data_7HVE
# 
_entry.id   7HVE 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7HVE         pdb_00007hve 10.2210/pdb7hve/pdb 
WWPDB D_1001407979 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.entry_id                        7HVE 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-01-10 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                                         15892.732 
1  3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-{[(4R)-2-methyl-5,6,7,8-tetrahydroimidazo[1,2-a]pyridin-3-yl]acetyl}piperidine-3-carboxamide' 304.387   
1  ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                            65.409    
1  ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                  78.133    
3  ?         ? ? ? 
5 water       nat water                                                                                                 18.015    
74 ?         ? ? ? 
# 
_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-{[(4R)-2-methyl-5,6,7,8-tetrahydroimidazo[1,2-a]pyridin-3-yl]acetyl}piperidine-3-carboxamide' A1BOC 
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 
A1BOC non-polymer         . '(3S)-1-{[(4R)-2-methyl-5,6,7,8-tetrahydroimidazo[1,2-a]pyridin-3-yl]acetyl}piperidine-3-carboxamide' 
? 'C16 H24 N4 O2'  304.387 
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        A1BOC 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1BOC 
_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 A1BOC 1  201 201 A1BOC LIG A . 
C 3 ZN    1  202 1   ZN    ZN  A . 
D 4 DMS   1  203 2   DMS   DMS A . 
E 4 DMS   1  204 6   DMS   DMS A . 
F 4 DMS   1  205 7   DMS   DMS A . 
G 5 HOH   1  301 76  HOH   HOH A . 
G 5 HOH   2  302 9   HOH   HOH A . 
G 5 HOH   3  303 15  HOH   HOH A . 
G 5 HOH   4  304 1   HOH   HOH A . 
G 5 HOH   5  305 54  HOH   HOH A . 
G 5 HOH   6  306 26  HOH   HOH A . 
G 5 HOH   7  307 66  HOH   HOH A . 
G 5 HOH   8  308 12  HOH   HOH A . 
G 5 HOH   9  309 10  HOH   HOH A . 
G 5 HOH   10 310 28  HOH   HOH A . 
G 5 HOH   11 311 37  HOH   HOH A . 
G 5 HOH   12 312 11  HOH   HOH A . 
G 5 HOH   13 313 69  HOH   HOH A . 
G 5 HOH   14 314 16  HOH   HOH A . 
G 5 HOH   15 315 27  HOH   HOH A . 
G 5 HOH   16 316 3   HOH   HOH A . 
G 5 HOH   17 317 64  HOH   HOH A . 
G 5 HOH   18 318 74  HOH   HOH A . 
G 5 HOH   19 319 60  HOH   HOH A . 
G 5 HOH   20 320 38  HOH   HOH A . 
G 5 HOH   21 321 41  HOH   HOH A . 
G 5 HOH   22 322 14  HOH   HOH A . 
G 5 HOH   23 323 43  HOH   HOH A . 
G 5 HOH   24 324 55  HOH   HOH A . 
G 5 HOH   25 325 42  HOH   HOH A . 
G 5 HOH   26 326 70  HOH   HOH A . 
G 5 HOH   27 327 45  HOH   HOH A . 
G 5 HOH   28 328 40  HOH   HOH A . 
G 5 HOH   29 329 53  HOH   HOH A . 
G 5 HOH   30 330 52  HOH   HOH A . 
G 5 HOH   31 331 18  HOH   HOH A . 
G 5 HOH   32 332 17  HOH   HOH A . 
G 5 HOH   33 333 25  HOH   HOH A . 
G 5 HOH   34 334 4   HOH   HOH A . 
G 5 HOH   35 335 56  HOH   HOH A . 
G 5 HOH   36 336 31  HOH   HOH A . 
G 5 HOH   37 337 62  HOH   HOH A . 
G 5 HOH   38 338 65  HOH   HOH A . 
G 5 HOH   39 339 33  HOH   HOH A . 
G 5 HOH   40 340 63  HOH   HOH A . 
G 5 HOH   41 341 29  HOH   HOH A . 
G 5 HOH   42 342 51  HOH   HOH A . 
G 5 HOH   43 343 68  HOH   HOH A . 
G 5 HOH   44 344 13  HOH   HOH A . 
G 5 HOH   45 345 61  HOH   HOH A . 
G 5 HOH   46 346 39  HOH   HOH A . 
G 5 HOH   47 347 19  HOH   HOH A . 
G 5 HOH   48 348 5   HOH   HOH A . 
G 5 HOH   49 349 71  HOH   HOH A . 
G 5 HOH   50 350 57  HOH   HOH A . 
G 5 HOH   51 351 22  HOH   HOH A . 
G 5 HOH   52 352 58  HOH   HOH A . 
G 5 HOH   53 353 6   HOH   HOH A . 
G 5 HOH   54 354 7   HOH   HOH A . 
G 5 HOH   55 355 75  HOH   HOH A . 
G 5 HOH   56 356 32  HOH   HOH A . 
G 5 HOH   57 357 24  HOH   HOH A . 
G 5 HOH   58 358 8   HOH   HOH A . 
G 5 HOH   59 359 59  HOH   HOH A . 
G 5 HOH   60 360 73  HOH   HOH A . 
G 5 HOH   61 361 79  HOH   HOH A . 
G 5 HOH   62 362 50  HOH   HOH A . 
G 5 HOH   63 363 34  HOH   HOH A . 
G 5 HOH   64 364 35  HOH   HOH A . 
G 5 HOH   65 365 80  HOH   HOH A . 
G 5 HOH   66 366 30  HOH   HOH A . 
G 5 HOH   67 367 78  HOH   HOH A . 
G 5 HOH   68 368 77  HOH   HOH A . 
G 5 HOH   69 369 44  HOH   HOH A . 
G 5 HOH   70 370 23  HOH   HOH A . 
G 5 HOH   71 371 21  HOH   HOH A . 
G 5 HOH   72 372 20  HOH   HOH A . 
G 5 HOH   73 373 72  HOH   HOH A . 
G 5 HOH   74 374 2   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           7HVE 
_cell.length_a           74.325 
_cell.length_b           61.113 
_cell.length_c           32.564 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.60 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HVE 
_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          7HVE 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.32 
_exptl_crystal.density_percent_sol   47.08 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2024-11-13 
_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   0.92202 
_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        0.92202 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HVE 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             37.12 
_reflns.d_resolution_high            1.62 
_reflns.number_obs                   18366 
_reflns.percent_possible_obs         98.5 
_reflns.pdbx_Rmerge_I_obs            0.194 
_reflns.pdbx_netI_over_sigmaI        5.2 
_reflns.pdbx_redundancy              7.0 
_reflns.pdbx_Rrim_I_all              0.209 
_reflns.pdbx_Rpim_I_all              0.079 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     128618 
_reflns.pdbx_chi_squared             0.73 
_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                  1.62 
_reflns_shell.d_res_low                   1.70 
_reflns_shell.number_measured_all         18646 
_reflns_shell.number_unique_obs           2640 
_reflns_shell.Rmerge_I_obs                3.221 
_reflns_shell.pdbx_chi_squared            0.57 
_reflns_shell.pdbx_redundancy             7.1 
_reflns_shell.percent_possible_obs        97.4 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.5 
_reflns_shell.pdbx_Rrim_I_all             3.475 
_reflns_shell.pdbx_Rpim_I_all             1.295 
_reflns_shell.pdbx_CC_half                0.376 
_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                                 7HVE 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     17765 
_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                             37.12 
_refine.ls_d_res_high                            1.617 
_refine.ls_percent_reflns_obs                    95.1 
_refine.ls_R_factor_obs                          0.2680 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2662 
_refine.ls_R_factor_R_free                       0.3082 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.480 
_refine.ls_number_reflns_R_free                  795 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.947 
_refine.correlation_coeff_Fo_to_Fc_free          0.922 
_refine.B_iso_mean                               36.06 
_refine.aniso_B[1][1]                            -0.28520 
_refine.aniso_B[2][2]                            0.15830 
_refine.aniso_B[3][3]                            0.12690 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.34310 
_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             0.131 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.130 
_refine.pdbx_overall_SU_R_Blow_DPI               0.133 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.131 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7HVE 
_refine_analyze.Luzzati_coordinate_error_obs    0.33 
_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         31 
_refine_hist.number_atoms_solvent             74 
_refine_hist.number_atoms_total               1179 
_refine_hist.d_res_high                       1.617 
_refine_hist.d_res_low                        37.12 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.010 ? 2.00  1137 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.96  ? 2.00  1546 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  381  'X-RAY DIFFRACTION' SINUSOIDAL   
t_incorr_chiral_ct        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_pseud_angle             ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_trig_c_planes           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_gen_planes              ?     ? 5.00  204  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1134 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.62  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.62 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  '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  870  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   40 
_refine_ls_shell.d_res_high                       1.62 
_refine_ls_shell.d_res_low                        1.64 
_refine_ls_shell.number_reflns_R_work             442 
_refine_ls_shell.R_factor_R_work                  0.5104 
_refine_ls_shell.percent_reflns_obs               64.79 
_refine_ls_shell.R_factor_R_free                  0.4830 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.07 
_refine_ls_shell.number_reflns_R_free             14 
_refine_ls_shell.number_reflns_all                456 
_refine_ls_shell.R_factor_all                     0.5095 
# 
_struct.entry_id                  7HVE 
_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-0032371-001 (A71EV2A-x3489)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HVE 
_struct_keywords.pdbx_keywords   HYDROLASE 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN, HYDROLASE
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G 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              7HVE 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G 
# 
_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 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
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 
disulf1 disulf ? ? A CYS 50  SG  ? ? ? 1_555 A CYS 52 SG ? ? A CYS 56  A CYS 58  1_555 ? ? ? ? ? ? ? 2.726 ? ? 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN  .  ZN ? ? A CYS 56  A ZN  202 1_555 ? ? ? ? ? ? ? 2.624 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN  .  ZN ? ? A CYS 58  A ZN  202 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN  .  ZN ? ? A CYS 116 A ZN  202 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN  .  ZN ? ? A HIS 118 A ZN  202 1_555 ? ? ? ? ? ? ? 2.586 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
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 69.7  ? 
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 97.8  ? 
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_555 105.0 ? 
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_555 118.4 ? 
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_555 127.1 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 123.3 ? 
# 
_pdbx_modification_feature.ordinal                            1 
_pdbx_modification_feature.label_comp_id                      CYS 
_pdbx_modification_feature.label_asym_id                      A 
_pdbx_modification_feature.label_seq_id                       50 
_pdbx_modification_feature.label_alt_id                       ? 
_pdbx_modification_feature.modified_residue_label_comp_id     CYS 
_pdbx_modification_feature.modified_residue_label_asym_id     A 
_pdbx_modification_feature.modified_residue_label_seq_id      52 
_pdbx_modification_feature.modified_residue_label_alt_id      ? 
_pdbx_modification_feature.auth_comp_id                       CYS 
_pdbx_modification_feature.auth_asym_id                       A 
_pdbx_modification_feature.auth_seq_id                        56 
_pdbx_modification_feature.PDB_ins_code                       ? 
_pdbx_modification_feature.symmetry                           1_555 
_pdbx_modification_feature.modified_residue_auth_comp_id      CYS 
_pdbx_modification_feature.modified_residue_auth_asym_id      A 
_pdbx_modification_feature.modified_residue_auth_seq_id       58 
_pdbx_modification_feature.modified_residue_PDB_ins_code      ? 
_pdbx_modification_feature.modified_residue_symmetry          1_555 
_pdbx_modification_feature.comp_id_linking_atom               SG 
_pdbx_modification_feature.modified_residue_id_linking_atom   SG 
_pdbx_modification_feature.modified_residue_id                . 
_pdbx_modification_feature.ref_pcm_id                         . 
_pdbx_modification_feature.ref_comp_id                        . 
_pdbx_modification_feature.type                               None 
_pdbx_modification_feature.category                           'Disulfide bridge' 
# 
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 LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
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 GLY A 116 ? O GLY A 122 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7HVE 
_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   Y 
# 
_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         15.6205 
_pdbx_refine_tls.origin_y         7.0798 
_pdbx_refine_tls.origin_z         14.1714 
_pdbx_refine_tls.T[1][1]          0.1703 
_pdbx_refine_tls.T[2][2]          -0.2240 
_pdbx_refine_tls.T[3][3]          -0.1705 
_pdbx_refine_tls.T[1][2]          -0.0611 
_pdbx_refine_tls.T[1][3]          -0.1380 
_pdbx_refine_tls.T[2][3]          0.0249 
_pdbx_refine_tls.L[1][1]          6.2977 
_pdbx_refine_tls.L[2][2]          2.2241 
_pdbx_refine_tls.L[3][3]          0.1565 
_pdbx_refine_tls.L[1][2]          2.3796 
_pdbx_refine_tls.L[1][3]          -0.5406 
_pdbx_refine_tls.L[2][3]          -0.5293 
_pdbx_refine_tls.S[1][1]          -0.5058 
_pdbx_refine_tls.S[1][2]          0.1789 
_pdbx_refine_tls.S[1][3]          0.6962 
_pdbx_refine_tls.S[2][1]          -0.0716 
_pdbx_refine_tls.S[2][2]          0.2758 
_pdbx_refine_tls.S[2][3]          0.1738 
_pdbx_refine_tls.S[3][1]          0.0527 
_pdbx_refine_tls.S[3][2]          -0.1262 
_pdbx_refine_tls.S[3][3]          0.2299 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
6 1 N 0 A DMS 203 ? D DMS ?   
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1BOC N1   N  Y N 1   
A1BOC N3   N  N N 2   
A1BOC C4   C  N N 3   
A1BOC C5   C  N N 4   
A1BOC C6   C  N N 5   
A1BOC C7   C  N N 6   
A1BOC C8   C  N N 7   
A1BOC C10  C  N N 8   
A1BOC C13  C  N N 9   
A1BOC C15  C  N N 10  
A1BOC O1   O  N N 11  
A1BOC C9   C  N S 12  
A1BOC C11  C  N N 13  
A1BOC N2   N  N N 14  
A1BOC O    O  N N 15  
A1BOC C3   C  Y N 16  
A1BOC C1   C  Y N 17  
A1BOC C    C  N N 18  
A1BOC C12  C  N N 19  
A1BOC C14  C  N N 20  
A1BOC C2   C  Y N 21  
A1BOC N    N  Y N 22  
A1BOC H13  H  N N 23  
A1BOC H12  H  N N 24  
A1BOC H4   H  N N 25  
A1BOC H5   H  N N 26  
A1BOC H6   H  N N 27  
A1BOC H7   H  N N 28  
A1BOC H8   H  N N 29  
A1BOC H9   H  N N 30  
A1BOC H10  H  N N 31  
A1BOC H11  H  N N 32  
A1BOC H18  H  N N 33  
A1BOC H19  H  N N 34  
A1BOC H22  H  N N 35  
A1BOC H23  H  N N 36  
A1BOC H    H  N N 37  
A1BOC H14  H  N N 38  
A1BOC H15  H  N N 39  
A1BOC H2   H  N N 40  
A1BOC H3   H  N N 41  
A1BOC H1   H  N N 42  
A1BOC H16  H  N N 43  
A1BOC H17  H  N N 44  
A1BOC H20  H  N N 45  
A1BOC H21  H  N N 46  
ALA   N    N  N N 47  
ALA   CA   C  N S 48  
ALA   C    C  N N 49  
ALA   O    O  N N 50  
ALA   CB   C  N N 51  
ALA   OXT  O  N N 52  
ALA   H    H  N N 53  
ALA   H2   H  N N 54  
ALA   HA   H  N N 55  
ALA   HB1  H  N N 56  
ALA   HB2  H  N N 57  
ALA   HB3  H  N N 58  
ALA   HXT  H  N N 59  
ARG   N    N  N N 60  
ARG   CA   C  N S 61  
ARG   C    C  N N 62  
ARG   O    O  N N 63  
ARG   CB   C  N N 64  
ARG   CG   C  N N 65  
ARG   CD   C  N N 66  
ARG   NE   N  N N 67  
ARG   CZ   C  N N 68  
ARG   NH1  N  N N 69  
ARG   NH2  N  N N 70  
ARG   OXT  O  N N 71  
ARG   H    H  N N 72  
ARG   H2   H  N N 73  
ARG   HA   H  N N 74  
ARG   HB2  H  N N 75  
ARG   HB3  H  N N 76  
ARG   HG2  H  N N 77  
ARG   HG3  H  N N 78  
ARG   HD2  H  N N 79  
ARG   HD3  H  N N 80  
ARG   HE   H  N N 81  
ARG   HH11 H  N N 82  
ARG   HH12 H  N N 83  
ARG   HH21 H  N N 84  
ARG   HH22 H  N N 85  
ARG   HXT  H  N N 86  
ASN   N    N  N N 87  
ASN   CA   C  N S 88  
ASN   C    C  N N 89  
ASN   O    O  N N 90  
ASN   CB   C  N N 91  
ASN   CG   C  N N 92  
ASN   OD1  O  N N 93  
ASN   ND2  N  N N 94  
ASN   OXT  O  N N 95  
ASN   H    H  N N 96  
ASN   H2   H  N N 97  
ASN   HA   H  N N 98  
ASN   HB2  H  N N 99  
ASN   HB3  H  N N 100 
ASN   HD21 H  N N 101 
ASN   HD22 H  N N 102 
ASN   HXT  H  N N 103 
ASP   N    N  N N 104 
ASP   CA   C  N S 105 
ASP   C    C  N N 106 
ASP   O    O  N N 107 
ASP   CB   C  N N 108 
ASP   CG   C  N N 109 
ASP   OD1  O  N N 110 
ASP   OD2  O  N N 111 
ASP   OXT  O  N N 112 
ASP   H    H  N N 113 
ASP   H2   H  N N 114 
ASP   HA   H  N N 115 
ASP   HB2  H  N N 116 
ASP   HB3  H  N N 117 
ASP   HD2  H  N N 118 
ASP   HXT  H  N N 119 
CYS   N    N  N N 120 
CYS   CA   C  N R 121 
CYS   C    C  N N 122 
CYS   O    O  N N 123 
CYS   CB   C  N N 124 
CYS   SG   S  N N 125 
CYS   OXT  O  N N 126 
CYS   H    H  N N 127 
CYS   H2   H  N N 128 
CYS   HA   H  N N 129 
CYS   HB2  H  N N 130 
CYS   HB3  H  N N 131 
CYS   HG   H  N N 132 
CYS   HXT  H  N N 133 
DMS   S    S  N N 134 
DMS   O    O  N N 135 
DMS   C1   C  N N 136 
DMS   C2   C  N N 137 
DMS   H11  H  N N 138 
DMS   H12  H  N N 139 
DMS   H13  H  N N 140 
DMS   H21  H  N N 141 
DMS   H22  H  N N 142 
DMS   H23  H  N N 143 
GLN   N    N  N N 144 
GLN   CA   C  N S 145 
GLN   C    C  N N 146 
GLN   O    O  N N 147 
GLN   CB   C  N N 148 
GLN   CG   C  N N 149 
GLN   CD   C  N N 150 
GLN   OE1  O  N N 151 
GLN   NE2  N  N N 152 
GLN   OXT  O  N N 153 
GLN   H    H  N N 154 
GLN   H2   H  N N 155 
GLN   HA   H  N N 156 
GLN   HB2  H  N N 157 
GLN   HB3  H  N N 158 
GLN   HG2  H  N N 159 
GLN   HG3  H  N N 160 
GLN   HE21 H  N N 161 
GLN   HE22 H  N N 162 
GLN   HXT  H  N N 163 
GLU   N    N  N N 164 
GLU   CA   C  N S 165 
GLU   C    C  N N 166 
GLU   O    O  N N 167 
GLU   CB   C  N N 168 
GLU   CG   C  N N 169 
GLU   CD   C  N N 170 
GLU   OE1  O  N N 171 
GLU   OE2  O  N N 172 
GLU   OXT  O  N N 173 
GLU   H    H  N N 174 
GLU   H2   H  N N 175 
GLU   HA   H  N N 176 
GLU   HB2  H  N N 177 
GLU   HB3  H  N N 178 
GLU   HG2  H  N N 179 
GLU   HG3  H  N N 180 
GLU   HE2  H  N N 181 
GLU   HXT  H  N N 182 
GLY   N    N  N N 183 
GLY   CA   C  N N 184 
GLY   C    C  N N 185 
GLY   O    O  N N 186 
GLY   OXT  O  N N 187 
GLY   H    H  N N 188 
GLY   H2   H  N N 189 
GLY   HA2  H  N N 190 
GLY   HA3  H  N N 191 
GLY   HXT  H  N N 192 
HIS   N    N  N N 193 
HIS   CA   C  N S 194 
HIS   C    C  N N 195 
HIS   O    O  N N 196 
HIS   CB   C  N N 197 
HIS   CG   C  Y N 198 
HIS   ND1  N  Y N 199 
HIS   CD2  C  Y N 200 
HIS   CE1  C  Y N 201 
HIS   NE2  N  Y N 202 
HIS   OXT  O  N N 203 
HIS   H    H  N N 204 
HIS   H2   H  N N 205 
HIS   HA   H  N N 206 
HIS   HB2  H  N N 207 
HIS   HB3  H  N N 208 
HIS   HD1  H  N N 209 
HIS   HD2  H  N N 210 
HIS   HE1  H  N N 211 
HIS   HE2  H  N N 212 
HIS   HXT  H  N N 213 
HOH   O    O  N N 214 
HOH   H1   H  N N 215 
HOH   H2   H  N N 216 
ILE   N    N  N N 217 
ILE   CA   C  N S 218 
ILE   C    C  N N 219 
ILE   O    O  N N 220 
ILE   CB   C  N S 221 
ILE   CG1  C  N N 222 
ILE   CG2  C  N N 223 
ILE   CD1  C  N N 224 
ILE   OXT  O  N N 225 
ILE   H    H  N N 226 
ILE   H2   H  N N 227 
ILE   HA   H  N N 228 
ILE   HB   H  N N 229 
ILE   HG12 H  N N 230 
ILE   HG13 H  N N 231 
ILE   HG21 H  N N 232 
ILE   HG22 H  N N 233 
ILE   HG23 H  N N 234 
ILE   HD11 H  N N 235 
ILE   HD12 H  N N 236 
ILE   HD13 H  N N 237 
ILE   HXT  H  N N 238 
LEU   N    N  N N 239 
LEU   CA   C  N S 240 
LEU   C    C  N N 241 
LEU   O    O  N N 242 
LEU   CB   C  N N 243 
LEU   CG   C  N N 244 
LEU   CD1  C  N N 245 
LEU   CD2  C  N N 246 
LEU   OXT  O  N N 247 
LEU   H    H  N N 248 
LEU   H2   H  N N 249 
LEU   HA   H  N N 250 
LEU   HB2  H  N N 251 
LEU   HB3  H  N N 252 
LEU   HG   H  N N 253 
LEU   HD11 H  N N 254 
LEU   HD12 H  N N 255 
LEU   HD13 H  N N 256 
LEU   HD21 H  N N 257 
LEU   HD22 H  N N 258 
LEU   HD23 H  N N 259 
LEU   HXT  H  N N 260 
LYS   N    N  N N 261 
LYS   CA   C  N S 262 
LYS   C    C  N N 263 
LYS   O    O  N N 264 
LYS   CB   C  N N 265 
LYS   CG   C  N N 266 
LYS   CD   C  N N 267 
LYS   CE   C  N N 268 
LYS   NZ   N  N N 269 
LYS   OXT  O  N N 270 
LYS   H    H  N N 271 
LYS   H2   H  N N 272 
LYS   HA   H  N N 273 
LYS   HB2  H  N N 274 
LYS   HB3  H  N N 275 
LYS   HG2  H  N N 276 
LYS   HG3  H  N N 277 
LYS   HD2  H  N N 278 
LYS   HD3  H  N N 279 
LYS   HE2  H  N N 280 
LYS   HE3  H  N N 281 
LYS   HZ1  H  N N 282 
LYS   HZ2  H  N N 283 
LYS   HZ3  H  N N 284 
LYS   HXT  H  N N 285 
MET   N    N  N N 286 
MET   CA   C  N S 287 
MET   C    C  N N 288 
MET   O    O  N N 289 
MET   CB   C  N N 290 
MET   CG   C  N N 291 
MET   SD   S  N N 292 
MET   CE   C  N N 293 
MET   OXT  O  N N 294 
MET   H    H  N N 295 
MET   H2   H  N N 296 
MET   HA   H  N N 297 
MET   HB2  H  N N 298 
MET   HB3  H  N N 299 
MET   HG2  H  N N 300 
MET   HG3  H  N N 301 
MET   HE1  H  N N 302 
MET   HE2  H  N N 303 
MET   HE3  H  N N 304 
MET   HXT  H  N N 305 
PHE   N    N  N N 306 
PHE   CA   C  N S 307 
PHE   C    C  N N 308 
PHE   O    O  N N 309 
PHE   CB   C  N N 310 
PHE   CG   C  Y N 311 
PHE   CD1  C  Y N 312 
PHE   CD2  C  Y N 313 
PHE   CE1  C  Y N 314 
PHE   CE2  C  Y N 315 
PHE   CZ   C  Y N 316 
PHE   OXT  O  N N 317 
PHE   H    H  N N 318 
PHE   H2   H  N N 319 
PHE   HA   H  N N 320 
PHE   HB2  H  N N 321 
PHE   HB3  H  N N 322 
PHE   HD1  H  N N 323 
PHE   HD2  H  N N 324 
PHE   HE1  H  N N 325 
PHE   HE2  H  N N 326 
PHE   HZ   H  N N 327 
PHE   HXT  H  N N 328 
PRO   N    N  N N 329 
PRO   CA   C  N S 330 
PRO   C    C  N N 331 
PRO   O    O  N N 332 
PRO   CB   C  N N 333 
PRO   CG   C  N N 334 
PRO   CD   C  N N 335 
PRO   OXT  O  N N 336 
PRO   H    H  N N 337 
PRO   HA   H  N N 338 
PRO   HB2  H  N N 339 
PRO   HB3  H  N N 340 
PRO   HG2  H  N N 341 
PRO   HG3  H  N N 342 
PRO   HD2  H  N N 343 
PRO   HD3  H  N N 344 
PRO   HXT  H  N N 345 
SER   N    N  N N 346 
SER   CA   C  N S 347 
SER   C    C  N N 348 
SER   O    O  N N 349 
SER   CB   C  N N 350 
SER   OG   O  N N 351 
SER   OXT  O  N N 352 
SER   H    H  N N 353 
SER   H2   H  N N 354 
SER   HA   H  N N 355 
SER   HB2  H  N N 356 
SER   HB3  H  N N 357 
SER   HG   H  N N 358 
SER   HXT  H  N N 359 
THR   N    N  N N 360 
THR   CA   C  N S 361 
THR   C    C  N N 362 
THR   O    O  N N 363 
THR   CB   C  N R 364 
THR   OG1  O  N N 365 
THR   CG2  C  N N 366 
THR   OXT  O  N N 367 
THR   H    H  N N 368 
THR   H2   H  N N 369 
THR   HA   H  N N 370 
THR   HB   H  N N 371 
THR   HG1  H  N N 372 
THR   HG21 H  N N 373 
THR   HG22 H  N N 374 
THR   HG23 H  N N 375 
THR   HXT  H  N N 376 
TRP   N    N  N N 377 
TRP   CA   C  N S 378 
TRP   C    C  N N 379 
TRP   O    O  N N 380 
TRP   CB   C  N N 381 
TRP   CG   C  Y N 382 
TRP   CD1  C  Y N 383 
TRP   CD2  C  Y N 384 
TRP   NE1  N  Y N 385 
TRP   CE2  C  Y N 386 
TRP   CE3  C  Y N 387 
TRP   CZ2  C  Y N 388 
TRP   CZ3  C  Y N 389 
TRP   CH2  C  Y N 390 
TRP   OXT  O  N N 391 
TRP   H    H  N N 392 
TRP   H2   H  N N 393 
TRP   HA   H  N N 394 
TRP   HB2  H  N N 395 
TRP   HB3  H  N N 396 
TRP   HD1  H  N N 397 
TRP   HE1  H  N N 398 
TRP   HE3  H  N N 399 
TRP   HZ2  H  N N 400 
TRP   HZ3  H  N N 401 
TRP   HH2  H  N N 402 
TRP   HXT  H  N N 403 
TYR   N    N  N N 404 
TYR   CA   C  N S 405 
TYR   C    C  N N 406 
TYR   O    O  N N 407 
TYR   CB   C  N N 408 
TYR   CG   C  Y N 409 
TYR   CD1  C  Y N 410 
TYR   CD2  C  Y N 411 
TYR   CE1  C  Y N 412 
TYR   CE2  C  Y N 413 
TYR   CZ   C  Y N 414 
TYR   OH   O  N N 415 
TYR   OXT  O  N N 416 
TYR   H    H  N N 417 
TYR   H2   H  N N 418 
TYR   HA   H  N N 419 
TYR   HB2  H  N N 420 
TYR   HB3  H  N N 421 
TYR   HD1  H  N N 422 
TYR   HD2  H  N N 423 
TYR   HE1  H  N N 424 
TYR   HE2  H  N N 425 
TYR   HH   H  N N 426 
TYR   HXT  H  N N 427 
VAL   N    N  N N 428 
VAL   CA   C  N S 429 
VAL   C    C  N N 430 
VAL   O    O  N N 431 
VAL   CB   C  N N 432 
VAL   CG1  C  N N 433 
VAL   CG2  C  N N 434 
VAL   OXT  O  N N 435 
VAL   H    H  N N 436 
VAL   H2   H  N N 437 
VAL   HA   H  N N 438 
VAL   HB   H  N N 439 
VAL   HG11 H  N N 440 
VAL   HG12 H  N N 441 
VAL   HG13 H  N N 442 
VAL   HG21 H  N N 443 
VAL   HG22 H  N N 444 
VAL   HG23 H  N N 445 
VAL   HXT  H  N N 446 
ZN    ZN   ZN N N 447 
# 
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 
A1BOC C   C1   sing N N 1   
A1BOC C1  N    sing Y N 2   
A1BOC N   C2   doub Y N 3   
A1BOC C2  N1   sing Y N 4   
A1BOC N1  C3   sing Y N 5   
A1BOC C1  C3   doub Y N 6   
A1BOC C3  C4   sing N N 7   
A1BOC C4  C5   sing N N 8   
A1BOC O   C5   doub N N 9   
A1BOC C5  N2   sing N N 10  
A1BOC N2  C6   sing N N 11  
A1BOC C6  C7   sing N N 12  
A1BOC C7  C8   sing N N 13  
A1BOC C8  C9   sing N N 14  
A1BOC C9  C10  sing N N 15  
A1BOC N3  C10  sing N N 16  
A1BOC C10 O1   doub N N 17  
A1BOC C11 C9   sing N N 18  
A1BOC N2  C11  sing N N 19  
A1BOC C12 N1   sing N N 20  
A1BOC C13 C12  sing N N 21  
A1BOC C14 C13  sing N N 22  
A1BOC C15 C14  sing N N 23  
A1BOC C2  C15  sing N N 24  
A1BOC N3  H13  sing N N 25  
A1BOC N3  H12  sing N N 26  
A1BOC C4  H4   sing N N 27  
A1BOC C4  H5   sing N N 28  
A1BOC C6  H6   sing N N 29  
A1BOC C6  H7   sing N N 30  
A1BOC C7  H8   sing N N 31  
A1BOC C7  H9   sing N N 32  
A1BOC C8  H10  sing N N 33  
A1BOC C8  H11  sing N N 34  
A1BOC C13 H18  sing N N 35  
A1BOC C13 H19  sing N N 36  
A1BOC C15 H22  sing N N 37  
A1BOC C15 H23  sing N N 38  
A1BOC C9  H    sing N N 39  
A1BOC C11 H14  sing N N 40  
A1BOC C11 H15  sing N N 41  
A1BOC C   H2   sing N N 42  
A1BOC C   H3   sing N N 43  
A1BOC C   H1   sing N N 44  
A1BOC C12 H16  sing N N 45  
A1BOC C12 H17  sing N N 46  
A1BOC C14 H20  sing N N 47  
A1BOC C14 H21  sing N N 48  
ALA   N   CA   sing N N 49  
ALA   N   H    sing N N 50  
ALA   N   H2   sing N N 51  
ALA   CA  C    sing N N 52  
ALA   CA  CB   sing N N 53  
ALA   CA  HA   sing N N 54  
ALA   C   O    doub N N 55  
ALA   C   OXT  sing N N 56  
ALA   CB  HB1  sing N N 57  
ALA   CB  HB2  sing N N 58  
ALA   CB  HB3  sing N N 59  
ALA   OXT HXT  sing N N 60  
ARG   N   CA   sing N N 61  
ARG   N   H    sing N N 62  
ARG   N   H2   sing N N 63  
ARG   CA  C    sing N N 64  
ARG   CA  CB   sing N N 65  
ARG   CA  HA   sing N N 66  
ARG   C   O    doub N N 67  
ARG   C   OXT  sing N N 68  
ARG   CB  CG   sing N N 69  
ARG   CB  HB2  sing N N 70  
ARG   CB  HB3  sing N N 71  
ARG   CG  CD   sing N N 72  
ARG   CG  HG2  sing N N 73  
ARG   CG  HG3  sing N N 74  
ARG   CD  NE   sing N N 75  
ARG   CD  HD2  sing N N 76  
ARG   CD  HD3  sing N N 77  
ARG   NE  CZ   sing N N 78  
ARG   NE  HE   sing N N 79  
ARG   CZ  NH1  sing N N 80  
ARG   CZ  NH2  doub N N 81  
ARG   NH1 HH11 sing N N 82  
ARG   NH1 HH12 sing N N 83  
ARG   NH2 HH21 sing N N 84  
ARG   NH2 HH22 sing N N 85  
ARG   OXT HXT  sing N N 86  
ASN   N   CA   sing N N 87  
ASN   N   H    sing N N 88  
ASN   N   H2   sing N N 89  
ASN   CA  C    sing N N 90  
ASN   CA  CB   sing N N 91  
ASN   CA  HA   sing N N 92  
ASN   C   O    doub N N 93  
ASN   C   OXT  sing N N 94  
ASN   CB  CG   sing N N 95  
ASN   CB  HB2  sing N N 96  
ASN   CB  HB3  sing N N 97  
ASN   CG  OD1  doub N N 98  
ASN   CG  ND2  sing N N 99  
ASN   ND2 HD21 sing N N 100 
ASN   ND2 HD22 sing N N 101 
ASN   OXT HXT  sing N N 102 
ASP   N   CA   sing N N 103 
ASP   N   H    sing N N 104 
ASP   N   H2   sing N N 105 
ASP   CA  C    sing N N 106 
ASP   CA  CB   sing N N 107 
ASP   CA  HA   sing N N 108 
ASP   C   O    doub N N 109 
ASP   C   OXT  sing N N 110 
ASP   CB  CG   sing N N 111 
ASP   CB  HB2  sing N N 112 
ASP   CB  HB3  sing N N 113 
ASP   CG  OD1  doub N N 114 
ASP   CG  OD2  sing N N 115 
ASP   OD2 HD2  sing N N 116 
ASP   OXT HXT  sing N N 117 
CYS   N   CA   sing N N 118 
CYS   N   H    sing N N 119 
CYS   N   H2   sing N N 120 
CYS   CA  C    sing N N 121 
CYS   CA  CB   sing N N 122 
CYS   CA  HA   sing N N 123 
CYS   C   O    doub N N 124 
CYS   C   OXT  sing N N 125 
CYS   CB  SG   sing N N 126 
CYS   CB  HB2  sing N N 127 
CYS   CB  HB3  sing N N 128 
CYS   SG  HG   sing N N 129 
CYS   OXT HXT  sing N N 130 
DMS   S   O    doub N N 131 
DMS   S   C1   sing N N 132 
DMS   S   C2   sing N N 133 
DMS   C1  H11  sing N N 134 
DMS   C1  H12  sing N N 135 
DMS   C1  H13  sing N N 136 
DMS   C2  H21  sing N N 137 
DMS   C2  H22  sing N N 138 
DMS   C2  H23  sing N N 139 
GLN   N   CA   sing N N 140 
GLN   N   H    sing N N 141 
GLN   N   H2   sing N N 142 
GLN   CA  C    sing N N 143 
GLN   CA  CB   sing N N 144 
GLN   CA  HA   sing N N 145 
GLN   C   O    doub N N 146 
GLN   C   OXT  sing N N 147 
GLN   CB  CG   sing N N 148 
GLN   CB  HB2  sing N N 149 
GLN   CB  HB3  sing N N 150 
GLN   CG  CD   sing N N 151 
GLN   CG  HG2  sing N N 152 
GLN   CG  HG3  sing N N 153 
GLN   CD  OE1  doub N N 154 
GLN   CD  NE2  sing N N 155 
GLN   NE2 HE21 sing N N 156 
GLN   NE2 HE22 sing N N 157 
GLN   OXT HXT  sing N N 158 
GLU   N   CA   sing N N 159 
GLU   N   H    sing N N 160 
GLU   N   H2   sing N N 161 
GLU   CA  C    sing N N 162 
GLU   CA  CB   sing N N 163 
GLU   CA  HA   sing N N 164 
GLU   C   O    doub N N 165 
GLU   C   OXT  sing N N 166 
GLU   CB  CG   sing N N 167 
GLU   CB  HB2  sing N N 168 
GLU   CB  HB3  sing N N 169 
GLU   CG  CD   sing N N 170 
GLU   CG  HG2  sing N N 171 
GLU   CG  HG3  sing N N 172 
GLU   CD  OE1  doub N N 173 
GLU   CD  OE2  sing N N 174 
GLU   OE2 HE2  sing N N 175 
GLU   OXT HXT  sing N N 176 
GLY   N   CA   sing N N 177 
GLY   N   H    sing N N 178 
GLY   N   H2   sing N N 179 
GLY   CA  C    sing N N 180 
GLY   CA  HA2  sing N N 181 
GLY   CA  HA3  sing N N 182 
GLY   C   O    doub N N 183 
GLY   C   OXT  sing N N 184 
GLY   OXT HXT  sing N N 185 
HIS   N   CA   sing N N 186 
HIS   N   H    sing N N 187 
HIS   N   H2   sing N N 188 
HIS   CA  C    sing N N 189 
HIS   CA  CB   sing N N 190 
HIS   CA  HA   sing N N 191 
HIS   C   O    doub N N 192 
HIS   C   OXT  sing N N 193 
HIS   CB  CG   sing N N 194 
HIS   CB  HB2  sing N N 195 
HIS   CB  HB3  sing N N 196 
HIS   CG  ND1  sing Y N 197 
HIS   CG  CD2  doub Y N 198 
HIS   ND1 CE1  doub Y N 199 
HIS   ND1 HD1  sing N N 200 
HIS   CD2 NE2  sing Y N 201 
HIS   CD2 HD2  sing N N 202 
HIS   CE1 NE2  sing Y N 203 
HIS   CE1 HE1  sing N N 204 
HIS   NE2 HE2  sing N N 205 
HIS   OXT HXT  sing N N 206 
HOH   O   H1   sing N N 207 
HOH   O   H2   sing N N 208 
ILE   N   CA   sing N N 209 
ILE   N   H    sing N N 210 
ILE   N   H2   sing N N 211 
ILE   CA  C    sing N N 212 
ILE   CA  CB   sing N N 213 
ILE   CA  HA   sing N N 214 
ILE   C   O    doub N N 215 
ILE   C   OXT  sing N N 216 
ILE   CB  CG1  sing N N 217 
ILE   CB  CG2  sing N N 218 
ILE   CB  HB   sing N N 219 
ILE   CG1 CD1  sing N N 220 
ILE   CG1 HG12 sing N N 221 
ILE   CG1 HG13 sing N N 222 
ILE   CG2 HG21 sing N N 223 
ILE   CG2 HG22 sing N N 224 
ILE   CG2 HG23 sing N N 225 
ILE   CD1 HD11 sing N N 226 
ILE   CD1 HD12 sing N N 227 
ILE   CD1 HD13 sing N N 228 
ILE   OXT HXT  sing N N 229 
LEU   N   CA   sing N N 230 
LEU   N   H    sing N N 231 
LEU   N   H2   sing N N 232 
LEU   CA  C    sing N N 233 
LEU   CA  CB   sing N N 234 
LEU   CA  HA   sing N N 235 
LEU   C   O    doub N N 236 
LEU   C   OXT  sing N N 237 
LEU   CB  CG   sing N N 238 
LEU   CB  HB2  sing N N 239 
LEU   CB  HB3  sing N N 240 
LEU   CG  CD1  sing N N 241 
LEU   CG  CD2  sing N N 242 
LEU   CG  HG   sing N N 243 
LEU   CD1 HD11 sing N N 244 
LEU   CD1 HD12 sing N N 245 
LEU   CD1 HD13 sing N N 246 
LEU   CD2 HD21 sing N N 247 
LEU   CD2 HD22 sing N N 248 
LEU   CD2 HD23 sing N N 249 
LEU   OXT HXT  sing N N 250 
LYS   N   CA   sing N N 251 
LYS   N   H    sing N N 252 
LYS   N   H2   sing N N 253 
LYS   CA  C    sing N N 254 
LYS   CA  CB   sing N N 255 
LYS   CA  HA   sing N N 256 
LYS   C   O    doub N N 257 
LYS   C   OXT  sing N N 258 
LYS   CB  CG   sing N N 259 
LYS   CB  HB2  sing N N 260 
LYS   CB  HB3  sing N N 261 
LYS   CG  CD   sing N N 262 
LYS   CG  HG2  sing N N 263 
LYS   CG  HG3  sing N N 264 
LYS   CD  CE   sing N N 265 
LYS   CD  HD2  sing N N 266 
LYS   CD  HD3  sing N N 267 
LYS   CE  NZ   sing N N 268 
LYS   CE  HE2  sing N N 269 
LYS   CE  HE3  sing N N 270 
LYS   NZ  HZ1  sing N N 271 
LYS   NZ  HZ2  sing N N 272 
LYS   NZ  HZ3  sing N N 273 
LYS   OXT HXT  sing N N 274 
MET   N   CA   sing N N 275 
MET   N   H    sing N N 276 
MET   N   H2   sing N N 277 
MET   CA  C    sing N N 278 
MET   CA  CB   sing N N 279 
MET   CA  HA   sing N N 280 
MET   C   O    doub N N 281 
MET   C   OXT  sing N N 282 
MET   CB  CG   sing N N 283 
MET   CB  HB2  sing N N 284 
MET   CB  HB3  sing N N 285 
MET   CG  SD   sing N N 286 
MET   CG  HG2  sing N N 287 
MET   CG  HG3  sing N N 288 
MET   SD  CE   sing N N 289 
MET   CE  HE1  sing N N 290 
MET   CE  HE2  sing N N 291 
MET   CE  HE3  sing N N 292 
MET   OXT HXT  sing N N 293 
PHE   N   CA   sing N N 294 
PHE   N   H    sing N N 295 
PHE   N   H2   sing N N 296 
PHE   CA  C    sing N N 297 
PHE   CA  CB   sing N N 298 
PHE   CA  HA   sing N N 299 
PHE   C   O    doub N N 300 
PHE   C   OXT  sing N N 301 
PHE   CB  CG   sing N N 302 
PHE   CB  HB2  sing N N 303 
PHE   CB  HB3  sing N N 304 
PHE   CG  CD1  doub Y N 305 
PHE   CG  CD2  sing Y N 306 
PHE   CD1 CE1  sing Y N 307 
PHE   CD1 HD1  sing N N 308 
PHE   CD2 CE2  doub Y N 309 
PHE   CD2 HD2  sing N N 310 
PHE   CE1 CZ   doub Y N 311 
PHE   CE1 HE1  sing N N 312 
PHE   CE2 CZ   sing Y N 313 
PHE   CE2 HE2  sing N N 314 
PHE   CZ  HZ   sing N N 315 
PHE   OXT HXT  sing N N 316 
PRO   N   CA   sing N N 317 
PRO   N   CD   sing N N 318 
PRO   N   H    sing N N 319 
PRO   CA  C    sing N N 320 
PRO   CA  CB   sing N N 321 
PRO   CA  HA   sing N N 322 
PRO   C   O    doub N N 323 
PRO   C   OXT  sing N N 324 
PRO   CB  CG   sing N N 325 
PRO   CB  HB2  sing N N 326 
PRO   CB  HB3  sing N N 327 
PRO   CG  CD   sing N N 328 
PRO   CG  HG2  sing N N 329 
PRO   CG  HG3  sing N N 330 
PRO   CD  HD2  sing N N 331 
PRO   CD  HD3  sing N N 332 
PRO   OXT HXT  sing N N 333 
SER   N   CA   sing N N 334 
SER   N   H    sing N N 335 
SER   N   H2   sing N N 336 
SER   CA  C    sing N N 337 
SER   CA  CB   sing N N 338 
SER   CA  HA   sing N N 339 
SER   C   O    doub N N 340 
SER   C   OXT  sing N N 341 
SER   CB  OG   sing N N 342 
SER   CB  HB2  sing N N 343 
SER   CB  HB3  sing N N 344 
SER   OG  HG   sing N N 345 
SER   OXT HXT  sing N N 346 
THR   N   CA   sing N N 347 
THR   N   H    sing N N 348 
THR   N   H2   sing N N 349 
THR   CA  C    sing N N 350 
THR   CA  CB   sing N N 351 
THR   CA  HA   sing N N 352 
THR   C   O    doub N N 353 
THR   C   OXT  sing N N 354 
THR   CB  OG1  sing N N 355 
THR   CB  CG2  sing N N 356 
THR   CB  HB   sing N N 357 
THR   OG1 HG1  sing N N 358 
THR   CG2 HG21 sing N N 359 
THR   CG2 HG22 sing N N 360 
THR   CG2 HG23 sing N N 361 
THR   OXT HXT  sing N N 362 
TRP   N   CA   sing N N 363 
TRP   N   H    sing N N 364 
TRP   N   H2   sing N N 365 
TRP   CA  C    sing N N 366 
TRP   CA  CB   sing N N 367 
TRP   CA  HA   sing N N 368 
TRP   C   O    doub N N 369 
TRP   C   OXT  sing N N 370 
TRP   CB  CG   sing N N 371 
TRP   CB  HB2  sing N N 372 
TRP   CB  HB3  sing N N 373 
TRP   CG  CD1  doub Y N 374 
TRP   CG  CD2  sing Y N 375 
TRP   CD1 NE1  sing Y N 376 
TRP   CD1 HD1  sing N N 377 
TRP   CD2 CE2  doub Y N 378 
TRP   CD2 CE3  sing Y N 379 
TRP   NE1 CE2  sing Y N 380 
TRP   NE1 HE1  sing N N 381 
TRP   CE2 CZ2  sing Y N 382 
TRP   CE3 CZ3  doub Y N 383 
TRP   CE3 HE3  sing N N 384 
TRP   CZ2 CH2  doub Y N 385 
TRP   CZ2 HZ2  sing N N 386 
TRP   CZ3 CH2  sing Y N 387 
TRP   CZ3 HZ3  sing N N 388 
TRP   CH2 HH2  sing N N 389 
TRP   OXT HXT  sing N N 390 
TYR   N   CA   sing N N 391 
TYR   N   H    sing N N 392 
TYR   N   H2   sing N N 393 
TYR   CA  C    sing N N 394 
TYR   CA  CB   sing N N 395 
TYR   CA  HA   sing N N 396 
TYR   C   O    doub N N 397 
TYR   C   OXT  sing N N 398 
TYR   CB  CG   sing N N 399 
TYR   CB  HB2  sing N N 400 
TYR   CB  HB3  sing N N 401 
TYR   CG  CD1  doub Y N 402 
TYR   CG  CD2  sing Y N 403 
TYR   CD1 CE1  sing Y N 404 
TYR   CD1 HD1  sing N N 405 
TYR   CD2 CE2  doub Y N 406 
TYR   CD2 HD2  sing N N 407 
TYR   CE1 CZ   doub Y N 408 
TYR   CE1 HE1  sing N N 409 
TYR   CE2 CZ   sing Y N 410 
TYR   CE2 HE2  sing N N 411 
TYR   CZ  OH   sing N N 412 
TYR   OH  HH   sing N N 413 
TYR   OXT HXT  sing N N 414 
VAL   N   CA   sing N N 415 
VAL   N   H    sing N N 416 
VAL   N   H2   sing N N 417 
VAL   CA  C    sing N N 418 
VAL   CA  CB   sing N N 419 
VAL   CA  HA   sing N N 420 
VAL   C   O    doub N N 421 
VAL   C   OXT  sing N N 422 
VAL   CB  CG1  sing N N 423 
VAL   CB  CG2  sing N N 424 
VAL   CB  HB   sing N N 425 
VAL   CG1 HG11 sing N N 426 
VAL   CG1 HG12 sing N N 427 
VAL   CG1 HG13 sing N N 428 
VAL   CG2 HG21 sing N N 429 
VAL   CG2 HG22 sing N N 430 
VAL   CG2 HG23 sing N N 431 
VAL   OXT HXT  sing N N 432 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002329 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7HVE 
_atom_sites.fract_transf_matrix[1][1]   0.013454 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000611 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016363 
_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]   0.030740 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.519 6.460   24.148 1.00 32.46 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.671 6.616   23.253 1.00 33.32 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.755 5.458   22.222 1.00 32.46 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.999 4.475   22.307 1.00 32.66 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.956 6.728   24.069 1.00 36.58 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 22.149 5.541   24.819 1.00 40.28 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.623 5.610   21.228 1.00 30.66 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.831 4.570   20.235 1.00 29.55 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 22.142 5.095   18.849 1.00 28.30 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.696 6.188   18.472 1.00 27.62 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.885 4.307   18.063 1.00 27.38 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 23.241 4.684   16.690 1.00 27.16 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 23.182 3.496   15.698 1.00 27.23 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 23.210 2.346   16.135 1.00 27.38 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.646 5.276   16.681 1.00 27.20 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 23.148 3.788   14.367 1.00 26.49 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 23.250 2.823   13.277 1.00 26.04 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.637 3.057   12.633 1.00 26.50 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 25.018 4.199   12.340 1.00 26.42 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 22.125 2.963   12.206 1.00 26.06 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.716 3.080   12.828 1.00 25.50 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 22.199 1.831   11.166 1.00 26.92 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.653 3.624   11.831 1.00 25.09 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.400 1.978   12.427 1.00 27.33 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.728 2.080   11.844 1.00 28.75 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.701 1.319   10.532 1.00 30.53 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.482 0.098   10.531 1.00 30.74 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.770 1.485   12.810 1.00 28.78 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.900 2.292   14.087 1.00 29.07 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.703 3.424   14.139 1.00 30.16 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 27.228 1.917   15.242 1.00 30.22 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.818 4.178   15.302 1.00 30.53 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 27.314 2.680   16.406 1.00 31.19 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 28.115 3.809   16.429 1.00 31.61 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 28.256 4.546   17.571 1.00 33.92 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.826 2.044   9.415  1.00 30.55 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.796 1.454   8.081  1.00 31.98 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.876 2.118   7.222  1.00 33.41 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.896 3.355   7.121  1.00 33.36 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.376 1.529   7.451  1.00 33.58 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.765 2.929   7.588  1.00 33.96 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.388 1.075   5.987  1.00 35.21 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.785 1.306   6.650  1.00 33.31 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.906 1.811   5.865  1.00 33.77 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.781 2.755   6.678  1.00 34.36 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 31.124 2.440   7.825  1.00 35.04 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 31.065 3.952   6.157  1.00 33.89 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.829 4.950   6.939  1.00 34.12 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.901 6.001   7.558  1.00 33.22 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 31.317 7.141   7.750  1.00 33.80 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.911 5.619   6.100  1.00 36.60 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 34.019 4.666   5.725  1.00 43.47 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.748 4.137   6.585  1.00 46.06 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.162 4.412   4.436  1.00 44.70 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.666 5.612   7.911  1.00 31.77 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.675 6.527   8.477  1.00 31.07 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 28.164 6.060   9.833  1.00 29.92 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 28.036 4.856   10.069 1.00 29.24 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.459 6.636   7.529  1.00 31.35 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.801 7.165   6.153  1.00 32.64 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.493 8.359   5.999  1.00 33.91 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.389 6.499   5.008  1.00 34.15 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.777 8.870   4.737  1.00 35.00 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.693 6.982   3.741  1.00 35.28 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.379 8.176   3.608  1.00 36.16 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.683 8.668   2.354  1.00 37.86 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.789 7.036   10.677 1.00 28.68 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 27.172 6.852   11.982 1.00 28.20 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.881 7.676   11.933 1.00 27.82 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.911 8.865   11.638 1.00 27.58 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 28.102 7.357   13.126 1.00 28.32 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 27.411 7.521   14.476 1.00 31.09 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.413 7.665   15.624 1.00 33.13 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 28.076 8.750   16.544 1.00 35.06 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.503 8.583   17.733 1.00 36.03 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 27.205 7.364   18.172 1.00 34.43 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 27.226 9.635   18.496 1.00 33.76 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.750 7.032   12.182 1.00 27.53 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 23.452 7.704   12.111 1.00 27.23 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.923 7.815   13.530 1.00 26.89 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.788 6.781   14.209 1.00 26.73 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 22.458 6.907   11.214 1.00 26.95 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 21.187 7.725   10.964 1.00 28.41 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 23.110 6.481   9.891  1.00 26.05 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.591 9.049   13.972 1.00 26.39 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 22.089 9.292   15.338 1.00 26.23 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.865 10.212  15.303 1.00 25.76 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.617 10.892  14.305 1.00 25.78 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 23.194 9.941   16.266 1.00 26.46 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.270 8.938   16.624 1.00 27.15 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.805 11.170  15.595 1.00 25.76 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 20.127 10.312  16.438 1.00 25.29 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 19.084 11.349  16.584 1.00 25.42 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.862 12.678  16.597 1.00 26.36 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.855 12.800  17.329 1.00 26.35 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 18.387 11.214  17.958 1.00 25.58 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.496 9.973   18.062 1.00 28.22 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.897 8.896   18.530 1.00 31.31 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 16.277 10.091  17.610 1.00 27.87 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.450 13.644  15.778 1.00 27.11 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 20.135 14.941  15.716 1.00 28.88 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 20.254 15.617  17.098 1.00 30.44 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 21.289 16.212  17.395 1.00 32.16 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 19.416 15.854  14.691 1.00 29.59 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 20.201 17.119  14.266 1.00 30.76 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 19.267 18.029  13.461 1.00 33.15 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.870 19.290  13.003 1.00 36.76 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.919 20.404  13.724 1.00 39.42 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 19.476 20.414  14.971 1.00 39.91 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 20.426 21.522  13.202 1.00 38.61 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 19.208 15.521  17.956 1.00 30.87 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 19.220 16.126  19.288 1.00 32.29 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 20.238 15.464  20.259 1.00 33.00 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.664 16.084  21.223 1.00 33.10 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.799 16.218  19.894 1.00 33.02 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 17.166 14.932  20.339 1.00 33.08 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.490 14.103  19.445 1.00 34.06 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 17.034 14.420  21.587 1.00 34.14 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 16.013 13.096  20.166 1.00 34.75 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 16.325 13.226  21.458 1.00 34.94 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.728 14.280  19.914 1.00 33.32 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.710 13.571  20.716 1.00 33.73 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 23.117 13.576  20.097 1.00 33.50 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 24.047 13.054  20.716 1.00 33.61 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 21.205 12.145  21.013 1.00 34.30 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.919 12.062  21.845 1.00 35.85 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.536 10.620  22.130 1.00 36.74 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 20.027 12.840  23.158 1.00 36.17 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 23.299 14.210  18.913 1.00 32.89 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.617 14.310  18.279 1.00 32.85 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.640 14.971  19.201 1.00 31.75 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 25.291 15.873  19.964 1.00 32.15 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.528 15.078  16.973 1.00 33.17 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.875 14.444  19.191 1.00 30.73 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.987 14.904  20.026 1.00 31.73 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.866 15.944  19.259 1.00 32.67 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.651 16.176  18.071 1.00 33.28 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.835 13.674  20.487 1.00 32.25 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.640 13.238  19.386 1.00 33.43 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.980 12.521  21.027 1.00 31.67 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.868 16.528  19.925 1.00 32.97 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.791 17.467  19.292 1.00 34.43 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 31.536 16.795  18.133 1.00 34.20 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.661 17.400  17.073 1.00 33.38 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.802 17.987  20.321 1.00 37.51 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.246 19.078  21.166 1.00 43.95 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.890 20.296  21.282 1.00 47.07 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.088 19.125  21.866 1.00 46.19 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 31.133 21.023  22.087 1.00 47.97 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.033 20.365  22.454 1.00 47.77 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 32.042 15.548  18.343 1.00 33.85 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.740 14.818  17.289 1.00 34.76 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.832 14.571  16.080 1.00 34.11 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 32.317 14.728  14.963 1.00 34.40 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 33.391 13.511  17.805 1.00 37.65 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.939 12.607  16.697 1.00 43.94 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 35.074 12.778  16.218 1.00 46.15 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.126 11.642  16.238 1.00 44.02 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 30.544 14.182  16.287 1.00 33.34 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 29.569 14.024  15.193 1.00 33.35 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 29.439 15.354  14.403 1.00 34.93 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 29.356 15.332  13.188 1.00 35.02 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 28.165 13.703  15.746 1.00 32.62 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.949 12.297  16.250 1.00 31.31 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.585 11.379  15.720 1.00 29.79 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 27.108 12.118  17.150 1.00 31.17 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 29.388 16.500  15.100 1.00 36.07 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 29.254 17.800  14.416 1.00 37.57 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 30.543 18.154  13.654 1.00 38.74 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 30.473 18.630  12.527 1.00 39.79 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.792 18.905  15.383 1.00 38.12 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 27.297 19.003  15.501 1.00 38.02 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 26.526 18.570  16.540 1.00 38.56 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 26.395 19.591  14.544 1.00 37.19 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 25.196 18.827  16.280 1.00 38.83 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 25.087 19.436  15.052 1.00 37.74 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 26.556 20.130  13.263 1.00 36.95 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.957 19.837  14.340 1.00 36.76 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 25.439 20.598  12.592 1.00 36.73 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 24.159 20.414  13.114 1.00 36.68 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.711 17.839  14.236 1.00 39.12 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 33.045 18.075  13.649 1.00 39.26 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 33.339 17.159  12.440 1.00 38.58 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 34.259 17.452  11.674 1.00 39.49 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 34.129 17.883  14.709 1.00 39.10 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 32.587 16.053  12.290 1.00 36.70 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.714 15.127  11.163 1.00 36.16 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 31.359 14.962  10.475 1.00 35.62 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 31.014 13.869  10.026 1.00 35.66 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 33.255 13.781  11.632 1.00 37.48 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.657 13.863  12.151 1.00 40.37 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.629 14.027  11.396 1.00 41.79 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.789 13.765  13.454 1.00 40.43 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.582 16.062  10.392 1.00 34.99 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 29.256 16.074  9.814  1.00 35.15 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 29.262 15.656  8.356  1.00 35.73 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 30.119 16.102  7.589  1.00 36.62 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.651 17.498  9.948  1.00 35.04 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 27.288 17.763  9.334  1.00 35.58 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 26.186 16.891  9.989  1.00 35.21 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.907 19.263  9.423  1.00 36.30 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 28.276 14.834  7.967  1.00 34.90 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 28.059 14.461  6.578  1.00 35.53 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.719 15.106  6.127  1.00 36.18 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.625 15.730  5.053  1.00 36.50 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 28.043 12.921  6.423  1.00 35.80 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.563 12.503  5.035  1.00 36.23 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.409 12.319  6.746  1.00 36.47 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.664 14.928  6.959  1.00 36.32 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.331 15.443  6.650  1.00 37.07 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.450 15.513  7.899  1.00 36.39 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.549 14.658  8.748  1.00 36.29 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.661 14.541  5.574  1.00 37.77 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 22.198 14.784  5.338  1.00 39.43 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.638 15.723  4.523  1.00 40.88 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 21.109 14.023  5.887  1.00 40.00 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 20.267 15.600  4.537  1.00 41.47 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.917 14.565  5.369  1.00 40.98 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 21.029 12.925  6.751  1.00 40.60 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.660 14.052  5.699  1.00 41.49 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.786 12.425  7.081  1.00 41.32 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.619 12.990  6.561  1.00 41.44 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.553 16.506  7.982  1.00 36.11 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.620 16.619  9.095  1.00 36.20 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.290 17.207  8.629  1.00 37.58 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.236 18.018  7.691  1.00 37.18 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.215 17.380  10.308 1.00 37.44 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.887 18.714  9.994  1.00 38.65 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.947 19.899  9.861  1.00 40.88 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.321 20.882  9.177  1.00 41.11 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.825 19.833  10.417 1.00 40.64 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.200 16.761  9.265  1.00 38.28 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.887 17.266  8.948  1.00 39.61 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 17.103 17.501  10.237 1.00 39.57 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.606 16.553  10.832 1.00 39.73 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.150 16.325  7.980  1.00 42.63 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 16.024 16.982  7.217  1.00 48.31 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.336 17.835  7.803  1.00 50.36 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.822 16.631  6.031  1.00 50.24 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.978 18.781  10.667 1.00 38.76 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 16.232 19.120  11.881 0.50 38.94 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 16.235 19.112  11.884 0.50 38.73 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.781 18.651  11.793 1.00 39.05 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 14.229 18.151  12.772 1.00 39.06 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 16.286 20.622  12.144 0.50 40.10 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 16.334 20.601  12.224 0.50 39.30 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.523 20.962  13.289 0.50 41.61 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 16.598 21.443  11.110 0.50 39.91 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 14.184 18.778  10.606 1.00 39.03 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.816 18.389  10.302 1.00 39.68 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.592 16.879  10.500 1.00 39.53 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.498 16.471  10.851 1.00 40.63 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 12.442 18.864  8.895  1.00 41.65 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.591 18.013  8.144  1.00 46.49 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.633 16.063  10.329 1.00 38.13 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.530 14.620  10.510 1.00 36.28 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 14.135 14.135  11.844 1.00 33.77 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.911 12.989  12.196 1.00 33.68 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.239 13.914  9.355  1.00 37.18 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.582 14.132  8.013  1.00 39.89 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.393 13.459  6.931  1.00 41.83 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.285 12.003  7.030  1.00 40.67 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.523 11.162  6.029  1.00 40.93 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.877 11.624  4.829  1.00 39.95 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.386 9.859   6.206  1.00 40.21 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.901 14.999  12.577 1.00 31.69 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.598 14.646  13.827 1.00 30.38 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.696 13.616  13.529 1.00 29.45 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.969 12.762  14.352 1.00 28.83 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.659 14.124  14.960 1.00 31.03 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.332 13.836  16.310 1.00 32.68 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 16.180 14.658  16.748 1.00 30.29 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 15.020 12.780  16.924 1.00 33.91 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 17.402 13.768  12.394 1.00 29.53 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.482 12.856  12.014 1.00 29.06 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.788 13.639  11.774 1.00 30.24 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.770 14.758  11.264 1.00 31.34 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 18.140 12.107  10.726 1.00 28.00 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 17.155 10.920  10.846 1.00 27.36 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.938 10.274  9.476  1.00 28.04 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.706 9.861   11.812 1.00 27.17 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.921 13.001  12.130 1.00 29.18 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 22.240 13.499  11.832 1.00 29.47 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 23.101 12.291  11.436 1.00 29.60 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 23.014 11.237  12.050 1.00 30.33 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.866 14.312  12.995 1.00 29.55 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 24.267 14.905  12.751 1.00 30.53 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 24.472 16.167  13.550 1.00 31.02 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 25.392 13.906  13.170 1.00 30.74 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.938 12.452  10.410 1.00 29.80 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.869 11.430  9.963  1.00 30.53 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 26.287 12.001  10.022 1.00 31.51 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.521 13.105  9.528  1.00 31.90 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.507 10.931  8.532  1.00 30.69 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.552 9.939   8.020  1.00 31.46 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 23.110 10.323  8.513  1.00 30.45 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 27.220 11.289  10.676 1.00 31.48 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.611 11.725  10.741 1.00 32.21 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.531 10.640  10.099 1.00 32.82 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 29.093 9.503   9.888  1.00 32.18 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 29.025 12.030  12.187 1.00 33.77 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 29.107 10.873  13.010 1.00 36.20 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.805 10.983  9.805  1.00 32.84 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.734 10.006  9.221  1.00 33.63 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.542 9.282   10.308 1.00 34.71 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.699 9.795   11.416 1.00 34.94 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.684 10.683  8.236  1.00 35.14 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.436 11.690  8.896  1.00 37.57 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 33.059 8.094   9.997  1.00 35.15 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.819 7.295   10.967 1.00 36.85 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 35.106 6.763   10.322 1.00 38.76 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 35.199 6.676   9.097  1.00 38.76 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.961 6.073   11.462 1.00 37.91 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.720 5.186   10.377 1.00 39.49 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.634 6.467   12.073 1.00 37.72 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 36.066 6.329   11.144 1.00 40.44 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 37.308 5.729   10.644 1.00 42.33 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 37.132 4.207   10.492 1.00 43.35 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.602 3.615   9.520  1.00 43.62 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 38.498 6.106   11.552 1.00 44.21 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 38.141 5.881   12.917 1.00 45.58 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.930 7.536   11.371 1.00 44.82 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 36.441 3.580   11.452 1.00 43.31 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 36.156 2.148   11.424 1.00 43.42 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.950 1.883   10.529 1.00 43.55 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 34.013 2.677   10.537 1.00 44.02 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.863 1.664   12.835 1.00 43.54 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.932 0.754   9.798  1.00 43.32 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.796 0.426   8.930  1.00 43.13 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.646 -0.249  9.705  1.00 42.26 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.878 -1.071  10.588 1.00 43.10 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 34.259 -0.398  7.715  1.00 45.95 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.133 -0.895  6.794  1.00 51.01 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.259 -0.360  5.380  1.00 56.17 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.850 0.702   5.131  1.00 57.20 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.691 -1.086  4.421  1.00 57.48 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 31.419 0.153   9.397  1.00 40.59 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 30.205 -0.334  10.032 1.00 39.56 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.558 -1.447  9.243  1.00 38.24 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.689 -1.495  8.016  1.00 37.69 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.850 -2.345  9.937  1.00 37.43 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 28.290 -3.516  9.286  1.00 37.72 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.789 -3.684  9.392  1.00 36.20 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 26.316 -4.791  9.082  1.00 36.28 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.994 -4.768  9.799  1.00 40.53 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.755 -4.832  9.414  1.00 48.15 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 26.037 -2.664  9.856  1.00 34.30 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.576 -2.801  9.937  1.00 34.53 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.968 -2.810  8.505  1.00 34.02 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.519 -2.161  7.611  1.00 33.96 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.940 -1.659  10.762 1.00 36.48 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 24.060 -1.814  12.275 1.00 42.79 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.853 -2.937  12.769 1.00 45.83 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 24.345 -0.792  12.968 1.00 42.96 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.853 -3.527  8.301  1.00 33.09 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.155 -3.578  7.001  1.00 33.72 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.900 -2.697  7.066  1.00 33.45 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 20.099 -2.867  7.996  1.00 33.70 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.721 -5.027  6.669  1.00 35.68 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.877 -5.831  6.438  1.00 37.22 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.834 -5.099  5.437  1.00 36.11 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.739 -1.737  6.140  1.00 32.61 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.542 -0.891  6.124  1.00 32.60 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.479 -1.587  5.276  1.00 32.84 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.782 -2.062  4.179  1.00 32.73 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.835 0.513   5.541  1.00 33.17 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 21.014 1.197   6.253  1.00 32.67 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.571 1.403   5.526  1.00 33.74 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.783 1.400   7.706  1.00 32.79 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.241 -1.633  5.760  1.00 32.88 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.148 -2.246  5.018  1.00 34.56 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.752 -1.348  3.815  1.00 35.10 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.812 -0.129  3.908  1.00 34.66 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.962 -2.448  5.954  1.00 34.45 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.476 -1.958  2.655  1.00 36.29 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.042 -1.258  1.437  1.00 37.53 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.783 -2.026  1.103  1.00 38.87 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.849 -3.118  0.542  1.00 39.09 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.111 -1.325  0.326  1.00 38.72 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.464 -0.790  0.790  1.00 40.01 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.481 0.688   1.153  1.00 40.36 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.819 1.109   1.558  1.00 40.00 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.114 2.285   2.106  1.00 38.77 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.156 3.156   2.379  1.00 37.45 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.358 2.571   2.445  1.00 36.75 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.651 -1.540  1.662  1.00 40.10 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.370 -2.235  1.655  1.00 40.24 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.218 -1.291  2.100  1.00 40.43 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.437 -0.116  2.413  1.00 40.81 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.475 -3.446  2.577  1.00 40.32 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.902 -3.009  4.292  1.00 43.38 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.990  -1.832  2.113  1.00 40.53 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.751  -1.123  2.459  1.00 40.97 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.030  -1.691  3.682  1.00 39.22 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.986  -1.144  4.055  1.00 38.46 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.774  -1.152  1.254  1.00 44.87 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 6.412  -2.535  0.748  1.00 53.77 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 7.086  -3.514  1.147  1.00 55.51 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 5.451  -2.645  -0.065 1.00 58.65 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.564  -2.806  4.261  1.00 37.62 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.075  -3.524  5.456  1.00 36.21 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.658  -2.568  6.592  1.00 33.97 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 7.352  -1.587  6.895  1.00 35.03 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.064  -4.604  5.923  1.00 36.09 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 9.804  -4.285  5.475  1.00 38.02 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.450  -2.784  7.125  1.00 30.95 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.829  -2.000  8.202  1.00 29.49 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.712  -2.764  9.518  1.00 26.75 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.829  -2.482  10.337 1.00 26.63 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.444  -1.470  7.797  1.00 31.72 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.457  -0.203  6.940  1.00 36.31 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 2.052  0.287   6.705  1.00 41.21 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.515  0.244   5.592  1.00 43.64 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 1.400  0.732   7.759  1.00 40.51 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.543  -3.782  9.700  1.00 25.77 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.609  -4.534  10.957 1.00 26.52 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.076  -4.731  11.214 1.00 25.65 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.880  -4.836  10.275 1.00 25.70 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.911  -5.937  10.916 1.00 29.40 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.451  -6.712  9.828  1.00 30.41 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.400  -5.860  10.806 1.00 29.96 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.429  -4.770  12.480 1.00 24.25 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.793  -5.003  12.890 1.00 23.81 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.930  -5.124  14.392 1.00 22.95 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.944  -5.307  15.103 1.00 21.92 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.151 -4.979  14.876 1.00 22.57 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.486 -5.124  16.288 1.00 21.01 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.390 -3.966  16.697 1.00 19.49 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.358 -3.694  15.999 1.00 19.83 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.247 -6.461  16.459 1.00 22.00 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.784 -6.619  17.869 1.00 24.11 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.377 -7.660  16.039 1.00 21.67 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.115 -3.333  17.820 1.00 18.48 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.977 -2.218  18.298 1.00 17.02 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.542 -2.477  19.677 1.00 19.40 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.881 -3.108  20.491 1.00 18.41 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.247 -0.850  18.195 1.00 17.43 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.312 -0.519  19.351 1.00 18.87 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 9.055  -1.098  19.443 1.00 19.07 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.696 0.365   20.358 1.00 19.37 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.177  -0.757  20.468 1.00 20.29 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.822  0.714   21.395 1.00 19.76 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.589  0.099   21.482 1.00 21.14 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.709  0.461   22.489 1.00 22.66 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.747 -1.971  19.940 1.00 20.34 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.360 -2.123  21.235 1.00 22.68 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.954 -0.942  22.123 1.00 23.22 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 14.039 0.210   21.700 1.00 21.56 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.886 -2.267  21.146 1.00 23.40 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.515 -2.375  22.525 1.00 25.14 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.226 -3.446  23.362 1.00 26.23 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.376 -1.396  22.999 1.00 26.22 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.792 -3.551  24.634 1.00 27.67 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.946 -1.486  24.270 1.00 27.43 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.647 -2.564  25.090 1.00 29.01 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 18.175 -2.657  26.366 1.00 32.08 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.481 -1.252  23.357 1.00 24.44 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 13.026 -0.304  24.371 1.00 25.75 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.973 -0.424  25.582 1.00 26.08 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.814 -1.348  26.389 1.00 25.31 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.585 -0.620  24.762 1.00 27.18 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.840 0.556   25.940 1.00 29.06 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.976 0.475   25.693 1.00 27.08 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.927 0.387   26.793 1.00 29.30 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 15.282 0.531   28.166 1.00 29.63 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.744 -0.112  29.109 1.00 31.72 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 17.082 1.365   26.624 1.00 33.29 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.651 2.709   26.713 1.00 38.45 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 14.203 1.317   28.270 1.00 29.87 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.481 1.554   29.535 1.00 32.31 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.724 0.320   30.067 1.00 33.99 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 12.093 0.388   31.121 1.00 34.74 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.553 2.760   29.405 1.00 33.19 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 11.448 2.474   28.564 1.00 36.28 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.755 -0.792  29.305 1.00 34.04 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 12.167 -2.061  29.664 1.00 33.94 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 13.159 -3.236  29.423 1.00 33.93 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.804 -4.386  29.698 1.00 34.04 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.877 -2.282  28.861 1.00 34.81 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.749  -1.286  29.146 1.00 37.65 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 9.039  -1.571  30.466 1.00 41.15 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.962  -0.612  30.716 1.00 43.34 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 8.114  0.539   31.363 1.00 47.25 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 9.307  0.897   31.830 1.00 46.50 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 7.083  1.359   31.521 1.00 48.40 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.367 -2.962  28.853 1.00 33.15 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.373 -3.950  28.432 1.00 33.97 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.720 -5.063  27.609 1.00 34.25 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 15.034 -6.234  27.806 1.00 35.24 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 16.194 -4.513  29.612 1.00 36.75 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 17.015 -3.470  30.356 1.00 41.00 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.956 -4.139  31.344 1.00 45.93 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.579 -3.180  32.257 1.00 50.58 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.400 -3.174  33.576 1.00 52.71 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.603 -4.070  34.150 1.00 53.11 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 19.000 -2.261  34.329 1.00 53.24 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.735 -4.686  26.763 1.00 32.73 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.928 -5.606  25.962 1.00 31.96 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.763 -5.106  24.500 1.00 30.25 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.811 -3.901  24.207 1.00 29.26 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.514 -5.736  26.583 1.00 33.74 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.372 -6.755  27.713 1.00 39.38 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 10.088 -6.554  28.516 1.00 44.54 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.998  -7.413  29.780 1.00 48.62 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.681 -6.810  30.975 1.00 50.01 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.513 -6.064  23.604 1.00 28.71 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.202 -5.827  22.200 1.00 27.72 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.714 -6.105  22.086 1.00 26.76 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.241 -7.113  22.634 1.00 27.53 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.978 -6.807  21.291 1.00 29.28 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.463 -6.601  21.290 1.00 31.40 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.096 -5.860  20.293 1.00 33.42 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.396 -7.049  22.161 1.00 32.04 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.383 -5.878  20.598 1.00 33.28 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.613 -6.571  21.716 1.00 33.07 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.959  -5.207  21.435 1.00 25.11 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.533  -5.358  21.263 1.00 24.07 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.175  -5.452  19.772 1.00 22.78 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.637  -4.631  18.991 1.00 22.64 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.808  -4.116  21.795 1.00 24.58 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.814  -3.971  23.307 1.00 25.64 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.996  -4.763  24.106 1.00 26.40 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.620  -3.025  23.934 1.00 26.55 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.981  -4.620  25.498 1.00 28.16 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.625  -2.884  25.324 1.00 27.54 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.784  -3.666  26.100 1.00 29.37 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.796  -3.550  27.473 1.00 33.19 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.309  -6.412  19.384 1.00 22.08 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.820  -6.450  17.980 1.00 21.55 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.722  -5.373  17.788 1.00 21.45 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.870  -5.211  18.668 1.00 22.73 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.230  -7.868  17.850 1.00 21.84 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.781  -8.218  19.253 1.00 22.67 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.675  -7.447  20.232 1.00 21.13 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.733  -4.635  16.686 1.00 20.61 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.753  -3.571  16.467 1.00 20.60 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.291  -3.501  15.012 1.00 21.72 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 5.022  -3.874  14.093 1.00 20.75 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.358  -2.176  16.855 1.00 20.95 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.514  -2.010  18.358 1.00 20.85 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.665  -1.908  16.108 1.00 19.88 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.107  -2.919  14.817 1.00 23.49 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.600  -2.482  13.520 1.00 25.64 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.787  -0.957  13.525 1.00 25.12 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.448  -0.308  14.514 1.00 24.72 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.133  -2.813  13.354 1.00 29.33 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 1.039  -4.165  12.944 1.00 34.28 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.349  -0.395  12.453 1.00 25.46 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.634  1.030   12.403 1.00 26.36 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 3.094  1.696   11.107 1.00 27.32 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.865  1.001   10.094 1.00 26.98 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 5.128  1.283   12.636 1.00 26.15 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 6.094  0.528   11.733 1.00 26.98 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.673  -0.659  12.146 1.00 27.59 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.496  1.061   10.518 1.00 27.96 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.554  -1.348  11.322 1.00 27.90 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.370  0.365   9.689  1.00 28.56 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.923  -0.814  10.112 1.00 28.17 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.788  3.009   11.164 1.00 27.47 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.243  3.694   9.988  1.00 28.06 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.362  4.002   8.948  1.00 27.68 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.531  3.938   9.298  1.00 25.67 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.495  4.956   10.410 1.00 29.03 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.408  5.839   11.034 1.00 30.62 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 3.019  4.305   7.669  1.00 28.89 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 4.037  4.648   6.662  1.00 30.24 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.670  6.007   7.071  1.00 31.95 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 4.058  6.745   7.854  1.00 31.42 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.395  4.734   5.236  1.00 31.82 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.952  3.366   4.704  1.00 37.82 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.490  3.398   3.251  1.00 44.69 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 1.755  2.115   2.945  1.00 49.66 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.694  1.818   1.485  1.00 53.18 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.914  6.325   6.657  1.00 33.53 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.525  7.595   7.103  1.00 35.11 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.719  8.816   6.638  1.00 37.69 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 5.170  8.819   5.525  1.00 37.89 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.939  7.530   6.527  1.00 35.62 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.832  6.628   5.356  1.00 35.84 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.819  5.582   5.760  1.00 33.60 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.564  9.811   7.530  1.00 38.86 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.735  10.965  7.218  1.00 40.02 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 5.005  12.191  8.114  1.00 40.35 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.849  12.143  9.017  1.00 39.49 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 3.261  10.566  7.291  1.00 42.37 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.875  10.323  8.634  1.00 45.51 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 4.269  13.295  7.846  1.00 40.85 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.339  14.532  8.608  1.00 42.84 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.381  14.379  9.757  1.00 44.19 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 2.186  14.214  9.529  1.00 44.89 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.877  15.721  7.748  1.00 43.30 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.946  16.454  7.002  1.00 45.45 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 4.310  17.514  6.053  1.00 46.45 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.887  17.136  7.964  1.00 46.60 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.900  14.430  10.988 1.00 44.23 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 3.114  14.288  12.207 1.00 45.30 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.452  15.459  13.139 1.00 47.03 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.613  15.843  13.242 1.00 46.96 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.435  12.902  12.866 1.00 45.20 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.712  11.763  12.131 1.00 46.21 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 3.126  12.873  14.368 1.00 45.07 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 3.508  10.539  12.060 1.00 47.74 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.447  16.008  13.827 1.00 48.34 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.671  17.100  14.766 1.00 49.91 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.327  16.567  16.069 1.00 49.71 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.862  15.589  16.650 1.00 49.11 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.346  17.839  15.054 1.00 50.82 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.472  18.963  16.050 1.00 52.94 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 2.095  20.147  15.705 1.00 54.53 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 0.957  18.840  17.326 1.00 54.35 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.227  21.178  16.628 1.00 56.05 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.079  19.873  18.242 1.00 55.75 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.707  21.040  17.886 1.00 56.05 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.427  17.203  16.502 1.00 49.59 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.140  16.814  17.717 1.00 49.89 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.180  18.004  18.679 1.00 51.75 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.655  19.084  18.299 1.00 51.71 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.572  16.308  17.411 1.00 49.17 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.313  15.972  18.697 1.00 48.86 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.547  15.103  16.465 1.00 49.15 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 4.687  17.808  19.930 1.00 52.76 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 4.682  18.840  20.983 1.00 54.12 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.097  19.371  21.267 1.00 54.59 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.090  18.746  20.875 1.00 54.75 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.070  18.275  22.283 1.00 56.88 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.672  17.717  22.121 1.00 61.98 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.578  18.764  22.155 1.00 69.47 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 1.699  19.736  22.939 1.00 70.53 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 0.591  18.607  21.401 1.00 71.63 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.194  20.509  21.966 1.00 54.87 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.482  21.124  22.283 1.00 55.17 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.306  20.324  23.285 1.00 54.97 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 7.753  19.611  24.128 1.00 55.45 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.268  22.528  22.816 1.00 55.71 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.634  20.449  23.182 1.00 53.92 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.623 19.837  24.075 1.00 53.62 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 11.795 20.840  24.262 1.00 54.18 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 11.752 21.927  23.674 1.00 55.60 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 11.129 18.516  23.493 1.00 52.83 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.979 18.730  22.377 1.00 52.60 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 12.842 20.495  25.047 1.00 53.72 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 13.988 21.422  25.224 1.00 54.19 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 14.925 21.467  23.985 1.00 53.49 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.810 22.323  23.910 1.00 54.08 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 14.786 21.124  26.520 1.00 57.21 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 15.743 19.931  26.433 1.00 64.57 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 16.729 19.823  27.592 1.00 72.76 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 17.793 19.181  27.419 1.00 73.21 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 16.441 20.394  28.670 1.00 75.73 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.716 20.565  23.014 1.00 52.04 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.542 20.502  21.808 1.00 51.39 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.874 21.163  20.611 1.00 50.56 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 15.563 21.597  19.692 1.00 51.06 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.890 19.040  21.448 1.00 51.21 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 16.398 18.219  22.611 1.00 51.42 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.742 18.222  22.956 1.00 52.39 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 15.535 17.443  23.369 1.00 51.73 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 18.217 17.456  24.014 1.00 53.15 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.995 16.690  24.440 1.00 52.45 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 17.341 16.675  24.742 1.00 53.64 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 17.799 15.911  25.791 1.00 55.18 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.540 21.199  20.590 1.00 49.36 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.788 21.743  19.468 1.00 48.54 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 11.520 22.442  19.949 1.00 51.08 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.881 21.980  20.902 1.00 51.37 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 12.301 20.581  18.553 1.00 46.21 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 13.365 19.713  17.920 1.00 43.69 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 14.074 20.149  16.809 1.00 42.88 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.563 18.404  18.341 1.00 42.57 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 15.001 19.328  16.179 1.00 42.43 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.507 17.584  17.736 1.00 41.73 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 15.210 18.039  16.641 1.00 41.33 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 16.198 17.273  16.070 1.00 39.10 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 11.040 23.453  19.200 1.00 52.68 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.689  23.989  19.490 1.00 53.85 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 8.620  22.974  18.979 1.00 55.07 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.976  21.996  18.310 1.00 54.97 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.646  25.267  18.654 1.00 54.81 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.517 24.953  17.473 1.00 54.99 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.624 24.054  17.980 1.00 52.65 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 7.321  23.216  19.238 1.00 55.04 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 6.277  22.326  18.724 1.00 55.28 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 6.220  22.542  17.198 1.00 54.79 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.988  23.658  16.749 1.00 55.36 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.935  22.665  19.365 1.00 55.83 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 6.505  21.499  16.413 1.00 53.12 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.542  21.593  14.950 1.00 51.53 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.942  20.296  14.300 1.00 51.35 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.388  19.458  15.009 1.00 52.25 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 8.014  21.815  14.519 1.00 50.60 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.867  20.512  14.584 1.00 50.43 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 10.203 20.624  15.281 1.00 49.94 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 11.147 19.607  14.800 1.00 49.66 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 11.216 18.360  15.258 1.00 47.04 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 12.095 17.506  14.748 1.00 42.89 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.396 17.954  16.222 1.00 46.59 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 6.059  20.135  12.961 1.00 50.10 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.681  18.923  12.240 1.00 49.17 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.978  18.229  11.899 1.00 46.42 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.867  18.858  11.319 1.00 46.52 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.971  19.251  10.919 1.00 50.48 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.518  19.599  11.105 1.00 52.55 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 2.584  18.621  11.406 1.00 53.55 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 3.081  20.915  11.016 1.00 53.89 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 1.252  18.938  11.610 1.00 54.97 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.745  21.244  11.205 1.00 55.04 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.838  20.254  11.523 1.00 56.62 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.478 20.579  11.726 1.00 59.29 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 7.114  16.952  12.262 1.00 43.49 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 8.318  16.202  11.937 1.00 41.05 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 8.002  15.285  10.741 1.00 39.77 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.975  14.608  10.742 1.00 40.01 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.835  15.454  13.186 1.00 40.62 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.943  14.449  12.919 1.00 39.99 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.676 14.025  14.180 1.00 40.99 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.934 14.820  15.101 1.00 40.90 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 11.071 12.767  14.223 1.00 39.64 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.831  15.308  9.697  1.00 38.71 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.594  14.492  8.498  1.00 38.15 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.260  13.102  8.586  1.00 36.48 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 10.057 12.845  9.512  1.00 35.26 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 9.081  15.229  7.249  1.00 41.22 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.487 15.396  7.306  1.00 44.88 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.878  12.191  7.645  1.00 35.56 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.408  10.819  7.575  1.00 35.83 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 9.286  10.064  8.931  1.00 33.06 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 10.133 9.238   9.273  1.00 32.14 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.867 10.859  7.084  1.00 38.18 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 11.024 11.482  5.737  1.00 42.00 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.991 10.721  4.590  1.00 44.65 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 11.200 12.779  5.394  1.00 43.49 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 11.142 11.570  3.587  1.00 45.13 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 11.273 12.818  4.023  1.00 44.82 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 8.237  10.386  9.707  1.00 32.11 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.975  9.786   11.014 1.00 31.34 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.950  8.628   10.937 1.00 30.35 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.953  8.737   10.239 1.00 31.41 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.483  10.860  11.984 1.00 31.30 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.408  10.496  13.477 1.00 32.39 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.750  10.028  14.023 1.00 32.91 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.879  11.673  14.303 1.00 33.56 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 7.192  7.534   11.650 1.00 28.97 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 6.275  6.368   11.642 1.00 27.67 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.747  6.095   13.061 1.00 27.78 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.537  6.052   14.007 1.00 28.05 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.978  5.128   11.056 1.00 27.80 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.543  5.316   9.619  1.00 30.32 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.677  3.942   9.168  1.00 33.74 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.917  4.110   10.395 1.00 30.19 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.428  5.925   13.233 1.00 27.57 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.842  5.727   14.570 1.00 27.20 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.307  4.324   14.828 1.00 26.48 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.616  3.757   13.963 1.00 26.85 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.668  6.713   14.792 1.00 27.75 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 3.013  8.204   14.989 1.00 29.88 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.748  9.014   15.221 1.00 30.84 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.929  8.389   16.136 1.00 30.77 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.549  3.825   16.047 1.00 25.21 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 3.074  2.549   16.582 1.00 25.17 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.539  2.742   18.013 1.00 24.24 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.959  3.662   18.726 1.00 24.10 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.212  1.528   16.603 1.00 25.72 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.642  1.854   18.435 1.00 23.72 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.118  1.812   19.795 1.00 23.68 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.213  1.068   20.612 1.00 23.61 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.522  -0.101  20.335 1.00 23.22 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.249 1.068   19.846 1.00 24.77 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.722 0.887   21.288 1.00 26.08 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.318 1.802   19.028 1.00 25.63 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.864  1.788   21.525 1.00 23.70 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.906  1.185   22.334 1.00 24.23 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.533  2.112   23.342 1.00 26.53 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.293  3.326   23.330 1.00 27.48 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 5.309  1.512   24.265 1.00 26.80 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.966  2.254   25.314 1.00 27.58 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 7.261  2.953   24.874 1.00 27.32 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 8.062  2.403   24.117 1.00 26.37 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 6.212  1.352   26.550 1.00 29.68 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.882  2.073   27.673 1.00 33.62 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 6.303  3.191   28.252 1.00 35.90 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 8.081  1.849   28.263 1.00 35.79 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 7.150  3.596   29.191 1.00 37.24 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 8.238  2.826   29.232 1.00 37.47 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 7.511  4.126   25.462 1.00 28.42 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.743  4.884   25.281 1.00 29.80 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.911  5.947   26.392 1.00 31.44 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 7.961  6.301   27.077 1.00 30.88 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.818  5.528   23.895 1.00 30.89 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.992  6.678   23.777 1.00 33.40 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 10.143 6.412   26.569 1.00 32.56 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 10.576 7.498   27.460 1.00 33.38 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 11.656 8.265   26.695 1.00 33.95 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 12.298 7.658   25.838 1.00 33.87 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 11.172 6.959   28.768 1.00 35.52 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 10.412 5.782   29.323 1.00 39.76 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 10.446 5.647   30.820 1.00 43.83 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 11.308 6.291   31.461 1.00 45.21 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 9.586  4.912   31.355 1.00 44.02 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 11.953 9.548   27.015 1.00 34.36 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.962 10.280  26.222 1.00 34.08 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 14.303 9.552   26.018 1.00 33.75 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 14.868 9.622   24.925 1.00 34.32 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 13.110 11.616  26.963 1.00 34.70 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 12.324 11.456  28.277 1.00 35.10 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 11.273 10.442  27.968 1.00 33.55 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.761 8.814   27.030 1.00 33.49 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 16.004 8.040   26.989 1.00 33.04 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 16.005 6.834   26.060 1.00 31.86 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 17.049 6.217   25.828 1.00 31.36 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.837 6.493   25.504 1.00 31.43 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.659 5.403   24.557 1.00 30.25 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 15.015 5.793   23.117 1.00 28.66 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 15.163 4.887   22.275 1.00 28.27 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 13.230 4.858   24.608 1.00 31.67 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.990 4.010   25.837 1.00 33.61 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.868 3.197   26.173 1.00 33.65 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.936 4.173   26.471 1.00 35.36 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 15.186 7.129   22.823 1.00 27.62 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.565 7.588   21.472 1.00 27.03 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.901 6.934   21.097 1.00 25.64 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.772 6.819   21.953 1.00 26.06 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.639 9.106   21.375 1.00 28.30 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 14.066 9.949   21.686 1.00 33.28 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 17.012 6.462   19.877 1.00 23.77 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 18.211 5.767   19.443 1.00 23.66 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.990 4.270   19.306 1.00 23.40 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.740 3.600   18.594 1.00 23.23 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.957 3.749   19.969 1.00 22.81 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.584 2.348   19.897 1.00 22.74 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 16.199 1.982   18.469 1.00 22.72 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.469 2.729   17.801 1.00 22.05 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.752 0.883   17.971 1.00 22.82 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.532 0.493   16.585 1.00 23.33 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.195 -0.238  16.378 1.00 22.39 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.812 -1.066  17.208 1.00 22.93 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.782 -0.334  16.084 1.00 25.52 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.978 0.604   15.777 1.00 26.70 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.457 -1.188  14.845 1.00 27.01 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.236 -0.098  15.325 1.00 28.49 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.489 0.077   15.274 1.00 21.48 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.307 -0.623  14.758 1.00 21.21 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.863 -1.460  13.570 1.00 22.55 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.619 -0.949  12.717 1.00 22.75 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.211 0.350   14.248 1.00 21.13 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 11.004 -0.305  13.500 1.00 21.69 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.087 -1.090  14.444 1.00 21.77 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 10.144 0.782   12.794 1.00 22.32 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.479 -2.727  13.516 1.00 22.90 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 14.071 -3.625  12.546 1.00 24.77 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 13.019 -4.596  11.988 1.00 25.91 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 12.103 -4.992  12.700 1.00 25.44 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 15.220 -4.319  13.304 1.00 27.41 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.069 -5.268  12.522 1.00 33.63 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.004 -6.032  13.468 1.00 38.34 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 18.273 -5.343  13.722 1.00 42.30 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 19.295 -5.300  12.863 1.00 43.13 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.193 -5.872  11.668 1.00 41.05 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 20.409 -4.649  13.180 1.00 42.92 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 13.095 -4.882  10.691 1.00 27.21 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 12.205 -5.859  10.052 1.00 28.71 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 13.103 -7.011  9.537  1.00 31.18 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.327 -6.964  9.689  1.00 31.01 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.445 -5.199  8.904  1.00 30.03 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.528 -4.573  7.584  1.00 29.87 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.512 -8.035  8.897  1.00 33.63 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.280 -9.140  8.321  1.00 36.45 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.329 -8.652  7.292  1.00 37.66 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.273 -9.394  7.011  1.00 39.50 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.328 -10.167 7.655  1.00 40.44 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.327 -9.500  6.700  1.00 46.09 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.487 -10.422 5.845  1.00 53.63 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.430  -10.017 5.340  1.00 55.75 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.922 -11.668 5.640  1.00 55.63 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 14.169 -7.431  6.734  1.00 36.54 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 15.105 -6.882  5.738  1.00 36.66 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.264 -6.048  6.334  1.00 34.81 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.139 -5.616  5.592  1.00 34.75 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.363 -6.021  4.696  1.00 38.75 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.353 -6.757  3.862  1.00 41.75 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 12.325 -7.462  4.436  1.00 43.86 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 13.221 -6.824  2.518  1.00 43.42 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 11.608 -7.944  3.438  1.00 44.68 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 12.106 -7.584  2.265  1.00 44.31 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.262 -5.813  7.647  1.00 32.83 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.305 -5.015  8.292  1.00 30.96 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.771 -3.804  9.046  1.00 29.53 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.596 -3.775  9.413  1.00 29.58 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.649 -2.807  9.323  1.00 28.01 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.304 -1.587  10.054 1.00 26.85 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.312 -0.685  9.309  1.00 26.10 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.580 -0.255  8.165  1.00 27.52 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.559 -0.782  10.492 1.00 27.87 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 18.148 0.488   11.222 1.00 28.11 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.489 -1.623  11.352 1.00 27.76 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 15.181 -0.372  9.959  1.00 24.47 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 14.108 0.480   9.395  1.00 26.13 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.263 1.953   9.837  1.00 25.87 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 14.136 2.883   9.052  1.00 26.01 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.704 -0.096  9.773  1.00 27.19 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.580 0.869   9.399  1.00 28.40 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.483 -1.457  9.132  1.00 27.10 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.561 2.141   11.113 1.00 24.50 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.774 3.468   11.670 1.00 23.76 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 15.081 3.416   13.161 1.00 23.61 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.295 2.327   13.710 1.00 22.29 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 15.127 4.589   13.810 1.00 23.99 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.429 4.687   15.240 1.00 24.44 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 14.319 5.464   15.991 1.00 24.77 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.696 6.380   15.408 1.00 24.75 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.820 5.339   15.422 1.00 25.63 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.896 6.686   14.732 1.00 26.74 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.954 4.415   14.951 1.00 25.87 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 18.099 7.486   15.155 1.00 27.17 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 14.081 5.135   17.305 1.00 23.85 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 13.086 5.822   18.140 1.00 23.21 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.434 7.313   18.143 1.00 24.10 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.595 7.647   18.359 1.00 24.01 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 13.065 5.291   19.598 1.00 23.30 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 12.125 6.140   20.452 1.00 23.58 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.654 3.819   19.656 1.00 23.95 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.450 8.185   17.853 1.00 25.40 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.655 9.622   17.802 1.00 26.93 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.667 10.363  18.740 1.00 28.23 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 12.050 11.341  19.396 1.00 28.77 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.498 10.134  16.372 1.00 28.64 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.820 11.517  16.286 1.00 29.53 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.407 9.890   18.805 1.00 27.95 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 9.364  10.554  19.599 1.00 28.98 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.493  9.567   20.398 1.00 30.55 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.492  8.373   20.110 1.00 29.90 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.444  11.399  18.656 1.00 29.81 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.692  10.529  17.815 1.00 31.35 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 9.203  12.359  17.783 1.00 31.36 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.716  10.088  21.347 1.00 31.56 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.779  9.296   22.133 1.00 32.72 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.825  10.184  22.906 1.00 33.62 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 6.139  11.344  23.187 1.00 34.64 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.671  9.636   23.251 1.00 33.93 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.626  10.315  24.009 1.00 35.24 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.254  9.694   23.816 1.00 37.17 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.939  9.215   22.720 1.00 37.89 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.425  9.691   24.885 1.00 37.51 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.058  9.166   24.847 1.00 37.82 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.036 7.662   24.459 1.00 36.32 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.012 7.254   23.841 1.00 36.06 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.824 10.013  23.888 1.00 40.34 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.874 11.507  24.163 1.00 46.55 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.605 11.985  25.273 1.00 47.14 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.253 12.283  23.146 1.00 48.87 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.976  6.866   24.794 1.00 35.34 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.991  5.448   24.442 1.00 34.21 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.320  5.154   22.981 1.00 32.63 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.990  4.087   22.457 1.00 32.06 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.966  6.109   22.318 1.00 32.01 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.383  6.028   20.928 1.00 32.22 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.878  6.287   20.887 1.00 30.61 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.382  7.123   21.634 1.00 30.67 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.655  7.086   20.073 1.00 34.23 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.147  7.032   20.084 1.00 37.39 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.447 8.374   19.731 1.00 38.92 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.366 5.935   19.164 1.00 38.94 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.593  5.548   20.028 1.00 28.99 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 6.022  5.685   19.828 1.00 27.29 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.276  5.975   18.346 1.00 26.29 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.673  5.338   17.478 1.00 25.19 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.813  4.445   20.352 1.00 27.14 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.269  3.134   19.776 1.00 27.05 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.306  4.593   20.088 1.00 27.62 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 7.118  6.972   18.084 1.00 26.42 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.487  7.382   16.739 1.00 27.22 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.913  7.030   16.362 1.00 26.98 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.843  7.234   17.143 1.00 28.21 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 9.092  6.556   15.151 1.00 25.83 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.386 6.168   14.598 1.00 25.90 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.753 6.998   13.390 1.00 25.75 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.942  7.142   12.475 1.00 25.10 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.372 4.691   14.155 1.00 25.29 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.844  3.752   15.220 1.00 25.08 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.660 3.322   16.254 1.00 25.28 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.550  3.270   15.160 1.00 25.51 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 10.179 2.464   17.227 1.00 25.38 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 8.079  2.382   16.124 1.00 26.29 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.893  2.007   17.167 1.00 25.66 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.991 7.534   13.386 1.00 25.88 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.550 8.266   12.265 1.00 26.40 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.971 7.250   11.198 1.00 26.50 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.929 6.504   11.422 1.00 26.00 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.772 9.038   12.724 1.00 27.68 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 12.298 7.231   10.038 1.00 26.74 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.638 6.279   8.983  1.00 27.90 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 14.017 6.594   8.364  1.00 29.10 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.402 7.758   8.307  1.00 30.78 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.534 6.278   7.886  1.00 30.67 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.764 5.239   6.825  1.00 35.52 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.967 4.065   7.182  1.00 34.74 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.772 5.610   5.617  1.00 40.10 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.791 5.564   7.955  1.00 28.27 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 16.073 5.789   7.276  1.00 29.39 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 16.161 5.041   5.918  1.00 30.21 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.171 5.170   5.240  1.00 31.49 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.292 5.408   8.133  1.00 30.01 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.400 6.272   9.383  1.00 30.13 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.282 3.910   8.457  1.00 30.05 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 15.132 4.242   5.543  1.00 30.14 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 15.079 3.414   4.336  1.00 31.25 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 15.160 4.188   3.018  1.00 34.76 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.524 3.596   2.003  1.00 36.58 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.834 2.495   4.326  1.00 30.62 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.771 1.491   5.487  1.00 31.06 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 12.463 0.715   5.440  1.00 32.98 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 11.356 1.578   5.859  1.00 34.98 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 10.100 1.176   6.012  1.00 34.94 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.757  -0.074  5.729  1.00 32.65 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 9.171  2.031   6.427  1.00 34.98 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.797 5.471   3.007  1.00 36.38 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.869 6.296   1.779  1.00 38.28 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 16.295 6.862   1.528  1.00 39.29 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.564 7.415   0.434  1.00 39.52 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.864 7.464   1.867  1.00 41.11 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 14.192 8.475   2.960  1.00 47.50 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.725 8.061   4.013  1.00 47.96 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.913 9.676   2.763  1.00 49.97 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.186 6.798   2.580  1.00 38.80 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.562 7.292   2.480  1.00 38.27 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.448 6.245   1.779  1.00 37.56 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 20.242 5.553   2.428  1.00 36.29 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 19.111 7.684   3.872  1.00 38.14 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 18.221 8.640   4.686  1.00 39.43 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.804 8.893   6.088  1.00 40.55 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.986 9.954   3.951  1.00 40.49 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 19.287 6.124   0.442  1.00 37.51 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.991 5.148   -0.395 1.00 38.86 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.502 5.313   -0.391 1.00 40.08 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 22.209 4.309   -0.511 1.00 41.38 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.449 5.114   -1.868 1.00 39.17 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.941 5.076   -2.037 1.00 41.13 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.538 5.042   -3.516 1.00 42.30 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.314 3.916   -1.243 1.00 42.16 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 22.003 6.552   -0.190 1.00 39.20 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.438 6.840   -0.149 1.00 39.15 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 24.181 6.260   1.079  1.00 39.71 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.403 6.199   1.055  1.00 40.23 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.717 8.347   -0.284 1.00 38.32 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.981 9.198   0.708  1.00 37.80 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.773 9.803   0.528  1.00 38.37 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 23.398 9.521   2.048  1.00 37.26 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 21.428 10.515  1.654  1.00 38.65 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 22.409 10.355  2.604  1.00 37.94 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.537 9.232   2.808  1.00 37.27 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.522 10.894  3.884  1.00 38.22 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.624 9.734   4.093  1.00 38.05 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.634 10.568  4.610  1.00 38.17 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.477 5.841   2.136  1.00 40.12 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 24.147 5.237   3.307  1.00 41.24 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.941 3.962   2.899  1.00 44.91 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.936 3.629   3.546  1.00 45.52 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 23.114 4.881   4.384  1.00 39.56 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.476 6.064   5.066  1.00 39.30 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.304 5.639   5.908  1.00 39.04 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.492 6.801   5.932  1.00 39.92 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.499 3.278   1.818  1.00 46.96 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 25.064 2.048   1.265  1.00 49.81 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 26.149 2.222   0.217  1.00 52.62 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.457 1.257   -0.483 1.00 52.97 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.945 1.214   0.628  1.00 51.94 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 23.056 0.527   1.634  1.00 56.53 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 23.500 0.337   2.785  1.00 57.71 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.919 0.184   1.276  1.00 58.77 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 26.717 3.423   0.082  1.00 54.48 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 27.760 3.655   -0.913 1.00 56.72 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 28.820 4.640   -0.419 1.00 57.91 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 29.684 5.057   -1.198 1.00 58.89 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 27.149 4.111   -2.250 1.00 60.27 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 26.205 5.294   -2.122 1.00 66.47 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 25.397 5.605   -3.368 1.00 74.34 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 25.188 6.807   -3.660 1.00 75.01 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 24.966 4.646   -4.049 1.00 77.05 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1BOC B 2 .   ? 8.729  11.198  25.204 1.00 36.45 ? 201 A1BOC A N1  1 
HETATM 1079 N  N3  . A1BOC B 2 .   ? 12.072 14.283  17.701 1.00 36.41 ? 201 A1BOC A N3  1 
HETATM 1080 C  C4  . A1BOC B 2 .   ? 10.645 12.159  23.896 1.00 35.32 ? 201 A1BOC A C4  1 
HETATM 1081 C  C5  . A1BOC B 2 .   ? 10.143 12.899  22.671 1.00 35.07 ? 201 A1BOC A C5  1 
HETATM 1082 C  C6  . A1BOC B 2 .   ? 11.948 14.595  23.064 1.00 35.88 ? 201 A1BOC A C6  1 
HETATM 1083 C  C7  . A1BOC B 2 .   ? 13.263 14.673  22.286 1.00 36.35 ? 201 A1BOC A C7  1 
HETATM 1084 C  C8  . A1BOC B 2 .   ? 13.051 15.211  20.867 1.00 36.63 ? 201 A1BOC A C8  1 
HETATM 1085 C  C10 . A1BOC B 2 .   ? 11.698 15.019  18.737 1.00 37.06 ? 201 A1BOC A C10 1 
HETATM 1086 C  C13 . A1BOC B 2 .   ? 7.470  12.232  27.050 1.00 37.07 ? 201 A1BOC A C13 1 
HETATM 1087 C  C15 . A1BOC B 2 .   ? 7.076  9.803   26.440 1.00 36.44 ? 201 A1BOC A C15 1 
HETATM 1088 O  O1  . A1BOC B 2 .   ? 11.118 16.101  18.612 1.00 37.04 ? 201 A1BOC A O1  1 
HETATM 1089 C  C9  . A1BOC B 2 .   ? 11.969 14.429  20.112 1.00 36.49 ? 201 A1BOC A C9  1 
HETATM 1090 C  C11 . A1BOC B 2 .   ? 10.687 14.528  20.940 1.00 36.12 ? 201 A1BOC A C11 1 
HETATM 1091 N  N2  . A1BOC B 2 .   ? 10.895 13.944  22.266 1.00 35.57 ? 201 A1BOC A N2  1 
HETATM 1092 O  O   . A1BOC B 2 .   ? 9.135  12.548  22.068 1.00 33.95 ? 201 A1BOC A O   1 
HETATM 1093 C  C3  . A1BOC B 2 .   ? 9.778  11.021  24.330 1.00 35.82 ? 201 A1BOC A C3  1 
HETATM 1094 C  C1  . A1BOC B 2 .   ? 9.801  9.662   24.041 1.00 35.41 ? 201 A1BOC A C1  1 
HETATM 1095 C  C   . A1BOC B 2 .   ? 10.728 8.870   23.178 1.00 34.98 ? 201 A1BOC A C   1 
HETATM 1096 C  C12 . A1BOC B 2 .   ? 8.189  12.467  25.733 1.00 36.88 ? 201 A1BOC A C12 1 
HETATM 1097 C  C14 . A1BOC B 2 .   ? 6.451  11.112  26.924 1.00 36.82 ? 201 A1BOC A C14 1 
HETATM 1098 C  C2  . A1BOC B 2 .   ? 8.173  9.960   25.432 1.00 36.38 ? 201 A1BOC A C2  1 
HETATM 1099 N  N   . A1BOC B 2 .   ? 8.793  9.026   24.735 1.00 35.73 ? 201 A1BOC A N   1 
HETATM 1100 ZN ZN  . ZN    C 3 .   ? 11.638 -5.263  5.610  1.00 48.30 2 202 ZN    A ZN  1 
HETATM 1101 S  S   . DMS   D 4 .   ? 19.563 20.706  5.580  0.00 30.52 ? 203 DMS   A S   1 
HETATM 1102 O  O   . DMS   D 4 .   ? 20.159 21.709  6.522  0.00 22.35 ? 203 DMS   A O   1 
HETATM 1103 C  C1  . DMS   D 4 .   ? 18.109 21.473  4.816  0.00 27.05 ? 203 DMS   A C1  1 
HETATM 1104 C  C2  . DMS   D 4 .   ? 20.577 20.700  4.077  0.00 26.99 ? 203 DMS   A C2  1 
HETATM 1105 S  S   . DMS   E 4 .   ? 20.233 -0.184  19.701 1.00 60.52 ? 204 DMS   A S   1 
HETATM 1106 O  O   . DMS   E 4 .   ? 18.761 -0.403  19.453 1.00 59.62 ? 204 DMS   A O   1 
HETATM 1107 C  C1  . DMS   E 4 .   ? 20.519 0.508   21.356 1.00 60.34 ? 204 DMS   A C1  1 
HETATM 1108 C  C2  . DMS   E 4 .   ? 20.908 1.227   18.766 1.00 60.42 ? 204 DMS   A C2  1 
HETATM 1109 S  S   . DMS   F 4 .   ? 3.825  10.989  18.797 1.00 60.64 ? 205 DMS   A S   1 
HETATM 1110 O  O   . DMS   F 4 .   ? 4.704  12.027  18.134 1.00 60.58 ? 205 DMS   A O   1 
HETATM 1111 C  C1  . DMS   F 4 .   ? 3.422  11.534  20.472 1.00 60.54 ? 205 DMS   A C1  1 
HETATM 1112 C  C2  . DMS   F 4 .   ? 4.858  9.610   19.288 1.00 60.42 ? 205 DMS   A C2  1 
HETATM 1113 O  O   . HOH   G 5 .   ? 22.887 -1.585  4.191  1.00 26.20 ? 301 HOH   A O   1 
HETATM 1114 O  O   . HOH   G 5 .   ? 23.705 -0.092  16.099 1.00 40.12 ? 302 HOH   A O   1 
HETATM 1115 O  O   . HOH   G 5 .   ? 3.011  7.981   9.908  1.00 47.79 ? 303 HOH   A O   1 
HETATM 1116 O  O   . HOH   G 5 .   ? 20.662 8.395   19.096 1.00 22.87 ? 304 HOH   A O   1 
HETATM 1117 O  O   . HOH   G 5 .   ? 24.557 21.522  8.166  1.00 26.60 ? 305 HOH   A O   1 
HETATM 1118 O  O   . HOH   G 5 .   ? 10.464 4.956   3.483  1.00 38.50 ? 306 HOH   A O   1 
HETATM 1119 O  O   . HOH   G 5 .   ? 15.266 8.003   -1.733 1.00 33.26 ? 307 HOH   A O   1 
HETATM 1120 O  O   . HOH   G 5 .   ? 11.939 11.476  11.404 1.00 25.80 ? 308 HOH   A O   1 
HETATM 1121 O  O   . HOH   G 5 .   ? 18.413 2.471   22.970 1.00 25.90 ? 309 HOH   A O   1 
HETATM 1122 O  O   . HOH   G 5 .   ? 10.385 4.018   33.724 1.00 57.17 ? 310 HOH   A O   1 
HETATM 1123 O  O   . HOH   G 5 .   ? 1.173  -2.366  19.956 1.00 26.69 ? 311 HOH   A O   1 
HETATM 1124 O  O   . HOH   G 5 .   ? 11.072 7.981   4.600  1.00 42.27 ? 312 HOH   A O   1 
HETATM 1125 O  O   . HOH   G 5 .   ? 6.238  -5.196  28.902 1.00 38.32 ? 313 HOH   A O   1 
HETATM 1126 O  O   . HOH   G 5 .   ? 18.501 20.872  9.294  1.00 27.37 ? 314 HOH   A O   1 
HETATM 1127 O  O   . HOH   G 5 .   ? 11.992 1.888   33.357 1.00 32.12 ? 315 HOH   A O   1 
HETATM 1128 O  O   . HOH   G 5 .   ? 15.111 2.261   23.094 1.00 23.81 ? 316 HOH   A O   1 
HETATM 1129 O  O   . HOH   G 5 .   ? 3.493  21.756  22.833 1.00 47.59 ? 317 HOH   A O   1 
HETATM 1130 O  O   . HOH   G 5 .   ? 10.370 18.131  20.277 1.00 44.05 ? 318 HOH   A O   1 
HETATM 1131 O  O   . HOH   G 5 .   ? 22.354 18.738  17.324 1.00 37.23 ? 319 HOH   A O   1 
HETATM 1132 O  O   . HOH   G 5 .   ? 3.975  -4.646  21.222 1.00 31.91 ? 320 HOH   A O   1 
HETATM 1133 O  O   . HOH   G 5 .   ? 16.214 11.840  23.855 1.00 32.37 ? 321 HOH   A O   1 
HETATM 1134 O  O   . HOH   G 5 .   ? 3.893  4.408   27.597 1.00 41.28 ? 322 HOH   A O   1 
HETATM 1135 O  O   . HOH   G 5 .   ? 23.793 18.097  19.217 1.00 37.58 ? 323 HOH   A O   1 
HETATM 1136 O  O   . HOH   G 5 .   ? 30.141 3.064   10.400 1.00 22.66 ? 324 HOH   A O   1 
HETATM 1137 O  O   . HOH   G 5 .   ? 19.600 8.796   25.664 1.00 26.83 ? 325 HOH   A O   1 
HETATM 1138 O  O   . HOH   G 5 .   ? 35.574 15.108  8.824  1.00 51.84 ? 326 HOH   A O   1 
HETATM 1139 O  O   . HOH   G 5 .   ? 0.394  2.125   24.360 1.00 29.19 ? 327 HOH   A O   1 
HETATM 1140 O  O   . HOH   G 5 .   ? 5.325  5.785   24.183 1.00 24.65 ? 328 HOH   A O   1 
HETATM 1141 O  O   . HOH   G 5 .   ? 19.997 -0.609  26.982 1.00 31.29 ? 329 HOH   A O   1 
HETATM 1142 O  O   . HOH   G 5 .   ? 36.484 15.281  15.109 1.00 49.70 ? 330 HOH   A O   1 
HETATM 1143 O  O   . HOH   G 5 .   ? 18.522 18.661  16.970 1.00 25.61 ? 331 HOH   A O   1 
HETATM 1144 O  O   . HOH   G 5 .   ? 3.930  -5.050  6.343  1.00 36.91 ? 332 HOH   A O   1 
HETATM 1145 O  O   . HOH   G 5 .   ? 7.368  3.736   33.052 1.00 41.67 ? 333 HOH   A O   1 
HETATM 1146 O  O   . HOH   G 5 .   ? 0.463  -0.103  16.561 1.00 19.28 ? 334 HOH   A O   1 
HETATM 1147 O  O   . HOH   G 5 .   ? 31.779 20.262  17.015 1.00 33.08 ? 335 HOH   A O   1 
HETATM 1148 O  O   . HOH   G 5 .   ? 30.940 10.663  19.318 1.00 33.61 ? 336 HOH   A O   1 
HETATM 1149 O  O   . HOH   G 5 .   ? 29.026 -2.262  12.824 1.00 33.23 ? 337 HOH   A O   1 
HETATM 1150 O  O   . HOH   G 5 .   ? 4.498  1.099   1.413  1.00 62.93 ? 338 HOH   A O   1 
HETATM 1151 O  O   . HOH   G 5 .   ? 24.258 2.182   19.484 1.00 35.38 ? 339 HOH   A O   1 
HETATM 1152 O  O   . HOH   G 5 .   ? 30.041 4.417   3.468  1.00 51.67 ? 340 HOH   A O   1 
HETATM 1153 O  O   . HOH   G 5 .   ? 6.317  1.469   6.199  1.00 38.13 ? 341 HOH   A O   1 
HETATM 1154 O  O   . HOH   G 5 .   ? 11.135 17.391  5.275  1.00 47.54 ? 342 HOH   A O   1 
HETATM 1155 O  O   . HOH   G 5 .   ? 0.290  4.189   6.637  1.00 37.05 ? 343 HOH   A O   1 
HETATM 1156 O  O   . HOH   G 5 .   ? 5.448  -1.408  24.060 1.00 23.11 ? 344 HOH   A O   1 
HETATM 1157 O  O   . HOH   G 5 .   ? 19.154 4.075   25.952 1.00 39.00 ? 345 HOH   A O   1 
HETATM 1158 O  O   . HOH   G 5 .   ? 4.290  -2.095  21.717 1.00 35.92 ? 346 HOH   A O   1 
HETATM 1159 O  O   . HOH   G 5 .   ? 1.378  -2.632  17.312 1.00 21.44 ? 347 HOH   A O   1 
HETATM 1160 O  O   . HOH   G 5 .   ? 13.225 10.408  9.427  1.00 24.15 ? 348 HOH   A O   1 
HETATM 1161 O  O   . HOH   G 5 .   ? 31.763 2.329   12.657 1.00 29.54 ? 349 HOH   A O   1 
HETATM 1162 O  O   . HOH   G 5 .   ? 18.704 0.297   30.015 1.00 39.11 ? 350 HOH   A O   1 
HETATM 1163 O  O   . HOH   G 5 .   ? 23.190 18.690  5.840  1.00 40.78 ? 351 HOH   A O   1 
HETATM 1164 O  O   . HOH   G 5 .   ? 15.148 -4.410  17.257 1.00 25.24 ? 352 HOH   A O   1 
HETATM 1165 O  O   . HOH   G 5 .   ? 20.336 23.387  15.739 1.00 30.78 ? 353 HOH   A O   1 
HETATM 1166 O  O   . HOH   G 5 .   ? 12.535 -8.096  13.195 1.00 34.56 ? 354 HOH   A O   1 
HETATM 1167 O  O   . HOH   G 5 .   ? 3.940  7.410   25.892 1.00 36.64 ? 355 HOH   A O   1 
HETATM 1168 O  O   . HOH   G 5 .   ? 22.633 8.646   20.904 1.00 26.32 ? 356 HOH   A O   1 
HETATM 1169 O  O   . HOH   G 5 .   ? 9.372  2.860   3.034  1.00 43.50 ? 357 HOH   A O   1 
HETATM 1170 O  O   . HOH   G 5 .   ? 8.715  -7.620  8.884  1.00 37.47 ? 358 HOH   A O   1 
HETATM 1171 O  O   . HOH   G 5 .   ? 14.654 20.981  7.525  1.00 47.76 ? 359 HOH   A O   1 
HETATM 1172 O  O   . HOH   G 5 .   ? 7.810  16.384  23.347 1.00 34.63 ? 360 HOH   A O   1 
HETATM 1173 O  O   . HOH   G 5 .   ? 24.845 7.009   20.493 1.00 37.49 ? 361 HOH   A O   1 
HETATM 1174 O  O   . HOH   G 5 .   ? 18.432 11.774  0.909  1.00 53.25 ? 362 HOH   A O   1 
HETATM 1175 O  O   . HOH   G 5 .   ? 7.041  12.046  4.826  1.00 38.06 ? 363 HOH   A O   1 
HETATM 1176 O  O   . HOH   G 5 .   ? 0.542  -3.117  9.647  1.00 36.91 ? 364 HOH   A O   1 
HETATM 1177 O  O   . HOH   G 5 .   ? 17.943 11.051  25.848 1.00 39.46 ? 365 HOH   A O   1 
HETATM 1178 O  O   . HOH   G 5 .   ? 30.645 15.449  23.222 1.00 61.26 ? 366 HOH   A O   1 
HETATM 1179 O  O   . HOH   G 5 .   ? 29.559 8.747   21.080 1.00 45.60 ? 367 HOH   A O   1 
HETATM 1180 O  O   . HOH   G 5 .   ? 32.659 8.090   15.350 1.00 37.83 ? 368 HOH   A O   1 
HETATM 1181 O  O   . HOH   G 5 .   ? -1.724 -4.640  15.474 0.50 41.82 ? 369 HOH   A O   1 
HETATM 1182 O  O   . HOH   G 5 .   ? 9.030  22.591  26.407 1.00 51.84 ? 370 HOH   A O   1 
HETATM 1183 O  O   . HOH   G 5 .   ? 0.955  -1.721  23.584 1.00 50.32 ? 371 HOH   A O   1 
HETATM 1184 O  O   . HOH   G 5 .   ? 2.147  2.550   26.866 1.00 38.45 ? 372 HOH   A O   1 
HETATM 1185 O  O   . HOH   G 5 .   ? 32.931 3.618   14.496 1.00 32.73 ? 373 HOH   A O   1 
HETATM 1186 O  O   . HOH   G 5 .   ? 20.021 -4.096  21.996 1.00 42.38 ? 374 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   ? 0.6505 0.3392 0.2438 0.0000  -0.1253 -0.0582 7   SER   A N   
2    C CA  . SER   A 1   ? 0.6640 0.3325 0.2695 0.0000  -0.1319 -0.0448 7   SER   A CA  
3    C C   . SER   A 1   ? 0.6610 0.3103 0.2618 -0.0012 -0.1220 -0.0212 7   SER   A C   
4    O O   . SER   A 1   ? 0.6666 0.3189 0.2556 -0.0015 -0.1109 -0.0139 7   SER   A O   
5    C CB  . SER   A 1   ? 0.7011 0.3865 0.3023 -0.0015 -0.1401 -0.0421 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.7476 0.4535 0.3292 -0.0035 -0.1345 -0.0244 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.6405 0.2713 0.2532 -0.0033 -0.1246 -0.0121 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.6319 0.2474 0.2435 -0.0077 -0.1125 0.0039  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.6184 0.2162 0.2409 -0.0143 -0.1147 0.0057  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.6070 0.2026 0.2397 -0.0156 -0.1252 -0.0017 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.6092 0.1969 0.2341 -0.0202 -0.1038 0.0163  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.6081 0.1849 0.2388 -0.0308 -0.1034 0.0187  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.6128 0.1834 0.2385 -0.0426 -0.0831 0.0217  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.6140 0.1845 0.2418 -0.0398 -0.0689 0.0240  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.6047 0.1783 0.2503 -0.0293 -0.1112 0.0226  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.6051 0.1737 0.2278 -0.0577 -0.0813 0.0217  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.6015 0.1684 0.2194 -0.0742 -0.0608 0.0188  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.6044 0.1682 0.2341 -0.0814 -0.0571 0.0209  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.6016 0.1680 0.2344 -0.0830 -0.0734 0.0267  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.6044 0.1804 0.2054 -0.0918 -0.0612 0.0171  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.5983 0.1779 0.1926 -0.0836 -0.0697 0.0168  10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.6167 0.1954 0.2108 -0.1120 -0.0365 0.0078  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.5921 0.1836 0.1777 -0.1000 -0.0791 0.0218  10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.6123 0.1706 0.2553 -0.0857 -0.0350 0.0165  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.6261 0.1815 0.2848 -0.0927 -0.0277 0.0166  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.6484 0.2089 0.3027 -0.1167 -0.0028 0.0030  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.6485 0.2056 0.3139 -0.1200 0.0198  -0.0074 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.6191 0.1660 0.3084 -0.0776 -0.0220 0.0226  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.6222 0.1708 0.3117 -0.0587 -0.0470 0.0336  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.6344 0.1831 0.3286 -0.0553 -0.0644 0.0383  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.6364 0.1898 0.3221 -0.0463 -0.0520 0.0377  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.6371 0.1904 0.3324 -0.0410 -0.0856 0.0430  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.6473 0.2085 0.3295 -0.0333 -0.0732 0.0430  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.6508 0.2118 0.3382 -0.0311 -0.0895 0.0438  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.6772 0.2483 0.3634 -0.0211 -0.1083 0.0443  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.6498 0.2221 0.2888 -0.1358 -0.0067 0.0028  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.6671 0.2528 0.2952 -0.1648 0.0164  -0.0124 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.6814 0.2766 0.3115 -0.1795 0.0169  -0.0099 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.6812 0.2834 0.3031 -0.1784 -0.0086 0.0076  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.6923 0.2952 0.2885 -0.1818 0.0109  -0.0138 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.6985 0.3090 0.2829 -0.1760 -0.0231 0.0079  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.7112 0.3370 0.2897 -0.2180 0.0322  -0.0298 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.6743 0.2695 0.3219 -0.1927 0.0464  -0.0271 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.6752 0.2799 0.3281 -0.2072 0.0515  -0.0270 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.6807 0.2713 0.3536 -0.1834 0.0282  -0.0066 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.6873 0.2582 0.3858 -0.1581 0.0247  -0.0021 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.6740 0.2775 0.3363 -0.1916 0.0092  0.0084  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.6741 0.2650 0.3575 -0.1695 -0.0149 0.0263  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.6658 0.2566 0.3399 -0.1555 -0.0482 0.0428  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.6689 0.2593 0.3560 -0.1478 -0.0704 0.0576  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.6991 0.3011 0.3906 -0.1841 -0.0138 0.0327  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.7800 0.3782 0.4935 -0.1929 0.0196  0.0148  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.8083 0.3861 0.5558 -0.1731 0.0269  0.0122  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.7929 0.4143 0.4913 -0.2246 0.0412  0.0022  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.6529 0.2433 0.3108 -0.1517 -0.0503 0.0387  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.6449 0.2361 0.2994 -0.1398 -0.0776 0.0505  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.6341 0.2102 0.2924 -0.1160 -0.0799 0.0438  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.6285 0.1988 0.2835 -0.1145 -0.0598 0.0328  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.6493 0.2615 0.2803 -0.1615 -0.0810 0.0554  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.6601 0.2972 0.2830 -0.1900 -0.0824 0.0669  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.6679 0.3091 0.3113 -0.1885 -0.1014 0.0854  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.6805 0.3414 0.2757 -0.2208 -0.0656 0.0602  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.6746 0.3439 0.3113 -0.2166 -0.1042 0.1008  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.6884 0.3801 0.2719 -0.2513 -0.0672 0.0723  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.6910 0.3876 0.2953 -0.2490 -0.0873 0.0949  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.7044 0.4362 0.2981 -0.2810 -0.0900 0.1113  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.6161 0.1893 0.2842 -0.0997 -0.1037 0.0503  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.6123 0.1786 0.2807 -0.0802 -0.1092 0.0442  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.6054 0.1794 0.2723 -0.0810 -0.1258 0.0476  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.5947 0.1736 0.2796 -0.0830 -0.1436 0.0569  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.6095 0.1691 0.2974 -0.0621 -0.1210 0.0441  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.6444 0.2057 0.3310 -0.0460 -0.1311 0.0370  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.6661 0.2274 0.3654 -0.0332 -0.1383 0.0357  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.6855 0.2532 0.3936 -0.0240 -0.1568 0.0266  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.6975 0.2749 0.3964 -0.0160 -0.1590 0.0169  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.6818 0.2632 0.3631 -0.0146 -0.1462 0.0203  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.6622 0.2476 0.3728 -0.0106 -0.1729 0.0029  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.6062 0.1818 0.2581 -0.0798 -0.1195 0.0417  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.5987 0.1820 0.2541 -0.0811 -0.1330 0.0454  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.5939 0.1727 0.2553 -0.0612 -0.1380 0.0343  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.5980 0.1739 0.2437 -0.0547 -0.1247 0.0266  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.5996 0.1920 0.2324 -0.0985 -0.1217 0.0467  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.6108 0.2140 0.2547 -0.1026 -0.1386 0.0566  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.5898 0.1912 0.2089 -0.1221 -0.1093 0.0504  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.5778 0.1589 0.2658 -0.0534 -0.1559 0.0331  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.5731 0.1550 0.2684 -0.0376 -0.1594 0.0173  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.5562 0.1435 0.2790 -0.0372 -0.1706 0.0159  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.5480 0.1387 0.2926 -0.0474 -0.1809 0.0315  18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.5712 0.1520 0.2820 -0.0270 -0.1674 0.0080  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.5880 0.1662 0.2775 -0.0248 -0.1566 0.0099  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.5518 0.1305 0.2964 -0.0310 -0.1822 0.0163  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.5473 0.1384 0.2752 -0.0262 -0.1691 -0.0019 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.5339 0.1294 0.3027 -0.0236 -0.1786 -0.0080 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.5315 0.1253 0.3448 -0.0210 -0.1929 -0.0101 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.5333 0.1264 0.3415 -0.0148 -0.1927 -0.0231 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.5346 0.1373 0.2999 -0.0130 -0.1708 -0.0334 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.5793 0.1847 0.3081 -0.0142 -0.1572 -0.0314 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.6304 0.2373 0.3219 -0.0125 -0.1463 -0.0318 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.5689 0.1761 0.3139 -0.0176 -0.1580 -0.0268 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.5250 0.1203 0.3849 -0.0270 -0.2060 0.0053  20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.5302 0.1240 0.4433 -0.0250 -0.2200 0.0061  20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.5405 0.1351 0.4810 -0.0124 -0.2182 -0.0291 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.5576 0.1501 0.5144 -0.0095 -0.2238 -0.0372 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.5180 0.1176 0.4885 -0.0340 -0.2350 0.0323  20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.5130 0.1125 0.5432 -0.0356 -0.2512 0.0451  20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.5170 0.1265 0.6162 -0.0438 -0.2668 0.0732  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.5384 0.1505 0.7078 -0.0464 -0.2838 0.0916  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.5490 0.1558 0.7929 -0.0353 -0.2880 0.0717  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.5550 0.1558 0.8057 -0.0223 -0.2753 0.0291  20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.5143 0.1241 0.8286 -0.0388 -0.3041 0.0931  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.5425 0.1430 0.4876 -0.0068 -0.2095 -0.0521 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.5504 0.1581 0.5182 0.0009  -0.2047 -0.0908 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.5755 0.1900 0.4884 0.0030  -0.1980 -0.1070 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5681 0.1919 0.4977 0.0052  -0.1980 -0.1358 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.5497 0.1653 0.5396 0.0038  -0.1951 -0.1119 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.5690 0.1912 0.4968 0.0041  -0.1812 -0.1145 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.5915 0.2083 0.4945 -0.0002 -0.1801 -0.0866 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5892 0.2261 0.4818 0.0065  -0.1683 -0.1417 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.6130 0.2376 0.4698 0.0018  -0.1664 -0.0973 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.6141 0.2521 0.4615 0.0056  -0.1594 -0.1278 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.5998 0.2108 0.4553 0.0006  -0.1938 -0.0863 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.6173 0.2359 0.4286 0.0017  -0.1894 -0.0921 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.6187 0.2276 0.4266 -0.0003 -0.1971 -0.0732 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.6272 0.2425 0.4073 0.0003  -0.1954 -0.0741 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.6399 0.2644 0.3991 0.0014  -0.1763 -0.0850 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.6555 0.2941 0.4126 0.0032  -0.1672 -0.1060 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.6807 0.3260 0.3892 0.0026  -0.1551 -0.0950 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.6479 0.3070 0.4195 0.0036  -0.1671 -0.1412 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.6044 0.2010 0.4443 -0.0040 -0.2061 -0.0545 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.6062 0.1950 0.4468 -0.0070 -0.2124 -0.0375 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.5852 0.1794 0.4417 -0.0026 -0.2193 -0.0560 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.5766 0.1786 0.4664 0.0004  -0.2232 -0.0817 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.6000 0.1821 0.4782 -0.0138 -0.2226 -0.0152 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.5806 0.1729 0.4140 -0.0034 -0.2191 -0.0452 24  THR   A N   
135  C CA  . THR   A 18  ? 0.5879 0.1875 0.4303 -0.0013 -0.2265 -0.0580 24  THR   A CA  
136  C C   . THR   A 18  ? 0.5888 0.1777 0.4747 -0.0026 -0.2387 -0.0482 24  THR   A C   
137  O O   . THR   A 18  ? 0.5942 0.1728 0.4973 -0.0066 -0.2407 -0.0276 24  THR   A O   
138  C CB  . THR   A 18  ? 0.6067 0.2124 0.4061 -0.0016 -0.2201 -0.0470 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.6273 0.2179 0.4250 -0.0044 -0.2175 -0.0212 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.6091 0.2245 0.3697 -0.0013 -0.2078 -0.0473 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5853 0.1798 0.4878 -0.0013 -0.2471 -0.0606 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5926 0.1780 0.5374 -0.0022 -0.2585 -0.0510 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.5997 0.1735 0.5263 -0.0063 -0.2549 -0.0179 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.5818 0.1481 0.5382 -0.0105 -0.2605 -0.0001 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.6241 0.2201 0.5808 -0.0012 -0.2667 -0.0709 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.6884 0.2948 0.6867 -0.0007 -0.2715 -0.1066 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7100 0.3147 0.7639 -0.0010 -0.2826 -0.1186 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.7130 0.3311 0.7108 -0.0007 -0.2645 -0.1339 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.7065 0.3226 0.7933 -0.0016 -0.2810 -0.1558 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.7120 0.3368 0.7662 -0.0017 -0.2697 -0.1665 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.6094 0.1847 0.4922 -0.0066 -0.2448 -0.0096 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.6287 0.1943 0.4978 -0.0118 -0.2365 0.0157  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.6248 0.1856 0.4856 -0.0194 -0.2289 0.0296  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.6267 0.1836 0.4967 -0.0278 -0.2282 0.0478  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.6749 0.2435 0.5122 -0.0104 -0.2255 0.0210  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.7611 0.3199 0.5885 -0.0169 -0.2106 0.0413  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.7851 0.3388 0.6298 -0.0194 -0.2114 0.0517  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.7712 0.3280 0.5733 -0.0212 -0.1952 0.0447  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.6198 0.1842 0.4627 -0.0187 -0.2233 0.0219  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.6221 0.1860 0.4590 -0.0278 -0.2187 0.0350  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.6263 0.1917 0.5092 -0.0332 -0.2341 0.0473  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.6266 0.1957 0.5081 -0.0462 -0.2334 0.0690  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.6160 0.1844 0.4391 -0.0240 -0.2145 0.0222  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.6134 0.1829 0.3933 -0.0219 -0.1986 0.0176  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.6021 0.1673 0.3625 -0.0272 -0.1870 0.0287  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.6128 0.1885 0.3831 -0.0159 -0.1966 0.0029  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.6258 0.1919 0.5528 -0.0253 -0.2475 0.0336  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.6248 0.1929 0.6099 -0.0296 -0.2628 0.0479  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.6355 0.2021 0.6343 -0.0360 -0.2684 0.0681  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.6391 0.2123 0.6603 -0.0476 -0.2756 0.0953  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.6134 0.1823 0.6526 -0.0199 -0.2723 0.0233  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.6063 0.1794 0.6591 -0.0190 -0.2704 0.0165  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.6191 0.1950 0.6508 -0.0120 -0.2608 -0.0119 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.5799 0.1578 0.6753 -0.0264 -0.2791 0.0409  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.6127 0.1919 0.6708 -0.0134 -0.2613 -0.0090 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.5851 0.1656 0.6833 -0.0222 -0.2732 0.0247  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.5642 0.1483 0.6915 -0.0384 -0.2913 0.0789  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.5573 0.1443 0.6950 -0.0283 -0.2800 0.0451  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.5445 0.1384 0.7128 -0.0457 -0.3000 0.1010  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.5422 0.1365 0.7149 -0.0403 -0.2943 0.0846  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.6473 0.2086 0.6306 -0.0303 -0.2648 0.0577  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.6459 0.2048 0.6409 -0.0350 -0.2679 0.0737  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.6486 0.2106 0.6067 -0.0492 -0.2544 0.0959  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.6549 0.2191 0.6264 -0.0572 -0.2561 0.1130  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.6475 0.2020 0.6363 -0.0253 -0.2674 0.0559  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.6389 0.2026 0.5528 -0.0534 -0.2395 0.0930  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.6417 0.2111 0.5212 -0.0696 -0.2232 0.1067  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.6361 0.2167 0.5006 -0.0813 -0.2221 0.1150  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.6484 0.2326 0.4737 -0.0909 -0.2048 0.1127  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.6725 0.2337 0.5180 -0.0652 -0.2033 0.0936  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.7061 0.2598 0.5681 -0.0570 -0.2044 0.0912  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.7198 0.2748 0.5933 -0.0655 -0.2013 0.1029  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.7077 0.2568 0.5716 -0.0421 -0.2094 0.0768  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.6133 0.2005 0.5157 -0.0811 -0.2406 0.1248  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.6121 0.2119 0.5114 -0.0915 -0.2440 0.1365  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.6216 0.2417 0.4944 -0.1178 -0.2377 0.1599  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.6252 0.2556 0.5107 -0.1299 -0.2419 0.1783  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.5876 0.1917 0.5522 -0.0868 -0.2667 0.1473  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.5837 0.2037 0.5643 -0.0980 -0.2755 0.1669  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.5922 0.2060 0.5395 -0.0904 -0.2639 0.1451  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.5637 0.1877 0.6279 -0.0933 -0.2978 0.1813  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.6199 0.2492 0.4569 -0.1288 -0.2278 0.1589  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.6282 0.2841 0.4378 -0.1585 -0.2224 0.1786  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.6220 0.2979 0.4547 -0.1689 -0.2413 0.2027  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.6113 0.3160 0.4593 -0.1918 -0.2548 0.2358  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.6510 0.3046 0.4045 -0.1663 -0.1943 0.1568  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.6561 0.3421 0.3783 -0.2004 -0.1877 0.1711  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.6684 0.3053 0.4118 -0.1584 -0.1760 0.1389  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.6264 0.2899 0.4636 -0.1533 -0.2424 0.1880  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.6215 0.3013 0.4856 -0.1607 -0.2585 0.2085  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.6128 0.2720 0.4979 -0.1358 -0.2593 0.1858  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.6289 0.2694 0.4804 -0.1214 -0.2426 0.1557  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.6383 0.3440 0.4529 -0.1889 -0.2495 0.2190  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.6473 0.3697 0.4810 -0.1968 -0.2635 0.2375  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.6414 0.3933 0.5186 -0.2144 -0.2877 0.2788  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.6646 0.3778 0.4776 -0.1887 -0.2542 0.2186  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.6427 0.4037 0.5291 -0.2175 -0.2943 0.2865  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.6583 0.3950 0.5038 -0.2017 -0.2734 0.2484  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.6931 0.3828 0.4668 -0.1729 -0.2321 0.1826  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.6678 0.4029 0.5058 -0.1982 -0.2702 0.2401  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.7053 0.3941 0.4707 -0.1696 -0.2290 0.1751  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.6894 0.3996 0.4856 -0.1817 -0.2474 0.2021  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.5874 0.2532 0.5315 -0.1327 -0.2780 0.2015  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.5855 0.2361 0.5540 -0.1123 -0.2769 0.1785  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.5810 0.2492 0.5975 -0.1211 -0.2928 0.2046  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.5543 0.2443 0.6142 -0.1374 -0.3118 0.2433  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.5943 0.2241 0.6040 -0.0884 -0.2785 0.1521  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.5857 0.2196 0.6633 -0.0895 -0.2967 0.1716  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.5814 0.2249 0.7469 -0.0898 -0.3151 0.1915  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.5613 0.2172 0.7834 -0.0990 -0.3326 0.2239  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.5739 0.2139 0.7562 -0.0817 -0.3117 0.1768  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.5942 0.2557 0.6046 -0.1118 -0.2853 0.1864  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.5894 0.2656 0.6501 -0.1180 -0.2989 0.2087  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.5827 0.2411 0.6796 -0.0947 -0.2921 0.1761  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.6035 0.2535 0.6527 -0.0878 -0.2759 0.1512  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.6374 0.3356 0.6468 -0.1414 -0.2969 0.2289  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.6818 0.4061 0.7478 -0.1568 -0.3182 0.2690  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.6841 0.4015 0.8277 -0.1422 -0.3273 0.2690  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.7063 0.4608 0.7418 -0.1852 -0.3252 0.3000  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.5439 0.1986 0.7302 -0.0840 -0.3035 0.1756  36  SER   A N   
241  C CA  A SER   A 30  ? 0.5360 0.1777 0.7656 -0.0646 -0.2950 0.1404  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.5337 0.1753 0.7626 -0.0646 -0.2949 0.1402  36  SER   A CA  
243  C C   . SER   A 30  ? 0.5347 0.1844 0.7647 -0.0682 -0.2924 0.1464  36  SER   A C   
244  O O   . SER   A 30  ? 0.5451 0.1848 0.7542 -0.0556 -0.2759 0.1115  36  SER   A O   
245  C CB  A SER   A 30  ? 0.5148 0.1547 0.8540 -0.0569 -0.3073 0.1412  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.5061 0.1447 0.8424 -0.0558 -0.3060 0.1378  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.5218 0.1523 0.9068 -0.0410 -0.2958 0.1024  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4895 0.1435 0.8835 -0.0699 -0.3284 0.1857  36  SER   A OG  
249  N N   . SER   A 31  ? 0.5205 0.1918 0.7707 -0.0877 -0.3092 0.1926  37  SER   A N   
250  C CA  . SER   A 31  ? 0.5229 0.2067 0.7783 -0.0955 -0.3112 0.2077  37  SER   A CA  
251  C C   . SER   A 31  ? 0.5562 0.2347 0.7112 -0.0965 -0.2916 0.1857  37  SER   A C   
252  O O   . SER   A 31  ? 0.5698 0.2481 0.7258 -0.0926 -0.2848 0.1765  37  SER   A O   
253  C CB  . SER   A 31  ? 0.5249 0.2401 0.8173 -0.1212 -0.3365 0.2674  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.5926 0.3275 0.8463 -0.1392 -0.3390 0.2886  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.5663 0.2399 0.6425 -0.1009 -0.2814 0.1764  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.5732 0.2411 0.5643 -0.1020 -0.2617 0.1562  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.5603 0.2051 0.5178 -0.0799 -0.2417 0.1124  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.5796 0.2192 0.4807 -0.0777 -0.2252 0.0957  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.6000 0.2818 0.5309 -0.1250 -0.2611 0.1755  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.6192 0.3328 0.5636 -0.1530 -0.2789 0.2184  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.6587 0.3894 0.5412 -0.1783 -0.2747 0.2300  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.6703 0.3942 0.4806 -0.1813 -0.2513 0.2036  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.6852 0.4288 0.4412 -0.2080 -0.2430 0.2084  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.6618 0.4371 0.4189 -0.2363 -0.2569 0.2400  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.6966 0.4314 0.4000 -0.2086 -0.2201 0.1816  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.5252 0.1592 0.5196 -0.0657 -0.2440 0.0955  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.5238 0.1429 0.4875 -0.0488 -0.2285 0.0576  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.5370 0.1520 0.4300 -0.0543 -0.2191 0.0588  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.5460 0.1538 0.3957 -0.0454 -0.2040 0.0365  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.5371 0.1533 0.4887 -0.0366 -0.2133 0.0280  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.5697 0.1797 0.4922 -0.0228 -0.1998 -0.0077 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.5312 0.1383 0.4815 -0.0172 -0.2048 -0.0203 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.6015 0.2122 0.4748 -0.0192 -0.1851 -0.0209 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.5373 0.1588 0.4260 -0.0693 -0.2280 0.0849  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.5514 0.1696 0.3833 -0.0762 -0.2170 0.0846  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.5601 0.1760 0.4128 -0.0767 -0.2261 0.0922  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.5542 0.1783 0.4583 -0.0821 -0.2435 0.1124  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.5446 0.1777 0.3416 -0.0995 -0.2142 0.1060  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.5490 0.1827 0.3079 -0.1017 -0.1996 0.0959  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.5620 0.2148 0.2885 -0.1293 -0.1970 0.1143  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.5647 0.1822 0.2854 -0.0873 -0.1793 0.0690  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.5621 0.1681 0.3787 -0.0717 -0.2142 0.0785  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.5630 0.1667 0.3899 -0.0738 -0.2196 0.0857  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.5831 0.1842 0.3575 -0.0817 -0.2020 0.0835  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.6056 0.1993 0.3474 -0.0749 -0.1863 0.0670  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.5566 0.1497 0.4166 -0.0553 -0.2255 0.0659  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.5645 0.1544 0.4412 -0.0561 -0.2325 0.0730  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.5530 0.1390 0.4866 -0.0438 -0.2452 0.0600  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.5846 0.1660 0.4171 -0.0518 -0.2179 0.0609  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.5837 0.1924 0.3560 -0.0970 -0.2037 0.1005  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.6062 0.2130 0.3409 -0.1058 -0.1851 0.0961  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.6142 0.2150 0.3680 -0.1014 -0.1897 0.0988  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.6055 0.2144 0.3922 -0.1067 -0.2065 0.1164  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.6100 0.2376 0.3185 -0.1344 -0.1781 0.1106  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.6297 0.2566 0.3089 -0.1455 -0.1554 0.1012  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.6110 0.2446 0.3014 -0.1389 -0.1738 0.1071  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.6230 0.2104 0.3628 -0.0910 -0.1762 0.0836  43  SER   A N   
298  C CA  . SER   A 37  ? 0.6282 0.2100 0.3856 -0.0872 -0.1793 0.0861  43  SER   A CA  
299  C C   . SER   A 37  ? 0.6440 0.2253 0.3779 -0.0987 -0.1566 0.0840  43  SER   A C   
300  O O   . SER   A 37  ? 0.6444 0.2266 0.3518 -0.1056 -0.1379 0.0756  43  SER   A O   
301  C CB  . SER   A 37  ? 0.6465 0.2163 0.4203 -0.0649 -0.1865 0.0712  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.6874 0.2510 0.4369 -0.0562 -0.1718 0.0578  43  SER   A OG  
303  N N   . SER   A 38  ? 0.6396 0.2193 0.3889 -0.1011 -0.1567 0.0898  44  SER   A N   
304  C CA  . SER   A 38  ? 0.6538 0.2330 0.3909 -0.1119 -0.1330 0.0852  44  SER   A CA  
305  C C   . SER   A 38  ? 0.6700 0.2326 0.4160 -0.0938 -0.1239 0.0740  44  SER   A C   
306  O O   . SER   A 38  ? 0.6703 0.2258 0.4313 -0.0757 -0.1396 0.0727  44  SER   A O   
307  C CB  . SER   A 38  ? 0.6650 0.2547 0.4154 -0.1268 -0.1355 0.0988  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.6879 0.2688 0.4709 -0.1113 -0.1546 0.1052  44  SER   A OG  
309  N N   . THR   A 39  ? 0.6783 0.2378 0.4196 -0.1005 -0.0983 0.0662  45  THR   A N   
310  C CA  . THR   A 39  ? 0.6981 0.2454 0.4567 -0.0854 -0.0894 0.0617  45  THR   A CA  
311  C C   . THR   A 39  ? 0.7163 0.2611 0.4954 -0.0947 -0.0685 0.0606  45  THR   A C   
312  O O   . THR   A 39  ? 0.7159 0.2702 0.4865 -0.1155 -0.0536 0.0567  45  THR   A O   
313  C CB  . THR   A 39  ? 0.7166 0.2610 0.4628 -0.0813 -0.0749 0.0529  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.7385 0.2872 0.4749 -0.1004 -0.0489 0.0431  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.7198 0.2676 0.4459 -0.0735 -0.0911 0.0518  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.7311 0.2666 0.5387 -0.0813 -0.0658 0.0637  46  THR   A N   
317  C CA  . THR   A 40  ? 0.7461 0.2778 0.5844 -0.0880 -0.0439 0.0623  46  THR   A CA  
318  C C   . THR   A 40  ? 0.7561 0.2845 0.6063 -0.0937 -0.0126 0.0504  46  THR   A C   
319  O O   . THR   A 40  ? 0.7547 0.2853 0.6174 -0.1106 0.0152  0.0381  46  THR   A O   
320  C CB  . THR   A 40  ? 0.7608 0.2863 0.6328 -0.0721 -0.0586 0.0752  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.7783 0.3034 0.6503 -0.0553 -0.0732 0.0812  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.7676 0.2961 0.6393 -0.0716 -0.0817 0.0828  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.7571 0.2821 0.6063 -0.0809 -0.0160 0.0530  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.7535 0.2752 0.6212 -0.0844 0.0114  0.0441  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.7651 0.2934 0.5962 -0.1012 0.0241  0.0268  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.7820 0.3165 0.5741 -0.1011 0.0037  0.0293  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.7512 0.2717 0.6313 -0.0657 -0.0004 0.0585  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.7566 0.2848 0.6046 -0.1161 0.0578  0.0086  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.7624 0.3007 0.5757 -0.1353 0.0708  -0.0096 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.7550 0.2894 0.5614 -0.1244 0.0682  -0.0082 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.7561 0.2814 0.6003 -0.1100 0.0746  -0.0010 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.7900 0.3347 0.6213 -0.1610 0.1096  -0.0359 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.8605 0.4203 0.6574 -0.1855 0.1262  -0.0582 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.9282 0.5120 0.6939 -0.2173 0.1350  -0.0713 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.9430 0.5335 0.6967 -0.2184 0.1168  -0.0561 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.9437 0.5444 0.6959 -0.2458 0.1630  -0.0994 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.7458 0.2895 0.5071 -0.1317 0.0568  -0.0113 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.7374 0.2797 0.4860 -0.1232 0.0527  -0.0103 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.7190 0.2657 0.4682 -0.1421 0.0822  -0.0326 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.7120 0.2703 0.4499 -0.1675 0.0996  -0.0508 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.7062 0.2469 0.4690 -0.1318 0.0884  -0.0320 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.7052 0.2484 0.4795 -0.1485 0.1187  -0.0550 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.6948 0.2438 0.4368 -0.1501 0.1116  -0.0569 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.6899 0.2389 0.4497 -0.1604 0.1367  -0.0747 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.7225 0.2532 0.5644 -0.1394 0.1432  -0.0560 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.8039 0.3286 0.6972 -0.1427 0.1609  -0.0597 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.6824 0.2357 0.3853 -0.1400 0.0801  -0.0404 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.6923 0.2516 0.3681 -0.1419 0.0738  -0.0420 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.6899 0.2666 0.3359 -0.1735 0.0846  -0.0609 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.6903 0.2785 0.3217 -0.1905 0.0829  -0.0638 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.7253 0.2860 0.3748 -0.1245 0.0397  -0.0223 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.8018 0.3544 0.4698 -0.0979 0.0293  -0.0067 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.8340 0.3830 0.5243 -0.0924 0.0440  -0.0066 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.8060 0.3590 0.4672 -0.0845 0.0060  0.0057  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.6794 0.2615 0.3165 -0.1829 0.0946  -0.0721 52  THR   A N   
356  C CA  . THR   A 46  ? 0.6902 0.2947 0.2963 -0.2156 0.1028  -0.0891 52  THR   A CA  
357  C C   . THR   A 46  ? 0.6952 0.3110 0.2649 -0.2146 0.0728  -0.0713 52  THR   A C   
358  O O   . THR   A 46  ? 0.7003 0.3059 0.2742 -0.1949 0.0638  -0.0625 52  THR   A O   
359  C CB  . THR   A 46  ? 0.7082 0.3131 0.3342 -0.2296 0.1355  -0.1162 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.7160 0.3126 0.3856 -0.2344 0.1667  -0.1357 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.7167 0.3496 0.3059 -0.2654 0.1416  -0.1340 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.6871 0.3253 0.2267 -0.2353 0.0569  -0.0635 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.6903 0.3413 0.2071 -0.2362 0.0287  -0.0441 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.6930 0.3651 0.1896 -0.2640 0.0401  -0.0580 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.6889 0.3814 0.1733 -0.2957 0.0602  -0.0775 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.6958 0.3647 0.1998 -0.2464 0.0032  -0.0222 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.6888 0.3389 0.2138 -0.2232 -0.0057 -0.0123 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.7016 0.3837 0.1966 -0.2465 -0.0264 0.0010  53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.6922 0.3181 0.2358 -0.1876 -0.0183 -0.0043 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.6952 0.3654 0.1885 -0.2544 0.0282  -0.0497 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.7156 0.4066 0.1908 -0.2801 0.0358  -0.0606 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.7195 0.4488 0.1653 -0.3129 0.0159  -0.0447 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.7118 0.4454 0.1595 -0.3052 -0.0119 -0.0169 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.7159 0.3935 0.1997 -0.2580 0.0266  -0.0525 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.7320 0.4924 0.1545 -0.3522 0.0313  -0.0628 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.7424 0.5489 0.1345 -0.3902 0.0128  -0.0456 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.7583 0.5815 0.1371 -0.4090 0.0184  -0.0568 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.7606 0.5948 0.1297 -0.4333 0.0484  -0.0920 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.7546 0.5895 0.1271 -0.4252 0.0299  -0.0611 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.7723 0.5833 0.1646 -0.4023 0.0306  -0.0558 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.7743 0.5822 0.1768 -0.3831 -0.0074 -0.0134 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.7707 0.5569 0.1921 -0.3636 -0.0044 -0.0123 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.7528 0.5267 0.1935 -0.3404 -0.0314 0.0166  55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.7315 0.5100 0.1815 -0.3313 -0.0620 0.0458  55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.7278 0.4834 0.1850 -0.3250 -0.0266 0.0146  55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.7727 0.5903 0.1605 -0.3915 -0.0073 -0.0310 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.7736 0.5981 0.1573 -0.3993 -0.0045 -0.0383 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.7709 0.5978 0.1674 -0.3845 -0.0397 -0.0006 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.7718 0.5947 0.1843 -0.3686 -0.0646 0.0288  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.7800 0.5661 0.1857 -0.3734 0.0247  -0.0683 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.8236 0.5604 0.2642 -0.3162 0.0157  -0.0527 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.7703 0.6042 0.1655 -0.3906 -0.0399 -0.0034 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.7684 0.6073 0.1808 -0.3804 -0.0690 0.0283  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.7504 0.5534 0.1863 -0.3447 -0.0612 0.0195  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.7339 0.5380 0.1894 -0.3334 -0.0823 0.0426  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.8086 0.6973 0.1991 -0.4251 -0.0812 0.0398  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.9252 0.8245 0.2934 -0.4495 -0.0530 0.0027  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.9559 0.8253 0.3280 -0.4352 -0.0211 -0.0331 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.9793 0.9186 0.3305 -0.4844 -0.0631 0.0102  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.7388 0.5140 0.1766 -0.3299 -0.0304 -0.0125 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.7243 0.4678 0.1835 -0.2979 -0.0183 -0.0221 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.6941 0.4194 0.1771 -0.2628 -0.0399 0.0016  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.7072 0.4255 0.1983 -0.2491 -0.0531 0.0145  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.7284 0.4467 0.1964 -0.2857 0.0136  -0.0505 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.7554 0.4725 0.2166 -0.2927 0.0226  -0.0590 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.6527 0.3745 0.1487 -0.2521 -0.0438 0.0067  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.6301 0.3385 0.1519 -0.2222 -0.0596 0.0231  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.6002 0.2831 0.1333 -0.1929 -0.0418 0.0098  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.5942 0.2722 0.1453 -0.1747 -0.0487 0.0173  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.6469 0.3764 0.1817 -0.2340 -0.0807 0.0439  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.6940 0.4483 0.2372 -0.2518 -0.1087 0.0718  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.7412 0.5148 0.3099 -0.2598 -0.1296 0.0959  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.7645 0.5711 0.3225 -0.2931 -0.1408 0.1100  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.7261 0.4825 0.3307 -0.2311 -0.1344 0.1007  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.5941 0.2642 0.1209 -0.1903 -0.0181 -0.0088 60  THR   A N   
416  C CA  . THR   A 54  ? 0.6056 0.2557 0.1465 -0.1641 -0.0023 -0.0157 60  THR   A CA  
417  C C   . THR   A 54  ? 0.5985 0.2359 0.1403 -0.1563 0.0091  -0.0229 60  THR   A C   
418  O O   . THR   A 54  ? 0.6007 0.2430 0.1328 -0.1756 0.0154  -0.0316 60  THR   A O   
419  C CB  . THR   A 54  ? 0.6401 0.2894 0.1876 -0.1708 0.0185  -0.0282 60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.6532 0.3092 0.1931 -0.1975 0.0354  -0.0465 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.6424 0.3030 0.1928 -0.1757 0.0086  -0.0205 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.5811 0.2054 0.1350 -0.1301 0.0117  -0.0187 61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.5769 0.1904 0.1375 -0.1206 0.0210  -0.0213 61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.5640 0.1713 0.1367 -0.0944 0.0215  -0.0127 61  GLY   A C   
425  O O   . GLY   A 55  ? 0.5484 0.1594 0.1249 -0.0848 0.0208  -0.0082 61  GLY   A O   
426  N N   . VAL   A 56  ? 0.5594 0.1608 0.1375 -0.0845 0.0221  -0.0095 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.5361 0.1384 0.1237 -0.0640 0.0219  0.0009  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.5193 0.1222 0.0991 -0.0553 0.0059  0.0041  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.5258 0.1226 0.1052 -0.0627 0.0051  0.0011  62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.5416 0.1383 0.1558 -0.0636 0.0424  0.0039  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.5622 0.1660 0.1879 -0.0461 0.0397  0.0210  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.5326 0.1282 0.1628 -0.0727 0.0605  -0.0019 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.5050 0.1168 0.0803 -0.0413 -0.0049 0.0082  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.4800 0.0947 0.0721 -0.0340 -0.0187 0.0047  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.5127 0.1388 0.0856 -0.0219 -0.0187 0.0160  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.4960 0.1339 0.0696 -0.0172 -0.0123 0.0218  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.4858 0.1034 0.0729 -0.0330 -0.0342 0.0014  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.5057 0.1368 0.0745 -0.0226 -0.0382 -0.0040 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.5064 0.1420 0.0763 -0.0233 -0.0306 -0.0036 63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.5083 0.1499 0.0776 -0.0136 -0.0466 -0.0112 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.5164 0.1661 0.0884 -0.0152 -0.0308 -0.0100 63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.5075 0.1652 0.0779 -0.0072 -0.0458 -0.0208 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.5233 0.1855 0.0945 -0.0076 -0.0370 -0.0194 63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.5357 0.2156 0.1098 -0.0025 -0.0342 -0.0309 63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.5242 0.1506 0.0979 -0.0187 -0.0263 0.0183  64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.5480 0.1918 0.1218 -0.0108 -0.0288 0.0282  64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.5540 0.2142 0.1141 -0.0057 -0.0416 0.0158  64  TYR   A C   
448  O O   . TYR   A 58  ? 0.5353 0.1881 0.0958 -0.0061 -0.0522 0.0026  64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.5547 0.1937 0.1406 -0.0110 -0.0301 0.0378  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.5687 0.2321 0.1546 -0.0055 -0.0363 0.0519  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.5736 0.2554 0.1678 -0.0042 -0.0287 0.0709  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.5819 0.2539 0.1603 -0.0037 -0.0506 0.0477  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.5821 0.2944 0.1747 -0.0031 -0.0365 0.0884  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.5887 0.2897 0.1637 -0.0026 -0.0577 0.0609  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5995 0.3228 0.1799 -0.0032 -0.0513 0.0826  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.6280 0.3880 0.2029 -0.0059 -0.0603 0.0999  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.5638 0.2490 0.1158 -0.0024 -0.0393 0.0196  65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.5769 0.2846 0.1169 -0.0003 -0.0462 0.0035  65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.5747 0.3115 0.1049 -0.0013 -0.0510 0.0135  65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5586 0.3190 0.0840 -0.0031 -0.0453 0.0314  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.5926 0.3114 0.1286 0.0002  -0.0374 -0.0015 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.6095 0.3573 0.1372 0.0005  -0.0401 -0.0293 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.5871 0.3250 0.1167 -0.0018 -0.0625 0.0052  66  SER   A N   
464  C CA  . SER   A 60  ? 0.6081 0.3769 0.1282 -0.0055 -0.0694 0.0161  66  SER   A CA  
465  C C   . SER   A 60  ? 0.6051 0.4167 0.1041 -0.0111 -0.0682 0.0070  66  SER   A C   
466  O O   . SER   A 60  ? 0.6234 0.4689 0.1127 -0.0173 -0.0703 0.0288  66  SER   A O   
467  C CB  . SER   A 60  ? 0.6594 0.4215 0.1840 -0.0057 -0.0820 0.0067  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.7249 0.4870 0.2490 -0.0055 -0.0871 -0.0258 66  SER   A OG  
469  N N   . SER   A 61  ? 0.6088 0.4218 0.1044 -0.0106 -0.0640 -0.0227 67  SER   A N   
470  C CA  . SER   A 61  ? 0.6319 0.4872 0.1087 -0.0179 -0.0591 -0.0394 67  SER   A CA  
471  C C   . SER   A 61  ? 0.6494 0.5268 0.1155 -0.0207 -0.0487 -0.0161 67  SER   A C   
472  O O   . SER   A 61  ? 0.6516 0.5686 0.0997 -0.0288 -0.0430 -0.0268 67  SER   A O   
473  C CB  . SER   A 61  ? 0.6417 0.4887 0.1308 -0.0160 -0.0551 -0.0793 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.6846 0.5044 0.1894 -0.0091 -0.0472 -0.0777 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.6533 0.5061 0.1340 -0.0151 -0.0448 0.0136  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.6465 0.5151 0.1281 -0.0166 -0.0355 0.0407  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.6415 0.5042 0.1436 -0.0159 -0.0374 0.0810  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.6347 0.5100 0.1488 -0.0171 -0.0301 0.1088  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.6630 0.5036 0.1559 -0.0103 -0.0242 0.0307  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.6991 0.5472 0.1842 -0.0107 -0.0201 -0.0045 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.7339 0.6299 0.1998 -0.0186 -0.0121 -0.0050 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.7594 0.6616 0.2259 -0.0192 -0.0048 -0.0425 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.8039 0.7276 0.2636 -0.0252 -0.0062 -0.0758 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.7930 0.7351 0.2386 -0.0317 -0.0165 -0.0757 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.8133 0.7397 0.2861 -0.0252 0.0033  -0.1108 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.6345 0.4765 0.1485 -0.0137 -0.0458 0.0840  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.6390 0.4681 0.1836 -0.0121 -0.0454 0.1161  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.6424 0.4448 0.2141 -0.0079 -0.0300 0.1270  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.6421 0.4523 0.2445 -0.0088 -0.0246 0.1594  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.6579 0.5318 0.2067 -0.0199 -0.0541 0.1516  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.7108 0.6118 0.2352 -0.0268 -0.0701 0.1410  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.7550 0.7010 0.2891 -0.0366 -0.0808 0.1832  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.8113 0.7961 0.3145 -0.0480 -0.0962 0.1718  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 0.8271 0.8736 0.3021 -0.0639 -0.1029 0.1816  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 0.8225 0.8986 0.2970 -0.0693 -0.0961 0.2065  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 0.8314 0.9133 0.2783 -0.0766 -0.1158 0.1656  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.6347 0.4102 0.1988 -0.0047 -0.0231 0.1006  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.6258 0.3788 0.2098 -0.0033 -0.0086 0.1038  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.6169 0.3308 0.2017 -0.0032 -0.0061 0.0793  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.6127 0.3192 0.1800 -0.0027 -0.0159 0.0580  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.6466 0.4190 0.2163 -0.0036 -0.0030 0.1001  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.7027 0.5114 0.2820 -0.0063 0.0008  0.1323  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7666 0.6033 0.3224 -0.0084 0.0041  0.1241  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.8015 0.6856 0.3601 -0.0145 0.0050  0.1585  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.8132 0.7428 0.3440 -0.0233 -0.0076 0.1631  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.5966 0.2894 0.2049 -0.0055 0.0074  0.0833  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.5938 0.2577 0.2017 -0.0105 0.0116  0.0633  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.5830 0.2478 0.1860 -0.0117 0.0181  0.0568  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.5841 0.2599 0.2021 -0.0103 0.0279  0.0716  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.6094 0.2541 0.2491 -0.0162 0.0255  0.0682  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.6332 0.2748 0.2848 -0.0153 0.0211  0.0751  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.6674 0.2914 0.3110 -0.0206 0.0176  0.0592  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.6293 0.2855 0.3025 -0.0110 0.0192  0.0987  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.6594 0.2854 0.3198 -0.0179 0.0147  0.0710  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.6440 0.2894 0.3233 -0.0122 0.0148  0.0954  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.5705 0.2263 0.1573 -0.0145 0.0116  0.0380  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.5576 0.2144 0.1424 -0.0163 0.0158  0.0320  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.5466 0.1841 0.1349 -0.0280 0.0189  0.0217  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.5502 0.1788 0.1313 -0.0336 0.0097  0.0137  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.5653 0.2332 0.1355 -0.0116 0.0042  0.0196  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.5727 0.2678 0.1339 -0.0045 0.0032  0.0234  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.5756 0.2892 0.1382 -0.0028 0.0129  0.0333  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.5839 0.2902 0.1347 -0.0018 -0.0072 0.0163  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.5911 0.3376 0.1412 -0.0005 0.0123  0.0371  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5899 0.3283 0.1283 0.0001  -0.0076 0.0171  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.6066 0.3668 0.1427 -0.0003 0.0022  0.0275  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.6472 0.4464 0.1674 -0.0024 0.0022  0.0292  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.5350 0.1697 0.1340 -0.0338 0.0310  0.0223  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.5325 0.1564 0.1301 -0.0494 0.0327  0.0109  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.5332 0.1623 0.1194 -0.0505 0.0179  0.0060  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.5456 0.1845 0.1334 -0.0407 0.0164  0.0084  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.5300 0.1524 0.1474 -0.0544 0.0512  0.0126  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.5337 0.1696 0.1581 -0.0396 0.0534  0.0270  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.5148 0.1603 0.1277 -0.0282 0.0425  0.0342  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.5261 0.1516 0.1055 -0.0630 0.0073  0.0009  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.5233 0.1551 0.1044 -0.0646 -0.0085 0.0013  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.5375 0.1719 0.1159 -0.0866 -0.0145 0.0018  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.5292 0.1613 0.0980 -0.1019 -0.0097 -0.0019 74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.5267 0.1593 0.1098 -0.0555 -0.0242 0.0006  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.5230 0.1618 0.1072 -0.0373 -0.0210 -0.0025 74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.5181 0.1440 0.0933 -0.0636 -0.0283 0.0010  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.5536 0.1963 0.1424 -0.0897 -0.0261 0.0070  75  SER   A N   
543  C CA  . SER   A 69  ? 0.5772 0.2301 0.1668 -0.1117 -0.0396 0.0144  75  SER   A CA  
544  C C   . SER   A 69  ? 0.5641 0.2202 0.1701 -0.1069 -0.0605 0.0235  75  SER   A C   
545  O O   . SER   A 69  ? 0.5532 0.2071 0.1790 -0.0884 -0.0638 0.0216  75  SER   A O   
546  C CB  . SER   A 69  ? 0.6172 0.2791 0.2180 -0.1180 -0.0406 0.0188  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.6843 0.3456 0.2725 -0.1300 -0.0232 0.0102  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.5676 0.2310 0.1688 -0.1244 -0.0730 0.0320  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.5702 0.2367 0.1945 -0.1205 -0.0928 0.0431  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.5710 0.2585 0.2086 -0.1452 -0.1138 0.0656  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.5695 0.2711 0.1843 -0.1700 -0.1118 0.0691  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.5751 0.2311 0.1872 -0.1131 -0.0899 0.0361  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.5955 0.2524 0.1771 -0.1312 -0.0802 0.0322  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.6130 0.2584 0.1770 -0.1259 -0.0581 0.0170  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.6049 0.2761 0.1813 -0.1538 -0.0927 0.0441  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.6228 0.2688 0.1685 -0.1428 -0.0459 0.0095  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.6203 0.2953 0.1696 -0.1728 -0.0804 0.0359  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.6244 0.2850 0.1608 -0.1662 -0.0561 0.0165  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.5571 0.2501 0.2367 -0.1401 -0.1337 0.0813  77  SER   A N   
560  C CA  . SER   A 71  ? 0.5490 0.2666 0.2507 -0.1641 -0.1569 0.1105  77  SER   A CA  
561  C C   . SER   A 71  ? 0.5470 0.2770 0.2278 -0.1849 -0.1657 0.1220  77  SER   A C   
562  O O   . SER   A 71  ? 0.5328 0.2474 0.1950 -0.1748 -0.1557 0.1070  77  SER   A O   
563  C CB  . SER   A 71  ? 0.5385 0.2583 0.3062 -0.1516 -0.1740 0.1256  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.5564 0.2625 0.3446 -0.1340 -0.1756 0.1176  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.5511 0.3123 0.2340 -0.2161 -0.1844 0.1497  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.5689 0.3480 0.2322 -0.2389 -0.1929 0.1624  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.5785 0.3484 0.2871 -0.2215 -0.2080 0.1754  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.5579 0.3168 0.3192 -0.2001 -0.2157 0.1795  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.5759 0.3995 0.2336 -0.2798 -0.2123 0.1937  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.6641 0.5004 0.2724 -0.3026 -0.1954 0.1754  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.7394 0.6267 0.3319 -0.3489 -0.2133 0.2026  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.8108 0.7083 0.3679 -0.3674 -0.1971 0.1817  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.8494 0.7999 0.3711 -0.4190 -0.2060 0.1945  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.6032 0.3751 0.2957 -0.2284 -0.2093 0.1772  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.6111 0.3725 0.3505 -0.2108 -0.2225 0.1870  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.6135 0.3980 0.4206 -0.2196 -0.2520 0.2273  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.6049 0.4247 0.4101 -0.2506 -0.2682 0.2585  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.6282 0.3931 0.3319 -0.2230 -0.2179 0.1843  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.6384 0.4315 0.2920 -0.2583 -0.2125 0.1879  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.6185 0.4031 0.2551 -0.2532 -0.1975 0.1686  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.6127 0.3794 0.4843 -0.1935 -0.2582 0.2258  80  SER   A N   
582  C CA  . SER   A 74  ? 0.5939 0.3792 0.5473 -0.1984 -0.2839 0.2627  80  SER   A CA  
583  C C   . SER   A 74  ? 0.5795 0.3448 0.6087 -0.1718 -0.2881 0.2559  80  SER   A C   
584  O O   . SER   A 74  ? 0.5836 0.3222 0.5948 -0.1501 -0.2716 0.2211  80  SER   A O   
585  C CB  . SER   A 74  ? 0.6151 0.4086 0.5861 -0.2010 -0.2850 0.2686  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.6616 0.4247 0.6430 -0.1702 -0.2649 0.2313  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.5504 0.3317 0.6702 -0.1754 -0.3106 0.2902  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.5502 0.3165 0.7611 -0.1533 -0.3148 0.2848  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.5642 0.3112 0.8034 -0.1304 -0.2975 0.2516  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.5600 0.3200 0.8256 -0.1374 -0.3032 0.2686  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.5143 0.3094 0.8216 -0.1696 -0.3461 0.3403  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.5321 0.3413 0.8535 -0.1826 -0.3635 0.3695  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.4999 0.3466 0.9184 -0.2038 -0.3977 0.4352  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.5461 0.3243 0.9002 -0.1557 -0.3522 0.3351  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.5761 0.2955 0.8089 -0.1050 -0.2765 0.2049  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.5880 0.2922 0.8410 -0.0842 -0.2564 0.1672  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.5890 0.2797 0.9183 -0.0648 -0.2510 0.1403  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.5945 0.2774 0.9123 -0.0611 -0.2516 0.1307  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.6260 0.3166 0.7748 -0.0771 -0.2316 0.1314  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.6524 0.3555 0.7480 -0.0941 -0.2324 0.1501  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.6260 0.3017 0.7848 -0.0541 -0.2082 0.0849  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.7062 0.4025 0.7052 -0.0980 -0.2180 0.1346  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.5799 0.2687 0.9880 -0.0534 -0.2438 0.1250  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.5773 0.2555 1.0637 -0.0369 -0.2342 0.0913  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.6029 0.2670 1.0189 -0.0221 -0.2072 0.0341  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.6158 0.2788 0.9713 -0.0181 -0.1897 0.0128  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.5495 0.2325 1.1490 -0.0315 -0.2320 0.0902  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.5486 0.2228 1.2401 -0.0166 -0.2184 0.0493  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.5390 0.2136 1.3193 -0.0178 -0.2340 0.0662  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.5685 0.2370 1.2595 -0.0033 -0.1888 -0.0074 83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.5312 0.1979 1.4006 -0.0053 -0.2192 0.0232  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5600 0.2241 1.3343 0.0069  -0.1736 -0.0515 83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5339 0.1960 1.3996 0.0062  -0.1884 -0.0375 83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.6007 0.2573 1.0263 -0.0157 -0.2052 0.0125  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.6272 0.2766 0.9918 -0.0050 -0.1834 -0.0373 84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.6226 0.2708 1.0729 0.0049  -0.1724 -0.0789 84  VAL   A C   
617  O O   . VAL   A 78  ? 0.5989 0.2444 1.1216 0.0042  -0.1856 -0.0685 84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.6478 0.2917 0.9286 -0.0090 -0.1893 -0.0291 84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.6622 0.3034 0.8907 0.0005  -0.1698 -0.0760 84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.6740 0.3204 0.8731 -0.0205 -0.1952 0.0040  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6361 0.2887 1.0796 0.0124  -0.1471 -0.1274 85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.6274 0.2836 1.1452 0.0189  -0.1304 -0.1786 85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.6383 0.2910 1.1449 0.0196  -0.1340 -0.1966 85  GLU   A C   
624  O O   . GLU   A 79  ? 0.6691 0.3171 1.0940 0.0166  -0.1449 -0.1753 85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.6712 0.3396 1.1503 0.0222  -0.1013 -0.2278 85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.7304 0.4027 1.2217 0.0223  -0.0951 -0.2149 85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.7802 0.4543 1.4050 0.0250  -0.0889 -0.2264 85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 0.7687 0.4470 1.4640 0.0277  -0.0738 -0.2725 85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.7953 0.4680 1.4585 0.0234  -0.0986 -0.1901 85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.6125 0.2681 1.2040 0.0227  -0.1232 -0.2383 86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.6164 0.2702 1.2097 0.0226  -0.1260 -0.2594 86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.6479 0.3121 1.1286 0.0209  -0.1130 -0.2927 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.6666 0.3449 1.0955 0.0200  -0.0938 -0.3195 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.5799 0.2362 1.3006 0.0248  -0.1148 -0.3009 86  ALA   A CB  
635  N N   . SER   A 81  ? 0.6472 0.3070 1.0944 0.0196  -0.1243 -0.2878 87  SER   A N   
636  C CA  . SER   A 81  ? 0.6708 0.3425 1.0240 0.0167  -0.1165 -0.3137 87  SER   A CA  
637  C C   . SER   A 81  ? 0.6649 0.3353 1.0582 0.0154  -0.1226 -0.3345 87  SER   A C   
638  O O   . SER   A 81  ? 0.6528 0.3123 1.1474 0.0176  -0.1314 -0.3279 87  SER   A O   
639  C CB  . SER   A 81  ? 0.6981 0.3634 0.9459 0.0158  -0.1276 -0.2703 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.6980 0.3467 0.9539 0.0154  -0.1495 -0.2295 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.6789 0.3619 1.0002 0.0112  -0.1194 -0.3561 88  GLU   A N   
642  C CA  . GLU   A 82  ? 0.6731 0.3557 1.0303 0.0092  -0.1261 -0.3755 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.6724 0.3327 1.0272 0.0124  -0.1513 -0.3227 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.6670 0.3231 1.0646 0.0118  -0.1598 -0.3303 88  GLU   A O   
645  C CB  . GLU   A 82  ? 0.7259 0.4351 1.0126 0.0008  -0.1152 -0.4173 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 0.8557 0.5666 1.0311 -0.0004 -0.1255 -0.3832 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 0.9687 0.7080 1.0878 -0.0104 -0.1211 -0.4151 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 0.9941 0.7297 1.0578 -0.0106 -0.1346 -0.3871 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 0.9920 0.7600 1.1254 -0.0197 -0.1038 -0.4686 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.6741 0.3225 0.9808 0.0140  -0.1621 -0.2715 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.6746 0.3070 0.9710 0.0136  -0.1831 -0.2223 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.6408 0.2625 1.0180 0.0133  -0.1973 -0.1835 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.6419 0.2555 1.0427 0.0108  -0.2150 -0.1492 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7091 0.3396 0.8971 0.0116  -0.1848 -0.1921 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.7333 0.3786 0.8420 0.0107  -0.1719 -0.2203 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.7550 0.4038 0.8317 0.0090  -0.1768 -0.2267 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.7460 0.4050 0.8146 0.0103  -0.1562 -0.2369 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.7813 0.4491 0.7889 0.0059  -0.1678 -0.2458 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.7717 0.4505 0.7708 0.0071  -0.1463 -0.2567 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.7953 0.4792 0.7636 0.0044  -0.1531 -0.2588 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.8285 0.5367 0.7313 -0.0008 -0.1460 -0.2717 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.6108 0.2356 1.0290 0.0144  -0.1904 -0.1847 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.5760 0.1962 1.0721 0.0121  -0.2054 -0.1425 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.5745 0.1993 1.1669 0.0157  -0.1937 -0.1676 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.5852 0.2177 1.1487 0.0183  -0.1729 -0.2057 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.5706 0.1912 0.9941 0.0062  -0.2122 -0.0983 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.5711 0.1879 0.9009 0.0005  -0.2206 -0.0709 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.5548 0.1695 0.9049 -0.0068 -0.2404 -0.0309 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.5911 0.2087 0.8177 0.0010  -0.2083 -0.0811 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.5770 0.1899 0.8450 -0.0136 -0.2451 -0.0080 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.6066 0.2204 0.7585 -0.0045 -0.2134 -0.0574 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.5959 0.2071 0.7675 -0.0121 -0.2307 -0.0227 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.5915 0.1999 0.6944 -0.0184 -0.2327 -0.0043 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.5571 0.1796 1.2650 0.0147  -0.2074 -0.1398 91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.5377 0.1644 1.3440 0.0178  -0.1969 -0.1548 91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.5685 0.1995 1.3245 0.0144  -0.1989 -0.1224 91  PRO   A C   
677  O O   . PRO   A 85  ? 0.5997 0.2304 1.2586 0.0086  -0.2098 -0.0873 91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.5052 0.1296 1.4476 0.0161  -0.2165 -0.1197 91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.5264 0.1500 1.4129 0.0080  -0.2426 -0.0613 91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.5424 0.1618 1.2963 0.0091  -0.2340 -0.0863 91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.5428 0.1783 1.3701 0.0170  -0.1880 -0.1339 92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5572 0.1974 1.3459 0.0132  -0.1912 -0.1020 92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.5381 0.1820 1.3616 0.0028  -0.2230 -0.0285 92  ALA   A C   
684  O O   . ALA   A 86  ? 0.5032 0.1499 1.4504 0.0015  -0.2361 -0.0056 92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5349 0.1799 1.4064 0.0183  -0.1724 -0.1312 92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.5512 0.1982 1.2690 -0.0065 -0.2349 0.0078  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.5227 0.1807 1.2544 -0.0216 -0.2643 0.0757  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.5486 0.2157 1.1868 -0.0329 -0.2677 0.1037  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.5793 0.2419 1.1640 -0.0264 -0.2479 0.0724  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.5239 0.1787 1.2198 -0.0259 -0.2760 0.0881  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.5725 0.2216 1.1218 -0.0277 -0.2664 0.0743  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.5827 0.2201 1.0949 -0.0198 -0.2580 0.0407  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.6167 0.2531 1.0171 -0.0273 -0.2598 0.0547  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.6178 0.2503 0.9194 -0.0251 -0.2437 0.0343  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.5938 0.2252 0.8106 -0.0326 -0.2448 0.0482  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.6156 0.2467 0.9079 -0.0160 -0.2256 0.0006  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.5336 0.2166 1.1534 -0.0518 -0.2920 0.1611  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.5488 0.2432 1.0763 -0.0665 -0.2953 0.1851  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.5498 0.2409 0.9732 -0.0735 -0.2942 0.1843  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.5426 0.2386 0.9863 -0.0803 -0.3088 0.2064  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.5387 0.2608 1.1187 -0.0884 -0.3234 0.2499  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.5329 0.2611 1.2025 -0.0847 -0.3246 0.2573  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.5623 0.2902 1.1823 -0.0841 -0.3118 0.2438  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.5006 0.2345 1.3125 -0.0815 -0.3376 0.2778  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.5501 0.2833 1.2550 -0.0802 -0.3116 0.2496  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.4826 0.2220 1.3868 -0.0779 -0.3373 0.2847  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.5216 0.2602 1.3697 -0.0769 -0.3238 0.2691  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.5224 0.2661 1.4644 -0.0729 -0.3224 0.2750  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.5500 0.2333 0.8692 -0.0716 -0.2763 0.1594  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.5511 0.2310 0.7774 -0.0783 -0.2725 0.1573  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.5485 0.2477 0.7150 -0.1023 -0.2802 0.1911  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.5556 0.2598 0.7049 -0.1055 -0.2747 0.1909  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.5739 0.2336 0.7360 -0.0603 -0.2469 0.1064  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.5988 0.2541 0.6663 -0.0663 -0.2393 0.1031  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.6306 0.2698 0.6571 -0.0489 -0.2199 0.0604  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.6175 0.2503 0.6863 -0.0353 -0.2168 0.0348  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.6415 0.2767 0.5880 -0.0510 -0.2068 0.0529  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.5392 0.2526 0.6789 -0.1213 -0.2927 0.2198  96  SER   A N   
719  C CA  . SER   A 90  ? 0.5428 0.2808 0.6258 -0.1493 -0.2990 0.2487  96  SER   A CA  
720  C C   . SER   A 90  ? 0.5595 0.2867 0.5399 -0.1510 -0.2763 0.2196  96  SER   A C   
721  O O   . SER   A 90  ? 0.5610 0.2632 0.5154 -0.1312 -0.2594 0.1845  96  SER   A O   
722  C CB  . SER   A 90  ? 0.5634 0.3305 0.6723 -0.1742 -0.3237 0.2965  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.6216 0.3781 0.7055 -0.1703 -0.3190 0.2852  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.5585 0.3067 0.4859 -0.1760 -0.2757 0.2341  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.5930 0.3341 0.4343 -0.1816 -0.2531 0.2084  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.5755 0.2856 0.3949 -0.1536 -0.2292 0.1663  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.5855 0.2807 0.3550 -0.1475 -0.2104 0.1418  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.6325 0.3748 0.4433 -0.1904 -0.2507 0.2086  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.6646 0.4431 0.4881 -0.2215 -0.2722 0.2504  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.7063 0.5145 0.4757 -0.2551 -0.2693 0.2607  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.6578 0.4504 0.5443 -0.2253 -0.2964 0.2842  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.6923 0.5352 0.4874 -0.2798 -0.2926 0.3022  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.6670 0.5009 0.5352 -0.2622 -0.3102 0.3201  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.5513 0.2548 0.4139 -0.1378 -0.2304 0.1603  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.5540 0.2357 0.4012 -0.1140 -0.2098 0.1245  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.5514 0.2375 0.3642 -0.1205 -0.1985 0.1202  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.5519 0.2561 0.3853 -0.1357 -0.2106 0.1433  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.5328 0.2066 0.4500 -0.0938 -0.2141 0.1145  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.5563 0.2130 0.4614 -0.0702 -0.1934 0.0749  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.5836 0.2279 0.4390 -0.0623 -0.1814 0.0543  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.5463 0.2005 0.5283 -0.0553 -0.1965 0.0618  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.5546 0.2262 0.3201 -0.1098 -0.1764 0.0932  99  MET   A N   
743  C CA  . MET   A 93  ? 0.5471 0.2212 0.2831 -0.1147 -0.1637 0.0873  99  MET   A CA  
744  C C   . MET   A 93  ? 0.5506 0.2115 0.2934 -0.0907 -0.1490 0.0630  99  MET   A C   
745  O O   . MET   A 93  ? 0.5621 0.2108 0.2930 -0.0746 -0.1387 0.0433  99  MET   A O   
746  C CB  . MET   A 93  ? 0.5683 0.2423 0.2454 -0.1289 -0.1489 0.0805  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.5987 0.2918 0.2616 -0.1574 -0.1599 0.1003  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.6632 0.3516 0.2671 -0.1700 -0.1354 0.0805  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.6261 0.2878 0.2332 -0.1409 -0.1261 0.0625  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.5398 0.2062 0.3014 -0.0899 -0.1480 0.0651  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.5349 0.1938 0.3047 -0.0695 -0.1334 0.0425  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.5392 0.1969 0.2700 -0.0699 -0.1159 0.0346  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.5440 0.2099 0.2663 -0.0859 -0.1185 0.0481  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.5178 0.1833 0.3533 -0.0645 -0.1429 0.0473  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.5251 0.1898 0.4203 -0.0574 -0.1554 0.0471  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.5100 0.1814 0.4802 -0.0534 -0.1613 0.0512  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.5439 0.1988 0.4264 -0.0407 -0.1428 0.0169  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.5314 0.1825 0.2440 -0.0536 -0.0991 0.0139  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.5402 0.1911 0.2249 -0.0500 -0.0812 0.0065  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.5223 0.1776 0.2209 -0.0328 -0.0709 -0.0111 101 ALA   A C   
761  O O   . ALA   A 95  ? 0.5140 0.1710 0.2305 -0.0234 -0.0733 -0.0242 101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.5633 0.2072 0.2067 -0.0512 -0.0695 0.0034  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.5170 0.1769 0.2073 -0.0306 -0.0584 -0.0131 102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.5117 0.1812 0.2070 -0.0178 -0.0453 -0.0293 102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.5229 0.1949 0.1793 -0.0124 -0.0346 -0.0340 102 VAL   A C   
766  O O   . VAL   A 96  ? 0.5278 0.1956 0.1590 -0.0165 -0.0274 -0.0234 102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.5216 0.1964 0.2230 -0.0193 -0.0365 -0.0250 102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.5338 0.2231 0.2339 -0.0082 -0.0205 -0.0411 102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.5179 0.1930 0.2628 -0.0261 -0.0494 -0.0158 102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.5212 0.2009 0.1783 -0.0051 -0.0346 -0.0489 103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.5362 0.2236 0.1608 -0.0018 -0.0277 -0.0494 103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.5601 0.2613 0.1866 0.0032  -0.0292 -0.0686 103 GLY   A C   
773  O O   . GLY   A 97  ? 0.5617 0.2625 0.2199 0.0047  -0.0353 -0.0844 103 GLY   A O   
774  N N   . HIS   A 98  ? 0.5681 0.2851 0.1652 0.0043  -0.0231 -0.0667 104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.5732 0.3102 0.1647 0.0054  -0.0240 -0.0851 104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.5730 0.2975 0.1674 0.0051  -0.0371 -0.0858 104 HIS   A C   
777  O O   . HIS   A 98  ? 0.5701 0.2781 0.1538 0.0037  -0.0420 -0.0663 104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.6002 0.3679 0.1597 0.0033  -0.0144 -0.0786 104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.6442 0.4405 0.1926 -0.0001 -0.0155 -0.0985 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.6620 0.4728 0.2292 -0.0014 -0.0110 -0.1328 104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.6738 0.4876 0.1987 -0.0040 -0.0206 -0.0898 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.6756 0.5139 0.2254 -0.0075 -0.0125 -0.1471 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.6864 0.5283 0.2091 -0.0093 -0.0198 -0.1201 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.5782 0.3135 0.1880 0.0057  -0.0404 -0.1106 105 SER   A N   
785  C CA  . SER   A 99  ? 0.5965 0.3248 0.2109 0.0054  -0.0522 -0.1148 105 SER   A CA  
786  C C   . SER   A 99  ? 0.6055 0.3579 0.2311 0.0038  -0.0501 -0.1485 105 SER   A C   
787  O O   . SER   A 99  ? 0.5878 0.3577 0.2279 0.0028  -0.0395 -0.1720 105 SER   A O   
788  C CB  . SER   A 99  ? 0.6098 0.3087 0.2551 0.0060  -0.0644 -0.1059 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.6264 0.3235 0.3192 0.0075  -0.0668 -0.1239 105 SER   A OG  
790  N N   . GLU   A 100 ? 0.6208 0.3756 0.2407 0.0022  -0.0590 -0.1525 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.6201 0.3957 0.2527 -0.0016 -0.0594 -0.1859 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.6277 0.3805 0.2819 0.0008  -0.0746 -0.1814 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.6383 0.3704 0.2782 0.0029  -0.0826 -0.1512 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.6489 0.4641 0.2366 -0.0101 -0.0550 -0.1895 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.7060 0.5422 0.2627 -0.0129 -0.0434 -0.1750 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.7506 0.6388 0.2760 -0.0254 -0.0352 -0.1912 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 0.7630 0.6735 0.2812 -0.0336 -0.0405 -0.2094 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 0.7514 0.6615 0.2598 -0.0289 -0.0235 -0.1859 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.6195 0.3772 0.3087 -0.0006 -0.0778 -0.2117 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.6151 0.3505 0.3293 0.0019  -0.0930 -0.2041 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.6257 0.3568 0.2997 0.0009  -0.1020 -0.1769 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.6379 0.3431 0.3229 0.0036  -0.1122 -0.1551 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.6046 0.3552 0.3586 -0.0014 -0.0913 -0.2461 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.6031 0.3903 0.3401 -0.0084 -0.0737 -0.2781 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.5916 0.3731 0.3099 -0.0048 -0.0661 -0.2557 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.6277 0.3865 0.2584 -0.0043 -0.0978 -0.1755 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.6321 0.3914 0.2319 -0.0057 -0.1051 -0.1481 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.6293 0.3662 0.2149 -0.0018 -0.1034 -0.1116 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.6291 0.3604 0.2021 -0.0021 -0.1081 -0.0887 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.6260 0.3502 0.2181 0.0009  -0.0958 -0.1075 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.6208 0.3248 0.2038 0.0022  -0.0917 -0.0796 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.6041 0.2777 0.2071 0.0023  -0.0995 -0.0691 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.6071 0.2661 0.2008 0.0001  -0.0955 -0.0487 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.6384 0.3460 0.2188 0.0028  -0.0806 -0.0803 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.6617 0.3999 0.2154 0.0007  -0.0713 -0.0778 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.6650 0.4125 0.2009 -0.0012 -0.0719 -0.0578 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.6779 0.4332 0.2323 -0.0001 -0.0634 -0.0943 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.5830 0.2497 0.2168 0.0029  -0.1100 -0.0831 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.5762 0.2205 0.2303 0.0004  -0.1194 -0.0695 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.5679 0.2046 0.2018 -0.0018 -0.1202 -0.0520 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.5732 0.2214 0.1955 0.0002  -0.1210 -0.0553 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.5786 0.2206 0.2761 0.0016  -0.1309 -0.0842 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.6251 0.2738 0.3656 0.0039  -0.1284 -0.1048 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.5503 0.1716 0.1812 -0.0076 -0.1187 -0.0345 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.5558 0.1694 0.1739 -0.0107 -0.1152 -0.0205 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.5592 0.1714 0.1582 -0.0134 -0.0996 -0.0096 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.5611 0.1638 0.1579 -0.0189 -0.0926 0.0007  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.5515 0.1736 0.1417 -0.0103 -0.0926 -0.0133 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.5544 0.1759 0.1339 -0.0125 -0.0775 -0.0033 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.5584 0.1656 0.1391 -0.0232 -0.0715 0.0007  112 GLY   A C   
831  O O   . GLY   A 106 ? 0.5490 0.1540 0.1349 -0.0282 -0.0793 -0.0028 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.5622 0.1623 0.1426 -0.0288 -0.0579 0.0082  113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.5720 0.1635 0.1510 -0.0435 -0.0497 0.0075  113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.5610 0.1552 0.1346 -0.0483 -0.0405 0.0054  113 ILE   A C   
835  O O   . ILE   A 107 ? 0.5659 0.1642 0.1413 -0.0408 -0.0315 0.0080  113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.5993 0.1827 0.1876 -0.0495 -0.0356 0.0104  113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.6140 0.1938 0.2067 -0.0503 -0.0464 0.0117  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.6199 0.1993 0.2072 -0.0673 -0.0184 0.0041  113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.6344 0.2068 0.2413 -0.0559 -0.0323 0.0134  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.5509 0.1458 0.1194 -0.0623 -0.0439 0.0033  114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.5482 0.1464 0.1114 -0.0723 -0.0355 0.0012  114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.5671 0.1628 0.1270 -0.0918 -0.0196 -0.0042 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.5704 0.1674 0.1265 -0.1037 -0.0236 -0.0043 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.5443 0.1507 0.1078 -0.0790 -0.0519 0.0045  114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.5512 0.1644 0.1086 -0.0940 -0.0458 0.0042  114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.5513 0.1639 0.1119 -0.0819 -0.0361 0.0012  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.5529 0.1777 0.1173 -0.1046 -0.0658 0.0142  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.5705 0.1645 0.1349 -0.0963 -0.0004 -0.0101 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.5933 0.1853 0.1625 -0.1144 0.0198  -0.0215 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.6063 0.2035 0.1748 -0.1291 0.0344  -0.0318 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.5987 0.1955 0.1722 -0.1185 0.0348  -0.0275 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.6219 0.2033 0.2162 -0.1011 0.0330  -0.0194 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.6957 0.2721 0.3101 -0.1156 0.0575  -0.0329 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.7458 0.3131 0.3980 -0.0995 0.0688  -0.0240 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.7956 0.3594 0.4521 -0.0916 0.0592  -0.0157 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.8043 0.3644 0.4699 -0.1038 0.0693  -0.0257 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.7764 0.3387 0.4446 -0.1267 0.0902  -0.0471 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.8008 0.3578 0.4720 -0.0951 0.0591  -0.0163 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.6227 0.2283 0.1826 -0.1558 0.0452  -0.0458 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.6392 0.2523 0.1994 -0.1744 0.0615  -0.0605 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.6641 0.2723 0.2481 -0.1875 0.0928  -0.0827 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.6599 0.2594 0.2587 -0.1814 0.0988  -0.0831 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.6583 0.2937 0.1890 -0.2006 0.0477  -0.0603 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.6572 0.3093 0.1684 -0.2286 0.0466  -0.0662 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.6902 0.3047 0.2827 -0.2070 0.1138  -0.1033 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.7166 0.3279 0.3403 -0.2226 0.1472  -0.1304 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.7335 0.3562 0.3411 -0.2450 0.1522  -0.1442 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.7478 0.3645 0.3884 -0.2525 0.1797  -0.1650 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.7612 0.3824 0.3929 -0.2453 0.1677  -0.1550 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.8401 0.4887 0.4223 -0.2732 0.1516  -0.1579 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.9298 0.5948 0.5132 -0.3025 0.1708  -0.1856 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.9606 0.6478 0.5098 -0.3205 0.1541  -0.1805 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.9431 0.5996 0.5708 -0.3098 0.2062  -0.2155 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.7282 0.3685 0.2917 -0.2563 0.1268  -0.1316 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.7307 0.3868 0.2756 -0.2794 0.1288  -0.1400 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.7096 0.3508 0.2623 -0.2568 0.1156  -0.1212 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.7086 0.3609 0.2509 -0.2733 0.1184  -0.1268 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.7615 0.4510 0.2598 -0.3085 0.1077  -0.1321 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.7963 0.5096 0.2803 -0.3400 0.1199  -0.1526 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.8222 0.5261 0.3182 -0.3284 0.1205  -0.1519 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.8145 0.5641 0.2710 -0.3841 0.1301  -0.1729 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.8292 0.5611 0.3072 -0.3642 0.1306  -0.1722 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.8232 0.5850 0.2753 -0.3999 0.1366  -0.1860 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.6860 0.3059 0.2554 -0.2217 0.1014  -0.0999 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.6638 0.2717 0.2407 -0.2008 0.0875  -0.0828 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.6518 0.2586 0.2116 -0.1808 0.0539  -0.0570 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.6542 0.2635 0.2061 -0.1749 0.0440  -0.0504 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.6339 0.2366 0.1936 -0.1697 0.0378  -0.0440 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.6220 0.2235 0.1747 -0.1513 0.0085  -0.0243 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.6132 0.2329 0.1457 -0.1666 -0.0113 -0.0150 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.6299 0.2665 0.1491 -0.1908 -0.0145 -0.0136 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.6342 0.2276 0.1972 -0.1377 -0.0020 -0.0156 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.6376 0.2313 0.1992 -0.1212 -0.0299 -0.0010 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.6292 0.2078 0.2177 -0.1216 0.0134  -0.0183 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.5922 0.2117 0.1258 -0.1539 -0.0253 -0.0064 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.6098 0.2463 0.1366 -0.1655 -0.0459 0.0069  121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.6016 0.2369 0.1445 -0.1512 -0.0715 0.0233  121 VAL   A C   
898  O O   . VAL   A 115 ? 0.5971 0.2480 0.1433 -0.1655 -0.0889 0.0386  121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.6230 0.2605 0.1497 -0.1617 -0.0433 0.0048  121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.6315 0.2852 0.1625 -0.1692 -0.0667 0.0221  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.6240 0.2661 0.1396 -0.1805 -0.0191 -0.0121 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.5850 0.2044 0.1413 -0.1246 -0.0731 0.0201  122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.5697 0.1867 0.1465 -0.1104 -0.0934 0.0284  122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.5693 0.1739 0.1538 -0.0849 -0.0903 0.0191  122 GLY   A C   
905  O O   . GLY   A 116 ? 0.5578 0.1564 0.1326 -0.0788 -0.0736 0.0115  122 GLY   A O   
906  N N   . ILE   A 117 ? 0.5672 0.1714 0.1727 -0.0723 -0.1062 0.0201  123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.5728 0.1727 0.1831 -0.0524 -0.1050 0.0093  123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.5682 0.1740 0.1990 -0.0427 -0.1137 0.0026  123 ILE   A C   
909  O O   . ILE   A 117 ? 0.5582 0.1678 0.2142 -0.0482 -0.1268 0.0096  123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.5867 0.1821 0.2052 -0.0477 -0.1120 0.0092  123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.5914 0.1893 0.2354 -0.0535 -0.1300 0.0171  123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.5967 0.1861 0.2000 -0.0543 -0.0989 0.0125  123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.5932 0.1871 0.2522 -0.0456 -0.1384 0.0139  123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.5572 0.1668 0.1821 -0.0295 -0.1064 -0.0099 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.5397 0.1574 0.1846 -0.0212 -0.1099 -0.0224 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.5390 0.1565 0.2201 -0.0186 -0.1249 -0.0280 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.5391 0.1542 0.2188 -0.0160 -0.1290 -0.0307 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.5429 0.1715 0.1710 -0.0111 -0.0995 -0.0357 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.5347 0.1747 0.1863 -0.0050 -0.1010 -0.0546 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.5592 0.1890 0.1618 -0.0129 -0.0849 -0.0271 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.5419 0.1618 0.2615 -0.0198 -0.1333 -0.0279 125 SER   A N   
922  C CA  . SER   A 119 ? 0.5447 0.1644 0.3139 -0.0177 -0.1470 -0.0317 125 SER   A CA  
923  C C   . SER   A 119 ? 0.5449 0.1722 0.3554 -0.0093 -0.1443 -0.0542 125 SER   A C   
924  O O   . SER   A 119 ? 0.5398 0.1696 0.3836 -0.0035 -0.1472 -0.0738 125 SER   A O   
925  C CB  . SER   A 119 ? 0.5582 0.1766 0.3534 -0.0303 -0.1618 -0.0045 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.5511 0.1692 0.4016 -0.0283 -0.1759 -0.0036 125 SER   A OG  
927  N N   . THR   A 120 ? 0.5398 0.1716 0.3508 -0.0096 -0.1371 -0.0540 126 THR   A N   
928  C CA  . THR   A 120 ? 0.5352 0.1750 0.3908 -0.0032 -0.1318 -0.0759 126 THR   A CA  
929  C C   . THR   A 120 ? 0.5629 0.2118 0.3860 0.0001  -0.1148 -0.0878 126 THR   A C   
930  O O   . THR   A 120 ? 0.5712 0.2179 0.3468 -0.0035 -0.1096 -0.0728 126 THR   A O   
931  C CB  . THR   A 120 ? 0.5246 0.1626 0.4454 -0.0082 -0.1449 -0.0571 126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.5520 0.1906 0.4487 -0.0170 -0.1462 -0.0322 126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.5332 0.1663 0.4920 -0.0134 -0.1633 -0.0383 126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.5614 0.2214 0.4163 0.0055  -0.1054 -0.1150 127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.5797 0.2518 0.4117 0.0077  -0.0890 -0.1267 127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.5687 0.2523 0.4565 0.0113  -0.0796 -0.1570 127 GLY   A C   
937  O O   . GLY   A 121 ? 0.5648 0.2498 0.5014 0.0130  -0.0822 -0.1778 127 GLY   A O   
938  N N   . GLY   A 122 ? 0.5707 0.2627 0.4558 0.0121  -0.0673 -0.1611 128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.5655 0.2703 0.5033 0.0147  -0.0538 -0.1915 128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.5868 0.2929 0.5327 0.0148  -0.0469 -0.1800 128 GLY   A C   
941  O O   . GLY   A 122 ? 0.6016 0.2942 0.5438 0.0118  -0.0590 -0.1456 128 GLY   A O   
942  N N   . ASN   A 123 ? 0.5812 0.3064 0.5377 0.0162  -0.0266 -0.2103 129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.5794 0.3079 0.5496 0.0169  -0.0176 -0.2037 129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.5845 0.3093 0.4862 0.0148  -0.0191 -0.1723 129 ASN   A C   
945  O O   . ASN   A 123 ? 0.5783 0.2968 0.4950 0.0139  -0.0212 -0.1529 129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.5874 0.3018 0.6436 0.0177  -0.0292 -0.1887 129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.6356 0.3522 0.7811 0.0202  -0.0261 -0.2179 129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.6366 0.3686 0.7860 0.0207  -0.0095 -0.2606 129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.6425 0.3467 0.8675 0.0200  -0.0420 -0.1949 129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.5929 0.3224 0.4275 0.0134  -0.0183 -0.1670 130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.5980 0.3234 0.3785 0.0113  -0.0180 -0.1392 130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.5873 0.2892 0.3632 0.0072  -0.0352 -0.1068 130 GLY   A C   
953  O O   . GLY   A 124 ? 0.5906 0.2872 0.3402 0.0036  -0.0341 -0.0862 130 GLY   A O   
954  N N   . LEU   A 125 ? 0.5740 0.2646 0.3775 0.0058  -0.0503 -0.1034 131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.5831 0.2575 0.3837 -0.0017 -0.0672 -0.0748 131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.5718 0.2408 0.3503 -0.0017 -0.0740 -0.0757 131 LEU   A C   
957  O O   . LEU   A 125 ? 0.5652 0.2399 0.3604 0.0035  -0.0728 -0.0973 131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.5877 0.2581 0.4549 -0.0055 -0.0818 -0.0637 131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.6130 0.2896 0.5182 -0.0050 -0.0767 -0.0631 131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.6039 0.2809 0.5941 -0.0051 -0.0882 -0.0603 131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.6435 0.3180 0.5181 -0.0145 -0.0799 -0.0370 131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.5667 0.2260 0.3089 -0.0086 -0.0794 -0.0547 132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.5539 0.2068 0.2762 -0.0097 -0.0856 -0.0519 132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.5407 0.1843 0.2740 -0.0213 -0.1012 -0.0287 132 VAL   A C   
965  O O   . VAL   A 126 ? 0.5301 0.1732 0.2539 -0.0316 -0.1021 -0.0123 132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.5689 0.2234 0.2391 -0.0081 -0.0739 -0.0507 132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.5766 0.2273 0.2238 -0.0145 -0.0660 -0.0353 132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.5822 0.2295 0.2378 -0.0095 -0.0805 -0.0463 132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.5363 0.1763 0.2912 -0.0215 -0.1132 -0.0279 133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.5438 0.1805 0.3101 -0.0343 -0.1291 -0.0044 133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.5549 0.1851 0.2853 -0.0386 -0.1292 0.0003  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.5738 0.2008 0.2972 -0.0292 -0.1261 -0.0139 133 GLY   A O   
973  N N   . PHE   A 128 ? 0.5464 0.1775 0.2576 -0.0546 -0.1329 0.0192  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.5589 0.1852 0.2400 -0.0620 -0.1308 0.0237  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.5487 0.1816 0.2481 -0.0774 -0.1479 0.0443  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.5324 0.1778 0.2436 -0.0928 -0.1575 0.0625  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.5653 0.1908 0.2047 -0.0719 -0.1149 0.0241  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.5683 0.1908 0.1937 -0.0595 -0.0989 0.0108  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.5770 0.1948 0.1886 -0.0466 -0.0888 0.0002  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.5713 0.1992 0.1986 -0.0627 -0.0948 0.0124  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.5810 0.2018 0.1816 -0.0375 -0.0756 -0.0066 134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.5852 0.2127 0.2009 -0.0523 -0.0798 0.0027  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.5823 0.2074 0.1851 -0.0400 -0.0706 -0.0057 134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.5511 0.1789 0.2532 -0.0749 -0.1525 0.0438  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.5503 0.1864 0.2663 -0.0904 -0.1675 0.0649  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.5643 0.2071 0.2356 -0.1113 -0.1579 0.0714  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.5709 0.2037 0.2134 -0.1079 -0.1429 0.0583  135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.5643 0.1916 0.2960 -0.0797 -0.1724 0.0586  135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.5614 0.2239 0.2306 -0.1348 -0.1661 0.0911  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.5863 0.2605 0.2132 -0.1593 -0.1547 0.0919  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.6032 0.2808 0.2216 -0.1694 -0.1555 0.0966  136 ASP   A C   
992  O O   . ASP   A 130 ? 0.6129 0.2935 0.2629 -0.1663 -0.1733 0.1123  136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.6123 0.3146 0.2384 -0.1862 -0.1659 0.1130  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.6832 0.4024 0.2640 -0.2153 -0.1513 0.1072  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.6868 0.3917 0.2416 -0.2102 -0.1272 0.0817  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.7329 0.4831 0.3075 -0.2454 -0.1635 0.1284  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.6052 0.2815 0.1875 -0.1806 -0.1347 0.0817  137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.6202 0.3023 0.1943 -0.1931 -0.1327 0.0850  137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.6335 0.3413 0.1730 -0.2292 -0.1198 0.0829  137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.6496 0.3672 0.1798 -0.2441 -0.1154 0.0840  137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.6369 0.2933 0.2102 -0.1719 -0.1175 0.0658  137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.6343 0.2729 0.2378 -0.1422 -0.1307 0.0659  137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.6482 0.2935 0.2001 -0.1697 -0.0903 0.0427  137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.6347 0.3550 0.1556 -0.2443 -0.1120 0.0769  138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.6510 0.3985 0.1380 -0.2809 -0.0966 0.0674  138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.6847 0.4741 0.1618 -0.3167 -0.1137 0.0929  138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.7096 0.5247 0.1555 -0.3496 -0.0978 0.0808  138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.6454 0.3977 0.1201 -0.2879 -0.0880 0.0566  138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.6603 0.3780 0.1419 -0.2591 -0.0669 0.0316  138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.6849 0.4095 0.1588 -0.2667 -0.0615 0.0251  138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.7027 0.4301 0.1964 -0.2549 -0.0875 0.0490  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.7001 0.4315 0.1959 -0.2555 -0.0889 0.0498  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.6763 0.4107 0.1534 -0.2690 -0.0672 0.0285  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.6913 0.4241 0.2135 -0.2434 -0.1113 0.0709  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.6919 0.4919 0.1985 -0.3129 -0.1447 0.1278  139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.7017 0.5461 0.2068 -0.3472 -0.1654 0.1613  139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.7133 0.5576 0.2219 -0.3486 -0.1646 0.1656  139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.7051 0.5901 0.2065 -0.3810 -0.1771 0.1913  139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.7182 0.5747 0.2691 -0.3419 -0.2000 0.2017  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.7930 0.6153 0.3963 -0.3031 -0.2128 0.2082  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.8126 0.5959 0.4138 -0.2727 -0.1952 0.1775  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.8035 0.6411 0.4539 -0.3049 -0.2404 0.2445  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.7165 0.5180 0.2398 -0.3135 -0.1526 0.1444  140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.7090 0.5053 0.2397 -0.3106 -0.1510 0.1463  140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.7100 0.5159 0.2014 -0.3337 -0.1197 0.1183  140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.7041 0.4789 0.1957 -0.3142 -0.0969 0.0899  140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.7110 0.4633 0.2749 -0.2672 -0.1531 0.1366  140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.7168 0.4578 0.3238 -0.2436 -0.1776 0.1535  140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.7353 0.4383 0.3670 -0.2055 -0.1752 0.1361  140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.7090 0.4784 0.3511 -0.2590 -0.2074 0.1942  140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.7038 0.5566 0.1649 -0.3777 -0.1181 0.1265  141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.7269 0.5979 0.1517 -0.4077 -0.0859 0.0961  141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.7437 0.6024 0.1768 -0.4017 -0.0728 0.0869  141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.7670 0.6176 0.1878 -0.4080 -0.0390 0.0507  141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.7221 0.6563 0.1097 -0.4621 -0.0895 0.1081  141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.7422 0.6976 0.1230 -0.4742 -0.1071 0.1246  141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.7468 0.7716 0.0888 -0.5322 -0.1122 0.1388  141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.7677 0.6879 0.1463 -0.4529 -0.0855 0.0886  141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.7243 0.5793 0.1857 -0.3878 -0.0982 0.1182  142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.7235 0.5669 0.1972 -0.3806 -0.0896 0.1138  142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.7412 0.5322 0.2355 -0.3412 -0.0710 0.0851  142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.7481 0.5301 0.2503 -0.3386 -0.0570 0.0750  142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.6990 0.5544 0.2027 -0.3777 -0.1230 0.1565  142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.6869 0.5175 0.2317 -0.3443 -0.1517 0.1775  142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.6825 0.5331 0.2421 -0.3512 -0.1778 0.2073  142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.6839 0.4680 0.2636 -0.3010 -0.1556 0.1680  142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.6816 0.4995 0.2873 -0.3142 -0.1955 0.2142  142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.6827 0.4613 0.2976 -0.2842 -0.1823 0.1891  142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.6925 0.4432 0.2803 -0.2770 -0.1400 0.1452  142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.6855 0.4280 0.3388 -0.2464 -0.1914 0.1830  142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.7025 0.4190 0.3244 -0.2399 -0.1518 0.1428  142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.6949 0.4085 0.3471 -0.2259 -0.1763 0.1593  142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.7532 0.5134 0.2576 -0.3126 -0.0712 0.0745  143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.7751 0.4930 0.2988 -0.2788 -0.0554 0.0522  143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.8252 0.5413 0.3399 -0.2928 -0.0167 0.0191  143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.8339 0.5239 0.3716 -0.2727 -0.0038 0.0077  143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.7591 0.4543 0.2896 -0.2531 -0.0604 0.0474  143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.7506 0.4397 0.3029 -0.2328 -0.0928 0.0719  143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.7514 0.4274 0.3046 -0.2159 -0.0946 0.0655  143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.7564 0.4226 0.3378 -0.2062 -0.1026 0.0760  143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.8506 0.5970 0.3367 -0.3288 0.0016  0.0037  144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.8867 0.6379 0.3681 -0.3490 0.0418  -0.0333 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.9160 0.6939 0.3893 -0.3788 0.0570  -0.0403 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.9179 0.7103 0.3843 -0.4051 0.0921  -0.0744 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.9148 0.6892 0.3693 -0.3762 0.0554  -0.0517 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.9783 0.7239 0.4455 -0.3491 0.0547  -0.0571 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.9956 0.7036 0.4936 -0.3124 0.0545  -0.0561 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 1.0077 0.7715 0.4538 -0.3661 0.0535  -0.0608 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.9355 0.7218 0.4126 -0.3768 0.0331  -0.0107 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.9571 0.7719 0.4260 -0.4062 0.0467  -0.0145 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.9687 0.7648 0.4668 -0.3825 0.0295  0.0083  145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.9744 0.7953 0.4679 -0.4048 0.0344  0.0134  145 GLU   A O   
1073 C CB  . GLU   A 139 ? 0.9962 0.8701 0.4237 -0.4533 0.0363  0.0011  145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.0705 0.9566 0.4983 -0.4469 -0.0094 0.0495  145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.1624 1.1092 0.5531 -0.4934 -0.0226 0.0698  145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.1601 1.1315 0.5583 -0.5002 -0.0570 0.1155  145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.1991 1.1714 0.5572 -0.5244 0.0011  0.0411  145 GLU   A OE2 
1078 N N1  . A1BOC B .   ? 0.6090 0.3234 0.4527 0.0101  -0.0748 -0.2198 201 A1BOC A N1  
1079 N N3  . A1BOC B .   ? 0.5859 0.2084 0.5889 -0.0107 -0.1850 -0.0429 201 A1BOC A N3  
1080 C C4  . A1BOC B .   ? 0.5963 0.2817 0.4642 0.0105  -0.1035 -0.1943 201 A1BOC A C4  
1081 C C5  . A1BOC B .   ? 0.5786 0.2450 0.5091 0.0111  -0.1161 -0.1736 201 A1BOC A C5  
1082 C C6  . A1BOC B .   ? 0.5726 0.2380 0.5526 0.0116  -0.1284 -0.2006 201 A1BOC A C6  
1083 C C7  . A1BOC B .   ? 0.5880 0.2400 0.5534 0.0102  -0.1445 -0.1748 201 A1BOC A C7  
1084 C C8  . A1BOC B .   ? 0.5805 0.2164 0.5950 0.0079  -0.1606 -0.1398 201 A1BOC A C8  
1085 C C10 . A1BOC B .   ? 0.5776 0.2039 0.6267 -0.0019 -0.1777 -0.0761 201 A1BOC A C10 
1086 C C13 . A1BOC B .   ? 0.5860 0.3399 0.4827 0.0063  -0.0456 -0.2936 201 A1BOC A C13 
1087 C C15 . A1BOC B .   ? 0.6138 0.3598 0.4111 0.0079  -0.0469 -0.2322 201 A1BOC A C15 
1088 O O1  . A1BOC B .   ? 0.5495 0.1768 0.6810 -0.0009 -0.1841 -0.0770 201 A1BOC A O1  
1089 C C9  . A1BOC B .   ? 0.5847 0.2180 0.5838 0.0046  -0.1599 -0.1129 201 A1BOC A C9  
1090 C C11 . A1BOC B .   ? 0.5675 0.2110 0.5939 0.0086  -0.1455 -0.1398 201 A1BOC A C11 
1091 N N2  . A1BOC B .   ? 0.5728 0.2307 0.5481 0.0111  -0.1288 -0.1725 201 A1BOC A N2  
1092 O O   . A1BOC B .   ? 0.5626 0.2243 0.5031 0.0103  -0.1160 -0.1557 201 A1BOC A O   
1093 C C3  . A1BOC B .   ? 0.6130 0.3096 0.4383 0.0101  -0.0901 -0.1913 201 A1BOC A C3  
1094 C C1  . A1BOC B .   ? 0.6276 0.3212 0.3967 0.0090  -0.0881 -0.1641 201 A1BOC A C1  
1095 C C   . A1BOC B .   ? 0.6394 0.3177 0.3718 0.0072  -0.0967 -0.1319 201 A1BOC A C   
1096 C C12 . A1BOC B .   ? 0.5886 0.3116 0.5013 0.0103  -0.0674 -0.2581 201 A1BOC A C12 
1097 C C14 . A1BOC B .   ? 0.5927 0.3476 0.4585 0.0077  -0.0380 -0.2729 201 A1BOC A C14 
1098 C C2  . A1BOC B .   ? 0.6215 0.3438 0.4170 0.0093  -0.0656 -0.2065 201 A1BOC A C2  
1099 N N   . A1BOC B .   ? 0.6317 0.3409 0.3850 0.0090  -0.0735 -0.1731 201 A1BOC A N   
# 
