data_7I4L
# 
_entry.id   7I4L 
# 
_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   7I4L         pdb_00007i4l 10.2210/pdb7i4l/pdb 
WWPDB D_1001408308 ?            ?                   
# 
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                        7I4L 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2025-03-12 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.email              frank.von-delft@diamond.ac.uk 
_pdbx_contact_author.name_first         Frank 
_pdbx_contact_author.name_last          'von Delft' 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0378-0017 
_pdbx_contact_author.name_mi            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Lithgo, R.M.'        1  ? 
'Fairhead, M.'        2  ? 
'Koekemoer, L.'       3  ? 
'Balcomb, B.H.'       4  ? 
'Capkin, E.'          5  ? 
'Chandran, A.V.'      6  ? 
'Golding, M.'         7  ? 
'Godoy, A.S.'         8  ? 
'Aschenbrenner, J.C.' 9  ? 
'Marples, P.G.'       10 ? 
'Ni, X.'              11 ? 
'Thompson, W.'        12 ? 
'Tomlinson, C.W.E.'   13 ? 
'Wild, C.'            14 ? 
'Winokan, M.'         15 ? 
'Xavier, M.-A.E.'     16 ? 
'Kenton, N.'          17 ? 
'Tucker, J.'          18 ? 
'DiPoto, M.'          19 ? 
'Lee, A.'             20 ? 
'Fearon, D.'          21 ? 
'von Delft, F.'       22 ? 
# 
_citation.id                        primary 
_citation.title                     
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Lithgo, R.M.'        ? 1  
primary 'Fairhead, M.'        ? 2  
primary 'Koekemoer, L.'       ? 3  
primary 'Balcomb, B.H.'       ? 4  
primary 'Capkin, E.'          ? 5  
primary 'Chandran, A.V.'      ? 6  
primary 'Golding, M.'         ? 7  
primary 'Godoy, A.S.'         ? 8  
primary 'Aschenbrenner, J.C.' ? 9  
primary 'Marples, P.G.'       ? 10 
primary 'Ni, X.'              ? 11 
primary 'Thompson, W.'        ? 12 
primary 'Tomlinson, C.W.E.'   ? 13 
primary 'Wild, C.'            ? 14 
primary 'Winokan, M.'         ? 15 
primary 'Xavier, M.-A.E.'     ? 16 
primary 'Kenton, N.'          ? 17 
primary 'Tucker, J.'          ? 18 
primary 'DiPoto, M.'          ? 19 
primary 'Lee, A.'             ? 20 
primary 'Fearon, D.'          ? 21 
primary 'von Delft, F.'       ? 22 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protease 2A'                                                                  15892.732 1   3.4.22.29 ? ? ? 
2 non-polymer syn '(3S)-N~1~-methyl-N~1~-[2-(methylsulfanyl)phenyl]piperidine-1,3-dicarboxamide' 307.411   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    172 ?         ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'P2A,Picornain 2A,Protein 2A' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(3S)-N~1~-methyl-N~1~-[2-(methylsulfanyl)phenyl]piperidine-1,3-dicarboxamide' A1B2Z 
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 
A1B2Z non-polymer         . '(3S)-N~1~-methyl-N~1~-[2-(methylsulfanyl)phenyl]piperidine-1,3-dicarboxamide' ? 'C15 H21 N3 O2 S' 
307.411 
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        A1B2Z 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B2Z 
_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 A1B2Z 1   201 201 A1B2Z LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 DMS   1   203 4   DMS   DMS A . 
E 5 HOH   1   301 79  HOH   HOH A . 
E 5 HOH   2   302 203 HOH   HOH A . 
E 5 HOH   3   303 261 HOH   HOH A . 
E 5 HOH   4   304 26  HOH   HOH A . 
E 5 HOH   5   305 104 HOH   HOH A . 
E 5 HOH   6   306 180 HOH   HOH A . 
E 5 HOH   7   307 34  HOH   HOH A . 
E 5 HOH   8   308 258 HOH   HOH A . 
E 5 HOH   9   309 181 HOH   HOH A . 
E 5 HOH   10  310 59  HOH   HOH A . 
E 5 HOH   11  311 47  HOH   HOH A . 
E 5 HOH   12  312 210 HOH   HOH A . 
E 5 HOH   13  313 57  HOH   HOH A . 
E 5 HOH   14  314 264 HOH   HOH A . 
E 5 HOH   15  315 13  HOH   HOH A . 
E 5 HOH   16  316 68  HOH   HOH A . 
E 5 HOH   17  317 252 HOH   HOH A . 
E 5 HOH   18  318 60  HOH   HOH A . 
E 5 HOH   19  319 24  HOH   HOH A . 
E 5 HOH   20  320 33  HOH   HOH A . 
E 5 HOH   21  321 251 HOH   HOH A . 
E 5 HOH   22  322 4   HOH   HOH A . 
E 5 HOH   23  323 211 HOH   HOH A . 
E 5 HOH   24  324 36  HOH   HOH A . 
E 5 HOH   25  325 147 HOH   HOH A . 
E 5 HOH   26  326 103 HOH   HOH A . 
E 5 HOH   27  327 107 HOH   HOH A . 
E 5 HOH   28  328 16  HOH   HOH A . 
E 5 HOH   29  329 111 HOH   HOH A . 
E 5 HOH   30  330 133 HOH   HOH A . 
E 5 HOH   31  331 266 HOH   HOH A . 
E 5 HOH   32  332 67  HOH   HOH A . 
E 5 HOH   33  333 146 HOH   HOH A . 
E 5 HOH   34  334 144 HOH   HOH A . 
E 5 HOH   35  335 254 HOH   HOH A . 
E 5 HOH   36  336 218 HOH   HOH A . 
E 5 HOH   37  337 256 HOH   HOH A . 
E 5 HOH   38  338 214 HOH   HOH A . 
E 5 HOH   39  339 255 HOH   HOH A . 
E 5 HOH   40  340 43  HOH   HOH A . 
E 5 HOH   41  341 29  HOH   HOH A . 
E 5 HOH   42  342 42  HOH   HOH A . 
E 5 HOH   43  343 186 HOH   HOH A . 
E 5 HOH   44  344 2   HOH   HOH A . 
E 5 HOH   45  345 278 HOH   HOH A . 
E 5 HOH   46  346 7   HOH   HOH A . 
E 5 HOH   47  347 137 HOH   HOH A . 
E 5 HOH   48  348 20  HOH   HOH A . 
E 5 HOH   49  349 9   HOH   HOH A . 
E 5 HOH   50  350 85  HOH   HOH A . 
E 5 HOH   51  351 77  HOH   HOH A . 
E 5 HOH   52  352 174 HOH   HOH A . 
E 5 HOH   53  353 28  HOH   HOH A . 
E 5 HOH   54  354 37  HOH   HOH A . 
E 5 HOH   55  355 197 HOH   HOH A . 
E 5 HOH   56  356 27  HOH   HOH A . 
E 5 HOH   57  357 249 HOH   HOH A . 
E 5 HOH   58  358 50  HOH   HOH A . 
E 5 HOH   59  359 219 HOH   HOH A . 
E 5 HOH   60  360 169 HOH   HOH A . 
E 5 HOH   61  361 253 HOH   HOH A . 
E 5 HOH   62  362 61  HOH   HOH A . 
E 5 HOH   63  363 12  HOH   HOH A . 
E 5 HOH   64  364 161 HOH   HOH A . 
E 5 HOH   65  365 84  HOH   HOH A . 
E 5 HOH   66  366 21  HOH   HOH A . 
E 5 HOH   67  367 157 HOH   HOH A . 
E 5 HOH   68  368 156 HOH   HOH A . 
E 5 HOH   69  369 62  HOH   HOH A . 
E 5 HOH   70  370 100 HOH   HOH A . 
E 5 HOH   71  371 5   HOH   HOH A . 
E 5 HOH   72  372 167 HOH   HOH A . 
E 5 HOH   73  373 15  HOH   HOH A . 
E 5 HOH   74  374 177 HOH   HOH A . 
E 5 HOH   75  375 131 HOH   HOH A . 
E 5 HOH   76  376 105 HOH   HOH A . 
E 5 HOH   77  377 242 HOH   HOH A . 
E 5 HOH   78  378 260 HOH   HOH A . 
E 5 HOH   79  379 265 HOH   HOH A . 
E 5 HOH   80  380 106 HOH   HOH A . 
E 5 HOH   81  381 11  HOH   HOH A . 
E 5 HOH   82  382 98  HOH   HOH A . 
E 5 HOH   83  383 269 HOH   HOH A . 
E 5 HOH   84  384 90  HOH   HOH A . 
E 5 HOH   85  385 201 HOH   HOH A . 
E 5 HOH   86  386 70  HOH   HOH A . 
E 5 HOH   87  387 95  HOH   HOH A . 
E 5 HOH   88  388 136 HOH   HOH A . 
E 5 HOH   89  389 8   HOH   HOH A . 
E 5 HOH   90  390 275 HOH   HOH A . 
E 5 HOH   91  391 40  HOH   HOH A . 
E 5 HOH   92  392 51  HOH   HOH A . 
E 5 HOH   93  393 257 HOH   HOH A . 
E 5 HOH   94  394 52  HOH   HOH A . 
E 5 HOH   95  395 96  HOH   HOH A . 
E 5 HOH   96  396 217 HOH   HOH A . 
E 5 HOH   97  397 279 HOH   HOH A . 
E 5 HOH   98  398 39  HOH   HOH A . 
E 5 HOH   99  399 80  HOH   HOH A . 
E 5 HOH   100 400 124 HOH   HOH A . 
E 5 HOH   101 401 112 HOH   HOH A . 
E 5 HOH   102 402 78  HOH   HOH A . 
E 5 HOH   103 403 119 HOH   HOH A . 
E 5 HOH   104 404 19  HOH   HOH A . 
E 5 HOH   105 405 248 HOH   HOH A . 
E 5 HOH   106 406 10  HOH   HOH A . 
E 5 HOH   107 407 185 HOH   HOH A . 
E 5 HOH   108 408 268 HOH   HOH A . 
E 5 HOH   109 409 83  HOH   HOH A . 
E 5 HOH   110 410 89  HOH   HOH A . 
E 5 HOH   111 411 216 HOH   HOH A . 
E 5 HOH   112 412 123 HOH   HOH A . 
E 5 HOH   113 413 182 HOH   HOH A . 
E 5 HOH   114 414 224 HOH   HOH A . 
E 5 HOH   115 415 159 HOH   HOH A . 
E 5 HOH   116 416 126 HOH   HOH A . 
E 5 HOH   117 417 227 HOH   HOH A . 
E 5 HOH   118 418 215 HOH   HOH A . 
E 5 HOH   119 419 212 HOH   HOH A . 
E 5 HOH   120 420 155 HOH   HOH A . 
E 5 HOH   121 421 23  HOH   HOH A . 
E 5 HOH   122 422 110 HOH   HOH A . 
E 5 HOH   123 423 128 HOH   HOH A . 
E 5 HOH   124 424 280 HOH   HOH A . 
E 5 HOH   125 425 76  HOH   HOH A . 
E 5 HOH   126 426 116 HOH   HOH A . 
E 5 HOH   127 427 175 HOH   HOH A . 
E 5 HOH   128 428 154 HOH   HOH A . 
E 5 HOH   129 429 233 HOH   HOH A . 
E 5 HOH   130 430 69  HOH   HOH A . 
E 5 HOH   131 431 17  HOH   HOH A . 
E 5 HOH   132 432 232 HOH   HOH A . 
E 5 HOH   133 433 228 HOH   HOH A . 
E 5 HOH   134 434 171 HOH   HOH A . 
E 5 HOH   135 435 140 HOH   HOH A . 
E 5 HOH   136 436 48  HOH   HOH A . 
E 5 HOH   137 437 46  HOH   HOH A . 
E 5 HOH   138 438 270 HOH   HOH A . 
E 5 HOH   139 439 65  HOH   HOH A . 
E 5 HOH   140 440 158 HOH   HOH A . 
E 5 HOH   141 441 272 HOH   HOH A . 
E 5 HOH   142 442 122 HOH   HOH A . 
E 5 HOH   143 443 246 HOH   HOH A . 
E 5 HOH   144 444 162 HOH   HOH A . 
E 5 HOH   145 445 277 HOH   HOH A . 
E 5 HOH   146 446 213 HOH   HOH A . 
E 5 HOH   147 447 117 HOH   HOH A . 
E 5 HOH   148 448 99  HOH   HOH A . 
E 5 HOH   149 449 207 HOH   HOH A . 
E 5 HOH   150 450 129 HOH   HOH A . 
E 5 HOH   151 451 113 HOH   HOH A . 
E 5 HOH   152 452 240 HOH   HOH A . 
E 5 HOH   153 453 276 HOH   HOH A . 
E 5 HOH   154 454 127 HOH   HOH A . 
E 5 HOH   155 455 152 HOH   HOH A . 
E 5 HOH   156 456 86  HOH   HOH A . 
E 5 HOH   157 457 271 HOH   HOH A . 
E 5 HOH   158 458 259 HOH   HOH A . 
E 5 HOH   159 459 164 HOH   HOH A . 
E 5 HOH   160 460 223 HOH   HOH A . 
E 5 HOH   161 461 56  HOH   HOH A . 
E 5 HOH   162 462 206 HOH   HOH A . 
E 5 HOH   163 463 32  HOH   HOH A . 
E 5 HOH   164 464 73  HOH   HOH A . 
E 5 HOH   165 465 165 HOH   HOH A . 
E 5 HOH   166 466 208 HOH   HOH A . 
E 5 HOH   167 467 94  HOH   HOH A . 
E 5 HOH   168 468 222 HOH   HOH A . 
E 5 HOH   169 469 153 HOH   HOH A . 
E 5 HOH   170 470 92  HOH   HOH A . 
E 5 HOH   171 471 274 HOH   HOH A . 
E 5 HOH   172 472 273 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           7I4L 
_cell.length_a           87.993 
_cell.length_b           58.157 
_cell.length_c           32.739 
_cell.angle_alpha        90.00 
_cell.angle_beta         93.17 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I4L 
_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          7I4L 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.63 
_exptl_crystal.density_percent_sol   53.26 
_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   2025-01-17 
_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                     7I4L 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             48.48 
_reflns.d_resolution_high            1.47 
_reflns.number_obs                   27890 
_reflns.percent_possible_obs         99.3 
_reflns.pdbx_Rmerge_I_obs            0.076 
_reflns.pdbx_netI_over_sigmaI        12.7 
_reflns.pdbx_redundancy              6.6 
_reflns.pdbx_Rrim_I_all              0.082 
_reflns.pdbx_Rpim_I_all              0.031 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     184693 
_reflns.pdbx_chi_squared             0.65 
_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                  1.47 
_reflns_shell.d_res_low                   1.49 
_reflns_shell.number_measured_all         6825 
_reflns_shell.number_unique_obs           1340 
_reflns_shell.Rmerge_I_obs                1.831 
_reflns_shell.pdbx_chi_squared            0.14 
_reflns_shell.pdbx_redundancy             5.1 
_reflns_shell.percent_possible_obs        96.1 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.4 
_reflns_shell.pdbx_Rrim_I_all             2.048 
_reflns_shell.pdbx_Rpim_I_all             0.900 
_reflns_shell.pdbx_CC_half                0.251 
_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                                 7I4L 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     27749 
_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                             17.78 
_refine.ls_d_res_high                            1.470 
_refine.ls_percent_reflns_obs                    98.7 
_refine.ls_R_factor_obs                          0.2039 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2024 
_refine.ls_R_factor_R_free                       0.2318 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.070 
_refine.ls_number_reflns_R_free                  1406 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.B_iso_mean                               33.60 
_refine.aniso_B[1][1]                            -3.44540 
_refine.aniso_B[2][2]                            1.07340 
_refine.aniso_B[3][3]                            2.37200 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -2.37910 
_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             0.071 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.073 
_refine.pdbx_overall_SU_R_Blow_DPI               0.075 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.077 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I4L 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1074 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.number_atoms_solvent             172 
_refine_hist.number_atoms_total               1272 
_refine_hist.d_res_high                       1.470 
_refine_hist.d_res_low                        17.78 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  1136 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.00  ? 2.00  1547 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  380  '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  205  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1136 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.31  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           15.42 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  139  '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  1025 'X-RAY DIFFRACTION' SEMIHARMONIC 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   51 
_refine_ls_shell.d_res_high                       1.47 
_refine_ls_shell.d_res_low                        1.48 
_refine_ls_shell.number_reflns_R_work             522 
_refine_ls_shell.R_factor_R_work                  0.3653 
_refine_ls_shell.percent_reflns_obs               86.65 
_refine_ls_shell.R_factor_R_free                  0.3636 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.95 
_refine_ls_shell.number_reflns_R_free             33 
_refine_ls_shell.number_reflns_all                555 
_refine_ls_shell.R_factor_all                     0.3652 
# 
_struct.entry_id                  7I4L 
_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-0036671-001 (A71EV2A-x4712)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I4L 
_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              7I4L 
_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  ? ALA A 23  ? THR A 24  ALA A 29  1 ? 6 
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 ? ? ? ? ? ? ? 2.340 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.403 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.337 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.130 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 110.6 ? 
2 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.5 ? 
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_555 116.7 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 109.5 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 100.0 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 113.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
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 THR A 120 ? N THR A 126 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
# 
_pdbx_entry_details.entry_id                   7I4L 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -101.34 42.14  
2 1 ASN A 30  ? ? -144.00 37.24  
3 1 SER A 125 ? ? -133.38 -30.28 
# 
_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         14.8923 
_pdbx_refine_tls.origin_y         7.6800 
_pdbx_refine_tls.origin_z         14.2832 
_pdbx_refine_tls.T[1][1]          -0.0508 
_pdbx_refine_tls.T[2][2]          -0.0312 
_pdbx_refine_tls.T[3][3]          0.0122 
_pdbx_refine_tls.T[1][2]          -0.0076 
_pdbx_refine_tls.T[1][3]          0.0140 
_pdbx_refine_tls.T[2][3]          -0.0077 
_pdbx_refine_tls.L[1][1]          0.7965 
_pdbx_refine_tls.L[2][2]          5.7932 
_pdbx_refine_tls.L[3][3]          0.3624 
_pdbx_refine_tls.L[1][2]          -0.1363 
_pdbx_refine_tls.L[1][3]          -0.1565 
_pdbx_refine_tls.L[2][3]          0.9738 
_pdbx_refine_tls.S[1][1]          -0.0367 
_pdbx_refine_tls.S[1][2]          0.0209 
_pdbx_refine_tls.S[1][3]          0.1206 
_pdbx_refine_tls.S[2][1]          -0.0467 
_pdbx_refine_tls.S[2][2]          0.1776 
_pdbx_refine_tls.S[2][3]          -0.3801 
_pdbx_refine_tls.S[3][1]          -0.0173 
_pdbx_refine_tls.S[3][2]          -0.0558 
_pdbx_refine_tls.S[3][3]          -0.1409 
# 
_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 
A1B2Z N1   N  N N 1   
A1B2Z C4   C  Y N 2   
A1B2Z C5   C  Y N 3   
A1B2Z C6   C  Y N 4   
A1B2Z C7   C  N N 5   
A1B2Z C8   C  N N 6   
A1B2Z C10  C  N N 7   
A1B2Z C13  C  N N 8   
A1B2Z O1   O  N N 9   
A1B2Z N2   N  N N 10  
A1B2Z C12  C  N S 11  
A1B2Z C11  C  N N 12  
A1B2Z C9   C  N N 13  
A1B2Z C14  C  N N 14  
A1B2Z O    O  N N 15  
A1B2Z N    N  N N 16  
A1B2Z C1   C  Y N 17  
A1B2Z S    S  N N 18  
A1B2Z C    C  N N 19  
A1B2Z C3   C  Y N 20  
A1B2Z C2   C  Y N 21  
A1B2Z H6   H  N N 22  
A1B2Z H7   H  N N 23  
A1B2Z H10  H  N N 24  
A1B2Z H8   H  N N 25  
A1B2Z H9   H  N N 26  
A1B2Z H13  H  N N 27  
A1B2Z H14  H  N N 28  
A1B2Z H18  H  N N 29  
A1B2Z H17  H  N N 30  
A1B2Z H    H  N N 31  
A1B2Z H15  H  N N 32  
A1B2Z H16  H  N N 33  
A1B2Z H11  H  N N 34  
A1B2Z H12  H  N N 35  
A1B2Z H19  H  N N 36  
A1B2Z H20  H  N N 37  
A1B2Z H2   H  N N 38  
A1B2Z H1   H  N N 39  
A1B2Z H3   H  N N 40  
A1B2Z H5   H  N N 41  
A1B2Z H4   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
DMS   S    S  N N 130 
DMS   O    O  N N 131 
DMS   C1   C  N N 132 
DMS   C2   C  N N 133 
DMS   H11  H  N N 134 
DMS   H12  H  N N 135 
DMS   H13  H  N N 136 
DMS   H21  H  N N 137 
DMS   H22  H  N N 138 
DMS   H23  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
HIS   N    N  N N 189 
HIS   CA   C  N S 190 
HIS   C    C  N N 191 
HIS   O    O  N N 192 
HIS   CB   C  N N 193 
HIS   CG   C  Y N 194 
HIS   ND1  N  Y N 195 
HIS   CD2  C  Y N 196 
HIS   CE1  C  Y N 197 
HIS   NE2  N  Y N 198 
HIS   OXT  O  N N 199 
HIS   H    H  N N 200 
HIS   H2   H  N N 201 
HIS   HA   H  N N 202 
HIS   HB2  H  N N 203 
HIS   HB3  H  N N 204 
HIS   HD1  H  N N 205 
HIS   HD2  H  N N 206 
HIS   HE1  H  N N 207 
HIS   HE2  H  N N 208 
HIS   HXT  H  N N 209 
HOH   O    O  N N 210 
HOH   H1   H  N N 211 
HOH   H2   H  N N 212 
ILE   N    N  N N 213 
ILE   CA   C  N S 214 
ILE   C    C  N N 215 
ILE   O    O  N N 216 
ILE   CB   C  N S 217 
ILE   CG1  C  N N 218 
ILE   CG2  C  N N 219 
ILE   CD1  C  N N 220 
ILE   OXT  O  N N 221 
ILE   H    H  N N 222 
ILE   H2   H  N N 223 
ILE   HA   H  N N 224 
ILE   HB   H  N N 225 
ILE   HG12 H  N N 226 
ILE   HG13 H  N N 227 
ILE   HG21 H  N N 228 
ILE   HG22 H  N N 229 
ILE   HG23 H  N N 230 
ILE   HD11 H  N N 231 
ILE   HD12 H  N N 232 
ILE   HD13 H  N N 233 
ILE   HXT  H  N N 234 
LEU   N    N  N N 235 
LEU   CA   C  N S 236 
LEU   C    C  N N 237 
LEU   O    O  N N 238 
LEU   CB   C  N N 239 
LEU   CG   C  N N 240 
LEU   CD1  C  N N 241 
LEU   CD2  C  N N 242 
LEU   OXT  O  N N 243 
LEU   H    H  N N 244 
LEU   H2   H  N N 245 
LEU   HA   H  N N 246 
LEU   HB2  H  N N 247 
LEU   HB3  H  N N 248 
LEU   HG   H  N N 249 
LEU   HD11 H  N N 250 
LEU   HD12 H  N N 251 
LEU   HD13 H  N N 252 
LEU   HD21 H  N N 253 
LEU   HD22 H  N N 254 
LEU   HD23 H  N N 255 
LEU   HXT  H  N N 256 
LYS   N    N  N N 257 
LYS   CA   C  N S 258 
LYS   C    C  N N 259 
LYS   O    O  N N 260 
LYS   CB   C  N N 261 
LYS   CG   C  N N 262 
LYS   CD   C  N N 263 
LYS   CE   C  N N 264 
LYS   NZ   N  N N 265 
LYS   OXT  O  N N 266 
LYS   H    H  N N 267 
LYS   H2   H  N N 268 
LYS   HA   H  N N 269 
LYS   HB2  H  N N 270 
LYS   HB3  H  N N 271 
LYS   HG2  H  N N 272 
LYS   HG3  H  N N 273 
LYS   HD2  H  N N 274 
LYS   HD3  H  N N 275 
LYS   HE2  H  N N 276 
LYS   HE3  H  N N 277 
LYS   HZ1  H  N N 278 
LYS   HZ2  H  N N 279 
LYS   HZ3  H  N N 280 
LYS   HXT  H  N N 281 
MET   N    N  N N 282 
MET   CA   C  N S 283 
MET   C    C  N N 284 
MET   O    O  N N 285 
MET   CB   C  N N 286 
MET   CG   C  N N 287 
MET   SD   S  N N 288 
MET   CE   C  N N 289 
MET   OXT  O  N N 290 
MET   H    H  N N 291 
MET   H2   H  N N 292 
MET   HA   H  N N 293 
MET   HB2  H  N N 294 
MET   HB3  H  N N 295 
MET   HG2  H  N N 296 
MET   HG3  H  N N 297 
MET   HE1  H  N N 298 
MET   HE2  H  N N 299 
MET   HE3  H  N N 300 
MET   HXT  H  N N 301 
PHE   N    N  N N 302 
PHE   CA   C  N S 303 
PHE   C    C  N N 304 
PHE   O    O  N N 305 
PHE   CB   C  N N 306 
PHE   CG   C  Y N 307 
PHE   CD1  C  Y N 308 
PHE   CD2  C  Y N 309 
PHE   CE1  C  Y N 310 
PHE   CE2  C  Y N 311 
PHE   CZ   C  Y N 312 
PHE   OXT  O  N N 313 
PHE   H    H  N N 314 
PHE   H2   H  N N 315 
PHE   HA   H  N N 316 
PHE   HB2  H  N N 317 
PHE   HB3  H  N N 318 
PHE   HD1  H  N N 319 
PHE   HD2  H  N N 320 
PHE   HE1  H  N N 321 
PHE   HE2  H  N N 322 
PHE   HZ   H  N N 323 
PHE   HXT  H  N N 324 
PRO   N    N  N N 325 
PRO   CA   C  N S 326 
PRO   C    C  N N 327 
PRO   O    O  N N 328 
PRO   CB   C  N N 329 
PRO   CG   C  N N 330 
PRO   CD   C  N N 331 
PRO   OXT  O  N N 332 
PRO   H    H  N N 333 
PRO   HA   H  N N 334 
PRO   HB2  H  N N 335 
PRO   HB3  H  N N 336 
PRO   HG2  H  N N 337 
PRO   HG3  H  N N 338 
PRO   HD2  H  N N 339 
PRO   HD3  H  N N 340 
PRO   HXT  H  N N 341 
SER   N    N  N N 342 
SER   CA   C  N S 343 
SER   C    C  N N 344 
SER   O    O  N N 345 
SER   CB   C  N N 346 
SER   OG   O  N N 347 
SER   OXT  O  N N 348 
SER   H    H  N N 349 
SER   H2   H  N N 350 
SER   HA   H  N N 351 
SER   HB2  H  N N 352 
SER   HB3  H  N N 353 
SER   HG   H  N N 354 
SER   HXT  H  N N 355 
THR   N    N  N N 356 
THR   CA   C  N S 357 
THR   C    C  N N 358 
THR   O    O  N N 359 
THR   CB   C  N R 360 
THR   OG1  O  N N 361 
THR   CG2  C  N N 362 
THR   OXT  O  N N 363 
THR   H    H  N N 364 
THR   H2   H  N N 365 
THR   HA   H  N N 366 
THR   HB   H  N N 367 
THR   HG1  H  N N 368 
THR   HG21 H  N N 369 
THR   HG22 H  N N 370 
THR   HG23 H  N N 371 
THR   HXT  H  N N 372 
TRP   N    N  N N 373 
TRP   CA   C  N S 374 
TRP   C    C  N N 375 
TRP   O    O  N N 376 
TRP   CB   C  N N 377 
TRP   CG   C  Y N 378 
TRP   CD1  C  Y N 379 
TRP   CD2  C  Y N 380 
TRP   NE1  N  Y N 381 
TRP   CE2  C  Y N 382 
TRP   CE3  C  Y N 383 
TRP   CZ2  C  Y N 384 
TRP   CZ3  C  Y N 385 
TRP   CH2  C  Y N 386 
TRP   OXT  O  N N 387 
TRP   H    H  N N 388 
TRP   H2   H  N N 389 
TRP   HA   H  N N 390 
TRP   HB2  H  N N 391 
TRP   HB3  H  N N 392 
TRP   HD1  H  N N 393 
TRP   HE1  H  N N 394 
TRP   HE3  H  N N 395 
TRP   HZ2  H  N N 396 
TRP   HZ3  H  N N 397 
TRP   HH2  H  N N 398 
TRP   HXT  H  N N 399 
TYR   N    N  N N 400 
TYR   CA   C  N S 401 
TYR   C    C  N N 402 
TYR   O    O  N N 403 
TYR   CB   C  N N 404 
TYR   CG   C  Y N 405 
TYR   CD1  C  Y N 406 
TYR   CD2  C  Y N 407 
TYR   CE1  C  Y N 408 
TYR   CE2  C  Y N 409 
TYR   CZ   C  Y N 410 
TYR   OH   O  N N 411 
TYR   OXT  O  N N 412 
TYR   H    H  N N 413 
TYR   H2   H  N N 414 
TYR   HA   H  N N 415 
TYR   HB2  H  N N 416 
TYR   HB3  H  N N 417 
TYR   HD1  H  N N 418 
TYR   HD2  H  N N 419 
TYR   HE1  H  N N 420 
TYR   HE2  H  N N 421 
TYR   HH   H  N N 422 
TYR   HXT  H  N N 423 
VAL   N    N  N N 424 
VAL   CA   C  N S 425 
VAL   C    C  N N 426 
VAL   O    O  N N 427 
VAL   CB   C  N N 428 
VAL   CG1  C  N N 429 
VAL   CG2  C  N N 430 
VAL   OXT  O  N N 431 
VAL   H    H  N N 432 
VAL   H2   H  N N 433 
VAL   HA   H  N N 434 
VAL   HB   H  N N 435 
VAL   HG11 H  N N 436 
VAL   HG12 H  N N 437 
VAL   HG13 H  N N 438 
VAL   HG21 H  N N 439 
VAL   HG22 H  N N 440 
VAL   HG23 H  N N 441 
VAL   HXT  H  N N 442 
ZN    ZN   ZN N N 443 
# 
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 
A1B2Z C   S    sing N N 1   
A1B2Z S   C1   sing N N 2   
A1B2Z C1  C2   doub Y N 3   
A1B2Z C2  C3   sing Y N 4   
A1B2Z C3  C4   doub Y N 5   
A1B2Z C4  C5   sing Y N 6   
A1B2Z C5  C6   doub Y N 7   
A1B2Z C1  C6   sing Y N 8   
A1B2Z C6  N    sing N N 9   
A1B2Z C7  N    sing N N 10  
A1B2Z N   C8   sing N N 11  
A1B2Z O   C8   doub N N 12  
A1B2Z C8  N1   sing N N 13  
A1B2Z N1  C9   sing N N 14  
A1B2Z C9  C10  sing N N 15  
A1B2Z C10 C11  sing N N 16  
A1B2Z C11 C12  sing N N 17  
A1B2Z C12 C13  sing N N 18  
A1B2Z N2  C13  sing N N 19  
A1B2Z C13 O1   doub N N 20  
A1B2Z C14 C12  sing N N 21  
A1B2Z N1  C14  sing N N 22  
A1B2Z C4  H6   sing N N 23  
A1B2Z C5  H7   sing N N 24  
A1B2Z C7  H10  sing N N 25  
A1B2Z C7  H8   sing N N 26  
A1B2Z C7  H9   sing N N 27  
A1B2Z C10 H13  sing N N 28  
A1B2Z C10 H14  sing N N 29  
A1B2Z N2  H18  sing N N 30  
A1B2Z N2  H17  sing N N 31  
A1B2Z C12 H    sing N N 32  
A1B2Z C11 H15  sing N N 33  
A1B2Z C11 H16  sing N N 34  
A1B2Z C9  H11  sing N N 35  
A1B2Z C9  H12  sing N N 36  
A1B2Z C14 H19  sing N N 37  
A1B2Z C14 H20  sing N N 38  
A1B2Z C   H2   sing N N 39  
A1B2Z C   H1   sing N N 40  
A1B2Z C   H3   sing N N 41  
A1B2Z C3  H5   sing N N 42  
A1B2Z C2  H4   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
DMS   S   O    doub N N 126 
DMS   S   C1   sing N N 127 
DMS   S   C2   sing N N 128 
DMS   C1  H11  sing N N 129 
DMS   C1  H12  sing N N 130 
DMS   C1  H13  sing N N 131 
DMS   C2  H21  sing N N 132 
DMS   C2  H22  sing N N 133 
DMS   C2  H23  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_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                    7I4L 
_atom_sites.fract_transf_matrix[1][1]   0.011365 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000629 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017195 
_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]   0.030591 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 18.643 7.157   24.203 1.00 32.13 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.902 7.227   23.470 1.00 32.52 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.008 6.067   22.447 1.00 31.97 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.320 5.041   22.579 1.00 31.48 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.081 7.186   24.444 1.00 36.76 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.090 5.924   25.089 1.00 41.10 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.855 6.252   21.436 1.00 30.98 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.053 5.246   20.403 1.00 30.31 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.374 5.802   19.027 1.00 29.79 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.954 6.913   18.679 1.00 29.22 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.045 5.001   18.202 1.00 28.69 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.412 5.415   16.860 1.00 29.02 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.374 4.252   15.856 1.00 28.70 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.414 3.070   16.259 1.00 30.56 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.829 6.030   16.889 1.00 29.71 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.353 4.574   14.549 1.00 26.99 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.500 3.616   13.449 1.00 26.51 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.942 3.795   12.915 1.00 28.44 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.367 4.928   12.715 1.00 28.75 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.491 3.870   12.302 1.00 25.57 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.030 3.885   12.823 1.00 25.09 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.642 2.815   11.198 1.00 25.37 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.039 4.473   11.801 1.00 24.23 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.664 2.692   12.656 1.00 29.77 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.038 2.746   12.142 1.00 31.98 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.063 1.984   10.806 1.00 32.88 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.033 0.758   10.796 1.00 34.47 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.022 2.125   13.170 1.00 32.50 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.142 2.951   14.438 1.00 34.22 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.898 4.122   14.467 1.00 34.99 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.446 2.599   15.590 1.00 35.46 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.943 4.925   15.602 1.00 35.98 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.506 3.379   16.737 1.00 36.88 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.261 4.541   16.740 1.00 37.38 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.325 5.308   17.878 1.00 39.87 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.016 2.714   9.676  1.00 33.12 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.980 2.136   8.324  1.00 32.69 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.129 2.742   7.506  1.00 34.68 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.233 3.967   7.430  1.00 34.91 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.614 2.342   7.619  1.00 33.81 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.167 3.812   7.616  1.00 33.58 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.612 1.737   6.208  1.00 34.48 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.039 1.908   6.985  1.00 36.06 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.202 2.425   6.257  1.00 37.70 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.023 3.365   7.120  1.00 40.87 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.267 3.055   8.290  1.00 42.22 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.395 4.556   6.592  1.00 40.77 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.108 5.512   7.404  1.00 41.69 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.144 6.607   7.892  1.00 40.50 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.499 7.780   7.940  1.00 40.69 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.329 6.058   6.666  1.00 45.53 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.360 4.972   6.500  1.00 51.98 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.226 4.779   7.357  1.00 56.30 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.281 4.204   5.419  1.00 52.17 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 28.931 6.197   8.310  1.00 38.94 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 27.914 7.138   8.812  1.00 38.30 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.369 6.733   10.198 1.00 35.46 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.272 5.543   10.497 1.00 36.02 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.729 7.215   7.831  1.00 39.43 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.076 7.763   6.465  1.00 41.45 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 27.670 9.011   6.325  1.00 42.94 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 26.764 7.057   5.309  1.00 42.62 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 27.936 9.547   5.073  1.00 44.70 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.048 7.574   4.050  1.00 44.56 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 27.643 8.817   3.937  1.00 46.29 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 27.965 9.354   2.708  1.00 49.83 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.057 7.731   11.038 1.00 33.92 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.433 7.575   12.353 1.00 32.61 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.132 8.385   12.250 1.00 31.11 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.179 9.572   11.963 1.00 31.66 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.330 8.142   13.481 1.00 33.89 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.617 8.336   14.822 1.00 36.76 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.616 8.681   15.922 1.00 39.75 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.105 9.667   16.886 1.00 41.42 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.592 9.359   18.075 1.00 44.42 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.461 8.087   18.442 1.00 44.03 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.183 10.320  18.897 1.00 44.97 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.979 7.736   12.400 1.00 28.92 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.685 8.416   12.311 1.00 27.51 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.109 8.513   13.711 1.00 26.79 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.923 7.475   14.352 1.00 26.12 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.693 7.638   11.418 1.00 27.72 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.370 8.396   11.298 1.00 27.24 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.307 7.321   10.033 1.00 27.93 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.875 9.720   14.194 1.00 25.46 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.339 9.919   15.539 1.00 25.71 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.154 10.888  15.485 1.00 24.18 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.937 11.586  14.483 1.00 23.95 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.445 10.513  16.470 1.00 28.16 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.585 9.526   16.664 1.00 30.84 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.954 11.852  15.910 1.00 29.10 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.392 10.983  16.601 1.00 22.82 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.374 12.024  16.718 1.00 21.93 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.107 13.382  16.742 1.00 23.21 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.040 13.556  17.538 1.00 23.68 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.622 11.903  18.059 1.00 22.41 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.806 10.636  18.161 1.00 22.76 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.265 9.600   18.700 1.00 23.23 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.579 10.682  17.628 1.00 22.20 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.675 14.349  15.939 1.00 22.27 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.370 15.658  15.918 1.00 23.30 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.406 16.297  17.316 1.00 24.93 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.440 16.836  17.718 1.00 26.96 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.696 16.597  14.924 1.00 23.89 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.458 17.902  14.623 1.00 25.24 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.493 18.799  13.878 1.00 27.07 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.083 20.049  13.368 1.00 29.83 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.129 21.188  14.055 1.00 32.65 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.701 21.234  15.314 1.00 31.44 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.602 22.296  13.487 1.00 34.79 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.305 16.166  18.092 1.00 24.78 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.250 16.792  19.422 1.00 24.34 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.220 16.163  20.450 1.00 27.66 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 19.476 16.780  21.484 1.00 29.11 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.806 16.866  19.963 1.00 24.43 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.258 15.569  20.457 1.00 24.66 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.649 14.664  19.594 1.00 25.06 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.221 15.069  21.715 1.00 26.03 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.254 13.651  20.357 1.00 26.49 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.601 13.834  21.637 1.00 26.63 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.747 14.967  20.172 1.00 27.76 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.702 14.289  21.056 1.00 29.90 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.139 14.289  20.479 1.00 32.50 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.012 13.625  21.044 1.00 34.55 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.249 12.835  21.305 1.00 29.14 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.923 12.707  22.062 1.00 30.75 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 18.583 11.239  22.307 1.00 29.83 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.966 13.476  23.410 1.00 31.25 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.377 14.951  19.330 1.00 33.48 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.709 14.937  18.711 1.00 35.68 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.728 15.595  19.675 1.00 38.56 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.396 16.614  20.280 1.00 38.70 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.665 15.675  17.383 1.00 35.97 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.854 14.894  19.936 1.00 40.83 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.906 15.327  20.862 1.00 43.83 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.778 16.405  20.197 1.00 45.68 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.564 16.760  19.023 1.00 45.79 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.770 14.108  21.307 1.00 46.01 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.596 13.687  20.217 1.00 48.04 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.956 12.945  21.867 1.00 46.91 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.756 16.965  20.956 1.00 46.93 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.654 17.922  20.380 1.00 48.08 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.522 17.255  19.266 1.00 48.00 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.724 17.864  18.225 1.00 48.64 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.519 18.561  21.455 1.00 50.09 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.255 19.702  20.883 1.00 55.87 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 30.591 20.847  20.479 1.00 58.94 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 32.558 19.797  20.544 1.00 57.39 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 31.528 21.637  19.984 1.00 59.57 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 32.728 21.039  19.994 1.00 58.89 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.981 16.018  19.455 1.00 48.56 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.762 15.330  18.409 1.00 49.16 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.965 15.239  17.059 1.00 48.91 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.555 15.424  15.992 1.00 49.97 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.185 13.945  18.876 1.00 52.00 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.318 13.379  18.061 1.00 58.33 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.437 13.912  18.076 1.00 61.33 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.058 12.288  17.334 1.00 58.63 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.619 14.989  17.120 1.00 46.47 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.724 14.919  15.937 1.00 43.64 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.677 16.197  15.085 1.00 41.93 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.724 16.105  13.852 1.00 41.44 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.278 14.591  16.352 1.00 41.63 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.150 13.177  16.810 1.00 40.85 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.797 12.295  16.194 1.00 41.25 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.472 12.951  17.822 1.00 40.13 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.479 17.372  15.716 1.00 41.44 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.449 18.612  14.947 1.00 43.18 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.824 18.938  14.338 1.00 45.48 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.877 19.499  13.239 1.00 45.88 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 27.961 19.771  15.798 1.00 42.71 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.474 19.754  15.996 1.00 41.95 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.803 19.366  17.115 1.00 42.66 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.479 20.201  15.062 1.00 41.46 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.444 19.509  16.926 1.00 42.23 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.220 20.047  15.684 1.00 41.66 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.525 20.701  13.753 1.00 41.40 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.018 20.360  15.033 1.00 41.49 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.338 21.053  13.130 1.00 41.56 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.099 20.834  13.752 1.00 41.48 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.918 18.501  14.996 1.00 46.31 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.248 18.749  14.458 1.00 48.80 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.591 17.833  13.296 1.00 50.15 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.710 17.938  12.813 1.00 51.07 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.298 18.610  15.554 1.00 49.64 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.669 16.901  12.872 1.00 49.71 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 31.912 15.945  11.792 1.00 49.89 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.605 15.723  10.985 1.00 47.60 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.333 14.605  10.556 1.00 47.37 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.360 14.598  12.404 1.00 52.94 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.761 14.574  12.980 1.00 59.54 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 34.753 14.423  12.256 1.00 61.52 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.876 14.683  14.303 1.00 60.86 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 29.811 16.781  10.790 1.00 45.28 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.500 16.760  10.119 1.00 43.20 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.512 16.392  8.626  1.00 42.41 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.364 16.879  7.876  1.00 42.37 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 27.795 18.127  10.310 1.00 41.42 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.420 18.310  9.643  1.00 40.97 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.349 17.418  10.318 1.00 40.66 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 25.937 19.768  9.743  1.00 40.63 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.539 15.529  8.207  1.00 40.67 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.293 15.125  6.824  1.00 39.87 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 25.962 15.762  6.336  1.00 40.33 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 25.923 16.430  5.297  1.00 42.33 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.283 13.583  6.645  1.00 40.73 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 26.974 13.209  5.202  1.00 41.28 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.605 12.973  7.090  1.00 41.61 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 24.871 15.602  7.130  1.00 37.82 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.572 16.135  6.768  1.00 36.55 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.690 16.189  8.031  1.00 34.56 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 22.826 15.357  8.928  1.00 33.97 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 22.925 15.257  5.669  1.00 36.64 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.442 15.430  5.447  1.00 37.03 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 20.839 16.279  4.565  1.00 38.58 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.379 14.702  6.095  1.00 35.91 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.469 16.128  4.622  1.00 38.78 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.162 15.150  5.536  1.00 37.07 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.342 13.686  7.056  1.00 35.64 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 17.925 14.625  5.917  1.00 36.35 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.114 13.157  7.418  1.00 35.06 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 17.927 13.639  6.866  1.00 35.39 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 21.839 17.182  8.112  1.00 32.83 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 20.901 17.305  9.227  1.00 31.96 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.615 17.921  8.744  1.00 31.88 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.633 18.768  7.833  1.00 33.69 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.512 18.030  10.441 1.00 32.89 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.053 19.442  10.175 1.00 35.03 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.037 20.564  10.106 1.00 38.43 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.353 21.585  9.446  1.00 36.89 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 19.929 20.428  10.689 1.00 35.35 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.480 17.501  9.328  1.00 30.04 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.210 18.083  8.975  1.00 28.81 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.429 18.228  10.295 1.00 26.80 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.015 17.219  10.887 1.00 25.42 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.493 17.259  7.886  1.00 30.41 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.184 17.840  7.349  1.00 35.52 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.590 18.695  8.029  1.00 37.88 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 14.748 17.420  6.246  1.00 38.47 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.268 19.477  10.777 1.00 25.75 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.545 19.754  12.010 0.50 24.90 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.551 19.687  12.039 0.50 25.27 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.089 19.239  11.906 1.00 24.75 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.537 18.689  12.864 1.00 25.23 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.551 21.262  12.266 0.50 25.85 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.618 21.145  12.489 0.50 27.34 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.739 21.600  13.371 0.50 27.11 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 14.855 21.953  11.614 0.50 30.01 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.469 19.432  10.724 1.00 24.57 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.078 19.009  10.555 1.00 24.89 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 11.890 17.475  10.661 1.00 23.51 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 10.773 17.036  10.880 1.00 24.46 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.480 19.539  9.258  1.00 28.49 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 11.857 18.722  8.159  1.00 34.64 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 12.962 16.689  10.484 1.00 22.40 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 12.907 15.217  10.632 1.00 21.87 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.533 14.728  11.972 1.00 21.70 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.527 13.518  12.248 1.00 20.97 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.708 14.559  9.486  1.00 23.19 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.067 14.750  8.153  1.00 25.70 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 13.927 14.122  7.090  1.00 25.72 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 13.843 12.657  7.164  1.00 23.99 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 13.909 11.865  6.093  1.00 26.21 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.063 12.389  4.871  1.00 27.74 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 13.830 10.544  6.231  1.00 27.42 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.115 15.648  12.789 1.00 21.81 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.854 15.253  14.004 1.00 21.13 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.008 14.289  13.695 1.00 21.92 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.319 13.428  14.527 1.00 21.44 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.945 14.656  15.133 1.00 21.16 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.703 14.369  16.434 1.00 22.02 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.537 15.220  16.843 1.00 21.80 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.450 13.306  17.063 1.00 21.41 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.703 14.441  12.521 1.00 21.85 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.807 13.535  12.190 1.00 22.89 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.122 14.317  11.986 1.00 24.07 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.114 15.439  11.501 1.00 25.46 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.537 12.761  10.873 1.00 23.29 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.505 11.607  10.946 1.00 23.90 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.302 10.961  9.566  1.00 24.19 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.908 10.550  12.012 1.00 23.90 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.219 13.675  12.310 1.00 23.99 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.578 14.201  12.061 1.00 26.31 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.441 13.028  11.739 1.00 28.22 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.358 11.999  12.421 1.00 27.64 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.117 14.968  13.285 1.00 27.40 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.524 15.665  13.127 1.00 29.57 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.547 17.006  13.864 1.00 30.55 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.660 14.740  13.618 1.00 30.83 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.257 13.161  10.662 1.00 29.27 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.180 12.123  10.217 1.00 32.16 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.588 12.707  10.307 1.00 34.89 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 25.820 13.837  9.849  1.00 35.24 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 23.845 11.630  8.784  1.00 33.15 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 24.906 10.644  8.262  1.00 34.59 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.436 10.996  8.741  1.00 32.62 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.485 11.995  10.992 1.00 36.39 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 27.889 12.418  11.096 1.00 38.42 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.798 11.342  10.488 1.00 40.72 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.375 10.209  10.268 1.00 39.94 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.268 12.756  12.538 1.00 38.98 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.141 11.654  13.421 1.00 39.54 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.035 11.723  10.129 1.00 43.15 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 30.971 10.781  9.514  1.00 45.18 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.701 9.986   10.587 1.00 47.19 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 31.955 10.510  11.668 1.00 47.99 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.014 11.551  8.701  1.00 47.24 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.651 12.507  9.533  1.00 49.97 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.090 8.741   10.288 1.00 48.54 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.833 7.927   11.244 1.00 50.89 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.152 7.463   10.615 1.00 54.70 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.234 7.278   9.393  1.00 55.27 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.011 6.707   11.726 1.00 51.83 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.972 5.718   10.708 1.00 52.40 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.594 7.075   12.150 1.00 51.45 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.126 7.147   11.459 1.00 57.24 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.406 6.630   10.968 1.00 60.29 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.311 5.150   10.626 1.00 61.12 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.917 4.691   9.652  1.00 62.68 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.504 6.903   11.999 1.00 63.98 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.163 6.213   13.206 1.00 66.99 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.693 8.381   12.270 1.00 64.33 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.556 4.388   11.422 1.00 59.47 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.410 2.956   11.200 1.00 58.48 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.100 2.616   10.497 1.00 56.25 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.121 3.337   10.645 1.00 55.85 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.518 2.211   12.519 1.00 58.99 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.085 1.525   9.724  1.00 54.34 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.883 1.125   8.997  1.00 52.82 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.881 0.381   9.903  1.00 48.77 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.277 -0.507  10.655 1.00 48.75 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.259 0.274   7.771  1.00 56.55 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 32.359 0.532   6.567  1.00 62.68 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 32.574 -0.446  5.441  1.00 69.17 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 33.660 -0.520  4.847  1.00 71.38 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 31.532 -1.198  5.104  1.00 69.80 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.599 0.737   9.783  1.00 45.20 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.490 0.171   10.538 1.00 42.39 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.826 -0.983  9.822  1.00 39.22 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.072 -1.207  8.634  1.00 40.50 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.021 -1.768  10.547 1.00 35.81 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.464 -2.994  9.984  1.00 34.46 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.941 -3.053  9.888  1.00 32.47 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.414 -4.126  9.592  1.00 33.30 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.998 -4.199  10.748 1.00 35.62 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 29.800 -4.265  10.826 1.00 40.72 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.234 -1.945  10.161 1.00 31.23 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.778 -1.968  10.046 1.00 31.35 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.392 -1.907  8.543  1.00 31.75 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.072 -1.250  7.732  1.00 32.57 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.158 -0.791  10.858 1.00 31.60 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.361 -0.952  12.368 1.00 34.42 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.416 -2.113  12.837 1.00 35.91 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.438 0.093   13.091 1.00 33.44 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.349 -2.624  8.178  1.00 30.62 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.784 -2.570  6.833  1.00 31.47 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.480 -1.763  6.952  1.00 29.83 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.677 -2.072  7.827  1.00 29.14 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.455 -3.980  6.330  1.00 35.79 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.671 -4.638  5.972  1.00 37.87 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.512 -3.975  5.102  1.00 37.23 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.279 -0.770  6.079  1.00 29.51 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.058 0.015   6.037  1.00 28.55 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.038 -0.756  5.183  1.00 28.50 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.379 -1.286  4.109  1.00 29.50 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.295 1.415   5.424  1.00 29.27 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.465 2.161   6.116  1.00 30.33 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.003 2.241   5.494  1.00 29.01 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.274 2.331   7.651  1.00 30.22 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.799 -0.853  5.677  1.00 26.01 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.717 -1.494  4.953  1.00 25.01 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.336 -0.638  3.753  1.00 25.27 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.322 0.589   3.857  1.00 25.06 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.501 -1.595  5.882  1.00 24.85 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.004 -1.273  2.614  1.00 25.63 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.501 -0.537  1.450  1.00 26.84 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.186 -1.254  1.082  1.00 28.03 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.184 -2.251  0.331  1.00 28.99 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.501 -0.510  0.279  1.00 28.80 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 16.875 0.069   0.614  1.00 31.80 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 16.882 1.530   1.068  1.00 33.81 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.233 1.957   1.455  1.00 35.11 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.505 3.089   2.099  1.00 37.25 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.531 3.934   2.413  1.00 35.59 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 19.751 3.382   2.439  1.00 38.76 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.070 -0.780  1.685  1.00 28.40 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.770 -1.465  1.640  1.00 28.04 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.618  -0.512  2.070  1.00 27.71 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 9.872  0.616   2.478  1.00 27.21 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.846 -2.639  2.619  1.00 27.34 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.007 -2.088  4.349  1.00 24.31 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.354  -1.030  2.071  1.00 27.77 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.210  -0.301  2.598  1.00 28.22 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.581  -1.114  3.746  1.00 27.20 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.374  -0.984  3.973  1.00 27.90 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.141  -0.007  1.522  1.00 32.33 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.499  -1.219  0.875  1.00 40.81 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.808  -2.358  1.297  1.00 42.03 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.672  -1.031  -0.049 1.00 45.75 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.395  -1.897  4.523  1.00 25.59 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.852  -2.644  5.681  1.00 23.89 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.145  -1.700  6.632  1.00 23.35 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.573  -0.552  6.828  1.00 23.09 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 7.960  -3.368  6.443  1.00 23.72 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.581  -4.860  5.624  1.00 25.84 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.115  -2.230  7.286  1.00 22.38 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.408  -1.516  8.344  1.00 23.02 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.347  -2.351  9.627  1.00 23.80 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.547  -2.051  10.509 1.00 23.96 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 2.985  -1.113  7.924  1.00 25.02 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 2.930  0.177   7.171  1.00 27.43 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.499  0.587   6.887  1.00 31.23 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 0.972  0.321   5.785  1.00 32.28 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.824  1.211   7.891  1.00 29.29 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.139  -3.440  9.714  1.00 22.07 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.267  -4.228  10.939 1.00 21.92 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.773  -4.413  11.176 1.00 21.65 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.586  -4.501  10.225 1.00 21.93 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.498  -5.566  10.891 1.00 24.67 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.117  -6.385  9.915  1.00 27.05 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.021  -5.390  10.526 1.00 24.62 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.146  -4.412  12.451 1.00 21.07 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.557  -4.509  12.826 1.00 19.35 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.707  -4.693  14.325 1.00 18.83 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.757  -5.092  15.000 1.00 20.56 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 9.924  -4.515  14.806 1.00 18.24 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.228 -4.696  16.225 1.00 19.53 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.063 -3.495  16.643 1.00 19.65 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.001 -3.157  15.934 1.00 19.86 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.041 -5.993  16.451 1.00 22.05 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.540 -6.068  17.900 1.00 23.06 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.203 -7.220  16.122 1.00 22.83 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 10.716 -2.839  17.766 1.00 19.65 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.567 -1.726  18.233 1.00 18.98 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.146 -1.993  19.594 1.00 19.99 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.516 -2.687  20.397 1.00 20.95 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 10.842 -0.365  18.214 1.00 18.20 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 9.894  -0.136  19.371 1.00 19.33 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.637  -0.742  19.400 1.00 20.72 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.216 0.749   20.398 1.00 19.42 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 7.731  -0.484  20.430 1.00 21.31 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.298  1.045   21.410 1.00 21.02 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.071  0.401   21.444 1.00 22.02 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.170  0.646   22.464 1.00 23.94 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.282 -1.325  19.902 1.00 19.71 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 13.889 -1.442  21.223 1.00 21.61 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.392 -0.310  22.118 1.00 21.82 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.529 0.864   21.740 1.00 22.27 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.408 -1.427  21.191 1.00 22.27 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 15.984 -1.570  22.589 1.00 24.49 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 15.717 -2.696  23.359 1.00 25.98 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 16.699 -0.537  23.176 1.00 26.75 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.199 -2.814  24.665 1.00 27.62 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.206 -0.650  24.471 1.00 28.42 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 16.938 -1.785  25.215 1.00 29.80 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.422 -1.907  26.504 1.00 33.07 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 12.875 -0.671  23.315 1.00 21.99 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.358 0.296   24.299 1.00 23.20 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.273 0.282   25.544 1.00 25.87 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.176 -0.644  26.368 1.00 27.21 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 10.921 -0.061  24.671 1.00 25.85 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.221 0.968   25.997 1.00 28.21 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.173 1.270   25.665 1.00 26.14 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.136 1.261   26.764 1.00 28.98 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.483 1.370   28.155 1.00 30.04 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 14.966 0.748   29.118 1.00 31.15 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.214 2.322   26.570 1.00 32.24 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 15.700 3.628   26.733 1.00 36.47 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.352 2.095   28.243 1.00 28.91 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 12.593 2.270   29.502 1.00 29.08 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 11.894 0.997   29.998 1.00 30.62 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.394 0.970   31.134 1.00 34.14 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 11.602 3.424   29.396 1.00 29.12 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.574 3.184   28.456 1.00 30.84 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 11.904 -0.066  29.182 1.00 29.93 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.390 -1.360  29.614 1.00 31.07 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.446 -2.454  29.477 1.00 32.28 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.138 -3.602  29.807 1.00 33.16 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.158 -1.740  28.781 1.00 29.66 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 8.940  -0.837  29.037 1.00 31.06 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.333  -1.123  30.406 1.00 32.82 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.151  -0.304  30.685 1.00 35.18 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.185  0.859   31.335 1.00 37.01 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.342  1.365   31.745 1.00 35.08 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.065  1.536   31.559 1.00 38.29 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 13.642 -2.153  28.879 1.00 32.12 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 14.683 -3.137  28.542 1.00 32.53 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.061 -4.268  27.706 1.00 32.17 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.332 -5.450  27.955 1.00 33.81 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.357 -3.706  29.810 1.00 34.51 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.199 -2.665  30.525 1.00 38.44 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.017 -3.323  31.613 1.00 42.64 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 17.706 -2.326  32.427 1.00 46.72 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.532 -2.174  33.738 1.00 49.39 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 16.708 -2.978  34.404 1.00 48.16 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.179 -1.217  34.393 1.00 50.85 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.153 -3.904  26.764 1.00 30.56 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.456 -4.911  25.971 1.00 29.03 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.306 -4.503  24.513 1.00 27.30 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.199 -3.321  24.201 1.00 28.10 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.032 -5.121  26.517 1.00 33.22 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 10.926 -6.009  27.736 1.00 42.49 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.795  -7.023  27.535 1.00 50.43 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.441  -7.720  28.826 1.00 56.45 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 9.296  -6.757  29.962 1.00 60.18 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.277 -5.490  23.618 1.00 25.63 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.024 -5.279  22.207 1.00 25.36 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.557 -5.637  22.024 1.00 26.95 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.100 -6.681  22.538 1.00 29.52 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.919 -6.171  21.308 1.00 23.73 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.387 -5.923  21.467 1.00 25.21 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.107 -5.189  20.532 1.00 26.19 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.219 -6.296  22.467 1.00 26.37 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.350 -5.160  20.977 1.00 26.55 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.455 -5.775  22.163 1.00 27.92 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.789  -4.772  21.344 1.00 24.81 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.363  -5.031  21.177 1.00 24.09 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.004  -5.119  19.702 1.00 23.27 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.367  -4.234  18.929 1.00 21.18 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.517  -3.897  21.753 1.00 24.86 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.533  -3.787  23.254 1.00 26.78 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 6.773  -4.645  24.040 1.00 28.34 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.219  -2.762  23.885 1.00 27.64 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 6.747  -4.525  25.428 1.00 29.60 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.190  -2.619  25.275 1.00 29.17 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.435  -3.491  26.041 1.00 30.91 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.414  -3.391  27.429 1.00 33.16 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.184  -6.111  19.347 1.00 23.99 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.647  -6.150  17.980 1.00 24.47 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.548  -5.071  17.821 1.00 25.93 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.707  -4.916  18.723 1.00 27.27 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.082  -7.588  17.868 1.00 25.59 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.775  -7.995  19.272 1.00 27.27 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.644  -7.204  20.209 1.00 24.44 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.576  -4.291  16.720 1.00 24.61 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.574  -3.261  16.481 1.00 25.48 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.151  -3.151  15.026 1.00 24.82 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.949  -3.478  14.105 1.00 23.91 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.103  -1.879  16.939 1.00 27.31 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.136  -1.766  18.449 1.00 29.28 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.450  -1.531  16.279 1.00 26.74 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.926  -2.569  14.819 1.00 22.80 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.399  -2.137  13.525 1.00 22.18 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.611  -0.613  13.552 1.00 22.52 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.381  0.026   14.590 1.00 24.50 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 0.901  -2.408  13.397 1.00 25.22 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.609  -3.799  13.355 1.00 33.51 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.035  -0.030  12.436 1.00 21.04 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.327  1.404   12.401 1.00 20.63 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.836  2.068   11.136 1.00 22.43 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.677  1.407   10.116 1.00 23.70 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.818  1.700   12.687 1.00 20.18 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.793  0.966   11.794 1.00 20.01 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.268  -0.291  12.140 1.00 19.05 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.267  1.551   10.626 1.00 21.14 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.158  -0.968  11.308 1.00 20.57 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.169  0.869   9.800  1.00 21.13 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.627  -0.373  10.158 1.00 20.02 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.486  3.360   11.232 1.00 21.77 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 1.935  4.077   10.111 1.00 22.96 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 2.992  4.404   9.030  1.00 23.50 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.187  4.190   9.231  1.00 23.07 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.209  5.341   10.605 1.00 24.61 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.112  6.248   11.215 1.00 25.68 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.539  4.880   7.844  1.00 24.10 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.491  5.247   6.795  1.00 25.88 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.122  6.608   7.145  1.00 25.38 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.482  7.408   7.823  1.00 26.11 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 2.799  5.329   5.407  1.00 29.55 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.742  3.922   4.769  1.00 35.41 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.338  3.868   3.281  1.00 42.33 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.712  2.496   2.734  1.00 46.73 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.928  2.097   1.524  1.00 50.74 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.365  6.875   6.703  1.00 25.43 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.009  8.177   7.035  1.00 25.35 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.144  9.361   6.611  1.00 25.09 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.670  9.424   5.460  1.00 26.42 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.333  8.121   6.280  1.00 27.12 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.612  6.619   6.124  1.00 28.77 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.247  6.046   5.854  1.00 25.39 ? 79  PRO   A CD  1 
ATOM   581  N  N   A SER   A 1 74  ? 4.900  10.273  7.563  0.50 24.33 ? 80  SER   A N   1 
ATOM   582  N  N   B SER   A 1 74  ? 4.892  10.287  7.537  0.50 24.44 ? 80  SER   A N   1 
ATOM   583  C  CA  A SER   A 1 74  ? 3.949  11.367  7.403  0.50 25.28 ? 80  SER   A CA  1 
ATOM   584  C  CA  B SER   A 1 74  ? 4.021  11.426  7.253  0.50 25.52 ? 80  SER   A CA  1 
ATOM   585  C  C   A SER   A 1 74  ? 4.384  12.657  8.128  0.50 25.54 ? 80  SER   A C   1 
ATOM   586  C  C   B SER   A 1 74  ? 4.392  12.668  8.084  0.50 25.64 ? 80  SER   A C   1 
ATOM   587  O  O   A SER   A 1 74  ? 5.291  12.623  8.962  0.50 25.09 ? 80  SER   A O   1 
ATOM   588  O  O   B SER   A 1 74  ? 5.303  12.617  8.912  0.50 25.21 ? 80  SER   A O   1 
ATOM   589  C  CB  A SER   A 1 74  ? 2.602  10.922  7.994  0.50 27.10 ? 80  SER   A CB  1 
ATOM   590  C  CB  B SER   A 1 74  ? 2.554  11.032  7.463  0.50 27.98 ? 80  SER   A CB  1 
ATOM   591  O  OG  A SER   A 1 74  ? 2.242  9.602   7.615  0.50 30.66 ? 80  SER   A OG  1 
ATOM   592  O  OG  B SER   A 1 74  ? 2.170  10.022  6.544  0.50 32.04 ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 3.696  13.788  7.841  1.00 26.28 ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 3.927  15.055  8.525  1.00 27.80 ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 2.952  15.021  9.730  1.00 28.44 ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 1.721  14.984  9.550  1.00 29.18 ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 3.556  16.181  7.530  1.00 29.40 ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 3.978  17.613  7.801  1.00 33.31 ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.462  17.743  7.851  1.00 33.69 ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 3.409  18.551  6.691  1.00 34.48 ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.493  14.989  10.954 1.00 27.60 ? 82  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 76  ? 2.701  14.826  12.169 1.00 28.90 ? 82  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 76  ? 3.007  15.922  13.188 1.00 30.22 ? 82  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 76  ? 4.176  16.289  13.362 1.00 28.72 ? 82  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 76  ? 2.969  13.400  12.749 1.00 29.79 ? 82  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 76  ? 2.451  12.315  11.774 1.00 31.67 ? 82  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 76  ? 2.386  13.216  14.177 1.00 30.36 ? 82  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 76  ? 2.819  10.944  12.140 1.00 34.23 ? 82  ILE   A CD1 1 
ATOM   609  N  N   . PHE   A 1 77  ? 1.943  16.475  13.833 1.00 31.78 ? 83  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 77  ? 2.107  17.524  14.838 1.00 33.15 ? 83  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 77  ? 2.806  16.975  16.047 1.00 31.96 ? 83  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 77  ? 2.372  15.974  16.616 1.00 33.67 ? 83  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 77  ? 0.744  18.085  15.303 1.00 35.15 ? 83  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 77  ? 0.852  19.113  16.422 1.00 37.52 ? 83  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 77  ? 1.145  20.437  16.141 1.00 37.71 ? 83  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 77  ? 0.714  18.735  17.753 1.00 38.89 ? 83  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 77  ? 1.258  21.376  17.162 1.00 38.65 ? 83  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 77  ? 0.814  19.679  18.774 1.00 40.32 ? 83  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 77  ? 1.123  20.986  18.468 1.00 39.43 ? 83  PHE   A CZ  1 
ATOM   620  N  N   . VAL   A 1 78  ? 3.857  17.669  16.486 1.00 29.34 ? 84  VAL   A N   1 
ATOM   621  C  CA  . VAL   A 1 78  ? 4.571  17.284  17.681 1.00 27.65 ? 84  VAL   A CA  1 
ATOM   622  C  C   . VAL   A 1 78  ? 4.559  18.484  18.627 1.00 28.01 ? 84  VAL   A C   1 
ATOM   623  O  O   . VAL   A 1 78  ? 4.994  19.584  18.252 1.00 27.32 ? 84  VAL   A O   1 
ATOM   624  C  CB  . VAL   A 1 78  ? 6.018  16.840  17.366 1.00 26.46 ? 84  VAL   A CB  1 
ATOM   625  C  CG1 . VAL   A 1 78  ? 6.775  16.544  18.659 1.00 25.63 ? 84  VAL   A CG1 1 
ATOM   626  C  CG2 . VAL   A 1 78  ? 6.022  15.621  16.448 1.00 25.98 ? 84  VAL   A CG2 1 
ATOM   627  N  N   . GLU   A 1 79  ? 4.070  18.252  19.835 1.00 28.79 ? 85  GLU   A N   1 
ATOM   628  C  CA  . GLU   A 1 79  ? 3.961  19.294  20.848 1.00 30.30 ? 85  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 79  ? 5.322  19.892  21.195 1.00 28.74 ? 85  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 79  ? 6.365  19.241  21.057 1.00 28.32 ? 85  GLU   A O   1 
ATOM   631  C  CB  . GLU   A 1 79  ? 3.330  18.706  22.120 1.00 34.59 ? 85  GLU   A CB  1 
ATOM   632  C  CG  . GLU   A 1 79  ? 2.117  19.481  22.578 1.00 46.25 ? 85  GLU   A CG  1 
ATOM   633  C  CD  . GLU   A 1 79  ? 1.609  18.972  23.905 1.00 56.15 ? 85  GLU   A CD  1 
ATOM   634  O  OE1 . GLU   A 1 79  ? 1.499  19.788  24.850 1.00 59.29 ? 85  GLU   A OE1 1 
ATOM   635  O  OE2 . GLU   A 1 79  ? 1.365  17.748  24.008 1.00 58.14 ? 85  GLU   A OE2 1 
ATOM   636  N  N   . ALA   A 1 80  ? 5.321  21.148  21.684 1.00 28.23 ? 86  ALA   A N   1 
ATOM   637  C  CA  . ALA   A 1 80  ? 6.560  21.790  22.113 1.00 27.97 ? 86  ALA   A CA  1 
ATOM   638  C  C   . ALA   A 1 80  ? 7.234  20.970  23.219 1.00 27.49 ? 86  ALA   A C   1 
ATOM   639  O  O   . ALA   A 1 80  ? 6.550  20.436  24.116 1.00 27.99 ? 86  ALA   A O   1 
ATOM   640  C  CB  . ALA   A 1 80  ? 6.272  23.195  22.649 1.00 27.66 ? 86  ALA   A CB  1 
ATOM   641  N  N   . SER   A 1 81  ? 8.555  20.895  23.158 1.00 25.64 ? 87  SER   A N   1 
ATOM   642  C  CA  . SER   A 1 81  ? 9.371  20.207  24.165 1.00 26.33 ? 87  SER   A CA  1 
ATOM   643  C  C   . SER   A 1 81  ? 10.568 21.133  24.498 1.00 27.96 ? 87  SER   A C   1 
ATOM   644  O  O   . SER   A 1 81  ? 10.635 22.278  24.008 1.00 28.36 ? 87  SER   A O   1 
ATOM   645  C  CB  . SER   A 1 81  ? 9.905  18.889  23.572 1.00 26.24 ? 87  SER   A CB  1 
ATOM   646  O  OG  . SER   A 1 81  ? 10.817 19.173  22.515 1.00 25.26 ? 87  SER   A OG  1 
ATOM   647  N  N   . GLU   A 1 82  ? 11.541 20.624  25.293 1.00 28.42 ? 88  GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 82  ? 12.736 21.416  25.563 1.00 30.06 ? 88  GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 82  ? 13.648 21.490  24.312 1.00 28.06 ? 88  GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 82  ? 14.579 22.294  24.297 1.00 28.81 ? 88  GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 82  ? 13.536 20.814  26.742 1.00 35.46 ? 88  GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 82  ? 12.719 20.623  28.009 1.00 46.22 ? 88  GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 82  ? 13.311 19.590  28.955 1.00 59.61 ? 88  GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 82  ? 13.890 18.590  28.464 1.00 62.10 ? 88  GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 82  ? 13.191 19.777  30.189 1.00 63.26 ? 88  GLU   A OE2 1 
ATOM   656  N  N   . TYR   A 1 83  ? 13.385 20.675  23.261 1.00 25.98 ? 89  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 83  ? 14.246 20.625  22.088 1.00 25.17 ? 89  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 83  ? 13.719 21.338  20.854 1.00 24.97 ? 89  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 83  ? 14.520 21.804  20.039 1.00 26.32 ? 89  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 83  ? 14.527 19.165  21.726 1.00 25.53 ? 89  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 83  ? 15.101 18.393  22.889 1.00 27.70 ? 89  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 83  ? 16.404 18.610  23.318 1.00 29.43 ? 89  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 83  ? 14.318 17.502  23.610 1.00 29.88 ? 89  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 83  ? 16.948 17.874  24.365 1.00 31.36 ? 89  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 83  ? 14.848 16.762  24.656 1.00 31.53 ? 89  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 83  ? 16.159 16.965  25.045 1.00 33.37 ? 89  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 83  ? 16.662 16.264  26.108 1.00 36.68 ? 89  TYR   A OH  1 
ATOM   668  N  N   . TYR   A 1 84  ? 12.407 21.446  20.719 1.00 23.50 ? 90  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 84  ? 11.791 22.111  19.554 1.00 23.90 ? 90  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 84  ? 10.535 22.815  19.976 1.00 25.32 ? 90  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 84  ? 9.769  22.292  20.789 1.00 25.25 ? 90  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 84  ? 11.370 21.086  18.472 1.00 23.00 ? 90  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 84  ? 12.478 20.229  17.894 1.00 22.57 ? 90  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 84  ? 13.318 20.717  16.895 1.00 22.73 ? 90  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 84  ? 12.681 18.927  18.335 1.00 22.33 ? 90  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 84  ? 14.357 19.952  16.386 1.00 23.08 ? 90  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 84  ? 13.700 18.139  17.811 1.00 22.16 ? 90  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 84  ? 14.502 18.632  16.801 1.00 22.83 ? 90  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 84  ? 15.510 17.817  16.331 1.00 24.10 ? 90  TYR   A OH  1 
ATOM   680  N  N   . PRO   A 1 85  ? 10.199 23.923  19.290 1.00 25.73 ? 91  PRO   A N   1 
ATOM   681  C  CA  . PRO   A 1 85  ? 8.867  24.514  19.495 1.00 25.85 ? 91  PRO   A CA  1 
ATOM   682  C  C   . PRO   A 1 85  ? 7.799  23.582  18.878 1.00 25.74 ? 91  PRO   A C   1 
ATOM   683  O  O   . PRO   A 1 85  ? 8.154  22.617  18.150 1.00 25.12 ? 91  PRO   A O   1 
ATOM   684  C  CB  . PRO   A 1 85  ? 8.951  25.848  18.728 1.00 26.52 ? 91  PRO   A CB  1 
ATOM   685  C  CG  . PRO   A 1 85  ? 9.959  25.613  17.667 1.00 27.86 ? 91  PRO   A CG  1 
ATOM   686  C  CD  . PRO   A 1 85  ? 10.958 24.617  18.226 1.00 26.29 ? 91  PRO   A CD  1 
ATOM   687  N  N   . ALA   A 1 86  ? 6.500  23.866  19.127 1.00 26.34 ? 92  ALA   A N   1 
ATOM   688  C  CA  . ALA   A 1 86  ? 5.395  23.081  18.539 1.00 27.89 ? 92  ALA   A CA  1 
ATOM   689  C  C   . ALA   A 1 86  ? 5.501  23.191  17.018 1.00 28.68 ? 92  ALA   A C   1 
ATOM   690  O  O   . ALA   A 1 86  ? 5.712  24.289  16.499 1.00 29.42 ? 92  ALA   A O   1 
ATOM   691  C  CB  . ALA   A 1 86  ? 4.044  23.607  19.017 1.00 28.60 ? 92  ALA   A CB  1 
ATOM   692  N  N   . ARG   A 1 87  ? 5.494  22.035  16.315 1.00 28.10 ? 93  ARG   A N   1 
ATOM   693  C  CA  . ARG   A 1 87  ? 5.729  22.056  14.879 1.00 27.53 ? 93  ARG   A CA  1 
ATOM   694  C  C   . ARG   A 1 87  ? 5.266  20.744  14.239 1.00 28.59 ? 93  ARG   A C   1 
ATOM   695  O  O   . ARG   A 1 87  ? 4.936  19.799  14.957 1.00 28.42 ? 93  ARG   A O   1 
ATOM   696  C  CB  . ARG   A 1 87  ? 7.242  22.231  14.641 1.00 28.58 ? 93  ARG   A CB  1 
ATOM   697  C  CG  . ARG   A 1 87  ? 8.041  20.913  14.854 1.00 28.12 ? 93  ARG   A CG  1 
ATOM   698  C  CD  . ARG   A 1 87  ? 9.464  21.125  15.281 1.00 27.48 ? 93  ARG   A CD  1 
ATOM   699  N  NE  . ARG   A 1 87  ? 10.389 20.084  14.811 1.00 25.98 ? 93  ARG   A NE  1 
ATOM   700  C  CZ  . ARG   A 1 87  ? 10.459 18.855  15.320 1.00 25.52 ? 93  ARG   A CZ  1 
ATOM   701  N  NH1 . ARG   A 1 87  ? 9.633  18.484  16.321 1.00 24.09 ? 93  ARG   A NH1 1 
ATOM   702  N  NH2 . ARG   A 1 87  ? 11.374 17.999  14.872 1.00 22.44 ? 93  ARG   A NH2 1 
ATOM   703  N  N   . TYR   A 1 88  ? 5.311  20.677  12.899 1.00 28.95 ? 94  TYR   A N   1 
ATOM   704  C  CA  . TYR   A 1 88  ? 5.050  19.408  12.230 1.00 30.09 ? 94  TYR   A CA  1 
ATOM   705  C  C   . TYR   A 1 88  ? 6.399  18.784  11.974 1.00 27.06 ? 94  TYR   A C   1 
ATOM   706  O  O   . TYR   A 1 88  ? 7.314  19.435  11.449 1.00 27.25 ? 94  TYR   A O   1 
ATOM   707  C  CB  . TYR   A 1 88  ? 4.400  19.598  10.867 1.00 33.13 ? 94  TYR   A CB  1 
ATOM   708  C  CG  . TYR   A 1 88  ? 2.972  20.063  10.930 1.00 37.91 ? 94  TYR   A CG  1 
ATOM   709  C  CD1 . TYR   A 1 88  ? 1.928  19.153  10.999 1.00 40.18 ? 94  TYR   A CD1 1 
ATOM   710  C  CD2 . TYR   A 1 88  ? 2.658  21.410  10.823 1.00 40.50 ? 94  TYR   A CD2 1 
ATOM   711  C  CE1 . TYR   A 1 88  ? 0.602  19.573  10.981 1.00 42.23 ? 94  TYR   A CE1 1 
ATOM   712  C  CE2 . TYR   A 1 88  ? 1.338  21.845  10.818 1.00 42.39 ? 94  TYR   A CE2 1 
ATOM   713  C  CZ  . TYR   A 1 88  ? 0.313  20.923  10.906 1.00 43.79 ? 94  TYR   A CZ  1 
ATOM   714  O  OH  . TYR   A 1 88  ? -0.991 21.355  10.905 1.00 46.50 ? 94  TYR   A OH  1 
ATOM   715  N  N   . GLN   A 1 89  ? 6.539  17.510  12.357 1.00 23.68 ? 95  GLN   A N   1 
ATOM   716  C  CA  . GLN   A 1 89  ? 7.774  16.778  12.060 1.00 22.99 ? 95  GLN   A CA  1 
ATOM   717  C  C   . GLN   A 1 89  ? 7.465  15.894  10.872 1.00 22.64 ? 95  GLN   A C   1 
ATOM   718  O  O   . GLN   A 1 89  ? 6.466  15.173  10.904 1.00 23.13 ? 95  GLN   A O   1 
ATOM   719  C  CB  . GLN   A 1 89  ? 8.206  15.907  13.256 1.00 22.53 ? 95  GLN   A CB  1 
ATOM   720  C  CG  . GLN   A 1 89  ? 9.477  15.053  12.958 1.00 22.85 ? 95  GLN   A CG  1 
ATOM   721  C  CD  . GLN   A 1 89  ? 10.151 14.561  14.233 1.00 22.80 ? 95  GLN   A CD  1 
ATOM   722  O  OE1 . GLN   A 1 89  ? 10.328 15.319  15.194 1.00 21.93 ? 95  GLN   A OE1 1 
ATOM   723  N  NE2 . GLN   A 1 89  ? 10.617 13.293  14.241 1.00 21.74 ? 95  GLN   A NE2 1 
ATOM   724  N  N   . SER   A 1 90  ? 8.294  15.926  9.835  1.00 22.23 ? 96  SER   A N   1 
ATOM   725  C  CA  . SER   A 1 90  ? 8.080  15.101  8.655  1.00 22.51 ? 96  SER   A CA  1 
ATOM   726  C  C   . SER   A 1 90  ? 8.712  13.715  8.762  1.00 22.21 ? 96  SER   A C   1 
ATOM   727  O  O   . SER   A 1 90  ? 9.555  13.477  9.628  1.00 21.86 ? 96  SER   A O   1 
ATOM   728  C  CB  . SER   A 1 90  ? 8.602  15.817  7.406  1.00 25.40 ? 96  SER   A CB  1 
ATOM   729  O  OG  . SER   A 1 90  ? 9.985  16.092  7.547  1.00 25.80 ? 96  SER   A OG  1 
ATOM   730  N  N   . HIS   A 1 91  ? 8.288  12.800  7.879  1.00 21.37 ? 97  HIS   A N   1 
ATOM   731  C  CA  . HIS   A 1 91  ? 8.824  11.436  7.778  1.00 21.10 ? 97  HIS   A CA  1 
ATOM   732  C  C   . HIS   A 1 91  ? 8.703  10.658  9.091  1.00 20.62 ? 97  HIS   A C   1 
ATOM   733  O  O   . HIS   A 1 91  ? 9.524  9.780   9.377  1.00 20.92 ? 97  HIS   A O   1 
ATOM   734  C  CB  . HIS   A 1 91  ? 10.281 11.465  7.253  1.00 22.14 ? 97  HIS   A CB  1 
ATOM   735  C  CG  . HIS   A 1 91  ? 10.419 12.110  5.895  1.00 25.47 ? 97  HIS   A CG  1 
ATOM   736  N  ND1 . HIS   A 1 91  ? 10.464 11.354  4.733  1.00 28.76 ? 97  HIS   A ND1 1 
ATOM   737  C  CD2 . HIS   A 1 91  ? 10.540 13.426  5.561  1.00 26.68 ? 97  HIS   A CD2 1 
ATOM   738  C  CE1 . HIS   A 1 91  ? 10.610 12.230  3.735  1.00 29.35 ? 97  HIS   A CE1 1 
ATOM   739  N  NE2 . HIS   A 1 91  ? 10.648 13.486  4.180  1.00 28.59 ? 97  HIS   A NE2 1 
ATOM   740  N  N   . LEU   A 1 92  ? 7.631  10.942  9.826  1.00 19.71 ? 98  LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 92  ? 7.421  10.295  11.122 1.00 20.11 ? 98  LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 92  ? 6.340  9.194   11.011 1.00 20.13 ? 98  LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 92  ? 5.337  9.361   10.303 1.00 20.11 ? 98  LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 92  ? 6.971  11.400  12.104 1.00 21.05 ? 98  LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 92  ? 6.805  10.994  13.567 1.00 22.35 ? 98  LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 92  ? 8.177  10.614  14.185 1.00 22.74 ? 98  LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 92  ? 6.196  12.189  14.381 1.00 23.82 ? 98  LEU   A CD2 1 
ATOM   748  N  N   . MET   A 1 93  ? 6.573  8.059   11.701 1.00 19.81 ? 99  MET   A N   1 
ATOM   749  C  CA  . MET   A 1 93  ? 5.647  6.924   11.720 1.00 19.92 ? 99  MET   A CA  1 
ATOM   750  C  C   . MET   A 1 93  ? 5.215  6.666   13.146 1.00 20.73 ? 99  MET   A C   1 
ATOM   751  O  O   . MET   A 1 93  ? 6.075  6.623   14.034 1.00 22.34 ? 99  MET   A O   1 
ATOM   752  C  CB  . MET   A 1 93  ? 6.395  5.683   11.186 1.00 20.28 ? 99  MET   A CB  1 
ATOM   753  C  CG  . MET   A 1 93  ? 6.917  5.909   9.781  1.00 23.70 ? 99  MET   A CG  1 
ATOM   754  S  SD  . MET   A 1 93  ? 7.976  4.592   9.232  1.00 24.89 ? 99  MET   A SD  1 
ATOM   755  C  CE  . MET   A 1 93  ? 9.325  4.713   10.390 1.00 21.89 ? 99  MET   A CE  1 
ATOM   756  N  N   . LEU   A 1 94  ? 3.921  6.513   13.401 1.00 21.01 ? 100 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 94  ? 3.447  6.246   14.780 1.00 21.41 ? 100 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 94  ? 3.044  4.788   14.948 1.00 22.43 ? 100 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 94  ? 2.573  4.134   14.008 1.00 22.67 ? 100 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 94  ? 2.220  7.129   15.181 1.00 23.06 ? 100 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 94  ? 2.430  8.634   15.096 1.00 26.47 ? 100 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 94  ? 1.162  9.413   15.567 1.00 27.84 ? 100 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 94  ? 3.706  9.079   15.867 1.00 27.07 ? 100 LEU   A CD2 1 
ATOM   764  N  N   . ALA   A 1 95  ? 3.224  4.306   16.153 1.00 22.17 ? 101 ALA   A N   1 
ATOM   765  C  CA  . ALA   A 1 95  ? 2.789  2.971   16.590 1.00 22.75 ? 101 ALA   A CA  1 
ATOM   766  C  C   . ALA   A 1 95  ? 2.165  3.084   17.995 1.00 22.74 ? 101 ALA   A C   1 
ATOM   767  O  O   . ALA   A 1 95  ? 2.433  4.058   18.716 1.00 22.36 ? 101 ALA   A O   1 
ATOM   768  C  CB  . ALA   A 1 95  ? 3.972  2.017   16.662 1.00 22.82 ? 101 ALA   A CB  1 
ATOM   769  N  N   . VAL   A 1 96  ? 1.332  2.104   18.378 1.00 23.49 ? 102 VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 96  ? 0.823  2.011   19.728 1.00 25.29 ? 102 VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 96  ? 1.893  1.212   20.499 1.00 26.90 ? 102 VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 96  ? 2.192  0.066   20.157 1.00 28.32 ? 102 VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 96  ? -0.561 1.325   19.746 1.00 27.50 ? 102 VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 96  ? -1.007 1.029   21.173 1.00 29.10 ? 102 VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 96  ? -1.587 2.188   19.019 1.00 28.04 ? 102 VAL   A CG2 1 
ATOM   776  N  N   . GLY   A 1 97  ? 2.534  1.863   21.440 1.00 26.67 ? 103 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 97  ? 3.600  1.235   22.218 1.00 27.58 ? 103 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 97  ? 4.112  2.178   23.285 1.00 27.97 ? 103 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 97  ? 3.881  3.395   23.217 1.00 29.21 ? 103 GLY   A O   1 
ATOM   780  N  N   . HIS   A 1 98  ? 4.792  1.623   24.298 1.00 26.53 ? 104 HIS   A N   1 
ATOM   781  C  CA  . HIS   A 1 98  ? 5.343  2.451   25.350 1.00 26.50 ? 104 HIS   A CA  1 
ATOM   782  C  C   . HIS   A 1 98  ? 6.579  3.190   24.858 1.00 25.74 ? 104 HIS   A C   1 
ATOM   783  O  O   . HIS   A 1 98  ? 7.423  2.632   24.177 1.00 25.72 ? 104 HIS   A O   1 
ATOM   784  C  CB  . HIS   A 1 98  ? 5.742  1.610   26.578 1.00 27.61 ? 104 HIS   A CB  1 
ATOM   785  C  CG  . HIS   A 1 98  ? 6.302  2.463   27.680 1.00 30.12 ? 104 HIS   A CG  1 
ATOM   786  N  ND1 . HIS   A 1 98  ? 5.507  3.394   28.346 1.00 33.67 ? 104 HIS   A ND1 1 
ATOM   787  C  CD2 . HIS   A 1 98  ? 7.580  2.627   28.076 1.00 31.38 ? 104 HIS   A CD2 1 
ATOM   788  C  CE1 . HIS   A 1 98  ? 6.321  4.053   29.159 1.00 33.87 ? 104 HIS   A CE1 1 
ATOM   789  N  NE2 . HIS   A 1 98  ? 7.573  3.608   29.057 1.00 33.88 ? 104 HIS   A NE2 1 
ATOM   790  N  N   . SER   A 1 99  ? 6.709  4.436   25.270 1.00 25.63 ? 105 SER   A N   1 
ATOM   791  C  CA  . SER   A 1 99  ? 7.895  5.208   25.094 1.00 25.58 ? 105 SER   A CA  1 
ATOM   792  C  C   . SER   A 1 99  ? 7.897  6.356   26.114 1.00 27.02 ? 105 SER   A C   1 
ATOM   793  O  O   . SER   A 1 99  ? 6.853  6.780   26.603 1.00 28.52 ? 105 SER   A O   1 
ATOM   794  C  CB  . SER   A 1 99  ? 8.036  5.750   23.674 1.00 26.06 ? 105 SER   A CB  1 
ATOM   795  O  OG  . SER   A 1 99  ? 7.091  6.772   23.417 1.00 27.08 ? 105 SER   A OG  1 
ATOM   796  N  N   . GLU   A 1 100 ? 9.072  6.763   26.483 1.00 26.85 ? 106 GLU   A N   1 
ATOM   797  C  CA  . GLU   A 1 100 ? 9.296  7.892   27.386 1.00 28.94 ? 106 GLU   A CA  1 
ATOM   798  C  C   . GLU   A 1 100 ? 10.471 8.655   26.804 1.00 31.69 ? 106 GLU   A C   1 
ATOM   799  O  O   . GLU   A 1 100 ? 11.280 8.086   26.043 1.00 32.90 ? 106 GLU   A O   1 
ATOM   800  C  CB  . GLU   A 1 100 ? 9.733  7.353   28.771 1.00 30.87 ? 106 GLU   A CB  1 
ATOM   801  C  CG  . GLU   A 1 100 ? 8.592  6.812   29.582 1.00 36.65 ? 106 GLU   A CG  1 
ATOM   802  C  CD  . GLU   A 1 100 ? 9.079  6.056   30.799 1.00 40.84 ? 106 GLU   A CD  1 
ATOM   803  O  OE1 . GLU   A 1 100 ? 9.732  6.678   31.666 1.00 43.29 ? 106 GLU   A OE1 1 
ATOM   804  O  OE2 . GLU   A 1 100 ? 8.809  4.840   30.880 1.00 40.15 ? 106 GLU   A OE2 1 
ATOM   805  N  N   . PRO   A 1 101 ? 10.652 9.942   27.175 1.00 35.01 ? 107 PRO   A N   1 
ATOM   806  C  CA  . PRO   A 1 101 ? 11.895 10.610  26.792 1.00 36.37 ? 107 PRO   A CA  1 
ATOM   807  C  C   . PRO   A 1 101 ? 12.997 9.870   27.580 1.00 36.39 ? 107 PRO   A C   1 
ATOM   808  O  O   . PRO   A 1 101 ? 12.890 9.544   28.803 1.00 39.89 ? 107 PRO   A O   1 
ATOM   809  C  CB  . PRO   A 1 101 ? 11.702 12.065  27.248 1.00 36.63 ? 107 PRO   A CB  1 
ATOM   810  C  CG  . PRO   A 1 101 ? 10.262 12.177  27.658 1.00 37.79 ? 107 PRO   A CG  1 
ATOM   811  C  CD  . PRO   A 1 101 ? 9.843  10.781  28.070 1.00 35.27 ? 107 PRO   A CD  1 
ATOM   812  N  N   . GLY   A 1 102 ? 13.986 9.541   26.806 1.00 32.30 ? 108 GLY   A N   1 
ATOM   813  C  CA  . GLY   A 1 102 ? 15.113 8.708   27.129 1.00 29.65 ? 108 GLY   A CA  1 
ATOM   814  C  C   . GLY   A 1 102 ? 15.158 7.550   26.140 1.00 27.98 ? 108 GLY   A C   1 
ATOM   815  O  O   . GLY   A 1 102 ? 16.230 7.010   25.875 1.00 28.32 ? 108 GLY   A O   1 
ATOM   816  N  N   . ASP   A 1 103 ? 13.985 7.151   25.577 1.00 25.54 ? 109 ASP   A N   1 
ATOM   817  C  CA  . ASP   A 1 103 ? 13.915 6.072   24.601 1.00 24.72 ? 109 ASP   A CA  1 
ATOM   818  C  C   . ASP   A 1 103 ? 14.330 6.493   23.195 1.00 23.00 ? 109 ASP   A C   1 
ATOM   819  O  O   . ASP   A 1 103 ? 14.522 5.608   22.339 1.00 21.89 ? 109 ASP   A O   1 
ATOM   820  C  CB  . ASP   A 1 103 ? 12.511 5.444   24.544 1.00 26.41 ? 109 ASP   A CB  1 
ATOM   821  C  CG  . ASP   A 1 103 ? 12.202 4.648   25.781 1.00 26.27 ? 109 ASP   A CG  1 
ATOM   822  O  OD1 . ASP   A 1 103 ? 13.118 4.005   26.297 1.00 27.22 ? 109 ASP   A OD1 1 
ATOM   823  O  OD2 . ASP   A 1 103 ? 11.042 4.697   26.246 1.00 27.55 ? 109 ASP   A OD2 1 
ATOM   824  N  N   . CYS   A 1 104 ? 14.481 7.823   22.926 1.00 23.13 ? 110 CYS   A N   1 
ATOM   825  C  CA  . CYS   A 1 104 ? 14.896 8.233   21.560 1.00 22.46 ? 110 CYS   A CA  1 
ATOM   826  C  C   . CYS   A 1 104 ? 16.194 7.559   21.162 1.00 23.65 ? 110 CYS   A C   1 
ATOM   827  O  O   . CYS   A 1 104 ? 17.078 7.407   22.017 1.00 25.16 ? 110 CYS   A O   1 
ATOM   828  C  CB  . CYS   A 1 104 ? 15.028 9.747   21.460 1.00 23.71 ? 110 CYS   A CB  1 
ATOM   829  S  SG  . CYS   A 1 104 ? 13.454 10.612  21.561 1.00 25.71 ? 110 CYS   A SG  1 
ATOM   830  N  N   . GLY   A 1 105 ? 16.289 7.117   19.924 1.00 22.66 ? 111 GLY   A N   1 
ATOM   831  C  CA  . GLY   A 1 105 ? 17.483 6.451   19.435 1.00 22.76 ? 111 GLY   A CA  1 
ATOM   832  C  C   . GLY   A 1 105 ? 17.362 4.940   19.330 1.00 23.24 ? 111 GLY   A C   1 
ATOM   833  O  O   . GLY   A 1 105 ? 18.155 4.286   18.642 1.00 23.08 ? 111 GLY   A O   1 
ATOM   834  N  N   . GLY   A 1 106 ? 16.330 4.359   19.972 1.00 22.22 ? 112 GLY   A N   1 
ATOM   835  C  CA  . GLY   A 1 106 ? 16.096 2.927   19.890 1.00 19.99 ? 112 GLY   A CA  1 
ATOM   836  C  C   . GLY   A 1 106 ? 15.783 2.546   18.456 1.00 19.64 ? 112 GLY   A C   1 
ATOM   837  O  O   . GLY   A 1 106 ? 15.036 3.261   17.788 1.00 19.90 ? 112 GLY   A O   1 
ATOM   838  N  N   . ILE   A 1 107 ? 16.337 1.412   17.958 1.00 19.38 ? 113 ILE   A N   1 
ATOM   839  C  CA  . ILE   A 1 107 ? 16.095 1.036   16.588 1.00 20.14 ? 113 ILE   A CA  1 
ATOM   840  C  C   . ILE   A 1 107 ? 14.746 0.321   16.364 1.00 18.79 ? 113 ILE   A C   1 
ATOM   841  O  O   . ILE   A 1 107 ? 14.361 -0.567  17.151 1.00 19.62 ? 113 ILE   A O   1 
ATOM   842  C  CB  . ILE   A 1 107 ? 17.308 0.190   16.042 1.00 23.24 ? 113 ILE   A CB  1 
ATOM   843  C  CG1 . ILE   A 1 107 ? 18.421 1.148   15.537 1.00 25.65 ? 113 ILE   A CG1 1 
ATOM   844  C  CG2 . ILE   A 1 107 ? 16.907 -0.797  14.905 1.00 24.74 ? 113 ILE   A CG2 1 
ATOM   845  C  CD1 . ILE   A 1 107 ? 19.777 0.489   15.325 1.00 28.66 ? 113 ILE   A CD1 1 
ATOM   846  N  N   . LEU   A 1 108 ? 14.119 0.631   15.207 1.00 17.77 ? 114 LEU   A N   1 
ATOM   847  C  CA  . LEU   A 1 108 ? 12.930 -0.080  14.697 1.00 17.43 ? 114 LEU   A CA  1 
ATOM   848  C  C   . LEU   A 1 108 ? 13.439 -0.893  13.498 1.00 18.35 ? 114 LEU   A C   1 
ATOM   849  O  O   . LEU   A 1 108 ? 14.067 -0.325  12.586 1.00 18.97 ? 114 LEU   A O   1 
ATOM   850  C  CB  . LEU   A 1 108 ? 11.824 0.925   14.264 1.00 17.07 ? 114 LEU   A CB  1 
ATOM   851  C  CG  . LEU   A 1 108 ? 10.688 0.322   13.425 1.00 19.18 ? 114 LEU   A CG  1 
ATOM   852  C  CD1 . LEU   A 1 108 ? 9.790  -0.601  14.317 1.00 19.27 ? 114 LEU   A CD1 1 
ATOM   853  C  CD2 . LEU   A 1 108 ? 9.836  1.467   12.789 1.00 20.38 ? 114 LEU   A CD2 1 
ATOM   854  N  N   . ARG   A 1 109 ? 13.188 -2.210  13.505 1.00 17.77 ? 115 ARG   A N   1 
ATOM   855  C  CA  . ARG   A 1 109 ? 13.694 -3.073  12.421 1.00 19.14 ? 115 ARG   A CA  1 
ATOM   856  C  C   . ARG   A 1 109 ? 12.576 -3.931  11.860 1.00 19.85 ? 115 ARG   A C   1 
ATOM   857  O  O   . ARG   A 1 109 ? 11.658 -4.324  12.575 1.00 19.56 ? 115 ARG   A O   1 
ATOM   858  C  CB  . ARG   A 1 109 ? 14.800 -3.976  12.991 1.00 22.65 ? 115 ARG   A CB  1 
ATOM   859  C  CG  . ARG   A 1 109 ? 14.248 -4.932  14.052 1.00 31.74 ? 115 ARG   A CG  1 
ATOM   860  C  CD  . ARG   A 1 109 ? 15.213 -6.006  14.541 1.00 40.53 ? 115 ARG   A CD  1 
ATOM   861  N  NE  . ARG   A 1 109 ? 15.943 -5.544  15.721 1.00 49.54 ? 115 ARG   A NE  1 
ATOM   862  C  CZ  . ARG   A 1 109 ? 17.172 -5.042  15.686 1.00 54.63 ? 115 ARG   A CZ  1 
ATOM   863  N  NH1 . ARG   A 1 109 ? 17.837 -4.970  14.535 1.00 56.19 ? 115 ARG   A NH1 1 
ATOM   864  N  NH2 . ARG   A 1 109 ? 17.754 -4.625  16.801 1.00 55.17 ? 115 ARG   A NH2 1 
ATOM   865  N  N   . CYS   A 1 110 ? 12.678 -4.230  10.558 1.00 19.70 ? 116 CYS   A N   1 
ATOM   866  C  CA  . CYS   A 1 110 ? 11.750 -5.150  9.917  1.00 21.13 ? 116 CYS   A CA  1 
ATOM   867  C  C   . CYS   A 1 110 ? 12.602 -6.322  9.347  1.00 23.07 ? 116 CYS   A C   1 
ATOM   868  O  O   . CYS   A 1 110 ? 13.823 -6.381  9.591  1.00 23.49 ? 116 CYS   A O   1 
ATOM   869  C  CB  . CYS   A 1 110 ? 10.986 -4.429  8.811  1.00 22.13 ? 116 CYS   A CB  1 
ATOM   870  S  SG  . CYS   A 1 110 ? 12.060 -3.925  7.440  1.00 22.21 ? 116 CYS   A SG  1 
ATOM   871  N  N   . GLN   A 1 111 ? 11.985 -7.222  8.527  1.00 25.09 ? 117 GLN   A N   1 
ATOM   872  C  CA  . GLN   A 1 111 ? 12.797 -8.309  7.961  1.00 26.96 ? 117 GLN   A CA  1 
ATOM   873  C  C   . GLN   A 1 111 ? 13.895 -7.811  7.007  1.00 28.26 ? 117 GLN   A C   1 
ATOM   874  O  O   . GLN   A 1 111 ? 14.819 -8.577  6.712  1.00 30.40 ? 117 GLN   A O   1 
ATOM   875  C  CB  . GLN   A 1 111 ? 11.906 -9.293  7.215  1.00 29.76 ? 117 GLN   A CB  1 
ATOM   876  C  CG  . GLN   A 1 111 ? 11.176 -8.660  6.054  1.00 33.38 ? 117 GLN   A CG  1 
ATOM   877  C  CD  . GLN   A 1 111 ? 10.262 -9.674  5.448  1.00 40.98 ? 117 GLN   A CD  1 
ATOM   878  O  OE1 . GLN   A 1 111 ? 9.036  -9.592  5.585  1.00 43.65 ? 117 GLN   A OE1 1 
ATOM   879  N  NE2 . GLN   A 1 111 ? 10.850 -10.668 4.798  1.00 43.01 ? 117 GLN   A NE2 1 
ATOM   880  N  N   . HIS   A 1 112 ? 13.797 -6.567  6.494  1.00 26.55 ? 118 HIS   A N   1 
ATOM   881  C  CA  . HIS   A 1 112 ? 14.780 -6.042  5.531  1.00 26.44 ? 118 HIS   A CA  1 
ATOM   882  C  C   . HIS   A 1 112 ? 15.953 -5.262  6.145  1.00 27.42 ? 118 HIS   A C   1 
ATOM   883  O  O   . HIS   A 1 112 ? 16.917 -4.926  5.435  1.00 28.88 ? 118 HIS   A O   1 
ATOM   884  C  CB  . HIS   A 1 112 ? 14.069 -5.184  4.479  1.00 26.74 ? 118 HIS   A CB  1 
ATOM   885  C  CG  . HIS   A 1 112 ? 12.936 -5.904  3.817  1.00 26.49 ? 118 HIS   A CG  1 
ATOM   886  N  ND1 . HIS   A 1 112 ? 11.632 -5.683  4.172  1.00 27.16 ? 118 HIS   A ND1 1 
ATOM   887  C  CD2 . HIS   A 1 112 ? 12.972 -6.837  2.833  1.00 27.08 ? 118 HIS   A CD2 1 
ATOM   888  C  CE1 . HIS   A 1 112 ? 10.901 -6.458  3.396  1.00 29.36 ? 118 HIS   A CE1 1 
ATOM   889  N  NE2 . HIS   A 1 112 ? 11.671 -7.203  2.593  1.00 29.10 ? 118 HIS   A NE2 1 
ATOM   890  N  N   . GLY   A 1 113 ? 15.834 -4.928  7.440  1.00 25.25 ? 119 GLY   A N   1 
ATOM   891  C  CA  . GLY   A 1 113 ? 16.877 -4.192  8.131  1.00 24.79 ? 119 GLY   A CA  1 
ATOM   892  C  C   . GLY   A 1 113 ? 16.335 -3.056  8.972  1.00 24.09 ? 119 GLY   A C   1 
ATOM   893  O  O   . GLY   A 1 113 ? 15.225 -3.147  9.517  1.00 23.37 ? 119 GLY   A O   1 
ATOM   894  N  N   . VAL   A 1 114 ? 17.157 -2.015  9.127  1.00 23.77 ? 120 VAL   A N   1 
ATOM   895  C  CA  . VAL   A 1 114 ? 16.776 -0.870  9.935  1.00 23.25 ? 120 VAL   A CA  1 
ATOM   896  C  C   . VAL   A 1 114 ? 15.792 0.014   9.212  1.00 22.58 ? 120 VAL   A C   1 
ATOM   897  O  O   . VAL   A 1 114 ? 16.048 0.464   8.096  1.00 22.90 ? 120 VAL   A O   1 
ATOM   898  C  CB  . VAL   A 1 114 ? 18.008 -0.063  10.398 1.00 23.57 ? 120 VAL   A CB  1 
ATOM   899  C  CG1 . VAL   A 1 114 ? 17.574 1.228   11.115 1.00 24.67 ? 120 VAL   A CG1 1 
ATOM   900  C  CG2 . VAL   A 1 114 ? 18.870 -0.924  11.315 1.00 24.58 ? 120 VAL   A CG2 1 
ATOM   901  N  N   . VAL   A 1 115 ? 14.650 0.301   9.888  1.00 20.68 ? 121 VAL   A N   1 
ATOM   902  C  CA  . VAL   A 1 115 ? 13.613 1.162   9.300  1.00 19.74 ? 121 VAL   A CA  1 
ATOM   903  C  C   . VAL   A 1 115 ? 13.773 2.600   9.807  1.00 20.23 ? 121 VAL   A C   1 
ATOM   904  O  O   . VAL   A 1 115 ? 13.504 3.565   9.080  1.00 21.09 ? 121 VAL   A O   1 
ATOM   905  C  CB  . VAL   A 1 115 ? 12.226 0.624   9.754  1.00 20.65 ? 121 VAL   A CB  1 
ATOM   906  C  CG1 . VAL   A 1 115 ? 11.090 1.546   9.307  1.00 19.86 ? 121 VAL   A CG1 1 
ATOM   907  C  CG2 . VAL   A 1 115 ? 12.008 -0.789  9.244  1.00 20.97 ? 121 VAL   A CG2 1 
ATOM   908  N  N   . GLY   A 1 116 ? 14.101 2.735   11.086 1.00 19.58 ? 122 GLY   A N   1 
ATOM   909  C  CA  . GLY   A 1 116 ? 14.203 4.071   11.681 1.00 20.36 ? 122 GLY   A CA  1 
ATOM   910  C  C   . GLY   A 1 116 ? 14.579 4.038   13.145 1.00 19.33 ? 122 GLY   A C   1 
ATOM   911  O  O   . GLY   A 1 116 ? 14.993 2.992   13.653 1.00 20.07 ? 122 GLY   A O   1 
ATOM   912  N  N   . ILE   A 1 117 ? 14.510 5.216   13.822 1.00 19.59 ? 123 ILE   A N   1 
ATOM   913  C  CA  . ILE   A 1 117 ? 14.833 5.274   15.256 1.00 19.68 ? 123 ILE   A CA  1 
ATOM   914  C  C   . ILE   A 1 117 ? 13.724 5.992   16.012 1.00 19.44 ? 123 ILE   A C   1 
ATOM   915  O  O   . ILE   A 1 117 ? 13.085 6.875   15.473 1.00 19.26 ? 123 ILE   A O   1 
ATOM   916  C  CB  . ILE   A 1 117 ? 16.179 6.023   15.521 1.00 20.98 ? 123 ILE   A CB  1 
ATOM   917  C  CG1 . ILE   A 1 117 ? 16.201 7.369   14.788 1.00 22.33 ? 123 ILE   A CG1 1 
ATOM   918  C  CG2 . ILE   A 1 117 ? 17.402 5.135   15.156 1.00 22.50 ? 123 ILE   A CG2 1 
ATOM   919  C  CD1 . ILE   A 1 117 ? 17.519 8.186   15.139 1.00 24.56 ? 123 ILE   A CD1 1 
ATOM   920  N  N   . VAL   A 1 118 ? 13.506 5.636   17.279 1.00 18.10 ? 124 VAL   A N   1 
ATOM   921  C  CA  . VAL   A 1 118 ? 12.496 6.336   18.114 1.00 17.55 ? 124 VAL   A CA  1 
ATOM   922  C  C   . VAL   A 1 118 ? 12.854 7.848   18.148 1.00 18.45 ? 124 VAL   A C   1 
ATOM   923  O  O   . VAL   A 1 118 ? 14.032 8.210   18.311 1.00 19.16 ? 124 VAL   A O   1 
ATOM   924  C  CB  . VAL   A 1 118 ? 12.496 5.766   19.547 1.00 18.75 ? 124 VAL   A CB  1 
ATOM   925  C  CG1 . VAL   A 1 118 ? 11.626 6.599   20.488 1.00 19.30 ? 124 VAL   A CG1 1 
ATOM   926  C  CG2 . VAL   A 1 118 ? 12.088 4.289   19.555 1.00 18.40 ? 124 VAL   A CG2 1 
ATOM   927  N  N   . SER   A 1 119 ? 11.849 8.688   17.940 1.00 17.39 ? 125 SER   A N   1 
ATOM   928  C  CA  . SER   A 1 119 ? 12.047 10.137  17.907 1.00 18.04 ? 125 SER   A CA  1 
ATOM   929  C  C   . SER   A 1 119 ? 11.010 10.889  18.738 1.00 19.81 ? 125 SER   A C   1 
ATOM   930  O  O   . SER   A 1 119 ? 11.316 11.953  19.254 1.00 20.68 ? 125 SER   A O   1 
ATOM   931  C  CB  . SER   A 1 119 ? 11.999 10.640  16.464 1.00 19.84 ? 125 SER   A CB  1 
ATOM   932  O  OG  . SER   A 1 119 ? 12.151 12.058  16.403 1.00 21.40 ? 125 SER   A OG  1 
ATOM   933  N  N   . THR   A 1 120 ? 9.775  10.358  18.869 1.00 19.32 ? 126 THR   A N   1 
ATOM   934  C  CA  . THR   A 1 120 ? 8.698  11.059  19.632 1.00 20.75 ? 126 THR   A CA  1 
ATOM   935  C  C   . THR   A 1 120 ? 7.844  10.015  20.416 1.00 22.08 ? 126 THR   A C   1 
ATOM   936  O  O   . THR   A 1 120 ? 8.002  8.815   20.212 1.00 21.09 ? 126 THR   A O   1 
ATOM   937  C  CB  . THR   A 1 120 ? 7.723  11.814  18.629 1.00 22.64 ? 126 THR   A CB  1 
ATOM   938  O  OG1 . THR   A 1 120 ? 6.836  10.904  17.962 1.00 24.69 ? 126 THR   A OG1 1 
ATOM   939  C  CG2 . THR   A 1 120 ? 8.408  12.679  17.606 1.00 22.87 ? 126 THR   A CG2 1 
ATOM   940  N  N   . GLY   A 1 121 ? 6.896  10.485  21.229 1.00 23.25 ? 127 GLY   A N   1 
ATOM   941  C  CA  . GLY   A 1 121 ? 5.967  9.592   21.887 1.00 25.46 ? 127 GLY   A CA  1 
ATOM   942  C  C   . GLY   A 1 121 ? 4.755  10.307  22.442 1.00 28.96 ? 127 GLY   A C   1 
ATOM   943  O  O   . GLY   A 1 121 ? 4.617  11.523  22.285 1.00 30.19 ? 127 GLY   A O   1 
ATOM   944  N  N   . GLY   A 1 122 ? 3.827  9.514   22.959 1.00 30.34 ? 128 GLY   A N   1 
ATOM   945  C  CA  . GLY   A 1 122 ? 2.573  10.000  23.547 1.00 32.16 ? 128 GLY   A CA  1 
ATOM   946  C  C   . GLY   A 1 122 ? 2.063  9.037   24.576 1.00 35.36 ? 128 GLY   A C   1 
ATOM   947  O  O   . GLY   A 1 122 ? 2.782  8.098   24.971 1.00 36.28 ? 128 GLY   A O   1 
ATOM   948  N  N   . ASN   A 1 123 ? 0.801  9.248   25.038 1.00 36.66 ? 129 ASN   A N   1 
ATOM   949  C  CA  . ASN   A 1 123 ? 0.217  8.306   25.964 1.00 37.09 ? 129 ASN   A CA  1 
ATOM   950  C  C   . ASN   A 1 123 ? -0.108 7.030   25.226 1.00 36.19 ? 129 ASN   A C   1 
ATOM   951  O  O   . ASN   A 1 123 ? -1.181 6.902   24.621 1.00 36.77 ? 129 ASN   A O   1 
ATOM   952  C  CB  . ASN   A 1 123 ? -1.023 8.889   26.600 1.00 39.67 ? 129 ASN   A CB  1 
ATOM   953  C  CG  . ASN   A 1 123 ? -1.504 8.116   27.806 1.00 44.35 ? 129 ASN   A CG  1 
ATOM   954  O  OD1 . ASN   A 1 123 ? -1.043 6.998   28.104 1.00 46.57 ? 129 ASN   A OD1 1 
ATOM   955  N  ND2 . ASN   A 1 123 ? -2.440 8.707   28.536 1.00 45.14 ? 129 ASN   A ND2 1 
ATOM   956  N  N   . GLY   A 1 124 ? 0.781  6.039   25.363 1.00 33.31 ? 130 GLY   A N   1 
ATOM   957  C  CA  . GLY   A 1 124 ? 0.611  4.747   24.719 1.00 32.21 ? 130 GLY   A CA  1 
ATOM   958  C  C   . GLY   A 1 124 ? 0.995  4.784   23.252 1.00 29.38 ? 130 GLY   A C   1 
ATOM   959  O  O   . GLY   A 1 124 ? 0.650  3.857   22.516 1.00 30.04 ? 130 GLY   A O   1 
ATOM   960  N  N   . LEU   A 1 125 ? 1.679  5.857   22.810 1.00 27.48 ? 131 LEU   A N   1 
ATOM   961  C  CA  . LEU   A 1 125 ? 2.155  5.978   21.426 1.00 25.42 ? 131 LEU   A CA  1 
ATOM   962  C  C   . LEU   A 1 125 ? 3.690  6.094   21.396 1.00 24.90 ? 131 LEU   A C   1 
ATOM   963  O  O   . LEU   A 1 125 ? 4.298  6.600   22.335 1.00 27.01 ? 131 LEU   A O   1 
ATOM   964  C  CB  . LEU   A 1 125 ? 1.570  7.234   20.728 1.00 26.63 ? 131 LEU   A CB  1 
ATOM   965  C  CG  . LEU   A 1 125 ? 0.047  7.233   20.549 1.00 28.25 ? 131 LEU   A CG  1 
ATOM   966  C  CD1 . LEU   A 1 125 ? -0.471 8.649   20.255 1.00 30.52 ? 131 LEU   A CD1 1 
ATOM   967  C  CD2 . LEU   A 1 125 ? -0.379 6.215   19.496 1.00 28.46 ? 131 LEU   A CD2 1 
ATOM   968  N  N   . VAL   A 1 126 ? 4.289  5.711   20.283 1.00 22.09 ? 132 VAL   A N   1 
ATOM   969  C  CA  . VAL   A 1 126 ? 5.723  5.904   20.068 1.00 21.51 ? 132 VAL   A CA  1 
ATOM   970  C  C   . VAL   A 1 126 ? 5.876  6.288   18.587 1.00 21.18 ? 132 VAL   A C   1 
ATOM   971  O  O   . VAL   A 1 126 ? 5.159  5.754   17.756 1.00 22.16 ? 132 VAL   A O   1 
ATOM   972  C  CB  . VAL   A 1 126 ? 6.551  4.623   20.405 1.00 22.13 ? 132 VAL   A CB  1 
ATOM   973  C  CG1 . VAL   A 1 126 ? 5.981  3.387   19.723 1.00 24.25 ? 132 VAL   A CG1 1 
ATOM   974  C  CG2 . VAL   A 1 126 ? 8.043  4.800   20.066 1.00 21.06 ? 132 VAL   A CG2 1 
ATOM   975  N  N   . GLY   A 1 127 ? 6.735  7.241   18.305 1.00 20.40 ? 133 GLY   A N   1 
ATOM   976  C  CA  . GLY   A 1 127 ? 6.941  7.707   16.942 1.00 20.12 ? 133 GLY   A CA  1 
ATOM   977  C  C   . GLY   A 1 127 ? 8.373  7.471   16.481 1.00 19.65 ? 133 GLY   A C   1 
ATOM   978  O  O   . GLY   A 1 127 ? 9.297  7.630   17.281 1.00 19.54 ? 133 GLY   A O   1 
ATOM   979  N  N   . PHE   A 1 128 ? 8.546  7.068   15.225 1.00 17.31 ? 134 PHE   A N   1 
ATOM   980  C  CA  . PHE   A 1 128 ? 9.870  6.729   14.678 1.00 16.42 ? 134 PHE   A CA  1 
ATOM   981  C  C   . PHE   A 1 128 ? 10.195 7.611   13.491 1.00 17.94 ? 134 PHE   A C   1 
ATOM   982  O  O   . PHE   A 1 128 ? 9.365  7.803   12.598 1.00 18.99 ? 134 PHE   A O   1 
ATOM   983  C  CB  . PHE   A 1 128 ? 9.871  5.281   14.184 1.00 16.51 ? 134 PHE   A CB  1 
ATOM   984  C  CG  . PHE   A 1 128 ? 9.377  4.266   15.203 1.00 17.36 ? 134 PHE   A CG  1 
ATOM   985  C  CD1 . PHE   A 1 128 ? 10.240 3.727   16.146 1.00 17.88 ? 134 PHE   A CD1 1 
ATOM   986  C  CD2 . PHE   A 1 128 ? 8.031  3.871   15.237 1.00 18.97 ? 134 PHE   A CD2 1 
ATOM   987  C  CE1 . PHE   A 1 128 ? 9.784  2.778   17.076 1.00 18.09 ? 134 PHE   A CE1 1 
ATOM   988  C  CE2 . PHE   A 1 128 ? 7.590  2.890   16.135 1.00 19.21 ? 134 PHE   A CE2 1 
ATOM   989  C  CZ  . PHE   A 1 128 ? 8.451  2.395   17.087 1.00 18.78 ? 134 PHE   A CZ  1 
ATOM   990  N  N   . ALA   A 1 129 ? 11.416 8.091   13.471 1.00 17.29 ? 135 ALA   A N   1 
ATOM   991  C  CA  . ALA   A 1 129 ? 11.920 8.876   12.347 1.00 18.10 ? 135 ALA   A CA  1 
ATOM   992  C  C   . ALA   A 1 129 ? 12.378 7.878   11.257 1.00 19.15 ? 135 ALA   A C   1 
ATOM   993  O  O   . ALA   A 1 129 ? 13.264 7.061   11.502 1.00 20.05 ? 135 ALA   A O   1 
ATOM   994  C  CB  . ALA   A 1 129 ? 13.104 9.740   12.799 1.00 18.47 ? 135 ALA   A CB  1 
ATOM   995  N  N   . ASP   A 1 130 ? 11.718 7.885   10.097 1.00 20.02 ? 136 ASP   A N   1 
ATOM   996  C  CA  . ASP   A 1 130 ? 12.069 6.947   9.017  1.00 20.32 ? 136 ASP   A CA  1 
ATOM   997  C  C   . ASP   A 1 130 ? 13.436 7.308   8.415  1.00 20.63 ? 136 ASP   A C   1 
ATOM   998  O  O   . ASP   A 1 130 ? 13.777 8.494   8.283  1.00 21.50 ? 136 ASP   A O   1 
ATOM   999  C  CB  . ASP   A 1 130 ? 11.032 7.066   7.876  1.00 21.27 ? 136 ASP   A CB  1 
ATOM   1000 C  CG  . ASP   A 1 130 ? 11.186 6.002   6.799  1.00 26.41 ? 136 ASP   A CG  1 
ATOM   1001 O  OD1 . ASP   A 1 130 ? 11.264 4.832   7.145  1.00 28.42 ? 136 ASP   A OD1 1 
ATOM   1002 O  OD2 . ASP   A 1 130 ? 11.251 6.366   5.599  1.00 29.76 ? 136 ASP   A OD2 1 
ATOM   1003 N  N   . VAL   A 1 131 ? 14.199 6.285   8.001  1.00 20.96 ? 137 VAL   A N   1 
ATOM   1004 C  CA  . VAL   A 1 131 ? 15.479 6.523   7.282  1.00 22.14 ? 137 VAL   A CA  1 
ATOM   1005 C  C   . VAL   A 1 131 ? 15.500 5.731   5.940  1.00 23.61 ? 137 VAL   A C   1 
ATOM   1006 O  O   . VAL   A 1 131 ? 16.513 5.784   5.220  1.00 25.17 ? 137 VAL   A O   1 
ATOM   1007 C  CB  . VAL   A 1 131 ? 16.726 6.162   8.132  1.00 23.12 ? 137 VAL   A CB  1 
ATOM   1008 C  CG1 . VAL   A 1 131 ? 16.756 6.967   9.429  1.00 23.55 ? 137 VAL   A CG1 1 
ATOM   1009 C  CG2 . VAL   A 1 131 ? 16.773 4.657   8.441  1.00 22.55 ? 137 VAL   A CG2 1 
ATOM   1010 N  N   . ARG   A 1 132 ? 14.399 5.021   5.588  1.00 23.40 ? 138 ARG   A N   1 
ATOM   1011 C  CA  . ARG   A 1 132 ? 14.357 4.175   4.396  1.00 23.70 ? 138 ARG   A CA  1 
ATOM   1012 C  C   . ARG   A 1 132 ? 14.416 4.953   3.081  1.00 26.30 ? 138 ARG   A C   1 
ATOM   1013 O  O   . ARG   A 1 132 ? 14.722 4.357   2.035  1.00 27.69 ? 138 ARG   A O   1 
ATOM   1014 C  CB  . ARG   A 1 132 ? 13.128 3.293   4.410  1.00 22.80 ? 138 ARG   A CB  1 
ATOM   1015 C  CG  . ARG   A 1 132 ? 13.167 2.253   5.508  1.00 23.20 ? 138 ARG   A CG  1 
ATOM   1016 C  CD  . ARG   A 1 132 ? 11.847 1.497   5.491  1.00 22.57 ? 138 ARG   A CD  1 
ATOM   1017 N  NE  . ARG   A 1 132 ? 10.713 2.344   5.867  1.00 22.65 ? 138 ARG   A NE  1 
ATOM   1018 C  CZ  . ARG   A 1 132 ? 9.468  1.901   6.017  1.00 24.19 ? 138 ARG   A CZ  1 
ATOM   1019 N  NH1 . ARG   A 1 132 ? 9.156  0.643   5.688  1.00 23.08 ? 138 ARG   A NH1 1 
ATOM   1020 N  NH2 . ARG   A 1 132 ? 8.516  2.718   6.460  1.00 23.47 ? 138 ARG   A NH2 1 
ATOM   1021 N  N   . ASP   A 1 133 ? 14.091 6.238   3.100  1.00 27.10 ? 139 ASP   A N   1 
ATOM   1022 C  CA  . ASP   A 1 133 ? 14.180 7.046   1.880  1.00 28.81 ? 139 ASP   A CA  1 
ATOM   1023 C  C   . ASP   A 1 133 ? 15.608 7.605   1.673  1.00 30.49 ? 139 ASP   A C   1 
ATOM   1024 O  O   . ASP   A 1 133 ? 15.842 8.240   0.652  1.00 32.43 ? 139 ASP   A O   1 
ATOM   1025 C  CB  . ASP   A 1 133 ? 13.181 8.201   1.940  1.00 30.04 ? 139 ASP   A CB  1 
ATOM   1026 C  CG  . ASP   A 1 133 ? 13.517 9.214   3.016  1.00 34.16 ? 139 ASP   A CG  1 
ATOM   1027 O  OD1 . ASP   A 1 133 ? 13.841 8.792   4.149  1.00 33.82 ? 139 ASP   A OD1 1 
ATOM   1028 O  OD2 . ASP   A 1 133 ? 13.479 10.443  2.715  1.00 35.86 ? 139 ASP   A OD2 1 
ATOM   1029 N  N   . LEU   A 1 134 ? 16.522 7.483   2.675  1.00 30.75 ? 140 LEU   A N   1 
ATOM   1030 C  CA  . LEU   A 1 134 ? 17.869 8.082   2.578  1.00 31.71 ? 140 LEU   A CA  1 
ATOM   1031 C  C   . LEU   A 1 134 ? 18.779 7.101   1.852  1.00 33.92 ? 140 LEU   A C   1 
ATOM   1032 O  O   . LEU   A 1 134 ? 19.644 6.449   2.457  1.00 33.23 ? 140 LEU   A O   1 
ATOM   1033 C  CB  . LEU   A 1 134 ? 18.395 8.418   3.996  1.00 31.49 ? 140 LEU   A CB  1 
ATOM   1034 C  CG  . LEU   A 1 134 ? 17.541 9.406   4.793  1.00 31.40 ? 140 LEU   A CG  1 
ATOM   1035 C  CD1 . LEU   A 1 134 ? 18.055 9.547   6.223  1.00 31.55 ? 140 LEU   A CD1 1 
ATOM   1036 C  CD2 . LEU   A 1 134 ? 17.501 10.771  4.119  1.00 32.53 ? 140 LEU   A CD2 1 
ATOM   1037 N  N   . LEU   A 1 135 ? 18.517 6.960   0.528  1.00 35.23 ? 141 LEU   A N   1 
ATOM   1038 C  CA  . LEU   A 1 135 ? 19.183 6.008   -0.356 1.00 37.10 ? 141 LEU   A CA  1 
ATOM   1039 C  C   . LEU   A 1 135 ? 20.686 6.175   -0.372 1.00 38.91 ? 141 LEU   A C   1 
ATOM   1040 O  O   . LEU   A 1 135 ? 21.406 5.190   -0.549 1.00 39.76 ? 141 LEU   A O   1 
ATOM   1041 C  CB  . LEU   A 1 135 ? 18.602 6.052   -1.792 1.00 37.27 ? 141 LEU   A CB  1 
ATOM   1042 C  CG  . LEU   A 1 135 ? 17.076 5.919   -1.946 1.00 39.52 ? 141 LEU   A CG  1 
ATOM   1043 C  CD1 . LEU   A 1 135 ? 16.698 5.723   -3.409 1.00 41.59 ? 141 LEU   A CD1 1 
ATOM   1044 C  CD2 . LEU   A 1 135 ? 16.489 4.752   -1.092 1.00 39.87 ? 141 LEU   A CD2 1 
ATOM   1045 N  N   . TRP   A 1 136 ? 21.158 7.420   -0.173 1.00 39.37 ? 142 TRP   A N   1 
ATOM   1046 C  CA  . TRP   A 1 136 ? 22.579 7.743   -0.156 1.00 40.28 ? 142 TRP   A CA  1 
ATOM   1047 C  C   . TRP   A 1 136 ? 23.329 7.087   1.019  1.00 40.92 ? 142 TRP   A C   1 
ATOM   1048 O  O   . TRP   A 1 136 ? 24.532 6.913   0.917  1.00 42.19 ? 142 TRP   A O   1 
ATOM   1049 C  CB  . TRP   A 1 136 ? 22.802 9.261   -0.209 1.00 39.97 ? 142 TRP   A CB  1 
ATOM   1050 C  CG  . TRP   A 1 136 ? 22.107 10.026  0.879  1.00 39.51 ? 142 TRP   A CG  1 
ATOM   1051 C  CD1 . TRP   A 1 136 ? 20.882 10.619  0.811  1.00 39.67 ? 142 TRP   A CD1 1 
ATOM   1052 C  CD2 . TRP   A 1 136 ? 22.622 10.321  2.185  1.00 39.13 ? 142 TRP   A CD2 1 
ATOM   1053 N  NE1 . TRP   A 1 136 ? 20.605 11.265  1.990  1.00 39.84 ? 142 TRP   A NE1 1 
ATOM   1054 C  CE2 . TRP   A 1 136 ? 21.651 11.089  2.856  1.00 39.14 ? 142 TRP   A CE2 1 
ATOM   1055 C  CE3 . TRP   A 1 136 ? 23.805 9.991   2.862  1.00 39.31 ? 142 TRP   A CE3 1 
ATOM   1056 C  CZ2 . TRP   A 1 136 ? 21.831 11.548  4.159  1.00 38.82 ? 142 TRP   A CZ2 1 
ATOM   1057 C  CZ3 . TRP   A 1 136 ? 23.984 10.459  4.149  1.00 39.26 ? 142 TRP   A CZ3 1 
ATOM   1058 C  CH2 . TRP   A 1 136 ? 23.006 11.227  4.782  1.00 38.79 ? 142 TRP   A CH2 1 
ATOM   1059 N  N   . LEU   A 1 137 ? 22.632 6.663   2.101  1.00 39.95 ? 143 LEU   A N   1 
ATOM   1060 C  CA  . LEU   A 1 137 ? 23.319 5.988   3.211  1.00 40.27 ? 143 LEU   A CA  1 
ATOM   1061 C  C   . LEU   A 1 137 ? 24.015 4.699   2.768  1.00 44.40 ? 143 LEU   A C   1 
ATOM   1062 O  O   . LEU   A 1 137 ? 24.937 4.269   3.450  1.00 44.79 ? 143 LEU   A O   1 
ATOM   1063 C  CB  . LEU   A 1 137 ? 22.340 5.646   4.365  1.00 38.37 ? 143 LEU   A CB  1 
ATOM   1064 C  CG  . LEU   A 1 137 ? 21.789 6.807   5.159  1.00 36.76 ? 143 LEU   A CG  1 
ATOM   1065 C  CD1 . LEU   A 1 137 ? 20.680 6.315   6.132  1.00 36.65 ? 143 LEU   A CD1 1 
ATOM   1066 C  CD2 . LEU   A 1 137 ? 22.877 7.480   5.974  1.00 36.43 ? 143 LEU   A CD2 1 
ATOM   1067 N  N   . ASP   A 1 138 ? 23.547 4.068   1.656  1.00 47.14 ? 144 ASP   A N   1 
ATOM   1068 C  CA  . ASP   A 1 138 ? 24.067 2.816   1.089  1.00 51.01 ? 144 ASP   A CA  1 
ATOM   1069 C  C   . ASP   A 1 138 ? 25.364 3.005   0.318  1.00 54.82 ? 144 ASP   A C   1 
ATOM   1070 O  O   . ASP   A 1 138 ? 26.129 2.048   0.174  1.00 56.30 ? 144 ASP   A O   1 
ATOM   1071 C  CB  . ASP   A 1 138 ? 23.040 2.184   0.127  1.00 52.97 ? 144 ASP   A CB  1 
ATOM   1072 C  CG  . ASP   A 1 138 ? 21.815 1.602   0.788  1.00 58.98 ? 144 ASP   A CG  1 
ATOM   1073 O  OD1 . ASP   A 1 138 ? 21.828 1.446   2.026  1.00 60.52 ? 144 ASP   A OD1 1 
ATOM   1074 O  OD2 . ASP   A 1 138 ? 20.828 1.315   0.065  1.00 61.27 ? 144 ASP   A OD2 1 
ATOM   1075 N  N   . GLU   A 1 139 ? 25.575 4.195   -0.251 1.00 56.45 ? 145 GLU   A N   1 
ATOM   1076 C  CA  . GLU   A 1 139 ? 26.762 4.479   -1.053 1.00 59.07 ? 145 GLU   A CA  1 
ATOM   1077 C  C   . GLU   A 1 139 ? 27.681 5.518   -0.405 1.00 60.44 ? 145 GLU   A C   1 
ATOM   1078 O  O   . GLU   A 1 139 ? 27.224 6.562   0.067  1.00 61.71 ? 145 GLU   A O   1 
ATOM   1079 C  CB  . GLU   A 1 139 ? 26.368 4.883   -2.489 1.00 62.82 ? 145 GLU   A CB  1 
ATOM   1080 C  CG  . GLU   A 1 139 ? 25.414 6.067   -2.569 1.00 69.68 ? 145 GLU   A CG  1 
ATOM   1081 C  CD  . GLU   A 1 139 ? 24.333 5.934   -3.624 1.00 79.68 ? 145 GLU   A CD  1 
ATOM   1082 O  OE1 . GLU   A 1 139 ? 24.487 6.535   -4.713 1.00 82.17 ? 145 GLU   A OE1 1 
ATOM   1083 O  OE2 . GLU   A 1 139 ? 23.334 5.223   -3.365 1.00 82.79 ? 145 GLU   A OE2 1 
HETATM 1084 N  N1  . A1B2Z B 2 .   ? 9.638  14.594  22.439 1.00 25.15 ? 201 A1B2Z A N1  1 
HETATM 1085 C  C4  . A1B2Z B 2 .   ? 6.127  11.136  25.826 1.00 28.78 ? 201 A1B2Z A C4  1 
HETATM 1086 C  C5  . A1B2Z B 2 .   ? 6.727  12.318  25.430 1.00 28.46 ? 201 A1B2Z A C5  1 
HETATM 1087 C  C6  . A1B2Z B 2 .   ? 7.881  12.287  24.648 1.00 27.72 ? 201 A1B2Z A C6  1 
HETATM 1088 C  C7  . A1B2Z B 2 .   ? 8.491  14.640  25.095 1.00 27.93 ? 201 A1B2Z A C7  1 
HETATM 1089 C  C8  . A1B2Z B 2 .   ? 8.595  13.767  22.810 1.00 25.88 ? 201 A1B2Z A C8  1 
HETATM 1090 C  C10 . A1B2Z B 2 .   ? 12.120 14.738  22.436 1.00 24.40 ? 201 A1B2Z A C10 1 
HETATM 1091 C  C13 . A1B2Z B 2 .   ? 10.770 15.482  18.880 1.00 22.72 ? 201 A1B2Z A C13 1 
HETATM 1092 O  O1  . A1B2Z B 2 .   ? 10.256 16.581  18.639 1.00 22.58 ? 201 A1B2Z A O1  1 
HETATM 1093 N  N2  . A1B2Z B 2 .   ? 11.281 14.701  17.938 1.00 22.30 ? 201 A1B2Z A N2  1 
HETATM 1094 C  C12 . A1B2Z B 2 .   ? 10.801 14.923  20.291 1.00 23.87 ? 201 A1B2Z A C12 1 
HETATM 1095 C  C11 . A1B2Z B 2 .   ? 12.050 15.398  21.058 1.00 24.63 ? 201 A1B2Z A C11 1 
HETATM 1096 C  C9  . A1B2Z B 2 .   ? 10.832 14.946  23.222 1.00 25.07 ? 201 A1B2Z A C9  1 
HETATM 1097 C  C14 . A1B2Z B 2 .   ? 9.556  15.247  21.127 1.00 23.91 ? 201 A1B2Z A C14 1 
HETATM 1098 O  O   . A1B2Z B 2 .   ? 7.848  13.278  21.983 1.00 25.19 ? 201 A1B2Z A O   1 
HETATM 1099 N  N   . A1B2Z B 2 .   ? 8.409  13.522  24.152 1.00 27.87 ? 201 A1B2Z A N   1 
HETATM 1100 C  C1  . A1B2Z B 2 .   ? 8.434  11.055  24.281 1.00 27.00 ? 201 A1B2Z A C1  1 
HETATM 1101 S  S   . A1B2Z B 2 .   ? 9.888  11.057  23.272 1.00 25.88 ? 201 A1B2Z A S   1 
HETATM 1102 C  C   . A1B2Z B 2 .   ? 10.205 9.285   22.990 1.00 25.33 ? 201 A1B2Z A C   1 
HETATM 1103 C  C3  . A1B2Z B 2 .   ? 6.671  9.927   25.467 1.00 28.12 ? 201 A1B2Z A C3  1 
HETATM 1104 C  C2  . A1B2Z B 2 .   ? 7.826  9.877   24.699 1.00 27.62 ? 201 A1B2Z A C2  1 
HETATM 1105 ZN ZN  . ZN    C 3 .   ? 10.870 -4.152  5.442  1.00 23.41 2 202 ZN    A ZN  1 
HETATM 1106 S  S   . DMS   D 4 .   ? 3.135  12.655  17.948 1.00 62.65 ? 203 DMS   A S   1 
HETATM 1107 O  O   . DMS   D 4 .   ? 3.038  14.076  18.449 1.00 62.87 ? 203 DMS   A O   1 
HETATM 1108 C  C1  . DMS   D 4 .   ? 1.512  11.891  18.305 1.00 62.62 ? 203 DMS   A C1  1 
HETATM 1109 C  C2  . DMS   D 4 .   ? 3.982  11.643  19.158 1.00 61.75 ? 203 DMS   A C2  1 
HETATM 1110 O  O   . HOH   E 5 .   ? 11.303 -4.786  31.627 1.00 47.58 ? 301 HOH   A O   1 
HETATM 1111 O  O   . HOH   E 5 .   ? 3.314  15.420  20.461 1.00 34.93 ? 302 HOH   A O   1 
HETATM 1112 O  O   . HOH   E 5 .   ? 4.715  21.223  25.612 1.00 51.26 ? 303 HOH   A O   1 
HETATM 1113 O  O   . HOH   E 5 .   ? 29.042 3.645   10.385 1.00 33.65 ? 304 HOH   A O   1 
HETATM 1114 O  O   . HOH   E 5 .   ? 3.975  -5.018  21.159 1.00 38.84 ? 305 HOH   A O   1 
HETATM 1115 O  O   . HOH   E 5 .   ? 7.080  25.811  14.960 1.00 39.28 ? 306 HOH   A O   1 
HETATM 1116 O  O   . HOH   E 5 .   ? 18.677 0.020   27.645 1.00 47.12 ? 307 HOH   A O   1 
HETATM 1117 O  O   . HOH   E 5 .   ? 33.924 -2.445  10.291 1.00 41.10 ? 308 HOH   A O   1 
HETATM 1118 O  O   . HOH   E 5 .   ? 23.614 22.629  8.801  1.00 41.45 ? 309 HOH   A O   1 
HETATM 1119 O  O   . HOH   E 5 .   ? 10.404 8.654   4.722  1.00 30.34 ? 310 HOH   A O   1 
HETATM 1120 O  O   . HOH   E 5 .   ? 30.946 3.259   12.058 1.00 49.04 ? 311 HOH   A O   1 
HETATM 1121 O  O   . HOH   E 5 .   ? 15.923 13.783  26.378 1.00 45.22 ? 312 HOH   A O   1 
HETATM 1122 O  O   . HOH   E 5 .   ? 17.533 -6.038  3.154  1.00 46.08 ? 313 HOH   A O   1 
HETATM 1123 O  O   . HOH   E 5 .   ? 9.548  24.651  23.849 1.00 37.70 ? 314 HOH   A O   1 
HETATM 1124 O  O   . HOH   E 5 .   ? 0.081  14.748  17.022 1.00 46.53 ? 315 HOH   A O   1 
HETATM 1125 O  O   . HOH   E 5 .   ? 6.323  -5.202  29.003 1.00 39.19 ? 316 HOH   A O   1 
HETATM 1126 O  O   . HOH   E 5 .   ? 9.479  18.672  20.277 1.00 23.76 ? 317 HOH   A O   1 
HETATM 1127 O  O   . HOH   E 5 .   ? 24.786 -6.650  9.048  1.00 64.49 ? 318 HOH   A O   1 
HETATM 1128 O  O   . HOH   E 5 .   ? 10.081 5.304   3.458  1.00 30.51 ? 319 HOH   A O   1 
HETATM 1129 O  O   . HOH   E 5 .   ? 0.458  0.061   16.445 1.00 24.00 ? 320 HOH   A O   1 
HETATM 1130 O  O   . HOH   E 5 .   ? 7.900  19.956  18.291 1.00 22.69 ? 321 HOH   A O   1 
HETATM 1131 O  O   . HOH   E 5 .   ? 19.897 9.344   19.135 1.00 23.77 ? 322 HOH   A O   1 
HETATM 1132 O  O   . HOH   E 5 .   ? 17.478 1.158   29.974 1.00 50.10 ? 323 HOH   A O   1 
HETATM 1133 O  O   . HOH   E 5 .   ? 22.235 -0.414  3.927  1.00 33.97 ? 324 HOH   A O   1 
HETATM 1134 O  O   . HOH   E 5 .   ? 11.063 17.780  5.745  1.00 49.12 ? 325 HOH   A O   1 
HETATM 1135 O  O   . HOH   E 5 .   ? 26.129 -1.771  6.061  1.00 59.68 ? 326 HOH   A O   1 
HETATM 1136 O  O   . HOH   E 5 .   ? 25.944 4.560   20.087 1.00 51.41 ? 327 HOH   A O   1 
HETATM 1137 O  O   . HOH   E 5 .   ? 17.795 21.678  9.555  1.00 37.09 ? 328 HOH   A O   1 
HETATM 1138 O  O   . HOH   E 5 .   ? 14.744 11.632  0.618  1.00 51.57 ? 329 HOH   A O   1 
HETATM 1139 O  O   . HOH   E 5 .   ? 29.999 11.381  20.573 1.00 63.12 ? 330 HOH   A O   1 
HETATM 1140 O  O   . HOH   E 5 .   ? 14.510 21.402  7.661  1.00 53.25 ? 331 HOH   A O   1 
HETATM 1141 O  O   . HOH   E 5 .   ? 15.672 -10.604 8.336  1.00 55.77 ? 332 HOH   A O   1 
HETATM 1142 O  O   . HOH   E 5 .   ? 30.910 19.076  8.426  1.00 47.65 ? 333 HOH   A O   1 
HETATM 1143 O  O   . HOH   E 5 .   ? 5.126  8.042   28.332 1.00 42.85 ? 334 HOH   A O   1 
HETATM 1144 O  O   . HOH   E 5 .   ? 6.546  17.826  25.002 1.00 36.47 ? 335 HOH   A O   1 
HETATM 1145 O  O   . HOH   E 5 .   ? -0.359 16.040  8.077  1.00 58.23 ? 336 HOH   A O   1 
HETATM 1146 O  O   . HOH   E 5 .   ? 15.092 23.777  18.190 1.00 32.63 ? 337 HOH   A O   1 
HETATM 1147 O  O   . HOH   E 5 .   ? 18.085 5.018   26.574 1.00 42.97 ? 338 HOH   A O   1 
HETATM 1148 O  O   . HOH   E 5 .   ? 12.004 21.715  12.972 1.00 30.62 ? 339 HOH   A O   1 
HETATM 1149 O  O   . HOH   E 5 .   ? 3.835  5.545   25.279 1.00 37.12 ? 340 HOH   A O   1 
HETATM 1150 O  O   . HOH   E 5 .   ? 17.635 2.889   23.087 1.00 30.98 ? 341 HOH   A O   1 
HETATM 1151 O  O   . HOH   E 5 .   ? 7.993  -8.291  23.388 1.00 36.82 ? 342 HOH   A O   1 
HETATM 1152 O  O   . HOH   E 5 .   ? 15.961 23.626  14.842 1.00 49.13 ? 343 HOH   A O   1 
HETATM 1153 O  O   . HOH   E 5 .   ? 14.760 2.925   23.160 1.00 25.59 ? 344 HOH   A O   1 
HETATM 1154 O  O   . HOH   E 5 .   ? 14.804 24.307  26.217 1.00 44.29 ? 345 HOH   A O   1 
HETATM 1155 O  O   . HOH   E 5 .   ? 8.652  3.107   2.788  1.00 29.50 ? 346 HOH   A O   1 
HETATM 1156 O  O   . HOH   E 5 .   ? 12.304 7.906   30.990 1.00 90.72 ? 347 HOH   A O   1 
HETATM 1157 O  O   . HOH   E 5 .   ? 9.580  4.921   33.840 1.00 36.73 ? 348 HOH   A O   1 
HETATM 1158 O  O   . HOH   E 5 .   ? 11.074 2.498   33.458 1.00 29.01 ? 349 HOH   A O   1 
HETATM 1159 O  O   . HOH   E 5 .   ? 17.014 20.588  19.640 1.00 34.33 ? 350 HOH   A O   1 
HETATM 1160 O  O   . HOH   E 5 .   ? 23.251 0.416   15.876 1.00 34.20 ? 351 HOH   A O   1 
HETATM 1161 O  O   . HOH   E 5 .   ? 6.920  3.892   32.853 1.00 34.76 ? 352 HOH   A O   1 
HETATM 1162 O  O   . HOH   E 5 .   ? 11.198 12.059  11.431 1.00 21.05 ? 353 HOH   A O   1 
HETATM 1163 O  O   . HOH   E 5 .   ? 0.605  -2.268  19.956 1.00 35.88 ? 354 HOH   A O   1 
HETATM 1164 O  O   . HOH   E 5 .   ? 22.347 -7.110  4.630  1.00 62.14 ? 355 HOH   A O   1 
HETATM 1165 O  O   . HOH   E 5 .   ? 21.776 19.224  18.450 1.00 52.35 ? 356 HOH   A O   1 
HETATM 1166 O  O   . HOH   E 5 .   ? 24.201 11.048  21.109 1.00 44.55 ? 357 HOH   A O   1 
HETATM 1167 O  O   . HOH   E 5 .   ? 17.749 19.315  17.229 1.00 26.43 ? 358 HOH   A O   1 
HETATM 1168 O  O   . HOH   E 5 .   ? 4.159  7.822   3.169  1.00 45.26 ? 359 HOH   A O   1 
HETATM 1169 O  O   . HOH   E 5 .   ? 8.239  -3.613  0.485  1.00 34.34 ? 360 HOH   A O   1 
HETATM 1170 O  O   . HOH   E 5 .   ? 6.859  16.875  22.591 1.00 30.29 ? 361 HOH   A O   1 
HETATM 1171 O  O   . HOH   E 5 .   ? 18.217 -2.764  18.931 1.00 68.40 ? 362 HOH   A O   1 
HETATM 1172 O  O   . HOH   E 5 .   ? 12.999 11.010  9.414  1.00 20.92 ? 363 HOH   A O   1 
HETATM 1173 O  O   . HOH   E 5 .   ? 3.461  0.929   30.519 1.00 59.47 ? 364 HOH   A O   1 
HETATM 1174 O  O   . HOH   E 5 .   ? 18.496 9.532   25.809 1.00 34.36 ? 365 HOH   A O   1 
HETATM 1175 O  O   . HOH   E 5 .   ? 15.027 12.711  24.220 1.00 28.28 ? 366 HOH   A O   1 
HETATM 1176 O  O   . HOH   E 5 .   ? 23.756 14.741  23.590 1.00 70.98 ? 367 HOH   A O   1 
HETATM 1177 O  O   . HOH   E 5 .   ? 28.048 -1.604  13.433 1.00 46.49 ? 368 HOH   A O   1 
HETATM 1178 O  O   . HOH   E 5 .   ? 13.041 -8.125  24.530 1.00 28.16 ? 369 HOH   A O   1 
HETATM 1179 O  O   . HOH   E 5 .   ? 18.504 13.247  1.763  1.00 44.91 ? 370 HOH   A O   1 
HETATM 1180 O  O   . HOH   E 5 .   ? 34.501 5.346   13.953 1.00 67.01 ? 371 HOH   A O   1 
HETATM 1181 O  O   . HOH   E 5 .   ? 5.303  14.630  22.302 1.00 34.14 ? 372 HOH   A O   1 
HETATM 1182 O  O   . HOH   E 5 .   ? 14.938 -3.443  17.453 1.00 34.87 ? 373 HOH   A O   1 
HETATM 1183 O  O   . HOH   E 5 .   ? 0.044  4.324   6.455  1.00 49.78 ? 374 HOH   A O   1 
HETATM 1184 O  O   . HOH   E 5 .   ? 30.534 -3.164  7.002  1.00 49.89 ? 375 HOH   A O   1 
HETATM 1185 O  O   . HOH   E 5 .   ? 14.277 15.024  3.656  1.00 34.28 ? 376 HOH   A O   1 
HETATM 1186 O  O   . HOH   E 5 .   ? 5.705  23.049  11.255 1.00 40.45 ? 377 HOH   A O   1 
HETATM 1187 O  O   . HOH   E 5 .   ? 2.887  22.635  22.288 1.00 37.12 ? 378 HOH   A O   1 
HETATM 1188 O  O   . HOH   E 5 .   ? 5.968  26.216  20.776 1.00 31.93 ? 379 HOH   A O   1 
HETATM 1189 O  O   . HOH   E 5 .   ? 3.904  -4.663  6.201  1.00 37.90 ? 380 HOH   A O   1 
HETATM 1190 O  O   . HOH   E 5 .   ? 5.107  -1.287  24.267 1.00 30.49 ? 381 HOH   A O   1 
HETATM 1191 O  O   . HOH   E 5 .   ? 7.569  8.324   32.780 1.00 67.56 ? 382 HOH   A O   1 
HETATM 1192 O  O   . HOH   E 5 .   ? 28.111 12.122  1.713  1.00 60.74 ? 383 HOH   A O   1 
HETATM 1193 O  O   . HOH   E 5 .   ? 20.297 2.300   18.256 1.00 35.42 ? 384 HOH   A O   1 
HETATM 1194 O  O   . HOH   E 5 .   ? 4.650  -4.644  2.781  1.00 54.29 ? 385 HOH   A O   1 
HETATM 1195 O  O   . HOH   E 5 .   ? 31.395 9.521   5.712  1.00 50.61 ? 386 HOH   A O   1 
HETATM 1196 O  O   . HOH   E 5 .   ? 20.869 -4.338  10.107 1.00 40.19 ? 387 HOH   A O   1 
HETATM 1197 O  O   . HOH   E 5 .   ? 16.665 19.452  27.810 1.00 63.19 ? 388 HOH   A O   1 
HETATM 1198 O  O   . HOH   E 5 .   ? 6.508  13.298  5.537  1.00 36.38 ? 389 HOH   A O   1 
HETATM 1199 O  O   . HOH   E 5 .   ? -0.820 15.580  13.140 1.00 34.63 ? 390 HOH   A O   1 
HETATM 1200 O  O   . HOH   E 5 .   ? 15.607 -3.995  1.520  1.00 32.97 ? 391 HOH   A O   1 
HETATM 1201 O  O   . HOH   E 5 .   ? 18.456 0.007   19.550 1.00 32.35 ? 392 HOH   A O   1 
HETATM 1202 O  O   . HOH   E 5 .   ? 1.981  6.009   28.113 1.00 44.87 ? 393 HOH   A O   1 
HETATM 1203 O  O   . HOH   E 5 .   ? 28.527 16.487  3.804  1.00 59.00 ? 394 HOH   A O   1 
HETATM 1204 O  O   . HOH   E 5 .   ? 1.953  13.769  5.393  1.00 38.13 ? 395 HOH   A O   1 
HETATM 1205 O  O   . HOH   E 5 .   ? 9.284  21.684  11.004 1.00 49.55 ? 396 HOH   A O   1 
HETATM 1206 O  O   . HOH   E 5 .   ? 30.278 11.179  17.825 1.00 50.68 ? 397 HOH   A O   1 
HETATM 1207 O  O   . HOH   E 5 .   ? 36.692 0.227   8.875  1.00 47.04 ? 398 HOH   A O   1 
HETATM 1208 O  O   . HOH   E 5 .   ? 1.337  -2.405  17.400 1.00 32.83 ? 399 HOH   A O   1 
HETATM 1209 O  O   . HOH   E 5 .   ? 2.557  3.423   27.591 1.00 41.38 ? 400 HOH   A O   1 
HETATM 1210 O  O   . HOH   E 5 .   ? 36.646 17.324  13.413 1.00 51.78 ? 401 HOH   A O   1 
HETATM 1211 O  O   . HOH   E 5 .   ? 27.543 20.792  20.818 1.00 49.66 ? 402 HOH   A O   1 
HETATM 1212 O  O   . HOH   E 5 .   ? 21.409 -4.442  12.631 1.00 52.67 ? 403 HOH   A O   1 
HETATM 1213 O  O   . HOH   E 5 .   ? 5.483  2.350   7.126  1.00 34.49 ? 404 HOH   A O   1 
HETATM 1214 O  O   . HOH   E 5 .   ? 25.768 -1.730  14.800 1.00 52.04 ? 405 HOH   A O   1 
HETATM 1215 O  O   . HOH   E 5 .   ? 21.683 9.219   21.187 1.00 33.52 ? 406 HOH   A O   1 
HETATM 1216 O  O   . HOH   E 5 .   ? 3.254  13.868  23.778 1.00 51.31 ? 407 HOH   A O   1 
HETATM 1217 O  O   . HOH   E 5 .   ? 0.476  1.243   24.195 1.00 37.77 ? 408 HOH   A O   1 
HETATM 1218 O  O   . HOH   E 5 .   ? 31.538 0.224   13.593 1.00 54.15 ? 409 HOH   A O   1 
HETATM 1219 O  O   . HOH   E 5 .   ? 23.564 2.723   19.701 1.00 42.59 ? 410 HOH   A O   1 
HETATM 1220 O  O   . HOH   E 5 .   ? 11.438 10.937  0.404  1.00 77.57 ? 411 HOH   A O   1 
HETATM 1221 O  O   . HOH   E 5 .   ? 8.875  -7.248  8.183  1.00 49.52 ? 412 HOH   A O   1 
HETATM 1222 O  O   . HOH   E 5 .   ? 29.849 5.363   3.614  1.00 48.00 ? 413 HOH   A O   1 
HETATM 1223 O  O   . HOH   E 5 .   ? 21.065 -1.943  33.393 1.00 59.06 ? 414 HOH   A O   1 
HETATM 1224 O  O   . HOH   E 5 .   ? 17.480 9.634   -1.678 1.00 50.81 ? 415 HOH   A O   1 
HETATM 1225 O  O   . HOH   E 5 .   ? 6.506  -7.924  14.285 1.00 47.41 ? 416 HOH   A O   1 
HETATM 1226 O  O   . HOH   E 5 .   ? -1.393 23.758  8.833  1.00 72.19 ? 417 HOH   A O   1 
HETATM 1227 O  O   . HOH   E 5 .   ? 18.351 -4.843  27.513 1.00 60.45 ? 418 HOH   A O   1 
HETATM 1228 O  O   . HOH   E 5 .   ? 18.417 -5.348  11.360 1.00 60.06 ? 419 HOH   A O   1 
HETATM 1229 O  O   . HOH   E 5 .   ? 4.525  -1.412  29.121 1.00 60.93 ? 420 HOH   A O   1 
HETATM 1230 O  O   . HOH   E 5 .   ? 22.270 19.322  5.692  1.00 37.55 ? 421 HOH   A O   1 
HETATM 1231 O  O   . HOH   E 5 .   ? 8.781  -4.546  32.315 1.00 55.90 ? 422 HOH   A O   1 
HETATM 1232 O  O   . HOH   E 5 .   ? 6.771  11.395  3.909  1.00 43.81 ? 423 HOH   A O   1 
HETATM 1233 O  O   . HOH   E 5 .   ? 35.181 10.989  12.102 1.00 57.02 ? 424 HOH   A O   1 
HETATM 1234 O  O   . HOH   E 5 .   ? 6.707  -3.669  -1.652 1.00 46.44 ? 425 HOH   A O   1 
HETATM 1235 O  O   . HOH   E 5 .   ? 22.417 17.124  23.062 1.00 66.52 ? 426 HOH   A O   1 
HETATM 1236 O  O   . HOH   E 5 .   ? 7.397  -4.999  2.740  1.00 40.93 ? 427 HOH   A O   1 
HETATM 1237 O  O   . HOH   E 5 .   ? 16.399 -6.693  25.532 1.00 58.54 ? 428 HOH   A O   1 
HETATM 1238 O  O   . HOH   E 5 .   ? 18.692 7.786   28.158 1.00 42.86 ? 429 HOH   A O   1 
HETATM 1239 O  O   . HOH   E 5 .   ? 24.051 7.431   20.818 1.00 64.34 ? 430 HOH   A O   1 
HETATM 1240 O  O   . HOH   E 5 .   ? 31.197 14.408  22.548 1.00 42.57 ? 431 HOH   A O   1 
HETATM 1241 O  O   . HOH   E 5 .   ? 8.828  19.718  6.574  1.00 56.66 ? 432 HOH   A O   1 
HETATM 1242 O  O   . HOH   E 5 .   ? 28.898 8.758   20.953 1.00 71.30 ? 433 HOH   A O   1 
HETATM 1243 O  O   . HOH   E 5 .   ? 1.389  14.684  22.127 1.00 48.99 ? 434 HOH   A O   1 
HETATM 1244 O  O   . HOH   E 5 .   ? 17.555 21.220  26.023 1.00 62.88 ? 435 HOH   A O   1 
HETATM 1245 O  O   . HOH   E 5 .   ? 3.306  9.748   28.156 1.00 45.78 ? 436 HOH   A O   1 
HETATM 1246 O  O   . HOH   E 5 .   ? 30.974 9.975   15.118 1.00 56.88 ? 437 HOH   A O   1 
HETATM 1247 O  O   . HOH   E 5 .   ? 19.032 -7.113  7.417  1.00 55.83 ? 438 HOH   A O   1 
HETATM 1248 O  O   . HOH   E 5 .   ? 1.932  1.281   26.535 1.00 44.79 ? 439 HOH   A O   1 
HETATM 1249 O  O   . HOH   E 5 .   ? 17.180 11.608  0.169  1.00 51.39 ? 440 HOH   A O   1 
HETATM 1250 O  O   . HOH   E 5 .   ? 12.439 15.629  26.812 1.00 53.12 ? 441 HOH   A O   1 
HETATM 1251 O  O   . HOH   E 5 .   ? 30.739 6.542   17.130 1.00 58.77 ? 442 HOH   A O   1 
HETATM 1252 O  O   . HOH   E 5 .   ? 16.437 11.973  28.261 1.00 59.23 ? 443 HOH   A O   1 
HETATM 1253 O  O   . HOH   E 5 .   ? 20.631 -4.572  33.107 1.00 77.83 ? 444 HOH   A O   1 
HETATM 1254 O  O   . HOH   E 5 .   ? 0.837  -1.482  23.292 1.00 40.18 ? 445 HOH   A O   1 
HETATM 1255 O  O   . HOH   E 5 .   ? 2.672  -6.549  14.995 1.00 60.35 ? 446 HOH   A O   1 
HETATM 1256 O  O   . HOH   E 5 .   ? 11.812 23.709  14.732 1.00 34.64 ? 447 HOH   A O   1 
HETATM 1257 O  O   . HOH   E 5 .   ? 3.840  -1.974  26.617 1.00 45.96 ? 448 HOH   A O   1 
HETATM 1258 O  O   . HOH   E 5 .   ? 19.731 9.862   -2.956 1.00 62.98 ? 449 HOH   A O   1 
HETATM 1259 O  O   . HOH   E 5 .   ? 13.510 -6.070  32.713 1.00 54.63 ? 450 HOH   A O   1 
HETATM 1260 O  O   . HOH   E 5 .   ? 13.852 24.810  15.683 1.00 44.07 ? 451 HOH   A O   1 
HETATM 1261 O  O   . HOH   E 5 .   ? 19.832 15.359  0.626  1.00 52.39 ? 452 HOH   A O   1 
HETATM 1262 O  O   . HOH   E 5 .   ? 3.635  -2.848  22.665 1.00 48.79 ? 453 HOH   A O   1 
HETATM 1263 O  O   . HOH   E 5 .   ? 16.383 14.465  2.067  1.00 57.25 ? 454 HOH   A O   1 
HETATM 1264 O  O   . HOH   E 5 .   ? 6.073  3.255   3.045  1.00 54.37 ? 455 HOH   A O   1 
HETATM 1265 O  O   . HOH   E 5 .   ? 8.497  7.610   2.594  1.00 45.66 ? 456 HOH   A O   1 
HETATM 1266 O  O   . HOH   E 5 .   ? 19.527 -2.813  21.937 1.00 67.51 ? 457 HOH   A O   1 
HETATM 1267 O  O   . HOH   E 5 .   ? 8.271  17.640  27.058 1.00 43.67 ? 458 HOH   A O   1 
HETATM 1268 O  O   . HOH   E 5 .   ? 19.856 13.331  26.989 1.00 48.68 ? 459 HOH   A O   1 
HETATM 1269 O  O   . HOH   E 5 .   ? 24.099 13.985  1.585  1.00 57.49 ? 460 HOH   A O   1 
HETATM 1270 O  O   . HOH   E 5 .   ? 22.077 10.351  23.944 1.00 47.30 ? 461 HOH   A O   1 
HETATM 1271 O  O   . HOH   E 5 .   ? 36.941 18.212  15.983 1.00 62.15 ? 462 HOH   A O   1 
HETATM 1272 O  O   . HOH   E 5 .   ? 0.185  12.366  21.605 1.00 45.61 ? 463 HOH   A O   1 
HETATM 1273 O  O   . HOH   E 5 .   ? 31.741 4.579   15.191 1.00 64.38 ? 464 HOH   A O   1 
HETATM 1274 O  O   . HOH   E 5 .   ? 16.456 -7.396  31.626 1.00 57.90 ? 465 HOH   A O   1 
HETATM 1275 O  O   . HOH   E 5 .   ? 3.286  -6.480  22.921 1.00 49.81 ? 466 HOH   A O   1 
HETATM 1276 O  O   . HOH   E 5 .   ? 25.766 10.950  -1.175 1.00 56.53 ? 467 HOH   A O   1 
HETATM 1277 O  O   . HOH   E 5 .   ? 21.159 12.478  -2.584 1.00 65.11 ? 468 HOH   A O   1 
HETATM 1278 O  O   . HOH   E 5 .   ? 20.703 11.030  26.119 1.00 50.86 ? 469 HOH   A O   1 
HETATM 1279 O  O   . HOH   E 5 .   ? 5.449  -7.890  23.671 1.00 60.14 ? 470 HOH   A O   1 
HETATM 1280 O  O   . HOH   E 5 .   ? 0.683  12.614  29.851 1.00 72.36 ? 471 HOH   A O   1 
HETATM 1281 O  O   . HOH   E 5 .   ? 4.995  13.729  28.289 1.00 63.14 ? 472 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   ? 0.4573 0.3311 0.4324 0.0434  -0.1158 -0.0540 7   SER   A N   
2    C CA  . SER   A 1   ? 0.4351 0.3298 0.4708 0.0424  -0.1254 -0.0633 7   SER   A CA  
3    C C   . SER   A 1   ? 0.4135 0.3288 0.4723 0.0365  -0.1144 -0.0598 7   SER   A C   
4    O O   . SER   A 1   ? 0.4209 0.3282 0.4468 0.0356  -0.1093 -0.0522 7   SER   A O   
5    C CB  . SER   A 1   ? 0.4958 0.3630 0.5381 0.0515  -0.1610 -0.0763 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.5718 0.4115 0.5783 0.0560  -0.1762 -0.0745 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.3744 0.3136 0.4890 0.0321  -0.1085 -0.0659 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.3527 0.3086 0.4902 0.0261  -0.0961 -0.0642 8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3244 0.3045 0.5030 0.0182  -0.0730 -0.0654 8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3155 0.3029 0.4918 0.0156  -0.0599 -0.0619 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.2968 0.2856 0.5078 0.0138  -0.0655 -0.0696 9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.2858 0.2885 0.5285 0.0057  -0.0399 -0.0711 9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2800 0.2875 0.5230 -0.0007 -0.0242 -0.0684 9   ALA   A C   
14   O O   . ALA   A 3   ? 0.3069 0.3104 0.5438 0.0018  -0.0366 -0.0689 9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.2733 0.2767 0.5787 0.0068  -0.0441 -0.0863 9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2551 0.2670 0.5033 -0.0087 0.0027  -0.0661 10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2485 0.2599 0.4989 -0.0156 0.0210  -0.0659 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2536 0.2632 0.5638 -0.0192 0.0353  -0.0799 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2510 0.2589 0.5825 -0.0207 0.0458  -0.0838 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2519 0.2597 0.4597 -0.0220 0.0415  -0.0546 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2601 0.2714 0.4216 -0.0186 0.0288  -0.0425 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.2532 0.2548 0.4560 -0.0288 0.0586  -0.0552 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2624 0.2688 0.3893 -0.0230 0.0423  -0.0326 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.2607 0.2699 0.6006 -0.0211 0.0381  -0.0877 11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.2675 0.2745 0.6732 -0.0251 0.0548  -0.1027 11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.2856 0.2836 0.6801 -0.0345 0.0861  -0.1017 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3062 0.3057 0.6979 -0.0344 0.0805  -0.1021 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2538 0.2655 0.7154 -0.0177 0.0262  -0.1161 11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2721 0.2847 0.7433 -0.0084 -0.0051 -0.1195 11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2656 0.2793 0.7846 -0.0085 -0.0004 -0.1296 11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3042 0.3124 0.7310 0.0001  -0.0370 -0.1122 11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2777 0.2896 0.7996 0.0000  -0.0296 -0.1327 11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3249 0.3269 0.7495 0.0085  -0.0643 -0.1151 11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3144 0.3190 0.7868 0.0086  -0.0622 -0.1256 11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3502 0.3463 0.8183 0.0172  -0.0909 -0.1294 11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.2986 0.2828 0.6769 -0.0423 0.1188  -0.0991 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.3078 0.2733 0.6610 -0.0516 0.1508  -0.0976 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.3238 0.2724 0.7217 -0.0591 0.1881  -0.1095 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.3275 0.2701 0.7288 -0.0599 0.1979  -0.1089 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.3538 0.3063 0.6247 -0.0540 0.1552  -0.0812 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.3598 0.3074 0.6086 -0.0529 0.1567  -0.0741 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.3824 0.3076 0.6200 -0.0631 0.1858  -0.0806 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.3300 0.2712 0.7690 -0.0644 0.2092  -0.1214 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.3393 0.2627 0.8304 -0.0722 0.2492  -0.1349 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3494 0.2888 0.9148 -0.0675 0.2374  -0.1461 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3442 0.3081 0.9519 -0.0585 0.1991  -0.1518 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3500 0.2727 0.9264 -0.0728 0.2674  -0.1487 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3333 0.2713 0.9796 -0.0683 0.2547  -0.1595 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3345 0.2775 0.9267 -0.0629 0.2338  -0.1452 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3297 0.2687 0.9476 -0.0639 0.2445  -0.1490 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.3646 0.2844 1.0811 -0.0773 0.3010  -0.1756 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4205 0.3427 1.2116 -0.0804 0.3134  -0.1931 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4375 0.3819 1.3200 -0.0746 0.2890  -0.2094 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.4434 0.3412 1.1975 -0.0890 0.3486  -0.1907 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3347 0.2871 0.8577 -0.0571 0.2037  -0.1298 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3417 0.2995 0.8142 -0.0518 0.1834  -0.1165 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3002 0.2816 0.7655 -0.0409 0.1358  -0.1132 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.3061 0.2944 0.7681 -0.0384 0.1200  -0.1136 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3925 0.3301 0.7756 -0.0562 0.1986  -0.0989 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.4354 0.3381 0.8014 -0.0663 0.2443  -0.0989 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4478 0.3399 0.8437 -0.0689 0.2647  -0.1039 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4771 0.3521 0.7901 -0.0731 0.2675  -0.0934 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4919 0.3443 0.8622 -0.0782 0.3092  -0.1026 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.5257 0.3582 0.8091 -0.0821 0.3105  -0.0926 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.5425 0.3625 0.8539 -0.0848 0.3327  -0.0969 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.6143 0.3857 0.8934 -0.0940 0.3789  -0.0961 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2792 0.2686 0.7410 -0.0347 0.1154  -0.1107 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2652 0.2677 0.7063 -0.0248 0.0749  -0.1064 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2688 0.2686 0.6445 -0.0244 0.0761  -0.0903 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2764 0.2709 0.6556 -0.0264 0.0895  -0.0895 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2592 0.2685 0.7598 -0.0175 0.0497  -0.1206 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.3065 0.3189 0.7713 -0.0075 0.0123  -0.1153 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3256 0.3379 0.8468 0.0005  -0.0178 -0.1314 16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3572 0.3659 0.8505 0.0071  -0.0387 -0.1283 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4118 0.4120 0.8640 0.0159  -0.0712 -0.1250 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.4156 0.4102 0.8470 0.0192  -0.0870 -0.1228 16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4292 0.4225 0.8569 0.0212  -0.0859 -0.1235 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2588 0.2611 0.5789 -0.0223 0.0643  -0.0780 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2596 0.2602 0.5254 -0.0216 0.0637  -0.0639 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2522 0.2613 0.5046 -0.0130 0.0343  -0.0617 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2461 0.2577 0.4888 -0.0094 0.0176  -0.0616 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2810 0.2756 0.4966 -0.0258 0.0728  -0.0524 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2908 0.2835 0.4606 -0.0246 0.0697  -0.0395 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2880 0.2661 0.5071 -0.0345 0.1023  -0.0553 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2358 0.2453 0.4863 -0.0098 0.0295  -0.0606 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2444 0.2553 0.4771 -0.0020 0.0051  -0.0594 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2366 0.2478 0.4343 -0.0017 0.0103  -0.0485 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2358 0.2450 0.4291 -0.0065 0.0286  -0.0434 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.2620 0.2705 0.5376 0.0035  -0.0119 -0.0733 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.2826 0.2902 0.5990 0.0049  -0.0232 -0.0854 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2632 0.2725 0.5699 0.0001  0.0047  -0.0774 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2286 0.2380 0.4004 0.0042  -0.0055 -0.0454 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2245 0.2343 0.3743 0.0053  -0.0015 -0.0378 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.2314 0.2401 0.4102 0.0059  0.0013  -0.0445 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.2302 0.2351 0.4345 0.0099  -0.0125 -0.0557 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.2424 0.2451 0.3638 0.0114  -0.0158 -0.0363 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.2565 0.2582 0.3502 0.0108  -0.0163 -0.0299 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.2661 0.2604 0.3560 0.0131  -0.0272 -0.0339 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.2530 0.2607 0.3298 0.0080  -0.0056 -0.0202 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2207 0.2300 0.3955 0.0026  0.0163  -0.0382 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2248 0.2319 0.4284 0.0026  0.0215  -0.0442 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.2450 0.2502 0.4522 0.0097  0.0030  -0.0508 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.2596 0.2626 0.5022 0.0115  -0.0035 -0.0624 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2388 0.2420 0.4269 -0.0010 0.0383  -0.0343 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2480 0.2457 0.4653 -0.0026 0.0500  -0.0394 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2828 0.2731 0.4725 -0.0040 0.0603  -0.0274 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.3149 0.2947 0.5238 -0.0065 0.0758  -0.0293 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3439 0.3268 0.5699 -0.0030 0.0710  -0.0331 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3256 0.3189 0.5502 0.0031  0.0514  -0.0364 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3696 0.3411 0.6113 -0.0059 0.0874  -0.0337 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.2558 0.2588 0.4269 0.0136  -0.0053 -0.0448 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.2560 0.2495 0.4194 0.0201  -0.0202 -0.0507 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.2997 0.2811 0.4703 0.0254  -0.0429 -0.0627 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.3237 0.2916 0.4909 0.0310  -0.0582 -0.0705 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.2716 0.2610 0.3955 0.0221  -0.0175 -0.0420 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.2868 0.2696 0.3805 0.0233  -0.0223 -0.0386 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.2908 0.2836 0.3778 0.0188  -0.0127 -0.0301 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.3201 0.2830 0.3858 0.0285  -0.0350 -0.0428 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.3210 0.3035 0.3818 0.0210  -0.0182 -0.0293 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.3352 0.2973 0.3795 0.0268  -0.0310 -0.0364 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.2974 0.2807 0.4766 0.0240  -0.0471 -0.0647 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.3257 0.2955 0.5149 0.0296  -0.0720 -0.0762 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.3348 0.3130 0.5869 0.0274  -0.0738 -0.0883 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.3573 0.3266 0.6289 0.0319  -0.0959 -0.0988 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.3298 0.2925 0.4849 0.0305  -0.0772 -0.0705 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.3740 0.3229 0.4715 0.0329  -0.0750 -0.0612 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.3753 0.3148 0.4434 0.0334  -0.0787 -0.0566 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.3973 0.3199 0.4703 0.0403  -0.0920 -0.0679 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.3320 0.3242 0.6160 0.0205  -0.0496 -0.0869 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.3369 0.3347 0.6842 0.0171  -0.0436 -0.0988 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.3614 0.3519 0.7518 0.0235  -0.0685 -0.1158 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.3698 0.3546 0.7462 0.0271  -0.0756 -0.1161 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3337 0.3383 0.6947 0.0086  -0.0099 -0.0933 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.3754 0.3635 0.8124 0.0262  -0.0864 -0.1297 24  THR   A N   
135  C CA  . THR   A 18  ? 0.4009 0.3794 0.8849 0.0335  -0.1173 -0.1481 24  THR   A CA  
136  C C   . THR   A 18  ? 0.3968 0.3859 0.9528 0.0283  -0.0984 -0.1588 24  THR   A C   
137  O O   . THR   A 18  ? 0.3931 0.3925 0.9543 0.0191  -0.0602 -0.1508 24  THR   A O   
138  C CB  . THR   A 18  ? 0.4212 0.3923 0.9347 0.0386  -0.1453 -0.1596 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4198 0.4066 0.9989 0.0310  -0.1220 -0.1660 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.4604 0.4183 0.9037 0.0428  -0.1597 -0.1486 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.3969 0.3794 1.0069 0.0343  -0.1256 -0.1773 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.3827 0.3742 1.0700 0.0293  -0.1076 -0.1895 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.3562 0.3588 1.1089 0.0210  -0.0798 -0.1959 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.3526 0.3611 1.1342 0.0118  -0.0400 -0.1946 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.3951 0.3765 1.1314 0.0381  -0.1465 -0.2097 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.4399 0.4307 1.2523 0.0324  -0.1243 -0.2209 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.4865 0.4803 1.2727 0.0276  -0.0969 -0.2106 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.4228 0.4202 1.3377 0.0297  -0.1201 -0.2406 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.4649 0.4645 1.3341 0.0226  -0.0787 -0.2243 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.4279 0.4305 1.3792 0.0232  -0.0903 -0.2430 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.3579 0.3594 1.1279 0.0240  -0.0980 -0.2021 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3425 0.3526 1.1725 0.0159  -0.0695 -0.2085 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3549 0.3683 1.1352 0.0045  -0.0190 -0.1895 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3527 0.3669 1.1789 -0.0049 0.0201  -0.1941 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.3751 0.3824 1.2181 0.0218  -0.0993 -0.2152 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4225 0.4375 1.3561 0.0156  -0.0788 -0.2300 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.4280 0.4458 1.4565 0.0156  -0.0814 -0.2504 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.4333 0.4509 1.3434 0.0100  -0.0569 -0.2213 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3562 0.3673 1.0423 0.0056  -0.0200 -0.1691 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3391 0.3494 0.9696 -0.0032 0.0186  -0.1508 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3174 0.3229 0.9530 -0.0104 0.0536  -0.1470 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.3156 0.3131 0.9460 -0.0196 0.0919  -0.1418 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3440 0.3533 0.8846 0.0007  0.0048  -0.1325 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3405 0.3500 0.8617 0.0048  -0.0166 -0.1315 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3338 0.3452 0.8882 0.0006  -0.0051 -0.1372 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.3482 0.3529 0.8237 0.0123  -0.0441 -0.1264 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3115 0.3171 0.9460 -0.0062 0.0415  -0.1480 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3341 0.3329 0.9737 -0.0126 0.0737  -0.1443 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3354 0.3304 1.0623 -0.0192 0.1003  -0.1612 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3461 0.3275 1.0697 -0.0280 0.1415  -0.1561 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3332 0.3334 0.9564 -0.0064 0.0545  -0.1426 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3521 0.3519 0.8898 -0.0034 0.0465  -0.1236 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3734 0.3757 0.8719 0.0049  0.0137  -0.1207 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3661 0.3590 0.8503 -0.0083 0.0720  -0.1059 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3905 0.3917 0.8222 0.0047  0.0201  -0.1031 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3876 0.3841 0.8114 -0.0028 0.0525  -0.0940 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3715 0.3508 0.8507 -0.0167 0.1092  -0.0992 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.4053 0.3970 0.7740 -0.0049 0.0658  -0.0769 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3980 0.3680 0.8130 -0.0181 0.1195  -0.0812 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.4110 0.3895 0.7756 -0.0121 0.0964  -0.0707 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3178 0.3207 1.1209 -0.0152 0.0780  -0.1813 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3182 0.3188 1.2171 -0.0217 0.1037  -0.1998 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.3352 0.3277 1.2426 -0.0311 0.1421  -0.1989 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.3206 0.3089 1.3110 -0.0374 0.1686  -0.2152 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.2969 0.3075 1.2818 -0.0135 0.0630  -0.2233 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.3575 0.3466 1.1845 -0.0322 0.1452  -0.1816 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.3643 0.3427 1.1888 -0.0407 0.1792  -0.1802 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.3760 0.3405 1.0922 -0.0443 0.1957  -0.1561 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.3847 0.3463 1.0687 -0.0464 0.1997  -0.1506 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.3869 0.3791 1.2456 -0.0353 0.1489  -0.1904 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.4287 0.4303 1.4031 -0.0325 0.1343  -0.2162 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.4318 0.4274 1.4783 -0.0404 0.1686  -0.2300 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.4347 0.4478 1.4298 -0.0208 0.0822  -0.2244 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.3670 0.3223 1.0312 -0.0447 0.2029  -0.1429 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.3780 0.3194 0.9439 -0.0463 0.2109  -0.1209 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.3910 0.3010 0.9195 -0.0566 0.2549  -0.1140 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.3864 0.2743 0.9492 -0.0646 0.2943  -0.1217 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.3671 0.3051 0.9015 -0.0435 0.2067  -0.1113 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.3975 0.3201 0.8390 -0.0441 0.2108  -0.0897 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.4024 0.3439 0.7986 -0.0370 0.1752  -0.0807 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.4004 0.3173 0.8258 -0.0419 0.2109  -0.0829 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.3953 0.2995 0.8505 -0.0564 0.2484  -0.0999 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.4158 0.2849 0.8140 -0.0646 0.2823  -0.0910 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.4577 0.3077 0.7671 -0.0630 0.2777  -0.0710 32  VAL   A C   
205  O O   . VAL   A 26  ? 0.5089 0.3199 0.7795 -0.0690 0.3088  -0.0645 32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.4282 0.3022 0.8172 -0.0657 0.2774  -0.0926 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.4718 0.3038 0.7928 -0.0739 0.3107  -0.0835 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.4032 0.2936 0.8840 -0.0668 0.2809  -0.1129 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.4275 0.3025 0.7068 -0.0547 0.2386  -0.0619 33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.4398 0.3014 0.6476 -0.0522 0.2291  -0.0448 33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.4024 0.2992 0.6114 -0.0427 0.1886  -0.0411 33  TRP   A C   
212  O O   . TRP   A 27  ? 0.3770 0.3002 0.6134 -0.0387 0.1674  -0.0476 33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.4726 0.3070 0.6127 -0.0559 0.2369  -0.0349 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.5020 0.3296 0.5752 -0.0513 0.2148  -0.0189 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.5524 0.3436 0.5700 -0.0523 0.2231  -0.0075 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.4837 0.3387 0.5421 -0.0451 0.1809  -0.0134 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.5671 0.3639 0.5423 -0.0465 0.1934  0.0038  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.5238 0.3600 0.5248 -0.0426 0.1698  0.0001  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.4592 0.3485 0.5464 -0.0415 0.1599  -0.0188 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.5152 0.3695 0.4963 -0.0372 0.1403  0.0070  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.4562 0.3601 0.5157 -0.0366 0.1338  -0.0108 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.4814 0.3699 0.4933 -0.0347 0.1250  0.0013  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.3913 0.2847 0.5714 -0.0392 0.1798  -0.0313 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.3724 0.2932 0.5486 -0.0310 0.1471  -0.0274 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.3935 0.3009 0.5167 -0.0289 0.1411  -0.0127 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.4340 0.3122 0.5339 -0.0321 0.1592  -0.0070 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.3595 0.3011 0.5891 -0.0265 0.1356  -0.0382 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.3840 0.3120 0.6350 -0.0287 0.1540  -0.0408 34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.4409 0.3619 0.6575 -0.0256 0.1491  -0.0292 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.4289 0.3277 0.6450 -0.0291 0.1705  -0.0273 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.4055 0.3406 0.5972 -0.0199 0.1257  -0.0222 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.3706 0.2957 0.4749 -0.0235 0.1160  -0.0066 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.3708 0.2868 0.4370 -0.0205 0.1063  0.0055  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.3303 0.2753 0.4126 -0.0136 0.0835  0.0050  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.3073 0.2689 0.3897 -0.0116 0.0704  0.0038  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.4139 0.3096 0.4319 -0.0228 0.1047  0.0141  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.4965 0.3768 0.4764 -0.0193 0.0910  0.0259  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.5167 0.4112 0.5115 -0.0143 0.0796  0.0279  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.5581 0.4100 0.4936 -0.0212 0.0903  0.0325  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.3119 0.2597 0.4069 -0.0104 0.0815  0.0052  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2901 0.2588 0.3969 -0.0043 0.0646  0.0041  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2945 0.2640 0.4015 -0.0043 0.0642  0.0038  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2953 0.2680 0.3772 -0.0019 0.0515  0.0128  36  SER   A C   
244  O O   . SER   A 30  ? 0.2940 0.2830 0.3816 0.0013  0.0409  0.0107  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2989 0.2644 0.4188 -0.0020 0.0675  0.0040  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.3152 0.2844 0.4391 -0.0016 0.0657  0.0023  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3078 0.2884 0.4340 0.0035  0.0541  0.0033  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.3621 0.3148 0.4634 -0.0015 0.0686  0.0126  36  SER   A OG  
249  N N   . SER   A 31  ? 0.3087 0.2621 0.3627 -0.0032 0.0522  0.0221  37  SER   A N   
250  C CA  . SER   A 31  ? 0.3167 0.2732 0.3559 -0.0004 0.0369  0.0289  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2973 0.2641 0.3319 -0.0020 0.0315  0.0271  37  SER   A C   
252  O O   . SER   A 31  ? 0.3059 0.2820 0.3415 0.0004  0.0196  0.0297  37  SER   A O   
253  C CB  . SER   A 31  ? 0.3819 0.3102 0.3902 -0.0003 0.0330  0.0384  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.4782 0.3839 0.4542 -0.0048 0.0379  0.0406  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2843 0.2488 0.3181 -0.0061 0.0412  0.0220  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2752 0.2492 0.3065 -0.0077 0.0369  0.0197  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2583 0.2514 0.3148 -0.0060 0.0357  0.0110  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2470 0.2473 0.3025 -0.0067 0.0319  0.0089  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.3048 0.2592 0.3170 -0.0134 0.0485  0.0192  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.3588 0.2852 0.3325 -0.0147 0.0466  0.0276  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.3755 0.2767 0.3251 -0.0208 0.0625  0.0261  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.3499 0.2621 0.2997 -0.0225 0.0573  0.0231  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.3970 0.2852 0.3137 -0.0266 0.0620  0.0244  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.4440 0.2912 0.3189 -0.0294 0.0723  0.0289  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.4070 0.3073 0.3277 -0.0280 0.0571  0.0213  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2514 0.2491 0.3283 -0.0035 0.0374  0.0056  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2334 0.2406 0.3289 -0.0011 0.0323  -0.0036 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2404 0.2458 0.3468 -0.0045 0.0364  -0.0100 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2304 0.2414 0.3429 -0.0024 0.0273  -0.0154 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2341 0.2492 0.3208 0.0029  0.0218  -0.0030 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.2427 0.2571 0.3370 0.0065  0.0136  -0.0122 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.2352 0.2467 0.3466 0.0084  0.0117  -0.0190 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.2393 0.2529 0.3213 0.0079  0.0077  -0.0127 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2426 0.2363 0.3514 -0.0098 0.0514  -0.0101 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2510 0.2422 0.3763 -0.0135 0.0589  -0.0175 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2565 0.2409 0.4172 -0.0161 0.0730  -0.0265 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2785 0.2523 0.4366 -0.0175 0.0842  -0.0236 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2702 0.2476 0.3672 -0.0191 0.0699  -0.0115 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2836 0.2681 0.3565 -0.0180 0.0573  -0.0059 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.3035 0.2695 0.3463 -0.0233 0.0667  -0.0012 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2722 0.2715 0.3644 -0.0154 0.0463  -0.0128 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2423 0.2313 0.4379 -0.0167 0.0725  -0.0376 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2579 0.2413 0.5003 -0.0199 0.0878  -0.0490 41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2743 0.2570 0.5408 -0.0234 0.0945  -0.0571 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2631 0.2566 0.5303 -0.0198 0.0756  -0.0592 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2555 0.2491 0.5364 -0.0140 0.0709  -0.0590 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2639 0.2535 0.6061 -0.0169 0.0847  -0.0731 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2700 0.2624 0.6285 -0.0125 0.0755  -0.0765 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2603 0.2569 0.6543 -0.0155 0.0737  -0.0882 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2871 0.2536 0.5712 -0.0309 0.1241  -0.0614 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.3149 0.2780 0.6289 -0.0355 0.1372  -0.0707 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.3258 0.2878 0.7122 -0.0378 0.1512  -0.0868 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.3322 0.2811 0.7256 -0.0412 0.1719  -0.0868 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.3513 0.2896 0.6186 -0.0433 0.1640  -0.0626 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.3599 0.2914 0.6629 -0.0491 0.1838  -0.0740 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.3645 0.3057 0.5693 -0.0404 0.1456  -0.0486 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.3212 0.2969 0.7644 -0.0349 0.1367  -0.1008 43  SER   A N   
298  C CA  . SER   A 37  ? 0.3189 0.2953 0.8455 -0.0368 0.1473  -0.1191 43  SER   A CA  
299  C C   . SER   A 37  ? 0.3357 0.3073 0.9039 -0.0425 0.1666  -0.1299 43  SER   A C   
300  O O   . SER   A 37  ? 0.3370 0.3089 0.8717 -0.0429 0.1624  -0.1241 43  SER   A O   
301  C CB  . SER   A 37  ? 0.3059 0.2996 0.8757 -0.0271 0.1086  -0.1296 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.3113 0.3153 0.8758 -0.0200 0.0744  -0.1313 43  SER   A OG  
303  N N   . SER   A 38  ? 0.3437 0.3088 0.9868 -0.0477 0.1920  -0.1459 44  SER   A N   
304  C CA  . SER   A 38  ? 0.3552 0.3140 1.0475 -0.0539 0.2157  -0.1581 44  SER   A CA  
305  C C   . SER   A 38  ? 0.3501 0.3311 1.1117 -0.0460 0.1782  -0.1735 44  SER   A C   
306  O O   . SER   A 38  ? 0.3438 0.3383 1.1412 -0.0377 0.1441  -0.1809 44  SER   A O   
307  C CB  . SER   A 38  ? 0.3676 0.3077 1.1196 -0.0633 0.2621  -0.1706 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3744 0.3283 1.1960 -0.0586 0.2454  -0.1832 44  SER   A OG  
309  N N   . THR   A 39  ? 0.3607 0.3416 1.1419 -0.0483 0.1835  -0.1792 45  THR   A N   
310  C CA  . THR   A 39  ? 0.3625 0.3601 1.2111 -0.0405 0.1471  -0.1941 45  THR   A CA  
311  C C   . THR   A 39  ? 0.3810 0.3739 1.3234 -0.0475 0.1775  -0.2141 45  THR   A C   
312  O O   . THR   A 39  ? 0.3992 0.3737 1.3273 -0.0586 0.2265  -0.2121 45  THR   A O   
313  C CB  . THR   A 39  ? 0.3922 0.3963 1.1807 -0.0344 0.1156  -0.1828 45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.4083 0.4033 1.1795 -0.0423 0.1459  -0.1800 45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.4189 0.4242 1.1118 -0.0297 0.0961  -0.1623 45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3784 0.3847 1.4117 -0.0405 0.1465  -0.2333 46  THR   A N   
317  C CA  . THR   A 40  ? 0.3832 0.3878 1.5198 -0.0461 0.1715  -0.2547 46  THR   A CA  
318  C C   . THR   A 40  ? 0.3997 0.4032 1.5192 -0.0476 0.1740  -0.2524 46  THR   A C   
319  O O   . THR   A 40  ? 0.4101 0.4026 1.5688 -0.0574 0.2183  -0.2613 46  THR   A O   
320  C CB  . THR   A 40  ? 0.3877 0.4061 1.6370 -0.0373 0.1332  -0.2779 46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4316 0.4591 1.6547 -0.0236 0.0702  -0.2746 46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3833 0.4018 1.6591 -0.0369 0.1348  -0.2826 46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.3958 0.4078 1.4561 -0.0381 0.1289  -0.2408 47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.3894 0.4011 1.4317 -0.0385 0.1266  -0.2380 47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4033 0.4055 1.3286 -0.0438 0.1459  -0.2146 47  ALA   A C   
326  O O   . ALA   A 41  ? 0.4234 0.4243 1.2745 -0.0422 0.1392  -0.1987 47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.3867 0.4089 1.4458 -0.0246 0.0649  -0.2421 47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.3858 0.3806 1.2982 -0.0500 0.1691  -0.2137 48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.4056 0.3893 1.2122 -0.0549 0.1852  -0.1936 48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.3706 0.3664 1.1162 -0.0453 0.1391  -0.1798 48  GLN   A C   
331  O O   . GLN   A 42  ? 0.3549 0.3599 1.1375 -0.0382 0.1080  -0.1870 48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.4569 0.4232 1.2685 -0.0657 0.2295  -0.1985 48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.5720 0.5103 1.2992 -0.0760 0.2726  -0.1853 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.6689 0.5859 1.3732 -0.0849 0.3071  -0.1866 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.6826 0.5838 1.4458 -0.0930 0.3471  -0.2022 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.7064 0.6200 1.3259 -0.0841 0.2944  -0.1711 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.3572 0.3493 1.0111 -0.0455 0.1372  -0.1605 49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.3405 0.3404 0.9299 -0.0382 0.1023  -0.1461 49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.3191 0.3127 0.8585 -0.0431 0.1149  -0.1374 49  GLY   A C   
340  O O   . GLY   A 43  ? 0.3405 0.3198 0.8784 -0.0526 0.1524  -0.1403 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.2870 0.2877 0.7859 -0.0367 0.0847  -0.1279 50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.2837 0.2802 0.7454 -0.0405 0.0924  -0.1218 50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.2866 0.2820 0.6650 -0.0406 0.0867  -0.1037 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.3073 0.3008 0.6572 -0.0425 0.0869  -0.0989 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2835 0.2865 0.7835 -0.0344 0.0671  -0.1292 50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.3101 0.3150 0.9219 -0.0338 0.0705  -0.1529 50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.2816 0.2784 0.6267 -0.0384 0.0807  -0.0948 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.3062 0.3024 0.5825 -0.0384 0.0755  -0.0794 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.3293 0.3087 0.5686 -0.0477 0.1055  -0.0752 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.3395 0.3049 0.5929 -0.0534 0.1319  -0.0810 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.3139 0.3158 0.5711 -0.0327 0.0594  -0.0723 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.3414 0.3504 0.6161 -0.0231 0.0276  -0.0750 51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.3594 0.3686 0.6364 -0.0202 0.0136  -0.0761 51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.3264 0.3368 0.6074 -0.0183 0.0161  -0.0758 51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.3316 0.3081 0.5238 -0.0492 0.1018  -0.0662 52  THR   A N   
356  C CA  . THR   A 46  ? 0.3652 0.3206 0.5098 -0.0563 0.1218  -0.0611 52  THR   A CA  
357  C C   . THR   A 46  ? 0.3589 0.3158 0.4588 -0.0533 0.1080  -0.0486 52  THR   A C   
358  O O   . THR   A 46  ? 0.3467 0.3201 0.4403 -0.0480 0.0855  -0.0428 52  THR   A O   
359  C CB  . THR   A 46  ? 0.4278 0.3781 0.5540 -0.0595 0.1228  -0.0611 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.4429 0.3869 0.6091 -0.0636 0.1415  -0.0734 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.4749 0.4011 0.5385 -0.0647 0.1320  -0.0539 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.3715 0.3082 0.4414 -0.0567 0.1224  -0.0448 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.3731 0.3080 0.4035 -0.0540 0.1094  -0.0338 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.3929 0.3134 0.3765 -0.0566 0.1044  -0.0282 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.4215 0.3164 0.3830 -0.0626 0.1214  -0.0317 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.3940 0.3083 0.4097 -0.0561 0.1252  -0.0320 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.3860 0.3115 0.4548 -0.0547 0.1335  -0.0402 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4018 0.3167 0.3837 -0.0520 0.1076  -0.0210 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.3637 0.3208 0.4638 -0.0466 0.1071  -0.0399 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.3607 0.2957 0.3318 -0.0522 0.0817  -0.0207 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.3640 0.2875 0.2986 -0.0536 0.0717  -0.0163 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.3944 0.2839 0.2817 -0.0558 0.0759  -0.0120 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.3937 0.2799 0.2787 -0.0536 0.0769  -0.0084 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.3506 0.2987 0.2949 -0.0482 0.0487  -0.0105 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.4228 0.2829 0.2683 -0.0596 0.0767  -0.0123 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.4707 0.2895 0.2595 -0.0605 0.0748  -0.0075 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.4946 0.3096 0.2608 -0.0585 0.0476  -0.0048 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.5225 0.3165 0.2626 -0.0623 0.0490  -0.0087 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.5242 0.2963 0.2739 -0.0674 0.1044  -0.0119 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.5488 0.3256 0.3337 -0.0703 0.1342  -0.0172 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.5679 0.3518 0.3647 -0.0667 0.1332  -0.0124 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.5669 0.3587 0.4084 -0.0694 0.1598  -0.0198 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.5795 0.3861 0.4499 -0.0665 0.1608  -0.0186 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5605 0.3748 0.4170 -0.0609 0.1393  -0.0098 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5803 0.3942 0.4981 -0.0690 0.1829  -0.0273 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.4863 0.3232 0.2695 -0.0527 0.0232  0.0006  56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.4784 0.3232 0.2639 -0.0501 -0.0038 0.0015  56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.4645 0.3226 0.2659 -0.0439 -0.0260 0.0071  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.4537 0.3171 0.2630 -0.0416 -0.0197 0.0106  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.4419 0.3241 0.2728 -0.0508 -0.0015 -0.0024 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.3705 0.2969 0.2564 -0.0464 0.0026  -0.0002 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.4577 0.3245 0.2729 -0.0413 -0.0510 0.0067  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.4474 0.3319 0.2928 -0.0357 -0.0703 0.0099  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.4025 0.3276 0.3036 -0.0350 -0.0719 0.0074  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.3976 0.3340 0.3284 -0.0316 -0.0900 0.0072  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.5193 0.3721 0.3371 -0.0324 -0.1008 0.0107  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.6331 0.4741 0.4436 -0.0337 -0.1194 0.0052  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.6353 0.4962 0.4656 -0.0375 -0.1070 0.0012  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.7144 0.5243 0.4995 -0.0304 -0.1486 0.0046  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.3699 0.3147 0.2877 -0.0379 -0.0522 0.0052  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.3231 0.2990 0.2854 -0.0372 -0.0503 0.0038  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2999 0.2940 0.2934 -0.0329 -0.0520 0.0068  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2997 0.2917 0.2857 -0.0308 -0.0468 0.0100  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.3150 0.3026 0.2837 -0.0395 -0.0307 0.0022  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.3525 0.3268 0.3023 -0.0449 -0.0265 -0.0031 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.2695 0.2808 0.3002 -0.0321 -0.0558 0.0051  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.2609 0.2886 0.3253 -0.0289 -0.0514 0.0067  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.2582 0.3009 0.3454 -0.0300 -0.0344 0.0057  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.2472 0.2994 0.3640 -0.0284 -0.0278 0.0056  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.2761 0.3045 0.3700 -0.0264 -0.0707 0.0049  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.3179 0.3313 0.3932 -0.0230 -0.0852 0.0078  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.3529 0.3677 0.4661 -0.0195 -0.1072 0.0052  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.3749 0.3721 0.4797 -0.0185 -0.1328 0.0025  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.3075 0.3408 0.4648 -0.0172 -0.0983 0.0048  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.2417 0.2824 0.3143 -0.0329 -0.0265 0.0045  60  THR   A N   
416  C CA  . THR   A 54  ? 0.2345 0.2813 0.3171 -0.0334 -0.0110 0.0046  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2419 0.2830 0.2976 -0.0333 -0.0040 0.0052  60  THR   A C   
418  O O   . THR   A 54  ? 0.2540 0.2882 0.2911 -0.0352 -0.0081 0.0037  60  THR   A O   
419  C CB  . THR   A 54  ? 0.2613 0.3112 0.3648 -0.0365 -0.0109 0.0014  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.2999 0.3434 0.3844 -0.0393 -0.0183 -0.0009 60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.2463 0.3022 0.3869 -0.0365 -0.0211 -0.0015 60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2355 0.2758 0.2894 -0.0310 0.0066  0.0066  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2215 0.2558 0.2579 -0.0296 0.0093  0.0059  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2197 0.2459 0.2499 -0.0261 0.0166  0.0072  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2407 0.2635 0.2768 -0.0263 0.0244  0.0088  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2186 0.2377 0.2366 -0.0232 0.0142  0.0058  62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2457 0.2483 0.2479 -0.0188 0.0162  0.0066  62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2505 0.2493 0.2467 -0.0144 0.0106  0.0049  62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2476 0.2537 0.2534 -0.0150 0.0050  0.0015  62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2831 0.2759 0.2786 -0.0184 0.0121  0.0048  62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.3126 0.2802 0.2836 -0.0122 0.0084  0.0054  62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2901 0.2853 0.2920 -0.0227 0.0185  0.0062  62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2600 0.2454 0.2413 -0.0105 0.0138  0.0066  63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2552 0.2350 0.2309 -0.0059 0.0062  0.0038  63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2868 0.2381 0.2347 0.0000  -0.0009 0.0024  63  TYR   A C   
436  O O   . TYR   A 57  ? 0.3136 0.2445 0.2381 0.0008  0.0064  0.0056  63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2414 0.2281 0.2222 -0.0057 0.0121  0.0055  63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2674 0.2367 0.2304 -0.0036 0.0230  0.0080  63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2829 0.2525 0.2520 -0.0070 0.0369  0.0109  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2816 0.2323 0.2240 0.0014  0.0212  0.0064  63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.3007 0.2517 0.2571 -0.0060 0.0528  0.0122  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3152 0.2455 0.2380 0.0027  0.0355  0.0081  63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3258 0.2553 0.2556 -0.0012 0.0533  0.0110  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3639 0.2693 0.2765 -0.0008 0.0730  0.0118  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2848 0.2304 0.2338 0.0045  -0.0148 -0.0027 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.3297 0.2425 0.2488 0.0117  -0.0279 -0.0051 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3461 0.2421 0.2411 0.0151  -0.0238 -0.0043 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.3397 0.2522 0.2542 0.0147  -0.0239 -0.0065 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.3323 0.2439 0.2700 0.0157  -0.0491 -0.0131 64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3854 0.2569 0.2883 0.0244  -0.0688 -0.0162 64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.4274 0.2676 0.2922 0.0270  -0.0711 -0.0124 64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.4181 0.2778 0.3204 0.0303  -0.0850 -0.0226 64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.4784 0.2717 0.2993 0.0358  -0.0911 -0.0146 64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4667 0.2828 0.3303 0.0391  -0.1074 -0.0261 64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.5109 0.2914 0.3299 0.0421  -0.1107 -0.0216 64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5861 0.3142 0.3562 0.0516  -0.1350 -0.0245 64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3756 0.2345 0.2256 0.0183  -0.0192 -0.0015 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4099 0.2436 0.2281 0.0215  -0.0119 -0.0012 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.4743 0.2617 0.2471 0.0303  -0.0337 -0.0055 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.5195 0.2671 0.2475 0.0331  -0.0344 -0.0029 65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4540 0.2747 0.2536 0.0176  0.0159  0.0048  65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5125 0.2926 0.2667 0.0208  0.0315  0.0046  65  CYS   A SG  
463  N N   . SER   A 60  ? 0.4734 0.2628 0.2571 0.0348  -0.0530 -0.0123 66  SER   A N   
464  C CA  . SER   A 60  ? 0.5364 0.2818 0.2828 0.0441  -0.0808 -0.0183 66  SER   A CA  
465  C C   . SER   A 60  ? 0.5942 0.2812 0.2658 0.0484  -0.0735 -0.0156 66  SER   A C   
466  O O   . SER   A 60  ? 0.6426 0.2784 0.2626 0.0555  -0.0924 -0.0169 66  SER   A O   
467  C CB  . SER   A 60  ? 0.5607 0.3217 0.3427 0.0477  -0.1029 -0.0277 66  SER   A CB  
468  O OG  . SER   A 60  ? 0.6139 0.3788 0.3928 0.0470  -0.0913 -0.0281 66  SER   A OG  
469  N N   . SER   A 61  ? 0.5814 0.2718 0.2453 0.0441  -0.0448 -0.0119 67  SER   A N   
470  C CA  . SER   A 61  ? 0.6257 0.2593 0.2200 0.0465  -0.0284 -0.0096 67  SER   A CA  
471  C C   . SER   A 61  ? 0.6722 0.2692 0.2222 0.0446  -0.0092 -0.0027 67  SER   A C   
472  O O   . SER   A 61  ? 0.7596 0.2968 0.2408 0.0470  0.0052  -0.0010 67  SER   A O   
473  C CB  . SER   A 61  ? 0.6152 0.2660 0.2252 0.0420  -0.0012 -0.0090 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.6067 0.3008 0.2643 0.0334  0.0256  -0.0036 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.6416 0.2689 0.2267 0.0404  -0.0083 0.0008  68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.6802 0.2732 0.2272 0.0389  0.0068  0.0069  68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.6977 0.2850 0.2439 0.0432  -0.0230 0.0062  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.7291 0.2870 0.2439 0.0425  -0.0138 0.0114  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.6339 0.2666 0.2267 0.0288  0.0410  0.0119  68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.6513 0.2826 0.2463 0.0245  0.0744  0.0124  68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.7233 0.2819 0.2419 0.0259  0.0989  0.0149  68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.7523 0.3070 0.2774 0.0212  0.1351  0.0142  68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.7927 0.3240 0.2897 0.0247  0.1367  0.0103  68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.7862 0.2980 0.2488 0.0329  0.1018  0.0065  68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.8058 0.3344 0.3148 0.0199  0.1724  0.0092  68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.6703 0.2898 0.2605 0.0467  -0.0553 -0.0005 69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.6669 0.2922 0.2768 0.0499  -0.0826 -0.0031 69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.6431 0.2976 0.2818 0.0419  -0.0614 0.0030  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.6785 0.3091 0.2970 0.0441  -0.0699 0.0052  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.7389 0.2932 0.2792 0.0604  -0.1101 -0.0043 69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.8039 0.3317 0.3251 0.0694  -0.1412 -0.0130 69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.9010 0.3593 0.3598 0.0808  -0.1774 -0.0155 69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.9742 0.3968 0.4043 0.0902  -0.2083 -0.0242 69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.0660 0.4092 0.4016 0.0977  -0.2166 -0.0233 69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.0941 0.3826 0.3532 0.0967  -0.1935 -0.0136 69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.1011 0.4150 0.4159 0.1061  -0.2471 -0.0327 69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.5922 0.2941 0.2748 0.0330  -0.0346 0.0056  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.5550 0.2829 0.2651 0.0254  -0.0155 0.0103  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.4901 0.2801 0.2671 0.0185  -0.0099 0.0086  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.4866 0.2976 0.2834 0.0176  -0.0078 0.0064  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.6258 0.3300 0.3063 0.0210  0.0186  0.0165  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.7883 0.4268 0.3991 0.0252  0.0227  0.0206  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.8882 0.5247 0.5032 0.0177  0.0554  0.0263  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 1.0154 0.5773 0.5522 0.0208  0.0699  0.0311  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 1.0986 0.6116 0.5764 0.0260  0.0730  0.0300  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.4505 0.2654 0.2578 0.0137  -0.0074 0.0096  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.4133 0.2774 0.2727 0.0069  -0.0011 0.0085  71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.4298 0.2999 0.2944 0.0007  0.0239  0.0133  71  HIS   A C   
509  O O   . HIS   A 65  ? 0.4768 0.3240 0.3210 -0.0002 0.0341  0.0166  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.3767 0.2600 0.2648 0.0053  -0.0137 0.0052  71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.3947 0.2728 0.2902 0.0111  -0.0375 -0.0015 71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3843 0.2917 0.3192 0.0093  -0.0427 -0.0072 71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.4294 0.2731 0.2993 0.0188  -0.0575 -0.0040 71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.3911 0.2855 0.3321 0.0154  -0.0640 -0.0139 71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.4343 0.2902 0.3365 0.0219  -0.0765 -0.0124 71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.3838 0.2816 0.2773 -0.0032 0.0338  0.0133  72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.3671 0.2717 0.2765 -0.0086 0.0552  0.0160  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.3288 0.2723 0.2829 -0.0140 0.0519  0.0146  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2900 0.2542 0.2605 -0.0139 0.0418  0.0128  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.3801 0.2776 0.2867 -0.0081 0.0699  0.0164  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.4371 0.2877 0.2926 -0.0037 0.0797  0.0178  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.4755 0.2937 0.3074 -0.0055 0.1019  0.0206  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.4621 0.2967 0.2912 0.0020  0.0689  0.0158  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.5285 0.2938 0.3026 -0.0016 0.1136  0.0220  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.5170 0.3010 0.2905 0.0064  0.0771  0.0166  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.5616 0.3088 0.3041 0.0045  0.1004  0.0200  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.6325 0.3191 0.3082 0.0089  0.1104  0.0210  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.3303 0.2793 0.3018 -0.0187 0.0614  0.0153  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.3133 0.2931 0.3234 -0.0234 0.0564  0.0134  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.3194 0.3109 0.3549 -0.0243 0.0630  0.0129  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.3407 0.3183 0.3772 -0.0243 0.0810  0.0136  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.3248 0.3019 0.3456 -0.0275 0.0643  0.0133  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.3656 0.3105 0.3600 -0.0260 0.0826  0.0162  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.3504 0.2731 0.3052 -0.0198 0.0778  0.0177  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2895 0.3020 0.3433 -0.0248 0.0496  0.0116  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2882 0.3113 0.3687 -0.0248 0.0513  0.0109  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2654 0.3066 0.3711 -0.0269 0.0351  0.0090  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2575 0.3016 0.3494 -0.0280 0.0224  0.0087  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.3180 0.3372 0.3825 -0.0206 0.0500  0.0120  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3592 0.3544 0.3990 -0.0179 0.0661  0.0129  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.3153 0.3388 0.3619 -0.0191 0.0347  0.0120  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2251 0.2747 0.3663 -0.0271 0.0350  0.0072  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2067 0.2670 0.3691 -0.0273 0.0149  0.0054  75  SER   A CA  
544  C C   . SER   A 69  ? 0.2132 0.2738 0.3685 -0.0236 0.0111  0.0077  75  SER   A C   
545  O O   . SER   A 69  ? 0.2375 0.2954 0.3979 -0.0217 0.0259  0.0081  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2255 0.2934 0.4395 -0.0288 0.0146  0.0008  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3263 0.3941 0.5527 -0.0326 0.0186  -0.0020 75  SER   A OG  
548  N N   . PHE   A 70  ? 0.1996 0.2596 0.3404 -0.0226 -0.0067 0.0089  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.1978 0.2563 0.3298 -0.0192 -0.0099 0.0114  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2200 0.2753 0.3569 -0.0178 -0.0313 0.0117  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.2399 0.2894 0.3711 -0.0195 -0.0461 0.0103  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2065 0.2586 0.3017 -0.0186 -0.0037 0.0135  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2147 0.2607 0.2849 -0.0213 -0.0095 0.0132  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2048 0.2503 0.2686 -0.0235 -0.0032 0.0116  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2385 0.2754 0.2893 -0.0216 -0.0190 0.0144  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2322 0.2719 0.2773 -0.0262 -0.0066 0.0103  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2495 0.2766 0.2767 -0.0248 -0.0195 0.0132  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2344 0.2647 0.2616 -0.0271 -0.0130 0.0107  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2078 0.2637 0.3556 -0.0144 -0.0343 0.0131  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2243 0.2723 0.3757 -0.0119 -0.0570 0.0139  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2545 0.2832 0.3554 -0.0123 -0.0658 0.0177  77  SER   A C   
562  O O   . SER   A 71  ? 0.2593 0.2854 0.3319 -0.0145 -0.0521 0.0189  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2330 0.2868 0.4151 -0.0080 -0.0564 0.0140  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2547 0.3071 0.4139 -0.0068 -0.0425 0.0173  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2718 0.2826 0.3612 -0.0100 -0.0890 0.0189  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.3214 0.3053 0.3567 -0.0108 -0.0930 0.0227  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.3191 0.3010 0.3443 -0.0088 -0.0819 0.0268  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.3131 0.3083 0.3707 -0.0054 -0.0821 0.0270  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3845 0.3394 0.3990 -0.0084 -0.1230 0.0231  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4659 0.4124 0.4672 -0.0118 -0.1313 0.0190  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.5808 0.4868 0.5409 -0.0099 -0.1609 0.0189  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.6483 0.5439 0.5834 -0.0147 -0.1596 0.0150  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.7187 0.5801 0.6292 -0.0124 -0.1939 0.0119  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3389 0.3037 0.3234 -0.0112 -0.0704 0.0292  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3404 0.3032 0.3196 -0.0096 -0.0591 0.0321  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3401 0.2908 0.3225 -0.0046 -0.0762 0.0359  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3750 0.2977 0.3312 -0.0031 -0.0963 0.0382  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3848 0.3242 0.3215 -0.0137 -0.0459 0.0329  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4065 0.3488 0.3378 -0.0178 -0.0427 0.0289  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3583 0.3031 0.3032 -0.0157 -0.0651 0.0283  79  PRO   A CD  
581  N N   A SER   A 74  ? 0.3138 0.2830 0.3277 -0.0017 -0.0700 0.0360  80  SER   A N   
582  N N   B SER   A 74  ? 0.3156 0.2841 0.3290 -0.0016 -0.0705 0.0361  80  SER   A N   
583  C CA  A SER   A 74  ? 0.3215 0.2861 0.3530 0.0035  -0.0856 0.0384  80  SER   A CA  
584  C CA  B SER   A 74  ? 0.3281 0.2883 0.3533 0.0035  -0.0867 0.0390  80  SER   A CA  
585  C C   A SER   A 74  ? 0.3196 0.2909 0.3599 0.0054  -0.0718 0.0400  80  SER   A C   
586  C C   B SER   A 74  ? 0.3217 0.2920 0.3606 0.0054  -0.0723 0.0401  80  SER   A C   
587  O O   A SER   A 74  ? 0.3093 0.2936 0.3505 0.0030  -0.0515 0.0379  80  SER   A O   
588  O O   B SER   A 74  ? 0.3116 0.2948 0.3513 0.0030  -0.0519 0.0380  80  SER   A O   
589  C CB  A SER   A 74  ? 0.3192 0.3064 0.4041 0.0057  -0.0947 0.0338  80  SER   A CB  
590  C CB  B SER   A 74  ? 0.3388 0.3138 0.4106 0.0064  -0.1039 0.0353  80  SER   A CB  
591  O OG  A SER   A 74  ? 0.3631 0.3513 0.4505 0.0033  -0.1032 0.0306  80  SER   A OG  
592  O OG  B SER   A 74  ? 0.3989 0.3607 0.4577 0.0054  -0.1218 0.0337  80  SER   A OG  
593  N N   . LEU   A 75  ? 0.3288 0.2909 0.3788 0.0102  -0.0854 0.0429  81  LEU   A N   
594  C CA  . LEU   A 75  ? 0.3412 0.3102 0.4048 0.0124  -0.0743 0.0439  81  LEU   A CA  
595  C C   . LEU   A 75  ? 0.3214 0.3193 0.4400 0.0144  -0.0701 0.0387  81  LEU   A C   
596  O O   . LEU   A 75  ? 0.3185 0.3197 0.4705 0.0175  -0.0866 0.0371  81  LEU   A O   
597  C CB  . LEU   A 75  ? 0.3770 0.3174 0.4228 0.0168  -0.0928 0.0499  81  LEU   A CB  
598  C CG  . LEU   A 75  ? 0.4282 0.3640 0.4734 0.0189  -0.0835 0.0528  81  LEU   A CG  
599  C CD1 . LEU   A 75  ? 0.4453 0.3745 0.4601 0.0143  -0.0603 0.0533  81  LEU   A CD1 
600  C CD2 . LEU   A 75  ? 0.4612 0.3628 0.4858 0.0240  -0.1071 0.0593  81  LEU   A CD2 
601  N N   . ILE   A 76  ? 0.3018 0.3170 0.4300 0.0126  -0.0480 0.0351  82  ILE   A N   
602  C CA  . ILE   A 76  ? 0.2983 0.3330 0.4669 0.0133  -0.0372 0.0298  82  ILE   A CA  
603  C C   . ILE   A 76  ? 0.3112 0.3501 0.4871 0.0151  -0.0219 0.0281  82  ILE   A C   
604  O O   . ILE   A 76  ? 0.3028 0.3367 0.4517 0.0141  -0.0139 0.0288  82  ILE   A O   
605  C CB  . ILE   A 76  ? 0.3085 0.3516 0.4716 0.0093  -0.0257 0.0263  82  ILE   A CB  
606  C CG1 . ILE   A 76  ? 0.3331 0.3732 0.4970 0.0077  -0.0417 0.0268  82  ILE   A CG1 
607  C CG2 . ILE   A 76  ? 0.3029 0.3571 0.4935 0.0092  -0.0067 0.0211  82  ILE   A CG2 
608  C CD1 . ILE   A 76  ? 0.3671 0.4126 0.5210 0.0037  -0.0322 0.0244  82  ILE   A CD1 
609  N N   . PHE   A 77  ? 0.3148 0.3618 0.5310 0.0177  -0.0179 0.0249  83  PHE   A N   
610  C CA  . PHE   A 77  ? 0.3293 0.3778 0.5525 0.0195  -0.0027 0.0223  83  PHE   A CA  
611  C C   . PHE   A 77  ? 0.3209 0.3696 0.5241 0.0171  0.0170  0.0181  83  PHE   A C   
612  O O   . PHE   A 77  ? 0.3395 0.3908 0.5491 0.0151  0.0265  0.0150  83  PHE   A O   
613  C CB  . PHE   A 77  ? 0.3354 0.3906 0.6095 0.0222  0.0009  0.0183  83  PHE   A CB  
614  C CG  . PHE   A 77  ? 0.3639 0.4180 0.6436 0.0236  0.0198  0.0145  83  PHE   A CG  
615  C CD1 . PHE   A 77  ? 0.3683 0.4179 0.6464 0.0267  0.0138  0.0170  83  PHE   A CD1 
616  C CD2 . PHE   A 77  ? 0.3819 0.4341 0.6619 0.0218  0.0441  0.0084  83  PHE   A CD2 
617  C CE1 . PHE   A 77  ? 0.3796 0.4270 0.6619 0.0280  0.0304  0.0127  83  PHE   A CE1 
618  C CE2 . PHE   A 77  ? 0.4028 0.4479 0.6810 0.0232  0.0609  0.0042  83  PHE   A CE2 
619  C CZ  . PHE   A 77  ? 0.3912 0.4356 0.6713 0.0263  0.0532  0.0061  83  PHE   A CZ  
620  N N   . VAL   A 78  ? 0.2975 0.3403 0.4771 0.0178  0.0226  0.0175  84  VAL   A N   
621  C CA  . VAL   A 78  ? 0.2855 0.3225 0.4427 0.0170  0.0360  0.0127  84  VAL   A CA  
622  C C   . VAL   A 78  ? 0.2907 0.3217 0.4518 0.0198  0.0461  0.0087  84  VAL   A C   
623  O O   . VAL   A 78  ? 0.2813 0.3121 0.4445 0.0216  0.0404  0.0100  84  VAL   A O   
624  C CB  . VAL   A 78  ? 0.2818 0.3151 0.4085 0.0154  0.0300  0.0133  84  VAL   A CB  
625  C CG1 . VAL   A 78  ? 0.2821 0.3052 0.3865 0.0162  0.0380  0.0074  84  VAL   A CG1 
626  C CG2 . VAL   A 78  ? 0.2765 0.3135 0.3973 0.0124  0.0221  0.0166  84  VAL   A CG2 
627  N N   . GLU   A 79  ? 0.3042 0.3264 0.4632 0.0200  0.0625  0.0036  85  GLU   A N   
628  C CA  . GLU   A 79  ? 0.3275 0.3385 0.4855 0.0224  0.0748  -0.0014 85  GLU   A CA  
629  C C   . GLU   A 79  ? 0.3205 0.3223 0.4492 0.0243  0.0682  -0.0039 85  GLU   A C   
630  O O   . GLU   A 79  ? 0.3235 0.3232 0.4293 0.0235  0.0589  -0.0038 85  GLU   A O   
631  C CB  . GLU   A 79  ? 0.3914 0.3846 0.5381 0.0216  0.0968  -0.0067 85  GLU   A CB  
632  C CG  . GLU   A 79  ? 0.5278 0.5196 0.7098 0.0221  0.1145  -0.0102 85  GLU   A CG  
633  C CD  . GLU   A 79  ? 0.6687 0.6340 0.8308 0.0207  0.1421  -0.0161 85  GLU   A CD  
634  O OE1 . GLU   A 79  ? 0.7189 0.6645 0.8692 0.0222  0.1579  -0.0215 85  GLU   A OE1 
635  O OE2 . GLU   A 79  ? 0.6987 0.6587 0.8519 0.0179  0.1491  -0.0153 85  GLU   A OE2 
636  N N   . ALA   A 80  ? 0.3142 0.3101 0.4483 0.0268  0.0728  -0.0074 86  ALA   A N   
637  C CA  . ALA   A 80  ? 0.3214 0.3075 0.4339 0.0288  0.0661  -0.0118 86  ALA   A CA  
638  C C   . ALA   A 80  ? 0.3363 0.3002 0.4081 0.0297  0.0667  -0.0176 86  ALA   A C   
639  O O   . ALA   A 80  ? 0.3545 0.3007 0.4082 0.0295  0.0810  -0.0199 86  ALA   A O   
640  C CB  . ALA   A 80  ? 0.3159 0.2956 0.4394 0.0315  0.0735  -0.0159 86  ALA   A CB  
641  N N   . SER   A 81  ? 0.3181 0.2795 0.3767 0.0306  0.0519  -0.0204 87  SER   A N   
642  C CA  . SER   A 81  ? 0.3474 0.2847 0.3683 0.0328  0.0448  -0.0268 87  SER   A CA  
643  C C   . SER   A 81  ? 0.3708 0.3005 0.3911 0.0361  0.0308  -0.0345 87  SER   A C   
644  O O   . SER   A 81  ? 0.3625 0.3052 0.4098 0.0360  0.0314  -0.0343 87  SER   A O   
645  C CB  . SER   A 81  ? 0.3444 0.2902 0.3621 0.0306  0.0356  -0.0235 87  SER   A CB  
646  O OG  . SER   A 81  ? 0.3172 0.2822 0.3603 0.0291  0.0247  -0.0224 87  SER   A OG  
647  N N   . GLU   A 82  ? 0.3934 0.3008 0.3855 0.0393  0.0161  -0.0418 88  GLU   A N   
648  C CA  . GLU   A 82  ? 0.4136 0.3147 0.4138 0.0426  -0.0009 -0.0510 88  GLU   A CA  
649  C C   . GLU   A 82  ? 0.3643 0.2940 0.4080 0.0395  -0.0081 -0.0496 88  GLU   A C   
650  O O   . GLU   A 82  ? 0.3660 0.2968 0.4317 0.0409  -0.0178 -0.0569 88  GLU   A O   
651  C CB  . GLU   A 82  ? 0.5071 0.3730 0.4674 0.0478  -0.0200 -0.0603 88  GLU   A CB  
652  C CG  . GLU   A 82  ? 0.6756 0.5014 0.5792 0.0506  -0.0109 -0.0617 88  GLU   A CG  
653  C CD  . GLU   A 82  ? 0.8745 0.6617 0.7288 0.0552  -0.0290 -0.0668 88  GLU   A CD  
654  O OE1 . GLU   A 82  ? 0.8989 0.6979 0.7628 0.0540  -0.0384 -0.0639 88  GLU   A OE1 
655  O OE2 . GLU   A 82  ? 0.9533 0.6943 0.7561 0.0603  -0.0344 -0.0738 88  GLU   A OE2 
656  N N   . TYR   A 83  ? 0.3271 0.2767 0.3832 0.0350  -0.0019 -0.0410 89  TYR   A N   
657  C CA  . TYR   A 83  ? 0.2999 0.2682 0.3882 0.0315  -0.0045 -0.0398 89  TYR   A CA  
658  C C   . TYR   A 83  ? 0.2842 0.2701 0.3944 0.0276  0.0083  -0.0311 89  TYR   A C   
659  O O   . TYR   A 83  ? 0.2910 0.2836 0.4253 0.0252  0.0095  -0.0320 89  TYR   A O   
660  C CB  . TYR   A 83  ? 0.3054 0.2771 0.3874 0.0294  -0.0085 -0.0376 89  TYR   A CB  
661  C CG  . TYR   A 83  ? 0.3482 0.2982 0.4061 0.0339  -0.0243 -0.0456 89  TYR   A CG  
662  C CD1 . TYR   A 83  ? 0.3681 0.3090 0.4410 0.0373  -0.0424 -0.0571 89  TYR   A CD1 
663  C CD2 . TYR   A 83  ? 0.3938 0.3278 0.4135 0.0353  -0.0219 -0.0424 89  TYR   A CD2 
664  C CE1 . TYR   A 83  ? 0.4093 0.3251 0.4573 0.0425  -0.0624 -0.0647 89  TYR   A CE1 
665  C CE2 . TYR   A 83  ? 0.4342 0.3407 0.4232 0.0399  -0.0377 -0.0488 89  TYR   A CE2 
666  C CZ  . TYR   A 83  ? 0.4569 0.3532 0.4579 0.0441  -0.0601 -0.0599 89  TYR   A CZ  
667  O OH  . TYR   A 83  ? 0.5212 0.3844 0.4879 0.0499  -0.0806 -0.0664 89  TYR   A OH  
668  N N   . TYR   A 84  ? 0.2668 0.2566 0.3696 0.0271  0.0178  -0.0234 90  TYR   A N   
669  C CA  . TYR   A 84  ? 0.2626 0.2636 0.3819 0.0247  0.0251  -0.0148 90  TYR   A CA  
670  C C   . TYR   A 84  ? 0.2801 0.2805 0.4014 0.0269  0.0318  -0.0123 90  TYR   A C   
671  O O   . TYR   A 84  ? 0.2854 0.2802 0.3938 0.0281  0.0361  -0.0135 90  TYR   A O   
672  C CB  . TYR   A 84  ? 0.2498 0.2587 0.3653 0.0211  0.0260  -0.0065 90  TYR   A CB  
673  C CG  . TYR   A 84  ? 0.2445 0.2539 0.3590 0.0180  0.0229  -0.0082 90  TYR   A CG  
674  C CD1 . TYR   A 84  ? 0.2429 0.2510 0.3696 0.0150  0.0269  -0.0076 90  TYR   A CD1 
675  C CD2 . TYR   A 84  ? 0.2459 0.2545 0.3481 0.0178  0.0184  -0.0108 90  TYR   A CD2 
676  C CE1 . TYR   A 84  ? 0.2463 0.2533 0.3773 0.0117  0.0281  -0.0107 90  TYR   A CE1 
677  C CE2 . TYR   A 84  ? 0.2420 0.2515 0.3485 0.0150  0.0160  -0.0133 90  TYR   A CE2 
678  C CZ  . TYR   A 84  ? 0.2452 0.2546 0.3675 0.0117  0.0219  -0.0133 90  TYR   A CZ  
679  O OH  . TYR   A 84  ? 0.2586 0.2675 0.3894 0.0086  0.0230  -0.0172 90  TYR   A OH  
680  N N   . PRO   A 85  ? 0.2781 0.2827 0.4170 0.0270  0.0346  -0.0079 91  PRO   A N   
681  C CA  . PRO   A 85  ? 0.2754 0.2817 0.4249 0.0289  0.0403  -0.0049 91  PRO   A CA  
682  C C   . PRO   A 85  ? 0.2706 0.2843 0.4233 0.0274  0.0397  0.0019  91  PRO   A C   
683  O O   . PRO   A 85  ? 0.2649 0.2816 0.4079 0.0247  0.0344  0.0055  91  PRO   A O   
684  C CB  . PRO   A 85  ? 0.2778 0.2849 0.4448 0.0296  0.0397  -0.0012 91  PRO   A CB  
685  C CG  . PRO   A 85  ? 0.2971 0.3028 0.4588 0.0264  0.0362  0.0022  91  PRO   A CG  
686  C CD  . PRO   A 85  ? 0.2812 0.2863 0.4314 0.0250  0.0340  -0.0049 91  PRO   A CD  
687  N N   . ALA   A 86  ? 0.2712 0.2876 0.4419 0.0290  0.0452  0.0029  92  ALA   A N   
688  C CA  . ALA   A 86  ? 0.2836 0.3075 0.4684 0.0280  0.0426  0.0077  92  ALA   A CA  
689  C C   . ALA   A 86  ? 0.2927 0.3182 0.4789 0.0273  0.0282  0.0160  92  ALA   A C   
690  O O   . ALA   A 86  ? 0.3022 0.3230 0.4927 0.0289  0.0243  0.0189  92  ALA   A O   
691  C CB  . ALA   A 86  ? 0.2815 0.3076 0.4978 0.0301  0.0511  0.0056  92  ALA   A CB  
692  N N   . ARG   A 87  ? 0.2883 0.3156 0.4637 0.0248  0.0213  0.0194  93  ARG   A N   
693  C CA  . ARG   A 87  ? 0.2876 0.3074 0.4509 0.0239  0.0088  0.0267  93  ARG   A CA  
694  C C   . ARG   A 87  ? 0.3024 0.3239 0.4600 0.0219  0.0003  0.0293  93  ARG   A C   
695  O O   . ARG   A 87  ? 0.2950 0.3256 0.4591 0.0207  0.0062  0.0253  93  ARG   A O   
696  C CB  . ARG   A 87  ? 0.3116 0.3234 0.4511 0.0215  0.0135  0.0262  93  ARG   A CB  
697  C CG  . ARG   A 87  ? 0.3101 0.3250 0.4332 0.0180  0.0167  0.0227  93  ARG   A CG  
698  C CD  . ARG   A 87  ? 0.3050 0.3171 0.4220 0.0167  0.0234  0.0170  93  ARG   A CD  
699  N NE  . ARG   A 87  ? 0.2912 0.3011 0.3949 0.0130  0.0241  0.0159  93  ARG   A NE  
700  C CZ  . ARG   A 87  ? 0.2853 0.3009 0.3835 0.0121  0.0227  0.0128  93  ARG   A CZ  
701  N NH1 . ARG   A 87  ? 0.2645 0.2856 0.3653 0.0143  0.0225  0.0108  93  ARG   A NH1 
702  N NH2 . ARG   A 87  ? 0.2496 0.2629 0.3400 0.0088  0.0237  0.0111  93  ARG   A NH2 
703  N N   . TYR   A 88  ? 0.3170 0.3254 0.4574 0.0214  -0.0125 0.0357  94  TYR   A N   
704  C CA  . TYR   A 88  ? 0.3359 0.3425 0.4650 0.0192  -0.0214 0.0374  94  TYR   A CA  
705  C C   . TYR   A 88  ? 0.3100 0.3103 0.4077 0.0148  -0.0131 0.0369  94  TYR   A C   
706  O O   . TYR   A 88  ? 0.3237 0.3096 0.4022 0.0137  -0.0083 0.0391  94  TYR   A O   
707  C CB  . TYR   A 88  ? 0.3839 0.3718 0.5031 0.0212  -0.0421 0.0438  94  TYR   A CB  
708  C CG  . TYR   A 88  ? 0.4295 0.4229 0.5880 0.0261  -0.0561 0.0434  94  TYR   A CG  
709  C CD1 . TYR   A 88  ? 0.4445 0.4494 0.6325 0.0265  -0.0648 0.0399  94  TYR   A CD1 
710  C CD2 . TYR   A 88  ? 0.4613 0.4463 0.6311 0.0304  -0.0619 0.0461  94  TYR   A CD2 
711  C CE1 . TYR   A 88  ? 0.4537 0.4631 0.6877 0.0310  -0.0788 0.0380  94  TYR   A CE1 
712  C CE2 . TYR   A 88  ? 0.4697 0.4589 0.6821 0.0353  -0.0769 0.0448  94  TYR   A CE2 
713  C CZ  . TYR   A 88  ? 0.4714 0.4735 0.7189 0.0356  -0.0852 0.0402  94  TYR   A CZ  
714  O OH  . TYR   A 88  ? 0.4865 0.4934 0.7870 0.0404  -0.0998 0.0372  94  TYR   A OH  
715  N N   . GLN   A 89  ? 0.2646 0.2745 0.3604 0.0122  -0.0095 0.0335  95  GLN   A N   
716  C CA  . GLN   A 89  ? 0.2657 0.2701 0.3377 0.0081  -0.0029 0.0322  95  GLN   A CA  
717  C C   . GLN   A 89  ? 0.2716 0.2644 0.3242 0.0059  -0.0129 0.0361  95  GLN   A C   
718  O O   . GLN   A 89  ? 0.2712 0.2716 0.3362 0.0067  -0.0221 0.0359  95  GLN   A O   
719  C CB  . GLN   A 89  ? 0.2530 0.2713 0.3317 0.0071  0.0054  0.0258  95  GLN   A CB  
720  C CG  . GLN   A 89  ? 0.2640 0.2780 0.3263 0.0033  0.0103  0.0232  95  GLN   A CG  
721  C CD  . GLN   A 89  ? 0.2589 0.2806 0.3267 0.0040  0.0151  0.0162  95  GLN   A CD  
722  O OE1 . GLN   A 89  ? 0.2448 0.2679 0.3206 0.0069  0.0176  0.0125  95  GLN   A OE1 
723  N NE2 . GLN   A 89  ? 0.2474 0.2704 0.3081 0.0017  0.0151  0.0140  95  GLN   A NE2 
724  N N   . SER   A 90  ? 0.2835 0.2552 0.3061 0.0031  -0.0101 0.0387  96  SER   A N   
725  C CA  . SER   A 90  ? 0.3026 0.2557 0.2971 0.0009  -0.0191 0.0419  96  SER   A CA  
726  C C   . SER   A 90  ? 0.2980 0.2584 0.2874 -0.0034 -0.0116 0.0376  96  SER   A C   
727  O O   . SER   A 90  ? 0.2840 0.2591 0.2874 -0.0048 0.0007  0.0324  96  SER   A O   
728  C CB  . SER   A 90  ? 0.3643 0.2810 0.3196 -0.0004 -0.0168 0.0472  96  SER   A CB  
729  O OG  . SER   A 90  ? 0.3717 0.2851 0.3237 -0.0042 0.0051  0.0440  96  SER   A OG  
730  N N   . HIS   A 91  ? 0.2983 0.2460 0.2675 -0.0050 -0.0217 0.0392  97  HIS   A N   
731  C CA  . HIS   A 91  ? 0.2965 0.2473 0.2578 -0.0093 -0.0157 0.0356  97  HIS   A CA  
732  C C   . HIS   A 91  ? 0.2695 0.2509 0.2632 -0.0088 -0.0123 0.0307  97  HIS   A C   
733  O O   . HIS   A 91  ? 0.2715 0.2584 0.2648 -0.0117 -0.0032 0.0266  97  HIS   A O   
734  C CB  . HIS   A 91  ? 0.3231 0.2560 0.2621 -0.0140 0.0031  0.0338  97  HIS   A CB  
735  C CG  . HIS   A 91  ? 0.3930 0.2856 0.2890 -0.0153 0.0044  0.0389  97  HIS   A CG  
736  N ND1 . HIS   A 91  ? 0.4583 0.3209 0.3136 -0.0186 0.0029  0.0401  97  HIS   A ND1 
737  C CD2 . HIS   A 91  ? 0.4189 0.2923 0.3025 -0.0137 0.0079  0.0431  97  HIS   A CD2 
738  C CE1 . HIS   A 91  ? 0.4930 0.3150 0.3071 -0.0188 0.0060  0.0453  97  HIS   A CE1 
739  N NE2 . HIS   A 91  ? 0.4761 0.3037 0.3066 -0.0159 0.0090  0.0476  97  HIS   A NE2 
740  N N   . LEU   A 92  ? 0.2441 0.2408 0.2641 -0.0052 -0.0194 0.0309  98  LEU   A N   
741  C CA  . LEU   A 92  ? 0.2345 0.2518 0.2779 -0.0047 -0.0132 0.0268  98  LEU   A CA  
742  C C   . LEU   A 92  ? 0.2284 0.2521 0.2845 -0.0054 -0.0214 0.0262  98  LEU   A C   
743  O O   . LEU   A 92  ? 0.2270 0.2460 0.2910 -0.0039 -0.0358 0.0281  98  LEU   A O   
744  C CB  . LEU   A 92  ? 0.2364 0.2623 0.3012 -0.0008 -0.0094 0.0263  98  LEU   A CB  
745  C CG  . LEU   A 92  ? 0.2443 0.2815 0.3232 0.0002  0.0006  0.0222  98  LEU   A CG  
746  C CD1 . LEU   A 92  ? 0.2554 0.2902 0.3186 -0.0007 0.0079  0.0185  98  LEU   A CD1 
747  C CD2 . LEU   A 92  ? 0.2558 0.2961 0.3530 0.0038  0.0053  0.0214  98  LEU   A CD2 
748  N N   . MET   A 93  ? 0.2204 0.2527 0.2798 -0.0073 -0.0138 0.0231  99  MET   A N   
749  C CA  . MET   A 93  ? 0.2145 0.2531 0.2890 -0.0087 -0.0177 0.0217  99  MET   A CA  
750  C C   . MET   A 93  ? 0.2153 0.2634 0.3090 -0.0077 -0.0047 0.0191  99  MET   A C   
751  O O   . MET   A 93  ? 0.2409 0.2869 0.3209 -0.0073 0.0055  0.0178  99  MET   A O   
752  C CB  . MET   A 93  ? 0.2276 0.2613 0.2817 -0.0125 -0.0175 0.0205  99  MET   A CB  
753  C CG  . MET   A 93  ? 0.2860 0.3022 0.3123 -0.0142 -0.0252 0.0225  99  MET   A CG  
754  S SD  . MET   A 93  ? 0.3112 0.3196 0.3148 -0.0191 -0.0193 0.0198  99  MET   A SD  
755  C CE  . MET   A 93  ? 0.2684 0.2855 0.2779 -0.0187 -0.0035 0.0167  99  MET   A CE  
756  N N   . LEU   A 94  ? 0.2064 0.2608 0.3311 -0.0073 -0.0045 0.0178  100 LEU   A N   
757  C CA  . LEU   A 94  ? 0.2062 0.2624 0.3450 -0.0071 0.0138  0.0151  100 LEU   A CA  
758  C C   . LEU   A 94  ? 0.2163 0.2734 0.3626 -0.0104 0.0192  0.0132  100 LEU   A C   
759  O O   . LEU   A 94  ? 0.2133 0.2750 0.3732 -0.0122 0.0068  0.0126  100 LEU   A O   
760  C CB  . LEU   A 94  ? 0.2130 0.2735 0.3897 -0.0050 0.0189  0.0133  100 LEU   A CB  
761  C CG  . LEU   A 94  ? 0.2571 0.3167 0.4320 -0.0016 0.0145  0.0150  100 LEU   A CG  
762  C CD1 . LEU   A 94  ? 0.2584 0.3225 0.4770 0.0004  0.0214  0.0120  100 LEU   A CD1 
763  C CD2 . LEU   A 94  ? 0.2794 0.3308 0.4182 -0.0005 0.0236  0.0155  100 LEU   A CD2 
764  N N   . ALA   A 95  ? 0.2198 0.2686 0.3541 -0.0108 0.0369  0.0122  101 ALA   A N   
765  C CA  . ALA   A 95  ? 0.2267 0.2714 0.3664 -0.0138 0.0479  0.0106  101 ALA   A CA  
766  C C   . ALA   A 95  ? 0.2303 0.2608 0.3730 -0.0134 0.0731  0.0088  101 ALA   A C   
767  O O   . ALA   A 95  ? 0.2339 0.2550 0.3609 -0.0106 0.0800  0.0089  101 ALA   A O   
768  C CB  . ALA   A 95  ? 0.2421 0.2792 0.3457 -0.0146 0.0452  0.0120  101 ALA   A CB  
769  N N   . VAL   A 96  ? 0.2352 0.2608 0.3967 -0.0167 0.0885  0.0067  102 VAL   A N   
770  C CA  . VAL   A 96  ? 0.2678 0.2708 0.4222 -0.0174 0.1177  0.0051  102 VAL   A CA  
771  C C   . VAL   A 96  ? 0.3159 0.2941 0.4120 -0.0165 0.1216  0.0081  102 VAL   A C   
772  O O   . VAL   A 96  ? 0.3357 0.3152 0.4253 -0.0185 0.1158  0.0093  102 VAL   A O   
773  C CB  . VAL   A 96  ? 0.2775 0.2840 0.4833 -0.0217 0.1350  0.0008  102 VAL   A CB  
774  C CG1 . VAL   A 96  ? 0.3141 0.2882 0.5035 -0.0236 0.1720  -0.0006 102 VAL   A CG1 
775  C CG2 . VAL   A 96  ? 0.2560 0.2851 0.5241 -0.0212 0.1262  -0.0034 102 VAL   A CG2 
776  N N   . GLY   A 97  ? 0.3343 0.2901 0.3890 -0.0128 0.1266  0.0089  103 GLY   A N   
777  C CA  . GLY   A 97  ? 0.3742 0.3016 0.3722 -0.0104 0.1243  0.0109  103 GLY   A CA  
778  C C   . GLY   A 97  ? 0.4022 0.3018 0.3587 -0.0057 0.1279  0.0100  103 GLY   A C   
779  O O   . GLY   A 97  ? 0.4092 0.3187 0.3820 -0.0043 0.1281  0.0083  103 GLY   A O   
780  N N   . HIS   A 98  ? 0.4156 0.2765 0.3161 -0.0027 0.1293  0.0109  104 HIS   A N   
781  C CA  . HIS   A 98  ? 0.4418 0.2694 0.2956 0.0025  0.1283  0.0092  104 HIS   A CA  
782  C C   . HIS   A 98  ? 0.4251 0.2718 0.2811 0.0068  0.0981  0.0075  104 HIS   A C   
783  O O   . HIS   A 98  ? 0.4163 0.2801 0.2807 0.0071  0.0780  0.0080  104 HIS   A O   
784  C CB  . HIS   A 98  ? 0.4969 0.2692 0.2829 0.0055  0.1338  0.0104  104 HIS   A CB  
785  C CG  . HIS   A 98  ? 0.5606 0.2918 0.2921 0.0117  0.1293  0.0077  104 HIS   A CG  
786  N ND1 . HIS   A 98  ? 0.6149 0.3266 0.3376 0.0111  0.1536  0.0054  104 HIS   A ND1 
787  C CD2 . HIS   A 98  ? 0.5954 0.3074 0.2895 0.0185  0.1005  0.0056  104 HIS   A CD2 
788  C CE1 . HIS   A 98  ? 0.6458 0.3235 0.3179 0.0175  0.1390  0.0024  104 HIS   A CE1 
789  N NE2 . HIS   A 98  ? 0.6527 0.3283 0.3064 0.0224  0.1058  0.0022  104 HIS   A NE2 
790  N N   . SER   A 99  ? 0.4285 0.2687 0.2768 0.0099  0.0971  0.0047  105 SER   A N   
791  C CA  . SER   A 99  ? 0.4262 0.2744 0.2715 0.0143  0.0721  0.0018  105 SER   A CA  
792  C C   . SER   A 99  ? 0.4637 0.2834 0.2794 0.0184  0.0769  -0.0019 105 SER   A C   
793  O O   . SER   A 99  ? 0.4878 0.2947 0.3012 0.0167  0.1014  -0.0020 105 SER   A O   
794  C CB  . SER   A 99  ? 0.3984 0.2947 0.2969 0.0117  0.0610  0.0024  105 SER   A CB  
795  O OG  . SER   A 99  ? 0.3968 0.3083 0.3238 0.0100  0.0736  0.0027  105 SER   A OG  
796  N N   . GLU   A 100 ? 0.4735 0.2798 0.2670 0.0239  0.0540  -0.0060 106 GLU   A N   
797  C CA  . GLU   A 100 ? 0.5187 0.2977 0.2834 0.0287  0.0518  -0.0110 106 GLU   A CA  
798  C C   . GLU   A 100 ? 0.5356 0.3398 0.3285 0.0315  0.0251  -0.0154 106 GLU   A C   
799  O O   . GLU   A 100 ? 0.5354 0.3620 0.3526 0.0309  0.0081  -0.0154 106 GLU   A O   
800  C CB  . GLU   A 100 ? 0.5885 0.3050 0.2794 0.0344  0.0456  -0.0134 106 GLU   A CB  
801  C CG  . GLU   A 100 ? 0.6882 0.3653 0.3389 0.0318  0.0780  -0.0100 106 GLU   A CG  
802  C CD  . GLU   A 100 ? 0.7906 0.4005 0.3608 0.0374  0.0699  -0.0107 106 GLU   A CD  
803  O OE1 . GLU   A 100 ? 0.8508 0.4205 0.3737 0.0442  0.0534  -0.0162 106 GLU   A OE1 
804  O OE2 . GLU   A 100 ? 0.7928 0.3872 0.3454 0.0354  0.0787  -0.0061 106 GLU   A OE2 
805  N N   . PRO   A 101 ? 0.5802 0.3786 0.3714 0.0344  0.0218  -0.0201 107 PRO   A N   
806  C CA  . PRO   A 101 ? 0.5839 0.3986 0.3996 0.0375  -0.0036 -0.0259 107 PRO   A CA  
807  C C   . PRO   A 101 ? 0.6082 0.3875 0.3871 0.0438  -0.0295 -0.0312 107 PRO   A C   
808  O O   . PRO   A 101 ? 0.6903 0.4177 0.4077 0.0484  -0.0313 -0.0328 107 PRO   A O   
809  C CB  . PRO   A 101 ? 0.5900 0.3977 0.4039 0.0396  0.0009  -0.0301 107 PRO   A CB  
810  C CG  . PRO   A 101 ? 0.6141 0.4095 0.4122 0.0367  0.0314  -0.0259 107 PRO   A CG  
811  C CD  . PRO   A 101 ? 0.6016 0.3726 0.3659 0.0354  0.0410  -0.0218 107 PRO   A CD  
812  N N   . GLY   A 102 ? 0.5353 0.3403 0.3518 0.0435  -0.0477 -0.0337 108 GLY   A N   
813  C CA  . GLY   A 102 ? 0.5109 0.2977 0.3181 0.0484  -0.0746 -0.0389 108 GLY   A CA  
814  C C   . GLY   A 102 ? 0.4705 0.2858 0.3069 0.0434  -0.0702 -0.0339 108 GLY   A C   
815  O O   . GLY   A 102 ? 0.4657 0.2861 0.3243 0.0453  -0.0903 -0.0390 108 GLY   A O   
816  N N   . ASP   A 103 ? 0.4323 0.2656 0.2726 0.0369  -0.0441 -0.0250 109 ASP   A N   
817  C CA  . ASP   A 103 ? 0.4050 0.2638 0.2705 0.0317  -0.0391 -0.0205 109 ASP   A CA  
818  C C   . ASP   A 103 ? 0.3507 0.2524 0.2708 0.0270  -0.0382 -0.0211 109 ASP   A C   
819  O O   . ASP   A 103 ? 0.3240 0.2434 0.2642 0.0231  -0.0371 -0.0192 109 ASP   A O   
820  C CB  . ASP   A 103 ? 0.4310 0.2898 0.2828 0.0269  -0.0142 -0.0122 109 ASP   A CB  
821  C CG  . ASP   A 103 ? 0.4634 0.2754 0.2592 0.0303  -0.0111 -0.0108 109 ASP   A CG  
822  O OD1 . ASP   A 103 ? 0.4915 0.2785 0.2642 0.0353  -0.0318 -0.0141 109 ASP   A OD1 
823  O OD2 . ASP   A 103 ? 0.4916 0.2885 0.2668 0.0281  0.0127  -0.0069 109 ASP   A OD2 
824  N N   . CYS   A 104 ? 0.3409 0.2557 0.2822 0.0270  -0.0372 -0.0237 110 CYS   A N   
825  C CA  . CYS   A 104 ? 0.3066 0.2542 0.2925 0.0221  -0.0335 -0.0238 110 CYS   A CA  
826  C C   . CYS   A 104 ? 0.3122 0.2641 0.3222 0.0223  -0.0466 -0.0301 110 CYS   A C   
827  O O   . CYS   A 104 ? 0.3394 0.2718 0.3447 0.0280  -0.0660 -0.0378 110 CYS   A O   
828  C CB  . CYS   A 104 ? 0.3147 0.2693 0.3171 0.0229  -0.0318 -0.0265 110 CYS   A CB  
829  S SG  . CYS   A 104 ? 0.3431 0.3006 0.3330 0.0214  -0.0134 -0.0191 110 CYS   A SG  
830  N N   . GLY   A 105 ? 0.2846 0.2576 0.3187 0.0164  -0.0373 -0.0276 111 GLY   A N   
831  C CA  . GLY   A 105 ? 0.2748 0.2525 0.3374 0.0154  -0.0445 -0.0342 111 GLY   A CA  
832  C C   . GLY   A 105 ? 0.2852 0.2603 0.3374 0.0140  -0.0455 -0.0317 111 GLY   A C   
833  O O   . GLY   A 105 ? 0.2720 0.2548 0.3502 0.0113  -0.0457 -0.0359 111 GLY   A O   
834  N N   . GLY   A 106 ? 0.2884 0.2516 0.3041 0.0152  -0.0432 -0.0250 112 GLY   A N   
835  C CA  . GLY   A 106 ? 0.2649 0.2248 0.2697 0.0136  -0.0423 -0.0219 112 GLY   A CA  
836  C C   . GLY   A 106 ? 0.2463 0.2294 0.2705 0.0061  -0.0281 -0.0183 112 GLY   A C   
837  O O   . GLY   A 106 ? 0.2448 0.2400 0.2712 0.0026  -0.0167 -0.0137 112 GLY   A O   
838  N N   . ILE   A 107 ? 0.2380 0.2241 0.2741 0.0038  -0.0299 -0.0206 113 ILE   A N   
839  C CA  . ILE   A 107 ? 0.2385 0.2402 0.2865 -0.0032 -0.0169 -0.0181 113 ILE   A CA  
840  C C   . ILE   A 107 ? 0.2270 0.2316 0.2555 -0.0063 -0.0093 -0.0103 113 ILE   A C   
841  O O   . ILE   A 107 ? 0.2464 0.2405 0.2586 -0.0042 -0.0123 -0.0083 113 ILE   A O   
842  C CB  . ILE   A 107 ? 0.2687 0.2720 0.3425 -0.0050 -0.0190 -0.0254 113 ILE   A CB  
843  C CG1 . ILE   A 107 ? 0.2869 0.2946 0.3932 -0.0060 -0.0156 -0.0331 113 ILE   A CG1 
844  C CG2 . ILE   A 107 ? 0.2861 0.2964 0.3577 -0.0116 -0.0076 -0.0224 113 ILE   A CG2 
845  C CD1 . ILE   A 107 ? 0.3130 0.3198 0.4563 -0.0064 -0.0186 -0.0434 113 ILE   A CD1 
846  N N   . LEU   A 108 ? 0.2093 0.2249 0.2409 -0.0113 -0.0001 -0.0067 114 LEU   A N   
847  C CA  . LEU   A 108 ? 0.2062 0.2263 0.2297 -0.0148 0.0045  -0.0015 114 LEU   A CA  
848  C C   . LEU   A 108 ? 0.2154 0.2376 0.2443 -0.0198 0.0073  -0.0040 114 LEU   A C   
849  O O   . LEU   A 108 ? 0.2219 0.2433 0.2556 -0.0223 0.0120  -0.0063 114 LEU   A O   
850  C CB  . LEU   A 108 ? 0.2002 0.2260 0.2225 -0.0156 0.0075  0.0031  114 LEU   A CB  
851  C CG  . LEU   A 108 ? 0.2252 0.2556 0.2478 -0.0193 0.0080  0.0064  114 LEU   A CG  
852  C CD1 . LEU   A 108 ? 0.2262 0.2560 0.2501 -0.0187 0.0107  0.0079  114 LEU   A CD1 
853  C CD2 . LEU   A 108 ? 0.2385 0.2718 0.2640 -0.0193 0.0059  0.0097  114 LEU   A CD2 
854  N N   . ARG   A 109 ? 0.2090 0.2306 0.2354 -0.0215 0.0068  -0.0038 115 ARG   A N   
855  C CA  . ARG   A 109 ? 0.2254 0.2465 0.2554 -0.0263 0.0104  -0.0070 115 ARG   A CA  
856  C C   . ARG   A 109 ? 0.2363 0.2593 0.2586 -0.0297 0.0104  -0.0039 115 ARG   A C   
857  O O   . ARG   A 109 ? 0.2321 0.2573 0.2539 -0.0282 0.0086  -0.0006 115 ARG   A O   
858  C CB  . ARG   A 109 ? 0.2672 0.2843 0.3090 -0.0245 0.0072  -0.0124 115 ARG   A CB  
859  C CG  . ARG   A 109 ? 0.3869 0.3994 0.4196 -0.0216 0.0017  -0.0094 115 ARG   A CG  
860  C CD  . ARG   A 109 ? 0.4981 0.5028 0.5388 -0.0194 -0.0047 -0.0140 115 ARG   A CD  
861  N NE  . ARG   A 109 ? 0.6160 0.6095 0.6567 -0.0125 -0.0164 -0.0165 115 ARG   A NE  
862  C CZ  . ARG   A 109 ? 0.6728 0.6664 0.7366 -0.0104 -0.0224 -0.0239 115 ARG   A CZ  
863  N NH1 . ARG   A 109 ? 0.6812 0.6844 0.7695 -0.0154 -0.0129 -0.0293 115 ARG   A NH1 
864  N NH2 . ARG   A 109 ? 0.6843 0.6649 0.7470 -0.0033 -0.0374 -0.0269 115 ARG   A NH2 
865  N N   . CYS   A 110 ? 0.2379 0.2566 0.2540 -0.0345 0.0134  -0.0057 116 CYS   A N   
866  C CA  . CYS   A 110 ? 0.2583 0.2763 0.2684 -0.0377 0.0103  -0.0047 116 CYS   A CA  
867  C C   . CYS   A 110 ? 0.2848 0.2969 0.2948 -0.0415 0.0154  -0.0100 116 CYS   A C   
868  O O   . CYS   A 110 ? 0.2874 0.2978 0.3076 -0.0409 0.0210  -0.0143 116 CYS   A O   
869  C CB  . CYS   A 110 ? 0.2781 0.2891 0.2735 -0.0395 0.0056  -0.0026 116 CYS   A CB  
870  S SG  . CYS   A 110 ? 0.2941 0.2839 0.2658 -0.0434 0.0146  -0.0058 116 CYS   A SG  
871  N N   . GLN   A 111 ? 0.3146 0.3223 0.3163 -0.0453 0.0130  -0.0109 117 GLN   A N   
872  C CA  . GLN   A 111 ? 0.3409 0.3414 0.3421 -0.0491 0.0197  -0.0165 117 GLN   A CA  
873  C C   . GLN   A 111 ? 0.3661 0.3511 0.3564 -0.0523 0.0318  -0.0211 117 GLN   A C   
874  O O   . GLN   A 111 ? 0.3924 0.3719 0.3906 -0.0552 0.0414  -0.0272 117 GLN   A O   
875  C CB  . GLN   A 111 ? 0.3811 0.3768 0.3728 -0.0527 0.0141  -0.0174 117 GLN   A CB  
876  C CG  . GLN   A 111 ? 0.4404 0.4213 0.4067 -0.0544 0.0071  -0.0166 117 GLN   A CG  
877  C CD  . GLN   A 111 ? 0.5396 0.5159 0.5016 -0.0570 -0.0031 -0.0188 117 GLN   A CD  
878  O OE1 . GLN   A 111 ? 0.5677 0.5508 0.5401 -0.0553 -0.0164 -0.0166 117 GLN   A OE1 
879  N NE2 . GLN   A 111 ? 0.5726 0.5373 0.5244 -0.0611 0.0034  -0.0241 117 GLN   A NE2 
880  N N   . HIS   A 112 ? 0.3532 0.3287 0.3267 -0.0523 0.0335  -0.0188 118 HIS   A N   
881  C CA  . HIS   A 112 ? 0.3638 0.3181 0.3228 -0.0561 0.0497  -0.0229 118 HIS   A CA  
882  C C   . HIS   A 112 ? 0.3651 0.3257 0.3509 -0.0543 0.0600  -0.0260 118 HIS   A C   
883  O O   . HIS   A 112 ? 0.3898 0.3334 0.3740 -0.0582 0.0784  -0.0312 118 HIS   A O   
884  C CB  . HIS   A 112 ? 0.3885 0.3198 0.3075 -0.0574 0.0465  -0.0188 118 HIS   A CB  
885  C CG  . HIS   A 112 ? 0.3964 0.3183 0.2919 -0.0585 0.0318  -0.0175 118 HIS   A CG  
886  N ND1 . HIS   A 112 ? 0.3989 0.3331 0.2998 -0.0547 0.0118  -0.0125 118 HIS   A ND1 
887  C CD2 . HIS   A 112 ? 0.4194 0.3195 0.2899 -0.0630 0.0346  -0.0219 118 HIS   A CD2 
888  C CE1 . HIS   A 112 ? 0.4373 0.3583 0.3201 -0.0567 0.0005  -0.0143 118 HIS   A CE1 
889  N NE2 . HIS   A 112 ? 0.4482 0.3481 0.3094 -0.0616 0.0130  -0.0197 118 HIS   A NE2 
890  N N   . GLY   A 113 ? 0.3230 0.3042 0.3321 -0.0485 0.0490  -0.0235 119 GLY   A N   
891  C CA  . GLY   A 113 ? 0.3061 0.2929 0.3428 -0.0457 0.0531  -0.0273 119 GLY   A CA  
892  C C   . GLY   A 113 ? 0.2941 0.2904 0.3306 -0.0405 0.0429  -0.0218 119 GLY   A C   
893  O O   . GLY   A 113 ? 0.2857 0.2899 0.3123 -0.0377 0.0313  -0.0158 119 GLY   A O   
894  N N   . VAL   A 114 ? 0.2854 0.2801 0.3375 -0.0393 0.0489  -0.0251 120 VAL   A N   
895  C CA  . VAL   A 114 ? 0.2760 0.2781 0.3294 -0.0344 0.0404  -0.0211 120 VAL   A CA  
896  C C   . VAL   A 114 ? 0.2791 0.2742 0.3045 -0.0357 0.0416  -0.0140 120 VAL   A C   
897  O O   . VAL   A 114 ? 0.2940 0.2721 0.3038 -0.0399 0.0536  -0.0142 120 VAL   A O   
898  C CB  . VAL   A 114 ? 0.2694 0.2723 0.3538 -0.0324 0.0440  -0.0282 120 VAL   A CB  
899  C CG1 . VAL   A 114 ? 0.2827 0.2904 0.3641 -0.0277 0.0365  -0.0242 120 VAL   A CG1 
900  C CG2 . VAL   A 114 ? 0.2703 0.2789 0.3846 -0.0289 0.0344  -0.0354 120 VAL   A CG2 
901  N N   . VAL   A 115 ? 0.2542 0.2587 0.2728 -0.0318 0.0294  -0.0078 121 VAL   A N   
902  C CA  . VAL   A 115 ? 0.2506 0.2498 0.2497 -0.0318 0.0260  -0.0015 121 VAL   A CA  
903  C C   . VAL   A 115 ? 0.2534 0.2550 0.2602 -0.0284 0.0266  -0.0003 121 VAL   A C   
904  O O   . VAL   A 115 ? 0.2727 0.2634 0.2651 -0.0290 0.0288  0.0031  121 VAL   A O   
905  C CB  . VAL   A 115 ? 0.2590 0.2683 0.2573 -0.0298 0.0143  0.0028  121 VAL   A CB  
906  C CG1 . VAL   A 115 ? 0.2532 0.2591 0.2424 -0.0284 0.0068  0.0081  121 VAL   A CG1 
907  C CG2 . VAL   A 115 ? 0.2656 0.2726 0.2584 -0.0332 0.0129  0.0013  121 VAL   A CG2 
908  N N   . GLY   A 116 ? 0.2352 0.2480 0.2607 -0.0242 0.0228  -0.0027 122 GLY   A N   
909  C CA  . GLY   A 116 ? 0.2418 0.2567 0.2748 -0.0206 0.0219  -0.0023 122 GLY   A CA  
910  C C   . GLY   A 116 ? 0.2226 0.2431 0.2687 -0.0155 0.0148  -0.0060 122 GLY   A C   
911  O O   . GLY   A 116 ? 0.2306 0.2511 0.2810 -0.0147 0.0106  -0.0093 122 GLY   A O   
912  N N   . ILE   A 117 ? 0.2244 0.2456 0.2742 -0.0117 0.0125  -0.0059 123 ILE   A N   
913  C CA  . ILE   A 117 ? 0.2254 0.2440 0.2783 -0.0062 0.0036  -0.0097 123 ILE   A CA  
914  C C   . ILE   A 117 ? 0.2268 0.2447 0.2670 -0.0030 0.0029  -0.0052 123 ILE   A C   
915  O O   . ILE   A 117 ? 0.2230 0.2451 0.2639 -0.0041 0.0074  -0.0012 123 ILE   A O   
916  C CB  . ILE   A 117 ? 0.2353 0.2510 0.3106 -0.0041 0.0006  -0.0180 123 ILE   A CB  
917  C CG1 . ILE   A 117 ? 0.2495 0.2670 0.3320 -0.0062 0.0098  -0.0166 123 ILE   A CG1 
918  C CG2 . ILE   A 117 ? 0.2475 0.2623 0.3449 -0.0061 0.0002  -0.0255 123 ILE   A CG2 
919  C CD1 . ILE   A 117 ? 0.2686 0.2837 0.3810 -0.0042 0.0077  -0.0262 123 ILE   A CD1 
920  N N   . VAL   A 118 ? 0.2175 0.2258 0.2443 0.0011  -0.0021 -0.0061 124 VAL   A N   
921  C CA  . VAL   A 118 ? 0.2166 0.2194 0.2309 0.0039  0.0016  -0.0031 124 VAL   A CA  
922  C C   . VAL   A 118 ? 0.2242 0.2285 0.2484 0.0059  0.0008  -0.0055 124 VAL   A C   
923  O O   . VAL   A 118 ? 0.2310 0.2319 0.2650 0.0078  -0.0066 -0.0118 124 VAL   A O   
924  C CB  . VAL   A 118 ? 0.2475 0.2286 0.2365 0.0083  -0.0021 -0.0051 124 VAL   A CB  
925  C CG1 . VAL   A 118 ? 0.2638 0.2326 0.2370 0.0110  0.0054  -0.0038 124 VAL   A CG1 
926  C CG2 . VAL   A 118 ? 0.2478 0.2250 0.2265 0.0062  0.0008  -0.0023 124 VAL   A CG2 
927  N N   . SER   A 119 ? 0.2079 0.2178 0.2349 0.0054  0.0077  -0.0011 125 SER   A N   
928  C CA  . SER   A 119 ? 0.2125 0.2240 0.2491 0.0070  0.0081  -0.0024 125 SER   A CA  
929  C C   . SER   A 119 ? 0.2385 0.2450 0.2692 0.0097  0.0138  -0.0009 125 SER   A C   
930  O O   . SER   A 119 ? 0.2509 0.2521 0.2827 0.0126  0.0127  -0.0042 125 SER   A O   
931  C CB  . SER   A 119 ? 0.2277 0.2490 0.2772 0.0033  0.0113  0.0015  125 SER   A CB  
932  O OG  . SER   A 119 ? 0.2446 0.2657 0.3029 0.0047  0.0129  0.0010  125 SER   A OG  
933  N N   . THR   A 120 ? 0.2328 0.2401 0.2613 0.0085  0.0214  0.0030  126 THR   A N   
934  C CA  . THR   A 120 ? 0.2525 0.2540 0.2820 0.0104  0.0317  0.0033  126 THR   A CA  
935  C C   . THR   A 120 ? 0.2775 0.2670 0.2945 0.0096  0.0429  0.0038  126 THR   A C   
936  O O   . THR   A 120 ? 0.2670 0.2565 0.2777 0.0076  0.0407  0.0049  126 THR   A O   
937  C CB  . THR   A 120 ? 0.2616 0.2793 0.3193 0.0088  0.0331  0.0076  126 THR   A CB  
938  O OG1 . THR   A 120 ? 0.2804 0.3067 0.3510 0.0058  0.0335  0.0109  126 THR   A OG1 
939  C CG2 . THR   A 120 ? 0.2594 0.2845 0.3250 0.0085  0.0247  0.0091  126 THR   A CG2 
940  N N   . GLY   A 121 ? 0.2959 0.2747 0.3127 0.0106  0.0574  0.0028  127 GLY   A N   
941  C CA  . GLY   A 121 ? 0.3307 0.2959 0.3407 0.0088  0.0740  0.0031  127 GLY   A CA  
942  C C   . GLY   A 121 ? 0.3716 0.3308 0.3980 0.0087  0.0939  0.0014  127 GLY   A C   
943  O O   . GLY   A 121 ? 0.3786 0.3461 0.4223 0.0103  0.0923  0.0005  127 GLY   A O   
944  N N   . GLY   A 122 ? 0.3927 0.3393 0.4208 0.0061  0.1137  0.0010  128 GLY   A N   
945  C CA  . GLY   A 122 ? 0.4112 0.3491 0.4615 0.0049  0.1390  -0.0020 128 GLY   A CA  
946  C C   . GLY   A 122 ? 0.4710 0.3765 0.4959 0.0026  0.1651  -0.0035 128 GLY   A C   
947  O O   . GLY   A 122 ? 0.5042 0.3894 0.4849 0.0031  0.1608  -0.0017 128 GLY   A O   
948  N N   . ASN   A 123 ? 0.4806 0.3777 0.5347 -0.0001 0.1943  -0.0071 129 ASN   A N   
949  C CA  . ASN   A 123 ? 0.5046 0.3672 0.5373 -0.0034 0.2251  -0.0086 129 ASN   A CA  
950  C C   . ASN   A 123 ? 0.4770 0.3590 0.5392 -0.0072 0.2209  -0.0063 129 ASN   A C   
951  O O   . ASN   A 123 ? 0.4544 0.3604 0.5821 -0.0107 0.2282  -0.0088 129 ASN   A O   
952  C CB  . ASN   A 123 ? 0.5319 0.3802 0.5953 -0.0060 0.2611  -0.0144 129 ASN   A CB  
953  C CG  . ASN   A 123 ? 0.6209 0.4186 0.6457 -0.0094 0.3006  -0.0165 129 ASN   A CG  
954  O OD1 . ASN   A 123 ? 0.6717 0.4467 0.6512 -0.0100 0.3004  -0.0129 129 ASN   A OD1 
955  N ND2 . ASN   A 123 ? 0.6331 0.4084 0.6735 -0.0117 0.3373  -0.0226 129 ASN   A ND2 
956  N N   . GLY   A 124 ? 0.4613 0.3286 0.4757 -0.0065 0.2097  -0.0025 130 GLY   A N   
957  C CA  . GLY   A 124 ? 0.4358 0.3179 0.4700 -0.0100 0.2049  -0.0002 130 GLY   A CA  
958  C C   . GLY   A 124 ? 0.3727 0.2999 0.4434 -0.0095 0.1713  0.0019  130 GLY   A C   
959  O O   . GLY   A 124 ? 0.3656 0.3105 0.4654 -0.0127 0.1659  0.0025  130 GLY   A O   
960  N N   . LEU   A 125 ? 0.3445 0.2870 0.4126 -0.0058 0.1502  0.0026  131 LEU   A N   
961  C CA  . LEU   A 125 ? 0.2997 0.2756 0.3904 -0.0054 0.1208  0.0050  131 LEU   A CA  
962  C C   . LEU   A 125 ? 0.3092 0.2803 0.3567 -0.0021 0.1013  0.0070  131 LEU   A C   
963  O O   . LEU   A 125 ? 0.3555 0.3040 0.3668 0.0012  0.1044  0.0057  131 LEU   A O   
964  C CB  . LEU   A 125 ? 0.2933 0.2914 0.4272 -0.0042 0.1130  0.0040  131 LEU   A CB  
965  C CG  . LEU   A 125 ? 0.2906 0.2990 0.4837 -0.0067 0.1258  0.0003  131 LEU   A CG  
966  C CD1 . LEU   A 125 ? 0.3035 0.3242 0.5319 -0.0041 0.1210  -0.0014 131 LEU   A CD1 
967  C CD2 . LEU   A 125 ? 0.2765 0.3034 0.5013 -0.0095 0.1120  0.0006  131 LEU   A CD2 
968  N N   . VAL   A 126 ? 0.2644 0.2554 0.3195 -0.0030 0.0811  0.0091  132 VAL   A N   
969  C CA  . VAL   A 126 ? 0.2658 0.2564 0.2951 -0.0006 0.0639  0.0094  132 VAL   A CA  
970  C C   . VAL   A 126 ? 0.2452 0.2604 0.2991 -0.0020 0.0481  0.0112  132 VAL   A C   
971  O O   . VAL   A 126 ? 0.2460 0.2734 0.3226 -0.0048 0.0452  0.0124  132 VAL   A O   
972  C CB  . VAL   A 126 ? 0.2879 0.2648 0.2881 -0.0007 0.0599  0.0095  132 VAL   A CB  
973  C CG1 . VAL   A 126 ? 0.3052 0.2930 0.3232 -0.0050 0.0616  0.0111  132 VAL   A CG1 
974  C CG2 . VAL   A 126 ? 0.2776 0.2573 0.2655 0.0015  0.0416  0.0080  132 VAL   A CG2 
975  N N   . GLY   A 127 ? 0.2365 0.2544 0.2843 0.0001  0.0389  0.0109  133 GLY   A N   
976  C CA  . GLY   A 127 ? 0.2239 0.2556 0.2849 -0.0012 0.0272  0.0130  133 GLY   A CA  
977  C C   . GLY   A 127 ? 0.2236 0.2537 0.2692 -0.0018 0.0194  0.0119  133 GLY   A C   
978  O O   . GLY   A 127 ? 0.2294 0.2508 0.2623 0.0006  0.0191  0.0085  133 GLY   A O   
979  N N   . PHE   A 128 ? 0.1915 0.2269 0.2392 -0.0049 0.0132  0.0136  134 PHE   A N   
980  C CA  . PHE   A 128 ? 0.1845 0.2169 0.2226 -0.0066 0.0105  0.0115  134 PHE   A CA  
981  C C   . PHE   A 128 ? 0.2049 0.2349 0.2419 -0.0081 0.0088  0.0133  134 PHE   A C   
982  O O   . PHE   A 128 ? 0.2190 0.2476 0.2551 -0.0092 0.0043  0.0173  134 PHE   A O   
983  C CB  . PHE   A 128 ? 0.1867 0.2198 0.2207 -0.0100 0.0091  0.0114  134 PHE   A CB  
984  C CG  . PHE   A 128 ? 0.1984 0.2302 0.2309 -0.0092 0.0124  0.0108  134 PHE   A CG  
985  C CD1 . PHE   A 128 ? 0.2117 0.2347 0.2330 -0.0072 0.0124  0.0077  134 PHE   A CD1 
986  C CD2 . PHE   A 128 ? 0.2139 0.2495 0.2572 -0.0103 0.0153  0.0130  134 PHE   A CD2 
987  C CE1 . PHE   A 128 ? 0.2205 0.2345 0.2321 -0.0064 0.0167  0.0080  134 PHE   A CE1 
988  C CE2 . PHE   A 128 ? 0.2198 0.2498 0.2604 -0.0105 0.0228  0.0125  134 PHE   A CE2 
989  C CZ  . PHE   A 128 ? 0.2255 0.2424 0.2456 -0.0084 0.0245  0.0107  134 PHE   A CZ  
990  N N   . ALA   A 129 ? 0.1981 0.2239 0.2350 -0.0082 0.0119  0.0099  135 ALA   A N   
991  C CA  . ALA   A 129 ? 0.2127 0.2300 0.2450 -0.0104 0.0155  0.0112  135 ALA   A CA  
992  C C   . ALA   A 129 ? 0.2329 0.2417 0.2529 -0.0153 0.0188  0.0107  135 ALA   A C   
993  O O   . ALA   A 129 ? 0.2414 0.2520 0.2682 -0.0167 0.0223  0.0056  135 ALA   A O   
994  C CB  . ALA   A 129 ? 0.2139 0.2294 0.2584 -0.0092 0.0207  0.0060  135 ALA   A CB  
995  N N   . ASP   A 130 ? 0.2542 0.2513 0.2553 -0.0173 0.0159  0.0155  136 ASP   A N   
996  C CA  . ASP   A 130 ? 0.2690 0.2521 0.2509 -0.0220 0.0195  0.0148  136 ASP   A CA  
997  C C   . ASP   A 130 ? 0.2799 0.2472 0.2569 -0.0257 0.0361  0.0111  136 ASP   A C   
998  O O   . ASP   A 130 ? 0.2936 0.2525 0.2708 -0.0251 0.0425  0.0120  136 ASP   A O   
999  C CB  . ASP   A 130 ? 0.2956 0.2612 0.2512 -0.0224 0.0091  0.0205  136 ASP   A CB  
1000 C CG  . ASP   A 130 ? 0.3756 0.3229 0.3050 -0.0268 0.0100  0.0195  136 ASP   A CG  
1001 O OD1 . ASP   A 130 ? 0.3933 0.3529 0.3337 -0.0283 0.0100  0.0161  136 ASP   A OD1 
1002 O OD2 . ASP   A 130 ? 0.4404 0.3565 0.3340 -0.0288 0.0114  0.0221  136 ASP   A OD2 
1003 N N   . VAL   A 131 ? 0.2866 0.2481 0.2619 -0.0299 0.0449  0.0064  137 VAL   A N   
1004 C CA  . VAL   A 131 ? 0.3081 0.2506 0.2823 -0.0346 0.0656  0.0015  137 VAL   A CA  
1005 C C   . VAL   A 131 ? 0.3480 0.2629 0.2863 -0.0402 0.0744  0.0020  137 VAL   A C   
1006 O O   . VAL   A 131 ? 0.3767 0.2698 0.3097 -0.0453 0.0965  -0.0025 137 VAL   A O   
1007 C CB  . VAL   A 131 ? 0.3011 0.2596 0.3178 -0.0346 0.0723  -0.0081 137 VAL   A CB  
1008 C CG1 . VAL   A 131 ? 0.2910 0.2688 0.3349 -0.0287 0.0618  -0.0095 137 VAL   A CG1 
1009 C CG2 . VAL   A 131 ? 0.2876 0.2569 0.3122 -0.0350 0.0662  -0.0115 137 VAL   A CG2 
1010 N N   . ARG   A 132 ? 0.3540 0.2666 0.2684 -0.0394 0.0586  0.0065  138 ARG   A N   
1011 C CA  . ARG   A 132 ? 0.3794 0.2642 0.2569 -0.0441 0.0631  0.0060  138 ARG   A CA  
1012 C C   . ARG   A 132 ? 0.4445 0.2834 0.2713 -0.0468 0.0730  0.0098  138 ARG   A C   
1013 O O   . ARG   A 132 ? 0.4855 0.2912 0.2754 -0.0518 0.0845  0.0078  138 ARG   A O   
1014 C CB  . ARG   A 132 ? 0.3674 0.2614 0.2374 -0.0420 0.0407  0.0088  138 ARG   A CB  
1015 C CG  . ARG   A 132 ? 0.3484 0.2763 0.2569 -0.0408 0.0364  0.0049  138 ARG   A CG  
1016 C CD  . ARG   A 132 ? 0.3393 0.2745 0.2440 -0.0391 0.0165  0.0075  138 ARG   A CD  
1017 N NE  . ARG   A 132 ? 0.3346 0.2789 0.2472 -0.0343 0.0007  0.0127  138 ARG   A NE  
1018 C CZ  . ARG   A 132 ? 0.3471 0.3015 0.2705 -0.0321 -0.0163 0.0141  138 ARG   A CZ  
1019 N NH1 . ARG   A 132 ? 0.3341 0.2877 0.2550 -0.0345 -0.0216 0.0113  138 ARG   A NH1 
1020 N NH2 . ARG   A 132 ? 0.3290 0.2934 0.2694 -0.0278 -0.0274 0.0173  138 ARG   A NH2 
1021 N N   . ASP   A 133 ? 0.4595 0.2914 0.2788 -0.0436 0.0688  0.0153  139 ASP   A N   
1022 C CA  . ASP   A 133 ? 0.5159 0.2975 0.2811 -0.0458 0.0787  0.0197  139 ASP   A CA  
1023 C C   . ASP   A 133 ? 0.5404 0.3051 0.3129 -0.0512 0.1139  0.0149  139 ASP   A C   
1024 O O   . ASP   A 133 ? 0.5970 0.3136 0.3216 -0.0541 0.1295  0.0180  139 ASP   A O   
1025 C CB  . ASP   A 133 ? 0.5362 0.3145 0.2909 -0.0397 0.0581  0.0279  139 ASP   A CB  
1026 C CG  . ASP   A 133 ? 0.5625 0.3718 0.3637 -0.0369 0.0633  0.0273  139 ASP   A CG  
1027 O OD1 . ASP   A 133 ? 0.5281 0.3781 0.3789 -0.0360 0.0637  0.0219  139 ASP   A OD1 
1028 O OD2 . ASP   A 133 ? 0.5965 0.3851 0.3810 -0.0354 0.0664  0.0322  139 ASP   A OD2 
1029 N N   . LEU   A 134 ? 0.5114 0.3123 0.3446 -0.0518 0.1251  0.0071  140 LEU   A N   
1030 C CA  . LEU   A 134 ? 0.5199 0.3091 0.3758 -0.0565 0.1568  0.0005  140 LEU   A CA  
1031 C C   . LEU   A 134 ? 0.5570 0.3243 0.4073 -0.0639 0.1829  -0.0075 140 LEU   A C   
1032 O O   . LEU   A 134 ? 0.5219 0.3151 0.4256 -0.0654 0.1910  -0.0173 140 LEU   A O   
1033 C CB  . LEU   A 134 ? 0.4785 0.3138 0.4044 -0.0526 0.1511  -0.0056 140 LEU   A CB  
1034 C CG  . LEU   A 134 ? 0.4679 0.3239 0.4011 -0.0457 0.1288  0.0009  140 LEU   A CG  
1035 C CD1 . LEU   A 134 ? 0.4366 0.3321 0.4300 -0.0417 0.1209  -0.0061 140 LEU   A CD1 
1036 C CD2 . LEU   A 134 ? 0.5021 0.3268 0.4073 -0.0464 0.1402  0.0066  140 LEU   A CD2 
1037 N N   . LEU   A 135 ? 0.6141 0.3292 0.3952 -0.0680 0.1937  -0.0033 141 LEU   A N   
1038 C CA  . LEU   A 135 ? 0.6559 0.3391 0.4146 -0.0754 0.2194  -0.0098 141 LEU   A CA  
1039 C C   . LEU   A 135 ? 0.6657 0.3434 0.4693 -0.0820 0.2596  -0.0210 141 LEU   A C   
1040 O O   . LEU   A 135 ? 0.6696 0.3468 0.4944 -0.0870 0.2776  -0.0304 141 LEU   A O   
1041 C CB  . LEU   A 135 ? 0.7119 0.3285 0.3757 -0.0780 0.2233  -0.0028 141 LEU   A CB  
1042 C CG  . LEU   A 135 ? 0.7558 0.3704 0.3756 -0.0712 0.1807  0.0070  141 LEU   A CG  
1043 C CD1 . LEU   A 135 ? 0.8376 0.3798 0.3627 -0.0740 0.1835  0.0109  141 LEU   A CD1 
1044 C CD2 . LEU   A 135 ? 0.7278 0.3961 0.3911 -0.0675 0.1524  0.0043  141 LEU   A CD2 
1045 N N   . TRP   A 136 ? 0.6657 0.3401 0.4900 -0.0820 0.2737  -0.0209 142 TRP   A N   
1046 C CA  . TRP   A 136 ? 0.6610 0.3308 0.5388 -0.0881 0.3122  -0.0327 142 TRP   A CA  
1047 C C   . TRP   A 136 ? 0.6194 0.3453 0.5904 -0.0860 0.3034  -0.0450 142 TRP   A C   
1048 O O   . TRP   A 136 ? 0.6201 0.3417 0.6412 -0.0917 0.3338  -0.0578 142 TRP   A O   
1049 C CB  . TRP   A 136 ? 0.6627 0.3154 0.5404 -0.0882 0.3265  -0.0294 142 TRP   A CB  
1050 C CG  . TRP   A 136 ? 0.6338 0.3298 0.5374 -0.0792 0.2902  -0.0233 142 TRP   A CG  
1051 C CD1 . TRP   A 136 ? 0.6549 0.3444 0.5081 -0.0734 0.2633  -0.0101 142 TRP   A CD1 
1052 C CD2 . TRP   A 136 ? 0.5844 0.3317 0.5705 -0.0750 0.2780  -0.0313 142 TRP   A CD2 
1053 N NE1 . TRP   A 136 ? 0.6265 0.3609 0.5262 -0.0665 0.2392  -0.0093 142 TRP   A NE1 
1054 C CE2 . TRP   A 136 ? 0.5806 0.3492 0.5574 -0.0672 0.2468  -0.0219 142 TRP   A CE2 
1055 C CE3 . TRP   A 136 ? 0.5503 0.3252 0.6180 -0.0766 0.2882  -0.0462 142 TRP   A CE3 
1056 C CZ2 . TRP   A 136 ? 0.5418 0.3541 0.5792 -0.0615 0.2281  -0.0266 142 TRP   A CZ2 
1057 C CZ3 . TRP   A 136 ? 0.5154 0.3330 0.6434 -0.0700 0.2652  -0.0509 142 TRP   A CZ3 
1058 C CH2 . TRP   A 136 ? 0.5103 0.3445 0.6191 -0.0628 0.2366  -0.0410 142 TRP   A CH2 
1059 N N   . LEU   A 137 ? 0.5837 0.3572 0.5770 -0.0780 0.2627  -0.0420 143 LEU   A N   
1060 C CA  . LEU   A 137 ? 0.5473 0.3650 0.6179 -0.0751 0.2509  -0.0529 143 LEU   A CA  
1061 C C   . LEU   A 137 ? 0.5960 0.4067 0.6843 -0.0806 0.2686  -0.0628 143 LEU   A C   
1062 O O   . LEU   A 137 ? 0.5687 0.4047 0.7284 -0.0797 0.2683  -0.0749 143 LEU   A O   
1063 C CB  . LEU   A 137 ? 0.5084 0.3670 0.5827 -0.0660 0.2072  -0.0465 143 LEU   A CB  
1064 C CG  . LEU   A 137 ? 0.4808 0.3568 0.5591 -0.0596 0.1874  -0.0403 143 LEU   A CG  
1065 C CD1 . LEU   A 137 ? 0.4720 0.3785 0.5420 -0.0520 0.1507  -0.0335 143 LEU   A CD1 
1066 C CD2 . LEU   A 137 ? 0.4480 0.3416 0.5947 -0.0580 0.1916  -0.0512 143 LEU   A CD2 
1067 N N   . ASP   A 138 ? 0.6641 0.4394 0.6875 -0.0855 0.2806  -0.0581 144 ASP   A N   
1068 C CA  . ASP   A 138 ? 0.7162 0.4783 0.7437 -0.0913 0.2992  -0.0665 144 ASP   A CA  
1069 C C   . ASP   A 138 ? 0.7677 0.4956 0.8196 -0.1005 0.3489  -0.0785 144 ASP   A C   
1070 O O   . ASP   A 138 ? 0.7741 0.5023 0.8626 -0.1049 0.3663  -0.0899 144 ASP   A O   
1071 C CB  . ASP   A 138 ? 0.7806 0.5101 0.7219 -0.0930 0.2934  -0.0572 144 ASP   A CB  
1072 C CG  . ASP   A 138 ? 0.8503 0.6129 0.7779 -0.0856 0.2494  -0.0487 144 ASP   A CG  
1073 O OD1 . ASP   A 138 ? 0.8355 0.6450 0.8188 -0.0796 0.2264  -0.0508 144 ASP   A OD1 
1074 O OD2 . ASP   A 138 ? 0.9101 0.6480 0.7701 -0.0855 0.2377  -0.0404 144 ASP   A OD2 
1075 N N   . GLU   A 139 ? 0.8075 0.5014 0.8361 -0.1041 0.3742  -0.0759 145 GLU   A N   
1076 C CA  . GLU   A 139 ? 0.8480 0.5016 0.8950 -0.1140 0.4281  -0.0870 145 GLU   A CA  
1077 C C   . GLU   A 139 ? 0.8328 0.5051 0.9584 -0.1137 0.4404  -0.0955 145 GLU   A C   
1078 O O   . GLU   A 139 ? 0.8470 0.5323 0.9655 -0.1082 0.4203  -0.0873 145 GLU   A O   
1079 C CB  . GLU   A 139 ? 0.9553 0.5350 0.8967 -0.1206 0.4578  -0.0782 145 GLU   A CB  
1080 C CG  . GLU   A 139 ? 1.0684 0.6320 0.9474 -0.1157 0.4387  -0.0626 145 GLU   A CG  
1081 C CD  . GLU   A 139 ? 1.2515 0.7620 1.0139 -0.1156 0.4295  -0.0494 145 GLU   A CD  
1082 O OE1 . GLU   A 139 ? 1.3294 0.7706 1.0221 -0.1215 0.4626  -0.0458 145 GLU   A OE1 
1083 O OE2 . GLU   A 139 ? 1.2903 0.8249 1.0306 -0.1096 0.3887  -0.0431 145 GLU   A OE2 
1084 N N1  . A1B2Z B .   ? 0.3324 0.2913 0.3320 0.0226  0.0330  -0.0115 201 A1B2Z A N1  
1085 C C4  . A1B2Z B .   ? 0.4430 0.3064 0.3441 0.0185  0.1050  -0.0088 201 A1B2Z A C4  
1086 C C5  . A1B2Z B .   ? 0.4274 0.3081 0.3457 0.0209  0.0901  -0.0108 201 A1B2Z A C5  
1087 C C6  . A1B2Z B .   ? 0.4078 0.3086 0.3369 0.0219  0.0656  -0.0105 201 A1B2Z A C6  
1088 C C7  . A1B2Z B .   ? 0.4101 0.3069 0.3441 0.0272  0.0578  -0.0178 201 A1B2Z A C7  
1089 C C8  . A1B2Z B .   ? 0.3476 0.2988 0.3370 0.0210  0.0463  -0.0087 201 A1B2Z A C8  
1090 C C10 . A1B2Z B .   ? 0.3241 0.2784 0.3244 0.0261  0.0045  -0.0212 201 A1B2Z A C10 
1091 C C13 . A1B2Z B .   ? 0.2635 0.2731 0.3268 0.0155  0.0196  -0.0030 201 A1B2Z A C13 
1092 O O1  . A1B2Z B .   ? 0.2566 0.2697 0.3318 0.0163  0.0231  -0.0008 201 A1B2Z A O1  
1093 N N2  . A1B2Z B .   ? 0.2555 0.2709 0.3209 0.0122  0.0166  -0.0011 201 A1B2Z A N2  
1094 C C12 . A1B2Z B .   ? 0.2910 0.2843 0.3318 0.0185  0.0193  -0.0080 201 A1B2Z A C12 
1095 C C11 . A1B2Z B .   ? 0.3071 0.2873 0.3415 0.0222  0.0089  -0.0166 201 A1B2Z A C11 
1096 C C9  . A1B2Z B .   ? 0.3436 0.2843 0.3247 0.0268  0.0197  -0.0190 201 A1B2Z A C9  
1097 C C14 . A1B2Z B .   ? 0.2969 0.2813 0.3301 0.0201  0.0310  -0.0073 201 A1B2Z A C14 
1098 O O   . A1B2Z B .   ? 0.3254 0.2945 0.3371 0.0174  0.0511  -0.0038 201 A1B2Z A O   
1099 N N   . A1B2Z B .   ? 0.3962 0.3145 0.3481 0.0234  0.0547  -0.0123 201 A1B2Z A N   
1100 C C1  . A1B2Z B .   ? 0.3997 0.3039 0.3224 0.0208  0.0552  -0.0084 201 A1B2Z A C1  
1101 S S   . A1B2Z B .   ? 0.3709 0.2986 0.3140 0.0212  0.0301  -0.0097 201 A1B2Z A S   
1102 C C   . A1B2Z B .   ? 0.3673 0.2941 0.3011 0.0191  0.0246  -0.0072 201 A1B2Z A C   
1103 C C3  . A1B2Z B .   ? 0.4362 0.3032 0.3290 0.0176  0.0932  -0.0062 201 A1B2Z A C3  
1104 C C2  . A1B2Z B .   ? 0.4193 0.3071 0.3230 0.0189  0.0677  -0.0061 201 A1B2Z A C2  
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