data_7I4Z
# 
_entry.id   7I4Z 
# 
_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   7I4Z         pdb_00007i4z 10.2210/pdb7i4z/pdb 
WWPDB D_1001408322 ?            ?                   
# 
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                        7I4Z 
_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 '(3R)-3-fluoro-1-{[2-(methylsulfanyl)phenyl]acetyl}piperidine-3-carboxamide' 310.387   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                   65.409    1   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                         78.133    1   ?         ? ? ? 
5 water       nat water                                                                        18.015    100 ?         ? ? ? 
# 
_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 '(3R)-3-fluoro-1-{[2-(methylsulfanyl)phenyl]acetyl}piperidine-3-carboxamide' A1B3G 
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 
A1B3G non-polymer         . '(3R)-3-fluoro-1-{[2-(methylsulfanyl)phenyl]acetyl}piperidine-3-carboxamide' ? 'C15 H19 F N2 O2 S' 
310.387 
ALA   'L-peptide linking' y ALANINE                                                                      ? 'C3 H7 N O2'        
89.093  
ARG   'L-peptide linking' y ARGININE                                                                     ? 'C6 H15 N4 O2 1'    
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                   ? 'C4 H8 N2 O3'       
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                              ? 'C4 H7 N O4'        
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                     ? 'C3 H7 N O2 S'      
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                         ? 'C2 H6 O S'         
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                    ? 'C5 H10 N2 O3'      
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                              ? 'C5 H9 N O4'        
147.129 
GLY   'peptide linking'   y GLYCINE                                                                      ? 'C2 H5 N O2'        
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                    ? 'C6 H10 N3 O2 1'    
156.162 
HOH   non-polymer         . WATER                                                                        ? 'H2 O'              
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                   ? 'C6 H13 N O2'       
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                      ? 'C6 H13 N O2'       
131.173 
LYS   'L-peptide linking' y LYSINE                                                                       ? 'C6 H15 N2 O2 1'    
147.195 
MET   'L-peptide linking' y METHIONINE                                                                   ? 'C5 H11 N O2 S'     
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                ? 'C9 H11 N O2'       
165.189 
PRO   'L-peptide linking' y PROLINE                                                                      ? 'C5 H9 N O2'        
115.130 
SER   'L-peptide linking' y SERINE                                                                       ? 'C3 H7 N O3'        
105.093 
THR   'L-peptide linking' y THREONINE                                                                    ? 'C4 H9 N O3'        
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                   ? 'C11 H12 N2 O2'     
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                     ? 'C9 H11 N O3'       
181.189 
VAL   'L-peptide linking' y VALINE                                                                       ? 'C5 H11 N O2'       
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                   ? 'Zn 2'              
65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B3G 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3G 
_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 A1B3G 1   201 201 A1B3G LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 6   DMS   DMS A . 
E 5 HOH   1   301 38  HOH   HOH A . 
E 5 HOH   2   302 99  HOH   HOH A . 
E 5 HOH   3   303 37  HOH   HOH A . 
E 5 HOH   4   304 59  HOH   HOH A . 
E 5 HOH   5   305 50  HOH   HOH A . 
E 5 HOH   6   306 78  HOH   HOH A . 
E 5 HOH   7   307 29  HOH   HOH A . 
E 5 HOH   8   308 22  HOH   HOH A . 
E 5 HOH   9   309 48  HOH   HOH A . 
E 5 HOH   10  310 36  HOH   HOH A . 
E 5 HOH   11  311 80  HOH   HOH A . 
E 5 HOH   12  312 18  HOH   HOH A . 
E 5 HOH   13  313 76  HOH   HOH A . 
E 5 HOH   14  314 27  HOH   HOH A . 
E 5 HOH   15  315 9   HOH   HOH A . 
E 5 HOH   16  316 40  HOH   HOH A . 
E 5 HOH   17  317 85  HOH   HOH A . 
E 5 HOH   18  318 8   HOH   HOH A . 
E 5 HOH   19  319 12  HOH   HOH A . 
E 5 HOH   20  320 14  HOH   HOH A . 
E 5 HOH   21  321 84  HOH   HOH A . 
E 5 HOH   22  322 16  HOH   HOH A . 
E 5 HOH   23  323 45  HOH   HOH A . 
E 5 HOH   24  324 25  HOH   HOH A . 
E 5 HOH   25  325 47  HOH   HOH A . 
E 5 HOH   26  326 13  HOH   HOH A . 
E 5 HOH   27  327 19  HOH   HOH A . 
E 5 HOH   28  328 34  HOH   HOH A . 
E 5 HOH   29  329 74  HOH   HOH A . 
E 5 HOH   30  330 91  HOH   HOH A . 
E 5 HOH   31  331 72  HOH   HOH A . 
E 5 HOH   32  332 86  HOH   HOH A . 
E 5 HOH   33  333 2   HOH   HOH A . 
E 5 HOH   34  334 23  HOH   HOH A . 
E 5 HOH   35  335 4   HOH   HOH A . 
E 5 HOH   36  336 90  HOH   HOH A . 
E 5 HOH   37  337 51  HOH   HOH A . 
E 5 HOH   38  338 7   HOH   HOH A . 
E 5 HOH   39  339 73  HOH   HOH A . 
E 5 HOH   40  340 55  HOH   HOH A . 
E 5 HOH   41  341 35  HOH   HOH A . 
E 5 HOH   42  342 21  HOH   HOH A . 
E 5 HOH   43  343 94  HOH   HOH A . 
E 5 HOH   44  344 17  HOH   HOH A . 
E 5 HOH   45  345 24  HOH   HOH A . 
E 5 HOH   46  346 71  HOH   HOH A . 
E 5 HOH   47  347 49  HOH   HOH A . 
E 5 HOH   48  348 53  HOH   HOH A . 
E 5 HOH   49  349 81  HOH   HOH A . 
E 5 HOH   50  350 33  HOH   HOH A . 
E 5 HOH   51  351 30  HOH   HOH A . 
E 5 HOH   52  352 88  HOH   HOH A . 
E 5 HOH   53  353 32  HOH   HOH A . 
E 5 HOH   54  354 42  HOH   HOH A . 
E 5 HOH   55  355 89  HOH   HOH A . 
E 5 HOH   56  356 11  HOH   HOH A . 
E 5 HOH   57  357 54  HOH   HOH A . 
E 5 HOH   58  358 10  HOH   HOH A . 
E 5 HOH   59  359 87  HOH   HOH A . 
E 5 HOH   60  360 39  HOH   HOH A . 
E 5 HOH   61  361 67  HOH   HOH A . 
E 5 HOH   62  362 5   HOH   HOH A . 
E 5 HOH   63  363 26  HOH   HOH A . 
E 5 HOH   64  364 75  HOH   HOH A . 
E 5 HOH   65  365 6   HOH   HOH A . 
E 5 HOH   66  366 41  HOH   HOH A . 
E 5 HOH   67  367 20  HOH   HOH A . 
E 5 HOH   68  368 79  HOH   HOH A . 
E 5 HOH   69  369 3   HOH   HOH A . 
E 5 HOH   70  370 58  HOH   HOH A . 
E 5 HOH   71  371 56  HOH   HOH A . 
E 5 HOH   72  372 43  HOH   HOH A . 
E 5 HOH   73  373 46  HOH   HOH A . 
E 5 HOH   74  374 66  HOH   HOH A . 
E 5 HOH   75  375 15  HOH   HOH A . 
E 5 HOH   76  376 65  HOH   HOH A . 
E 5 HOH   77  377 57  HOH   HOH A . 
E 5 HOH   78  378 102 HOH   HOH A . 
E 5 HOH   79  379 70  HOH   HOH A . 
E 5 HOH   80  380 82  HOH   HOH A . 
E 5 HOH   81  381 60  HOH   HOH A . 
E 5 HOH   82  382 92  HOH   HOH A . 
E 5 HOH   83  383 61  HOH   HOH A . 
E 5 HOH   84  384 63  HOH   HOH A . 
E 5 HOH   85  385 93  HOH   HOH A . 
E 5 HOH   86  386 31  HOH   HOH A . 
E 5 HOH   87  387 64  HOH   HOH A . 
E 5 HOH   88  388 100 HOH   HOH A . 
E 5 HOH   89  389 95  HOH   HOH A . 
E 5 HOH   90  390 68  HOH   HOH A . 
E 5 HOH   91  391 28  HOH   HOH A . 
E 5 HOH   92  392 83  HOH   HOH A . 
E 5 HOH   93  393 97  HOH   HOH A . 
E 5 HOH   94  394 52  HOH   HOH A . 
E 5 HOH   95  395 98  HOH   HOH A . 
E 5 HOH   96  396 44  HOH   HOH A . 
E 5 HOH   97  397 101 HOH   HOH A . 
E 5 HOH   98  398 69  HOH   HOH A . 
E 5 HOH   99  399 62  HOH   HOH A . 
E 5 HOH   100 400 96  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           7I4Z 
_cell.length_a           72.578 
_cell.length_b           61.633 
_cell.length_c           32.702 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.97 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I4Z 
_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          7I4Z 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.30 
_exptl_crystal.density_percent_sol   46.48 
_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   2025-01-16 
_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   0.92201 
_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        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I4Z 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             36.24 
_reflns.d_resolution_high            1.60 
_reflns.number_obs                   18924 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.151 
_reflns.pdbx_netI_over_sigmaI        6.1 
_reflns.pdbx_redundancy              5.2 
_reflns.pdbx_Rrim_I_all              0.168 
_reflns.pdbx_Rpim_I_all              0.073 
_reflns.pdbx_CC_half                 0.995 
_reflns.pdbx_number_measured_all     98004 
_reflns.pdbx_chi_squared             0.76 
_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                  1.60 
_reflns_shell.d_res_low                   1.69 
_reflns_shell.number_measured_all         12757 
_reflns_shell.number_unique_obs           2746 
_reflns_shell.Rmerge_I_obs                1.573 
_reflns_shell.pdbx_chi_squared            0.62 
_reflns_shell.pdbx_redundancy             4.6 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.776 
_reflns_shell.pdbx_Rpim_I_all             0.809 
_reflns_shell.pdbx_CC_half                0.425 
_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                                 7I4Z 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     18806 
_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                             32.66 
_refine.ls_d_res_high                            1.603 
_refine.ls_percent_reflns_obs                    99.2 
_refine.ls_R_factor_obs                          0.2295 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2284 
_refine.ls_R_factor_R_free                       0.2503 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.870 
_refine.ls_number_reflns_R_free                  915 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.948 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.B_iso_mean                               31.95 
_refine.aniso_B[1][1]                            -1.14990 
_refine.aniso_B[2][2]                            -1.67250 
_refine.aniso_B[3][3]                            2.82240 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            0.05410 
_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             0.107 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.101 
_refine.pdbx_overall_SU_R_Blow_DPI               0.110 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.103 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I4Z 
_refine_analyze.Luzzati_coordinate_error_obs    0.26 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             100 
_refine_hist.number_atoms_total               1200 
_refine_hist.d_res_high                       1.603 
_refine_hist.d_res_low                        32.66 
# 
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  1129 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  1537 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  377  '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  203  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1129 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.21  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.54 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  955  'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   46 
_refine_ls_shell.d_res_high                       1.60 
_refine_ls_shell.d_res_low                        1.62 
_refine_ls_shell.number_reflns_R_work             403 
_refine_ls_shell.R_factor_R_work                  0.3480 
_refine_ls_shell.percent_reflns_obs               83.66 
_refine_ls_shell.R_factor_R_free                  0.4247 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            3.59 
_refine_ls_shell.number_reflns_R_free             15 
_refine_ls_shell.number_reflns_all                418 
_refine_ls_shell.R_factor_all                     0.3508 
# 
_struct.entry_id                  7I4Z 
_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-0036747-001 (A71EV2A-x4753)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I4Z 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              7I4Z 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 144 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             Q65900 
_struct_ref_seq.db_align_beg                  869 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  1012 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       7 
_struct_ref_seq.pdbx_auth_seq_align_end       150 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.328 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.374 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 1.965 ? ? 
# 
_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_555 116.0 ? 
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_555 106.1 ? 
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_555 115.1 ? 
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_555 110.3 ? 
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_555 102.2 ? 
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_555 106.8 ? 
# 
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 121 ? GLY A 119 GLY A 127 
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 SER A 37  ? N SER A 43  O ARG A 10  ? O ARG A 16  
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 ILE A 117 ? N ILE A 123 O ALA A 129 ? O ALA A 135 
AA2 5 6 O ASP A 130 ? O ASP A 136 N HIS A 91  ? N HIS A 97  
AA2 6 7 O GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7I4Z 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A TYR 89  ? ? N A TYR 90  ? ? 1.63 
2 1 O   A ALA 92  ? ? N A ARG 93  ? ? 1.79 
3 1 OE2 A GLU 88  ? ? O A HOH 301 ? ? 2.12 
4 1 O   A HOH 377 ? ? O A HOH 390 ? ? 2.17 
# 
loop_
_pdbx_validate_rmsd_bond.id 
_pdbx_validate_rmsd_bond.PDB_model_num 
_pdbx_validate_rmsd_bond.auth_atom_id_1 
_pdbx_validate_rmsd_bond.auth_asym_id_1 
_pdbx_validate_rmsd_bond.auth_comp_id_1 
_pdbx_validate_rmsd_bond.auth_seq_id_1 
_pdbx_validate_rmsd_bond.PDB_ins_code_1 
_pdbx_validate_rmsd_bond.label_alt_id_1 
_pdbx_validate_rmsd_bond.auth_atom_id_2 
_pdbx_validate_rmsd_bond.auth_asym_id_2 
_pdbx_validate_rmsd_bond.auth_comp_id_2 
_pdbx_validate_rmsd_bond.auth_seq_id_2 
_pdbx_validate_rmsd_bond.PDB_ins_code_2 
_pdbx_validate_rmsd_bond.label_alt_id_2 
_pdbx_validate_rmsd_bond.bond_value 
_pdbx_validate_rmsd_bond.bond_target_value 
_pdbx_validate_rmsd_bond.bond_deviation 
_pdbx_validate_rmsd_bond.bond_standard_deviation 
_pdbx_validate_rmsd_bond.linker_flag 
1  1 CA A VAL 84 ? ? CB  A VAL 84 ? ? 1.707 1.543 0.164  0.021 N 
2  1 C  A VAL 84 ? ? O   A VAL 84 ? ? 1.011 1.229 -0.218 0.019 N 
3  1 N  A GLU 85 ? ? CA  A GLU 85 ? ? 1.301 1.459 -0.158 0.020 N 
4  1 C  A GLU 85 ? ? O   A GLU 85 ? ? 1.054 1.229 -0.175 0.019 N 
5  1 C  A ALA 86 ? ? O   A ALA 86 ? ? 0.804 1.229 -0.425 0.019 N 
6  1 CA A SER 87 ? ? C   A SER 87 ? ? 1.702 1.525 0.177  0.026 N 
7  1 C  A SER 87 ? ? O   A SER 87 ? ? 0.957 1.229 -0.272 0.019 N 
8  1 C  A SER 87 ? ? N   A GLU 88 ? ? 1.112 1.336 -0.224 0.023 Y 
9  1 N  A GLU 88 ? ? CA  A GLU 88 ? ? 1.662 1.459 0.203  0.020 N 
10 1 CA A GLU 88 ? ? CB  A GLU 88 ? ? 1.292 1.535 -0.243 0.022 N 
11 1 CD A GLU 88 ? ? OE1 A GLU 88 ? ? 1.164 1.252 -0.088 0.011 N 
12 1 C  A GLU 88 ? ? O   A GLU 88 ? ? 0.801 1.229 -0.428 0.019 N 
13 1 C  A GLU 88 ? ? N   A TYR 89 ? ? 1.493 1.336 0.157  0.023 Y 
14 1 CG A TYR 89 ? ? CD1 A TYR 89 ? ? 1.298 1.387 -0.089 0.013 N 
15 1 C  A TYR 89 ? ? O   A TYR 89 ? ? 0.770 1.229 -0.459 0.019 N 
16 1 C  A TYR 89 ? ? N   A TYR 90 ? ? 1.167 1.336 -0.169 0.023 Y 
17 1 N  A TYR 90 ? ? CA  A TYR 90 ? ? 1.629 1.459 0.170  0.020 N 
18 1 C  A TYR 90 ? ? O   A TYR 90 ? ? 1.399 1.229 0.170  0.019 N 
19 1 CA A PRO 91 ? ? CB  A PRO 91 ? ? 1.691 1.531 0.160  0.020 N 
20 1 CD A PRO 91 ? ? N   A PRO 91 ? ? 1.572 1.474 0.098  0.014 N 
21 1 C  A PRO 91 ? ? O   A PRO 91 ? ? 1.361 1.228 0.133  0.020 N 
22 1 CA A ALA 92 ? ? CB  A ALA 92 ? ? 1.341 1.520 -0.179 0.021 N 
23 1 C  A ALA 92 ? ? N   A ARG 93 ? ? 1.152 1.336 -0.184 0.023 Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1  1 CA  A VAL 84 ? ? CB  A VAL 84 ? ? CG1 A VAL 84 ? ? 127.60 110.90 16.70  1.50 N 
2  1 CA  A VAL 84 ? ? C   A VAL 84 ? ? N   A GLU 85 ? ? 135.74 117.20 18.54  2.20 Y 
3  1 O   A VAL 84 ? ? C   A VAL 84 ? ? N   A GLU 85 ? ? 107.08 122.70 -15.62 1.60 Y 
4  1 N   A GLU 85 ? ? CA  A GLU 85 ? ? CB  A GLU 85 ? ? 86.98  110.60 -23.62 1.80 N 
5  1 N   A ALA 86 ? ? CA  A ALA 86 ? ? C   A ALA 86 ? ? 127.70 111.00 16.70  2.70 N 
6  1 CB  A SER 87 ? ? CA  A SER 87 ? ? C   A SER 87 ? ? 97.82  110.10 -12.28 1.90 N 
7  1 CA  A SER 87 ? ? CB  A SER 87 ? ? OG  A SER 87 ? ? 127.52 111.20 16.32  2.70 N 
8  1 CB  A GLU 88 ? ? CA  A GLU 88 ? ? C   A GLU 88 ? ? 139.56 110.40 29.16  2.00 N 
9  1 N   A GLU 88 ? ? CA  A GLU 88 ? ? C   A GLU 88 ? ? 92.40  111.00 -18.60 2.70 N 
10 1 CA  A GLU 88 ? ? C   A GLU 88 ? ? N   A TYR 89 ? ? 132.01 117.20 14.81  2.20 Y 
11 1 O   A GLU 88 ? ? C   A GLU 88 ? ? N   A TYR 89 ? ? 112.61 122.70 -10.09 1.60 Y 
12 1 C   A GLU 88 ? ? N   A TYR 89 ? ? CA  A TYR 89 ? ? 146.04 121.70 24.34  2.50 Y 
13 1 CB  A TYR 89 ? ? CA  A TYR 89 ? ? C   A TYR 89 ? ? 122.66 110.40 12.26  2.00 N 
14 1 CB  A TYR 89 ? ? CG  A TYR 89 ? ? CD1 A TYR 89 ? ? 114.61 121.00 -6.39  0.60 N 
15 1 O   A TYR 89 ? ? C   A TYR 89 ? ? N   A TYR 90 ? ? 113.07 122.70 -9.63  1.60 Y 
16 1 CB  A TYR 90 ? ? CA  A TYR 90 ? ? C   A TYR 90 ? ? 91.20  110.40 -19.20 2.00 N 
17 1 CG  A TYR 90 ? ? CD2 A TYR 90 ? ? CE2 A TYR 90 ? ? 115.13 121.30 -6.17  0.80 N 
18 1 CE1 A TYR 90 ? ? CZ  A TYR 90 ? ? CE2 A TYR 90 ? ? 109.86 119.80 -9.94  1.60 N 
19 1 CZ  A TYR 90 ? ? CE2 A TYR 90 ? ? CD2 A TYR 90 ? ? 131.82 119.80 12.02  0.90 N 
20 1 N   A TYR 90 ? ? CA  A TYR 90 ? ? C   A TYR 90 ? ? 129.19 111.00 18.19  2.70 N 
21 1 C   A TYR 90 ? ? N   A PRO 91 ? ? CD  A PRO 91 ? ? 94.71  128.40 -33.69 2.10 Y 
22 1 CA  A PRO 91 ? ? N   A PRO 91 ? ? CD  A PRO 91 ? ? 135.42 111.70 23.72  1.40 N 
23 1 N   A PRO 91 ? ? CA  A PRO 91 ? ? CB  A PRO 91 ? ? 76.30  103.30 -27.00 1.20 N 
24 1 N   A PRO 91 ? ? CD  A PRO 91 ? ? CG  A PRO 91 ? ? 84.53  103.20 -18.67 1.50 N 
25 1 CA  A PRO 91 ? ? C   A PRO 91 ? ? N   A ALA 92 ? ? 130.89 117.20 13.69  2.20 Y 
26 1 O   A PRO 91 ? ? C   A PRO 91 ? ? N   A ALA 92 ? ? 106.94 122.70 -15.76 1.60 Y 
27 1 CB  A ALA 92 ? ? CA  A ALA 92 ? ? C   A ALA 92 ? ? 121.09 110.10 10.99  1.50 N 
28 1 O   A ALA 92 ? ? C   A ALA 92 ? ? N   A ARG 93 ? ? 102.79 122.70 -19.91 1.60 Y 
29 1 NE  A ARG 93 ? ? CZ  A ARG 93 ? ? NH1 A ARG 93 ? ? 125.23 120.30 4.93   0.50 N 
30 1 NE  A ARG 93 ? ? CZ  A ARG 93 ? ? NH2 A ARG 93 ? ? 109.69 120.30 -10.61 0.50 N 
31 1 N   A ARG 93 ? ? CA  A ARG 93 ? ? C   A ARG 93 ? ? 127.42 111.00 16.42  2.70 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -90.54 30.35   
2 1 ALA A 86  ? ? -55.08 -174.10 
3 1 SER A 87  ? ? 171.76 163.71  
4 1 PRO A 91  ? ? -41.15 155.83  
5 1 ALA A 92  ? ? -27.45 138.35  
6 1 THR A 126 ? ? 77.99  161.39  
# 
loop_
_pdbx_validate_main_chain_plane.id 
_pdbx_validate_main_chain_plane.PDB_model_num 
_pdbx_validate_main_chain_plane.auth_comp_id 
_pdbx_validate_main_chain_plane.auth_asym_id 
_pdbx_validate_main_chain_plane.auth_seq_id 
_pdbx_validate_main_chain_plane.PDB_ins_code 
_pdbx_validate_main_chain_plane.label_alt_id 
_pdbx_validate_main_chain_plane.improper_torsion_angle 
1 1 VAL A 84 ? ? -14.08 
2 1 ALA A 86 ? ? -10.98 
3 1 GLU A 88 ? ? 15.36  
4 1 TYR A 90 ? ? 26.63  
5 1 ALA A 92 ? ? -22.93 
# 
loop_
_pdbx_validate_polymer_linkage.id 
_pdbx_validate_polymer_linkage.PDB_model_num 
_pdbx_validate_polymer_linkage.auth_atom_id_1 
_pdbx_validate_polymer_linkage.auth_asym_id_1 
_pdbx_validate_polymer_linkage.auth_comp_id_1 
_pdbx_validate_polymer_linkage.auth_seq_id_1 
_pdbx_validate_polymer_linkage.PDB_ins_code_1 
_pdbx_validate_polymer_linkage.label_alt_id_1 
_pdbx_validate_polymer_linkage.auth_atom_id_2 
_pdbx_validate_polymer_linkage.auth_asym_id_2 
_pdbx_validate_polymer_linkage.auth_comp_id_2 
_pdbx_validate_polymer_linkage.auth_seq_id_2 
_pdbx_validate_polymer_linkage.PDB_ins_code_2 
_pdbx_validate_polymer_linkage.label_alt_id_2 
_pdbx_validate_polymer_linkage.dist 
1 1 C A SER 87 ? ? N A GLU 88 ? ? 1.11 
2 1 C A TYR 89 ? ? N A TYR 90 ? ? 1.17 
3 1 C A ALA 92 ? ? N A ARG 93 ? ? 1.15 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     400 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_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         15.0979 
_pdbx_refine_tls.origin_y         6.6236 
_pdbx_refine_tls.origin_z         14.2568 
_pdbx_refine_tls.T[1][1]          0.0106 
_pdbx_refine_tls.T[2][2]          -0.0468 
_pdbx_refine_tls.T[3][3]          0.0157 
_pdbx_refine_tls.T[1][2]          0.0151 
_pdbx_refine_tls.T[1][3]          -0.0038 
_pdbx_refine_tls.T[2][3]          -0.0180 
_pdbx_refine_tls.L[1][1]          0.7447 
_pdbx_refine_tls.L[2][2]          11.7384 
_pdbx_refine_tls.L[3][3]          0.6855 
_pdbx_refine_tls.L[1][2]          2.8192 
_pdbx_refine_tls.L[1][3]          -0.8550 
_pdbx_refine_tls.L[2][3]          -3.3028 
_pdbx_refine_tls.S[1][1]          -0.1011 
_pdbx_refine_tls.S[1][2]          0.0895 
_pdbx_refine_tls.S[1][3]          -0.0675 
_pdbx_refine_tls.S[2][1]          0.5168 
_pdbx_refine_tls.S[2][2]          0.1532 
_pdbx_refine_tls.S[2][3]          -0.4915 
_pdbx_refine_tls.S[3][1]          -0.1058 
_pdbx_refine_tls.S[3][2]          -0.1746 
_pdbx_refine_tls.S[3][3]          -0.0521 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   '{ A|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A GLU 146 ? A GLU 140 
2 1 Y 1 A ALA 147 ? A ALA 141 
3 1 Y 1 A MET 148 ? A MET 142 
4 1 Y 1 A GLU 149 ? A GLU 143 
5 1 Y 1 A GLN 150 ? A GLN 144 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1B3G N1   N  N N 1   
A1B3G C4   C  Y N 2   
A1B3G C5   C  Y N 3   
A1B3G C6   C  Y N 4   
A1B3G C7   C  N N 5   
A1B3G C8   C  N N 6   
A1B3G C10  C  N N 7   
A1B3G C13  C  N N 8   
A1B3G O1   O  N N 9   
A1B3G C12  C  N R 10  
A1B3G F    F  N N 11  
A1B3G C11  C  N N 12  
A1B3G C9   C  N N 13  
A1B3G C14  C  N N 14  
A1B3G N    N  N N 15  
A1B3G O    O  N N 16  
A1B3G C1   C  Y N 17  
A1B3G S    S  N N 18  
A1B3G C    C  N N 19  
A1B3G C3   C  Y N 20  
A1B3G C2   C  Y N 21  
A1B3G H16  H  N N 22  
A1B3G H15  H  N N 23  
A1B3G H5   H  N N 24  
A1B3G H6   H  N N 25  
A1B3G H7   H  N N 26  
A1B3G H8   H  N N 27  
A1B3G H11  H  N N 28  
A1B3G H12  H  N N 29  
A1B3G H13  H  N N 30  
A1B3G H14  H  N N 31  
A1B3G H10  H  N N 32  
A1B3G H9   H  N N 33  
A1B3G H17  H  N N 34  
A1B3G H18  H  N N 35  
A1B3G H1   H  N N 36  
A1B3G H    H  N N 37  
A1B3G H2   H  N N 38  
A1B3G H4   H  N N 39  
A1B3G H3   H  N N 40  
ALA   N    N  N N 41  
ALA   CA   C  N S 42  
ALA   C    C  N N 43  
ALA   O    O  N N 44  
ALA   CB   C  N N 45  
ALA   OXT  O  N N 46  
ALA   H    H  N N 47  
ALA   H2   H  N N 48  
ALA   HA   H  N N 49  
ALA   HB1  H  N N 50  
ALA   HB2  H  N N 51  
ALA   HB3  H  N N 52  
ALA   HXT  H  N N 53  
ARG   N    N  N N 54  
ARG   CA   C  N S 55  
ARG   C    C  N N 56  
ARG   O    O  N N 57  
ARG   CB   C  N N 58  
ARG   CG   C  N N 59  
ARG   CD   C  N N 60  
ARG   NE   N  N N 61  
ARG   CZ   C  N N 62  
ARG   NH1  N  N N 63  
ARG   NH2  N  N N 64  
ARG   OXT  O  N N 65  
ARG   H    H  N N 66  
ARG   H2   H  N N 67  
ARG   HA   H  N N 68  
ARG   HB2  H  N N 69  
ARG   HB3  H  N N 70  
ARG   HG2  H  N N 71  
ARG   HG3  H  N N 72  
ARG   HD2  H  N N 73  
ARG   HD3  H  N N 74  
ARG   HE   H  N N 75  
ARG   HH11 H  N N 76  
ARG   HH12 H  N N 77  
ARG   HH21 H  N N 78  
ARG   HH22 H  N N 79  
ARG   HXT  H  N N 80  
ASN   N    N  N N 81  
ASN   CA   C  N S 82  
ASN   C    C  N N 83  
ASN   O    O  N N 84  
ASN   CB   C  N N 85  
ASN   CG   C  N N 86  
ASN   OD1  O  N N 87  
ASN   ND2  N  N N 88  
ASN   OXT  O  N N 89  
ASN   H    H  N N 90  
ASN   H2   H  N N 91  
ASN   HA   H  N N 92  
ASN   HB2  H  N N 93  
ASN   HB3  H  N N 94  
ASN   HD21 H  N N 95  
ASN   HD22 H  N N 96  
ASN   HXT  H  N N 97  
ASP   N    N  N N 98  
ASP   CA   C  N S 99  
ASP   C    C  N N 100 
ASP   O    O  N N 101 
ASP   CB   C  N N 102 
ASP   CG   C  N N 103 
ASP   OD1  O  N N 104 
ASP   OD2  O  N N 105 
ASP   OXT  O  N N 106 
ASP   H    H  N N 107 
ASP   H2   H  N N 108 
ASP   HA   H  N N 109 
ASP   HB2  H  N N 110 
ASP   HB3  H  N N 111 
ASP   HD2  H  N N 112 
ASP   HXT  H  N N 113 
CYS   N    N  N N 114 
CYS   CA   C  N R 115 
CYS   C    C  N N 116 
CYS   O    O  N N 117 
CYS   CB   C  N N 118 
CYS   SG   S  N N 119 
CYS   OXT  O  N N 120 
CYS   H    H  N N 121 
CYS   H2   H  N N 122 
CYS   HA   H  N N 123 
CYS   HB2  H  N N 124 
CYS   HB3  H  N N 125 
CYS   HG   H  N N 126 
CYS   HXT  H  N N 127 
DMS   S    S  N N 128 
DMS   O    O  N N 129 
DMS   C1   C  N N 130 
DMS   C2   C  N N 131 
DMS   H11  H  N N 132 
DMS   H12  H  N N 133 
DMS   H13  H  N N 134 
DMS   H21  H  N N 135 
DMS   H22  H  N N 136 
DMS   H23  H  N N 137 
GLN   N    N  N N 138 
GLN   CA   C  N S 139 
GLN   C    C  N N 140 
GLN   O    O  N N 141 
GLN   CB   C  N N 142 
GLN   CG   C  N N 143 
GLN   CD   C  N N 144 
GLN   OE1  O  N N 145 
GLN   NE2  N  N N 146 
GLN   OXT  O  N N 147 
GLN   H    H  N N 148 
GLN   H2   H  N N 149 
GLN   HA   H  N N 150 
GLN   HB2  H  N N 151 
GLN   HB3  H  N N 152 
GLN   HG2  H  N N 153 
GLN   HG3  H  N N 154 
GLN   HE21 H  N N 155 
GLN   HE22 H  N N 156 
GLN   HXT  H  N N 157 
GLU   N    N  N N 158 
GLU   CA   C  N S 159 
GLU   C    C  N N 160 
GLU   O    O  N N 161 
GLU   CB   C  N N 162 
GLU   CG   C  N N 163 
GLU   CD   C  N N 164 
GLU   OE1  O  N N 165 
GLU   OE2  O  N N 166 
GLU   OXT  O  N N 167 
GLU   H    H  N N 168 
GLU   H2   H  N N 169 
GLU   HA   H  N N 170 
GLU   HB2  H  N N 171 
GLU   HB3  H  N N 172 
GLU   HG2  H  N N 173 
GLU   HG3  H  N N 174 
GLU   HE2  H  N N 175 
GLU   HXT  H  N N 176 
GLY   N    N  N N 177 
GLY   CA   C  N N 178 
GLY   C    C  N N 179 
GLY   O    O  N N 180 
GLY   OXT  O  N N 181 
GLY   H    H  N N 182 
GLY   H2   H  N N 183 
GLY   HA2  H  N N 184 
GLY   HA3  H  N N 185 
GLY   HXT  H  N N 186 
HIS   N    N  N N 187 
HIS   CA   C  N S 188 
HIS   C    C  N N 189 
HIS   O    O  N N 190 
HIS   CB   C  N N 191 
HIS   CG   C  Y N 192 
HIS   ND1  N  Y N 193 
HIS   CD2  C  Y N 194 
HIS   CE1  C  Y N 195 
HIS   NE2  N  Y N 196 
HIS   OXT  O  N N 197 
HIS   H    H  N N 198 
HIS   H2   H  N N 199 
HIS   HA   H  N N 200 
HIS   HB2  H  N N 201 
HIS   HB3  H  N N 202 
HIS   HD1  H  N N 203 
HIS   HD2  H  N N 204 
HIS   HE1  H  N N 205 
HIS   HE2  H  N N 206 
HIS   HXT  H  N N 207 
HOH   O    O  N N 208 
HOH   H1   H  N N 209 
HOH   H2   H  N N 210 
ILE   N    N  N N 211 
ILE   CA   C  N S 212 
ILE   C    C  N N 213 
ILE   O    O  N N 214 
ILE   CB   C  N S 215 
ILE   CG1  C  N N 216 
ILE   CG2  C  N N 217 
ILE   CD1  C  N N 218 
ILE   OXT  O  N N 219 
ILE   H    H  N N 220 
ILE   H2   H  N N 221 
ILE   HA   H  N N 222 
ILE   HB   H  N N 223 
ILE   HG12 H  N N 224 
ILE   HG13 H  N N 225 
ILE   HG21 H  N N 226 
ILE   HG22 H  N N 227 
ILE   HG23 H  N N 228 
ILE   HD11 H  N N 229 
ILE   HD12 H  N N 230 
ILE   HD13 H  N N 231 
ILE   HXT  H  N N 232 
LEU   N    N  N N 233 
LEU   CA   C  N S 234 
LEU   C    C  N N 235 
LEU   O    O  N N 236 
LEU   CB   C  N N 237 
LEU   CG   C  N N 238 
LEU   CD1  C  N N 239 
LEU   CD2  C  N N 240 
LEU   OXT  O  N N 241 
LEU   H    H  N N 242 
LEU   H2   H  N N 243 
LEU   HA   H  N N 244 
LEU   HB2  H  N N 245 
LEU   HB3  H  N N 246 
LEU   HG   H  N N 247 
LEU   HD11 H  N N 248 
LEU   HD12 H  N N 249 
LEU   HD13 H  N N 250 
LEU   HD21 H  N N 251 
LEU   HD22 H  N N 252 
LEU   HD23 H  N N 253 
LEU   HXT  H  N N 254 
LYS   N    N  N N 255 
LYS   CA   C  N S 256 
LYS   C    C  N N 257 
LYS   O    O  N N 258 
LYS   CB   C  N N 259 
LYS   CG   C  N N 260 
LYS   CD   C  N N 261 
LYS   CE   C  N N 262 
LYS   NZ   N  N N 263 
LYS   OXT  O  N N 264 
LYS   H    H  N N 265 
LYS   H2   H  N N 266 
LYS   HA   H  N N 267 
LYS   HB2  H  N N 268 
LYS   HB3  H  N N 269 
LYS   HG2  H  N N 270 
LYS   HG3  H  N N 271 
LYS   HD2  H  N N 272 
LYS   HD3  H  N N 273 
LYS   HE2  H  N N 274 
LYS   HE3  H  N N 275 
LYS   HZ1  H  N N 276 
LYS   HZ2  H  N N 277 
LYS   HZ3  H  N N 278 
LYS   HXT  H  N N 279 
MET   N    N  N N 280 
MET   CA   C  N S 281 
MET   C    C  N N 282 
MET   O    O  N N 283 
MET   CB   C  N N 284 
MET   CG   C  N N 285 
MET   SD   S  N N 286 
MET   CE   C  N N 287 
MET   OXT  O  N N 288 
MET   H    H  N N 289 
MET   H2   H  N N 290 
MET   HA   H  N N 291 
MET   HB2  H  N N 292 
MET   HB3  H  N N 293 
MET   HG2  H  N N 294 
MET   HG3  H  N N 295 
MET   HE1  H  N N 296 
MET   HE2  H  N N 297 
MET   HE3  H  N N 298 
MET   HXT  H  N N 299 
PHE   N    N  N N 300 
PHE   CA   C  N S 301 
PHE   C    C  N N 302 
PHE   O    O  N N 303 
PHE   CB   C  N N 304 
PHE   CG   C  Y N 305 
PHE   CD1  C  Y N 306 
PHE   CD2  C  Y N 307 
PHE   CE1  C  Y N 308 
PHE   CE2  C  Y N 309 
PHE   CZ   C  Y N 310 
PHE   OXT  O  N N 311 
PHE   H    H  N N 312 
PHE   H2   H  N N 313 
PHE   HA   H  N N 314 
PHE   HB2  H  N N 315 
PHE   HB3  H  N N 316 
PHE   HD1  H  N N 317 
PHE   HD2  H  N N 318 
PHE   HE1  H  N N 319 
PHE   HE2  H  N N 320 
PHE   HZ   H  N N 321 
PHE   HXT  H  N N 322 
PRO   N    N  N N 323 
PRO   CA   C  N S 324 
PRO   C    C  N N 325 
PRO   O    O  N N 326 
PRO   CB   C  N N 327 
PRO   CG   C  N N 328 
PRO   CD   C  N N 329 
PRO   OXT  O  N N 330 
PRO   H    H  N N 331 
PRO   HA   H  N N 332 
PRO   HB2  H  N N 333 
PRO   HB3  H  N N 334 
PRO   HG2  H  N N 335 
PRO   HG3  H  N N 336 
PRO   HD2  H  N N 337 
PRO   HD3  H  N N 338 
PRO   HXT  H  N N 339 
SER   N    N  N N 340 
SER   CA   C  N S 341 
SER   C    C  N N 342 
SER   O    O  N N 343 
SER   CB   C  N N 344 
SER   OG   O  N N 345 
SER   OXT  O  N N 346 
SER   H    H  N N 347 
SER   H2   H  N N 348 
SER   HA   H  N N 349 
SER   HB2  H  N N 350 
SER   HB3  H  N N 351 
SER   HG   H  N N 352 
SER   HXT  H  N N 353 
THR   N    N  N N 354 
THR   CA   C  N S 355 
THR   C    C  N N 356 
THR   O    O  N N 357 
THR   CB   C  N R 358 
THR   OG1  O  N N 359 
THR   CG2  C  N N 360 
THR   OXT  O  N N 361 
THR   H    H  N N 362 
THR   H2   H  N N 363 
THR   HA   H  N N 364 
THR   HB   H  N N 365 
THR   HG1  H  N N 366 
THR   HG21 H  N N 367 
THR   HG22 H  N N 368 
THR   HG23 H  N N 369 
THR   HXT  H  N N 370 
TRP   N    N  N N 371 
TRP   CA   C  N S 372 
TRP   C    C  N N 373 
TRP   O    O  N N 374 
TRP   CB   C  N N 375 
TRP   CG   C  Y N 376 
TRP   CD1  C  Y N 377 
TRP   CD2  C  Y N 378 
TRP   NE1  N  Y N 379 
TRP   CE2  C  Y N 380 
TRP   CE3  C  Y N 381 
TRP   CZ2  C  Y N 382 
TRP   CZ3  C  Y N 383 
TRP   CH2  C  Y N 384 
TRP   OXT  O  N N 385 
TRP   H    H  N N 386 
TRP   H2   H  N N 387 
TRP   HA   H  N N 388 
TRP   HB2  H  N N 389 
TRP   HB3  H  N N 390 
TRP   HD1  H  N N 391 
TRP   HE1  H  N N 392 
TRP   HE3  H  N N 393 
TRP   HZ2  H  N N 394 
TRP   HZ3  H  N N 395 
TRP   HH2  H  N N 396 
TRP   HXT  H  N N 397 
TYR   N    N  N N 398 
TYR   CA   C  N S 399 
TYR   C    C  N N 400 
TYR   O    O  N N 401 
TYR   CB   C  N N 402 
TYR   CG   C  Y N 403 
TYR   CD1  C  Y N 404 
TYR   CD2  C  Y N 405 
TYR   CE1  C  Y N 406 
TYR   CE2  C  Y N 407 
TYR   CZ   C  Y N 408 
TYR   OH   O  N N 409 
TYR   OXT  O  N N 410 
TYR   H    H  N N 411 
TYR   H2   H  N N 412 
TYR   HA   H  N N 413 
TYR   HB2  H  N N 414 
TYR   HB3  H  N N 415 
TYR   HD1  H  N N 416 
TYR   HD2  H  N N 417 
TYR   HE1  H  N N 418 
TYR   HE2  H  N N 419 
TYR   HH   H  N N 420 
TYR   HXT  H  N N 421 
VAL   N    N  N N 422 
VAL   CA   C  N S 423 
VAL   C    C  N N 424 
VAL   O    O  N N 425 
VAL   CB   C  N N 426 
VAL   CG1  C  N N 427 
VAL   CG2  C  N N 428 
VAL   OXT  O  N N 429 
VAL   H    H  N N 430 
VAL   H2   H  N N 431 
VAL   HA   H  N N 432 
VAL   HB   H  N N 433 
VAL   HG11 H  N N 434 
VAL   HG12 H  N N 435 
VAL   HG13 H  N N 436 
VAL   HG21 H  N N 437 
VAL   HG22 H  N N 438 
VAL   HG23 H  N N 439 
VAL   HXT  H  N N 440 
ZN    ZN   ZN N N 441 
# 
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 
A1B3G C   S    sing N N 1   
A1B3G S   C1   sing N N 2   
A1B3G C1  C2   doub Y N 3   
A1B3G C2  C3   sing Y N 4   
A1B3G C3  C4   doub Y N 5   
A1B3G C4  C5   sing Y N 6   
A1B3G C5  C6   doub Y N 7   
A1B3G C1  C6   sing Y N 8   
A1B3G C6  C7   sing N N 9   
A1B3G C7  C8   sing N N 10  
A1B3G O   C8   doub N N 11  
A1B3G C8  N    sing N N 12  
A1B3G N   C9   sing N N 13  
A1B3G C9  C10  sing N N 14  
A1B3G C10 C11  sing N N 15  
A1B3G C11 C12  sing N N 16  
A1B3G F   C12  sing N N 17  
A1B3G C12 C13  sing N N 18  
A1B3G N1  C13  sing N N 19  
A1B3G C13 O1   doub N N 20  
A1B3G C14 C12  sing N N 21  
A1B3G N   C14  sing N N 22  
A1B3G N1  H16  sing N N 23  
A1B3G N1  H15  sing N N 24  
A1B3G C4  H5   sing N N 25  
A1B3G C5  H6   sing N N 26  
A1B3G C7  H7   sing N N 27  
A1B3G C7  H8   sing N N 28  
A1B3G C10 H11  sing N N 29  
A1B3G C10 H12  sing N N 30  
A1B3G C11 H13  sing N N 31  
A1B3G C11 H14  sing N N 32  
A1B3G C9  H10  sing N N 33  
A1B3G C9  H9   sing N N 34  
A1B3G C14 H17  sing N N 35  
A1B3G C14 H18  sing N N 36  
A1B3G C   H1   sing N N 37  
A1B3G C   H    sing N N 38  
A1B3G C   H2   sing N N 39  
A1B3G C3  H4   sing N N 40  
A1B3G C2  H3   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_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                    7I4Z 
_atom_sites.fract_transf_matrix[1][1]   0.013778 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000715 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016225 
_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]   0.030620 
_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  
F  
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   ? 18.730 6.362   24.217 1.00 37.54 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.961 6.358   23.421 1.00 38.11 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.036 5.183   22.435 1.00 36.46 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.330 4.179   22.609 1.00 37.06 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.174 6.333   24.344 1.00 40.88 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.079 5.171   25.154 1.00 44.75 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.910 5.307   21.429 1.00 34.10 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.125 4.271   20.421 1.00 32.47 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.384 4.806   19.023 1.00 30.57 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.862 5.858   18.652 1.00 30.57 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.184 4.083   18.232 1.00 28.48 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.553 4.471   16.874 1.00 27.33 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.537 3.282   15.879 1.00 26.68 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.563 2.122   16.311 1.00 26.35 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.950 5.064   16.909 1.00 27.85 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.508 3.576   14.551 1.00 26.26 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.648 2.601   13.458 1.00 26.54 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.054 2.826   12.853 1.00 30.27 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.404 3.940   12.463 1.00 30.47 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.588 2.779   12.339 1.00 25.04 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.143 2.723   12.870 1.00 23.33 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.793 1.734   11.229 1.00 25.54 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.198 3.368   11.940 1.00 23.14 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.842 1.772   12.757 1.00 33.29 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.193 1.821   12.210 1.00 36.65 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.219 1.053   10.886 1.00 38.82 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.136 -0.167  10.922 1.00 38.87 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.146 1.133   13.215 1.00 37.33 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.312 1.954   14.473 1.00 38.07 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.159 3.050   14.503 1.00 39.47 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.583 1.663   15.617 1.00 38.55 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.256 3.859   15.628 1.00 40.48 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.686 2.452   16.754 1.00 39.43 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.553 3.525   16.768 1.00 40.77 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.691 4.283   17.894 1.00 42.35 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.249 1.754   9.734  1.00 40.11 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.256 1.118   8.404  1.00 41.53 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.350 1.734   7.530  1.00 43.37 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.359 2.953   7.297  1.00 43.95 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.874 1.177   7.704  1.00 42.09 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.303 2.596   7.704  1.00 41.91 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.961 0.627   6.287  1.00 43.00 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.324 0.918   7.094  1.00 43.96 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.456 1.435   6.330  1.00 46.14 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.232 2.440   7.162  1.00 47.72 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.317 2.263   8.383  1.00 48.56 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.632 3.574   6.572  1.00 47.88 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.322 4.615   7.331  1.00 47.73 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.347 5.639   7.932  1.00 43.94 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.744 6.790   8.147  1.00 43.22 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.353 5.322   6.461  1.00 52.72 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.402 4.378   5.928  1.00 60.30 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 33.811 3.416   6.584  1.00 61.83 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.881 4.647   4.723  1.00 64.64 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.114 5.201   8.261  1.00 40.69 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.067 6.086   8.797  1.00 38.25 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.518 5.676   10.154 1.00 35.55 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.311 4.492   10.444 1.00 34.09 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.879 6.173   7.814  1.00 37.41 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.237 6.784   6.479  1.00 38.76 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.822 8.043   6.402  1.00 39.93 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.892 6.156   5.291  1.00 39.87 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.151 8.612   5.178  1.00 41.52 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.192 6.724   4.061  1.00 41.59 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.845 7.943   4.007  1.00 43.33 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.148 8.510   2.791  1.00 46.12 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.153 6.694   10.938 1.00 33.58 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.481 6.508   12.210 1.00 31.10 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.206 7.363   12.126 1.00 27.61 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.286 8.563   11.878 1.00 27.71 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.388 6.938   13.371 1.00 32.29 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.686 7.176   14.694 1.00 35.05 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.706 7.548   15.742 1.00 38.63 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.207 8.559   16.670 1.00 41.00 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.742 8.297   17.888 1.00 42.74 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.692 7.044   18.336 1.00 40.69 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.319 9.286   18.670 1.00 41.09 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.036 6.742   12.266 1.00 24.73 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.725 7.418   12.229 1.00 23.32 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.231 7.542   13.659 1.00 22.05 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.194 6.543   14.355 1.00 22.25 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.686 6.643   11.384 1.00 22.34 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.419 7.496   11.171 1.00 21.77 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.282 6.160   10.042 1.00 21.75 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.827 8.719   14.101 1.00 20.37 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.359 8.917   15.483 1.00 20.02 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.149 9.862   15.470 1.00 17.72 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.976 10.607  14.500 1.00 16.63 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.478 9.560   16.370 1.00 21.74 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.573 8.577   16.737 1.00 23.21 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.048 10.819  15.722 1.00 22.12 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.387 9.962   16.594 1.00 17.39 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.344 11.007  16.696 1.00 17.43 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.107 12.337  16.742 1.00 19.22 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.108 12.448  17.481 1.00 20.47 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.550 10.911  18.007 1.00 18.01 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.759 9.632   18.140 1.00 18.93 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.287 8.601   18.566 1.00 22.51 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.495 9.678   17.796 1.00 16.62 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.684 13.295  15.929 1.00 17.71 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.341 14.589  15.843 1.00 17.17 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.390 15.293  17.205 1.00 19.96 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.435 15.867  17.533 1.00 21.43 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.695 15.446  14.745 1.00 16.10 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.497 16.728  14.386 1.00 17.39 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.555 17.641  13.614 1.00 17.29 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.138 18.894  13.101 1.00 17.37 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.193 20.031  13.792 1.00 21.46 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.814 20.062  15.065 1.00 21.28 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.622 21.150  13.211 1.00 21.69 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.313 15.183  18.024 1.00 21.07 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.284 15.813  19.366 1.00 23.38 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.272 15.190  20.351 1.00 27.22 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.616 15.814  21.359 1.00 28.62 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.859 15.875  19.943 1.00 23.71 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.281 14.581  20.429 1.00 23.78 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.762 13.644  19.546 1.00 24.86 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.101 14.133  21.705 1.00 23.33 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.319 12.633  20.302 1.00 25.17 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.493 12.884  21.613 1.00 24.31 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.802 14.004  20.031 1.00 28.57 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.775 13.327  20.885 1.00 29.80 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.202 13.312  20.321 1.00 30.73 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.074 12.644  20.899 1.00 31.70 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.285 11.893  21.145 1.00 30.18 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.970 11.795  21.952 1.00 32.09 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.573 10.351  22.199 1.00 32.16 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.075 12.542  23.297 1.00 32.39 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.430 13.952  19.160 1.00 30.59 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.741 13.951  18.517 1.00 31.89 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.785 14.612  19.418 1.00 34.59 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.461 15.555  20.147 1.00 34.20 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.668 14.667  17.160 1.00 31.10 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.016 14.086  19.385 1.00 37.26 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.149 14.564  20.192 1.00 40.59 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.970 15.670  19.464 1.00 42.36 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.713 15.954  18.295 1.00 40.47 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.057 13.358  20.541 1.00 43.33 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.771 12.957  19.371 1.00 45.72 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.296 12.189  21.136 1.00 43.61 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.020 16.244  20.139 1.00 45.63 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.884 17.239  19.501 1.00 48.62 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.619 16.588  18.331 1.00 48.32 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.763 17.229  17.288 1.00 47.23 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.916 17.787  20.494 1.00 53.22 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.332 18.616  21.591 1.00 60.41 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.871 19.895  21.359 1.00 63.88 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.230 18.344  22.915 1.00 63.05 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.467 20.350  22.533 1.00 64.96 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 29.669 19.455  23.502 1.00 64.92 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.077 15.311  18.513 1.00 48.56 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.742 14.486  17.493 1.00 49.20 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.856 14.285  16.282 1.00 46.09 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.326 14.484  15.170 1.00 47.04 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.170 13.125  18.045 1.00 53.57 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.362 12.557  17.330 1.00 61.87 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.362 13.246  17.129 1.00 65.10 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.277 11.295  16.913 1.00 63.99 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.576 13.922  16.486 1.00 43.13 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.582 13.791  15.409 1.00 39.86 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.495 15.065  14.566 1.00 37.62 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.559 15.004  13.349 1.00 37.08 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.196 13.444  15.993 1.00 38.58 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.113 12.014  16.486 1.00 39.57 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.783 11.158  15.908 1.00 39.18 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.392 11.766  17.471 1.00 40.00 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.396 16.224  15.219 1.00 36.24 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.296 17.517  14.534 1.00 35.85 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.641 17.934  13.849 1.00 38.80 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.616 18.563  12.794 1.00 39.04 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.828 18.579  15.550 1.00 33.47 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.335 18.656  15.672 1.00 30.30 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.554 18.161  16.678 1.00 29.81 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.439 19.190  14.693 1.00 28.36 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.223 18.415  16.408 1.00 29.73 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.128 19.040  15.194 1.00 28.53 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.616 19.777  13.440 1.00 28.45 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.009 19.498  14.499 1.00 27.94 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.508 20.247  12.765 1.00 28.00 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.220 20.065  13.275 1.00 27.80 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.785 17.579  14.450 1.00 40.71 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.136 17.846  13.902 1.00 43.99 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.452 16.943  12.679 1.00 45.91 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.412 17.218  11.941 1.00 48.27 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.205 17.587  14.974 1.00 44.42 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.733 15.809  12.557 1.00 44.12 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.854 14.836  11.480 1.00 43.20 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.511 14.694  10.729 1.00 39.10 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.162 13.605  10.296 1.00 38.02 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.272 13.507  12.073 1.00 46.52 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.715 13.525  12.517 1.00 53.09 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.600 13.864  11.737 1.00 55.85 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.993 13.121  13.761 1.00 53.17 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.762 15.785  10.613 1.00 36.26 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.439 15.834  9.980  1.00 33.48 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.453 15.443  8.503  1.00 32.94 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.256 15.987  7.741  1.00 34.42 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.855 17.255  10.120 1.00 32.30 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.478 17.502  9.487  1.00 31.65 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.387 16.569  10.110 1.00 32.17 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.083 18.970  9.577  1.00 29.89 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.545 14.520  8.097  1.00 30.16 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.301 14.162  6.701  1.00 29.83 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.969 14.833  6.220  1.00 28.05 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.929 15.522  5.196  1.00 30.02 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.246 12.627  6.504  1.00 31.72 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.755 12.277  5.107  1.00 32.50 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.612 11.972  6.772  1.00 33.38 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.899 14.669  7.001  1.00 24.57 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.572 15.195  6.690  1.00 22.18 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.710 15.221  7.985  1.00 19.89 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.891 14.401  8.878  1.00 20.16 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.928 14.248  5.622  1.00 21.58 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.443 14.375  5.429  1.00 21.21 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.789 15.250  4.612  1.00 22.30 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.425 13.572  6.054  1.00 20.12 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.422 15.090  4.742  1.00 22.18 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.174 14.076  5.632  1.00 21.12 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.447 12.568  7.028  1.00 19.46 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.964 13.475  6.008  1.00 20.37 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.252 11.978  7.401  1.00 19.68 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.028 12.454  6.921  1.00 19.56 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.813 16.166  8.083  1.00 17.90 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.894 16.251  9.225  1.00 16.80 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.567 16.838  8.730  1.00 16.45 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.535 17.580  7.739  1.00 15.73 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.505 17.018  10.425 1.00 17.88 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.092 18.384  10.084 1.00 18.86 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.102 19.521  9.891  1.00 21.21 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.422 20.467  9.136  1.00 24.65 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.004 19.467  10.481 1.00 21.19 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.469 16.457  9.386  1.00 15.50 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.171 16.965  9.013  1.00 15.15 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.350 17.109  10.283 1.00 15.24 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 15.858 16.123  10.821 1.00 15.30 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.492 16.076  7.954  1.00 17.03 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.210 16.651  7.388  1.00 20.20 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.520 17.384  8.108  1.00 18.60 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.892 16.352  6.218  1.00 23.36 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.176 18.372  10.750 1.00 15.15 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.409 18.668  11.939 0.50 15.52 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.409 18.621  11.962 0.50 15.67 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 13.966 18.129  11.824 1.00 15.73 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.414 17.639  12.790 1.00 16.44 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.397 20.181  12.160 0.50 17.08 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.416 20.110  12.313 0.50 17.71 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.904 20.515  13.439 0.50 18.73 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.788 20.824  11.262 0.50 20.42 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.347 18.246  10.612 1.00 14.52 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 11.969 17.789  10.461 1.00 16.18 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.831 16.278  10.617 1.00 15.29 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.729 15.830  10.899 1.00 16.79 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.354 18.255  9.145  1.00 19.07 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.891 17.479  8.085  1.00 24.22 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.914 15.508  10.443 1.00 13.75 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.916 14.029  10.633 1.00 13.06 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.516 13.588  11.958 1.00 14.42 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.478 12.395  12.267 1.00 15.20 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.672 13.326  9.486  1.00 13.09 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 12.998 13.542  8.148  1.00 12.92 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.770 12.922  7.001  1.00 14.58 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.807 11.460  7.103  1.00 14.39 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.928 10.644  6.051  1.00 16.50 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 13.991 11.138  4.821  1.00 17.27 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.950 9.323   6.226  1.00 17.29 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.118 14.539  12.737 1.00 14.18 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.860 14.244  13.969 1.00 13.44 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.013 13.259  13.638 1.00 13.22 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.301 12.373  14.452 1.00 12.89 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.966 13.649  15.063 1.00 14.48 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.715 13.380  16.360 1.00 17.93 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.588 14.203  16.727 1.00 17.73 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.462 12.322  16.986 1.00 20.44 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.647 13.382  12.450 1.00 12.50 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.793 12.486  12.111 1.00 12.54 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.099 13.255  11.865 1.00 15.02 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.096 14.369  11.355 1.00 16.70 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.540 11.659  10.833 1.00 12.37 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.489 10.543  10.908 1.00 13.48 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.348 9.866   9.516  1.00 12.67 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.851 9.512   11.975 1.00 14.59 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.207 12.618  12.161 1.00 15.32 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.522 13.181  11.892 1.00 17.11 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.396 12.000  11.573 1.00 18.54 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.279 10.957  12.221 1.00 19.25 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.045 13.998  13.117 1.00 17.79 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.426 14.611  12.966 1.00 20.42 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.528 15.930  13.678 1.00 21.17 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.528 13.629  13.413 1.00 21.98 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.237 12.130  10.538 1.00 19.52 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.209 11.095  10.151 1.00 22.15 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.614 11.690  10.258 1.00 25.48 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.872 12.769  9.711  1.00 25.32 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.959 10.541  8.726  1.00 22.60 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.011 9.466   8.355  1.00 24.29 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.539 9.977   8.627  1.00 22.75 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.506 10.988  10.959 1.00 28.90 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.910 11.377  11.065 1.00 32.43 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.853 10.299  10.523 1.00 36.70 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.501 9.123   10.459 1.00 34.52 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.282 11.769  12.488 1.00 33.69 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.120 10.691  13.389 1.00 36.38 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.084 10.709  10.138 1.00 41.30 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.052 9.766   9.598  1.00 46.38 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.859 9.081   10.689 1.00 51.64 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.088 9.661   11.749 1.00 52.30 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 31.982 10.450  8.611  1.00 47.68 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.570 11.574  9.243  1.00 52.24 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.244 7.827   10.447 1.00 55.13 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.996 7.024   11.413 1.00 59.82 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.330 6.549   10.808 1.00 66.24 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.529 6.654   9.599  1.00 66.90 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.149 5.819   11.865 1.00 59.68 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.063 4.897   10.786 1.00 60.16 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.770 6.208   12.338 1.00 59.20 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.231 6.018   11.652 1.00 70.78 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.535 5.473   11.257 1.00 75.07 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.510 3.925   11.115 1.00 77.40 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.488 3.315   10.664 1.00 80.29 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.566 5.844   12.323 1.00 78.67 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.171 5.210   13.554 1.00 81.48 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.697 7.328   12.516 1.00 78.69 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.460 3.287   11.610 1.00 76.16 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.311 1.848   11.539 1.00 75.35 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.126 1.518   10.632 1.00 74.04 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.230 2.344   10.439 1.00 74.09 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.095 1.285   12.929 1.00 75.63 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.146 0.330   10.042 1.00 73.03 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.113 -0.154  9.129  1.00 71.94 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.917 -0.755  9.874  1.00 69.34 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.082 -1.689  10.658 1.00 69.84 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.733 -1.182  8.158  1.00 74.72 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.739 -2.055  7.382  1.00 80.22 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.316 -1.462  6.062  1.00 87.24 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 32.718 -0.345  5.673  1.00 89.66 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.496 -2.217  5.338  1.00 88.25 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.726 -0.259  9.553  1.00 66.03 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.454 -0.704  10.110 1.00 63.85 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.809 -1.831  9.317  1.00 60.45 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 28.801 -1.817  8.082  1.00 60.39 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.222 -2.775  10.016 1.00 57.33 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.655 -3.953  9.376  1.00 55.39 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.147 -4.080  9.494  1.00 51.35 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.617 -5.147  9.154  1.00 51.33 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.360 -5.203  9.876  1.00 58.58 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.116 -5.271  9.451  1.00 68.26 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.438 -2.999  9.914  1.00 47.17 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.981 -3.084  9.965  1.00 44.89 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.465 -3.051  8.553  1.00 42.39 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 23.923 -2.257  7.732  1.00 43.54 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.343 -1.910  10.732 1.00 46.28 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.513 -1.965  12.223 1.00 49.76 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.651 -3.075  12.763 1.00 51.91 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.514 -0.901  12.850 1.00 50.42 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.527 -3.893  8.275  1.00 40.09 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.880 -3.941  6.981  1.00 39.05 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.660 -3.047  7.070  1.00 35.81 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.966 -3.073  8.084  1.00 36.18 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.538 -5.404  6.636  1.00 42.24 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.718 -5.981  6.060  1.00 45.95 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.390 -5.531  5.645  1.00 41.50 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.419 -2.233  6.045  1.00 32.57 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.225 -1.416  6.019  1.00 29.85 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.204 -2.129  5.158  1.00 28.87 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.540 -2.610  4.044  1.00 29.95 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.467 0.013   5.494  1.00 28.81 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.672 0.700   6.188  1.00 29.31 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.169 0.845   5.621  1.00 27.88 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.479 0.905   7.705  1.00 30.07 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.972 -2.204  5.663  1.00 26.82 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.846 -2.779  4.956  1.00 25.98 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.423 -1.840  3.828  1.00 26.99 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.407 -0.618  4.004  1.00 26.88 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.684 -2.967  5.913  1.00 23.47 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.055 -2.415  2.680  1.00 27.91 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.600 -1.661  1.513  1.00 30.48 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.265 -2.296  1.157  1.00 33.42 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.217 -3.213  0.333  1.00 36.34 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.621 -1.808  0.385  1.00 32.47 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.000 -1.209  0.672  1.00 33.27 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.993 0.277   1.096  1.00 33.88 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.346 0.761   1.396  1.00 33.12 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.619 1.869   2.079  1.00 32.32 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.644 2.673   2.468  1.00 27.90 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.877 2.207   2.330  1.00 32.94 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.192 -1.911  1.885  1.00 32.59 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.910 -2.613  1.777  1.00 32.17 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.740  -1.694  2.186  1.00 32.10 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.950  -0.546  2.553  1.00 31.45 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.990 -3.788  2.742  1.00 31.30 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.157 -3.261  4.475  1.00 28.78 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.497  -2.247  2.201  1.00 31.89 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.361  -1.509  2.730  1.00 32.55 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.683  -2.298  3.866  1.00 31.37 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.472  -2.203  4.051  1.00 32.49 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.376  -1.018  1.652  1.00 36.63 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.449  -2.049  1.052  1.00 45.60 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.635  -3.250  1.332  1.00 46.43 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.527  -1.652  0.301  1.00 51.74 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.463  -3.096  4.640  1.00 29.00 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.956  -3.839  5.803  1.00 26.43 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.229  -2.876  6.760  1.00 25.47 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.681  -1.745  6.972  1.00 25.71 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.096  -4.538  6.558  1.00 25.45 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.725  -6.059  5.796  1.00 27.21 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.148  -3.338  7.344  1.00 23.64 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.430  -2.650  8.402  1.00 22.78 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.402  -3.473  9.688  1.00 20.04 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.519  -3.250  10.507 1.00 20.19 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.001  -2.263  7.991  1.00 25.23 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.918  -0.958  7.193  1.00 29.76 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.478  -0.566  6.947  1.00 33.81 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.967  -0.668  5.832  1.00 35.62 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.778  -0.153  8.001  1.00 34.33 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.308  -4.493  9.829  1.00 18.63 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.499  -5.312  11.021 1.00 17.50 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 7.000  -5.466  11.269 1.00 15.37 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.811  -5.545  10.337 1.00 15.62 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.802  -6.705  10.961 1.00 20.63 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.502  -7.530  10.025 1.00 23.30 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.331  -6.619  10.578 1.00 20.76 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.353  -5.534  12.535 1.00 13.12 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.742  -5.633  12.928 1.00 12.11 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.886  -5.780  14.432 1.00 12.58 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.908  -6.047  15.118 1.00 14.55 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.101 -5.629  14.915 1.00 11.39 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.437 -5.774  16.338 1.00 11.19 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.306 -4.559  16.730 1.00 11.78 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.307 -4.277  16.058 1.00 12.00 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.219 -7.113  16.585 1.00 12.32 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.707 -7.194  18.045 1.00 13.34 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.328 -8.310  16.290 1.00 12.62 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.996 -3.916  17.854 1.00 11.56 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.850 -2.786  18.311 1.00 11.25 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.432 -3.056  19.688 1.00 13.33 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.844 -3.788  20.469 1.00 13.82 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.089 -1.409  18.294 1.00 11.77 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.144 -1.177  19.449 1.00 14.00 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.902  -1.801  19.494 1.00 14.94 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.470 -0.296  20.482 1.00 15.62 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.984  -1.513  20.505 1.00 16.91 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.569  -0.026  21.516 1.00 17.38 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.333  -0.655  21.530 1.00 17.83 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.429  -0.412  22.531 1.00 20.10 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.546 -2.397  20.003 1.00 15.30 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.163 -2.510  21.325 1.00 18.30 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.671 -1.358  22.202 1.00 18.96 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.762 -0.189  21.809 1.00 17.22 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.697 -2.503  21.248 1.00 20.25 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.307 -2.653  22.624 1.00 23.25 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.169 -3.835  23.336 1.00 25.84 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.936 -1.581  23.251 1.00 25.58 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.681 -3.970  24.618 1.00 28.14 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.443 -1.698  24.540 1.00 27.91 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.309 -2.895  25.219 1.00 30.51 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.772 -3.029  26.500 1.00 36.01 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.186 -1.700  23.407 1.00 21.44 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.653 -0.728  24.355 1.00 24.03 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.523 -0.707  25.629 1.00 26.05 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.375 -1.575  26.495 1.00 26.56 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.189 -1.047  24.657 1.00 25.44 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.471 -0.090  26.029 1.00 28.71 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.472 0.256   25.704 1.00 27.54 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.402 0.360   26.816 1.00 30.87 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.720 0.486   28.163 1.00 32.56 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.200 -0.121  29.132 1.00 35.04 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.399 1.498   26.614 1.00 35.10 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.742 2.738   26.427 1.00 40.90 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.581 1.204   28.238 1.00 32.46 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.840 1.365   29.508 1.00 34.59 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.211 0.042   30.037 1.00 35.99 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.753 -0.016  31.187 1.00 38.30 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.796 2.473   29.410 1.00 35.18 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.786 2.120   28.477 1.00 36.58 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.245 -1.014  29.231 1.00 34.73 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.755 -2.314  29.654 1.00 34.69 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.829 -3.402  29.554 1.00 35.15 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.541 -4.567  29.882 1.00 35.62 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.523 -2.692  28.821 1.00 34.63 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.280  -1.893  29.189 1.00 36.34 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.787  -2.214  30.596 1.00 38.63 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.552  -1.490  30.889 1.00 43.52 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.497  -0.256  31.376 1.00 46.22 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.615  0.400   31.674 1.00 47.86 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.325  0.327   31.593 1.00 46.91 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.054 -3.057  29.042 1.00 34.62 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.135 -3.997  28.729 1.00 34.91 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.560 -5.192  27.897 1.00 32.40 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.858 -6.381  28.145 1.00 31.89 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.866 -4.456  30.003 1.00 38.24 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.989 -3.526  30.400 1.00 45.65 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.855 -4.172  31.459 1.00 52.54 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.377 -3.163  32.368 1.00 60.70 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.214 -3.181  33.687 1.00 66.13 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.550 -4.175  34.270 1.00 66.53 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.690 -2.190  34.434 1.00 67.65 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.659 -4.862  26.938 1.00 29.41 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.976 -5.915  26.174 1.00 27.59 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.769 -5.509  24.723 1.00 24.80 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.600 -4.317  24.445 1.00 25.14 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.544 -6.130  26.728 1.00 30.20 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.357 -7.243  27.722 1.00 37.83 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.907  -7.253  28.202 1.00 44.65 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.532  -8.499  28.985 1.00 50.12 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.609  -8.277  30.461 1.00 52.12 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.617 -6.510  23.846 1.00 21.90 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.229 -6.252  22.469 1.00 19.75 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.713 -6.535  22.359 1.00 19.48 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.190 -7.416  23.062 1.00 20.91 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.980 -7.164  21.497 1.00 19.55 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.463 -6.974  21.459 1.00 20.26 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.080 -6.308  20.404 1.00 22.20 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.415 -7.433  22.296 1.00 20.45 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.374 -6.363  20.653 1.00 21.51 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.624 -7.005  21.793 1.00 21.89 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.993  -5.771  21.530 1.00 17.00 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.561  -6.013  21.362 1.00 16.33 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.188  -6.104  19.902 1.00 15.84 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.638  -5.299  19.104 1.00 14.87 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.743  -4.870  21.967 1.00 17.15 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.777  -4.828  23.473 1.00 19.59 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.973  -5.672  24.232 1.00 22.05 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.518  -3.869  24.137 1.00 22.24 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.965  -5.602  25.626 1.00 23.81 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.525  -3.797  25.526 1.00 23.88 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.732  -4.647  26.262 1.00 25.67 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.701  -4.512  27.632 1.00 29.05 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.298  -7.039  19.541 1.00 16.53 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.789  -7.053  18.151 1.00 16.07 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.733  -5.946  17.969 1.00 16.80 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.929  -5.723  18.891 1.00 18.43 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.179  -8.454  18.005 1.00 16.94 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.845  -8.865  19.418 1.00 18.03 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.672  -8.083  20.395 1.00 17.05 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.689  -5.288  16.794 1.00 15.84 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.738  -4.195  16.531 1.00 17.00 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.245  -4.203  15.105 1.00 18.21 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.952  -4.658  14.203 1.00 17.68 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.352  -2.762  16.793 1.00 17.39 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.480  -2.446  18.277 1.00 19.11 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.668  -2.557  16.052 1.00 17.38 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 3.033  -3.667  14.900 1.00 18.32 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.497  -3.295  13.601 1.00 20.64 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.677  -1.768  13.628 1.00 21.37 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.490  -1.149  14.690 1.00 22.90 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.009  -3.603  13.455 1.00 23.31 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.765  -4.999  13.414 1.00 29.02 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.132  -1.191  12.532 1.00 19.23 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.398  0.240   12.488 1.00 18.67 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.875  0.869   11.211 1.00 20.78 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.729  0.184   10.201 1.00 22.46 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.894  0.525   12.744 1.00 16.72 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.884  -0.187  11.842 1.00 14.85 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.459  -1.384  12.231 1.00 13.58 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.282  0.380   10.625 1.00 14.87 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.408  -2.021  11.424 1.00 14.08 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.234  -0.249  9.820  1.00 14.55 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.774  -1.462  10.204 1.00 13.77 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.532  2.174   11.254 1.00 20.51 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 1.948  2.854   10.119 1.00 22.31 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.000  3.189   9.029  1.00 23.16 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.193  3.014   9.248  1.00 21.83 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.290  4.144   10.610 1.00 24.78 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.292  5.032   11.104 1.00 26.39 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.554  3.679   7.868  1.00 25.21 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.477  4.075   6.797  1.00 27.04 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.137  5.430   7.124  1.00 27.07 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.539  6.218   7.849  1.00 27.68 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.709  4.177   5.466  1.00 31.80 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 1.975  2.886   5.129  1.00 38.67 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 1.662  2.824   3.636  1.00 47.07 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.658  1.967   2.886  1.00 52.45 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 2.028  0.692   2.420  1.00 55.87 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.364  5.717   6.631  1.00 26.44 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 5.996  7.015   6.953  1.00 27.06 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.140  8.213   6.561  1.00 27.85 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.651  8.279   5.433  1.00 27.56 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.308  6.997   6.163  1.00 27.92 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.569  5.568   5.857  1.00 28.35 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.230  4.880   5.781  1.00 26.09 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 4.917  9.136   7.497  1.00 28.92 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.077  10.310  7.223  1.00 30.39 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.406  11.512  8.146  1.00 29.30 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.250  11.394  9.047  1.00 27.53 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.604  9.913   7.354  1.00 34.62 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.315  9.477   8.673  1.00 38.76 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.743  12.670  7.896  1.00 29.98 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 3.862  13.906  8.667  1.00 31.20 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 2.941  13.786  9.849  1.00 32.86 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.727  13.636  9.659  1.00 35.03 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.399  15.122  7.819  1.00 31.62 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.458  15.800  6.984  1.00 33.36 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.856  16.936  6.154  1.00 35.65 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.564  16.364  7.859  1.00 33.25 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.480  13.844  11.059 1.00 32.63 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.681  13.726  12.263 1.00 34.55 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.048  14.868  13.204 1.00 36.09 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.231  15.122  13.425 1.00 35.49 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 2.872  12.326  12.932 1.00 35.23 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.274  11.202  12.060 1.00 36.17 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.278  12.282  14.345 1.00 36.11 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.924  9.864   12.275 1.00 37.39 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.070  15.650  13.672 1.00 37.10 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.420  16.852  14.486 1.00 39.55 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.083  16.435  15.806 1.00 38.94 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 2.838  15.293  16.244 1.00 39.80 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.187  17.720  14.746 1.00 42.29 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.433  18.827  15.738 1.00 44.93 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 2.092  19.984  15.357 1.00 47.11 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.038  18.696  17.059 1.00 46.70 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 2.330  20.996  16.272 1.00 48.90 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.279  19.708  17.974 1.00 47.81 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 1.922  20.856  17.578 1.00 48.36 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 3.880  17.318  16.430 1.00 38.27 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 4.632  16.848  17.708 1.00 38.99 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 4.892  17.894  18.930 1.00 40.96 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 5.295  18.774  18.639 1.00 40.92 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.121  16.020  17.606 1.00 38.90 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.076  15.742  18.701 1.00 39.80 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 5.959  14.865  16.702 1.00 38.52 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 5.060  17.804  20.159 1.00 42.46 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 5.185  18.852  20.919 1.00 44.32 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.454  19.281  21.393 1.00 44.53 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 7.342  18.717  21.320 1.00 44.34 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.297  18.184  21.855 1.00 49.46 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 2.830  18.301  21.483 1.00 57.96 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 1.920  18.679  22.638 1.00 67.46 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 2.023  19.826  23.116 1.00 71.68 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 1.115  17.826  23.058 1.00 70.04 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 6.384  20.478  21.903 1.00 44.55 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 7.681  20.949  22.240 1.00 45.60 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 8.770  20.239  23.187 1.00 46.77 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 8.503  19.665  23.683 1.00 47.76 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 7.566  22.345  22.715 1.00 45.77 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 9.913  20.903  23.488 1.00 46.37 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 10.946 20.191  24.186 1.00 46.52 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 12.431 21.007  24.341 1.00 47.46 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 12.641 21.681  23.695 1.00 47.43 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 11.488 18.894  23.455 1.00 47.45 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.890 18.780  22.163 1.00 49.09 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 13.173 20.648  25.087 1.00 47.33 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 14.634 21.365  25.422 1.00 47.37 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 15.022 21.430  23.914 1.00 44.45 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 15.700 21.848  23.826 1.00 45.02 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 15.179 21.122  26.568 1.00 52.25 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 14.441 20.263  27.488 1.00 60.48 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 13.989 18.944  27.018 1.00 68.98 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 14.910 18.260  26.822 1.00 69.41 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 12.734 18.689  26.892 1.00 72.25 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.772 20.496  22.777 1.00 41.19 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.040 20.198  21.369 1.00 38.58 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.208 20.935  20.406 1.00 36.10 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.489 21.243  19.759 1.00 36.87 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.153 18.541  21.372 1.00 37.81 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.465 17.780  22.584 1.00 38.30 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 16.717 17.799  22.927 1.00 39.48 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.560 17.048  23.223 1.00 39.10 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.159 17.094  23.929 1.00 40.95 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 14.975 16.318  24.275 1.00 40.73 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.248 16.454  24.675 1.00 42.30 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.937 15.813  25.631 1.00 44.60 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 13.046 20.825  20.393 1.00 33.50 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.158 21.483  19.196 1.00 32.26 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.773 22.153  19.267 1.00 34.14 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.090 21.775  20.428 1.00 34.90 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.610 20.372  18.291 1.00 29.16 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.639 19.421  17.757 1.00 25.29 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 12.743 18.108  18.190 1.00 24.45 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.399 19.786  16.753 1.00 24.26 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 13.661 17.199  17.746 1.00 23.24 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.242 18.854  16.314 1.00 23.29 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.542 17.552  16.788 1.00 22.31 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.496 16.716  16.295 1.00 18.46 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.485 23.422  18.956 1.00 34.74 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 9.165  23.846  19.067 1.00 35.99 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.839  23.042  18.645 1.00 36.75 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 7.849  22.087  17.676 1.00 36.25 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.775  24.767  17.787 1.00 37.06 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.468 23.919  16.932 1.00 36.58 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 11.614 23.548  17.869 1.00 34.52 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.590  23.148  19.069 1.00 37.62 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.628  22.511  18.329 1.00 38.44 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.810  22.226  16.688 1.00 36.15 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 5.563  23.022  15.913 1.00 36.22 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.415  22.519  18.900 1.00 39.79 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.518  21.249  16.152 1.00 33.65 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 5.766  20.902  14.826 1.00 31.77 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.308  19.643  14.096 1.00 29.78 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.060  18.789  14.822 1.00 29.68 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.140  21.131  14.235 1.00 31.14 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.053  19.855  14.297 1.00 29.62 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.381  20.002  14.936 1.00 27.73 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.379 19.022  14.582 1.00 25.40 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.685 17.897  15.266 1.00 22.71 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.373 16.862  14.778 1.00 18.25 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 9.852  17.772  16.344 1.00 23.56 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.347  19.518  12.678 1.00 29.39 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.088  18.235  12.044 1.00 29.48 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.462  17.548  11.831 1.00 25.99 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.418  18.175  11.328 1.00 24.14 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.417  18.391  10.672 1.00 31.86 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 2.971  18.858  10.707 1.00 36.66 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.925  17.948  10.648 1.00 40.12 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.657  20.209  10.679 1.00 39.27 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.596  18.373  10.620 1.00 42.39 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.340  20.645  10.638 1.00 41.78 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.311  19.724  10.626 1.00 44.25 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.993 20.163  10.578 1.00 49.45 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.568  16.288  12.255 1.00 23.13 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.793  15.513  12.020 1.00 20.82 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.492  14.608  10.827 1.00 19.92 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.451  13.938  10.808 1.00 20.20 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 8.221  14.693  13.258 1.00 20.40 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.512  13.869  13.006 1.00 18.77 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 10.158 13.370  14.272 1.00 19.74 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 10.343 14.113  15.239 1.00 18.09 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.580 12.107  14.269 1.00 18.09 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.332  14.653  9.789  1.00 18.09 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.087  13.869  8.573  1.00 17.59 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 8.795  12.495  8.638  1.00 17.93 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.615  12.262  9.547  1.00 17.59 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.581  14.638  7.349  1.00 18.60 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 9.986  14.885  7.392  1.00 20.07 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.383  11.568  7.734  1.00 17.74 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 8.959  10.238  7.641  1.00 17.37 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.821  9.494   8.985  1.00 16.73 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.689  8.707   9.350  1.00 15.95 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.426 10.366  7.212  1.00 17.44 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.575 10.968  5.842  1.00 20.78 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.640 10.176  4.704  1.00 24.12 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.569 12.266  5.460  1.00 22.32 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.715 11.018  3.678  1.00 24.61 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.696 12.282  4.086  1.00 23.62 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.698  9.713   9.681  1.00 17.24 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.504  9.127   11.005 1.00 17.83 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.459  8.017   10.957 1.00 17.44 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.404  8.202   10.350 1.00 18.47 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.046  10.252  11.960 1.00 18.64 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 6.786  9.868   13.433 1.00 20.25 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.042  9.330   14.090 1.00 20.75 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.236  11.100  14.242 1.00 22.55 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.715  6.912   11.660 1.00 16.43 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.763  5.785   11.711 1.00 16.61 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.320  5.574   13.153 1.00 18.89 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.144  5.701   14.038 1.00 19.88 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.459  4.523   11.178 1.00 17.01 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 6.965  4.721   9.747  1.00 19.59 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.029  3.405   9.178  1.00 21.48 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.394  3.573   10.274 1.00 16.96 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.022  5.304   13.411 1.00 19.41 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.565  5.085   14.777 1.00 20.72 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.154  3.625   14.984 1.00 20.89 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.665  2.978   14.072 1.00 20.64 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.374  6.008   15.161 1.00 22.78 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.641  7.501   15.243 1.00 26.38 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.418  8.237   15.807 1.00 28.55 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.869  7.830   16.089 1.00 26.86 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.304  3.158   16.200 1.00 21.06 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.888  1.821   16.632 1.00 22.32 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.343  1.893   18.057 1.00 24.19 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.646  2.823   18.809 1.00 25.01 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.072  0.869   16.580 1.00 22.75 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.480  0.948   18.404 1.00 24.68 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 0.960  0.817   19.756 1.00 27.72 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.028  0.010   20.519 1.00 28.57 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.377  -1.114  20.149 1.00 28.94 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.425 0.107   19.785 1.00 29.86 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.891 -0.134  21.221 1.00 30.61 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.468 0.941   19.029 1.00 30.13 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.603  0.647   21.513 1.00 28.69 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.656  0.045   22.300 1.00 29.60 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.191  1.011   23.324 1.00 29.59 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.020  2.233   23.213 1.00 29.97 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.858  0.441   24.305 1.00 28.57 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.465  1.262   25.361 1.00 28.70 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.708  2.026   24.908 1.00 28.47 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.578  1.453   24.249 1.00 26.96 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.786  0.409   26.588 1.00 29.75 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.470  1.199   27.646 1.00 35.14 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.804  2.137   28.395 1.00 40.28 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.758  1.246   28.032 1.00 37.05 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.649  2.705   29.222 1.00 41.49 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.849  2.177   29.022 1.00 40.55 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.769  3.292   25.300 1.00 28.88 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 7.960  4.116   25.062 1.00 30.79 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 7.946  5.254   26.083 1.00 34.43 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.856  5.698   26.423 1.00 35.34 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 7.974  4.688   23.672 1.00 30.16 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 6.930  5.622   23.463 1.00 31.68 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.105  5.625   26.560 1.00 36.12 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.213  6.810   27.426 1.00 38.69 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.370 7.627   26.852 1.00 40.70 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.167 7.063   26.085 1.00 40.49 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 9.518  6.384   28.863 1.00 42.72 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 8.410  5.610   29.538 1.00 49.46 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 8.879  4.956   30.826 1.00 53.88 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 9.742  5.543   31.499 1.00 56.86 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 8.402  3.858   31.136 1.00 51.45 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.520 8.932   27.182 1.00 42.49 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 11.706 9.660   26.747 1.00 43.62 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 12.859 8.836   27.325 1.00 43.98 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 12.734 8.476   28.477 1.00 48.41 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 11.546 11.046  27.398 1.00 44.20 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.080 11.143  27.775 1.00 44.28 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.585  9.725   27.970 1.00 41.66 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 13.937 8.605   26.579 1.00 40.00 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.055 7.723   26.967 1.00 37.35 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.078 6.522   26.007 1.00 34.73 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.138 5.963   25.770 1.00 35.05 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 13.915 6.215   25.451 1.00 31.81 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 13.797 5.075   24.496 1.00 28.43 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.262 5.489   23.092 1.00 25.29 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.583 4.608   22.305 1.00 23.59 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.374 4.538   24.503 1.00 29.07 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.128 3.647   25.711 1.00 30.91 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.087 3.016   26.166 1.00 30.39 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 10.992 3.605   26.182 1.00 31.89 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.332 6.793   22.831 1.00 24.50 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 14.822 7.292   21.512 1.00 22.88 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.147 6.603   21.140 1.00 22.37 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.010 6.492   21.994 1.00 23.43 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 14.912 8.821   21.514 1.00 23.76 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.280 9.605   21.511 1.00 26.13 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.284 6.148   19.886 1.00 21.03 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.517 5.476   19.465 1.00 21.00 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.410 3.960   19.382 1.00 21.18 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.209 3.309   18.687 1.00 21.58 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.405 3.370   20.048 1.00 19.46 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.189 1.924   19.937 1.00 16.89 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.885 1.527   18.493 1.00 14.21 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.143 2.230   17.807 1.00 13.19 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.506 0.455   18.018 1.00 13.19 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.316 0.043   16.637 1.00 13.03 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 14.996 -0.689  16.422 1.00 13.13 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.619 -1.570  17.238 1.00 14.66 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.575 -0.789  16.209 1.00 15.91 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.753 0.169   15.915 1.00 18.88 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.282 -1.709  15.030 1.00 17.26 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.095 -0.557  15.718 1.00 21.85 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.352 -0.411  15.254 1.00 11.68 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.187 -1.170  14.779 1.00 11.77 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.709 -2.024  13.586 1.00 13.50 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.373 -1.472  12.690 1.00 12.84 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.123 -0.193  14.257 1.00 13.24 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.934 -0.832  13.500 1.00 14.20 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.132 -1.776  14.416 1.00 14.16 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.983  0.281   12.949 1.00 14.75 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.429 -3.352  13.579 1.00 14.26 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.895 -4.215  12.517 1.00 14.14 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.749 -5.075  11.998 1.00 15.28 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.902 -5.468  12.772 1.00 13.96 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.943 -5.218  13.066 1.00 16.04 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.258 -4.649  13.530 1.00 21.92 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.151 -5.775  14.069 1.00 26.64 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.667 -6.500  12.919 1.00 31.04 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.814 -6.216  12.309 1.00 34.94 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.154 -6.852  11.206 1.00 36.97 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.654 -5.335  12.836 1.00 35.34 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.794 -5.416  10.707 1.00 16.01 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.866 -6.371  10.094 1.00 18.32 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.774 -7.521  9.563  1.00 21.62 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 13.982 -7.483  9.795  1.00 22.42 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.079 -5.695  8.969  1.00 19.75 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.117 -5.115  7.600  1.00 20.24 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.226 -8.530  8.864  1.00 24.01 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.046 -9.627  8.320  1.00 27.33 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.116 -9.133  7.306  1.00 29.85 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.068 -9.875  6.996  1.00 31.85 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.134 -10.665 7.638  1.00 30.39 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.403 -10.061 6.434  1.00 34.97 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.360 -10.989 5.858  1.00 43.36 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.147  -10.792 6.050  1.00 46.28 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.819 -12.013 5.135  1.00 44.11 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.964 -7.896  6.775  1.00 29.41 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.906 -7.351  5.785  1.00 29.33 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.071 -6.590  6.386  1.00 27.70 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.018 -6.310  5.667  1.00 28.97 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.215 -6.456  4.729  1.00 31.28 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 13.003 -7.059  4.090  1.00 35.70 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.737 -6.741  4.533  1.00 38.63 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.902 -7.924  3.052  1.00 38.68 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.901 -7.432  3.773  1.00 39.54 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.556 -8.190  2.885  1.00 40.35 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 16.005 -6.245  7.680  1.00 24.65 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.073 -5.482  8.303  1.00 22.53 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.541 -4.266  9.061  1.00 18.98 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.381 -4.256  9.478  1.00 18.52 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.407 -3.277  9.306  1.00 18.70 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.041 -2.066  10.047 1.00 17.99 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.029 -1.184  9.284  1.00 16.78 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.300 -0.782  8.146  1.00 17.41 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.289 -1.225  10.464 1.00 19.95 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.857 0.077   11.151 1.00 19.66 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.190 -2.028  11.407 1.00 20.99 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.891 -0.855  9.938  1.00 14.50 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.824 -0.001  9.392  1.00 14.12 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 13.980 1.478   9.856  1.00 13.72 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.764 2.419   9.089  1.00 14.21 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.423 -0.543  9.844  1.00 15.35 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.297 0.414   9.436  1.00 15.84 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.148 -1.959  9.335  1.00 16.22 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.297 1.652   11.135 1.00 12.68 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.461 2.982   11.694 1.00 12.63 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.808 2.967   13.168 1.00 12.66 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.227 1.937   13.696 1.00 12.69 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.696 4.136   13.803 1.00 10.70 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.011 4.238   15.226 1.00 10.98 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.865 4.898   15.978 1.00 12.42 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.208 5.763   15.428 1.00 12.46 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.323 5.013   15.470 1.00 12.97 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.368 6.340   14.725 1.00 14.06 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.575 4.155   15.168 1.00 14.73 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.545 7.229   15.232 1.00 15.90 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.648 4.537   17.275 1.00 12.16 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.589 5.188   18.053 1.00 12.55 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 12.777 6.719   18.059 1.00 13.75 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 13.884 7.215   18.246 1.00 13.06 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.592 4.657   19.514 1.00 13.63 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.552 5.404   20.345 1.00 14.22 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.327 3.134   19.549 1.00 15.53 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 11.694 7.466   17.806 1.00 14.25 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 11.722 8.922   17.823 1.00 15.36 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 10.230 9.267   18.077 1.00 19.50 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 9.379  8.923   17.258 1.00 20.85 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.193 9.477   16.479 1.00 16.35 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.047 10.891  16.522 1.00 17.92 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 9.930  9.940   19.182 1.00 20.92 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 8.577  10.309  19.678 1.00 22.04 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 7.833  9.130   20.358 1.00 24.78 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.098  7.974   20.084 1.00 24.43 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 7.625  10.981  18.624 1.00 22.26 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 6.949  9.953   17.871 1.00 23.20 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 8.295  12.045  17.742 1.00 20.62 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 6.815  9.454   21.149 1.00 28.09 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 5.955  8.456   21.747 1.00 31.19 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 4.990  9.088   22.723 1.00 35.67 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 4.767  10.302  22.698 1.00 36.31 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.421  8.260   23.567 1.00 39.70 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.504  8.701   24.613 1.00 44.65 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.096  8.180   24.427 1.00 48.79 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.624  8.096   23.294 1.00 50.18 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.401  7.901   25.536 1.00 50.41 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.012  7.452   25.557 1.00 51.16 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? -0.204 6.032   25.056 1.00 48.12 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -1.306 5.715   24.600 1.00 49.19 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.873 8.445   24.775 1.00 56.07 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.815 9.891   25.264 1.00 63.85 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.868 10.164  26.473 1.00 67.18 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -0.775 10.855  24.337 1.00 64.62 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 0.790  5.148   25.223 1.00 44.05 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 0.669  3.792   24.717 1.00 41.94 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.054  3.701   23.250 1.00 38.94 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 0.779  2.692   22.600 1.00 38.90 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 1.716  4.748   22.720 1.00 36.20 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.198  4.843   21.354 1.00 33.89 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.731  4.952   21.363 1.00 30.75 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.332  5.370   22.351 1.00 32.80 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.619  6.106   20.663 1.00 34.49 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.078  6.130   20.517 1.00 38.17 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.408 7.501   20.084 1.00 39.71 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.382 5.029   19.549 1.00 38.90 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.355  4.587   20.255 1.00 25.59 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.771  4.752   20.065 1.00 22.11 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 5.959  5.093   18.595 1.00 20.02 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.310  4.478   17.743 1.00 20.20 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.580  3.500   20.472 1.00 21.42 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.034  2.222   19.818 1.00 21.46 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.069  3.678   20.183 1.00 21.29 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 6.799  6.093   18.319 1.00 17.35 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.117  6.509   16.961 1.00 16.49 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.505  6.065   16.531 1.00 16.63 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.377  5.849   17.379 1.00 17.97 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.723  5.913   15.206 1.00 14.07 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.017 5.495   14.652 1.00 12.61 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.327 6.420   13.469 1.00 12.33 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.496  6.585   12.561 1.00 13.35 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 9.956  4.045   14.111 1.00 12.54 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.452  3.054   15.137 1.00 13.22 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.282 2.588   16.142 1.00 12.86 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.146  2.576   15.087 1.00 14.37 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.809  1.703   17.119 1.00 12.88 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.669  1.697   16.061 1.00 14.66 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.515  1.253   17.071 1.00 13.83 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.555 6.967   13.451 1.00 10.22 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 11.979 7.753   12.321 1.00 9.83  ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.445 6.726   11.231 1.00 10.39 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.382 5.943   11.461 1.00 9.55  ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.130 8.662   12.752 1.00 10.40 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.762 6.693   10.082 1.00 12.06 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.131 5.770   8.999  1.00 13.58 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.507 6.111   8.429  1.00 14.07 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 13.863 7.290   8.362  1.00 13.90 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.100 5.902   7.882  1.00 18.42 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.271 4.866   6.809  1.00 25.38 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.402 3.685   7.158  1.00 24.35 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.321 5.252   5.600  1.00 28.82 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.293 5.078   8.016  1.00 12.99 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.569 5.332   7.319  1.00 15.47 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.598 4.568   5.960  1.00 17.55 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.609 4.611   5.259  1.00 19.70 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.835 5.024   8.160  1.00 16.00 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 16.820 5.810   9.485  1.00 16.44 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 16.959 3.526   8.437  1.00 16.27 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.555 3.773   5.645  1.00 17.94 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.506 2.943   4.441  1.00 18.68 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.608 3.709   3.125  1.00 22.24 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.014 3.123   2.120  1.00 24.15 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.239 2.109   4.435  1.00 17.57 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.183 1.156   5.621  1.00 16.84 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.871 0.393   5.581  1.00 16.69 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.750 1.258   5.972  1.00 16.79 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.507  0.832   6.131  1.00 18.55 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.190  -0.421  5.853  1.00 19.21 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.560  1.667   6.553  1.00 19.43 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.258 4.999   3.118  1.00 23.06 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.371 5.794   1.883  1.00 24.16 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.801 6.370   1.687  1.00 25.35 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.107 6.885   0.599  1.00 26.36 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.354 6.941   1.877  1.00 26.15 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.558 7.946   3.000  1.00 26.81 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 13.816 7.512   4.147  1.00 25.18 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.430 9.172   2.739  1.00 25.76 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.677 6.296   2.705  1.00 24.33 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.034 6.876   2.600  1.00 24.82 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 18.943 5.890   1.916  1.00 28.12 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.765 5.217   2.553  1.00 27.74 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.593 7.273   3.976  1.00 22.68 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.676 8.160   4.828  1.00 22.42 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.294 8.406   6.189  1.00 22.12 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.362 9.463   4.115  1.00 22.99 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.758 5.783   0.601  1.00 30.73 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.464 4.811   -0.228 1.00 33.89 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 20.985 4.984   -0.203 1.00 35.69 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.702 3.983   -0.370 1.00 36.94 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 18.930 4.829   -1.673 1.00 34.70 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.411 4.802   -1.901 1.00 36.27 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.103 4.618   -3.395 1.00 38.46 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.724 3.677   -1.107 1.00 36.85 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.474 6.229   0.035  1.00 36.43 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 22.911 6.559   0.052  1.00 36.62 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.683 5.965   1.236  1.00 38.79 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 24.915 5.909   1.199  1.00 39.53 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.139 8.088   -0.028 1.00 34.98 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.370 8.873   1.005  1.00 31.99 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.126 9.418   0.868  1.00 31.64 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.823 9.236   2.316  1.00 31.29 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.765 10.072  2.027  1.00 31.68 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.809 10.015  2.912  1.00 31.38 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.017 9.032   3.022  1.00 31.72 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 21.927 10.535  4.199  1.00 31.52 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.138 9.572   4.293  1.00 31.64 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.113 10.340  4.854  1.00 31.57 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 22.972 5.482   2.271  1.00 38.79 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.618 4.859   3.422  1.00 39.46 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.428 3.627   3.023  1.00 45.16 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.419 3.316   3.678  1.00 45.51 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.559 4.464   4.466  1.00 36.46 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 21.859 5.634   5.162  1.00 34.07 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 20.785 5.113   6.127  1.00 32.86 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 22.855 6.504   5.938  1.00 33.60 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 23.985 2.916   1.964  1.00 49.48 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.585 1.692   1.437  1.00 54.48 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.775 1.882   0.566  1.00 59.36 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.525 0.922   0.375  1.00 60.95 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.561 0.969   0.579  1.00 57.13 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.520 0.284   1.387  1.00 61.99 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.862 -0.241  2.462  1.00 63.12 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.362 0.249   0.939  1.00 65.04 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.882 3.046   -0.086 1.00 61.63 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.972 3.322   -1.018 1.00 64.80 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.801 4.522   -0.583 1.00 66.98 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.732 4.905   -1.306 1.00 69.03 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.420 3.554   -2.435 1.00 67.86 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.356 4.640   -2.499 1.00 72.65 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.025 4.182   -3.067 1.00 78.40 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.294 5.030   -3.630 1.00 79.69 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.715 2.972   -2.953 1.00 79.35 ? 145 GLU   A OE2 1 
HETATM 1078 N  N1  . A1B3G B 2 .   ? 11.363 13.697  17.862 1.00 27.77 ? 201 A1B3G A N1  1 
HETATM 1079 C  C4  . A1B3G B 2 .   ? 6.779  10.235  26.026 1.00 35.60 ? 201 A1B3G A C4  1 
HETATM 1080 C  C5  . A1B3G B 2 .   ? 7.539  11.308  25.590 1.00 35.49 ? 201 A1B3G A C5  1 
HETATM 1081 C  C6  . A1B3G B 2 .   ? 8.581  11.131  24.682 1.00 34.48 ? 201 A1B3G A C6  1 
HETATM 1082 C  C7  . A1B3G B 2 .   ? 9.425  12.331  24.313 1.00 34.19 ? 201 A1B3G A C7  1 
HETATM 1083 C  C8  . A1B3G B 2 .   ? 9.155  12.785  22.893 1.00 33.25 ? 201 A1B3G A C8  1 
HETATM 1084 C  C10 . A1B3G B 2 .   ? 12.376 14.353  22.471 1.00 32.26 ? 201 A1B3G A C10 1 
HETATM 1085 C  C13 . A1B3G B 2 .   ? 10.989 14.516  18.833 1.00 29.40 ? 201 A1B3G A C13 1 
HETATM 1086 O  O1  . A1B3G B 2 .   ? 10.513 15.637  18.643 1.00 29.18 ? 201 A1B3G A O1  1 
HETATM 1087 C  C12 . A1B3G B 2 .   ? 11.163 14.026  20.279 1.00 31.16 ? 201 A1B3G A C12 1 
HETATM 1088 F  F   . A1B3G B 2 .   ? 11.522 12.690  20.309 1.00 31.95 ? 201 A1B3G A F   1 
HETATM 1089 C  C11 . A1B3G B 2 .   ? 12.256 14.786  21.009 1.00 31.81 ? 201 A1B3G A C11 1 
HETATM 1090 C  C9  . A1B3G B 2 .   ? 11.025 14.431  23.156 1.00 32.50 ? 201 A1B3G A C9  1 
HETATM 1091 C  C14 . A1B3G B 2 .   ? 9.812  14.209  21.017 1.00 32.13 ? 201 A1B3G A C14 1 
HETATM 1092 N  N   . A1B3G B 2 .   ? 9.982  13.729  22.391 1.00 32.79 ? 201 A1B3G A N   1 
HETATM 1093 O  O   . A1B3G B 2 .   ? 8.209  12.341  22.258 1.00 32.48 ? 201 A1B3G A O   1 
HETATM 1094 C  C1  . A1B3G B 2 .   ? 8.815  9.839   24.186 1.00 33.29 ? 201 A1B3G A C1  1 
HETATM 1095 S  S   . A1B3G B 2 .   ? 10.116 9.644   23.004 1.00 30.84 ? 201 A1B3G A S   1 
HETATM 1096 C  C   . A1B3G B 2 .   ? 10.183 7.871   22.723 1.00 30.06 ? 201 A1B3G A C   1 
HETATM 1097 C  C3  . A1B3G B 2 .   ? 7.034  8.974   25.559 1.00 34.93 ? 201 A1B3G A C3  1 
HETATM 1098 C  C2  . A1B3G B 2 .   ? 8.038  8.766   24.622 1.00 34.02 ? 201 A1B3G A C2  1 
HETATM 1099 ZN ZN  . ZN    C 3 .   ? 10.898 -5.299  5.571  1.00 24.56 2 202 ZN    A ZN  1 
HETATM 1100 S  S   . DMS   D 4 .   ? 19.813 -0.747  20.067 1.00 70.96 ? 203 DMS   A S   1 
HETATM 1101 O  O   . DMS   D 4 .   ? 18.373 -0.986  19.710 1.00 70.46 ? 203 DMS   A O   1 
HETATM 1102 C  C1  . DMS   D 4 .   ? 19.932 -0.043  21.739 1.00 70.90 ? 203 DMS   A C1  1 
HETATM 1103 C  C2  . DMS   D 4 .   ? 20.395 0.752   19.221 1.00 70.98 ? 203 DMS   A C2  1 
HETATM 1104 O  O   . HOH   E 5 .   ? 10.961 17.541  26.696 1.00 44.59 ? 301 HOH   A O   1 
HETATM 1105 O  O   . HOH   E 5 .   ? 23.827 -0.592  15.019 1.00 33.39 ? 302 HOH   A O   1 
HETATM 1106 O  O   . HOH   E 5 .   ? 20.041 22.008  7.893  1.00 26.39 ? 303 HOH   A O   1 
HETATM 1107 O  O   . HOH   E 5 .   ? 22.788 -2.086  4.083  1.00 38.28 ? 304 HOH   A O   1 
HETATM 1108 O  O   . HOH   E 5 .   ? 15.677 -11.705 5.449  1.00 44.90 ? 305 HOH   A O   1 
HETATM 1109 O  O   . HOH   E 5 .   ? 3.659  6.982   3.575  1.00 34.89 ? 306 HOH   A O   1 
HETATM 1110 O  O   . HOH   E 5 .   ? 23.631 21.271  8.024  1.00 27.91 ? 307 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 8.847  1.797   2.830  1.00 27.38 ? 308 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 6.693  -6.419  29.112 1.00 32.44 ? 309 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 7.832  -4.521  0.637  1.00 29.29 ? 310 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 13.855 10.724  0.646  1.00 31.97 ? 311 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 10.410 7.514   4.583  1.00 28.86 ? 312 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 18.150 18.591  5.725  1.00 36.17 ? 313 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 9.359  17.771  19.881 1.00 29.07 ? 314 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 20.075 8.378   18.942 1.00 23.10 ? 315 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 6.725  2.911   32.970 1.00 30.65 ? 316 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 4.064  5.225   24.994 1.00 43.19 ? 317 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 0.467  -1.004  16.446 1.00 24.59 ? 318 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 14.830 2.069   23.147 1.00 23.30 ? 319 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 17.693 20.560  9.633  1.00 24.22 ? 320 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 14.405 20.247  8.651  1.00 25.96 ? 321 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 11.125 10.983  11.439 1.00 16.05 ? 322 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 31.051 19.893  16.695 1.00 44.10 ? 323 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 10.050 4.199   3.405  1.00 21.94 ? 324 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 8.121  19.077  18.041 1.00 28.25 ? 325 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 11.057 16.563  5.487  1.00 47.23 ? 326 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 14.769 -5.083  17.003 1.00 26.07 ? 327 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 17.687 2.043   23.198 1.00 28.09 ? 328 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 10.828 -5.768  31.681 1.00 38.88 ? 329 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 5.454  -7.333  7.267  1.00 50.91 ? 330 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 21.632 -6.124  10.170 1.00 31.45 ? 331 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 16.664 -8.071  10.715 1.00 30.00 ? 332 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 12.979 9.758   9.397  1.00 12.10 ? 333 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 17.875 18.293  17.057 1.00 22.02 ? 334 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 5.329  -2.344  24.418 1.00 23.03 ? 335 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 17.636 -7.314  3.088  1.00 37.20 ? 336 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 22.691 17.717  19.595 1.00 43.29 ? 337 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 11.019 1.588   33.424 1.00 24.95 ? 338 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 28.482 -2.672  12.859 1.00 42.61 ? 339 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 9.013  20.435  10.608 1.00 30.60 ? 340 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 29.937 10.341  19.461 1.00 44.57 ? 341 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? 3.944  -5.764  6.312  1.00 32.51 ? 342 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 7.996  16.466  23.026 1.00 37.94 ? 343 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 14.515 11.819  24.128 1.00 27.71 ? 344 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 9.679  3.741   33.777 1.00 35.99 ? 345 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 6.660  11.952  5.411  1.00 27.87 ? 346 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 18.462 11.810  1.558  1.00 40.57 ? 347 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 30.216 4.498   3.830  1.00 55.87 ? 348 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 31.287 4.298   -2.604 1.00 50.03 ? 349 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 15.856 22.999  14.722 1.00 47.30 ? 350 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 14.063 13.806  3.525  1.00 30.78 ? 351 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 21.447 18.663  17.760 1.00 43.40 ? 352 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 2.669  -5.544  20.851 1.00 48.30 ? 353 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 30.220 20.158  10.326 1.00 61.13 ? 354 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 30.587 9.972   14.960 1.00 38.65 ? 355 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 5.040  6.912   28.505 1.00 43.01 ? 356 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 0.527  0.265   24.379 1.00 35.00 ? 357 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 5.464  1.112   7.276  1.00 32.41 ? 358 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 23.814 1.635   19.023 1.00 41.77 ? 359 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 8.662  -8.231  9.202  1.00 36.05 ? 360 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 19.424 23.076  15.585 1.00 22.79 ? 361 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 22.225 18.441  6.042  1.00 23.05 ? 362 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 12.200 -8.556  13.027 1.00 34.04 ? 363 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 6.055  22.092  11.074 1.00 42.08 ? 364 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 11.729 20.703  12.324 1.00 24.84 ? 365 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 35.230 8.686   7.333  1.00 45.49 ? 366 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 1.570  -3.313  17.643 1.00 25.56 ? 367 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 32.572 13.684  20.746 1.00 35.31 ? 368 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 16.144 -5.296  1.917  1.00 28.35 ? 369 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? -1.293 1.542   5.304  1.00 99.47 ? 370 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 1.617  12.611  5.487  1.00 44.98 ? 371 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? -1.743 -4.893  15.460 1.00 45.87 ? 372 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 7.258  25.182  14.120 1.00 42.10 ? 373 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 6.918  -5.877  2.818  1.00 38.29 ? 374 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 22.048 8.336   20.779 1.00 32.57 ? 375 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 11.947 13.105  1.044  1.00 53.47 ? 376 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 3.777  10.200  19.073 1.00 45.06 ? 377 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 16.793 -4.114  17.978 1.00 32.90 ? 378 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 6.336  -9.026  14.295 1.00 30.59 ? 379 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 29.279 2.074   20.095 1.00 60.76 ? 380 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 13.368 -6.588  32.620 1.00 39.96 ? 381 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 20.387 9.263   25.455 1.00 48.29 ? 382 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 2.345  2.060   27.506 1.00 34.94 ? 383 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 2.444  14.775  19.759 1.00 38.72 ? 384 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 15.095 -9.931  12.165 1.00 34.42 ? 385 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 20.812 21.268  17.792 1.00 34.60 ? 386 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 24.747 6.123   21.264 1.00 52.58 ? 387 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? -1.041 14.275  12.035 1.00 32.68 ? 388 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 14.238 13.299  26.197 1.00 40.98 ? 389 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 3.431  12.136  18.151 1.00 53.67 ? 390 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 4.646  -2.276  28.677 1.00 51.34 ? 391 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 4.945  14.058  21.398 1.00 40.18 ? 392 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 26.658 -2.550  15.236 1.00 29.69 ? 393 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 11.597 22.810  14.092 1.00 31.75 ? 394 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 19.593 -6.651  24.503 1.00 48.25 ? 395 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? 8.648  6.367   2.650  1.00 55.09 ? 396 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 0.842  -2.783  23.655 1.00 30.14 ? 397 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 9.388  -9.258  12.449 1.00 37.83 ? 398 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 9.289  24.321  12.669 1.00 44.95 ? 399 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 35.442 20.239  16.328 0.50 54.12 ? 400 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   ? 0.8103 0.2163 0.3998 -0.0689 -0.2524 0.0255  7   SER   A N   
2    C CA  . SER   A 1   ? 0.7528 0.2253 0.4698 -0.0700 -0.2860 0.0379  7   SER   A CA  
3    C C   . SER   A 1   ? 0.6595 0.2303 0.4953 -0.0556 -0.2640 0.0354  7   SER   A C   
4    O O   . SER   A 1   ? 0.6714 0.2493 0.4873 -0.0511 -0.2434 0.0285  7   SER   A O   
5    C CB  . SER   A 1   ? 0.8156 0.2144 0.5230 -0.1001 -0.3647 0.0625  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.8910 0.2475 0.5617 -0.1136 -0.3873 0.0689  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.5689 0.2048 0.5220 -0.0498 -0.2654 0.0414  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4871 0.1995 0.5469 -0.0391 -0.2383 0.0393  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.4170 0.1920 0.5526 -0.0259 -0.2018 0.0326  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.4294 0.2090 0.5230 -0.0186 -0.1815 0.0224  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3403 0.1565 0.5854 -0.0236 -0.1890 0.0389  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2890 0.1482 0.6014 -0.0143 -0.1486 0.0331  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2514 0.1445 0.6176 -0.0094 -0.1016 0.0257  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2422 0.1325 0.6266 -0.0129 -0.1084 0.0307  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2668 0.1182 0.6732 -0.0199 -0.1778 0.0545  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2337 0.1484 0.6158 -0.0039 -0.0537 0.0141  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2208 0.1460 0.6416 -0.0037 -0.0022 0.0070  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2313 0.1529 0.7660 -0.0026 0.0185  0.0198  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2305 0.1518 0.7753 -0.0003 0.0211  0.0204  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2271 0.1571 0.5670 -0.0045 0.0374  -0.0131 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2340 0.1709 0.4814 -0.0042 0.0194  -0.0204 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2317 0.1490 0.5898 -0.0102 0.0904  -0.0204 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2506 0.1925 0.4362 -0.0070 0.0387  -0.0301 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2400 0.1580 0.8669 -0.0036 0.0377  0.0313  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2408 0.1521 0.9994 -0.0013 0.0670  0.0483  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2744 0.1652 1.0355 -0.0014 0.1500  0.0336  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.2724 0.1574 1.0472 -0.0036 0.1692  0.0331  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2077 0.1216 1.0890 -0.0045 0.0254  0.0801  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2211 0.1318 1.0936 -0.0113 -0.0591 0.0986  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2182 0.1255 1.1559 -0.0122 -0.0825 0.1165  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.2601 0.1602 1.0445 -0.0189 -0.1127 0.0971  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2481 0.1371 1.1527 -0.0227 -0.1609 0.1319  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2926 0.1667 1.0388 -0.0296 -0.1854 0.1118  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2921 0.1584 1.0985 -0.0330 -0.2122 0.1302  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3419 0.1681 1.0989 -0.0482 -0.2865 0.1459  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3083 0.1787 1.0369 -0.0017 0.1985  0.0201  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3511 0.1761 1.0507 -0.0076 0.2812  0.0044  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3583 0.1526 1.1370 -0.0043 0.3367  0.0110  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3715 0.1715 1.1270 -0.0025 0.3235  0.0084  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4200 0.2266 0.9528 -0.0193 0.2901  -0.0223 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4337 0.2596 0.8993 -0.0187 0.2530  -0.0280 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.4718 0.2081 0.9538 -0.0323 0.3720  -0.0371 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3414 0.1023 1.2265 -0.0022 0.4017  0.0221  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3477 0.0745 1.3309 0.0029  0.4637  0.0327  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3106 0.0862 1.4164 0.0131  0.4024  0.0607  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2863 0.1071 1.4519 0.0151  0.3270  0.0813  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3143 0.0771 1.4279 0.0161  0.4223  0.0595  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.2639 0.0682 1.4812 0.0232  0.3593  0.0859  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.2478 0.0863 1.3354 0.0200  0.2799  0.0717  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.2222 0.0762 1.3436 0.0234  0.2463  0.0825  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3052 0.0797 1.6184 0.0297  0.4222  0.0960  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.3648 0.0988 1.8276 0.0348  0.5099  0.1149  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.3409 0.0916 1.9169 0.0366  0.4961  0.1390  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4376 0.1111 1.9074 0.0368  0.6061  0.1061  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.2481 0.0967 1.2012 0.0138  0.2510  0.0511  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.2498 0.1234 1.0802 0.0116  0.1893  0.0378  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.2167 0.1153 1.0185 0.0093  0.1177  0.0448  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1972 0.0949 1.0031 0.0068  0.1214  0.0454  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.2969 0.1503 0.9742 0.0044  0.2248  0.0067  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3321 0.1463 0.9943 0.0015  0.2878  -0.0035 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.3295 0.1528 1.0348 0.0077  0.2776  0.0041  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.3911 0.1497 0.9739 -0.0105 0.3543  -0.0220 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.3701 0.1514 1.0560 0.0044  0.3376  -0.0056 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4430 0.1476 0.9895 -0.0175 0.4131  -0.0321 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4418 0.1598 1.0448 -0.0088 0.4068  -0.0239 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5101 0.1691 1.0729 -0.0162 0.4675  -0.0342 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2043 0.1166 0.9550 0.0089  0.0578  0.0467  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1921 0.1096 0.8801 0.0046  -0.0040 0.0492  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1920 0.1133 0.7439 0.0058  -0.0090 0.0271  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1977 0.1200 0.7352 0.0082  -0.0131 0.0252  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1857 0.0947 0.9463 -0.0011 -0.0728 0.0790  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2607 0.1508 0.9202 -0.0094 -0.1370 0.0794  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2931 0.1564 1.0183 -0.0224 -0.2087 0.1125  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3738 0.2001 0.9839 -0.0313 -0.2588 0.1098  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4409 0.2224 0.9606 -0.0448 -0.3066 0.1133  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4112 0.1883 0.9464 -0.0504 -0.3165 0.1199  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4742 0.2064 0.8805 -0.0539 -0.3406 0.1098  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1838 0.1083 0.6476 0.0044  -0.0051 0.0126  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2009 0.1304 0.5548 0.0056  -0.0079 -0.0025 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2060 0.1226 0.5093 0.0048  -0.0554 0.0031  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2101 0.1186 0.5166 0.0016  -0.0704 0.0079  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2061 0.1410 0.5017 0.0021  0.0289  -0.0176 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2242 0.1673 0.4356 0.0023  0.0257  -0.0256 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1916 0.1129 0.5217 -0.0029 0.0814  -0.0231 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2065 0.1122 0.4554 0.0065  -0.0745 0.0020  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2365 0.1069 0.4175 0.0032  -0.1108 0.0062  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2351 0.1027 0.3354 0.0091  -0.0948 -0.0039 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2096 0.1027 0.3196 0.0137  -0.0721 -0.0093 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2629 0.0953 0.4680 -0.0059 -0.1610 0.0237  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2549 0.0811 0.5458 -0.0148 -0.1897 0.0425  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2527 0.0965 0.4913 -0.0024 -0.1569 0.0252  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2703 0.0977 0.2926 0.0079  -0.1061 -0.0038 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2952 0.1110 0.2561 0.0144  -0.0862 -0.0087 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3237 0.1206 0.2860 0.0123  -0.1041 -0.0050 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3532 0.1092 0.3155 0.0017  -0.1438 0.0042  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3515 0.1067 0.2261 0.0125  -0.0866 -0.0081 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3608 0.1281 0.2301 0.0149  -0.0702 -0.0104 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.4067 0.1631 0.2856 0.0076  -0.0918 -0.0079 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3268 0.1161 0.1886 0.0241  -0.0348 -0.0119 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2927 0.1182 0.2621 0.0199  -0.0805 -0.0092 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2881 0.1021 0.2621 0.0193  -0.0931 -0.0067 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3761 0.1123 0.2699 0.0120  -0.1164 -0.0025 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.4022 0.1091 0.3031 0.0029  -0.1519 0.0051  20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2560 0.1116 0.2440 0.0278  -0.0622 -0.0113 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2652 0.1213 0.2742 0.0281  -0.0722 -0.0098 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2575 0.1407 0.2588 0.0352  -0.0437 -0.0122 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2496 0.1403 0.2700 0.0368  -0.0469 -0.0120 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3258 0.1805 0.3090 0.0382  -0.0552 -0.0100 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3657 0.1615 0.2813 0.0359  -0.0605 -0.0084 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3172 0.1854 0.3216 0.0404  -0.0552 -0.0099 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.4308 0.1232 0.2467 0.0134  -0.0967 -0.0054 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.5281 0.1203 0.2398 0.0027  -0.1096 -0.0032 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.6088 0.1375 0.2880 -0.0180 -0.1640 0.0058  21  HIS   A C   
114  O O   . HIS   A 15  ? 0.6878 0.1216 0.2780 -0.0350 -0.1917 0.0110  21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.5698 0.1212 0.2099 0.0103  -0.0612 -0.0076 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.5808 0.1208 0.2018 0.0097  -0.0512 -0.0085 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.5407 0.1648 0.2391 0.0205  -0.0336 -0.0094 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.6392 0.0846 0.1627 -0.0021 -0.0547 -0.0083 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.5697 0.1586 0.2280 0.0174  -0.0281 -0.0097 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.6301 0.1111 0.1823 0.0042  -0.0388 -0.0094 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.5861 0.1606 0.3387 -0.0198 -0.1834 0.0103  22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.6207 0.1442 0.3675 -0.0407 -0.2407 0.0247  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.5795 0.1448 0.4435 -0.0462 -0.2810 0.0403  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.5915 0.1279 0.4850 -0.0635 -0.3319 0.0586  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.6228 0.1555 0.3685 -0.0397 -0.2312 0.0222  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.7057 0.1777 0.3357 -0.0377 -0.1952 0.0118  22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.7009 0.1840 0.3369 -0.0373 -0.1899 0.0106  22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.7999 0.1388 0.2920 -0.0595 -0.2201 0.0163  22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.5293 0.1625 0.4704 -0.0318 -0.2560 0.0358  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.4915 0.1644 0.5556 -0.0336 -0.2791 0.0507  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.5511 0.1563 0.6068 -0.0556 -0.3468 0.0737  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.6054 0.1417 0.5523 -0.0653 -0.3618 0.0712  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.4409 0.1801 0.5609 -0.0161 -0.2342 0.0393  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.5423 0.1597 0.7136 -0.0655 -0.3875 0.0987  24  THR   A N   
135  C CA  . THR   A 18  ? 0.5980 0.1539 0.7905 -0.0912 -0.4654 0.1302  24  THR   A CA  
136  C C   . THR   A 18  ? 0.5807 0.1681 0.8606 -0.0854 -0.4676 0.1395  24  THR   A C   
137  O O   . THR   A 18  ? 0.5179 0.1749 0.8450 -0.0616 -0.4060 0.1209  24  THR   A O   
138  C CB  . THR   A 18  ? 0.5971 0.1536 0.8959 -0.1056 -0.5113 0.1601  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.5412 0.1832 1.0127 -0.0876 -0.4755 0.1673  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.6317 0.1669 0.8585 -0.1091 -0.5049 0.1505  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.6315 0.1633 0.9388 -0.1101 -0.5433 0.1719  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.6275 0.1879 1.0318 -0.1057 -0.5498 0.1851  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.5304 0.1804 1.1251 -0.0860 -0.5087 0.1942  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4808 0.1814 1.1323 -0.0669 -0.4605 0.1832  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.7106 0.1901 1.1213 -0.1405 -0.6485 0.2251  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.9047 0.2749 1.1158 -0.1634 -0.6842 0.2165  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.9780 0.3393 1.1098 -0.1538 -0.6538 0.1954  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 1.0205 0.2761 1.0989 -0.1980 -0.7471 0.2290  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 1.0913 0.3324 1.0445 -0.1809 -0.6912 0.1940  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 1.1307 0.2986 1.0374 -0.2094 -0.7479 0.2132  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4990 0.1599 1.1863 -0.0918 -0.5236 0.2143  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.4252 0.1555 1.2887 -0.0746 -0.4749 0.2237  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3787 0.1652 1.2072 -0.0467 -0.3771 0.1823  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3445 0.1724 1.2703 -0.0311 -0.3239 0.1801  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4567 0.1794 1.3992 -0.0868 -0.5066 0.2498  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4728 0.2411 1.6370 -0.0786 -0.4836 0.2805  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4717 0.2443 1.7574 -0.0813 -0.5038 0.3094  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4686 0.2684 1.6944 -0.0679 -0.4353 0.2758  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3904 0.1704 1.0780 -0.0427 -0.3540 0.1517  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3516 0.1753 0.9878 -0.0221 -0.2741 0.1156  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3218 0.1641 0.9435 -0.0112 -0.2426 0.1017  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2869 0.1650 0.9569 0.0017  -0.1829 0.0901  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3908 0.1956 0.8792 -0.0229 -0.2696 0.0926  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.4003 0.2001 0.9030 -0.0286 -0.2788 0.0987  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3467 0.1766 0.9654 -0.0246 -0.2571 0.1089  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4544 0.2139 0.8515 -0.0376 -0.3043 0.0939  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3393 0.1476 0.8900 -0.0188 -0.2827 0.1041  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3356 0.1588 0.8678 -0.0095 -0.2588 0.0923  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3174 0.1612 0.9955 -0.0065 -0.2563 0.1130  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3056 0.1777 1.0001 0.0060  -0.2089 0.0996  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3637 0.1330 0.7751 -0.0201 -0.3015 0.0906  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3693 0.1326 0.6494 -0.0131 -0.2681 0.0638  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.4116 0.1291 0.5917 -0.0213 -0.2820 0.0594  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3415 0.1455 0.5904 0.0029  -0.2126 0.0414  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.4335 0.1634 0.5329 -0.0091 -0.2351 0.0371  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3853 0.1701 0.5285 0.0047  -0.1968 0.0276  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3103 0.1594 0.6112 0.0141  -0.1756 0.0342  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3811 0.1957 0.4849 0.0167  -0.1518 0.0114  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3160 0.1883 0.5596 0.0233  -0.1355 0.0160  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3471 0.2065 0.5025 0.0245  -0.1258 0.0068  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3115 0.1373 1.0981 -0.0193 -0.3073 0.1481  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.2910 0.1343 1.2460 -0.0168 -0.3059 0.1761  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.2660 0.1489 1.3296 -0.0004 -0.2245 0.1706  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.2476 0.1443 1.4422 0.0071  -0.1939 0.1862  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2755 0.0847 1.3275 -0.0390 -0.3911 0.2226  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.2569 0.1474 1.2719 0.0029  -0.1913 0.1526  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2173 0.1267 1.2974 0.0142  -0.1122 0.1433  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2116 0.1285 1.1456 0.0210  -0.0578 0.1016  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2010 0.1191 1.1246 0.0227  -0.0155 0.0902  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2326 0.1379 1.3971 0.0076  -0.1304 0.1658  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.2560 0.1564 1.6048 0.0005  -0.1728 0.2142  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2458 0.1547 1.7214 0.0094  -0.1310 0.2282  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.2556 0.1365 1.6283 -0.0176 -0.2562 0.2437  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2109 0.1297 1.0370 0.0227  -0.0636 0.0825  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2168 0.1424 0.9129 0.0258  -0.0268 0.0505  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2080 0.1307 0.9130 0.0292  0.0504  0.0354  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.2075 0.1233 0.9770 0.0331  0.0833  0.0398  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2293 0.1566 0.8413 0.0270  -0.0487 0.0410  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2568 0.1931 0.7528 0.0287  -0.0190 0.0157  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.2881 0.2237 0.7103 0.0255  -0.0296 0.0083  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2515 0.1903 0.6940 0.0313  -0.0355 0.0113  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1992 0.1174 0.8296 0.0255  0.0797  0.0179  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2159 0.1109 0.8067 0.0213  0.1475  0.0007  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.2363 0.1341 0.6953 0.0153  0.1435  -0.0180 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.2788 0.1586 0.7033 0.0111  0.1737  -0.0267 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.2433 0.1203 0.8416 0.0165  0.1810  -0.0023 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.2957 0.1297 0.8096 0.0053  0.2440  -0.0221 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2161 0.0875 0.9647 0.0221  0.1959  0.0201  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2075 0.1249 0.6011 0.0143  0.1049  -0.0209 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2081 0.1326 0.5022 0.0090  0.0971  -0.0310 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1831 0.1289 0.4437 0.0140  0.0519  -0.0268 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1790 0.1247 0.4625 0.0160  0.0342  -0.0214 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.2299 0.1275 0.4624 -0.0059 0.1336  -0.0414 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.2515 0.1570 0.3973 -0.0153 0.1159  -0.0440 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2856 0.1843 0.3776 -0.0253 0.1151  -0.0448 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.2429 0.1634 0.3581 -0.0168 0.0953  -0.0416 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2955 0.2084 0.3389 -0.0323 0.0913  -0.0393 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.2728 0.1995 0.3300 -0.0261 0.0813  -0.0379 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2230 0.1540 0.3623 -0.0102 0.0834  -0.0394 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2684 0.2084 0.2970 -0.0299 0.0636  -0.0316 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.2361 0.1781 0.3337 -0.0135 0.0683  -0.0372 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.2490 0.1970 0.2972 -0.0221 0.0594  -0.0326 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1715 0.1284 0.3803 0.0152  0.0374  -0.0280 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1684 0.1318 0.3382 0.0199  0.0096  -0.0245 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1769 0.1524 0.2957 0.0172  0.0157  -0.0248 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1687 0.1472 0.2819 0.0123  0.0272  -0.0260 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1819 0.1324 0.3651 0.0264  -0.0228 -0.0174 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1878 0.1392 0.3895 0.0295  -0.0257 -0.0158 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2312 0.1906 0.3840 0.0324  -0.0208 -0.0182 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2674 0.2350 0.4344 0.0331  -0.0120 -0.0194 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2475 0.2034 0.3544 0.0343  -0.0226 -0.0171 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1738 0.1532 0.2620 0.0189  0.0086  -0.0209 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1730 0.1658 0.2369 0.0164  0.0122  -0.0138 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1819 0.1680 0.2291 0.0266  0.0075  -0.0075 35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1874 0.1691 0.2248 0.0268  0.0082  -0.0061 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2004 0.1971 0.2497 0.0008  0.0199  -0.0112 35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2393 0.2488 0.2794 -0.0071 0.0142  0.0038  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2111 0.2319 0.2640 0.0041  0.0119  0.0136  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2894 0.2895 0.3087 -0.0269 0.0123  0.0081  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1860 0.1641 0.2256 0.0346  0.0079  -0.0037 36  SER   A N   
241  C CA  A SER   A 30  ? 0.2080 0.1608 0.2208 0.0435  0.0156  0.0018  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2102 0.1625 0.2225 0.0435  0.0155  0.0017  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2014 0.1705 0.2258 0.0436  0.0312  0.0145  36  SER   A C   
244  O O   . SER   A 30  ? 0.2248 0.1700 0.2299 0.0490  0.0421  0.0170  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2354 0.1742 0.2395 0.0499  0.0216  0.0046  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2465 0.1804 0.2461 0.0503  0.0213  0.0040  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.2874 0.1767 0.2477 0.0568  0.0351  0.0065  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2579 0.2272 0.2908 0.0491  0.0300  0.0136  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1638 0.1678 0.2203 0.0350  0.0298  0.0256  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1705 0.1906 0.2539 0.0320  0.0362  0.0449  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1627 0.1819 0.2364 0.0268  0.0320  0.0416  37  SER   A C   
252  O O   . SER   A 31  ? 0.1725 0.1971 0.2682 0.0283  0.0401  0.0573  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1870 0.2345 0.3032 0.0176  0.0234  0.0629  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2598 0.3076 0.3528 -0.0013 0.0062  0.0548  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1532 0.1654 0.2038 0.0213  0.0222  0.0239  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1488 0.1578 0.1898 0.0167  0.0199  0.0190  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1822 0.1643 0.2016 0.0273  0.0212  0.0079  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1953 0.1738 0.2086 0.0251  0.0197  0.0049  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1511 0.1614 0.1847 0.0009  0.0138  0.0096  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1478 0.1647 0.1785 -0.0180 0.0065  0.0220  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1867 0.1805 0.1869 -0.0368 0.0101  0.0107  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1925 0.1751 0.1790 -0.0425 0.0147  0.0049  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2426 0.1941 0.1902 -0.0649 0.0199  0.0012  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.2751 0.1965 0.1847 -0.0859 0.0196  0.0031  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.2597 0.2006 0.1968 -0.0686 0.0265  -0.0041 38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1937 0.1496 0.1953 0.0355  0.0198  0.0030  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2093 0.1234 0.1779 0.0383  0.0091  -0.0045 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1957 0.1189 0.1876 0.0309  -0.0086 -0.0120 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2033 0.1043 0.1821 0.0292  -0.0194 -0.0135 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2445 0.1269 0.1785 0.0427  0.0225  -0.0008 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3260 0.1482 0.2070 0.0395  0.0054  -0.0067 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3415 0.1314 0.2005 0.0361  -0.0129 -0.0090 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3706 0.1745 0.2314 0.0378  0.0054  -0.0073 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1659 0.1155 0.1936 0.0258  -0.0072 -0.0151 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1542 0.1054 0.2169 0.0203  -0.0118 -0.0200 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1746 0.1209 0.2751 0.0206  -0.0197 -0.0202 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1942 0.1470 0.2934 0.0222  -0.0149 -0.0205 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1432 0.1119 0.2149 0.0110  0.0086  -0.0234 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1627 0.1369 0.2124 0.0069  0.0129  -0.0213 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1551 0.1292 0.1969 -0.0086 0.0295  -0.0241 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1787 0.1409 0.2347 0.0107  0.0032  -0.0227 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1668 0.1034 0.3119 0.0185  -0.0310 -0.0175 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1704 0.1040 0.3758 0.0184  -0.0372 -0.0126 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1654 0.1004 0.4385 0.0151  -0.0254 -0.0091 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1764 0.1055 0.4497 0.0129  -0.0364 -0.0062 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1912 0.0956 0.3892 0.0180  -0.0793 -0.0024 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2009 0.1013 0.4736 0.0165  -0.0953 0.0086  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2322 0.1053 0.4668 0.0149  -0.1264 0.0137  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1966 0.0874 0.5512 0.0104  -0.1179 0.0249  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1576 0.0956 0.4884 0.0148  0.0035  -0.0093 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1658 0.0975 0.5782 0.0131  0.0277  -0.0036 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1751 0.1026 0.6903 0.0161  0.0173  0.0134  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1715 0.0998 0.6908 0.0187  0.0268  0.0115  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1831 0.1031 0.5723 0.0075  0.0861  -0.0174 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1812 0.0834 0.6584 0.0067  0.1234  -0.0109 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2156 0.1389 0.5099 0.0012  0.0860  -0.0286 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1903 0.1132 0.7948 0.0145  -0.0051 0.0330  43  SER   A N   
298  C CA  . SER   A 37  ? 0.1942 0.1134 0.9247 0.0154  -0.0181 0.0573  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2085 0.1236 1.0622 0.0170  0.0257  0.0702  43  SER   A C   
300  O O   . SER   A 37  ? 0.1859 0.0986 1.0270 0.0153  0.0468  0.0640  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2093 0.1166 0.9543 0.0076  -0.0975 0.0799  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2485 0.1458 0.9879 0.0002  -0.1288 0.0885  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2253 0.1369 1.2071 0.0208  0.0431  0.0901  44  SER   A N   
304  C CA  . SER   A 38  ? 0.2478 0.1490 1.3654 0.0241  0.0965  0.1060  44  SER   A CA  
305  C C   . SER   A 38  ? 0.2692 0.1772 1.5156 0.0189  0.0421  0.1433  44  SER   A C   
306  O O   . SER   A 38  ? 0.2717 0.1831 1.5324 0.0108  -0.0393 0.1645  44  SER   A O   
307  C CB  . SER   A 38  ? 0.2381 0.1263 1.4472 0.0312  0.1518  0.1131  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2710 0.1736 1.5404 0.0306  0.0897  0.1361  44  SER   A OG  
309  N N   . THR   A 39  ? 0.2875 0.1891 1.6181 0.0205  0.0849  0.1521  45  THR   A N   
310  C CA  . THR   A 39  ? 0.2998 0.2073 1.7658 0.0141  0.0365  0.1909  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3139 0.2138 1.9890 0.0215  0.0983  0.2219  45  THR   A C   
312  O O   . THR   A 39  ? 0.3257 0.2059 2.0103 0.0315  0.1906  0.2056  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3253 0.2337 1.7087 0.0092  0.0271  0.1768  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3321 0.2274 1.7263 0.0166  0.1214  0.1596  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.3847 0.2956 1.5690 0.0049  -0.0111 0.1448  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3133 0.2209 2.1550 0.0149  0.0488  0.2687  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2917 0.1943 2.3662 0.0217  0.1020  0.3082  46  THR   A CA  
318  C C   . THR   A 40  ? 0.3094 0.2040 2.4276 0.0241  0.1551  0.3079  46  THR   A C   
319  O O   . THR   A 40  ? 0.2944 0.1741 2.5822 0.0332  0.2339  0.3303  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2749 0.1904 2.5239 0.0090  0.0023  0.3688  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3279 0.2459 2.5222 -0.0089 -0.0916 0.3800  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2846 0.2019 2.5033 0.0046  -0.0521 0.3738  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3354 0.2375 2.3206 0.0155  0.1086  0.2888  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3201 0.2162 2.3265 0.0166  0.1500  0.2858  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.3771 0.2532 2.1831 0.0216  0.2241  0.2283  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4340 0.3111 2.0700 0.0204  0.2092  0.1946  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3209 0.2334 2.3193 0.0013  0.0449  0.3069  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3634 0.2160 2.1953 0.0255  0.3042  0.2204  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4203 0.2399 2.0733 0.0251  0.3758  0.1719  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.4287 0.2695 1.9364 0.0171  0.3168  0.1513  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.4059 0.2627 1.9849 0.0144  0.2842  0.1715  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4419 0.2104 2.1867 0.0301  0.4940  0.1748  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5849 0.3063 2.1568 0.0234  0.5603  0.1325  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.7437 0.4027 2.1683 0.0185  0.6345  0.0966  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.7691 0.4217 2.2159 0.0225  0.6443  0.0996  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.8270 0.4321 2.0939 0.0069  0.6854  0.0635  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.4531 0.2898 1.7661 0.0133  0.3109  0.1129  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.4694 0.3219 1.6348 0.0069  0.2662  0.0909  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.4657 0.2842 1.5471 0.0025  0.3346  0.0655  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.4976 0.2668 1.5301 -0.0004 0.4141  0.0470  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.4316 0.2671 1.4797 -0.0007 0.3020  0.0639  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.4415 0.2442 1.4189 -0.0065 0.3597  0.0436  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4455 0.2569 1.2487 -0.0142 0.3271  0.0169  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.4725 0.2604 1.2174 -0.0211 0.3595  0.0036  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.4359 0.2431 1.5469 -0.0037 0.3703  0.0670  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.4897 0.2744 1.8294 0.0049  0.4353  0.1025  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4100 0.2498 1.1326 -0.0137 0.2685  0.0103  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4276 0.2746 1.0036 -0.0202 0.2439  -0.0103 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4459 0.2448 0.9199 -0.0325 0.3012  -0.0317 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.4698 0.2407 0.9439 -0.0345 0.3347  -0.0349 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4517 0.3323 0.9743 -0.0163 0.1783  -0.0100 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.4723 0.3802 1.0379 -0.0115 0.1124  0.0073  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.4878 0.3986 1.0860 -0.0126 0.1049  0.0143  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.4799 0.3978 1.0380 -0.0089 0.0681  0.0142  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.4526 0.2347 0.8358 -0.0433 0.3094  -0.0446 52  THR   A N   
356  C CA  . THR   A 46  ? 0.4992 0.2226 0.7618 -0.0627 0.3497  -0.0622 52  THR   A CA  
357  C C   . THR   A 46  ? 0.4806 0.2307 0.6495 -0.0675 0.2968  -0.0665 52  THR   A C   
358  O O   . THR   A 46  ? 0.4678 0.2692 0.6376 -0.0590 0.2441  -0.0611 52  THR   A O   
359  C CB  . THR   A 46  ? 0.5678 0.2514 0.7858 -0.0754 0.3832  -0.0699 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.6094 0.2397 0.8969 -0.0754 0.4582  -0.0683 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6278 0.2584 0.6905 -0.1015 0.3882  -0.0840 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.4774 0.1888 0.5715 -0.0813 0.3127  -0.0739 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4616 0.1950 0.4776 -0.0881 0.2651  -0.0735 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.5044 0.1868 0.4059 -0.1155 0.2704  -0.0791 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.5664 0.1655 0.4059 -0.1370 0.3214  -0.0882 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4541 0.1811 0.4596 -0.0886 0.2648  -0.0737 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4099 0.1725 0.5314 -0.0654 0.2647  -0.0664 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4514 0.2103 0.3977 -0.0932 0.2119  -0.0683 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3776 0.2088 0.5560 -0.0461 0.2067  -0.0556 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4753 0.1971 0.3465 -0.1170 0.2202  -0.0719 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.5107 0.1927 0.2835 -0.1449 0.2073  -0.0698 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.5672 0.2013 0.2571 -0.1700 0.1993  -0.0668 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.5439 0.2144 0.2630 -0.1590 0.1786  -0.0614 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4514 0.1970 0.2432 -0.1354 0.1559  -0.0574 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.6454 0.1907 0.2244 -0.2067 0.2125  -0.0690 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.7336 0.2123 0.2121 -0.2400 0.1988  -0.0635 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.8061 0.2570 0.2067 -0.2723 0.1515  -0.0476 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.9094 0.2641 0.2071 -0.3055 0.1717  -0.0529 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.8220 0.1879 0.2239 -0.2606 0.2671  -0.0808 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.7927 0.1827 0.2887 -0.2297 0.3171  -0.0919 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.7544 0.2185 0.3144 -0.2092 0.2810  -0.0839 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.7060 0.1903 0.3622 -0.1816 0.3245  -0.0914 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.6428 0.2018 0.3836 -0.1558 0.2988  -0.0856 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5700 0.1846 0.3055 -0.1532 0.2393  -0.0744 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.6158 0.1870 0.4488 -0.1342 0.3345  -0.0885 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.7484 0.2824 0.2076 -0.2608 0.0920  -0.0266 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.7577 0.2837 0.1809 -0.2852 0.0443  -0.0058 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.7125 0.3093 0.1980 -0.2797 -0.0168 0.0240  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.6677 0.3146 0.2127 -0.2571 -0.0180 0.0252  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.7134 0.2836 0.1923 -0.2618 0.0599  -0.0139 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.5892 0.2875 0.2167 -0.2055 0.0552  -0.0141 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.7078 0.3110 0.1927 -0.2983 -0.0645 0.0503  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.6626 0.3383 0.2359 -0.2879 -0.1127 0.0826  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.5978 0.3405 0.2534 -0.2631 -0.1190 0.0918  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.5828 0.3574 0.2940 -0.2687 -0.1610 0.1258  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.7465 0.3726 0.2725 -0.3340 -0.1727 0.1182  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.8977 0.4682 0.3669 -0.3768 -0.2182 0.1431  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.9209 0.4781 0.3652 -0.3738 -0.1956 0.1273  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.9918 0.5298 0.4442 -0.4154 -0.2806 0.1813  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.5566 0.3182 0.2270 -0.2363 -0.0766 0.0641  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.4815 0.3009 0.2220 -0.2108 -0.0763 0.0684  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4123 0.3035 0.2519 -0.1820 -0.0891 0.0882  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4007 0.3115 0.2645 -0.1650 -0.0776 0.0821  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.4623 0.2927 0.2121 -0.1841 -0.0302 0.0363  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.5388 0.2936 0.2013 -0.2100 -0.0030 0.0168  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.3597 0.2833 0.2553 -0.1764 -0.1069 0.1111  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2982 0.2784 0.2889 -0.1465 -0.1032 0.1289  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2437 0.2509 0.2668 -0.1179 -0.0767 0.1176  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2118 0.2496 0.3057 -0.0996 -0.0719 0.1377  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3049 0.2968 0.3570 -0.1643 -0.1441 0.1757  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3639 0.3471 0.4198 -0.1796 -0.1665 0.1924  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3790 0.3810 0.5249 -0.1944 -0.2080 0.2456  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.4229 0.3882 0.5423 -0.2367 -0.2606 0.2737  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3328 0.3836 0.5879 -0.1620 -0.1847 0.2636  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2484 0.2377 0.2217 -0.1164 -0.0580 0.0886  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2224 0.2291 0.2136 -0.0921 -0.0353 0.0747  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2110 0.2042 0.1687 -0.0819 -0.0107 0.0417  60  THR   A C   
418  O O   . THR   A 54  ? 0.2391 0.2017 0.1529 -0.0988 -0.0059 0.0285  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2645 0.2669 0.2525 -0.1047 -0.0467 0.0843  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.3355 0.2966 0.2531 -0.1294 -0.0472 0.0679  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2473 0.2601 0.2815 -0.1202 -0.0788 0.1240  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.1704 0.1782 0.1500 -0.0564 0.0053  0.0312  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.1647 0.1623 0.1331 -0.0470 0.0200  0.0079  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.1642 0.1664 0.1473 -0.0250 0.0259  0.0033  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.1837 0.1922 0.1770 -0.0170 0.0275  0.0143  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.1527 0.1441 0.1359 -0.0179 0.0285  -0.0103 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.1558 0.1334 0.1360 -0.0042 0.0254  -0.0139 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.1693 0.1312 0.1471 0.0015  0.0185  -0.0174 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.1650 0.1297 0.1614 -0.0040 0.0167  -0.0229 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.1683 0.1413 0.1586 -0.0077 0.0233  -0.0221 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.1931 0.1403 0.1733 0.0005  0.0097  -0.0228 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.1697 0.1539 0.1560 -0.0134 0.0296  -0.0190 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.1839 0.1200 0.1355 0.0110  0.0170  -0.0140 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.1931 0.1031 0.1311 0.0131  0.0054  -0.0163 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2474 0.1085 0.1505 0.0121  -0.0130 -0.0173 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2706 0.1100 0.1445 0.0139  -0.0079 -0.0162 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2071 0.1105 0.1295 0.0199  0.0191  -0.0102 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2629 0.1249 0.1441 0.0287  0.0372  -0.0046 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2663 0.1402 0.1612 0.0338  0.0585  0.0043  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.3222 0.1232 0.1480 0.0304  0.0368  -0.0067 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3162 0.1451 0.1811 0.0435  0.0880  0.0113  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3804 0.1246 0.1555 0.0372  0.0660  -0.0024 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3731 0.1321 0.1723 0.0452  0.0958  0.0063  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.4363 0.1333 0.1939 0.0534  0.1358  0.0120  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2811 0.1175 0.1828 0.0071  -0.0369 -0.0169 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.3543 0.1287 0.2124 -0.0009 -0.0669 -0.0130 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.4114 0.1214 0.1877 0.0000  -0.0610 -0.0123 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.3874 0.1013 0.1656 0.0029  -0.0559 -0.0126 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.3616 0.1359 0.2718 -0.0113 -0.1040 -0.0063 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.4395 0.1414 0.3025 -0.0260 -0.1476 0.0037  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4858 0.1658 0.3300 -0.0319 -0.1587 0.0064  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.5017 0.1460 0.3242 -0.0372 -0.1803 0.0114  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.5613 0.1611 0.3470 -0.0507 -0.2043 0.0177  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.5812 0.1398 0.3395 -0.0577 -0.2280 0.0234  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.6290 0.1634 0.3667 -0.0653 -0.2408 0.0268  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.7567 0.1941 0.4174 -0.0903 -0.2924 0.0404  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.4915 0.1331 0.1900 -0.0039 -0.0586 -0.0116 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.5851 0.1412 0.1868 -0.0051 -0.0414 -0.0119 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.6744 0.1280 0.1873 -0.0276 -0.0860 -0.0074 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.7165 0.1173 0.1753 -0.0367 -0.0939 -0.0063 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.6164 0.1590 0.1910 0.0076  0.0109  -0.0130 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.7471 0.1553 0.1886 0.0053  0.0502  -0.0135 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.7075 0.1313 0.2076 -0.0395 -0.1212 -0.0025 66  SER   A N   
464  C CA  . SER   A 60  ? 0.8099 0.1325 0.2307 -0.0672 -0.1779 0.0076  66  SER   A CA  
465  C C   . SER   A 60  ? 0.9289 0.1163 0.1918 -0.0802 -0.1615 0.0045  66  SER   A C   
466  O O   . SER   A 60  ? 1.0110 0.1163 0.2041 -0.1048 -0.2056 0.0128  66  SER   A O   
467  C CB  . SER   A 60  ? 0.8620 0.1741 0.2976 -0.0774 -0.2153 0.0154  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.9557 0.2511 0.3471 -0.0662 -0.1728 0.0064  66  SER   A OG  
469  N N   . SER   A 61  ? 0.9559 0.1134 0.1640 -0.0651 -0.0954 -0.0054 67  SER   A N   
470  C CA  . SER   A 61  ? 1.0833 0.0963 0.1346 -0.0759 -0.0607 -0.0095 67  SER   A CA  
471  C C   . SER   A 61  ? 1.1151 0.1099 0.1426 -0.0746 -0.0420 -0.0115 67  SER   A C   
472  O O   . SER   A 61  ? 1.2363 0.0959 0.1231 -0.0884 -0.0183 -0.0141 67  SER   A O   
473  C CB  . SER   A 61  ? 1.1097 0.0966 0.1304 -0.0578 0.0145  -0.0161 67  SER   A CB  
474  O OG  . SER   A 61  ? 1.0487 0.1520 0.1891 -0.0272 0.0664  -0.0173 67  SER   A OG  
475  N N   . ARG   A 62  ? 1.0159 0.1340 0.1695 -0.0608 -0.0523 -0.0103 68  ARG   A N   
476  C CA  . ARG   A 62  ? 1.0209 0.1330 0.1644 -0.0599 -0.0416 -0.0114 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.9916 0.1483 0.1956 -0.0743 -0.1104 -0.0033 68  ARG   A C   
478  O O   . ARG   A 62  ? 0.9978 0.1554 0.2004 -0.0749 -0.1090 -0.0034 68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.9557 0.1666 0.1937 -0.0290 0.0218  -0.0155 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 1.0162 0.1654 0.1992 -0.0152 0.0982  -0.0175 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 1.1420 0.1445 0.1813 -0.0273 0.1294  -0.0202 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 1.2341 0.1787 0.2409 -0.0108 0.2169  -0.0199 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 1.3334 0.1754 0.2476 -0.0169 0.2477  -0.0219 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 1.4018 0.1824 0.2342 -0.0417 0.1907  -0.0246 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 1.3604 0.1551 0.2669 0.0009  0.3368  -0.0188 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.9471 0.1476 0.2209 -0.0839 -0.1665 0.0057  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.8983 0.1581 0.2701 -0.0935 -0.2234 0.0177  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.7962 0.1654 0.2693 -0.0712 -0.1882 0.0104  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.7774 0.1561 0.2783 -0.0784 -0.2120 0.0162  69  ARG   A O   
490  C CB  . ARG   A 63  ? 1.0075 0.1541 0.2913 -0.1281 -0.2886 0.0332  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 1.1355 0.2128 0.3862 -0.1556 -0.3538 0.0501  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 1.2694 0.2551 0.4719 -0.1939 -0.4356 0.0737  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 1.4625 0.3090 0.5350 -0.2291 -0.4878 0.0867  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.6476 0.3282 0.5367 -0.2636 -0.5146 0.0913  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.6885 0.3280 0.5113 -0.2652 -0.4926 0.0840  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.7553 0.2998 0.5152 -0.2987 -0.5620 0.1031  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.7177 0.1612 0.2385 -0.0463 -0.1320 -0.0007 70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.6408 0.1707 0.2367 -0.0295 -0.1000 -0.0062 70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.5428 0.1694 0.2299 -0.0135 -0.0741 -0.0104 70  LYS   A C   
500  O O   . LYS   A 64  ? 0.5524 0.1749 0.2278 -0.0086 -0.0603 -0.0116 70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.7081 0.2005 0.2388 -0.0190 -0.0494 -0.0116 70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.8429 0.2787 0.3159 -0.0280 -0.0567 -0.0107 70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.9598 0.3572 0.3796 -0.0146 0.0050  -0.0146 70  LYS   A CD  
504  C CE  . LYS   A 64  ? 1.0565 0.4140 0.4339 -0.0192 0.0085  -0.0150 70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 1.1823 0.3895 0.4084 -0.0393 0.0033  -0.0150 70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.4558 0.1576 0.2186 -0.0068 -0.0633 -0.0125 71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3828 0.1585 0.2090 0.0032  -0.0378 -0.0158 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3779 0.1685 0.1938 0.0141  0.0001  -0.0153 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.4122 0.1806 0.2019 0.0151  0.0073  -0.0148 71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3355 0.1675 0.2398 -0.0006 -0.0456 -0.0171 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.3315 0.1586 0.2797 -0.0094 -0.0763 -0.0121 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3283 0.1875 0.3279 -0.0087 -0.0695 -0.0131 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3413 0.1354 0.3002 -0.0203 -0.1135 -0.0026 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.3071 0.1545 0.3555 -0.0166 -0.0986 -0.0037 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3312 0.1401 0.3603 -0.0250 -0.1301 0.0049  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3270 0.1509 0.1678 0.0212  0.0223  -0.0122 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3078 0.1496 0.1630 0.0297  0.0525  -0.0040 72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2603 0.1663 0.1753 0.0263  0.0525  0.0014  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2368 0.1606 0.1676 0.0225  0.0450  0.0004  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3419 0.1421 0.1677 0.0393  0.0824  0.0033  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.4306 0.1418 0.1719 0.0395  0.0934  -0.0008 72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.4799 0.1598 0.1981 0.0441  0.1179  0.0023  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.5078 0.1543 0.1831 0.0332  0.0821  -0.0060 72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.5688 0.1467 0.1891 0.0408  0.1327  -0.0018 72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5975 0.1392 0.1707 0.0271  0.0907  -0.0089 72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.6436 0.1471 0.1845 0.0306  0.1187  -0.0074 72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.7677 0.1480 0.1882 0.0216  0.1328  -0.0108 72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2511 0.1840 0.1931 0.0253  0.0597  0.0092  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2170 0.1935 0.2002 0.0156  0.0538  0.0191  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2144 0.1970 0.2269 0.0212  0.0665  0.0386  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2407 0.2015 0.2579 0.0344  0.0914  0.0485  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2183 0.2102 0.2152 0.0104  0.0523  0.0239  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2487 0.2105 0.2259 0.0239  0.0692  0.0231  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2667 0.1836 0.1975 0.0303  0.0712  0.0116  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.1871 0.1931 0.2215 0.0103  0.0531  0.0463  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.1847 0.2002 0.2609 0.0136  0.0602  0.0690  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.1811 0.2233 0.2876 -0.0076 0.0334  0.0870  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.1858 0.2271 0.2587 -0.0254 0.0144  0.0747  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2017 0.1997 0.2595 0.0221  0.0692  0.0611  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.2515 0.2025 0.2720 0.0393  0.0968  0.0524  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2104 0.2120 0.2381 0.0112  0.0487  0.0419  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.1565 0.2133 0.3263 -0.0079 0.0331  0.1189  75  SER   A N   
543  C CA  . SER   A 69  ? 0.1703 0.2427 0.3714 -0.0313 -0.0001 0.1437  75  SER   A CA  
544  C C   . SER   A 69  ? 0.1745 0.2468 0.3906 -0.0217 0.0109  0.1462  75  SER   A C   
545  O O   . SER   A 69  ? 0.1907 0.2536 0.4257 0.0024  0.0467  0.1458  75  SER   A O   
546  C CB  . SER   A 69  ? 0.1701 0.2602 0.4552 -0.0378 -0.0122 0.1856  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.2466 0.3363 0.5199 -0.0477 -0.0244 0.1855  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1552 0.2270 0.3484 -0.0407 -0.0148 0.1451  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1446 0.2173 0.3476 -0.0327 -0.0065 0.1454  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.1595 0.2397 0.3902 -0.0581 -0.0427 0.1732  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.1931 0.2626 0.3979 -0.0878 -0.0783 0.1819  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.1488 0.2040 0.2825 -0.0243 0.0063  0.1070  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.1492 0.1913 0.2239 -0.0441 -0.0106 0.0860  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.1465 0.1792 0.1904 -0.0421 -0.0031 0.0665  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.1617 0.1931 0.2104 -0.0647 -0.0280 0.0858  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.1747 0.1881 0.1721 -0.0587 -0.0070 0.0481  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.1866 0.1905 0.1760 -0.0823 -0.0297 0.0655  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.1867 0.1818 0.1549 -0.0789 -0.0166 0.0475  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.1361 0.2267 0.4163 -0.0496 -0.0355 0.1901  77  SER   A N   
560  C CA  . SER   A 71  ? 0.1443 0.2413 0.4619 -0.0745 -0.0740 0.2226  77  SER   A CA  
561  C C   . SER   A 71  ? 0.1921 0.2651 0.4227 -0.0968 -0.0964 0.2004  77  SER   A C   
562  O O   . SER   A 71  ? 0.2030 0.2616 0.3648 -0.0875 -0.0754 0.1616  77  SER   A O   
563  C CB  . SER   A 71  ? 0.1400 0.2551 0.5462 -0.0549 -0.0512 0.2474  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.1799 0.2847 0.5379 -0.0350 -0.0199 0.2150  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2191 0.2822 0.4567 -0.1277 -0.1389 0.2279  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.2833 0.3111 0.4329 -0.1506 -0.1545 0.2087  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.2752 0.3178 0.4356 -0.1274 -0.1278 0.1935  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.2454 0.3191 0.4874 -0.1050 -0.1119 0.2115  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3568 0.3544 0.4971 -0.1968 -0.2143 0.2465  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4602 0.4315 0.5775 -0.2257 -0.2478 0.2635  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.6122 0.5183 0.6579 -0.2823 -0.3096 0.2883  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.7538 0.5850 0.6540 -0.3100 -0.3055 0.2558  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.8193 0.6102 0.6933 -0.3487 -0.3538 0.2843  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3020 0.3181 0.3845 -0.1320 -0.1180 0.1616  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3009 0.3310 0.3963 -0.1107 -0.0960 0.1486  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.2845 0.3311 0.4424 -0.1175 -0.1174 0.1836  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.2918 0.3176 0.4378 -0.1521 -0.1595 0.2084  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3533 0.3454 0.3621 -0.1238 -0.0896 0.1176  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.3879 0.3486 0.3407 -0.1395 -0.0889 0.1044  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3467 0.3138 0.3309 -0.1558 -0.1202 0.1370  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.2669 0.3426 0.4892 -0.0873 -0.0895 0.1882  80  SER   A N   
582  C CA  . SER   A 74  ? 0.2534 0.3478 0.5534 -0.0898 -0.1023 0.2241  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2261 0.3332 0.5538 -0.0566 -0.0596 0.2122  80  SER   A C   
584  O O   . SER   A 74  ? 0.2226 0.3192 0.5045 -0.0341 -0.0261 0.1780  80  SER   A O   
585  C CB  . SER   A 74  ? 0.2672 0.3813 0.6667 -0.0956 -0.1182 0.2705  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3035 0.4290 0.7402 -0.0638 -0.0725 0.2641  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2051 0.3280 0.6058 -0.0569 -0.0647 0.2430  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2086 0.3364 0.6407 -0.0291 -0.0241 0.2385  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2043 0.3344 0.7098 -0.0044 0.0198  0.2560  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.1920 0.3407 0.7984 -0.0113 0.0099  0.2997  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.1886 0.3315 0.6811 -0.0424 -0.0478 0.2703  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2397 0.3708 0.6573 -0.0551 -0.0672 0.2469  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2423 0.3869 0.7253 -0.0706 -0.0946 0.2835  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.2602 0.3797 0.6235 -0.0270 -0.0248 0.2060  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2264 0.3297 0.6836 0.0217  0.0676  0.2258  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.2421 0.3260 0.7449 0.0446  0.1205  0.2377  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.2853 0.3295 0.7566 0.0671  0.1718  0.2213  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3173 0.3383 0.6927 0.0688  0.1675  0.1852  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.2745 0.3410 0.7232 0.0478  0.1270  0.2174  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.2622 0.3615 0.7507 0.0250  0.0812  0.2395  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.2947 0.3195 0.7577 0.0723  0.1916  0.2207  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3078 0.3958 0.7168 0.0207  0.0706  0.2099  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.2757 0.3048 0.8291 0.0832  0.2224  0.2499  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3385 0.3125 0.8517 0.1025  0.2790  0.2357  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.3967 0.2976 0.7851 0.1128  0.3125  0.1982  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4149 0.3006 0.7966 0.1153  0.3256  0.1983  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3342 0.2996 0.9728 0.1173  0.3364  0.2784  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4047 0.3041 0.9985 0.1345  0.3990  0.2657  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4314 0.3450 1.0135 0.1307  0.3800  0.2597  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4715 0.2830 1.0198 0.1521  0.4782  0.2580  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.4931 0.3392 1.0258 0.1446  0.4370  0.2477  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5322 0.2646 1.0197 0.1637  0.5377  0.2456  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5340 0.2864 1.0169 0.1601  0.5158  0.2411  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.4379 0.2906 0.7255 0.1154  0.3197  0.1680  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.5190 0.2888 0.6735 0.1181  0.3379  0.1346  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.5946 0.2774 0.6844 0.1270  0.3897  0.1267  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.5871 0.2844 0.6833 0.1259  0.3784  0.1255  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.5381 0.3265 0.6136 0.1036  0.2741  0.1037  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.6198 0.3212 0.5711 0.1018  0.2824  0.0775  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.4904 0.3542 0.6192 0.0926  0.2282  0.1099  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6726 0.2548 0.6859 0.1333  0.4461  0.1196  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.7671 0.2315 0.6852 0.1378  0.5054  0.1101  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.8267 0.2453 0.6198 0.1240  0.4639  0.0809  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.8324 0.2751 0.5773 0.1109  0.3992  0.0626  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.8984 0.2525 0.7285 0.1396  0.5610  0.1034  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.9575 0.3339 0.9107 0.1555  0.6194  0.1350  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 1.1079 0.3855 1.0697 0.1704  0.7250  0.1515  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.1929 0.4213 1.1091 0.1704  0.7467  0.1454  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 1.1304 0.3787 1.1522 0.1827  0.7904  0.1722  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.8725 0.2111 0.6091 0.1263  0.5061  0.0782  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.9466 0.2264 0.5596 0.1110  0.4673  0.0540  86  ALA   A CA  
632  C C   . ALA   A 80  ? 1.0448 0.2271 0.5052 0.0918  0.4381  0.0317  86  ALA   A C   
633  O O   . ALA   A 80  ? 1.0978 0.2098 0.5071 0.0915  0.4760  0.0315  86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.9942 0.1845 0.5605 0.1154  0.5278  0.0563  86  ALA   A CB  
635  N N   . SER   A 81  ? 1.0640 0.2396 0.4583 0.0745  0.3694  0.0161  87  SER   A N   
636  C CA  . SER   A 81  ? 1.1405 0.2256 0.4012 0.0514  0.3258  0.0009  87  SER   A CA  
637  C C   . SER   A 81  ? 1.1975 0.2303 0.3756 0.0325  0.2752  -0.0083 87  SER   A C   
638  O O   . SER   A 81  ? 1.1644 0.2423 0.3953 0.0406  0.2790  -0.0052 87  SER   A O   
639  C CB  . SER   A 81  ? 1.0963 0.2805 0.4262 0.0493  0.2671  -0.0001 87  SER   A CB  
640  O OG  . SER   A 81  ? 1.0383 0.3499 0.4769 0.0530  0.2159  0.0015  87  SER   A OG  
641  N N   . GLU   A 82  ? 1.2693 0.2062 0.3229 0.0053  0.2230  -0.0165 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.3050 0.1981 0.2968 -0.0157 0.1628  -0.0194 88  GLU   A CA  
643  C C   . GLU   A 82  ? 1.1682 0.2157 0.3049 -0.0075 0.1029  -0.0160 88  GLU   A C   
644  O O   . GLU   A 82  ? 1.1810 0.2214 0.3082 -0.0169 0.0650  -0.0155 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.4669 0.2176 0.3007 -0.0518 0.1096  -0.0218 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.5589 0.3322 0.4070 -0.0584 0.0756  -0.0202 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.7569 0.3986 0.4656 -0.0987 0.0043  -0.0168 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.8275 0.3711 0.4388 -0.1240 -0.0335 -0.0137 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.8026 0.4395 0.5033 -0.1071 -0.0200 -0.0146 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 1.0399 0.2184 0.3069 0.0098  0.1017  -0.0130 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.9194 0.2316 0.3149 0.0169  0.0586  -0.0108 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.8182 0.2309 0.3223 0.0390  0.0968  -0.0062 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.7833 0.2648 0.3526 0.0407  0.0685  -0.0060 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.8717 0.2436 0.3213 0.0150  0.0274  -0.0104 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.9450 0.2172 0.2930 -0.0056 -0.0009 -0.0112 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.9877 0.2135 0.2990 -0.0290 -0.0697 -0.0069 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.9881 0.2124 0.2850 -0.0034 0.0375  -0.0129 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 1.0696 0.1987 0.2876 -0.0526 -0.1049 -0.0034 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 1.0765 0.2007 0.2702 -0.0250 0.0101  -0.0133 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 1.1271 0.2022 0.2780 -0.0511 -0.0643 -0.0081 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 1.2264 0.1956 0.2728 -0.0772 -0.1001 -0.0044 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.7736 0.1943 0.3050 0.0541  0.1575  0.0006  90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.6885 0.2041 0.3332 0.0704  0.1822  0.0117  90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.7239 0.1992 0.3740 0.0834  0.2533  0.0236  90  TYR   A C   
665  O O   . TYR   A 84  ? 0.7742 0.1762 0.3755 0.0858  0.2988  0.0259  90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.5823 0.1986 0.3269 0.0760  0.1728  0.0196  90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.5093 0.1774 0.2744 0.0661  0.1167  0.0106  90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.5084 0.1667 0.2539 0.0607  0.1028  0.0065  90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4592 0.1883 0.2742 0.0633  0.0846  0.0081  90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.4677 0.1716 0.2437 0.0528  0.0593  0.0005  90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.4233 0.1941 0.2674 0.0556  0.0461  0.0017  90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.4200 0.1792 0.2484 0.0507  0.0346  -0.0015 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3487 0.1414 0.2114 0.0436  0.0023  -0.0062 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.6870 0.2176 0.4155 0.0930  0.2680  0.0348  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.6947 0.2043 0.4686 0.1076  0.3394  0.0538  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.6466 0.2230 0.5265 0.1160  0.3554  0.0744  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.6068 0.2516 0.5189 0.1094  0.3069  0.0714  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.6649 0.2338 0.5093 0.1122  0.3318  0.0625  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.6153 0.2760 0.4986 0.1032  0.2605  0.0550  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.6337 0.2514 0.4263 0.0910  0.2229  0.0342  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.6410 0.2011 0.5872 0.1298  0.4219  0.0984  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5896 0.2165 0.6543 0.1359  0.4306  0.1246  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.4834 0.2326 0.6574 0.1290  0.3698  0.1398  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.4673 0.2433 0.6657 0.1278  0.3561  0.1426  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5981 0.1816 0.7324 0.1521  0.5161  0.1530  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.4172 0.2285 0.6328 0.1206  0.3284  0.1451  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3418 0.2434 0.6221 0.1069  0.2670  0.1546  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.2846 0.2347 0.6121 0.0965  0.2354  0.1673  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3014 0.2223 0.6041 0.1014  0.2555  0.1627  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.3624 0.2653 0.5555 0.0973  0.2221  0.1212  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.3663 0.2657 0.4937 0.0886  0.1892  0.0972  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.3893 0.2439 0.4203 0.0859  0.1724  0.0671  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.3575 0.2382 0.3694 0.0748  0.1299  0.0517  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.3396 0.2015 0.3217 0.0729  0.1270  0.0448  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.2763 0.1637 0.2533 0.0633  0.0927  0.0330  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.3739 0.1875 0.3336 0.0806  0.1635  0.0505  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.2414 0.2548 0.6204 0.0793  0.1841  0.1814  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.2252 0.2722 0.6226 0.0637  0.1465  0.1892  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2161 0.2574 0.5138 0.0541  0.1141  0.1507  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2046 0.2487 0.4639 0.0489  0.0955  0.1335  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.2111 0.3078 0.6916 0.0425  0.1028  0.2243  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.2223 0.3357 0.8350 0.0472  0.1228  0.2737  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.2346 0.3647 0.9248 0.0408  0.1151  0.3060  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.2343 0.3503 0.9075 0.0556  0.1444  0.2926  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.2085 0.3572 1.0450 0.0439  0.1305  0.3589  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.2123 0.3464 1.0287 0.0592  0.1627  0.3439  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.2088 0.3595 1.1128 0.0536  0.1562  0.3785  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.2133 0.3836 1.2819 0.0569  0.1734  0.4359  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.1944 0.2257 0.4588 0.0531  0.1117  0.1390  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.1903 0.2183 0.3825 0.0438  0.0842  0.1085  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.1611 0.2212 0.3746 0.0218  0.0485  0.1203  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.1452 0.2173 0.4048 0.0177  0.0470  0.1432  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2174 0.2059 0.3518 0.0539  0.1013  0.0878  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2140 0.2026 0.2966 0.0443  0.0727  0.0618  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.2610 0.2038 0.2853 0.0518  0.0806  0.0434  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.2688 0.1645 0.2540 0.0604  0.0977  0.0382  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2433 0.1907 0.2534 0.0454  0.0652  0.0337  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.1471 0.2131 0.3273 0.0054  0.0213  0.1079  96  SER   A N   
719  C CA  . SER   A 90  ? 0.1398 0.2135 0.3149 -0.0216 -0.0110 0.1180  96  SER   A CA  
720  C C   . SER   A 90  ? 0.1666 0.2252 0.2893 -0.0267 -0.0124 0.0946  96  SER   A C   
721  O O   . SER   A 90  ? 0.1747 0.2219 0.2719 -0.0102 0.0055  0.0714  96  SER   A O   
722  C CB  . SER   A 90  ? 0.1612 0.2308 0.3145 -0.0400 -0.0318 0.1174  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2013 0.2558 0.3056 -0.0330 -0.0198 0.0855  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.1706 0.2236 0.2798 -0.0517 -0.0360 0.1050  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.1878 0.2224 0.2499 -0.0595 -0.0348 0.0858  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.1715 0.2145 0.2498 -0.0375 -0.0154 0.0789  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.1762 0.2070 0.2230 -0.0327 -0.0059 0.0563  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2124 0.2244 0.2257 -0.0614 -0.0235 0.0570  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.2733 0.2623 0.2541 -0.0861 -0.0373 0.0617  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3503 0.2957 0.2704 -0.1174 -0.0470 0.0607  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.2869 0.2816 0.2798 -0.0866 -0.0433 0.0693  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3751 0.2951 0.2649 -0.1370 -0.0586 0.0668  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3354 0.2893 0.2728 -0.1183 -0.0577 0.0720  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.1553 0.2139 0.2861 -0.0257 -0.0081 0.1012  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.1629 0.2159 0.2987 -0.0055 0.0160  0.0953  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.1447 0.2075 0.3106 -0.0137 0.0080  0.1149  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.1344 0.2131 0.3542 -0.0260 -0.0088 0.1470  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.1651 0.2116 0.3316 0.0160  0.0450  0.1043  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.1992 0.2169 0.3534 0.0355  0.0786  0.0988  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2389 0.2283 0.3212 0.0385  0.0755  0.0674  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2293 0.2223 0.4051 0.0531  0.1170  0.1102  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.1442 0.1967 0.2834 -0.0071 0.0178  0.0996  99  MET   A N   
743  C CA  . MET   A 93  ? 0.1346 0.1955 0.3011 -0.0133 0.0121  0.1166  99  MET   A CA  
744  C C   . MET   A 93  ? 0.1627 0.2112 0.3439 0.0106  0.0471  0.1166  99  MET   A C   
745  O O   . MET   A 93  ? 0.2001 0.2224 0.3331 0.0240  0.0648  0.0925  99  MET   A O   
746  C CB  . MET   A 93  ? 0.1602 0.2122 0.2740 -0.0294 -0.0043 0.0976  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2082 0.2497 0.2865 -0.0555 -0.0285 0.0948  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.2647 0.2774 0.2741 -0.0715 -0.0282 0.0677  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.2098 0.2218 0.2127 -0.0446 -0.0014 0.0379  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1440 0.2024 0.3909 0.0143  0.0576  0.1459  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.1673 0.1999 0.4202 0.0362  0.1005  0.1457  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.1667 0.2039 0.4231 0.0325  0.0957  0.1482  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.1428 0.2078 0.4335 0.0141  0.0632  0.1661  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.1660 0.1957 0.5039 0.0500  0.1364  0.1788  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2166 0.2323 0.5534 0.0585  0.1547  0.1774  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2187 0.2210 0.6449 0.0751  0.2051  0.2106  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.2742 0.2422 0.5043 0.0675  0.1697  0.1385  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.1941 0.1958 0.4102 0.0479  0.1270  0.1322  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2102 0.2101 0.4277 0.0485  0.1309  0.1334  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2534 0.2029 0.4629 0.0695  0.1856  0.1352  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2941 0.1957 0.4605 0.0805  0.2165  0.1249  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2419 0.2379 0.3847 0.0395  0.1055  0.1020  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2461 0.1974 0.4940 0.0733  0.2006  0.1501  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.3109 0.2022 0.5400 0.0913  0.2582  0.1503  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3737 0.2239 0.4881 0.0882  0.2476  0.1144  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3706 0.2525 0.4764 0.0780  0.2125  0.1056  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2976 0.2092 0.6279 0.0967  0.2792  0.1844  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3434 0.1796 0.6402 0.1149  0.3470  0.1810  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2436 0.1953 0.7060 0.0968  0.2822  0.2278  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.4293 0.2054 0.4554 0.0939  0.2732  0.0957  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4932 0.2196 0.4119 0.0871  0.2557  0.0674  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.5583 0.1900 0.3761 0.0878  0.2784  0.0534  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.5644 0.1816 0.3928 0.0930  0.3005  0.0600  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.6032 0.1637 0.3187 0.0797  0.2699  0.0357  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.6811 0.1329 0.2764 0.0722  0.2788  0.0227  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.6773 0.1486 0.2558 0.0610  0.2272  0.0126  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.6264 0.1609 0.2372 0.0525  0.1734  0.0064  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.7627 0.1213 0.2462 0.0607  0.2751  0.0110  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.9242 0.1475 0.2633 0.0462  0.2802  0.0007  104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 1.0421 0.1668 0.3215 0.0526  0.3500  0.0043  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.9914 0.1682 0.2482 0.0242  0.2207  -0.0097 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 1.1420 0.1518 0.2826 0.0318  0.3305  -0.0068 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 1.1255 0.1640 0.2512 0.0132  0.2476  -0.0136 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.7241 0.1276 0.2456 0.0603  0.2490  0.0111  105 SER   A N   
785  C CA  . SER   A 99  ? 0.7594 0.1594 0.2512 0.0492  0.2058  0.0028  105 SER   A CA  
786  C C   . SER   A 99  ? 0.8858 0.1591 0.2631 0.0437  0.2386  -0.0007 105 SER   A C   
787  O O   . SER   A 99  ? 0.9191 0.1399 0.2838 0.0555  0.3074  0.0064  105 SER   A O   
788  C CB  . SER   A 99  ? 0.6754 0.1892 0.2814 0.0571  0.1900  0.0094  105 SER   A CB  
789  O OG  . SER   A 99  ? 0.6823 0.1960 0.3252 0.0700  0.2376  0.0215  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.9543 0.1699 0.2483 0.0242  0.1910  -0.0095 106 GLU   A N   
791  C CA  . GLU   A 100 ? 1.0712 0.1579 0.2409 0.0125  0.2090  -0.0134 106 GLU   A CA  
792  C C   . GLU   A 100 ? 1.0791 0.2008 0.2665 0.0024  0.1504  -0.0152 106 GLU   A C   
793  O O   . GLU   A 100 ? 1.0149 0.2351 0.2883 0.0006  0.0949  -0.0145 106 GLU   A O   
794  C CB  . GLU   A 100 ? 1.2264 0.1624 0.2342 -0.0126 0.1972  -0.0195 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 1.3505 0.2172 0.3115 -0.0046 0.2666  -0.0190 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 1.5067 0.2324 0.3080 -0.0339 0.2398  -0.0250 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.6329 0.2325 0.2952 -0.0618 0.2096  -0.0283 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.4677 0.2064 0.2808 -0.0320 0.2421  -0.0247 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 1.1567 0.1936 0.2643 -0.0048 0.1644  -0.0170 107 PRO   A N   
800  C CA  . PRO   A 101 ? 1.1593 0.2199 0.2781 -0.0171 0.1022  -0.0173 107 PRO   A CA  
801  C C   . PRO   A 101 ? 1.2093 0.2066 0.2550 -0.0468 0.0274  -0.0163 107 PRO   A C   
802  O O   . PRO   A 101 ? 1.3592 0.2175 0.2628 -0.0678 0.0284  -0.0176 107 PRO   A O   
803  C CB  . PRO   A 101 ? 1.2288 0.1914 0.2592 -0.0200 0.1409  -0.0191 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 1.2770 0.1563 0.2493 -0.0087 0.2307  -0.0194 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 1.2291 0.1304 0.2234 -0.0047 0.2374  -0.0185 107 PRO   A CD  
806  N N   . GLY   A 102 ? 1.0910 0.1883 0.2404 -0.0487 -0.0329 -0.0116 108 GLY   A N   
807  C CA  . GLY   A 102 ? 1.0566 0.1490 0.2133 -0.0703 -0.1072 -0.0038 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.9296 0.1605 0.2297 -0.0527 -0.1090 -0.0036 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.8952 0.1710 0.2655 -0.0620 -0.1629 0.0046  108 GLY   A O   
810  N N   . ASP   A 103 ? 0.8562 0.1494 0.2032 -0.0288 -0.0488 -0.0101 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.7353 0.1454 0.1997 -0.0155 -0.0477 -0.0103 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.6219 0.1393 0.1996 -0.0050 -0.0536 -0.0100 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.5461 0.1418 0.2083 -0.0012 -0.0630 -0.0099 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.7345 0.1635 0.2066 0.0007  0.0080  -0.0126 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.8174 0.1581 0.1990 -0.0103 0.0085  -0.0134 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.8247 0.1417 0.1884 -0.0281 -0.0439 -0.0108 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.8612 0.1545 0.1961 -0.0017 0.0624  -0.0143 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.6150 0.1277 0.1882 -0.0022 -0.0472 -0.0102 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.5327 0.1350 0.2018 0.0055  -0.0524 -0.0102 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.4921 0.1300 0.2277 -0.0041 -0.0980 -0.0064 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.5356 0.1157 0.2390 -0.0203 -0.1407 0.0007  110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.5619 0.1373 0.2035 0.0068  -0.0458 -0.0100 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.6056 0.1669 0.2202 0.0232  0.0210  -0.0098 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.4176 0.1388 0.2426 0.0033  -0.0879 -0.0085 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.3822 0.1329 0.2826 -0.0036 -0.1163 -0.0036 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.3659 0.1411 0.2976 -0.0042 -0.1123 -0.0042 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.3321 0.1451 0.3426 -0.0058 -0.1155 -0.0016 111 GLY   A O   
828  N N   . GLY   A 106 ? 0.3711 0.1228 0.2454 -0.0022 -0.0987 -0.0074 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.3208 0.0985 0.2224 -0.0020 -0.0925 -0.0087 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2437 0.0906 0.2057 0.0046  -0.0625 -0.0144 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2256 0.0944 0.1810 0.0105  -0.0396 -0.0172 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2039 0.0757 0.2216 0.0007  -0.0637 -0.0142 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.1755 0.0900 0.2295 0.0013  -0.0340 -0.0203 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.1821 0.1114 0.2055 0.0027  -0.0148 -0.0233 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2114 0.1288 0.2168 0.0035  -0.0204 -0.0221 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.1849 0.1073 0.3123 -0.0040 -0.0333 -0.0178 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2070 0.1256 0.3849 -0.0048 -0.0419 -0.0120 113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.1915 0.1337 0.3307 -0.0077 0.0021  -0.0256 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2123 0.1321 0.4858 -0.0086 -0.0413 -0.0022 113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.1567 0.1090 0.1781 0.0000  0.0047  -0.0250 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.1582 0.1251 0.1640 -0.0041 0.0166  -0.0229 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.1745 0.1439 0.1945 -0.0171 0.0309  -0.0291 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.1653 0.1286 0.1939 -0.0230 0.0411  -0.0328 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.1773 0.1554 0.1702 -0.0045 0.0206  -0.0144 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.1863 0.1783 0.1750 -0.0149 0.0235  -0.0049 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.1856 0.1788 0.1738 -0.0082 0.0249  0.0004  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.1874 0.1905 0.1825 -0.0178 0.0200  0.0106  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.1851 0.1544 0.2021 -0.0220 0.0366  -0.0305 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.1880 0.1437 0.2057 -0.0358 0.0574  -0.0371 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.2158 0.1689 0.1958 -0.0486 0.0585  -0.0336 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.1942 0.1630 0.1733 -0.0419 0.0458  -0.0270 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.1992 0.1495 0.2609 -0.0314 0.0640  -0.0409 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.2558 0.2035 0.3735 -0.0236 0.0578  -0.0384 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.2976 0.2413 0.4733 -0.0223 0.0589  -0.0350 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.3526 0.2787 0.5482 -0.0312 0.1019  -0.0408 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.3884 0.2988 0.6405 -0.0321 0.1287  -0.0393 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.4254 0.3028 0.6763 -0.0419 0.1792  -0.0464 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.3711 0.2904 0.6812 -0.0244 0.1073  -0.0291 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.2465 0.1698 0.1920 -0.0691 0.0751  -0.0374 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.2965 0.2020 0.1974 -0.0883 0.0723  -0.0328 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.3554 0.2214 0.2449 -0.0987 0.1066  -0.0462 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.3510 0.2149 0.2858 -0.0876 0.1289  -0.0542 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.3390 0.2217 0.1897 -0.1111 0.0580  -0.0223 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.3809 0.2038 0.1845 -0.1304 0.0871  -0.0344 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.4156 0.2459 0.2509 -0.1207 0.1122  -0.0461 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.4799 0.2608 0.2978 -0.1316 0.1541  -0.0590 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.5376 0.2615 0.3351 -0.1420 0.1969  -0.0694 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.5720 0.2555 0.3826 -0.1440 0.2454  -0.0794 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.5590 0.2963 0.2992 -0.1594 0.1491  -0.0559 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.6647 0.3491 0.3149 -0.1922 0.1303  -0.0472 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.8112 0.4513 0.3849 -0.2240 0.1082  -0.0372 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.8357 0.5071 0.4157 -0.2300 0.0584  -0.0156 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.8705 0.4313 0.3744 -0.2460 0.1465  -0.0503 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.5438 0.2600 0.3136 -0.1486 0.1844  -0.0658 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.5716 0.2279 0.3149 -0.1595 0.2265  -0.0753 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.5054 0.2005 0.3467 -0.1319 0.2413  -0.0773 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.5372 0.1841 0.3795 -0.1367 0.2866  -0.0845 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.6418 0.2537 0.2930 -0.1869 0.2068  -0.0698 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.7445 0.3121 0.2997 -0.2205 0.1773  -0.0602 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.7590 0.3804 0.3285 -0.2203 0.1175  -0.0401 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.8516 0.3196 0.2985 -0.2566 0.1999  -0.0655 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.8194 0.3813 0.3014 -0.2562 0.0975  -0.0307 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.8908 0.3556 0.2868 -0.2805 0.1438  -0.0467 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4159 0.1870 0.3338 -0.1058 0.2043  -0.0696 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.3498 0.1514 0.3550 -0.0844 0.2060  -0.0674 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.2847 0.1362 0.3002 -0.0710 0.1592  -0.0594 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.2815 0.1573 0.2650 -0.0710 0.1274  -0.0538 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.2598 0.1236 0.3272 -0.0590 0.1579  -0.0573 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.2368 0.1365 0.3103 -0.0468 0.1196  -0.0507 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.2448 0.1399 0.2528 -0.0577 0.1103  -0.0495 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.2744 0.1353 0.2518 -0.0715 0.1325  -0.0539 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.2354 0.1427 0.3801 -0.0344 0.1169  -0.0466 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.2282 0.1590 0.3599 -0.0250 0.0810  -0.0414 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.2202 0.1350 0.4423 -0.0259 0.1094  -0.0392 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.2118 0.1361 0.2032 -0.0522 0.0791  -0.0410 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.2182 0.1464 0.1719 -0.0611 0.0636  -0.0321 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.1987 0.1471 0.1754 -0.0468 0.0514  -0.0284 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2128 0.1556 0.1715 -0.0549 0.0492  -0.0246 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.2312 0.1781 0.1737 -0.0623 0.0434  -0.0197 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.2373 0.1945 0.1702 -0.0693 0.0236  -0.0025 121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.2599 0.1842 0.1723 -0.0793 0.0504  -0.0216 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.1700 0.1344 0.1775 -0.0282 0.0413  -0.0284 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.1635 0.1352 0.1813 -0.0164 0.0303  -0.0254 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.1621 0.1284 0.1904 -0.0030 0.0160  -0.0248 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.1604 0.1205 0.2013 -0.0027 0.0127  -0.0270 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.1431 0.1029 0.1605 0.0053  0.0068  -0.0212 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.1612 0.0930 0.1629 0.0121  -0.0097 -0.0199 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.1988 0.1136 0.1594 0.0196  -0.0023 -0.0145 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.1935 0.1228 0.1573 0.0221  0.0095  -0.0097 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.1854 0.1004 0.2069 0.0114  -0.0282 -0.0198 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.1941 0.1202 0.2200 0.0133  -0.0209 -0.0202 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.1864 0.1067 0.2665 0.0059  -0.0340 -0.0195 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.2204 0.1231 0.2605 0.0130  -0.0443 -0.0171 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2221 0.0968 0.1430 0.0224  -0.0065 -0.0136 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2525 0.0939 0.1304 0.0300  0.0138  -0.0084 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2787 0.1019 0.1419 0.0329  0.0165  -0.0073 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2799 0.0829 0.1334 0.0276  -0.0074 -0.0111 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.3091 0.0848 0.1242 0.0282  0.0097  -0.0099 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3524 0.0740 0.1140 0.0358  0.0438  -0.0054 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.3212 0.1163 0.1524 0.0265  0.0088  -0.0105 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2787 0.1114 0.1514 0.0408  0.0446  0.0010  125 SER   A N   
922  C CA  . SER   A 119 ? 0.3025 0.1176 0.1636 0.0448  0.0534  0.0031  125 SER   A CA  
923  C C   . SER   A 119 ? 0.3545 0.1608 0.2256 0.0553  0.0950  0.0170  125 SER   A C   
924  O O   . SER   A 119 ? 0.3339 0.1922 0.2663 0.0564  0.1019  0.0296  125 SER   A O   
925  C CB  . SER   A 119 ? 0.2797 0.1498 0.1917 0.0413  0.0399  0.0031  125 SER   A CB  
926  O OG  . SER   A 119 ? 0.3072 0.1625 0.2112 0.0465  0.0514  0.0068  125 SER   A OG  
927  N N   . THR   A 120 ? 0.4161 0.1497 0.2292 0.0607  0.1228  0.0172  126 THR   A N   
928  C CA  . THR   A 120 ? 0.4376 0.1407 0.2590 0.0725  0.1766  0.0316  126 THR   A CA  
929  C C   . THR   A 120 ? 0.4835 0.1631 0.2948 0.0756  0.1988  0.0354  126 THR   A C   
930  O O   . THR   A 120 ? 0.4623 0.1780 0.2878 0.0698  0.1708  0.0309  126 THR   A O   
931  C CB  . THR   A 120 ? 0.3854 0.1537 0.3067 0.0798  0.1932  0.0530  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.3521 0.1840 0.3455 0.0772  0.1817  0.0665  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.3466 0.1495 0.2873 0.0758  0.1688  0.0505  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.5492 0.1707 0.3474 0.0860  0.2559  0.0459  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.5951 0.1936 0.3964 0.0914  0.2872  0.0529  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.6908 0.2000 0.4644 0.1031  0.3632  0.0630  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.7033 0.1896 0.4867 0.1092  0.3942  0.0701  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.7713 0.2259 0.5112 0.1062  0.3977  0.0639  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.8827 0.2305 0.5831 0.1167  0.4829  0.0721  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.8792 0.2684 0.7062 0.1332  0.5319  0.1012  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.8127 0.3149 0.7791 0.1375  0.5058  0.1233  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.9498 0.2376 0.7280 0.1405  0.6044  0.1040  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.9116 0.2192 0.8132 0.1579  0.6646  0.1351  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.8199 0.2163 0.7919 0.1555  0.6185  0.1420  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.7646 0.2214 0.8828 0.1668  0.6400  0.1754  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.8986 0.2703 0.9614 0.1718  0.6932  0.1706  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 1.0451 0.3269 1.0541 0.1769  0.7522  0.1676  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 1.1775 0.3144 1.0608 0.1782  0.8241  0.1536  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.9996 0.3558 1.0999 0.1787  0.7280  0.1825  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.8026 0.1972 0.6738 0.1403  0.5593  0.1137  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.7292 0.2053 0.6589 0.1367  0.5148  0.1178  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.6188 0.2233 0.6375 0.1280  0.4384  0.1237  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.5713 0.2492 0.6575 0.1238  0.4036  0.1333  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.5817 0.2039 0.5898 0.1230  0.4130  0.1171  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.4995 0.2206 0.5674 0.1123  0.3474  0.1195  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4989 0.2057 0.4638 0.0996  0.2996  0.0869  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.5886 0.2096 0.4481 0.0983  0.3149  0.0687  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.4657 0.2194 0.6252 0.1178  0.3620  0.1447  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.4584 0.2354 0.7564 0.1293  0.4044  0.1875  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.4460 0.2361 0.8266 0.1354  0.4264  0.2126  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.4107 0.2717 0.7957 0.1177  0.3532  0.2074  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.3980 0.1803 0.3939 0.0879  0.2425  0.0822  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3749 0.1563 0.3089 0.0771  0.2000  0.0582  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.3006 0.1594 0.3007 0.0691  0.1654  0.0653  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2633 0.1753 0.3288 0.0636  0.1522  0.0812  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3879 0.1575 0.2683 0.0685  0.1709  0.0399  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3488 0.1776 0.2888 0.0653  0.1583  0.0486  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3961 0.1709 0.2420 0.0574  0.1268  0.0220  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2758 0.1308 0.2526 0.0662  0.1511  0.0554  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2310 0.1437 0.2518 0.0568  0.1211  0.0590  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2404 0.1636 0.2279 0.0458  0.0855  0.0376  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.2880 0.1720 0.2228 0.0464  0.0792  0.0219  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.1828 0.1504 0.2014 0.0334  0.0628  0.0395  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.1682 0.1422 0.1687 0.0236  0.0410  0.0217  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.1531 0.1466 0.1690 0.0152  0.0319  0.0237  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.1504 0.1650 0.1917 0.0057  0.0272  0.0397  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.1600 0.1503 0.1662 0.0124  0.0321  0.0199  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.1762 0.1530 0.1733 0.0195  0.0408  0.0209  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.1920 0.1392 0.1573 0.0240  0.0376  0.0073  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.1770 0.1676 0.2015 0.0195  0.0490  0.0387  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2053 0.1316 0.1526 0.0290  0.0457  0.0082  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.1888 0.1632 0.2049 0.0272  0.0618  0.0395  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2048 0.1451 0.1755 0.0318  0.0613  0.0224  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.1347 0.1172 0.1367 0.0160  0.0256  0.0097  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.1222 0.1174 0.1337 0.0077  0.0204  0.0090  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.1298 0.1279 0.1369 -0.0090 0.0173  0.0022  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.1227 0.1105 0.1297 -0.0085 0.0197  -0.0099 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.1370 0.1160 0.1420 0.0149  0.0170  -0.0014 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.1514 0.1543 0.1526 -0.0260 0.0122  0.0124  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.1864 0.1698 0.1599 -0.0465 0.0145  0.0056  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2018 0.1649 0.1680 -0.0489 0.0297  -0.0104 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.1944 0.1624 0.1711 -0.0428 0.0289  -0.0106 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2569 0.2327 0.2104 -0.0704 -0.0024 0.0238  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3762 0.3115 0.2768 -0.0974 -0.0005 0.0186  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3664 0.2966 0.2620 -0.0960 0.0083  0.0110  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4470 0.3458 0.3021 -0.1220 -0.0057 0.0215  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2003 0.1381 0.1551 -0.0571 0.0480  -0.0225 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2399 0.1500 0.1978 -0.0608 0.0730  -0.0344 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.3045 0.1595 0.2027 -0.0881 0.0963  -0.0398 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3462 0.1626 0.2396 -0.0936 0.1299  -0.0499 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2242 0.1417 0.2419 -0.0433 0.0840  -0.0415 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2090 0.1573 0.2585 -0.0238 0.0566  -0.0357 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2277 0.1368 0.2535 -0.0454 0.0947  -0.0448 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3292 0.1709 0.1815 -0.1059 0.0824  -0.0324 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3875 0.1600 0.1623 -0.1371 0.1006  -0.0367 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.4755 0.1884 0.1810 -0.1629 0.1079  -0.0368 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.5514 0.1835 0.1829 -0.1879 0.1400  -0.0464 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.3845 0.1568 0.1264 -0.1534 0.0707  -0.0231 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.3431 0.1588 0.1382 -0.1316 0.0709  -0.0254 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3493 0.1661 0.1187 -0.1476 0.0413  -0.0094 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.3235 0.1852 0.1291 -0.1417 0.0045  0.0132  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.3369 0.2144 0.1536 -0.1498 -0.0246 0.0347  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.3667 0.2163 0.1471 -0.1675 -0.0280 0.0357  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.3165 0.2348 0.1869 -0.1406 -0.0480 0.0577  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.4708 0.2129 0.1925 -0.1587 0.0822  -0.0264 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.5271 0.2103 0.1808 -0.1843 0.0860  -0.0256 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.5403 0.2058 0.2168 -0.1703 0.1325  -0.0436 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.5967 0.1971 0.2077 -0.1920 0.1501  -0.0474 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.5349 0.2555 0.2032 -0.1879 0.0380  -0.0033 139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4853 0.2855 0.2480 -0.1500 0.0334  -0.0026 139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4308 0.2747 0.2514 -0.1229 0.0412  -0.0089 139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4656 0.2767 0.2364 -0.1500 0.0199  0.0054  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.4804 0.1959 0.2483 -0.1371 0.1503  -0.0517 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.4744 0.1800 0.2885 -0.1229 0.1886  -0.0621 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.5471 0.1807 0.3407 -0.1337 0.2483  -0.0747 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.5103 0.1617 0.3820 -0.1152 0.2722  -0.0777 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.3867 0.1665 0.3086 -0.0884 0.1728  -0.0593 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3576 0.1982 0.2959 -0.0758 0.1235  -0.0479 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3122 0.1986 0.3297 -0.0487 0.1099  -0.0463 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3774 0.2115 0.2846 -0.0846 0.1132  -0.0433 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.6474 0.1895 0.3307 -0.1669 0.2728  -0.0798 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.7371 0.1819 0.3687 -0.1844 0.3399  -0.0926 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.7332 0.1671 0.4558 -0.1629 0.4035  -0.0998 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.7585 0.1442 0.5009 -0.1629 0.4619  -0.1063 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.8406 0.1678 0.3100 -0.2305 0.3502  -0.0956 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.8903 0.2157 0.2719 -0.2597 0.2793  -0.0804 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 1.0254 0.2040 0.2319 -0.3133 0.2933  -0.0825 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.8720 0.2452 0.2828 -0.2535 0.2508  -0.0743 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.7053 0.1845 0.4943 -0.1444 0.3925  -0.0958 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.6754 0.1488 0.5670 -0.1243 0.4457  -0.0968 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.6308 0.1712 0.6720 -0.0948 0.4439  -0.0875 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.6118 0.1370 0.7532 -0.0817 0.4939  -0.0831 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.6370 0.1396 0.5524 -0.1154 0.4264  -0.0933 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.5549 0.1572 0.5035 -0.0998 0.3462  -0.0832 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.5718 0.1898 0.4406 -0.1134 0.2958  -0.0797 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4776 0.1645 0.5468 -0.0700 0.3113  -0.0730 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.5211 0.2276 0.4551 -0.0909 0.2421  -0.0701 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.4684 0.2115 0.5124 -0.0660 0.2494  -0.0674 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.4320 0.1441 0.6291 -0.0490 0.3251  -0.0649 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.4227 0.2333 0.5416 -0.0433 0.2065  -0.0583 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.3823 0.1647 0.6553 -0.0294 0.2700  -0.0530 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.3840 0.2086 0.6070 -0.0274 0.2146  -0.0519 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.6024 0.2098 0.6618 -0.0863 0.3877  -0.0816 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.5510 0.2124 0.7358 -0.0639 0.3763  -0.0707 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.6275 0.2336 0.8547 -0.0669 0.4452  -0.0721 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5773 0.2116 0.9404 -0.0491 0.4541  -0.0582 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.4999 0.2213 0.6642 -0.0597 0.3116  -0.0670 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.4546 0.2340 0.6061 -0.0511 0.2489  -0.0617 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.4333 0.2548 0.5605 -0.0479 0.2012  -0.0581 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4016 0.2184 0.6568 -0.0313 0.2303  -0.0508 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.7496 0.2708 0.8597 -0.0919 0.4917  -0.0862 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.8351 0.2818 0.9530 -0.0997 0.5683  -0.0908 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.9098 0.2781 1.0674 -0.1003 0.6576  -0.0923 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.9261 0.2461 1.1438 -0.0979 0.7276  -0.0901 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.9522 0.3195 0.8991 -0.1327 0.5794  -0.1057 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.9997 0.4278 0.9278 -0.1322 0.5155  -0.1024 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.9530 0.4487 0.9967 -0.1094 0.4983  -0.0928 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 1.0891 0.4929 0.8893 -0.1563 0.4811  -0.1069 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.9635 0.3041 1.0739 -0.1064 0.6648  -0.0969 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 1.0254 0.2779 1.1588 -0.1087 0.7575  -0.0995 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.9870 0.3044 1.2535 -0.0841 0.7401  -0.0850 145 GLU   A C   
1072 O O   . GLU   A 139 ? 1.0220 0.2753 1.3254 -0.0828 0.8147  -0.0844 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.1744 0.3003 1.1036 -0.1460 0.7958  -0.1196 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.2552 0.4207 1.0844 -0.1581 0.7118  -0.1219 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.4106 0.5159 1.0522 -0.1961 0.6781  -0.1311 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.4701 0.5541 1.0037 -0.2175 0.6377  -0.1324 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.4427 0.5214 1.0508 -0.2059 0.6885  -0.1342 145 GLU   A OE2 
1078 N N1  . A1B3G B .   ? 0.4901 0.2436 0.3216 0.0608  0.1027  0.0142  201 A1B3G A N1  
1079 C C4  . A1B3G B .   ? 0.9550 0.0967 0.3009 0.0683  0.3872  0.0149  201 A1B3G A C4  
1080 C C5  . A1B3G B .   ? 0.9500 0.1070 0.2916 0.0630  0.3563  0.0108  201 A1B3G A C5  
1081 C C6  . A1B3G B .   ? 0.8857 0.1415 0.2831 0.0560  0.2798  0.0060  201 A1B3G A C6  
1082 C C7  . A1B3G B .   ? 0.8846 0.1440 0.2706 0.0499  0.2506  0.0019  201 A1B3G A C7  
1083 C C8  . A1B3G B .   ? 0.7827 0.1719 0.3089 0.0645  0.2464  0.0120  201 A1B3G A C8  
1084 C C10 . A1B3G B .   ? 0.7959 0.1761 0.2537 0.0325  0.1150  -0.0072 201 A1B3G A C10 
1085 C C13 . A1B3G B .   ? 0.5546 0.2341 0.3285 0.0653  0.1344  0.0155  201 A1B3G A C13 
1086 O O1  . A1B3G B .   ? 0.5466 0.2239 0.3385 0.0725  0.1608  0.0233  201 A1B3G A O1  
1087 C C12 . A1B3G B .   ? 0.6443 0.2243 0.3153 0.0588  0.1403  0.0074  201 A1B3G A C12 
1088 F F   . A1B3G B .   ? 0.6457 0.2465 0.3220 0.0522  0.1115  0.0029  201 A1B3G A F   
1089 C C11 . A1B3G B .   ? 0.7090 0.2099 0.2899 0.0458  0.1137  -0.0020 201 A1B3G A C11 
1090 C C9  . A1B3G B .   ? 0.8329 0.1497 0.2522 0.0429  0.1872  -0.0027 201 A1B3G A C9  
1091 C C14 . A1B3G B .   ? 0.6827 0.2056 0.3326 0.0697  0.2064  0.0169  201 A1B3G A C14 
1092 N N   . A1B3G B .   ? 0.7679 0.1786 0.2994 0.0598  0.2147  0.0079  201 A1B3G A N   
1093 O O   . A1B3G B .   ? 0.7156 0.1778 0.3406 0.0775  0.2693  0.0253  201 A1B3G A O   
1094 C C1  . A1B3G B .   ? 0.8230 0.1611 0.2809 0.0545  0.2384  0.0053  201 A1B3G A C1  
1095 S S   . A1B3G B .   ? 0.7308 0.1786 0.2622 0.0467  0.1595  0.0003  201 A1B3G A S   
1096 C C   . A1B3G B .   ? 0.6840 0.1944 0.2638 0.0444  0.1313  -0.0007 201 A1B3G A C   
1097 C C3  . A1B3G B .   ? 0.8992 0.1261 0.3018 0.0662  0.3390  0.0138  201 A1B3G A C3  
1098 C C2  . A1B3G B .   ? 0.8362 0.1611 0.2952 0.0593  0.2662  0.0090  201 A1B3G A C2  
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