data_7I5P
# 
_entry.id   7I5P 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_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   7I5P         pdb_00007i5p 10.2210/pdb7i5p/pdb 
WWPDB D_1001408348 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_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_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I5P 
_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   2025-03-12 
_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-{[5-bromo-2-(methylsulfanyl)phenyl]acetyl}pyrrolidine-3-carboxamide' 357.266   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                   65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    1   ?         ? ? ? 
5 water       nat water                                                                        18.015    174 ?         ? ? ? 
# 
_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-{[5-bromo-2-(methylsulfanyl)phenyl]acetyl}pyrrolidine-3-carboxamide' A1B36 
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 
A1B36 non-polymer         . '(3S)-1-{[5-bromo-2-(methylsulfanyl)phenyl]acetyl}pyrrolidine-3-carboxamide' ? 'C14 H17 Br N2 O2 S' 
357.266 
ALA   'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'         
89.093  
ARG   'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1'     
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'        
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'         
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'       
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                         ? 'C2 H6 O S'          
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'       
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'         
147.129 
GLY   'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'         
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1'     
156.162 
HOH   non-polymer         . WATER                                                                        ? 'H2 O'               
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                   ? 'C6 H13 N O2'        
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                      ? 'C6 H13 N O2'        
131.173 
LYS   'L-peptide linking' y LYSINE                                                                       ? 'C6 H15 N2 O2 1'     
147.195 
MET   'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'      
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                ? 'C9 H11 N O2'        
165.189 
PRO   'L-peptide linking' y PROLINE                                                                      ? 'C5 H9 N O2'         
115.130 
SER   'L-peptide linking' y SERINE                                                                       ? 'C3 H7 N O3'         
105.093 
THR   'L-peptide linking' y THREONINE                                                                    ? 'C4 H9 N O3'         
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                   ? 'C11 H12 N2 O2'      
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                     ? 'C9 H11 N O3'        
181.189 
VAL   'L-peptide linking' y VALINE                                                                       ? 'C5 H11 N O2'        
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                   ? 'Zn 2'               
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B36 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B36 
_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 A1B36 1   201 201 A1B36 LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 1   DMS   DMS A . 
E 5 HOH   1   301 262 HOH   HOH A . 
E 5 HOH   2   302 49  HOH   HOH A . 
E 5 HOH   3   303 30  HOH   HOH A . 
E 5 HOH   4   304 36  HOH   HOH A . 
E 5 HOH   5   305 121 HOH   HOH A . 
E 5 HOH   6   306 42  HOH   HOH A . 
E 5 HOH   7   307 75  HOH   HOH A . 
E 5 HOH   8   308 59  HOH   HOH A . 
E 5 HOH   9   309 150 HOH   HOH A . 
E 5 HOH   10  310 154 HOH   HOH A . 
E 5 HOH   11  311 26  HOH   HOH A . 
E 5 HOH   12  312 104 HOH   HOH A . 
E 5 HOH   13  313 137 HOH   HOH A . 
E 5 HOH   14  314 181 HOH   HOH A . 
E 5 HOH   15  315 119 HOH   HOH A . 
E 5 HOH   16  316 68  HOH   HOH A . 
E 5 HOH   17  317 169 HOH   HOH A . 
E 5 HOH   18  318 61  HOH   HOH A . 
E 5 HOH   19  319 227 HOH   HOH A . 
E 5 HOH   20  320 85  HOH   HOH A . 
E 5 HOH   21  321 4   HOH   HOH A . 
E 5 HOH   22  322 55  HOH   HOH A . 
E 5 HOH   23  323 261 HOH   HOH A . 
E 5 HOH   24  324 7   HOH   HOH A . 
E 5 HOH   25  325 2   HOH   HOH A . 
E 5 HOH   26  326 216 HOH   HOH A . 
E 5 HOH   27  327 263 HOH   HOH A . 
E 5 HOH   28  328 260 HOH   HOH A . 
E 5 HOH   29  329 25  HOH   HOH A . 
E 5 HOH   30  330 34  HOH   HOH A . 
E 5 HOH   31  331 33  HOH   HOH A . 
E 5 HOH   32  332 255 HOH   HOH A . 
E 5 HOH   33  333 251 HOH   HOH A . 
E 5 HOH   34  334 214 HOH   HOH A . 
E 5 HOH   35  335 41  HOH   HOH A . 
E 5 HOH   36  336 24  HOH   HOH A . 
E 5 HOH   37  337 77  HOH   HOH A . 
E 5 HOH   38  338 254 HOH   HOH A . 
E 5 HOH   39  339 266 HOH   HOH A . 
E 5 HOH   40  340 111 HOH   HOH A . 
E 5 HOH   41  341 29  HOH   HOH A . 
E 5 HOH   42  342 249 HOH   HOH A . 
E 5 HOH   43  343 21  HOH   HOH A . 
E 5 HOH   44  344 211 HOH   HOH A . 
E 5 HOH   45  345 147 HOH   HOH A . 
E 5 HOH   46  346 268 HOH   HOH A . 
E 5 HOH   47  347 35  HOH   HOH A . 
E 5 HOH   48  348 124 HOH   HOH A . 
E 5 HOH   49  349 28  HOH   HOH A . 
E 5 HOH   50  350 218 HOH   HOH A . 
E 5 HOH   51  351 135 HOH   HOH A . 
E 5 HOH   52  352 179 HOH   HOH A . 
E 5 HOH   53  353 9   HOH   HOH A . 
E 5 HOH   54  354 253 HOH   HOH A . 
E 5 HOH   55  355 144 HOH   HOH A . 
E 5 HOH   56  356 19  HOH   HOH A . 
E 5 HOH   57  357 265 HOH   HOH A . 
E 5 HOH   58  358 174 HOH   HOH A . 
E 5 HOH   59  359 258 HOH   HOH A . 
E 5 HOH   60  360 82  HOH   HOH A . 
E 5 HOH   61  361 62  HOH   HOH A . 
E 5 HOH   62  362 37  HOH   HOH A . 
E 5 HOH   63  363 157 HOH   HOH A . 
E 5 HOH   64  364 270 HOH   HOH A . 
E 5 HOH   65  365 252 HOH   HOH A . 
E 5 HOH   66  366 197 HOH   HOH A . 
E 5 HOH   67  367 103 HOH   HOH A . 
E 5 HOH   68  368 281 HOH   HOH A . 
E 5 HOH   69  369 108 HOH   HOH A . 
E 5 HOH   70  370 60  HOH   HOH A . 
E 5 HOH   71  371 105 HOH   HOH A . 
E 5 HOH   72  372 177 HOH   HOH A . 
E 5 HOH   73  373 50  HOH   HOH A . 
E 5 HOH   74  374 84  HOH   HOH A . 
E 5 HOH   75  375 12  HOH   HOH A . 
E 5 HOH   76  376 11  HOH   HOH A . 
E 5 HOH   77  377 161 HOH   HOH A . 
E 5 HOH   78  378 79  HOH   HOH A . 
E 5 HOH   79  379 170 HOH   HOH A . 
E 5 HOH   80  380 156 HOH   HOH A . 
E 5 HOH   81  381 273 HOH   HOH A . 
E 5 HOH   82  382 167 HOH   HOH A . 
E 5 HOH   83  383 257 HOH   HOH A . 
E 5 HOH   84  384 20  HOH   HOH A . 
E 5 HOH   85  385 16  HOH   HOH A . 
E 5 HOH   86  386 131 HOH   HOH A . 
E 5 HOH   87  387 259 HOH   HOH A . 
E 5 HOH   88  388 100 HOH   HOH A . 
E 5 HOH   89  389 47  HOH   HOH A . 
E 5 HOH   90  390 14  HOH   HOH A . 
E 5 HOH   91  391 90  HOH   HOH A . 
E 5 HOH   92  392 168 HOH   HOH A . 
E 5 HOH   93  393 40  HOH   HOH A . 
E 5 HOH   94  394 186 HOH   HOH A . 
E 5 HOH   95  395 51  HOH   HOH A . 
E 5 HOH   96  396 217 HOH   HOH A . 
E 5 HOH   97  397 95  HOH   HOH A . 
E 5 HOH   98  398 106 HOH   HOH A . 
E 5 HOH   99  399 203 HOH   HOH A . 
E 5 HOH   100 400 15  HOH   HOH A . 
E 5 HOH   101 401 8   HOH   HOH A . 
E 5 HOH   102 402 18  HOH   HOH A . 
E 5 HOH   103 403 89  HOH   HOH A . 
E 5 HOH   104 404 219 HOH   HOH A . 
E 5 HOH   105 405 192 HOH   HOH A . 
E 5 HOH   106 406 5   HOH   HOH A . 
E 5 HOH   107 407 96  HOH   HOH A . 
E 5 HOH   108 408 10  HOH   HOH A . 
E 5 HOH   109 409 80  HOH   HOH A . 
E 5 HOH   110 410 38  HOH   HOH A . 
E 5 HOH   111 411 248 HOH   HOH A . 
E 5 HOH   112 412 43  HOH   HOH A . 
E 5 HOH   113 413 220 HOH   HOH A . 
E 5 HOH   114 414 91  HOH   HOH A . 
E 5 HOH   115 415 76  HOH   HOH A . 
E 5 HOH   116 416 250 HOH   HOH A . 
E 5 HOH   117 417 48  HOH   HOH A . 
E 5 HOH   118 418 126 HOH   HOH A . 
E 5 HOH   119 419 23  HOH   HOH A . 
E 5 HOH   120 420 27  HOH   HOH A . 
E 5 HOH   121 421 276 HOH   HOH A . 
E 5 HOH   122 422 175 HOH   HOH A . 
E 5 HOH   123 423 128 HOH   HOH A . 
E 5 HOH   124 424 236 HOH   HOH A . 
E 5 HOH   125 425 123 HOH   HOH A . 
E 5 HOH   126 426 159 HOH   HOH A . 
E 5 HOH   127 427 264 HOH   HOH A . 
E 5 HOH   128 428 201 HOH   HOH A . 
E 5 HOH   129 429 155 HOH   HOH A . 
E 5 HOH   130 430 138 HOH   HOH A . 
E 5 HOH   131 431 101 HOH   HOH A . 
E 5 HOH   132 432 83  HOH   HOH A . 
E 5 HOH   133 433 256 HOH   HOH A . 
E 5 HOH   134 434 69  HOH   HOH A . 
E 5 HOH   135 435 233 HOH   HOH A . 
E 5 HOH   136 436 275 HOH   HOH A . 
E 5 HOH   137 437 158 HOH   HOH A . 
E 5 HOH   138 438 278 HOH   HOH A . 
E 5 HOH   139 439 213 HOH   HOH A . 
E 5 HOH   140 440 134 HOH   HOH A . 
E 5 HOH   141 441 215 HOH   HOH A . 
E 5 HOH   142 442 224 HOH   HOH A . 
E 5 HOH   143 443 269 HOH   HOH A . 
E 5 HOH   144 444 152 HOH   HOH A . 
E 5 HOH   145 445 189 HOH   HOH A . 
E 5 HOH   146 446 246 HOH   HOH A . 
E 5 HOH   147 447 112 HOH   HOH A . 
E 5 HOH   148 448 162 HOH   HOH A . 
E 5 HOH   149 449 102 HOH   HOH A . 
E 5 HOH   150 450 65  HOH   HOH A . 
E 5 HOH   151 451 117 HOH   HOH A . 
E 5 HOH   152 452 99  HOH   HOH A . 
E 5 HOH   153 453 271 HOH   HOH A . 
E 5 HOH   154 454 274 HOH   HOH A . 
E 5 HOH   155 455 243 HOH   HOH A . 
E 5 HOH   156 456 171 HOH   HOH A . 
E 5 HOH   157 457 86  HOH   HOH A . 
E 5 HOH   158 458 127 HOH   HOH A . 
E 5 HOH   159 459 240 HOH   HOH A . 
E 5 HOH   160 460 56  HOH   HOH A . 
E 5 HOH   161 461 204 HOH   HOH A . 
E 5 HOH   162 462 280 HOH   HOH A . 
E 5 HOH   163 463 46  HOH   HOH A . 
E 5 HOH   164 464 187 HOH   HOH A . 
E 5 HOH   165 465 267 HOH   HOH A . 
E 5 HOH   166 466 277 HOH   HOH A . 
E 5 HOH   167 467 118 HOH   HOH A . 
E 5 HOH   168 468 153 HOH   HOH A . 
E 5 HOH   169 469 279 HOH   HOH A . 
E 5 HOH   170 470 221 HOH   HOH A . 
E 5 HOH   171 471 184 HOH   HOH A . 
E 5 HOH   172 472 98  HOH   HOH A . 
E 5 HOH   173 473 206 HOH   HOH A . 
E 5 HOH   174 474 244 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           7I5P 
_cell.length_a           88.481 
_cell.length_b           57.614 
_cell.length_c           32.709 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.42 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I5P 
_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          7I5P 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.62 
_exptl_crystal.density_percent_sol   53.06 
_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   2025-01-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I5P 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.27 
_reflns.d_resolution_high            1.51 
_reflns.number_obs                   25703 
_reflns.percent_possible_obs         99.6 
_reflns.pdbx_Rmerge_I_obs            0.072 
_reflns.pdbx_netI_over_sigmaI        9.7 
_reflns.pdbx_redundancy              6.7 
_reflns.pdbx_Rrim_I_all              0.078 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     171245 
_reflns.pdbx_chi_squared             0.43 
_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                  1.51 
_reflns_shell.d_res_low                   1.54 
_reflns_shell.number_measured_all         6711 
_reflns_shell.number_unique_obs           1257 
_reflns_shell.Rmerge_I_obs                2.352 
_reflns_shell.pdbx_chi_squared            0.05 
_reflns_shell.pdbx_redundancy             5.3 
_reflns_shell.percent_possible_obs        95.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.2 
_reflns_shell.pdbx_Rrim_I_all             2.613 
_reflns_shell.pdbx_Rpim_I_all             1.118 
_reflns_shell.pdbx_CC_half                0.307 
_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                                 7I5P 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     23914 
_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                             22.10 
_refine.ls_d_res_high                            1.512 
_refine.ls_percent_reflns_obs                    92.9 
_refine.ls_R_factor_obs                          0.1954 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1933 
_refine.ls_R_factor_R_free                       0.2343 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.090 
_refine.ls_number_reflns_R_free                  1218 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.B_iso_mean                               34.81 
_refine.aniso_B[1][1]                            -6.84910 
_refine.aniso_B[2][2]                            -2.88070 
_refine.aniso_B[3][3]                            9.72980 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.05430 
_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             0.078 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.084 
_refine.pdbx_overall_SU_R_Blow_DPI               0.084 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.088 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I5P 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         25 
_refine_hist.number_atoms_solvent             174 
_refine_hist.number_atoms_total               1273 
_refine_hist.d_res_high                       1.512 
_refine_hist.d_res_low                        22.10 
# 
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  1141 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.94  ? 2.00  1556 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  383  '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  208  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1141 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.94  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.55 ? ?     ?    '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  1058 '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                       1.51 
_refine_ls_shell.d_res_low                        1.55 
_refine_ls_shell.number_reflns_R_work             457 
_refine_ls_shell.R_factor_R_work                  0.4250 
_refine_ls_shell.percent_reflns_obs               24.99 
_refine_ls_shell.R_factor_R_free                  0.5265 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.59 
_refine_ls_shell.number_reflns_R_free             22 
_refine_ls_shell.number_reflns_all                479 
_refine_ls_shell.R_factor_all                     0.4310 
# 
_struct.entry_id                  7I5P 
_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-0036545-001 (A71EV2A-x4856)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I5P 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I5P 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 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 ? ? ? ? ? ? ? 2.338 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.419 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.134 ? ? 
# 
_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_555 110.6 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 108.0 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.9 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 109.0 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 98.5  ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 114.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I5P 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -103.69 41.31  
2 1 SER A 125 ? ? -134.32 -35.65 
# 
_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         15.1304 
_pdbx_refine_tls.origin_y         7.6768 
_pdbx_refine_tls.origin_z         13.9796 
_pdbx_refine_tls.T[1][1]          -0.1142 
_pdbx_refine_tls.T[2][2]          -0.0694 
_pdbx_refine_tls.T[3][3]          0.1621 
_pdbx_refine_tls.T[1][2]          -0.0101 
_pdbx_refine_tls.T[1][3]          -0.0052 
_pdbx_refine_tls.T[2][3]          0.0108 
_pdbx_refine_tls.L[1][1]          1.0841 
_pdbx_refine_tls.L[2][2]          2.5043 
_pdbx_refine_tls.L[3][3]          0.4824 
_pdbx_refine_tls.L[1][2]          -0.2851 
_pdbx_refine_tls.L[1][3]          -0.2637 
_pdbx_refine_tls.L[2][3]          -0.1628 
_pdbx_refine_tls.S[1][1]          -0.0326 
_pdbx_refine_tls.S[1][2]          0.0375 
_pdbx_refine_tls.S[1][3]          0.1266 
_pdbx_refine_tls.S[2][1]          0.0319 
_pdbx_refine_tls.S[2][2]          0.0107 
_pdbx_refine_tls.S[2][3]          -0.2285 
_pdbx_refine_tls.S[3][1]          -0.0242 
_pdbx_refine_tls.S[3][2]          -0.0193 
_pdbx_refine_tls.S[3][3]          0.0218 
# 
_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 473 ? 5.99 . 
2 1 O ? A HOH 474 ? 7.52 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B36 N1   N  N N 1   
A1B36 C4   C  Y N 2   
A1B36 C5   C  Y N 3   
A1B36 C6   C  Y N 4   
A1B36 C7   C  N N 5   
A1B36 C8   C  N N 6   
A1B36 C10  C  N N 7   
A1B36 C13  C  N N 8   
A1B36 O1   O  N N 9   
A1B36 C12  C  N N 10  
A1B36 C11  C  N S 11  
A1B36 C9   C  N N 12  
A1B36 N    N  N N 13  
A1B36 O    O  N N 14  
A1B36 C1   C  Y N 15  
A1B36 S    S  N N 16  
A1B36 C    C  N N 17  
A1B36 BR   BR N N 18  
A1B36 C3   C  Y N 19  
A1B36 C2   C  Y N 20  
A1B36 H14  H  N N 21  
A1B36 H13  H  N N 22  
A1B36 H6   H  N N 23  
A1B36 H8   H  N N 24  
A1B36 H7   H  N N 25  
A1B36 H11  H  N N 26  
A1B36 H12  H  N N 27  
A1B36 H15  H  N N 28  
A1B36 H16  H  N N 29  
A1B36 H    H  N N 30  
A1B36 H9   H  N N 31  
A1B36 H10  H  N N 32  
A1B36 H2   H  N N 33  
A1B36 H1   H  N N 34  
A1B36 H3   H  N N 35  
A1B36 H5   H  N N 36  
A1B36 H4   H  N N 37  
ALA   N    N  N N 38  
ALA   CA   C  N S 39  
ALA   C    C  N N 40  
ALA   O    O  N N 41  
ALA   CB   C  N N 42  
ALA   OXT  O  N N 43  
ALA   H    H  N N 44  
ALA   H2   H  N N 45  
ALA   HA   H  N N 46  
ALA   HB1  H  N N 47  
ALA   HB2  H  N N 48  
ALA   HB3  H  N N 49  
ALA   HXT  H  N N 50  
ARG   N    N  N N 51  
ARG   CA   C  N S 52  
ARG   C    C  N N 53  
ARG   O    O  N N 54  
ARG   CB   C  N N 55  
ARG   CG   C  N N 56  
ARG   CD   C  N N 57  
ARG   NE   N  N N 58  
ARG   CZ   C  N N 59  
ARG   NH1  N  N N 60  
ARG   NH2  N  N N 61  
ARG   OXT  O  N N 62  
ARG   H    H  N N 63  
ARG   H2   H  N N 64  
ARG   HA   H  N N 65  
ARG   HB2  H  N N 66  
ARG   HB3  H  N N 67  
ARG   HG2  H  N N 68  
ARG   HG3  H  N N 69  
ARG   HD2  H  N N 70  
ARG   HD3  H  N N 71  
ARG   HE   H  N N 72  
ARG   HH11 H  N N 73  
ARG   HH12 H  N N 74  
ARG   HH21 H  N N 75  
ARG   HH22 H  N N 76  
ARG   HXT  H  N N 77  
ASN   N    N  N N 78  
ASN   CA   C  N S 79  
ASN   C    C  N N 80  
ASN   O    O  N N 81  
ASN   CB   C  N N 82  
ASN   CG   C  N N 83  
ASN   OD1  O  N N 84  
ASN   ND2  N  N N 85  
ASN   OXT  O  N N 86  
ASN   H    H  N N 87  
ASN   H2   H  N N 88  
ASN   HA   H  N N 89  
ASN   HB2  H  N N 90  
ASN   HB3  H  N N 91  
ASN   HD21 H  N N 92  
ASN   HD22 H  N N 93  
ASN   HXT  H  N N 94  
ASP   N    N  N N 95  
ASP   CA   C  N S 96  
ASP   C    C  N N 97  
ASP   O    O  N N 98  
ASP   CB   C  N N 99  
ASP   CG   C  N N 100 
ASP   OD1  O  N N 101 
ASP   OD2  O  N N 102 
ASP   OXT  O  N N 103 
ASP   H    H  N N 104 
ASP   H2   H  N N 105 
ASP   HA   H  N N 106 
ASP   HB2  H  N N 107 
ASP   HB3  H  N N 108 
ASP   HD2  H  N N 109 
ASP   HXT  H  N N 110 
CYS   N    N  N N 111 
CYS   CA   C  N R 112 
CYS   C    C  N N 113 
CYS   O    O  N N 114 
CYS   CB   C  N N 115 
CYS   SG   S  N N 116 
CYS   OXT  O  N N 117 
CYS   H    H  N N 118 
CYS   H2   H  N N 119 
CYS   HA   H  N N 120 
CYS   HB2  H  N N 121 
CYS   HB3  H  N N 122 
CYS   HG   H  N N 123 
CYS   HXT  H  N N 124 
DMS   S    S  N N 125 
DMS   O    O  N N 126 
DMS   C1   C  N N 127 
DMS   C2   C  N N 128 
DMS   H11  H  N N 129 
DMS   H12  H  N N 130 
DMS   H13  H  N N 131 
DMS   H21  H  N N 132 
DMS   H22  H  N N 133 
DMS   H23  H  N N 134 
GLN   N    N  N N 135 
GLN   CA   C  N S 136 
GLN   C    C  N N 137 
GLN   O    O  N N 138 
GLN   CB   C  N N 139 
GLN   CG   C  N N 140 
GLN   CD   C  N N 141 
GLN   OE1  O  N N 142 
GLN   NE2  N  N N 143 
GLN   OXT  O  N N 144 
GLN   H    H  N N 145 
GLN   H2   H  N N 146 
GLN   HA   H  N N 147 
GLN   HB2  H  N N 148 
GLN   HB3  H  N N 149 
GLN   HG2  H  N N 150 
GLN   HG3  H  N N 151 
GLN   HE21 H  N N 152 
GLN   HE22 H  N N 153 
GLN   HXT  H  N N 154 
GLU   N    N  N N 155 
GLU   CA   C  N S 156 
GLU   C    C  N N 157 
GLU   O    O  N N 158 
GLU   CB   C  N N 159 
GLU   CG   C  N N 160 
GLU   CD   C  N N 161 
GLU   OE1  O  N N 162 
GLU   OE2  O  N N 163 
GLU   OXT  O  N N 164 
GLU   H    H  N N 165 
GLU   H2   H  N N 166 
GLU   HA   H  N N 167 
GLU   HB2  H  N N 168 
GLU   HB3  H  N N 169 
GLU   HG2  H  N N 170 
GLU   HG3  H  N N 171 
GLU   HE2  H  N N 172 
GLU   HXT  H  N N 173 
GLY   N    N  N N 174 
GLY   CA   C  N N 175 
GLY   C    C  N N 176 
GLY   O    O  N N 177 
GLY   OXT  O  N N 178 
GLY   H    H  N N 179 
GLY   H2   H  N N 180 
GLY   HA2  H  N N 181 
GLY   HA3  H  N N 182 
GLY   HXT  H  N N 183 
HIS   N    N  N N 184 
HIS   CA   C  N S 185 
HIS   C    C  N N 186 
HIS   O    O  N N 187 
HIS   CB   C  N N 188 
HIS   CG   C  Y N 189 
HIS   ND1  N  Y N 190 
HIS   CD2  C  Y N 191 
HIS   CE1  C  Y N 192 
HIS   NE2  N  Y N 193 
HIS   OXT  O  N N 194 
HIS   H    H  N N 195 
HIS   H2   H  N N 196 
HIS   HA   H  N N 197 
HIS   HB2  H  N N 198 
HIS   HB3  H  N N 199 
HIS   HD1  H  N N 200 
HIS   HD2  H  N N 201 
HIS   HE1  H  N N 202 
HIS   HE2  H  N N 203 
HIS   HXT  H  N N 204 
HOH   O    O  N N 205 
HOH   H1   H  N N 206 
HOH   H2   H  N N 207 
ILE   N    N  N N 208 
ILE   CA   C  N S 209 
ILE   C    C  N N 210 
ILE   O    O  N N 211 
ILE   CB   C  N S 212 
ILE   CG1  C  N N 213 
ILE   CG2  C  N N 214 
ILE   CD1  C  N N 215 
ILE   OXT  O  N N 216 
ILE   H    H  N N 217 
ILE   H2   H  N N 218 
ILE   HA   H  N N 219 
ILE   HB   H  N N 220 
ILE   HG12 H  N N 221 
ILE   HG13 H  N N 222 
ILE   HG21 H  N N 223 
ILE   HG22 H  N N 224 
ILE   HG23 H  N N 225 
ILE   HD11 H  N N 226 
ILE   HD12 H  N N 227 
ILE   HD13 H  N N 228 
ILE   HXT  H  N N 229 
LEU   N    N  N N 230 
LEU   CA   C  N S 231 
LEU   C    C  N N 232 
LEU   O    O  N N 233 
LEU   CB   C  N N 234 
LEU   CG   C  N N 235 
LEU   CD1  C  N N 236 
LEU   CD2  C  N N 237 
LEU   OXT  O  N N 238 
LEU   H    H  N N 239 
LEU   H2   H  N N 240 
LEU   HA   H  N N 241 
LEU   HB2  H  N N 242 
LEU   HB3  H  N N 243 
LEU   HG   H  N N 244 
LEU   HD11 H  N N 245 
LEU   HD12 H  N N 246 
LEU   HD13 H  N N 247 
LEU   HD21 H  N N 248 
LEU   HD22 H  N N 249 
LEU   HD23 H  N N 250 
LEU   HXT  H  N N 251 
LYS   N    N  N N 252 
LYS   CA   C  N S 253 
LYS   C    C  N N 254 
LYS   O    O  N N 255 
LYS   CB   C  N N 256 
LYS   CG   C  N N 257 
LYS   CD   C  N N 258 
LYS   CE   C  N N 259 
LYS   NZ   N  N N 260 
LYS   OXT  O  N N 261 
LYS   H    H  N N 262 
LYS   H2   H  N N 263 
LYS   HA   H  N N 264 
LYS   HB2  H  N N 265 
LYS   HB3  H  N N 266 
LYS   HG2  H  N N 267 
LYS   HG3  H  N N 268 
LYS   HD2  H  N N 269 
LYS   HD3  H  N N 270 
LYS   HE2  H  N N 271 
LYS   HE3  H  N N 272 
LYS   HZ1  H  N N 273 
LYS   HZ2  H  N N 274 
LYS   HZ3  H  N N 275 
LYS   HXT  H  N N 276 
MET   N    N  N N 277 
MET   CA   C  N S 278 
MET   C    C  N N 279 
MET   O    O  N N 280 
MET   CB   C  N N 281 
MET   CG   C  N N 282 
MET   SD   S  N N 283 
MET   CE   C  N N 284 
MET   OXT  O  N N 285 
MET   H    H  N N 286 
MET   H2   H  N N 287 
MET   HA   H  N N 288 
MET   HB2  H  N N 289 
MET   HB3  H  N N 290 
MET   HG2  H  N N 291 
MET   HG3  H  N N 292 
MET   HE1  H  N N 293 
MET   HE2  H  N N 294 
MET   HE3  H  N N 295 
MET   HXT  H  N N 296 
PHE   N    N  N N 297 
PHE   CA   C  N S 298 
PHE   C    C  N N 299 
PHE   O    O  N N 300 
PHE   CB   C  N N 301 
PHE   CG   C  Y N 302 
PHE   CD1  C  Y N 303 
PHE   CD2  C  Y N 304 
PHE   CE1  C  Y N 305 
PHE   CE2  C  Y N 306 
PHE   CZ   C  Y N 307 
PHE   OXT  O  N N 308 
PHE   H    H  N N 309 
PHE   H2   H  N N 310 
PHE   HA   H  N N 311 
PHE   HB2  H  N N 312 
PHE   HB3  H  N N 313 
PHE   HD1  H  N N 314 
PHE   HD2  H  N N 315 
PHE   HE1  H  N N 316 
PHE   HE2  H  N N 317 
PHE   HZ   H  N N 318 
PHE   HXT  H  N N 319 
PRO   N    N  N N 320 
PRO   CA   C  N S 321 
PRO   C    C  N N 322 
PRO   O    O  N N 323 
PRO   CB   C  N N 324 
PRO   CG   C  N N 325 
PRO   CD   C  N N 326 
PRO   OXT  O  N N 327 
PRO   H    H  N N 328 
PRO   HA   H  N N 329 
PRO   HB2  H  N N 330 
PRO   HB3  H  N N 331 
PRO   HG2  H  N N 332 
PRO   HG3  H  N N 333 
PRO   HD2  H  N N 334 
PRO   HD3  H  N N 335 
PRO   HXT  H  N N 336 
SER   N    N  N N 337 
SER   CA   C  N S 338 
SER   C    C  N N 339 
SER   O    O  N N 340 
SER   CB   C  N N 341 
SER   OG   O  N N 342 
SER   OXT  O  N N 343 
SER   H    H  N N 344 
SER   H2   H  N N 345 
SER   HA   H  N N 346 
SER   HB2  H  N N 347 
SER   HB3  H  N N 348 
SER   HG   H  N N 349 
SER   HXT  H  N N 350 
THR   N    N  N N 351 
THR   CA   C  N S 352 
THR   C    C  N N 353 
THR   O    O  N N 354 
THR   CB   C  N R 355 
THR   OG1  O  N N 356 
THR   CG2  C  N N 357 
THR   OXT  O  N N 358 
THR   H    H  N N 359 
THR   H2   H  N N 360 
THR   HA   H  N N 361 
THR   HB   H  N N 362 
THR   HG1  H  N N 363 
THR   HG21 H  N N 364 
THR   HG22 H  N N 365 
THR   HG23 H  N N 366 
THR   HXT  H  N N 367 
TRP   N    N  N N 368 
TRP   CA   C  N S 369 
TRP   C    C  N N 370 
TRP   O    O  N N 371 
TRP   CB   C  N N 372 
TRP   CG   C  Y N 373 
TRP   CD1  C  Y N 374 
TRP   CD2  C  Y N 375 
TRP   NE1  N  Y N 376 
TRP   CE2  C  Y N 377 
TRP   CE3  C  Y N 378 
TRP   CZ2  C  Y N 379 
TRP   CZ3  C  Y N 380 
TRP   CH2  C  Y N 381 
TRP   OXT  O  N N 382 
TRP   H    H  N N 383 
TRP   H2   H  N N 384 
TRP   HA   H  N N 385 
TRP   HB2  H  N N 386 
TRP   HB3  H  N N 387 
TRP   HD1  H  N N 388 
TRP   HE1  H  N N 389 
TRP   HE3  H  N N 390 
TRP   HZ2  H  N N 391 
TRP   HZ3  H  N N 392 
TRP   HH2  H  N N 393 
TRP   HXT  H  N N 394 
TYR   N    N  N N 395 
TYR   CA   C  N S 396 
TYR   C    C  N N 397 
TYR   O    O  N N 398 
TYR   CB   C  N N 399 
TYR   CG   C  Y N 400 
TYR   CD1  C  Y N 401 
TYR   CD2  C  Y N 402 
TYR   CE1  C  Y N 403 
TYR   CE2  C  Y N 404 
TYR   CZ   C  Y N 405 
TYR   OH   O  N N 406 
TYR   OXT  O  N N 407 
TYR   H    H  N N 408 
TYR   H2   H  N N 409 
TYR   HA   H  N N 410 
TYR   HB2  H  N N 411 
TYR   HB3  H  N N 412 
TYR   HD1  H  N N 413 
TYR   HD2  H  N N 414 
TYR   HE1  H  N N 415 
TYR   HE2  H  N N 416 
TYR   HH   H  N N 417 
TYR   HXT  H  N N 418 
VAL   N    N  N N 419 
VAL   CA   C  N S 420 
VAL   C    C  N N 421 
VAL   O    O  N N 422 
VAL   CB   C  N N 423 
VAL   CG1  C  N N 424 
VAL   CG2  C  N N 425 
VAL   OXT  O  N N 426 
VAL   H    H  N N 427 
VAL   H2   H  N N 428 
VAL   HA   H  N N 429 
VAL   HB   H  N N 430 
VAL   HG11 H  N N 431 
VAL   HG12 H  N N 432 
VAL   HG13 H  N N 433 
VAL   HG21 H  N N 434 
VAL   HG22 H  N N 435 
VAL   HG23 H  N N 436 
VAL   HXT  H  N N 437 
ZN    ZN   ZN N N 438 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1B36 C   S    sing N N 1   
A1B36 S   C1   sing N N 2   
A1B36 C1  C2   doub Y N 3   
A1B36 C2  C3   sing Y N 4   
A1B36 C3  C4   doub Y N 5   
A1B36 BR  C4   sing N N 6   
A1B36 C4  C5   sing Y N 7   
A1B36 C5  C6   doub Y N 8   
A1B36 C1  C6   sing Y N 9   
A1B36 C6  C7   sing N N 10  
A1B36 C7  C8   sing N N 11  
A1B36 O   C8   doub N N 12  
A1B36 C8  N    sing N N 13  
A1B36 N   C9   sing N N 14  
A1B36 C9  C10  sing N N 15  
A1B36 C10 C11  sing N N 16  
A1B36 C11 C12  sing N N 17  
A1B36 N1  C12  sing N N 18  
A1B36 C12 O1   doub N N 19  
A1B36 C13 C11  sing N N 20  
A1B36 N   C13  sing N N 21  
A1B36 N1  H14  sing N N 22  
A1B36 N1  H13  sing N N 23  
A1B36 C5  H6   sing N N 24  
A1B36 C7  H8   sing N N 25  
A1B36 C7  H7   sing N N 26  
A1B36 C10 H11  sing N N 27  
A1B36 C10 H12  sing N N 28  
A1B36 C13 H15  sing N N 29  
A1B36 C13 H16  sing N N 30  
A1B36 C11 H    sing N N 31  
A1B36 C9  H9   sing N N 32  
A1B36 C9  H10  sing N N 33  
A1B36 C   H2   sing N N 34  
A1B36 C   H1   sing N N 35  
A1B36 C   H3   sing N N 36  
A1B36 C3  H5   sing N N 37  
A1B36 C2  H4   sing N N 38  
ALA   N   CA   sing N N 39  
ALA   N   H    sing N N 40  
ALA   N   H2   sing N N 41  
ALA   CA  C    sing N N 42  
ALA   CA  CB   sing N N 43  
ALA   CA  HA   sing N N 44  
ALA   C   O    doub N N 45  
ALA   C   OXT  sing N N 46  
ALA   CB  HB1  sing N N 47  
ALA   CB  HB2  sing N N 48  
ALA   CB  HB3  sing N N 49  
ALA   OXT HXT  sing N N 50  
ARG   N   CA   sing N N 51  
ARG   N   H    sing N N 52  
ARG   N   H2   sing N N 53  
ARG   CA  C    sing N N 54  
ARG   CA  CB   sing N N 55  
ARG   CA  HA   sing N N 56  
ARG   C   O    doub N N 57  
ARG   C   OXT  sing N N 58  
ARG   CB  CG   sing N N 59  
ARG   CB  HB2  sing N N 60  
ARG   CB  HB3  sing N N 61  
ARG   CG  CD   sing N N 62  
ARG   CG  HG2  sing N N 63  
ARG   CG  HG3  sing N N 64  
ARG   CD  NE   sing N N 65  
ARG   CD  HD2  sing N N 66  
ARG   CD  HD3  sing N N 67  
ARG   NE  CZ   sing N N 68  
ARG   NE  HE   sing N N 69  
ARG   CZ  NH1  sing N N 70  
ARG   CZ  NH2  doub N N 71  
ARG   NH1 HH11 sing N N 72  
ARG   NH1 HH12 sing N N 73  
ARG   NH2 HH21 sing N N 74  
ARG   NH2 HH22 sing N N 75  
ARG   OXT HXT  sing N N 76  
ASN   N   CA   sing N N 77  
ASN   N   H    sing N N 78  
ASN   N   H2   sing N N 79  
ASN   CA  C    sing N N 80  
ASN   CA  CB   sing N N 81  
ASN   CA  HA   sing N N 82  
ASN   C   O    doub N N 83  
ASN   C   OXT  sing N N 84  
ASN   CB  CG   sing N N 85  
ASN   CB  HB2  sing N N 86  
ASN   CB  HB3  sing N N 87  
ASN   CG  OD1  doub N N 88  
ASN   CG  ND2  sing N N 89  
ASN   ND2 HD21 sing N N 90  
ASN   ND2 HD22 sing N N 91  
ASN   OXT HXT  sing N N 92  
ASP   N   CA   sing N N 93  
ASP   N   H    sing N N 94  
ASP   N   H2   sing N N 95  
ASP   CA  C    sing N N 96  
ASP   CA  CB   sing N N 97  
ASP   CA  HA   sing N N 98  
ASP   C   O    doub N N 99  
ASP   C   OXT  sing N N 100 
ASP   CB  CG   sing N N 101 
ASP   CB  HB2  sing N N 102 
ASP   CB  HB3  sing N N 103 
ASP   CG  OD1  doub N N 104 
ASP   CG  OD2  sing N N 105 
ASP   OD2 HD2  sing N N 106 
ASP   OXT HXT  sing N N 107 
CYS   N   CA   sing N N 108 
CYS   N   H    sing N N 109 
CYS   N   H2   sing N N 110 
CYS   CA  C    sing N N 111 
CYS   CA  CB   sing N N 112 
CYS   CA  HA   sing N N 113 
CYS   C   O    doub N N 114 
CYS   C   OXT  sing N N 115 
CYS   CB  SG   sing N N 116 
CYS   CB  HB2  sing N N 117 
CYS   CB  HB3  sing N N 118 
CYS   SG  HG   sing N N 119 
CYS   OXT HXT  sing N N 120 
DMS   S   O    doub N N 121 
DMS   S   C1   sing N N 122 
DMS   S   C2   sing N N 123 
DMS   C1  H11  sing N N 124 
DMS   C1  H12  sing N N 125 
DMS   C1  H13  sing N N 126 
DMS   C2  H21  sing N N 127 
DMS   C2  H22  sing N N 128 
DMS   C2  H23  sing N N 129 
GLN   N   CA   sing N N 130 
GLN   N   H    sing N N 131 
GLN   N   H2   sing N N 132 
GLN   CA  C    sing N N 133 
GLN   CA  CB   sing N N 134 
GLN   CA  HA   sing N N 135 
GLN   C   O    doub N N 136 
GLN   C   OXT  sing N N 137 
GLN   CB  CG   sing N N 138 
GLN   CB  HB2  sing N N 139 
GLN   CB  HB3  sing N N 140 
GLN   CG  CD   sing N N 141 
GLN   CG  HG2  sing N N 142 
GLN   CG  HG3  sing N N 143 
GLN   CD  OE1  doub N N 144 
GLN   CD  NE2  sing N N 145 
GLN   NE2 HE21 sing N N 146 
GLN   NE2 HE22 sing N N 147 
GLN   OXT HXT  sing N N 148 
GLU   N   CA   sing N N 149 
GLU   N   H    sing N N 150 
GLU   N   H2   sing N N 151 
GLU   CA  C    sing N N 152 
GLU   CA  CB   sing N N 153 
GLU   CA  HA   sing N N 154 
GLU   C   O    doub N N 155 
GLU   C   OXT  sing N N 156 
GLU   CB  CG   sing N N 157 
GLU   CB  HB2  sing N N 158 
GLU   CB  HB3  sing N N 159 
GLU   CG  CD   sing N N 160 
GLU   CG  HG2  sing N N 161 
GLU   CG  HG3  sing N N 162 
GLU   CD  OE1  doub N N 163 
GLU   CD  OE2  sing N N 164 
GLU   OE2 HE2  sing N N 165 
GLU   OXT HXT  sing N N 166 
GLY   N   CA   sing N N 167 
GLY   N   H    sing N N 168 
GLY   N   H2   sing N N 169 
GLY   CA  C    sing N N 170 
GLY   CA  HA2  sing N N 171 
GLY   CA  HA3  sing N N 172 
GLY   C   O    doub N N 173 
GLY   C   OXT  sing N N 174 
GLY   OXT HXT  sing N N 175 
HIS   N   CA   sing N N 176 
HIS   N   H    sing N N 177 
HIS   N   H2   sing N N 178 
HIS   CA  C    sing N N 179 
HIS   CA  CB   sing N N 180 
HIS   CA  HA   sing N N 181 
HIS   C   O    doub N N 182 
HIS   C   OXT  sing N N 183 
HIS   CB  CG   sing N N 184 
HIS   CB  HB2  sing N N 185 
HIS   CB  HB3  sing N N 186 
HIS   CG  ND1  sing Y N 187 
HIS   CG  CD2  doub Y N 188 
HIS   ND1 CE1  doub Y N 189 
HIS   ND1 HD1  sing N N 190 
HIS   CD2 NE2  sing Y N 191 
HIS   CD2 HD2  sing N N 192 
HIS   CE1 NE2  sing Y N 193 
HIS   CE1 HE1  sing N N 194 
HIS   NE2 HE2  sing N N 195 
HIS   OXT HXT  sing N N 196 
HOH   O   H1   sing N N 197 
HOH   O   H2   sing N N 198 
ILE   N   CA   sing N N 199 
ILE   N   H    sing N N 200 
ILE   N   H2   sing N N 201 
ILE   CA  C    sing N N 202 
ILE   CA  CB   sing N N 203 
ILE   CA  HA   sing N N 204 
ILE   C   O    doub N N 205 
ILE   C   OXT  sing N N 206 
ILE   CB  CG1  sing N N 207 
ILE   CB  CG2  sing N N 208 
ILE   CB  HB   sing N N 209 
ILE   CG1 CD1  sing N N 210 
ILE   CG1 HG12 sing N N 211 
ILE   CG1 HG13 sing N N 212 
ILE   CG2 HG21 sing N N 213 
ILE   CG2 HG22 sing N N 214 
ILE   CG2 HG23 sing N N 215 
ILE   CD1 HD11 sing N N 216 
ILE   CD1 HD12 sing N N 217 
ILE   CD1 HD13 sing N N 218 
ILE   OXT HXT  sing N N 219 
LEU   N   CA   sing N N 220 
LEU   N   H    sing N N 221 
LEU   N   H2   sing N N 222 
LEU   CA  C    sing N N 223 
LEU   CA  CB   sing N N 224 
LEU   CA  HA   sing N N 225 
LEU   C   O    doub N N 226 
LEU   C   OXT  sing N N 227 
LEU   CB  CG   sing N N 228 
LEU   CB  HB2  sing N N 229 
LEU   CB  HB3  sing N N 230 
LEU   CG  CD1  sing N N 231 
LEU   CG  CD2  sing N N 232 
LEU   CG  HG   sing N N 233 
LEU   CD1 HD11 sing N N 234 
LEU   CD1 HD12 sing N N 235 
LEU   CD1 HD13 sing N N 236 
LEU   CD2 HD21 sing N N 237 
LEU   CD2 HD22 sing N N 238 
LEU   CD2 HD23 sing N N 239 
LEU   OXT HXT  sing N N 240 
LYS   N   CA   sing N N 241 
LYS   N   H    sing N N 242 
LYS   N   H2   sing N N 243 
LYS   CA  C    sing N N 244 
LYS   CA  CB   sing N N 245 
LYS   CA  HA   sing N N 246 
LYS   C   O    doub N N 247 
LYS   C   OXT  sing N N 248 
LYS   CB  CG   sing N N 249 
LYS   CB  HB2  sing N N 250 
LYS   CB  HB3  sing N N 251 
LYS   CG  CD   sing N N 252 
LYS   CG  HG2  sing N N 253 
LYS   CG  HG3  sing N N 254 
LYS   CD  CE   sing N N 255 
LYS   CD  HD2  sing N N 256 
LYS   CD  HD3  sing N N 257 
LYS   CE  NZ   sing N N 258 
LYS   CE  HE2  sing N N 259 
LYS   CE  HE3  sing N N 260 
LYS   NZ  HZ1  sing N N 261 
LYS   NZ  HZ2  sing N N 262 
LYS   NZ  HZ3  sing N N 263 
LYS   OXT HXT  sing N N 264 
MET   N   CA   sing N N 265 
MET   N   H    sing N N 266 
MET   N   H2   sing N N 267 
MET   CA  C    sing N N 268 
MET   CA  CB   sing N N 269 
MET   CA  HA   sing N N 270 
MET   C   O    doub N N 271 
MET   C   OXT  sing N N 272 
MET   CB  CG   sing N N 273 
MET   CB  HB2  sing N N 274 
MET   CB  HB3  sing N N 275 
MET   CG  SD   sing N N 276 
MET   CG  HG2  sing N N 277 
MET   CG  HG3  sing N N 278 
MET   SD  CE   sing N N 279 
MET   CE  HE1  sing N N 280 
MET   CE  HE2  sing N N 281 
MET   CE  HE3  sing N N 282 
MET   OXT HXT  sing N N 283 
PHE   N   CA   sing N N 284 
PHE   N   H    sing N N 285 
PHE   N   H2   sing N N 286 
PHE   CA  C    sing N N 287 
PHE   CA  CB   sing N N 288 
PHE   CA  HA   sing N N 289 
PHE   C   O    doub N N 290 
PHE   C   OXT  sing N N 291 
PHE   CB  CG   sing N N 292 
PHE   CB  HB2  sing N N 293 
PHE   CB  HB3  sing N N 294 
PHE   CG  CD1  doub Y N 295 
PHE   CG  CD2  sing Y N 296 
PHE   CD1 CE1  sing Y N 297 
PHE   CD1 HD1  sing N N 298 
PHE   CD2 CE2  doub Y N 299 
PHE   CD2 HD2  sing N N 300 
PHE   CE1 CZ   doub Y N 301 
PHE   CE1 HE1  sing N N 302 
PHE   CE2 CZ   sing Y N 303 
PHE   CE2 HE2  sing N N 304 
PHE   CZ  HZ   sing N N 305 
PHE   OXT HXT  sing N N 306 
PRO   N   CA   sing N N 307 
PRO   N   CD   sing N N 308 
PRO   N   H    sing N N 309 
PRO   CA  C    sing N N 310 
PRO   CA  CB   sing N N 311 
PRO   CA  HA   sing N N 312 
PRO   C   O    doub N N 313 
PRO   C   OXT  sing N N 314 
PRO   CB  CG   sing N N 315 
PRO   CB  HB2  sing N N 316 
PRO   CB  HB3  sing N N 317 
PRO   CG  CD   sing N N 318 
PRO   CG  HG2  sing N N 319 
PRO   CG  HG3  sing N N 320 
PRO   CD  HD2  sing N N 321 
PRO   CD  HD3  sing N N 322 
PRO   OXT HXT  sing N N 323 
SER   N   CA   sing N N 324 
SER   N   H    sing N N 325 
SER   N   H2   sing N N 326 
SER   CA  C    sing N N 327 
SER   CA  CB   sing N N 328 
SER   CA  HA   sing N N 329 
SER   C   O    doub N N 330 
SER   C   OXT  sing N N 331 
SER   CB  OG   sing N N 332 
SER   CB  HB2  sing N N 333 
SER   CB  HB3  sing N N 334 
SER   OG  HG   sing N N 335 
SER   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TRP   N   CA   sing N N 353 
TRP   N   H    sing N N 354 
TRP   N   H2   sing N N 355 
TRP   CA  C    sing N N 356 
TRP   CA  CB   sing N N 357 
TRP   CA  HA   sing N N 358 
TRP   C   O    doub N N 359 
TRP   C   OXT  sing N N 360 
TRP   CB  CG   sing N N 361 
TRP   CB  HB2  sing N N 362 
TRP   CB  HB3  sing N N 363 
TRP   CG  CD1  doub Y N 364 
TRP   CG  CD2  sing Y N 365 
TRP   CD1 NE1  sing Y N 366 
TRP   CD1 HD1  sing N N 367 
TRP   CD2 CE2  doub Y N 368 
TRP   CD2 CE3  sing Y N 369 
TRP   NE1 CE2  sing Y N 370 
TRP   NE1 HE1  sing N N 371 
TRP   CE2 CZ2  sing Y N 372 
TRP   CE3 CZ3  doub Y N 373 
TRP   CE3 HE3  sing N N 374 
TRP   CZ2 CH2  doub Y N 375 
TRP   CZ2 HZ2  sing N N 376 
TRP   CZ3 CH2  sing Y N 377 
TRP   CZ3 HZ3  sing N N 378 
TRP   CH2 HH2  sing N N 379 
TRP   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_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                    7I5P 
_atom_sites.fract_transf_matrix[1][1]   0.011302 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000478 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017357 
_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]   0.030600 
_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 
BR 
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   ? 19.025 7.175   23.984 1.00 33.64  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.183 7.360   23.109 1.00 34.29  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.294 6.179   22.132 1.00 34.15  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.625 5.154   22.329 1.00 34.07  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.458 7.513   23.945 1.00 36.41  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.764 6.256   24.523 1.00 39.45  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.106 6.346   21.078 1.00 33.80  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.332 5.305   20.083 1.00 33.55  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.654 5.802   18.676 1.00 32.81  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.259 6.902   18.294 1.00 32.22  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.335 4.970   17.869 1.00 31.62  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.696 5.360   16.509 1.00 31.52  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.637 4.195   15.523 1.00 30.40  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.672 3.034   15.941 1.00 31.71  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.120 5.962   16.509 1.00 31.94  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.590 4.493   14.208 1.00 28.64  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.709 3.489   13.137 1.00 28.65  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.130 3.651   12.553 1.00 29.84  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.559 4.793   12.311 1.00 30.50  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.670 3.752   12.004 1.00 28.05  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.217 3.739   12.530 1.00 26.84  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.874 2.743   10.845 1.00 28.19  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.210 4.392   11.550 1.00 27.02  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.876 2.544   12.353 1.00 30.92  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.238 2.627   11.785 1.00 31.89  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.242 1.877   10.459 1.00 32.59  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.194 0.643   10.469 1.00 33.71  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.295 2.047   12.753 1.00 32.07  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.451 2.867   14.014 1.00 33.43  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.243 4.009   14.031 1.00 34.10  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.746 2.548   15.165 1.00 34.75  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.342 4.802   15.166 1.00 35.00  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.851 3.323   16.311 1.00 35.64  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.649 4.452   16.306 1.00 36.23  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.701 5.251   17.416 1.00 38.52  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.160 2.605   9.326  1.00 32.26  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.137 2.057   7.965  1.00 32.69  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.284 2.658   7.161  1.00 34.79  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.409 3.895   7.075  1.00 34.38  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.772 2.257   7.246  1.00 33.79  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.304 3.730   7.295  1.00 33.50  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.818 1.722   5.809  1.00 33.71  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.172 1.803   6.626  1.00 35.59  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.332 2.289   5.868  1.00 36.92  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.189 3.236   6.693  1.00 37.91  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.427 2.946   7.867  1.00 38.55  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.516 4.434   6.168  1.00 38.27  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.257 5.408   6.964  1.00 39.01  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.331 6.520   7.467  1.00 37.98  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.721 7.691   7.500  1.00 38.33  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.479 5.954   6.203  1.00 41.45  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.539 4.891   6.087  1.00 46.99  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.315 4.650   7.018  1.00 48.74  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.546 4.180   4.974  1.00 48.82  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.116 6.140   7.907  1.00 36.22  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.094 7.082   8.399  1.00 34.49  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.563 6.684   9.769  1.00 33.25  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.450 5.498   10.074 1.00 32.81  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.896 7.158   7.424  1.00 34.68  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.234 7.696   6.055  1.00 35.50  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.880 8.924   5.905  1.00 36.03  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.886 7.000   4.909  1.00 36.07  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.192 9.423   4.649  1.00 36.85  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.184 7.495   3.646  1.00 37.09  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.834 8.710   3.520  1.00 38.17  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.144 9.199   2.276  1.00 40.34  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.213 7.683   10.582 1.00 32.59  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.616 7.510   11.906 1.00 32.17  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.322 8.320   11.890 1.00 31.40  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.350 9.536   11.681 1.00 31.30  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.565 8.009   13.006 1.00 34.16  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.916 8.191   14.371 1.00 36.64  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.953 8.623   15.393 1.00 38.02  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.445 9.640   16.318 1.00 39.90  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.923 9.379   17.514 1.00 39.80  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.787 8.126   17.926 1.00 38.36  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.489 10.366  18.284 1.00 39.50  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.190 7.645   12.036 1.00 29.67  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.892 8.324   12.009 1.00 29.60  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.364 8.432   13.409 1.00 29.27  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.145 7.400   14.061 1.00 29.72  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.869 7.574   11.123 1.00 30.63  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.573 8.376   10.991 1.00 30.41  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.476 7.252   9.746  1.00 30.94  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.119 9.654   13.866 1.00 28.04  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.579 9.837   15.209 1.00 28.63  ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.394 10.806  15.154 1.00 28.21  ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.188 11.494  14.136 1.00 29.17  ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.662 10.404  16.170 1.00 29.37  ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.828 9.441   16.346 1.00 30.81  ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.130 11.792  15.693 1.00 29.56  ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.643 10.938  16.277 1.00 27.04  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.645 12.001  16.399 1.00 25.72  ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.415 13.339  16.409 1.00 26.74  ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.413 13.478  17.146 1.00 26.84  ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.928 11.908  17.750 1.00 26.31  ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.078 10.653  17.847 1.00 27.37  ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.551 9.619   18.323 1.00 28.37  ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.844 10.703  17.323 1.00 25.64  ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.934 14.333  15.668 1.00 26.30  ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.638 15.631  15.615 1.00 27.47  ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.716 16.261  16.993 1.00 28.87  ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.769 16.810  17.359 1.00 30.23  ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.928 16.565  14.653 1.00 27.94  ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.713 17.857  14.332 1.00 29.63  ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.764 18.715  13.529 1.00 30.27  ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.342 19.977  13.042 1.00 33.65  ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.295 21.129  13.710 1.00 36.60  ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.825 21.168  14.950 1.00 36.27  ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.700 22.253  13.135 1.00 36.30  ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.632 16.128  17.794 1.00 28.09  ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.627 16.746  19.125 1.00 29.37  ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.638 16.107  20.100 1.00 30.44  ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.966 16.725  21.103 1.00 30.66  ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.216 16.854  19.735 1.00 29.69  ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.637 15.563  20.212 1.00 30.06  ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.963 14.707  19.347 1.00 31.46  ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.617 15.032  21.459 1.00 31.28  ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.569 13.679  20.091 1.00 31.50  ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.926 13.831  21.369 1.00 31.48  ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.150 14.921  19.789 1.00 31.13  ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.153 14.244  20.625 1.00 33.29  ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.564 14.259  20.016 1.00 35.20  ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.463 13.632  20.570 1.00 35.85  ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.712 12.784  20.916 1.00 33.05  ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.359 12.657  21.613 1.00 34.62  ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.009 11.166  21.864 1.00 35.31  ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.322 13.472  22.927 1.00 35.04  ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.758 14.916  18.861 1.00 36.02  ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.078 14.968  18.220 1.00 37.69  ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.086 15.674  19.137 1.00 39.84  ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.719 16.613  19.841 1.00 39.35  ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.978 15.705  16.898 1.00 37.73  ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.311 15.167  19.183 1.00 42.43  ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.405 15.727  19.990 1.00 45.49  ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.126 16.832  19.188 1.00 47.96  ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.032 16.851  17.955 1.00 48.22  ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.394 14.613  20.346 1.00 47.57  ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.043 14.156  19.154 1.00 49.19  ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.728 13.436  21.061 1.00 47.29  ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.901 17.727  19.861 1.00 49.08  ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.631 18.795  19.133 1.00 49.00  ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.532 18.202  18.006 1.00 48.48  ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.634 18.775  16.925 1.00 49.53  ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.394 19.733  20.106 1.00 50.26  ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.438 19.051  20.936 1.00 53.94  ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 32.794 19.355  20.789 1.00 56.96  ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 31.301 18.135  21.924 1.00 55.33  ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 33.436 18.577  21.658 1.00 57.34  ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 32.582 17.826  22.366 1.00 57.27  ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.012 16.986  18.227 1.00 47.00  ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.819 16.127  17.357 1.00 47.59  ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.091 15.602  16.116 1.00 46.99  ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.736 15.328  15.110 1.00 47.97  ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.355 14.978  18.170 1.00 49.92  ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.214 15.434  19.336 1.00 57.81  ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 33.025 15.000  20.479 1.00 62.80  ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 34.179 16.313  19.085 1.00 56.58  ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.757 15.387  16.202 1.00 44.31  ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.936 14.989  15.064 1.00 41.47  ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.803 16.227  14.136 1.00 39.03  ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.847 16.087  12.915 1.00 38.41  ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.517 14.573  15.545 1.00 40.74  ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.432 13.200  16.168 1.00 42.86  ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.016 12.257  15.599 1.00 42.13  ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.792 13.071  17.241 1.00 43.06  ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.579 17.415  14.710 1.00 38.12  ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.473 18.656  13.928 1.00 39.29  ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.777 18.975  13.150 1.00 40.75  ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.732 19.376  11.979 1.00 41.12  ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.134 19.828  14.852 1.00 39.54  ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.698 19.816  15.263 1.00 39.45  ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.185 19.415  16.459 1.00 40.53  ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.584 20.185  14.444 1.00 39.88  ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.803 19.495  16.433 1.00 41.19  ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.412 19.998  15.214 1.00 40.80  ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.458 20.619  13.118 1.00 40.34  ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.142 20.257  14.708 1.00 40.83  ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.199 20.899  12.627 1.00 41.23  ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.054 20.684  13.409 1.00 41.01  ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.925 18.733  13.777 1.00 40.88  ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.215 18.948  13.101 1.00 43.07  ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.337 17.978  11.900 1.00 43.50  ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 32.866 18.350  10.848 1.00 44.43  ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.365 18.705  14.083 1.00 43.44  ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.813 16.751  12.045 1.00 42.23  ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.922 15.761  10.982 1.00 42.30  ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.618 15.594  10.205 1.00 40.84  ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.325 14.486  9.725  1.00 40.98  ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.338 14.431  11.601 1.00 45.56  ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.748 14.503  12.144 1.00 51.01  ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.709 14.691  11.388 1.00 52.19  ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.906 14.367  13.462 1.00 52.21  ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.838 16.669  10.097 1.00 37.73  ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.535 16.641  9.457  1.00 36.90  ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.560 16.269  7.980  1.00 36.86  ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.402 16.758  7.217  1.00 36.05  ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.841 18.008  9.619  1.00 35.66  ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.400 18.126  9.072  1.00 35.81  ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.450 17.251  9.897  1.00 35.40  ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 25.910 19.601  9.110  1.00 35.64  ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.592 15.437  7.577  1.00 35.71  ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.363 15.073  6.193  1.00 36.12  ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.003 15.732  5.778  1.00 36.07  ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.899 16.427  4.759  1.00 36.43  ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.305 13.517  6.029  1.00 36.73  ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.816 13.135  4.635  1.00 37.36  ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.657 12.858  6.330  1.00 36.88  ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.946 15.499  6.595  1.00 34.73  ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.628 15.982  6.302  1.00 34.94  ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.802 16.002  7.574  1.00 33.97  ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.928 15.113  8.409  1.00 33.10  ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.940 15.061  5.278  1.00 34.81  ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.466 15.313  5.088  1.00 34.99  ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.883 16.248  4.277  1.00 36.34  ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.394 14.601  5.723  1.00 33.95  ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.504 16.152  4.365  1.00 36.56  ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.182 15.167  5.268  1.00 34.93  ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.341 13.542  6.643  1.00 33.60  ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.937 14.677  5.665  1.00 34.13  ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.101 13.073  7.049  1.00 33.18  ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.923 13.623  6.543  1.00 33.44  ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.953 17.026  7.705  1.00 32.00  ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.050 17.119  8.840  1.00 31.43  ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.753 17.804  8.393  1.00 31.05  ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.755 18.630  7.456  1.00 31.33  ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.717 17.848  10.020 1.00 33.10  ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.267 19.236  9.664  1.00 35.29  ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.310 20.415  9.795  1.00 38.86  ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.669 21.517  9.317  1.00 39.26  ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.213 20.248  10.380 1.00 36.80  ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.637 17.475  9.064  1.00 29.77  ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.371 18.103  8.750  1.00 29.74  ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.585 18.212  10.052 1.00 28.65  ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.158 17.196  10.616 1.00 28.02  ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.632 17.312  7.665  1.00 32.03  ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.360 17.920  7.135  1.00 39.08  ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.845 18.871  7.765  1.00 42.11  ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.870 17.445  6.082  1.00 41.17  ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.439 19.446  10.550 1.00 27.81  ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.715 19.719  11.784 0.50 28.35  ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.728 19.653  11.811 0.50 28.54  ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.266 19.201  11.693 1.00 28.23  ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.738 18.643  12.659 1.00 29.83  ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.705 21.228  12.040 0.50 29.43  ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.795 21.117  12.250 0.50 30.34  ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.010 21.537  13.232 0.50 31.60  ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.992 21.904  11.392 0.50 32.97  ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.630 19.371  10.506 1.00 26.81  ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.237 18.929  10.356 1.00 27.89  ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.083 17.406  10.389 1.00 27.03  ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.988 16.955  10.585 1.00 28.41  ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.563 19.520  9.124  1.00 31.57  ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.242 19.107  7.954  1.00 38.05  ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.158 16.650  10.246 1.00 25.78  ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.116 15.184  10.355 1.00 25.49  ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.744 14.683  11.688 1.00 26.12  ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.745 13.452  11.940 1.00 25.76  ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.906 14.567  9.186  1.00 26.87  ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.198 14.674  7.847  1.00 27.78  ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.080 14.078  6.757  1.00 27.87  ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.051 12.615  6.855  1.00 27.75  ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.120 11.794  5.808  1.00 29.43  ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.247 12.283  4.574  1.00 28.39  ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.076 10.480  5.985  1.00 28.05  ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.326 15.599  12.513 1.00 25.26  ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.086 15.229  13.731 1.00 25.48  ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.204 14.225  13.390 1.00 26.41  ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.471 13.312  14.193 1.00 26.56  ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.180 14.671  14.886 1.00 26.04  ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.949 14.387  16.186 1.00 26.73  ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.820 15.214  16.559 1.00 26.59  ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.746 13.287  16.783 1.00 28.37  ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.898 14.398  12.220 1.00 26.38  ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.001 13.487  11.848 1.00 27.08  ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.303 14.256  11.605 1.00 27.72  ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.269 15.383  11.102 1.00 27.45  ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.703 12.692  10.570 1.00 27.26  ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.638 11.576  10.660 1.00 28.95  ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.444 10.906  9.299  1.00 28.48  ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.032 10.542  11.670 1.00 28.81  ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.425 13.614  11.949 1.00 27.28  ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.770 14.123  11.676 1.00 28.69  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.617 12.931  11.284 1.00 29.51  ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.499 11.846  11.877 1.00 29.67  ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.358 14.876  12.885 1.00 29.34  ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.761 15.539  12.687 1.00 31.15  ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.822 16.900  13.380 1.00 31.97  ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.869 14.633  13.196 1.00 32.22  ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.429 13.091  10.240 1.00 29.76  ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.324 12.026  9.797  1.00 31.47  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.733 12.617  9.802  1.00 33.00  ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.960 13.700  9.234  1.00 32.41  ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.956 11.474  8.396  1.00 32.52  ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.016 10.479  7.894  1.00 33.76  ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.554 10.845  8.383  1.00 32.03  ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.649 11.956  10.494 1.00 33.45  ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.055 12.394  10.542 1.00 34.68  ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.962 11.296  9.976  1.00 36.45  ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.577 10.124  9.935  1.00 35.36  ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.469 12.762  11.966 1.00 35.25  ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.299 11.660  12.846 1.00 37.54  ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.178 11.678  9.510  1.00 38.26  ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.100 10.700  8.933  1.00 39.87  ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.842 9.943   10.042 1.00 41.56  ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.070 10.507  11.117 1.00 42.70  ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.132 11.411  8.057  1.00 42.09  ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.804 12.385  8.836  1.00 45.06  ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.237 8.679   9.784  1.00 41.27  ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.007 7.887   10.753 1.00 42.66  ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.320 7.378   10.099 1.00 45.59  ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.380 7.231   8.868  1.00 46.42  ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.206 6.635   11.268 1.00 42.72  ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.139 5.645   10.243 1.00 43.58  ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.808 6.969   11.776 1.00 41.34  ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.331 7.033   10.915 1.00 46.86  ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.561 6.462   10.358 1.00 49.50  ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.403 4.941   10.149 1.00 50.27  ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.946 4.384   9.188  1.00 51.41  ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.778 6.803   11.241 1.00 53.47  ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.573 6.206   12.525 1.00 56.18  ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.985 8.316   11.391 1.00 54.19  ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.664 4.270   11.043 1.00 49.30  ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.469 2.826   10.941 1.00 49.20  ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.198 2.487   10.155 1.00 48.28  ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.205 3.201   10.243 1.00 47.75  ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.389 2.215   12.333 1.00 49.68  ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.225 1.380   9.411  1.00 47.12  ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.067 0.950   8.639  1.00 46.50  ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.025 0.261   9.543  1.00 43.10  ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.368 -0.629  10.319 1.00 42.62  ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.521 0.007   7.521  1.00 50.05  ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.469 -0.250  6.451  1.00 56.36  ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.114 -1.024  5.333  1.00 62.86  ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.071 -0.551  4.697  1.00 63.96  ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.627 -2.242  5.090  1.00 63.59  ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.772 0.691   9.419  1.00 40.31  ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.631 0.174   10.167 1.00 38.40  ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.011 -1.031  9.491  1.00 36.51  ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.306 -1.299  8.323  1.00 37.40  ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.188 -1.799  10.231 1.00 33.42  ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.655 -3.043  9.711  1.00 33.23  ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.126 -3.122  9.620  1.00 32.60  ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.594 -4.206  9.332  1.00 32.79  ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.207 -4.204  10.522 1.00 34.67  ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.007 -4.335  10.445 1.00 38.84  ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.420 -2.027  9.935  1.00 31.78  ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.955 -2.058  9.857  1.00 32.19  ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.559 -2.024  8.370  1.00 33.07  ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.251 -1.418  7.537  1.00 34.44  ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.324 -0.870  10.645 1.00 32.20  ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.532 -0.997  12.155 1.00 36.99  ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.627 -2.147  12.650 1.00 38.42  ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.616 0.054   12.845 1.00 36.80  ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.520 -2.753  8.030  1.00 32.43  ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.959 -2.720  6.681  1.00 33.47  ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.657 -1.899  6.760  1.00 31.88  ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.851 -2.156  7.643  1.00 30.31  ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.598 -4.139  6.240  1.00 37.12  ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.827 -4.838  5.994  1.00 40.03  ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.719 -4.161  4.973  1.00 37.68  ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.462 -0.964  5.849  1.00 31.54  ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.259 -0.148  5.811  1.00 31.29  ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.223 -0.887  4.959  1.00 30.78  ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.564 -1.433  3.906  1.00 30.85  ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.550 1.252   5.241  1.00 31.99  ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.680 1.974   6.047  1.00 32.46  ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.266 2.112   5.223  1.00 32.50  ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.353 2.093   7.560  1.00 32.43  ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.974 -0.927  5.424  1.00 28.09  ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.894 -1.558  4.688  1.00 27.64  ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.504 -0.695  3.498  1.00 27.17  ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.433 0.519   3.625  1.00 27.34  ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.678 -1.698  5.607  1.00 27.59  ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.183 -1.314  2.358  1.00 27.68  ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.669 -0.565  1.196  1.00 28.11  ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.336 -1.254  0.832  1.00 28.92  ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.315 -2.230  0.072  1.00 28.83  ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.674 -0.565  0.041  1.00 29.06  ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.064 -0.043  0.434  1.00 31.04  ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.117 1.430   0.808  1.00 34.67  ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.483 1.826   1.185  1.00 36.55  ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.786 2.955   1.821  1.00 38.66  ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.834 3.827   2.133  1.00 36.68  ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.045 3.227   2.138  1.00 38.41  ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.249 -0.824  1.496  1.00 29.35  ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.969 -1.519  1.443  1.00 29.68  ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.810  -0.593  1.872  1.00 30.64  ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.045 0.556   2.288  1.00 29.55  ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.065 -2.691  2.410  1.00 29.27  ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.176 -2.160  4.148  1.00 29.35  ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.554  -1.143  1.871  1.00 31.76  ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.397  -0.414  2.396  1.00 32.77  ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.779  -1.185  3.597  1.00 32.59  ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.572  -1.068  3.848  1.00 32.56  ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.319  -0.154  1.313  1.00 36.17  ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.697  -1.397  0.705  1.00 44.15  ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.130  -2.519  1.061  1.00 45.28  ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.785  -1.253  -0.147 1.00 48.86  ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.595  -1.967  4.345  1.00 31.48  ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.117  -2.678  5.542  1.00 30.13  ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.387  -1.732  6.514  1.00 28.48  ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.770  -0.567  6.666  1.00 27.84  ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.275  -3.373  6.252  1.00 30.96  ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.775  -4.938  5.492  1.00 31.46  ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.314  -2.224  7.117  1.00 26.79  ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.589  -1.467  8.137  1.00 26.60  ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.501  -2.263  9.466  1.00 26.70  ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.657  -1.951  10.305 1.00 25.95  ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.179  -1.059  7.646  1.00 29.33  ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.123  0.270   6.917  1.00 32.77  ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.654  0.641   6.704  1.00 36.88  ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.101  0.438   5.610  1.00 37.19  ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.974  1.179   7.757  1.00 36.60  ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.312  -3.352  9.612  1.00 25.03  ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.418  -4.136  10.826 1.00 24.80  ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.929  -4.356  11.035 1.00 25.15  ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.723  -4.407  10.082 1.00 24.73  ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.645  -5.477  10.764 1.00 27.49  ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.250  -6.310  9.798  1.00 30.61  ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.141  -5.299  10.437 1.00 27.56  ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.321  -4.375  12.287 1.00 24.90  ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.732  -4.460  12.644 1.00 24.56  ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.879  -4.632  14.136 1.00 24.77  ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.917  -4.968  14.822 1.00 26.26  ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.089 -4.467  14.626 1.00 23.81  ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.393 -4.613  16.047 1.00 24.38  ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.237 -3.428  16.453 1.00 24.13  ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.176 -3.084  15.735 1.00 25.17  ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.165 -5.932  16.292 1.00 25.76  ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.644 -6.039  17.738 1.00 26.58  ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.311 -7.134  15.911 1.00 26.86  ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.942 -2.808  17.603 1.00 24.03  ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.791 -1.684  18.047 1.00 23.15  ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.393 -1.933  19.413 1.00 24.35  ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.782 -2.606  20.227 1.00 25.56  ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.075 -0.302  18.010 1.00 22.75  ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.135 -0.040  19.171 1.00 24.55  ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.883  -0.645  19.232 1.00 25.86  ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.489 0.830   20.200 1.00 25.20  ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.998  -0.374  20.274 1.00 26.77  ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.609  1.112   21.248 1.00 25.92  ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.361  0.517   21.278 1.00 26.89  ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.482  0.774   22.311 1.00 27.69  ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.532 -1.304  19.692 1.00 24.55  ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.136 -1.409  21.013 1.00 25.15  ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.666 -0.252  21.918 1.00 25.55  ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.879 0.908   21.592 1.00 25.10  ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.655 -1.434  20.948 1.00 24.76  ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.253 -1.549  22.331 1.00 25.71  ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.998 -2.661  23.132 1.00 27.12  ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.053 -0.537  22.851 1.00 27.73  ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.560 -2.776  24.411 1.00 28.41  ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.632 -0.649  24.116 1.00 28.50  ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.352 -1.749  24.904 1.00 29.68  ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.899 -1.816  26.170 1.00 31.09  ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.151 -0.594  23.097 1.00 26.00  ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.695 0.366   24.089 1.00 26.87  ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.649 0.322   25.298 1.00 27.51  ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.549 -0.600  26.100 1.00 28.14  ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.263 0.036   24.493 1.00 28.55  ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.610 1.091   25.806 1.00 29.75  ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.599 1.289   25.410 1.00 26.37  ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.575 1.236   26.492 1.00 27.35  ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.955 1.420   27.875 1.00 27.69  ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.454 0.837   28.845 1.00 28.59  ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.737 2.200   26.272 1.00 29.99  ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.334 3.541   26.443 1.00 34.15  ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.840 2.169   27.971 1.00 26.70  ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.132 2.352   29.268 1.00 26.74  ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.454 1.063   29.795 1.00 27.87  ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.950 1.037   30.936 1.00 29.87  ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.109 3.486   29.193 1.00 25.88  ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.047 3.200   28.298 1.00 27.99  ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.433 0.012   29.003 1.00 26.47  ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.928 -1.304  29.432 1.00 26.90  ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.967 -2.416  29.221 1.00 27.83  ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.692 -3.572  29.547 1.00 28.10  ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.658 -1.662  28.641 1.00 28.60  ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.485  -0.716  28.939 1.00 29.29  ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.847  -1.086  30.268 1.00 30.75  ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.703  -0.229  30.584 1.00 33.10  ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.802  0.945   31.196 1.00 34.04  ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.991  1.403   31.587 1.00 32.65  ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.713  1.675   31.424 1.00 34.28  ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.136 -2.111  28.584 1.00 28.39  ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.147 -3.120  28.204 1.00 29.69  ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.454 -4.246  27.406 1.00 30.10  ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.677 -5.436  27.656 1.00 31.44  ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.921 -3.694  29.425 1.00 31.39  ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.699 -2.650  30.223 1.00 35.86  ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.504 -3.342  31.330 1.00 39.47  ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.190 -2.379  32.184 1.00 41.93  ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.079 -2.339  33.512 1.00 44.56  ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.283 -3.197  34.145 1.00 44.31  ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.728 -1.406  34.215 1.00 42.51  ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.554 -3.850  26.486 1.00 28.88  ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.768 -4.825  25.748 1.00 29.52  ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.594 -4.417  24.308 1.00 28.35  ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.561 -3.220  23.993 1.00 28.77  ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.372 -4.996  26.412 1.00 32.82  ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.936 -6.454  26.504 1.00 40.86  ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.582  -6.589  27.215 1.00 48.44  ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 8.623  -7.503  26.475 1.00 52.87  ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.209  -8.858  26.275 1.00 56.31  ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.463 -5.411  23.448 1.00 26.41  ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.225 -5.216  22.014 1.00 26.50  ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.752 -5.556  21.822 1.00 27.84  ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.306 -6.639  22.259 1.00 29.07  ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 13.117 -6.151  21.158 1.00 27.31  ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.586 -5.909  21.337 1.00 28.09  ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.326 -5.217  20.389 1.00 30.16  ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.385 -6.193  22.389 1.00 27.84  ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.557 -5.164  20.868 1.00 30.27  ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.632 -5.715  22.079 1.00 29.45  ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.976  -4.657  21.184 1.00 26.90  ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.548  -4.899  21.016 1.00 26.71  ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.140  -4.998  19.537 1.00 26.10  ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.478  -4.130  18.761 1.00 25.53  ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.753  -3.721  21.634 1.00 26.76  ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.827  -3.612  23.140 1.00 28.21  ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.082  -4.461  23.956 1.00 30.41  ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.537  -2.586  23.746 1.00 28.65  ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.105  -4.332  25.348 1.00 32.02  ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.528  -2.417  25.126 1.00 30.08  ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.816  -3.292  25.927 1.00 32.83  ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.878  -3.150  27.299 1.00 34.81  ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.356  -6.001  19.163 1.00 26.15  ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.832  -6.054  17.777 1.00 26.39  ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.722  -4.972  17.635 1.00 28.62  ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.911  -4.810  18.554 1.00 30.26  ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.281  -7.498  17.660 1.00 27.94  ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.950  -7.888  19.058 1.00 28.82  ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.855  -7.113  20.002 1.00 26.86  ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.729  -4.197  16.542 1.00 26.85  ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.753  -3.124  16.349 1.00 27.68  ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.306  -3.035  14.893 1.00 26.98  ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.044  -3.455  13.975 1.00 26.54  ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.365  -1.755  16.761 1.00 30.02  ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.389  -1.582  18.277 1.00 31.99  ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.750  -1.533  16.139 1.00 29.65  ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.106  -2.453  14.695 1.00 26.18  ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.584  -2.051  13.389 1.00 25.86  ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.815  -0.526  13.398 1.00 24.70  ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.540  0.116   14.417 1.00 25.17  ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.081  -2.283  13.281 1.00 28.99  ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.810  -3.656  13.030 1.00 36.64  ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.251  0.047   12.295 1.00 22.91  ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.486  1.499   12.262 1.00 23.34  ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.958  2.139   10.983 1.00 25.15  ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.835  1.462   9.969  1.00 26.88  ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.966  1.852   12.535 1.00 23.48  ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.954  1.114   11.667 1.00 23.73  ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.404  -0.152  12.020 1.00 24.55  ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.355  1.637   10.450 1.00 24.89  ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.276  -0.853  11.184 1.00 25.75  ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.243  0.951   9.634  1.00 25.56  ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.686  -0.299  9.996  1.00 24.75  ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.563  3.430   11.051 1.00 25.03  ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.031  4.115   9.887  1.00 25.55  ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.173  4.433   8.882  1.00 25.87  ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.339  4.397   9.241  1.00 25.65  ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.341  5.411   10.340 1.00 27.12  ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.295  6.228   10.997 1.00 29.46  ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.835  4.724   7.624  1.00 26.63  ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.845  5.085   6.627  1.00 28.19  ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.431  6.489   6.975  1.00 27.92  ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.754  7.294   7.615  1.00 27.82  ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.191  5.110   5.220  1.00 31.42  ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.865  3.693   4.739  1.00 35.42  ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.316  3.647   3.327  1.00 41.00  ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.379  2.219   2.823  1.00 43.50  ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.787  2.086   1.465  1.00 45.37  ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.656  6.800   6.534  1.00 27.99  ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.250  8.133   6.862  1.00 28.35  ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.379  9.307   6.420  1.00 28.43  ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.911  9.371   5.260  1.00 29.50  ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.609  8.106   6.148  1.00 29.20  ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.946  6.604   6.049  1.00 30.27  ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.591  5.958   5.765  1.00 27.98  ? 79  PRO   A CD  1 
ATOM   581  N  N   A SER   A 1 74  ? 5.082  10.204  7.359  0.50 28.06  ? 80  SER   A N   1 
ATOM   582  N  N   B SER   A 1 74  ? 5.098  10.213  7.354  0.50 27.93  ? 80  SER   A N   1 
ATOM   583  C  CA  A SER   A 1 74  ? 4.201  11.337  7.073  0.50 28.61  ? 80  SER   A CA  1 
ATOM   584  C  CA  B SER   A 1 74  ? 4.213  11.343  7.065  0.50 28.35  ? 80  SER   A CA  1 
ATOM   585  C  C   A SER   A 1 74  ? 4.586  12.599  7.864  0.50 28.60  ? 80  SER   A C   1 
ATOM   586  C  C   B SER   A 1 74  ? 4.603  12.606  7.848  0.50 28.46  ? 80  SER   A C   1 
ATOM   587  O  O   A SER   A 1 74  ? 5.472  12.544  8.720  0.50 28.52  ? 80  SER   A O   1 
ATOM   588  O  O   B SER   A 1 74  ? 5.504  12.559  8.689  0.50 28.37  ? 80  SER   A O   1 
ATOM   589  C  CB  A SER   A 1 74  ? 2.739  10.950  7.328  0.50 29.69  ? 80  SER   A CB  1 
ATOM   590  C  CB  B SER   A 1 74  ? 2.754  10.962  7.345  0.50 29.08  ? 80  SER   A CB  1 
ATOM   591  O  OG  A SER   A 1 74  ? 2.473  10.784  8.713  0.50 31.35  ? 80  SER   A OG  1 
ATOM   592  O  OG  B SER   A 1 74  ? 2.433  9.660   6.885  0.50 30.12  ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 3.922  13.736  7.574  1.00 28.47  ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 4.168  15.004  8.260  1.00 28.78  ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 3.180  14.980  9.458  1.00 29.53  ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 1.957  14.912  9.257  1.00 29.80  ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 3.845  16.135  7.268  1.00 28.89  ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 4.178  17.540  7.693  1.00 31.09  ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.636  17.721  7.879  1.00 30.37  ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 3.567  18.584  6.701  1.00 32.31  ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.719  14.993  10.693 1.00 28.79  ? 82  ILE   A N   1 
ATOM   602  C  CA  A ILE   A 1 76  ? 2.959  14.841  11.938 0.50 29.19  ? 82  ILE   A CA  1 
ATOM   603  C  CA  B ILE   A 1 76  ? 2.921  14.872  11.906 0.50 29.18  ? 82  ILE   A CA  1 
ATOM   604  C  C   . ILE   A 1 76  ? 3.253  15.967  12.908 1.00 29.40  ? 82  ILE   A C   1 
ATOM   605  O  O   . ILE   A 1 76  ? 4.418  16.286  13.095 1.00 28.52  ? 82  ILE   A O   1 
ATOM   606  C  CB  A ILE   A 1 76  ? 3.407  13.496  12.578 0.50 30.02  ? 82  ILE   A CB  1 
ATOM   607  C  CB  B ILE   A 1 76  ? 3.156  13.454  12.495 0.50 30.03  ? 82  ILE   A CB  1 
ATOM   608  C  CG1 A ILE   A 1 76  ? 2.939  12.285  11.747 0.50 31.59  ? 82  ILE   A CG1 1 
ATOM   609  C  CG1 B ILE   A 1 76  ? 2.495  12.380  11.613 0.50 31.25  ? 82  ILE   A CG1 1 
ATOM   610  C  CG2 A ILE   A 1 76  ? 3.015  13.361  14.072 0.50 30.47  ? 82  ILE   A CG2 1 
ATOM   611  C  CG2 B ILE   A 1 76  ? 2.695  13.329  13.955 0.50 30.66  ? 82  ILE   A CG2 1 
ATOM   612  C  CD1 A ILE   A 1 76  ? 1.466  11.873  11.927 0.50 33.07  ? 82  ILE   A CD1 1 
ATOM   613  C  CD1 B ILE   A 1 76  ? 2.874  10.951  11.969 0.50 32.41  ? 82  ILE   A CD1 1 
ATOM   614  N  N   . PHE   A 1 77  ? 2.220  16.522  13.576 1.00 30.01  ? 83  PHE   A N   1 
ATOM   615  C  CA  . PHE   A 1 77  ? 2.458  17.571  14.564 1.00 31.61  ? 83  PHE   A CA  1 
ATOM   616  C  C   . PHE   A 1 77  ? 3.073  16.930  15.799 1.00 31.30  ? 83  PHE   A C   1 
ATOM   617  O  O   . PHE   A 1 77  ? 2.564  15.919  16.309 1.00 32.80  ? 83  PHE   A O   1 
ATOM   618  C  CB  . PHE   A 1 77  ? 1.160  18.327  14.954 1.00 33.23  ? 83  PHE   A CB  1 
ATOM   619  C  CG  . PHE   A 1 77  ? 1.454  19.662  15.609 1.00 35.43  ? 83  PHE   A CG  1 
ATOM   620  C  CD1 . PHE   A 1 77  ? 2.051  20.688  14.894 1.00 37.34  ? 83  PHE   A CD1 1 
ATOM   621  C  CD2 . PHE   A 1 77  ? 1.209  19.859  16.957 1.00 37.20  ? 83  PHE   A CD2 1 
ATOM   622  C  CE1 . PHE   A 1 77  ? 2.332  21.915  15.499 1.00 38.72  ? 83  PHE   A CE1 1 
ATOM   623  C  CE2 . PHE   A 1 77  ? 1.465  21.087  17.555 1.00 37.64  ? 83  PHE   A CE2 1 
ATOM   624  C  CZ  . PHE   A 1 77  ? 2.008  22.113  16.820 1.00 38.34  ? 83  PHE   A CZ  1 
ATOM   625  N  N   . VAL   A 1 78  ? 4.162  17.502  16.268 1.00 29.22  ? 84  VAL   A N   1 
ATOM   626  C  CA  . VAL   A 1 78  ? 4.902  17.005  17.429 1.00 28.99  ? 84  VAL   A CA  1 
ATOM   627  C  C   . VAL   A 1 78  ? 4.929  18.089  18.490 1.00 29.93  ? 84  VAL   A C   1 
ATOM   628  O  O   . VAL   A 1 78  ? 5.358  19.224  18.231 1.00 29.69  ? 84  VAL   A O   1 
ATOM   629  C  CB  . VAL   A 1 78  ? 6.322  16.585  17.002 1.00 28.48  ? 84  VAL   A CB  1 
ATOM   630  C  CG1 . VAL   A 1 78  ? 7.222  16.281  18.222 1.00 29.05  ? 84  VAL   A CG1 1 
ATOM   631  C  CG2 . VAL   A 1 78  ? 6.259  15.390  16.048 1.00 27.68  ? 84  VAL   A CG2 1 
ATOM   632  N  N   . GLU   A 1 79  ? 4.437  17.748  19.686 1.00 30.36  ? 85  GLU   A N   1 
ATOM   633  C  CA  . GLU   A 1 79  ? 4.392  18.698  20.784 1.00 30.92  ? 85  GLU   A CA  1 
ATOM   634  C  C   . GLU   A 1 79  ? 5.745  19.310  21.135 1.00 30.00  ? 85  GLU   A C   1 
ATOM   635  O  O   . GLU   A 1 79  ? 6.786  18.737  20.826 1.00 28.70  ? 85  GLU   A O   1 
ATOM   636  C  CB  . GLU   A 1 79  ? 3.772  18.028  22.020 1.00 34.03  ? 85  GLU   A CB  1 
ATOM   637  C  CG  . GLU   A 1 79  ? 2.307  17.717  21.818 1.00 42.54  ? 85  GLU   A CG  1 
ATOM   638  C  CD  . GLU   A 1 79  ? 1.517  18.988  21.573 1.00 51.68  ? 85  GLU   A CD  1 
ATOM   639  O  OE1 . GLU   A 1 79  ? 1.447  19.824  22.504 1.00 53.19  ? 85  GLU   A OE1 1 
ATOM   640  O  OE2 . GLU   A 1 79  ? 1.033  19.184  20.432 1.00 54.37  ? 85  GLU   A OE2 1 
ATOM   641  N  N   . ALA   A 1 80  ? 5.726  20.489  21.775 1.00 30.26  ? 86  ALA   A N   1 
ATOM   642  C  CA  . ALA   A 1 80  ? 6.954  21.127  22.222 1.00 31.29  ? 86  ALA   A CA  1 
ATOM   643  C  C   . ALA   A 1 80  ? 7.664  20.250  23.258 1.00 31.19  ? 86  ALA   A C   1 
ATOM   644  O  O   . ALA   A 1 80  ? 7.022  19.502  24.025 1.00 30.67  ? 86  ALA   A O   1 
ATOM   645  C  CB  . ALA   A 1 80  ? 6.653  22.507  22.826 1.00 31.51  ? 86  ALA   A CB  1 
ATOM   646  N  N   . SER   A 1 81  ? 8.993  20.311  23.235 1.00 30.23  ? 87  SER   A N   1 
ATOM   647  C  CA  . SER   A 1 81  ? 9.853  19.621  24.196 1.00 30.95  ? 87  SER   A CA  1 
ATOM   648  C  C   . SER   A 1 81  ? 11.019 20.547  24.559 1.00 32.59  ? 87  SER   A C   1 
ATOM   649  O  O   . SER   A 1 81  ? 11.076 21.685  24.058 1.00 32.43  ? 87  SER   A O   1 
ATOM   650  C  CB  . SER   A 1 81  ? 10.393 18.319  23.584 1.00 31.07  ? 87  SER   A CB  1 
ATOM   651  O  OG  . SER   A 1 81  ? 11.354 18.606  22.574 1.00 31.52  ? 87  SER   A OG  1 
ATOM   652  N  N   . GLU   A 1 82  ? 11.993 20.061  25.372 1.00 33.95  ? 88  GLU   A N   1 
ATOM   653  C  CA  . GLU   A 1 82  ? 13.148 20.911  25.674 1.00 35.61  ? 88  GLU   A CA  1 
ATOM   654  C  C   . GLU   A 1 82  ? 14.053 21.107  24.423 1.00 35.35  ? 88  GLU   A C   1 
ATOM   655  O  O   . GLU   A 1 82  ? 14.832 22.049  24.392 1.00 35.70  ? 88  GLU   A O   1 
ATOM   656  C  CB  . GLU   A 1 82  ? 13.938 20.423  26.909 1.00 39.10  ? 88  GLU   A CB  1 
ATOM   657  C  CG  . GLU   A 1 82  ? 14.608 19.079  26.706 1.00 46.08  ? 88  GLU   A CG  1 
ATOM   658  C  CD  . GLU   A 1 82  ? 15.756 18.738  27.648 1.00 54.24  ? 88  GLU   A CD  1 
ATOM   659  O  OE1 . GLU   A 1 82  ? 16.678 19.575  27.801 1.00 55.70  ? 88  GLU   A OE1 1 
ATOM   660  O  OE2 . GLU   A 1 82  ? 15.746 17.619  28.213 1.00 55.68  ? 88  GLU   A OE2 1 
ATOM   661  N  N   . TYR   A 1 83  ? 13.886 20.285  23.362 1.00 34.29  ? 89  TYR   A N   1 
ATOM   662  C  CA  . TYR   A 1 83  ? 14.724 20.343  22.155 1.00 33.85  ? 89  TYR   A CA  1 
ATOM   663  C  C   . TYR   A 1 83  ? 14.132 21.080  20.958 1.00 32.69  ? 89  TYR   A C   1 
ATOM   664  O  O   . TYR   A 1 83  ? 14.888 21.572  20.130 1.00 32.92  ? 89  TYR   A O   1 
ATOM   665  C  CB  . TYR   A 1 83  ? 15.099 18.920  21.750 1.00 34.19  ? 89  TYR   A CB  1 
ATOM   666  C  CG  . TYR   A 1 83  ? 15.994 18.284  22.787 1.00 36.14  ? 89  TYR   A CG  1 
ATOM   667  C  CD1 . TYR   A 1 83  ? 17.321 18.683  22.929 1.00 37.66  ? 89  TYR   A CD1 1 
ATOM   668  C  CD2 . TYR   A 1 83  ? 15.493 17.358  23.695 1.00 37.68  ? 89  TYR   A CD2 1 
ATOM   669  C  CE1 . TYR   A 1 83  ? 18.145 18.118  23.892 1.00 39.63  ? 89  TYR   A CE1 1 
ATOM   670  C  CE2 . TYR   A 1 83  ? 16.308 16.792  24.671 1.00 39.44  ? 89  TYR   A CE2 1 
ATOM   671  C  CZ  . TYR   A 1 83  ? 17.633 17.178  24.768 1.00 41.58  ? 89  TYR   A CZ  1 
ATOM   672  O  OH  . TYR   A 1 83  ? 18.456 16.606  25.711 1.00 45.46  ? 89  TYR   A OH  1 
ATOM   673  N  N   . TYR   A 1 84  ? 12.806 21.128  20.841 1.00 31.62  ? 90  TYR   A N   1 
ATOM   674  C  CA  . TYR   A 1 84  ? 12.166 21.850  19.738 1.00 31.17  ? 90  TYR   A CA  1 
ATOM   675  C  C   . TYR   A 1 84  ? 10.889 22.510  20.223 1.00 33.02  ? 90  TYR   A C   1 
ATOM   676  O  O   . TYR   A 1 84  ? 10.168 21.942  21.058 1.00 33.41  ? 90  TYR   A O   1 
ATOM   677  C  CB  . TYR   A 1 84  ? 11.757 20.893  18.591 1.00 29.75  ? 90  TYR   A CB  1 
ATOM   678  C  CG  . TYR   A 1 84  ? 12.858 20.080  17.945 1.00 27.92  ? 90  TYR   A CG  1 
ATOM   679  C  CD1 . TYR   A 1 84  ? 13.621 20.602  16.906 1.00 27.81  ? 90  TYR   A CD1 1 
ATOM   680  C  CD2 . TYR   A 1 84  ? 13.087 18.762  18.321 1.00 28.39  ? 90  TYR   A CD2 1 
ATOM   681  C  CE1 . TYR   A 1 84  ? 14.600 19.844  16.278 1.00 27.13  ? 90  TYR   A CE1 1 
ATOM   682  C  CE2 . TYR   A 1 84  ? 14.075 18.001  17.718 1.00 27.92  ? 90  TYR   A CE2 1 
ATOM   683  C  CZ  . TYR   A 1 84  ? 14.796 18.526  16.660 1.00 27.80  ? 90  TYR   A CZ  1 
ATOM   684  O  OH  . TYR   A 1 84  ? 15.773 17.757  16.061 1.00 27.77  ? 90  TYR   A OH  1 
ATOM   685  N  N   . PRO   A 1 85  ? 10.490 23.630  19.600 1.00 33.16  ? 91  PRO   A N   1 
ATOM   686  C  CA  . PRO   A 1 85  ? 9.134  24.138  19.853 1.00 32.93  ? 91  PRO   A CA  1 
ATOM   687  C  C   . PRO   A 1 85  ? 8.119  23.207  19.148 1.00 32.20  ? 91  PRO   A C   1 
ATOM   688  O  O   . PRO   A 1 85  ? 8.515  22.316  18.349 1.00 31.46  ? 91  PRO   A O   1 
ATOM   689  C  CB  . PRO   A 1 85  ? 9.145  25.542  19.218 1.00 33.82  ? 91  PRO   A CB  1 
ATOM   690  C  CG  . PRO   A 1 85  ? 10.145 25.455  18.115 1.00 34.90  ? 91  PRO   A CG  1 
ATOM   691  C  CD  . PRO   A 1 85  ? 11.185 24.394  18.540 1.00 33.48  ? 91  PRO   A CD  1 
ATOM   692  N  N   . ALA   A 1 86  ? 6.800  23.405  19.422 1.00 32.17  ? 92  ALA   A N   1 
ATOM   693  C  CA  . ALA   A 1 86  ? 5.725  22.614  18.784 1.00 32.89  ? 92  ALA   A CA  1 
ATOM   694  C  C   . ALA   A 1 86  ? 5.828  22.824  17.266 1.00 32.17  ? 92  ALA   A C   1 
ATOM   695  O  O   . ALA   A 1 86  ? 6.077  23.959  16.825 1.00 32.06  ? 92  ALA   A O   1 
ATOM   696  C  CB  . ALA   A 1 86  ? 4.364  23.051  19.299 1.00 34.59  ? 92  ALA   A CB  1 
ATOM   697  N  N   . ARG   A 1 87  ? 5.885  21.724  16.495 1.00 30.75  ? 93  ARG   A N   1 
ATOM   698  C  CA  . ARG   A 1 87  ? 6.129  21.852  15.050 1.00 30.28  ? 93  ARG   A CA  1 
ATOM   699  C  C   . ARG   A 1 87  ? 5.681  20.601  14.284 1.00 31.13  ? 93  ARG   A C   1 
ATOM   700  O  O   . ARG   A 1 87  ? 5.389  19.598  14.921 1.00 32.00  ? 93  ARG   A O   1 
ATOM   701  C  CB  . ARG   A 1 87  ? 7.647  22.097  14.803 1.00 30.65  ? 93  ARG   A CB  1 
ATOM   702  C  CG  . ARG   A 1 87  ? 8.490  20.801  14.720 1.00 32.35  ? 93  ARG   A CG  1 
ATOM   703  C  CD  . ARG   A 1 87  ? 9.896  20.934  15.232 1.00 33.09  ? 93  ARG   A CD  1 
ATOM   704  N  NE  . ARG   A 1 87  ? 10.793 19.883  14.740 1.00 32.41  ? 93  ARG   A NE  1 
ATOM   705  C  CZ  . ARG   A 1 87  ? 10.841 18.646  15.235 1.00 32.17  ? 93  ARG   A CZ  1 
ATOM   706  N  NH1 . ARG   A 1 87  ? 9.998  18.274  16.205 1.00 29.03  ? 93  ARG   A NH1 1 
ATOM   707  N  NH2 . ARG   A 1 87  ? 11.736 17.771  14.772 1.00 28.47  ? 93  ARG   A NH2 1 
ATOM   708  N  N   . TYR   A 1 88  ? 5.682  20.637  12.925 1.00 30.09  ? 94  TYR   A N   1 
ATOM   709  C  CA  . TYR   A 1 88  ? 5.394  19.415  12.173 1.00 30.07  ? 94  TYR   A CA  1 
ATOM   710  C  C   . TYR   A 1 88  ? 6.720  18.759  11.864 1.00 28.72  ? 94  TYR   A C   1 
ATOM   711  O  O   . TYR   A 1 88  ? 7.649  19.422  11.375 1.00 28.80  ? 94  TYR   A O   1 
ATOM   712  C  CB  . TYR   A 1 88  ? 4.662  19.705  10.856 1.00 31.67  ? 94  TYR   A CB  1 
ATOM   713  C  CG  . TYR   A 1 88  ? 3.224  20.100  11.083 1.00 33.79  ? 94  TYR   A CG  1 
ATOM   714  C  CD1 . TYR   A 1 88  ? 2.226  19.139  11.173 1.00 34.69  ? 94  TYR   A CD1 1 
ATOM   715  C  CD2 . TYR   A 1 88  ? 2.869  21.430  11.268 1.00 35.61  ? 94  TYR   A CD2 1 
ATOM   716  C  CE1 . TYR   A 1 88  ? 0.901  19.491  11.396 1.00 35.55  ? 94  TYR   A CE1 1 
ATOM   717  C  CE2 . TYR   A 1 88  ? 1.543  21.798  11.492 1.00 36.34  ? 94  TYR   A CE2 1 
ATOM   718  C  CZ  . TYR   A 1 88  ? 0.561  20.822  11.549 1.00 37.28  ? 94  TYR   A CZ  1 
ATOM   719  O  OH  . TYR   A 1 88  ? -0.754 21.147  11.779 1.00 38.63  ? 94  TYR   A OH  1 
ATOM   720  N  N   . GLN   A 1 89  ? 6.826  17.465  12.147 1.00 26.73  ? 95  GLN   A N   1 
ATOM   721  C  CA  . GLN   A 1 89  ? 8.050  16.720  11.807 1.00 26.49  ? 95  GLN   A CA  1 
ATOM   722  C  C   . GLN   A 1 89  ? 7.697  15.829  10.604 1.00 26.77  ? 95  GLN   A C   1 
ATOM   723  O  O   . GLN   A 1 89  ? 6.655  15.140  10.633 1.00 27.40  ? 95  GLN   A O   1 
ATOM   724  C  CB  . GLN   A 1 89  ? 8.520  15.861  13.007 1.00 26.93  ? 95  GLN   A CB  1 
ATOM   725  C  CG  . GLN   A 1 89  ? 9.701  14.911  12.680 1.00 26.60  ? 95  GLN   A CG  1 
ATOM   726  C  CD  . GLN   A 1 89  ? 10.403 14.392  13.928 1.00 26.03  ? 95  GLN   A CD  1 
ATOM   727  O  OE1 . GLN   A 1 89  ? 10.555 15.093  14.938 1.00 25.91  ? 95  GLN   A OE1 1 
ATOM   728  N  NE2 . GLN   A 1 89  ? 10.876 13.175  13.881 1.00 26.10  ? 95  GLN   A NE2 1 
ATOM   729  N  N   . SER   A 1 90  ? 8.526  15.854  9.558  1.00 25.69  ? 96  SER   A N   1 
ATOM   730  C  CA  . SER   A 1 90  ? 8.282  15.063  8.357  1.00 25.39  ? 96  SER   A CA  1 
ATOM   731  C  C   . SER   A 1 90  ? 8.951  13.669  8.449  1.00 25.12  ? 96  SER   A C   1 
ATOM   732  O  O   . SER   A 1 90  ? 9.820  13.438  9.323  1.00 24.37  ? 96  SER   A O   1 
ATOM   733  C  CB  . SER   A 1 90  ? 8.814  15.809  7.129  1.00 26.93  ? 96  SER   A CB  1 
ATOM   734  O  OG  . SER   A 1 90  ? 10.217 15.973  7.258  1.00 27.68  ? 96  SER   A OG  1 
ATOM   735  N  N   . HIS   A 1 91  ? 8.518  12.744  7.556  1.00 24.91  ? 97  HIS   A N   1 
ATOM   736  C  CA  . HIS   A 1 91  ? 9.042  11.367  7.440  1.00 25.16  ? 97  HIS   A CA  1 
ATOM   737  C  C   . HIS   A 1 91  ? 8.917  10.618  8.788  1.00 25.21  ? 97  HIS   A C   1 
ATOM   738  O  O   . HIS   A 1 91  ? 9.793  9.831   9.145  1.00 24.44  ? 97  HIS   A O   1 
ATOM   739  C  CB  . HIS   A 1 91  ? 10.510 11.398  6.949  1.00 25.61  ? 97  HIS   A CB  1 
ATOM   740  C  CG  . HIS   A 1 91  ? 10.677 12.056  5.604  1.00 29.95  ? 97  HIS   A CG  1 
ATOM   741  N  ND1 . HIS   A 1 91  ? 10.748 11.308  4.436  1.00 32.36  ? 97  HIS   A ND1 1 
ATOM   742  C  CD2 . HIS   A 1 91  ? 10.753 13.372  5.281  1.00 30.35  ? 97  HIS   A CD2 1 
ATOM   743  C  CE1 . HIS   A 1 91  ? 10.881 12.187  3.445  1.00 32.19  ? 97  HIS   A CE1 1 
ATOM   744  N  NE2 . HIS   A 1 91  ? 10.883 13.441  3.898  1.00 30.42  ? 97  HIS   A NE2 1 
ATOM   745  N  N   . LEU   A 1 92  ? 7.832  10.892  9.534  1.00 25.14  ? 98  LEU   A N   1 
ATOM   746  C  CA  . LEU   A 1 92  ? 7.636  10.281  10.845 1.00 26.24  ? 98  LEU   A CA  1 
ATOM   747  C  C   . LEU   A 1 92  ? 6.578  9.164   10.753 1.00 25.55  ? 98  LEU   A C   1 
ATOM   748  O  O   . LEU   A 1 92  ? 5.535  9.336   10.101 1.00 25.68  ? 98  LEU   A O   1 
ATOM   749  C  CB  . LEU   A 1 92  ? 7.177  11.360  11.843 1.00 27.33  ? 98  LEU   A CB  1 
ATOM   750  C  CG  . LEU   A 1 92  ? 7.045  10.931  13.320 1.00 28.87  ? 98  LEU   A CG  1 
ATOM   751  C  CD1 . LEU   A 1 92  ? 8.408  10.560  13.891 1.00 28.70  ? 98  LEU   A CD1 1 
ATOM   752  C  CD2 . LEU   A 1 92  ? 6.435  12.096  14.168 1.00 30.69  ? 98  LEU   A CD2 1 
ATOM   753  N  N   . MET   A 1 93  ? 6.847  8.038   11.410 1.00 24.45  ? 99  MET   A N   1 
ATOM   754  C  CA  . MET   A 1 93  ? 5.931  6.889   11.433 1.00 23.81  ? 99  MET   A CA  1 
ATOM   755  C  C   . MET   A 1 93  ? 5.512  6.672   12.887 1.00 24.77  ? 99  MET   A C   1 
ATOM   756  O  O   . MET   A 1 93  ? 6.371  6.704   13.759 1.00 25.60  ? 99  MET   A O   1 
ATOM   757  C  CB  . MET   A 1 93  ? 6.692  5.625   10.940 1.00 23.59  ? 99  MET   A CB  1 
ATOM   758  C  CG  . MET   A 1 93  ? 7.316  5.838   9.545  1.00 25.85  ? 99  MET   A CG  1 
ATOM   759  S  SD  . MET   A 1 93  ? 8.359  4.465   9.043  1.00 29.76  ? 99  MET   A SD  1 
ATOM   760  C  CE  . MET   A 1 93  ? 9.798  4.674   10.233 1.00 26.43  ? 99  MET   A CE  1 
ATOM   761  N  N   . LEU   A 1 94  ? 4.236  6.454   13.164 1.00 24.81  ? 100 LEU   A N   1 
ATOM   762  C  CA  . LEU   A 1 94  ? 3.769  6.239   14.528 1.00 25.37  ? 100 LEU   A CA  1 
ATOM   763  C  C   . LEU   A 1 94  ? 3.322  4.797   14.755 1.00 25.46  ? 100 LEU   A C   1 
ATOM   764  O  O   . LEU   A 1 94  ? 2.779  4.159   13.855 1.00 25.53  ? 100 LEU   A O   1 
ATOM   765  C  CB  . LEU   A 1 94  ? 2.551  7.156   14.848 1.00 26.51  ? 100 LEU   A CB  1 
ATOM   766  C  CG  . LEU   A 1 94  ? 2.811  8.668   14.847 1.00 29.85  ? 100 LEU   A CG  1 
ATOM   767  C  CD1 . LEU   A 1 94  ? 1.526  9.450   15.275 1.00 31.35  ? 100 LEU   A CD1 1 
ATOM   768  C  CD2 . LEU   A 1 94  ? 3.953  9.024   15.765 1.00 31.42  ? 100 LEU   A CD2 1 
ATOM   769  N  N   . ALA   A 1 95  ? 3.433  4.362   15.994 1.00 24.77  ? 101 ALA   A N   1 
ATOM   770  C  CA  . ALA   A 1 95  ? 2.975  3.048   16.460 1.00 25.04  ? 101 ALA   A CA  1 
ATOM   771  C  C   . ALA   A 1 95  ? 2.418  3.220   17.889 1.00 25.16  ? 101 ALA   A C   1 
ATOM   772  O  O   . ALA   A 1 95  ? 2.739  4.192   18.586 1.00 25.40  ? 101 ALA   A O   1 
ATOM   773  C  CB  . ALA   A 1 95  ? 4.146  2.058   16.493 1.00 24.71  ? 101 ALA   A CB  1 
ATOM   774  N  N   . VAL   A 1 96  ? 1.577  2.277   18.303 1.00 24.79  ? 102 VAL   A N   1 
ATOM   775  C  CA  . VAL   A 1 96  ? 1.088  2.228   19.658 1.00 24.67  ? 102 VAL   A CA  1 
ATOM   776  C  C   . VAL   A 1 96  ? 2.169  1.454   20.412 1.00 26.13  ? 102 VAL   A C   1 
ATOM   777  O  O   . VAL   A 1 96  ? 2.426  0.256   20.131 1.00 26.29  ? 102 VAL   A O   1 
ATOM   778  C  CB  . VAL   A 1 96  ? -0.299 1.526   19.740 1.00 25.70  ? 102 VAL   A CB  1 
ATOM   779  C  CG1 . VAL   A 1 96  ? -0.715 1.308   21.190 1.00 27.40  ? 102 VAL   A CG1 1 
ATOM   780  C  CG2 . VAL   A 1 96  ? -1.356 2.342   19.007 1.00 25.92  ? 102 VAL   A CG2 1 
ATOM   781  N  N   . GLY   A 1 97  ? 2.783  2.107   21.370 1.00 26.34  ? 103 GLY   A N   1 
ATOM   782  C  CA  . GLY   A 1 97  ? 3.836  1.459   22.152 1.00 27.91  ? 103 GLY   A CA  1 
ATOM   783  C  C   . GLY   A 1 97  ? 4.436  2.397   23.171 1.00 28.39  ? 103 GLY   A C   1 
ATOM   784  O  O   . GLY   A 1 97  ? 4.226  3.619   23.101 1.00 28.42  ? 103 GLY   A O   1 
ATOM   785  N  N   . HIS   A 1 98  ? 5.182  1.819   24.131 1.00 27.69  ? 104 HIS   A N   1 
ATOM   786  C  CA  . HIS   A 1 98  ? 5.759  2.638   25.180 1.00 27.57  ? 104 HIS   A CA  1 
ATOM   787  C  C   . HIS   A 1 98  ? 7.012  3.367   24.725 1.00 26.07  ? 104 HIS   A C   1 
ATOM   788  O  O   . HIS   A 1 98  ? 7.826  2.822   24.002 1.00 26.04  ? 104 HIS   A O   1 
ATOM   789  C  CB  . HIS   A 1 98  ? 6.096  1.799   26.417 1.00 28.61  ? 104 HIS   A CB  1 
ATOM   790  C  CG  . HIS   A 1 98  ? 6.646  2.611   27.551 1.00 31.06  ? 104 HIS   A CG  1 
ATOM   791  N  ND1 . HIS   A 1 98  ? 5.870  3.559   28.218 1.00 33.26  ? 104 HIS   A ND1 1 
ATOM   792  C  CD2 . HIS   A 1 98  ? 7.902  2.646   28.050 1.00 32.10  ? 104 HIS   A CD2 1 
ATOM   793  C  CE1 . HIS   A 1 98  ? 6.677  4.119   29.109 1.00 33.68  ? 104 HIS   A CE1 1 
ATOM   794  N  NE2 . HIS   A 1 98  ? 7.913  3.597   29.042 1.00 33.25  ? 104 HIS   A NE2 1 
ATOM   795  N  N   . SER   A 1 99  ? 7.161  4.614   25.189 1.00 25.57  ? 105 SER   A N   1 
ATOM   796  C  CA  . SER   A 1 99  ? 8.378  5.363   24.947 1.00 26.07  ? 105 SER   A CA  1 
ATOM   797  C  C   . SER   A 1 99  ? 8.489  6.519   25.938 1.00 27.36  ? 105 SER   A C   1 
ATOM   798  O  O   . SER   A 1 99  ? 7.488  7.057   26.383 1.00 27.48  ? 105 SER   A O   1 
ATOM   799  C  CB  . SER   A 1 99  ? 8.464  5.860   23.510 1.00 27.67  ? 105 SER   A CB  1 
ATOM   800  O  OG  . SER   A 1 99  ? 7.557  6.914   23.240 1.00 29.11  ? 105 SER   A OG  1 
ATOM   801  N  N   . GLU   A 1 100 ? 9.727  6.810   26.357 1.00 27.77  ? 106 GLU   A N   1 
ATOM   802  C  CA  . GLU   A 1 100 ? 10.095 7.921   27.221 1.00 28.41  ? 106 GLU   A CA  1 
ATOM   803  C  C   . GLU   A 1 100 ? 11.158 8.751   26.487 1.00 28.96  ? 106 GLU   A C   1 
ATOM   804  O  O   . GLU   A 1 100 ? 11.788 8.238   25.557 1.00 28.92  ? 106 GLU   A O   1 
ATOM   805  C  CB  . GLU   A 1 100 ? 10.587 7.379   28.573 1.00 30.48  ? 106 GLU   A CB  1 
ATOM   806  C  CG  . GLU   A 1 100 ? 9.456  6.642   29.262 1.00 33.88  ? 106 GLU   A CG  1 
ATOM   807  C  CD  . GLU   A 1 100 ? 9.815  5.964   30.565 1.00 38.09  ? 106 GLU   A CD  1 
ATOM   808  O  OE1 . GLU   A 1 100 ? 10.567 6.579   31.351 1.00 38.51  ? 106 GLU   A OE1 1 
ATOM   809  O  OE2 . GLU   A 1 100 ? 9.337  4.833   30.808 1.00 38.08  ? 106 GLU   A OE2 1 
ATOM   810  N  N   . PRO   A 1 101 ? 11.360 10.042  26.829 1.00 29.47  ? 107 PRO   A N   1 
ATOM   811  C  CA  . PRO   A 1 101 ? 12.330 10.852  26.068 1.00 29.54  ? 107 PRO   A CA  1 
ATOM   812  C  C   . PRO   A 1 101 ? 13.702 10.185  25.760 1.00 29.29  ? 107 PRO   A C   1 
ATOM   813  O  O   . PRO   A 1 101 ? 14.172 10.235  24.614 1.00 29.18  ? 107 PRO   A O   1 
ATOM   814  C  CB  . PRO   A 1 101 ? 12.469 12.105  26.921 1.00 30.10  ? 107 PRO   A CB  1 
ATOM   815  C  CG  . PRO   A 1 101 ? 11.118 12.281  27.544 1.00 30.68  ? 107 PRO   A CG  1 
ATOM   816  C  CD  . PRO   A 1 101 ? 10.690 10.837  27.874 1.00 28.73  ? 107 PRO   A CD  1 
ATOM   817  N  N   . GLY   A 1 102 ? 14.302 9.528   26.757 1.00 29.34  ? 108 GLY   A N   1 
ATOM   818  C  CA  . GLY   A 1 102 ? 15.590 8.842   26.612 1.00 29.36  ? 108 GLY   A CA  1 
ATOM   819  C  C   . GLY   A 1 102 ? 15.562 7.595   25.732 1.00 29.18  ? 108 GLY   A C   1 
ATOM   820  O  O   . GLY   A 1 102 ? 16.606 6.985   25.483 1.00 29.39  ? 108 GLY   A O   1 
ATOM   821  N  N   . ASP   A 1 103 ? 14.371 7.191   25.231 1.00 27.47  ? 109 ASP   A N   1 
ATOM   822  C  CA  . ASP   A 1 103 ? 14.285 6.077   24.281 1.00 26.75  ? 109 ASP   A CA  1 
ATOM   823  C  C   . ASP   A 1 103 ? 14.682 6.483   22.867 1.00 25.36  ? 109 ASP   A C   1 
ATOM   824  O  O   . ASP   A 1 103 ? 14.882 5.602   22.042 1.00 25.09  ? 109 ASP   A O   1 
ATOM   825  C  CB  . ASP   A 1 103 ? 12.896 5.415   24.242 1.00 26.69  ? 109 ASP   A CB  1 
ATOM   826  C  CG  . ASP   A 1 103 ? 12.631 4.658   25.529 1.00 29.55  ? 109 ASP   A CG  1 
ATOM   827  O  OD1 . ASP   A 1 103 ? 13.590 4.088   26.080 1.00 29.05  ? 109 ASP   A OD1 1 
ATOM   828  O  OD2 . ASP   A 1 103 ? 11.455 4.638   25.977 1.00 28.57  ? 109 ASP   A OD2 1 
ATOM   829  N  N   . CYS   A 1 104 ? 14.796 7.805   22.563 1.00 25.41  ? 110 CYS   A N   1 
ATOM   830  C  CA  . CYS   A 1 104 ? 15.201 8.257   21.220 1.00 25.68  ? 110 CYS   A CA  1 
ATOM   831  C  C   . CYS   A 1 104 ? 16.536 7.605   20.831 1.00 26.06  ? 110 CYS   A C   1 
ATOM   832  O  O   . CYS   A 1 104 ? 17.437 7.483   21.680 1.00 26.96  ? 110 CYS   A O   1 
ATOM   833  C  CB  . CYS   A 1 104 ? 15.302 9.779   21.172 1.00 26.21  ? 110 CYS   A CB  1 
ATOM   834  S  SG  . CYS   A 1 104 ? 13.699 10.624  21.281 1.00 28.74  ? 110 CYS   A SG  1 
ATOM   835  N  N   . GLY   A 1 105 ? 16.630 7.153   19.601 1.00 25.03  ? 111 GLY   A N   1 
ATOM   836  C  CA  . GLY   A 1 105 ? 17.826 6.473   19.121 1.00 25.64  ? 111 GLY   A CA  1 
ATOM   837  C  C   . GLY   A 1 105 ? 17.647 4.966   19.020 1.00 26.11  ? 111 GLY   A C   1 
ATOM   838  O  O   . GLY   A 1 105 ? 18.417 4.303   18.313 1.00 26.63  ? 111 GLY   A O   1 
ATOM   839  N  N   . GLY   A 1 106 ? 16.645 4.394   19.723 1.00 25.26  ? 112 GLY   A N   1 
ATOM   840  C  CA  . GLY   A 1 106 ? 16.414 2.950   19.653 1.00 24.67  ? 112 GLY   A CA  1 
ATOM   841  C  C   . GLY   A 1 106 ? 16.031 2.544   18.238 1.00 24.66  ? 112 GLY   A C   1 
ATOM   842  O  O   . GLY   A 1 106 ? 15.315 3.282   17.562 1.00 24.29  ? 112 GLY   A O   1 
ATOM   843  N  N   . ILE   A 1 107 ? 16.590 1.442   17.741 1.00 24.15  ? 113 ILE   A N   1 
ATOM   844  C  CA  . ILE   A 1 107 ? 16.329 1.066   16.351 1.00 24.88  ? 113 ILE   A CA  1 
ATOM   845  C  C   . ILE   A 1 107 ? 14.960 0.391   16.141 1.00 24.22  ? 113 ILE   A C   1 
ATOM   846  O  O   . ILE   A 1 107 ? 14.567 -0.459  16.931 1.00 24.74  ? 113 ILE   A O   1 
ATOM   847  C  CB  . ILE   A 1 107 ? 17.521 0.175   15.824 1.00 27.50  ? 113 ILE   A CB  1 
ATOM   848  C  CG1 . ILE   A 1 107 ? 18.701 1.107   15.393 1.00 29.85  ? 113 ILE   A CG1 1 
ATOM   849  C  CG2 . ILE   A 1 107 ? 17.104 -0.719  14.645 1.00 28.25  ? 113 ILE   A CG2 1 
ATOM   850  C  CD1 . ILE   A 1 107 ? 19.967 0.388   15.103 1.00 32.94  ? 113 ILE   A CD1 1 
ATOM   851  N  N   . LEU   A 1 108 ? 14.337 0.665   14.983 1.00 23.32  ? 114 LEU   A N   1 
ATOM   852  C  CA  . LEU   A 1 108 ? 13.151 -0.031  14.480 1.00 23.05  ? 114 LEU   A CA  1 
ATOM   853  C  C   . LEU   A 1 108 ? 13.630 -0.866  13.287 1.00 23.64  ? 114 LEU   A C   1 
ATOM   854  O  O   . LEU   A 1 108 ? 14.262 -0.326  12.364 1.00 22.68  ? 114 LEU   A O   1 
ATOM   855  C  CB  . LEU   A 1 108 ? 12.081 0.965   14.005 1.00 23.68  ? 114 LEU   A CB  1 
ATOM   856  C  CG  . LEU   A 1 108 ? 10.894 0.339   13.244 1.00 25.02  ? 114 LEU   A CG  1 
ATOM   857  C  CD1 . LEU   A 1 108 ? 10.052 -0.556  14.190 1.00 25.13  ? 114 LEU   A CD1 1 
ATOM   858  C  CD2 . LEU   A 1 108 ? 10.035 1.454   12.600 1.00 26.85  ? 114 LEU   A CD2 1 
ATOM   859  N  N   . ARG   A 1 109 ? 13.362 -2.166  13.325 1.00 23.95  ? 115 ARG   A N   1 
ATOM   860  C  CA  . ARG   A 1 109 ? 13.810 -3.042  12.250 1.00 25.49  ? 115 ARG   A CA  1 
ATOM   861  C  C   . ARG   A 1 109 ? 12.731 -3.940  11.694 1.00 25.63  ? 115 ARG   A C   1 
ATOM   862  O  O   . ARG   A 1 109 ? 11.786 -4.271  12.399 1.00 23.87  ? 115 ARG   A O   1 
ATOM   863  C  CB  . ARG   A 1 109 ? 15.032 -3.846  12.656 1.00 28.50  ? 115 ARG   A CB  1 
ATOM   864  C  CG  . ARG   A 1 109 ? 14.861 -4.894  13.737 1.00 37.81  ? 115 ARG   A CG  1 
ATOM   865  C  CD  . ARG   A 1 109 ? 16.132 -5.808  13.700 1.00 44.12  ? 115 ARG   A CD  1 
ATOM   866  N  NE  . ARG   A 1 109 ? 17.359 -5.049  14.009 1.00 48.92  ? 115 ARG   A NE  1 
ATOM   867  C  CZ  . ARG   A 1 109 ? 18.354 -4.804  13.154 1.00 52.26  ? 115 ARG   A CZ  1 
ATOM   868  N  NH1 . ARG   A 1 109 ? 18.316 -5.294  11.921 1.00 52.93  ? 115 ARG   A NH1 1 
ATOM   869  N  NH2 . ARG   A 1 109 ? 19.397 -4.073  13.531 1.00 51.63  ? 115 ARG   A NH2 1 
ATOM   870  N  N   . CYS   A 1 110 ? 12.817 -4.228  10.382 1.00 25.77  ? 116 CYS   A N   1 
ATOM   871  C  CA  . CYS   A 1 110 ? 11.899 -5.164  9.735  1.00 27.28  ? 116 CYS   A CA  1 
ATOM   872  C  C   . CYS   A 1 110 ? 12.756 -6.350  9.204  1.00 29.09  ? 116 CYS   A C   1 
ATOM   873  O  O   . CYS   A 1 110 ? 13.972 -6.387  9.427  1.00 29.59  ? 116 CYS   A O   1 
ATOM   874  C  CB  . CYS   A 1 110 ? 11.156 -4.457  8.598  1.00 27.51  ? 116 CYS   A CB  1 
ATOM   875  S  SG  . CYS   A 1 110 ? 12.231 -4.002  7.209  1.00 28.90  ? 116 CYS   A SG  1 
ATOM   876  N  N   . GLN   A 1 111 ? 12.136 -7.302  8.481  1.00 30.19  ? 117 GLN   A N   1 
ATOM   877  C  CA  . GLN   A 1 111 ? 12.916 -8.408  7.889  1.00 32.26  ? 117 GLN   A CA  1 
ATOM   878  C  C   . GLN   A 1 111 ? 14.001 -7.925  6.917  1.00 33.12  ? 117 GLN   A C   1 
ATOM   879  O  O   . GLN   A 1 111 ? 14.920 -8.683  6.608  1.00 34.86  ? 117 GLN   A O   1 
ATOM   880  C  CB  . GLN   A 1 111 ? 11.984 -9.371  7.142  1.00 35.05  ? 117 GLN   A CB  1 
ATOM   881  C  CG  . GLN   A 1 111 ? 11.277 -8.727  5.954  1.00 37.59  ? 117 GLN   A CG  1 
ATOM   882  C  CD  . GLN   A 1 111 ? 10.355 -9.721  5.300  1.00 42.68  ? 117 GLN   A CD  1 
ATOM   883  O  OE1 . GLN   A 1 111 ? 9.129  -9.639  5.434  1.00 45.57  ? 117 GLN   A OE1 1 
ATOM   884  N  NE2 . GLN   A 1 111 ? 10.931 -10.689 4.606  1.00 41.12  ? 117 GLN   A NE2 1 
ATOM   885  N  N   . HIS   A 1 112 ? 13.936 -6.666  6.443  1.00 33.03  ? 118 HIS   A N   1 
ATOM   886  C  CA  . HIS   A 1 112 ? 14.919 -6.165  5.470  1.00 32.79  ? 118 HIS   A CA  1 
ATOM   887  C  C   . HIS   A 1 112 ? 16.116 -5.403  6.072  1.00 33.55  ? 118 HIS   A C   1 
ATOM   888  O  O   . HIS   A 1 112 ? 17.093 -5.117  5.366  1.00 34.75  ? 118 HIS   A O   1 
ATOM   889  C  CB  . HIS   A 1 112 ? 14.202 -5.297  4.422  1.00 32.97  ? 118 HIS   A CB  1 
ATOM   890  C  CG  . HIS   A 1 112 ? 13.099 -6.030  3.720  1.00 33.15  ? 118 HIS   A CG  1 
ATOM   891  N  ND1 . HIS   A 1 112 ? 11.771 -5.751  3.977  1.00 33.77  ? 118 HIS   A ND1 1 
ATOM   892  C  CD2 . HIS   A 1 112 ? 13.172 -7.056  2.836  1.00 34.03  ? 118 HIS   A CD2 1 
ATOM   893  C  CE1 . HIS   A 1 112 ? 11.074 -6.578  3.216  1.00 34.94  ? 118 HIS   A CE1 1 
ATOM   894  N  NE2 . HIS   A 1 112 ? 11.879 -7.398  2.521  1.00 35.70  ? 118 HIS   A NE2 1 
ATOM   895  N  N   . GLY   A 1 113 ? 16.027 -5.047  7.346  1.00 32.03  ? 119 GLY   A N   1 
ATOM   896  C  CA  . GLY   A 1 113 ? 17.085 -4.292  7.998  1.00 31.20  ? 119 GLY   A CA  1 
ATOM   897  C  C   . GLY   A 1 113 ? 16.543 -3.113  8.783  1.00 29.76  ? 119 GLY   A C   1 
ATOM   898  O  O   . GLY   A 1 113 ? 15.394 -3.122  9.224  1.00 28.73  ? 119 GLY   A O   1 
ATOM   899  N  N   . VAL   A 1 114 ? 17.378 -2.089  8.953  1.00 28.09  ? 120 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 114 ? 16.987 -0.912  9.729  1.00 27.40  ? 120 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 114 ? 15.975 -0.049  8.997  1.00 26.46  ? 120 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 114 ? 16.222 0.343   7.857  1.00 26.80  ? 120 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 114 ? 18.228 -0.091  10.133 1.00 27.88  ? 120 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 114 ? 17.810 1.203   10.829 1.00 29.12  ? 120 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 114 ? 19.141 -0.930  11.025 1.00 28.56  ? 120 VAL   A CG2 1 
ATOM   906  N  N   . VAL   A 1 115 ? 14.851 0.294   9.673  1.00 24.64  ? 121 VAL   A N   1 
ATOM   907  C  CA  . VAL   A 1 115 ? 13.805 1.136   9.074  1.00 24.50  ? 121 VAL   A CA  1 
ATOM   908  C  C   . VAL   A 1 115 ? 13.968 2.614   9.546  1.00 25.35  ? 121 VAL   A C   1 
ATOM   909  O  O   . VAL   A 1 115 ? 13.719 3.560   8.802  1.00 25.33  ? 121 VAL   A O   1 
ATOM   910  C  CB  . VAL   A 1 115 ? 12.417 0.582   9.490  1.00 25.76  ? 121 VAL   A CB  1 
ATOM   911  C  CG1 . VAL   A 1 115 ? 11.283 1.536   9.098  1.00 26.01  ? 121 VAL   A CG1 1 
ATOM   912  C  CG2 . VAL   A 1 115 ? 12.187 -0.819  8.921  1.00 24.97  ? 121 VAL   A CG2 1 
ATOM   913  N  N   . GLY   A 1 116 ? 14.305 2.784   10.819 1.00 24.19  ? 122 GLY   A N   1 
ATOM   914  C  CA  . GLY   A 1 116 ? 14.441 4.122   11.393 1.00 25.13  ? 122 GLY   A CA  1 
ATOM   915  C  C   . GLY   A 1 116 ? 14.806 4.063   12.865 1.00 24.87  ? 122 GLY   A C   1 
ATOM   916  O  O   . GLY   A 1 116 ? 15.246 3.016   13.352 1.00 25.50  ? 122 GLY   A O   1 
ATOM   917  N  N   . ILE   A 1 117 ? 14.731 5.198   13.548 1.00 23.80  ? 123 ILE   A N   1 
ATOM   918  C  CA  . ILE   A 1 117 ? 15.076 5.242   14.980 1.00 24.11  ? 123 ILE   A CA  1 
ATOM   919  C  C   . ILE   A 1 117 ? 13.979 5.968   15.749 1.00 24.43  ? 123 ILE   A C   1 
ATOM   920  O  O   . ILE   A 1 117 ? 13.343 6.855   15.182 1.00 23.95  ? 123 ILE   A O   1 
ATOM   921  C  CB  . ILE   A 1 117 ? 16.424 5.981   15.217 1.00 25.61  ? 123 ILE   A CB  1 
ATOM   922  C  CG1 . ILE   A 1 117 ? 16.402 7.364   14.562 1.00 27.16  ? 123 ILE   A CG1 1 
ATOM   923  C  CG2 . ILE   A 1 117 ? 17.632 5.135   14.758 1.00 26.81  ? 123 ILE   A CG2 1 
ATOM   924  C  CD1 . ILE   A 1 117 ? 17.723 8.238   14.919 1.00 29.63  ? 123 ILE   A CD1 1 
ATOM   925  N  N   . VAL   A 1 118 ? 13.780 5.644   17.064 1.00 23.89  ? 124 VAL   A N   1 
ATOM   926  C  CA  . VAL   A 1 118 ? 12.789 6.345   17.898 1.00 22.64  ? 124 VAL   A CA  1 
ATOM   927  C  C   . VAL   A 1 118 ? 13.142 7.853   17.906 1.00 22.83  ? 124 VAL   A C   1 
ATOM   928  O  O   . VAL   A 1 118 ? 14.316 8.228   18.065 1.00 22.90  ? 124 VAL   A O   1 
ATOM   929  C  CB  . VAL   A 1 118 ? 12.800 5.802   19.337 1.00 23.54  ? 124 VAL   A CB  1 
ATOM   930  C  CG1 . VAL   A 1 118 ? 11.861 6.597   20.239 1.00 24.12  ? 124 VAL   A CG1 1 
ATOM   931  C  CG2 . VAL   A 1 118 ? 12.454 4.310   19.366 1.00 23.77  ? 124 VAL   A CG2 1 
ATOM   932  N  N   . SER   A 1 119 ? 12.141 8.677   17.693 1.00 22.46  ? 125 SER   A N   1 
ATOM   933  C  CA  . SER   A 1 119 ? 12.310 10.132  17.615 1.00 22.82  ? 125 SER   A CA  1 
ATOM   934  C  C   . SER   A 1 119 ? 11.248 10.861  18.428 1.00 24.28  ? 125 SER   A C   1 
ATOM   935  O  O   . SER   A 1 119 ? 11.526 11.942  18.911 1.00 25.10  ? 125 SER   A O   1 
ATOM   936  C  CB  . SER   A 1 119 ? 12.257 10.590  16.157 1.00 24.21  ? 125 SER   A CB  1 
ATOM   937  O  OG  . SER   A 1 119 ? 12.468 11.996  16.026 1.00 26.58  ? 125 SER   A OG  1 
ATOM   938  N  N   . THR   A 1 120 ? 10.000 10.353  18.483 1.00 23.84  ? 126 THR   A N   1 
ATOM   939  C  CA  . THR   A 1 120 ? 8.922  11.051  19.226 1.00 25.02  ? 126 THR   A CA  1 
ATOM   940  C  C   . THR   A 1 120 ? 8.127  10.039  20.097 1.00 25.24  ? 126 THR   A C   1 
ATOM   941  O  O   . THR   A 1 120 ? 8.355  8.820   19.994 1.00 24.35  ? 126 THR   A O   1 
ATOM   942  C  CB  . THR   A 1 120 ? 7.953  11.802  18.218 1.00 26.77  ? 126 THR   A CB  1 
ATOM   943  O  OG1 . THR   A 1 120 ? 7.105  10.840  17.568 1.00 27.03  ? 126 THR   A OG1 1 
ATOM   944  C  CG2 . THR   A 1 120 ? 8.698  12.647  17.160 1.00 27.16  ? 126 THR   A CG2 1 
ATOM   945  N  N   . GLY   A 1 121 ? 7.222  10.535  20.960 1.00 25.97  ? 127 GLY   A N   1 
ATOM   946  C  CA  . GLY   A 1 121 ? 6.425  9.632   21.767 1.00 26.98  ? 127 GLY   A CA  1 
ATOM   947  C  C   . GLY   A 1 121 ? 5.630  10.311  22.843 1.00 28.84  ? 127 GLY   A C   1 
ATOM   948  O  O   . GLY   A 1 121 ? 5.580  11.534  22.926 1.00 28.24  ? 127 GLY   A O   1 
ATOM   949  N  N   . GLY   A 1 122 ? 5.061  9.496   23.693 1.00 31.79  ? 128 GLY   A N   1 
ATOM   950  C  CA  . GLY   A 1 122 ? 4.229  9.987   24.777 1.00 32.96  ? 128 GLY   A CA  1 
ATOM   951  C  C   . GLY   A 1 122 ? 2.805  9.525   24.604 1.00 33.41  ? 128 GLY   A C   1 
ATOM   952  O  O   . GLY   A 1 122 ? 2.356  9.277   23.486 1.00 32.50  ? 128 GLY   A O   1 
ATOM   953  N  N   . ASN   A 1 123 ? 2.088  9.422   25.719 1.00 34.82  ? 129 ASN   A N   1 
ATOM   954  C  CA  . ASN   A 1 123 ? 0.690  8.999   25.738 1.00 36.22  ? 129 ASN   A CA  1 
ATOM   955  C  C   . ASN   A 1 123 ? 0.406  7.701   25.000 1.00 34.80  ? 129 ASN   A C   1 
ATOM   956  O  O   . ASN   A 1 123 ? -0.586 7.581   24.272 1.00 36.04  ? 129 ASN   A O   1 
ATOM   957  C  CB  . ASN   A 1 123 ? -0.218 10.104  25.265 1.00 39.17  ? 129 ASN   A CB  1 
ATOM   958  C  CG  . ASN   A 1 123 ? -0.308 11.212  26.278 1.00 44.68  ? 129 ASN   A CG  1 
ATOM   959  O  OD1 . ASN   A 1 123 ? 0.012  11.052  27.480 1.00 47.47  ? 129 ASN   A OD1 1 
ATOM   960  N  ND2 . ASN   A 1 123 ? -0.749 12.353  25.821 1.00 45.10  ? 129 ASN   A ND2 1 
ATOM   961  N  N   . GLY   A 1 124 ? 1.256  6.727   25.230 1.00 32.26  ? 130 GLY   A N   1 
ATOM   962  C  CA  . GLY   A 1 124 ? 1.056  5.400   24.663 1.00 30.89  ? 130 GLY   A CA  1 
ATOM   963  C  C   . GLY   A 1 124 ? 1.419  5.245   23.205 1.00 29.92  ? 130 GLY   A C   1 
ATOM   964  O  O   . GLY   A 1 124 ? 1.169  4.184   22.623 1.00 29.71  ? 130 GLY   A O   1 
ATOM   965  N  N   . LEU   A 1 125 ? 2.051  6.278   22.620 1.00 28.87  ? 131 LEU   A N   1 
ATOM   966  C  CA  . LEU   A 1 125 ? 2.516  6.204   21.249 1.00 28.90  ? 131 LEU   A CA  1 
ATOM   967  C  C   . LEU   A 1 125 ? 4.058  6.274   21.226 1.00 28.74  ? 131 LEU   A C   1 
ATOM   968  O  O   . LEU   A 1 125 ? 4.709  6.690   22.205 1.00 30.11  ? 131 LEU   A O   1 
ATOM   969  C  CB  . LEU   A 1 125 ? 1.945  7.377   20.423 1.00 29.69  ? 131 LEU   A CB  1 
ATOM   970  C  CG  . LEU   A 1 125 ? 0.425  7.495   20.376 1.00 32.75  ? 131 LEU   A CG  1 
ATOM   971  C  CD1 . LEU   A 1 125 ? 0.006  8.794   19.703 1.00 35.11  ? 131 LEU   A CD1 1 
ATOM   972  C  CD2 . LEU   A 1 125 ? -0.203 6.271   19.761 1.00 32.11  ? 131 LEU   A CD2 1 
ATOM   973  N  N   . VAL   A 1 126 ? 4.629  5.861   20.096 1.00 26.01  ? 132 VAL   A N   1 
ATOM   974  C  CA  . VAL   A 1 126 ? 6.058  5.941   19.846 1.00 25.46  ? 132 VAL   A CA  1 
ATOM   975  C  C   . VAL   A 1 126 ? 6.197  6.253   18.367 1.00 25.36  ? 132 VAL   A C   1 
ATOM   976  O  O   . VAL   A 1 126 ? 5.458  5.723   17.549 1.00 25.71  ? 132 VAL   A O   1 
ATOM   977  C  CB  . VAL   A 1 126 ? 6.839  4.672   20.282 1.00 25.03  ? 132 VAL   A CB  1 
ATOM   978  C  CG1 . VAL   A 1 126 ? 6.288  3.419   19.611 1.00 24.56  ? 132 VAL   A CG1 1 
ATOM   979  C  CG2 . VAL   A 1 126 ? 8.348  4.830   19.997 1.00 25.35  ? 132 VAL   A CG2 1 
ATOM   980  N  N   . GLY   A 1 127 ? 7.022  7.238   18.061 1.00 24.24  ? 133 GLY   A N   1 
ATOM   981  C  CA  . GLY   A 1 127 ? 7.234  7.677   16.693 1.00 23.17  ? 133 GLY   A CA  1 
ATOM   982  C  C   . GLY   A 1 127 ? 8.668  7.419   16.276 1.00 22.57  ? 133 GLY   A C   1 
ATOM   983  O  O   . GLY   A 1 127 ? 9.597  7.577   17.083 1.00 23.05  ? 133 GLY   A O   1 
ATOM   984  N  N   . PHE   A 1 128 ? 8.848  7.064   15.011 1.00 21.28  ? 134 PHE   A N   1 
ATOM   985  C  CA  . PHE   A 1 128 ? 10.167 6.713   14.465 1.00 22.35  ? 134 PHE   A CA  1 
ATOM   986  C  C   . PHE   A 1 128 ? 10.504 7.594   13.260 1.00 23.47  ? 134 PHE   A C   1 
ATOM   987  O  O   . PHE   A 1 128 ? 9.684  7.740   12.343 1.00 23.72  ? 134 PHE   A O   1 
ATOM   988  C  CB  . PHE   A 1 128 ? 10.155 5.262   13.976 1.00 22.21  ? 134 PHE   A CB  1 
ATOM   989  C  CG  . PHE   A 1 128 ? 9.614  4.281   15.006 1.00 23.13  ? 134 PHE   A CG  1 
ATOM   990  C  CD1 . PHE   A 1 128 ? 10.438 3.774   16.006 1.00 24.17  ? 134 PHE   A CD1 1 
ATOM   991  C  CD2 . PHE   A 1 128 ? 8.285  3.868   14.970 1.00 24.45  ? 134 PHE   A CD2 1 
ATOM   992  C  CE1 . PHE   A 1 128 ? 9.936  2.882   16.958 1.00 24.81  ? 134 PHE   A CE1 1 
ATOM   993  C  CE2 . PHE   A 1 128 ? 7.796  2.946   15.903 1.00 24.59  ? 134 PHE   A CE2 1 
ATOM   994  C  CZ  . PHE   A 1 128 ? 8.621  2.483   16.902 1.00 24.33  ? 134 PHE   A CZ  1 
ATOM   995  N  N   . ALA   A 1 129 ? 11.739 8.089   13.217 1.00 23.60  ? 135 ALA   A N   1 
ATOM   996  C  CA  . ALA   A 1 129 ? 12.221 8.873   12.080 1.00 25.04  ? 135 ALA   A CA  1 
ATOM   997  C  C   . ALA   A 1 129 ? 12.640 7.852   10.995 1.00 24.97  ? 135 ALA   A C   1 
ATOM   998  O  O   . ALA   A 1 129 ? 13.549 7.052   11.230 1.00 25.07  ? 135 ALA   A O   1 
ATOM   999  C  CB  . ALA   A 1 129 ? 13.421 9.723   12.505 1.00 25.10  ? 135 ALA   A CB  1 
ATOM   1000 N  N   . ASP   A 1 130 ? 11.952 7.836   9.836  1.00 24.20  ? 136 ASP   A N   1 
ATOM   1001 C  CA  . ASP   A 1 130 ? 12.294 6.912   8.761  1.00 24.16  ? 136 ASP   A CA  1 
ATOM   1002 C  C   . ASP   A 1 130 ? 13.672 7.216   8.160  1.00 24.77  ? 136 ASP   A C   1 
ATOM   1003 O  O   . ASP   A 1 130 ? 14.026 8.393   8.010  1.00 25.00  ? 136 ASP   A O   1 
ATOM   1004 C  CB  . ASP   A 1 130 ? 11.263 7.050   7.617  1.00 25.95  ? 136 ASP   A CB  1 
ATOM   1005 C  CG  . ASP   A 1 130 ? 11.426 6.016   6.522  1.00 31.11  ? 136 ASP   A CG  1 
ATOM   1006 O  OD1 . ASP   A 1 130 ? 11.552 4.834   6.846  1.00 30.91  ? 136 ASP   A OD1 1 
ATOM   1007 O  OD2 . ASP   A 1 130 ? 11.429 6.395   5.339  1.00 35.30  ? 136 ASP   A OD2 1 
ATOM   1008 N  N   . VAL   A 1 131 ? 14.445 6.171   7.790  1.00 24.23  ? 137 VAL   A N   1 
ATOM   1009 C  CA  . VAL   A 1 131 ? 15.712 6.408   7.070  1.00 25.91  ? 137 VAL   A CA  1 
ATOM   1010 C  C   . VAL   A 1 131 ? 15.738 5.650   5.716  1.00 27.57  ? 137 VAL   A C   1 
ATOM   1011 O  O   . VAL   A 1 131 ? 16.710 5.761   4.981  1.00 28.82  ? 137 VAL   A O   1 
ATOM   1012 C  CB  . VAL   A 1 131 ? 16.975 6.054   7.919  1.00 26.02  ? 137 VAL   A CB  1 
ATOM   1013 C  CG1 . VAL   A 1 131 ? 16.998 6.875   9.203  1.00 26.49  ? 137 VAL   A CG1 1 
ATOM   1014 C  CG2 . VAL   A 1 131 ? 17.033 4.545   8.226  1.00 25.88  ? 137 VAL   A CG2 1 
ATOM   1015 N  N   . ARG   A 1 132 ? 14.675 4.869   5.391  1.00 27.69  ? 138 ARG   A N   1 
ATOM   1016 C  CA  . ARG   A 1 132 ? 14.618 4.051   4.179  1.00 27.58  ? 138 ARG   A CA  1 
ATOM   1017 C  C   . ARG   A 1 132 ? 14.701 4.831   2.869  1.00 29.13  ? 138 ARG   A C   1 
ATOM   1018 O  O   . ARG   A 1 132 ? 15.110 4.241   1.873  1.00 30.31  ? 138 ARG   A O   1 
ATOM   1019 C  CB  . ARG   A 1 132 ? 13.363 3.156   4.183  1.00 25.67  ? 138 ARG   A CB  1 
ATOM   1020 C  CG  . ARG   A 1 132 ? 13.371 2.175   5.318  1.00 24.32  ? 138 ARG   A CG  1 
ATOM   1021 C  CD  . ARG   A 1 132 ? 12.075 1.380   5.289  1.00 25.80  ? 138 ARG   A CD  1 
ATOM   1022 N  NE  . ARG   A 1 132 ? 10.955 2.242   5.694  1.00 25.13  ? 138 ARG   A NE  1 
ATOM   1023 C  CZ  . ARG   A 1 132 ? 9.703  1.818   5.845  1.00 27.11  ? 138 ARG   A CZ  1 
ATOM   1024 N  NH1 . ARG   A 1 132 ? 9.396  0.537   5.628  1.00 26.40  ? 138 ARG   A NH1 1 
ATOM   1025 N  NH2 . ARG   A 1 132 ? 8.757  2.658   6.265  1.00 25.52  ? 138 ARG   A NH2 1 
ATOM   1026 N  N   . ASP   A 1 133 ? 14.323 6.129   2.854  1.00 28.21  ? 139 ASP   A N   1 
ATOM   1027 C  CA  . ASP   A 1 133 ? 14.425 6.940   1.634  1.00 29.17  ? 139 ASP   A CA  1 
ATOM   1028 C  C   . ASP   A 1 133 ? 15.869 7.497   1.395  1.00 30.72  ? 139 ASP   A C   1 
ATOM   1029 O  O   . ASP   A 1 133 ? 16.143 8.052   0.319  1.00 31.87  ? 139 ASP   A O   1 
ATOM   1030 C  CB  . ASP   A 1 133 ? 13.442 8.120   1.701  1.00 30.38  ? 139 ASP   A CB  1 
ATOM   1031 C  CG  . ASP   A 1 133 ? 13.795 9.126   2.791  1.00 35.48  ? 139 ASP   A CG  1 
ATOM   1032 O  OD1 . ASP   A 1 133 ? 14.149 8.687   3.909  1.00 34.94  ? 139 ASP   A OD1 1 
ATOM   1033 O  OD2 . ASP   A 1 133 ? 13.761 10.362  2.505  1.00 36.22  ? 139 ASP   A OD2 1 
ATOM   1034 N  N   . LEU   A 1 134 ? 16.763 7.410   2.410  1.00 30.41  ? 140 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 134 ? 18.130 7.969   2.298  1.00 31.28  ? 140 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 134 ? 19.035 6.978   1.565  1.00 31.86  ? 140 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 134 ? 19.836 6.274   2.175  1.00 31.49  ? 140 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 134 ? 18.665 8.287   3.713  1.00 30.84  ? 140 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 134 ? 17.764 9.255   4.516  1.00 31.21  ? 140 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 134 ? 18.278 9.423   5.932  1.00 31.39  ? 140 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 134 ? 17.638 10.607  3.811  1.00 31.56  ? 140 LEU   A CD2 1 
ATOM   1042 N  N   . LEU   A 1 135 ? 18.820 6.864   0.254  1.00 32.15  ? 141 LEU   A N   1 
ATOM   1043 C  CA  . LEU   A 1 135 ? 19.504 5.895   -0.596 1.00 33.23  ? 141 LEU   A CA  1 
ATOM   1044 C  C   . LEU   A 1 135 ? 21.032 6.017   -0.578 1.00 33.96  ? 141 LEU   A C   1 
ATOM   1045 O  O   . LEU   A 1 135 ? 21.735 5.001   -0.698 1.00 33.64  ? 141 LEU   A O   1 
ATOM   1046 C  CB  . LEU   A 1 135 ? 18.982 6.026   -2.039 1.00 33.98  ? 141 LEU   A CB  1 
ATOM   1047 C  CG  . LEU   A 1 135 ? 17.480 5.900   -2.222 1.00 36.62  ? 141 LEU   A CG  1 
ATOM   1048 C  CD1 . LEU   A 1 135 ? 17.135 5.837   -3.697 1.00 38.87  ? 141 LEU   A CD1 1 
ATOM   1049 C  CD2 . LEU   A 1 135 ? 16.882 4.683   -1.482 1.00 36.47  ? 141 LEU   A CD2 1 
ATOM   1050 N  N   . TRP   A 1 136 ? 21.527 7.262   -0.421 1.00 34.43  ? 142 TRP   A N   1 
ATOM   1051 C  CA  . TRP   A 1 136 ? 22.956 7.578   -0.368 1.00 35.94  ? 142 TRP   A CA  1 
ATOM   1052 C  C   . TRP   A 1 136 ? 23.650 6.956   0.831  1.00 37.34  ? 142 TRP   A C   1 
ATOM   1053 O  O   . TRP   A 1 136 ? 24.849 6.751   0.762  1.00 38.32  ? 142 TRP   A O   1 
ATOM   1054 C  CB  . TRP   A 1 136 ? 23.200 9.103   -0.411 1.00 35.85  ? 142 TRP   A CB  1 
ATOM   1055 C  CG  . TRP   A 1 136 ? 22.463 9.878   0.643  1.00 35.72  ? 142 TRP   A CG  1 
ATOM   1056 C  CD1 . TRP   A 1 136 ? 21.248 10.489  0.521  1.00 36.30  ? 142 TRP   A CD1 1 
ATOM   1057 C  CD2 . TRP   A 1 136 ? 22.930 10.170  1.968  1.00 35.76  ? 142 TRP   A CD2 1 
ATOM   1058 N  NE1 . TRP   A 1 136 ? 20.931 11.144  1.687  1.00 36.49  ? 142 TRP   A NE1 1 
ATOM   1059 C  CE2 . TRP   A 1 136 ? 21.938 10.947  2.599  1.00 36.17  ? 142 TRP   A CE2 1 
ATOM   1060 C  CE3 . TRP   A 1 136 ? 24.099 9.856   2.680  1.00 36.27  ? 142 TRP   A CE3 1 
ATOM   1061 C  CZ2 . TRP   A 1 136 ? 22.070 11.398  3.909  1.00 36.57  ? 142 TRP   A CZ2 1 
ATOM   1062 C  CZ3 . TRP   A 1 136 ? 24.233 10.315  3.975  1.00 36.92  ? 142 TRP   A CZ3 1 
ATOM   1063 C  CH2 . TRP   A 1 136 ? 23.227 11.078  4.576  1.00 36.82  ? 142 TRP   A CH2 1 
ATOM   1064 N  N   . LEU   A 1 137 ? 22.924 6.596   1.912  1.00 37.63  ? 143 LEU   A N   1 
ATOM   1065 C  CA  . LEU   A 1 137 ? 23.554 5.913   3.055  1.00 38.89  ? 143 LEU   A CA  1 
ATOM   1066 C  C   . LEU   A 1 137 ? 24.289 4.619   2.627  1.00 42.28  ? 143 LEU   A C   1 
ATOM   1067 O  O   . LEU   A 1 137 ? 25.222 4.201   3.315  1.00 41.87  ? 143 LEU   A O   1 
ATOM   1068 C  CB  . LEU   A 1 137 ? 22.503 5.549   4.123  1.00 37.82  ? 143 LEU   A CB  1 
ATOM   1069 C  CG  . LEU   A 1 137 ? 21.929 6.712   4.905  1.00 37.23  ? 143 LEU   A CG  1 
ATOM   1070 C  CD1 . LEU   A 1 137 ? 20.816 6.232   5.869  1.00 36.82  ? 143 LEU   A CD1 1 
ATOM   1071 C  CD2 . LEU   A 1 137 ? 23.028 7.409   5.722  1.00 37.96  ? 143 LEU   A CD2 1 
ATOM   1072 N  N   . ASP   A 1 138 ? 23.856 4.008   1.493  1.00 44.98  ? 144 ASP   A N   1 
ATOM   1073 C  CA  . ASP   A 1 138 ? 24.377 2.763   0.909  1.00 49.16  ? 144 ASP   A CA  1 
ATOM   1074 C  C   . ASP   A 1 138 ? 25.591 2.924   0.030  1.00 52.63  ? 144 ASP   A C   1 
ATOM   1075 O  O   . ASP   A 1 138 ? 25.991 1.933   -0.581 1.00 53.13  ? 144 ASP   A O   1 
ATOM   1076 C  CB  . ASP   A 1 138 ? 23.317 2.132   -0.003 1.00 52.07  ? 144 ASP   A CB  1 
ATOM   1077 C  CG  . ASP   A 1 138 ? 22.210 1.421   0.692  1.00 59.38  ? 144 ASP   A CG  1 
ATOM   1078 O  OD1 . ASP   A 1 138 ? 22.376 1.095   1.886  1.00 61.95  ? 144 ASP   A OD1 1 
ATOM   1079 O  OD2 . ASP   A 1 138 ? 21.161 1.190   0.047  1.00 62.27  ? 144 ASP   A OD2 1 
ATOM   1080 N  N   . GLU   A 1 139 ? 26.131 4.142   -0.122 1.00 54.84  ? 145 GLU   A N   1 
ATOM   1081 C  CA  . GLU   A 1 139 ? 27.279 4.338   -1.007 1.00 57.75  ? 145 GLU   A CA  1 
ATOM   1082 C  C   . GLU   A 1 139 ? 28.250 5.378   -0.454 1.00 59.33  ? 145 GLU   A C   1 
ATOM   1083 O  O   . GLU   A 1 139 ? 28.639 5.290   0.711  1.00 60.19  ? 145 GLU   A O   1 
ATOM   1084 C  CB  . GLU   A 1 139 ? 26.793 4.743   -2.402 1.00 61.37  ? 145 GLU   A CB  1 
ATOM   1085 C  CG  . GLU   A 1 139 ? 25.975 6.019   -2.391 1.00 67.16  ? 145 GLU   A CG  1 
ATOM   1086 C  CD  . GLU   A 1 139 ? 25.024 6.152   -3.562 1.00 75.66  ? 145 GLU   A CD  1 
ATOM   1087 O  OE1 . GLU   A 1 139 ? 24.871 7.282   -4.083 1.00 77.51  ? 145 GLU   A OE1 1 
ATOM   1088 O  OE2 . GLU   A 1 139 ? 24.437 5.120   -3.963 1.00 78.30  ? 145 GLU   A OE2 1 
HETATM 1089 N  N1  . A1B36 B 2 .   ? 11.708 14.528  17.505 1.00 27.14  ? 201 A1B36 A N1  1 
HETATM 1090 C  C4  . A1B36 B 2 .   ? 7.421  11.814  25.924 1.00 41.40  ? 201 A1B36 A C4  1 
HETATM 1091 C  C5  . A1B36 B 2 .   ? 7.885  12.854  25.149 1.00 36.52  ? 201 A1B36 A C5  1 
HETATM 1092 C  C6  . A1B36 B 2 .   ? 8.767  12.591  24.105 1.00 32.64  ? 201 A1B36 A C6  1 
HETATM 1093 C  C7  . A1B36 B 2 .   ? 9.114  13.721  23.161 1.00 30.66  ? 201 A1B36 A C7  1 
HETATM 1094 C  C8  . A1B36 B 2 .   ? 10.550 14.191  23.304 1.00 29.86  ? 201 A1B36 A C8  1 
HETATM 1095 C  C10 . A1B36 B 2 .   ? 12.667 15.691  20.752 1.00 29.57  ? 201 A1B36 A C10 1 
HETATM 1096 C  C13 . A1B36 B 2 .   ? 10.584 14.522  20.824 1.00 28.66  ? 201 A1B36 A C13 1 
HETATM 1097 O  O1  . A1B36 B 2 .   ? 10.795 16.356  18.437 1.00 27.02  ? 201 A1B36 A O1  1 
HETATM 1098 C  C12 . A1B36 B 2 .   ? 11.394 15.284  18.544 1.00 27.46  ? 201 A1B36 A C12 1 
HETATM 1099 C  C11 . A1B36 B 2 .   ? 11.798 14.745  19.907 1.00 28.42  ? 201 A1B36 A C11 1 
HETATM 1100 C  C9  . A1B36 B 2 .   ? 12.548 15.091  22.146 1.00 29.33  ? 201 A1B36 A C9  1 
HETATM 1101 N  N   . A1B36 B 2 .   ? 11.172 14.570  22.168 1.00 29.03  ? 201 A1B36 A N   1 
HETATM 1102 O  O   . A1B36 B 2 .   ? 11.101 14.253  24.399 1.00 30.29  ? 201 A1B36 A O   1 
HETATM 1103 C  C1  . A1B36 B 2 .   ? 9.186  11.270  23.895 1.00 31.35  ? 201 A1B36 A C1  1 
HETATM 1104 S  S   . A1B36 B 2 .   ? 10.372 10.991  22.619 1.00 28.87  ? 201 A1B36 A S   1 
HETATM 1105 C  C   . A1B36 B 2 .   ? 10.490 9.182   22.540 1.00 27.75  ? 201 A1B36 A C   1 
HETATM 1106 BR BR  . A1B36 B 2 .   ? 6.184  12.183  27.307 1.00 51.89  ? 201 A1B36 A BR  1 
HETATM 1107 C  C3  . A1B36 B 2 .   ? 7.808  10.515  25.709 1.00 37.04  ? 201 A1B36 A C3  1 
HETATM 1108 C  C2  . A1B36 B 2 .   ? 8.692  10.240  24.685 1.00 33.35  ? 201 A1B36 A C2  1 
HETATM 1109 ZN ZN  . ZN    C 3 .   ? 11.070 -4.207  5.273  1.00 29.52  2 202 ZN    A ZN  1 
HETATM 1110 S  S   . DMS   D 4 .   ? 20.052 -2.606  21.109 1.00 112.19 ? 203 DMS   A S   1 
HETATM 1111 O  O   . DMS   D 4 .   ? 20.399 -3.506  22.265 1.00 112.01 ? 203 DMS   A O   1 
HETATM 1112 C  C1  . DMS   D 4 .   ? 21.599 -1.908  20.464 1.00 112.21 ? 203 DMS   A C1  1 
HETATM 1113 C  C2  . DMS   D 4 .   ? 19.702 -3.652  19.666 1.00 112.13 ? 203 DMS   A C2  1 
HETATM 1114 O  O   . HOH   E 5 .   ? -1.390 12.704  23.555 1.00 45.76  ? 301 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 22.095 -5.170  21.894 1.00 43.13  ? 302 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 2.829  8.370   9.666  1.00 42.47  ? 303 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 22.492 -0.710  3.676  1.00 42.20  ? 304 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 27.730 3.881   2.650  1.00 48.06  ? 305 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 8.464  -8.250  23.037 1.00 39.99  ? 306 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 3.199  21.732  22.525 1.00 40.50  ? 307 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 10.529 8.684   4.500  1.00 30.21  ? 308 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 10.138 24.087  24.428 1.00 42.10  ? 309 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 15.602 -7.552  26.443 1.00 60.97  ? 310 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 29.369 3.611   10.167 1.00 38.47  ? 311 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 4.249  -4.777  21.088 1.00 38.69  ? 312 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 13.011 7.334   30.773 1.00 41.29  ? 313 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 23.987 22.698  8.964  1.00 37.75  ? 314 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 22.176 -4.337  12.443 1.00 44.38  ? 315 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 6.764  -5.032  28.775 1.00 42.09  ? 316 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 8.422  -3.589  0.292  1.00 40.98  ? 317 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 17.576 -4.696  16.622 1.00 45.96  ? 318 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? -1.865 23.579  11.878 1.00 57.92  ? 319 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 17.236 20.704  19.180 1.00 43.58  ? 320 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 20.284 9.342   18.813 1.00 27.40  ? 321 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 8.277  19.645  18.203 1.00 30.05  ? 322 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 15.015 23.918  26.313 1.00 47.24  ? 323 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 8.958  2.994   2.665  1.00 34.18  ? 324 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 15.090 2.959   22.856 1.00 27.16  ? 325 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 12.192 11.053  0.419  1.00 62.02  ? 326 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 26.371 4.422   19.615 1.00 55.74  ? 327 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 4.961  20.161  25.649 1.00 42.66  ? 328 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 0.335  2.249   24.335 1.00 32.58  ? 329 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 19.406 0.148   27.300 1.00 42.28  ? 330 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 0.688  0.111   16.420 1.00 24.16  ? 331 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 7.387  25.716  15.197 1.00 44.93  ? 332 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 9.836  18.283  20.326 1.00 28.96  ? 333 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 18.598 5.055   26.191 1.00 34.99  ? 334 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? -1.005 1.976   4.784  1.00 49.39  ? 335 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 10.327 5.209   3.133  1.00 29.16  ? 336 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 23.417 0.408   15.693 1.00 37.42  ? 337 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 13.657 14.810  25.217 1.00 34.95  ? 338 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 15.387 23.535  18.273 1.00 48.00  ? 339 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 15.315 11.503  0.542  1.00 38.09  ? 340 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 18.032 2.954   22.818 1.00 29.61  ? 341 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 7.321  16.821  24.630 1.00 33.58  ? 342 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 15.345 12.707  23.830 1.00 30.75  ? 343 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 18.059 0.935   29.785 1.00 49.89  ? 344 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 11.156 17.885  5.481  1.00 61.96  ? 345 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 13.897 15.632  27.637 1.00 46.88  ? 346 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 18.485 19.828  5.287  1.00 48.30  ? 347 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 3.296  4.172   27.351 1.00 39.72  ? 348 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 11.412 12.082  11.163 1.00 26.25  ? 349 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? -0.373 16.392  8.856  1.00 67.29  ? 350 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 24.233 17.366  2.721  1.00 54.66  ? 351 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 9.565  15.681  26.252 1.00 34.12  ? 352 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 13.268 2.510   0.671  1.00 32.14  ? 353 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 12.251 21.661  12.771 1.00 34.64  ? 354 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 6.049  8.089   28.556 1.00 42.38  ? 355 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 6.020  2.073   6.042  1.00 31.23  ? 356 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 9.483  9.133   31.827 1.00 42.79  ? 357 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 7.362  4.130   32.689 1.00 42.76  ? 358 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 34.084 -2.821  9.854  1.00 41.87  ? 359 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 13.762 9.640   29.527 1.00 36.22  ? 360 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 13.045 -8.109  24.089 1.00 37.22  ? 361 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 0.934  -2.134  19.675 1.00 37.88  ? 362 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 23.447 17.174  22.334 1.00 67.81  ? 363 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 14.699 21.662  8.350  1.00 49.60  ? 364 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 7.233  16.141  21.932 1.00 29.53  ? 365 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 22.338 -7.384  4.792  1.00 61.94  ? 366 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 26.762 -1.528  6.174  1.00 56.14  ? 367 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 17.832 23.236  16.664 1.00 58.82  ? 368 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 0.819  8.679   4.731  1.00 50.49  ? 369 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 24.561 -6.540  8.020  1.00 63.37  ? 370 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 14.544 14.824  3.267  1.00 37.31  ? 371 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 0.194  4.294   6.565  1.00 39.06  ? 372 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 18.061 19.250  16.975 1.00 32.15  ? 373 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 19.070 9.626   25.511 1.00 37.31  ? 374 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 13.223 10.952  9.092  1.00 26.75  ? 375 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 5.436  -1.054  23.918 1.00 31.57  ? 376 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 5.434  0.785   -2.105 1.00 44.88  ? 377 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 11.951 -4.420  -1.255 1.00 56.97  ? 378 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 4.207  13.718  24.256 1.00 41.99  ? 379 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 28.470 -1.596  13.113 1.00 49.42  ? 380 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 30.076 5.041   3.363  1.00 60.80  ? 381 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 6.375  13.651  21.100 1.00 29.16  ? 382 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 6.162  25.709  21.080 1.00 35.22  ? 383 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 10.372 4.732   33.594 1.00 39.04  ? 384 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 17.876 21.506  9.071  1.00 40.38  ? 385 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 30.771 -3.584  6.901  1.00 52.72  ? 386 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 11.229 17.810  27.072 1.00 38.83  ? 387 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 19.101 13.386  2.125  1.00 55.23  ? 388 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 31.250 3.000   12.414 1.00 50.35  ? 389 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 3.027  13.623  18.068 1.00 37.84  ? 390 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 20.510 2.251   18.135 1.00 39.54  ? 391 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? -0.467 15.587  12.811 1.00 30.23  ? 392 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 15.742 -4.084  1.496  1.00 39.45  ? 393 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 16.280 23.969  14.348 1.00 72.57  ? 394 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 18.704 0.062   19.300 1.00 36.64  ? 395 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 6.158  23.252  11.602 1.00 35.93  ? 396 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 21.168 -4.686  9.843  1.00 48.62  ? 397 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 4.124  -4.819  6.268  1.00 44.58  ? 398 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 3.889  14.872  20.237 1.00 29.57  ? 399 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 15.308 -3.286  17.518 1.00 42.30  ? 400 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 6.681  13.284  5.257  1.00 33.77  ? 401 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 4.365  11.363  18.666 1.00 35.66  ? 402 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 23.752 2.763   19.372 1.00 45.32  ? 403 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 4.672  7.546   2.851  1.00 50.38  ? 404 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 34.919 7.925   13.786 1.00 74.44  ? 405 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 34.922 5.424   13.779 1.00 66.35  ? 406 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 2.022  13.643  5.209  1.00 41.80  ? 407 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 22.093 9.211   20.815 1.00 33.96  ? 408 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 1.585  -2.331  17.335 1.00 36.33  ? 409 HOH   A O   1 
HETATM 1223 O  O   . HOH   E 5 .   ? 3.998  -1.948  21.537 1.00 40.06  ? 410 HOH   A O   1 
HETATM 1224 O  O   . HOH   E 5 .   ? 26.120 -1.886  14.400 1.00 58.17  ? 411 HOH   A O   1 
HETATM 1225 O  O   . HOH   E 5 .   ? 4.476  6.556   25.278 1.00 44.43  ? 412 HOH   A O   1 
HETATM 1226 O  O   . HOH   E 5 .   ? 31.828 2.230   3.306  1.00 56.69  ? 413 HOH   A O   1 
HETATM 1227 O  O   . HOH   E 5 .   ? 19.659 24.657  15.089 1.00 64.92  ? 414 HOH   A O   1 
HETATM 1228 O  O   . HOH   E 5 .   ? 6.703  -3.682  -1.763 1.00 52.46  ? 415 HOH   A O   1 
HETATM 1229 O  O   . HOH   E 5 .   ? 2.882  10.835  20.842 1.00 42.66  ? 416 HOH   A O   1 
HETATM 1230 O  O   . HOH   E 5 .   ? 3.772  9.639   28.330 1.00 42.73  ? 417 HOH   A O   1 
HETATM 1231 O  O   . HOH   E 5 .   ? 6.165  -7.465  14.119 1.00 52.13  ? 418 HOH   A O   1 
HETATM 1232 O  O   . HOH   E 5 .   ? 22.667 19.277  5.633  1.00 41.21  ? 419 HOH   A O   1 
HETATM 1233 O  O   . HOH   E 5 .   ? 21.771 19.628  18.423 1.00 55.10  ? 420 HOH   A O   1 
HETATM 1234 O  O   . HOH   E 5 .   ? 2.105  6.809   28.307 1.00 55.53  ? 421 HOH   A O   1 
HETATM 1235 O  O   . HOH   E 5 .   ? 7.519  -5.063  2.424  1.00 50.91  ? 422 HOH   A O   1 
HETATM 1236 O  O   . HOH   E 5 .   ? 6.905  11.466  3.798  1.00 60.96  ? 423 HOH   A O   1 
HETATM 1237 O  O   . HOH   E 5 .   ? 0.977  20.757  25.596 1.00 71.18  ? 424 HOH   A O   1 
HETATM 1238 O  O   . HOH   E 5 .   ? 8.864  -7.156  8.547  1.00 47.41  ? 425 HOH   A O   1 
HETATM 1239 O  O   . HOH   E 5 .   ? 18.020 9.646   -1.907 1.00 51.85  ? 426 HOH   A O   1 
HETATM 1240 O  O   . HOH   E 5 .   ? 30.423 11.247  17.715 1.00 54.51  ? 427 HOH   A O   1 
HETATM 1241 O  O   . HOH   E 5 .   ? 4.693  -4.786  3.090  1.00 51.71  ? 428 HOH   A O   1 
HETATM 1242 O  O   . HOH   E 5 .   ? 5.056  -1.235  28.766 1.00 60.27  ? 429 HOH   A O   1 
HETATM 1243 O  O   . HOH   E 5 .   ? 2.068  -6.466  17.785 1.00 68.44  ? 430 HOH   A O   1 
HETATM 1244 O  O   . HOH   E 5 .   ? 34.741 10.977  13.197 1.00 58.97  ? 431 HOH   A O   1 
HETATM 1245 O  O   . HOH   E 5 .   ? 31.687 0.290   13.543 1.00 53.29  ? 432 HOH   A O   1 
HETATM 1246 O  O   . HOH   E 5 .   ? 35.424 10.968  10.594 1.00 62.82  ? 433 HOH   A O   1 
HETATM 1247 O  O   . HOH   E 5 .   ? 24.476 7.607   20.403 1.00 56.87  ? 434 HOH   A O   1 
HETATM 1248 O  O   . HOH   E 5 .   ? 19.191 7.699   27.618 1.00 52.59  ? 435 HOH   A O   1 
HETATM 1249 O  O   . HOH   E 5 .   ? 12.430 14.394  0.986  1.00 68.67  ? 436 HOH   A O   1 
HETATM 1250 O  O   . HOH   E 5 .   ? 17.694 11.194  0.120  1.00 48.95  ? 437 HOH   A O   1 
HETATM 1251 O  O   . HOH   E 5 .   ? -0.552 23.812  14.183 1.00 62.02  ? 438 HOH   A O   1 
HETATM 1252 O  O   . HOH   E 5 .   ? 3.171  -6.457  14.665 1.00 57.20  ? 439 HOH   A O   1 
HETATM 1253 O  O   . HOH   E 5 .   ? 17.247 11.891  25.785 1.00 42.92  ? 440 HOH   A O   1 
HETATM 1254 O  O   . HOH   E 5 .   ? 17.932 -6.019  25.986 1.00 53.94  ? 441 HOH   A O   1 
HETATM 1255 O  O   . HOH   E 5 .   ? 22.115 -2.887  34.532 1.00 63.89  ? 442 HOH   A O   1 
HETATM 1256 O  O   . HOH   E 5 .   ? 19.091 -7.327  7.664  1.00 53.29  ? 443 HOH   A O   1 
HETATM 1257 O  O   . HOH   E 5 .   ? 6.318  3.019   3.390  1.00 41.60  ? 444 HOH   A O   1 
HETATM 1258 O  O   . HOH   E 5 .   ? 8.274  -7.410  1.283  1.00 90.16  ? 445 HOH   A O   1 
HETATM 1259 O  O   . HOH   E 5 .   ? 16.468 12.151  28.481 1.00 61.31  ? 446 HOH   A O   1 
HETATM 1260 O  O   . HOH   E 5 .   ? 37.080 17.234  13.192 1.00 52.91  ? 447 HOH   A O   1 
HETATM 1261 O  O   . HOH   E 5 .   ? 21.085 -4.987  32.742 1.00 64.99  ? 448 HOH   A O   1 
HETATM 1262 O  O   . HOH   E 5 .   ? 28.962 16.586  23.633 1.00 58.30  ? 449 HOH   A O   1 
HETATM 1263 O  O   . HOH   E 5 .   ? 2.167  2.243   26.643 1.00 42.92  ? 450 HOH   A O   1 
HETATM 1264 O  O   . HOH   E 5 .   ? 12.087 23.649  14.848 1.00 47.46  ? 451 HOH   A O   1 
HETATM 1265 O  O   . HOH   E 5 .   ? 4.247  -1.773  26.312 1.00 54.46  ? 452 HOH   A O   1 
HETATM 1266 O  O   . HOH   E 5 .   ? 0.889  -1.116  23.594 1.00 52.44  ? 453 HOH   A O   1 
HETATM 1267 O  O   . HOH   E 5 .   ? 8.213  13.534  0.866  1.00 66.86  ? 454 HOH   A O   1 
HETATM 1268 O  O   . HOH   E 5 .   ? -1.622 21.015  24.855 1.00 77.63  ? 455 HOH   A O   1 
HETATM 1269 O  O   . HOH   E 5 .   ? 2.547  14.229  22.371 1.00 42.96  ? 456 HOH   A O   1 
HETATM 1270 O  O   . HOH   E 5 .   ? 8.649  7.473   2.460  1.00 44.77  ? 457 HOH   A O   1 
HETATM 1271 O  O   . HOH   E 5 .   ? 16.600 14.116  1.572  1.00 52.30  ? 458 HOH   A O   1 
HETATM 1272 O  O   . HOH   E 5 .   ? 20.058 15.087  0.292  1.00 66.23  ? 459 HOH   A O   1 
HETATM 1273 O  O   . HOH   E 5 .   ? 22.958 10.401  23.284 1.00 47.43  ? 460 HOH   A O   1 
HETATM 1274 O  O   . HOH   E 5 .   ? 0.525  12.595  21.533 1.00 56.12  ? 461 HOH   A O   1 
HETATM 1275 O  O   . HOH   E 5 .   ? 14.077 24.468  16.249 1.00 45.87  ? 462 HOH   A O   1 
HETATM 1276 O  O   . HOH   E 5 .   ? 31.918 8.920   15.130 1.00 57.64  ? 463 HOH   A O   1 
HETATM 1277 O  O   . HOH   E 5 .   ? 5.158  15.770  25.628 1.00 41.20  ? 464 HOH   A O   1 
HETATM 1278 O  O   . HOH   E 5 .   ? 7.855  9.998   29.780 1.00 39.37  ? 465 HOH   A O   1 
HETATM 1279 O  O   . HOH   E 5 .   ? 3.863  25.133  22.503 1.00 45.25  ? 466 HOH   A O   1 
HETATM 1280 O  O   . HOH   E 5 .   ? 14.233 11.965  -1.789 1.00 48.65  ? 467 HOH   A O   1 
HETATM 1281 O  O   . HOH   E 5 .   ? 21.538 10.849  25.450 1.00 43.99  ? 468 HOH   A O   1 
HETATM 1282 O  O   . HOH   E 5 .   ? 9.842  25.134  14.111 1.00 48.51  ? 469 HOH   A O   1 
HETATM 1283 O  O   . HOH   E 5 .   ? 5.894  5.254   1.999  1.00 59.77  ? 470 HOH   A O   1 
HETATM 1284 O  O   . HOH   E 5 .   ? 8.585  14.844  28.565 1.00 47.76  ? 471 HOH   A O   1 
HETATM 1285 O  O   . HOH   E 5 .   ? 8.097  12.522  29.947 1.00 42.99  ? 472 HOH   A O   1 
HETATM 1286 O  O   . HOH   E 5 .   ? 38.792 18.357  15.864 1.00 57.26  ? 473 HOH   A O   1 
HETATM 1287 O  O   . HOH   E 5 .   ? 1.554  20.575  4.321  1.00 63.57  ? 474 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   ? 0.3548 0.3387 0.5846 0.0031  -0.0759 -0.0117 7   SER   A N   
2    C  CA  . SER   A 1   ? 0.3489 0.3438 0.6101 0.0000  -0.0789 -0.0103 7   SER   A CA  
3    C  C   . SER   A 1   ? 0.3397 0.3453 0.6126 -0.0008 -0.0696 -0.0049 7   SER   A C   
4    O  O   . SER   A 1   ? 0.3446 0.3482 0.6019 0.0010  -0.0643 -0.0028 7   SER   A O   
5    C  CB  . SER   A 1   ? 0.3745 0.3643 0.6444 0.0005  -0.0962 -0.0130 7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.4169 0.4037 0.6783 0.0034  -0.1010 -0.0103 7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.3229 0.3385 0.6228 -0.0035 -0.0665 -0.0028 8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.3131 0.3372 0.6244 -0.0042 -0.0571 0.0015  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.2942 0.3268 0.6257 -0.0070 -0.0474 0.0038  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.2866 0.3194 0.6182 -0.0084 -0.0446 0.0030  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.2721 0.3104 0.6189 -0.0075 -0.0410 0.0070  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.2636 0.3076 0.6264 -0.0095 -0.0300 0.0097  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.2489 0.2957 0.6103 -0.0094 -0.0183 0.0122  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.2674 0.3131 0.6243 -0.0079 -0.0198 0.0122  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.2576 0.3044 0.6517 -0.0105 -0.0346 0.0105  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.2249 0.2738 0.5893 -0.0107 -0.0064 0.0144  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.2252 0.2747 0.5885 -0.0106 0.0055  0.0162  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.2302 0.2818 0.6218 -0.0106 0.0118  0.0192  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.2337 0.2862 0.6388 -0.0117 0.0126  0.0208  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.2247 0.2726 0.5685 -0.0115 0.0145  0.0166  10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.2172 0.2642 0.5385 -0.0116 0.0089  0.0141  10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.2283 0.2742 0.5685 -0.0114 0.0267  0.0175  10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.2244 0.2710 0.5312 -0.0124 0.0138  0.0149  10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.2399 0.2920 0.6431 -0.0095 0.0168  0.0203  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.2413 0.2955 0.6748 -0.0092 0.0247  0.0236  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.2541 0.3043 0.6798 -0.0085 0.0422  0.0249  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.2707 0.3191 0.6910 -0.0073 0.0447  0.0236  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.2337 0.2914 0.6932 -0.0077 0.0151  0.0240  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.2479 0.3073 0.7149 -0.0082 -0.0031 0.0223  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2468 0.3091 0.7398 -0.0098 -0.0062 0.0232  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2725 0.3291 0.7187 -0.0071 -0.0164 0.0194  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2568 0.3189 0.7542 -0.0105 -0.0236 0.0203  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2836 0.3390 0.7315 -0.0073 -0.0327 0.0170  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2818 0.3398 0.7549 -0.0091 -0.0370 0.0169  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.3121 0.3671 0.7842 -0.0096 -0.0538 0.0133  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.2529 0.2999 0.6731 -0.0092 0.0540  0.0271  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.2649 0.3051 0.6721 -0.0084 0.0712  0.0281  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2843 0.3228 0.7150 -0.0077 0.0853  0.0331  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2759 0.3156 0.7149 -0.0087 0.0850  0.0359  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2929 0.3278 0.6632 -0.0092 0.0728  0.0264  12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2898 0.3262 0.6566 -0.0102 0.0677  0.0285  12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.3007 0.3259 0.6543 -0.0081 0.0896  0.0269  12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2907 0.3263 0.7354 -0.0059 0.0985  0.0344  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2996 0.3330 0.7702 -0.0049 0.1146  0.0397  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2959 0.3386 0.8058 -0.0062 0.1055  0.0424  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2958 0.3462 0.8226 -0.0066 0.0894  0.0402  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2973 0.3384 0.8182 -0.0070 0.1133  0.0467  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2915 0.3408 0.8500 -0.0090 0.1031  0.0483  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2841 0.3341 0.8250 -0.0112 0.0893  0.0463  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2812 0.3325 0.8425 -0.0129 0.0891  0.0490  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.3108 0.3588 0.9054 -0.0086 0.1213  0.0548  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3707 0.4208 0.9940 -0.0064 0.1308  0.0563  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3776 0.4371 1.0371 -0.0068 0.1185  0.0555  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.4031 0.4434 1.0085 -0.0036 0.1518  0.0580  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.2737 0.3230 0.7796 -0.0113 0.0780  0.0416  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.2582 0.3075 0.7447 -0.0128 0.0658  0.0394  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.2438 0.2973 0.7223 -0.0132 0.0459  0.0337  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.2407 0.2949 0.7112 -0.0120 0.0433  0.0314  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.2762 0.3183 0.7232 -0.0120 0.0738  0.0402  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.2895 0.3242 0.7351 -0.0110 0.0929  0.0463  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2882 0.3228 0.7579 -0.0119 0.0975  0.0510  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.3085 0.3348 0.7270 -0.0090 0.1064  0.0474  15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.3023 0.3284 0.7693 -0.0105 0.1166  0.0577  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.3268 0.3436 0.7389 -0.0074 0.1245  0.0534  15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.3326 0.3492 0.7687 -0.0080 0.1302  0.0591  15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.3661 0.3718 0.7950 -0.0059 0.1498  0.0661  15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.2349 0.2896 0.7139 -0.0147 0.0330  0.0315  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.2333 0.2891 0.6999 -0.0148 0.0151  0.0261  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.2338 0.2862 0.6732 -0.0152 0.0130  0.0247  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.2304 0.2815 0.6774 -0.0163 0.0142  0.0262  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.2477 0.3066 0.7434 -0.0159 0.0006  0.0241  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.2857 0.3422 0.7643 -0.0157 -0.0176 0.0185  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.2934 0.3513 0.7998 -0.0167 -0.0333 0.0159  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.3228 0.3755 0.8177 -0.0177 -0.0464 0.0109  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.3307 0.3782 0.8031 -0.0162 -0.0605 0.0061  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.3170 0.3644 0.7760 -0.0137 -0.0633 0.0064  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.3328 0.3738 0.7943 -0.0170 -0.0704 0.0011  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.2221 0.2731 0.6323 -0.0142 0.0110  0.0224  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.2298 0.2784 0.6166 -0.0142 0.0093  0.0214  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.2289 0.2764 0.6070 -0.0139 -0.0047 0.0166  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.2379 0.2853 0.6062 -0.0128 -0.0094 0.0143  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.2518 0.2990 0.6129 -0.0134 0.0173  0.0222  17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.2558 0.3015 0.5980 -0.0132 0.0155  0.0222  17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.2551 0.3005 0.6200 -0.0131 0.0318  0.0263  17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.2136 0.2588 0.5932 -0.0144 -0.0102 0.0152  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.2262 0.2676 0.5939 -0.0137 -0.0223 0.0101  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.2270 0.2654 0.5795 -0.0133 -0.0208 0.0096  18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.2378 0.2772 0.5933 -0.0137 -0.0127 0.0134  18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.2297 0.2690 0.6173 -0.0146 -0.0342 0.0070  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.2407 0.2835 0.6463 -0.0145 -0.0377 0.0078  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.2256 0.2645 0.6332 -0.0166 -0.0317 0.0083  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.2191 0.2526 0.5557 -0.0120 -0.0284 0.0052  19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.2069 0.2366 0.5339 -0.0113 -0.0275 0.0042  19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.2143 0.2412 0.5605 -0.0128 -0.0304 0.0035  19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.2122 0.2365 0.5711 -0.0139 -0.0394 0.0000  19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.2229 0.2456 0.5313 -0.0093 -0.0343 -0.0010 19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.2415 0.2660 0.5326 -0.0078 -0.0308 -0.0001 19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.2552 0.2791 0.5436 -0.0074 -0.0343 -0.0008 19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.2217 0.2487 0.5037 -0.0071 -0.0238 0.0018  19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.2079 0.2347 0.5567 -0.0129 -0.0239 0.0066  20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.2171 0.2406 0.5860 -0.0145 -0.0252 0.0065  20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.2383 0.2534 0.6054 -0.0146 -0.0367 -0.0012 20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.2498 0.2623 0.6366 -0.0168 -0.0435 -0.0040 20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.2235 0.2467 0.5915 -0.0137 -0.0162 0.0117  20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.2381 0.2580 0.6296 -0.0155 -0.0143 0.0135  20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.2490 0.2672 0.6339 -0.0136 -0.0064 0.0189  20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.2862 0.3005 0.6918 -0.0149 -0.0018 0.0226  20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.3230 0.3303 0.7373 -0.0154 -0.0062 0.0187  20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.3240 0.3267 0.7273 -0.0149 -0.0156 0.0102  20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.3143 0.3179 0.7472 -0.0163 -0.0004 0.0232  20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.2380 0.2480 0.5815 -0.0122 -0.0391 -0.0050 21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.2604 0.2593 0.5964 -0.0116 -0.0490 -0.0129 21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.2748 0.2702 0.6117 -0.0124 -0.0618 -0.0178 21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.2817 0.2669 0.6163 -0.0126 -0.0723 -0.0247 21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.2750 0.2673 0.5859 -0.0083 -0.0459 -0.0153 21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.2862 0.2793 0.5765 -0.0061 -0.0453 -0.0154 21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.3020 0.3046 0.5889 -0.0056 -0.0367 -0.0096 21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.3110 0.2950 0.5825 -0.0043 -0.0522 -0.0205 21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.3091 0.3091 0.5786 -0.0039 -0.0379 -0.0112 21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.3164 0.3049 0.5749 -0.0027 -0.0465 -0.0172 21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.2796 0.2827 0.6205 -0.0126 -0.0615 -0.0144 22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.3064 0.3074 0.6512 -0.0129 -0.0741 -0.0177 22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.3164 0.3253 0.6957 -0.0159 -0.0762 -0.0150 22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.3216 0.3309 0.7094 -0.0160 -0.0866 -0.0165 22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.3095 0.3121 0.6342 -0.0103 -0.0727 -0.0159 22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.3426 0.3371 0.6356 -0.0071 -0.0696 -0.0181 22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.3563 0.3522 0.6332 -0.0049 -0.0674 -0.0156 22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.3580 0.3373 0.6361 -0.0058 -0.0803 -0.0258 22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.3181 0.3328 0.7175 -0.0179 -0.0657 -0.0102 23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.3254 0.3470 0.7598 -0.0206 -0.0646 -0.0068 23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.3473 0.3639 0.8026 -0.0229 -0.0804 -0.0130 23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.3471 0.3545 0.7935 -0.0233 -0.0876 -0.0189 23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.3204 0.3455 0.7677 -0.0218 -0.0494 -0.0005 23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.3693 0.3915 0.8514 -0.0243 -0.0866 -0.0121 24  THR   A N   
135  C  CA  . THR   A 18  ? 0.4005 0.4197 0.9084 -0.0269 -0.1037 -0.0177 24  THR   A CA  
136  C  C   . THR   A 18  ? 0.4178 0.4404 0.9641 -0.0309 -0.0968 -0.0150 24  THR   A C   
137  O  O   . THR   A 18  ? 0.4162 0.4448 0.9710 -0.0309 -0.0783 -0.0072 24  THR   A O   
138  C  CB  . THR   A 18  ? 0.4197 0.4447 0.9432 -0.0263 -0.1134 -0.0167 24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.4269 0.4632 0.9788 -0.0270 -0.0986 -0.0087 24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.4295 0.4509 0.9164 -0.0221 -0.1184 -0.0178 24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.4255 0.4435 0.9960 -0.0342 -0.1115 -0.0212 25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.4100 0.4308 1.0211 -0.0383 -0.1044 -0.0184 25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.3879 0.4210 1.0330 -0.0389 -0.0899 -0.0089 25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.3947 0.4301 1.0570 -0.0401 -0.0724 -0.0021 25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.4203 0.4342 1.0550 -0.0422 -0.1247 -0.0276 25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.4598 0.4767 1.1131 -0.0429 -0.1450 -0.0317 25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.4778 0.5015 1.1847 -0.0471 -0.1512 -0.0310 25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.4875 0.5008 1.1138 -0.0398 -0.1606 -0.0360 25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.4806 0.5059 1.1921 -0.0462 -0.1712 -0.0347 25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 0.4984 0.5168 1.1607 -0.0417 -0.1775 -0.0377 25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.3662 0.4056 1.0140 -0.0371 -0.0950 -0.0077 26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.3613 0.4113 1.0357 -0.0366 -0.0826 0.0003  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.3604 0.4126 1.0125 -0.0338 -0.0588 0.0083  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.3629 0.4208 1.0390 -0.0339 -0.0428 0.0155  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.3889 0.4425 1.0655 -0.0347 -0.0980 -0.0021 26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.4814 0.5327 1.1824 -0.0373 -0.1236 -0.0096 26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.5543 0.6000 1.2319 -0.0354 -0.1430 -0.0158 26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.4490 0.5037 1.1971 -0.0416 -0.1246 -0.0094 26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.3434 0.3905 0.9496 -0.0311 -0.0566 0.0068  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.3152 0.3631 0.8975 -0.0287 -0.0369 0.0133  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.2821 0.3270 0.8739 -0.0303 -0.0232 0.0179  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.2732 0.3195 0.8666 -0.0293 -0.0046 0.0256  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.3230 0.3663 0.8586 -0.0260 -0.0410 0.0098  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.3545 0.3998 0.8742 -0.0236 -0.0485 0.0077  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.3393 0.3904 0.8709 -0.0228 -0.0409 0.0119  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.3671 0.4070 0.8622 -0.0224 -0.0611 0.0020  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.2716 0.3106 0.8661 -0.0322 -0.0318 0.0134  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.2842 0.3192 0.8896 -0.0335 -0.0198 0.0180  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.2863 0.3251 0.9369 -0.0360 -0.0086 0.0244  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.2906 0.3277 0.9441 -0.0353 0.0104  0.0328  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.2902 0.3175 0.8946 -0.0354 -0.0330 0.0105  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.3053 0.3271 0.8665 -0.0324 -0.0360 0.0071  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.3283 0.3463 0.8654 -0.0312 -0.0511 -0.0012 28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.3194 0.3387 0.8573 -0.0298 -0.0228 0.0126  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.3496 0.3635 0.8519 -0.0281 -0.0466 -0.0012 28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.3438 0.3589 0.8475 -0.0274 -0.0305 0.0070  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.3238 0.3433 0.8656 -0.0290 -0.0052 0.0222  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.3533 0.3663 0.8319 -0.0245 -0.0220 0.0105  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.3457 0.3619 0.8591 -0.0259 0.0017  0.0256  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.3534 0.3675 0.8374 -0.0238 -0.0070 0.0198  28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.2748 0.3185 0.9601 -0.0385 -0.0198 0.0209  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.2849 0.3332 1.0185 -0.0409 -0.0089 0.0270  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.2911 0.3431 1.0187 -0.0376 0.0127  0.0361  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2960 0.3471 1.0450 -0.0379 0.0324  0.0444  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.2749 0.3290 1.0466 -0.0437 -0.0279 0.0211  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.2845 0.3389 0.9810 -0.0344 0.0099  0.0345  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.2875 0.3436 0.9761 -0.0314 0.0288  0.0414  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.2871 0.3373 0.9272 -0.0283 0.0399  0.0443  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.2960 0.3469 0.9142 -0.0255 0.0473  0.0459  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.3255 0.3881 1.0175 -0.0301 0.0189  0.0380  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.3747 0.4440 1.1195 -0.0327 0.0099  0.0370  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.3764 0.4482 1.1586 -0.0336 0.0251  0.0433  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.3876 0.4592 1.1371 -0.0338 -0.0148 0.0293  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.2548 0.2992 0.8796 -0.0287 0.0402  0.0447  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.2604 0.2996 0.8418 -0.0258 0.0472  0.0472  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.2652 0.3005 0.8348 -0.0231 0.0693  0.0560  31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.2476 0.2801 0.8419 -0.0235 0.0844  0.0628  31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.2489 0.2823 0.8239 -0.0266 0.0436  0.0468  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.2664 0.2950 0.7994 -0.0234 0.0478  0.0492  31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.2699 0.3016 0.7736 -0.0222 0.0343  0.0420  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.2655 0.2880 0.8005 -0.0239 0.0471  0.0506  31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.2643 0.2980 0.7948 -0.0203 0.0713  0.0557  32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.2789 0.3062 0.7872 -0.0173 0.0897  0.0627  32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.2919 0.3134 0.7653 -0.0155 0.0885  0.0647  32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.3016 0.3151 0.7674 -0.0137 0.1015  0.0724  32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.2916 0.3210 0.7828 -0.0157 0.0913  0.0599  32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.3136 0.3339 0.7721 -0.0125 0.1074  0.0653  32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.2798 0.3146 0.8070 -0.0167 0.0940  0.0592  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.2805 0.3056 0.7334 -0.0155 0.0729  0.0581  33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.2942 0.3156 0.7178 -0.0136 0.0702  0.0595  33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.2824 0.3086 0.6995 -0.0145 0.0527  0.0516  33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.2694 0.3007 0.6877 -0.0154 0.0440  0.0453  33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.3050 0.3230 0.6948 -0.0108 0.0771  0.0619  33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.3176 0.3340 0.6777 -0.0089 0.0707  0.0621  33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.3412 0.3510 0.6885 -0.0066 0.0755  0.0690  33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.3088 0.3304 0.6509 -0.0089 0.0584  0.0557  33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.3512 0.3628 0.6751 -0.0051 0.0658  0.0670  33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.3288 0.3478 0.6506 -0.0067 0.0558  0.0587  33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.3021 0.3300 0.6446 -0.0103 0.0498  0.0483  33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.3230 0.3462 0.6274 -0.0063 0.0456  0.0544  33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.3022 0.3331 0.6253 -0.0098 0.0407  0.0442  33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.3120 0.3409 0.6176 -0.0079 0.0390  0.0471  33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.2609 0.2843 0.6705 -0.0137 0.0488  0.0524  34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.2560 0.2818 0.6564 -0.0138 0.0349  0.0454  34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.2589 0.2816 0.6395 -0.0112 0.0355  0.0489  34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.2639 0.2815 0.6452 -0.0098 0.0442  0.0565  34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.2689 0.2945 0.6942 -0.0164 0.0257  0.0398  34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.2909 0.3113 0.7386 -0.0174 0.0316  0.0443  34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.3403 0.3556 0.7805 -0.0161 0.0295  0.0450  34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.3417 0.3519 0.7981 -0.0164 0.0364  0.0502  34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.3207 0.3367 0.7409 -0.0145 0.0219  0.0406  34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.2472 0.2725 0.6113 -0.0102 0.0265  0.0440  35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.2523 0.2759 0.6019 -0.0076 0.0258  0.0470  35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.2389 0.2638 0.5858 -0.0074 0.0158  0.0397  35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.2334 0.2621 0.5693 -0.0076 0.0109  0.0348  35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.2885 0.3134 0.6151 -0.0056 0.0293  0.0512  35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.3827 0.4063 0.6959 -0.0025 0.0279  0.0558  35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.4188 0.4415 0.7397 -0.0016 0.0241  0.0549  35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.4155 0.4383 0.7106 -0.0008 0.0301  0.0601  35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.2265 0.2468 0.5835 -0.0071 0.0139  0.0389  36  SER   A N   
241  C  CA  A SER   A 30  ? 0.2350 0.2536 0.5885 -0.0064 0.0064  0.0319  36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.2375 0.2563 0.5906 -0.0064 0.0062  0.0317  36  SER   A CA  
243  C  C   . SER   A 30  ? 0.2384 0.2609 0.5734 -0.0036 0.0054  0.0326  36  SER   A C   
244  O  O   . SER   A 30  ? 0.2611 0.2844 0.5879 -0.0033 0.0008  0.0266  36  SER   A O   
245  C  CB  A SER   A 30  ? 0.2468 0.2583 0.6133 -0.0059 0.0069  0.0322  36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.2582 0.2698 0.6248 -0.0063 0.0056  0.0306  36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.2773 0.2848 0.6385 -0.0048 0.0011  0.0251  36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.2928 0.3030 0.6571 -0.0034 0.0110  0.0381  36  SER   A OG  
249  N  N   . SER   A 31  ? 0.2220 0.2462 0.5505 -0.0015 0.0098  0.0403  37  SER   A N   
250  C  CA  . SER   A 31  ? 0.2385 0.2672 0.5539 0.0009  0.0076  0.0412  37  SER   A CA  
251  C  C   . SER   A 31  ? 0.2297 0.2641 0.5334 -0.0005 0.0054  0.0379  37  SER   A C   
252  O  O   . SER   A 31  ? 0.2482 0.2864 0.5449 0.0007  0.0027  0.0367  37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2865 0.3150 0.5979 0.0037  0.0101  0.0501  37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.3712 0.3988 0.6758 0.0031  0.0145  0.0553  37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.2136 0.2484 0.5177 -0.0029 0.0069  0.0366  38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.2117 0.2507 0.5062 -0.0043 0.0054  0.0331  38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.2183 0.2566 0.5175 -0.0059 0.0015  0.0261  38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.2151 0.2561 0.5074 -0.0068 0.0002  0.0232  38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.2304 0.2693 0.5210 -0.0053 0.0107  0.0368  38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.2465 0.2848 0.5243 -0.0034 0.0130  0.0430  38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.2511 0.2860 0.5219 -0.0041 0.0200  0.0460  38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.2513 0.2892 0.5137 -0.0057 0.0186  0.0410  38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.2785 0.3137 0.5261 -0.0058 0.0223  0.0421  38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.2711 0.2997 0.5079 -0.0039 0.0278  0.0484  38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.2621 0.2995 0.5041 -0.0074 0.0209  0.0371  38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.2054 0.2388 0.5156 -0.0062 -0.0009 0.0233  39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.2079 0.2387 0.5217 -0.0075 -0.0066 0.0169  39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.2168 0.2507 0.5358 -0.0094 -0.0057 0.0174  39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.2199 0.2540 0.5352 -0.0098 -0.0102 0.0133  39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.2200 0.2492 0.5200 -0.0061 -0.0105 0.0118  39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.2309 0.2545 0.5301 -0.0067 -0.0175 0.0055  39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.2270 0.2459 0.5375 -0.0077 -0.0217 0.0032  39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.2553 0.2791 0.5435 -0.0061 -0.0194 0.0033  39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.2130 0.2483 0.5409 -0.0103 0.0009  0.0228  40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.2186 0.2563 0.5541 -0.0117 0.0039  0.0236  40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.2194 0.2553 0.5784 -0.0132 0.0068  0.0258  40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.2149 0.2479 0.5803 -0.0130 0.0109  0.0297  40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.2243 0.2639 0.5475 -0.0111 0.0118  0.0278  40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.2511 0.2934 0.5555 -0.0105 0.0094  0.0253  40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.2492 0.2915 0.5415 -0.0103 0.0164  0.0288  40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.2483 0.2919 0.5543 -0.0113 0.0046  0.0205  40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.2085 0.2463 0.5819 -0.0146 0.0049  0.0240  41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.2171 0.2547 0.6181 -0.0163 0.0084  0.0264  41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.2240 0.2650 0.6322 -0.0165 0.0133  0.0277  41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.2281 0.2714 0.6278 -0.0160 0.0076  0.0241  41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.2200 0.2555 0.6391 -0.0181 -0.0033 0.0210  41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.2311 0.2669 0.6854 -0.0205 -0.0013 0.0230  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.2391 0.2698 0.7057 -0.0222 -0.0090 0.0194  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.2372 0.2773 0.7098 -0.0215 -0.0072 0.0207  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.2224 0.2628 0.6454 -0.0168 0.0256  0.0334  42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.2399 0.2826 0.6730 -0.0167 0.0327  0.0350  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.2462 0.2901 0.7174 -0.0184 0.0359  0.0373  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.2361 0.2767 0.7186 -0.0190 0.0434  0.0418  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.2612 0.3004 0.6739 -0.0148 0.0475  0.0398  42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.2723 0.3120 0.6984 -0.0144 0.0576  0.0415  42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.2664 0.3052 0.6453 -0.0136 0.0429  0.0370  42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.2433 0.2917 0.7359 -0.0191 0.0292  0.0346  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.2440 0.2950 0.7787 -0.0210 0.0310  0.0366  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.2602 0.3141 0.8105 -0.0198 0.0418  0.0398  43  SER   A C   
300  O  O   . SER   A 37  ? 0.2531 0.3074 0.7831 -0.0179 0.0424  0.0383  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.2441 0.2978 0.7973 -0.0230 0.0107  0.0303  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.2767 0.3326 0.8172 -0.0217 -0.0013 0.0256  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.2701 0.3254 0.8583 -0.0208 0.0517  0.0443  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.2836 0.3409 0.8903 -0.0193 0.0644  0.0478  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.2942 0.3592 0.9258 -0.0196 0.0486  0.0437  44  SER   A C   
306  O  O   . SER   A 38  ? 0.3020 0.3704 0.9499 -0.0217 0.0301  0.0395  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.3007 0.3565 0.9420 -0.0200 0.0822  0.0549  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.3243 0.3846 1.0030 -0.0233 0.0701  0.0534  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.2890 0.3557 0.9233 -0.0172 0.0555  0.0448  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.2959 0.3695 0.9556 -0.0167 0.0415  0.0423  45  THR   A CA  
311  C  C   . THR   A 39  ? 0.3181 0.3951 1.0190 -0.0155 0.0570  0.0477  45  THR   A C   
312  O  O   . THR   A 39  ? 0.3324 0.4040 1.0273 -0.0140 0.0803  0.0524  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.3084 0.3809 0.9338 -0.0144 0.0332  0.0384  45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.3246 0.3936 0.9375 -0.0119 0.0521  0.0412  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.3065 0.3749 0.8895 -0.0150 0.0224  0.0338  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.3185 0.4033 1.0587 -0.0155 0.0442  0.0471  46  THR   A N   
317  C  CA  . THR   A 40  ? 0.3365 0.4254 1.1191 -0.0138 0.0588  0.0523  46  THR   A CA  
318  C  C   . THR   A 40  ? 0.3527 0.4397 1.1174 -0.0099 0.0657  0.0523  46  THR   A C   
319  O  O   . THR   A 40  ? 0.3638 0.4483 1.1411 -0.0076 0.0878  0.0567  46  THR   A O   
320  C  CB  . THR   A 40  ? 0.3646 0.4634 1.2035 -0.0156 0.0421  0.0523  46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.4014 0.5032 1.2299 -0.0147 0.0161  0.0471  46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.3665 0.4661 1.2264 -0.0200 0.0364  0.0518  46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.3505 0.4372 1.0856 -0.0089 0.0479  0.0475  47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.3554 0.4399 1.0741 -0.0054 0.0529  0.0472  47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.3645 0.4395 1.0305 -0.0049 0.0654  0.0453  47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.3690 0.4410 1.0042 -0.0069 0.0596  0.0427  47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.3609 0.4491 1.0774 -0.0043 0.0279  0.0440  47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.3544 0.4246 1.0113 -0.0022 0.0816  0.0463  48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.3658 0.4264 0.9745 -0.0019 0.0921  0.0438  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.3333 0.3937 0.9105 -0.0019 0.0751  0.0389  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.3222 0.3858 0.9115 0.0000  0.0659  0.0385  48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.4126 0.4661 1.0229 0.0009  0.1157  0.0457  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.5125 0.5540 1.0749 0.0010  0.1290  0.0432  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.5962 0.6288 1.1633 0.0040  0.1535  0.0450  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6018 0.6329 1.1957 0.0051  0.1698  0.0499  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.6160 0.6415 1.1585 0.0055  0.1575  0.0408  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.3122 0.3685 0.8509 -0.0036 0.0720  0.0359  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.2989 0.3541 0.8061 -0.0039 0.0587  0.0316  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.2858 0.3340 0.7673 -0.0028 0.0695  0.0295  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.2995 0.3420 0.7796 -0.0020 0.0876  0.0305  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.2536 0.3011 0.7151 -0.0026 0.0591  0.0263  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.2600 0.3009 0.7015 -0.0019 0.0678  0.0237  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.2658 0.3029 0.6698 -0.0040 0.0641  0.0196  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.2752 0.3070 0.6635 -0.0039 0.0686  0.0167  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.2724 0.3146 0.7304 0.0006  0.0626  0.0245  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.3076 0.3543 0.8140 0.0035  0.0690  0.0295  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.2584 0.2983 0.6509 -0.0058 0.0553  0.0193  51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.2748 0.3122 0.6362 -0.0075 0.0518  0.0159  51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.2942 0.3251 0.6371 -0.0084 0.0647  0.0147  51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.3098 0.3385 0.6602 -0.0079 0.0746  0.0174  51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.2753 0.3169 0.6311 -0.0086 0.0394  0.0161  51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.3319 0.3766 0.6970 -0.0075 0.0257  0.0162  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.3503 0.3934 0.7162 -0.0061 0.0241  0.0159  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.3268 0.3741 0.6972 -0.0077 0.0164  0.0167  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.2954 0.3219 0.6150 -0.0096 0.0651  0.0108  52  THR   A N   
356  C  CA  . THR   A 46  ? 0.3187 0.3377 0.6153 -0.0106 0.0737  0.0087  52  THR   A CA  
357  C  C   . THR   A 46  ? 0.3036 0.3254 0.5821 -0.0124 0.0641  0.0079  52  THR   A C   
358  O  O   . THR   A 46  ? 0.2833 0.3093 0.5590 -0.0134 0.0543  0.0061  52  THR   A O   
359  C  CB  . THR   A 46  ? 0.3717 0.3834 0.6554 -0.0111 0.0786  0.0038  52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.4042 0.4120 0.7047 -0.0089 0.0898  0.0047  52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.3915 0.3946 0.6457 -0.0125 0.0825  0.0000  52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.3043 0.3231 0.5712 -0.0124 0.0678  0.0098  53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.3053 0.3266 0.5570 -0.0136 0.0592  0.0098  53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.3092 0.3243 0.5360 -0.0150 0.0590  0.0052  53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.3173 0.3229 0.5319 -0.0145 0.0684  0.0035  53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.3144 0.3348 0.5664 -0.0125 0.0626  0.0148  53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.3089 0.3350 0.5894 -0.0117 0.0626  0.0186  53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.3246 0.3476 0.5626 -0.0132 0.0534  0.0153  53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.3021 0.3363 0.5937 -0.0124 0.0493  0.0171  53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.2759 0.2955 0.4959 -0.0167 0.0485  0.0029  54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.2782 0.2934 0.4784 -0.0186 0.0454  -0.0017 54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.2805 0.2904 0.4614 -0.0178 0.0455  0.0002  54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.2801 0.2940 0.4647 -0.0166 0.0429  0.0050  54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.2738 0.2967 0.4780 -0.0204 0.0345  -0.0035 54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.2978 0.2974 0.4566 -0.0185 0.0476  -0.0038 55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.3132 0.3060 0.4487 -0.0175 0.0455  -0.0020 55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.3287 0.3202 0.4498 -0.0202 0.0342  -0.0083 55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.3368 0.3176 0.4411 -0.0213 0.0365  -0.0143 55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.3356 0.3141 0.4545 -0.0150 0.0594  -0.0006 55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.3529 0.3336 0.4930 -0.0127 0.0715  0.0052  55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.3925 0.3805 0.5445 -0.0114 0.0688  0.0125  55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.4078 0.3978 0.5833 -0.0099 0.0795  0.0170  55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.4254 0.4231 0.6203 -0.0094 0.0773  0.0222  55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.3994 0.4028 0.5916 -0.0098 0.0664  0.0239  55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.4138 0.4131 0.6326 -0.0086 0.0860  0.0256  55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.3272 0.3297 0.4584 -0.0215 0.0222  -0.0075 56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.3316 0.3364 0.4598 -0.0247 0.0110  -0.0131 56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.3369 0.3526 0.4746 -0.0248 -0.0006 -0.0097 56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.3186 0.3396 0.4647 -0.0223 0.0008  -0.0033 56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.3194 0.3281 0.4647 -0.0272 0.0133  -0.0175 56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.3063 0.3288 0.4800 -0.0262 0.0134  -0.0123 56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.3488 0.3685 0.4895 -0.0278 -0.0115 -0.0142 57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.3529 0.3840 0.5083 -0.0278 -0.0213 -0.0112 57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.3399 0.3798 0.5186 -0.0306 -0.0222 -0.0141 57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.3327 0.3804 0.5239 -0.0319 -0.0307 -0.0142 57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.4010 0.4300 0.5433 -0.0283 -0.0346 -0.0122 57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.5063 0.5301 0.6412 -0.0324 -0.0420 -0.0208 57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 0.5203 0.5410 0.6591 -0.0348 -0.0353 -0.0260 57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 0.5698 0.5919 0.6949 -0.0330 -0.0552 -0.0223 57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.3242 0.3625 0.5096 -0.0311 -0.0130 -0.0157 58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.2985 0.3429 0.5033 -0.0330 -0.0119 -0.0171 58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.2691 0.3234 0.4897 -0.0313 -0.0145 -0.0122 58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.2608 0.3169 0.4801 -0.0282 -0.0134 -0.0073 58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.3092 0.3498 0.5173 -0.0322 -0.0018 -0.0172 58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.3224 0.3521 0.5207 -0.0349 0.0025  -0.0244 58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.2407 0.3005 0.4766 -0.0335 -0.0172 -0.0137 59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.2305 0.2981 0.4820 -0.0317 -0.0170 -0.0095 59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.2277 0.2954 0.4914 -0.0321 -0.0096 -0.0097 59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.2120 0.2847 0.4893 -0.0313 -0.0082 -0.0073 59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.2594 0.3340 0.5212 -0.0328 -0.0266 -0.0094 59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.3049 0.3811 0.5591 -0.0300 -0.0325 -0.0054 59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.3488 0.4334 0.6192 -0.0306 -0.0419 -0.0044 59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.3543 0.4386 0.6201 -0.0325 -0.0528 -0.0067 59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.3363 0.4278 0.6264 -0.0288 -0.0382 -0.0009 59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.2102 0.2716 0.4690 -0.0332 -0.0043 -0.0122 60  THR   A N   
416  C  CA  . THR   A 54  ? 0.2056 0.2648 0.4719 -0.0329 0.0029  -0.0113 60  THR   A CA  
417  C  C   . THR   A 54  ? 0.2156 0.2684 0.4716 -0.0307 0.0078  -0.0105 60  THR   A C   
418  O  O   . THR   A 54  ? 0.2147 0.2641 0.4610 -0.0310 0.0071  -0.0125 60  THR   A O   
419  C  CB  . THR   A 54  ? 0.2366 0.2948 0.5133 -0.0370 0.0036  -0.0153 60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.2811 0.3333 0.5485 -0.0393 0.0026  -0.0202 60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.2300 0.2956 0.5217 -0.0397 -0.0026 -0.0164 60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.2124 0.2632 0.4705 -0.0280 0.0125  -0.0073 61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.2117 0.2577 0.4639 -0.0255 0.0153  -0.0057 61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.2151 0.2576 0.4685 -0.0226 0.0187  -0.0023 61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.2325 0.2747 0.4905 -0.0229 0.0214  -0.0014 61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.2055 0.2444 0.4549 -0.0197 0.0186  -0.0003 62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.2155 0.2490 0.4619 -0.0163 0.0198  0.0030  62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.2136 0.2470 0.4561 -0.0135 0.0152  0.0045  62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.2252 0.2608 0.4704 -0.0138 0.0130  0.0039  62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.2344 0.2621 0.4822 -0.0157 0.0227  0.0037  62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.2492 0.2698 0.4908 -0.0114 0.0220  0.0078  62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.2469 0.2737 0.5000 -0.0190 0.0275  0.0016  62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.2157 0.2454 0.4520 -0.0106 0.0142  0.0063  63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.2062 0.2345 0.4390 -0.0082 0.0085  0.0068  63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.2274 0.2465 0.4513 -0.0044 0.0058  0.0088  63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.2473 0.2601 0.4636 -0.0029 0.0099  0.0104  63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.2005 0.2316 0.4321 -0.0080 0.0074  0.0061  63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.2281 0.2532 0.4513 -0.0055 0.0104  0.0069  63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.2436 0.2696 0.4693 -0.0064 0.0171  0.0076  63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.2422 0.2599 0.4553 -0.0022 0.0070  0.0068  63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.2594 0.2791 0.4785 -0.0037 0.0224  0.0088  63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.2574 0.2674 0.4600 0.0006  0.0116  0.0072  63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.2683 0.2794 0.4742 0.0000  0.0203  0.0086  63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.2843 0.2869 0.4809 0.0032  0.0272  0.0096  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.2303 0.2479 0.4548 -0.0028 -0.0013 0.0087  64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.2445 0.2524 0.4587 0.0010  -0.0069 0.0102  64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.2562 0.2576 0.4569 0.0033  -0.0096 0.0088  64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.2477 0.2526 0.4533 0.0023  -0.0134 0.0066  64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.2359 0.2449 0.4599 0.0017  -0.0150 0.0106  64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.2554 0.2537 0.4676 0.0059  -0.0234 0.0121  64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.2802 0.2698 0.4803 0.0088  -0.0211 0.0153  64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.2820 0.2775 0.4940 0.0072  -0.0343 0.0102  64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.3054 0.2832 0.4910 0.0133  -0.0300 0.0172  64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.2999 0.2842 0.4990 0.0112  -0.0445 0.0111  64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.3230 0.2980 0.5068 0.0146  -0.0424 0.0148  64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.3508 0.3127 0.5176 0.0192  -0.0534 0.0160  64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.2715 0.2616 0.4547 0.0066  -0.0076 0.0102  65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.2915 0.2718 0.4577 0.0095  -0.0085 0.0086  65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.3095 0.2766 0.4591 0.0137  -0.0186 0.0089  65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.3256 0.2827 0.4609 0.0168  -0.0165 0.0122  65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.3173 0.2929 0.4746 0.0106  0.0036  0.0103  65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.3457 0.3057 0.4790 0.0152  0.0060  0.0085  65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.2943 0.2609 0.4466 0.0136  -0.0303 0.0056  66  SER   A N   
464  C  CA  . SER   A 60  ? 0.3153 0.2700 0.4540 0.0172  -0.0429 0.0054  66  SER   A CA  
465  C  C   . SER   A 60  ? 0.3370 0.2725 0.4428 0.0221  -0.0420 0.0048  66  SER   A C   
466  O  O   . SER   A 60  ? 0.3586 0.2813 0.4462 0.0262  -0.0491 0.0069  66  SER   A O   
467  C  CB  . SER   A 60  ? 0.3425 0.3015 0.4957 0.0155  -0.0562 0.0017  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.3983 0.3536 0.5455 0.0151  -0.0569 -0.0030 66  SER   A OG  
469  N  N   . SER   A 61  ? 0.3284 0.2606 0.4255 0.0222  -0.0324 0.0026  67  SER   A N   
470  C  CA  . SER   A 61  ? 0.3465 0.2586 0.4107 0.0273  -0.0278 0.0020  67  SER   A CA  
471  C  C   . SER   A 61  ? 0.3684 0.2722 0.4182 0.0304  -0.0164 0.0082  67  SER   A C   
472  O  O   . SER   A 61  ? 0.4103 0.2949 0.4299 0.0354  -0.0113 0.0090  67  SER   A O   
473  C  CB  . SER   A 61  ? 0.3366 0.2477 0.3990 0.0269  -0.0188 -0.0017 67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.3526 0.2770 0.4339 0.0241  -0.0048 0.0011  67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.3398 0.2562 0.4096 0.0277  -0.0117 0.0123  68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.3507 0.2600 0.4114 0.0300  -0.0016 0.0185  68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.3581 0.2711 0.4281 0.0299  -0.0095 0.0222  68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.3655 0.2724 0.4298 0.0319  -0.0022 0.0278  68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.3624 0.2827 0.4414 0.0265  0.0146  0.0200  68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.3751 0.2910 0.4469 0.0275  0.0250  0.0177  68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 0.4106 0.3050 0.4529 0.0334  0.0356  0.0214  68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 0.4439 0.3330 0.4807 0.0349  0.0479  0.0196  68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 0.4658 0.3437 0.4837 0.0378  0.0442  0.0149  68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 0.4557 0.3265 0.4582 0.0392  0.0273  0.0113  68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 0.4710 0.3445 0.4869 0.0393  0.0572  0.0135  68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.3554 0.2793 0.4440 0.0274  -0.0228 0.0197  69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.3646 0.2947 0.4688 0.0269  -0.0291 0.0230  69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.3620 0.3003 0.4815 0.0241  -0.0151 0.0262  69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.3809 0.3145 0.4992 0.0261  -0.0132 0.0312  69  ARG   A O   
490  C  CB  . ARG   A 63  ? 0.3988 0.3125 0.4816 0.0330  -0.0396 0.0271  69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 0.4635 0.3679 0.5313 0.0355  -0.0565 0.0231  69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 0.5210 0.4098 0.5689 0.0416  -0.0689 0.0277  69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 0.5618 0.4392 0.5920 0.0442  -0.0868 0.0231  69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 0.6162 0.4703 0.6067 0.0504  -0.0926 0.0241  69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 0.6263 0.4661 0.5911 0.0548  -0.0798 0.0303  69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 0.5987 0.4423 0.5739 0.0521  -0.1105 0.0185  69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.3383 0.2879 0.4713 0.0196  -0.0059 0.0233  70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.3395 0.2959 0.4861 0.0165  0.0062  0.0251  70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.3115 0.2847 0.4809 0.0108  0.0076  0.0210  70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.3144 0.2927 0.4861 0.0095  0.0040  0.0174  70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.3887 0.3363 0.5221 0.0180  0.0193  0.0273  70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.4908 0.4345 0.6274 0.0181  0.0292  0.0322  70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.5934 0.5277 0.7194 0.0198  0.0435  0.0351  70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 0.6396 0.5819 0.7872 0.0153  0.0552  0.0359  70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 0.6812 0.6222 0.8362 0.0148  0.0551  0.0390  70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.2796 0.2596 0.4641 0.0076  0.0131  0.0215  71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.2702 0.2638 0.4728 0.0024  0.0150  0.0177  71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.2857 0.2809 0.4912 0.0001  0.0250  0.0175  71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.3038 0.2928 0.5080 0.0007  0.0319  0.0204  71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.2744 0.2725 0.4907 0.0006  0.0141  0.0175  71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.2835 0.2811 0.5027 0.0030  0.0049  0.0183  71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.3027 0.3089 0.5343 0.0008  0.0011  0.0156  71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.2857 0.2747 0.4974 0.0074  -0.0015 0.0218  71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.3037 0.3076 0.5390 0.0036  -0.0069 0.0174  71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.3007 0.2945 0.5239 0.0076  -0.0100 0.0209  71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.2692 0.2723 0.4807 -0.0025 0.0258  0.0146  72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.2635 0.2694 0.4820 -0.0047 0.0340  0.0145  72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.2464 0.2641 0.4810 -0.0100 0.0329  0.0108  72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.2363 0.2605 0.4731 -0.0111 0.0272  0.0085  72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.2669 0.2709 0.4790 -0.0025 0.0362  0.0147  72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.2967 0.2861 0.4889 0.0029  0.0393  0.0177  72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.3293 0.3095 0.5164 0.0048  0.0498  0.0216  72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.3092 0.2926 0.4867 0.0062  0.0322  0.0166  72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.3629 0.3269 0.5269 0.0104  0.0536  0.0247  72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.3400 0.3078 0.4951 0.0114  0.0344  0.0187  72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.3812 0.3386 0.5276 0.0138  0.0454  0.0229  72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.4215 0.3606 0.5407 0.0196  0.0478  0.0252  72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.2430 0.2624 0.4881 -0.0131 0.0381  0.0103  73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.2386 0.2677 0.4965 -0.0181 0.0354  0.0060  73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.2626 0.2983 0.5265 -0.0185 0.0347  0.0057  73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.2840 0.3166 0.5492 -0.0166 0.0410  0.0084  73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.2557 0.2824 0.5236 -0.0211 0.0410  0.0054  73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.2712 0.2890 0.5348 -0.0177 0.0493  0.0105  73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.2545 0.2658 0.5000 -0.0122 0.0467  0.0135  73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.2367 0.2802 0.5034 -0.0204 0.0279  0.0031  74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.2427 0.2927 0.5162 -0.0203 0.0262  0.0034  74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.2285 0.2868 0.5101 -0.0241 0.0193  0.0003  74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.2250 0.2827 0.5009 -0.0261 0.0154  -0.0024 74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.2763 0.3248 0.5397 -0.0165 0.0237  0.0049  74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.3073 0.3466 0.5616 -0.0122 0.0297  0.0076  74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.2745 0.3224 0.5296 -0.0165 0.0182  0.0038  74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.2119 0.2769 0.5059 -0.0247 0.0177  0.0008  75  SER   A N   
543  C  CA  . SER   A 69  ? 0.2034 0.2759 0.5033 -0.0273 0.0088  -0.0012 75  SER   A CA  
544  C  C   . SER   A 69  ? 0.1900 0.2643 0.4843 -0.0237 0.0063  0.0015  75  SER   A C   
545  O  O   . SER   A 69  ? 0.1957 0.2685 0.4922 -0.0204 0.0116  0.0042  75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2336 0.3130 0.5550 -0.0296 0.0078  -0.0015 75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3283 0.4066 0.6574 -0.0339 0.0083  -0.0049 75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.1692 0.2453 0.4560 -0.0240 -0.0008 0.0010  76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.1756 0.2528 0.4585 -0.0207 -0.0027 0.0040  76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.1962 0.2787 0.4808 -0.0214 -0.0113 0.0047  76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.2190 0.3020 0.5004 -0.0243 -0.0169 0.0021  76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.1841 0.2549 0.4530 -0.0188 -0.0004 0.0045  76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.1916 0.2593 0.4508 -0.0208 -0.0016 0.0023  76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.2038 0.2675 0.4614 -0.0223 0.0021  0.0001  76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.2087 0.2765 0.4604 -0.0210 -0.0056 0.0028  76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.2228 0.2830 0.4728 -0.0239 0.0022  -0.0022 76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.2220 0.2852 0.4639 -0.0225 -0.0047 0.0007  76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.2130 0.2727 0.4548 -0.0240 -0.0008 -0.0021 76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.1921 0.2775 0.4815 -0.0184 -0.0128 0.0083  77  SER   A N   
560  C  CA  . SER   A 71  ? 0.1967 0.2865 0.4875 -0.0181 -0.0216 0.0103  77  SER   A CA  
561  C  C   . SER   A 71  ? 0.2091 0.2934 0.4804 -0.0178 -0.0241 0.0108  77  SER   A C   
562  O  O   . SER   A 71  ? 0.2113 0.2901 0.4734 -0.0173 -0.0184 0.0104  77  SER   A O   
563  C  CB  . SER   A 71  ? 0.2114 0.3049 0.5142 -0.0144 -0.0210 0.0145  77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.2459 0.3335 0.5400 -0.0116 -0.0151 0.0159  77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.2205 0.3055 0.4858 -0.0179 -0.0325 0.0121  78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.2491 0.3272 0.4946 -0.0170 -0.0330 0.0136  78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.2461 0.3226 0.4921 -0.0133 -0.0286 0.0188  78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.2388 0.3199 0.4985 -0.0111 -0.0287 0.0214  78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.2934 0.3709 0.5296 -0.0174 -0.0439 0.0143  78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.3459 0.4220 0.5778 -0.0216 -0.0485 0.0078  78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.4223 0.4952 0.6402 -0.0220 -0.0608 0.0072  78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.4590 0.5265 0.6672 -0.0263 -0.0633 -0.0006 78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.4898 0.5523 0.6817 -0.0271 -0.0772 -0.0026 78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.2536 0.3233 0.4866 -0.0125 -0.0241 0.0203  79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.2578 0.3255 0.4940 -0.0095 -0.0200 0.0249  79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.2565 0.3267 0.4971 -0.0065 -0.0253 0.0303  79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.2735 0.3427 0.5047 -0.0059 -0.0319 0.0329  79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.2756 0.3356 0.4983 -0.0095 -0.0146 0.0260  79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.2920 0.3502 0.5081 -0.0126 -0.0130 0.0204  79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.2611 0.3239 0.4781 -0.0142 -0.0212 0.0179  79  PRO   A CD  
581  N  N   A SER   A 74  ? 0.2463 0.3190 0.5008 -0.0044 -0.0231 0.0319  80  SER   A N   
582  N  N   B SER   A 74  ? 0.2447 0.3173 0.4991 -0.0044 -0.0230 0.0320  80  SER   A N   
583  C  CA  A SER   A 74  ? 0.2496 0.3250 0.5123 -0.0012 -0.0273 0.0373  80  SER   A CA  
584  C  CA  B SER   A 74  ? 0.2465 0.3217 0.5090 -0.0012 -0.0273 0.0373  80  SER   A CA  
585  C  C   A SER   A 74  ? 0.2476 0.3201 0.5189 0.0015  -0.0216 0.0395  80  SER   A C   
586  C  C   B SER   A 74  ? 0.2460 0.3184 0.5171 0.0015  -0.0216 0.0396  80  SER   A C   
587  O  O   A SER   A 74  ? 0.2479 0.3167 0.5192 0.0005  -0.0157 0.0362  80  SER   A O   
588  O  O   B SER   A 74  ? 0.2461 0.3148 0.5170 0.0005  -0.0157 0.0363  80  SER   A O   
589  C  CB  A SER   A 74  ? 0.2557 0.3394 0.5328 -0.0013 -0.0330 0.0361  80  SER   A CB  
590  C  CB  B SER   A 74  ? 0.2480 0.3317 0.5251 -0.0013 -0.0328 0.0361  80  SER   A CB  
591  O  OG  A SER   A 74  ? 0.2717 0.3576 0.5617 -0.0015 -0.0268 0.0327  80  SER   A OG  
592  O  OG  B SER   A 74  ? 0.2621 0.3481 0.5344 -0.0047 -0.0376 0.0322  80  SER   A OG  
593  N  N   . LEU   A 75  ? 0.2431 0.3166 0.5222 0.0049  -0.0242 0.0450  81  LEU   A N   
594  C  CA  . LEU   A 75  ? 0.2452 0.3148 0.5334 0.0076  -0.0191 0.0469  81  LEU   A CA  
595  C  C   . LEU   A 75  ? 0.2483 0.3222 0.5517 0.0086  -0.0172 0.0436  81  LEU   A C   
596  O  O   . LEU   A 75  ? 0.2458 0.3263 0.5600 0.0099  -0.0214 0.0456  81  LEU   A O   
597  C  CB  . LEU   A 75  ? 0.2469 0.3149 0.5358 0.0112  -0.0225 0.0551  81  LEU   A CB  
598  C  CG  . LEU   A 75  ? 0.2737 0.3362 0.5715 0.0140  -0.0173 0.0581  81  LEU   A CG  
599  C  CD1 . LEU   A 75  ? 0.2690 0.3242 0.5607 0.0120  -0.0111 0.0564  81  LEU   A CD1 
600  C  CD2 . LEU   A 75  ? 0.2885 0.3502 0.5891 0.0183  -0.0216 0.0675  81  LEU   A CD2 
601  N  N   . ILE   A 76  ? 0.2403 0.3095 0.5442 0.0080  -0.0107 0.0385  82  ILE   A N   
602  C  CA  A ILE   A 76  ? 0.2422 0.3120 0.5549 0.0090  -0.0063 0.0347  82  ILE   A CA  
603  C  CA  B ILE   A 76  ? 0.2419 0.3118 0.5550 0.0091  -0.0064 0.0349  82  ILE   A CA  
604  C  C   . ILE   A 76  ? 0.2468 0.3082 0.5623 0.0115  -0.0007 0.0330  82  ILE   A C   
605  O  O   . ILE   A 76  ? 0.2404 0.2952 0.5483 0.0104  0.0001  0.0311  82  ILE   A O   
606  C  CB  A ILE   A 76  ? 0.2560 0.3249 0.5596 0.0058  -0.0043 0.0290  82  ILE   A CB  
607  C  CB  B ILE   A 76  ? 0.2550 0.3254 0.5607 0.0059  -0.0048 0.0295  82  ILE   A CB  
608  C  CG1 A ILE   A 76  ? 0.2737 0.3501 0.5765 0.0031  -0.0092 0.0293  82  ILE   A CG1 
609  C  CG1 B ILE   A 76  ? 0.2671 0.3459 0.5744 0.0037  -0.0103 0.0304  82  ILE   A CG1 
610  C  CG2 A ILE   A 76  ? 0.2625 0.3270 0.5683 0.0071  0.0026  0.0247  82  ILE   A CG2 
611  C  CG2 B ILE   A 76  ? 0.2632 0.3297 0.5721 0.0074  0.0023  0.0255  82  ILE   A CG2 
612  C  CD1 A ILE   A 76  ? 0.2850 0.3687 0.6029 0.0036  -0.0097 0.0297  82  ILE   A CD1 
613  C  CD1 B ILE   A 76  ? 0.2845 0.3629 0.5841 0.0002  -0.0088 0.0257  82  ILE   A CD1 
614  N  N   . PHE   A 77  ? 0.2506 0.3117 0.5778 0.0148  0.0035  0.0332  83  PHE   A N   
615  C  CA  . PHE   A 77  ? 0.2742 0.3250 0.6020 0.0174  0.0094  0.0303  83  PHE   A CA  
616  C  C   . PHE   A 77  ? 0.2774 0.3202 0.5916 0.0159  0.0132  0.0230  83  PHE   A C   
617  O  O   . PHE   A 77  ? 0.2964 0.3413 0.6083 0.0153  0.0160  0.0210  83  PHE   A O   
618  C  CB  . PHE   A 77  ? 0.2891 0.3403 0.6330 0.0219  0.0146  0.0323  83  PHE   A CB  
619  C  CG  . PHE   A 77  ? 0.3206 0.3602 0.6654 0.0248  0.0195  0.0303  83  PHE   A CG  
620  C  CD1 . PHE   A 77  ? 0.3446 0.3818 0.6923 0.0252  0.0163  0.0340  83  PHE   A CD1 
621  C  CD2 . PHE   A 77  ? 0.3478 0.3770 0.6885 0.0270  0.0280  0.0244  83  PHE   A CD2 
622  C  CE1 . PHE   A 77  ? 0.3652 0.3909 0.7152 0.0274  0.0207  0.0316  83  PHE   A CE1 
623  C  CE2 . PHE   A 77  ? 0.3577 0.3746 0.6980 0.0295  0.0321  0.0214  83  PHE   A CE2 
624  C  CZ  . PHE   A 77  ? 0.3648 0.3805 0.7114 0.0295  0.0281  0.0249  83  PHE   A CZ  
625  N  N   . VAL   A 78  ? 0.2570 0.2903 0.5629 0.0153  0.0128  0.0194  84  VAL   A N   
626  C  CA  . VAL   A 78  ? 0.2621 0.2862 0.5533 0.0142  0.0138  0.0126  84  VAL   A CA  
627  C  C   . VAL   A 78  ? 0.2796 0.2900 0.5674 0.0170  0.0177  0.0079  84  VAL   A C   
628  O  O   . VAL   A 78  ? 0.2759 0.2823 0.5699 0.0174  0.0161  0.0083  84  VAL   A O   
629  C  CB  . VAL   A 78  ? 0.2574 0.2821 0.5424 0.0104  0.0075  0.0118  84  VAL   A CB  
630  C  CG1 . VAL   A 78  ? 0.2728 0.2869 0.5442 0.0096  0.0059  0.0050  84  VAL   A CG1 
631  C  CG2 . VAL   A 78  ? 0.2436 0.2793 0.5287 0.0079  0.0050  0.0153  84  VAL   A CG2 
632  N  N   . GLU   A 79  ? 0.2914 0.2934 0.5687 0.0192  0.0235  0.0034  85  GLU   A N   
633  C  CA  . GLU   A 79  ? 0.3065 0.2926 0.5759 0.0223  0.0281  -0.0023 85  GLU   A CA  
634  C  C   . GLU   A 79  ? 0.3011 0.2769 0.5619 0.0203  0.0208  -0.0077 85  GLU   A C   
635  O  O   . GLU   A 79  ? 0.2842 0.2640 0.5421 0.0167  0.0131  -0.0079 85  GLU   A O   
636  C  CB  . GLU   A 79  ? 0.3542 0.3307 0.6080 0.0250  0.0362  -0.0061 85  GLU   A CB  
637  C  CG  . GLU   A 79  ? 0.4545 0.4393 0.7226 0.0275  0.0455  -0.0012 85  GLU   A CG  
638  C  CD  . GLU   A 79  ? 0.5646 0.5490 0.8499 0.0311  0.0507  0.0010  85  GLU   A CD  
639  O  OE1 . GLU   A 79  ? 0.5920 0.5605 0.8684 0.0344  0.0570  -0.0042 85  GLU   A OE1 
640  O  OE2 . GLU   A 79  ? 0.5869 0.5856 0.8933 0.0306  0.0477  0.0076  85  GLU   A OE2 
641  N  N   . ALA   A 80  ? 0.3096 0.2719 0.5684 0.0227  0.0232  -0.0124 86  ALA   A N   
642  C  CA  . ALA   A 80  ? 0.3285 0.2795 0.5808 0.0206  0.0155  -0.0188 86  ALA   A CA  
643  C  C   . ALA   A 80  ? 0.3380 0.2797 0.5673 0.0196  0.0101  -0.0251 86  ALA   A C   
644  O  O   . ALA   A 80  ? 0.3385 0.2750 0.5516 0.0223  0.0159  -0.0264 86  ALA   A O   
645  C  CB  . ALA   A 80  ? 0.3363 0.2721 0.5887 0.0236  0.0199  -0.0238 86  ALA   A CB  
646  N  N   . SER   A 81  ? 0.3263 0.2664 0.5561 0.0160  -0.0008 -0.0282 87  SER   A N   
647  C  CA  . SER   A 81  ? 0.3449 0.2757 0.5552 0.0151  -0.0092 -0.0341 87  SER   A CA  
648  C  C   . SER   A 81  ? 0.3684 0.2887 0.5813 0.0127  -0.0200 -0.0410 87  SER   A C   
649  O  O   . SER   A 81  ? 0.3606 0.2809 0.5905 0.0118  -0.0189 -0.0408 87  SER   A O   
650  C  CB  . SER   A 81  ? 0.3403 0.2853 0.5548 0.0122  -0.0135 -0.0290 87  SER   A CB  
651  O  OG  . SER   A 81  ? 0.3355 0.2909 0.5712 0.0082  -0.0195 -0.0259 87  SER   A OG  
652  N  N   . GLU   A 82  ? 0.3931 0.3050 0.5918 0.0114  -0.0313 -0.0468 88  GLU   A N   
653  C  CA  . GLU   A 82  ? 0.4147 0.3179 0.6203 0.0085  -0.0436 -0.0536 88  GLU   A CA  
654  C  C   . GLU   A 82  ? 0.3950 0.3147 0.6334 0.0037  -0.0473 -0.0478 88  GLU   A C   
655  O  O   . GLU   A 82  ? 0.3960 0.3111 0.6493 0.0009  -0.0540 -0.0517 88  GLU   A O   
656  C  CB  . GLU   A 82  ? 0.4715 0.3602 0.6538 0.0088  -0.0569 -0.0614 88  GLU   A CB  
657  C  CG  . GLU   A 82  ? 0.5556 0.4557 0.7394 0.0072  -0.0632 -0.0568 88  GLU   A CG  
658  C  CD  . GLU   A 82  ? 0.6664 0.5560 0.8385 0.0063  -0.0807 -0.0632 88  GLU   A CD  
659  O  OE1 . GLU   A 82  ? 0.6825 0.5668 0.8672 0.0033  -0.0926 -0.0692 88  GLU   A OE1 
660  O  OE2 . GLU   A 82  ? 0.6923 0.5791 0.8442 0.0086  -0.0830 -0.0620 88  GLU   A OE2 
661  N  N   . TYR   A 83  ? 0.3719 0.3093 0.6216 0.0028  -0.0417 -0.0386 89  TYR   A N   
662  C  CA  . TYR   A 83  ? 0.3527 0.3040 0.6293 -0.0011 -0.0429 -0.0325 89  TYR   A CA  
663  C  C   . TYR   A 83  ? 0.3298 0.2893 0.6232 -0.0009 -0.0328 -0.0252 89  TYR   A C   
664  O  O   . TYR   A 83  ? 0.3237 0.2886 0.6384 -0.0037 -0.0333 -0.0216 89  TYR   A O   
665  C  CB  . TYR   A 83  ? 0.3533 0.3164 0.6293 -0.0021 -0.0440 -0.0278 89  TYR   A CB  
666  C  CG  . TYR   A 83  ? 0.3839 0.3398 0.6496 -0.0027 -0.0562 -0.0338 89  TYR   A CG  
667  C  CD1 . TYR   A 83  ? 0.3982 0.3521 0.6805 -0.0060 -0.0675 -0.0373 89  TYR   A CD1 
668  C  CD2 . TYR   A 83  ? 0.4142 0.3637 0.6538 0.0003  -0.0568 -0.0359 89  TYR   A CD2 
669  C  CE1 . TYR   A 83  ? 0.4283 0.3756 0.7021 -0.0062 -0.0808 -0.0425 89  TYR   A CE1 
670  C  CE2 . TYR   A 83  ? 0.4432 0.3845 0.6709 0.0005  -0.0690 -0.0407 89  TYR   A CE2 
671  C  CZ  . TYR   A 83  ? 0.4649 0.4054 0.7096 -0.0028 -0.0820 -0.0441 89  TYR   A CZ  
672  O  OH  . TYR   A 83  ? 0.5199 0.4528 0.7544 -0.0024 -0.0962 -0.0485 89  TYR   A OH  
673  N  N   . TYR   A 84  ? 0.3186 0.2791 0.6036 0.0027  -0.0237 -0.0223 90  TYR   A N   
674  C  CA  . TYR   A 84  ? 0.3058 0.2732 0.6055 0.0036  -0.0158 -0.0149 90  TYR   A CA  
675  C  C   . TYR   A 84  ? 0.3339 0.2939 0.6267 0.0079  -0.0088 -0.0164 90  TYR   A C   
676  O  O   . TYR   A 84  ? 0.3463 0.3016 0.6217 0.0105  -0.0063 -0.0198 90  TYR   A O   
677  C  CB  . TYR   A 84  ? 0.2817 0.2647 0.5839 0.0035  -0.0114 -0.0060 90  TYR   A CB  
678  C  CG  . TYR   A 84  ? 0.2537 0.2450 0.5622 0.0000  -0.0151 -0.0032 90  TYR   A CG  
679  C  CD1 . TYR   A 84  ? 0.2452 0.2406 0.5711 -0.0021 -0.0138 0.0021  90  TYR   A CD1 
680  C  CD2 . TYR   A 84  ? 0.2623 0.2568 0.5597 -0.0007 -0.0183 -0.0050 90  TYR   A CD2 
681  C  CE1 . TYR   A 84  ? 0.2320 0.2344 0.5645 -0.0048 -0.0149 0.0050  90  TYR   A CE1 
682  C  CE2 . TYR   A 84  ? 0.2515 0.2532 0.5561 -0.0034 -0.0205 -0.0024 90  TYR   A CE2 
683  C  CZ  . TYR   A 84  ? 0.2427 0.2487 0.5648 -0.0054 -0.0182 0.0027  90  TYR   A CZ  
684  O  OH  . TYR   A 84  ? 0.2377 0.2499 0.5675 -0.0077 -0.0184 0.0054  90  TYR   A OH  
685  N  N   . PRO   A 85  ? 0.3309 0.2907 0.6382 0.0092  -0.0039 -0.0124 91  PRO   A N   
686  C  CA  . PRO   A 85  ? 0.3301 0.2861 0.6350 0.0139  0.0043  -0.0117 91  PRO   A CA  
687  C  C   . PRO   A 85  ? 0.3162 0.2865 0.6208 0.0157  0.0088  -0.0040 91  PRO   A C   
688  O  O   . PRO   A 85  ? 0.3025 0.2845 0.6084 0.0131  0.0057  0.0008  91  PRO   A O   
689  C  CB  . PRO   A 85  ? 0.3361 0.2893 0.6597 0.0145  0.0071  -0.0080 91  PRO   A CB  
690  C  CG  . PRO   A 85  ? 0.3424 0.3047 0.6790 0.0107  0.0034  -0.0018 91  PRO   A CG  
691  C  CD  . PRO   A 85  ? 0.3267 0.2908 0.6545 0.0069  -0.0042 -0.0066 91  PRO   A CD  
692  N  N   . ALA   A 86  ? 0.3163 0.2855 0.6207 0.0200  0.0164  -0.0029 92  ALA   A N   
693  C  CA  . ALA   A 86  ? 0.3195 0.3022 0.6281 0.0217  0.0199  0.0040  92  ALA   A CA  
694  C  C   . ALA   A 86  ? 0.3015 0.2963 0.6245 0.0206  0.0170  0.0135  92  ALA   A C   
695  O  O   . ALA   A 86  ? 0.2977 0.2888 0.6316 0.0213  0.0173  0.0163  92  ALA   A O   
696  C  CB  . ALA   A 86  ? 0.3408 0.3197 0.6536 0.0267  0.0288  0.0040  92  ALA   A CB  
697  N  N   . ARG   A 87  ? 0.2804 0.2871 0.6009 0.0184  0.0136  0.0177  93  ARG   A N   
698  C  CA  . ARG   A 87  ? 0.2692 0.2843 0.5973 0.0174  0.0106  0.0261  93  ARG   A CA  
699  C  C   . ARG   A 87  ? 0.2772 0.3044 0.6011 0.0163  0.0080  0.0300  93  ARG   A C   
700  O  O   . ARG   A 87  ? 0.2900 0.3191 0.6067 0.0154  0.0084  0.0258  93  ARG   A O   
701  C  CB  . ARG   A 87  ? 0.2754 0.2863 0.6030 0.0138  0.0078  0.0250  93  ARG   A CB  
702  C  CG  . ARG   A 87  ? 0.2986 0.3141 0.6167 0.0100  0.0042  0.0229  93  ARG   A CG  
703  C  CD  . ARG   A 87  ? 0.3098 0.3187 0.6286 0.0068  0.0013  0.0177  93  ARG   A CD  
704  N  NE  . ARG   A 87  ? 0.3004 0.3151 0.6160 0.0037  -0.0011 0.0187  93  ARG   A NE  
705  C  CZ  . ARG   A 87  ? 0.2998 0.3173 0.6051 0.0026  -0.0033 0.0150  93  ARG   A CZ  
706  N  NH1 . ARG   A 87  ? 0.2640 0.2790 0.5599 0.0044  -0.0028 0.0107  93  ARG   A NH1 
707  N  NH2 . ARG   A 87  ? 0.2517 0.2735 0.5564 -0.0001 -0.0048 0.0159  93  ARG   A NH2 
708  N  N   . TYR   A 88  ? 0.2610 0.2946 0.5875 0.0161  0.0052  0.0377  94  TYR   A N   
709  C  CA  . TYR   A 88  ? 0.2598 0.3028 0.5798 0.0145  0.0015  0.0399  94  TYR   A CA  
710  C  C   . TYR   A 88  ? 0.2463 0.2881 0.5567 0.0107  0.0004  0.0383  94  TYR   A C   
711  O  O   . TYR   A 88  ? 0.2483 0.2857 0.5604 0.0100  0.0015  0.0410  94  TYR   A O   
712  C  CB  . TYR   A 88  ? 0.2769 0.3258 0.6008 0.0168  -0.0021 0.0487  94  TYR   A CB  
713  C  CG  . TYR   A 88  ? 0.2980 0.3510 0.6349 0.0206  -0.0022 0.0508  94  TYR   A CG  
714  C  CD1 . TYR   A 88  ? 0.3056 0.3669 0.6456 0.0203  -0.0046 0.0496  94  TYR   A CD1 
715  C  CD2 . TYR   A 88  ? 0.3186 0.3668 0.6675 0.0244  0.0009  0.0539  94  TYR   A CD2 
716  C  CE1 . TYR   A 88  ? 0.3094 0.3753 0.6661 0.0238  -0.0040 0.0519  94  TYR   A CE1 
717  C  CE2 . TYR   A 88  ? 0.3215 0.3736 0.6855 0.0284  0.0017  0.0561  94  TYR   A CE2 
718  C  CZ  . TYR   A 88  ? 0.3287 0.3902 0.6975 0.0281  -0.0007 0.0553  94  TYR   A CZ  
719  O  OH  . TYR   A 88  ? 0.3379 0.4042 0.7259 0.0320  0.0008  0.0579  94  TYR   A OH  
720  N  N   . GLN   A 89  ? 0.2226 0.2680 0.5250 0.0082  -0.0008 0.0342  95  GLN   A N   
721  C  CA  . GLN   A 89  ? 0.2222 0.2671 0.5172 0.0049  -0.0014 0.0329  95  GLN   A CA  
722  C  C   . GLN   A 89  ? 0.2260 0.2773 0.5138 0.0041  -0.0037 0.0367  95  GLN   A C   
723  O  O   . GLN   A 89  ? 0.2324 0.2892 0.5194 0.0043  -0.0060 0.0359  95  GLN   A O   
724  C  CB  . GLN   A 89  ? 0.2301 0.2727 0.5203 0.0031  -0.0015 0.0256  95  GLN   A CB  
725  C  CG  . GLN   A 89  ? 0.2273 0.2708 0.5125 0.0000  -0.0022 0.0245  95  GLN   A CG  
726  C  CD  . GLN   A 89  ? 0.2225 0.2617 0.5050 -0.0012 -0.0037 0.0181  95  GLN   A CD  
727  O  OE1 . GLN   A 89  ? 0.2226 0.2551 0.5066 -0.0002 -0.0046 0.0145  95  GLN   A OE1 
728  N  NE2 . GLN   A 89  ? 0.2243 0.2658 0.5017 -0.0031 -0.0043 0.0167  95  GLN   A NE2 
729  N  N   . SER   A 90  ? 0.2147 0.2642 0.4973 0.0032  -0.0027 0.0406  96  SER   A N   
730  C  CA  . SER   A 90  ? 0.2136 0.2659 0.4850 0.0026  -0.0048 0.0435  96  SER   A CA  
731  C  C   . SER   A 90  ? 0.2125 0.2657 0.4764 -0.0006 -0.0038 0.0386  96  SER   A C   
732  O  O   . SER   A 90  ? 0.2022 0.2534 0.4703 -0.0021 -0.0015 0.0344  96  SER   A O   
733  C  CB  . SER   A 90  ? 0.2367 0.2837 0.5027 0.0041  -0.0024 0.0508  96  SER   A CB  
734  O  OG  . SER   A 90  ? 0.2468 0.2889 0.5160 0.0024  0.0037  0.0501  96  SER   A OG  
735  N  N   . HIS   A 91  ? 0.2127 0.2681 0.4656 -0.0014 -0.0065 0.0390  97  HIS   A N   
736  C  CA  . HIS   A 91  ? 0.2186 0.2740 0.4635 -0.0042 -0.0053 0.0346  97  HIS   A CA  
737  C  C   . HIS   A 91  ? 0.2159 0.2744 0.4677 -0.0058 -0.0055 0.0286  97  HIS   A C   
738  O  O   . HIS   A 91  ? 0.2071 0.2639 0.4577 -0.0075 -0.0028 0.0254  97  HIS   A O   
739  C  CB  . HIS   A 91  ? 0.2275 0.2768 0.4688 -0.0049 0.0014  0.0361  97  HIS   A CB  
740  C  CG  . HIS   A 91  ? 0.2877 0.3315 0.5189 -0.0030 0.0038  0.0427  97  HIS   A CG  
741  N  ND1 . HIS   A 91  ? 0.3256 0.3650 0.5388 -0.0033 0.0048  0.0435  97  HIS   A ND1 
742  C  CD2 . HIS   A 91  ? 0.2927 0.3330 0.5275 -0.0006 0.0056  0.0489  97  HIS   A CD2 
743  C  CE1 . HIS   A 91  ? 0.3285 0.3614 0.5330 -0.0007 0.0075  0.0504  97  HIS   A CE1 
744  N  NE2 . HIS   A 91  ? 0.3014 0.3350 0.5195 0.0010  0.0082  0.0544  97  HIS   A NE2 
745  N  N   . LEU   A 92  ? 0.2112 0.2734 0.4706 -0.0046 -0.0079 0.0277  98  LEU   A N   
746  C  CA  . LEU   A 92  ? 0.2236 0.2864 0.4869 -0.0052 -0.0067 0.0230  98  LEU   A CA  
747  C  C   . LEU   A 92  ? 0.2131 0.2810 0.4766 -0.0066 -0.0088 0.0211  98  LEU   A C   
748  O  O   . LEU   A 92  ? 0.2120 0.2845 0.4792 -0.0061 -0.0127 0.0233  98  LEU   A O   
749  C  CB  . LEU   A 92  ? 0.2353 0.2963 0.5067 -0.0026 -0.0054 0.0230  98  LEU   A CB  
750  C  CG  . LEU   A 92  ? 0.2559 0.3139 0.5272 -0.0023 -0.0028 0.0184  98  LEU   A CG  
751  C  CD1 . LEU   A 92  ? 0.2574 0.3100 0.5232 -0.0035 -0.0026 0.0154  98  LEU   A CD1 
752  C  CD2 . LEU   A 92  ? 0.2783 0.3326 0.5553 0.0009  -0.0006 0.0183  98  LEU   A CD2 
753  N  N   . MET   A 93  ? 0.2003 0.2673 0.4616 -0.0084 -0.0066 0.0172  99  MET   A N   
754  C  CA  . MET   A 93  ? 0.1900 0.2609 0.4537 -0.0102 -0.0075 0.0151  99  MET   A CA  
755  C  C   . MET   A 93  ? 0.2010 0.2703 0.4697 -0.0091 -0.0030 0.0132  99  MET   A C   
756  O  O   . MET   A 93  ? 0.2153 0.2787 0.4786 -0.0083 -0.0003 0.0118  99  MET   A O   
757  C  CB  . MET   A 93  ? 0.1907 0.2596 0.4462 -0.0130 -0.0070 0.0124  99  MET   A CB  
758  C  CG  . MET   A 93  ? 0.2229 0.2900 0.4692 -0.0135 -0.0090 0.0141  99  MET   A CG  
759  S  SD  . MET   A 93  ? 0.2772 0.3397 0.5140 -0.0161 -0.0058 0.0107  99  MET   A SD  
760  C  CE  . MET   A 93  ? 0.2346 0.2934 0.4761 -0.0147 -0.0007 0.0108  99  MET   A CE  
761  N  N   . LEU   A 94  ? 0.1969 0.2703 0.4754 -0.0089 -0.0021 0.0134  100 LEU   A N   
762  C  CA  . LEU   A 94  ? 0.2041 0.2740 0.4856 -0.0074 0.0045  0.0123  100 LEU   A CA  
763  C  C   . LEU   A 94  ? 0.2039 0.2749 0.4885 -0.0098 0.0072  0.0106  100 LEU   A C   
764  O  O   . LEU   A 94  ? 0.2004 0.2776 0.4920 -0.0127 0.0032  0.0102  100 LEU   A O   
765  C  CB  . LEU   A 94  ? 0.2133 0.2861 0.5079 -0.0046 0.0069  0.0145  100 LEU   A CB  
766  C  CG  . LEU   A 94  ? 0.2567 0.3269 0.5505 -0.0016 0.0060  0.0163  100 LEU   A CG  
767  C  CD1 . LEU   A 94  ? 0.2701 0.3424 0.5789 0.0016  0.0103  0.0184  100 LEU   A CD1 
768  C  CD2 . LEU   A 94  ? 0.2845 0.3446 0.5648 -0.0003 0.0086  0.0139  100 LEU   A CD2 
769  N  N   . ALA   A 95  ? 0.1991 0.2633 0.4788 -0.0084 0.0140  0.0098  101 ALA   A N   
770  C  CA  . ALA   A 95  ? 0.2018 0.2648 0.4847 -0.0100 0.0190  0.0092  101 ALA   A CA  
771  C  C   . ALA   A 95  ? 0.2063 0.2619 0.4878 -0.0064 0.0288  0.0103  101 ALA   A C   
772  O  O   . ALA   A 95  ? 0.2146 0.2636 0.4868 -0.0029 0.0305  0.0104  101 ALA   A O   
773  C  CB  . ALA   A 95  ? 0.2032 0.2614 0.4742 -0.0115 0.0180  0.0075  101 ALA   A CB  
774  N  N   . VAL   A 96  ? 0.1987 0.2542 0.4891 -0.0073 0.0357  0.0111  102 VAL   A N   
775  C  CA  . VAL   A 96  ? 0.2018 0.2478 0.4880 -0.0037 0.0473  0.0128  102 VAL   A CA  
776  C  C   . VAL   A 96  ? 0.2309 0.2658 0.4961 -0.0028 0.0485  0.0123  102 VAL   A C   
777  O  O   . VAL   A 96  ? 0.2321 0.2680 0.4990 -0.0056 0.0478  0.0122  102 VAL   A O   
778  C  CB  . VAL   A 96  ? 0.2059 0.2566 0.5140 -0.0051 0.0555  0.0147  102 VAL   A CB  
779  C  CG1 . VAL   A 96  ? 0.2342 0.2722 0.5347 -0.0011 0.0704  0.0171  102 VAL   A CG1 
780  C  CG2 . VAL   A 96  ? 0.1970 0.2594 0.5284 -0.0056 0.0525  0.0155  102 VAL   A CG2 
781  N  N   . GLY   A 97  ? 0.2438 0.2673 0.4898 0.0013  0.0498  0.0120  103 GLY   A N   
782  C  CA  . GLY   A 97  ? 0.2742 0.2865 0.4999 0.0029  0.0489  0.0120  103 GLY   A CA  
783  C  C   . GLY   A 97  ? 0.2916 0.2909 0.4960 0.0074  0.0478  0.0107  103 GLY   A C   
784  O  O   . GLY   A 97  ? 0.2911 0.2913 0.4974 0.0087  0.0466  0.0091  103 GLY   A O   
785  N  N   . HIS   A 98  ? 0.2940 0.2804 0.4779 0.0100  0.0475  0.0113  104 HIS   A N   
786  C  CA  . HIS   A 98  ? 0.3049 0.2768 0.4658 0.0143  0.0449  0.0093  104 HIS   A CA  
787  C  C   . HIS   A 98  ? 0.2849 0.2603 0.4453 0.0129  0.0309  0.0060  104 HIS   A C   
788  O  O   . HIS   A 98  ? 0.2790 0.2625 0.4479 0.0100  0.0238  0.0063  104 HIS   A O   
789  C  CB  . HIS   A 98  ? 0.3319 0.2868 0.4684 0.0182  0.0481  0.0114  104 HIS   A CB  
790  C  CG  . HIS   A 98  ? 0.3779 0.3153 0.4868 0.0230  0.0440  0.0087  104 HIS   A CG  
791  N  ND1 . HIS   A 98  ? 0.4128 0.3398 0.5110 0.0264  0.0523  0.0069  104 HIS   A ND1 
792  C  CD2 . HIS   A 98  ? 0.3997 0.3285 0.4915 0.0245  0.0315  0.0069  104 HIS   A CD2 
793  C  CE1 . HIS   A 98  ? 0.4321 0.3434 0.5042 0.0298  0.0444  0.0034  104 HIS   A CE1 
794  N  NE2 . HIS   A 98  ? 0.4276 0.3399 0.4959 0.0287  0.0308  0.0034  104 HIS   A NE2 
795  N  N   . SER   A 99  ? 0.2840 0.2523 0.4353 0.0152  0.0282  0.0028  105 SER   A N   
796  C  CA  . SER   A 99  ? 0.2900 0.2592 0.4412 0.0141  0.0154  -0.0004 105 SER   A CA  
797  C  C   . SER   A 99  ? 0.3173 0.2716 0.4507 0.0177  0.0135  -0.0046 105 SER   A C   
798  O  O   . SER   A 99  ? 0.3227 0.2706 0.4508 0.0203  0.0230  -0.0052 105 SER   A O   
799  C  CB  . SER   A 99  ? 0.2967 0.2827 0.4718 0.0100  0.0119  -0.0003 105 SER   A CB  
800  O  OG  . SER   A 99  ? 0.3114 0.3001 0.4944 0.0105  0.0168  -0.0008 105 SER   A OG  
801  N  N   . GLU   A 100 ? 0.3280 0.2754 0.4517 0.0180  0.0011  -0.0077 106 GLU   A N   
802  C  CA  . GLU   A 100 ? 0.3465 0.2792 0.4538 0.0206  -0.0047 -0.0132 106 GLU   A CA  
803  C  C   . GLU   A 100 ? 0.3445 0.2859 0.4699 0.0170  -0.0168 -0.0159 106 GLU   A C   
804  O  O   . GLU   A 100 ? 0.3331 0.2884 0.4772 0.0136  -0.0209 -0.0131 106 GLU   A O   
805  C  CB  . GLU   A 100 ? 0.3893 0.3028 0.4661 0.0247  -0.0096 -0.0144 106 GLU   A CB  
806  C  CG  . GLU   A 100 ? 0.4414 0.3451 0.5010 0.0285  0.0054  -0.0109 106 GLU   A CG  
807  C  CD  . GLU   A 100 ? 0.5127 0.3957 0.5387 0.0333  0.0028  -0.0103 106 GLU   A CD  
808  O  OE1 . GLU   A 100 ? 0.5299 0.3981 0.5352 0.0355  -0.0089 -0.0154 106 GLU   A OE1 
809  O  OE2 . GLU   A 100 ? 0.5154 0.3961 0.5353 0.0350  0.0120  -0.0047 106 GLU   A OE2 
810  N  N   . PRO   A 101 ? 0.3549 0.2881 0.4766 0.0176  -0.0213 -0.0212 107 PRO   A N   
811  C  CA  . PRO   A 101 ? 0.3458 0.2877 0.4887 0.0139  -0.0311 -0.0230 107 PRO   A CA  
812  C  C   . PRO   A 101 ? 0.3366 0.2854 0.4907 0.0113  -0.0428 -0.0218 107 PRO   A C   
813  O  O   . PRO   A 101 ? 0.3223 0.2857 0.5008 0.0077  -0.0434 -0.0191 107 PRO   A O   
814  C  CB  . PRO   A 101 ? 0.3626 0.2886 0.4926 0.0157  -0.0360 -0.0300 107 PRO   A CB  
815  C  CG  . PRO   A 101 ? 0.3794 0.2948 0.4914 0.0198  -0.0227 -0.0305 107 PRO   A CG  
816  C  CD  . PRO   A 101 ? 0.3589 0.2741 0.4585 0.0217  -0.0163 -0.0257 107 PRO   A CD  
817  N  N   . GLY   A 102 ? 0.3470 0.2847 0.4830 0.0136  -0.0510 -0.0231 108 GLY   A N   
818  C  CA  . GLY   A 102 ? 0.3416 0.2848 0.4890 0.0120  -0.0625 -0.0217 108 GLY   A CA  
819  C  C   . GLY   A 102 ? 0.3301 0.2873 0.4913 0.0104  -0.0559 -0.0152 108 GLY   A C   
820  O  O   . GLY   A 102 ? 0.3265 0.2895 0.5007 0.0092  -0.0633 -0.0134 108 GLY   A O   
821  N  N   . ASP   A 103 ? 0.3068 0.2697 0.4673 0.0104  -0.0421 -0.0120 109 ASP   A N   
822  C  CA  . ASP   A 103 ? 0.2888 0.2646 0.4631 0.0083  -0.0360 -0.0070 109 ASP   A CA  
823  C  C   . ASP   A 103 ? 0.2577 0.2483 0.4575 0.0042  -0.0351 -0.0059 109 ASP   A C   
824  O  O   . ASP   A 103 ? 0.2476 0.2473 0.4585 0.0024  -0.0319 -0.0028 109 ASP   A O   
825  C  CB  . ASP   A 103 ? 0.2904 0.2667 0.4569 0.0093  -0.0230 -0.0043 109 ASP   A CB  
826  C  CG  . ASP   A 103 ? 0.3396 0.3014 0.4818 0.0134  -0.0215 -0.0034 109 ASP   A CG  
827  O  OD1 . ASP   A 103 ? 0.3375 0.2935 0.4729 0.0148  -0.0304 -0.0029 109 ASP   A OD1 
828  O  OD2 . ASP   A 103 ? 0.3331 0.2888 0.4637 0.0155  -0.0111 -0.0028 109 ASP   A OD2 
829  N  N   . CYS   A 104 ? 0.2552 0.2469 0.4635 0.0030  -0.0372 -0.0082 110 CYS   A N   
830  C  CA  . CYS   A 104 ? 0.2471 0.2508 0.4777 -0.0003 -0.0353 -0.0062 110 CYS   A CA  
831  C  C   . CYS   A 104 ? 0.2453 0.2542 0.4907 -0.0019 -0.0405 -0.0047 110 CYS   A C   
832  O  O   . CYS   A 104 ? 0.2591 0.2620 0.5034 -0.0009 -0.0503 -0.0066 110 CYS   A O   
833  C  CB  . CYS   A 104 ? 0.2525 0.2537 0.4896 -0.0009 -0.0378 -0.0088 110 CYS   A CB  
834  S  SG  . CYS   A 104 ? 0.2891 0.2868 0.5160 0.0011  -0.0293 -0.0094 110 CYS   A SG  
835  N  N   . GLY   A 105 ? 0.2248 0.2436 0.4827 -0.0040 -0.0340 -0.0013 111 GLY   A N   
836  C  CA  . GLY   A 105 ? 0.2257 0.2495 0.4992 -0.0052 -0.0358 0.0006  111 GLY   A CA  
837  C  C   . GLY   A 105 ? 0.2329 0.2583 0.5009 -0.0046 -0.0316 0.0027  111 GLY   A C   
838  O  O   . GLY   A 105 ? 0.2334 0.2638 0.5145 -0.0056 -0.0292 0.0047  111 GLY   A O   
839  N  N   . GLY   A 106 ? 0.2298 0.2502 0.4797 -0.0028 -0.0297 0.0022  112 GLY   A N   
840  C  CA  . GLY   A 106 ? 0.2235 0.2446 0.4693 -0.0025 -0.0251 0.0042  112 GLY   A CA  
841  C  C   . GLY   A 106 ? 0.2181 0.2475 0.4715 -0.0052 -0.0164 0.0055  112 GLY   A C   
842  O  O   . GLY   A 106 ? 0.2122 0.2452 0.4655 -0.0065 -0.0129 0.0053  112 GLY   A O   
843  N  N   . ILE   A 107 ? 0.2086 0.2402 0.4688 -0.0058 -0.0136 0.0068  113 ILE   A N   
844  C  CA  . ILE   A 107 ? 0.2146 0.2517 0.4792 -0.0083 -0.0059 0.0071  113 ILE   A CA  
845  C  C   . ILE   A 107 ? 0.2094 0.2469 0.4639 -0.0093 -0.0009 0.0064  113 ILE   A C   
846  O  O   . ILE   A 107 ? 0.2194 0.2530 0.4678 -0.0083 -0.0005 0.0066  113 ILE   A O   
847  C  CB  . ILE   A 107 ? 0.2433 0.2815 0.5201 -0.0084 -0.0035 0.0082  113 ILE   A CB  
848  C  CG1 . ILE   A 107 ? 0.2669 0.3077 0.5595 -0.0086 -0.0049 0.0092  113 ILE   A CG1 
849  C  CG2 . ILE   A 107 ? 0.2530 0.2927 0.5276 -0.0104 0.0050  0.0075  113 ILE   A CG2 
850  C  CD1 . ILE   A 107 ? 0.3004 0.3421 0.6092 -0.0081 -0.0028 0.0107  113 ILE   A CD1 
851  N  N   . LEU   A 108 ? 0.1967 0.2385 0.4509 -0.0115 0.0028  0.0058  114 LEU   A N   
852  C  CA  . LEU   A 108 ? 0.1944 0.2378 0.4435 -0.0133 0.0064  0.0046  114 LEU   A CA  
853  C  C   . LEU   A 108 ? 0.2012 0.2448 0.4521 -0.0152 0.0105  0.0035  114 LEU   A C   
854  O  O   . LEU   A 108 ? 0.1882 0.2327 0.4410 -0.0155 0.0120  0.0041  114 LEU   A O   
855  C  CB  . LEU   A 108 ? 0.2018 0.2490 0.4487 -0.0140 0.0055  0.0046  114 LEU   A CB  
856  C  CG  . LEU   A 108 ? 0.2186 0.2686 0.4637 -0.0164 0.0070  0.0031  114 LEU   A CG  
857  C  CD1 . LEU   A 108 ? 0.2202 0.2687 0.4659 -0.0165 0.0090  0.0026  114 LEU   A CD1 
858  C  CD2 . LEU   A 108 ? 0.2403 0.2947 0.4853 -0.0166 0.0045  0.0041  114 LEU   A CD2 
859  N  N   . ARG   A 109 ? 0.2063 0.2477 0.4562 -0.0163 0.0133  0.0020  115 ARG   A N   
860  C  CA  . ARG   A 109 ? 0.2263 0.2658 0.4764 -0.0179 0.0178  0.0000  115 ARG   A CA  
861  C  C   . ARG   A 109 ? 0.2299 0.2686 0.4754 -0.0208 0.0193  -0.0034 115 ARG   A C   
862  O  O   . ARG   A 109 ? 0.2070 0.2465 0.4535 -0.0213 0.0182  -0.0035 115 ARG   A O   
863  C  CB  . ARG   A 109 ? 0.2631 0.2991 0.5206 -0.0162 0.0203  0.0010  115 ARG   A CB  
864  C  CG  . ARG   A 109 ? 0.3817 0.4143 0.6404 -0.0151 0.0201  0.0018  115 ARG   A CG  
865  C  CD  . ARG   A 109 ? 0.4599 0.4890 0.7276 -0.0136 0.0234  0.0027  115 ARG   A CD  
866  N  NE  . ARG   A 109 ? 0.5169 0.5478 0.7940 -0.0111 0.0200  0.0055  115 ARG   A NE  
867  C  CZ  . ARG   A 109 ? 0.5558 0.5879 0.8421 -0.0110 0.0238  0.0057  115 ARG   A CZ  
868  N  NH1 . ARG   A 109 ? 0.5661 0.5959 0.8492 -0.0127 0.0318  0.0030  115 ARG   A NH1 
869  N  NH2 . ARG   A 109 ? 0.5428 0.5772 0.8415 -0.0091 0.0200  0.0083  115 ARG   A NH2 
870  N  N   . CYS   A 110 ? 0.2342 0.2707 0.4742 -0.0226 0.0217  -0.0063 116 CYS   A N   
871  C  CA  . CYS   A 110 ? 0.2555 0.2898 0.4911 -0.0259 0.0217  -0.0109 116 CYS   A CA  
872  C  C   . CYS   A 110 ? 0.2813 0.3083 0.5159 -0.0263 0.0282  -0.0138 116 CYS   A C   
873  O  O   . CYS   A 110 ? 0.2864 0.3115 0.5262 -0.0238 0.0325  -0.0114 116 CYS   A O   
874  C  CB  . CYS   A 110 ? 0.2611 0.2970 0.4872 -0.0274 0.0175  -0.0125 116 CYS   A CB  
875  S  SG  . CYS   A 110 ? 0.2850 0.3147 0.4985 -0.0262 0.0220  -0.0126 116 CYS   A SG  
876  N  N   . GLN   A 111 ? 0.2984 0.3209 0.5279 -0.0294 0.0287  -0.0192 117 GLN   A N   
877  C  CA  . GLN   A 111 ? 0.3283 0.3420 0.5556 -0.0297 0.0358  -0.0228 117 GLN   A CA  
878  C  C   . GLN   A 111 ? 0.3435 0.3525 0.5625 -0.0277 0.0415  -0.0225 117 GLN   A C   
879  O  O   . GLN   A 111 ? 0.3673 0.3694 0.5879 -0.0266 0.0495  -0.0239 117 GLN   A O   
880  C  CB  . GLN   A 111 ? 0.3676 0.3758 0.5883 -0.0339 0.0342  -0.0300 117 GLN   A CB  
881  C  CG  . GLN   A 111 ? 0.4053 0.4126 0.6106 -0.0359 0.0280  -0.0335 117 GLN   A CG  
882  C  CD  . GLN   A 111 ? 0.4732 0.4748 0.6737 -0.0403 0.0241  -0.0413 117 GLN   A CD  
883  O  OE1 . GLN   A 111 ? 0.5060 0.5133 0.7121 -0.0432 0.0157  -0.0427 117 GLN   A OE1 
884  N  NE2 . GLN   A 111 ? 0.4601 0.4501 0.6522 -0.0411 0.0303  -0.0469 117 GLN   A NE2 
885  N  N   . HIS   A 112 ? 0.3438 0.3559 0.5554 -0.0268 0.0386  -0.0200 118 HIS   A N   
886  C  CA  . HIS   A 112 ? 0.3454 0.3518 0.5488 -0.0248 0.0457  -0.0188 118 HIS   A CA  
887  C  C   . HIS   A 112 ? 0.3486 0.3593 0.5667 -0.0215 0.0496  -0.0125 118 HIS   A C   
888  O  O   . HIS   A 112 ? 0.3658 0.3717 0.5827 -0.0196 0.0580  -0.0109 118 HIS   A O   
889  C  CB  . HIS   A 112 ? 0.3544 0.3589 0.5392 -0.0255 0.0412  -0.0194 118 HIS   A CB  
890  C  CG  . HIS   A 112 ? 0.3631 0.3625 0.5338 -0.0289 0.0355  -0.0262 118 HIS   A CG  
891  N  ND1 . HIS   A 112 ? 0.3681 0.3746 0.5405 -0.0312 0.0243  -0.0269 118 HIS   A ND1 
892  C  CD2 . HIS   A 112 ? 0.3827 0.3703 0.5398 -0.0304 0.0394  -0.0328 118 HIS   A CD2 
893  C  CE1 . HIS   A 112 ? 0.3888 0.3886 0.5500 -0.0342 0.0204  -0.0338 118 HIS   A CE1 
894  N  NE2 . HIS   A 112 ? 0.4062 0.3938 0.5563 -0.0340 0.0291  -0.0381 118 HIS   A NE2 
895  N  N   . GLY   A 113 ? 0.3222 0.3411 0.5539 -0.0208 0.0437  -0.0091 119 GLY   A N   
896  C  CA  . GLY   A 113 ? 0.3054 0.3285 0.5518 -0.0181 0.0443  -0.0040 119 GLY   A CA  
897  C  C   . GLY   A 113 ? 0.2839 0.3142 0.5327 -0.0178 0.0359  -0.0011 119 GLY   A C   
898  O  O   . GLY   A 113 ? 0.2716 0.3047 0.5153 -0.0191 0.0299  -0.0023 119 GLY   A O   
899  N  N   . VAL   A 114 ? 0.2587 0.2915 0.5170 -0.0161 0.0360  0.0027  120 VAL   A N   
900  C  CA  . VAL   A 114 ? 0.2473 0.2854 0.5084 -0.0156 0.0285  0.0050  120 VAL   A CA  
901  C  C   . VAL   A 114 ? 0.2393 0.2782 0.4879 -0.0166 0.0266  0.0051  120 VAL   A C   
902  O  O   . VAL   A 114 ? 0.2469 0.2825 0.4889 -0.0165 0.0315  0.0062  120 VAL   A O   
903  C  CB  . VAL   A 114 ? 0.2474 0.2872 0.5248 -0.0139 0.0284  0.0084  120 VAL   A CB  
904  C  CG1 . VAL   A 114 ? 0.2615 0.3048 0.5401 -0.0136 0.0210  0.0098  120 VAL   A CG1 
905  C  CG2 . VAL   A 114 ? 0.2513 0.2910 0.5427 -0.0125 0.0271  0.0087  120 VAL   A CG2 
906  N  N   . VAL   A 115 ? 0.2160 0.2586 0.4616 -0.0170 0.0198  0.0047  121 VAL   A N   
907  C  CA  . VAL   A 115 ? 0.2165 0.2610 0.4535 -0.0175 0.0166  0.0053  121 VAL   A CA  
908  C  C   . VAL   A 115 ? 0.2242 0.2713 0.4676 -0.0159 0.0139  0.0088  121 VAL   A C   
909  O  O   . VAL   A 115 ? 0.2254 0.2724 0.4646 -0.0154 0.0138  0.0112  121 VAL   A O   
910  C  CB  . VAL   A 115 ? 0.2326 0.2798 0.4665 -0.0190 0.0120  0.0028  121 VAL   A CB  
911  C  CG1 . VAL   A 115 ? 0.2358 0.2865 0.4660 -0.0190 0.0072  0.0041  121 VAL   A CG1 
912  C  CG2 . VAL   A 115 ? 0.2254 0.2693 0.4539 -0.0212 0.0142  -0.0012 121 VAL   A CG2 
913  N  N   . GLY   A 116 ? 0.2062 0.2545 0.4584 -0.0149 0.0109  0.0088  122 GLY   A N   
914  C  CA  . GLY   A 116 ? 0.2159 0.2651 0.4739 -0.0136 0.0077  0.0107  122 GLY   A CA  
915  C  C   . GLY   A 116 ? 0.2112 0.2591 0.4745 -0.0124 0.0033  0.0094  122 GLY   A C   
916  O  O   . GLY   A 116 ? 0.2193 0.2658 0.4839 -0.0123 0.0033  0.0082  122 GLY   A O   
917  N  N   . ILE   A 117 ? 0.1971 0.2442 0.4629 -0.0113 -0.0006 0.0096  123 ILE   A N   
918  C  CA  . ILE   A 117 ? 0.2020 0.2454 0.4686 -0.0099 -0.0061 0.0078  123 ILE   A CA  
919  C  C   . ILE   A 117 ? 0.2095 0.2506 0.4683 -0.0085 -0.0080 0.0066  123 ILE   A C   
920  O  O   . ILE   A 117 ? 0.2024 0.2456 0.4620 -0.0086 -0.0065 0.0078  123 ILE   A O   
921  C  CB  . ILE   A 117 ? 0.2171 0.2591 0.4968 -0.0097 -0.0099 0.0080  123 ILE   A CB  
922  C  CG1 . ILE   A 117 ? 0.2345 0.2775 0.5201 -0.0102 -0.0084 0.0097  123 ILE   A CG1 
923  C  CG2 . ILE   A 117 ? 0.2280 0.2716 0.5189 -0.0104 -0.0077 0.0092  123 ILE   A CG2 
924  C  CD1 . ILE   A 117 ? 0.2607 0.3019 0.5633 -0.0106 -0.0128 0.0094  123 ILE   A CD1 
925  N  N   . VAL   A 118 ? 0.2072 0.2426 0.4580 -0.0067 -0.0108 0.0047  124 VAL   A N   
926  C  CA  . VAL   A 118 ? 0.1957 0.2266 0.4381 -0.0048 -0.0108 0.0034  124 VAL   A CA  
927  C  C   . VAL   A 118 ? 0.1969 0.2259 0.4447 -0.0045 -0.0139 0.0025  124 VAL   A C   
928  O  O   . VAL   A 118 ? 0.1961 0.2231 0.4508 -0.0050 -0.0191 0.0016  124 VAL   A O   
929  C  CB  . VAL   A 118 ? 0.2143 0.2361 0.4440 -0.0024 -0.0130 0.0016  124 VAL   A CB  
930  C  CG1 . VAL   A 118 ? 0.2276 0.2422 0.4468 0.0001  -0.0111 -0.0001 124 VAL   A CG1 
931  C  CG2 . VAL   A 118 ? 0.2183 0.2410 0.4440 -0.0027 -0.0089 0.0031  124 VAL   A CG2 
932  N  N   . SER   A 119 ? 0.1919 0.2219 0.4394 -0.0038 -0.0109 0.0031  125 SER   A N   
933  C  CA  . SER   A 119 ? 0.1953 0.2231 0.4488 -0.0034 -0.0125 0.0027  125 SER   A CA  
934  C  C   . SER   A 119 ? 0.2180 0.2399 0.4645 -0.0008 -0.0104 0.0009  125 SER   A C   
935  O  O   . SER   A 119 ? 0.2304 0.2458 0.4776 0.0002  -0.0129 -0.0015 125 SER   A O   
936  C  CB  . SER   A 119 ? 0.2070 0.2423 0.4706 -0.0048 -0.0097 0.0069  125 SER   A CB  
937  O  OG  . SER   A 119 ? 0.2354 0.2681 0.5064 -0.0044 -0.0105 0.0074  125 SER   A OG  
938  N  N   . THR   A 120 ? 0.2131 0.2373 0.4554 0.0003  -0.0050 0.0020  126 THR   A N   
939  C  CA  . THR   A 120 ? 0.2313 0.2498 0.4694 0.0033  -0.0006 0.0008  126 THR   A CA  
940  C  C   . THR   A 120 ? 0.2389 0.2535 0.4666 0.0049  0.0048  0.0002  126 THR   A C   
941  O  O   . THR   A 120 ? 0.2275 0.2450 0.4528 0.0034  0.0045  0.0011  126 THR   A O   
942  C  CB  . THR   A 120 ? 0.2466 0.2732 0.4975 0.0035  0.0026  0.0046  126 THR   A CB  
943  O  OG1 . THR   A 120 ? 0.2454 0.2809 0.5007 0.0024  0.0051  0.0074  126 THR   A OG1 
944  C  CG2 . THR   A 120 ? 0.2470 0.2774 0.5074 0.0020  -0.0012 0.0070  126 THR   A CG2 
945  N  N   . GLY   A 121 ? 0.2527 0.2596 0.4745 0.0082  0.0109  -0.0012 127 GLY   A N   
946  C  CA  . GLY   A 121 ? 0.2700 0.2721 0.4830 0.0100  0.0183  -0.0008 127 GLY   A CA  
947  C  C   . GLY   A 121 ? 0.3007 0.2906 0.5043 0.0143  0.0263  -0.0028 127 GLY   A C   
948  O  O   . GLY   A 121 ? 0.2939 0.2797 0.4994 0.0158  0.0260  -0.0048 127 GLY   A O   
949  N  N   . GLY   A 122 ? 0.3442 0.3268 0.5369 0.0164  0.0342  -0.0023 128 GLY   A N   
950  C  CA  . GLY   A 122 ? 0.3674 0.3362 0.5488 0.0211  0.0450  -0.0037 128 GLY   A CA  
951  C  C   . GLY   A 122 ? 0.3654 0.3412 0.5627 0.0218  0.0572  0.0004  128 GLY   A C   
952  O  O   . GLY   A 122 ? 0.3407 0.3332 0.5612 0.0187  0.0551  0.0036  128 GLY   A O   
953  N  N   . ASN   A 123 ? 0.3921 0.3541 0.5768 0.0261  0.0700  0.0003  129 ASN   A N   
954  C  CA  . ASN   A 123 ? 0.4025 0.3692 0.6044 0.0273  0.0840  0.0044  129 ASN   A CA  
955  C  C   . ASN   A 123 ? 0.3739 0.3551 0.5933 0.0231  0.0829  0.0084  129 ASN   A C   
956  O  O   . ASN   A 123 ? 0.3756 0.3707 0.6228 0.0214  0.0861  0.0115  129 ASN   A O   
957  C  CB  . ASN   A 123 ? 0.4299 0.4038 0.6544 0.0287  0.0882  0.0052  129 ASN   A CB  
958  C  CG  . ASN   A 123 ? 0.5117 0.4671 0.7188 0.0340  0.0958  0.0013  129 ASN   A CG  
959  O  OD1 . ASN   A 123 ? 0.5638 0.4990 0.7407 0.0374  0.1014  -0.0016 129 ASN   A OD1 
960  N  ND2 . ASN   A 123 ? 0.5097 0.4700 0.7339 0.0351  0.0960  0.0011  129 ASN   A ND2 
961  N  N   . GLY   A 124 ? 0.3484 0.3254 0.5519 0.0216  0.0780  0.0082  130 GLY   A N   
962  C  CA  . GLY   A 124 ? 0.3230 0.3106 0.5401 0.0178  0.0779  0.0113  130 GLY   A CA  
963  C  C   . GLY   A 124 ? 0.2986 0.3041 0.5342 0.0124  0.0653  0.0112  130 GLY   A C   
964  O  O   . GLY   A 124 ? 0.2887 0.3031 0.5371 0.0089  0.0647  0.0129  130 GLY   A O   
965  N  N   . LEU   A 125 ? 0.2839 0.2934 0.5196 0.0119  0.0555  0.0091  131 LEU   A N   
966  C  CA  . LEU   A 125 ? 0.2754 0.2989 0.5236 0.0075  0.0444  0.0092  131 LEU   A CA  
967  C  C   . LEU   A 125 ? 0.2802 0.2992 0.5127 0.0067  0.0349  0.0069  131 LEU   A C   
968  O  O   . LEU   A 125 ? 0.3077 0.3140 0.5222 0.0095  0.0345  0.0047  131 LEU   A O   
969  C  CB  . LEU   A 125 ? 0.2770 0.3094 0.5417 0.0076  0.0416  0.0101  131 LEU   A CB  
970  C  CG  . LEU   A 125 ? 0.3068 0.3452 0.5924 0.0088  0.0494  0.0128  131 LEU   A CG  
971  C  CD1 . LEU   A 125 ? 0.3299 0.3747 0.6294 0.0101  0.0458  0.0141  131 LEU   A CD1 
972  C  CD2 . LEU   A 125 ? 0.2901 0.3387 0.5914 0.0051  0.0491  0.0145  131 LEU   A CD2 
973  N  N   . VAL   A 126 ? 0.2398 0.2687 0.4797 0.0029  0.0273  0.0073  132 VAL   A N   
974  C  CA  . VAL   A 126 ? 0.2360 0.2633 0.4680 0.0017  0.0191  0.0058  132 VAL   A CA  
975  C  C   . VAL   A 126 ? 0.2268 0.2656 0.4713 -0.0012 0.0136  0.0069  132 VAL   A C   
976  O  O   . VAL   A 126 ? 0.2251 0.2722 0.4796 -0.0034 0.0142  0.0082  132 VAL   A O   
977  C  CB  . VAL   A 126 ? 0.2353 0.2580 0.4577 0.0011  0.0182  0.0055  132 VAL   A CB  
978  C  CG1 . VAL   A 126 ? 0.2237 0.2538 0.4557 -0.0019 0.0210  0.0070  132 VAL   A CG1 
979  C  CG2 . VAL   A 126 ? 0.2406 0.2628 0.4599 0.0001  0.0096  0.0043  132 VAL   A CG2 
980  N  N   . GLY   A 127 ? 0.2131 0.2511 0.4569 -0.0010 0.0087  0.0064  133 GLY   A N   
981  C  CA  . GLY   A 127 ? 0.1940 0.2401 0.4463 -0.0030 0.0048  0.0082  133 GLY   A CA  
982  C  C   . GLY   A 127 ? 0.1876 0.2330 0.4371 -0.0047 0.0008  0.0077  133 GLY   A C   
983  O  O   . GLY   A 127 ? 0.1976 0.2362 0.4421 -0.0038 -0.0013 0.0059  133 GLY   A O   
984  N  N   . PHE   A 128 ? 0.1681 0.2194 0.4211 -0.0070 -0.0004 0.0093  134 PHE   A N   
985  C  CA  . PHE   A 128 ? 0.1820 0.2328 0.4344 -0.0085 -0.0017 0.0093  134 PHE   A CA  
986  C  C   . PHE   A 128 ? 0.1943 0.2474 0.4502 -0.0089 -0.0022 0.0122  134 PHE   A C   
987  O  O   . PHE   A 128 ? 0.1963 0.2533 0.4517 -0.0092 -0.0024 0.0142  134 PHE   A O   
988  C  CB  . PHE   A 128 ? 0.1803 0.2333 0.4303 -0.0106 -0.0002 0.0085  134 PHE   A CB  
989  C  CG  . PHE   A 128 ? 0.1937 0.2443 0.4408 -0.0102 0.0017  0.0069  134 PHE   A CG  
990  C  CD1 . PHE   A 128 ? 0.2102 0.2550 0.4533 -0.0091 0.0013  0.0059  134 PHE   A CD1 
991  C  CD2 . PHE   A 128 ? 0.2085 0.2623 0.4581 -0.0108 0.0037  0.0069  134 PHE   A CD2 
992  C  CE1 . PHE   A 128 ? 0.2212 0.2620 0.4594 -0.0082 0.0041  0.0055  134 PHE   A CE1 
993  C  CE2 . PHE   A 128 ? 0.2119 0.2626 0.4599 -0.0105 0.0074  0.0062  134 PHE   A CE2 
994  C  CZ  . PHE   A 128 ? 0.2134 0.2569 0.4541 -0.0090 0.0081  0.0057  134 PHE   A CZ  
995  N  N   . ALA   A 129 ? 0.1955 0.2459 0.4552 -0.0089 -0.0025 0.0127  135 ALA   A N   
996  C  CA  . ALA   A 129 ? 0.2125 0.2634 0.4756 -0.0092 -0.0008 0.0162  135 ALA   A CA  
997  C  C   . ALA   A 129 ? 0.2129 0.2647 0.4712 -0.0107 0.0024  0.0169  135 ALA   A C   
998  O  O   . ALA   A 129 ? 0.2137 0.2643 0.4744 -0.0116 0.0038  0.0153  135 ALA   A O   
999  C  CB  . ALA   A 129 ? 0.2112 0.2585 0.4839 -0.0090 -0.0014 0.0163  135 ALA   A CB  
1000 N  N   . ASP   A 130 ? 0.2053 0.2583 0.4560 -0.0109 0.0030  0.0191  136 ASP   A N   
1001 C  CA  . ASP   A 130 ? 0.2082 0.2595 0.4504 -0.0121 0.0063  0.0189  136 ASP   A CA  
1002 C  C   . ASP   A 130 ? 0.2163 0.2633 0.4615 -0.0118 0.0126  0.0215  136 ASP   A C   
1003 O  O   . ASP   A 130 ? 0.2179 0.2634 0.4687 -0.0107 0.0140  0.0252  136 ASP   A O   
1004 C  CB  . ASP   A 130 ? 0.2345 0.2860 0.4654 -0.0119 0.0038  0.0208  136 ASP   A CB  
1005 C  CG  . ASP   A 130 ? 0.3057 0.3532 0.5232 -0.0132 0.0060  0.0192  136 ASP   A CG  
1006 O  OD1 . ASP   A 130 ? 0.3030 0.3506 0.5207 -0.0149 0.0069  0.0149  136 ASP   A OD1 
1007 O  OD2 . ASP   A 130 ? 0.3644 0.4072 0.5698 -0.0122 0.0071  0.0222  136 ASP   A OD2 
1008 N  N   . VAL   A 131 ? 0.2110 0.2554 0.4541 -0.0128 0.0174  0.0199  137 VAL   A N   
1009 C  CA  . VAL   A 131 ? 0.2325 0.2723 0.4797 -0.0122 0.0258  0.0229  137 VAL   A CA  
1010 C  C   . VAL   A 131 ? 0.2613 0.2948 0.4914 -0.0123 0.0321  0.0229  137 VAL   A C   
1011 O  O   . VAL   A 131 ? 0.2788 0.3067 0.5095 -0.0114 0.0414  0.0256  137 VAL   A O   
1012 C  CB  . VAL   A 131 ? 0.2274 0.2684 0.4929 -0.0126 0.0276  0.0216  137 VAL   A CB  
1013 C  CG1 . VAL   A 131 ? 0.2278 0.2723 0.5062 -0.0124 0.0202  0.0210  137 VAL   A CG1 
1014 C  CG2 . VAL   A 131 ? 0.2263 0.2676 0.4895 -0.0135 0.0276  0.0175  137 VAL   A CG2 
1015 N  N   . ARG   A 132 ? 0.2678 0.3012 0.4831 -0.0133 0.0275  0.0195  138 ARG   A N   
1016 C  CA  . ARG   A 132 ? 0.2753 0.3011 0.4716 -0.0135 0.0317  0.0177  138 ARG   A CA  
1017 C  C   . ARG   A 132 ? 0.3033 0.3207 0.4829 -0.0115 0.0363  0.0225  138 ARG   A C   
1018 O  O   . ARG   A 132 ? 0.3268 0.3345 0.4903 -0.0110 0.0435  0.0215  138 ARG   A O   
1019 C  CB  . ARG   A 132 ? 0.2536 0.2814 0.4404 -0.0155 0.0234  0.0125  138 ARG   A CB  
1020 C  CG  . ARG   A 132 ? 0.2304 0.2633 0.4303 -0.0172 0.0218  0.0083  138 ARG   A CG  
1021 C  CD  . ARG   A 132 ? 0.2506 0.2855 0.4443 -0.0195 0.0144  0.0038  138 ARG   A CD  
1022 N  NE  . ARG   A 132 ? 0.2381 0.2799 0.4367 -0.0191 0.0063  0.0059  138 ARG   A NE  
1023 C  CZ  . ARG   A 132 ? 0.2613 0.3074 0.4615 -0.0209 -0.0008 0.0032  138 ARG   A CZ  
1024 N  NH1 . ARG   A 132 ? 0.2541 0.2980 0.4509 -0.0235 -0.0015 -0.0020 138 ARG   A NH1 
1025 N  NH2 . ARG   A 132 ? 0.2363 0.2889 0.4443 -0.0200 -0.0065 0.0057  138 ARG   A NH2 
1026 N  N   . ASP   A 133 ? 0.2902 0.3097 0.4719 -0.0099 0.0329  0.0277  139 ASP   A N   
1027 C  CA  . ASP   A 133 ? 0.3110 0.3213 0.4762 -0.0074 0.0378  0.0337  139 ASP   A CA  
1028 C  C   . ASP   A 133 ? 0.3292 0.3340 0.5041 -0.0059 0.0517  0.0387  139 ASP   A C   
1029 O  O   . ASP   A 133 ? 0.3521 0.3467 0.5121 -0.0035 0.0594  0.0443  139 ASP   A O   
1030 C  CB  . ASP   A 133 ? 0.3248 0.3391 0.4905 -0.0059 0.0290  0.0381  139 ASP   A CB  
1031 C  CG  . ASP   A 133 ? 0.3786 0.4000 0.5694 -0.0058 0.0291  0.0405  139 ASP   A CG  
1032 O  OD1 . ASP   A 133 ? 0.3640 0.3917 0.5717 -0.0077 0.0281  0.0361  139 ASP   A OD1 
1033 O  OD2 . ASP   A 133 ? 0.3883 0.4073 0.5807 -0.0036 0.0302  0.0468  139 ASP   A OD2 
1034 N  N   . LEU   A 134 ? 0.3145 0.3255 0.5153 -0.0072 0.0545  0.0373  140 LEU   A N   
1035 C  CA  . LEU   A 134 ? 0.3211 0.3289 0.5386 -0.0064 0.0665  0.0419  140 LEU   A CA  
1036 C  C   . LEU   A 134 ? 0.3331 0.3328 0.5447 -0.0059 0.0792  0.0408  140 LEU   A C   
1037 O  O   . LEU   A 134 ? 0.3210 0.3245 0.5511 -0.0070 0.0820  0.0379  140 LEU   A O   
1038 C  CB  . LEU   A 134 ? 0.3019 0.3196 0.5502 -0.0080 0.0614  0.0402  140 LEU   A CB  
1039 C  CG  . LEU   A 134 ? 0.3029 0.3269 0.5561 -0.0082 0.0499  0.0404  140 LEU   A CG  
1040 C  CD1 . LEU   A 134 ? 0.2947 0.3257 0.5724 -0.0097 0.0440  0.0372  140 LEU   A CD1 
1041 C  CD2 . LEU   A 134 ? 0.3101 0.3291 0.5599 -0.0063 0.0536  0.0474  140 LEU   A CD2 
1042 N  N   . LEU   A 135 ? 0.3503 0.3376 0.5335 -0.0039 0.0862  0.0429  141 LEU   A N   
1043 C  CA  . LEU   A 135 ? 0.3720 0.3483 0.5422 -0.0029 0.0992  0.0412  141 LEU   A CA  
1044 C  C   . LEU   A 135 ? 0.3737 0.3480 0.5686 -0.0020 0.1153  0.0450  141 LEU   A C   
1045 O  O   . LEU   A 135 ? 0.3694 0.3402 0.5685 -0.0019 0.1242  0.0418  141 LEU   A O   
1046 C  CB  . LEU   A 135 ? 0.3997 0.3603 0.5310 -0.0002 0.1034  0.0437  141 LEU   A CB  
1047 C  CG  . LEU   A 135 ? 0.4406 0.4024 0.5483 -0.0009 0.0868  0.0403  141 LEU   A CG  
1048 C  CD1 . LEU   A 135 ? 0.4887 0.4325 0.5555 0.0019  0.0906  0.0419  141 LEU   A CD1 
1049 C  CD2 . LEU   A 135 ? 0.4341 0.4044 0.5470 -0.0044 0.0760  0.0310  141 LEU   A CD2 
1050 N  N   . TRP   A 136 ? 0.3726 0.3492 0.5865 -0.0013 0.1190  0.0518  142 TRP   A N   
1051 C  CA  . TRP   A 136 ? 0.3820 0.3581 0.6257 -0.0008 0.1333  0.0563  142 TRP   A CA  
1052 C  C   . TRP   A 136 ? 0.3842 0.3725 0.6620 -0.0032 0.1282  0.0517  142 TRP   A C   
1053 O  O   . TRP   A 136 ? 0.3891 0.3765 0.6905 -0.0026 0.1405  0.0538  142 TRP   A O   
1054 C  CB  . TRP   A 136 ? 0.3761 0.3522 0.6340 -0.0002 0.1363  0.0643  142 TRP   A CB  
1055 C  CG  . TRP   A 136 ? 0.3667 0.3545 0.6361 -0.0022 0.1186  0.0627  142 TRP   A CG  
1056 C  CD1 . TRP   A 136 ? 0.3810 0.3684 0.6297 -0.0016 0.1083  0.0637  142 TRP   A CD1 
1057 C  CD2 . TRP   A 136 ? 0.3514 0.3514 0.6560 -0.0049 0.1096  0.0600  142 TRP   A CD2 
1058 N  NE1 . TRP   A 136 ? 0.3730 0.3713 0.6420 -0.0035 0.0954  0.0617  142 TRP   A NE1 
1059 C  CE2 . TRP   A 136 ? 0.3559 0.3614 0.6569 -0.0057 0.0954  0.0589  142 TRP   A CE2 
1060 C  CE3 . TRP   A 136 ? 0.3443 0.3506 0.6831 -0.0065 0.1117  0.0583  142 TRP   A CE3 
1061 C  CZ2 . TRP   A 136 ? 0.3494 0.3644 0.6756 -0.0079 0.0840  0.0556  142 TRP   A CZ2 
1062 C  CZ3 . TRP   A 136 ? 0.3406 0.3571 0.7050 -0.0088 0.0983  0.0552  142 TRP   A CZ3 
1063 C  CH2 . TRP   A 136 ? 0.3411 0.3609 0.6972 -0.0095 0.0850  0.0536  142 TRP   A CH2 
1064 N  N   . LEU   A 137 ? 0.3834 0.3824 0.6641 -0.0054 0.1108  0.0458  143 LEU   A N   
1065 C  CA  . LEU   A 137 ? 0.3868 0.3955 0.6953 -0.0069 0.1049  0.0418  143 LEU   A CA  
1066 C  C   . LEU   A 137 ? 0.4309 0.4346 0.7410 -0.0059 0.1163  0.0396  143 LEU   A C   
1067 O  O   . LEU   A 137 ? 0.4138 0.4236 0.7534 -0.0062 0.1166  0.0390  143 LEU   A O   
1068 C  CB  . LEU   A 137 ? 0.3727 0.3897 0.6745 -0.0087 0.0868  0.0360  143 LEU   A CB  
1069 C  CG  . LEU   A 137 ? 0.3612 0.3844 0.6690 -0.0097 0.0749  0.0368  143 LEU   A CG  
1070 C  CD1 . LEU   A 137 ? 0.3574 0.3866 0.6552 -0.0108 0.0601  0.0313  143 LEU   A CD1 
1071 C  CD2 . LEU   A 137 ? 0.3571 0.3857 0.6996 -0.0105 0.0733  0.0386  143 LEU   A CD2 
1072 N  N   . ASP   A 138 ? 0.4796 0.4716 0.7579 -0.0045 0.1251  0.0384  144 ASP   A N   
1073 C  CA  . ASP   A 138 ? 0.5373 0.5210 0.8094 -0.0032 0.1373  0.0354  144 ASP   A CA  
1074 C  C   . ASP   A 138 ? 0.5811 0.5552 0.8633 -0.0005 0.1590  0.0407  144 ASP   A C   
1075 O  O   . ASP   A 138 ? 0.5935 0.5581 0.8671 0.0011  0.1714  0.0383  144 ASP   A O   
1076 C  CB  . ASP   A 138 ? 0.5921 0.5646 0.8215 -0.0029 0.1366  0.0310  144 ASP   A CB  
1077 C  CG  . ASP   A 138 ? 0.6857 0.6650 0.9056 -0.0054 0.1197  0.0242  144 ASP   A CG  
1078 O  OD1 . ASP   A 138 ? 0.7062 0.6970 0.9504 -0.0068 0.1111  0.0224  144 ASP   A OD1 
1079 O  OD2 . ASP   A 138 ? 0.7350 0.7076 0.9233 -0.0058 0.1148  0.0209  144 ASP   A OD2 
1080 N  N   . GLU   A 139 ? 0.6036 0.5781 0.9019 0.0001  0.1653  0.0479  145 GLU   A N   
1081 C  CA  . GLU   A 139 ? 0.6402 0.6046 0.9494 0.0028  0.1885  0.0539  145 GLU   A CA  
1082 C  C   . GLU   A 139 ? 0.6424 0.6159 0.9960 0.0020  0.1909  0.0601  145 GLU   A C   
1083 O  O   . GLU   A 139 ? 0.6373 0.6250 1.0246 -0.0003 0.1784  0.0579  145 GLU   A O   
1084 C  CB  . GLU   A 139 ? 0.7062 0.6524 0.9731 0.0056  0.2005  0.0575  145 GLU   A CB  
1085 C  CG  . GLU   A 139 ? 0.7829 0.7311 1.0379 0.0049  0.1899  0.0617  145 GLU   A CG  
1086 C  CD  . GLU   A 139 ? 0.9127 0.8450 1.1171 0.0074  0.1917  0.0628  145 GLU   A CD  
1087 O  OE1 . GLU   A 139 ? 0.9414 0.8675 1.1362 0.0091  0.1956  0.0703  145 GLU   A OE1 
1088 O  OE2 . GLU   A 139 ? 0.9584 0.8837 1.1328 0.0076  0.1887  0.0561  145 GLU   A OE2 
1089 N  N1  . A1B36 B .   ? 0.2474 0.2652 0.5185 -0.0005 -0.0118 0.0024  201 A1B36 A N1  
1090 C  C4  . A1B36 B .   ? 0.4950 0.4374 0.6405 0.0213  0.0165  -0.0172 201 A1B36 A C4  
1091 C  C5  . A1B36 B .   ? 0.4253 0.3747 0.5875 0.0189  0.0102  -0.0183 201 A1B36 A C5  
1092 C  C6  . A1B36 B .   ? 0.3661 0.3292 0.5447 0.0146  0.0017  -0.0159 201 A1B36 A C6  
1093 C  C7  . A1B36 B .   ? 0.3322 0.3028 0.5301 0.0124  -0.0021 -0.0155 201 A1B36 A C7  
1094 C  C8  . A1B36 B .   ? 0.3231 0.2892 0.5220 0.0103  -0.0138 -0.0193 201 A1B36 A C8  
1095 C  C10 . A1B36 B .   ? 0.2955 0.2823 0.5459 0.0021  -0.0242 -0.0140 201 A1B36 A C10 
1096 C  C13 . A1B36 B .   ? 0.2872 0.2790 0.5227 0.0057  -0.0114 -0.0100 201 A1B36 A C13 
1097 O  O1  . A1B36 B .   ? 0.2502 0.2559 0.5206 0.0031  -0.0095 -0.0013 201 A1B36 A O1  
1098 C  C12 . A1B36 B .   ? 0.2565 0.2647 0.5221 0.0015  -0.0124 -0.0020 201 A1B36 A C12 
1099 C  C11 . A1B36 B .   ? 0.2768 0.2753 0.5278 0.0023  -0.0170 -0.0080 201 A1B36 A C11 
1100 C  C9  . A1B36 B .   ? 0.3037 0.2789 0.5318 0.0045  -0.0271 -0.0192 201 A1B36 A C9  
1101 N  N   . A1B36 B .   ? 0.3021 0.2795 0.5216 0.0070  -0.0171 -0.0164 201 A1B36 A N   
1102 O  O   . A1B36 B .   ? 0.3389 0.2911 0.5210 0.0116  -0.0198 -0.0247 201 A1B36 A O   
1103 C  C1  . A1B36 B .   ? 0.3480 0.3175 0.5258 0.0129  -0.0008 -0.0131 201 A1B36 A C1  
1104 S  S   . A1B36 B .   ? 0.3051 0.2893 0.5024 0.0081  -0.0096 -0.0105 201 A1B36 A S   
1105 C  C   . A1B36 B .   ? 0.2905 0.2798 0.4841 0.0072  -0.0084 -0.0072 201 A1B36 A C   
1106 BR BR  . A1B36 B .   ? 0.6425 0.5641 0.7651 0.0277  0.0318  -0.0197 201 A1B36 A BR  
1107 C  C3  . A1B36 B .   ? 0.4376 0.3866 0.5831 0.0194  0.0138  -0.0139 201 A1B36 A C3  
1108 C  C2  . A1B36 B .   ? 0.3808 0.3436 0.5429 0.0152  0.0049  -0.0121 201 A1B36 A C2  
# 
