
920  N N   . ILE   A 117 ? 0.1534 0.1923 0.2059 -0.0149 -0.0148 0.0019  123 ILE   A N   
921  C CA  . ILE   A 117 ? 0.1503 0.1880 0.2045 -0.0120 -0.0173 0.0015  123 ILE   A CA  
922  C C   . ILE   A 117 ? 0.1618 0.1989 0.2124 -0.0100 -0.0190 0.0009  123 ILE   A C   
923  O O   . ILE   A 117 ? 0.1590 0.1973 0.2106 -0.0100 -0.0195 0.0016  123 ILE   A O   
924  C CB  . ILE   A 117 ? 0.1701 0.2061 0.2304 -0.0116 -0.0200 0.0025  123 ILE   A CB  
925  C CG1 . ILE   A 117 ? 0.1858 0.2219 0.2474 -0.0120 -0.0213 0.0029  123 ILE   A CG1 
926  C CG2 . ILE   A 117 ? 0.2000 0.2358 0.2684 -0.0127 -0.0168 0.0040  123 ILE   A CG2 
927  C CD1 . ILE   A 117 ? 0.2038 0.2381 0.2733 -0.0118 -0.0245 0.0041  123 ILE   A CD1 
928  N N   . VAL   A 118 ? 0.1700 0.2038 0.2163 -0.0084 -0.0195 0.0001  124 VAL   A N   
929  C CA  . VAL   A 118 ? 0.1672 0.1972 0.2086 -0.0066 -0.0185 -0.0010 124 VAL   A CA  
930  C C   . VAL   A 118 ? 0.1642 0.1909 0.2060 -0.0063 -0.0207 -0.0017 124 VAL   A C   
931  O O   . VAL   A 118 ? 0.1714 0.1962 0.2138 -0.0074 -0.0246 -0.0017 124 VAL   A O   
932  C CB  . VAL   A 118 ? 0.1793 0.2032 0.2119 -0.0059 -0.0185 -0.0020 124 VAL   A CB  
933  C CG1 . VAL   A 118 ? 0.2123 0.2284 0.2370 -0.0045 -0.0154 -0.0039 124 VAL   A CG1 
934  C CG2 . VAL   A 118 ? 0.1819 0.2090 0.2152 -0.0058 -0.0157 -0.0011 124 VAL   A CG2 
935  N N   . SER   A 119 ? 0.1489 0.1752 0.1930 -0.0050 -0.0179 -0.0016 125 SER   A N   
936  C CA  . SER   A 119 ? 0.1545 0.1775 0.2009 -0.0046 -0.0187 -0.0020 125 SER   A CA  
937  C C   . SER   A 119 ? 0.1888 0.2048 0.2331 -0.0026 -0.0134 -0.0035 125 SER   A C   
938  O O   . SER   A 119 ? 0.2114 0.2198 0.2525 -0.0027 -0.0131 -0.0057 125 SER   A O   
939  C CB  . SER   A 119 ? 0.1619 0.1923 0.2182 -0.0055 -0.0200 0.0012  125 SER   A CB  
940  O OG  . SER   A 119 ? 0.1889 0.2168 0.2494 -0.0049 -0.0205 0.0014  125 SER   A OG  
941  N N   . THR   A 120 ? 0.1927 0.2102 0.2399 -0.0010 -0.0083 -0.0023 126 THR   A N   
942  C CA  . THR   A 120 ? 0.2176 0.2277 0.2660 0.0013  -0.0004 -0.0031 126 THR   A CA  
943  C C   . THR   A 120 ? 0.2192 0.2248 0.2613 0.0024  0.0054  -0.0040 126 THR   A C   
944  O O   . THR   A 120 ? 0.2067 0.2171 0.2459 0.0015  0.0026  -0.0034 126 THR   A O   
945  C CB  . THR   A 120 ? 0.2295 0.2467 0.2970 0.0027  0.0016  0.0019  126 THR   A CB  
946  O OG1 . THR   A 120 ? 0.2344 0.2609 0.3109 0.0024  0.0006  0.0061  126 THR   A OG1 
947  C CG2 . THR   A 120 ? 0.2198 0.2416 0.2936 0.0015  -0.0040 0.0039  126 THR   A CG2 
948  N N   . GLY   A 121 ? 0.2475 0.2433 0.2883 0.0044  0.0147  -0.0054 127 GLY   A N   
949  C CA  . GLY   A 121 ? 0.2691 0.2594 0.3050 0.0058  0.0223  -0.0058 127 GLY   A CA  
950  C C   . GLY   A 121 ? 0.2993 0.2776 0.3372 0.0082  0.0352  -0.0070 127 GLY   A C   
951  O O   . GLY   A 121 ? 0.3110 0.2827 0.3507 0.0086  0.0383  -0.0085 127 GLY   A O   
952  N N   . GLY   A 122 ? 0.3321 0.3056 0.3685 0.0098  0.0438  -0.0066 128 GLY   A N   
953  C CA  . GLY   A 122 ? 0.3528 0.3120 0.3899 0.0123  0.0592  -0.0079 128 GLY   A CA  
954  C C   . GLY   A 122 ? 0.3548 0.3217 0.4145 0.0155  0.0665  -0.0022 128 GLY   A C   
955  O O   . GLY   A 122 ? 0.3270 0.3114 0.4069 0.0156  0.0585  0.0036  128 GLY   A O   
956  N N   . ASN   A 123 ? 0.3739 0.3264 0.4302 0.0176  0.0821  -0.0035 129 ASN   A N   
957  C CA  . ASN   A 123 ? 0.3739 0.3324 0.4558 0.0211  0.0912  0.0027  129 ASN   A CA  
958  C C   . ASN   A 123 ? 0.3573 0.3299 0.4443 0.0202  0.0829  0.0062  129 ASN   A C   
959  O O   . ASN   A 123 ? 0.3573 0.3420 0.4717 0.0218  0.0833  0.0132  129 ASN   A O   
960  C CB  . ASN   A 123 ? 0.3872 0.3565 0.5035 0.0233  0.0918  0.0096  129 ASN   A CB  
961  C CG  . ASN   A 123 ? 0.4615 0.4155 0.5784 0.0251  0.1043  0.0069  129 ASN   A CG  
962  O OD1 . ASN   A 123 ? 0.5000 0.4325 0.5972 0.0255  0.1188  0.0008  129 ASN   A OD1 
963  N ND2 . ASN   A 123 ? 0.4590 0.4223 0.5983 0.0258  0.0999  0.0117  129 ASN   A ND2 
964  N N   . GLY   A 124 ? 0.3418 0.3126 0.4041 0.0175  0.0752  0.0021  130 GLY   A N   
965  C CA  . GLY   A 124 ? 0.3053 0.2880 0.3715 0.0165  0.0682  0.0048  130 GLY   A CA  
966  C C   . GLY   A 124 ? 0.2500 0.2514 0.3303 0.0142  0.0534  0.0082  130 GLY   A C   
967  O O   . GLY   A 124 ? 0.2285 0.2401 0.3164 0.0130  0.0485  0.0110  130 GLY   A O   
968  N N   . LEU   A 125 ? 0.2320 0.2361 0.3130 0.0131  0.0469  0.0076  131 LEU   A N   
969  C CA  . LEU   A 125 ? 0.2157 0.2341 0.3053 0.0103  0.0342  0.0104  131 LEU   A CA  
970  C C   . LEU   A 125 ? 0.2371 0.2529 0.3067 0.0080  0.0263  0.0055  131 LEU   A C   
971  O O   . LEU   A 125 ? 0.2760 0.2799 0.3301 0.0084  0.0295  0.0011  131 LEU   A O   
972  C CB  . LEU   A 125 ? 0.2147 0.2390 0.3257 0.0109  0.0332  0.0155  131 LEU   A CB  
973  C CG  . LEU   A 125 ? 0.2226 0.2518 0.3605 0.0128  0.0393  0.0227  131 LEU   A CG  
974  C CD1 . LEU   A 125 ? 0.2612 0.2924 0.4201 0.0143  0.0411  0.0279  131 LEU   A CD1 
975  C CD2 . LEU   A 125 ? 0.2105 0.2528 0.3592 0.0095  0.0303  0.0275  131 LEU   A CD2 
976  N N   . VAL   A 126 ? 0.1813 0.2071 0.2519 0.0051  0.0166  0.0065  132 VAL   A N   
977  C CA  . VAL   A 126 ? 0.1579 0.1831 0.2160 0.0029  0.0095  0.0034  132 VAL   A CA  
978  C C   . VAL   A 126 ? 0.1561 0.1908 0.2243 0.0006  0.0024  0.0064  132 VAL   A C   
979  O O   . VAL   A 126 ? 0.1656 0.2083 0.2439 -0.0013 -0.0001 0.0101  132 VAL   A O   
980  C CB  . VAL   A 126 ? 0.1744 0.1992 0.2212 0.0015  0.0069  0.0014  132 VAL   A CB  
981  C CG1 . VAL   A 126 ? 0.1896 0.2224 0.2445 0.0003  0.0062  0.0038  132 VAL   A CG1 
982  C CG2 . VAL   A 126 ? 0.1743 0.1994 0.2138 -0.0006 -0.0002 -0.0004 132 VAL   A CG2 
983  N N   . GLY   A 127 ? 0.1601 0.1931 0.2246 0.0001  -0.0010 0.0050  133 GLY   A N   
984  C CA  . GLY   A 127 ? 0.1544 0.1947 0.2260 -0.0025 -0.0070 0.0080  133 GLY   A CA  
985  C C   . GLY   A 127 ? 0.1527 0.1932 0.2151 -0.0048 -0.0117 0.0056  133 GLY   A C   
986  O O   . GLY   A 127 ? 0.1898 0.2247 0.2441 -0.0040 -0.0117 0.0024  133 GLY   A O   
987  N N   . PHE   A 128 ? 0.1482 0.1942 0.2124 -0.0083 -0.0157 0.0078  134 PHE   A N   
988  C CA  . PHE   A 128 ? 0.1637 0.2090 0.2212 -0.0106 -0.0178 0.0059  134 PHE   A CA  
989  C C   . PHE   A 128 ? 0.1597 0.2068 0.2193 -0.0131 -0.0209 0.0084  134 PHE   A C   
990  O O   . PHE   A 128 ? 0.1775 0.2282 0.2407 -0.0157 -0.0235 0.0124  134 PHE   A O   
991  C CB  . PHE   A 128 ? 0.1704 0.2171 0.2241 -0.0135 -0.0170 0.0053  134 PHE   A CB  
992  C CG  . PHE   A 128 ? 0.1719 0.2179 0.2251 -0.0115 -0.0139 0.0041  134 PHE   A CG  
993  C CD1 . PHE   A 128 ? 0.1857 0.2281 0.2344 -0.0098 -0.0123 0.0017  134 PHE   A CD1 
994  C CD2 . PHE   A 128 ? 0.1749 0.2238 0.2335 -0.0117 -0.0131 0.0062  134 PHE   A CD2 
995  C CE1 . PHE   A 128 ? 0.1893 0.2303 0.2364 -0.0082 -0.0095 0.0012  134 PHE   A CE1 
996  C CE2 . PHE   A 128 ? 0.1865 0.2341 0.2447 -0.0098 -0.0093 0.0053  134 PHE   A CE2 
997  C CZ  . PHE   A 128 ? 0.1802 0.2236 0.2315 -0.0080 -0.0073 0.0026  134 PHE   A CZ  
998  N N   . ALA   A 129 ? 0.1559 0.2003 0.2134 -0.0128 -0.0213 0.0069  135 ALA   A N   
999  C CA  . ALA   A 129 ? 0.1725 0.2175 0.2306 -0.0153 -0.0231 0.0092  135 ALA   A CA  
1000 C C   . ALA   A 129 ? 0.1778 0.2217 0.2285 -0.0199 -0.0219 0.0089  135 ALA   A C   
1001 O O   . ALA   A 129 ? 0.1745 0.2157 0.2229 -0.0197 -0.0186 0.0062  135 ALA   A O   
1002 C CB  . ALA   A 129 ? 0.1671 0.2092 0.2273 -0.0135 -0.0232 0.0077  135 ALA   A CB  
1003 N N   . ASP   A 130 ? 0.1886 0.2330 0.2350 -0.0245 -0.0243 0.0121  136 ASP   A N   
1004 C CA  . ASP   A 130 ? 0.1978 0.2376 0.2326 -0.0303 -0.0222 0.0112  136 ASP   A CA  
1005 C C   . ASP   A 130 ? 0.1955 0.2299 0.2266 -0.0313 -0.0180 0.0101  136 ASP   A C   
1006 O O   . ASP   A 130 ? 0.1978 0.2331 0.2335 -0.0299 -0.0197 0.0124  136 ASP   A O   
1007 C CB  . ASP   A 130 ? 0.2228 0.2628 0.2513 -0.0366 -0.0279 0.0157  136 ASP   A CB  
1008 C CG  . ASP   A 130 ? 0.2769 0.3089 0.2885 -0.0442 -0.0258 0.0140  136 ASP   A CG  
1009 O OD1 . ASP   A 130 ? 0.2725 0.3023 0.2810 -0.0447 -0.0217 0.0101  136 ASP   A OD1 
1010 O OD2 . ASP   A 130 ? 0.3209 0.3475 0.3210 -0.0503 -0.0278 0.0167  136 ASP   A OD2 
1011 N N   . VAL   A 131 ? 0.2044 0.2325 0.2284 -0.0340 -0.0116 0.0071  137 VAL   A N   
1012 C CA  . VAL   A 131 ? 0.2214 0.2425 0.2423 -0.0357 -0.0049 0.0064  137 VAL   A CA  
1013 C C   . VAL   A 131 ? 0.2467 0.2572 0.2492 -0.0436 0.0002  0.0052  137 VAL   A C   
1014 O O   . VAL   A 131 ? 0.2575 0.2596 0.2549 -0.0457 0.0079  0.0045  137 VAL   A O   
1015 C CB  . VAL   A 131 ? 0.2238 0.2446 0.2569 -0.0311 0.0008  0.0043  137 VAL   A CB  
1016 C CG1 . VAL   A 131 ? 0.2189 0.2471 0.2655 -0.0252 -0.0053 0.0053  137 VAL   A CG1 
1017 C CG2 . VAL   A 131 ? 0.2244 0.2428 0.2562 -0.0318 0.0058  0.0014  137 VAL   A CG2 
1018 N N   . ARG   A 132 ? 0.2418 0.2511 0.2336 -0.0483 -0.0032 0.0047  138 ARG   A N   
1019 C CA  . ARG   A 132 ? 0.2546 0.2515 0.2253 -0.0572 0.0012  0.0028  138 ARG   A CA  
1020 C C   . ARG   A 132 ? 0.2995 0.2882 0.2538 -0.0639 -0.0003 0.0058  138 ARG   A C   
1021 O O   . ARG   A 132 ? 0.3382 0.3124 0.2717 -0.0716 0.0064  0.0032  138 ARG   A O   
1022 C CB  . ARG   A 132 ? 0.2430 0.2411 0.2073 -0.0615 -0.0045 0.0023  138 ARG   A CB  
1023 C CG  . ARG   A 132 ? 0.2229 0.2266 0.2005 -0.0557 -0.0012 -0.0009 138 ARG   A CG  
1024 C CD  . ARG   A 132 ? 0.2335 0.2391 0.2067 -0.0598 -0.0072 -0.0005 138 ARG   A CD  
1025 N NE  . ARG   A 132 ? 0.2328 0.2494 0.2161 -0.0578 -0.0183 0.0051  138 ARG   A NE  
1026 C CZ  . ARG   A 132 ? 0.2411 0.2625 0.2279 -0.0598 -0.0249 0.0074  138 ARG   A CZ  
1027 N NH1 . ARG   A 132 ? 0.2764 0.2919 0.2538 -0.0654 -0.0232 0.0044  138 ARG   A NH1 
1028 N NH2 . ARG   A 132 ? 0.2443 0.2757 0.2451 -0.0567 -0.0328 0.0130  138 ARG   A NH2 
1029 N N   . ASP   A 133 ? 0.2754 0.2717 0.2372 -0.0616 -0.0083 0.0112  139 ASP   A N   
1030 C CA  . ASP   A 133 ? 0.2868 0.2754 0.2332 -0.0681 -0.0103 0.0152  139 ASP   A CA  
1031 C C   . ASP   A 133 ? 0.2976 0.2802 0.2464 -0.0653 -0.0001 0.0142  139 ASP   A C   
1032 O O   . ASP   A 133 ? 0.3242 0.2978 0.2582 -0.0708 0.0010  0.0171  139 ASP   A O   
1033 C CB  . ASP   A 133 ? 0.2965 0.2959 0.2525 -0.0671 -0.0234 0.0227  139 ASP   A CB  
1034 C CG  . ASP   A 133 ? 0.3120 0.3227 0.2921 -0.0572 -0.0239 0.0239  139 ASP   A CG  
1035 O OD1 . ASP   A 133 ? 0.2930 0.3088 0.2864 -0.0504 -0.0201 0.0195  139 ASP   A OD1 
1036 O OD2 . ASP   A 133 ? 0.3260 0.3395 0.3110 -0.0566 -0.0284 0.0293  139 ASP   A OD2 
1037 N N   . LEU   A 134 ? 0.2752 0.2623 0.2427 -0.0575 0.0067  0.0110  140 LEU   A N   
1038 C CA  . LEU   A 134 ? 0.2771 0.2601 0.2525 -0.0544 0.0156  0.0111  140 LEU   A CA  
1039 C C   . LEU   A 134 ? 0.2978 0.2653 0.2606 -0.0589 0.0304  0.0069  140 LEU   A C   
1040 O O   . LEU   A 134 ? 0.3016 0.2685 0.2776 -0.0549 0.0392  0.0038  140 LEU   A O   
1041 C CB  . LEU   A 134 ? 0.2525 0.2473 0.2546 -0.0451 0.0140  0.0106  140 LEU   A CB  
1042 C CG  . LEU   A 134 ? 0.2613 0.2687 0.2743 -0.0408 0.0019  0.0136  140 LEU   A CG  
1043 C CD1 . LEU   A 134 ? 0.2532 0.2686 0.2868 -0.0333 0.0004  0.0122  140 LEU   A CD1 
1044 C CD2 . LEU   A 134 ? 0.2824 0.2899 0.2942 -0.0420 -0.0018 0.0183  140 LEU   A CD2 
1045 N N   . LEU   A 135 ? 0.3141 0.2671 0.2496 -0.0681 0.0333  0.0071  141 LEU   A N   
1046 C CA  . LEU   A 135 ? 0.3487 0.2828 0.2658 -0.0743 0.0487  0.0023  141 LEU   A CA  
1047 C C   . LEU   A 135 ? 0.3678 0.2951 0.2978 -0.0703 0.0646  0.0014  141 LEU   A C   
1048 O O   . LEU   A 135 ? 0.3835 0.2994 0.3126 -0.0714 0.0795  -0.0030 141 LEU   A O   
1049 C CB  . LEU   A 135 ? 0.3642 0.2818 0.2446 -0.0866 0.0472  0.0029  141 LEU   A CB  
1050 C CG  . LEU   A 135 ? 0.3869 0.3109 0.2558 -0.0920 0.0297  0.0058  141 LEU   A CG  
1051 C CD1 . LEU   A 135 ? 0.4313 0.3363 0.2612 -0.1061 0.0273  0.0075  141 LEU   A CD1 
1052 C CD2 . LEU   A 135 ? 0.3939 0.3217 0.2673 -0.0913 0.0288  0.0011  141 LEU   A CD2 
1053 N N   . TRP   A 136 ? 0.3552 0.2892 0.2997 -0.0657 0.0621  0.0058  142 TRP   A N   
1054 C CA  . TRP   A 136 ? 0.3624 0.2916 0.3236 -0.0617 0.0760  0.0064  142 TRP   A CA  
1055 C C   . TRP   A 136 ? 0.3651 0.3033 0.3575 -0.0538 0.0800  0.0052  142 TRP   A C   
1056 O O   . TRP   A 136 ? 0.3779 0.3104 0.3863 -0.0513 0.0936  0.0058  142 TRP   A O   
1057 C CB  . TRP   A 136 ? 0.3556 0.2911 0.3263 -0.0588 0.0704  0.0119  142 TRP   A CB  
1058 C CG  . TRP   A 136 ? 0.3260 0.2813 0.3142 -0.0529 0.0529  0.0148  142 TRP   A CG  
1059 C CD1 . TRP   A 136 ? 0.3320 0.2940 0.3100 -0.0550 0.0388  0.0176  142 TRP   A CD1 
1060 C CD2 . TRP   A 136 ? 0.3043 0.2736 0.3231 -0.0444 0.0485  0.0154  142 TRP   A CD2 
1061 N NE1 . TRP   A 136 ? 0.3238 0.3019 0.3239 -0.0479 0.0280  0.0190  142 TRP   A NE1 
1062 C CE2 . TRP   A 136 ? 0.3080 0.2900 0.3311 -0.0419 0.0332  0.0175  142 TRP   A CE2 
1063 C CE3 . TRP   A 136 ? 0.3045 0.2757 0.3480 -0.0394 0.0557  0.0151  142 TRP   A CE3 
1064 C CZ2 . TRP   A 136 ? 0.2991 0.2935 0.3451 -0.0351 0.0257  0.0179  142 TRP   A CZ2 
1065 C CZ3 . TRP   A 136 ? 0.2948 0.2798 0.3621 -0.0331 0.0458  0.0166  142 TRP   A CZ3 
1066 C CH2 . TRP   A 136 ? 0.2949 0.2902 0.3608 -0.0313 0.0313  0.0173  142 TRP   A CH2 
1067 N N   . LEU   A 137 ? 0.3587 0.3106 0.3607 -0.0502 0.0685  0.0043  143 LEU   A N   
1068 C CA  . LEU   A 137 ? 0.3626 0.3219 0.3913 -0.0439 0.0711  0.0040  143 LEU   A CA  
1069 C C   . LEU   A 137 ? 0.4115 0.3562 0.4368 -0.0469 0.0888  0.0005  143 LEU   A C   
1070 O O   . LEU   A 137 ? 0.4193 0.3665 0.4702 -0.0422 0.0957  0.0019  143 LEU   A O   
1071 C CB  . LEU   A 137 ? 0.3432 0.3165 0.3768 -0.0408 0.0567  0.0034  143 LEU   A CB  
1072 C CG  . LEU   A 137 ? 0.3254 0.3129 0.3687 -0.0363 0.0414  0.0065  143 LEU   A CG  
1073 C CD1 . LEU   A 137 ? 0.3140 0.3107 0.3556 -0.0347 0.0307  0.0051  143 LEU   A CD1 
1074 C CD2 . LEU   A 137 ? 0.3158 0.3099 0.3862 -0.0305 0.0406  0.0096  143 LEU   A CD2 
1075 N N   . ASP   A 138 ? 0.4499 0.3786 0.4441 -0.0552 0.0961  -0.0037 144 ASP   A N   
1076 C CA  . ASP   A 138 ? 0.4835 0.3951 0.4704 -0.0591 0.1145  -0.0083 144 ASP   A CA  
1077 C C   . ASP   A 138 ? 0.5273 0.4219 0.5155 -0.0607 0.1348  -0.0080 144 ASP   A C   
1078 O O   . ASP   A 138 ? 0.5392 0.4173 0.5222 -0.0639 0.1530  -0.0119 144 ASP   A O   
1079 C CB  . ASP   A 138 ? 0.5056 0.4042 0.4551 -0.0689 0.1136  -0.0134 144 ASP   A CB  
1080 C CG  . ASP   A 138 ? 0.5432 0.4550 0.4905 -0.0685 0.0972  -0.0142 144 ASP   A CG  
1081 O OD1 . ASP   A 138 ? 0.5423 0.4716 0.5162 -0.0604 0.0890  -0.0117 144 ASP   A OD1 
1082 O OD2 . ASP   A 138 ? 0.5767 0.4804 0.4951 -0.0769 0.0923  -0.0168 144 ASP   A OD2 
1083 N N   . GLU   A 139 ? 0.5503 0.4471 0.5442 -0.0589 0.1335  -0.0037 145 GLU   A N   
1084 C CA  . GLU   A 139 ? 0.6015 0.4813 0.5968 -0.0604 0.1540  -0.0030 145 GLU   A CA  
1085 C C   . GLU   A 139 ? 0.6294 0.5204 0.6566 -0.0533 0.1522  0.0036  145 GLU   A C   
1086 O O   . GLU   A 139 ? 0.6306 0.5397 0.6683 -0.0492 0.1334  0.0071  145 GLU   A O   
1087 C CB  . GLU   A 139 ? 0.6623 0.5208 0.6129 -0.0710 0.1598  -0.0061 145 GLU   A CB  
1088 C CG  . GLU   A 139 ? 0.7282 0.5964 0.6635 -0.0729 0.1401  -0.0025 145 GLU   A CG  
1089 C CD  . GLU   A 139 ? 0.8522 0.7092 0.7444 -0.0838 0.1327  -0.0055 145 GLU   A CD  
1090 O OE1 . GLU   A 139 ? 0.8671 0.7116 0.7318 -0.0909 0.1328  -0.0037 145 GLU   A OE1 
1091 O OE2 . GLU   A 139 ? 0.9032 0.7634 0.7893 -0.0856 0.1262  -0.0091 145 GLU   A OE2 
1092 N N   . GLU   A 140 ? 0.6522 0.5307 0.6940 -0.0523 0.1726  0.0054  146 GLU   A N   
1093 C CA  . GLU   A 140 ? 0.6676 0.5534 0.7411 -0.0465 0.1743  0.0121  146 GLU   A CA  
1094 C C   . GLU   A 140 ? 0.6697 0.5816 0.7756 -0.0389 0.1528  0.0171  146 GLU   A C   
1095 O O   . GLU   A 140 ? 0.6671 0.5867 0.8039 -0.0341 0.1521  0.0229  146 GLU   A O   
1096 C CB  . GLU   A 140 ? 0.7109 0.5856 0.7604 -0.0511 0.1778  0.0131  146 GLU   A CB  
1097 C CG  . GLU   A 140 ? 0.7794 0.6702 0.8265 -0.0495 0.1558  0.0166  146 GLU   A CG  
1098 C CD  . GLU   A 140 ? 0.8737 0.7696 0.9465 -0.0450 0.1573  0.0228  146 GLU   A CD  
1099 O OE1 . GLU   A 140 ? 0.8916 0.8014 0.9678 -0.0428 0.1399  0.0257  146 GLU   A OE1 
1100 O OE2 . GLU   A 140 ? 0.9035 0.7890 0.9947 -0.0436 0.1766  0.0250  146 GLU   A OE2 
1101 N N1  . A1BSG B .   ? 0.2753 0.2382 0.2839 -0.0041 0.0014  -0.0186 201 A1BSG A N1  
1102 C C4  . A1BSG B .   ? 0.2917 0.2476 0.2871 -0.0083 -0.0068 -0.0212 201 A1BSG A C4  
1103 C C5  . A1BSG B .   ? 0.2976 0.2506 0.2978 -0.0026 0.0119  -0.0205 201 A1BSG A C5  
1104 C C6  . A1BSG B .   ? 0.2970 0.2551 0.2924 -0.0024 0.0106  -0.0187 201 A1BSG A C6  
1105 C C7  . A1BSG B .   ? 0.2820 0.2536 0.2826 -0.0032 0.0009  -0.0156 201 A1BSG A C7  
1106 C C8  . A1BSG B .   ? 0.2829 0.2579 0.2795 -0.0030 0.0005  -0.0142 201 A1BSG A C8  
1107 C C10 . A1BSG B .   ? 0.3217 0.2732 0.3027 -0.0012 0.0197  -0.0188 201 A1BSG A C10 
1108 C C13 . A1BSG B .   ? 0.3441 0.2808 0.3138 -0.0001 0.0328  -0.0210 201 A1BSG A C13 
1109 O O1  . A1BSG B .   ? 0.3216 0.2622 0.2958 -0.0117 -0.0069 -0.0251 201 A1BSG A O1  
1110 C C3  . A1BSG B .   ? 0.2925 0.2583 0.3001 -0.0093 -0.0158 -0.0187 201 A1BSG A C3  
1111 C C2  . A1BSG B .   ? 0.2831 0.2619 0.3123 -0.0059 -0.0134 -0.0145 201 A1BSG A C2  
1112 C C14 . A1BSG B .   ? 0.2572 0.2355 0.2887 -0.0012 0.0012  -0.0133 201 A1BSG A C14 
1113 C C1  . A1BSG B .   ? 0.2624 0.2509 0.3002 -0.0029 -0.0088 -0.0110 201 A1BSG A C1  
1114 C C   . A1BSG B .   ? 0.2490 0.2496 0.3058 -0.0011 -0.0089 -0.0057 201 A1BSG A C   
1115 O O   . A1BSG B .   ? 0.2469 0.2457 0.3134 0.0006  -0.0042 -0.0044 201 A1BSG A O   
1116 N N   . A1BSG B .   ? 0.2320 0.2440 0.2936 -0.0018 -0.0136 -0.0022 201 A1BSG A N   
1117 C C11 . A1BSG B .   ? 0.3153 0.2632 0.3012 -0.0013 0.0206  -0.0204 201 A1BSG A C11 
1118 O O2  . A1BSG B .   ? 0.3398 0.2722 0.3206 -0.0003 0.0334  -0.0236 201 A1BSG A O2  
1119 C C12 . A1BSG B .   ? 0.3513 0.2763 0.3233 0.0008  0.0426  -0.0239 201 A1BSG A C12 
1120 C C9  . A1BSG B .   ? 0.2949 0.2602 0.2814 -0.0021 0.0092  -0.0157 201 A1BSG A C9  
# 
