data_7I52
# 
_entry.id   7I52 
# 
_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   7I52         pdb_00007i52 10.2210/pdb7i52/pdb 
WWPDB D_1001408325 ?            ?                   
# 
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                        7I52 
_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 2   3.4.22.29 ? ? ? 
2 non-polymer syn '(2S)-4-{[2-methoxy-5-(trifluoromethyl)phenyl]acetyl}thiomorpholine-2-carboxamide' 362.367   1   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                                         65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                               78.133    1   ?         ? ? ? 
5 water       nat water                                                                              18.015    404 ?         ? ? ? 
# 
_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,C 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2S)-4-{[2-methoxy-5-(trifluoromethyl)phenyl]acetyl}thiomorpholine-2-carboxamide' A1B3J 
3 'ZINC ION'                                                                         ZN    
4 'DIMETHYL SULFOXIDE'                                                               DMS   
5 water                                                                              HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B3J non-polymer         . '(2S)-4-{[2-methoxy-5-(trifluoromethyl)phenyl]acetyl}thiomorpholine-2-carboxamide' ? 
'C15 H17 F3 N2 O3 S' 362.367 
ALA   'L-peptide linking' y ALANINE                                                                            ? 'C3 H7 N O2' 
89.093  
ARG   'L-peptide linking' y ARGININE                                                                           ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                         ? 'C4 H8 N2 O3' 
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                    ? 'C4 H7 N O4' 
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                           ? 'C3 H7 N O2 S' 
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                               ? 'C2 H6 O S' 
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                          ? 'C5 H10 N2 O3' 
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                    ? 'C5 H9 N O4' 
147.129 
GLY   'peptide linking'   y GLYCINE                                                                            ? 'C2 H5 N O2' 
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                          ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                              ? 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                         ? 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                            ? 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                                             ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                         ? 'C5 H11 N O2 S' 
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                      ? 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                                            ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                             ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                          ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                         ? 'C11 H12 N2 O2' 
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                           ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                             ? 'C5 H11 N O2' 
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                         ? 'Zn 2' 65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 146 GLU GLU A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
B 1 1   SER 1   7   7   SER SER C . n 
B 1 2   GLY 2   8   8   GLY GLY C . n 
B 1 3   ALA 3   9   9   ALA ALA C . n 
B 1 4   ILE 4   10  10  ILE ILE C . n 
B 1 5   TYR 5   11  11  TYR TYR C . n 
B 1 6   VAL 6   12  12  VAL VAL C . n 
B 1 7   GLY 7   13  13  GLY GLY C . n 
B 1 8   ASN 8   14  14  ASN ASN C . n 
B 1 9   TYR 9   15  15  TYR TYR C . n 
B 1 10  ARG 10  16  16  ARG ARG C . n 
B 1 11  VAL 11  17  17  VAL VAL C . n 
B 1 12  VAL 12  18  18  VAL VAL C . n 
B 1 13  ASN 13  19  19  ASN ASN C . n 
B 1 14  ARG 14  20  20  ARG ARG C . n 
B 1 15  HIS 15  21  21  HIS HIS C . n 
B 1 16  LEU 16  22  22  LEU LEU C . n 
B 1 17  ALA 17  23  23  ALA ALA C . n 
B 1 18  THR 18  24  24  THR THR C . n 
B 1 19  HIS 19  25  25  HIS HIS C . n 
B 1 20  ASN 20  26  26  ASN ASN C . n 
B 1 21  ASP 21  27  27  ASP ASP C . n 
B 1 22  TRP 22  28  28  TRP TRP C . n 
B 1 23  ALA 23  29  29  ALA ALA C . n 
B 1 24  ASN 24  30  30  ASN ASN C . n 
B 1 25  LEU 25  31  31  LEU LEU C . n 
B 1 26  VAL 26  32  32  VAL VAL C . n 
B 1 27  TRP 27  33  33  TRP TRP C . n 
B 1 28  GLU 28  34  34  GLU GLU C . n 
B 1 29  ASP 29  35  35  ASP ASP C . n 
B 1 30  SER 30  36  36  SER SER C . n 
B 1 31  SER 31  37  37  SER SER C . n 
B 1 32  ARG 32  38  38  ARG ARG C . n 
B 1 33  ASP 33  39  39  ASP ASP C . n 
B 1 34  LEU 34  40  40  LEU LEU C . n 
B 1 35  LEU 35  41  41  LEU LEU C . n 
B 1 36  VAL 36  42  42  VAL VAL C . n 
B 1 37  SER 37  43  43  SER SER C . n 
B 1 38  SER 38  44  44  SER SER C . n 
B 1 39  THR 39  45  45  THR THR C . n 
B 1 40  THR 40  46  46  THR THR C . n 
B 1 41  ALA 41  47  47  ALA ALA C . n 
B 1 42  GLN 42  48  48  GLN GLN C . n 
B 1 43  GLY 43  49  49  GLY GLY C . n 
B 1 44  CYS 44  50  50  CYS CYS C . n 
B 1 45  ASP 45  51  51  ASP ASP C . n 
B 1 46  THR 46  52  52  THR THR C . n 
B 1 47  ILE 47  53  53  ILE ILE C . n 
B 1 48  ALA 48  54  54  ALA ALA C . n 
B 1 49  ARG 49  55  55  ARG ARG C . n 
B 1 50  CYS 50  56  56  CYS CYS C . n 
B 1 51  ASP 51  57  57  ASP ASP C . n 
B 1 52  CYS 52  58  58  CYS CYS C . n 
B 1 53  GLN 53  59  59  GLN GLN C . n 
B 1 54  THR 54  60  60  THR THR C . n 
B 1 55  GLY 55  61  61  GLY GLY C . n 
B 1 56  VAL 56  62  62  VAL VAL C . n 
B 1 57  TYR 57  63  63  TYR TYR C . n 
B 1 58  TYR 58  64  64  TYR TYR C . n 
B 1 59  CYS 59  65  65  CYS CYS C . n 
B 1 60  SER 60  66  66  SER SER C . n 
B 1 61  SER 61  67  67  SER SER C . n 
B 1 62  ARG 62  68  68  ARG ARG C . n 
B 1 63  ARG 63  69  69  ARG ARG C . n 
B 1 64  LYS 64  70  70  LYS LYS C . n 
B 1 65  HIS 65  71  71  HIS HIS C . n 
B 1 66  TYR 66  72  72  TYR TYR C . n 
B 1 67  PRO 67  73  73  PRO PRO C . n 
B 1 68  VAL 68  74  74  VAL VAL C . n 
B 1 69  SER 69  75  75  SER SER C . n 
B 1 70  PHE 70  76  76  PHE PHE C . n 
B 1 71  SER 71  77  77  SER SER C . n 
B 1 72  LYS 72  78  78  LYS LYS C . n 
B 1 73  PRO 73  79  79  PRO PRO C . n 
B 1 74  SER 74  80  80  SER SER C . n 
B 1 75  LEU 75  81  81  LEU LEU C . n 
B 1 76  ILE 76  82  82  ILE ILE C . n 
B 1 77  PHE 77  83  83  PHE PHE C . n 
B 1 78  VAL 78  84  84  VAL VAL C . n 
B 1 79  GLU 79  85  85  GLU GLU C . n 
B 1 80  ALA 80  86  86  ALA ALA C . n 
B 1 81  SER 81  87  87  SER SER C . n 
B 1 82  GLU 82  88  88  GLU GLU C . n 
B 1 83  TYR 83  89  89  TYR TYR C . n 
B 1 84  TYR 84  90  90  TYR TYR C . n 
B 1 85  PRO 85  91  91  PRO PRO C . n 
B 1 86  ALA 86  92  92  ALA ALA C . n 
B 1 87  ARG 87  93  93  ARG ARG C . n 
B 1 88  TYR 88  94  94  TYR TYR C . n 
B 1 89  GLN 89  95  95  GLN GLN C . n 
B 1 90  SER 90  96  96  SER SER C . n 
B 1 91  HIS 91  97  97  HIS HIS C . n 
B 1 92  LEU 92  98  98  LEU LEU C . n 
B 1 93  MET 93  99  99  MET MET C . n 
B 1 94  LEU 94  100 100 LEU LEU C . n 
B 1 95  ALA 95  101 101 ALA ALA C . n 
B 1 96  VAL 96  102 102 VAL VAL C . n 
B 1 97  GLY 97  103 103 GLY GLY C . n 
B 1 98  HIS 98  104 104 HIS HIS C . n 
B 1 99  SER 99  105 105 SER SER C . n 
B 1 100 GLU 100 106 106 GLU GLU C . n 
B 1 101 PRO 101 107 107 PRO PRO C . n 
B 1 102 GLY 102 108 108 GLY GLY C . n 
B 1 103 ASP 103 109 109 ASP ASP C . n 
B 1 104 CYS 104 110 110 CYS CYS C . n 
B 1 105 GLY 105 111 111 GLY GLY C . n 
B 1 106 GLY 106 112 112 GLY GLY C . n 
B 1 107 ILE 107 113 113 ILE ILE C . n 
B 1 108 LEU 108 114 114 LEU LEU C . n 
B 1 109 ARG 109 115 115 ARG ARG C . n 
B 1 110 CYS 110 116 116 CYS CYS C . n 
B 1 111 GLN 111 117 117 GLN GLN C . n 
B 1 112 HIS 112 118 118 HIS HIS C . n 
B 1 113 GLY 113 119 119 GLY GLY C . n 
B 1 114 VAL 114 120 120 VAL VAL C . n 
B 1 115 VAL 115 121 121 VAL VAL C . n 
B 1 116 GLY 116 122 122 GLY GLY C . n 
B 1 117 ILE 117 123 123 ILE ILE C . n 
B 1 118 VAL 118 124 124 VAL VAL C . n 
B 1 119 SER 119 125 125 SER SER C . n 
B 1 120 THR 120 126 126 THR THR C . n 
B 1 121 GLY 121 127 127 GLY GLY C . n 
B 1 122 GLY 122 128 128 GLY GLY C . n 
B 1 123 ASN 123 129 129 ASN ASN C . n 
B 1 124 GLY 124 130 130 GLY GLY C . n 
B 1 125 LEU 125 131 131 LEU LEU C . n 
B 1 126 VAL 126 132 132 VAL VAL C . n 
B 1 127 GLY 127 133 133 GLY GLY C . n 
B 1 128 PHE 128 134 134 PHE PHE C . n 
B 1 129 ALA 129 135 135 ALA ALA C . n 
B 1 130 ASP 130 136 136 ASP ASP C . n 
B 1 131 VAL 131 137 137 VAL VAL C . n 
B 1 132 ARG 132 138 138 ARG ARG C . n 
B 1 133 ASP 133 139 139 ASP ASP C . n 
B 1 134 LEU 134 140 140 LEU LEU C . n 
B 1 135 LEU 135 141 141 LEU LEU C . n 
B 1 136 TRP 136 142 142 TRP TRP C . n 
B 1 137 LEU 137 143 143 LEU LEU C . n 
B 1 138 ASP 138 144 144 ASP ASP C . n 
B 1 139 GLU 139 145 145 GLU GLU C . n 
B 1 140 GLU 140 146 146 GLU GLU C . n 
B 1 141 ALA 141 147 ?   ?   ?   C . n 
B 1 142 MET 142 148 ?   ?   ?   C . n 
B 1 143 GLU 143 149 ?   ?   ?   C . n 
B 1 144 GLN 144 150 ?   ?   ?   C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1B3J 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3J 
_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 
C 2 A1B3J 1   201 201 A1B3J LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 3 ZN    1   201 1   ZN    ZN  C . 
F 4 DMS   1   202 1   DMS   DMS C . 
G 5 HOH   1   401 401 HOH   HOH A . 
G 5 HOH   2   402 347 HOH   HOH A . 
G 5 HOH   3   403 404 HOH   HOH A . 
G 5 HOH   4   404 262 HOH   HOH A . 
G 5 HOH   5   405 76  HOH   HOH A . 
G 5 HOH   6   406 316 HOH   HOH A . 
G 5 HOH   7   407 219 HOH   HOH A . 
G 5 HOH   8   408 248 HOH   HOH A . 
G 5 HOH   9   409 56  HOH   HOH A . 
G 5 HOH   10  410 255 HOH   HOH A . 
G 5 HOH   11  411 14  HOH   HOH A . 
G 5 HOH   12  412 87  HOH   HOH A . 
G 5 HOH   13  413 366 HOH   HOH A . 
G 5 HOH   14  414 194 HOH   HOH A . 
G 5 HOH   15  415 183 HOH   HOH A . 
G 5 HOH   16  416 102 HOH   HOH A . 
G 5 HOH   17  417 308 HOH   HOH A . 
G 5 HOH   18  418 127 HOH   HOH A . 
G 5 HOH   19  419 354 HOH   HOH A . 
G 5 HOH   20  420 346 HOH   HOH A . 
G 5 HOH   21  421 40  HOH   HOH A . 
G 5 HOH   22  422 4   HOH   HOH A . 
G 5 HOH   23  423 381 HOH   HOH A . 
G 5 HOH   24  424 136 HOH   HOH A . 
G 5 HOH   25  425 185 HOH   HOH A . 
G 5 HOH   26  426 167 HOH   HOH A . 
G 5 HOH   27  427 82  HOH   HOH A . 
G 5 HOH   28  428 114 HOH   HOH A . 
G 5 HOH   29  429 212 HOH   HOH A . 
G 5 HOH   30  430 186 HOH   HOH A . 
G 5 HOH   31  431 310 HOH   HOH A . 
G 5 HOH   32  432 311 HOH   HOH A . 
G 5 HOH   33  433 234 HOH   HOH A . 
G 5 HOH   34  434 153 HOH   HOH A . 
G 5 HOH   35  435 21  HOH   HOH A . 
G 5 HOH   36  436 98  HOH   HOH A . 
G 5 HOH   37  437 2   HOH   HOH A . 
G 5 HOH   38  438 191 HOH   HOH A . 
G 5 HOH   39  439 20  HOH   HOH A . 
G 5 HOH   40  440 294 HOH   HOH A . 
G 5 HOH   41  441 23  HOH   HOH A . 
G 5 HOH   42  442 364 HOH   HOH A . 
G 5 HOH   43  443 239 HOH   HOH A . 
G 5 HOH   44  444 209 HOH   HOH A . 
G 5 HOH   45  445 97  HOH   HOH A . 
G 5 HOH   46  446 177 HOH   HOH A . 
G 5 HOH   47  447 345 HOH   HOH A . 
G 5 HOH   48  448 254 HOH   HOH A . 
G 5 HOH   49  449 324 HOH   HOH A . 
G 5 HOH   50  450 8   HOH   HOH A . 
G 5 HOH   51  451 124 HOH   HOH A . 
G 5 HOH   52  452 266 HOH   HOH A . 
G 5 HOH   53  453 36  HOH   HOH A . 
G 5 HOH   54  454 65  HOH   HOH A . 
G 5 HOH   55  455 16  HOH   HOH A . 
G 5 HOH   56  456 22  HOH   HOH A . 
G 5 HOH   57  457 351 HOH   HOH A . 
G 5 HOH   58  458 165 HOH   HOH A . 
G 5 HOH   59  459 320 HOH   HOH A . 
G 5 HOH   60  460 307 HOH   HOH A . 
G 5 HOH   61  461 223 HOH   HOH A . 
G 5 HOH   62  462 32  HOH   HOH A . 
G 5 HOH   63  463 349 HOH   HOH A . 
G 5 HOH   64  464 193 HOH   HOH A . 
G 5 HOH   65  465 226 HOH   HOH A . 
G 5 HOH   66  466 408 HOH   HOH A . 
G 5 HOH   67  467 157 HOH   HOH A . 
G 5 HOH   68  468 133 HOH   HOH A . 
G 5 HOH   69  469 394 HOH   HOH A . 
G 5 HOH   70  470 317 HOH   HOH A . 
G 5 HOH   71  471 85  HOH   HOH A . 
G 5 HOH   72  472 141 HOH   HOH A . 
G 5 HOH   73  473 355 HOH   HOH A . 
G 5 HOH   74  474 92  HOH   HOH A . 
G 5 HOH   75  475 88  HOH   HOH A . 
G 5 HOH   76  476 77  HOH   HOH A . 
G 5 HOH   77  477 5   HOH   HOH A . 
G 5 HOH   78  478 30  HOH   HOH A . 
G 5 HOH   79  479 75  HOH   HOH A . 
G 5 HOH   80  480 108 HOH   HOH A . 
G 5 HOH   81  481 301 HOH   HOH A . 
G 5 HOH   82  482 398 HOH   HOH A . 
G 5 HOH   83  483 275 HOH   HOH A . 
G 5 HOH   84  484 31  HOH   HOH A . 
G 5 HOH   85  485 122 HOH   HOH A . 
G 5 HOH   86  486 41  HOH   HOH A . 
G 5 HOH   87  487 49  HOH   HOH A . 
G 5 HOH   88  488 353 HOH   HOH A . 
G 5 HOH   89  489 232 HOH   HOH A . 
G 5 HOH   90  490 260 HOH   HOH A . 
G 5 HOH   91  491 350 HOH   HOH A . 
G 5 HOH   92  492 252 HOH   HOH A . 
G 5 HOH   93  493 208 HOH   HOH A . 
G 5 HOH   94  494 28  HOH   HOH A . 
G 5 HOH   95  495 57  HOH   HOH A . 
G 5 HOH   96  496 46  HOH   HOH A . 
G 5 HOH   97  497 71  HOH   HOH A . 
G 5 HOH   98  498 147 HOH   HOH A . 
G 5 HOH   99  499 251 HOH   HOH A . 
G 5 HOH   100 500 178 HOH   HOH A . 
G 5 HOH   101 501 356 HOH   HOH A . 
G 5 HOH   102 502 272 HOH   HOH A . 
G 5 HOH   103 503 91  HOH   HOH A . 
G 5 HOH   104 504 78  HOH   HOH A . 
G 5 HOH   105 505 359 HOH   HOH A . 
G 5 HOH   106 506 180 HOH   HOH A . 
G 5 HOH   107 507 50  HOH   HOH A . 
G 5 HOH   108 508 70  HOH   HOH A . 
G 5 HOH   109 509 164 HOH   HOH A . 
G 5 HOH   110 510 58  HOH   HOH A . 
G 5 HOH   111 511 112 HOH   HOH A . 
G 5 HOH   112 512 131 HOH   HOH A . 
G 5 HOH   113 513 79  HOH   HOH A . 
G 5 HOH   114 514 89  HOH   HOH A . 
G 5 HOH   115 515 63  HOH   HOH A . 
G 5 HOH   116 516 144 HOH   HOH A . 
G 5 HOH   117 517 99  HOH   HOH A . 
G 5 HOH   118 518 110 HOH   HOH A . 
G 5 HOH   119 519 283 HOH   HOH A . 
G 5 HOH   120 520 196 HOH   HOH A . 
G 5 HOH   121 521 106 HOH   HOH A . 
G 5 HOH   122 522 218 HOH   HOH A . 
G 5 HOH   123 523 90  HOH   HOH A . 
G 5 HOH   124 524 236 HOH   HOH A . 
G 5 HOH   125 525 238 HOH   HOH A . 
G 5 HOH   126 526 273 HOH   HOH A . 
G 5 HOH   127 527 105 HOH   HOH A . 
G 5 HOH   128 528 348 HOH   HOH A . 
G 5 HOH   129 529 257 HOH   HOH A . 
G 5 HOH   130 530 93  HOH   HOH A . 
G 5 HOH   131 531 200 HOH   HOH A . 
G 5 HOH   132 532 81  HOH   HOH A . 
G 5 HOH   133 533 34  HOH   HOH A . 
G 5 HOH   134 534 315 HOH   HOH A . 
G 5 HOH   135 535 247 HOH   HOH A . 
G 5 HOH   136 536 148 HOH   HOH A . 
G 5 HOH   137 537 374 HOH   HOH A . 
G 5 HOH   138 538 187 HOH   HOH A . 
G 5 HOH   139 539 113 HOH   HOH A . 
G 5 HOH   140 540 385 HOH   HOH A . 
G 5 HOH   141 541 357 HOH   HOH A . 
G 5 HOH   142 542 72  HOH   HOH A . 
G 5 HOH   143 543 388 HOH   HOH A . 
G 5 HOH   144 544 37  HOH   HOH A . 
G 5 HOH   145 545 43  HOH   HOH A . 
G 5 HOH   146 546 9   HOH   HOH A . 
G 5 HOH   147 547 240 HOH   HOH A . 
G 5 HOH   148 548 172 HOH   HOH A . 
G 5 HOH   149 549 399 HOH   HOH A . 
G 5 HOH   150 550 370 HOH   HOH A . 
G 5 HOH   151 551 111 HOH   HOH A . 
G 5 HOH   152 552 344 HOH   HOH A . 
G 5 HOH   153 553 1   HOH   HOH A . 
G 5 HOH   154 554 84  HOH   HOH A . 
G 5 HOH   155 555 143 HOH   HOH A . 
G 5 HOH   156 556 258 HOH   HOH A . 
G 5 HOH   157 557 309 HOH   HOH A . 
G 5 HOH   158 558 329 HOH   HOH A . 
G 5 HOH   159 559 352 HOH   HOH A . 
G 5 HOH   160 560 174 HOH   HOH A . 
G 5 HOH   161 561 319 HOH   HOH A . 
G 5 HOH   162 562 343 HOH   HOH A . 
G 5 HOH   163 563 339 HOH   HOH A . 
G 5 HOH   164 564 335 HOH   HOH A . 
G 5 HOH   165 565 151 HOH   HOH A . 
G 5 HOH   166 566 206 HOH   HOH A . 
G 5 HOH   167 567 228 HOH   HOH A . 
G 5 HOH   168 568 259 HOH   HOH A . 
G 5 HOH   169 569 362 HOH   HOH A . 
G 5 HOH   170 570 156 HOH   HOH A . 
G 5 HOH   171 571 318 HOH   HOH A . 
G 5 HOH   172 572 340 HOH   HOH A . 
G 5 HOH   173 573 256 HOH   HOH A . 
G 5 HOH   174 574 302 HOH   HOH A . 
G 5 HOH   175 575 235 HOH   HOH A . 
G 5 HOH   176 576 264 HOH   HOH A . 
G 5 HOH   177 577 268 HOH   HOH A . 
G 5 HOH   178 578 213 HOH   HOH A . 
G 5 HOH   179 579 358 HOH   HOH A . 
G 5 HOH   180 580 276 HOH   HOH A . 
G 5 HOH   181 581 166 HOH   HOH A . 
G 5 HOH   182 582 313 HOH   HOH A . 
G 5 HOH   183 583 296 HOH   HOH A . 
G 5 HOH   184 584 371 HOH   HOH A . 
G 5 HOH   185 585 198 HOH   HOH A . 
G 5 HOH   186 586 245 HOH   HOH A . 
G 5 HOH   187 587 379 HOH   HOH A . 
G 5 HOH   188 588 160 HOH   HOH A . 
G 5 HOH   189 589 169 HOH   HOH A . 
G 5 HOH   190 590 123 HOH   HOH A . 
G 5 HOH   191 591 217 HOH   HOH A . 
G 5 HOH   192 592 407 HOH   HOH A . 
G 5 HOH   193 593 303 HOH   HOH A . 
G 5 HOH   194 594 182 HOH   HOH A . 
G 5 HOH   195 595 413 HOH   HOH A . 
G 5 HOH   196 596 202 HOH   HOH A . 
G 5 HOH   197 597 279 HOH   HOH A . 
G 5 HOH   198 598 341 HOH   HOH A . 
G 5 HOH   199 599 269 HOH   HOH A . 
G 5 HOH   200 600 336 HOH   HOH A . 
G 5 HOH   201 601 270 HOH   HOH A . 
G 5 HOH   202 602 286 HOH   HOH A . 
G 5 HOH   203 603 342 HOH   HOH A . 
H 5 HOH   1   301 414 HOH   HOH C . 
H 5 HOH   2   302 393 HOH   HOH C . 
H 5 HOH   3   303 300 HOH   HOH C . 
H 5 HOH   4   304 295 HOH   HOH C . 
H 5 HOH   5   305 126 HOH   HOH C . 
H 5 HOH   6   306 323 HOH   HOH C . 
H 5 HOH   7   307 412 HOH   HOH C . 
H 5 HOH   8   308 409 HOH   HOH C . 
H 5 HOH   9   309 360 HOH   HOH C . 
H 5 HOH   10  310 220 HOH   HOH C . 
H 5 HOH   11  311 103 HOH   HOH C . 
H 5 HOH   12  312 250 HOH   HOH C . 
H 5 HOH   13  313 281 HOH   HOH C . 
H 5 HOH   14  314 321 HOH   HOH C . 
H 5 HOH   15  315 190 HOH   HOH C . 
H 5 HOH   16  316 83  HOH   HOH C . 
H 5 HOH   17  317 173 HOH   HOH C . 
H 5 HOH   18  318 293 HOH   HOH C . 
H 5 HOH   19  319 229 HOH   HOH C . 
H 5 HOH   20  320 377 HOH   HOH C . 
H 5 HOH   21  321 68  HOH   HOH C . 
H 5 HOH   22  322 274 HOH   HOH C . 
H 5 HOH   23  323 168 HOH   HOH C . 
H 5 HOH   24  324 176 HOH   HOH C . 
H 5 HOH   25  325 52  HOH   HOH C . 
H 5 HOH   26  326 19  HOH   HOH C . 
H 5 HOH   27  327 140 HOH   HOH C . 
H 5 HOH   28  328 184 HOH   HOH C . 
H 5 HOH   29  329 45  HOH   HOH C . 
H 5 HOH   30  330 361 HOH   HOH C . 
H 5 HOH   31  331 74  HOH   HOH C . 
H 5 HOH   32  332 199 HOH   HOH C . 
H 5 HOH   33  333 154 HOH   HOH C . 
H 5 HOH   34  334 6   HOH   HOH C . 
H 5 HOH   35  335 61  HOH   HOH C . 
H 5 HOH   36  336 288 HOH   HOH C . 
H 5 HOH   37  337 67  HOH   HOH C . 
H 5 HOH   38  338 42  HOH   HOH C . 
H 5 HOH   39  339 130 HOH   HOH C . 
H 5 HOH   40  340 222 HOH   HOH C . 
H 5 HOH   41  341 17  HOH   HOH C . 
H 5 HOH   42  342 69  HOH   HOH C . 
H 5 HOH   43  343 135 HOH   HOH C . 
H 5 HOH   44  344 54  HOH   HOH C . 
H 5 HOH   45  345 64  HOH   HOH C . 
H 5 HOH   46  346 384 HOH   HOH C . 
H 5 HOH   47  347 149 HOH   HOH C . 
H 5 HOH   48  348 15  HOH   HOH C . 
H 5 HOH   49  349 159 HOH   HOH C . 
H 5 HOH   50  350 189 HOH   HOH C . 
H 5 HOH   51  351 205 HOH   HOH C . 
H 5 HOH   52  352 233 HOH   HOH C . 
H 5 HOH   53  353 215 HOH   HOH C . 
H 5 HOH   54  354 216 HOH   HOH C . 
H 5 HOH   55  355 18  HOH   HOH C . 
H 5 HOH   56  356 132 HOH   HOH C . 
H 5 HOH   57  357 387 HOH   HOH C . 
H 5 HOH   58  358 389 HOH   HOH C . 
H 5 HOH   59  359 116 HOH   HOH C . 
H 5 HOH   60  360 73  HOH   HOH C . 
H 5 HOH   61  361 47  HOH   HOH C . 
H 5 HOH   62  362 12  HOH   HOH C . 
H 5 HOH   63  363 246 HOH   HOH C . 
H 5 HOH   64  364 221 HOH   HOH C . 
H 5 HOH   65  365 365 HOH   HOH C . 
H 5 HOH   66  366 391 HOH   HOH C . 
H 5 HOH   67  367 94  HOH   HOH C . 
H 5 HOH   68  368 109 HOH   HOH C . 
H 5 HOH   69  369 107 HOH   HOH C . 
H 5 HOH   70  370 158 HOH   HOH C . 
H 5 HOH   71  371 80  HOH   HOH C . 
H 5 HOH   72  372 53  HOH   HOH C . 
H 5 HOH   73  373 386 HOH   HOH C . 
H 5 HOH   74  374 330 HOH   HOH C . 
H 5 HOH   75  375 392 HOH   HOH C . 
H 5 HOH   76  376 115 HOH   HOH C . 
H 5 HOH   77  377 363 HOH   HOH C . 
H 5 HOH   78  378 402 HOH   HOH C . 
H 5 HOH   79  379 207 HOH   HOH C . 
H 5 HOH   80  380 367 HOH   HOH C . 
H 5 HOH   81  381 197 HOH   HOH C . 
H 5 HOH   82  382 390 HOH   HOH C . 
H 5 HOH   83  383 10  HOH   HOH C . 
H 5 HOH   84  384 44  HOH   HOH C . 
H 5 HOH   85  385 397 HOH   HOH C . 
H 5 HOH   86  386 380 HOH   HOH C . 
H 5 HOH   87  387 137 HOH   HOH C . 
H 5 HOH   88  388 104 HOH   HOH C . 
H 5 HOH   89  389 39  HOH   HOH C . 
H 5 HOH   90  390 66  HOH   HOH C . 
H 5 HOH   91  391 128 HOH   HOH C . 
H 5 HOH   92  392 60  HOH   HOH C . 
H 5 HOH   93  393 267 HOH   HOH C . 
H 5 HOH   94  394 3   HOH   HOH C . 
H 5 HOH   95  395 372 HOH   HOH C . 
H 5 HOH   96  396 38  HOH   HOH C . 
H 5 HOH   97  397 249 HOH   HOH C . 
H 5 HOH   98  398 369 HOH   HOH C . 
H 5 HOH   99  399 337 HOH   HOH C . 
H 5 HOH   100 400 55  HOH   HOH C . 
H 5 HOH   101 401 29  HOH   HOH C . 
H 5 HOH   102 402 155 HOH   HOH C . 
H 5 HOH   103 403 96  HOH   HOH C . 
H 5 HOH   104 404 175 HOH   HOH C . 
H 5 HOH   105 405 203 HOH   HOH C . 
H 5 HOH   106 406 327 HOH   HOH C . 
H 5 HOH   107 407 142 HOH   HOH C . 
H 5 HOH   108 408 150 HOH   HOH C . 
H 5 HOH   109 409 125 HOH   HOH C . 
H 5 HOH   110 410 62  HOH   HOH C . 
H 5 HOH   111 411 179 HOH   HOH C . 
H 5 HOH   112 412 230 HOH   HOH C . 
H 5 HOH   113 413 95  HOH   HOH C . 
H 5 HOH   114 414 13  HOH   HOH C . 
H 5 HOH   115 415 278 HOH   HOH C . 
H 5 HOH   116 416 25  HOH   HOH C . 
H 5 HOH   117 417 24  HOH   HOH C . 
H 5 HOH   118 418 145 HOH   HOH C . 
H 5 HOH   119 419 26  HOH   HOH C . 
H 5 HOH   120 420 225 HOH   HOH C . 
H 5 HOH   121 421 138 HOH   HOH C . 
H 5 HOH   122 422 119 HOH   HOH C . 
H 5 HOH   123 423 120 HOH   HOH C . 
H 5 HOH   124 424 171 HOH   HOH C . 
H 5 HOH   125 425 332 HOH   HOH C . 
H 5 HOH   126 426 101 HOH   HOH C . 
H 5 HOH   127 427 237 HOH   HOH C . 
H 5 HOH   128 428 152 HOH   HOH C . 
H 5 HOH   129 429 227 HOH   HOH C . 
H 5 HOH   130 430 211 HOH   HOH C . 
H 5 HOH   131 431 242 HOH   HOH C . 
H 5 HOH   132 432 100 HOH   HOH C . 
H 5 HOH   133 433 192 HOH   HOH C . 
H 5 HOH   134 434 139 HOH   HOH C . 
H 5 HOH   135 435 284 HOH   HOH C . 
H 5 HOH   136 436 291 HOH   HOH C . 
H 5 HOH   137 437 325 HOH   HOH C . 
H 5 HOH   138 438 162 HOH   HOH C . 
H 5 HOH   139 439 285 HOH   HOH C . 
H 5 HOH   140 440 292 HOH   HOH C . 
H 5 HOH   141 441 129 HOH   HOH C . 
H 5 HOH   142 442 263 HOH   HOH C . 
H 5 HOH   143 443 33  HOH   HOH C . 
H 5 HOH   144 444 48  HOH   HOH C . 
H 5 HOH   145 445 282 HOH   HOH C . 
H 5 HOH   146 446 214 HOH   HOH C . 
H 5 HOH   147 447 188 HOH   HOH C . 
H 5 HOH   148 448 35  HOH   HOH C . 
H 5 HOH   149 449 373 HOH   HOH C . 
H 5 HOH   150 450 51  HOH   HOH C . 
H 5 HOH   151 451 201 HOH   HOH C . 
H 5 HOH   152 452 368 HOH   HOH C . 
H 5 HOH   153 453 59  HOH   HOH C . 
H 5 HOH   154 454 338 HOH   HOH C . 
H 5 HOH   155 455 163 HOH   HOH C . 
H 5 HOH   156 456 118 HOH   HOH C . 
H 5 HOH   157 457 322 HOH   HOH C . 
H 5 HOH   158 458 403 HOH   HOH C . 
H 5 HOH   159 459 378 HOH   HOH C . 
H 5 HOH   160 460 395 HOH   HOH C . 
H 5 HOH   161 461 146 HOH   HOH C . 
H 5 HOH   162 462 406 HOH   HOH C . 
H 5 HOH   163 463 181 HOH   HOH C . 
H 5 HOH   164 464 411 HOH   HOH C . 
H 5 HOH   165 465 277 HOH   HOH C . 
H 5 HOH   166 466 331 HOH   HOH C . 
H 5 HOH   167 467 243 HOH   HOH C . 
H 5 HOH   168 468 161 HOH   HOH C . 
H 5 HOH   169 469 405 HOH   HOH C . 
H 5 HOH   170 470 265 HOH   HOH C . 
H 5 HOH   171 471 334 HOH   HOH C . 
H 5 HOH   172 472 328 HOH   HOH C . 
H 5 HOH   173 473 314 HOH   HOH C . 
H 5 HOH   174 474 410 HOH   HOH C . 
H 5 HOH   175 475 290 HOH   HOH C . 
H 5 HOH   176 476 231 HOH   HOH C . 
H 5 HOH   177 477 204 HOH   HOH C . 
H 5 HOH   178 478 253 HOH   HOH C . 
H 5 HOH   179 479 271 HOH   HOH C . 
H 5 HOH   180 480 299 HOH   HOH C . 
H 5 HOH   181 481 375 HOH   HOH C . 
H 5 HOH   182 482 287 HOH   HOH C . 
H 5 HOH   183 483 280 HOH   HOH C . 
H 5 HOH   184 484 289 HOH   HOH C . 
H 5 HOH   185 485 305 HOH   HOH C . 
H 5 HOH   186 486 376 HOH   HOH C . 
H 5 HOH   187 487 86  HOH   HOH C . 
H 5 HOH   188 488 134 HOH   HOH C . 
H 5 HOH   189 489 210 HOH   HOH C . 
H 5 HOH   190 490 241 HOH   HOH C . 
H 5 HOH   191 491 261 HOH   HOH C . 
H 5 HOH   192 492 170 HOH   HOH C . 
H 5 HOH   193 493 11  HOH   HOH C . 
H 5 HOH   194 494 121 HOH   HOH C . 
H 5 HOH   195 495 244 HOH   HOH C . 
H 5 HOH   196 496 298 HOH   HOH C . 
H 5 HOH   197 497 297 HOH   HOH C . 
H 5 HOH   198 498 224 HOH   HOH C . 
H 5 HOH   199 499 333 HOH   HOH C . 
H 5 HOH   200 500 304 HOH   HOH C . 
H 5 HOH   201 501 195 HOH   HOH C . 
# 
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           7I52 
_cell.length_a           86.656 
_cell.length_b           57.097 
_cell.length_c           64.783 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.72 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I52 
_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          7I52 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.51 
_exptl_crystal.density_percent_sol   51.05 
_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                     7I52 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.56 
_reflns.d_resolution_high            1.15 
_reflns.number_obs                   85293 
_reflns.percent_possible_obs         76.3 
_reflns.pdbx_Rmerge_I_obs            0.038 
_reflns.pdbx_netI_over_sigmaI        27.2 
_reflns.pdbx_redundancy              5.3 
_reflns.pdbx_Rrim_I_all              0.041 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     448038 
_reflns.pdbx_chi_squared             1.02 
_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                  1.15 
_reflns_shell.d_res_low                   1.17 
_reflns_shell.number_measured_all         307 
_reflns_shell.number_unique_obs           305 
_reflns_shell.Rmerge_I_obs                0.159 
_reflns_shell.pdbx_chi_squared            0.05 
_reflns_shell.pdbx_redundancy             1.0 
_reflns_shell.percent_possible_obs        5.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.7 
_reflns_shell.pdbx_Rrim_I_all             0.224 
_reflns_shell.pdbx_Rpim_I_all             0.159 
_reflns_shell.pdbx_CC_half                0.811 
_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                                 7I52 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     85250 
_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                             16.53 
_refine.ls_d_res_high                            1.150 
_refine.ls_percent_reflns_obs                    76.4 
_refine.ls_R_factor_obs                          0.1758 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1752 
_refine.ls_R_factor_R_free                       0.1857 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.030 
_refine.ls_number_reflns_R_free                  4290 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.965 
_refine.correlation_coeff_Fo_to_Fc_free          0.965 
_refine.B_iso_mean                               18.55 
_refine.aniso_B[1][1]                            -0.92150 
_refine.aniso_B[2][2]                            0.36750 
_refine.aniso_B[3][3]                            0.55390 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.64330 
_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             0.041 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.041 
_refine.pdbx_overall_SU_R_Blow_DPI               0.044 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.043 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I52 
_refine_analyze.Luzzati_coordinate_error_obs    0.14 
_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        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             404 
_refine_hist.number_atoms_total               2600 
_refine_hist.d_res_high                       1.150 
_refine_hist.d_res_low                        16.53 
# 
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                  0.014 ? 2.00  2273 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.16  ? 2.00  3101 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  764  '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  408  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2273 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           5.25  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.23 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  280  '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  2129 '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                       1.15 
_refine_ls_shell.d_res_low                        1.20 
_refine_ls_shell.number_reflns_R_work             1609 
_refine_ls_shell.R_factor_R_work                  0.2920 
_refine_ls_shell.percent_reflns_obs               12.30 
_refine_ls_shell.R_factor_R_free                  0.3070 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.63 
_refine_ls_shell.number_reflns_R_free             96 
_refine_ls_shell.number_reflns_all                1705 
_refine_ls_shell.R_factor_all                     0.2928 
# 
_struct.entry_id                  7I52 
_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-0036725-001 (A71EV2A-x4777)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I52 
_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 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I52 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I52 C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_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 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 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 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.226 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.292 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.086 ? ? 
# 
_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 ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 107.7 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 104.7 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.4 ? 
4  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.0 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.4 ? 
6  SG ? A CYS 110 ? A CYS 116 ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 120.3 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 108.9 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.8 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.4 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.0 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 102.1 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.8 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 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 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 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  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 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 SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I52 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 CB C SER 66  ? ? O C HOH 304 ? ? 1.59 
2 1 O  A HOH 513 ? ? O A HOH 549 ? ? 1.64 
3 1 O  C HOH 320 ? ? O C HOH 384 ? ? 1.82 
4 1 CB A SER 105 ? ? O A HOH 402 ? ? 2.02 
5 1 O  C HOH 382 ? ? O C HOH 390 ? ? 2.03 
6 1 O  A HOH 538 ? ? O A HOH 595 ? ? 2.10 
# 
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 ? ? -104.28 40.07 
2 1 ASN C 14 ? ? -105.02 40.76 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 14.8609 8.1131   14.3735 -0.0155 -0.0153 -0.0029 0.0092 -0.0017 0.0052 1.2250 0.7160 0.6541 0.7516 
-0.6186 -0.3591 0.0007 0.0528 0.0995 0.0347 0.0438 0.0185 -0.0176 -0.0619 -0.0445 
'X-RAY DIFFRACTION' 2 ? refined 25.8200 -20.1981 17.7552 -0.0187 -0.0111 0.0102  0.0079 0.0012  0.0163 0.5482 0.8254 0.1843 
-0.1493 -0.1371 -0.0889 0.0093 0.0110 0.1007 0.0247 0.0333 0.0265 0.0295  0.0057  -0.0427 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? C HOH 500 ? 6.22 . 
2 1 O ? C HOH 501 ? 6.35 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A ALA 147 ? A ALA 141 
2 1 Y 1 A MET 148 ? A MET 142 
3 1 Y 1 A GLU 149 ? A GLU 143 
4 1 Y 1 A GLN 150 ? A GLN 144 
5 1 Y 1 C ALA 147 ? B ALA 141 
6 1 Y 1 C MET 148 ? B MET 142 
7 1 Y 1 C GLU 149 ? B GLU 143 
8 1 Y 1 C GLN 150 ? B 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 
A1B3J N1   N  N N 1   
A1B3J C4   C  Y N 2   
A1B3J C5   C  N N 3   
A1B3J C6   C  Y N 4   
A1B3J C7   C  Y N 5   
A1B3J C8   C  N N 6   
A1B3J C10  C  N N 7   
A1B3J C13  C  N N 8   
A1B3J O2   O  N N 9   
A1B3J C12  C  N R 10  
A1B3J S    S  N N 11  
A1B3J C11  C  N N 12  
A1B3J C14  C  N N 13  
A1B3J N    N  N N 14  
A1B3J C9   C  N N 15  
A1B3J O1   O  N N 16  
A1B3J C1   C  Y N 17  
A1B3J O    O  N N 18  
A1B3J C    C  N N 19  
A1B3J F2   F  N N 20  
A1B3J F1   F  N N 21  
A1B3J F    F  N N 22  
A1B3J C3   C  Y N 23  
A1B3J C2   C  Y N 24  
A1B3J H14  H  N N 25  
A1B3J H13  H  N N 26  
A1B3J H6   H  N N 27  
A1B3J H7   H  N N 28  
A1B3J H8   H  N N 29  
A1B3J H9   H  N N 30  
A1B3J H10  H  N N 31  
A1B3J H    H  N N 32  
A1B3J H12  H  N N 33  
A1B3J H11  H  N N 34  
A1B3J H16  H  N N 35  
A1B3J H15  H  N N 36  
A1B3J H2   H  N N 37  
A1B3J H1   H  N N 38  
A1B3J H3   H  N N 39  
A1B3J H5   H  N N 40  
A1B3J H4   H  N N 41  
ALA   N    N  N N 42  
ALA   CA   C  N S 43  
ALA   C    C  N N 44  
ALA   O    O  N N 45  
ALA   CB   C  N N 46  
ALA   OXT  O  N N 47  
ALA   H    H  N N 48  
ALA   H2   H  N N 49  
ALA   HA   H  N N 50  
ALA   HB1  H  N N 51  
ALA   HB2  H  N N 52  
ALA   HB3  H  N N 53  
ALA   HXT  H  N N 54  
ARG   N    N  N N 55  
ARG   CA   C  N S 56  
ARG   C    C  N N 57  
ARG   O    O  N N 58  
ARG   CB   C  N N 59  
ARG   CG   C  N N 60  
ARG   CD   C  N N 61  
ARG   NE   N  N N 62  
ARG   CZ   C  N N 63  
ARG   NH1  N  N N 64  
ARG   NH2  N  N N 65  
ARG   OXT  O  N N 66  
ARG   H    H  N N 67  
ARG   H2   H  N N 68  
ARG   HA   H  N N 69  
ARG   HB2  H  N N 70  
ARG   HB3  H  N N 71  
ARG   HG2  H  N N 72  
ARG   HG3  H  N N 73  
ARG   HD2  H  N N 74  
ARG   HD3  H  N N 75  
ARG   HE   H  N N 76  
ARG   HH11 H  N N 77  
ARG   HH12 H  N N 78  
ARG   HH21 H  N N 79  
ARG   HH22 H  N N 80  
ARG   HXT  H  N N 81  
ASN   N    N  N N 82  
ASN   CA   C  N S 83  
ASN   C    C  N N 84  
ASN   O    O  N N 85  
ASN   CB   C  N N 86  
ASN   CG   C  N N 87  
ASN   OD1  O  N N 88  
ASN   ND2  N  N N 89  
ASN   OXT  O  N N 90  
ASN   H    H  N N 91  
ASN   H2   H  N N 92  
ASN   HA   H  N N 93  
ASN   HB2  H  N N 94  
ASN   HB3  H  N N 95  
ASN   HD21 H  N N 96  
ASN   HD22 H  N N 97  
ASN   HXT  H  N N 98  
ASP   N    N  N N 99  
ASP   CA   C  N S 100 
ASP   C    C  N N 101 
ASP   O    O  N N 102 
ASP   CB   C  N N 103 
ASP   CG   C  N N 104 
ASP   OD1  O  N N 105 
ASP   OD2  O  N N 106 
ASP   OXT  O  N N 107 
ASP   H    H  N N 108 
ASP   H2   H  N N 109 
ASP   HA   H  N N 110 
ASP   HB2  H  N N 111 
ASP   HB3  H  N N 112 
ASP   HD2  H  N N 113 
ASP   HXT  H  N N 114 
CYS   N    N  N N 115 
CYS   CA   C  N R 116 
CYS   C    C  N N 117 
CYS   O    O  N N 118 
CYS   CB   C  N N 119 
CYS   SG   S  N N 120 
CYS   OXT  O  N N 121 
CYS   H    H  N N 122 
CYS   H2   H  N N 123 
CYS   HA   H  N N 124 
CYS   HB2  H  N N 125 
CYS   HB3  H  N N 126 
CYS   HG   H  N N 127 
CYS   HXT  H  N N 128 
DMS   S    S  N N 129 
DMS   O    O  N N 130 
DMS   C1   C  N N 131 
DMS   C2   C  N N 132 
DMS   H11  H  N N 133 
DMS   H12  H  N N 134 
DMS   H13  H  N N 135 
DMS   H21  H  N N 136 
DMS   H22  H  N N 137 
DMS   H23  H  N N 138 
GLN   N    N  N N 139 
GLN   CA   C  N S 140 
GLN   C    C  N N 141 
GLN   O    O  N N 142 
GLN   CB   C  N N 143 
GLN   CG   C  N N 144 
GLN   CD   C  N N 145 
GLN   OE1  O  N N 146 
GLN   NE2  N  N N 147 
GLN   OXT  O  N N 148 
GLN   H    H  N N 149 
GLN   H2   H  N N 150 
GLN   HA   H  N N 151 
GLN   HB2  H  N N 152 
GLN   HB3  H  N N 153 
GLN   HG2  H  N N 154 
GLN   HG3  H  N N 155 
GLN   HE21 H  N N 156 
GLN   HE22 H  N N 157 
GLN   HXT  H  N N 158 
GLU   N    N  N N 159 
GLU   CA   C  N S 160 
GLU   C    C  N N 161 
GLU   O    O  N N 162 
GLU   CB   C  N N 163 
GLU   CG   C  N N 164 
GLU   CD   C  N N 165 
GLU   OE1  O  N N 166 
GLU   OE2  O  N N 167 
GLU   OXT  O  N N 168 
GLU   H    H  N N 169 
GLU   H2   H  N N 170 
GLU   HA   H  N N 171 
GLU   HB2  H  N N 172 
GLU   HB3  H  N N 173 
GLU   HG2  H  N N 174 
GLU   HG3  H  N N 175 
GLU   HE2  H  N N 176 
GLU   HXT  H  N N 177 
GLY   N    N  N N 178 
GLY   CA   C  N N 179 
GLY   C    C  N N 180 
GLY   O    O  N N 181 
GLY   OXT  O  N N 182 
GLY   H    H  N N 183 
GLY   H2   H  N N 184 
GLY   HA2  H  N N 185 
GLY   HA3  H  N N 186 
GLY   HXT  H  N N 187 
HIS   N    N  N N 188 
HIS   CA   C  N S 189 
HIS   C    C  N N 190 
HIS   O    O  N N 191 
HIS   CB   C  N N 192 
HIS   CG   C  Y N 193 
HIS   ND1  N  Y N 194 
HIS   CD2  C  Y N 195 
HIS   CE1  C  Y N 196 
HIS   NE2  N  Y N 197 
HIS   OXT  O  N N 198 
HIS   H    H  N N 199 
HIS   H2   H  N N 200 
HIS   HA   H  N N 201 
HIS   HB2  H  N N 202 
HIS   HB3  H  N N 203 
HIS   HD1  H  N N 204 
HIS   HD2  H  N N 205 
HIS   HE1  H  N N 206 
HIS   HE2  H  N N 207 
HIS   HXT  H  N N 208 
HOH   O    O  N N 209 
HOH   H1   H  N N 210 
HOH   H2   H  N N 211 
ILE   N    N  N N 212 
ILE   CA   C  N S 213 
ILE   C    C  N N 214 
ILE   O    O  N N 215 
ILE   CB   C  N S 216 
ILE   CG1  C  N N 217 
ILE   CG2  C  N N 218 
ILE   CD1  C  N N 219 
ILE   OXT  O  N N 220 
ILE   H    H  N N 221 
ILE   H2   H  N N 222 
ILE   HA   H  N N 223 
ILE   HB   H  N N 224 
ILE   HG12 H  N N 225 
ILE   HG13 H  N N 226 
ILE   HG21 H  N N 227 
ILE   HG22 H  N N 228 
ILE   HG23 H  N N 229 
ILE   HD11 H  N N 230 
ILE   HD12 H  N N 231 
ILE   HD13 H  N N 232 
ILE   HXT  H  N N 233 
LEU   N    N  N N 234 
LEU   CA   C  N S 235 
LEU   C    C  N N 236 
LEU   O    O  N N 237 
LEU   CB   C  N N 238 
LEU   CG   C  N N 239 
LEU   CD1  C  N N 240 
LEU   CD2  C  N N 241 
LEU   OXT  O  N N 242 
LEU   H    H  N N 243 
LEU   H2   H  N N 244 
LEU   HA   H  N N 245 
LEU   HB2  H  N N 246 
LEU   HB3  H  N N 247 
LEU   HG   H  N N 248 
LEU   HD11 H  N N 249 
LEU   HD12 H  N N 250 
LEU   HD13 H  N N 251 
LEU   HD21 H  N N 252 
LEU   HD22 H  N N 253 
LEU   HD23 H  N N 254 
LEU   HXT  H  N N 255 
LYS   N    N  N N 256 
LYS   CA   C  N S 257 
LYS   C    C  N N 258 
LYS   O    O  N N 259 
LYS   CB   C  N N 260 
LYS   CG   C  N N 261 
LYS   CD   C  N N 262 
LYS   CE   C  N N 263 
LYS   NZ   N  N N 264 
LYS   OXT  O  N N 265 
LYS   H    H  N N 266 
LYS   H2   H  N N 267 
LYS   HA   H  N N 268 
LYS   HB2  H  N N 269 
LYS   HB3  H  N N 270 
LYS   HG2  H  N N 271 
LYS   HG3  H  N N 272 
LYS   HD2  H  N N 273 
LYS   HD3  H  N N 274 
LYS   HE2  H  N N 275 
LYS   HE3  H  N N 276 
LYS   HZ1  H  N N 277 
LYS   HZ2  H  N N 278 
LYS   HZ3  H  N N 279 
LYS   HXT  H  N N 280 
MET   N    N  N N 281 
MET   CA   C  N S 282 
MET   C    C  N N 283 
MET   O    O  N N 284 
MET   CB   C  N N 285 
MET   CG   C  N N 286 
MET   SD   S  N N 287 
MET   CE   C  N N 288 
MET   OXT  O  N N 289 
MET   H    H  N N 290 
MET   H2   H  N N 291 
MET   HA   H  N N 292 
MET   HB2  H  N N 293 
MET   HB3  H  N N 294 
MET   HG2  H  N N 295 
MET   HG3  H  N N 296 
MET   HE1  H  N N 297 
MET   HE2  H  N N 298 
MET   HE3  H  N N 299 
MET   HXT  H  N N 300 
PHE   N    N  N N 301 
PHE   CA   C  N S 302 
PHE   C    C  N N 303 
PHE   O    O  N N 304 
PHE   CB   C  N N 305 
PHE   CG   C  Y N 306 
PHE   CD1  C  Y N 307 
PHE   CD2  C  Y N 308 
PHE   CE1  C  Y N 309 
PHE   CE2  C  Y N 310 
PHE   CZ   C  Y N 311 
PHE   OXT  O  N N 312 
PHE   H    H  N N 313 
PHE   H2   H  N N 314 
PHE   HA   H  N N 315 
PHE   HB2  H  N N 316 
PHE   HB3  H  N N 317 
PHE   HD1  H  N N 318 
PHE   HD2  H  N N 319 
PHE   HE1  H  N N 320 
PHE   HE2  H  N N 321 
PHE   HZ   H  N N 322 
PHE   HXT  H  N N 323 
PRO   N    N  N N 324 
PRO   CA   C  N S 325 
PRO   C    C  N N 326 
PRO   O    O  N N 327 
PRO   CB   C  N N 328 
PRO   CG   C  N N 329 
PRO   CD   C  N N 330 
PRO   OXT  O  N N 331 
PRO   H    H  N N 332 
PRO   HA   H  N N 333 
PRO   HB2  H  N N 334 
PRO   HB3  H  N N 335 
PRO   HG2  H  N N 336 
PRO   HG3  H  N N 337 
PRO   HD2  H  N N 338 
PRO   HD3  H  N N 339 
PRO   HXT  H  N N 340 
SER   N    N  N N 341 
SER   CA   C  N S 342 
SER   C    C  N N 343 
SER   O    O  N N 344 
SER   CB   C  N N 345 
SER   OG   O  N N 346 
SER   OXT  O  N N 347 
SER   H    H  N N 348 
SER   H2   H  N N 349 
SER   HA   H  N N 350 
SER   HB2  H  N N 351 
SER   HB3  H  N N 352 
SER   HG   H  N N 353 
SER   HXT  H  N N 354 
THR   N    N  N N 355 
THR   CA   C  N S 356 
THR   C    C  N N 357 
THR   O    O  N N 358 
THR   CB   C  N R 359 
THR   OG1  O  N N 360 
THR   CG2  C  N N 361 
THR   OXT  O  N N 362 
THR   H    H  N N 363 
THR   H2   H  N N 364 
THR   HA   H  N N 365 
THR   HB   H  N N 366 
THR   HG1  H  N N 367 
THR   HG21 H  N N 368 
THR   HG22 H  N N 369 
THR   HG23 H  N N 370 
THR   HXT  H  N N 371 
TRP   N    N  N N 372 
TRP   CA   C  N S 373 
TRP   C    C  N N 374 
TRP   O    O  N N 375 
TRP   CB   C  N N 376 
TRP   CG   C  Y N 377 
TRP   CD1  C  Y N 378 
TRP   CD2  C  Y N 379 
TRP   NE1  N  Y N 380 
TRP   CE2  C  Y N 381 
TRP   CE3  C  Y N 382 
TRP   CZ2  C  Y N 383 
TRP   CZ3  C  Y N 384 
TRP   CH2  C  Y N 385 
TRP   OXT  O  N N 386 
TRP   H    H  N N 387 
TRP   H2   H  N N 388 
TRP   HA   H  N N 389 
TRP   HB2  H  N N 390 
TRP   HB3  H  N N 391 
TRP   HD1  H  N N 392 
TRP   HE1  H  N N 393 
TRP   HE3  H  N N 394 
TRP   HZ2  H  N N 395 
TRP   HZ3  H  N N 396 
TRP   HH2  H  N N 397 
TRP   HXT  H  N N 398 
TYR   N    N  N N 399 
TYR   CA   C  N S 400 
TYR   C    C  N N 401 
TYR   O    O  N N 402 
TYR   CB   C  N N 403 
TYR   CG   C  Y N 404 
TYR   CD1  C  Y N 405 
TYR   CD2  C  Y N 406 
TYR   CE1  C  Y N 407 
TYR   CE2  C  Y N 408 
TYR   CZ   C  Y N 409 
TYR   OH   O  N N 410 
TYR   OXT  O  N N 411 
TYR   H    H  N N 412 
TYR   H2   H  N N 413 
TYR   HA   H  N N 414 
TYR   HB2  H  N N 415 
TYR   HB3  H  N N 416 
TYR   HD1  H  N N 417 
TYR   HD2  H  N N 418 
TYR   HE1  H  N N 419 
TYR   HE2  H  N N 420 
TYR   HH   H  N N 421 
TYR   HXT  H  N N 422 
VAL   N    N  N N 423 
VAL   CA   C  N S 424 
VAL   C    C  N N 425 
VAL   O    O  N N 426 
VAL   CB   C  N N 427 
VAL   CG1  C  N N 428 
VAL   CG2  C  N N 429 
VAL   OXT  O  N N 430 
VAL   H    H  N N 431 
VAL   H2   H  N N 432 
VAL   HA   H  N N 433 
VAL   HB   H  N N 434 
VAL   HG11 H  N N 435 
VAL   HG12 H  N N 436 
VAL   HG13 H  N N 437 
VAL   HG21 H  N N 438 
VAL   HG22 H  N N 439 
VAL   HG23 H  N N 440 
VAL   HXT  H  N N 441 
ZN    ZN   ZN N N 442 
# 
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 
A1B3J C   O    sing N N 1   
A1B3J O   C1   sing N N 2   
A1B3J C1  C2   doub Y N 3   
A1B3J C2  C3   sing Y N 4   
A1B3J C3  C4   doub Y N 5   
A1B3J C5  C4   sing N N 6   
A1B3J F   C5   sing N N 7   
A1B3J F1  C5   sing N N 8   
A1B3J F2  C5   sing N N 9   
A1B3J C4  C6   sing Y N 10  
A1B3J C6  C7   doub Y N 11  
A1B3J C1  C7   sing Y N 12  
A1B3J C7  C8   sing N N 13  
A1B3J C8  C9   sing N N 14  
A1B3J O1  C9   doub N N 15  
A1B3J C9  N    sing N N 16  
A1B3J N   C10  sing N N 17  
A1B3J C10 C11  sing N N 18  
A1B3J C11 S    sing N N 19  
A1B3J S   C12  sing N N 20  
A1B3J C12 C13  sing N N 21  
A1B3J N1  C13  sing N N 22  
A1B3J C13 O2   doub N N 23  
A1B3J C14 C12  sing N N 24  
A1B3J N   C14  sing N N 25  
A1B3J N1  H14  sing N N 26  
A1B3J N1  H13  sing N N 27  
A1B3J C6  H6   sing N N 28  
A1B3J C8  H7   sing N N 29  
A1B3J C8  H8   sing N N 30  
A1B3J C10 H9   sing N N 31  
A1B3J C10 H10  sing N N 32  
A1B3J C12 H    sing N N 33  
A1B3J C11 H12  sing N N 34  
A1B3J C11 H11  sing N N 35  
A1B3J C14 H16  sing N N 36  
A1B3J C14 H15  sing N N 37  
A1B3J C   H2   sing N N 38  
A1B3J C   H1   sing N N 39  
A1B3J C   H3   sing N N 40  
A1B3J C3  H5   sing N N 41  
A1B3J C2  H4   sing N N 42  
ALA   N   CA   sing N N 43  
ALA   N   H    sing N N 44  
ALA   N   H2   sing N N 45  
ALA   CA  C    sing N N 46  
ALA   CA  CB   sing N N 47  
ALA   CA  HA   sing N N 48  
ALA   C   O    doub N N 49  
ALA   C   OXT  sing N N 50  
ALA   CB  HB1  sing N N 51  
ALA   CB  HB2  sing N N 52  
ALA   CB  HB3  sing N N 53  
ALA   OXT HXT  sing N N 54  
ARG   N   CA   sing N N 55  
ARG   N   H    sing N N 56  
ARG   N   H2   sing N N 57  
ARG   CA  C    sing N N 58  
ARG   CA  CB   sing N N 59  
ARG   CA  HA   sing N N 60  
ARG   C   O    doub N N 61  
ARG   C   OXT  sing N N 62  
ARG   CB  CG   sing N N 63  
ARG   CB  HB2  sing N N 64  
ARG   CB  HB3  sing N N 65  
ARG   CG  CD   sing N N 66  
ARG   CG  HG2  sing N N 67  
ARG   CG  HG3  sing N N 68  
ARG   CD  NE   sing N N 69  
ARG   CD  HD2  sing N N 70  
ARG   CD  HD3  sing N N 71  
ARG   NE  CZ   sing N N 72  
ARG   NE  HE   sing N N 73  
ARG   CZ  NH1  sing N N 74  
ARG   CZ  NH2  doub N N 75  
ARG   NH1 HH11 sing N N 76  
ARG   NH1 HH12 sing N N 77  
ARG   NH2 HH21 sing N N 78  
ARG   NH2 HH22 sing N N 79  
ARG   OXT HXT  sing N N 80  
ASN   N   CA   sing N N 81  
ASN   N   H    sing N N 82  
ASN   N   H2   sing N N 83  
ASN   CA  C    sing N N 84  
ASN   CA  CB   sing N N 85  
ASN   CA  HA   sing N N 86  
ASN   C   O    doub N N 87  
ASN   C   OXT  sing N N 88  
ASN   CB  CG   sing N N 89  
ASN   CB  HB2  sing N N 90  
ASN   CB  HB3  sing N N 91  
ASN   CG  OD1  doub N N 92  
ASN   CG  ND2  sing N N 93  
ASN   ND2 HD21 sing N N 94  
ASN   ND2 HD22 sing N N 95  
ASN   OXT HXT  sing N N 96  
ASP   N   CA   sing N N 97  
ASP   N   H    sing N N 98  
ASP   N   H2   sing N N 99  
ASP   CA  C    sing N N 100 
ASP   CA  CB   sing N N 101 
ASP   CA  HA   sing N N 102 
ASP   C   O    doub N N 103 
ASP   C   OXT  sing N N 104 
ASP   CB  CG   sing N N 105 
ASP   CB  HB2  sing N N 106 
ASP   CB  HB3  sing N N 107 
ASP   CG  OD1  doub N N 108 
ASP   CG  OD2  sing N N 109 
ASP   OD2 HD2  sing N N 110 
ASP   OXT HXT  sing N N 111 
CYS   N   CA   sing N N 112 
CYS   N   H    sing N N 113 
CYS   N   H2   sing N N 114 
CYS   CA  C    sing N N 115 
CYS   CA  CB   sing N N 116 
CYS   CA  HA   sing N N 117 
CYS   C   O    doub N N 118 
CYS   C   OXT  sing N N 119 
CYS   CB  SG   sing N N 120 
CYS   CB  HB2  sing N N 121 
CYS   CB  HB3  sing N N 122 
CYS   SG  HG   sing N N 123 
CYS   OXT HXT  sing N N 124 
DMS   S   O    doub N N 125 
DMS   S   C1   sing N N 126 
DMS   S   C2   sing N N 127 
DMS   C1  H11  sing N N 128 
DMS   C1  H12  sing N N 129 
DMS   C1  H13  sing N N 130 
DMS   C2  H21  sing N N 131 
DMS   C2  H22  sing N N 132 
DMS   C2  H23  sing N N 133 
GLN   N   CA   sing N N 134 
GLN   N   H    sing N N 135 
GLN   N   H2   sing N N 136 
GLN   CA  C    sing N N 137 
GLN   CA  CB   sing N N 138 
GLN   CA  HA   sing N N 139 
GLN   C   O    doub N N 140 
GLN   C   OXT  sing N N 141 
GLN   CB  CG   sing N N 142 
GLN   CB  HB2  sing N N 143 
GLN   CB  HB3  sing N N 144 
GLN   CG  CD   sing N N 145 
GLN   CG  HG2  sing N N 146 
GLN   CG  HG3  sing N N 147 
GLN   CD  OE1  doub N N 148 
GLN   CD  NE2  sing N N 149 
GLN   NE2 HE21 sing N N 150 
GLN   NE2 HE22 sing N N 151 
GLN   OXT HXT  sing N N 152 
GLU   N   CA   sing N N 153 
GLU   N   H    sing N N 154 
GLU   N   H2   sing N N 155 
GLU   CA  C    sing N N 156 
GLU   CA  CB   sing N N 157 
GLU   CA  HA   sing N N 158 
GLU   C   O    doub N N 159 
GLU   C   OXT  sing N N 160 
GLU   CB  CG   sing N N 161 
GLU   CB  HB2  sing N N 162 
GLU   CB  HB3  sing N N 163 
GLU   CG  CD   sing N N 164 
GLU   CG  HG2  sing N N 165 
GLU   CG  HG3  sing N N 166 
GLU   CD  OE1  doub N N 167 
GLU   CD  OE2  sing N N 168 
GLU   OE2 HE2  sing N N 169 
GLU   OXT HXT  sing N N 170 
GLY   N   CA   sing N N 171 
GLY   N   H    sing N N 172 
GLY   N   H2   sing N N 173 
GLY   CA  C    sing N N 174 
GLY   CA  HA2  sing N N 175 
GLY   CA  HA3  sing N N 176 
GLY   C   O    doub N N 177 
GLY   C   OXT  sing N N 178 
GLY   OXT HXT  sing N N 179 
HIS   N   CA   sing N N 180 
HIS   N   H    sing N N 181 
HIS   N   H2   sing N N 182 
HIS   CA  C    sing N N 183 
HIS   CA  CB   sing N N 184 
HIS   CA  HA   sing N N 185 
HIS   C   O    doub N N 186 
HIS   C   OXT  sing N N 187 
HIS   CB  CG   sing N N 188 
HIS   CB  HB2  sing N N 189 
HIS   CB  HB3  sing N N 190 
HIS   CG  ND1  sing Y N 191 
HIS   CG  CD2  doub Y N 192 
HIS   ND1 CE1  doub Y N 193 
HIS   ND1 HD1  sing N N 194 
HIS   CD2 NE2  sing Y N 195 
HIS   CD2 HD2  sing N N 196 
HIS   CE1 NE2  sing Y N 197 
HIS   CE1 HE1  sing N N 198 
HIS   NE2 HE2  sing N N 199 
HIS   OXT HXT  sing N N 200 
HOH   O   H1   sing N N 201 
HOH   O   H2   sing N N 202 
ILE   N   CA   sing N N 203 
ILE   N   H    sing N N 204 
ILE   N   H2   sing N N 205 
ILE   CA  C    sing N N 206 
ILE   CA  CB   sing N N 207 
ILE   CA  HA   sing N N 208 
ILE   C   O    doub N N 209 
ILE   C   OXT  sing N N 210 
ILE   CB  CG1  sing N N 211 
ILE   CB  CG2  sing N N 212 
ILE   CB  HB   sing N N 213 
ILE   CG1 CD1  sing N N 214 
ILE   CG1 HG12 sing N N 215 
ILE   CG1 HG13 sing N N 216 
ILE   CG2 HG21 sing N N 217 
ILE   CG2 HG22 sing N N 218 
ILE   CG2 HG23 sing N N 219 
ILE   CD1 HD11 sing N N 220 
ILE   CD1 HD12 sing N N 221 
ILE   CD1 HD13 sing N N 222 
ILE   OXT HXT  sing N N 223 
LEU   N   CA   sing N N 224 
LEU   N   H    sing N N 225 
LEU   N   H2   sing N N 226 
LEU   CA  C    sing N N 227 
LEU   CA  CB   sing N N 228 
LEU   CA  HA   sing N N 229 
LEU   C   O    doub N N 230 
LEU   C   OXT  sing N N 231 
LEU   CB  CG   sing N N 232 
LEU   CB  HB2  sing N N 233 
LEU   CB  HB3  sing N N 234 
LEU   CG  CD1  sing N N 235 
LEU   CG  CD2  sing N N 236 
LEU   CG  HG   sing N N 237 
LEU   CD1 HD11 sing N N 238 
LEU   CD1 HD12 sing N N 239 
LEU   CD1 HD13 sing N N 240 
LEU   CD2 HD21 sing N N 241 
LEU   CD2 HD22 sing N N 242 
LEU   CD2 HD23 sing N N 243 
LEU   OXT HXT  sing N N 244 
LYS   N   CA   sing N N 245 
LYS   N   H    sing N N 246 
LYS   N   H2   sing N N 247 
LYS   CA  C    sing N N 248 
LYS   CA  CB   sing N N 249 
LYS   CA  HA   sing N N 250 
LYS   C   O    doub N N 251 
LYS   C   OXT  sing N N 252 
LYS   CB  CG   sing N N 253 
LYS   CB  HB2  sing N N 254 
LYS   CB  HB3  sing N N 255 
LYS   CG  CD   sing N N 256 
LYS   CG  HG2  sing N N 257 
LYS   CG  HG3  sing N N 258 
LYS   CD  CE   sing N N 259 
LYS   CD  HD2  sing N N 260 
LYS   CD  HD3  sing N N 261 
LYS   CE  NZ   sing N N 262 
LYS   CE  HE2  sing N N 263 
LYS   CE  HE3  sing N N 264 
LYS   NZ  HZ1  sing N N 265 
LYS   NZ  HZ2  sing N N 266 
LYS   NZ  HZ3  sing N N 267 
LYS   OXT HXT  sing N N 268 
MET   N   CA   sing N N 269 
MET   N   H    sing N N 270 
MET   N   H2   sing N N 271 
MET   CA  C    sing N N 272 
MET   CA  CB   sing N N 273 
MET   CA  HA   sing N N 274 
MET   C   O    doub N N 275 
MET   C   OXT  sing N N 276 
MET   CB  CG   sing N N 277 
MET   CB  HB2  sing N N 278 
MET   CB  HB3  sing N N 279 
MET   CG  SD   sing N N 280 
MET   CG  HG2  sing N N 281 
MET   CG  HG3  sing N N 282 
MET   SD  CE   sing N N 283 
MET   CE  HE1  sing N N 284 
MET   CE  HE2  sing N N 285 
MET   CE  HE3  sing N N 286 
MET   OXT HXT  sing N N 287 
PHE   N   CA   sing N N 288 
PHE   N   H    sing N N 289 
PHE   N   H2   sing N N 290 
PHE   CA  C    sing N N 291 
PHE   CA  CB   sing N N 292 
PHE   CA  HA   sing N N 293 
PHE   C   O    doub N N 294 
PHE   C   OXT  sing N N 295 
PHE   CB  CG   sing N N 296 
PHE   CB  HB2  sing N N 297 
PHE   CB  HB3  sing N N 298 
PHE   CG  CD1  doub Y N 299 
PHE   CG  CD2  sing Y N 300 
PHE   CD1 CE1  sing Y N 301 
PHE   CD1 HD1  sing N N 302 
PHE   CD2 CE2  doub Y N 303 
PHE   CD2 HD2  sing N N 304 
PHE   CE1 CZ   doub Y N 305 
PHE   CE1 HE1  sing N N 306 
PHE   CE2 CZ   sing Y N 307 
PHE   CE2 HE2  sing N N 308 
PHE   CZ  HZ   sing N N 309 
PHE   OXT HXT  sing N N 310 
PRO   N   CA   sing N N 311 
PRO   N   CD   sing N N 312 
PRO   N   H    sing N N 313 
PRO   CA  C    sing N N 314 
PRO   CA  CB   sing N N 315 
PRO   CA  HA   sing N N 316 
PRO   C   O    doub N N 317 
PRO   C   OXT  sing N N 318 
PRO   CB  CG   sing N N 319 
PRO   CB  HB2  sing N N 320 
PRO   CB  HB3  sing N N 321 
PRO   CG  CD   sing N N 322 
PRO   CG  HG2  sing N N 323 
PRO   CG  HG3  sing N N 324 
PRO   CD  HD2  sing N N 325 
PRO   CD  HD3  sing N N 326 
PRO   OXT HXT  sing N N 327 
SER   N   CA   sing N N 328 
SER   N   H    sing N N 329 
SER   N   H2   sing N N 330 
SER   CA  C    sing N N 331 
SER   CA  CB   sing N N 332 
SER   CA  HA   sing N N 333 
SER   C   O    doub N N 334 
SER   C   OXT  sing N N 335 
SER   CB  OG   sing N N 336 
SER   CB  HB2  sing N N 337 
SER   CB  HB3  sing N N 338 
SER   OG  HG   sing N N 339 
SER   OXT HXT  sing N N 340 
THR   N   CA   sing N N 341 
THR   N   H    sing N N 342 
THR   N   H2   sing N N 343 
THR   CA  C    sing N N 344 
THR   CA  CB   sing N N 345 
THR   CA  HA   sing N N 346 
THR   C   O    doub N N 347 
THR   C   OXT  sing N N 348 
THR   CB  OG1  sing N N 349 
THR   CB  CG2  sing N N 350 
THR   CB  HB   sing N N 351 
THR   OG1 HG1  sing N N 352 
THR   CG2 HG21 sing N N 353 
THR   CG2 HG22 sing N N 354 
THR   CG2 HG23 sing N N 355 
THR   OXT HXT  sing N N 356 
TRP   N   CA   sing N N 357 
TRP   N   H    sing N N 358 
TRP   N   H2   sing N N 359 
TRP   CA  C    sing N N 360 
TRP   CA  CB   sing N N 361 
TRP   CA  HA   sing N N 362 
TRP   C   O    doub N N 363 
TRP   C   OXT  sing N N 364 
TRP   CB  CG   sing N N 365 
TRP   CB  HB2  sing N N 366 
TRP   CB  HB3  sing N N 367 
TRP   CG  CD1  doub Y N 368 
TRP   CG  CD2  sing Y N 369 
TRP   CD1 NE1  sing Y N 370 
TRP   CD1 HD1  sing N N 371 
TRP   CD2 CE2  doub Y N 372 
TRP   CD2 CE3  sing Y N 373 
TRP   NE1 CE2  sing Y N 374 
TRP   NE1 HE1  sing N N 375 
TRP   CE2 CZ2  sing Y N 376 
TRP   CE3 CZ3  doub Y N 377 
TRP   CE3 HE3  sing N N 378 
TRP   CZ2 CH2  doub Y N 379 
TRP   CZ2 HZ2  sing N N 380 
TRP   CZ3 CH2  sing Y N 381 
TRP   CZ3 HZ3  sing N N 382 
TRP   CH2 HH2  sing N N 383 
TRP   OXT HXT  sing N N 384 
TYR   N   CA   sing N N 385 
TYR   N   H    sing N N 386 
TYR   N   H2   sing N N 387 
TYR   CA  C    sing N N 388 
TYR   CA  CB   sing N N 389 
TYR   CA  HA   sing N N 390 
TYR   C   O    doub N N 391 
TYR   C   OXT  sing N N 392 
TYR   CB  CG   sing N N 393 
TYR   CB  HB2  sing N N 394 
TYR   CB  HB3  sing N N 395 
TYR   CG  CD1  doub Y N 396 
TYR   CG  CD2  sing Y N 397 
TYR   CD1 CE1  sing Y N 398 
TYR   CD1 HD1  sing N N 399 
TYR   CD2 CE2  doub Y N 400 
TYR   CD2 HD2  sing N N 401 
TYR   CE1 CZ   doub Y N 402 
TYR   CE1 HE1  sing N N 403 
TYR   CE2 CZ   sing Y N 404 
TYR   CE2 HE2  sing N N 405 
TYR   CZ  OH   sing N N 406 
TYR   OH  HH   sing N N 407 
TYR   OXT HXT  sing N N 408 
VAL   N   CA   sing N N 409 
VAL   N   H    sing N N 410 
VAL   N   H2   sing N N 411 
VAL   CA  C    sing N N 412 
VAL   CA  CB   sing N N 413 
VAL   CA  HA   sing N N 414 
VAL   C   O    doub N N 415 
VAL   C   OXT  sing N N 416 
VAL   CB  CG1  sing N N 417 
VAL   CB  CG2  sing N N 418 
VAL   CB  HB   sing N N 419 
VAL   CG1 HG11 sing N N 420 
VAL   CG1 HG12 sing N N 421 
VAL   CG1 HG13 sing N N 422 
VAL   CG2 HG21 sing N N 423 
VAL   CG2 HG22 sing N N 424 
VAL   CG2 HG23 sing N N 425 
VAL   OXT HXT  sing N N 426 
# 
_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                    7I52 
_atom_sites.fract_transf_matrix[1][1]   0.011540 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000953 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017514 
_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]   0.015489 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.670 8.164   24.808 1.00 14.68 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.923 8.236   24.029 1.00 14.17 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.052 7.021   23.107 1.00 13.99 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.319 6.022   23.276 1.00 14.85 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.106 8.285   25.001 1.00 16.77 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.190 7.065   25.704 1.00 20.46 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.974 7.082   22.139 1.00 12.75 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.243 5.975   21.235 1.00 12.17 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.662 6.428   19.864 1.00 10.93 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.367 7.558   19.477 1.00 12.50 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.333 5.569   19.162 1.00 10.36 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.824 5.921   17.820 1.00 10.61 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.797 4.702   16.932 1.00 10.26 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.698 3.559   17.401 1.00 11.42 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.274 6.445   17.940 1.00 11.80 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.876 4.937   15.618 1.00 10.09 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.109 3.886   14.617 1.00 9.99  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.567 3.981   14.230 1.00 11.01 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.070 5.088   13.924 1.00 11.01 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.256 4.090   13.357 1.00 9.71  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.758 4.266   13.702 1.00 11.83 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.429 2.903   12.388 1.00 11.39 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.961 4.788   12.484 1.00 12.33 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.275 2.843   14.195 1.00 10.35 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.683 2.806   13.801 1.00 11.49 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.800 1.977   12.531 1.00 11.81 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.797 0.732   12.588 1.00 12.39 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.571 2.222   14.932 1.00 12.51 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.608 3.122   16.140 1.00 12.45 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.485 4.199   16.204 1.00 13.52 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.766 2.906   17.222 1.00 13.81 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.475 5.077   17.287 1.00 13.94 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.788 3.752   18.339 1.00 14.11 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.623 4.855   18.342 1.00 14.35 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.632 5.722   19.431 1.00 17.05 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.841 2.622   11.370 1.00 11.91 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.936 1.990   10.058 1.00 12.09 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.178 2.481   9.347  1.00 13.46 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.424 3.694   9.283  1.00 12.46 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.646 2.246   9.214  1.00 13.56 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.299 3.737   9.119  1.00 14.71 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.798 1.625   7.833  1.00 14.75 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.039 1.568   8.872  1.00 14.15 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.278 2.002   8.221  1.00 14.80 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.104 2.887   9.150  1.00 13.81 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.217 2.590   10.354 1.00 13.67 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.570 4.027   8.620  1.00 12.96 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.268 5.012   9.457  1.00 12.85 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.359 6.202   9.757  1.00 11.90 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.860 7.338   9.884  1.00 12.64 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.627 5.461   8.880  1.00 14.20 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.696 4.395   9.011  1.00 17.84 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.463 4.331   9.994  1.00 20.55 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.735 3.508   8.055  1.00 17.50 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.089 5.924   10.015 1.00 11.10 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.119 6.955   10.368 1.00 10.54 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.453 6.636   11.699 1.00 10.36 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.175 5.448   12.030 1.00 11.21 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.005 7.026   9.283  1.00 11.24 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.510 7.409   7.911  1.00 12.80 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.144 8.629   7.691  1.00 14.42 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.337 6.560   6.832  1.00 14.35 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.614 8.982   6.427  1.00 14.85 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.749 6.931   5.553  1.00 15.97 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.362 8.148   5.359  1.00 16.08 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.817 8.538   4.109  1.00 20.00 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.104 7.688   12.434 1.00 10.29 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.297 7.626   13.653 1.00 10.56 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.074 8.496   13.412 1.00 10.24 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.229 9.702   13.120 1.00 10.69 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.124 8.160   14.866 1.00 11.15 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.350 8.487   16.125 1.00 12.15 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.278 8.886   17.296 1.00 13.07 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.724 9.961   18.132 1.00 13.33 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.027 9.775   19.252 1.00 15.04 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.728 8.540   19.663 1.00 16.26 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.585 10.821  19.945 1.00 14.72 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.870 7.906   13.483 1.00 9.48  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.602 8.637   13.236 1.00 9.40  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.918 8.832   14.577 1.00 10.17 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.624 7.841   15.283 1.00 10.84 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.675 7.828   12.304 1.00 10.01 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.434 8.676   11.949 1.00 10.78 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.377 7.330   11.038 1.00 11.26 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.673 10.099  14.928 1.00 9.38  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.049 10.445  16.231 0.50 9.39  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.091 10.416  16.244 0.50 11.39 ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 19.951 11.437  16.038 1.00 10.43 ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.814 12.065  14.946 1.00 11.24 ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.075 11.055  17.249 0.50 8.95  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.257 11.029  17.121 0.50 15.22 ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 22.981 9.974   17.776 0.50 10.44 ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.845 11.358  18.539 0.50 16.23 ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.834 12.289  16.661 0.50 6.65  ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.455 10.121  17.161 0.50 17.50 ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.113 11.608  17.079 1.00 9.85  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.121 12.687  17.024 1.00 10.07 ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 18.924 14.011  17.040 1.00 10.63 ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.858 14.190  17.848 1.00 10.74 ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.259 12.694  18.295 1.00 10.24 ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.390 11.455  18.398 1.00 10.94 ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.794 10.452  19.027 1.00 11.48 ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.220 11.494  17.748 1.00 11.38 ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.544 14.939  16.149 1.00 10.61 ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.297 16.223  16.091 1.00 11.10 ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.263 16.914  17.465 1.00 11.94 ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.290 17.474  17.879 1.00 12.79 ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.685 17.117  15.030 1.00 11.55 ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.486 18.427  14.757 1.00 12.10 ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.721 19.289  13.779 1.00 13.10 ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.459 20.498  13.332 1.00 14.58 ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.435 21.664  13.959 1.00 15.86 ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.848 21.779  15.139 1.00 16.13 ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.035 22.725  13.420 1.00 17.22 ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.121 16.815  18.179 1.00 11.29 ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.023 17.523  19.452 1.00 13.48 ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 18.899 16.939  20.562 1.00 13.95 ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.010 17.569  21.626 1.00 15.71 ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.556 17.687  19.903 1.00 14.81 ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.884 16.441  20.410 1.00 13.41 ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.274 15.539  19.556 1.00 13.03 ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.682 16.024  21.681 1.00 14.06 ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.730 14.577  20.322 1.00 14.23 ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 14.979 14.812  21.612 1.00 14.40 ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.412 15.707  20.390 1.00 13.60 ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.300 15.026  21.347 1.00 13.05 ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.755 14.984  20.894 1.00 14.17 ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.579 14.355  21.547 1.00 15.02 ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.780 13.613  21.659 1.00 12.60 ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.370 13.623  22.268 1.00 13.09 ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.901 12.180  22.513 1.00 14.03 ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.314 14.425  23.600 1.00 15.44 ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.078 15.613  19.734 1.00 13.20 ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.455 15.579  19.241 1.00 13.45 ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.436 16.224  20.220 1.00 14.22 ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.110 17.257  20.837 1.00 14.60 ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.527 16.282  17.877 1.00 13.12 ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.609 15.607  20.341 1.00 13.79 ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.667 16.127  21.256 1.00 13.60 ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.597 17.110  20.527 1.00 14.48 ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.550 17.259  19.283 1.00 13.83 ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.537 14.948  21.770 1.00 15.50 ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.253 14.399  20.647 1.00 15.11 ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.706 13.837  22.459 1.00 17.04 ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.525 17.778  21.260 1.00 14.54 ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.514 18.616  20.625 1.00 14.97 ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.357 17.808  19.657 1.00 13.76 ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.634 18.274  18.552 1.00 13.98 ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.436 19.287  21.682 1.00 16.41 ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.702 19.913  21.074 1.00 23.52 ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.654 21.074  20.313 1.00 27.06 ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 32.961 19.395  20.965 1.00 27.23 ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.902 21.348  19.957 1.00 27.77 ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.728 20.330  20.256 1.00 29.46 ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.728 16.558  20.040 1.00 13.94 ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.530 15.749  19.127 1.00 14.30 ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.756 15.456  17.826 1.00 12.81 ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.342 15.482  16.743 1.00 13.50 ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 31.970 14.417  19.749 1.00 16.18 ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 32.932 13.691  18.839 1.00 23.19 ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.082 14.147  18.646 1.00 26.30 ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.466 12.600  18.201 1.00 24.69 ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.419 15.225  17.924 1.00 11.86 ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.625 15.053  16.709 1.00 11.46 ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.684 16.300  15.800 1.00 10.98 ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.918 16.189  14.593 1.00 11.72 ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.154 14.771  17.037 1.00 12.05 ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.888 13.415  17.633 1.00 13.60 ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.544 12.422  17.197 1.00 13.59 ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.069 13.344  18.568 1.00 12.97 ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.491 17.482  16.381 1.00 10.98 ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.531 18.739  15.597 1.00 11.40 ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 29.939 19.000  15.029 1.00 11.70 ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.024 19.555  13.927 1.00 12.61 ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.072 19.927  16.484 1.00 12.20 ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.570 19.999  16.618 1.00 11.75 ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.826 19.709  17.722 1.00 14.19 ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.637 20.447  15.612 1.00 12.49 ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.486 19.947  17.470 1.00 13.12 ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.342 20.354  16.159 1.00 13.17 ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.783 20.898  14.285 1.00 14.28 ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.194 20.749  15.434 1.00 14.71 ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.655 21.178  13.550 1.00 14.69 ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.404 21.189  14.135 1.00 15.28 ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 30.998 18.592  15.745 1.00 11.86 ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.363 18.819  15.262 1.00 12.09 ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.768 17.809  14.191 1.00 12.86 ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.807 17.964  13.561 1.00 14.51 ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.331 18.763  16.454 1.00 14.54 ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 31.968 16.731  13.994 1.00 12.31 ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.265 15.680  12.977 1.00 12.79 ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 30.999 15.492  12.111 1.00 12.01 ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.607 14.366  11.772 1.00 12.77 ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.678 14.345  13.653 1.00 13.91 ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.014 14.539  14.321 1.00 15.13 ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.060 14.474  13.659 1.00 18.26 ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.013 14.820  15.627 1.00 16.39 ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.354 16.583  11.761 1.00 12.13 ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.051 16.545  11.119 1.00 11.39 ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.100 16.111  9.676  1.00 12.07 ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 29.945 16.569  8.894  1.00 13.91 ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.471 17.974  11.178 1.00 12.07 ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.069 18.127  10.579 1.00 12.31 ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.032 17.355  11.406 1.00 13.07 ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.655 19.600  10.517 1.00 14.83 ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.181 15.217  9.281  1.00 11.44 ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.005 14.813  7.885  1.00 11.68 ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.756 15.508  7.312  1.00 12.00 ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.795 16.047  6.194  1.00 13.81 ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.889 13.282  7.792  1.00 11.56 ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.528 12.862  6.342  1.00 14.21 ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.189 12.615  8.276  1.00 13.30 ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.616 15.464  8.040  1.00 11.82 ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.357 16.016  7.526  1.00 11.80 ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.410 16.230  8.674  1.00 12.19 ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.432 15.451  9.646  1.00 11.94 ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.744 14.992  6.513  1.00 12.68 ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.331 15.266  6.057  1.00 13.97 ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.915 16.139  5.076  1.00 16.34 ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.145 14.670  6.585  1.00 13.52 ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.540 16.089  4.955  1.00 17.67 ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.046 15.167  5.846  1.00 15.54 ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.906 13.743  7.598  1.00 14.21 ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.724 14.715  6.075  1.00 16.74 ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.619 13.267  7.782  1.00 15.17 ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.540 13.797  7.078  1.00 16.51 ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.586 17.274  8.621  1.00 12.48 ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.566 17.470  9.642  1.00 12.79 ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.334 18.106  9.024  1.00 13.93 ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.458 18.911  8.065  1.00 14.67 ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.084 18.316  10.792 1.00 14.92 ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.675 19.674  10.400 1.00 15.74 ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.710 20.850  10.224 1.00 16.55 ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.037 21.811  9.472  1.00 17.13 ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.617 20.832  10.838 1.00 15.27 ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.156 17.820  9.592  1.00 13.18 ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.909 18.388  9.084  1.00 12.76 ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 16.949 18.567  10.245 1.00 12.79 ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.419 17.575  10.805 1.00 13.02 ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.315 17.450  7.997  1.00 14.64 ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.054 17.945  7.331  1.00 17.95 ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.216 18.518  8.023  1.00 21.40 ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.876 17.695  6.128  1.00 22.31 ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.723 19.835  10.637 1.00 13.43 ? 36  SER   A N   1 
ATOM   245  C  CA  . SER   A 1 30  ? 15.875 20.142  11.771 1.00 14.69 ? 36  SER   A CA  1 
ATOM   246  C  C   . SER   A 1 30  ? 14.405 19.729  11.507 1.00 15.65 ? 36  SER   A C   1 
ATOM   247  O  O   . SER   A 1 30  ? 13.750 19.215  12.443 1.00 15.84 ? 36  SER   A O   1 
ATOM   248  C  CB  . SER   A 1 30  ? 16.021 21.632  12.110 1.00 17.48 ? 36  SER   A CB  1 
ATOM   249  O  OG  . SER   A 1 30  ? 15.086 22.052  13.085 1.00 21.81 ? 36  SER   A OG  1 
ATOM   250  N  N   . SER   A 1 31  ? 13.932 19.825  10.258 1.00 15.20 ? 37  SER   A N   1 
ATOM   251  C  CA  . SER   A 1 31  ? 12.557 19.414  9.951  1.00 15.47 ? 37  SER   A CA  1 
ATOM   252  C  C   . SER   A 1 31  ? 12.301 17.939  10.146 1.00 14.59 ? 37  SER   A C   1 
ATOM   253  O  O   . SER   A 1 31  ? 11.169 17.544  10.389 1.00 15.92 ? 37  SER   A O   1 
ATOM   254  C  CB  . SER   A 1 31  ? 12.149 19.810  8.539  1.00 18.36 ? 37  SER   A CB  1 
ATOM   255  O  OG  . SER   A 1 31  ? 12.685 18.981  7.530  1.00 24.43 ? 37  SER   A OG  1 
ATOM   256  N  N   . ARG   A 1 32  ? 13.358 17.109  10.127 1.00 12.78 ? 38  ARG   A N   1 
ATOM   257  C  CA  . ARG   A 1 32  ? 13.266 15.658  10.340 1.00 13.12 ? 38  ARG   A CA  1 
ATOM   258  C  C   . ARG   A 1 32  ? 13.730 15.219  11.736 1.00 12.45 ? 38  ARG   A C   1 
ATOM   259  O  O   . ARG   A 1 32  ? 13.653 14.026  12.055 1.00 11.80 ? 38  ARG   A O   1 
ATOM   260  C  CB  . ARG   A 1 32  ? 14.136 14.920  9.286  1.00 13.49 ? 38  ARG   A CB  1 
ATOM   261  C  CG  . ARG   A 1 32  ? 13.611 15.102  7.860  1.00 15.50 ? 38  ARG   A CG  1 
ATOM   262  C  CD  . ARG   A 1 32  ? 14.485 14.429  6.822  1.00 14.69 ? 38  ARG   A CD  1 
ATOM   263  N  NE  . ARG   A 1 32  ? 14.386 12.961  6.964  1.00 12.63 ? 38  ARG   A NE  1 
ATOM   264  C  CZ  . ARG   A 1 32  ? 14.572 12.114  5.958  1.00 13.21 ? 38  ARG   A CZ  1 
ATOM   265  N  NH1 . ARG   A 1 32  ? 14.855 12.570  4.730  1.00 15.41 ? 38  ARG   A NH1 1 
ATOM   266  N  NH2 . ARG   A 1 32  ? 14.429 10.800  6.145  1.00 13.96 ? 38  ARG   A NH2 1 
ATOM   267  N  N   . ASP   A 1 33  ? 14.300 16.130  12.539 1.00 11.80 ? 39  ASP   A N   1 
ATOM   268  C  CA  . ASP   A 1 33  ? 14.929 15.803  13.813 1.00 11.80 ? 39  ASP   A CA  1 
ATOM   269  C  C   . ASP   A 1 33  ? 16.080 14.793  13.674 1.00 11.43 ? 39  ASP   A C   1 
ATOM   270  O  O   . ASP   A 1 33  ? 16.282 13.944  14.550 1.00 11.58 ? 39  ASP   A O   1 
ATOM   271  C  CB  . ASP   A 1 33  ? 13.922 15.330  14.888 1.00 12.70 ? 39  ASP   A CB  1 
ATOM   272  C  CG  . ASP   A 1 33  ? 14.541 15.093  16.265 1.00 12.24 ? 39  ASP   A CG  1 
ATOM   273  O  OD1 . ASP   A 1 33  ? 15.383 15.928  16.724 1.00 13.04 ? 39  ASP   A OD1 1 
ATOM   274  O  OD2 . ASP   A 1 33  ? 14.148 14.091  16.952 1.00 12.93 ? 39  ASP   A OD2 1 
ATOM   275  N  N   . LEU   A 1 34  ? 16.865 14.916  12.583 1.00 10.79 ? 40  LEU   A N   1 
ATOM   276  C  CA  . LEU   A 1 34  ? 17.962 13.955  12.385 1.00 9.89  ? 40  LEU   A CA  1 
ATOM   277  C  C   . LEU   A 1 34  ? 19.316 14.664  12.246 1.00 10.31 ? 40  LEU   A C   1 
ATOM   278  O  O   . LEU   A 1 34  ? 19.410 15.773  11.656 1.00 11.40 ? 40  LEU   A O   1 
ATOM   279  C  CB  . LEU   A 1 34  ? 17.732 13.143  11.110 1.00 10.94 ? 40  LEU   A CB  1 
ATOM   280  C  CG  . LEU   A 1 34  ? 16.665 11.999  11.157 1.00 12.44 ? 40  LEU   A CG  1 
ATOM   281  C  CD1 . LEU   A 1 34  ? 16.588 11.304  9.800  1.00 13.52 ? 40  LEU   A CD1 1 
ATOM   282  C  CD2 . LEU   A 1 34  ? 16.937 10.989  12.301 1.00 12.29 ? 40  LEU   A CD2 1 
ATOM   283  N  N   . LEU   A 1 35  ? 20.359 14.000  12.703 1.00 9.97  ? 41  LEU   A N   1 
ATOM   284  C  CA  . LEU   A 1 35  ? 21.746 14.452  12.488 1.00 9.67  ? 41  LEU   A CA  1 
ATOM   285  C  C   . LEU   A 1 35  ? 22.589 13.217  12.337 1.00 10.06 ? 41  LEU   A C   1 
ATOM   286  O  O   . LEU   A 1 35  ? 22.406 12.195  13.043 1.00 10.68 ? 41  LEU   A O   1 
ATOM   287  C  CB  . LEU   A 1 35  ? 22.229 15.292  13.705 1.00 10.58 ? 41  LEU   A CB  1 
ATOM   288  C  CG  . LEU   A 1 35  ? 23.659 15.866  13.618 1.00 10.33 ? 41  LEU   A CG  1 
ATOM   289  C  CD1 . LEU   A 1 35  ? 23.754 17.233  14.300 1.00 12.52 ? 41  LEU   A CD1 1 
ATOM   290  C  CD2 . LEU   A 1 35  ? 24.687 14.926  14.230 1.00 11.19 ? 41  LEU   A CD2 1 
ATOM   291  N  N   . VAL   A 1 36  ? 23.565 13.300  11.417 1.00 10.26 ? 42  VAL   A N   1 
ATOM   292  C  CA  . VAL   A 1 36  ? 24.511 12.197  11.167 1.00 9.54  ? 42  VAL   A CA  1 
ATOM   293  C  C   . VAL   A 1 36  ? 25.912 12.718  11.327 1.00 9.80  ? 42  VAL   A C   1 
ATOM   294  O  O   . VAL   A 1 36  ? 26.243 13.781  10.737 1.00 10.84 ? 42  VAL   A O   1 
ATOM   295  C  CB  . VAL   A 1 36  ? 24.287 11.608  9.742  1.00 9.99  ? 42  VAL   A CB  1 
ATOM   296  C  CG1 . VAL   A 1 36  ? 25.313 10.501  9.467  1.00 11.41 ? 42  VAL   A CG1 1 
ATOM   297  C  CG2 . VAL   A 1 36  ? 22.836 11.072  9.611  1.00 11.54 ? 42  VAL   A CG2 1 
ATOM   298  N  N   . SER   A 1 37  ? 26.731 12.039  12.114 1.00 9.78  ? 43  SER   A N   1 
ATOM   299  C  CA  . SER   A 1 37  ? 28.145 12.369  12.279 1.00 9.93  ? 43  SER   A CA  1 
ATOM   300  C  C   . SER   A 1 37  ? 29.014 11.203  11.833 1.00 11.22 ? 43  SER   A C   1 
ATOM   301  O  O   . SER   A 1 37  ? 28.534 10.059  11.625 1.00 11.31 ? 43  SER   A O   1 
ATOM   302  C  CB  . SER   A 1 37  ? 28.438 12.729  13.730 1.00 11.42 ? 43  SER   A CB  1 
ATOM   303  O  OG  . SER   A 1 37  ? 28.105 11.671  14.616 1.00 12.15 ? 43  SER   A OG  1 
ATOM   304  N  N   . SER   A 1 38  ? 30.312 11.467  11.639 1.00 11.60 ? 44  SER   A N   1 
ATOM   305  C  CA  . SER   A 1 38  ? 31.236 10.418  11.200 1.00 12.80 ? 44  SER   A CA  1 
ATOM   306  C  C   . SER   A 1 38  ? 31.863 9.721   12.400 1.00 14.46 ? 44  SER   A C   1 
ATOM   307  O  O   . SER   A 1 38  ? 32.053 10.346  13.469 1.00 16.47 ? 44  SER   A O   1 
ATOM   308  C  CB  . SER   A 1 38  ? 32.320 11.013  10.300 1.00 15.25 ? 44  SER   A CB  1 
ATOM   309  O  OG  . SER   A 1 38  ? 33.024 11.988  11.052 1.00 18.43 ? 44  SER   A OG  1 
ATOM   310  N  N   . THR   A 1 39  ? 32.217 8.422   12.230 1.00 14.62 ? 45  THR   A N   1 
ATOM   311  C  CA  . THR   A 1 39  ? 32.805 7.625   13.310 1.00 16.33 ? 45  THR   A CA  1 
ATOM   312  C  C   . THR   A 1 39  ? 34.141 7.029   12.872 1.00 18.05 ? 45  THR   A C   1 
ATOM   313  O  O   . THR   A 1 39  ? 34.368 6.783   11.680 1.00 17.08 ? 45  THR   A O   1 
ATOM   314  C  CB  . THR   A 1 39  ? 31.877 6.434   13.684 1.00 16.87 ? 45  THR   A CB  1 
ATOM   315  O  OG1 . THR   A 1 39  ? 31.733 5.542   12.578 1.00 17.63 ? 45  THR   A OG1 1 
ATOM   316  C  CG2 . THR   A 1 39  ? 30.484 6.882   14.093 1.00 18.29 ? 45  THR   A CG2 1 
ATOM   317  N  N   . THR   A 1 40  ? 35.009 6.763   13.852 1.00 19.38 ? 46  THR   A N   1 
ATOM   318  C  CA  . THR   A 1 40  ? 36.281 6.113   13.566 1.00 20.94 ? 46  THR   A CA  1 
ATOM   319  C  C   . THR   A 1 40  ? 36.068 4.616   13.353 1.00 20.70 ? 46  THR   A C   1 
ATOM   320  O  O   . THR   A 1 40  ? 36.624 4.052   12.400 1.00 23.44 ? 46  THR   A O   1 
ATOM   321  C  CB  . THR   A 1 40  ? 37.315 6.456   14.663 1.00 25.42 ? 46  THR   A CB  1 
ATOM   322  O  OG1 . THR   A 1 40  ? 36.820 5.985   15.898 1.00 30.21 ? 46  THR   A OG1 1 
ATOM   323  C  CG2 . THR   A 1 40  ? 37.527 7.945   14.785 1.00 25.94 ? 46  THR   A CG2 1 
ATOM   324  N  N   . ALA   A 1 41  ? 35.254 3.991   14.210 1.00 20.51 ? 47  ALA   A N   1 
ATOM   325  C  CA  . ALA   A 1 41  ? 34.981 2.552   14.114 1.00 21.25 ? 47  ALA   A CA  1 
ATOM   326  C  C   . ALA   A 1 41  ? 33.765 2.255   13.206 1.00 20.11 ? 47  ALA   A C   1 
ATOM   327  O  O   . ALA   A 1 41  ? 32.813 3.036   13.205 1.00 19.17 ? 47  ALA   A O   1 
ATOM   328  C  CB  . ALA   A 1 41  ? 34.680 2.009   15.506 1.00 24.24 ? 47  ALA   A CB  1 
ATOM   329  N  N   . GLN   A 1 42  ? 33.740 1.111   12.531 1.00 18.35 ? 48  GLN   A N   1 
ATOM   330  C  CA  . GLN   A 1 42  ? 32.610 0.683   11.691 1.00 18.97 ? 48  GLN   A CA  1 
ATOM   331  C  C   . GLN   A 1 42  ? 31.516 0.097   12.554 1.00 19.03 ? 48  GLN   A C   1 
ATOM   332  O  O   . GLN   A 1 42  ? 31.794 -0.646  13.497 1.00 20.64 ? 48  GLN   A O   1 
ATOM   333  C  CB  . GLN   A 1 42  ? 33.049 -0.347  10.641 1.00 21.46 ? 48  GLN   A CB  1 
ATOM   334  C  CG  . GLN   A 1 42  ? 33.879 0.278   9.503  1.00 27.27 ? 48  GLN   A CG  1 
ATOM   335  C  CD  . GLN   A 1 42  ? 34.265 -0.760  8.494  1.00 32.95 ? 48  GLN   A CD  1 
ATOM   336  O  OE1 . GLN   A 1 42  ? 35.127 -1.611  8.748  1.00 32.07 ? 48  GLN   A OE1 1 
ATOM   337  N  NE2 . GLN   A 1 42  ? 33.595 -0.729  7.347  1.00 35.06 ? 48  GLN   A NE2 1 
ATOM   338  N  N   . GLY   A 1 43  ? 30.270 0.434   12.225 1.00 16.01 ? 49  GLY   A N   1 
ATOM   339  C  CA  . GLY   A 1 43  ? 29.105 -0.073  12.942 1.00 15.33 ? 49  GLY   A CA  1 
ATOM   340  C  C   . GLY   A 1 43  ? 28.520 -1.338  12.343 1.00 14.33 ? 49  GLY   A C   1 
ATOM   341  O  O   . GLY   A 1 43  ? 28.820 -1.686  11.192 1.00 16.13 ? 49  GLY   A O   1 
ATOM   342  N  N   . CYS   A 1 44  ? 27.560 -1.928  13.097 1.00 14.09 ? 50  CYS   A N   1 
ATOM   343  C  CA  . CYS   A 1 44  ? 26.964 -3.232  12.741 1.00 14.47 ? 50  CYS   A CA  1 
ATOM   344  C  C   . CYS   A 1 44  ? 25.512 -3.169  12.300 1.00 14.35 ? 50  CYS   A C   1 
ATOM   345  O  O   . CYS   A 1 44  ? 24.972 -4.218  11.895 1.00 15.32 ? 50  CYS   A O   1 
ATOM   346  C  CB  . CYS   A 1 44  ? 27.139 -4.254  13.862 1.00 15.80 ? 50  CYS   A CB  1 
ATOM   347  S  SG  . CYS   A 1 44  ? 28.854 -4.657  14.201 1.00 19.57 ? 50  CYS   A SG  1 
ATOM   348  N  N   . ASP   A 1 45  ? 24.845 -2.024  12.428 1.00 13.01 ? 51  ASP   A N   1 
ATOM   349  C  CA  . ASP   A 1 45  ? 23.466 -1.920  11.994 1.00 12.21 ? 51  ASP   A CA  1 
ATOM   350  C  C   . ASP   A 1 45  ? 23.403 -1.867  10.476 1.00 13.55 ? 51  ASP   A C   1 
ATOM   351  O  O   . ASP   A 1 45  ? 24.283 -1.280  9.823  1.00 15.46 ? 51  ASP   A O   1 
ATOM   352  C  CB  . ASP   A 1 45  ? 22.844 -0.657  12.598 1.00 11.54 ? 51  ASP   A CB  1 
ATOM   353  C  CG  . ASP   A 1 45  ? 22.727 -0.705  14.109 1.00 12.58 ? 51  ASP   A CG  1 
ATOM   354  O  OD1 . ASP   A 1 45  ? 22.366 -1.804  14.645 1.00 13.78 ? 51  ASP   A OD1 1 
ATOM   355  O  OD2 . ASP   A 1 45  ? 22.926 0.367   14.774 1.00 13.37 ? 51  ASP   A OD2 1 
ATOM   356  N  N   . THR   A 1 46  ? 22.371 -2.417  9.913  1.00 14.18 ? 52  THR   A N   1 
ATOM   357  C  CA  . THR   A 1 46  ? 22.081 -2.306  8.462  1.00 15.30 ? 52  THR   A CA  1 
ATOM   358  C  C   . THR   A 1 46  ? 20.744 -1.586  8.293  1.00 14.18 ? 52  THR   A C   1 
ATOM   359  O  O   . THR   A 1 46  ? 19.840 -1.743  9.127  1.00 15.29 ? 52  THR   A O   1 
ATOM   360  C  CB  . THR   A 1 46  ? 22.060 -3.652  7.805  1.00 19.97 ? 52  THR   A CB  1 
ATOM   361  O  OG1 . THR   A 1 46  ? 21.036 -4.387  8.418  1.00 25.14 ? 52  THR   A OG1 1 
ATOM   362  C  CG2 . THR   A 1 46  ? 23.404 -4.380  7.976  1.00 21.13 ? 52  THR   A CG2 1 
ATOM   363  N  N   . ILE   A 1 47  ? 20.626 -0.757  7.267  1.00 14.12 ? 53  ILE   A N   1 
ATOM   364  C  CA  . ILE   A 1 47  ? 19.407 -0.004  7.037  1.00 12.77 ? 53  ILE   A CA  1 
ATOM   365  C  C   . ILE   A 1 47  ? 18.434 -0.795  6.154  1.00 13.67 ? 53  ILE   A C   1 
ATOM   366  O  O   . ILE   A 1 47  ? 18.815 -1.328  5.084  1.00 14.41 ? 53  ILE   A O   1 
ATOM   367  C  CB  . ILE   A 1 47  ? 19.722 1.353   6.402  1.00 13.29 ? 53  ILE   A CB  1 
ATOM   368  C  CG1 . ILE   A 1 47  ? 20.813 2.149   7.174  1.00 13.83 ? 53  ILE   A CG1 1 
ATOM   369  C  CG2 . ILE   A 1 47  ? 18.437 2.231   6.253  1.00 13.15 ? 53  ILE   A CG2 1 
ATOM   370  C  CD1 . ILE   A 1 47  ? 20.451 2.429   8.669  1.00 14.08 ? 53  ILE   A CD1 1 
ATOM   371  N  N   . ALA   A 1 48  ? 17.163 -0.824  6.524  1.00 11.80 ? 54  ALA   A N   1 
ATOM   372  C  CA  . ALA   A 1 48  ? 16.101 -1.438  5.734  1.00 12.17 ? 54  ALA   A CA  1 
ATOM   373  C  C   . ALA   A 1 48  ? 15.842 -0.579  4.479  1.00 13.10 ? 54  ALA   A C   1 
ATOM   374  O  O   . ALA   A 1 48  ? 15.840 0.686   4.513  1.00 13.19 ? 54  ALA   A O   1 
ATOM   375  C  CB  . ALA   A 1 48  ? 14.815 -1.494  6.544  1.00 12.54 ? 54  ALA   A CB  1 
ATOM   376  N  N   . ARG   A 1 49  ? 15.614 -1.283  3.335  1.00 14.69 ? 55  ARG   A N   1 
ATOM   377  C  CA  . ARG   A 1 49  ? 15.313 -0.623  2.063  1.00 15.49 ? 55  ARG   A CA  1 
ATOM   378  C  C   . ARG   A 1 49  ? 14.042 -1.319  1.586  1.00 18.08 ? 55  ARG   A C   1 
ATOM   379  O  O   . ARG   A 1 49  ? 14.094 -2.280  0.811  1.00 20.13 ? 55  ARG   A O   1 
ATOM   380  C  CB  . ARG   A 1 49  ? 16.509 -0.734  1.066  1.00 16.04 ? 55  ARG   A CB  1 
ATOM   381  C  CG  . ARG   A 1 49  ? 17.808 -0.123  1.611  1.00 16.47 ? 55  ARG   A CG  1 
ATOM   382  C  CD  . ARG   A 1 49  ? 17.784 1.402   1.848  1.00 15.12 ? 55  ARG   A CD  1 
ATOM   383  N  NE  . ARG   A 1 49  ? 19.105 1.875   2.327  1.00 14.91 ? 55  ARG   A NE  1 
ATOM   384  C  CZ  . ARG   A 1 49  ? 19.299 3.026   2.961  1.00 14.34 ? 55  ARG   A CZ  1 
ATOM   385  N  NH1 . ARG   A 1 49  ? 18.295 3.876   3.135  1.00 14.86 ? 55  ARG   A NH1 1 
ATOM   386  N  NH2 . ARG   A 1 49  ? 20.502 3.334   3.451  1.00 16.39 ? 55  ARG   A NH2 1 
ATOM   387  N  N   . CYS   A 1 50  ? 12.903 -0.817  2.072  1.00 17.10 ? 56  CYS   A N   1 
ATOM   388  C  CA  . CYS   A 1 50  ? 11.593 -1.469  1.934  1.00 17.49 ? 56  CYS   A CA  1 
ATOM   389  C  C   . CYS   A 1 50  ? 10.454 -0.478  2.207  1.00 18.61 ? 56  CYS   A C   1 
ATOM   390  O  O   . CYS   A 1 50  ? 10.600 0.669   2.563  1.00 21.79 ? 56  CYS   A O   1 
ATOM   391  C  CB  . CYS   A 1 50  ? 11.535 -2.613  2.939  1.00 16.38 ? 56  CYS   A CB  1 
ATOM   392  S  SG  . CYS   A 1 50  ? 11.493 -2.050  4.650  1.00 16.75 ? 56  CYS   A SG  1 
ATOM   393  N  N   . ASP   A 1 51  ? 9.180  -1.054  2.100  1.00 22.25 ? 57  ASP   A N   1 
ATOM   394  C  CA  A ASP   A 1 51  ? 7.967  -0.298  2.384  0.50 24.29 ? 57  ASP   A CA  1 
ATOM   395  C  CA  B ASP   A 1 51  ? 7.891  -0.405  2.294  0.50 24.39 ? 57  ASP   A CA  1 
ATOM   396  C  C   . ASP   A 1 51  ? 7.188  -0.933  3.563  1.00 23.87 ? 57  ASP   A C   1 
ATOM   397  O  O   . ASP   A 1 51  ? 5.964  -0.762  3.668  1.00 24.52 ? 57  ASP   A O   1 
ATOM   398  C  CB  A ASP   A 1 51  ? 7.066  -0.199  1.139  0.50 28.38 ? 57  ASP   A CB  1 
ATOM   399  C  CB  B ASP   A 1 51  ? 6.978  -0.761  1.089  0.50 28.49 ? 57  ASP   A CB  1 
ATOM   400  C  CG  A ASP   A 1 51  ? 6.587  -1.543  0.617  0.50 33.20 ? 57  ASP   A CG  1 
ATOM   401  C  CG  B ASP   A 1 51  ? 5.911  0.268   0.759  0.50 34.90 ? 57  ASP   A CG  1 
ATOM   402  O  OD1 A ASP   A 1 51  ? 7.230  -2.571  0.932  0.50 32.67 ? 57  ASP   A OD1 1 
ATOM   403  O  OD1 B ASP   A 1 51  ? 5.181  0.071   -0.240 0.50 35.75 ? 57  ASP   A OD1 1 
ATOM   404  O  OD2 A ASP   A 1 51  ? 5.588  -1.565  -0.151 0.50 37.13 ? 57  ASP   A OD2 1 
ATOM   405  O  OD2 B ASP   A 1 51  ? 5.805  1.269   1.494  0.50 38.84 ? 57  ASP   A OD2 1 
ATOM   406  N  N   . CYS   A 1 52  ? 7.884  -1.657  4.477  1.00 19.70 ? 58  CYS   A N   1 
ATOM   407  C  CA  . CYS   A 1 52  ? 7.193  -2.240  5.656  1.00 17.04 ? 58  CYS   A CA  1 
ATOM   408  C  C   . CYS   A 1 52  ? 6.475  -1.192  6.457  1.00 17.39 ? 58  CYS   A C   1 
ATOM   409  O  O   . CYS   A 1 52  ? 6.940  -0.035  6.630  1.00 18.11 ? 58  CYS   A O   1 
ATOM   410  C  CB  . CYS   A 1 52  ? 8.173  -2.976  6.564  1.00 19.04 ? 58  CYS   A CB  1 
ATOM   411  S  SG  . CYS   A 1 52  ? 8.899  -4.507  5.889  1.00 19.40 ? 58  CYS   A SG  1 
ATOM   412  N  N   . GLN   A 1 53  ? 5.335  -1.606  6.993  1.00 14.86 ? 59  GLN   A N   1 
ATOM   413  C  CA  A GLN   A 1 53  ? 4.490  -0.816  7.928  0.50 14.71 ? 59  GLN   A CA  1 
ATOM   414  C  CA  B GLN   A 1 53  ? 4.604  -0.765  7.871  0.50 15.48 ? 59  GLN   A CA  1 
ATOM   415  C  C   . GLN   A 1 53  ? 4.266  -1.553  9.217  1.00 13.82 ? 59  GLN   A C   1 
ATOM   416  O  O   . GLN   A 1 53  ? 3.413  -1.166  9.993  1.00 14.18 ? 59  GLN   A O   1 
ATOM   417  C  CB  A GLN   A 1 53  ? 3.108  -0.303  7.405  0.50 14.29 ? 59  GLN   A CB  1 
ATOM   418  C  CB  B GLN   A 1 53  ? 3.466  -0.121  7.067  0.50 17.48 ? 59  GLN   A CB  1 
ATOM   419  C  CG  A GLN   A 1 53  ? 3.171  0.914   6.429  0.50 14.26 ? 59  GLN   A CG  1 
ATOM   420  C  CG  B GLN   A 1 53  ? 4.026  0.710   5.832  0.50 16.89 ? 59  GLN   A CG  1 
ATOM   421  C  CD  A GLN   A 1 53  ? 1.797  1.417   6.023  0.50 18.11 ? 59  GLN   A CD  1 
ATOM   422  C  CD  B GLN   A 1 53  ? 5.034  1.815   6.234  0.50 16.21 ? 59  GLN   A CD  1 
ATOM   423  O  OE1 A GLN   A 1 53  ? 1.347  1.245   4.871  0.50 19.66 ? 59  GLN   A OE1 1 
ATOM   424  O  OE1 B GLN   A 1 53  ? 6.032  2.207   5.513  0.50 16.27 ? 59  GLN   A OE1 1 
ATOM   425  N  NE2 A GLN   A 1 53  ? 1.101  2.057   6.937  0.50 14.62 ? 59  GLN   A NE2 1 
ATOM   426  N  NE2 B GLN   A 1 53  ? 4.799  2.364   7.417  0.50 17.41 ? 59  GLN   A NE2 1 
ATOM   427  N  N   . THR   A 1 54  ? 5.000  -2.672  9.458  1.00 12.30 ? 60  THR   A N   1 
ATOM   428  C  CA  . THR   A 1 54  ? 5.007  -3.394  10.710 1.00 12.50 ? 60  THR   A CA  1 
ATOM   429  C  C   . THR   A 1 54  ? 6.477  -3.633  11.115 1.00 11.49 ? 60  THR   A C   1 
ATOM   430  O  O   . THR   A 1 54  ? 7.343  -3.824  10.247 1.00 13.36 ? 60  THR   A O   1 
ATOM   431  C  CB  . THR   A 1 54  ? 4.246  -4.670  10.687 1.00 14.85 ? 60  THR   A CB  1 
ATOM   432  O  OG1 . THR   A 1 54  ? 4.851  -5.594  9.846  1.00 21.81 ? 60  THR   A OG1 1 
ATOM   433  C  CG2 . THR   A 1 54  ? 2.803  -4.503  10.295 1.00 15.73 ? 60  THR   A CG2 1 
ATOM   434  N  N   . GLY   A 1 55  ? 6.729  -3.563  12.406 1.00 10.87 ? 61  GLY   A N   1 
ATOM   435  C  CA  . GLY   A 1 55  ? 8.092  -3.758  12.893 1.00 10.65 ? 61  GLY   A CA  1 
ATOM   436  C  C   . GLY   A 1 55  ? 8.085  -3.804  14.401 1.00 9.96  ? 61  GLY   A C   1 
ATOM   437  O  O   . GLY   A 1 55  ? 7.061  -4.049  15.030 1.00 10.45 ? 61  GLY   A O   1 
ATOM   438  N  N   . VAL   A 1 56  ? 9.281  -3.598  14.995 1.00 9.14  ? 62  VAL   A N   1 
ATOM   439  C  CA  . VAL   A 1 56  ? 9.458  -3.660  16.440 1.00 8.64  ? 62  VAL   A CA  1 
ATOM   440  C  C   . VAL   A 1 56  ? 10.302 -2.463  16.877 1.00 8.65  ? 62  VAL   A C   1 
ATOM   441  O  O   . VAL   A 1 56  ? 11.275 -2.168  16.192 1.00 9.95  ? 62  VAL   A O   1 
ATOM   442  C  CB  . VAL   A 1 56  ? 10.169 -5.000  16.797 1.00 10.83 ? 62  VAL   A CB  1 
ATOM   443  C  CG1 . VAL   A 1 56  ? 10.517 -5.078  18.265 1.00 12.84 ? 62  VAL   A CG1 1 
ATOM   444  C  CG2 . VAL   A 1 56  ? 9.268  -6.207  16.429 1.00 11.06 ? 62  VAL   A CG2 1 
ATOM   445  N  N   . TYR   A 1 57  ? 9.945  -1.802  17.968 1.00 8.60  ? 63  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 57  ? 10.806 -0.706  18.459 1.00 8.46  ? 63  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 57  ? 11.232 -0.914  19.897 1.00 8.62  ? 63  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 57  ? 10.540 -1.581  20.685 1.00 9.83  ? 63  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 57  ? 10.100 0.699   18.322 1.00 9.07  ? 63  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 57  ? 9.122  1.077   19.413 1.00 9.17  ? 63  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 57  ? 7.836  0.555   19.425 1.00 10.28 ? 63  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 57  ? 9.468  1.984   20.419 1.00 9.57  ? 63  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 57  ? 6.931  0.891   20.424 1.00 10.85 ? 63  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 57  ? 8.546  2.352   21.404 1.00 10.71 ? 63  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 57  ? 7.290  1.801   21.388 1.00 11.72 ? 63  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 57  ? 6.327  2.099   22.351 1.00 13.99 ? 63  TYR   A OH  1 
ATOM   457  N  N   . TYR   A 1 58  ? 12.362 -0.310  20.276 1.00 8.62  ? 64  TYR   A N   1 
ATOM   458  C  CA  . TYR   A 1 58  ? 12.839 -0.353  21.656 1.00 9.01  ? 64  TYR   A CA  1 
ATOM   459  C  C   . TYR   A 1 58  ? 12.371 0.857   22.447 1.00 9.03  ? 64  TYR   A C   1 
ATOM   460  O  O   . TYR   A 1 58  ? 12.609 2.012   22.059 1.00 9.37  ? 64  TYR   A O   1 
ATOM   461  C  CB  . TYR   A 1 58  ? 14.384 -0.416  21.697 1.00 10.31 ? 64  TYR   A CB  1 
ATOM   462  C  CG  . TYR   A 1 58  ? 14.861 -0.555  23.121 1.00 10.40 ? 64  TYR   A CG  1 
ATOM   463  C  CD1 . TYR   A 1 58  ? 14.552 -1.677  23.860 1.00 10.14 ? 64  TYR   A CD1 1 
ATOM   464  C  CD2 . TYR   A 1 58  ? 15.610 0.458   23.739 1.00 10.88 ? 64  TYR   A CD2 1 
ATOM   465  C  CE1 . TYR   A 1 58  ? 14.939 -1.786  25.198 1.00 12.57 ? 64  TYR   A CE1 1 
ATOM   466  C  CE2 . TYR   A 1 58  ? 16.000 0.356   25.075 1.00 11.75 ? 64  TYR   A CE2 1 
ATOM   467  C  CZ  . TYR   A 1 58  ? 15.694 -0.790  25.778 1.00 12.34 ? 64  TYR   A CZ  1 
ATOM   468  O  OH  . TYR   A 1 58  ? 16.030 -0.960  27.140 1.00 14.94 ? 64  TYR   A OH  1 
ATOM   469  N  N   . CYS   A 1 59  ? 11.762 0.561   23.584 1.00 8.94  ? 65  CYS   A N   1 
ATOM   470  C  CA  . CYS   A 1 59  ? 11.218 1.565   24.524 1.00 9.74  ? 65  CYS   A CA  1 
ATOM   471  C  C   . CYS   A 1 59  ? 12.042 1.541   25.822 1.00 10.00 ? 65  CYS   A C   1 
ATOM   472  O  O   . CYS   A 1 59  ? 11.843 0.634   26.680 1.00 10.69 ? 65  CYS   A O   1 
ATOM   473  C  CB  . CYS   A 1 59  ? 9.767  1.236   24.811 1.00 9.70  ? 65  CYS   A CB  1 
ATOM   474  S  SG  . CYS   A 1 59  ? 8.998  2.357   26.023 1.00 11.19 ? 65  CYS   A SG  1 
ATOM   475  N  N   . SER   A 1 60  ? 12.943 2.513   26.013 1.00 10.13 ? 66  SER   A N   1 
ATOM   476  C  CA  . SER   A 1 60  ? 13.839 2.505   27.203 1.00 11.32 ? 66  SER   A CA  1 
ATOM   477  C  C   . SER   A 1 60  ? 13.082 2.700   28.521 1.00 11.56 ? 66  SER   A C   1 
ATOM   478  O  O   . SER   A 1 60  ? 13.496 2.147   29.538 1.00 13.10 ? 66  SER   A O   1 
ATOM   479  C  CB  . SER   A 1 60  ? 14.963 3.537   27.056 1.00 13.10 ? 66  SER   A CB  1 
ATOM   480  O  OG  . SER   A 1 60  ? 14.512 4.866   27.147 1.00 15.07 ? 66  SER   A OG  1 
ATOM   481  N  N   . SER   A 1 61  ? 11.940 3.423   28.482 1.00 10.52 ? 67  SER   A N   1 
ATOM   482  C  CA  . SER   A 1 61  ? 11.147 3.635   29.695 1.00 10.83 ? 67  SER   A CA  1 
ATOM   483  C  C   . SER   A 1 61  ? 10.322 2.414   30.123 1.00 11.02 ? 67  SER   A C   1 
ATOM   484  O  O   . SER   A 1 61  ? 9.683  2.445   31.166 1.00 11.51 ? 67  SER   A O   1 
ATOM   485  C  CB  . SER   A 1 61  ? 10.240 4.848   29.530 1.00 11.73 ? 67  SER   A CB  1 
ATOM   486  O  OG  . SER   A 1 61  ? 9.251  4.644   28.556 1.00 12.40 ? 67  SER   A OG  1 
ATOM   487  N  N   . ARG   A 1 62  ? 10.418 1.305   29.361 1.00 10.94 ? 68  ARG   A N   1 
ATOM   488  C  CA  . ARG   A 1 62  ? 9.834  0.012   29.734 1.00 11.48 ? 68  ARG   A CA  1 
ATOM   489  C  C   . ARG   A 1 62  ? 10.893 -1.106  29.701 1.00 12.42 ? 68  ARG   A C   1 
ATOM   490  O  O   . ARG   A 1 62  ? 10.544 -2.270  29.962 1.00 13.24 ? 68  ARG   A O   1 
ATOM   491  C  CB  . ARG   A 1 62  ? 8.653  -0.330  28.790 1.00 11.56 ? 68  ARG   A CB  1 
ATOM   492  C  CG  . ARG   A 1 62  ? 7.492  0.640   28.932 1.00 12.62 ? 68  ARG   A CG  1 
ATOM   493  C  CD  . ARG   A 1 62  ? 6.726  0.310   30.204 1.00 12.85 ? 68  ARG   A CD  1 
ATOM   494  N  NE  . ARG   A 1 62  ? 5.570  1.204   30.381 1.00 14.56 ? 68  ARG   A NE  1 
ATOM   495  C  CZ  . ARG   A 1 62  ? 5.598  2.366   31.027 1.00 13.76 ? 68  ARG   A CZ  1 
ATOM   496  N  NH1 . ARG   A 1 62  ? 6.735  2.818   31.560 1.00 14.02 ? 68  ARG   A NH1 1 
ATOM   497  N  NH2 . ARG   A 1 62  ? 4.475  3.085   31.178 1.00 15.07 ? 68  ARG   A NH2 1 
ATOM   498  N  N   . ARG   A 1 63  ? 12.119 -0.840  29.225 1.00 13.50 ? 69  ARG   A N   1 
ATOM   499  C  CA  . ARG   A 1 63  ? 13.128 -1.902  28.965 1.00 14.91 ? 69  ARG   A CA  1 
ATOM   500  C  C   . ARG   A 1 63  ? 12.529 -3.010  28.102 1.00 16.45 ? 69  ARG   A C   1 
ATOM   501  O  O   . ARG   A 1 63  ? 12.719 -4.216  28.384 1.00 18.67 ? 69  ARG   A O   1 
ATOM   502  C  CB  . ARG   A 1 63  ? 13.678 -2.506  30.266 1.00 18.71 ? 69  ARG   A CB  1 
ATOM   503  C  CG  . ARG   A 1 63  ? 14.659 -1.643  30.848 1.00 19.45 ? 69  ARG   A CG  1 
ATOM   504  C  CD  . ARG   A 1 63  ? 15.482 -2.500  31.824 1.00 20.14 ? 69  ARG   A CD  1 
ATOM   505  N  NE  . ARG   A 1 63  ? 16.243 -1.564  32.612 1.00 20.70 ? 69  ARG   A NE  1 
ATOM   506  C  CZ  . ARG   A 1 63  ? 15.907 -1.147  33.824 1.00 17.14 ? 69  ARG   A CZ  1 
ATOM   507  N  NH1 . ARG   A 1 63  ? 14.840 -1.658  34.444 1.00 18.11 ? 69  ARG   A NH1 1 
ATOM   508  N  NH2 . ARG   A 1 63  ? 16.644 -0.235  34.440 1.00 19.23 ? 69  ARG   A NH2 1 
ATOM   509  N  N   . LYS   A 1 64  ? 11.799 -2.642  27.066 1.00 13.41 ? 70  LYS   A N   1 
ATOM   510  C  CA  . LYS   A 1 64  ? 11.100 -3.643  26.271 1.00 13.69 ? 70  LYS   A CA  1 
ATOM   511  C  C   . LYS   A 1 64  ? 11.065 -3.264  24.830 1.00 12.65 ? 70  LYS   A C   1 
ATOM   512  O  O   . LYS   A 1 64  ? 10.984 -2.072  24.483 1.00 12.33 ? 70  LYS   A O   1 
ATOM   513  C  CB  . LYS   A 1 64  ? 9.646  -3.770  26.790 1.00 16.35 ? 70  LYS   A CB  1 
ATOM   514  C  CG  . LYS   A 1 64  ? 9.502  -4.709  28.005 1.00 25.78 ? 70  LYS   A CG  1 
ATOM   515  C  CD  . LYS   A 1 64  ? 8.079  -5.162  28.223 1.00 34.33 ? 70  LYS   A CD  1 
ATOM   516  C  CE  . LYS   A 1 64  ? 7.980  -5.993  29.495 1.00 39.69 ? 70  LYS   A CE  1 
ATOM   517  N  NZ  . LYS   A 1 64  ? 8.595  -5.304  30.670 1.00 43.33 ? 70  LYS   A NZ  1 
ATOM   518  N  N   . HIS   A 1 65  ? 11.049 -4.281  23.964 1.00 11.85 ? 71  HIS   A N   1 
ATOM   519  C  CA  . HIS   A 1 65  ? 10.806 -4.137  22.531 1.00 10.82 ? 71  HIS   A CA  1 
ATOM   520  C  C   . HIS   A 1 65  ? 9.349  -4.476  22.264 1.00 12.19 ? 71  HIS   A C   1 
ATOM   521  O  O   . HIS   A 1 65  ? 8.856  -5.525  22.702 1.00 16.30 ? 71  HIS   A O   1 
ATOM   522  C  CB  . HIS   A 1 65  ? 11.710 -5.097  21.721 1.00 10.24 ? 71  HIS   A CB  1 
ATOM   523  C  CG  . HIS   A 1 65  ? 13.176 -4.772  21.827 1.00 11.58 ? 71  HIS   A CG  1 
ATOM   524  N  ND1 . HIS   A 1 65  ? 13.887 -4.092  20.844 1.00 15.25 ? 71  HIS   A ND1 1 
ATOM   525  C  CD2 . HIS   A 1 65  ? 14.027 -5.073  22.839 1.00 11.70 ? 71  HIS   A CD2 1 
ATOM   526  C  CE1 . HIS   A 1 65  ? 15.169 -4.053  21.280 1.00 12.64 ? 71  HIS   A CE1 1 
ATOM   527  N  NE2 . HIS   A 1 65  ? 15.263 -4.587  22.472 1.00 15.59 ? 71  HIS   A NE2 1 
ATOM   528  N  N   . TYR   A 1 66  ? 8.646  -3.617  21.526 1.00 10.52 ? 72  TYR   A N   1 
ATOM   529  C  CA  . TYR   A 1 66  ? 7.228  -3.805  21.235 1.00 11.28 ? 72  TYR   A CA  1 
ATOM   530  C  C   . TYR   A 1 66  ? 6.986  -3.916  19.748 1.00 10.18 ? 72  TYR   A C   1 
ATOM   531  O  O   . TYR   A 1 66  ? 7.483  -3.076  18.978 1.00 10.06 ? 72  TYR   A O   1 
ATOM   532  C  CB  . TYR   A 1 66  ? 6.405  -2.559  21.714 1.00 11.79 ? 72  TYR   A CB  1 
ATOM   533  C  CG  . TYR   A 1 66  ? 6.331  -2.400  23.217 1.00 12.15 ? 72  TYR   A CG  1 
ATOM   534  C  CD1 . TYR   A 1 66  ? 5.508  -3.234  23.995 1.00 13.62 ? 72  TYR   A CD1 1 
ATOM   535  C  CD2 . TYR   A 1 66  ? 7.055  -1.407  23.859 1.00 11.96 ? 72  TYR   A CD2 1 
ATOM   536  C  CE1 . TYR   A 1 66  ? 5.413  -3.078  25.376 1.00 14.51 ? 72  TYR   A CE1 1 
ATOM   537  C  CE2 . TYR   A 1 66  ? 6.951  -1.221  25.247 1.00 13.56 ? 72  TYR   A CE2 1 
ATOM   538  C  CZ  . TYR   A 1 66  ? 6.129  -2.062  25.994 1.00 13.95 ? 72  TYR   A CZ  1 
ATOM   539  O  OH  . TYR   A 1 66  ? 6.037  -1.855  27.361 1.00 16.37 ? 72  TYR   A OH  1 
ATOM   540  N  N   . PRO   A 1 67  ? 6.152  -4.881  19.346 1.00 10.22 ? 73  PRO   A N   1 
ATOM   541  C  CA  . PRO   A 1 67  ? 5.715  -4.919  17.930 1.00 10.59 ? 73  PRO   A CA  1 
ATOM   542  C  C   . PRO   A 1 67  ? 4.710  -3.811  17.637 1.00 11.54 ? 73  PRO   A C   1 
ATOM   543  O  O   . PRO   A 1 67  ? 3.774  -3.631  18.461 1.00 14.74 ? 73  PRO   A O   1 
ATOM   544  C  CB  . PRO   A 1 67  ? 5.051  -6.302  17.759 1.00 13.51 ? 73  PRO   A CB  1 
ATOM   545  C  CG  . PRO   A 1 67  ? 4.713  -6.729  19.137 1.00 15.32 ? 73  PRO   A CG  1 
ATOM   546  C  CD  . PRO   A 1 67  ? 5.588  -5.977  20.147 1.00 11.14 ? 73  PRO   A CD  1 
ATOM   547  N  N   . VAL   A 1 68  ? 4.834  -3.172  16.530 1.00 9.98  ? 74  VAL   A N   1 
ATOM   548  C  CA  . VAL   A 1 68  ? 3.925  -2.053  16.163 1.00 12.11 ? 74  VAL   A CA  1 
ATOM   549  C  C   . VAL   A 1 68  ? 3.582  -2.070  14.704 1.00 11.38 ? 74  VAL   A C   1 
ATOM   550  O  O   . VAL   A 1 68  ? 4.373  -2.445  13.864 1.00 12.13 ? 74  VAL   A O   1 
ATOM   551  C  CB  . VAL   A 1 68  ? 4.502  -0.677  16.543 1.00 15.19 ? 74  VAL   A CB  1 
ATOM   552  C  CG1 . VAL   A 1 68  ? 4.443  -0.496  18.056 1.00 16.69 ? 74  VAL   A CG1 1 
ATOM   553  C  CG2 . VAL   A 1 68  ? 5.903  -0.485  15.987 1.00 16.29 ? 74  VAL   A CG2 1 
ATOM   554  N  N   . SER   A 1 69  ? 2.390  -1.523  14.383 1.00 12.12 ? 75  SER   A N   1 
ATOM   555  C  CA  . SER   A 1 69  ? 1.992  -1.085  13.048 1.00 12.08 ? 75  SER   A CA  1 
ATOM   556  C  C   . SER   A 1 69  ? 2.221  0.430   12.965 1.00 10.66 ? 75  SER   A C   1 
ATOM   557  O  O   . SER   A 1 69  ? 1.846  1.132   13.931 1.00 12.21 ? 75  SER   A O   1 
ATOM   558  C  CB  . SER   A 1 69  ? 0.505  -1.360  12.851 1.00 16.21 ? 75  SER   A CB  1 
ATOM   559  O  OG  . SER   A 1 69  ? -0.075 -0.731  11.725 1.00 25.33 ? 75  SER   A OG  1 
ATOM   560  N  N   . PHE   A 1 70  ? 2.812  0.940   11.905 1.00 11.85 ? 76  PHE   A N   1 
ATOM   561  C  CA  . PHE   A 1 70  ? 3.136  2.360   11.820 1.00 12.29 ? 76  PHE   A CA  1 
ATOM   562  C  C   . PHE   A 1 70  ? 2.744  2.941   10.487 1.00 13.20 ? 76  PHE   A C   1 
ATOM   563  O  O   . PHE   A 1 70  ? 2.655  2.227   9.488  1.00 13.95 ? 76  PHE   A O   1 
ATOM   564  C  CB  . PHE   A 1 70  ? 4.630  2.613   12.177 1.00 12.31 ? 76  PHE   A CB  1 
ATOM   565  C  CG  . PHE   A 1 70  ? 5.641  1.798   11.382 1.00 11.63 ? 76  PHE   A CG  1 
ATOM   566  C  CD1 . PHE   A 1 70  ? 6.065  0.544   11.825 1.00 10.92 ? 76  PHE   A CD1 1 
ATOM   567  C  CD2 . PHE   A 1 70  ? 6.220  2.309   10.241 1.00 11.84 ? 76  PHE   A CD2 1 
ATOM   568  C  CE1 . PHE   A 1 70  ? 6.994  -0.180  11.110 1.00 12.13 ? 76  PHE   A CE1 1 
ATOM   569  C  CE2 . PHE   A 1 70  ? 7.170  1.581   9.521  1.00 12.48 ? 76  PHE   A CE2 1 
ATOM   570  C  CZ  . PHE   A 1 70  ? 7.548  0.335   9.968  1.00 12.18 ? 76  PHE   A CZ  1 
ATOM   571  N  N   . SER   A 1 71  ? 2.445  4.232   10.461 1.00 12.95 ? 77  SER   A N   1 
ATOM   572  C  CA  . SER   A 1 71  ? 2.036  4.917   9.227  1.00 13.93 ? 77  SER   A CA  1 
ATOM   573  C  C   . SER   A 1 71  ? 3.206  5.136   8.266  1.00 14.02 ? 77  SER   A C   1 
ATOM   574  O  O   . SER   A 1 71  ? 4.372  5.012   8.654  1.00 13.78 ? 77  SER   A O   1 
ATOM   575  C  CB  . SER   A 1 71  ? 1.340  6.246   9.570  1.00 15.75 ? 77  SER   A CB  1 
ATOM   576  O  OG  . SER   A 1 71  ? 2.201  7.168   10.225 1.00 17.00 ? 77  SER   A OG  1 
ATOM   577  N  N   . LYS   A 1 72  ? 2.922  5.455   7.032  1.00 14.54 ? 78  LYS   A N   1 
ATOM   578  C  CA  . LYS   A 1 72  ? 3.973  5.778   6.069  1.00 14.56 ? 78  LYS   A CA  1 
ATOM   579  C  C   . LYS   A 1 72  ? 4.606  7.142   6.401  1.00 15.57 ? 78  LYS   A C   1 
ATOM   580  O  O   . LYS   A 1 72  ? 3.919  8.023   6.956  1.00 16.60 ? 78  LYS   A O   1 
ATOM   581  C  CB  . LYS   A 1 72  ? 3.391  5.762   4.651  1.00 16.70 ? 78  LYS   A CB  1 
ATOM   582  C  CG  . LYS   A 1 72  ? 2.942  4.386   4.228  1.00 19.35 ? 78  LYS   A CG  1 
ATOM   583  C  CD  . LYS   A 1 72  ? 2.519  4.356   2.756  1.00 27.08 ? 78  LYS   A CD  1 
ATOM   584  C  CE  . LYS   A 1 72  ? 2.241  2.958   2.288  1.00 33.76 ? 78  LYS   A CE  1 
ATOM   585  N  NZ  . LYS   A 1 72  ? 2.268  2.886   0.807  1.00 37.81 ? 78  LYS   A NZ  1 
ATOM   586  N  N   . PRO   A 1 73  ? 5.866  7.391   6.043  1.00 14.75 ? 79  PRO   A N   1 
ATOM   587  C  CA  . PRO   A 1 73  ? 6.496  8.676   6.388  1.00 14.93 ? 79  PRO   A CA  1 
ATOM   588  C  C   . PRO   A 1 73  ? 5.705  9.849   5.838  1.00 16.47 ? 79  PRO   A C   1 
ATOM   589  O  O   . PRO   A 1 73  ? 5.338  9.846   4.659  1.00 19.00 ? 79  PRO   A O   1 
ATOM   590  C  CB  . PRO   A 1 73  ? 7.912  8.558   5.776  1.00 17.32 ? 79  PRO   A CB  1 
ATOM   591  C  CG  . PRO   A 1 73  ? 8.140  7.112   5.568  1.00 20.94 ? 79  PRO   A CG  1 
ATOM   592  C  CD  . PRO   A 1 73  ? 6.807  6.459   5.375  1.00 16.70 ? 79  PRO   A CD  1 
ATOM   593  N  N   . SER   A 1 74  ? 5.428  10.826  6.689  1.00 15.91 ? 80  SER   A N   1 
ATOM   594  C  CA  . SER   A 1 74  ? 4.519  11.926  6.324  1.00 17.36 ? 80  SER   A CA  1 
ATOM   595  C  C   . SER   A 1 74  ? 4.927  13.199  7.045  1.00 16.02 ? 80  SER   A C   1 
ATOM   596  O  O   . SER   A 1 74  ? 5.750  13.199  7.959  1.00 15.73 ? 80  SER   A O   1 
ATOM   597  C  CB  . SER   A 1 74  ? 3.061  11.587  6.723  1.00 22.82 ? 80  SER   A CB  1 
ATOM   598  O  OG  . SER   A 1 74  ? 2.690  10.232  6.525  1.00 31.53 ? 80  SER   A OG  1 
ATOM   599  N  N   . LEU   A 1 75  ? 4.215  14.301  6.698  1.00 17.63 ? 81  LEU   A N   1 
ATOM   600  C  CA  . LEU   A 1 75  ? 4.406  15.610  7.305  1.00 19.50 ? 81  LEU   A CA  1 
ATOM   601  C  C   . LEU   A 1 75  ? 3.318  15.734  8.381  1.00 20.07 ? 81  LEU   A C   1 
ATOM   602  O  O   . LEU   A 1 75  ? 2.107  15.796  8.052  1.00 22.35 ? 81  LEU   A O   1 
ATOM   603  C  CB  . LEU   A 1 75  ? 4.195  16.695  6.222  1.00 21.01 ? 81  LEU   A CB  1 
ATOM   604  C  CG  . LEU   A 1 75  ? 4.534  18.115  6.618  1.00 24.25 ? 81  LEU   A CG  1 
ATOM   605  C  CD1 . LEU   A 1 75  ? 6.023  18.284  6.866  1.00 24.28 ? 81  LEU   A CD1 1 
ATOM   606  C  CD2 . LEU   A 1 75  ? 4.130  19.094  5.493  1.00 26.53 ? 81  LEU   A CD2 1 
ATOM   607  N  N   . ILE   A 1 76  ? 3.701  15.702  9.655  1.00 18.70 ? 82  ILE   A N   1 
ATOM   608  C  CA  . ILE   A 1 76  ? 2.802  15.668  10.817 1.00 20.42 ? 82  ILE   A CA  1 
ATOM   609  C  C   . ILE   A 1 76  ? 3.048  16.850  11.730 1.00 21.53 ? 82  ILE   A C   1 
ATOM   610  O  O   . ILE   A 1 76  ? 4.212  17.220  11.996 1.00 20.40 ? 82  ILE   A O   1 
ATOM   611  C  CB  . ILE   A 1 76  ? 3.064  14.371  11.595 1.00 21.89 ? 82  ILE   A CB  1 
ATOM   612  C  CG1 . ILE   A 1 76  ? 2.884  13.128  10.668 1.00 24.24 ? 82  ILE   A CG1 1 
ATOM   613  C  CG2 . ILE   A 1 76  ? 2.255  14.314  12.941 1.00 23.67 ? 82  ILE   A CG2 1 
ATOM   614  C  CD1 . ILE   A 1 76  ? 2.731  11.985  11.191 1.00 24.84 ? 82  ILE   A CD1 1 
ATOM   615  N  N   . PHE   A 1 77  ? 1.972  17.452  12.259 1.00 23.27 ? 83  PHE   A N   1 
ATOM   616  C  CA  . PHE   A 1 77  ? 2.112  18.554  13.200 1.00 23.37 ? 83  PHE   A CA  1 
ATOM   617  C  C   . PHE   A 1 77  ? 2.431  17.966  14.565 1.00 24.80 ? 83  PHE   A C   1 
ATOM   618  O  O   . PHE   A 1 77  ? 1.735  17.074  15.050 1.00 27.91 ? 83  PHE   A O   1 
ATOM   619  C  CB  . PHE   A 1 77  ? 0.789  19.370  13.270 1.00 24.67 ? 83  PHE   A CB  1 
ATOM   620  C  CG  . PHE   A 1 77  ? 0.995  20.674  13.981 1.00 27.28 ? 83  PHE   A CG  1 
ATOM   621  C  CD1 . PHE   A 1 77  ? 1.723  21.691  13.389 1.00 28.89 ? 83  PHE   A CD1 1 
ATOM   622  C  CD2 . PHE   A 1 77  ? 0.556  20.841  15.286 1.00 30.11 ? 83  PHE   A CD2 1 
ATOM   623  C  CE1 . PHE   A 1 77  ? 1.932  22.886  14.052 1.00 31.07 ? 83  PHE   A CE1 1 
ATOM   624  C  CE2 . PHE   A 1 77  ? 0.758  22.037  15.951 1.00 30.73 ? 83  PHE   A CE2 1 
ATOM   625  C  CZ  . PHE   A 1 77  ? 1.436  23.054  15.328 1.00 31.25 ? 83  PHE   A CZ  1 
ATOM   626  N  N   . VAL   A 1 78  ? 3.542  18.417  15.172 1.00 21.82 ? 84  VAL   A N   1 
ATOM   627  C  CA  . VAL   A 1 78  ? 3.976  17.917  16.466 1.00 20.31 ? 84  VAL   A CA  1 
ATOM   628  C  C   . VAL   A 1 78  ? 3.906  19.081  17.472 1.00 20.15 ? 84  VAL   A C   1 
ATOM   629  O  O   . VAL   A 1 78  ? 4.406  20.160  17.176 1.00 20.91 ? 84  VAL   A O   1 
ATOM   630  C  CB  . VAL   A 1 78  ? 5.440  17.392  16.344 1.00 18.55 ? 84  VAL   A CB  1 
ATOM   631  C  CG1 . VAL   A 1 78  ? 5.966  16.895  17.697 1.00 19.14 ? 84  VAL   A CG1 1 
ATOM   632  C  CG2 . VAL   A 1 78  ? 5.511  16.293  15.265 1.00 19.33 ? 84  VAL   A CG2 1 
ATOM   633  N  N   . GLU   A 1 79  ? 3.388  18.790  18.674 1.00 20.53 ? 85  GLU   A N   1 
ATOM   634  C  CA  . GLU   A 1 79  ? 3.268  19.812  19.707 1.00 23.08 ? 85  GLU   A CA  1 
ATOM   635  C  C   . GLU   A 1 79  ? 4.617  20.283  20.204 1.00 23.58 ? 85  GLU   A C   1 
ATOM   636  O  O   . GLU   A 1 79  ? 5.616  19.557  20.110 1.00 23.64 ? 85  GLU   A O   1 
ATOM   637  C  CB  . GLU   A 1 79  ? 2.454  19.273  20.891 1.00 27.00 ? 85  GLU   A CB  1 
ATOM   638  C  CG  . GLU   A 1 79  ? 0.971  19.095  20.569 1.00 34.89 ? 85  GLU   A CG  1 
ATOM   639  C  CD  . GLU   A 1 79  ? 0.293  20.315  19.974 1.00 46.34 ? 85  GLU   A CD  1 
ATOM   640  O  OE1 . GLU   A 1 79  ? 0.470  21.435  20.511 1.00 48.87 ? 85  GLU   A OE1 1 
ATOM   641  O  OE2 . GLU   A 1 79  ? -0.399 20.152  18.946 1.00 51.37 ? 85  GLU   A OE2 1 
ATOM   642  N  N   . ALA   A 1 80  ? 4.630  21.482  20.810 1.00 23.93 ? 86  ALA   A N   1 
ATOM   643  C  CA  . ALA   A 1 80  ? 5.838  22.048  21.401 1.00 25.24 ? 86  ALA   A CA  1 
ATOM   644  C  C   . ALA   A 1 80  ? 6.409  21.142  22.449 1.00 25.91 ? 86  ALA   A C   1 
ATOM   645  O  O   . ALA   A 1 80  ? 5.678  20.451  23.185 1.00 27.21 ? 86  ALA   A O   1 
ATOM   646  C  CB  . ALA   A 1 80  ? 5.527  23.384  22.048 1.00 26.34 ? 86  ALA   A CB  1 
ATOM   647  N  N   . SER   A 1 81  ? 7.747  21.087  22.483 1.00 25.59 ? 87  SER   A N   1 
ATOM   648  C  CA  . SER   A 1 81  ? 8.441  20.297  23.489 1.00 25.00 ? 87  SER   A CA  1 
ATOM   649  C  C   . SER   A 1 81  ? 9.552  21.192  24.079 1.00 25.15 ? 87  SER   A C   1 
ATOM   650  O  O   . SER   A 1 81  ? 9.656  22.362  23.744 1.00 26.41 ? 87  SER   A O   1 
ATOM   651  C  CB  . SER   A 1 81  ? 9.064  19.054  22.854 1.00 24.98 ? 87  SER   A CB  1 
ATOM   652  O  OG  . SER   A 1 81  ? 10.110 19.459  21.977 1.00 22.85 ? 87  SER   A OG  1 
ATOM   653  N  N   . GLU   A 1 82  ? 10.475 20.578  24.860 1.00 25.53 ? 88  GLU   A N   1 
ATOM   654  C  CA  . GLU   A 1 82  ? 11.626 21.321  25.380 1.00 25.58 ? 88  GLU   A CA  1 
ATOM   655  C  C   . GLU   A 1 82  ? 12.603 21.678  24.221 1.00 23.17 ? 88  GLU   A C   1 
ATOM   656  O  O   . GLU   A 1 82  ? 13.392 22.617  24.350 1.00 23.90 ? 88  GLU   A O   1 
ATOM   657  C  CB  . GLU   A 1 82  ? 12.371 20.397  26.364 1.00 30.42 ? 88  GLU   A CB  1 
ATOM   658  C  CG  . GLU   A 1 82  ? 13.470 21.062  27.155 1.00 40.44 ? 88  GLU   A CG  1 
ATOM   659  C  CD  . GLU   A 1 82  ? 14.227 20.078  28.021 1.00 49.95 ? 88  GLU   A CD  1 
ATOM   660  O  OE1 . GLU   A 1 82  ? 15.475 20.184  28.079 1.00 53.45 ? 88  GLU   A OE1 1 
ATOM   661  O  OE2 . GLU   A 1 82  ? 13.575 19.193  28.625 1.00 50.79 ? 88  GLU   A OE2 1 
ATOM   662  N  N   . TYR   A 1 83  ? 12.537 20.948  23.084 1.00 21.52 ? 89  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 83  ? 13.536 21.102  22.009 1.00 20.45 ? 89  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 83  ? 13.073 21.780  20.735 1.00 19.66 ? 89  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 83  ? 13.894 22.270  19.954 1.00 18.96 ? 89  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 83  ? 14.079 19.715  21.675 1.00 21.14 ? 89  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 83  ? 14.715 19.042  22.869 1.00 22.51 ? 89  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 83  ? 16.022 19.323  23.233 1.00 24.80 ? 89  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 83  ? 13.984 18.191  23.681 1.00 25.91 ? 89  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 83  ? 16.622 18.677  24.310 1.00 26.78 ? 89  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 83  ? 14.565 17.549  24.765 1.00 27.56 ? 89  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 83  ? 15.864 17.843  25.116 1.00 29.17 ? 89  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 83  ? 16.429 17.149  26.165 1.00 32.85 ? 89  TYR   A OH  1 
ATOM   674  N  N   . TYR   A 1 84  ? 11.749 21.795  20.495 1.00 20.85 ? 90  TYR   A N   1 
ATOM   675  C  CA  . TYR   A 1 84  ? 11.214 22.447  19.292 1.00 20.23 ? 90  TYR   A CA  1 
ATOM   676  C  C   . TYR   A 1 84  ? 9.893  23.132  19.645 1.00 21.29 ? 90  TYR   A C   1 
ATOM   677  O  O   . TYR   A 1 84  ? 9.148  22.577  20.462 1.00 22.01 ? 90  TYR   A O   1 
ATOM   678  C  CB  . TYR   A 1 84  ? 10.882 21.393  18.192 1.00 19.50 ? 90  TYR   A CB  1 
ATOM   679  C  CG  . TYR   A 1 84  ? 12.074 20.618  17.631 1.00 17.08 ? 90  TYR   A CG  1 
ATOM   680  C  CD1 . TYR   A 1 84  ? 12.946 21.203  16.725 1.00 16.95 ? 90  TYR   A CD1 1 
ATOM   681  C  CD2 . TYR   A 1 84  ? 12.311 19.302  18.007 1.00 16.39 ? 90  TYR   A CD2 1 
ATOM   682  C  CE1 . TYR   A 1 84  ? 14.034 20.493  16.210 1.00 15.38 ? 90  TYR   A CE1 1 
ATOM   683  C  CE2 . TYR   A 1 84  ? 13.401 18.594  17.526 1.00 15.69 ? 90  TYR   A CE2 1 
ATOM   684  C  CZ  . TYR   A 1 84  ? 14.270 19.199  16.641 1.00 14.77 ? 90  TYR   A CZ  1 
ATOM   685  O  OH  . TYR   A 1 84  ? 15.342 18.497  16.134 1.00 14.21 ? 90  TYR   A OH  1 
ATOM   686  N  N   . PRO   A 1 85  ? 9.564  24.217  18.944 1.00 22.73 ? 91  PRO   A N   1 
ATOM   687  C  CA  . PRO   A 1 85  ? 8.209  24.791  19.082 1.00 23.95 ? 91  PRO   A CA  1 
ATOM   688  C  C   . PRO   A 1 85  ? 7.225  23.858  18.366 1.00 25.38 ? 91  PRO   A C   1 
ATOM   689  O  O   . PRO   A 1 85  ? 7.645  22.925  17.624 1.00 25.34 ? 91  PRO   A O   1 
ATOM   690  C  CB  . PRO   A 1 85  ? 8.337  26.145  18.347 1.00 26.10 ? 91  PRO   A CB  1 
ATOM   691  C  CG  . PRO   A 1 85  ? 9.351  25.903  17.292 1.00 26.80 ? 91  PRO   A CG  1 
ATOM   692  C  CD  . PRO   A 1 85  ? 10.354 24.936  17.913 1.00 23.26 ? 91  PRO   A CD  1 
ATOM   693  N  N   . ALA   A 1 86  ? 5.911  24.096  18.505 1.00 25.94 ? 92  ALA   A N   1 
ATOM   694  C  CA  . ALA   A 1 86  ? 4.910  23.304  17.770 1.00 25.70 ? 92  ALA   A CA  1 
ATOM   695  C  C   . ALA   A 1 86  ? 5.173  23.605  16.261 1.00 25.60 ? 92  ALA   A C   1 
ATOM   696  O  O   . ALA   A 1 86  ? 5.439  24.748  15.895 1.00 27.14 ? 92  ALA   A O   1 
ATOM   697  C  CB  . ALA   A 1 86  ? 3.509  23.770  18.171 1.00 25.50 ? 92  ALA   A CB  1 
ATOM   698  N  N   . ARG   A 1 87  ? 5.287  22.560  15.431 1.00 24.61 ? 93  ARG   A N   1 
ATOM   699  C  CA  . ARG   A 1 87  ? 5.673  22.746  14.037 1.00 23.52 ? 93  ARG   A CA  1 
ATOM   700  C  C   . ARG   A 1 87  ? 5.317  21.462  13.272 1.00 22.05 ? 93  ARG   A C   1 
ATOM   701  O  O   . ARG   A 1 87  ? 4.948  20.464  13.872 1.00 23.07 ? 93  ARG   A O   1 
ATOM   702  C  CB  . ARG   A 1 87  ? 7.217  22.986  13.954 1.00 24.22 ? 93  ARG   A CB  1 
ATOM   703  C  CG  . ARG   A 1 87  ? 8.079  21.674  13.904 1.00 24.58 ? 93  ARG   A CG  1 
ATOM   704  C  CD  . ARG   A 1 87  ? 9.444  21.863  14.465 1.00 22.80 ? 93  ARG   A CD  1 
ATOM   705  N  NE  . ARG   A 1 87  ? 10.386 20.781  14.097 1.00 22.24 ? 93  ARG   A NE  1 
ATOM   706  C  CZ  . ARG   A 1 87  ? 10.385 19.551  14.572 1.00 22.62 ? 93  ARG   A CZ  1 
ATOM   707  N  NH1 . ARG   A 1 87  ? 9.444  19.163  15.444 1.00 23.16 ? 93  ARG   A NH1 1 
ATOM   708  N  NH2 . ARG   A 1 87  ? 11.331 18.689  14.196 1.00 17.73 ? 93  ARG   A NH2 1 
ATOM   709  N  N   . TYR   A 1 88  ? 5.515  21.483  11.953 1.00 22.29 ? 94  TYR   A N   1 
ATOM   710  C  CA  . TYR   A 1 88  ? 5.386  20.285  11.148 1.00 23.35 ? 94  TYR   A CA  1 
ATOM   711  C  C   . TYR   A 1 88  ? 6.744  19.592  11.058 1.00 20.17 ? 94  TYR   A C   1 
ATOM   712  O  O   . TYR   A 1 88  ? 7.728  20.194  10.658 1.00 21.09 ? 94  TYR   A O   1 
ATOM   713  C  CB  . TYR   A 1 88  ? 4.939  20.632  9.741  1.00 24.38 ? 94  TYR   A CB  1 
ATOM   714  C  CG  . TYR   A 1 88  ? 3.461  20.958  9.683  1.00 24.90 ? 94  TYR   A CG  1 
ATOM   715  C  CD1 . TYR   A 1 88  ? 2.513  19.952  9.613  1.00 25.23 ? 94  TYR   A CD1 1 
ATOM   716  C  CD2 . TYR   A 1 88  ? 3.007  22.268  9.787  1.00 26.48 ? 94  TYR   A CD2 1 
ATOM   717  C  CE1 . TYR   A 1 88  ? 1.153  20.235  9.596  1.00 27.01 ? 94  TYR   A CE1 1 
ATOM   718  C  CE2 . TYR   A 1 88  ? 1.647  22.562  9.763  1.00 27.40 ? 94  TYR   A CE2 1 
ATOM   719  C  CZ  . TYR   A 1 88  ? 0.722  21.537  9.693  1.00 27.86 ? 94  TYR   A CZ  1 
ATOM   720  O  OH  . TYR   A 1 88  ? -0.639 21.753  9.695  1.00 31.45 ? 94  TYR   A OH  1 
ATOM   721  N  N   . GLN   A 1 89  ? 6.775  18.281  11.368 1.00 17.85 ? 95  GLN   A N   1 
ATOM   722  C  CA  . GLN   A 1 89  ? 7.971  17.446  11.246 1.00 16.13 ? 95  GLN   A CA  1 
ATOM   723  C  C   . GLN   A 1 89  ? 7.764  16.555  10.017 1.00 15.78 ? 95  GLN   A C   1 
ATOM   724  O  O   . GLN   A 1 89  ? 6.687  15.957  9.838  1.00 16.48 ? 95  GLN   A O   1 
ATOM   725  C  CB  . GLN   A 1 89  ? 8.209  16.639  12.523 1.00 16.03 ? 95  GLN   A CB  1 
ATOM   726  C  CG  . GLN   A 1 89  ? 9.455  15.787  12.429 1.00 15.62 ? 95  GLN   A CG  1 
ATOM   727  C  CD  . GLN   A 1 89  ? 10.010 15.329  13.767 1.00 14.48 ? 95  GLN   A CD  1 
ATOM   728  O  OE1 . GLN   A 1 89  ? 10.025 16.044  14.788 1.00 15.74 ? 95  GLN   A OE1 1 
ATOM   729  N  NE2 . GLN   A 1 89  ? 10.512 14.091  13.764 1.00 13.81 ? 95  GLN   A NE2 1 
ATOM   730  N  N   . SER   A 1 90  ? 8.781  16.455  9.156  1.00 14.54 ? 96  SER   A N   1 
ATOM   731  C  CA  . SER   A 1 90  ? 8.676  15.672  7.945  1.00 14.99 ? 96  SER   A CA  1 
ATOM   732  C  C   . SER   A 1 90  ? 9.273  14.269  8.138  1.00 13.57 ? 96  SER   A C   1 
ATOM   733  O  O   . SER   A 1 90  ? 10.043 14.038  9.084  1.00 13.32 ? 96  SER   A O   1 
ATOM   734  C  CB  . SER   A 1 90  ? 9.360  16.405  6.795  1.00 16.83 ? 96  SER   A CB  1 
ATOM   735  O  OG  . SER   A 1 90  ? 10.745 16.502  7.081  1.00 19.64 ? 96  SER   A OG  1 
ATOM   736  N  N   . HIS   A 1 91  ? 8.880  13.344  7.226  1.00 13.75 ? 97  HIS   A N   1 
ATOM   737  C  CA  . HIS   A 1 91  ? 9.366  11.969  7.197  1.00 13.26 ? 97  HIS   A CA  1 
ATOM   738  C  C   . HIS   A 1 91  ? 9.106  11.273  8.545  1.00 12.65 ? 97  HIS   A C   1 
ATOM   739  O  O   . HIS   A 1 91  ? 9.933  10.423  8.973  1.00 12.84 ? 97  HIS   A O   1 
ATOM   740  C  CB  . HIS   A 1 91  ? 10.883 11.922  6.815  1.00 14.50 ? 97  HIS   A CB  1 
ATOM   741  C  CG  . HIS   A 1 91  ? 11.192 12.508  5.448  1.00 15.50 ? 97  HIS   A CG  1 
ATOM   742  N  ND1 . HIS   A 1 91  ? 11.300 11.701  4.340  1.00 18.44 ? 97  HIS   A ND1 1 
ATOM   743  C  CD2 . HIS   A 1 91  ? 11.331 13.796  5.065  1.00 17.62 ? 97  HIS   A CD2 1 
ATOM   744  C  CE1 . HIS   A 1 91  ? 11.575 12.515  3.315  1.00 18.63 ? 97  HIS   A CE1 1 
ATOM   745  N  NE2 . HIS   A 1 91  ? 11.578 13.781  3.695  1.00 19.21 ? 97  HIS   A NE2 1 
ATOM   746  N  N   . LEU   A 1 92  ? 7.994  11.568  9.175  1.00 11.99 ? 98  LEU   A N   1 
ATOM   747  C  CA  . LEU   A 1 92  ? 7.641  11.019  10.489 1.00 11.93 ? 98  LEU   A CA  1 
ATOM   748  C  C   . LEU   A 1 92  ? 6.582  9.932   10.303 1.00 12.06 ? 98  LEU   A C   1 
ATOM   749  O  O   . LEU   A 1 92  ? 5.652  10.107  9.503  1.00 12.98 ? 98  LEU   A O   1 
ATOM   750  C  CB  . LEU   A 1 92  ? 7.084  12.142  11.382 1.00 13.34 ? 98  LEU   A CB  1 
ATOM   751  C  CG  . LEU   A 1 92  ? 6.785  11.745  12.864 1.00 15.32 ? 98  LEU   A CG  1 
ATOM   752  C  CD1 . LEU   A 1 92  ? 8.036  11.427  13.597 1.00 16.17 ? 98  LEU   A CD1 1 
ATOM   753  C  CD2 . LEU   A 1 92  ? 6.079  12.903  13.624 1.00 18.92 ? 98  LEU   A CD2 1 
ATOM   754  N  N   . MET   A 1 93  ? 6.690  8.834   11.074 1.00 12.44 ? 99  MET   A N   1 
ATOM   755  C  CA  . MET   A 1 93  ? 5.736  7.705   11.053 1.00 11.87 ? 99  MET   A CA  1 
ATOM   756  C  C   . MET   A 1 93  ? 5.159  7.571   12.448 1.00 12.09 ? 99  MET   A C   1 
ATOM   757  O  O   . MET   A 1 93  ? 5.910  7.575   13.434 1.00 13.15 ? 99  MET   A O   1 
ATOM   758  C  CB  . MET   A 1 93  ? 6.501  6.440   10.705 1.00 12.85 ? 99  MET   A CB  1 
ATOM   759  C  CG  . MET   A 1 93  ? 7.128  6.532   9.315  1.00 13.87 ? 99  MET   A CG  1 
ATOM   760  S  SD  . MET   A 1 93  ? 8.231  5.163   8.826  1.00 16.11 ? 99  MET   A SD  1 
ATOM   761  C  CE  . MET   A 1 93  ? 9.549  5.351   10.108 1.00 20.68 ? 99  MET   A CE  1 
ATOM   762  N  N   . LEU   A 1 94  ? 3.846  7.388   12.585 1.00 12.22 ? 100 LEU   A N   1 
ATOM   763  C  CA  . LEU   A 1 94  ? 3.224  7.264   13.892 1.00 12.47 ? 100 LEU   A CA  1 
ATOM   764  C  C   . LEU   A 1 94  ? 2.741  5.852   14.173 1.00 12.04 ? 100 LEU   A C   1 
ATOM   765  O  O   . LEU   A 1 94  ? 2.294  5.143   13.245 1.00 13.35 ? 100 LEU   A O   1 
ATOM   766  C  CB  . LEU   A 1 94  ? 2.012  8.208   14.032 1.00 14.74 ? 100 LEU   A CB  1 
ATOM   767  C  CG  . LEU   A 1 94  ? 2.272  9.702   13.992 1.00 19.27 ? 100 LEU   A CG  1 
ATOM   768  C  CD1 . LEU   A 1 94  ? 1.009  10.503  14.367 1.00 21.45 ? 100 LEU   A CD1 1 
ATOM   769  C  CD2 . LEU   A 1 94  ? 3.316  10.132  15.000 1.00 22.31 ? 100 LEU   A CD2 1 
ATOM   770  N  N   . ALA   A 1 95  ? 2.765  5.465   15.436 1.00 12.00 ? 101 ALA   A N   1 
ATOM   771  C  CA  . ALA   A 1 95  ? 2.234  4.170   15.889 1.00 11.86 ? 101 ALA   A CA  1 
ATOM   772  C  C   . ALA   A 1 95  ? 1.605  4.369   17.272 1.00 11.52 ? 101 ALA   A C   1 
ATOM   773  O  O   . ALA   A 1 95  ? 1.890  5.358   17.975 1.00 11.97 ? 101 ALA   A O   1 
ATOM   774  C  CB  . ALA   A 1 95  ? 3.375  3.106   16.015 1.00 13.20 ? 101 ALA   A CB  1 
ATOM   775  N  N   . VAL   A 1 96  ? 0.807  3.370   17.696 1.00 11.33 ? 102 VAL   A N   1 
ATOM   776  C  CA  . VAL   A 1 96  ? 0.293  3.352   19.040 1.00 11.23 ? 102 VAL   A CA  1 
ATOM   777  C  C   . VAL   A 1 96  ? 1.331  2.595   19.913 1.00 12.95 ? 102 VAL   A C   1 
ATOM   778  O  O   . VAL   A 1 96  ? 1.675  1.452   19.633 1.00 15.36 ? 102 VAL   A O   1 
ATOM   779  C  CB  . VAL   A 1 96  ? -1.059 2.624   19.059 1.00 11.91 ? 102 VAL   A CB  1 
ATOM   780  C  CG1 . VAL   A 1 96  ? -1.559 2.442   20.499 1.00 13.39 ? 102 VAL   A CG1 1 
ATOM   781  C  CG2 . VAL   A 1 96  ? -2.064 3.424   18.235 1.00 12.62 ? 102 VAL   A CG2 1 
ATOM   782  N  N   . GLY   A 1 97  ? 1.816  3.295   20.917 1.00 12.97 ? 103 GLY   A N   1 
ATOM   783  C  CA  . GLY   A 1 97  ? 2.838  2.704   21.792 1.00 14.12 ? 103 GLY   A CA  1 
ATOM   784  C  C   . GLY   A 1 97  ? 3.249  3.695   22.816 1.00 14.78 ? 103 GLY   A C   1 
ATOM   785  O  O   . GLY   A 1 97  ? 3.004  4.888   22.717 1.00 15.68 ? 103 GLY   A O   1 
ATOM   786  N  N   . HIS   A 1 98  ? 3.880  3.156   23.891 1.00 16.04 ? 104 HIS   A N   1 
ATOM   787  C  CA  . HIS   A 1 98  ? 4.352  3.999   24.952 1.00 17.23 ? 104 HIS   A CA  1 
ATOM   788  C  C   . HIS   A 1 98  ? 5.633  4.719   24.582 1.00 15.74 ? 104 HIS   A C   1 
ATOM   789  O  O   . HIS   A 1 98  ? 6.582  4.125   24.017 1.00 15.28 ? 104 HIS   A O   1 
ATOM   790  C  CB  . HIS   A 1 98  ? 4.588  3.159   26.241 1.00 17.20 ? 104 HIS   A CB  1 
ATOM   791  C  CG  . HIS   A 1 98  ? 4.952  4.032   27.396 1.00 17.78 ? 104 HIS   A CG  1 
ATOM   792  N  ND1 . HIS   A 1 98  ? 4.008  4.864   27.980 1.00 17.97 ? 104 HIS   A ND1 1 
ATOM   793  C  CD2 . HIS   A 1 98  ? 6.148  4.252   27.994 1.00 18.60 ? 104 HIS   A CD2 1 
ATOM   794  C  CE1 . HIS   A 1 98  ? 4.675  5.591   28.878 1.00 18.74 ? 104 HIS   A CE1 1 
ATOM   795  N  NE2 . HIS   A 1 98  ? 5.954  5.208   28.954 1.00 19.22 ? 104 HIS   A NE2 1 
ATOM   796  N  N   . SER   A 1 99  ? 5.712  5.964   24.883 1.00 17.01 ? 105 SER   A N   1 
ATOM   797  C  CA  . SER   A 1 99  ? 6.868  6.726   24.794 1.00 16.35 ? 105 SER   A CA  1 
ATOM   798  C  C   . SER   A 1 99  ? 6.890  7.836   25.843 1.00 17.67 ? 105 SER   A C   1 
ATOM   799  O  O   . SER   A 1 99  ? 5.802  8.303   26.251 1.00 20.89 ? 105 SER   A O   1 
ATOM   800  C  CB  . SER   A 1 99  ? 7.135  7.217   23.374 1.00 17.66 ? 105 SER   A CB  1 
ATOM   801  O  OG  . SER   A 1 99  ? 6.081  8.072   22.966 1.00 20.41 ? 105 SER   A OG  1 
ATOM   802  N  N   . GLU   A 1 100 ? 8.117  8.273   26.218 1.00 14.57 ? 106 GLU   A N   1 
ATOM   803  C  CA  . GLU   A 1 100 ? 8.487  9.396   27.102 1.00 15.79 ? 106 GLU   A CA  1 
ATOM   804  C  C   . GLU   A 1 100 ? 9.654  10.117  26.450 1.00 16.89 ? 106 GLU   A C   1 
ATOM   805  O  O   . GLU   A 1 100 ? 10.314 9.582   25.538 1.00 14.79 ? 106 GLU   A O   1 
ATOM   806  C  CB  . GLU   A 1 100 ? 8.897  8.872   28.494 1.00 16.89 ? 106 GLU   A CB  1 
ATOM   807  C  CG  . GLU   A 1 100 ? 7.746  8.121   29.157 1.00 18.33 ? 106 GLU   A CG  1 
ATOM   808  C  CD  . GLU   A 1 100 ? 7.938  7.534   30.551 1.00 20.45 ? 106 GLU   A CD  1 
ATOM   809  O  OE1 . GLU   A 1 100 ? 8.753  8.075   31.329 1.00 26.08 ? 106 GLU   A OE1 1 
ATOM   810  O  OE2 . GLU   A 1 100 ? 7.288  6.511   30.851 1.00 18.67 ? 106 GLU   A OE2 1 
ATOM   811  N  N   . PRO   A 1 101 ? 9.912  11.383  26.791 1.00 17.65 ? 107 PRO   A N   1 
ATOM   812  C  CA  . PRO   A 1 101 ? 10.936 12.154  26.040 1.00 17.77 ? 107 PRO   A CA  1 
ATOM   813  C  C   . PRO   A 1 101 ? 12.300 11.464  25.888 1.00 16.85 ? 107 PRO   A C   1 
ATOM   814  O  O   . PRO   A 1 101 ? 12.865 11.413  24.776 1.00 16.38 ? 107 PRO   A O   1 
ATOM   815  C  CB  . PRO   A 1 101 ? 10.986 13.496  26.815 1.00 20.53 ? 107 PRO   A CB  1 
ATOM   816  C  CG  . PRO   A 1 101 ? 9.615  13.616  27.363 1.00 21.92 ? 107 PRO   A CG  1 
ATOM   817  C  CD  . PRO   A 1 101 ? 9.175  12.243  27.747 1.00 18.68 ? 107 PRO   A CD  1 
ATOM   818  N  N   . GLY   A 1 102 ? 12.811 10.841  26.949 1.00 15.31 ? 108 GLY   A N   1 
ATOM   819  C  CA  . GLY   A 1 102 ? 14.085 10.126  26.958 1.00 15.02 ? 108 GLY   A CA  1 
ATOM   820  C  C   . GLY   A 1 102 ? 14.089 8.818   26.166 1.00 12.83 ? 108 GLY   A C   1 
ATOM   821  O  O   . GLY   A 1 102 ? 15.134 8.196   25.996 1.00 13.09 ? 108 GLY   A O   1 
ATOM   822  N  N   . ASP   A 1 103 ? 12.921 8.389   25.647 1.00 11.65 ? 109 ASP   A N   1 
ATOM   823  C  CA  . ASP   A 1 103 ? 12.869 7.237   24.737 1.00 10.95 ? 109 ASP   A CA  1 
ATOM   824  C  C   . ASP   A 1 103 ? 13.390 7.567   23.316 1.00 10.76 ? 109 ASP   A C   1 
ATOM   825  O  O   . ASP   A 1 103 ? 13.657 6.639   22.516 1.00 10.72 ? 109 ASP   A O   1 
ATOM   826  C  CB  . ASP   A 1 103 ? 11.432 6.673   24.623 1.00 11.08 ? 109 ASP   A CB  1 
ATOM   827  C  CG  . ASP   A 1 103 ? 11.036 5.930   25.874 1.00 11.26 ? 109 ASP   A CG  1 
ATOM   828  O  OD1 . ASP   A 1 103 ? 11.904 5.258   26.436 1.00 12.06 ? 109 ASP   A OD1 1 
ATOM   829  O  OD2 . ASP   A 1 103 ? 9.829  6.020   26.277 1.00 11.91 ? 109 ASP   A OD2 1 
ATOM   830  N  N   . CYS   A 1 104 ? 13.571 8.876   23.000 1.00 10.59 ? 110 CYS   A N   1 
ATOM   831  C  CA  . CYS   A 1 104 ? 14.127 9.234   21.678 1.00 10.96 ? 110 CYS   A CA  1 
ATOM   832  C  C   . CYS   A 1 104 ? 15.456 8.534   21.466 1.00 10.65 ? 110 CYS   A C   1 
ATOM   833  O  O   . CYS   A 1 104 ? 16.307 8.447   22.359 1.00 11.25 ? 110 CYS   A O   1 
ATOM   834  C  CB  . CYS   A 1 104 ? 14.304 10.745  21.591 1.00 12.12 ? 110 CYS   A CB  1 
ATOM   835  S  SG  . CYS   A 1 104 ? 12.736 11.634  21.332 1.00 13.54 ? 110 CYS   A SG  1 
ATOM   836  N  N   . GLY   A 1 105 ? 15.638 8.006   20.260 1.00 9.87  ? 111 GLY   A N   1 
ATOM   837  C  CA  . GLY   A 1 105 ? 16.837 7.299   19.876 1.00 10.54 ? 111 GLY   A CA  1 
ATOM   838  C  C   . GLY   A 1 105 ? 16.661 5.789   19.809 1.00 10.41 ? 111 GLY   A C   1 
ATOM   839  O  O   . GLY   A 1 105 ? 17.519 5.090   19.251 1.00 10.85 ? 111 GLY   A O   1 
ATOM   840  N  N   . GLY   A 1 106 ? 15.587 5.258   20.421 1.00 9.91  ? 112 GLY   A N   1 
ATOM   841  C  CA  . GLY   A 1 106 ? 15.333 3.821   20.328 1.00 9.77  ? 112 GLY   A CA  1 
ATOM   842  C  C   . GLY   A 1 106 ? 15.097 3.404   18.878 1.00 8.93  ? 112 GLY   A C   1 
ATOM   843  O  O   . GLY   A 1 106 ? 14.403 4.116   18.131 1.00 9.48  ? 112 GLY   A O   1 
ATOM   844  N  N   . ILE   A 1 107 ? 15.613 2.246   18.486 1.00 9.20  ? 113 ILE   A N   1 
ATOM   845  C  CA  . ILE   A 1 107 ? 15.464 1.823   17.081 1.00 9.33  ? 113 ILE   A CA  1 
ATOM   846  C  C   . ILE   A 1 107 ? 14.126 1.177   16.807 1.00 8.68  ? 113 ILE   A C   1 
ATOM   847  O  O   . ILE   A 1 107 ? 13.648 0.333   17.597 1.00 8.88  ? 113 ILE   A O   1 
ATOM   848  C  CB  . ILE   A 1 107 ? 16.623 0.850   16.746 1.00 9.34  ? 113 ILE   A CB  1 
ATOM   849  C  CG1 . ILE   A 1 107 ? 17.898 1.705   16.470 1.00 11.32 ? 113 ILE   A CG1 1 
ATOM   850  C  CG2 . ILE   A 1 107 ? 16.343 -0.037  15.523 1.00 10.38 ? 113 ILE   A CG2 1 
ATOM   851  C  CD1 . ILE   A 1 107 ? 19.185 0.872   16.373 1.00 14.30 ? 113 ILE   A CD1 1 
ATOM   852  N  N   . LEU   A 1 108 ? 13.556 1.504   15.637 1.00 8.24  ? 114 LEU   A N   1 
ATOM   853  C  CA  . LEU   A 1 108 ? 12.457 0.777   15.017 1.00 8.50  ? 114 LEU   A CA  1 
ATOM   854  C  C   . LEU   A 1 108 ? 13.103 -0.082  13.905 1.00 8.41  ? 114 LEU   A C   1 
ATOM   855  O  O   . LEU   A 1 108 ? 13.852 0.461   13.068 1.00 9.24  ? 114 LEU   A O   1 
ATOM   856  C  CB  . LEU   A 1 108 ? 11.458 1.783   14.374 1.00 9.11  ? 114 LEU   A CB  1 
ATOM   857  C  CG  . LEU   A 1 108 ? 10.340 1.162   13.499 1.00 9.44  ? 114 LEU   A CG  1 
ATOM   858  C  CD1 . LEU   A 1 108 ? 9.366  0.344   14.352 1.00 10.41 ? 114 LEU   A CD1 1 
ATOM   859  C  CD2 . LEU   A 1 108 ? 9.581  2.290   12.740 1.00 11.39 ? 114 LEU   A CD2 1 
ATOM   860  N  N   . ARG   A 1 109 ? 12.751 -1.353  13.830 1.00 8.90  ? 115 ARG   A N   1 
ATOM   861  C  CA  . ARG   A 1 109 ? 13.328 -2.286  12.816 1.00 9.45  ? 115 ARG   A CA  1 
ATOM   862  C  C   . ARG   A 1 109 ? 12.256 -3.188  12.279 1.00 9.91  ? 115 ARG   A C   1 
ATOM   863  O  O   . ARG   A 1 109 ? 11.244 -3.477  12.916 1.00 10.18 ? 115 ARG   A O   1 
ATOM   864  C  CB  . ARG   A 1 109 ? 14.512 -3.080  13.440 1.00 10.75 ? 115 ARG   A CB  1 
ATOM   865  C  CG  . ARG   A 1 109 ? 14.033 -4.058  14.533 1.00 11.20 ? 115 ARG   A CG  1 
ATOM   866  C  CD  . ARG   A 1 109 ? 15.244 -4.800  15.110 1.00 12.80 ? 115 ARG   A CD  1 
ATOM   867  N  NE  . ARG   A 1 109 ? 16.050 -3.920  15.934 1.00 13.73 ? 115 ARG   A NE  1 
ATOM   868  C  CZ  . ARG   A 1 109 ? 17.348 -3.720  15.808 1.00 13.24 ? 115 ARG   A CZ  1 
ATOM   869  N  NH1 . ARG   A 1 109 ? 18.000 -4.156  14.730 1.00 14.12 ? 115 ARG   A NH1 1 
ATOM   870  N  NH2 . ARG   A 1 109 ? 18.005 -3.001  16.711 1.00 14.46 ? 115 ARG   A NH2 1 
ATOM   871  N  N   . CYS   A 1 110 ? 12.515 -3.693  11.079 1.00 12.16 ? 116 CYS   A N   1 
ATOM   872  C  CA  . CYS   A 1 110 ? 11.616 -4.658  10.392 1.00 15.54 ? 116 CYS   A CA  1 
ATOM   873  C  C   . CYS   A 1 110 ? 12.475 -5.822  9.987  1.00 17.95 ? 116 CYS   A C   1 
ATOM   874  O  O   . CYS   A 1 110 ? 13.654 -5.923  10.356 1.00 16.84 ? 116 CYS   A O   1 
ATOM   875  C  CB  . CYS   A 1 110 ? 10.944 -3.993  9.195  1.00 15.16 ? 116 CYS   A CB  1 
ATOM   876  S  SG  . CYS   A 1 110 ? 12.113 -3.635  7.857  1.00 14.75 ? 116 CYS   A SG  1 
ATOM   877  N  N   . GLN   A 1 111 ? 11.840 -6.779  9.230  1.00 20.39 ? 117 GLN   A N   1 
ATOM   878  C  CA  . GLN   A 1 111 ? 12.611 -7.917  8.770  1.00 23.38 ? 117 GLN   A CA  1 
ATOM   879  C  C   . GLN   A 1 111 ? 13.837 -7.566  7.902  1.00 23.58 ? 117 GLN   A C   1 
ATOM   880  O  O   . GLN   A 1 111 ? 14.774 -8.355  7.831  1.00 26.30 ? 117 GLN   A O   1 
ATOM   881  C  CB  . GLN   A 1 111 ? 11.731 -8.957  8.010  1.00 28.12 ? 117 GLN   A CB  1 
ATOM   882  C  CG  . GLN   A 1 111 ? 11.204 -8.421  6.690  1.00 33.72 ? 117 GLN   A CG  1 
ATOM   883  C  CD  . GLN   A 1 111 ? 10.265 -9.363  5.970  1.00 40.10 ? 117 GLN   A CD  1 
ATOM   884  O  OE1 . GLN   A 1 111 ? 9.036  -9.242  6.064  1.00 42.11 ? 117 GLN   A OE1 1 
ATOM   885  N  NE2 . GLN   A 1 111 ? 10.826 -10.281 5.199  1.00 39.99 ? 117 GLN   A NE2 1 
ATOM   886  N  N   . HIS   A 1 112 ? 13.864 -6.378  7.294  1.00 19.31 ? 118 HIS   A N   1 
ATOM   887  C  CA  . HIS   A 1 112 ? 14.970 -5.960  6.394  1.00 18.91 ? 118 HIS   A CA  1 
ATOM   888  C  C   . HIS   A 1 112 ? 16.117 -5.184  7.070  1.00 18.30 ? 118 HIS   A C   1 
ATOM   889  O  O   . HIS   A 1 112 ? 17.163 -4.915  6.452  1.00 20.72 ? 118 HIS   A O   1 
ATOM   890  C  CB  . HIS   A 1 112 ? 14.387 -5.125  5.259  1.00 19.10 ? 118 HIS   A CB  1 
ATOM   891  C  CG  . HIS   A 1 112 ? 13.268 -5.852  4.544  1.00 20.62 ? 118 HIS   A CG  1 
ATOM   892  N  ND1 . HIS   A 1 112 ? 11.945 -5.463  4.650  1.00 20.61 ? 118 HIS   A ND1 1 
ATOM   893  C  CD2 . HIS   A 1 112 ? 13.343 -6.847  3.615  1.00 23.33 ? 118 HIS   A CD2 1 
ATOM   894  C  CE1 . HIS   A 1 112 ? 11.241 -6.305  3.893  1.00 24.34 ? 118 HIS   A CE1 1 
ATOM   895  N  NE2 . HIS   A 1 112 ? 12.048 -7.142  3.240  1.00 25.78 ? 118 HIS   A NE2 1 
ATOM   896  N  N   . GLY   A 1 113 ? 15.896 -4.718  8.314  1.00 16.13 ? 119 GLY   A N   1 
ATOM   897  C  CA  . GLY   A 1 113 ? 16.921 -3.946  8.999  1.00 14.91 ? 119 GLY   A CA  1 
ATOM   898  C  C   . GLY   A 1 113 ? 16.305 -2.763  9.762  1.00 12.38 ? 119 GLY   A C   1 
ATOM   899  O  O   . GLY   A 1 113 ? 15.106 -2.764  10.092 1.00 12.56 ? 119 GLY   A O   1 
ATOM   900  N  N   . VAL   A 1 114 ? 17.157 -1.746  10.029 1.00 11.28 ? 120 VAL   A N   1 
ATOM   901  C  CA  . VAL   A 1 114 ? 16.697 -0.554  10.787 1.00 11.14 ? 120 VAL   A CA  1 
ATOM   902  C  C   . VAL   A 1 114 ? 15.860 0.371   9.919  1.00 9.64  ? 120 VAL   A C   1 
ATOM   903  O  O   . VAL   A 1 114 ? 16.276 0.725   8.787  1.00 10.61 ? 120 VAL   A O   1 
ATOM   904  C  CB  . VAL   A 1 114 ? 17.915 0.204   11.367 1.00 10.84 ? 120 VAL   A CB  1 
ATOM   905  C  CG1 . VAL   A 1 114 ? 17.502 1.539   12.013 1.00 12.10 ? 120 VAL   A CG1 1 
ATOM   906  C  CG2 . VAL   A 1 114 ? 18.692 -0.671  12.341 1.00 12.38 ? 120 VAL   A CG2 1 
ATOM   907  N  N   . VAL   A 1 115 ? 14.714 0.776   10.414 1.00 9.25  ? 121 VAL   A N   1 
ATOM   908  C  CA  . VAL   A 1 115 ? 13.762 1.611   9.730  1.00 10.25 ? 121 VAL   A CA  1 
ATOM   909  C  C   . VAL   A 1 115 ? 13.905 3.070   10.139 1.00 9.71  ? 121 VAL   A C   1 
ATOM   910  O  O   . VAL   A 1 115 ? 13.751 3.997   9.323  1.00 10.74 ? 121 VAL   A O   1 
ATOM   911  C  CB  . VAL   A 1 115 ? 12.319 1.118   10.003 1.00 10.95 ? 121 VAL   A CB  1 
ATOM   912  C  CG1 . VAL   A 1 115 ? 11.249 2.101   9.463  1.00 13.50 ? 121 VAL   A CG1 1 
ATOM   913  C  CG2 . VAL   A 1 115 ? 12.088 -0.271  9.439  1.00 12.53 ? 121 VAL   A CG2 1 
ATOM   914  N  N   . GLY   A 1 116 ? 14.097 3.313   11.446 1.00 9.65  ? 122 GLY   A N   1 
ATOM   915  C  CA  . GLY   A 1 116 ? 14.196 4.691   11.938 1.00 10.04 ? 122 GLY   A CA  1 
ATOM   916  C  C   . GLY   A 1 116 ? 14.412 4.699   13.445 1.00 8.99  ? 122 GLY   A C   1 
ATOM   917  O  O   . GLY   A 1 116 ? 14.737 3.640   14.027 1.00 9.55  ? 122 GLY   A O   1 
ATOM   918  N  N   . ILE   A 1 117 ? 14.290 5.876   14.069 1.00 8.87  ? 123 ILE   A N   1 
ATOM   919  C  CA  . ILE   A 1 117 ? 14.498 6.019   15.519 1.00 8.65  ? 123 ILE   A CA  1 
ATOM   920  C  C   . ILE   A 1 117 ? 13.338 6.775   16.121 1.00 9.10  ? 123 ILE   A C   1 
ATOM   921  O  O   . ILE   A 1 117 ? 12.736 7.671   15.469 1.00 10.01 ? 123 ILE   A O   1 
ATOM   922  C  CB  . ILE   A 1 117 ? 15.841 6.737   15.888 1.00 10.03 ? 123 ILE   A CB  1 
ATOM   923  C  CG1 . ILE   A 1 117 ? 15.992 8.065   15.161 1.00 11.48 ? 123 ILE   A CG1 1 
ATOM   924  C  CG2 . ILE   A 1 117 ? 17.000 5.783   15.662 1.00 11.53 ? 123 ILE   A CG2 1 
ATOM   925  C  CD1 . ILE   A 1 117 ? 17.261 8.894   15.644 1.00 12.46 ? 123 ILE   A CD1 1 
ATOM   926  N  N   . VAL   A 1 118 ? 13.029 6.510   17.393 1.00 9.24  ? 124 VAL   A N   1 
ATOM   927  C  CA  . VAL   A 1 118 ? 11.999 7.268   18.113 1.00 9.65  ? 124 VAL   A CA  1 
ATOM   928  C  C   . VAL   A 1 118 ? 12.378 8.754   18.114 1.00 9.85  ? 124 VAL   A C   1 
ATOM   929  O  O   . VAL   A 1 118 ? 13.549 9.111   18.420 1.00 9.78  ? 124 VAL   A O   1 
ATOM   930  C  CB  . VAL   A 1 118 ? 11.874 6.774   19.574 1.00 10.06 ? 124 VAL   A CB  1 
ATOM   931  C  CG1 . VAL   A 1 118 ? 10.894 7.636   20.378 1.00 10.82 ? 124 VAL   A CG1 1 
ATOM   932  C  CG2 . VAL   A 1 118 ? 11.425 5.306   19.646 1.00 10.30 ? 124 VAL   A CG2 1 
ATOM   933  N  N   . SER   A 1 119 ? 11.398 9.616   17.785 1.00 9.75  ? 125 SER   A N   1 
ATOM   934  C  CA  . SER   A 1 119 ? 11.600 11.062  17.731 1.00 10.86 ? 125 SER   A CA  1 
ATOM   935  C  C   . SER   A 1 119 ? 10.498 11.833  18.445 1.00 12.19 ? 125 SER   A C   1 
ATOM   936  O  O   . SER   A 1 119 ? 10.793 12.955  18.914 1.00 14.03 ? 125 SER   A O   1 
ATOM   937  C  CB  . SER   A 1 119 ? 11.750 11.492  16.279 1.00 11.97 ? 125 SER   A CB  1 
ATOM   938  O  OG  . SER   A 1 119 ? 11.827 12.903  16.074 1.00 13.16 ? 125 SER   A OG  1 
ATOM   939  N  N   . THR   A 1 120 ? 9.248  11.306  18.528 1.00 12.20 ? 126 THR   A N   1 
ATOM   940  C  CA  . THR   A 1 120 ? 8.167  12.106  19.150 1.00 13.61 ? 126 THR   A CA  1 
ATOM   941  C  C   . THR   A 1 120 ? 7.332  11.154  20.009 1.00 15.47 ? 126 THR   A C   1 
ATOM   942  O  O   . THR   A 1 120 ? 7.435  9.914   19.907 1.00 13.95 ? 126 THR   A O   1 
ATOM   943  C  CB  . THR   A 1 120 ? 7.260  12.803  18.066 1.00 14.30 ? 126 THR   A CB  1 
ATOM   944  O  OG1 . THR   A 1 120 ? 6.448  11.797  17.417 1.00 15.10 ? 126 THR   A OG1 1 
ATOM   945  C  CG2 . THR   A 1 120 ? 8.032  13.631  17.077 1.00 14.53 ? 126 THR   A CG2 1 
ATOM   946  N  N   . GLY   A 1 121 ? 6.443  11.723  20.826 1.00 18.36 ? 127 GLY   A N   1 
ATOM   947  C  CA  . GLY   A 1 121 ? 5.521  10.904  21.589 1.00 21.12 ? 127 GLY   A CA  1 
ATOM   948  C  C   . GLY   A 1 121 ? 4.463  11.692  22.327 1.00 23.51 ? 127 GLY   A C   1 
ATOM   949  O  O   . GLY   A 1 121 ? 4.464  12.924  22.304 1.00 25.04 ? 127 GLY   A O   1 
ATOM   950  N  N   . GLY   A 1 122 ? 3.646  10.925  23.045 1.00 25.19 ? 128 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 122 ? 2.611  11.436  23.953 1.00 26.19 ? 128 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 122 ? 1.330  10.647  23.791 1.00 28.02 ? 128 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 122 ? 1.007  10.240  22.668 1.00 29.29 ? 128 GLY   A O   1 
ATOM   954  N  N   . ASN   A 1 123 ? 0.553  10.503  24.896 1.00 26.96 ? 129 ASN   A N   1 
ATOM   955  C  CA  . ASN   A 1 123 ? -0.771 9.875   25.012 1.00 26.68 ? 129 ASN   A CA  1 
ATOM   956  C  C   . ASN   A 1 123 ? -0.991 8.544   24.255 1.00 23.36 ? 129 ASN   A C   1 
ATOM   957  O  O   . ASN   A 1 123 ? -2.081 8.329   23.656 1.00 22.43 ? 129 ASN   A O   1 
ATOM   958  C  CB  . ASN   A 1 123 ? -1.880 10.889  24.632 1.00 30.22 ? 129 ASN   A CB  1 
ATOM   959  C  CG  . ASN   A 1 123 ? -1.536 12.156  23.826 1.00 37.17 ? 129 ASN   A CG  1 
ATOM   960  O  OD1 . ASN   A 1 123 ? -1.487 13.290  24.372 1.00 39.05 ? 129 ASN   A OD1 1 
ATOM   961  N  ND2 . ASN   A 1 123 ? -1.425 12.034  22.495 1.00 36.90 ? 129 ASN   A ND2 1 
ATOM   962  N  N   . GLY   A 1 124 ? -0.079 7.598   24.441 1.00 20.27 ? 130 GLY   A N   1 
ATOM   963  C  CA  . GLY   A 1 124 ? -0.204 6.308   23.826 1.00 18.47 ? 130 GLY   A CA  1 
ATOM   964  C  C   . GLY   A 1 124 ? 0.190  6.353   22.367 1.00 14.34 ? 130 GLY   A C   1 
ATOM   965  O  O   . GLY   A 1 124 ? -0.041 5.356   21.748 1.00 16.95 ? 130 GLY   A O   1 
ATOM   966  N  N   . LEU   A 1 125 ? 0.865  7.426   21.878 1.00 14.98 ? 131 LEU   A N   1 
ATOM   967  C  CA  . LEU   A 1 125 ? 1.444  7.442   20.502 1.00 14.12 ? 131 LEU   A CA  1 
ATOM   968  C  C   . LEU   A 1 125 ? 2.971  7.529   20.587 1.00 15.01 ? 131 LEU   A C   1 
ATOM   969  O  O   . LEU   A 1 125 ? 3.555  8.090   21.563 1.00 16.63 ? 131 LEU   A O   1 
ATOM   970  C  CB  . LEU   A 1 125 ? 0.953  8.641   19.692 1.00 14.93 ? 131 LEU   A CB  1 
ATOM   971  C  CG  . LEU   A 1 125 ? -0.573 8.624   19.457 1.00 15.36 ? 131 LEU   A CG  1 
ATOM   972  C  CD1 . LEU   A 1 125 ? -1.079 10.009  19.107 1.00 18.70 ? 131 LEU   A CD1 1 
ATOM   973  C  CD2 . LEU   A 1 125 ? -0.982 7.508   18.427 1.00 16.02 ? 131 LEU   A CD2 1 
ATOM   974  N  N   . VAL   A 1 126 ? 3.621  6.957   19.588 1.00 11.58 ? 132 VAL   A N   1 
ATOM   975  C  CA  . VAL   A 1 126 ? 5.089  7.080   19.424 1.00 11.60 ? 132 VAL   A CA  1 
ATOM   976  C  C   . VAL   A 1 126 ? 5.339  7.445   17.947 1.00 11.92 ? 132 VAL   A C   1 
ATOM   977  O  O   . VAL   A 1 126 ? 4.710  6.859   17.060 1.00 12.49 ? 132 VAL   A O   1 
ATOM   978  C  CB  . VAL   A 1 126 ? 5.808  5.785   19.873 1.00 11.47 ? 132 VAL   A CB  1 
ATOM   979  C  CG1 . VAL   A 1 126 ? 5.265  4.532   19.185 1.00 12.60 ? 132 VAL   A CG1 1 
ATOM   980  C  CG2 . VAL   A 1 126 ? 7.341  5.917   19.728 1.00 11.81 ? 132 VAL   A CG2 1 
ATOM   981  N  N   . GLY   A 1 127 ? 6.236  8.400   17.701 1.00 11.72 ? 133 GLY   A N   1 
ATOM   982  C  CA  . GLY   A 1 127 ? 6.586  8.785   16.332 1.00 11.78 ? 133 GLY   A CA  1 
ATOM   983  C  C   . GLY   A 1 127 ? 8.031  8.441   16.059 1.00 10.80 ? 133 GLY   A C   1 
ATOM   984  O  O   . GLY   A 1 127 ? 8.904  8.635   16.926 1.00 11.99 ? 133 GLY   A O   1 
ATOM   985  N  N   . PHE   A 1 128 ? 8.292  7.997   14.844 1.00 10.27 ? 134 PHE   A N   1 
ATOM   986  C  CA  . PHE   A 1 128 ? 9.647  7.570   14.418 1.00 10.12 ? 134 PHE   A CA  1 
ATOM   987  C  C   . PHE   A 1 128 ? 10.115 8.375   13.218 1.00 10.85 ? 134 PHE   A C   1 
ATOM   988  O  O   . PHE   A 1 128 ? 9.350  8.540   12.247 1.00 11.17 ? 134 PHE   A O   1 
ATOM   989  C  CB  . PHE   A 1 128 ? 9.610  6.068   13.981 1.00 10.17 ? 134 PHE   A CB  1 
ATOM   990  C  CG  . PHE   A 1 128 ? 8.999  5.144   15.017 1.00 10.02 ? 134 PHE   A CG  1 
ATOM   991  C  CD1 . PHE   A 1 128 ? 9.752  4.678   16.104 1.00 9.73  ? 134 PHE   A CD1 1 
ATOM   992  C  CD2 . PHE   A 1 128 ? 7.673  4.748   14.910 1.00 11.35 ? 134 PHE   A CD2 1 
ATOM   993  C  CE1 . PHE   A 1 128 ? 9.172  3.817   17.051 1.00 9.66  ? 134 PHE   A CE1 1 
ATOM   994  C  CE2 . PHE   A 1 128 ? 7.112  3.884   15.859 1.00 11.01 ? 134 PHE   A CE2 1 
ATOM   995  C  CZ  . PHE   A 1 128 ? 7.881  3.428   16.918 1.00 10.48 ? 134 PHE   A CZ  1 
ATOM   996  N  N   . ALA   A 1 129 ? 11.356 8.866   13.299 1.00 10.10 ? 135 ALA   A N   1 
ATOM   997  C  CA  . ALA   A 1 129 ? 11.986 9.518   12.152 1.00 10.59 ? 135 ALA   A CA  1 
ATOM   998  C  C   . ALA   A 1 129 ? 12.466 8.441   11.188 1.00 10.04 ? 135 ALA   A C   1 
ATOM   999  O  O   . ALA   A 1 129 ? 13.358 7.648   11.559 1.00 10.69 ? 135 ALA   A O   1 
ATOM   1000 C  CB  . ALA   A 1 129 ? 13.124 10.389  12.652 1.00 11.30 ? 135 ALA   A CB  1 
ATOM   1001 N  N   . ASP   A 1 130 ? 11.926 8.392   9.965  1.00 10.58 ? 136 ASP   A N   1 
ATOM   1002 C  CA  . ASP   A 1 130 ? 12.355 7.403   8.980  1.00 11.12 ? 136 ASP   A CA  1 
ATOM   1003 C  C   . ASP   A 1 130 ? 13.766 7.702   8.483  1.00 11.20 ? 136 ASP   A C   1 
ATOM   1004 O  O   . ASP   A 1 130 ? 14.148 8.872   8.328  1.00 12.35 ? 136 ASP   A O   1 
ATOM   1005 C  CB  . ASP   A 1 130 ? 11.388 7.452   7.766  1.00 13.49 ? 136 ASP   A CB  1 
ATOM   1006 C  CG  . ASP   A 1 130 ? 11.673 6.451   6.705  1.00 16.45 ? 136 ASP   A CG  1 
ATOM   1007 O  OD1 . ASP   A 1 130 ? 11.804 5.258   7.022  1.00 16.09 ? 136 ASP   A OD1 1 
ATOM   1008 O  OD2 . ASP   A 1 130 ? 11.912 6.888   5.530  1.00 23.30 ? 136 ASP   A OD2 1 
ATOM   1009 N  N   . VAL   A 1 131 ? 14.536 6.631   8.196  1.00 10.36 ? 137 VAL   A N   1 
ATOM   1010 C  CA  . VAL   A 1 131 ? 15.848 6.764   7.558  1.00 10.38 ? 137 VAL   A CA  1 
ATOM   1011 C  C   . VAL   A 1 131 ? 15.963 5.954   6.271  1.00 11.01 ? 137 VAL   A C   1 
ATOM   1012 O  O   . VAL   A 1 131 ? 17.046 5.961   5.644  1.00 10.75 ? 137 VAL   A O   1 
ATOM   1013 C  CB  . VAL   A 1 131 ? 17.028 6.433   8.507  1.00 10.53 ? 137 VAL   A CB  1 
ATOM   1014 C  CG1 . VAL   A 1 131 ? 17.053 7.350   9.737  1.00 12.03 ? 137 VAL   A CG1 1 
ATOM   1015 C  CG2 . VAL   A 1 131 ? 17.054 4.961   8.906  1.00 11.82 ? 137 VAL   A CG2 1 
ATOM   1016 N  N   . ARG   A 1 132 ? 14.888 5.271   5.836  1.00 11.13 ? 138 ARG   A N   1 
ATOM   1017 C  CA  . ARG   A 1 132 ? 14.977 4.356   4.695  1.00 11.49 ? 138 ARG   A CA  1 
ATOM   1018 C  C   . ARG   A 1 132 ? 15.247 5.043   3.375  1.00 12.77 ? 138 ARG   A C   1 
ATOM   1019 O  O   . ARG   A 1 132 ? 15.713 4.389   2.414  1.00 13.93 ? 138 ARG   A O   1 
ATOM   1020 C  CB  . ARG   A 1 132 ? 13.734 3.482   4.592  1.00 11.97 ? 138 ARG   A CB  1 
ATOM   1021 C  CG  . ARG   A 1 132 ? 13.607 2.521   5.798  1.00 11.43 ? 138 ARG   A CG  1 
ATOM   1022 C  CD  . ARG   A 1 132 ? 12.311 1.736   5.661  1.00 13.01 ? 138 ARG   A CD  1 
ATOM   1023 N  NE  . ARG   A 1 132 ? 11.170 2.644   5.900  1.00 12.98 ? 138 ARG   A NE  1 
ATOM   1024 C  CZ  . ARG   A 1 132 ? 9.901  2.259   5.987  1.00 15.51 ? 138 ARG   A CZ  1 
ATOM   1025 N  NH1 . ARG   A 1 132 ? 9.565  0.999   5.722  1.00 15.35 ? 138 ARG   A NH1 1 
ATOM   1026 N  NH2 . ARG   A 1 132 ? 8.957  3.146   6.302  1.00 16.35 ? 138 ARG   A NH2 1 
ATOM   1027 N  N   . ASP   A 1 133 ? 14.936 6.361   3.254  1.00 12.69 ? 139 ASP   A N   1 
ATOM   1028 C  CA  . ASP   A 1 133 ? 15.210 7.077   2.011  1.00 13.23 ? 139 ASP   A CA  1 
ATOM   1029 C  C   . ASP   A 1 133 ? 16.650 7.587   1.924  1.00 13.48 ? 139 ASP   A C   1 
ATOM   1030 O  O   . ASP   A 1 133 ? 17.057 8.080   0.855  1.00 14.84 ? 139 ASP   A O   1 
ATOM   1031 C  CB  . ASP   A 1 133 ? 14.215 8.252   1.874  1.00 15.47 ? 139 ASP   A CB  1 
ATOM   1032 C  CG  . ASP   A 1 133 ? 14.444 9.306   2.964  1.00 18.36 ? 139 ASP   A CG  1 
ATOM   1033 O  OD1 . ASP   A 1 133 ? 14.571 8.935   4.165  1.00 17.36 ? 139 ASP   A OD1 1 
ATOM   1034 O  OD2 . ASP   A 1 133 ? 14.484 10.509  2.641  1.00 20.26 ? 139 ASP   A OD2 1 
ATOM   1035 N  N   . LEU   A 1 134 ? 17.451 7.509   3.009  1.00 12.27 ? 140 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 134 ? 18.816 8.064   3.047  1.00 12.21 ? 140 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 134 ? 19.779 7.023   2.503  1.00 12.18 ? 140 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 134 ? 20.481 6.318   3.244  1.00 12.57 ? 140 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 134 ? 19.167 8.468   4.501  1.00 12.15 ? 140 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 134 ? 18.207 9.492   5.140  1.00 13.42 ? 140 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 134 ? 18.594 9.750   6.593  1.00 14.13 ? 140 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 134 ? 18.201 10.782  4.369  1.00 15.93 ? 140 LEU   A CD2 1 
ATOM   1043 N  N   . LEU   A 1 135 ? 19.773 6.870   1.171  1.00 12.05 ? 141 LEU   A N   1 
ATOM   1044 C  CA  . LEU   A 1 135 ? 20.519 5.782   0.538  1.00 12.78 ? 141 LEU   A CA  1 
ATOM   1045 C  C   . LEU   A 1 135 ? 22.012 5.890   0.718  1.00 12.88 ? 141 LEU   A C   1 
ATOM   1046 O  O   . LEU   A 1 135 ? 22.730 4.861   0.767  1.00 14.13 ? 141 LEU   A O   1 
ATOM   1047 C  CB  . LEU   A 1 135 ? 20.159 5.660   -0.982 1.00 14.07 ? 141 LEU   A CB  1 
ATOM   1048 C  CG  . LEU   A 1 135 ? 18.656 5.656   -1.279 1.00 15.92 ? 141 LEU   A CG  1 
ATOM   1049 C  CD1 . LEU   A 1 135 ? 18.440 5.375   -2.771 1.00 17.69 ? 141 LEU   A CD1 1 
ATOM   1050 C  CD2 . LEU   A 1 135 ? 17.881 4.597   -0.468 1.00 17.87 ? 141 LEU   A CD2 1 
ATOM   1051 N  N   . TRP   A 1 136 ? 22.502 7.132   0.875  1.00 11.86 ? 142 TRP   A N   1 
ATOM   1052 C  CA  . TRP   A 1 136 ? 23.921 7.370   1.056  1.00 12.77 ? 142 TRP   A CA  1 
ATOM   1053 C  C   . TRP   A 1 136 ? 24.469 6.778   2.348  1.00 13.23 ? 142 TRP   A C   1 
ATOM   1054 O  O   . TRP   A 1 136 ? 25.699 6.654   2.487  1.00 14.30 ? 142 TRP   A O   1 
ATOM   1055 C  CB  . TRP   A 1 136 ? 24.224 8.884   0.935  1.00 13.55 ? 142 TRP   A CB  1 
ATOM   1056 C  CG  . TRP   A 1 136 ? 23.411 9.716   1.880  1.00 12.77 ? 142 TRP   A CG  1 
ATOM   1057 C  CD1 . TRP   A 1 136 ? 22.276 10.394  1.577  1.00 13.10 ? 142 TRP   A CD1 1 
ATOM   1058 C  CD2 . TRP   A 1 136 ? 23.738 10.050  3.240  1.00 12.97 ? 142 TRP   A CD2 1 
ATOM   1059 N  NE1 . TRP   A 1 136 ? 21.822 11.073  2.699  1.00 14.50 ? 142 TRP   A NE1 1 
ATOM   1060 C  CE2 . TRP   A 1 136 ? 22.729 10.904  3.712  1.00 13.60 ? 142 TRP   A CE2 1 
ATOM   1061 C  CE3 . TRP   A 1 136 ? 24.811 9.742   4.086  1.00 14.04 ? 142 TRP   A CE3 1 
ATOM   1062 C  CZ2 . TRP   A 1 136 ? 22.741 11.401  5.031  1.00 15.11 ? 142 TRP   A CZ2 1 
ATOM   1063 C  CZ3 . TRP   A 1 136 ? 24.841 10.263  5.367  1.00 15.67 ? 142 TRP   A CZ3 1 
ATOM   1064 C  CH2 . TRP   A 1 136 ? 23.832 11.100  5.809  1.00 15.34 ? 142 TRP   A CH2 1 
ATOM   1065 N  N   . LEU   A 1 137 ? 23.614 6.442   3.342  1.00 11.97 ? 143 LEU   A N   1 
ATOM   1066 C  CA  . LEU   A 1 137 ? 24.133 5.777   4.553  1.00 13.95 ? 143 LEU   A CA  1 
ATOM   1067 C  C   . LEU   A 1 137 ? 24.816 4.456   4.244  1.00 15.38 ? 143 LEU   A C   1 
ATOM   1068 O  O   . LEU   A 1 137 ? 25.650 4.000   5.047  1.00 16.54 ? 143 LEU   A O   1 
ATOM   1069 C  CB  . LEU   A 1 137 ? 23.002 5.525   5.554  1.00 13.31 ? 143 LEU   A CB  1 
ATOM   1070 C  CG  . LEU   A 1 137 ? 22.446 6.767   6.221  1.00 12.68 ? 143 LEU   A CG  1 
ATOM   1071 C  CD1 . LEU   A 1 137 ? 21.177 6.413   7.010  1.00 14.66 ? 143 LEU   A CD1 1 
ATOM   1072 C  CD2 . LEU   A 1 137 ? 23.516 7.396   7.187  1.00 13.63 ? 143 LEU   A CD2 1 
ATOM   1073 N  N   . ASP   A 1 138 ? 24.500 3.842   3.069  1.00 16.82 ? 144 ASP   A N   1 
ATOM   1074 C  CA  . ASP   A 1 138 ? 25.060 2.521   2.718  1.00 18.70 ? 144 ASP   A CA  1 
ATOM   1075 C  C   . ASP   A 1 138 ? 26.395 2.586   2.008  1.00 22.72 ? 144 ASP   A C   1 
ATOM   1076 O  O   . ASP   A 1 138 ? 26.940 1.532   1.642  1.00 24.79 ? 144 ASP   A O   1 
ATOM   1077 C  CB  . ASP   A 1 138 ? 24.082 1.775   1.764  1.00 19.09 ? 144 ASP   A CB  1 
ATOM   1078 C  CG  . ASP   A 1 138 ? 22.726 1.429   2.339  1.00 21.68 ? 144 ASP   A CG  1 
ATOM   1079 O  OD1 . ASP   A 1 138 ? 22.559 1.529   3.583  1.00 23.26 ? 144 ASP   A OD1 1 
ATOM   1080 O  OD2 . ASP   A 1 138 ? 21.808 1.066   1.558  1.00 28.50 ? 144 ASP   A OD2 1 
ATOM   1081 N  N   . GLU   A 1 139 ? 26.950 3.788   1.771  1.00 23.49 ? 145 GLU   A N   1 
ATOM   1082 C  CA  . GLU   A 1 139 ? 28.224 3.900   1.042  1.00 27.32 ? 145 GLU   A CA  1 
ATOM   1083 C  C   . GLU   A 1 139 ? 29.189 4.871   1.718  1.00 28.57 ? 145 GLU   A C   1 
ATOM   1084 O  O   . GLU   A 1 139 ? 28.780 5.676   2.549  1.00 28.21 ? 145 GLU   A O   1 
ATOM   1085 C  CB  . GLU   A 1 139 ? 27.928 4.319   -0.396 1.00 32.60 ? 145 GLU   A CB  1 
ATOM   1086 C  CG  . GLU   A 1 139 ? 27.195 5.643   -0.466 1.00 40.89 ? 145 GLU   A CG  1 
ATOM   1087 C  CD  . GLU   A 1 139 ? 26.399 5.922   -1.726 1.00 49.03 ? 145 GLU   A CD  1 
ATOM   1088 O  OE1 . GLU   A 1 139 ? 26.078 7.111   -1.967 1.00 49.00 ? 145 GLU   A OE1 1 
ATOM   1089 O  OE2 . GLU   A 1 139 ? 26.094 4.960   -2.470 1.00 53.20 ? 145 GLU   A OE2 1 
ATOM   1090 N  N   . GLU   A 1 140 ? 30.491 4.765   1.410  1.00 30.80 ? 146 GLU   A N   1 
ATOM   1091 C  CA  . GLU   A 1 140 ? 31.508 5.630   2.025  1.00 33.49 ? 146 GLU   A CA  1 
ATOM   1092 C  C   . GLU   A 1 140 ? 31.329 7.095   1.645  1.00 35.68 ? 146 GLU   A C   1 
ATOM   1093 O  O   . GLU   A 1 140 ? 30.836 7.408   0.553  1.00 36.98 ? 146 GLU   A O   1 
ATOM   1094 C  CB  . GLU   A 1 140 ? 32.933 5.147   1.676  1.00 37.38 ? 146 GLU   A CB  1 
ATOM   1095 C  CG  . GLU   A 1 140 ? 33.313 3.877   2.421  1.00 46.17 ? 146 GLU   A CG  1 
ATOM   1096 C  CD  . GLU   A 1 140 ? 34.797 3.724   2.693  1.00 56.16 ? 146 GLU   A CD  1 
ATOM   1097 O  OE1 . GLU   A 1 140 ? 35.157 3.388   3.846  1.00 57.75 ? 146 GLU   A OE1 1 
ATOM   1098 O  OE2 . GLU   A 1 140 ? 35.600 3.947   1.757  1.00 59.18 ? 146 GLU   A OE2 1 
ATOM   1099 N  N   . SER   B 1 1   ? 21.859 -21.314 7.595  1.00 16.67 ? 7   SER   C N   1 
ATOM   1100 C  CA  . SER   B 1 1   ? 20.733 -21.105 8.531  1.00 15.72 ? 7   SER   C CA  1 
ATOM   1101 C  C   . SER   B 1 1   ? 20.707 -22.213 9.597  1.00 15.50 ? 7   SER   C C   1 
ATOM   1102 O  O   . SER   B 1 1   ? 21.387 -23.245 9.456  1.00 17.30 ? 7   SER   C O   1 
ATOM   1103 C  CB  . SER   B 1 1   ? 19.417 -21.133 7.750  1.00 19.30 ? 7   SER   C CB  1 
ATOM   1104 O  OG  . SER   B 1 1   ? 19.269 -22.408 7.149  1.00 24.14 ? 7   SER   C OG  1 
ATOM   1105 N  N   . GLY   B 1 2   ? 19.949 -21.995 10.678 1.00 15.60 ? 8   GLY   C N   1 
ATOM   1106 C  CA  . GLY   B 1 2   ? 19.769 -23.001 11.722 1.00 14.75 ? 8   GLY   C CA  1 
ATOM   1107 C  C   . GLY   B 1 2   ? 19.497 -22.374 13.073 1.00 13.44 ? 8   GLY   C C   1 
ATOM   1108 O  O   . GLY   B 1 2   ? 19.882 -21.240 13.321 1.00 13.79 ? 8   GLY   C O   1 
ATOM   1109 N  N   . ALA   B 1 3   ? 18.844 -23.108 13.951 1.00 12.37 ? 9   ALA   C N   1 
ATOM   1110 C  CA  . ALA   B 1 3   ? 18.518 -22.621 15.290 1.00 12.76 ? 9   ALA   C CA  1 
ATOM   1111 C  C   . ALA   B 1 3   ? 18.648 -23.743 16.314 1.00 11.83 ? 9   ALA   C C   1 
ATOM   1112 O  O   . ALA   B 1 3   ? 18.713 -24.942 15.938 1.00 12.95 ? 9   ALA   C O   1 
ATOM   1113 C  CB  . ALA   B 1 3   ? 17.079 -22.091 15.301 1.00 15.62 ? 9   ALA   C CB  1 
ATOM   1114 N  N   . ILE   B 1 4   ? 18.670 -23.367 17.594 1.00 11.93 ? 10  ILE   C N   1 
ATOM   1115 C  CA  . ILE   B 1 4   ? 18.583 -24.295 18.735 1.00 11.76 ? 10  ILE   C CA  1 
ATOM   1116 C  C   . ILE   B 1 4   ? 17.193 -24.096 19.332 1.00 11.62 ? 10  ILE   C C   1 
ATOM   1117 O  O   . ILE   B 1 4   ? 16.753 -22.948 19.527 1.00 12.54 ? 10  ILE   C O   1 
ATOM   1118 C  CB  . ILE   B 1 4   ? 19.629 -23.974 19.800 1.00 11.72 ? 10  ILE   C CB  1 
ATOM   1119 C  CG1 . ILE   B 1 4   ? 21.056 -23.838 19.199 1.00 13.33 ? 10  ILE   C CG1 1 
ATOM   1120 C  CG2 . ILE   B 1 4   ? 19.591 -25.071 20.896 1.00 13.87 ? 10  ILE   C CG2 1 
ATOM   1121 C  CD1 . ILE   B 1 4   ? 22.022 -23.237 20.239 1.00 13.68 ? 10  ILE   C CD1 1 
ATOM   1122 N  N   . TYR   B 1 5   ? 16.488 -25.197 19.629 1.00 11.66 ? 11  TYR   C N   1 
ATOM   1123 C  CA  . TYR   B 1 5   ? 15.145 -25.161 20.218 1.00 12.88 ? 11  TYR   C CA  1 
ATOM   1124 C  C   . TYR   B 1 5   ? 15.202 -25.833 21.586 1.00 12.99 ? 11  TYR   C C   1 
ATOM   1125 O  O   . TYR   B 1 5   ? 15.285 -27.066 21.661 1.00 14.85 ? 11  TYR   C O   1 
ATOM   1126 C  CB  . TYR   B 1 5   ? 14.092 -25.856 19.307 1.00 13.69 ? 11  TYR   C CB  1 
ATOM   1127 C  CG  . TYR   B 1 5   ? 13.895 -25.098 18.007 1.00 14.00 ? 11  TYR   C CG  1 
ATOM   1128 C  CD1 . TYR   B 1 5   ? 13.060 -23.981 17.941 1.00 13.68 ? 11  TYR   C CD1 1 
ATOM   1129 C  CD2 . TYR   B 1 5   ? 14.609 -25.439 16.865 1.00 14.83 ? 11  TYR   C CD2 1 
ATOM   1130 C  CE1 . TYR   B 1 5   ? 12.930 -23.254 16.762 1.00 15.49 ? 11  TYR   C CE1 1 
ATOM   1131 C  CE2 . TYR   B 1 5   ? 14.485 -24.719 15.685 1.00 16.65 ? 11  TYR   C CE2 1 
ATOM   1132 C  CZ  . TYR   B 1 5   ? 13.636 -23.639 15.637 1.00 16.35 ? 11  TYR   C CZ  1 
ATOM   1133 O  OH  . TYR   B 1 5   ? 13.560 -22.910 14.476 1.00 18.47 ? 11  TYR   C OH  1 
ATOM   1134 N  N   . VAL   B 1 6   ? 15.254 -25.084 22.673 1.00 13.47 ? 12  VAL   C N   1 
ATOM   1135 C  CA  . VAL   B 1 6   ? 15.338 -25.608 24.045 1.00 14.60 ? 12  VAL   C CA  1 
ATOM   1136 C  C   . VAL   B 1 6   ? 14.205 -24.986 24.881 1.00 14.77 ? 12  VAL   C C   1 
ATOM   1137 O  O   . VAL   B 1 6   ? 14.012 -23.772 24.865 1.00 13.92 ? 12  VAL   C O   1 
ATOM   1138 C  CB  . VAL   B 1 6   ? 16.747 -25.345 24.647 1.00 15.52 ? 12  VAL   C CB  1 
ATOM   1139 C  CG1 . VAL   B 1 6   ? 17.115 -23.857 24.557 1.00 15.84 ? 12  VAL   C CG1 1 
ATOM   1140 C  CG2 . VAL   B 1 6   ? 16.798 -25.835 26.080 1.00 16.63 ? 12  VAL   C CG2 1 
ATOM   1141 N  N   . GLY   B 1 7   ? 13.393 -25.809 25.588 1.00 15.74 ? 13  GLY   C N   1 
ATOM   1142 C  CA  . GLY   B 1 7   ? 12.284 -25.254 26.363 1.00 15.91 ? 13  GLY   C CA  1 
ATOM   1143 C  C   . GLY   B 1 7   ? 11.351 -24.429 25.484 1.00 16.27 ? 13  GLY   C C   1 
ATOM   1144 O  O   . GLY   B 1 7   ? 11.059 -24.846 24.352 1.00 17.48 ? 13  GLY   C O   1 
ATOM   1145 N  N   . ASN   B 1 8   ? 11.008 -23.239 25.917 1.00 16.03 ? 14  ASN   C N   1 
ATOM   1146 C  CA  . ASN   B 1 8   ? 10.210 -22.350 25.073 1.00 16.31 ? 14  ASN   C CA  1 
ATOM   1147 C  C   . ASN   B 1 8   ? 11.088 -21.242 24.498 1.00 15.13 ? 14  ASN   C C   1 
ATOM   1148 O  O   . ASN   B 1 8   ? 10.618 -20.111 24.334 1.00 15.23 ? 14  ASN   C O   1 
ATOM   1149 C  CB  . ASN   B 1 8   ? 8.955  -21.767 25.797 1.00 18.21 ? 14  ASN   C CB  1 
ATOM   1150 C  CG  . ASN   B 1 8   ? 7.867  -22.825 25.959 1.00 25.57 ? 14  ASN   C CG  1 
ATOM   1151 O  OD1 . ASN   B 1 8   ? 6.993  -22.987 25.100 1.00 28.08 ? 14  ASN   C OD1 1 
ATOM   1152 N  ND2 . ASN   B 1 8   ? 7.976  -23.616 27.002 1.00 27.40 ? 14  ASN   C ND2 1 
ATOM   1153 N  N   . TYR   B 1 9   ? 12.295 -21.600 24.089 1.00 12.85 ? 15  TYR   C N   1 
ATOM   1154 C  CA  . TYR   B 1 9   ? 13.263 -20.641 23.494 1.00 12.05 ? 15  TYR   C CA  1 
ATOM   1155 C  C   . TYR   B 1 9   ? 13.718 -21.117 22.125 1.00 12.25 ? 15  TYR   C C   1 
ATOM   1156 O  O   . TYR   B 1 9   ? 13.904 -22.337 21.899 1.00 13.20 ? 15  TYR   C O   1 
ATOM   1157 C  CB  . TYR   B 1 9   ? 14.504 -20.499 24.410 1.00 13.24 ? 15  TYR   C CB  1 
ATOM   1158 C  CG  . TYR   B 1 9   ? 14.194 -19.988 25.815 1.00 14.91 ? 15  TYR   C CG  1 
ATOM   1159 C  CD1 . TYR   B 1 9   ? 13.644 -18.727 26.012 1.00 17.48 ? 15  TYR   C CD1 1 
ATOM   1160 C  CD2 . TYR   B 1 9   ? 14.499 -20.751 26.935 1.00 17.14 ? 15  TYR   C CD2 1 
ATOM   1161 C  CE1 . TYR   B 1 9   ? 13.360 -18.263 27.296 1.00 20.36 ? 15  TYR   C CE1 1 
ATOM   1162 C  CE2 . TYR   B 1 9   ? 14.251 -20.281 28.224 1.00 20.02 ? 15  TYR   C CE2 1 
ATOM   1163 C  CZ  . TYR   B 1 9   ? 13.714 -19.028 28.391 1.00 22.11 ? 15  TYR   C CZ  1 
ATOM   1164 O  OH  . TYR   B 1 9   ? 13.455 -18.543 29.662 1.00 27.81 ? 15  TYR   C OH  1 
ATOM   1165 N  N   . ARG   B 1 10  ? 13.977 -20.171 21.240 1.00 11.69 ? 16  ARG   C N   1 
ATOM   1166 C  CA  . ARG   B 1 10  ? 14.602 -20.397 19.921 1.00 11.58 ? 16  ARG   C CA  1 
ATOM   1167 C  C   . ARG   B 1 10  ? 15.860 -19.521 19.918 1.00 11.42 ? 16  ARG   C C   1 
ATOM   1168 O  O   . ARG   B 1 10  ? 15.778 -18.297 20.124 1.00 12.23 ? 16  ARG   C O   1 
ATOM   1169 C  CB  . ARG   B 1 10  ? 13.628 -19.968 18.798 1.00 12.97 ? 16  ARG   C CB  1 
ATOM   1170 C  CG  . ARG   B 1 10  ? 14.258 -19.804 17.401 1.00 13.96 ? 16  ARG   C CG  1 
ATOM   1171 C  CD  . ARG   B 1 10  ? 13.178 -19.513 16.348 1.00 13.77 ? 16  ARG   C CD  1 
ATOM   1172 N  NE  . ARG   B 1 10  ? 13.609 -18.555 15.324 1.00 14.32 ? 16  ARG   C NE  1 
ATOM   1173 C  CZ  . ARG   B 1 10  ? 14.142 -18.857 14.133 1.00 15.97 ? 16  ARG   C CZ  1 
ATOM   1174 N  NH1 . ARG   B 1 10  ? 14.398 -20.132 13.803 1.00 17.32 ? 16  ARG   C NH1 1 
ATOM   1175 N  NH2 . ARG   B 1 10  ? 14.477 -17.889 13.284 1.00 17.30 ? 16  ARG   C NH2 1 
ATOM   1176 N  N   . VAL   B 1 11  ? 17.036 -20.121 19.661 1.00 11.15 ? 17  VAL   C N   1 
ATOM   1177 C  CA  . VAL   B 1 11  ? 18.326 -19.410 19.642 1.00 10.22 ? 17  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 11  ? 18.792 -19.353 18.215 1.00 11.07 ? 17  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 11  ? 18.973 -20.426 17.569 1.00 11.54 ? 17  VAL   C O   1 
ATOM   1180 C  CB  . VAL   B 1 11  ? 19.389 -20.149 20.512 1.00 11.34 ? 17  VAL   C CB  1 
ATOM   1181 C  CG1 . VAL   B 1 11  ? 20.657 -19.298 20.585 1.00 13.76 ? 17  VAL   C CG1 1 
ATOM   1182 C  CG2 . VAL   B 1 11  ? 18.856 -20.482 21.922 1.00 13.00 ? 17  VAL   C CG2 1 
ATOM   1183 N  N   . VAL   B 1 12  ? 19.046 -18.136 17.674 1.00 10.52 ? 18  VAL   C N   1 
ATOM   1184 C  CA  A VAL   B 1 12  ? 19.506 -17.963 16.291 0.50 10.53 ? 18  VAL   C CA  1 
ATOM   1185 C  CA  B VAL   B 1 12  ? 19.459 -17.992 16.284 0.50 12.22 ? 18  VAL   C CA  1 
ATOM   1186 C  C   . VAL   B 1 12  ? 20.629 -16.974 16.218 1.00 11.23 ? 18  VAL   C C   1 
ATOM   1187 O  O   . VAL   B 1 12  ? 20.885 -16.215 17.191 1.00 11.59 ? 18  VAL   C O   1 
ATOM   1188 C  CB  A VAL   B 1 12  ? 18.343 -17.439 15.378 0.50 10.71 ? 18  VAL   C CB  1 
ATOM   1189 C  CB  B VAL   B 1 12  ? 18.175 -17.451 15.535 0.50 15.74 ? 18  VAL   C CB  1 
ATOM   1190 C  CG1 A VAL   B 1 12  ? 17.369 -18.567 15.076 0.50 11.33 ? 18  VAL   C CG1 1 
ATOM   1191 C  CG1 B VAL   B 1 12  ? 18.390 -17.266 14.052 0.50 16.22 ? 18  VAL   C CG1 1 
ATOM   1192 C  CG2 A VAL   B 1 12  ? 17.686 -16.131 15.917 0.50 8.23  ? 18  VAL   C CG2 1 
ATOM   1193 C  CG2 B VAL   B 1 12  ? 16.990 -18.377 15.742 0.50 18.89 ? 18  VAL   C CG2 1 
ATOM   1194 N  N   . ASN   B 1 13  ? 21.319 -16.929 15.067 1.00 10.68 ? 19  ASN   C N   1 
ATOM   1195 C  CA  . ASN   B 1 13  ? 22.311 -15.879 14.862 1.00 10.27 ? 19  ASN   C CA  1 
ATOM   1196 C  C   . ASN   B 1 13  ? 21.502 -14.530 14.808 1.00 11.41 ? 19  ASN   C C   1 
ATOM   1197 O  O   . ASN   B 1 13  ? 20.487 -14.433 14.104 1.00 10.85 ? 19  ASN   C O   1 
ATOM   1198 C  CB  . ASN   B 1 13  ? 23.001 -16.017 13.487 1.00 11.13 ? 19  ASN   C CB  1 
ATOM   1199 C  CG  . ASN   B 1 13  ? 23.863 -17.274 13.404 1.00 10.85 ? 19  ASN   C CG  1 
ATOM   1200 O  OD1 . ASN   B 1 13  ? 23.388 -18.347 12.990 1.00 12.11 ? 19  ASN   C OD1 1 
ATOM   1201 N  ND2 . ASN   B 1 13  ? 25.104 -17.179 13.879 1.00 11.96 ? 19  ASN   C ND2 1 
ATOM   1202 N  N   . ARG   B 1 14  ? 22.014 -13.501 15.505 1.00 10.85 ? 20  ARG   C N   1 
ATOM   1203 C  CA  . ARG   B 1 14  ? 21.278 -12.206 15.523 1.00 10.92 ? 20  ARG   C CA  1 
ATOM   1204 C  C   . ARG   B 1 14  ? 21.135 -11.667 14.091 1.00 11.75 ? 20  ARG   C C   1 
ATOM   1205 O  O   . ARG   B 1 14  ? 20.056 -11.135 13.748 1.00 12.51 ? 20  ARG   C O   1 
ATOM   1206 C  CB  . ARG   B 1 14  ? 22.038 -11.215 16.397 1.00 11.01 ? 20  ARG   C CB  1 
ATOM   1207 C  CG  . ARG   B 1 14  ? 21.219 -9.884  16.642 1.00 11.69 ? 20  ARG   C CG  1 
ATOM   1208 C  CD  . ARG   B 1 14  ? 22.086 -8.930  17.418 1.00 12.20 ? 20  ARG   C CD  1 
ATOM   1209 N  NE  . ARG   B 1 14  ? 21.412 -7.673  17.839 1.00 13.10 ? 20  ARG   C NE  1 
ATOM   1210 C  CZ  . ARG   B 1 14  ? 21.340 -6.568  17.107 1.00 12.79 ? 20  ARG   C CZ  1 
ATOM   1211 N  NH1 . ARG   B 1 14  ? 21.718 -6.579  15.836 1.00 14.36 ? 20  ARG   C NH1 1 
ATOM   1212 N  NH2 . ARG   B 1 14  ? 20.817 -5.466  17.620 1.00 13.89 ? 20  ARG   C NH2 1 
ATOM   1213 N  N   . HIS   B 1 15  ? 22.145 -11.877 13.233 1.00 11.75 ? 21  HIS   C N   1 
ATOM   1214 C  CA  . HIS   B 1 15  ? 22.046 -11.326 11.873 1.00 13.15 ? 21  HIS   C CA  1 
ATOM   1215 C  C   . HIS   B 1 15  ? 21.030 -12.043 10.987 1.00 13.05 ? 21  HIS   C C   1 
ATOM   1216 O  O   . HIS   B 1 15  ? 20.753 -11.524 9.910  1.00 14.86 ? 21  HIS   C O   1 
ATOM   1217 C  CB  . HIS   B 1 15  ? 23.440 -11.227 11.196 1.00 13.63 ? 21  HIS   C CB  1 
ATOM   1218 C  CG  . HIS   B 1 15  ? 24.025 -12.545 10.759 1.00 12.32 ? 21  HIS   C CG  1 
ATOM   1219 N  ND1 . HIS   B 1 15  ? 24.754 -13.374 11.629 1.00 12.52 ? 21  HIS   C ND1 1 
ATOM   1220 C  CD2 . HIS   B 1 15  ? 24.042 -13.096 9.522  1.00 13.06 ? 21  HIS   C CD2 1 
ATOM   1221 C  CE1 . HIS   B 1 15  ? 25.151 -14.431 10.889 1.00 13.74 ? 21  HIS   C CE1 1 
ATOM   1222 N  NE2 . HIS   B 1 15  ? 24.733 -14.295 9.617  1.00 13.04 ? 21  HIS   C NE2 1 
ATOM   1223 N  N   . LEU   B 1 16  ? 20.516 -13.205 11.405 1.00 11.89 ? 22  LEU   C N   1 
ATOM   1224 C  CA  . LEU   B 1 16  ? 19.498 -13.967 10.659 1.00 13.20 ? 22  LEU   C CA  1 
ATOM   1225 C  C   . LEU   B 1 16  ? 18.119 -13.900 11.341 1.00 13.31 ? 22  LEU   C C   1 
ATOM   1226 O  O   . LEU   B 1 16  ? 17.190 -14.638 10.921 1.00 14.19 ? 22  LEU   C O   1 
ATOM   1227 C  CB  . LEU   B 1 16  ? 19.961 -15.424 10.486 1.00 13.08 ? 22  LEU   C CB  1 
ATOM   1228 C  CG  . LEU   B 1 16  ? 21.254 -15.558 9.672  1.00 13.82 ? 22  LEU   C CG  1 
ATOM   1229 C  CD1 . LEU   B 1 16  ? 21.715 -17.026 9.600  1.00 14.35 ? 22  LEU   C CD1 1 
ATOM   1230 C  CD2 . LEU   B 1 16  ? 21.146 -14.930 8.278  1.00 14.55 ? 22  LEU   C CD2 1 
ATOM   1231 N  N   . ALA   B 1 17  ? 17.972 -13.138 12.450 1.00 13.72 ? 23  ALA   C N   1 
ATOM   1232 C  CA  . ALA   B 1 17  ? 16.691 -13.088 13.180 1.00 13.49 ? 23  ALA   C CA  1 
ATOM   1233 C  C   . ALA   B 1 17  ? 15.571 -12.563 12.303 1.00 14.98 ? 23  ALA   C C   1 
ATOM   1234 O  O   . ALA   B 1 17  ? 15.795 -11.637 11.508 1.00 15.36 ? 23  ALA   C O   1 
ATOM   1235 C  CB  . ALA   B 1 17  ? 16.833 -12.204 14.421 1.00 15.04 ? 23  ALA   C CB  1 
ATOM   1236 N  N   . THR   B 1 18  ? 14.378 -13.133 12.470 1.00 15.61 ? 24  THR   C N   1 
ATOM   1237 C  CA  . THR   B 1 18  ? 13.221 -12.708 11.670 1.00 15.86 ? 24  THR   C CA  1 
ATOM   1238 C  C   . THR   B 1 18  ? 12.411 -11.625 12.437 1.00 14.92 ? 24  THR   C C   1 
ATOM   1239 O  O   . THR   B 1 18  ? 12.640 -11.316 13.608 1.00 15.39 ? 24  THR   C O   1 
ATOM   1240 C  CB  . THR   B 1 18  ? 12.295 -13.932 11.417 1.00 16.98 ? 24  THR   C CB  1 
ATOM   1241 O  OG1 . THR   B 1 18  ? 11.773 -14.347 12.665 1.00 17.30 ? 24  THR   C OG1 1 
ATOM   1242 C  CG2 . THR   B 1 18  ? 13.021 -15.109 10.710 1.00 18.37 ? 24  THR   C CG2 1 
ATOM   1243 N  N   . HIS   B 1 19  ? 11.372 -11.052 11.754 1.00 16.21 ? 25  HIS   C N   1 
ATOM   1244 C  CA  . HIS   B 1 19  ? 10.452 -10.120 12.447 1.00 17.10 ? 25  HIS   C CA  1 
ATOM   1245 C  C   . HIS   B 1 19  ? 9.763  -10.854 13.585 1.00 15.15 ? 25  HIS   C C   1 
ATOM   1246 O  O   . HIS   B 1 19  ? 9.674  -10.293 14.678 1.00 16.89 ? 25  HIS   C O   1 
ATOM   1247 C  CB  . HIS   B 1 19  ? 9.354  -9.598  11.497 1.00 18.31 ? 25  HIS   C CB  1 
ATOM   1248 C  CG  . HIS   B 1 19  ? 8.213  -8.886  12.203 1.00 20.83 ? 25  HIS   C CG  1 
ATOM   1249 N  ND1 . HIS   B 1 19  ? 8.375  -7.640  12.794 1.00 22.63 ? 25  HIS   C ND1 1 
ATOM   1250 C  CD2 . HIS   B 1 19  ? 7.003  -9.370  12.556 1.00 22.85 ? 25  HIS   C CD2 1 
ATOM   1251 C  CE1 . HIS   B 1 19  ? 7.180  -7.312  13.287 1.00 22.29 ? 25  HIS   C CE1 1 
ATOM   1252 N  NE2 . HIS   B 1 19  ? 6.337  -8.350  13.233 1.00 22.32 ? 25  HIS   C NE2 1 
ATOM   1253 N  N   . ASN   B 1 20  ? 9.340  -12.104 13.376 1.00 16.03 ? 26  ASN   C N   1 
ATOM   1254 C  CA  . ASN   B 1 20  ? 8.714  -12.852 14.470 1.00 16.78 ? 26  ASN   C CA  1 
ATOM   1255 C  C   . ASN   B 1 20  ? 9.644  -13.022 15.655 1.00 15.21 ? 26  ASN   C C   1 
ATOM   1256 O  O   . ASN   B 1 20  ? 9.220  -12.922 16.804 1.00 14.92 ? 26  ASN   C O   1 
ATOM   1257 C  CB  . ASN   B 1 20  ? 8.173  -14.219 14.025 1.00 18.64 ? 26  ASN   C CB  1 
ATOM   1258 C  CG  . ASN   B 1 20  ? 7.373  -14.900 15.132 1.00 25.70 ? 26  ASN   C CG  1 
ATOM   1259 O  OD1 . ASN   B 1 20  ? 6.271  -14.462 15.475 1.00 28.58 ? 26  ASN   C OD1 1 
ATOM   1260 N  ND2 . ASN   B 1 20  ? 7.936  -15.930 15.770 1.00 27.39 ? 26  ASN   C ND2 1 
ATOM   1261 N  N   . ASP   B 1 21  ? 10.970 -13.236 15.391 1.00 14.02 ? 27  ASP   C N   1 
ATOM   1262 C  CA  . ASP   B 1 21  ? 11.923 -13.315 16.492 1.00 14.21 ? 27  ASP   C CA  1 
ATOM   1263 C  C   . ASP   B 1 21  ? 11.965 -12.013 17.300 1.00 13.34 ? 27  ASP   C C   1 
ATOM   1264 O  O   . ASP   B 1 21  ? 11.895 -12.026 18.518 1.00 14.72 ? 27  ASP   C O   1 
ATOM   1265 C  CB  . ASP   B 1 21  ? 13.343 -13.631 15.997 1.00 14.19 ? 27  ASP   C CB  1 
ATOM   1266 C  CG  . ASP   B 1 21  ? 13.550 -15.052 15.511 1.00 14.04 ? 27  ASP   C CG  1 
ATOM   1267 O  OD1 . ASP   B 1 21  ? 12.963 -15.977 16.117 1.00 15.73 ? 27  ASP   C OD1 1 
ATOM   1268 O  OD2 . ASP   B 1 21  ? 14.228 -15.228 14.479 1.00 14.29 ? 27  ASP   C OD2 1 
ATOM   1269 N  N   . TRP   B 1 22  ? 12.051 -10.859 16.590 1.00 14.28 ? 28  TRP   C N   1 
ATOM   1270 C  CA  . TRP   B 1 22  ? 12.097 -9.565  17.278 1.00 14.33 ? 28  TRP   C CA  1 
ATOM   1271 C  C   . TRP   B 1 22  ? 10.759 -9.223  17.997 1.00 14.85 ? 28  TRP   C C   1 
ATOM   1272 O  O   . TRP   B 1 22  ? 10.785 -8.602  19.073 1.00 15.79 ? 28  TRP   C O   1 
ATOM   1273 C  CB  . TRP   B 1 22  ? 12.475 -8.443  16.309 1.00 14.85 ? 28  TRP   C CB  1 
ATOM   1274 C  CG  . TRP   B 1 22  ? 13.962 -8.396  16.043 1.00 14.80 ? 28  TRP   C CG  1 
ATOM   1275 C  CD1 . TRP   B 1 22  ? 14.617 -8.886  14.956 1.00 16.37 ? 28  TRP   C CD1 1 
ATOM   1276 C  CD2 . TRP   B 1 22  ? 14.974 -7.807  16.893 1.00 13.60 ? 28  TRP   C CD2 1 
ATOM   1277 N  NE1 . TRP   B 1 22  ? 15.978 -8.618  15.053 1.00 16.01 ? 28  TRP   C NE1 1 
ATOM   1278 C  CE2 . TRP   B 1 22  ? 16.216 -7.953  16.235 1.00 15.10 ? 28  TRP   C CE2 1 
ATOM   1279 C  CE3 . TRP   B 1 22  ? 14.944 -7.118  18.114 1.00 16.05 ? 28  TRP   C CE3 1 
ATOM   1280 C  CZ2 . TRP   B 1 22  ? 17.391 -7.430  16.742 1.00 14.98 ? 28  TRP   C CZ2 1 
ATOM   1281 C  CZ3 . TRP   B 1 22  ? 16.134 -6.632  18.629 1.00 16.56 ? 28  TRP   C CZ3 1 
ATOM   1282 C  CH2 . TRP   B 1 22  ? 17.334 -6.792  17.933 1.00 16.23 ? 28  TRP   C CH2 1 
ATOM   1283 N  N   . ALA   B 1 23  ? 9.649  -9.697  17.440 1.00 15.14 ? 29  ALA   C N   1 
ATOM   1284 C  CA  . ALA   B 1 23  ? 8.318  -9.449  18.054 1.00 15.71 ? 29  ALA   C CA  1 
ATOM   1285 C  C   . ALA   B 1 23  ? 8.082  -10.346 19.282 1.00 17.00 ? 29  ALA   C C   1 
ATOM   1286 O  O   . ALA   B 1 23  ? 7.120  -10.138 20.025 1.00 17.90 ? 29  ALA   C O   1 
ATOM   1287 C  CB  . ALA   B 1 23  ? 7.218  -9.708  17.030 1.00 16.98 ? 29  ALA   C CB  1 
ATOM   1288 N  N   . ASN   B 1 24  ? 8.941  -11.388 19.486 1.00 16.27 ? 30  ASN   C N   1 
ATOM   1289 C  CA  . ASN   B 1 24  ? 8.828  -12.292 20.634 1.00 15.35 ? 30  ASN   C CA  1 
ATOM   1290 C  C   . ASN   B 1 24  ? 10.201 -12.347 21.348 1.00 15.11 ? 30  ASN   C C   1 
ATOM   1291 O  O   . ASN   B 1 24  ? 10.636 -13.413 21.777 1.00 15.17 ? 30  ASN   C O   1 
ATOM   1292 C  CB  . ASN   B 1 24  ? 8.358  -13.687 20.155 1.00 16.99 ? 30  ASN   C CB  1 
ATOM   1293 C  CG  . ASN   B 1 24  ? 6.939  -13.628 19.671 1.00 18.76 ? 30  ASN   C CG  1 
ATOM   1294 O  OD1 . ASN   B 1 24  ? 5.975  -13.620 20.495 1.00 21.06 ? 30  ASN   C OD1 1 
ATOM   1295 N  ND2 . ASN   B 1 24  ? 6.772  -13.506 18.361 1.00 19.86 ? 30  ASN   C ND2 1 
ATOM   1296 N  N   . LEU   B 1 25  ? 10.921 -11.232 21.408 1.00 15.42 ? 31  LEU   C N   1 
ATOM   1297 C  CA  . LEU   B 1 25  ? 12.296 -11.201 21.908 1.00 14.72 ? 31  LEU   C CA  1 
ATOM   1298 C  C   . LEU   B 1 25  ? 12.430 -11.518 23.371 1.00 16.63 ? 31  LEU   C C   1 
ATOM   1299 O  O   . LEU   B 1 25  ? 11.661 -11.019 24.206 1.00 17.46 ? 31  LEU   C O   1 
ATOM   1300 C  CB  . LEU   B 1 25  ? 12.850 -9.794  21.644 1.00 15.53 ? 31  LEU   C CB  1 
ATOM   1301 C  CG  . LEU   B 1 25  ? 14.322 -9.632  22.016 1.00 15.61 ? 31  LEU   C CG  1 
ATOM   1302 C  CD1 . LEU   B 1 25  ? 15.243 -10.490 21.126 1.00 15.74 ? 31  LEU   C CD1 1 
ATOM   1303 C  CD2 . LEU   B 1 25  ? 14.714 -8.177  21.906 1.00 17.57 ? 31  LEU   C CD2 1 
ATOM   1304 N  N   . VAL   B 1 26  ? 13.417 -12.358 23.711 1.00 15.29 ? 32  VAL   C N   1 
ATOM   1305 C  CA  . VAL   B 1 26  ? 13.768 -12.622 25.102 1.00 15.69 ? 32  VAL   C CA  1 
ATOM   1306 C  C   . VAL   B 1 26  ? 15.092 -11.907 25.429 1.00 16.34 ? 32  VAL   C C   1 
ATOM   1307 O  O   . VAL   B 1 26  ? 15.201 -11.231 26.462 1.00 17.21 ? 32  VAL   C O   1 
ATOM   1308 C  CB  . VAL   B 1 26  ? 13.901 -14.141 25.348 1.00 16.20 ? 32  VAL   C CB  1 
ATOM   1309 C  CG1 . VAL   B 1 26  ? 14.461 -14.453 26.740 1.00 18.19 ? 32  VAL   C CG1 1 
ATOM   1310 C  CG2 . VAL   B 1 26  ? 12.561 -14.844 25.133 1.00 17.34 ? 32  VAL   C CG2 1 
ATOM   1311 N  N   . TRP   B 1 27  ? 16.120 -12.049 24.551 1.00 14.12 ? 33  TRP   C N   1 
ATOM   1312 C  CA  . TRP   B 1 27  ? 17.434 -11.475 24.842 1.00 14.02 ? 33  TRP   C CA  1 
ATOM   1313 C  C   . TRP   B 1 27  ? 18.218 -11.425 23.526 1.00 14.17 ? 33  TRP   C C   1 
ATOM   1314 O  O   . TRP   B 1 27  ? 18.027 -12.306 22.664 1.00 14.07 ? 33  TRP   C O   1 
ATOM   1315 C  CB  . TRP   B 1 27  ? 18.165 -12.375 25.877 1.00 15.97 ? 33  TRP   C CB  1 
ATOM   1316 C  CG  . TRP   B 1 27  ? 19.644 -12.108 26.076 1.00 16.08 ? 33  TRP   C CG  1 
ATOM   1317 C  CD1 . TRP   B 1 27  ? 20.233 -11.138 26.849 1.00 18.19 ? 33  TRP   C CD1 1 
ATOM   1318 C  CD2 . TRP   B 1 27  ? 20.724 -12.790 25.412 1.00 14.32 ? 33  TRP   C CD2 1 
ATOM   1319 N  NE1 . TRP   B 1 27  ? 21.620 -11.244 26.779 1.00 18.99 ? 33  TRP   C NE1 1 
ATOM   1320 C  CE2 . TRP   B 1 27  ? 21.939 -12.254 25.901 1.00 16.28 ? 33  TRP   C CE2 1 
ATOM   1321 C  CE3 . TRP   B 1 27  ? 20.779 -13.822 24.463 1.00 13.98 ? 33  TRP   C CE3 1 
ATOM   1322 C  CZ2 . TRP   B 1 27  ? 23.194 -12.754 25.505 1.00 16.13 ? 33  TRP   C CZ2 1 
ATOM   1323 C  CZ3 . TRP   B 1 27  ? 22.026 -14.334 24.106 1.00 16.05 ? 33  TRP   C CZ3 1 
ATOM   1324 C  CH2 . TRP   B 1 27  ? 23.201 -13.761 24.577 1.00 15.93 ? 33  TRP   C CH2 1 
ATOM   1325 N  N   . GLU   B 1 28  ? 19.070 -10.438 23.356 1.00 13.03 ? 34  GLU   C N   1 
ATOM   1326 C  CA  . GLU   B 1 28  ? 19.928 -10.349 22.176 1.00 14.11 ? 34  GLU   C CA  1 
ATOM   1327 C  C   . GLU   B 1 28  ? 21.216 -9.660  22.524 1.00 14.29 ? 34  GLU   C C   1 
ATOM   1328 O  O   . GLU   B 1 28  ? 21.238 -8.784  23.419 1.00 14.36 ? 34  GLU   C O   1 
ATOM   1329 C  CB  . GLU   B 1 28  ? 19.239 -9.675  21.005 1.00 15.55 ? 34  GLU   C CB  1 
ATOM   1330 C  CG  . GLU   B 1 28  ? 18.696 -8.295  21.283 1.00 15.89 ? 34  GLU   C CG  1 
ATOM   1331 C  CD  . GLU   B 1 28  ? 19.657 -7.128  21.210 1.00 17.77 ? 34  GLU   C CD  1 
ATOM   1332 O  OE1 . GLU   B 1 28  ? 19.376 -6.102  21.869 1.00 20.44 ? 34  GLU   C OE1 1 
ATOM   1333 O  OE2 . GLU   B 1 28  ? 20.676 -7.209  20.484 1.00 16.81 ? 34  GLU   C OE2 1 
ATOM   1334 N  N   . ASP   B 1 29  ? 22.308 -10.024 21.819 1.00 12.83 ? 35  ASP   C N   1 
ATOM   1335 C  CA  . ASP   B 1 29  ? 23.603 -9.374  22.050 1.00 13.15 ? 35  ASP   C CA  1 
ATOM   1336 C  C   . ASP   B 1 29  ? 24.371 -9.347  20.720 1.00 13.39 ? 35  ASP   C C   1 
ATOM   1337 O  O   . ASP   B 1 29  ? 24.802 -10.398 20.213 1.00 12.63 ? 35  ASP   C O   1 
ATOM   1338 C  CB  . ASP   B 1 29  ? 24.350 -10.164 23.142 1.00 15.51 ? 35  ASP   C CB  1 
ATOM   1339 C  CG  . ASP   B 1 29  ? 25.689 -9.598  23.539 1.00 19.55 ? 35  ASP   C CG  1 
ATOM   1340 O  OD1 . ASP   B 1 29  ? 26.416 -9.120  22.656 1.00 19.79 ? 35  ASP   C OD1 1 
ATOM   1341 O  OD2 . ASP   B 1 29  ? 26.069 -9.746  24.715 1.00 22.85 ? 35  ASP   C OD2 1 
ATOM   1342 N  N   . SER   B 1 30  ? 24.534 -8.132  20.145 1.00 13.39 ? 36  SER   C N   1 
ATOM   1343 C  CA  A SER   B 1 30  ? 25.231 -7.948  18.877 0.50 13.56 ? 36  SER   C CA  1 
ATOM   1344 C  CA  B SER   B 1 30  ? 25.198 -8.031  18.866 0.50 13.74 ? 36  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 30  ? 26.689 -8.414  18.954 1.00 14.21 ? 36  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 30  ? 27.207 -9.016  17.990 1.00 13.70 ? 36  SER   C O   1 
ATOM   1347 C  CB  A SER   B 1 30  ? 25.216 -6.478  18.457 0.50 14.68 ? 36  SER   C CB  1 
ATOM   1348 C  CB  B SER   B 1 30  ? 25.006 -6.647  18.271 0.50 15.71 ? 36  SER   C CB  1 
ATOM   1349 O  OG  A SER   B 1 30  ? 26.159 -6.225  17.420 0.50 14.85 ? 36  SER   C OG  1 
ATOM   1350 O  OG  B SER   B 1 30  ? 25.511 -5.688  19.175 0.50 17.19 ? 36  SER   C OG  1 
ATOM   1351 N  N   . SER   B 1 31  ? 27.355 -8.165  20.106 1.00 13.60 ? 37  SER   C N   1 
ATOM   1352 C  CA  . SER   B 1 31  ? 28.770 -8.557  20.217 1.00 14.53 ? 37  SER   C CA  1 
ATOM   1353 C  C   . SER   B 1 31  ? 28.954 -10.056 20.171 1.00 13.57 ? 37  SER   C C   1 
ATOM   1354 O  O   . SER   B 1 31  ? 30.044 -10.491 19.795 1.00 14.14 ? 37  SER   C O   1 
ATOM   1355 C  CB  . SER   B 1 31  ? 29.398 -8.008  21.484 1.00 17.69 ? 37  SER   C CB  1 
ATOM   1356 O  OG  . SER   B 1 31  ? 29.013 -8.702  22.650 1.00 21.78 ? 37  SER   C OG  1 
ATOM   1357 N  N   . ARG   B 1 32  ? 27.910 -10.863 20.498 1.00 12.27 ? 38  ARG   C N   1 
ATOM   1358 C  CA  . ARG   B 1 32  ? 27.982 -12.322 20.439 1.00 12.78 ? 38  ARG   C CA  1 
ATOM   1359 C  C   . ARG   B 1 32  ? 27.350 -12.885 19.161 1.00 12.02 ? 38  ARG   C C   1 
ATOM   1360 O  O   . ARG   B 1 32  ? 27.387 -14.101 18.953 1.00 11.32 ? 38  ARG   C O   1 
ATOM   1361 C  CB  . ARG   B 1 32  ? 27.231 -12.914 21.661 1.00 13.82 ? 38  ARG   C CB  1 
ATOM   1362 C  CG  . ARG   B 1 32  ? 27.897 -12.557 22.977 1.00 14.55 ? 38  ARG   C CG  1 
ATOM   1363 C  CD  . ARG   B 1 32  ? 27.154 -13.117 24.192 1.00 12.27 ? 38  ARG   C CD  1 
ATOM   1364 N  NE  . ARG   B 1 32  ? 27.215 -14.604 24.217 1.00 12.23 ? 38  ARG   C NE  1 
ATOM   1365 C  CZ  . ARG   B 1 32  ? 27.178 -15.343 25.328 1.00 12.62 ? 38  ARG   C CZ  1 
ATOM   1366 N  NH1 . ARG   B 1 32  ? 27.071 -14.770 26.518 1.00 14.08 ? 38  ARG   C NH1 1 
ATOM   1367 N  NH2 . ARG   B 1 32  ? 27.339 -16.666 25.259 1.00 12.64 ? 38  ARG   C NH2 1 
ATOM   1368 N  N   . ASP   B 1 33  ? 26.674 -12.047 18.340 1.00 10.89 ? 39  ASP   C N   1 
ATOM   1369 C  CA  . ASP   B 1 33  ? 25.896 -12.497 17.197 1.00 10.77 ? 39  ASP   C CA  1 
ATOM   1370 C  C   . ASP   B 1 33  ? 24.782 -13.473 17.635 1.00 10.44 ? 39  ASP   C C   1 
ATOM   1371 O  O   . ASP   B 1 33  ? 24.470 -14.428 16.888 1.00 10.95 ? 39  ASP   C O   1 
ATOM   1372 C  CB  . ASP   B 1 33  ? 26.725 -13.124 16.082 1.00 10.79 ? 39  ASP   C CB  1 
ATOM   1373 C  CG  . ASP   B 1 33  ? 25.933 -13.457 14.815 1.00 11.41 ? 39  ASP   C CG  1 
ATOM   1374 O  OD1 . ASP   B 1 33  ? 25.039 -12.664 14.436 1.00 12.45 ? 39  ASP   C OD1 1 
ATOM   1375 O  OD2 . ASP   B 1 33  ? 26.260 -14.473 14.160 1.00 11.52 ? 39  ASP   C OD2 1 
ATOM   1376 N  N   . LEU   B 1 34  ? 24.119 -13.229 18.794 1.00 10.25 ? 40  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 34  ? 23.038 -14.143 19.231 1.00 11.25 ? 40  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 34  ? 21.736 -13.386 19.499 1.00 10.86 ? 40  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 34  ? 21.754 -12.225 19.972 1.00 11.74 ? 40  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 34  ? 23.443 -14.848 20.545 1.00 11.46 ? 40  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 34  ? 24.496 -15.967 20.453 1.00 11.52 ? 40  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 34  ? 24.749 -16.552 21.875 1.00 13.37 ? 40  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 34  ? 24.041 -17.101 19.499 1.00 12.62 ? 40  LEU   C CD2 1 
ATOM   1384 N  N   . LEU   B 1 35  ? 20.640 -14.071 19.272 1.00 10.40 ? 41  LEU   C N   1 
ATOM   1385 C  CA  . LEU   B 1 35  ? 19.315 -13.572 19.653 1.00 11.34 ? 41  LEU   C CA  1 
ATOM   1386 C  C   . LEU   B 1 35  ? 18.481 -14.787 20.059 1.00 11.60 ? 41  LEU   C C   1 
ATOM   1387 O  O   . LEU   B 1 35  ? 18.558 -15.863 19.432 1.00 12.18 ? 41  LEU   C O   1 
ATOM   1388 C  CB  . LEU   B 1 35  ? 18.658 -12.853 18.438 1.00 11.64 ? 41  LEU   C CB  1 
ATOM   1389 C  CG  . LEU   B 1 35  ? 17.260 -12.261 18.690 1.00 11.91 ? 41  LEU   C CG  1 
ATOM   1390 C  CD1 . LEU   B 1 35  ? 17.047 -10.952 17.925 1.00 14.01 ? 41  LEU   C CD1 1 
ATOM   1391 C  CD2 . LEU   B 1 35  ? 16.167 -13.280 18.367 1.00 13.15 ? 41  LEU   C CD2 1 
ATOM   1392 N  N   . VAL   B 1 36  ? 17.701 -14.609 21.130 1.00 11.90 ? 42  VAL   C N   1 
ATOM   1393 C  CA  . VAL   B 1 36  ? 16.779 -15.623 21.641 1.00 11.96 ? 42  VAL   C CA  1 
ATOM   1394 C  C   . VAL   B 1 36  ? 15.358 -15.079 21.628 1.00 11.73 ? 42  VAL   C C   1 
ATOM   1395 O  O   . VAL   B 1 36  ? 15.139 -13.951 22.113 1.00 13.19 ? 42  VAL   C O   1 
ATOM   1396 C  CB  . VAL   B 1 36  ? 17.192 -16.062 23.063 1.00 12.20 ? 42  VAL   C CB  1 
ATOM   1397 C  CG1 . VAL   B 1 36  ? 16.228 -17.120 23.605 1.00 13.88 ? 42  VAL   C CG1 1 
ATOM   1398 C  CG2 . VAL   B 1 36  ? 18.638 -16.632 23.046 1.00 13.48 ? 42  VAL   C CG2 1 
ATOM   1399 N  N   . SER   B 1 37  ? 14.435 -15.831 21.073 1.00 11.90 ? 43  SER   C N   1 
ATOM   1400 C  CA  . SER   B 1 37  ? 13.024 -15.477 21.064 1.00 12.10 ? 43  SER   C CA  1 
ATOM   1401 C  C   . SER   B 1 37  ? 12.214 -16.578 21.755 1.00 12.96 ? 43  SER   C C   1 
ATOM   1402 O  O   . SER   B 1 37  ? 12.692 -17.711 21.981 1.00 13.42 ? 43  SER   C O   1 
ATOM   1403 C  CB  . SER   B 1 37  ? 12.533 -15.276 19.633 1.00 13.10 ? 43  SER   C CB  1 
ATOM   1404 O  OG  . SER   B 1 37  ? 12.705 -16.440 18.831 1.00 14.43 ? 43  SER   C OG  1 
ATOM   1405 N  N   . SER   B 1 38  ? 10.973 -16.257 22.136 1.00 13.93 ? 44  SER   C N   1 
ATOM   1406 C  CA  . SER   B 1 38  ? 10.105 -17.238 22.789 1.00 15.09 ? 44  SER   C CA  1 
ATOM   1407 C  C   . SER   B 1 38  ? 9.291  -18.022 21.758 1.00 17.14 ? 44  SER   C C   1 
ATOM   1408 O  O   . SER   B 1 38  ? 8.963  -17.511 20.694 1.00 18.34 ? 44  SER   C O   1 
ATOM   1409 C  CB  . SER   B 1 38  ? 9.209  -16.528 23.799 1.00 17.46 ? 44  SER   C CB  1 
ATOM   1410 O  OG  . SER   B 1 38  ? 8.364  -15.644 23.089 1.00 20.90 ? 44  SER   C OG  1 
ATOM   1411 N  N   . THR   B 1 39  ? 8.929  -19.262 22.092 1.00 16.83 ? 45  THR   C N   1 
ATOM   1412 C  CA  . THR   B 1 39  ? 8.166  -20.160 21.209 1.00 17.94 ? 45  THR   C CA  1 
ATOM   1413 C  C   . THR   B 1 39  ? 6.872  -20.626 21.903 1.00 20.11 ? 45  THR   C C   1 
ATOM   1414 O  O   . THR   B 1 39  ? 6.826  -20.731 23.112 1.00 19.83 ? 45  THR   C O   1 
ATOM   1415 C  CB  . THR   B 1 39  ? 9.007  -21.423 20.849 1.00 18.62 ? 45  THR   C CB  1 
ATOM   1416 O  OG1 . THR   B 1 39  ? 9.297  -22.173 22.021 1.00 19.35 ? 45  THR   C OG1 1 
ATOM   1417 C  CG2 . THR   B 1 39  ? 10.352 -21.067 20.182 1.00 18.89 ? 45  THR   C CG2 1 
ATOM   1418 N  N   . THR   B 1 40  ? 5.876  -20.992 21.111 1.00 22.65 ? 46  THR   C N   1 
ATOM   1419 C  CA  . THR   B 1 40  ? 4.629  -21.547 21.665 1.00 24.72 ? 46  THR   C CA  1 
ATOM   1420 C  C   . THR   B 1 40  ? 4.853  -23.010 22.028 1.00 24.85 ? 46  THR   C C   1 
ATOM   1421 O  O   . THR   B 1 40  ? 4.439  -23.458 23.108 1.00 27.23 ? 46  THR   C O   1 
ATOM   1422 C  CB  . THR   B 1 40  ? 3.472  -21.300 20.702 1.00 29.13 ? 46  THR   C CB  1 
ATOM   1423 O  OG1 . THR   B 1 40  ? 3.792  -21.901 19.451 1.00 33.61 ? 46  THR   C OG1 1 
ATOM   1424 C  CG2 . THR   B 1 40  ? 3.253  -19.829 20.460 1.00 28.73 ? 46  THR   C CG2 1 
ATOM   1425 N  N   . ALA   B 1 41  ? 5.522  -23.768 21.132 1.00 22.26 ? 47  ALA   C N   1 
ATOM   1426 C  CA  . ALA   B 1 41  ? 5.769  -25.184 21.377 1.00 22.89 ? 47  ALA   C CA  1 
ATOM   1427 C  C   . ALA   B 1 41  ? 7.101  -25.432 22.100 1.00 21.24 ? 47  ALA   C C   1 
ATOM   1428 O  O   . ALA   B 1 41  ? 8.030  -24.671 21.902 1.00 20.71 ? 47  ALA   C O   1 
ATOM   1429 C  CB  . ALA   B 1 41  ? 5.772  -25.933 20.057 1.00 24.85 ? 47  ALA   C CB  1 
ATOM   1430 N  N   . GLN   B 1 42  ? 7.219  -26.495 22.895 1.00 20.64 ? 48  GLN   C N   1 
ATOM   1431 C  CA  . GLN   B 1 42  ? 8.454  -26.844 23.583 1.00 21.02 ? 48  GLN   C CA  1 
ATOM   1432 C  C   . GLN   B 1 42  ? 9.422  -27.496 22.599 1.00 20.39 ? 48  GLN   C C   1 
ATOM   1433 O  O   . GLN   B 1 42  ? 9.003  -28.294 21.748 1.00 21.92 ? 48  GLN   C O   1 
ATOM   1434 C  CB  . GLN   B 1 42  ? 8.183  -27.774 24.787 1.00 25.64 ? 48  GLN   C CB  1 
ATOM   1435 C  CG  . GLN   B 1 42  ? 7.568  -27.014 25.973 1.00 34.85 ? 48  GLN   C CG  1 
ATOM   1436 C  CD  . GLN   B 1 42  ? 7.438  -27.939 27.151 1.00 46.53 ? 48  GLN   C CD  1 
ATOM   1437 O  OE1 . GLN   B 1 42  ? 6.590  -28.837 27.176 1.00 50.70 ? 48  GLN   C OE1 1 
ATOM   1438 N  NE2 . GLN   B 1 42  ? 8.279  -27.758 28.158 1.00 49.82 ? 48  GLN   C NE2 1 
ATOM   1439 N  N   . GLY   B 1 43  ? 10.700 -27.145 22.729 1.00 17.94 ? 49  GLY   C N   1 
ATOM   1440 C  CA  . GLY   B 1 43  ? 11.799 -27.706 21.938 1.00 17.82 ? 49  GLY   C CA  1 
ATOM   1441 C  C   . GLY   B 1 43  ? 12.453 -28.853 22.683 1.00 18.14 ? 49  GLY   C C   1 
ATOM   1442 O  O   . GLY   B 1 43  ? 12.227 -29.031 23.890 1.00 20.46 ? 49  GLY   C O   1 
ATOM   1443 N  N   . CYS   B 1 44  ? 13.282 -29.584 21.991 1.00 16.15 ? 50  CYS   C N   1 
ATOM   1444 C  CA  . CYS   B 1 44  ? 13.859 -30.802 22.540 1.00 16.55 ? 50  CYS   C CA  1 
ATOM   1445 C  C   . CYS   B 1 44  ? 15.361 -30.839 22.587 1.00 16.99 ? 50  CYS   C C   1 
ATOM   1446 O  O   . CYS   B 1 44  ? 15.911 -31.898 22.955 1.00 20.01 ? 50  CYS   C O   1 
ATOM   1447 C  CB  . CYS   B 1 44  ? 13.301 -31.994 21.762 1.00 16.93 ? 50  CYS   C CB  1 
ATOM   1448 S  SG  . CYS   B 1 44  ? 11.492 -32.123 21.889 1.00 23.76 ? 50  CYS   C SG  1 
ATOM   1449 N  N   . ASP   B 1 45  ? 16.063 -29.782 22.180 1.00 13.96 ? 51  ASP   C N   1 
ATOM   1450 C  CA  . ASP   B 1 45  ? 17.515 -29.784 22.221 1.00 13.97 ? 51  ASP   C CA  1 
ATOM   1451 C  C   . ASP   B 1 45  ? 17.929 -29.597 23.674 1.00 15.24 ? 51  ASP   C C   1 
ATOM   1452 O  O   . ASP   B 1 45  ? 17.233 -28.918 24.472 1.00 17.11 ? 51  ASP   C O   1 
ATOM   1453 C  CB  . ASP   B 1 45  ? 18.083 -28.627 21.366 1.00 14.72 ? 51  ASP   C CB  1 
ATOM   1454 C  CG  . ASP   B 1 45  ? 17.885 -28.782 19.880 1.00 17.37 ? 51  ASP   C CG  1 
ATOM   1455 O  OD1 . ASP   B 1 45  ? 17.890 -29.934 19.398 1.00 19.37 ? 51  ASP   C OD1 1 
ATOM   1456 O  OD2 . ASP   B 1 45  ? 17.736 -27.736 19.172 1.00 16.03 ? 51  ASP   C OD2 1 
ATOM   1457 N  N   . THR   B 1 46  ? 19.031 -30.215 24.035 1.00 13.37 ? 52  THR   C N   1 
ATOM   1458 C  CA  . THR   B 1 46  ? 19.664 -30.048 25.351 1.00 13.17 ? 52  THR   C CA  1 
ATOM   1459 C  C   . THR   B 1 46  ? 20.921 -29.190 25.191 1.00 12.48 ? 52  THR   C C   1 
ATOM   1460 O  O   . THR   B 1 46  ? 21.731 -29.492 24.297 1.00 13.22 ? 52  THR   C O   1 
ATOM   1461 C  CB  . THR   B 1 46  ? 20.040 -31.405 25.927 1.00 15.51 ? 52  THR   C CB  1 
ATOM   1462 O  OG1 . THR   B 1 46  ? 18.837 -32.200 26.139 1.00 17.90 ? 52  THR   C OG1 1 
ATOM   1463 C  CG2 . THR   B 1 46  ? 20.853 -31.297 27.241 1.00 18.67 ? 52  THR   C CG2 1 
ATOM   1464 N  N   . ILE   B 1 47  ? 21.096 -28.159 26.009 1.00 12.92 ? 53  ILE   C N   1 
ATOM   1465 C  CA  . ILE   B 1 47  ? 22.299 -27.339 25.951 1.00 12.44 ? 53  ILE   C CA  1 
ATOM   1466 C  C   . ILE   B 1 47  ? 23.396 -28.023 26.794 1.00 11.58 ? 53  ILE   C C   1 
ATOM   1467 O  O   . ILE   B 1 47  ? 23.167 -28.453 27.940 1.00 13.00 ? 53  ILE   C O   1 
ATOM   1468 C  CB  . ILE   B 1 47  ? 22.041 -25.946 26.539 1.00 13.44 ? 53  ILE   C CB  1 
ATOM   1469 C  CG1 . ILE   B 1 47  ? 20.835 -25.256 25.883 1.00 14.04 ? 53  ILE   C CG1 1 
ATOM   1470 C  CG2 . ILE   B 1 47  ? 23.308 -25.089 26.473 1.00 14.08 ? 53  ILE   C CG2 1 
ATOM   1471 C  CD1 . ILE   B 1 47  ? 21.025 -25.135 24.356 1.00 16.24 ? 53  ILE   C CD1 1 
ATOM   1472 N  N   . ALA   B 1 48  ? 24.606 -28.106 26.249 1.00 10.90 ? 54  ALA   C N   1 
ATOM   1473 C  CA  . ALA   B 1 48  ? 25.745 -28.665 26.992 1.00 10.94 ? 54  ALA   C CA  1 
ATOM   1474 C  C   . ALA   B 1 48  ? 26.100 -27.723 28.158 1.00 10.38 ? 54  ALA   C C   1 
ATOM   1475 O  O   . ALA   B 1 48  ? 26.065 -26.473 28.006 1.00 11.35 ? 54  ALA   C O   1 
ATOM   1476 C  CB  . ALA   B 1 48  ? 26.949 -28.772 26.058 1.00 11.39 ? 54  ALA   C CB  1 
ATOM   1477 N  N   . ARG   B 1 49  ? 26.477 -28.333 29.312 1.00 11.07 ? 55  ARG   C N   1 
ATOM   1478 C  CA  . ARG   B 1 49  ? 26.914 -27.575 30.485 1.00 11.12 ? 55  ARG   C CA  1 
ATOM   1479 C  C   . ARG   B 1 49  ? 28.243 -28.216 30.869 1.00 11.30 ? 55  ARG   C C   1 
ATOM   1480 O  O   . ARG   B 1 49  ? 28.279 -29.247 31.562 1.00 12.86 ? 55  ARG   C O   1 
ATOM   1481 C  CB  . ARG   B 1 49  ? 25.880 -27.601 31.627 1.00 12.20 ? 55  ARG   C CB  1 
ATOM   1482 C  CG  . ARG   B 1 49  ? 24.515 -27.044 31.181 1.00 11.77 ? 55  ARG   C CG  1 
ATOM   1483 C  CD  . ARG   B 1 49  ? 24.555 -25.554 30.836 1.00 13.16 ? 55  ARG   C CD  1 
ATOM   1484 N  NE  . ARG   B 1 49  ? 23.198 -25.112 30.483 1.00 13.32 ? 55  ARG   C NE  1 
ATOM   1485 C  CZ  . ARG   B 1 49  ? 22.935 -24.006 29.777 1.00 12.59 ? 55  ARG   C CZ  1 
ATOM   1486 N  NH1 . ARG   B 1 49  ? 23.912 -23.180 29.433 1.00 12.99 ? 55  ARG   C NH1 1 
ATOM   1487 N  NH2 . ARG   B 1 49  ? 21.674 -23.722 29.399 1.00 14.44 ? 55  ARG   C NH2 1 
ATOM   1488 N  N   . CYS   B 1 50  ? 29.333 -27.649 30.340 1.00 10.78 ? 56  CYS   C N   1 
ATOM   1489 C  CA  . CYS   B 1 50  ? 30.675 -28.282 30.375 1.00 10.92 ? 56  CYS   C CA  1 
ATOM   1490 C  C   . CYS   B 1 50  ? 31.720 -27.305 29.842 1.00 11.29 ? 56  CYS   C C   1 
ATOM   1491 O  O   . CYS   B 1 50  ? 31.409 -26.191 29.391 1.00 11.75 ? 56  CYS   C O   1 
ATOM   1492 C  CB  . CYS   B 1 50  ? 30.629 -29.504 29.448 1.00 10.44 ? 56  CYS   C CB  1 
ATOM   1493 S  SG  . CYS   B 1 50  ? 30.472 -29.063 27.673 1.00 11.39 ? 56  CYS   C SG  1 
ATOM   1494 N  N   . ASP   B 1 51  ? 33.007 -27.777 29.895 1.00 12.65 ? 57  ASP   C N   1 
ATOM   1495 C  CA  . ASP   B 1 51  ? 34.125 -27.037 29.286 1.00 13.19 ? 57  ASP   C CA  1 
ATOM   1496 C  C   . ASP   B 1 51  ? 34.804 -27.911 28.201 1.00 13.02 ? 57  ASP   C C   1 
ATOM   1497 O  O   . ASP   B 1 51  ? 36.008 -27.755 27.937 1.00 14.22 ? 57  ASP   C O   1 
ATOM   1498 C  CB  . ASP   B 1 51  ? 35.159 -26.618 30.347 1.00 15.84 ? 57  ASP   C CB  1 
ATOM   1499 C  CG  . ASP   B 1 51  ? 35.836 -27.743 31.072 1.00 19.74 ? 57  ASP   C CG  1 
ATOM   1500 O  OD1 . ASP   B 1 51  ? 35.502 -28.896 30.820 1.00 18.80 ? 57  ASP   C OD1 1 
ATOM   1501 O  OD2 . ASP   B 1 51  ? 36.784 -27.453 31.878 1.00 25.86 ? 57  ASP   C OD2 1 
ATOM   1502 N  N   . CYS   B 1 52  ? 34.035 -28.778 27.503 1.00 11.88 ? 58  CYS   C N   1 
ATOM   1503 C  CA  . CYS   B 1 52  ? 34.607 -29.550 26.365 1.00 11.49 ? 58  CYS   C CA  1 
ATOM   1504 C  C   . CYS   B 1 52  ? 35.258 -28.641 25.347 1.00 10.93 ? 58  CYS   C C   1 
ATOM   1505 O  O   . CYS   B 1 52  ? 34.814 -27.507 25.101 1.00 11.41 ? 58  CYS   C O   1 
ATOM   1506 C  CB  . CYS   B 1 52  ? 33.533 -30.376 25.641 1.00 11.90 ? 58  CYS   C CB  1 
ATOM   1507 S  SG  . CYS   B 1 52  ? 32.912 -31.776 26.575 1.00 12.28 ? 58  CYS   C SG  1 
ATOM   1508 N  N   . GLN   B 1 53  ? 36.304 -29.167 24.729 1.00 10.64 ? 59  GLN   C N   1 
ATOM   1509 C  CA  . GLN   B 1 53  ? 36.995 -28.578 23.571 1.00 11.53 ? 59  GLN   C CA  1 
ATOM   1510 C  C   . GLN   B 1 53  ? 37.054 -29.504 22.400 1.00 11.30 ? 59  GLN   C C   1 
ATOM   1511 O  O   . GLN   B 1 53  ? 37.822 -29.281 21.455 1.00 11.40 ? 59  GLN   C O   1 
ATOM   1512 C  CB  . GLN   B 1 53  ? 38.417 -28.117 23.931 1.00 12.28 ? 59  GLN   C CB  1 
ATOM   1513 C  CG  . GLN   B 1 53  ? 38.388 -26.897 24.837 1.00 16.40 ? 59  GLN   C CG  1 
ATOM   1514 C  CD  . GLN   B 1 53  ? 39.762 -26.318 25.053 1.00 18.65 ? 59  GLN   C CD  1 
ATOM   1515 O  OE1 . GLN   B 1 53  ? 40.270 -26.326 26.207 1.00 20.40 ? 59  GLN   C OE1 1 
ATOM   1516 N  NE2 . GLN   B 1 53  ? 40.398 -25.787 23.984 1.00 16.17 ? 59  GLN   C NE2 1 
ATOM   1517 N  N   . THR   B 1 54  ? 36.270 -30.599 22.406 1.00 10.68 ? 60  THR   C N   1 
ATOM   1518 C  CA  . THR   B 1 54  ? 36.155 -31.470 21.235 1.00 11.73 ? 60  THR   C CA  1 
ATOM   1519 C  C   . THR   B 1 54  ? 34.661 -31.727 21.000 1.00 11.27 ? 60  THR   C C   1 
ATOM   1520 O  O   . THR   B 1 54  ? 33.875 -31.839 21.946 1.00 11.94 ? 60  THR   C O   1 
ATOM   1521 C  CB  . THR   B 1 54  ? 36.896 -32.764 21.336 1.00 14.73 ? 60  THR   C CB  1 
ATOM   1522 O  OG1 . THR   B 1 54  ? 36.351 -33.526 22.336 1.00 19.26 ? 60  THR   C OG1 1 
ATOM   1523 C  CG2 . THR   B 1 54  ? 38.372 -32.564 21.621 1.00 15.02 ? 60  THR   C CG2 1 
ATOM   1524 N  N   . GLY   B 1 55  ? 34.271 -31.790 19.730 1.00 10.30 ? 61  GLY   C N   1 
ATOM   1525 C  CA  . GLY   B 1 55  ? 32.862 -31.989 19.386 1.00 10.24 ? 61  GLY   C CA  1 
ATOM   1526 C  C   . GLY   B 1 55  ? 32.740 -32.167 17.881 1.00 9.35  ? 61  GLY   C C   1 
ATOM   1527 O  O   . GLY   B 1 55  ? 33.734 -32.477 17.196 1.00 10.97 ? 61  GLY   C O   1 
ATOM   1528 N  N   . VAL   B 1 56  ? 31.514 -32.078 17.403 1.00 9.15  ? 62  VAL   C N   1 
ATOM   1529 C  CA  . VAL   B 1 56  ? 31.207 -32.290 15.971 1.00 8.78  ? 62  VAL   C CA  1 
ATOM   1530 C  C   . VAL   B 1 56  ? 30.304 -31.143 15.532 1.00 8.71  ? 62  VAL   C C   1 
ATOM   1531 O  O   . VAL   B 1 56  ? 29.363 -30.828 16.239 1.00 9.73  ? 62  VAL   C O   1 
ATOM   1532 C  CB  . VAL   B 1 56  ? 30.447 -33.645 15.815 1.00 9.35  ? 62  VAL   C CB  1 
ATOM   1533 C  CG1 . VAL   B 1 56  ? 29.984 -33.843 14.362 1.00 11.00 ? 62  VAL   C CG1 1 
ATOM   1534 C  CG2 . VAL   B 1 56  ? 31.358 -34.832 16.232 1.00 10.56 ? 62  VAL   C CG2 1 
ATOM   1535 N  N   . TYR   B 1 57  ? 30.573 -30.559 14.353 1.00 9.17  ? 63  TYR   C N   1 
ATOM   1536 C  CA  . TYR   B 1 57  ? 29.670 -29.493 13.853 1.00 8.64  ? 63  TYR   C CA  1 
ATOM   1537 C  C   . TYR   B 1 57  ? 29.106 -29.842 12.481 1.00 8.91  ? 63  TYR   C C   1 
ATOM   1538 O  O   . TYR   B 1 57  ? 29.771 -30.534 11.704 1.00 9.98  ? 63  TYR   C O   1 
ATOM   1539 C  CB  . TYR   B 1 57  ? 30.352 -28.072 13.832 1.00 9.73  ? 63  TYR   C CB  1 
ATOM   1540 C  CG  . TYR   B 1 57  ? 31.221 -27.756 12.621 1.00 9.64  ? 63  TYR   C CG  1 
ATOM   1541 C  CD1 . TYR   B 1 57  ? 32.499 -28.255 12.523 1.00 10.53 ? 63  TYR   C CD1 1 
ATOM   1542 C  CD2 . TYR   B 1 57  ? 30.753 -26.935 11.596 1.00 9.50  ? 63  TYR   C CD2 1 
ATOM   1543 C  CE1 . TYR   B 1 57  ? 33.315 -27.951 11.436 1.00 10.86 ? 63  TYR   C CE1 1 
ATOM   1544 C  CE2 . TYR   B 1 57  ? 31.569 -26.601 10.507 1.00 10.45 ? 63  TYR   C CE2 1 
ATOM   1545 C  CZ  . TYR   B 1 57  ? 32.845 -27.113 10.434 1.00 10.71 ? 63  TYR   C CZ  1 
ATOM   1546 O  OH  . TYR   B 1 57  ? 33.709 -26.819 9.375  1.00 13.06 ? 63  TYR   C OH  1 
ATOM   1547 N  N   . TYR   B 1 58  ? 27.950 -29.278 12.186 1.00 9.49  ? 64  TYR   C N   1 
ATOM   1548 C  CA  . TYR   B 1 58  ? 27.326 -29.428 10.859 1.00 9.61  ? 64  TYR   C CA  1 
ATOM   1549 C  C   . TYR   B 1 58  ? 27.704 -28.294 9.948  1.00 9.58  ? 64  TYR   C C   1 
ATOM   1550 O  O   . TYR   B 1 58  ? 27.460 -27.103 10.252 1.00 10.37 ? 64  TYR   C O   1 
ATOM   1551 C  CB  . TYR   B 1 58  ? 25.807 -29.540 10.959 1.00 10.64 ? 64  TYR   C CB  1 
ATOM   1552 C  CG  . TYR   B 1 58  ? 25.199 -29.822 9.593  1.00 11.38 ? 64  TYR   C CG  1 
ATOM   1553 C  CD1 . TYR   B 1 58  ? 25.532 -30.980 8.895  1.00 12.01 ? 64  TYR   C CD1 1 
ATOM   1554 C  CD2 . TYR   B 1 58  ? 24.327 -28.926 9.000  1.00 11.89 ? 64  TYR   C CD2 1 
ATOM   1555 C  CE1 . TYR   B 1 58  ? 25.029 -31.231 7.613  1.00 12.45 ? 64  TYR   C CE1 1 
ATOM   1556 C  CE2 . TYR   B 1 58  ? 23.806 -29.177 7.718  1.00 12.45 ? 64  TYR   C CE2 1 
ATOM   1557 C  CZ  . TYR   B 1 58  ? 24.167 -30.337 7.058  1.00 12.62 ? 64  TYR   C CZ  1 
ATOM   1558 O  OH  . TYR   B 1 58  ? 23.703 -30.607 5.761  1.00 15.76 ? 64  TYR   C OH  1 
ATOM   1559 N  N   . CYS   B 1 59  ? 28.220 -28.663 8.777  1.00 9.41  ? 65  CYS   C N   1 
ATOM   1560 C  CA  . CYS   B 1 59  ? 28.633 -27.721 7.712  1.00 10.16 ? 65  CYS   C CA  1 
ATOM   1561 C  C   . CYS   B 1 59  ? 27.690 -27.918 6.500  1.00 10.91 ? 65  CYS   C C   1 
ATOM   1562 O  O   . CYS   B 1 59  ? 27.860 -28.862 5.717  1.00 11.89 ? 65  CYS   C O   1 
ATOM   1563 C  CB  . CYS   B 1 59  ? 30.070 -27.994 7.319  1.00 10.43 ? 65  CYS   C CB  1 
ATOM   1564 S  SG  . CYS   B 1 59  ? 30.664 -26.938 5.971  1.00 12.59 ? 65  CYS   C SG  1 
ATOM   1565 N  N   . SER   B 1 60  ? 26.704 -27.052 6.372  1.00 11.97 ? 66  SER   C N   1 
ATOM   1566 C  CA  . SER   B 1 60  ? 25.718 -27.216 5.319  1.00 12.88 ? 66  SER   C CA  1 
ATOM   1567 C  C   . SER   B 1 60  ? 26.332 -27.139 3.908  1.00 13.05 ? 66  SER   C C   1 
ATOM   1568 O  O   . SER   B 1 60  ? 25.896 -27.896 3.035  1.00 14.33 ? 66  SER   C O   1 
ATOM   1569 C  CB  . SER   B 1 60  ? 24.604 -26.206 5.508  1.00 16.39 ? 66  SER   C CB  1 
ATOM   1570 O  OG  . SER   B 1 60  ? 25.040 -24.861 5.497  1.00 25.57 ? 66  SER   C OG  1 
ATOM   1571 N  N   . SER   B 1 61  ? 27.324 -26.259 3.718  1.00 12.04 ? 67  SER   C N   1 
ATOM   1572 C  CA  . SER   B 1 61  ? 27.968 -26.100 2.391  1.00 12.71 ? 67  SER   C CA  1 
ATOM   1573 C  C   . SER   B 1 61  ? 28.802 -27.303 1.989  1.00 14.08 ? 67  SER   C C   1 
ATOM   1574 O  O   . SER   B 1 61  ? 29.219 -27.364 0.817  1.00 16.35 ? 67  SER   C O   1 
ATOM   1575 C  CB  . SER   B 1 61  ? 28.804 -24.834 2.349  1.00 13.86 ? 67  SER   C CB  1 
ATOM   1576 O  OG  . SER   B 1 61  ? 29.914 -24.928 3.203  1.00 13.80 ? 67  SER   C OG  1 
ATOM   1577 N  N   . ARG   B 1 62  ? 28.980 -28.324 2.846  1.00 12.58 ? 68  ARG   C N   1 
ATOM   1578 C  CA  . ARG   B 1 62  ? 29.625 -29.591 2.485  1.00 13.47 ? 68  ARG   C CA  1 
ATOM   1579 C  C   . ARG   B 1 62  ? 28.681 -30.785 2.705  1.00 13.73 ? 68  ARG   C C   1 
ATOM   1580 O  O   . ARG   B 1 62  ? 29.089 -31.936 2.531  1.00 14.76 ? 68  ARG   C O   1 
ATOM   1581 C  CB  . ARG   B 1 62  ? 30.904 -29.786 3.308  1.00 13.28 ? 68  ARG   C CB  1 
ATOM   1582 C  CG  . ARG   B 1 62  ? 31.948 -28.690 3.080  1.00 16.90 ? 68  ARG   C CG  1 
ATOM   1583 C  CD  . ARG   B 1 62  ? 32.618 -28.909 1.761  1.00 17.08 ? 68  ARG   C CD  1 
ATOM   1584 N  NE  . ARG   B 1 62  ? 33.650 -27.881 1.464  1.00 19.59 ? 68  ARG   C NE  1 
ATOM   1585 C  CZ  . ARG   B 1 62  ? 33.428 -26.719 0.866  1.00 21.54 ? 68  ARG   C CZ  1 
ATOM   1586 N  NH1 . ARG   B 1 62  ? 32.222 -26.424 0.396  1.00 23.69 ? 68  ARG   C NH1 1 
ATOM   1587 N  NH2 . ARG   B 1 62  ? 34.450 -25.901 0.579  1.00 23.33 ? 68  ARG   C NH2 1 
ATOM   1588 N  N   . ARG   B 1 63  ? 27.470 -30.540 3.263  1.00 14.21 ? 69  ARG   C N   1 
ATOM   1589 C  CA  . ARG   B 1 63  ? 26.530 -31.597 3.686  1.00 15.69 ? 69  ARG   C CA  1 
ATOM   1590 C  C   . ARG   B 1 63  ? 27.234 -32.620 4.569  1.00 16.08 ? 69  ARG   C C   1 
ATOM   1591 O  O   . ARG   B 1 63  ? 27.103 -33.845 4.371  1.00 17.71 ? 69  ARG   C O   1 
ATOM   1592 C  CB  . ARG   B 1 63  ? 25.887 -32.285 2.468  1.00 16.65 ? 69  ARG   C CB  1 
ATOM   1593 C  CG  . ARG   B 1 63  ? 25.034 -31.357 1.635  1.00 18.39 ? 69  ARG   C CG  1 
ATOM   1594 C  CD  . ARG   B 1 63  ? 23.778 -30.989 2.317  1.00 24.26 ? 69  ARG   C CD  1 
ATOM   1595 N  NE  . ARG   B 1 63  ? 22.798 -30.520 1.345  1.00 27.42 ? 69  ARG   C NE  1 
ATOM   1596 C  CZ  . ARG   B 1 63  ? 22.602 -29.248 1.033  1.00 28.04 ? 69  ARG   C CZ  1 
ATOM   1597 N  NH1 . ARG   B 1 63  ? 23.343 -28.293 1.591  1.00 26.91 ? 69  ARG   C NH1 1 
ATOM   1598 N  NH2 . ARG   B 1 63  ? 21.657 -28.914 0.172  1.00 28.29 ? 69  ARG   C NH2 1 
ATOM   1599 N  N   . LYS   B 1 64  ? 28.044 -32.115 5.532  1.00 13.51 ? 70  LYS   C N   1 
ATOM   1600 C  CA  . LYS   B 1 64  ? 28.855 -33.021 6.334  1.00 14.04 ? 70  LYS   C CA  1 
ATOM   1601 C  C   . LYS   B 1 64  ? 28.957 -32.554 7.750  1.00 12.83 ? 70  LYS   C C   1 
ATOM   1602 O  O   . LYS   B 1 64  ? 28.977 -31.336 8.012  1.00 12.76 ? 70  LYS   C O   1 
ATOM   1603 C  CB  . LYS   B 1 64  ? 30.267 -33.063 5.733  1.00 17.98 ? 70  LYS   C CB  1 
ATOM   1604 C  CG  . LYS   B 1 64  ? 30.400 -34.100 4.602  1.00 28.01 ? 70  LYS   C CG  1 
ATOM   1605 C  CD  . LYS   B 1 64  ? 31.851 -34.480 4.337  1.00 37.10 ? 70  LYS   C CD  1 
ATOM   1606 C  CE  . LYS   B 1 64  ? 31.952 -35.412 3.162  1.00 42.95 ? 70  LYS   C CE  1 
ATOM   1607 N  NZ  . LYS   B 1 64  ? 31.237 -34.879 1.974  1.00 46.92 ? 70  LYS   C NZ  1 
ATOM   1608 N  N   . HIS   B 1 65  ? 29.050 -33.508 8.655  1.00 11.63 ? 71  HIS   C N   1 
ATOM   1609 C  CA  . HIS   B 1 65  ? 29.358 -33.238 10.063 1.00 11.73 ? 71  HIS   C CA  1 
ATOM   1610 C  C   . HIS   B 1 65  ? 30.823 -33.525 10.266 1.00 12.85 ? 71  HIS   C C   1 
ATOM   1611 O  O   . HIS   B 1 65  ? 31.306 -34.624 9.940  1.00 15.80 ? 71  HIS   C O   1 
ATOM   1612 C  CB  . HIS   B 1 65  ? 28.531 -34.140 10.999 1.00 12.40 ? 71  HIS   C CB  1 
ATOM   1613 C  CG  . HIS   B 1 65  ? 27.065 -33.864 10.964 1.00 11.07 ? 71  HIS   C CG  1 
ATOM   1614 N  ND1 . HIS   B 1 65  ? 26.406 -33.092 11.916 1.00 13.80 ? 71  HIS   C ND1 1 
ATOM   1615 C  CD2 . HIS   B 1 65  ? 26.163 -34.270 10.041 1.00 11.36 ? 71  HIS   C CD2 1 
ATOM   1616 C  CE1 . HIS   B 1 65  ? 25.110 -33.104 11.571 1.00 11.72 ? 71  HIS   C CE1 1 
ATOM   1617 N  NE2 . HIS   B 1 65  ? 24.916 -33.798 10.474 1.00 14.69 ? 71  HIS   C NE2 1 
ATOM   1618 N  N   . TYR   B 1 66  ? 31.583 -32.560 10.819 1.00 11.07 ? 72  TYR   C N   1 
ATOM   1619 C  CA  . TYR   B 1 66  ? 33.032 -32.730 10.983 1.00 10.62 ? 72  TYR   C CA  1 
ATOM   1620 C  C   . TYR   B 1 66  ? 33.404 -32.770 12.470 1.00 10.30 ? 72  TYR   C C   1 
ATOM   1621 O  O   . TYR   B 1 66  ? 32.962 -31.904 13.236 1.00 10.08 ? 72  TYR   C O   1 
ATOM   1622 C  CB  . TYR   B 1 66  ? 33.761 -31.487 10.414 1.00 11.94 ? 72  TYR   C CB  1 
ATOM   1623 C  CG  . TYR   B 1 66  ? 33.733 -31.384 8.900  1.00 12.10 ? 72  TYR   C CG  1 
ATOM   1624 C  CD1 . TYR   B 1 66  ? 34.574 -32.154 8.121  1.00 14.43 ? 72  TYR   C CD1 1 
ATOM   1625 C  CD2 . TYR   B 1 66  ? 32.931 -30.447 8.255  1.00 13.20 ? 72  TYR   C CD2 1 
ATOM   1626 C  CE1 . TYR   B 1 66  ? 34.578 -32.043 6.730  1.00 15.47 ? 72  TYR   C CE1 1 
ATOM   1627 C  CE2 . TYR   B 1 66  ? 32.935 -30.314 6.870  1.00 14.25 ? 72  TYR   C CE2 1 
ATOM   1628 C  CZ  . TYR   B 1 66  ? 33.768 -31.111 6.118  1.00 15.11 ? 72  TYR   C CZ  1 
ATOM   1629 O  OH  . TYR   B 1 66  ? 33.752 -30.925 4.733  1.00 17.15 ? 72  TYR   C OH  1 
ATOM   1630 N  N   . PRO   B 1 67  ? 34.217 -33.750 12.875 1.00 10.48 ? 73  PRO   C N   1 
ATOM   1631 C  CA  . PRO   B 1 67  ? 34.758 -33.731 14.253 1.00 10.45 ? 73  PRO   C CA  1 
ATOM   1632 C  C   . PRO   B 1 67  ? 35.866 -32.666 14.359 1.00 11.18 ? 73  PRO   C C   1 
ATOM   1633 O  O   . PRO   B 1 67  ? 36.740 -32.596 13.465 1.00 13.55 ? 73  PRO   C O   1 
ATOM   1634 C  CB  . PRO   B 1 67  ? 35.353 -35.138 14.452 1.00 13.18 ? 73  PRO   C CB  1 
ATOM   1635 C  CG  . PRO   B 1 67  ? 35.572 -35.654 13.071 1.00 15.27 ? 73  PRO   C CG  1 
ATOM   1636 C  CD  . PRO   B 1 67  ? 34.705 -34.923 12.094 1.00 12.21 ? 73  PRO   C CD  1 
ATOM   1637 N  N   . VAL   B 1 68  ? 35.827 -31.860 15.393 1.00 9.96  ? 74  VAL   C N   1 
ATOM   1638 C  CA  . VAL   B 1 68  ? 36.798 -30.756 15.537 1.00 10.82 ? 74  VAL   C CA  1 
ATOM   1639 C  C   . VAL   B 1 68  ? 37.188 -30.591 16.982 1.00 10.17 ? 74  VAL   C C   1 
ATOM   1640 O  O   . VAL   B 1 68  ? 36.451 -30.876 17.921 1.00 10.37 ? 74  VAL   C O   1 
ATOM   1641 C  CB  . VAL   B 1 68  ? 36.197 -29.389 15.041 1.00 12.58 ? 74  VAL   C CB  1 
ATOM   1642 C  CG1 . VAL   B 1 68  ? 36.096 -29.336 13.502 1.00 14.66 ? 74  VAL   C CG1 1 
ATOM   1643 C  CG2 . VAL   B 1 68  ? 34.837 -29.088 15.724 1.00 14.02 ? 74  VAL   C CG2 1 
ATOM   1644 N  N   . SER   B 1 69  ? 38.415 -30.059 17.166 1.00 10.55 ? 75  SER   C N   1 
ATOM   1645 C  CA  . SER   B 1 69  ? 38.876 -29.406 18.401 1.00 10.67 ? 75  SER   C CA  1 
ATOM   1646 C  C   . SER   B 1 69  ? 38.560 -27.915 18.298 1.00 9.83  ? 75  SER   C C   1 
ATOM   1647 O  O   . SER   B 1 69  ? 38.699 -27.316 17.207 1.00 10.66 ? 75  SER   C O   1 
ATOM   1648 C  CB  . SER   B 1 69  ? 40.381 -29.576 18.569 1.00 12.55 ? 75  SER   C CB  1 
ATOM   1649 O  OG  . SER   B 1 69  ? 40.665 -30.948 18.721 1.00 18.12 ? 75  SER   C OG  1 
ATOM   1650 N  N   . PHE   B 1 70  ? 38.108 -27.309 19.375 1.00 9.97  ? 76  PHE   C N   1 
ATOM   1651 C  CA  . PHE   B 1 70  ? 37.735 -25.893 19.346 1.00 10.44 ? 76  PHE   C CA  1 
ATOM   1652 C  C   . PHE   B 1 70  ? 38.222 -25.152 20.594 1.00 10.50 ? 76  PHE   C C   1 
ATOM   1653 O  O   . PHE   B 1 70  ? 38.399 -25.777 21.658 1.00 10.87 ? 76  PHE   C O   1 
ATOM   1654 C  CB  . PHE   B 1 70  ? 36.215 -25.681 19.086 1.00 10.38 ? 76  PHE   C CB  1 
ATOM   1655 C  CG  . PHE   B 1 70  ? 35.316 -26.379 20.094 1.00 9.70  ? 76  PHE   C CG  1 
ATOM   1656 C  CD1 . PHE   B 1 70  ? 34.890 -27.679 19.882 1.00 10.42 ? 76  PHE   C CD1 1 
ATOM   1657 C  CD2 . PHE   B 1 70  ? 34.872 -25.718 21.224 1.00 10.92 ? 76  PHE   C CD2 1 
ATOM   1658 C  CE1 . PHE   B 1 70  ? 34.081 -28.321 20.814 1.00 10.09 ? 76  PHE   C CE1 1 
ATOM   1659 C  CE2 . PHE   B 1 70  ? 34.009 -26.357 22.137 1.00 10.75 ? 76  PHE   C CE2 1 
ATOM   1660 C  CZ  . PHE   B 1 70  ? 33.641 -27.653 21.932 1.00 10.83 ? 76  PHE   C CZ  1 
ATOM   1661 N  N   . SER   B 1 71  ? 38.481 -23.881 20.446 1.00 10.26 ? 77  SER   C N   1 
ATOM   1662 C  CA  . SER   B 1 71  ? 39.077 -23.097 21.518 1.00 11.61 ? 77  SER   C CA  1 
ATOM   1663 C  C   . SER   B 1 71  ? 38.087 -22.720 22.614 1.00 12.34 ? 77  SER   C C   1 
ATOM   1664 O  O   . SER   B 1 71  ? 36.887 -22.978 22.517 1.00 13.21 ? 77  SER   C O   1 
ATOM   1665 C  CB  . SER   B 1 71  ? 39.802 -21.876 20.938 1.00 11.63 ? 77  SER   C CB  1 
ATOM   1666 O  OG  . SER   B 1 71  ? 38.906 -20.966 20.304 1.00 13.70 ? 77  SER   C OG  1 
ATOM   1667 N  N   . LYS   B 1 72  ? 38.569 -22.092 23.672 1.00 13.47 ? 78  LYS   C N   1 
ATOM   1668 C  CA  . LYS   B 1 72  ? 37.698 -21.660 24.783 1.00 13.08 ? 78  LYS   C CA  1 
ATOM   1669 C  C   . LYS   B 1 72  ? 37.000 -20.344 24.389 1.00 13.22 ? 78  LYS   C C   1 
ATOM   1670 O  O   . LYS   B 1 72  ? 37.588 -19.527 23.679 1.00 14.90 ? 78  LYS   C O   1 
ATOM   1671 C  CB  . LYS   B 1 72  ? 38.575 -21.413 26.034 1.00 17.10 ? 78  LYS   C CB  1 
ATOM   1672 C  CG  . LYS   B 1 72  ? 39.231 -22.700 26.516 1.00 20.09 ? 78  LYS   C CG  1 
ATOM   1673 C  CD  . LYS   B 1 72  ? 39.768 -22.606 27.961 1.00 31.66 ? 78  LYS   C CD  1 
ATOM   1674 C  CE  . LYS   B 1 72  ? 39.978 -24.012 28.515 1.00 40.47 ? 78  LYS   C CE  1 
ATOM   1675 N  NZ  . LYS   B 1 72  ? 39.766 -24.093 29.993 1.00 44.69 ? 78  LYS   C NZ  1 
ATOM   1676 N  N   . PRO   B 1 73  ? 35.756 -20.105 24.849 1.00 12.47 ? 79  PRO   C N   1 
ATOM   1677 C  CA  . PRO   B 1 73  ? 35.033 -18.858 24.436 1.00 13.22 ? 79  PRO   C CA  1 
ATOM   1678 C  C   . PRO   B 1 73  ? 35.796 -17.606 24.800 1.00 13.53 ? 79  PRO   C C   1 
ATOM   1679 O  O   . PRO   B 1 73  ? 36.240 -17.471 25.967 1.00 15.63 ? 79  PRO   C O   1 
ATOM   1680 C  CB  . PRO   B 1 73  ? 33.711 -18.912 25.201 1.00 15.00 ? 79  PRO   C CB  1 
ATOM   1681 C  CG  . PRO   B 1 73  ? 33.558 -20.331 25.613 1.00 17.00 ? 79  PRO   C CG  1 
ATOM   1682 C  CD  . PRO   B 1 73  ? 34.947 -20.962 25.751 1.00 13.36 ? 79  PRO   C CD  1 
ATOM   1683 N  N   . SER   B 1 74  ? 36.051 -16.727 23.827 1.00 12.76 ? 80  SER   C N   1 
ATOM   1684 C  CA  . SER   B 1 74  ? 36.926 -15.572 24.049 1.00 14.30 ? 80  SER   C CA  1 
ATOM   1685 C  C   . SER   B 1 74  ? 36.525 -14.415 23.151 1.00 13.72 ? 80  SER   C C   1 
ATOM   1686 O  O   . SER   B 1 74  ? 35.659 -14.556 22.298 1.00 13.36 ? 80  SER   C O   1 
ATOM   1687 C  CB  . SER   B 1 74  ? 38.370 -15.945 23.695 1.00 17.84 ? 80  SER   C CB  1 
ATOM   1688 O  OG  . SER   B 1 74  ? 38.760 -17.155 24.322 1.00 24.62 ? 80  SER   C OG  1 
ATOM   1689 N  N   . LEU   B 1 75  ? 37.187 -13.279 23.342 1.00 14.51 ? 81  LEU   C N   1 
ATOM   1690 C  CA  . LEU   B 1 75  ? 37.005 -12.072 22.531 1.00 15.48 ? 81  LEU   C CA  1 
ATOM   1691 C  C   . LEU   B 1 75  ? 38.013 -12.143 21.361 1.00 15.80 ? 81  LEU   C C   1 
ATOM   1692 O  O   . LEU   B 1 75  ? 39.253 -12.098 21.606 1.00 18.25 ? 81  LEU   C O   1 
ATOM   1693 C  CB  . LEU   B 1 75  ? 37.268 -10.830 23.411 1.00 17.72 ? 81  LEU   C CB  1 
ATOM   1694 C  CG  . LEU   B 1 75  ? 36.989 -9.482  22.777 1.00 19.93 ? 81  LEU   C CG  1 
ATOM   1695 C  CD1 . LEU   B 1 75  ? 35.493 -9.274  22.562 1.00 19.47 ? 81  LEU   C CD1 1 
ATOM   1696 C  CD2 . LEU   B 1 75  ? 37.523 -8.362  23.701 1.00 22.18 ? 81  LEU   C CD2 1 
ATOM   1697 N  N   . ILE   B 1 76  ? 37.533 -12.372 20.135 1.00 16.37 ? 82  ILE   C N   1 
ATOM   1698 C  CA  . ILE   B 1 76  ? 38.367 -12.633 18.950 1.00 17.17 ? 82  ILE   C CA  1 
ATOM   1699 C  C   . ILE   B 1 76  ? 38.124 -11.580 17.891 1.00 16.89 ? 82  ILE   C C   1 
ATOM   1700 O  O   . ILE   B 1 76  ? 36.948 -11.216 17.652 1.00 16.10 ? 82  ILE   C O   1 
ATOM   1701 C  CB  . ILE   B 1 76  ? 37.985 -14.022 18.393 1.00 19.31 ? 82  ILE   C CB  1 
ATOM   1702 C  CG1 . ILE   B 1 76  ? 38.207 -15.156 19.434 1.00 22.20 ? 82  ILE   C CG1 1 
ATOM   1703 C  CG2 . ILE   B 1 76  ? 38.675 -14.339 17.026 1.00 20.81 ? 82  ILE   C CG2 1 
ATOM   1704 C  CD1 . ILE   B 1 76  ? 39.627 -15.830 19.500 1.00 24.07 ? 82  ILE   C CD1 1 
ATOM   1705 N  N   . PHE   B 1 77  ? 39.194 -11.095 17.229 1.00 16.92 ? 83  PHE   C N   1 
ATOM   1706 C  CA  . PHE   B 1 77  ? 39.012 -10.137 16.144 1.00 17.59 ? 83  PHE   C CA  1 
ATOM   1707 C  C   . PHE   B 1 77  ? 38.635 -10.976 14.898 1.00 18.08 ? 83  PHE   C C   1 
ATOM   1708 O  O   . PHE   B 1 77  ? 39.351 -11.924 14.521 1.00 20.80 ? 83  PHE   C O   1 
ATOM   1709 C  CB  . PHE   B 1 77  ? 40.320 -9.352  15.870 1.00 18.20 ? 83  PHE   C CB  1 
ATOM   1710 C  CG  . PHE   B 1 77  ? 40.051 -8.181  14.933 1.00 18.98 ? 83  PHE   C CG  1 
ATOM   1711 C  CD1 . PHE   B 1 77  ? 39.367 -7.069  15.369 1.00 20.43 ? 83  PHE   C CD1 1 
ATOM   1712 C  CD2 . PHE   B 1 77  ? 40.408 -8.240  13.587 1.00 21.21 ? 83  PHE   C CD2 1 
ATOM   1713 C  CE1 . PHE   B 1 77  ? 39.067 -6.014  14.498 1.00 21.87 ? 83  PHE   C CE1 1 
ATOM   1714 C  CE2 . PHE   B 1 77  ? 40.113 -7.176  12.722 1.00 21.54 ? 83  PHE   C CE2 1 
ATOM   1715 C  CZ  . PHE   B 1 77  ? 39.451 -6.072  13.183 1.00 21.90 ? 83  PHE   C CZ  1 
ATOM   1716 N  N   . VAL   B 1 78  ? 37.521 -10.611 14.250 1.00 15.29 ? 84  VAL   C N   1 
ATOM   1717 C  CA  . VAL   B 1 78  ? 36.986 -11.328 13.095 1.00 15.50 ? 84  VAL   C CA  1 
ATOM   1718 C  C   . VAL   B 1 78  ? 37.083 -10.381 11.888 1.00 14.81 ? 84  VAL   C C   1 
ATOM   1719 O  O   . VAL   B 1 78  ? 36.612 -9.247  11.985 1.00 15.43 ? 84  VAL   C O   1 
ATOM   1720 C  CB  . VAL   B 1 78  ? 35.503 -11.710 13.399 1.00 15.52 ? 84  VAL   C CB  1 
ATOM   1721 C  CG1 . VAL   B 1 78  ? 34.905 -12.469 12.224 1.00 16.15 ? 84  VAL   C CG1 1 
ATOM   1722 C  CG2 . VAL   B 1 78  ? 35.390 -12.526 14.693 1.00 15.93 ? 84  VAL   C CG2 1 
ATOM   1723 N  N   . GLU   B 1 79  ? 37.576 -10.847 10.739 1.00 13.95 ? 85  GLU   C N   1 
ATOM   1724 C  CA  . GLU   B 1 79  ? 37.606 -10.043 9.522  1.00 15.03 ? 85  GLU   C CA  1 
ATOM   1725 C  C   . GLU   B 1 79  ? 36.195 -9.780  8.995  1.00 14.48 ? 85  GLU   C C   1 
ATOM   1726 O  O   . GLU   B 1 79  ? 35.220 -10.455 9.377  1.00 14.07 ? 85  GLU   C O   1 
ATOM   1727 C  CB  . GLU   B 1 79  ? 38.451 -10.726 8.433  1.00 17.45 ? 85  GLU   C CB  1 
ATOM   1728 C  CG  . GLU   B 1 79  ? 39.937 -10.766 8.773  1.00 21.68 ? 85  GLU   C CG  1 
ATOM   1729 C  CD  . GLU   B 1 79  ? 40.549 -9.388  9.011  1.00 28.75 ? 85  GLU   C CD  1 
ATOM   1730 O  OE1 . GLU   B 1 79  ? 40.215 -8.426  8.276  1.00 33.54 ? 85  GLU   C OE1 1 
ATOM   1731 O  OE2 . GLU   B 1 79  ? 41.358 -9.255  9.958  1.00 31.27 ? 85  GLU   C OE2 1 
ATOM   1732 N  N   . ALA   B 1 80  ? 36.051 -8.761  8.138  1.00 15.44 ? 86  ALA   C N   1 
ATOM   1733 C  CA  . ALA   B 1 80  ? 34.753 -8.431  7.581  1.00 16.75 ? 86  ALA   C CA  1 
ATOM   1734 C  C   . ALA   B 1 80  ? 34.128 -9.618  6.872  1.00 17.41 ? 86  ALA   C C   1 
ATOM   1735 O  O   . ALA   B 1 80  ? 34.845 -10.400 6.235  1.00 19.15 ? 86  ALA   C O   1 
ATOM   1736 C  CB  . ALA   B 1 80  ? 34.925 -7.291  6.578  1.00 18.64 ? 86  ALA   C CB  1 
ATOM   1737 N  N   . SER   B 1 81  ? 32.824 -9.761  7.022  1.00 16.14 ? 87  SER   C N   1 
ATOM   1738 C  CA  . SER   B 1 81  ? 32.108 -10.792 6.314  1.00 16.94 ? 87  SER   C CA  1 
ATOM   1739 C  C   . SER   B 1 81  ? 30.993 -10.128 5.503  1.00 17.63 ? 87  SER   C C   1 
ATOM   1740 O  O   . SER   B 1 81  ? 30.846 -8.878  5.512  1.00 17.44 ? 87  SER   C O   1 
ATOM   1741 C  CB  . SER   B 1 81  ? 31.509 -11.787 7.317  1.00 15.63 ? 87  SER   C CB  1 
ATOM   1742 O  OG  . SER   B 1 81  ? 30.490 -11.113 8.053  1.00 16.05 ? 87  SER   C OG  1 
ATOM   1743 N  N   . GLU   B 1 82  ? 30.160 -10.945 4.877  1.00 18.84 ? 88  GLU   C N   1 
ATOM   1744 C  CA  . GLU   B 1 82  ? 29.037 -10.338 4.154  1.00 19.92 ? 88  GLU   C CA  1 
ATOM   1745 C  C   . GLU   B 1 82  ? 27.994 -9.681  5.084  1.00 19.57 ? 88  GLU   C C   1 
ATOM   1746 O  O   . GLU   B 1 82  ? 27.207 -8.840  4.629  1.00 21.72 ? 88  GLU   C O   1 
ATOM   1747 C  CB  . GLU   B 1 82  ? 28.415 -11.331 3.183  1.00 24.79 ? 88  GLU   C CB  1 
ATOM   1748 C  CG  . GLU   B 1 82  ? 27.571 -12.438 3.749  1.00 33.34 ? 88  GLU   C CG  1 
ATOM   1749 C  CD  . GLU   B 1 82  ? 26.890 -13.215 2.636  1.00 39.43 ? 88  GLU   C CD  1 
ATOM   1750 O  OE1 . GLU   B 1 82  ? 27.528 -13.407 1.574  1.00 39.79 ? 88  GLU   C OE1 1 
ATOM   1751 O  OE2 . GLU   B 1 82  ? 25.722 -13.628 2.826  1.00 41.44 ? 88  GLU   C OE2 1 
ATOM   1752 N  N   . TYR   B 1 83  ? 28.031 -9.987  6.390  1.00 16.34 ? 89  TYR   C N   1 
ATOM   1753 C  CA  . TYR   B 1 83  ? 27.013 -9.514  7.299  1.00 16.27 ? 89  TYR   C CA  1 
ATOM   1754 C  C   . TYR   B 1 83  ? 27.523 -8.669  8.495  1.00 17.41 ? 89  TYR   C C   1 
ATOM   1755 O  O   . TYR   B 1 83  ? 26.684 -8.106  9.197  1.00 18.51 ? 89  TYR   C O   1 
ATOM   1756 C  CB  . TYR   B 1 83  ? 26.145 -10.714 7.773  1.00 16.01 ? 89  TYR   C CB  1 
ATOM   1757 C  CG  . TYR   B 1 83  ? 26.958 -11.931 8.234  1.00 15.35 ? 89  TYR   C CG  1 
ATOM   1758 C  CD1 . TYR   B 1 83  ? 27.371 -12.915 7.330  1.00 16.17 ? 89  TYR   C CD1 1 
ATOM   1759 C  CD2 . TYR   B 1 83  ? 27.364 -12.061 9.553  1.00 15.14 ? 89  TYR   C CD2 1 
ATOM   1760 C  CE1 . TYR   B 1 83  ? 28.139 -14.012 7.739  1.00 15.65 ? 89  TYR   C CE1 1 
ATOM   1761 C  CE2 . TYR   B 1 83  ? 28.134 -13.140 9.972  1.00 15.30 ? 89  TYR   C CE2 1 
ATOM   1762 C  CZ  . TYR   B 1 83  ? 28.531 -14.118 9.059  1.00 14.76 ? 89  TYR   C CZ  1 
ATOM   1763 O  OH  . TYR   B 1 83  ? 29.341 -15.186 9.428  1.00 15.69 ? 89  TYR   C OH  1 
ATOM   1764 N  N   . TYR   B 1 84  ? 28.830 -8.539  8.755  1.00 15.45 ? 90  TYR   C N   1 
ATOM   1765 C  CA  . TYR   B 1 84  ? 29.383 -7.629  9.780  1.00 15.23 ? 90  TYR   C CA  1 
ATOM   1766 C  C   . TYR   B 1 84  ? 30.705 -7.025  9.250  1.00 14.80 ? 90  TYR   C C   1 
ATOM   1767 O  O   . TYR   B 1 84  ? 31.419 -7.676  8.492  1.00 15.00 ? 90  TYR   C O   1 
ATOM   1768 C  CB  . TYR   B 1 84  ? 29.744 -8.382  11.100 1.00 14.50 ? 90  TYR   C CB  1 
ATOM   1769 C  CG  . TYR   B 1 84  ? 28.555 -8.824  11.935 1.00 12.87 ? 90  TYR   C CG  1 
ATOM   1770 C  CD1 . TYR   B 1 84  ? 27.638 -7.897  12.454 1.00 14.00 ? 90  TYR   C CD1 1 
ATOM   1771 C  CD2 . TYR   B 1 84  ? 28.355 -10.149 12.217 1.00 12.92 ? 90  TYR   C CD2 1 
ATOM   1772 C  CE1 . TYR   B 1 84  ? 26.563 -8.304  13.255 1.00 13.87 ? 90  TYR   C CE1 1 
ATOM   1773 C  CE2 . TYR   B 1 84  ? 27.290 -10.571 13.018 1.00 12.65 ? 90  TYR   C CE2 1 
ATOM   1774 C  CZ  . TYR   B 1 84  ? 26.410 -9.646  13.552 1.00 13.08 ? 90  TYR   C CZ  1 
ATOM   1775 O  OH  . TYR   B 1 84  ? 25.325 -10.040 14.322 1.00 12.51 ? 90  TYR   C OH  1 
ATOM   1776 N  N   . PRO   B 1 85  ? 31.079 -5.823  9.715  1.00 15.08 ? 91  PRO   C N   1 
ATOM   1777 C  CA  . PRO   B 1 85  ? 32.436 -5.321  9.423  1.00 15.14 ? 91  PRO   C CA  1 
ATOM   1778 C  C   . PRO   B 1 85  ? 33.470 -6.107  10.245 1.00 15.16 ? 91  PRO   C C   1 
ATOM   1779 O  O   . PRO   B 1 85  ? 33.109 -6.924  11.146 1.00 15.01 ? 91  PRO   C O   1 
ATOM   1780 C  CB  . PRO   B 1 85  ? 32.347 -3.857  9.897  1.00 16.27 ? 91  PRO   C CB  1 
ATOM   1781 C  CG  . PRO   B 1 85  ? 31.416 -3.944  11.068 1.00 16.84 ? 91  PRO   C CG  1 
ATOM   1782 C  CD  . PRO   B 1 85  ? 30.352 -4.975  10.691 1.00 16.11 ? 91  PRO   C CD  1 
ATOM   1783 N  N   . ALA   B 1 86  ? 34.772 -5.849  9.999  1.00 14.73 ? 92  ALA   C N   1 
ATOM   1784 C  CA  . ALA   B 1 86  ? 35.831 -6.394  10.835 1.00 16.74 ? 92  ALA   C CA  1 
ATOM   1785 C  C   . ALA   B 1 86  ? 35.644 -5.840  12.251 1.00 17.19 ? 92  ALA   C C   1 
ATOM   1786 O  O   . ALA   B 1 86  ? 35.375 -4.625  12.413 1.00 18.95 ? 92  ALA   C O   1 
ATOM   1787 C  CB  . ALA   B 1 86  ? 37.183 -5.946  10.282 1.00 16.98 ? 92  ALA   C CB  1 
ATOM   1788 N  N   . ARG   B 1 87  ? 35.662 -6.728  13.248 1.00 16.12 ? 93  ARG   C N   1 
ATOM   1789 C  CA  . ARG   B 1 87  ? 35.361 -6.302  14.611 1.00 15.99 ? 93  ARG   C CA  1 
ATOM   1790 C  C   . ARG   B 1 87  ? 35.737 -7.386  15.606 1.00 15.78 ? 93  ARG   C C   1 
ATOM   1791 O  O   . ARG   B 1 87  ? 35.973 -8.532  15.219 1.00 15.23 ? 93  ARG   C O   1 
ATOM   1792 C  CB  . ARG   B 1 87  ? 33.847 -6.004  14.779 1.00 17.14 ? 93  ARG   C CB  1 
ATOM   1793 C  CG  . ARG   B 1 87  ? 33.010 -7.291  14.640 1.00 15.39 ? 93  ARG   C CG  1 
ATOM   1794 C  CD  . ARG   B 1 87  ? 31.532 -7.003  14.783 1.00 16.19 ? 93  ARG   C CD  1 
ATOM   1795 N  NE  . ARG   B 1 87  ? 30.804 -8.266  14.989 1.00 15.56 ? 93  ARG   C NE  1 
ATOM   1796 C  CZ  . ARG   B 1 87  ? 29.728 -8.426  15.746 1.00 15.89 ? 93  ARG   C CZ  1 
ATOM   1797 N  NH1 . ARG   B 1 87  ? 29.146 -7.373  16.328 1.00 16.25 ? 93  ARG   C NH1 1 
ATOM   1798 N  NH2 . ARG   B 1 87  ? 29.220 -9.642  15.933 1.00 16.68 ? 93  ARG   C NH2 1 
ATOM   1799 N  N   . TYR   B 1 88  ? 35.704 -7.030  16.919 1.00 16.52 ? 94  TYR   C N   1 
ATOM   1800 C  CA  . TYR   B 1 88  ? 35.849 -8.060  17.947 1.00 17.88 ? 94  TYR   C CA  1 
ATOM   1801 C  C   . TYR   B 1 88  ? 34.462 -8.675  18.215 1.00 15.83 ? 94  TYR   C C   1 
ATOM   1802 O  O   . TYR   B 1 88  ? 33.477 -7.954  18.381 1.00 17.41 ? 94  TYR   C O   1 
ATOM   1803 C  CB  . TYR   B 1 88  ? 36.341 -7.461  19.289 1.00 20.41 ? 94  TYR   C CB  1 
ATOM   1804 C  CG  . TYR   B 1 88  ? 37.810 -7.135  19.222 1.00 23.29 ? 94  TYR   C CG  1 
ATOM   1805 C  CD1 . TYR   B 1 88  ? 38.765 -8.115  19.422 1.00 24.87 ? 94  TYR   C CD1 1 
ATOM   1806 C  CD2 . TYR   B 1 88  ? 38.237 -5.850  18.894 1.00 25.29 ? 94  TYR   C CD2 1 
ATOM   1807 C  CE1 . TYR   B 1 88  ? 40.124 -7.817  19.323 1.00 26.55 ? 94  TYR   C CE1 1 
ATOM   1808 C  CE2 . TYR   B 1 88  ? 39.577 -5.543  18.790 1.00 27.26 ? 94  TYR   C CE2 1 
ATOM   1809 C  CZ  . TYR   B 1 88  ? 40.514 -6.525  18.992 1.00 28.32 ? 94  TYR   C CZ  1 
ATOM   1810 O  OH  . TYR   B 1 88  ? 41.821 -6.120  18.860 1.00 32.45 ? 94  TYR   C OH  1 
ATOM   1811 N  N   . GLN   B 1 89  ? 34.395 -9.999  18.268 1.00 14.67 ? 95  GLN   C N   1 
ATOM   1812 C  CA  . GLN   B 1 89  ? 33.183 -10.722 18.636 1.00 13.82 ? 95  GLN   C CA  1 
ATOM   1813 C  C   . GLN   B 1 89  ? 33.497 -11.439 19.941 1.00 13.41 ? 95  GLN   C C   1 
ATOM   1814 O  O   . GLN   B 1 89  ? 34.586 -12.041 20.090 1.00 14.05 ? 95  GLN   C O   1 
ATOM   1815 C  CB  . GLN   B 1 89  ? 32.818 -11.672 17.507 1.00 14.90 ? 95  GLN   C CB  1 
ATOM   1816 C  CG  . GLN   B 1 89  ? 31.540 -12.443 17.796 1.00 15.41 ? 95  GLN   C CG  1 
ATOM   1817 C  CD  . GLN   B 1 89  ? 30.833 -13.020 16.585 1.00 13.31 ? 95  GLN   C CD  1 
ATOM   1818 O  OE1 . GLN   B 1 89  ? 30.799 -12.425 15.479 1.00 14.24 ? 95  GLN   C OE1 1 
ATOM   1819 N  NE2 . GLN   B 1 89  ? 30.263 -14.181 16.801 1.00 13.66 ? 95  GLN   C NE2 1 
ATOM   1820 N  N   . SER   B 1 90  ? 32.580 -11.404 20.885 1.00 12.28 ? 96  SER   C N   1 
ATOM   1821 C  CA  . SER   B 1 90  ? 32.770 -12.016 22.186 1.00 12.91 ? 96  SER   C CA  1 
ATOM   1822 C  C   . SER   B 1 90  ? 32.167 -13.433 22.263 1.00 12.18 ? 96  SER   C C   1 
ATOM   1823 O  O   . SER   B 1 90  ? 31.322 -13.799 21.448 1.00 11.83 ? 96  SER   C O   1 
ATOM   1824 C  CB  . SER   B 1 90  ? 32.227 -11.122 23.310 1.00 14.22 ? 96  SER   C CB  1 
ATOM   1825 O  OG  . SER   B 1 90  ? 30.821 -11.080 23.198 1.00 14.65 ? 96  SER   C OG  1 
ATOM   1826 N  N   . HIS   B 1 91  ? 32.617 -14.214 23.255 1.00 12.19 ? 97  HIS   C N   1 
ATOM   1827 C  CA  . HIS   B 1 91  ? 32.121 -15.567 23.511 1.00 11.72 ? 97  HIS   C CA  1 
ATOM   1828 C  C   . HIS   B 1 91  ? 32.225 -16.452 22.240 1.00 11.41 ? 97  HIS   C C   1 
ATOM   1829 O  O   . HIS   B 1 91  ? 31.322 -17.271 22.003 1.00 12.20 ? 97  HIS   C O   1 
ATOM   1830 C  CB  . HIS   B 1 91  ? 30.681 -15.547 24.081 1.00 12.78 ? 97  HIS   C CB  1 
ATOM   1831 C  CG  . HIS   B 1 91  ? 30.547 -14.789 25.387 1.00 13.74 ? 97  HIS   C CG  1 
ATOM   1832 N  ND1 . HIS   B 1 91  ? 30.577 -15.439 26.599 1.00 16.32 ? 97  HIS   C ND1 1 
ATOM   1833 C  CD2 . HIS   B 1 91  ? 30.460 -13.444 25.618 1.00 14.16 ? 97  HIS   C CD2 1 
ATOM   1834 C  CE1 . HIS   B 1 91  ? 30.423 -14.501 27.534 1.00 16.29 ? 97  HIS   C CE1 1 
ATOM   1835 N  NE2 . HIS   B 1 91  ? 30.358 -13.283 26.998 1.00 16.28 ? 97  HIS   C NE2 1 
ATOM   1836 N  N   . LEU   B 1 92  ? 33.293 -16.297 21.500 1.00 10.77 ? 98  LEU   C N   1 
ATOM   1837 C  CA  . LEU   B 1 92  ? 33.506 -17.002 20.254 1.00 10.92 ? 98  LEU   C CA  1 
ATOM   1838 C  C   . LEU   B 1 92  ? 34.585 -18.055 20.441 1.00 10.96 ? 98  LEU   C C   1 
ATOM   1839 O  O   . LEU   B 1 92  ? 35.564 -17.848 21.160 1.00 11.47 ? 98  LEU   C O   1 
ATOM   1840 C  CB  . LEU   B 1 92  ? 33.968 -15.999 19.142 1.00 12.15 ? 98  LEU   C CB  1 
ATOM   1841 C  CG  . LEU   B 1 92  ? 34.064 -16.565 17.715 1.00 12.77 ? 98  LEU   C CG  1 
ATOM   1842 C  CD1 . LEU   B 1 92  ? 32.728 -16.887 17.158 1.00 13.73 ? 98  LEU   C CD1 1 
ATOM   1843 C  CD2 . LEU   B 1 92  ? 34.739 -15.561 16.751 1.00 15.44 ? 98  LEU   C CD2 1 
ATOM   1844 N  N   . MET   B 1 93  ? 34.407 -19.219 19.773 1.00 10.63 ? 99  MET   C N   1 
ATOM   1845 C  CA  . MET   B 1 93  ? 35.360 -20.344 19.822 1.00 9.56  ? 99  MET   C CA  1 
ATOM   1846 C  C   . MET   B 1 93  ? 35.760 -20.646 18.389 1.00 10.59 ? 99  MET   C C   1 
ATOM   1847 O  O   . MET   B 1 93  ? 34.874 -20.700 17.525 1.00 11.50 ? 99  MET   C O   1 
ATOM   1848 C  CB  . MET   B 1 93  ? 34.630 -21.576 20.395 1.00 11.43 ? 99  MET   C CB  1 
ATOM   1849 C  CG  . MET   B 1 93  ? 34.160 -21.324 21.820 1.00 12.68 ? 99  MET   C CG  1 
ATOM   1850 S  SD  . MET   B 1 93  ? 33.115 -22.637 22.465 1.00 13.53 ? 99  MET   C SD  1 
ATOM   1851 C  CE  . MET   B 1 93  ? 31.653 -22.508 21.378 1.00 14.47 ? 99  MET   C CE  1 
ATOM   1852 N  N   . LEU   B 1 94  ? 37.028 -20.926 18.123 1.00 10.33 ? 100 LEU   C N   1 
ATOM   1853 C  CA  . LEU   B 1 94  ? 37.471 -21.226 16.763 1.00 11.07 ? 100 LEU   C CA  1 
ATOM   1854 C  C   . LEU   B 1 94  ? 37.894 -22.684 16.633 1.00 10.19 ? 100 LEU   C C   1 
ATOM   1855 O  O   . LEU   B 1 94  ? 38.421 -23.272 17.573 1.00 11.89 ? 100 LEU   C O   1 
ATOM   1856 C  CB  . LEU   B 1 94  ? 38.722 -20.383 16.385 1.00 11.70 ? 100 LEU   C CB  1 
ATOM   1857 C  CG  . LEU   B 1 94  ? 38.551 -18.872 16.338 1.00 13.04 ? 100 LEU   C CG  1 
ATOM   1858 C  CD1 . LEU   B 1 94  ? 39.846 -18.222 15.884 1.00 16.68 ? 100 LEU   C CD1 1 
ATOM   1859 C  CD2 . LEU   B 1 94  ? 37.384 -18.426 15.430 1.00 14.73 ? 100 LEU   C CD2 1 
ATOM   1860 N  N   . ALA   B 1 95  ? 37.752 -23.207 15.422 1.00 10.80 ? 101 ALA   C N   1 
ATOM   1861 C  CA  . ALA   B 1 95  ? 38.276 -24.501 15.008 1.00 10.58 ? 101 ALA   C CA  1 
ATOM   1862 C  C   . ALA   B 1 95  ? 38.851 -24.366 13.585 1.00 11.01 ? 101 ALA   C C   1 
ATOM   1863 O  O   . ALA   B 1 95  ? 38.484 -23.439 12.855 1.00 10.41 ? 101 ALA   C O   1 
ATOM   1864 C  CB  . ALA   B 1 95  ? 37.178 -25.591 15.035 1.00 11.49 ? 101 ALA   C CB  1 
ATOM   1865 N  N   . VAL   B 1 96  ? 39.699 -25.307 13.186 1.00 11.00 ? 102 VAL   C N   1 
ATOM   1866 C  CA  . VAL   B 1 96  ? 40.168 -25.368 11.804 1.00 12.46 ? 102 VAL   C CA  1 
ATOM   1867 C  C   . VAL   B 1 96  ? 39.104 -26.119 10.998 1.00 12.07 ? 102 VAL   C C   1 
ATOM   1868 O  O   . VAL   B 1 96  ? 38.793 -27.297 11.287 1.00 13.54 ? 102 VAL   C O   1 
ATOM   1869 C  CB  . VAL   B 1 96  ? 41.539 -26.105 11.762 1.00 13.38 ? 102 VAL   C CB  1 
ATOM   1870 C  CG1 . VAL   B 1 96  ? 42.018 -26.280 10.315 1.00 15.02 ? 102 VAL   C CG1 1 
ATOM   1871 C  CG2 . VAL   B 1 96  ? 42.561 -25.325 12.574 1.00 14.61 ? 102 VAL   C CG2 1 
ATOM   1872 N  N   . GLY   B 1 97  ? 38.501 -25.430 10.043 1.00 12.89 ? 103 GLY   C N   1 
ATOM   1873 C  CA  . GLY   B 1 97  ? 37.441 -26.048 9.263  1.00 13.79 ? 103 GLY   C CA  1 
ATOM   1874 C  C   . GLY   B 1 97  ? 36.779 -25.081 8.338  1.00 13.07 ? 103 GLY   C C   1 
ATOM   1875 O  O   . GLY   B 1 97  ? 37.054 -23.860 8.353  1.00 15.63 ? 103 GLY   C O   1 
ATOM   1876 N  N   . HIS   B 1 98  ? 35.893 -25.607 7.496  1.00 13.36 ? 104 HIS   C N   1 
ATOM   1877 C  CA  . HIS   B 1 98  ? 35.209 -24.809 6.518  1.00 13.55 ? 104 HIS   C CA  1 
ATOM   1878 C  C   . HIS   B 1 98  ? 33.937 -24.129 7.050  1.00 12.99 ? 104 HIS   C C   1 
ATOM   1879 O  O   . HIS   B 1 98  ? 33.127 -24.765 7.762  1.00 12.61 ? 104 HIS   C O   1 
ATOM   1880 C  CB  . HIS   B 1 98  ? 34.881 -25.695 5.328  1.00 16.77 ? 104 HIS   C CB  1 
ATOM   1881 C  CG  . HIS   B 1 98  ? 34.347 -24.900 4.201  1.00 18.85 ? 104 HIS   C CG  1 
ATOM   1882 N  ND1 . HIS   B 1 98  ? 35.117 -23.925 3.555  1.00 20.79 ? 104 HIS   C ND1 1 
ATOM   1883 C  CD2 . HIS   B 1 98  ? 33.083 -24.857 3.722  1.00 20.90 ? 104 HIS   C CD2 1 
ATOM   1884 C  CE1 . HIS   B 1 98  ? 34.290 -23.337 2.702  1.00 23.24 ? 104 HIS   C CE1 1 
ATOM   1885 N  NE2 . HIS   B 1 98  ? 33.063 -23.872 2.755  1.00 24.05 ? 104 HIS   C NE2 1 
ATOM   1886 N  N   . SER   B 1 99  ? 33.715 -22.849 6.663  1.00 12.99 ? 105 SER   C N   1 
ATOM   1887 C  CA  . SER   B 1 99  ? 32.475 -22.120 7.055  1.00 13.73 ? 105 SER   C CA  1 
ATOM   1888 C  C   . SER   B 1 99  ? 32.216 -20.970 6.047  1.00 14.63 ? 105 SER   C C   1 
ATOM   1889 O  O   . SER   B 1 99  ? 33.078 -20.071 5.943  1.00 17.36 ? 105 SER   C O   1 
ATOM   1890 C  CB  . SER   B 1 99  ? 32.723 -21.527 8.445  1.00 15.31 ? 105 SER   C CB  1 
ATOM   1891 O  OG  . SER   B 1 99  ? 31.638 -20.681 8.812  1.00 15.59 ? 105 SER   C OG  1 
ATOM   1892 N  N   . GLU   B 1 100 ? 31.125 -21.043 5.306  1.00 15.19 ? 106 GLU   C N   1 
ATOM   1893 C  CA  . GLU   B 1 100 ? 30.634 -20.025 4.327  1.00 16.18 ? 106 GLU   C CA  1 
ATOM   1894 C  C   . GLU   B 1 100 ? 29.524 -19.276 5.088  1.00 14.14 ? 106 GLU   C C   1 
ATOM   1895 O  O   . GLU   B 1 100 ? 28.967 -19.766 6.071  1.00 13.16 ? 106 GLU   C O   1 
ATOM   1896 C  CB  . GLU   B 1 100 ? 29.910 -20.709 3.118  1.00 18.65 ? 106 GLU   C CB  1 
ATOM   1897 C  CG  . GLU   B 1 100 ? 30.572 -21.801 2.330  1.00 25.76 ? 106 GLU   C CG  1 
ATOM   1898 C  CD  . GLU   B 1 100 ? 31.458 -21.330 1.213  1.00 30.01 ? 106 GLU   C CD  1 
ATOM   1899 O  OE1 . GLU   B 1 100 ? 32.141 -22.188 0.620  1.00 29.79 ? 106 GLU   C OE1 1 
ATOM   1900 O  OE2 . GLU   B 1 100 ? 31.532 -20.099 0.983  1.00 30.61 ? 106 GLU   C OE2 1 
ATOM   1901 N  N   . PRO   B 1 101 ? 29.113 -18.086 4.594  1.00 14.64 ? 107 PRO   C N   1 
ATOM   1902 C  CA  . PRO   B 1 101 ? 28.012 -17.361 5.273  1.00 14.40 ? 107 PRO   C CA  1 
ATOM   1903 C  C   . PRO   B 1 101 ? 26.760 -18.225 5.450  1.00 14.25 ? 107 PRO   C C   1 
ATOM   1904 O  O   . PRO   B 1 101 ? 26.140 -18.162 6.529  1.00 14.38 ? 107 PRO   C O   1 
ATOM   1905 C  CB  . PRO   B 1 101 ? 27.742 -16.157 4.330  1.00 16.43 ? 107 PRO   C CB  1 
ATOM   1906 C  CG  . PRO   B 1 101 ? 28.985 -16.031 3.501  1.00 20.14 ? 107 PRO   C CG  1 
ATOM   1907 C  CD  . PRO   B 1 101 ? 29.746 -17.302 3.496  1.00 17.27 ? 107 PRO   C CD  1 
ATOM   1908 N  N   . GLY   B 1 102 ? 26.405 -19.061 4.469  1.00 13.54 ? 108 GLY   C N   1 
ATOM   1909 C  CA  . GLY   B 1 102 ? 25.193 -19.877 4.589  1.00 13.59 ? 108 GLY   C CA  1 
ATOM   1910 C  C   . GLY   B 1 102 ? 25.287 -20.974 5.641  1.00 12.42 ? 108 GLY   C C   1 
ATOM   1911 O  O   . GLY   B 1 102 ? 24.296 -21.659 5.947  1.00 13.98 ? 108 GLY   C O   1 
ATOM   1912 N  N   . ASP   B 1 103 ? 26.512 -21.248 6.155  1.00 11.67 ? 109 ASP   C N   1 
ATOM   1913 C  CA  . ASP   B 1 103 ? 26.677 -22.260 7.192  1.00 10.94 ? 109 ASP   C CA  1 
ATOM   1914 C  C   . ASP   B 1 103 ? 26.302 -21.776 8.586  1.00 11.22 ? 109 ASP   C C   1 
ATOM   1915 O  O   . ASP   B 1 103 ? 26.198 -22.577 9.528  1.00 11.01 ? 109 ASP   C O   1 
ATOM   1916 C  CB  . ASP   B 1 103 ? 28.150 -22.729 7.208  1.00 12.71 ? 109 ASP   C CB  1 
ATOM   1917 C  CG  . ASP   B 1 103 ? 28.463 -23.550 5.993  1.00 13.50 ? 109 ASP   C CG  1 
ATOM   1918 O  OD1 . ASP   B 1 103 ? 27.603 -24.297 5.558  1.00 14.26 ? 109 ASP   C OD1 1 
ATOM   1919 O  OD2 . ASP   B 1 103 ? 29.596 -23.400 5.434  1.00 14.63 ? 109 ASP   C OD2 1 
ATOM   1920 N  N   . CYS   B 1 104 ? 26.118 -20.435 8.776  1.00 10.77 ? 110 CYS   C N   1 
ATOM   1921 C  CA  . CYS   B 1 104 ? 25.717 -19.898 10.083 1.00 10.82 ? 110 CYS   C CA  1 
ATOM   1922 C  C   . CYS   B 1 104 ? 24.467 -20.612 10.572 1.00 10.84 ? 110 CYS   C C   1 
ATOM   1923 O  O   . CYS   B 1 104 ? 23.512 -20.811 9.802  1.00 11.84 ? 110 CYS   C O   1 
ATOM   1924 C  CB  . CYS   B 1 104 ? 25.487 -18.389 10.014 1.00 11.65 ? 110 CYS   C CB  1 
ATOM   1925 S  SG  . CYS   B 1 104 ? 27.002 -17.417 9.883  1.00 12.79 ? 110 CYS   C SG  1 
ATOM   1926 N  N   . GLY   B 1 105 ? 24.453 -20.935 11.842 1.00 9.25  ? 111 GLY   C N   1 
ATOM   1927 C  CA  . GLY   B 1 105 ? 23.322 -21.628 12.468 1.00 10.81 ? 111 GLY   C CA  1 
ATOM   1928 C  C   . GLY   B 1 105 ? 23.543 -23.126 12.629 1.00 10.40 ? 111 GLY   C C   1 
ATOM   1929 O  O   . GLY   B 1 105 ? 22.767 -23.785 13.350 1.00 11.17 ? 111 GLY   C O   1 
ATOM   1930 N  N   . GLY   B 1 106 ? 24.554 -23.696 11.957 1.00 10.68 ? 112 GLY   C N   1 
ATOM   1931 C  CA  . GLY   B 1 106 ? 24.871 -25.129 12.118 1.00 11.11 ? 112 GLY   C CA  1 
ATOM   1932 C  C   . GLY   B 1 106 ? 25.257 -25.419 13.565 1.00 9.67  ? 112 GLY   C C   1 
ATOM   1933 O  O   . GLY   B 1 106 ? 25.979 -24.627 14.191 1.00 10.29 ? 112 GLY   C O   1 
ATOM   1934 N  N   . ILE   B 1 107 ? 24.813 -26.559 14.081 1.00 9.36  ? 113 ILE   C N   1 
ATOM   1935 C  CA  . ILE   B 1 107 ? 25.086 -26.866 15.492 1.00 9.41  ? 113 ILE   C CA  1 
ATOM   1936 C  C   . ILE   B 1 107 ? 26.459 -27.499 15.671 1.00 9.45  ? 113 ILE   C C   1 
ATOM   1937 O  O   . ILE   B 1 107 ? 26.895 -28.357 14.893 1.00 9.59  ? 113 ILE   C O   1 
ATOM   1938 C  CB  . ILE   B 1 107 ? 23.970 -27.834 16.019 1.00 11.89 ? 113 ILE   C CB  1 
ATOM   1939 C  CG1 . ILE   B 1 107 ? 22.733 -26.897 16.434 1.00 15.82 ? 113 ILE   C CG1 1 
ATOM   1940 C  CG2 . ILE   B 1 107 ? 24.423 -28.675 17.232 1.00 12.00 ? 113 ILE   C CG2 1 
ATOM   1941 C  CD1 . ILE   B 1 107 ? 21.422 -27.653 16.807 1.00 19.97 ? 113 ILE   C CD1 1 
ATOM   1942 N  N   . LEU   B 1 108 ? 27.141 -27.063 16.775 1.00 8.89  ? 114 LEU   C N   1 
ATOM   1943 C  CA  . LEU   B 1 108 ? 28.317 -27.737 17.326 1.00 9.22  ? 114 LEU   C CA  1 
ATOM   1944 C  C   . LEU   B 1 108 ? 27.810 -28.491 18.575 1.00 9.06  ? 114 LEU   C C   1 
ATOM   1945 O  O   . LEU   B 1 108 ? 27.184 -27.901 19.457 1.00 9.13  ? 114 LEU   C O   1 
ATOM   1946 C  CB  . LEU   B 1 108 ? 29.369 -26.681 17.740 1.00 8.76  ? 114 LEU   C CB  1 
ATOM   1947 C  CG  . LEU   B 1 108 ? 30.583 -27.181 18.520 1.00 9.46  ? 114 LEU   C CG  1 
ATOM   1948 C  CD1 . LEU   B 1 108 ? 31.457 -28.120 17.668 1.00 10.88 ? 114 LEU   C CD1 1 
ATOM   1949 C  CD2 . LEU   B 1 108 ? 31.392 -26.007 19.031 1.00 10.34 ? 114 LEU   C CD2 1 
ATOM   1950 N  N   . ARG   B 1 109 ? 28.112 -29.792 18.645 1.00 9.27  ? 115 ARG   C N   1 
ATOM   1951 C  CA  . ARG   B 1 109 ? 27.658 -30.624 19.791 1.00 9.57  ? 115 ARG   C CA  1 
ATOM   1952 C  C   . ARG   B 1 109 ? 28.790 -31.459 20.357 1.00 9.86  ? 115 ARG   C C   1 
ATOM   1953 O  O   . ARG   B 1 109 ? 29.702 -31.876 19.642 1.00 10.64 ? 115 ARG   C O   1 
ATOM   1954 C  CB  . ARG   B 1 109 ? 26.500 -31.537 19.333 1.00 12.60 ? 115 ARG   C CB  1 
ATOM   1955 C  CG  . ARG   B 1 109 ? 26.911 -32.534 18.301 1.00 16.57 ? 115 ARG   C CG  1 
ATOM   1956 C  CD  . ARG   B 1 109 ? 25.739 -33.423 17.851 1.00 21.24 ? 115 ARG   C CD  1 
ATOM   1957 N  NE  . ARG   B 1 109 ? 24.802 -32.706 16.976 1.00 28.50 ? 115 ARG   C NE  1 
ATOM   1958 C  CZ  . ARG   B 1 109 ? 23.538 -32.402 17.289 1.00 38.22 ? 115 ARG   C CZ  1 
ATOM   1959 N  NH1 . ARG   B 1 109 ? 23.065 -32.656 18.511 1.00 40.60 ? 115 ARG   C NH1 1 
ATOM   1960 N  NH2 . ARG   B 1 109 ? 22.767 -31.761 16.416 1.00 40.44 ? 115 ARG   C NH2 1 
ATOM   1961 N  N   . CYS   B 1 110 ? 28.698 -31.700 21.653 1.00 10.28 ? 116 CYS   C N   1 
ATOM   1962 C  CA  . CYS   B 1 110 ? 29.661 -32.575 22.374 1.00 10.46 ? 116 CYS   C CA  1 
ATOM   1963 C  C   . CYS   B 1 110 ? 28.810 -33.683 23.050 1.00 12.37 ? 116 CYS   C C   1 
ATOM   1964 O  O   . CYS   B 1 110 ? 27.579 -33.771 22.845 1.00 12.21 ? 116 CYS   C O   1 
ATOM   1965 C  CB  . CYS   B 1 110 ? 30.459 -31.766 23.391 1.00 10.30 ? 116 CYS   C CB  1 
ATOM   1966 S  SG  . CYS   B 1 110 ? 29.441 -31.129 24.748 1.00 10.62 ? 116 CYS   C SG  1 
ATOM   1967 N  N   . GLN   B 1 111 ? 29.458 -34.543 23.898 1.00 13.42 ? 117 GLN   C N   1 
ATOM   1968 C  CA  . GLN   B 1 111 ? 28.678 -35.567 24.579 1.00 14.54 ? 117 GLN   C CA  1 
ATOM   1969 C  C   . GLN   B 1 111 ? 27.614 -34.998 25.509 1.00 14.33 ? 117 GLN   C C   1 
ATOM   1970 O  O   . GLN   B 1 111 ? 26.651 -35.719 25.852 1.00 15.98 ? 117 GLN   C O   1 
ATOM   1971 C  CB  . GLN   B 1 111 ? 29.609 -36.513 25.402 1.00 16.07 ? 117 GLN   C CB  1 
ATOM   1972 C  CG  . GLN   B 1 111 ? 30.316 -35.811 26.570 1.00 18.67 ? 117 GLN   C CG  1 
ATOM   1973 C  CD  . GLN   B 1 111 ? 31.255 -36.704 27.349 1.00 29.59 ? 117 GLN   C CD  1 
ATOM   1974 O  OE1 . GLN   B 1 111 ? 32.471 -36.708 27.110 1.00 32.68 ? 117 GLN   C OE1 1 
ATOM   1975 N  NE2 . GLN   B 1 111 ? 30.708 -37.418 28.317 1.00 30.41 ? 117 GLN   C NE2 1 
ATOM   1976 N  N   . HIS   B 1 112 ? 27.720 -33.723 25.921 1.00 12.34 ? 118 HIS   C N   1 
ATOM   1977 C  CA  . HIS   B 1 112 ? 26.746 -33.154 26.856 1.00 12.54 ? 118 HIS   C CA  1 
ATOM   1978 C  C   . HIS   B 1 112 ? 25.545 -32.452 26.187 1.00 13.16 ? 118 HIS   C C   1 
ATOM   1979 O  O   . HIS   B 1 112 ? 24.606 -32.047 26.879 1.00 14.29 ? 118 HIS   C O   1 
ATOM   1980 C  CB  . HIS   B 1 112 ? 27.446 -32.176 27.788 1.00 13.95 ? 118 HIS   C CB  1 
ATOM   1981 C  CG  . HIS   B 1 112 ? 28.618 -32.801 28.489 1.00 12.59 ? 118 HIS   C CG  1 
ATOM   1982 N  ND1 . HIS   B 1 112 ? 29.933 -32.514 28.133 1.00 11.56 ? 118 HIS   C ND1 1 
ATOM   1983 C  CD2 . HIS   B 1 112 ? 28.635 -33.617 29.575 1.00 15.56 ? 118 HIS   C CD2 1 
ATOM   1984 C  CE1 . HIS   B 1 112 ? 30.704 -33.227 28.938 1.00 14.27 ? 118 HIS   C CE1 1 
ATOM   1985 N  NE2 . HIS   B 1 112 ? 29.960 -33.883 29.840 1.00 16.38 ? 118 HIS   C NE2 1 
ATOM   1986 N  N   . GLY   B 1 113 ? 25.613 -32.203 24.882 1.00 11.70 ? 119 GLY   C N   1 
ATOM   1987 C  CA  . GLY   B 1 113 ? 24.541 -31.523 24.166 1.00 11.67 ? 119 GLY   C CA  1 
ATOM   1988 C  C   . GLY   B 1 113 ? 25.085 -30.466 23.224 1.00 10.64 ? 119 GLY   C C   1 
ATOM   1989 O  O   . GLY   B 1 113 ? 26.218 -30.563 22.717 1.00 10.24 ? 119 GLY   C O   1 
ATOM   1990 N  N   . VAL   B 1 114 ? 24.241 -29.449 22.957 1.00 10.50 ? 120 VAL   C N   1 
ATOM   1991 C  CA  . VAL   B 1 114 ? 24.581 -28.376 22.006 1.00 10.75 ? 120 VAL   C CA  1 
ATOM   1992 C  C   . VAL   B 1 114 ? 25.501 -27.365 22.685 1.00 10.15 ? 120 VAL   C C   1 
ATOM   1993 O  O   . VAL   B 1 114 ? 25.193 -26.818 23.762 1.00 10.59 ? 120 VAL   C O   1 
ATOM   1994 C  CB  . VAL   B 1 114 ? 23.283 -27.686 21.533 1.00 11.66 ? 120 VAL   C CB  1 
ATOM   1995 C  CG1 . VAL   B 1 114 ? 23.637 -26.472 20.662 1.00 12.68 ? 120 VAL   C CG1 1 
ATOM   1996 C  CG2 . VAL   B 1 114 ? 22.374 -28.671 20.788 1.00 12.98 ? 120 VAL   C CG2 1 
ATOM   1997 N  N   . VAL   B 1 115 ? 26.661 -27.135 22.077 1.00 9.07  ? 121 VAL   C N   1 
ATOM   1998 C  CA  . VAL   B 1 115 ? 27.676 -26.194 22.567 1.00 9.29  ? 121 VAL   C CA  1 
ATOM   1999 C  C   . VAL   B 1 115 ? 27.428 -24.778 22.073 1.00 9.83  ? 121 VAL   C C   1 
ATOM   2000 O  O   . VAL   B 1 115 ? 27.694 -23.789 22.783 1.00 10.47 ? 121 VAL   C O   1 
ATOM   2001 C  CB  . VAL   B 1 115 ? 29.073 -26.718 22.166 1.00 8.94  ? 121 VAL   C CB  1 
ATOM   2002 C  CG1 . VAL   B 1 115 ? 30.142 -25.716 22.545 1.00 11.33 ? 121 VAL   C CG1 1 
ATOM   2003 C  CG2 . VAL   B 1 115 ? 29.358 -28.082 22.783 1.00 11.25 ? 121 VAL   C CG2 1 
ATOM   2004 N  N   . GLY   B 1 116 ? 27.082 -24.679 20.792 1.00 9.49  ? 122 GLY   C N   1 
ATOM   2005 C  CA  . GLY   B 1 116 ? 26.875 -23.371 20.182 1.00 10.84 ? 122 GLY   C CA  1 
ATOM   2006 C  C   . GLY   B 1 116 ? 26.533 -23.549 18.706 1.00 9.64  ? 122 GLY   C C   1 
ATOM   2007 O  O   . GLY   B 1 116 ? 26.218 -24.669 18.269 1.00 9.96  ? 122 GLY   C O   1 
ATOM   2008 N  N   . ILE   B 1 117 ? 26.520 -22.408 17.960 1.00 9.43  ? 123 ILE   C N   1 
ATOM   2009 C  CA  . ILE   B 1 117 ? 26.160 -22.433 16.544 1.00 9.38  ? 123 ILE   C CA  1 
ATOM   2010 C  C   . ILE   B 1 117 ? 27.219 -21.692 15.740 1.00 9.17  ? 123 ILE   C C   1 
ATOM   2011 O  O   . ILE   B 1 117 ? 27.855 -20.728 16.208 1.00 10.39 ? 123 ILE   C O   1 
ATOM   2012 C  CB  . ILE   B 1 117 ? 24.757 -21.791 16.265 1.00 9.96  ? 123 ILE   C CB  1 
ATOM   2013 C  CG1 . ILE   B 1 117 ? 24.649 -20.385 16.906 1.00 11.72 ? 123 ILE   C CG1 1 
ATOM   2014 C  CG2 . ILE   B 1 117 ? 23.641 -22.736 16.724 1.00 12.01 ? 123 ILE   C CG2 1 
ATOM   2015 C  CD1 . ILE   B 1 117 ? 23.304 -19.585 16.493 1.00 12.19 ? 123 ILE   C CD1 1 
ATOM   2016 N  N   . VAL   B 1 118 ? 27.398 -22.117 14.480 1.00 9.19  ? 124 VAL   C N   1 
ATOM   2017 C  CA  . VAL   B 1 118 ? 28.309 -21.431 13.561 1.00 9.56  ? 124 VAL   C CA  1 
ATOM   2018 C  C   . VAL   B 1 118 ? 27.933 -19.955 13.441 1.00 9.57  ? 124 VAL   C C   1 
ATOM   2019 O  O   . VAL   B 1 118 ? 26.739 -19.627 13.226 1.00 9.45  ? 124 VAL   C O   1 
ATOM   2020 C  CB  . VAL   B 1 118 ? 28.303 -22.099 12.168 1.00 9.18  ? 124 VAL   C CB  1 
ATOM   2021 C  CG1 . VAL   B 1 118 ? 29.165 -21.344 11.162 1.00 10.77 ? 124 VAL   C CG1 1 
ATOM   2022 C  CG2 . VAL   B 1 118 ? 28.768 -23.556 12.233 1.00 10.39 ? 124 VAL   C CG2 1 
ATOM   2023 N  N   . SER   B 1 119 ? 28.959 -19.078 13.541 1.00 9.34  ? 125 SER   C N   1 
ATOM   2024 C  CA  . SER   B 1 119 ? 28.766 -17.626 13.412 1.00 9.47  ? 125 SER   C CA  1 
ATOM   2025 C  C   . SER   B 1 119 ? 29.775 -16.954 12.514 1.00 10.79 ? 125 SER   C C   1 
ATOM   2026 O  O   . SER   B 1 119 ? 29.432 -15.882 11.964 1.00 10.97 ? 125 SER   C O   1 
ATOM   2027 C  CB  . SER   B 1 119 ? 28.780 -17.029 14.817 1.00 10.87 ? 125 SER   C CB  1 
ATOM   2028 O  OG  . SER   B 1 119 ? 28.681 -15.594 14.798 1.00 12.19 ? 125 SER   C OG  1 
ATOM   2029 N  N   . THR   B 1 120 ? 31.026 -17.495 12.386 1.00 10.75 ? 126 THR   C N   1 
ATOM   2030 C  CA  . THR   B 1 120 ? 32.035 -16.791 11.578 1.00 11.09 ? 126 THR   C CA  1 
ATOM   2031 C  C   . THR   B 1 120 ? 32.743 -17.813 10.688 1.00 10.38 ? 126 THR   C C   1 
ATOM   2032 O  O   . THR   B 1 120 ? 32.679 -19.043 10.909 1.00 10.38 ? 126 THR   C O   1 
ATOM   2033 C  CB  . THR   B 1 120 ? 33.112 -16.060 12.460 1.00 11.23 ? 126 THR   C CB  1 
ATOM   2034 O  OG1 . THR   B 1 120 ? 33.948 -17.036 13.115 1.00 12.05 ? 126 THR   C OG1 1 
ATOM   2035 C  CG2 . THR   B 1 120 ? 32.498 -15.136 13.453 1.00 12.53 ? 126 THR   C CG2 1 
ATOM   2036 N  N   . GLY   B 1 121 ? 33.433 -17.316 9.693  1.00 11.26 ? 127 GLY   C N   1 
ATOM   2037 C  CA  . GLY   B 1 121 ? 34.244 -18.158 8.818  1.00 13.29 ? 127 GLY   C CA  1 
ATOM   2038 C  C   . GLY   B 1 121 ? 35.264 -17.323 8.062  1.00 15.72 ? 127 GLY   C C   1 
ATOM   2039 O  O   . GLY   B 1 121 ? 35.002 -16.190 7.687  1.00 18.56 ? 127 GLY   C O   1 
ATOM   2040 N  N   . GLY   B 1 122 ? 36.408 -17.885 7.781  1.00 19.37 ? 128 GLY   C N   1 
ATOM   2041 C  CA  . GLY   B 1 122 ? 37.457 -17.167 7.056  1.00 21.45 ? 128 GLY   C CA  1 
ATOM   2042 C  C   . GLY   B 1 122 ? 38.797 -17.724 7.395  1.00 21.21 ? 128 GLY   C C   1 
ATOM   2043 O  O   . GLY   B 1 122 ? 39.010 -18.203 8.497  1.00 21.42 ? 128 GLY   C O   1 
ATOM   2044 N  N   . ASN   B 1 123 ? 39.748 -17.589 6.450  1.00 19.87 ? 129 ASN   C N   1 
ATOM   2045 C  CA  . ASN   B 1 123 ? 41.142 -18.006 6.639  1.00 20.15 ? 129 ASN   C CA  1 
ATOM   2046 C  C   . ASN   B 1 123 ? 41.220 -19.466 7.039  1.00 18.39 ? 129 ASN   C C   1 
ATOM   2047 O  O   . ASN   B 1 123 ? 42.153 -19.828 7.759  1.00 21.62 ? 129 ASN   C O   1 
ATOM   2048 C  CB  . ASN   B 1 123 ? 41.909 -17.094 7.686  1.00 23.92 ? 129 ASN   C CB  1 
ATOM   2049 C  CG  . ASN   B 1 123 ? 42.741 -15.964 7.091  1.00 29.99 ? 129 ASN   C CG  1 
ATOM   2050 O  OD1 . ASN   B 1 123 ? 43.167 -16.015 5.929  1.00 31.20 ? 129 ASN   C OD1 1 
ATOM   2051 N  ND2 . ASN   B 1 123 ? 43.005 -14.896 7.868  1.00 32.09 ? 129 ASN   C ND2 1 
ATOM   2052 N  N   . GLY   B 1 124 ? 40.276 -20.319 6.585  1.00 16.65 ? 130 GLY   C N   1 
ATOM   2053 C  CA  . GLY   B 1 124 ? 40.287 -21.745 6.955  1.00 16.02 ? 130 GLY   C CA  1 
ATOM   2054 C  C   . GLY   B 1 124 ? 39.899 -22.050 8.393  1.00 13.99 ? 130 GLY   C C   1 
ATOM   2055 O  O   . GLY   B 1 124 ? 40.164 -23.151 8.899  1.00 14.53 ? 130 GLY   C O   1 
ATOM   2056 N  N   . LEU   B 1 125 ? 39.256 -21.105 9.032  1.00 12.53 ? 131 LEU   C N   1 
ATOM   2057 C  CA  . LEU   B 1 125 ? 38.779 -21.241 10.400 1.00 12.26 ? 131 LEU   C CA  1 
ATOM   2058 C  C   . LEU   B 1 125 ? 37.259 -21.115 10.426 1.00 12.73 ? 131 LEU   C C   1 
ATOM   2059 O  O   . LEU   B 1 125 ? 36.633 -20.442 9.582  1.00 15.58 ? 131 LEU   C O   1 
ATOM   2060 C  CB  . LEU   B 1 125 ? 39.400 -20.146 11.273 1.00 14.31 ? 131 LEU   C CB  1 
ATOM   2061 C  CG  . LEU   B 1 125 ? 40.938 -20.188 11.359 1.00 17.26 ? 131 LEU   C CG  1 
ATOM   2062 C  CD1 . LEU   B 1 125 ? 41.545 -18.838 11.766 1.00 21.15 ? 131 LEU   C CD1 1 
ATOM   2063 C  CD2 . LEU   B 1 125 ? 41.447 -21.324 12.197 1.00 18.29 ? 131 LEU   C CD2 1 
ATOM   2064 N  N   . VAL   B 1 126 ? 36.645 -21.784 11.366 1.00 10.65 ? 132 VAL   C N   1 
ATOM   2065 C  CA  . VAL   B 1 126 ? 35.191 -21.674 11.614 1.00 10.09 ? 132 VAL   C CA  1 
ATOM   2066 C  C   . VAL   B 1 126 ? 35.036 -21.212 13.062 1.00 9.63  ? 132 VAL   C C   1 
ATOM   2067 O  O   . VAL   B 1 126 ? 35.700 -21.739 13.963 1.00 10.60 ? 132 VAL   C O   1 
ATOM   2068 C  CB  . VAL   B 1 126 ? 34.453 -23.012 11.367 1.00 10.19 ? 132 VAL   C CB  1 
ATOM   2069 C  CG1 . VAL   B 1 126 ? 35.068 -24.208 12.052 1.00 12.52 ? 132 VAL   C CG1 1 
ATOM   2070 C  CG2 . VAL   B 1 126 ? 32.943 -22.909 11.670 1.00 11.38 ? 132 VAL   C CG2 1 
ATOM   2071 N  N   . GLY   B 1 127 ? 34.157 -20.233 13.261 1.00 9.58  ? 133 GLY   C N   1 
ATOM   2072 C  CA  . GLY   B 1 127 ? 33.909 -19.734 14.607 1.00 9.52  ? 133 GLY   C CA  1 
ATOM   2073 C  C   . GLY   B 1 127 ? 32.488 -20.066 15.034 1.00 9.86  ? 133 GLY   C C   1 
ATOM   2074 O  O   . GLY   B 1 127 ? 31.531 -19.927 14.245 1.00 10.16 ? 133 GLY   C O   1 
ATOM   2075 N  N   . PHE   B 1 128 ? 32.351 -20.414 16.312 1.00 9.02  ? 134 PHE   C N   1 
ATOM   2076 C  CA  . PHE   B 1 128 ? 31.069 -20.801 16.940 1.00 9.28  ? 134 PHE   C CA  1 
ATOM   2077 C  C   . PHE   B 1 128 ? 30.729 -19.861 18.080 1.00 9.17  ? 134 PHE   C C   1 
ATOM   2078 O  O   . PHE   B 1 128 ? 31.584 -19.600 18.947 1.00 10.04 ? 134 PHE   C O   1 
ATOM   2079 C  CB  . PHE   B 1 128 ? 31.130 -22.236 17.515 1.00 9.54  ? 134 PHE   C CB  1 
ATOM   2080 C  CG  . PHE   B 1 128 ? 31.655 -23.250 16.519 1.00 9.52  ? 134 PHE   C CG  1 
ATOM   2081 C  CD1 . PHE   B 1 128 ? 30.809 -23.840 15.577 1.00 9.74  ? 134 PHE   C CD1 1 
ATOM   2082 C  CD2 . PHE   B 1 128 ? 33.001 -23.627 16.524 1.00 10.12 ? 134 PHE   C CD2 1 
ATOM   2083 C  CE1 . PHE   B 1 128 ? 31.307 -24.803 14.690 1.00 10.11 ? 134 PHE   C CE1 1 
ATOM   2084 C  CE2 . PHE   B 1 128 ? 33.500 -24.581 15.617 1.00 10.34 ? 134 PHE   C CE2 1 
ATOM   2085 C  CZ  . PHE   B 1 128 ? 32.652 -25.161 14.722 1.00 10.43 ? 134 PHE   C CZ  1 
ATOM   2086 N  N   . ALA   B 1 129 ? 29.480 -19.366 18.088 1.00 9.55  ? 135 ALA   C N   1 
ATOM   2087 C  CA  . ALA   B 1 129 ? 28.992 -18.557 19.207 1.00 9.35  ? 135 ALA   C CA  1 
ATOM   2088 C  C   . ALA   B 1 129 ? 28.605 -19.544 20.344 1.00 10.16 ? 135 ALA   C C   1 
ATOM   2089 O  O   . ALA   B 1 129 ? 27.697 -20.381 20.178 1.00 10.35 ? 135 ALA   C O   1 
ATOM   2090 C  CB  . ALA   B 1 129 ? 27.769 -17.750 18.764 1.00 10.38 ? 135 ALA   C CB  1 
ATOM   2091 N  N   . ASP   B 1 130 ? 29.294 -19.470 21.485 1.00 9.77  ? 136 ASP   C N   1 
ATOM   2092 C  CA  . ASP   B 1 130 ? 29.003 -20.357 22.631 1.00 10.24 ? 136 ASP   C CA  1 
ATOM   2093 C  C   . ASP   B 1 130 ? 27.659 -20.003 23.235 1.00 10.65 ? 136 ASP   C C   1 
ATOM   2094 O  O   . ASP   B 1 130 ? 27.267 -18.817 23.321 1.00 10.87 ? 136 ASP   C O   1 
ATOM   2095 C  CB  . ASP   B 1 130 ? 30.077 -20.128 23.717 1.00 11.47 ? 136 ASP   C CB  1 
ATOM   2096 C  CG  . ASP   B 1 130 ? 29.965 -21.056 24.909 1.00 12.99 ? 136 ASP   C CG  1 
ATOM   2097 O  OD1 . ASP   B 1 130 ? 29.836 -22.275 24.709 1.00 14.07 ? 136 ASP   C OD1 1 
ATOM   2098 O  OD2 . ASP   B 1 130 ? 29.892 -20.540 26.054 1.00 16.15 ? 136 ASP   C OD2 1 
ATOM   2099 N  N   . VAL   B 1 131 ? 26.947 -21.028 23.715 1.00 10.15 ? 137 VAL   C N   1 
ATOM   2100 C  CA  . VAL   B 1 131 ? 25.701 -20.843 24.487 1.00 10.24 ? 137 VAL   C CA  1 
ATOM   2101 C  C   . VAL   B 1 131 ? 25.764 -21.508 25.865 1.00 11.12 ? 137 VAL   C C   1 
ATOM   2102 O  O   . VAL   B 1 131 ? 24.789 -21.448 26.637 1.00 11.32 ? 137 VAL   C O   1 
ATOM   2103 C  CB  . VAL   B 1 131 ? 24.428 -21.287 23.753 1.00 11.34 ? 137 VAL   C CB  1 
ATOM   2104 C  CG1 . VAL   B 1 131 ? 24.257 -20.466 22.448 1.00 11.86 ? 137 VAL   C CG1 1 
ATOM   2105 C  CG2 . VAL   B 1 131 ? 24.455 -22.764 23.462 1.00 12.18 ? 137 VAL   C CG2 1 
ATOM   2106 N  N   . ARG   B 1 132 ? 26.892 -22.156 26.224 1.00 11.17 ? 138 ARG   C N   1 
ATOM   2107 C  CA  . ARG   B 1 132 ? 26.967 -22.944 27.477 1.00 11.26 ? 138 ARG   C CA  1 
ATOM   2108 C  C   . ARG   B 1 132 ? 26.914 -22.101 28.730 1.00 11.36 ? 138 ARG   C C   1 
ATOM   2109 O  O   . ARG   B 1 132 ? 26.599 -22.663 29.803 1.00 12.90 ? 138 ARG   C O   1 
ATOM   2110 C  CB  . ARG   B 1 132 ? 28.228 -23.793 27.466 1.00 10.64 ? 138 ARG   C CB  1 
ATOM   2111 C  CG  . ARG   B 1 132 ? 28.228 -24.854 26.340 1.00 10.66 ? 138 ARG   C CG  1 
ATOM   2112 C  CD  . ARG   B 1 132 ? 29.531 -25.631 26.368 1.00 11.10 ? 138 ARG   C CD  1 
ATOM   2113 N  NE  . ARG   B 1 132 ? 30.623 -24.734 25.966 1.00 11.03 ? 138 ARG   C NE  1 
ATOM   2114 C  CZ  . ARG   B 1 132 ? 31.879 -25.113 25.802 1.00 11.27 ? 138 ARG   C CZ  1 
ATOM   2115 N  NH1 . ARG   B 1 132 ? 32.267 -26.351 26.142 1.00 11.92 ? 138 ARG   C NH1 1 
ATOM   2116 N  NH2 . ARG   B 1 132 ? 32.775 -24.259 25.319 1.00 11.82 ? 138 ARG   C NH2 1 
ATOM   2117 N  N   . ASP   B 1 133 ? 27.221 -20.808 28.656 1.00 11.04 ? 139 ASP   C N   1 
ATOM   2118 C  CA  . ASP   B 1 133 ? 27.144 -19.939 29.835 1.00 12.17 ? 139 ASP   C CA  1 
ATOM   2119 C  C   . ASP   B 1 133 ? 25.722 -19.393 30.070 1.00 12.98 ? 139 ASP   C C   1 
ATOM   2120 O  O   . ASP   B 1 133 ? 25.501 -18.780 31.132 1.00 14.76 ? 139 ASP   C O   1 
ATOM   2121 C  CB  . ASP   B 1 133 ? 28.114 -18.752 29.696 1.00 14.28 ? 139 ASP   C CB  1 
ATOM   2122 C  CG  . ASP   B 1 133 ? 27.746 -17.833 28.544 1.00 14.87 ? 139 ASP   C CG  1 
ATOM   2123 O  OD1 . ASP   B 1 133 ? 27.392 -18.338 27.464 1.00 14.50 ? 139 ASP   C OD1 1 
ATOM   2124 O  OD2 . ASP   B 1 133 ? 27.768 -16.577 28.739 1.00 17.63 ? 139 ASP   C OD2 1 
ATOM   2125 N  N   . LEU   B 1 134 ? 24.764 -19.596 29.122 1.00 12.59 ? 140 LEU   C N   1 
ATOM   2126 C  CA  . LEU   B 1 134 ? 23.412 -19.034 29.213 1.00 12.32 ? 140 LEU   C CA  1 
ATOM   2127 C  C   . LEU   B 1 134 ? 22.559 -20.000 30.007 1.00 12.38 ? 140 LEU   C C   1 
ATOM   2128 O  O   . LEU   B 1 134 ? 21.741 -20.736 29.458 1.00 12.60 ? 140 LEU   C O   1 
ATOM   2129 C  CB  . LEU   B 1 134 ? 22.859 -18.782 27.805 1.00 12.00 ? 140 LEU   C CB  1 
ATOM   2130 C  CG  . LEU   B 1 134 ? 23.720 -17.827 26.939 1.00 12.27 ? 140 LEU   C CG  1 
ATOM   2131 C  CD1 . LEU   B 1 134 ? 23.139 -17.721 25.494 1.00 14.10 ? 140 LEU   C CD1 1 
ATOM   2132 C  CD2 . LEU   B 1 134 ? 23.811 -16.448 27.572 1.00 15.22 ? 140 LEU   C CD2 1 
ATOM   2133 N  N   . LEU   B 1 135 ? 22.772 -20.022 31.344 1.00 12.99 ? 141 LEU   C N   1 
ATOM   2134 C  CA  . LEU   B 1 135 ? 22.139 -21.061 32.175 1.00 14.00 ? 141 LEU   C CA  1 
ATOM   2135 C  C   . LEU   B 1 135 ? 20.623 -20.975 32.230 1.00 13.43 ? 141 LEU   C C   1 
ATOM   2136 O  O   . LEU   B 1 135 ? 19.931 -21.992 32.403 1.00 14.64 ? 141 LEU   C O   1 
ATOM   2137 C  CB  . LEU   B 1 135 ? 22.724 -21.066 33.613 1.00 13.97 ? 141 LEU   C CB  1 
ATOM   2138 C  CG  . LEU   B 1 135 ? 24.265 -21.050 33.685 1.00 14.18 ? 141 LEU   C CG  1 
ATOM   2139 C  CD1 . LEU   B 1 135 ? 24.782 -21.073 35.167 1.00 15.37 ? 141 LEU   C CD1 1 
ATOM   2140 C  CD2 . LEU   B 1 135 ? 24.902 -22.229 32.912 1.00 14.79 ? 141 LEU   C CD2 1 
ATOM   2141 N  N   . TRP   B 1 136 ? 20.107 -19.750 32.007 1.00 13.47 ? 142 TRP   C N   1 
ATOM   2142 C  CA  . TRP   B 1 136 ? 18.666 -19.498 32.061 1.00 14.52 ? 142 TRP   C CA  1 
ATOM   2143 C  C   . TRP   B 1 136 ? 17.935 -20.201 30.915 1.00 15.69 ? 142 TRP   C C   1 
ATOM   2144 O  O   . TRP   B 1 136 ? 16.704 -20.344 30.966 1.00 16.97 ? 142 TRP   C O   1 
ATOM   2145 C  CB  . TRP   B 1 136 ? 18.388 -17.992 32.053 1.00 14.93 ? 142 TRP   C CB  1 
ATOM   2146 C  CG  . TRP   B 1 136 ? 19.081 -17.250 30.938 1.00 14.68 ? 142 TRP   C CG  1 
ATOM   2147 C  CD1 . TRP   B 1 136 ? 20.244 -16.562 31.023 1.00 15.08 ? 142 TRP   C CD1 1 
ATOM   2148 C  CD2 . TRP   B 1 136 ? 18.571 -17.019 29.601 1.00 14.96 ? 142 TRP   C CD2 1 
ATOM   2149 N  NE1 . TRP   B 1 136 ? 20.549 -15.986 29.793 1.00 16.01 ? 142 TRP   C NE1 1 
ATOM   2150 C  CE2 . TRP   B 1 136 ? 19.505 -16.212 28.924 1.00 15.80 ? 142 TRP   C CE2 1 
ATOM   2151 C  CE3 . TRP   B 1 136 ? 17.410 -17.399 28.947 1.00 15.01 ? 142 TRP   C CE3 1 
ATOM   2152 C  CZ2 . TRP   B 1 136 ? 19.333 -15.847 27.569 1.00 15.40 ? 142 TRP   C CZ2 1 
ATOM   2153 C  CZ3 . TRP   B 1 136 ? 17.202 -16.977 27.640 1.00 15.47 ? 142 TRP   C CZ3 1 
ATOM   2154 C  CH2 . TRP   B 1 136 ? 18.159 -16.219 26.967 1.00 15.62 ? 142 TRP   C CH2 1 
ATOM   2155 N  N   . LEU   B 1 137 ? 18.634 -20.645 29.842 1.00 14.20 ? 143 LEU   C N   1 
ATOM   2156 C  CA  . LEU   B 1 137 ? 17.958 -21.427 28.791 1.00 14.31 ? 143 LEU   C CA  1 
ATOM   2157 C  C   . LEU   B 1 137 ? 17.340 -22.724 29.369 1.00 17.17 ? 143 LEU   C C   1 
ATOM   2158 O  O   . LEU   B 1 137 ? 16.437 -23.295 28.754 1.00 18.90 ? 143 LEU   C O   1 
ATOM   2159 C  CB  . LEU   B 1 137 ? 18.896 -21.786 27.635 1.00 13.97 ? 143 LEU   C CB  1 
ATOM   2160 C  CG  . LEU   B 1 137 ? 19.344 -20.594 26.787 1.00 13.27 ? 143 LEU   C CG  1 
ATOM   2161 C  CD1 . LEU   B 1 137 ? 20.507 -21.018 25.856 1.00 14.73 ? 143 LEU   C CD1 1 
ATOM   2162 C  CD2 . LEU   B 1 137 ? 18.195 -20.042 25.914 1.00 14.81 ? 143 LEU   C CD2 1 
ATOM   2163 N  N   . ASP   B 1 138 ? 17.873 -23.214 30.515 1.00 15.93 ? 144 ASP   C N   1 
ATOM   2164 C  CA  . ASP   B 1 138 ? 17.420 -24.500 31.077 1.00 17.42 ? 144 ASP   C CA  1 
ATOM   2165 C  C   . ASP   B 1 138 ? 16.178 -24.367 31.967 1.00 20.07 ? 144 ASP   C C   1 
ATOM   2166 O  O   . ASP   B 1 138 ? 15.728 -25.400 32.514 1.00 21.62 ? 144 ASP   C O   1 
ATOM   2167 C  CB  . ASP   B 1 138 ? 18.525 -25.141 31.938 1.00 17.50 ? 144 ASP   C CB  1 
ATOM   2168 C  CG  . ASP   B 1 138 ? 19.761 -25.595 31.164 1.00 18.30 ? 144 ASP   C CG  1 
ATOM   2169 O  OD1 . ASP   B 1 138 ? 19.717 -25.625 29.917 1.00 18.88 ? 144 ASP   C OD1 1 
ATOM   2170 O  OD2 . ASP   B 1 138 ? 20.785 -25.924 31.823 1.00 21.03 ? 144 ASP   C OD2 1 
ATOM   2171 N  N   . GLU   B 1 139 ? 15.623 -23.165 32.119 1.00 20.76 ? 145 GLU   C N   1 
ATOM   2172 C  CA  . GLU   B 1 139 ? 14.476 -22.977 33.012 1.00 25.23 ? 145 GLU   C CA  1 
ATOM   2173 C  C   . GLU   B 1 139 ? 13.452 -21.978 32.464 1.00 29.16 ? 145 GLU   C C   1 
ATOM   2174 O  O   . GLU   B 1 139 ? 13.683 -21.298 31.467 1.00 30.53 ? 145 GLU   C O   1 
ATOM   2175 C  CB  . GLU   B 1 139 ? 15.032 -22.454 34.366 1.00 30.87 ? 145 GLU   C CB  1 
ATOM   2176 C  CG  . GLU   B 1 139 ? 15.693 -21.095 34.218 1.00 39.30 ? 145 GLU   C CG  1 
ATOM   2177 C  CD  . GLU   B 1 139 ? 16.660 -20.669 35.308 1.00 49.30 ? 145 GLU   C CD  1 
ATOM   2178 O  OE1 . GLU   B 1 139 ? 16.994 -19.461 35.367 1.00 49.89 ? 145 GLU   C OE1 1 
ATOM   2179 O  OE2 . GLU   B 1 139 ? 17.079 -21.541 36.103 1.00 53.18 ? 145 GLU   C OE2 1 
ATOM   2180 N  N   . GLU   B 1 140 ? 12.369 -21.787 33.251 1.00 31.97 ? 146 GLU   C N   1 
ATOM   2181 C  CA  . GLU   B 1 140 ? 11.373 -20.720 33.149 1.00 34.79 ? 146 GLU   C CA  1 
ATOM   2182 C  C   . GLU   B 1 140 ? 10.819 -20.478 31.775 1.00 36.79 ? 146 GLU   C C   1 
ATOM   2183 O  O   . GLU   B 1 140 ? 10.559 -19.330 31.402 1.00 37.79 ? 146 GLU   C O   1 
ATOM   2184 C  CB  . GLU   B 1 140 ? 11.980 -19.427 33.719 1.00 37.08 ? 146 GLU   C CB  1 
ATOM   2185 C  CG  . GLU   B 1 140 ? 12.031 -19.417 35.237 1.00 45.24 ? 146 GLU   C CG  1 
ATOM   2186 C  CD  . GLU   B 1 140 ? 12.783 -18.244 35.835 1.00 55.25 ? 146 GLU   C CD  1 
ATOM   2187 O  OE1 . GLU   B 1 140 ? 12.405 -17.084 35.549 1.00 57.04 ? 146 GLU   C OE1 1 
ATOM   2188 O  OE2 . GLU   B 1 140 ? 13.746 -18.488 36.599 1.00 58.83 ? 146 GLU   C OE2 1 
HETATM 2189 N  N1  . A1B3J C 2 .   ? 10.948 15.688  17.505 1.00 20.07 ? 201 A1B3J A N1  1 
HETATM 2190 C  C4  . A1B3J C 2 .   ? 5.620  12.864  25.523 1.00 34.48 ? 201 A1B3J A C4  1 
HETATM 2191 C  C5  . A1B3J C 2 .   ? 4.509  13.285  26.428 1.00 37.92 ? 201 A1B3J A C5  1 
HETATM 2192 C  C6  . A1B3J C 2 .   ? 6.396  13.834  24.913 1.00 33.46 ? 201 A1B3J A C6  1 
HETATM 2193 C  C7  . A1B3J C 2 .   ? 7.485  13.516  24.120 1.00 31.96 ? 201 A1B3J A C7  1 
HETATM 2194 C  C8  . A1B3J C 2 .   ? 8.442  14.602  23.696 1.00 31.83 ? 201 A1B3J A C8  1 
HETATM 2195 C  C10 . A1B3J C 2 .   ? 10.890 15.236  22.412 1.00 30.24 ? 201 A1B3J A C10 1 
HETATM 2196 C  C13 . A1B3J C 2 .   ? 10.266 16.588  18.219 1.00 24.18 ? 201 A1B3J A C13 1 
HETATM 2197 O  O2  . A1B3J C 2 .   ? 9.642  17.533  17.726 1.00 24.65 ? 201 A1B3J A O2  1 
HETATM 2198 C  C12 . A1B3J C 2 .   ? 10.280 16.553  19.735 1.00 26.76 ? 201 A1B3J A C12 1 
HETATM 2199 S  S   . A1B3J C 2 .   ? 12.016 16.551  20.279 1.00 29.14 ? 201 A1B3J A S   1 
HETATM 2200 C  C11 . A1B3J C 2 .   ? 11.668 16.471  22.046 1.00 30.17 ? 201 A1B3J A C11 1 
HETATM 2201 C  C14 . A1B3J C 2 .   ? 9.696  15.231  20.191 1.00 29.21 ? 201 A1B3J A C14 1 
HETATM 2202 N  N   . A1B3J C 2 .   ? 9.626  15.145  21.653 1.00 29.98 ? 201 A1B3J A N   1 
HETATM 2203 C  C9  . A1B3J C 2 .   ? 8.444  14.788  22.193 1.00 29.97 ? 201 A1B3J A C9  1 
HETATM 2204 O  O1  . A1B3J C 2 .   ? 7.446  14.589  21.514 1.00 27.55 ? 201 A1B3J A O1  1 
HETATM 2205 C  C1  . A1B3J C 2 .   ? 7.756  12.175  23.866 1.00 30.48 ? 201 A1B3J A C1  1 
HETATM 2206 O  O   . A1B3J C 2 .   ? 8.664  11.959  22.861 1.00 28.66 ? 201 A1B3J A O   1 
HETATM 2207 C  C   . A1B3J C 2 .   ? 9.495  10.799  22.922 1.00 27.77 ? 201 A1B3J A C   1 
HETATM 2208 F  F2  . A1B3J C 2 .   ? 4.158  12.347  27.297 1.00 38.79 ? 201 A1B3J A F2  1 
HETATM 2209 F  F1  . A1B3J C 2 .   ? 3.404  13.666  25.772 1.00 38.06 ? 201 A1B3J A F1  1 
HETATM 2210 F  F   . A1B3J C 2 .   ? 4.837  14.368  27.117 1.00 40.05 ? 201 A1B3J A F   1 
HETATM 2211 C  C3  . A1B3J C 2 .   ? 5.955  11.529  25.318 1.00 32.42 ? 201 A1B3J A C3  1 
HETATM 2212 C  C2  . A1B3J C 2 .   ? 7.007  11.178  24.482 1.00 30.77 ? 201 A1B3J A C2  1 
HETATM 2213 ZN ZN  . ZN    D 3 .   ? 11.176 -4.038  5.879  1.00 18.60 2 202 ZN    A ZN  1 
HETATM 2214 ZN ZN  . ZN    E 3 .   ? 30.654 -31.189 26.692 1.00 11.35 2 201 ZN    C ZN  1 
HETATM 2215 S  S   . DMS   F 4 .   ? 20.755 -32.091 9.242  1.00 84.80 ? 202 DMS   C S   1 
HETATM 2216 O  O   . DMS   F 4 .   ? 21.868 -32.511 8.338  1.00 84.96 ? 202 DMS   C O   1 
HETATM 2217 C  C1  . DMS   F 4 .   ? 21.315 -32.278 10.942 1.00 84.73 ? 202 DMS   C C1  1 
HETATM 2218 C  C2  . DMS   F 4 .   ? 20.683 -30.281 9.278  1.00 84.74 ? 202 DMS   C C2  1 
HETATM 2219 O  O   . HOH   G 5 .   ? 2.082  22.943  21.326 1.00 29.36 ? 401 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 8.309  8.473   22.311 1.00 23.84 ? 402 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? 11.281 8.881   4.334  1.00 20.75 ? 403 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 14.167 17.354  4.363  1.00 40.90 ? 404 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 35.360 -3.913  7.804  1.00 20.89 ? 405 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? 0.188  18.275  17.321 1.00 32.49 ? 406 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 3.038  9.504   8.947  1.00 26.08 ? 407 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 37.555 14.871  14.068 1.00 51.23 ? 408 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 6.576  3.106   3.174  1.00 33.96 ? 409 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 35.538 7.890   9.677  1.00 47.15 ? 410 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 7.385  20.380  17.263 1.00 22.77 ? 411 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 13.947 2.846   1.268  1.00 21.88 ? 412 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 4.223  9.435   27.999 1.00 36.47 ? 413 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 20.170 19.810  5.600  1.00 38.92 ? 414 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 29.500 22.275  19.371 1.00 24.54 ? 415 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 17.443 0.981   28.281 1.00 23.07 ? 416 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 12.550 -5.845  30.478 1.00 43.83 ? 417 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 27.907 8.025   1.661  1.00 32.80 ? 418 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 0.451  -0.897  19.378 1.00 21.79 ? 419 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 12.462 22.339  12.746 1.00 31.61 ? 420 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 19.373 10.104  19.646 1.00 11.97 ? 421 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 28.173 3.103   4.916  1.00 29.21 ? 422 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 15.859 23.972  14.790 1.00 40.27 ? 423 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? 8.436  -2.875  31.805 1.00 24.54 ? 424 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 23.465 21.694  7.200  1.00 21.93 ? 425 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 0.664  -1.181  9.181  1.00 33.25 ? 426 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 4.646  -3.608  28.851 1.00 25.57 ? 427 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 30.441 10.513  15.615 1.00 26.09 ? 428 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 36.317 -2.534  10.977 1.00 28.07 ? 429 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 24.930 5.182   21.443 1.00 28.87 ? 430 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 9.489  22.158  10.130 1.00 48.15 ? 431 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? 28.680 11.052  3.142  1.00 48.78 ? 432 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 33.848 14.146  9.658  1.00 30.33 ? 433 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 10.535 10.102  31.390 1.00 21.57 ? 434 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 22.657 0.878   17.413 1.00 14.63 ? 435 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 2.599  -2.791  20.750 1.00 24.74 ? 436 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 10.833 5.620   3.392  1.00 22.77 ? 437 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 5.647  17.849  23.952 1.00 38.09 ? 438 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? -0.085 1.310   15.841 1.00 11.79 ? 439 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 3.238  20.880  24.313 1.00 45.31 ? 440 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 14.131 13.813  24.004 1.00 19.12 ? 441 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 21.849 2.396   -0.824 1.00 30.03 ? 442 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 3.798  -8.118  9.863  1.00 46.12 ? 443 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 8.427  24.806  23.834 1.00 26.39 ? 444 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 3.971  12.889  17.910 1.00 27.80 ? 445 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 21.697 5.016   24.654 1.00 35.83 ? 446 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 8.545  19.220  19.614 1.00 24.11 ? 447 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 31.334 -2.380  15.596 1.00 52.31 ? 448 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 35.283 10.950  12.256 1.00 45.34 ? 449 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 13.750 4.048   23.537 1.00 11.27 ? 450 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 23.391 11.739  21.922 1.00 30.69 ? 451 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 17.009 -3.477  27.737 1.00 31.77 ? 452 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 11.340 12.714  11.146 1.00 13.93 ? 453 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 20.954 -4.147  14.184 1.00 15.03 ? 454 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 28.944 3.372   12.698 1.00 15.38 ? 455 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 29.891 11.602  18.517 1.00 24.97 ? 456 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 26.618 -5.447  10.021 1.00 20.93 ? 457 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 33.992 -2.350  13.514 1.00 31.91 ? 458 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 11.872 15.462  1.498  1.00 41.73 ? 459 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 15.045 11.362  0.048  1.00 32.13 ? 460 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 12.201 16.889  27.863 1.00 33.61 ? 461 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 18.428 21.891  9.472  1.00 17.64 ? 462 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 16.585 3.875   23.701 1.00 15.73 ? 463 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 5.867  16.896  21.381 1.00 31.75 ? 464 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 33.740 11.095  15.573 1.00 32.65 ? 465 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 20.759 -1.085  3.084  1.00 29.76 ? 466 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 20.405 17.907  24.030 1.00 36.84 ? 467 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 26.925 -1.226  8.892  1.00 23.53 ? 468 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 4.758  14.766  20.213 1.00 40.87 ? 469 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 19.673 20.279  21.915 1.00 37.06 ? 470 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 20.829 -2.559  16.873 1.00 13.59 ? 471 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 2.613  16.151  19.258 1.00 30.63 ? 472 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 29.449 11.951  21.342 1.00 31.28 ? 473 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 30.094 -1.411  8.700  1.00 28.86 ? 474 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 31.624 19.925  11.641 1.00 19.98 ? 475 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 30.552 2.969   14.889 1.00 20.52 ? 476 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 11.617 17.980  4.843  1.00 37.89 ? 477 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 9.606  4.011   33.512 1.00 12.69 ? 478 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 12.184 11.158  29.682 1.00 19.31 ? 479 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 6.664  -6.933  23.796 1.00 21.98 ? 480 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 5.034  8.232   2.354  1.00 32.43 ? 481 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 7.571  -4.637  2.840  1.00 39.51 ? 482 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 3.232  -0.783  2.911  1.00 48.79 ? 483 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 13.265 11.417  9.217  1.00 12.86 ? 484 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 5.472  5.340   32.695 1.00 20.28 ? 485 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 17.592 20.009  16.987 1.00 15.39 ? 486 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 32.283 2.104   6.053  1.00 35.63 ? 487 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 30.432 4.513   5.809  1.00 21.34 ? 488 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 3.123  0.540   29.064 1.00 34.70 ? 489 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 32.784 16.548  9.238  1.00 31.53 ? 490 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 19.462 2.990   19.392 1.00 17.45 ? 491 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 36.540 18.035  14.423 1.00 27.59 ? 492 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 30.979 15.634  22.743 1.00 23.22 ? 493 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 11.623 -6.971  24.775 1.00 26.90 ? 494 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 22.892 -0.652  5.420  1.00 20.75 ? 495 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 4.172  0.303   24.024 1.00 17.34 ? 496 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 27.225 -1.346  15.892 1.00 24.98 ? 497 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 28.938 15.784  4.295  1.00 29.93 ? 498 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 13.674 24.961  25.992 1.00 38.07 ? 499 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 24.173 -3.476  16.132 1.00 32.60 ? 500 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 23.268 -6.537  11.913 1.00 28.49 ? 501 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 36.835 2.411   10.043 1.00 37.45 ? 502 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 3.258  7.689   24.402 1.00 30.17 ? 503 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 14.479 -2.404  17.974 1.00 16.85 ? 504 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 25.469 19.648  21.715 1.00 25.00 ? 505 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 18.099 17.763  4.278  1.00 31.30 ? 506 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 3.883  -3.921  6.040  1.00 26.65 ? 507 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 17.041 6.269   27.037 1.00 25.01 ? 508 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 0.256  6.091   6.100  1.00 23.78 ? 509 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 17.746 10.740  26.135 1.00 21.05 ? 510 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? 7.164  26.472  14.326 1.00 36.01 ? 511 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 16.491 21.305  19.096 1.00 25.23 ? 512 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 15.013 21.826  8.456  1.00 27.48 ? 513 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 16.289 9.413   -1.616 1.00 20.80 ? 514 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 33.981 18.633  10.733 1.00 26.37 ? 515 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 28.032 17.592  24.124 1.00 21.81 ? 516 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 32.031 8.753   7.616  1.00 21.88 ? 517 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 36.236 -0.396  12.727 1.00 30.98 ? 518 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 1.173  11.642  27.516 1.00 42.14 ? 519 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 5.203  26.480  20.051 1.00 28.02 ? 520 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 15.459 15.225  3.626  1.00 30.92 ? 521 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 25.231 17.964  4.606  1.00 32.52 ? 522 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 8.269  6.582   33.818 1.00 18.24 ? 523 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 35.884 15.367  10.977 1.00 42.14 ? 524 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 8.546  -6.467  9.714  1.00 29.86 ? 525 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? 6.217  23.898  10.404 1.00 35.70 ? 526 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 22.523 19.469  19.675 1.00 29.77 ? 527 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? 17.522 0.800   20.238 1.00 17.68 ? 528 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 3.570  27.044  16.137 1.00 49.17 ? 529 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? 7.325  13.845  4.737  1.00 21.34 ? 530 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 19.878 13.285  2.231  1.00 30.20 ? 531 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? 16.792 -3.997  2.909  1.00 25.45 ? 532 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 0.546  -1.203  16.722 1.00 18.09 ? 533 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 14.209 24.370  17.838 1.00 37.34 ? 534 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 4.629  -5.656  14.308 1.00 42.33 ? 535 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 33.932 5.155   16.644 1.00 29.67 ? 536 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 23.292 16.803  23.710 1.00 49.12 ? 537 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? 3.371  -0.334  21.405 1.00 24.14 ? 538 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 22.733 3.475   20.875 1.00 19.46 ? 539 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 25.041 10.698  22.940 1.00 37.49 ? 540 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 9.247  3.376   2.941  1.00 29.60 ? 541 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 23.260 19.126  6.286  1.00 18.34 ? 542 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 19.329 21.453  6.795  1.00 39.14 ? 543 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 16.957 -5.576  12.220 1.00 30.66 ? 544 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? 21.031 9.955   21.925 1.00 15.73 ? 545 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 15.203 14.334  26.310 1.00 33.83 ? 546 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 31.029 19.447  8.930  1.00 33.84 ? 547 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 5 .   ? 19.470 -0.448  33.235 1.00 34.51 ? 548 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 5 .   ? 15.881 21.394  7.139  1.00 26.44 ? 549 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 5 .   ? 19.496 16.783  26.250 1.00 43.13 ? 550 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 5 .   ? 23.402 8.294   21.700 1.00 23.70 ? 551 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 5 .   ? 1.189  -4.979  17.390 1.00 36.51 ? 552 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 5 .   ? 21.018 -4.790  11.503 1.00 27.01 ? 553 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 5 .   ? 17.221 -2.417  19.674 1.00 18.10 ? 554 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 5 .   ? 34.077 7.803   16.658 1.00 33.75 ? 555 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 5 .   ? 8.093  11.134  31.642 1.00 35.93 ? 556 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 5 .   ? 36.629 16.153  16.794 1.00 34.90 ? 557 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 5 .   ? 2.161  14.529  16.874 1.00 29.48 ? 558 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 5 .   ? 19.681 9.255   -0.904 1.00 26.75 ? 559 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 5 .   ? 6.023  -3.573  31.456 1.00 27.00 ? 560 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 5 .   ? 5.145  3.691   -0.566 1.00 59.18 ? 561 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 5 .   ? 8.600  21.133  7.667  1.00 48.89 ? 562 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 5 .   ? 10.648 17.283  25.620 1.00 31.14 ? 563 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 5 .   ? 38.106 2.775   16.288 1.00 57.20 ? 564 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 5 .   ? 14.733 13.174  28.680 1.00 36.61 ? 565 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 5 .   ? 19.075 -3.326  33.781 1.00 40.61 ? 566 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 5 .   ? 19.174 -6.310  10.794 1.00 42.91 ? 567 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 5 .   ? 31.653 9.159   17.454 1.00 38.29 ? 568 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 5 .   ? 31.905 6.987   5.396  1.00 28.27 ? 569 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 5 .   ? 0.983  3.743   26.160 1.00 36.60 ? 570 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 5 .   ? 4.406  8.901   30.628 1.00 57.81 ? 571 HOH   A O   1 
HETATM 2390 O  O   . HOH   G 5 .   ? 1.985  -5.242  14.674 1.00 43.07 ? 572 HOH   A O   1 
HETATM 2391 O  O   . HOH   G 5 .   ? 35.386 4.181   18.875 1.00 48.96 ? 573 HOH   A O   1 
HETATM 2392 O  O   . HOH   G 5 .   ? 30.866 12.958  23.039 1.00 40.61 ? 574 HOH   A O   1 
HETATM 2393 O  O   . HOH   G 5 .   ? 16.851 -4.981  34.308 1.00 29.72 ? 575 HOH   A O   1 
HETATM 2394 O  O   . HOH   G 5 .   ? 29.748 0.681   16.522 1.00 32.22 ? 576 HOH   A O   1 
HETATM 2395 O  O   . HOH   G 5 .   ? 33.333 -4.252  5.651  1.00 43.80 ? 577 HOH   A O   1 
HETATM 2396 O  O   . HOH   G 5 .   ? 38.558 0.832   13.622 1.00 52.67 ? 578 HOH   A O   1 
HETATM 2397 O  O   . HOH   G 5 .   ? 18.584 2.100   22.711 1.00 34.16 ? 579 HOH   A O   1 
HETATM 2398 O  O   . HOH   G 5 .   ? 36.771 20.487  17.691 1.00 38.27 ? 580 HOH   A O   1 
HETATM 2399 O  O   . HOH   G 5 .   ? 0.097  0.093   23.154 1.00 29.86 ? 581 HOH   A O   1 
HETATM 2400 O  O   . HOH   G 5 .   ? 21.771 14.895  1.208  1.00 49.19 ? 582 HOH   A O   1 
HETATM 2401 O  O   . HOH   G 5 .   ? 23.789 1.049   19.894 1.00 31.38 ? 583 HOH   A O   1 
HETATM 2402 O  O   . HOH   G 5 .   ? 17.796 24.479  10.434 1.00 31.96 ? 584 HOH   A O   1 
HETATM 2403 O  O   . HOH   G 5 .   ? 30.294 7.043   17.936 1.00 35.41 ? 585 HOH   A O   1 
HETATM 2404 O  O   . HOH   G 5 .   ? 33.578 16.764  23.100 1.00 46.27 ? 586 HOH   A O   1 
HETATM 2405 O  O   . HOH   G 5 .   ? 21.331 2.934   23.209 1.00 32.27 ? 587 HOH   A O   1 
HETATM 2406 O  O   . HOH   G 5 .   ? 12.471 -5.018  33.112 1.00 29.87 ? 588 HOH   A O   1 
HETATM 2407 O  O   . HOH   G 5 .   ? 6.223  5.587   1.698  1.00 30.91 ? 589 HOH   A O   1 
HETATM 2408 O  O   . HOH   G 5 .   ? 31.299 4.551   17.028 1.00 24.11 ? 590 HOH   A O   1 
HETATM 2409 O  O   . HOH   G 5 .   ? 37.766 -4.530  6.687  1.00 29.00 ? 591 HOH   A O   1 
HETATM 2410 O  O   . HOH   G 5 .   ? -0.419 13.883  17.273 1.00 33.23 ? 592 HOH   A O   1 
HETATM 2411 O  O   . HOH   G 5 .   ? 28.105 16.990  2.013  1.00 47.13 ? 593 HOH   A O   1 
HETATM 2412 O  O   . HOH   G 5 .   ? 21.380 -1.048  18.965 1.00 28.20 ? 594 HOH   A O   1 
HETATM 2413 O  O   . HOH   G 5 .   ? 2.572  -1.681  22.809 1.00 31.79 ? 595 HOH   A O   1 
HETATM 2414 O  O   . HOH   G 5 .   ? 2.376  -5.002  22.588 1.00 34.61 ? 596 HOH   A O   1 
HETATM 2415 O  O   . HOH   G 5 .   ? 32.222 11.260  6.576  1.00 31.50 ? 597 HOH   A O   1 
HETATM 2416 O  O   . HOH   G 5 .   ? 7.946  16.870  25.965 1.00 35.84 ? 598 HOH   A O   1 
HETATM 2417 O  O   . HOH   G 5 .   ? 7.801  16.462  3.450  1.00 51.60 ? 599 HOH   A O   1 
HETATM 2418 O  O   . HOH   G 5 .   ? 39.244 -2.665  10.655 1.00 36.33 ? 600 HOH   A O   1 
HETATM 2419 O  O   . HOH   G 5 .   ? 28.972 1.558   19.269 1.00 48.22 ? 601 HOH   A O   1 
HETATM 2420 O  O   . HOH   G 5 .   ? 38.107 19.819  15.420 1.00 35.21 ? 602 HOH   A O   1 
HETATM 2421 O  O   . HOH   G 5 .   ? 26.523 0.437   20.091 1.00 45.27 ? 603 HOH   A O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 17.504 -33.269 24.067 1.00 38.09 ? 301 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 17.041 -9.701  10.725 1.00 56.28 ? 302 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 31.638 -17.914 -0.084 1.00 37.94 ? 303 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 23.554 -26.417 4.338  1.00 20.34 ? 304 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 38.338 -7.366  6.971  1.00 19.72 ? 305 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 15.210 -26.529 34.712 1.00 61.79 ? 306 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 31.016 -32.647 0.741  1.00 36.96 ? 307 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 14.709 -18.673 31.914 1.00 36.90 ? 308 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 10.198 -20.020 28.940 1.00 34.28 ? 309 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 18.943 -32.281 19.784 1.00 36.67 ? 310 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 38.627 -18.629 21.460 1.00 24.89 ? 311 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 38.496 -27.207 28.537 1.00 43.00 ? 312 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 41.100 -10.750 22.896 1.00 45.20 ? 313 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 16.288 -15.975 8.847  1.00 40.17 ? 314 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 28.273 -5.217  18.613 1.00 37.60 ? 315 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 19.757 -4.118  20.183 1.00 21.03 ? 316 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 17.898 -5.994  24.059 1.00 23.96 ? 317 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 43.281 -3.920  19.125 1.00 47.19 ? 318 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 24.597 -9.940  26.919 1.00 35.97 ? 319 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 36.068 -17.692 11.642 1.00 23.63 ? 320 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 22.937 -5.926  21.081 1.00 18.56 ? 321 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 29.142 -9.701  25.124 1.00 51.28 ? 322 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 42.614 -11.317 11.111 1.00 27.24 ? 323 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 14.774 -23.907 12.302 1.00 30.25 ? 324 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 30.773 -18.139 26.864 1.00 17.06 ? 325 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 20.741 -18.744 12.791 1.00 12.90 ? 326 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 21.740 -26.067 34.327 1.00 24.33 ? 327 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 36.234 -26.218 34.199 1.00 32.44 ? 328 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 17.906 -27.567 16.487 1.00 16.14 ? 329 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 18.581 -8.872  13.819 1.00 25.13 ? 330 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 22.014 -28.746 4.764  1.00 23.76 ? 331 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 24.694 -5.898  15.170 1.00 26.77 ? 332 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 10.256 -17.485 18.302 1.00 26.01 ? 333 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 37.211 -18.723 28.180 1.00 28.19 ? 334 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 37.422 -31.931 10.901 1.00 22.51 ? 335 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 3.309  -13.032 20.314 1.00 45.22 ? 336 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 40.125 -29.607 11.907 1.00 22.87 ? 337 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 32.539 -23.714 29.064 1.00 15.64 ? 338 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 24.798 -15.745 7.283  1.00 17.97 ? 339 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 7.221  -30.370 22.043 1.00 30.28 ? 340 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 40.540 -27.270 15.162 1.00 11.21 ? 341 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 31.046 -23.820 -1.308 1.00 20.91 ? 342 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 41.240 -25.048 7.212  1.00 31.73 ? 343 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 31.014 -21.530 28.373 1.00 14.47 ? 344 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 23.937 -8.122  9.464  1.00 22.13 ? 345 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 37.163 -10.398 4.734  1.00 37.21 ? 346 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 13.955 -24.372 29.320 1.00 31.32 ? 347 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 26.036 -25.282 8.735  1.00 12.20 ? 348 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 13.273 -11.197 28.446 1.00 35.04 ? 349 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 26.456 -15.270 30.798 1.00 28.62 ? 350 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 6.889  -9.261  22.645 1.00 30.28 ? 351 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 31.144 -6.138  5.820  1.00 38.41 ? 352 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 35.304 -32.766 3.346  1.00 33.34 ? 353 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 16.255 -17.254 10.994 1.00 35.86 ? 354 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 11.935 -24.291 21.695 1.00 16.57 ? 355 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 9.945  -8.846  23.928 1.00 26.46 ? 356 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 14.664 -28.790 25.537 1.00 35.89 ? 357 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 4.741  -25.053 25.370 1.00 41.73 ? 358 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 20.769 -25.659 13.860 1.00 17.55 ? 359 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 35.196 -13.144 8.646  1.00 17.51 ? 360 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 19.220 -27.725 28.145 1.00 17.57 ? 361 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 29.899 -15.274 19.546 1.00 14.47 ? 362 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 5.899  -16.860 22.574 1.00 52.68 ? 363 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 35.996 -28.466 2.875  1.00 35.00 ? 364 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 10.624 -16.897 12.514 1.00 32.57 ? 365 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 21.966 -21.310 4.425  1.00 51.60 ? 366 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 25.833 -37.886 24.270 1.00 29.54 ? 367 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 32.030 -10.466 13.736 1.00 17.45 ? 368 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 10.462 -16.954 15.053 1.00 28.83 ? 369 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 9.206  -8.035  21.343 1.00 24.21 ? 370 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 34.131 -33.723 24.073 1.00 30.98 ? 371 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 29.769 -13.093 12.926 1.00 14.10 ? 372 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 39.342 -33.690 13.713 1.00 40.38 ? 373 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 27.180 -35.654 20.761 1.00 23.95 ? 374 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 22.373 -10.851 7.680  1.00 44.33 ? 375 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 36.314 -21.311 6.899  1.00 22.03 ? 376 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 23.846 -3.399  18.939 1.00 35.31 ? 377 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 41.964 -12.128 20.752 1.00 42.72 ? 378 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 29.950 -15.874 30.420 1.00 28.53 ? 379 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 32.164 -34.613 24.783 1.00 25.63 ? 380 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 13.128 -29.542 19.147 1.00 30.37 ? 381 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 36.280 -32.518 25.002 1.00 38.95 ? 382 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 22.915 -8.548  14.003 1.00 14.42 ? 383 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 36.600 -16.177 12.508 1.00 29.59 ? 384 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 11.006 -21.928 13.643 1.00 43.22 ? 385 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 45.382 -14.742 4.624  1.00 35.49 ? 386 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 34.751 -35.020 18.061 1.00 25.60 ? 387 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 4.299  -10.418 19.555 1.00 28.07 ? 388 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 32.990 -9.847  11.085 1.00 13.84 ? 389 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 37.769 -31.393 25.807 1.00 25.81 ? 390 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 3.865  -8.272  14.706 1.00 25.92 ? 391 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 23.206 -25.411 8.908  1.00 18.55 ? 392 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 30.067 -10.483 27.620 1.00 42.06 ? 393 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 28.916 -36.269 7.836  1.00 18.43 ? 394 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 24.517 -13.775 5.443  1.00 36.38 ? 395 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 31.267 -12.185 10.625 1.00 13.41 ? 396 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 5.826  -12.509 23.165 1.00 48.72 ? 397 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 22.324 -23.779 6.049  1.00 31.70 ? 398 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 23.592 -33.697 29.034 1.00 27.39 ? 399 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 22.965 -28.218 12.587 1.00 18.86 ? 400 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 28.126 -16.360 22.045 1.00 12.38 ? 401 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 11.508 -22.595 28.700 1.00 25.94 ? 402 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 22.931 -33.378 5.376  1.00 29.86 ? 403 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? 22.433 -13.779 29.722 1.00 34.11 ? 404 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? 17.524 -24.138 8.702  1.00 39.34 ? 405 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? 4.530  -16.215 17.016 1.00 46.27 ? 406 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? 43.291 -25.604 23.698 1.00 24.47 ? 407 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? 10.991 -6.451  13.275 1.00 23.02 ? 408 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? 8.779  -13.365 10.808 1.00 22.11 ? 409 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? 34.372 -13.481 25.473 1.00 18.56 ? 410 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? 26.652 -6.067  22.018 1.00 27.72 ? 411 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? 31.209 -35.713 31.750 1.00 38.11 ? 412 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? 26.751 -12.058 27.573 1.00 24.78 ? 413 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 5 .   ? 10.079 -24.897 19.820 1.00 20.54 ? 414 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 5 .   ? 22.888 -7.538  25.501 1.00 39.82 ? 415 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 5 .   ? 35.598 -24.707 24.646 1.00 16.32 ? 416 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 5 .   ? 30.304 -18.104 8.351  1.00 25.76 ? 417 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 5 .   ? 37.778 -20.209 5.037  1.00 35.73 ? 418 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 5 .   ? 26.082 -31.059 30.827 1.00 16.86 ? 419 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 5 .   ? 10.650 -11.973 9.055  1.00 26.02 ? 420 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 5 .   ? 31.566 -13.472 4.320  1.00 32.10 ? 421 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 5 .   ? 26.426 -31.272 14.831 1.00 17.28 ? 422 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 5 .   ? 36.943 -29.267 10.085 1.00 19.12 ? 423 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 5 .   ? 21.657 -18.925 5.862  1.00 25.90 ? 424 HOH   C O   1 
HETATM 2546 O  O   . HOH   H 5 .   ? 33.054 -30.332 31.670 1.00 17.68 ? 425 HOH   C O   1 
HETATM 2547 O  O   . HOH   H 5 .   ? 35.781 -28.563 7.724  1.00 16.58 ? 426 HOH   C O   1 
HETATM 2548 O  O   . HOH   H 5 .   ? 6.342  -18.849 25.364 1.00 55.63 ? 427 HOH   C O   1 
HETATM 2549 O  O   . HOH   H 5 .   ? 20.452 -23.655 34.818 1.00 28.46 ? 428 HOH   C O   1 
HETATM 2550 O  O   . HOH   H 5 .   ? 9.748  -18.500 26.685 1.00 28.85 ? 429 HOH   C O   1 
HETATM 2551 O  O   . HOH   H 5 .   ? 38.932 -13.065 25.752 1.00 26.77 ? 430 HOH   C O   1 
HETATM 2552 O  O   . HOH   H 5 .   ? 4.646  -27.964 23.251 1.00 34.78 ? 431 HOH   C O   1 
HETATM 2553 O  O   . HOH   H 5 .   ? 41.720 -12.450 18.076 1.00 22.27 ? 432 HOH   C O   1 
HETATM 2554 O  O   . HOH   H 5 .   ? 35.120 -4.187  17.645 1.00 29.51 ? 433 HOH   C O   1 
HETATM 2555 O  O   . HOH   H 5 .   ? 20.235 -32.301 22.233 1.00 27.72 ? 434 HOH   C O   1 
HETATM 2556 O  O   . HOH   H 5 .   ? 10.367 -30.960 25.257 1.00 29.19 ? 435 HOH   C O   1 
HETATM 2557 O  O   . HOH   H 5 .   ? 37.981 -23.659 4.438  1.00 36.39 ? 436 HOH   C O   1 
HETATM 2558 O  O   . HOH   H 5 .   ? 42.295 -12.073 13.908 1.00 30.93 ? 437 HOH   C O   1 
HETATM 2559 O  O   . HOH   H 5 .   ? 35.176 -13.677 6.034  1.00 32.77 ? 438 HOH   C O   1 
HETATM 2560 O  O   . HOH   H 5 .   ? 4.053  -12.776 17.265 1.00 38.71 ? 439 HOH   C O   1 
HETATM 2561 O  O   . HOH   H 5 .   ? 6.794  -17.103 18.630 1.00 46.29 ? 440 HOH   C O   1 
HETATM 2562 O  O   . HOH   H 5 .   ? 17.159 -25.280 12.695 1.00 22.73 ? 441 HOH   C O   1 
HETATM 2563 O  O   . HOH   H 5 .   ? 39.021 -16.669 3.659  1.00 39.24 ? 442 HOH   C O   1 
HETATM 2564 O  O   . HOH   H 5 .   ? 32.800 -14.371 9.379  1.00 14.35 ? 443 HOH   C O   1 
HETATM 2565 O  O   . HOH   H 5 .   ? 34.596 -23.201 -0.848 1.00 37.19 ? 444 HOH   C O   1 
HETATM 2566 O  O   . HOH   H 5 .   ? 37.281 -23.915 31.736 1.00 52.51 ? 445 HOH   C O   1 
HETATM 2567 O  O   . HOH   H 5 .   ? 16.380 -20.526 11.528 1.00 23.55 ? 446 HOH   C O   1 
HETATM 2568 O  O   . HOH   H 5 .   ? 36.604 -24.867 27.177 1.00 31.19 ? 447 HOH   C O   1 
HETATM 2569 O  O   . HOH   H 5 .   ? 18.645 -8.340  25.522 1.00 18.84 ? 448 HOH   C O   1 
HETATM 2570 O  O   . HOH   H 5 .   ? 18.679 -11.673 7.683  1.00 41.06 ? 449 HOH   C O   1 
HETATM 2571 O  O   . HOH   H 5 .   ? 40.059 -29.931 14.600 1.00 15.41 ? 450 HOH   C O   1 
HETATM 2572 O  O   . HOH   H 5 .   ? 33.697 -36.131 8.785  1.00 38.03 ? 451 HOH   C O   1 
HETATM 2573 O  O   . HOH   H 5 .   ? 15.065 -30.064 18.221 1.00 36.67 ? 452 HOH   C O   1 
HETATM 2574 O  O   . HOH   H 5 .   ? 18.807 -19.140 10.778 1.00 17.85 ? 453 HOH   C O   1 
HETATM 2575 O  O   . HOH   H 5 .   ? 6.570  -20.077 18.226 1.00 30.93 ? 454 HOH   C O   1 
HETATM 2576 O  O   . HOH   H 5 .   ? 6.542  -23.024 18.288 1.00 33.95 ? 455 HOH   C O   1 
HETATM 2577 O  O   . HOH   H 5 .   ? 33.997 -15.592 27.097 1.00 30.04 ? 456 HOH   C O   1 
HETATM 2578 O  O   . HOH   H 5 .   ? 8.837  -12.941 24.636 1.00 52.25 ? 457 HOH   C O   1 
HETATM 2579 O  O   . HOH   H 5 .   ? 23.370 -17.579 33.265 1.00 19.94 ? 458 HOH   C O   1 
HETATM 2580 O  O   . HOH   H 5 .   ? 33.512 -32.981 0.790  1.00 40.08 ? 459 HOH   C O   1 
HETATM 2581 O  O   . HOH   H 5 .   ? 9.760  -24.624 29.458 1.00 42.76 ? 460 HOH   C O   1 
HETATM 2582 O  O   . HOH   H 5 .   ? 37.527 -13.931 9.867  1.00 27.59 ? 461 HOH   C O   1 
HETATM 2583 O  O   . HOH   H 5 .   ? 31.589 -15.696 7.100  1.00 27.71 ? 462 HOH   C O   1 
HETATM 2584 O  O   . HOH   H 5 .   ? 17.020 -32.030 28.860 1.00 64.53 ? 463 HOH   C O   1 
HETATM 2585 O  O   . HOH   H 5 .   ? 23.401 -31.137 13.209 1.00 32.69 ? 464 HOH   C O   1 
HETATM 2586 O  O   . HOH   H 5 .   ? 24.226 -16.619 3.174  1.00 37.64 ? 465 HOH   C O   1 
HETATM 2587 O  O   . HOH   H 5 .   ? 19.121 -8.770  11.537 1.00 44.72 ? 466 HOH   C O   1 
HETATM 2588 O  O   . HOH   H 5 .   ? 42.036 -31.515 15.644 1.00 29.50 ? 467 HOH   C O   1 
HETATM 2589 O  O   . HOH   H 5 .   ? 20.353 -19.671 36.070 1.00 29.11 ? 468 HOH   C O   1 
HETATM 2590 O  O   . HOH   H 5 .   ? 34.275 -31.874 29.575 1.00 22.72 ? 469 HOH   C O   1 
HETATM 2591 O  O   . HOH   H 5 .   ? 38.911 -21.091 31.590 1.00 47.62 ? 470 HOH   C O   1 
HETATM 2592 O  O   . HOH   H 5 .   ? 23.814 -15.705 31.444 1.00 28.45 ? 471 HOH   C O   1 
HETATM 2593 O  O   . HOH   H 5 .   ? 21.149 -17.466 34.573 1.00 25.32 ? 472 HOH   C O   1 
HETATM 2594 O  O   . HOH   H 5 .   ? 19.900 -29.263 3.284  1.00 62.53 ? 473 HOH   C O   1 
HETATM 2595 O  O   . HOH   H 5 .   ? 8.927  -19.231 16.879 1.00 37.86 ? 474 HOH   C O   1 
HETATM 2596 O  O   . HOH   H 5 .   ? 22.921 -16.735 5.407  1.00 37.98 ? 475 HOH   C O   1 
HETATM 2597 O  O   . HOH   H 5 .   ? 21.459 -26.874 10.278 1.00 33.21 ? 476 HOH   C O   1 
HETATM 2598 O  O   . HOH   H 5 .   ? 28.423 -12.661 30.232 1.00 50.27 ? 477 HOH   C O   1 
HETATM 2599 O  O   . HOH   H 5 .   ? 16.424 -27.555 14.157 1.00 30.90 ? 478 HOH   C O   1 
HETATM 2600 O  O   . HOH   H 5 .   ? 38.752 -8.420  4.577  1.00 37.54 ? 479 HOH   C O   1 
HETATM 2601 O  O   . HOH   H 5 .   ? 20.031 -9.244  6.728  1.00 62.24 ? 480 HOH   C O   1 
HETATM 2602 O  O   . HOH   H 5 .   ? 21.351 -24.957 3.997  1.00 38.35 ? 481 HOH   C O   1 
HETATM 2603 O  O   . HOH   H 5 .   ? 6.189  -12.564 10.940 1.00 44.98 ? 482 HOH   C O   1 
HETATM 2604 O  O   . HOH   H 5 .   ? 20.684 -7.237  27.089 1.00 67.46 ? 483 HOH   C O   1 
HETATM 2605 O  O   . HOH   H 5 .   ? 38.812 -13.682 6.154  1.00 53.78 ? 484 HOH   C O   1 
HETATM 2606 O  O   . HOH   H 5 .   ? 18.505 -26.089 10.139 1.00 35.52 ? 485 HOH   C O   1 
HETATM 2607 O  O   . HOH   H 5 .   ? 22.199 -3.042  20.715 1.00 45.69 ? 486 HOH   C O   1 
HETATM 2608 O  O   . HOH   H 5 .   ? 32.562 -19.333 29.021 1.00 27.06 ? 487 HOH   C O   1 
HETATM 2609 O  O   . HOH   H 5 .   ? 23.050 -8.512  7.114  1.00 51.91 ? 488 HOH   C O   1 
HETATM 2610 O  O   . HOH   H 5 .   ? 10.042 -21.378 16.226 1.00 33.55 ? 489 HOH   C O   1 
HETATM 2611 O  O   . HOH   H 5 .   ? 18.078 -17.927 8.266  1.00 35.85 ? 490 HOH   C O   1 
HETATM 2612 O  O   . HOH   H 5 .   ? 18.162 -16.412 38.265 1.00 34.18 ? 491 HOH   C O   1 
HETATM 2613 O  O   . HOH   H 5 .   ? 9.032  -23.515 17.686 1.00 31.44 ? 492 HOH   C O   1 
HETATM 2614 O  O   . HOH   H 5 .   ? 22.751 -11.965 5.788  1.00 36.83 ? 493 HOH   C O   1 
HETATM 2615 O  O   . HOH   H 5 .   ? 35.227 -23.086 28.957 1.00 26.37 ? 494 HOH   C O   1 
HETATM 2616 O  O   . HOH   H 5 .   ? 37.596 -34.424 9.344  1.00 42.81 ? 495 HOH   C O   1 
HETATM 2617 O  O   . HOH   H 5 .   ? 39.430 -11.305 4.702  1.00 47.67 ? 496 HOH   C O   1 
HETATM 2618 O  O   . HOH   H 5 .   ? 34.352 -10.732 26.527 1.00 40.51 ? 497 HOH   C O   1 
HETATM 2619 O  O   . HOH   H 5 .   ? 19.341 -17.619 5.791  1.00 36.29 ? 498 HOH   C O   1 
HETATM 2620 O  O   . HOH   H 5 .   ? 19.603 -15.174 34.615 1.00 33.16 ? 499 HOH   C O   1 
HETATM 2621 O  O   . HOH   H 5 .   ? 37.563 -19.029 32.853 1.00 73.22 ? 500 HOH   C O   1 
HETATM 2622 O  O   . HOH   H 5 .   ? 36.488 -16.500 32.239 1.00 66.45 ? 501 HOH   C 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   ? 0.1966 0.1883 0.1727 -0.0120 -0.0063 -0.0099 7   SER   A N   
2    C CA  . SER   A 1   ? 0.1876 0.1817 0.1690 -0.0106 -0.0093 -0.0075 7   SER   A CA  
3    C C   . SER   A 1   ? 0.1826 0.1787 0.1703 -0.0054 -0.0117 -0.0027 7   SER   A C   
4    O O   . SER   A 1   ? 0.1937 0.1899 0.1807 -0.0040 -0.0119 -0.0009 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2200 0.2199 0.1974 -0.0167 -0.0131 -0.0063 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2654 0.2708 0.2413 -0.0177 -0.0172 -0.0013 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1645 0.1616 0.1583 -0.0032 -0.0128 -0.0012 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1547 0.1529 0.1547 0.0007  -0.0137 0.0023  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1378 0.1346 0.1429 0.0031  -0.0122 0.0014  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1588 0.1531 0.1631 0.0029  -0.0102 -0.0013 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1283 0.1264 0.1391 0.0050  -0.0126 0.0039  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1303 0.1275 0.1454 0.0064  -0.0109 0.0030  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1248 0.1212 0.1439 0.0082  -0.0089 0.0040  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1390 0.1354 0.1596 0.0089  -0.0088 0.0061  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1430 0.1433 0.1620 0.0052  -0.0128 0.0040  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1225 0.1178 0.1431 0.0084  -0.0065 0.0024  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1203 0.1145 0.1447 0.0087  -0.0032 0.0020  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1306 0.1261 0.1618 0.0092  -0.0027 0.0028  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1301 0.1269 0.1611 0.0085  -0.0038 0.0021  10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1182 0.1119 0.1388 0.0070  -0.0009 -0.0003 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1468 0.1409 0.1618 0.0066  -0.0018 -0.0003 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1394 0.1313 0.1619 0.0055  0.0036  -0.0020 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1532 0.1498 0.1656 0.0045  -0.0007 -0.0006 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1200 0.1149 0.1583 0.0104  -0.0004 0.0045  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1310 0.1276 0.1781 0.0112  0.0010  0.0057  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1352 0.1280 0.1856 0.0105  0.0077  0.0028  11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1418 0.1317 0.1974 0.0116  0.0116  0.0036  11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1397 0.1402 0.1954 0.0133  -0.0014 0.0115  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1389 0.1442 0.1900 0.0119  -0.0076 0.0136  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1508 0.1601 0.2027 0.0104  -0.0102 0.0137  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1579 0.1636 0.2033 0.0112  -0.0103 0.0150  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1569 0.1698 0.2031 0.0076  -0.0149 0.0142  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1622 0.1719 0.2020 0.0085  -0.0151 0.0159  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1641 0.1771 0.2040 0.0064  -0.0171 0.0150  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.1994 0.2158 0.2326 0.0023  -0.0207 0.0147  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1377 0.1301 0.1847 0.0081  0.0096  -0.0007 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1409 0.1302 0.1885 0.0055  0.0163  -0.0046 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1558 0.1465 0.2091 0.0050  0.0183  -0.0053 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1429 0.1368 0.1936 0.0046  0.0144  -0.0047 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1632 0.1524 0.1997 0.0012  0.0168  -0.0079 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1783 0.1713 0.2092 0.0006  0.0116  -0.0067 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.1794 0.1663 0.2147 -0.0036 0.0239  -0.0125 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1624 0.1505 0.2248 0.0054  0.0249  -0.0064 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1679 0.1577 0.2368 0.0051  0.0274  -0.0070 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1517 0.1473 0.2258 0.0082  0.0207  -0.0020 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1475 0.1455 0.2265 0.0113  0.0169  0.0028  13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1409 0.1390 0.2124 0.0063  0.0190  -0.0031 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1369 0.1404 0.2111 0.0077  0.0128  0.0005  14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1286 0.1322 0.1913 0.0061  0.0075  -0.0002 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1374 0.1434 0.1993 0.0051  0.0045  0.0002  14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1503 0.1568 0.2324 0.0072  0.0148  0.0005  14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.1907 0.1988 0.2882 0.0100  0.0191  0.0035  14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2199 0.2342 0.3268 0.0125  0.0153  0.0093  14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1869 0.1901 0.2879 0.0094  0.0274  0.0000  14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1217 0.1228 0.1772 0.0060  0.0066  -0.0009 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1177 0.1184 0.1643 0.0052  0.0026  -0.0011 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1161 0.1169 0.1607 0.0067  -0.0007 0.0007  15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1265 0.1263 0.1731 0.0081  0.0006  0.0017  15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1297 0.1285 0.1690 0.0029  0.0049  -0.0033 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1492 0.1487 0.1884 0.0000  0.0079  -0.0049 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1690 0.1700 0.2090 -0.0006 0.0064  -0.0042 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1697 0.1683 0.2072 -0.0030 0.0129  -0.0076 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1742 0.1761 0.2137 -0.0036 0.0092  -0.0054 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.1904 0.1902 0.2262 -0.0070 0.0158  -0.0093 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.1908 0.1925 0.2276 -0.0070 0.0137  -0.0078 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2406 0.2438 0.2756 -0.0112 0.0165  -0.0091 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1166 0.1179 0.1566 0.0062  -0.0041 0.0009  16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1215 0.1225 0.1571 0.0065  -0.0067 0.0017  16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1206 0.1187 0.1497 0.0059  -0.0062 0.0000  16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1269 0.1242 0.1552 0.0050  -0.0061 -0.0007 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1274 0.1319 0.1641 0.0050  -0.0103 0.0032  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1425 0.1465 0.1726 0.0035  -0.0125 0.0028  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1524 0.1615 0.1826 0.0002  -0.0160 0.0042  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1591 0.1659 0.1814 -0.0034 -0.0161 0.0010  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1827 0.1896 0.1991 -0.0054 -0.0171 0.0006  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1970 0.2063 0.2144 -0.0037 -0.0187 0.0040  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1820 0.1858 0.1916 -0.0092 -0.0156 -0.0034 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1126 0.1094 0.1382 0.0066  -0.0056 0.0000  17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1133 0.1088 0.1349 0.0065  -0.0050 -0.0003 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1245 0.1188 0.1430 0.0068  -0.0061 -0.0006 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1334 0.1280 0.1504 0.0071  -0.0069 -0.0002 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1214 0.1178 0.1412 0.0061  -0.0033 0.0000  17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1314 0.1289 0.1494 0.0061  -0.0031 0.0016  17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1363 0.1338 0.1579 0.0044  -0.0011 -0.0007 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1156 0.1078 0.1330 0.0063  -0.0054 -0.0015 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1175 0.1077 0.1315 0.0055  -0.0051 -0.0029 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1428 0.1331 0.1568 0.0055  -0.0052 -0.0029 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1314 0.1189 0.1462 0.0065  -0.0020 -0.0030 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1403 0.1280 0.1588 0.0077  -0.0007 -0.0010 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1127 0.1026 0.1250 0.0024  -0.0061 -0.0049 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.1917 0.1820 0.2046 0.0024  -0.0064 -0.0047 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1298 0.1242 0.1425 0.0014  -0.0096 -0.0032 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2067 0.1955 0.2144 -0.0005 -0.0058 -0.0071 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.0831 0.0713 0.0981 0.0014  -0.0046 -0.0059 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2182 0.2130 0.2336 0.0019  -0.0095 -0.0028 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1256 0.1108 0.1377 0.0060  -0.0003 -0.0046 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1285 0.1104 0.1438 0.0073  0.0040  -0.0044 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1362 0.1140 0.1535 0.0058  0.0065  -0.0064 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1394 0.1159 0.1526 0.0022  0.0059  -0.0098 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1326 0.1118 0.1446 0.0063  0.0065  -0.0071 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1411 0.1237 0.1509 0.0075  0.0046  -0.0054 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1489 0.1333 0.1539 0.0058  0.0015  -0.0062 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1445 0.1290 0.1588 0.0102  0.0062  -0.0023 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1343 0.1106 0.1581 0.0081  0.0094  -0.0036 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1413 0.1128 0.1677 0.0066  0.0125  -0.0052 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.1552 0.1202 0.1783 0.0032  0.0172  -0.0111 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.1678 0.1302 0.1880 -0.0009 0.0178  -0.0149 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1443 0.1152 0.1795 0.0099  0.0156  -0.0001 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1517 0.1173 0.1908 0.0087  0.0191  -0.0008 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.1610 0.1265 0.2103 0.0125  0.0224  0.0060  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1797 0.1404 0.2338 0.0118  0.0257  0.0066  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.1977 0.1491 0.2559 0.0110  0.0330  0.0036  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2034 0.1492 0.2602 0.0100  0.0379  -0.0014 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2146 0.1617 0.2780 0.0106  0.0362  0.0051  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.1478 0.1106 0.1706 0.0039  0.0205  -0.0121 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.1790 0.1350 0.1981 -0.0004 0.0263  -0.0185 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.1879 0.1461 0.1961 -0.0067 0.0226  -0.0232 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2135 0.1669 0.2165 -0.0125 0.0273  -0.0293 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.1956 0.1484 0.2186 0.0020  0.0322  -0.0186 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.1780 0.1358 0.1959 0.0022  0.0285  -0.0180 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.1698 0.1343 0.1910 0.0068  0.0240  -0.0120 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.1893 0.1461 0.1988 -0.0021 0.0294  -0.0228 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.1862 0.1529 0.2016 0.0056  0.0223  -0.0133 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.1921 0.1547 0.2004 0.0005  0.0251  -0.0194 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.1820 0.1478 0.1868 -0.0062 0.0150  -0.0203 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.1762 0.1467 0.1729 -0.0116 0.0104  -0.0221 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.1885 0.1635 0.1862 -0.0131 0.0058  -0.0206 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.1988 0.1797 0.1922 -0.0169 0.0011  -0.0200 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.1696 0.1453 0.1637 -0.0099 0.0061  -0.0192 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.1776 0.1497 0.1701 -0.0093 0.0106  -0.0210 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.1886 0.1658 0.1785 -0.0078 0.0062  -0.0179 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2113 0.1788 0.1967 -0.0164 0.0157  -0.0276 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.1748 0.1478 0.1789 -0.0100 0.0070  -0.0190 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.1759 0.1532 0.1817 -0.0113 0.0032  -0.0176 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.1873 0.1652 0.1879 -0.0189 0.0033  -0.0217 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.1953 0.1666 0.1927 -0.0230 0.0090  -0.0268 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.1704 0.1449 0.1831 -0.0076 0.0054  -0.0156 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.1793 0.1652 0.1796 -0.0212 -0.0024 -0.0194 24  THR   A N   
139  C CA  . THR   A 18  ? 0.1773 0.1669 0.1726 -0.0296 -0.0037 -0.0221 24  THR   A CA  
140  C C   . THR   A 18  ? 0.1877 0.1756 0.1869 -0.0309 -0.0020 -0.0234 24  THR   A C   
141  O O   . THR   A 18  ? 0.1782 0.1632 0.1842 -0.0250 -0.0008 -0.0212 24  THR   A O   
142  C CB  . THR   A 18  ? 0.1973 0.1988 0.1927 -0.0313 -0.0112 -0.0170 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.1881 0.1933 0.1926 -0.0258 -0.0139 -0.0123 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2171 0.2210 0.2095 -0.0298 -0.0133 -0.0146 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.1891 0.1796 0.1837 -0.0394 -0.0023 -0.0267 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.1935 0.1835 0.1917 -0.0413 -0.0013 -0.0276 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.1728 0.1705 0.1793 -0.0360 -0.0066 -0.0213 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.1749 0.1693 0.1870 -0.0327 -0.0046 -0.0207 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2127 0.2069 0.2038 -0.0528 -0.0016 -0.0319 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3004 0.2974 0.2957 -0.0553 -0.0024 -0.0316 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3478 0.3345 0.3459 -0.0543 0.0040  -0.0351 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3419 0.3513 0.3414 -0.0569 -0.0090 -0.0268 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3538 0.3464 0.3549 -0.0575 0.0014  -0.0340 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3699 0.3765 0.3729 -0.0585 -0.0064 -0.0288 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.1712 0.1790 0.1793 -0.0352 -0.0127 -0.0163 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.1705 0.1847 0.1880 -0.0301 -0.0162 -0.0107 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.1524 0.1598 0.1744 -0.0219 -0.0132 -0.0098 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.1589 0.1669 0.1871 -0.0192 -0.0127 -0.0083 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.1897 0.2147 0.2103 -0.0297 -0.0220 -0.0046 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.2727 0.3037 0.3048 -0.0251 -0.0239 0.0006  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3089 0.3453 0.3453 -0.0281 -0.0250 0.0014  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.2905 0.3198 0.3278 -0.0182 -0.0232 0.0036  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.1434 0.1450 0.1620 -0.0188 -0.0111 -0.0108 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.1390 0.1356 0.1609 -0.0126 -0.0085 -0.0096 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1341 0.1250 0.1580 -0.0125 -0.0045 -0.0113 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1418 0.1332 0.1702 -0.0095 -0.0042 -0.0091 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1491 0.1413 0.1673 -0.0102 -0.0067 -0.0103 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.1675 0.1644 0.1847 -0.0090 -0.0100 -0.0078 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1641 0.1661 0.1863 -0.0068 -0.0126 -0.0043 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1619 0.1571 0.1738 -0.0104 -0.0095 -0.0093 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1372 0.1225 0.1577 -0.0163 -0.0010 -0.0152 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1437 0.1225 0.1670 -0.0162 0.0035  -0.0162 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1451 0.1279 0.1716 -0.0184 0.0018  -0.0156 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.1561 0.1362 0.1867 -0.0163 0.0040  -0.0140 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1577 0.1284 0.1774 -0.0204 0.0091  -0.0212 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1538 0.1186 0.1739 -0.0166 0.0131  -0.0210 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.1869 0.1503 0.2020 -0.0184 0.0142  -0.0237 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.1625 0.1228 0.1891 -0.0110 0.0166  -0.0172 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.1739 0.1319 0.1927 -0.0137 0.0186  -0.0223 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.1724 0.1293 0.1988 -0.0090 0.0196  -0.0176 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.1832 0.1432 0.2161 -0.0079 0.0172  -0.0128 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.1905 0.1442 0.2240 -0.0036 0.0233  -0.0131 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.1871 0.1451 0.2259 -0.0030 0.0199  -0.0079 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.1952 0.1500 0.2351 -0.0009 0.0231  -0.0079 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1450 0.1352 0.1704 -0.0227 -0.0021 -0.0161 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1449 0.1401 0.1744 -0.0249 -0.0037 -0.0152 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.1507 0.1511 0.1868 -0.0199 -0.0059 -0.0109 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.1688 0.1728 0.2096 -0.0207 -0.0063 -0.0100 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.1742 0.1773 0.2011 -0.0320 -0.0073 -0.0163 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1434 0.1443 0.1800 -0.0151 -0.0069 -0.0086 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1463 0.1510 0.1886 -0.0111 -0.0075 -0.0055 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1389 0.1383 0.1791 -0.0072 -0.0050 -0.0050 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1476 0.1487 0.1889 -0.0045 -0.0053 -0.0035 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1569 0.1688 0.2027 -0.0101 -0.0109 -0.0027 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.1686 0.1882 0.2182 -0.0141 -0.0138 -0.0015 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2044 0.2282 0.2611 -0.0140 -0.0135 0.0000  30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.1852 0.2077 0.2299 -0.0187 -0.0165 -0.0020 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1430 0.1367 0.1811 -0.0075 -0.0023 -0.0058 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1352 0.1257 0.1718 -0.0045 -0.0006 -0.0041 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.1423 0.1353 0.1809 -0.0034 0.0000  -0.0018 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.1645 0.1584 0.2054 -0.0049 0.0010  -0.0015 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1461 0.1302 0.1825 -0.0051 0.0027  -0.0044 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.1495 0.1316 0.1866 -0.0020 0.0045  -0.0010 31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.1600 0.1422 0.1943 -0.0003 0.0036  -0.0015 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.1826 0.1583 0.2228 -0.0020 0.0088  0.0001  31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1345 0.1288 0.1713 -0.0016 -0.0001 -0.0004 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1367 0.1336 0.1733 -0.0021 0.0010  0.0014  32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1414 0.1378 0.1767 -0.0017 0.0017  0.0051  32  VAL   A C   
209  O O   . VAL   A 26  ? 0.1635 0.1617 0.1993 -0.0033 0.0026  0.0079  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1347 0.1340 0.1704 -0.0017 0.0009  0.0003  32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.1682 0.1702 0.2016 -0.0040 0.0029  0.0012  32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.1547 0.1556 0.1950 -0.0016 0.0007  -0.0016 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1400 0.1348 0.1742 0.0004  0.0013  0.0059  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1391 0.1350 0.1742 0.0013  0.0019  0.0108  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1450 0.1374 0.1809 0.0038  0.0025  0.0104  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1430 0.1344 0.1761 0.0043  0.0015  0.0068  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.1492 0.1514 0.1810 -0.0005 0.0009  0.0128  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.1639 0.1702 0.1967 -0.0001 0.0005  0.0187  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.1915 0.2020 0.2274 -0.0011 0.0005  0.0255  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.1580 0.1659 0.1899 0.0014  -0.0003 0.0195  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2061 0.2216 0.2436 -0.0003 -0.0004 0.0309  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.1806 0.1946 0.2154 0.0011  -0.0008 0.0269  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.1684 0.1738 0.1976 0.0027  -0.0007 0.0153  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.1943 0.2123 0.2295 0.0019  -0.0016 0.0297  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.1798 0.1883 0.2083 0.0034  -0.0013 0.0174  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.1937 0.2082 0.2255 0.0031  -0.0016 0.0243  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1477 0.1383 0.1880 0.0055  0.0047  0.0144  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1524 0.1395 0.1942 0.0079  0.0065  0.0141  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.1637 0.1534 0.2121 0.0101  0.0081  0.0215  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.1709 0.1624 0.2240 0.0100  0.0089  0.0269  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.1818 0.1610 0.2242 0.0074  0.0096  0.0092  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.1920 0.1667 0.2392 0.0067  0.0130  0.0104  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2007 0.1715 0.2566 0.0095  0.0180  0.0155  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2068 0.1761 0.2681 0.0095  0.0201  0.0194  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.1841 0.1534 0.2426 0.0118  0.0203  0.0161  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1535 0.1439 0.2033 0.0122  0.0089  0.0226  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1441 0.1385 0.2023 0.0148  0.0104  0.0309  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1448 0.1346 0.2066 0.0176  0.0142  0.0293  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1486 0.1404 0.2055 0.0174  0.0124  0.0265  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.1649 0.1708 0.2205 0.0128  0.0058  0.0361  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2012 0.2150 0.2658 0.0144  0.0060  0.0465  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.2432 0.2539 0.3158 0.0183  0.0096  0.0487  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2534 0.2773 0.3169 0.0113  0.0026  0.0526  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.1522 0.1350 0.2229 0.0200  0.0202  0.0306  36  SER   A N   
245  C CA  . SER   A 30  ? 0.1689 0.1457 0.2435 0.0221  0.0257  0.0281  36  SER   A CA  
246  C C   . SER   A 30  ? 0.1762 0.1612 0.2572 0.0251  0.0249  0.0353  36  SER   A C   
247  O O   . SER   A 30  ? 0.1800 0.1634 0.2586 0.0255  0.0263  0.0314  36  SER   A O   
248  C CB  . SER   A 30  ? 0.2046 0.1712 0.2883 0.0235  0.0338  0.0278  36  SER   A CB  
249  O OG  . SER   A 30  ? 0.2595 0.2199 0.3492 0.0256  0.0410  0.0260  36  SER   A OG  
250  N N   . SER   A 31  ? 0.1650 0.1600 0.2525 0.0260  0.0219  0.0456  37  SER   A N   
251  C CA  . SER   A 31  ? 0.1629 0.1681 0.2566 0.0278  0.0204  0.0533  37  SER   A CA  
252  C C   . SER   A 31  ? 0.1538 0.1644 0.2362 0.0250  0.0153  0.0490  37  SER   A C   
253  O O   . SER   A 31  ? 0.1677 0.1835 0.2536 0.0263  0.0154  0.0519  37  SER   A O   
254  C CB  . SER   A 31  ? 0.1928 0.2098 0.2950 0.0279  0.0175  0.0662  37  SER   A CB  
255  O OG  . SER   A 31  ? 0.2703 0.2959 0.3621 0.0228  0.0106  0.0666  37  SER   A OG  
256  N N   . ARG   A 32  ? 0.1358 0.1446 0.2054 0.0213  0.0115  0.0417  38  ARG   A N   
257  C CA  . ARG   A 32  ? 0.1424 0.1545 0.2016 0.0185  0.0076  0.0370  38  ARG   A CA  
258  C C   . ARG   A 32  ? 0.1394 0.1422 0.1915 0.0185  0.0092  0.0274  38  ARG   A C   
259  O O   . ARG   A 32  ? 0.1331 0.1376 0.1777 0.0167  0.0066  0.0238  38  ARG   A O   
260  C CB  . ARG   A 32  ? 0.1482 0.1652 0.1992 0.0141  0.0030  0.0362  38  ARG   A CB  
261  C CG  . ARG   A 32  ? 0.1685 0.1972 0.2233 0.0120  0.0004  0.0456  38  ARG   A CG  
262  C CD  . ARG   A 32  ? 0.1598 0.1924 0.2059 0.0066  -0.0027 0.0436  38  ARG   A CD  
263  N NE  . ARG   A 32  ? 0.1363 0.1703 0.1731 0.0033  -0.0043 0.0379  38  ARG   A NE  
264  C CZ  . ARG   A 32  ? 0.1441 0.1842 0.1737 -0.0026 -0.0062 0.0373  38  ARG   A CZ  
265  N NH1 . ARG   A 32  ? 0.1698 0.2166 0.1994 -0.0064 -0.0074 0.0421  38  ARG   A NH1 
266  N NH2 . ARG   A 32  ? 0.1560 0.1959 0.1784 -0.0054 -0.0063 0.0319  38  ARG   A NH2 
267  N N   . ASP   A 33  ? 0.1336 0.1271 0.1875 0.0195  0.0134  0.0232  39  ASP   A N   
268  C CA  . ASP   A 33  ? 0.1387 0.1250 0.1848 0.0177  0.0142  0.0147  39  ASP   A CA  
269  C C   . ASP   A 33  ? 0.1365 0.1243 0.1735 0.0148  0.0092  0.0109  39  ASP   A C   
270  O O   . ASP   A 33  ? 0.1410 0.1275 0.1715 0.0133  0.0078  0.0064  39  ASP   A O   
271  C CB  . ASP   A 33  ? 0.1509 0.1360 0.1956 0.0183  0.0162  0.0123  39  ASP   A CB  
272  C CG  . ASP   A 33  ? 0.1501 0.1287 0.1864 0.0155  0.0172  0.0042  39  ASP   A CG  
273  O OD1 . ASP   A 33  ? 0.1626 0.1349 0.1979 0.0136  0.0199  0.0002  39  ASP   A OD1 
274  O OD2 . ASP   A 33  ? 0.1603 0.1404 0.1907 0.0145  0.0154  0.0020  39  ASP   A OD2 
275  N N   . LEU   A 34  ? 0.1273 0.1178 0.1648 0.0138  0.0071  0.0131  40  LEU   A N   
276  C CA  . LEU   A 34  ? 0.1176 0.1095 0.1487 0.0114  0.0035  0.0098  40  LEU   A CA  
277  C C   . LEU   A 34  ? 0.1239 0.1125 0.1554 0.0101  0.0038  0.0078  40  LEU   A C   
278  O O   . LEU   A 34  ? 0.1364 0.1238 0.1729 0.0107  0.0059  0.0106  40  LEU   A O   
279  C CB  . LEU   A 34  ? 0.1288 0.1280 0.1588 0.0101  0.0009  0.0132  40  LEU   A CB  
280  C CG  . LEU   A 34  ? 0.1474 0.1509 0.1744 0.0097  -0.0003 0.0140  40  LEU   A CG  
281  C CD1 . LEU   A 34  ? 0.1595 0.1700 0.1842 0.0064  -0.0020 0.0163  40  LEU   A CD1 
282  C CD2 . LEU   A 34  ? 0.1483 0.1482 0.1703 0.0095  -0.0009 0.0088  40  LEU   A CD2 
283  N N   . LEU   A 35  ? 0.1211 0.1092 0.1483 0.0084  0.0018  0.0038  41  LEU   A N   
284  C CA  . LEU   A 35  ? 0.1176 0.1045 0.1453 0.0067  0.0014  0.0022  41  LEU   A CA  
285  C C   . LEU   A 35  ? 0.1221 0.1124 0.1477 0.0057  -0.0014 0.0009  41  LEU   A C   
286  O O   . LEU   A 35  ? 0.1306 0.1217 0.1536 0.0059  -0.0028 -0.0002 41  LEU   A O   
287  C CB  . LEU   A 35  ? 0.1312 0.1129 0.1579 0.0050  0.0032  -0.0017 41  LEU   A CB  
288  C CG  . LEU   A 35  ? 0.1281 0.1092 0.1553 0.0024  0.0028  -0.0036 41  LEU   A CG  
289  C CD1 . LEU   A 35  ? 0.1578 0.1325 0.1855 0.0003  0.0069  -0.0065 41  LEU   A CD1 
290  C CD2 . LEU   A 35  ? 0.1385 0.1234 0.1631 0.0004  -0.0008 -0.0054 41  LEU   A CD2 
291  N N   . VAL   A 36  ? 0.1235 0.1154 0.1508 0.0046  -0.0016 0.0013  42  VAL   A N   
292  C CA  . VAL   A 36  ? 0.1133 0.1080 0.1410 0.0039  -0.0028 0.0002  42  VAL   A CA  
293  C C   . VAL   A 36  ? 0.1158 0.1105 0.1461 0.0026  -0.0032 -0.0010 42  VAL   A C   
294  O O   . VAL   A 36  ? 0.1288 0.1225 0.1606 0.0016  -0.0020 -0.0006 42  VAL   A O   
295  C CB  . VAL   A 36  ? 0.1183 0.1158 0.1457 0.0030  -0.0016 0.0015  42  VAL   A CB  
296  C CG1 . VAL   A 36  ? 0.1352 0.1339 0.1645 0.0022  -0.0009 -0.0003 42  VAL   A CG1 
297  C CG2 . VAL   A 36  ? 0.1384 0.1373 0.1628 0.0033  -0.0016 0.0030  42  VAL   A CG2 
298  N N   . SER   A 37  ? 0.1144 0.1110 0.1461 0.0023  -0.0049 -0.0018 43  SER   A N   
299  C CA  . SER   A 37  ? 0.1143 0.1132 0.1497 0.0006  -0.0058 -0.0021 43  SER   A CA  
300  C C   . SER   A 37  ? 0.1276 0.1303 0.1686 0.0015  -0.0056 -0.0010 43  SER   A C   
301  O O   . SER   A 37  ? 0.1286 0.1311 0.1700 0.0031  -0.0046 -0.0005 43  SER   A O   
302  C CB  . SER   A 37  ? 0.1334 0.1334 0.1670 -0.0015 -0.0081 -0.0029 43  SER   A CB  
303  O OG  . SER   A 37  ? 0.1423 0.1445 0.1749 -0.0007 -0.0101 -0.0016 43  SER   A OG  
304  N N   . SER   A 38  ? 0.1296 0.1353 0.1758 0.0003  -0.0057 -0.0007 44  SER   A N   
305  C CA  . SER   A 38  ? 0.1411 0.1502 0.1951 0.0015  -0.0043 0.0007  44  SER   A CA  
306  C C   . SER   A 38  ? 0.1585 0.1728 0.2179 0.0022  -0.0073 0.0039  44  SER   A C   
307  O O   . SER   A 38  ? 0.1839 0.2010 0.2409 -0.0001 -0.0110 0.0046  44  SER   A O   
308  C CB  . SER   A 38  ? 0.1702 0.1807 0.2284 0.0000  -0.0025 0.0000  44  SER   A CB  
309  O OG  . SER   A 38  ? 0.2094 0.2227 0.2681 -0.0022 -0.0054 0.0004  44  SER   A OG  
310  N N   . THR   A 39  ? 0.1574 0.1733 0.2247 0.0047  -0.0053 0.0061  45  THR   A N   
311  C CA  . THR   A 39  ? 0.1746 0.1966 0.2494 0.0058  -0.0080 0.0113  45  THR   A CA  
312  C C   . THR   A 39  ? 0.1901 0.2168 0.2789 0.0075  -0.0055 0.0145  45  THR   A C   
313  O O   . THR   A 39  ? 0.1779 0.2010 0.2701 0.0083  0.0000  0.0117  45  THR   A O   
314  C CB  . THR   A 39  ? 0.1826 0.2018 0.2566 0.0083  -0.0071 0.0126  45  THR   A CB  
315  O OG1 . THR   A 39  ? 0.1925 0.2068 0.2704 0.0103  -0.0009 0.0106  45  THR   A OG1 
316  C CG2 . THR   A 39  ? 0.2062 0.2209 0.2678 0.0071  -0.0088 0.0097  45  THR   A CG2 
317  N N   . THR   A 40  ? 0.2011 0.2367 0.2985 0.0075  -0.0094 0.0207  46  THR   A N   
318  C CA  . THR   A 40  ? 0.2134 0.2549 0.3273 0.0098  -0.0069 0.0255  46  THR   A CA  
319  C C   . THR   A 40  ? 0.2084 0.2465 0.3317 0.0144  -0.0017 0.0280  46  THR   A C   
320  O O   . THR   A 40  ? 0.2406 0.2761 0.3740 0.0166  0.0052  0.0270  46  THR   A O   
321  C CB  . THR   A 40  ? 0.2636 0.3179 0.3842 0.0075  -0.0135 0.0324  46  THR   A CB  
322  O OG1 . THR   A 40  ? 0.3238 0.3821 0.4419 0.0071  -0.0183 0.0372  46  THR   A OG1 
323  C CG2 . THR   A 40  ? 0.2730 0.3290 0.3838 0.0021  -0.0171 0.0285  46  THR   A CG2 
324  N N   . ALA   A 41  ? 0.2074 0.2447 0.3273 0.0154  -0.0041 0.0306  47  ALA   A N   
325  C CA  . ALA   A 41  ? 0.2152 0.2485 0.3438 0.0194  0.0012  0.0332  47  ALA   A CA  
326  C C   . ALA   A 41  ? 0.2083 0.2296 0.3262 0.0191  0.0068  0.0251  47  ALA   A C   
327  O O   . ALA   A 41  ? 0.2025 0.2207 0.3053 0.0164  0.0038  0.0203  47  ALA   A O   
328  C CB  . ALA   A 41  ? 0.2508 0.2896 0.3806 0.0201  -0.0044 0.0406  47  ALA   A CB  
329  N N   . GLN   A 42  ? 0.1854 0.2006 0.3112 0.0214  0.0150  0.0240  48  GLN   A N   
330  C CA  . GLN   A 42  ? 0.1998 0.2051 0.3157 0.0198  0.0206  0.0166  48  GLN   A CA  
331  C C   . GLN   A 42  ? 0.2034 0.2065 0.3134 0.0205  0.0180  0.0184  48  GLN   A C   
332  O O   . GLN   A 42  ? 0.2194 0.2258 0.3390 0.0235  0.0165  0.0256  48  GLN   A O   
333  C CB  . GLN   A 42  ? 0.2300 0.2289 0.3563 0.0206  0.0317  0.0137  48  GLN   A CB  
334  C CG  . GLN   A 42  ? 0.3030 0.3021 0.4310 0.0184  0.0358  0.0093  48  GLN   A CG  
335  C CD  . GLN   A 42  ? 0.3742 0.3662 0.5116 0.0183  0.0481  0.0053  48  GLN   A CD  
336  O OE1 . GLN   A 42  ? 0.3567 0.3493 0.5125 0.0224  0.0533  0.0103  48  GLN   A OE1 
337  N NE2 . GLN   A 42  ? 0.4071 0.3925 0.5324 0.0130  0.0535  -0.0034 48  GLN   A NE2 
338  N N   . GLY   A 43  ? 0.1717 0.1701 0.2666 0.0176  0.0173  0.0127  49  GLY   A N   
339  C CA  . GLY   A 43  ? 0.1661 0.1621 0.2541 0.0177  0.0153  0.0133  49  GLY   A CA  
340  C C   . GLY   A 43  ? 0.1556 0.1437 0.2450 0.0175  0.0233  0.0102  49  GLY   A C   
341  O O   . GLY   A 43  ? 0.1790 0.1625 0.2712 0.0159  0.0310  0.0055  49  GLY   A O   
342  N N   . CYS   A 44  ? 0.1546 0.1409 0.2398 0.0179  0.0217  0.0118  50  CYS   A N   
343  C CA  . CYS   A 44  ? 0.1614 0.1399 0.2483 0.0174  0.0293  0.0094  50  CYS   A CA  
344  C C   . CYS   A 44  ? 0.1662 0.1412 0.2380 0.0132  0.0296  0.0033  50  CYS   A C   
345  O O   . CYS   A 44  ? 0.1806 0.1491 0.2522 0.0114  0.0364  0.0001  50  CYS   A O   
346  C CB  . CYS   A 44  ? 0.1748 0.1535 0.2723 0.0214  0.0292  0.0171  50  CYS   A CB  
347  S SG  . CYS   A 44  ? 0.2135 0.1970 0.3331 0.0264  0.0310  0.0259  50  CYS   A SG  
348  N N   . ASP   A 45  ? 0.1516 0.1308 0.2119 0.0115  0.0228  0.0020  51  ASP   A N   
349  C CA  . ASP   A 45  ? 0.1461 0.1238 0.1941 0.0076  0.0228  -0.0024 51  ASP   A CA  
350  C C   . ASP   A 45  ? 0.1651 0.1409 0.2088 0.0027  0.0283  -0.0085 51  ASP   A C   
351  O O   . ASP   A 45  ? 0.1878 0.1652 0.2344 0.0023  0.0292  -0.0094 51  ASP   A O   
352  C CB  . ASP   A 45  ? 0.1386 0.1215 0.1783 0.0078  0.0148  -0.0010 51  ASP   A CB  
353  C CG  . ASP   A 45  ? 0.1506 0.1357 0.1915 0.0107  0.0097  0.0039  51  ASP   A CG  
354  O OD1 . ASP   A 45  ? 0.1661 0.1484 0.2092 0.0115  0.0116  0.0057  51  ASP   A OD1 
355  O OD2 . ASP   A 45  ? 0.1601 0.1493 0.1987 0.0113  0.0042  0.0057  51  ASP   A OD2 
356  N N   . THR   A 46  ? 0.1764 0.1498 0.2126 -0.0018 0.0316  -0.0124 52  THR   A N   
357  C CA  . THR   A 46  ? 0.1929 0.1666 0.2218 -0.0086 0.0359  -0.0181 52  THR   A CA  
358  C C   . THR   A 46  ? 0.1806 0.1602 0.1981 -0.0119 0.0304  -0.0179 52  THR   A C   
359  O O   . THR   A 46  ? 0.1952 0.1754 0.2102 -0.0103 0.0270  -0.0158 52  THR   A O   
360  C CB  . THR   A 46  ? 0.2541 0.2207 0.2841 -0.0130 0.0459  -0.0233 52  THR   A CB  
361  O OG1 . THR   A 46  ? 0.3212 0.2858 0.3481 -0.0134 0.0457  -0.0230 52  THR   A OG1 
362  C CG2 . THR   A 46  ? 0.2659 0.2266 0.3105 -0.0089 0.0525  -0.0226 52  THR   A CG2 
363  N N   . ILE   A 47  ? 0.1802 0.1646 0.1918 -0.0162 0.0293  -0.0191 53  ILE   A N   
364  C CA  . ILE   A 47  ? 0.1634 0.1549 0.1668 -0.0190 0.0241  -0.0172 53  ILE   A CA  
365  C C   . ILE   A 47  ? 0.1770 0.1702 0.1722 -0.0274 0.0281  -0.0209 53  ILE   A C   
366  O O   . ILE   A 47  ? 0.1879 0.1794 0.1802 -0.0340 0.0344  -0.0258 53  ILE   A O   
367  C CB  . ILE   A 47  ? 0.1685 0.1658 0.1708 -0.0195 0.0205  -0.0149 53  ILE   A CB  
368  C CG1 . ILE   A 47  ? 0.1734 0.1689 0.1833 -0.0127 0.0174  -0.0122 53  ILE   A CG1 
369  C CG2 . ILE   A 47  ? 0.1657 0.1711 0.1626 -0.0211 0.0150  -0.0107 53  ILE   A CG2 
370  C CD1 . ILE   A 47  ? 0.1760 0.1708 0.1884 -0.0067 0.0125  -0.0087 53  ILE   A CD1 
371  N N   . ALA   A 48  ? 0.1535 0.1507 0.1442 -0.0283 0.0246  -0.0188 54  ALA   A N   
372  C CA  . ALA   A 48  ? 0.1596 0.1610 0.1418 -0.0371 0.0270  -0.0214 54  ALA   A CA  
373  C C   . ALA   A 48  ? 0.1701 0.1816 0.1462 -0.0438 0.0246  -0.0197 54  ALA   A C   
374  O O   . ALA   A 48  ? 0.1685 0.1859 0.1470 -0.0401 0.0187  -0.0141 54  ALA   A O   
375  C CB  . ALA   A 48  ? 0.1636 0.1686 0.1443 -0.0354 0.0227  -0.0181 54  ALA   A CB  
376  N N   . ARG   A 49  ? 0.1921 0.2058 0.1602 -0.0546 0.0299  -0.0247 55  ARG   A N   
377  C CA  . ARG   A 49  ? 0.2010 0.2259 0.1617 -0.0632 0.0278  -0.0228 55  ARG   A CA  
378  C C   . ARG   A 49  ? 0.2344 0.2666 0.1861 -0.0732 0.0285  -0.0240 55  ARG   A C   
379  O O   . ARG   A 49  ? 0.2636 0.2935 0.2077 -0.0834 0.0357  -0.0313 55  ARG   A O   
380  C CB  . ARG   A 49  ? 0.2098 0.2310 0.1687 -0.0683 0.0341  -0.0283 55  ARG   A CB  
381  C CG  . ARG   A 49  ? 0.2143 0.2285 0.1832 -0.0583 0.0336  -0.0271 55  ARG   A CG  
382  C CD  . ARG   A 49  ? 0.1935 0.2146 0.1662 -0.0522 0.0251  -0.0188 55  ARG   A CD  
383  N NE  . ARG   A 49  ? 0.1902 0.2045 0.1716 -0.0444 0.0255  -0.0189 55  ARG   A NE  
384  C CZ  . ARG   A 49  ? 0.1807 0.1965 0.1677 -0.0369 0.0196  -0.0134 55  ARG   A CZ  
385  N NH1 . ARG   A 49  ? 0.1851 0.2082 0.1714 -0.0356 0.0136  -0.0070 55  ARG   A NH1 
386  N NH2 . ARG   A 49  ? 0.2061 0.2161 0.2005 -0.0309 0.0202  -0.0140 55  ARG   A NH2 
387  N N   . CYS   A 50  ? 0.2187 0.2596 0.1715 -0.0705 0.0215  -0.0170 56  CYS   A N   
388  C CA  . CYS   A 50  ? 0.2232 0.2715 0.1697 -0.0781 0.0210  -0.0168 56  CYS   A CA  
389  C C   . CYS   A 50  ? 0.2317 0.2935 0.1820 -0.0748 0.0122  -0.0064 56  CYS   A C   
390  O O   . CYS   A 50  ? 0.2687 0.3326 0.2265 -0.0666 0.0073  0.0002  56  CYS   A O   
391  C CB  . CYS   A 50  ? 0.2125 0.2486 0.1611 -0.0743 0.0257  -0.0222 56  CYS   A CB  
392  S SG  . CYS   A 50  ? 0.2153 0.2459 0.1753 -0.0587 0.0204  -0.0167 56  CYS   A SG  
393  N N   . ASP   A 51  ? 0.2764 0.3471 0.2218 -0.0817 0.0110  -0.0051 57  ASP   A N   
394  C CA  A ASP   A 51  ? 0.2961 0.3796 0.2472 -0.0783 0.0037  0.0050  57  ASP   A CA  
395  C CA  B ASP   A 51  ? 0.2974 0.3820 0.2473 -0.0798 0.0039  0.0047  57  ASP   A CA  
396  C C   . ASP   A 51  ? 0.2916 0.3705 0.2450 -0.0741 0.0043  0.0036  57  ASP   A C   
397  O O   . ASP   A 51  ? 0.2953 0.3859 0.2503 -0.0759 0.0004  0.0096  57  ASP   A O   
398  C CB  A ASP   A 51  ? 0.3432 0.4466 0.2886 -0.0902 -0.0003 0.0113  57  ASP   A CB  
399  C CB  B ASP   A 51  ? 0.3463 0.4489 0.2875 -0.0944 0.0018  0.0079  57  ASP   A CB  
400  C CG  A ASP   A 51  ? 0.4070 0.5144 0.3402 -0.1044 0.0038  0.0048  57  ASP   A CG  
401  C CG  B ASP   A 51  ? 0.4190 0.5401 0.3668 -0.0935 -0.0062 0.0209  57  ASP   A CG  
402  O OD1 A ASP   A 51  ? 0.4067 0.4992 0.3354 -0.1056 0.0112  -0.0059 57  ASP   A OD1 
403  O OD1 B ASP   A 51  ? 0.4261 0.5645 0.3678 -0.1056 -0.0089 0.0254  57  ASP   A OD1 
404  O OD2 A ASP   A 51  ? 0.4524 0.5780 0.3805 -0.1152 -0.0001 0.0105  57  ASP   A OD2 
405  O OD2 B ASP   A 51  ? 0.4657 0.5845 0.4253 -0.0812 -0.0092 0.0268  57  ASP   A OD2 
406  N N   . CYS   A 52  ? 0.2438 0.3062 0.1986 -0.0682 0.0091  -0.0035 58  CYS   A N   
407  C CA  . CYS   A 52  ? 0.2110 0.2684 0.1682 -0.0638 0.0096  -0.0043 58  CYS   A CA  
408  C C   . CYS   A 52  ? 0.2104 0.2740 0.1762 -0.0552 0.0037  0.0040  58  CYS   A C   
409  O O   . CYS   A 52  ? 0.2172 0.2811 0.1898 -0.0481 0.0007  0.0086  58  CYS   A O   
410  C CB  . CYS   A 52  ? 0.2413 0.2813 0.2008 -0.0574 0.0146  -0.0106 58  CYS   A CB  
411  S SG  . CYS   A 52  ? 0.2519 0.2808 0.2043 -0.0661 0.0245  -0.0212 58  CYS   A SG  
412  N N   . GLN   A 53  ? 0.1769 0.2448 0.1430 -0.0560 0.0028  0.0055  59  GLN   A N   
413  C CA  A GLN   A 53  ? 0.1706 0.2429 0.1454 -0.0482 -0.0010 0.0123  59  GLN   A CA  
414  C CA  B GLN   A 53  ? 0.1805 0.2525 0.1553 -0.0481 -0.0010 0.0122  59  GLN   A CA  
415  C C   . GLN   A 53  ? 0.1626 0.2249 0.1377 -0.0437 0.0013  0.0085  59  GLN   A C   
416  O O   . GLN   A 53  ? 0.1641 0.2300 0.1446 -0.0393 -0.0005 0.0125  59  GLN   A O   
417  C CB  A GLN   A 53  ? 0.1579 0.2489 0.1362 -0.0523 -0.0054 0.0210  59  GLN   A CB  
418  C CB  B GLN   A 53  ? 0.1985 0.2896 0.1761 -0.0530 -0.0055 0.0210  59  GLN   A CB  
419  C CG  A GLN   A 53  ? 0.1518 0.2552 0.1350 -0.0531 -0.0094 0.0294  59  GLN   A CG  
420  C CG  B GLN   A 53  ? 0.1885 0.2875 0.1658 -0.0566 -0.0079 0.0252  59  GLN   A CG  
421  C CD  A GLN   A 53  ? 0.1920 0.3148 0.1815 -0.0561 -0.0139 0.0400  59  GLN   A CD  
422  C CD  B GLN   A 53  ? 0.1801 0.2708 0.1648 -0.0466 -0.0083 0.0267  59  GLN   A CD  
423  O OE1 A GLN   A 53  ? 0.2082 0.3460 0.1929 -0.0667 -0.0163 0.0437  59  GLN   A OE1 
424  O OE1 B GLN   A 53  ? 0.1823 0.2710 0.1650 -0.0479 -0.0081 0.0258  59  GLN   A OE1 
425  N NE2 A GLN   A 53  ? 0.1436 0.2677 0.1443 -0.0476 -0.0147 0.0454  59  GLN   A NE2 
426  N NE2 B GLN   A 53  ? 0.1943 0.2797 0.1874 -0.0369 -0.0086 0.0287  59  GLN   A NE2 
427  N N   . THR   A 54  ? 0.1493 0.1990 0.1192 -0.0451 0.0061  0.0009  60  THR   A N   
428  C CA  . THR   A 54  ? 0.1550 0.1942 0.1256 -0.0405 0.0084  -0.0021 60  THR   A CA  
429  C C   . THR   A 54  ? 0.1463 0.1719 0.1182 -0.0356 0.0111  -0.0059 60  THR   A C   
430  O O   . THR   A 54  ? 0.1717 0.1945 0.1415 -0.0389 0.0137  -0.0091 60  THR   A O   
431  C CB  . THR   A 54  ? 0.1868 0.2255 0.1517 -0.0474 0.0117  -0.0057 60  THR   A CB  
432  O OG1 . THR   A 54  ? 0.2788 0.3120 0.2377 -0.0546 0.0168  -0.0118 60  THR   A OG1 
433  C CG2 . THR   A 54  ? 0.1933 0.2469 0.1574 -0.0529 0.0088  -0.0015 60  THR   A CG2 
434  N N   . GLY   A 55  ? 0.1396 0.1582 0.1152 -0.0282 0.0105  -0.0052 61  GLY   A N   
435  C CA  . GLY   A 55  ? 0.1395 0.1474 0.1176 -0.0236 0.0122  -0.0071 61  GLY   A CA  
436  C C   . GLY   A 55  ? 0.1316 0.1346 0.1123 -0.0175 0.0109  -0.0055 61  GLY   A C   
437  O O   . GLY   A 55  ? 0.1376 0.1426 0.1168 -0.0180 0.0104  -0.0046 61  GLY   A O   
438  N N   . VAL   A 56  ? 0.1221 0.1188 0.1062 -0.0126 0.0104  -0.0051 62  VAL   A N   
439  C CA  . VAL   A 56  ? 0.1166 0.1093 0.1022 -0.0081 0.0090  -0.0032 62  VAL   A CA  
440  C C   . VAL   A 56  ? 0.1156 0.1088 0.1042 -0.0037 0.0058  -0.0014 62  VAL   A C   
441  O O   . VAL   A 56  ? 0.1316 0.1240 0.1226 -0.0033 0.0060  -0.0020 62  VAL   A O   
442  C CB  . VAL   A 56  ? 0.1465 0.1312 0.1339 -0.0080 0.0125  -0.0038 62  VAL   A CB  
443  C CG1 . VAL   A 56  ? 0.1723 0.1543 0.1613 -0.0041 0.0103  -0.0005 62  VAL   A CG1 
444  C CG2 . VAL   A 56  ? 0.1510 0.1340 0.1351 -0.0131 0.0167  -0.0063 62  VAL   A CG2 
445  N N   . TYR   A 57  ? 0.1148 0.1091 0.1029 -0.0013 0.0035  0.0001  63  TYR   A N   
446  C CA  . TYR   A 57  ? 0.1125 0.1064 0.1025 0.0017  0.0012  0.0009  63  TYR   A CA  
447  C C   . TYR   A 57  ? 0.1159 0.1071 0.1046 0.0028  -0.0001 0.0022  63  TYR   A C   
448  O O   . TYR   A 57  ? 0.1323 0.1228 0.1182 0.0019  0.0004  0.0027  63  TYR   A O   
449  C CB  . TYR   A 57  ? 0.1185 0.1168 0.1095 0.0026  0.0005  0.0013  63  TYR   A CB  
450  C CG  . TYR   A 57  ? 0.1200 0.1190 0.1095 0.0032  0.0010  0.0014  63  TYR   A CG  
451  C CD1 . TYR   A 57  ? 0.1334 0.1353 0.1219 0.0017  0.0022  0.0018  63  TYR   A CD1 
452  C CD2 . TYR   A 57  ? 0.1259 0.1228 0.1149 0.0044  0.0008  0.0007  63  TYR   A CD2 
453  C CE1 . TYR   A 57  ? 0.1406 0.1432 0.1284 0.0021  0.0034  0.0017  63  TYR   A CE1 
454  C CE2 . TYR   A 57  ? 0.1408 0.1378 0.1283 0.0042  0.0025  -0.0001 63  TYR   A CE2 
455  C CZ  . TYR   A 57  ? 0.1528 0.1525 0.1402 0.0034  0.0039  0.0005  63  TYR   A CZ  
456  O OH  . TYR   A 57  ? 0.1817 0.1817 0.1682 0.0031  0.0064  -0.0005 63  TYR   A OH  
457  N N   . TYR   A 58  ? 0.1156 0.1062 0.1059 0.0042  -0.0020 0.0029  64  TYR   A N   
458  C CA  . TYR   A 58  ? 0.1213 0.1115 0.1096 0.0039  -0.0041 0.0047  64  TYR   A CA  
459  C C   . TYR   A 58  ? 0.1224 0.1138 0.1069 0.0029  -0.0044 0.0028  64  TYR   A C   
460  O O   . TYR   A 58  ? 0.1261 0.1179 0.1120 0.0036  -0.0041 0.0012  64  TYR   A O   
461  C CB  . TYR   A 58  ? 0.1363 0.1266 0.1287 0.0047  -0.0060 0.0071  64  TYR   A CB  
462  C CG  . TYR   A 58  ? 0.1376 0.1299 0.1278 0.0032  -0.0089 0.0103  64  TYR   A CG  
463  C CD1 . TYR   A 58  ? 0.1347 0.1267 0.1240 0.0025  -0.0091 0.0136  64  TYR   A CD1 
464  C CD2 . TYR   A 58  ? 0.1434 0.1384 0.1317 0.0016  -0.0114 0.0102  64  TYR   A CD2 
465  C CE1 . TYR   A 58  ? 0.1653 0.1607 0.1516 0.0001  -0.0122 0.0175  64  TYR   A CE1 
466  C CE2 . TYR   A 58  ? 0.1544 0.1530 0.1391 -0.0016 -0.0144 0.0133  64  TYR   A CE2 
467  C CZ  . TYR   A 58  ? 0.1619 0.1612 0.1458 -0.0023 -0.0151 0.0174  64  TYR   A CZ  
468  O OH  . TYR   A 58  ? 0.1945 0.1988 0.1741 -0.0063 -0.0185 0.0216  64  TYR   A OH  
469  N N   . CYS   A 59  ? 0.1228 0.1143 0.1026 0.0011  -0.0043 0.0031  65  CYS   A N   
470  C CA  . CYS   A 59  ? 0.1343 0.1260 0.1097 -0.0009 -0.0031 0.0004  65  CYS   A CA  
471  C C   . CYS   A 59  ? 0.1389 0.1318 0.1092 -0.0044 -0.0056 0.0017  65  CYS   A C   
472  O O   . CYS   A 59  ? 0.1485 0.1425 0.1151 -0.0064 -0.0067 0.0042  65  CYS   A O   
473  C CB  . CYS   A 59  ? 0.1344 0.1263 0.1078 -0.0014 -0.0004 -0.0006 65  CYS   A CB  
474  S SG  . CYS   A 59  ? 0.1552 0.1462 0.1238 -0.0041 0.0032  -0.0045 65  CYS   A SG  
475  N N   . SER   A 60  ? 0.1405 0.1340 0.1102 -0.0059 -0.0065 0.0004  66  SER   A N   
476  C CA  . SER   A 60  ? 0.1562 0.1531 0.1208 -0.0107 -0.0097 0.0022  66  SER   A CA  
477  C C   . SER   A 60  ? 0.1621 0.1593 0.1176 -0.0160 -0.0079 -0.0003 66  SER   A C   
478  O O   . SER   A 60  ? 0.1820 0.1834 0.1325 -0.0203 -0.0111 0.0031  66  SER   A O   
479  C CB  . SER   A 60  ? 0.1780 0.1760 0.1435 -0.0121 -0.0108 0.0008  66  SER   A CB  
480  O OG  . SER   A 60  ? 0.2051 0.1996 0.1679 -0.0138 -0.0066 -0.0052 66  SER   A OG  
481  N N   . SER   A 61  ? 0.1506 0.1440 0.1050 -0.0156 -0.0026 -0.0055 67  SER   A N   
482  C CA  . SER   A 61  ? 0.1575 0.1503 0.1037 -0.0208 0.0006  -0.0089 67  SER   A CA  
483  C C   . SER   A 61  ? 0.1602 0.1543 0.1041 -0.0209 0.0000  -0.0059 67  SER   A C   
484  O O   . SER   A 61  ? 0.1688 0.1631 0.1055 -0.0256 0.0024  -0.0082 67  SER   A O   
485  C CB  . SER   A 61  ? 0.1698 0.1579 0.1180 -0.0201 0.0077  -0.0151 67  SER   A CB  
486  O OG  . SER   A 61  ? 0.1761 0.1630 0.1321 -0.0141 0.0098  -0.0141 67  SER   A OG  
487  N N   . ARG   A 62  ? 0.1570 0.1519 0.1066 -0.0164 -0.0029 -0.0010 68  ARG   A N   
488  C CA  . ARG   A 62  ? 0.1641 0.1599 0.1122 -0.0167 -0.0038 0.0026  68  ARG   A CA  
489  C C   . ARG   A 62  ? 0.1741 0.1723 0.1254 -0.0158 -0.0087 0.0098  68  ARG   A C   
490  O O   . ARG   A 62  ? 0.1844 0.1826 0.1359 -0.0156 -0.0092 0.0138  68  ARG   A O   
491  C CB  . ARG   A 62  ? 0.1643 0.1577 0.1174 -0.0124 -0.0006 0.0012  68  ARG   A CB  
492  C CG  . ARG   A 62  ? 0.1784 0.1705 0.1306 -0.0129 0.0046  -0.0040 68  ARG   A CG  
493  C CD  . ARG   A 62  ? 0.1837 0.1763 0.1283 -0.0174 0.0065  -0.0051 68  ARG   A CD  
494  N NE  . ARG   A 62  ? 0.2055 0.1967 0.1509 -0.0177 0.0127  -0.0101 68  ARG   A NE  
495  C CZ  . ARG   A 62  ? 0.1970 0.1862 0.1395 -0.0208 0.0169  -0.0150 68  ARG   A CZ  
496  N NH1 . ARG   A 62  ? 0.2022 0.1914 0.1391 -0.0248 0.0148  -0.0159 68  ARG   A NH1 
497  N NH2 . ARG   A 62  ? 0.2133 0.2006 0.1587 -0.0204 0.0238  -0.0191 68  ARG   A NH2 
498  N N   . ARG   A 63  ? 0.1857 0.1854 0.1417 -0.0143 -0.0114 0.0118  69  ARG   A N   
499  C CA  . ARG   A 63  ? 0.2006 0.2022 0.1636 -0.0120 -0.0148 0.0191  69  ARG   A CA  
500  C C   . ARG   A 63  ? 0.2197 0.2168 0.1884 -0.0078 -0.0121 0.0200  69  ARG   A C   
501  O O   . ARG   A 63  ? 0.2467 0.2439 0.2187 -0.0073 -0.0128 0.0259  69  ARG   A O   
502  C CB  . ARG   A 63  ? 0.2480 0.2555 0.2076 -0.0164 -0.0189 0.0261  69  ARG   A CB  
503  C CG  . ARG   A 63  ? 0.2564 0.2697 0.2128 -0.0207 -0.0223 0.0267  69  ARG   A CG  
504  C CD  . ARG   A 63  ? 0.2621 0.2836 0.2196 -0.0240 -0.0276 0.0370  69  ARG   A CD  
505  N NE  . ARG   A 63  ? 0.2690 0.2978 0.2198 -0.0309 -0.0311 0.0368  69  ARG   A NE  
506  C CZ  . ARG   A 63  ? 0.2266 0.2597 0.1649 -0.0394 -0.0318 0.0351  69  ARG   A CZ  
507  N NH1 . ARG   A 63  ? 0.2417 0.2728 0.1735 -0.0415 -0.0297 0.0344  69  ARG   A NH1 
508  N NH2 . ARG   A 63  ? 0.2532 0.2927 0.1849 -0.0468 -0.0343 0.0337  69  ARG   A NH2 
509  N N   . LYS   A 64  ? 0.1818 0.1755 0.1520 -0.0054 -0.0088 0.0148  70  LYS   A N   
510  C CA  . LYS   A 64  ? 0.1855 0.1757 0.1591 -0.0033 -0.0059 0.0146  70  LYS   A CA  
511  C C   . LYS   A 64  ? 0.1714 0.1600 0.1493 -0.0009 -0.0039 0.0111  70  LYS   A C   
512  O O   . LYS   A 64  ? 0.1672 0.1571 0.1443 -0.0005 -0.0039 0.0079  70  LYS   A O   
513  C CB  . LYS   A 64  ? 0.2212 0.2111 0.1889 -0.0054 -0.0037 0.0122  70  LYS   A CB  
514  C CG  . LYS   A 64  ? 0.3418 0.3323 0.3057 -0.0080 -0.0048 0.0166  70  LYS   A CG  
515  C CD  . LYS   A 64  ? 0.4517 0.4410 0.4117 -0.0095 -0.0018 0.0145  70  LYS   A CD  
516  C CE  . LYS   A 64  ? 0.5208 0.5111 0.4763 -0.0127 -0.0031 0.0192  70  LYS   A CE  
517  N NZ  . LYS   A 64  ? 0.5673 0.5620 0.5169 -0.0163 -0.0063 0.0207  70  LYS   A NZ  
518  N N   . HIS   A 65  ? 0.1609 0.1464 0.1431 0.0002  -0.0015 0.0117  71  HIS   A N   
519  C CA  . HIS   A 65  ? 0.1473 0.1320 0.1319 0.0007  0.0009  0.0081  71  HIS   A CA  
520  C C   . HIS   A 65  ? 0.1656 0.1508 0.1467 -0.0013 0.0033  0.0057  71  HIS   A C   
521  O O   . HIS   A 65  ? 0.2188 0.2018 0.1986 -0.0027 0.0049  0.0069  71  HIS   A O   
522  C CB  . HIS   A 65  ? 0.1391 0.1199 0.1299 0.0016  0.0033  0.0093  71  HIS   A CB  
523  C CG  . HIS   A 65  ? 0.1541 0.1355 0.1503 0.0039  0.0012  0.0121  71  HIS   A CG  
524  N ND1 . HIS   A 65  ? 0.1994 0.1813 0.1986 0.0048  0.0014  0.0101  71  HIS   A ND1 
525  C CD2 . HIS   A 65  ? 0.1543 0.1369 0.1535 0.0048  -0.0013 0.0177  71  HIS   A CD2 
526  C CE1 . HIS   A 65  ? 0.1641 0.1472 0.1688 0.0066  -0.0006 0.0141  71  HIS   A CE1 
527  N NE2 . HIS   A 65  ? 0.2011 0.1853 0.2059 0.0065  -0.0026 0.0189  71  HIS   A NE2 
528  N N   . TYR   A 66  ? 0.1435 0.1323 0.1240 -0.0017 0.0036  0.0031  72  TYR   A N   
529  C CA  . TYR   A 66  ? 0.1527 0.1445 0.1312 -0.0039 0.0053  0.0018  72  TYR   A CA  
530  C C   . TYR   A 66  ? 0.1375 0.1319 0.1174 -0.0060 0.0067  0.0003  72  TYR   A C   
531  O O   . TYR   A 66  ? 0.1344 0.1310 0.1167 -0.0050 0.0056  0.0001  72  TYR   A O   
532  C CB  . TYR   A 66  ? 0.1578 0.1541 0.1359 -0.0029 0.0046  0.0015  72  TYR   A CB  
533  C CG  . TYR   A 66  ? 0.1641 0.1587 0.1387 -0.0029 0.0042  0.0018  72  TYR   A CG  
534  C CD1 . TYR   A 66  ? 0.1841 0.1782 0.1552 -0.0048 0.0054  0.0021  72  TYR   A CD1 
535  C CD2 . TYR   A 66  ? 0.1622 0.1560 0.1362 -0.0018 0.0030  0.0014  72  TYR   A CD2 
536  C CE1 . TYR   A 66  ? 0.1972 0.1904 0.1638 -0.0059 0.0053  0.0023  72  TYR   A CE1 
537  C CE2 . TYR   A 66  ? 0.1843 0.1773 0.1535 -0.0035 0.0031  0.0010  72  TYR   A CE2 
538  C CZ  . TYR   A 66  ? 0.1906 0.1835 0.1559 -0.0056 0.0042  0.0016  72  TYR   A CZ  
539  O OH  . TYR   A 66  ? 0.2233 0.2160 0.1828 -0.0083 0.0044  0.0010  72  TYR   A OH  
540  N N   . PRO   A 67  ? 0.1386 0.1335 0.1164 -0.0097 0.0090  -0.0008 73  PRO   A N   
541  C CA  . PRO   A 67  ? 0.1417 0.1414 0.1191 -0.0137 0.0102  -0.0024 73  PRO   A CA  
542  C C   . PRO   A 67  ? 0.1500 0.1594 0.1290 -0.0137 0.0080  -0.0004 73  PRO   A C   
543  O O   . PRO   A 67  ? 0.1897 0.2015 0.1689 -0.0127 0.0077  0.0008  73  PRO   A O   
544  C CB  . PRO   A 67  ? 0.1805 0.1781 0.1546 -0.0187 0.0137  -0.0044 73  PRO   A CB  
545  C CG  . PRO   A 67  ? 0.2050 0.1991 0.1782 -0.0167 0.0137  -0.0029 73  PRO   A CG  
546  C CD  . PRO   A 67  ? 0.1522 0.1438 0.1274 -0.0113 0.0109  -0.0007 73  PRO   A CD  
547  N N   . VAL   A 68  ? 0.1278 0.1426 0.1086 -0.0149 0.0070  0.0003  74  VAL   A N   
548  C CA  . VAL   A 68  ? 0.1501 0.1751 0.1349 -0.0144 0.0049  0.0040  74  VAL   A CA  
549  C C   . VAL   A 68  ? 0.1381 0.1720 0.1223 -0.0199 0.0042  0.0053  74  VAL   A C   
550  O O   . VAL   A 68  ? 0.1495 0.1809 0.1306 -0.0231 0.0051  0.0029  74  VAL   A O   
551  C CB  . VAL   A 68  ? 0.1878 0.2116 0.1776 -0.0086 0.0035  0.0058  74  VAL   A CB  
552  C CG1 . VAL   A 68  ? 0.2088 0.2270 0.1985 -0.0049 0.0043  0.0049  74  VAL   A CG1 
553  C CG2 . VAL   A 68  ? 0.2035 0.2227 0.1929 -0.0078 0.0030  0.0044  74  VAL   A CG2 
554  N N   . SER   A 69  ? 0.1423 0.1878 0.1304 -0.0213 0.0026  0.0099  75  SER   A N   
555  C CA  . SER   A 69  ? 0.1371 0.1950 0.1269 -0.0259 0.0005  0.0140  75  SER   A CA  
556  C C   . SER   A 69  ? 0.1152 0.1765 0.1135 -0.0200 -0.0014 0.0193  75  SER   A C   
557  O O   . SER   A 69  ? 0.1333 0.1928 0.1379 -0.0140 -0.0008 0.0212  75  SER   A O   
558  C CB  . SER   A 69  ? 0.1848 0.2551 0.1760 -0.0305 -0.0004 0.0178  75  SER   A CB  
559  O OG  . SER   A 69  ? 0.2938 0.3795 0.2891 -0.0344 -0.0034 0.0245  75  SER   A OG  
560  N N   . PHE   A 70  ? 0.1288 0.1940 0.1275 -0.0219 -0.0030 0.0212  76  PHE   A N   
561  C CA  . PHE   A 70  ? 0.1310 0.1978 0.1380 -0.0163 -0.0043 0.0261  76  PHE   A CA  
562  C C   . PHE   A 70  ? 0.1367 0.2177 0.1472 -0.0204 -0.0072 0.0334  76  PHE   A C   
563  O O   . PHE   A 70  ? 0.1462 0.2339 0.1498 -0.0288 -0.0083 0.0327  76  PHE   A O   
564  C CB  . PHE   A 70  ? 0.1364 0.1902 0.1411 -0.0123 -0.0031 0.0212  76  PHE   A CB  
565  C CG  . PHE   A 70  ? 0.1317 0.1815 0.1286 -0.0172 -0.0026 0.0164  76  PHE   A CG  
566  C CD1 . PHE   A 70  ? 0.1279 0.1688 0.1183 -0.0190 -0.0001 0.0101  76  PHE   A CD1 
567  C CD2 . PHE   A 70  ? 0.1330 0.1871 0.1298 -0.0198 -0.0038 0.0183  76  PHE   A CD2 
568  C CE1 . PHE   A 70  ? 0.1465 0.1828 0.1317 -0.0231 0.0019  0.0056  76  PHE   A CE1 
569  C CE2 . PHE   A 70  ? 0.1448 0.1946 0.1348 -0.0246 -0.0021 0.0132  76  PHE   A CE2 
570  C CZ  . PHE   A 70  ? 0.1459 0.1863 0.1306 -0.0260 0.0012  0.0067  76  PHE   A CZ  
571  N N   . SER   A 71  ? 0.1279 0.2143 0.1496 -0.0154 -0.0080 0.0408  77  SER   A N   
572  C CA  . SER   A 71  ? 0.1333 0.2351 0.1608 -0.0187 -0.0113 0.0502  77  SER   A CA  
573  C C   . SER   A 71  ? 0.1370 0.2368 0.1591 -0.0217 -0.0124 0.0489  77  SER   A C   
574  O O   . SER   A 71  ? 0.1401 0.2261 0.1572 -0.0191 -0.0104 0.0415  77  SER   A O   
575  C CB  . SER   A 71  ? 0.1492 0.2563 0.1929 -0.0114 -0.0107 0.0594  77  SER   A CB  
576  O OG  . SER   A 71  ? 0.1679 0.2621 0.2160 -0.0038 -0.0078 0.0569  77  SER   A OG  
577  N N   . LYS   A 72  ? 0.1384 0.2525 0.1617 -0.0274 -0.0157 0.0563  78  LYS   A N   
578  C CA  . LYS   A 72  ? 0.1403 0.2539 0.1591 -0.0306 -0.0166 0.0559  78  LYS   A CA  
579  C C   . LYS   A 72  ? 0.1519 0.2589 0.1809 -0.0216 -0.0158 0.0594  78  LYS   A C   
580  O O   . LYS   A 72  ? 0.1598 0.2691 0.2016 -0.0149 -0.0152 0.0661  78  LYS   A O   
581  C CB  . LYS   A 72  ? 0.1616 0.2945 0.1783 -0.0406 -0.0207 0.0639  78  LYS   A CB  
582  C CG  . LYS   A 72  ? 0.1976 0.3356 0.2018 -0.0515 -0.0206 0.0585  78  LYS   A CG  
583  C CD  . LYS   A 72  ? 0.2907 0.4483 0.2900 -0.0638 -0.0246 0.0654  78  LYS   A CD  
584  C CE  . LYS   A 72  ? 0.3793 0.5396 0.3639 -0.0764 -0.0231 0.0576  78  LYS   A CE  
585  N NZ  . LYS   A 72  ? 0.4285 0.6040 0.4041 -0.0901 -0.0256 0.0608  78  LYS   A NZ  
586  N N   . PRO   A 73  ? 0.1455 0.2448 0.1703 -0.0216 -0.0151 0.0554  79  PRO   A N   
587  C CA  . PRO   A 73  ? 0.1470 0.2393 0.1808 -0.0137 -0.0138 0.0580  79  PRO   A CA  
588  C C   . PRO   A 73  ? 0.1578 0.2629 0.2050 -0.0118 -0.0157 0.0713  79  PRO   A C   
589  O O   . PRO   A 73  ? 0.1851 0.3051 0.2315 -0.0186 -0.0193 0.0788  79  PRO   A O   
590  C CB  . PRO   A 73  ? 0.1824 0.2680 0.2078 -0.0168 -0.0134 0.0522  79  PRO   A CB  
591  C CG  . PRO   A 73  ? 0.2331 0.3165 0.2459 -0.0236 -0.0127 0.0438  79  PRO   A CG  
592  C CD  . PRO   A 73  ? 0.1760 0.2711 0.1875 -0.0288 -0.0144 0.0473  79  PRO   A CD  
593  N N   . SER   A 74  ? 0.1484 0.2480 0.2082 -0.0032 -0.0127 0.0745  80  SER   A N   
594  C CA  . SER   A 74  ? 0.1573 0.2686 0.2337 0.0002  -0.0131 0.0883  80  SER   A CA  
595  C C   . SER   A 74  ? 0.1404 0.2397 0.2284 0.0091  -0.0080 0.0888  80  SER   A C   
596  O O   . SER   A 74  ? 0.1439 0.2272 0.2267 0.0123  -0.0045 0.0784  80  SER   A O   
597  C CB  . SER   A 74  ? 0.2208 0.3419 0.3044 0.0008  -0.0133 0.0934  80  SER   A CB  
598  O OG  . SER   A 74  ? 0.3333 0.4603 0.4044 -0.0069 -0.0162 0.0887  80  SER   A OG  
599  N N   . LEU   A 75  ? 0.1520 0.2601 0.2576 0.0131  -0.0071 0.1019  81  LEU   A N   
600  C CA  . LEU   A 75  ? 0.1746 0.2722 0.2941 0.0213  -0.0008 0.1039  81  LEU   A CA  
601  C C   . LEU   A 75  ? 0.1788 0.2741 0.3095 0.0268  0.0044  0.1044  81  LEU   A C   
602  O O   . LEU   A 75  ? 0.1987 0.3089 0.3416 0.0274  0.0032  0.1157  81  LEU   A O   
603  C CB  . LEU   A 75  ? 0.1850 0.2942 0.3192 0.0223  -0.0022 0.1194  81  LEU   A CB  
604  C CG  . LEU   A 75  ? 0.2248 0.3226 0.3738 0.0300  0.0049  0.1222  81  LEU   A CG  
605  C CD1 . LEU   A 75  ? 0.2347 0.3161 0.3717 0.0294  0.0066  0.1104  81  LEU   A CD1 
606  C CD2 . LEU   A 75  ? 0.2434 0.3555 0.4092 0.0311  0.0031  0.1403  81  LEU   A CD2 
607  N N   . ILE   A 76  ? 0.1686 0.2471 0.2947 0.0301  0.0100  0.0926  82  ILE   A N   
608  C CA  . ILE   A 76  ? 0.1897 0.2637 0.3224 0.0340  0.0156  0.0899  82  ILE   A CA  
609  C C   . ILE   A 76  ? 0.2054 0.2643 0.3483 0.0402  0.0251  0.0865  82  ILE   A C   
610  O O   . ILE   A 76  ? 0.1978 0.2439 0.3332 0.0399  0.0269  0.0787  82  ILE   A O   
611  C CB  . ILE   A 76  ? 0.2165 0.2841 0.3311 0.0302  0.0138  0.0771  82  ILE   A CB  
612  C CG1 . ILE   A 76  ? 0.2456 0.3264 0.3490 0.0230  0.0057  0.0788  82  ILE   A CG1 
613  C CG2 . ILE   A 76  ? 0.2398 0.3008 0.3586 0.0335  0.0202  0.0724  82  ILE   A CG2 
614  C CD1 . ILE   A 76  ? 0.2576 0.3365 0.3496 0.0199  0.0044  0.0713  82  ILE   A CD1 
615  N N   . PHE   A 77  ? 0.2215 0.2812 0.3815 0.0454  0.0319  0.0918  83  PHE   A N   
616  C CA  . PHE   A 77  ? 0.2247 0.2688 0.3945 0.0504  0.0429  0.0874  83  PHE   A CA  
617  C C   . PHE   A 77  ? 0.2523 0.2828 0.4071 0.0481  0.0463  0.0718  83  PHE   A C   
618  O O   . PHE   A 77  ? 0.2920 0.3267 0.4418 0.0466  0.0449  0.0692  83  PHE   A O   
619  C CB  . PHE   A 77  ? 0.2307 0.2806 0.4261 0.0568  0.0503  0.0989  83  PHE   A CB  
620  C CG  . PHE   A 77  ? 0.2650 0.2986 0.4731 0.0618  0.0630  0.0958  83  PHE   A CG  
621  C CD1 . PHE   A 77  ? 0.2846 0.3134 0.4998 0.0636  0.0651  0.1001  83  PHE   A CD1 
622  C CD2 . PHE   A 77  ? 0.3040 0.3256 0.5146 0.0634  0.0732  0.0867  83  PHE   A CD2 
623  C CE1 . PHE   A 77  ? 0.3139 0.3263 0.5404 0.0674  0.0777  0.0963  83  PHE   A CE1 
624  C CE2 . PHE   A 77  ? 0.3137 0.3191 0.5349 0.0666  0.0862  0.0825  83  PHE   A CE2 
625  C CZ  . PHE   A 77  ? 0.3191 0.3198 0.5486 0.0687  0.0886  0.0872  83  PHE   A CZ  
626  N N   . VAL   A 78  ? 0.2226 0.2377 0.3689 0.0470  0.0502  0.0616  84  VAL   A N   
627  C CA  . VAL   A 78  ? 0.2124 0.2157 0.3435 0.0436  0.0527  0.0476  84  VAL   A CA  
628  C C   . VAL   A 78  ? 0.2123 0.2011 0.3522 0.0458  0.0656  0.0421  84  VAL   A C   
629  O O   . VAL   A 78  ? 0.2214 0.2039 0.3694 0.0477  0.0703  0.0439  84  VAL   A O   
630  C CB  . VAL   A 78  ? 0.1978 0.1968 0.3101 0.0387  0.0460  0.0400  84  VAL   A CB  
631  C CG1 . VAL   A 78  ? 0.2140 0.2024 0.3110 0.0347  0.0479  0.0269  84  VAL   A CG1 
632  C CG2 . VAL   A 78  ? 0.2059 0.2180 0.3107 0.0362  0.0352  0.0449  84  VAL   A CG2 
633  N N   . GLU   A 79  ? 0.2204 0.2034 0.3562 0.0444  0.0712  0.0343  85  GLU   A N   
634  C CA  . GLU   A 79  ? 0.2552 0.2239 0.3977 0.0450  0.0847  0.0274  85  GLU   A CA  
635  C C   . GLU   A 79  ? 0.2702 0.2259 0.3999 0.0401  0.0868  0.0169  85  GLU   A C   
636  O O   . GLU   A 79  ? 0.2762 0.2334 0.3888 0.0357  0.0776  0.0127  85  GLU   A O   
637  C CB  . GLU   A 79  ? 0.3072 0.2735 0.4453 0.0430  0.0896  0.0205  85  GLU   A CB  
638  C CG  . GLU   A 79  ? 0.3977 0.3752 0.5527 0.0482  0.0911  0.0307  85  GLU   A CG  
639  C CD  . GLU   A 79  ? 0.5334 0.5121 0.7152 0.0554  0.0995  0.0416  85  GLU   A CD  
640  O OE1 . GLU   A 79  ? 0.5673 0.5321 0.7574 0.0565  0.1119  0.0370  85  GLU   A OE1 
641  O OE2 . GLU   A 79  ? 0.5876 0.5818 0.7824 0.0594  0.0938  0.0554  85  GLU   A OE2 
642  N N   . ALA   A 80  ? 0.2762 0.2186 0.4145 0.0404  0.0998  0.0121  86  ALA   A N   
643  C CA  . ALA   A 80  ? 0.3009 0.2304 0.4276 0.0346  0.1036  0.0013  86  ALA   A CA  
644  C C   . ALA   A 80  ? 0.3177 0.2452 0.4215 0.0266  0.0993  -0.0101 86  ALA   A C   
645  O O   . ALA   A 80  ? 0.3350 0.2647 0.4341 0.0252  0.1001  -0.0131 86  ALA   A O   
646  C CB  . ALA   A 80  ? 0.3155 0.2304 0.4548 0.0350  0.1205  -0.0034 86  ALA   A CB  
647  N N   . SER   A 81  ? 0.3193 0.2441 0.4090 0.0213  0.0939  -0.0155 87  SER   A N   
648  C CA  . SER   A 81  ? 0.3191 0.2430 0.3878 0.0132  0.0895  -0.0251 87  SER   A CA  
649  C C   . SER   A 81  ? 0.3272 0.2401 0.3882 0.0063  0.0951  -0.0345 87  SER   A C   
650  O O   . SER   A 81  ? 0.3421 0.2472 0.4143 0.0081  0.1033  -0.0340 87  SER   A O   
651  C CB  . SER   A 81  ? 0.3185 0.2537 0.3770 0.0133  0.0747  -0.0208 87  SER   A CB  
652  O OG  . SER   A 81  ? 0.2911 0.2267 0.3505 0.0138  0.0704  -0.0181 87  SER   A OG  
653  N N   . GLU   A 82  ? 0.3380 0.2520 0.3800 -0.0020 0.0894  -0.0417 88  GLU   A N   
654  C CA  . GLU   A 82  ? 0.3442 0.2505 0.3772 -0.0100 0.0928  -0.0500 88  GLU   A CA  
655  C C   . GLU   A 82  ? 0.3114 0.2199 0.3491 -0.0069 0.0870  -0.0446 88  GLU   A C   
656  O O   . GLU   A 82  ? 0.3237 0.2244 0.3601 -0.0114 0.0921  -0.0496 88  GLU   A O   
657  C CB  . GLU   A 82  ? 0.4106 0.3219 0.4234 -0.0191 0.0854  -0.0559 88  GLU   A CB  
658  C CG  . GLU   A 82  ? 0.5433 0.4488 0.5443 -0.0298 0.0888  -0.0651 88  GLU   A CG  
659  C CD  . GLU   A 82  ? 0.6670 0.5811 0.6499 -0.0383 0.0794  -0.0678 88  GLU   A CD  
660  O OE1 . GLU   A 82  ? 0.7129 0.6297 0.6883 -0.0439 0.0743  -0.0693 88  GLU   A OE1 
661  O OE2 . GLU   A 82  ? 0.6781 0.5967 0.6551 -0.0393 0.0770  -0.0676 88  GLU   A OE2 
662  N N   . TYR   A 83  ? 0.2854 0.2041 0.3282 0.0001  0.0770  -0.0347 89  TYR   A N   
663  C CA  . TYR   A 83  ? 0.2702 0.1922 0.3147 0.0019  0.0704  -0.0299 89  TYR   A CA  
664  C C   . TYR   A 83  ? 0.2542 0.1768 0.3158 0.0098  0.0725  -0.0206 89  TYR   A C   
665  O O   . TYR   A 83  ? 0.2447 0.1670 0.3089 0.0103  0.0704  -0.0180 89  TYR   A O   
666  C CB  . TYR   A 83  ? 0.2783 0.2116 0.3132 0.0018  0.0573  -0.0267 89  TYR   A CB  
667  C CG  . TYR   A 83  ? 0.3005 0.2350 0.3196 -0.0061 0.0540  -0.0339 89  TYR   A CG  
668  C CD1 . TYR   A 83  ? 0.3329 0.2661 0.3434 -0.0128 0.0521  -0.0387 89  TYR   A CD1 
669  C CD2 . TYR   A 83  ? 0.3447 0.2819 0.3578 -0.0075 0.0532  -0.0355 89  TYR   A CD2 
670  C CE1 . TYR   A 83  ? 0.3613 0.2981 0.3580 -0.0204 0.0480  -0.0434 89  TYR   A CE1 
671  C CE2 . TYR   A 83  ? 0.3696 0.3092 0.3685 -0.0150 0.0495  -0.0405 89  TYR   A CE2 
672  C CZ  . TYR   A 83  ? 0.3926 0.3322 0.3835 -0.0217 0.0472  -0.0443 89  TYR   A CZ  
673  O OH  . TYR   A 83  ? 0.4420 0.3866 0.4197 -0.0294 0.0425  -0.0473 89  TYR   A OH  
674  N N   . TYR   A 84  ? 0.2645 0.1893 0.3385 0.0158  0.0762  -0.0145 90  TYR   A N   
675  C CA  . TYR   A 84  ? 0.2497 0.1773 0.3416 0.0231  0.0779  -0.0036 90  TYR   A CA  
676  C C   . TYR   A 84  ? 0.2595 0.1822 0.3673 0.0274  0.0894  -0.0012 90  TYR   A C   
677  O O   . TYR   A 84  ? 0.2696 0.1928 0.3738 0.0264  0.0913  -0.0049 90  TYR   A O   
678  C CB  . TYR   A 84  ? 0.2353 0.1778 0.3279 0.0270  0.0663  0.0062  90  TYR   A CB  
679  C CG  . TYR   A 84  ? 0.2070 0.1553 0.2868 0.0239  0.0555  0.0055  90  TYR   A CG  
680  C CD1 . TYR   A 84  ? 0.2044 0.1526 0.2870 0.0241  0.0536  0.0088  90  TYR   A CD1 
681  C CD2 . TYR   A 84  ? 0.2009 0.1546 0.2672 0.0208  0.0479  0.0019  90  TYR   A CD2 
682  C CE1 . TYR   A 84  ? 0.1863 0.1397 0.2584 0.0214  0.0447  0.0079  90  TYR   A CE1 
683  C CE2 . TYR   A 84  ? 0.1937 0.1521 0.2505 0.0184  0.0394  0.0013  90  TYR   A CE2 
684  C CZ  . TYR   A 84  ? 0.1811 0.1392 0.2408 0.0186  0.0381  0.0040  90  TYR   A CZ  
685  O OH  . TYR   A 84  ? 0.1752 0.1379 0.2268 0.0164  0.0305  0.0034  90  TYR   A OH  
686  N N   . PRO   A 85  ? 0.2727 0.1924 0.3988 0.0327  0.0960  0.0064  91  PRO   A N   
687  C CA  . PRO   A 85  ? 0.2822 0.1999 0.4279 0.0385  0.1064  0.0119  91  PRO   A CA  
688  C C   . PRO   A 85  ? 0.2929 0.2272 0.4443 0.0434  0.0975  0.0231  91  PRO   A C   
689  O O   . PRO   A 85  ? 0.2919 0.2376 0.4332 0.0423  0.0846  0.0268  91  PRO   A O   
690  C CB  . PRO   A 85  ? 0.3053 0.2170 0.4694 0.0429  0.1140  0.0191  91  PRO   A CB  
691  C CG  . PRO   A 85  ? 0.3142 0.2332 0.4710 0.0419  0.1024  0.0237  91  PRO   A CG  
692  C CD  . PRO   A 85  ? 0.2776 0.1969 0.4095 0.0342  0.0942  0.0121  91  PRO   A CD  
693  N N   . ALA   A 86  ? 0.2937 0.2301 0.4620 0.0485  0.1046  0.0292  92  ALA   A N   
694  C CA  . ALA   A 86  ? 0.2826 0.2361 0.4580 0.0527  0.0966  0.0410  92  ALA   A CA  
695  C C   . ALA   A 86  ? 0.2747 0.2387 0.4593 0.0559  0.0893  0.0546  92  ALA   A C   
696  O O   . ALA   A 86  ? 0.2920 0.2497 0.4896 0.0587  0.0958  0.0589  92  ALA   A O   
697  C CB  . ALA   A 86  ? 0.2731 0.2265 0.4691 0.0581  0.1073  0.0461  92  ALA   A CB  
698  N N   . ARG   A 87  ? 0.2606 0.2391 0.4354 0.0541  0.0760  0.0595  93  ARG   A N   
699  C CA  . ARG   A 87  ? 0.2421 0.2306 0.4211 0.0549  0.0685  0.0705  93  ARG   A CA  
700  C C   . ARG   A 87  ? 0.2205 0.2265 0.3909 0.0525  0.0561  0.0760  93  ARG   A C   
701  O O   . ARG   A 87  ? 0.2362 0.2442 0.3964 0.0502  0.0535  0.0700  93  ARG   A O   
702  C CB  . ARG   A 87  ? 0.2587 0.2377 0.4238 0.0508  0.0665  0.0623  93  ARG   A CB  
703  C CG  . ARG   A 87  ? 0.2696 0.2527 0.4114 0.0447  0.0555  0.0545  93  ARG   A CG  
704  C CD  . ARG   A 87  ? 0.2556 0.2265 0.3840 0.0405  0.0566  0.0428  93  ARG   A CD  
705  N NE  . ARG   A 87  ? 0.2526 0.2288 0.3636 0.0359  0.0463  0.0387  93  ARG   A NE  
706  C CZ  . ARG   A 87  ? 0.2607 0.2401 0.3587 0.0330  0.0411  0.0331  93  ARG   A CZ  
707  N NH1 . ARG   A 87  ? 0.2675 0.2462 0.3661 0.0337  0.0442  0.0306  93  ARG   A NH1 
708  N NH2 . ARG   A 87  ? 0.2020 0.1847 0.2870 0.0293  0.0333  0.0299  93  ARG   A NH2 
709  N N   . TYR   A 88  ? 0.2187 0.2365 0.3916 0.0519  0.0487  0.0865  94  TYR   A N   
710  C CA  . TYR   A 88  ? 0.2307 0.2638 0.3926 0.0475  0.0375  0.0898  94  TYR   A CA  
711  C C   . TYR   A 88  ? 0.1993 0.2272 0.3398 0.0419  0.0316  0.0792  94  TYR   A C   
712  O O   . TYR   A 88  ? 0.2133 0.2358 0.3522 0.0412  0.0318  0.0784  94  TYR   A O   
713  C CB  . TYR   A 88  ? 0.2342 0.2840 0.4082 0.0480  0.0325  0.1064  94  TYR   A CB  
714  C CG  . TYR   A 88  ? 0.2301 0.2911 0.4249 0.0527  0.0355  0.1193  94  TYR   A CG  
715  C CD1 . TYR   A 88  ? 0.2306 0.3052 0.4227 0.0504  0.0303  0.1221  94  TYR   A CD1 
716  C CD2 . TYR   A 88  ? 0.2435 0.3007 0.4617 0.0596  0.0446  0.1281  94  TYR   A CD2 
717  C CE1 . TYR   A 88  ? 0.2427 0.3287 0.4549 0.0546  0.0330  0.1342  94  TYR   A CE1 
718  C CE2 . TYR   A 88  ? 0.2445 0.3124 0.4842 0.0645  0.0479  0.1408  94  TYR   A CE2 
719  C CZ  . TYR   A 88  ? 0.2464 0.3292 0.4830 0.0620  0.0419  0.1437  94  TYR   A CZ  
720  O OH  . TYR   A 88  ? 0.2807 0.3757 0.5387 0.0664  0.0447  0.1563  94  TYR   A OH  
721  N N   . GLN   A 89  ? 0.1743 0.2046 0.2994 0.0378  0.0264  0.0718  95  GLN   A N   
722  C CA  . GLN   A 89  ? 0.1597 0.1867 0.2664 0.0328  0.0209  0.0630  95  GLN   A CA  
723  C C   . GLN   A 89  ? 0.1521 0.1942 0.2534 0.0284  0.0127  0.0691  95  GLN   A C   
724  O O   . GLN   A 89  ? 0.1565 0.2093 0.2602 0.0275  0.0104  0.0741  95  GLN   A O   
725  C CB  . GLN   A 89  ? 0.1655 0.1835 0.2600 0.0312  0.0221  0.0508  95  GLN   A CB  
726  C CG  . GLN   A 89  ? 0.1667 0.1817 0.2451 0.0268  0.0169  0.0430  95  GLN   A CG  
727  C CD  . GLN   A 89  ? 0.1592 0.1637 0.2274 0.0254  0.0187  0.0319  95  GLN   A CD  
728  O OE1 . GLN   A 89  ? 0.1774 0.1726 0.2481 0.0268  0.0249  0.0273  95  GLN   A OE1 
729  N NE2 . GLN   A 89  ? 0.1541 0.1604 0.2103 0.0220  0.0136  0.0274  95  GLN   A NE2 
730  N N   . SER   A 90  ? 0.1384 0.1818 0.2321 0.0248  0.0087  0.0684  96  SER   A N   
731  C CA  . SER   A 90  ? 0.1418 0.1986 0.2291 0.0191  0.0020  0.0731  96  SER   A CA  
732  C C   . SER   A 90  ? 0.1305 0.1843 0.2009 0.0143  -0.0010 0.0625  96  SER   A C   
733  O O   . SER   A 90  ? 0.1336 0.1751 0.1976 0.0155  0.0012  0.0527  96  SER   A O   
734  C CB  . SER   A 90  ? 0.1630 0.2238 0.2526 0.0174  0.0002  0.0794  96  SER   A CB  
735  O OG  . SER   A 90  ? 0.2054 0.2539 0.2870 0.0170  0.0015  0.0700  96  SER   A OG  
736  N N   . HIS   A 91  ? 0.1309 0.1965 0.1949 0.0082  -0.0056 0.0652  97  HIS   A N   
737  C CA  . HIS   A 91  ? 0.1302 0.1938 0.1797 0.0030  -0.0075 0.0563  97  HIS   A CA  
738  C C   . HIS   A 91  ? 0.1265 0.1815 0.1728 0.0057  -0.0053 0.0487  97  HIS   A C   
739  O O   . HIS   A 91  ? 0.1347 0.1817 0.1714 0.0042  -0.0050 0.0398  97  HIS   A O   
740  C CB  . HIS   A 91  ? 0.1508 0.2071 0.1928 0.0009  -0.0075 0.0502  97  HIS   A CB  
741  C CG  . HIS   A 91  ? 0.1603 0.2251 0.2035 -0.0028 -0.0096 0.0570  97  HIS   A CG  
742  N ND1 . HIS   A 91  ? 0.1978 0.2711 0.2319 -0.0110 -0.0122 0.0568  97  HIS   A ND1 
743  C CD2 . HIS   A 91  ? 0.1836 0.2498 0.2361 0.0000  -0.0091 0.0645  97  HIS   A CD2 
744  C CE1 . HIS   A 91  ? 0.1969 0.2769 0.2339 -0.0133 -0.0136 0.0639  97  HIS   A CE1 
745  N NE2 . HIS   A 91  ? 0.2016 0.2779 0.2503 -0.0065 -0.0121 0.0693  97  HIS   A NE2 
746  N N   . LEU   A 92  ? 0.1146 0.1719 0.1690 0.0092  -0.0035 0.0525  98  LEU   A N   
747  C CA  . LEU   A 92  ? 0.1171 0.1671 0.1690 0.0114  -0.0011 0.0460  98  LEU   A CA  
748  C C   . LEU   A 92  ? 0.1168 0.1761 0.1653 0.0076  -0.0033 0.0475  98  LEU   A C   
749  O O   . LEU   A 92  ? 0.1220 0.1946 0.1767 0.0057  -0.0054 0.0563  98  LEU   A O   
750  C CB  . LEU   A 92  ? 0.1326 0.1779 0.1964 0.0176  0.0039  0.0484  98  LEU   A CB  
751  C CG  . LEU   A 92  ? 0.1617 0.1982 0.2223 0.0195  0.0074  0.0411  98  LEU   A CG  
752  C CD1 . LEU   A 92  ? 0.1797 0.2047 0.2299 0.0186  0.0076  0.0316  98  LEU   A CD1 
753  C CD2 . LEU   A 92  ? 0.2043 0.2369 0.2778 0.0247  0.0138  0.0437  98  LEU   A CD2 
754  N N   . MET   A 93  ? 0.1267 0.1798 0.1661 0.0062  -0.0029 0.0397  99  MET   A N   
755  C CA  . MET   A 93  ? 0.1188 0.1784 0.1538 0.0023  -0.0042 0.0395  99  MET   A CA  
756  C C   . MET   A 93  ? 0.1231 0.1766 0.1599 0.0060  -0.0012 0.0362  99  MET   A C   
757  O O   . MET   A 93  ? 0.1416 0.1834 0.1745 0.0085  0.0008  0.0297  99  MET   A O   
758  C CB  . MET   A 93  ? 0.1364 0.1926 0.1591 -0.0032 -0.0054 0.0326  99  MET   A CB  
759  C CG  . MET   A 93  ? 0.1485 0.2102 0.1682 -0.0080 -0.0075 0.0346  99  MET   A CG  
760  S SD  . MET   A 93  ? 0.1832 0.2386 0.1902 -0.0141 -0.0066 0.0258  99  MET   A SD  
761  C CE  . MET   A 93  ? 0.2464 0.2856 0.2539 -0.0071 -0.0044 0.0194  99  MET   A CE  
762  N N   . LEU   A 94  ? 0.1204 0.1820 0.1621 0.0058  -0.0009 0.0404  100 LEU   A N   
763  C CA  . LEU   A 94  ? 0.1248 0.1810 0.1680 0.0088  0.0025  0.0373  100 LEU   A CA  
764  C C   . LEU   A 94  ? 0.1219 0.1794 0.1563 0.0045  0.0013  0.0334  100 LEU   A C   
765  O O   . LEU   A 94  ? 0.1363 0.2034 0.1677 -0.0009 -0.0015 0.0360  100 LEU   A O   
766  C CB  . LEU   A 94  ? 0.1461 0.2096 0.2042 0.0128  0.0052  0.0450  100 LEU   A CB  
767  C CG  . LEU   A 94  ? 0.2006 0.2612 0.2705 0.0181  0.0085  0.0491  100 LEU   A CG  
768  C CD1 . LEU   A 94  ? 0.2209 0.2867 0.3073 0.0227  0.0133  0.0560  100 LEU   A CD1 
769  C CD2 . LEU   A 94  ? 0.2460 0.2908 0.3111 0.0205  0.0123  0.0406  100 LEU   A CD2 
770  N N   . ALA   A 95  ? 0.1257 0.1741 0.1560 0.0062  0.0039  0.0276  101 ALA   A N   
771  C CA  . ALA   A 95  ? 0.1264 0.1748 0.1495 0.0028  0.0036  0.0243  101 ALA   A CA  
772  C C   . ALA   A 95  ? 0.1229 0.1666 0.1483 0.0059  0.0074  0.0223  101 ALA   A C   
773  O O   . ALA   A 95  ? 0.1293 0.1667 0.1589 0.0098  0.0106  0.0211  101 ALA   A O   
774  C CB  . ALA   A 95  ? 0.1501 0.1896 0.1617 0.0001  0.0025  0.0178  101 ALA   A CB  
775  N N   . VAL   A 96  ? 0.1211 0.1668 0.1426 0.0032  0.0077  0.0209  102 VAL   A N   
776  C CA  . VAL   A 96  ? 0.1215 0.1622 0.1428 0.0049  0.0113  0.0180  102 VAL   A CA  
777  C C   . VAL   A 96  ? 0.1509 0.1804 0.1607 0.0037  0.0109  0.0115  102 VAL   A C   
778  O O   . VAL   A 96  ? 0.1842 0.2126 0.1869 0.0004  0.0086  0.0099  102 VAL   A O   
779  C CB  . VAL   A 96  ? 0.1268 0.1759 0.1496 0.0023  0.0116  0.0203  102 VAL   A CB  
780  C CG1 . VAL   A 96  ? 0.1483 0.1915 0.1689 0.0032  0.0156  0.0165  102 VAL   A CG1 
781  C CG2 . VAL   A 96  ? 0.1270 0.1892 0.1631 0.0036  0.0117  0.0284  102 VAL   A CG2 
782  N N   . GLY   A 97  ? 0.1539 0.1759 0.1631 0.0059  0.0134  0.0085  103 GLY   A N   
783  C CA  . GLY   A 97  ? 0.1745 0.1880 0.1740 0.0044  0.0124  0.0039  103 GLY   A CA  
784  C C   . GLY   A 97  ? 0.1850 0.1925 0.1842 0.0056  0.0155  0.0009  103 GLY   A C   
785  O O   . GLY   A 97  ? 0.1938 0.2015 0.2004 0.0080  0.0188  0.0016  103 GLY   A O   
786  N N   . HIS   A 98  ? 0.2058 0.2078 0.1959 0.0031  0.0148  -0.0024 104 HIS   A N   
787  C CA  . HIS   A 98  ? 0.2237 0.2204 0.2108 0.0021  0.0176  -0.0061 104 HIS   A CA  
788  C C   . HIS   A 98  ? 0.2055 0.1995 0.1930 0.0028  0.0159  -0.0067 104 HIS   A C   
789  O O   . HIS   A 98  ? 0.2003 0.1946 0.1858 0.0028  0.0113  -0.0051 104 HIS   A O   
790  C CB  . HIS   A 98  ? 0.2276 0.2217 0.2044 -0.0020 0.0166  -0.0082 104 HIS   A CB  
791  C CG  . HIS   A 98  ? 0.2379 0.2277 0.2098 -0.0051 0.0200  -0.0125 104 HIS   A CG  
792  N ND1 . HIS   A 98  ? 0.2401 0.2283 0.2145 -0.0056 0.0269  -0.0158 104 HIS   A ND1 
793  C CD2 . HIS   A 98  ? 0.2513 0.2388 0.2167 -0.0083 0.0179  -0.0142 104 HIS   A CD2 
794  C CE1 . HIS   A 98  ? 0.2533 0.2371 0.2217 -0.0097 0.0294  -0.0203 104 HIS   A CE1 
795  N NE2 . HIS   A 98  ? 0.2614 0.2455 0.2235 -0.0118 0.0235  -0.0192 104 HIS   A NE2 
796  N N   . SER   A 99  ? 0.2217 0.2125 0.2122 0.0032  0.0201  -0.0091 105 SER   A N   
797  C CA  . SER   A 99  ? 0.2146 0.2021 0.2044 0.0028  0.0194  -0.0107 105 SER   A CA  
798  C C   . SER   A 99  ? 0.2340 0.2158 0.2218 0.0000  0.0256  -0.0159 105 SER   A C   
799  O O   . SER   A 99  ? 0.2738 0.2543 0.2658 0.0005  0.0320  -0.0175 105 SER   A O   
800  C CB  . SER   A 99  ? 0.2277 0.2175 0.2259 0.0066  0.0179  -0.0071 105 SER   A CB  
801  O OG  . SER   A 99  ? 0.2587 0.2500 0.2670 0.0097  0.0227  -0.0050 105 SER   A OG  
802  N N   . GLU   A 100 ? 0.1974 0.1762 0.1799 -0.0031 0.0243  -0.0187 106 GLU   A N   
803  C CA  . GLU   A 100 ? 0.2161 0.1891 0.1950 -0.0075 0.0299  -0.0246 106 GLU   A CA  
804  C C   . GLU   A 100 ? 0.2296 0.2011 0.2109 -0.0069 0.0281  -0.0244 106 GLU   A C   
805  O O   . GLU   A 100 ? 0.2011 0.1764 0.1844 -0.0041 0.0218  -0.0201 106 GLU   A O   
806  C CB  . GLU   A 100 ? 0.2343 0.2076 0.1999 -0.0151 0.0285  -0.0280 106 GLU   A CB  
807  C CG  . GLU   A 100 ? 0.2531 0.2277 0.2157 -0.0160 0.0304  -0.0281 106 GLU   A CG  
808  C CD  . GLU   A 100 ? 0.2839 0.2599 0.2333 -0.0238 0.0292  -0.0305 106 GLU   A CD  
809  O OE1 . GLU   A 100 ? 0.3583 0.3331 0.2996 -0.0306 0.0298  -0.0343 106 GLU   A OE1 
810  O OE2 . GLU   A 100 ? 0.2612 0.2401 0.2080 -0.0237 0.0273  -0.0280 106 GLU   A OE2 
811  N N   . PRO   A 101 ? 0.2409 0.2065 0.2231 -0.0094 0.0344  -0.0292 107 PRO   A N   
812  C CA  . PRO   A 101 ? 0.2417 0.2056 0.2277 -0.0083 0.0332  -0.0287 107 PRO   A CA  
813  C C   . PRO   A 101 ? 0.2306 0.1991 0.2104 -0.0104 0.0245  -0.0266 107 PRO   A C   
814  O O   . PRO   A 101 ? 0.2221 0.1929 0.2074 -0.0064 0.0206  -0.0227 107 PRO   A O   
815  C CB  . PRO   A 101 ? 0.2798 0.2354 0.2646 -0.0130 0.0425  -0.0359 107 PRO   A CB  
816  C CG  . PRO   A 101 ? 0.2973 0.2501 0.2853 -0.0123 0.0501  -0.0380 107 PRO   A CG  
817  C CD  . PRO   A 101 ? 0.2564 0.2155 0.2380 -0.0129 0.0443  -0.0355 107 PRO   A CD  
818  N N   . GLY   A 102 ? 0.2137 0.1849 0.1829 -0.0165 0.0212  -0.0282 108 GLY   A N   
819  C CA  . GLY   A 102 ? 0.2097 0.1865 0.1747 -0.0186 0.0133  -0.0250 108 GLY   A CA  
820  C C   . GLY   A 102 ? 0.1788 0.1606 0.1479 -0.0132 0.0072  -0.0185 108 GLY   A C   
821  O O   . GLY   A 102 ? 0.1808 0.1668 0.1497 -0.0135 0.0015  -0.0150 108 GLY   A O   
822  N N   . ASP   A 103 ? 0.1626 0.1438 0.1362 -0.0086 0.0089  -0.0168 109 ASP   A N   
823  C CA  . ASP   A 103 ? 0.1512 0.1361 0.1288 -0.0043 0.0045  -0.0118 109 ASP   A CA  
824  C C   . ASP   A 103 ? 0.1462 0.1315 0.1311 -0.0003 0.0034  -0.0097 109 ASP   A C   
825  O O   . ASP   A 103 ? 0.1440 0.1319 0.1313 0.0019  0.0001  -0.0064 109 ASP   A O   
826  C CB  . ASP   A 103 ? 0.1521 0.1375 0.1313 -0.0020 0.0067  -0.0108 109 ASP   A CB  
827  C CG  . ASP   A 103 ? 0.1567 0.1427 0.1284 -0.0057 0.0064  -0.0116 109 ASP   A CG  
828  O OD1 . ASP   A 103 ? 0.1676 0.1559 0.1346 -0.0085 0.0022  -0.0098 109 ASP   A OD1 
829  O OD2 . ASP   A 103 ? 0.1653 0.1503 0.1367 -0.0058 0.0106  -0.0133 109 ASP   A OD2 
830  N N   . CYS   A 104 ? 0.1440 0.1262 0.1323 0.0001  0.0066  -0.0117 110 CYS   A N   
831  C CA  . CYS   A 104 ? 0.1463 0.1294 0.1410 0.0032  0.0054  -0.0094 110 CYS   A CA  
832  C C   . CYS   A 104 ? 0.1420 0.1277 0.1351 0.0022  0.0003  -0.0078 110 CYS   A C   
833  O O   . CYS   A 104 ? 0.1507 0.1372 0.1394 -0.0013 -0.0017 -0.0088 110 CYS   A O   
834  C CB  . CYS   A 104 ? 0.1612 0.1400 0.1594 0.0029  0.0097  -0.0118 110 CYS   A CB  
835  S SG  . CYS   A 104 ? 0.1773 0.1537 0.1836 0.0063  0.0166  -0.0110 110 CYS   A SG  
836  N N   . GLY   A 105 ? 0.1299 0.1179 0.1273 0.0050  -0.0015 -0.0050 111 GLY   A N   
837  C CA  . GLY   A 105 ? 0.1374 0.1274 0.1358 0.0049  -0.0049 -0.0033 111 GLY   A CA  
838  C C   . GLY   A 105 ? 0.1352 0.1269 0.1333 0.0056  -0.0064 -0.0011 111 GLY   A C   
839  O O   . GLY   A 105 ? 0.1394 0.1322 0.1406 0.0063  -0.0077 0.0006  111 GLY   A O   
840  N N   . GLY   A 106 ? 0.1300 0.1215 0.1249 0.0053  -0.0056 -0.0012 112 GLY   A N   
841  C CA  . GLY   A 106 ? 0.1281 0.1203 0.1229 0.0057  -0.0062 0.0008  112 GLY   A CA  
842  C C   . GLY   A 106 ? 0.1162 0.1088 0.1143 0.0069  -0.0049 0.0010  112 GLY   A C   
843  O O   . GLY   A 106 ? 0.1225 0.1163 0.1216 0.0073  -0.0036 0.0006  112 GLY   A O   
844  N N   . ILE   A 107 ? 0.1193 0.1112 0.1193 0.0070  -0.0047 0.0021  113 ILE   A N   
845  C CA  . ILE   A 107 ? 0.1202 0.1124 0.1220 0.0064  -0.0025 0.0012  113 ILE   A CA  
846  C C   . ILE   A 107 ? 0.1126 0.1057 0.1114 0.0048  -0.0009 0.0007  113 ILE   A C   
847  O O   . ILE   A 107 ? 0.1163 0.1080 0.1133 0.0045  -0.0006 0.0011  113 ILE   A O   
848  C CB  . ILE   A 107 ? 0.1196 0.1095 0.1256 0.0067  -0.0012 0.0018  113 ILE   A CB  
849  C CG1 . ILE   A 107 ? 0.1432 0.1340 0.1530 0.0077  -0.0025 0.0021  113 ILE   A CG1 
850  C CG2 . ILE   A 107 ? 0.1332 0.1218 0.1394 0.0045  0.0027  -0.0002 113 ILE   A CG2 
851  C CD1 . ILE   A 107 ? 0.1791 0.1687 0.1956 0.0087  -0.0013 0.0037  113 ILE   A CD1 
852  N N   . LEU   A 108 ? 0.1062 0.1025 0.1046 0.0031  0.0000  0.0002  114 LEU   A N   
853  C CA  . LEU   A 108 ? 0.1094 0.1083 0.1052 0.0000  0.0017  -0.0003 114 LEU   A CA  
854  C C   . LEU   A 108 ? 0.1089 0.1061 0.1046 -0.0032 0.0045  -0.0025 114 LEU   A C   
855  O O   . LEU   A 108 ? 0.1186 0.1167 0.1158 -0.0037 0.0047  -0.0028 114 LEU   A O   
856  C CB  . LEU   A 108 ? 0.1146 0.1204 0.1109 -0.0009 0.0006  0.0018  114 LEU   A CB  
857  C CG  . LEU   A 108 ? 0.1178 0.1294 0.1114 -0.0056 0.0015  0.0022  114 LEU   A CG  
858  C CD1 . LEU   A 108 ? 0.1310 0.1419 0.1224 -0.0060 0.0022  0.0018  114 LEU   A CD1 
859  C CD2 . LEU   A 108 ? 0.1386 0.1592 0.1352 -0.0061 -0.0003 0.0065  114 LEU   A CD2 
860  N N   . ARG   A 109 ? 0.1166 0.1113 0.1104 -0.0059 0.0076  -0.0043 115 ARG   A N   
861  C CA  . ARG   A 109 ? 0.1247 0.1160 0.1183 -0.0098 0.0124  -0.0076 115 ARG   A CA  
862  C C   . ARG   A 109 ? 0.1318 0.1244 0.1203 -0.0157 0.0154  -0.0100 115 ARG   A C   
863  O O   . ARG   A 109 ? 0.1354 0.1294 0.1218 -0.0159 0.0143  -0.0089 115 ARG   A O   
864  C CB  . ARG   A 109 ? 0.1417 0.1255 0.1412 -0.0064 0.0149  -0.0075 115 ARG   A CB  
865  C CG  . ARG   A 109 ? 0.1485 0.1285 0.1483 -0.0052 0.0157  -0.0062 115 ARG   A CG  
866  C CD  . ARG   A 109 ? 0.1681 0.1423 0.1759 -0.0017 0.0178  -0.0040 115 ARG   A CD  
867  N NE  . ARG   A 109 ? 0.1779 0.1548 0.1890 0.0027  0.0127  -0.0002 115 ARG   A NE  
868  C CZ  . ARG   A 109 ? 0.1696 0.1461 0.1875 0.0050  0.0129  0.0013  115 ARG   A CZ  
869  N NH1 . ARG   A 109 ? 0.1805 0.1537 0.2024 0.0036  0.0182  -0.0013 115 ARG   A NH1 
870  N NH2 . ARG   A 109 ? 0.1832 0.1630 0.2033 0.0078  0.0079  0.0051  115 ARG   A NH2 
871  N N   . CYS   A 110 ? 0.1613 0.1533 0.1475 -0.0215 0.0198  -0.0137 116 CYS   A N   
872  C CA  . CYS   A 110 ? 0.2058 0.1989 0.1859 -0.0295 0.0240  -0.0173 116 CYS   A CA  
873  C C   . CYS   A 110 ? 0.2390 0.2224 0.2208 -0.0321 0.0320  -0.0224 116 CYS   A C   
874  O O   . CYS   A 110 ? 0.2247 0.2015 0.2137 -0.0268 0.0338  -0.0219 116 CYS   A O   
875  C CB  . CYS   A 110 ? 0.1993 0.2032 0.1736 -0.0362 0.0218  -0.0169 116 CYS   A CB  
876  S SG  . CYS   A 110 ? 0.1943 0.1982 0.1678 -0.0401 0.0247  -0.0198 116 CYS   A SG  
877  N N   . GLN   A 111 ? 0.2722 0.2547 0.2478 -0.0410 0.0378  -0.0274 117 GLN   A N   
878  C CA  . GLN   A 111 ? 0.3129 0.2848 0.2907 -0.0443 0.0475  -0.0332 117 GLN   A CA  
879  C C   . GLN   A 111 ? 0.3152 0.2851 0.2957 -0.0449 0.0508  -0.0357 117 GLN   A C   
880  O O   . GLN   A 111 ? 0.3508 0.3106 0.3378 -0.0439 0.0587  -0.0388 117 GLN   A O   
881  C CB  . GLN   A 111 ? 0.3762 0.3470 0.3454 -0.0556 0.0543  -0.0396 117 GLN   A CB  
882  C CG  . GLN   A 111 ? 0.4468 0.4287 0.4058 -0.0659 0.0528  -0.0419 117 GLN   A CG  
883  C CD  . GLN   A 111 ? 0.5304 0.5138 0.4795 -0.0787 0.0585  -0.0480 117 GLN   A CD  
884  O OE1 . GLN   A 111 ? 0.5544 0.5476 0.4979 -0.0825 0.0536  -0.0454 117 GLN   A OE1 
885  N NE2 . GLN   A 111 ? 0.5328 0.5070 0.4796 -0.0862 0.0694  -0.0563 117 GLN   A NE2 
886  N N   . HIS   A 112 ? 0.2592 0.2384 0.2363 -0.0459 0.0451  -0.0336 118 HIS   A N   
887  C CA  . HIS   A 112 ? 0.2538 0.2323 0.2324 -0.0474 0.0480  -0.0359 118 HIS   A CA  
888  C C   . HIS   A 112 ? 0.2434 0.2200 0.2319 -0.0372 0.0441  -0.0313 118 HIS   A C   
889  O O   . HIS   A 112 ? 0.2735 0.2485 0.2651 -0.0373 0.0470  -0.0330 118 HIS   A O   
890  C CB  . HIS   A 112 ? 0.2554 0.2458 0.2246 -0.0552 0.0443  -0.0356 118 HIS   A CB  
891  C CG  . HIS   A 112 ? 0.2767 0.2714 0.2355 -0.0669 0.0474  -0.0397 118 HIS   A CG  
892  N ND1 . HIS   A 112 ? 0.2745 0.2805 0.2282 -0.0694 0.0407  -0.0352 118 HIS   A ND1 
893  C CD2 . HIS   A 112 ? 0.3146 0.3049 0.2669 -0.0777 0.0569  -0.0479 118 HIS   A CD2 
894  C CE1 . HIS   A 112 ? 0.3240 0.3324 0.2684 -0.0813 0.0455  -0.0404 118 HIS   A CE1 
895  N NE2 . HIS   A 112 ? 0.3461 0.3449 0.2887 -0.0871 0.0556  -0.0486 118 HIS   A NE2 
896  N N   . GLY   A 113 ? 0.2140 0.1921 0.2065 -0.0292 0.0373  -0.0255 119 GLY   A N   
897  C CA  . GLY   A 113 ? 0.1961 0.1737 0.1965 -0.0211 0.0332  -0.0213 119 GLY   A CA  
898  C C   . GLY   A 113 ? 0.1624 0.1469 0.1611 -0.0169 0.0243  -0.0161 119 GLY   A C   
899  O O   . GLY   A 113 ? 0.1650 0.1531 0.1591 -0.0181 0.0217  -0.0149 119 GLY   A O   
900  N N   . VAL   A 114 ? 0.1465 0.1326 0.1496 -0.0122 0.0205  -0.0133 120 VAL   A N   
901  C CA  . VAL   A 114 ? 0.1433 0.1342 0.1457 -0.0083 0.0137  -0.0091 120 VAL   A CA  
902  C C   . VAL   A 114 ? 0.1235 0.1220 0.1210 -0.0118 0.0112  -0.0081 120 VAL   A C   
903  O O   . VAL   A 114 ? 0.1353 0.1364 0.1315 -0.0154 0.0124  -0.0091 120 VAL   A O   
904  C CB  . VAL   A 114 ? 0.1378 0.1276 0.1463 -0.0033 0.0111  -0.0070 120 VAL   A CB  
905  C CG1 . VAL   A 114 ? 0.1529 0.1466 0.1602 -0.0005 0.0057  -0.0040 120 VAL   A CG1 
906  C CG2 . VAL   A 114 ? 0.1569 0.1418 0.1716 0.0003  0.0124  -0.0058 120 VAL   A CG2 
907  N N   . VAL   A 115 ? 0.1177 0.1204 0.1133 -0.0110 0.0079  -0.0054 121 VAL   A N   
908  C CA  . VAL   A 115 ? 0.1283 0.1396 0.1217 -0.0136 0.0053  -0.0024 121 VAL   A CA  
909  C C   . VAL   A 115 ? 0.1194 0.1324 0.1171 -0.0086 0.0018  0.0015  121 VAL   A C   
910  O O   . VAL   A 115 ? 0.1301 0.1491 0.1288 -0.0100 0.0003  0.0047  121 VAL   A O   
911  C CB  . VAL   A 115 ? 0.1368 0.1521 0.1272 -0.0157 0.0048  -0.0013 121 VAL   A CB  
912  C CG1 . VAL   A 115 ? 0.1652 0.1913 0.1564 -0.0172 0.0015  0.0041  121 VAL   A CG1 
913  C CG2 . VAL   A 115 ? 0.1590 0.1728 0.1442 -0.0222 0.0090  -0.0055 121 VAL   A CG2 
914  N N   . GLY   A 116 ? 0.1193 0.1277 0.1197 -0.0035 0.0007  0.0017  122 GLY   A N   
915  C CA  . GLY   A 116 ? 0.1229 0.1316 0.1271 0.0003  -0.0013 0.0042  122 GLY   A CA  
916  C C   . GLY   A 116 ? 0.1111 0.1145 0.1158 0.0038  -0.0018 0.0030  122 GLY   A C   
917  O O   . GLY   A 116 ? 0.1199 0.1199 0.1231 0.0037  -0.0012 0.0012  122 GLY   A O   
918  N N   . ILE   A 117 ? 0.1091 0.1118 0.1161 0.0063  -0.0023 0.0041  123 ILE   A N   
919  C CA  . ILE   A 117 ? 0.1081 0.1066 0.1142 0.0080  -0.0025 0.0025  123 ILE   A CA  
920  C C   . ILE   A 117 ? 0.1131 0.1122 0.1205 0.0092  -0.0011 0.0034  123 ILE   A C   
921  O O   . ILE   A 117 ? 0.1221 0.1241 0.1339 0.0101  -0.0001 0.0061  123 ILE   A O   
922  C CB  . ILE   A 117 ? 0.1261 0.1215 0.1333 0.0085  -0.0032 0.0013  123 ILE   A CB  
923  C CG1 . ILE   A 117 ? 0.1431 0.1391 0.1540 0.0092  -0.0024 0.0024  123 ILE   A CG1 
924  C CG2 . ILE   A 117 ? 0.1453 0.1402 0.1528 0.0079  -0.0041 0.0007  123 ILE   A CG2 
925  C CD1 . ILE   A 117 ? 0.1564 0.1492 0.1680 0.0090  -0.0027 0.0006  123 ILE   A CD1 
926  N N   . VAL   A 118 ? 0.1167 0.1131 0.1211 0.0092  -0.0006 0.0016  124 VAL   A N   
927  C CA  . VAL   A 118 ? 0.1217 0.1175 0.1276 0.0101  0.0021  0.0015  124 VAL   A CA  
928  C C   . VAL   A 118 ? 0.1237 0.1167 0.1338 0.0112  0.0043  0.0011  124 VAL   A C   
929  O O   . VAL   A 118 ? 0.1246 0.1145 0.1327 0.0101  0.0036  -0.0012 124 VAL   A O   
930  C CB  . VAL   A 118 ? 0.1296 0.1225 0.1300 0.0086  0.0024  -0.0012 124 VAL   A CB  
931  C CG1 . VAL   A 118 ? 0.1394 0.1304 0.1412 0.0090  0.0066  -0.0026 124 VAL   A CG1 
932  C CG2 . VAL   A 118 ? 0.1332 0.1280 0.1303 0.0077  0.0009  -0.0004 124 VAL   A CG2 
933  N N   . SER   A 119 ? 0.1198 0.1143 0.1365 0.0132  0.0074  0.0037  125 SER   A N   
934  C CA  . SER   A 119 ? 0.1330 0.1240 0.1557 0.0146  0.0110  0.0039  125 SER   A CA  
935  C C   . SER   A 119 ? 0.1489 0.1374 0.1770 0.0162  0.0169  0.0037  125 SER   A C   
936  O O   . SER   A 119 ? 0.1734 0.1556 0.2043 0.0162  0.0217  0.0011  125 SER   A O   
937  C CB  . SER   A 119 ? 0.1435 0.1391 0.1722 0.0160  0.0095  0.0091  125 SER   A CB  
938  O OG  . SER   A 119 ? 0.1570 0.1496 0.1934 0.0179  0.0134  0.0109  125 SER   A OG  
939  N N   . THR   A 120 ? 0.1468 0.1397 0.1772 0.0172  0.0176  0.0061  126 THR   A N   
940  C CA  . THR   A 120 ? 0.1627 0.1534 0.2009 0.0192  0.0243  0.0064  126 THR   A CA  
941  C C   . THR   A 120 ? 0.1876 0.1796 0.2206 0.0178  0.0245  0.0042  126 THR   A C   
942  O O   . THR   A 120 ? 0.1696 0.1652 0.1952 0.0159  0.0193  0.0041  126 THR   A O   
943  C CB  . THR   A 120 ? 0.1645 0.1619 0.2169 0.0232  0.0259  0.0150  126 THR   A CB  
944  O OG1 . THR   A 120 ? 0.1712 0.1788 0.2236 0.0228  0.0214  0.0198  126 THR   A OG1 
945  C CG2 . THR   A 120 ? 0.1658 0.1632 0.2232 0.0244  0.0250  0.0185  126 THR   A CG2 
946  N N   . GLY   A 121 ? 0.2236 0.2124 0.2615 0.0186  0.0313  0.0026  127 GLY   A N   
947  C CA  . GLY   A 121 ? 0.2592 0.2497 0.2934 0.0173  0.0322  0.0010  127 GLY   A CA  
948  C C   . GLY   A 121 ? 0.2878 0.2751 0.3303 0.0188  0.0411  -0.0002 127 GLY   A C   
949  O O   . GLY   A 121 ? 0.3057 0.2883 0.3576 0.0210  0.0475  0.0000  127 GLY   A O   
950  N N   . GLY   A 122 ? 0.3097 0.2989 0.3485 0.0173  0.0419  -0.0017 128 GLY   A N   
951  C CA  . GLY   A 122 ? 0.3214 0.3074 0.3661 0.0177  0.0509  -0.0042 128 GLY   A CA  
952  C C   . GLY   A 122 ? 0.3401 0.3349 0.3895 0.0192  0.0498  0.0004  128 GLY   A C   
953  O O   . GLY   A 122 ? 0.3512 0.3555 0.4062 0.0214  0.0443  0.0078  128 GLY   A O   
954  N N   . ASN   A 123 ? 0.3282 0.3202 0.3758 0.0174  0.0556  -0.0038 129 ASN   A N   
955  C CA  . ASN   A 123 ? 0.3207 0.3199 0.3732 0.0182  0.0567  -0.0007 129 ASN   A CA  
956  C C   . ASN   A 123 ? 0.2769 0.2861 0.3247 0.0174  0.0473  0.0042  129 ASN   A C   
957  O O   . ASN   A 123 ? 0.2583 0.2775 0.3162 0.0195  0.0469  0.0107  129 ASN   A O   
958  C CB  . ASN   A 123 ? 0.3573 0.3603 0.4308 0.0237  0.0644  0.0053  129 ASN   A CB  
959  C CG  . ASN   A 123 ? 0.4410 0.4429 0.5284 0.0283  0.0672  0.0101  129 ASN   A CG  
960  O OD1 . ASN   A 123 ? 0.4654 0.4580 0.5602 0.0296  0.0772  0.0065  129 ASN   A OD1 
961  N ND2 . ASN   A 123 ? 0.4325 0.4441 0.5254 0.0307  0.0597  0.0188  129 ASN   A ND2 
962  N N   . GLY   A 124 ? 0.2436 0.2502 0.2763 0.0135  0.0410  0.0007  130 GLY   A N   
963  C CA  . GLY   A 124 ? 0.2203 0.2338 0.2478 0.0119  0.0338  0.0038  130 GLY   A CA  
964  C C   . GLY   A 124 ? 0.1644 0.1840 0.1965 0.0136  0.0285  0.0094  130 GLY   A C   
965  O O   . GLY   A 124 ? 0.1964 0.2222 0.2253 0.0116  0.0238  0.0118  130 GLY   A O   
966  N N   . LEU   A 125 ? 0.1714 0.1885 0.2092 0.0161  0.0294  0.0106  131 LEU   A N   
967  C CA  . LEU   A 125 ? 0.1581 0.1805 0.1979 0.0166  0.0240  0.0153  131 LEU   A CA  
968  C C   . LEU   A 125 ? 0.1749 0.1892 0.2060 0.0155  0.0216  0.0108  131 LEU   A C   
969  O O   . LEU   A 125 ? 0.1996 0.2052 0.2272 0.0151  0.0251  0.0055  131 LEU   A O   
970  C CB  . LEU   A 125 ? 0.1612 0.1893 0.2166 0.0206  0.0265  0.0224  131 LEU   A CB  
971  C CG  . LEU   A 125 ? 0.1592 0.1981 0.2264 0.0221  0.0283  0.0292  131 LEU   A CG  
972  C CD1 . LEU   A 125 ? 0.1944 0.2364 0.2799 0.0272  0.0335  0.0362  131 LEU   A CD1 
973  C CD2 . LEU   A 125 ? 0.1646 0.2158 0.2281 0.0183  0.0212  0.0339  131 LEU   A CD2 
974  N N   . VAL   A 126 ? 0.1316 0.1492 0.1590 0.0141  0.0161  0.0126  132 VAL   A N   
975  C CA  . VAL   A 126 ? 0.1357 0.1475 0.1574 0.0134  0.0137  0.0097  132 VAL   A CA  
976  C C   . VAL   A 126 ? 0.1359 0.1538 0.1630 0.0141  0.0110  0.0149  132 VAL   A C   
977  O O   . VAL   A 126 ? 0.1399 0.1663 0.1682 0.0124  0.0084  0.0189  132 VAL   A O   
978  C CB  . VAL   A 126 ? 0.1390 0.1474 0.1495 0.0104  0.0104  0.0058  132 VAL   A CB  
979  C CG1 . VAL   A 126 ? 0.1522 0.1664 0.1602 0.0081  0.0076  0.0078  132 VAL   A CG1 
980  C CG2 . VAL   A 126 ? 0.1462 0.1498 0.1528 0.0100  0.0081  0.0037  132 VAL   A CG2 
981  N N   . GLY   A 127 ? 0.1339 0.1479 0.1636 0.0156  0.0116  0.0146  133 GLY   A N   
982  C CA  . GLY   A 127 ? 0.1314 0.1508 0.1653 0.0157  0.0090  0.0195  133 GLY   A CA  
983  C C   . GLY   A 127 ? 0.1231 0.1379 0.1494 0.0139  0.0061  0.0158  133 GLY   A C   
984  O O   . GLY   A 127 ? 0.1421 0.1490 0.1644 0.0141  0.0072  0.0109  133 GLY   A O   
985  N N   . PHE   A 128 ? 0.1150 0.1355 0.1399 0.0116  0.0029  0.0183  134 PHE   A N   
986  C CA  . PHE   A 128 ? 0.1161 0.1331 0.1351 0.0097  0.0008  0.0150  134 PHE   A CA  
987  C C   . PHE   A 128 ? 0.1229 0.1435 0.1459 0.0095  -0.0001 0.0188  134 PHE   A C   
988  O O   . PHE   A 128 ? 0.1226 0.1523 0.1495 0.0081  -0.0012 0.0246  134 PHE   A O   
989  C CB  . PHE   A 128 ? 0.1183 0.1376 0.1305 0.0058  -0.0009 0.0132  134 PHE   A CB  
990  C CG  . PHE   A 128 ? 0.1184 0.1353 0.1269 0.0055  -0.0001 0.0107  134 PHE   A CG  
991  C CD1 . PHE   A 128 ? 0.1187 0.1281 0.1230 0.0063  0.0001  0.0066  134 PHE   A CD1 
992  C CD2 . PHE   A 128 ? 0.1328 0.1560 0.1422 0.0041  0.0001  0.0131  134 PHE   A CD2 
993  C CE1 . PHE   A 128 ? 0.1196 0.1272 0.1204 0.0057  0.0007  0.0051  134 PHE   A CE1 
994  C CE2 . PHE   A 128 ? 0.1306 0.1514 0.1364 0.0036  0.0010  0.0108  134 PHE   A CE2 
995  C CZ  . PHE   A 128 ? 0.1281 0.1408 0.1294 0.0044  0.0014  0.0068  134 PHE   A CZ  
996  N N   . ALA   A 129 ? 0.1156 0.1303 0.1378 0.0103  0.0001  0.0162  135 ALA   A N   
997  C CA  . ALA   A 129 ? 0.1200 0.1375 0.1448 0.0095  -0.0009 0.0191  135 ALA   A CA  
998  C C   . ALA   A 129 ? 0.1140 0.1347 0.1326 0.0051  -0.0028 0.0176  135 ALA   A C   
999  O O   . ALA   A 129 ? 0.1256 0.1409 0.1395 0.0044  -0.0027 0.0126  135 ALA   A O   
1000 C CB  . ALA   A 129 ? 0.1313 0.1411 0.1571 0.0114  0.0005  0.0162  135 ALA   A CB  
1001 N N   . ASP   A 130 ? 0.1178 0.1475 0.1367 0.0016  -0.0041 0.0221  136 ASP   A N   
1002 C CA  . ASP   A 130 ? 0.1260 0.1584 0.1381 -0.0040 -0.0046 0.0198  136 ASP   A CA  
1003 C C   . ASP   A 130 ? 0.1286 0.1569 0.1399 -0.0045 -0.0041 0.0174  136 ASP   A C   
1004 O O   . ASP   A 130 ? 0.1417 0.1698 0.1578 -0.0022 -0.0044 0.0204  136 ASP   A O   
1005 C CB  . ASP   A 130 ? 0.1518 0.1969 0.1639 -0.0092 -0.0064 0.0259  136 ASP   A CB  
1006 C CG  . ASP   A 130 ? 0.1909 0.2395 0.1948 -0.0170 -0.0060 0.0229  136 ASP   A CG  
1007 O OD1 . ASP   A 130 ? 0.1898 0.2333 0.1881 -0.0190 -0.0040 0.0167  136 ASP   A OD1 
1008 O OD2 . ASP   A 130 ? 0.2758 0.3311 0.2786 -0.0214 -0.0070 0.0262  136 ASP   A OD2 
1009 N N   . VAL   A 131 ? 0.1209 0.1458 0.1268 -0.0077 -0.0026 0.0120  137 VAL   A N   
1010 C CA  . VAL   A 131 ? 0.1222 0.1445 0.1276 -0.0090 -0.0015 0.0097  137 VAL   A CA  
1011 C C   . VAL   A 131 ? 0.1309 0.1571 0.1304 -0.0164 0.0004  0.0076  137 VAL   A C   
1012 O O   . VAL   A 131 ? 0.1285 0.1526 0.1274 -0.0183 0.0023  0.0050  137 VAL   A O   
1013 C CB  . VAL   A 131 ? 0.1266 0.1399 0.1336 -0.0053 -0.0003 0.0051  137 VAL   A CB  
1014 C CG1 . VAL   A 131 ? 0.1454 0.1551 0.1564 0.0001  -0.0018 0.0064  137 VAL   A CG1 
1015 C CG2 . VAL   A 131 ? 0.1451 0.1545 0.1495 -0.0064 0.0019  0.0011  137 VAL   A CG2 
1016 N N   . ARG   A 132 ? 0.1319 0.1642 0.1269 -0.0215 0.0004  0.0083  138 ARG   A N   
1017 C CA  . ARG   A 132 ? 0.1379 0.1731 0.1257 -0.0302 0.0034  0.0046  138 ARG   A CA  
1018 C C   . ARG   A 132 ? 0.1524 0.1951 0.1377 -0.0358 0.0027  0.0075  138 ARG   A C   
1019 O O   . ARG   A 132 ? 0.1690 0.2122 0.1480 -0.0434 0.0064  0.0030  138 ARG   A O   
1020 C CB  . ARG   A 132 ? 0.1439 0.1843 0.1266 -0.0355 0.0036  0.0044  138 ARG   A CB  
1021 C CG  . ARG   A 132 ? 0.1396 0.1712 0.1234 -0.0313 0.0057  0.0003  138 ARG   A CG  
1022 C CD  . ARG   A 132 ? 0.1593 0.1968 0.1382 -0.0370 0.0058  0.0004  138 ARG   A CD  
1023 N NE  . ARG   A 132 ? 0.1545 0.2015 0.1373 -0.0345 0.0007  0.0081  138 ARG   A NE  
1024 C CZ  . ARG   A 132 ? 0.1847 0.2387 0.1658 -0.0376 -0.0006 0.0104  138 ARG   A CZ  
1025 N NH1 . ARG   A 132 ? 0.1853 0.2387 0.1593 -0.0446 0.0026  0.0053  138 ARG   A NH1 
1026 N NH2 . ARG   A 132 ? 0.1906 0.2526 0.1781 -0.0339 -0.0044 0.0180  138 ARG   A NH2 
1027 N N   . ASP   A 133 ? 0.1476 0.1966 0.1379 -0.0329 -0.0015 0.0154  139 ASP   A N   
1028 C CA  . ASP   A 133 ? 0.1523 0.2093 0.1409 -0.0382 -0.0026 0.0195  139 ASP   A CA  
1029 C C   . ASP   A 133 ? 0.1573 0.2068 0.1482 -0.0354 -0.0007 0.0166  139 ASP   A C   
1030 O O   . ASP   A 133 ? 0.1735 0.2283 0.1620 -0.0403 -0.0008 0.0188  139 ASP   A O   
1031 C CB  . ASP   A 133 ? 0.1752 0.2426 0.1701 -0.0362 -0.0074 0.0306  139 ASP   A CB  
1032 C CG  . ASP   A 133 ? 0.2109 0.2708 0.2160 -0.0256 -0.0080 0.0330  139 ASP   A CG  
1033 O OD1 . ASP   A 133 ? 0.2007 0.2512 0.2076 -0.0200 -0.0066 0.0280  139 ASP   A OD1 
1034 O OD2 . ASP   A 133 ? 0.2316 0.2951 0.2431 -0.0234 -0.0096 0.0401  139 ASP   A OD2 
1035 N N   . LEU   A 134 ? 0.1441 0.1825 0.1396 -0.0281 0.0008  0.0121  140 LEU   A N   
1036 C CA  . LEU   A 134 ? 0.1441 0.1764 0.1432 -0.0251 0.0021  0.0100  140 LEU   A CA  
1037 C C   . LEU   A 134 ? 0.1466 0.1747 0.1416 -0.0296 0.0071  0.0027  140 LEU   A C   
1038 O O   . LEU   A 134 ? 0.1532 0.1733 0.1512 -0.0261 0.0098  -0.0022 140 LEU   A O   
1039 C CB  . LEU   A 134 ? 0.1439 0.1682 0.1495 -0.0165 0.0011  0.0093  140 LEU   A CB  
1040 C CG  . LEU   A 134 ? 0.1577 0.1842 0.1681 -0.0119 -0.0019 0.0154  140 LEU   A CG  
1041 C CD1 . LEU   A 134 ? 0.1680 0.1863 0.1825 -0.0055 -0.0019 0.0130  140 LEU   A CD1 
1042 C CD2 . LEU   A 134 ? 0.1867 0.2182 0.2005 -0.0125 -0.0033 0.0217  140 LEU   A CD2 
1043 N N   . LEU   A 135 ? 0.1450 0.1792 0.1336 -0.0383 0.0090  0.0022  141 LEU   A N   
1044 C CA  . LEU   A 135 ? 0.1571 0.1872 0.1413 -0.0442 0.0155  -0.0056 141 LEU   A CA  
1045 C C   . LEU   A 135 ? 0.1590 0.1815 0.1491 -0.0402 0.0187  -0.0092 141 LEU   A C   
1046 O O   . LEU   A 135 ? 0.1765 0.1922 0.1682 -0.0409 0.0249  -0.0157 141 LEU   A O   
1047 C CB  . LEU   A 135 ? 0.1738 0.2130 0.1480 -0.0562 0.0171  -0.0057 141 LEU   A CB  
1048 C CG  . LEU   A 135 ? 0.1953 0.2455 0.1640 -0.0614 0.0129  -0.0003 141 LEU   A CG  
1049 C CD1 . LEU   A 135 ? 0.2183 0.2780 0.1757 -0.0752 0.0151  -0.0014 141 LEU   A CD1 
1050 C CD2 . LEU   A 135 ? 0.2215 0.2679 0.1896 -0.0599 0.0141  -0.0036 141 LEU   A CD2 
1051 N N   . TRP   A 136 ? 0.1441 0.1676 0.1390 -0.0358 0.0151  -0.0048 142 TRP   A N   
1052 C CA  . TRP   A 136 ? 0.1555 0.1733 0.1564 -0.0323 0.0174  -0.0074 142 TRP   A CA  
1053 C C   . TRP   A 136 ? 0.1612 0.1717 0.1696 -0.0252 0.0182  -0.0099 142 TRP   A C   
1054 O O   . TRP   A 136 ? 0.1741 0.1807 0.1886 -0.0230 0.0210  -0.0123 142 TRP   A O   
1055 C CB  . TRP   A 136 ? 0.1634 0.1842 0.1673 -0.0300 0.0133  -0.0019 142 TRP   A CB  
1056 C CG  . TRP   A 136 ? 0.1522 0.1735 0.1595 -0.0241 0.0081  0.0036  142 TRP   A CG  
1057 C CD1 . TRP   A 136 ? 0.1548 0.1826 0.1604 -0.0252 0.0046  0.0101  142 TRP   A CD1 
1058 C CD2 . TRP   A 136 ? 0.1546 0.1701 0.1681 -0.0167 0.0063  0.0034  142 TRP   A CD2 
1059 N NE1 . TRP   A 136 ? 0.1715 0.1965 0.1827 -0.0184 0.0019  0.0132  142 TRP   A NE1 
1060 C CE2 . TRP   A 136 ? 0.1615 0.1789 0.1764 -0.0138 0.0028  0.0087  142 TRP   A CE2 
1061 C CE3 . TRP   A 136 ? 0.1683 0.1782 0.1869 -0.0129 0.0075  -0.0002 142 TRP   A CE3 
1062 C CZ2 . TRP   A 136 ? 0.1807 0.1931 0.2002 -0.0080 0.0013  0.0088  142 TRP   A CZ2 
1063 C CZ3 . TRP   A 136 ? 0.1887 0.1954 0.2112 -0.0077 0.0047  0.0009  142 TRP   A CZ3 
1064 C CH2 . TRP   A 136 ? 0.1845 0.1919 0.2066 -0.0057 0.0021  0.0047  142 TRP   A CH2 
1065 N N   . LEU   A 137 ? 0.1456 0.1547 0.1544 -0.0214 0.0155  -0.0085 143 LEU   A N   
1066 C CA  . LEU   A 137 ? 0.1704 0.1737 0.1858 -0.0157 0.0162  -0.0101 143 LEU   A CA  
1067 C C   . LEU   A 137 ? 0.1891 0.1879 0.2073 -0.0176 0.0231  -0.0151 143 LEU   A C   
1068 O O   . LEU   A 137 ? 0.2024 0.1973 0.2288 -0.0128 0.0243  -0.0153 143 LEU   A O   
1069 C CB  . LEU   A 137 ? 0.1629 0.1660 0.1769 -0.0128 0.0129  -0.0081 143 LEU   A CB  
1070 C CG  . LEU   A 137 ? 0.1540 0.1593 0.1684 -0.0092 0.0075  -0.0036 143 LEU   A CG  
1071 C CD1 . LEU   A 137 ? 0.1798 0.1854 0.1919 -0.0076 0.0055  -0.0022 143 LEU   A CD1 
1072 C CD2 . LEU   A 137 ? 0.1650 0.1672 0.1856 -0.0044 0.0057  -0.0031 143 LEU   A CD2 
1073 N N   . ASP   A 138 ? 0.2093 0.2089 0.2210 -0.0251 0.0282  -0.0190 144 ASP   A N   
1074 C CA  . ASP   A 138 ? 0.2341 0.2278 0.2486 -0.0277 0.0369  -0.0248 144 ASP   A CA  
1075 C C   . ASP   A 138 ? 0.2839 0.2758 0.3035 -0.0292 0.0424  -0.0278 144 ASP   A C   
1076 O O   . ASP   A 138 ? 0.3107 0.2970 0.3342 -0.0314 0.0513  -0.0329 144 ASP   A O   
1077 C CB  . ASP   A 138 ? 0.2421 0.2371 0.2460 -0.0370 0.0413  -0.0291 144 ASP   A CB  
1078 C CG  . ASP   A 138 ? 0.2759 0.2726 0.2751 -0.0369 0.0376  -0.0272 144 ASP   A CG  
1079 O OD1 . ASP   A 138 ? 0.2947 0.2897 0.2993 -0.0292 0.0330  -0.0235 144 ASP   A OD1 
1080 O OD2 . ASP   A 138 ? 0.3642 0.3648 0.3538 -0.0453 0.0392  -0.0293 144 ASP   A OD2 
1081 N N   . GLU   A 139 ? 0.2921 0.2880 0.3123 -0.0282 0.0385  -0.0249 145 GLU   A N   
1082 C CA  . GLU   A 139 ? 0.3395 0.3343 0.3644 -0.0300 0.0438  -0.0277 145 GLU   A CA  
1083 C C   . GLU   A 139 ? 0.3520 0.3483 0.3854 -0.0235 0.0390  -0.0235 145 GLU   A C   
1084 O O   . GLU   A 139 ? 0.3468 0.3453 0.3798 -0.0193 0.0315  -0.0188 145 GLU   A O   
1085 C CB  . GLU   A 139 ? 0.4085 0.4079 0.4223 -0.0395 0.0457  -0.0299 145 GLU   A CB  
1086 C CG  . GLU   A 139 ? 0.5131 0.5198 0.5208 -0.0397 0.0369  -0.0235 145 GLU   A CG  
1087 C CD  . GLU   A 139 ? 0.6178 0.6316 0.6133 -0.0495 0.0367  -0.0231 145 GLU   A CD  
1088 O OE1 . GLU   A 139 ? 0.6161 0.6363 0.6093 -0.0496 0.0306  -0.0168 145 GLU   A OE1 
1089 O OE2 . GLU   A 139 ? 0.6730 0.6865 0.6617 -0.0576 0.0429  -0.0285 145 GLU   A OE2 
1090 N N   . GLU   A 140 ? 0.3779 0.3727 0.4195 -0.0231 0.0440  -0.0254 146 GLU   A N   
1091 C CA  . GLU   A 140 ? 0.4084 0.4055 0.4585 -0.0179 0.0398  -0.0217 146 GLU   A CA  
1092 C C   . GLU   A 140 ? 0.4370 0.4384 0.4801 -0.0198 0.0339  -0.0189 146 GLU   A C   
1093 O O   . GLU   A 140 ? 0.4559 0.4594 0.4900 -0.0261 0.0353  -0.0202 146 GLU   A O   
1094 C CB  . GLU   A 140 ? 0.4545 0.4502 0.5156 -0.0178 0.0471  -0.0242 146 GLU   A CB  
1095 C CG  . GLU   A 140 ? 0.5625 0.5548 0.6369 -0.0126 0.0513  -0.0236 146 GLU   A CG  
1096 C CD  . GLU   A 140 ? 0.6830 0.6777 0.7731 -0.0082 0.0526  -0.0208 146 GLU   A CD  
1097 O OE1 . GLU   A 140 ? 0.6991 0.6947 0.8006 -0.0023 0.0510  -0.0162 146 GLU   A OE1 
1098 O OE2 . GLU   A 140 ? 0.7203 0.7169 0.8115 -0.0108 0.0549  -0.0225 146 GLU   A OE2 
1099 N N   . SER   B 1   ? 0.2021 0.2152 0.2163 0.0046  -0.0135 0.0357  7   SER   C N   
1100 C CA  . SER   B 1   ? 0.1867 0.2014 0.2093 0.0035  -0.0139 0.0361  7   SER   C CA  
1101 C C   . SER   B 1   ? 0.1847 0.1975 0.2065 0.0027  -0.0135 0.0327  7   SER   C C   
1102 O O   . SER   B 1   ? 0.2107 0.2210 0.2255 0.0028  -0.0138 0.0303  7   SER   C O   
1103 C CB  . SER   B 1   ? 0.2309 0.2473 0.2553 0.0026  -0.0181 0.0386  7   SER   C CB  
1104 O OG  . SER   B 1   ? 0.2952 0.3096 0.3124 0.0018  -0.0216 0.0367  7   SER   C OG  
1105 N N   . GLY   B 2   ? 0.1834 0.1970 0.2123 0.0021  -0.0123 0.0327  8   GLY   C N   
1106 C CA  . GLY   B 2   ? 0.1734 0.1850 0.2019 0.0016  -0.0116 0.0302  8   GLY   C CA  
1107 C C   . GLY   B 2   ? 0.1547 0.1666 0.1894 0.0019  -0.0083 0.0300  8   GLY   C C   
1108 O O   . GLY   B 2   ? 0.1577 0.1707 0.1955 0.0027  -0.0062 0.0305  8   GLY   C O   
1109 N N   . ALA   B 3   ? 0.1411 0.1516 0.1772 0.0014  -0.0075 0.0291  9   ALA   C N   
1110 C CA  . ALA   B 3   ? 0.1448 0.1548 0.1853 0.0019  -0.0040 0.0288  9   ALA   C CA  
1111 C C   . ALA   B 3   ? 0.1354 0.1423 0.1719 0.0021  -0.0025 0.0267  9   ALA   C C   
1112 O O   . ALA   B 3   ? 0.1515 0.1569 0.1839 0.0015  -0.0045 0.0260  9   ALA   C O   
1113 C CB  . ALA   B 3   ? 0.1772 0.1893 0.2271 0.0011  -0.0037 0.0315  9   ALA   C CB  
1114 N N   . ILE   B 4   ? 0.1368 0.1423 0.1741 0.0032  0.0009  0.0258  10  ILE   C N   
1115 C CA  . ILE   B 4   ? 0.1370 0.1392 0.1708 0.0037  0.0030  0.0246  10  ILE   C CA  
1116 C C   . ILE   B 4   ? 0.1328 0.1350 0.1738 0.0034  0.0056  0.0265  10  ILE   C C   
1117 O O   . ILE   B 4   ? 0.1421 0.1457 0.1886 0.0036  0.0074  0.0274  10  ILE   C O   
1118 C CB  . ILE   B 4   ? 0.1389 0.1391 0.1673 0.0055  0.0049  0.0221  10  ILE   C CB  
1119 C CG1 . ILE   B 4   ? 0.1604 0.1615 0.1845 0.0060  0.0027  0.0205  10  ILE   C CG1 
1120 C CG2 . ILE   B 4   ? 0.1691 0.1657 0.1924 0.0064  0.0067  0.0214  10  ILE   C CG2 
1121 C CD1 . ILE   B 4   ? 0.1663 0.1662 0.1873 0.0075  0.0041  0.0180  10  ILE   C CD1 
1122 N N   . TYR   B 5   ? 0.1337 0.1341 0.1754 0.0028  0.0062  0.0272  11  TYR   C N   
1123 C CA  . TYR   B 5   ? 0.1466 0.1468 0.1961 0.0025  0.0092  0.0293  11  TYR   C CA  
1124 C C   . TYR   B 5   ? 0.1510 0.1469 0.1956 0.0039  0.0134  0.0286  11  TYR   C C   
1125 O O   . TYR   B 5   ? 0.1763 0.1701 0.2177 0.0037  0.0129  0.0285  11  TYR   C O   
1126 C CB  . TYR   B 5   ? 0.1538 0.1559 0.2105 0.0003  0.0064  0.0313  11  TYR   C CB  
1127 C CG  . TYR   B 5   ? 0.1548 0.1610 0.2160 -0.0008 0.0023  0.0325  11  TYR   C CG  
1128 C CD1 . TYR   B 5   ? 0.1468 0.1559 0.2171 -0.0008 0.0033  0.0348  11  TYR   C CD1 
1129 C CD2 . TYR   B 5   ? 0.1669 0.1739 0.2226 -0.0014 -0.0023 0.0315  11  TYR   C CD2 
1130 C CE1 . TYR   B 5   ? 0.1674 0.1801 0.2412 -0.0015 -0.0005 0.0363  11  TYR   C CE1 
1131 C CE2 . TYR   B 5   ? 0.1881 0.1984 0.2463 -0.0020 -0.0058 0.0328  11  TYR   C CE2 
1132 C CZ  . TYR   B 5   ? 0.1802 0.1934 0.2475 -0.0021 -0.0051 0.0354  11  TYR   C CZ  
1133 O OH  . TYR   B 5   ? 0.2054 0.2217 0.2745 -0.0023 -0.0086 0.0372  11  TYR   C OH  
1134 N N   . VAL   B 6   ? 0.1583 0.1524 0.2011 0.0056  0.0174  0.0280  12  VAL   C N   
1135 C CA  . VAL   B 6   ? 0.1762 0.1657 0.2127 0.0075  0.0216  0.0274  12  VAL   C CA  
1136 C C   . VAL   B 6   ? 0.1769 0.1652 0.2192 0.0082  0.0270  0.0291  12  VAL   C C   
1137 O O   . VAL   B 6   ? 0.1643 0.1541 0.2107 0.0084  0.0280  0.0289  12  VAL   C O   
1138 C CB  . VAL   B 6   ? 0.1921 0.1798 0.2179 0.0094  0.0208  0.0243  12  VAL   C CB  
1139 C CG1 . VAL   B 6   ? 0.1949 0.1845 0.2225 0.0096  0.0205  0.0228  12  VAL   C CG1 
1140 C CG2 . VAL   B 6   ? 0.2103 0.1931 0.2285 0.0116  0.0248  0.0239  12  VAL   C CG2 
1141 N N   . GLY   B 7   ? 0.1896 0.1751 0.2334 0.0087  0.0310  0.0310  13  GLY   C N   
1142 C CA  . GLY   B 7   ? 0.1902 0.1743 0.2400 0.0095  0.0370  0.0329  13  GLY   C CA  
1143 C C   . GLY   B 7   ? 0.1887 0.1775 0.2521 0.0078  0.0359  0.0348  13  GLY   C C   
1144 O O   . GLY   B 7   ? 0.2007 0.1931 0.2705 0.0056  0.0314  0.0360  13  GLY   C O   
1145 N N   . ASN   B 8   ? 0.1845 0.1732 0.2512 0.0088  0.0393  0.0348  14  ASN   C N   
1146 C CA  . ASN   B 8   ? 0.1822 0.1755 0.2617 0.0074  0.0381  0.0368  14  ASN   C CA  
1147 C C   . ASN   B 8   ? 0.1674 0.1629 0.2444 0.0074  0.0347  0.0347  14  ASN   C C   
1148 O O   . ASN   B 8   ? 0.1655 0.1628 0.2502 0.0076  0.0361  0.0357  14  ASN   C O   
1149 C CB  . ASN   B 8   ? 0.2035 0.1958 0.2925 0.0084  0.0449  0.0391  14  ASN   C CB  
1150 C CG  . ASN   B 8   ? 0.2943 0.2862 0.3911 0.0077  0.0474  0.0423  14  ASN   C CG  
1151 O OD1 . ASN   B 8   ? 0.3203 0.3166 0.4299 0.0057  0.0448  0.0450  14  ASN   C OD1 
1152 N ND2 . ASN   B 8   ? 0.3218 0.3086 0.4108 0.0092  0.0519  0.0419  14  ASN   C ND2 
1153 N N   . TYR   B 9   ? 0.1416 0.1372 0.2095 0.0072  0.0302  0.0324  15  TYR   C N   
1154 C CA  . TYR   B 9   ? 0.1316 0.1292 0.1971 0.0071  0.0270  0.0306  15  TYR   C CA  
1155 C C   . TYR   B 9   ? 0.1330 0.1341 0.1985 0.0054  0.0209  0.0311  15  TYR   C C   
1156 O O   . TYR   B 9   ? 0.1467 0.1471 0.2080 0.0048  0.0187  0.0309  15  TYR   C O   
1157 C CB  . TYR   B 9   ? 0.1518 0.1457 0.2055 0.0088  0.0279  0.0267  15  TYR   C CB  
1158 C CG  . TYR   B 9   ? 0.1753 0.1649 0.2263 0.0108  0.0337  0.0254  15  TYR   C CG  
1159 C CD1 . TYR   B 9   ? 0.2056 0.1953 0.2634 0.0113  0.0369  0.0256  15  TYR   C CD1 
1160 C CD2 . TYR   B 9   ? 0.2085 0.1934 0.2493 0.0125  0.0361  0.0239  15  TYR   C CD2 
1161 C CE1 . TYR   B 9   ? 0.2447 0.2297 0.2990 0.0132  0.0426  0.0240  15  TYR   C CE1 
1162 C CE2 . TYR   B 9   ? 0.2479 0.2282 0.2844 0.0146  0.0415  0.0225  15  TYR   C CE2 
1163 C CZ  . TYR   B 9   ? 0.2723 0.2525 0.3151 0.0149  0.0447  0.0223  15  TYR   C CZ  
1164 O OH  . TYR   B 9   ? 0.3479 0.3229 0.3856 0.0171  0.0504  0.0205  15  TYR   C OH  
1165 N N   . ARG   B 10  ? 0.1236 0.1279 0.1927 0.0050  0.0184  0.0316  16  ARG   C N   
1166 C CA  . ARG   B 10  ? 0.1220 0.1290 0.1891 0.0038  0.0130  0.0318  16  ARG   C CA  
1167 C C   . ARG   B 10  ? 0.1216 0.1284 0.1840 0.0047  0.0127  0.0296  16  ARG   C C   
1168 O O   . ARG   B 10  ? 0.1301 0.1374 0.1972 0.0053  0.0148  0.0297  16  ARG   C O   
1169 C CB  . ARG   B 10  ? 0.1349 0.1461 0.2120 0.0026  0.0104  0.0354  16  ARG   C CB  
1170 C CG  . ARG   B 10  ? 0.1472 0.1611 0.2221 0.0019  0.0055  0.0360  16  ARG   C CG  
1171 C CD  . ARG   B 10  ? 0.1406 0.1583 0.2245 0.0009  0.0025  0.0397  16  ARG   C CD  
1172 N NE  . ARG   B 10  ? 0.1465 0.1667 0.2309 0.0012  0.0002  0.0413  16  ARG   C NE  
1173 C CZ  . ARG   B 10  ? 0.1688 0.1902 0.2478 0.0008  -0.0041 0.0417  16  ARG   C CZ  
1174 N NH1 . ARG   B 10  ? 0.1887 0.2087 0.2606 -0.0001 -0.0069 0.0400  16  ARG   C NH1 
1175 N NH2 . ARG   B 10  ? 0.1848 0.2080 0.2646 0.0014  -0.0052 0.0437  16  ARG   C NH2 
1176 N N   . VAL   B 11  ? 0.1211 0.1272 0.1752 0.0048  0.0102  0.0275  17  VAL   C N   
1177 C CA  . VAL   B 11  ? 0.1105 0.1166 0.1610 0.0056  0.0097  0.0253  17  VAL   C CA  
1178 C C   . VAL   B 11  ? 0.1203 0.1292 0.1710 0.0048  0.0062  0.0267  17  VAL   C C   
1179 O O   . VAL   B 11  ? 0.1277 0.1366 0.1740 0.0042  0.0035  0.0268  17  VAL   C O   
1180 C CB  . VAL   B 11  ? 0.1289 0.1319 0.1700 0.0066  0.0098  0.0219  17  VAL   C CB  
1181 C CG1 . VAL   B 11  ? 0.1600 0.1633 0.1995 0.0073  0.0093  0.0195  17  VAL   C CG1 
1182 C CG2 . VAL   B 11  ? 0.1519 0.1515 0.1905 0.0076  0.0132  0.0209  17  VAL   C CG2 
1183 N N   . VAL   B 12  ? 0.1112 0.1220 0.1666 0.0050  0.0064  0.0277  18  VAL   C N   
1184 C CA  A VAL   B 12  ? 0.1106 0.1238 0.1657 0.0046  0.0037  0.0295  18  VAL   C CA  
1185 C CA  B VAL   B 12  ? 0.1321 0.1452 0.1872 0.0046  0.0037  0.0296  18  VAL   C CA  
1186 C C   . VAL   B 12  ? 0.1191 0.1325 0.1749 0.0053  0.0048  0.0284  18  VAL   C C   
1187 O O   . VAL   B 12  ? 0.1233 0.1355 0.1815 0.0059  0.0073  0.0264  18  VAL   C O   
1188 C CB  A VAL   B 12  ? 0.1096 0.1255 0.1719 0.0040  0.0026  0.0336  18  VAL   C CB  
1189 C CB  B VAL   B 12  ? 0.1731 0.1889 0.2362 0.0040  0.0029  0.0336  18  VAL   C CB  
1190 C CG1 A VAL   B 12  ? 0.1175 0.1338 0.1794 0.0029  0.0001  0.0348  18  VAL   C CG1 
1191 C CG1 B VAL   B 12  ? 0.1787 0.1967 0.2410 0.0038  -0.0001 0.0362  18  VAL   C CG1 
1192 C CG2 A VAL   B 12  ? 0.0749 0.0914 0.1464 0.0045  0.0058  0.0349  18  VAL   C CG2 
1193 C CG2 B VAL   B 12  ? 0.2124 0.2281 0.2771 0.0031  0.0020  0.0345  18  VAL   C CG2 
1194 N N   . ASN   B 13  ? 0.1124 0.1272 0.1662 0.0053  0.0031  0.0297  19  ASN   C N   
1195 C CA  . ASN   B 13  ? 0.1061 0.1215 0.1627 0.0059  0.0045  0.0295  19  ASN   C CA  
1196 C C   . ASN   B 13  ? 0.1170 0.1337 0.1830 0.0060  0.0064  0.0321  19  ASN   C C   
1197 O O   . ASN   B 13  ? 0.1083 0.1266 0.1773 0.0058  0.0054  0.0356  19  ASN   C O   
1198 C CB  . ASN   B 13  ? 0.1177 0.1342 0.1711 0.0062  0.0031  0.0315  19  ASN   C CB  
1199 C CG  . ASN   B 13  ? 0.1174 0.1325 0.1624 0.0063  0.0017  0.0292  19  ASN   C CG  
1200 O OD1 . ASN   B 13  ? 0.1353 0.1498 0.1752 0.0058  -0.0005 0.0296  19  ASN   C OD1 
1201 N ND2 . ASN   B 13  ? 0.1319 0.1463 0.1763 0.0068  0.0028  0.0266  19  ASN   C ND2 
1202 N N   . ARG   B 14  ? 0.1085 0.1244 0.1792 0.0064  0.0090  0.0302  20  ARG   C N   
1203 C CA  . ARG   B 14  ? 0.1061 0.1227 0.1861 0.0066  0.0113  0.0324  20  ARG   C CA  
1204 C C   . ARG   B 14  ? 0.1147 0.1338 0.1981 0.0068  0.0105  0.0373  20  ARG   C C   
1205 O O   . ARG   B 14  ? 0.1218 0.1423 0.2112 0.0069  0.0108  0.0408  20  ARG   C O   
1206 C CB  . ARG   B 14  ? 0.1064 0.1213 0.1904 0.0069  0.0139  0.0291  20  ARG   C CB  
1207 C CG  . ARG   B 14  ? 0.1117 0.1265 0.2058 0.0071  0.0170  0.0306  20  ARG   C CG  
1208 C CD  . ARG   B 14  ? 0.1176 0.1304 0.2154 0.0072  0.0192  0.0267  20  ARG   C CD  
1209 N NE  . ARG   B 14  ? 0.1263 0.1380 0.2333 0.0075  0.0226  0.0271  20  ARG   C NE  
1210 C CZ  . ARG   B 14  ? 0.1190 0.1319 0.2350 0.0077  0.0243  0.0305  20  ARG   C CZ  
1211 N NH1 . ARG   B 14  ? 0.1380 0.1534 0.2544 0.0078  0.0229  0.0345  20  ARG   C NH1 
1212 N NH2 . ARG   B 14  ? 0.1307 0.1420 0.2551 0.0080  0.0277  0.0301  20  ARG   C NH2 
1213 N N   . HIS   B 15  ? 0.1159 0.1355 0.1951 0.0071  0.0095  0.0379  21  HIS   C N   
1214 C CA  . HIS   B 15  ? 0.1324 0.1537 0.2135 0.0077  0.0092  0.0429  21  HIS   C CA  
1215 C C   . HIS   B 15  ? 0.1320 0.1547 0.2092 0.0075  0.0058  0.0461  21  HIS   C C   
1216 O O   . HIS   B 15  ? 0.1539 0.1782 0.2326 0.0082  0.0051  0.0506  21  HIS   C O   
1217 C CB  . HIS   B 15  ? 0.1395 0.1606 0.2178 0.0082  0.0101  0.0429  21  HIS   C CB  
1218 C CG  . HIS   B 15  ? 0.1265 0.1470 0.1945 0.0082  0.0078  0.0415  21  HIS   C CG  
1219 N ND1 . HIS   B 15  ? 0.1310 0.1500 0.1947 0.0078  0.0075  0.0368  21  HIS   C ND1 
1220 C CD2 . HIS   B 15  ? 0.1381 0.1589 0.1994 0.0087  0.0061  0.0442  21  HIS   C CD2 
1221 C CE1 . HIS   B 15  ? 0.1494 0.1680 0.2047 0.0080  0.0057  0.0370  21  HIS   C CE1 
1222 N NE2 . HIS   B 15  ? 0.1410 0.1604 0.1943 0.0085  0.0049  0.0411  21  HIS   C NE2 
1223 N N   . LEU   B 16  ? 0.1190 0.1412 0.1914 0.0067  0.0035  0.0441  22  LEU   C N   
1224 C CA  . LEU   B 16  ? 0.1361 0.1596 0.2057 0.0062  -0.0002 0.0464  22  LEU   C CA  
1225 C C   . LEU   B 16  ? 0.1348 0.1593 0.2117 0.0056  -0.0003 0.0472  22  LEU   C C   
1226 O O   . LEU   B 16  ? 0.1459 0.1714 0.2220 0.0049  -0.0037 0.0485  22  LEU   C O   
1227 C CB  . LEU   B 16  ? 0.1385 0.1605 0.1980 0.0057  -0.0027 0.0437  22  LEU   C CB  
1228 C CG  . LEU   B 16  ? 0.1505 0.1715 0.2030 0.0064  -0.0024 0.0435  22  LEU   C CG  
1229 C CD1 . LEU   B 16  ? 0.1611 0.1802 0.2040 0.0060  -0.0043 0.0405  22  LEU   C CD1 
1230 C CD2 . LEU   B 16  ? 0.1595 0.1819 0.2113 0.0074  -0.0034 0.0481  22  LEU   C CD2 
1231 N N   . ALA   B 17  ? 0.1380 0.1616 0.2217 0.0058  0.0034  0.0458  23  ALA   C N   
1232 C CA  . ALA   B 17  ? 0.1326 0.1567 0.2233 0.0054  0.0044  0.0463  23  ALA   C CA  
1233 C C   . ALA   B 17  ? 0.1479 0.1751 0.2462 0.0056  0.0025  0.0515  23  ALA   C C   
1234 O O   . ALA   B 17  ? 0.1514 0.1799 0.2525 0.0064  0.0025  0.0546  23  ALA   C O   
1235 C CB  . ALA   B 17  ? 0.1512 0.1733 0.2471 0.0059  0.0091  0.0439  23  ALA   C CB  
1236 N N   . THR   B 18  ? 0.1542 0.1826 0.2564 0.0048  0.0009  0.0525  24  THR   C N   
1237 C CA  . THR   B 18  ? 0.1534 0.1853 0.2640 0.0049  -0.0017 0.0575  24  THR   C CA  
1238 C C   . THR   B 18  ? 0.1372 0.1695 0.2602 0.0056  0.0027  0.0591  24  THR   C C   
1239 O O   . THR   B 18  ? 0.1435 0.1732 0.2680 0.0059  0.0075  0.0561  24  THR   C O   
1240 C CB  . THR   B 18  ? 0.1673 0.2005 0.2773 0.0036  -0.0060 0.0578  24  THR   C CB  
1241 O OG1 . THR   B 18  ? 0.1706 0.2023 0.2845 0.0031  -0.0027 0.0555  24  THR   C OG1 
1242 C CG2 . THR   B 18  ? 0.1895 0.2215 0.2870 0.0028  -0.0101 0.0557  24  THR   C CG2 
1243 N N   . HIS   B 19  ? 0.1492 0.1849 0.2818 0.0061  0.0008  0.0642  25  HIS   C N   
1244 C CA  . HIS   B 19  ? 0.1558 0.1922 0.3016 0.0068  0.0049  0.0660  25  HIS   C CA  
1245 C C   . HIS   B 19  ? 0.1308 0.1658 0.2792 0.0060  0.0074  0.0634  25  HIS   C C   
1246 O O   . HIS   B 19  ? 0.1522 0.1847 0.3048 0.0067  0.0131  0.0616  25  HIS   C O   
1247 C CB  . HIS   B 19  ? 0.1663 0.2070 0.3224 0.0073  0.0016  0.0722  25  HIS   C CB  
1248 C CG  . HIS   B 19  ? 0.1929 0.2347 0.3639 0.0080  0.0055  0.0744  25  HIS   C CG  
1249 N ND1 . HIS   B 19  ? 0.2141 0.2540 0.3917 0.0093  0.0115  0.0744  25  HIS   C ND1 
1250 C CD2 . HIS   B 19  ? 0.2150 0.2587 0.3947 0.0073  0.0052  0.0755  25  HIS   C CD2 
1251 C CE1 . HIS   B 19  ? 0.2050 0.2463 0.3956 0.0097  0.0140  0.0766  25  HIS   C CE1 
1252 N NE2 . HIS   B 19  ? 0.2041 0.2476 0.3965 0.0086  0.0107  0.0772  25  HIS   C NE2 
1253 N N   . ASN   B 20  ? 0.1427 0.1786 0.2879 0.0047  0.0035  0.0630  26  ASN   C N   
1254 C CA  . ASN   B 20  ? 0.1519 0.1861 0.2995 0.0040  0.0064  0.0608  26  ASN   C CA  
1255 C C   . ASN   B 20  ? 0.1365 0.1659 0.2754 0.0044  0.0112  0.0558  26  ASN   C C   
1256 O O   . ASN   B 20  ? 0.1325 0.1595 0.2749 0.0049  0.0164  0.0543  26  ASN   C O   
1257 C CB  . ASN   B 20  ? 0.1755 0.2113 0.3215 0.0024  0.0014  0.0610  26  ASN   C CB  
1258 C CG  . ASN   B 20  ? 0.2637 0.2981 0.4148 0.0019  0.0051  0.0598  26  ASN   C CG  
1259 O OD1 . ASN   B 20  ? 0.2954 0.3313 0.4593 0.0022  0.0076  0.0625  26  ASN   C OD1 
1260 N ND2 . ASN   B 20  ? 0.2895 0.3204 0.4310 0.0013  0.0062  0.0560  26  ASN   C ND2 
1261 N N   . ASP   B 21  ? 0.1259 0.1536 0.2531 0.0044  0.0096  0.0529  27  ASP   C N   
1262 C CA  . ASP   B 21  ? 0.1324 0.1558 0.2517 0.0049  0.0134  0.0482  27  ASP   C CA  
1263 C C   . ASP   B 21  ? 0.1202 0.1417 0.2450 0.0061  0.0189  0.0473  27  ASP   C C   
1264 O O   . ASP   B 21  ? 0.1392 0.1573 0.2628 0.0067  0.0233  0.0445  27  ASP   C O   
1265 C CB  . ASP   B 21  ? 0.1361 0.1586 0.2442 0.0047  0.0108  0.0458  27  ASP   C CB  
1266 C CG  . ASP   B 21  ? 0.1370 0.1596 0.2369 0.0037  0.0066  0.0449  27  ASP   C CG  
1267 O OD1 . ASP   B 21  ? 0.1589 0.1804 0.2585 0.0031  0.0071  0.0440  27  ASP   C OD1 
1268 O OD2 . ASP   B 21  ? 0.1416 0.1653 0.2361 0.0035  0.0030  0.0454  27  ASP   C OD2 
1269 N N   . TRP   B 22  ? 0.1294 0.1528 0.2604 0.0067  0.0187  0.0500  28  TRP   C N   
1270 C CA  . TRP   B 22  ? 0.1287 0.1500 0.2658 0.0078  0.0238  0.0491  28  TRP   C CA  
1271 C C   . TRP   B 22  ? 0.1318 0.1529 0.2795 0.0084  0.0281  0.0507  28  TRP   C C   
1272 O O   . TRP   B 22  ? 0.1446 0.1619 0.2935 0.0093  0.0335  0.0479  28  TRP   C O   
1273 C CB  . TRP   B 22  ? 0.1329 0.1563 0.2750 0.0084  0.0229  0.0522  28  TRP   C CB  
1274 C CG  . TRP   B 22  ? 0.1356 0.1577 0.2690 0.0082  0.0217  0.0494  28  TRP   C CG  
1275 C CD1 . TRP   B 22  ? 0.1570 0.1810 0.2840 0.0078  0.0174  0.0508  28  TRP   C CD1 
1276 C CD2 . TRP   B 22  ? 0.1225 0.1409 0.2532 0.0085  0.0250  0.0447  28  TRP   C CD2 
1277 N NE1 . TRP   B 22  ? 0.1548 0.1769 0.2765 0.0079  0.0182  0.0477  28  TRP   C NE1 
1278 C CE2 . TRP   B 22  ? 0.1435 0.1624 0.2678 0.0082  0.0224  0.0439  28  TRP   C CE2 
1279 C CE3 . TRP   B 22  ? 0.1538 0.1687 0.2873 0.0091  0.0297  0.0411  28  TRP   C CE3 
1280 C CZ2 . TRP   B 22  ? 0.1435 0.1599 0.2657 0.0083  0.0242  0.0399  28  TRP   C CZ2 
1281 C CZ3 . TRP   B 22  ? 0.1624 0.1744 0.2924 0.0091  0.0310  0.0367  28  TRP   C CZ3 
1282 C CH2 . TRP   B 22  ? 0.1595 0.1726 0.2846 0.0086  0.0280  0.0362  28  TRP   C CH2 
1283 N N   . ALA   B 23  ? 0.1320 0.1566 0.2865 0.0079  0.0257  0.0548  29  ALA   C N   
1284 C CA  . ALA   B 23  ? 0.1353 0.1601 0.3015 0.0085  0.0298  0.0569  29  ALA   C CA  
1285 C C   . ALA   B 23  ? 0.1545 0.1757 0.3158 0.0085  0.0334  0.0536  29  ALA   C C   
1286 O O   . ALA   B 23  ? 0.1636 0.1837 0.3330 0.0092  0.0384  0.0545  29  ALA   C O   
1287 C CB  . ALA   B 23  ? 0.1462 0.1765 0.3223 0.0079  0.0253  0.0625  29  ALA   C CB  
1288 N N   . ASN   B 24  ? 0.1502 0.1694 0.2984 0.0077  0.0312  0.0501  30  ASN   C N   
1289 C CA  . ASN   B 24  ? 0.1420 0.1573 0.2840 0.0079  0.0346  0.0472  30  ASN   C CA  
1290 C C   . ASN   B 24  ? 0.1450 0.1560 0.2732 0.0084  0.0355  0.0418  30  ASN   C C   
1291 O O   . ASN   B 24  ? 0.1496 0.1585 0.2681 0.0081  0.0346  0.0395  30  ASN   C O   
1292 C CB  . ASN   B 24  ? 0.1622 0.1799 0.3035 0.0064  0.0305  0.0488  30  ASN   C CB  
1293 C CG  . ASN   B 24  ? 0.1784 0.2001 0.3344 0.0059  0.0299  0.0536  30  ASN   C CG  
1294 O OD1 . ASN   B 24  ? 0.2052 0.2257 0.3691 0.0066  0.0352  0.0547  30  ASN   C OD1 
1295 N ND2 . ASN   B 24  ? 0.1892 0.2157 0.3498 0.0050  0.0238  0.0568  30  ASN   C ND2 
1296 N N   . LEU   B 25  ? 0.1495 0.1592 0.2771 0.0091  0.0367  0.0400  31  LEU   C N   
1297 C CA  . LEU   B 25  ? 0.1456 0.1521 0.2618 0.0094  0.0362  0.0350  31  LEU   C CA  
1298 C C   . LEU   B 25  ? 0.1742 0.1752 0.2823 0.0105  0.0405  0.0309  31  LEU   C C   
1299 O O   . LEU   B 25  ? 0.1843 0.1826 0.2966 0.0116  0.0460  0.0307  31  LEU   C O   
1300 C CB  . LEU   B 25  ? 0.1543 0.1608 0.2751 0.0098  0.0371  0.0344  31  LEU   C CB  
1301 C CG  . LEU   B 25  ? 0.1593 0.1632 0.2707 0.0098  0.0360  0.0295  31  LEU   C CG  
1302 C CD1 . LEU   B 25  ? 0.1624 0.1689 0.2668 0.0088  0.0304  0.0298  31  LEU   C CD1 
1303 C CD2 . LEU   B 25  ? 0.1820 0.1854 0.3001 0.0102  0.0378  0.0287  31  LEU   C CD2 
1304 N N   . VAL   B 26  ? 0.1619 0.1611 0.2579 0.0104  0.0381  0.0276  32  VAL   C N   
1305 C CA  . VAL   B 26  ? 0.1721 0.1658 0.2582 0.0117  0.0413  0.0233  32  VAL   C CA  
1306 C C   . VAL   B 26  ? 0.1830 0.1747 0.2631 0.0120  0.0400  0.0186  32  VAL   C C   
1307 O O   . VAL   B 26  ? 0.1965 0.1837 0.2737 0.0132  0.0436  0.0150  32  VAL   C O   
1308 C CB  . VAL   B 26  ? 0.1818 0.1748 0.2590 0.0116  0.0395  0.0233  32  VAL   C CB  
1309 C CG1 . VAL   B 26  ? 0.2130 0.2003 0.2778 0.0132  0.0420  0.0189  32  VAL   C CG1 
1310 C CG2 . VAL   B 26  ? 0.1934 0.1880 0.2776 0.0111  0.0411  0.0276  32  VAL   C CG2 
1311 N N   . TRP   B 27  ? 0.1545 0.1491 0.2327 0.0110  0.0349  0.0184  33  TRP   C N   
1312 C CA  . TRP   B 27  ? 0.1553 0.1484 0.2289 0.0111  0.0333  0.0140  33  TRP   C CA  
1313 C C   . TRP   B 27  ? 0.1547 0.1523 0.2314 0.0099  0.0289  0.0158  33  TRP   C C   
1314 O O   . TRP   B 27  ? 0.1526 0.1532 0.2288 0.0091  0.0262  0.0190  33  TRP   C O   
1315 C CB  . TRP   B 27  ? 0.1856 0.1752 0.2461 0.0120  0.0323  0.0100  33  TRP   C CB  
1316 C CG  . TRP   B 27  ? 0.1889 0.1778 0.2443 0.0119  0.0290  0.0057  33  TRP   C CG  
1317 C CD1 . TRP   B 27  ? 0.2169 0.2028 0.2714 0.0125  0.0299  0.0010  33  TRP   C CD1 
1318 C CD2 . TRP   B 27  ? 0.1668 0.1585 0.2188 0.0112  0.0242  0.0056  33  TRP   C CD2 
1319 N NE1 . TRP   B 27  ? 0.2280 0.2147 0.2787 0.0121  0.0256  -0.0020 33  TRP   C NE1 
1320 C CE2 . TRP   B 27  ? 0.1930 0.1834 0.2423 0.0114  0.0224  0.0010  33  TRP   C CE2 
1321 C CE3 . TRP   B 27  ? 0.1618 0.1567 0.2128 0.0105  0.0214  0.0089  33  TRP   C CE3 
1322 C CZ2 . TRP   B 27  ? 0.1913 0.1837 0.2377 0.0110  0.0180  -0.0001 33  TRP   C CZ2 
1323 C CZ3 . TRP   B 27  ? 0.1889 0.1852 0.2357 0.0102  0.0175  0.0075  33  TRP   C CZ3 
1324 C CH2 . TRP   B 27  ? 0.1881 0.1835 0.2335 0.0105  0.0160  0.0034  33  TRP   C CH2 
1325 N N   . GLU   B 28  ? 0.1392 0.1369 0.2191 0.0097  0.0284  0.0139  34  GLU   C N   
1326 C CA  . GLU   B 28  ? 0.1509 0.1522 0.2331 0.0088  0.0250  0.0155  34  GLU   C CA  
1327 C C   . GLU   B 28  ? 0.1538 0.1538 0.2355 0.0087  0.0242  0.0113  34  GLU   C C   
1328 O O   . GLU   B 28  ? 0.1551 0.1519 0.2386 0.0092  0.0266  0.0078  34  GLU   C O   
1329 C CB  . GLU   B 28  ? 0.1646 0.1693 0.2569 0.0084  0.0254  0.0207  34  GLU   C CB  
1330 C CG  . GLU   B 28  ? 0.1662 0.1696 0.2681 0.0088  0.0294  0.0209  34  GLU   C CG  
1331 C CD  . GLU   B 28  ? 0.1886 0.1914 0.2953 0.0086  0.0300  0.0188  34  GLU   C CD  
1332 O OE1 . GLU   B 28  ? 0.2214 0.2215 0.3336 0.0091  0.0335  0.0168  34  GLU   C OE1 
1333 O OE2 . GLU   B 28  ? 0.1761 0.1809 0.2819 0.0081  0.0273  0.0191  34  GLU   C OE2 
1334 N N   . ASP   B 29  ? 0.1352 0.1375 0.2150 0.0082  0.0209  0.0114  35  ASP   C N   
1335 C CA  . ASP   B 29  ? 0.1388 0.1405 0.2201 0.0080  0.0198  0.0076  35  ASP   C CA  
1336 C C   . ASP   B 29  ? 0.1394 0.1448 0.2245 0.0074  0.0180  0.0107  35  ASP   C C   
1337 O O   . ASP   B 29  ? 0.1311 0.1381 0.2106 0.0073  0.0155  0.0118  35  ASP   C O   
1338 C CB  . ASP   B 29  ? 0.1729 0.1722 0.2443 0.0085  0.0176  0.0028  35  ASP   C CB  
1339 C CG  . ASP   B 29  ? 0.2237 0.2224 0.2965 0.0083  0.0157  -0.0018 35  ASP   C CG  
1340 O OD1 . ASP   B 29  ? 0.2237 0.2250 0.3034 0.0075  0.0150  -0.0004 35  ASP   C OD1 
1341 O OD2 . ASP   B 29  ? 0.2687 0.2644 0.3351 0.0089  0.0146  -0.0066 35  ASP   C OD2 
1342 N N   . SER   B 30  ? 0.1358 0.1421 0.2308 0.0071  0.0198  0.0122  36  SER   C N   
1343 C CA  A SER   B 30  ? 0.1356 0.1450 0.2348 0.0068  0.0191  0.0155  36  SER   C CA  
1344 C CA  B SER   B 30  ? 0.1381 0.1475 0.2367 0.0068  0.0190  0.0156  36  SER   C CA  
1345 C C   . SER   B 30  ? 0.1447 0.1545 0.2407 0.0066  0.0167  0.0125  36  SER   C C   
1346 O O   . SER   B 30  ? 0.1382 0.1502 0.2320 0.0066  0.0155  0.0152  36  SER   C O   
1347 C CB  A SER   B 30  ? 0.1458 0.1554 0.2566 0.0066  0.0220  0.0173  36  SER   C CB  
1348 C CB  B SER   B 30  ? 0.1590 0.1690 0.2688 0.0067  0.0219  0.0184  36  SER   C CB  
1349 O OG  A SER   B 30  ? 0.1459 0.1576 0.2606 0.0065  0.0219  0.0197  36  SER   C OG  
1350 O OG  B SER   B 30  ? 0.1768 0.1843 0.2920 0.0064  0.0233  0.0138  36  SER   C OG  
1351 N N   . SER   B 31  ? 0.1379 0.1455 0.2334 0.0064  0.0159  0.0069  37  SER   C N   
1352 C CA  . SER   B 31  ? 0.1499 0.1583 0.2440 0.0063  0.0133  0.0040  37  SER   C CA  
1353 C C   . SER   B 31  ? 0.1408 0.1500 0.2248 0.0068  0.0106  0.0044  37  SER   C C   
1354 O O   . SER   B 31  ? 0.1475 0.1583 0.2313 0.0068  0.0089  0.0041  37  SER   C O   
1355 C CB  . SER   B 31  ? 0.1902 0.1962 0.2856 0.0060  0.0121  -0.0023 37  SER   C CB  
1356 O OG  . SER   B 31  ? 0.2462 0.2495 0.3317 0.0067  0.0106  -0.0057 37  SER   C OG  
1357 N N   . ARG   B 32  ? 0.1274 0.1353 0.2036 0.0072  0.0106  0.0053  38  ARG   C N   
1358 C CA  . ARG   B 32  ? 0.1368 0.1451 0.2038 0.0077  0.0084  0.0059  38  ARG   C CA  
1359 C C   . ARG   B 32  ? 0.1268 0.1370 0.1928 0.0075  0.0088  0.0110  38  ARG   C C   
1360 O O   . ARG   B 32  ? 0.1203 0.1306 0.1792 0.0078  0.0071  0.0117  38  ARG   C O   
1361 C CB  . ARG   B 32  ? 0.1535 0.1587 0.2127 0.0083  0.0083  0.0036  38  ARG   C CB  
1362 C CG  . ARG   B 32  ? 0.1643 0.1670 0.2214 0.0088  0.0072  -0.0018 38  ARG   C CG  
1363 C CD  . ARG   B 32  ? 0.1397 0.1388 0.1879 0.0098  0.0077  -0.0037 38  ARG   C CD  
1364 N NE  . ARG   B 32  ? 0.1420 0.1411 0.1816 0.0105  0.0059  -0.0025 38  ARG   C NE  
1365 C CZ  . ARG   B 32  ? 0.1510 0.1472 0.1814 0.0117  0.0051  -0.0047 38  ARG   C CZ  
1366 N NH1 . ARG   B 32  ? 0.1716 0.1644 0.1989 0.0125  0.0058  -0.0084 38  ARG   C NH1 
1367 N NH2 . ARG   B 32  ? 0.1534 0.1497 0.1773 0.0123  0.0036  -0.0033 38  ARG   C NH2 
1368 N N   . ASP   B 33  ? 0.1100 0.1214 0.1825 0.0072  0.0108  0.0146  39  ASP   C N   
1369 C CA  . ASP   B 33  ? 0.1083 0.1213 0.1794 0.0071  0.0106  0.0194  39  ASP   C CA  
1370 C C   . ASP   B 33  ? 0.1065 0.1184 0.1717 0.0071  0.0098  0.0197  39  ASP   C C   
1371 O O   . ASP   B 33  ? 0.1142 0.1270 0.1748 0.0069  0.0082  0.0219  39  ASP   C O   
1372 C CB  . ASP   B 33  ? 0.1092 0.1238 0.1771 0.0073  0.0093  0.0212  39  ASP   C CB  
1373 C CG  . ASP   B 33  ? 0.1173 0.1332 0.1832 0.0073  0.0088  0.0259  39  ASP   C CG  
1374 O OD1 . ASP   B 33  ? 0.1283 0.1451 0.1995 0.0072  0.0099  0.0290  39  ASP   C OD1 
1375 O OD2 . ASP   B 33  ? 0.1208 0.1369 0.1802 0.0074  0.0072  0.0266  39  ASP   C OD2 
1376 N N   . LEU   B 34  ? 0.1047 0.1146 0.1703 0.0072  0.0112  0.0175  40  LEU   C N   
1377 C CA  . LEU   B 34  ? 0.1192 0.1280 0.1804 0.0073  0.0112  0.0182  40  LEU   C CA  
1378 C C   . LEU   B 34  ? 0.1123 0.1207 0.1798 0.0073  0.0139  0.0199  40  LEU   C C   
1379 O O   . LEU   B 34  ? 0.1219 0.1293 0.1950 0.0075  0.0162  0.0186  40  LEU   C O   
1380 C CB  . LEU   B 34  ? 0.1253 0.1311 0.1790 0.0080  0.0109  0.0141  40  LEU   C CB  
1381 C CG  . LEU   B 34  ? 0.1285 0.1343 0.1750 0.0082  0.0082  0.0127  40  LEU   C CG  
1382 C CD1 . LEU   B 34  ? 0.1554 0.1581 0.1946 0.0092  0.0080  0.0091  40  LEU   C CD1 
1383 C CD2 . LEU   B 34  ? 0.1430 0.1500 0.1864 0.0077  0.0067  0.0158  40  LEU   C CD2 
1384 N N   . LEU   B 35  ? 0.1063 0.1153 0.1735 0.0070  0.0137  0.0226  41  LEU   C N   
1385 C CA  . LEU   B 35  ? 0.1163 0.1249 0.1897 0.0071  0.0165  0.0243  41  LEU   C CA  
1386 C C   . LEU   B 35  ? 0.1212 0.1288 0.1907 0.0070  0.0164  0.0249  41  LEU   C C   
1387 O O   . LEU   B 35  ? 0.1296 0.1383 0.1948 0.0064  0.0134  0.0259  41  LEU   C O   
1388 C CB  . LEU   B 35  ? 0.1162 0.1281 0.1982 0.0067  0.0160  0.0290  41  LEU   C CB  
1389 C CG  . LEU   B 35  ? 0.1166 0.1288 0.2073 0.0069  0.0187  0.0315  41  LEU   C CG  
1390 C CD1 . LEU   B 35  ? 0.1393 0.1537 0.2395 0.0071  0.0196  0.0347  41  LEU   C CD1 
1391 C CD2 . LEU   B 35  ? 0.1315 0.1453 0.2226 0.0063  0.0171  0.0343  41  LEU   C CD2 
1392 N N   . VAL   B 36  ? 0.1254 0.1305 0.1963 0.0076  0.0199  0.0240  42  VAL   C N   
1393 C CA  . VAL   B 36  ? 0.1272 0.1310 0.1962 0.0076  0.0211  0.0249  42  VAL   C CA  
1394 C C   . VAL   B 36  ? 0.1206 0.1254 0.1998 0.0076  0.0240  0.0281  42  VAL   C C   
1395 O O   . VAL   B 36  ? 0.1379 0.1415 0.2219 0.0083  0.0274  0.0275  42  VAL   C O   
1396 C CB  . VAL   B 36  ? 0.1347 0.1340 0.1949 0.0089  0.0234  0.0212  42  VAL   C CB  
1397 C CG1 . VAL   B 36  ? 0.1570 0.1546 0.2156 0.0091  0.0254  0.0226  42  VAL   C CG1 
1398 C CG2 . VAL   B 36  ? 0.1540 0.1528 0.2052 0.0090  0.0199  0.0183  42  VAL   C CG2 
1399 N N   . SER   B 37  ? 0.1207 0.1276 0.2037 0.0067  0.0226  0.0313  43  SER   C N   
1400 C CA  . SER   B 37  ? 0.1191 0.1275 0.2130 0.0066  0.0251  0.0347  43  SER   C CA  
1401 C C   . SER   B 37  ? 0.1309 0.1374 0.2240 0.0066  0.0271  0.0352  43  SER   C C   
1402 O O   . SER   B 37  ? 0.1401 0.1449 0.2248 0.0064  0.0257  0.0336  43  SER   C O   
1403 C CB  . SER   B 37  ? 0.1277 0.1409 0.2293 0.0055  0.0209  0.0387  43  SER   C CB  
1404 O OG  . SER   B 37  ? 0.1456 0.1604 0.2425 0.0043  0.0161  0.0392  43  SER   C OG  
1405 N N   . SER   B 38  ? 0.1399 0.1466 0.2427 0.0069  0.0310  0.0376  44  SER   C N   
1406 C CA  . SER   B 38  ? 0.1547 0.1597 0.2589 0.0069  0.0339  0.0386  44  SER   C CA  
1407 C C   . SER   B 38  ? 0.1766 0.1859 0.2887 0.0050  0.0296  0.0421  44  SER   C C   
1408 O O   . SER   B 38  ? 0.1879 0.2014 0.3075 0.0041  0.0259  0.0446  44  SER   C O   
1409 C CB  . SER   B 38  ? 0.1834 0.1860 0.2941 0.0084  0.0410  0.0393  44  SER   C CB  
1410 O OG  . SER   B 38  ? 0.2210 0.2276 0.3453 0.0080  0.0407  0.0427  44  SER   C OG  
1411 N N   . THR   B 39  ? 0.1737 0.1815 0.2842 0.0045  0.0301  0.0423  45  THR   C N   
1412 C CA  . THR   B 39  ? 0.1843 0.1954 0.3020 0.0025  0.0258  0.0449  45  THR   C CA  
1413 C C   . THR   B 39  ? 0.2087 0.2191 0.3364 0.0025  0.0306  0.0473  45  THR   C C   
1414 O O   . THR   B 39  ? 0.2078 0.2138 0.3318 0.0040  0.0369  0.0465  45  THR   C O   
1415 C CB  . THR   B 39  ? 0.1969 0.2068 0.3040 0.0015  0.0216  0.0427  45  THR   C CB  
1416 O OG1 . THR   B 39  ? 0.2102 0.2153 0.3097 0.0026  0.0259  0.0410  45  THR   C OG1 
1417 C CG2 . THR   B 39  ? 0.2033 0.2137 0.3006 0.0017  0.0174  0.0404  45  THR   C CG2 
1418 N N   . THR   B 40  ? 0.2355 0.2500 0.3752 0.0007  0.0272  0.0503  46  THR   C N   
1419 C CA  . THR   B 40  ? 0.2580 0.2722 0.4091 0.0003  0.0313  0.0529  46  THR   C CA  
1420 C C   . THR   B 40  ? 0.2628 0.2738 0.4075 -0.0004 0.0315  0.0516  46  THR   C C   
1421 O O   . THR   B 40  ? 0.2940 0.3012 0.4394 0.0007  0.0381  0.0522  46  THR   C O   
1422 C CB  . THR   B 40  ? 0.3063 0.3264 0.4742 -0.0013 0.0273  0.0566  46  THR   C CB  
1423 O OG1 . THR   B 40  ? 0.3629 0.3860 0.5281 -0.0034 0.0186  0.0560  46  THR   C OG1 
1424 C CG2 . THR   B 40  ? 0.2981 0.3209 0.4726 -0.0002 0.0281  0.0583  46  THR   C CG2 
1425 N N   . ALA   B 41  ? 0.2320 0.2440 0.3699 -0.0020 0.0247  0.0499  47  ALA   C N   
1426 C CA  . ALA   B 41  ? 0.2429 0.2518 0.3752 -0.0027 0.0244  0.0486  47  ALA   C CA  
1427 C C   . ALA   B 41  ? 0.2293 0.2333 0.3445 -0.0009 0.0265  0.0454  47  ALA   C C   
1428 O O   . ALA   B 41  ? 0.2252 0.2295 0.3323 0.0000  0.0248  0.0435  47  ALA   C O   
1429 C CB  . ALA   B 41  ? 0.2661 0.2780 0.4000 -0.0053 0.0162  0.0482  47  ALA   C CB  
1430 N N   . GLN   B 42  ? 0.2248 0.2245 0.3350 -0.0003 0.0299  0.0450  48  GLN   C N   
1431 C CA  . GLN   B 42  ? 0.2363 0.2315 0.3308 0.0015  0.0313  0.0423  48  GLN   C CA  
1432 C C   . GLN   B 42  ? 0.2305 0.2266 0.3176 0.0002  0.0245  0.0400  48  GLN   C C   
1433 O O   . GLN   B 42  ? 0.2474 0.2452 0.3401 -0.0020 0.0204  0.0405  48  GLN   C O   
1434 C CB  . GLN   B 42  ? 0.2975 0.2875 0.3893 0.0029  0.0376  0.0433  48  GLN   C CB  
1435 C CG  . GLN   B 42  ? 0.4142 0.4017 0.5081 0.0051  0.0456  0.0448  48  GLN   C CG  
1436 C CD  . GLN   B 42  ? 0.5657 0.5476 0.6546 0.0069  0.0519  0.0459  48  GLN   C CD  
1437 O OE1 . GLN   B 42  ? 0.6157 0.5972 0.7135 0.0058  0.0539  0.0485  48  GLN   C OE1 
1438 N NE2 . GLN   B 42  ? 0.6137 0.5909 0.6882 0.0097  0.0550  0.0441  48  GLN   C NE2 
1439 N N   . GLY   B 43  ? 0.2040 0.1988 0.2790 0.0016  0.0234  0.0373  49  GLY   C N   
1440 C CA  . GLY   B 43  ? 0.2052 0.2001 0.2718 0.0010  0.0181  0.0350  49  GLY   C CA  
1441 C C   . GLY   B 43  ? 0.2138 0.2042 0.2714 0.0021  0.0199  0.0339  49  GLY   C C   
1442 O O   . GLY   B 43  ? 0.2451 0.2319 0.3006 0.0039  0.0254  0.0347  49  GLY   C O   
1443 N N   . CYS   B 44  ? 0.1906 0.1807 0.2424 0.0015  0.0157  0.0321  50  CYS   C N   
1444 C CA  . CYS   B 44  ? 0.1995 0.1855 0.2440 0.0024  0.0170  0.0314  50  CYS   C CA  
1445 C C   . CYS   B 44  ? 0.2092 0.1940 0.2423 0.0039  0.0151  0.0289  50  CYS   C C   
1446 O O   . CYS   B 44  ? 0.2504 0.2320 0.2777 0.0048  0.0156  0.0284  50  CYS   C O   
1447 C CB  . CYS   B 44  ? 0.2024 0.1882 0.2525 0.0001  0.0144  0.0319  50  CYS   C CB  
1448 S SG  . CYS   B 44  ? 0.2833 0.2704 0.3490 -0.0017 0.0169  0.0351  50  CYS   C SG  
1449 N N   . ASP   B 45  ? 0.1708 0.1583 0.2014 0.0043  0.0129  0.0274  51  ASP   C N   
1450 C CA  . ASP   B 45  ? 0.1743 0.1610 0.1955 0.0057  0.0111  0.0250  51  ASP   C CA  
1451 C C   . ASP   B 45  ? 0.1935 0.1771 0.2083 0.0083  0.0148  0.0246  51  ASP   C C   
1452 O O   . ASP   B 45  ? 0.2167 0.1996 0.2337 0.0090  0.0184  0.0255  51  ASP   C O   
1453 C CB  . ASP   B 45  ? 0.1823 0.1727 0.2042 0.0052  0.0082  0.0239  51  ASP   C CB  
1454 C CG  . ASP   B 45  ? 0.2138 0.2069 0.2393 0.0032  0.0042  0.0241  51  ASP   C CG  
1455 O OD1 . ASP   B 45  ? 0.2401 0.2317 0.2642 0.0023  0.0025  0.0238  51  ASP   C OD1 
1456 O OD2 . ASP   B 45  ? 0.1946 0.1909 0.2238 0.0025  0.0026  0.0246  51  ASP   C OD2 
1457 N N   . THR   B 46  ? 0.1733 0.1548 0.1799 0.0098  0.0139  0.0232  52  THR   C N   
1458 C CA  . THR   B 46  ? 0.1744 0.1530 0.1730 0.0125  0.0160  0.0224  52  THR   C CA  
1459 C C   . THR   B 46  ? 0.1662 0.1469 0.1611 0.0132  0.0130  0.0197  52  THR   C C   
1460 O O   . THR   B 46  ? 0.1751 0.1576 0.1696 0.0126  0.0097  0.0187  52  THR   C O   
1461 C CB  . THR   B 46  ? 0.2073 0.1821 0.1999 0.0140  0.0169  0.0231  52  THR   C CB  
1462 O OG1 . THR   B 46  ? 0.2368 0.2094 0.2340 0.0133  0.0203  0.0258  52  THR   C OG1 
1463 C CG2 . THR   B 46  ? 0.2516 0.2235 0.2344 0.0171  0.0180  0.0222  52  THR   C CG2 
1464 N N   . ILE   B 47  ? 0.1727 0.1530 0.1651 0.0145  0.0143  0.0183  53  ILE   C N   
1465 C CA  . ILE   B 47  ? 0.1668 0.1490 0.1568 0.0151  0.0114  0.0156  53  ILE   C CA  
1466 C C   . ILE   B 47  ? 0.1597 0.1394 0.1408 0.0174  0.0101  0.0143  53  ILE   C C   
1467 O O   . ILE   B 47  ? 0.1810 0.1569 0.1559 0.0194  0.0125  0.0149  53  ILE   C O   
1468 C CB  . ILE   B 47  ? 0.1790 0.1613 0.1702 0.0155  0.0131  0.0142  53  ILE   C CB  
1469 C CG1 . ILE   B 47  ? 0.1828 0.1672 0.1833 0.0137  0.0150  0.0160  53  ILE   C CG1 
1470 C CG2 . ILE   B 47  ? 0.1869 0.1711 0.1769 0.0159  0.0100  0.0112  53  ILE   C CG2 
1471 C CD1 . ILE   B 47  ? 0.2072 0.1958 0.2139 0.0116  0.0117  0.0167  53  ILE   C CD1 
1472 N N   . ALA   B 48  ? 0.1506 0.1324 0.1310 0.0175  0.0065  0.0128  54  ALA   C N   
1473 C CA  . ALA   B 48  ? 0.1541 0.1343 0.1273 0.0197  0.0046  0.0116  54  ALA   C CA  
1474 C C   . ALA   B 48  ? 0.1489 0.1280 0.1175 0.0214  0.0044  0.0093  54  ALA   C C   
1475 O O   . ALA   B 48  ? 0.1593 0.1402 0.1319 0.0204  0.0042  0.0075  54  ALA   C O   
1476 C CB  . ALA   B 48  ? 0.1579 0.1412 0.1337 0.0192  0.0010  0.0105  54  ALA   C CB  
1477 N N   . ARG   B 49  ? 0.1618 0.1374 0.1216 0.0240  0.0042  0.0092  55  ARG   C N   
1478 C CA  . ARG   B 49  ? 0.1651 0.1390 0.1184 0.0259  0.0032  0.0065  55  ARG   C CA  
1479 C C   . ARG   B 49  ? 0.1691 0.1431 0.1173 0.0279  -0.0010 0.0056  55  ARG   C C   
1480 O O   . ARG   B 49  ? 0.1922 0.1630 0.1332 0.0301  -0.0005 0.0075  55  ARG   C O   
1481 C CB  . ARG   B 49  ? 0.1828 0.1517 0.1292 0.0275  0.0077  0.0076  55  ARG   C CB  
1482 C CG  . ARG   B 49  ? 0.1748 0.1440 0.1283 0.0256  0.0121  0.0090  55  ARG   C CG  
1483 C CD  . ARG   B 49  ? 0.1895 0.1614 0.1489 0.0240  0.0113  0.0062  55  ARG   C CD  
1484 N NE  . ARG   B 49  ? 0.1892 0.1613 0.1555 0.0225  0.0157  0.0081  55  ARG   C NE  
1485 C CZ  . ARG   B 49  ? 0.1761 0.1512 0.1509 0.0206  0.0157  0.0073  55  ARG   C CZ  
1486 N NH1 . ARG   B 49  ? 0.1796 0.1573 0.1566 0.0201  0.0122  0.0045  55  ARG   C NH1 
1487 N NH2 . ARG   B 49  ? 0.1971 0.1727 0.1789 0.0194  0.0193  0.0096  55  ARG   C NH2 
1488 N N   . CYS   B 50  ? 0.1596 0.1375 0.1127 0.0271  -0.0050 0.0032  56  CYS   C N   
1489 C CA  . CYS   B 50  ? 0.1612 0.1405 0.1131 0.0286  -0.0093 0.0027  56  CYS   C CA  
1490 C C   . CYS   B 50  ? 0.1620 0.1458 0.1212 0.0274  -0.0129 -0.0003 56  CYS   C C   
1491 O O   . CYS   B 50  ? 0.1653 0.1508 0.1303 0.0255  -0.0120 -0.0017 56  CYS   C O   
1492 C CB  . CYS   B 50  ? 0.1539 0.1337 0.1088 0.0280  -0.0082 0.0057  56  CYS   C CB  
1493 S SG  . CYS   B 50  ? 0.1609 0.1450 0.1271 0.0246  -0.0074 0.0059  56  CYS   C SG  
1494 N N   . ASP   B 51  ? 0.1785 0.1641 0.1382 0.0287  -0.0170 -0.0009 57  ASP   C N   
1495 C CA  . ASP   B 51  ? 0.1808 0.1709 0.1492 0.0276  -0.0202 -0.0032 57  ASP   C CA  
1496 C C   . ASP   B 51  ? 0.1761 0.1686 0.1501 0.0274  -0.0204 -0.0012 57  ASP   C C   
1497 O O   . ASP   B 51  ? 0.1882 0.1840 0.1681 0.0276  -0.0234 -0.0024 57  ASP   C O   
1498 C CB  . ASP   B 51  ? 0.2152 0.2057 0.1810 0.0294  -0.0253 -0.0064 57  ASP   C CB  
1499 C CG  . ASP   B 51  ? 0.2672 0.2564 0.2265 0.0323  -0.0283 -0.0052 57  ASP   C CG  
1500 O OD1 . ASP   B 51  ? 0.2567 0.2442 0.2134 0.0330  -0.0260 -0.0019 57  ASP   C OD1 
1501 O OD2 . ASP   B 51  ? 0.3449 0.3350 0.3027 0.0338  -0.0335 -0.0078 57  ASP   C OD2 
1502 N N   . CYS   B 52  ? 0.1624 0.1534 0.1356 0.0267  -0.0169 0.0018  58  CYS   C N   
1503 C CA  . CYS   B 52  ? 0.1552 0.1480 0.1334 0.0263  -0.0165 0.0033  58  CYS   C CA  
1504 C C   . CYS   B 52  ? 0.1437 0.1406 0.1310 0.0246  -0.0170 0.0020  58  CYS   C C   
1505 O O   . CYS   B 52  ? 0.1483 0.1463 0.1389 0.0230  -0.0160 0.0010  58  CYS   C O   
1506 C CB  . CYS   B 52  ? 0.1617 0.1521 0.1384 0.0251  -0.0129 0.0058  58  CYS   C CB  
1507 S SG  . CYS   B 52  ? 0.1710 0.1565 0.1391 0.0271  -0.0115 0.0082  58  CYS   C SG  
1508 N N   . GLN   B 53  ? 0.1380 0.1368 0.1296 0.0253  -0.0178 0.0025  59  GLN   C N   
1509 C CA  . GLN   B 53  ? 0.1453 0.1474 0.1455 0.0240  -0.0172 0.0022  59  GLN   C CA  
1510 C C   . GLN   B 53  ? 0.1423 0.1438 0.1433 0.0238  -0.0146 0.0041  59  GLN   C C   
1511 O O   . GLN   B 53  ? 0.1408 0.1445 0.1479 0.0235  -0.0137 0.0042  59  GLN   C O   
1512 C CB  . GLN   B 53  ? 0.1515 0.1570 0.1583 0.0251  -0.0205 0.0003  59  GLN   C CB  
1513 C CG  . GLN   B 53  ? 0.2029 0.2094 0.2106 0.0246  -0.0231 -0.0024 59  GLN   C CG  
1514 C CD  . GLN   B 53  ? 0.2274 0.2375 0.2436 0.0251  -0.0266 -0.0045 59  GLN   C CD  
1515 O OE1 . GLN   B 53  ? 0.2503 0.2605 0.2642 0.0266  -0.0310 -0.0064 59  GLN   C OE1 
1516 N NE2 . GLN   B 53  ? 0.1916 0.2049 0.2178 0.0239  -0.0250 -0.0042 59  GLN   C NE2 
1517 N N   . THR   B 54  ? 0.1377 0.1357 0.1324 0.0241  -0.0131 0.0057  60  THR   C N   
1518 C CA  . THR   B 54  ? 0.1516 0.1482 0.1461 0.0236  -0.0106 0.0070  60  THR   C CA  
1519 C C   . THR   B 54  ? 0.1481 0.1419 0.1381 0.0220  -0.0087 0.0080  60  THR   C C   
1520 O O   . THR   B 54  ? 0.1586 0.1505 0.1445 0.0222  -0.0089 0.0083  60  THR   C O   
1521 C CB  . THR   B 54  ? 0.1905 0.1855 0.1838 0.0256  -0.0108 0.0078  60  THR   C CB  
1522 O OG1 . THR   B 54  ? 0.2508 0.2428 0.2382 0.0267  -0.0114 0.0086  60  THR   C OG1 
1523 C CG2 . THR   B 54  ? 0.1911 0.1892 0.1901 0.0273  -0.0131 0.0070  60  THR   C CG2 
1524 N N   . GLY   B 55  ? 0.1356 0.1292 0.1265 0.0204  -0.0069 0.0085  61  GLY   C N   
1525 C CA  . GLY   B 55  ? 0.1365 0.1280 0.1246 0.0187  -0.0057 0.0094  61  GLY   C CA  
1526 C C   . GLY   B 55  ? 0.1251 0.1164 0.1136 0.0174  -0.0045 0.0096  61  GLY   C C   
1527 O O   . GLY   B 55  ? 0.1453 0.1368 0.1348 0.0183  -0.0038 0.0093  61  GLY   C O   
1528 N N   . VAL   B 56  ? 0.1234 0.1137 0.1107 0.0156  -0.0041 0.0102  62  VAL   C N   
1529 C CA  . VAL   B 56  ? 0.1193 0.1088 0.1054 0.0143  -0.0036 0.0103  62  VAL   C CA  
1530 C C   . VAL   B 56  ? 0.1170 0.1087 0.1052 0.0126  -0.0039 0.0112  62  VAL   C C   
1531 O O   . VAL   B 56  ? 0.1295 0.1215 0.1189 0.0119  -0.0043 0.0117  62  VAL   C O   
1532 C CB  . VAL   B 56  ? 0.1291 0.1147 0.1117 0.0136  -0.0035 0.0103  62  VAL   C CB  
1533 C CG1 . VAL   B 56  ? 0.1511 0.1355 0.1315 0.0122  -0.0037 0.0099  62  VAL   C CG1 
1534 C CG2 . VAL   B 56  ? 0.1458 0.1288 0.1266 0.0155  -0.0029 0.0097  62  VAL   C CG2 
1535 N N   . TYR   B 57  ? 0.1223 0.1153 0.1109 0.0122  -0.0035 0.0115  63  TYR   C N   
1536 C CA  . TYR   B 57  ? 0.1141 0.1092 0.1048 0.0108  -0.0040 0.0128  63  TYR   C CA  
1537 C C   . TYR   B 57  ? 0.1194 0.1130 0.1063 0.0098  -0.0046 0.0133  63  TYR   C C   
1538 O O   . TYR   B 57  ? 0.1349 0.1265 0.1178 0.0104  -0.0039 0.0125  63  TYR   C O   
1539 C CB  . TYR   B 57  ? 0.1252 0.1236 0.1207 0.0113  -0.0031 0.0134  63  TYR   C CB  
1540 C CG  . TYR   B 57  ? 0.1240 0.1230 0.1192 0.0119  -0.0016 0.0140  63  TYR   C CG  
1541 C CD1 . TYR   B 57  ? 0.1355 0.1339 0.1305 0.0134  -0.0003 0.0131  63  TYR   C CD1 
1542 C CD2 . TYR   B 57  ? 0.1219 0.1219 0.1172 0.0112  -0.0013 0.0158  63  TYR   C CD2 
1543 C CE1 . TYR   B 57  ? 0.1396 0.1383 0.1346 0.0142  0.0018  0.0139  63  TYR   C CE1 
1544 C CE2 . TYR   B 57  ? 0.1342 0.1344 0.1287 0.0121  0.0007  0.0168  63  TYR   C CE2 
1545 C CZ  . TYR   B 57  ? 0.1378 0.1372 0.1321 0.0136  0.0025  0.0158  63  TYR   C CZ  
1546 O OH  . TYR   B 57  ? 0.1677 0.1670 0.1615 0.0147  0.0053  0.0169  63  TYR   C OH  
1547 N N   . TYR   B 58  ? 0.1258 0.1206 0.1142 0.0083  -0.0058 0.0146  64  TYR   C N   
1548 C CA  . TYR   B 58  ? 0.1287 0.1227 0.1136 0.0073  -0.0073 0.0152  64  TYR   C CA  
1549 C C   . TYR   B 58  ? 0.1277 0.1237 0.1128 0.0078  -0.0066 0.0168  64  TYR   C C   
1550 O O   . TYR   B 58  ? 0.1349 0.1339 0.1253 0.0077  -0.0062 0.0185  64  TYR   C O   
1551 C CB  . TYR   B 58  ? 0.1411 0.1353 0.1281 0.0054  -0.0096 0.0159  64  TYR   C CB  
1552 C CG  . TYR   B 58  ? 0.1522 0.1452 0.1349 0.0044  -0.0121 0.0161  64  TYR   C CG  
1553 C CD1 . TYR   B 58  ? 0.1636 0.1529 0.1397 0.0045  -0.0127 0.0140  64  TYR   C CD1 
1554 C CD2 . TYR   B 58  ? 0.1571 0.1525 0.1420 0.0036  -0.0140 0.0182  64  TYR   C CD2 
1555 C CE1 . TYR   B 58  ? 0.1715 0.1593 0.1422 0.0037  -0.0154 0.0137  64  TYR   C CE1 
1556 C CE2 . TYR   B 58  ? 0.1662 0.1605 0.1462 0.0028  -0.0170 0.0183  64  TYR   C CE2 
1557 C CZ  . TYR   B 58  ? 0.1723 0.1627 0.1448 0.0029  -0.0177 0.0158  64  TYR   C CZ  
1558 O OH  . TYR   B 58  ? 0.2147 0.2034 0.1808 0.0022  -0.0210 0.0154  64  TYR   C OH  
1559 N N   . CYS   B 59  ? 0.1281 0.1222 0.1072 0.0085  -0.0061 0.0166  65  CYS   C N   
1560 C CA  . CYS   B 59  ? 0.1378 0.1329 0.1154 0.0093  -0.0048 0.0186  65  CYS   C CA  
1561 C C   . CYS   B 59  ? 0.1499 0.1435 0.1213 0.0085  -0.0076 0.0193  65  CYS   C C   
1562 O O   . CYS   B 59  ? 0.1660 0.1561 0.1297 0.0087  -0.0080 0.0177  65  CYS   C O   
1563 C CB  . CYS   B 59  ? 0.1425 0.1362 0.1175 0.0111  -0.0016 0.0178  65  CYS   C CB  
1564 S SG  . CYS   B 59  ? 0.1705 0.1647 0.1432 0.0125  0.0011  0.0206  65  CYS   C SG  
1565 N N   . SER   B 60  ? 0.1613 0.1575 0.1360 0.0075  -0.0095 0.0215  66  SER   C N   
1566 C CA  . SER   B 60  ? 0.1748 0.1701 0.1445 0.0067  -0.0131 0.0223  66  SER   C CA  
1567 C C   . SER   B 60  ? 0.1808 0.1738 0.1412 0.0082  -0.0122 0.0231  66  SER   C C   
1568 O O   . SER   B 60  ? 0.2006 0.1907 0.1530 0.0078  -0.0150 0.0218  66  SER   C O   
1569 C CB  . SER   B 60  ? 0.2157 0.2147 0.1923 0.0057  -0.0151 0.0251  66  SER   C CB  
1570 O OG  . SER   B 60  ? 0.3296 0.3313 0.3105 0.0068  -0.0125 0.0279  66  SER   C OG  
1571 N N   . SER   B 61  ? 0.1673 0.1614 0.1290 0.0099  -0.0082 0.0250  67  SER   C N   
1572 C CA  . SER   B 61  ? 0.1794 0.1711 0.1323 0.0117  -0.0062 0.0264  67  SER   C CA  
1573 C C   . SER   B 61  ? 0.2010 0.1881 0.1458 0.0127  -0.0044 0.0233  67  SER   C C   
1574 O O   . SER   B 61  ? 0.2339 0.2180 0.1694 0.0142  -0.0028 0.0239  67  SER   C O   
1575 C CB  . SER   B 61  ? 0.1915 0.1856 0.1497 0.0133  -0.0018 0.0295  67  SER   C CB  
1576 O OG  . SER   B 61  ? 0.1886 0.1833 0.1527 0.0139  0.0018  0.0280  67  SER   C OG  
1577 N N   . ARG   B 62  ? 0.1817 0.1677 0.1287 0.0119  -0.0046 0.0200  68  ARG   C N   
1578 C CA  . ARG   B 62  ? 0.1970 0.1782 0.1366 0.0126  -0.0032 0.0169  68  ARG   C CA  
1579 C C   . ARG   B 62  ? 0.2019 0.1807 0.1392 0.0107  -0.0075 0.0138  68  ARG   C C   
1580 O O   . ARG   B 62  ? 0.2180 0.1925 0.1502 0.0110  -0.0067 0.0108  68  ARG   C O   
1581 C CB  . ARG   B 62  ? 0.1925 0.1742 0.1378 0.0139  0.0010  0.0161  68  ARG   C CB  
1582 C CG  . ARG   B 62  ? 0.2364 0.2203 0.1855 0.0157  0.0055  0.0188  68  ARG   C CG  
1583 C CD  . ARG   B 62  ? 0.2431 0.2231 0.1827 0.0177  0.0088  0.0192  68  ARG   C CD  
1584 N NE  . ARG   B 62  ? 0.2730 0.2547 0.2167 0.0196  0.0138  0.0222  68  ARG   C NE  
1585 C CZ  . ARG   B 62  ? 0.2969 0.2804 0.2409 0.0201  0.0147  0.0258  68  ARG   C CZ  
1586 N NH1 . ARG   B 62  ? 0.3258 0.3094 0.2649 0.0190  0.0105  0.0270  68  ARG   C NH1 
1587 N NH2 . ARG   B 62  ? 0.3178 0.3024 0.2661 0.0218  0.0199  0.0284  68  ARG   C NH2 
1588 N N   . ARG   B 63  ? 0.2051 0.1867 0.1481 0.0086  -0.0114 0.0145  69  ARG   C N   
1589 C CA  . ARG   B 63  ? 0.2241 0.2040 0.1680 0.0066  -0.0150 0.0119  69  ARG   C CA  
1590 C C   . ARG   B 63  ? 0.2291 0.2069 0.1750 0.0069  -0.0126 0.0095  69  ARG   C C   
1591 O O   . ARG   B 63  ? 0.2525 0.2261 0.1943 0.0063  -0.0136 0.0066  69  ARG   C O   
1592 C CB  . ARG   B 63  ? 0.2407 0.2168 0.1751 0.0057  -0.0188 0.0100  69  ARG   C CB  
1593 C CG  . ARG   B 63  ? 0.2627 0.2410 0.1951 0.0054  -0.0224 0.0126  69  ARG   C CG  
1594 C CD  . ARG   B 63  ? 0.3324 0.3148 0.2744 0.0033  -0.0260 0.0140  69  ARG   C CD  
1595 N NE  . ARG   B 63  ? 0.3731 0.3566 0.3121 0.0026  -0.0310 0.0156  69  ARG   C NE  
1596 C CZ  . ARG   B 63  ? 0.3792 0.3662 0.3201 0.0035  -0.0311 0.0196  69  ARG   C CZ  
1597 N NH1 . ARG   B 63  ? 0.3622 0.3519 0.3084 0.0049  -0.0263 0.0221  69  ARG   C NH1 
1598 N NH2 . ARG   B 63  ? 0.3828 0.3709 0.3211 0.0029  -0.0362 0.0211  69  ARG   C NH2 
1599 N N   . LYS   B 64  ? 0.1935 0.1740 0.1459 0.0081  -0.0093 0.0107  70  LYS   C N   
1600 C CA  . LYS   B 64  ? 0.2002 0.1788 0.1542 0.0089  -0.0070 0.0089  70  LYS   C CA  
1601 C C   . LYS   B 64  ? 0.1809 0.1630 0.1434 0.0090  -0.0063 0.0100  70  LYS   C C   
1602 O O   . LYS   B 64  ? 0.1773 0.1632 0.1444 0.0092  -0.0058 0.0121  70  LYS   C O   
1603 C CB  . LYS   B 64  ? 0.2520 0.2290 0.2021 0.0112  -0.0030 0.0086  70  LYS   C CB  
1604 C CG  . LYS   B 64  ? 0.3842 0.3555 0.3245 0.0116  -0.0028 0.0061  70  LYS   C CG  
1605 C CD  . LYS   B 64  ? 0.5008 0.4697 0.4390 0.0140  0.0020  0.0054  70  LYS   C CD  
1606 C CE  . LYS   B 64  ? 0.5804 0.5433 0.5080 0.0146  0.0026  0.0028  70  LYS   C CE  
1607 N NZ  . LYS   B 64  ? 0.6337 0.5957 0.5533 0.0140  0.0004  0.0034  70  LYS   C NZ  
1608 N N   . HIS   B 65  ? 0.1658 0.1462 0.1300 0.0090  -0.0060 0.0087  71  HIS   C N   
1609 C CA  . HIS   B 65  ? 0.1641 0.1469 0.1346 0.0097  -0.0050 0.0094  71  HIS   C CA  
1610 C C   . HIS   B 65  ? 0.1784 0.1607 0.1490 0.0118  -0.0024 0.0088  71  HIS   C C   
1611 O O   . HIS   B 65  ? 0.2183 0.1969 0.1852 0.0126  -0.0013 0.0073  71  HIS   C O   
1612 C CB  . HIS   B 65  ? 0.1726 0.1537 0.1448 0.0086  -0.0062 0.0088  71  HIS   C CB  
1613 C CG  . HIS   B 65  ? 0.1547 0.1369 0.1291 0.0065  -0.0087 0.0096  71  HIS   C CG  
1614 N ND1 . HIS   B 65  ? 0.1865 0.1715 0.1664 0.0060  -0.0088 0.0112  71  HIS   C ND1 
1615 C CD2 . HIS   B 65  ? 0.1597 0.1402 0.1317 0.0048  -0.0111 0.0089  71  HIS   C CD2 
1616 C CE1 . HIS   B 65  ? 0.1594 0.1447 0.1411 0.0040  -0.0111 0.0118  71  HIS   C CE1 
1617 N NE2 . HIS   B 65  ? 0.1993 0.1821 0.1766 0.0032  -0.0128 0.0104  71  HIS   C NE2 
1618 N N   . TYR   B 66  ? 0.1531 0.1389 0.1285 0.0129  -0.0012 0.0099  72  TYR   C N   
1619 C CA  . TYR   B 66  ? 0.1468 0.1328 0.1240 0.0150  0.0011  0.0095  72  TYR   C CA  
1620 C C   . TYR   B 66  ? 0.1405 0.1283 0.1225 0.0158  0.0004  0.0094  72  TYR   C C   
1621 O O   . TYR   B 66  ? 0.1357 0.1261 0.1211 0.0152  -0.0009 0.0101  72  TYR   C O   
1622 C CB  . TYR   B 66  ? 0.1614 0.1505 0.1417 0.0157  0.0028  0.0108  72  TYR   C CB  
1623 C CG  . TYR   B 66  ? 0.1659 0.1532 0.1407 0.0157  0.0043  0.0113  72  TYR   C CG  
1624 C CD1 . TYR   B 66  ? 0.1978 0.1820 0.1686 0.0172  0.0069  0.0104  72  TYR   C CD1 
1625 C CD2 . TYR   B 66  ? 0.1797 0.1683 0.1534 0.0146  0.0034  0.0129  72  TYR   C CD2 
1626 C CE1 . TYR   B 66  ? 0.2139 0.1958 0.1782 0.0175  0.0086  0.0108  72  TYR   C CE1 
1627 C CE2 . TYR   B 66  ? 0.1957 0.1824 0.1632 0.0150  0.0046  0.0136  72  TYR   C CE2 
1628 C CZ  . TYR   B 66  ? 0.2095 0.1927 0.1718 0.0165  0.0073  0.0125  72  TYR   C CZ  
1629 O OH  . TYR   B 66  ? 0.2387 0.2195 0.1934 0.0171  0.0088  0.0133  72  TYR   C OH  
1630 N N   . PRO   B 67  ? 0.1435 0.1294 0.1254 0.0174  0.0011  0.0087  73  PRO   C N   
1631 C CA  . PRO   B 67  ? 0.1411 0.1289 0.1270 0.0186  0.0001  0.0088  73  PRO   C CA  
1632 C C   . PRO   B 67  ? 0.1470 0.1388 0.1389 0.0196  0.0006  0.0090  73  PRO   C C   
1633 O O   . PRO   B 67  ? 0.1765 0.1685 0.1698 0.0205  0.0027  0.0091  73  PRO   C O   
1634 C CB  . PRO   B 67  ? 0.1773 0.1618 0.1616 0.0202  0.0009  0.0082  73  PRO   C CB  
1635 C CG  . PRO   B 67  ? 0.2058 0.1876 0.1868 0.0202  0.0031  0.0075  73  PRO   C CG  
1636 C CD  . PRO   B 67  ? 0.1680 0.1500 0.1460 0.0183  0.0029  0.0076  73  PRO   C CD  
1637 N N   . VAL   B 68  ? 0.1294 0.1239 0.1249 0.0195  -0.0012 0.0090  74  VAL   C N   
1638 C CA  . VAL   B 68  ? 0.1368 0.1352 0.1391 0.0201  -0.0013 0.0089  74  VAL   C CA  
1639 C C   . VAL   B 68  ? 0.1272 0.1272 0.1321 0.0211  -0.0039 0.0081  74  VAL   C C   
1640 O O   . VAL   B 68  ? 0.1314 0.1300 0.1326 0.0209  -0.0055 0.0079  74  VAL   C O   
1641 C CB  . VAL   B 68  ? 0.1577 0.1582 0.1622 0.0185  -0.0008 0.0096  74  VAL   C CB  
1642 C CG1 . VAL   B 68  ? 0.1851 0.1845 0.1872 0.0180  0.0018  0.0107  74  VAL   C CG1 
1643 C CG2 . VAL   B 68  ? 0.1769 0.1769 0.1787 0.0170  -0.0024 0.0096  74  VAL   C CG2 
1644 N N   . SER   B 69  ? 0.1286 0.1317 0.1405 0.0221  -0.0044 0.0076  75  SER   C N   
1645 C CA  . SER   B 69  ? 0.1280 0.1336 0.1439 0.0226  -0.0075 0.0064  75  SER   C CA  
1646 C C   . SER   B 69  ? 0.1151 0.1231 0.1353 0.0210  -0.0074 0.0059  75  SER   C C   
1647 O O   . SER   B 69  ? 0.1241 0.1332 0.1479 0.0202  -0.0048 0.0068  75  SER   C O   
1648 C CB  . SER   B 69  ? 0.1486 0.1567 0.1716 0.0244  -0.0084 0.0060  75  SER   C CB  
1649 O OG  . SER   B 69  ? 0.2211 0.2269 0.2406 0.0261  -0.0085 0.0066  75  SER   C OG  
1650 N N   . PHE   B 70  ? 0.1170 0.1254 0.1364 0.0206  -0.0098 0.0046  76  PHE   C N   
1651 C CA  . PHE   B 70  ? 0.1210 0.1311 0.1446 0.0191  -0.0095 0.0040  76  PHE   C CA  
1652 C C   . PHE   B 70  ? 0.1201 0.1318 0.1471 0.0194  -0.0128 0.0014  76  PHE   C C   
1653 O O   . PHE   B 70  ? 0.1266 0.1372 0.1493 0.0208  -0.0156 0.0003  76  PHE   C O   
1654 C CB  . PHE   B 70  ? 0.1226 0.1307 0.1411 0.0176  -0.0080 0.0050  76  PHE   C CB  
1655 C CG  . PHE   B 70  ? 0.1174 0.1227 0.1284 0.0180  -0.0091 0.0047  76  PHE   C CG  
1656 C CD1 . PHE   B 70  ? 0.1295 0.1320 0.1346 0.0184  -0.0084 0.0060  76  PHE   C CD1 
1657 C CD2 . PHE   B 70  ? 0.1333 0.1382 0.1432 0.0179  -0.0105 0.0032  76  PHE   C CD2 
1658 C CE1 . PHE   B 70  ? 0.1281 0.1279 0.1272 0.0188  -0.0089 0.0061  76  PHE   C CE1 
1659 C CE2 . PHE   B 70  ? 0.1346 0.1365 0.1373 0.0184  -0.0107 0.0034  76  PHE   C CE2 
1660 C CZ  . PHE   B 70  ? 0.1381 0.1375 0.1358 0.0189  -0.0099 0.0050  76  PHE   C CZ  
1661 N N   . SER   B 71  ? 0.1138 0.1277 0.1482 0.0184  -0.0126 0.0005  77  SER   C N   
1662 C CA  . SER   B 71  ? 0.1290 0.1444 0.1678 0.0185  -0.0160 -0.0025 77  SER   C CA  
1663 C C   . SER   B 71  ? 0.1411 0.1542 0.1735 0.0182  -0.0174 -0.0043 77  SER   C C   
1664 O O   . SER   B 71  ? 0.1552 0.1658 0.1810 0.0178  -0.0154 -0.0028 77  SER   C O   
1665 C CB  . SER   B 71  ? 0.1242 0.1428 0.1749 0.0174  -0.0150 -0.0030 77  SER   C CB  
1666 O OG  . SER   B 71  ? 0.1502 0.1683 0.2020 0.0158  -0.0119 -0.0018 77  SER   C OG  
1667 N N   . LYS   B 72  ? 0.1546 0.1683 0.1889 0.0185  -0.0209 -0.0075 78  LYS   C N   
1668 C CA  . LYS   B 72  ? 0.1529 0.1636 0.1803 0.0185  -0.0219 -0.0096 78  LYS   C CA  
1669 C C   . LYS   B 72  ? 0.1529 0.1638 0.1854 0.0166  -0.0192 -0.0099 78  LYS   C C   
1670 O O   . LYS   B 72  ? 0.1700 0.1836 0.2125 0.0155  -0.0184 -0.0100 78  LYS   C O   
1671 C CB  . LYS   B 72  ? 0.2037 0.2149 0.2312 0.0196  -0.0272 -0.0134 78  LYS   C CB  
1672 C CG  . LYS   B 72  ? 0.2434 0.2543 0.2657 0.0219  -0.0301 -0.0127 78  LYS   C CG  
1673 C CD  . LYS   B 72  ? 0.3916 0.4017 0.4095 0.0234  -0.0358 -0.0163 78  LYS   C CD  
1674 C CE  . LYS   B 72  ? 0.5067 0.5151 0.5157 0.0260  -0.0376 -0.0145 78  LYS   C CE  
1675 N NZ  . LYS   B 72  ? 0.5646 0.5700 0.5632 0.0278  -0.0416 -0.0169 78  LYS   C NZ  
1676 N N   . PRO   B 73  ? 0.1466 0.1545 0.1728 0.0163  -0.0175 -0.0100 79  PRO   C N   
1677 C CA  . PRO   B 73  ? 0.1543 0.1622 0.1859 0.0146  -0.0146 -0.0099 79  PRO   C CA  
1678 C C   . PRO   B 73  ? 0.1550 0.1643 0.1950 0.0139  -0.0164 -0.0134 79  PRO   C C   
1679 O O   . PRO   B 73  ? 0.1829 0.1910 0.2200 0.0147  -0.0200 -0.0173 79  PRO   C O   
1680 C CB  . PRO   B 73  ? 0.1808 0.1850 0.2041 0.0149  -0.0130 -0.0100 79  PRO   C CB  
1681 C CG  . PRO   B 73  ? 0.2099 0.2123 0.2237 0.0165  -0.0138 -0.0087 79  PRO   C CG  
1682 C CD  . PRO   B 73  ? 0.1629 0.1672 0.1776 0.0176  -0.0176 -0.0097 79  PRO   C CD  
1683 N N   . SER   B 74  ? 0.1409 0.1526 0.1913 0.0125  -0.0143 -0.0122 80  SER   C N   
1684 C CA  . SER   B 74  ? 0.1564 0.1697 0.2171 0.0116  -0.0158 -0.0154 80  SER   C CA  
1685 C C   . SER   B 74  ? 0.1458 0.1599 0.2156 0.0101  -0.0119 -0.0136 80  SER   C C   
1686 O O   . SER   B 74  ? 0.1419 0.1558 0.2098 0.0099  -0.0084 -0.0096 80  SER   C O   
1687 C CB  . SER   B 74  ? 0.1978 0.2145 0.2655 0.0120  -0.0181 -0.0155 80  SER   C CB  
1688 O OG  . SER   B 74  ? 0.2864 0.3027 0.3462 0.0136  -0.0215 -0.0161 80  SER   C OG  
1689 N N   . LEU   B 75  ? 0.1520 0.1671 0.2320 0.0091  -0.0127 -0.0164 81  LEU   C N   
1690 C CA  . LEU   B 75  ? 0.1606 0.1765 0.2511 0.0077  -0.0089 -0.0147 81  LEU   C CA  
1691 C C   . LEU   B 75  ? 0.1604 0.1799 0.2602 0.0076  -0.0074 -0.0116 81  LEU   C C   
1692 O O   . LEU   B 75  ? 0.1883 0.2099 0.2953 0.0075  -0.0101 -0.0139 81  LEU   C O   
1693 C CB  . LEU   B 75  ? 0.1870 0.2017 0.2845 0.0067  -0.0105 -0.0197 81  LEU   C CB  
1694 C CG  . LEU   B 75  ? 0.2113 0.2260 0.3199 0.0054  -0.0065 -0.0184 81  LEU   C CG  
1695 C CD1 . LEU   B 75  ? 0.2081 0.2205 0.3113 0.0055  -0.0028 -0.0156 81  LEU   C CD1 
1696 C CD2 . LEU   B 75  ? 0.2376 0.2511 0.3542 0.0043  -0.0089 -0.0244 81  LEU   C CD2 
1697 N N   . ILE   B 76  ? 0.1677 0.1878 0.2665 0.0077  -0.0034 -0.0064 82  ILE   C N   
1698 C CA  . ILE   B 76  ? 0.1752 0.1978 0.2795 0.0081  -0.0011 -0.0029 82  ILE   C CA  
1699 C C   . ILE   B 76  ? 0.1688 0.1918 0.2812 0.0074  0.0036  0.0008  82  ILE   C C   
1700 O O   . ILE   B 76  ? 0.1606 0.1821 0.2693 0.0072  0.0055  0.0029  82  ILE   C O   
1701 C CB  . ILE   B 76  ? 0.2061 0.2282 0.2992 0.0093  -0.0007 0.0001  82  ILE   C CB  
1702 C CG1 . ILE   B 76  ? 0.2458 0.2672 0.3306 0.0102  -0.0050 -0.0029 82  ILE   C CG1 
1703 C CG2 . ILE   B 76  ? 0.2235 0.2473 0.3200 0.0099  0.0026  0.0042  82  ILE   C CG2 
1704 C CD1 . ILE   B 76  ? 0.2673 0.2909 0.3562 0.0111  -0.0072 -0.0039 82  ILE   C CD1 
1705 N N   . PHE   B 77  ? 0.1646 0.1898 0.2883 0.0072  0.0056  0.0021  83  PHE   C N   
1706 C CA  . PHE   B 77  ? 0.1706 0.1961 0.3017 0.0069  0.0106  0.0064  83  PHE   C CA  
1707 C C   . PHE   B 77  ? 0.1798 0.2051 0.3020 0.0082  0.0135  0.0117  83  PHE   C C   
1708 O O   . PHE   B 77  ? 0.2149 0.2411 0.3343 0.0092  0.0135  0.0124  83  PHE   C O   
1709 C CB  . PHE   B 77  ? 0.1723 0.2000 0.3192 0.0064  0.0124  0.0063  83  PHE   C CB  
1710 C CG  . PHE   B 77  ? 0.1796 0.2070 0.3347 0.0061  0.0177  0.0105  83  PHE   C CG  
1711 C CD1 . PHE   B 77  ? 0.1969 0.2228 0.3567 0.0050  0.0181  0.0093  83  PHE   C CD1 
1712 C CD2 . PHE   B 77  ? 0.2070 0.2350 0.3638 0.0072  0.0227  0.0162  83  PHE   C CD2 
1713 C CE1 . PHE   B 77  ? 0.2128 0.2382 0.3800 0.0050  0.0231  0.0138  83  PHE   C CE1 
1714 C CE2 . PHE   B 77  ? 0.2092 0.2366 0.3727 0.0073  0.0277  0.0207  83  PHE   C CE2 
1715 C CZ  . PHE   B 77  ? 0.2123 0.2386 0.3813 0.0061  0.0278  0.0196  83  PHE   C CZ  
1716 N N   . VAL   B 78  ? 0.1463 0.1703 0.2645 0.0083  0.0159  0.0153  84  VAL   C N   
1717 C CA  . VAL   B 78  ? 0.1523 0.1757 0.2611 0.0094  0.0179  0.0199  84  VAL   C CA  
1718 C C   . VAL   B 78  ? 0.1413 0.1649 0.2565 0.0098  0.0228  0.0250  84  VAL   C C   
1719 O O   . VAL   B 78  ? 0.1470 0.1703 0.2690 0.0092  0.0242  0.0259  84  VAL   C O   
1720 C CB  . VAL   B 78  ? 0.1565 0.1782 0.2550 0.0092  0.0158  0.0200  84  VAL   C CB  
1721 C CG1 . VAL   B 78  ? 0.1679 0.1889 0.2567 0.0101  0.0169  0.0242  84  VAL   C CG1 
1722 C CG2 . VAL   B 78  ? 0.1639 0.1849 0.2566 0.0089  0.0116  0.0152  84  VAL   C CG2 
1723 N N   . GLU   B 79  ? 0.1315 0.1551 0.2437 0.0111  0.0258  0.0287  85  GLU   C N   
1724 C CA  . GLU   B 79  ? 0.1440 0.1673 0.2600 0.0120  0.0308  0.0342  85  GLU   C CA  
1725 C C   . GLU   B 79  ? 0.1398 0.1619 0.2486 0.0122  0.0308  0.0377  85  GLU   C C   
1726 O O   . GLU   B 79  ? 0.1379 0.1594 0.2375 0.0119  0.0271  0.0362  85  GLU   C O   
1727 C CB  . GLU   B 79  ? 0.1760 0.1989 0.2881 0.0137  0.0342  0.0372  85  GLU   C CB  
1728 C CG  . GLU   B 79  ? 0.2254 0.2500 0.3482 0.0137  0.0354  0.0349  85  GLU   C CG  
1729 C CD  . GLU   B 79  ? 0.3088 0.3349 0.4486 0.0127  0.0379  0.0351  85  GLU   C CD  
1730 O OE1 . GLU   B 79  ? 0.3685 0.3938 0.5120 0.0131  0.0419  0.0395  85  GLU   C OE1 
1731 O OE2 . GLU   B 79  ? 0.3369 0.3647 0.4866 0.0116  0.0356  0.0307  85  GLU   C OE2 
1732 N N   . ALA   B 80  ? 0.1503 0.1721 0.2641 0.0129  0.0348  0.0426  86  ALA   C N   
1733 C CA  . ALA   B 80  ? 0.1690 0.1900 0.2773 0.0134  0.0346  0.0465  86  ALA   C CA  
1734 C C   . ALA   B 80  ? 0.1828 0.2028 0.2757 0.0143  0.0325  0.0480  86  ALA   C C   
1735 O O   . ALA   B 80  ? 0.2072 0.2264 0.2941 0.0154  0.0338  0.0486  86  ALA   C O   
1736 C CB  . ALA   B 80  ? 0.1908 0.2114 0.3059 0.0145  0.0398  0.0524  86  ALA   C CB  
1737 N N   . SER   B 81  ? 0.1688 0.1885 0.2561 0.0138  0.0293  0.0483  87  SER   C N   
1738 C CA  . SER   B 81  ? 0.1838 0.2025 0.2575 0.0145  0.0269  0.0497  87  SER   C CA  
1739 C C   . SER   B 81  ? 0.1930 0.2117 0.2651 0.0152  0.0269  0.0550  87  SER   C C   
1740 O O   . SER   B 81  ? 0.1871 0.2065 0.2689 0.0153  0.0293  0.0576  87  SER   C O   
1741 C CB  . SER   B 81  ? 0.1688 0.1876 0.2374 0.0132  0.0222  0.0450  87  SER   C CB  
1742 O OG  . SER   B 81  ? 0.1722 0.1917 0.2460 0.0122  0.0207  0.0445  87  SER   C OG  
1743 N N   . GLU   B 82  ? 0.2123 0.2304 0.2730 0.0156  0.0238  0.0562  88  GLU   C N   
1744 C CA  . GLU   B 82  ? 0.2264 0.2447 0.2858 0.0163  0.0228  0.0612  88  GLU   C CA  
1745 C C   . GLU   B 82  ? 0.2185 0.2385 0.2865 0.0150  0.0210  0.0604  88  GLU   C C   
1746 O O   . GLU   B 82  ? 0.2443 0.2650 0.3158 0.0157  0.0212  0.0648  88  GLU   C O   
1747 C CB  . GLU   B 82  ? 0.2931 0.3103 0.3385 0.0171  0.0195  0.0627  88  GLU   C CB  
1748 C CG  . GLU   B 82  ? 0.4032 0.4205 0.4430 0.0156  0.0143  0.0589  88  GLU   C CG  
1749 C CD  . GLU   B 82  ? 0.4849 0.5010 0.5121 0.0163  0.0109  0.0609  88  GLU   C CD  
1750 O OE1 . GLU   B 82  ? 0.4928 0.5070 0.5119 0.0180  0.0128  0.0630  88  GLU   C OE1 
1751 O OE2 . GLU   B 82  ? 0.5106 0.5277 0.5362 0.0152  0.0063  0.0603  88  GLU   C OE2 
1752 N N   . TYR   B 83  ? 0.1762 0.1966 0.2479 0.0134  0.0196  0.0550  89  TYR   C N   
1753 C CA  . TYR   B 83  ? 0.1730 0.1942 0.2511 0.0124  0.0182  0.0539  89  TYR   C CA  
1754 C C   . TYR   B 83  ? 0.1837 0.2049 0.2729 0.0115  0.0205  0.0504  89  TYR   C C   
1755 O O   . TYR   B 83  ? 0.1956 0.2171 0.2906 0.0108  0.0203  0.0497  89  TYR   C O   
1756 C CB  . TYR   B 83  ? 0.1721 0.1933 0.2428 0.0114  0.0139  0.0511  89  TYR   C CB  
1757 C CG  . TYR   B 83  ? 0.1664 0.1865 0.2302 0.0109  0.0128  0.0464  89  TYR   C CG  
1758 C CD1 . TYR   B 83  ? 0.1804 0.1995 0.2343 0.0115  0.0118  0.0470  89  TYR   C CD1 
1759 C CD2 . TYR   B 83  ? 0.1627 0.1824 0.2300 0.0100  0.0128  0.0415  89  TYR   C CD2 
1760 C CE1 . TYR   B 83  ? 0.1760 0.1940 0.2245 0.0113  0.0111  0.0430  89  TYR   C CE1 
1761 C CE2 . TYR   B 83  ? 0.1669 0.1857 0.2285 0.0098  0.0117  0.0377  89  TYR   C CE2 
1762 C CZ  . TYR   B 83  ? 0.1634 0.1814 0.2162 0.0104  0.0110  0.0386  89  TYR   C CZ  
1763 O OH  . TYR   B 83  ? 0.1771 0.1941 0.2250 0.0104  0.0103  0.0351  89  TYR   C OH  
1764 N N   . TYR   B 84  ? 0.1579 0.1787 0.2506 0.0114  0.0227  0.0479  90  TYR   C N   
1765 C CA  . TYR   B 84  ? 0.1514 0.1720 0.2552 0.0105  0.0245  0.0445  90  TYR   C CA  
1766 C C   . TYR   B 84  ? 0.1437 0.1645 0.2542 0.0110  0.0282  0.0459  90  TYR   C C   
1767 O O   . TYR   B 84  ? 0.1480 0.1688 0.2530 0.0119  0.0289  0.0472  90  TYR   C O   
1768 C CB  . TYR   B 84  ? 0.1431 0.1632 0.2445 0.0094  0.0219  0.0379  90  TYR   C CB  
1769 C CG  . TYR   B 84  ? 0.1241 0.1437 0.2213 0.0087  0.0193  0.0358  90  TYR   C CG  
1770 C CD1 . TYR   B 84  ? 0.1364 0.1556 0.2401 0.0084  0.0203  0.0361  90  TYR   C CD1 
1771 C CD2 . TYR   B 84  ? 0.1281 0.1474 0.2155 0.0086  0.0163  0.0337  90  TYR   C CD2 
1772 C CE1 . TYR   B 84  ? 0.1359 0.1544 0.2365 0.0080  0.0186  0.0343  90  TYR   C CE1 
1773 C CE2 . TYR   B 84  ? 0.1260 0.1445 0.2103 0.0081  0.0145  0.0319  90  TYR   C CE2 
1774 C CZ  . TYR   B 84  ? 0.1294 0.1476 0.2202 0.0078  0.0157  0.0322  90  TYR   C CZ  
1775 O OH  . TYR   B 84  ? 0.1232 0.1406 0.2116 0.0074  0.0147  0.0309  90  TYR   C OH  
1776 N N   . PRO   B 85  ? 0.1431 0.1637 0.2661 0.0105  0.0308  0.0450  91  PRO   C N   
1777 C CA  . PRO   B 85  ? 0.1411 0.1619 0.2724 0.0107  0.0341  0.0453  91  PRO   C CA  
1778 C C   . PRO   B 85  ? 0.1415 0.1627 0.2719 0.0098  0.0319  0.0394  91  PRO   C C   
1779 O O   . PRO   B 85  ? 0.1419 0.1629 0.2656 0.0091  0.0279  0.0351  91  PRO   C O   
1780 C CB  . PRO   B 85  ? 0.1509 0.1712 0.2962 0.0099  0.0366  0.0451  91  PRO   C CB  
1781 C CG  . PRO   B 85  ? 0.1590 0.1786 0.3024 0.0089  0.0334  0.0407  91  PRO   C CG  
1782 C CD  . PRO   B 85  ? 0.1539 0.1739 0.2842 0.0095  0.0306  0.0427  91  PRO   C CD  
1783 N N   . ALA   B 86  ? 0.1333 0.1551 0.2713 0.0099  0.0345  0.0394  92  ALA   C N   
1784 C CA  . ALA   B 86  ? 0.1577 0.1803 0.2980 0.0091  0.0322  0.0339  92  ALA   C CA  
1785 C C   . ALA   B 86  ? 0.1616 0.1838 0.3080 0.0075  0.0295  0.0281  92  ALA   C C   
1786 O O   . ALA   B 86  ? 0.1808 0.2023 0.3370 0.0068  0.0315  0.0285  92  ALA   C O   
1787 C CB  . ALA   B 86  ? 0.1568 0.1804 0.3078 0.0094  0.0361  0.0355  92  ALA   C CB  
1788 N N   . ARG   B 87  ? 0.1503 0.1724 0.2898 0.0070  0.0250  0.0230  93  ARG   C N   
1789 C CA  . ARG   B 87  ? 0.1481 0.1691 0.2903 0.0058  0.0223  0.0175  93  ARG   C CA  
1790 C C   . ARG   B 87  ? 0.1480 0.1690 0.2826 0.0056  0.0176  0.0123  93  ARG   C C   
1791 O O   . ARG   B 87  ? 0.1435 0.1653 0.2700 0.0065  0.0166  0.0135  93  ARG   C O   
1792 C CB  . ARG   B 87  ? 0.1648 0.1842 0.3024 0.0058  0.0225  0.0188  93  ARG   C CB  
1793 C CG  . ARG   B 87  ? 0.1475 0.1666 0.2707 0.0065  0.0203  0.0200  93  ARG   C CG  
1794 C CD  . ARG   B 87  ? 0.1589 0.1769 0.2793 0.0066  0.0207  0.0216  93  ARG   C CD  
1795 N NE  . ARG   B 87  ? 0.1552 0.1728 0.2634 0.0069  0.0179  0.0212  93  ARG   C NE  
1796 C CZ  . ARG   B 87  ? 0.1611 0.1774 0.2653 0.0067  0.0169  0.0197  93  ARG   C CZ  
1797 N NH1 . ARG   B 87  ? 0.1639 0.1788 0.2746 0.0063  0.0185  0.0187  93  ARG   C NH1 
1798 N NH2 . ARG   B 87  ? 0.1746 0.1906 0.2686 0.0070  0.0146  0.0193  93  ARG   C NH2 
1799 N N   . TYR   B 88  ? 0.1573 0.1770 0.2936 0.0048  0.0148  0.0066  94  TYR   C N   
1800 C CA  . TYR   B 88  ? 0.1777 0.1969 0.3049 0.0050  0.0103  0.0022  94  TYR   C CA  
1801 C C   . TYR   B 88  ? 0.1564 0.1737 0.2715 0.0055  0.0098  0.0031  94  TYR   C C   
1802 O O   . TYR   B 88  ? 0.1765 0.1922 0.2928 0.0052  0.0115  0.0036  94  TYR   C O   
1803 C CB  . TYR   B 88  ? 0.2085 0.2265 0.3406 0.0040  0.0072  -0.0045 94  TYR   C CB  
1804 C CG  . TYR   B 88  ? 0.2403 0.2606 0.3840 0.0034  0.0062  -0.0063 94  TYR   C CG  
1805 C CD1 . TYR   B 88  ? 0.2606 0.2828 0.4017 0.0040  0.0029  -0.0078 94  TYR   C CD1 
1806 C CD2 . TYR   B 88  ? 0.2607 0.2813 0.4189 0.0023  0.0089  -0.0060 94  TYR   C CD2 
1807 C CE1 . TYR   B 88  ? 0.2769 0.3016 0.4304 0.0035  0.0021  -0.0091 94  TYR   C CE1 
1808 C CE2 . TYR   B 88  ? 0.2808 0.3037 0.4513 0.0017  0.0083  -0.0074 94  TYR   C CE2 
1809 C CZ  . TYR   B 88  ? 0.2942 0.3193 0.4626 0.0022  0.0049  -0.0089 94  TYR   C CZ  
1810 O OH  . TYR   B 88  ? 0.3408 0.3684 0.5237 0.0015  0.0046  -0.0100 94  TYR   C OH  
1811 N N   . GLN   B 89  ? 0.1451 0.1625 0.2496 0.0063  0.0077  0.0033  95  GLN   C N   
1812 C CA  . GLN   B 89  ? 0.1386 0.1543 0.2322 0.0067  0.0069  0.0037  95  GLN   C CA  
1813 C C   . GLN   B 89  ? 0.1360 0.1504 0.2229 0.0071  0.0032  -0.0012 95  GLN   C C   
1814 O O   . GLN   B 89  ? 0.1439 0.1594 0.2305 0.0075  0.0008  -0.0028 95  GLN   C O   
1815 C CB  . GLN   B 89  ? 0.1541 0.1707 0.2414 0.0074  0.0078  0.0084  95  GLN   C CB  
1816 C CG  . GLN   B 89  ? 0.1643 0.1793 0.2420 0.0076  0.0071  0.0091  95  GLN   C CG  
1817 C CD  . GLN   B 89  ? 0.1389 0.1547 0.2122 0.0078  0.0081  0.0140  95  GLN   C CD  
1818 O OE1 . GLN   B 89  ? 0.1488 0.1657 0.2265 0.0079  0.0102  0.0177  95  GLN   C OE1 
1819 N NE2 . GLN   B 89  ? 0.1466 0.1613 0.2110 0.0081  0.0065  0.0138  95  GLN   C NE2 
1820 N N   . SER   B 90  ? 0.1245 0.1362 0.2059 0.0072  0.0028  -0.0033 96  SER   C N   
1821 C CA  . SER   B 90  ? 0.1358 0.1455 0.2094 0.0079  -0.0004 -0.0076 96  SER   C CA  
1822 C C   . SER   B 90  ? 0.1305 0.1394 0.1927 0.0089  -0.0011 -0.0058 96  SER   C C   
1823 O O   . SER   B 90  ? 0.1267 0.1360 0.1870 0.0088  0.0010  -0.0017 96  SER   C O   
1824 C CB  . SER   B 90  ? 0.1533 0.1599 0.2270 0.0077  -0.0001 -0.0115 96  SER   C CB  
1825 O OG  . SER   B 90  ? 0.1603 0.1653 0.2308 0.0078  0.0030  -0.0089 96  SER   C OG  
1826 N N   . HIS   B 91  ? 0.1335 0.1411 0.1884 0.0098  -0.0042 -0.0088 97  HIS   C N   
1827 C CA  . HIS   B 91  ? 0.1316 0.1377 0.1759 0.0109  -0.0048 -0.0075 97  HIS   C CA  
1828 C C   . HIS   B 91  ? 0.1270 0.1354 0.1712 0.0108  -0.0041 -0.0033 97  HIS   C C   
1829 O O   . HIS   B 91  ? 0.1394 0.1467 0.1776 0.0110  -0.0030 -0.0009 97  HIS   C O   
1830 C CB  . HIS   B 91  ? 0.1478 0.1509 0.1866 0.0111  -0.0025 -0.0070 97  HIS   C CB  
1831 C CG  . HIS   B 91  ? 0.1617 0.1617 0.1985 0.0115  -0.0028 -0.0113 97  HIS   C CG  
1832 N ND1 . HIS   B 91  ? 0.1987 0.1957 0.2255 0.0130  -0.0046 -0.0139 97  HIS   C ND1 
1833 C CD2 . HIS   B 91  ? 0.1651 0.1644 0.2086 0.0108  -0.0015 -0.0136 97  HIS   C CD2 
1834 C CE1 . HIS   B 91  ? 0.1995 0.1937 0.2259 0.0131  -0.0043 -0.0177 97  HIS   C CE1 
1835 N NE2 . HIS   B 91  ? 0.1955 0.1908 0.2320 0.0118  -0.0025 -0.0179 97  HIS   C NE2 
1836 N N   . LEU   B 92  ? 0.1159 0.1269 0.1665 0.0106  -0.0046 -0.0028 98  LEU   C N   
1837 C CA  . LEU   B 92  ? 0.1173 0.1300 0.1677 0.0107  -0.0035 0.0007  98  LEU   C CA  
1838 C C   . LEU   B 92  ? 0.1185 0.1318 0.1661 0.0117  -0.0059 -0.0003 98  LEU   C C   
1839 O O   . LEU   B 92  ? 0.1237 0.1377 0.1745 0.0121  -0.0084 -0.0034 98  LEU   C O   
1840 C CB  . LEU   B 92  ? 0.1288 0.1438 0.1890 0.0099  -0.0011 0.0028  98  LEU   C CB  
1841 C CG  . LEU   B 92  ? 0.1367 0.1527 0.1958 0.0101  0.0008  0.0068  98  LEU   C CG  
1842 C CD1 . LEU   B 92  ? 0.1512 0.1661 0.2046 0.0098  0.0020  0.0097  98  LEU   C CD1 
1843 C CD2 . LEU   B 92  ? 0.1667 0.1847 0.2354 0.0098  0.0034  0.0088  98  LEU   C CD2 
1844 N N   . MET   B 93  ? 0.1164 0.1293 0.1584 0.0122  -0.0053 0.0021  99  MET   C N   
1845 C CA  . MET   B 93  ? 0.1036 0.1168 0.1430 0.0135  -0.0070 0.0017  99  MET   C CA  
1846 C C   . MET   B 93  ? 0.1155 0.1298 0.1570 0.0135  -0.0046 0.0046  99  MET   C C   
1847 O O   . MET   B 93  ? 0.1283 0.1418 0.1669 0.0128  -0.0026 0.0071  99  MET   C O   
1848 C CB  . MET   B 93  ? 0.1316 0.1420 0.1609 0.0142  -0.0079 0.0019  99  MET   C CB  
1849 C CG  . MET   B 93  ? 0.1493 0.1578 0.1747 0.0146  -0.0095 -0.0006 99  MET   C CG  
1850 S SD  . MET   B 93  ? 0.1649 0.1698 0.1794 0.0154  -0.0093 0.0004  99  MET   C SD  
1851 C CE  . MET   B 93  ? 0.1768 0.1813 0.1917 0.0138  -0.0060 0.0037  99  MET   C CE  
1852 N N   . LEU   B 94  ? 0.1103 0.1262 0.1560 0.0143  -0.0049 0.0043  100 LEU   C N   
1853 C CA  . LEU   B 94  ? 0.1190 0.1355 0.1661 0.0146  -0.0019 0.0070  100 LEU   C CA  
1854 C C   . LEU   B 94  ? 0.1101 0.1254 0.1517 0.0159  -0.0024 0.0072  100 LEU   C C   
1855 O O   . LEU   B 94  ? 0.1319 0.1471 0.1727 0.0169  -0.0051 0.0053  100 LEU   C O   
1856 C CB  . LEU   B 94  ? 0.1223 0.1416 0.1808 0.0147  -0.0006 0.0070  100 LEU   C CB  
1857 C CG  . LEU   B 94  ? 0.1361 0.1567 0.2026 0.0135  0.0005  0.0070  100 LEU   C CG  
1858 C CD1 . LEU   B 94  ? 0.1774 0.2007 0.2557 0.0136  0.0023  0.0074  100 LEU   C CD1 
1859 C CD2 . LEU   B 94  ? 0.1591 0.1785 0.2220 0.0127  0.0033  0.0101  100 LEU   C CD2 
1860 N N   . ALA   B 95  ? 0.1195 0.1335 0.1575 0.0161  0.0003  0.0095  101 ALA   C N   
1861 C CA  . ALA   B 95  ? 0.1186 0.1311 0.1524 0.0174  0.0010  0.0098  101 ALA   C CA  
1862 C C   . ALA   B 95  ? 0.1233 0.1360 0.1592 0.0179  0.0050  0.0120  101 ALA   C C   
1863 O O   . ALA   B 95  ? 0.1150 0.1281 0.1525 0.0171  0.0070  0.0137  101 ALA   C O   
1864 C CB  . ALA   B 95  ? 0.1346 0.1438 0.1582 0.0172  0.0002  0.0100  101 ALA   C CB  
1865 N N   . VAL   B 96  ? 0.1237 0.1354 0.1588 0.0193  0.0064  0.0121  102 VAL   C N   
1866 C CA  . VAL   B 96  ? 0.1427 0.1534 0.1773 0.0201  0.0108  0.0142  102 VAL   C CA  
1867 C C   . VAL   B 96  ? 0.1429 0.1498 0.1659 0.0198  0.0114  0.0149  102 VAL   C C   
1868 O O   . VAL   B 96  ? 0.1644 0.1688 0.1811 0.0200  0.0098  0.0137  102 VAL   C O   
1869 C CB  . VAL   B 96  ? 0.1527 0.1638 0.1920 0.0220  0.0124  0.0138  102 VAL   C CB  
1870 C CG1 . VAL   B 96  ? 0.1746 0.1839 0.2120 0.0232  0.0177  0.0159  102 VAL   C CG1 
1871 C CG2 . VAL   B 96  ? 0.1626 0.1780 0.2146 0.0222  0.0110  0.0129  102 VAL   C CG2 
1872 N N   . GLY   B 97  ? 0.1544 0.1608 0.1747 0.0191  0.0132  0.0169  103 GLY   C N   
1873 C CA  . GLY   B 97  ? 0.1704 0.1735 0.1801 0.0186  0.0128  0.0174  103 GLY   C CA  
1874 C C   . GLY   B 97  ? 0.1619 0.1651 0.1698 0.0180  0.0140  0.0199  103 GLY   C C   
1875 O O   . GLY   B 97  ? 0.1909 0.1968 0.2063 0.0179  0.0154  0.0214  103 GLY   C O   
1876 N N   . HIS   B 98  ? 0.1697 0.1700 0.1679 0.0177  0.0134  0.0204  104 HIS   C N   
1877 C CA  . HIS   B 98  ? 0.1732 0.1733 0.1682 0.0174  0.0140  0.0231  104 HIS   C CA  
1878 C C   . HIS   B 98  ? 0.1648 0.1668 0.1618 0.0156  0.0107  0.0237  104 HIS   C C   
1879 O O   . HIS   B 98  ? 0.1609 0.1624 0.1560 0.0144  0.0074  0.0219  104 HIS   C O   
1880 C CB  . HIS   B 98  ? 0.2193 0.2152 0.2025 0.0179  0.0144  0.0231  104 HIS   C CB  
1881 C CG  . HIS   B 98  ? 0.2473 0.2428 0.2261 0.0182  0.0152  0.0262  104 HIS   C CG  
1882 N ND1 . HIS   B 98  ? 0.2705 0.2669 0.2527 0.0196  0.0196  0.0292  104 HIS   C ND1 
1883 C CD2 . HIS   B 98  ? 0.2756 0.2704 0.2483 0.0171  0.0119  0.0270  104 HIS   C CD2 
1884 C CE1 . HIS   B 98  ? 0.3033 0.2992 0.2803 0.0196  0.0188  0.0319  104 HIS   C CE1 
1885 N NE2 . HIS   B 98  ? 0.3158 0.3108 0.2870 0.0181  0.0139  0.0306  104 HIS   C NE2 
1886 N N   . SER   B 99  ? 0.1629 0.1669 0.1640 0.0155  0.0118  0.0265  105 SER   C N   
1887 C CA  . SER   B 99  ? 0.1707 0.1765 0.1744 0.0141  0.0091  0.0275  105 SER   C CA  
1888 C C   . SER   B 99  ? 0.1816 0.1881 0.1861 0.0145  0.0109  0.0315  105 SER   C C   
1889 O O   . SER   B 99  ? 0.2134 0.2214 0.2247 0.0154  0.0144  0.0330  105 SER   C O   
1890 C CB  . SER   B 99  ? 0.1867 0.1950 0.2000 0.0134  0.0087  0.0258  105 SER   C CB  
1891 O OG  . SER   B 99  ? 0.1885 0.1984 0.2054 0.0122  0.0071  0.0269  105 SER   C OG  
1892 N N   . GLU   B 100 ? 0.1912 0.1968 0.1893 0.0142  0.0087  0.0332  106 GLU   C N   
1893 C CA  . GLU   B 100 ? 0.2037 0.2099 0.2012 0.0148  0.0094  0.0375  106 GLU   C CA  
1894 C C   . GLU   B 100 ? 0.1746 0.1835 0.1793 0.0133  0.0069  0.0382  106 GLU   C C   
1895 O O   . GLU   B 100 ? 0.1614 0.1708 0.1680 0.0119  0.0043  0.0355  106 GLU   C O   
1896 C CB  . GLU   B 100 ? 0.2400 0.2435 0.2251 0.0151  0.0070  0.0385  106 GLU   C CB  
1897 C CG  . GLU   B 100 ? 0.3348 0.3344 0.3094 0.0163  0.0082  0.0370  106 GLU   C CG  
1898 C CD  . GLU   B 100 ? 0.3906 0.3885 0.3612 0.0186  0.0130  0.0399  106 GLU   C CD  
1899 O OE1 . GLU   B 100 ? 0.3916 0.3861 0.3542 0.0198  0.0150  0.0385  106 GLU   C OE1 
1900 O OE2 . GLU   B 100 ? 0.3957 0.3956 0.3719 0.0192  0.0153  0.0437  106 GLU   C OE2 
1901 N N   . PRO   B 101 ? 0.1791 0.1894 0.1877 0.0137  0.0078  0.0421  107 PRO   C N   
1902 C CA  . PRO   B 101 ? 0.1728 0.1856 0.1888 0.0125  0.0058  0.0429  107 PRO   C CA  
1903 C C   . PRO   B 101 ? 0.1724 0.1849 0.1841 0.0112  0.0011  0.0416  107 PRO   C C   
1904 O O   . PRO   B 101 ? 0.1716 0.1854 0.1892 0.0099  -0.0001 0.0400  107 PRO   C O   
1905 C CB  . PRO   B 101 ? 0.1974 0.2111 0.2156 0.0136  0.0073  0.0481  107 PRO   C CB  
1906 C CG  . PRO   B 101 ? 0.2460 0.2581 0.2610 0.0154  0.0115  0.0497  107 PRO   C CG  
1907 C CD  . PRO   B 101 ? 0.2129 0.2228 0.2206 0.0155  0.0116  0.0461  107 PRO   C CD  
1908 N N   . GLY   B 102 ? 0.1675 0.1780 0.1691 0.0114  -0.0014 0.0420  108 GLY   C N   
1909 C CA  . GLY   B 102 ? 0.1690 0.1795 0.1680 0.0099  -0.0062 0.0407  108 GLY   C CA  
1910 C C   . GLY   B 102 ? 0.1545 0.1638 0.1536 0.0087  -0.0069 0.0363  108 GLY   C C   
1911 O O   . GLY   B 102 ? 0.1743 0.1836 0.1732 0.0073  -0.0102 0.0351  108 GLY   C O   
1912 N N   . ASP   B 103 ? 0.1453 0.1537 0.1445 0.0094  -0.0038 0.0340  109 ASP   C N   
1913 C CA  . ASP   B 103 ? 0.1364 0.1436 0.1355 0.0087  -0.0044 0.0302  109 ASP   C CA  
1914 C C   . ASP   B 103 ? 0.1365 0.1456 0.1441 0.0079  -0.0041 0.0293  109 ASP   C C   
1915 O O   . ASP   B 103 ? 0.1343 0.1424 0.1417 0.0073  -0.0047 0.0267  109 ASP   C O   
1916 C CB  . ASP   B 103 ? 0.1603 0.1658 0.1567 0.0099  -0.0015 0.0283  109 ASP   C CB  
1917 C CG  . ASP   B 103 ? 0.1746 0.1772 0.1612 0.0107  -0.0016 0.0282  109 ASP   C CG  
1918 O OD1 . ASP   B 103 ? 0.1866 0.1876 0.1676 0.0098  -0.0048 0.0276  109 ASP   C OD1 
1919 O OD2 . ASP   B 103 ? 0.1898 0.1915 0.1746 0.0122  0.0017  0.0288  109 ASP   C OD2 
1920 N N   . CYS   B 104 ? 0.1277 0.1391 0.1426 0.0080  -0.0027 0.0314  110 CYS   C N   
1921 C CA  . CYS   B 104 ? 0.1254 0.1380 0.1477 0.0074  -0.0021 0.0304  110 CYS   C CA  
1922 C C   . CYS   B 104 ? 0.1259 0.1381 0.1478 0.0062  -0.0045 0.0297  110 CYS   C C   
1923 O O   . CYS   B 104 ? 0.1390 0.1515 0.1594 0.0056  -0.0069 0.0317  110 CYS   C O   
1924 C CB  . CYS   B 104 ? 0.1326 0.1473 0.1627 0.0076  -0.0004 0.0330  110 CYS   C CB  
1925 S SG  . CYS   B 104 ? 0.1455 0.1608 0.1798 0.0088  0.0032  0.0331  110 CYS   C SG  
1926 N N   . GLY   B 105 ? 0.1055 0.1169 0.1290 0.0059  -0.0038 0.0273  111 GLY   C N   
1927 C CA  . GLY   B 105 ? 0.1253 0.1360 0.1492 0.0050  -0.0051 0.0268  111 GLY   C CA  
1928 C C   . GLY   B 105 ? 0.1232 0.1314 0.1407 0.0048  -0.0062 0.0246  111 GLY   C C   
1929 O O   . GLY   B 105 ? 0.1330 0.1401 0.1512 0.0041  -0.0066 0.0240  111 GLY   C O   
1930 N N   . GLY   B 106 ? 0.1290 0.1360 0.1408 0.0054  -0.0064 0.0237  112 GLY   C N   
1931 C CA  . GLY   B 106 ? 0.1373 0.1415 0.1433 0.0054  -0.0072 0.0215  112 GLY   C CA  
1932 C C   . GLY   B 106 ? 0.1190 0.1223 0.1261 0.0061  -0.0057 0.0196  112 GLY   C C   
1933 O O   . GLY   B 106 ? 0.1256 0.1299 0.1353 0.0069  -0.0042 0.0189  112 GLY   C O   
1934 N N   . ILE   B 107 ? 0.1166 0.1177 0.1213 0.0057  -0.0063 0.0186  113 ILE   C N   
1935 C CA  . ILE   B 107 ? 0.1178 0.1175 0.1224 0.0065  -0.0049 0.0172  113 ILE   C CA  
1936 C C   . ILE   B 107 ? 0.1200 0.1185 0.1206 0.0080  -0.0046 0.0155  113 ILE   C C   
1937 O O   . ILE   B 107 ? 0.1235 0.1205 0.1204 0.0081  -0.0052 0.0150  113 ILE   C O   
1938 C CB  . ILE   B 107 ? 0.1499 0.1476 0.1544 0.0057  -0.0051 0.0175  113 ILE   C CB  
1939 C CG1 . ILE   B 107 ? 0.1970 0.1963 0.2077 0.0049  -0.0042 0.0192  113 ILE   C CG1 
1940 C CG2 . ILE   B 107 ? 0.1532 0.1482 0.1545 0.0070  -0.0038 0.0163  113 ILE   C CG2 
1941 C CD1 . ILE   B 107 ? 0.2492 0.2472 0.2625 0.0038  -0.0040 0.0202  113 ILE   C CD1 
1942 N N   . LEU   B 108 ? 0.1125 0.1113 0.1140 0.0092  -0.0038 0.0143  114 LEU   C N   
1943 C CA  . LEU   B 108 ? 0.1181 0.1157 0.1167 0.0107  -0.0039 0.0128  114 LEU   C CA  
1944 C C   . LEU   B 108 ? 0.1177 0.1129 0.1137 0.0113  -0.0035 0.0125  114 LEU   C C   
1945 O O   . LEU   B 108 ? 0.1182 0.1133 0.1154 0.0113  -0.0028 0.0126  114 LEU   C O   
1946 C CB  . LEU   B 108 ? 0.1103 0.1102 0.1122 0.0117  -0.0038 0.0117  114 LEU   C CB  
1947 C CG  . LEU   B 108 ? 0.1199 0.1193 0.1202 0.0134  -0.0045 0.0101  114 LEU   C CG  
1948 C CD1 . LEU   B 108 ? 0.1387 0.1375 0.1373 0.0141  -0.0045 0.0101  114 LEU   C CD1 
1949 C CD2 . LEU   B 108 ? 0.1288 0.1305 0.1336 0.0139  -0.0050 0.0087  114 LEU   C CD2 
1950 N N   . ARG   B 109 ? 0.1224 0.1151 0.1146 0.0120  -0.0037 0.0123  115 ARG   C N   
1951 C CA  . ARG   B 109 ? 0.1282 0.1180 0.1175 0.0128  -0.0030 0.0126  115 ARG   C CA  
1952 C C   . ARG   B 109 ? 0.1335 0.1218 0.1193 0.0149  -0.0035 0.0118  115 ARG   C C   
1953 O O   . ARG   B 109 ? 0.1434 0.1320 0.1290 0.0153  -0.0041 0.0113  115 ARG   C O   
1954 C CB  . ARG   B 109 ? 0.1672 0.1549 0.1566 0.0113  -0.0025 0.0138  115 ARG   C CB  
1955 C CG  . ARG   B 109 ? 0.2186 0.2049 0.2062 0.0110  -0.0033 0.0132  115 ARG   C CG  
1956 C CD  . ARG   B 109 ? 0.2783 0.2623 0.2666 0.0092  -0.0033 0.0139  115 ARG   C CD  
1957 N NE  . ARG   B 109 ? 0.3683 0.3544 0.3600 0.0072  -0.0045 0.0145  115 ARG   C NE  
1958 C CZ  . ARG   B 109 ? 0.4898 0.4766 0.4858 0.0059  -0.0042 0.0158  115 ARG   C CZ  
1959 N NH1 . ARG   B 109 ? 0.5201 0.5054 0.5170 0.0066  -0.0020 0.0167  115 ARG   C NH1 
1960 N NH2 . ARG   B 109 ? 0.5161 0.5051 0.5154 0.0043  -0.0057 0.0165  115 ARG   C NH2 
1961 N N   . CYS   B 110 ? 0.1404 0.1269 0.1233 0.0163  -0.0030 0.0120  116 CYS   C N   
1962 C CA  . CYS   B 110 ? 0.1445 0.1292 0.1237 0.0186  -0.0037 0.0119  116 CYS   C CA  
1963 C C   . CYS   B 110 ? 0.1712 0.1519 0.1470 0.0191  -0.0019 0.0136  116 CYS   C C   
1964 O O   . CYS   B 110 ? 0.1690 0.1487 0.1464 0.0175  -0.0002 0.0147  116 CYS   C O   
1965 C CB  . CYS   B 110 ? 0.1424 0.1286 0.1204 0.0203  -0.0052 0.0106  116 CYS   C CB  
1966 S SG  . CYS   B 110 ? 0.1481 0.1326 0.1227 0.0208  -0.0038 0.0108  116 CYS   C SG  
1967 N N   . GLN   B 111 ? 0.1865 0.1650 0.1583 0.0215  -0.0021 0.0142  117 GLN   C N   
1968 C CA  . GLN   B 111 ? 0.2031 0.1774 0.1718 0.0222  0.0001  0.0163  117 GLN   C CA  
1969 C C   . GLN   B 111 ? 0.2014 0.1746 0.1685 0.0222  0.0022  0.0172  117 GLN   C C   
1970 O O   . GLN   B 111 ? 0.2235 0.1935 0.1901 0.0221  0.0050  0.0193  117 GLN   C O   
1971 C CB  . GLN   B 111 ? 0.2248 0.1968 0.1890 0.0253  -0.0005 0.0172  117 GLN   C CB  
1972 C CG  . GLN   B 111 ? 0.2588 0.2318 0.2186 0.0276  -0.0024 0.0165  117 GLN   C CG  
1973 C CD  . GLN   B 111 ? 0.3993 0.3704 0.3547 0.0308  -0.0038 0.0177  117 GLN   C CD  
1974 O OE1 . GLN   B 111 ? 0.4369 0.4105 0.3943 0.0318  -0.0066 0.0166  117 GLN   C OE1 
1975 N NE2 . GLN   B 111 ? 0.4128 0.3798 0.3628 0.0326  -0.0017 0.0202  117 GLN   C NE2 
1976 N N   . HIS   B 112 ? 0.1756 0.1510 0.1423 0.0223  0.0014  0.0158  118 HIS   C N   
1977 C CA  . HIS   B 112 ? 0.1793 0.1531 0.1439 0.0226  0.0039  0.0165  118 HIS   C CA  
1978 C C   . HIS   B 112 ? 0.1846 0.1599 0.1554 0.0199  0.0056  0.0167  118 HIS   C C   
1979 O O   . HIS   B 112 ? 0.1996 0.1734 0.1701 0.0201  0.0084  0.0176  118 HIS   C O   
1980 C CB  . HIS   B 112 ? 0.1984 0.1728 0.1587 0.0244  0.0022  0.0145  118 HIS   C CB  
1981 C CG  . HIS   B 112 ? 0.1835 0.1568 0.1380 0.0272  -0.0002 0.0143  118 HIS   C CG  
1982 N ND1 . HIS   B 112 ? 0.1687 0.1452 0.1251 0.0275  -0.0041 0.0123  118 HIS   C ND1 
1983 C CD2 . HIS   B 112 ? 0.2250 0.1944 0.1720 0.0299  0.0007  0.0160  118 HIS   C CD2 
1984 C CE1 . HIS   B 112 ? 0.2054 0.1802 0.1564 0.0303  -0.0058 0.0129  118 HIS   C CE1 
1985 N NE2 . HIS   B 112 ? 0.2358 0.2062 0.1804 0.0318  -0.0031 0.0151  118 HIS   C NE2 
1986 N N   . GLY   B 113 ? 0.1633 0.1417 0.1397 0.0178  0.0039  0.0160  119 GLY   C N   
1987 C CA  . GLY   B 113 ? 0.1602 0.1405 0.1428 0.0154  0.0048  0.0165  119 GLY   C CA  
1988 C C   . GLY   B 113 ? 0.1446 0.1289 0.1308 0.0142  0.0025  0.0150  119 GLY   C C   
1989 O O   . GLY   B 113 ? 0.1393 0.1249 0.1246 0.0147  0.0004  0.0138  119 GLY   C O   
1990 N N   . VAL   B 114 ? 0.1406 0.1268 0.1317 0.0128  0.0034  0.0154  120 VAL   C N   
1991 C CA  . VAL   B 114 ? 0.1411 0.1309 0.1363 0.0117  0.0017  0.0146  120 VAL   C CA  
1992 C C   . VAL   B 114 ? 0.1336 0.1244 0.1277 0.0130  0.0012  0.0126  120 VAL   C C   
1993 O O   . VAL   B 114 ? 0.1401 0.1296 0.1327 0.0139  0.0028  0.0120  120 VAL   C O   
1994 C CB  . VAL   B 114 ? 0.1500 0.1414 0.1515 0.0100  0.0028  0.0162  120 VAL   C CB  
1995 C CG1 . VAL   B 114 ? 0.1605 0.1553 0.1660 0.0092  0.0015  0.0158  120 VAL   C CG1 
1996 C CG2 . VAL   B 114 ? 0.1662 0.1570 0.1699 0.0084  0.0024  0.0178  120 VAL   C CG2 
1997 N N   . VAL   B 115 ? 0.1190 0.1119 0.1138 0.0132  -0.0008 0.0114  121 VAL   C N   
1998 C CA  . VAL   B 115 ? 0.1211 0.1153 0.1164 0.0141  -0.0019 0.0092  121 VAL   C CA  
1999 C C   . VAL   B 115 ? 0.1251 0.1219 0.1266 0.0129  -0.0014 0.0091  121 VAL   C C   
2000 O O   . VAL   B 115 ? 0.1327 0.1297 0.1355 0.0134  -0.0013 0.0073  121 VAL   C O   
2001 C CB  . VAL   B 115 ? 0.1166 0.1119 0.1112 0.0150  -0.0040 0.0083  121 VAL   C CB  
2002 C CG1 . VAL   B 115 ? 0.1454 0.1427 0.1426 0.0156  -0.0055 0.0061  121 VAL   C CG1 
2003 C CG2 . VAL   B 115 ? 0.1487 0.1413 0.1375 0.0165  -0.0044 0.0086  121 VAL   C CG2 
2004 N N   . GLY   B 116 ? 0.1188 0.1175 0.1241 0.0115  -0.0013 0.0108  122 GLY   C N   
2005 C CA  . GLY   B 116 ? 0.1332 0.1342 0.1446 0.0105  -0.0008 0.0114  122 GLY   C CA  
2006 C C   . GLY   B 116 ? 0.1168 0.1194 0.1301 0.0093  -0.0012 0.0137  122 GLY   C C   
2007 O O   . GLY   B 116 ? 0.1224 0.1237 0.1323 0.0090  -0.0018 0.0145  122 GLY   C O   
2008 N N   . ILE   B 117 ? 0.1116 0.1165 0.1301 0.0087  -0.0007 0.0148  123 ILE   C N   
2009 C CA  . ILE   B 117 ? 0.1103 0.1165 0.1297 0.0078  -0.0013 0.0172  123 ILE   C CA  
2010 C C   . ILE   B 117 ? 0.1061 0.1142 0.1281 0.0082  -0.0009 0.0175  123 ILE   C C   
2011 O O   . ILE   B 117 ? 0.1199 0.1289 0.1461 0.0086  0.0000  0.0164  123 ILE   C O   
2012 C CB  . ILE   B 117 ? 0.1158 0.1231 0.1397 0.0068  -0.0009 0.0195  123 ILE   C CB  
2013 C CG1 . ILE   B 117 ? 0.1357 0.1440 0.1658 0.0070  0.0009  0.0193  123 ILE   C CG1 
2014 C CG2 . ILE   B 117 ? 0.1428 0.1484 0.1650 0.0062  -0.0012 0.0199  123 ILE   C CG2 
2015 C CD1 . ILE   B 117 ? 0.1391 0.1488 0.1753 0.0061  0.0016  0.0222  123 ILE   C CD1 
2016 N N   . VAL   B 118 ? 0.1072 0.1154 0.1264 0.0081  -0.0014 0.0190  124 VAL   C N   
2017 C CA  . VAL   B 118 ? 0.1108 0.1204 0.1321 0.0086  -0.0004 0.0201  124 VAL   C CA  
2018 C C   . VAL   B 118 ? 0.1079 0.1194 0.1362 0.0083  0.0009  0.0218  124 VAL   C C   
2019 O O   . VAL   B 118 ? 0.1058 0.1178 0.1356 0.0076  0.0004  0.0238  124 VAL   C O   
2020 C CB  . VAL   B 118 ? 0.1080 0.1168 0.1238 0.0087  -0.0009 0.0217  124 VAL   C CB  
2021 C CG1 . VAL   B 118 ? 0.1272 0.1371 0.1448 0.0095  0.0011  0.0235  124 VAL   C CG1 
2022 C CG2 . VAL   B 118 ? 0.1263 0.1327 0.1358 0.0091  -0.0016 0.0198  124 VAL   C CG2 
2023 N N   . SER   B 119 ? 0.1029 0.1156 0.1364 0.0088  0.0025  0.0213  125 SER   C N   
2024 C CA  . SER   B 119 ? 0.1015 0.1157 0.1426 0.0086  0.0041  0.0229  125 SER   C CA  
2025 C C   . SER   B 119 ? 0.1167 0.1320 0.1614 0.0092  0.0061  0.0246  125 SER   C C   
2026 O O   . SER   B 119 ? 0.1169 0.1333 0.1668 0.0092  0.0077  0.0274  125 SER   C O   
2027 C CB  . SER   B 119 ? 0.1178 0.1318 0.1634 0.0084  0.0043  0.0200  125 SER   C CB  
2028 O OG  . SER   B 119 ? 0.1315 0.1466 0.1853 0.0081  0.0061  0.0209  125 SER   C OG  
2029 N N   . THR   B 120 ? 0.1166 0.1318 0.1601 0.0100  0.0066  0.0232  126 THR   C N   
2030 C CA  . THR   B 120 ? 0.1190 0.1352 0.1674 0.0107  0.0093  0.0250  126 THR   C CA  
2031 C C   . THR   B 120 ? 0.1124 0.1276 0.1544 0.0117  0.0100  0.0257  126 THR   C C   
2032 O O   . THR   B 120 ? 0.1152 0.1289 0.1502 0.0118  0.0082  0.0239  126 THR   C O   
2033 C CB  . THR   B 120 ? 0.1172 0.1346 0.1748 0.0106  0.0100  0.0223  126 THR   C CB  
2034 O OG1 . THR   B 120 ? 0.1285 0.1457 0.1837 0.0110  0.0083  0.0192  126 THR   C OG1 
2035 C CG2 . THR   B 120 ? 0.1318 0.1495 0.1949 0.0097  0.0093  0.0207  126 THR   C CG2 
2036 N N   . GLY   B 121 ? 0.1226 0.1381 0.1669 0.0125  0.0131  0.0283  127 GLY   C N   
2037 C CA  . GLY   B 121 ? 0.1506 0.1648 0.1895 0.0138  0.0148  0.0289  127 GLY   C CA  
2038 C C   . GLY   B 121 ? 0.1790 0.1939 0.2243 0.0148  0.0192  0.0315  127 GLY   C C   
2039 O O   . GLY   B 121 ? 0.2130 0.2288 0.2634 0.0148  0.0210  0.0343  127 GLY   C O   
2040 N N   . GLY   B 122 ? 0.2254 0.2399 0.2708 0.0159  0.0213  0.0309  128 GLY   C N   
2041 C CA  . GLY   B 122 ? 0.2493 0.2643 0.3016 0.0171  0.0262  0.0336  128 GLY   C CA  
2042 C C   . GLY   B 122 ? 0.2443 0.2601 0.3017 0.0178  0.0275  0.0314  128 GLY   C C   
2043 O O   . GLY   B 122 ? 0.2458 0.2627 0.3056 0.0171  0.0241  0.0278  128 GLY   C O   
2044 N N   . ASN   B 123 ? 0.2266 0.2419 0.2865 0.0194  0.0326  0.0341  129 ASN   C N   
2045 C CA  . ASN   B 123 ? 0.2275 0.2437 0.2946 0.0203  0.0347  0.0327  129 ASN   C CA  
2046 C C   . ASN   B 123 ? 0.2081 0.2230 0.2676 0.0207  0.0319  0.0296  129 ASN   C C   
2047 O O   . ASN   B 123 ? 0.2460 0.2628 0.3128 0.0209  0.0310  0.0273  129 ASN   C O   
2048 C CB  . ASN   B 123 ? 0.2683 0.2884 0.3520 0.0192  0.0337  0.0308  129 ASN   C CB  
2049 C CG  . ASN   B 123 ? 0.3406 0.3620 0.4367 0.0197  0.0391  0.0339  129 ASN   C CG  
2050 O OD1 . ASN   B 123 ? 0.3573 0.3770 0.4511 0.0214  0.0447  0.0376  129 ASN   C OD1 
2051 N ND2 . ASN   B 123 ? 0.3618 0.3860 0.4714 0.0182  0.0379  0.0326  129 ASN   C ND2 
2052 N N   . GLY   B 124 ? 0.1917 0.2036 0.2373 0.0208  0.0303  0.0296  130 GLY   C N   
2053 C CA  . GLY   B 124 ? 0.1867 0.1968 0.2251 0.0211  0.0278  0.0267  130 GLY   C CA  
2054 C C   . GLY   B 124 ? 0.1598 0.1715 0.2002 0.0197  0.0224  0.0233  130 GLY   C C   
2055 O O   . GLY   B 124 ? 0.1680 0.1788 0.2055 0.0202  0.0205  0.0210  130 GLY   C O   
2056 N N   . LEU   B 125 ? 0.1393 0.1529 0.1840 0.0183  0.0201  0.0231  131 LEU   C N   
2057 C CA  . LEU   B 125 ? 0.1351 0.1498 0.1808 0.0171  0.0153  0.0200  131 LEU   C CA  
2058 C C   . LEU   B 125 ? 0.1439 0.1573 0.1825 0.0159  0.0132  0.0205  131 LEU   C C   
2059 O O   . LEU   B 125 ? 0.1806 0.1936 0.2177 0.0156  0.0148  0.0233  131 LEU   C O   
2060 C CB  . LEU   B 125 ? 0.1559 0.1737 0.2139 0.0165  0.0146  0.0187  131 LEU   C CB  
2061 C CG  . LEU   B 125 ? 0.1894 0.2093 0.2571 0.0175  0.0161  0.0181  131 LEU   C CG  
2062 C CD1 . LEU   B 125 ? 0.2331 0.2559 0.3145 0.0167  0.0165  0.0177  131 LEU   C CD1 
2063 C CD2 . LEU   B 125 ? 0.2030 0.2229 0.2690 0.0182  0.0130  0.0154  131 LEU   C CD2 
2064 N N   . VAL   B 126 ? 0.1191 0.1318 0.1537 0.0152  0.0097  0.0182  132 VAL   C N   
2065 C CA  . VAL   B 126 ? 0.1139 0.1257 0.1438 0.0140  0.0075  0.0185  132 VAL   C CA  
2066 C C   . VAL   B 126 ? 0.1060 0.1191 0.1406 0.0133  0.0051  0.0160  132 VAL   C C   
2067 O O   . VAL   B 126 ? 0.1179 0.1313 0.1534 0.0139  0.0035  0.0136  132 VAL   C O   
2068 C CB  . VAL   B 126 ? 0.1194 0.1284 0.1392 0.0139  0.0060  0.0181  132 VAL   C CB  
2069 C CG1 . VAL   B 126 ? 0.1501 0.1579 0.1676 0.0147  0.0049  0.0158  132 VAL   C CG1 
2070 C CG2 . VAL   B 126 ? 0.1356 0.1442 0.1525 0.0126  0.0039  0.0184  132 VAL   C CG2 
2071 N N   . GLY   B 127 ? 0.1043 0.1182 0.1416 0.0123  0.0050  0.0167  133 GLY   C N   
2072 C CA  . GLY   B 127 ? 0.1023 0.1166 0.1429 0.0117  0.0031  0.0142  133 GLY   C CA  
2073 C C   . GLY   B 127 ? 0.1089 0.1217 0.1440 0.0110  0.0018  0.0143  133 GLY   C C   
2074 O O   . GLY   B 127 ? 0.1134 0.1259 0.1466 0.0104  0.0024  0.0169  133 GLY   C O   
2075 N N   . PHE   B 128 ? 0.0992 0.1110 0.1324 0.0111  0.0000  0.0118  134 PHE   C N   
2076 C CA  . PHE   B 128 ? 0.1047 0.1147 0.1331 0.0106  -0.0008 0.0117  134 PHE   C CA  
2077 C C   . PHE   B 128 ? 0.1022 0.1121 0.1340 0.0104  -0.0009 0.0098  134 PHE   C C   
2078 O O   . PHE   B 128 ? 0.1126 0.1226 0.1461 0.0110  -0.0020 0.0070  134 PHE   C O   
2079 C CB  . PHE   B 128 ? 0.1110 0.1190 0.1324 0.0114  -0.0022 0.0105  134 PHE   C CB  
2080 C CG  . PHE   B 128 ? 0.1120 0.1195 0.1300 0.0118  -0.0021 0.0115  134 PHE   C CG  
2081 C CD1 . PHE   B 128 ? 0.1165 0.1229 0.1306 0.0111  -0.0018 0.0134  134 PHE   C CD1 
2082 C CD2 . PHE   B 128 ? 0.1191 0.1272 0.1382 0.0130  -0.0024 0.0104  134 PHE   C CD2 
2083 C CE1 . PHE   B 128 ? 0.1229 0.1282 0.1330 0.0116  -0.0016 0.0138  134 PHE   C CE1 
2084 C CE2 . PHE   B 128 ? 0.1232 0.1304 0.1392 0.0136  -0.0016 0.0112  134 PHE   C CE2 
2085 C CZ  . PHE   B 128 ? 0.1266 0.1321 0.1375 0.0129  -0.0011 0.0128  134 PHE   C CZ  
2086 N N   . ALA   B 129 ? 0.1069 0.1164 0.1396 0.0096  0.0002  0.0112  135 ALA   C N   
2087 C CA  . ALA   B 129 ? 0.1039 0.1125 0.1387 0.0096  0.0007  0.0093  135 ALA   C CA  
2088 C C   . ALA   B 129 ? 0.1175 0.1234 0.1449 0.0103  -0.0001 0.0077  135 ALA   C C   
2089 O O   . ALA   B 129 ? 0.1216 0.1264 0.1452 0.0101  0.0003  0.0095  135 ALA   C O   
2090 C CB  . ALA   B 129 ? 0.1154 0.1244 0.1544 0.0087  0.0026  0.0118  135 ALA   C CB  
2091 N N   . ASP   B 130 ? 0.1136 0.1184 0.1391 0.0112  -0.0013 0.0045  136 ASP   C N   
2092 C CA  . ASP   B 130 ? 0.1232 0.1251 0.1408 0.0123  -0.0019 0.0032  136 ASP   C CA  
2093 C C   . ASP   B 130 ? 0.1294 0.1291 0.1460 0.0122  0.0006  0.0037  136 ASP   C C   
2094 O O   . ASP   B 130 ? 0.1304 0.1304 0.1521 0.0116  0.0021  0.0032  136 ASP   C O   
2095 C CB  . ASP   B 130 ? 0.1397 0.1408 0.1554 0.0135  -0.0042 -0.0005 136 ASP   C CB  
2096 C CG  . ASP   B 130 ? 0.1630 0.1610 0.1695 0.0151  -0.0051 -0.0016 136 ASP   C CG  
2097 O OD1 . ASP   B 130 ? 0.1785 0.1757 0.1806 0.0156  -0.0051 0.0003  136 ASP   C OD1 
2098 O OD2 . ASP   B 130 ? 0.2049 0.2007 0.2082 0.0159  -0.0053 -0.0043 136 ASP   C OD2 
2099 N N   . VAL   B 131 ? 0.1259 0.1232 0.1365 0.0128  0.0013  0.0048  137 VAL   C N   
2100 C CA  . VAL   B 131 ? 0.1283 0.1231 0.1375 0.0130  0.0042  0.0053  137 VAL   C CA  
2101 C C   . VAL   B 131 ? 0.1438 0.1347 0.1440 0.0149  0.0045  0.0037  137 VAL   C C   
2102 O O   . VAL   B 131 ? 0.1481 0.1362 0.1459 0.0155  0.0075  0.0041  137 VAL   C O   
2103 C CB  . VAL   B 131 ? 0.1411 0.1364 0.1532 0.0119  0.0060  0.0089  137 VAL   C CB  
2104 C CG1 . VAL   B 131 ? 0.1438 0.1426 0.1641 0.0103  0.0057  0.0107  137 VAL   C CG1 
2105 C CG2 . VAL   B 131 ? 0.1534 0.1481 0.1611 0.0120  0.0049  0.0103  137 VAL   C CG2 
2106 N N   . ARG   B 132 ? 0.1462 0.1368 0.1413 0.0160  0.0016  0.0021  138 ARG   C N   
2107 C CA  . ARG   B 132 ? 0.1518 0.1386 0.1373 0.0181  0.0016  0.0013  138 ARG   C CA  
2108 C C   . ARG   B 132 ? 0.1556 0.1395 0.1367 0.0194  0.0023  -0.0017 138 ARG   C C   
2109 O O   . ARG   B 132 ? 0.1793 0.1593 0.1517 0.0213  0.0035  -0.0017 138 ARG   C O   
2110 C CB  . ARG   B 132 ? 0.1447 0.1324 0.1270 0.0192  -0.0021 0.0007  138 ARG   C CB  
2111 C CG  . ARG   B 132 ? 0.1437 0.1330 0.1283 0.0183  -0.0022 0.0035  138 ARG   C CG  
2112 C CD  . ARG   B 132 ? 0.1499 0.1399 0.1320 0.0196  -0.0054 0.0028  138 ARG   C CD  
2113 N NE  . ARG   B 132 ? 0.1460 0.1393 0.1339 0.0191  -0.0079 0.0006  138 ARG   C NE  
2114 C CZ  . ARG   B 132 ? 0.1480 0.1431 0.1370 0.0198  -0.0108 -0.0002 138 ARG   C CZ  
2115 N NH1 . ARG   B 132 ? 0.1585 0.1521 0.1423 0.0215  -0.0118 0.0008  138 ARG   C NH1 
2116 N NH2 . ARG   B 132 ? 0.1516 0.1499 0.1477 0.0191  -0.0123 -0.0017 138 ARG   C NH2 
2117 N N   . ASP   B 133 ? 0.1493 0.1346 0.1356 0.0186  0.0016  -0.0043 139 ASP   C N   
2118 C CA  . ASP   B 133 ? 0.1662 0.1481 0.1482 0.0197  0.0023  -0.0078 139 ASP   C CA  
2119 C C   . ASP   B 133 ? 0.1768 0.1563 0.1602 0.0195  0.0076  -0.0066 139 ASP   C C   
2120 O O   . ASP   B 133 ? 0.2024 0.1780 0.1806 0.0207  0.0092  -0.0094 139 ASP   C O   
2121 C CB  . ASP   B 133 ? 0.1902 0.1743 0.1783 0.0188  -0.0006 -0.0115 139 ASP   C CB  
2122 C CG  . ASP   B 133 ? 0.1926 0.1800 0.1925 0.0166  0.0013  -0.0100 139 ASP   C CG  
2123 O OD1 . ASP   B 133 ? 0.1856 0.1755 0.1897 0.0156  0.0021  -0.0062 139 ASP   C OD1 
2124 O OD2 . ASP   B 133 ? 0.2261 0.2130 0.2307 0.0160  0.0019  -0.0127 139 ASP   C OD2 
2125 N N   . LEU   B 134 ? 0.1688 0.1503 0.1590 0.0180  0.0102  -0.0027 140 LEU   C N   
2126 C CA  . LEU   B 134 ? 0.1646 0.1447 0.1587 0.0177  0.0151  -0.0011 140 LEU   C CA  
2127 C C   . LEU   B 134 ? 0.1691 0.1453 0.1561 0.0192  0.0184  0.0009  140 LEU   C C   
2128 O O   . LEU   B 134 ? 0.1703 0.1476 0.1607 0.0184  0.0202  0.0047  140 LEU   C O   
2129 C CB  . LEU   B 134 ? 0.1554 0.1399 0.1607 0.0155  0.0155  0.0023  140 LEU   C CB  
2130 C CG  . LEU   B 134 ? 0.1552 0.1433 0.1678 0.0142  0.0128  0.0010  140 LEU   C CG  
2131 C CD1 . LEU   B 134 ? 0.1740 0.1661 0.1957 0.0124  0.0130  0.0050  140 LEU   C CD1 
2132 C CD2 . LEU   B 134 ? 0.1924 0.1788 0.2073 0.0144  0.0141  -0.0024 140 LEU   C CD2 
2133 N N   . LEU   B 135 ? 0.1819 0.1534 0.1584 0.0215  0.0193  -0.0017 141 LEU   C N   
2134 C CA  . LEU   B 135 ? 0.1988 0.1662 0.1669 0.0234  0.0226  0.0004  141 LEU   C CA  
2135 C C   . LEU   B 135 ? 0.1905 0.1563 0.1633 0.0232  0.0288  0.0035  141 LEU   C C   
2136 O O   . LEU   B 135 ? 0.2071 0.1712 0.1781 0.0238  0.0317  0.0069  141 LEU   C O   
2137 C CB  . LEU   B 135 ? 0.2048 0.1670 0.1592 0.0262  0.0220  -0.0029 141 LEU   C CB  
2138 C CG  . LEU   B 135 ? 0.2082 0.1720 0.1587 0.0266  0.0153  -0.0064 141 LEU   C CG  
2139 C CD1 . LEU   B 135 ? 0.2299 0.1884 0.1658 0.0296  0.0142  -0.0097 141 LEU   C CD1 
2140 C CD2 . LEU   B 135 ? 0.2141 0.1814 0.1663 0.0260  0.0118  -0.0038 141 LEU   C CD2 
2141 N N   . TRP   B 136 ? 0.1882 0.1549 0.1687 0.0222  0.0310  0.0026  142 TRP   C N   
2142 C CA  . TRP   B 136 ? 0.1998 0.1653 0.1866 0.0221  0.0370  0.0054  142 TRP   C CA  
2143 C C   . TRP   B 136 ? 0.2098 0.1796 0.2068 0.0200  0.0368  0.0101  142 TRP   C C   
2144 O O   . TRP   B 136 ? 0.2244 0.1935 0.2269 0.0200  0.0415  0.0132  142 TRP   C O   
2145 C CB  . TRP   B 136 ? 0.2028 0.1683 0.1961 0.0216  0.0390  0.0032  142 TRP   C CB  
2146 C CG  . TRP   B 136 ? 0.1950 0.1657 0.1969 0.0195  0.0344  0.0023  142 TRP   C CG  
2147 C CD1 . TRP   B 136 ? 0.2008 0.1718 0.2005 0.0194  0.0306  -0.0019 142 TRP   C CD1 
2148 C CD2 . TRP   B 136 ? 0.1926 0.1685 0.2073 0.0173  0.0337  0.0057  142 TRP   C CD2 
2149 N NE1 . TRP   B 136 ? 0.2073 0.1834 0.2176 0.0173  0.0279  -0.0009 142 TRP   C NE1 
2150 C CE2 . TRP   B 136 ? 0.2008 0.1798 0.2198 0.0161  0.0298  0.0038  142 TRP   C CE2 
2151 C CE3 . TRP   B 136 ? 0.1896 0.1678 0.2127 0.0162  0.0358  0.0103  142 TRP   C CE3 
2152 C CZ2 . TRP   B 136 ? 0.1904 0.1745 0.2202 0.0142  0.0281  0.0066  142 TRP   C CZ2 
2153 C CZ3 . TRP   B 136 ? 0.1902 0.1735 0.2241 0.0143  0.0336  0.0127  142 TRP   C CZ3 
2154 C CH2 . TRP   B 136 ? 0.1903 0.1763 0.2269 0.0134  0.0300  0.0110  142 TRP   C CH2 
2155 N N   . LEU   B 137 ? 0.1885 0.1626 0.1884 0.0184  0.0315  0.0107  143 LEU   C N   
2156 C CA  . LEU   B 137 ? 0.1861 0.1636 0.1939 0.0165  0.0308  0.0146  143 LEU   C CA  
2157 C C   . LEU   B 137 ? 0.2248 0.1992 0.2284 0.0175  0.0338  0.0171  143 LEU   C C   
2158 O O   . LEU   B 137 ? 0.2436 0.2198 0.2548 0.0161  0.0347  0.0204  143 LEU   C O   
2159 C CB  . LEU   B 137 ? 0.1799 0.1616 0.1891 0.0150  0.0251  0.0144  143 LEU   C CB  
2160 C CG  . LEU   B 137 ? 0.1677 0.1530 0.1835 0.0137  0.0227  0.0133  143 LEU   C CG  
2161 C CD1 . LEU   B 137 ? 0.1857 0.1740 0.2002 0.0128  0.0176  0.0126  143 LEU   C CD1 
2162 C CD2 . LEU   B 137 ? 0.1823 0.1707 0.2096 0.0121  0.0241  0.0164  143 LEU   C CD2 
2163 N N   . ASP   B 138 ? 0.2145 0.1844 0.2063 0.0199  0.0348  0.0156  144 ASP   C N   
2164 C CA  . ASP   B 138 ? 0.2361 0.2026 0.2232 0.0211  0.0377  0.0183  144 ASP   C CA  
2165 C C   . ASP   B 138 ? 0.2707 0.2333 0.2587 0.0224  0.0450  0.0203  144 ASP   C C   
2166 O O   . ASP   B 138 ? 0.2925 0.2518 0.2771 0.0236  0.0483  0.0229  144 ASP   C O   
2167 C CB  . ASP   B 138 ? 0.2428 0.2059 0.2164 0.0234  0.0357  0.0165  144 ASP   C CB  
2168 C CG  . ASP   B 138 ? 0.2521 0.2185 0.2246 0.0225  0.0292  0.0152  144 ASP   C CG  
2169 O OD1 . ASP   B 138 ? 0.2551 0.2259 0.2365 0.0200  0.0266  0.0160  144 ASP   C OD1 
2170 O OD2 . ASP   B 138 ? 0.2907 0.2551 0.2533 0.0244  0.0268  0.0133  144 ASP   C OD2 
2171 N N   . GLU   B 139 ? 0.2778 0.2403 0.2705 0.0224  0.0479  0.0194  145 GLU   C N   
2172 C CA  . GLU   B 139 ? 0.3356 0.2940 0.3290 0.0240  0.0556  0.0212  145 GLU   C CA  
2173 C C   . GLU   B 139 ? 0.3798 0.3410 0.3871 0.0225  0.0583  0.0224  145 GLU   C C   
2174 O O   . GLU   B 139 ? 0.3929 0.3590 0.4081 0.0205  0.0540  0.0216  145 GLU   C O   
2175 C CB  . GLU   B 139 ? 0.4139 0.3663 0.3929 0.0271  0.0578  0.0176  145 GLU   C CB  
2176 C CG  . GLU   B 139 ? 0.5200 0.4738 0.4993 0.0266  0.0548  0.0131  145 GLU   C CG  
2177 C CD  . GLU   B 139 ? 0.6532 0.6022 0.6177 0.0291  0.0536  0.0083  145 GLU   C CD  
2178 O OE1 . GLU   B 139 ? 0.6604 0.6095 0.6259 0.0288  0.0525  0.0045  145 GLU   C OE1 
2179 O OE2 . GLU   B 139 ? 0.7078 0.6530 0.6599 0.0313  0.0535  0.0084  145 GLU   C OE2 
2180 N N   . GLU   B 140 ? 0.4159 0.3734 0.4252 0.0241  0.0659  0.0242  146 GLU   C N   
2181 C CA  . GLU   B 140 ? 0.4477 0.4061 0.4681 0.0237  0.0702  0.0250  146 GLU   C CA  
2182 C C   . GLU   B 140 ? 0.4651 0.4304 0.5022 0.0207  0.0670  0.0277  146 GLU   C C   
2183 O O   . GLU   B 140 ? 0.4743 0.4420 0.5195 0.0200  0.0671  0.0271  146 GLU   C O   
2184 C CB  . GLU   B 140 ? 0.4796 0.4355 0.4936 0.0250  0.0704  0.0203  146 GLU   C CB  
2185 C CG  . GLU   B 140 ? 0.5905 0.5385 0.5899 0.0284  0.0759  0.0180  146 GLU   C CG  
2186 C CD  . GLU   B 140 ? 0.7208 0.6657 0.7129 0.0296  0.0754  0.0125  146 GLU   C CD  
2187 O OE1 . GLU   B 140 ? 0.7398 0.6859 0.7416 0.0289  0.0774  0.0119  146 GLU   C OE1 
2188 O OE2 . GLU   B 140 ? 0.7723 0.7135 0.7494 0.0313  0.0727  0.0088  146 GLU   C OE2 
2189 N N1  . A1B3J C .   ? 0.2441 0.2218 0.2966 0.0215  0.0298  0.0084  201 A1B3J A N1  
2190 C C4  . A1B3J C .   ? 0.4410 0.4056 0.4636 0.0072  0.0549  -0.0213 201 A1B3J A C4  
2191 C C5  . A1B3J C .   ? 0.4846 0.4450 0.5113 0.0064  0.0649  -0.0251 201 A1B3J A C5  
2192 C C6  . A1B3J C .   ? 0.4276 0.3885 0.4553 0.0086  0.0560  -0.0207 201 A1B3J A C6  
2193 C C7  . A1B3J C .   ? 0.4088 0.3730 0.4327 0.0088  0.0478  -0.0180 201 A1B3J A C7  
2194 C C8  . A1B3J C .   ? 0.4077 0.3668 0.4349 0.0088  0.0497  -0.0190 201 A1B3J A C8  
2195 C C10 . A1B3J C .   ? 0.3887 0.3470 0.4131 0.0077  0.0417  -0.0177 201 A1B3J A C10 
2196 C C13 . A1B3J C .   ? 0.2959 0.2674 0.3555 0.0228  0.0381  0.0068  201 A1B3J A C13 
2197 O O2  . A1B3J C .   ? 0.2972 0.2686 0.3706 0.0267  0.0431  0.0125  201 A1B3J A O2  
2198 C C12 . A1B3J C .   ? 0.3338 0.2976 0.3855 0.0191  0.0428  -0.0022 201 A1B3J A C12 
2199 S S   . A1B3J C .   ? 0.3702 0.3289 0.4082 0.0129  0.0397  -0.0099 201 A1B3J A S   
2200 C C11 . A1B3J C .   ? 0.3883 0.3408 0.4172 0.0074  0.0454  -0.0189 201 A1B3J A C11 
2201 C C14 . A1B3J C .   ? 0.3655 0.3348 0.4096 0.0179  0.0385  -0.0029 201 A1B3J A C14 
2202 N N   . A1B3J C .   ? 0.3800 0.3432 0.4159 0.0136  0.0427  -0.0108 201 A1B3J A N   
2203 C C9  . A1B3J C .   ? 0.3787 0.3433 0.4166 0.0145  0.0459  -0.0107 201 A1B3J A C9  
2204 O O1  . A1B3J C .   ? 0.3429 0.3137 0.3902 0.0189  0.0455  -0.0041 201 A1B3J A O1  
2205 C C1  . A1B3J C .   ? 0.3903 0.3612 0.4065 0.0081  0.0387  -0.0155 201 A1B3J A C1  
2206 O O   . A1B3J C .   ? 0.3662 0.3404 0.3825 0.0095  0.0321  -0.0120 201 A1B3J A O   
2207 C C   . A1B3J C .   ? 0.3571 0.3344 0.3636 0.0070  0.0246  -0.0121 201 A1B3J A C   
2208 F F2  . A1B3J C .   ? 0.4984 0.4607 0.5149 0.0024  0.0633  -0.0279 201 A1B3J A F2  
2209 F F1  . A1B3J C .   ? 0.4798 0.4435 0.5228 0.0126  0.0691  -0.0190 201 A1B3J A F1  
2210 F F   . A1B3J C .   ? 0.5150 0.4659 0.5409 0.0029  0.0737  -0.0320 201 A1B3J A F   
2211 C C3  . A1B3J C .   ? 0.4158 0.3867 0.4294 0.0061  0.0453  -0.0189 201 A1B3J A C3  
2212 C C2  . A1B3J C .   ? 0.3947 0.3686 0.4057 0.0067  0.0375  -0.0160 201 A1B3J A C2  
# 
