data_7I5G
# 
_entry.id   7I5G 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   7I5G         pdb_00007i5g 10.2210/pdb7i5g/pdb 
WWPDB D_1001408339 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I5G 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                                          15892.732 
1   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-1-[(2S)-1-acetyl-2,3-dihydro-1H-indole-2-carbonyl]piperidine-3-carboxamide (non-preferred name)' 315.367   
1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                                             65.409    
1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                                   78.133    
2   ?         ? ? ? 
5 water       nat water                                                                                                  18.015    
182 ?         ? ? ? 
# 
_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-[(2S)-1-acetyl-2,3-dihydro-1H-indole-2-carbonyl]piperidine-3-carboxamide (non-preferred name)' A1B3X 
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 
A1B3X non-polymer         . '(3S)-1-[(2S)-1-acetyl-2,3-dihydro-1H-indole-2-carbonyl]piperidine-3-carboxamide (non-preferred name)' 
? 'C17 H21 N3 O3'  315.367 
ALA   'L-peptide linking' y ALANINE                                                                                                
? 'C3 H7 N O2'     89.093  
ARG   'L-peptide linking' y ARGININE                                                                                               
? 'C6 H15 N4 O2 1' 175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                                             
? 'C4 H8 N2 O3'    132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                                        
? 'C4 H7 N O4'     133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                                               
? 'C3 H7 N O2 S'   121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                                                   
? 'C2 H6 O S'      78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                                              
? 'C5 H10 N2 O3'   146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                                        
? 'C5 H9 N O4'     147.129 
GLY   'peptide linking'   y GLYCINE                                                                                                
? 'C2 H5 N O2'     75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                                              
? 'C6 H10 N3 O2 1' 156.162 
HOH   non-polymer         . WATER                                                                                                  
? 'H2 O'           18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                                             
? 'C6 H13 N O2'    131.173 
LEU   'L-peptide linking' y LEUCINE                                                                                                
? 'C6 H13 N O2'    131.173 
LYS   'L-peptide linking' y LYSINE                                                                                                 
? 'C6 H15 N2 O2 1' 147.195 
MET   'L-peptide linking' y METHIONINE                                                                                             
? 'C5 H11 N O2 S'  149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                                          
? 'C9 H11 N O2'    165.189 
PRO   'L-peptide linking' y PROLINE                                                                                                
? 'C5 H9 N O2'     115.130 
SER   'L-peptide linking' y SERINE                                                                                                 
? 'C3 H7 N O3'     105.093 
THR   'L-peptide linking' y THREONINE                                                                                              
? 'C4 H9 N O3'     119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                                             
? 'C11 H12 N2 O2'  204.225 
TYR   'L-peptide linking' y TYROSINE                                                                                               
? 'C9 H11 N O3'    181.189 
VAL   'L-peptide linking' y VALINE                                                                                                 
? 'C5 H11 N O2'    117.146 
ZN    non-polymer         . 'ZINC ION'                                                                                             
? 'Zn 2'           65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B3X 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3X 
_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 A1B3X 1   201 201 A1B3X LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 0   DMS   DMS A . 
E 4 DMS   1   204 1   DMS   DMS A . 
F 5 HOH   1   301 203 HOH   HOH A . 
F 5 HOH   2   302 229 HOH   HOH A . 
F 5 HOH   3   303 59  HOH   HOH A . 
F 5 HOH   4   304 281 HOH   HOH A . 
F 5 HOH   5   305 283 HOH   HOH A . 
F 5 HOH   6   306 191 HOH   HOH A . 
F 5 HOH   7   307 42  HOH   HOH A . 
F 5 HOH   8   308 34  HOH   HOH A . 
F 5 HOH   9   309 257 HOH   HOH A . 
F 5 HOH   10  310 36  HOH   HOH A . 
F 5 HOH   11  311 234 HOH   HOH A . 
F 5 HOH   12  312 30  HOH   HOH A . 
F 5 HOH   13  313 268 HOH   HOH A . 
F 5 HOH   14  314 4   HOH   HOH A . 
F 5 HOH   15  315 210 HOH   HOH A . 
F 5 HOH   16  316 13  HOH   HOH A . 
F 5 HOH   17  317 284 HOH   HOH A . 
F 5 HOH   18  318 35  HOH   HOH A . 
F 5 HOH   19  319 252 HOH   HOH A . 
F 5 HOH   20  320 260 HOH   HOH A . 
F 5 HOH   21  321 111 HOH   HOH A . 
F 5 HOH   22  322 68  HOH   HOH A . 
F 5 HOH   23  323 147 HOH   HOH A . 
F 5 HOH   24  324 43  HOH   HOH A . 
F 5 HOH   25  325 104 HOH   HOH A . 
F 5 HOH   26  326 263 HOH   HOH A . 
F 5 HOH   27  327 119 HOH   HOH A . 
F 5 HOH   28  328 25  HOH   HOH A . 
F 5 HOH   29  329 57  HOH   HOH A . 
F 5 HOH   30  330 24  HOH   HOH A . 
F 5 HOH   31  331 33  HOH   HOH A . 
F 5 HOH   32  332 26  HOH   HOH A . 
F 5 HOH   33  333 121 HOH   HOH A . 
F 5 HOH   34  334 186 HOH   HOH A . 
F 5 HOH   35  335 251 HOH   HOH A . 
F 5 HOH   36  336 219 HOH   HOH A . 
F 5 HOH   37  337 205 HOH   HOH A . 
F 5 HOH   38  338 211 HOH   HOH A . 
F 5 HOH   39  339 272 HOH   HOH A . 
F 5 HOH   40  340 20  HOH   HOH A . 
F 5 HOH   41  341 21  HOH   HOH A . 
F 5 HOH   42  342 2   HOH   HOH A . 
F 5 HOH   43  343 77  HOH   HOH A . 
F 5 HOH   44  344 107 HOH   HOH A . 
F 5 HOH   45  345 154 HOH   HOH A . 
F 5 HOH   46  346 85  HOH   HOH A . 
F 5 HOH   47  347 144 HOH   HOH A . 
F 5 HOH   48  348 266 HOH   HOH A . 
F 5 HOH   49  349 236 HOH   HOH A . 
F 5 HOH   50  350 16  HOH   HOH A . 
F 5 HOH   51  351 124 HOH   HOH A . 
F 5 HOH   52  352 261 HOH   HOH A . 
F 5 HOH   53  353 159 HOH   HOH A . 
F 5 HOH   54  354 49  HOH   HOH A . 
F 5 HOH   55  355 28  HOH   HOH A . 
F 5 HOH   56  356 9   HOH   HOH A . 
F 5 HOH   57  357 212 HOH   HOH A . 
F 5 HOH   58  358 174 HOH   HOH A . 
F 5 HOH   59  359 171 HOH   HOH A . 
F 5 HOH   60  360 169 HOH   HOH A . 
F 5 HOH   61  361 7   HOH   HOH A . 
F 5 HOH   62  362 259 HOH   HOH A . 
F 5 HOH   63  363 98  HOH   HOH A . 
F 5 HOH   64  364 91  HOH   HOH A . 
F 5 HOH   65  365 131 HOH   HOH A . 
F 5 HOH   66  366 95  HOH   HOH A . 
F 5 HOH   67  367 282 HOH   HOH A . 
F 5 HOH   68  368 29  HOH   HOH A . 
F 5 HOH   69  369 258 HOH   HOH A . 
F 5 HOH   70  370 12  HOH   HOH A . 
F 5 HOH   71  371 37  HOH   HOH A . 
F 5 HOH   72  372 105 HOH   HOH A . 
F 5 HOH   73  373 90  HOH   HOH A . 
F 5 HOH   74  374 161 HOH   HOH A . 
F 5 HOH   75  375 62  HOH   HOH A . 
F 5 HOH   76  376 182 HOH   HOH A . 
F 5 HOH   77  377 279 HOH   HOH A . 
F 5 HOH   78  378 271 HOH   HOH A . 
F 5 HOH   79  379 96  HOH   HOH A . 
F 5 HOH   80  380 50  HOH   HOH A . 
F 5 HOH   81  381 69  HOH   HOH A . 
F 5 HOH   82  382 8   HOH   HOH A . 
F 5 HOH   83  383 100 HOH   HOH A . 
F 5 HOH   84  384 51  HOH   HOH A . 
F 5 HOH   85  385 278 HOH   HOH A . 
F 5 HOH   86  386 214 HOH   HOH A . 
F 5 HOH   87  387 84  HOH   HOH A . 
F 5 HOH   88  388 11  HOH   HOH A . 
F 5 HOH   89  389 39  HOH   HOH A . 
F 5 HOH   90  390 114 HOH   HOH A . 
F 5 HOH   91  391 135 HOH   HOH A . 
F 5 HOH   92  392 116 HOH   HOH A . 
F 5 HOH   93  393 48  HOH   HOH A . 
F 5 HOH   94  394 47  HOH   HOH A . 
F 5 HOH   95  395 75  HOH   HOH A . 
F 5 HOH   96  396 262 HOH   HOH A . 
F 5 HOH   97  397 220 HOH   HOH A . 
F 5 HOH   98  398 215 HOH   HOH A . 
F 5 HOH   99  399 156 HOH   HOH A . 
F 5 HOH   100 400 177 HOH   HOH A . 
F 5 HOH   101 401 93  HOH   HOH A . 
F 5 HOH   102 402 253 HOH   HOH A . 
F 5 HOH   103 403 15  HOH   HOH A . 
F 5 HOH   104 404 276 HOH   HOH A . 
F 5 HOH   105 405 168 HOH   HOH A . 
F 5 HOH   106 406 224 HOH   HOH A . 
F 5 HOH   107 407 89  HOH   HOH A . 
F 5 HOH   108 408 256 HOH   HOH A . 
F 5 HOH   109 409 80  HOH   HOH A . 
F 5 HOH   110 410 132 HOH   HOH A . 
F 5 HOH   111 411 197 HOH   HOH A . 
F 5 HOH   112 412 70  HOH   HOH A . 
F 5 HOH   113 413 280 HOH   HOH A . 
F 5 HOH   114 414 83  HOH   HOH A . 
F 5 HOH   115 415 123 HOH   HOH A . 
F 5 HOH   116 416 40  HOH   HOH A . 
F 5 HOH   117 417 185 HOH   HOH A . 
F 5 HOH   118 418 126 HOH   HOH A . 
F 5 HOH   119 419 10  HOH   HOH A . 
F 5 HOH   120 420 79  HOH   HOH A . 
F 5 HOH   121 421 38  HOH   HOH A . 
F 5 HOH   122 422 23  HOH   HOH A . 
F 5 HOH   123 423 254 HOH   HOH A . 
F 5 HOH   124 424 201 HOH   HOH A . 
F 5 HOH   125 425 76  HOH   HOH A . 
F 5 HOH   126 426 255 HOH   HOH A . 
F 5 HOH   127 427 248 HOH   HOH A . 
F 5 HOH   128 428 120 HOH   HOH A . 
F 5 HOH   129 429 152 HOH   HOH A . 
F 5 HOH   130 430 5   HOH   HOH A . 
F 5 HOH   131 431 102 HOH   HOH A . 
F 5 HOH   132 432 155 HOH   HOH A . 
F 5 HOH   133 433 112 HOH   HOH A . 
F 5 HOH   134 434 277 HOH   HOH A . 
F 5 HOH   135 435 128 HOH   HOH A . 
F 5 HOH   136 436 213 HOH   HOH A . 
F 5 HOH   137 437 140 HOH   HOH A . 
F 5 HOH   138 438 175 HOH   HOH A . 
F 5 HOH   139 439 207 HOH   HOH A . 
F 5 HOH   140 440 290 HOH   HOH A . 
F 5 HOH   141 441 239 HOH   HOH A . 
F 5 HOH   142 442 94  HOH   HOH A . 
F 5 HOH   143 443 133 HOH   HOH A . 
F 5 HOH   144 444 233 HOH   HOH A . 
F 5 HOH   145 445 228 HOH   HOH A . 
F 5 HOH   146 446 232 HOH   HOH A . 
F 5 HOH   147 447 291 HOH   HOH A . 
F 5 HOH   148 448 274 HOH   HOH A . 
F 5 HOH   149 449 289 HOH   HOH A . 
F 5 HOH   150 450 74  HOH   HOH A . 
F 5 HOH   151 451 65  HOH   HOH A . 
F 5 HOH   152 452 127 HOH   HOH A . 
F 5 HOH   153 453 117 HOH   HOH A . 
F 5 HOH   154 454 141 HOH   HOH A . 
F 5 HOH   155 455 285 HOH   HOH A . 
F 5 HOH   156 456 158 HOH   HOH A . 
F 5 HOH   157 457 240 HOH   HOH A . 
F 5 HOH   158 458 108 HOH   HOH A . 
F 5 HOH   159 459 275 HOH   HOH A . 
F 5 HOH   160 460 129 HOH   HOH A . 
F 5 HOH   161 461 216 HOH   HOH A . 
F 5 HOH   162 462 99  HOH   HOH A . 
F 5 HOH   163 463 273 HOH   HOH A . 
F 5 HOH   164 464 187 HOH   HOH A . 
F 5 HOH   165 465 86  HOH   HOH A . 
F 5 HOH   166 466 73  HOH   HOH A . 
F 5 HOH   167 467 221 HOH   HOH A . 
F 5 HOH   168 468 288 HOH   HOH A . 
F 5 HOH   169 469 153 HOH   HOH A . 
F 5 HOH   170 470 56  HOH   HOH A . 
F 5 HOH   171 471 165 HOH   HOH A . 
F 5 HOH   172 472 286 HOH   HOH A . 
F 5 HOH   173 473 125 HOH   HOH A . 
F 5 HOH   174 474 122 HOH   HOH A . 
F 5 HOH   175 475 61  HOH   HOH A . 
F 5 HOH   176 476 222 HOH   HOH A . 
F 5 HOH   177 477 208 HOH   HOH A . 
F 5 HOH   178 478 287 HOH   HOH A . 
F 5 HOH   179 479 209 HOH   HOH A . 
F 5 HOH   180 480 292 HOH   HOH A . 
F 5 HOH   181 481 92  HOH   HOH A . 
F 5 HOH   182 482 241 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           7I5G 
_cell.length_a           89.048 
_cell.length_b           58.247 
_cell.length_c           32.694 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.63 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I5G 
_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          7I5G 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.66 
_exptl_crystal.density_percent_sol   53.84 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-22 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92204 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I5G 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             44.48 
_reflns.d_resolution_high            1.58 
_reflns.number_obs                   22498 
_reflns.percent_possible_obs         97.5 
_reflns.pdbx_Rmerge_I_obs            0.073 
_reflns.pdbx_netI_over_sigmaI        10.2 
_reflns.pdbx_redundancy              7.1 
_reflns.pdbx_Rrim_I_all              0.079 
_reflns.pdbx_Rpim_I_all              0.030 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     158987 
_reflns.pdbx_chi_squared             0.77 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.number_all                   ? 
_reflns.pdbx_Rsym_value              ? 
_reflns.B_iso_Wilson_estimate        ? 
# 
_reflns_shell.pdbx_diffrn_id              1 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.d_res_high                  1.58 
_reflns_shell.d_res_low                   1.66 
_reflns_shell.number_measured_all         21789 
_reflns_shell.number_unique_obs           3228 
_reflns_shell.Rmerge_I_obs                1.721 
_reflns_shell.pdbx_chi_squared            0.59 
_reflns_shell.pdbx_redundancy             6.8 
_reflns_shell.percent_possible_obs        96.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.866 
_reflns_shell.pdbx_Rpim_I_all             0.712 
_reflns_shell.pdbx_CC_half                0.484 
_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                                 7I5G 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     22460 
_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                             44.48 
_refine.ls_d_res_high                            1.576 
_refine.ls_percent_reflns_obs                    97.1 
_refine.ls_R_factor_obs                          0.1873 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1855 
_refine.ls_R_factor_R_free                       0.2193 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.120 
_refine.ls_number_reflns_R_free                  1150 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.954 
_refine.B_iso_mean                               33.92 
_refine.aniso_B[1][1]                            -2.20630 
_refine.aniso_B[2][2]                            0.96490 
_refine.aniso_B[3][3]                            1.24140 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.82490 
_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             0.081 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.084 
_refine.pdbx_overall_SU_R_Blow_DPI               0.087 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.088 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I5G 
_refine_analyze.Luzzati_coordinate_error_obs    0.21 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1083 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         32 
_refine_hist.number_atoms_solvent             182 
_refine_hist.number_atoms_total               1297 
_refine_hist.d_res_high                       1.576 
_refine_hist.d_res_low                        44.48 
# 
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  1151 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.96  ? 2.00  1568 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  389  '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  209  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1151 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.10  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.21 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  141  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  1038 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.58 
_refine_ls_shell.d_res_low                        1.59 
_refine_ls_shell.number_reflns_R_work             427 
_refine_ls_shell.R_factor_R_work                  0.3305 
_refine_ls_shell.percent_reflns_obs               89.25 
_refine_ls_shell.R_factor_R_free                  0.3513 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.11 
_refine_ls_shell.number_reflns_R_free             23 
_refine_ls_shell.number_reflns_all                450 
_refine_ls_shell.R_factor_all                     0.3316 
# 
_struct.entry_id                  7I5G 
_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-0036322-001 (A71EV2A-x4836)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I5G 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I5G 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.347 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.120 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.0 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 108.2 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 115.6 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 109.4 ? 
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 99.9  ? 
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_555 113.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N GLY A 43  ? N GLY A 49  O GLY A 7   ? O GLY A 13  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I5G 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_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         15.1801 
_pdbx_refine_tls.origin_y         7.6588 
_pdbx_refine_tls.origin_z         14.0096 
_pdbx_refine_tls.T[1][1]          -0.0220 
_pdbx_refine_tls.T[2][2]          -0.0184 
_pdbx_refine_tls.T[3][3]          -0.0259 
_pdbx_refine_tls.T[1][2]          -0.0166 
_pdbx_refine_tls.T[1][3]          -0.0036 
_pdbx_refine_tls.T[2][3]          -0.0015 
_pdbx_refine_tls.L[1][1]          0.8434 
_pdbx_refine_tls.L[2][2]          2.7167 
_pdbx_refine_tls.L[3][3]          0.4931 
_pdbx_refine_tls.L[1][2]          0.2901 
_pdbx_refine_tls.L[1][3]          -0.1703 
_pdbx_refine_tls.L[2][3]          -0.0268 
_pdbx_refine_tls.S[1][1]          -0.0182 
_pdbx_refine_tls.S[1][2]          0.0187 
_pdbx_refine_tls.S[1][3]          0.0601 
_pdbx_refine_tls.S[2][1]          0.0122 
_pdbx_refine_tls.S[2][2]          0.0378 
_pdbx_refine_tls.S[2][3]          -0.1621 
_pdbx_refine_tls.S[3][1]          -0.0700 
_pdbx_refine_tls.S[3][2]          0.0051 
_pdbx_refine_tls.S[3][3]          -0.0196 
# 
_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 ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B3X N1   N  N N 1   
A1B3X C4   C  Y N 2   
A1B3X C5   C  Y N 3   
A1B3X C6   C  Y N 4   
A1B3X C7   C  Y N 5   
A1B3X C8   C  N N 6   
A1B3X C10  C  N N 7   
A1B3X C13  C  N N 8   
A1B3X C15  C  N N 9   
A1B3X O2   O  N N 10  
A1B3X N2   N  N N 11  
A1B3X C14  C  N S 12  
A1B3X C12  C  N N 13  
A1B3X C11  C  N N 14  
A1B3X C16  C  N N 15  
A1B3X O1   O  N N 16  
A1B3X C9   C  N R 17  
A1B3X N    N  N N 18  
A1B3X C1   C  N N 19  
A1B3X O    O  N N 20  
A1B3X C    C  N N 21  
A1B3X C2   C  Y N 22  
A1B3X C3   C  Y N 23  
A1B3X H6   H  N N 24  
A1B3X H7   H  N N 25  
A1B3X H8   H  N N 26  
A1B3X H10  H  N N 27  
A1B3X H9   H  N N 28  
A1B3X H15  H  N N 29  
A1B3X H16  H  N N 30  
A1B3X H18  H  N N 31  
A1B3X H17  H  N N 32  
A1B3X H1   H  N N 33  
A1B3X H13  H  N N 34  
A1B3X H14  H  N N 35  
A1B3X H12  H  N N 36  
A1B3X H11  H  N N 37  
A1B3X H19  H  N N 38  
A1B3X H20  H  N N 39  
A1B3X H    H  N N 40  
A1B3X H3   H  N N 41  
A1B3X H2   H  N N 42  
A1B3X H4   H  N N 43  
A1B3X H5   H  N N 44  
ALA   N    N  N N 45  
ALA   CA   C  N S 46  
ALA   C    C  N N 47  
ALA   O    O  N N 48  
ALA   CB   C  N N 49  
ALA   OXT  O  N N 50  
ALA   H    H  N N 51  
ALA   H2   H  N N 52  
ALA   HA   H  N N 53  
ALA   HB1  H  N N 54  
ALA   HB2  H  N N 55  
ALA   HB3  H  N N 56  
ALA   HXT  H  N N 57  
ARG   N    N  N N 58  
ARG   CA   C  N S 59  
ARG   C    C  N N 60  
ARG   O    O  N N 61  
ARG   CB   C  N N 62  
ARG   CG   C  N N 63  
ARG   CD   C  N N 64  
ARG   NE   N  N N 65  
ARG   CZ   C  N N 66  
ARG   NH1  N  N N 67  
ARG   NH2  N  N N 68  
ARG   OXT  O  N N 69  
ARG   H    H  N N 70  
ARG   H2   H  N N 71  
ARG   HA   H  N N 72  
ARG   HB2  H  N N 73  
ARG   HB3  H  N N 74  
ARG   HG2  H  N N 75  
ARG   HG3  H  N N 76  
ARG   HD2  H  N N 77  
ARG   HD3  H  N N 78  
ARG   HE   H  N N 79  
ARG   HH11 H  N N 80  
ARG   HH12 H  N N 81  
ARG   HH21 H  N N 82  
ARG   HH22 H  N N 83  
ARG   HXT  H  N N 84  
ASN   N    N  N N 85  
ASN   CA   C  N S 86  
ASN   C    C  N N 87  
ASN   O    O  N N 88  
ASN   CB   C  N N 89  
ASN   CG   C  N N 90  
ASN   OD1  O  N N 91  
ASN   ND2  N  N N 92  
ASN   OXT  O  N N 93  
ASN   H    H  N N 94  
ASN   H2   H  N N 95  
ASN   HA   H  N N 96  
ASN   HB2  H  N N 97  
ASN   HB3  H  N N 98  
ASN   HD21 H  N N 99  
ASN   HD22 H  N N 100 
ASN   HXT  H  N N 101 
ASP   N    N  N N 102 
ASP   CA   C  N S 103 
ASP   C    C  N N 104 
ASP   O    O  N N 105 
ASP   CB   C  N N 106 
ASP   CG   C  N N 107 
ASP   OD1  O  N N 108 
ASP   OD2  O  N N 109 
ASP   OXT  O  N N 110 
ASP   H    H  N N 111 
ASP   H2   H  N N 112 
ASP   HA   H  N N 113 
ASP   HB2  H  N N 114 
ASP   HB3  H  N N 115 
ASP   HD2  H  N N 116 
ASP   HXT  H  N N 117 
CYS   N    N  N N 118 
CYS   CA   C  N R 119 
CYS   C    C  N N 120 
CYS   O    O  N N 121 
CYS   CB   C  N N 122 
CYS   SG   S  N N 123 
CYS   OXT  O  N N 124 
CYS   H    H  N N 125 
CYS   H2   H  N N 126 
CYS   HA   H  N N 127 
CYS   HB2  H  N N 128 
CYS   HB3  H  N N 129 
CYS   HG   H  N N 130 
CYS   HXT  H  N N 131 
DMS   S    S  N N 132 
DMS   O    O  N N 133 
DMS   C1   C  N N 134 
DMS   C2   C  N N 135 
DMS   H11  H  N N 136 
DMS   H12  H  N N 137 
DMS   H13  H  N N 138 
DMS   H21  H  N N 139 
DMS   H22  H  N N 140 
DMS   H23  H  N N 141 
GLN   N    N  N N 142 
GLN   CA   C  N S 143 
GLN   C    C  N N 144 
GLN   O    O  N N 145 
GLN   CB   C  N N 146 
GLN   CG   C  N N 147 
GLN   CD   C  N N 148 
GLN   OE1  O  N N 149 
GLN   NE2  N  N N 150 
GLN   OXT  O  N N 151 
GLN   H    H  N N 152 
GLN   H2   H  N N 153 
GLN   HA   H  N N 154 
GLN   HB2  H  N N 155 
GLN   HB3  H  N N 156 
GLN   HG2  H  N N 157 
GLN   HG3  H  N N 158 
GLN   HE21 H  N N 159 
GLN   HE22 H  N N 160 
GLN   HXT  H  N N 161 
GLU   N    N  N N 162 
GLU   CA   C  N S 163 
GLU   C    C  N N 164 
GLU   O    O  N N 165 
GLU   CB   C  N N 166 
GLU   CG   C  N N 167 
GLU   CD   C  N N 168 
GLU   OE1  O  N N 169 
GLU   OE2  O  N N 170 
GLU   OXT  O  N N 171 
GLU   H    H  N N 172 
GLU   H2   H  N N 173 
GLU   HA   H  N N 174 
GLU   HB2  H  N N 175 
GLU   HB3  H  N N 176 
GLU   HG2  H  N N 177 
GLU   HG3  H  N N 178 
GLU   HE2  H  N N 179 
GLU   HXT  H  N N 180 
GLY   N    N  N N 181 
GLY   CA   C  N N 182 
GLY   C    C  N N 183 
GLY   O    O  N N 184 
GLY   OXT  O  N N 185 
GLY   H    H  N N 186 
GLY   H2   H  N N 187 
GLY   HA2  H  N N 188 
GLY   HA3  H  N N 189 
GLY   HXT  H  N N 190 
HIS   N    N  N N 191 
HIS   CA   C  N S 192 
HIS   C    C  N N 193 
HIS   O    O  N N 194 
HIS   CB   C  N N 195 
HIS   CG   C  Y N 196 
HIS   ND1  N  Y N 197 
HIS   CD2  C  Y N 198 
HIS   CE1  C  Y N 199 
HIS   NE2  N  Y N 200 
HIS   OXT  O  N N 201 
HIS   H    H  N N 202 
HIS   H2   H  N N 203 
HIS   HA   H  N N 204 
HIS   HB2  H  N N 205 
HIS   HB3  H  N N 206 
HIS   HD1  H  N N 207 
HIS   HD2  H  N N 208 
HIS   HE1  H  N N 209 
HIS   HE2  H  N N 210 
HIS   HXT  H  N N 211 
HOH   O    O  N N 212 
HOH   H1   H  N N 213 
HOH   H2   H  N N 214 
ILE   N    N  N N 215 
ILE   CA   C  N S 216 
ILE   C    C  N N 217 
ILE   O    O  N N 218 
ILE   CB   C  N S 219 
ILE   CG1  C  N N 220 
ILE   CG2  C  N N 221 
ILE   CD1  C  N N 222 
ILE   OXT  O  N N 223 
ILE   H    H  N N 224 
ILE   H2   H  N N 225 
ILE   HA   H  N N 226 
ILE   HB   H  N N 227 
ILE   HG12 H  N N 228 
ILE   HG13 H  N N 229 
ILE   HG21 H  N N 230 
ILE   HG22 H  N N 231 
ILE   HG23 H  N N 232 
ILE   HD11 H  N N 233 
ILE   HD12 H  N N 234 
ILE   HD13 H  N N 235 
ILE   HXT  H  N N 236 
LEU   N    N  N N 237 
LEU   CA   C  N S 238 
LEU   C    C  N N 239 
LEU   O    O  N N 240 
LEU   CB   C  N N 241 
LEU   CG   C  N N 242 
LEU   CD1  C  N N 243 
LEU   CD2  C  N N 244 
LEU   OXT  O  N N 245 
LEU   H    H  N N 246 
LEU   H2   H  N N 247 
LEU   HA   H  N N 248 
LEU   HB2  H  N N 249 
LEU   HB3  H  N N 250 
LEU   HG   H  N N 251 
LEU   HD11 H  N N 252 
LEU   HD12 H  N N 253 
LEU   HD13 H  N N 254 
LEU   HD21 H  N N 255 
LEU   HD22 H  N N 256 
LEU   HD23 H  N N 257 
LEU   HXT  H  N N 258 
LYS   N    N  N N 259 
LYS   CA   C  N S 260 
LYS   C    C  N N 261 
LYS   O    O  N N 262 
LYS   CB   C  N N 263 
LYS   CG   C  N N 264 
LYS   CD   C  N N 265 
LYS   CE   C  N N 266 
LYS   NZ   N  N N 267 
LYS   OXT  O  N N 268 
LYS   H    H  N N 269 
LYS   H2   H  N N 270 
LYS   HA   H  N N 271 
LYS   HB2  H  N N 272 
LYS   HB3  H  N N 273 
LYS   HG2  H  N N 274 
LYS   HG3  H  N N 275 
LYS   HD2  H  N N 276 
LYS   HD3  H  N N 277 
LYS   HE2  H  N N 278 
LYS   HE3  H  N N 279 
LYS   HZ1  H  N N 280 
LYS   HZ2  H  N N 281 
LYS   HZ3  H  N N 282 
LYS   HXT  H  N N 283 
MET   N    N  N N 284 
MET   CA   C  N S 285 
MET   C    C  N N 286 
MET   O    O  N N 287 
MET   CB   C  N N 288 
MET   CG   C  N N 289 
MET   SD   S  N N 290 
MET   CE   C  N N 291 
MET   OXT  O  N N 292 
MET   H    H  N N 293 
MET   H2   H  N N 294 
MET   HA   H  N N 295 
MET   HB2  H  N N 296 
MET   HB3  H  N N 297 
MET   HG2  H  N N 298 
MET   HG3  H  N N 299 
MET   HE1  H  N N 300 
MET   HE2  H  N N 301 
MET   HE3  H  N N 302 
MET   HXT  H  N N 303 
PHE   N    N  N N 304 
PHE   CA   C  N S 305 
PHE   C    C  N N 306 
PHE   O    O  N N 307 
PHE   CB   C  N N 308 
PHE   CG   C  Y N 309 
PHE   CD1  C  Y N 310 
PHE   CD2  C  Y N 311 
PHE   CE1  C  Y N 312 
PHE   CE2  C  Y N 313 
PHE   CZ   C  Y N 314 
PHE   OXT  O  N N 315 
PHE   H    H  N N 316 
PHE   H2   H  N N 317 
PHE   HA   H  N N 318 
PHE   HB2  H  N N 319 
PHE   HB3  H  N N 320 
PHE   HD1  H  N N 321 
PHE   HD2  H  N N 322 
PHE   HE1  H  N N 323 
PHE   HE2  H  N N 324 
PHE   HZ   H  N N 325 
PHE   HXT  H  N N 326 
PRO   N    N  N N 327 
PRO   CA   C  N S 328 
PRO   C    C  N N 329 
PRO   O    O  N N 330 
PRO   CB   C  N N 331 
PRO   CG   C  N N 332 
PRO   CD   C  N N 333 
PRO   OXT  O  N N 334 
PRO   H    H  N N 335 
PRO   HA   H  N N 336 
PRO   HB2  H  N N 337 
PRO   HB3  H  N N 338 
PRO   HG2  H  N N 339 
PRO   HG3  H  N N 340 
PRO   HD2  H  N N 341 
PRO   HD3  H  N N 342 
PRO   HXT  H  N N 343 
SER   N    N  N N 344 
SER   CA   C  N S 345 
SER   C    C  N N 346 
SER   O    O  N N 347 
SER   CB   C  N N 348 
SER   OG   O  N N 349 
SER   OXT  O  N N 350 
SER   H    H  N N 351 
SER   H2   H  N N 352 
SER   HA   H  N N 353 
SER   HB2  H  N N 354 
SER   HB3  H  N N 355 
SER   HG   H  N N 356 
SER   HXT  H  N N 357 
THR   N    N  N N 358 
THR   CA   C  N S 359 
THR   C    C  N N 360 
THR   O    O  N N 361 
THR   CB   C  N R 362 
THR   OG1  O  N N 363 
THR   CG2  C  N N 364 
THR   OXT  O  N N 365 
THR   H    H  N N 366 
THR   H2   H  N N 367 
THR   HA   H  N N 368 
THR   HB   H  N N 369 
THR   HG1  H  N N 370 
THR   HG21 H  N N 371 
THR   HG22 H  N N 372 
THR   HG23 H  N N 373 
THR   HXT  H  N N 374 
TRP   N    N  N N 375 
TRP   CA   C  N S 376 
TRP   C    C  N N 377 
TRP   O    O  N N 378 
TRP   CB   C  N N 379 
TRP   CG   C  Y N 380 
TRP   CD1  C  Y N 381 
TRP   CD2  C  Y N 382 
TRP   NE1  N  Y N 383 
TRP   CE2  C  Y N 384 
TRP   CE3  C  Y N 385 
TRP   CZ2  C  Y N 386 
TRP   CZ3  C  Y N 387 
TRP   CH2  C  Y N 388 
TRP   OXT  O  N N 389 
TRP   H    H  N N 390 
TRP   H2   H  N N 391 
TRP   HA   H  N N 392 
TRP   HB2  H  N N 393 
TRP   HB3  H  N N 394 
TRP   HD1  H  N N 395 
TRP   HE1  H  N N 396 
TRP   HE3  H  N N 397 
TRP   HZ2  H  N N 398 
TRP   HZ3  H  N N 399 
TRP   HH2  H  N N 400 
TRP   HXT  H  N N 401 
TYR   N    N  N N 402 
TYR   CA   C  N S 403 
TYR   C    C  N N 404 
TYR   O    O  N N 405 
TYR   CB   C  N N 406 
TYR   CG   C  Y N 407 
TYR   CD1  C  Y N 408 
TYR   CD2  C  Y N 409 
TYR   CE1  C  Y N 410 
TYR   CE2  C  Y N 411 
TYR   CZ   C  Y N 412 
TYR   OH   O  N N 413 
TYR   OXT  O  N N 414 
TYR   H    H  N N 415 
TYR   H2   H  N N 416 
TYR   HA   H  N N 417 
TYR   HB2  H  N N 418 
TYR   HB3  H  N N 419 
TYR   HD1  H  N N 420 
TYR   HD2  H  N N 421 
TYR   HE1  H  N N 422 
TYR   HE2  H  N N 423 
TYR   HH   H  N N 424 
TYR   HXT  H  N N 425 
VAL   N    N  N N 426 
VAL   CA   C  N S 427 
VAL   C    C  N N 428 
VAL   O    O  N N 429 
VAL   CB   C  N N 430 
VAL   CG1  C  N N 431 
VAL   CG2  C  N N 432 
VAL   OXT  O  N N 433 
VAL   H    H  N N 434 
VAL   H2   H  N N 435 
VAL   HA   H  N N 436 
VAL   HB   H  N N 437 
VAL   HG11 H  N N 438 
VAL   HG12 H  N N 439 
VAL   HG13 H  N N 440 
VAL   HG21 H  N N 441 
VAL   HG22 H  N N 442 
VAL   HG23 H  N N 443 
VAL   HXT  H  N N 444 
ZN    ZN   ZN N N 445 
# 
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 
A1B3X C   C1   sing N N 1   
A1B3X O   C1   doub N N 2   
A1B3X C1  N    sing N N 3   
A1B3X N   C2   sing N N 4   
A1B3X C2  C3   doub Y N 5   
A1B3X C3  C4   sing Y N 6   
A1B3X C4  C5   doub Y N 7   
A1B3X C5  C6   sing Y N 8   
A1B3X C6  C7   doub Y N 9   
A1B3X C2  C7   sing Y N 10  
A1B3X C7  C8   sing N N 11  
A1B3X C8  C9   sing N N 12  
A1B3X N   C9   sing N N 13  
A1B3X C9  C10  sing N N 14  
A1B3X O1  C10  doub N N 15  
A1B3X C10 N1   sing N N 16  
A1B3X N1  C11  sing N N 17  
A1B3X C11 C12  sing N N 18  
A1B3X C12 C13  sing N N 19  
A1B3X C13 C14  sing N N 20  
A1B3X C14 C15  sing N N 21  
A1B3X N2  C15  sing N N 22  
A1B3X C15 O2   doub N N 23  
A1B3X C16 C14  sing N N 24  
A1B3X N1  C16  sing N N 25  
A1B3X C4  H6   sing N N 26  
A1B3X C5  H7   sing N N 27  
A1B3X C6  H8   sing N N 28  
A1B3X C8  H10  sing N N 29  
A1B3X C8  H9   sing N N 30  
A1B3X C13 H15  sing N N 31  
A1B3X C13 H16  sing N N 32  
A1B3X N2  H18  sing N N 33  
A1B3X N2  H17  sing N N 34  
A1B3X C14 H1   sing N N 35  
A1B3X C12 H13  sing N N 36  
A1B3X C12 H14  sing N N 37  
A1B3X C11 H12  sing N N 38  
A1B3X C11 H11  sing N N 39  
A1B3X C16 H19  sing N N 40  
A1B3X C16 H20  sing N N 41  
A1B3X C9  H    sing N N 42  
A1B3X C   H3   sing N N 43  
A1B3X C   H2   sing N N 44  
A1B3X C   H4   sing N N 45  
A1B3X C3  H5   sing N N 46  
ALA   N   CA   sing N N 47  
ALA   N   H    sing N N 48  
ALA   N   H2   sing N N 49  
ALA   CA  C    sing N N 50  
ALA   CA  CB   sing N N 51  
ALA   CA  HA   sing N N 52  
ALA   C   O    doub N N 53  
ALA   C   OXT  sing N N 54  
ALA   CB  HB1  sing N N 55  
ALA   CB  HB2  sing N N 56  
ALA   CB  HB3  sing N N 57  
ALA   OXT HXT  sing N N 58  
ARG   N   CA   sing N N 59  
ARG   N   H    sing N N 60  
ARG   N   H2   sing N N 61  
ARG   CA  C    sing N N 62  
ARG   CA  CB   sing N N 63  
ARG   CA  HA   sing N N 64  
ARG   C   O    doub N N 65  
ARG   C   OXT  sing N N 66  
ARG   CB  CG   sing N N 67  
ARG   CB  HB2  sing N N 68  
ARG   CB  HB3  sing N N 69  
ARG   CG  CD   sing N N 70  
ARG   CG  HG2  sing N N 71  
ARG   CG  HG3  sing N N 72  
ARG   CD  NE   sing N N 73  
ARG   CD  HD2  sing N N 74  
ARG   CD  HD3  sing N N 75  
ARG   NE  CZ   sing N N 76  
ARG   NE  HE   sing N N 77  
ARG   CZ  NH1  sing N N 78  
ARG   CZ  NH2  doub N N 79  
ARG   NH1 HH11 sing N N 80  
ARG   NH1 HH12 sing N N 81  
ARG   NH2 HH21 sing N N 82  
ARG   NH2 HH22 sing N N 83  
ARG   OXT HXT  sing N N 84  
ASN   N   CA   sing N N 85  
ASN   N   H    sing N N 86  
ASN   N   H2   sing N N 87  
ASN   CA  C    sing N N 88  
ASN   CA  CB   sing N N 89  
ASN   CA  HA   sing N N 90  
ASN   C   O    doub N N 91  
ASN   C   OXT  sing N N 92  
ASN   CB  CG   sing N N 93  
ASN   CB  HB2  sing N N 94  
ASN   CB  HB3  sing N N 95  
ASN   CG  OD1  doub N N 96  
ASN   CG  ND2  sing N N 97  
ASN   ND2 HD21 sing N N 98  
ASN   ND2 HD22 sing N N 99  
ASN   OXT HXT  sing N N 100 
ASP   N   CA   sing N N 101 
ASP   N   H    sing N N 102 
ASP   N   H2   sing N N 103 
ASP   CA  C    sing N N 104 
ASP   CA  CB   sing N N 105 
ASP   CA  HA   sing N N 106 
ASP   C   O    doub N N 107 
ASP   C   OXT  sing N N 108 
ASP   CB  CG   sing N N 109 
ASP   CB  HB2  sing N N 110 
ASP   CB  HB3  sing N N 111 
ASP   CG  OD1  doub N N 112 
ASP   CG  OD2  sing N N 113 
ASP   OD2 HD2  sing N N 114 
ASP   OXT HXT  sing N N 115 
CYS   N   CA   sing N N 116 
CYS   N   H    sing N N 117 
CYS   N   H2   sing N N 118 
CYS   CA  C    sing N N 119 
CYS   CA  CB   sing N N 120 
CYS   CA  HA   sing N N 121 
CYS   C   O    doub N N 122 
CYS   C   OXT  sing N N 123 
CYS   CB  SG   sing N N 124 
CYS   CB  HB2  sing N N 125 
CYS   CB  HB3  sing N N 126 
CYS   SG  HG   sing N N 127 
CYS   OXT HXT  sing N N 128 
DMS   S   O    doub N N 129 
DMS   S   C1   sing N N 130 
DMS   S   C2   sing N N 131 
DMS   C1  H11  sing N N 132 
DMS   C1  H12  sing N N 133 
DMS   C1  H13  sing N N 134 
DMS   C2  H21  sing N N 135 
DMS   C2  H22  sing N N 136 
DMS   C2  H23  sing N N 137 
GLN   N   CA   sing N N 138 
GLN   N   H    sing N N 139 
GLN   N   H2   sing N N 140 
GLN   CA  C    sing N N 141 
GLN   CA  CB   sing N N 142 
GLN   CA  HA   sing N N 143 
GLN   C   O    doub N N 144 
GLN   C   OXT  sing N N 145 
GLN   CB  CG   sing N N 146 
GLN   CB  HB2  sing N N 147 
GLN   CB  HB3  sing N N 148 
GLN   CG  CD   sing N N 149 
GLN   CG  HG2  sing N N 150 
GLN   CG  HG3  sing N N 151 
GLN   CD  OE1  doub N N 152 
GLN   CD  NE2  sing N N 153 
GLN   NE2 HE21 sing N N 154 
GLN   NE2 HE22 sing N N 155 
GLN   OXT HXT  sing N N 156 
GLU   N   CA   sing N N 157 
GLU   N   H    sing N N 158 
GLU   N   H2   sing N N 159 
GLU   CA  C    sing N N 160 
GLU   CA  CB   sing N N 161 
GLU   CA  HA   sing N N 162 
GLU   C   O    doub N N 163 
GLU   C   OXT  sing N N 164 
GLU   CB  CG   sing N N 165 
GLU   CB  HB2  sing N N 166 
GLU   CB  HB3  sing N N 167 
GLU   CG  CD   sing N N 168 
GLU   CG  HG2  sing N N 169 
GLU   CG  HG3  sing N N 170 
GLU   CD  OE1  doub N N 171 
GLU   CD  OE2  sing N N 172 
GLU   OE2 HE2  sing N N 173 
GLU   OXT HXT  sing N N 174 
GLY   N   CA   sing N N 175 
GLY   N   H    sing N N 176 
GLY   N   H2   sing N N 177 
GLY   CA  C    sing N N 178 
GLY   CA  HA2  sing N N 179 
GLY   CA  HA3  sing N N 180 
GLY   C   O    doub N N 181 
GLY   C   OXT  sing N N 182 
GLY   OXT HXT  sing N N 183 
HIS   N   CA   sing N N 184 
HIS   N   H    sing N N 185 
HIS   N   H2   sing N N 186 
HIS   CA  C    sing N N 187 
HIS   CA  CB   sing N N 188 
HIS   CA  HA   sing N N 189 
HIS   C   O    doub N N 190 
HIS   C   OXT  sing N N 191 
HIS   CB  CG   sing N N 192 
HIS   CB  HB2  sing N N 193 
HIS   CB  HB3  sing N N 194 
HIS   CG  ND1  sing Y N 195 
HIS   CG  CD2  doub Y N 196 
HIS   ND1 CE1  doub Y N 197 
HIS   ND1 HD1  sing N N 198 
HIS   CD2 NE2  sing Y N 199 
HIS   CD2 HD2  sing N N 200 
HIS   CE1 NE2  sing Y N 201 
HIS   CE1 HE1  sing N N 202 
HIS   NE2 HE2  sing N N 203 
HIS   OXT HXT  sing N N 204 
HOH   O   H1   sing N N 205 
HOH   O   H2   sing N N 206 
ILE   N   CA   sing N N 207 
ILE   N   H    sing N N 208 
ILE   N   H2   sing N N 209 
ILE   CA  C    sing N N 210 
ILE   CA  CB   sing N N 211 
ILE   CA  HA   sing N N 212 
ILE   C   O    doub N N 213 
ILE   C   OXT  sing N N 214 
ILE   CB  CG1  sing N N 215 
ILE   CB  CG2  sing N N 216 
ILE   CB  HB   sing N N 217 
ILE   CG1 CD1  sing N N 218 
ILE   CG1 HG12 sing N N 219 
ILE   CG1 HG13 sing N N 220 
ILE   CG2 HG21 sing N N 221 
ILE   CG2 HG22 sing N N 222 
ILE   CG2 HG23 sing N N 223 
ILE   CD1 HD11 sing N N 224 
ILE   CD1 HD12 sing N N 225 
ILE   CD1 HD13 sing N N 226 
ILE   OXT HXT  sing N N 227 
LEU   N   CA   sing N N 228 
LEU   N   H    sing N N 229 
LEU   N   H2   sing N N 230 
LEU   CA  C    sing N N 231 
LEU   CA  CB   sing N N 232 
LEU   CA  HA   sing N N 233 
LEU   C   O    doub N N 234 
LEU   C   OXT  sing N N 235 
LEU   CB  CG   sing N N 236 
LEU   CB  HB2  sing N N 237 
LEU   CB  HB3  sing N N 238 
LEU   CG  CD1  sing N N 239 
LEU   CG  CD2  sing N N 240 
LEU   CG  HG   sing N N 241 
LEU   CD1 HD11 sing N N 242 
LEU   CD1 HD12 sing N N 243 
LEU   CD1 HD13 sing N N 244 
LEU   CD2 HD21 sing N N 245 
LEU   CD2 HD22 sing N N 246 
LEU   CD2 HD23 sing N N 247 
LEU   OXT HXT  sing N N 248 
LYS   N   CA   sing N N 249 
LYS   N   H    sing N N 250 
LYS   N   H2   sing N N 251 
LYS   CA  C    sing N N 252 
LYS   CA  CB   sing N N 253 
LYS   CA  HA   sing N N 254 
LYS   C   O    doub N N 255 
LYS   C   OXT  sing N N 256 
LYS   CB  CG   sing N N 257 
LYS   CB  HB2  sing N N 258 
LYS   CB  HB3  sing N N 259 
LYS   CG  CD   sing N N 260 
LYS   CG  HG2  sing N N 261 
LYS   CG  HG3  sing N N 262 
LYS   CD  CE   sing N N 263 
LYS   CD  HD2  sing N N 264 
LYS   CD  HD3  sing N N 265 
LYS   CE  NZ   sing N N 266 
LYS   CE  HE2  sing N N 267 
LYS   CE  HE3  sing N N 268 
LYS   NZ  HZ1  sing N N 269 
LYS   NZ  HZ2  sing N N 270 
LYS   NZ  HZ3  sing N N 271 
LYS   OXT HXT  sing N N 272 
MET   N   CA   sing N N 273 
MET   N   H    sing N N 274 
MET   N   H2   sing N N 275 
MET   CA  C    sing N N 276 
MET   CA  CB   sing N N 277 
MET   CA  HA   sing N N 278 
MET   C   O    doub N N 279 
MET   C   OXT  sing N N 280 
MET   CB  CG   sing N N 281 
MET   CB  HB2  sing N N 282 
MET   CB  HB3  sing N N 283 
MET   CG  SD   sing N N 284 
MET   CG  HG2  sing N N 285 
MET   CG  HG3  sing N N 286 
MET   SD  CE   sing N N 287 
MET   CE  HE1  sing N N 288 
MET   CE  HE2  sing N N 289 
MET   CE  HE3  sing N N 290 
MET   OXT HXT  sing N N 291 
PHE   N   CA   sing N N 292 
PHE   N   H    sing N N 293 
PHE   N   H2   sing N N 294 
PHE   CA  C    sing N N 295 
PHE   CA  CB   sing N N 296 
PHE   CA  HA   sing N N 297 
PHE   C   O    doub N N 298 
PHE   C   OXT  sing N N 299 
PHE   CB  CG   sing N N 300 
PHE   CB  HB2  sing N N 301 
PHE   CB  HB3  sing N N 302 
PHE   CG  CD1  doub Y N 303 
PHE   CG  CD2  sing Y N 304 
PHE   CD1 CE1  sing Y N 305 
PHE   CD1 HD1  sing N N 306 
PHE   CD2 CE2  doub Y N 307 
PHE   CD2 HD2  sing N N 308 
PHE   CE1 CZ   doub Y N 309 
PHE   CE1 HE1  sing N N 310 
PHE   CE2 CZ   sing Y N 311 
PHE   CE2 HE2  sing N N 312 
PHE   CZ  HZ   sing N N 313 
PHE   OXT HXT  sing N N 314 
PRO   N   CA   sing N N 315 
PRO   N   CD   sing N N 316 
PRO   N   H    sing N N 317 
PRO   CA  C    sing N N 318 
PRO   CA  CB   sing N N 319 
PRO   CA  HA   sing N N 320 
PRO   C   O    doub N N 321 
PRO   C   OXT  sing N N 322 
PRO   CB  CG   sing N N 323 
PRO   CB  HB2  sing N N 324 
PRO   CB  HB3  sing N N 325 
PRO   CG  CD   sing N N 326 
PRO   CG  HG2  sing N N 327 
PRO   CG  HG3  sing N N 328 
PRO   CD  HD2  sing N N 329 
PRO   CD  HD3  sing N N 330 
PRO   OXT HXT  sing N N 331 
SER   N   CA   sing N N 332 
SER   N   H    sing N N 333 
SER   N   H2   sing N N 334 
SER   CA  C    sing N N 335 
SER   CA  CB   sing N N 336 
SER   CA  HA   sing N N 337 
SER   C   O    doub N N 338 
SER   C   OXT  sing N N 339 
SER   CB  OG   sing N N 340 
SER   CB  HB2  sing N N 341 
SER   CB  HB3  sing N N 342 
SER   OG  HG   sing N N 343 
SER   OXT HXT  sing N N 344 
THR   N   CA   sing N N 345 
THR   N   H    sing N N 346 
THR   N   H2   sing N N 347 
THR   CA  C    sing N N 348 
THR   CA  CB   sing N N 349 
THR   CA  HA   sing N N 350 
THR   C   O    doub N N 351 
THR   C   OXT  sing N N 352 
THR   CB  OG1  sing N N 353 
THR   CB  CG2  sing N N 354 
THR   CB  HB   sing N N 355 
THR   OG1 HG1  sing N N 356 
THR   CG2 HG21 sing N N 357 
THR   CG2 HG22 sing N N 358 
THR   CG2 HG23 sing N N 359 
THR   OXT HXT  sing N N 360 
TRP   N   CA   sing N N 361 
TRP   N   H    sing N N 362 
TRP   N   H2   sing N N 363 
TRP   CA  C    sing N N 364 
TRP   CA  CB   sing N N 365 
TRP   CA  HA   sing N N 366 
TRP   C   O    doub N N 367 
TRP   C   OXT  sing N N 368 
TRP   CB  CG   sing N N 369 
TRP   CB  HB2  sing N N 370 
TRP   CB  HB3  sing N N 371 
TRP   CG  CD1  doub Y N 372 
TRP   CG  CD2  sing Y N 373 
TRP   CD1 NE1  sing Y N 374 
TRP   CD1 HD1  sing N N 375 
TRP   CD2 CE2  doub Y N 376 
TRP   CD2 CE3  sing Y N 377 
TRP   NE1 CE2  sing Y N 378 
TRP   NE1 HE1  sing N N 379 
TRP   CE2 CZ2  sing Y N 380 
TRP   CE3 CZ3  doub Y N 381 
TRP   CE3 HE3  sing N N 382 
TRP   CZ2 CH2  doub Y N 383 
TRP   CZ2 HZ2  sing N N 384 
TRP   CZ3 CH2  sing Y N 385 
TRP   CZ3 HZ3  sing N N 386 
TRP   CH2 HH2  sing N N 387 
TRP   OXT HXT  sing N N 388 
TYR   N   CA   sing N N 389 
TYR   N   H    sing N N 390 
TYR   N   H2   sing N N 391 
TYR   CA  C    sing N N 392 
TYR   CA  CB   sing N N 393 
TYR   CA  HA   sing N N 394 
TYR   C   O    doub N N 395 
TYR   C   OXT  sing N N 396 
TYR   CB  CG   sing N N 397 
TYR   CB  HB2  sing N N 398 
TYR   CB  HB3  sing N N 399 
TYR   CG  CD1  doub Y N 400 
TYR   CG  CD2  sing Y N 401 
TYR   CD1 CE1  sing Y N 402 
TYR   CD1 HD1  sing N N 403 
TYR   CD2 CE2  doub Y N 404 
TYR   CD2 HD2  sing N N 405 
TYR   CE1 CZ   doub Y N 406 
TYR   CE1 HE1  sing N N 407 
TYR   CE2 CZ   sing Y N 408 
TYR   CE2 HE2  sing N N 409 
TYR   CZ  OH   sing N N 410 
TYR   OH  HH   sing N N 411 
TYR   OXT HXT  sing N N 412 
VAL   N   CA   sing N N 413 
VAL   N   H    sing N N 414 
VAL   N   H2   sing N N 415 
VAL   CA  C    sing N N 416 
VAL   CA  CB   sing N N 417 
VAL   CA  HA   sing N N 418 
VAL   C   O    doub N N 419 
VAL   C   OXT  sing N N 420 
VAL   CB  CG1  sing N N 421 
VAL   CB  CG2  sing N N 422 
VAL   CB  HB   sing N N 423 
VAL   CG1 HG11 sing N N 424 
VAL   CG1 HG12 sing N N 425 
VAL   CG1 HG13 sing N N 426 
VAL   CG2 HG21 sing N N 427 
VAL   CG2 HG22 sing N N 428 
VAL   CG2 HG23 sing N N 429 
VAL   OXT HXT  sing N N 430 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I5G 
_atom_sites.fract_transf_matrix[1][1]   0.011230 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000516 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017168 
_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]   0.030619 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.904 7.071   24.176 1.00 34.98 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.089 7.245   23.332 1.00 35.15 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.264 6.069   22.351 1.00 34.13 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.669 4.992   22.536 1.00 34.19 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.331 7.380   24.206 1.00 37.76 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.462 6.187   24.962 1.00 40.81 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.014 6.310   21.277 1.00 32.26 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.280 5.287   20.275 1.00 31.03 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.545 5.844   18.887 1.00 30.19 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.111 6.950   18.560 1.00 29.80 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.260 5.067   18.041 1.00 28.90 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.565 5.516   16.688 1.00 29.26 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.570 4.340   15.698 1.00 28.44 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.564 3.170   16.124 1.00 29.41 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.937 6.221   16.686 1.00 29.89 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.529 4.635   14.389 1.00 27.55 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.656 3.648   13.323 1.00 27.39 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.086 3.824   12.735 1.00 29.79 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.518 4.954   12.499 1.00 29.92 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.613 3.836   12.197 1.00 26.88 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.166 3.867   12.710 1.00 26.27 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.797 2.781   11.089 1.00 27.33 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.190 4.510   11.615 1.00 25.61 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.805 2.721   12.501 1.00 31.09 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.154 2.786   11.942 1.00 31.77 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.192 2.062   10.609 1.00 32.01 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.198 0.832   10.584 1.00 33.06 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.191 2.223   12.938 1.00 32.01 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.325 3.078   14.179 1.00 33.79 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.137 4.204   14.187 1.00 35.13 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.593 2.796   15.323 1.00 35.24 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.229 5.017   15.308 1.00 36.46 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.665 3.608   16.443 1.00 36.42 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.508 4.702   16.441 1.00 37.42 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.584 5.504   17.548 1.00 40.08 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.076 2.801   9.494  1.00 31.73 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.078 2.196   8.157  1.00 31.82 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.216 2.783   7.314  1.00 33.44 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.378 4.010   7.258  1.00 33.68 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.700 2.338   7.443  1.00 33.00 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.239 3.797   7.400  1.00 32.60 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.751 1.728   6.037  1.00 33.65 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.081 1.928   6.740  1.00 33.38 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.251 2.412   5.999  1.00 34.76 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.110 3.332   6.851  1.00 35.78 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.350 3.020   8.023  1.00 36.42 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.419 4.548   6.347  1.00 34.85 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.147 5.523   7.138  1.00 35.16 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.216 6.663   7.601  1.00 34.42 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.628 7.818   7.678  1.00 33.81 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.389 6.056   6.397  1.00 37.52 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.494 5.034   6.331  1.00 43.18 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.349 4.945   7.224  1.00 45.50 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.480 4.211   5.292  1.00 44.04 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.970 6.317   7.956  1.00 33.91 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 27.975 7.265   8.448  1.00 33.52 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.460 6.863   9.840  1.00 32.23 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.343 5.674   10.148 1.00 32.02 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.773 7.308   7.484  1.00 34.48 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.111 7.749   6.076  1.00 36.02 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.665 8.998   5.832  1.00 37.61 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.853 6.928   4.988  1.00 37.05 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 27.967 9.413   4.541  1.00 39.18 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.153 7.332   3.692  1.00 38.89 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.702 8.581   3.470  1.00 40.62 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.024 8.990   2.190  1.00 43.55 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.150 7.853   10.683 1.00 31.19 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.514 7.655   11.996 1.00 31.01 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.193 8.460   11.945 1.00 29.89 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.219 9.662   11.685 1.00 30.02 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.424 8.156   13.145 1.00 32.87 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.733 8.385   14.495 1.00 35.38 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.748 8.757   15.580 1.00 36.33 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.264 9.819   16.472 1.00 39.02 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.693 9.602   17.655 1.00 40.57 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.493 8.360   18.089 1.00 38.64 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.276 10.624  18.395 1.00 41.62 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.045 7.799   12.134 1.00 28.02 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.748 8.470   12.086 1.00 27.49 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.240 8.605   13.498 1.00 27.05 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.068 7.602   14.186 1.00 27.61 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.719 7.682   11.235 1.00 27.79 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.405 8.456   11.080 1.00 28.26 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.303 7.294   9.870  1.00 27.30 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.002 9.826   13.941 1.00 26.02 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.504 10.067  15.297 1.00 26.65 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.303 10.992  15.269 1.00 25.86 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.046 11.665  14.255 1.00 25.76 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.604 10.678  16.209 1.00 28.60 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.775 9.727   16.327 1.00 31.92 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.052 12.064  15.699 1.00 28.00 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.546 11.047  16.402 1.00 25.18 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.507 12.061  16.552 1.00 24.36 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.238 13.442  16.574 1.00 24.93 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.220 13.616  17.313 1.00 25.47 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.759 11.902  17.893 1.00 24.86 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.929 10.631  17.947 1.00 25.16 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.395 9.591   18.416 1.00 26.83 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.679 10.684  17.456 1.00 25.00 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.786 14.384  15.770 1.00 24.94 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.441 15.702  15.665 1.00 25.86 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.546 16.388  17.021 1.00 27.57 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.589 16.951  17.343 1.00 28.44 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.693 16.604  14.670 1.00 25.77 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.435 17.924  14.311 1.00 26.69 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.469 18.775  13.515 1.00 28.15 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.027 20.015  12.957 1.00 30.64 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.076 21.176  13.602 1.00 34.56 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.716 21.253  14.883 1.00 33.48 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.522 22.266  12.986 1.00 36.24 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.492 16.262  17.845 1.00 27.38 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.466 16.908  19.163 1.00 27.38 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.459 16.306  20.180 1.00 29.65 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.743 16.943  21.200 1.00 30.52 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.038 16.972  19.723 1.00 27.54 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.527 15.685  20.295 1.00 27.21 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.919 14.723  19.493 1.00 28.30 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.515 15.257  21.580 1.00 27.93 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.554 13.749  20.316 1.00 28.72 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.874 14.032  21.585 1.00 28.46 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.004 15.125  19.887 1.00 29.52 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.000 14.451  20.715 1.00 30.51 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.424 14.486  20.074 1.00 31.03 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.356 13.919  20.640 1.00 31.31 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.575 13.009  21.021 1.00 30.09 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.244 12.850  21.781 1.00 30.25 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.940 11.364  22.044 1.00 30.15 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.260 13.634  23.117 1.00 30.99 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.587 15.129  18.902 1.00 31.12 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.889 15.231  18.243 1.00 32.38 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.881 16.004  19.142 1.00 34.59 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.479 16.932  19.844 1.00 35.22 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.733 15.965  16.919 1.00 31.68 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.138 15.585  19.152 1.00 36.13 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.192 16.244  19.937 1.00 38.04 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.839 17.373  19.120 1.00 39.26 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.642 17.431  17.903 1.00 39.27 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.251 15.209  20.365 1.00 39.61 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.922 14.671  19.214 1.00 39.79 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.669 14.082  21.214 1.00 39.30 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.643 18.262  19.765 1.00 39.67 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.357 19.308  19.020 1.00 40.64 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.304 18.671  17.968 1.00 40.26 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.473 19.223  16.888 1.00 40.79 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.132 20.268  19.969 1.00 41.90 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.185 19.598  20.801 1.00 46.41 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 32.524 19.976  20.720 1.00 49.37 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 31.066 18.606  21.716 1.00 47.81 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 33.168 19.191  21.571 1.00 49.86 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 32.332 18.348  22.194 1.00 49.65 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.849 17.483  18.264 1.00 39.85 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.705 16.698  17.372 1.00 41.13 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.944 16.136  16.168 1.00 41.73 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.549 15.884  15.114 1.00 42.88 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.322 15.538  18.142 1.00 43.57 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.246 16.010  19.238 1.00 51.16 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.009 16.988  19.086 1.00 53.45 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.183 15.337  20.378 1.00 53.34 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.625 15.876  16.333 1.00 39.53 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.813 15.388  15.218 1.00 37.71 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.662 16.527  14.203 1.00 36.46 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.714 16.276  12.998 1.00 36.90 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.414 14.927  15.706 1.00 37.43 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.342 13.510  16.245 1.00 38.99 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.876 12.593  15.580 1.00 39.27 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.712 13.310  17.316 1.00 38.59 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.468 17.771  14.691 1.00 34.95 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.337 18.974  13.864 1.00 35.49 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.634 19.282  13.077 1.00 35.76 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.569 19.643  11.899 1.00 35.15 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.927 20.163  14.737 1.00 35.68 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.471 20.116  15.109 1.00 35.45 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.937 19.762  16.315 1.00 36.84 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.364 20.425  14.251 1.00 35.34 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.558 19.830  16.262 1.00 36.71 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.181 20.242  15.005 1.00 35.93 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.256 20.854  12.920 1.00 35.73 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 22.919 20.504  14.482 1.00 36.08 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.002 21.129  12.410 1.00 36.16 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 22.848 20.915  13.177 1.00 36.20 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.801 19.090  13.706 1.00 35.43 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.073 19.265  13.002 1.00 36.98 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.207 18.225  11.869 1.00 38.08 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 32.803 18.510  10.830 1.00 39.36 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.236 19.112  13.981 1.00 37.89 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.663 17.007  12.070 1.00 37.67 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.739 15.962  11.070 1.00 37.84 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.416 15.804  10.295 1.00 37.16 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.110 14.710  9.822  1.00 37.23 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.103 14.638  11.771 1.00 40.13 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.474 14.711  12.418 1.00 44.93 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.448 15.103  11.788 1.00 46.12 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.587 14.361  13.691 1.00 46.73 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.636 16.871  10.180 1.00 35.06 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.329 16.809  9.525  1.00 34.11 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.398 16.443  8.052  1.00 33.86 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.240 16.984  7.323  1.00 33.39 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.645 18.177  9.654  1.00 32.85 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.268 18.320  8.999  1.00 32.41 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.231 17.498  9.761  1.00 32.22 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 25.863 19.808  8.883  1.00 32.31 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.456 15.573  7.610  1.00 32.54 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.240 15.187  6.217  1.00 32.64 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.860 15.789  5.776  1.00 32.58 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.727 16.363  4.683  1.00 32.93 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.204 13.633  6.076  1.00 33.41 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.809 13.227  4.660  1.00 33.28 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.536 13.004  6.475  1.00 34.61 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.827 15.617  6.641  1.00 31.09 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.479 16.071  6.333  1.00 31.54 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.645 16.137  7.602  1.00 31.18 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.792 15.288  8.490  1.00 30.85 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.825 15.112  5.315  1.00 31.94 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.351 15.318  5.070  1.00 33.02 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.771 16.115  4.120  1.00 34.71 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.276 14.662  5.758  1.00 33.09 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.395 16.008  4.188  1.00 35.05 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.067 15.103  5.173  1.00 34.13 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.219 13.715  6.786  1.00 32.92 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.824 14.651  5.606  1.00 33.75 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 18.984 13.265  7.206  1.00 33.14 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.805 13.739  6.626  1.00 33.40 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.769 17.136  7.693  1.00 29.76 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.859 17.244  8.833  1.00 29.89 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.551 17.881  8.400  1.00 29.80 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.535 18.712  7.477  1.00 30.10 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.493 17.991  10.016 1.00 31.54 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.057 19.372  9.662  1.00 35.28 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.092 20.539  9.712  1.00 37.03 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.449 21.608  9.163  1.00 34.77 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.990 20.397  10.303 1.00 34.92 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.434 17.487  9.043  1.00 28.70 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.146 18.086  8.740  1.00 28.80 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.391 18.208  10.067 1.00 27.95 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.986 17.202  10.644 1.00 27.32 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.401 17.232  7.714  1.00 30.20 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.088 17.772  7.205  1.00 35.91 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.471 18.596  7.912  1.00 37.77 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.661 17.354  6.095  1.00 37.33 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.234 19.445  10.564 1.00 27.79 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.545 19.723  11.819 0.50 27.61 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.555 19.654  11.844 0.50 28.17 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.085 19.231  11.771 1.00 28.17 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.551 18.731  12.766 1.00 28.36 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.572 21.227  12.086 0.50 27.83 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.664 21.108  12.292 0.50 30.16 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.789 21.560  13.215 0.50 28.46 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.972 21.936  11.378 0.50 33.19 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.436 19.397  10.608 1.00 27.43 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.052 18.980  10.437 1.00 27.67 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.898 17.430  10.552 1.00 26.56 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.815 16.977  10.823 1.00 28.12 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.454 19.504  9.133  1.00 31.09 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.776 18.673  8.029  1.00 35.68 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.968 16.660  10.356 1.00 24.85 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.936 15.193  10.510 1.00 23.80 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.577 14.716  11.839 1.00 23.61 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.564 13.500  12.104 1.00 23.05 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.704 14.535  9.354  1.00 24.66 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.024 14.714  8.024  1.00 25.44 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.884 14.122  6.912  1.00 25.64 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.886 12.656  7.007  1.00 25.53 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.933 11.843  5.953  1.00 28.14 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.079 12.343  4.719  1.00 28.28 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.874 10.523  6.123  1.00 27.99 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.188 15.635  12.640 1.00 23.56 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.953 15.267  13.860 1.00 23.31 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.085 14.279  13.510 1.00 24.45 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.378 13.391  14.301 1.00 24.94 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.063 14.660  15.003 1.00 25.02 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.828 14.389  16.324 1.00 25.28 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.662 15.229  16.714 1.00 24.41 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.571 13.339  16.974 1.00 25.26 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.740 14.428  12.333 1.00 24.91 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.835 13.535  11.963 1.00 25.68 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.128 14.326  11.704 1.00 26.15 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.077 15.458  11.209 1.00 26.36 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.502 12.749  10.686 1.00 25.98 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.517 11.582  10.822 1.00 26.79 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.378 10.864  9.488  1.00 25.48 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.942 10.588  11.949 1.00 27.96 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.261 13.700  12.021 1.00 26.16 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.599 14.222  11.721 1.00 27.51 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.477 13.035  11.363 1.00 28.37 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.408 11.982  12.009 1.00 27.86 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.187 15.052  12.892 1.00 27.56 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.568 15.712  12.643 1.00 28.55 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.660 17.091  13.350 1.00 29.24 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.697 14.805  13.163 1.00 28.78 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.272 13.188  10.297 1.00 27.88 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.207 12.160  9.862  1.00 29.60 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.607 12.778  9.913  1.00 31.33 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.817 13.863  9.359  1.00 31.95 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.874 11.612  8.446  1.00 29.94 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.943 10.612  7.980  1.00 31.22 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.481 10.956  8.419  1.00 28.93 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.530 12.130  10.614 1.00 31.89 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.928 12.552  10.655 1.00 33.60 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.826 11.457  10.028 1.00 34.92 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.425 10.300  9.916  1.00 34.29 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.373 12.879  12.082 1.00 34.75 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.094 11.811  12.978 1.00 34.94 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.041 11.830  9.623  1.00 35.98 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.013 10.910  9.034  1.00 36.96 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.772 10.155  10.141 1.00 37.65 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.955 10.686  11.235 1.00 37.95 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.008 11.692  8.172  1.00 38.53 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.636 12.702  8.946  1.00 39.79 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.174 8.907   9.883  1.00 38.69 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.928 8.119   10.871 1.00 40.62 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.250 7.621   10.245 1.00 43.53 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.322 7.480   9.019  1.00 44.33 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.102 6.891   11.345 1.00 41.38 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.066 5.914   10.312 1.00 41.97 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.687 7.253   11.761 1.00 41.05 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.247 7.254   11.074 1.00 44.85 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.496 6.705   10.529 1.00 47.13 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.384 5.198   10.295 1.00 47.64 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.867 4.685   9.285  1.00 48.53 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.693 7.049   11.428 1.00 49.95 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.442 6.520   12.730 1.00 52.46 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.944 8.544   11.520 1.00 50.66 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.762 4.485   11.233 1.00 46.95 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.589 3.044   11.114 1.00 46.86 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.299 2.715   10.362 1.00 45.49 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.298 3.416   10.515 1.00 44.49 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.553 2.412   12.496 1.00 47.48 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.315 1.642   9.572  1.00 44.56 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.124 1.224   8.838  1.00 44.24 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.129 0.489   9.778  1.00 41.64 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.552 -0.315  10.612 1.00 41.71 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.520 0.352   7.638  1.00 47.81 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.566 0.498   6.460  1.00 54.71 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.855 -0.529  5.398  1.00 61.47 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.969 -0.612  4.868  1.00 63.19 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.854 -1.336  5.069  1.00 62.39 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.839 0.816   9.644  1.00 38.86 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.731 0.282   10.435 1.00 37.67 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.106 -0.943  9.799  1.00 36.40 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.358 -1.232  8.627  1.00 37.22 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.307 -1.703  10.572 1.00 34.59 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.775 -2.974  10.089 1.00 33.94 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.253 -3.061  9.987  1.00 33.15 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.741 -4.164  9.781  1.00 33.70 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.317 -4.112  10.941 1.00 34.41 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.118 -4.218  10.938 1.00 37.90 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.533 -1.941  10.141 1.00 31.83 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.073 -1.967  10.006 1.00 31.86 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.691 -1.903  8.522  1.00 31.80 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.403 -1.302  7.705  1.00 31.89 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.427 -0.780  10.783 1.00 32.77 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.553 -0.918  12.293 1.00 37.69 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.523 -2.063  12.783 1.00 40.22 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.691 0.132   12.992 1.00 37.21 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.593 -2.562  8.169  1.00 31.71 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.050 -2.496  6.811  1.00 33.09 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.729 -1.721  6.872  1.00 31.60 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.922 -1.998  7.750  1.00 31.25 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.820 -3.910  6.261  1.00 37.48 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.096 -4.479  6.001  1.00 39.61 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 21.010 -3.907  4.955  1.00 38.74 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.524 -0.743  5.984  1.00 30.38 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.279 0.027   5.971  1.00 28.98 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.235 -0.728  5.123  1.00 28.89 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.559 -1.201  4.032  1.00 29.57 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.506 1.456   5.419  1.00 29.24 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.648 2.201   6.177  1.00 29.15 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.203 2.263   5.469  1.00 28.89 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.366 2.361   7.687  1.00 29.02 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.994 -0.845  5.610  1.00 27.76 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.900 -1.481  4.874  1.00 27.48 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.504 -0.626  3.668  1.00 27.15 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.469 0.595   3.776  1.00 27.11 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.683 -1.616  5.800  1.00 26.77 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.184 -1.265  2.529  1.00 27.05 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.700 -0.553  1.336  1.00 27.99 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.425 -1.303  0.972  1.00 28.45 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.454 -2.293  0.228  1.00 29.09 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.737 -0.561  0.210  1.00 28.44 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.093 0.062   0.618  1.00 31.51 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.051 1.541   1.019  1.00 33.90 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.382 1.996   1.453  1.00 36.29 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.616 3.135   2.098  1.00 36.99 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.622 3.975   2.360  1.00 34.59 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.840 3.439   2.494  1.00 35.66 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.309 -0.861  1.576  1.00 28.94 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.028 -1.565  1.518  1.00 28.61 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.871  -0.626  1.942  1.00 28.58 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.121 0.493   2.379  1.00 28.12 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.116 -2.729  2.502  1.00 28.84 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.214 -2.183  4.241  1.00 27.91 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.618  -1.161  1.952  1.00 29.02 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.460  -0.447  2.492  1.00 29.57 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.829  -1.302  3.617  1.00 29.65 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.613  -1.253  3.823  1.00 30.61 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.412  -0.114  1.402  1.00 33.03 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.782  -1.313  0.734  1.00 41.04 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.292  -2.442  0.930  1.00 42.81 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.771  -1.127  0.007  1.00 44.78 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.648  -2.052  4.399  1.00 28.24 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.138  -2.803  5.547  1.00 27.23 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.417  -1.845  6.510  1.00 25.99 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.830  -0.683  6.688  1.00 25.35 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.280  -3.494  6.296  1.00 28.01 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.929  -4.976  5.497  1.00 30.26 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.345  -2.345  7.115  1.00 24.22 ? 59  GLN   A N   1 
ATOM   407  C  CA  A GLN   A 1 53  ? 4.570  -1.626  8.124  0.50 24.52 ? 59  GLN   A CA  1 
ATOM   408  C  CA  B GLN   A 1 53  ? 4.680  -1.552  8.130  0.50 24.85 ? 59  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 53  ? 4.518  -2.406  9.434  1.00 24.47 ? 59  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 53  ? 3.718  -2.088  10.306 1.00 24.73 ? 59  GLN   A O   1 
ATOM   411  C  CB  A GLN   A 1 53  ? 3.137  -1.306  7.650  0.50 25.57 ? 59  GLN   A CB  1 
ATOM   412  C  CB  B GLN   A 1 53  ? 3.406  -0.855  7.586  0.50 27.07 ? 59  GLN   A CB  1 
ATOM   413  C  CG  A GLN   A 1 53  ? 2.998  0.116   7.142  0.50 26.12 ? 59  GLN   A CG  1 
ATOM   414  C  CG  B GLN   A 1 53  ? 3.709  0.125   6.383  0.50 30.47 ? 59  GLN   A CG  1 
ATOM   415  C  CD  A GLN   A 1 53  ? 1.567  0.487   6.910  0.50 26.09 ? 59  GLN   A CD  1 
ATOM   416  C  CD  B GLN   A 1 53  ? 4.673  1.281   6.695  0.50 35.39 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 A GLN   A 1 53  ? 1.026  0.302   5.807  0.50 26.15 ? 59  GLN   A OE1 1 
ATOM   418  O  OE1 B GLN   A 1 53  ? 5.526  1.709   5.890  0.50 35.55 ? 59  GLN   A OE1 1 
ATOM   419  N  NE2 A GLN   A 1 53  ? 0.917  1.011   7.959  0.50 24.05 ? 59  GLN   A NE2 1 
ATOM   420  N  NE2 B GLN   A 1 53  ? 4.575  1.816   7.875  0.50 35.90 ? 59  GLN   A NE2 1 
ATOM   421  N  N   . THR   A 1 54  ? 5.360  -3.487  9.584  1.00 23.66 ? 60  THR   A N   1 
ATOM   422  C  CA  . THR   A 1 54  ? 5.473  -4.287  10.818 1.00 23.43 ? 60  THR   A CA  1 
ATOM   423  C  C   . THR   A 1 54  ? 6.974  -4.496  11.047 1.00 23.08 ? 60  THR   A C   1 
ATOM   424  O  O   . THR   A 1 54  ? 7.786  -4.538  10.096 1.00 22.33 ? 60  THR   A O   1 
ATOM   425  C  CB  . THR   A 1 54  ? 4.697  -5.597  10.838 1.00 26.54 ? 60  THR   A CB  1 
ATOM   426  O  OG1 . THR   A 1 54  ? 5.296  -6.483  9.905  1.00 29.28 ? 60  THR   A OG1 1 
ATOM   427  C  CG2 . THR   A 1 54  ? 3.200  -5.415  10.523 1.00 26.34 ? 60  THR   A CG2 1 
ATOM   428  N  N   . GLY   A 1 55  ? 7.350  -4.521  12.309 1.00 22.67 ? 61  GLY   A N   1 
ATOM   429  C  CA  . GLY   A 1 55  ? 8.767  -4.630  12.668 1.00 22.70 ? 61  GLY   A CA  1 
ATOM   430  C  C   . GLY   A 1 55  ? 8.919  -4.788  14.170 1.00 22.09 ? 61  GLY   A C   1 
ATOM   431  O  O   . GLY   A 1 55  ? 7.972  -5.136  14.846 1.00 23.25 ? 61  GLY   A O   1 
ATOM   432  N  N   . VAL   A 1 56  ? 10.132 -4.654  14.668 1.00 21.62 ? 62  VAL   A N   1 
ATOM   433  C  CA  . VAL   A 1 56  ? 10.449 -4.795  16.094 1.00 21.96 ? 62  VAL   A CA  1 
ATOM   434  C  C   . VAL   A 1 56  ? 11.294 -3.591  16.508 1.00 22.34 ? 62  VAL   A C   1 
ATOM   435  O  O   . VAL   A 1 56  ? 12.205 -3.236  15.782 1.00 22.73 ? 62  VAL   A O   1 
ATOM   436  C  CB  . VAL   A 1 56  ? 11.237 -6.107  16.315 1.00 22.46 ? 62  VAL   A CB  1 
ATOM   437  C  CG1 . VAL   A 1 56  ? 11.681 -6.237  17.776 1.00 23.41 ? 62  VAL   A CG1 1 
ATOM   438  C  CG2 . VAL   A 1 56  ? 10.389 -7.303  15.920 1.00 22.87 ? 62  VAL   A CG2 1 
ATOM   439  N  N   . TYR   A 1 57  ? 10.973 -2.940  17.642 1.00 22.62 ? 63  TYR   A N   1 
ATOM   440  C  CA  . TYR   A 1 57  ? 11.798 -1.802  18.096 1.00 22.22 ? 63  TYR   A CA  1 
ATOM   441  C  C   . TYR   A 1 57  ? 12.379 -2.034  19.467 1.00 22.78 ? 63  TYR   A C   1 
ATOM   442  O  O   . TYR   A 1 57  ? 11.780 -2.754  20.261 1.00 23.52 ? 63  TYR   A O   1 
ATOM   443  C  CB  . TYR   A 1 57  ? 11.027 -0.448  18.057 1.00 21.65 ? 63  TYR   A CB  1 
ATOM   444  C  CG  . TYR   A 1 57  ? 10.105 -0.187  19.240 1.00 23.05 ? 63  TYR   A CG  1 
ATOM   445  C  CD1 . TYR   A 1 57  ? 8.863  -0.812  19.336 1.00 23.71 ? 63  TYR   A CD1 1 
ATOM   446  C  CD2 . TYR   A 1 57  ? 10.476 0.679   20.263 1.00 23.44 ? 63  TYR   A CD2 1 
ATOM   447  C  CE1 . TYR   A 1 57  ? 7.998  -0.547  20.399 1.00 24.65 ? 63  TYR   A CE1 1 
ATOM   448  C  CE2 . TYR   A 1 57  ? 9.617  0.953   21.327 1.00 24.37 ? 63  TYR   A CE2 1 
ATOM   449  C  CZ  . TYR   A 1 57  ? 8.385  0.324   21.402 1.00 25.11 ? 63  TYR   A CZ  1 
ATOM   450  O  OH  . TYR   A 1 57  ? 7.521  0.581   22.450 1.00 25.63 ? 63  TYR   A OH  1 
ATOM   451  N  N   . TYR   A 1 58  ? 13.490 -1.357  19.784 1.00 21.90 ? 64  TYR   A N   1 
ATOM   452  C  CA  . TYR   A 1 58  ? 14.071 -1.465  21.115 1.00 23.23 ? 64  TYR   A CA  1 
ATOM   453  C  C   . TYR   A 1 58  ? 13.597 -0.315  22.002 1.00 24.35 ? 64  TYR   A C   1 
ATOM   454  O  O   . TYR   A 1 58  ? 13.744 0.869   21.625 1.00 23.98 ? 64  TYR   A O   1 
ATOM   455  C  CB  . TYR   A 1 58  ? 15.595 -1.478  21.050 1.00 23.25 ? 64  TYR   A CB  1 
ATOM   456  C  CG  . TYR   A 1 58  ? 16.212 -1.607  22.427 1.00 25.34 ? 64  TYR   A CG  1 
ATOM   457  C  CD1 . TYR   A 1 58  ? 15.941 -2.709  23.232 1.00 26.79 ? 64  TYR   A CD1 1 
ATOM   458  C  CD2 . TYR   A 1 58  ? 16.969 -0.576  22.970 1.00 26.77 ? 64  TYR   A CD2 1 
ATOM   459  C  CE1 . TYR   A 1 58  ? 16.495 -2.829  24.514 1.00 27.62 ? 64  TYR   A CE1 1 
ATOM   460  C  CE2 . TYR   A 1 58  ? 17.491 -0.661  24.261 1.00 28.51 ? 64  TYR   A CE2 1 
ATOM   461  C  CZ  . TYR   A 1 58  ? 17.244 -1.787  25.035 1.00 29.39 ? 64  TYR   A CZ  1 
ATOM   462  O  OH  . TYR   A 1 58  ? 17.811 -1.912  26.294 1.00 30.20 ? 64  TYR   A OH  1 
ATOM   463  N  N   . CYS   A 1 59  ? 13.102 -0.666  23.200 1.00 24.55 ? 65  CYS   A N   1 
ATOM   464  C  CA  . CYS   A 1 59  ? 12.620 0.286   24.204 1.00 25.26 ? 65  CYS   A CA  1 
ATOM   465  C  C   . CYS   A 1 59  ? 13.573 0.272   25.426 1.00 26.36 ? 65  CYS   A C   1 
ATOM   466  O  O   . CYS   A 1 59  ? 13.475 -0.636  26.256 1.00 27.13 ? 65  CYS   A O   1 
ATOM   467  C  CB  . CYS   A 1 59  ? 11.202 -0.087  24.608 1.00 26.39 ? 65  CYS   A CB  1 
ATOM   468  S  SG  . CYS   A 1 59  ? 10.527 0.961   25.922 1.00 29.30 ? 65  CYS   A SG  1 
ATOM   469  N  N   . SER   A 1 60  ? 14.490 1.254   25.532 1.00 25.45 ? 66  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 60  ? 15.475 1.238   26.628 1.00 27.74 ? 66  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 60  ? 14.857 1.329   28.027 1.00 28.00 ? 66  SER   A C   1 
ATOM   472  O  O   . SER   A 1 60  ? 15.384 0.724   28.968 1.00 28.91 ? 66  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 60  ? 16.543 2.313   26.441 1.00 31.80 ? 66  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 60  ? 16.020 3.609   26.666 1.00 35.71 ? 66  SER   A OG  1 
ATOM   475  N  N   . SER   A 1 61  ? 13.717 2.038   28.155 1.00 27.19 ? 67  SER   A N   1 
ATOM   476  C  CA  . SER   A 1 61  ? 13.014 2.174   29.440 1.00 26.67 ? 67  SER   A CA  1 
ATOM   477  C  C   . SER   A 1 61  ? 12.338 0.890   29.946 1.00 27.81 ? 67  SER   A C   1 
ATOM   478  O  O   . SER   A 1 61  ? 11.848 0.865   31.085 1.00 29.76 ? 67  SER   A O   1 
ATOM   479  C  CB  . SER   A 1 61  ? 12.002 3.316   29.402 1.00 27.13 ? 67  SER   A CB  1 
ATOM   480  O  OG  . SER   A 1 61  ? 10.964 3.110   28.469 1.00 29.76 ? 67  SER   A OG  1 
ATOM   481  N  N   . ARG   A 1 62  ? 12.272 -0.136  29.107 1.00 26.57 ? 68  ARG   A N   1 
ATOM   482  C  CA  . ARG   A 1 62  ? 11.751 -1.434  29.503 1.00 26.91 ? 68  ARG   A CA  1 
ATOM   483  C  C   . ARG   A 1 62  ? 12.826 -2.534  29.339 1.00 27.78 ? 68  ARG   A C   1 
ATOM   484  O  O   . ARG   A 1 62  ? 12.547 -3.696  29.642 1.00 27.92 ? 68  ARG   A O   1 
ATOM   485  C  CB  . ARG   A 1 62  ? 10.516 -1.778  28.647 1.00 28.12 ? 68  ARG   A CB  1 
ATOM   486  C  CG  . ARG   A 1 62  ? 9.318  -0.849  28.924 1.00 29.51 ? 68  ARG   A CG  1 
ATOM   487  C  CD  . ARG   A 1 62  ? 8.682  -1.158  30.285 1.00 30.97 ? 68  ARG   A CD  1 
ATOM   488  N  NE  . ARG   A 1 62  ? 7.527  -0.299  30.549 1.00 31.84 ? 68  ARG   A NE  1 
ATOM   489  C  CZ  . ARG   A 1 62  ? 7.603  0.879   31.170 1.00 35.16 ? 68  ARG   A CZ  1 
ATOM   490  N  NH1 . ARG   A 1 62  ? 8.773  1.333   31.612 1.00 34.03 ? 68  ARG   A NH1 1 
ATOM   491  N  NH2 . ARG   A 1 62  ? 6.505  1.600   31.376 1.00 34.85 ? 68  ARG   A NH2 1 
ATOM   492  N  N   . ARG   A 1 63  ? 14.011 -2.213  28.739 1.00 28.47 ? 69  ARG   A N   1 
ATOM   493  C  CA  . ARG   A 1 63  ? 15.066 -3.195  28.399 1.00 29.43 ? 69  ARG   A CA  1 
ATOM   494  C  C   . ARG   A 1 63  ? 14.415 -4.346  27.598 1.00 29.07 ? 69  ARG   A C   1 
ATOM   495  O  O   . ARG   A 1 63  ? 14.587 -5.529  27.934 1.00 30.99 ? 69  ARG   A O   1 
ATOM   496  C  CB  . ARG   A 1 63  ? 15.766 -3.742  29.658 1.00 30.45 ? 69  ARG   A CB  1 
ATOM   497  C  CG  . ARG   A 1 63  ? 16.624 -2.721  30.383 1.00 33.29 ? 69  ARG   A CG  1 
ATOM   498  C  CD  . ARG   A 1 63  ? 17.323 -3.364  31.562 1.00 35.93 ? 69  ARG   A CD  1 
ATOM   499  N  NE  . ARG   A 1 63  ? 18.101 -2.403  32.338 1.00 38.31 ? 69  ARG   A NE  1 
ATOM   500  C  CZ  . ARG   A 1 63  ? 18.009 -2.248  33.659 1.00 39.21 ? 69  ARG   A CZ  1 
ATOM   501  N  NH1 . ARG   A 1 63  ? 17.128 -2.957  34.360 1.00 37.11 ? 69  ARG   A NH1 1 
ATOM   502  N  NH2 . ARG   A 1 63  ? 18.754 -1.338  34.281 1.00 38.64 ? 69  ARG   A NH2 1 
ATOM   503  N  N   . LYS   A 1 64  ? 13.564 -3.979  26.634 1.00 27.34 ? 70  LYS   A N   1 
ATOM   504  C  CA  . LYS   A 1 64  ? 12.800 -4.967  25.883 1.00 27.65 ? 70  LYS   A CA  1 
ATOM   505  C  C   . LYS   A 1 64  ? 12.605 -4.554  24.430 1.00 27.24 ? 70  LYS   A C   1 
ATOM   506  O  O   . LYS   A 1 64  ? 12.508 -3.360  24.124 1.00 27.50 ? 70  LYS   A O   1 
ATOM   507  C  CB  . LYS   A 1 64  ? 11.425 -5.153  26.549 1.00 30.37 ? 70  LYS   A CB  1 
ATOM   508  C  CG  . LYS   A 1 64  ? 10.566 -6.261  25.951 1.00 37.76 ? 70  LYS   A CG  1 
ATOM   509  C  CD  . LYS   A 1 64  ? 9.762  -6.957  27.049 1.00 43.51 ? 70  LYS   A CD  1 
ATOM   510  C  CE  . LYS   A 1 64  ? 8.924  -8.118  26.547 1.00 46.88 ? 70  LYS   A CE  1 
ATOM   511  N  NZ  . LYS   A 1 64  ? 9.758  -9.312  26.209 1.00 48.97 ? 70  LYS   A NZ  1 
ATOM   512  N  N   . HIS   A 1 65  ? 12.573 -5.545  23.541 1.00 25.60 ? 71  HIS   A N   1 
ATOM   513  C  CA  . HIS   A 1 65  ? 12.300 -5.348  22.126 1.00 25.30 ? 71  HIS   A CA  1 
ATOM   514  C  C   . HIS   A 1 65  ? 10.798 -5.704  21.955 1.00 26.36 ? 71  HIS   A C   1 
ATOM   515  O  O   . HIS   A 1 65  ? 10.334 -6.725  22.495 1.00 27.94 ? 71  HIS   A O   1 
ATOM   516  C  CB  . HIS   A 1 65  ? 13.188 -6.266  21.249 1.00 25.44 ? 71  HIS   A CB  1 
ATOM   517  C  CG  . HIS   A 1 65  ? 14.661 -6.015  21.388 1.00 25.47 ? 71  HIS   A CG  1 
ATOM   518  N  ND1 . HIS   A 1 65  ? 15.363 -5.246  20.469 1.00 26.86 ? 71  HIS   A ND1 1 
ATOM   519  C  CD2 . HIS   A 1 65  ? 15.509 -6.409  22.365 1.00 26.09 ? 71  HIS   A CD2 1 
ATOM   520  C  CE1 . HIS   A 1 65  ? 16.613 -5.219  20.899 1.00 27.57 ? 71  HIS   A CE1 1 
ATOM   521  N  NE2 . HIS   A 1 65  ? 16.742 -5.865  22.062 1.00 28.09 ? 71  HIS   A NE2 1 
ATOM   522  N  N   . TYR   A 1 66  ? 10.032 -4.853  21.243 1.00 24.57 ? 72  TYR   A N   1 
ATOM   523  C  CA  . TYR   A 1 66  ? 8.614  -5.113  21.036 1.00 24.88 ? 72  TYR   A CA  1 
ATOM   524  C  C   . TYR   A 1 66  ? 8.224  -5.211  19.563 1.00 24.19 ? 72  TYR   A C   1 
ATOM   525  O  O   . TYR   A 1 66  ? 8.559  -4.330  18.768 1.00 22.80 ? 72  TYR   A O   1 
ATOM   526  C  CB  . TYR   A 1 66  ? 7.755  -4.001  21.650 1.00 25.30 ? 72  TYR   A CB  1 
ATOM   527  C  CG  . TYR   A 1 66  ? 7.821  -3.885  23.153 1.00 26.65 ? 72  TYR   A CG  1 
ATOM   528  C  CD1 . TYR   A 1 66  ? 7.050  -4.704  23.964 1.00 27.82 ? 72  TYR   A CD1 1 
ATOM   529  C  CD2 . TYR   A 1 66  ? 8.574  -2.885  23.759 1.00 27.50 ? 72  TYR   A CD2 1 
ATOM   530  C  CE1 . TYR   A 1 66  ? 7.048  -4.551  25.352 1.00 28.89 ? 72  TYR   A CE1 1 
ATOM   531  C  CE2 . TYR   A 1 66  ? 8.574  -2.715  25.144 1.00 28.86 ? 72  TYR   A CE2 1 
ATOM   532  C  CZ  . TYR   A 1 66  ? 7.817  -3.558  25.937 1.00 30.35 ? 72  TYR   A CZ  1 
ATOM   533  O  OH  . TYR   A 1 66  ? 7.845  -3.441  27.320 1.00 32.20 ? 72  TYR   A OH  1 
ATOM   534  N  N   . PRO   A 1 67  ? 7.432  -6.219  19.213 1.00 24.75 ? 73  PRO   A N   1 
ATOM   535  C  CA  . PRO   A 1 67  ? 6.893  -6.275  17.836 1.00 24.72 ? 73  PRO   A CA  1 
ATOM   536  C  C   . PRO   A 1 67  ? 5.767  -5.223  17.680 1.00 26.01 ? 73  PRO   A C   1 
ATOM   537  O  O   . PRO   A 1 67  ? 4.890  -5.116  18.550 1.00 26.63 ? 73  PRO   A O   1 
ATOM   538  C  CB  . PRO   A 1 67  ? 6.348  -7.713  17.721 1.00 25.97 ? 73  PRO   A CB  1 
ATOM   539  C  CG  . PRO   A 1 67  ? 5.979  -8.086  19.146 1.00 27.35 ? 73  PRO   A CG  1 
ATOM   540  C  CD  . PRO   A 1 67  ? 6.952  -7.347  20.056 1.00 25.19 ? 73  PRO   A CD  1 
ATOM   541  N  N   . VAL   A 1 68  ? 5.796  -4.438  16.593 1.00 24.57 ? 74  VAL   A N   1 
ATOM   542  C  CA  . VAL   A 1 68  ? 4.789  -3.401  16.378 1.00 24.89 ? 74  VAL   A CA  1 
ATOM   543  C  C   . VAL   A 1 68  ? 4.346  -3.291  14.921 1.00 24.36 ? 74  VAL   A C   1 
ATOM   544  O  O   . VAL   A 1 68  ? 5.115  -3.627  13.995 1.00 24.18 ? 74  VAL   A O   1 
ATOM   545  C  CB  . VAL   A 1 68  ? 5.357  -2.011  16.813 1.00 26.12 ? 74  VAL   A CB  1 
ATOM   546  C  CG1 . VAL   A 1 68  ? 5.376  -1.869  18.322 1.00 27.34 ? 74  VAL   A CG1 1 
ATOM   547  C  CG2 . VAL   A 1 68  ? 6.735  -1.724  16.203 1.00 25.98 ? 74  VAL   A CG2 1 
ATOM   548  N  N   . SER   A 1 69  ? 3.119  -2.739  14.738 1.00 23.10 ? 75  SER   A N   1 
ATOM   549  C  CA  . SER   A 1 69  ? 2.597  -2.294  13.448 1.00 24.11 ? 75  SER   A CA  1 
ATOM   550  C  C   . SER   A 1 69  ? 2.806  -0.774  13.493 1.00 23.52 ? 75  SER   A C   1 
ATOM   551  O  O   . SER   A 1 69  ? 2.568  -0.156  14.529 1.00 24.17 ? 75  SER   A O   1 
ATOM   552  C  CB  . SER   A 1 69  ? 1.099  -2.556  13.312 1.00 27.55 ? 75  SER   A CB  1 
ATOM   553  O  OG  . SER   A 1 69  ? 0.888  -3.955  13.267 1.00 35.67 ? 75  SER   A OG  1 
ATOM   554  N  N   . PHE   A 1 70  ? 3.272  -0.186  12.406 1.00 22.22 ? 76  PHE   A N   1 
ATOM   555  C  CA  . PHE   A 1 70  ? 3.522  1.270   12.401 1.00 21.50 ? 76  PHE   A CA  1 
ATOM   556  C  C   . PHE   A 1 70  ? 2.974  1.924   11.133 1.00 23.29 ? 76  PHE   A C   1 
ATOM   557  O  O   . PHE   A 1 70  ? 2.861  1.264   10.103 1.00 23.87 ? 76  PHE   A O   1 
ATOM   558  C  CB  . PHE   A 1 70  ? 5.019  1.592   12.670 1.00 20.82 ? 76  PHE   A CB  1 
ATOM   559  C  CG  . PHE   A 1 70  ? 6.009  0.888   11.759 1.00 21.26 ? 76  PHE   A CG  1 
ATOM   560  C  CD1 . PHE   A 1 70  ? 6.484  -0.382  12.067 1.00 21.66 ? 76  PHE   A CD1 1 
ATOM   561  C  CD2 . PHE   A 1 70  ? 6.424  1.473   10.564 1.00 22.90 ? 76  PHE   A CD2 1 
ATOM   562  C  CE1 . PHE   A 1 70  ? 7.361  -1.048  11.199 1.00 22.24 ? 76  PHE   A CE1 1 
ATOM   563  C  CE2 . PHE   A 1 70  ? 7.291  0.805   9.703  1.00 22.88 ? 76  PHE   A CE2 1 
ATOM   564  C  CZ  . PHE   A 1 70  ? 7.753  -0.457  10.021 1.00 21.59 ? 76  PHE   A CZ  1 
ATOM   565  N  N   . SER   A 1 71  ? 2.601  3.229   11.212 1.00 23.43 ? 77  SER   A N   1 
ATOM   566  C  CA  . SER   A 1 71  ? 2.017  3.941   10.077 1.00 22.72 ? 77  SER   A CA  1 
ATOM   567  C  C   . SER   A 1 71  ? 3.059  4.347   9.021  1.00 23.60 ? 77  SER   A C   1 
ATOM   568  O  O   . SER   A 1 71  ? 4.252  4.264   9.283  1.00 24.70 ? 77  SER   A O   1 
ATOM   569  C  CB  . SER   A 1 71  ? 1.258  5.184   10.575 1.00 23.50 ? 77  SER   A CB  1 
ATOM   570  O  OG  . SER   A 1 71  ? 2.160  6.059   11.237 1.00 25.50 ? 77  SER   A OG  1 
ATOM   571  N  N   . LYS   A 1 72  ? 2.618  4.764   7.817  1.00 23.92 ? 78  LYS   A N   1 
ATOM   572  C  CA  . LYS   A 1 72  ? 3.557  5.187   6.773  1.00 25.94 ? 78  LYS   A CA  1 
ATOM   573  C  C   . LYS   A 1 72  ? 4.191  6.544   7.124  1.00 26.28 ? 78  LYS   A C   1 
ATOM   574  O  O   . LYS   A 1 72  ? 3.569  7.357   7.810  1.00 27.27 ? 78  LYS   A O   1 
ATOM   575  C  CB  . LYS   A 1 72  ? 2.847  5.224   5.388  1.00 30.15 ? 78  LYS   A CB  1 
ATOM   576  C  CG  . LYS   A 1 72  ? 2.666  3.797   4.860  1.00 37.43 ? 78  LYS   A CG  1 
ATOM   577  C  CD  . LYS   A 1 72  ? 2.277  3.672   3.398  1.00 44.30 ? 78  LYS   A CD  1 
ATOM   578  C  CE  . LYS   A 1 72  ? 2.584  2.264   2.915  1.00 48.51 ? 78  LYS   A CE  1 
ATOM   579  N  NZ  . LYS   A 1 72  ? 2.103  2.027   1.521  1.00 51.83 ? 78  LYS   A NZ  1 
ATOM   580  N  N   . PRO   A 1 73  ? 5.437  6.793   6.696  1.00 26.48 ? 79  PRO   A N   1 
ATOM   581  C  CA  . PRO   A 1 73  ? 6.090  8.081   7.050  1.00 26.41 ? 79  PRO   A CA  1 
ATOM   582  C  C   . PRO   A 1 73  ? 5.252  9.283   6.586  1.00 27.10 ? 79  PRO   A C   1 
ATOM   583  O  O   . PRO   A 1 73  ? 4.772  9.322   5.432  1.00 28.07 ? 79  PRO   A O   1 
ATOM   584  C  CB  . PRO   A 1 73  ? 7.455  8.009   6.342  1.00 28.08 ? 79  PRO   A CB  1 
ATOM   585  C  CG  . PRO   A 1 73  ? 7.689  6.489   6.098  1.00 29.43 ? 79  PRO   A CG  1 
ATOM   586  C  CD  . PRO   A 1 73  ? 6.305  5.922   5.878  1.00 26.64 ? 79  PRO   A CD  1 
ATOM   587  N  N   . SER   A 1 74  ? 4.972  10.201  7.510  1.00 26.51 ? 80  SER   A N   1 
ATOM   588  C  CA  . SER   A 1 74  ? 4.082  11.320  7.198  1.00 28.14 ? 80  SER   A CA  1 
ATOM   589  C  C   . SER   A 1 74  ? 4.406  12.567  8.037  1.00 27.72 ? 80  SER   A C   1 
ATOM   590  O  O   . SER   A 1 74  ? 5.316  12.520  8.867  1.00 26.71 ? 80  SER   A O   1 
ATOM   591  C  CB  . SER   A 1 74  ? 2.623  10.877  7.367  1.00 31.46 ? 80  SER   A CB  1 
ATOM   592  O  OG  . SER   A 1 74  ? 2.320  10.717  8.739  1.00 36.18 ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 3.677  13.677  7.816  1.00 27.88 ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 3.892  14.938  8.537  1.00 28.84 ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 2.935  14.935  9.741  1.00 28.40 ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 1.711  14.923  9.563  1.00 28.35 ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 3.537  16.056  7.534  1.00 30.22 ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 3.974  17.475  7.813  1.00 33.82 ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.504  17.594  7.831  1.00 33.60 ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 3.416  18.422  6.719  1.00 36.10 ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.490  14.896  10.962 1.00 27.69 ? 82  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 76  ? 2.728  14.755  12.195 1.00 29.17 ? 82  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 76  ? 3.104  15.829  13.190 1.00 31.06 ? 82  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 76  ? 4.286  16.100  13.369 1.00 30.89 ? 82  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 76  ? 3.019  13.342  12.756 1.00 30.44 ? 82  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 76  ? 2.474  12.255  11.801 1.00 31.37 ? 82  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 76  ? 2.499  13.171  14.208 1.00 31.14 ? 82  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 76  ? 2.700  10.819  12.259 1.00 33.13 ? 82  ILE   A CD1 1 
ATOM   609  N  N   . PHE   A 1 77  ? 2.093  16.445  13.837 1.00 32.41 ? 83  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 77  ? 2.311  17.486  14.834 1.00 33.51 ? 83  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 77  ? 2.989  16.923  16.069 1.00 32.70 ? 83  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 77  ? 2.559  15.909  16.622 1.00 33.13 ? 83  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 77  ? 0.971  18.100  15.243 1.00 35.51 ? 83  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 77  ? 1.115  19.199  16.267 1.00 38.57 ? 83  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 77  ? 1.422  20.486  15.882 1.00 39.86 ? 83  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 77  ? 0.963  18.934  17.617 1.00 40.60 ? 83  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 77  ? 1.546  21.502  16.827 1.00 41.25 ? 83  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 77  ? 1.096  19.948  18.560 1.00 41.95 ? 83  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 77  ? 1.405  21.219  18.158 1.00 41.32 ? 83  PHE   A CZ  1 
ATOM   620  N  N   . VAL   A 1 78  ? 4.045  17.598  16.524 1.00 31.10 ? 84  VAL   A N   1 
ATOM   621  C  CA  . VAL   A 1 78  ? 4.778  17.172  17.713 1.00 29.92 ? 84  VAL   A CA  1 
ATOM   622  C  C   . VAL   A 1 78  ? 4.766  18.354  18.693 1.00 30.23 ? 84  VAL   A C   1 
ATOM   623  O  O   . VAL   A 1 78  ? 5.196  19.455  18.339 1.00 29.78 ? 84  VAL   A O   1 
ATOM   624  C  CB  . VAL   A 1 78  ? 6.229  16.763  17.361 1.00 29.45 ? 84  VAL   A CB  1 
ATOM   625  C  CG1 . VAL   A 1 78  ? 7.022  16.439  18.635 1.00 30.02 ? 84  VAL   A CG1 1 
ATOM   626  C  CG2 . VAL   A 1 78  ? 6.245  15.578  16.396 1.00 28.94 ? 84  VAL   A CG2 1 
ATOM   627  N  N   . GLU   A 1 79  ? 4.300  18.113  19.917 1.00 30.66 ? 85  GLU   A N   1 
ATOM   628  C  CA  . GLU   A 1 79  ? 4.228  19.166  20.931 1.00 31.40 ? 85  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 79  ? 5.591  19.784  21.239 1.00 31.41 ? 85  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 79  ? 6.632  19.149  21.047 1.00 30.55 ? 85  GLU   A O   1 
ATOM   631  C  CB  . GLU   A 1 79  ? 3.644  18.598  22.219 1.00 34.85 ? 85  GLU   A CB  1 
ATOM   632  C  CG  . GLU   A 1 79  ? 2.221  18.134  22.038 1.00 44.16 ? 85  GLU   A CG  1 
ATOM   633  C  CD  . GLU   A 1 79  ? 1.443  18.130  23.332 1.00 53.78 ? 85  GLU   A CD  1 
ATOM   634  O  OE1 . GLU   A 1 79  ? 0.806  17.096  23.639 1.00 54.08 ? 85  GLU   A OE1 1 
ATOM   635  O  OE2 . GLU   A 1 79  ? 1.480  19.159  24.046 1.00 59.85 ? 85  GLU   A OE2 1 
ATOM   636  N  N   . ALA   A 1 80  ? 5.574  21.027  21.755 1.00 31.58 ? 86  ALA   A N   1 
ATOM   637  C  CA  . ALA   A 1 80  ? 6.792  21.720  22.152 1.00 31.88 ? 86  ALA   A CA  1 
ATOM   638  C  C   . ALA   A 1 80  ? 7.520  20.934  23.245 1.00 31.43 ? 86  ALA   A C   1 
ATOM   639  O  O   . ALA   A 1 80  ? 6.881  20.297  24.099 1.00 31.44 ? 86  ALA   A O   1 
ATOM   640  C  CB  . ALA   A 1 80  ? 6.453  23.127  22.655 1.00 31.93 ? 86  ALA   A CB  1 
ATOM   641  N  N   . SER   A 1 81  ? 8.860  20.968  23.196 1.00 30.38 ? 87  SER   A N   1 
ATOM   642  C  CA  . SER   A 1 81  ? 9.738  20.328  24.175 1.00 30.22 ? 87  SER   A CA  1 
ATOM   643  C  C   . SER   A 1 81  ? 10.941 21.275  24.453 1.00 31.46 ? 87  SER   A C   1 
ATOM   644  O  O   . SER   A 1 81  ? 10.979 22.401  23.928 1.00 32.43 ? 87  SER   A O   1 
ATOM   645  C  CB  . SER   A 1 81  ? 10.241 18.990  23.623 1.00 29.60 ? 87  SER   A CB  1 
ATOM   646  O  OG  . SER   A 1 81  ? 11.150 19.199  22.550 1.00 29.33 ? 87  SER   A OG  1 
ATOM   647  N  N   . GLU   A 1 82  ? 11.927 20.823  25.263 1.00 32.09 ? 88  GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 82  ? 13.122 21.654  25.482 1.00 33.25 ? 88  GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 82  ? 14.025 21.698  24.218 1.00 32.80 ? 88  GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 82  ? 14.887 22.565  24.136 1.00 33.60 ? 88  GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 82  ? 13.912 21.203  26.727 1.00 37.12 ? 88  GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 82  ? 14.480 19.808  26.620 1.00 46.76 ? 88  GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 82  ? 15.077 19.214  27.883 1.00 58.11 ? 88  GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 82  ? 14.392 18.398  28.544 1.00 61.28 ? 88  GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 82  ? 16.243 19.547  28.197 1.00 60.48 ? 88  GLU   A OE2 1 
ATOM   656  N  N   . TYR   A 1 83  ? 13.752 20.847  23.197 1.00 31.09 ? 89  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 83  ? 14.553 20.729  21.974 1.00 29.87 ? 89  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 83  ? 13.988 21.407  20.750 1.00 29.32 ? 89  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 83  ? 14.748 21.865  19.887 1.00 29.54 ? 89  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 83  ? 14.778 19.245  21.678 1.00 29.98 ? 89  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 83  ? 15.492 18.558  22.818 1.00 31.40 ? 89  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 83  ? 16.852 18.741  23.021 1.00 33.00 ? 89  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 83  ? 14.805 17.736  23.700 1.00 32.94 ? 89  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 83  ? 17.515 18.116  24.066 1.00 34.44 ? 89  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 83  ? 15.462 17.083  24.734 1.00 34.19 ? 89  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 83  ? 16.818 17.277  24.916 1.00 36.27 ? 89  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 83  ? 17.490 16.617  25.917 1.00 40.19 ? 89  TYR   A OH  1 
ATOM   668  N  N   . TYR   A 1 84  ? 12.666 21.435  20.627 1.00 28.72 ? 90  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 84  ? 12.019 22.081  19.490 1.00 28.62 ? 90  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 84  ? 10.755 22.799  19.950 1.00 30.60 ? 90  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 84  ? 10.048 22.292  20.821 1.00 30.83 ? 90  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 84  ? 11.566 21.041  18.436 1.00 27.36 ? 90  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 84  ? 12.664 20.195  17.842 1.00 25.64 ? 90  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 84  ? 13.445 20.667  16.788 1.00 26.06 ? 90  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 84  ? 12.916 18.917  18.318 1.00 25.96 ? 90  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 84  ? 14.456 19.888  16.234 1.00 26.66 ? 90  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 84  ? 13.904 18.113  17.747 1.00 25.75 ? 90  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 84  ? 14.654 18.594  16.690 1.00 26.05 ? 90  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 84  ? 15.646 17.825  16.141 1.00 26.49 ? 90  TYR   A OH  1 
ATOM   680  N  N   . PRO   A 1 85  ? 10.362 23.889  19.263 1.00 31.30 ? 91  PRO   A N   1 
ATOM   681  C  CA  . PRO   A 1 85  ? 9.031  24.451  19.523 1.00 32.23 ? 91  PRO   A CA  1 
ATOM   682  C  C   . PRO   A 1 85  ? 7.968  23.499  18.918 1.00 32.26 ? 91  PRO   A C   1 
ATOM   683  O  O   . PRO   A 1 85  ? 8.304  22.542  18.177 1.00 31.80 ? 91  PRO   A O   1 
ATOM   684  C  CB  . PRO   A 1 85  ? 9.072  25.804  18.791 1.00 33.54 ? 91  PRO   A CB  1 
ATOM   685  C  CG  . PRO   A 1 85  ? 10.017 25.599  17.667 1.00 34.16 ? 91  PRO   A CG  1 
ATOM   686  C  CD  . PRO   A 1 85  ? 11.060 24.600  18.166 1.00 31.95 ? 91  PRO   A CD  1 
ATOM   687  N  N   . ALA   A 1 86  ? 6.672  23.754  19.194 1.00 32.75 ? 92  ALA   A N   1 
ATOM   688  C  CA  . ALA   A 1 86  ? 5.585  22.962  18.602 1.00 33.96 ? 92  ALA   A CA  1 
ATOM   689  C  C   . ALA   A 1 86  ? 5.677  23.096  17.067 1.00 33.99 ? 92  ALA   A C   1 
ATOM   690  O  O   . ALA   A 1 86  ? 5.911  24.207  16.574 1.00 34.37 ? 92  ALA   A O   1 
ATOM   691  C  CB  . ALA   A 1 86  ? 4.244  23.458  19.107 1.00 34.96 ? 92  ALA   A CB  1 
ATOM   692  N  N   . ARG   A 1 87  ? 5.677  21.955  16.336 1.00 32.37 ? 93  ARG   A N   1 
ATOM   693  C  CA  . ARG   A 1 87  ? 5.863  21.980  14.879 1.00 31.67 ? 93  ARG   A CA  1 
ATOM   694  C  C   . ARG   A 1 87  ? 5.371  20.664  14.249 1.00 32.23 ? 93  ARG   A C   1 
ATOM   695  O  O   . ARG   A 1 87  ? 5.130  19.715  14.976 1.00 32.29 ? 93  ARG   A O   1 
ATOM   696  C  CB  . ARG   A 1 87  ? 7.378  22.129  14.575 1.00 32.13 ? 93  ARG   A CB  1 
ATOM   697  C  CG  . ARG   A 1 87  ? 8.176  20.814  14.784 1.00 32.59 ? 93  ARG   A CG  1 
ATOM   698  C  CD  . ARG   A 1 87  ? 9.605  21.014  15.198 1.00 32.39 ? 93  ARG   A CD  1 
ATOM   699  N  NE  . ARG   A 1 87  ? 10.522 19.976  14.715 1.00 31.93 ? 93  ARG   A NE  1 
ATOM   700  C  CZ  . ARG   A 1 87  ? 10.666 18.770  15.261 1.00 32.11 ? 93  ARG   A CZ  1 
ATOM   701  N  NH1 . ARG   A 1 87  ? 9.873  18.382  16.268 1.00 29.99 ? 93  ARG   A NH1 1 
ATOM   702  N  NH2 . ARG   A 1 87  ? 11.582 17.930  14.792 1.00 27.85 ? 93  ARG   A NH2 1 
ATOM   703  N  N   . TYR   A 1 88  ? 5.347  20.580  12.900 1.00 32.45 ? 94  TYR   A N   1 
ATOM   704  C  CA  . TYR   A 1 88  ? 5.086  19.303  12.248 1.00 33.13 ? 94  TYR   A CA  1 
ATOM   705  C  C   . TYR   A 1 88  ? 6.440  18.679  11.989 1.00 30.63 ? 94  TYR   A C   1 
ATOM   706  O  O   . TYR   A 1 88  ? 7.311  19.323  11.401 1.00 30.49 ? 94  TYR   A O   1 
ATOM   707  C  CB  . TYR   A 1 88  ? 4.455  19.490  10.867 1.00 35.83 ? 94  TYR   A CB  1 
ATOM   708  C  CG  . TYR   A 1 88  ? 3.026  19.950  10.927 1.00 40.19 ? 94  TYR   A CG  1 
ATOM   709  C  CD1 . TYR   A 1 88  ? 1.997  19.054  11.172 1.00 42.30 ? 94  TYR   A CD1 1 
ATOM   710  C  CD2 . TYR   A 1 88  ? 2.700  21.285  10.747 1.00 42.63 ? 94  TYR   A CD2 1 
ATOM   711  C  CE1 . TYR   A 1 88  ? 0.671  19.472  11.208 1.00 44.74 ? 94  TYR   A CE1 1 
ATOM   712  C  CE2 . TYR   A 1 88  ? 1.382  21.715  10.789 1.00 44.75 ? 94  TYR   A CE2 1 
ATOM   713  C  CZ  . TYR   A 1 88  ? 0.369  20.807  11.026 1.00 46.50 ? 94  TYR   A CZ  1 
ATOM   714  O  OH  . TYR   A 1 88  ? -0.934 21.247  11.056 1.00 50.01 ? 94  TYR   A OH  1 
ATOM   715  N  N   . GLN   A 1 89  ? 6.618  17.414  12.383 1.00 27.98 ? 95  GLN   A N   1 
ATOM   716  C  CA  . GLN   A 1 89  ? 7.844  16.681  12.045 1.00 26.60 ? 95  GLN   A CA  1 
ATOM   717  C  C   . GLN   A 1 89  ? 7.515  15.802  10.817 1.00 25.56 ? 95  GLN   A C   1 
ATOM   718  O  O   . GLN   A 1 89  ? 6.481  15.136  10.815 1.00 25.47 ? 95  GLN   A O   1 
ATOM   719  C  CB  . GLN   A 1 89  ? 8.306  15.819  13.234 1.00 27.23 ? 95  GLN   A CB  1 
ATOM   720  C  CG  . GLN   A 1 89  ? 9.521  14.920  12.935 1.00 26.99 ? 95  GLN   A CG  1 
ATOM   721  C  CD  . GLN   A 1 89  ? 10.232 14.456  14.200 1.00 26.63 ? 95  GLN   A CD  1 
ATOM   722  O  OE1 . GLN   A 1 89  ? 10.427 15.226  15.157 1.00 24.74 ? 95  GLN   A OE1 1 
ATOM   723  N  NE2 . GLN   A 1 89  ? 10.671 13.199  14.209 1.00 25.81 ? 95  GLN   A NE2 1 
ATOM   724  N  N   . SER   A 1 90  ? 8.365  15.810  9.787  1.00 24.26 ? 96  SER   A N   1 
ATOM   725  C  CA  . SER   A 1 90  ? 8.104  15.020  8.582  1.00 24.53 ? 96  SER   A CA  1 
ATOM   726  C  C   . SER   A 1 90  ? 8.773  13.644  8.672  1.00 24.17 ? 96  SER   A C   1 
ATOM   727  O  O   . SER   A 1 90  ? 9.674  13.438  9.507  1.00 24.48 ? 96  SER   A O   1 
ATOM   728  C  CB  . SER   A 1 90  ? 8.615  15.757  7.342  1.00 25.84 ? 96  SER   A CB  1 
ATOM   729  O  OG  . SER   A 1 90  ? 10.009 16.015  7.470  1.00 27.59 ? 96  SER   A OG  1 
ATOM   730  N  N   . HIS   A 1 91  ? 8.329  12.710  7.807  1.00 23.69 ? 97  HIS   A N   1 
ATOM   731  C  CA  . HIS   A 1 91  ? 8.883  11.357  7.717  1.00 24.02 ? 97  HIS   A CA  1 
ATOM   732  C  C   . HIS   A 1 91  ? 8.775  10.595  9.058  1.00 24.07 ? 97  HIS   A C   1 
ATOM   733  O  O   . HIS   A 1 91  ? 9.634  9.768   9.374  1.00 23.81 ? 97  HIS   A O   1 
ATOM   734  C  CB  . HIS   A 1 91  ? 10.345 11.413  7.201  1.00 24.84 ? 97  HIS   A CB  1 
ATOM   735  C  CG  . HIS   A 1 91  ? 10.464 12.014  5.828  1.00 27.47 ? 97  HIS   A CG  1 
ATOM   736  N  ND1 . HIS   A 1 91  ? 10.486 11.224  4.706  1.00 30.78 ? 97  HIS   A ND1 1 
ATOM   737  C  CD2 . HIS   A 1 91  ? 10.559 13.317  5.457  1.00 28.48 ? 97  HIS   A CD2 1 
ATOM   738  C  CE1 . HIS   A 1 91  ? 10.618 12.059  3.676  1.00 31.36 ? 97  HIS   A CE1 1 
ATOM   739  N  NE2 . HIS   A 1 91  ? 10.688 13.335  4.084  1.00 30.60 ? 97  HIS   A NE2 1 
ATOM   740  N  N   . LEU   A 1 92  ? 7.716  10.888  9.832  1.00 23.48 ? 98  LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 92  ? 7.494  10.248  11.129 1.00 23.50 ? 98  LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 92  ? 6.448  9.132   11.011 1.00 22.88 ? 98  LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 92  ? 5.451  9.287   10.283 1.00 23.98 ? 98  LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 92  ? 7.047  11.319  12.145 1.00 23.55 ? 98  LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 92  ? 6.944  10.877  13.613 1.00 25.01 ? 98  LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 92  ? 8.328  10.576  14.164 1.00 24.75 ? 98  LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 92  ? 6.313  12.005  14.478 1.00 26.71 ? 98  LEU   A CD2 1 
ATOM   748  N  N   . MET   A 1 93  ? 6.677  8.009   11.721 1.00 22.26 ? 99  MET   A N   1 
ATOM   749  C  CA  . MET   A 1 93  ? 5.781  6.841   11.723 1.00 22.07 ? 99  MET   A CA  1 
ATOM   750  C  C   . MET   A 1 93  ? 5.392  6.549   13.147 1.00 23.04 ? 99  MET   A C   1 
ATOM   751  O  O   . MET   A 1 93  ? 6.263  6.588   14.015 1.00 23.69 ? 99  MET   A O   1 
ATOM   752  C  CB  . MET   A 1 93  ? 6.539  5.616   11.160 1.00 23.39 ? 99  MET   A CB  1 
ATOM   753  C  CG  . MET   A 1 93  ? 7.063  5.863   9.718  1.00 24.91 ? 99  MET   A CG  1 
ATOM   754  S  SD  . MET   A 1 93  ? 8.103  4.507   9.144  1.00 27.15 ? 99  MET   A SD  1 
ATOM   755  C  CE  . MET   A 1 93  ? 9.456  4.632   10.224 1.00 23.80 ? 99  MET   A CE  1 
ATOM   756  N  N   . LEU   A 1 94  ? 4.105  6.322   13.422 1.00 22.59 ? 100 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 94  ? 3.671  6.037   14.789 1.00 22.28 ? 100 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 94  ? 3.267  4.574   14.944 1.00 23.51 ? 100 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 94  ? 2.732  3.936   14.017 1.00 23.88 ? 100 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 94  ? 2.443  6.908   15.233 1.00 22.88 ? 100 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 94  ? 2.594  8.416   15.157 1.00 25.60 ? 100 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 94  ? 1.355  9.127   15.766 1.00 27.51 ? 100 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 94  ? 3.846  8.867   15.881 1.00 26.88 ? 100 LEU   A CD2 1 
ATOM   764  N  N   . ALA   A 1 95  ? 3.447  4.090   16.158 1.00 23.96 ? 101 ALA   A N   1 
ATOM   765  C  CA  . ALA   A 1 95  ? 3.012  2.761   16.600 1.00 23.40 ? 101 ALA   A CA  1 
ATOM   766  C  C   . ALA   A 1 95  ? 2.403  2.907   18.000 1.00 24.17 ? 101 ALA   A C   1 
ATOM   767  O  O   . ALA   A 1 95  ? 2.718  3.861   18.738 1.00 25.14 ? 101 ALA   A O   1 
ATOM   768  C  CB  . ALA   A 1 95  ? 4.206  1.806   16.677 1.00 24.20 ? 101 ALA   A CB  1 
ATOM   769  N  N   . VAL   A 1 96  ? 1.544  1.947   18.366 1.00 23.62 ? 102 VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 96  ? 0.988  1.890   19.709 1.00 23.54 ? 102 VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 96  ? 2.056  1.124   20.508 1.00 24.85 ? 102 VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 96  ? 2.366  -0.039  20.211 1.00 25.19 ? 102 VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 96  ? -0.391 1.167   19.711 1.00 25.23 ? 102 VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 96  ? -0.864 0.903   21.142 1.00 26.42 ? 102 VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 96  ? -1.430 2.003   18.951 1.00 24.92 ? 102 VAL   A CG2 1 
ATOM   776  N  N   . GLY   A 1 97  ? 2.634  1.790   21.488 1.00 25.72 ? 103 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 97  ? 3.704  1.196   22.288 1.00 27.53 ? 103 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 97  ? 4.277  2.187   23.283 1.00 28.23 ? 103 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 97  ? 3.958  3.389   23.253 1.00 28.19 ? 103 GLY   A O   1 
ATOM   780  N  N   . HIS   A 1 98  ? 5.154  1.691   24.158 1.00 28.04 ? 104 HIS   A N   1 
ATOM   781  C  CA  . HIS   A 1 98  ? 5.769  2.542   25.161 1.00 28.43 ? 104 HIS   A CA  1 
ATOM   782  C  C   . HIS   A 1 98  ? 7.041  3.282   24.705 1.00 28.24 ? 104 HIS   A C   1 
ATOM   783  O  O   . HIS   A 1 98  ? 7.960  2.721   24.105 1.00 28.08 ? 104 HIS   A O   1 
ATOM   784  C  CB  . HIS   A 1 98  ? 6.046  1.744   26.448 1.00 29.16 ? 104 HIS   A CB  1 
ATOM   785  C  CG  . HIS   A 1 98  ? 6.618  2.586   27.541 1.00 30.71 ? 104 HIS   A CG  1 
ATOM   786  N  ND1 . HIS   A 1 98  ? 5.824  3.476   28.252 1.00 32.92 ? 104 HIS   A ND1 1 
ATOM   787  C  CD2 . HIS   A 1 98  ? 7.906  2.754   27.921 1.00 31.68 ? 104 HIS   A CD2 1 
ATOM   788  C  CE1 . HIS   A 1 98  ? 6.649  4.125   29.059 1.00 33.37 ? 104 HIS   A CE1 1 
ATOM   789  N  NE2 . HIS   A 1 98  ? 7.909  3.700   28.917 1.00 33.00 ? 104 HIS   A NE2 1 
ATOM   790  N  N   . SER   A 1 99  ? 7.126  4.547   25.078 1.00 28.33 ? 105 SER   A N   1 
ATOM   791  C  CA  . SER   A 1 99  ? 8.297  5.365   24.858 1.00 29.07 ? 105 SER   A CA  1 
ATOM   792  C  C   . SER   A 1 99  ? 8.277  6.490   25.905 1.00 30.17 ? 105 SER   A C   1 
ATOM   793  O  O   . SER   A 1 99  ? 7.232  7.087   26.119 1.00 31.92 ? 105 SER   A O   1 
ATOM   794  C  CB  . SER   A 1 99  ? 8.304  5.968   23.460 1.00 30.94 ? 105 SER   A CB  1 
ATOM   795  O  OG  . SER   A 1 99  ? 9.516  6.698   23.323 1.00 34.96 ? 105 SER   A OG  1 
ATOM   796  N  N   . GLU   A 1 100 ? 9.405  6.743   26.547 1.00 29.13 ? 106 GLU   A N   1 
ATOM   797  C  CA  . GLU   A 1 100 ? 9.468  7.878   27.499 1.00 30.97 ? 106 GLU   A CA  1 
ATOM   798  C  C   . GLU   A 1 100 ? 10.756 8.655   27.237 1.00 31.50 ? 106 GLU   A C   1 
ATOM   799  O  O   . GLU   A 1 100 ? 11.642 8.117   26.581 1.00 31.34 ? 106 GLU   A O   1 
ATOM   800  C  CB  . GLU   A 1 100 ? 9.340  7.386   28.944 1.00 33.29 ? 106 GLU   A CB  1 
ATOM   801  C  CG  . GLU   A 1 100 ? 10.388 6.393   29.379 1.00 41.01 ? 106 GLU   A CG  1 
ATOM   802  C  CD  . GLU   A 1 100 ? 10.115 5.889   30.785 1.00 38.60 ? 106 GLU   A CD  1 
ATOM   803  O  OE1 . GLU   A 1 100 ? 10.603 6.513   31.733 1.00 38.33 ? 106 GLU   A OE1 1 
ATOM   804  O  OE2 . GLU   A 1 100 ? 9.395  4.894   30.922 1.00 37.17 ? 106 GLU   A OE2 1 
ATOM   805  N  N   . PRO   A 1 101 ? 10.888 9.906   27.733 1.00 32.46 ? 107 PRO   A N   1 
ATOM   806  C  CA  . PRO   A 1 101 ? 12.152 10.637  27.581 1.00 33.01 ? 107 PRO   A CA  1 
ATOM   807  C  C   . PRO   A 1 101 ? 13.347 9.756   27.964 1.00 32.42 ? 107 PRO   A C   1 
ATOM   808  O  O   . PRO   A 1 101 ? 13.318 9.109   29.020 1.00 32.73 ? 107 PRO   A O   1 
ATOM   809  C  CB  . PRO   A 1 101 ? 11.992 11.812  28.560 1.00 33.84 ? 107 PRO   A CB  1 
ATOM   810  C  CG  . PRO   A 1 101 ? 10.493 12.041  28.603 1.00 34.31 ? 107 PRO   A CG  1 
ATOM   811  C  CD  . PRO   A 1 101 ? 9.924  10.646  28.578 1.00 32.16 ? 107 PRO   A CD  1 
ATOM   812  N  N   . GLY   A 1 102 ? 14.312 9.642   27.054 1.00 31.13 ? 108 GLY   A N   1 
ATOM   813  C  CA  . GLY   A 1 102 ? 15.464 8.763   27.214 1.00 30.18 ? 108 GLY   A CA  1 
ATOM   814  C  C   . GLY   A 1 102 ? 15.479 7.606   26.215 1.00 29.63 ? 108 GLY   A C   1 
ATOM   815  O  O   . GLY   A 1 102 ? 16.529 6.983   25.994 1.00 30.03 ? 108 GLY   A O   1 
ATOM   816  N  N   . ASP   A 1 103 ? 14.309 7.319   25.576 1.00 27.45 ? 109 ASP   A N   1 
ATOM   817  C  CA  . ASP   A 1 103 ? 14.134 6.213   24.629 1.00 26.25 ? 109 ASP   A CA  1 
ATOM   818  C  C   . ASP   A 1 103 ? 14.522 6.557   23.179 1.00 24.50 ? 109 ASP   A C   1 
ATOM   819  O  O   . ASP   A 1 103 ? 14.657 5.640   22.344 1.00 23.99 ? 109 ASP   A O   1 
ATOM   820  C  CB  . ASP   A 1 103 ? 12.697 5.655   24.664 1.00 27.32 ? 109 ASP   A CB  1 
ATOM   821  C  CG  . ASP   A 1 103 ? 12.432 4.722   25.829 1.00 28.35 ? 109 ASP   A CG  1 
ATOM   822  O  OD1 . ASP   A 1 103 ? 13.380 4.041   26.268 1.00 27.84 ? 109 ASP   A OD1 1 
ATOM   823  O  OD2 . ASP   A 1 103 ? 11.283 4.680   26.295 1.00 28.09 ? 109 ASP   A OD2 1 
ATOM   824  N  N   . CYS   A 1 104 ? 14.758 7.859   22.868 1.00 24.33 ? 110 CYS   A N   1 
ATOM   825  C  CA  . CYS   A 1 104 ? 15.157 8.200   21.477 1.00 24.95 ? 110 CYS   A CA  1 
ATOM   826  C  C   . CYS   A 1 104 ? 16.428 7.466   21.069 1.00 24.83 ? 110 CYS   A C   1 
ATOM   827  O  O   . CYS   A 1 104 ? 17.334 7.272   21.894 1.00 25.24 ? 110 CYS   A O   1 
ATOM   828  C  CB  . CYS   A 1 104 ? 15.315 9.704   21.285 1.00 26.96 ? 110 CYS   A CB  1 
ATOM   829  S  SG  . CYS   A 1 104 ? 13.775 10.639  21.480 1.00 29.26 ? 110 CYS   A SG  1 
ATOM   830  N  N   . GLY   A 1 105 ? 16.509 7.091   19.812 1.00 23.61 ? 111 GLY   A N   1 
ATOM   831  C  CA  . GLY   A 1 105 ? 17.688 6.402   19.309 1.00 24.78 ? 111 GLY   A CA  1 
ATOM   832  C  C   . GLY   A 1 105 ? 17.534 4.895   19.208 1.00 25.29 ? 111 GLY   A C   1 
ATOM   833  O  O   . GLY   A 1 105 ? 18.344 4.243   18.540 1.00 26.30 ? 111 GLY   A O   1 
ATOM   834  N  N   . GLY   A 1 106 ? 16.534 4.313   19.890 1.00 24.08 ? 112 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 106 ? 16.290 2.870   19.789 1.00 23.44 ? 112 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 106 ? 15.954 2.477   18.346 1.00 23.49 ? 112 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 106 ? 15.225 3.196   17.664 1.00 23.00 ? 112 GLY   A O   1 
ATOM   838  N  N   . ILE   A 1 107 ? 16.532 1.373   17.839 1.00 23.19 ? 113 ILE   A N   1 
ATOM   839  C  CA  . ILE   A 1 107 ? 16.280 1.002   16.437 1.00 24.08 ? 113 ILE   A CA  1 
ATOM   840  C  C   . ILE   A 1 107 ? 14.949 0.277   16.224 1.00 23.05 ? 113 ILE   A C   1 
ATOM   841  O  O   . ILE   A 1 107 ? 14.550 -0.576  17.045 1.00 23.35 ? 113 ILE   A O   1 
ATOM   842  C  CB  . ILE   A 1 107 ? 17.493 0.186   15.894 1.00 26.95 ? 113 ILE   A CB  1 
ATOM   843  C  CG1 . ILE   A 1 107 ? 18.620 1.159   15.467 1.00 29.56 ? 113 ILE   A CG1 1 
ATOM   844  C  CG2 . ILE   A 1 107 ? 17.108 -0.743  14.703 1.00 28.15 ? 113 ILE   A CG2 1 
ATOM   845  C  CD1 . ILE   A 1 107 ? 19.945 0.487   15.217 1.00 32.89 ? 113 ILE   A CD1 1 
ATOM   846  N  N   . LEU   A 1 108 ? 14.288 0.611   15.105 1.00 21.63 ? 114 LEU   A N   1 
ATOM   847  C  CA  . LEU   A 1 108 ? 13.101 -0.094  14.587 1.00 21.04 ? 114 LEU   A CA  1 
ATOM   848  C  C   . LEU   A 1 108 ? 13.602 -0.905  13.365 1.00 21.38 ? 114 LEU   A C   1 
ATOM   849  O  O   . LEU   A 1 108 ? 14.234 -0.335  12.480 1.00 21.42 ? 114 LEU   A O   1 
ATOM   850  C  CB  . LEU   A 1 108 ? 11.977 0.863   14.168 1.00 20.88 ? 114 LEU   A CB  1 
ATOM   851  C  CG  . LEU   A 1 108 ? 10.825 0.217   13.361 1.00 21.85 ? 114 LEU   A CG  1 
ATOM   852  C  CD1 . LEU   A 1 108 ? 9.932  -0.683  14.289 1.00 22.19 ? 114 LEU   A CD1 1 
ATOM   853  C  CD2 . LEU   A 1 108 ? 9.955  1.340   12.707 1.00 22.88 ? 114 LEU   A CD2 1 
ATOM   854  N  N   . ARG   A 1 109 ? 13.418 -2.235  13.386 1.00 21.24 ? 115 ARG   A N   1 
ATOM   855  C  CA  . ARG   A 1 109 ? 13.932 -3.103  12.314 1.00 22.51 ? 115 ARG   A CA  1 
ATOM   856  C  C   . ARG   A 1 109 ? 12.832 -4.009  11.727 1.00 22.97 ? 115 ARG   A C   1 
ATOM   857  O  O   . ARG   A 1 109 ? 11.904 -4.385  12.432 1.00 22.58 ? 115 ARG   A O   1 
ATOM   858  C  CB  . ARG   A 1 109 ? 15.042 -3.952  12.968 1.00 26.07 ? 115 ARG   A CB  1 
ATOM   859  C  CG  . ARG   A 1 109 ? 15.516 -5.184  12.229 1.00 36.17 ? 115 ARG   A CG  1 
ATOM   860  C  CD  . ARG   A 1 109 ? 16.508 -5.991  13.094 1.00 42.71 ? 115 ARG   A CD  1 
ATOM   861  N  NE  . ARG   A 1 109 ? 17.587 -5.144  13.618 1.00 47.81 ? 115 ARG   A NE  1 
ATOM   862  C  CZ  . ARG   A 1 109 ? 18.614 -4.704  12.896 1.00 50.74 ? 115 ARG   A CZ  1 
ATOM   863  N  NH1 . ARG   A 1 109 ? 18.729 -5.045  11.616 1.00 50.73 ? 115 ARG   A NH1 1 
ATOM   864  N  NH2 . ARG   A 1 109 ? 19.533 -3.925  13.449 1.00 50.72 ? 115 ARG   A NH2 1 
ATOM   865  N  N   . CYS   A 1 110 ? 12.945 -4.345  10.441 1.00 23.56 ? 116 CYS   A N   1 
ATOM   866  C  CA  . CYS   A 1 110 ? 12.046 -5.311  9.808  1.00 24.54 ? 116 CYS   A CA  1 
ATOM   867  C  C   . CYS   A 1 110 ? 12.956 -6.442  9.211  1.00 26.90 ? 116 CYS   A C   1 
ATOM   868  O  O   . CYS   A 1 110 ? 14.168 -6.442  9.442  1.00 27.75 ? 116 CYS   A O   1 
ATOM   869  C  CB  . CYS   A 1 110 ? 11.242 -4.623  8.712  1.00 24.64 ? 116 CYS   A CB  1 
ATOM   870  S  SG  . CYS   A 1 110 ? 12.297 -4.023  7.363  1.00 25.15 ? 116 CYS   A SG  1 
ATOM   871  N  N   . GLN   A 1 111 ? 12.382 -7.386  8.424  1.00 28.09 ? 117 GLN   A N   1 
ATOM   872  C  CA  . GLN   A 1 111 ? 13.214 -8.425  7.800  1.00 30.14 ? 117 GLN   A CA  1 
ATOM   873  C  C   . GLN   A 1 111 ? 14.296 -7.872  6.841  1.00 31.67 ? 117 GLN   A C   1 
ATOM   874  O  O   . GLN   A 1 111 ? 15.246 -8.599  6.524  1.00 33.63 ? 117 GLN   A O   1 
ATOM   875  C  CB  . GLN   A 1 111 ? 12.337 -9.423  7.052  1.00 32.95 ? 117 GLN   A CB  1 
ATOM   876  C  CG  . GLN   A 1 111 ? 11.635 -8.794  5.866  1.00 36.68 ? 117 GLN   A CG  1 
ATOM   877  C  CD  . GLN   A 1 111 ? 10.703 -9.779  5.213  1.00 44.15 ? 117 GLN   A CD  1 
ATOM   878  O  OE1 . GLN   A 1 111 ? 9.483  -9.757  5.438  1.00 45.79 ? 117 GLN   A OE1 1 
ATOM   879  N  NE2 . GLN   A 1 111 ? 11.263 -10.649 4.384  1.00 44.43 ? 117 GLN   A NE2 1 
ATOM   880  N  N   . HIS   A 1 112 ? 14.161 -6.620  6.360  1.00 30.46 ? 118 HIS   A N   1 
ATOM   881  C  CA  . HIS   A 1 112 ? 15.119 -6.045  5.402  1.00 30.06 ? 118 HIS   A CA  1 
ATOM   882  C  C   . HIS   A 1 112 ? 16.276 -5.231  6.025  1.00 30.28 ? 118 HIS   A C   1 
ATOM   883  O  O   . HIS   A 1 112 ? 17.238 -4.864  5.315  1.00 32.24 ? 118 HIS   A O   1 
ATOM   884  C  CB  . HIS   A 1 112 ? 14.373 -5.195  4.359  1.00 30.41 ? 118 HIS   A CB  1 
ATOM   885  C  CG  . HIS   A 1 112 ? 13.243 -5.941  3.695  1.00 31.48 ? 118 HIS   A CG  1 
ATOM   886  N  ND1 . HIS   A 1 112 ? 11.937 -5.735  4.063  1.00 32.61 ? 118 HIS   A ND1 1 
ATOM   887  C  CD2 . HIS   A 1 112 ? 13.276 -6.841  2.675  1.00 32.17 ? 118 HIS   A CD2 1 
ATOM   888  C  CE1 . HIS   A 1 112 ? 11.205 -6.523  3.291  1.00 33.01 ? 118 HIS   A CE1 1 
ATOM   889  N  NE2 . HIS   A 1 112 ? 11.977 -7.233  2.446  1.00 32.86 ? 118 HIS   A NE2 1 
ATOM   890  N  N   . GLY   A 1 113 ? 16.168 -4.930  7.321  1.00 27.81 ? 119 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 113 ? 17.192 -4.158  8.011  1.00 27.44 ? 119 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 113 ? 16.594 -3.063  8.877  1.00 26.16 ? 119 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 113 ? 15.479 -3.199  9.390  1.00 25.10 ? 119 GLY   A O   1 
ATOM   894  N  N   . VAL   A 1 114 ? 17.358 -1.985  9.059  1.00 25.87 ? 120 VAL   A N   1 
ATOM   895  C  CA  . VAL   A 1 114 ? 16.953 -0.839  9.873  1.00 25.62 ? 120 VAL   A CA  1 
ATOM   896  C  C   . VAL   A 1 114 ? 15.970 0.019   9.126  1.00 25.56 ? 120 VAL   A C   1 
ATOM   897  O  O   . VAL   A 1 114 ? 16.252 0.455   8.013  1.00 25.99 ? 120 VAL   A O   1 
ATOM   898  C  CB  . VAL   A 1 114 ? 18.173 0.001   10.305 1.00 26.88 ? 120 VAL   A CB  1 
ATOM   899  C  CG1 . VAL   A 1 114 ? 17.736 1.270   11.050 1.00 28.09 ? 120 VAL   A CG1 1 
ATOM   900  C  CG2 . VAL   A 1 114 ? 19.134 -0.841  11.143 1.00 27.57 ? 120 VAL   A CG2 1 
ATOM   901  N  N   . VAL   A 1 115 ? 14.830 0.314   9.761  1.00 24.03 ? 121 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 115 ? 13.777 1.150   9.194  1.00 23.24 ? 121 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 115 ? 13.909 2.593   9.710  1.00 23.34 ? 121 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 115 ? 13.639 3.551   8.979  1.00 24.16 ? 121 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 115 ? 12.397 0.576   9.626  1.00 23.37 ? 121 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 115 ? 11.242 1.479   9.184  1.00 23.14 ? 121 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 115 ? 12.195 -0.852  9.129  1.00 23.79 ? 121 VAL   A CG2 1 
ATOM   908  N  N   . GLY   A 1 116 ? 14.215 2.734   11.005 1.00 21.86 ? 122 GLY   A N   1 
ATOM   909  C  CA  . GLY   A 1 116 ? 14.296 4.069   11.596 1.00 22.50 ? 122 GLY   A CA  1 
ATOM   910  C  C   . GLY   A 1 116 ? 14.683 4.029   13.063 1.00 22.10 ? 122 GLY   A C   1 
ATOM   911  O  O   . GLY   A 1 116 ? 15.132 2.995   13.558 1.00 22.62 ? 122 GLY   A O   1 
ATOM   912  N  N   . ILE   A 1 117 ? 14.599 5.174   13.725 1.00 22.05 ? 123 ILE   A N   1 
ATOM   913  C  CA  . ILE   A 1 117 ? 14.970 5.240   15.159 1.00 21.94 ? 123 ILE   A CA  1 
ATOM   914  C  C   . ILE   A 1 117 ? 13.858 5.944   15.925 1.00 22.52 ? 123 ILE   A C   1 
ATOM   915  O  O   . ILE   A 1 117 ? 13.228 6.854   15.391 1.00 22.93 ? 123 ILE   A O   1 
ATOM   916  C  CB  . ILE   A 1 117 ? 16.316 6.004   15.400 1.00 24.08 ? 123 ILE   A CB  1 
ATOM   917  C  CG1 . ILE   A 1 117 ? 16.345 7.314   14.616 1.00 26.04 ? 123 ILE   A CG1 1 
ATOM   918  C  CG2 . ILE   A 1 117 ? 17.544 5.131   15.076 1.00 25.84 ? 123 ILE   A CG2 1 
ATOM   919  C  CD1 . ILE   A 1 117 ? 17.566 8.211   14.980 1.00 28.69 ? 123 ILE   A CD1 1 
ATOM   920  N  N   . VAL   A 1 118 ? 13.675 5.610   17.216 1.00 21.12 ? 124 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 118 ? 12.684 6.305   18.046 1.00 20.00 ? 124 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 118 ? 12.985 7.819   18.068 1.00 20.97 ? 124 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 118 ? 14.134 8.229   18.285 1.00 21.66 ? 124 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 118 ? 12.679 5.756   19.492 1.00 19.73 ? 124 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 118 ? 11.795 6.600   20.406 1.00 20.34 ? 124 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 118 ? 12.227 4.281   19.505 1.00 20.12 ? 124 VAL   A CG2 1 
ATOM   927  N  N   . SER   A 1 119 ? 11.950 8.626   17.877 1.00 21.15 ? 125 SER   A N   1 
ATOM   928  C  CA  . SER   A 1 119 ? 12.116 10.081  17.893 1.00 22.58 ? 125 SER   A CA  1 
ATOM   929  C  C   . SER   A 1 119 ? 11.095 10.769  18.789 1.00 24.39 ? 125 SER   A C   1 
ATOM   930  O  O   . SER   A 1 119 ? 11.387 11.834  19.294 1.00 24.56 ? 125 SER   A O   1 
ATOM   931  C  CB  . SER   A 1 119 ? 12.066 10.621  16.458 1.00 24.07 ? 125 SER   A CB  1 
ATOM   932  O  OG  . SER   A 1 119 ? 12.218 12.033  16.424 1.00 25.33 ? 125 SER   A OG  1 
ATOM   933  N  N   . THR   A 1 120 ? 9.902  10.190  18.972 1.00 24.55 ? 126 THR   A N   1 
ATOM   934  C  CA  . THR   A 1 120 ? 8.845  10.808  19.808 1.00 24.82 ? 126 THR   A CA  1 
ATOM   935  C  C   . THR   A 1 120 ? 8.119  9.744   20.670 1.00 25.49 ? 126 THR   A C   1 
ATOM   936  O  O   . THR   A 1 120 ? 8.237  8.540   20.415 1.00 24.82 ? 126 THR   A O   1 
ATOM   937  C  CB  . THR   A 1 120 ? 7.783  11.565  18.915 1.00 27.21 ? 126 THR   A CB  1 
ATOM   938  O  OG1 . THR   A 1 120 ? 6.894  10.626  18.297 1.00 29.06 ? 126 THR   A OG1 1 
ATOM   939  C  CG2 . THR   A 1 120 ? 8.371  12.498  17.892 1.00 27.39 ? 126 THR   A CG2 1 
ATOM   940  N  N   . GLY   A 1 121 ? 7.322  10.195  21.632 1.00 27.04 ? 127 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? 6.545  9.278   22.449 1.00 29.88 ? 127 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? 5.503  9.974   23.276 1.00 32.06 ? 127 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? 5.251  11.161  23.081 1.00 31.78 ? 127 GLY   A O   1 
ATOM   944  N  N   . GLY   A 1 122 ? 4.963  9.229   24.236 1.00 34.80 ? 128 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 122 ? 3.951  9.718   25.175 1.00 36.24 ? 128 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 122 ? 2.553  9.347   24.745 1.00 36.92 ? 128 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 122 ? 2.327  9.103   23.560 1.00 37.18 ? 128 GLY   A O   1 
ATOM   948  N  N   . ASN   A 1 123 ? 1.597  9.340   25.699 1.00 37.22 ? 129 ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 123 ? 0.200  8.997   25.436 1.00 37.89 ? 129 ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 123 ? 0.017  7.556   24.896 1.00 36.58 ? 129 ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 123 ? -0.972 7.277   24.214 1.00 37.44 ? 129 ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 123 ? -0.449 10.024  24.486 1.00 40.46 ? 129 ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 123 ? -0.519 11.436  25.029 1.00 46.23 ? 129 ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 123 ? -0.531 11.667  26.253 1.00 47.26 ? 129 ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 123 ? -0.603 12.416  24.123 1.00 48.09 ? 129 ASN   A ND2 1 
ATOM   956  N  N   . GLY   A 1 124 ? 0.946  6.649   25.209 1.00 34.15 ? 130 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? 0.862  5.272   24.733 1.00 31.62 ? 130 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 1.235  5.080   23.265 1.00 28.90 ? 130 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? 0.978  4.014   22.686 1.00 29.13 ? 130 GLY   A O   1 
ATOM   960  N  N   . LEU   A 1 125 ? 1.901  6.076   22.675 1.00 27.90 ? 131 LEU   A N   1 
ATOM   961  C  CA  . LEU   A 1 125 ? 2.336  6.035   21.277 1.00 27.51 ? 131 LEU   A CA  1 
ATOM   962  C  C   . LEU   A 1 125 ? 3.860  6.191   21.200 1.00 27.86 ? 131 LEU   A C   1 
ATOM   963  O  O   . LEU   A 1 125 ? 4.456  6.807   22.082 1.00 30.57 ? 131 LEU   A O   1 
ATOM   964  C  CB  . LEU   A 1 125 ? 1.687  7.201   20.522 1.00 27.59 ? 131 LEU   A CB  1 
ATOM   965  C  CG  . LEU   A 1 125 ? 0.161  7.109   20.349 1.00 27.74 ? 131 LEU   A CG  1 
ATOM   966  C  CD1 . LEU   A 1 125 ? -0.409 8.463   19.939 1.00 30.03 ? 131 LEU   A CD1 1 
ATOM   967  C  CD2 . LEU   A 1 125 ? -0.220 6.030   19.353 1.00 27.12 ? 131 LEU   A CD2 1 
ATOM   968  N  N   . VAL   A 1 126 ? 4.494  5.614   20.176 1.00 24.70 ? 132 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 126 ? 5.927  5.772   19.978 1.00 24.21 ? 132 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 126 ? 6.093  6.176   18.524 1.00 23.54 ? 132 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 126 ? 5.399  5.634   17.658 1.00 23.88 ? 132 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 126 ? 6.751  4.497   20.317 1.00 24.44 ? 132 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 126 ? 6.136  3.258   19.686 1.00 26.12 ? 132 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 126 ? 8.232  4.662   19.907 1.00 24.63 ? 132 VAL   A CG2 1 
ATOM   975  N  N   . GLY   A 1 127 ? 6.917  7.193   18.272 1.00 22.09 ? 133 GLY   A N   1 
ATOM   976  C  CA  . GLY   A 1 127 ? 7.140  7.656   16.905 1.00 22.17 ? 133 GLY   A CA  1 
ATOM   977  C  C   . GLY   A 1 127 ? 8.558  7.398   16.454 1.00 22.09 ? 133 GLY   A C   1 
ATOM   978  O  O   . GLY   A 1 127 ? 9.485  7.565   17.241 1.00 22.42 ? 133 GLY   A O   1 
ATOM   979  N  N   . PHE   A 1 128 ? 8.727  7.000   15.195 1.00 21.28 ? 134 PHE   A N   1 
ATOM   980  C  CA  . PHE   A 1 128 ? 10.042 6.643   14.642 1.00 20.82 ? 134 PHE   A CA  1 
ATOM   981  C  C   . PHE   A 1 128 ? 10.367 7.541   13.456 1.00 21.65 ? 134 PHE   A C   1 
ATOM   982  O  O   . PHE   A 1 128 ? 9.536  7.719   12.568 1.00 21.19 ? 134 PHE   A O   1 
ATOM   983  C  CB  . PHE   A 1 128 ? 10.063 5.184   14.141 1.00 20.14 ? 134 PHE   A CB  1 
ATOM   984  C  CG  . PHE   A 1 128 ? 9.565  4.178   15.174 1.00 20.34 ? 134 PHE   A CG  1 
ATOM   985  C  CD1 . PHE   A 1 128 ? 10.425 3.654   16.126 1.00 20.58 ? 134 PHE   A CD1 1 
ATOM   986  C  CD2 . PHE   A 1 128 ? 8.251  3.728   15.157 1.00 21.38 ? 134 PHE   A CD2 1 
ATOM   987  C  CE1 . PHE   A 1 128 ? 9.954  2.748   17.098 1.00 21.29 ? 134 PHE   A CE1 1 
ATOM   988  C  CE2 . PHE   A 1 128 ? 7.786  2.816   16.112 1.00 22.02 ? 134 PHE   A CE2 1 
ATOM   989  C  CZ  . PHE   A 1 128 ? 8.638  2.342   17.089 1.00 21.16 ? 134 PHE   A CZ  1 
ATOM   990  N  N   . ALA   A 1 129 ? 11.591 8.029   13.419 1.00 21.16 ? 135 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 129 ? 12.063 8.822   12.290 1.00 21.95 ? 135 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 129 ? 12.488 7.845   11.208 1.00 21.92 ? 135 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 129 ? 13.416 7.079   11.434 1.00 22.28 ? 135 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 129 ? 13.258 9.677   12.719 1.00 22.02 ? 135 ALA   A CB  1 
ATOM   995  N  N   . ASP   A 1 130 ? 11.803 7.830   10.050 1.00 21.86 ? 136 ASP   A N   1 
ATOM   996  C  CA  . ASP   A 1 130 ? 12.165 6.893   8.963  1.00 22.69 ? 136 ASP   A CA  1 
ATOM   997  C  C   . ASP   A 1 130 ? 13.514 7.233   8.316  1.00 23.74 ? 136 ASP   A C   1 
ATOM   998  O  O   . ASP   A 1 130 ? 13.860 8.414   8.176  1.00 24.75 ? 136 ASP   A O   1 
ATOM   999  C  CB  . ASP   A 1 130 ? 11.085 6.955   7.868  1.00 26.10 ? 136 ASP   A CB  1 
ATOM   1000 C  CG  . ASP   A 1 130 ? 11.237 5.939   6.760  1.00 30.84 ? 136 ASP   A CG  1 
ATOM   1001 O  OD1 . ASP   A 1 130 ? 11.271 4.747   7.056  1.00 30.77 ? 136 ASP   A OD1 1 
ATOM   1002 O  OD2 . ASP   A 1 130 ? 11.313 6.348   5.586  1.00 35.18 ? 136 ASP   A OD2 1 
ATOM   1003 N  N   . VAL   A 1 131 ? 14.292 6.196   7.926  1.00 22.59 ? 137 VAL   A N   1 
ATOM   1004 C  CA  . VAL   A 1 131 ? 15.561 6.452   7.219  1.00 23.48 ? 137 VAL   A CA  1 
ATOM   1005 C  C   . VAL   A 1 131 ? 15.603 5.709   5.852  1.00 24.96 ? 137 VAL   A C   1 
ATOM   1006 O  O   . VAL   A 1 131 ? 16.601 5.805   5.155  1.00 27.09 ? 137 VAL   A O   1 
ATOM   1007 C  CB  . VAL   A 1 131 ? 16.818 6.085   8.051  1.00 23.61 ? 137 VAL   A CB  1 
ATOM   1008 C  CG1 . VAL   A 1 131 ? 16.874 6.884   9.355  1.00 23.90 ? 137 VAL   A CG1 1 
ATOM   1009 C  CG2 . VAL   A 1 131 ? 16.892 4.567   8.317  1.00 23.96 ? 137 VAL   A CG2 1 
ATOM   1010 N  N   . ARG   A 1 132 ? 14.535 4.964   5.477  1.00 24.18 ? 138 ARG   A N   1 
ATOM   1011 C  CA  . ARG   A 1 132 ? 14.486 4.135   4.269  1.00 24.62 ? 138 ARG   A CA  1 
ATOM   1012 C  C   . ARG   A 1 132 ? 14.566 4.916   2.966  1.00 26.92 ? 138 ARG   A C   1 
ATOM   1013 O  O   . ARG   A 1 132 ? 14.934 4.340   1.928  1.00 28.06 ? 138 ARG   A O   1 
ATOM   1014 C  CB  . ARG   A 1 132 ? 13.240 3.234   4.283  1.00 23.45 ? 138 ARG   A CB  1 
ATOM   1015 C  CG  . ARG   A 1 132 ? 13.254 2.229   5.421  1.00 23.88 ? 138 ARG   A CG  1 
ATOM   1016 C  CD  . ARG   A 1 132 ? 11.962 1.430   5.387  1.00 24.22 ? 138 ARG   A CD  1 
ATOM   1017 N  NE  . ARG   A 1 132 ? 10.836 2.249   5.827  1.00 25.25 ? 138 ARG   A NE  1 
ATOM   1018 C  CZ  . ARG   A 1 132 ? 9.587  1.803   5.932  1.00 27.12 ? 138 ARG   A CZ  1 
ATOM   1019 N  NH1 . ARG   A 1 132 ? 9.288  0.551   5.579  1.00 25.14 ? 138 ARG   A NH1 1 
ATOM   1020 N  NH2 . ARG   A 1 132 ? 8.622  2.609   6.382  1.00 25.85 ? 138 ARG   A NH2 1 
ATOM   1021 N  N   . ASP   A 1 133 ? 14.208 6.214   2.995  1.00 26.67 ? 139 ASP   A N   1 
ATOM   1022 C  CA  . ASP   A 1 133 ? 14.299 7.031   1.794  1.00 27.73 ? 139 ASP   A CA  1 
ATOM   1023 C  C   . ASP   A 1 133 ? 15.717 7.618   1.588  1.00 28.97 ? 139 ASP   A C   1 
ATOM   1024 O  O   . ASP   A 1 133 ? 15.968 8.198   0.541  1.00 29.49 ? 139 ASP   A O   1 
ATOM   1025 C  CB  . ASP   A 1 133 ? 13.260 8.162   1.817  1.00 30.11 ? 139 ASP   A CB  1 
ATOM   1026 C  CG  . ASP   A 1 133 ? 13.547 9.173   2.912  1.00 33.50 ? 139 ASP   A CG  1 
ATOM   1027 O  OD1 . ASP   A 1 133 ? 13.825 8.749   4.037  1.00 33.68 ? 139 ASP   A OD1 1 
ATOM   1028 O  OD2 . ASP   A 1 133 ? 13.516 10.396  2.626  1.00 34.50 ? 139 ASP   A OD2 1 
ATOM   1029 N  N   . LEU   A 1 134 ? 16.645 7.457   2.561  1.00 28.33 ? 140 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 134 ? 17.993 8.034   2.477  1.00 29.17 ? 140 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 134 ? 18.924 7.085   1.724  1.00 31.11 ? 140 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 134 ? 19.842 6.490   2.294  1.00 30.81 ? 140 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 134 ? 18.486 8.350   3.912  1.00 29.08 ? 140 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 134 ? 17.602 9.359   4.669  1.00 29.76 ? 140 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 134 ? 18.128 9.604   6.087  1.00 30.68 ? 140 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 134 ? 17.531 10.708  3.937  1.00 30.52 ? 140 LEU   A CD2 1 
ATOM   1037 N  N   . LEU   A 1 135 ? 18.640 6.922   0.408  1.00 31.26 ? 141 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 135 ? 19.332 5.945   -0.428 1.00 32.85 ? 141 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 135 ? 20.832 6.130   -0.482 1.00 34.52 ? 141 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 135 ? 21.568 5.147   -0.609 1.00 35.23 ? 141 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 135 ? 18.739 5.904   -1.845 1.00 33.32 ? 141 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 135 ? 17.211 5.786   -1.971 1.00 34.90 ? 141 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 135 ? 16.806 5.593   -3.419 1.00 35.69 ? 141 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 135 ? 16.635 4.663   -1.102 1.00 34.61 ? 141 LEU   A CD2 1 
ATOM   1045 N  N   . TRP   A 1 136 ? 21.286 7.385   -0.339 1.00 34.53 ? 142 TRP   A N   1 
ATOM   1046 C  CA  . TRP   A 1 136 ? 22.699 7.746   -0.360 1.00 35.02 ? 142 TRP   A CA  1 
ATOM   1047 C  C   . TRP   A 1 136 ? 23.485 7.137   0.813  1.00 35.95 ? 142 TRP   A C   1 
ATOM   1048 O  O   . TRP   A 1 136 ? 24.700 7.022   0.713  1.00 37.40 ? 142 TRP   A O   1 
ATOM   1049 C  CB  . TRP   A 1 136 ? 22.865 9.272   -0.420 1.00 34.19 ? 142 TRP   A CB  1 
ATOM   1050 C  CG  . TRP   A 1 136 ? 22.146 10.006  0.674  1.00 33.12 ? 142 TRP   A CG  1 
ATOM   1051 C  CD1 . TRP   A 1 136 ? 20.904 10.570  0.609  1.00 33.24 ? 142 TRP   A CD1 1 
ATOM   1052 C  CD2 . TRP   A 1 136 ? 22.674 10.341  1.960  1.00 32.21 ? 142 TRP   A CD2 1 
ATOM   1053 N  NE1 . TRP   A 1 136 ? 20.625 11.228  1.779  1.00 33.32 ? 142 TRP   A NE1 1 
ATOM   1054 C  CE2 . TRP   A 1 136 ? 21.687 11.080  2.639  1.00 32.55 ? 142 TRP   A CE2 1 
ATOM   1055 C  CE3 . TRP   A 1 136 ? 23.877 10.059  2.620  1.00 32.73 ? 142 TRP   A CE3 1 
ATOM   1056 C  CZ2 . TRP   A 1 136 ? 21.863 11.538  3.939  1.00 32.83 ? 142 TRP   A CZ2 1 
ATOM   1057 C  CZ3 . TRP   A 1 136 ? 24.046 10.514  3.913  1.00 33.15 ? 142 TRP   A CZ3 1 
ATOM   1058 C  CH2 . TRP   A 1 136 ? 23.050 11.247  4.553  1.00 32.92 ? 142 TRP   A CH2 1 
ATOM   1059 N  N   . LEU   A 1 137 ? 22.813 6.718   1.903  1.00 35.40 ? 143 LEU   A N   1 
ATOM   1060 C  CA  . LEU   A 1 137 ? 23.506 6.055   3.020  1.00 35.74 ? 143 LEU   A CA  1 
ATOM   1061 C  C   . LEU   A 1 137 ? 24.222 4.765   2.564  1.00 37.89 ? 143 LEU   A C   1 
ATOM   1062 O  O   . LEU   A 1 137 ? 25.155 4.319   3.238  1.00 37.32 ? 143 LEU   A O   1 
ATOM   1063 C  CB  . LEU   A 1 137 ? 22.523 5.698   4.158  1.00 34.45 ? 143 LEU   A CB  1 
ATOM   1064 C  CG  . LEU   A 1 137 ? 21.993 6.843   5.005  1.00 33.60 ? 143 LEU   A CG  1 
ATOM   1065 C  CD1 . LEU   A 1 137 ? 20.828 6.366   5.905  1.00 33.85 ? 143 LEU   A CD1 1 
ATOM   1066 C  CD2 . LEU   A 1 137 ? 23.100 7.435   5.882  1.00 33.03 ? 143 LEU   A CD2 1 
ATOM   1067 N  N   . ASP   A 1 138 ? 23.751 4.141   1.454  1.00 39.72 ? 144 ASP   A N   1 
ATOM   1068 C  CA  . ASP   A 1 138 ? 24.320 2.897   0.922  1.00 42.78 ? 144 ASP   A CA  1 
ATOM   1069 C  C   . ASP   A 1 138 ? 25.524 3.133   -0.000 1.00 46.33 ? 144 ASP   A C   1 
ATOM   1070 O  O   . ASP   A 1 138 ? 26.047 2.159   -0.535 1.00 47.36 ? 144 ASP   A O   1 
ATOM   1071 C  CB  . ASP   A 1 138 ? 23.269 2.108   0.120  1.00 43.76 ? 144 ASP   A CB  1 
ATOM   1072 C  CG  . ASP   A 1 138 ? 22.033 1.667   0.872  1.00 47.59 ? 144 ASP   A CG  1 
ATOM   1073 O  OD1 . ASP   A 1 138 ? 22.064 1.663   2.125  1.00 48.14 ? 144 ASP   A OD1 1 
ATOM   1074 O  OD2 . ASP   A 1 138 ? 21.025 1.340   0.210  1.00 49.19 ? 144 ASP   A OD2 1 
ATOM   1075 N  N   . GLU   A 1 139 ? 25.953 4.388   -0.217 1.00 48.29 ? 145 GLU   A N   1 
ATOM   1076 C  CA  . GLU   A 1 139 ? 27.083 4.646   -1.111 1.00 51.58 ? 145 GLU   A CA  1 
ATOM   1077 C  C   . GLU   A 1 139 ? 28.059 5.693   -0.584 1.00 54.15 ? 145 GLU   A C   1 
ATOM   1078 O  O   . GLU   A 1 139 ? 27.670 6.544   0.217  1.00 54.74 ? 145 GLU   A O   1 
ATOM   1079 C  CB  . GLU   A 1 139 ? 26.588 4.997   -2.521 1.00 54.58 ? 145 GLU   A CB  1 
ATOM   1080 C  CG  . GLU   A 1 139 ? 25.606 6.150   -2.562 1.00 60.63 ? 145 GLU   A CG  1 
ATOM   1081 C  CD  . GLU   A 1 139 ? 24.490 5.953   -3.568 1.00 69.94 ? 145 GLU   A CD  1 
ATOM   1082 O  OE1 . GLU   A 1 139 ? 24.332 6.822   -4.457 1.00 72.15 ? 145 GLU   A OE1 1 
ATOM   1083 O  OE2 . GLU   A 1 139 ? 23.775 4.928   -3.471 1.00 72.80 ? 145 GLU   A OE2 1 
ATOM   1084 N  N   . GLU   A 1 140 ? 29.331 5.621   -1.052 1.00 55.61 ? 146 GLU   A N   1 
ATOM   1085 C  CA  . GLU   A 1 140 ? 30.468 6.506   -0.746 1.00 57.62 ? 146 GLU   A CA  1 
ATOM   1086 C  C   . GLU   A 1 140 ? 30.459 7.117   0.668  1.00 59.20 ? 146 GLU   A C   1 
ATOM   1087 O  O   . GLU   A 1 140 ? 31.225 8.044   0.957  1.00 59.94 ? 146 GLU   A O   1 
ATOM   1088 C  CB  . GLU   A 1 140 ? 30.614 7.608   -1.809 1.00 60.42 ? 146 GLU   A CB  1 
ATOM   1089 C  CG  . GLU   A 1 140 ? 29.702 8.819   -1.667 1.00 65.80 ? 146 GLU   A CG  1 
ATOM   1090 C  CD  . GLU   A 1 140 ? 30.384 10.149  -1.945 1.00 73.49 ? 146 GLU   A CD  1 
ATOM   1091 O  OE1 . GLU   A 1 140 ? 29.786 11.201  -1.619 1.00 75.61 ? 146 GLU   A OE1 1 
ATOM   1092 O  OE2 . GLU   A 1 140 ? 31.519 10.144  -2.479 1.00 74.85 ? 146 GLU   A OE2 1 
HETATM 1093 N  N1  . A1B3X B 2 .   ? 10.258 14.556  22.434 1.00 29.65 ? 201 A1B3X A N1  1 
HETATM 1094 C  C4  . A1B3X B 2 .   ? 6.286  11.480  27.023 1.00 40.00 ? 201 A1B3X A C4  1 
HETATM 1095 C  C5  . A1B3X B 2 .   ? 6.212  12.799  27.423 1.00 39.64 ? 201 A1B3X A C5  1 
HETATM 1096 C  C6  . A1B3X B 2 .   ? 7.117  13.726  26.943 1.00 39.16 ? 201 A1B3X A C6  1 
HETATM 1097 C  C7  . A1B3X B 2 .   ? 8.100  13.328  26.046 1.00 37.83 ? 201 A1B3X A C7  1 
HETATM 1098 C  C8  . A1B3X B 2 .   ? 9.208  14.128  25.419 1.00 35.77 ? 201 A1B3X A C8  1 
HETATM 1099 C  C10 . A1B3X B 2 .   ? 9.524  13.559  22.967 1.00 31.29 ? 201 A1B3X A C10 1 
HETATM 1100 C  C13 . A1B3X B 2 .   ? 12.450 15.570  20.872 1.00 28.56 ? 201 A1B3X A C13 1 
HETATM 1101 C  C15 . A1B3X B 2 .   ? 10.998 15.395  18.816 1.00 27.49 ? 201 A1B3X A C15 1 
HETATM 1102 O  O2  . A1B3X B 2 .   ? 10.548 16.534  18.639 1.00 26.76 ? 201 A1B3X A O2  1 
HETATM 1103 N  N2  . A1B3X B 2 .   ? 11.281 14.560  17.828 1.00 26.98 ? 201 A1B3X A N2  1 
HETATM 1104 C  C14 . A1B3X B 2 .   ? 11.250 14.863  20.216 1.00 28.28 ? 201 A1B3X A C14 1 
HETATM 1105 C  C12 . A1B3X B 2 .   ? 12.650 15.101  22.314 1.00 28.65 ? 201 A1B3X A C12 1 
HETATM 1106 C  C11 . A1B3X B 2 .   ? 11.365 15.251  23.108 1.00 29.36 ? 201 A1B3X A C11 1 
HETATM 1107 C  C16 . A1B3X B 2 .   ? 9.995  15.044  21.076 1.00 28.82 ? 201 A1B3X A C16 1 
HETATM 1108 O  O1  . A1B3X B 2 .   ? 8.617  13.025  22.349 1.00 30.03 ? 201 A1B3X A O1  1 
HETATM 1109 C  C9  . A1B3X B 2 .   ? 9.835  13.147  24.411 1.00 34.16 ? 201 A1B3X A C9  1 
HETATM 1110 N  N   . A1B3X B 2 .   ? 9.254  11.836  24.740 1.00 36.22 ? 201 A1B3X A N   1 
HETATM 1111 C  C1  . A1B3X B 2 .   ? 9.799  10.686  24.232 1.00 37.08 ? 201 A1B3X A C1  1 
HETATM 1112 O  O   . A1B3X B 2 .   ? 10.785 10.721  23.488 1.00 38.58 ? 201 A1B3X A O   1 
HETATM 1113 C  C   . A1B3X B 2 .   ? 9.108  9.411   24.536 1.00 36.28 ? 201 A1B3X A C   1 
HETATM 1114 C  C2  . A1B3X B 2 .   ? 8.168  11.996  25.644 1.00 38.05 ? 201 A1B3X A C2  1 
HETATM 1115 C  C3  . A1B3X B 2 .   ? 7.261  11.063  26.127 1.00 39.35 ? 201 A1B3X A C3  1 
HETATM 1116 ZN ZN  . ZN    C 3 .   ? 11.142 -4.233  5.331  1.00 26.88 2 202 ZN    A ZN  1 
HETATM 1117 S  S   . DMS   D 4 .   ? 14.576 21.348  7.437  1.00 86.36 ? 203 DMS   A S   1 
HETATM 1118 O  O   . DMS   D 4 .   ? 13.898 21.849  8.683  1.00 86.24 ? 203 DMS   A O   1 
HETATM 1119 C  C1  . DMS   D 4 .   ? 13.337 21.285  6.108  1.00 86.31 ? 203 DMS   A C1  1 
HETATM 1120 C  C2  . DMS   D 4 .   ? 15.524 22.733  6.736  1.00 86.50 ? 203 DMS   A C2  1 
HETATM 1121 S  S   . DMS   E 4 .   ? 3.671  12.144  18.452 1.00 71.21 ? 204 DMS   A S   1 
HETATM 1122 O  O   . DMS   E 4 .   ? 3.846  13.548  18.942 1.00 71.00 ? 204 DMS   A O   1 
HETATM 1123 C  C1  . DMS   E 4 .   ? 1.895  11.791  18.348 1.00 71.33 ? 204 DMS   A C1  1 
HETATM 1124 C  C2  . DMS   E 4 .   ? 3.939  11.037  19.860 1.00 71.12 ? 204 DMS   A C2  1 
HETATM 1125 O  O   . HOH   F 5 .   ? 3.565  15.243  20.467 1.00 36.94 ? 301 HOH   A O   1 
HETATM 1126 O  O   . HOH   F 5 .   ? 26.578 8.655   -0.140 1.00 54.45 ? 302 HOH   A O   1 
HETATM 1127 O  O   . HOH   F 5 .   ? 10.485 8.509   4.603  1.00 33.11 ? 303 HOH   A O   1 
HETATM 1128 O  O   . HOH   F 5 .   ? 10.036 24.732  23.876 1.00 46.01 ? 304 HOH   A O   1 
HETATM 1129 O  O   . HOH   F 5 .   ? 5.121  21.039  25.870 1.00 54.69 ? 305 HOH   A O   1 
HETATM 1130 O  O   . HOH   F 5 .   ? 24.081 12.644  22.795 1.00 48.88 ? 306 HOH   A O   1 
HETATM 1131 O  O   . HOH   F 5 .   ? 8.497  -8.485  23.076 1.00 38.55 ? 307 HOH   A O   1 
HETATM 1132 O  O   . HOH   F 5 .   ? 19.334 0.046   27.172 1.00 41.03 ? 308 HOH   A O   1 
HETATM 1133 O  O   . HOH   F 5 .   ? 7.337  25.714  14.945 1.00 40.80 ? 309 HOH   A O   1 
HETATM 1134 O  O   . HOH   F 5 .   ? 22.440 -0.288  3.867  1.00 35.40 ? 310 HOH   A O   1 
HETATM 1135 O  O   . HOH   F 5 .   ? 23.349 9.267   -4.254 1.00 58.67 ? 311 HOH   A O   1 
HETATM 1136 O  O   . HOH   F 5 .   ? 1.862  8.275   9.802  1.00 40.20 ? 312 HOH   A O   1 
HETATM 1137 O  O   . HOH   F 5 .   ? 15.128 23.768  18.070 1.00 43.84 ? 313 HOH   A O   1 
HETATM 1138 O  O   . HOH   F 5 .   ? 20.088 9.377   18.950 1.00 27.87 ? 314 HOH   A O   1 
HETATM 1139 O  O   . HOH   F 5 .   ? 16.987 14.006  26.087 1.00 42.87 ? 315 HOH   A O   1 
HETATM 1140 O  O   . HOH   F 5 .   ? 0.254  14.631  17.017 1.00 35.08 ? 316 HOH   A O   1 
HETATM 1141 O  O   . HOH   F 5 .   ? 30.726 10.932  13.589 1.00 48.05 ? 317 HOH   A O   1 
HETATM 1142 O  O   . HOH   F 5 .   ? 18.384 19.896  5.378  1.00 52.27 ? 318 HOH   A O   1 
HETATM 1143 O  O   . HOH   F 5 .   ? 9.734  18.592  20.368 1.00 27.36 ? 319 HOH   A O   1 
HETATM 1144 O  O   . HOH   F 5 .   ? 23.821 22.838  8.955  1.00 39.09 ? 320 HOH   A O   1 
HETATM 1145 O  O   . HOH   F 5 .   ? 12.655 11.165  0.206  1.00 51.89 ? 321 HOH   A O   1 
HETATM 1146 O  O   . HOH   F 5 .   ? 6.860  -5.368  28.905 1.00 43.10 ? 322 HOH   A O   1 
HETATM 1147 O  O   . HOH   F 5 .   ? 10.975 17.766  5.633  1.00 59.48 ? 323 HOH   A O   1 
HETATM 1148 O  O   . HOH   F 5 .   ? 4.519  6.016   24.649 1.00 39.92 ? 324 HOH   A O   1 
HETATM 1149 O  O   . HOH   F 5 .   ? 4.038  -4.839  21.085 1.00 36.50 ? 325 HOH   A O   1 
HETATM 1150 O  O   . HOH   F 5 .   ? 15.372 24.366  26.074 1.00 43.00 ? 326 HOH   A O   1 
HETATM 1151 O  O   . HOH   F 5 .   ? 22.093 -4.319  12.444 1.00 51.50 ? 327 HOH   A O   1 
HETATM 1152 O  O   . HOH   F 5 .   ? 0.517  1.886   24.280 1.00 33.28 ? 328 HOH   A O   1 
HETATM 1153 O  O   . HOH   F 5 .   ? 18.178 -6.367  3.275  1.00 46.49 ? 329 HOH   A O   1 
HETATM 1154 O  O   . HOH   F 5 .   ? 10.096 5.236   3.443  1.00 31.63 ? 330 HOH   A O   1 
HETATM 1155 O  O   . HOH   F 5 .   ? 0.700  -0.156  16.484 1.00 23.51 ? 331 HOH   A O   1 
HETATM 1156 O  O   . HOH   F 5 .   ? 29.244 3.776   10.519 1.00 35.24 ? 332 HOH   A O   1 
HETATM 1157 O  O   . HOH   F 5 .   ? 27.753 3.715   2.709  1.00 51.03 ? 333 HOH   A O   1 
HETATM 1158 O  O   . HOH   F 5 .   ? 15.934 23.523  14.715 1.00 48.57 ? 334 HOH   A O   1 
HETATM 1159 O  O   . HOH   F 5 .   ? 8.092  19.833  18.366 1.00 28.14 ? 335 HOH   A O   1 
HETATM 1160 O  O   . HOH   F 5 .   ? 4.284  7.737   3.250  1.00 41.82 ? 336 HOH   A O   1 
HETATM 1161 O  O   . HOH   F 5 .   ? 19.843 -0.758  30.997 1.00 62.59 ? 337 HOH   A O   1 
HETATM 1162 O  O   . HOH   F 5 .   ? 18.085 0.753   29.479 1.00 45.52 ? 338 HOH   A O   1 
HETATM 1163 O  O   . HOH   F 5 .   ? 21.320 17.189  23.439 1.00 52.42 ? 339 HOH   A O   1 
HETATM 1164 O  O   . HOH   F 5 .   ? 10.034 4.789   33.802 1.00 36.65 ? 340 HOH   A O   1 
HETATM 1165 O  O   . HOH   F 5 .   ? 15.397 12.828  24.019 1.00 28.27 ? 341 HOH   A O   1 
HETATM 1166 O  O   . HOH   F 5 .   ? 14.861 2.944   23.057 1.00 23.72 ? 342 HOH   A O   1 
HETATM 1167 O  O   . HOH   F 5 .   ? 23.416 0.561   15.837 1.00 37.58 ? 343 HOH   A O   1 
HETATM 1168 O  O   . HOH   F 5 .   ? 26.079 4.721   19.726 1.00 47.17 ? 344 HOH   A O   1 
HETATM 1169 O  O   . HOH   F 5 .   ? 15.099 -7.874  26.568 1.00 55.55 ? 345 HOH   A O   1 
HETATM 1170 O  O   . HOH   F 5 .   ? 17.205 20.745  19.302 1.00 36.78 ? 346 HOH   A O   1 
HETATM 1171 O  O   . HOH   F 5 .   ? 5.643  8.018   28.203 1.00 37.88 ? 347 HOH   A O   1 
HETATM 1172 O  O   . HOH   F 5 .   ? 34.191 -2.543  10.318 1.00 50.28 ? 348 HOH   A O   1 
HETATM 1173 O  O   . HOH   F 5 .   ? 0.493  20.668  26.164 1.00 62.28 ? 349 HOH   A O   1 
HETATM 1174 O  O   . HOH   F 5 .   ? 17.723 21.670  9.313  1.00 37.76 ? 350 HOH   A O   1 
HETATM 1175 O  O   . HOH   F 5 .   ? 3.145  3.739   27.520 1.00 38.43 ? 351 HOH   A O   1 
HETATM 1176 O  O   . HOH   F 5 .   ? 12.031 21.707  12.821 1.00 34.12 ? 352 HOH   A O   1 
HETATM 1177 O  O   . HOH   F 5 .   ? 15.271 9.776   30.898 1.00 41.84 ? 353 HOH   A O   1 
HETATM 1178 O  O   . HOH   F 5 .   ? 20.457 23.820  10.546 1.00 50.69 ? 354 HOH   A O   1 
HETATM 1179 O  O   . HOH   F 5 .   ? 11.254 12.043  11.342 1.00 24.71 ? 355 HOH   A O   1 
HETATM 1180 O  O   . HOH   F 5 .   ? 11.620 2.479   33.375 1.00 28.84 ? 356 HOH   A O   1 
HETATM 1181 O  O   . HOH   F 5 .   ? 16.833 -7.230  9.909  1.00 58.04 ? 357 HOH   A O   1 
HETATM 1182 O  O   . HOH   F 5 .   ? 7.347  4.055   32.667 1.00 35.84 ? 358 HOH   A O   1 
HETATM 1183 O  O   . HOH   F 5 .   ? 1.694  14.817  22.237 1.00 37.45 ? 359 HOH   A O   1 
HETATM 1184 O  O   . HOH   F 5 .   ? 8.668  -3.774  0.199  1.00 36.22 ? 360 HOH   A O   1 
HETATM 1185 O  O   . HOH   F 5 .   ? 8.782  2.965   2.626  1.00 31.31 ? 361 HOH   A O   1 
HETATM 1186 O  O   . HOH   F 5 .   ? 6.177  14.429  22.142 1.00 34.44 ? 362 HOH   A O   1 
HETATM 1187 O  O   . HOH   F 5 .   ? 11.508 9.153   31.186 1.00 38.25 ? 363 HOH   A O   1 
HETATM 1188 O  O   . HOH   F 5 .   ? 22.149 -2.365  15.236 1.00 51.71 ? 364 HOH   A O   1 
HETATM 1189 O  O   . HOH   F 5 .   ? 30.871 -3.141  7.186  1.00 45.88 ? 365 HOH   A O   1 
HETATM 1190 O  O   . HOH   F 5 .   ? 21.022 -4.543  10.020 1.00 45.61 ? 366 HOH   A O   1 
HETATM 1191 O  O   . HOH   F 5 .   ? 31.260 19.105  8.522  1.00 44.11 ? 367 HOH   A O   1 
HETATM 1192 O  O   . HOH   F 5 .   ? 17.805 2.890   22.951 1.00 29.73 ? 368 HOH   A O   1 
HETATM 1193 O  O   . HOH   F 5 .   ? 7.286  17.659  25.081 1.00 43.06 ? 369 HOH   A O   1 
HETATM 1194 O  O   . HOH   F 5 .   ? 13.039 10.926  9.243  1.00 24.13 ? 370 HOH   A O   1 
HETATM 1195 O  O   . HOH   F 5 .   ? 0.875  -2.436  19.812 1.00 46.57 ? 371 HOH   A O   1 
HETATM 1196 O  O   . HOH   F 5 .   ? 14.418 14.932  3.539  1.00 35.86 ? 372 HOH   A O   1 
HETATM 1197 O  O   . HOH   F 5 .   ? 20.485 2.358   18.242 1.00 39.82 ? 373 HOH   A O   1 
HETATM 1198 O  O   . HOH   F 5 .   ? 3.955  0.717   30.398 1.00 55.21 ? 374 HOH   A O   1 
HETATM 1199 O  O   . HOH   F 5 .   ? 13.432 -8.159  24.385 1.00 31.58 ? 375 HOH   A O   1 
HETATM 1200 O  O   . HOH   F 5 .   ? 30.014 5.133   3.551  1.00 49.49 ? 376 HOH   A O   1 
HETATM 1201 O  O   . HOH   F 5 .   ? 27.193 -1.154  6.710  1.00 45.48 ? 377 HOH   A O   1 
HETATM 1202 O  O   . HOH   F 5 .   ? 18.017 23.397  16.698 1.00 53.50 ? 378 HOH   A O   1 
HETATM 1203 O  O   . HOH   F 5 .   ? 2.046  13.620  5.422  1.00 39.13 ? 379 HOH   A O   1 
HETATM 1204 O  O   . HOH   F 5 .   ? 17.935 19.407  16.976 1.00 30.60 ? 380 HOH   A O   1 
HETATM 1205 O  O   . HOH   F 5 .   ? 24.481 8.049   20.152 1.00 49.41 ? 381 HOH   A O   1 
HETATM 1206 O  O   . HOH   F 5 .   ? 6.482  13.305  5.647  1.00 31.50 ? 382 HOH   A O   1 
HETATM 1207 O  O   . HOH   F 5 .   ? 18.431 13.130  1.498  1.00 46.91 ? 383 HOH   A O   1 
HETATM 1208 O  O   . HOH   F 5 .   ? 18.628 0.038   19.368 1.00 37.89 ? 384 HOH   A O   1 
HETATM 1209 O  O   . HOH   F 5 .   ? 4.171  -4.843  6.168  1.00 38.83 ? 385 HOH   A O   1 
HETATM 1210 O  O   . HOH   F 5 .   ? 18.596 4.900   26.184 1.00 40.54 ? 386 HOH   A O   1 
HETATM 1211 O  O   . HOH   F 5 .   ? 18.547 9.599   25.597 1.00 36.24 ? 387 HOH   A O   1 
HETATM 1212 O  O   . HOH   F 5 .   ? 5.488  -1.208  24.001 1.00 28.72 ? 388 HOH   A O   1 
HETATM 1213 O  O   . HOH   F 5 .   ? 36.735 0.025   9.306  1.00 47.62 ? 389 HOH   A O   1 
HETATM 1214 O  O   . HOH   F 5 .   ? 32.621 15.120  7.285  1.00 58.30 ? 390 HOH   A O   1 
HETATM 1215 O  O   . HOH   F 5 .   ? 24.006 17.200  2.452  1.00 49.97 ? 391 HOH   A O   1 
HETATM 1216 O  O   . HOH   F 5 .   ? 23.810 17.292  22.688 1.00 53.04 ? 392 HOH   A O   1 
HETATM 1217 O  O   . HOH   F 5 .   ? 2.522  10.195  28.361 1.00 51.58 ? 393 HOH   A O   1 
HETATM 1218 O  O   . HOH   F 5 .   ? 31.000 3.433   12.362 1.00 42.71 ? 394 HOH   A O   1 
HETATM 1219 O  O   . HOH   F 5 .   ? 3.023  22.298  22.524 1.00 37.86 ? 395 HOH   A O   1 
HETATM 1220 O  O   . HOH   F 5 .   ? 15.700 10.245  24.518 1.00 29.63 ? 396 HOH   A O   1 
HETATM 1221 O  O   . HOH   F 5 .   ? 31.856 2.817   3.255  1.00 52.40 ? 397 HOH   A O   1 
HETATM 1222 O  O   . HOH   F 5 .   ? 18.601 -4.566  27.333 1.00 62.18 ? 398 HOH   A O   1 
HETATM 1223 O  O   . HOH   F 5 .   ? 28.467 -1.285  13.497 1.00 44.21 ? 399 HOH   A O   1 
HETATM 1224 O  O   . HOH   F 5 .   ? 0.095  3.672   6.720  1.00 51.49 ? 400 HOH   A O   1 
HETATM 1225 O  O   . HOH   F 5 .   ? 6.208  26.232  20.750 1.00 42.37 ? 401 HOH   A O   1 
HETATM 1226 O  O   . HOH   F 5 .   ? 7.355  16.704  22.567 1.00 34.66 ? 402 HOH   A O   1 
HETATM 1227 O  O   . HOH   F 5 .   ? 15.247 -3.450  17.366 1.00 35.45 ? 403 HOH   A O   1 
HETATM 1228 O  O   . HOH   F 5 .   ? 22.718 19.252  19.239 1.00 52.13 ? 404 HOH   A O   1 
HETATM 1229 O  O   . HOH   F 5 .   ? -0.677 15.534  13.211 1.00 34.22 ? 405 HOH   A O   1 
HETATM 1230 O  O   . HOH   F 5 .   ? 21.586 -1.828  33.454 1.00 61.84 ? 406 HOH   A O   1 
HETATM 1231 O  O   . HOH   F 5 .   ? 23.784 3.025   19.616 1.00 42.13 ? 407 HOH   A O   1 
HETATM 1232 O  O   . HOH   F 5 .   ? 5.938  22.991  11.221 1.00 39.72 ? 408 HOH   A O   1 
HETATM 1233 O  O   . HOH   F 5 .   ? 1.406  -2.710  17.213 1.00 32.94 ? 409 HOH   A O   1 
HETATM 1234 O  O   . HOH   F 5 .   ? 20.819 3.227   -2.804 1.00 54.84 ? 410 HOH   A O   1 
HETATM 1235 O  O   . HOH   F 5 .   ? 23.182 -6.438  3.704  1.00 75.15 ? 411 HOH   A O   1 
HETATM 1236 O  O   . HOH   F 5 .   ? 31.326 9.578   5.322  1.00 42.43 ? 412 HOH   A O   1 
HETATM 1237 O  O   . HOH   F 5 .   ? 17.654 -4.705  16.609 1.00 51.25 ? 413 HOH   A O   1 
HETATM 1238 O  O   . HOH   F 5 .   ? 32.158 -0.106  13.611 1.00 49.41 ? 414 HOH   A O   1 
HETATM 1239 O  O   . HOH   F 5 .   ? 9.376  -7.439  8.017  1.00 47.62 ? 415 HOH   A O   1 
HETATM 1240 O  O   . HOH   F 5 .   ? 15.753 -4.011  1.236  1.00 33.25 ? 416 HOH   A O   1 
HETATM 1241 O  O   . HOH   F 5 .   ? 3.827  13.768  23.769 1.00 61.69 ? 417 HOH   A O   1 
HETATM 1242 O  O   . HOH   F 5 .   ? 6.897  -7.910  14.153 1.00 38.12 ? 418 HOH   A O   1 
HETATM 1243 O  O   . HOH   F 5 .   ? 21.825 9.247   21.050 1.00 35.50 ? 419 HOH   A O   1 
HETATM 1244 O  O   . HOH   F 5 .   ? 11.451 -4.440  -0.641 1.00 53.15 ? 420 HOH   A O   1 
HETATM 1245 O  O   . HOH   F 5 .   ? 4.096  -2.114  21.687 1.00 43.36 ? 421 HOH   A O   1 
HETATM 1246 O  O   . HOH   F 5 .   ? 22.357 19.335  5.604  1.00 36.67 ? 422 HOH   A O   1 
HETATM 1247 O  O   . HOH   F 5 .   ? 11.486 18.174  26.835 1.00 50.66 ? 423 HOH   A O   1 
HETATM 1248 O  O   . HOH   F 5 .   ? 3.586  -3.611  3.445  1.00 59.55 ? 424 HOH   A O   1 
HETATM 1249 O  O   . HOH   F 5 .   ? 6.903  -3.825  -1.814 1.00 53.00 ? 425 HOH   A O   1 
HETATM 1250 O  O   . HOH   F 5 .   ? 8.036  7.987   32.775 1.00 44.49 ? 426 HOH   A O   1 
HETATM 1251 O  O   . HOH   F 5 .   ? 26.059 -1.843  14.637 1.00 53.35 ? 427 HOH   A O   1 
HETATM 1252 O  O   . HOH   F 5 .   ? 30.519 6.667   17.894 1.00 71.32 ? 428 HOH   A O   1 
HETATM 1253 O  O   . HOH   F 5 .   ? 6.165  3.056   3.083  1.00 43.29 ? 429 HOH   A O   1 
HETATM 1254 O  O   . HOH   F 5 .   ? 34.649 5.626   13.992 1.00 58.51 ? 430 HOH   A O   1 
HETATM 1255 O  O   . HOH   F 5 .   ? 28.322 17.862  22.933 1.00 49.71 ? 431 HOH   A O   1 
HETATM 1256 O  O   . HOH   F 5 .   ? 5.029  -1.305  28.763 1.00 61.23 ? 432 HOH   A O   1 
HETATM 1257 O  O   . HOH   F 5 .   ? 36.650 17.076  13.095 1.00 51.88 ? 433 HOH   A O   1 
HETATM 1258 O  O   . HOH   F 5 .   ? 31.372 12.570  15.306 1.00 49.26 ? 434 HOH   A O   1 
HETATM 1259 O  O   . HOH   F 5 .   ? 7.069  11.381  4.205  1.00 55.28 ? 435 HOH   A O   1 
HETATM 1260 O  O   . HOH   F 5 .   ? 2.806  -6.309  14.732 1.00 53.31 ? 436 HOH   A O   1 
HETATM 1261 O  O   . HOH   F 5 .   ? 17.967 21.545  25.096 1.00 62.94 ? 437 HOH   A O   1 
HETATM 1262 O  O   . HOH   F 5 .   ? 7.611  -5.124  2.527  1.00 43.72 ? 438 HOH   A O   1 
HETATM 1263 O  O   . HOH   F 5 .   ? 19.314 9.441   -2.190 1.00 48.15 ? 439 HOH   A O   1 
HETATM 1264 O  O   . HOH   F 5 .   ? 19.529 -7.036  6.622  1.00 57.18 ? 440 HOH   A O   1 
HETATM 1265 O  O   . HOH   F 5 .   ? -0.940 6.471   28.110 1.00 75.93 ? 441 HOH   A O   1 
HETATM 1266 O  O   . HOH   F 5 .   ? 26.347 10.821  -1.253 1.00 64.59 ? 442 HOH   A O   1 
HETATM 1267 O  O   . HOH   F 5 .   ? 30.221 11.544  18.377 1.00 59.94 ? 443 HOH   A O   1 
HETATM 1268 O  O   . HOH   F 5 .   ? 18.940 8.246   28.235 1.00 51.71 ? 444 HOH   A O   1 
HETATM 1269 O  O   . HOH   F 5 .   ? 28.968 10.098  20.627 1.00 72.08 ? 445 HOH   A O   1 
HETATM 1270 O  O   . HOH   F 5 .   ? 8.766  19.892  6.444  1.00 61.38 ? 446 HOH   A O   1 
HETATM 1271 O  O   . HOH   F 5 .   ? 19.684 -3.731  22.449 1.00 60.91 ? 447 HOH   A O   1 
HETATM 1272 O  O   . HOH   F 5 .   ? 13.236 12.789  25.293 1.00 39.00 ? 448 HOH   A O   1 
HETATM 1273 O  O   . HOH   F 5 .   ? -1.922 20.088  25.111 1.00 74.79 ? 449 HOH   A O   1 
HETATM 1274 O  O   . HOH   F 5 .   ? 26.278 10.679  22.105 1.00 62.29 ? 450 HOH   A O   1 
HETATM 1275 O  O   . HOH   F 5 .   ? 2.199  1.549   26.432 1.00 42.00 ? 451 HOH   A O   1 
HETATM 1276 O  O   . HOH   F 5 .   ? 16.686 14.456  2.081  1.00 57.82 ? 452 HOH   A O   1 
HETATM 1277 O  O   . HOH   F 5 .   ? 11.745 23.657  14.720 1.00 37.05 ? 453 HOH   A O   1 
HETATM 1278 O  O   . HOH   F 5 .   ? 24.890 6.177   21.711 1.00 57.86 ? 454 HOH   A O   1 
HETATM 1279 O  O   . HOH   F 5 .   ? 12.651 15.395  26.648 1.00 56.82 ? 455 HOH   A O   1 
HETATM 1280 O  O   . HOH   F 5 .   ? 15.787 12.131  -0.118 1.00 76.63 ? 456 HOH   A O   1 
HETATM 1281 O  O   . HOH   F 5 .   ? 20.066 15.249  0.343  1.00 55.82 ? 457 HOH   A O   1 
HETATM 1282 O  O   . HOH   F 5 .   ? 0.983  8.664   4.306  1.00 51.21 ? 458 HOH   A O   1 
HETATM 1283 O  O   . HOH   F 5 .   ? 0.909  -1.735  23.602 1.00 50.24 ? 459 HOH   A O   1 
HETATM 1284 O  O   . HOH   F 5 .   ? 14.128 -6.229  32.477 1.00 55.39 ? 460 HOH   A O   1 
HETATM 1285 O  O   . HOH   F 5 .   ? 10.167 10.831  0.210  1.00 49.48 ? 461 HOH   A O   1 
HETATM 1286 O  O   . HOH   F 5 .   ? 4.099  -1.804  26.332 1.00 58.92 ? 462 HOH   A O   1 
HETATM 1287 O  O   . HOH   F 5 .   ? 13.825 24.808  15.754 1.00 46.11 ? 463 HOH   A O   1 
HETATM 1288 O  O   . HOH   F 5 .   ? 2.891  12.539  28.597 1.00 59.85 ? 464 HOH   A O   1 
HETATM 1289 O  O   . HOH   F 5 .   ? 8.559  7.345   2.489  1.00 41.11 ? 465 HOH   A O   1 
HETATM 1290 O  O   . HOH   F 5 .   ? 32.000 4.853   14.585 1.00 43.16 ? 466 HOH   A O   1 
HETATM 1291 O  O   . HOH   F 5 .   ? 5.625  5.719   2.327  1.00 57.91 ? 467 HOH   A O   1 
HETATM 1292 O  O   . HOH   F 5 .   ? 5.819  28.167  18.804 1.00 49.84 ? 468 HOH   A O   1 
HETATM 1293 O  O   . HOH   F 5 .   ? 20.731 10.880  25.819 1.00 48.28 ? 469 HOH   A O   1 
HETATM 1294 O  O   . HOH   F 5 .   ? 22.244 10.655  23.584 1.00 45.91 ? 470 HOH   A O   1 
HETATM 1295 O  O   . HOH   F 5 .   ? 17.907 -7.300  30.473 1.00 68.25 ? 471 HOH   A O   1 
HETATM 1296 O  O   . HOH   F 5 .   ? 8.959  17.456  27.008 1.00 53.51 ? 472 HOH   A O   1 
HETATM 1297 O  O   . HOH   F 5 .   ? 5.434  -7.790  25.882 1.00 82.71 ? 473 HOH   A O   1 
HETATM 1298 O  O   . HOH   F 5 .   ? 31.210 7.278   15.316 1.00 60.80 ? 474 HOH   A O   1 
HETATM 1299 O  O   . HOH   F 5 .   ? 18.710 -2.677  18.550 1.00 59.41 ? 475 HOH   A O   1 
HETATM 1300 O  O   . HOH   F 5 .   ? 20.791 12.339  -2.777 1.00 60.54 ? 476 HOH   A O   1 
HETATM 1301 O  O   . HOH   F 5 .   ? 4.042  -6.819  22.868 1.00 44.64 ? 477 HOH   A O   1 
HETATM 1302 O  O   . HOH   F 5 .   ? 3.527  25.710  22.243 1.00 46.21 ? 478 HOH   A O   1 
HETATM 1303 O  O   . HOH   F 5 .   ? 3.468  -4.752  25.802 1.00 72.88 ? 479 HOH   A O   1 
HETATM 1304 O  O   . HOH   F 5 .   ? 9.674  25.149  13.651 1.00 52.24 ? 480 HOH   A O   1 
HETATM 1305 O  O   . HOH   F 5 .   ? 5.887  -8.514  23.299 1.00 52.21 ? 481 HOH   A O   1 
HETATM 1306 O  O   . HOH   F 5 .   ? 23.955 11.693  -2.786 1.00 61.70 ? 482 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   ? 0.4826 0.4244 0.4221 -0.0200 -0.0650 -0.0110 7   SER   A N   
2    C CA  . SER   A 1   ? 0.4709 0.4252 0.4395 -0.0210 -0.0692 -0.0110 7   SER   A CA  
3    C C   . SER   A 1   ? 0.4472 0.4150 0.4348 -0.0191 -0.0644 -0.0081 7   SER   A C   
4    O O   . SER   A 1   ? 0.4513 0.4179 0.4300 -0.0173 -0.0620 -0.0058 7   SER   A O   
5    C CB  . SER   A 1   ? 0.5051 0.4523 0.4774 -0.0234 -0.0858 -0.0118 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.5489 0.4899 0.5118 -0.0224 -0.0941 -0.0087 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4112 0.3905 0.4239 -0.0198 -0.0612 -0.0084 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3860 0.3763 0.4165 -0.0186 -0.0552 -0.0067 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3670 0.3662 0.4140 -0.0196 -0.0450 -0.0076 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3646 0.3623 0.4054 -0.0206 -0.0403 -0.0087 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3411 0.3483 0.4086 -0.0195 -0.0406 -0.0071 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3397 0.3525 0.4198 -0.0209 -0.0293 -0.0079 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.3254 0.3429 0.4122 -0.0201 -0.0201 -0.0075 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3372 0.3551 0.4253 -0.0182 -0.0237 -0.0066 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3383 0.3537 0.4434 -0.0233 -0.0326 -0.0092 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.3133 0.3321 0.4013 -0.0216 -0.0081 -0.0081 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.3091 0.3297 0.4020 -0.0217 0.0022  -0.0087 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.3294 0.3529 0.4496 -0.0236 0.0089  -0.0102 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.3294 0.3521 0.4554 -0.0258 0.0112  -0.0104 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.3109 0.3277 0.3828 -0.0228 0.0113  -0.0085 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.3110 0.3260 0.3612 -0.0211 0.0056  -0.0070 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3164 0.3321 0.3900 -0.0236 0.0219  -0.0100 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.3098 0.3209 0.3424 -0.0225 0.0115  -0.0060 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3388 0.3652 0.4774 -0.0227 0.0128  -0.0111 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3364 0.3656 0.5051 -0.0243 0.0211  -0.0127 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3414 0.3670 0.5078 -0.0253 0.0383  -0.0148 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3530 0.3792 0.5238 -0.0234 0.0399  -0.0156 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.3271 0.3624 0.5265 -0.0223 0.0100  -0.0122 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.3492 0.3852 0.5497 -0.0225 -0.0070 -0.0108 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.3594 0.3972 0.5781 -0.0252 -0.0079 -0.0117 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3752 0.4080 0.5558 -0.0204 -0.0212 -0.0090 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3774 0.4137 0.5942 -0.0260 -0.0238 -0.0112 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3927 0.4227 0.5685 -0.0212 -0.0358 -0.0084 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3986 0.4303 0.5928 -0.0240 -0.0379 -0.0097 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.4360 0.4632 0.6238 -0.0252 -0.0528 -0.0098 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3439 0.3634 0.4982 -0.0285 0.0511  -0.0155 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3506 0.3625 0.4959 -0.0304 0.0682  -0.0178 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3660 0.3746 0.5299 -0.0336 0.0840  -0.0194 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3696 0.3769 0.5332 -0.0357 0.0842  -0.0179 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3818 0.3849 0.4871 -0.0317 0.0695  -0.0170 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3826 0.3829 0.4732 -0.0332 0.0659  -0.0142 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3982 0.3901 0.4901 -0.0345 0.0864  -0.0198 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3589 0.3662 0.5431 -0.0339 0.0977  -0.0224 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3698 0.3740 0.5769 -0.0370 0.1149  -0.0242 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3682 0.3827 0.6085 -0.0370 0.1060  -0.0226 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3659 0.3910 0.6270 -0.0338 0.0892  -0.0215 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3583 0.3680 0.5977 -0.0408 0.1143  -0.0218 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3497 0.3679 0.6181 -0.0415 0.1049  -0.0206 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3506 0.3665 0.5906 -0.0421 0.0917  -0.0177 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3397 0.3553 0.5897 -0.0447 0.0918  -0.0168 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3701 0.3861 0.6694 -0.0455 0.1240  -0.0221 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4256 0.4479 0.7671 -0.0442 0.1331  -0.0250 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4366 0.4715 0.8205 -0.0426 0.1216  -0.0250 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4434 0.4561 0.7740 -0.0447 0.1531  -0.0276 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3554 0.3699 0.5630 -0.0394 0.0805  -0.0163 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3598 0.3721 0.5415 -0.0391 0.0685  -0.0138 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3418 0.3613 0.5216 -0.0354 0.0483  -0.0133 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3373 0.3602 0.5192 -0.0328 0.0446  -0.0139 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3891 0.3906 0.5304 -0.0398 0.0752  -0.0123 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4155 0.4052 0.5480 -0.0438 0.0946  -0.0122 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4340 0.4200 0.5748 -0.0470 0.1004  -0.0108 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4382 0.4183 0.5513 -0.0450 0.1072  -0.0134 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4623 0.4347 0.5918 -0.0511 0.1192  -0.0100 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4709 0.4364 0.5704 -0.0493 0.1256  -0.0132 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4916 0.4530 0.5986 -0.0522 0.1318  -0.0111 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5394 0.4841 0.6310 -0.0568 0.1513  -0.0104 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.3303 0.3502 0.5045 -0.0355 0.0361  -0.0122 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.3306 0.3530 0.4947 -0.0326 0.0186  -0.0117 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.3294 0.3454 0.4608 -0.0323 0.0170  -0.0101 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.3332 0.3453 0.4622 -0.0344 0.0198  -0.0095 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.3449 0.3713 0.5328 -0.0333 0.0049  -0.0126 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3836 0.4074 0.5534 -0.0317 -0.0121 -0.0123 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3875 0.4131 0.5799 -0.0331 -0.0269 -0.0135 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.4299 0.4485 0.6042 -0.0341 -0.0372 -0.0144 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4582 0.4712 0.6122 -0.0325 -0.0504 -0.0144 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4351 0.4490 0.5840 -0.0297 -0.0555 -0.0129 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4800 0.4846 0.6169 -0.0339 -0.0572 -0.0160 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.3136 0.3285 0.4225 -0.0296 0.0135  -0.0092 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.3172 0.3272 0.4000 -0.0288 0.0121  -0.0075 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.3140 0.3239 0.3899 -0.0268 -0.0007 -0.0078 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.3209 0.3329 0.3952 -0.0248 -0.0066 -0.0081 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.3282 0.3361 0.3915 -0.0279 0.0178  -0.0064 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.3430 0.3463 0.3845 -0.0270 0.0160  -0.0041 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.3219 0.3269 0.3885 -0.0303 0.0311  -0.0068 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.3042 0.3100 0.3745 -0.0274 -0.0044 -0.0079 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.3167 0.3191 0.3768 -0.0260 -0.0149 -0.0089 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.3146 0.3116 0.3565 -0.0249 -0.0127 -0.0080 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.3144 0.3100 0.3543 -0.0257 -0.0055 -0.0063 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3370 0.3379 0.4116 -0.0281 -0.0240 -0.0112 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3697 0.3766 0.4666 -0.0286 -0.0280 -0.0116 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.3274 0.3258 0.4105 -0.0309 -0.0196 -0.0117 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.3121 0.3045 0.3403 -0.0231 -0.0187 -0.0090 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.3079 0.2944 0.3234 -0.0220 -0.0165 -0.0088 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3140 0.2959 0.3373 -0.0245 -0.0174 -0.0103 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3188 0.2989 0.3502 -0.0267 -0.0243 -0.0130 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3214 0.3014 0.3217 -0.0203 -0.0210 -0.0106 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3266 0.3098 0.3194 -0.0180 -0.0193 -0.0090 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3471 0.3316 0.3406 -0.0181 -0.0237 -0.0092 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3261 0.3105 0.3134 -0.0159 -0.0134 -0.0072 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.3153 0.2950 0.3372 -0.0245 -0.0113 -0.0084 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.3259 0.3007 0.3560 -0.0271 -0.0106 -0.0093 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3516 0.3185 0.3774 -0.0278 -0.0178 -0.0136 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3597 0.3244 0.3966 -0.0311 -0.0221 -0.0161 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.3275 0.2989 0.3529 -0.0261 -0.0035 -0.0056 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.3378 0.3037 0.3727 -0.0292 -0.0008 -0.0055 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.3609 0.3213 0.3876 -0.0273 0.0043  -0.0012 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3923 0.3460 0.4258 -0.0300 0.0086  0.0004  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.4435 0.3898 0.4798 -0.0306 0.0069  -0.0019 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.4322 0.3760 0.4639 -0.0292 0.0012  -0.0067 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.4649 0.4046 0.5075 -0.0330 0.0116  0.0003  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3563 0.3182 0.3658 -0.0251 -0.0190 -0.0148 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.3635 0.3141 0.3628 -0.0259 -0.0243 -0.0194 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.3932 0.3414 0.3921 -0.0285 -0.0353 -0.0226 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.4106 0.3475 0.4013 -0.0307 -0.0418 -0.0269 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.3734 0.3175 0.3556 -0.0225 -0.0197 -0.0199 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.3724 0.3179 0.3436 -0.0206 -0.0208 -0.0196 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.3816 0.3373 0.3565 -0.0183 -0.0165 -0.0155 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.3900 0.3261 0.3453 -0.0212 -0.0255 -0.0227 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3914 0.3447 0.3550 -0.0173 -0.0180 -0.0163 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.3967 0.3376 0.3469 -0.0189 -0.0230 -0.0202 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.3855 0.3429 0.3933 -0.0284 -0.0381 -0.0205 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3969 0.3535 0.4087 -0.0304 -0.0499 -0.0222 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3910 0.3564 0.4317 -0.0333 -0.0528 -0.0218 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3908 0.3574 0.4415 -0.0348 -0.0635 -0.0226 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3938 0.3531 0.3964 -0.0278 -0.0512 -0.0200 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.4077 0.3576 0.3839 -0.0253 -0.0477 -0.0205 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.4080 0.3604 0.3774 -0.0233 -0.0489 -0.0181 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.4293 0.3619 0.3863 -0.0274 -0.0544 -0.0250 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3858 0.3565 0.4403 -0.0342 -0.0432 -0.0202 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3898 0.3677 0.4726 -0.0372 -0.0425 -0.0200 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4157 0.3882 0.5101 -0.0413 -0.0545 -0.0239 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4324 0.3941 0.5118 -0.0423 -0.0583 -0.0268 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3785 0.3582 0.4668 -0.0378 -0.0289 -0.0175 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4241 0.4034 0.5454 -0.0436 -0.0608 -0.0243 24  THR   A N   
135  C CA  . THR   A 18  ? 0.4441 0.4195 0.5817 -0.0481 -0.0742 -0.0279 24  THR   A CA  
136  C C   . THR   A 18  ? 0.4512 0.4287 0.6119 -0.0518 -0.0658 -0.0285 24  THR   A C   
137  O O   . THR   A 18  ? 0.4481 0.4306 0.6136 -0.0509 -0.0499 -0.0254 24  THR   A O   
138  C CB  . THR   A 18  ? 0.4540 0.4365 0.6144 -0.0486 -0.0866 -0.0275 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4419 0.4375 0.6324 -0.0483 -0.0754 -0.0249 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4593 0.4377 0.5961 -0.0452 -0.0954 -0.0263 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.4535 0.4258 0.6279 -0.0566 -0.0766 -0.0323 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.4567 0.4308 0.6567 -0.0607 -0.0685 -0.0328 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4356 0.4234 0.6708 -0.0614 -0.0586 -0.0299 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4380 0.4273 0.6846 -0.0629 -0.0428 -0.0280 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.4713 0.4378 0.6831 -0.0663 -0.0838 -0.0380 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.5198 0.4904 0.7531 -0.0685 -0.1030 -0.0398 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.5412 0.5179 0.8168 -0.0736 -0.1091 -0.0414 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.5431 0.5116 0.7618 -0.0662 -0.1177 -0.0397 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.5429 0.5220 0.8297 -0.0740 -0.1284 -0.0421 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.5537 0.5272 0.8054 -0.0696 -0.1343 -0.0409 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4227 0.4187 0.6727 -0.0599 -0.0665 -0.0292 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4237 0.4321 0.7070 -0.0598 -0.0567 -0.0270 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.4361 0.4465 0.7030 -0.0562 -0.0368 -0.0233 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.4412 0.4575 0.7305 -0.0572 -0.0217 -0.0219 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4472 0.4620 0.7464 -0.0582 -0.0723 -0.0271 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.5374 0.5500 0.8565 -0.0622 -0.0942 -0.0303 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5575 0.5706 0.9030 -0.0672 -0.0944 -0.0325 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5709 0.5794 0.8763 -0.0606 -0.1138 -0.0305 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.4230 0.4278 0.6510 -0.0523 -0.0366 -0.0221 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.4057 0.4112 0.6159 -0.0493 -0.0203 -0.0188 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3928 0.3927 0.5997 -0.0518 -0.0057 -0.0172 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3978 0.3984 0.6060 -0.0519 0.0100  -0.0147 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.4159 0.4170 0.5892 -0.0450 -0.0249 -0.0179 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.4348 0.4407 0.6059 -0.0418 -0.0326 -0.0175 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.4302 0.4434 0.6185 -0.0412 -0.0258 -0.0164 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4384 0.4392 0.5888 -0.0400 -0.0441 -0.0184 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3785 0.3708 0.5788 -0.0537 -0.0108 -0.0187 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3887 0.3737 0.5860 -0.0561 0.0011  -0.0169 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3797 0.3679 0.6111 -0.0609 0.0121  -0.0166 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3749 0.3584 0.6022 -0.0621 0.0285  -0.0132 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3979 0.3738 0.5839 -0.0571 -0.0081 -0.0194 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.4085 0.3787 0.5597 -0.0525 -0.0110 -0.0185 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.4321 0.4001 0.5675 -0.0503 -0.0237 -0.0215 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.4161 0.3813 0.5454 -0.0497 -0.0005 -0.0142 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.4413 0.4043 0.5491 -0.0461 -0.0200 -0.0196 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.4327 0.3946 0.5379 -0.0456 -0.0071 -0.0151 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.4227 0.3846 0.5501 -0.0504 0.0134  -0.0095 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.4429 0.4004 0.5275 -0.0420 -0.0010 -0.0114 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.4384 0.3942 0.5415 -0.0470 0.0176  -0.0055 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.4454 0.4004 0.5297 -0.0427 0.0100  -0.0065 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3620 0.3573 0.6270 -0.0636 0.0031  -0.0199 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3673 0.3671 0.6707 -0.0681 0.0143  -0.0199 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.3789 0.3828 0.6852 -0.0664 0.0315  -0.0172 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.3908 0.3924 0.7122 -0.0696 0.0497  -0.0157 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3634 0.3715 0.7050 -0.0708 -0.0017 -0.0238 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.3773 0.3856 0.6684 -0.0618 0.0267  -0.0168 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.3786 0.3892 0.6699 -0.0602 0.0419  -0.0152 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.3874 0.3895 0.6348 -0.0574 0.0504  -0.0119 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.3913 0.3948 0.6283 -0.0549 0.0561  -0.0113 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.3987 0.4198 0.7063 -0.0571 0.0308  -0.0169 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.4407 0.4706 0.7958 -0.0599 0.0216  -0.0195 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.4444 0.4762 0.8318 -0.0637 0.0341  -0.0200 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.4602 0.4945 0.8209 -0.0583 -0.0007 -0.0210 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.3720 0.3649 0.5952 -0.0579 0.0503  -0.0100 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.3757 0.3606 0.5597 -0.0551 0.0550  -0.0064 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.3781 0.3562 0.5524 -0.0566 0.0742  -0.0037 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.3689 0.3419 0.5580 -0.0608 0.0883  -0.0030 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.3684 0.3442 0.5356 -0.0556 0.0519  -0.0045 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.3780 0.3450 0.5083 -0.0528 0.0547  -0.0001 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.3793 0.3518 0.4929 -0.0479 0.0424  -0.0012 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.3833 0.3399 0.5043 -0.0539 0.0553  0.0025  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.3712 0.3471 0.5180 -0.0535 0.0750  -0.0022 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.3828 0.3484 0.5089 -0.0548 0.0908  0.0003  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.3982 0.3532 0.4866 -0.0533 0.0871  0.0050  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.4134 0.3545 0.4835 -0.0558 0.0981  0.0089  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.3911 0.3622 0.5161 -0.0527 0.0924  -0.0021 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.4035 0.3611 0.4999 -0.0543 0.1069  0.0000  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.3895 0.3710 0.5544 -0.0536 0.0955  -0.0060 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.3810 0.3419 0.4583 -0.0490 0.0716  0.0047  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.3990 0.3524 0.4470 -0.0468 0.0666  0.0089  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.3919 0.3531 0.4396 -0.0427 0.0511  0.0074  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.3809 0.3521 0.4393 -0.0409 0.0441  0.0037  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.4142 0.3619 0.4375 -0.0464 0.0712  0.0107  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.4385 0.3809 0.4352 -0.0437 0.0628  0.0148  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.4720 0.4003 0.4466 -0.0448 0.0651  0.0205  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.4385 0.3891 0.4296 -0.0395 0.0507  0.0138  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.4814 0.4102 0.4401 -0.0413 0.0538  0.0231  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.4617 0.4042 0.4307 -0.0382 0.0460  0.0188  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.4284 0.3913 0.4310 -0.0370 0.0438  0.0097  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.4572 0.4054 0.4197 -0.0345 0.0353  0.0192  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.4332 0.4001 0.4257 -0.0335 0.0344  0.0102  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.4448 0.4050 0.4192 -0.0323 0.0307  0.0147  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.3801 0.3354 0.4153 -0.0411 0.0464  0.0105  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.3809 0.3412 0.4136 -0.0372 0.0343  0.0090  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.3885 0.3416 0.4022 -0.0347 0.0318  0.0138  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.3983 0.3411 0.4042 -0.0363 0.0373  0.0183  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.3951 0.3578 0.4454 -0.0380 0.0288  0.0051  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.4429 0.3973 0.5005 -0.0412 0.0342  0.0067  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.4718 0.4177 0.5175 -0.0392 0.0317  0.0096  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4453 0.3823 0.4935 -0.0417 0.0376  0.0124  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4479 0.3954 0.4834 -0.0351 0.0246  0.0093  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.3753 0.3329 0.3823 -0.0306 0.0238  0.0132  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.3824 0.3347 0.3773 -0.0277 0.0203  0.0176  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.3685 0.3256 0.3681 -0.0240 0.0135  0.0145  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.3583 0.3225 0.3572 -0.0222 0.0100  0.0120  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.4055 0.3568 0.3851 -0.0272 0.0199  0.0212  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.4833 0.4289 0.4522 -0.0244 0.0146  0.0268  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.5045 0.4503 0.4803 -0.0214 0.0108  0.0271  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.5082 0.4484 0.4619 -0.0254 0.0139  0.0308  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.3668 0.3183 0.3707 -0.0231 0.0127  0.0144  36  SER   A N   
241  C CA  A SER   A 30  ? 0.3634 0.3157 0.3697 -0.0200 0.0086  0.0109  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.3705 0.3232 0.3767 -0.0200 0.0085  0.0107  36  SER   A CA  
243  C C   . SER   A 30  ? 0.3714 0.3268 0.3721 -0.0157 0.0060  0.0133  36  SER   A C   
244  O O   . SER   A 30  ? 0.3724 0.3315 0.3735 -0.0136 0.0041  0.0097  36  SER   A O   
245  C CB  A SER   A 30  ? 0.3679 0.3111 0.3786 -0.0200 0.0099  0.0109  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.3968 0.3409 0.4081 -0.0201 0.0095  0.0098  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3765 0.3177 0.3873 -0.0168 0.0079  0.0074  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.4384 0.3760 0.4467 -0.0185 0.0111  0.0160  36  SER   A OG  
249  N N   . SER   A 31  ? 0.3647 0.3174 0.3603 -0.0148 0.0055  0.0195  37  SER   A N   
250  C CA  . SER   A 31  ? 0.3671 0.3230 0.3612 -0.0111 0.0016  0.0224  37  SER   A CA  
251  C C   . SER   A 31  ? 0.3511 0.3161 0.3421 -0.0114 -0.0001 0.0201  37  SER   A C   
252  O O   . SER   A 31  ? 0.3684 0.3378 0.3623 -0.0086 -0.0027 0.0204  37  SER   A O   
253  C CB  . SER   A 31  ? 0.4145 0.3640 0.4030 -0.0105 -0.0012 0.0301  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.4768 0.4256 0.4531 -0.0136 -0.0018 0.0326  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.3296 0.2971 0.3174 -0.0148 0.0022  0.0177  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.3145 0.2895 0.3003 -0.0152 0.0012  0.0153  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.3089 0.2881 0.3002 -0.0154 0.0015  0.0095  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.3002 0.2850 0.2906 -0.0154 0.0006  0.0077  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.3283 0.3019 0.3069 -0.0188 0.0041  0.0165  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.3441 0.3113 0.3110 -0.0193 0.0023  0.0221  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.3521 0.3142 0.3080 -0.0234 0.0075  0.0224  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.3486 0.3174 0.3039 -0.0239 0.0074  0.0189  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.3878 0.3518 0.3298 -0.0266 0.0092  0.0194  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.3992 0.3506 0.3249 -0.0294 0.0119  0.0232  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.3836 0.3534 0.3265 -0.0268 0.0090  0.0159  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.3080 0.2832 0.3039 -0.0159 0.0019  0.0069  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.3035 0.2799 0.3023 -0.0168 -0.0001 0.0018  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.3147 0.2962 0.3180 -0.0195 0.0001  0.0008  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.3195 0.3042 0.3237 -0.0194 -0.0030 -0.0019 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.3266 0.3039 0.3203 -0.0142 -0.0019 -0.0006 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3315 0.3059 0.3230 -0.0154 -0.0055 -0.0053 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3213 0.2906 0.3157 -0.0175 -0.0075 -0.0077 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3324 0.3085 0.3187 -0.0146 -0.0070 -0.0064 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.3197 0.3007 0.3259 -0.0220 0.0044  0.0031  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.3258 0.3108 0.3393 -0.0244 0.0069  0.0018  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.3284 0.3108 0.3543 -0.0278 0.0105  0.0011  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.3337 0.3098 0.3579 -0.0288 0.0137  0.0033  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.3322 0.3174 0.3374 -0.0250 0.0116  0.0044  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.3435 0.3331 0.3412 -0.0227 0.0084  0.0044  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3307 0.3182 0.3193 -0.0244 0.0127  0.0062  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.3540 0.3494 0.3591 -0.0218 0.0048  0.0009  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.3221 0.3093 0.3625 -0.0296 0.0100  -0.0017 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.3335 0.3201 0.3918 -0.0332 0.0144  -0.0026 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.3380 0.3305 0.4093 -0.0342 0.0184  -0.0039 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.3292 0.3271 0.4021 -0.0323 0.0125  -0.0055 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.3304 0.3161 0.4005 -0.0343 0.0064  -0.0058 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.3353 0.3210 0.4286 -0.0386 0.0100  -0.0069 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.3452 0.3247 0.4410 -0.0401 0.0047  -0.0087 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.3280 0.3216 0.4437 -0.0396 0.0052  -0.0097 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.3297 0.3198 0.4097 -0.0372 0.0296  -0.0031 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.3447 0.3392 0.4406 -0.0384 0.0364  -0.0047 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.3564 0.3525 0.4813 -0.0419 0.0403  -0.0062 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.3665 0.3561 0.4913 -0.0446 0.0473  -0.0047 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.3567 0.3448 0.4359 -0.0394 0.0490  -0.0029 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3657 0.3568 0.4636 -0.0408 0.0588  -0.0053 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.3525 0.3400 0.4067 -0.0364 0.0433  -0.0015 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.3522 0.3566 0.5029 -0.0417 0.0348  -0.0089 43  SER   A N   
298  C CA  . SER   A 37  ? 0.3613 0.3690 0.5462 -0.0451 0.0379  -0.0106 43  SER   A CA  
299  C C   . SER   A 37  ? 0.3691 0.3815 0.5764 -0.0455 0.0488  -0.0118 43  SER   A C   
300  O O   . SER   A 37  ? 0.3636 0.3778 0.5614 -0.0428 0.0492  -0.0120 43  SER   A O   
301  C CB  . SER   A 37  ? 0.3686 0.3813 0.5703 -0.0450 0.0201  -0.0128 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3708 0.3882 0.5685 -0.0416 0.0077  -0.0135 43  SER   A OG  
303  N N   . SER   A 38  ? 0.3716 0.3855 0.6102 -0.0490 0.0585  -0.0129 44  SER   A N   
304  C CA  . SER   A 38  ? 0.3735 0.3914 0.6394 -0.0495 0.0711  -0.0145 44  SER   A CA  
305  C C   . SER   A 38  ? 0.3670 0.3970 0.6667 -0.0474 0.0562  -0.0163 44  SER   A C   
306  O O   . SER   A 38  ? 0.3661 0.4001 0.6758 -0.0476 0.0386  -0.0167 44  SER   A O   
307  C CB  . SER   A 38  ? 0.3872 0.4010 0.6757 -0.0544 0.0890  -0.0147 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3933 0.4117 0.7070 -0.0568 0.0787  -0.0153 44  SER   A OG  
309  N N   . THR   A 39  ? 0.3736 0.4079 0.6885 -0.0454 0.0619  -0.0174 45  THR   A N   
310  C CA  . THR   A 39  ? 0.3832 0.4281 0.7320 -0.0430 0.0474  -0.0182 45  THR   A CA  
311  C C   . THR   A 39  ? 0.4029 0.4532 0.7978 -0.0441 0.0624  -0.0200 45  THR   A C   
312  O O   . THR   A 39  ? 0.4170 0.4607 0.8066 -0.0458 0.0855  -0.0210 45  THR   A O   
313  C CB  . THR   A 39  ? 0.4000 0.4456 0.7267 -0.0382 0.0379  -0.0174 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.4094 0.4522 0.7332 -0.0373 0.0558  -0.0184 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.4131 0.4525 0.6940 -0.0370 0.0283  -0.0158 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.4016 0.4624 0.8402 -0.0431 0.0493  -0.0204 46  THR   A N   
317  C CA  . THR   A 40  ? 0.4119 0.4788 0.8999 -0.0435 0.0635  -0.0221 46  THR   A CA  
318  C C   . THR   A 40  ? 0.4178 0.4856 0.9066 -0.0391 0.0692  -0.0225 46  THR   A C   
319  O O   . THR   A 40  ? 0.4245 0.4901 0.9293 -0.0397 0.0923  -0.0247 46  THR   A O   
320  C CB  . THR   A 40  ? 0.4263 0.5044 0.9674 -0.0447 0.0473  -0.0222 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4580 0.5402 0.9950 -0.0411 0.0193  -0.0203 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.4343 0.5108 0.9798 -0.0499 0.0452  -0.0226 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.4144 0.4840 0.8857 -0.0350 0.0492  -0.0207 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.4133 0.4831 0.8841 -0.0308 0.0526  -0.0208 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4172 0.4763 0.8351 -0.0304 0.0641  -0.0213 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4195 0.4733 0.7978 -0.0315 0.0578  -0.0201 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.4168 0.4922 0.8949 -0.0268 0.0253  -0.0179 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4063 0.4618 0.8249 -0.0289 0.0802  -0.0234 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4218 0.4667 0.7924 -0.0288 0.0896  -0.0242 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3968 0.4430 0.7424 -0.0250 0.0696  -0.0217 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3876 0.4403 0.7570 -0.0215 0.0569  -0.0203 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4662 0.5049 0.8456 -0.0289 0.1134  -0.0280 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5678 0.5927 0.9183 -0.0336 0.1367  -0.0305 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6608 0.6752 0.9996 -0.0335 0.1558  -0.0344 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6746 0.6855 1.0407 -0.0346 0.1766  -0.0379 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.6877 0.6960 0.9866 -0.0324 0.1497  -0.0344 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3793 0.4185 0.6787 -0.0259 0.0675  -0.0209 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3738 0.4124 0.6450 -0.0231 0.0521  -0.0187 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3654 0.3983 0.6192 -0.0219 0.0615  -0.0205 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3777 0.4046 0.6319 -0.0239 0.0808  -0.0238 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.3476 0.3809 0.5859 -0.0190 0.0487  -0.0185 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.3450 0.3733 0.5713 -0.0179 0.0560  -0.0203 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.3507 0.3734 0.5355 -0.0186 0.0527  -0.0197 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3620 0.3810 0.5374 -0.0176 0.0554  -0.0209 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.3407 0.3737 0.5931 -0.0137 0.0470  -0.0187 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3638 0.4040 0.6725 -0.0125 0.0516  -0.0195 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.3416 0.3636 0.5043 -0.0202 0.0469  -0.0180 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3550 0.3725 0.4830 -0.0208 0.0439  -0.0173 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3638 0.3725 0.4720 -0.0243 0.0585  -0.0202 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3642 0.3693 0.4780 -0.0268 0.0700  -0.0217 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3705 0.3900 0.4846 -0.0207 0.0322  -0.0143 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4284 0.4523 0.5514 -0.0179 0.0168  -0.0116 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4586 0.4829 0.5865 -0.0156 0.0129  -0.0109 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4216 0.4470 0.5451 -0.0181 0.0085  -0.0102 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3721 0.3759 0.4569 -0.0248 0.0582  -0.0209 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4015 0.3946 0.4613 -0.0286 0.0683  -0.0233 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3913 0.3836 0.4259 -0.0293 0.0588  -0.0204 52  THR   A C   
358  O O   . THR   A 46  ? 0.3859 0.3836 0.4180 -0.0271 0.0480  -0.0184 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4610 0.4479 0.5152 -0.0292 0.0747  -0.0270 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4803 0.4661 0.5586 -0.0288 0.0866  -0.0301 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4922 0.4659 0.5139 -0.0336 0.0809  -0.0294 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3839 0.3690 0.4012 -0.0323 0.0632  -0.0197 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3735 0.3576 0.3700 -0.0327 0.0540  -0.0166 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3828 0.3588 0.3561 -0.0350 0.0536  -0.0181 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.3989 0.3637 0.3607 -0.0383 0.0637  -0.0213 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3811 0.3601 0.3698 -0.0347 0.0573  -0.0143 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3692 0.3554 0.3831 -0.0332 0.0582  -0.0135 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.3827 0.3611 0.3538 -0.0343 0.0469  -0.0105 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3596 0.3569 0.3859 -0.0295 0.0448  -0.0116 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3693 0.3497 0.3358 -0.0338 0.0423  -0.0161 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3744 0.3482 0.3217 -0.0362 0.0390  -0.0173 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3821 0.3441 0.3053 -0.0398 0.0393  -0.0158 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3814 0.3446 0.3039 -0.0390 0.0365  -0.0121 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3609 0.3438 0.3125 -0.0338 0.0272  -0.0148 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.3923 0.3413 0.2942 -0.0440 0.0419  -0.0187 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4185 0.3529 0.2921 -0.0479 0.0398  -0.0168 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.4298 0.3609 0.2904 -0.0500 0.0288  -0.0178 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.4464 0.3662 0.2926 -0.0537 0.0329  -0.0226 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.4356 0.3528 0.2923 -0.0520 0.0550  -0.0198 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.4660 0.3882 0.3430 -0.0501 0.0670  -0.0195 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.4927 0.4204 0.3751 -0.0481 0.0617  -0.0137 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5137 0.4467 0.4187 -0.0468 0.0724  -0.0142 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5153 0.4561 0.4339 -0.0447 0.0691  -0.0105 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.4866 0.4300 0.3978 -0.0433 0.0568  -0.0059 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.4892 0.4349 0.4309 -0.0440 0.0777  -0.0115 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4298 0.3712 0.2985 -0.0476 0.0153  -0.0136 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4257 0.3688 0.2924 -0.0488 0.0037  -0.0141 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4198 0.3716 0.2946 -0.0463 -0.0095 -0.0083 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4101 0.3665 0.2920 -0.0433 -0.0088 -0.0044 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4180 0.3722 0.3057 -0.0466 0.0066  -0.0174 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3900 0.3633 0.3072 -0.0400 0.0058  -0.0137 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.4229 0.3781 0.3017 -0.0473 -0.0208 -0.0081 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4213 0.3868 0.3154 -0.0444 -0.0320 -0.0032 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4096 0.3890 0.3281 -0.0421 -0.0327 -0.0047 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.4154 0.4012 0.3466 -0.0416 -0.0422 -0.0025 57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.4731 0.4293 0.3525 -0.0478 -0.0465 -0.0003 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5796 0.5294 0.4503 -0.0527 -0.0535 -0.0043 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6018 0.5515 0.4734 -0.0540 -0.0449 -0.0098 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.6313 0.5754 0.4948 -0.0554 -0.0684 -0.0018 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3873 0.3713 0.3144 -0.0405 -0.0224 -0.0079 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3641 0.3589 0.3115 -0.0382 -0.0218 -0.0085 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.3397 0.3445 0.3034 -0.0341 -0.0249 -0.0041 58  CYS   A C   
403  O O   . CYS   A 52  ? 0.3319 0.3371 0.2943 -0.0317 -0.0235 -0.0015 58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3717 0.3683 0.3244 -0.0364 -0.0112 -0.0111 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.4068 0.3936 0.3492 -0.0404 -0.0054 -0.0171 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3095 0.3214 0.2892 -0.0335 -0.0279 -0.0037 59  GLN   A N   
407  C CA  A GLN   A 53  ? 0.3047 0.3252 0.3019 -0.0298 -0.0281 -0.0004 59  GLN   A CA  
408  C CA  B GLN   A 53  ? 0.3093 0.3295 0.3054 -0.0296 -0.0277 -0.0004 59  GLN   A CA  
409  C C   . GLN   A 53  ? 0.2985 0.3239 0.3075 -0.0279 -0.0206 -0.0015 59  GLN   A C   
410  O O   . GLN   A 53  ? 0.2951 0.3259 0.3185 -0.0256 -0.0189 0.0004  59  GLN   A O   
411  C CB  A GLN   A 53  ? 0.3130 0.3368 0.3219 -0.0307 -0.0383 0.0020  59  GLN   A CB  
412  C CB  B GLN   A 53  ? 0.3336 0.3562 0.3385 -0.0299 -0.0380 0.0028  59  GLN   A CB  
413  C CG  A GLN   A 53  ? 0.3217 0.3436 0.3273 -0.0291 -0.0442 0.0060  59  GLN   A CG  
414  C CG  B GLN   A 53  ? 0.3853 0.3996 0.3730 -0.0312 -0.0449 0.0051  59  GLN   A CG  
415  C CD  A GLN   A 53  ? 0.3136 0.3405 0.3374 -0.0288 -0.0544 0.0092  59  GLN   A CD  
416  C CD  B GLN   A 53  ? 0.4506 0.4629 0.4313 -0.0282 -0.0388 0.0068  59  GLN   A CD  
417  O OE1 A GLN   A 53  ? 0.3175 0.3401 0.3362 -0.0323 -0.0664 0.0099  59  GLN   A OE1 
418  O OE1 B GLN   A 53  ? 0.4617 0.4652 0.4240 -0.0298 -0.0380 0.0070  59  GLN   A OE1 
419  N NE2 A GLN   A 53  ? 0.2777 0.3128 0.3234 -0.0248 -0.0499 0.0110  59  GLN   A NE2 
420  N NE2 B GLN   A 53  ? 0.4501 0.4691 0.4448 -0.0241 -0.0336 0.0079  59  GLN   A NE2 
421  N N   . THR   A 54  ? 0.2912 0.3134 0.2942 -0.0290 -0.0153 -0.0044 60  THR   A N   
422  C CA  . THR   A 54  ? 0.2853 0.3092 0.2956 -0.0273 -0.0086 -0.0046 60  THR   A CA  
423  C C   . THR   A 54  ? 0.2853 0.3052 0.2865 -0.0262 -0.0039 -0.0059 60  THR   A C   
424  O O   . THR   A 54  ? 0.2803 0.2959 0.2721 -0.0279 -0.0040 -0.0079 60  THR   A O   
425  C CB  . THR   A 54  ? 0.3216 0.3463 0.3405 -0.0299 -0.0086 -0.0062 60  THR   A CB  
426  O OG1 . THR   A 54  ? 0.3614 0.3804 0.3707 -0.0331 -0.0095 -0.0097 60  THR   A OG1 
427  C CG2 . THR   A 54  ? 0.3128 0.3425 0.3456 -0.0315 -0.0145 -0.0051 60  THR   A CG2 
428  N N   . GLY   A 55  ? 0.2792 0.2993 0.2829 -0.0234 0.0003  -0.0044 61  GLY   A N   
429  C CA  . GLY   A 55  ? 0.2822 0.2992 0.2813 -0.0219 0.0028  -0.0049 61  GLY   A CA  
430  C C   . GLY   A 55  ? 0.2747 0.2899 0.2748 -0.0193 0.0050  -0.0028 61  GLY   A C   
431  O O   . GLY   A 55  ? 0.2884 0.3034 0.2915 -0.0191 0.0070  -0.0015 61  GLY   A O   
432  N N   . VAL   A 56  ? 0.2705 0.2831 0.2680 -0.0176 0.0047  -0.0024 62  VAL   A N   
433  C CA  . VAL   A 56  ? 0.2774 0.2853 0.2717 -0.0155 0.0046  -0.0001 62  VAL   A CA  
434  C C   . VAL   A 56  ? 0.2838 0.2906 0.2743 -0.0140 0.0016  0.0003  62  VAL   A C   
435  O O   . VAL   A 56  ? 0.2867 0.2960 0.2810 -0.0144 0.0003  -0.0010 62  VAL   A O   
436  C CB  . VAL   A 56  ? 0.2840 0.2884 0.2812 -0.0152 0.0045  0.0002  62  VAL   A CB  
437  C CG1 . VAL   A 56  ? 0.3005 0.2976 0.2913 -0.0131 0.0021  0.0034  62  VAL   A CG1 
438  C CG2 . VAL   A 56  ? 0.2878 0.2923 0.2888 -0.0171 0.0077  -0.0006 62  VAL   A CG2 
439  N N   . TYR   A 57  ? 0.2915 0.2936 0.2744 -0.0127 0.0015  0.0018  63  TYR   A N   
440  C CA  . TYR   A 57  ? 0.2886 0.2883 0.2673 -0.0118 -0.0023 0.0017  63  TYR   A CA  
441  C C   . TYR   A 57  ? 0.3021 0.2923 0.2713 -0.0108 -0.0061 0.0033  63  TYR   A C   
442  O O   . TYR   A 57  ? 0.3161 0.2998 0.2775 -0.0106 -0.0036 0.0051  63  TYR   A O   
443  C CB  . TYR   A 57  ? 0.2821 0.2826 0.2581 -0.0115 -0.0002 0.0011  63  TYR   A CB  
444  C CG  . TYR   A 57  ? 0.3053 0.2985 0.2721 -0.0107 0.0037  0.0019  63  TYR   A CG  
445  C CD1 . TYR   A 57  ? 0.3126 0.3062 0.2821 -0.0109 0.0096  0.0026  63  TYR   A CD1 
446  C CD2 . TYR   A 57  ? 0.3170 0.3013 0.2723 -0.0100 0.0023  0.0015  63  TYR   A CD2 
447  C CE1 . TYR   A 57  ? 0.3295 0.3154 0.2917 -0.0102 0.0160  0.0031  63  TYR   A CE1 
448  C CE2 . TYR   A 57  ? 0.3357 0.3106 0.2798 -0.0095 0.0081  0.0015  63  TYR   A CE2 
449  C CZ  . TYR   A 57  ? 0.3436 0.3192 0.2914 -0.0095 0.0159  0.0024  63  TYR   A CZ  
450  O OH  . TYR   A 57  ? 0.3569 0.3222 0.2949 -0.0092 0.0243  0.0023  63  TYR   A OH  
451  N N   . TYR   A 58  ? 0.2917 0.2798 0.2605 -0.0106 -0.0122 0.0029  64  TYR   A N   
452  C CA  . TYR   A 58  ? 0.3160 0.2931 0.2734 -0.0101 -0.0187 0.0046  64  TYR   A CA  
453  C C   . TYR   A 58  ? 0.3385 0.3068 0.2798 -0.0103 -0.0181 0.0037  64  TYR   A C   
454  O O   . TYR   A 58  ? 0.3316 0.3032 0.2764 -0.0106 -0.0183 0.0016  64  TYR   A O   
455  C CB  . TYR   A 58  ? 0.3121 0.2910 0.2804 -0.0099 -0.0276 0.0047  64  TYR   A CB  
456  C CG  . TYR   A 58  ? 0.3469 0.3132 0.3028 -0.0097 -0.0374 0.0069  64  TYR   A CG  
457  C CD1 . TYR   A 58  ? 0.3721 0.3289 0.3167 -0.0090 -0.0387 0.0103  64  TYR   A CD1 
458  C CD2 . TYR   A 58  ? 0.3677 0.3294 0.3202 -0.0105 -0.0457 0.0058  64  TYR   A CD2 
459  C CE1 . TYR   A 58  ? 0.3929 0.3350 0.3217 -0.0091 -0.0492 0.0130  64  TYR   A CE1 
460  C CE2 . TYR   A 58  ? 0.3996 0.3471 0.3368 -0.0108 -0.0567 0.0078  64  TYR   A CE2 
461  C CZ  . TYR   A 58  ? 0.4187 0.3557 0.3425 -0.0101 -0.0587 0.0116  64  TYR   A CZ  
462  O OH  . TYR   A 58  ? 0.4403 0.3609 0.3462 -0.0107 -0.0713 0.0143  64  TYR   A OH  
463  N N   . CYS   A 59  ? 0.3517 0.3067 0.2743 -0.0103 -0.0168 0.0053  65  CYS   A N   
464  C CA  . CYS   A 59  ? 0.3715 0.3137 0.2745 -0.0108 -0.0144 0.0040  65  CYS   A CA  
465  C C   . CYS   A 59  ? 0.3970 0.3233 0.2811 -0.0116 -0.0253 0.0052  65  CYS   A C   
466  O O   . CYS   A 59  ? 0.4159 0.3302 0.2848 -0.0118 -0.0263 0.0082  65  CYS   A O   
467  C CB  . CYS   A 59  ? 0.3906 0.3272 0.2848 -0.0107 -0.0024 0.0047  65  CYS   A CB  
468  S SG  . CYS   A 59  ? 0.4426 0.3600 0.3107 -0.0113 0.0044  0.0026  65  CYS   A SG  
469  N N   . SER   A 60  ? 0.3856 0.3108 0.2704 -0.0124 -0.0340 0.0030  66  SER   A N   
470  C CA  . SER   A 60  ? 0.4249 0.3353 0.2939 -0.0137 -0.0476 0.0041  66  SER   A CA  
471  C C   . SER   A 60  ? 0.4479 0.3346 0.2812 -0.0150 -0.0454 0.0043  66  SER   A C   
472  O O   . SER   A 60  ? 0.4706 0.3421 0.2858 -0.0158 -0.0553 0.0073  66  SER   A O   
473  C CB  . SER   A 60  ? 0.4715 0.3857 0.3510 -0.0149 -0.0575 0.0013  66  SER   A CB  
474  O OG  . SER   A 60  ? 0.5269 0.4350 0.3950 -0.0160 -0.0521 -0.0027 66  SER   A OG  
475  N N   . SER   A 61  ? 0.4425 0.3249 0.2657 -0.0151 -0.0318 0.0015  67  SER   A N   
476  C CA  . SER   A 61  ? 0.4555 0.3137 0.2440 -0.0166 -0.0253 0.0009  67  SER   A CA  
477  C C   . SER   A 61  ? 0.4775 0.3264 0.2529 -0.0163 -0.0180 0.0052  67  SER   A C   
478  O O   . SER   A 61  ? 0.5208 0.3463 0.2638 -0.0179 -0.0123 0.0054  67  SER   A O   
479  C CB  . SER   A 61  ? 0.4628 0.3193 0.2488 -0.0165 -0.0112 -0.0037 67  SER   A CB  
480  O OG  . SER   A 61  ? 0.4828 0.3561 0.2920 -0.0144 0.0018  -0.0033 67  SER   A OG  
481  N N   . ARG   A 62  ? 0.4486 0.3138 0.2473 -0.0147 -0.0169 0.0083  68  ARG   A N   
482  C CA  . ARG   A 62  ? 0.4583 0.3159 0.2483 -0.0146 -0.0113 0.0127  68  ARG   A CA  
483  C C   . ARG   A 62  ? 0.4650 0.3264 0.2642 -0.0138 -0.0255 0.0172  68  ARG   A C   
484  O O   . ARG   A 62  ? 0.4709 0.3257 0.2643 -0.0137 -0.0227 0.0215  68  ARG   A O   
485  C CB  . ARG   A 62  ? 0.4614 0.3342 0.2728 -0.0136 0.0043  0.0121  68  ARG   A CB  
486  C CG  . ARG   A 62  ? 0.4830 0.3506 0.2879 -0.0140 0.0198  0.0085  68  ARG   A CG  
487  C CD  . ARG   A 62  ? 0.5212 0.3625 0.2929 -0.0157 0.0299  0.0099  68  ARG   A CD  
488  N NE  . ARG   A 62  ? 0.5350 0.3710 0.3037 -0.0159 0.0469  0.0062  68  ARG   A NE  
489  C CZ  . ARG   A 62  ? 0.5879 0.4102 0.3377 -0.0166 0.0486  0.0021  68  ARG   A CZ  
490  N NH1 . ARG   A 62  ? 0.5832 0.3955 0.3142 -0.0178 0.0331  0.0013  68  ARG   A NH1 
491  N NH2 . ARG   A 62  ? 0.5852 0.4030 0.3359 -0.0164 0.0658  -0.0014 68  ARG   A NH2 
492  N N   . ARG   A 63  ? 0.4630 0.3369 0.2819 -0.0131 -0.0389 0.0162  69  ARG   A N   
493  C CA  . ARG   A 63  ? 0.4668 0.3479 0.3034 -0.0118 -0.0509 0.0199  69  ARG   A CA  
494  C C   . ARG   A 63  ? 0.4526 0.3453 0.3068 -0.0105 -0.0406 0.0216  69  ARG   A C   
495  O O   . ARG   A 63  ? 0.4801 0.3661 0.3314 -0.0098 -0.0436 0.0262  69  ARG   A O   
496  C CB  . ARG   A 63  ? 0.4952 0.3545 0.3074 -0.0125 -0.0648 0.0248  69  ARG   A CB  
497  C CG  . ARG   A 63  ? 0.5397 0.3876 0.3374 -0.0143 -0.0793 0.0230  69  ARG   A CG  
498  C CD  . ARG   A 63  ? 0.5886 0.4143 0.3624 -0.0150 -0.0957 0.0286  69  ARG   A CD  
499  N NE  . ARG   A 63  ? 0.6291 0.4409 0.3855 -0.0175 -0.1114 0.0268  69  ARG   A NE  
500  C CZ  . ARG   A 63  ? 0.6649 0.4471 0.3779 -0.0203 -0.1179 0.0283  69  ARG   A CZ  
501  N NH1 . ARG   A 63  ? 0.6551 0.4180 0.3370 -0.0208 -0.1077 0.0319  69  ARG   A NH1 
502  N NH2 . ARG   A 63  ? 0.6665 0.4366 0.3651 -0.0230 -0.1335 0.0258  69  ARG   A NH2 
503  N N   . LYS   A 64  ? 0.4207 0.3281 0.2900 -0.0104 -0.0285 0.0181  70  LYS   A N   
504  C CA  . LYS   A 64  ? 0.4165 0.3336 0.3006 -0.0099 -0.0188 0.0188  70  LYS   A CA  
505  C C   . LYS   A 64  ? 0.3960 0.3336 0.3054 -0.0097 -0.0144 0.0149  70  LYS   A C   
506  O O   . LYS   A 64  ? 0.3970 0.3396 0.3084 -0.0099 -0.0134 0.0117  70  LYS   A O   
507  C CB  . LYS   A 64  ? 0.4602 0.3664 0.3274 -0.0110 -0.0057 0.0197  70  LYS   A CB  
508  C CG  . LYS   A 64  ? 0.5466 0.4601 0.4280 -0.0112 0.0036  0.0208  70  LYS   A CG  
509  C CD  . LYS   A 64  ? 0.6325 0.5279 0.4930 -0.0124 0.0125  0.0243  70  LYS   A CD  
510  C CE  . LYS   A 64  ? 0.6681 0.5694 0.5435 -0.0131 0.0215  0.0255  70  LYS   A CE  
511  N NZ  . LYS   A 64  ? 0.6906 0.5943 0.5757 -0.0123 0.0133  0.0284  70  LYS   A NZ  
512  N N   . HIS   A 65  ? 0.3661 0.3136 0.2929 -0.0094 -0.0121 0.0152  71  HIS   A N   
513  C CA  . HIS   A 65  ? 0.3505 0.3141 0.2968 -0.0098 -0.0078 0.0118  71  HIS   A CA  
514  C C   . HIS   A 65  ? 0.3633 0.3283 0.3099 -0.0109 0.0027  0.0115  71  HIS   A C   
515  O O   . HIS   A 65  ? 0.3874 0.3452 0.3291 -0.0113 0.0065  0.0140  71  HIS   A O   
516  C CB  . HIS   A 65  ? 0.3438 0.3149 0.3077 -0.0093 -0.0111 0.0116  71  HIS   A CB  
517  C CG  . HIS   A 65  ? 0.3422 0.3133 0.3125 -0.0082 -0.0208 0.0120  71  HIS   A CG  
518  N ND1 . HIS   A 65  ? 0.3519 0.3328 0.3358 -0.0084 -0.0219 0.0090  71  HIS   A ND1 
519  C CD2 . HIS   A 65  ? 0.3547 0.3163 0.3201 -0.0070 -0.0300 0.0155  71  HIS   A CD2 
520  C CE1 . HIS   A 65  ? 0.3594 0.3381 0.3500 -0.0074 -0.0310 0.0103  71  HIS   A CE1 
521  N NE2 . HIS   A 65  ? 0.3735 0.3407 0.3531 -0.0065 -0.0374 0.0143  71  HIS   A NE2 
522  N N   . TYR   A 66  ? 0.3354 0.3090 0.2890 -0.0114 0.0071  0.0088  72  TYR   A N   
523  C CA  . TYR   A 66  ? 0.3366 0.3131 0.2958 -0.0125 0.0156  0.0085  72  TYR   A CA  
524  C C   . TYR   A 66  ? 0.3176 0.3073 0.2940 -0.0137 0.0154  0.0061  72  TYR   A C   
525  O O   . TYR   A 66  ? 0.2965 0.2928 0.2771 -0.0135 0.0119  0.0043  72  TYR   A O   
526  C CB  . TYR   A 66  ? 0.3452 0.3178 0.2981 -0.0121 0.0215  0.0079  72  TYR   A CB  
527  C CG  . TYR   A 66  ? 0.3753 0.3310 0.3064 -0.0118 0.0244  0.0097  72  TYR   A CG  
528  C CD1 . TYR   A 66  ? 0.3960 0.3416 0.3194 -0.0127 0.0329  0.0120  72  TYR   A CD1 
529  C CD2 . TYR   A 66  ? 0.3933 0.3415 0.3102 -0.0111 0.0194  0.0089  72  TYR   A CD2 
530  C CE1 . TYR   A 66  ? 0.4243 0.3508 0.3226 -0.0129 0.0367  0.0136  72  TYR   A CE1 
531  C CE2 . TYR   A 66  ? 0.4248 0.3544 0.3172 -0.0114 0.0217  0.0100  72  TYR   A CE2 
532  C CZ  . TYR   A 66  ? 0.4512 0.3692 0.3326 -0.0123 0.0307  0.0125  72  TYR   A CZ  
533  O OH  . TYR   A 66  ? 0.4920 0.3877 0.3438 -0.0131 0.0335  0.0138  72  TYR   A OH  
534  N N   . PRO   A 67  ? 0.3211 0.3133 0.3060 -0.0153 0.0191  0.0062  73  PRO   A N   
535  C CA  . PRO   A 67  ? 0.3129 0.3153 0.3112 -0.0171 0.0177  0.0037  73  PRO   A CA  
536  C C   . PRO   A 67  ? 0.3253 0.3326 0.3303 -0.0170 0.0197  0.0034  73  PRO   A C   
537  O O   . PRO   A 67  ? 0.3340 0.3378 0.3400 -0.0166 0.0264  0.0047  73  PRO   A O   
538  C CB  . PRO   A 67  ? 0.3267 0.3281 0.3319 -0.0192 0.0206  0.0038  73  PRO   A CB  
539  C CG  . PRO   A 67  ? 0.3499 0.3416 0.3476 -0.0185 0.0271  0.0070  73  PRO   A CG  
540  C CD  . PRO   A 67  ? 0.3305 0.3145 0.3121 -0.0160 0.0245  0.0086  73  PRO   A CD  
541  N N   . VAL   A 68  ? 0.3033 0.3174 0.3128 -0.0174 0.0147  0.0020  74  VAL   A N   
542  C CA  . VAL   A 68  ? 0.3030 0.3217 0.3210 -0.0168 0.0151  0.0023  74  VAL   A CA  
543  C C   . VAL   A 68  ? 0.2911 0.3168 0.3178 -0.0188 0.0084  0.0013  74  VAL   A C   
544  O O   . VAL   A 68  ? 0.2909 0.3164 0.3114 -0.0204 0.0039  -0.0002 74  VAL   A O   
545  C CB  . VAL   A 68  ? 0.3223 0.3382 0.3319 -0.0143 0.0148  0.0026  74  VAL   A CB  
546  C CG1 . VAL   A 68  ? 0.3440 0.3509 0.3441 -0.0128 0.0213  0.0034  74  VAL   A CG1 
547  C CG2 . VAL   A 68  ? 0.3233 0.3391 0.3247 -0.0144 0.0092  0.0017  74  VAL   A CG2 
548  N N   . SER   A 69  ? 0.2689 0.2994 0.3095 -0.0186 0.0078  0.0023  75  SER   A N   
549  C CA  . SER   A 69  ? 0.2776 0.3132 0.3253 -0.0201 -0.0008 0.0024  75  SER   A CA  
550  C C   . SER   A 69  ? 0.2712 0.3065 0.3160 -0.0172 -0.0018 0.0040  75  SER   A C   
551  O O   . SER   A 69  ? 0.2789 0.3127 0.3267 -0.0146 0.0048  0.0047  75  SER   A O   
552  C CB  . SER   A 69  ? 0.3119 0.3534 0.3814 -0.0213 -0.0021 0.0032  75  SER   A CB  
553  O OG  . SER   A 69  ? 0.4136 0.4549 0.4867 -0.0243 -0.0011 0.0016  75  SER   A OG  
554  N N   . PHE   A 70  ? 0.2574 0.2921 0.2946 -0.0180 -0.0090 0.0043  76  PHE   A N   
555  C CA  . PHE   A 70  ? 0.2497 0.2831 0.2841 -0.0155 -0.0098 0.0060  76  PHE   A CA  
556  C C   . PHE   A 70  ? 0.2709 0.3055 0.3085 -0.0164 -0.0195 0.0083  76  PHE   A C   
557  O O   . PHE   A 70  ? 0.2800 0.3138 0.3133 -0.0197 -0.0262 0.0078  76  PHE   A O   
558  C CB  . PHE   A 70  ? 0.2482 0.2765 0.2664 -0.0149 -0.0070 0.0049  76  PHE   A CB  
559  C CG  . PHE   A 70  ? 0.2585 0.2842 0.2651 -0.0177 -0.0093 0.0032  76  PHE   A CG  
560  C CD1 . PHE   A 70  ? 0.2646 0.2894 0.2689 -0.0189 -0.0063 0.0011  76  PHE   A CD1 
561  C CD2 . PHE   A 70  ? 0.2832 0.3058 0.2811 -0.0193 -0.0137 0.0039  76  PHE   A CD2 
562  C CE1 . PHE   A 70  ? 0.2758 0.2975 0.2716 -0.0214 -0.0069 -0.0009 76  PHE   A CE1 
563  C CE2 . PHE   A 70  ? 0.2881 0.3064 0.2749 -0.0221 -0.0134 0.0018  76  PHE   A CE2 
564  C CZ  . PHE   A 70  ? 0.2718 0.2900 0.2587 -0.0231 -0.0097 -0.0009 76  PHE   A CZ  
565  N N   . SER   A 71  ? 0.2704 0.3054 0.3146 -0.0136 -0.0206 0.0109  77  SER   A N   
566  C CA  . SER   A 71  ? 0.2603 0.2951 0.3081 -0.0139 -0.0310 0.0143  77  SER   A CA  
567  C C   . SER   A 71  ? 0.2813 0.3084 0.3069 -0.0160 -0.0354 0.0150  77  SER   A C   
568  O O   . SER   A 71  ? 0.3009 0.3245 0.3131 -0.0164 -0.0290 0.0128  77  SER   A O   
569  C CB  . SER   A 71  ? 0.2636 0.3008 0.3284 -0.0098 -0.0298 0.0171  77  SER   A CB  
570  O OG  . SER   A 71  ? 0.2939 0.3264 0.3485 -0.0076 -0.0226 0.0163  77  SER   A OG  
571  N N   . LYS   A 72  ? 0.2879 0.3113 0.3096 -0.0175 -0.0462 0.0183  78  LYS   A N   
572  C CA  . LYS   A 72  ? 0.3248 0.3381 0.3228 -0.0198 -0.0487 0.0194  78  LYS   A CA  
573  C C   . LYS   A 72  ? 0.3307 0.3411 0.3265 -0.0169 -0.0438 0.0214  78  LYS   A C   
574  O O   . LYS   A 72  ? 0.3364 0.3511 0.3487 -0.0131 -0.0430 0.0233  78  LYS   A O   
575  C CB  . LYS   A 72  ? 0.3828 0.3896 0.3730 -0.0228 -0.0628 0.0228  78  LYS   A CB  
576  C CG  . LYS   A 72  ? 0.4776 0.4832 0.4612 -0.0273 -0.0665 0.0192  78  LYS   A CG  
577  C CD  . LYS   A 72  ? 0.5744 0.5688 0.5400 -0.0318 -0.0801 0.0212  78  LYS   A CD  
578  C CE  . LYS   A 72  ? 0.6342 0.6235 0.5855 -0.0369 -0.0791 0.0157  78  LYS   A CE  
579  N NZ  . LYS   A 72  ? 0.6875 0.6636 0.6183 -0.0421 -0.0933 0.0168  78  LYS   A NZ  
580  N N   . PRO   A 73  ? 0.3421 0.3449 0.3193 -0.0187 -0.0393 0.0207  79  PRO   A N   
581  C CA  . PRO   A 73  ? 0.3423 0.3421 0.3189 -0.0164 -0.0345 0.0223  79  PRO   A CA  
582  C C   . PRO   A 73  ? 0.3503 0.3470 0.3322 -0.0143 -0.0422 0.0280  79  PRO   A C   
583  O O   . PRO   A 73  ? 0.3679 0.3581 0.3405 -0.0163 -0.0519 0.0318  79  PRO   A O   
584  C CB  . PRO   A 73  ? 0.3730 0.3642 0.3298 -0.0198 -0.0295 0.0209  79  PRO   A CB  
585  C CG  . PRO   A 73  ? 0.3917 0.3839 0.3424 -0.0229 -0.0279 0.0168  79  PRO   A CG  
586  C CD  . PRO   A 73  ? 0.3529 0.3488 0.3107 -0.0230 -0.0372 0.0179  79  PRO   A CD  
587  N N   . SER   A 74  ? 0.3367 0.3369 0.3337 -0.0102 -0.0388 0.0287  80  SER   A N   
588  C CA  . SER   A 74  ? 0.3545 0.3528 0.3620 -0.0074 -0.0456 0.0342  80  SER   A CA  
589  C C   . SER   A 74  ? 0.3472 0.3439 0.3621 -0.0039 -0.0385 0.0341  80  SER   A C   
590  O O   . SER   A 74  ? 0.3356 0.3327 0.3465 -0.0043 -0.0294 0.0295  80  SER   A O   
591  C CB  . SER   A 74  ? 0.3865 0.3931 0.4158 -0.0055 -0.0521 0.0353  80  SER   A CB  
592  O OG  . SER   A 74  ? 0.4379 0.4522 0.4845 -0.0026 -0.0426 0.0314  80  SER   A OG  
593  N N   . LEU   A 75  ? 0.3464 0.3404 0.3725 -0.0008 -0.0433 0.0390  81  LEU   A N   
594  C CA  . LEU   A 75  ? 0.3571 0.3479 0.3906 0.0024  -0.0368 0.0389  81  LEU   A CA  
595  C C   . LEU   A 75  ? 0.3413 0.3396 0.3983 0.0065  -0.0313 0.0361  81  LEU   A C   
596  O O   . LEU   A 75  ? 0.3326 0.3356 0.4091 0.0090  -0.0369 0.0392  81  LEU   A O   
597  C CB  . LEU   A 75  ? 0.3776 0.3601 0.4108 0.0037  -0.0453 0.0465  81  LEU   A CB  
598  C CG  . LEU   A 75  ? 0.4251 0.4000 0.4599 0.0059  -0.0404 0.0479  81  LEU   A CG  
599  C CD1 . LEU   A 75  ? 0.4309 0.3998 0.4459 0.0020  -0.0328 0.0447  81  LEU   A CD1 
600  C CD2 . LEU   A 75  ? 0.4567 0.4229 0.4921 0.0074  -0.0511 0.0569  81  LEU   A CD2 
601  N N   . ILE   A 76  ? 0.3328 0.3313 0.3879 0.0068  -0.0204 0.0301  82  ILE   A N   
602  C CA  . ILE   A 76  ? 0.3450 0.3474 0.4158 0.0097  -0.0122 0.0263  82  ILE   A CA  
603  C C   . ILE   A 76  ? 0.3717 0.3667 0.4418 0.0116  -0.0030 0.0230  82  ILE   A C   
604  O O   . ILE   A 76  ? 0.3769 0.3663 0.4305 0.0093  -0.0011 0.0206  82  ILE   A O   
605  C CB  . ILE   A 76  ? 0.3623 0.3693 0.4250 0.0070  -0.0084 0.0218  82  ILE   A CB  
606  C CG1 . ILE   A 76  ? 0.3708 0.3846 0.4366 0.0050  -0.0171 0.0245  82  ILE   A CG1 
607  C CG2 . ILE   A 76  ? 0.3684 0.3753 0.4393 0.0090  0.0030  0.0172  82  ILE   A CG2 
608  C CD1 . ILE   A 76  ? 0.3937 0.4117 0.4532 0.0024  -0.0137 0.0205  82  ILE   A CD1 
609  N N   . PHE   A 77  ? 0.3825 0.3769 0.4719 0.0157  0.0028  0.0226  83  PHE   A N   
610  C CA  . PHE   A 77  ? 0.3998 0.3850 0.4884 0.0176  0.0126  0.0186  83  PHE   A CA  
611  C C   . PHE   A 77  ? 0.3968 0.3774 0.4682 0.0153  0.0212  0.0115  83  PHE   A C   
612  O O   . PHE   A 77  ? 0.4008 0.3852 0.4730 0.0148  0.0255  0.0093  83  PHE   A O   
613  C CB  . PHE   A 77  ? 0.4164 0.4016 0.5314 0.0226  0.0187  0.0193  83  PHE   A CB  
614  C CG  . PHE   A 77  ? 0.4595 0.4330 0.5731 0.0246  0.0301  0.0145  83  PHE   A CG  
615  C CD1 . PHE   A 77  ? 0.4775 0.4440 0.5928 0.0260  0.0277  0.0168  83  PHE   A CD1 
616  C CD2 . PHE   A 77  ? 0.4890 0.4564 0.5971 0.0245  0.0435  0.0076  83  PHE   A CD2 
617  C CE1 . PHE   A 77  ? 0.4999 0.4542 0.6134 0.0275  0.0383  0.0117  83  PHE   A CE1 
618  C CE2 . PHE   A 77  ? 0.5123 0.4661 0.6155 0.0258  0.0540  0.0024  83  PHE   A CE2 
619  C CZ  . PHE   A 77  ? 0.5052 0.4530 0.6117 0.0272  0.0512  0.0042  83  PHE   A CZ  
620  N N   . VAL   A 78  ? 0.3849 0.3563 0.4406 0.0136  0.0233  0.0081  84  VAL   A N   
621  C CA  . VAL   A 78  ? 0.3783 0.3430 0.4155 0.0110  0.0288  0.0017  84  VAL   A CA  
622  C C   . VAL   A 78  ? 0.3878 0.3390 0.4220 0.0123  0.0373  -0.0030 84  VAL   A C   
623  O O   . VAL   A 78  ? 0.3832 0.3296 0.4188 0.0125  0.0350  -0.0022 84  VAL   A O   
624  C CB  . VAL   A 78  ? 0.3775 0.3432 0.3982 0.0067  0.0215  0.0013  84  VAL   A CB  
625  C CG1 . VAL   A 78  ? 0.3935 0.3508 0.3961 0.0042  0.0247  -0.0048 84  VAL   A CG1 
626  C CG2 . VAL   A 78  ? 0.3669 0.3438 0.3890 0.0052  0.0149  0.0051  84  VAL   A CG2 
627  N N   . GLU   A 79  ? 0.3977 0.3412 0.4260 0.0128  0.0475  -0.0081 85  GLU   A N   
628  C CA  . GLU   A 79  ? 0.4145 0.3422 0.4365 0.0137  0.0571  -0.0137 85  GLU   A CA  
629  C C   . GLU   A 79  ? 0.4245 0.3422 0.4268 0.0099  0.0520  -0.0174 85  GLU   A C   
630  O O   . GLU   A 79  ? 0.4162 0.3379 0.4067 0.0064  0.0432  -0.0170 85  GLU   A O   
631  C CB  . GLU   A 79  ? 0.4649 0.3831 0.4764 0.0136  0.0694  -0.0188 85  GLU   A CB  
632  C CG  . GLU   A 79  ? 0.5717 0.4988 0.6073 0.0172  0.0768  -0.0158 85  GLU   A CG  
633  C CD  . GLU   A 79  ? 0.6996 0.6129 0.7309 0.0183  0.0945  -0.0213 85  GLU   A CD  
634  O OE1 . GLU   A 79  ? 0.7013 0.6180 0.7354 0.0181  0.1007  -0.0209 85  GLU   A OE1 
635  O OE2 . GLU   A 79  ? 0.7840 0.6817 0.8083 0.0190  0.1032  -0.0263 85  GLU   A OE2 
636  N N   . ALA   A 80  ? 0.4317 0.3359 0.4324 0.0107  0.0579  -0.0214 86  ALA   A N   
637  C CA  . ALA   A 80  ? 0.4449 0.3379 0.4287 0.0068  0.0534  -0.0258 86  ALA   A CA  
638  C C   . ALA   A 80  ? 0.4510 0.3351 0.4081 0.0025  0.0516  -0.0312 86  ALA   A C   
639  O O   . ALA   A 80  ? 0.4566 0.3344 0.4034 0.0031  0.0596  -0.0338 86  ALA   A O   
640  C CB  . ALA   A 80  ? 0.4498 0.3275 0.4359 0.0085  0.0620  -0.0302 86  ALA   A CB  
641  N N   . SER   A 81  ? 0.4413 0.3246 0.3882 -0.0018 0.0408  -0.0323 87  SER   A N   
642  C CA  . SER   A 81  ? 0.4503 0.3246 0.3732 -0.0062 0.0352  -0.0367 87  SER   A CA  
643  C C   . SER   A 81  ? 0.4721 0.3361 0.3873 -0.0104 0.0274  -0.0411 87  SER   A C   
644  O O   . SER   A 81  ? 0.4803 0.3435 0.4082 -0.0097 0.0288  -0.0408 87  SER   A O   
645  C CB  . SER   A 81  ? 0.4364 0.3261 0.3622 -0.0072 0.0265  -0.0320 87  SER   A CB  
646  O OG  . SER   A 81  ? 0.4245 0.3256 0.3642 -0.0087 0.0178  -0.0285 87  SER   A OG  
647  N N   . GLU   A 82  ? 0.4892 0.3450 0.3852 -0.0150 0.0183  -0.0447 88  GLU   A N   
648  C CA  . GLU   A 82  ? 0.5077 0.3554 0.4004 -0.0196 0.0089  -0.0487 88  GLU   A CA  
649  C C   . GLU   A 82  ? 0.4879 0.3535 0.4047 -0.0206 0.0009  -0.0435 88  GLU   A C   
650  O O   . GLU   A 82  ? 0.4977 0.3592 0.4199 -0.0239 -0.0045 -0.0458 88  GLU   A O   
651  C CB  . GLU   A 82  ? 0.5708 0.4030 0.4367 -0.0243 -0.0006 -0.0540 88  GLU   A CB  
652  C CG  . GLU   A 82  ? 0.6888 0.5325 0.5552 -0.0254 -0.0109 -0.0499 88  GLU   A CG  
653  C CD  . GLU   A 82  ? 0.8478 0.6750 0.6852 -0.0290 -0.0196 -0.0535 88  GLU   A CD  
654  O OE1 . GLU   A 82  ? 0.8969 0.7161 0.7153 -0.0273 -0.0125 -0.0534 88  GLU   A OE1 
655  O OE2 . GLU   A 82  ? 0.8807 0.7025 0.7148 -0.0335 -0.0340 -0.0560 88  GLU   A OE2 
656  N N   . TYR   A 83  ? 0.4553 0.3392 0.3867 -0.0179 0.0018  -0.0367 89  TYR   A N   
657  C CA  . TYR   A 83  ? 0.4285 0.3274 0.3790 -0.0190 -0.0034 -0.0317 89  TYR   A CA  
658  C C   . TYR   A 83  ? 0.4138 0.3198 0.3806 -0.0161 0.0027  -0.0265 89  TYR   A C   
659  O O   . TYR   A 83  ? 0.4109 0.3217 0.3900 -0.0181 0.0002  -0.0239 89  TYR   A O   
660  C CB  . TYR   A 83  ? 0.4253 0.3368 0.3771 -0.0187 -0.0075 -0.0282 89  TYR   A CB  
661  C CG  . TYR   A 83  ? 0.4508 0.3549 0.3875 -0.0217 -0.0160 -0.0321 89  TYR   A CG  
662  C CD1 . TYR   A 83  ? 0.4699 0.3726 0.4112 -0.0261 -0.0266 -0.0343 89  TYR   A CD1 
663  C CD2 . TYR   A 83  ? 0.4784 0.3761 0.3971 -0.0204 -0.0138 -0.0332 89  TYR   A CD2 
664  C CE1 . TYR   A 83  ? 0.4952 0.3902 0.4231 -0.0288 -0.0370 -0.0371 89  TYR   A CE1 
665  C CE2 . TYR   A 83  ? 0.5027 0.3914 0.4048 -0.0232 -0.0228 -0.0358 89  TYR   A CE2 
666  C CZ  . TYR   A 83  ? 0.5280 0.4154 0.4346 -0.0273 -0.0354 -0.0376 89  TYR   A CZ  
667  O OH  . TYR   A 83  ? 0.5858 0.4640 0.4771 -0.0300 -0.0469 -0.0394 89  TYR   A OH  
668  N N   . TYR   A 84  ? 0.4055 0.3121 0.3737 -0.0116 0.0105  -0.0245 90  TYR   A N   
669  C CA  . TYR   A 84  ? 0.3975 0.3094 0.3808 -0.0084 0.0144  -0.0188 90  TYR   A CA  
670  C C   . TYR   A 84  ? 0.4246 0.3282 0.4098 -0.0043 0.0230  -0.0201 90  TYR   A C   
671  O O   . TYR   A 84  ? 0.4316 0.3312 0.4086 -0.0027 0.0280  -0.0233 90  TYR   A O   
672  C CB  . TYR   A 84  ? 0.3741 0.3008 0.3645 -0.0065 0.0131  -0.0122 90  TYR   A CB  
673  C CG  . TYR   A 84  ? 0.3493 0.2849 0.3399 -0.0099 0.0070  -0.0104 90  TYR   A CG  
674  C CD1 . TYR   A 84  ? 0.3513 0.2894 0.3495 -0.0121 0.0054  -0.0069 90  TYR   A CD1 
675  C CD2 . TYR   A 84  ? 0.3541 0.2944 0.3378 -0.0109 0.0041  -0.0120 90  TYR   A CD2 
676  C CE1 . TYR   A 84  ? 0.3557 0.3011 0.3560 -0.0152 0.0021  -0.0058 90  TYR   A CE1 
677  C CE2 . TYR   A 84  ? 0.3477 0.2962 0.3346 -0.0136 -0.0005 -0.0105 90  TYR   A CE2 
678  C CZ  . TYR   A 84  ? 0.3476 0.2989 0.3434 -0.0156 -0.0008 -0.0076 90  TYR   A CZ  
679  O OH  . TYR   A 84  ? 0.3493 0.3075 0.3498 -0.0182 -0.0031 -0.0066 90  TYR   A OH  
680  N N   . PRO   A 85  ? 0.4299 0.3314 0.4278 -0.0020 0.0257  -0.0168 91  PRO   A N   
681  C CA  . PRO   A 85  ? 0.4407 0.3371 0.4469 0.0031  0.0342  -0.0168 91  PRO   A CA  
682  C C   . PRO   A 85  ? 0.4332 0.3429 0.4498 0.0069  0.0345  -0.0110 91  PRO   A C   
683  O O   . PRO   A 85  ? 0.4237 0.3451 0.4395 0.0054  0.0279  -0.0069 91  PRO   A O   
684  C CB  . PRO   A 85  ? 0.4547 0.3463 0.4732 0.0043  0.0344  -0.0133 91  PRO   A CB  
685  C CG  . PRO   A 85  ? 0.4594 0.3592 0.4792 0.0011  0.0265  -0.0078 91  PRO   A CG  
686  C CD  . PRO   A 85  ? 0.4346 0.3381 0.4413 -0.0036 0.0218  -0.0121 91  PRO   A CD  
687  N N   . ALA   A 86  ? 0.4361 0.3439 0.4645 0.0116  0.0424  -0.0108 92  ALA   A N   
688  C CA  . ALA   A 86  ? 0.4423 0.3627 0.4855 0.0151  0.0418  -0.0053 92  ALA   A CA  
689  C C   . ALA   A 86  ? 0.4362 0.3657 0.4895 0.0156  0.0319  0.0035  92  ALA   A C   
690  O O   . ALA   A 86  ? 0.4414 0.3650 0.4996 0.0162  0.0304  0.0062  92  ALA   A O   
691  C CB  . ALA   A 86  ? 0.4507 0.3668 0.5108 0.0203  0.0523  -0.0064 92  ALA   A CB  
692  N N   . ARG   A 87  ? 0.4122 0.3536 0.4642 0.0144  0.0251  0.0075  93  ARG   A N   
693  C CA  . ARG   A 87  ? 0.4007 0.3475 0.4553 0.0137  0.0158  0.0153  93  ARG   A CA  
694  C C   . ARG   A 87  ? 0.4033 0.3618 0.4595 0.0135  0.0102  0.0187  93  ARG   A C   
695  O O   . ARG   A 87  ? 0.4032 0.3661 0.4575 0.0131  0.0137  0.0148  93  ARG   A O   
696  C CB  . ARG   A 87  ? 0.4128 0.3560 0.4519 0.0087  0.0130  0.0143  93  ARG   A CB  
697  C CG  . ARG   A 87  ? 0.4207 0.3704 0.4470 0.0048  0.0111  0.0111  93  ARG   A CG  
698  C CD  . ARG   A 87  ? 0.4233 0.3681 0.4392 0.0005  0.0113  0.0067  93  ARG   A CD  
699  N NE  . ARG   A 87  ? 0.4175 0.3691 0.4265 -0.0032 0.0075  0.0071  93  ARG   A NE  
700  C CZ  . ARG   A 87  ? 0.4198 0.3769 0.4234 -0.0041 0.0068  0.0040  93  ARG   A CZ  
701  N NH1 . ARG   A 87  ? 0.3935 0.3499 0.3960 -0.0019 0.0099  0.0009  93  ARG   A NH1 
702  N NH2 . ARG   A 87  ? 0.3653 0.3277 0.3651 -0.0073 0.0040  0.0044  93  ARG   A NH2 
703  N N   . TYR   A 88  ? 0.4052 0.3667 0.4612 0.0128  0.0013  0.0258  94  TYR   A N   
704  C CA  . TYR   A 88  ? 0.4117 0.3823 0.4648 0.0113  -0.0047 0.0280  94  TYR   A CA  
705  C C   . TYR   A 88  ? 0.3865 0.3569 0.4205 0.0062  -0.0053 0.0259  94  TYR   A C   
706  O O   . TYR   A 88  ? 0.3896 0.3537 0.4152 0.0040  -0.0062 0.0278  94  TYR   A O   
707  C CB  . TYR   A 88  ? 0.4443 0.4152 0.5020 0.0122  -0.0150 0.0364  94  TYR   A CB  
708  C CG  . TYR   A 88  ? 0.4906 0.4639 0.5726 0.0174  -0.0173 0.0399  94  TYR   A CG  
709  C CD1 . TYR   A 88  ? 0.5091 0.4920 0.6061 0.0189  -0.0183 0.0392  94  TYR   A CD1 
710  C CD2 . TYR   A 88  ? 0.5202 0.4862 0.6133 0.0208  -0.0178 0.0438  94  TYR   A CD2 
711  C CE1 . TYR   A 88  ? 0.5297 0.5158 0.6543 0.0238  -0.0200 0.0424  94  TYR   A CE1 
712  C CE2 . TYR   A 88  ? 0.5373 0.5060 0.6572 0.0261  -0.0198 0.0472  94  TYR   A CE2 
713  C CZ  . TYR   A 88  ? 0.5502 0.5294 0.6871 0.0276  -0.0208 0.0464  94  TYR   A CZ  
714  O OH  . TYR   A 88  ? 0.5831 0.5657 0.7515 0.0328  -0.0225 0.0499  94  TYR   A OH  
715  N N   . GLN   A 89  ? 0.3525 0.3294 0.3812 0.0044  -0.0042 0.0222  95  GLN   A N   
716  C CA  . GLN   A 89  ? 0.3395 0.3172 0.3538 0.0000  -0.0050 0.0206  95  GLN   A CA  
717  C C   . GLN   A 89  ? 0.3264 0.3082 0.3365 -0.0015 -0.0114 0.0248  95  GLN   A C   
718  O O   . GLN   A 89  ? 0.3208 0.3084 0.3385 0.0001  -0.0142 0.0256  95  GLN   A O   
719  C CB  . GLN   A 89  ? 0.3478 0.3284 0.3583 -0.0010 -0.0008 0.0143  95  GLN   A CB  
720  C CG  . GLN   A 89  ? 0.3472 0.3302 0.3479 -0.0050 -0.0018 0.0126  95  GLN   A CG  
721  C CD  . GLN   A 89  ? 0.3442 0.3266 0.3409 -0.0060 0.0006  0.0070  95  GLN   A CD  
722  O OE1 . GLN   A 89  ? 0.3225 0.2989 0.3186 -0.0055 0.0029  0.0039  95  GLN   A OE1 
723  N NE2 . GLN   A 89  ? 0.3334 0.3208 0.3265 -0.0077 -0.0004 0.0057  95  GLN   A NE2 
724  N N   . SER   A 90  ? 0.3155 0.2929 0.3132 -0.0048 -0.0130 0.0271  96  SER   A N   
725  C CA  . SER   A 90  ? 0.3221 0.2995 0.3106 -0.0069 -0.0187 0.0305  96  SER   A CA  
726  C C   . SER   A 90  ? 0.3182 0.3004 0.2998 -0.0099 -0.0160 0.0260  96  SER   A C   
727  O O   . SER   A 90  ? 0.3210 0.3053 0.3039 -0.0107 -0.0104 0.0214  96  SER   A O   
728  C CB  . SER   A 90  ? 0.3467 0.3132 0.3218 -0.0093 -0.0203 0.0356  96  SER   A CB  
729  O OG  . SER   A 90  ? 0.3720 0.3349 0.3415 -0.0122 -0.0127 0.0328  96  SER   A OG  
730  N N   . HIS   A 91  ? 0.3142 0.2971 0.2888 -0.0117 -0.0208 0.0275  97  HIS   A N   
731  C CA  . HIS   A 91  ? 0.3196 0.3056 0.2875 -0.0145 -0.0183 0.0236  97  HIS   A CA  
732  C C   . HIS   A 91  ? 0.3135 0.3085 0.2927 -0.0127 -0.0151 0.0189  97  HIS   A C   
733  O O   . HIS   A 91  ? 0.3105 0.3074 0.2868 -0.0144 -0.0111 0.0152  97  HIS   A O   
734  C CB  . HIS   A 91  ? 0.3359 0.3155 0.2923 -0.0180 -0.0118 0.0223  97  HIS   A CB  
735  C CG  . HIS   A 91  ? 0.3785 0.3463 0.3192 -0.0205 -0.0133 0.0271  97  HIS   A CG  
736  N ND1 . HIS   A 91  ? 0.4282 0.3894 0.3520 -0.0240 -0.0145 0.0276  97  HIS   A ND1 
737  C CD2 . HIS   A 91  ? 0.3949 0.3546 0.3325 -0.0202 -0.0134 0.0314  97  HIS   A CD2 
738  C CE1 . HIS   A 91  ? 0.4450 0.3931 0.3534 -0.0260 -0.0152 0.0324  97  HIS   A CE1 
739  N NE2 . HIS   A 91  ? 0.4328 0.3800 0.3498 -0.0236 -0.0145 0.0352  97  HIS   A NE2 
740  N N   . LEU   A 92  ? 0.3004 0.2995 0.2922 -0.0093 -0.0164 0.0193  98  LEU   A N   
741  C CA  . LEU   A 92  ? 0.2963 0.3009 0.2957 -0.0078 -0.0122 0.0155  98  LEU   A CA  
742  C C   . LEU   A 92  ? 0.2843 0.2948 0.2901 -0.0078 -0.0151 0.0156  98  LEU   A C   
743  O O   . LEU   A 92  ? 0.2958 0.3075 0.3080 -0.0073 -0.0212 0.0191  98  LEU   A O   
744  C CB  . LEU   A 92  ? 0.2946 0.2974 0.3029 -0.0044 -0.0087 0.0150  98  LEU   A CB  
745  C CG  . LEU   A 92  ? 0.3121 0.3157 0.3225 -0.0032 -0.0027 0.0108  98  LEU   A CG  
746  C CD1 . LEU   A 92  ? 0.3134 0.3141 0.3129 -0.0054 -0.0010 0.0074  98  LEU   A CD1 
747  C CD2 . LEU   A 92  ? 0.3326 0.3318 0.3505 0.0000  0.0020  0.0101  98  LEU   A CD2 
748  N N   . MET   A 93  ? 0.2758 0.2893 0.2807 -0.0086 -0.0115 0.0122  99  MET   A N   
749  C CA  . MET   A 93  ? 0.2694 0.2881 0.2810 -0.0092 -0.0128 0.0118  99  MET   A CA  
750  C C   . MET   A 93  ? 0.2789 0.2990 0.2973 -0.0072 -0.0061 0.0096  99  MET   A C   
751  O O   . MET   A 93  ? 0.2911 0.3075 0.3014 -0.0070 -0.0017 0.0072  99  MET   A O   
752  C CB  . MET   A 93  ? 0.2896 0.3081 0.2910 -0.0125 -0.0136 0.0099  99  MET   A CB  
753  C CG  . MET   A 93  ? 0.3144 0.3280 0.3040 -0.0152 -0.0179 0.0114  99  MET   A CG  
754  S SD  . MET   A 93  ? 0.3476 0.3587 0.3255 -0.0189 -0.0152 0.0080  99  MET   A SD  
755  C CE  . MET   A 93  ? 0.3045 0.3159 0.2838 -0.0177 -0.0084 0.0056  99  MET   A CE  
756  N N   . LEU   A 94  ? 0.2671 0.2912 0.3001 -0.0059 -0.0050 0.0104  100 LEU   A N   
757  C CA  . LEU   A 94  ? 0.2621 0.2850 0.2995 -0.0044 0.0039  0.0083  100 LEU   A CA  
758  C C   . LEU   A 94  ? 0.2754 0.3016 0.3161 -0.0062 0.0053  0.0075  100 LEU   A C   
759  O O   . LEU   A 94  ? 0.2757 0.3074 0.3242 -0.0080 -0.0007 0.0086  100 LEU   A O   
760  C CB  . LEU   A 94  ? 0.2635 0.2871 0.3187 -0.0012 0.0084  0.0094  100 LEU   A CB  
761  C CG  . LEU   A 94  ? 0.2990 0.3187 0.3549 0.0012  0.0080  0.0104  100 LEU   A CG  
762  C CD1 . LEU   A 94  ? 0.3165 0.3362 0.3926 0.0047  0.0150  0.0108  100 LEU   A CD1 
763  C CD2 . LEU   A 94  ? 0.3244 0.3359 0.3612 0.0008  0.0115  0.0076  100 LEU   A CD2 
764  N N   . ALA   A 95  ? 0.2849 0.3064 0.3192 -0.0060 0.0132  0.0055  101 ALA   A N   
765  C CA  . ALA   A 95  ? 0.2765 0.2989 0.3137 -0.0074 0.0172  0.0050  101 ALA   A CA  
766  C C   . ALA   A 95  ? 0.2883 0.3039 0.3260 -0.0058 0.0289  0.0041  101 ALA   A C   
767  O O   . ALA   A 95  ? 0.3062 0.3143 0.3346 -0.0041 0.0331  0.0030  101 ALA   A O   
768  C CB  . ALA   A 95  ? 0.2931 0.3122 0.3143 -0.0093 0.0151  0.0039  101 ALA   A CB  
769  N N   . VAL   A 96  ? 0.2777 0.2945 0.3251 -0.0068 0.0348  0.0043  102 VAL   A N   
770  C CA  . VAL   A 96  ? 0.2806 0.2885 0.3254 -0.0060 0.0482  0.0035  102 VAL   A CA  
771  C C   . VAL   A 96  ? 0.3093 0.3067 0.3283 -0.0074 0.0490  0.0030  102 VAL   A C   
772  O O   . VAL   A 96  ? 0.3134 0.3131 0.3307 -0.0093 0.0452  0.0038  102 VAL   A O   
773  C CB  . VAL   A 96  ? 0.2921 0.3055 0.3610 -0.0069 0.0550  0.0044  102 VAL   A CB  
774  C CG1 . VAL   A 96  ? 0.3135 0.3147 0.3756 -0.0068 0.0714  0.0036  102 VAL   A CG1 
775  C CG2 . VAL   A 96  ? 0.2752 0.2989 0.3726 -0.0051 0.0522  0.0054  102 VAL   A CG2 
776  N N   . GLY   A 97  ? 0.3309 0.3161 0.3303 -0.0064 0.0527  0.0017  103 GLY   A N   
777  C CA  . GLY   A 97  ? 0.3659 0.3397 0.3403 -0.0076 0.0507  0.0018  103 GLY   A CA  
778  C C   . GLY   A 97  ? 0.3867 0.3463 0.3398 -0.0068 0.0526  -0.0001 103 GLY   A C   
779  O O   . GLY   A 97  ? 0.3846 0.3440 0.3425 -0.0053 0.0555  -0.0018 103 GLY   A O   
780  N N   . HIS   A 98  ? 0.3965 0.3433 0.3258 -0.0080 0.0499  0.0002  104 HIS   A N   
781  C CA  . HIS   A 98  ? 0.4146 0.3454 0.3201 -0.0082 0.0495  -0.0018 104 HIS   A CA  
782  C C   . HIS   A 98  ? 0.4115 0.3463 0.3152 -0.0082 0.0364  -0.0030 104 HIS   A C   
783  O O   . HIS   A 98  ? 0.4052 0.3479 0.3138 -0.0087 0.0262  -0.0015 104 HIS   A O   
784  C CB  . HIS   A 98  ? 0.4396 0.3510 0.3172 -0.0098 0.0519  -0.0006 104 HIS   A CB  
785  C CG  . HIS   A 98  ? 0.4754 0.3670 0.3244 -0.0107 0.0506  -0.0030 104 HIS   A CG  
786  N ND1 . HIS   A 98  ? 0.5110 0.3897 0.3501 -0.0105 0.0636  -0.0062 104 HIS   A ND1 
787  C CD2 . HIS   A 98  ? 0.4961 0.3798 0.3278 -0.0118 0.0372  -0.0032 104 HIS   A CD2 
788  C CE1 . HIS   A 98  ? 0.5313 0.3931 0.3436 -0.0119 0.0575  -0.0086 104 HIS   A CE1 
789  N NE2 . HIS   A 98  ? 0.5274 0.3917 0.3348 -0.0128 0.0408  -0.0066 104 HIS   A NE2 
790  N N   . SER   A 99  ? 0.4175 0.3450 0.3139 -0.0078 0.0378  -0.0059 105 SER   A N   
791  C CA  . SER   A 99  ? 0.4277 0.3558 0.3211 -0.0083 0.0269  -0.0074 105 SER   A CA  
792  C C   . SER   A 99  ? 0.4541 0.3644 0.3278 -0.0088 0.0309  -0.0112 105 SER   A C   
793  O O   . SER   A 99  ? 0.4766 0.3830 0.3531 -0.0075 0.0428  -0.0129 105 SER   A O   
794  C CB  . SER   A 99  ? 0.4375 0.3830 0.3550 -0.0071 0.0235  -0.0069 105 SER   A CB  
795  O OG  . SER   A 99  ? 0.4897 0.4344 0.4041 -0.0081 0.0141  -0.0083 105 SER   A OG  
796  N N   . GLU   A 100 ? 0.4507 0.3499 0.3062 -0.0107 0.0211  -0.0127 106 GLU   A N   
797  C CA  . GLU   A 100 ? 0.4879 0.3677 0.3210 -0.0121 0.0226  -0.0170 106 GLU   A CA  
798  C C   . GLU   A 100 ? 0.4916 0.3752 0.3299 -0.0133 0.0097  -0.0187 106 GLU   A C   
799  O O   . GLU   A 100 ? 0.4814 0.3769 0.3322 -0.0137 -0.0013 -0.0162 106 GLU   A O   
800  C CB  . GLU   A 100 ? 0.5358 0.3936 0.3356 -0.0146 0.0191  -0.0169 106 GLU   A CB  
801  C CG  . GLU   A 100 ? 0.6460 0.4867 0.4255 -0.0148 0.0343  -0.0173 106 GLU   A CG  
802  C CD  . GLU   A 100 ? 0.6327 0.4538 0.3802 -0.0175 0.0256  -0.0154 106 GLU   A CD  
803  O OE1 . GLU   A 100 ? 0.6432 0.4470 0.3663 -0.0200 0.0156  -0.0180 106 GLU   A OE1 
804  O OE2 . GLU   A 100 ? 0.6138 0.4369 0.3616 -0.0171 0.0274  -0.0110 106 GLU   A OE2 
805  N N   . PRO   A 101 ? 0.5122 0.3826 0.3386 -0.0145 0.0104  -0.0233 107 PRO   A N   
806  C CA  . PRO   A 101 ? 0.5179 0.3890 0.3471 -0.0166 -0.0031 -0.0252 107 PRO   A CA  
807  C C   . PRO   A 101 ? 0.5139 0.3826 0.3353 -0.0189 -0.0186 -0.0232 107 PRO   A C   
808  O O   . PRO   A 101 ? 0.5320 0.3839 0.3275 -0.0202 -0.0204 -0.0228 107 PRO   A O   
809  C CB  . PRO   A 101 ? 0.5431 0.3926 0.3500 -0.0184 0.0007  -0.0311 107 PRO   A CB  
810  C CG  . PRO   A 101 ? 0.5493 0.3964 0.3578 -0.0155 0.0196  -0.0319 107 PRO   A CG  
811  C CD  . PRO   A 101 ? 0.5200 0.3727 0.3294 -0.0143 0.0242  -0.0275 107 PRO   A CD  
812  N N   . GLY   A 102 ? 0.4841 0.3694 0.3292 -0.0190 -0.0284 -0.0212 108 GLY   A N   
813  C CA  . GLY   A 102 ? 0.4708 0.3579 0.3181 -0.0204 -0.0427 -0.0187 108 GLY   A CA  
814  C C   . GLY   A 102 ? 0.4502 0.3561 0.3196 -0.0182 -0.0412 -0.0141 108 GLY   A C   
815  O O   . GLY   A 102 ? 0.4488 0.3614 0.3307 -0.0188 -0.0518 -0.0121 108 GLY   A O   
816  N N   . ASP   A 103 ? 0.4174 0.3319 0.2936 -0.0158 -0.0281 -0.0128 109 ASP   A N   
817  C CA  . ASP   A 103 ? 0.3911 0.3211 0.2850 -0.0141 -0.0255 -0.0092 109 ASP   A CA  
818  C C   . ASP   A 103 ? 0.3544 0.3021 0.2742 -0.0137 -0.0253 -0.0088 109 ASP   A C   
819  O O   . ASP   A 103 ? 0.3396 0.2986 0.2732 -0.0130 -0.0248 -0.0065 109 ASP   A O   
820  C CB  . ASP   A 103 ? 0.4063 0.3361 0.2957 -0.0124 -0.0131 -0.0079 109 ASP   A CB  
821  C CG  . ASP   A 103 ? 0.4317 0.3465 0.2989 -0.0129 -0.0123 -0.0064 109 ASP   A CG  
822  O OD1 . ASP   A 103 ? 0.4288 0.3389 0.2901 -0.0139 -0.0230 -0.0046 109 ASP   A OD1 
823  O OD2 . ASP   A 103 ? 0.4343 0.3416 0.2913 -0.0124 -0.0008 -0.0068 109 ASP   A OD2 
824  N N   . CYS   A 104 ? 0.3504 0.2987 0.2755 -0.0144 -0.0253 -0.0111 110 CYS   A N   
825  C CA  . CYS   A 104 ? 0.3464 0.3087 0.2929 -0.0145 -0.0242 -0.0102 110 CYS   A CA  
826  C C   . CYS   A 104 ? 0.3379 0.3073 0.2982 -0.0156 -0.0312 -0.0091 110 CYS   A C   
827  O O   . CYS   A 104 ? 0.3460 0.3094 0.3037 -0.0169 -0.0407 -0.0097 110 CYS   A O   
828  C CB  . CYS   A 104 ? 0.3717 0.3315 0.3211 -0.0154 -0.0234 -0.0123 110 CYS   A CB  
829  S SG  . CYS   A 104 ? 0.4058 0.3594 0.3465 -0.0132 -0.0132 -0.0134 110 CYS   A SG  
830  N N   . GLY   A 105 ? 0.3138 0.2946 0.2889 -0.0153 -0.0270 -0.0075 111 GLY   A N   
831  C CA  . GLY   A 105 ? 0.3209 0.3084 0.3121 -0.0162 -0.0306 -0.0069 111 GLY   A CA  
832  C C   . GLY   A 105 ? 0.3259 0.3168 0.3184 -0.0149 -0.0298 -0.0050 111 GLY   A C   
833  O O   . GLY   A 105 ? 0.3313 0.3286 0.3392 -0.0152 -0.0297 -0.0046 111 GLY   A O   
834  N N   . GLY   A 106 ? 0.3173 0.3029 0.2949 -0.0136 -0.0283 -0.0041 112 GLY   A N   
835  C CA  . GLY   A 106 ? 0.3080 0.2960 0.2867 -0.0127 -0.0268 -0.0023 112 GLY   A CA  
836  C C   . GLY   A 106 ? 0.3018 0.2996 0.2911 -0.0128 -0.0195 -0.0022 112 GLY   A C   
837  O O   . GLY   A 106 ? 0.2953 0.2955 0.2830 -0.0130 -0.0146 -0.0026 112 GLY   A O   
838  N N   . ILE   A 107 ? 0.2931 0.2951 0.2929 -0.0128 -0.0192 -0.0018 113 ILE   A N   
839  C CA  . ILE   A 107 ? 0.3003 0.3084 0.3063 -0.0136 -0.0122 -0.0025 113 ILE   A CA  
840  C C   . ILE   A 107 ? 0.2897 0.2982 0.2879 -0.0133 -0.0082 -0.0019 113 ILE   A C   
841  O O   . ILE   A 107 ? 0.2962 0.3013 0.2897 -0.0124 -0.0094 -0.0007 113 ILE   A O   
842  C CB  . ILE   A 107 ? 0.3303 0.3416 0.3520 -0.0139 -0.0114 -0.0033 113 ILE   A CB  
843  C CG1 . ILE   A 107 ? 0.3586 0.3720 0.3924 -0.0152 -0.0112 -0.0044 113 ILE   A CG1 
844  C CG2 . ILE   A 107 ? 0.3444 0.3580 0.3671 -0.0148 -0.0040 -0.0044 113 ILE   A CG2 
845  C CD1 . ILE   A 107 ? 0.3931 0.4094 0.4474 -0.0152 -0.0108 -0.0052 113 ILE   A CD1 
846  N N   . LEU   A 108 ? 0.2711 0.2825 0.2681 -0.0145 -0.0040 -0.0025 114 LEU   A N   
847  C CA  . LEU   A 108 ? 0.2643 0.2772 0.2580 -0.0150 -0.0014 -0.0023 114 LEU   A CA  
848  C C   . LEU   A 108 ? 0.2669 0.2809 0.2644 -0.0169 0.0017  -0.0040 114 LEU   A C   
849  O O   . LEU   A 108 ? 0.2672 0.2810 0.2655 -0.0182 0.0039  -0.0049 114 LEU   A O   
850  C CB  . LEU   A 108 ? 0.2632 0.2772 0.2530 -0.0151 -0.0010 -0.0015 114 LEU   A CB  
851  C CG  . LEU   A 108 ? 0.2747 0.2909 0.2645 -0.0164 -0.0003 -0.0014 114 LEU   A CG  
852  C CD1 . LEU   A 108 ? 0.2784 0.2947 0.2701 -0.0156 0.0008  -0.0008 114 LEU   A CD1 
853  C CD2 . LEU   A 108 ? 0.2877 0.3049 0.2765 -0.0165 -0.0021 0.0000  114 LEU   A CD2 
854  N N   . ARG   A 109 ? 0.2647 0.2783 0.2640 -0.0172 0.0029  -0.0047 115 ARG   A N   
855  C CA  . ARG   A 109 ? 0.2802 0.2928 0.2823 -0.0190 0.0069  -0.0072 115 ARG   A CA  
856  C C   . ARG   A 109 ? 0.2880 0.2996 0.2853 -0.0209 0.0078  -0.0083 115 ARG   A C   
857  O O   . ARG   A 109 ? 0.2826 0.2953 0.2800 -0.0202 0.0059  -0.0069 115 ARG   A O   
858  C CB  . ARG   A 109 ? 0.3219 0.3339 0.3347 -0.0174 0.0070  -0.0072 115 ARG   A CB  
859  C CG  . ARG   A 109 ? 0.4486 0.4585 0.4673 -0.0184 0.0121  -0.0098 115 ARG   A CG  
860  C CD  . ARG   A 109 ? 0.5269 0.5366 0.5593 -0.0159 0.0102  -0.0086 115 ARG   A CD  
861  N NE  . ARG   A 109 ? 0.5877 0.5994 0.6295 -0.0144 0.0066  -0.0074 115 ARG   A NE  
862  C CZ  . ARG   A 109 ? 0.6207 0.6338 0.6732 -0.0152 0.0112  -0.0094 115 ARG   A CZ  
863  N NH1 . ARG   A 109 ? 0.6216 0.6324 0.6735 -0.0174 0.0205  -0.0128 115 ARG   A NH1 
864  N NH2 . ARG   A 109 ? 0.6161 0.6316 0.6796 -0.0142 0.0068  -0.0082 115 ARG   A NH2 
865  N N   . CYS   A 110 ? 0.2981 0.3064 0.2907 -0.0237 0.0111  -0.0111 116 CYS   A N   
866  C CA  . CYS   A 110 ? 0.3129 0.3187 0.3009 -0.0263 0.0109  -0.0130 116 CYS   A CA  
867  C C   . CYS   A 110 ? 0.3439 0.3444 0.3339 -0.0277 0.0173  -0.0169 116 CYS   A C   
868  O O   . CYS   A 110 ? 0.3518 0.3524 0.3502 -0.0259 0.0212  -0.0172 116 CYS   A O   
869  C CB  . CYS   A 110 ? 0.3188 0.3222 0.2952 -0.0292 0.0078  -0.0132 116 CYS   A CB  
870  S SG  . CYS   A 110 ? 0.3321 0.3272 0.2964 -0.0317 0.0133  -0.0154 116 CYS   A SG  
871  N N   . GLN   A 111 ? 0.3627 0.3581 0.3465 -0.0309 0.0183  -0.0201 117 GLN   A N   
872  C CA  . GLN   A 111 ? 0.3906 0.3791 0.3754 -0.0323 0.0258  -0.0244 117 GLN   A CA  
873  C C   . GLN   A 111 ? 0.4139 0.3964 0.3930 -0.0336 0.0335  -0.0269 117 GLN   A C   
874  O O   . GLN   A 111 ? 0.4383 0.4160 0.4237 -0.0336 0.0420  -0.0303 117 GLN   A O   
875  C CB  . GLN   A 111 ? 0.4313 0.4134 0.4073 -0.0363 0.0251  -0.0282 117 GLN   A CB  
876  C CG  . GLN   A 111 ? 0.4869 0.4630 0.4439 -0.0406 0.0213  -0.0296 117 GLN   A CG  
877  C CD  . GLN   A 111 ? 0.5862 0.5558 0.5354 -0.0450 0.0179  -0.0333 117 GLN   A CD  
878  O OE1 . GLN   A 111 ? 0.6045 0.5789 0.5563 -0.0460 0.0090  -0.0314 117 GLN   A OE1 
879  N NE2 . GLN   A 111 ? 0.5965 0.5546 0.5371 -0.0480 0.0251  -0.0390 117 GLN   A NE2 
880  N N   . HIS   A 112 ? 0.4024 0.3841 0.3708 -0.0346 0.0316  -0.0252 118 HIS   A N   
881  C CA  . HIS   A 112 ? 0.4025 0.3764 0.3632 -0.0365 0.0401  -0.0272 118 HIS   A CA  
882  C C   . HIS   A 112 ? 0.3979 0.3780 0.3748 -0.0334 0.0435  -0.0249 118 HIS   A C   
883  O O   . HIS   A 112 ? 0.4248 0.3990 0.4011 -0.0348 0.0530  -0.0267 118 HIS   A O   
884  C CB  . HIS   A 112 ? 0.4173 0.3835 0.3546 -0.0402 0.0365  -0.0265 118 HIS   A CB  
885  C CG  . HIS   A 112 ? 0.4382 0.3976 0.3603 -0.0439 0.0309  -0.0288 118 HIS   A CG  
886  N ND1 . HIS   A 112 ? 0.4502 0.4160 0.3729 -0.0436 0.0189  -0.0257 118 HIS   A ND1 
887  C CD2 . HIS   A 112 ? 0.4565 0.4026 0.3632 -0.0483 0.0358  -0.0342 118 HIS   A CD2 
888  C CE1 . HIS   A 112 ? 0.4621 0.4198 0.3722 -0.0478 0.0153  -0.0290 118 HIS   A CE1 
889  N NE2 . HIS   A 112 ? 0.4685 0.4133 0.3668 -0.0509 0.0251  -0.0344 118 HIS   A NE2 
890  N N   . GLY   A 113 ? 0.3586 0.3491 0.3490 -0.0296 0.0360  -0.0211 119 GLY   A N   
891  C CA  . GLY   A 113 ? 0.3471 0.3430 0.3527 -0.0270 0.0363  -0.0191 119 GLY   A CA  
892  C C   . GLY   A 113 ? 0.3294 0.3313 0.3333 -0.0252 0.0273  -0.0150 119 GLY   A C   
893  O O   . GLY   A 113 ? 0.3171 0.3214 0.3153 -0.0245 0.0208  -0.0133 119 GLY   A O   
894  N N   . VAL   A 114 ? 0.3229 0.3267 0.3333 -0.0246 0.0278  -0.0137 120 VAL   A N   
895  C CA  . VAL   A 114 ? 0.3189 0.3265 0.3280 -0.0231 0.0205  -0.0106 120 VAL   A CA  
896  C C   . VAL   A 114 ? 0.3246 0.3290 0.3174 -0.0248 0.0194  -0.0093 120 VAL   A C   
897  O O   . VAL   A 114 ? 0.3349 0.3332 0.3195 -0.0273 0.0248  -0.0099 120 VAL   A O   
898  C CB  . VAL   A 114 ? 0.3294 0.3394 0.3526 -0.0223 0.0210  -0.0101 120 VAL   A CB  
899  C CG1 . VAL   A 114 ? 0.3454 0.3571 0.3646 -0.0213 0.0142  -0.0077 120 VAL   A CG1 
900  C CG2 . VAL   A 114 ? 0.3307 0.3441 0.3728 -0.0203 0.0190  -0.0106 120 VAL   A CG2 
901  N N   . VAL   A 115 ? 0.3057 0.3130 0.2941 -0.0233 0.0126  -0.0071 121 VAL   A N   
902  C CA  . VAL   A 115 ? 0.3001 0.3054 0.2774 -0.0241 0.0094  -0.0051 121 VAL   A CA  
903  C C   . VAL   A 115 ? 0.3002 0.3066 0.2800 -0.0226 0.0074  -0.0028 121 VAL   A C   
904  O O   . VAL   A 115 ? 0.3144 0.3170 0.2867 -0.0236 0.0071  -0.0009 121 VAL   A O   
905  C CB  . VAL   A 115 ? 0.3010 0.3095 0.2776 -0.0232 0.0043  -0.0043 121 VAL   A CB  
906  C CG1 . VAL   A 115 ? 0.3001 0.3081 0.2710 -0.0234 -0.0006 -0.0016 121 VAL   A CG1 
907  C CG2 . VAL   A 115 ? 0.3076 0.3144 0.2820 -0.0252 0.0058  -0.0068 121 VAL   A CG2 
908  N N   . GLY   A 116 ? 0.2773 0.2874 0.2658 -0.0202 0.0051  -0.0028 122 GLY   A N   
909  C CA  . GLY   A 116 ? 0.2851 0.2949 0.2750 -0.0190 0.0030  -0.0014 122 GLY   A CA  
910  C C   . GLY   A 116 ? 0.2777 0.2887 0.2732 -0.0171 -0.0003 -0.0021 122 GLY   A C   
911  O O   . GLY   A 116 ? 0.2825 0.2946 0.2823 -0.0167 -0.0011 -0.0030 122 GLY   A O   
912  N N   . ILE   A 117 ? 0.2782 0.2871 0.2726 -0.0162 -0.0025 -0.0017 123 ILE   A N   
913  C CA  . ILE   A 117 ? 0.2774 0.2840 0.2722 -0.0151 -0.0066 -0.0026 123 ILE   A CA  
914  C C   . ILE   A 117 ? 0.2886 0.2916 0.2754 -0.0134 -0.0069 -0.0022 123 ILE   A C   
915  O O   . ILE   A 117 ? 0.2941 0.2970 0.2803 -0.0131 -0.0050 -0.0013 123 ILE   A O   
916  C CB  . ILE   A 117 ? 0.3024 0.3076 0.3051 -0.0163 -0.0092 -0.0038 123 ILE   A CB  
917  C CG1 . ILE   A 117 ? 0.3273 0.3313 0.3307 -0.0174 -0.0062 -0.0033 123 ILE   A CG1 
918  C CG2 . ILE   A 117 ? 0.3193 0.3279 0.3347 -0.0173 -0.0091 -0.0045 123 ILE   A CG2 
919  C CD1 . ILE   A 117 ? 0.3584 0.3606 0.3712 -0.0190 -0.0087 -0.0047 123 ILE   A CD1 
920  N N   . VAL   A 118 ? 0.2747 0.2730 0.2550 -0.0124 -0.0088 -0.0029 124 VAL   A N   
921  C CA  . VAL   A 118 ? 0.2651 0.2576 0.2372 -0.0111 -0.0066 -0.0033 124 VAL   A CA  
922  C C   . VAL   A 118 ? 0.2785 0.2673 0.2509 -0.0113 -0.0072 -0.0044 124 VAL   A C   
923  O O   . VAL   A 118 ? 0.2874 0.2740 0.2615 -0.0128 -0.0115 -0.0057 124 VAL   A O   
924  C CB  . VAL   A 118 ? 0.2684 0.2523 0.2288 -0.0107 -0.0081 -0.0041 124 VAL   A CB  
925  C CG1 . VAL   A 118 ? 0.2828 0.2575 0.2326 -0.0098 -0.0036 -0.0054 124 VAL   A CG1 
926  C CG2 . VAL   A 118 ? 0.2727 0.2590 0.2329 -0.0104 -0.0063 -0.0025 124 VAL   A CG2 
927  N N   . SER   A 119 ? 0.2810 0.2690 0.2537 -0.0099 -0.0031 -0.0038 125 SER   A N   
928  C CA  . SER   A 119 ? 0.3003 0.2838 0.2737 -0.0099 -0.0028 -0.0047 125 SER   A CA  
929  C C   . SER   A 119 ? 0.3276 0.3035 0.2955 -0.0080 0.0019  -0.0062 125 SER   A C   
930  O O   . SER   A 119 ? 0.3337 0.3018 0.2977 -0.0083 0.0019  -0.0084 125 SER   A O   
931  C CB  . SER   A 119 ? 0.3145 0.3035 0.2965 -0.0101 -0.0023 -0.0020 125 SER   A CB  
932  O OG  . SER   A 119 ? 0.3317 0.3156 0.3151 -0.0101 -0.0017 -0.0022 125 SER   A OG  
933  N N   . THR   A 120 ? 0.3289 0.3063 0.2977 -0.0062 0.0068  -0.0052 126 THR   A N   
934  C CA  . THR   A 120 ? 0.3357 0.3054 0.3021 -0.0041 0.0141  -0.0068 126 THR   A CA  
935  C C   . THR   A 120 ? 0.3474 0.3138 0.3074 -0.0037 0.0196  -0.0073 126 THR   A C   
936  O O   . THR   A 120 ? 0.3367 0.3089 0.2975 -0.0046 0.0172  -0.0056 126 THR   A O   
937  C CB  . THR   A 120 ? 0.3586 0.3341 0.3412 -0.0016 0.0169  -0.0042 126 THR   A CB  
938  O OG1 . THR   A 120 ? 0.3755 0.3603 0.3685 -0.0009 0.0173  -0.0013 126 THR   A OG1 
939  C CG2 . THR   A 120 ? 0.3582 0.3363 0.3464 -0.0021 0.0120  -0.0023 126 THR   A CG2 
940  N N   . GLY   A 121 ? 0.3723 0.3286 0.3267 -0.0024 0.0283  -0.0095 127 GLY   A N   
941  C CA  . GLY   A 121 ? 0.4118 0.3632 0.3602 -0.0023 0.0362  -0.0098 127 GLY   A CA  
942  C C   . GLY   A 121 ? 0.4434 0.3842 0.3906 -0.0006 0.0489  -0.0123 127 GLY   A C   
943  O O   . GLY   A 121 ? 0.4378 0.3771 0.3926 0.0011  0.0512  -0.0135 127 GLY   A O   
944  N N   . GLY   A 122 ? 0.4848 0.4163 0.4210 -0.0011 0.0578  -0.0131 128 GLY   A N   
945  C CA  . GLY   A 122 ? 0.5088 0.4271 0.4412 0.0001  0.0734  -0.0160 128 GLY   A CA  
946  C C   . GLY   A 122 ? 0.5047 0.4337 0.4646 0.0023  0.0829  -0.0138 128 GLY   A C   
947  O O   . GLY   A 122 ? 0.4941 0.4410 0.4775 0.0033  0.0752  -0.0103 128 GLY   A O   
948  N N   . ASN   A 123 ? 0.5134 0.4303 0.4707 0.0029  0.0998  -0.0160 129 ASN   A N   
949  C CA  . ASN   A 123 ? 0.5087 0.4349 0.4959 0.0048  0.1106  -0.0142 129 ASN   A CA  
950  C C   . ASN   A 123 ? 0.4844 0.4235 0.4820 0.0032  0.1053  -0.0103 129 ASN   A C   
951  O O   . ASN   A 123 ? 0.4801 0.4334 0.5093 0.0045  0.1069  -0.0079 129 ASN   A O   
952  C CB  . ASN   A 123 ? 0.5257 0.4653 0.5462 0.0084  0.1083  -0.0130 129 ASN   A CB  
953  C CG  . ASN   A 123 ? 0.6042 0.5312 0.6211 0.0105  0.1168  -0.0169 129 ASN   A CG  
954  O OD1 . ASN   A 123 ? 0.6321 0.5385 0.6251 0.0094  0.1297  -0.0216 129 ASN   A OD1 
955  N ND2 . ASN   A 123 ? 0.6167 0.5541 0.6565 0.0134  0.1099  -0.0151 129 ASN   A ND2 
956  N N   . GLY   A 124 ? 0.4637 0.3974 0.4364 0.0004  0.0986  -0.0096 130 GLY   A N   
957  C CA  . GLY   A 124 ? 0.4255 0.3696 0.4064 -0.0011 0.0939  -0.0063 130 GLY   A CA  
958  C C   . GLY   A 124 ? 0.3785 0.3422 0.3774 -0.0010 0.0779  -0.0036 130 GLY   A C   
959  O O   . GLY   A 124 ? 0.3741 0.3477 0.3848 -0.0022 0.0742  -0.0014 130 GLY   A O   
960  N N   . LEU   A 125 ? 0.3648 0.3321 0.3632 0.0001  0.0686  -0.0041 131 LEU   A N   
961  C CA  . LEU   A 125 ? 0.3509 0.3330 0.3614 -0.0001 0.0547  -0.0017 131 LEU   A CA  
962  C C   . LEU   A 125 ? 0.3633 0.3418 0.3535 -0.0015 0.0448  -0.0025 131 LEU   A C   
963  O O   . LEU   A 125 ? 0.4078 0.3739 0.3798 -0.0016 0.0468  -0.0049 131 LEU   A O   
964  C CB  . LEU   A 125 ? 0.3424 0.3317 0.3741 0.0025  0.0532  -0.0008 131 LEU   A CB  
965  C CG  . LEU   A 125 ? 0.3322 0.3287 0.3929 0.0042  0.0601  0.0006  131 LEU   A CG  
966  C CD1 . LEU   A 125 ? 0.3542 0.3532 0.4335 0.0074  0.0600  0.0014  131 LEU   A CD1 
967  C CD2 . LEU   A 125 ? 0.3150 0.3246 0.3910 0.0024  0.0518  0.0034  131 LEU   A CD2 
968  N N   . VAL   A 126 ? 0.3189 0.3072 0.3125 -0.0028 0.0346  -0.0007 132 VAL   A N   
969  C CA  . VAL   A 126 ? 0.3175 0.3041 0.2983 -0.0040 0.0262  -0.0013 132 VAL   A CA  
970  C C   . VAL   A 126 ? 0.3016 0.2986 0.2943 -0.0041 0.0189  0.0004  132 VAL   A C   
971  O O   . VAL   A 126 ? 0.2990 0.3044 0.3041 -0.0044 0.0170  0.0023  132 VAL   A O   
972  C CB  . VAL   A 126 ? 0.3250 0.3092 0.2944 -0.0059 0.0228  -0.0011 132 VAL   A CB  
973  C CG1 . VAL   A 126 ? 0.3398 0.3324 0.3203 -0.0067 0.0231  0.0006  132 VAL   A CG1 
974  C CG2 . VAL   A 126 ? 0.3287 0.3141 0.2928 -0.0070 0.0138  -0.0015 132 VAL   A CG2 
975  N N   . GLY   A 127 ? 0.2853 0.2801 0.2738 -0.0041 0.0150  -0.0001 133 GLY   A N   
976  C CA  . GLY   A 127 ? 0.2816 0.2832 0.2776 -0.0045 0.0092  0.0020  133 GLY   A CA  
977  C C   . GLY   A 127 ? 0.2829 0.2848 0.2717 -0.0067 0.0042  0.0015  133 GLY   A C   
978  O O   . GLY   A 127 ? 0.2917 0.2880 0.2723 -0.0073 0.0037  -0.0005 133 GLY   A O   
979  N N   . PHE   A 128 ? 0.2697 0.2771 0.2617 -0.0082 0.0006  0.0032  134 PHE   A N   
980  C CA  . PHE   A 128 ? 0.2652 0.2729 0.2530 -0.0104 -0.0017 0.0025  134 PHE   A CA  
981  C C   . PHE   A 128 ? 0.2758 0.2830 0.2638 -0.0114 -0.0032 0.0042  134 PHE   A C   
982  O O   . PHE   A 128 ? 0.2691 0.2775 0.2585 -0.0113 -0.0051 0.0067  134 PHE   A O   
983  C CB  . PHE   A 128 ? 0.2552 0.2667 0.2432 -0.0119 -0.0022 0.0023  134 PHE   A CB  
984  C CG  . PHE   A 128 ? 0.2578 0.2692 0.2458 -0.0111 -0.0003 0.0015  134 PHE   A CG  
985  C CD1 . PHE   A 128 ? 0.2636 0.2714 0.2468 -0.0111 -0.0004 0.0002  134 PHE   A CD1 
986  C CD2 . PHE   A 128 ? 0.2683 0.2824 0.2616 -0.0106 0.0013  0.0024  134 PHE   A CD2 
987  C CE1 . PHE   A 128 ? 0.2747 0.2796 0.2546 -0.0105 0.0017  0.0003  134 PHE   A CE1 
988  C CE2 . PHE   A 128 ? 0.2770 0.2895 0.2700 -0.0102 0.0048  0.0019  134 PHE   A CE2 
989  C CZ  . PHE   A 128 ? 0.2709 0.2779 0.2552 -0.0102 0.0053  0.0011  134 PHE   A CZ  
990  N N   . ALA   A 129 ? 0.2709 0.2756 0.2575 -0.0127 -0.0029 0.0033  135 ALA   A N   
991  C CA  . ALA   A 129 ? 0.2822 0.2844 0.2674 -0.0142 -0.0026 0.0051  135 ALA   A CA  
992  C C   . ALA   A 129 ? 0.2827 0.2858 0.2644 -0.0167 -0.0014 0.0051  135 ALA   A C   
993  O O   . ALA   A 129 ? 0.2859 0.2904 0.2703 -0.0178 0.0004  0.0028  135 ALA   A O   
994  C CB  . ALA   A 129 ? 0.2833 0.2823 0.2712 -0.0152 -0.0015 0.0036  135 ALA   A CB  
995  N N   . ASP   A 130 ? 0.2848 0.2858 0.2601 -0.0177 -0.0028 0.0076  136 ASP   A N   
996  C CA  . ASP   A 130 ? 0.2987 0.2973 0.2662 -0.0207 -0.0010 0.0069  136 ASP   A CA  
997  C C   . ASP   A 130 ? 0.3147 0.3080 0.2793 -0.0233 0.0052  0.0062  136 ASP   A C   
998  O O   . ASP   A 130 ? 0.3289 0.3183 0.2933 -0.0235 0.0065  0.0081  136 ASP   A O   
999  C CB  . ASP   A 130 ? 0.3463 0.3410 0.3042 -0.0217 -0.0058 0.0099  136 ASP   A CB  
1000 C CG  . ASP   A 130 ? 0.4122 0.4017 0.3579 -0.0253 -0.0048 0.0086  136 ASP   A CG  
1001 O OD1 . ASP   A 130 ? 0.4088 0.4023 0.3580 -0.0256 -0.0035 0.0055  136 ASP   A OD1 
1002 O OD2 . ASP   A 130 ? 0.4752 0.4551 0.4062 -0.0279 -0.0049 0.0107  136 ASP   A OD2 
1003 N N   . VAL   A 131 ? 0.3005 0.2932 0.2646 -0.0253 0.0102  0.0034  137 VAL   A N   
1004 C CA  . VAL   A 131 ? 0.3138 0.3008 0.2774 -0.0280 0.0184  0.0025  137 VAL   A CA  
1005 C C   . VAL   A 131 ? 0.3408 0.3189 0.2888 -0.0315 0.0238  0.0017  137 VAL   A C   
1006 O O   . VAL   A 131 ? 0.3706 0.3420 0.3166 -0.0341 0.0332  0.0006  137 VAL   A O   
1007 C CB  . VAL   A 131 ? 0.3075 0.3003 0.2894 -0.0274 0.0219  -0.0005 137 VAL   A CB  
1008 C CG1 . VAL   A 131 ? 0.3058 0.3037 0.2984 -0.0250 0.0161  -0.0001 137 VAL   A CG1 
1009 C CG2 . VAL   A 131 ? 0.3089 0.3057 0.2955 -0.0269 0.0222  -0.0033 137 VAL   A CG2 
1010 N N   . ARG   A 132 ? 0.3349 0.3118 0.2722 -0.0318 0.0184  0.0017  138 ARG   A N   
1011 C CA  . ARG   A 132 ? 0.3497 0.3164 0.2694 -0.0355 0.0221  -0.0001 138 ARG   A CA  
1012 C C   . ARG   A 132 ? 0.3912 0.3428 0.2889 -0.0391 0.0251  0.0026  138 ARG   A C   
1013 O O   . ARG   A 132 ? 0.4153 0.3547 0.2959 -0.0429 0.0322  0.0003  138 ARG   A O   
1014 C CB  . ARG   A 132 ? 0.3354 0.3048 0.2509 -0.0354 0.0133  -0.0006 138 ARG   A CB  
1015 C CG  . ARG   A 132 ? 0.3311 0.3119 0.2644 -0.0328 0.0128  -0.0034 138 ARG   A CG  
1016 C CD  . ARG   A 132 ? 0.3357 0.3185 0.2662 -0.0331 0.0050  -0.0036 138 ARG   A CD  
1017 N NE  . ARG   A 132 ? 0.3453 0.3333 0.2806 -0.0308 -0.0039 0.0004  138 ARG   A NE  
1018 C CZ  . ARG   A 132 ? 0.3666 0.3584 0.3055 -0.0306 -0.0114 0.0011  138 ARG   A CZ  
1019 N NH1 . ARG   A 132 ? 0.3431 0.3333 0.2788 -0.0331 -0.0122 -0.0020 138 ARG   A NH1 
1020 N NH2 . ARG   A 132 ? 0.3459 0.3428 0.2935 -0.0281 -0.0177 0.0046  138 ARG   A NH2 
1021 N N   . ASP   A 133 ? 0.3890 0.3393 0.2849 -0.0379 0.0204  0.0074  139 ASP   A N   
1022 C CA  . ASP   A 133 ? 0.4153 0.3494 0.2889 -0.0412 0.0229  0.0110  139 ASP   A CA  
1023 C C   . ASP   A 133 ? 0.4317 0.3602 0.3087 -0.0430 0.0370  0.0103  139 ASP   A C   
1024 O O   . ASP   A 133 ? 0.4505 0.3630 0.3071 -0.0464 0.0425  0.0129  139 ASP   A O   
1025 C CB  . ASP   A 133 ? 0.4467 0.3800 0.3173 -0.0391 0.0114  0.0171  139 ASP   A CB  
1026 C CG  . ASP   A 133 ? 0.4790 0.4224 0.3712 -0.0354 0.0118  0.0184  139 ASP   A CG  
1027 O OD1 . ASP   A 133 ? 0.4704 0.4267 0.3824 -0.0329 0.0129  0.0148  139 ASP   A OD1 
1028 O OD2 . ASP   A 133 ? 0.4955 0.4322 0.3832 -0.0352 0.0109  0.0230  139 ASP   A OD2 
1029 N N   . LEU   A 134 ? 0.4111 0.3515 0.3138 -0.0411 0.0426  0.0069  140 LEU   A N   
1030 C CA  . LEU   A 134 ? 0.4191 0.3567 0.3323 -0.0428 0.0549  0.0062  140 LEU   A CA  
1031 C C   . LEU   A 134 ? 0.4474 0.3773 0.3571 -0.0461 0.0691  0.0018  140 LEU   A C   
1032 O O   . LEU   A 134 ? 0.4329 0.3717 0.3661 -0.0452 0.0750  -0.0021 140 LEU   A O   
1033 C CB  . LEU   A 134 ? 0.4027 0.3561 0.3460 -0.0393 0.0513  0.0048  140 LEU   A CB  
1034 C CG  . LEU   A 134 ? 0.4089 0.3674 0.3546 -0.0362 0.0398  0.0084  140 LEU   A CG  
1035 C CD1 . LEU   A 134 ? 0.4082 0.3788 0.3786 -0.0335 0.0364  0.0062  140 LEU   A CD1 
1036 C CD2 . LEU   A 134 ? 0.4264 0.3734 0.3599 -0.0379 0.0418  0.0132  140 LEU   A CD2 
1037 N N   . LEU   A 135 ? 0.4657 0.3775 0.3446 -0.0501 0.0740  0.0026  141 LEU   A N   
1038 C CA  . LEU   A 135 ? 0.4928 0.3934 0.3620 -0.0538 0.0883  -0.0022 141 LEU   A CA  
1039 C C   . LEU   A 135 ? 0.5076 0.4074 0.3965 -0.0553 0.1060  -0.0047 141 LEU   A C   
1040 O O   . LEU   A 135 ? 0.5133 0.4129 0.4126 -0.0561 0.1173  -0.0099 141 LEU   A O   
1041 C CB  . LEU   A 135 ? 0.5205 0.3978 0.3475 -0.0585 0.0898  -0.0007 141 LEU   A CB  
1042 C CG  . LEU   A 135 ? 0.5473 0.4236 0.3550 -0.0578 0.0708  0.0023  141 LEU   A CG  
1043 C CD1 . LEU   A 135 ? 0.5802 0.4310 0.3450 -0.0634 0.0721  0.0030  141 LEU   A CD1 
1044 C CD2 . LEU   A 135 ? 0.5321 0.4253 0.3578 -0.0545 0.0614  -0.0014 141 LEU   A CD2 
1045 N N   . TRP   A 136 ? 0.5049 0.4047 0.4024 -0.0555 0.1085  -0.0010 142 TRP   A N   
1046 C CA  . TRP   A 136 ? 0.5035 0.4031 0.4239 -0.0572 0.1247  -0.0027 142 TRP   A CA  
1047 C C   . TRP   A 136 ? 0.4945 0.4145 0.4569 -0.0538 0.1233  -0.0068 142 TRP   A C   
1048 O O   . TRP   A 136 ? 0.5050 0.4256 0.4904 -0.0553 0.1375  -0.0096 142 TRP   A O   
1049 C CB  . TRP   A 136 ? 0.4946 0.3897 0.4147 -0.0584 0.1253  0.0025  142 TRP   A CB  
1050 C CG  . TRP   A 136 ? 0.4725 0.3819 0.4041 -0.0541 0.1069  0.0057  142 TRP   A CG  
1051 C CD1 . TRP   A 136 ? 0.4823 0.3881 0.3926 -0.0527 0.0935  0.0105  142 TRP   A CD1 
1052 C CD2 . TRP   A 136 ? 0.4433 0.3703 0.4100 -0.0512 0.1010  0.0043  142 TRP   A CD2 
1053 N NE1 . TRP   A 136 ? 0.4719 0.3920 0.4022 -0.0489 0.0817  0.0116  142 TRP   A NE1 
1054 C CE2 . TRP   A 136 ? 0.4473 0.3797 0.4099 -0.0481 0.0855  0.0077  142 TRP   A CE2 
1055 C CE3 . TRP   A 136 ? 0.4345 0.3727 0.4364 -0.0510 0.1065  0.0004  142 TRP   A CE3 
1056 C CZ2 . TRP   A 136 ? 0.4379 0.3843 0.4254 -0.0452 0.0764  0.0068  142 TRP   A CZ2 
1057 C CZ3 . TRP   A 136 ? 0.4266 0.3793 0.4537 -0.0481 0.0949  0.0000  142 TRP   A CZ3 
1058 C CH2 . TRP   A 136 ? 0.4259 0.3815 0.4435 -0.0456 0.0806  0.0029  142 TRP   A CH2 
1059 N N   . LEU   A 137 ? 0.4789 0.4144 0.4517 -0.0494 0.1065  -0.0070 143 LEU   A N   
1060 C CA  . LEU   A 137 ? 0.4659 0.4181 0.4741 -0.0462 0.1032  -0.0102 143 LEU   A CA  
1061 C C   . LEU   A 137 ? 0.4908 0.4404 0.5082 -0.0471 0.1160  -0.0151 143 LEU   A C   
1062 O O   . LEU   A 137 ? 0.4687 0.4292 0.5199 -0.0452 0.1176  -0.0174 143 LEU   A O   
1063 C CB  . LEU   A 137 ? 0.4449 0.4096 0.4544 -0.0418 0.0845  -0.0093 143 LEU   A CB  
1064 C CG  . LEU   A 137 ? 0.4317 0.4023 0.4427 -0.0399 0.0719  -0.0058 143 LEU   A CG  
1065 C CD1 . LEU   A 137 ? 0.4341 0.4127 0.4394 -0.0362 0.0570  -0.0052 143 LEU   A CD1 
1066 C CD2 . LEU   A 137 ? 0.4112 0.3905 0.4532 -0.0393 0.0711  -0.0065 143 LEU   A CD2 
1067 N N   . ASP   A 138 ? 0.5290 0.4636 0.5164 -0.0498 0.1238  -0.0167 144 ASP   A N   
1068 C CA  . ASP   A 138 ? 0.5683 0.4972 0.5598 -0.0510 0.1374  -0.0221 144 ASP   A CA  
1069 C C   . ASP   A 138 ? 0.6153 0.5319 0.6130 -0.0549 0.1606  -0.0244 144 ASP   A C   
1070 O O   . ASP   A 138 ? 0.6295 0.5392 0.6308 -0.0561 0.1749  -0.0293 144 ASP   A O   
1071 C CB  . ASP   A 138 ? 0.5976 0.5134 0.5518 -0.0529 0.1356  -0.0237 144 ASP   A CB  
1072 C CG  . ASP   A 138 ? 0.6445 0.5707 0.5929 -0.0497 0.1156  -0.0222 144 ASP   A CG  
1073 O OD1 . ASP   A 138 ? 0.6370 0.5808 0.6115 -0.0454 0.1046  -0.0209 144 ASP   A OD1 
1074 O OD2 . ASP   A 138 ? 0.6787 0.5943 0.5960 -0.0518 0.1109  -0.0223 144 ASP   A OD2 
1075 N N   . GLU   A 139 ? 0.6412 0.5536 0.6402 -0.0572 0.1660  -0.0211 145 GLU   A N   
1076 C CA  . GLU   A 139 ? 0.6851 0.5844 0.6902 -0.0614 0.1903  -0.0231 145 GLU   A CA  
1077 C C   . GLU   A 139 ? 0.7022 0.6116 0.7435 -0.0614 0.1933  -0.0210 145 GLU   A C   
1078 O O   . GLU   A 139 ? 0.7042 0.6244 0.7514 -0.0593 0.1767  -0.0171 145 GLU   A O   
1079 C CB  . GLU   A 139 ? 0.7488 0.6209 0.7041 -0.0668 0.2013  -0.0217 145 GLU   A CB  
1080 C CG  . GLU   A 139 ? 0.8361 0.7040 0.7636 -0.0672 0.1863  -0.0150 145 GLU   A CG  
1081 C CD  . GLU   A 139 ? 0.9784 0.8255 0.8535 -0.0701 0.1822  -0.0136 145 GLU   A CD  
1082 O OE1 . GLU   A 139 ? 1.0234 0.8508 0.8671 -0.0741 0.1873  -0.0093 145 GLU   A OE1 
1083 O OE2 . GLU   A 139 ? 1.0168 0.8667 0.8824 -0.0687 0.1733  -0.0165 145 GLU   A OE2 
1084 N N   . GLU   A 140 ? 0.7139 0.6187 0.7803 -0.0640 0.2154  -0.0241 146 GLU   A N   
1085 C CA  . GLU   A 140 ? 0.7236 0.6360 0.8297 -0.0651 0.2230  -0.0232 146 GLU   A CA  
1086 C C   . GLU   A 140 ? 0.7261 0.6608 0.8624 -0.0613 0.1999  -0.0205 146 GLU   A C   
1087 O O   . GLU   A 140 ? 0.7245 0.6645 0.8887 -0.0628 0.2022  -0.0192 146 GLU   A O   
1088 C CB  . GLU   A 140 ? 0.7741 0.6660 0.8557 -0.0708 0.2396  -0.0202 146 GLU   A CB  
1089 C CG  . GLU   A 140 ? 0.8526 0.7413 0.9063 -0.0711 0.2240  -0.0138 146 GLU   A CG  
1090 C CD  . GLU   A 140 ? 0.9496 0.8309 1.0117 -0.0751 0.2352  -0.0104 146 GLU   A CD  
1091 O OE1 . GLU   A 140 ? 0.9820 0.8624 1.0284 -0.0748 0.2221  -0.0052 146 GLU   A OE1 
1092 O OE2 . GLU   A 140 ? 0.9605 0.8367 1.0468 -0.0785 0.2578  -0.0129 146 GLU   A OE2 
1093 N N1  . A1B3X B .   ? 0.4218 0.3493 0.3556 -0.0068 0.0160  -0.0198 201 A1B3X A N1  
1094 C C4  . A1B3X B .   ? 0.5899 0.4688 0.4610 -0.0049 0.0628  -0.0256 201 A1B3X A C4  
1095 C C5  . A1B3X B .   ? 0.5913 0.4581 0.4568 -0.0046 0.0679  -0.0302 201 A1B3X A C5  
1096 C C6  . A1B3X B .   ? 0.5827 0.4528 0.4523 -0.0053 0.0572  -0.0313 201 A1B3X A C6  
1097 C C7  . A1B3X B .   ? 0.5573 0.4428 0.4373 -0.0063 0.0425  -0.0277 201 A1B3X A C7  
1098 C C8  . A1B3X B .   ? 0.5270 0.4180 0.4142 -0.0077 0.0309  -0.0280 201 A1B3X A C8  
1099 C C10 . A1B3X B .   ? 0.4451 0.3713 0.3723 -0.0059 0.0211  -0.0194 201 A1B3X A C10 
1100 C C13 . A1B3X B .   ? 0.3984 0.3367 0.3502 -0.0109 0.0015  -0.0178 201 A1B3X A C13 
1101 C C15 . A1B3X B .   ? 0.3711 0.3276 0.3457 -0.0064 0.0072  -0.0093 201 A1B3X A C15 
1102 O O2  . A1B3X B .   ? 0.3615 0.3138 0.3414 -0.0049 0.0103  -0.0090 201 A1B3X A O2  
1103 N N2  . A1B3X B .   ? 0.3594 0.3262 0.3394 -0.0072 0.0039  -0.0059 201 A1B3X A N2  
1104 C C14 . A1B3X B .   ? 0.3890 0.3369 0.3485 -0.0077 0.0069  -0.0138 201 A1B3X A C14 
1105 C C12 . A1B3X B .   ? 0.4101 0.3362 0.3423 -0.0124 -0.0005 -0.0219 201 A1B3X A C12 
1106 C C11 . A1B3X B .   ? 0.4260 0.3421 0.3477 -0.0100 0.0097  -0.0239 201 A1B3X A C11 
1107 C C16 . A1B3X B .   ? 0.4005 0.3402 0.3544 -0.0051 0.0158  -0.0157 201 A1B3X A C16 
1108 O O1  . A1B3X B .   ? 0.4214 0.3578 0.3617 -0.0037 0.0254  -0.0161 201 A1B3X A O1  
1109 C C9  . A1B3X B .   ? 0.4958 0.4052 0.3970 -0.0081 0.0211  -0.0231 201 A1B3X A C9  
1110 N N   . A1B3X B .   ? 0.5233 0.4337 0.4192 -0.0075 0.0251  -0.0210 201 A1B3X A N   
1111 C C1  . A1B3X B .   ? 0.5288 0.4501 0.4299 -0.0083 0.0176  -0.0176 201 A1B3X A C1  
1112 O O   . A1B3X B .   ? 0.5415 0.4721 0.4523 -0.0093 0.0082  -0.0163 201 A1B3X A O   
1113 C C   . A1B3X B .   ? 0.5198 0.4416 0.4172 -0.0077 0.0227  -0.0154 201 A1B3X A C   
1114 C C2  . A1B3X B .   ? 0.5544 0.4517 0.4397 -0.0064 0.0383  -0.0235 201 A1B3X A C2  
1115 C C3  . A1B3X B .   ? 0.5734 0.4675 0.4542 -0.0057 0.0478  -0.0223 201 A1B3X A C3  
# 
