data_7I5A
# 
_entry.id   7I5A 
# 
_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   7I5A         pdb_00007i5a 10.2210/pdb7i5a/pdb 
WWPDB D_1001408333 ?            ?                   
# 
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                        7I5A 
_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 '1-[(3R)-3-(2-hydroxyethyl)piperidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' 293.424   1   ?         ? ? 
? 
3 non-polymer syn 'ZINC ION'                                                                          65.409    1   ?         ? ? 
? 
4 water       nat water                                                                               18.015    106 ?         ? ? 
? 
# 
_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 '1-[(3R)-3-(2-hydroxyethyl)piperidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' A1B3R 
3 'ZINC ION'                                                                          ZN    
4 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 
A1B3R non-polymer         . '1-[(3R)-3-(2-hydroxyethyl)piperidin-1-yl]-2-[2-(methylsulfanyl)phenyl]ethan-1-one' ? 'C16 H23 N O2 S' 
293.424 
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 
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        A1B3R 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3R 
_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 A1B3R 1   201 201 A1B3R LIG A . 
C 3 ZN    1   202 1   ZN    ZN  A . 
D 4 HOH   1   301 98  HOH   HOH A . 
D 4 HOH   2   302 37  HOH   HOH A . 
D 4 HOH   3   303 85  HOH   HOH A . 
D 4 HOH   4   304 99  HOH   HOH A . 
D 4 HOH   5   305 94  HOH   HOH A . 
D 4 HOH   6   306 110 HOH   HOH A . 
D 4 HOH   7   307 47  HOH   HOH A . 
D 4 HOH   8   308 81  HOH   HOH A . 
D 4 HOH   9   309 51  HOH   HOH A . 
D 4 HOH   10  310 38  HOH   HOH A . 
D 4 HOH   11  311 4   HOH   HOH A . 
D 4 HOH   12  312 92  HOH   HOH A . 
D 4 HOH   13  313 59  HOH   HOH A . 
D 4 HOH   14  314 18  HOH   HOH A . 
D 4 HOH   15  315 36  HOH   HOH A . 
D 4 HOH   16  316 32  HOH   HOH A . 
D 4 HOH   17  317 63  HOH   HOH A . 
D 4 HOH   18  318 29  HOH   HOH A . 
D 4 HOH   19  319 25  HOH   HOH A . 
D 4 HOH   20  320 13  HOH   HOH A . 
D 4 HOH   21  321 72  HOH   HOH A . 
D 4 HOH   22  322 42  HOH   HOH A . 
D 4 HOH   23  323 22  HOH   HOH A . 
D 4 HOH   24  324 9   HOH   HOH A . 
D 4 HOH   25  325 86  HOH   HOH A . 
D 4 HOH   26  326 8   HOH   HOH A . 
D 4 HOH   27  327 93  HOH   HOH A . 
D 4 HOH   28  328 76  HOH   HOH A . 
D 4 HOH   29  329 14  HOH   HOH A . 
D 4 HOH   30  330 88  HOH   HOH A . 
D 4 HOH   31  331 90  HOH   HOH A . 
D 4 HOH   32  332 45  HOH   HOH A . 
D 4 HOH   33  333 19  HOH   HOH A . 
D 4 HOH   34  334 82  HOH   HOH A . 
D 4 HOH   35  335 12  HOH   HOH A . 
D 4 HOH   36  336 79  HOH   HOH A . 
D 4 HOH   37  337 16  HOH   HOH A . 
D 4 HOH   38  338 34  HOH   HOH A . 
D 4 HOH   39  339 54  HOH   HOH A . 
D 4 HOH   40  340 7   HOH   HOH A . 
D 4 HOH   41  341 48  HOH   HOH A . 
D 4 HOH   42  342 23  HOH   HOH A . 
D 4 HOH   43  343 57  HOH   HOH A . 
D 4 HOH   44  344 2   HOH   HOH A . 
D 4 HOH   45  345 35  HOH   HOH A . 
D 4 HOH   46  346 87  HOH   HOH A . 
D 4 HOH   47  347 6   HOH   HOH A . 
D 4 HOH   48  348 30  HOH   HOH A . 
D 4 HOH   49  349 17  HOH   HOH A . 
D 4 HOH   50  350 40  HOH   HOH A . 
D 4 HOH   51  351 49  HOH   HOH A . 
D 4 HOH   52  352 71  HOH   HOH A . 
D 4 HOH   53  353 58  HOH   HOH A . 
D 4 HOH   54  354 21  HOH   HOH A . 
D 4 HOH   55  355 103 HOH   HOH A . 
D 4 HOH   56  356 74  HOH   HOH A . 
D 4 HOH   57  357 53  HOH   HOH A . 
D 4 HOH   58  358 78  HOH   HOH A . 
D 4 HOH   59  359 20  HOH   HOH A . 
D 4 HOH   60  360 39  HOH   HOH A . 
D 4 HOH   61  361 46  HOH   HOH A . 
D 4 HOH   62  362 50  HOH   HOH A . 
D 4 HOH   63  363 108 HOH   HOH A . 
D 4 HOH   64  364 67  HOH   HOH A . 
D 4 HOH   65  365 56  HOH   HOH A . 
D 4 HOH   66  366 64  HOH   HOH A . 
D 4 HOH   67  367 5   HOH   HOH A . 
D 4 HOH   68  368 10  HOH   HOH A . 
D 4 HOH   69  369 55  HOH   HOH A . 
D 4 HOH   70  370 3   HOH   HOH A . 
D 4 HOH   71  371 28  HOH   HOH A . 
D 4 HOH   72  372 33  HOH   HOH A . 
D 4 HOH   73  373 80  HOH   HOH A . 
D 4 HOH   74  374 91  HOH   HOH A . 
D 4 HOH   75  375 15  HOH   HOH A . 
D 4 HOH   76  376 26  HOH   HOH A . 
D 4 HOH   77  377 43  HOH   HOH A . 
D 4 HOH   78  378 60  HOH   HOH A . 
D 4 HOH   79  379 83  HOH   HOH A . 
D 4 HOH   80  380 66  HOH   HOH A . 
D 4 HOH   81  381 84  HOH   HOH A . 
D 4 HOH   82  382 75  HOH   HOH A . 
D 4 HOH   83  383 95  HOH   HOH A . 
D 4 HOH   84  384 106 HOH   HOH A . 
D 4 HOH   85  385 109 HOH   HOH A . 
D 4 HOH   86  386 96  HOH   HOH A . 
D 4 HOH   87  387 27  HOH   HOH A . 
D 4 HOH   88  388 31  HOH   HOH A . 
D 4 HOH   89  389 101 HOH   HOH A . 
D 4 HOH   90  390 24  HOH   HOH A . 
D 4 HOH   91  391 70  HOH   HOH A . 
D 4 HOH   92  392 89  HOH   HOH A . 
D 4 HOH   93  393 61  HOH   HOH A . 
D 4 HOH   94  394 68  HOH   HOH A . 
D 4 HOH   95  395 102 HOH   HOH A . 
D 4 HOH   96  396 44  HOH   HOH A . 
D 4 HOH   97  397 100 HOH   HOH A . 
D 4 HOH   98  398 104 HOH   HOH A . 
D 4 HOH   99  399 52  HOH   HOH A . 
D 4 HOH   100 400 69  HOH   HOH A . 
D 4 HOH   101 401 107 HOH   HOH A . 
D 4 HOH   102 402 73  HOH   HOH A . 
D 4 HOH   103 403 62  HOH   HOH A . 
D 4 HOH   104 404 105 HOH   HOH A . 
D 4 HOH   105 405 97  HOH   HOH A . 
D 4 HOH   106 406 111 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           7I5A 
_cell.length_a           73.215 
_cell.length_b           61.710 
_cell.length_c           32.822 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.74 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I5A 
_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          7I5A 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.33 
_exptl_crystal.density_percent_sol   47.21 
_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                     7I5A 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             47.18 
_reflns.d_resolution_high            1.45 
_reflns.number_obs                   25591 
_reflns.percent_possible_obs         98.9 
_reflns.pdbx_Rmerge_I_obs            0.120 
_reflns.pdbx_netI_over_sigmaI        7.5 
_reflns.pdbx_redundancy              6.5 
_reflns.pdbx_Rrim_I_all              0.130 
_reflns.pdbx_Rpim_I_all              0.050 
_reflns.pdbx_CC_half                 0.994 
_reflns.pdbx_number_measured_all     165777 
_reflns.pdbx_chi_squared             0.32 
_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                  1.45 
_reflns_shell.d_res_low                   1.47 
_reflns_shell.number_measured_all         5570 
_reflns_shell.number_unique_obs           1155 
_reflns_shell.Rmerge_I_obs                2.743 
_reflns_shell.pdbx_chi_squared            0.05 
_reflns_shell.pdbx_redundancy             4.8 
_reflns_shell.percent_possible_obs        91.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             3.069 
_reflns_shell.pdbx_Rpim_I_all             1.353 
_reflns_shell.pdbx_CC_half                0.260 
_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                                 7I5A 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     24954 
_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                             47.16 
_refine.ls_d_res_high                            1.449 
_refine.ls_percent_reflns_obs                    96.2 
_refine.ls_R_factor_obs                          0.2215 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2202 
_refine.ls_R_factor_R_free                       0.2476 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.820 
_refine.ls_number_reflns_R_free                  1203 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.947 
_refine.B_iso_mean                               31.08 
_refine.aniso_B[1][1]                            -0.27450 
_refine.aniso_B[2][2]                            -0.99890 
_refine.aniso_B[3][3]                            1.27340 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -4.15920 
_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             0.079 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.080 
_refine.pdbx_overall_SU_R_Blow_DPI               0.081 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.081 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I5A 
_refine_analyze.Luzzati_coordinate_error_obs    0.24 
_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         29 
_refine_hist.number_atoms_solvent             104 
_refine_hist.number_atoms_total               1207 
_refine_hist.d_res_high                       1.449 
_refine_hist.d_res_low                        47.16 
# 
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  1131 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.94  ? 2.00  1536 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  378  '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  202  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 1131 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           3.93  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           13.48 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  138  'X-RAY DIFFRACTION' SEMIHARMONIC 
t_sum_occupancies         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_distance        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_angle           ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_utility_torsion         ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_ideal_dist_contact      ?     ? 4.00  890  '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                       1.45 
_refine_ls_shell.d_res_low                        1.47 
_refine_ls_shell.number_reflns_R_work             487 
_refine_ls_shell.R_factor_R_work                  0.3943 
_refine_ls_shell.percent_reflns_obs               63.18 
_refine_ls_shell.R_factor_R_free                  0.4119 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            2.60 
_refine_ls_shell.number_reflns_R_free             13 
_refine_ls_shell.number_reflns_all                500 
_refine_ls_shell.R_factor_all                     0.3948 
# 
_struct.entry_id                  7I5A 
_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-0036771-001 (A71EV2A-x4809)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I5A 
_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 ? 
# 
_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              7I5A 
_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 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2 AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3 AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4 AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5 AA5 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 C ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.447 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 C ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.219 ? ? 
# 
_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_555 115.6 ? 
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_555 107.8 ? 
3 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 114.9 ? 
4 SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 107.3 ? 
5 SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 101.1 ? 
6 SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? C ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 109.6 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N 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 GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
# 
_pdbx_entry_details.entry_id                   7I5A 
_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_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 CB A PHE 83  ? ? CA A PHE 83  ? ? C A PHE 83  ? ? 96.25  110.40 -14.15 2.00 N 
2 1 CB A GLU 106 ? ? CA A GLU 106 ? ? C A GLU 106 ? ? 122.67 110.40 12.27  2.00 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 ? ? -91.45 30.93  
2 1 GLU A 85 ? ? -66.03 -93.06 
3 1 SER A 87 ? ? 158.57 176.95 
4 1 GLU A 88 ? ? -50.69 -6.69  
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         15.2942 
_pdbx_refine_tls.origin_y         6.6288 
_pdbx_refine_tls.origin_z         14.3139 
_pdbx_refine_tls.T[1][1]          0.0162 
_pdbx_refine_tls.T[2][2]          -0.0519 
_pdbx_refine_tls.T[3][3]          -0.0121 
_pdbx_refine_tls.T[1][2]          -0.0015 
_pdbx_refine_tls.T[1][3]          -0.0751 
_pdbx_refine_tls.T[2][3]          -0.0113 
_pdbx_refine_tls.L[1][1]          0.9563 
_pdbx_refine_tls.L[2][2]          6.7548 
_pdbx_refine_tls.L[3][3]          0.9913 
_pdbx_refine_tls.L[1][2]          1.9275 
_pdbx_refine_tls.L[1][3]          -0.7733 
_pdbx_refine_tls.L[2][3]          -2.6136 
_pdbx_refine_tls.S[1][1]          -0.0923 
_pdbx_refine_tls.S[1][2]          0.0342 
_pdbx_refine_tls.S[1][3]          0.0106 
_pdbx_refine_tls.S[2][1]          0.2010 
_pdbx_refine_tls.S[2][2]          0.0962 
_pdbx_refine_tls.S[2][3]          -0.2405 
_pdbx_refine_tls.S[3][1]          -0.0376 
_pdbx_refine_tls.S[3][2]          -0.1292 
_pdbx_refine_tls.S[3][3]          -0.0038 
# 
_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 
A1B3R C4   C  Y N 1   
A1B3R C5   C  Y N 2   
A1B3R C6   C  Y N 3   
A1B3R C7   C  N N 4   
A1B3R C8   C  N N 5   
A1B3R C10  C  N N 6   
A1B3R C13  C  N N 7   
A1B3R C15  C  N N 8   
A1B3R O    O  N N 9   
A1B3R N    N  N N 10  
A1B3R C12  C  N R 11  
A1B3R C14  C  N N 12  
A1B3R O1   O  N N 13  
A1B3R C11  C  N N 14  
A1B3R C9   C  N N 15  
A1B3R C1   C  Y N 16  
A1B3R S    S  N N 17  
A1B3R C    C  N N 18  
A1B3R C3   C  Y N 19  
A1B3R C2   C  Y N 20  
A1B3R H6   H  N N 21  
A1B3R H7   H  N N 22  
A1B3R H8   H  N N 23  
A1B3R H9   H  N N 24  
A1B3R H12  H  N N 25  
A1B3R H13  H  N N 26  
A1B3R H17  H  N N 27  
A1B3R H16  H  N N 28  
A1B3R H21  H  N N 29  
A1B3R H22  H  N N 30  
A1B3R H    H  N N 31  
A1B3R H18  H  N N 32  
A1B3R H19  H  N N 33  
A1B3R H20  H  N N 34  
A1B3R H14  H  N N 35  
A1B3R H15  H  N N 36  
A1B3R H11  H  N N 37  
A1B3R H10  H  N N 38  
A1B3R H2   H  N N 39  
A1B3R H1   H  N N 40  
A1B3R H3   H  N N 41  
A1B3R H5   H  N N 42  
A1B3R H4   H  N N 43  
ALA   N    N  N N 44  
ALA   CA   C  N S 45  
ALA   C    C  N N 46  
ALA   O    O  N N 47  
ALA   CB   C  N N 48  
ALA   OXT  O  N N 49  
ALA   H    H  N N 50  
ALA   H2   H  N N 51  
ALA   HA   H  N N 52  
ALA   HB1  H  N N 53  
ALA   HB2  H  N N 54  
ALA   HB3  H  N N 55  
ALA   HXT  H  N N 56  
ARG   N    N  N N 57  
ARG   CA   C  N S 58  
ARG   C    C  N N 59  
ARG   O    O  N N 60  
ARG   CB   C  N N 61  
ARG   CG   C  N N 62  
ARG   CD   C  N N 63  
ARG   NE   N  N N 64  
ARG   CZ   C  N N 65  
ARG   NH1  N  N N 66  
ARG   NH2  N  N N 67  
ARG   OXT  O  N N 68  
ARG   H    H  N N 69  
ARG   H2   H  N N 70  
ARG   HA   H  N N 71  
ARG   HB2  H  N N 72  
ARG   HB3  H  N N 73  
ARG   HG2  H  N N 74  
ARG   HG3  H  N N 75  
ARG   HD2  H  N N 76  
ARG   HD3  H  N N 77  
ARG   HE   H  N N 78  
ARG   HH11 H  N N 79  
ARG   HH12 H  N N 80  
ARG   HH21 H  N N 81  
ARG   HH22 H  N N 82  
ARG   HXT  H  N N 83  
ASN   N    N  N N 84  
ASN   CA   C  N S 85  
ASN   C    C  N N 86  
ASN   O    O  N N 87  
ASN   CB   C  N N 88  
ASN   CG   C  N N 89  
ASN   OD1  O  N N 90  
ASN   ND2  N  N N 91  
ASN   OXT  O  N N 92  
ASN   H    H  N N 93  
ASN   H2   H  N N 94  
ASN   HA   H  N N 95  
ASN   HB2  H  N N 96  
ASN   HB3  H  N N 97  
ASN   HD21 H  N N 98  
ASN   HD22 H  N N 99  
ASN   HXT  H  N N 100 
ASP   N    N  N N 101 
ASP   CA   C  N S 102 
ASP   C    C  N N 103 
ASP   O    O  N N 104 
ASP   CB   C  N N 105 
ASP   CG   C  N N 106 
ASP   OD1  O  N N 107 
ASP   OD2  O  N N 108 
ASP   OXT  O  N N 109 
ASP   H    H  N N 110 
ASP   H2   H  N N 111 
ASP   HA   H  N N 112 
ASP   HB2  H  N N 113 
ASP   HB3  H  N N 114 
ASP   HD2  H  N N 115 
ASP   HXT  H  N N 116 
CYS   N    N  N N 117 
CYS   CA   C  N R 118 
CYS   C    C  N N 119 
CYS   O    O  N N 120 
CYS   CB   C  N N 121 
CYS   SG   S  N N 122 
CYS   OXT  O  N N 123 
CYS   H    H  N N 124 
CYS   H2   H  N N 125 
CYS   HA   H  N N 126 
CYS   HB2  H  N N 127 
CYS   HB3  H  N N 128 
CYS   HG   H  N N 129 
CYS   HXT  H  N N 130 
GLN   N    N  N N 131 
GLN   CA   C  N S 132 
GLN   C    C  N N 133 
GLN   O    O  N N 134 
GLN   CB   C  N N 135 
GLN   CG   C  N N 136 
GLN   CD   C  N N 137 
GLN   OE1  O  N N 138 
GLN   NE2  N  N N 139 
GLN   OXT  O  N N 140 
GLN   H    H  N N 141 
GLN   H2   H  N N 142 
GLN   HA   H  N N 143 
GLN   HB2  H  N N 144 
GLN   HB3  H  N N 145 
GLN   HG2  H  N N 146 
GLN   HG3  H  N N 147 
GLN   HE21 H  N N 148 
GLN   HE22 H  N N 149 
GLN   HXT  H  N N 150 
GLU   N    N  N N 151 
GLU   CA   C  N S 152 
GLU   C    C  N N 153 
GLU   O    O  N N 154 
GLU   CB   C  N N 155 
GLU   CG   C  N N 156 
GLU   CD   C  N N 157 
GLU   OE1  O  N N 158 
GLU   OE2  O  N N 159 
GLU   OXT  O  N N 160 
GLU   H    H  N N 161 
GLU   H2   H  N N 162 
GLU   HA   H  N N 163 
GLU   HB2  H  N N 164 
GLU   HB3  H  N N 165 
GLU   HG2  H  N N 166 
GLU   HG3  H  N N 167 
GLU   HE2  H  N N 168 
GLU   HXT  H  N N 169 
GLY   N    N  N N 170 
GLY   CA   C  N N 171 
GLY   C    C  N N 172 
GLY   O    O  N N 173 
GLY   OXT  O  N N 174 
GLY   H    H  N N 175 
GLY   H2   H  N N 176 
GLY   HA2  H  N N 177 
GLY   HA3  H  N N 178 
GLY   HXT  H  N N 179 
HIS   N    N  N N 180 
HIS   CA   C  N S 181 
HIS   C    C  N N 182 
HIS   O    O  N N 183 
HIS   CB   C  N N 184 
HIS   CG   C  Y N 185 
HIS   ND1  N  Y N 186 
HIS   CD2  C  Y N 187 
HIS   CE1  C  Y N 188 
HIS   NE2  N  Y N 189 
HIS   OXT  O  N N 190 
HIS   H    H  N N 191 
HIS   H2   H  N N 192 
HIS   HA   H  N N 193 
HIS   HB2  H  N N 194 
HIS   HB3  H  N N 195 
HIS   HD1  H  N N 196 
HIS   HD2  H  N N 197 
HIS   HE1  H  N N 198 
HIS   HE2  H  N N 199 
HIS   HXT  H  N N 200 
HOH   O    O  N N 201 
HOH   H1   H  N N 202 
HOH   H2   H  N N 203 
ILE   N    N  N N 204 
ILE   CA   C  N S 205 
ILE   C    C  N N 206 
ILE   O    O  N N 207 
ILE   CB   C  N S 208 
ILE   CG1  C  N N 209 
ILE   CG2  C  N N 210 
ILE   CD1  C  N N 211 
ILE   OXT  O  N N 212 
ILE   H    H  N N 213 
ILE   H2   H  N N 214 
ILE   HA   H  N N 215 
ILE   HB   H  N N 216 
ILE   HG12 H  N N 217 
ILE   HG13 H  N N 218 
ILE   HG21 H  N N 219 
ILE   HG22 H  N N 220 
ILE   HG23 H  N N 221 
ILE   HD11 H  N N 222 
ILE   HD12 H  N N 223 
ILE   HD13 H  N N 224 
ILE   HXT  H  N N 225 
LEU   N    N  N N 226 
LEU   CA   C  N S 227 
LEU   C    C  N N 228 
LEU   O    O  N N 229 
LEU   CB   C  N N 230 
LEU   CG   C  N N 231 
LEU   CD1  C  N N 232 
LEU   CD2  C  N N 233 
LEU   OXT  O  N N 234 
LEU   H    H  N N 235 
LEU   H2   H  N N 236 
LEU   HA   H  N N 237 
LEU   HB2  H  N N 238 
LEU   HB3  H  N N 239 
LEU   HG   H  N N 240 
LEU   HD11 H  N N 241 
LEU   HD12 H  N N 242 
LEU   HD13 H  N N 243 
LEU   HD21 H  N N 244 
LEU   HD22 H  N N 245 
LEU   HD23 H  N N 246 
LEU   HXT  H  N N 247 
LYS   N    N  N N 248 
LYS   CA   C  N S 249 
LYS   C    C  N N 250 
LYS   O    O  N N 251 
LYS   CB   C  N N 252 
LYS   CG   C  N N 253 
LYS   CD   C  N N 254 
LYS   CE   C  N N 255 
LYS   NZ   N  N N 256 
LYS   OXT  O  N N 257 
LYS   H    H  N N 258 
LYS   H2   H  N N 259 
LYS   HA   H  N N 260 
LYS   HB2  H  N N 261 
LYS   HB3  H  N N 262 
LYS   HG2  H  N N 263 
LYS   HG3  H  N N 264 
LYS   HD2  H  N N 265 
LYS   HD3  H  N N 266 
LYS   HE2  H  N N 267 
LYS   HE3  H  N N 268 
LYS   HZ1  H  N N 269 
LYS   HZ2  H  N N 270 
LYS   HZ3  H  N N 271 
LYS   HXT  H  N N 272 
MET   N    N  N N 273 
MET   CA   C  N S 274 
MET   C    C  N N 275 
MET   O    O  N N 276 
MET   CB   C  N N 277 
MET   CG   C  N N 278 
MET   SD   S  N N 279 
MET   CE   C  N N 280 
MET   OXT  O  N N 281 
MET   H    H  N N 282 
MET   H2   H  N N 283 
MET   HA   H  N N 284 
MET   HB2  H  N N 285 
MET   HB3  H  N N 286 
MET   HG2  H  N N 287 
MET   HG3  H  N N 288 
MET   HE1  H  N N 289 
MET   HE2  H  N N 290 
MET   HE3  H  N N 291 
MET   HXT  H  N N 292 
PHE   N    N  N N 293 
PHE   CA   C  N S 294 
PHE   C    C  N N 295 
PHE   O    O  N N 296 
PHE   CB   C  N N 297 
PHE   CG   C  Y N 298 
PHE   CD1  C  Y N 299 
PHE   CD2  C  Y N 300 
PHE   CE1  C  Y N 301 
PHE   CE2  C  Y N 302 
PHE   CZ   C  Y N 303 
PHE   OXT  O  N N 304 
PHE   H    H  N N 305 
PHE   H2   H  N N 306 
PHE   HA   H  N N 307 
PHE   HB2  H  N N 308 
PHE   HB3  H  N N 309 
PHE   HD1  H  N N 310 
PHE   HD2  H  N N 311 
PHE   HE1  H  N N 312 
PHE   HE2  H  N N 313 
PHE   HZ   H  N N 314 
PHE   HXT  H  N N 315 
PRO   N    N  N N 316 
PRO   CA   C  N S 317 
PRO   C    C  N N 318 
PRO   O    O  N N 319 
PRO   CB   C  N N 320 
PRO   CG   C  N N 321 
PRO   CD   C  N N 322 
PRO   OXT  O  N N 323 
PRO   H    H  N N 324 
PRO   HA   H  N N 325 
PRO   HB2  H  N N 326 
PRO   HB3  H  N N 327 
PRO   HG2  H  N N 328 
PRO   HG3  H  N N 329 
PRO   HD2  H  N N 330 
PRO   HD3  H  N N 331 
PRO   HXT  H  N N 332 
SER   N    N  N N 333 
SER   CA   C  N S 334 
SER   C    C  N N 335 
SER   O    O  N N 336 
SER   CB   C  N N 337 
SER   OG   O  N N 338 
SER   OXT  O  N N 339 
SER   H    H  N N 340 
SER   H2   H  N N 341 
SER   HA   H  N N 342 
SER   HB2  H  N N 343 
SER   HB3  H  N N 344 
SER   HG   H  N N 345 
SER   HXT  H  N N 346 
THR   N    N  N N 347 
THR   CA   C  N S 348 
THR   C    C  N N 349 
THR   O    O  N N 350 
THR   CB   C  N R 351 
THR   OG1  O  N N 352 
THR   CG2  C  N N 353 
THR   OXT  O  N N 354 
THR   H    H  N N 355 
THR   H2   H  N N 356 
THR   HA   H  N N 357 
THR   HB   H  N N 358 
THR   HG1  H  N N 359 
THR   HG21 H  N N 360 
THR   HG22 H  N N 361 
THR   HG23 H  N N 362 
THR   HXT  H  N N 363 
TRP   N    N  N N 364 
TRP   CA   C  N S 365 
TRP   C    C  N N 366 
TRP   O    O  N N 367 
TRP   CB   C  N N 368 
TRP   CG   C  Y N 369 
TRP   CD1  C  Y N 370 
TRP   CD2  C  Y N 371 
TRP   NE1  N  Y N 372 
TRP   CE2  C  Y N 373 
TRP   CE3  C  Y N 374 
TRP   CZ2  C  Y N 375 
TRP   CZ3  C  Y N 376 
TRP   CH2  C  Y N 377 
TRP   OXT  O  N N 378 
TRP   H    H  N N 379 
TRP   H2   H  N N 380 
TRP   HA   H  N N 381 
TRP   HB2  H  N N 382 
TRP   HB3  H  N N 383 
TRP   HD1  H  N N 384 
TRP   HE1  H  N N 385 
TRP   HE3  H  N N 386 
TRP   HZ2  H  N N 387 
TRP   HZ3  H  N N 388 
TRP   HH2  H  N N 389 
TRP   HXT  H  N N 390 
TYR   N    N  N N 391 
TYR   CA   C  N S 392 
TYR   C    C  N N 393 
TYR   O    O  N N 394 
TYR   CB   C  N N 395 
TYR   CG   C  Y N 396 
TYR   CD1  C  Y N 397 
TYR   CD2  C  Y N 398 
TYR   CE1  C  Y N 399 
TYR   CE2  C  Y N 400 
TYR   CZ   C  Y N 401 
TYR   OH   O  N N 402 
TYR   OXT  O  N N 403 
TYR   H    H  N N 404 
TYR   H2   H  N N 405 
TYR   HA   H  N N 406 
TYR   HB2  H  N N 407 
TYR   HB3  H  N N 408 
TYR   HD1  H  N N 409 
TYR   HD2  H  N N 410 
TYR   HE1  H  N N 411 
TYR   HE2  H  N N 412 
TYR   HH   H  N N 413 
TYR   HXT  H  N N 414 
VAL   N    N  N N 415 
VAL   CA   C  N S 416 
VAL   C    C  N N 417 
VAL   O    O  N N 418 
VAL   CB   C  N N 419 
VAL   CG1  C  N N 420 
VAL   CG2  C  N N 421 
VAL   OXT  O  N N 422 
VAL   H    H  N N 423 
VAL   H2   H  N N 424 
VAL   HA   H  N N 425 
VAL   HB   H  N N 426 
VAL   HG11 H  N N 427 
VAL   HG12 H  N N 428 
VAL   HG13 H  N N 429 
VAL   HG21 H  N N 430 
VAL   HG22 H  N N 431 
VAL   HG23 H  N N 432 
VAL   HXT  H  N N 433 
ZN    ZN   ZN N N 434 
# 
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 
A1B3R C   S    sing N N 1   
A1B3R S   C1   sing N N 2   
A1B3R C1  C2   doub Y N 3   
A1B3R C2  C3   sing Y N 4   
A1B3R C3  C4   doub Y N 5   
A1B3R C4  C5   sing Y N 6   
A1B3R C5  C6   doub Y N 7   
A1B3R C1  C6   sing Y N 8   
A1B3R C6  C7   sing N N 9   
A1B3R C7  C8   sing N N 10  
A1B3R C8  O    doub N N 11  
A1B3R N   C8   sing N N 12  
A1B3R N   C9   sing N N 13  
A1B3R C9  C10  sing N N 14  
A1B3R C10 C11  sing N N 15  
A1B3R C11 C12  sing N N 16  
A1B3R C13 C12  sing N N 17  
A1B3R C14 C13  sing N N 18  
A1B3R O1  C14  sing N N 19  
A1B3R C12 C15  sing N N 20  
A1B3R C15 N    sing N N 21  
A1B3R C4  H6   sing N N 22  
A1B3R C5  H7   sing N N 23  
A1B3R C7  H8   sing N N 24  
A1B3R C7  H9   sing N N 25  
A1B3R C10 H12  sing N N 26  
A1B3R C10 H13  sing N N 27  
A1B3R C13 H17  sing N N 28  
A1B3R C13 H16  sing N N 29  
A1B3R C15 H21  sing N N 30  
A1B3R C15 H22  sing N N 31  
A1B3R C12 H    sing N N 32  
A1B3R C14 H18  sing N N 33  
A1B3R C14 H19  sing N N 34  
A1B3R O1  H20  sing N N 35  
A1B3R C11 H14  sing N N 36  
A1B3R C11 H15  sing N N 37  
A1B3R C9  H11  sing N N 38  
A1B3R C9  H10  sing N N 39  
A1B3R C   H2   sing N N 40  
A1B3R C   H1   sing N N 41  
A1B3R C   H3   sing N N 42  
A1B3R C3  H5   sing N N 43  
A1B3R C2  H4   sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
GLN   N   CA   sing N N 127 
GLN   N   H    sing N N 128 
GLN   N   H2   sing N N 129 
GLN   CA  C    sing N N 130 
GLN   CA  CB   sing N N 131 
GLN   CA  HA   sing N N 132 
GLN   C   O    doub N N 133 
GLN   C   OXT  sing N N 134 
GLN   CB  CG   sing N N 135 
GLN   CB  HB2  sing N N 136 
GLN   CB  HB3  sing N N 137 
GLN   CG  CD   sing N N 138 
GLN   CG  HG2  sing N N 139 
GLN   CG  HG3  sing N N 140 
GLN   CD  OE1  doub N N 141 
GLN   CD  NE2  sing N N 142 
GLN   NE2 HE21 sing N N 143 
GLN   NE2 HE22 sing N N 144 
GLN   OXT HXT  sing N N 145 
GLU   N   CA   sing N N 146 
GLU   N   H    sing N N 147 
GLU   N   H2   sing N N 148 
GLU   CA  C    sing N N 149 
GLU   CA  CB   sing N N 150 
GLU   CA  HA   sing N N 151 
GLU   C   O    doub N N 152 
GLU   C   OXT  sing N N 153 
GLU   CB  CG   sing N N 154 
GLU   CB  HB2  sing N N 155 
GLU   CB  HB3  sing N N 156 
GLU   CG  CD   sing N N 157 
GLU   CG  HG2  sing N N 158 
GLU   CG  HG3  sing N N 159 
GLU   CD  OE1  doub N N 160 
GLU   CD  OE2  sing N N 161 
GLU   OE2 HE2  sing N N 162 
GLU   OXT HXT  sing N N 163 
GLY   N   CA   sing N N 164 
GLY   N   H    sing N N 165 
GLY   N   H2   sing N N 166 
GLY   CA  C    sing N N 167 
GLY   CA  HA2  sing N N 168 
GLY   CA  HA3  sing N N 169 
GLY   C   O    doub N N 170 
GLY   C   OXT  sing N N 171 
GLY   OXT HXT  sing N N 172 
HIS   N   CA   sing N N 173 
HIS   N   H    sing N N 174 
HIS   N   H2   sing N N 175 
HIS   CA  C    sing N N 176 
HIS   CA  CB   sing N N 177 
HIS   CA  HA   sing N N 178 
HIS   C   O    doub N N 179 
HIS   C   OXT  sing N N 180 
HIS   CB  CG   sing N N 181 
HIS   CB  HB2  sing N N 182 
HIS   CB  HB3  sing N N 183 
HIS   CG  ND1  sing Y N 184 
HIS   CG  CD2  doub Y N 185 
HIS   ND1 CE1  doub Y N 186 
HIS   ND1 HD1  sing N N 187 
HIS   CD2 NE2  sing Y N 188 
HIS   CD2 HD2  sing N N 189 
HIS   CE1 NE2  sing Y N 190 
HIS   CE1 HE1  sing N N 191 
HIS   NE2 HE2  sing N N 192 
HIS   OXT HXT  sing N N 193 
HOH   O   H1   sing N N 194 
HOH   O   H2   sing N N 195 
ILE   N   CA   sing N N 196 
ILE   N   H    sing N N 197 
ILE   N   H2   sing N N 198 
ILE   CA  C    sing N N 199 
ILE   CA  CB   sing N N 200 
ILE   CA  HA   sing N N 201 
ILE   C   O    doub N N 202 
ILE   C   OXT  sing N N 203 
ILE   CB  CG1  sing N N 204 
ILE   CB  CG2  sing N N 205 
ILE   CB  HB   sing N N 206 
ILE   CG1 CD1  sing N N 207 
ILE   CG1 HG12 sing N N 208 
ILE   CG1 HG13 sing N N 209 
ILE   CG2 HG21 sing N N 210 
ILE   CG2 HG22 sing N N 211 
ILE   CG2 HG23 sing N N 212 
ILE   CD1 HD11 sing N N 213 
ILE   CD1 HD12 sing N N 214 
ILE   CD1 HD13 sing N N 215 
ILE   OXT HXT  sing N N 216 
LEU   N   CA   sing N N 217 
LEU   N   H    sing N N 218 
LEU   N   H2   sing N N 219 
LEU   CA  C    sing N N 220 
LEU   CA  CB   sing N N 221 
LEU   CA  HA   sing N N 222 
LEU   C   O    doub N N 223 
LEU   C   OXT  sing N N 224 
LEU   CB  CG   sing N N 225 
LEU   CB  HB2  sing N N 226 
LEU   CB  HB3  sing N N 227 
LEU   CG  CD1  sing N N 228 
LEU   CG  CD2  sing N N 229 
LEU   CG  HG   sing N N 230 
LEU   CD1 HD11 sing N N 231 
LEU   CD1 HD12 sing N N 232 
LEU   CD1 HD13 sing N N 233 
LEU   CD2 HD21 sing N N 234 
LEU   CD2 HD22 sing N N 235 
LEU   CD2 HD23 sing N N 236 
LEU   OXT HXT  sing N N 237 
LYS   N   CA   sing N N 238 
LYS   N   H    sing N N 239 
LYS   N   H2   sing N N 240 
LYS   CA  C    sing N N 241 
LYS   CA  CB   sing N N 242 
LYS   CA  HA   sing N N 243 
LYS   C   O    doub N N 244 
LYS   C   OXT  sing N N 245 
LYS   CB  CG   sing N N 246 
LYS   CB  HB2  sing N N 247 
LYS   CB  HB3  sing N N 248 
LYS   CG  CD   sing N N 249 
LYS   CG  HG2  sing N N 250 
LYS   CG  HG3  sing N N 251 
LYS   CD  CE   sing N N 252 
LYS   CD  HD2  sing N N 253 
LYS   CD  HD3  sing N N 254 
LYS   CE  NZ   sing N N 255 
LYS   CE  HE2  sing N N 256 
LYS   CE  HE3  sing N N 257 
LYS   NZ  HZ1  sing N N 258 
LYS   NZ  HZ2  sing N N 259 
LYS   NZ  HZ3  sing N N 260 
LYS   OXT HXT  sing N N 261 
MET   N   CA   sing N N 262 
MET   N   H    sing N N 263 
MET   N   H2   sing N N 264 
MET   CA  C    sing N N 265 
MET   CA  CB   sing N N 266 
MET   CA  HA   sing N N 267 
MET   C   O    doub N N 268 
MET   C   OXT  sing N N 269 
MET   CB  CG   sing N N 270 
MET   CB  HB2  sing N N 271 
MET   CB  HB3  sing N N 272 
MET   CG  SD   sing N N 273 
MET   CG  HG2  sing N N 274 
MET   CG  HG3  sing N N 275 
MET   SD  CE   sing N N 276 
MET   CE  HE1  sing N N 277 
MET   CE  HE2  sing N N 278 
MET   CE  HE3  sing N N 279 
MET   OXT HXT  sing N N 280 
PHE   N   CA   sing N N 281 
PHE   N   H    sing N N 282 
PHE   N   H2   sing N N 283 
PHE   CA  C    sing N N 284 
PHE   CA  CB   sing N N 285 
PHE   CA  HA   sing N N 286 
PHE   C   O    doub N N 287 
PHE   C   OXT  sing N N 288 
PHE   CB  CG   sing N N 289 
PHE   CB  HB2  sing N N 290 
PHE   CB  HB3  sing N N 291 
PHE   CG  CD1  doub Y N 292 
PHE   CG  CD2  sing Y N 293 
PHE   CD1 CE1  sing Y N 294 
PHE   CD1 HD1  sing N N 295 
PHE   CD2 CE2  doub Y N 296 
PHE   CD2 HD2  sing N N 297 
PHE   CE1 CZ   doub Y N 298 
PHE   CE1 HE1  sing N N 299 
PHE   CE2 CZ   sing Y N 300 
PHE   CE2 HE2  sing N N 301 
PHE   CZ  HZ   sing N N 302 
PHE   OXT HXT  sing N N 303 
PRO   N   CA   sing N N 304 
PRO   N   CD   sing N N 305 
PRO   N   H    sing N N 306 
PRO   CA  C    sing N N 307 
PRO   CA  CB   sing N N 308 
PRO   CA  HA   sing N N 309 
PRO   C   O    doub N N 310 
PRO   C   OXT  sing N N 311 
PRO   CB  CG   sing N N 312 
PRO   CB  HB2  sing N N 313 
PRO   CB  HB3  sing N N 314 
PRO   CG  CD   sing N N 315 
PRO   CG  HG2  sing N N 316 
PRO   CG  HG3  sing N N 317 
PRO   CD  HD2  sing N N 318 
PRO   CD  HD3  sing N N 319 
PRO   OXT HXT  sing N N 320 
SER   N   CA   sing N N 321 
SER   N   H    sing N N 322 
SER   N   H2   sing N N 323 
SER   CA  C    sing N N 324 
SER   CA  CB   sing N N 325 
SER   CA  HA   sing N N 326 
SER   C   O    doub N N 327 
SER   C   OXT  sing N N 328 
SER   CB  OG   sing N N 329 
SER   CB  HB2  sing N N 330 
SER   CB  HB3  sing N N 331 
SER   OG  HG   sing N N 332 
SER   OXT HXT  sing N N 333 
THR   N   CA   sing N N 334 
THR   N   H    sing N N 335 
THR   N   H2   sing N N 336 
THR   CA  C    sing N N 337 
THR   CA  CB   sing N N 338 
THR   CA  HA   sing N N 339 
THR   C   O    doub N N 340 
THR   C   OXT  sing N N 341 
THR   CB  OG1  sing N N 342 
THR   CB  CG2  sing N N 343 
THR   CB  HB   sing N N 344 
THR   OG1 HG1  sing N N 345 
THR   CG2 HG21 sing N N 346 
THR   CG2 HG22 sing N N 347 
THR   CG2 HG23 sing N N 348 
THR   OXT HXT  sing N N 349 
TRP   N   CA   sing N N 350 
TRP   N   H    sing N N 351 
TRP   N   H2   sing N N 352 
TRP   CA  C    sing N N 353 
TRP   CA  CB   sing N N 354 
TRP   CA  HA   sing N N 355 
TRP   C   O    doub N N 356 
TRP   C   OXT  sing N N 357 
TRP   CB  CG   sing N N 358 
TRP   CB  HB2  sing N N 359 
TRP   CB  HB3  sing N N 360 
TRP   CG  CD1  doub Y N 361 
TRP   CG  CD2  sing Y N 362 
TRP   CD1 NE1  sing Y N 363 
TRP   CD1 HD1  sing N N 364 
TRP   CD2 CE2  doub Y N 365 
TRP   CD2 CE3  sing Y N 366 
TRP   NE1 CE2  sing Y N 367 
TRP   NE1 HE1  sing N N 368 
TRP   CE2 CZ2  sing Y N 369 
TRP   CE3 CZ3  doub Y N 370 
TRP   CE3 HE3  sing N N 371 
TRP   CZ2 CH2  doub Y N 372 
TRP   CZ2 HZ2  sing N N 373 
TRP   CZ3 CH2  sing Y N 374 
TRP   CZ3 HZ3  sing N N 375 
TRP   CH2 HH2  sing N N 376 
TRP   OXT HXT  sing N N 377 
TYR   N   CA   sing N N 378 
TYR   N   H    sing N N 379 
TYR   N   H2   sing N N 380 
TYR   CA  C    sing N N 381 
TYR   CA  CB   sing N N 382 
TYR   CA  HA   sing N N 383 
TYR   C   O    doub N N 384 
TYR   C   OXT  sing N N 385 
TYR   CB  CG   sing N N 386 
TYR   CB  HB2  sing N N 387 
TYR   CB  HB3  sing N N 388 
TYR   CG  CD1  doub Y N 389 
TYR   CG  CD2  sing Y N 390 
TYR   CD1 CE1  sing Y N 391 
TYR   CD1 HD1  sing N N 392 
TYR   CD2 CE2  doub Y N 393 
TYR   CD2 HD2  sing N N 394 
TYR   CE1 CZ   doub Y N 395 
TYR   CE1 HE1  sing N N 396 
TYR   CE2 CZ   sing Y N 397 
TYR   CE2 HE2  sing N N 398 
TYR   CZ  OH   sing N N 399 
TYR   OH  HH   sing N N 400 
TYR   OXT HXT  sing N N 401 
VAL   N   CA   sing N N 402 
VAL   N   H    sing N N 403 
VAL   N   H2   sing N N 404 
VAL   CA  C    sing N N 405 
VAL   CA  CB   sing N N 406 
VAL   CA  HA   sing N N 407 
VAL   C   O    doub N N 408 
VAL   C   OXT  sing N N 409 
VAL   CB  CG1  sing N N 410 
VAL   CB  CG2  sing N N 411 
VAL   CB  HB   sing N N 412 
VAL   CG1 HG11 sing N N 413 
VAL   CG1 HG12 sing N N 414 
VAL   CG1 HG13 sing N N 415 
VAL   CG2 HG21 sing N N 416 
VAL   CG2 HG22 sing N N 417 
VAL   CG2 HG23 sing N N 418 
VAL   OXT HXT  sing N N 419 
# 
_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                    7I5A 
_atom_sites.fract_transf_matrix[1][1]   0.013658 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000654 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016205 
_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]   0.030502 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 19.143 5.996   24.365 1.00 33.19 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 20.330 6.158   23.523 1.00 33.72 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 20.451 4.988   22.535 1.00 32.04 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 19.806 3.952   22.728 1.00 32.32 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 21.579 6.257   24.396 1.00 37.09 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 21.659 5.083   25.188 1.00 42.23 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 21.265 5.158   21.492 1.00 29.96 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 21.471 4.126   20.480 1.00 28.77 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 21.729 4.676   19.090 1.00 27.99 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 21.309 5.793   18.770 1.00 27.53 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 22.430 3.908   18.251 1.00 26.64 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 22.755 4.361   16.891 1.00 26.41 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 22.806 3.172   15.893 1.00 25.73 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 22.888 2.025   16.326 1.00 25.86 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 24.115 5.064   16.914 1.00 27.07 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 22.781 3.460   14.574 1.00 24.98 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.923 2.491   13.490 1.00 25.55 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 24.303 2.725   12.846 1.00 28.02 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.672 3.860   12.563 1.00 27.21 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.805 2.692   12.426 1.00 24.74 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 20.420 2.651   13.048 1.00 23.60 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.945 1.699   11.280 1.00 25.51 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 19.367 3.256   12.123 1.00 23.07 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 25.062 1.646   12.629 1.00 30.47 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 26.391 1.680   12.022 1.00 32.53 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 26.354 0.875   10.728 1.00 34.56 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 26.220 -0.355  10.785 1.00 35.67 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 27.409 1.035   12.985 1.00 32.71 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 27.571 1.827   14.257 1.00 32.45 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 28.409 2.932   14.308 1.00 33.52 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 26.815 1.536   15.378 1.00 32.86 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 28.504 3.714   15.451 1.00 34.57 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 26.896 2.311   16.524 1.00 33.87 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 27.755 3.390   16.562 1.00 35.08 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 27.834 4.161   17.687 1.00 36.80 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 26.461 1.559   9.578  1.00 35.18 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 26.442 0.988   8.229  1.00 36.33 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.563 1.615   7.382  1.00 37.27 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.562 2.817   7.104  1.00 37.51 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 25.049 1.123   7.556  1.00 37.65 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.492 2.545   7.689  1.00 37.56 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 25.104 0.688   6.097  1.00 39.16 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.546 0.804   6.996  1.00 37.48 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.704 1.293   6.265  1.00 39.52 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.473 2.301   7.101  1.00 40.47 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.580 2.131   8.323  1.00 40.99 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.863 3.408   6.503  1.00 40.26 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.566 4.464   7.227  1.00 40.80 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.589 5.511   7.800  1.00 38.48 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.974 6.664   7.975  1.00 38.31 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.603 5.114   6.325  1.00 44.47 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.835 4.261   6.136  1.00 51.70 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.275 3.547   7.044  1.00 53.13 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 34.437 4.320   4.954  1.00 55.27 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.354 5.097   8.159  1.00 35.89 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.347 6.026   8.712  1.00 34.24 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.794 5.602   10.081 1.00 31.82 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.618 4.408   10.364 1.00 31.39 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.142 6.185   7.753  1.00 33.79 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.481 6.775   6.408  1.00 35.16 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.026 8.050   6.304  1.00 36.29 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.193 6.093   5.234  1.00 36.38 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.345 8.599   5.069  1.00 38.02 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.486 6.641   3.989  1.00 37.79 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.066 7.896   3.911  1.00 39.46 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.356 8.464   2.687  1.00 41.61 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.421 6.625   10.889 1.00 29.38 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.767 6.470   12.185 1.00 27.41 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.453 7.291   12.110 1.00 25.24 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.483 8.497   11.853 1.00 24.03 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.662 6.995   13.317 1.00 28.82 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.991 7.118   14.686 1.00 30.32 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 28.015 7.475   15.758 1.00 33.29 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 27.555 8.509   16.689 1.00 34.60 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 27.013 8.262   17.880 1.00 36.60 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 26.827 7.005   18.288 1.00 34.53 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 26.632 9.265   18.664 1.00 35.83 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 24.314 6.630   12.296 1.00 23.68 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.992 7.291   12.273 1.00 22.52 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 22.477 7.437   13.705 1.00 22.31 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 22.265 6.419   14.386 1.00 23.38 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.960 6.513   11.419 1.00 22.75 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.680 7.371   11.244 1.00 22.42 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.549 6.122   10.060 1.00 22.80 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 22.241 8.669   14.164 1.00 20.76 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.761 8.885   15.536 1.00 20.65 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 20.550 9.833   15.553 1.00 19.51 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 20.314 10.554  14.574 1.00 18.74 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.899 9.511   16.395 1.00 23.25 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 24.024 8.524   16.588 1.00 25.70 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 23.388 10.803  15.755 1.00 23.03 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.811 9.898   16.688 1.00 18.26 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.745 10.923  16.825 1.00 18.33 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 19.486 12.290  16.833 1.00 19.75 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 20.486 12.450  17.565 1.00 21.17 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.982 10.819  18.162 1.00 18.42 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 17.114 9.581   18.261 1.00 20.83 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.555 8.546   18.785 1.00 23.05 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.894 9.650   17.749 1.00 19.23 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 19.060 13.213  15.972 1.00 18.48 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.703 14.547  15.892 1.00 18.09 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.759 15.244  17.274 1.00 20.53 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.792 15.856  17.592 1.00 22.47 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.941 15.424  14.878 1.00 17.45 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.666 16.738  14.524 1.00 19.02 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.718 17.594  13.703 1.00 18.93 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.296 18.842  13.170 1.00 19.97 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.367 19.984  13.854 1.00 22.67 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.986 20.030  15.127 1.00 20.62 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.819 21.090  13.267 1.00 23.59 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.701 15.090  18.122 1.00 21.14 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 18.691 15.741  19.461 1.00 23.39 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 19.696 15.144  20.463 1.00 25.10 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 20.028 15.790  21.492 1.00 26.44 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 17.276 15.809  20.076 1.00 24.52 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 16.707 14.500  20.556 1.00 24.50 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 16.023 13.632  19.695 1.00 25.73 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 16.672 13.989  21.817 1.00 25.55 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 15.619 12.616  20.460 1.00 26.85 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 15.988 12.785  21.746 1.00 26.89 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 20.219 13.942  20.145 1.00 24.42 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 21.206 13.279  20.982 1.00 26.48 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 22.629 13.307  20.377 1.00 27.10 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 23.529 12.703  20.966 1.00 27.83 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 20.763 11.827  21.287 1.00 27.17 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 19.432 11.724  22.063 1.00 29.57 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 19.027 10.268  22.301 1.00 29.95 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 19.494 12.503  23.403 1.00 30.45 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.817 13.910  19.161 1.00 26.27 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 24.140 13.940  18.525 1.00 27.31 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 25.187 14.614  19.432 1.00 28.96 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.859 15.586  20.110 1.00 29.50 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 24.080 14.678  17.196 1.00 26.78 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 26.423 14.100  19.436 1.00 30.55 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 27.530 14.632  20.268 1.00 32.84 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 28.340 15.747  19.533 1.00 34.00 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 28.117 15.962  18.354 1.00 32.70 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 28.478 13.460  20.601 1.00 35.25 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 29.074 13.032  19.372 1.00 37.09 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 27.776 12.337  21.286 1.00 35.50 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 29.382 16.359  20.190 1.00 35.94 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 30.240 17.316  19.496 1.00 38.16 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.969 16.620  18.336 1.00 37.35 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 31.095 17.209  17.257 1.00 37.65 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 31.282 17.915  20.463 1.00 41.83 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 30.688 18.661  21.612 1.00 48.87 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 29.887 19.762  21.412 1.00 52.30 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 30.872 18.487  22.946 1.00 52.04 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 29.585 20.214  22.620 1.00 53.72 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 30.152 19.476  23.576 1.00 53.77 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 31.429 15.367  18.569 1.00 36.90 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 32.091 14.543  17.567 1.00 37.54 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 31.186 14.304  16.356 1.00 35.22 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.634 14.459  15.223 1.00 35.91 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 32.521 13.206  18.162 1.00 42.38 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 33.442 12.455  17.234 1.00 51.84 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.522 12.955  16.885 1.00 55.44 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 33.040 11.249  16.803 1.00 53.67 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.899 13.985  16.582 1.00 32.67 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.955 13.814  15.470 1.00 30.55 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.871 15.098  14.620 1.00 29.15 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.949 15.022  13.395 1.00 29.59 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.556 13.454  15.992 1.00 30.23 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 27.463 12.030  16.510 1.00 31.52 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 28.002 11.125  15.848 1.00 31.75 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.843 11.826  17.579 1.00 32.88 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.751 16.271  15.266 1.00 27.87 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.641 17.538  14.522 1.00 28.86 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.970 17.927  13.812 1.00 31.30 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.938 18.505  12.717 1.00 31.12 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.146 18.671  15.460 1.00 28.07 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.655 18.697  15.630 1.00 26.33 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.938 18.205  16.682 1.00 26.81 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.699 19.248  14.708 1.00 24.78 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.585 18.427  16.476 1.00 26.22 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.412 19.021  15.248 1.00 25.43 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.800 19.817  13.436 1.00 24.66 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.244 19.444  14.603 1.00 24.91 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.642 20.243  12.797 1.00 24.80 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.381 20.027  13.367 1.00 24.70 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 31.121 17.573  14.409 1.00 33.31 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.422 17.865  13.790 1.00 36.09 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.706 16.945  12.570 1.00 37.40 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.589 17.253  11.771 1.00 38.77 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.549 17.737  14.822 1.00 36.64 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.979 15.816  12.440 1.00 35.94 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.139 14.874  11.323 1.00 35.15 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.784 14.702  10.589 1.00 32.69 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.449 13.608  10.158 1.00 31.87 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.639 13.540  11.841 1.00 37.54 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 34.053 13.617  12.412 1.00 42.72 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.019 13.899  11.699 1.00 46.11 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 34.201 13.345  13.698 1.00 42.27 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.003 15.789  10.509 1.00 31.52 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 28.674 15.791  9.924  1.00 29.64 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 28.682 15.420  8.440  1.00 30.51 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.465 15.984  7.680  1.00 32.29 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.054 17.187  10.113 1.00 28.20 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 26.678 17.389  9.502  1.00 27.33 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.639 16.533  10.222 1.00 27.30 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.280 18.864  9.520  1.00 26.18 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 27.752 14.525  8.018  1.00 28.48 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.555 14.152  6.619  1.00 28.05 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.200 14.764  6.132  1.00 27.33 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.124 15.420  5.085  1.00 28.64 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.547 12.608  6.455  1.00 28.65 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.090 12.218  5.053  1.00 29.42 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 28.933 12.026  6.754  1.00 29.19 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.155 14.598  6.950  1.00 25.51 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 23.807 15.080  6.658  1.00 24.08 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 22.972 15.132  7.961  1.00 22.51 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.125 14.293  8.849  1.00 21.88 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.151 14.109  5.634  1.00 24.18 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 21.670 14.278  5.391  1.00 24.14 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.064 15.138  4.515  1.00 25.34 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 20.612 13.550  6.039  1.00 22.91 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 19.685 14.976  4.569  1.00 25.32 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 19.388 14.003  5.495  1.00 23.71 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.585 12.566  7.034  1.00 22.40 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.150 13.459  5.880  1.00 22.84 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.357 12.062  7.442  1.00 22.90 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.162 12.496  6.858  1.00 22.41 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.068 16.097  8.050  1.00 20.76 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.144 16.193  9.181  1.00 20.22 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 19.818 16.787  8.691  1.00 19.48 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 19.802 17.580  7.749  1.00 19.45 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 21.710 17.002  10.355 1.00 21.09 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.264 18.372  9.970  1.00 21.29 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.245 19.491  9.872  1.00 24.04 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 21.496 20.466  9.121  1.00 28.34 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.187 19.401  10.531 1.00 21.96 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 18.723 16.383  9.328  1.00 18.51 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.402 16.908  8.996  1.00 17.88 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.620 17.113  10.304 1.00 18.11 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.221 16.148  10.960 1.00 19.04 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 16.707 16.017  7.964  1.00 19.22 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 15.393 16.563  7.453  1.00 24.49 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 14.715 17.266  8.212  1.00 23.48 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.047 16.280  6.269  1.00 26.77 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.422 18.399  10.701 1.00 18.14 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.742 18.718  11.949 0.50 18.49 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.749 18.686  11.962 0.50 18.75 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.298 18.192  11.939 1.00 19.16 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.814 17.714  12.950 1.00 19.84 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.756 20.229  12.193 0.50 19.49 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.803 20.179  12.286 0.50 20.52 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 15.152 20.553  13.434 0.50 20.41 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.052 20.909  11.334 0.50 22.61 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.624 18.284  10.786 1.00 18.26 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.231 17.832  10.692 1.00 18.74 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.103 16.309  10.881 1.00 18.66 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.016 15.838  11.219 1.00 19.60 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 11.575 18.258  9.382  1.00 21.72 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.014 17.466  8.288  1.00 25.13 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.189 15.553  10.659 1.00 16.53 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.159 14.083  10.817 1.00 16.04 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.775 13.608  12.137 1.00 16.14 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.700 12.400  12.446 1.00 16.78 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 13.903 13.385  9.652  1.00 16.49 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.243 13.615  8.303  1.00 17.72 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.007 12.962  7.149  1.00 19.95 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.038 11.492  7.221  1.00 19.85 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.184 10.697  6.150  1.00 19.73 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.224 11.218  4.923  1.00 20.67 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.212 9.368   6.295  1.00 20.40 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.430 14.524  12.889 1.00 16.73 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 15.171 14.165  14.106 1.00 15.81 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.297 13.175  13.774 1.00 15.90 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.623 12.344  14.617 1.00 17.04 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 14.276 13.601  15.230 1.00 16.82 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 15.010 13.358  16.555 1.00 20.07 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.882 14.191  16.919 1.00 20.02 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.766 12.281  17.200 1.00 19.45 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.937 13.303  12.570 1.00 15.16 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 18.095 12.451  12.202 1.00 15.64 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.381 13.243  11.977 1.00 17.40 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.369 14.315  11.365 1.00 18.89 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.868 11.634  10.899 1.00 15.41 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.796 10.530  10.970 1.00 17.41 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.708 9.779   9.601  1.00 16.76 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.092 9.518   12.082 1.00 18.30 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.498 12.604  12.284 1.00 17.33 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.807 13.136  11.967 1.00 18.71 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.706 11.944  11.618 1.00 19.66 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.611 10.896  12.274 1.00 20.41 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.406 13.975  13.124 1.00 19.66 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.808 14.582  12.860 1.00 21.75 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.993 15.911  13.633 1.00 23.39 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.945 13.618  13.315 1.00 23.59 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.512 12.072  10.543 1.00 19.80 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.462 11.039  10.111 1.00 20.94 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.871 11.649  10.146 1.00 23.09 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.107 12.735  9.578  1.00 23.03 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.132 10.469  8.699  1.00 22.53 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.156 9.398   8.255  1.00 23.85 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.701 9.906   8.664  1.00 22.03 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.785 10.959  10.845 1.00 24.23 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.170 11.397  10.917 1.00 26.99 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 29.084 10.289  10.349 1.00 30.28 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.677 9.131   10.234 1.00 29.47 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.560 11.763  12.351 1.00 27.67 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.438 10.651  13.230 1.00 28.76 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.324 10.664  9.984  1.00 33.33 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.274 9.700   9.442  1.00 37.20 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 32.053 8.963   10.539 1.00 41.52 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.245 9.474   11.644 1.00 42.25 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.244 10.399  8.495  1.00 38.69 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 32.887 11.464  9.173  1.00 41.04 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.494 7.743   10.234 1.00 43.97 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 33.268 6.931   11.172 1.00 47.71 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.494 6.390   10.443 1.00 52.85 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.462 6.222   9.220  1.00 54.13 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 32.446 5.723   11.684 1.00 47.81 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 32.240 4.824   10.603 1.00 48.29 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 31.102 6.117   12.282 1.00 47.53 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 35.532 6.043   11.190 1.00 55.43 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.732 5.464   10.598 1.00 58.58 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.551 3.933   10.413 1.00 60.34 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 37.097 3.353   9.473  1.00 62.11 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.963 5.861   11.430 1.00 61.50 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 37.714 5.536   12.801 1.00 63.80 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 38.287 7.337   11.318 1.00 62.52 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.800 3.275   11.310 1.00 59.69 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 35.579 1.832   11.224 1.00 60.00 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 34.399 1.478   10.297 1.00 60.06 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 33.561 2.333   10.013 1.00 59.90 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 35.361 1.263   12.616 1.00 60.28 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 34.342 0.221   9.810  1.00 60.47 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 33.286 -0.227  8.899  1.00 60.72 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 32.117 -0.868  9.648  1.00 58.96 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 32.306 -1.834  10.373 1.00 59.24 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 33.856 -1.205  7.850  1.00 64.06 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.245 -1.049  6.454  1.00 70.43 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 33.682 0.224   5.758  1.00 77.30 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 34.805 0.718   5.954  1.00 80.67 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 32.817 0.780   4.910  1.00 77.07 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.924 -0.325  9.444  1.00 56.42 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.678 -0.783  10.049 1.00 54.70 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 29.033 -1.919  9.280  1.00 51.84 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 29.077 -1.948  8.048  1.00 52.05 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 28.393 -2.825  9.994  1.00 48.91 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 27.808 -4.010  9.387  1.00 47.14 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 26.304 -4.151  9.559  1.00 43.48 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 25.789 -5.277  9.412  1.00 43.40 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 28.527 -5.247  9.901  1.00 49.82 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 30.248 -5.354  9.379  1.00 57.46 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 25.590 -3.050  9.877  1.00 39.91 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 24.137 -3.151  10.001 1.00 38.43 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.555 -3.194  8.578  1.00 37.65 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.078 -2.546  7.667  1.00 38.81 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 23.531 -1.974  10.823 1.00 39.86 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 23.733 -2.049  12.333 1.00 43.53 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 23.775 -3.163  12.866 1.00 45.21 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 23.825 -0.977  12.984 1.00 44.67 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.499 -3.944  8.381  1.00 36.80 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 21.843 -4.048  7.076  1.00 36.63 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.611 -3.176  7.097  1.00 34.30 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.753 -3.414  7.933  1.00 34.06 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.366 -5.488  6.852  1.00 39.05 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 22.516 -6.343  6.784  1.00 41.55 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 20.538 -5.627  5.574  1.00 38.74 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.482 -2.223  6.172  1.00 31.69 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.280 -1.395  6.132  1.00 28.93 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.212 -2.111  5.294  1.00 28.32 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.512 -2.603  4.187  1.00 29.24 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.600 0.000   5.554  1.00 28.24 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.840 0.639   6.248  1.00 29.17 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.366 0.929   5.632  1.00 27.26 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.647 0.951   7.744  1.00 29.84 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 16.985 -2.155  5.799  1.00 26.78 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 15.852 -2.743  5.082  1.00 26.21 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.462 -1.819  3.913  1.00 26.47 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.483 -0.598  4.060  1.00 25.67 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.663 -2.884  6.027  1.00 25.03 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.119 -2.419  2.746  1.00 27.35 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 14.653 -1.692  1.571  1.00 29.33 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 13.315 -2.370  1.237  1.00 31.12 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 13.293 -3.389  0.527  1.00 32.38 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 15.680 -1.834  0.439  1.00 30.94 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.077 -1.266  0.776  1.00 31.79 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.105 0.234   1.236  1.00 32.73 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 18.467 0.676   1.569  1.00 34.06 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 18.761 1.812   2.211  1.00 32.87 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 17.796 2.638   2.590  1.00 28.70 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.023 2.124   2.476  1.00 31.16 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.202 -1.871  1.844  1.00 31.38 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 10.900 -2.558  1.773  1.00 32.02 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 9.755  -1.609  2.220  1.00 32.22 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.010 -0.479  2.647  1.00 30.88 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 10.968 -3.742  2.730  1.00 31.33 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.099 -3.221  4.467  1.00 29.62 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 8.497  -2.145  2.248  1.00 32.01 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 7.379  -1.381  2.789  1.00 32.99 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 6.713  -2.140  3.955  1.00 32.81 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 5.513  -1.994  4.173  1.00 33.22 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 6.370  -0.952  1.700  1.00 36.43 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 5.546  -2.074  1.110  1.00 43.29 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 5.853  -3.258  1.395  1.00 44.06 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 4.572  -1.772  0.373  1.00 48.93 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.495  -2.944  4.732  1.00 31.43 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 6.992  -3.694  5.907  1.00 29.51 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.279  -2.765  6.854  1.00 27.14 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 6.722  -1.629  7.065  1.00 27.52 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.133  -4.397  6.649  1.00 29.79 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 8.722  -5.929  5.878  1.00 31.27 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.218  -3.242  7.444  1.00 25.13 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 4.511  -2.535  8.490  1.00 24.58 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 4.463  -3.381  9.768  1.00 22.59 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 3.640  -3.113  10.626 1.00 22.91 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 3.101  -2.082  8.057  1.00 27.98 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 3.081  -0.834  7.157  1.00 31.88 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 1.655  -0.403  6.859  1.00 36.23 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 1.174  -0.500  5.726  1.00 38.50 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 0.940  0.059   7.879  1.00 35.77 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 5.328  -4.416  9.900  1.00 21.43 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 5.484  -5.227  11.114 1.00 21.00 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 6.995  -5.410  11.374 1.00 18.52 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 7.808  -5.501  10.436 1.00 19.59 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 4.741  -6.595  11.063 1.00 25.46 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 5.409  -7.470  10.145 1.00 28.44 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 3.265  -6.466  10.665 1.00 26.59 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 7.349  -5.451  12.653 1.00 17.60 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 8.744  -5.609  13.028 1.00 16.89 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 8.909  -5.730  14.533 1.00 16.52 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 7.925  -5.963  15.225 1.00 16.67 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 10.132 -5.584  15.028 1.00 15.72 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 10.459 -5.734  16.468 1.00 15.60 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 11.333 -4.548  16.879 1.00 16.05 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 12.326 -4.276  16.189 1.00 16.14 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 11.197 -7.090  16.705 1.00 17.94 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 11.675 -7.240  18.171 1.00 19.56 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 10.289 -8.248  16.316 1.00 18.89 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 11.041 -3.915  18.021 1.00 15.80 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 11.912 -2.815  18.481 1.00 15.28 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 12.471 -3.087  19.855 1.00 15.77 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 11.858 -3.803  20.624 1.00 16.39 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 11.209 -1.423  18.461 1.00 15.33 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 10.234 -1.173  19.604 1.00 16.50 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 8.964  -1.752  19.609 1.00 17.55 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 10.538 -0.276  20.630 1.00 17.25 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 8.033  -1.466  20.615 1.00 18.22 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 9.615  0.004   21.654 1.00 18.58 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 8.367  -0.606  21.650 1.00 18.68 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 7.441  -0.369  22.661 1.00 20.77 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 13.645 -2.508  20.149 1.00 15.93 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 14.255 -2.657  21.464 1.00 17.68 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 13.800 -1.489  22.339 1.00 18.12 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 13.956 -0.303  21.963 1.00 17.08 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 15.798 -2.681  21.392 1.00 18.14 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 16.407 -2.844  22.767 1.00 20.21 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 16.199 -3.998  23.502 1.00 21.58 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 17.160 -1.827  23.343 1.00 22.60 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 16.734 -4.154  24.778 1.00 23.68 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.688 -1.960  24.628 1.00 24.46 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.477 -3.131  25.336 1.00 26.21 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.972 -3.254  26.616 1.00 29.76 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 13.278 -1.834  23.556 1.00 19.17 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 12.793 -0.846  24.534 1.00 21.55 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 13.686 -0.856  25.799 1.00 23.72 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 13.536 -1.726  26.673 1.00 24.31 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 11.324 -1.106  24.867 1.00 22.82 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 10.664 -0.098  26.243 1.00 25.31 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 14.647 0.108   25.886 1.00 24.60 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 15.580 0.137   27.002 1.00 26.78 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 14.908 0.291   28.353 1.00 27.39 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 15.374 -0.323  29.327 1.00 29.03 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 16.653 1.199   26.817 1.00 31.08 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 16.033 2.460   26.668 1.00 37.99 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 13.783 1.035   28.425 1.00 26.45 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 13.058 1.210   29.708 1.00 27.14 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 12.387 -0.069  30.257 1.00 27.71 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 11.886 -0.066  31.397 1.00 30.38 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 12.031 2.328   29.611 1.00 28.31 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 10.974 2.001   28.725 1.00 29.83 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 12.437 -1.166  29.479 1.00 25.81 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 11.923 -2.461  29.918 1.00 25.72 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 12.954 -3.599  29.720 1.00 26.60 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 12.650 -4.762  30.062 1.00 27.88 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 10.631 -2.813  29.154 1.00 26.15 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 9.455  -1.866  29.424 1.00 27.65 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 8.781  -2.160  30.750 1.00 28.68 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 7.577  -1.338  30.960 1.00 32.81 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 7.573  -0.156  31.568 1.00 34.90 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 8.709  0.374   32.015 1.00 35.08 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 6.436  0.521   31.710 1.00 35.33 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 14.161 -3.282  29.153 1.00 26.36 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 15.208 -4.243  28.774 1.00 27.52 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 14.574 -5.405  27.963 1.00 25.94 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 14.808 -6.582  28.246 1.00 26.35 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 15.982 -4.760  30.001 1.00 30.81 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 16.996 -3.761  30.536 1.00 36.72 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.805 -4.410  31.662 1.00 43.50 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 18.344 -3.422  32.592 1.00 51.10 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 18.197 -3.478  33.914 1.00 55.90 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.515 -4.476  34.475 1.00 56.10 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 18.708 -2.523  34.686 1.00 56.63 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 13.707 -5.046  26.995 1.00 23.20 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 12.974 -6.086  26.235 1.00 22.73 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 12.761 -5.660  24.791 1.00 21.07 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 12.682 -4.467  24.517 1.00 20.56 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 11.542 -6.244  26.810 1.00 25.43 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 11.395 -7.193  27.994 1.00 33.69 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 9.915  -7.261  28.376 1.00 41.23 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 9.537  -8.496  29.167 1.00 47.21 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 10.020 -8.438  30.576 1.00 49.24 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 12.555 -6.642  23.910 1.00 19.90 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 12.194 -6.341  22.528 1.00 18.74 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 10.676 -6.609  22.435 1.00 19.59 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 10.138 -7.574  23.057 1.00 20.27 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 12.935 -7.281  21.561 1.00 18.46 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 14.430 -7.133  21.571 1.00 20.52 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 15.099 -6.399  20.596 1.00 23.21 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 15.347 -7.675  22.402 1.00 21.80 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 16.386 -6.489  20.893 1.00 22.12 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 16.585 -7.228  21.973 1.00 22.81 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 9.975  -5.793  21.640 1.00 17.64 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 8.532  -5.986  21.470 1.00 17.50 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 8.177  -6.051  19.992 1.00 17.41 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 8.642  -5.221  19.207 1.00 17.70 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 7.752  -4.789  22.073 1.00 18.23 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 7.785  -4.704  23.593 1.00 20.18 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 7.047  -5.584  24.375 1.00 22.11 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 8.477  -3.688  24.237 1.00 22.21 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 7.050  -5.495  25.776 1.00 24.07 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 8.513  -3.608  25.634 1.00 23.71 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 7.791  -4.507  26.394 1.00 25.33 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 7.778  -4.382  27.772 1.00 28.57 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 7.283  -6.974  19.608 1.00 16.96 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 6.786  -6.981  18.207 1.00 17.34 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 5.689  -5.904  18.028 1.00 19.57 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 4.861  -5.733  18.934 1.00 21.63 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 6.188  -8.382  18.045 1.00 18.41 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 5.818  -8.801  19.451 1.00 19.02 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 6.654  -8.030  20.450 1.00 17.66 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 5.661  -5.196  16.892 1.00 18.93 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 4.688  -4.116  16.693 1.00 19.94 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 4.206  -4.058  15.257 1.00 19.61 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 4.943  -4.441  14.346 1.00 20.64 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 5.314  -2.710  16.985 1.00 21.61 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 5.432  -2.401  18.471 1.00 24.24 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 6.645  -2.544  16.276 1.00 21.11 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 2.982  -3.523  15.045 1.00 19.33 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 2.497  -3.139  13.724 1.00 21.40 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 2.712  -1.603  13.691 1.00 22.08 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 2.537  -0.958  14.737 1.00 24.60 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 1.003  -3.419  13.564 1.00 24.83 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 0.762  -4.815  13.487 1.00 31.61 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 3.189  -1.046  12.588 1.00 20.35 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 3.461  0.400   12.541 1.00 20.52 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 2.941  1.039   11.280 1.00 23.44 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 2.753  0.361   10.249 1.00 25.87 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 4.947  0.727   12.782 1.00 19.37 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 5.933  -0.021  11.906 1.00 18.81 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 6.451  -1.243  12.305 1.00 18.59 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 6.358  0.513   10.697 1.00 19.83 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 7.356  -1.931  11.499 1.00 19.50 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 7.278  -0.164  9.899  1.00 19.90 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 7.773  -1.386  10.302 1.00 19.56 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 2.675  2.364   11.347 1.00 23.06 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 2.126  3.073   10.205 1.00 24.06 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 3.187  3.381   9.113  1.00 23.79 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 4.385  3.214   9.348  1.00 23.61 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 1.440  4.367   10.671 1.00 26.08 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 2.393  5.261   11.240 1.00 26.76 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 2.748  3.787   7.900  1.00 24.60 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 3.708  4.180   6.846  1.00 26.44 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 4.342  5.543   7.199  1.00 27.14 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 3.711  6.326   7.896  1.00 27.92 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 3.057  4.194   5.430  1.00 30.85 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 2.890  2.751   4.875  1.00 36.64 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 2.455  2.684   3.378  1.00 43.86 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 2.254  1.221   3.032  1.00 50.41 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 1.983  0.984   1.589  1.00 55.17 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 5.591  5.815   6.767  1.00 26.44 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 6.236  7.102   7.122  1.00 27.43 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 5.404  8.306   6.689  1.00 27.83 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 4.931  8.351   5.534  1.00 27.80 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 7.578  7.065   6.382  1.00 28.78 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 7.829  5.647   6.061  1.00 29.79 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 6.466  4.984   5.919  1.00 26.70 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 5.146  9.236   7.635  1.00 28.34 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 4.297  10.397  7.350  1.00 29.87 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 4.610  11.629  8.250  1.00 28.73 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 5.488  11.554  9.132  1.00 27.14 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 2.817  9.994   7.411  1.00 34.20 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 2.397  9.703   8.733  1.00 39.04 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 3.927  12.781  7.965  1.00 28.58 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 4.048  14.053  8.680  1.00 29.94 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 3.100  13.999  9.846  1.00 32.31 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 1.873  14.031  9.633  1.00 33.87 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 3.573  15.226  7.778  1.00 30.27 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 4.588  15.896  6.911  1.00 32.01 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 3.923  17.016  6.078  1.00 33.33 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 5.702  16.494  7.741  1.00 32.63 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 3.589  13.942  11.151 1.00 31.66 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 2.890  13.871  12.496 1.00 33.49 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 3.366  14.887  13.604 1.00 35.22 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 4.569  15.259  13.640 1.00 34.12 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 3.005  12.407  13.047 1.00 34.30 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 2.359  11.358  12.144 1.00 35.68 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 2.488  12.314  14.474 1.00 34.89 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 2.829  9.961   12.401 1.00 37.94 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 2.505  15.324  14.560 1.00 36.92 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 2.763  16.324  15.630 1.00 39.83 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 3.643  16.010  16.866 1.00 40.58 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 3.391  14.995  17.420 1.00 41.39 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 1.445  16.415  16.384 1.00 41.60 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 1.128  17.820  16.816 1.00 43.68 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 0.749  18.772  15.891 1.00 46.00 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 1.266  18.191  18.138 1.00 45.10 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 0.508  20.074  16.288 1.00 47.19 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 1.016  19.491  18.536 1.00 46.15 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 0.617  20.423  17.610 1.00 46.60 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 4.501  16.946  17.339 1.00 40.56 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 5.437  16.794  18.518 1.00 41.35 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 5.567  18.138  19.247 1.00 43.06 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 6.046  19.017  18.574 1.00 42.92 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 6.818  16.272  18.074 1.00 41.36 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 7.658  15.903  19.274 1.00 41.81 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 6.630  15.035  17.202 1.00 41.19 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 5.373  18.216  20.593 1.00 44.27 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 5.165  19.501  21.333 1.00 45.45 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 6.375  20.382  21.310 1.00 45.17 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 6.427  21.226  20.442 1.00 44.78 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 4.779  19.249  22.815 1.00 49.60 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 4.645  17.786  23.172 1.00 58.69 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 3.754  16.993  22.238 1.00 70.41 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 4.059  15.813  22.026 1.00 72.53 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 2.808  17.579  21.682 1.00 74.35 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 7.178  20.244  22.323 1.00 44.74 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 8.386  21.048  22.486 1.00 45.31 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 9.229  20.308  23.501 1.00 45.82 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 8.786  19.278  23.912 1.00 46.40 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 8.078  22.437  23.045 1.00 45.55 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 10.374 20.879  23.845 1.00 45.37 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 11.284 20.262  24.845 1.00 45.28 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 12.732 20.823  24.653 1.00 46.11 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 12.942 21.603  23.732 1.00 46.40 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 11.321 18.811  24.706 1.00 45.01 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 11.868 18.454  23.438 1.00 44.43 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 13.661 20.435  25.490 1.00 45.66 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 15.007 21.058  25.384 1.00 45.52 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 15.484 20.978  23.900 1.00 43.23 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 16.428 21.724  23.536 1.00 44.05 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 16.024 20.377  26.291 1.00 50.74 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 15.649 18.958  26.741 1.00 59.62 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 14.406 18.747  27.593 1.00 69.16 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 14.504 18.829  28.848 1.00 70.43 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 13.342 18.480  27.002 1.00 72.22 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 14.736 20.280  23.017 1.00 39.89 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 15.182 19.999  21.620 1.00 37.45 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 14.278 20.694  20.517 1.00 35.23 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 14.942 21.273  19.704 1.00 36.10 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 15.445 18.483  21.454 1.00 36.54 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 15.853 17.723  22.705 1.00 36.44 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 17.148 17.738  23.184 1.00 37.20 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 14.939 16.958  23.405 1.00 37.29 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 17.515 17.016  24.308 1.00 38.60 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 15.277 16.251  24.545 1.00 38.44 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 16.572 16.285  25.008 1.00 39.90 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 16.897 15.577  26.134 1.00 42.16 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 12.932 20.644  20.486 1.00 33.24 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 12.109 21.250  19.354 1.00 32.06 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 10.764 21.903  19.749 1.00 33.71 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 10.134 21.368  20.607 1.00 34.46 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 11.660 20.186  18.355 1.00 29.27 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 12.740 19.276  17.833 1.00 26.56 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 13.019 18.072  18.457 1.00 25.81 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 13.489 19.617  16.721 1.00 25.52 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 14.016 17.235  17.987 1.00 24.63 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 14.485 18.790  16.233 1.00 24.77 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 14.744 17.585  16.859 1.00 24.29 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 15.734 16.771  16.387 1.00 22.55 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 10.247 22.981  19.102 1.00 34.30 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 8.863  23.518  19.364 1.00 35.75 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 7.845  22.767  18.475 1.00 37.11 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 8.289  22.058  17.622 1.00 37.07 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 9.047  25.019  19.090 1.00 36.42 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 10.127 25.081  18.014 1.00 36.33 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 10.976 23.836  18.169 1.00 34.05 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 6.517  22.919  18.695 1.00 37.80 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 5.524  22.109  17.947 1.00 38.16 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 5.841  22.138  16.448 1.00 36.48 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 6.036  23.239  15.918 1.00 36.29 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 4.097  22.532  18.230 1.00 38.96 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 5.836  20.954  15.826 1.00 34.79 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 6.015  20.871  14.371 1.00 33.33 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 5.539  19.511  13.878 1.00 32.48 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 5.291  18.634  14.690 1.00 32.30 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 7.469  21.110  13.972 1.00 34.00 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 8.314  19.839  13.996 1.00 33.76 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 9.521  19.802  14.906 1.00 33.44 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 10.512 18.800  14.536 1.00 32.96 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 10.786 17.715  15.255 1.00 30.36 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 11.707 16.855  14.862 1.00 25.38 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 10.116 17.483  16.364 1.00 29.74 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 5.318  19.450  12.588 1.00 31.60 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 5.067  18.132  11.965 1.00 31.66 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 6.407  17.413  11.745 1.00 28.60 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 7.334  17.997  11.107 1.00 27.59 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 4.436  18.266  10.604 1.00 34.08 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 3.041  18.847  10.626 1.00 38.48 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 1.919  18.052  10.775 1.00 41.08 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 2.852  20.213  10.524 1.00 40.76 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 0.646  18.604  10.795 1.00 43.30 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 1.594  20.782  10.544 1.00 42.52 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 0.483  19.974  10.681 1.00 44.72 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? -0.753 20.549  10.733 1.00 48.21 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 6.540  16.233  12.328 1.00 25.42 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 7.735  15.406  12.151 1.00 22.25 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 7.580  14.653  10.827 1.00 21.89 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 6.567  13.991  10.637 1.00 22.73 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 7.996  14.519  13.371 1.00 20.68 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 9.259  13.645  13.226 1.00 20.56 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 9.893  13.160  14.509 1.00 23.03 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 9.556  13.605  15.595 1.00 24.48 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 10.863 12.260  14.394 1.00 21.44 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 8.555  14.796  9.945  1.00 19.61 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 8.370  14.045  8.703  1.00 19.77 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 9.034  12.661  8.787  1.00 19.47 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 9.894  12.424  9.666  1.00 19.16 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 8.960  14.824  7.528  1.00 21.56 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 10.363 14.980  7.673  1.00 23.30 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 8.578  11.745  7.909  1.00 19.22 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 9.123  10.402  7.810  1.00 19.44 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 8.969  9.640   9.139  1.00 19.11 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 9.834  8.844   9.483  1.00 18.83 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 10.600 10.485  7.371  1.00 20.20 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 10.765 11.099  6.004  1.00 23.12 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 10.740 10.317  4.847  1.00 26.85 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 10.872 12.404  5.642  1.00 25.36 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 10.852 11.167  3.827  1.00 27.22 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 10.947 12.431  4.254  1.00 26.91 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 7.887  9.912   9.881  1.00 19.46 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 7.681  9.272   11.192 1.00 19.62 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 6.631  8.119   11.110 1.00 19.55 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 5.600  8.267   10.439 1.00 20.53 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 7.222  10.353  12.216 1.00 19.52 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 7.070  9.941   13.701 1.00 20.83 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 8.401  9.574   14.288 1.00 20.29 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 6.397  11.105  14.545 1.00 22.55 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 6.879  7.018   11.841 1.00 18.31 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 5.955  5.866   11.835 1.00 18.93 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 5.500  5.612   13.261 1.00 20.00 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 6.375  5.547   14.133 1.00 21.01 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 6.727  4.641   11.324 1.00 19.29 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 7.190  4.813   9.863  1.00 21.77 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 8.316  3.505   9.353  1.00 25.13 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 9.720  3.767   10.480 1.00 22.19 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 4.170  5.435   13.531 1.00 19.34 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 3.719  5.195   14.904 1.00 20.50 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 3.271  3.760   15.103 1.00 21.00 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 2.690  3.152   14.189 1.00 22.20 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 2.479  6.067   15.226 1.00 22.45 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 2.654  7.563   15.272 1.00 26.33 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 1.343  8.224   15.775 1.00 27.90 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 3.792  7.962   16.177 1.00 27.23 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 3.426  3.285   16.329 1.00 20.01 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 2.960  1.959   16.738 1.00 21.51 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 2.391  2.049   18.163 1.00 22.55 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 2.737  2.967   18.909 1.00 23.10 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 4.127  0.993   16.751 1.00 21.96 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 1.506  1.124   18.533 1.00 23.02 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 1.014  1.043   19.902 1.00 24.84 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 2.089  0.255   20.708 1.00 27.15 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 2.376  -0.902  20.404 1.00 28.03 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? -0.366 0.349   19.980 1.00 25.77 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? -0.776 0.137   21.424 1.00 26.90 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? -1.427 1.158   19.244 1.00 26.01 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 2.698  0.853   21.657 1.00 27.04 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 3.743  0.087   22.306 1.00 27.18 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 4.360  0.965   23.339 1.00 27.20 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 4.375  2.181   23.121 1.00 28.43 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 4.859  0.350   24.399 1.00 25.77 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 5.565  1.099   25.461 1.00 25.64 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 6.850  1.881   25.064 1.00 24.51 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 7.666  1.382   24.330 1.00 23.14 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 5.858  0.198   26.683 1.00 26.30 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 6.569  0.955   27.749 1.00 28.77 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 5.941  1.923   28.491 1.00 32.30 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 7.860  0.970   28.132 1.00 30.19 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 6.804  2.470   29.317 1.00 32.93 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 7.980  1.902   29.124 1.00 32.75 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 6.977  3.088   25.619 1.00 24.56 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 8.135  3.998   25.470 1.00 25.91 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 8.049  5.147   26.500 1.00 28.71 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 6.986  5.560   26.782 1.00 30.27 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 8.163  4.730   24.091 1.00 26.92 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 7.039  5.560   23.865 1.00 28.40 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 9.189  5.602   26.966 1.00 29.31 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 9.193  6.919   27.689 1.00 31.48 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 10.640 7.534   27.523 1.00 33.34 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 11.479 6.967   26.848 1.00 33.86 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 8.490  6.810   29.049 1.00 34.17 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 7.277  7.721   29.212 1.00 38.70 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 5.915  7.246   28.724 1.00 43.56 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 5.124  8.075   28.231 1.00 44.41 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 5.628  6.064   28.858 1.00 45.66 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 10.936 8.770   27.964 1.00 34.75 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 12.247 9.378   27.696 1.00 34.67 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 13.392 8.414   27.949 1.00 33.14 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 13.142 7.706   28.908 1.00 33.28 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 12.177 10.577  28.658 1.00 35.99 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 10.726 10.967  28.707 1.00 36.93 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 9.994  9.646   28.659 1.00 34.77 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 14.548 8.470   27.261 1.00 31.35 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 15.689 7.522   27.356 1.00 30.55 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 15.629 6.402   26.289 1.00 28.29 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 16.676 5.853   25.961 1.00 28.88 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 14.433 6.199   25.747 1.00 26.12 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 14.155 5.123   24.761 1.00 24.26 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 14.522 5.537   23.339 1.00 22.79 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 14.605 4.624   22.484 1.00 22.29 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 12.699 4.718   24.798 1.00 25.18 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 12.367 3.795   25.964 1.00 27.14 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 13.295 3.125   26.441 1.00 26.35 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 11.183 3.760   26.369 1.00 28.16 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 14.817 6.814   23.175 1.00 22.82 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 15.272 7.294   21.816 1.00 22.11 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 16.548 6.521   21.371 1.00 22.01 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.454 6.340   22.203 1.00 22.20 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 15.359 8.829   21.825 1.00 22.57 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 13.714 9.555   22.092 1.00 26.19 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 16.619 6.063   20.103 1.00 20.84 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.806 5.369   19.619 1.00 21.63 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.665 3.847   19.562 1.00 21.78 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 18.474 3.163   18.919 1.00 21.49 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 16.632 3.300   20.215 1.00 20.70 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 16.348 1.864   20.119 1.00 18.95 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 15.985 1.517   18.671 1.00 18.43 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 15.245 2.255   18.023 1.00 18.32 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 16.548 0.429   18.155 1.00 17.72 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 16.341 0.047   16.770 1.00 17.21 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 15.032 -0.726  16.554 1.00 15.93 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 14.679 -1.619  17.375 1.00 16.77 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.607 -0.736  16.276 1.00 19.55 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 18.792 0.263   15.986 1.00 21.09 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.318 -1.605  15.067 1.00 20.22 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 20.188 -0.464  15.793 1.00 23.62 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 14.363 -0.419  15.404 1.00 14.73 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 13.186 -1.153  14.906 1.00 15.28 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 13.702 -1.964  13.707 1.00 16.42 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 14.362 -1.405  12.814 1.00 16.95 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 12.118 -0.179  14.388 1.00 15.82 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 10.910 -0.810  13.672 1.00 17.02 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 10.169 -1.779  14.582 1.00 17.69 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 9.926  0.311   13.181 1.00 18.09 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 13.416 -3.281  13.690 1.00 16.64 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 13.921 -4.139  12.625 1.00 18.12 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 12.790 -5.013  12.089 1.00 19.10 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 11.984 -5.498  12.861 1.00 18.76 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 14.926 -5.157  13.219 1.00 21.40 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 16.256 -4.630  13.686 1.00 28.33 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.094 -5.818  14.153 1.00 32.42 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.634 -6.497  12.973 1.00 37.26 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 18.819 -6.217  12.432 1.00 38.90 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 19.202 -6.819  11.318 1.00 38.29 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 19.637 -5.351  13.019 1.00 39.74 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 12.847 -5.337  10.801 1.00 20.18 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 11.920 -6.314  10.176 1.00 22.83 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 12.801 -7.475  9.623  1.00 26.35 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 14.009 -7.485  9.861  1.00 25.22 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 11.122 -5.635  9.065  1.00 23.14 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 12.148 -5.058  7.682  1.00 24.14 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 12.213 -8.466  8.905  1.00 29.92 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 13.009 -9.561  8.339  1.00 32.68 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 14.096 -9.057  7.348  1.00 33.53 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 15.090 -9.762  7.111  1.00 35.76 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 12.085 -10.565 7.629  1.00 37.24 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 11.303 -9.948  6.463  1.00 43.23 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 10.344 -10.937 5.845  1.00 50.48 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 9.127  -10.694 5.777  1.00 52.31 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 10.880 -12.062 5.361  1.00 51.44 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 13.918 -7.858  6.773  1.00 31.36 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 14.875 -7.335  5.790  1.00 30.58 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 16.049 -6.549  6.413  1.00 29.51 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.019 -6.244  5.706  1.00 30.68 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 14.163 -6.499  4.695  1.00 31.90 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 12.984 -7.191  4.046  1.00 35.60 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 11.682 -6.824  4.331  1.00 37.33 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 12.956 -8.140  3.078  1.00 38.09 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 10.901 -7.608  3.606  1.00 39.03 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 11.618 -8.422  2.829  1.00 39.26 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 15.963 -6.211  7.707  1.00 26.66 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.038 -5.471  8.356  1.00 25.26 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 16.553 -4.250  9.136  1.00 21.95 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 15.409 -4.214  9.554  1.00 22.06 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.413 -3.268  9.359  1.00 20.94 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.075 -2.048  10.111 1.00 20.51 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 16.055 -1.159  9.384  1.00 20.07 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 16.299 -0.755  8.226  1.00 20.62 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 18.351 -1.231  10.502 1.00 21.41 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.958 0.088   11.166 1.00 20.92 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 19.244 -2.042  11.463 1.00 22.00 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 14.938 -0.831  10.070 1.00 19.27 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 13.872 0.014   9.529  1.00 18.83 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 14.006 1.486   9.993  1.00 18.08 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 13.825 2.422   9.208  1.00 18.35 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 12.472 -0.555  9.928  1.00 20.85 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 11.353 0.428   9.594  1.00 21.56 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 12.210 -1.917  9.283  1.00 21.29 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 14.265 1.655   11.285 1.00 16.63 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 14.362 3.003   11.846 1.00 16.73 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 14.767 3.019   13.305 1.00 16.47 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 15.184 1.991   13.840 1.00 16.13 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 14.689 4.204   13.947 1.00 16.10 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 15.077 4.265   15.360 1.00 16.55 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 13.980 4.985   16.158 1.00 16.04 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 13.321 5.883   15.643 1.00 15.43 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 16.442 4.984   15.532 1.00 18.50 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 16.491 6.304   14.752 1.00 20.08 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.660 4.084   15.218 1.00 20.73 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.789 7.154   15.222 1.00 21.93 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 13.803 4.609   17.439 1.00 15.30 ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 12.822 5.306   18.282 1.00 14.86 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 13.179 6.825   18.344 1.00 16.07 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 14.341 7.186   18.591 1.00 15.93 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 12.781 4.723   19.719 1.00 16.65 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 11.868 5.560   20.599 1.00 18.62 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 12.307 3.261   19.712 1.00 17.41 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 12.215 7.721   18.165 1.00 16.89 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 12.502 9.189   18.115 1.00 18.25 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 11.585 9.956   19.085 1.00 20.75 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 12.096 10.913  19.682 1.00 22.91 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 12.341 9.722   16.718 1.00 19.41 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 12.476 11.122  16.623 1.00 20.20 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 10.296 9.544   19.180 1.00 22.12 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 9.262  10.124  20.078 1.00 24.94 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 8.236  9.030   20.475 1.00 26.25 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 8.321  7.908   20.048 1.00 25.29 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 8.513  11.312  19.427 1.00 27.78 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 7.843  12.124  20.385 1.00 29.47 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 7.452  10.843  18.452 1.00 28.34 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 7.203  9.439   21.214 1.00 28.14 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 6.145  8.528   21.681 1.00 31.01 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 5.323  9.280   22.706 1.00 34.16 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 5.705  10.408  23.108 1.00 34.94 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 4.284  8.684   23.195 1.00 36.46 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 3.492  9.528   24.107 1.00 39.48 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 2.204  8.872   24.407 1.00 41.57 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 1.669  8.206   23.532 1.00 41.59 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 1.721  9.069   25.630 1.00 42.76 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 0.490  8.310   25.998 1.00 43.92 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 0.398  6.828   25.524 1.00 42.54 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? -0.709 6.395   25.069 1.00 44.32 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? -0.771 8.992   25.434 1.00 46.84 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? -0.808 10.493  25.585 1.00 53.37 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? -0.657 10.990  26.691 1.00 55.89 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? -1.015 11.212  24.489 1.00 54.38 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 1.471  6.029   25.561 1.00 39.11 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 1.260  4.648   25.124 1.00 36.62 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 1.578  4.378   23.668 1.00 33.64 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 1.369  3.240   23.259 1.00 33.46 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 2.080  5.379   22.948 1.00 31.56 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 2.387  5.248   21.514 1.00 29.38 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 3.878  5.459   21.399 1.00 28.02 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 4.397  6.202   22.193 1.00 29.91 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 1.698  6.305   20.656 1.00 29.12 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 0.188  6.142   20.477 1.00 31.69 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? -0.456 7.504   20.298 1.00 32.92 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? -0.113 5.248   19.279 1.00 32.30 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 4.449  4.877   20.355 1.00 23.59 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 5.889  5.065   20.114 1.00 21.71 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 6.096  5.528   18.659 1.00 20.56 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 5.407  5.031   17.779 1.00 21.29 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 6.702  3.793   20.448 1.00 21.35 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 6.188  2.549   19.740 1.00 21.91 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 8.191  3.994   20.210 1.00 21.49 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 7.011  6.486   18.505 1.00 19.04 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 7.337  7.015   17.171 1.00 19.46 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 8.741  6.656   16.693 1.00 19.56 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 9.706  6.838   17.397 1.00 20.24 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 8.802  6.155   15.457 1.00 17.62 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 10.091 5.713   14.865 1.00 16.61 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 10.466 6.605   13.652 1.00 16.21 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 9.608  6.749   12.800 1.00 17.11 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 10.061 4.246   14.426 1.00 16.18 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 9.555  3.242   15.434 1.00 16.93 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 10.404 2.698   16.381 1.00 17.01 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 8.232  2.824   15.423 1.00 17.97 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 9.931  1.778   17.305 1.00 18.06 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 7.770  1.893   16.337 1.00 18.61 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 8.617  1.376   17.282 1.00 18.06 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 11.720 7.098   13.604 1.00 14.99 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 12.193 7.847   12.459 1.00 14.74 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 12.634 6.794   11.422 1.00 15.51 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 13.591 6.030   11.667 1.00 15.65 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 13.379 8.719   12.882 1.00 14.28 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 11.994 6.802   10.224 1.00 15.44 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 12.343 5.855   9.166  1.00 17.21 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 13.712 6.156   8.574  1.00 18.64 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 14.097 7.345   8.455  1.00 18.75 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 11.308 5.957   8.026  1.00 19.62 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 11.474 4.909   6.940  1.00 24.30 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 11.670 3.739   7.281  1.00 23.88 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 11.441 5.284   5.732  1.00 26.36 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 14.467 5.083   8.167  1.00 18.06 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 15.740 5.315   7.474  1.00 18.21 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 15.795 4.561   6.112  1.00 19.67 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 16.819 4.610   5.431  1.00 22.13 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 16.995 4.982   8.318  1.00 18.74 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.045 5.803   9.625  1.00 17.83 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.068 3.481   8.603  1.00 18.30 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 14.736 3.797   5.756  1.00 18.81 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 14.709 2.951   4.563  1.00 19.62 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 14.823 3.722   3.248  1.00 23.26 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 15.244 3.134   2.256  1.00 25.20 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 13.445 2.070   4.545  1.00 20.39 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 13.290 1.194   5.778  1.00 22.59 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 11.963 0.455   5.756  1.00 20.15 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 10.828 1.307   6.138  1.00 22.94 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 9.581  0.879   6.281  1.00 24.79 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 9.266  -0.377  5.986  1.00 23.99 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 8.632  1.706   6.724  1.00 25.13 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 14.470 5.009   3.236  1.00 23.32 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 14.568 5.800   1.999  1.00 24.82 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 15.987 6.366   1.760  1.00 26.65 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 16.234 6.939   0.682  1.00 28.10 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 13.554 6.957   2.021  1.00 26.31 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 13.854 7.981   3.101  1.00 28.16 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 14.180 7.555   4.251  1.00 27.36 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 13.751 9.217   2.808  1.00 27.01 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 16.897 6.290   2.761  1.00 25.45 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 18.238 6.881   2.633  1.00 24.94 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 19.127 5.890   1.924  1.00 27.16 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 19.926 5.192   2.560  1.00 27.51 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 18.805 7.252   4.024  1.00 23.78 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 17.887 8.169   4.859  1.00 22.92 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 18.434 8.341   6.281  1.00 22.42 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.683 9.552   4.196  1.00 23.08 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 18.928 5.769   0.586  1.00 28.47 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 19.621 4.754   -0.205 1.00 31.17 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 21.132 4.925   -0.198 1.00 32.82 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 21.852 3.927   -0.322 1.00 33.97 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 19.074 4.701   -1.649 1.00 32.08 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 17.547 4.646   -1.819 1.00 33.96 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.181 4.402   -3.297 1.00 35.26 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 16.896 3.521   -0.965 1.00 34.37 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 21.621 6.177   -0.011 1.00 32.80 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 23.039 6.482   -0.003 1.00 33.14 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 23.802 5.900   1.179  1.00 34.89 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 25.024 5.831   1.107  1.00 35.91 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 23.283 7.993   -0.128 1.00 32.34 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 22.528 8.807   0.881  1.00 30.71 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 21.283 9.346   0.743  1.00 30.90 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 22.978 9.161   2.193  1.00 29.90 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 20.944 10.042  1.880  1.00 30.86 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 21.968 9.941   2.786  1.00 30.32 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 24.153 8.915   2.914  1.00 30.28 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 22.092 10.465  4.072  1.00 30.43 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 24.280 9.447   4.180  1.00 31.02 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 23.265 10.230  4.738  1.00 30.51 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 23.117 5.427   2.239  1.00 35.45 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 23.804 4.813   3.373  1.00 36.34 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 24.598 3.567   2.957  1.00 41.06 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 25.593 3.243   3.605  1.00 40.94 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 22.790 4.416   4.448  1.00 34.59 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 22.123 5.559   5.188  1.00 33.82 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 21.099 5.017   6.174  1.00 33.64 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 23.158 6.403   5.933  1.00 33.66 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 24.135 2.859   1.898  1.00 44.77 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 24.749 1.632   1.381  1.00 49.28 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 25.887 1.882   0.415  1.00 53.83 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 26.705 0.989   0.219  1.00 54.74 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 23.705 0.800   0.637  1.00 51.58 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 22.601 0.286   1.512  1.00 56.77 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 22.843 0.099   2.721  1.00 58.09 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 21.487 0.078   0.993  1.00 59.64 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 25.905 3.043   -0.260 1.00 56.35 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 26.955 3.335   -1.237 1.00 59.23 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 27.880 4.458   -0.786 1.00 60.80 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 28.871 4.737   -1.468 1.00 62.12 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 26.353 3.654   -2.616 1.00 62.46 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 25.258 4.707   -2.579 1.00 68.31 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 24.047 4.385   -3.434 1.00 76.38 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 23.276 5.322   -3.747 1.00 78.31 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 23.867 3.199   -3.793 1.00 79.32 ? 145 GLU   A OE2 1 
HETATM 1078 C  C4  . A1B3R B 2 .   ? 7.340  10.308  26.438 1.00 33.21 ? 201 A1B3R A C4  1 
HETATM 1079 C  C5  . A1B3R B 2 .   ? 8.298  11.277  26.190 1.00 33.41 ? 201 A1B3R A C5  1 
HETATM 1080 C  C6  . A1B3R B 2 .   ? 9.328  11.058  25.287 1.00 32.64 ? 201 A1B3R A C6  1 
HETATM 1081 C  C7  . A1B3R B 2 .   ? 10.302 12.177  24.973 1.00 32.87 ? 201 A1B3R A C7  1 
HETATM 1082 C  C8  . A1B3R B 2 .   ? 9.966  12.884  23.672 1.00 31.79 ? 201 A1B3R A C8  1 
HETATM 1083 C  C10 . A1B3R B 2 .   ? 13.135 14.247  22.713 1.00 29.46 ? 201 A1B3R A C10 1 
HETATM 1084 C  C13 . A1B3R B 2 .   ? 10.978 14.670  19.510 1.00 27.81 ? 201 A1B3R A C13 1 
HETATM 1085 C  C15 . A1B3R B 2 .   ? 10.357 14.486  21.947 1.00 29.41 ? 201 A1B3R A C15 1 
HETATM 1086 O  O   . A1B3R B 2 .   ? 8.974  12.545  23.068 1.00 31.67 ? 201 A1B3R A O   1 
HETATM 1087 N  N   . A1B3R B 2 .   ? 10.765 13.873  23.208 1.00 30.03 ? 201 A1B3R A N   1 
HETATM 1088 C  C12 . A1B3R B 2 .   ? 11.395 14.157  20.885 1.00 28.43 ? 201 A1B3R A C12 1 
HETATM 1089 C  C14 . A1B3R B 2 .   ? 12.013 14.319  18.466 1.00 26.23 ? 201 A1B3R A C14 1 
HETATM 1090 O  O1  . A1B3R B 2 .   ? 11.666 14.863  17.186 1.00 25.50 ? 201 A1B3R A O1  1 
HETATM 1091 C  C11 . A1B3R B 2 .   ? 12.737 14.724  21.320 1.00 28.81 ? 201 A1B3R A C11 1 
HETATM 1092 C  C9  . A1B3R B 2 .   ? 12.022 14.428  23.705 1.00 29.74 ? 201 A1B3R A C9  1 
HETATM 1093 C  C1  . A1B3R B 2 .   ? 9.383  9.806   24.661 1.00 31.25 ? 201 A1B3R A C1  1 
HETATM 1094 S  S   . A1B3R B 2 .   ? 10.693 9.595   23.510 1.00 29.45 ? 201 A1B3R A S   1 
HETATM 1095 C  C   . A1B3R B 2 .   ? 10.660 7.781   23.160 1.00 29.08 ? 201 A1B3R A C   1 
HETATM 1096 C  C3  . A1B3R B 2 .   ? 7.405  9.092   25.815 1.00 32.53 ? 201 A1B3R A C3  1 
HETATM 1097 C  C2  . A1B3R B 2 .   ? 8.430  8.827   24.928 1.00 32.08 ? 201 A1B3R A C2  1 
HETATM 1098 ZN ZN  . ZN    C 3 .   ? 10.849 -5.216  5.614  1.00 26.61 2 202 ZN    A ZN  1 
HETATM 1099 O  O   . HOH   D 4 .   ? 5.351  6.212   31.128 1.00 43.75 ? 301 HOH   A O   1 
HETATM 1100 O  O   . HOH   D 4 .   ? 20.315 22.037  7.911  1.00 37.36 ? 302 HOH   A O   1 
HETATM 1101 O  O   . HOH   D 4 .   ? 35.621 14.900  17.564 1.00 50.10 ? 303 HOH   A O   1 
HETATM 1102 O  O   . HOH   D 4 .   ? 3.121  7.495   9.879  1.00 40.32 ? 304 HOH   A O   1 
HETATM 1103 O  O   . HOH   D 4 .   ? 22.192 -5.027  12.461 1.00 48.75 ? 305 HOH   A O   1 
HETATM 1104 O  O   . HOH   D 4 .   ? 4.189  6.818   26.245 1.00 30.00 ? 306 HOH   A O   1 
HETATM 1105 O  O   . HOH   D 4 .   ? 8.560  19.077  18.207 1.00 34.09 ? 307 HOH   A O   1 
HETATM 1106 O  O   . HOH   D 4 .   ? 18.305 22.521  22.003 1.00 43.96 ? 308 HOH   A O   1 
HETATM 1107 O  O   . HOH   D 4 .   ? 23.296 17.584  19.697 1.00 44.71 ? 309 HOH   A O   1 
HETATM 1108 O  O   . HOH   D 4 .   ? 11.075 17.247  26.835 1.00 47.25 ? 310 HOH   A O   1 
HETATM 1109 O  O   . HOH   D 4 .   ? 5.399  -2.179  24.541 1.00 28.05 ? 311 HOH   A O   1 
HETATM 1110 O  O   . HOH   D 4 .   ? 1.009  -3.103  20.294 1.00 40.75 ? 312 HOH   A O   1 
HETATM 1111 O  O   . HOH   D 4 .   ? 22.718 -1.974  4.296  1.00 38.39 ? 313 HOH   A O   1 
HETATM 1112 O  O   . HOH   D 4 .   ? 10.760 7.573   4.681  1.00 29.25 ? 314 HOH   A O   1 
HETATM 1113 O  O   . HOH   D 4 .   ? 8.024  -4.554  0.727  1.00 28.94 ? 315 HOH   A O   1 
HETATM 1114 O  O   . HOH   D 4 .   ? 3.895  -5.429  21.352 1.00 38.98 ? 316 HOH   A O   1 
HETATM 1115 O  O   . HOH   D 4 .   ? 2.672  14.680  20.083 1.00 38.67 ? 317 HOH   A O   1 
HETATM 1116 O  O   . HOH   D 4 .   ? 23.755 21.256  7.985  1.00 29.64 ? 318 HOH   A O   1 
HETATM 1117 O  O   . HOH   D 4 .   ? 10.350 4.228   3.553  1.00 24.42 ? 319 HOH   A O   1 
HETATM 1118 O  O   . HOH   D 4 .   ? 12.560 16.282  5.310  1.00 57.58 ? 320 HOH   A O   1 
HETATM 1119 O  O   . HOH   D 4 .   ? 10.958 -5.757  31.873 1.00 40.46 ? 321 HOH   A O   1 
HETATM 1120 O  O   . HOH   D 4 .   ? 31.025 19.975  10.767 1.00 42.56 ? 322 HOH   A O   1 
HETATM 1121 O  O   . HOH   D 4 .   ? 8.916  1.953   2.951  1.00 31.95 ? 323 HOH   A O   1 
HETATM 1122 O  O   . HOH   D 4 .   ? 20.255 8.254   19.094 1.00 21.75 ? 324 HOH   A O   1 
HETATM 1123 O  O   . HOH   D 4 .   ? -0.259 15.409  8.707  1.00 55.65 ? 325 HOH   A O   1 
HETATM 1124 O  O   . HOH   D 4 .   ? 0.485  -0.844  16.501 1.00 22.81 ? 326 HOH   A O   1 
HETATM 1125 O  O   . HOH   D 4 .   ? 18.404 18.584  5.643  1.00 44.64 ? 327 HOH   A O   1 
HETATM 1126 O  O   . HOH   D 4 .   ? 16.491 12.888  26.350 1.00 42.05 ? 328 HOH   A O   1 
HETATM 1127 O  O   . HOH   D 4 .   ? 17.979 20.581  9.385  1.00 24.79 ? 329 HOH   A O   1 
HETATM 1128 O  O   . HOH   D 4 .   ? 19.245 -1.058  27.698 1.00 42.15 ? 330 HOH   A O   1 
HETATM 1129 O  O   . HOH   D 4 .   ? 17.744 -7.429  3.311  1.00 43.06 ? 331 HOH   A O   1 
HETATM 1130 O  O   . HOH   D 4 .   ? 31.284 19.946  16.876 1.00 34.78 ? 332 HOH   A O   1 
HETATM 1131 O  O   . HOH   D 4 .   ? 14.744 -5.161  17.231 1.00 26.95 ? 333 HOH   A O   1 
HETATM 1132 O  O   . HOH   D 4 .   ? 21.656 18.474  18.016 1.00 38.28 ? 334 HOH   A O   1 
HETATM 1133 O  O   . HOH   D 4 .   ? 14.909 1.917   23.380 1.00 20.65 ? 335 HOH   A O   1 
HETATM 1134 O  O   . HOH   D 4 .   ? 27.760 15.473  2.808  1.00 43.42 ? 336 HOH   A O   1 
HETATM 1135 O  O   . HOH   D 4 .   ? 11.480 10.977  11.476 1.00 19.11 ? 337 HOH   A O   1 
HETATM 1136 O  O   . HOH   D 4 .   ? 18.013 1.850   23.241 1.00 28.64 ? 338 HOH   A O   1 
HETATM 1137 O  O   . HOH   D 4 .   ? 0.640  0.762   24.375 1.00 37.68 ? 339 HOH   A O   1 
HETATM 1138 O  O   . HOH   D 4 .   ? 11.439 1.516   33.685 1.00 24.53 ? 340 HOH   A O   1 
HETATM 1139 O  O   . HOH   D 4 .   ? 6.706  -6.468  29.335 1.00 35.85 ? 341 HOH   A O   1 
HETATM 1140 O  O   . HOH   D 4 .   ? 18.070 18.288  17.173 1.00 21.01 ? 342 HOH   A O   1 
HETATM 1141 O  O   . HOH   D 4 .   ? 2.287  10.148  21.540 1.00 53.07 ? 343 HOH   A O   1 
HETATM 1142 O  O   . HOH   D 4 .   ? 13.187 9.849   9.471  1.00 16.67 ? 344 HOH   A O   1 
HETATM 1143 O  O   . HOH   D 4 .   ? 30.258 10.448  19.612 1.00 38.71 ? 345 HOH   A O   1 
HETATM 1144 O  O   . HOH   D 4 .   ? 19.025 8.395   25.923 1.00 41.37 ? 346 HOH   A O   1 
HETATM 1145 O  O   . HOH   D 4 .   ? 12.328 20.706  12.929 1.00 28.84 ? 347 HOH   A O   1 
HETATM 1146 O  O   . HOH   D 4 .   ? 14.864 13.785  3.802  1.00 34.40 ? 348 HOH   A O   1 
HETATM 1147 O  O   . HOH   D 4 .   ? 15.364 11.667  24.322 1.00 27.06 ? 349 HOH   A O   1 
HETATM 1148 O  O   . HOH   D 4 .   ? 7.040  2.960   33.125 1.00 28.45 ? 350 HOH   A O   1 
HETATM 1149 O  O   . HOH   D 4 .   ? 18.803 11.977  1.758  1.00 38.32 ? 351 HOH   A O   1 
HETATM 1150 O  O   . HOH   D 4 .   ? 6.819  12.256  5.667  1.00 27.71 ? 352 HOH   A O   1 
HETATM 1151 O  O   . HOH   D 4 .   ? 0.305  3.018   6.531  1.00 45.51 ? 353 HOH   A O   1 
HETATM 1152 O  O   . HOH   D 4 .   ? 4.211  -5.860  6.676  1.00 38.38 ? 354 HOH   A O   1 
HETATM 1153 O  O   . HOH   D 4 .   ? 28.753 -2.703  12.883 1.00 37.63 ? 355 HOH   A O   1 
HETATM 1154 O  O   . HOH   D 4 .   ? 21.892 -6.245  10.350 1.00 36.93 ? 356 HOH   A O   1 
HETATM 1155 O  O   . HOH   D 4 .   ? 30.349 4.191   3.740  1.00 59.65 ? 357 HOH   A O   1 
HETATM 1156 O  O   . HOH   D 4 .   ? 18.112 0.094   30.247 1.00 42.41 ? 358 HOH   A O   1 
HETATM 1157 O  O   . HOH   D 4 .   ? 1.709  -3.125  17.644 1.00 28.29 ? 359 HOH   A O   1 
HETATM 1158 O  O   . HOH   D 4 .   ? 8.609  -8.076  9.272  1.00 40.85 ? 360 HOH   A O   1 
HETATM 1159 O  O   . HOH   D 4 .   ? 7.608  25.331  14.536 1.00 49.90 ? 361 HOH   A O   1 
HETATM 1160 O  O   . HOH   D 4 .   ? 15.946 -11.930 5.268  1.00 50.14 ? 362 HOH   A O   1 
HETATM 1161 O  O   . HOH   D 4 .   ? 14.377 20.213  7.937  1.00 30.00 ? 363 HOH   A O   1 
HETATM 1162 O  O   . HOH   D 4 .   ? 19.785 23.048  15.527 1.00 30.38 ? 364 HOH   A O   1 
HETATM 1163 O  O   . HOH   D 4 .   ? 1.848  12.814  5.795  1.00 36.76 ? 365 HOH   A O   1 
HETATM 1164 O  O   . HOH   D 4 .   ? 24.874 6.776   20.598 1.00 52.97 ? 366 HOH   A O   1 
HETATM 1165 O  O   . HOH   D 4 .   ? 22.603 18.280  6.007  1.00 26.96 ? 367 HOH   A O   1 
HETATM 1166 O  O   . HOH   D 4 .   ? 5.639  1.382   7.264  1.00 32.54 ? 368 HOH   A O   1 
HETATM 1167 O  O   . HOH   D 4 .   ? 8.941  20.499  10.359 1.00 44.24 ? 369 HOH   A O   1 
HETATM 1168 O  O   . HOH   D 4 .   ? 15.745 -5.266  1.735  1.00 36.58 ? 370 HOH   A O   1 
HETATM 1169 O  O   . HOH   D 4 .   ? 5.043  -2.116  29.373 1.00 46.37 ? 371 HOH   A O   1 
HETATM 1170 O  O   . HOH   D 4 .   ? 16.175 23.187  14.702 1.00 45.94 ? 372 HOH   A O   1 
HETATM 1171 O  O   . HOH   D 4 .   ? 23.935 1.735   19.921 1.00 37.94 ? 373 HOH   A O   1 
HETATM 1172 O  O   . HOH   D 4 .   ? 31.581 18.088  8.656  1.00 43.64 ? 374 HOH   A O   1 
HETATM 1173 O  O   . HOH   D 4 .   ? 22.260 8.133   21.195 1.00 30.73 ? 375 HOH   A O   1 
HETATM 1174 O  O   . HOH   D 4 .   ? 11.945 -8.662  13.140 1.00 38.89 ? 376 HOH   A O   1 
HETATM 1175 O  O   . HOH   D 4 .   ? -1.753 -4.957  15.492 1.00 52.44 ? 377 HOH   A O   1 
HETATM 1176 O  O   . HOH   D 4 .   ? 13.480 -6.783  32.441 1.00 56.21 ? 378 HOH   A O   1 
HETATM 1177 O  O   . HOH   D 4 .   ? 25.980 3.705   20.316 1.00 47.65 ? 379 HOH   A O   1 
HETATM 1178 O  O   . HOH   D 4 .   ? 7.096  -5.891  2.853  1.00 34.22 ? 380 HOH   A O   1 
HETATM 1179 O  O   . HOH   D 4 .   ? 2.804  2.506   27.757 1.00 39.12 ? 381 HOH   A O   1 
HETATM 1180 O  O   . HOH   D 4 .   ? 6.195  22.417  11.326 1.00 38.29 ? 382 HOH   A O   1 
HETATM 1181 O  O   . HOH   D 4 .   ? 7.277  16.303  24.401 1.00 54.45 ? 383 HOH   A O   1 
HETATM 1182 O  O   . HOH   D 4 .   ? 16.945 22.152  17.071 1.00 41.05 ? 384 HOH   A O   1 
HETATM 1183 O  O   . HOH   D 4 .   ? 19.291 -0.706  20.025 1.00 30.00 ? 385 HOH   A O   1 
HETATM 1184 O  O   . HOH   D 4 .   ? 8.891  22.361  26.747 1.00 43.15 ? 386 HOH   A O   1 
HETATM 1185 O  O   . HOH   D 4 .   ? 9.290  17.868  20.515 1.00 36.49 ? 387 HOH   A O   1 
HETATM 1186 O  O   . HOH   D 4 .   ? 21.031 21.276  17.832 1.00 36.30 ? 388 HOH   A O   1 
HETATM 1187 O  O   . HOH   D 4 .   ? 0.257  -4.139  9.866  1.00 47.45 ? 389 HOH   A O   1 
HETATM 1188 O  O   . HOH   D 4 .   ? 11.647 3.750   1.277  1.00 35.77 ? 390 HOH   A O   1 
HETATM 1189 O  O   . HOH   D 4 .   ? 6.643  -9.273  14.237 1.00 39.93 ? 391 HOH   A O   1 
HETATM 1190 O  O   . HOH   D 4 .   ? 15.517 -10.203 11.842 1.00 45.68 ? 392 HOH   A O   1 
HETATM 1191 O  O   . HOH   D 4 .   ? 2.012  0.558   26.767 1.00 40.47 ? 393 HOH   A O   1 
HETATM 1192 O  O   . HOH   D 4 .   ? 4.023  11.956  19.505 1.00 54.85 ? 394 HOH   A O   1 
HETATM 1193 O  O   . HOH   D 4 .   ? 26.784 -2.478  15.052 1.00 35.76 ? 395 HOH   A O   1 
HETATM 1194 O  O   . HOH   D 4 .   ? 8.819  6.375   2.786  1.00 43.79 ? 396 HOH   A O   1 
HETATM 1195 O  O   . HOH   D 4 .   ? 0.798  -2.758  23.732 1.00 42.21 ? 397 HOH   A O   1 
HETATM 1196 O  O   . HOH   D 4 .   ? 33.059 21.314  12.297 1.00 39.19 ? 398 HOH   A O   1 
HETATM 1197 O  O   . HOH   D 4 .   ? 11.778 22.753  14.485 1.00 36.92 ? 399 HOH   A O   1 
HETATM 1198 O  O   . HOH   D 4 .   ? 9.167  -9.479  12.847 1.00 46.48 ? 400 HOH   A O   1 
HETATM 1199 O  O   . HOH   D 4 .   ? 23.029 -2.855  17.233 1.00 44.46 ? 401 HOH   A O   1 
HETATM 1200 O  O   . HOH   D 4 .   ? 18.604 -3.571  18.666 1.00 37.62 ? 402 HOH   A O   1 
HETATM 1201 O  O   . HOH   D 4 .   ? 9.897  24.306  13.412 1.00 40.47 ? 403 HOH   A O   1 
HETATM 1202 O  O   . HOH   D 4 .   ? 29.649 21.753  9.292  1.00 43.98 ? 404 HOH   A O   1 
HETATM 1203 O  O   . HOH   D 4 .   ? 9.812  14.331  27.874 1.00 56.60 ? 405 HOH   A O   1 
HETATM 1204 O  O   . HOH   D 4 .   ? 4.668  13.236  27.665 1.00 30.00 ? 406 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   ? 0.6016 0.2886 0.3711 -0.0603 -0.2111 0.0167  7   SER   A N   
2    C CA  . SER   A 1   ? 0.5745 0.2952 0.4115 -0.0606 -0.2267 0.0272  7   SER   A CA  
3    C C   . SER   A 1   ? 0.5129 0.2855 0.4188 -0.0492 -0.2129 0.0292  7   SER   A C   
4    O O   . SER   A 1   ? 0.5168 0.2954 0.4159 -0.0457 -0.2021 0.0256  7   SER   A O   
5    C CB  . SER   A 1   ? 0.6284 0.3178 0.4632 -0.0819 -0.2696 0.0460  7   SER   A CB  
6    O OG  . SER   A 1   ? 0.6994 0.3773 0.5279 -0.0910 -0.2845 0.0548  7   SER   A OG  
7    N N   . GLY   A 2   ? 0.4557 0.2598 0.4229 -0.0444 -0.2108 0.0348  8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.4086 0.2503 0.4342 -0.0353 -0.1924 0.0362  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.3784 0.2450 0.4402 -0.0263 -0.1725 0.0321  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.3818 0.2453 0.4189 -0.0233 -0.1668 0.0237  8   GLY   A O   
11   N N   . ALA   A 3   ? 0.3353 0.2223 0.4544 -0.0225 -0.1594 0.0387  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.3177 0.2196 0.4660 -0.0158 -0.1369 0.0352  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.2960 0.2089 0.4728 -0.0108 -0.1069 0.0328  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.2928 0.2057 0.4842 -0.0121 -0.1071 0.0381  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.3099 0.2108 0.5076 -0.0194 -0.1525 0.0517  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.2844 0.2006 0.4643 -0.0070 -0.0808 0.0253  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.2877 0.2002 0.4828 -0.0052 -0.0479 0.0222  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.2999 0.2091 0.5557 -0.0025 -0.0324 0.0344  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.2867 0.1977 0.5493 -0.0017 -0.0373 0.0361  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.2972 0.2046 0.4384 -0.0072 -0.0302 0.0058  10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.2965 0.2101 0.3902 -0.0088 -0.0453 -0.0019 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.3133 0.2030 0.4531 -0.0100 0.0041  0.0015  10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.3036 0.2166 0.3565 -0.0123 -0.0387 -0.0109 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.3167 0.2201 0.6208 -0.0006 -0.0112 0.0443  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.3213 0.2190 0.6956 0.0036  0.0117  0.0596  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.3599 0.2316 0.7217 0.0048  0.0622  0.0497  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.3760 0.2387 0.7406 0.0046  0.0782  0.0494  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.2937 0.2016 0.7474 0.0040  -0.0046 0.0857  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.2846 0.2056 0.7428 -0.0023 -0.0566 0.0978  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.2841 0.2095 0.7800 -0.0038 -0.0734 0.1119  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.3041 0.2267 0.7179 -0.0085 -0.0877 0.0937  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.3007 0.2278 0.7848 -0.0133 -0.1219 0.1215  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.3226 0.2434 0.7210 -0.0175 -0.1325 0.1023  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.3268 0.2478 0.7582 -0.0210 -0.1506 0.1163  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.3611 0.2708 0.7662 -0.0333 -0.1953 0.1244  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.3802 0.2345 0.7220 0.0045  0.0874  0.0417  12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.4179 0.2329 0.7296 0.0016  0.1373  0.0310  12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.4208 0.2187 0.7765 0.0062  0.1688  0.0399  12  VAL   A C   
39   O O   . VAL   A 6   ? 0.4258 0.2308 0.7688 0.0057  0.1564  0.0374  12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.4733 0.2726 0.6848 -0.0094 0.1349  0.0086  12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.4738 0.2952 0.6579 -0.0108 0.1019  0.0040  12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.5249 0.2714 0.6918 -0.0177 0.1834  -0.0016 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.4120 0.1867 0.8254 0.0116  0.2119  0.0521  13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.4250 0.1818 0.8946 0.0179  0.2480  0.0647  13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.3969 0.1960 0.9448 0.0241  0.2088  0.0865  13  GLY   A C   
46   O O   . GLY   A 7   ? 0.3778 0.2109 0.9687 0.0248  0.1671  0.1011  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.3943 0.1893 0.9461 0.0255  0.2154  0.0871  14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.3672 0.1978 0.9854 0.0289  0.1765  0.1072  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.3528 0.2074 0.9020 0.0223  0.1235  0.0922  14  ASN   A C   
50   O O   . ASN   A 8   ? 0.3383 0.2083 0.9089 0.0228  0.1003  0.0999  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.4017 0.2155 1.0725 0.0351  0.2134  0.1190  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.4623 0.2624 1.2395 0.0442  0.2577  0.1458  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.4488 0.2706 1.2994 0.0464  0.2397  0.1682  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.5159 0.2767 1.3075 0.0494  0.3187  0.1464  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.3443 0.2016 0.8175 0.0165  0.1051  0.0733  15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.3380 0.2139 0.7490 0.0115  0.0623  0.0602  15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.3047 0.1997 0.7045 0.0085  0.0223  0.0621  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.2993 0.1909 0.7024 0.0082  0.0300  0.0628  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.3689 0.2268 0.6882 0.0056  0.0775  0.0355  15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.3991 0.2317 0.7051 0.0045  0.1112  0.0306  15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.4012 0.2447 0.7329 0.0077  0.1009  0.0371  15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.4444 0.2363 0.7016 -0.0020 0.1524  0.0187  15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.4365 0.2543 0.7538 0.0063  0.1328  0.0328  15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.4813 0.2405 0.7142 -0.0059 0.1843  0.0138  15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.4866 0.2607 0.7521 -0.0008 0.1749  0.0210  15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.5338 0.2740 0.7733 -0.0049 0.2066  0.0163  15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.2770 0.1865 0.6528 0.0054  -0.0178 0.0609  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.2594 0.1769 0.6054 0.0008  -0.0543 0.0597  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.2576 0.1752 0.5261 -0.0007 -0.0626 0.0396  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.2451 0.1639 0.5038 -0.0004 -0.0689 0.0373  16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.2607 0.1837 0.6505 -0.0042 -0.0933 0.0811  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.2976 0.2158 0.6385 -0.0122 -0.1318 0.0786  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.3234 0.2366 0.7050 -0.0226 -0.1726 0.1035  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.3665 0.2621 0.6861 -0.0320 -0.2058 0.0980  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.4154 0.2916 0.6835 -0.0417 -0.2309 0.0963  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.3866 0.2648 0.6605 -0.0426 -0.2297 0.0994  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.4352 0.2850 0.6411 -0.0508 -0.2541 0.0906  16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.2542 0.1708 0.4747 -0.0020 -0.0608 0.0274  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.2594 0.1776 0.4188 -0.0030 -0.0670 0.0132  17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.2653 0.1822 0.4001 -0.0048 -0.0947 0.0141  17  VAL   A C   
81   O O   . VAL   A 11  ? 0.2806 0.1957 0.4121 -0.0063 -0.0994 0.0157  17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.2757 0.1904 0.3982 -0.0051 -0.0456 0.0017  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.2852 0.2048 0.3621 -0.0065 -0.0526 -0.0066 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.2770 0.1776 0.4118 -0.0069 -0.0142 0.0006  17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.2548 0.1672 0.3669 -0.0054 -0.1103 0.0124  18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.2703 0.1678 0.3468 -0.0089 -0.1315 0.0122  18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.2723 0.1653 0.3037 -0.0058 -0.1257 0.0019  18  VAL   A C   
88   O O   . VAL   A 12  ? 0.2578 0.1616 0.2927 -0.0024 -0.1140 -0.0019 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.3029 0.1848 0.3956 -0.0164 -0.1595 0.0252  18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.3142 0.2009 0.4612 -0.0203 -0.1688 0.0414  18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.2947 0.1794 0.4009 -0.0148 -0.1593 0.0261  18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.2767 0.1501 0.2670 -0.0074 -0.1327 -0.0009 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.2924 0.1562 0.2480 -0.0035 -0.1233 -0.0073 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.3143 0.1659 0.2703 -0.0059 -0.1338 -0.0052 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.3395 0.1707 0.2941 -0.0143 -0.1556 0.0013  19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.3196 0.1522 0.2281 -0.0053 -0.1238 -0.0097 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.3474 0.1905 0.2536 -0.0023 -0.1127 -0.0112 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.3764 0.2151 0.2844 -0.0071 -0.1231 -0.0084 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.3218 0.1798 0.2292 0.0046  -0.0937 -0.0131 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.2918 0.1564 0.2538 -0.0003 -0.1214 -0.0083 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.2898 0.1444 0.2532 -0.0019 -0.1294 -0.0068 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.3512 0.1610 0.2677 -0.0086 -0.1418 -0.0073 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.3812 0.1739 0.2986 -0.0166 -0.1620 -0.0021 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.2735 0.1459 0.2438 0.0051  -0.1125 -0.0097 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.2911 0.1602 0.2714 0.0045  -0.1187 -0.0082 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.2844 0.1677 0.2673 0.0106  -0.1026 -0.0094 20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.2929 0.1777 0.2882 0.0110  -0.1057 -0.0081 20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.3426 0.2021 0.3168 0.0108  -0.1091 -0.0092 20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.3421 0.1658 0.2757 0.0087  -0.1090 -0.0121 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.3481 0.2121 0.3363 0.0116  -0.1109 -0.0078 20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.3814 0.1667 0.2550 -0.0073 -0.1299 -0.0122 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.4495 0.1770 0.2622 -0.0161 -0.1361 -0.0142 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.4885 0.1854 0.2798 -0.0324 -0.1672 -0.0078 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.5424 0.1837 0.2784 -0.0462 -0.1820 -0.0070 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.4859 0.1877 0.2583 -0.0097 -0.1074 -0.0202 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.4879 0.1908 0.2521 -0.0090 -0.1019 -0.0204 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.4727 0.2240 0.2811 0.0010  -0.0894 -0.0188 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.5344 0.1905 0.2456 -0.0185 -0.1068 -0.0216 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.4988 0.2358 0.2856 -0.0010 -0.0868 -0.0193 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.5376 0.2179 0.2661 -0.0122 -0.0963 -0.0211 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.4548 0.1839 0.2892 -0.0328 -0.1782 -0.0013 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.4887 0.1971 0.3201 -0.0483 -0.2100 0.0099  22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.4661 0.2007 0.3631 -0.0526 -0.2328 0.0244  22  LEU   A C   
124  O O   . LEU   A 16  ? 0.4731 0.1979 0.3865 -0.0656 -0.2614 0.0393  22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.4934 0.2117 0.3271 -0.0465 -0.2049 0.0099  22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.5554 0.2418 0.3263 -0.0437 -0.1834 -0.0009 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.5531 0.2531 0.3317 -0.0416 -0.1793 -0.0002 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.6183 0.2308 0.3077 -0.0601 -0.1958 -0.0017 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.4293 0.1985 0.3703 -0.0418 -0.2185 0.0223  23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.4122 0.2048 0.4207 -0.0438 -0.2325 0.0368  23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.4475 0.2051 0.4476 -0.0624 -0.2717 0.0524  23  ALA   A C   
132  O O   . ALA   A 17  ? 0.4887 0.2057 0.4265 -0.0705 -0.2797 0.0464  23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.3855 0.2077 0.4242 -0.0315 -0.2100 0.0306  23  ALA   A CB  
134  N N   . THR   A 18  ? 0.4424 0.2123 0.5060 -0.0700 -0.2950 0.0741  24  THR   A N   
135  C CA  . THR   A 18  ? 0.4801 0.2191 0.5486 -0.0915 -0.3401 0.0960  24  THR   A CA  
136  C C   . THR   A 18  ? 0.4752 0.2279 0.5887 -0.0897 -0.3441 0.1040  24  THR   A C   
137  O O   . THR   A 18  ? 0.4367 0.2241 0.5816 -0.0715 -0.3106 0.0932  24  THR   A O   
138  C CB  . THR   A 18  ? 0.4849 0.2360 0.6183 -0.1006 -0.3642 0.1219  24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.4600 0.2609 0.6882 -0.0843 -0.3395 0.1294  24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.5046 0.2444 0.5998 -0.1026 -0.3616 0.1158  24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.5055 0.2311 0.6291 -0.1105 -0.3878 0.1265  25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.5101 0.2518 0.6879 -0.1089 -0.3928 0.1375  25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.4448 0.2410 0.7334 -0.0925 -0.3697 0.1505  25  HIS   A C   
144  O O   . HIS   A 19  ? 0.4290 0.2501 0.7513 -0.0783 -0.3434 0.1445  25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.5702 0.2725 0.7466 -0.1376 -0.4495 0.1649  25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.7219 0.3556 0.7793 -0.1578 -0.4712 0.1531  25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.7940 0.4082 0.7850 -0.1500 -0.4466 0.1278  25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.8024 0.3772 0.7977 -0.1873 -0.5148 0.1658  25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.8701 0.4118 0.7591 -0.1732 -0.4701 0.1240  25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.8829 0.3955 0.7645 -0.1975 -0.5124 0.1457  25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.4170 0.2263 0.7586 -0.0951 -0.3768 0.1685  26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.3773 0.2285 0.8204 -0.0800 -0.3485 0.1814  26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.3460 0.2207 0.7716 -0.0568 -0.2922 0.1520  26  ASN   A C   
154  O O   . ASN   A 20  ? 0.3290 0.2258 0.8095 -0.0443 -0.2622 0.1538  26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.4221 0.2771 0.9109 -0.0871 -0.3637 0.2030  26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.4912 0.3814 1.0970 -0.0739 -0.3355 0.2233  26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.5063 0.4072 1.1928 -0.0754 -0.3430 0.2484  26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.5053 0.4106 1.1233 -0.0609 -0.2994 0.2137  26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.3432 0.2088 0.6893 -0.0529 -0.2785 0.1263  27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.3178 0.2018 0.6413 -0.0355 -0.2327 0.1013  27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.3014 0.1901 0.6161 -0.0290 -0.2188 0.0914  27  ASP   A C   
162  O O   . ASP   A 21  ? 0.2913 0.1981 0.6349 -0.0179 -0.1855 0.0864  27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.3447 0.2163 0.5875 -0.0347 -0.2270 0.0798  27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.3577 0.2307 0.6093 -0.0369 -0.2288 0.0849  27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.3337 0.2265 0.6462 -0.0305 -0.2099 0.0935  27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.4012 0.2514 0.5967 -0.0451 -0.2464 0.0803  27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.3068 0.1739 0.5784 -0.0376 -0.2436 0.0893  28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.3209 0.1921 0.5834 -0.0317 -0.2319 0.0804  28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.3198 0.2064 0.6631 -0.0304 -0.2320 0.0997  28  TRP   A C   
170  O O   . TRP   A 22  ? 0.3091 0.2093 0.6641 -0.0205 -0.2063 0.0921  28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.3458 0.1832 0.5377 -0.0415 -0.2548 0.0729  28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.3507 0.1784 0.4712 -0.0355 -0.2354 0.0505  28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.3840 0.1853 0.4492 -0.0416 -0.2425 0.0446  28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.3317 0.1752 0.4346 -0.0228 -0.2053 0.0342  28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.3914 0.1928 0.4119 -0.0318 -0.2158 0.0264  28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.3634 0.1930 0.4099 -0.0206 -0.1947 0.0212  28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.3121 0.1800 0.4450 -0.0138 -0.1858 0.0316  28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.3594 0.2007 0.3862 -0.0104 -0.1690 0.0090  28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.3204 0.1972 0.4248 -0.0056 -0.1632 0.0181  28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.3383 0.2045 0.3956 -0.0039 -0.1559 0.0085  28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.3263 0.2102 0.7289 -0.0407 -0.2601 0.1268  29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.3260 0.2254 0.8197 -0.0389 -0.2588 0.1503  29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.3146 0.2372 0.8692 -0.0231 -0.2108 0.1513  29  ALA   A C   
184  O O   . ALA   A 23  ? 0.3060 0.2390 0.9281 -0.0170 -0.1933 0.1649  29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.3185 0.2076 0.8660 -0.0569 -0.3066 0.1848  29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.3040 0.2291 0.8323 -0.0173 -0.1878 0.1376  30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.2779 0.2125 0.8451 -0.0051 -0.1396 0.1356  30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.2751 0.2061 0.7607 0.0014  -0.1094 0.1036  30  ASN   A C   
189  O O   . ASN   A 24  ? 0.2674 0.1965 0.7471 0.0055  -0.0818 0.0966  30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.2895 0.2270 0.9100 -0.0070 -0.1421 0.1541  30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.3202 0.2634 1.0394 -0.0145 -0.1709 0.1927  30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.3350 0.2853 1.1318 -0.0084 -0.1511 0.2104  30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.3163 0.2539 1.0360 -0.0291 -0.2182 0.2088  30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.2815 0.2098 0.7063 0.0005  -0.1176 0.0870  31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.2818 0.2084 0.6358 0.0038  -0.0983 0.0625  31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.2927 0.2159 0.6506 0.0092  -0.0550 0.0555  31  LEU   A C   
197  O O   . LEU   A 25  ? 0.3042 0.2254 0.6974 0.0120  -0.0394 0.0624  31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.2795 0.2042 0.5877 0.0022  -0.1152 0.0529  31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.2885 0.2143 0.5357 0.0047  -0.0993 0.0334  31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.3023 0.2259 0.5091 0.0030  -0.1046 0.0254  31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2829 0.2078 0.5041 0.0047  -0.1102 0.0284  31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.2838 0.2010 0.5974 0.0086  -0.0360 0.0417  32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.2908 0.1921 0.5830 0.0082  0.0026  0.0327  32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.3056 0.2064 0.5266 0.0034  -0.0021 0.0169  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.3318 0.2229 0.5334 0.0008  0.0124  0.0127  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.3021 0.1903 0.5963 0.0074  0.0262  0.0318  32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.3378 0.1973 0.5828 0.0018  0.0630  0.0194  32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.2811 0.1694 0.6587 0.0127  0.0368  0.0517  32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.2902 0.2013 0.4778 0.0018  -0.0238 0.0110  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.2885 0.2029 0.4236 -0.0023 -0.0302 0.0017  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.2699 0.1959 0.3894 -0.0001 -0.0548 0.0002  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.2588 0.1848 0.3877 0.0009  -0.0620 0.0024  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.3079 0.2058 0.4051 -0.0108 -0.0092 -0.0047 33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.3213 0.2235 0.3725 -0.0179 -0.0199 -0.0088 33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.3456 0.2454 0.3716 -0.0249 -0.0220 -0.0084 33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.3092 0.2196 0.3418 -0.0194 -0.0308 -0.0102 33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.3519 0.2594 0.3509 -0.0313 -0.0350 -0.0069 33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.3281 0.2420 0.3309 -0.0273 -0.0389 -0.0084 33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.2982 0.2131 0.3398 -0.0153 -0.0351 -0.0108 33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.3194 0.2418 0.3065 -0.0307 -0.0491 -0.0061 33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.3098 0.2317 0.3287 -0.0179 -0.0440 -0.0114 33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.3103 0.2363 0.3049 -0.0251 -0.0499 -0.0086 33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.2537 0.1859 0.3490 0.0001  -0.0646 -0.0025 34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.2526 0.1878 0.3280 0.0024  -0.0789 -0.0041 34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.2484 0.1909 0.3008 0.0012  -0.0765 -0.0049 34  GLU   A C   
226  O O   . GLU   A 28  ? 0.2467 0.1921 0.3002 -0.0011 -0.0726 -0.0033 34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.2640 0.1915 0.3460 0.0052  -0.0965 -0.0014 34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.2624 0.1898 0.3567 0.0064  -0.0998 0.0008  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.3040 0.2331 0.3762 0.0088  -0.0983 -0.0019 34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.3535 0.2873 0.4358 0.0093  -0.0956 -0.0005 34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.2868 0.2119 0.3356 0.0105  -0.0977 -0.0039 34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.2407 0.1856 0.2771 0.0022  -0.0789 -0.0049 35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.2324 0.1862 0.2608 0.0014  -0.0774 -0.0001 35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.2395 0.1880 0.2605 0.0085  -0.0780 0.0007  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.2554 0.2005 0.2675 0.0090  -0.0770 -0.0005 35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.2510 0.2097 0.2697 -0.0087 -0.0742 0.0036  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.3132 0.2832 0.3340 -0.0131 -0.0781 0.0150  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2945 0.2703 0.3275 -0.0048 -0.0777 0.0199  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.3465 0.3150 0.3558 -0.0266 -0.0812 0.0208  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.2418 0.1841 0.2635 0.0140  -0.0766 0.0023  36  SER   A N   
241  C CA  A SER   A 30  ? 0.2570 0.1814 0.2641 0.0203  -0.0699 0.0022  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.2604 0.1847 0.2672 0.0203  -0.0700 0.0021  36  SER   A CA  
243  C C   . SER   A 30  ? 0.2591 0.1946 0.2743 0.0221  -0.0598 0.0107  36  SER   A C   
244  O O   . SER   A 30  ? 0.2774 0.1979 0.2784 0.0258  -0.0523 0.0094  36  SER   A O   
245  C CB  A SER   A 30  ? 0.2747 0.1857 0.2800 0.0249  -0.0652 0.0029  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2891 0.1982 0.2922 0.0248  -0.0655 0.0023  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.3043 0.1853 0.2859 0.0300  -0.0526 0.0015  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.3004 0.2299 0.3289 0.0263  -0.0595 0.0119  36  SER   A OG  
249  N N   . SER   A 31  ? 0.2321 0.1912 0.2705 0.0178  -0.0612 0.0215  37  SER   A N   
250  C CA  . SER   A 31  ? 0.2277 0.2000 0.2843 0.0172  -0.0562 0.0353  37  SER   A CA  
251  C C   . SER   A 31  ? 0.2302 0.2039 0.2748 0.0126  -0.0598 0.0322  37  SER   A C   
252  O O   . SER   A 31  ? 0.2361 0.2152 0.2935 0.0143  -0.0539 0.0422  37  SER   A O   
253  C CB  . SER   A 31  ? 0.2493 0.2435 0.3324 0.0086  -0.0644 0.0517  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2960 0.2948 0.3640 -0.0057 -0.0781 0.0496  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.2110 0.1800 0.2370 0.0073  -0.0674 0.0204  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.2086 0.1771 0.2236 0.0030  -0.0693 0.0169  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.2213 0.1721 0.2199 0.0094  -0.0672 0.0066  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.2320 0.1820 0.2236 0.0073  -0.0679 0.0044  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.2171 0.1863 0.2233 -0.0084 -0.0747 0.0128  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.2296 0.2063 0.2371 -0.0210 -0.0806 0.0238  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.2704 0.2329 0.2547 -0.0343 -0.0800 0.0179  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.2778 0.2308 0.2456 -0.0397 -0.0766 0.0131  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.2924 0.2258 0.2316 -0.0557 -0.0739 0.0117  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.3155 0.2349 0.2348 -0.0695 -0.0762 0.0156  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.3093 0.2319 0.2340 -0.0596 -0.0685 0.0069  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.2375 0.1709 0.2271 0.0147  -0.0673 0.0014  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.2412 0.1507 0.2090 0.0155  -0.0723 -0.0058 39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.2374 0.1528 0.2140 0.0099  -0.0825 -0.0091 39  ASP   A C   
269  O O   . ASP   A 33  ? 0.2590 0.1628 0.2256 0.0084  -0.0880 -0.0109 39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.2660 0.1593 0.2140 0.0188  -0.0633 -0.0054 39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.3295 0.1886 0.2443 0.0158  -0.0715 -0.0114 39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.3406 0.1787 0.2412 0.0125  -0.0814 -0.0139 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.3282 0.1804 0.2305 0.0144  -0.0715 -0.0122 39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.2170 0.1462 0.2128 0.0066  -0.0830 -0.0086 40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.2176 0.1476 0.2291 0.0029  -0.0851 -0.0098 40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.2344 0.1607 0.2660 0.0029  -0.0905 -0.0082 40  LEU   A C   
277  O O   . LEU   A 34  ? 0.2512 0.1811 0.2854 0.0038  -0.0885 -0.0079 40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.2110 0.1496 0.2249 -0.0029 -0.0738 -0.0101 40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.2400 0.1822 0.2394 -0.0060 -0.0708 -0.0097 40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.2358 0.1748 0.2262 -0.0164 -0.0614 -0.0100 40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.2530 0.1893 0.2531 -0.0033 -0.0742 -0.0114 40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.2277 0.1494 0.2813 0.0013  -0.0958 -0.0049 41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.2345 0.1551 0.3211 0.0009  -0.0995 0.0009  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.2342 0.1564 0.3562 -0.0002 -0.0900 0.0064  41  LEU   A C   
285  O O   . LEU   A 35  ? 0.2445 0.1647 0.3664 -0.0014 -0.0938 0.0079  41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.2517 0.1580 0.3375 -0.0014 -0.1230 0.0064  41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.2638 0.1703 0.3924 -0.0031 -0.1316 0.0167  41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.2968 0.1860 0.4061 -0.0070 -0.1527 0.0187  41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.2723 0.1778 0.4462 -0.0071 -0.1421 0.0309  41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.2259 0.1490 0.3774 0.0006  -0.0734 0.0093  42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.2282 0.1471 0.4204 0.0010  -0.0557 0.0163  42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.2359 0.1557 0.4858 0.0029  -0.0604 0.0308  42  VAL   A C   
293  O O   . VAL   A 36  ? 0.2342 0.1545 0.4865 0.0040  -0.0581 0.0303  42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.2589 0.1664 0.4307 -0.0013 -0.0226 0.0080  42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.2661 0.1604 0.4796 0.0000  0.0046  0.0151  42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.2704 0.1777 0.3889 -0.0060 -0.0239 -0.0024 42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.2330 0.1540 0.5336 0.0025  -0.0694 0.0462  43  SER   A N   
298  C CA  . SER   A 37  ? 0.2441 0.1675 0.6139 0.0029  -0.0763 0.0663  43  SER   A CA  
299  C C   . SER   A 37  ? 0.2652 0.1856 0.6996 0.0071  -0.0455 0.0792  43  SER   A C   
300  O O   . SER   A 37  ? 0.2611 0.1761 0.6824 0.0079  -0.0275 0.0732  43  SER   A O   
301  C CB  . SER   A 37  ? 0.2486 0.1722 0.6304 -0.0048 -0.1216 0.0807  43  SER   A CB  
302  O OG  . SER   A 37  ? 0.2626 0.1843 0.6460 -0.0089 -0.1344 0.0863  43  SER   A OG  
303  N N   . SER   A 38  ? 0.2792 0.2009 0.7863 0.0101  -0.0366 0.0981  44  SER   A N   
304  C CA  . SER   A 38  ? 0.3061 0.2214 0.8859 0.0156  -0.0009 0.1140  44  SER   A CA  
305  C C   . SER   A 38  ? 0.3326 0.2591 0.9859 0.0126  -0.0265 0.1414  44  SER   A C   
306  O O   . SER   A 38  ? 0.3358 0.2719 0.9975 0.0040  -0.0756 0.1543  44  SER   A O   
307  C CB  . SER   A 38  ? 0.3094 0.2188 0.9419 0.0212  0.0265  0.1247  44  SER   A CB  
308  O OG  . SER   A 38  ? 0.3205 0.2456 0.9931 0.0175  -0.0135 0.1423  44  SER   A OG  
309  N N   . THR   A 39  ? 0.3493 0.2694 1.0521 0.0176  0.0067  0.1513  45  THR   A N   
310  C CA  . THR   A 39  ? 0.3659 0.2971 1.1497 0.0148  -0.0140 0.1812  45  THR   A CA  
311  C C   . THR   A 39  ? 0.3968 0.3225 1.2886 0.0241  0.0314  0.2064  45  THR   A C   
312  O O   . THR   A 39  ? 0.4253 0.3289 1.3026 0.0326  0.0880  0.1924  45  THR   A O   
313  C CB  . THR   A 39  ? 0.3825 0.3112 1.1229 0.0125  -0.0160 0.1694  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.3987 0.3081 1.1281 0.0207  0.0423  0.1557  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.4148 0.3440 1.0472 0.0056  -0.0480 0.1428  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.3892 0.3299 1.3869 0.0214  0.0088  0.2448  46  THR   A N   
317  C CA  . THR   A 40  ? 0.3902 0.3269 1.5086 0.0314  0.0540  0.2750  46  THR   A CA  
318  C C   . THR   A 40  ? 0.4136 0.3366 1.5423 0.0376  0.0953  0.2721  46  THR   A C   
319  O O   . THR   A 40  ? 0.4264 0.3277 1.6058 0.0490  0.1601  0.2780  46  THR   A O   
320  C CB  . THR   A 40  ? 0.3787 0.3390 1.6189 0.0243  0.0088  0.3234  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.4079 0.3813 1.6351 0.0090  -0.0550 0.3348  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.3899 0.3563 1.6292 0.0204  -0.0160 0.3269  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.4192 0.3502 1.4985 0.0297  0.0611  0.2633  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.4251 0.3444 1.5102 0.0344  0.0948  0.2603  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.4758 0.3657 1.4407 0.0376  0.1376  0.2156  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.5065 0.3930 1.3765 0.0337  0.1250  0.1876  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.4202 0.3597 1.5106 0.0234  0.0381  0.2738  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.4870 0.3531 1.4576 0.0432  0.1875  0.2112  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.5396 0.3704 1.3973 0.0422  0.2269  0.1728  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.5390 0.3804 1.3209 0.0348  0.1930  0.1545  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.5235 0.3751 1.3521 0.0352  0.1850  0.1698  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.5854 0.3713 1.4773 0.0503  0.3061  0.1760  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.7193 0.4524 1.5042 0.0469  0.3563  0.1426  48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.8079 0.5343 1.5948 0.0487  0.3657  0.1427  48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.8083 0.5538 1.7028 0.0568  0.3654  0.1725  48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.8528 0.5511 1.5243 0.0400  0.3732  0.1120  48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.5450 0.3831 1.2156 0.0280  0.1756  0.1237  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.5468 0.3931 1.1386 0.0212  0.1464  0.1046  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.5409 0.3525 1.0762 0.0191  0.1893  0.0854  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.5678 0.3397 1.0699 0.0182  0.2369  0.0735  49  GLY   A O   
341  N N   . CYS   A 44  ? 0.5074 0.3283 1.0224 0.0162  0.1717  0.0817  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.5128 0.3004 0.9780 0.0128  0.2084  0.0660  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.4981 0.2888 0.8650 0.0035  0.1826  0.0427  50  CYS   A C   
344  O O   . CYS   A 44  ? 0.5144 0.2855 0.8489 -0.0006 0.2003  0.0340  50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.5197 0.3087 1.0645 0.0187  0.2246  0.0863  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.5810 0.3537 1.2486 0.0300  0.2750  0.1160  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.4597 0.2734 0.7833 0.0001  0.1429  0.0344  51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.4673 0.2843 0.7085 -0.0080 0.1217  0.0162  51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.4956 0.2716 0.6633 -0.0183 0.1531  -0.0013 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.5184 0.2725 0.6836 -0.0193 0.1762  -0.0025 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.4807 0.3307 0.7031 -0.0078 0.0746  0.0149  51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.5050 0.3831 0.7659 -0.0041 0.0375  0.0283  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.5195 0.3987 0.7994 -0.0036 0.0385  0.0339  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.5124 0.4067 0.7780 -0.0034 0.0069  0.0332  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.5101 0.2717 0.6164 -0.0280 0.1527  -0.0132 52  THR   A N   
356  C CA  . THR   A 46  ? 0.5499 0.2662 0.5756 -0.0438 0.1744  -0.0275 52  THR   A CA  
357  C C   . THR   A 46  ? 0.5307 0.2674 0.5053 -0.0518 0.1364  -0.0334 52  THR   A C   
358  O O   . THR   A 46  ? 0.5196 0.2851 0.4895 -0.0509 0.1072  -0.0329 52  THR   A O   
359  C CB  . THR   A 46  ? 0.6036 0.2882 0.5920 -0.0531 0.1933  -0.0340 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.6256 0.2871 0.6661 -0.0450 0.2350  -0.0271 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.6497 0.2815 0.5408 -0.0756 0.2060  -0.0472 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.5155 0.2351 0.4534 -0.0601 0.1388  -0.0377 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.4877 0.2265 0.3850 -0.0683 0.1039  -0.0396 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.5175 0.2197 0.3389 -0.0905 0.1047  -0.0455 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.5641 0.2088 0.3380 -0.1051 0.1361  -0.0517 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.4791 0.2187 0.3753 -0.0682 0.1016  -0.0387 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.4567 0.2233 0.4282 -0.0491 0.1037  -0.0311 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.4672 0.2324 0.3364 -0.0744 0.0649  -0.0369 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.4347 0.2506 0.4485 -0.0364 0.0684  -0.0244 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.4934 0.2227 0.3014 -0.0947 0.0718  -0.0424 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.5177 0.2180 0.2603 -0.1181 0.0624  -0.0429 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.5464 0.2206 0.2388 -0.1373 0.0542  -0.0410 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.5175 0.2218 0.2362 -0.1290 0.0393  -0.0364 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.4826 0.2263 0.2420 -0.1147 0.0286  -0.0353 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.6038 0.2165 0.2190 -0.1652 0.0634  -0.0439 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.6607 0.2385 0.2152 -0.1902 0.0510  -0.0398 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.7068 0.2663 0.2091 -0.2176 0.0214  -0.0309 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.7669 0.2625 0.2007 -0.2403 0.0373  -0.0368 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.7237 0.2278 0.2242 -0.2019 0.0942  -0.0509 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.7070 0.2294 0.2714 -0.1743 0.1259  -0.0560 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.6808 0.2625 0.3002 -0.1579 0.1000  -0.0488 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.6725 0.2681 0.3533 -0.1343 0.1276  -0.0514 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.6205 0.2678 0.3606 -0.1158 0.1103  -0.0461 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.5522 0.2403 0.2980 -0.1161 0.0710  -0.0394 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.5774 0.2329 0.3736 -0.0976 0.1332  -0.0456 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.6788 0.2940 0.2193 -0.2146 -0.0198 -0.0155 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.6963 0.3081 0.2121 -0.2361 -0.0509 -0.0021 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.6622 0.3326 0.2293 -0.2327 -0.0919 0.0197  56  CYS   A C   
389  O O   . CYS   A 50  ? 0.6153 0.3261 0.2320 -0.2123 -0.0928 0.0213  56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.6727 0.3013 0.2163 -0.2207 -0.0382 -0.0090 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.5878 0.3022 0.2353 -0.1785 -0.0419 -0.0077 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.6586 0.3353 0.2221 -0.2503 -0.1230 0.0376  57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.6309 0.3645 0.2580 -0.2438 -0.1554 0.0615  57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.5984 0.3723 0.2759 -0.2276 -0.1593 0.0670  57  ASP   A C   
395  O O   . ASP   A 51  ? 0.5814 0.3843 0.2964 -0.2333 -0.1873 0.0916  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.6919 0.4039 0.2884 -0.2803 -0.1950 0.0878  57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.8099 0.4811 0.3539 -0.3157 -0.2191 0.1008  57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.8352 0.4853 0.3534 -0.3135 -0.1997 0.0850  57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.8894 0.5492 0.4204 -0.3472 -0.2599 0.1290  57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.5781 0.3541 0.2620 -0.2071 -0.1305 0.0464  58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.5279 0.3383 0.2550 -0.1904 -0.1305 0.0490  58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.4557 0.3216 0.2537 -0.1696 -0.1415 0.0641  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.4465 0.3302 0.2688 -0.1542 -0.1349 0.0610  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.5308 0.3386 0.2625 -0.1689 -0.0983 0.0259  58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.5937 0.3381 0.2563 -0.1891 -0.0777 0.0109  58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.4116 0.3008 0.2422 -0.1685 -0.1545 0.0800  59  GLN   A N   
407  C CA  . GLN   A 53  ? 0.3669 0.3018 0.2651 -0.1466 -0.1554 0.0938  59  GLN   A CA  
408  C C   . GLN   A 53  ? 0.3293 0.2799 0.2493 -0.1267 -0.1398 0.0860  59  GLN   A C   
409  O O   . GLN   A 53  ? 0.3076 0.2865 0.2764 -0.1129 -0.1391 0.1001  59  GLN   A O   
410  C CB  . GLN   A 53  ? 0.3924 0.3440 0.3267 -0.1624 -0.1843 0.1282  59  GLN   A CB  
411  C CG  . GLN   A 53  ? 0.4422 0.3916 0.3774 -0.1736 -0.1986 0.1399  59  GLN   A CG  
412  C CD  . GLN   A 53  ? 0.4724 0.4437 0.4602 -0.1878 -0.2282 0.1796  59  GLN   A CD  
413  O OE1 . GLN   A 53  ? 0.5170 0.4666 0.4792 -0.2212 -0.2602 0.1990  59  GLN   A OE1 
414  N NE2 . GLN   A 53  ? 0.4288 0.4390 0.4914 -0.1644 -0.2177 0.1948  59  GLN   A NE2 
415  N N   . THR   A 54  ? 0.3330 0.2625 0.2185 -0.1255 -0.1253 0.0651  60  THR   A N   
416  C CA  . THR   A 54  ? 0.3185 0.2595 0.2200 -0.1073 -0.1107 0.0560  60  THR   A CA  
417  C C   . THR   A 54  ? 0.2982 0.2245 0.1810 -0.0959 -0.0899 0.0319  60  THR   A C   
418  O O   . THR   A 54  ? 0.3325 0.2307 0.1812 -0.1071 -0.0836 0.0219  60  THR   A O   
419  C CB  . THR   A 54  ? 0.3806 0.3142 0.2724 -0.1208 -0.1192 0.0633  60  THR   A CB  
420  O OG1 . THR   A 54  ? 0.4498 0.3438 0.2872 -0.1393 -0.1155 0.0504  60  THR   A OG1 
421  C CG2 . THR   A 54  ? 0.3825 0.3290 0.2988 -0.1366 -0.1446 0.0925  60  THR   A CG2 
422  N N   . GLY   A 55  ? 0.2737 0.2153 0.1797 -0.0748 -0.0790 0.0253  61  GLY   A N   
423  C CA  . GLY   A 55  ? 0.2695 0.2013 0.1708 -0.0646 -0.0644 0.0087  61  GLY   A CA  
424  C C   . GLY   A 55  ? 0.2536 0.1985 0.1755 -0.0466 -0.0601 0.0063  61  GLY   A C   
425  O O   . GLY   A 55  ? 0.2481 0.2044 0.1810 -0.0425 -0.0631 0.0147  61  GLY   A O   
426  N N   . VAL   A 56  ? 0.2436 0.1832 0.1705 -0.0376 -0.0537 -0.0029 62  VAL   A N   
427  C CA  . VAL   A 56  ? 0.2378 0.1803 0.1746 -0.0253 -0.0539 -0.0044 62  VAL   A CA  
428  C C   . VAL   A 56  ? 0.2428 0.1824 0.1848 -0.0181 -0.0565 -0.0071 62  VAL   A C   
429  O O   . VAL   A 56  ? 0.2435 0.1782 0.1915 -0.0206 -0.0540 -0.0109 62  VAL   A O   
430  C CB  . VAL   A 56  ? 0.2689 0.2034 0.2093 -0.0267 -0.0491 -0.0088 62  VAL   A CB  
431  C CG1 . VAL   A 56  ? 0.2874 0.2204 0.2352 -0.0179 -0.0545 -0.0080 62  VAL   A CG1 
432  C CG2 . VAL   A 56  ? 0.2844 0.2183 0.2149 -0.0350 -0.0470 -0.0066 62  VAL   A CG2 
433  N N   . TYR   A 57  ? 0.2421 0.1790 0.1793 -0.0102 -0.0595 -0.0049 63  TYR   A N   
434  C CA  . TYR   A 57  ? 0.2395 0.1667 0.1744 -0.0062 -0.0647 -0.0070 63  TYR   A CA  
435  C C   . TYR   A 57  ? 0.2551 0.1651 0.1791 -0.0045 -0.0725 -0.0068 63  TYR   A C   
436  O O   . TYR   A 57  ? 0.2688 0.1731 0.1810 -0.0035 -0.0703 -0.0053 63  TYR   A O   
437  C CB  . TYR   A 57  ? 0.2422 0.1693 0.1708 -0.0020 -0.0614 -0.0044 63  TYR   A CB  
438  C CG  . TYR   A 57  ? 0.2664 0.1809 0.1796 0.0043  -0.0537 -0.0007 63  TYR   A CG  
439  C CD1 . TYR   A 57  ? 0.2737 0.1978 0.1953 0.0058  -0.0449 0.0064  63  TYR   A CD1 
440  C CD2 . TYR   A 57  ? 0.2929 0.1808 0.1817 0.0077  -0.0530 -0.0029 63  TYR   A CD2 
441  C CE1 . TYR   A 57  ? 0.2902 0.1994 0.2026 0.0131  -0.0307 0.0115  63  TYR   A CE1 
442  C CE2 . TYR   A 57  ? 0.3246 0.1896 0.1916 0.0131  -0.0381 -0.0002 63  TYR   A CE2 
443  C CZ  . TYR   A 57  ? 0.3171 0.1937 0.1991 0.0171  -0.0246 0.0072  63  TYR   A CZ  
444  O OH  . TYR   A 57  ? 0.3578 0.2086 0.2230 0.0238  -0.0034 0.0114  63  TYR   A OH  
445  N N   . TYR   A 58  ? 0.2596 0.1588 0.1869 -0.0062 -0.0835 -0.0064 64  TYR   A N   
446  C CA  . TYR   A 58  ? 0.2946 0.1708 0.2065 -0.0096 -0.0982 -0.0028 64  TYR   A CA  
447  C C   . TYR   A 58  ? 0.3230 0.1714 0.1942 -0.0090 -0.0987 -0.0041 64  TYR   A C   
448  O O   . TYR   A 58  ? 0.3111 0.1575 0.1805 -0.0076 -0.0979 -0.0058 64  TYR   A O   
449  C CB  . TYR   A 58  ? 0.2905 0.1663 0.2324 -0.0149 -0.1141 0.0036  64  TYR   A CB  
450  C CG  . TYR   A 58  ? 0.3313 0.1802 0.2563 -0.0232 -0.1367 0.0119  64  TYR   A CG  
451  C CD1 . TYR   A 58  ? 0.3529 0.1957 0.2712 -0.0261 -0.1406 0.0153  64  TYR   A CD1 
452  C CD2 . TYR   A 58  ? 0.3742 0.1996 0.2849 -0.0306 -0.1566 0.0174  64  TYR   A CD2 
453  C CE1 . TYR   A 58  ? 0.3970 0.2095 0.2931 -0.0374 -0.1649 0.0249  64  TYR   A CE1 
454  C CE2 . TYR   A 58  ? 0.4176 0.2096 0.3024 -0.0436 -0.1826 0.0272  64  TYR   A CE2 
455  C CZ  . TYR   A 58  ? 0.4446 0.2297 0.3215 -0.0474 -0.1872 0.0313  64  TYR   A CZ  
456  O OH  . TYR   A 58  ? 0.5135 0.2597 0.3575 -0.0636 -0.2160 0.0426  64  TYR   A OH  
457  N N   . CYS   A 59  ? 0.3579 0.1786 0.1920 -0.0109 -0.0980 -0.0035 65  CYS   A N   
458  C CA  . CYS   A 59  ? 0.4189 0.1980 0.2018 -0.0117 -0.0916 -0.0054 65  CYS   A CA  
459  C C   . CYS   A 59  ? 0.4757 0.2094 0.2163 -0.0257 -0.1149 -0.0016 65  CYS   A C   
460  O O   . CYS   A 59  ? 0.4978 0.2115 0.2144 -0.0310 -0.1191 0.0008  65  CYS   A O   
461  C CB  . CYS   A 59  ? 0.4418 0.2153 0.2099 -0.0037 -0.0656 -0.0064 65  CYS   A CB  
462  S SG  . CYS   A 59  ? 0.5191 0.2260 0.2165 -0.0045 -0.0461 -0.0087 65  CYS   A SG  
463  N N   . SER   A 60  ? 0.4960 0.2117 0.2271 -0.0339 -0.1335 0.0007  66  SER   A N   
464  C CA  . SER   A 60  ? 0.5512 0.2220 0.2441 -0.0521 -0.1638 0.0086  66  SER   A CA  
465  C C   . SER   A 60  ? 0.6087 0.2143 0.2177 -0.0606 -0.1565 0.0053  66  SER   A C   
466  O O   . SER   A 60  ? 0.6519 0.2233 0.2280 -0.0764 -0.1796 0.0129  66  SER   A O   
467  C CB  . SER   A 60  ? 0.6068 0.2686 0.3057 -0.0606 -0.1860 0.0138  66  SER   A CB  
468  O OG  . SER   A 60  ? 0.7105 0.3547 0.3781 -0.0546 -0.1655 0.0042  66  SER   A OG  
469  N N   . SER   A 61  ? 0.6147 0.2000 0.1903 -0.0506 -0.1222 -0.0043 67  SER   A N   
470  C CA  . SER   A 61  ? 0.6756 0.1890 0.1666 -0.0573 -0.1043 -0.0083 67  SER   A CA  
471  C C   . SER   A 61  ? 0.6863 0.1974 0.1690 -0.0554 -0.0938 -0.0071 67  SER   A C   
472  O O   . SER   A 61  ? 0.7673 0.2121 0.1748 -0.0632 -0.0796 -0.0095 67  SER   A O   
473  C CB  . SER   A 61  ? 0.7047 0.1969 0.1742 -0.0451 -0.0639 -0.0160 67  SER   A CB  
474  O OG  . SER   A 61  ? 0.6844 0.2326 0.2165 -0.0244 -0.0352 -0.0162 67  SER   A OG  
475  N N   . ARG   A 62  ? 0.6169 0.1931 0.1705 -0.0467 -0.1003 -0.0035 68  ARG   A N   
476  C CA  . ARG   A 62  ? 0.6145 0.1948 0.1682 -0.0454 -0.0947 -0.0014 68  ARG   A CA  
477  C C   . ARG   A 62  ? 0.5995 0.2137 0.1976 -0.0531 -0.1285 0.0073  68  ARG   A C   
478  O O   . ARG   A 62  ? 0.6121 0.2325 0.2147 -0.0529 -0.1273 0.0099  68  ARG   A O   
479  C CB  . ARG   A 62  ? 0.5900 0.2145 0.1892 -0.0254 -0.0604 -0.0044 68  ARG   A CB  
480  C CG  . ARG   A 62  ? 0.6291 0.2224 0.1993 -0.0157 -0.0212 -0.0079 68  ARG   A CG  
481  C CD  . ARG   A 62  ? 0.6857 0.2153 0.1889 -0.0196 0.0004  -0.0087 68  ARG   A CD  
482  N NE  . ARG   A 62  ? 0.7526 0.2531 0.2409 -0.0074 0.0469  -0.0095 68  ARG   A NE  
483  C CZ  . ARG   A 62  ? 0.8211 0.2570 0.2478 -0.0119 0.0646  -0.0140 68  ARG   A CZ  
484  N NH1 . ARG   A 62  ? 0.8564 0.2500 0.2264 -0.0306 0.0347  -0.0182 68  ARG   A NH1 
485  N NH2 . ARG   A 62  ? 0.8352 0.2468 0.2603 0.0015  0.1128  -0.0125 68  ARG   A NH2 
486  N N   . ARG   A 63  ? 0.5761 0.2123 0.2130 -0.0589 -0.1556 0.0134  69  ARG   A N   
487  C CA  . ARG   A 63  ? 0.5586 0.2311 0.2560 -0.0634 -0.1813 0.0245  69  ARG   A CA  
488  C C   . ARG   A 63  ? 0.5046 0.2277 0.2532 -0.0488 -0.1602 0.0207  69  ARG   A C   
489  O O   . ARG   A 63  ? 0.5010 0.2324 0.2679 -0.0523 -0.1696 0.0274  69  ARG   A O   
490  C CB  . ARG   A 63  ? 0.6249 0.2558 0.2900 -0.0847 -0.2161 0.0384  69  ARG   A CB  
491  C CG  . ARG   A 63  ? 0.7238 0.3133 0.3581 -0.1041 -0.2493 0.0483  69  ARG   A CG  
492  C CD  . ARG   A 63  ? 0.8300 0.3816 0.4413 -0.1289 -0.2909 0.0674  69  ARG   A CD  
493  N NE  . ARG   A 63  ? 0.9739 0.4561 0.5115 -0.1540 -0.3213 0.0749  69  ARG   A NE  
494  C CZ  . ARG   A 63  ? 1.0912 0.4977 0.5349 -0.1771 -0.3379 0.0787  69  ARG   A CZ  
495  N NH1 . ARG   A 63  ? 1.1065 0.5013 0.5236 -0.1758 -0.3252 0.0757  69  ARG   A NH1 
496  N NH2 . ARG   A 63  ? 1.1491 0.4851 0.5177 -0.2031 -0.3664 0.0853  69  ARG   A NH2 
497  N N   . LYS   A 64  ? 0.4541 0.2061 0.2212 -0.0342 -0.1329 0.0111  70  LYS   A N   
498  C CA  . LYS   A 64  ? 0.4228 0.2140 0.2268 -0.0241 -0.1148 0.0082  70  LYS   A CA  
499  C C   . LYS   A 64  ? 0.3766 0.2049 0.2191 -0.0155 -0.1014 0.0036  70  LYS   A C   
500  O O   . LYS   A 64  ? 0.3749 0.1981 0.2082 -0.0132 -0.0973 0.0007  70  LYS   A O   
501  C CB  . LYS   A 64  ? 0.4737 0.2492 0.2435 -0.0180 -0.0918 0.0044  70  LYS   A CB  
502  C CG  . LYS   A 64  ? 0.5981 0.3459 0.3362 -0.0242 -0.0966 0.0079  70  LYS   A CG  
503  C CD  . LYS   A 64  ? 0.7053 0.4409 0.4202 -0.0155 -0.0669 0.0051  70  LYS   A CD  
504  C CE  . LYS   A 64  ? 0.7895 0.5141 0.4903 -0.0178 -0.0653 0.0081  70  LYS   A CE  
505  N NZ  . LYS   A 64  ? 0.8571 0.5217 0.4923 -0.0317 -0.0787 0.0104  70  LYS   A NZ  
506  N N   . HIS   A 65  ? 0.3394 0.1991 0.2174 -0.0122 -0.0934 0.0029  71  HIS   A N   
507  C CA  . HIS   A 65  ? 0.3081 0.1941 0.2098 -0.0081 -0.0812 -0.0009 71  HIS   A CA  
508  C C   . HIS   A 65  ? 0.3188 0.2128 0.2129 -0.0036 -0.0659 -0.0008 71  HIS   A C   
509  O O   . HIS   A 65  ? 0.3307 0.2214 0.2182 -0.0033 -0.0627 0.0012  71  HIS   A O   
510  C CB  . HIS   A 65  ? 0.2866 0.1908 0.2239 -0.0109 -0.0803 -0.0008 71  HIS   A CB  
511  C CG  . HIS   A 65  ? 0.3056 0.2059 0.2682 -0.0141 -0.0919 0.0039  71  HIS   A CG  
512  N ND1 . HIS   A 65  ? 0.3308 0.2379 0.3133 -0.0138 -0.0882 0.0027  71  HIS   A ND1 
513  C CD2 . HIS   A 65  ? 0.3200 0.2111 0.2971 -0.0185 -0.1072 0.0127  71  HIS   A CD2 
514  C CE1 . HIS   A 65  ? 0.3082 0.2111 0.3209 -0.0166 -0.0998 0.0114  71  HIS   A CE1 
515  N NE2 . HIS   A 65  ? 0.3201 0.2140 0.3325 -0.0203 -0.1136 0.0190  71  HIS   A NE2 
516  N N   . TYR   A 66  ? 0.2880 0.1937 0.1887 -0.0009 -0.0575 -0.0002 72  TYR   A N   
517  C CA  . TYR   A 66  ? 0.2805 0.1969 0.1876 0.0020  -0.0458 0.0059  72  TYR   A CA  
518  C C   . TYR   A 66  ? 0.2644 0.2038 0.1932 -0.0038 -0.0475 0.0088  72  TYR   A C   
519  O O   . TYR   A 66  ? 0.2656 0.2085 0.1983 -0.0060 -0.0507 0.0068  72  TYR   A O   
520  C CB  . TYR   A 66  ? 0.2981 0.2003 0.1945 0.0093  -0.0330 0.0101  72  TYR   A CB  
521  C CG  . TYR   A 66  ? 0.3475 0.2127 0.2067 0.0124  -0.0261 0.0079  72  TYR   A CG  
522  C CD1 . TYR   A 66  ? 0.3779 0.2337 0.2287 0.0146  -0.0160 0.0115  72  TYR   A CD1 
523  C CD2 . TYR   A 66  ? 0.3945 0.2283 0.2212 0.0113  -0.0287 0.0032  72  TYR   A CD2 
524  C CE1 . TYR   A 66  ? 0.4326 0.2443 0.2378 0.0149  -0.0077 0.0093  72  TYR   A CE1 
525  C CE2 . TYR   A 66  ? 0.4453 0.2325 0.2230 0.0093  -0.0237 0.0013  72  TYR   A CE2 
526  C CZ  . TYR   A 66  ? 0.4744 0.2488 0.2391 0.0110  -0.0121 0.0040  72  TYR   A CZ  
527  O OH  . TYR   A 66  ? 0.5539 0.2724 0.2593 0.0070  -0.0044 0.0020  72  TYR   A OH  
528  N N   . PRO   A 67  ? 0.2514 0.2025 0.1905 -0.0081 -0.0464 0.0151  73  PRO   A N   
529  C CA  . PRO   A 67  ? 0.2483 0.2124 0.1982 -0.0188 -0.0521 0.0211  73  PRO   A CA  
530  C C   . PRO   A 67  ? 0.2666 0.2411 0.2359 -0.0163 -0.0504 0.0350  73  PRO   A C   
531  O O   . PRO   A 67  ? 0.2886 0.2632 0.2699 -0.0070 -0.0398 0.0434  73  PRO   A O   
532  C CB  . PRO   A 67  ? 0.2601 0.2277 0.2115 -0.0263 -0.0543 0.0252  73  PRO   A CB  
533  C CG  . PRO   A 67  ? 0.2683 0.2329 0.2214 -0.0154 -0.0463 0.0267  73  PRO   A CG  
534  C CD  . PRO   A 67  ? 0.2612 0.2103 0.1994 -0.0057 -0.0418 0.0186  73  PRO   A CD  
535  N N   . VAL   A 68  ? 0.2547 0.2353 0.2291 -0.0247 -0.0584 0.0394  74  VAL   A N   
536  C CA  . VAL   A 68  ? 0.2547 0.2469 0.2562 -0.0226 -0.0579 0.0557  74  VAL   A CA  
537  C C   . VAL   A 68  ? 0.2453 0.2457 0.2542 -0.0408 -0.0755 0.0683  74  VAL   A C   
538  O O   . VAL   A 68  ? 0.2719 0.2605 0.2520 -0.0538 -0.0837 0.0584  74  VAL   A O   
539  C CB  . VAL   A 68  ? 0.2793 0.2648 0.2768 -0.0125 -0.0503 0.0490  74  VAL   A CB  
540  C CG1 . VAL   A 68  ? 0.3218 0.2905 0.3088 0.0027  -0.0334 0.0431  74  VAL   A CG1 
541  C CG2 . VAL   A 68  ? 0.2833 0.2611 0.2577 -0.0186 -0.0578 0.0341  74  VAL   A CG2 
542  N N   . SER   A 69  ? 0.2236 0.2397 0.2711 -0.0430 -0.0803 0.0921  75  SER   A N   
543  C CA  . SER   A 69  ? 0.2449 0.2665 0.3017 -0.0624 -0.1018 0.1090  75  SER   A CA  
544  C C   . SER   A 69  ? 0.2466 0.2733 0.3190 -0.0528 -0.0952 0.1106  75  SER   A C   
545  O O   . SER   A 69  ? 0.2703 0.3002 0.3644 -0.0331 -0.0747 0.1109  75  SER   A O   
546  C CB  . SER   A 69  ? 0.2669 0.3058 0.3706 -0.0713 -0.1145 0.1407  75  SER   A CB  
547  O OG  . SER   A 69  ? 0.3602 0.3930 0.4478 -0.0828 -0.1236 0.1406  75  SER   A OG  
548  N N   . PHE   A 70  ? 0.2329 0.2536 0.2868 -0.0661 -0.1088 0.1088  76  PHE   A N   
549  C CA  . PHE   A 70  ? 0.2289 0.2542 0.2966 -0.0570 -0.1027 0.1092  76  PHE   A CA  
550  C C   . PHE   A 70  ? 0.2595 0.2904 0.3407 -0.0761 -0.1251 0.1298  76  PHE   A C   
551  O O   . PHE   A 70  ? 0.3019 0.3219 0.3592 -0.1008 -0.1476 0.1369  76  PHE   A O   
552  C CB  . PHE   A 70  ? 0.2322 0.2418 0.2622 -0.0476 -0.0910 0.0811  76  PHE   A CB  
553  C CG  . PHE   A 70  ? 0.2462 0.2368 0.2318 -0.0622 -0.0980 0.0652  76  PHE   A CG  
554  C CD1 . PHE   A 70  ? 0.2543 0.2339 0.2182 -0.0613 -0.0916 0.0515  76  PHE   A CD1 
555  C CD2 . PHE   A 70  ? 0.2695 0.2491 0.2349 -0.0765 -0.1073 0.0646  76  PHE   A CD2 
556  C CE1 . PHE   A 70  ? 0.2856 0.2427 0.2128 -0.0735 -0.0909 0.0383  76  PHE   A CE1 
557  C CE2 . PHE   A 70  ? 0.2937 0.2469 0.2154 -0.0893 -0.1057 0.0499  76  PHE   A CE2 
558  C CZ  . PHE   A 70  ? 0.2989 0.2405 0.2037 -0.0871 -0.0956 0.0370  76  PHE   A CZ  
559  N N   . SER   A 71  ? 0.2387 0.2820 0.3553 -0.0668 -0.1199 0.1412  77  SER   A N   
560  C CA  . SER   A 71  ? 0.2421 0.2928 0.3792 -0.0850 -0.1432 0.1650  77  SER   A CA  
561  C C   . SER   A 71  ? 0.2639 0.2935 0.3464 -0.0999 -0.1542 0.1484  77  SER   A C   
562  O O   . SER   A 71  ? 0.2805 0.2943 0.3221 -0.0912 -0.1391 0.1195  77  SER   A O   
563  C CB  . SER   A 71  ? 0.2397 0.3107 0.4406 -0.0688 -0.1304 0.1849  77  SER   A CB  
564  O OG  . SER   A 71  ? 0.2576 0.3197 0.4393 -0.0497 -0.1076 0.1614  77  SER   A OG  
565  N N   . LYS   A 72  ? 0.2754 0.3016 0.3577 -0.1240 -0.1811 0.1690  78  LYS   A N   
566  C CA  . LYS   A 72  ? 0.3253 0.3259 0.3535 -0.1385 -0.1878 0.1546  78  LYS   A CA  
567  C C   . LYS   A 72  ? 0.3241 0.3361 0.3711 -0.1174 -0.1701 0.1447  78  LYS   A C   
568  O O   . LYS   A 72  ? 0.3068 0.3436 0.4106 -0.1006 -0.1616 0.1590  78  LYS   A O   
569  C CB  . LYS   A 72  ? 0.3927 0.3768 0.4026 -0.1752 -0.2245 0.1801  78  LYS   A CB  
570  C CG  . LYS   A 72  ? 0.4947 0.4467 0.4507 -0.2018 -0.2401 0.1791  78  LYS   A CG  
571  C CD  . LYS   A 72  ? 0.6135 0.5298 0.5231 -0.2454 -0.2784 0.2002  78  LYS   A CD  
572  C CE  . LYS   A 72  ? 0.7271 0.6073 0.5810 -0.2698 -0.2897 0.1976  78  LYS   A CE  
573  N NZ  . LYS   A 72  ? 0.8286 0.6559 0.6118 -0.3169 -0.3249 0.2129  78  LYS   A NZ  
574  N N   . PRO   A 73  ? 0.3375 0.3285 0.3388 -0.1174 -0.1613 0.1209  79  PRO   A N   
575  C CA  . PRO   A 73  ? 0.3411 0.3417 0.3595 -0.0983 -0.1464 0.1117  79  PRO   A CA  
576  C C   . PRO   A 73  ? 0.3256 0.3443 0.3875 -0.1025 -0.1598 0.1382  79  PRO   A C   
577  O O   . PRO   A 73  ? 0.3312 0.3420 0.3832 -0.1284 -0.1857 0.1570  79  PRO   A O   
578  C CB  . PRO   A 73  ? 0.3855 0.3579 0.3501 -0.1054 -0.1406 0.0890  79  PRO   A CB  
579  C CG  . PRO   A 73  ? 0.4214 0.3684 0.3422 -0.1191 -0.1403 0.0791  79  PRO   A CG  
580  C CD  . PRO   A 73  ? 0.3753 0.3293 0.3096 -0.1351 -0.1617 0.1029  79  PRO   A CD  
581  N N   . SER   A 74  ? 0.3093 0.3483 0.4191 -0.0790 -0.1425 0.1423  80  SER   A N   
582  C CA  . SER   A 74  ? 0.3042 0.3624 0.4682 -0.0794 -0.1497 0.1701  80  SER   A CA  
583  C C   . SER   A 74  ? 0.2793 0.3433 0.4690 -0.0531 -0.1226 0.1618  80  SER   A C   
584  O O   . SER   A 74  ? 0.2731 0.3242 0.4339 -0.0366 -0.1019 0.1350  80  SER   A O   
585  C CB  . SER   A 74  ? 0.3339 0.4113 0.5545 -0.0869 -0.1623 0.2050  80  SER   A CB  
586  O OG  . SER   A 74  ? 0.3822 0.4676 0.6337 -0.0642 -0.1357 0.2032  80  SER   A OG  
587  N N   . LEU   A 75  ? 0.2548 0.3346 0.4966 -0.0519 -0.1249 0.1865  81  LEU   A N   
588  C CA  . LEU   A 75  ? 0.2625 0.3436 0.5313 -0.0300 -0.0990 0.1836  81  LEU   A CA  
589  C C   . LEU   A 75  ? 0.2755 0.3607 0.5914 -0.0118 -0.0720 0.1964  81  LEU   A C   
590  O O   . LEU   A 75  ? 0.2668 0.3718 0.6484 -0.0161 -0.0773 0.2312  81  LEU   A O   
591  C CB  . LEU   A 75  ? 0.2470 0.3434 0.5597 -0.0384 -0.1129 0.2100  81  LEU   A CB  
592  C CG  . LEU   A 75  ? 0.2855 0.3727 0.5582 -0.0472 -0.1250 0.1954  81  LEU   A CG  
593  C CD1 . LEU   A 75  ? 0.2795 0.3835 0.6034 -0.0565 -0.1404 0.2269  81  LEU   A CD1 
594  C CD2 . LEU   A 75  ? 0.3089 0.3801 0.5506 -0.0263 -0.0987 0.1640  81  LEU   A CD2 
595  N N   . ILE   A 76  ? 0.2847 0.3481 0.5699 0.0071  -0.0430 0.1715  82  ILE   A N   
596  C CA  . ILE   A 76  ? 0.3015 0.3559 0.6151 0.0242  -0.0111 0.1790  82  ILE   A CA  
597  C C   . ILE   A 76  ? 0.3368 0.3629 0.6384 0.0433  0.0238  0.1660  82  ILE   A C   
598  O O   . ILE   A 76  ? 0.3499 0.3541 0.5924 0.0450  0.0234  0.1375  82  ILE   A O   
599  C CB  . ILE   A 76  ? 0.3300 0.3726 0.6008 0.0237  -0.0108 0.1608  82  ILE   A CB  
600  C CG1 . ILE   A 76  ? 0.3359 0.4012 0.6187 0.0037  -0.0427 0.1760  82  ILE   A CG1 
601  C CG2 . ILE   A 76  ? 0.3406 0.3625 0.6227 0.0418  0.0269  0.1624  82  ILE   A CG2 
602  C CD1 . ILE   A 76  ? 0.3825 0.4379 0.6212 0.0006  -0.0465 0.1573  82  ILE   A CD1 
603  N N   . PHE   A 77  ? 0.3408 0.3628 0.6992 0.0569  0.0557  0.1885  83  PHE   A N   
604  C CA  . PHE   A 77  ? 0.3973 0.3804 0.7357 0.0738  0.0943  0.1760  83  PHE   A CA  
605  C C   . PHE   A 77  ? 0.4480 0.3840 0.7097 0.0808  0.1150  0.1457  83  PHE   A C   
606  O O   . PHE   A 77  ? 0.4609 0.3924 0.7193 0.0821  0.1221  0.1470  83  PHE   A O   
607  C CB  . PHE   A 77  ? 0.3922 0.3759 0.8123 0.0871  0.1305  0.2090  83  PHE   A CB  
608  C CG  . PHE   A 77  ? 0.4414 0.3783 0.8400 0.1028  0.1742  0.1980  83  PHE   A CG  
609  C CD1 . PHE   A 77  ? 0.4711 0.4089 0.8677 0.1020  0.1681  0.1944  83  PHE   A CD1 
610  C CD2 . PHE   A 77  ? 0.4847 0.3702 0.8587 0.1170  0.2230  0.1911  83  PHE   A CD2 
611  C CE1 . PHE   A 77  ? 0.5111 0.3999 0.8821 0.1149  0.2088  0.1839  83  PHE   A CE1 
612  C CE2 . PHE   A 77  ? 0.5271 0.3573 0.8692 0.1286  0.2655  0.1804  83  PHE   A CE2 
613  C CZ  . PHE   A 77  ? 0.5327 0.3649 0.8729 0.1273  0.2575  0.1765  83  PHE   A CZ  
614  N N   . VAL   A 78  ? 0.4808 0.3815 0.6787 0.0823  0.1192  0.1196  84  VAL   A N   
615  C CA  . VAL   A 78  ? 0.5341 0.3847 0.6522 0.0836  0.1302  0.0928  84  VAL   A CA  
616  C C   . VAL   A 78  ? 0.5881 0.3800 0.6679 0.0922  0.1659  0.0836  84  VAL   A C   
617  O O   . VAL   A 78  ? 0.5894 0.3785 0.6630 0.0910  0.1597  0.0787  84  VAL   A O   
618  C CB  . VAL   A 78  ? 0.5488 0.4074 0.6152 0.0707  0.0905  0.0697  84  VAL   A CB  
619  C CG1 . VAL   A 78  ? 0.5987 0.4031 0.5867 0.0692  0.0969  0.0468  84  VAL   A CG1 
620  C CG2 . VAL   A 78  ? 0.5237 0.4268 0.6144 0.0613  0.0616  0.0759  84  VAL   A CG2 
621  N N   . GLU   A 79  ? 0.6327 0.3711 0.6780 0.0992  0.2036  0.0798  85  GLU   A N   
622  C CA  . GLU   A 79  ? 0.6906 0.3542 0.6820 0.1050  0.2447  0.0699  85  GLU   A CA  
623  C C   . GLU   A 79  ? 0.7280 0.3527 0.6355 0.0934  0.2229  0.0442  85  GLU   A C   
624  O O   . GLU   A 79  ? 0.7285 0.3689 0.6038 0.0815  0.1821  0.0307  85  GLU   A O   
625  C CB  . GLU   A 79  ? 0.7755 0.3813 0.7278 0.1101  0.2852  0.0677  85  GLU   A CB  
626  C CG  . GLU   A 79  ? 0.8510 0.4873 0.8918 0.1232  0.3145  0.0966  85  GLU   A CG  
627  C CD  . GLU   A 79  ? 0.9725 0.6137 1.0890 0.1367  0.3515  0.1211  85  GLU   A CD  
628  O OE1 . GLU   A 79  ? 1.0319 0.6172 1.1066 0.1400  0.3808  0.1114  85  GLU   A OE1 
629  O OE2 . GLU   A 79  ? 0.9687 0.6679 1.1883 0.1427  0.3501  0.1522  85  GLU   A OE2 
630  N N   . ALA   A 80  ? 0.7529 0.3215 0.6256 0.0963  0.2524  0.0391  86  ALA   A N   
631  C CA  . ALA   A 80  ? 0.8017 0.3254 0.5946 0.0837  0.2327  0.0179  86  ALA   A CA  
632  C C   . ALA   A 80  ? 0.8588 0.3267 0.5557 0.0684  0.2167  -0.0012 86  ALA   A C   
633  O O   . ALA   A 80  ? 0.8865 0.3202 0.5562 0.0699  0.2404  -0.0012 86  ALA   A O   
634  C CB  . ALA   A 80  ? 0.8330 0.2958 0.6018 0.0893  0.2748  0.0175  86  ALA   A CB  
635  N N   . SER   A 81  ? 0.8728 0.3296 0.5215 0.0530  0.1764  -0.0148 87  SER   A N   
636  C CA  . SER   A 81  ? 0.9167 0.3236 0.4801 0.0341  0.1496  -0.0287 87  SER   A CA  
637  C C   . SER   A 81  ? 0.9569 0.3274 0.4675 0.0183  0.1213  -0.0382 87  SER   A C   
638  O O   . SER   A 81  ? 0.9413 0.3342 0.4873 0.0243  0.1233  -0.0354 87  SER   A O   
639  C CB  . SER   A 81  ? 0.8783 0.3511 0.4808 0.0308  0.1098  -0.0265 87  SER   A CB  
640  O OG  . SER   A 81  ? 0.8270 0.3707 0.4903 0.0313  0.0755  -0.0231 87  SER   A OG  
641  N N   . GLU   A 82  ? 0.9967 0.3120 0.4262 -0.0035 0.0918  -0.0470 88  GLU   A N   
642  C CA  . GLU   A 82  ? 1.0193 0.3038 0.4065 -0.0213 0.0576  -0.0518 88  GLU   A CA  
643  C C   . GLU   A 82  ? 0.9331 0.3066 0.4029 -0.0184 0.0161  -0.0459 88  GLU   A C   
644  O O   . GLU   A 82  ? 0.9494 0.3141 0.4104 -0.0275 -0.0064 -0.0467 88  GLU   A O   
645  C CB  . GLU   A 82  ? 1.1478 0.3490 0.4311 -0.0491 0.0306  -0.0574 88  GLU   A CB  
646  C CG  . GLU   A 82  ? 1.2454 0.4774 0.5425 -0.0544 0.0030  -0.0535 88  GLU   A CG  
647  C CD  . GLU   A 82  ? 1.4223 0.5790 0.6266 -0.0850 -0.0335 -0.0542 88  GLU   A CD  
648  O OE1 . GLU   A 82  ? 1.4859 0.5722 0.6180 -0.1058 -0.0494 -0.0565 88  GLU   A OE1 
649  O OE2 . GLU   A 82  ? 1.4578 0.6248 0.6615 -0.0900 -0.0490 -0.0509 88  GLU   A OE2 
650  N N   . TYR   A 83  ? 0.8372 0.2923 0.3861 -0.0057 0.0102  -0.0395 89  TYR   A N   
651  C CA  . TYR   A 83  ? 0.7562 0.2885 0.3783 -0.0027 -0.0206 -0.0343 89  TYR   A CA  
652  C C   . TYR   A 83  ? 0.6874 0.2732 0.3781 0.0145  0.0001  -0.0287 89  TYR   A C   
653  O O   . TYR   A 83  ? 0.6745 0.2960 0.4012 0.0142  -0.0189 -0.0267 89  TYR   A O   
654  C CB  . TYR   A 83  ? 0.7185 0.2960 0.3737 -0.0034 -0.0406 -0.0311 89  TYR   A CB  
655  C CG  . TYR   A 83  ? 0.7552 0.2815 0.3481 -0.0194 -0.0576 -0.0335 89  TYR   A CG  
656  C CD1 . TYR   A 83  ? 0.7832 0.2830 0.3475 -0.0387 -0.0971 -0.0315 89  TYR   A CD1 
657  C CD2 . TYR   A 83  ? 0.7811 0.2870 0.3486 -0.0166 -0.0368 -0.0350 89  TYR   A CD2 
658  C CE1 . TYR   A 83  ? 0.8349 0.2876 0.3442 -0.0566 -0.1185 -0.0300 89  TYR   A CE1 
659  C CE2 . TYR   A 83  ? 0.8318 0.2893 0.3396 -0.0329 -0.0544 -0.0363 89  TYR   A CE2 
660  C CZ  . TYR   A 83  ? 0.8694 0.2997 0.3468 -0.0539 -0.0968 -0.0334 89  TYR   A CZ  
661  O OH  . TYR   A 83  ? 0.9347 0.3144 0.3528 -0.0734 -0.1190 -0.0312 89  TYR   A OH  
662  N N   . TYR   A 84  ? 0.6542 0.2436 0.3653 0.0282  0.0380  -0.0235 90  TYR   A N   
663  C CA  . TYR   A 84  ? 0.5987 0.2390 0.3804 0.0417  0.0530  -0.0130 90  TYR   A CA  
664  C C   . TYR   A 84  ? 0.6279 0.2380 0.4149 0.0538  0.1002  -0.0059 90  TYR   A C   
665  O O   . TYR   A 84  ? 0.6590 0.2311 0.4190 0.0569  0.1280  -0.0057 90  TYR   A O   
666  C CB  . TYR   A 84  ? 0.5187 0.2285 0.3650 0.0468  0.0432  -0.0032 90  TYR   A CB  
667  C CG  . TYR   A 84  ? 0.4691 0.2147 0.3253 0.0378  0.0057  -0.0075 90  TYR   A CG  
668  C CD1 . TYR   A 84  ? 0.4675 0.2090 0.3043 0.0323  -0.0057 -0.0114 90  TYR   A CD1 
669  C CD2 . TYR   A 84  ? 0.4321 0.2156 0.3220 0.0357  -0.0142 -0.0060 90  TYR   A CD2 
670  C CE1 . TYR   A 84  ? 0.4360 0.2096 0.2903 0.0256  -0.0342 -0.0131 90  TYR   A CE1 
671  C CE2 . TYR   A 84  ? 0.4093 0.2202 0.3118 0.0287  -0.0405 -0.0086 90  TYR   A CE2 
672  C CZ  . TYR   A 84  ? 0.4092 0.2164 0.2973 0.0243  -0.0491 -0.0116 90  TYR   A CZ  
673  O OH  . TYR   A 84  ? 0.3743 0.2038 0.2788 0.0182  -0.0705 -0.0128 90  TYR   A OH  
674  N N   . PRO   A 85  ? 0.6105 0.2458 0.4471 0.0625  0.1124  0.0038  91  PRO   A N   
675  C CA  . PRO   A 85  ? 0.6235 0.2434 0.4915 0.0766  0.1600  0.0174  91  PRO   A CA  
676  C C   . PRO   A 85  ? 0.5982 0.2738 0.5380 0.0845  0.1643  0.0358  91  PRO   A C   
677  O O   . PRO   A 85  ? 0.5750 0.2994 0.5339 0.0780  0.1295  0.0358  91  PRO   A O   
678  C CB  . PRO   A 85  ? 0.6117 0.2522 0.5200 0.0812  0.1615  0.0247  91  PRO   A CB  
679  C CG  . PRO   A 85  ? 0.5843 0.2818 0.5142 0.0725  0.1132  0.0217  91  PRO   A CG  
680  C CD  . PRO   A 85  ? 0.5785 0.2613 0.4540 0.0604  0.0847  0.0061  91  PRO   A CD  
681  N N   . ALA   A 86  ? 0.5954 0.2625 0.5783 0.0975  0.2070  0.0535  92  ALA   A N   
682  C CA  . ALA   A 86  ? 0.5566 0.2773 0.6159 0.1030  0.2076  0.0760  92  ALA   A CA  
683  C C   . ALA   A 86  ? 0.4876 0.2838 0.6148 0.0978  0.1690  0.0906  92  ALA   A C   
684  O O   . ALA   A 86  ? 0.4761 0.2802 0.6227 0.0989  0.1670  0.0945  92  ALA   A O   
685  C CB  . ALA   A 86  ? 0.5590 0.2561 0.6651 0.1184  0.2625  0.0972  92  ALA   A CB  
686  N N   . ARG   A 87  ? 0.4430 0.2864 0.5924 0.0897  0.1367  0.0956  93  ARG   A N   
687  C CA  . ARG   A 87  ? 0.3914 0.2915 0.5836 0.0800  0.0994  0.1066  93  ARG   A CA  
688  C C   . ARG   A 87  ? 0.3568 0.2975 0.5799 0.0713  0.0759  0.1197  93  ARG   A C   
689  O O   . ARG   A 87  ? 0.3636 0.2921 0.5714 0.0735  0.0853  0.1162  93  ARG   A O   
690  C CB  . ARG   A 87  ? 0.4194 0.3151 0.5572 0.0708  0.0706  0.0821  93  ARG   A CB  
691  C CG  . ARG   A 87  ? 0.4325 0.3262 0.5241 0.0623  0.0488  0.0642  93  ARG   A CG  
692  C CD  . ARG   A 87  ? 0.4574 0.3229 0.4904 0.0576  0.0360  0.0409  93  ARG   A CD  
693  N NE  . ARG   A 87  ? 0.4509 0.3341 0.4673 0.0477  0.0071  0.0306  93  ARG   A NE  
694  C CZ  . ARG   A 87  ? 0.4291 0.3030 0.4216 0.0452  0.0038  0.0239  93  ARG   A CZ  
695  N NH1 . ARG   A 87  ? 0.3646 0.2524 0.3472 0.0370  -0.0191 0.0158  93  ARG   A NH1 
696  N NH2 . ARG   A 87  ? 0.4345 0.2820 0.4136 0.0511  0.0262  0.0258  93  ARG   A NH2 
697  N N   . TYR   A 88  ? 0.3208 0.3035 0.5765 0.0589  0.0436  0.1328  94  TYR   A N   
698  C CA  . TYR   A 88  ? 0.3087 0.3195 0.5746 0.0457  0.0171  0.1414  94  TYR   A CA  
699  C C   . TYR   A 88  ? 0.2939 0.2975 0.4952 0.0365  -0.0049 0.1131  94  TYR   A C   
700  O O   . TYR   A 88  ? 0.2890 0.2910 0.4685 0.0325  -0.0166 0.1012  94  TYR   A O   
701  C CB  . TYR   A 88  ? 0.3095 0.3571 0.6282 0.0316  -0.0092 0.1698  94  TYR   A CB  
702  C CG  . TYR   A 88  ? 0.3325 0.3956 0.7341 0.0380  0.0068  0.2064  94  TYR   A CG  
703  C CD1 . TYR   A 88  ? 0.3453 0.4249 0.7905 0.0341  0.0034  0.2303  94  TYR   A CD1 
704  C CD2 . TYR   A 88  ? 0.3488 0.4091 0.7909 0.0487  0.0273  0.2192  94  TYR   A CD2 
705  C CE1 . TYR   A 88  ? 0.3378 0.4341 0.8734 0.0400  0.0184  0.2693  94  TYR   A CE1 
706  C CE2 . TYR   A 88  ? 0.3367 0.4118 0.8672 0.0555  0.0453  0.2569  94  TYR   A CE2 
707  C CZ  . TYR   A 88  ? 0.3415 0.4353 0.9223 0.0516  0.0412  0.2831  94  TYR   A CZ  
708  O OH  . TYR   A 88  ? 0.3466 0.4567 1.0284 0.0589  0.0602  0.3252  94  TYR   A OH  
709  N N   . GLN   A 89  ? 0.2639 0.2619 0.4399 0.0345  -0.0075 0.1037  95  GLN   A N   
710  C CA  . GLN   A 89  ? 0.2417 0.2349 0.3690 0.0259  -0.0260 0.0815  95  GLN   A CA  
711  C C   . GLN   A 89  ? 0.2255 0.2430 0.3634 0.0086  -0.0511 0.0927  95  GLN   A C   
712  O O   . GLN   A 89  ? 0.2217 0.2529 0.3890 0.0041  -0.0542 0.1115  95  GLN   A O   
713  C CB  . GLN   A 89  ? 0.2413 0.2112 0.3332 0.0318  -0.0156 0.0659  95  GLN   A CB  
714  C CG  . GLN   A 89  ? 0.2536 0.2207 0.3070 0.0232  -0.0340 0.0470  95  GLN   A CG  
715  C CD  . GLN   A 89  ? 0.3063 0.2454 0.3233 0.0285  -0.0265 0.0320  95  GLN   A CD  
716  O OE1 . GLN   A 89  ? 0.3390 0.2500 0.3412 0.0370  -0.0081 0.0301  95  GLN   A OE1 
717  N NE2 . GLN   A 89  ? 0.2922 0.2322 0.2901 0.0220  -0.0399 0.0215  95  GLN   A NE2 
718  N N   . SER   A 90  ? 0.2048 0.2227 0.3177 -0.0027 -0.0677 0.0830  96  SER   A N   
719  C CA  . SER   A 90  ? 0.2064 0.2326 0.3121 -0.0228 -0.0892 0.0915  96  SER   A CA  
720  C C   . SER   A 90  ? 0.2196 0.2335 0.2866 -0.0282 -0.0914 0.0744  96  SER   A C   
721  O O   . SER   A 90  ? 0.2259 0.2279 0.2742 -0.0170 -0.0802 0.0556  96  SER   A O   
722  C CB  . SER   A 90  ? 0.2332 0.2579 0.3281 -0.0337 -0.1010 0.0916  96  SER   A CB  
723  O OG  . SER   A 90  ? 0.2705 0.2803 0.3346 -0.0278 -0.0935 0.0680  96  SER   A OG  
724  N N   . HIS   A 91  ? 0.2202 0.2339 0.2762 -0.0469 -0.1067 0.0834  97  HIS   A N   
725  C CA  . HIS   A 91  ? 0.2402 0.2388 0.2596 -0.0543 -0.1070 0.0694  97  HIS   A CA  
726  C C   . HIS   A 91  ? 0.2329 0.2341 0.2592 -0.0399 -0.0950 0.0626  97  HIS   A C   
727  O O   . HIS   A 91  ? 0.2415 0.2305 0.2436 -0.0373 -0.0888 0.0456  97  HIS   A O   
728  C CB  . HIS   A 91  ? 0.2667 0.2467 0.2539 -0.0550 -0.1003 0.0492  97  HIS   A CB  
729  C CG  . HIS   A 91  ? 0.3127 0.2824 0.2832 -0.0714 -0.1096 0.0548  97  HIS   A CG  
730  N ND1 . HIS   A 91  ? 0.3817 0.3268 0.3115 -0.0950 -0.1177 0.0566  97  HIS   A ND1 
731  C CD2 . HIS   A 91  ? 0.3342 0.3105 0.3190 -0.0693 -0.1122 0.0601  97  HIS   A CD2 
732  C CE1 . HIS   A 91  ? 0.3940 0.3293 0.3112 -0.1072 -0.1254 0.0628  97  HIS   A CE1 
733  N NE2 . HIS   A 91  ? 0.3708 0.3276 0.3239 -0.0915 -0.1228 0.0653  97  HIS   A NE2 
734  N N   . LEU   A 92  ? 0.2211 0.2357 0.2826 -0.0307 -0.0898 0.0774  98  LEU   A N   
735  C CA  . LEU   A 92  ? 0.2239 0.2348 0.2869 -0.0175 -0.0755 0.0714  98  LEU   A CA  
736  C C   . LEU   A 92  ? 0.2157 0.2355 0.2917 -0.0261 -0.0827 0.0858  98  LEU   A C   
737  O O   . LEU   A 92  ? 0.2130 0.2471 0.3201 -0.0366 -0.0951 0.1098  98  LEU   A O   
738  C CB  . LEU   A 92  ? 0.2151 0.2238 0.3028 0.0001  -0.0559 0.0766  98  LEU   A CB  
739  C CG  . LEU   A 92  ? 0.2407 0.2325 0.3181 0.0138  -0.0360 0.0690  98  LEU   A CG  
740  C CD1 . LEU   A 92  ? 0.2556 0.2268 0.2884 0.0156  -0.0375 0.0453  98  LEU   A CD1 
741  C CD2 . LEU   A 92  ? 0.2595 0.2389 0.3584 0.0286  -0.0104 0.0779  98  LEU   A CD2 
742  N N   . MET   A 93  ? 0.2092 0.2207 0.2657 -0.0222 -0.0765 0.0738  99  MET   A N   
743  C CA  . MET   A 93  ? 0.2114 0.2299 0.2782 -0.0299 -0.0828 0.0858  99  MET   A CA  
744  C C   . MET   A 93  ? 0.2215 0.2373 0.3009 -0.0130 -0.0630 0.0852  99  MET   A C   
745  O O   . MET   A 93  ? 0.2494 0.2485 0.3005 -0.0030 -0.0520 0.0657  99  MET   A O   
746  C CB  . MET   A 93  ? 0.2340 0.2394 0.2597 -0.0424 -0.0913 0.0708  99  MET   A CB  
747  C CG  . MET   A 93  ? 0.2770 0.2723 0.2777 -0.0616 -0.1056 0.0702  99  MET   A CG  
748  S SD  . MET   A 93  ? 0.3455 0.3136 0.2955 -0.0726 -0.1022 0.0494  99  MET   A SD  
749  C CE  . MET   A 93  ? 0.3085 0.2743 0.2603 -0.0499 -0.0833 0.0277  99  MET   A CE  
750  N N   . LEU   A 94  ? 0.1950 0.2235 0.3162 -0.0110 -0.0585 0.1078  100 LEU   A N   
751  C CA  . LEU   A 94  ? 0.2107 0.2292 0.3392 0.0052  -0.0339 0.1070  100 LEU   A CA  
752  C C   . LEU   A 94  ? 0.2161 0.2387 0.3431 -0.0002 -0.0391 0.1099  100 LEU   A C   
753  O O   . LEU   A 94  ? 0.2201 0.2588 0.3647 -0.0161 -0.0600 0.1256  100 LEU   A O   
754  C CB  . LEU   A 94  ? 0.2133 0.2396 0.4001 0.0154  -0.0151 0.1329  100 LEU   A CB  
755  C CG  . LEU   A 94  ? 0.2614 0.2805 0.4585 0.0244  -0.0014 0.1338  100 LEU   A CG  
756  C CD1 . LEU   A 94  ? 0.2592 0.2808 0.5201 0.0371  0.0267  0.1612  100 LEU   A CD1 
757  C CD2 . LEU   A 94  ? 0.3029 0.2889 0.4428 0.0342  0.0134  0.1049  100 LEU   A CD2 
758  N N   . ALA   A 95  ? 0.2163 0.2210 0.3228 0.0116  -0.0204 0.0978  101 ALA   A N   
759  C CA  . ALA   A 95  ? 0.2346 0.2413 0.3412 0.0097  -0.0206 0.1003  101 ALA   A CA  
760  C C   . ALA   A 95  ? 0.2529 0.2398 0.3641 0.0265  0.0109  0.1024  101 ALA   A C   
761  O O   . ALA   A 95  ? 0.2751 0.2365 0.3662 0.0372  0.0308  0.0933  101 ALA   A O   
762  C CB  . ALA   A 95  ? 0.2600 0.2563 0.3181 0.0036  -0.0321 0.0769  101 ALA   A CB  
763  N N   . VAL   A 96  ? 0.2493 0.2423 0.3829 0.0274  0.0169  0.1148  102 VAL   A N   
764  C CA  . VAL   A 96  ? 0.2827 0.2495 0.4116 0.0421  0.0499  0.1151  102 VAL   A CA  
765  C C   . VAL   A 96  ? 0.3429 0.2835 0.4052 0.0412  0.0466  0.0881  102 VAL   A C   
766  O O   . VAL   A 96  ? 0.3528 0.3065 0.4056 0.0323  0.0271  0.0828  102 VAL   A O   
767  C CB  . VAL   A 96  ? 0.2697 0.2541 0.4553 0.0438  0.0585  0.1416  102 VAL   A CB  
768  C CG1 . VAL   A 96  ? 0.3005 0.2505 0.4712 0.0585  0.0965  0.1389  102 VAL   A CG1 
769  C CG2 . VAL   A 96  ? 0.2385 0.2489 0.5008 0.0435  0.0595  0.1742  102 VAL   A CG2 
770  N N   . GLY   A 97  ? 0.3698 0.2711 0.3863 0.0482  0.0635  0.0730  103 GLY   A N   
771  C CA  . GLY   A 97  ? 0.4007 0.2745 0.3574 0.0446  0.0556  0.0522  103 GLY   A CA  
772  C C   . GLY   A 97  ? 0.4354 0.2592 0.3388 0.0480  0.0701  0.0398  103 GLY   A C   
773  O O   . GLY   A 97  ? 0.4528 0.2654 0.3622 0.0531  0.0847  0.0433  103 GLY   A O   
774  N N   . HIS   A 98  ? 0.4471 0.2360 0.2958 0.0434  0.0661  0.0271  104 HIS   A N   
775  C CA  . HIS   A 98  ? 0.4864 0.2170 0.2707 0.0410  0.0744  0.0162  104 HIS   A CA  
776  C C   . HIS   A 98  ? 0.4760 0.2095 0.2458 0.0330  0.0473  0.0068  104 HIS   A C   
777  O O   . HIS   A 98  ? 0.4417 0.2082 0.2292 0.0265  0.0184  0.0035  104 HIS   A O   
778  C CB  . HIS   A 98  ? 0.5280 0.2160 0.2552 0.0344  0.0733  0.0091  104 HIS   A CB  
779  C CG  . HIS   A 98  ? 0.6094 0.2265 0.2574 0.0260  0.0768  -0.0006 104 HIS   A CG  
780  N ND1 . HIS   A 98  ? 0.6846 0.2461 0.2966 0.0315  0.1158  0.0000  104 HIS   A ND1 
781  C CD2 . HIS   A 98  ? 0.6502 0.2437 0.2534 0.0112  0.0449  -0.0087 104 HIS   A CD2 
782  C CE1 . HIS   A 98  ? 0.7397 0.2385 0.2730 0.0177  0.1055  -0.0100 104 HIS   A CE1 
783  N NE2 . HIS   A 98  ? 0.7330 0.2506 0.2609 0.0045  0.0601  -0.0140 104 HIS   A NE2 
784  N N   . SER   A 99  ? 0.5032 0.1942 0.2359 0.0329  0.0592  0.0025  105 SER   A N   
785  C CA  . SER   A 99  ? 0.5314 0.2121 0.2410 0.0243  0.0355  -0.0055 105 SER   A CA  
786  C C   . SER   A 99  ? 0.6143 0.2217 0.2549 0.0205  0.0533  -0.0113 105 SER   A C   
787  O O   . SER   A 99  ? 0.6484 0.2240 0.2776 0.0292  0.0919  -0.0078 105 SER   A O   
788  C CB  . SER   A 99  ? 0.5077 0.2407 0.2745 0.0285  0.0260  -0.0017 105 SER   A CB  
789  O OG  . SER   A 99  ? 0.5174 0.2519 0.3096 0.0390  0.0543  0.0066  105 SER   A OG  
790  N N   . GLU   A 100 ? 0.6464 0.2243 0.2430 0.0066  0.0258  -0.0182 106 GLU   A N   
791  C CA  . GLU   A 100 ? 0.7242 0.2270 0.2450 -0.0034 0.0316  -0.0243 106 GLU   A CA  
792  C C   . GLU   A 100 ? 0.7385 0.2575 0.2709 -0.0112 -0.0008 -0.0259 106 GLU   A C   
793  O O   . GLU   A 100 ? 0.7068 0.2848 0.2949 -0.0111 -0.0283 -0.0229 106 GLU   A O   
794  C CB  . GLU   A 100 ? 0.8113 0.2414 0.2457 -0.0208 0.0233  -0.0280 106 GLU   A CB  
795  C CG  . GLU   A 100 ? 0.8826 0.2883 0.2998 -0.0128 0.0604  -0.0268 106 GLU   A CG  
796  C CD  . GLU   A 100 ? 0.9931 0.3333 0.3289 -0.0306 0.0499  -0.0293 106 GLU   A CD  
797  O OE1 . GLU   A 100 ? 1.0550 0.3242 0.3083 -0.0516 0.0319  -0.0333 106 GLU   A OE1 
798  O OE2 . GLU   A 100 ? 1.0083 0.3657 0.3608 -0.0256 0.0576  -0.0262 106 GLU   A OE2 
799  N N   . PRO   A 101 ? 0.7916 0.2565 0.2725 -0.0182 0.0039  -0.0302 107 PRO   A N   
800  C CA  . PRO   A 101 ? 0.7748 0.2630 0.2794 -0.0230 -0.0240 -0.0300 107 PRO   A CA  
801  C C   . PRO   A 101 ? 0.7362 0.2560 0.2668 -0.0354 -0.0722 -0.0254 107 PRO   A C   
802  O O   . PRO   A 101 ? 0.6958 0.2757 0.2930 -0.0295 -0.0865 -0.0223 107 PRO   A O   
803  C CB  . PRO   A 101 ? 0.8465 0.2517 0.2695 -0.0343 -0.0144 -0.0354 107 PRO   A CB  
804  C CG  . PRO   A 101 ? 0.9024 0.2397 0.2611 -0.0328 0.0274  -0.0393 107 PRO   A CG  
805  C CD  . PRO   A 101 ? 0.8411 0.2273 0.2527 -0.0181 0.0442  -0.0347 107 PRO   A CD  
806  N N   . GLY   A 102 ? 0.7427 0.2223 0.2260 -0.0523 -0.0948 -0.0229 108 GLY   A N   
807  C CA  . GLY   A 102 ? 0.7118 0.2197 0.2293 -0.0639 -0.1384 -0.0137 108 GLY   A CA  
808  C C   . GLY   A 102 ? 0.6304 0.2147 0.2299 -0.0505 -0.1378 -0.0105 108 GLY   A C   
809  O O   . GLY   A 102 ? 0.6139 0.2272 0.2561 -0.0566 -0.1664 -0.0019 108 GLY   A O   
810  N N   . ASP   A 103 ? 0.5849 0.1992 0.2085 -0.0332 -0.1043 -0.0155 109 ASP   A N   
811  C CA  . ASP   A 103 ? 0.5172 0.1963 0.2083 -0.0227 -0.1017 -0.0133 109 ASP   A CA  
812  C C   . ASP   A 103 ? 0.4617 0.1917 0.2125 -0.0155 -0.1039 -0.0126 109 ASP   A C   
813  O O   . ASP   A 103 ? 0.4246 0.1987 0.2236 -0.0115 -0.1058 -0.0107 109 ASP   A O   
814  C CB  . ASP   A 103 ? 0.5239 0.2137 0.2192 -0.0106 -0.0706 -0.0152 109 ASP   A CB  
815  C CG  . ASP   A 103 ? 0.5755 0.2285 0.2271 -0.0170 -0.0697 -0.0148 109 ASP   A CG  
816  O OD1 . ASP   A 103 ? 0.5709 0.2157 0.2146 -0.0292 -0.0978 -0.0112 109 ASP   A OD1 
817  O OD2 . ASP   A 103 ? 0.6036 0.2345 0.2318 -0.0101 -0.0399 -0.0162 109 ASP   A OD2 
818  N N   . CYS   A 104 ? 0.4679 0.1875 0.2118 -0.0152 -0.1029 -0.0144 110 CYS   A N   
819  C CA  . CYS   A 104 ? 0.4260 0.1909 0.2233 -0.0092 -0.1043 -0.0136 110 CYS   A CA  
820  C C   . CYS   A 104 ? 0.4043 0.1916 0.2403 -0.0154 -0.1275 -0.0081 110 CYS   A C   
821  O O   . CYS   A 104 ? 0.4202 0.1818 0.2416 -0.0269 -0.1511 -0.0022 110 CYS   A O   
822  C CB  . CYS   A 104 ? 0.4428 0.1897 0.2250 -0.0088 -0.1012 -0.0156 110 CYS   A CB  
823  S SG  . CYS   A 104 ? 0.5023 0.2310 0.2617 0.0023  -0.0647 -0.0186 110 CYS   A SG  
824  N N   . GLY   A 105 ? 0.3597 0.1889 0.2431 -0.0094 -0.1202 -0.0080 111 GLY   A N   
825  C CA  . GLY   A 105 ? 0.3495 0.1968 0.2756 -0.0132 -0.1327 -0.0018 111 GLY   A CA  
826  C C   . GLY   A 105 ? 0.3409 0.2025 0.2840 -0.0127 -0.1282 -0.0005 111 GLY   A C   
827  O O   . GLY   A 105 ? 0.3177 0.1963 0.3024 -0.0133 -0.1281 0.0041  111 GLY   A O   
828  N N   . GLY   A 106 ? 0.3404 0.1928 0.2534 -0.0112 -0.1210 -0.0039 112 GLY   A N   
829  C CA  . GLY   A 106 ? 0.3088 0.1755 0.2357 -0.0105 -0.1152 -0.0033 112 GLY   A CA  
830  C C   . GLY   A 106 ? 0.2840 0.1793 0.2369 -0.0064 -0.0982 -0.0069 112 GLY   A C   
831  O O   . GLY   A 106 ? 0.2822 0.1852 0.2286 -0.0033 -0.0885 -0.0099 112 GLY   A O   
832  N N   . ILE   A 107 ? 0.2623 0.1682 0.2428 -0.0082 -0.0947 -0.0050 113 ILE   A N   
833  C CA  . ILE   A 107 ? 0.2473 0.1665 0.2399 -0.0087 -0.0780 -0.0088 113 ILE   A CA  
834  C C   . ILE   A 107 ? 0.2354 0.1605 0.2092 -0.0097 -0.0695 -0.0116 113 ILE   A C   
835  O O   . ILE   A 107 ? 0.2490 0.1717 0.2167 -0.0092 -0.0720 -0.0103 113 ILE   A O   
836  C CB  . ILE   A 107 ? 0.2648 0.1834 0.2945 -0.0105 -0.0716 -0.0049 113 ILE   A CB  
837  C CG1 . ILE   A 107 ? 0.2757 0.1926 0.3330 -0.0097 -0.0756 0.0000  113 ILE   A CG1 
838  C CG2 . ILE   A 107 ? 0.2745 0.1922 0.3015 -0.0140 -0.0502 -0.0100 113 ILE   A CG2 
839  C CD1 . ILE   A 107 ? 0.2905 0.2058 0.4012 -0.0100 -0.0692 0.0103  113 ILE   A CD1 
840  N N   . LEU   A 108 ? 0.2208 0.1521 0.1869 -0.0133 -0.0615 -0.0133 114 LEU   A N   
841  C CA  . LEU   A 108 ? 0.2306 0.1665 0.1836 -0.0188 -0.0571 -0.0121 114 LEU   A CA  
842  C C   . LEU   A 108 ? 0.2495 0.1748 0.1995 -0.0282 -0.0461 -0.0157 114 LEU   A C   
843  O O   . LEU   A 108 ? 0.2588 0.1760 0.2091 -0.0315 -0.0397 -0.0179 114 LEU   A O   
844  C CB  . LEU   A 108 ? 0.2367 0.1810 0.1832 -0.0208 -0.0598 -0.0069 114 LEU   A CB  
845  C CG  . LEU   A 108 ? 0.2532 0.2020 0.1917 -0.0310 -0.0614 -0.0001 114 LEU   A CG  
846  C CD1 . LEU   A 108 ? 0.2594 0.2127 0.2002 -0.0276 -0.0614 0.0032  114 LEU   A CD1 
847  C CD2 . LEU   A 108 ? 0.2607 0.2203 0.2062 -0.0335 -0.0677 0.0110  114 LEU   A CD2 
848  N N   . ARG   A 109 ? 0.2563 0.1762 0.1996 -0.0329 -0.0410 -0.0165 115 ARG   A N   
849  C CA  . ARG   A 109 ? 0.2857 0.1845 0.2183 -0.0427 -0.0251 -0.0209 115 ARG   A CA  
850  C C   . ARG   A 109 ? 0.3108 0.2011 0.2138 -0.0557 -0.0265 -0.0196 115 ARG   A C   
851  O O   . ARG   A 109 ? 0.3006 0.2046 0.2075 -0.0528 -0.0355 -0.0155 115 ARG   A O   
852  C CB  . ARG   A 109 ? 0.3205 0.2141 0.2785 -0.0368 -0.0149 -0.0219 115 ARG   A CB  
853  C CG  . ARG   A 109 ? 0.3944 0.2917 0.3903 -0.0277 -0.0146 -0.0187 115 ARG   A CG  
854  C CD  . ARG   A 109 ? 0.4373 0.3295 0.4649 -0.0248 -0.0054 -0.0147 115 ARG   A CD  
855  N NE  . ARG   A 109 ? 0.5074 0.3739 0.5342 -0.0305 0.0244  -0.0183 115 ARG   A NE  
856  C CZ  . ARG   A 109 ? 0.5220 0.3764 0.5797 -0.0278 0.0430  -0.0151 115 ARG   A CZ  
857  N NH1 . ARG   A 109 ? 0.5290 0.3501 0.5758 -0.0338 0.0767  -0.0196 115 ARG   A NH1 
858  N NH2 . ARG   A 109 ? 0.5135 0.3842 0.6122 -0.0201 0.0295  -0.0063 115 ARG   A NH2 
859  N N   . CYS   A 110 ? 0.3447 0.2061 0.2159 -0.0713 -0.0159 -0.0228 116 CYS   A N   
860  C CA  . CYS   A 110 ? 0.3970 0.2390 0.2314 -0.0891 -0.0185 -0.0210 116 CYS   A CA  
861  C C   . CYS   A 110 ? 0.4608 0.2640 0.2764 -0.0956 0.0088  -0.0302 116 CYS   A C   
862  O O   . CYS   A 110 ? 0.4377 0.2384 0.2822 -0.0836 0.0275  -0.0345 116 CYS   A O   
863  C CB  . CYS   A 110 ? 0.4168 0.2457 0.2168 -0.1079 -0.0320 -0.0144 116 CYS   A CB  
864  S SG  . CYS   A 110 ? 0.4554 0.2417 0.2200 -0.1194 -0.0127 -0.0227 116 CYS   A SG  
865  N N   . GLN   A 111 ? 0.5321 0.3024 0.3023 -0.1151 0.0120  -0.0313 117 GLN   A N   
866  C CA  . GLN   A 111 ? 0.5903 0.3146 0.3368 -0.1220 0.0439  -0.0405 117 GLN   A CA  
867  C C   . GLN   A 111 ? 0.6196 0.3051 0.3492 -0.1256 0.0725  -0.0475 117 GLN   A C   
868  O O   . GLN   A 111 ? 0.6569 0.3104 0.3914 -0.1225 0.1080  -0.0536 117 GLN   A O   
869  C CB  . GLN   A 111 ? 0.6811 0.3669 0.3670 -0.1473 0.0397  -0.0404 117 GLN   A CB  
870  C CG  . GLN   A 111 ? 0.7864 0.4428 0.4131 -0.1740 0.0214  -0.0352 117 GLN   A CG  
871  C CD  . GLN   A 111 ? 0.9115 0.5285 0.4779 -0.2026 0.0095  -0.0313 117 GLN   A CD  
872  O OE1 . GLN   A 111 ? 0.9312 0.5650 0.4913 -0.2165 -0.0267 -0.0163 117 GLN   A OE1 
873  N NE2 . GLN   A 111 ? 0.9570 0.5176 0.4800 -0.2131 0.0405  -0.0426 117 GLN   A NE2 
874  N N   . HIS   A 112 ? 0.5969 0.2837 0.3108 -0.1315 0.0601  -0.0450 118 HIS   A N   
875  C CA  . HIS   A 112 ? 0.6071 0.2542 0.3005 -0.1361 0.0875  -0.0511 118 HIS   A CA  
876  C C   . HIS   A 112 ? 0.5597 0.2392 0.3223 -0.1111 0.0980  -0.0500 118 HIS   A C   
877  O O   . HIS   A 112 ? 0.5858 0.2341 0.3460 -0.1111 0.1272  -0.0538 118 HIS   A O   
878  C CB  . HIS   A 112 ? 0.6520 0.2742 0.2859 -0.1593 0.0700  -0.0482 118 HIS   A CB  
879  C CG  . HIS   A 112 ? 0.7331 0.3207 0.2988 -0.1888 0.0515  -0.0443 118 HIS   A CG  
880  N ND1 . HIS   A 112 ? 0.7405 0.3646 0.3134 -0.1959 0.0088  -0.0302 118 HIS   A ND1 
881  C CD2 . HIS   A 112 ? 0.8143 0.3293 0.3034 -0.2148 0.0704  -0.0506 118 HIS   A CD2 
882  C CE1 . HIS   A 112 ? 0.7983 0.3780 0.3069 -0.2256 -0.0021 -0.0263 118 HIS   A CE1 
883  N NE2 . HIS   A 112 ? 0.8441 0.3540 0.2934 -0.2393 0.0332  -0.0396 118 HIS   A NE2 
884  N N   . GLY   A 113 ? 0.4856 0.2217 0.3056 -0.0922 0.0746  -0.0438 119 GLY   A N   
885  C CA  . GLY   A 113 ? 0.4385 0.2017 0.3195 -0.0727 0.0774  -0.0401 119 GLY   A CA  
886  C C   . GLY   A 113 ? 0.3748 0.1825 0.2767 -0.0636 0.0442  -0.0348 119 GLY   A C   
887  O O   . GLY   A 113 ? 0.3746 0.2013 0.2622 -0.0664 0.0213  -0.0321 119 GLY   A O   
888  N N   . VAL   A 114 ? 0.3455 0.1670 0.2832 -0.0528 0.0437  -0.0319 120 VAL   A N   
889  C CA  . VAL   A 114 ? 0.3234 0.1787 0.2772 -0.0444 0.0165  -0.0276 120 VAL   A CA  
890  C C   . VAL   A 114 ? 0.3303 0.1855 0.2466 -0.0543 0.0042  -0.0279 120 VAL   A C   
891  O O   . VAL   A 114 ? 0.3535 0.1845 0.2456 -0.0641 0.0161  -0.0304 120 VAL   A O   
892  C CB  . VAL   A 114 ? 0.3159 0.1810 0.3165 -0.0328 0.0175  -0.0231 120 VAL   A CB  
893  C CG1 . VAL   A 114 ? 0.3007 0.1900 0.3043 -0.0271 -0.0079 -0.0204 120 VAL   A CG1 
894  C CG2 . VAL   A 114 ? 0.3052 0.1771 0.3535 -0.0243 0.0190  -0.0161 120 VAL   A CG2 
895  N N   . VAL   A 115 ? 0.3126 0.1925 0.2272 -0.0521 -0.0181 -0.0232 121 VAL   A N   
896  C CA  . VAL   A 115 ? 0.3116 0.1977 0.2063 -0.0604 -0.0324 -0.0177 121 VAL   A CA  
897  C C   . VAL   A 115 ? 0.2876 0.1943 0.2052 -0.0491 -0.0420 -0.0147 121 VAL   A C   
898  O O   . VAL   A 115 ? 0.2948 0.1994 0.2031 -0.0550 -0.0456 -0.0119 121 VAL   A O   
899  C CB  . VAL   A 115 ? 0.3353 0.2339 0.2231 -0.0650 -0.0467 -0.0102 121 VAL   A CB  
900  C CG1 . VAL   A 115 ? 0.3396 0.2521 0.2276 -0.0706 -0.0634 0.0018  121 VAL   A CG1 
901  C CG2 . VAL   A 115 ? 0.3597 0.2331 0.2162 -0.0805 -0.0404 -0.0121 121 VAL   A CG2 
902  N N   . GLY   A 116 ? 0.2559 0.1780 0.1979 -0.0350 -0.0469 -0.0148 122 GLY   A N   
903  C CA  . GLY   A 116 ? 0.2489 0.1824 0.2043 -0.0257 -0.0549 -0.0127 122 GLY   A CA  
904  C C   . GLY   A 116 ? 0.2405 0.1766 0.2085 -0.0151 -0.0608 -0.0133 122 GLY   A C   
905  O O   . GLY   A 116 ? 0.2357 0.1677 0.2094 -0.0143 -0.0597 -0.0145 122 GLY   A O   
906  N N   . ILE   A 117 ? 0.2352 0.1728 0.2038 -0.0087 -0.0674 -0.0118 123 ILE   A N   
907  C CA  . ILE   A 117 ? 0.2451 0.1727 0.2109 -0.0033 -0.0752 -0.0120 123 ILE   A CA  
908  C C   . ILE   A 117 ? 0.2464 0.1686 0.1944 0.0017  -0.0736 -0.0100 123 ILE   A C   
909  O O   . ILE   A 117 ? 0.2355 0.1646 0.1861 0.0033  -0.0688 -0.0070 123 ILE   A O   
910  C CB  . ILE   A 117 ? 0.2679 0.1876 0.2472 -0.0029 -0.0836 -0.0116 123 ILE   A CB  
911  C CG1 . ILE   A 117 ? 0.2857 0.2095 0.2678 -0.0020 -0.0815 -0.0121 123 ILE   A CG1 
912  C CG2 . ILE   A 117 ? 0.2865 0.2066 0.2945 -0.0057 -0.0827 -0.0093 123 ILE   A CG2 
913  C CD1 . ILE   A 117 ? 0.3086 0.2217 0.3031 -0.0018 -0.0939 -0.0096 123 ILE   A CD1 
914  N N   . VAL   A 118 ? 0.2485 0.1542 0.1786 0.0037  -0.0754 -0.0103 124 VAL   A N   
915  C CA  . VAL   A 118 ? 0.2554 0.1449 0.1644 0.0090  -0.0661 -0.0086 124 VAL   A CA  
916  C C   . VAL   A 118 ? 0.2782 0.1537 0.1786 0.0108  -0.0665 -0.0098 124 VAL   A C   
917  O O   . VAL   A 118 ? 0.2829 0.1454 0.1770 0.0065  -0.0803 -0.0123 124 VAL   A O   
918  C CB  . VAL   A 118 ? 0.2980 0.1586 0.1760 0.0083  -0.0671 -0.0101 124 VAL   A CB  
919  C CG1 . VAL   A 118 ? 0.3425 0.1736 0.1915 0.0134  -0.0501 -0.0093 124 VAL   A CG1 
920  C CG2 . VAL   A 118 ? 0.2999 0.1745 0.1872 0.0076  -0.0649 -0.0085 124 VAL   A CG2 
921  N N   . SER   A 119 ? 0.2868 0.1640 0.1910 0.0165  -0.0518 -0.0056 125 SER   A N   
922  C CA  . SER   A 119 ? 0.3099 0.1748 0.2086 0.0188  -0.0490 -0.0063 125 SER   A CA  
923  C C   . SER   A 119 ? 0.3584 0.1935 0.2364 0.0255  -0.0273 -0.0038 125 SER   A C   
924  O O   . SER   A 119 ? 0.4065 0.2086 0.2556 0.0250  -0.0249 -0.0081 125 SER   A O   
925  C CB  . SER   A 119 ? 0.3026 0.1997 0.2354 0.0186  -0.0505 -0.0015 125 SER   A CB  
926  O OG  . SER   A 119 ? 0.3157 0.2042 0.2478 0.0215  -0.0471 -0.0012 125 SER   A OG  
927  N N   . THR   A 120 ? 0.3683 0.2108 0.2614 0.0312  -0.0094 0.0043  126 THR   A N   
928  C CA  . THR   A 120 ? 0.4193 0.2291 0.2992 0.0395  0.0202  0.0088  126 THR   A CA  
929  C C   . THR   A 120 ? 0.4374 0.2415 0.3184 0.0434  0.0365  0.0144  126 THR   A C   
930  O O   . THR   A 120 ? 0.4113 0.2424 0.3072 0.0394  0.0221  0.0154  126 THR   A O   
931  C CB  . THR   A 120 ? 0.4335 0.2642 0.3578 0.0464  0.0338  0.0213  126 THR   A CB  
932  O OG1 . THR   A 120 ? 0.4758 0.2628 0.3813 0.0547  0.0671  0.0236  126 THR   A OG1 
933  C CG2 . THR   A 120 ? 0.4065 0.2821 0.3880 0.0474  0.0331  0.0385  126 THR   A CG2 
934  N N   . GLY   A 121 ? 0.4803 0.2451 0.3439 0.0510  0.0693  0.0181  127 GLY   A N   
935  C CA  . GLY   A 121 ? 0.5161 0.2747 0.3873 0.0562  0.0899  0.0257  127 GLY   A CA  
936  C C   . GLY   A 121 ? 0.5771 0.2866 0.4342 0.0663  0.1352  0.0315  127 GLY   A C   
937  O O   . GLY   A 121 ? 0.6057 0.2811 0.4407 0.0686  0.1513  0.0281  127 GLY   A O   
938  N N   . GLY   A 122 ? 0.6067 0.3064 0.4721 0.0720  0.1584  0.0395  128 GLY   A N   
939  C CA  . GLY   A 122 ? 0.6677 0.3128 0.5196 0.0826  0.2102  0.0460  128 GLY   A CA  
940  C C   . GLY   A 122 ? 0.6603 0.3351 0.5839 0.0934  0.2336  0.0688  128 GLY   A C   
941  O O   . GLY   A 122 ? 0.6142 0.3561 0.6102 0.0926  0.2093  0.0841  128 GLY   A O   
942  N N   . ASN   A 123 ? 0.7005 0.3216 0.6026 0.1017  0.2804  0.0726  129 ASN   A N   
943  C CA  . ASN   A 123 ? 0.6822 0.3268 0.6597 0.1133  0.3084  0.0979  129 ASN   A CA  
944  C C   . ASN   A 123 ? 0.6348 0.3355 0.6462 0.1072  0.2731  0.1035  129 ASN   A C   
945  O O   . ASN   A 123 ? 0.6144 0.3586 0.7111 0.1131  0.2784  0.1298  129 ASN   A O   
946  C CB  . ASN   A 123 ? 0.6738 0.3565 0.7495 0.1239  0.3245  0.1257  129 ASN   A CB  
947  C CG  . ASN   A 123 ? 0.7841 0.4080 0.8356 0.1326  0.3695  0.1234  129 ASN   A CG  
948  O OD1 . ASN   A 123 ? 0.8633 0.4083 0.8518 0.1375  0.4167  0.1141  129 ASN   A OD1 
949  N ND2 . ASN   A 123 ? 0.7714 0.4265 0.8683 0.1338  0.3585  0.1322  129 ASN   A ND2 
950  N N   . GLY   A 124 ? 0.6144 0.3098 0.5619 0.0949  0.2394  0.0816  130 GLY   A N   
951  C CA  . GLY   A 124 ? 0.5586 0.3008 0.5318 0.0888  0.2086  0.0850  130 GLY   A CA  
952  C C   . GLY   A 124 ? 0.4834 0.2926 0.5022 0.0797  0.1628  0.0892  130 GLY   A C   
953  O O   . GLY   A 124 ? 0.4597 0.3070 0.5046 0.0734  0.1391  0.0947  130 GLY   A O   
954  N N   . LEU   A 125 ? 0.4542 0.2711 0.4737 0.0773  0.1508  0.0852  131 LEU   A N   
955  C CA  . LEU   A 125 ? 0.3994 0.2677 0.4491 0.0672  0.1111  0.0872  131 LEU   A CA  
956  C C   . LEU   A 125 ? 0.4068 0.2613 0.3967 0.0588  0.0864  0.0622  131 LEU   A C   
957  O O   . LEU   A 125 ? 0.4619 0.2718 0.4029 0.0612  0.0996  0.0496  131 LEU   A O   
958  C CB  . LEU   A 125 ? 0.3681 0.2598 0.4786 0.0710  0.1171  0.1075  131 LEU   A CB  
959  C CG  . LEU   A 125 ? 0.3669 0.2787 0.5584 0.0786  0.1387  0.1406  131 LEU   A CG  
960  C CD1 . LEU   A 125 ? 0.3615 0.2826 0.6066 0.0844  0.1519  0.1600  131 LEU   A CD1 
961  C CD2 . LEU   A 125 ? 0.3445 0.3038 0.5788 0.0664  0.1057  0.1566  131 LEU   A CD2 
962  N N   . VAL   A 126 ? 0.3359 0.2261 0.3343 0.0481  0.0523  0.0581  132 VAL   A N   
963  C CA  . VAL   A 126 ? 0.3265 0.2106 0.2879 0.0410  0.0305  0.0400  132 VAL   A CA  
964  C C   . VAL   A 126 ? 0.2884 0.2091 0.2837 0.0346  0.0113  0.0460  132 VAL   A C   
965  O O   . VAL   A 126 ? 0.2760 0.2270 0.3060 0.0286  0.0011  0.0591  132 VAL   A O   
966  C CB  . VAL   A 126 ? 0.3338 0.2135 0.2638 0.0340  0.0131  0.0271  132 VAL   A CB  
967  C CG1 . VAL   A 126 ? 0.3207 0.2320 0.2795 0.0292  0.0039  0.0350  132 VAL   A CG1 
968  C CG2 . VAL   A 126 ? 0.3427 0.2215 0.2523 0.0267  -0.0092 0.0139  132 VAL   A CG2 
969  N N   . GLY   A 127 ? 0.2766 0.1894 0.2575 0.0340  0.0058  0.0377  133 GLY   A N   
970  C CA  . GLY   A 127 ? 0.2654 0.2050 0.2692 0.0273  -0.0106 0.0416  133 GLY   A CA  
971  C C   . GLY   A 127 ? 0.2750 0.2142 0.2539 0.0195  -0.0298 0.0259  133 GLY   A C   
972  O O   . GLY   A 127 ? 0.3013 0.2170 0.2506 0.0213  -0.0310 0.0138  133 GLY   A O   
973  N N   . PHE   A 128 ? 0.2393 0.2002 0.2299 0.0091  -0.0447 0.0280  134 PHE   A N   
974  C CA  . PHE   A 128 ? 0.2326 0.1913 0.2072 0.0022  -0.0560 0.0156  134 PHE   A CA  
975  C C   . PHE   A 128 ? 0.2222 0.1891 0.2046 -0.0036 -0.0622 0.0175  134 PHE   A C   
976  O O   . PHE   A 128 ? 0.2247 0.2045 0.2211 -0.0112 -0.0668 0.0297  134 PHE   A O   
977  C CB  . PHE   A 128 ? 0.2265 0.1909 0.1973 -0.0069 -0.0615 0.0146  134 PHE   A CB  
978  C CG  . PHE   A 128 ? 0.2387 0.1990 0.2054 -0.0027 -0.0567 0.0151  134 PHE   A CG  
979  C CD1 . PHE   A 128 ? 0.2502 0.1956 0.2006 0.0009  -0.0566 0.0051  134 PHE   A CD1 
980  C CD2 . PHE   A 128 ? 0.2430 0.2143 0.2254 -0.0042 -0.0543 0.0280  134 PHE   A CD2 
981  C CE1 . PHE   A 128 ? 0.2680 0.2070 0.2110 0.0038  -0.0525 0.0058  134 PHE   A CE1 
982  C CE2 . PHE   A 128 ? 0.2538 0.2205 0.2328 0.0000  -0.0481 0.0285  134 PHE   A CE2 
983  C CZ  . PHE   A 128 ? 0.2602 0.2097 0.2163 0.0041  -0.0465 0.0162  134 PHE   A CZ  
984  N N   . ALA   A 129 ? 0.2127 0.1705 0.1866 -0.0022 -0.0643 0.0075  135 ALA   A N   
985  C CA  . ALA   A 129 ? 0.2066 0.1688 0.1848 -0.0078 -0.0681 0.0078  135 ALA   A CA  
986  C C   . ALA   A 129 ? 0.2207 0.1799 0.1888 -0.0197 -0.0696 0.0044  135 ALA   A C   
987  O O   . ALA   A 129 ? 0.2267 0.1768 0.1910 -0.0188 -0.0662 -0.0039 135 ALA   A O   
988  C CB  . ALA   A 129 ? 0.2048 0.1565 0.1811 -0.0017 -0.0688 -0.0001 135 ALA   A CB  
989  N N   . ASP   A 130 ? 0.2211 0.1824 0.1833 -0.0326 -0.0743 0.0123  136 ASP   A N   
990  C CA  . ASP   A 130 ? 0.2570 0.2019 0.1951 -0.0476 -0.0725 0.0085  136 ASP   A CA  
991  C C   . ASP   A 130 ? 0.2826 0.2118 0.2138 -0.0479 -0.0623 -0.0014 136 ASP   A C   
992  O O   . ASP   A 130 ? 0.2788 0.2128 0.2208 -0.0429 -0.0635 -0.0010 136 ASP   A O   
993  C CB  . ASP   A 130 ? 0.2930 0.2353 0.2174 -0.0661 -0.0848 0.0219  136 ASP   A CB  
994  C CG  . ASP   A 130 ? 0.3759 0.2884 0.2591 -0.0865 -0.0831 0.0187  136 ASP   A CG  
995  O OD1 . ASP   A 130 ? 0.3767 0.2802 0.2504 -0.0861 -0.0753 0.0117  136 ASP   A OD1 
996  O OD2 . ASP   A 130 ? 0.4178 0.3104 0.2731 -0.1041 -0.0885 0.0229  136 ASP   A OD2 
997  N N   . VAL   A 131 ? 0.2872 0.1953 0.2035 -0.0535 -0.0493 -0.0092 137 VAL   A N   
998  C CA  . VAL   A 131 ? 0.2960 0.1849 0.2111 -0.0543 -0.0335 -0.0157 137 VAL   A CA  
999  C C   . VAL   A 131 ? 0.3416 0.1923 0.2133 -0.0734 -0.0190 -0.0188 137 VAL   A C   
1000 O O   . VAL   A 131 ? 0.3830 0.2088 0.2492 -0.0751 0.0018  -0.0241 137 VAL   A O   
1001 C CB  . VAL   A 131 ? 0.2904 0.1821 0.2395 -0.0405 -0.0237 -0.0200 137 VAL   A CB  
1002 C CG1 . VAL   A 131 ? 0.2618 0.1773 0.2384 -0.0268 -0.0398 -0.0171 137 VAL   A CG1 
1003 C CG2 . VAL   A 131 ? 0.2888 0.1708 0.2355 -0.0422 -0.0144 -0.0225 137 VAL   A CG2 
1004 N N   . ARG   A 132 ? 0.3451 0.1855 0.1842 -0.0887 -0.0278 -0.0148 138 ARG   A N   
1005 C CA  . ARG   A 132 ? 0.3896 0.1826 0.1735 -0.1110 -0.0156 -0.0180 138 ARG   A CA  
1006 C C   . ARG   A 132 ? 0.4597 0.2208 0.2034 -0.1282 -0.0134 -0.0166 138 ARG   A C   
1007 O O   . ARG   A 132 ? 0.5189 0.2273 0.2115 -0.1448 0.0074  -0.0230 138 ARG   A O   
1008 C CB  . ARG   A 132 ? 0.4086 0.1988 0.1672 -0.1262 -0.0334 -0.0106 138 ARG   A CB  
1009 C CG  . ARG   A 132 ? 0.4171 0.2330 0.2083 -0.1111 -0.0335 -0.0123 138 ARG   A CG  
1010 C CD  . ARG   A 132 ? 0.3919 0.2089 0.1648 -0.1258 -0.0530 -0.0022 138 ARG   A CD  
1011 N NE  . ARG   A 132 ? 0.4052 0.2587 0.2077 -0.1232 -0.0787 0.0139  138 ARG   A NE  
1012 C CZ  . ARG   A 132 ? 0.4232 0.2883 0.2305 -0.1324 -0.0981 0.0285  138 ARG   A CZ  
1013 N NH1 . ARG   A 132 ? 0.4318 0.2729 0.2069 -0.1479 -0.0993 0.0281  138 ARG   A NH1 
1014 N NH2 . ARG   A 132 ? 0.4025 0.3019 0.2506 -0.1260 -0.1148 0.0452  138 ARG   A NH2 
1015 N N   . ASP   A 133 ? 0.4455 0.2325 0.2081 -0.1251 -0.0319 -0.0084 139 ASP   A N   
1016 C CA  . ASP   A 133 ? 0.4870 0.2444 0.2118 -0.1422 -0.0323 -0.0057 139 ASP   A CA  
1017 C C   . ASP   A 133 ? 0.5101 0.2548 0.2477 -0.1302 -0.0044 -0.0160 139 ASP   A C   
1018 O O   . ASP   A 133 ? 0.5516 0.2635 0.2524 -0.1442 0.0020  -0.0159 139 ASP   A O   
1019 C CB  . ASP   A 133 ? 0.4879 0.2786 0.2333 -0.1447 -0.0638 0.0105  139 ASP   A CB  
1020 C CG  . ASP   A 133 ? 0.4742 0.3127 0.2832 -0.1169 -0.0652 0.0101  139 ASP   A CG  
1021 O OD1 . ASP   A 133 ? 0.4459 0.3055 0.2881 -0.0977 -0.0579 0.0036  139 ASP   A OD1 
1022 O OD2 . ASP   A 133 ? 0.4513 0.3019 0.2729 -0.1161 -0.0746 0.0170  139 ASP   A OD2 
1023 N N   . LEU   A 134 ? 0.4683 0.2385 0.2600 -0.1057 0.0091  -0.0220 140 LEU   A N   
1024 C CA  . LEU   A 134 ? 0.4547 0.2191 0.2738 -0.0935 0.0316  -0.0267 140 LEU   A CA  
1025 C C   . LEU   A 134 ? 0.5079 0.2215 0.3025 -0.1001 0.0700  -0.0343 140 LEU   A C   
1026 O O   . LEU   A 134 ? 0.4971 0.2159 0.3322 -0.0862 0.0878  -0.0363 140 LEU   A O   
1027 C CB  . LEU   A 134 ? 0.4021 0.2116 0.2899 -0.0688 0.0237  -0.0252 140 LEU   A CB  
1028 C CG  . LEU   A 134 ? 0.3711 0.2220 0.2778 -0.0616 -0.0076 -0.0189 140 LEU   A CG  
1029 C CD1 . LEU   A 134 ? 0.3388 0.2184 0.2947 -0.0423 -0.0148 -0.0185 140 LEU   A CD1 
1030 C CD2 . LEU   A 134 ? 0.3742 0.2286 0.2741 -0.0658 -0.0167 -0.0145 140 LEU   A CD2 
1031 N N   . LEU   A 135 ? 0.5667 0.2247 0.2902 -0.1238 0.0833  -0.0371 141 LEU   A N   
1032 C CA  . LEU   A 135 ? 0.6361 0.2295 0.3186 -0.1341 0.1261  -0.0452 141 LEU   A CA  
1033 C C   . LEU   A 135 ? 0.6429 0.2280 0.3760 -0.1160 0.1654  -0.0473 141 LEU   A C   
1034 O O   . LEU   A 135 ? 0.6679 0.2180 0.4050 -0.1135 0.2041  -0.0511 141 LEU   A O   
1035 C CB  . LEU   A 135 ? 0.7044 0.2285 0.2862 -0.1675 0.1305  -0.0474 141 LEU   A CB  
1036 C CG  . LEU   A 135 ? 0.7421 0.2714 0.2768 -0.1906 0.0859  -0.0390 141 LEU   A CG  
1037 C CD1 . LEU   A 135 ? 0.8236 0.2679 0.2482 -0.2293 0.0917  -0.0398 141 LEU   A CD1 
1038 C CD2 . LEU   A 135 ? 0.7344 0.2870 0.2847 -0.1871 0.0727  -0.0381 141 LEU   A CD2 
1039 N N   . TRP   A 136 ? 0.6164 0.2346 0.3953 -0.1028 0.1562  -0.0425 142 TRP   A N   
1040 C CA  . TRP   A 136 ? 0.6024 0.2176 0.4394 -0.0862 0.1884  -0.0399 142 TRP   A CA  
1041 C C   . TRP   A 136 ? 0.5841 0.2356 0.5062 -0.0646 0.1919  -0.0334 142 TRP   A C   
1042 O O   . TRP   A 136 ? 0.5829 0.2235 0.5580 -0.0534 0.2244  -0.0276 142 TRP   A O   
1043 C CB  . TRP   A 136 ? 0.5764 0.2164 0.4359 -0.0805 0.1730  -0.0355 142 TRP   A CB  
1044 C CG  . TRP   A 136 ? 0.5249 0.2281 0.4139 -0.0720 0.1239  -0.0307 142 TRP   A CG  
1045 C CD1 . TRP   A 136 ? 0.5363 0.2527 0.3852 -0.0836 0.0910  -0.0298 142 TRP   A CD1 
1046 C CD2 . TRP   A 136 ? 0.4724 0.2273 0.4364 -0.0515 0.1045  -0.0242 142 TRP   A CD2 
1047 N NE1 . TRP   A 136 ? 0.5018 0.2734 0.3972 -0.0691 0.0590  -0.0248 142 TRP   A NE1 
1048 C CE2 . TRP   A 136 ? 0.4672 0.2592 0.4255 -0.0508 0.0656  -0.0226 142 TRP   A CE2 
1049 C CE3 . TRP   A 136 ? 0.4486 0.2177 0.4842 -0.0356 0.1157  -0.0173 142 TRP   A CE3 
1050 C CZ2 . TRP   A 136 ? 0.4380 0.2723 0.4460 -0.0358 0.0410  -0.0177 142 TRP   A CZ2 
1051 C CZ3 . TRP   A 136 ? 0.4262 0.2403 0.5122 -0.0231 0.0839  -0.0102 142 TRP   A CZ3 
1052 C CH2 . TRP   A 136 ? 0.4172 0.2593 0.4827 -0.0238 0.0486  -0.0122 142 TRP   A CH2 
1053 N N   . LEU   A 137 ? 0.5731 0.2634 0.5103 -0.0600 0.1607  -0.0321 143 LEU   A N   
1054 C CA  . LEU   A 137 ? 0.5501 0.2698 0.5609 -0.0433 0.1601  -0.0243 143 LEU   A CA  
1055 C C   . LEU   A 137 ? 0.6198 0.2974 0.6430 -0.0431 0.2074  -0.0238 143 LEU   A C   
1056 O O   . LEU   A 137 ? 0.5865 0.2806 0.6885 -0.0287 0.2177  -0.0119 143 LEU   A O   
1057 C CB  . LEU   A 137 ? 0.5175 0.2734 0.5233 -0.0423 0.1228  -0.0250 143 LEU   A CB  
1058 C CG  . LEU   A 137 ? 0.4914 0.2906 0.5030 -0.0378 0.0810  -0.0227 143 LEU   A CG  
1059 C CD1 . LEU   A 137 ? 0.4841 0.3080 0.4861 -0.0373 0.0541  -0.0234 143 LEU   A CD1 
1060 C CD2 . LEU   A 137 ? 0.4582 0.2843 0.5366 -0.0235 0.0710  -0.0132 143 LEU   A CD2 
1061 N N   . ASP   A 138 ? 0.7122 0.3319 0.6569 -0.0607 0.2351  -0.0346 144 ASP   A N   
1062 C CA  . ASP   A 138 ? 0.7895 0.3550 0.7280 -0.0634 0.2868  -0.0367 144 ASP   A CA  
1063 C C   . ASP   A 138 ? 0.8599 0.3758 0.8096 -0.0615 0.3405  -0.0345 144 ASP   A C   
1064 O O   . ASP   A 138 ? 0.8737 0.3534 0.8528 -0.0561 0.3892  -0.0308 144 ASP   A O   
1065 C CB  . ASP   A 138 ? 0.8706 0.3841 0.7052 -0.0874 0.2923  -0.0498 144 ASP   A CB  
1066 C CG  . ASP   A 138 ? 0.9258 0.4793 0.7519 -0.0896 0.2493  -0.0506 144 ASP   A CG  
1067 O OD1 . ASP   A 138 ? 0.9001 0.5069 0.8002 -0.0715 0.2310  -0.0426 144 ASP   A OD1 
1068 O OD2 . ASP   A 138 ? 0.9971 0.5265 0.7424 -0.1110 0.2325  -0.0573 144 ASP   A OD2 
1069 N N   . GLU   A 139 ? 0.9037 0.4111 0.8263 -0.0669 0.3366  -0.0366 145 GLU   A N   
1070 C CA  . GLU   A 139 ? 0.9559 0.4109 0.8835 -0.0658 0.3907  -0.0348 145 GLU   A CA  
1071 C C   . GLU   A 139 ? 0.9279 0.4320 0.9501 -0.0464 0.3806  -0.0203 145 GLU   A C   
1072 O O   . GLU   A 139 ? 0.9478 0.4170 0.9956 -0.0415 0.4260  -0.0148 145 GLU   A O   
1073 C CB  . GLU   A 139 ? 1.0607 0.4453 0.8671 -0.0923 0.4048  -0.0487 145 GLU   A CB  
1074 C CG  . GLU   A 139 ? 1.1366 0.5587 0.9001 -0.1034 0.3453  -0.0514 145 GLU   A CG  
1075 C CD  . GLU   A 139 ? 1.2971 0.6669 0.9381 -0.1354 0.3320  -0.0618 145 GLU   A CD  
1076 O OE1 . GLU   A 139 ? 1.3305 0.7135 0.9316 -0.1483 0.2939  -0.0610 145 GLU   A OE1 
1077 O OE2 . GLU   A 139 ? 1.3713 0.6853 0.9574 -0.1491 0.3581  -0.0687 145 GLU   A OE2 
1078 C C4  . A1B3R B .   ? 0.7128 0.2202 0.3288 0.0429  0.1518  -0.0078 201 A1B3R A C4  
1079 C C5  . A1B3R B .   ? 0.7228 0.2223 0.3245 0.0375  0.1366  -0.0135 201 A1B3R A C5  
1080 C C6  . A1B3R B .   ? 0.6851 0.2376 0.3174 0.0308  0.0916  -0.0157 201 A1B3R A C6  
1081 C C7  . A1B3R B .   ? 0.6957 0.2378 0.3153 0.0256  0.0780  -0.0204 201 A1B3R A C7  
1082 C C8  . A1B3R B .   ? 0.6329 0.2418 0.3331 0.0368  0.0776  -0.0117 201 A1B3R A C8  
1083 C C10 . A1B3R B .   ? 0.6112 0.2249 0.2832 0.0109  -0.0038 -0.0252 201 A1B3R A C10 
1084 C C13 . A1B3R B .   ? 0.4802 0.2429 0.3335 0.0402  0.0211  -0.0010 201 A1B3R A C13 
1085 C C15 . A1B3R B .   ? 0.5621 0.2273 0.3281 0.0414  0.0618  -0.0071 201 A1B3R A C15 
1086 O O   . A1B3R B .   ? 0.5946 0.2521 0.3566 0.0467  0.0872  -0.0006 201 A1B3R A O   
1087 N N   . A1B3R B .   ? 0.6109 0.2209 0.3090 0.0328  0.0622  -0.0154 201 A1B3R A N   
1088 C C12 . A1B3R B .   ? 0.5244 0.2378 0.3180 0.0342  0.0220  -0.0095 201 A1B3R A C12 
1089 C C14 . A1B3R B .   ? 0.4361 0.2433 0.3171 0.0337  -0.0100 -0.0026 201 A1B3R A C14 
1090 O O1  . A1B3R B .   ? 0.3982 0.2447 0.3261 0.0365  -0.0105 0.0061  201 A1B3R A O1  
1091 C C11 . A1B3R B .   ? 0.5593 0.2340 0.3014 0.0213  -0.0021 -0.0194 201 A1B3R A C11 
1092 C C9  . A1B3R B .   ? 0.6442 0.2068 0.2791 0.0174  0.0384  -0.0254 201 A1B3R A C9  
1093 C C1  . A1B3R B .   ? 0.6352 0.2439 0.3082 0.0293  0.0645  -0.0130 201 A1B3R A C1  
1094 S S   . A1B3R B .   ? 0.5810 0.2461 0.2920 0.0218  0.0180  -0.0152 201 A1B3R A S   
1095 C C   . A1B3R B .   ? 0.5514 0.2602 0.2932 0.0196  -0.0009 -0.0128 201 A1B3R A C   
1096 C C3  . A1B3R B .   ? 0.6714 0.2375 0.3273 0.0407  0.1206  -0.0053 201 A1B3R A C3  
1097 C C2  . A1B3R B .   ? 0.6407 0.2553 0.3231 0.0338  0.0782  -0.0084 201 A1B3R A C2  
# 
