data_7I56
# 
_entry.id   7I56 
# 
_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   7I56         pdb_00007i56 10.2210/pdb7i56/pdb 
WWPDB D_1001408329 ?            ?                   
# 
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                        7I56 
_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 '(4aR,7aS)-1-{[2-(methylsulfanyl)phenyl]acetyl}octahydro-5H-pyrrolo[3,4-b]pyridin-5-one' 304.407   1 ?         ? 
? ? 
3 non-polymer syn 'ZINC ION'                                                                               65.409    2 ?         ? 
? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                     78.133    3 ?         ? 
? ? 
5 water       nat water                                                                                    18.015    2 ?         ? 
? ? 
# 
_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 '(4aR,7aS)-1-{[2-(methylsulfanyl)phenyl]acetyl}octahydro-5H-pyrrolo[3,4-b]pyridin-5-one' A1B3N 
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 
A1B3N non-polymer         . '(4aR,7aS)-1-{[2-(methylsulfanyl)phenyl]acetyl}octahydro-5H-pyrrolo[3,4-b]pyridin-5-one' ? 
'C16 H20 N2 O2 S' 304.407 
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        A1B3N 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B3N 
_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 A1B3N 1 201 201 A1B3N LIG A . 
D 3 ZN    1 202 1   ZN    ZN  A . 
E 4 DMS   1 201 1   DMS   DMS C . 
F 3 ZN    1 202 1   ZN    ZN  C . 
G 4 DMS   1 203 1   DMS   DMS C . 
H 4 DMS   1 204 6   DMS   DMS C . 
I 5 HOH   1 301 2   HOH   HOH A . 
I 5 HOH   2 302 1   HOH   HOH A . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7I56 
_cell.length_a           86.349 
_cell.length_b           56.829 
_cell.length_c           64.750 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.71 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I56 
_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          7I56 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.49 
_exptl_crystal.density_percent_sol   50.61 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-16 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I56 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.51 
_reflns.d_resolution_high            1.21 
_reflns.number_obs                   81376 
_reflns.percent_possible_obs         85.5 
_reflns.pdbx_Rmerge_I_obs            0.053 
_reflns.pdbx_netI_over_sigmaI        16.1 
_reflns.pdbx_redundancy              5.4 
_reflns.pdbx_Rrim_I_all              0.058 
_reflns.pdbx_Rpim_I_all              0.023 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     441267 
_reflns.pdbx_chi_squared             0.70 
_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                  1.21 
_reflns_shell.d_res_low                   1.23 
_reflns_shell.number_measured_all         2237 
_reflns_shell.number_unique_obs           1436 
_reflns_shell.Rmerge_I_obs                1.015 
_reflns_shell.pdbx_chi_squared            0.14 
_reflns_shell.pdbx_redundancy             1.6 
_reflns_shell.percent_possible_obs        30.6 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.3 
_reflns_shell.pdbx_Rrim_I_all             1.391 
_reflns_shell.pdbx_Rpim_I_all             0.945 
_reflns_shell.pdbx_CC_half                0.320 
_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                                 7I56 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     80900 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.000 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             17.70 
_refine.ls_d_res_high                            1.210 
_refine.ls_percent_reflns_obs                    85.1 
_refine.ls_R_factor_obs                          0.2571 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.2565 
_refine.ls_R_factor_R_free                       0.2701 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.000 
_refine.ls_number_reflns_R_free                  4043 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.920 
_refine.correlation_coeff_Fo_to_Fc_free          0.928 
_refine.B_iso_mean                               21.14 
_refine.aniso_B[1][1]                            -0.43420 
_refine.aniso_B[2][2]                            -1.02670 
_refine.aniso_B[3][3]                            1.46090 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.45330 
_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             0.057 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.057 
_refine.pdbx_overall_SU_R_Blow_DPI               0.055 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.055 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I56 
_refine_analyze.Luzzati_coordinate_error_obs    0.22 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        2166 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             0 
_refine_hist.number_atoms_total               2201 
_refine_hist.d_res_high                       1.210 
_refine_hist.d_res_low                        17.70 
# 
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                  0.012 ? 2.00  2268 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.08  ? 2.00  3089 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  760  '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  403  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2268 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.67  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.69 ? ?     ?    '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  1547 '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                       1.21 
_refine_ls_shell.d_res_low                        1.24 
_refine_ls_shell.number_reflns_R_work             1546 
_refine_ls_shell.R_factor_R_work                  0.3578 
_refine_ls_shell.percent_reflns_obs               26.96 
_refine_ls_shell.R_factor_R_free                  0.3367 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.45 
_refine_ls_shell.number_reflns_R_free             72 
_refine_ls_shell.number_reflns_all                1618 
_refine_ls_shell.R_factor_all                     0.3568 
# 
_struct.entry_id                  7I56 
_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-0036764-001 (A71EV2A-x4791)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I56 
_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 4 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I 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 7I56 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I56 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,I   
2 1 B,E,F,G,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 ? ? ? ? ? ? ? 2.341 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.244 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.238 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.072 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 56  C ZN 202 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 58  C ZN 202 1_555 ? ? ? ? ? ? ? 2.277 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 F ZN . ZN ? ? C CYS 116 C ZN 202 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 F ZN . ZN ? ? C HIS 118 C ZN 202 1_555 ? ? ? ? ? ? ? 2.095 ? ? 
# 
_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_555 109.3 ? 
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_555 105.7 ? 
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_555 118.2 ? 
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_555 102.7 ? 
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_555 102.5 ? 
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_555 117.3 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 110.1 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.5 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.5 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 105.2 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.6 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? F ZN . ? C ZN 202 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 115.2 ? 
# 
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 VAL A 68  ? O VAL A 74  N GLY A 55  ? N GLY A 61  
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 VAL A 126 ? O VAL A 132 N ALA A 95  ? N ALA A 101 
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                   7I56 
_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_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 OH A TYR 94 ? ? 1_555 OE2 C GLU 85 ? ? 3_455 1.42 
2 1 OH A TYR 94 ? ? 1_555 CD  C GLU 85 ? ? 3_455 1.90 
# 
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 SER A 87  ? ? -129.80 -166.73 
2 1 SER A 125 ? ? -131.35 -35.84  
3 1 SER C 125 ? ? -134.17 -30.60  
# 
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 14.9297 8.2022   14.4638 -0.0229 -0.0200 0.0014 0.0061 -0.0063 0.0036 1.4802 1.1089 0.7199 1.1520  
-0.6284 -0.3933 -0.0081 0.0560  0.1289 0.0414 0.0550 0.0510  -0.0270 -0.0687 -0.0469 
'X-RAY DIFFRACTION' 2 ? refined 25.6368 -20.1233 17.6920 -0.0262 -0.0231 0.0130 0.0083 -0.0038 0.0175 0.8294 1.1487 0.2881 -0.4686 
-0.2385 -0.0152 -0.0021 -0.0013 0.1394 0.0399 0.0615 -0.0014 0.0212  0.0109  -0.0594 
# 
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_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 
A1B3N N1   N  N N 1   
A1B3N C4   C  Y N 2   
A1B3N C5   C  Y N 3   
A1B3N C6   C  Y N 4   
A1B3N C7   C  N N 5   
A1B3N C8   C  N N 6   
A1B3N C10  C  N N 7   
A1B3N C13  C  N N 8   
A1B3N C15  C  N S 9   
A1B3N O1   O  N N 10  
A1B3N C14  C  N N 11  
A1B3N C12  C  N R 12  
A1B3N C11  C  N N 13  
A1B3N C9   C  N N 14  
A1B3N N    N  N N 15  
A1B3N O    O  N N 16  
A1B3N C1   C  Y N 17  
A1B3N S    S  N N 18  
A1B3N C    C  N N 19  
A1B3N C3   C  Y N 20  
A1B3N C2   C  Y N 21  
A1B3N H17  H  N N 22  
A1B3N H7   H  N N 23  
A1B3N H8   H  N N 24  
A1B3N H9   H  N N 25  
A1B3N H10  H  N N 26  
A1B3N H14  H  N N 27  
A1B3N H13  H  N N 28  
A1B3N H1   H  N N 29  
A1B3N H19  H  N N 30  
A1B3N H18  H  N N 31  
A1B3N H    H  N N 32  
A1B3N H15  H  N N 33  
A1B3N H16  H  N N 34  
A1B3N H11  H  N N 35  
A1B3N H12  H  N N 36  
A1B3N H3   H  N N 37  
A1B3N H2   H  N N 38  
A1B3N H4   H  N N 39  
A1B3N H6   H  N N 40  
A1B3N H5   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 
A1B3N C   S    sing N N 1   
A1B3N S   C1   sing N N 2   
A1B3N C1  C2   doub Y N 3   
A1B3N C2  C3   sing Y N 4   
A1B3N C3  C4   doub Y N 5   
A1B3N C4  C5   sing Y N 6   
A1B3N C5  C6   doub Y N 7   
A1B3N C1  C6   sing Y N 8   
A1B3N C6  C7   sing N N 9   
A1B3N C7  C8   sing N N 10  
A1B3N O   C8   doub N N 11  
A1B3N C8  N    sing N N 12  
A1B3N N   C9   sing N N 13  
A1B3N C9  C10  sing N N 14  
A1B3N C10 C11  sing N N 15  
A1B3N C11 C12  sing N N 16  
A1B3N C12 C13  sing N N 17  
A1B3N C13 O1   doub N N 18  
A1B3N N1  C13  sing N N 19  
A1B3N C14 N1   sing N N 20  
A1B3N C15 C14  sing N N 21  
A1B3N C12 C15  sing N N 22  
A1B3N N   C15  sing N N 23  
A1B3N N1  H17  sing N N 24  
A1B3N C4  H7   sing N N 25  
A1B3N C5  H8   sing N N 26  
A1B3N C7  H9   sing N N 27  
A1B3N C7  H10  sing N N 28  
A1B3N C10 H14  sing N N 29  
A1B3N C10 H13  sing N N 30  
A1B3N C15 H1   sing N N 31  
A1B3N C14 H19  sing N N 32  
A1B3N C14 H18  sing N N 33  
A1B3N C12 H    sing N N 34  
A1B3N C11 H15  sing N N 35  
A1B3N C11 H16  sing N N 36  
A1B3N C9  H11  sing N N 37  
A1B3N C9  H12  sing N N 38  
A1B3N C   H3   sing N N 39  
A1B3N C   H2   sing N N 40  
A1B3N C   H4   sing N N 41  
A1B3N C3  H6   sing N N 42  
A1B3N C2  H5   sing N N 43  
ALA   N   CA   sing N N 44  
ALA   N   H    sing N N 45  
ALA   N   H2   sing N N 46  
ALA   CA  C    sing N N 47  
ALA   CA  CB   sing N N 48  
ALA   CA  HA   sing N N 49  
ALA   C   O    doub N N 50  
ALA   C   OXT  sing N N 51  
ALA   CB  HB1  sing N N 52  
ALA   CB  HB2  sing N N 53  
ALA   CB  HB3  sing N N 54  
ALA   OXT HXT  sing N N 55  
ARG   N   CA   sing N N 56  
ARG   N   H    sing N N 57  
ARG   N   H2   sing N N 58  
ARG   CA  C    sing N N 59  
ARG   CA  CB   sing N N 60  
ARG   CA  HA   sing N N 61  
ARG   C   O    doub N N 62  
ARG   C   OXT  sing N N 63  
ARG   CB  CG   sing N N 64  
ARG   CB  HB2  sing N N 65  
ARG   CB  HB3  sing N N 66  
ARG   CG  CD   sing N N 67  
ARG   CG  HG2  sing N N 68  
ARG   CG  HG3  sing N N 69  
ARG   CD  NE   sing N N 70  
ARG   CD  HD2  sing N N 71  
ARG   CD  HD3  sing N N 72  
ARG   NE  CZ   sing N N 73  
ARG   NE  HE   sing N N 74  
ARG   CZ  NH1  sing N N 75  
ARG   CZ  NH2  doub N N 76  
ARG   NH1 HH11 sing N N 77  
ARG   NH1 HH12 sing N N 78  
ARG   NH2 HH21 sing N N 79  
ARG   NH2 HH22 sing N N 80  
ARG   OXT HXT  sing N N 81  
ASN   N   CA   sing N N 82  
ASN   N   H    sing N N 83  
ASN   N   H2   sing N N 84  
ASN   CA  C    sing N N 85  
ASN   CA  CB   sing N N 86  
ASN   CA  HA   sing N N 87  
ASN   C   O    doub N N 88  
ASN   C   OXT  sing N N 89  
ASN   CB  CG   sing N N 90  
ASN   CB  HB2  sing N N 91  
ASN   CB  HB3  sing N N 92  
ASN   CG  OD1  doub N N 93  
ASN   CG  ND2  sing N N 94  
ASN   ND2 HD21 sing N N 95  
ASN   ND2 HD22 sing N N 96  
ASN   OXT HXT  sing N N 97  
ASP   N   CA   sing N N 98  
ASP   N   H    sing N N 99  
ASP   N   H2   sing N N 100 
ASP   CA  C    sing N N 101 
ASP   CA  CB   sing N N 102 
ASP   CA  HA   sing N N 103 
ASP   C   O    doub N N 104 
ASP   C   OXT  sing N N 105 
ASP   CB  CG   sing N N 106 
ASP   CB  HB2  sing N N 107 
ASP   CB  HB3  sing N N 108 
ASP   CG  OD1  doub N N 109 
ASP   CG  OD2  sing N N 110 
ASP   OD2 HD2  sing N N 111 
ASP   OXT HXT  sing N N 112 
CYS   N   CA   sing N N 113 
CYS   N   H    sing N N 114 
CYS   N   H2   sing N N 115 
CYS   CA  C    sing N N 116 
CYS   CA  CB   sing N N 117 
CYS   CA  HA   sing N N 118 
CYS   C   O    doub N N 119 
CYS   C   OXT  sing N N 120 
CYS   CB  SG   sing N N 121 
CYS   CB  HB2  sing N N 122 
CYS   CB  HB3  sing N N 123 
CYS   SG  HG   sing N N 124 
CYS   OXT HXT  sing N N 125 
DMS   S   O    doub N N 126 
DMS   S   C1   sing N N 127 
DMS   S   C2   sing N N 128 
DMS   C1  H11  sing N N 129 
DMS   C1  H12  sing N N 130 
DMS   C1  H13  sing N N 131 
DMS   C2  H21  sing N N 132 
DMS   C2  H22  sing N N 133 
DMS   C2  H23  sing N N 134 
GLN   N   CA   sing N N 135 
GLN   N   H    sing N N 136 
GLN   N   H2   sing N N 137 
GLN   CA  C    sing N N 138 
GLN   CA  CB   sing N N 139 
GLN   CA  HA   sing N N 140 
GLN   C   O    doub N N 141 
GLN   C   OXT  sing N N 142 
GLN   CB  CG   sing N N 143 
GLN   CB  HB2  sing N N 144 
GLN   CB  HB3  sing N N 145 
GLN   CG  CD   sing N N 146 
GLN   CG  HG2  sing N N 147 
GLN   CG  HG3  sing N N 148 
GLN   CD  OE1  doub N N 149 
GLN   CD  NE2  sing N N 150 
GLN   NE2 HE21 sing N N 151 
GLN   NE2 HE22 sing N N 152 
GLN   OXT HXT  sing N N 153 
GLU   N   CA   sing N N 154 
GLU   N   H    sing N N 155 
GLU   N   H2   sing N N 156 
GLU   CA  C    sing N N 157 
GLU   CA  CB   sing N N 158 
GLU   CA  HA   sing N N 159 
GLU   C   O    doub N N 160 
GLU   C   OXT  sing N N 161 
GLU   CB  CG   sing N N 162 
GLU   CB  HB2  sing N N 163 
GLU   CB  HB3  sing N N 164 
GLU   CG  CD   sing N N 165 
GLU   CG  HG2  sing N N 166 
GLU   CG  HG3  sing N N 167 
GLU   CD  OE1  doub N N 168 
GLU   CD  OE2  sing N N 169 
GLU   OE2 HE2  sing N N 170 
GLU   OXT HXT  sing N N 171 
GLY   N   CA   sing N N 172 
GLY   N   H    sing N N 173 
GLY   N   H2   sing N N 174 
GLY   CA  C    sing N N 175 
GLY   CA  HA2  sing N N 176 
GLY   CA  HA3  sing N N 177 
GLY   C   O    doub N N 178 
GLY   C   OXT  sing N N 179 
GLY   OXT HXT  sing N N 180 
HIS   N   CA   sing N N 181 
HIS   N   H    sing N N 182 
HIS   N   H2   sing N N 183 
HIS   CA  C    sing N N 184 
HIS   CA  CB   sing N N 185 
HIS   CA  HA   sing N N 186 
HIS   C   O    doub N N 187 
HIS   C   OXT  sing N N 188 
HIS   CB  CG   sing N N 189 
HIS   CB  HB2  sing N N 190 
HIS   CB  HB3  sing N N 191 
HIS   CG  ND1  sing Y N 192 
HIS   CG  CD2  doub Y N 193 
HIS   ND1 CE1  doub Y N 194 
HIS   ND1 HD1  sing N N 195 
HIS   CD2 NE2  sing Y N 196 
HIS   CD2 HD2  sing N N 197 
HIS   CE1 NE2  sing Y N 198 
HIS   CE1 HE1  sing N N 199 
HIS   NE2 HE2  sing N N 200 
HIS   OXT HXT  sing N N 201 
HOH   O   H1   sing N N 202 
HOH   O   H2   sing N N 203 
ILE   N   CA   sing N N 204 
ILE   N   H    sing N N 205 
ILE   N   H2   sing N N 206 
ILE   CA  C    sing N N 207 
ILE   CA  CB   sing N N 208 
ILE   CA  HA   sing N N 209 
ILE   C   O    doub N N 210 
ILE   C   OXT  sing N N 211 
ILE   CB  CG1  sing N N 212 
ILE   CB  CG2  sing N N 213 
ILE   CB  HB   sing N N 214 
ILE   CG1 CD1  sing N N 215 
ILE   CG1 HG12 sing N N 216 
ILE   CG1 HG13 sing N N 217 
ILE   CG2 HG21 sing N N 218 
ILE   CG2 HG22 sing N N 219 
ILE   CG2 HG23 sing N N 220 
ILE   CD1 HD11 sing N N 221 
ILE   CD1 HD12 sing N N 222 
ILE   CD1 HD13 sing N N 223 
ILE   OXT HXT  sing N N 224 
LEU   N   CA   sing N N 225 
LEU   N   H    sing N N 226 
LEU   N   H2   sing N N 227 
LEU   CA  C    sing N N 228 
LEU   CA  CB   sing N N 229 
LEU   CA  HA   sing N N 230 
LEU   C   O    doub N N 231 
LEU   C   OXT  sing N N 232 
LEU   CB  CG   sing N N 233 
LEU   CB  HB2  sing N N 234 
LEU   CB  HB3  sing N N 235 
LEU   CG  CD1  sing N N 236 
LEU   CG  CD2  sing N N 237 
LEU   CG  HG   sing N N 238 
LEU   CD1 HD11 sing N N 239 
LEU   CD1 HD12 sing N N 240 
LEU   CD1 HD13 sing N N 241 
LEU   CD2 HD21 sing N N 242 
LEU   CD2 HD22 sing N N 243 
LEU   CD2 HD23 sing N N 244 
LEU   OXT HXT  sing N N 245 
LYS   N   CA   sing N N 246 
LYS   N   H    sing N N 247 
LYS   N   H2   sing N N 248 
LYS   CA  C    sing N N 249 
LYS   CA  CB   sing N N 250 
LYS   CA  HA   sing N N 251 
LYS   C   O    doub N N 252 
LYS   C   OXT  sing N N 253 
LYS   CB  CG   sing N N 254 
LYS   CB  HB2  sing N N 255 
LYS   CB  HB3  sing N N 256 
LYS   CG  CD   sing N N 257 
LYS   CG  HG2  sing N N 258 
LYS   CG  HG3  sing N N 259 
LYS   CD  CE   sing N N 260 
LYS   CD  HD2  sing N N 261 
LYS   CD  HD3  sing N N 262 
LYS   CE  NZ   sing N N 263 
LYS   CE  HE2  sing N N 264 
LYS   CE  HE3  sing N N 265 
LYS   NZ  HZ1  sing N N 266 
LYS   NZ  HZ2  sing N N 267 
LYS   NZ  HZ3  sing N N 268 
LYS   OXT HXT  sing N N 269 
MET   N   CA   sing N N 270 
MET   N   H    sing N N 271 
MET   N   H2   sing N N 272 
MET   CA  C    sing N N 273 
MET   CA  CB   sing N N 274 
MET   CA  HA   sing N N 275 
MET   C   O    doub N N 276 
MET   C   OXT  sing N N 277 
MET   CB  CG   sing N N 278 
MET   CB  HB2  sing N N 279 
MET   CB  HB3  sing N N 280 
MET   CG  SD   sing N N 281 
MET   CG  HG2  sing N N 282 
MET   CG  HG3  sing N N 283 
MET   SD  CE   sing N N 284 
MET   CE  HE1  sing N N 285 
MET   CE  HE2  sing N N 286 
MET   CE  HE3  sing N N 287 
MET   OXT HXT  sing N N 288 
PHE   N   CA   sing N N 289 
PHE   N   H    sing N N 290 
PHE   N   H2   sing N N 291 
PHE   CA  C    sing N N 292 
PHE   CA  CB   sing N N 293 
PHE   CA  HA   sing N N 294 
PHE   C   O    doub N N 295 
PHE   C   OXT  sing N N 296 
PHE   CB  CG   sing N N 297 
PHE   CB  HB2  sing N N 298 
PHE   CB  HB3  sing N N 299 
PHE   CG  CD1  doub Y N 300 
PHE   CG  CD2  sing Y N 301 
PHE   CD1 CE1  sing Y N 302 
PHE   CD1 HD1  sing N N 303 
PHE   CD2 CE2  doub Y N 304 
PHE   CD2 HD2  sing N N 305 
PHE   CE1 CZ   doub Y N 306 
PHE   CE1 HE1  sing N N 307 
PHE   CE2 CZ   sing Y N 308 
PHE   CE2 HE2  sing N N 309 
PHE   CZ  HZ   sing N N 310 
PHE   OXT HXT  sing N N 311 
PRO   N   CA   sing N N 312 
PRO   N   CD   sing N N 313 
PRO   N   H    sing N N 314 
PRO   CA  C    sing N N 315 
PRO   CA  CB   sing N N 316 
PRO   CA  HA   sing N N 317 
PRO   C   O    doub N N 318 
PRO   C   OXT  sing N N 319 
PRO   CB  CG   sing N N 320 
PRO   CB  HB2  sing N N 321 
PRO   CB  HB3  sing N N 322 
PRO   CG  CD   sing N N 323 
PRO   CG  HG2  sing N N 324 
PRO   CG  HG3  sing N N 325 
PRO   CD  HD2  sing N N 326 
PRO   CD  HD3  sing N N 327 
PRO   OXT HXT  sing N N 328 
SER   N   CA   sing N N 329 
SER   N   H    sing N N 330 
SER   N   H2   sing N N 331 
SER   CA  C    sing N N 332 
SER   CA  CB   sing N N 333 
SER   CA  HA   sing N N 334 
SER   C   O    doub N N 335 
SER   C   OXT  sing N N 336 
SER   CB  OG   sing N N 337 
SER   CB  HB2  sing N N 338 
SER   CB  HB3  sing N N 339 
SER   OG  HG   sing N N 340 
SER   OXT HXT  sing N N 341 
THR   N   CA   sing N N 342 
THR   N   H    sing N N 343 
THR   N   H2   sing N N 344 
THR   CA  C    sing N N 345 
THR   CA  CB   sing N N 346 
THR   CA  HA   sing N N 347 
THR   C   O    doub N N 348 
THR   C   OXT  sing N N 349 
THR   CB  OG1  sing N N 350 
THR   CB  CG2  sing N N 351 
THR   CB  HB   sing N N 352 
THR   OG1 HG1  sing N N 353 
THR   CG2 HG21 sing N N 354 
THR   CG2 HG22 sing N N 355 
THR   CG2 HG23 sing N N 356 
THR   OXT HXT  sing N N 357 
TRP   N   CA   sing N N 358 
TRP   N   H    sing N N 359 
TRP   N   H2   sing N N 360 
TRP   CA  C    sing N N 361 
TRP   CA  CB   sing N N 362 
TRP   CA  HA   sing N N 363 
TRP   C   O    doub N N 364 
TRP   C   OXT  sing N N 365 
TRP   CB  CG   sing N N 366 
TRP   CB  HB2  sing N N 367 
TRP   CB  HB3  sing N N 368 
TRP   CG  CD1  doub Y N 369 
TRP   CG  CD2  sing Y N 370 
TRP   CD1 NE1  sing Y N 371 
TRP   CD1 HD1  sing N N 372 
TRP   CD2 CE2  doub Y N 373 
TRP   CD2 CE3  sing Y N 374 
TRP   NE1 CE2  sing Y N 375 
TRP   NE1 HE1  sing N N 376 
TRP   CE2 CZ2  sing Y N 377 
TRP   CE3 CZ3  doub Y N 378 
TRP   CE3 HE3  sing N N 379 
TRP   CZ2 CH2  doub Y N 380 
TRP   CZ2 HZ2  sing N N 381 
TRP   CZ3 CH2  sing Y N 382 
TRP   CZ3 HZ3  sing N N 383 
TRP   CH2 HH2  sing N N 384 
TRP   OXT HXT  sing N N 385 
TYR   N   CA   sing N N 386 
TYR   N   H    sing N N 387 
TYR   N   H2   sing N N 388 
TYR   CA  C    sing N N 389 
TYR   CA  CB   sing N N 390 
TYR   CA  HA   sing N N 391 
TYR   C   O    doub N N 392 
TYR   C   OXT  sing N N 393 
TYR   CB  CG   sing N N 394 
TYR   CB  HB2  sing N N 395 
TYR   CB  HB3  sing N N 396 
TYR   CG  CD1  doub Y N 397 
TYR   CG  CD2  sing Y N 398 
TYR   CD1 CE1  sing Y N 399 
TYR   CD1 HD1  sing N N 400 
TYR   CD2 CE2  doub Y N 401 
TYR   CD2 HD2  sing N N 402 
TYR   CE1 CZ   doub Y N 403 
TYR   CE1 HE1  sing N N 404 
TYR   CE2 CZ   sing Y N 405 
TYR   CE2 HE2  sing N N 406 
TYR   CZ  OH   sing N N 407 
TYR   OH  HH   sing N N 408 
TYR   OXT HXT  sing N N 409 
VAL   N   CA   sing N N 410 
VAL   N   H    sing N N 411 
VAL   N   H2   sing N N 412 
VAL   CA  C    sing N N 413 
VAL   CA  CB   sing N N 414 
VAL   CA  HA   sing N N 415 
VAL   C   O    doub N N 416 
VAL   C   OXT  sing N N 417 
VAL   CB  CG1  sing N N 418 
VAL   CB  CG2  sing N N 419 
VAL   CB  HB   sing N N 420 
VAL   CG1 HG11 sing N N 421 
VAL   CG1 HG12 sing N N 422 
VAL   CG1 HG13 sing N N 423 
VAL   CG2 HG21 sing N N 424 
VAL   CG2 HG22 sing N N 425 
VAL   CG2 HG23 sing N N 426 
VAL   OXT HXT  sing N N 427 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I56 
_atom_sites.fract_transf_matrix[1][1]   0.011581 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000954 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017597 
_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]   0.015496 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.793 8.072   24.770 1.00 19.59  ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 19.034 8.146   23.996 1.00 19.35  ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 19.141 6.915   23.066 1.00 18.81  ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.416 5.906   23.244 1.00 18.91  ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.222 8.180   24.954 1.00 21.76  ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.290 6.948   25.651 1.00 25.30  ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 20.071 6.977   22.112 1.00 16.96  ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.326 5.864   21.208 1.00 15.79  ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.725 6.351   19.832 1.00 14.45  ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.446 7.489   19.451 1.00 16.34  ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.406 5.490   19.101 1.00 13.86  ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.878 5.846   17.773 1.00 14.26  ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.836 4.619   16.851 1.00 14.73  ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.726 3.484   17.310 1.00 15.89  ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.336 6.341   17.891 1.00 15.66  ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.922 4.861   15.549 1.00 13.47  ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.108 3.810   14.539 1.00 14.21  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.574 3.894   14.114 1.00 14.47  ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.072 5.006   13.841 1.00 14.63  ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.210 4.043   13.295 1.00 13.31  ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.766 4.221   13.661 1.00 15.84  ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.422 2.888   12.278 1.00 15.58  ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.931 4.814   12.447 1.00 17.00  ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.291 2.754   14.091 1.00 14.57  ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.689 2.728   13.669 1.00 16.09  ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.777 1.897   12.380 1.00 16.87  ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.725 0.659   12.446 1.00 17.40  ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.560 2.120   14.785 1.00 17.35  ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.622 3.015   15.996 1.00 16.50  ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.515 4.084   16.056 1.00 17.13  ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.805 2.793   17.093 1.00 17.74  ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.547 4.947   17.153 1.00 18.14  ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.841 3.642   18.209 1.00 18.63  ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.707 4.728   18.223 1.00 19.69  ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.760 5.570   19.325 1.00 22.24  ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.832 2.556   11.221 1.00 16.59  ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.917 1.913   9.918  1.00 17.84  ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.161 2.406   9.207  1.00 18.33  ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.396 3.632   9.110  1.00 17.95  ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.623 2.170   9.102  1.00 19.16  ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.274 3.672   9.010  1.00 19.23  ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.721 1.546   7.712  1.00 20.37  ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.036 1.484   8.770  1.00 19.40  ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.270 1.895   8.093  1.00 19.90  ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.098 2.791   9.002  1.00 18.87  ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.191 2.509   10.199 1.00 19.63  ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.540 3.943   8.479  1.00 18.50  ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.256 4.932   9.298  1.00 18.35  ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.372 6.107   9.651  1.00 17.00  ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.863 7.242   9.795  1.00 17.57  ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.597 5.376   8.686  1.00 19.93  ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.673 4.333   8.819  1.00 23.60  ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.387 4.273   9.819  1.00 27.48  ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.746 3.440   7.862  1.00 21.75  ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.087 5.829   9.896  1.00 15.77  ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.126 6.867   10.272 1.00 15.01  ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.453 6.530   11.601 1.00 14.29  ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.162 5.359   11.911 1.00 15.83  ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 27.009 6.997   9.205  1.00 16.80  ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.483 7.382   7.825  1.00 17.56  ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.186 8.564   7.609  1.00 18.76  ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.286 6.536   6.741  1.00 19.41  ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.636 8.918   6.334  1.00 20.30  ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.696 6.896   5.463  1.00 21.38  ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.355 8.096   5.264  1.00 22.10  ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.817 8.459   4.007  1.00 26.54  ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.117 7.606   12.341 1.00 14.11  ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.350 7.520   13.585 1.00 14.17  ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.116 8.391   13.358 1.00 13.60  ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.274 9.592   13.054 1.00 13.98  ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.195 8.065   14.756 1.00 15.09  ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.444 8.402   16.022 1.00 16.86  ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.365 8.758   17.198 1.00 17.71  ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.814 9.811   18.050 1.00 18.31  ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 26.134 9.605   19.183 1.00 20.25  ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.882 8.359   19.607 1.00 19.23  ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.669 10.632  19.876 1.00 19.73  ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.905 7.808   13.383 1.00 13.25  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.658 8.562   13.169 1.00 13.94  ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.985 8.764   14.512 1.00 14.36  ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.670 7.786   15.226 1.00 13.66  ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.706 7.796   12.230 1.00 14.38  ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.477 8.646   11.921 1.00 15.65  ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.409 7.296   10.964 1.00 15.14  ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.755 10.028  14.883 1.00 13.33  ? 18  VAL   A N   1 
ATOM   86   C  CA  A VAL   A 1 12  ? 21.145 10.376  16.177 0.50 13.23  ? 18  VAL   A CA  1 
ATOM   87   C  CA  B VAL   A 1 12  ? 21.147 10.328  16.179 0.50 15.38  ? 18  VAL   A CA  1 
ATOM   88   C  C   . VAL   A 1 12  ? 20.025 11.364  16.015 1.00 13.58  ? 18  VAL   A C   1 
ATOM   89   O  O   . VAL   A 1 12  ? 19.881 12.011  14.930 1.00 13.74  ? 18  VAL   A O   1 
ATOM   90   C  CB  A VAL   A 1 12  ? 22.181 10.972  17.188 0.50 11.81  ? 18  VAL   A CB  1 
ATOM   91   C  CB  B VAL   A 1 12  ? 22.262 10.840  17.155 0.50 18.52  ? 18  VAL   A CB  1 
ATOM   92   C  CG1 A VAL   A 1 12  ? 23.109 9.899   17.721 0.50 13.34  ? 18  VAL   A CG1 1 
ATOM   93   C  CG1 B VAL   A 1 12  ? 21.730 11.079  18.558 0.50 20.45  ? 18  VAL   A CG1 1 
ATOM   94   C  CG2 A VAL   A 1 12  ? 22.925 12.215  16.618 0.50 8.87   ? 18  VAL   A CG2 1 
ATOM   95   C  CG2 B VAL   A 1 12  ? 23.434 9.876   17.214 0.50 20.28  ? 18  VAL   A CG2 1 
ATOM   96   N  N   . ASN   A 1 13  ? 19.207 11.541  17.080 1.00 13.51  ? 19  ASN   A N   1 
ATOM   97   C  CA  . ASN   A 1 13  ? 18.215 12.619  17.046 1.00 13.35  ? 19  ASN   A CA  1 
ATOM   98   C  C   . ASN   A 1 13  ? 19.018 13.941  17.055 1.00 14.55  ? 19  ASN   A C   1 
ATOM   99   O  O   . ASN   A 1 13  ? 19.974 14.101  17.846 1.00 15.15  ? 19  ASN   A O   1 
ATOM   100  C  CB  . ASN   A 1 13  ? 17.361 12.617  18.318 1.00 13.47  ? 19  ASN   A CB  1 
ATOM   101  C  CG  . ASN   A 1 13  ? 16.499 11.374  18.420 1.00 14.19  ? 19  ASN   A CG  1 
ATOM   102  O  OD1 . ASN   A 1 13  ? 16.921 10.369  19.015 1.00 14.88  ? 19  ASN   A OD1 1 
ATOM   103  N  ND2 . ASN   A 1 13  ? 15.323 11.442  17.811 1.00 15.54  ? 19  ASN   A ND2 1 
ATOM   104  N  N   . ARG   A 1 14  ? 18.673 14.856  16.143 1.00 14.27  ? 20  ARG   A N   1 
ATOM   105  C  CA  . ARG   A 1 14  ? 19.403 16.149  16.095 1.00 13.64  ? 20  ARG   A CA  1 
ATOM   106  C  C   . ARG   A 1 14  ? 19.392 16.842  17.471 1.00 16.06  ? 20  ARG   A C   1 
ATOM   107  O  O   . ARG   A 1 14  ? 20.403 17.386  17.892 1.00 17.08  ? 20  ARG   A O   1 
ATOM   108  C  CB  . ARG   A 1 14  ? 18.790 17.038  15.015 1.00 15.34  ? 20  ARG   A CB  1 
ATOM   109  C  CG  . ARG   A 1 14  ? 19.582 18.357  14.787 1.00 15.30  ? 20  ARG   A CG  1 
ATOM   110  C  CD  . ARG   A 1 14  ? 18.810 19.244  13.833 1.00 17.10  ? 20  ARG   A CD  1 
ATOM   111  N  NE  . ARG   A 1 14  ? 19.570 20.437  13.386 1.00 16.15  ? 20  ARG   A NE  1 
ATOM   112  C  CZ  . ARG   A 1 14  ? 19.556 21.599  14.020 1.00 20.16  ? 20  ARG   A CZ  1 
ATOM   113  N  NH1 . ARG   A 1 14  ? 18.997 21.700  15.218 1.00 20.57  ? 20  ARG   A NH1 1 
ATOM   114  N  NH2 . ARG   A 1 14  ? 20.180 22.657  13.497 1.00 21.74  ? 20  ARG   A NH2 1 
ATOM   115  N  N   . HIS   A 1 15  ? 18.250 16.720  18.186 1.00 15.83  ? 21  HIS   A N   1 
ATOM   116  C  CA  . HIS   A 1 15  ? 18.142 17.420  19.484 1.00 16.92  ? 21  HIS   A CA  1 
ATOM   117  C  C   . HIS   A 1 15  ? 19.012 16.802  20.596 1.00 17.30  ? 21  HIS   A C   1 
ATOM   118  O  O   . HIS   A 1 15  ? 19.175 17.426  21.665 1.00 19.57  ? 21  HIS   A O   1 
ATOM   119  C  CB  . HIS   A 1 15  ? 16.668 17.587  19.927 1.00 18.69  ? 21  HIS   A CB  1 
ATOM   120  C  CG  . HIS   A 1 15  ? 15.994 16.339  20.425 1.00 18.48  ? 21  HIS   A CG  1 
ATOM   121  N  ND1 . HIS   A 1 15  ? 15.380 15.465  19.566 1.00 18.49  ? 21  HIS   A ND1 1 
ATOM   122  C  CD2 . HIS   A 1 15  ? 15.811 15.897  21.693 1.00 18.54  ? 21  HIS   A CD2 1 
ATOM   123  C  CE1 . HIS   A 1 15  ? 14.844 14.511  20.335 1.00 20.04  ? 21  HIS   A CE1 1 
ATOM   124  N  NE2 . HIS   A 1 15  ? 15.068 14.746  21.627 1.00 19.67  ? 21  HIS   A NE2 1 
ATOM   125  N  N   . LEU   A 1 16  ? 19.527 15.578  20.389 1.00 16.78  ? 22  LEU   A N   1 
ATOM   126  C  CA  . LEU   A 1 16  ? 20.413 14.878  21.335 1.00 16.62  ? 22  LEU   A CA  1 
ATOM   127  C  C   . LEU   A 1 16  ? 21.878 14.807  20.881 1.00 18.46  ? 22  LEU   A C   1 
ATOM   128  O  O   . LEU   A 1 16  ? 22.702 14.164  21.531 1.00 20.07  ? 22  LEU   A O   1 
ATOM   129  C  CB  . LEU   A 1 16  ? 19.862 13.477  21.646 1.00 16.93  ? 22  LEU   A CB  1 
ATOM   130  C  CG  . LEU   A 1 16  ? 18.481 13.509  22.283 1.00 17.93  ? 22  LEU   A CG  1 
ATOM   131  C  CD1 . LEU   A 1 16  ? 17.968 12.056  22.498 1.00 18.50  ? 22  LEU   A CD1 1 
ATOM   132  C  CD2 . LEU   A 1 16  ? 18.504 14.286  23.644 1.00 19.50  ? 22  LEU   A CD2 1 
ATOM   133  N  N   . ALA   A 1 17  ? 22.199 15.431  19.749 1.00 17.03  ? 23  ALA   A N   1 
ATOM   134  C  CA  . ALA   A 1 17  ? 23.562 15.429  19.239 1.00 17.17  ? 23  ALA   A CA  1 
ATOM   135  C  C   . ALA   A 1 17  ? 24.551 16.080  20.218 1.00 18.67  ? 23  ALA   A C   1 
ATOM   136  O  O   . ALA   A 1 17  ? 24.239 17.094  20.851 1.00 19.91  ? 23  ALA   A O   1 
ATOM   137  C  CB  . ALA   A 1 17  ? 23.610 16.139  17.865 1.00 16.82  ? 23  ALA   A CB  1 
ATOM   138  N  N   . THR   A 1 18  ? 25.746 15.461  20.337 1.00 17.24  ? 24  THR   A N   1 
ATOM   139  C  CA  . THR   A 1 18  ? 26.795 15.960  21.255 1.00 16.48  ? 24  THR   A CA  1 
ATOM   140  C  C   . THR   A 1 18  ? 27.723 16.960  20.539 1.00 17.75  ? 24  THR   A C   1 
ATOM   141  O  O   . THR   A 1 18  ? 27.650 17.108  19.290 1.00 16.69  ? 24  THR   A O   1 
ATOM   142  C  CB  . THR   A 1 18  ? 27.642 14.782  21.751 1.00 19.41  ? 24  THR   A CB  1 
ATOM   143  O  OG1 . THR   A 1 18  ? 28.336 14.232  20.619 1.00 19.63  ? 24  THR   A OG1 1 
ATOM   144  C  CG2 . THR   A 1 18  ? 26.792 13.671  22.433 1.00 19.69  ? 24  THR   A CG2 1 
ATOM   145  N  N   . HIS   A 1 19  ? 28.661 17.614  21.265 1.00 17.96  ? 25  HIS   A N   1 
ATOM   146  C  CA  . HIS   A 1 19  ? 29.639 18.459  20.610 1.00 18.24  ? 25  HIS   A CA  1 
ATOM   147  C  C   . HIS   A 1 19  ? 30.489 17.647  19.636 1.00 17.52  ? 25  HIS   A C   1 
ATOM   148  O  O   . HIS   A 1 19  ? 30.742 18.131  18.545 1.00 17.91  ? 25  HIS   A O   1 
ATOM   149  C  CB  . HIS   A 1 19  ? 30.576 19.150  21.636 1.00 20.69  ? 25  HIS   A CB  1 
ATOM   150  C  CG  . HIS   A 1 19  ? 31.813 19.771  20.988 1.00 25.92  ? 25  HIS   A CG  1 
ATOM   151  N  ND1 . HIS   A 1 19  ? 31.736 20.926  20.191 1.00 28.64  ? 25  HIS   A ND1 1 
ATOM   152  C  CD2 . HIS   A 1 19  ? 33.102 19.318  20.948 1.00 28.57  ? 25  HIS   A CD2 1 
ATOM   153  C  CE1 . HIS   A 1 19  ? 32.978 21.196  19.798 1.00 29.70  ? 25  HIS   A CE1 1 
ATOM   154  N  NE2 . HIS   A 1 19  ? 33.831 20.228  20.165 1.00 30.53  ? 25  HIS   A NE2 1 
ATOM   155  N  N   . ASN   A 1 20  ? 30.855 16.386  19.986 1.00 17.44  ? 26  ASN   A N   1 
ATOM   156  C  CA  . ASN   A 1 20  ? 31.659 15.587  19.066 1.00 17.25  ? 26  ASN   A CA  1 
ATOM   157  C  C   . ASN   A 1 20  ? 30.872 15.316  17.777 1.00 16.84  ? 26  ASN   A C   1 
ATOM   158  O  O   . ASN   A 1 20  ? 31.438 15.366  16.673 1.00 17.85  ? 26  ASN   A O   1 
ATOM   159  C  CB  . ASN   A 1 20  ? 32.075 14.277  19.713 1.00 19.23  ? 26  ASN   A CB  1 
ATOM   160  C  CG  . ASN   A 1 20  ? 33.029 13.506  18.826 1.00 26.75  ? 26  ASN   A CG  1 
ATOM   161  O  OD1 . ASN   A 1 20  ? 34.211 13.888  18.652 1.00 31.09  ? 26  ASN   A OD1 1 
ATOM   162  N  ND2 . ASN   A 1 20  ? 32.542 12.410  18.235 1.00 27.39  ? 26  ASN   A ND2 1 
ATOM   163  N  N   . ASP   A 1 21  ? 29.525 15.059  17.911 1.00 16.55  ? 27  ASP   A N   1 
ATOM   164  C  CA  . ASP   A 1 21  ? 28.725 14.903  16.693 1.00 16.38  ? 27  ASP   A CA  1 
ATOM   165  C  C   . ASP   A 1 21  ? 28.804 16.152  15.793 1.00 14.71  ? 27  ASP   A C   1 
ATOM   166  O  O   . ASP   A 1 21  ? 28.972 16.026  14.580 1.00 15.92  ? 27  ASP   A O   1 
ATOM   167  C  CB  . ASP   A 1 21  ? 27.257 14.601  17.006 1.00 15.60  ? 27  ASP   A CB  1 
ATOM   168  C  CG  . ASP   A 1 21  ? 26.995 13.253  17.609 1.00 17.02  ? 27  ASP   A CG  1 
ATOM   169  O  OD1 . ASP   A 1 21  ? 27.672 12.265  17.189 1.00 16.51  ? 27  ASP   A OD1 1 
ATOM   170  O  OD2 . ASP   A 1 21  ? 26.171 13.192  18.545 1.00 15.85  ? 27  ASP   A OD2 1 
ATOM   171  N  N   . TRP   A 1 22  ? 28.588 17.331  16.365 1.00 14.58  ? 28  TRP   A N   1 
ATOM   172  C  CA  . TRP   A 1 22  ? 28.621 18.576  15.597 1.00 14.13  ? 28  TRP   A CA  1 
ATOM   173  C  C   . TRP   A 1 22  ? 30.035 18.869  15.026 1.00 15.04  ? 28  TRP   A C   1 
ATOM   174  O  O   . TRP   A 1 22  ? 30.103 19.412  13.929 1.00 16.66  ? 28  TRP   A O   1 
ATOM   175  C  CB  . TRP   A 1 22  ? 28.133 19.744  16.500 1.00 15.11  ? 28  TRP   A CB  1 
ATOM   176  C  CG  . TRP   A 1 22  ? 26.630 19.826  16.628 1.00 14.79  ? 28  TRP   A CG  1 
ATOM   177  C  CD1 . TRP   A 1 22  ? 25.881 19.521  17.723 1.00 16.77  ? 28  TRP   A CD1 1 
ATOM   178  C  CD2 . TRP   A 1 22  ? 25.705 20.261  15.613 1.00 15.71  ? 28  TRP   A CD2 1 
ATOM   179  N  NE1 . TRP   A 1 22  ? 24.539 19.805  17.484 1.00 16.51  ? 28  TRP   A NE1 1 
ATOM   180  C  CE2 . TRP   A 1 22  ? 24.408 20.218  16.165 1.00 15.87  ? 28  TRP   A CE2 1 
ATOM   181  C  CE3 . TRP   A 1 22  ? 25.867 20.753  14.312 1.00 17.19  ? 28  TRP   A CE3 1 
ATOM   182  C  CZ2 . TRP   A 1 22  ? 23.282 20.617  15.425 1.00 17.85  ? 28  TRP   A CZ2 1 
ATOM   183  C  CZ3 . TRP   A 1 22  ? 24.759 21.068  13.570 1.00 17.99  ? 28  TRP   A CZ3 1 
ATOM   184  C  CH2 . TRP   A 1 22  ? 23.506 21.122  14.154 1.00 17.95  ? 28  TRP   A CH2 1 
ATOM   185  N  N   . ALA   A 1 23  ? 31.114 18.453  15.712 1.00 15.24  ? 29  ALA   A N   1 
ATOM   186  C  CA  . ALA   A 1 23  ? 32.463 18.680  15.231 1.00 15.67  ? 29  ALA   A CA  1 
ATOM   187  C  C   . ALA   A 1 23  ? 32.871 17.665  14.139 1.00 16.98  ? 29  ALA   A C   1 
ATOM   188  O  O   . ALA   A 1 23  ? 33.889 17.840  13.487 1.00 19.18  ? 29  ALA   A O   1 
ATOM   189  C  CB  . ALA   A 1 23  ? 33.417 18.639  16.412 1.00 17.45  ? 29  ALA   A CB  1 
ATOM   190  N  N   . ASN   A 1 24  ? 32.097 16.580  13.955 1.00 16.16  ? 30  ASN   A N   1 
ATOM   191  C  CA  . ASN   A 1 24  ? 32.350 15.562  12.931 1.00 16.51  ? 30  ASN   A CA  1 
ATOM   192  C  C   . ASN   A 1 24  ? 31.064 15.379  12.093 1.00 16.71  ? 30  ASN   A C   1 
ATOM   193  O  O   . ASN   A 1 24  ? 30.694 14.255  11.750 1.00 16.30  ? 30  ASN   A O   1 
ATOM   194  C  CB  . ASN   A 1 24  ? 32.738 14.248  13.630 1.00 16.64  ? 30  ASN   A CB  1 
ATOM   195  C  CG  . ASN   A 1 24  ? 34.101 14.391  14.290 1.00 20.46  ? 30  ASN   A CG  1 
ATOM   196  O  OD1 . ASN   A 1 24  ? 35.145 14.329  13.617 1.00 23.05  ? 30  ASN   A OD1 1 
ATOM   197  N  ND2 . ASN   A 1 24  ? 34.146 14.699  15.597 1.00 20.70  ? 30  ASN   A ND2 1 
ATOM   198  N  N   . LEU   A 1 25  ? 30.420 16.457  11.742 1.00 16.20  ? 31  LEU   A N   1 
ATOM   199  C  CA  . LEU   A 1 25  ? 29.105 16.445  11.093 1.00 15.42  ? 31  LEU   A CA  1 
ATOM   200  C  C   . LEU   A 1 25  ? 29.168 16.005  9.647  1.00 17.15  ? 31  LEU   A C   1 
ATOM   201  O  O   . LEU   A 1 25  ? 30.009 16.476  8.879  1.00 18.81  ? 31  LEU   A O   1 
ATOM   202  C  CB  . LEU   A 1 25  ? 28.517 17.864  11.204 1.00 15.75  ? 31  LEU   A CB  1 
ATOM   203  C  CG  . LEU   A 1 25  ? 27.131 18.027  10.590 1.00 16.51  ? 31  LEU   A CG  1 
ATOM   204  C  CD1 . LEU   A 1 25  ? 26.066 17.229  11.378 1.00 16.88  ? 31  LEU   A CD1 1 
ATOM   205  C  CD2 . LEU   A 1 25  ? 26.747 19.495  10.552 1.00 18.49  ? 31  LEU   A CD2 1 
ATOM   206  N  N   . VAL   A 1 26  ? 28.236 15.162  9.238  1.00 15.61  ? 32  VAL   A N   1 
ATOM   207  C  CA  . VAL   A 1 26  ? 28.075 14.744  7.848  1.00 15.95  ? 32  VAL   A CA  1 
ATOM   208  C  C   . VAL   A 1 26  ? 26.814 15.453  7.268  1.00 16.43  ? 32  VAL   A C   1 
ATOM   209  O  O   . VAL   A 1 26  ? 26.859 16.005  6.169  1.00 18.54  ? 32  VAL   A O   1 
ATOM   210  C  CB  . VAL   A 1 26  ? 27.933 13.200  7.746  1.00 16.12  ? 32  VAL   A CB  1 
ATOM   211  C  CG1 . VAL   A 1 26  ? 27.587 12.775  6.294  1.00 17.19  ? 32  VAL   A CG1 1 
ATOM   212  C  CG2 . VAL   A 1 26  ? 29.243 12.500  8.211  1.00 17.90  ? 32  VAL   A CG2 1 
ATOM   213  N  N   . TRP   A 1 27  ? 25.686 15.431  7.989  1.00 16.18  ? 33  TRP   A N   1 
ATOM   214  C  CA  . TRP   A 1 27  ? 24.433 15.977  7.507  1.00 16.40  ? 33  TRP   A CA  1 
ATOM   215  C  C   . TRP   A 1 27  ? 23.481 16.177  8.679  1.00 16.51  ? 33  TRP   A C   1 
ATOM   216  O  O   . TRP   A 1 27  ? 23.487 15.388  9.644  1.00 15.80  ? 33  TRP   A O   1 
ATOM   217  C  CB  . TRP   A 1 27  ? 23.810 14.954  6.501  1.00 16.98  ? 33  TRP   A CB  1 
ATOM   218  C  CG  . TRP   A 1 27  ? 22.401 15.224  6.055  1.00 18.16  ? 33  TRP   A CG  1 
ATOM   219  C  CD1 . TRP   A 1 27  ? 21.998 16.066  5.057  1.00 19.81  ? 33  TRP   A CD1 1 
ATOM   220  C  CD2 . TRP   A 1 27  ? 21.207 14.611  6.565  1.00 17.84  ? 33  TRP   A CD2 1 
ATOM   221  N  NE1 . TRP   A 1 27  ? 20.624 15.998  4.909  1.00 21.85  ? 33  TRP   A NE1 1 
ATOM   222  C  CE2 . TRP   A 1 27  ? 20.119 15.096  5.804  1.00 19.83  ? 33  TRP   A CE2 1 
ATOM   223  C  CE3 . TRP   A 1 27  ? 20.943 13.705  7.596  1.00 18.22  ? 33  TRP   A CE3 1 
ATOM   224  C  CZ2 . TRP   A 1 27  ? 18.791 14.682  6.035  1.00 20.67  ? 33  TRP   A CZ2 1 
ATOM   225  C  CZ3 . TRP   A 1 27  ? 19.639 13.264  7.772  1.00 19.11  ? 33  TRP   A CZ3 1 
ATOM   226  C  CH2 . TRP   A 1 27  ? 18.578 13.817  7.054  1.00 20.50  ? 33  TRP   A CH2 1 
ATOM   227  N  N   . GLU   A 1 28  ? 22.646 17.204  8.615  1.00 16.23  ? 34  GLU   A N   1 
ATOM   228  C  CA  . GLU   A 1 28  ? 21.643 17.423  9.634  1.00 16.20  ? 34  GLU   A CA  1 
ATOM   229  C  C   . GLU   A 1 28  ? 20.423 18.064  9.014  1.00 17.24  ? 34  GLU   A C   1 
ATOM   230  O  O   . GLU   A 1 28  ? 20.522 18.848  8.051  1.00 17.58  ? 34  GLU   A O   1 
ATOM   231  C  CB  . GLU   A 1 28  ? 22.181 18.276  10.816 1.00 17.24  ? 34  GLU   A CB  1 
ATOM   232  C  CG  . GLU   A 1 28  ? 22.769 19.628  10.413 1.00 19.38  ? 34  GLU   A CG  1 
ATOM   233  C  CD  . GLU   A 1 28  ? 21.807 20.802  10.239 1.00 20.15  ? 34  GLU   A CD  1 
ATOM   234  O  OE1 . GLU   A 1 28  ? 22.130 21.745  9.463  1.00 19.70  ? 34  GLU   A OE1 1 
ATOM   235  O  OE2 . GLU   A 1 28  ? 20.713 20.797  10.856 1.00 18.97  ? 34  GLU   A OE2 1 
ATOM   236  N  N   . ASP   A 1 29  ? 19.259 17.801  9.587  1.00 16.94  ? 35  ASP   A N   1 
ATOM   237  C  CA  . ASP   A 1 29  ? 17.985 18.351  9.098  1.00 17.18  ? 35  ASP   A CA  1 
ATOM   238  C  C   . ASP   A 1 29  ? 17.030 18.518  10.293 1.00 17.49  ? 35  ASP   A C   1 
ATOM   239  O  O   . ASP   A 1 29  ? 16.513 17.544  10.866 1.00 16.84  ? 35  ASP   A O   1 
ATOM   240  C  CB  . ASP   A 1 29  ? 17.417 17.434  7.993  1.00 18.16  ? 35  ASP   A CB  1 
ATOM   241  C  CG  . ASP   A 1 29  ? 16.126 17.888  7.374  1.00 23.98  ? 35  ASP   A CG  1 
ATOM   242  O  OD1 . ASP   A 1 29  ? 15.331 18.518  8.078  1.00 26.46  ? 35  ASP   A OD1 1 
ATOM   243  O  OD2 . ASP   A 1 29  ? 15.923 17.627  6.170  1.00 25.16  ? 35  ASP   A OD2 1 
ATOM   244  N  N   . SER   A 1 30  ? 16.801 19.774  10.698 1.00 17.96  ? 36  SER   A N   1 
ATOM   245  C  CA  A SER   A 1 30  ? 15.964 20.095  11.838 0.50 18.33  ? 36  SER   A CA  1 
ATOM   246  C  CA  B SER   A 1 30  ? 15.973 20.065  11.848 0.50 19.05  ? 36  SER   A CA  1 
ATOM   247  C  C   . SER   A 1 30  ? 14.510 19.690  11.600 1.00 18.69  ? 36  SER   A C   1 
ATOM   248  O  O   . SER   A 1 30  ? 13.867 19.190  12.531 1.00 19.37  ? 36  SER   A O   1 
ATOM   249  C  CB  A SER   A 1 30  ? 16.070 21.578  12.159 0.50 18.99  ? 36  SER   A CB  1 
ATOM   250  C  CB  B SER   A 1 30  ? 16.133 21.520  12.264 0.50 21.90  ? 36  SER   A CB  1 
ATOM   251  O  OG  A SER   A 1 30  ? 15.028 21.998  13.023 0.50 19.54  ? 36  SER   A OG  1 
ATOM   252  O  OG  B SER   A 1 30  ? 15.842 22.388  11.182 0.50 27.04  ? 36  SER   A OG  1 
ATOM   253  N  N   . SER   A 1 31  ? 14.011 19.826  10.346 1.00 19.43  ? 37  SER   A N   1 
ATOM   254  C  CA  . SER   A 1 31  ? 12.623 19.421  10.071 1.00 19.50  ? 37  SER   A CA  1 
ATOM   255  C  C   . SER   A 1 31  ? 12.369 17.922  10.278 1.00 18.98  ? 37  SER   A C   1 
ATOM   256  O  O   . SER   A 1 31  ? 11.228 17.520  10.542 1.00 20.23  ? 37  SER   A O   1 
ATOM   257  C  CB  . SER   A 1 31  ? 12.203 19.821  8.656  1.00 22.41  ? 37  SER   A CB  1 
ATOM   258  O  OG  . SER   A 1 31  ? 12.766 18.992  7.657  1.00 28.52  ? 37  SER   A OG  1 
ATOM   259  N  N   . ARG   A 1 32  ? 13.418 17.101  10.188 1.00 17.04  ? 38  ARG   A N   1 
ATOM   260  C  CA  . ARG   A 1 32  ? 13.336 15.647  10.383 1.00 16.51  ? 38  ARG   A CA  1 
ATOM   261  C  C   . ARG   A 1 32  ? 13.832 15.175  11.757 1.00 16.86  ? 38  ARG   A C   1 
ATOM   262  O  O   . ARG   A 1 32  ? 13.718 13.974  12.055 1.00 16.55  ? 38  ARG   A O   1 
ATOM   263  C  CB  . ARG   A 1 32  ? 14.197 14.915  9.322  1.00 17.34  ? 38  ARG   A CB  1 
ATOM   264  C  CG  . ARG   A 1 32  ? 13.711 15.145  7.883  1.00 19.78  ? 38  ARG   A CG  1 
ATOM   265  C  CD  . ARG   A 1 32  ? 14.559 14.435  6.844  1.00 18.26  ? 38  ARG   A CD  1 
ATOM   266  N  NE  . ARG   A 1 32  ? 14.418 12.980  6.955  1.00 15.88  ? 38  ARG   A NE  1 
ATOM   267  C  CZ  . ARG   A 1 32  ? 14.564 12.136  5.947  1.00 17.88  ? 38  ARG   A CZ  1 
ATOM   268  N  NH1 . ARG   A 1 32  ? 14.791 12.593  4.712  1.00 20.96  ? 38  ARG   A NH1 1 
ATOM   269  N  NH2 . ARG   A 1 32  ? 14.404 10.825  6.139  1.00 17.24  ? 38  ARG   A NH2 1 
ATOM   270  N  N   . ASP   A 1 33  ? 14.403 16.085  12.578 1.00 16.00  ? 39  ASP   A N   1 
ATOM   271  C  CA  . ASP   A 1 33  ? 15.041 15.756  13.857 1.00 15.32  ? 39  ASP   A CA  1 
ATOM   272  C  C   . ASP   A 1 33  ? 16.166 14.720  13.668 1.00 14.49  ? 39  ASP   A C   1 
ATOM   273  O  O   . ASP   A 1 33  ? 16.369 13.884  14.554 1.00 15.31  ? 39  ASP   A O   1 
ATOM   274  C  CB  . ASP   A 1 33  ? 14.038 15.275  14.909 1.00 15.71  ? 39  ASP   A CB  1 
ATOM   275  C  CG  . ASP   A 1 33  ? 14.662 15.047  16.276 1.00 15.14  ? 39  ASP   A CG  1 
ATOM   276  O  OD1 . ASP   A 1 33  ? 15.512 15.876  16.700 1.00 16.44  ? 39  ASP   A OD1 1 
ATOM   277  O  OD2 . ASP   A 1 33  ? 14.279 14.075  16.944 1.00 17.18  ? 39  ASP   A OD2 1 
ATOM   278  N  N   . LEU   A 1 34  ? 16.959 14.822  12.593 1.00 15.06  ? 40  LEU   A N   1 
ATOM   279  C  CA  . LEU   A 1 34  ? 18.052 13.887  12.370 1.00 14.39  ? 40  LEU   A CA  1 
ATOM   280  C  C   . LEU   A 1 34  ? 19.418 14.587  12.243 1.00 14.01  ? 40  LEU   A C   1 
ATOM   281  O  O   . LEU   A 1 34  ? 19.518 15.689  11.657 1.00 14.09  ? 40  LEU   A O   1 
ATOM   282  C  CB  . LEU   A 1 34  ? 17.807 13.094  11.071 1.00 15.09  ? 40  LEU   A CB  1 
ATOM   283  C  CG  . LEU   A 1 34  ? 16.705 12.008  11.120 1.00 14.95  ? 40  LEU   A CG  1 
ATOM   284  C  CD1 . LEU   A 1 34  ? 16.607 11.276  9.769  1.00 16.46  ? 40  LEU   A CD1 1 
ATOM   285  C  CD2 . LEU   A 1 34  ? 17.017 10.975  12.240 1.00 17.02  ? 40  LEU   A CD2 1 
ATOM   286  N  N   . LEU   A 1 35  ? 20.472 13.914  12.693 1.00 12.29  ? 41  LEU   A N   1 
ATOM   287  C  CA  . LEU   A 1 35  ? 21.843 14.373  12.504 1.00 12.51  ? 41  LEU   A CA  1 
ATOM   288  C  C   . LEU   A 1 35  ? 22.683 13.137  12.321 1.00 12.65  ? 41  LEU   A C   1 
ATOM   289  O  O   . LEU   A 1 35  ? 22.487 12.103  13.010 1.00 13.93  ? 41  LEU   A O   1 
ATOM   290  C  CB  . LEU   A 1 35  ? 22.304 15.191  13.722 1.00 13.50  ? 41  LEU   A CB  1 
ATOM   291  C  CG  . LEU   A 1 35  ? 23.736 15.793  13.614 1.00 14.34  ? 41  LEU   A CG  1 
ATOM   292  C  CD1 . LEU   A 1 35  ? 23.841 17.148  14.304 1.00 16.33  ? 41  LEU   A CD1 1 
ATOM   293  C  CD2 . LEU   A 1 35  ? 24.779 14.853  14.233 1.00 15.30  ? 41  LEU   A CD2 1 
ATOM   294  N  N   . VAL   A 1 36  ? 23.651 13.217  11.389 1.00 13.10  ? 42  VAL   A N   1 
ATOM   295  C  CA  . VAL   A 1 36  ? 24.557 12.130  11.096 1.00 12.70  ? 42  VAL   A CA  1 
ATOM   296  C  C   . VAL   A 1 36  ? 25.989 12.618  11.253 1.00 13.03  ? 42  VAL   A C   1 
ATOM   297  O  O   . VAL   A 1 36  ? 26.338 13.684  10.723 1.00 14.75  ? 42  VAL   A O   1 
ATOM   298  C  CB  . VAL   A 1 36  ? 24.317 11.519  9.693  1.00 13.13  ? 42  VAL   A CB  1 
ATOM   299  C  CG1 . VAL   A 1 36  ? 25.348 10.411  9.406  1.00 14.41  ? 42  VAL   A CG1 1 
ATOM   300  C  CG2 . VAL   A 1 36  ? 22.863 11.009  9.562  1.00 14.56  ? 42  VAL   A CG2 1 
ATOM   301  N  N   . SER   A 1 37  ? 26.796 11.912  12.029 1.00 13.47  ? 43  SER   A N   1 
ATOM   302  C  CA  . SER   A 1 37  ? 28.218 12.258  12.235 1.00 14.36  ? 43  SER   A CA  1 
ATOM   303  C  C   . SER   A 1 37  ? 29.085 11.077  11.775 1.00 15.91  ? 43  SER   A C   1 
ATOM   304  O  O   . SER   A 1 37  ? 28.606 9.947   11.543 1.00 15.57  ? 43  SER   A O   1 
ATOM   305  C  CB  . SER   A 1 37  ? 28.495 12.624  13.692 1.00 15.26  ? 43  SER   A CB  1 
ATOM   306  O  OG  . SER   A 1 37  ? 28.182 11.540  14.546 1.00 15.31  ? 43  SER   A OG  1 
ATOM   307  N  N   . SER   A 1 38  ? 30.383 11.352  11.569 1.00 16.88  ? 44  SER   A N   1 
ATOM   308  C  CA  . SER   A 1 38  ? 31.317 10.309  11.118 1.00 17.88  ? 44  SER   A CA  1 
ATOM   309  C  C   . SER   A 1 38  ? 31.933 9.569   12.314 1.00 19.83  ? 44  SER   A C   1 
ATOM   310  O  O   . SER   A 1 38  ? 32.110 10.165  13.409 1.00 21.40  ? 44  SER   A O   1 
ATOM   311  C  CB  . SER   A 1 38  ? 32.391 10.928  10.221 1.00 20.63  ? 44  SER   A CB  1 
ATOM   312  O  OG  . SER   A 1 38  ? 33.132 11.873  10.975 1.00 23.38  ? 44  SER   A OG  1 
ATOM   313  N  N   . THR   A 1 39  ? 32.248 8.262   12.114 1.00 19.75  ? 45  THR   A N   1 
ATOM   314  C  CA  . THR   A 1 39  ? 32.841 7.465   13.184 1.00 21.36  ? 45  THR   A CA  1 
ATOM   315  C  C   . THR   A 1 39  ? 34.193 6.892   12.732 1.00 23.13  ? 45  THR   A C   1 
ATOM   316  O  O   . THR   A 1 39  ? 34.391 6.650   11.535 1.00 21.50  ? 45  THR   A O   1 
ATOM   317  C  CB  . THR   A 1 39  ? 31.908 6.281   13.548 1.00 22.42  ? 45  THR   A CB  1 
ATOM   318  O  OG1 . THR   A 1 39  ? 31.787 5.416   12.412 1.00 23.26  ? 45  THR   A OG1 1 
ATOM   319  C  CG2 . THR   A 1 39  ? 30.540 6.730   14.027 1.00 22.53  ? 45  THR   A CG2 1 
ATOM   320  N  N   . THR   A 1 40  ? 35.036 6.544   13.705 1.00 24.33  ? 46  THR   A N   1 
ATOM   321  C  CA  . THR   A 1 40  ? 36.300 5.921   13.368 1.00 26.31  ? 46  THR   A CA  1 
ATOM   322  C  C   . THR   A 1 40  ? 36.084 4.424   13.126 1.00 27.21  ? 46  THR   A C   1 
ATOM   323  O  O   . THR   A 1 40  ? 36.620 3.884   12.155 1.00 28.53  ? 46  THR   A O   1 
ATOM   324  C  CB  . THR   A 1 40  ? 37.354 6.288   14.403 1.00 30.35  ? 46  THR   A CB  1 
ATOM   325  O  OG1 . THR   A 1 40  ? 36.885 5.904   15.693 1.00 33.61  ? 46  THR   A OG1 1 
ATOM   326  C  CG2 . THR   A 1 40  ? 37.637 7.765   14.391 1.00 30.58  ? 46  THR   A CG2 1 
ATOM   327  N  N   . ALA   A 1 41  ? 35.283 3.776   13.977 1.00 27.94  ? 47  ALA   A N   1 
ATOM   328  C  CA  . ALA   A 1 41  ? 34.985 2.349   13.830 1.00 28.78  ? 47  ALA   A CA  1 
ATOM   329  C  C   . ALA   A 1 41  ? 33.761 2.085   12.957 1.00 27.43  ? 47  ALA   A C   1 
ATOM   330  O  O   . ALA   A 1 41  ? 32.825 2.873   12.972 1.00 26.55  ? 47  ALA   A O   1 
ATOM   331  C  CB  . ALA   A 1 41  ? 34.735 1.723   15.189 1.00 30.95  ? 47  ALA   A CB  1 
ATOM   332  N  N   . GLN   A 1 42  ? 33.714 0.933   12.286 1.00 26.49  ? 48  GLN   A N   1 
ATOM   333  C  CA  . GLN   A 1 42  ? 32.568 0.567   11.457 1.00 26.89  ? 48  GLN   A CA  1 
ATOM   334  C  C   . GLN   A 1 42  ? 31.486 -0.043  12.312 1.00 25.60  ? 48  GLN   A C   1 
ATOM   335  O  O   . GLN   A 1 42  ? 31.759 -0.782  13.261 1.00 26.46  ? 48  GLN   A O   1 
ATOM   336  C  CB  . GLN   A 1 42  ? 32.971 -0.404  10.347 1.00 29.09  ? 48  GLN   A CB  1 
ATOM   337  C  CG  . GLN   A 1 42  ? 33.837 0.261   9.280  1.00 33.11  ? 48  GLN   A CG  1 
ATOM   338  C  CD  . GLN   A 1 42  ? 34.354 -0.754  8.307  1.00 39.07  ? 48  GLN   A CD  1 
ATOM   339  O  OE1 . GLN   A 1 42  ? 35.161 -1.611  8.660  1.00 39.65  ? 48  GLN   A OE1 1 
ATOM   340  N  NE2 . GLN   A 1 42  ? 33.887 -0.677  7.066  1.00 41.67  ? 48  GLN   A NE2 1 
ATOM   341  N  N   . GLY   A 1 43  ? 30.253 0.313   11.993 1.00 22.94  ? 49  GLY   A N   1 
ATOM   342  C  CA  . GLY   A 1 43  ? 29.062 -0.147  12.693 1.00 23.07  ? 49  GLY   A CA  1 
ATOM   343  C  C   . GLY   A 1 43  ? 28.450 -1.394  12.112 1.00 21.59  ? 49  GLY   A C   1 
ATOM   344  O  O   . GLY   A 1 43  ? 28.735 -1.753  10.976 1.00 21.95  ? 49  GLY   A O   1 
ATOM   345  N  N   . CYS   A 1 44  ? 27.504 -2.001  12.871 1.00 20.42  ? 50  CYS   A N   1 
ATOM   346  C  CA  . CYS   A 1 44  ? 26.878 -3.299  12.541 1.00 21.23  ? 50  CYS   A CA  1 
ATOM   347  C  C   . CYS   A 1 44  ? 25.428 -3.237  12.095 1.00 20.45  ? 50  CYS   A C   1 
ATOM   348  O  O   . CYS   A 1 44  ? 24.854 -4.279  11.778 1.00 21.50  ? 50  CYS   A O   1 
ATOM   349  C  CB  . CYS   A 1 44  ? 27.015 -4.247  13.727 1.00 22.73  ? 50  CYS   A CB  1 
ATOM   350  S  SG  . CYS   A 1 44  ? 28.732 -4.633  14.160 1.00 28.81  ? 50  CYS   A SG  1 
ATOM   351  N  N   . ASP   A 1 45  ? 24.784 -2.081  12.246 1.00 18.05  ? 51  ASP   A N   1 
ATOM   352  C  CA  . ASP   A 1 45  ? 23.388 -1.996  11.841 1.00 17.40  ? 51  ASP   A CA  1 
ATOM   353  C  C   . ASP   A 1 45  ? 23.285 -1.973  10.306 1.00 19.46  ? 51  ASP   A C   1 
ATOM   354  O  O   . ASP   A 1 45  ? 24.141 -1.383  9.641  1.00 21.07  ? 51  ASP   A O   1 
ATOM   355  C  CB  . ASP   A 1 45  ? 22.746 -0.748  12.456 1.00 16.30  ? 51  ASP   A CB  1 
ATOM   356  C  CG  . ASP   A 1 45  ? 22.668 -0.783  13.979 1.00 17.79  ? 51  ASP   A CG  1 
ATOM   357  O  OD1 . ASP   A 1 45  ? 22.289 -1.873  14.546 1.00 19.43  ? 51  ASP   A OD1 1 
ATOM   358  O  OD2 . ASP   A 1 45  ? 22.910 0.267   14.610 1.00 17.96  ? 51  ASP   A OD2 1 
ATOM   359  N  N   . THR   A 1 46  ? 22.246 -2.540  9.773  1.00 20.42  ? 52  THR   A N   1 
ATOM   360  C  CA  . THR   A 1 46  ? 21.922 -2.537  8.334  1.00 21.21  ? 52  THR   A CA  1 
ATOM   361  C  C   . THR   A 1 46  ? 20.610 -1.724  8.202  1.00 20.10  ? 52  THR   A C   1 
ATOM   362  O  O   . THR   A 1 46  ? 19.700 -1.891  9.019  1.00 21.72  ? 52  THR   A O   1 
ATOM   363  C  CB  . THR   A 1 46  ? 21.664 -3.970  7.890  1.00 27.20  ? 52  THR   A CB  1 
ATOM   364  O  OG1 . THR   A 1 46  ? 22.941 -4.651  7.881  1.00 31.08  ? 52  THR   A OG1 1 
ATOM   365  C  CG2 . THR   A 1 46  ? 20.973 -4.066  6.527  1.00 29.40  ? 52  THR   A CG2 1 
ATOM   366  N  N   . ILE   A 1 47  ? 20.524 -0.833  7.204  1.00 18.53  ? 53  ILE   A N   1 
ATOM   367  C  CA  . ILE   A 1 47  ? 19.319 -0.050  7.009  1.00 17.18  ? 53  ILE   A CA  1 
ATOM   368  C  C   . ILE   A 1 47  ? 18.328 -0.804  6.123  1.00 18.03  ? 53  ILE   A C   1 
ATOM   369  O  O   . ILE   A 1 47  ? 18.693 -1.302  5.056  1.00 19.12  ? 53  ILE   A O   1 
ATOM   370  C  CB  . ILE   A 1 47  ? 19.662 1.322   6.377  1.00 16.76  ? 53  ILE   A CB  1 
ATOM   371  C  CG1 . ILE   A 1 47  ? 20.791 2.056   7.139  1.00 18.17  ? 53  ILE   A CG1 1 
ATOM   372  C  CG2 . ILE   A 1 47  ? 18.387 2.230   6.254  1.00 16.52  ? 53  ILE   A CG2 1 
ATOM   373  C  CD1 . ILE   A 1 47  ? 20.445 2.369   8.638  1.00 17.34  ? 53  ILE   A CD1 1 
ATOM   374  N  N   . ALA   A 1 48  ? 17.054 -0.835  6.506  1.00 16.29  ? 54  ALA   A N   1 
ATOM   375  C  CA  . ALA   A 1 48  ? 15.992 -1.414  5.694  1.00 16.41  ? 54  ALA   A CA  1 
ATOM   376  C  C   . ALA   A 1 48  ? 15.733 -0.561  4.429  1.00 17.12  ? 54  ALA   A C   1 
ATOM   377  O  O   . ALA   A 1 48  ? 15.729 0.687   4.463  1.00 17.22  ? 54  ALA   A O   1 
ATOM   378  C  CB  . ALA   A 1 48  ? 14.709 -1.468  6.503  1.00 16.28  ? 54  ALA   A CB  1 
ATOM   379  N  N   . ARG   A 1 49  ? 15.494 -1.242  3.297  1.00 18.64  ? 55  ARG   A N   1 
ATOM   380  C  CA  . ARG   A 1 49  ? 15.149 -0.537  2.062  1.00 19.78  ? 55  ARG   A CA  1 
ATOM   381  C  C   . ARG   A 1 49  ? 13.858 -1.220  1.597  1.00 22.45  ? 55  ARG   A C   1 
ATOM   382  O  O   . ARG   A 1 49  ? 13.912 -2.211  0.839  1.00 24.00  ? 55  ARG   A O   1 
ATOM   383  C  CB  . ARG   A 1 49  ? 16.303 -0.659  1.042  1.00 20.51  ? 55  ARG   A CB  1 
ATOM   384  C  CG  . ARG   A 1 49  ? 17.658 -0.080  1.512  1.00 21.02  ? 55  ARG   A CG  1 
ATOM   385  C  CD  . ARG   A 1 49  ? 17.669 1.413   1.854  1.00 20.17  ? 55  ARG   A CD  1 
ATOM   386  N  NE  . ARG   A 1 49  ? 19.004 1.864   2.300  1.00 19.91  ? 55  ARG   A NE  1 
ATOM   387  C  CZ  . ARG   A 1 49  ? 19.222 3.021   2.927  1.00 20.08  ? 55  ARG   A CZ  1 
ATOM   388  N  NH1 . ARG   A 1 49  ? 18.232 3.890   3.105  1.00 18.69  ? 55  ARG   A NH1 1 
ATOM   389  N  NH2 . ARG   A 1 49  ? 20.440 3.330   3.368  1.00 21.34  ? 55  ARG   A NH2 1 
ATOM   390  N  N   . CYS   A 1 50  ? 12.718 -0.647  2.012  1.00 22.21  ? 56  CYS   A N   1 
ATOM   391  C  CA  . CYS   A 1 50  ? 11.357 -1.234  1.906  1.00 22.41  ? 56  CYS   A CA  1 
ATOM   392  C  C   . CYS   A 1 50  ? 10.215 -0.243  2.215  1.00 23.79  ? 56  CYS   A C   1 
ATOM   393  O  O   . CYS   A 1 50  ? 10.426 0.875   2.627  1.00 25.95  ? 56  CYS   A O   1 
ATOM   394  C  CB  . CYS   A 1 50  ? 11.294 -2.408  2.866  1.00 22.34  ? 56  CYS   A CB  1 
ATOM   395  S  SG  . CYS   A 1 50  ? 11.302 -1.911  4.615  1.00 22.21  ? 56  CYS   A SG  1 
ATOM   396  N  N   . ASP   A 1 51  ? 8.924  -0.735  2.103  1.00 27.00  ? 57  ASP   A N   1 
ATOM   397  C  CA  . ASP   A 1 51  ? 7.758  0.068   2.496  1.00 28.87  ? 57  ASP   A CA  1 
ATOM   398  C  C   . ASP   A 1 51  ? 7.003  -0.664  3.606  1.00 28.03  ? 57  ASP   A C   1 
ATOM   399  O  O   . ASP   A 1 51  ? 5.775  -0.490  3.728  1.00 28.89  ? 57  ASP   A O   1 
ATOM   400  C  CB  . ASP   A 1 51  ? 6.794  0.352   1.309  1.00 33.37  ? 57  ASP   A CB  1 
ATOM   401  C  CG  . ASP   A 1 51  ? 6.253  -0.889  0.635  1.00 41.36  ? 57  ASP   A CG  1 
ATOM   402  O  OD1 . ASP   A 1 51  ? 6.658  -2.019  1.036  1.00 42.72  ? 57  ASP   A OD1 1 
ATOM   403  O  OD2 . ASP   A 1 51  ? 5.434  -0.743  -0.310 1.00 45.92  ? 57  ASP   A OD2 1 
ATOM   404  N  N   . CYS   A 1 52  ? 7.714  -1.419  4.497  1.00 24.64  ? 58  CYS   A N   1 
ATOM   405  C  CA  . CYS   A 1 52  ? 7.043  -2.105  5.626  1.00 22.03  ? 58  CYS   A CA  1 
ATOM   406  C  C   . CYS   A 1 52  ? 6.294  -1.071  6.477  1.00 22.60  ? 58  CYS   A C   1 
ATOM   407  O  O   . CYS   A 1 52  ? 6.721  0.089   6.655  1.00 22.94  ? 58  CYS   A O   1 
ATOM   408  C  CB  . CYS   A 1 52  ? 8.051  -2.856  6.498  1.00 21.72  ? 58  CYS   A CB  1 
ATOM   409  S  SG  . CYS   A 1 52  ? 8.769  -4.391  5.806  1.00 23.18  ? 58  CYS   A SG  1 
ATOM   410  N  N   . GLN   A 1 53  ? 5.155  -1.501  6.991  1.00 19.94  ? 59  GLN   A N   1 
ATOM   411  C  CA  . GLN   A 1 53  ? 4.377  -0.713  7.938  1.00 19.65  ? 59  GLN   A CA  1 
ATOM   412  C  C   . GLN   A 1 53  ? 4.174  -1.513  9.228  1.00 17.12  ? 59  GLN   A C   1 
ATOM   413  O  O   . GLN   A 1 53  ? 3.348  -1.134  10.027 1.00 17.73  ? 59  GLN   A O   1 
ATOM   414  C  CB  . GLN   A 1 53  ? 3.016  -0.247  7.371  1.00 23.07  ? 59  GLN   A CB  1 
ATOM   415  C  CG  . GLN   A 1 53  ? 3.093  0.940   6.444  1.00 25.75  ? 59  GLN   A CG  1 
ATOM   416  C  CD  . GLN   A 1 53  ? 1.703  1.433   6.063  1.00 30.58  ? 59  GLN   A CD  1 
ATOM   417  O  OE1 . GLN   A 1 53  ? 1.206  1.205   4.943  1.00 32.95  ? 59  GLN   A OE1 1 
ATOM   418  N  NE2 . GLN   A 1 53  ? 1.014  2.098   6.980  1.00 27.21  ? 59  GLN   A NE2 1 
ATOM   419  N  N   . THR   A 1 54  ? 4.915  -2.613  9.425  1.00 16.22  ? 60  THR   A N   1 
ATOM   420  C  CA  . THR   A 1 54  ? 4.915  -3.336  10.710 1.00 16.42  ? 60  THR   A CA  1 
ATOM   421  C  C   . THR   A 1 54  ? 6.367  -3.620  11.105 1.00 15.90  ? 60  THR   A C   1 
ATOM   422  O  O   . THR   A 1 54  ? 7.239  -3.839  10.247 1.00 18.50  ? 60  THR   A O   1 
ATOM   423  C  CB  . THR   A 1 54  ? 4.128  -4.630  10.692 1.00 18.57  ? 60  THR   A CB  1 
ATOM   424  O  OG1 . THR   A 1 54  ? 4.730  -5.541  9.809  1.00 24.73  ? 60  THR   A OG1 1 
ATOM   425  C  CG2 . THR   A 1 54  ? 2.670  -4.436  10.311 1.00 19.33  ? 60  THR   A CG2 1 
ATOM   426  N  N   . GLY   A 1 55  ? 6.625  -3.537  12.407 1.00 14.60  ? 61  GLY   A N   1 
ATOM   427  C  CA  . GLY   A 1 55  ? 7.985  -3.729  12.884 1.00 13.98  ? 61  GLY   A CA  1 
ATOM   428  C  C   . GLY   A 1 55  ? 8.019  -3.779  14.394 1.00 13.83  ? 61  GLY   A C   1 
ATOM   429  O  O   . GLY   A 1 55  ? 6.988  -4.027  15.005 1.00 14.17  ? 61  GLY   A O   1 
ATOM   430  N  N   . VAL   A 1 56  ? 9.193  -3.560  14.978 1.00 12.38  ? 62  VAL   A N   1 
ATOM   431  C  CA  . VAL   A 1 56  ? 9.371  -3.637  16.421 1.00 12.48  ? 62  VAL   A CA  1 
ATOM   432  C  C   . VAL   A 1 56  ? 10.236 -2.473  16.834 1.00 12.25  ? 62  VAL   A C   1 
ATOM   433  O  O   . VAL   A 1 56  ? 11.214 -2.155  16.158 1.00 13.66  ? 62  VAL   A O   1 
ATOM   434  C  CB  . VAL   A 1 56  ? 10.052 -4.989  16.742 1.00 15.25  ? 62  VAL   A CB  1 
ATOM   435  C  CG1 . VAL   A 1 56  ? 10.405 -5.090  18.210 1.00 16.57  ? 62  VAL   A CG1 1 
ATOM   436  C  CG2 . VAL   A 1 56  ? 9.155  -6.170  16.374 1.00 15.06  ? 62  VAL   A CG2 1 
ATOM   437  N  N   . TYR   A 1 57  ? 9.876  -1.792  17.945 1.00 11.87  ? 63  TYR   A N   1 
ATOM   438  C  CA  . TYR   A 1 57  ? 10.741 -0.700  18.437 1.00 12.47  ? 63  TYR   A CA  1 
ATOM   439  C  C   . TYR   A 1 57  ? 11.189 -0.896  19.878 1.00 12.60  ? 63  TYR   A C   1 
ATOM   440  O  O   . TYR   A 1 57  ? 10.501 -1.542  20.641 1.00 13.72  ? 63  TYR   A O   1 
ATOM   441  C  CB  . TYR   A 1 57  ? 10.086 0.714   18.283 1.00 12.50  ? 63  TYR   A CB  1 
ATOM   442  C  CG  . TYR   A 1 57  ? 9.118  1.134   19.385 1.00 12.50  ? 63  TYR   A CG  1 
ATOM   443  C  CD1 . TYR   A 1 57  ? 7.828  0.615   19.438 1.00 14.29  ? 63  TYR   A CD1 1 
ATOM   444  C  CD2 . TYR   A 1 57  ? 9.494  2.036   20.378 1.00 13.72  ? 63  TYR   A CD2 1 
ATOM   445  C  CE1 . TYR   A 1 57  ? 6.943  0.983   20.433 1.00 14.50  ? 63  TYR   A CE1 1 
ATOM   446  C  CE2 . TYR   A 1 57  ? 8.593  2.439   21.361 1.00 14.16  ? 63  TYR   A CE2 1 
ATOM   447  C  CZ  . TYR   A 1 57  ? 7.323  1.903   21.391 1.00 15.02  ? 63  TYR   A CZ  1 
ATOM   448  O  OH  . TYR   A 1 57  ? 6.427  2.241   22.397 1.00 16.45  ? 63  TYR   A OH  1 
ATOM   449  N  N   . TYR   A 1 58  ? 12.347 -0.327  20.228 1.00 12.24  ? 64  TYR   A N   1 
ATOM   450  C  CA  . TYR   A 1 58  ? 12.820 -0.357  21.627 1.00 12.81  ? 64  TYR   A CA  1 
ATOM   451  C  C   . TYR   A 1 58  ? 12.370 0.855   22.414 1.00 12.93  ? 64  TYR   A C   1 
ATOM   452  O  O   . TYR   A 1 58  ? 12.611 1.995   22.020 1.00 13.27  ? 64  TYR   A O   1 
ATOM   453  C  CB  . TYR   A 1 58  ? 14.359 -0.463  21.680 1.00 14.10  ? 64  TYR   A CB  1 
ATOM   454  C  CG  . TYR   A 1 58  ? 14.826 -0.615  23.099 1.00 14.84  ? 64  TYR   A CG  1 
ATOM   455  C  CD1 . TYR   A 1 58  ? 14.506 -1.737  23.821 1.00 15.18  ? 64  TYR   A CD1 1 
ATOM   456  C  CD2 . TYR   A 1 58  ? 15.605 0.365   23.706 1.00 14.71  ? 64  TYR   A CD2 1 
ATOM   457  C  CE1 . TYR   A 1 58  ? 14.897 -1.866  25.150 1.00 16.50  ? 64  TYR   A CE1 1 
ATOM   458  C  CE2 . TYR   A 1 58  ? 15.989 0.257   25.037 1.00 15.93  ? 64  TYR   A CE2 1 
ATOM   459  C  CZ  . TYR   A 1 58  ? 15.679 -0.888  25.729 1.00 17.80  ? 64  TYR   A CZ  1 
ATOM   460  O  OH  . TYR   A 1 58  ? 16.024 -0.988  27.071 1.00 18.96  ? 64  TYR   A OH  1 
ATOM   461  N  N   . CYS   A 1 59  ? 11.741 0.573   23.549 1.00 13.04  ? 65  CYS   A N   1 
ATOM   462  C  CA  . CYS   A 1 59  ? 11.249 1.557   24.520 1.00 13.18  ? 65  CYS   A CA  1 
ATOM   463  C  C   . CYS   A 1 59  ? 12.087 1.514   25.799 1.00 14.81  ? 65  CYS   A C   1 
ATOM   464  O  O   . CYS   A 1 59  ? 11.882 0.587   26.634 1.00 14.73  ? 65  CYS   A O   1 
ATOM   465  C  CB  . CYS   A 1 59  ? 9.785  1.264   24.809 1.00 13.03  ? 65  CYS   A CB  1 
ATOM   466  S  SG  . CYS   A 1 59  ? 9.051  2.409   26.017 1.00 15.41  ? 65  CYS   A SG  1 
ATOM   467  N  N   . SER   A 1 60  ? 12.991 2.454   25.978 1.00 14.74  ? 66  SER   A N   1 
ATOM   468  C  CA  . SER   A 1 60  ? 13.888 2.422   27.135 1.00 15.66  ? 66  SER   A CA  1 
ATOM   469  C  C   . SER   A 1 60  ? 13.165 2.584   28.478 1.00 16.44  ? 66  SER   A C   1 
ATOM   470  O  O   . SER   A 1 60  ? 13.551 1.959   29.466 1.00 17.32  ? 66  SER   A O   1 
ATOM   471  C  CB  . SER   A 1 60  ? 15.015 3.446   26.973 1.00 16.81  ? 66  SER   A CB  1 
ATOM   472  O  OG  . SER   A 1 60  ? 14.601 4.796   27.114 1.00 19.96  ? 66  SER   A OG  1 
ATOM   473  N  N   . SER   A 1 61  ? 12.045 3.351   28.489 1.00 15.33  ? 67  SER   A N   1 
ATOM   474  C  CA  . SER   A 1 61  ? 11.258 3.562   29.711 1.00 16.50  ? 67  SER   A CA  1 
ATOM   475  C  C   . SER   A 1 61  ? 10.456 2.357   30.140 1.00 16.86  ? 67  SER   A C   1 
ATOM   476  O  O   . SER   A 1 61  ? 9.853  2.397   31.188 1.00 17.59  ? 67  SER   A O   1 
ATOM   477  C  CB  . SER   A 1 61  ? 10.366 4.795   29.607 1.00 17.51  ? 67  SER   A CB  1 
ATOM   478  O  OG  . SER   A 1 61  ? 9.390  4.645   28.599 1.00 15.99  ? 67  SER   A OG  1 
ATOM   479  N  N   . ARG   A 1 62  ? 10.477 1.272   29.339 1.00 15.74  ? 68  ARG   A N   1 
ATOM   480  C  CA  . ARG   A 1 62  ? 9.862  -0.007  29.720 1.00 15.76  ? 68  ARG   A CA  1 
ATOM   481  C  C   . ARG   A 1 62  ? 10.871 -1.152  29.642 1.00 16.81  ? 68  ARG   A C   1 
ATOM   482  O  O   . ARG   A 1 62  ? 10.497 -2.320  29.887 1.00 17.31  ? 68  ARG   A O   1 
ATOM   483  C  CB  . ARG   A 1 62  ? 8.673  -0.302  28.781 1.00 16.21  ? 68  ARG   A CB  1 
ATOM   484  C  CG  . ARG   A 1 62  ? 7.511  0.697   28.907 1.00 18.04  ? 68  ARG   A CG  1 
ATOM   485  C  CD  . ARG   A 1 62  ? 6.752  0.412   30.188 1.00 16.77  ? 68  ARG   A CD  1 
ATOM   486  N  NE  . ARG   A 1 62  ? 5.616  1.320   30.355 1.00 19.60  ? 68  ARG   A NE  1 
ATOM   487  C  CZ  . ARG   A 1 62  ? 5.673  2.486   30.985 1.00 19.39  ? 68  ARG   A CZ  1 
ATOM   488  N  NH1 . ARG   A 1 62  ? 6.826  2.911   31.520 1.00 20.56  ? 68  ARG   A NH1 1 
ATOM   489  N  NH2 . ARG   A 1 62  ? 4.575  3.233   31.114 1.00 22.25  ? 68  ARG   A NH2 1 
ATOM   490  N  N   . ARG   A 1 63  ? 12.126 -0.893  29.211 1.00 16.93  ? 69  ARG   A N   1 
ATOM   491  C  CA  . ARG   A 1 63  ? 13.104 -1.982  28.911 1.00 18.05  ? 69  ARG   A CA  1 
ATOM   492  C  C   . ARG   A 1 63  ? 12.493 -3.098  28.050 1.00 19.90  ? 69  ARG   A C   1 
ATOM   493  O  O   . ARG   A 1 63  ? 12.695 -4.302  28.297 1.00 21.87  ? 69  ARG   A O   1 
ATOM   494  C  CB  . ARG   A 1 63  ? 13.650 -2.613  30.198 1.00 20.87  ? 69  ARG   A CB  1 
ATOM   495  C  CG  . ARG   A 1 63  ? 14.664 -1.754  30.812 1.00 21.95  ? 69  ARG   A CG  1 
ATOM   496  C  CD  . ARG   A 1 63  ? 15.441 -2.568  31.826 1.00 22.53  ? 69  ARG   A CD  1 
ATOM   497  N  NE  . ARG   A 1 63  ? 16.239 -1.647  32.614 1.00 24.85  ? 69  ARG   A NE  1 
ATOM   498  C  CZ  . ARG   A 1 63  ? 15.953 -1.272  33.859 1.00 25.62  ? 69  ARG   A CZ  1 
ATOM   499  N  NH1 . ARG   A 1 63  ? 14.882 -1.766  34.485 1.00 23.98  ? 69  ARG   A NH1 1 
ATOM   500  N  NH2 . ARG   A 1 63  ? 16.731 -0.409  34.488 1.00 25.67  ? 69  ARG   A NH2 1 
ATOM   501  N  N   . LYS   A 1 64  ? 11.746 -2.714  27.046 1.00 17.52  ? 70  LYS   A N   1 
ATOM   502  C  CA  . LYS   A 1 64  ? 11.037 -3.699  26.229 1.00 18.47  ? 70  LYS   A CA  1 
ATOM   503  C  C   . LYS   A 1 64  ? 11.016 -3.299  24.783 1.00 16.92  ? 70  LYS   A C   1 
ATOM   504  O  O   . LYS   A 1 64  ? 10.961 -2.107  24.450 1.00 16.01  ? 70  LYS   A O   1 
ATOM   505  C  CB  . LYS   A 1 64  ? 9.579  -3.770  26.726 1.00 20.12  ? 70  LYS   A CB  1 
ATOM   506  C  CG  . LYS   A 1 64  ? 9.388  -4.770  27.888 1.00 27.56  ? 70  LYS   A CG  1 
ATOM   507  C  CD  . LYS   A 1 64  ? 7.929  -5.125  28.117 1.00 35.94  ? 70  LYS   A CD  1 
ATOM   508  C  CE  . LYS   A 1 64  ? 7.753  -5.778  29.474 1.00 42.60  ? 70  LYS   A CE  1 
ATOM   509  N  NZ  . LYS   A 1 64  ? 8.217  -4.876  30.572 1.00 47.12  ? 70  LYS   A NZ  1 
ATOM   510  N  N   . HIS   A 1 65  ? 10.992 -4.290  23.920 1.00 15.63  ? 71  HIS   A N   1 
ATOM   511  C  CA  . HIS   A 1 65  ? 10.763 -4.128  22.487 1.00 15.16  ? 71  HIS   A CA  1 
ATOM   512  C  C   . HIS   A 1 65  ? 9.284  -4.469  22.216 1.00 17.02  ? 71  HIS   A C   1 
ATOM   513  O  O   . HIS   A 1 65  ? 8.782  -5.516  22.662 1.00 19.73  ? 71  HIS   A O   1 
ATOM   514  C  CB  . HIS   A 1 65  ? 11.654 -5.082  21.670 1.00 13.62  ? 71  HIS   A CB  1 
ATOM   515  C  CG  . HIS   A 1 65  ? 13.113 -4.795  21.768 1.00 15.42  ? 71  HIS   A CG  1 
ATOM   516  N  ND1 . HIS   A 1 65  ? 13.804 -4.096  20.792 1.00 19.22  ? 71  HIS   A ND1 1 
ATOM   517  C  CD2 . HIS   A 1 65  ? 13.973 -5.112  22.768 1.00 16.12  ? 71  HIS   A CD2 1 
ATOM   518  C  CE1 . HIS   A 1 65  ? 15.079 -4.061  21.204 1.00 16.77  ? 71  HIS   A CE1 1 
ATOM   519  N  NE2 . HIS   A 1 65  ? 15.215 -4.649  22.377 1.00 18.91  ? 71  HIS   A NE2 1 
ATOM   520  N  N   . TYR   A 1 66  ? 8.575  -3.573  21.491 1.00 14.89  ? 72  TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 66  ? 7.140  -3.757  21.247 1.00 13.85  ? 72  TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 66  ? 6.893  -3.875  19.762 1.00 13.54  ? 72  TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 66  ? 7.379  -3.044  18.989 1.00 13.52  ? 72  TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 66  ? 6.355  -2.481  21.695 1.00 14.69  ? 72  TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 66  ? 6.270  -2.291  23.186 1.00 15.88  ? 72  TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 66  ? 5.357  -3.010  23.945 1.00 16.27  ? 72  TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 66  ? 7.047  -1.345  23.824 1.00 16.01  ? 72  TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 66  ? 5.287  -2.853  25.325 1.00 17.63  ? 72  TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 66  ? 6.985  -1.175  25.203 1.00 17.26  ? 72  TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 66  ? 6.090  -1.925  25.945 1.00 17.78  ? 72  TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 66  ? 5.981  -1.728  27.317 1.00 19.98  ? 72  TYR   A OH  1 
ATOM   532  N  N   . PRO   A 1 67  ? 6.082  -4.852  19.351 1.00 13.34  ? 73  PRO   A N   1 
ATOM   533  C  CA  . PRO   A 1 67  ? 5.666  -4.914  17.937 1.00 13.53  ? 73  PRO   A CA  1 
ATOM   534  C  C   . PRO   A 1 67  ? 4.606  -3.826  17.661 1.00 14.66  ? 73  PRO   A C   1 
ATOM   535  O  O   . PRO   A 1 67  ? 3.663  -3.632  18.462 1.00 16.35  ? 73  PRO   A O   1 
ATOM   536  C  CB  . PRO   A 1 67  ? 5.031  -6.317  17.802 1.00 15.92  ? 73  PRO   A CB  1 
ATOM   537  C  CG  . PRO   A 1 67  ? 4.693  -6.745  19.177 1.00 17.26  ? 73  PRO   A CG  1 
ATOM   538  C  CD  . PRO   A 1 67  ? 5.513  -5.945  20.171 1.00 14.17  ? 73  PRO   A CD  1 
ATOM   539  N  N   . VAL   A 1 68  ? 4.756  -3.150  16.535 1.00 13.12  ? 74  VAL   A N   1 
ATOM   540  C  CA  . VAL   A 1 68  ? 3.824  -2.048  16.205 1.00 14.84  ? 74  VAL   A CA  1 
ATOM   541  C  C   . VAL   A 1 68  ? 3.527  -2.017  14.724 1.00 14.48  ? 74  VAL   A C   1 
ATOM   542  O  O   . VAL   A 1 68  ? 4.312  -2.388  13.877 1.00 15.25  ? 74  VAL   A O   1 
ATOM   543  C  CB  . VAL   A 1 68  ? 4.377  -0.654  16.595 1.00 16.77  ? 74  VAL   A CB  1 
ATOM   544  C  CG1 . VAL   A 1 68  ? 4.334  -0.465  18.109 1.00 17.74  ? 74  VAL   A CG1 1 
ATOM   545  C  CG2 . VAL   A 1 68  ? 5.782  -0.434  16.056 1.00 17.91  ? 74  VAL   A CG2 1 
ATOM   546  N  N   . SER   A 1 69  ? 2.341  -1.474  14.400 1.00 14.53  ? 75  SER   A N   1 
ATOM   547  C  CA  . SER   A 1 69  ? 1.959  -1.046  13.064 1.00 14.35  ? 75  SER   A CA  1 
ATOM   548  C  C   . SER   A 1 69  ? 2.187  0.464   13.005 1.00 14.38  ? 75  SER   A C   1 
ATOM   549  O  O   . SER   A 1 69  ? 1.858  1.165   13.987 1.00 15.76  ? 75  SER   A O   1 
ATOM   550  C  CB  . SER   A 1 69  ? 0.468  -1.286  12.850 1.00 17.55  ? 75  SER   A CB  1 
ATOM   551  O  OG  . SER   A 1 69  ? 0.254  -2.683  12.863 1.00 25.17  ? 75  SER   A OG  1 
ATOM   552  N  N   . PHE   A 1 70  ? 2.787  0.972   11.918 1.00 14.99  ? 76  PHE   A N   1 
ATOM   553  C  CA  . PHE   A 1 70  ? 3.112  2.386   11.857 1.00 15.50  ? 76  PHE   A CA  1 
ATOM   554  C  C   . PHE   A 1 70  ? 2.726  2.973   10.533 1.00 16.19  ? 76  PHE   A C   1 
ATOM   555  O  O   . PHE   A 1 70  ? 2.645  2.256   9.510  1.00 17.73  ? 76  PHE   A O   1 
ATOM   556  C  CB  . PHE   A 1 70  ? 4.609  2.617   12.215 1.00 16.08  ? 76  PHE   A CB  1 
ATOM   557  C  CG  . PHE   A 1 70  ? 5.636  1.828   11.417 1.00 15.21  ? 76  PHE   A CG  1 
ATOM   558  C  CD1 . PHE   A 1 70  ? 6.049  0.569   11.830 1.00 14.83  ? 76  PHE   A CD1 1 
ATOM   559  C  CD2 . PHE   A 1 70  ? 6.198  2.359   10.257 1.00 15.62  ? 76  PHE   A CD2 1 
ATOM   560  C  CE1 . PHE   A 1 70  ? 6.969  -0.165  11.063 1.00 15.76  ? 76  PHE   A CE1 1 
ATOM   561  C  CE2 . PHE   A 1 70  ? 7.135  1.616   9.507  1.00 16.46  ? 76  PHE   A CE2 1 
ATOM   562  C  CZ  . PHE   A 1 70  ? 7.495  0.368   9.917  1.00 15.85  ? 76  PHE   A CZ  1 
ATOM   563  N  N   . SER   A 1 71  ? 2.507  4.290   10.510 1.00 16.57  ? 77  SER   A N   1 
ATOM   564  C  CA  . SER   A 1 71  ? 2.082  4.962   9.278  1.00 17.92  ? 77  SER   A CA  1 
ATOM   565  C  C   . SER   A 1 71  ? 3.238  5.201   8.302  1.00 18.35  ? 77  SER   A C   1 
ATOM   566  O  O   . SER   A 1 71  ? 4.411  5.034   8.665  1.00 18.13  ? 77  SER   A O   1 
ATOM   567  C  CB  . SER   A 1 71  ? 1.345  6.264   9.621  1.00 19.87  ? 77  SER   A CB  1 
ATOM   568  O  OG  . SER   A 1 71  ? 2.188  7.186   10.305 1.00 20.49  ? 77  SER   A OG  1 
ATOM   569  N  N   . LYS   A 1 72  ? 2.921  5.534   7.060  1.00 18.98  ? 78  LYS   A N   1 
ATOM   570  C  CA  . LYS   A 1 72  ? 3.973  5.841   6.087  1.00 18.62  ? 78  LYS   A CA  1 
ATOM   571  C  C   . LYS   A 1 72  ? 4.601  7.213   6.417  1.00 19.95  ? 78  LYS   A C   1 
ATOM   572  O  O   . LYS   A 1 72  ? 3.923  8.066   6.992  1.00 20.24  ? 78  LYS   A O   1 
ATOM   573  C  CB  . LYS   A 1 72  ? 3.373  5.825   4.666  1.00 20.93  ? 78  LYS   A CB  1 
ATOM   574  C  CG  . LYS   A 1 72  ? 2.942  4.441   4.263  1.00 23.92  ? 78  LYS   A CG  1 
ATOM   575  C  CD  . LYS   A 1 72  ? 2.670  4.335   2.754  1.00 27.69  ? 78  LYS   A CD  1 
ATOM   576  C  CE  . LYS   A 1 72  ? 2.381  2.888   2.385  1.00 34.50  ? 78  LYS   A CE  1 
ATOM   577  N  NZ  . LYS   A 1 72  ? 2.374  2.678   0.903  1.00 39.08  ? 78  LYS   A NZ  1 
ATOM   578  N  N   . PRO   A 1 73  ? 5.878  7.445   6.090  1.00 19.05  ? 79  PRO   A N   1 
ATOM   579  C  CA  . PRO   A 1 73  ? 6.506  8.733   6.433  1.00 19.20  ? 79  PRO   A CA  1 
ATOM   580  C  C   . PRO   A 1 73  ? 5.713  9.927   5.869  1.00 20.82  ? 79  PRO   A C   1 
ATOM   581  O  O   . PRO   A 1 73  ? 5.383  9.961   4.682  1.00 22.92  ? 79  PRO   A O   1 
ATOM   582  C  CB  . PRO   A 1 73  ? 7.929  8.618   5.859  1.00 20.52  ? 79  PRO   A CB  1 
ATOM   583  C  CG  . PRO   A 1 73  ? 8.138  7.179   5.577  1.00 23.09  ? 79  PRO   A CG  1 
ATOM   584  C  CD  . PRO   A 1 73  ? 6.818  6.507   5.433  1.00 19.79  ? 79  PRO   A CD  1 
ATOM   585  N  N   . SER   A 1 74  ? 5.429  10.900  6.724  1.00 20.64  ? 80  SER   A N   1 
ATOM   586  C  CA  . SER   A 1 74  ? 4.577  12.021  6.358  1.00 23.19  ? 80  SER   A CA  1 
ATOM   587  C  C   . SER   A 1 74  ? 4.995  13.313  7.093  1.00 21.40  ? 80  SER   A C   1 
ATOM   588  O  O   . SER   A 1 74  ? 5.822  13.277  8.015  1.00 20.55  ? 80  SER   A O   1 
ATOM   589  C  CB  . SER   A 1 74  ? 3.122  11.695  6.736  1.00 28.60  ? 80  SER   A CB  1 
ATOM   590  O  OG  . SER   A 1 74  ? 2.680  10.443  6.244  1.00 37.46  ? 80  SER   A OG  1 
ATOM   591  N  N   . LEU   A 1 75  ? 4.275  14.429  6.772  1.00 23.66  ? 81  LEU   A N   1 
ATOM   592  C  CA  . LEU   A 1 75  ? 4.465  15.721  7.406  1.00 25.51  ? 81  LEU   A CA  1 
ATOM   593  C  C   . LEU   A 1 75  ? 3.347  15.818  8.474  1.00 27.01  ? 81  LEU   A C   1 
ATOM   594  O  O   . LEU   A 1 75  ? 2.140  15.840  8.147  1.00 29.39  ? 81  LEU   A O   1 
ATOM   595  C  CB  . LEU   A 1 75  ? 4.294  16.825  6.336  1.00 26.32  ? 81  LEU   A CB  1 
ATOM   596  C  CG  . LEU   A 1 75  ? 4.616  18.256  6.760  1.00 29.27  ? 81  LEU   A CG  1 
ATOM   597  C  CD1 . LEU   A 1 75  ? 6.077  18.437  7.059  1.00 29.98  ? 81  LEU   A CD1 1 
ATOM   598  C  CD2 . LEU   A 1 75  ? 4.233  19.260  5.668  1.00 30.37  ? 81  LEU   A CD2 1 
ATOM   599  N  N   . ILE   A 1 76  ? 3.739  15.613  9.814  1.00 25.79  ? 82  ILE   A N   1 
ATOM   600  C  CA  . ILE   A 1 76  ? 2.851  15.595  11.073 1.00 26.76  ? 82  ILE   A CA  1 
ATOM   601  C  C   . ILE   A 1 76  ? 3.070  16.802  12.011 1.00 27.31  ? 82  ILE   A C   1 
ATOM   602  O  O   . ILE   A 1 76  ? 4.220  17.107  12.361 1.00 26.24  ? 82  ILE   A O   1 
ATOM   603  C  CB  . ILE   A 1 76  ? 2.941  14.362  12.064 1.00 27.82  ? 82  ILE   A CB  1 
ATOM   604  C  CG1 . ILE   A 1 76  ? 3.727  13.199  11.455 1.00 28.08  ? 82  ILE   A CG1 1 
ATOM   605  C  CG2 . ILE   A 1 76  ? 1.565  13.927  12.535 1.00 30.37  ? 82  ILE   A CG2 1 
ATOM   606  C  CD1 . ILE   A 1 76  ? 3.000  12.476  10.346 1.00 27.50  ? 82  ILE   A CD1 1 
ATOM   607  N  N   . PHE   A 1 77  ? 1.941  17.485  12.212 1.00 27.31  ? 83  PHE   A N   1 
ATOM   608  C  CA  . PHE   A 1 77  ? 2.077  18.528  13.237 1.00 27.89  ? 83  PHE   A CA  1 
ATOM   609  C  C   . PHE   A 1 77  ? 2.366  17.853  14.568 1.00 28.32  ? 83  PHE   A C   1 
ATOM   610  O  O   . PHE   A 1 77  ? 1.736  16.889  14.854 1.00 30.10  ? 83  PHE   A O   1 
ATOM   611  C  CB  . PHE   A 1 77  ? 0.844  19.417  13.190 1.00 29.21  ? 83  PHE   A CB  1 
ATOM   612  C  CG  . PHE   A 1 77  ? 1.014  20.634  14.070 1.00 32.45  ? 83  PHE   A CG  1 
ATOM   613  C  CD1 . PHE   A 1 77  ? 1.864  21.663  13.691 1.00 34.83  ? 83  PHE   A CD1 1 
ATOM   614  C  CD2 . PHE   A 1 77  ? 0.345  20.751  15.275 1.00 34.24  ? 83  PHE   A CD2 1 
ATOM   615  C  CE1 . PHE   A 1 77  ? 2.037  22.776  14.498 1.00 36.74  ? 83  PHE   A CE1 1 
ATOM   616  C  CE2 . PHE   A 1 77  ? 0.502  21.876  16.066 1.00 35.21  ? 83  PHE   A CE2 1 
ATOM   617  C  CZ  . PHE   A 1 77  ? 1.352  22.890  15.679 1.00 36.28  ? 83  PHE   A CZ  1 
ATOM   618  N  N   . VAL   A 1 78  ? 3.449  18.264  15.212 1.00 26.73  ? 84  VAL   A N   1 
ATOM   619  C  CA  . VAL   A 1 78  ? 3.884  17.715  16.521 1.00 25.17  ? 84  VAL   A CA  1 
ATOM   620  C  C   . VAL   A 1 78  ? 3.850  18.867  17.556 1.00 25.57  ? 84  VAL   A C   1 
ATOM   621  O  O   . VAL   A 1 78  ? 4.299  19.951  17.169 1.00 26.20  ? 84  VAL   A O   1 
ATOM   622  C  CB  . VAL   A 1 78  ? 5.300  17.094  16.362 1.00 23.62  ? 84  VAL   A CB  1 
ATOM   623  C  CG1 . VAL   A 1 78  ? 5.950  16.783  17.696 1.00 23.93  ? 84  VAL   A CG1 1 
ATOM   624  C  CG2 . VAL   A 1 78  ? 5.324  15.896  15.427 1.00 24.55  ? 84  VAL   A CG2 1 
ATOM   625  N  N   . GLU   A 1 79  ? 3.337  18.553  18.763 1.00 26.06  ? 85  GLU   A N   1 
ATOM   626  C  CA  . GLU   A 1 79  ? 3.122  19.565  19.837 1.00 27.97  ? 85  GLU   A CA  1 
ATOM   627  C  C   . GLU   A 1 79  ? 4.492  19.996  20.374 1.00 27.38  ? 85  GLU   A C   1 
ATOM   628  O  O   . GLU   A 1 79  ? 5.415  19.211  20.354 1.00 27.54  ? 85  GLU   A O   1 
ATOM   629  C  CB  . GLU   A 1 79  ? 2.102  19.018  20.852 1.00 32.31  ? 85  GLU   A CB  1 
ATOM   630  C  CG  . GLU   A 1 79  ? 0.641  19.037  20.375 1.00 41.17  ? 85  GLU   A CG  1 
ATOM   631  C  CD  . GLU   A 1 79  ? 0.002  20.353  19.941 1.00 51.28  ? 85  GLU   A CD  1 
ATOM   632  O  OE1 . GLU   A 1 79  ? 0.141  21.348  20.656 1.00 54.17  ? 85  GLU   A OE1 1 
ATOM   633  O  OE2 . GLU   A 1 79  ? -0.626 20.381  18.873 1.00 54.91  ? 85  GLU   A OE2 1 
ATOM   634  N  N   . ALA   A 1 80  ? 4.556  21.235  20.874 1.00 28.32  ? 86  ALA   A N   1 
ATOM   635  C  CA  . ALA   A 1 80  ? 5.767  21.747  21.509 1.00 28.88  ? 86  ALA   A CA  1 
ATOM   636  C  C   . ALA   A 1 80  ? 6.310  20.857  22.620 1.00 29.94  ? 86  ALA   A C   1 
ATOM   637  O  O   . ALA   A 1 80  ? 5.526  20.245  23.294 1.00 30.94  ? 86  ALA   A O   1 
ATOM   638  C  CB  . ALA   A 1 80  ? 5.528  23.199  21.943 1.00 30.04  ? 86  ALA   A CB  1 
ATOM   639  N  N   . SER   A 1 81  ? 7.631  20.723  22.583 1.00 28.89  ? 87  SER   A N   1 
ATOM   640  C  CA  . SER   A 1 81  ? 8.365  20.001  23.636 1.00 29.06  ? 87  SER   A CA  1 
ATOM   641  C  C   . SER   A 1 81  ? 9.549  20.862  24.154 1.00 29.63  ? 87  SER   A C   1 
ATOM   642  O  O   . SER   A 1 81  ? 9.593  22.053  23.812 1.00 29.48  ? 87  SER   A O   1 
ATOM   643  C  CB  . SER   A 1 81  ? 8.801  18.620  23.046 1.00 29.70  ? 87  SER   A CB  1 
ATOM   644  O  OG  . SER   A 1 81  ? 9.708  18.801  21.968 1.00 29.38  ? 87  SER   A OG  1 
ATOM   645  N  N   . GLU   A 1 82  ? 10.491 20.298  24.910 1.00 29.60  ? 88  GLU   A N   1 
ATOM   646  C  CA  . GLU   A 1 82  ? 11.640 21.061  25.544 1.00 29.45  ? 88  GLU   A CA  1 
ATOM   647  C  C   . GLU   A 1 82  ? 12.663 21.419  24.527 1.00 27.01  ? 88  GLU   A C   1 
ATOM   648  O  O   . GLU   A 1 82  ? 13.513 22.273  24.789 1.00 28.19  ? 88  GLU   A O   1 
ATOM   649  C  CB  . GLU   A 1 82  ? 12.414 20.129  26.465 1.00 34.16  ? 88  GLU   A CB  1 
ATOM   650  C  CG  . GLU   A 1 82  ? 11.811 18.716  26.492 1.00 41.18  ? 88  GLU   A CG  1 
ATOM   651  C  CD  . GLU   A 1 82  ? 11.510 18.013  27.811 1.00 45.39  ? 88  GLU   A CD  1 
ATOM   652  O  OE1 . GLU   A 1 82  ? 10.615 18.497  28.555 1.00 51.68  ? 88  GLU   A OE1 1 
ATOM   653  O  OE2 . GLU   A 1 82  ? 12.130 16.959  28.070 1.00 40.66  ? 88  GLU   A OE2 1 
ATOM   654  N  N   . TYR   A 1 83  ? 12.646 20.682  23.438 1.00 24.93  ? 89  TYR   A N   1 
ATOM   655  C  CA  . TYR   A 1 83  ? 13.734 20.857  22.458 1.00 23.76  ? 89  TYR   A CA  1 
ATOM   656  C  C   . TYR   A 1 83  ? 13.223 21.501  21.185 1.00 23.36  ? 89  TYR   A C   1 
ATOM   657  O  O   . TYR   A 1 83  ? 14.042 21.976  20.392 1.00 23.91  ? 89  TYR   A O   1 
ATOM   658  C  CB  . TYR   A 1 83  ? 14.287 19.480  22.094 1.00 23.85  ? 89  TYR   A CB  1 
ATOM   659  C  CG  . TYR   A 1 83  ? 14.978 18.699  23.164 1.00 25.24  ? 89  TYR   A CG  1 
ATOM   660  C  CD1 . TYR   A 1 83  ? 16.346 18.806  23.307 1.00 27.47  ? 89  TYR   A CD1 1 
ATOM   661  C  CD2 . TYR   A 1 83  ? 14.284 17.807  23.962 1.00 27.01  ? 89  TYR   A CD2 1 
ATOM   662  C  CE1 . TYR   A 1 83  ? 17.014 18.069  24.262 1.00 29.41  ? 89  TYR   A CE1 1 
ATOM   663  C  CE2 . TYR   A 1 83  ? 14.946 17.068  24.927 1.00 29.16  ? 89  TYR   A CE2 1 
ATOM   664  C  CZ  . TYR   A 1 83  ? 16.313 17.198  25.071 1.00 30.81  ? 89  TYR   A CZ  1 
ATOM   665  O  OH  . TYR   A 1 83  ? 16.949 16.465  26.022 1.00 32.70  ? 89  TYR   A OH  1 
ATOM   666  N  N   . TYR   A 1 84  ? 11.910 21.475  20.969 1.00 23.32  ? 90  TYR   A N   1 
ATOM   667  C  CA  . TYR   A 1 84  ? 11.312 22.049  19.742 1.00 23.38  ? 90  TYR   A CA  1 
ATOM   668  C  C   . TYR   A 1 84  ? 10.007 22.803  20.086 1.00 25.25  ? 90  TYR   A C   1 
ATOM   669  O  O   . TYR   A 1 84  ? 9.246  22.415  20.987 1.00 25.36  ? 90  TYR   A O   1 
ATOM   670  C  CB  . TYR   A 1 84  ? 11.033 20.996  18.650 1.00 22.76  ? 90  TYR   A CB  1 
ATOM   671  C  CG  . TYR   A 1 84  ? 12.211 20.321  17.992 1.00 21.09  ? 90  TYR   A CG  1 
ATOM   672  C  CD1 . TYR   A 1 84  ? 13.074 21.012  17.155 1.00 20.94  ? 90  TYR   A CD1 1 
ATOM   673  C  CD2 . TYR   A 1 84  ? 12.436 18.965  18.181 1.00 19.67  ? 90  TYR   A CD2 1 
ATOM   674  C  CE1 . TYR   A 1 84  ? 14.135 20.369  16.533 1.00 19.19  ? 90  TYR   A CE1 1 
ATOM   675  C  CE2 . TYR   A 1 84  ? 13.489 18.314  17.568 1.00 18.42  ? 90  TYR   A CE2 1 
ATOM   676  C  CZ  . TYR   A 1 84  ? 14.346 19.014  16.737 1.00 18.43  ? 90  TYR   A CZ  1 
ATOM   677  O  OH  . TYR   A 1 84  ? 15.403 18.361  16.157 1.00 19.10  ? 90  TYR   A OH  1 
ATOM   678  N  N   . PRO   A 1 85  ? 9.755  23.919  19.366 1.00 26.39  ? 91  PRO   A N   1 
ATOM   679  C  CA  . PRO   A 1 85  ? 8.418  24.538  19.496 1.00 27.27  ? 91  PRO   A CA  1 
ATOM   680  C  C   . PRO   A 1 85  ? 7.394  23.675  18.726 1.00 27.84  ? 91  PRO   A C   1 
ATOM   681  O  O   . PRO   A 1 85  ? 7.794  22.681  18.021 1.00 27.93  ? 91  PRO   A O   1 
ATOM   682  C  CB  . PRO   A 1 85  ? 8.600  25.816  18.670 1.00 29.24  ? 91  PRO   A CB  1 
ATOM   683  C  CG  . PRO   A 1 85  ? 9.616  25.404  17.611 1.00 30.11  ? 91  PRO   A CG  1 
ATOM   684  C  CD  . PRO   A 1 85  ? 10.624 24.577  18.385 1.00 26.73  ? 91  PRO   A CD  1 
ATOM   685  N  N   . ALA   A 1 86  ? 6.119  24.067  18.752 1.00 28.83  ? 92  ALA   A N   1 
ATOM   686  C  CA  . ALA   A 1 86  ? 5.062  23.307  18.022 1.00 29.33  ? 92  ALA   A CA  1 
ATOM   687  C  C   . ALA   A 1 86  ? 5.220  23.574  16.518 1.00 30.32  ? 92  ALA   A C   1 
ATOM   688  O  O   . ALA   A 1 86  ? 5.276  24.713  16.139 1.00 32.13  ? 92  ALA   A O   1 
ATOM   689  C  CB  . ALA   A 1 86  ? 3.669  23.718  18.447 1.00 28.92  ? 92  ALA   A CB  1 
ATOM   690  N  N   . ARG   A 1 87  ? 5.489  22.558  15.702 1.00 29.93  ? 93  ARG   A N   1 
ATOM   691  C  CA  . ARG   A 1 87  ? 5.750  22.711  14.253 1.00 30.00  ? 93  ARG   A CA  1 
ATOM   692  C  C   . ARG   A 1 87  ? 5.331  21.402  13.557 1.00 29.70  ? 93  ARG   A C   1 
ATOM   693  O  O   . ARG   A 1 87  ? 4.955  20.461  14.249 1.00 29.61  ? 93  ARG   A O   1 
ATOM   694  C  CB  . ARG   A 1 87  ? 7.231  23.038  14.011 1.00 30.58  ? 93  ARG   A CB  1 
ATOM   695  C  CG  . ARG   A 1 87  ? 8.133  21.816  13.895 1.00 32.20  ? 93  ARG   A CG  1 
ATOM   696  C  CD  . ARG   A 1 87  ? 9.312  21.614  14.833 1.00 31.12  ? 93  ARG   A CD  1 
ATOM   697  N  NE  . ARG   A 1 87  ? 9.799  20.230  14.737 1.00 29.49  ? 93  ARG   A NE  1 
ATOM   698  C  CZ  . ARG   A 1 87  ? 11.017 19.910  14.356 1.00 31.27  ? 93  ARG   A CZ  1 
ATOM   699  N  NH1 . ARG   A 1 87  ? 11.869 20.872  14.039 1.00 32.66  ? 93  ARG   A NH1 1 
ATOM   700  N  NH2 . ARG   A 1 87  ? 11.386 18.646  14.312 1.00 25.33  ? 93  ARG   A NH2 1 
ATOM   701  N  N   . TYR   A 1 88  ? 5.590  21.321  12.236 1.00 29.82  ? 94  TYR   A N   1 
ATOM   702  C  CA  . TYR   A 1 88  ? 5.150  20.127  11.470 1.00 29.46  ? 94  TYR   A CA  1 
ATOM   703  C  C   . TYR   A 1 88  ? 6.359  19.247  11.150 1.00 25.97  ? 94  TYR   A C   1 
ATOM   704  O  O   . TYR   A 1 88  ? 6.902  19.397  10.039 1.00 26.76  ? 94  TYR   A O   1 
ATOM   705  C  CB  . TYR   A 1 88  ? 4.489  20.566  10.163 1.00 31.44  ? 94  TYR   A CB  1 
ATOM   706  C  CG  . TYR   A 1 88  ? 3.051  20.152  9.992  1.00 33.09  ? 94  TYR   A CG  1 
ATOM   707  C  CD1 . TYR   A 1 88  ? 2.723  18.910  9.478  1.00 34.41  ? 94  TYR   A CD1 1 
ATOM   708  C  CD2 . TYR   A 1 88  ? 2.017  21.011  10.320 1.00 34.32  ? 94  TYR   A CD2 1 
ATOM   709  C  CE1 . TYR   A 1 88  ? 1.405  18.525  9.307  1.00 35.57  ? 94  TYR   A CE1 1 
ATOM   710  C  CE2 . TYR   A 1 88  ? 0.692  20.643  10.154 1.00 35.49  ? 94  TYR   A CE2 1 
ATOM   711  C  CZ  . TYR   A 1 88  ? 0.385  19.393  9.649  1.00 36.32  ? 94  TYR   A CZ  1 
ATOM   712  O  OH  . TYR   A 1 88  ? -0.917 19.020  9.483  1.00 38.30  ? 94  TYR   A OH  1 
ATOM   713  N  N   . GLN   A 1 89  ? 6.776  18.362  12.064 1.00 22.70  ? 95  GLN   A N   1 
ATOM   714  C  CA  . GLN   A 1 89  ? 7.935  17.456  11.645 1.00 19.50  ? 95  GLN   A CA  1 
ATOM   715  C  C   . GLN   A 1 89  ? 7.803  16.710  10.234 1.00 19.30  ? 95  GLN   A C   1 
ATOM   716  O  O   . GLN   A 1 89  ? 6.666  16.245  10.017 1.00 20.55  ? 95  GLN   A O   1 
ATOM   717  C  CB  . GLN   A 1 89  ? 8.177  16.511  12.830 1.00 19.84  ? 95  GLN   A CB  1 
ATOM   718  C  CG  . GLN   A 1 89  ? 9.546  15.876  12.727 1.00 20.69  ? 95  GLN   A CG  1 
ATOM   719  C  CD  . GLN   A 1 89  ? 10.076 15.341  14.036 1.00 19.95  ? 95  GLN   A CD  1 
ATOM   720  O  OE1 . GLN   A 1 89  ? 10.006 15.984  15.077 1.00 21.93  ? 95  GLN   A OE1 1 
ATOM   721  N  NE2 . GLN   A 1 89  ? 10.677 14.166  13.959 1.00 19.29  ? 95  GLN   A NE2 1 
ATOM   722  N  N   . SER   A 1 90  ? 8.829  16.549  9.277  1.00 18.47  ? 96  SER   A N   1 
ATOM   723  C  CA  . SER   A 1 90  ? 8.727  15.764  8.048  1.00 18.49  ? 96  SER   A CA  1 
ATOM   724  C  C   . SER   A 1 90  ? 9.334  14.360  8.218  1.00 18.45  ? 96  SER   A C   1 
ATOM   725  O  O   . SER   A 1 90  ? 10.094 14.113  9.152  1.00 18.23  ? 96  SER   A O   1 
ATOM   726  C  CB  . SER   A 1 90  ? 9.433  16.503  6.903  1.00 20.74  ? 96  SER   A CB  1 
ATOM   727  O  OG  . SER   A 1 90  ? 10.824 16.558  7.164  1.00 24.63  ? 96  SER   A OG  1 
ATOM   728  N  N   . HIS   A 1 91  ? 8.951  13.472  7.288  1.00 17.87  ? 97  HIS   A N   1 
ATOM   729  C  CA  . HIS   A 1 91  ? 9.429  12.090  7.241  1.00 17.70  ? 97  HIS   A CA  1 
ATOM   730  C  C   . HIS   A 1 91  ? 9.157  11.368  8.576  1.00 16.46  ? 97  HIS   A C   1 
ATOM   731  O  O   . HIS   A 1 91  ? 9.968  10.538  8.991  1.00 17.31  ? 97  HIS   A O   1 
ATOM   732  C  CB  . HIS   A 1 91  ? 10.940 12.058  6.839  1.00 18.48  ? 97  HIS   A CB  1 
ATOM   733  C  CG  . HIS   A 1 91  ? 11.202 12.621  5.462  1.00 19.90  ? 97  HIS   A CG  1 
ATOM   734  N  ND1 . HIS   A 1 91  ? 11.297 11.791  4.357  1.00 21.85  ? 97  HIS   A ND1 1 
ATOM   735  C  CD2 . HIS   A 1 91  ? 11.380 13.905  5.060  1.00 22.30  ? 97  HIS   A CD2 1 
ATOM   736  C  CE1 . HIS   A 1 91  ? 11.526 12.594  3.317  1.00 23.88  ? 97  HIS   A CE1 1 
ATOM   737  N  NE2 . HIS   A 1 91  ? 11.568 13.869  3.688  1.00 23.42  ? 97  HIS   A NE2 1 
ATOM   738  N  N   . LEU   A 1 92  ? 8.026  11.647  9.196  1.00 15.77  ? 98  LEU   A N   1 
ATOM   739  C  CA  . LEU   A 1 92  ? 7.693  11.090  10.521 1.00 15.61  ? 98  LEU   A CA  1 
ATOM   740  C  C   . LEU   A 1 92  ? 6.624  9.994   10.351 1.00 16.16  ? 98  LEU   A C   1 
ATOM   741  O  O   . LEU   A 1 92  ? 5.714  10.164  9.548  1.00 17.06  ? 98  LEU   A O   1 
ATOM   742  C  CB  . LEU   A 1 92  ? 7.145  12.220  11.433 1.00 18.09  ? 98  LEU   A CB  1 
ATOM   743  C  CG  . LEU   A 1 92  ? 6.893  11.807  12.923 1.00 19.65  ? 98  LEU   A CG  1 
ATOM   744  C  CD1 . LEU   A 1 92  ? 8.193  11.544  13.612 1.00 19.24  ? 98  LEU   A CD1 1 
ATOM   745  C  CD2 . LEU   A 1 92  ? 6.158  12.894  13.689 1.00 22.31  ? 98  LEU   A CD2 1 
ATOM   746  N  N   . MET   A 1 93  ? 6.763  8.894   11.098 1.00 15.94  ? 99  MET   A N   1 
ATOM   747  C  CA  . MET   A 1 93  ? 5.804  7.780   11.088 1.00 15.96  ? 99  MET   A CA  1 
ATOM   748  C  C   . MET   A 1 93  ? 5.220  7.635   12.479 1.00 16.56  ? 99  MET   A C   1 
ATOM   749  O  O   . MET   A 1 93  ? 5.953  7.722   13.442 1.00 16.90  ? 99  MET   A O   1 
ATOM   750  C  CB  . MET   A 1 93  ? 6.537  6.491   10.712 1.00 15.88  ? 99  MET   A CB  1 
ATOM   751  C  CG  . MET   A 1 93  ? 7.182  6.612   9.334  1.00 17.15  ? 99  MET   A CG  1 
ATOM   752  S  SD  . MET   A 1 93  ? 8.261  5.213   8.922  1.00 21.29  ? 99  MET   A SD  1 
ATOM   753  C  CE  . MET   A 1 93  ? 9.580  5.474   10.178 1.00 26.69  ? 99  MET   A CE  1 
ATOM   754  N  N   . LEU   A 1 94  ? 3.898  7.418   12.607 1.00 15.70  ? 100 LEU   A N   1 
ATOM   755  C  CA  . LEU   A 1 94  ? 3.290  7.296   13.925 1.00 16.66  ? 100 LEU   A CA  1 
ATOM   756  C  C   . LEU   A 1 94  ? 2.796  5.871   14.225 1.00 15.99  ? 100 LEU   A C   1 
ATOM   757  O  O   . LEU   A 1 94  ? 2.366  5.160   13.306 1.00 17.41  ? 100 LEU   A O   1 
ATOM   758  C  CB  . LEU   A 1 94  ? 2.056  8.246   14.103 1.00 18.94  ? 100 LEU   A CB  1 
ATOM   759  C  CG  . LEU   A 1 94  ? 2.301  9.727   14.120 1.00 22.31  ? 100 LEU   A CG  1 
ATOM   760  C  CD1 . LEU   A 1 94  ? 1.005  10.477  14.547 1.00 23.91  ? 100 LEU   A CD1 1 
ATOM   761  C  CD2 . LEU   A 1 94  ? 3.368  10.128  15.150 1.00 23.52  ? 100 LEU   A CD2 1 
ATOM   762  N  N   . ALA   A 1 95  ? 2.855  5.494   15.490 1.00 15.73  ? 101 ALA   A N   1 
ATOM   763  C  CA  . ALA   A 1 95  ? 2.305  4.214   15.959 1.00 15.34  ? 101 ALA   A CA  1 
ATOM   764  C  C   . ALA   A 1 95  ? 1.711  4.432   17.353 1.00 15.04  ? 101 ALA   A C   1 
ATOM   765  O  O   . ALA   A 1 95  ? 1.981  5.434   18.025 1.00 14.96  ? 101 ALA   A O   1 
ATOM   766  C  CB  . ALA   A 1 95  ? 3.429  3.165   16.065 1.00 15.37  ? 101 ALA   A CB  1 
ATOM   767  N  N   . VAL   A 1 96  ? 0.872  3.497   17.800 1.00 14.83  ? 102 VAL   A N   1 
ATOM   768  C  CA  . VAL   A 1 96  ? 0.360  3.502   19.141 1.00 15.00  ? 102 VAL   A CA  1 
ATOM   769  C  C   . VAL   A 1 96  ? 1.379  2.800   20.027 1.00 16.74  ? 102 VAL   A C   1 
ATOM   770  O  O   . VAL   A 1 96  ? 1.706  1.625   19.822 1.00 17.57  ? 102 VAL   A O   1 
ATOM   771  C  CB  . VAL   A 1 96  ? -1.005 2.802   19.200 1.00 14.73  ? 102 VAL   A CB  1 
ATOM   772  C  CG1 . VAL   A 1 96  ? -1.509 2.659   20.629 1.00 16.36  ? 102 VAL   A CG1 1 
ATOM   773  C  CG2 . VAL   A 1 96  ? -1.990 3.537   18.299 1.00 16.33  ? 102 VAL   A CG2 1 
ATOM   774  N  N   . GLY   A 1 97  ? 1.888  3.547   20.999 1.00 16.08  ? 103 GLY   A N   1 
ATOM   775  C  CA  . GLY   A 1 97  ? 2.868  2.977   21.923 1.00 17.17  ? 103 GLY   A CA  1 
ATOM   776  C  C   . GLY   A 1 97  ? 3.358  3.997   22.929 1.00 16.78  ? 103 GLY   A C   1 
ATOM   777  O  O   . GLY   A 1 97  ? 3.060  5.168   22.826 1.00 18.77  ? 103 GLY   A O   1 
ATOM   778  N  N   . HIS   A 1 98  ? 3.790  3.377   24.041 1.00 18.39  ? 104 HIS   A N   1 
ATOM   779  C  CA  . HIS   A 1 98  ? 4.333  4.216   25.142 1.00 19.42  ? 104 HIS   A CA  1 
ATOM   780  C  C   . HIS   A 1 98  ? 5.729  4.811   24.885 1.00 18.53  ? 104 HIS   A C   1 
ATOM   781  O  O   . HIS   A 1 98  ? 6.537  4.160   24.289 1.00 18.29  ? 104 HIS   A O   1 
ATOM   782  C  CB  . HIS   A 1 98  ? 4.410  3.453   26.454 1.00 20.81  ? 104 HIS   A CB  1 
ATOM   783  C  CG  . HIS   A 1 98  ? 5.044  4.264   27.526 1.00 21.91  ? 104 HIS   A CG  1 
ATOM   784  N  ND1 . HIS   A 1 98  ? 4.353  5.227   28.237 1.00 23.82  ? 104 HIS   A ND1 1 
ATOM   785  C  CD2 . HIS   A 1 98  ? 6.323  4.328   27.935 1.00 23.26  ? 104 HIS   A CD2 1 
ATOM   786  C  CE1 . HIS   A 1 98  ? 5.163  5.799   29.095 1.00 23.73  ? 104 HIS   A CE1 1 
ATOM   787  N  NE2 . HIS   A 1 98  ? 6.383  5.278   28.921 1.00 24.15  ? 104 HIS   A NE2 1 
ATOM   788  N  N   . SER   A 1 99  ? 5.944  6.030   25.347 1.00 18.97  ? 105 SER   A N   1 
ATOM   789  C  CA  . SER   A 1 99  ? 7.191  6.785   25.153 1.00 19.93  ? 105 SER   A CA  1 
ATOM   790  C  C   . SER   A 1 99  ? 7.276  7.930   26.167 1.00 22.77  ? 105 SER   A C   1 
ATOM   791  O  O   . SER   A 1 99  ? 6.210  8.330   26.624 1.00 28.08  ? 105 SER   A O   1 
ATOM   792  C  CB  . SER   A 1 99  ? 7.269  7.357   23.760 1.00 23.04  ? 105 SER   A CB  1 
ATOM   793  O  OG  . SER   A 1 99  ? 6.156  8.076   23.317 1.00 31.30  ? 105 SER   A OG  1 
ATOM   794  N  N   . GLU   A 1 100 ? 8.502  8.244   26.611 1.00 19.05  ? 106 GLU   A N   1 
ATOM   795  C  CA  . GLU   A 1 100 ? 8.781  9.452   27.370 1.00 17.52  ? 106 GLU   A CA  1 
ATOM   796  C  C   . GLU   A 1 100 ? 9.969  10.094  26.670 1.00 18.65  ? 106 GLU   A C   1 
ATOM   797  O  O   . GLU   A 1 100 ? 10.542 9.425   25.844 1.00 17.72  ? 106 GLU   A O   1 
ATOM   798  C  CB  . GLU   A 1 100 ? 9.119  8.968   28.765 1.00 18.77  ? 106 GLU   A CB  1 
ATOM   799  C  CG  . GLU   A 1 100 ? 8.004  8.185   29.418 1.00 21.32  ? 106 GLU   A CG  1 
ATOM   800  C  CD  . GLU   A 1 100 ? 8.344  7.571   30.756 1.00 26.91  ? 106 GLU   A CD  1 
ATOM   801  O  OE1 . GLU   A 1 100 ? 9.203  8.107   31.462 1.00 31.14  ? 106 GLU   A OE1 1 
ATOM   802  O  OE2 . GLU   A 1 100 ? 7.715  6.591   31.057 1.00 27.87  ? 106 GLU   A OE2 1 
ATOM   803  N  N   . PRO   A 1 101 ? 10.315 11.364  26.840 1.00 18.97  ? 107 PRO   A N   1 
ATOM   804  C  CA  . PRO   A 1 101 ? 11.385 12.022  26.034 1.00 18.24  ? 107 PRO   A CA  1 
ATOM   805  C  C   . PRO   A 1 101 ? 12.726 11.271  25.833 1.00 18.87  ? 107 PRO   A C   1 
ATOM   806  O  O   . PRO   A 1 101 ? 13.279 11.298  24.806 1.00 19.26  ? 107 PRO   A O   1 
ATOM   807  C  CB  . PRO   A 1 101 ? 11.627 13.253  26.913 1.00 19.60  ? 107 PRO   A CB  1 
ATOM   808  C  CG  . PRO   A 1 101 ? 10.214 13.642  27.317 1.00 21.26  ? 107 PRO   A CG  1 
ATOM   809  C  CD  . PRO   A 1 101 ? 9.587  12.317  27.686 1.00 19.41  ? 107 PRO   A CD  1 
ATOM   810  N  N   . GLY   A 1 102 ? 13.225 10.684  26.950 1.00 18.60  ? 108 GLY   A N   1 
ATOM   811  C  CA  . GLY   A 1 102 ? 14.480 9.883   26.947 1.00 18.73  ? 108 GLY   A CA  1 
ATOM   812  C  C   . GLY   A 1 102 ? 14.453 8.611   26.140 1.00 16.02  ? 108 GLY   A C   1 
ATOM   813  O  O   . GLY   A 1 102 ? 15.447 8.030   25.972 1.00 16.66  ? 108 GLY   A O   1 
ATOM   814  N  N   . ASP   A 1 103 ? 13.254 8.193   25.772 1.00 15.27  ? 109 ASP   A N   1 
ATOM   815  C  CA  . ASP   A 1 103 ? 13.259 7.086   24.788 1.00 15.75  ? 109 ASP   A CA  1 
ATOM   816  C  C   . ASP   A 1 103 ? 13.594 7.585   23.393 1.00 15.11  ? 109 ASP   A C   1 
ATOM   817  O  O   . ASP   A 1 103 ? 13.772 6.704   22.590 1.00 14.43  ? 109 ASP   A O   1 
ATOM   818  C  CB  . ASP   A 1 103 ? 11.847 6.551   24.710 1.00 14.18  ? 109 ASP   A CB  1 
ATOM   819  C  CG  . ASP   A 1 103 ? 11.423 5.931   26.025 1.00 16.64  ? 109 ASP   A CG  1 
ATOM   820  O  OD1 . ASP   A 1 103 ? 12.202 5.210   26.588 1.00 16.61  ? 109 ASP   A OD1 1 
ATOM   821  O  OD2 . ASP   A 1 103 ? 10.272 6.151   26.419 1.00 16.41  ? 109 ASP   A OD2 1 
ATOM   822  N  N   . CYS   A 1 104 ? 13.824 8.886   23.170 1.00 14.59  ? 110 CYS   A N   1 
ATOM   823  C  CA  . CYS   A 1 104 ? 14.261 9.310   21.763 1.00 14.41  ? 110 CYS   A CA  1 
ATOM   824  C  C   . CYS   A 1 104 ? 15.589 8.535   21.448 1.00 14.78  ? 110 CYS   A C   1 
ATOM   825  O  O   . CYS   A 1 104 ? 16.375 8.485   22.348 1.00 15.32  ? 110 CYS   A O   1 
ATOM   826  C  CB  . CYS   A 1 104 ? 14.426 10.829  21.521 1.00 14.97  ? 110 CYS   A CB  1 
ATOM   827  S  SG  . CYS   A 1 104 ? 12.831 11.728  21.542 1.00 17.61  ? 110 CYS   A SG  1 
ATOM   828  N  N   . GLY   A 1 105 ? 15.743 7.943   20.222 1.00 13.05  ? 111 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 105 ? 16.941 7.201   19.876 1.00 13.28  ? 111 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 105 ? 16.748 5.697   19.803 1.00 13.25  ? 111 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 105 ? 17.579 4.998   19.225 1.00 13.58  ? 111 GLY   A O   1 
ATOM   832  N  N   . GLY   A 1 106 ? 15.656 5.205   20.381 1.00 12.25  ? 112 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 106 ? 15.366 3.774   20.285 1.00 12.39  ? 112 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 106 ? 15.105 3.370   18.851 1.00 12.45  ? 112 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 106 ? 14.413 4.100   18.138 1.00 13.13  ? 112 GLY   A O   1 
ATOM   836  N  N   . ILE   A 1 107 ? 15.601 2.226   18.439 1.00 12.85  ? 113 ILE   A N   1 
ATOM   837  C  CA  . ILE   A 1 107 ? 15.417 1.803   17.031 1.00 12.45  ? 113 ILE   A CA  1 
ATOM   838  C  C   . ILE   A 1 107 ? 14.086 1.146   16.761 1.00 12.03  ? 113 ILE   A C   1 
ATOM   839  O  O   . ILE   A 1 107 ? 13.630 0.313   17.540 1.00 12.69  ? 113 ILE   A O   1 
ATOM   840  C  CB  . ILE   A 1 107 ? 16.569 0.827   16.671 1.00 12.80  ? 113 ILE   A CB  1 
ATOM   841  C  CG1 . ILE   A 1 107 ? 17.853 1.674   16.396 1.00 14.77  ? 113 ILE   A CG1 1 
ATOM   842  C  CG2 . ILE   A 1 107 ? 16.276 -0.028  15.431 1.00 14.04  ? 113 ILE   A CG2 1 
ATOM   843  C  CD1 . ILE   A 1 107 ? 19.176 0.787   16.322 1.00 17.71  ? 113 ILE   A CD1 1 
ATOM   844  N  N   . LEU   A 1 108 ? 13.515 1.482   15.624 1.00 11.89  ? 114 LEU   A N   1 
ATOM   845  C  CA  . LEU   A 1 108 ? 12.366 0.784   14.994 1.00 11.83  ? 114 LEU   A CA  1 
ATOM   846  C  C   . LEU   A 1 108 ? 12.969 -0.061  13.855 1.00 11.78  ? 114 LEU   A C   1 
ATOM   847  O  O   . LEU   A 1 108 ? 13.754 0.475   13.046 1.00 12.92  ? 114 LEU   A O   1 
ATOM   848  C  CB  . LEU   A 1 108 ? 11.393 1.817   14.376 1.00 12.48  ? 114 LEU   A CB  1 
ATOM   849  C  CG  . LEU   A 1 108 ? 10.269 1.212   13.488 1.00 13.02  ? 114 LEU   A CG  1 
ATOM   850  C  CD1 . LEU   A 1 108 ? 9.269  0.423   14.352 1.00 14.12  ? 114 LEU   A CD1 1 
ATOM   851  C  CD2 . LEU   A 1 108 ? 9.481  2.336   12.719 1.00 14.94  ? 114 LEU   A CD2 1 
ATOM   852  N  N   . ARG   A 1 109 ? 12.671 -1.358  13.827 1.00 11.89  ? 115 ARG   A N   1 
ATOM   853  C  CA  . ARG   A 1 109 ? 13.233 -2.283  12.799 1.00 13.40  ? 115 ARG   A CA  1 
ATOM   854  C  C   . ARG   A 1 109 ? 12.162 -3.188  12.249 1.00 14.46  ? 115 ARG   A C   1 
ATOM   855  O  O   . ARG   A 1 109 ? 11.145 -3.468  12.903 1.00 13.41  ? 115 ARG   A O   1 
ATOM   856  C  CB  . ARG   A 1 109 ? 14.396 -3.104  13.421 1.00 15.07  ? 115 ARG   A CB  1 
ATOM   857  C  CG  . ARG   A 1 109 ? 13.936 -4.028  14.530 1.00 15.11  ? 115 ARG   A CG  1 
ATOM   858  C  CD  . ARG   A 1 109 ? 15.126 -4.784  15.094 1.00 16.53  ? 115 ARG   A CD  1 
ATOM   859  N  NE  . ARG   A 1 109 ? 15.968 -3.924  15.901 1.00 17.69  ? 115 ARG   A NE  1 
ATOM   860  C  CZ  . ARG   A 1 109 ? 17.260 -3.730  15.709 1.00 17.88  ? 115 ARG   A CZ  1 
ATOM   861  N  NH1 . ARG   A 1 109 ? 17.857 -4.195  14.613 1.00 18.44  ? 115 ARG   A NH1 1 
ATOM   862  N  NH2 . ARG   A 1 109 ? 17.956 -2.992  16.562 1.00 18.02  ? 115 ARG   A NH2 1 
ATOM   863  N  N   . CYS   A 1 110 ? 12.411 -3.665  11.023 1.00 15.55  ? 116 CYS   A N   1 
ATOM   864  C  CA  . CYS   A 1 110 ? 11.512 -4.631  10.359 1.00 19.62  ? 116 CYS   A CA  1 
ATOM   865  C  C   . CYS   A 1 110 ? 12.366 -5.819  9.921  1.00 23.18  ? 116 CYS   A C   1 
ATOM   866  O  O   . CYS   A 1 110 ? 13.551 -5.929  10.289 1.00 22.33  ? 116 CYS   A O   1 
ATOM   867  C  CB  . CYS   A 1 110 ? 10.811 -3.965  9.184  1.00 18.46  ? 116 CYS   A CB  1 
ATOM   868  S  SG  . CYS   A 1 110 ? 11.950 -3.564  7.805  1.00 18.74  ? 116 CYS   A SG  1 
ATOM   869  N  N   . GLN   A 1 111 ? 11.749 -6.754  9.133  1.00 25.43  ? 117 GLN   A N   1 
ATOM   870  C  CA  . GLN   A 1 111 ? 12.501 -7.906  8.629  1.00 27.55  ? 117 GLN   A CA  1 
ATOM   871  C  C   . GLN   A 1 111 ? 13.705 -7.512  7.763  1.00 27.99  ? 117 GLN   A C   1 
ATOM   872  O  O   . GLN   A 1 111 ? 14.622 -8.312  7.620  1.00 31.42  ? 117 GLN   A O   1 
ATOM   873  C  CB  . GLN   A 1 111 ? 11.608 -8.909  7.851  1.00 31.09  ? 117 GLN   A CB  1 
ATOM   874  C  CG  . GLN   A 1 111 ? 11.077 -8.326  6.560  1.00 34.76  ? 117 GLN   A CG  1 
ATOM   875  C  CD  . GLN   A 1 111 ? 10.132 -9.245  5.834  1.00 40.82  ? 117 GLN   A CD  1 
ATOM   876  O  OE1 . GLN   A 1 111 ? 8.918  -9.245  6.076  1.00 42.32  ? 117 GLN   A OE1 1 
ATOM   877  N  NE2 . GLN   A 1 111 ? 10.668 -10.018 4.901  1.00 40.79  ? 117 GLN   A NE2 1 
ATOM   878  N  N   . HIS   A 1 112 ? 13.716 -6.298  7.191  1.00 24.61  ? 118 HIS   A N   1 
ATOM   879  C  CA  . HIS   A 1 112 ? 14.816 -5.862  6.303  1.00 23.14  ? 118 HIS   A CA  1 
ATOM   880  C  C   . HIS   A 1 112 ? 15.980 -5.132  7.010  1.00 22.50  ? 118 HIS   A C   1 
ATOM   881  O  O   . HIS   A 1 112 ? 17.053 -4.917  6.413  1.00 24.15  ? 118 HIS   A O   1 
ATOM   882  C  CB  . HIS   A 1 112 ? 14.230 -4.993  5.177  1.00 22.76  ? 118 HIS   A CB  1 
ATOM   883  C  CG  . HIS   A 1 112 ? 13.104 -5.696  4.438  1.00 26.59  ? 118 HIS   A CG  1 
ATOM   884  N  ND1 . HIS   A 1 112 ? 11.762 -5.330  4.581  1.00 27.70  ? 118 HIS   A ND1 1 
ATOM   885  C  CD2 . HIS   A 1 112 ? 13.175 -6.696  3.521  1.00 30.79  ? 118 HIS   A CD2 1 
ATOM   886  C  CE1 . HIS   A 1 112 ? 11.074 -6.148  3.790  1.00 31.74  ? 118 HIS   A CE1 1 
ATOM   887  N  NE2 . HIS   A 1 112 ? 11.880 -6.999  3.152  1.00 32.98  ? 118 HIS   A NE2 1 
ATOM   888  N  N   . GLY   A 1 113 ? 15.765 -4.681  8.259  1.00 20.44  ? 119 GLY   A N   1 
ATOM   889  C  CA  . GLY   A 1 113 ? 16.796 -3.919  8.958  1.00 19.11  ? 119 GLY   A CA  1 
ATOM   890  C  C   . GLY   A 1 113 ? 16.223 -2.747  9.741  1.00 16.76  ? 119 GLY   A C   1 
ATOM   891  O  O   . GLY   A 1 113 ? 15.035 -2.709  10.053 1.00 16.40  ? 119 GLY   A O   1 
ATOM   892  N  N   . VAL   A 1 114 ? 17.058 -1.742  9.983  1.00 15.32  ? 120 VAL   A N   1 
ATOM   893  C  CA  . VAL   A 1 114 ? 16.644 -0.539  10.727 1.00 15.51  ? 120 VAL   A CA  1 
ATOM   894  C  C   . VAL   A 1 114 ? 15.792 0.386   9.882  1.00 13.96  ? 120 VAL   A C   1 
ATOM   895  O  O   . VAL   A 1 114 ? 16.184 0.723   8.765  1.00 14.31  ? 120 VAL   A O   1 
ATOM   896  C  CB  . VAL   A 1 114 ? 17.878 0.228   11.287 1.00 15.82  ? 120 VAL   A CB  1 
ATOM   897  C  CG1 . VAL   A 1 114 ? 17.428 1.512   11.988 1.00 16.44  ? 120 VAL   A CG1 1 
ATOM   898  C  CG2 . VAL   A 1 114 ? 18.657 -0.662  12.243 1.00 17.80  ? 120 VAL   A CG2 1 
ATOM   899  N  N   . VAL   A 1 115 ? 14.615 0.771   10.362 1.00 12.34  ? 121 VAL   A N   1 
ATOM   900  C  CA  . VAL   A 1 115 ? 13.663 1.649   9.696  1.00 13.45  ? 121 VAL   A CA  1 
ATOM   901  C  C   . VAL   A 1 115 ? 13.778 3.100   10.133 1.00 13.54  ? 121 VAL   A C   1 
ATOM   902  O  O   . VAL   A 1 115 ? 13.666 4.012   9.326  1.00 14.95  ? 121 VAL   A O   1 
ATOM   903  C  CB  . VAL   A 1 115 ? 12.225 1.159   9.958  1.00 15.09  ? 121 VAL   A CB  1 
ATOM   904  C  CG1 . VAL   A 1 115 ? 11.167 2.120   9.402  1.00 17.24  ? 121 VAL   A CG1 1 
ATOM   905  C  CG2 . VAL   A 1 115 ? 12.024 -0.253  9.441  1.00 16.25  ? 121 VAL   A CG2 1 
ATOM   906  N  N   . GLY   A 1 116 ? 14.022 3.347   11.421 1.00 13.31  ? 122 GLY   A N   1 
ATOM   907  C  CA  . GLY   A 1 116 ? 14.150 4.711   11.930 1.00 14.55  ? 122 GLY   A CA  1 
ATOM   908  C  C   . GLY   A 1 116 ? 14.387 4.733   13.423 1.00 13.01  ? 122 GLY   A C   1 
ATOM   909  O  O   . GLY   A 1 116 ? 14.700 3.671   13.990 1.00 12.89  ? 122 GLY   A O   1 
ATOM   910  N  N   . ILE   A 1 117 ? 14.269 5.909   14.051 1.00 12.24  ? 123 ILE   A N   1 
ATOM   911  C  CA  . ILE   A 1 117 ? 14.501 6.040   15.487 1.00 12.00  ? 123 ILE   A CA  1 
ATOM   912  C  C   . ILE   A 1 117 ? 13.373 6.802   16.121 1.00 12.45  ? 123 ILE   A C   1 
ATOM   913  O  O   . ILE   A 1 117 ? 12.795 7.701   15.488 1.00 13.58  ? 123 ILE   A O   1 
ATOM   914  C  CB  . ILE   A 1 117 ? 15.871 6.708   15.856 1.00 13.26  ? 123 ILE   A CB  1 
ATOM   915  C  CG1 . ILE   A 1 117 ? 16.053 8.038   15.124 1.00 14.83  ? 123 ILE   A CG1 1 
ATOM   916  C  CG2 . ILE   A 1 117 ? 17.004 5.715   15.643 1.00 15.98  ? 123 ILE   A CG2 1 
ATOM   917  C  CD1 . ILE   A 1 117 ? 17.295 8.826   15.663 1.00 15.32  ? 123 ILE   A CD1 1 
ATOM   918  N  N   . VAL   A 1 118 ? 13.116 6.545   17.408 1.00 12.13  ? 124 VAL   A N   1 
ATOM   919  C  CA  . VAL   A 1 118 ? 12.056 7.285   18.135 1.00 12.42  ? 124 VAL   A CA  1 
ATOM   920  C  C   . VAL   A 1 118 ? 12.449 8.771   18.154 1.00 14.00  ? 124 VAL   A C   1 
ATOM   921  O  O   . VAL   A 1 118 ? 13.639 9.112   18.454 1.00 12.55  ? 124 VAL   A O   1 
ATOM   922  C  CB  . VAL   A 1 118 ? 11.938 6.787   19.580 1.00 12.91  ? 124 VAL   A CB  1 
ATOM   923  C  CG1 . VAL   A 1 118 ? 10.947 7.657   20.396 1.00 13.90  ? 124 VAL   A CG1 1 
ATOM   924  C  CG2 . VAL   A 1 118 ? 11.504 5.314   19.631 1.00 13.90  ? 124 VAL   A CG2 1 
ATOM   925  N  N   . SER   A 1 119 ? 11.515 9.674   17.848 1.00 13.48  ? 125 SER   A N   1 
ATOM   926  C  CA  . SER   A 1 119 ? 11.789 11.153  17.684 1.00 14.46  ? 125 SER   A CA  1 
ATOM   927  C  C   . SER   A 1 119 ? 10.763 11.957  18.489 1.00 15.90  ? 125 SER   A C   1 
ATOM   928  O  O   . SER   A 1 119 ? 11.041 13.056  18.937 1.00 16.86  ? 125 SER   A O   1 
ATOM   929  C  CB  . SER   A 1 119 ? 11.736 11.681  16.195 1.00 14.71  ? 125 SER   A CB  1 
ATOM   930  O  OG  . SER   A 1 119 ? 11.995 13.091  16.104 1.00 17.64  ? 125 SER   A OG  1 
ATOM   931  N  N   . THR   A 1 120 ? 9.497  11.441  18.532 1.00 16.30  ? 126 THR   A N   1 
ATOM   932  C  CA  . THR   A 1 120 ? 8.428  12.161  19.316 1.00 17.63  ? 126 THR   A CA  1 
ATOM   933  C  C   . THR   A 1 120 ? 7.396  11.185  19.961 1.00 17.52  ? 126 THR   A C   1 
ATOM   934  O  O   . THR   A 1 120 ? 7.557  10.005  19.775 1.00 16.58  ? 126 THR   A O   1 
ATOM   935  C  CB  . THR   A 1 120 ? 7.745  13.170  18.401 1.00 19.98  ? 126 THR   A CB  1 
ATOM   936  O  OG1 . THR   A 1 120 ? 7.017  14.135  19.161 1.00 29.42  ? 126 THR   A OG1 1 
ATOM   937  C  CG2 . THR   A 1 120 ? 6.780  12.492  17.454 1.00 17.60  ? 126 THR   A CG2 1 
ATOM   938  N  N   . GLY   A 1 121 ? 6.440  11.742  20.746 1.00 19.23  ? 127 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 121 ? 5.437  10.896  21.424 1.00 21.50  ? 127 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 121 ? 4.462  11.792  22.179 1.00 24.32  ? 127 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 121 ? 4.751  12.977  22.309 1.00 26.14  ? 127 GLY   A O   1 
ATOM   942  N  N   . GLY   A 1 122 ? 3.441  11.160  22.758 1.00 26.08  ? 128 GLY   A N   1 
ATOM   943  C  CA  . GLY   A 1 122 ? 2.434  11.867  23.554 1.00 27.61  ? 128 GLY   A CA  1 
ATOM   944  C  C   . GLY   A 1 122 ? 1.079  11.198  23.398 1.00 30.00  ? 128 GLY   A C   1 
ATOM   945  O  O   . GLY   A 1 122 ? 0.852  10.689  22.351 1.00 29.92  ? 128 GLY   A O   1 
ATOM   946  N  N   . ASN   A 1 123 ? 0.358  11.085  24.514 1.00 30.80  ? 129 ASN   A N   1 
ATOM   947  C  CA  . ASN   A 1 123 ? -1.036 10.573  24.470 1.00 31.40  ? 129 ASN   A CA  1 
ATOM   948  C  C   . ASN   A 1 123 ? -1.034 9.148   23.885 1.00 30.05  ? 129 ASN   A C   1 
ATOM   949  O  O   . ASN   A 1 123 ? -2.065 8.766   23.374 1.00 31.33  ? 129 ASN   A O   1 
ATOM   950  C  CB  . ASN   A 1 123 ? -1.947 11.596  23.762 1.00 32.77  ? 129 ASN   A CB  1 
ATOM   951  C  CG  . ASN   A 1 123 ? -1.807 13.014  24.254 1.00 35.45  ? 129 ASN   A CG  1 
ATOM   952  O  OD1 . ASN   A 1 123 ? -1.686 13.257  25.446 1.00 35.83  ? 129 ASN   A OD1 1 
ATOM   953  N  ND2 . ASN   A 1 123 ? -1.817 13.951  23.328 1.00 36.39  ? 129 ASN   A ND2 1 
ATOM   954  N  N   . GLY   A 1 124 ? 0.058  8.418   24.070 1.00 26.74  ? 130 GLY   A N   1 
ATOM   955  C  CA  . GLY   A 1 124 ? 0.003  6.988   23.704 1.00 23.32  ? 130 GLY   A CA  1 
ATOM   956  C  C   . GLY   A 1 124 ? 0.391  6.767   22.255 1.00 20.07  ? 130 GLY   A C   1 
ATOM   957  O  O   . GLY   A 1 124 ? 0.156  5.681   21.789 1.00 19.26  ? 130 GLY   A O   1 
ATOM   958  N  N   . LEU   A 1 125 ? 0.994  7.785   21.614 1.00 18.13  ? 131 LEU   A N   1 
ATOM   959  C  CA  . LEU   A 1 125 ? 1.486  7.668   20.200 1.00 17.88  ? 131 LEU   A CA  1 
ATOM   960  C  C   . LEU   A 1 125 ? 2.989  7.788   20.200 1.00 18.27  ? 131 LEU   A C   1 
ATOM   961  O  O   . LEU   A 1 125 ? 3.532  8.514   21.085 1.00 20.28  ? 131 LEU   A O   1 
ATOM   962  C  CB  . LEU   A 1 125 ? 0.977  8.786   19.265 1.00 19.39  ? 131 LEU   A CB  1 
ATOM   963  C  CG  . LEU   A 1 125 ? -0.544 8.899   19.202 1.00 21.24  ? 131 LEU   A CG  1 
ATOM   964  C  CD1 . LEU   A 1 125 ? -1.018 10.257  18.700 1.00 23.41  ? 131 LEU   A CD1 1 
ATOM   965  C  CD2 . LEU   A 1 125 ? -1.058 7.803   18.303 1.00 20.90  ? 131 LEU   A CD2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 3.596  7.037   19.368 1.00 15.25  ? 132 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 5.050  7.307   19.312 1.00 15.00  ? 132 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 5.383  7.653   17.898 1.00 14.56  ? 132 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 4.751  7.095   17.024 1.00 15.20  ? 132 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 5.875  6.128   19.803 1.00 15.63  ? 132 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 5.461  4.801   19.190 1.00 15.90  ? 132 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 7.376  6.329   19.635 1.00 14.94  ? 132 VAL   A CG2 1 
ATOM   973  N  N   . GLY   A 1 127 ? 6.450  8.469   17.742 1.00 14.78  ? 133 GLY   A N   1 
ATOM   974  C  CA  . GLY   A 1 127 ? 6.765  8.978   16.412 1.00 14.29  ? 133 GLY   A CA  1 
ATOM   975  C  C   . GLY   A 1 127 ? 8.188  8.605   16.061 1.00 15.27  ? 133 GLY   A C   1 
ATOM   976  O  O   . GLY   A 1 127 ? 9.027  8.789   16.885 1.00 16.11  ? 133 GLY   A O   1 
ATOM   977  N  N   . PHE   A 1 128 ? 8.350  8.071   14.846 1.00 13.68  ? 134 PHE   A N   1 
ATOM   978  C  CA  . PHE   A 1 128 ? 9.691  7.651   14.434 1.00 13.62  ? 134 PHE   A CA  1 
ATOM   979  C  C   . PHE   A 1 128 ? 10.153 8.473   13.258 1.00 14.92  ? 134 PHE   A C   1 
ATOM   980  O  O   . PHE   A 1 128 ? 9.405  8.642   12.282 1.00 15.23  ? 134 PHE   A O   1 
ATOM   981  C  CB  . PHE   A 1 128 ? 9.643  6.171   14.024 1.00 14.54  ? 134 PHE   A CB  1 
ATOM   982  C  CG  . PHE   A 1 128 ? 9.024  5.227   15.037 1.00 14.29  ? 134 PHE   A CG  1 
ATOM   983  C  CD1 . PHE   A 1 128 ? 9.768  4.742   16.110 1.00 14.59  ? 134 PHE   A CD1 1 
ATOM   984  C  CD2 . PHE   A 1 128 ? 7.694  4.849   14.935 1.00 14.88  ? 134 PHE   A CD2 1 
ATOM   985  C  CE1 . PHE   A 1 128 ? 9.202  3.875   17.038 1.00 13.49  ? 134 PHE   A CE1 1 
ATOM   986  C  CE2 . PHE   A 1 128 ? 7.147  3.951   15.844 1.00 14.60  ? 134 PHE   A CE2 1 
ATOM   987  C  CZ  . PHE   A 1 128 ? 7.900  3.507   16.926 1.00 14.66  ? 134 PHE   A CZ  1 
ATOM   988  N  N   . ALA   A 1 129 ? 11.409 8.926   13.323 1.00 13.41  ? 135 ALA   A N   1 
ATOM   989  C  CA  . ALA   A 1 129 ? 12.037 9.604   12.184 1.00 13.66  ? 135 ALA   A CA  1 
ATOM   990  C  C   . ALA   A 1 129 ? 12.517 8.515   11.222 1.00 14.14  ? 135 ALA   A C   1 
ATOM   991  O  O   . ALA   A 1 129 ? 13.394 7.730   11.580 1.00 14.41  ? 135 ALA   A O   1 
ATOM   992  C  CB  . ALA   A 1 129 ? 13.206 10.424  12.701 1.00 13.83  ? 135 ALA   A CB  1 
ATOM   993  N  N   . ASP   A 1 130 ? 11.981 8.478   9.995  1.00 13.73  ? 136 ASP   A N   1 
ATOM   994  C  CA  . ASP   A 1 130 ? 12.376 7.491   9.014  1.00 14.91  ? 136 ASP   A CA  1 
ATOM   995  C  C   . ASP   A 1 130 ? 13.787 7.741   8.518  1.00 14.13  ? 136 ASP   A C   1 
ATOM   996  O  O   . ASP   A 1 130 ? 14.189 8.897   8.332  1.00 15.88  ? 136 ASP   A O   1 
ATOM   997  C  CB  . ASP   A 1 130 ? 11.424 7.600   7.771  1.00 17.45  ? 136 ASP   A CB  1 
ATOM   998  C  CG  . ASP   A 1 130 ? 11.679 6.558   6.703  1.00 21.37  ? 136 ASP   A CG  1 
ATOM   999  O  OD1 . ASP   A 1 130 ? 11.691 5.371   7.033  1.00 19.64  ? 136 ASP   A OD1 1 
ATOM   1000 O  OD2 . ASP   A 1 130 ? 11.877 6.954   5.511  1.00 25.76  ? 136 ASP   A OD2 1 
ATOM   1001 N  N   . VAL   A 1 131 ? 14.523 6.653   8.186  1.00 14.59  ? 137 VAL   A N   1 
ATOM   1002 C  CA  . VAL   A 1 131 ? 15.837 6.758   7.543  1.00 14.73  ? 137 VAL   A CA  1 
ATOM   1003 C  C   . VAL   A 1 131 ? 15.954 5.934   6.243  1.00 14.90  ? 137 VAL   A C   1 
ATOM   1004 O  O   . VAL   A 1 131 ? 17.023 5.916   5.619  1.00 15.19  ? 137 VAL   A O   1 
ATOM   1005 C  CB  . VAL   A 1 131 ? 17.012 6.417   8.497  1.00 14.03  ? 137 VAL   A CB  1 
ATOM   1006 C  CG1 . VAL   A 1 131 ? 17.016 7.340   9.725  1.00 14.55  ? 137 VAL   A CG1 1 
ATOM   1007 C  CG2 . VAL   A 1 131 ? 17.013 4.954   8.900  1.00 14.86  ? 137 VAL   A CG2 1 
ATOM   1008 N  N   . ARG   A 1 132 ? 14.879 5.262   5.829  1.00 14.97  ? 138 ARG   A N   1 
ATOM   1009 C  CA  . ARG   A 1 132 ? 14.912 4.353   4.682  1.00 15.01  ? 138 ARG   A CA  1 
ATOM   1010 C  C   . ARG   A 1 132 ? 15.166 5.046   3.348  1.00 17.39  ? 138 ARG   A C   1 
ATOM   1011 O  O   . ARG   A 1 132 ? 15.596 4.387   2.397  1.00 18.22  ? 138 ARG   A O   1 
ATOM   1012 C  CB  . ARG   A 1 132 ? 13.626 3.511   4.602  1.00 15.34  ? 138 ARG   A CB  1 
ATOM   1013 C  CG  . ARG   A 1 132 ? 13.512 2.558   5.809  1.00 15.40  ? 138 ARG   A CG  1 
ATOM   1014 C  CD  . ARG   A 1 132 ? 12.199 1.790   5.677  1.00 17.13  ? 138 ARG   A CD  1 
ATOM   1015 N  NE  . ARG   A 1 132 ? 11.070 2.721   5.935  1.00 16.60  ? 138 ARG   A NE  1 
ATOM   1016 C  CZ  . ARG   A 1 132 ? 9.790  2.343   6.000  1.00 19.22  ? 138 ARG   A CZ  1 
ATOM   1017 N  NH1 . ARG   A 1 132 ? 9.451  1.090   5.735  1.00 19.20  ? 138 ARG   A NH1 1 
ATOM   1018 N  NH2 . ARG   A 1 132 ? 8.848  3.226   6.324  1.00 20.21  ? 138 ARG   A NH2 1 
ATOM   1019 N  N   . ASP   A 1 133 ? 14.929 6.371   3.261  1.00 16.69  ? 139 ASP   A N   1 
ATOM   1020 C  CA  . ASP   A 1 133 ? 15.174 7.088   2.004  1.00 17.69  ? 139 ASP   A CA  1 
ATOM   1021 C  C   . ASP   A 1 133 ? 16.618 7.615   1.922  1.00 17.15  ? 139 ASP   A C   1 
ATOM   1022 O  O   . ASP   A 1 133 ? 16.983 8.128   0.861  1.00 19.56  ? 139 ASP   A O   1 
ATOM   1023 C  CB  . ASP   A 1 133 ? 14.170 8.267   1.901  1.00 18.92  ? 139 ASP   A CB  1 
ATOM   1024 C  CG  . ASP   A 1 133 ? 14.419 9.327   2.968  1.00 22.02  ? 139 ASP   A CG  1 
ATOM   1025 O  OD1 . ASP   A 1 133 ? 14.596 8.957   4.164  1.00 20.83  ? 139 ASP   A OD1 1 
ATOM   1026 O  OD2 . ASP   A 1 133 ? 14.441 10.512  2.626  1.00 24.83  ? 139 ASP   A OD2 1 
ATOM   1027 N  N   . LEU   A 1 134 ? 17.430 7.497   2.971  1.00 15.77  ? 140 LEU   A N   1 
ATOM   1028 C  CA  . LEU   A 1 134 ? 18.791 8.051   3.023  1.00 15.36  ? 140 LEU   A CA  1 
ATOM   1029 C  C   . LEU   A 1 134 ? 19.731 6.993   2.467  1.00 17.34  ? 140 LEU   A C   1 
ATOM   1030 O  O   . LEU   A 1 134 ? 20.428 6.317   3.209  1.00 17.62  ? 140 LEU   A O   1 
ATOM   1031 C  CB  . LEU   A 1 134 ? 19.158 8.452   4.465  1.00 15.61  ? 140 LEU   A CB  1 
ATOM   1032 C  CG  . LEU   A 1 134 ? 18.220 9.482   5.145  1.00 16.55  ? 140 LEU   A CG  1 
ATOM   1033 C  CD1 . LEU   A 1 134 ? 18.608 9.702   6.594  1.00 16.82  ? 140 LEU   A CD1 1 
ATOM   1034 C  CD2 . LEU   A 1 134 ? 18.193 10.803  4.380  1.00 18.67  ? 140 LEU   A CD2 1 
ATOM   1035 N  N   . LEU   A 1 135 ? 19.684 6.811   1.152  1.00 16.64  ? 141 LEU   A N   1 
ATOM   1036 C  CA  . LEU   A 1 135 ? 20.446 5.739   0.503  1.00 17.75  ? 141 LEU   A CA  1 
ATOM   1037 C  C   . LEU   A 1 135 ? 21.927 5.862   0.669  1.00 18.22  ? 141 LEU   A C   1 
ATOM   1038 O  O   . LEU   A 1 135 ? 22.634 4.842   0.664  1.00 19.80  ? 141 LEU   A O   1 
ATOM   1039 C  CB  . LEU   A 1 135 ? 20.073 5.605   -1.000 1.00 18.84  ? 141 LEU   A CB  1 
ATOM   1040 C  CG  . LEU   A 1 135 ? 18.554 5.579   -1.286 1.00 21.09  ? 141 LEU   A CG  1 
ATOM   1041 C  CD1 . LEU   A 1 135 ? 18.341 5.288   -2.774 1.00 22.23  ? 141 LEU   A CD1 1 
ATOM   1042 C  CD2 . LEU   A 1 135 ? 17.816 4.514   -0.503 1.00 23.23  ? 141 LEU   A CD2 1 
ATOM   1043 N  N   . TRP   A 1 136 ? 22.415 7.104   0.811  1.00 16.46  ? 142 TRP   A N   1 
ATOM   1044 C  CA  . TRP   A 1 136 ? 23.844 7.342   0.981  1.00 16.98  ? 142 TRP   A CA  1 
ATOM   1045 C  C   . TRP   A 1 136 ? 24.409 6.741   2.270  1.00 17.17  ? 142 TRP   A C   1 
ATOM   1046 O  O   . TRP   A 1 136 ? 25.650 6.628   2.373  1.00 18.19  ? 142 TRP   A O   1 
ATOM   1047 C  CB  . TRP   A 1 136 ? 24.160 8.835   0.870  1.00 17.40  ? 142 TRP   A CB  1 
ATOM   1048 C  CG  . TRP   A 1 136 ? 23.382 9.698   1.819  1.00 16.67  ? 142 TRP   A CG  1 
ATOM   1049 C  CD1 . TRP   A 1 136 ? 22.225 10.364  1.548  1.00 17.22  ? 142 TRP   A CD1 1 
ATOM   1050 C  CD2 . TRP   A 1 136 ? 23.714 10.003  3.182  1.00 16.90  ? 142 TRP   A CD2 1 
ATOM   1051 N  NE1 . TRP   A 1 136 ? 21.805 11.056  2.668  1.00 18.38  ? 142 TRP   A NE1 1 
ATOM   1052 C  CE2 . TRP   A 1 136 ? 22.718 10.872  3.668  1.00 17.70  ? 142 TRP   A CE2 1 
ATOM   1053 C  CE3 . TRP   A 1 136 ? 24.792 9.678   4.014  1.00 17.87  ? 142 TRP   A CE3 1 
ATOM   1054 C  CZ2 . TRP   A 1 136 ? 22.746 11.382  4.978  1.00 18.97  ? 142 TRP   A CZ2 1 
ATOM   1055 C  CZ3 . TRP   A 1 136 ? 24.838 10.202  5.301  1.00 18.86  ? 142 TRP   A CZ3 1 
ATOM   1056 C  CH2 . TRP   A 1 136 ? 23.817 11.036  5.768  1.00 18.53  ? 142 TRP   A CH2 1 
ATOM   1057 N  N   . LEU   A 1 137 ? 23.557 6.377   3.258  1.00 16.88  ? 143 LEU   A N   1 
ATOM   1058 C  CA  . LEU   A 1 137 ? 24.091 5.745   4.477  1.00 18.11  ? 143 LEU   A CA  1 
ATOM   1059 C  C   . LEU   A 1 137 ? 24.783 4.416   4.156  1.00 20.79  ? 143 LEU   A C   1 
ATOM   1060 O  O   . LEU   A 1 137 ? 25.618 3.954   4.953  1.00 21.72  ? 143 LEU   A O   1 
ATOM   1061 C  CB  . LEU   A 1 137 ? 22.966 5.507   5.499  1.00 17.17  ? 143 LEU   A CB  1 
ATOM   1062 C  CG  . LEU   A 1 137 ? 22.406 6.731   6.172  1.00 17.47  ? 143 LEU   A CG  1 
ATOM   1063 C  CD1 . LEU   A 1 137 ? 21.137 6.331   6.910  1.00 18.25  ? 143 LEU   A CD1 1 
ATOM   1064 C  CD2 . LEU   A 1 137 ? 23.479 7.403   7.069  1.00 18.00  ? 143 LEU   A CD2 1 
ATOM   1065 N  N   . ASP   A 1 138 ? 24.426 3.777   3.002  1.00 22.06  ? 144 ASP   A N   1 
ATOM   1066 C  CA  . ASP   A 1 138 ? 24.952 2.468   2.584  1.00 24.45  ? 144 ASP   A CA  1 
ATOM   1067 C  C   . ASP   A 1 138 ? 26.321 2.506   1.910  1.00 28.56  ? 144 ASP   A C   1 
ATOM   1068 O  O   . ASP   A 1 138 ? 26.832 1.439   1.536  1.00 29.59  ? 144 ASP   A O   1 
ATOM   1069 C  CB  . ASP   A 1 138 ? 23.964 1.742   1.630  1.00 26.10  ? 144 ASP   A CB  1 
ATOM   1070 C  CG  . ASP   A 1 138 ? 22.619 1.391   2.222  1.00 29.05  ? 144 ASP   A CG  1 
ATOM   1071 O  OD1 . ASP   A 1 138 ? 22.487 1.446   3.466  1.00 28.43  ? 144 ASP   A OD1 1 
ATOM   1072 O  OD2 . ASP   A 1 138 ? 21.685 1.083   1.445  1.00 34.37  ? 144 ASP   A OD2 1 
ATOM   1073 N  N   . GLU   A 1 139 ? 26.912 3.689   1.713  1.00 30.60  ? 145 GLU   A N   1 
ATOM   1074 C  CA  . GLU   A 1 139 ? 28.204 3.778   1.016  1.00 34.00  ? 145 GLU   A CA  1 
ATOM   1075 C  C   . GLU   A 1 139 ? 29.108 4.899   1.565  1.00 36.55  ? 145 GLU   A C   1 
ATOM   1076 O  O   . GLU   A 1 139 ? 28.679 5.656   2.434  1.00 36.04  ? 145 GLU   A O   1 
ATOM   1077 C  CB  . GLU   A 1 139 ? 27.905 4.012   -0.473 1.00 37.17  ? 145 GLU   A CB  1 
ATOM   1078 C  CG  . GLU   A 1 139 ? 27.340 5.395   -0.752 1.00 43.03  ? 145 GLU   A CG  1 
ATOM   1079 C  CD  . GLU   A 1 139 ? 26.139 5.423   -1.677 1.00 50.37  ? 145 GLU   A CD  1 
ATOM   1080 O  OE1 . GLU   A 1 139 ? 25.810 6.523   -2.181 1.00 50.46  ? 145 GLU   A OE1 1 
ATOM   1081 O  OE2 . GLU   A 1 139 ? 25.517 4.354   -1.890 1.00 53.88  ? 145 GLU   A OE2 1 
ATOM   1082 N  N   . GLU   A 1 140 ? 30.348 5.010   1.046  1.00 39.09  ? 146 GLU   A N   1 
ATOM   1083 C  CA  . GLU   A 1 140 ? 31.286 6.105   1.352  1.00 42.26  ? 146 GLU   A CA  1 
ATOM   1084 C  C   . GLU   A 1 140 ? 31.406 6.385   2.862  1.00 44.52  ? 146 GLU   A C   1 
ATOM   1085 O  O   . GLU   A 1 140 ? 32.339 7.048   3.321  1.00 45.83  ? 146 GLU   A O   1 
ATOM   1086 C  CB  . GLU   A 1 140 ? 30.867 7.350   0.522  1.00 46.05  ? 146 GLU   A CB  1 
ATOM   1087 C  CG  . GLU   A 1 140 ? 31.020 8.734   1.144  1.00 54.09  ? 146 GLU   A CG  1 
ATOM   1088 C  CD  . GLU   A 1 140 ? 32.271 9.505   0.766  1.00 63.05  ? 146 GLU   A CD  1 
ATOM   1089 O  OE1 . GLU   A 1 140 ? 32.161 10.729  0.521  1.00 65.71  ? 146 GLU   A OE1 1 
ATOM   1090 O  OE2 . GLU   A 1 140 ? 33.362 8.892   0.719  1.00 65.53  ? 146 GLU   A OE2 1 
ATOM   1091 N  N   . SER   B 1 1   ? 21.805 -21.230 7.542  1.00 19.54  ? 7   SER   C N   1 
ATOM   1092 C  CA  . SER   B 1 1   ? 20.651 -21.062 8.447  1.00 19.19  ? 7   SER   C CA  1 
ATOM   1093 C  C   . SER   B 1 1   ? 20.615 -22.179 9.520  1.00 19.43  ? 7   SER   C C   1 
ATOM   1094 O  O   . SER   B 1 1   ? 21.286 -23.223 9.396  1.00 21.01  ? 7   SER   C O   1 
ATOM   1095 C  CB  . SER   B 1 1   ? 19.369 -21.142 7.618  1.00 21.78  ? 7   SER   C CB  1 
ATOM   1096 O  OG  . SER   B 1 1   ? 19.268 -22.422 7.018  1.00 26.63  ? 7   SER   C OG  1 
ATOM   1097 N  N   . GLY   B 1 2   ? 19.797 -21.962 10.553 1.00 18.89  ? 8   GLY   C N   1 
ATOM   1098 C  CA  . GLY   B 1 2   ? 19.649 -22.952 11.620 1.00 18.31  ? 8   GLY   C CA  1 
ATOM   1099 C  C   . GLY   B 1 2   ? 19.375 -22.339 12.974 1.00 17.02  ? 8   GLY   C C   1 
ATOM   1100 O  O   . GLY   B 1 2   ? 19.758 -21.211 13.242 1.00 17.94  ? 8   GLY   C O   1 
ATOM   1101 N  N   . ALA   B 1 3   ? 18.718 -23.085 13.846 1.00 16.79  ? 9   ALA   C N   1 
ATOM   1102 C  CA  . ALA   B 1 3   ? 18.358 -22.604 15.192 1.00 16.70  ? 9   ALA   C CA  1 
ATOM   1103 C  C   . ALA   B 1 3   ? 18.502 -23.726 16.233 1.00 15.17  ? 9   ALA   C C   1 
ATOM   1104 O  O   . ALA   B 1 3   ? 18.583 -24.908 15.862 1.00 16.72  ? 9   ALA   C O   1 
ATOM   1105 C  CB  . ALA   B 1 3   ? 16.902 -22.103 15.172 1.00 18.65  ? 9   ALA   C CB  1 
ATOM   1106 N  N   . ILE   B 1 4   ? 18.499 -23.350 17.527 1.00 14.91  ? 10  ILE   C N   1 
ATOM   1107 C  CA  . ILE   B 1 4   ? 18.431 -24.308 18.641 1.00 15.12  ? 10  ILE   C CA  1 
ATOM   1108 C  C   . ILE   B 1 4   ? 17.002 -24.113 19.245 1.00 15.72  ? 10  ILE   C C   1 
ATOM   1109 O  O   . ILE   B 1 4   ? 16.564 -22.971 19.437 1.00 17.25  ? 10  ILE   C O   1 
ATOM   1110 C  CB  . ILE   B 1 4   ? 19.477 -23.979 19.712 1.00 15.37  ? 10  ILE   C CB  1 
ATOM   1111 C  CG1 . ILE   B 1 4   ? 20.896 -23.832 19.116 1.00 17.36  ? 10  ILE   C CG1 1 
ATOM   1112 C  CG2 . ILE   B 1 4   ? 19.390 -25.033 20.853 1.00 16.87  ? 10  ILE   C CG2 1 
ATOM   1113 C  CD1 . ILE   B 1 4   ? 21.861 -23.180 20.142 1.00 16.55  ? 10  ILE   C CD1 1 
ATOM   1114 N  N   . TYR   B 1 5   ? 16.294 -25.201 19.526 1.00 15.27  ? 11  TYR   C N   1 
ATOM   1115 C  CA  . TYR   B 1 5   ? 14.969 -25.150 20.116 1.00 16.14  ? 11  TYR   C CA  1 
ATOM   1116 C  C   . TYR   B 1 5   ? 15.011 -25.827 21.487 1.00 16.73  ? 11  TYR   C C   1 
ATOM   1117 O  O   . TYR   B 1 5   ? 15.086 -27.057 21.556 1.00 17.50  ? 11  TYR   C O   1 
ATOM   1118 C  CB  . TYR   B 1 5   ? 13.943 -25.878 19.194 1.00 17.09  ? 11  TYR   C CB  1 
ATOM   1119 C  CG  . TYR   B 1 5   ? 13.751 -25.129 17.888 1.00 17.19  ? 11  TYR   C CG  1 
ATOM   1120 C  CD1 . TYR   B 1 5   ? 12.895 -24.036 17.811 1.00 17.70  ? 11  TYR   C CD1 1 
ATOM   1121 C  CD2 . TYR   B 1 5   ? 14.461 -25.483 16.747 1.00 18.23  ? 11  TYR   C CD2 1 
ATOM   1122 C  CE1 . TYR   B 1 5   ? 12.766 -23.304 16.636 1.00 20.18  ? 11  TYR   C CE1 1 
ATOM   1123 C  CE2 . TYR   B 1 5   ? 14.344 -24.764 15.565 1.00 19.90  ? 11  TYR   C CE2 1 
ATOM   1124 C  CZ  . TYR   B 1 5   ? 13.481 -23.684 15.511 1.00 20.69  ? 11  TYR   C CZ  1 
ATOM   1125 O  OH  . TYR   B 1 5   ? 13.344 -22.975 14.342 1.00 23.16  ? 11  TYR   C OH  1 
ATOM   1126 N  N   . VAL   B 1 6   ? 15.066 -25.070 22.582 1.00 17.45  ? 12  VAL   C N   1 
ATOM   1127 C  CA  . VAL   B 1 6   ? 15.130 -25.595 23.962 1.00 19.01  ? 12  VAL   C CA  1 
ATOM   1128 C  C   . VAL   B 1 6   ? 14.000 -24.992 24.777 1.00 20.41  ? 12  VAL   C C   1 
ATOM   1129 O  O   . VAL   B 1 6   ? 13.817 -23.779 24.767 1.00 18.77  ? 12  VAL   C O   1 
ATOM   1130 C  CB  . VAL   B 1 6   ? 16.537 -25.322 24.550 1.00 20.38  ? 12  VAL   C CB  1 
ATOM   1131 C  CG1 . VAL   B 1 6   ? 16.911 -23.828 24.449 1.00 21.28  ? 12  VAL   C CG1 1 
ATOM   1132 C  CG2 . VAL   B 1 6   ? 16.634 -25.817 25.972 1.00 21.57  ? 12  VAL   C CG2 1 
ATOM   1133 N  N   . GLY   B 1 7   ? 13.171 -25.818 25.427 1.00 20.09  ? 13  GLY   C N   1 
ATOM   1134 C  CA  . GLY   B 1 7   ? 12.051 -25.311 26.207 1.00 20.88  ? 13  GLY   C CA  1 
ATOM   1135 C  C   . GLY   B 1 7   ? 11.121 -24.480 25.345 1.00 21.04  ? 13  GLY   C C   1 
ATOM   1136 O  O   . GLY   B 1 7   ? 10.853 -24.861 24.205 1.00 22.30  ? 13  GLY   C O   1 
ATOM   1137 N  N   . ASN   B 1 8   ? 10.783 -23.292 25.800 1.00 20.46  ? 14  ASN   C N   1 
ATOM   1138 C  CA  . ASN   B 1 8   ? 9.977  -22.381 24.964 1.00 20.80  ? 14  ASN   C CA  1 
ATOM   1139 C  C   . ASN   B 1 8   ? 10.838 -21.276 24.354 1.00 19.85  ? 14  ASN   C C   1 
ATOM   1140 O  O   . ASN   B 1 8   ? 10.363 -20.148 24.191 1.00 19.94  ? 14  ASN   C O   1 
ATOM   1141 C  CB  . ASN   B 1 8   ? 8.757  -21.805 25.707 1.00 23.58  ? 14  ASN   C CB  1 
ATOM   1142 C  CG  . ASN   B 1 8   ? 7.662  -22.840 25.814 1.00 30.24  ? 14  ASN   C CG  1 
ATOM   1143 O  OD1 . ASN   B 1 8   ? 6.805  -22.971 24.926 1.00 31.61  ? 14  ASN   C OD1 1 
ATOM   1144 N  ND2 . ASN   B 1 8   ? 7.732  -23.640 26.861 1.00 32.81  ? 14  ASN   C ND2 1 
ATOM   1145 N  N   . TYR   B 1 9   ? 12.084 -21.614 23.974 1.00 18.10  ? 15  TYR   C N   1 
ATOM   1146 C  CA  . TYR   B 1 9   ? 13.016 -20.652 23.381 1.00 17.35  ? 15  TYR   C CA  1 
ATOM   1147 C  C   . TYR   B 1 9   ? 13.506 -21.148 22.020 1.00 16.42  ? 15  TYR   C C   1 
ATOM   1148 O  O   . TYR   B 1 9   ? 13.711 -22.366 21.809 1.00 17.53  ? 15  TYR   C O   1 
ATOM   1149 C  CB  . TYR   B 1 9   ? 14.246 -20.463 24.287 1.00 18.52  ? 15  TYR   C CB  1 
ATOM   1150 C  CG  . TYR   B 1 9   ? 13.942 -19.950 25.687 1.00 20.72  ? 15  TYR   C CG  1 
ATOM   1151 C  CD1 . TYR   B 1 9   ? 13.330 -18.722 25.881 1.00 22.46  ? 15  TYR   C CD1 1 
ATOM   1152 C  CD2 . TYR   B 1 9   ? 14.251 -20.710 26.812 1.00 23.05  ? 15  TYR   C CD2 1 
ATOM   1153 C  CE1 . TYR   B 1 9   ? 13.037 -18.257 27.165 1.00 25.66  ? 15  TYR   C CE1 1 
ATOM   1154 C  CE2 . TYR   B 1 9   ? 13.983 -20.245 28.098 1.00 25.33  ? 15  TYR   C CE2 1 
ATOM   1155 C  CZ  . TYR   B 1 9   ? 13.397 -19.009 28.267 1.00 28.06  ? 15  TYR   C CZ  1 
ATOM   1156 O  OH  . TYR   B 1 9   ? 13.117 -18.533 29.529 1.00 33.34  ? 15  TYR   C OH  1 
ATOM   1157 N  N   . ARG   B 1 10  ? 13.754 -20.193 21.120 1.00 16.43  ? 16  ARG   C N   1 
ATOM   1158 C  CA  . ARG   B 1 10  ? 14.365 -20.436 19.813 1.00 15.75  ? 16  ARG   C CA  1 
ATOM   1159 C  C   . ARG   B 1 10  ? 15.649 -19.565 19.800 1.00 15.37  ? 16  ARG   C C   1 
ATOM   1160 O  O   . ARG   B 1 10  ? 15.551 -18.353 20.009 1.00 15.79  ? 16  ARG   C O   1 
ATOM   1161 C  CB  . ARG   B 1 10  ? 13.402 -20.017 18.684 1.00 17.04  ? 16  ARG   C CB  1 
ATOM   1162 C  CG  . ARG   B 1 10  ? 14.030 -19.803 17.297 1.00 18.95  ? 16  ARG   C CG  1 
ATOM   1163 C  CD  . ARG   B 1 10  ? 12.990 -19.553 16.221 1.00 17.63  ? 16  ARG   C CD  1 
ATOM   1164 N  NE  . ARG   B 1 10  ? 13.443 -18.596 15.209 1.00 19.52  ? 16  ARG   C NE  1 
ATOM   1165 C  CZ  . ARG   B 1 10  ? 13.934 -18.909 14.012 1.00 20.82  ? 16  ARG   C CZ  1 
ATOM   1166 N  NH1 . ARG   B 1 10  ? 14.153 -20.186 13.684 1.00 22.25  ? 16  ARG   C NH1 1 
ATOM   1167 N  NH2 . ARG   B 1 10  ? 14.328 -17.948 13.175 1.00 19.68  ? 16  ARG   C NH2 1 
ATOM   1168 N  N   . VAL   B 1 11  ? 16.835 -20.150 19.589 1.00 13.74  ? 17  VAL   C N   1 
ATOM   1169 C  CA  . VAL   B 1 11  ? 18.114 -19.402 19.570 1.00 14.87  ? 17  VAL   C CA  1 
ATOM   1170 C  C   . VAL   B 1 11  ? 18.602 -19.350 18.147 1.00 14.70  ? 17  VAL   C C   1 
ATOM   1171 O  O   . VAL   B 1 11  ? 18.775 -20.410 17.473 1.00 14.84  ? 17  VAL   C O   1 
ATOM   1172 C  CB  . VAL   B 1 11  ? 19.177 -20.115 20.425 1.00 16.60  ? 17  VAL   C CB  1 
ATOM   1173 C  CG1 . VAL   B 1 11  ? 20.451 -19.269 20.490 1.00 17.76  ? 17  VAL   C CG1 1 
ATOM   1174 C  CG2 . VAL   B 1 11  ? 18.633 -20.472 21.830 1.00 17.31  ? 17  VAL   C CG2 1 
ATOM   1175 N  N   . VAL   B 1 12  ? 18.837 -18.145 17.618 1.00 14.60  ? 18  VAL   C N   1 
ATOM   1176 C  CA  A VAL   B 1 12  ? 19.285 -17.939 16.232 0.50 14.49  ? 18  VAL   C CA  1 
ATOM   1177 C  CA  B VAL   B 1 12  ? 19.283 -17.988 16.236 0.50 16.09  ? 18  VAL   C CA  1 
ATOM   1178 C  C   . VAL   B 1 12  ? 20.443 -16.955 16.152 1.00 14.96  ? 18  VAL   C C   1 
ATOM   1179 O  O   . VAL   B 1 12  ? 20.678 -16.172 17.106 1.00 15.47  ? 18  VAL   C O   1 
ATOM   1180 C  CB  A VAL   B 1 12  ? 18.138 -17.431 15.305 0.50 13.69  ? 18  VAL   C CB  1 
ATOM   1181 C  CB  B VAL   B 1 12  ? 18.060 -17.561 15.365 0.50 18.79  ? 18  VAL   C CB  1 
ATOM   1182 C  CG1 A VAL   B 1 12  ? 17.151 -18.553 15.005 0.50 15.71  ? 18  VAL   C CG1 1 
ATOM   1183 C  CG1 B VAL   B 1 12  ? 18.419 -17.471 13.894 0.50 20.07  ? 18  VAL   C CG1 1 
ATOM   1184 C  CG2 A VAL   B 1 12  ? 17.493 -16.124 15.825 0.50 11.31  ? 18  VAL   C CG2 1 
ATOM   1185 C  CG2 B VAL   B 1 12  ? 16.891 -18.528 15.549 0.50 20.82  ? 18  VAL   C CG2 1 
ATOM   1186 N  N   . ASN   B 1 13  ? 21.118 -16.900 14.989 1.00 14.49  ? 19  ASN   C N   1 
ATOM   1187 C  CA  . ASN   B 1 13  ? 22.106 -15.839 14.789 1.00 13.25  ? 19  ASN   C CA  1 
ATOM   1188 C  C   . ASN   B 1 13  ? 21.293 -14.498 14.726 1.00 14.93  ? 19  ASN   C C   1 
ATOM   1189 O  O   . ASN   B 1 13  ? 20.275 -14.409 14.037 1.00 15.21  ? 19  ASN   C O   1 
ATOM   1190 C  CB  . ASN   B 1 13  ? 22.826 -15.990 13.423 1.00 14.45  ? 19  ASN   C CB  1 
ATOM   1191 C  CG  . ASN   B 1 13  ? 23.673 -17.258 13.363 1.00 14.69  ? 19  ASN   C CG  1 
ATOM   1192 O  OD1 . ASN   B 1 13  ? 23.205 -18.341 12.967 1.00 16.28  ? 19  ASN   C OD1 1 
ATOM   1193 N  ND2 . ASN   B 1 13  ? 24.925 -17.128 13.823 1.00 15.34  ? 19  ASN   C ND2 1 
ATOM   1194 N  N   . ARG   B 1 14  ? 21.780 -13.479 15.445 1.00 15.47  ? 20  ARG   C N   1 
ATOM   1195 C  CA  . ARG   B 1 14  ? 21.061 -12.176 15.457 1.00 15.13  ? 20  ARG   C CA  1 
ATOM   1196 C  C   . ARG   B 1 14  ? 20.906 -11.624 14.023 1.00 16.33  ? 20  ARG   C C   1 
ATOM   1197 O  O   . ARG   B 1 14  ? 19.837 -11.109 13.680 1.00 16.39  ? 20  ARG   C O   1 
ATOM   1198 C  CB  . ARG   B 1 14  ? 21.804 -11.201 16.348 1.00 14.97  ? 20  ARG   C CB  1 
ATOM   1199 C  CG  . ARG   B 1 14  ? 21.013 -9.862  16.550 1.00 15.97  ? 20  ARG   C CG  1 
ATOM   1200 C  CD  . ARG   B 1 14  ? 21.893 -8.899  17.327 1.00 16.18  ? 20  ARG   C CD  1 
ATOM   1201 N  NE  . ARG   B 1 14  ? 21.209 -7.652  17.771 1.00 16.72  ? 20  ARG   C NE  1 
ATOM   1202 C  CZ  . ARG   B 1 14  ? 21.132 -6.550  17.031 1.00 16.86  ? 20  ARG   C CZ  1 
ATOM   1203 N  NH1 . ARG   B 1 14  ? 21.524 -6.560  15.773 1.00 17.83  ? 20  ARG   C NH1 1 
ATOM   1204 N  NH2 . ARG   B 1 14  ? 20.601 -5.439  17.531 1.00 17.94  ? 20  ARG   C NH2 1 
ATOM   1205 N  N   . HIS   B 1 15  ? 21.949 -11.824 13.170 1.00 15.29  ? 21  HIS   C N   1 
ATOM   1206 C  CA  . HIS   B 1 15  ? 21.866 -11.293 11.803 1.00 16.15  ? 21  HIS   C CA  1 
ATOM   1207 C  C   . HIS   B 1 15  ? 20.851 -12.032 10.889 1.00 17.09  ? 21  HIS   C C   1 
ATOM   1208 O  O   . HIS   B 1 15  ? 20.540 -11.530 9.812  1.00 18.57  ? 21  HIS   C O   1 
ATOM   1209 C  CB  . HIS   B 1 15  ? 23.266 -11.223 11.169 1.00 16.53  ? 21  HIS   C CB  1 
ATOM   1210 C  CG  . HIS   B 1 15  ? 23.861 -12.527 10.716 1.00 17.02  ? 21  HIS   C CG  1 
ATOM   1211 N  ND1 . HIS   B 1 15  ? 24.582 -13.344 11.593 1.00 17.32  ? 21  HIS   C ND1 1 
ATOM   1212 C  CD2 . HIS   B 1 15  ? 23.865 -13.085 9.480  1.00 17.66  ? 21  HIS   C CD2 1 
ATOM   1213 C  CE1 . HIS   B 1 15  ? 24.980 -14.389 10.858 1.00 17.40  ? 21  HIS   C CE1 1 
ATOM   1214 N  NE2 . HIS   B 1 15  ? 24.584 -14.261 9.577  1.00 17.57  ? 21  HIS   C NE2 1 
ATOM   1215 N  N   . LEU   B 1 16  ? 20.351 -13.200 11.328 1.00 15.72  ? 22  LEU   C N   1 
ATOM   1216 C  CA  . LEU   B 1 16  ? 19.336 -13.992 10.602 1.00 16.89  ? 22  LEU   C CA  1 
ATOM   1217 C  C   . LEU   B 1 16  ? 17.951 -13.957 11.263 1.00 18.11  ? 22  LEU   C C   1 
ATOM   1218 O  O   . LEU   B 1 16  ? 17.034 -14.664 10.820 1.00 18.51  ? 22  LEU   C O   1 
ATOM   1219 C  CB  . LEU   B 1 16  ? 19.841 -15.438 10.416 1.00 17.38  ? 22  LEU   C CB  1 
ATOM   1220 C  CG  . LEU   B 1 16  ? 21.121 -15.550 9.593  1.00 16.91  ? 22  LEU   C CG  1 
ATOM   1221 C  CD1 . LEU   B 1 16  ? 21.591 -17.015 9.529  1.00 17.73  ? 22  LEU   C CD1 1 
ATOM   1222 C  CD2 . LEU   B 1 16  ? 20.931 -14.986 8.176  1.00 17.44  ? 22  LEU   C CD2 1 
ATOM   1223 N  N   . ALA   B 1 17  ? 17.780 -13.163 12.335 1.00 17.46  ? 23  ALA   C N   1 
ATOM   1224 C  CA  . ALA   B 1 17  ? 16.506 -13.107 13.048 1.00 17.59  ? 23  ALA   C CA  1 
ATOM   1225 C  C   . ALA   B 1 17  ? 15.395 -12.551 12.149 1.00 19.26  ? 23  ALA   C C   1 
ATOM   1226 O  O   . ALA   B 1 17  ? 15.606 -11.625 11.357 1.00 20.31  ? 23  ALA   C O   1 
ATOM   1227 C  CB  . ALA   B 1 17  ? 16.647 -12.252 14.323 1.00 18.31  ? 23  ALA   C CB  1 
ATOM   1228 N  N   . THR   B 1 18  ? 14.201 -13.109 12.296 1.00 19.61  ? 24  THR   C N   1 
ATOM   1229 C  CA  . THR   B 1 18  ? 13.041 -12.719 11.497 1.00 20.16  ? 24  THR   C CA  1 
ATOM   1230 C  C   . THR   B 1 18  ? 12.214 -11.656 12.255 1.00 19.40  ? 24  THR   C C   1 
ATOM   1231 O  O   . THR   B 1 18  ? 12.459 -11.378 13.436 1.00 19.98  ? 24  THR   C O   1 
ATOM   1232 C  CB  . THR   B 1 18  ? 12.142 -13.967 11.232 1.00 21.50  ? 24  THR   C CB  1 
ATOM   1233 O  OG1 . THR   B 1 18  ? 11.613 -14.407 12.485 1.00 22.13  ? 24  THR   C OG1 1 
ATOM   1234 C  CG2 . THR   B 1 18  ? 12.877 -15.137 10.532 1.00 22.55  ? 24  THR   C CG2 1 
ATOM   1235 N  N   . HIS   B 1 19  ? 11.179 -11.078 11.576 1.00 21.75  ? 25  HIS   C N   1 
ATOM   1236 C  CA  . HIS   B 1 19  ? 10.291 -10.156 12.286 1.00 23.12  ? 25  HIS   C CA  1 
ATOM   1237 C  C   . HIS   B 1 19  ? 9.584  -10.895 13.415 1.00 21.49  ? 25  HIS   C C   1 
ATOM   1238 O  O   . HIS   B 1 19  ? 9.525  -10.331 14.507 1.00 22.17  ? 25  HIS   C O   1 
ATOM   1239 C  CB  . HIS   B 1 19  ? 9.233  -9.566  11.356 1.00 25.09  ? 25  HIS   C CB  1 
ATOM   1240 C  CG  . HIS   B 1 19  ? 8.115  -8.853  12.079 1.00 27.39  ? 25  HIS   C CG  1 
ATOM   1241 N  ND1 . HIS   B 1 19  ? 8.330  -7.651  12.740 1.00 29.03  ? 25  HIS   C ND1 1 
ATOM   1242 C  CD2 . HIS   B 1 19  ? 6.860  -9.275  12.346 1.00 28.75  ? 25  HIS   C CD2 1 
ATOM   1243 C  CE1 . HIS   B 1 19  ? 7.160  -7.313  13.269 1.00 29.86  ? 25  HIS   C CE1 1 
ATOM   1244 N  NE2 . HIS   B 1 19  ? 6.247  -8.264  13.074 1.00 29.55  ? 25  HIS   C NE2 1 
ATOM   1245 N  N   . ASN   B 1 20  ? 9.151  -12.162 13.209 1.00 21.26  ? 26  ASN   C N   1 
ATOM   1246 C  CA  . ASN   B 1 20  ? 8.515  -12.899 14.298 1.00 21.89  ? 26  ASN   C CA  1 
ATOM   1247 C  C   . ASN   B 1 20  ? 9.445  -13.064 15.501 1.00 20.56  ? 26  ASN   C C   1 
ATOM   1248 O  O   . ASN   B 1 20  ? 9.031  -12.919 16.647 1.00 19.81  ? 26  ASN   C O   1 
ATOM   1249 C  CB  . ASN   B 1 20  ? 8.006  -14.237 13.822 1.00 23.24  ? 26  ASN   C CB  1 
ATOM   1250 C  CG  . ASN   B 1 20  ? 7.200  -14.947 14.895 1.00 28.53  ? 26  ASN   C CG  1 
ATOM   1251 O  OD1 . ASN   B 1 20  ? 6.047  -14.568 15.204 1.00 31.16  ? 26  ASN   C OD1 1 
ATOM   1252 N  ND2 . ASN   B 1 20  ? 7.772  -15.998 15.494 1.00 30.42  ? 26  ASN   C ND2 1 
ATOM   1253 N  N   . ASP   B 1 21  ? 10.784 -13.300 15.234 1.00 18.35  ? 27  ASP   C N   1 
ATOM   1254 C  CA  . ASP   B 1 21  ? 11.718 -13.359 16.336 1.00 18.03  ? 27  ASP   C CA  1 
ATOM   1255 C  C   . ASP   B 1 21  ? 11.750 -12.055 17.128 1.00 17.47  ? 27  ASP   C C   1 
ATOM   1256 O  O   . ASP   B 1 21  ? 11.711 -12.079 18.351 1.00 18.45  ? 27  ASP   C O   1 
ATOM   1257 C  CB  . ASP   B 1 21  ? 13.150 -13.676 15.839 1.00 17.72  ? 27  ASP   C CB  1 
ATOM   1258 C  CG  . ASP   B 1 21  ? 13.343 -15.095 15.345 1.00 17.51  ? 27  ASP   C CG  1 
ATOM   1259 O  OD1 . ASP   B 1 21  ? 12.760 -16.026 15.958 1.00 18.78  ? 27  ASP   C OD1 1 
ATOM   1260 O  OD2 . ASP   B 1 21  ? 14.016 -15.266 14.306 1.00 17.82  ? 27  ASP   C OD2 1 
ATOM   1261 N  N   . TRP   B 1 22  ? 11.848 -10.893 16.423 1.00 17.88  ? 28  TRP   C N   1 
ATOM   1262 C  CA  . TRP   B 1 22  ? 11.903 -9.621  17.121 1.00 18.04  ? 28  TRP   C CA  1 
ATOM   1263 C  C   . TRP   B 1 22  ? 10.543 -9.261  17.814 1.00 18.37  ? 28  TRP   C C   1 
ATOM   1264 O  O   . TRP   B 1 22  ? 10.554 -8.675  18.908 1.00 19.95  ? 28  TRP   C O   1 
ATOM   1265 C  CB  . TRP   B 1 22  ? 12.298 -8.519  16.126 1.00 18.54  ? 28  TRP   C CB  1 
ATOM   1266 C  CG  . TRP   B 1 22  ? 13.780 -8.455  15.849 1.00 18.97  ? 28  TRP   C CG  1 
ATOM   1267 C  CD1 . TRP   B 1 22  ? 14.428 -8.931  14.749 1.00 20.33  ? 28  TRP   C CD1 1 
ATOM   1268 C  CD2 . TRP   B 1 22  ? 14.782 -7.890  16.699 1.00 17.56  ? 28  TRP   C CD2 1 
ATOM   1269 N  NE1 . TRP   B 1 22  ? 15.787 -8.675  14.852 1.00 19.90  ? 28  TRP   C NE1 1 
ATOM   1270 C  CE2 . TRP   B 1 22  ? 16.030 -8.046  16.045 1.00 18.94  ? 28  TRP   C CE2 1 
ATOM   1271 C  CE3 . TRP   B 1 22  ? 14.750 -7.222  17.922 1.00 19.83  ? 28  TRP   C CE3 1 
ATOM   1272 C  CZ2 . TRP   B 1 22  ? 17.210 -7.518  16.549 1.00 19.80  ? 28  TRP   C CZ2 1 
ATOM   1273 C  CZ3 . TRP   B 1 22  ? 15.952 -6.764  18.452 1.00 20.73  ? 28  TRP   C CZ3 1 
ATOM   1274 C  CH2 . TRP   B 1 22  ? 17.157 -6.895  17.744 1.00 20.09  ? 28  TRP   C CH2 1 
ATOM   1275 N  N   . ALA   B 1 23  ? 9.437  -9.729  17.258 1.00 19.16  ? 29  ALA   C N   1 
ATOM   1276 C  CA  . ALA   B 1 23  ? 8.111  -9.483  17.856 1.00 19.37  ? 29  ALA   C CA  1 
ATOM   1277 C  C   . ALA   B 1 23  ? 7.848  -10.361 19.100 1.00 20.84  ? 29  ALA   C C   1 
ATOM   1278 O  O   . ALA   B 1 23  ? 6.880  -10.154 19.810 1.00 21.30  ? 29  ALA   C O   1 
ATOM   1279 C  CB  . ALA   B 1 23  ? 7.037  -9.756  16.833 1.00 19.85  ? 29  ALA   C CB  1 
ATOM   1280 N  N   . ASN   B 1 24  ? 8.677  -11.403 19.323 1.00 20.39  ? 30  ASN   C N   1 
ATOM   1281 C  CA  . ASN   B 1 24  ? 8.576  -12.309 20.469 1.00 20.77  ? 30  ASN   C CA  1 
ATOM   1282 C  C   . ASN   B 1 24  ? 9.963  -12.389 21.148 1.00 19.99  ? 30  ASN   C C   1 
ATOM   1283 O  O   . ASN   B 1 24  ? 10.384 -13.454 21.592 1.00 18.80  ? 30  ASN   C O   1 
ATOM   1284 C  CB  . ASN   B 1 24  ? 8.123  -13.684 19.944 1.00 21.38  ? 30  ASN   C CB  1 
ATOM   1285 C  CG  . ASN   B 1 24  ? 6.697  -13.640 19.471 1.00 22.79  ? 30  ASN   C CG  1 
ATOM   1286 O  OD1 . ASN   B 1 24  ? 5.762  -13.657 20.286 1.00 24.64  ? 30  ASN   C OD1 1 
ATOM   1287 N  ND2 . ASN   B 1 24  ? 6.488  -13.557 18.169 1.00 23.99  ? 30  ASN   C ND2 1 
ATOM   1288 N  N   . LEU   B 1 25  ? 10.683 -11.272 21.215 1.00 19.77  ? 31  LEU   C N   1 
ATOM   1289 C  CA  . LEU   B 1 25  ? 12.054 -11.236 21.747 1.00 19.79  ? 31  LEU   C CA  1 
ATOM   1290 C  C   . LEU   B 1 25  ? 12.188 -11.532 23.231 1.00 20.35  ? 31  LEU   C C   1 
ATOM   1291 O  O   . LEU   B 1 25  ? 11.423 -11.011 24.043 1.00 21.05  ? 31  LEU   C O   1 
ATOM   1292 C  CB  . LEU   B 1 25  ? 12.611 -9.856  21.443 1.00 20.29  ? 31  LEU   C CB  1 
ATOM   1293 C  CG  . LEU   B 1 25  ? 14.084 -9.647  21.841 1.00 20.10  ? 31  LEU   C CG  1 
ATOM   1294 C  CD1 . LEU   B 1 25  ? 15.038 -10.543 21.011 1.00 20.09  ? 31  LEU   C CD1 1 
ATOM   1295 C  CD2 . LEU   B 1 25  ? 14.467 -8.204  21.760 1.00 20.96  ? 31  LEU   C CD2 1 
ATOM   1296 N  N   . VAL   B 1 26  ? 13.165 -12.349 23.586 1.00 18.42  ? 32  VAL   C N   1 
ATOM   1297 C  CA  . VAL   B 1 26  ? 13.497 -12.640 24.990 1.00 19.57  ? 32  VAL   C CA  1 
ATOM   1298 C  C   . VAL   B 1 26  ? 14.819 -11.926 25.327 1.00 19.81  ? 32  VAL   C C   1 
ATOM   1299 O  O   . VAL   B 1 26  ? 14.923 -11.242 26.365 1.00 21.00  ? 32  VAL   C O   1 
ATOM   1300 C  CB  . VAL   B 1 26  ? 13.631 -14.165 25.215 1.00 20.90  ? 32  VAL   C CB  1 
ATOM   1301 C  CG1 . VAL   B 1 26  ? 14.156 -14.489 26.622 1.00 22.66  ? 32  VAL   C CG1 1 
ATOM   1302 C  CG2 . VAL   B 1 26  ? 12.290 -14.863 25.003 1.00 21.35  ? 32  VAL   C CG2 1 
ATOM   1303 N  N   . TRP   B 1 27  ? 15.830 -12.047 24.450 1.00 18.24  ? 33  TRP   C N   1 
ATOM   1304 C  CA  . TRP   B 1 27  ? 17.144 -11.461 24.726 1.00 19.10  ? 33  TRP   C CA  1 
ATOM   1305 C  C   . TRP   B 1 27  ? 17.923 -11.409 23.415 1.00 18.34  ? 33  TRP   C C   1 
ATOM   1306 O  O   . TRP   B 1 27  ? 17.774 -12.292 22.554 1.00 17.56  ? 33  TRP   C O   1 
ATOM   1307 C  CB  . TRP   B 1 27  ? 17.877 -12.379 25.734 1.00 20.07  ? 33  TRP   C CB  1 
ATOM   1308 C  CG  . TRP   B 1 27  ? 19.343 -12.110 25.953 1.00 20.49  ? 33  TRP   C CG  1 
ATOM   1309 C  CD1 . TRP   B 1 27  ? 19.897 -11.182 26.792 1.00 22.55  ? 33  TRP   C CD1 1 
ATOM   1310 C  CD2 . TRP   B 1 27  ? 20.440 -12.801 25.345 1.00 19.51  ? 33  TRP   C CD2 1 
ATOM   1311 N  NE1 . TRP   B 1 27  ? 21.274 -11.281 26.768 1.00 23.30  ? 33  TRP   C NE1 1 
ATOM   1312 C  CE2 . TRP   B 1 27  ? 21.631 -12.267 25.885 1.00 21.16  ? 33  TRP   C CE2 1 
ATOM   1313 C  CE3 . TRP   B 1 27  ? 20.534 -13.784 24.354 1.00 19.75  ? 33  TRP   C CE3 1 
ATOM   1314 C  CZ2 . TRP   B 1 27  ? 22.890 -12.704 25.492 1.00 20.77  ? 33  TRP   C CZ2 1 
ATOM   1315 C  CZ3 . TRP   B 1 27  ? 21.786 -14.277 24.031 1.00 20.70  ? 33  TRP   C CZ3 1 
ATOM   1316 C  CH2 . TRP   B 1 27  ? 22.944 -13.672 24.529 1.00 20.79  ? 33  TRP   C CH2 1 
ATOM   1317 N  N   . GLU   B 1 28  ? 18.787 -10.409 23.277 1.00 17.68  ? 34  GLU   C N   1 
ATOM   1318 C  CA  . GLU   B 1 28  ? 19.648 -10.309 22.108 1.00 18.63  ? 34  GLU   C CA  1 
ATOM   1319 C  C   . GLU   B 1 28  ? 20.945 -9.636  22.490 1.00 17.59  ? 34  GLU   C C   1 
ATOM   1320 O  O   . GLU   B 1 28  ? 20.955 -8.746  23.388 1.00 18.17  ? 34  GLU   C O   1 
ATOM   1321 C  CB  . GLU   B 1 28  ? 18.985 -9.621  20.911 1.00 19.32  ? 34  GLU   C CB  1 
ATOM   1322 C  CG  . GLU   B 1 28  ? 18.435 -8.245  21.245 1.00 21.14  ? 34  GLU   C CG  1 
ATOM   1323 C  CD  . GLU   B 1 28  ? 19.399 -7.077  21.139 1.00 22.05  ? 34  GLU   C CD  1 
ATOM   1324 O  OE1 . GLU   B 1 28  ? 19.113 -6.046  21.787 1.00 25.12  ? 34  GLU   C OE1 1 
ATOM   1325 O  OE2 . GLU   B 1 28  ? 20.415 -7.155  20.405 1.00 21.04  ? 34  GLU   C OE2 1 
ATOM   1326 N  N   . ASP   B 1 29  ? 22.028 -9.962  21.773 1.00 16.48  ? 35  ASP   C N   1 
ATOM   1327 C  CA  . ASP   B 1 29  ? 23.321 -9.342  22.003 1.00 17.18  ? 35  ASP   C CA  1 
ATOM   1328 C  C   . ASP   B 1 29  ? 24.107 -9.281  20.675 1.00 17.33  ? 35  ASP   C C   1 
ATOM   1329 O  O   . ASP   B 1 29  ? 24.546 -10.324 20.162 1.00 17.11  ? 35  ASP   C O   1 
ATOM   1330 C  CB  . ASP   B 1 29  ? 24.020 -10.118 23.123 1.00 18.67  ? 35  ASP   C CB  1 
ATOM   1331 C  CG  . ASP   B 1 29  ? 25.375 -9.589  23.521 1.00 24.15  ? 35  ASP   C CG  1 
ATOM   1332 O  OD1 . ASP   B 1 29  ? 26.063 -8.994  22.661 1.00 25.74  ? 35  ASP   C OD1 1 
ATOM   1333 O  OD2 . ASP   B 1 29  ? 25.754 -9.763  24.706 1.00 26.52  ? 35  ASP   C OD2 1 
ATOM   1334 N  N   . SER   B 1 30  ? 24.270 -8.062  20.106 1.00 17.94  ? 36  SER   C N   1 
ATOM   1335 C  CA  A SER   B 1 30  ? 24.986 -7.886  18.837 0.50 18.71  ? 36  SER   C CA  1 
ATOM   1336 C  CA  B SER   B 1 30  ? 24.972 -7.920  18.835 0.50 18.58  ? 36  SER   C CA  1 
ATOM   1337 C  C   . SER   B 1 30  ? 26.451 -8.301  18.919 1.00 18.92  ? 36  SER   C C   1 
ATOM   1338 O  O   . SER   B 1 30  ? 26.961 -8.918  17.967 1.00 19.81  ? 36  SER   C O   1 
ATOM   1339 C  CB  A SER   B 1 30  ? 24.877 -6.449  18.336 0.50 20.24  ? 36  SER   C CB  1 
ATOM   1340 C  CB  B SER   B 1 30  ? 24.783 -6.522  18.264 0.50 19.71  ? 36  SER   C CB  1 
ATOM   1341 O  OG  A SER   B 1 30  ? 25.822 -6.182  17.304 0.50 22.32  ? 36  SER   C OG  1 
ATOM   1342 O  OG  B SER   B 1 30  ? 25.229 -5.540  19.181 0.50 20.82  ? 36  SER   C OG  1 
ATOM   1343 N  N   . SER   B 1 31  ? 27.092 -8.062  20.072 1.00 18.71  ? 37  SER   C N   1 
ATOM   1344 C  CA  . SER   B 1 31  ? 28.492 -8.461  20.210 1.00 19.56  ? 37  SER   C CA  1 
ATOM   1345 C  C   . SER   B 1 31  ? 28.693 -9.978  20.139 1.00 18.68  ? 37  SER   C C   1 
ATOM   1346 O  O   . SER   B 1 31  ? 29.789 -10.439 19.795 1.00 19.49  ? 37  SER   C O   1 
ATOM   1347 C  CB  . SER   B 1 31  ? 29.095 -7.920  21.507 1.00 22.68  ? 37  SER   C CB  1 
ATOM   1348 O  OG  . SER   B 1 31  ? 28.644 -8.603  22.663 1.00 28.40  ? 37  SER   C OG  1 
ATOM   1349 N  N   . ARG   B 1 32  ? 27.643 -10.757 20.465 1.00 18.23  ? 38  ARG   C N   1 
ATOM   1350 C  CA  . ARG   B 1 32  ? 27.707 -12.219 20.404 1.00 17.45  ? 38  ARG   C CA  1 
ATOM   1351 C  C   . ARG   B 1 32  ? 27.072 -12.818 19.144 1.00 16.33  ? 38  ARG   C C   1 
ATOM   1352 O  O   . ARG   B 1 32  ? 27.182 -14.037 18.925 1.00 16.80  ? 38  ARG   C O   1 
ATOM   1353 C  CB  . ARG   B 1 32  ? 26.980 -12.831 21.609 1.00 19.61  ? 38  ARG   C CB  1 
ATOM   1354 C  CG  . ARG   B 1 32  ? 27.599 -12.467 22.953 1.00 21.31  ? 38  ARG   C CG  1 
ATOM   1355 C  CD  . ARG   B 1 32  ? 26.858 -13.051 24.152 1.00 19.05  ? 38  ARG   C CD  1 
ATOM   1356 N  NE  . ARG   B 1 32  ? 26.957 -14.519 24.197 1.00 17.93  ? 38  ARG   C NE  1 
ATOM   1357 C  CZ  . ARG   B 1 32  ? 26.931 -15.249 25.307 1.00 19.02  ? 38  ARG   C CZ  1 
ATOM   1358 N  NH1 . ARG   B 1 32  ? 26.820 -14.662 26.499 1.00 21.48  ? 38  ARG   C NH1 1 
ATOM   1359 N  NH2 . ARG   B 1 32  ? 27.050 -16.568 25.239 1.00 18.25  ? 38  ARG   C NH2 1 
ATOM   1360 N  N   . ASP   B 1 33  ? 26.431 -11.984 18.304 1.00 16.17  ? 39  ASP   C N   1 
ATOM   1361 C  CA  . ASP   B 1 33  ? 25.637 -12.428 17.150 1.00 15.54  ? 39  ASP   C CA  1 
ATOM   1362 C  C   . ASP   B 1 33  ? 24.548 -13.429 17.597 1.00 15.29  ? 39  ASP   C C   1 
ATOM   1363 O  O   . ASP   B 1 33  ? 24.274 -14.355 16.842 1.00 15.47  ? 39  ASP   C O   1 
ATOM   1364 C  CB  . ASP   B 1 33  ? 26.510 -13.048 16.052 1.00 16.18  ? 39  ASP   C CB  1 
ATOM   1365 C  CG  . ASP   B 1 33  ? 25.743 -13.376 14.762 1.00 17.35  ? 39  ASP   C CG  1 
ATOM   1366 O  OD1 . ASP   B 1 33  ? 24.854 -12.587 14.381 1.00 17.47  ? 39  ASP   C OD1 1 
ATOM   1367 O  OD2 . ASP   B 1 33  ? 26.047 -14.414 14.130 1.00 16.29  ? 39  ASP   C OD2 1 
ATOM   1368 N  N   . LEU   B 1 34  ? 23.881 -13.215 18.738 1.00 14.48  ? 40  LEU   C N   1 
ATOM   1369 C  CA  . LEU   B 1 34  ? 22.806 -14.115 19.182 1.00 14.80  ? 40  LEU   C CA  1 
ATOM   1370 C  C   . LEU   B 1 34  ? 21.494 -13.369 19.431 1.00 14.37  ? 40  LEU   C C   1 
ATOM   1371 O  O   . LEU   B 1 34  ? 21.501 -12.214 19.905 1.00 15.46  ? 40  LEU   C O   1 
ATOM   1372 C  CB  . LEU   B 1 34  ? 23.193 -14.794 20.520 1.00 15.50  ? 40  LEU   C CB  1 
ATOM   1373 C  CG  . LEU   B 1 34  ? 24.283 -15.890 20.424 1.00 15.58  ? 40  LEU   C CG  1 
ATOM   1374 C  CD1 . LEU   B 1 34  ? 24.530 -16.506 21.848 1.00 17.97  ? 40  LEU   C CD1 1 
ATOM   1375 C  CD2 . LEU   B 1 34  ? 23.869 -17.034 19.440 1.00 16.17  ? 40  LEU   C CD2 1 
ATOM   1376 N  N   . LEU   B 1 35  ? 20.375 -14.063 19.222 1.00 13.67  ? 41  LEU   C N   1 
ATOM   1377 C  CA  . LEU   B 1 35  ? 19.050 -13.554 19.538 1.00 16.11  ? 41  LEU   C CA  1 
ATOM   1378 C  C   . LEU   B 1 35  ? 18.222 -14.781 19.970 1.00 15.66  ? 41  LEU   C C   1 
ATOM   1379 O  O   . LEU   B 1 35  ? 18.325 -15.857 19.364 1.00 16.42  ? 41  LEU   C O   1 
ATOM   1380 C  CB  . LEU   B 1 35  ? 18.444 -12.851 18.306 1.00 15.78  ? 41  LEU   C CB  1 
ATOM   1381 C  CG  . LEU   B 1 35  ? 17.046 -12.232 18.574 1.00 15.25  ? 41  LEU   C CG  1 
ATOM   1382 C  CD1 . LEU   B 1 35  ? 16.839 -10.937 17.808 1.00 17.12  ? 41  LEU   C CD1 1 
ATOM   1383 C  CD2 . LEU   B 1 35  ? 15.924 -13.257 18.214 1.00 16.84  ? 41  LEU   C CD2 1 
ATOM   1384 N  N   . VAL   B 1 36  ? 17.417 -14.600 21.006 1.00 15.02  ? 42  VAL   C N   1 
ATOM   1385 C  CA  . VAL   B 1 36  ? 16.539 -15.635 21.544 1.00 14.76  ? 42  VAL   C CA  1 
ATOM   1386 C  C   . VAL   B 1 36  ? 15.124 -15.098 21.507 1.00 15.34  ? 42  VAL   C C   1 
ATOM   1387 O  O   . VAL   B 1 36  ? 14.868 -13.982 22.008 1.00 16.85  ? 42  VAL   C O   1 
ATOM   1388 C  CB  . VAL   B 1 36  ? 16.923 -16.094 22.959 1.00 15.93  ? 42  VAL   C CB  1 
ATOM   1389 C  CG1 . VAL   B 1 36  ? 15.949 -17.147 23.482 1.00 18.10  ? 42  VAL   C CG1 1 
ATOM   1390 C  CG2 . VAL   B 1 36  ? 18.360 -16.655 22.955 1.00 16.45  ? 42  VAL   C CG2 1 
ATOM   1391 N  N   . SER   B 1 37  ? 14.194 -15.870 20.925 1.00 15.75  ? 43  SER   C N   1 
ATOM   1392 C  CA  . SER   B 1 37  ? 12.764 -15.549 20.900 1.00 15.88  ? 43  SER   C CA  1 
ATOM   1393 C  C   . SER   B 1 37  ? 11.969 -16.624 21.593 1.00 17.26  ? 43  SER   C C   1 
ATOM   1394 O  O   . SER   B 1 37  ? 12.473 -17.724 21.845 1.00 17.28  ? 43  SER   C O   1 
ATOM   1395 C  CB  . SER   B 1 37  ? 12.292 -15.331 19.474 1.00 16.40  ? 43  SER   C CB  1 
ATOM   1396 O  OG  . SER   B 1 37  ? 12.467 -16.486 18.668 1.00 19.54  ? 43  SER   C OG  1 
ATOM   1397 N  N   . SER   B 1 38  ? 10.723 -16.301 21.965 1.00 17.83  ? 44  SER   C N   1 
ATOM   1398 C  CA  . SER   B 1 38  ? 9.860  -17.268 22.630 1.00 18.62  ? 44  SER   C CA  1 
ATOM   1399 C  C   . SER   B 1 38  ? 9.032  -18.082 21.606 1.00 20.95  ? 44  SER   C C   1 
ATOM   1400 O  O   . SER   B 1 38  ? 8.732  -17.610 20.512 1.00 21.84  ? 44  SER   C O   1 
ATOM   1401 C  CB  . SER   B 1 38  ? 8.931  -16.557 23.620 1.00 20.99  ? 44  SER   C CB  1 
ATOM   1402 O  OG  . SER   B 1 38  ? 8.063  -15.663 22.937 1.00 26.07  ? 44  SER   C OG  1 
ATOM   1403 N  N   . THR   B 1 39  ? 8.701  -19.337 21.950 1.00 21.71  ? 45  THR   C N   1 
ATOM   1404 C  CA  . THR   B 1 39  ? 7.948  -20.211 21.056 1.00 22.84  ? 45  THR   C CA  1 
ATOM   1405 C  C   . THR   B 1 39  ? 6.661  -20.688 21.745 1.00 25.39  ? 45  THR   C C   1 
ATOM   1406 O  O   . THR   B 1 39  ? 6.627  -20.786 22.974 1.00 24.81  ? 45  THR   C O   1 
ATOM   1407 C  CB  . THR   B 1 39  ? 8.796  -21.470 20.705 1.00 23.28  ? 45  THR   C CB  1 
ATOM   1408 O  OG1 . THR   B 1 39  ? 9.043  -22.203 21.902 1.00 24.28  ? 45  THR   C OG1 1 
ATOM   1409 C  CG2 . THR   B 1 39  ? 10.147 -21.125 20.003 1.00 24.69  ? 45  THR   C CG2 1 
ATOM   1410 N  N   . THR   B 1 40  ? 5.680  -21.089 20.944 1.00 26.95  ? 46  THR   C N   1 
ATOM   1411 C  CA  . THR   B 1 40  ? 4.443  -21.635 21.526 1.00 28.82  ? 46  THR   C CA  1 
ATOM   1412 C  C   . THR   B 1 40  ? 4.651  -23.109 21.878 1.00 30.22  ? 46  THR   C C   1 
ATOM   1413 O  O   . THR   B 1 40  ? 4.237  -23.556 22.954 1.00 31.89  ? 46  THR   C O   1 
ATOM   1414 C  CB  . THR   B 1 40  ? 3.262  -21.336 20.619 1.00 33.56  ? 46  THR   C CB  1 
ATOM   1415 O  OG1 . THR   B 1 40  ? 3.539  -21.878 19.329 1.00 37.50  ? 46  THR   C OG1 1 
ATOM   1416 C  CG2 . THR   B 1 40  ? 3.035  -19.852 20.476 1.00 33.17  ? 46  THR   C CG2 1 
ATOM   1417 N  N   . ALA   B 1 41  ? 5.330  -23.861 21.000 1.00 29.69  ? 47  ALA   C N   1 
ATOM   1418 C  CA  . ALA   B 1 41  ? 5.608  -25.271 21.269 1.00 29.76  ? 47  ALA   C CA  1 
ATOM   1419 C  C   . ALA   B 1 41  ? 6.934  -25.489 21.993 1.00 28.46  ? 47  ALA   C C   1 
ATOM   1420 O  O   . ALA   B 1 41  ? 7.868  -24.722 21.793 1.00 27.06  ? 47  ALA   C O   1 
ATOM   1421 C  CB  . ALA   B 1 41  ? 5.611  -26.062 19.971 1.00 31.03  ? 47  ALA   C CB  1 
ATOM   1422 N  N   . GLN   B 1 42  ? 7.046  -26.572 22.773 1.00 28.19  ? 48  GLN   C N   1 
ATOM   1423 C  CA  . GLN   B 1 42  ? 8.283  -26.874 23.464 1.00 27.86  ? 48  GLN   C CA  1 
ATOM   1424 C  C   . GLN   B 1 42  ? 9.259  -27.536 22.502 1.00 25.94  ? 48  GLN   C C   1 
ATOM   1425 O  O   . GLN   B 1 42  ? 8.875  -28.340 21.647 1.00 26.73  ? 48  GLN   C O   1 
ATOM   1426 C  CB  . GLN   B 1 42  ? 8.036  -27.742 24.705 1.00 31.26  ? 48  GLN   C CB  1 
ATOM   1427 C  CG  . GLN   B 1 42  ? 7.361  -26.947 25.812 1.00 38.88  ? 48  GLN   C CG  1 
ATOM   1428 C  CD  . GLN   B 1 42  ? 6.983  -27.867 26.939 1.00 48.69  ? 48  GLN   C CD  1 
ATOM   1429 O  OE1 . GLN   B 1 42  ? 6.149  -28.769 26.782 1.00 51.29  ? 48  GLN   C OE1 1 
ATOM   1430 N  NE2 . GLN   B 1 42  ? 7.584  -27.662 28.101 1.00 51.41  ? 48  GLN   C NE2 1 
ATOM   1431 N  N   . GLY   B 1 43  ? 10.529 -27.190 22.641 1.00 23.33  ? 49  GLY   C N   1 
ATOM   1432 C  CA  . GLY   B 1 43  ? 11.615 -27.741 21.838 1.00 22.12  ? 49  GLY   C CA  1 
ATOM   1433 C  C   . GLY   B 1 43  ? 12.309 -28.849 22.602 1.00 22.02  ? 49  GLY   C C   1 
ATOM   1434 O  O   . GLY   B 1 43  ? 12.122 -28.975 23.835 1.00 23.53  ? 49  GLY   C O   1 
ATOM   1435 N  N   . CYS   B 1 44  ? 13.112 -29.624 21.898 1.00 22.25  ? 50  CYS   C N   1 
ATOM   1436 C  CA  . CYS   B 1 44  ? 13.718 -30.833 22.486 1.00 23.75  ? 50  CYS   C CA  1 
ATOM   1437 C  C   . CYS   B 1 44  ? 15.217 -30.815 22.585 1.00 21.96  ? 50  CYS   C C   1 
ATOM   1438 O  O   . CYS   B 1 44  ? 15.804 -31.870 22.924 1.00 24.99  ? 50  CYS   C O   1 
ATOM   1439 C  CB  . CYS   B 1 44  ? 13.302 -32.042 21.660 1.00 27.21  ? 50  CYS   C CB  1 
ATOM   1440 S  SG  . CYS   B 1 44  ? 14.010 -32.064 19.990 1.00 47.51  ? 50  CYS   C SG  1 
ATOM   1441 N  N   . ASP   B 1 45  ? 15.877 -29.757 22.148 1.00 18.74  ? 51  ASP   C N   1 
ATOM   1442 C  CA  . ASP   B 1 45  ? 17.341 -29.744 22.175 1.00 18.48  ? 51  ASP   C CA  1 
ATOM   1443 C  C   . ASP   B 1 45  ? 17.760 -29.557 23.627 1.00 19.29  ? 51  ASP   C C   1 
ATOM   1444 O  O   . ASP   B 1 45  ? 17.040 -28.909 24.421 1.00 21.46  ? 51  ASP   C O   1 
ATOM   1445 C  CB  . ASP   B 1 45  ? 17.926 -28.625 21.307 1.00 18.82  ? 51  ASP   C CB  1 
ATOM   1446 C  CG  . ASP   B 1 45  ? 17.732 -28.794 19.815 1.00 23.17  ? 51  ASP   C CG  1 
ATOM   1447 O  OD1 . ASP   B 1 45  ? 17.789 -29.945 19.329 1.00 25.49  ? 51  ASP   C OD1 1 
ATOM   1448 O  OD2 . ASP   B 1 45  ? 17.564 -27.764 19.114 1.00 20.40  ? 51  ASP   C OD2 1 
ATOM   1449 N  N   . THR   B 1 46  ? 18.899 -30.139 23.971 1.00 18.20  ? 52  THR   C N   1 
ATOM   1450 C  CA  . THR   B 1 46  ? 19.479 -30.006 25.302 1.00 18.31  ? 52  THR   C CA  1 
ATOM   1451 C  C   . THR   B 1 46  ? 20.754 -29.167 25.102 1.00 18.09  ? 52  THR   C C   1 
ATOM   1452 O  O   . THR   B 1 46  ? 21.578 -29.485 24.231 1.00 18.21  ? 52  THR   C O   1 
ATOM   1453 C  CB  . THR   B 1 46  ? 19.883 -31.392 25.817 1.00 21.60  ? 52  THR   C CB  1 
ATOM   1454 O  OG1 . THR   B 1 46  ? 18.684 -32.181 25.999 1.00 23.07  ? 52  THR   C OG1 1 
ATOM   1455 C  CG2 . THR   B 1 46  ? 20.665 -31.296 27.134 1.00 24.42  ? 52  THR   C CG2 1 
ATOM   1456 N  N   . ILE   B 1 47  ? 20.935 -28.146 25.941 1.00 17.47  ? 53  ILE   C N   1 
ATOM   1457 C  CA  . ILE   B 1 47  ? 22.130 -27.317 25.893 1.00 16.33  ? 53  ILE   C CA  1 
ATOM   1458 C  C   . ILE   B 1 47  ? 23.222 -27.995 26.726 1.00 16.80  ? 53  ILE   C C   1 
ATOM   1459 O  O   . ILE   B 1 47  ? 22.965 -28.410 27.860 1.00 18.01  ? 53  ILE   C O   1 
ATOM   1460 C  CB  . ILE   B 1 47  ? 21.841 -25.923 26.471 1.00 17.21  ? 53  ILE   C CB  1 
ATOM   1461 C  CG1 . ILE   B 1 47  ? 20.646 -25.259 25.792 1.00 18.70  ? 53  ILE   C CG1 1 
ATOM   1462 C  CG2 . ILE   B 1 47  ? 23.095 -25.028 26.371 1.00 17.65  ? 53  ILE   C CG2 1 
ATOM   1463 C  CD1 . ILE   B 1 47  ? 20.776 -25.148 24.260 1.00 20.30  ? 53  ILE   C CD1 1 
ATOM   1464 N  N   . ALA   B 1 48  ? 24.456 -28.061 26.215 1.00 15.16  ? 54  ALA   C N   1 
ATOM   1465 C  CA  . ALA   B 1 48  ? 25.560 -28.604 26.978 1.00 14.86  ? 54  ALA   C CA  1 
ATOM   1466 C  C   . ALA   B 1 48  ? 25.903 -27.662 28.152 1.00 15.93  ? 54  ALA   C C   1 
ATOM   1467 O  O   . ALA   B 1 48  ? 25.866 -26.423 28.019 1.00 15.78  ? 54  ALA   C O   1 
ATOM   1468 C  CB  . ALA   B 1 48  ? 26.772 -28.705 26.061 1.00 14.97  ? 54  ALA   C CB  1 
ATOM   1469 N  N   . ARG   B 1 49  ? 26.245 -28.267 29.299 1.00 15.62  ? 55  ARG   C N   1 
ATOM   1470 C  CA  . ARG   B 1 49  ? 26.708 -27.498 30.456 1.00 15.55  ? 55  ARG   C CA  1 
ATOM   1471 C  C   . ARG   B 1 49  ? 28.018 -28.151 30.844 1.00 16.43  ? 55  ARG   C C   1 
ATOM   1472 O  O   . ARG   B 1 49  ? 28.025 -29.142 31.576 1.00 18.55  ? 55  ARG   C O   1 
ATOM   1473 C  CB  . ARG   B 1 49  ? 25.682 -27.514 31.597 1.00 16.76  ? 55  ARG   C CB  1 
ATOM   1474 C  CG  . ARG   B 1 49  ? 24.312 -26.962 31.186 1.00 16.66  ? 55  ARG   C CG  1 
ATOM   1475 C  CD  . ARG   B 1 49  ? 24.314 -25.498 30.759 1.00 17.73  ? 55  ARG   C CD  1 
ATOM   1476 N  NE  . ARG   B 1 49  ? 22.948 -25.053 30.406 1.00 18.49  ? 55  ARG   C NE  1 
ATOM   1477 C  CZ  . ARG   B 1 49  ? 22.685 -23.957 29.702 1.00 19.11  ? 55  ARG   C CZ  1 
ATOM   1478 N  NH1 . ARG   B 1 49  ? 23.655 -23.112 29.396 1.00 17.49  ? 55  ARG   C NH1 1 
ATOM   1479 N  NH2 . ARG   B 1 49  ? 21.430 -23.654 29.373 1.00 19.09  ? 55  ARG   C NH2 1 
ATOM   1480 N  N   . CYS   B 1 50  ? 29.114 -27.561 30.377 1.00 15.84  ? 56  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 50  ? 30.466 -28.147 30.388 1.00 16.26  ? 56  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 50  ? 31.532 -27.177 29.882 1.00 17.30  ? 56  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 50  ? 31.226 -26.073 29.441 1.00 17.62  ? 56  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 50  ? 30.436 -29.380 29.474 1.00 14.59  ? 56  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 50  ? 30.274 -28.990 27.679 1.00 16.11  ? 56  CYS   C SG  1 
ATOM   1486 N  N   . ASP   B 1 51  ? 32.832 -27.629 29.909 1.00 17.74  ? 57  ASP   C N   1 
ATOM   1487 C  CA  . ASP   B 1 51  ? 33.964 -26.901 29.356 1.00 18.79  ? 57  ASP   C CA  1 
ATOM   1488 C  C   . ASP   B 1 51  ? 34.601 -27.767 28.255 1.00 18.79  ? 57  ASP   C C   1 
ATOM   1489 O  O   . ASP   B 1 51  ? 35.798 -27.618 27.988 1.00 20.08  ? 57  ASP   C O   1 
ATOM   1490 C  CB  . ASP   B 1 51  ? 34.999 -26.522 30.430 1.00 21.51  ? 57  ASP   C CB  1 
ATOM   1491 C  CG  . ASP   B 1 51  ? 35.591 -27.687 31.177 1.00 26.36  ? 57  ASP   C CG  1 
ATOM   1492 O  OD1 . ASP   B 1 51  ? 35.232 -28.821 30.879 1.00 27.54  ? 57  ASP   C OD1 1 
ATOM   1493 O  OD2 . ASP   B 1 51  ? 36.459 -27.449 32.071 1.00 32.20  ? 57  ASP   C OD2 1 
ATOM   1494 N  N   . CYS   B 1 52  ? 33.823 -28.631 27.559 1.00 17.68  ? 58  CYS   C N   1 
ATOM   1495 C  CA  . CYS   B 1 52  ? 34.394 -29.407 26.423 1.00 16.33  ? 58  CYS   C CA  1 
ATOM   1496 C  C   . CYS   B 1 52  ? 35.073 -28.489 25.398 1.00 15.68  ? 58  CYS   C C   1 
ATOM   1497 O  O   . CYS   B 1 52  ? 34.628 -27.353 25.139 1.00 16.40  ? 58  CYS   C O   1 
ATOM   1498 C  CB  . CYS   B 1 52  ? 33.324 -30.229 25.698 1.00 15.80  ? 58  CYS   C CB  1 
ATOM   1499 S  SG  . CYS   B 1 52  ? 32.700 -31.668 26.618 1.00 17.26  ? 58  CYS   C SG  1 
ATOM   1500 N  N   . GLN   B 1 53  ? 36.136 -29.009 24.809 1.00 14.80  ? 59  GLN   C N   1 
ATOM   1501 C  CA  . GLN   B 1 53  ? 36.826 -28.340 23.699 1.00 16.15  ? 59  GLN   C CA  1 
ATOM   1502 C  C   . GLN   B 1 53  ? 36.906 -29.295 22.513 1.00 15.10  ? 59  GLN   C C   1 
ATOM   1503 O  O   . GLN   B 1 53  ? 37.672 -29.036 21.578 1.00 15.79  ? 59  GLN   C O   1 
ATOM   1504 C  CB  . GLN   B 1 53  ? 38.241 -27.848 24.083 1.00 17.58  ? 59  GLN   C CB  1 
ATOM   1505 C  CG  . GLN   B 1 53  ? 38.219 -26.545 24.905 1.00 20.83  ? 59  GLN   C CG  1 
ATOM   1506 C  CD  . GLN   B 1 53  ? 39.594 -25.999 25.143 1.00 23.56  ? 59  GLN   C CD  1 
ATOM   1507 O  OE1 . GLN   B 1 53  ? 40.093 -26.068 26.273 1.00 26.97  ? 59  GLN   C OE1 1 
ATOM   1508 N  NE2 . GLN   B 1 53  ? 40.229 -25.487 24.090 1.00 21.71  ? 59  GLN   C NE2 1 
ATOM   1509 N  N   . THR   B 1 54  ? 36.123 -30.411 22.507 1.00 14.56  ? 60  THR   C N   1 
ATOM   1510 C  CA  . THR   B 1 54  ? 36.041 -31.248 21.309 1.00 15.85  ? 60  THR   C CA  1 
ATOM   1511 C  C   . THR   B 1 54  ? 34.558 -31.529 21.050 1.00 14.86  ? 60  THR   C C   1 
ATOM   1512 O  O   . THR   B 1 54  ? 33.752 -31.631 21.982 1.00 15.80  ? 60  THR   C O   1 
ATOM   1513 C  CB  . THR   B 1 54  ? 36.801 -32.542 21.393 1.00 18.65  ? 60  THR   C CB  1 
ATOM   1514 O  OG1 . THR   B 1 54  ? 36.222 -33.341 22.389 1.00 21.83  ? 60  THR   C OG1 1 
ATOM   1515 C  CG2 . THR   B 1 54  ? 38.253 -32.332 21.685 1.00 18.18  ? 60  THR   C CG2 1 
ATOM   1516 N  N   . GLY   B 1 55  ? 34.208 -31.616 19.761 1.00 13.65  ? 61  GLY   C N   1 
ATOM   1517 C  CA  . GLY   B 1 55  ? 32.806 -31.856 19.416 1.00 14.12  ? 61  GLY   C CA  1 
ATOM   1518 C  C   . GLY   B 1 55  ? 32.679 -32.046 17.916 1.00 13.23  ? 61  GLY   C C   1 
ATOM   1519 O  O   . GLY   B 1 55  ? 33.676 -32.365 17.249 1.00 13.61  ? 61  GLY   C O   1 
ATOM   1520 N  N   . VAL   B 1 56  ? 31.447 -31.951 17.423 1.00 11.86  ? 62  VAL   C N   1 
ATOM   1521 C  CA  . VAL   B 1 56  ? 31.177 -32.134 15.983 1.00 11.96  ? 62  VAL   C CA  1 
ATOM   1522 C  C   . VAL   B 1 56  ? 30.264 -31.034 15.556 1.00 11.70  ? 62  VAL   C C   1 
ATOM   1523 O  O   . VAL   B 1 56  ? 29.308 -30.733 16.253 1.00 13.16  ? 62  VAL   C O   1 
ATOM   1524 C  CB  . VAL   B 1 56  ? 30.457 -33.503 15.824 1.00 12.94  ? 62  VAL   C CB  1 
ATOM   1525 C  CG1 . VAL   B 1 56  ? 30.007 -33.707 14.377 1.00 14.22  ? 62  VAL   C CG1 1 
ATOM   1526 C  CG2 . VAL   B 1 56  ? 31.404 -34.651 16.234 1.00 13.36  ? 62  VAL   C CG2 1 
ATOM   1527 N  N   . TYR   B 1 57  ? 30.538 -30.421 14.356 1.00 13.01  ? 63  TYR   C N   1 
ATOM   1528 C  CA  . TYR   B 1 57  ? 29.631 -29.378 13.851 1.00 11.39  ? 63  TYR   C CA  1 
ATOM   1529 C  C   . TYR   B 1 57  ? 29.079 -29.715 12.484 1.00 12.35  ? 63  TYR   C C   1 
ATOM   1530 O  O   . TYR   B 1 57  ? 29.711 -30.426 11.724 1.00 12.95  ? 63  TYR   C O   1 
ATOM   1531 C  CB  . TYR   B 1 57  ? 30.294 -27.954 13.845 1.00 12.70  ? 63  TYR   C CB  1 
ATOM   1532 C  CG  . TYR   B 1 57  ? 31.168 -27.633 12.636 1.00 12.71  ? 63  TYR   C CG  1 
ATOM   1533 C  CD1 . TYR   B 1 57  ? 32.462 -28.122 12.537 1.00 13.32  ? 63  TYR   C CD1 1 
ATOM   1534 C  CD2 . TYR   B 1 57  ? 30.708 -26.811 11.611 1.00 13.65  ? 63  TYR   C CD2 1 
ATOM   1535 C  CE1 . TYR   B 1 57  ? 33.278 -27.825 11.449 1.00 14.68  ? 63  TYR   C CE1 1 
ATOM   1536 C  CE2 . TYR   B 1 57  ? 31.521 -26.496 10.524 1.00 14.69  ? 63  TYR   C CE2 1 
ATOM   1537 C  CZ  . TYR   B 1 57  ? 32.811 -26.999 10.456 1.00 14.75  ? 63  TYR   C CZ  1 
ATOM   1538 O  OH  . TYR   B 1 57  ? 33.650 -26.690 9.392  1.00 16.59  ? 63  TYR   C OH  1 
ATOM   1539 N  N   . TYR   B 1 58  ? 27.897 -29.172 12.187 1.00 12.84  ? 64  TYR   C N   1 
ATOM   1540 C  CA  . TYR   B 1 58  ? 27.293 -29.336 10.852 1.00 12.86  ? 64  TYR   C CA  1 
ATOM   1541 C  C   . TYR   B 1 58  ? 27.669 -28.187 9.928  1.00 13.39  ? 64  TYR   C C   1 
ATOM   1542 O  O   . TYR   B 1 58  ? 27.439 -27.017 10.247 1.00 13.92  ? 64  TYR   C O   1 
ATOM   1543 C  CB  . TYR   B 1 58  ? 25.763 -29.459 10.927 1.00 14.29  ? 64  TYR   C CB  1 
ATOM   1544 C  CG  . TYR   B 1 58  ? 25.199 -29.730 9.543  1.00 14.63  ? 64  TYR   C CG  1 
ATOM   1545 C  CD1 . TYR   B 1 58  ? 25.532 -30.884 8.856  1.00 14.78  ? 64  TYR   C CD1 1 
ATOM   1546 C  CD2 . TYR   B 1 58  ? 24.310 -28.847 8.952  1.00 14.49  ? 64  TYR   C CD2 1 
ATOM   1547 C  CE1 . TYR   B 1 58  ? 25.028 -31.142 7.572  1.00 15.75  ? 64  TYR   C CE1 1 
ATOM   1548 C  CE2 . TYR   B 1 58  ? 23.797 -29.094 7.674  1.00 15.07  ? 64  TYR   C CE2 1 
ATOM   1549 C  CZ  . TYR   B 1 58  ? 24.148 -30.259 7.016  1.00 16.64  ? 64  TYR   C CZ  1 
ATOM   1550 O  OH  . TYR   B 1 58  ? 23.711 -30.477 5.718  1.00 19.01  ? 64  TYR   C OH  1 
ATOM   1551 N  N   . CYS   B 1 59  ? 28.200 -28.538 8.768  1.00 13.14  ? 65  CYS   C N   1 
ATOM   1552 C  CA  . CYS   B 1 59  ? 28.595 -27.601 7.702  1.00 13.16  ? 65  CYS   C CA  1 
ATOM   1553 C  C   . CYS   B 1 59  ? 27.674 -27.799 6.492  1.00 13.97  ? 65  CYS   C C   1 
ATOM   1554 O  O   . CYS   B 1 59  ? 27.875 -28.742 5.712  1.00 15.21  ? 65  CYS   C O   1 
ATOM   1555 C  CB  . CYS   B 1 59  ? 30.035 -27.878 7.322  1.00 13.01  ? 65  CYS   C CB  1 
ATOM   1556 S  SG  . CYS   B 1 59  ? 30.644 -26.830 5.973  1.00 16.32  ? 65  CYS   C SG  1 
ATOM   1557 N  N   . SER   B 1 60  ? 26.684 -26.933 6.339  1.00 15.85  ? 66  SER   C N   1 
ATOM   1558 C  CA  . SER   B 1 60  ? 25.706 -27.066 5.266  1.00 16.67  ? 66  SER   C CA  1 
ATOM   1559 C  C   . SER   B 1 60  ? 26.291 -26.975 3.879  1.00 17.06  ? 66  SER   C C   1 
ATOM   1560 O  O   . SER   B 1 60  ? 25.862 -27.742 3.024  1.00 18.72  ? 66  SER   C O   1 
ATOM   1561 C  CB  . SER   B 1 60  ? 24.550 -26.085 5.449  1.00 20.78  ? 66  SER   C CB  1 
ATOM   1562 O  OG  . SER   B 1 60  ? 24.956 -24.746 5.285  1.00 29.60  ? 66  SER   C OG  1 
ATOM   1563 N  N   . SER   B 1 61  ? 27.333 -26.142 3.696  1.00 16.54  ? 67  SER   C N   1 
ATOM   1564 C  CA  . SER   B 1 61  ? 27.997 -25.989 2.377  1.00 17.38  ? 67  SER   C CA  1 
ATOM   1565 C  C   . SER   B 1 61  ? 28.833 -27.180 1.981  1.00 18.56  ? 67  SER   C C   1 
ATOM   1566 O  O   . SER   B 1 61  ? 29.301 -27.180 0.854  1.00 20.87  ? 67  SER   C O   1 
ATOM   1567 C  CB  . SER   B 1 61  ? 28.848 -24.738 2.333  1.00 17.93  ? 67  SER   C CB  1 
ATOM   1568 O  OG  . SER   B 1 61  ? 29.913 -24.796 3.246  1.00 18.91  ? 67  SER   C OG  1 
ATOM   1569 N  N   . ARG   B 1 62  ? 28.972 -28.217 2.850  1.00 16.17  ? 68  ARG   C N   1 
ATOM   1570 C  CA  . ARG   B 1 62  ? 29.618 -29.467 2.485  1.00 16.44  ? 68  ARG   C CA  1 
ATOM   1571 C  C   . ARG   B 1 62  ? 28.678 -30.650 2.711  1.00 17.04  ? 68  ARG   C C   1 
ATOM   1572 O  O   . ARG   B 1 62  ? 29.084 -31.809 2.514  1.00 18.26  ? 68  ARG   C O   1 
ATOM   1573 C  CB  . ARG   B 1 62  ? 30.895 -29.682 3.313  1.00 16.83  ? 68  ARG   C CB  1 
ATOM   1574 C  CG  . ARG   B 1 62  ? 31.965 -28.604 3.110  1.00 19.98  ? 68  ARG   C CG  1 
ATOM   1575 C  CD  . ARG   B 1 62  ? 32.655 -28.867 1.781  1.00 20.72  ? 68  ARG   C CD  1 
ATOM   1576 N  NE  . ARG   B 1 62  ? 33.713 -27.893 1.478  1.00 24.37  ? 68  ARG   C NE  1 
ATOM   1577 C  CZ  . ARG   B 1 62  ? 33.517 -26.751 0.833  1.00 29.60  ? 68  ARG   C CZ  1 
ATOM   1578 N  NH1 . ARG   B 1 62  ? 32.308 -26.426 0.395  1.00 28.33  ? 68  ARG   C NH1 1 
ATOM   1579 N  NH2 . ARG   B 1 62  ? 34.541 -25.935 0.581  1.00 31.14  ? 68  ARG   C NH2 1 
ATOM   1580 N  N   . ARG   B 1 63  ? 27.453 -30.418 3.237  1.00 17.46  ? 69  ARG   C N   1 
ATOM   1581 C  CA  . ARG   B 1 63  ? 26.544 -31.508 3.654  1.00 18.09  ? 69  ARG   C CA  1 
ATOM   1582 C  C   . ARG   B 1 63  ? 27.239 -32.538 4.528  1.00 18.82  ? 69  ARG   C C   1 
ATOM   1583 O  O   . ARG   B 1 63  ? 27.080 -33.745 4.336  1.00 21.23  ? 69  ARG   C O   1 
ATOM   1584 C  CB  . ARG   B 1 63  ? 25.899 -32.171 2.434  1.00 21.13  ? 69  ARG   C CB  1 
ATOM   1585 C  CG  . ARG   B 1 63  ? 24.830 -31.317 1.824  1.00 27.93  ? 69  ARG   C CG  1 
ATOM   1586 C  CD  . ARG   B 1 63  ? 23.859 -32.194 1.091  1.00 36.73  ? 69  ARG   C CD  1 
ATOM   1587 N  NE  . ARG   B 1 63  ? 22.786 -31.366 0.554  1.00 43.28  ? 69  ARG   C NE  1 
ATOM   1588 C  CZ  . ARG   B 1 63  ? 22.696 -30.983 -0.713 1.00 47.88  ? 69  ARG   C CZ  1 
ATOM   1589 N  NH1 . ARG   B 1 63  ? 23.580 -31.413 -1.611 1.00 47.94  ? 69  ARG   C NH1 1 
ATOM   1590 N  NH2 . ARG   B 1 63  ? 21.693 -30.211 -1.107 1.00 48.49  ? 69  ARG   C NH2 1 
ATOM   1591 N  N   . LYS   B 1 64  ? 28.059 -32.047 5.475  1.00 17.14  ? 70  LYS   C N   1 
ATOM   1592 C  CA  . LYS   B 1 64  ? 28.839 -32.966 6.292  1.00 16.69  ? 70  LYS   C CA  1 
ATOM   1593 C  C   . LYS   B 1 64  ? 28.941 -32.456 7.722  1.00 15.72  ? 70  LYS   C C   1 
ATOM   1594 O  O   . LYS   B 1 64  ? 28.960 -31.239 7.966  1.00 16.43  ? 70  LYS   C O   1 
ATOM   1595 C  CB  . LYS   B 1 64  ? 30.259 -33.025 5.706  1.00 20.49  ? 70  LYS   C CB  1 
ATOM   1596 C  CG  . LYS   B 1 64  ? 30.408 -34.091 4.621  1.00 28.79  ? 70  LYS   C CG  1 
ATOM   1597 C  CD  . LYS   B 1 64  ? 31.880 -34.390 4.292  1.00 35.65  ? 70  LYS   C CD  1 
ATOM   1598 C  CE  . LYS   B 1 64  ? 32.008 -35.108 2.970  1.00 41.03  ? 70  LYS   C CE  1 
ATOM   1599 N  NZ  . LYS   B 1 64  ? 31.420 -34.312 1.850  1.00 45.01  ? 70  LYS   C NZ  1 
ATOM   1600 N  N   . HIS   B 1 65  ? 29.062 -33.394 8.647  1.00 14.46  ? 71  HIS   C N   1 
ATOM   1601 C  CA  . HIS   B 1 65  ? 29.375 -33.125 10.059 1.00 14.47  ? 71  HIS   C CA  1 
ATOM   1602 C  C   . HIS   B 1 65  ? 30.851 -33.401 10.260 1.00 16.37  ? 71  HIS   C C   1 
ATOM   1603 O  O   . HIS   B 1 65  ? 31.348 -34.482 9.877  1.00 19.19  ? 71  HIS   C O   1 
ATOM   1604 C  CB  . HIS   B 1 65  ? 28.555 -34.024 10.985 1.00 14.59  ? 71  HIS   C CB  1 
ATOM   1605 C  CG  . HIS   B 1 65  ? 27.076 -33.759 10.941 1.00 13.91  ? 71  HIS   C CG  1 
ATOM   1606 N  ND1 . HIS   B 1 65  ? 26.432 -32.980 11.894 1.00 16.28  ? 71  HIS   C ND1 1 
ATOM   1607 C  CD2 . HIS   B 1 65  ? 26.161 -34.196 10.043 1.00 14.28  ? 71  HIS   C CD2 1 
ATOM   1608 C  CE1 . HIS   B 1 65  ? 25.138 -32.979 11.572 1.00 14.87  ? 71  HIS   C CE1 1 
ATOM   1609 N  NE2 . HIS   B 1 65  ? 24.918 -33.706 10.463 1.00 17.02  ? 71  HIS   C NE2 1 
ATOM   1610 N  N   . TYR   B 1 66  ? 31.602 -32.418 10.832 1.00 14.44  ? 72  TYR   C N   1 
ATOM   1611 C  CA  . TYR   B 1 66  ? 33.051 -32.593 11.001 1.00 13.84  ? 72  TYR   C CA  1 
ATOM   1612 C  C   . TYR   B 1 66  ? 33.413 -32.632 12.484 1.00 14.28  ? 72  TYR   C C   1 
ATOM   1613 O  O   . TYR   B 1 66  ? 32.992 -31.758 13.228 1.00 13.89  ? 72  TYR   C O   1 
ATOM   1614 C  CB  . TYR   B 1 66  ? 33.797 -31.353 10.432 1.00 14.94  ? 72  TYR   C CB  1 
ATOM   1615 C  CG  . TYR   B 1 66  ? 33.766 -31.254 8.920  1.00 15.17  ? 72  TYR   C CG  1 
ATOM   1616 C  CD1 . TYR   B 1 66  ? 34.643 -31.990 8.142  1.00 17.78  ? 72  TYR   C CD1 1 
ATOM   1617 C  CD2 . TYR   B 1 66  ? 32.905 -30.386 8.278  1.00 16.89  ? 72  TYR   C CD2 1 
ATOM   1618 C  CE1 . TYR   B 1 66  ? 34.636 -31.885 6.756  1.00 18.91  ? 72  TYR   C CE1 1 
ATOM   1619 C  CE2 . TYR   B 1 66  ? 32.881 -30.281 6.890  1.00 17.39  ? 72  TYR   C CE2 1 
ATOM   1620 C  CZ  . TYR   B 1 66  ? 33.734 -31.046 6.139  1.00 17.47  ? 72  TYR   C CZ  1 
ATOM   1621 O  OH  . TYR   B 1 66  ? 33.723 -30.885 4.776  1.00 20.77  ? 72  TYR   C OH  1 
ATOM   1622 N  N   . PRO   B 1 67  ? 34.232 -33.588 12.907 1.00 13.84  ? 73  PRO   C N   1 
ATOM   1623 C  CA  . PRO   B 1 67  ? 34.737 -33.558 14.297 1.00 14.09  ? 73  PRO   C CA  1 
ATOM   1624 C  C   . PRO   B 1 67  ? 35.844 -32.472 14.389 1.00 15.26  ? 73  PRO   C C   1 
ATOM   1625 O  O   . PRO   B 1 67  ? 36.741 -32.401 13.525 1.00 17.34  ? 73  PRO   C O   1 
ATOM   1626 C  CB  . PRO   B 1 67  ? 35.366 -34.957 14.492 1.00 15.88  ? 73  PRO   C CB  1 
ATOM   1627 C  CG  . PRO   B 1 67  ? 35.559 -35.518 13.168 1.00 17.62  ? 73  PRO   C CG  1 
ATOM   1628 C  CD  . PRO   B 1 67  ? 34.742 -34.750 12.129 1.00 14.41  ? 73  PRO   C CD  1 
ATOM   1629 N  N   . VAL   B 1 68  ? 35.780 -31.662 15.450 1.00 13.53  ? 74  VAL   C N   1 
ATOM   1630 C  CA  . VAL   B 1 68  ? 36.734 -30.559 15.619 1.00 14.35  ? 74  VAL   C CA  1 
ATOM   1631 C  C   . VAL   B 1 68  ? 37.115 -30.361 17.058 1.00 14.86  ? 74  VAL   C C   1 
ATOM   1632 O  O   . VAL   B 1 68  ? 36.387 -30.664 17.990 1.00 14.54  ? 74  VAL   C O   1 
ATOM   1633 C  CB  . VAL   B 1 68  ? 36.151 -29.206 15.112 1.00 16.29  ? 74  VAL   C CB  1 
ATOM   1634 C  CG1 . VAL   B 1 68  ? 36.112 -29.157 13.574 1.00 18.48  ? 74  VAL   C CG1 1 
ATOM   1635 C  CG2 . VAL   B 1 68  ? 34.778 -28.908 15.751 1.00 17.15  ? 74  VAL   C CG2 1 
ATOM   1636 N  N   . SER   B 1 69  ? 38.332 -29.825 17.240 1.00 14.36  ? 75  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 69  ? 38.764 -29.195 18.491 1.00 14.76  ? 75  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 69  ? 38.481 -27.702 18.378 1.00 14.52  ? 75  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 69  ? 38.648 -27.107 17.278 1.00 15.67  ? 75  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 69  ? 40.279 -29.351 18.644 1.00 17.28  ? 75  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 69  ? 40.496 -30.740 18.784 1.00 22.89  ? 75  SER   C OG  1 
ATOM   1642 N  N   . PHE   B 1 70  ? 37.983 -27.086 19.461 1.00 14.04  ? 76  PHE   C N   1 
ATOM   1643 C  CA  . PHE   B 1 70  ? 37.633 -25.675 19.410 1.00 13.74  ? 76  PHE   C CA  1 
ATOM   1644 C  C   . PHE   B 1 70  ? 38.099 -24.954 20.646 1.00 15.26  ? 76  PHE   C C   1 
ATOM   1645 O  O   . PHE   B 1 70  ? 38.242 -25.560 21.710 1.00 15.85  ? 76  PHE   C O   1 
ATOM   1646 C  CB  . PHE   B 1 70  ? 36.107 -25.482 19.164 1.00 13.95  ? 76  PHE   C CB  1 
ATOM   1647 C  CG  . PHE   B 1 70  ? 35.181 -26.186 20.151 1.00 13.71  ? 76  PHE   C CG  1 
ATOM   1648 C  CD1 . PHE   B 1 70  ? 34.759 -27.487 19.928 1.00 14.25  ? 76  PHE   C CD1 1 
ATOM   1649 C  CD2 . PHE   B 1 70  ? 34.730 -25.525 21.289 1.00 15.29  ? 76  PHE   C CD2 1 
ATOM   1650 C  CE1 . PHE   B 1 70  ? 33.943 -28.142 20.839 1.00 14.13  ? 76  PHE   C CE1 1 
ATOM   1651 C  CE2 . PHE   B 1 70  ? 33.887 -26.174 22.184 1.00 14.96  ? 76  PHE   C CE2 1 
ATOM   1652 C  CZ  . PHE   B 1 70  ? 33.503 -27.474 21.965 1.00 14.29  ? 76  PHE   C CZ  1 
ATOM   1653 N  N   . SER   B 1 71  ? 38.331 -23.642 20.513 1.00 15.34  ? 77  SER   C N   1 
ATOM   1654 C  CA  . SER   B 1 71  ? 38.923 -22.877 21.605 1.00 16.30  ? 77  SER   C CA  1 
ATOM   1655 C  C   . SER   B 1 71  ? 37.906 -22.489 22.683 1.00 17.27  ? 77  SER   C C   1 
ATOM   1656 O  O   . SER   B 1 71  ? 36.698 -22.684 22.498 1.00 17.50  ? 77  SER   C O   1 
ATOM   1657 C  CB  . SER   B 1 71  ? 39.641 -21.638 21.065 1.00 17.89  ? 77  SER   C CB  1 
ATOM   1658 O  OG  . SER   B 1 71  ? 38.747 -20.766 20.373 1.00 19.60  ? 77  SER   C OG  1 
ATOM   1659 N  N   . LYS   B 1 72  ? 38.377 -21.917 23.806 1.00 19.59  ? 78  LYS   C N   1 
ATOM   1660 C  CA  . LYS   B 1 72  ? 37.450 -21.534 24.875 1.00 19.49  ? 78  LYS   C CA  1 
ATOM   1661 C  C   . LYS   B 1 72  ? 36.747 -20.204 24.472 1.00 19.44  ? 78  LYS   C C   1 
ATOM   1662 O  O   . LYS   B 1 72  ? 37.319 -19.413 23.732 1.00 21.11  ? 78  LYS   C O   1 
ATOM   1663 C  CB  . LYS   B 1 72  ? 38.221 -21.355 26.192 1.00 24.85  ? 78  LYS   C CB  1 
ATOM   1664 C  CG  . LYS   B 1 72  ? 38.890 -22.624 26.664 1.00 29.22  ? 78  LYS   C CG  1 
ATOM   1665 C  CD  . LYS   B 1 72  ? 38.904 -22.724 28.215 1.00 37.11  ? 78  LYS   C CD  1 
ATOM   1666 C  CE  . LYS   B 1 72  ? 39.204 -24.125 28.694 1.00 41.75  ? 78  LYS   C CE  1 
ATOM   1667 N  NZ  . LYS   B 1 72  ? 39.333 -24.196 30.176 1.00 45.42  ? 78  LYS   C NZ  1 
ATOM   1668 N  N   . PRO   B 1 73  ? 35.495 -19.956 24.900 1.00 18.96  ? 79  PRO   C N   1 
ATOM   1669 C  CA  . PRO   B 1 73  ? 34.803 -18.705 24.481 1.00 18.95  ? 79  PRO   C CA  1 
ATOM   1670 C  C   . PRO   B 1 73  ? 35.571 -17.453 24.833 1.00 19.64  ? 79  PRO   C C   1 
ATOM   1671 O  O   . PRO   B 1 73  ? 35.967 -17.273 25.985 1.00 21.93  ? 79  PRO   C O   1 
ATOM   1672 C  CB  . PRO   B 1 73  ? 33.448 -18.763 25.180 1.00 20.95  ? 79  PRO   C CB  1 
ATOM   1673 C  CG  . PRO   B 1 73  ? 33.291 -20.187 25.644 1.00 22.53  ? 79  PRO   C CG  1 
ATOM   1674 C  CD  . PRO   B 1 73  ? 34.657 -20.807 25.772 1.00 20.25  ? 79  PRO   C CD  1 
ATOM   1675 N  N   . SER   B 1 74  ? 35.823 -16.590 23.840 1.00 17.73  ? 80  SER   C N   1 
ATOM   1676 C  CA  . SER   B 1 74  ? 36.686 -15.425 24.040 1.00 19.14  ? 80  SER   C CA  1 
ATOM   1677 C  C   . SER   B 1 74  ? 36.263 -14.248 23.139 1.00 19.55  ? 80  SER   C C   1 
ATOM   1678 O  O   . SER   B 1 74  ? 35.370 -14.394 22.315 1.00 18.98  ? 80  SER   C O   1 
ATOM   1679 C  CB  . SER   B 1 74  ? 38.130 -15.780 23.678 1.00 21.57  ? 80  SER   C CB  1 
ATOM   1680 O  OG  . SER   B 1 74  ? 38.628 -16.982 24.241 1.00 27.22  ? 80  SER   C OG  1 
ATOM   1681 N  N   . LEU   B 1 75  ? 36.941 -13.084 23.313 1.00 21.00  ? 81  LEU   C N   1 
ATOM   1682 C  CA  . LEU   B 1 75  ? 36.750 -11.870 22.523 1.00 21.74  ? 81  LEU   C CA  1 
ATOM   1683 C  C   . LEU   B 1 75  ? 37.776 -11.951 21.382 1.00 22.91  ? 81  LEU   C C   1 
ATOM   1684 O  O   . LEU   B 1 75  ? 39.014 -11.954 21.615 1.00 24.17  ? 81  LEU   C O   1 
ATOM   1685 C  CB  . LEU   B 1 75  ? 37.005 -10.631 23.406 1.00 23.24  ? 81  LEU   C CB  1 
ATOM   1686 C  CG  . LEU   B 1 75  ? 36.716 -9.279  22.767 1.00 25.26  ? 81  LEU   C CG  1 
ATOM   1687 C  CD1 . LEU   B 1 75  ? 35.240 -9.095  22.521 1.00 25.70  ? 81  LEU   C CD1 1 
ATOM   1688 C  CD2 . LEU   B 1 75  ? 37.218 -8.121  23.678 1.00 27.69  ? 81  LEU   C CD2 1 
ATOM   1689 N  N   . ILE   B 1 76  ? 37.279 -12.123 20.165 1.00 24.07  ? 82  ILE   C N   1 
ATOM   1690 C  CA  . ILE   B 1 76  ? 38.124 -12.391 18.998 1.00 25.54  ? 82  ILE   C CA  1 
ATOM   1691 C  C   . ILE   B 1 76  ? 37.880 -11.324 17.940 1.00 25.77  ? 82  ILE   C C   1 
ATOM   1692 O  O   . ILE   B 1 76  ? 36.719 -11.016 17.674 1.00 24.36  ? 82  ILE   C O   1 
ATOM   1693 C  CB  . ILE   B 1 76  ? 37.712 -13.779 18.411 1.00 27.61  ? 82  ILE   C CB  1 
ATOM   1694 C  CG1 . ILE   B 1 76  ? 37.934 -14.940 19.405 1.00 29.35  ? 82  ILE   C CG1 1 
ATOM   1695 C  CG2 . ILE   B 1 76  ? 38.373 -14.072 17.043 1.00 29.51  ? 82  ILE   C CG2 1 
ATOM   1696 C  CD1 . ILE   B 1 76  ? 39.405 -15.298 19.695 1.00 30.42  ? 82  ILE   C CD1 1 
ATOM   1697 N  N   . PHE   B 1 77  ? 38.938 -10.809 17.284 1.00 26.11  ? 83  PHE   C N   1 
ATOM   1698 C  CA  . PHE   B 1 77  ? 38.750 -9.894  16.157 1.00 25.35  ? 83  PHE   C CA  1 
ATOM   1699 C  C   . PHE   B 1 77  ? 38.408 -10.790 14.943 1.00 25.40  ? 83  PHE   C C   1 
ATOM   1700 O  O   . PHE   B 1 77  ? 39.115 -11.758 14.665 1.00 27.46  ? 83  PHE   C O   1 
ATOM   1701 C  CB  . PHE   B 1 77  ? 40.042 -9.103  15.845 1.00 26.39  ? 83  PHE   C CB  1 
ATOM   1702 C  CG  . PHE   B 1 77  ? 39.773 -7.959  14.904 1.00 27.80  ? 83  PHE   C CG  1 
ATOM   1703 C  CD1 . PHE   B 1 77  ? 39.022 -6.870  15.311 1.00 28.98  ? 83  PHE   C CD1 1 
ATOM   1704 C  CD2 . PHE   B 1 77  ? 40.210 -8.005  13.587 1.00 29.49  ? 83  PHE   C CD2 1 
ATOM   1705 C  CE1 . PHE   B 1 77  ? 38.747 -5.827  14.433 1.00 30.08  ? 83  PHE   C CE1 1 
ATOM   1706 C  CE2 . PHE   B 1 77  ? 39.947 -6.955  12.716 1.00 30.53  ? 83  PHE   C CE2 1 
ATOM   1707 C  CZ  . PHE   B 1 77  ? 39.221 -5.875  13.144 1.00 30.15  ? 83  PHE   C CZ  1 
ATOM   1708 N  N   . VAL   B 1 78  ? 37.279 -10.485 14.264 1.00 22.27  ? 84  VAL   C N   1 
ATOM   1709 C  CA  . VAL   B 1 78  ? 36.786 -11.224 13.117 1.00 22.01  ? 84  VAL   C CA  1 
ATOM   1710 C  C   . VAL   B 1 78  ? 36.860 -10.296 11.902 1.00 22.33  ? 84  VAL   C C   1 
ATOM   1711 O  O   . VAL   B 1 78  ? 36.384 -9.155  11.975 1.00 22.43  ? 84  VAL   C O   1 
ATOM   1712 C  CB  . VAL   B 1 78  ? 35.311 -11.656 13.387 1.00 22.86  ? 84  VAL   C CB  1 
ATOM   1713 C  CG1 . VAL   B 1 78  ? 34.769 -12.444 12.203 1.00 21.99  ? 84  VAL   C CG1 1 
ATOM   1714 C  CG2 . VAL   B 1 78  ? 35.203 -12.471 14.676 1.00 23.61  ? 84  VAL   C CG2 1 
ATOM   1715 N  N   . GLU   B 1 79  ? 37.384 -10.784 10.762 1.00 21.64  ? 85  GLU   C N   1 
ATOM   1716 C  CA  . GLU   B 1 79  ? 37.427 -9.968  9.544  1.00 21.70  ? 85  GLU   C CA  1 
ATOM   1717 C  C   . GLU   B 1 79  ? 36.033 -9.721  8.976  1.00 20.58  ? 85  GLU   C C   1 
ATOM   1718 O  O   . GLU   B 1 79  ? 35.091 -10.437 9.299  1.00 19.67  ? 85  GLU   C O   1 
ATOM   1719 C  CB  . GLU   B 1 79  ? 38.324 -10.622 8.479  1.00 25.38  ? 85  GLU   C CB  1 
ATOM   1720 C  CG  . GLU   B 1 79  ? 39.787 -10.639 8.879  1.00 32.18  ? 85  GLU   C CG  1 
ATOM   1721 C  CD  . GLU   B 1 79  ? 40.384 -9.275  9.165  1.00 42.08  ? 85  GLU   C CD  1 
ATOM   1722 O  OE1 . GLU   B 1 79  ? 40.153 -8.338  8.367  1.00 44.62  ? 85  GLU   C OE1 1 
ATOM   1723 O  OE2 . GLU   B 1 79  ? 41.064 -9.137  10.208 1.00 45.62  ? 85  GLU   C OE2 1 
ATOM   1724 N  N   . ALA   B 1 80  ? 35.902 -8.715  8.104  1.00 21.77  ? 86  ALA   C N   1 
ATOM   1725 C  CA  . ALA   B 1 80  ? 34.608 -8.405  7.512  1.00 23.38  ? 86  ALA   C CA  1 
ATOM   1726 C  C   . ALA   B 1 80  ? 34.012 -9.600  6.767  1.00 23.96  ? 86  ALA   C C   1 
ATOM   1727 O  O   . ALA   B 1 80  ? 34.714 -10.408 6.152  1.00 25.21  ? 86  ALA   C O   1 
ATOM   1728 C  CB  . ALA   B 1 80  ? 34.756 -7.242  6.544  1.00 25.17  ? 86  ALA   C CB  1 
ATOM   1729 N  N   . SER   B 1 81  ? 32.711 -9.736  6.902  1.00 23.28  ? 87  SER   C N   1 
ATOM   1730 C  CA  . SER   B 1 81  ? 31.984 -10.789 6.237  1.00 23.68  ? 87  SER   C CA  1 
ATOM   1731 C  C   . SER   B 1 81  ? 30.881 -10.128 5.425  1.00 25.55  ? 87  SER   C C   1 
ATOM   1732 O  O   . SER   B 1 81  ? 30.760 -8.868  5.411  1.00 25.76  ? 87  SER   C O   1 
ATOM   1733 C  CB  . SER   B 1 81  ? 31.404 -11.752 7.270  1.00 21.31  ? 87  SER   C CB  1 
ATOM   1734 O  OG  . SER   B 1 81  ? 30.354 -11.117 7.993  1.00 22.09  ? 87  SER   C OG  1 
ATOM   1735 N  N   . GLU   B 1 82  ? 30.040 -10.959 4.778  1.00 26.28  ? 88  GLU   C N   1 
ATOM   1736 C  CA  . GLU   B 1 82  ? 28.963 -10.370 4.002  1.00 27.87  ? 88  GLU   C CA  1 
ATOM   1737 C  C   . GLU   B 1 82  ? 27.879 -9.732  4.884  1.00 26.58  ? 88  GLU   C C   1 
ATOM   1738 O  O   . GLU   B 1 82  ? 27.146 -8.861  4.390  1.00 27.27  ? 88  GLU   C O   1 
ATOM   1739 C  CB  . GLU   B 1 82  ? 28.390 -11.351 2.970  1.00 33.05  ? 88  GLU   C CB  1 
ATOM   1740 C  CG  . GLU   B 1 82  ? 27.477 -12.418 3.525  1.00 40.34  ? 88  GLU   C CG  1 
ATOM   1741 C  CD  . GLU   B 1 82  ? 26.814 -13.237 2.433  1.00 47.01  ? 88  GLU   C CD  1 
ATOM   1742 O  OE1 . GLU   B 1 82  ? 27.442 -13.425 1.365  1.00 47.14  ? 88  GLU   C OE1 1 
ATOM   1743 O  OE2 . GLU   B 1 82  ? 25.662 -13.682 2.642  1.00 48.96  ? 88  GLU   C OE2 1 
ATOM   1744 N  N   . TYR   B 1 83  ? 27.862 -10.041 6.208  1.00 23.51  ? 89  TYR   C N   1 
ATOM   1745 C  CA  . TYR   B 1 83  ? 26.832 -9.562  7.127  1.00 21.65  ? 89  TYR   C CA  1 
ATOM   1746 C  C   . TYR   B 1 83  ? 27.320 -8.711  8.344  1.00 23.17  ? 89  TYR   C C   1 
ATOM   1747 O  O   . TYR   B 1 83  ? 26.472 -8.131  9.014  1.00 23.59  ? 89  TYR   C O   1 
ATOM   1748 C  CB  . TYR   B 1 83  ? 25.982 -10.770 7.616  1.00 20.88  ? 89  TYR   C CB  1 
ATOM   1749 C  CG  . TYR   B 1 83  ? 26.794 -11.958 8.113  1.00 20.13  ? 89  TYR   C CG  1 
ATOM   1750 C  CD1 . TYR   B 1 83  ? 27.279 -12.926 7.226  1.00 21.03  ? 89  TYR   C CD1 1 
ATOM   1751 C  CD2 . TYR   B 1 83  ? 27.179 -12.054 9.439  1.00 19.29  ? 89  TYR   C CD2 1 
ATOM   1752 C  CE1 . TYR   B 1 83  ? 28.044 -14.003 7.673  1.00 20.52  ? 89  TYR   C CE1 1 
ATOM   1753 C  CE2 . TYR   B 1 83  ? 27.931 -13.131 9.899  1.00 19.61  ? 89  TYR   C CE2 1 
ATOM   1754 C  CZ  . TYR   B 1 83  ? 28.351 -14.113 9.017  1.00 19.36  ? 89  TYR   C CZ  1 
ATOM   1755 O  OH  . TYR   B 1 83  ? 29.194 -15.116 9.442  1.00 19.33  ? 89  TYR   C OH  1 
ATOM   1756 N  N   . TYR   B 1 84  ? 28.651 -8.564  8.605  1.00 21.91  ? 90  TYR   C N   1 
ATOM   1757 C  CA  . TYR   B 1 84  ? 29.197 -7.663  9.656  1.00 20.94  ? 90  TYR   C CA  1 
ATOM   1758 C  C   . TYR   B 1 84  ? 30.545 -7.066  9.162  1.00 21.86  ? 90  TYR   C C   1 
ATOM   1759 O  O   . TYR   B 1 84  ? 31.293 -7.721  8.425  1.00 22.19  ? 90  TYR   C O   1 
ATOM   1760 C  CB  . TYR   B 1 84  ? 29.538 -8.413  10.983 1.00 19.28  ? 90  TYR   C CB  1 
ATOM   1761 C  CG  . TYR   B 1 84  ? 28.360 -8.824  11.842 1.00 18.84  ? 90  TYR   C CG  1 
ATOM   1762 C  CD1 . TYR   B 1 84  ? 27.434 -7.886  12.295 1.00 19.33  ? 90  TYR   C CD1 1 
ATOM   1763 C  CD2 . TYR   B 1 84  ? 28.164 -10.138 12.179 1.00 18.90  ? 90  TYR   C CD2 1 
ATOM   1764 C  CE1 . TYR   B 1 84  ? 26.351 -8.266  13.091 1.00 20.40  ? 90  TYR   C CE1 1 
ATOM   1765 C  CE2 . TYR   B 1 84  ? 27.076 -10.536 12.952 1.00 17.88  ? 90  TYR   C CE2 1 
ATOM   1766 C  CZ  . TYR   B 1 84  ? 26.185 -9.599  13.424 1.00 19.14  ? 90  TYR   C CZ  1 
ATOM   1767 O  OH  . TYR   B 1 84  ? 25.109 -9.999  14.183 1.00 18.45  ? 90  TYR   C OH  1 
ATOM   1768 N  N   . PRO   B 1 85  ? 30.918 -5.872  9.646  1.00 22.05  ? 91  PRO   C N   1 
ATOM   1769 C  CA  . PRO   B 1 85  ? 32.260 -5.337  9.323  1.00 21.86  ? 91  PRO   C CA  1 
ATOM   1770 C  C   . PRO   B 1 85  ? 33.305 -6.095  10.168 1.00 21.98  ? 91  PRO   C C   1 
ATOM   1771 O  O   . PRO   B 1 85  ? 32.960 -6.882  11.076 1.00 21.80  ? 91  PRO   C O   1 
ATOM   1772 C  CB  . PRO   B 1 85  ? 32.155 -3.879  9.801  1.00 23.58  ? 91  PRO   C CB  1 
ATOM   1773 C  CG  . PRO   B 1 85  ? 31.253 -3.967  10.963 1.00 23.42  ? 91  PRO   C CG  1 
ATOM   1774 C  CD  . PRO   B 1 85  ? 30.187 -4.997  10.588 1.00 22.37  ? 91  PRO   C CD  1 
ATOM   1775 N  N   . ALA   B 1 86  ? 34.612 -5.819  9.932  1.00 21.23  ? 92  ALA   C N   1 
ATOM   1776 C  CA  . ALA   B 1 86  ? 35.675 -6.343  10.783 1.00 23.39  ? 92  ALA   C CA  1 
ATOM   1777 C  C   . ALA   B 1 86  ? 35.458 -5.757  12.206 1.00 25.09  ? 92  ALA   C C   1 
ATOM   1778 O  O   . ALA   B 1 86  ? 35.197 -4.548  12.330 1.00 27.02  ? 92  ALA   C O   1 
ATOM   1779 C  CB  . ALA   B 1 86  ? 37.034 -5.880  10.243 1.00 24.26  ? 92  ALA   C CB  1 
ATOM   1780 N  N   . ARG   B 1 87  ? 35.430 -6.616  13.233 1.00 24.44  ? 93  ARG   C N   1 
ATOM   1781 C  CA  . ARG   B 1 87  ? 35.098 -6.152  14.574 1.00 24.90  ? 93  ARG   C CA  1 
ATOM   1782 C  C   . ARG   B 1 87  ? 35.470 -7.219  15.597 1.00 24.82  ? 93  ARG   C C   1 
ATOM   1783 O  O   . ARG   B 1 87  ? 35.762 -8.372  15.242 1.00 23.97  ? 93  ARG   C O   1 
ATOM   1784 C  CB  . ARG   B 1 87  ? 33.565 -5.890  14.670 1.00 25.30  ? 93  ARG   C CB  1 
ATOM   1785 C  CG  . ARG   B 1 87  ? 32.764 -7.173  14.514 1.00 24.47  ? 93  ARG   C CG  1 
ATOM   1786 C  CD  . ARG   B 1 87  ? 31.317 -6.911  14.854 1.00 23.26  ? 93  ARG   C CD  1 
ATOM   1787 N  NE  . ARG   B 1 87  ? 30.621 -8.168  15.121 1.00 23.06  ? 93  ARG   C NE  1 
ATOM   1788 C  CZ  . ARG   B 1 87  ? 29.477 -8.327  15.781 1.00 24.22  ? 93  ARG   C CZ  1 
ATOM   1789 N  NH1 . ARG   B 1 87  ? 28.858 -7.283  16.321 1.00 23.04  ? 93  ARG   C NH1 1 
ATOM   1790 N  NH2 . ARG   B 1 87  ? 28.972 -9.536  15.941 1.00 23.96  ? 93  ARG   C NH2 1 
ATOM   1791 N  N   . TYR   B 1 88  ? 35.375 -6.870  16.879 1.00 26.15  ? 94  TYR   C N   1 
ATOM   1792 C  CA  . TYR   B 1 88  ? 35.533 -7.844  17.937 1.00 27.35  ? 94  TYR   C CA  1 
ATOM   1793 C  C   . TYR   B 1 88  ? 34.163 -8.474  18.186 1.00 25.18  ? 94  TYR   C C   1 
ATOM   1794 O  O   . TYR   B 1 88  ? 33.154 -7.778  18.308 1.00 26.85  ? 94  TYR   C O   1 
ATOM   1795 C  CB  . TYR   B 1 88  ? 35.972 -7.149  19.219 1.00 30.05  ? 94  TYR   C CB  1 
ATOM   1796 C  CG  . TYR   B 1 88  ? 37.426 -6.758  19.159 1.00 32.44  ? 94  TYR   C CG  1 
ATOM   1797 C  CD1 . TYR   B 1 88  ? 38.420 -7.683  19.419 1.00 32.89  ? 94  TYR   C CD1 1 
ATOM   1798 C  CD2 . TYR   B 1 88  ? 37.807 -5.485  18.758 1.00 33.67  ? 94  TYR   C CD2 1 
ATOM   1799 C  CE1 . TYR   B 1 88  ? 39.762 -7.343  19.324 1.00 34.39  ? 94  TYR   C CE1 1 
ATOM   1800 C  CE2 . TYR   B 1 88  ? 39.140 -5.130  18.663 1.00 34.75  ? 94  TYR   C CE2 1 
ATOM   1801 C  CZ  . TYR   B 1 88  ? 40.117 -6.057  18.962 1.00 35.68  ? 94  TYR   C CZ  1 
ATOM   1802 O  OH  . TYR   B 1 88  ? 41.436 -5.700  18.852 1.00 38.25  ? 94  TYR   C OH  1 
ATOM   1803 N  N   . GLN   B 1 89  ? 34.146 -9.805  18.272 1.00 21.02  ? 95  GLN   C N   1 
ATOM   1804 C  CA  . GLN   B 1 89  ? 32.940 -10.572 18.613 1.00 19.42  ? 95  GLN   C CA  1 
ATOM   1805 C  C   . GLN   B 1 89  ? 33.223 -11.291 19.952 1.00 19.54  ? 95  GLN   C C   1 
ATOM   1806 O  O   . GLN   B 1 89  ? 34.309 -11.881 20.118 1.00 20.10  ? 95  GLN   C O   1 
ATOM   1807 C  CB  . GLN   B 1 89  ? 32.582 -11.554 17.464 1.00 19.05  ? 95  GLN   C CB  1 
ATOM   1808 C  CG  . GLN   B 1 89  ? 31.330 -12.340 17.756 1.00 20.58  ? 95  GLN   C CG  1 
ATOM   1809 C  CD  . GLN   B 1 89  ? 30.640 -12.923 16.544 1.00 18.42  ? 95  GLN   C CD  1 
ATOM   1810 O  OE1 . GLN   B 1 89  ? 30.595 -12.346 15.445 1.00 20.94  ? 95  GLN   C OE1 1 
ATOM   1811 N  NE2 . GLN   B 1 89  ? 30.061 -14.084 16.741 1.00 18.49  ? 95  GLN   C NE2 1 
ATOM   1812 N  N   . SER   B 1 90  ? 32.303 -11.273 20.880 1.00 18.10  ? 96  SER   C N   1 
ATOM   1813 C  CA  . SER   B 1 90  ? 32.476 -11.895 22.189 1.00 17.92  ? 96  SER   C CA  1 
ATOM   1814 C  C   . SER   B 1 90  ? 31.885 -13.312 22.242 1.00 17.89  ? 96  SER   C C   1 
ATOM   1815 O  O   . SER   B 1 90  ? 31.024 -13.661 21.434 1.00 17.88  ? 96  SER   C O   1 
ATOM   1816 C  CB  . SER   B 1 90  ? 31.937 -11.009 23.316 1.00 19.03  ? 96  SER   C CB  1 
ATOM   1817 O  OG  . SER   B 1 90  ? 30.532 -10.995 23.206 1.00 20.39  ? 96  SER   C OG  1 
ATOM   1818 N  N   . HIS   B 1 91  ? 32.345 -14.083 23.253 1.00 16.56  ? 97  HIS   C N   1 
ATOM   1819 C  CA  . HIS   B 1 91  ? 31.852 -15.439 23.517 1.00 16.19  ? 97  HIS   C CA  1 
ATOM   1820 C  C   . HIS   B 1 91  ? 31.986 -16.326 22.264 1.00 16.95  ? 97  HIS   C C   1 
ATOM   1821 O  O   . HIS   B 1 91  ? 31.101 -17.158 22.016 1.00 17.19  ? 97  HIS   C O   1 
ATOM   1822 C  CB  . HIS   B 1 91  ? 30.398 -15.406 24.079 1.00 17.11  ? 97  HIS   C CB  1 
ATOM   1823 C  CG  . HIS   B 1 91  ? 30.278 -14.670 25.392 1.00 19.25  ? 97  HIS   C CG  1 
ATOM   1824 N  ND1 . HIS   B 1 91  ? 30.285 -15.352 26.601 1.00 21.50  ? 97  HIS   C ND1 1 
ATOM   1825 C  CD2 . HIS   B 1 91  ? 30.159 -13.339 25.641 1.00 19.64  ? 97  HIS   C CD2 1 
ATOM   1826 C  CE1 . HIS   B 1 91  ? 30.161 -14.427 27.543 1.00 21.55  ? 97  HIS   C CE1 1 
ATOM   1827 N  NE2 . HIS   B 1 91  ? 30.083 -13.196 27.020 1.00 21.30  ? 97  HIS   C NE2 1 
ATOM   1828 N  N   . LEU   B 1 92  ? 33.081 -16.132 21.507 1.00 15.90  ? 98  LEU   C N   1 
ATOM   1829 C  CA  . LEU   B 1 92  ? 33.264 -16.851 20.246 1.00 15.47  ? 98  LEU   C CA  1 
ATOM   1830 C  C   . LEU   B 1 92  ? 34.350 -17.919 20.454 1.00 16.33  ? 98  LEU   C C   1 
ATOM   1831 O  O   . LEU   B 1 92  ? 35.340 -17.682 21.146 1.00 16.69  ? 98  LEU   C O   1 
ATOM   1832 C  CB  . LEU   B 1 92  ? 33.733 -15.842 19.149 1.00 16.95  ? 98  LEU   C CB  1 
ATOM   1833 C  CG  . LEU   B 1 92  ? 33.822 -16.408 17.726 1.00 18.37  ? 98  LEU   C CG  1 
ATOM   1834 C  CD1 . LEU   B 1 92  ? 32.461 -16.740 17.199 1.00 18.96  ? 98  LEU   C CD1 1 
ATOM   1835 C  CD2 . LEU   B 1 92  ? 34.510 -15.421 16.797 1.00 20.42  ? 98  LEU   C CD2 1 
ATOM   1836 N  N   . MET   B 1 93  ? 34.144 -19.091 19.836 1.00 15.00  ? 99  MET   C N   1 
ATOM   1837 C  CA  . MET   B 1 93  ? 35.105 -20.205 19.888 1.00 14.65  ? 99  MET   C CA  1 
ATOM   1838 C  C   . MET   B 1 93  ? 35.543 -20.496 18.448 1.00 15.31  ? 99  MET   C C   1 
ATOM   1839 O  O   . MET   B 1 93  ? 34.698 -20.537 17.579 1.00 15.99  ? 99  MET   C O   1 
ATOM   1840 C  CB  . MET   B 1 93  ? 34.413 -21.431 20.493 1.00 16.98  ? 99  MET   C CB  1 
ATOM   1841 C  CG  . MET   B 1 93  ? 33.900 -21.154 21.899 1.00 18.69  ? 99  MET   C CG  1 
ATOM   1842 S  SD  . MET   B 1 93  ? 32.883 -22.505 22.492 1.00 18.74  ? 99  MET   C SD  1 
ATOM   1843 C  CE  . MET   B 1 93  ? 31.428 -22.353 21.367 1.00 20.18  ? 99  MET   C CE  1 
ATOM   1844 N  N   . LEU   B 1 94  ? 36.839 -20.779 18.193 1.00 15.12  ? 100 LEU   C N   1 
ATOM   1845 C  CA  . LEU   B 1 94  ? 37.290 -21.040 16.838 1.00 15.75  ? 100 LEU   C CA  1 
ATOM   1846 C  C   . LEU   B 1 94  ? 37.749 -22.487 16.698 1.00 14.54  ? 100 LEU   C C   1 
ATOM   1847 O  O   . LEU   B 1 94  ? 38.292 -23.080 17.650 1.00 15.77  ? 100 LEU   C O   1 
ATOM   1848 C  CB  . LEU   B 1 94  ? 38.525 -20.165 16.466 1.00 17.12  ? 100 LEU   C CB  1 
ATOM   1849 C  CG  . LEU   B 1 94  ? 38.326 -18.672 16.367 1.00 19.21  ? 100 LEU   C CG  1 
ATOM   1850 C  CD1 . LEU   B 1 94  ? 39.649 -17.946 15.974 1.00 22.48  ? 100 LEU   C CD1 1 
ATOM   1851 C  CD2 . LEU   B 1 94  ? 37.182 -18.294 15.447 1.00 19.41  ? 100 LEU   C CD2 1 
ATOM   1852 N  N   . ALA   B 1 95  ? 37.625 -22.990 15.481 1.00 14.88  ? 101 ALA   C N   1 
ATOM   1853 C  CA  . ALA   B 1 95  ? 38.187 -24.288 15.087 1.00 15.15  ? 101 ALA   C CA  1 
ATOM   1854 C  C   . ALA   B 1 95  ? 38.743 -24.171 13.679 1.00 14.67  ? 101 ALA   C C   1 
ATOM   1855 O  O   . ALA   B 1 95  ? 38.363 -23.251 12.940 1.00 15.03  ? 101 ALA   C O   1 
ATOM   1856 C  CB  . ALA   B 1 95  ? 37.073 -25.357 15.111 1.00 15.51  ? 101 ALA   C CB  1 
ATOM   1857 N  N   . VAL   B 1 96  ? 39.622 -25.103 13.277 1.00 15.10  ? 102 VAL   C N   1 
ATOM   1858 C  CA  . VAL   B 1 96  ? 40.108 -25.168 11.906 1.00 15.51  ? 102 VAL   C CA  1 
ATOM   1859 C  C   . VAL   B 1 96  ? 39.022 -25.936 11.117 1.00 16.16  ? 102 VAL   C C   1 
ATOM   1860 O  O   . VAL   B 1 96  ? 38.729 -27.133 11.392 1.00 16.80  ? 102 VAL   C O   1 
ATOM   1861 C  CB  . VAL   B 1 96  ? 41.466 -25.886 11.863 1.00 16.77  ? 102 VAL   C CB  1 
ATOM   1862 C  CG1 . VAL   B 1 96  ? 41.934 -26.048 10.419 1.00 17.50  ? 102 VAL   C CG1 1 
ATOM   1863 C  CG2 . VAL   B 1 96  ? 42.474 -25.113 12.677 1.00 18.04  ? 102 VAL   C CG2 1 
ATOM   1864 N  N   . GLY   B 1 97  ? 38.449 -25.274 10.137 1.00 16.95  ? 103 GLY   C N   1 
ATOM   1865 C  CA  . GLY   B 1 97  ? 37.364 -25.893 9.362  1.00 17.88  ? 103 GLY   C CA  1 
ATOM   1866 C  C   . GLY   B 1 97  ? 36.719 -24.935 8.392  1.00 17.72  ? 103 GLY   C C   1 
ATOM   1867 O  O   . GLY   B 1 97  ? 37.036 -23.735 8.378  1.00 19.34  ? 103 GLY   C O   1 
ATOM   1868 N  N   . HIS   B 1 98  ? 35.813 -25.453 7.557  1.00 17.27  ? 104 HIS   C N   1 
ATOM   1869 C  CA  . HIS   B 1 98  ? 35.160 -24.659 6.540  1.00 17.14  ? 104 HIS   C CA  1 
ATOM   1870 C  C   . HIS   B 1 98  ? 33.858 -24.001 7.050  1.00 16.67  ? 104 HIS   C C   1 
ATOM   1871 O  O   . HIS   B 1 98  ? 33.059 -24.637 7.742  1.00 16.36  ? 104 HIS   C O   1 
ATOM   1872 C  CB  . HIS   B 1 98  ? 34.882 -25.541 5.333  1.00 19.54  ? 104 HIS   C CB  1 
ATOM   1873 C  CG  . HIS   B 1 98  ? 34.322 -24.759 4.198  1.00 22.54  ? 104 HIS   C CG  1 
ATOM   1874 N  ND1 . HIS   B 1 98  ? 35.093 -23.814 3.518  1.00 24.83  ? 104 HIS   C ND1 1 
ATOM   1875 C  CD2 . HIS   B 1 98  ? 33.067 -24.749 3.698  1.00 25.33  ? 104 HIS   C CD2 1 
ATOM   1876 C  CE1 . HIS   B 1 98  ? 34.300 -23.321 2.582  1.00 27.14  ? 104 HIS   C CE1 1 
ATOM   1877 N  NE2 . HIS   B 1 98  ? 33.068 -23.853 2.649  1.00 27.49  ? 104 HIS   C NE2 1 
ATOM   1878 N  N   . SER   B 1 99  ? 33.657 -22.725 6.692  1.00 17.25  ? 105 SER   C N   1 
ATOM   1879 C  CA  . SER   B 1 99  ? 32.432 -22.001 7.078  1.00 17.78  ? 105 SER   C CA  1 
ATOM   1880 C  C   . SER   B 1 99  ? 32.203 -20.828 6.104  1.00 20.44  ? 105 SER   C C   1 
ATOM   1881 O  O   . SER   B 1 99  ? 33.079 -19.956 5.954  1.00 22.48  ? 105 SER   C O   1 
ATOM   1882 C  CB  . SER   B 1 99  ? 32.605 -21.442 8.485  1.00 18.94  ? 105 SER   C CB  1 
ATOM   1883 O  OG  . SER   B 1 99  ? 31.506 -20.596 8.817  1.00 20.23  ? 105 SER   C OG  1 
ATOM   1884 N  N   . GLU   B 1 100 ? 31.078 -20.874 5.408  1.00 19.71  ? 106 GLU   C N   1 
ATOM   1885 C  CA  . GLU   B 1 100 ? 30.606 -19.835 4.480  1.00 19.90  ? 106 GLU   C CA  1 
ATOM   1886 C  C   . GLU   B 1 100 ? 29.428 -19.138 5.129  1.00 18.63  ? 106 GLU   C C   1 
ATOM   1887 O  O   . GLU   B 1 100 ? 28.867 -19.677 6.068  1.00 16.32  ? 106 GLU   C O   1 
ATOM   1888 C  CB  . GLU   B 1 100 ? 30.108 -20.515 3.185  1.00 23.54  ? 106 GLU   C CB  1 
ATOM   1889 C  CG  . GLU   B 1 100 ? 31.228 -21.171 2.445  1.00 31.20  ? 106 GLU   C CG  1 
ATOM   1890 C  CD  . GLU   B 1 100 ? 30.815 -21.873 1.183  1.00 36.59  ? 106 GLU   C CD  1 
ATOM   1891 O  OE1 . GLU   B 1 100 ? 29.752 -21.538 0.614  1.00 42.49  ? 106 GLU   C OE1 1 
ATOM   1892 O  OE2 . GLU   B 1 100 ? 31.586 -22.749 0.748  1.00 36.00  ? 106 GLU   C OE2 1 
ATOM   1893 N  N   . PRO   B 1 101 ? 29.012 -17.961 4.661  1.00 18.88  ? 107 PRO   C N   1 
ATOM   1894 C  CA  . PRO   B 1 101 ? 27.861 -17.289 5.315  1.00 18.07  ? 107 PRO   C CA  1 
ATOM   1895 C  C   . PRO   B 1 101 ? 26.612 -18.163 5.473  1.00 18.50  ? 107 PRO   C C   1 
ATOM   1896 O  O   . PRO   B 1 101 ? 25.998 -18.134 6.537  1.00 18.46  ? 107 PRO   C O   1 
ATOM   1897 C  CB  . PRO   B 1 101 ? 27.613 -16.056 4.423  1.00 19.47  ? 107 PRO   C CB  1 
ATOM   1898 C  CG  . PRO   B 1 101 ? 28.907 -15.839 3.746  1.00 22.16  ? 107 PRO   C CG  1 
ATOM   1899 C  CD  . PRO   B 1 101 ? 29.618 -17.125 3.598  1.00 20.66  ? 107 PRO   C CD  1 
ATOM   1900 N  N   . GLY   B 1 102 ? 26.282 -18.988 4.465  1.00 17.72  ? 108 GLY   C N   1 
ATOM   1901 C  CA  . GLY   B 1 102 ? 25.081 -19.831 4.555  1.00 17.12  ? 108 GLY   C CA  1 
ATOM   1902 C  C   . GLY   B 1 102 ? 25.195 -20.909 5.637  1.00 17.39  ? 108 GLY   C C   1 
ATOM   1903 O  O   . GLY   B 1 102 ? 24.223 -21.607 5.957  1.00 18.05  ? 108 GLY   C O   1 
ATOM   1904 N  N   . ASP   B 1 103 ? 26.425 -21.187 6.123  1.00 15.93  ? 109 ASP   C N   1 
ATOM   1905 C  CA  . ASP   B 1 103 ? 26.611 -22.192 7.180  1.00 14.75  ? 109 ASP   C CA  1 
ATOM   1906 C  C   . ASP   B 1 103 ? 26.228 -21.707 8.561  1.00 14.94  ? 109 ASP   C C   1 
ATOM   1907 O  O   . ASP   B 1 103 ? 26.111 -22.508 9.490  1.00 14.52  ? 109 ASP   C O   1 
ATOM   1908 C  CB  . ASP   B 1 103 ? 28.064 -22.660 7.220  1.00 15.18  ? 109 ASP   C CB  1 
ATOM   1909 C  CG  . ASP   B 1 103 ? 28.413 -23.446 5.998  1.00 18.47  ? 109 ASP   C CG  1 
ATOM   1910 O  OD1 . ASP   B 1 103 ? 27.569 -24.219 5.549  1.00 17.70  ? 109 ASP   C OD1 1 
ATOM   1911 O  OD2 . ASP   B 1 103 ? 29.557 -23.281 5.494  1.00 19.60  ? 109 ASP   C OD2 1 
ATOM   1912 N  N   . CYS   B 1 104 ? 25.981 -20.383 8.729  1.00 14.61  ? 110 CYS   C N   1 
ATOM   1913 C  CA  . CYS   B 1 104 ? 25.577 -19.838 10.035 1.00 14.84  ? 110 CYS   C CA  1 
ATOM   1914 C  C   . CYS   B 1 104 ? 24.332 -20.551 10.549 1.00 14.52  ? 110 CYS   C C   1 
ATOM   1915 O  O   . CYS   B 1 104 ? 23.400 -20.789 9.781  1.00 15.76  ? 110 CYS   C O   1 
ATOM   1916 C  CB  . CYS   B 1 104 ? 25.340 -18.324 9.937  1.00 13.94  ? 110 CYS   C CB  1 
ATOM   1917 S  SG  . CYS   B 1 104 ? 26.869 -17.344 9.847  1.00 16.99  ? 110 CYS   C SG  1 
ATOM   1918 N  N   . GLY   B 1 105 ? 24.332 -20.889 11.827 1.00 13.06  ? 111 GLY   C N   1 
ATOM   1919 C  CA  . GLY   B 1 105 ? 23.177 -21.592 12.404 1.00 14.46  ? 111 GLY   C CA  1 
ATOM   1920 C  C   . GLY   B 1 105 ? 23.392 -23.088 12.565 1.00 13.71  ? 111 GLY   C C   1 
ATOM   1921 O  O   . GLY   B 1 105 ? 22.630 -23.736 13.284 1.00 14.65  ? 111 GLY   C O   1 
ATOM   1922 N  N   . GLY   B 1 106 ? 24.446 -23.643 11.935 1.00 13.34  ? 112 GLY   C N   1 
ATOM   1923 C  CA  . GLY   B 1 106 ? 24.757 -25.072 12.083 1.00 13.98  ? 112 GLY   C CA  1 
ATOM   1924 C  C   . GLY   B 1 106 ? 25.157 -25.356 13.524 1.00 13.52  ? 112 GLY   C C   1 
ATOM   1925 O  O   . GLY   B 1 106 ? 25.885 -24.564 14.143 1.00 13.52  ? 112 GLY   C O   1 
ATOM   1926 N  N   . ILE   B 1 107 ? 24.716 -26.487 14.063 1.00 13.65  ? 113 ILE   C N   1 
ATOM   1927 C  CA  . ILE   B 1 107 ? 24.981 -26.781 15.468 1.00 12.88  ? 113 ILE   C CA  1 
ATOM   1928 C  C   . ILE   B 1 107 ? 26.371 -27.396 15.655 1.00 12.59  ? 113 ILE   C C   1 
ATOM   1929 O  O   . ILE   B 1 107 ? 26.780 -28.254 14.873 1.00 13.43  ? 113 ILE   C O   1 
ATOM   1930 C  CB  . ILE   B 1 107 ? 23.874 -27.755 15.971 1.00 15.23  ? 113 ILE   C CB  1 
ATOM   1931 C  CG1 . ILE   B 1 107 ? 22.626 -26.855 16.385 1.00 19.52  ? 113 ILE   C CG1 1 
ATOM   1932 C  CG2 . ILE   B 1 107 ? 24.307 -28.588 17.176 1.00 14.90  ? 113 ILE   C CG2 1 
ATOM   1933 C  CD1 . ILE   B 1 107 ? 21.270 -27.646 16.715 1.00 23.65  ? 113 ILE   C CD1 1 
ATOM   1934 N  N   . LEU   B 1 108 ? 27.027 -26.977 16.750 1.00 11.94  ? 114 LEU   C N   1 
ATOM   1935 C  CA  . LEU   B 1 108 ? 28.221 -27.626 17.306 1.00 11.90  ? 114 LEU   C CA  1 
ATOM   1936 C  C   . LEU   B 1 108 ? 27.715 -28.406 18.540 1.00 12.71  ? 114 LEU   C C   1 
ATOM   1937 O  O   . LEU   B 1 108 ? 27.066 -27.811 19.395 1.00 12.60  ? 114 LEU   C O   1 
ATOM   1938 C  CB  . LEU   B 1 108 ? 29.235 -26.537 17.725 1.00 12.18  ? 114 LEU   C CB  1 
ATOM   1939 C  CG  . LEU   B 1 108 ? 30.448 -27.047 18.542 1.00 13.56  ? 114 LEU   C CG  1 
ATOM   1940 C  CD1 . LEU   B 1 108 ? 31.378 -27.944 17.698 1.00 14.18  ? 114 LEU   C CD1 1 
ATOM   1941 C  CD2 . LEU   B 1 108 ? 31.281 -25.861 19.085 1.00 14.76  ? 114 LEU   C CD2 1 
ATOM   1942 N  N   . ARG   B 1 109 ? 28.015 -29.706 18.623 1.00 13.04  ? 115 ARG   C N   1 
ATOM   1943 C  CA  . ARG   B 1 109 ? 27.553 -30.523 19.764 1.00 13.69  ? 115 ARG   C CA  1 
ATOM   1944 C  C   . ARG   B 1 109 ? 28.691 -31.343 20.329 1.00 13.77  ? 115 ARG   C C   1 
ATOM   1945 O  O   . ARG   B 1 109 ? 29.635 -31.718 19.630 1.00 13.70  ? 115 ARG   C O   1 
ATOM   1946 C  CB  . ARG   B 1 109 ? 26.388 -31.434 19.336 1.00 17.01  ? 115 ARG   C CB  1 
ATOM   1947 C  CG  . ARG   B 1 109 ? 26.798 -32.408 18.241 1.00 19.68  ? 115 ARG   C CG  1 
ATOM   1948 C  CD  . ARG   B 1 109 ? 25.637 -33.302 17.815 1.00 25.32  ? 115 ARG   C CD  1 
ATOM   1949 N  NE  . ARG   B 1 109 ? 24.654 -32.558 17.004 1.00 31.45  ? 115 ARG   C NE  1 
ATOM   1950 C  CZ  . ARG   B 1 109 ? 23.404 -32.280 17.390 1.00 40.43  ? 115 ARG   C CZ  1 
ATOM   1951 N  NH1 . ARG   B 1 109 ? 22.988 -32.605 18.612 1.00 41.71  ? 115 ARG   C NH1 1 
ATOM   1952 N  NH2 . ARG   B 1 109 ? 22.584 -31.615 16.581 1.00 42.25  ? 115 ARG   C NH2 1 
ATOM   1953 N  N   . CYS   B 1 110 ? 28.561 -31.606 21.636 1.00 13.49  ? 116 CYS   C N   1 
ATOM   1954 C  CA  . CYS   B 1 110 ? 29.548 -32.470 22.342 1.00 14.25  ? 116 CYS   C CA  1 
ATOM   1955 C  C   . CYS   B 1 110 ? 28.728 -33.585 23.012 1.00 15.87  ? 116 CYS   C C   1 
ATOM   1956 O  O   . CYS   B 1 110 ? 27.496 -33.702 22.795 1.00 15.92  ? 116 CYS   C O   1 
ATOM   1957 C  CB  . CYS   B 1 110 ? 30.346 -31.673 23.377 1.00 12.71  ? 116 CYS   C CB  1 
ATOM   1958 S  SG  . CYS   B 1 110 ? 29.305 -31.027 24.754 1.00 14.06  ? 116 CYS   C SG  1 
ATOM   1959 N  N   . GLN   B 1 111 ? 29.388 -34.416 23.888 1.00 16.15  ? 117 GLN   C N   1 
ATOM   1960 C  CA  . GLN   B 1 111 ? 28.631 -35.474 24.586 1.00 17.54  ? 117 GLN   C CA  1 
ATOM   1961 C  C   . GLN   B 1 111 ? 27.534 -34.933 25.500 1.00 18.08  ? 117 GLN   C C   1 
ATOM   1962 O  O   . GLN   B 1 111 ? 26.590 -35.667 25.861 1.00 19.98  ? 117 GLN   C O   1 
ATOM   1963 C  CB  . GLN   B 1 111 ? 29.559 -36.419 25.400 1.00 18.20  ? 117 GLN   C CB  1 
ATOM   1964 C  CG  . GLN   B 1 111 ? 30.241 -35.677 26.559 1.00 21.09  ? 117 GLN   C CG  1 
ATOM   1965 C  CD  . GLN   B 1 111 ? 31.194 -36.546 27.322 1.00 30.87  ? 117 GLN   C CD  1 
ATOM   1966 O  OE1 . GLN   B 1 111 ? 32.379 -36.630 26.986 1.00 32.36  ? 117 GLN   C OE1 1 
ATOM   1967 N  NE2 . GLN   B 1 111 ? 30.704 -37.151 28.391 1.00 32.66  ? 117 GLN   C NE2 1 
ATOM   1968 N  N   . HIS   B 1 112 ? 27.611 -33.642 25.880 1.00 16.84  ? 118 HIS   C N   1 
ATOM   1969 C  CA  . HIS   B 1 112 ? 26.609 -33.068 26.798 1.00 17.12  ? 118 HIS   C CA  1 
ATOM   1970 C  C   . HIS   B 1 112 ? 25.420 -32.400 26.125 1.00 17.85  ? 118 HIS   C C   1 
ATOM   1971 O  O   . HIS   B 1 112 ? 24.445 -32.066 26.804 1.00 20.03  ? 118 HIS   C O   1 
ATOM   1972 C  CB  . HIS   B 1 112 ? 27.299 -32.102 27.739 1.00 17.30  ? 118 HIS   C CB  1 
ATOM   1973 C  CG  . HIS   B 1 112 ? 28.468 -32.734 28.457 1.00 16.99  ? 118 HIS   C CG  1 
ATOM   1974 N  ND1 . HIS   B 1 112 ? 29.801 -32.436 28.144 1.00 16.98  ? 118 HIS   C ND1 1 
ATOM   1975 C  CD2 . HIS   B 1 112 ? 28.457 -33.573 29.524 1.00 21.01  ? 118 HIS   C CD2 1 
ATOM   1976 C  CE1 . HIS   B 1 112 ? 30.531 -33.146 28.993 1.00 20.03  ? 118 HIS   C CE1 1 
ATOM   1977 N  NE2 . HIS   B 1 112 ? 29.771 -33.842 29.826 1.00 21.55  ? 118 HIS   C NE2 1 
ATOM   1978 N  N   . GLY   B 1 113 ? 25.521 -32.131 24.823 1.00 16.62  ? 119 GLY   C N   1 
ATOM   1979 C  CA  . GLY   B 1 113 ? 24.434 -31.453 24.116 1.00 15.87  ? 119 GLY   C CA  1 
ATOM   1980 C  C   . GLY   B 1 113 ? 24.923 -30.382 23.166 1.00 15.15  ? 119 GLY   C C   1 
ATOM   1981 O  O   . GLY   B 1 113 ? 26.060 -30.449 22.680 1.00 14.72  ? 119 GLY   C O   1 
ATOM   1982 N  N   . VAL   B 1 114 ? 24.075 -29.393 22.903 1.00 15.37  ? 120 VAL   C N   1 
ATOM   1983 C  CA  . VAL   B 1 114 ? 24.396 -28.336 21.967 1.00 14.66  ? 120 VAL   C CA  1 
ATOM   1984 C  C   . VAL   B 1 114 ? 25.325 -27.321 22.651 1.00 14.55  ? 120 VAL   C C   1 
ATOM   1985 O  O   . VAL   B 1 114 ? 25.016 -26.784 23.734 1.00 15.40  ? 120 VAL   C O   1 
ATOM   1986 C  CB  . VAL   B 1 114 ? 23.100 -27.643 21.474 1.00 14.86  ? 120 VAL   C CB  1 
ATOM   1987 C  CG1 . VAL   B 1 114 ? 23.435 -26.437 20.620 1.00 16.36  ? 120 VAL   C CG1 1 
ATOM   1988 C  CG2 . VAL   B 1 114 ? 22.186 -28.622 20.721 1.00 16.91  ? 120 VAL   C CG2 1 
ATOM   1989 N  N   . VAL   B 1 115 ? 26.498 -27.087 22.073 1.00 12.81  ? 121 VAL   C N   1 
ATOM   1990 C  CA  . VAL   B 1 115 ? 27.504 -26.119 22.566 1.00 13.43  ? 121 VAL   C CA  1 
ATOM   1991 C  C   . VAL   B 1 115 ? 27.290 -24.714 22.024 1.00 14.43  ? 121 VAL   C C   1 
ATOM   1992 O  O   . VAL   B 1 115 ? 27.502 -23.732 22.744 1.00 14.38  ? 121 VAL   C O   1 
ATOM   1993 C  CB  . VAL   B 1 115 ? 28.906 -26.629 22.199 1.00 13.14  ? 121 VAL   C CB  1 
ATOM   1994 C  CG1 . VAL   B 1 115 ? 29.975 -25.632 22.623 1.00 14.64  ? 121 VAL   C CG1 1 
ATOM   1995 C  CG2 . VAL   B 1 115 ? 29.155 -28.007 22.790 1.00 15.04  ? 121 VAL   C CG2 1 
ATOM   1996 N  N   . GLY   B 1 116 ? 26.930 -24.610 20.750 1.00 13.55  ? 122 GLY   C N   1 
ATOM   1997 C  CA  . GLY   B 1 116 ? 26.727 -23.309 20.132 1.00 15.24  ? 122 GLY   C CA  1 
ATOM   1998 C  C   . GLY   B 1 116 ? 26.378 -23.463 18.672 1.00 13.18  ? 122 GLY   C C   1 
ATOM   1999 O  O   . GLY   B 1 116 ? 26.053 -24.578 18.236 1.00 13.56  ? 122 GLY   C O   1 
ATOM   2000 N  N   . ILE   B 1 117 ? 26.372 -22.323 17.952 1.00 12.26  ? 123 ILE   C N   1 
ATOM   2001 C  CA  . ILE   B 1 117 ? 26.030 -22.371 16.531 1.00 12.58  ? 123 ILE   C CA  1 
ATOM   2002 C  C   . ILE   B 1 117 ? 27.078 -21.630 15.734 1.00 13.24  ? 123 ILE   C C   1 
ATOM   2003 O  O   . ILE   B 1 117 ? 27.680 -20.669 16.206 1.00 13.82  ? 123 ILE   C O   1 
ATOM   2004 C  CB  . ILE   B 1 117 ? 24.618 -21.740 16.251 1.00 13.57  ? 123 ILE   C CB  1 
ATOM   2005 C  CG1 . ILE   B 1 117 ? 24.464 -20.339 16.874 1.00 15.92  ? 123 ILE   C CG1 1 
ATOM   2006 C  CG2 . ILE   B 1 117 ? 23.499 -22.686 16.666 1.00 15.24  ? 123 ILE   C CG2 1 
ATOM   2007 C  CD1 . ILE   B 1 117 ? 23.166 -19.556 16.413 1.00 15.68  ? 123 ILE   C CD1 1 
ATOM   2008 N  N   . VAL   B 1 118 ? 27.243 -22.033 14.462 1.00 12.73  ? 124 VAL   C N   1 
ATOM   2009 C  CA  . VAL   B 1 118 ? 28.188 -21.358 13.562 1.00 13.25  ? 124 VAL   C CA  1 
ATOM   2010 C  C   . VAL   B 1 118 ? 27.797 -19.876 13.424 1.00 14.08  ? 124 VAL   C C   1 
ATOM   2011 O  O   . VAL   B 1 118 ? 26.596 -19.547 13.225 1.00 13.24  ? 124 VAL   C O   1 
ATOM   2012 C  CB  . VAL   B 1 118 ? 28.185 -22.032 12.178 1.00 12.61  ? 124 VAL   C CB  1 
ATOM   2013 C  CG1 . VAL   B 1 118 ? 29.059 -21.266 11.186 1.00 13.93  ? 124 VAL   C CG1 1 
ATOM   2014 C  CG2 . VAL   B 1 118 ? 28.653 -23.484 12.240 1.00 14.47  ? 124 VAL   C CG2 1 
ATOM   2015 N  N   . SER   B 1 119 ? 28.796 -19.013 13.514 1.00 13.20  ? 125 SER   C N   1 
ATOM   2016 C  CA  . SER   B 1 119 ? 28.580 -17.548 13.420 1.00 14.09  ? 125 SER   C CA  1 
ATOM   2017 C  C   . SER   B 1 119 ? 29.591 -16.870 12.497 1.00 15.58  ? 125 SER   C C   1 
ATOM   2018 O  O   . SER   B 1 119 ? 29.255 -15.811 11.940 1.00 14.94  ? 125 SER   C O   1 
ATOM   2019 C  CB  . SER   B 1 119 ? 28.635 -16.947 14.826 1.00 14.99  ? 125 SER   C CB  1 
ATOM   2020 O  OG  . SER   B 1 119 ? 28.506 -15.513 14.764 1.00 16.64  ? 125 SER   C OG  1 
ATOM   2021 N  N   . THR   B 1 120 ? 30.846 -17.399 12.382 1.00 15.40  ? 126 THR   C N   1 
ATOM   2022 C  CA  . THR   B 1 120 ? 31.866 -16.712 11.582 1.00 15.25  ? 126 THR   C CA  1 
ATOM   2023 C  C   . THR   B 1 120 ? 32.600 -17.725 10.691 1.00 14.42  ? 126 THR   C C   1 
ATOM   2024 O  O   . THR   B 1 120 ? 32.523 -18.940 10.922 1.00 14.94  ? 126 THR   C O   1 
ATOM   2025 C  CB  . THR   B 1 120 ? 32.935 -15.972 12.464 1.00 16.48  ? 126 THR   C CB  1 
ATOM   2026 O  OG1 . THR   B 1 120 ? 33.828 -16.912 13.100 1.00 16.66  ? 126 THR   C OG1 1 
ATOM   2027 C  CG2 . THR   B 1 120 ? 32.341 -15.001 13.468 1.00 18.16  ? 126 THR   C CG2 1 
ATOM   2028 N  N   . GLY   B 1 121 ? 33.302 -17.227 9.673  1.00 16.42  ? 127 GLY   C N   1 
ATOM   2029 C  CA  . GLY   B 1 121 ? 34.083 -18.094 8.797  1.00 18.65  ? 127 GLY   C CA  1 
ATOM   2030 C  C   . GLY   B 1 121 ? 35.108 -17.294 8.017  1.00 22.31  ? 127 GLY   C C   1 
ATOM   2031 O  O   . GLY   B 1 121 ? 35.017 -16.084 7.905  1.00 24.11  ? 127 GLY   C O   1 
ATOM   2032 N  N   . GLY   B 1 122 ? 36.030 -17.978 7.391  1.00 24.73  ? 128 GLY   C N   1 
ATOM   2033 C  CA  . GLY   B 1 122 ? 37.097 -17.334 6.612  1.00 26.72  ? 128 GLY   C CA  1 
ATOM   2034 C  C   . GLY   B 1 122 ? 38.483 -17.704 7.120  1.00 26.91  ? 128 GLY   C C   1 
ATOM   2035 O  O   . GLY   B 1 122 ? 38.659 -18.098 8.271  1.00 25.91  ? 128 GLY   C O   1 
ATOM   2036 N  N   . ASN   B 1 123 ? 39.492 -17.517 6.274  1.00 26.21  ? 129 ASN   C N   1 
ATOM   2037 C  CA  . ASN   B 1 123 ? 40.896 -17.858 6.574  1.00 26.63  ? 129 ASN   C CA  1 
ATOM   2038 C  C   . ASN   B 1 123 ? 41.037 -19.336 7.011  1.00 24.79  ? 129 ASN   C C   1 
ATOM   2039 O  O   . ASN   B 1 123 ? 42.017 -19.665 7.671  1.00 27.74  ? 129 ASN   C O   1 
ATOM   2040 C  CB  . ASN   B 1 123 ? 41.537 -16.906 7.640  1.00 30.06  ? 129 ASN   C CB  1 
ATOM   2041 C  CG  . ASN   B 1 123 ? 42.510 -15.846 7.131  1.00 37.08  ? 129 ASN   C CG  1 
ATOM   2042 O  OD1 . ASN   B 1 123 ? 42.988 -15.852 5.971  1.00 38.24  ? 129 ASN   C OD1 1 
ATOM   2043 N  ND2 . ASN   B 1 123 ? 42.847 -14.903 8.000  1.00 38.74  ? 129 ASN   C ND2 1 
ATOM   2044 N  N   . GLY   B 1 124 ? 40.107 -20.218 6.617  1.00 22.37  ? 130 GLY   C N   1 
ATOM   2045 C  CA  . GLY   B 1 124 ? 40.188 -21.630 7.004  1.00 21.57  ? 130 GLY   C CA  1 
ATOM   2046 C  C   . GLY   B 1 124 ? 39.823 -21.917 8.440  1.00 18.81  ? 130 GLY   C C   1 
ATOM   2047 O  O   . GLY   B 1 124 ? 40.111 -23.001 8.944  1.00 18.98  ? 130 GLY   C O   1 
ATOM   2048 N  N   . LEU   B 1 125 ? 39.155 -20.964 9.085  1.00 17.41  ? 131 LEU   C N   1 
ATOM   2049 C  CA  . LEU   B 1 125 ? 38.672 -21.103 10.460 1.00 17.71  ? 131 LEU   C CA  1 
ATOM   2050 C  C   . LEU   B 1 125 ? 37.136 -21.003 10.479 1.00 16.99  ? 131 LEU   C C   1 
ATOM   2051 O  O   . LEU   B 1 125 ? 36.525 -20.321 9.632  1.00 19.22  ? 131 LEU   C O   1 
ATOM   2052 C  CB  . LEU   B 1 125 ? 39.236 -19.985 11.322 1.00 19.00  ? 131 LEU   C CB  1 
ATOM   2053 C  CG  . LEU   B 1 125 ? 40.761 -19.927 11.338 1.00 22.84  ? 131 LEU   C CG  1 
ATOM   2054 C  CD1 . LEU   B 1 125 ? 41.242 -18.483 11.636 1.00 27.06  ? 131 LEU   C CD1 1 
ATOM   2055 C  CD2 . LEU   B 1 125 ? 41.323 -20.981 12.256 1.00 23.62  ? 131 LEU   C CD2 1 
ATOM   2056 N  N   . VAL   B 1 126 ? 36.521 -21.674 11.406 1.00 14.64  ? 132 VAL   C N   1 
ATOM   2057 C  CA  . VAL   B 1 126 ? 35.066 -21.553 11.631 1.00 13.49  ? 132 VAL   C CA  1 
ATOM   2058 C  C   . VAL   B 1 126 ? 34.910 -21.077 13.096 1.00 13.54  ? 132 VAL   C C   1 
ATOM   2059 O  O   . VAL   B 1 126 ? 35.584 -21.556 14.022 1.00 14.51  ? 132 VAL   C O   1 
ATOM   2060 C  CB  . VAL   B 1 126 ? 34.344 -22.899 11.387 1.00 13.70  ? 132 VAL   C CB  1 
ATOM   2061 C  CG1 . VAL   B 1 126 ? 34.987 -24.044 12.140 1.00 15.53  ? 132 VAL   C CG1 1 
ATOM   2062 C  CG2 . VAL   B 1 126 ? 32.847 -22.816 11.716 1.00 13.90  ? 132 VAL   C CG2 1 
ATOM   2063 N  N   . GLY   B 1 127 ? 34.015 -20.109 13.271 1.00 14.15  ? 133 GLY   C N   1 
ATOM   2064 C  CA  . GLY   B 1 127 ? 33.744 -19.586 14.616 1.00 13.96  ? 133 GLY   C CA  1 
ATOM   2065 C  C   . GLY   B 1 127 ? 32.333 -19.930 15.077 1.00 14.20  ? 133 GLY   C C   1 
ATOM   2066 O  O   . GLY   B 1 127 ? 31.389 -19.824 14.296 1.00 13.79  ? 133 GLY   C O   1 
ATOM   2067 N  N   . PHE   B 1 128 ? 32.187 -20.297 16.368 1.00 12.38  ? 134 PHE   C N   1 
ATOM   2068 C  CA  . PHE   B 1 128 ? 30.894 -20.665 16.952 1.00 13.44  ? 134 PHE   C CA  1 
ATOM   2069 C  C   . PHE   B 1 128 ? 30.539 -19.725 18.073 1.00 14.16  ? 134 PHE   C C   1 
ATOM   2070 O  O   . PHE   B 1 128 ? 31.388 -19.458 18.951 1.00 14.77  ? 134 PHE   C O   1 
ATOM   2071 C  CB  . PHE   B 1 128 ? 30.977 -22.110 17.540 1.00 12.68  ? 134 PHE   C CB  1 
ATOM   2072 C  CG  . PHE   B 1 128 ? 31.520 -23.141 16.549 1.00 13.08  ? 134 PHE   C CG  1 
ATOM   2073 C  CD1 . PHE   B 1 128 ? 30.688 -23.734 15.609 1.00 13.24  ? 134 PHE   C CD1 1 
ATOM   2074 C  CD2 . PHE   B 1 128 ? 32.871 -23.494 16.546 1.00 13.79  ? 134 PHE   C CD2 1 
ATOM   2075 C  CE1 . PHE   B 1 128 ? 31.177 -24.684 14.736 1.00 13.45  ? 134 PHE   C CE1 1 
ATOM   2076 C  CE2 . PHE   B 1 128 ? 33.367 -24.457 15.661 1.00 14.30  ? 134 PHE   C CE2 1 
ATOM   2077 C  CZ  . PHE   B 1 128 ? 32.535 -25.008 14.734 1.00 13.52  ? 134 PHE   C CZ  1 
ATOM   2078 N  N   . ALA   B 1 129 ? 29.268 -19.274 18.071 1.00 13.23  ? 135 ALA   C N   1 
ATOM   2079 C  CA  . ALA   B 1 129 ? 28.767 -18.474 19.183 1.00 13.75  ? 135 ALA   C CA  1 
ATOM   2080 C  C   . ALA   B 1 129 ? 28.385 -19.462 20.312 1.00 14.51  ? 135 ALA   C C   1 
ATOM   2081 O  O   . ALA   B 1 129 ? 27.474 -20.287 20.140 1.00 14.56  ? 135 ALA   C O   1 
ATOM   2082 C  CB  . ALA   B 1 129 ? 27.550 -17.680 18.714 1.00 14.89  ? 135 ALA   C CB  1 
ATOM   2083 N  N   . ASP   B 1 130 ? 29.034 -19.344 21.473 1.00 13.58  ? 136 ASP   C N   1 
ATOM   2084 C  CA  . ASP   B 1 130 ? 28.753 -20.232 22.592 1.00 14.58  ? 136 ASP   C CA  1 
ATOM   2085 C  C   . ASP   B 1 130 ? 27.393 -19.923 23.183 1.00 15.77  ? 136 ASP   C C   1 
ATOM   2086 O  O   . ASP   B 1 130 ? 27.027 -18.753 23.285 1.00 15.87  ? 136 ASP   C O   1 
ATOM   2087 C  CB  . ASP   B 1 130 ? 29.822 -19.984 23.701 1.00 16.59  ? 136 ASP   C CB  1 
ATOM   2088 C  CG  . ASP   B 1 130 ? 29.713 -20.909 24.890 1.00 20.86  ? 136 ASP   C CG  1 
ATOM   2089 O  OD1 . ASP   B 1 130 ? 29.660 -22.125 24.691 1.00 19.18  ? 136 ASP   C OD1 1 
ATOM   2090 O  OD2 . ASP   B 1 130 ? 29.645 -20.391 26.043 1.00 22.79  ? 136 ASP   C OD2 1 
ATOM   2091 N  N   . VAL   B 1 131 ? 26.705 -20.945 23.698 1.00 14.65  ? 137 VAL   C N   1 
ATOM   2092 C  CA  . VAL   B 1 131 ? 25.457 -20.761 24.453 1.00 15.74  ? 137 VAL   C CA  1 
ATOM   2093 C  C   . VAL   B 1 131 ? 25.509 -21.459 25.827 1.00 16.22  ? 137 VAL   C C   1 
ATOM   2094 O  O   . VAL   B 1 131 ? 24.532 -21.404 26.577 1.00 16.40  ? 137 VAL   C O   1 
ATOM   2095 C  CB  . VAL   B 1 131 ? 24.210 -21.231 23.673 1.00 15.65  ? 137 VAL   C CB  1 
ATOM   2096 C  CG1 . VAL   B 1 131 ? 24.089 -20.433 22.359 1.00 16.04  ? 137 VAL   C CG1 1 
ATOM   2097 C  CG2 . VAL   B 1 131 ? 24.238 -22.722 23.385 1.00 15.20  ? 137 VAL   C CG2 1 
ATOM   2098 N  N   . ARG   B 1 132 ? 26.652 -22.100 26.182 1.00 15.17  ? 138 ARG   C N   1 
ATOM   2099 C  CA  . ARG   B 1 132 ? 26.739 -22.869 27.459 1.00 14.96  ? 138 ARG   C CA  1 
ATOM   2100 C  C   . ARG   B 1 132 ? 26.667 -22.038 28.703 1.00 16.66  ? 138 ARG   C C   1 
ATOM   2101 O  O   . ARG   B 1 132 ? 26.342 -22.597 29.765 1.00 18.25  ? 138 ARG   C O   1 
ATOM   2102 C  CB  . ARG   B 1 132 ? 28.012 -23.696 27.467 1.00 14.71  ? 138 ARG   C CB  1 
ATOM   2103 C  CG  . ARG   B 1 132 ? 27.987 -24.773 26.345 1.00 14.75  ? 138 ARG   C CG  1 
ATOM   2104 C  CD  . ARG   B 1 132 ? 29.320 -25.533 26.380 1.00 14.96  ? 138 ARG   C CD  1 
ATOM   2105 N  NE  . ARG   B 1 132 ? 30.407 -24.623 25.999 1.00 14.66  ? 138 ARG   C NE  1 
ATOM   2106 C  CZ  . ARG   B 1 132 ? 31.666 -25.005 25.840 1.00 16.04  ? 138 ARG   C CZ  1 
ATOM   2107 N  NH1 . ARG   B 1 132 ? 32.043 -26.239 26.182 1.00 15.14  ? 138 ARG   C NH1 1 
ATOM   2108 N  NH2 . ARG   B 1 132 ? 32.565 -24.154 25.368 1.00 16.42  ? 138 ARG   C NH2 1 
ATOM   2109 N  N   . ASP   B 1 133 ? 26.893 -20.723 28.600 1.00 16.19  ? 139 ASP   C N   1 
ATOM   2110 C  CA  . ASP   B 1 133 ? 26.833 -19.857 29.778 1.00 16.34  ? 139 ASP   C CA  1 
ATOM   2111 C  C   . ASP   B 1 133 ? 25.415 -19.287 29.999 1.00 17.14  ? 139 ASP   C C   1 
ATOM   2112 O  O   . ASP   B 1 133 ? 25.220 -18.629 31.020 1.00 17.47  ? 139 ASP   C O   1 
ATOM   2113 C  CB  . ASP   B 1 133 ? 27.817 -18.657 29.648 1.00 16.90  ? 139 ASP   C CB  1 
ATOM   2114 C  CG  . ASP   B 1 133 ? 27.456 -17.740 28.502 1.00 21.36  ? 139 ASP   C CG  1 
ATOM   2115 O  OD1 . ASP   B 1 133 ? 27.122 -18.247 27.419 1.00 19.85  ? 139 ASP   C OD1 1 
ATOM   2116 O  OD2 . ASP   B 1 133 ? 27.441 -16.508 28.709 1.00 21.95  ? 139 ASP   C OD2 1 
ATOM   2117 N  N   . LEU   B 1 134 ? 24.458 -19.515 29.071 1.00 16.76  ? 140 LEU   C N   1 
ATOM   2118 C  CA  . LEU   B 1 134 ? 23.111 -18.936 29.172 1.00 16.71  ? 140 LEU   C CA  1 
ATOM   2119 C  C   . LEU   B 1 134 ? 22.267 -19.942 29.929 1.00 17.70  ? 140 LEU   C C   1 
ATOM   2120 O  O   . LEU   B 1 134 ? 21.468 -20.686 29.364 1.00 17.51  ? 140 LEU   C O   1 
ATOM   2121 C  CB  . LEU   B 1 134 ? 22.564 -18.691 27.744 1.00 16.79  ? 140 LEU   C CB  1 
ATOM   2122 C  CG  . LEU   B 1 134 ? 23.399 -17.773 26.861 1.00 17.47  ? 140 LEU   C CG  1 
ATOM   2123 C  CD1 . LEU   B 1 134 ? 22.842 -17.713 25.403 1.00 18.96  ? 140 LEU   C CD1 1 
ATOM   2124 C  CD2 . LEU   B 1 134 ? 23.545 -16.379 27.456 1.00 20.02  ? 140 LEU   C CD2 1 
ATOM   2125 N  N   . LEU   B 1 135 ? 22.490 -20.002 31.247 1.00 18.21  ? 141 LEU   C N   1 
ATOM   2126 C  CA  . LEU   B 1 135 ? 21.834 -21.034 32.079 1.00 19.04  ? 141 LEU   C CA  1 
ATOM   2127 C  C   . LEU   B 1 135 ? 20.344 -20.933 32.097 1.00 19.02  ? 141 LEU   C C   1 
ATOM   2128 O  O   . LEU   B 1 135 ? 19.661 -21.937 32.290 1.00 19.33  ? 141 LEU   C O   1 
ATOM   2129 C  CB  . LEU   B 1 135 ? 22.403 -21.046 33.518 1.00 19.34  ? 141 LEU   C CB  1 
ATOM   2130 C  CG  . LEU   B 1 135 ? 23.962 -21.032 33.598 1.00 19.34  ? 141 LEU   C CG  1 
ATOM   2131 C  CD1 . LEU   B 1 135 ? 24.452 -21.054 35.085 1.00 21.67  ? 141 LEU   C CD1 1 
ATOM   2132 C  CD2 . LEU   B 1 135 ? 24.602 -22.203 32.834 1.00 20.60  ? 141 LEU   C CD2 1 
ATOM   2133 N  N   . TRP   B 1 136 ? 19.829 -19.721 31.922 1.00 18.48  ? 142 TRP   C N   1 
ATOM   2134 C  CA  . TRP   B 1 136 ? 18.389 -19.493 31.959 1.00 19.44  ? 142 TRP   C CA  1 
ATOM   2135 C  C   . TRP   B 1 136 ? 17.660 -20.182 30.810 1.00 20.72  ? 142 TRP   C C   1 
ATOM   2136 O  O   . TRP   B 1 136 ? 16.436 -20.312 30.881 1.00 22.15  ? 142 TRP   C O   1 
ATOM   2137 C  CB  . TRP   B 1 136 ? 18.084 -17.984 31.963 1.00 19.45  ? 142 TRP   C CB  1 
ATOM   2138 C  CG  . TRP   B 1 136 ? 18.756 -17.214 30.862 1.00 18.91  ? 142 TRP   C CG  1 
ATOM   2139 C  CD1 . TRP   B 1 136 ? 19.935 -16.528 30.940 1.00 19.32  ? 142 TRP   C CD1 1 
ATOM   2140 C  CD2 . TRP   B 1 136 ? 18.251 -16.993 29.518 1.00 18.08  ? 142 TRP   C CD2 1 
ATOM   2141 N  NE1 . TRP   B 1 136 ? 20.212 -15.926 29.722 1.00 19.59  ? 142 TRP   C NE1 1 
ATOM   2142 C  CE2 . TRP   B 1 136 ? 19.182 -16.183 28.845 1.00 19.04  ? 142 TRP   C CE2 1 
ATOM   2143 C  CE3 . TRP   B 1 136 ? 17.110 -17.405 28.836 1.00 19.18  ? 142 TRP   C CE3 1 
ATOM   2144 C  CZ2 . TRP   B 1 136 ? 19.029 -15.817 27.493 1.00 19.56  ? 142 TRP   C CZ2 1 
ATOM   2145 C  CZ3 . TRP   B 1 136 ? 16.926 -16.994 27.527 1.00 20.00  ? 142 TRP   C CZ3 1 
ATOM   2146 C  CH2 . TRP   B 1 136 ? 17.889 -16.223 26.864 1.00 19.94  ? 142 TRP   C CH2 1 
ATOM   2147 N  N   . LEU   B 1 137 ? 18.368 -20.637 29.754 1.00 19.12  ? 143 LEU   C N   1 
ATOM   2148 C  CA  . LEU   B 1 137 ? 17.685 -21.374 28.674 1.00 19.58  ? 143 LEU   C CA  1 
ATOM   2149 C  C   . LEU   B 1 137 ? 17.059 -22.674 29.218 1.00 22.61  ? 143 LEU   C C   1 
ATOM   2150 O  O   . LEU   B 1 137 ? 16.117 -23.179 28.605 1.00 24.77  ? 143 LEU   C O   1 
ATOM   2151 C  CB  . LEU   B 1 137 ? 18.661 -21.715 27.544 1.00 19.32  ? 143 LEU   C CB  1 
ATOM   2152 C  CG  . LEU   B 1 137 ? 19.123 -20.543 26.676 1.00 19.06  ? 143 LEU   C CG  1 
ATOM   2153 C  CD1 . LEU   B 1 137 ? 20.275 -21.001 25.791 1.00 20.04  ? 143 LEU   C CD1 1 
ATOM   2154 C  CD2 . LEU   B 1 137 ? 17.953 -19.969 25.843 1.00 19.42  ? 143 LEU   C CD2 1 
ATOM   2155 N  N   . ASP   B 1 138 ? 17.591 -23.217 30.368 1.00 21.88  ? 144 ASP   C N   1 
ATOM   2156 C  CA  . ASP   B 1 138 ? 17.141 -24.476 30.948 1.00 24.80  ? 144 ASP   C CA  1 
ATOM   2157 C  C   . ASP   B 1 138 ? 15.872 -24.367 31.803 1.00 27.83  ? 144 ASP   C C   1 
ATOM   2158 O  O   . ASP   B 1 138 ? 15.446 -25.388 32.358 1.00 28.62  ? 144 ASP   C O   1 
ATOM   2159 C  CB  . ASP   B 1 138 ? 18.241 -25.117 31.819 1.00 24.77  ? 144 ASP   C CB  1 
ATOM   2160 C  CG  . ASP   B 1 138 ? 19.483 -25.541 31.062 1.00 27.38  ? 144 ASP   C CG  1 
ATOM   2161 O  OD1 . ASP   B 1 138 ? 19.434 -25.599 29.816 1.00 27.11  ? 144 ASP   C OD1 1 
ATOM   2162 O  OD2 . ASP   B 1 138 ? 20.525 -25.800 31.722 1.00 29.59  ? 144 ASP   C OD2 1 
ATOM   2163 N  N   . GLU   B 1 139 ? 15.303 -23.165 31.975 1.00 29.29  ? 145 GLU   C N   1 
ATOM   2164 C  CA  . GLU   B 1 139 ? 14.121 -22.995 32.832 1.00 33.24  ? 145 GLU   C CA  1 
ATOM   2165 C  C   . GLU   B 1 139 ? 13.159 -21.889 32.327 1.00 37.06  ? 145 GLU   C C   1 
ATOM   2166 O  O   . GLU   B 1 139 ? 13.461 -21.226 31.347 1.00 37.42  ? 145 GLU   C O   1 
ATOM   2167 C  CB  . GLU   B 1 139 ? 14.625 -22.665 34.253 1.00 37.05  ? 145 GLU   C CB  1 
ATOM   2168 C  CG  . GLU   B 1 139 ? 15.234 -21.277 34.346 1.00 44.65  ? 145 GLU   C CG  1 
ATOM   2169 C  CD  . GLU   B 1 139 ? 16.556 -21.169 35.076 1.00 54.55  ? 145 GLU   C CD  1 
ATOM   2170 O  OE1 . GLU   B 1 139 ? 16.941 -20.031 35.431 1.00 56.55  ? 145 GLU   C OE1 1 
ATOM   2171 O  OE2 . GLU   B 1 139 ? 17.209 -22.217 35.286 1.00 58.75  ? 145 GLU   C OE2 1 
ATOM   2172 N  N   . GLU   B 1 140 ? 12.022 -21.663 33.034 1.00 39.24  ? 146 GLU   C N   1 
ATOM   2173 C  CA  . GLU   B 1 140 ? 11.092 -20.545 32.775 1.00 41.32  ? 146 GLU   C CA  1 
ATOM   2174 C  C   . GLU   B 1 140 ? 10.746 -20.365 31.289 1.00 43.92  ? 146 GLU   C C   1 
ATOM   2175 O  O   . GLU   B 1 140 ? 9.773  -19.688 30.937 1.00 45.25  ? 146 GLU   C O   1 
ATOM   2176 C  CB  . GLU   B 1 140 ? 11.691 -19.261 33.415 1.00 43.53  ? 146 GLU   C CB  1 
ATOM   2177 C  CG  . GLU   B 1 140 ? 11.515 -17.923 32.706 1.00 48.79  ? 146 GLU   C CG  1 
ATOM   2178 C  CD  . GLU   B 1 140 ? 10.396 -17.045 33.232 1.00 56.21  ? 146 GLU   C CD  1 
ATOM   2179 O  OE1 . GLU   B 1 140 ? 10.600 -15.812 33.318 1.00 57.05  ? 146 GLU   C OE1 1 
ATOM   2180 O  OE2 . GLU   B 1 140 ? 9.315  -17.589 33.556 1.00 59.08  ? 146 GLU   C OE2 1 
HETATM 2181 N  N1  . A1B3N C 2 .   ? 4.197  16.343  21.339 1.00 71.66  ? 201 A1B3N A N1  1 
HETATM 2182 C  C4  . A1B3N C 2 .   ? 5.531  12.414  25.924 1.00 71.95  ? 201 A1B3N A C4  1 
HETATM 2183 C  C5  . A1B3N C 2 .   ? 6.187  13.550  25.473 1.00 71.98  ? 201 A1B3N A C5  1 
HETATM 2184 C  C6  . A1B3N C 2 .   ? 7.224  13.458  24.546 1.00 71.90  ? 201 A1B3N A C6  1 
HETATM 2185 C  C7  . A1B3N C 2 .   ? 7.936  14.675  23.998 1.00 71.89  ? 201 A1B3N A C7  1 
HETATM 2186 C  C8  . A1B3N C 2 .   ? 7.508  15.985  24.623 1.00 71.87  ? 201 A1B3N A C8  1 
HETATM 2187 C  C10 . A1B3N C 2 .   ? 4.376  17.239  25.608 1.00 71.79  ? 201 A1B3N A C10 1 
HETATM 2188 C  C13 . A1B3N C 2 .   ? 3.273  15.904  22.193 1.00 71.74  ? 201 A1B3N A C13 1 
HETATM 2189 C  C15 . A1B3N C 2 .   ? 5.406  15.910  23.284 1.00 71.74  ? 201 A1B3N A C15 1 
HETATM 2190 O  O1  . A1B3N C 2 .   ? 2.107  15.634  21.903 1.00 71.77  ? 201 A1B3N A O1  1 
HETATM 2191 C  C14 . A1B3N C 2 .   ? 5.486  16.633  21.943 1.00 71.60  ? 201 A1B3N A C14 1 
HETATM 2192 C  C12 . A1B3N C 2 .   ? 3.889  15.814  23.576 1.00 71.72  ? 201 A1B3N A C12 1 
HETATM 2193 C  C11 . A1B3N C 2 .   ? 3.368  16.903  24.521 1.00 71.79  ? 201 A1B3N A C11 1 
HETATM 2194 C  C9  . A1B3N C 2 .   ? 5.710  17.637  25.006 1.00 71.73  ? 201 A1B3N A C9  1 
HETATM 2195 N  N   . A1B3N C 2 .   ? 6.302  16.505  24.296 1.00 71.77  ? 201 A1B3N A N   1 
HETATM 2196 O  O   . A1B3N C 2 .   ? 8.280  16.570  25.345 1.00 71.98  ? 201 A1B3N A O   1 
HETATM 2197 C  C1  . A1B3N C 2 .   ? 7.594  12.187  24.104 1.00 71.82  ? 201 A1B3N A C1  1 
HETATM 2198 S  S   . A1B3N C 2 .   ? 8.972  12.154  22.999 1.00 71.89  ? 201 A1B3N A S   1 
HETATM 2199 C  C   . A1B3N C 2 .   ? 9.125  10.419  22.648 1.00 71.49  ? 201 A1B3N A C   1 
HETATM 2200 C  C3  . A1B3N C 2 .   ? 5.882  11.183  25.450 1.00 71.88  ? 201 A1B3N A C3  1 
HETATM 2201 C  C2  . A1B3N C 2 .   ? 6.911  11.054  24.537 1.00 71.80  ? 201 A1B3N A C2  1 
HETATM 2202 ZN ZN  . ZN    D 3 .   ? 10.955 -3.884  5.826  1.00 24.15  2 202 ZN    A ZN  1 
HETATM 2203 S  S   . DMS   E 4 .   ? 18.678 -4.090  25.488 1.00 51.92  ? 201 DMS   C S   1 
HETATM 2204 O  O   . DMS   E 4 .   ? 19.023 -3.016  24.476 1.00 51.87  ? 201 DMS   C O   1 
HETATM 2205 C  C1  . DMS   E 4 .   ? 17.806 -5.441  24.621 1.00 51.77  ? 201 DMS   C C1  1 
HETATM 2206 C  C2  . DMS   E 4 .   ? 20.191 -5.024  25.882 1.00 52.10  ? 201 DMS   C C2  1 
HETATM 2207 ZN ZN  . ZN    F 3 .   ? 30.501 -31.082 26.707 1.00 15.99  2 202 ZN    C ZN  1 
HETATM 2208 S  S   . DMS   G 4 .   ? 21.128 -32.634 10.349 1.00 52.77  ? 203 DMS   C S   1 
HETATM 2209 O  O   . DMS   G 4 .   ? 21.264 -32.243 8.901  1.00 52.70  ? 203 DMS   C O   1 
HETATM 2210 C  C1  . DMS   G 4 .   ? 22.159 -31.497 11.316 1.00 52.80  ? 203 DMS   C C1  1 
HETATM 2211 C  C2  . DMS   G 4 .   ? 19.540 -31.920 10.904 1.00 52.76  ? 203 DMS   C C2  1 
HETATM 2212 S  S   . DMS   H 4 .   ? 28.451 -4.962  5.940  1.00 126.12 ? 204 DMS   C S   1 
HETATM 2213 O  O   . DMS   H 4 .   ? 27.938 -5.249  7.320  1.00 126.10 ? 204 DMS   C O   1 
HETATM 2214 C  C1  . DMS   H 4 .   ? 28.724 -3.173  5.822  1.00 126.13 ? 204 DMS   C C1  1 
HETATM 2215 C  C2  . DMS   H 4 .   ? 30.208 -5.413  5.895  1.00 126.09 ? 204 DMS   C C2  1 
HETATM 2216 O  O   . HOH   I 5 .   ? 14.631 13.718  23.995 1.00 30.00  ? 301 HOH   A O   1 
HETATM 2217 O  O   . HOH   I 5 .   ? 11.902 14.790  23.681 1.00 30.00  ? 302 HOH   A O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.2621 0.2487 0.2335 -0.0246 -0.0096 -0.0128 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2558 0.2456 0.2340 -0.0219 -0.0142 -0.0092 7   SER   A CA  
3    C C   . SER   A 1   ? 0.2447 0.2379 0.2323 -0.0150 -0.0177 -0.0036 7   SER   A C   
4    O O   . SER   A 1   ? 0.2459 0.2396 0.2329 -0.0138 -0.0180 -0.0018 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2868 0.2813 0.2588 -0.0302 -0.0196 -0.0065 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.3305 0.3302 0.3004 -0.0327 -0.0251 -0.0002 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.2178 0.2130 0.2137 -0.0115 -0.0195 -0.0016 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1992 0.1965 0.2042 -0.0064 -0.0210 0.0023  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1802 0.1769 0.1921 -0.0026 -0.0190 0.0009  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.2055 0.1997 0.2158 -0.0024 -0.0163 -0.0025 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1691 0.1678 0.1895 0.0000  -0.0197 0.0036  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1725 0.1710 0.1985 0.0021  -0.0174 0.0020  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1763 0.1746 0.2087 0.0042  -0.0147 0.0025  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1901 0.1883 0.2252 0.0048  -0.0150 0.0050  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1876 0.1890 0.2185 0.0007  -0.0200 0.0035  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1599 0.1577 0.1943 0.0044  -0.0115 0.0001  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1678 0.1647 0.2076 0.0044  -0.0072 -0.0011 10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1674 0.1657 0.2168 0.0046  -0.0062 -0.0009 10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1693 0.1690 0.2174 0.0038  -0.0075 -0.0017 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1583 0.1551 0.1923 0.0020  -0.0040 -0.0041 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1926 0.1899 0.2194 0.0020  -0.0054 -0.0034 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1863 0.1815 0.2239 -0.0004 0.0019  -0.0068 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.2077 0.2078 0.2303 -0.0009 -0.0043 -0.0037 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1651 0.1629 0.2257 0.0059  -0.0034 0.0006  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1796 0.1791 0.2525 0.0064  -0.0013 0.0011  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1892 0.1849 0.2671 0.0048  0.0078  -0.0039 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1942 0.1868 0.2800 0.0058  0.0124  -0.0034 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1901 0.1932 0.2759 0.0090  -0.0049 0.0082  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1801 0.1878 0.2590 0.0079  -0.0133 0.0121  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1866 0.1983 0.2660 0.0063  -0.0163 0.0125  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1985 0.2062 0.2695 0.0071  -0.0174 0.0149  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.2011 0.2161 0.2721 0.0032  -0.0228 0.0147  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.2114 0.2226 0.2739 0.0039  -0.0237 0.0171  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.2238 0.2384 0.2861 0.0017  -0.0261 0.0167  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2583 0.2757 0.3110 -0.0032 -0.0311 0.0177  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1875 0.1830 0.2599 0.0011  0.0110  -0.0087 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.2041 0.1962 0.2777 -0.0032 0.0202  -0.0146 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.2073 0.2009 0.2883 -0.0047 0.0236  -0.0168 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.2032 0.2001 0.2786 -0.0054 0.0188  -0.0159 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.2264 0.2182 0.2835 -0.0089 0.0208  -0.0179 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.2291 0.2250 0.2766 -0.0096 0.0140  -0.0157 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2432 0.2323 0.2985 -0.0164 0.0306  -0.0247 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.2169 0.2078 0.3123 -0.0049 0.0324  -0.0195 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.2198 0.2123 0.3242 -0.0064 0.0369  -0.0220 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.2024 0.2012 0.3133 -0.0018 0.0281  -0.0155 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.2088 0.2103 0.3270 0.0031  0.0222  -0.0088 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1988 0.2003 0.3038 -0.0047 0.0262  -0.0173 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1940 0.2011 0.3019 -0.0021 0.0180  -0.0121 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1827 0.1900 0.2730 -0.0031 0.0102  -0.0110 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1900 0.1999 0.2775 -0.0040 0.0061  -0.0100 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.2096 0.2199 0.3277 -0.0037 0.0217  -0.0139 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.2473 0.2597 0.3895 -0.0005 0.0275  -0.0119 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2898 0.3086 0.4455 0.0035  0.0220  -0.0044 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.2235 0.2307 0.3722 -0.0026 0.0392  -0.0180 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1715 0.1760 0.2517 -0.0028 0.0086  -0.0108 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1667 0.1707 0.2331 -0.0031 0.0027  -0.0095 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1582 0.1622 0.2228 0.0001  -0.0022 -0.0058 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1765 0.1795 0.2455 0.0018  -0.0005 -0.0049 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1938 0.1957 0.2489 -0.0070 0.0052  -0.0121 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.2039 0.2062 0.2570 -0.0124 0.0096  -0.0155 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.2188 0.2225 0.2714 -0.0135 0.0076  -0.0149 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.2285 0.2296 0.2794 -0.0177 0.0166  -0.0197 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.2390 0.2433 0.2889 -0.0194 0.0116  -0.0176 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2545 0.2564 0.3014 -0.0247 0.0209  -0.0231 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2632 0.2668 0.3096 -0.0253 0.0180  -0.0216 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.3207 0.3253 0.3626 -0.0329 0.0222  -0.0247 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1583 0.1626 0.2154 0.0001  -0.0072 -0.0044 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1609 0.1647 0.2129 0.0014  -0.0111 -0.0021 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1581 0.1588 0.1998 0.0008  -0.0110 -0.0037 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1641 0.1638 0.2032 -0.0004 -0.0112 -0.0045 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1709 0.1779 0.2244 0.0003  -0.0160 0.0006  16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1967 0.2026 0.2412 -0.0010 -0.0193 0.0014  16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.2059 0.2165 0.2506 -0.0046 -0.0242 0.0043  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.2185 0.2260 0.2513 -0.0086 -0.0247 0.0016  16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.2457 0.2527 0.2710 -0.0112 -0.0263 0.0020  16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.2309 0.2406 0.2590 -0.0098 -0.0284 0.0061  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.2439 0.2469 0.2589 -0.0156 -0.0246 -0.0020 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1555 0.1549 0.1932 0.0016  -0.0101 -0.0036 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1667 0.1647 0.1982 0.0015  -0.0099 -0.0036 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1739 0.1701 0.2016 0.0025  -0.0115 -0.0032 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1651 0.1617 0.1921 0.0031  -0.0122 -0.0026 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1726 0.1718 0.2022 0.0004  -0.0076 -0.0035 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1894 0.1895 0.2158 0.0003  -0.0081 -0.0014 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1810 0.1815 0.2128 -0.0027 -0.0045 -0.0054 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1624 0.1562 0.1880 0.0022  -0.0111 -0.0039 18  VAL   A N   
86   C CA  A VAL   A 12  ? 0.1634 0.1545 0.1847 0.0016  -0.0108 -0.0051 18  VAL   A CA  
87   C CA  B VAL   A 12  ? 0.1906 0.1818 0.2118 0.0016  -0.0108 -0.0051 18  VAL   A CA  
88   C C   . VAL   A 12  ? 0.1686 0.1567 0.1907 0.0029  -0.0074 -0.0053 18  VAL   A C   
89   O O   . VAL   A 12  ? 0.1691 0.1576 0.1953 0.0040  -0.0065 -0.0032 18  VAL   A O   
90   C CB  A VAL   A 12  ? 0.1467 0.1368 0.1651 -0.0019 -0.0122 -0.0068 18  VAL   A CB  
91   C CB  B VAL   A 12  ? 0.2314 0.2220 0.2502 -0.0018 -0.0125 -0.0065 18  VAL   A CB  
92   C CG1 A VAL   A 12  ? 0.1642 0.1589 0.1839 -0.0032 -0.0163 -0.0044 18  VAL   A CG1 
93   C CG1 B VAL   A 12  ? 0.2591 0.2471 0.2708 -0.0050 -0.0116 -0.0087 18  VAL   A CG1 
94   C CG2 A VAL   A 12  ? 0.1094 0.0976 0.1298 -0.0029 -0.0110 -0.0079 18  VAL   A CG2 
95   C CG2 B VAL   A 12  ? 0.2508 0.2463 0.2734 -0.0024 -0.0163 -0.0041 18  VAL   A CG2 
96   N N   . ASN   A 13  ? 0.1697 0.1548 0.1888 0.0024  -0.0050 -0.0072 19  ASN   A N   
97   C CA  . ASN   A 13  ? 0.1674 0.1489 0.1909 0.0039  -0.0002 -0.0074 19  ASN   A CA  
98   C C   . ASN   A 13  ? 0.1839 0.1605 0.2086 0.0023  0.0021  -0.0094 19  ASN   A C   
99   O O   . ASN   A 13  ? 0.1941 0.1689 0.2127 -0.0019 0.0014  -0.0129 19  ASN   A O   
100  C CB  . ASN   A 13  ? 0.1713 0.1493 0.1913 0.0025  0.0037  -0.0108 19  ASN   A CB  
101  C CG  . ASN   A 13  ? 0.1794 0.1616 0.1979 0.0037  0.0019  -0.0092 19  ASN   A CG  
102  O OD1 . ASN   A 13  ? 0.1898 0.1737 0.2017 0.0015  -0.0014 -0.0097 19  ASN   A OD1 
103  N ND2 . ASN   A 13  ? 0.1935 0.1780 0.2190 0.0070  0.0039  -0.0062 19  ASN   A ND2 
104  N N   . ARG   A 14  ? 0.1781 0.1534 0.2108 0.0048  0.0044  -0.0063 20  ARG   A N   
105  C CA  . ARG   A 14  ? 0.1713 0.1409 0.2059 0.0032  0.0073  -0.0080 20  ARG   A CA  
106  C C   . ARG   A 14  ? 0.2060 0.1677 0.2364 -0.0006 0.0134  -0.0147 20  ARG   A C   
107  O O   . ARG   A 14  ? 0.2218 0.1803 0.2469 -0.0052 0.0139  -0.0186 20  ARG   A O   
108  C CB  . ARG   A 14  ? 0.1892 0.1584 0.2351 0.0067  0.0093  -0.0021 20  ARG   A CB  
109  C CG  . ARG   A 14  ? 0.1899 0.1529 0.2388 0.0052  0.0123  -0.0029 20  ARG   A CG  
110  C CD  . ARG   A 14  ? 0.2082 0.1708 0.2706 0.0089  0.0145  0.0048  20  ARG   A CD  
111  N NE  . ARG   A 14  ? 0.1968 0.1540 0.2628 0.0076  0.0167  0.0056  20  ARG   A NE  
112  C CZ  . ARG   A 14  ? 0.2494 0.1961 0.3204 0.0072  0.0247  0.0021  20  ARG   A CZ  
113  N NH1 . ARG   A 14  ? 0.2569 0.1972 0.3276 0.0066  0.0315  -0.0042 20  ARG   A NH1 
114  N NH2 . ARG   A 14  ? 0.2697 0.2114 0.3449 0.0061  0.0266  0.0037  20  ARG   A NH2 
115  N N   . HIS   A 15  ? 0.2034 0.1628 0.2351 0.0002  0.0179  -0.0165 21  HIS   A N   
116  C CA  . HIS   A 15  ? 0.2216 0.1726 0.2485 -0.0050 0.0257  -0.0241 21  HIS   A CA  
117  C C   . HIS   A 15  ? 0.2310 0.1837 0.2425 -0.0128 0.0221  -0.0288 21  HIS   A C   
118  O O   . HIS   A 15  ? 0.2643 0.2108 0.2683 -0.0201 0.0279  -0.0357 21  HIS   A O   
119  C CB  . HIS   A 15  ? 0.2429 0.1902 0.2771 -0.0025 0.0334  -0.0252 21  HIS   A CB  
120  C CG  . HIS   A 15  ? 0.2401 0.1931 0.2688 -0.0026 0.0303  -0.0250 21  HIS   A CG  
121  N ND1 . HIS   A 15  ? 0.2358 0.1968 0.2700 0.0029  0.0248  -0.0181 21  HIS   A ND1 
122  C CD2 . HIS   A 15  ? 0.2452 0.1963 0.2630 -0.0084 0.0327  -0.0308 21  HIS   A CD2 
123  C CE1 . HIS   A 15  ? 0.2570 0.2203 0.2844 0.0011  0.0242  -0.0201 21  HIS   A CE1 
124  N NE2 . HIS   A 15  ? 0.2573 0.2149 0.2750 -0.0056 0.0287  -0.0274 21  HIS   A NE2 
125  N N   . LEU   A 16  ? 0.2229 0.1843 0.2303 -0.0121 0.0132  -0.0248 22  LEU   A N   
126  C CA  . LEU   A 16  ? 0.2232 0.1888 0.2193 -0.0189 0.0080  -0.0260 22  LEU   A CA  
127  C C   . LEU   A 16  ? 0.2448 0.2156 0.2411 -0.0202 0.0016  -0.0232 22  LEU   A C   
128  O O   . LEU   A 16  ? 0.2651 0.2417 0.2557 -0.0250 -0.0040 -0.0217 22  LEU   A O   
129  C CB  . LEU   A 16  ? 0.2261 0.1973 0.2199 -0.0174 0.0037  -0.0229 22  LEU   A CB  
130  C CG  . LEU   A 16  ? 0.2406 0.2076 0.2331 -0.0175 0.0100  -0.0262 22  LEU   A CG  
131  C CD1 . LEU   A 16  ? 0.2467 0.2194 0.2368 -0.0160 0.0054  -0.0227 22  LEU   A CD1 
132  C CD2 . LEU   A 16  ? 0.2660 0.2269 0.2481 -0.0272 0.0164  -0.0338 22  LEU   A CD2 
133  N N   . ALA   A 17  ? 0.2246 0.1941 0.2285 -0.0162 0.0022  -0.0217 23  ALA   A N   
134  C CA  . ALA   A 17  ? 0.2244 0.1985 0.2296 -0.0173 -0.0026 -0.0196 23  ALA   A CA  
135  C C   . ALA   A 17  ? 0.2462 0.2198 0.2434 -0.0263 -0.0027 -0.0232 23  ALA   A C   
136  O O   . ALA   A 17  ? 0.2661 0.2320 0.2583 -0.0311 0.0038  -0.0289 23  ALA   A O   
137  C CB  . ALA   A 17  ? 0.2179 0.1898 0.2314 -0.0127 -0.0008 -0.0177 23  ALA   A CB  
138  N N   . THR   A 18  ? 0.2252 0.2075 0.2223 -0.0290 -0.0097 -0.0198 24  THR   A N   
139  C CA  . THR   A 18  ? 0.2172 0.2023 0.2068 -0.0389 -0.0118 -0.0215 24  THR   A CA  
140  C C   . THR   A 18  ? 0.2325 0.2161 0.2256 -0.0398 -0.0105 -0.0229 24  THR   A C   
141  O O   . THR   A 18  ? 0.2170 0.1985 0.2186 -0.0326 -0.0091 -0.0214 24  THR   A O   
142  C CB  . THR   A 18  ? 0.2497 0.2471 0.2408 -0.0413 -0.0207 -0.0147 24  THR   A CB  
143  O OG1 . THR   A 18  ? 0.2465 0.2491 0.2502 -0.0343 -0.0240 -0.0099 24  THR   A OG1 
144  C CG2 . THR   A 18  ? 0.2535 0.2530 0.2417 -0.0404 -0.0227 -0.0122 24  THR   A CG2 
145  N N   . HIS   A 19  ? 0.2369 0.2225 0.2229 -0.0497 -0.0114 -0.0252 25  HIS   A N   
146  C CA  . HIS   A 19  ? 0.2394 0.2247 0.2288 -0.0511 -0.0108 -0.0261 25  HIS   A CA  
147  C C   . HIS   A 19  ? 0.2232 0.2179 0.2245 -0.0449 -0.0171 -0.0194 25  HIS   A C   
148  O O   . HIS   A 19  ? 0.2271 0.2189 0.2344 -0.0407 -0.0148 -0.0198 25  HIS   A O   
149  C CB  . HIS   A 19  ? 0.2731 0.2611 0.2521 -0.0644 -0.0117 -0.0292 25  HIS   A CB  
150  C CG  . HIS   A 19  ? 0.3367 0.3280 0.3203 -0.0663 -0.0132 -0.0285 25  HIS   A CG  
151  N ND1 . HIS   A 19  ? 0.3740 0.3545 0.3595 -0.0642 -0.0062 -0.0330 25  HIS   A ND1 
152  C CD2 . HIS   A 19  ? 0.3641 0.3686 0.3529 -0.0692 -0.0210 -0.0229 25  HIS   A CD2 
153  C CE1 . HIS   A 19  ? 0.3842 0.3711 0.3731 -0.0671 -0.0096 -0.0312 25  HIS   A CE1 
154  N NE2 . HIS   A 19  ? 0.3887 0.3905 0.3808 -0.0696 -0.0184 -0.0251 25  HIS   A NE2 
155  N N   . ASN   A 20  ? 0.2171 0.2226 0.2228 -0.0440 -0.0239 -0.0133 26  ASN   A N   
156  C CA  . ASN   A 20  ? 0.2077 0.2210 0.2270 -0.0381 -0.0277 -0.0077 26  ASN   A CA  
157  C C   . ASN   A 20  ? 0.2025 0.2097 0.2276 -0.0288 -0.0235 -0.0086 26  ASN   A C   
158  O O   . ASN   A 20  ? 0.2124 0.2207 0.2451 -0.0258 -0.0225 -0.0081 26  ASN   A O   
159  C CB  . ASN   A 20  ? 0.2269 0.2514 0.2525 -0.0384 -0.0345 -0.0003 26  ASN   A CB  
160  C CG  . ASN   A 20  ? 0.3139 0.3461 0.3563 -0.0330 -0.0366 0.0049  26  ASN   A CG  
161  O OD1 . ASN   A 20  ? 0.3647 0.4033 0.4132 -0.0360 -0.0385 0.0066  26  ASN   A OD1 
162  N ND2 . ASN   A 20  ? 0.3195 0.3509 0.3702 -0.0253 -0.0352 0.0071  26  ASN   A ND2 
163  N N   . ASP   A 21  ? 0.2024 0.2035 0.2231 -0.0255 -0.0208 -0.0101 27  ASP   A N   
164  C CA  . ASP   A 21  ? 0.2003 0.1969 0.2252 -0.0185 -0.0173 -0.0103 27  ASP   A CA  
165  C C   . ASP   A 21  ? 0.1810 0.1717 0.2061 -0.0185 -0.0133 -0.0127 27  ASP   A C   
166  O O   . ASP   A 21  ? 0.1943 0.1860 0.2247 -0.0155 -0.0127 -0.0113 27  ASP   A O   
167  C CB  . ASP   A 21  ? 0.1934 0.1852 0.2142 -0.0157 -0.0150 -0.0111 27  ASP   A CB  
168  C CG  . ASP   A 21  ? 0.2095 0.2062 0.2309 -0.0146 -0.0184 -0.0081 27  ASP   A CG  
169  O OD1 . ASP   A 21  ? 0.1985 0.2012 0.2278 -0.0123 -0.0212 -0.0045 27  ASP   A OD1 
170  O OD2 . ASP   A 21  ? 0.1978 0.1920 0.2125 -0.0163 -0.0177 -0.0094 27  ASP   A OD2 
171  N N   . TRP   A 22  ? 0.1836 0.1675 0.2027 -0.0224 -0.0099 -0.0163 28  TRP   A N   
172  C CA  . TRP   A 22  ? 0.1797 0.1570 0.2002 -0.0224 -0.0056 -0.0178 28  TRP   A CA  
173  C C   . TRP   A 22  ? 0.1888 0.1704 0.2121 -0.0253 -0.0077 -0.0174 28  TRP   A C   
174  O O   . TRP   A 22  ? 0.2091 0.1882 0.2359 -0.0235 -0.0058 -0.0164 28  TRP   A O   
175  C CB  . TRP   A 22  ? 0.1973 0.1649 0.2119 -0.0267 0.0002  -0.0227 28  TRP   A CB  
176  C CG  . TRP   A 22  ? 0.1949 0.1560 0.2110 -0.0225 0.0049  -0.0228 28  TRP   A CG  
177  C CD1 . TRP   A 22  ? 0.2223 0.1815 0.2334 -0.0242 0.0070  -0.0256 28  TRP   A CD1 
178  C CD2 . TRP   A 22  ? 0.2053 0.1622 0.2295 -0.0164 0.0081  -0.0193 28  TRP   A CD2 
179  N NE1 . TRP   A 22  ? 0.2191 0.1723 0.2358 -0.0190 0.0122  -0.0248 28  TRP   A NE1 
180  C CE2 . TRP   A 22  ? 0.2082 0.1609 0.2338 -0.0140 0.0123  -0.0200 28  TRP   A CE2 
181  C CE3 . TRP   A 22  ? 0.2218 0.1787 0.2525 -0.0138 0.0078  -0.0149 28  TRP   A CE3 
182  C CZ2 . TRP   A 22  ? 0.2309 0.1807 0.2664 -0.0083 0.0155  -0.0154 28  TRP   A CZ2 
183  C CZ3 . TRP   A 22  ? 0.2302 0.1847 0.2687 -0.0089 0.0101  -0.0099 28  TRP   A CZ3 
184  C CH2 . TRP   A 22  ? 0.2298 0.1805 0.2719 -0.0061 0.0142  -0.0099 28  TRP   A CH2 
185  N N   . ALA   A 23  ? 0.1890 0.1784 0.2119 -0.0297 -0.0120 -0.0171 29  ALA   A N   
186  C CA  . ALA   A 23  ? 0.1910 0.1860 0.2184 -0.0325 -0.0139 -0.0163 29  ALA   A CA  
187  C C   . ALA   A 23  ? 0.2020 0.2036 0.2395 -0.0274 -0.0154 -0.0129 29  ALA   A C   
188  O O   . ALA   A 23  ? 0.2268 0.2322 0.2696 -0.0288 -0.0154 -0.0127 29  ALA   A O   
189  C CB  . ALA   A 23  ? 0.2119 0.2145 0.2367 -0.0398 -0.0181 -0.0160 29  ALA   A CB  
190  N N   . ASN   A 24  ? 0.1904 0.1930 0.2305 -0.0223 -0.0158 -0.0110 30  ASN   A N   
191  C CA  . ASN   A 24  ? 0.1906 0.1974 0.2393 -0.0186 -0.0152 -0.0092 30  ASN   A CA  
192  C C   . ASN   A 24  ? 0.1961 0.1975 0.2414 -0.0151 -0.0122 -0.0095 30  ASN   A C   
193  O O   . ASN   A 24  ? 0.1891 0.1926 0.2377 -0.0123 -0.0117 -0.0085 30  ASN   A O   
194  C CB  . ASN   A 24  ? 0.1872 0.2017 0.2435 -0.0171 -0.0184 -0.0059 30  ASN   A CB  
195  C CG  . ASN   A 24  ? 0.2307 0.2536 0.2932 -0.0212 -0.0222 -0.0035 30  ASN   A CG  
196  O OD1 . ASN   A 24  ? 0.2587 0.2864 0.3309 -0.0214 -0.0211 -0.0029 30  ASN   A OD1 
197  N ND2 . ASN   A 24  ? 0.2349 0.2603 0.2913 -0.0258 -0.0264 -0.0021 30  ASN   A ND2 
198  N N   . LEU   A 25  ? 0.1936 0.1885 0.2335 -0.0156 -0.0102 -0.0102 31  LEU   A N   
199  C CA  . LEU   A 25  ? 0.1857 0.1771 0.2233 -0.0130 -0.0085 -0.0085 31  LEU   A CA  
200  C C   . LEU   A 25  ? 0.2060 0.2002 0.2454 -0.0137 -0.0072 -0.0074 31  LEU   A C   
201  O O   . LEU   A 25  ? 0.2264 0.2215 0.2669 -0.0167 -0.0061 -0.0080 31  LEU   A O   
202  C CB  . LEU   A 25  ? 0.1931 0.1772 0.2281 -0.0135 -0.0064 -0.0082 31  LEU   A CB  
203  C CG  . LEU   A 25  ? 0.2032 0.1850 0.2389 -0.0108 -0.0051 -0.0043 31  LEU   A CG  
204  C CD1 . LEU   A 25  ? 0.2082 0.1903 0.2429 -0.0077 -0.0055 -0.0043 31  LEU   A CD1 
205  C CD2 . LEU   A 25  ? 0.2302 0.2047 0.2678 -0.0109 -0.0021 -0.0027 31  LEU   A CD2 
206  N N   . VAL   A 26  ? 0.1864 0.1820 0.2248 -0.0122 -0.0069 -0.0060 32  VAL   A N   
207  C CA  . VAL   A 26  ? 0.1902 0.1885 0.2275 -0.0151 -0.0051 -0.0053 32  VAL   A CA  
208  C C   . VAL   A 26  ? 0.1978 0.1949 0.2315 -0.0156 -0.0060 -0.0004 32  VAL   A C   
209  O O   . VAL   A 26  ? 0.2247 0.2231 0.2566 -0.0197 -0.0058 0.0023  32  VAL   A O   
210  C CB  . VAL   A 26  ? 0.1909 0.1920 0.2296 -0.0147 -0.0035 -0.0073 32  VAL   A CB  
211  C CG1 . VAL   A 26  ? 0.2050 0.2085 0.2396 -0.0200 -0.0007 -0.0074 32  VAL   A CG1 
212  C CG2 . VAL   A 26  ? 0.2101 0.2133 0.2567 -0.0138 -0.0023 -0.0101 32  VAL   A CG2 
213  N N   . TRP   A 27  ? 0.1952 0.1907 0.2290 -0.0119 -0.0071 0.0017  33  TRP   A N   
214  C CA  . TRP   A 27  ? 0.1975 0.1936 0.2318 -0.0117 -0.0080 0.0078  33  TRP   A CA  
215  C C   . TRP   A 27  ? 0.1992 0.1917 0.2363 -0.0067 -0.0077 0.0083  33  TRP   A C   
216  O O   . TRP   A 27  ? 0.1910 0.1829 0.2265 -0.0047 -0.0076 0.0044  33  TRP   A O   
217  C CB  . TRP   A 27  ? 0.2040 0.2065 0.2345 -0.0154 -0.0086 0.0097  33  TRP   A CB  
218  C CG  . TRP   A 27  ? 0.2172 0.2237 0.2490 -0.0158 -0.0107 0.0173  33  TRP   A CG  
219  C CD1 . TRP   A 27  ? 0.2364 0.2466 0.2697 -0.0193 -0.0127 0.0252  33  TRP   A CD1 
220  C CD2 . TRP   A 27  ? 0.2121 0.2206 0.2451 -0.0130 -0.0115 0.0189  33  TRP   A CD2 
221  N NE1 . TRP   A 27  ? 0.2594 0.2750 0.2960 -0.0188 -0.0150 0.0324  33  TRP   A NE1 
222  C CE2 . TRP   A 27  ? 0.2343 0.2487 0.2704 -0.0150 -0.0140 0.0281  33  TRP   A CE2 
223  C CE3 . TRP   A 27  ? 0.2179 0.2244 0.2501 -0.0094 -0.0105 0.0142  33  TRP   A CE3 
224  C CZ2 . TRP   A 27  ? 0.2425 0.2614 0.2814 -0.0133 -0.0153 0.0322  33  TRP   A CZ2 
225  C CZ3 . TRP   A 27  ? 0.2276 0.2375 0.2609 -0.0081 -0.0114 0.0175  33  TRP   A CZ3 
226  C CH2 . TRP   A 27  ? 0.2419 0.2578 0.2792 -0.0096 -0.0136 0.0262  33  TRP   A CH2 
227  N N   . GLU   A 28  ? 0.1947 0.1850 0.2369 -0.0050 -0.0070 0.0135  34  GLU   A N   
228  C CA  . GLU   A 28  ? 0.1941 0.1808 0.2405 -0.0007 -0.0050 0.0138  34  GLU   A CA  
229  C C   . GLU   A 28  ? 0.2037 0.1928 0.2587 0.0009  -0.0050 0.0227  34  GLU   A C   
230  O O   . GLU   A 28  ? 0.2062 0.1968 0.2651 -0.0010 -0.0061 0.0290  34  GLU   A O   
231  C CB  . GLU   A 28  ? 0.2101 0.1880 0.2569 0.0002  -0.0012 0.0083  34  GLU   A CB  
232  C CG  . GLU   A 28  ? 0.2377 0.2104 0.2881 -0.0011 0.0009  0.0098  34  GLU   A CG  
233  C CD  . GLU   A 28  ? 0.2453 0.2134 0.3069 0.0017  0.0047  0.0160  34  GLU   A CD  
234  O OE1 . GLU   A 28  ? 0.2386 0.2049 0.3048 0.0005  0.0051  0.0206  34  GLU   A OE1 
235  O OE2 . GLU   A 28  ? 0.2290 0.1954 0.2964 0.0051  0.0076  0.0169  34  GLU   A OE2 
236  N N   . ASP   A 29  ? 0.1982 0.1880 0.2576 0.0042  -0.0039 0.0242  35  ASP   A N   
237  C CA  . ASP   A 29  ? 0.1959 0.1896 0.2671 0.0064  -0.0039 0.0341  35  ASP   A CA  
238  C C   . ASP   A 29  ? 0.1991 0.1879 0.2777 0.0113  0.0011  0.0320  35  ASP   A C   
239  O O   . ASP   A 29  ? 0.1914 0.1827 0.2657 0.0119  0.0008  0.0286  35  ASP   A O   
240  C CB  . ASP   A 29  ? 0.2055 0.2113 0.2734 0.0025  -0.0095 0.0404  35  ASP   A CB  
241  C CG  . ASP   A 29  ? 0.2723 0.2859 0.3528 0.0033  -0.0115 0.0529  35  ASP   A CG  
242  O OD1 . ASP   A 29  ? 0.3006 0.3107 0.3941 0.0089  -0.0076 0.0555  35  ASP   A OD1 
243  O OD2 . ASP   A 29  ? 0.2847 0.3087 0.3626 -0.0025 -0.0168 0.0604  35  ASP   A OD2 
244  N N   . SER   A 30  ? 0.2037 0.1848 0.2939 0.0144  0.0070  0.0335  36  SER   A N   
245  C CA  A SER   A 30  ? 0.2079 0.1825 0.3061 0.0181  0.0143  0.0302  36  SER   A CA  
246  C CA  B SER   A 30  ? 0.2172 0.1918 0.3150 0.0181  0.0142  0.0300  36  SER   A CA  
247  C C   . SER   A 30  ? 0.2059 0.1891 0.3150 0.0212  0.0132  0.0382  36  SER   A C   
248  O O   . SER   A 30  ? 0.2153 0.1970 0.3236 0.0227  0.0166  0.0332  36  SER   A O   
249  C CB  A SER   A 30  ? 0.2160 0.1795 0.3260 0.0200  0.0224  0.0300  36  SER   A CB  
250  C CB  B SER   A 30  ? 0.2534 0.2164 0.3621 0.0198  0.0226  0.0290  36  SER   A CB  
251  O OG  A SER   A 30  ? 0.2207 0.1784 0.3432 0.0238  0.0311  0.0287  36  SER   A OG  
252  O OG  B SER   A 30  ? 0.3127 0.2787 0.4359 0.0217  0.0212  0.0410  36  SER   A OG  
253  N N   . SER   A 31  ? 0.2089 0.2024 0.3269 0.0210  0.0077  0.0508  37  SER   A N   
254  C CA  . SER   A 31  ? 0.2026 0.2068 0.3316 0.0229  0.0056  0.0599  37  SER   A CA  
255  C C   . SER   A 31  ? 0.1985 0.2092 0.3134 0.0201  0.0016  0.0547  37  SER   A C   
256  O O   . SER   A 31  ? 0.2101 0.2264 0.3323 0.0221  0.0023  0.0579  37  SER   A O   
257  C CB  . SER   A 31  ? 0.2318 0.2481 0.3715 0.0210  -0.0009 0.0758  37  SER   A CB  
258  O OG  . SER   A 31  ? 0.3118 0.3368 0.4351 0.0137  -0.0091 0.0766  37  SER   A OG  
259  N N   . ARG   A 32  ? 0.1805 0.1900 0.2768 0.0158  -0.0017 0.0468  38  ARG   A N   
260  C CA  . ARG   A 32  ? 0.1768 0.1905 0.2600 0.0130  -0.0045 0.0414  38  ARG   A CA  
261  C C   . ARG   A 32  ? 0.1874 0.1917 0.2614 0.0143  -0.0005 0.0296  38  ARG   A C   
262  O O   . ARG   A 32  ? 0.1857 0.1924 0.2507 0.0127  -0.0023 0.0256  38  ARG   A O   
263  C CB  . ARG   A 32  ? 0.1899 0.2087 0.2603 0.0067  -0.0099 0.0409  38  ARG   A CB  
264  C CG  . ARG   A 32  ? 0.2156 0.2459 0.2902 0.0022  -0.0150 0.0525  38  ARG   A CG  
265  C CD  . ARG   A 32  ? 0.1996 0.2340 0.2602 -0.0058 -0.0185 0.0503  38  ARG   A CD  
266  N NE  . ARG   A 32  ? 0.1724 0.2090 0.2221 -0.0091 -0.0186 0.0440  38  ARG   A NE  
267  C CZ  . ARG   A 32  ? 0.1990 0.2421 0.2384 -0.0175 -0.0206 0.0437  38  ARG   A CZ  
268  N NH1 . ARG   A 32  ? 0.2365 0.2860 0.2737 -0.0245 -0.0236 0.0499  38  ARG   A NH1 
269  N NH2 . ARG   A 32  ? 0.1936 0.2369 0.2247 -0.0201 -0.0192 0.0375  38  ARG   A NH2 
270  N N   . ASP   A 33  ? 0.1794 0.1734 0.2552 0.0161  0.0046  0.0243  39  ASP   A N   
271  C CA  . ASP   A 33  ? 0.1768 0.1630 0.2422 0.0150  0.0075  0.0140  39  ASP   A CA  
272  C C   . ASP   A 33  ? 0.1700 0.1584 0.2221 0.0115  0.0022  0.0101  39  ASP   A C   
273  O O   . ASP   A 33  ? 0.1835 0.1706 0.2276 0.0104  0.0020  0.0049  39  ASP   A O   
274  C CB  . ASP   A 33  ? 0.1819 0.1671 0.2478 0.0162  0.0112  0.0108  39  ASP   A CB  
275  C CG  . ASP   A 33  ? 0.1809 0.1588 0.2355 0.0133  0.0139  0.0012  39  ASP   A CG  
276  O OD1 . ASP   A 33  ? 0.2006 0.1714 0.2528 0.0113  0.0168  -0.0031 39  ASP   A OD1 
277  O OD2 . ASP   A 33  ? 0.2084 0.1880 0.2563 0.0122  0.0131  -0.0015 39  ASP   A OD2 
278  N N   . LEU   A 34  ? 0.1766 0.1680 0.2275 0.0096  -0.0012 0.0128  40  LEU   A N   
279  C CA  . LEU   A 34  ? 0.1707 0.1638 0.2124 0.0067  -0.0044 0.0091  40  LEU   A CA  
280  C C   . LEU   A 34  ? 0.1676 0.1569 0.2077 0.0051  -0.0044 0.0067  40  LEU   A C   
281  O O   . LEU   A 34  ? 0.1675 0.1552 0.2127 0.0051  -0.0034 0.0099  40  LEU   A O   
282  C CB  . LEU   A 34  ? 0.1775 0.1785 0.2175 0.0041  -0.0077 0.0132  40  LEU   A CB  
283  C CG  . LEU   A 34  ? 0.1746 0.1805 0.2130 0.0039  -0.0084 0.0144  40  LEU   A CG  
284  C CD1 . LEU   A 34  ? 0.1925 0.2060 0.2271 -0.0013 -0.0108 0.0172  40  LEU   A CD1 
285  C CD2 . LEU   A 34  ? 0.2039 0.2063 0.2366 0.0047  -0.0077 0.0081  40  LEU   A CD2 
286  N N   . LEU   A 35  ? 0.1479 0.1368 0.1823 0.0034  -0.0058 0.0020  41  LEU   A N   
287  C CA  . LEU   A 35  ? 0.1514 0.1389 0.1848 0.0013  -0.0063 0.0000  41  LEU   A CA  
288  C C   . LEU   A 35  ? 0.1526 0.1441 0.1838 0.0000  -0.0084 -0.0018 41  LEU   A C   
289  O O   . LEU   A 35  ? 0.1691 0.1617 0.1987 0.0008  -0.0093 -0.0029 41  LEU   A O   
290  C CB  . LEU   A 35  ? 0.1666 0.1481 0.1982 0.0003  -0.0043 -0.0040 41  LEU   A CB  
291  C CG  . LEU   A 35  ? 0.1778 0.1584 0.2085 -0.0027 -0.0049 -0.0060 41  LEU   A CG  
292  C CD1 . LEU   A 35  ? 0.2056 0.1789 0.2359 -0.0046 -0.0010 -0.0088 41  LEU   A CD1 
293  C CD2 . LEU   A 35  ? 0.1895 0.1744 0.2176 -0.0047 -0.0082 -0.0080 41  LEU   A CD2 
294  N N   . VAL   A 36  ? 0.1574 0.1508 0.1897 -0.0022 -0.0087 -0.0018 42  VAL   A N   
295  C CA  . VAL   A 36  ? 0.1508 0.1473 0.1844 -0.0033 -0.0088 -0.0037 42  VAL   A CA  
296  C C   . VAL   A 36  ? 0.1540 0.1506 0.1904 -0.0048 -0.0092 -0.0053 42  VAL   A C   
297  O O   . VAL   A 36  ? 0.1764 0.1716 0.2125 -0.0064 -0.0086 -0.0050 42  VAL   A O   
298  C CB  . VAL   A 36  ? 0.1554 0.1551 0.1883 -0.0061 -0.0071 -0.0031 42  VAL   A CB  
299  C CG1 . VAL   A 36  ? 0.1699 0.1711 0.2065 -0.0073 -0.0047 -0.0063 42  VAL   A CG1 
300  C CG2 . VAL   A 36  ? 0.1741 0.1752 0.2040 -0.0057 -0.0073 -0.0009 42  VAL   A CG2 
301  N N   . SER   A 37  ? 0.1577 0.1565 0.1976 -0.0043 -0.0105 -0.0061 43  SER   A N   
302  C CA  . SER   A 37  ? 0.1666 0.1679 0.2110 -0.0061 -0.0116 -0.0066 43  SER   A CA  
303  C C   . SER   A 37  ? 0.1817 0.1873 0.2353 -0.0056 -0.0101 -0.0064 43  SER   A C   
304  O O   . SER   A 37  ? 0.1767 0.1823 0.2325 -0.0040 -0.0081 -0.0064 43  SER   A O   
305  C CB  . SER   A 37  ? 0.1787 0.1804 0.2208 -0.0073 -0.0149 -0.0061 43  SER   A CB  
306  O OG  . SER   A 37  ? 0.1781 0.1822 0.2213 -0.0060 -0.0169 -0.0041 43  SER   A OG  
307  N N   . SER   A 38  ? 0.1906 0.1996 0.2510 -0.0072 -0.0099 -0.0066 44  SER   A N   
308  C CA  . SER   A 38  ? 0.1979 0.2108 0.2708 -0.0064 -0.0069 -0.0065 44  SER   A CA  
309  C C   . SER   A 38  ? 0.2173 0.2357 0.3002 -0.0045 -0.0107 -0.0018 44  SER   A C   
310  O O   . SER   A 38  ? 0.2376 0.2586 0.3168 -0.0061 -0.0162 0.0008  44  SER   A O   
311  C CB  . SER   A 38  ? 0.2307 0.2453 0.3077 -0.0092 -0.0041 -0.0086 44  SER   A CB  
312  O OG  . SER   A 38  ? 0.2646 0.2820 0.3416 -0.0108 -0.0085 -0.0070 44  SER   A OG  
313  N N   . THR   A 39  ? 0.2115 0.2317 0.3073 -0.0019 -0.0073 -0.0004 45  THR   A N   
314  C CA  . THR   A 39  ? 0.2255 0.2519 0.3341 0.0002  -0.0111 0.0064  45  THR   A CA  
315  C C   . THR   A 39  ? 0.2391 0.2709 0.3687 0.0015  -0.0072 0.0085  45  THR   A C   
316  O O   . THR   A 39  ? 0.2182 0.2464 0.3522 0.0014  0.0009  0.0031  45  THR   A O   
317  C CB  . THR   A 39  ? 0.2399 0.2632 0.3488 0.0031  -0.0102 0.0081  45  THR   A CB  
318  O OG1 . THR   A 39  ? 0.2500 0.2686 0.3653 0.0044  -0.0014 0.0039  45  THR   A OG1 
319  C CG2 . THR   A 39  ? 0.2489 0.2675 0.3395 0.0021  -0.0132 0.0062  45  THR   A CG2 
320  N N   . THR   A 40  ? 0.2466 0.2874 0.3904 0.0024  -0.0125 0.0168  46  THR   A N   
321  C CA  . THR   A 40  ? 0.2614 0.3085 0.4298 0.0046  -0.0086 0.0205  46  THR   A CA  
322  C C   . THR   A 40  ? 0.2688 0.3123 0.4528 0.0094  -0.0017 0.0220  46  THR   A C   
323  O O   . THR   A 40  ? 0.2815 0.3225 0.4800 0.0109  0.0083  0.0182  46  THR   A O   
324  C CB  . THR   A 40  ? 0.3049 0.3650 0.4834 0.0027  -0.0175 0.0299  46  THR   A CB  
325  O OG1 . THR   A 40  ? 0.3461 0.4100 0.5209 0.0021  -0.0256 0.0377  46  THR   A OG1 
326  C CG2 . THR   A 40  ? 0.3121 0.3738 0.4760 -0.0029 -0.0212 0.0261  46  THR   A CG2 
327  N N   . ALA   A 41  ? 0.2797 0.3219 0.4598 0.0111  -0.0057 0.0265  47  ALA   A N   
328  C CA  . ALA   A 41  ? 0.2873 0.3248 0.4812 0.0153  0.0010  0.0281  47  ALA   A CA  
329  C C   . ALA   A 41  ? 0.2798 0.3052 0.4573 0.0143  0.0084  0.0179  47  ALA   A C   
330  O O   . ALA   A 41  ? 0.2772 0.2995 0.4319 0.0114  0.0045  0.0135  47  ALA   A O   
331  C CB  . ALA   A 41  ? 0.3116 0.3543 0.5102 0.0169  -0.0074 0.0392  47  ALA   A CB  
332  N N   . GLN   A 42  ? 0.2658 0.2848 0.4559 0.0162  0.0192  0.0149  48  GLN   A N   
333  C CA  . GLN   A 42  ? 0.2794 0.2881 0.4541 0.0136  0.0264  0.0056  48  GLN   A CA  
334  C C   . GLN   A 42  ? 0.2666 0.2727 0.4334 0.0152  0.0219  0.0094  48  GLN   A C   
335  O O   . GLN   A 42  ? 0.2715 0.2808 0.4529 0.0190  0.0186  0.0184  48  GLN   A O   
336  C CB  . GLN   A 42  ? 0.3046 0.3065 0.4941 0.0129  0.0415  -0.0010 48  GLN   A CB  
337  C CG  . GLN   A 42  ? 0.3543 0.3573 0.5464 0.0093  0.0477  -0.0074 48  GLN   A CG  
338  C CD  . GLN   A 42  ? 0.4266 0.4226 0.6352 0.0079  0.0642  -0.0143 48  GLN   A CD  
339  O OE1 . GLN   A 42  ? 0.4244 0.4213 0.6609 0.0130  0.0697  -0.0092 48  GLN   A OE1 
340  N NE2 . GLN   A 42  ? 0.4672 0.4564 0.6596 0.0001  0.0729  -0.0258 48  GLN   A NE2 
341  N N   . GLY   A 43  ? 0.2419 0.2433 0.3862 0.0118  0.0211  0.0033  49  GLY   A N   
342  C CA  . GLY   A 43  ? 0.2481 0.2468 0.3818 0.0123  0.0174  0.0053  49  GLY   A CA  
343  C C   . GLY   A 43  ? 0.2312 0.2217 0.3674 0.0115  0.0272  0.0008  49  GLY   A C   
344  O O   . GLY   A 43  ? 0.2359 0.2216 0.3765 0.0087  0.0378  -0.0064 49  GLY   A O   
345  N N   . CYS   A 44  ? 0.2189 0.2072 0.3496 0.0126  0.0242  0.0039  50  CYS   A N   
346  C CA  . CYS   A 44  ? 0.2309 0.2111 0.3646 0.0119  0.0329  0.0008  50  CYS   A CA  
347  C C   . CYS   A 44  ? 0.2295 0.2062 0.3413 0.0069  0.0337  -0.0057 50  CYS   A C   
348  O O   . CYS   A 44  ? 0.2449 0.2150 0.3569 0.0048  0.0412  -0.0092 50  CYS   A O   
349  C CB  . CYS   A 44  ? 0.2450 0.2257 0.3930 0.0167  0.0298  0.0106  50  CYS   A CB  
350  S SG  . CYS   A 44  ? 0.3093 0.2954 0.4897 0.0224  0.0303  0.0207  50  CYS   A SG  
351  N N   . ASP   A 45  ? 0.2032 0.1846 0.2979 0.0054  0.0255  -0.0060 51  ASP   A N   
352  C CA  . ASP   A 45  ? 0.2015 0.1814 0.2783 0.0010  0.0255  -0.0103 51  ASP   A CA  
353  C C   . ASP   A 45  ? 0.2303 0.2081 0.3008 -0.0060 0.0336  -0.0185 51  ASP   A C   
354  O O   . ASP   A 45  ? 0.2492 0.2285 0.3229 -0.0075 0.0357  -0.0207 51  ASP   A O   
355  C CB  . ASP   A 45  ? 0.1900 0.1754 0.2540 0.0018  0.0155  -0.0075 51  ASP   A CB  
356  C CG  . ASP   A 45  ? 0.2075 0.1950 0.2734 0.0059  0.0082  -0.0007 51  ASP   A CG  
357  O OD1 . ASP   A 45  ? 0.2282 0.2127 0.2975 0.0069  0.0095  0.0017  51  ASP   A OD1 
358  O OD2 . ASP   A 45  ? 0.2094 0.2011 0.2719 0.0069  0.0015  0.0020  51  ASP   A OD2 
359  N N   . THR   A 46  ? 0.2467 0.2219 0.3070 -0.0115 0.0377  -0.0227 52  THR   A N   
360  C CA  . THR   A 46  ? 0.2604 0.2350 0.3103 -0.0210 0.0445  -0.0300 52  THR   A CA  
361  C C   . THR   A 46  ? 0.2497 0.2311 0.2828 -0.0244 0.0367  -0.0280 52  THR   A C   
362  O O   . THR   A 46  ? 0.2711 0.2535 0.3007 -0.0216 0.0320  -0.0245 52  THR   A O   
363  C CB  . THR   A 46  ? 0.3382 0.3051 0.3901 -0.0262 0.0560  -0.0360 52  THR   A CB  
364  O OG1 . THR   A 46  ? 0.3831 0.3436 0.4542 -0.0228 0.0648  -0.0376 52  THR   A OG1 
365  C CG2 . THR   A 46  ? 0.3712 0.3386 0.4073 -0.0390 0.0621  -0.0435 52  THR   A CG2 
366  N N   . ILE   A 47  ? 0.2311 0.2175 0.2553 -0.0305 0.0355  -0.0293 53  ILE   A N   
367  C CA  . ILE   A 47  ? 0.2156 0.2094 0.2277 -0.0335 0.0283  -0.0255 53  ILE   A CA  
368  C C   . ILE   A 47  ? 0.2296 0.2250 0.2306 -0.0442 0.0328  -0.0291 53  ILE   A C   
369  O O   . ILE   A 47  ? 0.2454 0.2386 0.2424 -0.0535 0.0411  -0.0354 53  ILE   A O   
370  C CB  . ILE   A 47  ? 0.2093 0.2089 0.2184 -0.0351 0.0238  -0.0229 53  ILE   A CB  
371  C CG1 . ILE   A 47  ? 0.2245 0.2222 0.2439 -0.0265 0.0206  -0.0207 53  ILE   A CG1 
372  C CG2 . ILE   A 47  ? 0.2063 0.2142 0.2074 -0.0368 0.0159  -0.0166 53  ILE   A CG2 
373  C CD1 . ILE   A 47  ? 0.2126 0.2102 0.2359 -0.0174 0.0137  -0.0156 53  ILE   A CD1 
374  N N   . ALA   A 48  ? 0.2080 0.2080 0.2031 -0.0443 0.0278  -0.0252 54  ALA   A N   
375  C CA  . ALA   A 48  ? 0.2119 0.2161 0.1956 -0.0554 0.0302  -0.0271 54  ALA   A CA  
376  C C   . ALA   A 48  ? 0.2208 0.2347 0.1949 -0.0655 0.0274  -0.0249 54  ALA   A C   
377  O O   . ALA   A 48  ? 0.2193 0.2394 0.1957 -0.0615 0.0198  -0.0182 54  ALA   A O   
378  C CB  . ALA   A 48  ? 0.2093 0.2179 0.1914 -0.0518 0.0243  -0.0220 54  ALA   A CB  
379  N N   . ARG   A 49  ? 0.2433 0.2587 0.2063 -0.0798 0.0338  -0.0302 55  ARG   A N   
380  C CA  . ARG   A 49  ? 0.2577 0.2842 0.2096 -0.0921 0.0304  -0.0269 55  ARG   A CA  
381  C C   . ARG   A 49  ? 0.2930 0.3269 0.2332 -0.1040 0.0303  -0.0264 55  ARG   A C   
382  O O   . ARG   A 49  ? 0.3171 0.3473 0.2474 -0.1170 0.0399  -0.0352 55  ARG   A O   
383  C CB  . ARG   A 49  ? 0.2700 0.2916 0.2177 -0.1011 0.0392  -0.0348 55  ARG   A CB  
384  C CG  . ARG   A 49  ? 0.2745 0.2890 0.2351 -0.0896 0.0400  -0.0358 55  ARG   A CG  
385  C CD  . ARG   A 49  ? 0.2597 0.2812 0.2253 -0.0812 0.0287  -0.0258 55  ARG   A CD  
386  N NE  . ARG   A 49  ? 0.2550 0.2696 0.2318 -0.0719 0.0302  -0.0277 55  ARG   A NE  
387  C CZ  . ARG   A 49  ? 0.2542 0.2709 0.2379 -0.0622 0.0223  -0.0210 55  ARG   A CZ  
388  N NH1 . ARG   A 49  ? 0.2344 0.2589 0.2166 -0.0602 0.0134  -0.0122 55  ARG   A NH1 
389  N NH2 . ARG   A 49  ? 0.2689 0.2799 0.2621 -0.0549 0.0239  -0.0231 55  ARG   A NH2 
390  N N   . CYS   A 50  ? 0.2858 0.3303 0.2278 -0.1003 0.0202  -0.0163 56  CYS   A N   
391  C CA  . CYS   A 50  ? 0.2879 0.3409 0.2228 -0.1082 0.0182  -0.0137 56  CYS   A CA  
392  C C   . CYS   A 50  ? 0.2986 0.3659 0.2395 -0.1035 0.0062  -0.0001 56  CYS   A C   
393  O O   . CYS   A 50  ? 0.3219 0.3909 0.2733 -0.0931 0.0003  0.0067  56  CYS   A O   
394  C CB  . CYS   A 50  ? 0.2898 0.3309 0.2282 -0.1019 0.0247  -0.0207 56  CYS   A CB  
395  S SG  . CYS   A 50  ? 0.2844 0.3204 0.2392 -0.0806 0.0187  -0.0155 56  CYS   A SG  
396  N N   . ASP   A 51  ? 0.3375 0.4149 0.2735 -0.1109 0.0036  0.0036  57  ASP   A N   
397  C CA  . ASP   A 51  ? 0.3535 0.4444 0.2988 -0.1055 -0.0064 0.0165  57  ASP   A CA  
398  C C   . ASP   A 51  ? 0.3427 0.4297 0.2926 -0.0983 -0.0049 0.0143  57  ASP   A C   
399  O O   . ASP   A 51  ? 0.3480 0.4477 0.3019 -0.0994 -0.0106 0.0227  57  ASP   A O   
400  C CB  . ASP   A 51  ? 0.4062 0.5174 0.3444 -0.1215 -0.0130 0.0265  57  ASP   A CB  
401  C CG  . ASP   A 51  ? 0.5116 0.6266 0.4333 -0.1390 -0.0083 0.0203  57  ASP   A CG  
402  O OD1 . ASP   A 51  ? 0.5357 0.6357 0.4518 -0.1385 0.0015  0.0074  57  ASP   A OD1 
403  O OD2 . ASP   A 51  ? 0.5657 0.6988 0.4801 -0.1540 -0.0143 0.0288  57  ASP   A OD2 
404  N N   . CYS   A 52  ? 0.3050 0.3752 0.2562 -0.0901 0.0023  0.0044  58  CYS   A N   
405  C CA  . CYS   A 52  ? 0.2722 0.3378 0.2270 -0.0833 0.0036  0.0027  58  CYS   A CA  
406  C C   . CYS   A 52  ? 0.2726 0.3455 0.2405 -0.0721 -0.0039 0.0123  58  CYS   A C   
407  O O   . CYS   A 52  ? 0.2738 0.3472 0.2506 -0.0642 -0.0076 0.0170  58  CYS   A O   
408  C CB  . CYS   A 52  ? 0.2735 0.3211 0.2307 -0.0750 0.0108  -0.0064 58  CYS   A CB  
409  S SG  . CYS   A 52  ? 0.2996 0.3351 0.2462 -0.0863 0.0232  -0.0190 58  CYS   A SG  
410  N N   . GLN   A 53  ? 0.2367 0.3149 0.2060 -0.0722 -0.0050 0.0145  59  GLN   A N   
411  C CA  . GLN   A 53  ? 0.2270 0.3101 0.2095 -0.0618 -0.0094 0.0216  59  GLN   A CA  
412  C C   . GLN   A 53  ? 0.1984 0.2712 0.1810 -0.0553 -0.0054 0.0157  59  GLN   A C   
413  O O   . GLN   A 53  ? 0.2018 0.2787 0.1930 -0.0492 -0.0073 0.0197  59  GLN   A O   
414  C CB  . GLN   A 53  ? 0.2619 0.3646 0.2500 -0.0676 -0.0156 0.0328  59  GLN   A CB  
415  C CG  . GLN   A 53  ? 0.2898 0.4040 0.2845 -0.0698 -0.0216 0.0429  59  GLN   A CG  
416  C CD  . GLN   A 53  ? 0.3406 0.4753 0.3458 -0.0737 -0.0283 0.0565  59  GLN   A CD  
417  O OE1 . GLN   A 53  ? 0.3679 0.5175 0.3664 -0.0876 -0.0324 0.0625  59  GLN   A OE1 
418  N NE2 . GLN   A 53  ? 0.2914 0.4284 0.3141 -0.0625 -0.0292 0.0620  59  GLN   A NE2 
419  N N   . THR   A 54  ? 0.1941 0.2538 0.1684 -0.0568 0.0006  0.0066  60  THR   A N   
420  C CA  . THR   A 54  ? 0.1999 0.2489 0.1749 -0.0503 0.0040  0.0021  60  THR   A CA  
421  C C   . THR   A 54  ? 0.1982 0.2325 0.1734 -0.0450 0.0078  -0.0036 60  THR   A C   
422  O O   . THR   A 54  ? 0.2336 0.2641 0.2053 -0.0496 0.0109  -0.0072 60  THR   A O   
423  C CB  . THR   A 54  ? 0.2299 0.2787 0.1970 -0.0580 0.0076  -0.0014 60  THR   A CB  
424  O OG1 . THR   A 54  ? 0.3130 0.3558 0.2711 -0.0671 0.0135  -0.0079 60  THR   A OG1 
425  C CG2 . THR   A 54  ? 0.2338 0.2990 0.2015 -0.0642 0.0036  0.0049  60  THR   A CG2 
426  N N   . GLY   A 55  ? 0.1825 0.2096 0.1624 -0.0359 0.0073  -0.0038 61  GLY   A N   
427  C CA  . GLY   A 55  ? 0.1778 0.1933 0.1601 -0.0307 0.0095  -0.0069 61  GLY   A CA  
428  C C   . GLY   A 55  ? 0.1767 0.1867 0.1619 -0.0235 0.0082  -0.0060 61  GLY   A C   
429  O O   . GLY   A 55  ? 0.1808 0.1935 0.1643 -0.0239 0.0078  -0.0050 61  GLY   A O   
430  N N   . VAL   A 56  ? 0.1593 0.1626 0.1484 -0.0182 0.0076  -0.0062 62  VAL   A N   
431  C CA  . VAL   A 56  ? 0.1618 0.1604 0.1520 -0.0134 0.0060  -0.0048 62  VAL   A CA  
432  C C   . VAL   A 56  ? 0.1576 0.1561 0.1517 -0.0087 0.0027  -0.0033 62  VAL   A C   
433  O O   . VAL   A 56  ? 0.1747 0.1721 0.1721 -0.0081 0.0028  -0.0038 62  VAL   A O   
434  C CB  . VAL   A 56  ? 0.1993 0.1893 0.1907 -0.0138 0.0091  -0.0056 62  VAL   A CB  
435  C CG1 . VAL   A 56  ? 0.2170 0.2033 0.2094 -0.0102 0.0062  -0.0024 62  VAL   A CG1 
436  C CG2 . VAL   A 56  ? 0.1988 0.1875 0.1858 -0.0193 0.0136  -0.0079 62  VAL   A CG2 
437  N N   . TYR   A 57  ? 0.1528 0.1521 0.1461 -0.0063 0.0005  -0.0021 63  TYR   A N   
438  C CA  . TYR   A 57  ? 0.1600 0.1583 0.1556 -0.0032 -0.0018 -0.0015 63  TYR   A CA  
439  C C   . TYR   A 57  ? 0.1639 0.1583 0.1566 -0.0030 -0.0036 -0.0006 63  TYR   A C   
440  O O   . TYR   A 57  ? 0.1798 0.1733 0.1683 -0.0048 -0.0030 -0.0003 63  TYR   A O   
441  C CB  . TYR   A 57  ? 0.1580 0.1609 0.1561 -0.0018 -0.0018 -0.0015 63  TYR   A CB  
442  C CG  . TYR   A 57  ? 0.1582 0.1616 0.1550 -0.0017 -0.0004 -0.0022 63  TYR   A CG  
443  C CD1 . TYR   A 57  ? 0.1799 0.1869 0.1760 -0.0033 0.0014  -0.0021 63  TYR   A CD1 
444  C CD2 . TYR   A 57  ? 0.1751 0.1753 0.1708 -0.0011 0.0001  -0.0038 63  TYR   A CD2 
445  C CE1 . TYR   A 57  ? 0.1827 0.1899 0.1783 -0.0035 0.0040  -0.0034 63  TYR   A CE1 
446  C CE2 . TYR   A 57  ? 0.1813 0.1812 0.1755 -0.0021 0.0033  -0.0059 63  TYR   A CE2 
447  C CZ  . TYR   A 57  ? 0.1908 0.1941 0.1856 -0.0030 0.0055  -0.0057 63  TYR   A CZ  
448  O OH  . TYR   A 57  ? 0.2095 0.2122 0.2034 -0.0044 0.0098  -0.0084 63  TYR   A OH  
449  N N   . TYR   A 58  ? 0.1592 0.1521 0.1536 -0.0019 -0.0060 0.0004  64  TYR   A N   
450  C CA  . TYR   A 58  ? 0.1683 0.1596 0.1587 -0.0037 -0.0087 0.0023  64  TYR   A CA  
451  C C   . TYR   A 58  ? 0.1713 0.1632 0.1567 -0.0055 -0.0079 -0.0006 64  TYR   A C   
452  O O   . TYR   A 58  ? 0.1746 0.1670 0.1626 -0.0041 -0.0070 -0.0025 64  TYR   A O   
453  C CB  . TYR   A 58  ? 0.1831 0.1740 0.1786 -0.0030 -0.0121 0.0057  64  TYR   A CB  
454  C CG  . TYR   A 58  ? 0.1937 0.1851 0.1848 -0.0066 -0.0161 0.0096  64  TYR   A CG  
455  C CD1 . TYR   A 58  ? 0.1992 0.1897 0.1880 -0.0088 -0.0173 0.0133  64  TYR   A CD1 
456  C CD2 . TYR   A 58  ? 0.1924 0.1857 0.1809 -0.0092 -0.0190 0.0098  64  TYR   A CD2 
457  C CE1 . TYR   A 58  ? 0.2169 0.2094 0.2004 -0.0138 -0.0218 0.0181  64  TYR   A CE1 
458  C CE2 . TYR   A 58  ? 0.2093 0.2047 0.1915 -0.0150 -0.0232 0.0137  64  TYR   A CE2 
459  C CZ  . TYR   A 58  ? 0.2336 0.2292 0.2137 -0.0173 -0.0251 0.0185  64  TYR   A CZ  
460  O OH  . TYR   A 58  ? 0.2496 0.2485 0.2222 -0.0247 -0.0300 0.0234  64  TYR   A OH  
461  N N   . CYS   A 59  ? 0.1754 0.1666 0.1537 -0.0092 -0.0074 -0.0010 65  CYS   A N   
462  C CA  . CYS   A 59  ? 0.1793 0.1698 0.1515 -0.0127 -0.0046 -0.0049 65  CYS   A CA  
463  C C   . CYS   A 59  ? 0.2030 0.1929 0.1667 -0.0190 -0.0081 -0.0032 65  CYS   A C   
464  O O   . CYS   A 59  ? 0.2040 0.1941 0.1615 -0.0231 -0.0100 -0.0004 65  CYS   A O   
465  C CB  . CYS   A 59  ? 0.1781 0.1690 0.1481 -0.0137 -0.0003 -0.0073 65  CYS   A CB  
466  S SG  . CYS   A 59  ? 0.2110 0.1996 0.1750 -0.0188 0.0061  -0.0137 65  CYS   A SG  
467  N N   . SER   A 60  ? 0.2025 0.1922 0.1653 -0.0209 -0.0092 -0.0041 66  SER   A N   
468  C CA  . SER   A 60  ? 0.2164 0.2077 0.1709 -0.0285 -0.0137 -0.0013 66  SER   A CA  
469  C C   . SER   A 60  ? 0.2311 0.2213 0.1723 -0.0375 -0.0108 -0.0050 66  SER   A C   
470  O O   . SER   A 60  ? 0.2440 0.2370 0.1769 -0.0447 -0.0156 -0.0002 66  SER   A O   
471  C CB  . SER   A 60  ? 0.2301 0.2222 0.1862 -0.0295 -0.0153 -0.0021 66  SER   A CB  
472  O OG  . SER   A 60  ? 0.2725 0.2607 0.2252 -0.0316 -0.0087 -0.0099 66  SER   A OG  
473  N N   . SER   A 61  ? 0.2186 0.2051 0.1588 -0.0372 -0.0024 -0.0128 67  SER   A N   
474  C CA  . SER   A 61  ? 0.2381 0.2225 0.1664 -0.0461 0.0030  -0.0181 67  SER   A CA  
475  C C   . SER   A 61  ? 0.2436 0.2293 0.1677 -0.0476 0.0019  -0.0153 67  SER   A C   
476  O O   . SER   A 61  ? 0.2569 0.2413 0.1700 -0.0560 0.0059  -0.0193 67  SER   A O   
477  C CB  . SER   A 61  ? 0.2512 0.2307 0.1833 -0.0450 0.0138  -0.0272 67  SER   A CB  
478  O OG  . SER   A 61  ? 0.2274 0.2076 0.1725 -0.0355 0.0168  -0.0267 67  SER   A OG  
479  N N   . ARG   A 62  ? 0.2260 0.2138 0.1582 -0.0406 -0.0028 -0.0090 68  ARG   A N   
480  C CA  . ARG   A 62  ? 0.2272 0.2158 0.1558 -0.0422 -0.0045 -0.0053 68  ARG   A CA  
481  C C   . ARG   A 62  ? 0.2387 0.2295 0.1704 -0.0411 -0.0130 0.0046  68  ARG   A C   
482  O O   . ARG   A 62  ? 0.2455 0.2362 0.1760 -0.0420 -0.0147 0.0090  68  ARG   A O   
483  C CB  . ARG   A 62  ? 0.2303 0.2184 0.1673 -0.0350 0.0003  -0.0079 68  ARG   A CB  
484  C CG  . ARG   A 62  ? 0.2534 0.2404 0.1914 -0.0354 0.0091  -0.0159 68  ARG   A CG  
485  C CD  . ARG   A 62  ? 0.2417 0.2276 0.1679 -0.0440 0.0128  -0.0190 68  ARG   A CD  
486  N NE  . ARG   A 62  ? 0.2769 0.2613 0.2066 -0.0443 0.0230  -0.0269 68  ARG   A NE  
487  C CZ  . ARG   A 62  ? 0.2765 0.2574 0.2030 -0.0492 0.0297  -0.0337 68  ARG   A CZ  
488  N NH1 . ARG   A 62  ? 0.2949 0.2742 0.2122 -0.0553 0.0265  -0.0337 68  ARG   A NH1 
489  N NH2 . ARG   A 62  ? 0.3110 0.2901 0.2441 -0.0487 0.0405  -0.0405 68  ARG   A NH2 
490  N N   . ARG   A 63  ? 0.2375 0.2301 0.1758 -0.0385 -0.0176 0.0085  69  ARG   A N   
491  C CA  . ARG   A 63  ? 0.2480 0.2426 0.1953 -0.0354 -0.0241 0.0183  69  ARG   A CA  
492  C C   . ARG   A 63  ? 0.2696 0.2612 0.2252 -0.0289 -0.0216 0.0194  69  ARG   A C   
493  O O   . ARG   A 63  ? 0.2937 0.2848 0.2526 -0.0292 -0.0245 0.0266  69  ARG   A O   
494  C CB  . ARG   A 63  ? 0.2847 0.2833 0.2251 -0.0440 -0.0308 0.0271  69  ARG   A CB  
495  C CG  . ARG   A 63  ? 0.2985 0.3017 0.2339 -0.0506 -0.0352 0.0288  69  ARG   A CG  
496  C CD  . ARG   A 63  ? 0.3041 0.3139 0.2379 -0.0579 -0.0443 0.0416  69  ARG   A CD  
497  N NE  . ARG   A 63  ? 0.3347 0.3504 0.2590 -0.0679 -0.0484 0.0424  69  ARG   A NE  
498  C CZ  . ARG   A 63  ? 0.3498 0.3681 0.2554 -0.0816 -0.0491 0.0407  69  ARG   A CZ  
499  N NH1 . ARG   A 63  ? 0.3335 0.3490 0.2287 -0.0863 -0.0460 0.0385  69  ARG   A NH1 
500  N NH2 . ARG   A 63  ? 0.3517 0.3754 0.2482 -0.0919 -0.0523 0.0408  69  ARG   A NH2 
501  N N   . LYS   A 64  ? 0.2390 0.2286 0.1980 -0.0238 -0.0162 0.0127  70  LYS   A N   
502  C CA  . LYS   A 64  ? 0.2501 0.2375 0.2142 -0.0199 -0.0131 0.0124  70  LYS   A CA  
503  C C   . LYS   A 64  ? 0.2277 0.2152 0.1998 -0.0142 -0.0101 0.0086  70  LYS   A C   
504  O O   . LYS   A 64  ? 0.2156 0.2047 0.1880 -0.0130 -0.0088 0.0047  70  LYS   A O   
505  C CB  . LYS   A 64  ? 0.2737 0.2610 0.2296 -0.0231 -0.0092 0.0082  70  LYS   A CB  
506  C CG  . LYS   A 64  ? 0.3708 0.3571 0.3192 -0.0289 -0.0115 0.0129  70  LYS   A CG  
507  C CD  . LYS   A 64  ? 0.4791 0.4649 0.4215 -0.0313 -0.0068 0.0088  70  LYS   A CD  
508  C CE  . LYS   A 64  ? 0.5671 0.5524 0.4991 -0.0389 -0.0090 0.0127  70  LYS   A CE  
509  N NZ  . LYS   A 64  ? 0.6268 0.6142 0.5492 -0.0459 -0.0112 0.0122  70  LYS   A NZ  
510  N N   . HIS   A 65  ? 0.2102 0.1955 0.1883 -0.0118 -0.0083 0.0097  71  HIS   A N   
511  C CA  . HIS   A 65  ? 0.2023 0.1882 0.1856 -0.0088 -0.0049 0.0060  71  HIS   A CA  
512  C C   . HIS   A 65  ? 0.2268 0.2142 0.2059 -0.0107 -0.0014 0.0028  71  HIS   A C   
513  O O   . HIS   A 65  ? 0.2628 0.2478 0.2389 -0.0130 -0.0003 0.0040  71  HIS   A O   
514  C CB  . HIS   A 65  ? 0.1811 0.1634 0.1730 -0.0070 -0.0035 0.0080  71  HIS   A CB  
515  C CG  . HIS   A 65  ? 0.2016 0.1837 0.2007 -0.0048 -0.0066 0.0117  71  HIS   A CG  
516  N ND1 . HIS   A 65  ? 0.2476 0.2308 0.2518 -0.0025 -0.0058 0.0094  71  HIS   A ND1 
517  C CD2 . HIS   A 65  ? 0.2094 0.1915 0.2117 -0.0052 -0.0109 0.0183  71  HIS   A CD2 
518  C CE1 . HIS   A 65  ? 0.2141 0.1977 0.2253 -0.0012 -0.0091 0.0141  71  HIS   A CE1 
519  N NE2 . HIS   A 65  ? 0.2414 0.2250 0.2521 -0.0028 -0.0126 0.0201  71  HIS   A NE2 
520  N N   . TYR   A 66  ? 0.1979 0.1900 0.1778 -0.0099 0.0002  -0.0003 72  TYR   A N   
521  C CA  . TYR   A 66  ? 0.1840 0.1802 0.1620 -0.0119 0.0029  -0.0021 72  TYR   A CA  
522  C C   . TYR   A 66  ? 0.1777 0.1776 0.1590 -0.0126 0.0043  -0.0028 72  TYR   A C   
523  O O   . TYR   A 66  ? 0.1752 0.1777 0.1607 -0.0109 0.0033  -0.0026 72  TYR   A O   
524  C CB  . TYR   A 66  ? 0.1928 0.1935 0.1717 -0.0110 0.0038  -0.0035 72  TYR   A CB  
525  C CG  . TYR   A 66  ? 0.2109 0.2087 0.1840 -0.0129 0.0042  -0.0046 72  TYR   A CG  
526  C CD1 . TYR   A 66  ? 0.2177 0.2153 0.1853 -0.0163 0.0061  -0.0052 72  TYR   A CD1 
527  C CD2 . TYR   A 66  ? 0.2136 0.2093 0.1855 -0.0127 0.0033  -0.0054 72  TYR   A CD2 
528  C CE1 . TYR   A 66  ? 0.2381 0.2333 0.1984 -0.0199 0.0068  -0.0064 72  TYR   A CE1 
529  C CE2 . TYR   A 66  ? 0.2328 0.2262 0.1969 -0.0169 0.0041  -0.0069 72  TYR   A CE2 
530  C CZ  . TYR   A 66  ? 0.2414 0.2346 0.1995 -0.0208 0.0059  -0.0074 72  TYR   A CZ  
531  O OH  . TYR   A 66  ? 0.2731 0.2644 0.2218 -0.0267 0.0072  -0.0094 72  TYR   A OH  
532  N N   . PRO   A 67  ? 0.1758 0.1768 0.1544 -0.0164 0.0066  -0.0036 73  PRO   A N   
533  C CA  . PRO   A 67  ? 0.1759 0.1827 0.1555 -0.0198 0.0079  -0.0043 73  PRO   A CA  
534  C C   . PRO   A 67  ? 0.1854 0.2029 0.1688 -0.0195 0.0064  -0.0023 73  PRO   A C   
535  O O   . PRO   A 67  ? 0.2055 0.2260 0.1896 -0.0188 0.0069  -0.0017 73  PRO   A O   
536  C CB  . PRO   A 67  ? 0.2086 0.2131 0.1830 -0.0252 0.0113  -0.0060 73  PRO   A CB  
537  C CG  . PRO   A 67  ? 0.2279 0.2283 0.1996 -0.0239 0.0112  -0.0053 73  PRO   A CG  
538  C CD  . PRO   A 67  ? 0.1891 0.1866 0.1627 -0.0189 0.0082  -0.0037 73  PRO   A CD  
539  N N   . VAL   A 68  ? 0.1627 0.1862 0.1497 -0.0203 0.0049  -0.0006 74  VAL   A N   
540  C CA  . VAL   A 68  ? 0.1783 0.2129 0.1728 -0.0194 0.0031  0.0036  74  VAL   A CA  
541  C C   . VAL   A 68  ? 0.1704 0.2146 0.1653 -0.0252 0.0014  0.0067  74  VAL   A C   
542  O O   . VAL   A 68  ? 0.1827 0.2241 0.1726 -0.0290 0.0018  0.0048  74  VAL   A O   
543  C CB  . VAL   A 68  ? 0.2009 0.2338 0.2026 -0.0130 0.0021  0.0049  74  VAL   A CB  
544  C CG1 . VAL   A 68  ? 0.2155 0.2420 0.2165 -0.0095 0.0041  0.0023  74  VAL   A CG1 
545  C CG2 . VAL   A 68  ? 0.2175 0.2451 0.2177 -0.0121 0.0008  0.0038  74  VAL   A CG2 
546  N N   . SER   A 69  ? 0.1644 0.2213 0.1664 -0.0266 -0.0005 0.0123  75  SER   A N   
547  C CA  . SER   A 69  ? 0.1567 0.2265 0.1620 -0.0321 -0.0040 0.0185  75  SER   A CA  
548  C C   . SER   A 69  ? 0.1519 0.2248 0.1696 -0.0256 -0.0063 0.0239  75  SER   A C   
549  O O   . SER   A 69  ? 0.1670 0.2378 0.1940 -0.0184 -0.0045 0.0245  75  SER   A O   
550  C CB  . SER   A 69  ? 0.1913 0.2750 0.2005 -0.0371 -0.0054 0.0237  75  SER   A CB  
551  O OG  . SER   A 69  ? 0.2930 0.3733 0.2901 -0.0440 -0.0027 0.0183  75  SER   A OG  
552  N N   . PHE   A 70  ? 0.1584 0.2349 0.1760 -0.0284 -0.0091 0.0272  76  PHE   A N   
553  C CA  . PHE   A 70  ? 0.1606 0.2383 0.1898 -0.0223 -0.0108 0.0323  76  PHE   A CA  
554  C C   . PHE   A 70  ? 0.1627 0.2550 0.1975 -0.0279 -0.0159 0.0422  76  PHE   A C   
555  O O   . PHE   A 70  ? 0.1833 0.2824 0.2080 -0.0383 -0.0180 0.0429  76  PHE   A O   
556  C CB  . PHE   A 70  ? 0.1745 0.2380 0.1985 -0.0179 -0.0090 0.0257  76  PHE   A CB  
557  C CG  . PHE   A 70  ? 0.1691 0.2280 0.1809 -0.0239 -0.0087 0.0209  76  PHE   A CG  
558  C CD1 . PHE   A 70  ? 0.1705 0.2204 0.1727 -0.0258 -0.0052 0.0134  76  PHE   A CD1 
559  C CD2 . PHE   A 70  ? 0.1730 0.2361 0.1842 -0.0280 -0.0110 0.0240  76  PHE   A CD2 
560  C CE1 . PHE   A 70  ? 0.1868 0.2316 0.1806 -0.0313 -0.0030 0.0087  76  PHE   A CE1 
561  C CE2 . PHE   A 70  ? 0.1889 0.2472 0.1893 -0.0344 -0.0090 0.0184  76  PHE   A CE2 
562  C CZ  . PHE   A 70  ? 0.1868 0.2358 0.1796 -0.0357 -0.0044 0.0106  76  PHE   A CZ  
563  N N   . SER   A 71  ? 0.1606 0.2578 0.2114 -0.0221 -0.0175 0.0502  77  SER   A N   
564  C CA  . SER   A 71  ? 0.1697 0.2826 0.2287 -0.0272 -0.0234 0.0625  77  SER   A CA  
565  C C   . SER   A 71  ? 0.1792 0.2894 0.2289 -0.0320 -0.0257 0.0619  77  SER   A C   
566  O O   . SER   A 71  ? 0.1841 0.2798 0.2248 -0.0291 -0.0222 0.0522  77  SER   A O   
567  C CB  . SER   A 71  ? 0.1843 0.3033 0.2674 -0.0189 -0.0234 0.0726  77  SER   A CB  
568  O OG  . SER   A 71  ? 0.1950 0.3002 0.2835 -0.0098 -0.0192 0.0682  77  SER   A OG  
569  N N   . LYS   A 72  ? 0.1815 0.3065 0.2330 -0.0403 -0.0316 0.0724  78  LYS   A N   
570  C CA  . LYS   A 72  ? 0.1805 0.3039 0.2233 -0.0459 -0.0335 0.0724  78  LYS   A CA  
571  C C   . LYS   A 72  ? 0.1951 0.3115 0.2512 -0.0356 -0.0330 0.0755  78  LYS   A C   
572  O O   . LYS   A 72  ? 0.1917 0.3107 0.2667 -0.0271 -0.0326 0.0824  78  LYS   A O   
573  C CB  . LYS   A 72  ? 0.2042 0.3472 0.2440 -0.0599 -0.0406 0.0839  78  LYS   A CB  
574  C CG  . LYS   A 72  ? 0.2460 0.3939 0.2689 -0.0725 -0.0398 0.0784  78  LYS   A CG  
575  C CD  . LYS   A 72  ? 0.2913 0.4565 0.3044 -0.0901 -0.0459 0.0868  78  LYS   A CD  
576  C CE  . LYS   A 72  ? 0.3835 0.5504 0.3770 -0.1041 -0.0429 0.0784  78  LYS   A CE  
577  N NZ  . LYS   A 72  ? 0.4422 0.6225 0.4203 -0.1241 -0.0467 0.0826  78  LYS   A NZ  
578  N N   . PRO   A 73  ? 0.1898 0.2969 0.2374 -0.0362 -0.0318 0.0700  79  PRO   A N   
579  C CA  . PRO   A 73  ? 0.1903 0.2899 0.2494 -0.0271 -0.0307 0.0721  79  PRO   A CA  
580  C C   . PRO   A 73  ? 0.2000 0.3127 0.2783 -0.0261 -0.0356 0.0886  79  PRO   A C   
581  O O   . PRO   A 73  ? 0.2222 0.3496 0.2990 -0.0359 -0.0418 0.0989  79  PRO   A O   
582  C CB  . PRO   A 73  ? 0.2143 0.3060 0.2595 -0.0315 -0.0298 0.0650  79  PRO   A CB  
583  C CG  . PRO   A 73  ? 0.2532 0.3434 0.2808 -0.0400 -0.0278 0.0559  79  PRO   A CG  
584  C CD  . PRO   A 73  ? 0.2073 0.3094 0.2351 -0.0455 -0.0301 0.0608  79  PRO   A CD  
585  N N   . SER   A 74  ? 0.1933 0.3009 0.2902 -0.0149 -0.0322 0.0914  80  SER   A N   
586  C CA  . SER   A 74  ? 0.2138 0.3328 0.3344 -0.0119 -0.0351 0.1078  80  SER   A CA  
587  C C   . SER   A 74  ? 0.1902 0.2963 0.3267 -0.0007 -0.0291 0.1071  80  SER   A C   
588  O O   . SER   A 74  ? 0.1877 0.2772 0.3159 0.0041  -0.0229 0.0935  80  SER   A O   
589  C CB  . SER   A 74  ? 0.2740 0.4045 0.4081 -0.0105 -0.0354 0.1144  80  SER   A CB  
590  O OG  . SER   A 74  ? 0.3885 0.5281 0.5068 -0.0203 -0.0390 0.1120  80  SER   A OG  
591  N N   . LEU   A 75  ? 0.2075 0.3221 0.3693 0.0032  -0.0303 0.1226  81  LEU   A N   
592  C CA  . LEU   A 75  ? 0.2283 0.3315 0.4094 0.0133  -0.0232 0.1235  81  LEU   A CA  
593  C C   . LEU   A 75  ? 0.2413 0.3435 0.4413 0.0212  -0.0159 0.1229  81  LEU   A C   
594  O O   . LEU   A 75  ? 0.2600 0.3779 0.4786 0.0212  -0.0189 0.1364  81  LEU   A O   
595  C CB  . LEU   A 75  ? 0.2288 0.3425 0.4288 0.0125  -0.0285 0.1423  81  LEU   A CB  
596  C CG  . LEU   A 75  ? 0.2637 0.3647 0.4838 0.0218  -0.0210 0.1443  81  LEU   A CG  
597  C CD1 . LEU   A 75  ? 0.2850 0.3683 0.4858 0.0215  -0.0174 0.1299  81  LEU   A CD1 
598  C CD2 . LEU   A 75  ? 0.2655 0.3796 0.5089 0.0212  -0.0268 0.1663  81  LEU   A CD2 
599  N N   . ILE   A 76  ? 0.2338 0.3187 0.4274 0.0264  -0.0066 0.1072  82  ILE   A N   
600  C CA  . ILE   A 76  ? 0.2430 0.3244 0.4493 0.0322  0.0020  0.1028  82  ILE   A CA  
601  C C   . ILE   A 76  ? 0.2510 0.3156 0.4710 0.0399  0.0141  0.0965  82  ILE   A C   
602  O O   . ILE   A 76  ? 0.2468 0.2969 0.4535 0.0397  0.0172  0.0863  82  ILE   A O   
603  C CB  . ILE   A 76  ? 0.2657 0.3429 0.4483 0.0286  0.0026  0.0886  82  ILE   A CB  
604  C CG1 . ILE   A 76  ? 0.2722 0.3606 0.4342 0.0193  -0.0079 0.0902  82  ILE   A CG1 
605  C CG2 . ILE   A 76  ? 0.2926 0.3720 0.4892 0.0326  0.0094  0.0876  82  ILE   A CG2 
606  C CD1 . ILE   A 76  ? 0.2707 0.3586 0.4154 0.0156  -0.0080 0.0808  82  ILE   A CD1 
607  N N   . PHE   A 77  ? 0.2412 0.3078 0.4886 0.0461  0.0219  0.1023  83  PHE   A N   
608  C CA  . PHE   A 77  ? 0.2496 0.2992 0.5108 0.0523  0.0361  0.0947  83  PHE   A CA  
609  C C   . PHE   A 77  ? 0.2666 0.3028 0.5065 0.0502  0.0433  0.0752  83  PHE   A C   
610  O O   . PHE   A 77  ? 0.2894 0.3317 0.5225 0.0482  0.0420  0.0722  83  PHE   A O   
611  C CB  . PHE   A 77  ? 0.2516 0.3074 0.5510 0.0594  0.0439  0.1063  83  PHE   A CB  
612  C CG  . PHE   A 77  ? 0.2927 0.3303 0.6099 0.0653  0.0593  0.1008  83  PHE   A CG  
613  C CD1 . PHE   A 77  ? 0.3223 0.3539 0.6472 0.0670  0.0592  0.1066  83  PHE   A CD1 
614  C CD2 . PHE   A 77  ? 0.3168 0.3425 0.6416 0.0679  0.0746  0.0887  83  PHE   A CD2 
615  C CE1 . PHE   A 77  ? 0.3471 0.3607 0.6882 0.0715  0.0746  0.1006  83  PHE   A CE1 
616  C CE2 . PHE   A 77  ? 0.3297 0.3376 0.6703 0.0717  0.0905  0.0822  83  PHE   A CE2 
617  C CZ  . PHE   A 77  ? 0.3427 0.3443 0.6916 0.0737  0.0906  0.0882  83  PHE   A CZ  
618  N N   . VAL   A 78  ? 0.2568 0.2758 0.4829 0.0491  0.0492  0.0625  84  VAL   A N   
619  C CA  . VAL   A 78  ? 0.2485 0.2549 0.4532 0.0455  0.0554  0.0450  84  VAL   A CA  
620  C C   . VAL   A 78  ? 0.2544 0.2448 0.4724 0.0480  0.0717  0.0368  84  VAL   A C   
621  O O   . VAL   A 78  ? 0.2613 0.2443 0.4901 0.0502  0.0758  0.0392  84  VAL   A O   
622  C CB  . VAL   A 78  ? 0.2401 0.2415 0.4158 0.0401  0.0476  0.0375  84  VAL   A CB  
623  C CG1 . VAL   A 78  ? 0.2551 0.2451 0.4092 0.0354  0.0526  0.0215  84  VAL   A CG1 
624  C CG2 . VAL   A 78  ? 0.2510 0.2666 0.4151 0.0370  0.0337  0.0448  84  VAL   A CG2 
625  N N   . GLU   A 79  ? 0.2636 0.2478 0.4786 0.0463  0.0815  0.0261  85  GLU   A N   
626  C CA  . GLU   A 79  ? 0.2898 0.2579 0.5152 0.0465  0.0991  0.0160  85  GLU   A CA  
627  C C   . GLU   A 79  ? 0.2944 0.2476 0.4982 0.0405  0.1017  0.0038  85  GLU   A C   
628  O O   . GLU   A 79  ? 0.3044 0.2597 0.4825 0.0358  0.0905  0.0009  85  GLU   A O   
629  C CB  . GLU   A 79  ? 0.3458 0.3115 0.5704 0.0441  0.1089  0.0067  85  GLU   A CB  
630  C CG  . GLU   A 79  ? 0.4442 0.4237 0.6964 0.0505  0.1096  0.0186  85  GLU   A CG  
631  C CD  . GLU   A 79  ? 0.5589 0.5393 0.8502 0.0589  0.1176  0.0306  85  GLU   A CD  
632  O OE1 . GLU   A 79  ? 0.5969 0.5612 0.9000 0.0597  0.1335  0.0230  85  GLU   A OE1 
633  O OE2 . GLU   A 79  ? 0.5929 0.5902 0.9033 0.0640  0.1080  0.0482  85  GLU   A OE2 
634  N N   . ALA   A 80  ? 0.3077 0.2454 0.5230 0.0402  0.1176  -0.0036 86  ALA   A N   
635  C CA  . ALA   A 80  ? 0.3261 0.2496 0.5216 0.0330  0.1216  -0.0157 86  ALA   A CA  
636  C C   . ALA   A 80  ? 0.3514 0.2728 0.5136 0.0232  0.1182  -0.0285 86  ALA   A C   
637  O O   . ALA   A 80  ? 0.3650 0.2879 0.5226 0.0205  0.1221  -0.0338 86  ALA   A O   
638  C CB  . ALA   A 80  ? 0.3407 0.2472 0.5536 0.0326  0.1420  -0.0236 86  ALA   A CB  
639  N N   . SER   A 81  ? 0.3461 0.2653 0.4864 0.0178  0.1103  -0.0321 87  SER   A N   
640  C CA  . SER   A 81  ? 0.3588 0.2765 0.4687 0.0077  0.1062  -0.0425 87  SER   A CA  
641  C C   . SER   A 81  ? 0.3743 0.2789 0.4724 -0.0005 0.1131  -0.0527 87  SER   A C   
642  O O   . SER   A 81  ? 0.3701 0.2658 0.4841 0.0023  0.1220  -0.0523 87  SER   A O   
643  C CB  . SER   A 81  ? 0.3674 0.2981 0.4627 0.0088  0.0878  -0.0351 87  SER   A CB  
644  O OG  . SER   A 81  ? 0.3632 0.2948 0.4582 0.0106  0.0805  -0.0300 87  SER   A OG  
645  N N   . GLU   A 82  ? 0.3833 0.2869 0.4543 -0.0109 0.1087  -0.0607 88  GLU   A N   
646  C CA  . GLU   A 82  ? 0.3893 0.2830 0.4466 -0.0205 0.1132  -0.0696 88  GLU   A CA  
647  C C   . GLU   A 82  ? 0.3565 0.2534 0.4165 -0.0160 0.1033  -0.0619 88  GLU   A C   
648  O O   . GLU   A 82  ? 0.3759 0.2640 0.4313 -0.0215 0.1083  -0.0674 88  GLU   A O   
649  C CB  . GLU   A 82  ? 0.4582 0.3535 0.4861 -0.0340 0.1091  -0.0780 88  GLU   A CB  
650  C CG  . GLU   A 82  ? 0.5457 0.4545 0.5645 -0.0319 0.0953  -0.0714 88  GLU   A CG  
651  C CD  . GLU   A 82  ? 0.6047 0.5145 0.6054 -0.0421 0.0969  -0.0782 88  GLU   A CD  
652  O OE1 . GLU   A 82  ? 0.6860 0.5877 0.6897 -0.0463 0.1113  -0.0866 88  GLU   A OE1 
653  O OE2 . GLU   A 82  ? 0.5471 0.4659 0.5319 -0.0457 0.0840  -0.0744 88  GLU   A OE2 
654  N N   . TYR   A 83  ? 0.3237 0.2328 0.3908 -0.0068 0.0901  -0.0497 89  TYR   A N   
655  C CA  . TYR   A 83  ? 0.3074 0.2206 0.3748 -0.0037 0.0802  -0.0426 89  TYR   A CA  
656  C C   . TYR   A 83  ? 0.2938 0.2086 0.3852 0.0063  0.0806  -0.0317 89  TYR   A C   
657  O O   . TYR   A 83  ? 0.3005 0.2145 0.3936 0.0073  0.0768  -0.0280 89  TYR   A O   
658  C CB  . TYR   A 83  ? 0.3091 0.2350 0.3622 -0.0039 0.0646  -0.0379 89  TYR   A CB  
659  C CG  . TYR   A 83  ? 0.3340 0.2599 0.3649 -0.0140 0.0623  -0.0458 89  TYR   A CG  
660  C CD1 . TYR   A 83  ? 0.3672 0.2917 0.3846 -0.0214 0.0589  -0.0494 89  TYR   A CD1 
661  C CD2 . TYR   A 83  ? 0.3579 0.2867 0.3817 -0.0167 0.0627  -0.0483 89  TYR   A CD2 
662  C CE1 . TYR   A 83  ? 0.3974 0.3246 0.3955 -0.0314 0.0551  -0.0541 89  TYR   A CE1 
663  C CE2 . TYR   A 83  ? 0.3915 0.3216 0.3950 -0.0267 0.0594  -0.0536 89  TYR   A CE2 
664  C CZ  . TYR   A 83  ? 0.4166 0.3464 0.4077 -0.0343 0.0554  -0.0560 89  TYR   A CZ  
665  O OH  . TYR   A 83  ? 0.4456 0.3789 0.4179 -0.0450 0.0510  -0.0591 89  TYR   A OH  
666  N N   . TYR   A 84  ? 0.2859 0.2039 0.3962 0.0132  0.0846  -0.0257 90  TYR   A N   
667  C CA  . TYR   A 84  ? 0.2772 0.1990 0.4122 0.0220  0.0840  -0.0130 90  TYR   A CA  
668  C C   . TYR   A 84  ? 0.2945 0.2110 0.4539 0.0265  0.0979  -0.0122 90  TYR   A C   
669  O O   . TYR   A 84  ? 0.2963 0.2134 0.4537 0.0251  0.1027  -0.0175 90  TYR   A O   
670  C CB  . TYR   A 84  ? 0.2635 0.2021 0.3990 0.0263  0.0694  -0.0010 90  TYR   A CB  
671  C CG  . TYR   A 84  ? 0.2468 0.1914 0.3630 0.0230  0.0566  -0.0004 90  TYR   A CG  
672  C CD1 . TYR   A 84  ? 0.2451 0.1881 0.3624 0.0229  0.0534  0.0033  90  TYR   A CD1 
673  C CD2 . TYR   A 84  ? 0.2326 0.1840 0.3308 0.0198  0.0485  -0.0034 90  TYR   A CD2 
674  C CE1 . TYR   A 84  ? 0.2264 0.1749 0.3279 0.0199  0.0429  0.0035  90  TYR   A CE1 
675  C CE2 . TYR   A 84  ? 0.2200 0.1762 0.3037 0.0171  0.0385  -0.0030 90  TYR   A CE2 
676  C CZ  . TYR   A 84  ? 0.2196 0.1749 0.3055 0.0173  0.0357  0.0006  90  TYR   A CZ  
677  O OH  . TYR   A 84  ? 0.2308 0.1909 0.3039 0.0145  0.0270  0.0005  90  TYR   A OH  
678  N N   . PRO   A 85  ? 0.3018 0.2142 0.4866 0.0325  0.1043  -0.0043 91  PRO   A N   
679  C CA  . PRO   A 85  ? 0.3039 0.2141 0.5183 0.0388  0.1168  0.0000  91  PRO   A CA  
680  C C   . PRO   A 85  ? 0.3015 0.2304 0.5260 0.0445  0.1060  0.0133  91  PRO   A C   
681  O O   . PRO   A 85  ? 0.3036 0.2452 0.5123 0.0433  0.0901  0.0187  91  PRO   A O   
682  C CB  . PRO   A 85  ? 0.3227 0.2265 0.5617 0.0440  0.1224  0.0088  91  PRO   A CB  
683  C CG  . PRO   A 85  ? 0.3349 0.2480 0.5611 0.0434  0.1057  0.0172  91  PRO   A CG  
684  C CD  . PRO   A 85  ? 0.3043 0.2164 0.4949 0.0346  0.0992  0.0040  91  PRO   A CD  
685  N N   . ALA   A 86  ? 0.3042 0.2355 0.5558 0.0504  0.1147  0.0189  92  ALA   A N   
686  C CA  . ALA   A 86  ? 0.2998 0.2500 0.5644 0.0554  0.1050  0.0331  92  ALA   A CA  
687  C C   . ALA   A 86  ? 0.3050 0.2663 0.5808 0.0591  0.0927  0.0509  92  ALA   A C   
688  O O   . ALA   A 86  ? 0.3243 0.2783 0.6180 0.0623  0.0984  0.0563  92  ALA   A O   
689  C CB  . ALA   A 86  ? 0.2840 0.2337 0.5809 0.0613  0.1187  0.0366  92  ALA   A CB  
690  N N   . ARG   A 87  ? 0.2994 0.2768 0.5611 0.0570  0.0763  0.0583  93  ARG   A N   
691  C CA  . ARG   A 87  ? 0.2955 0.2837 0.5608 0.0574  0.0640  0.0732  93  ARG   A CA  
692  C C   . ARG   A 87  ? 0.2894 0.2967 0.5423 0.0540  0.0487  0.0809  93  ARG   A C   
693  O O   . ARG   A 87  ? 0.2918 0.3021 0.5310 0.0516  0.0475  0.0734  93  ARG   A O   
694  C CB  . ARG   A 87  ? 0.3140 0.2913 0.5567 0.0527  0.0616  0.0645  93  ARG   A CB  
695  C CG  . ARG   A 87  ? 0.3460 0.3230 0.5545 0.0461  0.0551  0.0513  93  ARG   A CG  
696  C CD  . ARG   A 87  ? 0.3411 0.3117 0.5295 0.0415  0.0508  0.0452  93  ARG   A CD  
697  N NE  . ARG   A 87  ? 0.3277 0.3033 0.4894 0.0363  0.0420  0.0380  93  ARG   A NE  
698  C CZ  . ARG   A 87  ? 0.3567 0.3314 0.5000 0.0321  0.0354  0.0343  93  ARG   A CZ  
699  N NH1 . ARG   A 87  ? 0.3754 0.3443 0.5214 0.0317  0.0363  0.0360  93  ARG   A NH1 
700  N NH2 . ARG   A 87  ? 0.2866 0.2659 0.4099 0.0282  0.0286  0.0289  93  ARG   A NH2 
701  N N   . TYR   A 88  ? 0.2867 0.3054 0.5408 0.0523  0.0373  0.0945  94  TYR   A N   
702  C CA  . TYR   A 88  ? 0.2814 0.3171 0.5210 0.0467  0.0233  0.1010  94  TYR   A CA  
703  C C   . TYR   A 88  ? 0.2496 0.2800 0.4569 0.0403  0.0175  0.0896  94  TYR   A C   
704  O O   . TYR   A 88  ? 0.2638 0.2874 0.4657 0.0390  0.0168  0.0885  94  TYR   A O   
705  C CB  . TYR   A 88  ? 0.2946 0.3471 0.5528 0.0462  0.0144  0.1224  94  TYR   A CB  
706  C CG  . TYR   A 88  ? 0.3013 0.3653 0.5908 0.0515  0.0170  0.1358  94  TYR   A CG  
707  C CD1 . TYR   A 88  ? 0.3143 0.3923 0.6008 0.0489  0.0121  0.1381  94  TYR   A CD1 
708  C CD2 . TYR   A 88  ? 0.3065 0.3672 0.6302 0.0591  0.0251  0.1465  94  TYR   A CD2 
709  C CE1 . TYR   A 88  ? 0.3148 0.4050 0.6316 0.0536  0.0143  0.1511  94  TYR   A CE1 
710  C CE2 . TYR   A 88  ? 0.3066 0.3789 0.6630 0.0645  0.0280  0.1600  94  TYR   A CE2 
711  C CZ  . TYR   A 88  ? 0.3133 0.4009 0.6659 0.0616  0.0222  0.1624  94  TYR   A CZ  
712  O OH  . TYR   A 88  ? 0.3230 0.4233 0.7089 0.0668  0.0250  0.1760  94  TYR   A OH  
713  N N   . GLN   A 89  ? 0.2142 0.2472 0.4013 0.0365  0.0143  0.0806  95  GLN   A N   
714  C CA  . GLN   A 89  ? 0.1841 0.2133 0.3433 0.0308  0.0092  0.0704  95  GLN   A CA  
715  C C   . GLN   A 89  ? 0.1791 0.2241 0.3300 0.0245  -0.0017 0.0788  95  GLN   A C   
716  O O   . GLN   A 89  ? 0.1889 0.2460 0.3457 0.0235  -0.0047 0.0855  95  GLN   A O   
717  C CB  . GLN   A 89  ? 0.1968 0.2170 0.3400 0.0302  0.0138  0.0553  95  GLN   A CB  
718  C CG  . GLN   A 89  ? 0.2168 0.2335 0.3358 0.0252  0.0089  0.0466  95  GLN   A CG  
719  C CD  . GLN   A 89  ? 0.2158 0.2214 0.3207 0.0245  0.0136  0.0327  95  GLN   A CD  
720  O OE1 . GLN   A 89  ? 0.2429 0.2383 0.3521 0.0264  0.0219  0.0266  95  GLN   A OE1 
721  N NE2 . GLN   A 89  ? 0.2127 0.2201 0.3003 0.0206  0.0086  0.0278  95  GLN   A NE2 
722  N N   . SER   A 90  ? 0.1726 0.2183 0.3107 0.0195  -0.0072 0.0791  96  SER   A N   
723  C CA  . SER   A 90  ? 0.1714 0.2312 0.2998 0.0114  -0.0163 0.0858  96  SER   A CA  
724  C C   . SER   A 90  ? 0.1796 0.2370 0.2844 0.0063  -0.0175 0.0736  96  SER   A C   
725  O O   . SER   A 90  ? 0.1840 0.2291 0.2797 0.0089  -0.0131 0.0614  96  SER   A O   
726  C CB  . SER   A 90  ? 0.1989 0.2618 0.3275 0.0073  -0.0208 0.0937  96  SER   A CB  
727  O OG  . SER   A 90  ? 0.2570 0.3072 0.3715 0.0069  -0.0182 0.0821  96  SER   A OG  
728  N N   . HIS   A 91  ? 0.1710 0.2408 0.2673 -0.0018 -0.0234 0.0779  97  HIS   A N   
729  C CA  . HIS   A 91  ? 0.1761 0.2443 0.2522 -0.0076 -0.0239 0.0677  97  HIS   A CA  
730  C C   . HIS   A 91  ? 0.1639 0.2242 0.2373 -0.0026 -0.0191 0.0580  97  HIS   A C   
731  O O   . HIS   A 91  ? 0.1819 0.2341 0.2419 -0.0036 -0.0172 0.0474  97  HIS   A O   
732  C CB  . HIS   A 91  ? 0.1930 0.2533 0.2561 -0.0109 -0.0235 0.0604  97  HIS   A CB  
733  C CG  . HIS   A 91  ? 0.2083 0.2768 0.2709 -0.0180 -0.0282 0.0693  97  HIS   A CG  
734  N ND1 . HIS   A 91  ? 0.2347 0.3117 0.2837 -0.0295 -0.0313 0.0696  97  HIS   A ND1 
735  C CD2 . HIS   A 91  ? 0.2348 0.3041 0.3083 -0.0160 -0.0296 0.0779  97  HIS   A CD2 
736  C CE1 . HIS   A 91  ? 0.2577 0.3411 0.3085 -0.0348 -0.0353 0.0786  97  HIS   A CE1 
737  N NE2 . HIS   A 91  ? 0.2481 0.3274 0.3143 -0.0265 -0.0348 0.0845  97  HIS   A NE2 
738  N N   . LEU   A 92  ? 0.1496 0.2129 0.2366 0.0023  -0.0171 0.0623  98  LEU   A N   
739  C CA  . LEU   A 92  ? 0.1507 0.2067 0.2356 0.0065  -0.0121 0.0536  98  LEU   A CA  
740  C C   . LEU   A 92  ? 0.1552 0.2216 0.2372 0.0022  -0.0144 0.0558  98  LEU   A C   
741  O O   . LEU   A 92  ? 0.1590 0.2391 0.2502 -0.0008 -0.0184 0.0668  98  LEU   A O   
742  C CB  . LEU   A 92  ? 0.1779 0.2288 0.2807 0.0144  -0.0060 0.0552  98  LEU   A CB  
743  C CG  . LEU   A 92  ? 0.2018 0.2436 0.3012 0.0176  0.0004  0.0450  98  LEU   A CG  
744  C CD1 . LEU   A 92  ? 0.2061 0.2354 0.2897 0.0169  0.0020  0.0338  98  LEU   A CD1 
745  C CD2 . LEU   A 92  ? 0.2305 0.2683 0.3490 0.0237  0.0081  0.0467  98  LEU   A CD2 
746  N N   . MET   A 93  ? 0.1587 0.2189 0.2282 0.0015  -0.0122 0.0461  99  MET   A N   
747  C CA  . MET   A 93  ? 0.1578 0.2255 0.2230 -0.0027 -0.0133 0.0464  99  MET   A CA  
748  C C   . MET   A 93  ? 0.1662 0.2279 0.2351 0.0027  -0.0081 0.0412  99  MET   A C   
749  O O   . MET   A 93  ? 0.1763 0.2258 0.2400 0.0061  -0.0044 0.0332  99  MET   A O   
750  C CB  . MET   A 93  ? 0.1641 0.2285 0.2107 -0.0093 -0.0143 0.0391  99  MET   A CB  
751  C CG  . MET   A 93  ? 0.1803 0.2496 0.2215 -0.0161 -0.0179 0.0424  99  MET   A CG  
752  S SD  . MET   A 93  ? 0.2416 0.3036 0.2639 -0.0232 -0.0158 0.0320  99  MET   A SD  
753  C CE  . MET   A 93  ? 0.3153 0.3610 0.3378 -0.0141 -0.0120 0.0235  99  MET   A CE  
754  N N   . LEU   A 94  ? 0.1494 0.2203 0.2269 0.0025  -0.0078 0.0460  100 LEU   A N   
755  C CA  . LEU   A 94  ? 0.1622 0.2275 0.2431 0.0066  -0.0020 0.0407  100 LEU   A CA  
756  C C   . LEU   A 94  ? 0.1572 0.2243 0.2261 0.0020  -0.0024 0.0364  100 LEU   A C   
757  O O   . LEU   A 94  ? 0.1731 0.2504 0.2380 -0.0042 -0.0068 0.0406  100 LEU   A O   
758  C CB  . LEU   A 94  ? 0.1808 0.2539 0.2849 0.0113  0.0013  0.0488  100 LEU   A CB  
759  C CG  . LEU   A 94  ? 0.2193 0.2884 0.3400 0.0173  0.0048  0.0527  100 LEU   A CG  
760  C CD1 . LEU   A 94  ? 0.2293 0.3041 0.3752 0.0225  0.0107  0.0591  100 LEU   A CD1 
761  C CD2 . LEU   A 94  ? 0.2433 0.2950 0.3552 0.0200  0.0106  0.0413  100 LEU   A CD2 
762  N N   . ALA   A 95  ? 0.1590 0.2164 0.2221 0.0041  0.0022  0.0282  101 ALA   A N   
763  C CA  . ALA   A 95  ? 0.1573 0.2151 0.2106 0.0005  0.0028  0.0243  101 ALA   A CA  
764  C C   . ALA   A 95  ? 0.1539 0.2064 0.2113 0.0037  0.0091  0.0198  101 ALA   A C   
765  O O   . ALA   A 95  ? 0.1530 0.1987 0.2166 0.0079  0.0137  0.0174  101 ALA   A O   
766  C CB  . ALA   A 95  ? 0.1667 0.2151 0.2022 -0.0026 0.0014  0.0174  101 ALA   A CB  
767  N N   . VAL   A 96  ? 0.1516 0.2069 0.2049 0.0009  0.0103  0.0181  102 VAL   A N   
768  C CA  . VAL   A 96  ? 0.1555 0.2053 0.2090 0.0021  0.0166  0.0127  102 VAL   A CA  
769  C C   . VAL   A 96  ? 0.1877 0.2251 0.2231 0.0000  0.0166  0.0050  102 VAL   A C   
770  O O   . VAL   A 96  ? 0.2026 0.2387 0.2262 -0.0036 0.0130  0.0039  102 VAL   A O   
771  C CB  . VAL   A 96  ? 0.1477 0.2070 0.2051 -0.0005 0.0176  0.0150  102 VAL   A CB  
772  C CG1 . VAL   A 96  ? 0.1712 0.2241 0.2261 -0.0007 0.0246  0.0083  102 VAL   A CG1 
773  C CG2 . VAL   A 96  ? 0.1562 0.2303 0.2342 0.0014  0.0165  0.0250  102 VAL   A CG2 
774  N N   . GLY   A 97  ? 0.1828 0.2113 0.2171 0.0015  0.0208  0.0001  103 GLY   A N   
775  C CA  . GLY   A 97  ? 0.2051 0.2237 0.2234 -0.0014 0.0200  -0.0055 103 GLY   A CA  
776  C C   . GLY   A 97  ? 0.2033 0.2138 0.2206 -0.0015 0.0250  -0.0106 103 GLY   A C   
777  O O   . GLY   A 97  ? 0.2243 0.2350 0.2538 0.0015  0.0298  -0.0105 103 GLY   A O   
778  N N   . HIS   A 98  ? 0.2309 0.2344 0.2336 -0.0058 0.0241  -0.0147 104 HIS   A N   
779  C CA  . HIS   A 98  ? 0.2480 0.2442 0.2458 -0.0088 0.0286  -0.0202 104 HIS   A CA  
780  C C   . HIS   A 98  ? 0.2381 0.2311 0.2350 -0.0076 0.0250  -0.0195 104 HIS   A C   
781  O O   . HIS   A 98  ? 0.2360 0.2302 0.2288 -0.0069 0.0179  -0.0160 104 HIS   A O   
782  C CB  . HIS   A 98  ? 0.2721 0.2646 0.2539 -0.0162 0.0285  -0.0236 104 HIS   A CB  
783  C CG  . HIS   A 98  ? 0.2908 0.2768 0.2648 -0.0222 0.0337  -0.0299 104 HIS   A CG  
784  N ND1 . HIS   A 98  ? 0.3142 0.2973 0.2935 -0.0240 0.0445  -0.0361 104 HIS   A ND1 
785  C CD2 . HIS   A 98  ? 0.3131 0.2954 0.2752 -0.0275 0.0300  -0.0308 104 HIS   A CD2 
786  C CE1 . HIS   A 98  ? 0.3190 0.2957 0.2868 -0.0315 0.0476  -0.0418 104 HIS   A CE1 
787  N NE2 . HIS   A 98  ? 0.3278 0.3048 0.2848 -0.0341 0.0383  -0.0382 104 HIS   A NE2 
788  N N   . SER   A 99  ? 0.2431 0.2320 0.2454 -0.0072 0.0308  -0.0230 105 SER   A N   
789  C CA  . SER   A 99  ? 0.2567 0.2421 0.2585 -0.0067 0.0288  -0.0232 105 SER   A CA  
790  C C   . SER   A 99  ? 0.2961 0.2738 0.2953 -0.0117 0.0381  -0.0309 105 SER   A C   
791  O O   . SER   A 99  ? 0.3623 0.3383 0.3662 -0.0128 0.0469  -0.0350 105 SER   A O   
792  C CB  . SER   A 99  ? 0.2898 0.2795 0.3062 0.0002  0.0270  -0.0177 105 SER   A CB  
793  O OG  . SER   A 99  ? 0.3884 0.3808 0.4199 0.0037  0.0335  -0.0164 105 SER   A OG  
794  N N   . GLU   A 100 ? 0.2541 0.2277 0.2419 -0.0170 0.0358  -0.0335 106 GLU   A N   
795  C CA  . GLU   A 100 ? 0.2392 0.2051 0.2214 -0.0238 0.0435  -0.0412 106 GLU   A CA  
796  C C   . GLU   A 100 ? 0.2531 0.2177 0.2378 -0.0217 0.0396  -0.0393 106 GLU   A C   
797  O O   . GLU   A 100 ? 0.2388 0.2087 0.2259 -0.0168 0.0305  -0.0326 106 GLU   A O   
798  C CB  . GLU   A 100 ? 0.2622 0.2266 0.2245 -0.0353 0.0423  -0.0452 106 GLU   A CB  
799  C CG  . GLU   A 100 ? 0.2952 0.2606 0.2543 -0.0380 0.0466  -0.0473 106 GLU   A CG  
800  C CD  . GLU   A 100 ? 0.3730 0.3379 0.3117 -0.0504 0.0450  -0.0500 106 GLU   A CD  
801  O OE1 . GLU   A 100 ? 0.4313 0.3941 0.3579 -0.0592 0.0437  -0.0525 106 GLU   A OE1 
802  O OE2 . GLU   A 100 ? 0.3857 0.3531 0.3201 -0.0522 0.0448  -0.0492 106 GLU   A OE2 
803  N N   . PRO   A 101 ? 0.2594 0.2168 0.2447 -0.0252 0.0472  -0.0453 107 PRO   A N   
804  C CA  . PRO   A 101 ? 0.2492 0.2055 0.2382 -0.0228 0.0438  -0.0432 107 PRO   A CA  
805  C C   . PRO   A 101 ? 0.2589 0.2205 0.2376 -0.0250 0.0319  -0.0386 107 PRO   A C   
806  O O   . PRO   A 101 ? 0.2603 0.2254 0.2460 -0.0189 0.0257  -0.0330 107 PRO   A O   
807  C CB  . PRO   A 101 ? 0.2706 0.2170 0.2570 -0.0298 0.0551  -0.0524 107 PRO   A CB  
808  C CG  . PRO   A 101 ? 0.2907 0.2329 0.2843 -0.0297 0.0669  -0.0573 107 PRO   A CG  
809  C CD  . PRO   A 101 ? 0.2676 0.2167 0.2531 -0.0309 0.0611  -0.0546 107 PRO   A CD  
810  N N   . GLY   A 102 ? 0.2601 0.2233 0.2234 -0.0338 0.0285  -0.0399 108 GLY   A N   
811  C CA  . GLY   A 102 ? 0.2621 0.2313 0.2181 -0.0363 0.0174  -0.0341 108 GLY   A CA  
812  C C   . GLY   A 102 ? 0.2234 0.1990 0.1862 -0.0285 0.0096  -0.0263 108 GLY   A C   
813  O O   . GLY   A 102 ? 0.2304 0.2106 0.1922 -0.0285 0.0016  -0.0208 108 GLY   A O   
814  N N   . ASP   A 103 ? 0.2113 0.1874 0.1815 -0.0224 0.0123  -0.0254 109 ASP   A N   
815  C CA  . ASP   A 103 ? 0.2137 0.1949 0.1898 -0.0160 0.0063  -0.0191 109 ASP   A CA  
816  C C   . ASP   A 103 ? 0.2015 0.1843 0.1881 -0.0095 0.0043  -0.0161 109 ASP   A C   
817  O O   . ASP   A 103 ? 0.1906 0.1770 0.1805 -0.0061 -0.0003 -0.0117 109 ASP   A O   
818  C CB  . ASP   A 103 ? 0.1923 0.1747 0.1716 -0.0134 0.0098  -0.0192 109 ASP   A CB  
819  C CG  . ASP   A 103 ? 0.2275 0.2093 0.1955 -0.0202 0.0103  -0.0209 109 ASP   A CG  
820  O OD1 . ASP   A 103 ? 0.2293 0.2126 0.1892 -0.0246 0.0043  -0.0179 109 ASP   A OD1 
821  O OD2 . ASP   A 103 ? 0.2250 0.2054 0.1933 -0.0212 0.0168  -0.0246 109 ASP   A OD2 
822  N N   . CYS   A 104 ? 0.1946 0.1741 0.1858 -0.0086 0.0082  -0.0186 110 CYS   A N   
823  C CA  . CYS   A 104 ? 0.1888 0.1700 0.1887 -0.0035 0.0058  -0.0153 110 CYS   A CA  
824  C C   . CYS   A 104 ? 0.1933 0.1776 0.1905 -0.0042 -0.0012 -0.0122 110 CYS   A C   
825  O O   . CYS   A 104 ? 0.2025 0.1866 0.1928 -0.0092 -0.0037 -0.0129 110 CYS   A O   
826  C CB  . CYS   A 104 ? 0.1960 0.1723 0.2006 -0.0035 0.0110  -0.0182 110 CYS   A CB  
827  S SG  . CYS   A 104 ? 0.2259 0.1999 0.2432 0.0007  0.0197  -0.0187 110 CYS   A SG  
828  N N   . GLY   A 105 ? 0.1684 0.1560 0.1715 -0.0002 -0.0040 -0.0087 111 GLY   A N   
829  C CA  . GLY   A 105 ? 0.1703 0.1604 0.1740 -0.0002 -0.0087 -0.0060 111 GLY   A CA  
830  C C   . GLY   A 105 ? 0.1691 0.1614 0.1729 0.0005  -0.0107 -0.0034 111 GLY   A C   
831  O O   . GLY   A 105 ? 0.1715 0.1652 0.1795 0.0015  -0.0127 -0.0012 111 GLY   A O   
832  N N   . GLY   A 106 ? 0.1578 0.1497 0.1578 -0.0003 -0.0092 -0.0040 112 GLY   A N   
833  C CA  . GLY   A 106 ? 0.1593 0.1523 0.1593 0.0001  -0.0103 -0.0017 112 GLY   A CA  
834  C C   . GLY   A 106 ? 0.1577 0.1523 0.1628 0.0024  -0.0089 -0.0013 112 GLY   A C   
835  O O   . GLY   A 106 ? 0.1652 0.1616 0.1721 0.0033  -0.0071 -0.0020 112 GLY   A O   
836  N N   . ILE   A 107 ? 0.1621 0.1563 0.1698 0.0025  -0.0092 0.0001  113 ILE   A N   
837  C CA  . ILE   A 107 ? 0.1557 0.1510 0.1662 0.0023  -0.0066 -0.0009 113 ILE   A CA  
838  C C   . ILE   A 107 ? 0.1511 0.1479 0.1582 0.0007  -0.0046 -0.0014 113 ILE   A C   
839  O O   . ILE   A 107 ? 0.1608 0.1559 0.1653 0.0001  -0.0044 -0.0010 113 ILE   A O   
840  C CB  . ILE   A 107 ? 0.1591 0.1521 0.1753 0.0025  -0.0056 -0.0003 113 ILE   A CB  
841  C CG1 . ILE   A 107 ? 0.1822 0.1758 0.2032 0.0036  -0.0070 0.0000  113 ILE   A CG1 
842  C CG2 . ILE   A 107 ? 0.1747 0.1669 0.1917 0.0001  -0.0009 -0.0026 113 ILE   A CG2 
843  C CD1 . ILE   A 107 ? 0.2167 0.2087 0.2474 0.0046  -0.0059 0.0017  113 ILE   A CD1 
844  N N   . LEU   A 108 ? 0.1479 0.1486 0.1551 -0.0009 -0.0034 -0.0017 114 LEU   A N   
845  C CA  . LEU   A 108 ? 0.1470 0.1511 0.1512 -0.0044 -0.0016 -0.0019 114 LEU   A CA  
846  C C   . LEU   A 108 ? 0.1470 0.1497 0.1507 -0.0084 0.0015  -0.0041 114 LEU   A C   
847  O O   . LEU   A 108 ? 0.1607 0.1640 0.1662 -0.0092 0.0017  -0.0046 114 LEU   A O   
848  C CB  . LEU   A 108 ? 0.1524 0.1639 0.1581 -0.0051 -0.0029 0.0008  114 LEU   A CB  
849  C CG  . LEU   A 108 ? 0.1578 0.1760 0.1607 -0.0105 -0.0022 0.0021  114 LEU   A CG  
850  C CD1 . LEU   A 108 ? 0.1727 0.1907 0.1733 -0.0106 -0.0011 0.0015  114 LEU   A CD1 
851  C CD2 . LEU   A 108 ? 0.1774 0.2053 0.1851 -0.0115 -0.0047 0.0076  114 LEU   A CD2 
852  N N   . ARG   A 109 ? 0.1502 0.1499 0.1516 -0.0113 0.0049  -0.0061 115 ARG   A N   
853  C CA  . ARG   A 109 ? 0.1706 0.1669 0.1719 -0.0161 0.0104  -0.0098 115 ARG   A CA  
854  C C   . ARG   A 109 ? 0.1856 0.1835 0.1804 -0.0229 0.0139  -0.0120 115 ARG   A C   
855  O O   . ARG   A 109 ? 0.1726 0.1723 0.1646 -0.0226 0.0124  -0.0105 115 ARG   A O   
856  C CB  . ARG   A 109 ? 0.1919 0.1799 0.2008 -0.0124 0.0132  -0.0104 115 ARG   A CB  
857  C CG  . ARG   A 109 ? 0.1936 0.1778 0.2028 -0.0105 0.0131  -0.0086 115 ARG   A CG  
858  C CD  . ARG   A 109 ? 0.2103 0.1879 0.2298 -0.0069 0.0150  -0.0067 115 ARG   A CD  
859  N NE  . ARG   A 109 ? 0.2227 0.2027 0.2467 -0.0022 0.0091  -0.0024 115 ARG   A NE  
860  C CZ  . ARG   A 109 ? 0.2223 0.2015 0.2556 0.0001  0.0094  -0.0013 115 ARG   A CZ  
861  N NH1 . ARG   A 109 ? 0.2285 0.2044 0.2677 -0.0017 0.0163  -0.0051 115 ARG   A NH1 
862  N NH2 . ARG   A 109 ? 0.2221 0.2043 0.2582 0.0031  0.0035  0.0029  115 ARG   A NH2 
863  N N   . CYS   A 110 ? 0.2007 0.1980 0.1922 -0.0304 0.0192  -0.0161 116 CYS   A N   
864  C CA  . CYS   A 110 ? 0.2545 0.2528 0.2382 -0.0395 0.0239  -0.0195 116 CYS   A CA  
865  C C   . CYS   A 110 ? 0.3025 0.2901 0.2883 -0.0433 0.0338  -0.0261 116 CYS   A C   
866  O O   . CYS   A 110 ? 0.2908 0.2713 0.2865 -0.0373 0.0361  -0.0265 116 CYS   A O   
867  C CB  . CYS   A 110 ? 0.2385 0.2482 0.2146 -0.0481 0.0213  -0.0180 116 CYS   A CB  
868  S SG  . CYS   A 110 ? 0.2428 0.2521 0.2169 -0.0546 0.0250  -0.0216 116 CYS   A SG  
869  N N   . GLN   A 111 ? 0.3341 0.3206 0.3116 -0.0540 0.0406  -0.0313 117 GLN   A N   
870  C CA  . GLN   A 111 ? 0.3639 0.3388 0.3443 -0.0588 0.0526  -0.0390 117 GLN   A CA  
871  C C   . GLN   A 111 ? 0.3690 0.3416 0.3530 -0.0608 0.0572  -0.0427 117 GLN   A C   
872  O O   . GLN   A 111 ? 0.4131 0.3749 0.4058 -0.0608 0.0673  -0.0479 117 GLN   A O   
873  C CB  . GLN   A 111 ? 0.4129 0.3869 0.3815 -0.0724 0.0602  -0.0453 117 GLN   A CB  
874  C CG  . GLN   A 111 ? 0.4602 0.4456 0.4151 -0.0853 0.0586  -0.0467 117 GLN   A CG  
875  C CD  . GLN   A 111 ? 0.5409 0.5276 0.4824 -0.1006 0.0649  -0.0523 117 GLN   A CD  
876  O OE1 . GLN   A 111 ? 0.5590 0.5546 0.4943 -0.1032 0.0590  -0.0481 117 GLN   A OE1 
877  N NE2 . GLN   A 111 ? 0.5449 0.5231 0.4817 -0.1118 0.0777  -0.0622 117 GLN   A NE2 
878  N N   . HIS   A 112 ? 0.3244 0.3070 0.3035 -0.0625 0.0505  -0.0397 118 HIS   A N   
879  C CA  . HIS   A 112 ? 0.3057 0.2871 0.2866 -0.0656 0.0546  -0.0433 118 HIS   A CA  
880  C C   . HIS   A 112 ? 0.2938 0.2729 0.2883 -0.0531 0.0504  -0.0393 118 HIS   A C   
881  O O   . HIS   A 112 ? 0.3140 0.2904 0.3132 -0.0543 0.0552  -0.0426 118 HIS   A O   
882  C CB  . HIS   A 112 ? 0.3013 0.2948 0.2688 -0.0762 0.0500  -0.0418 118 HIS   A CB  
883  C CG  . HIS   A 112 ? 0.3530 0.3511 0.3063 -0.0905 0.0532  -0.0450 118 HIS   A CG  
884  N ND1 . HIS   A 112 ? 0.3653 0.3752 0.3122 -0.0924 0.0443  -0.0381 118 HIS   A ND1 
885  C CD2 . HIS   A 112 ? 0.4109 0.4035 0.3556 -0.1045 0.0650  -0.0545 118 HIS   A CD2 
886  C CE1 . HIS   A 112 ? 0.4198 0.4320 0.3541 -0.1074 0.0498  -0.0429 118 HIS   A CE1 
887  N NE2 . HIS   A 112 ? 0.4401 0.4415 0.3717 -0.1155 0.0627  -0.0534 118 HIS   A NE2 
888  N N   . GLY   A 113 ? 0.2651 0.2463 0.2651 -0.0425 0.0417  -0.0322 119 GLY   A N   
889  C CA  . GLY   A 113 ? 0.2449 0.2256 0.2556 -0.0326 0.0369  -0.0281 119 GLY   A CA  
890  C C   . GLY   A 113 ? 0.2135 0.2016 0.2217 -0.0268 0.0260  -0.0213 119 GLY   A C   
891  O O   . GLY   A 113 ? 0.2095 0.2019 0.2115 -0.0277 0.0223  -0.0190 119 GLY   A O   
892  N N   . VAL   A 114 ? 0.1930 0.1827 0.2065 -0.0216 0.0217  -0.0187 120 VAL   A N   
893  C CA  . VAL   A 114 ? 0.1940 0.1890 0.2062 -0.0164 0.0133  -0.0134 120 VAL   A CA  
894  C C   . VAL   A 114 ? 0.1741 0.1770 0.1792 -0.0210 0.0101  -0.0114 120 VAL   A C   
895  O O   . VAL   A 114 ? 0.1787 0.1838 0.1813 -0.0264 0.0119  -0.0129 120 VAL   A O   
896  C CB  . VAL   A 114 ? 0.1959 0.1895 0.2158 -0.0105 0.0104  -0.0115 120 VAL   A CB  
897  C CG1 . VAL   A 114 ? 0.2031 0.2007 0.2209 -0.0068 0.0037  -0.0075 120 VAL   A CG1 
898  C CG2 . VAL   A 114 ? 0.2197 0.2081 0.2487 -0.0060 0.0117  -0.0105 120 VAL   A CG2 
899  N N   . VAL   A 115 ? 0.1529 0.1606 0.1555 -0.0196 0.0058  -0.0076 121 VAL   A N   
900  C CA  . VAL   A 115 ? 0.1649 0.1816 0.1645 -0.0230 0.0021  -0.0032 121 VAL   A CA  
901  C C   . VAL   A 115 ? 0.1635 0.1821 0.1687 -0.0170 -0.0024 0.0012  121 VAL   A C   
902  O O   . VAL   A 115 ? 0.1793 0.2035 0.1852 -0.0194 -0.0047 0.0050  121 VAL   A O   
903  C CB  . VAL   A 115 ? 0.1851 0.2066 0.1818 -0.0249 0.0011  -0.0011 121 VAL   A CB  
904  C CG1 . VAL   A 115 ? 0.2081 0.2409 0.2061 -0.0272 -0.0035 0.0058  121 VAL   A CG1 
905  C CG2 . VAL   A 115 ? 0.2026 0.2220 0.1927 -0.0324 0.0063  -0.0059 121 VAL   A CG2 
906  N N   . GLY   A 116 ? 0.1610 0.1746 0.1700 -0.0101 -0.0034 0.0009  122 GLY   A N   
907  C CA  . GLY   A 116 ? 0.1752 0.1887 0.1889 -0.0053 -0.0059 0.0035  122 GLY   A CA  
908  C C   . GLY   A 116 ? 0.1572 0.1652 0.1720 -0.0005 -0.0060 0.0017  122 GLY   A C   
909  O O   . GLY   A 116 ? 0.1576 0.1620 0.1703 -0.0005 -0.0051 -0.0005 122 GLY   A O   
910  N N   . ILE   A 117 ? 0.1468 0.1537 0.1647 0.0026  -0.0066 0.0029  123 ILE   A N   
911  C CA  . ILE   A 117 ? 0.1458 0.1478 0.1624 0.0047  -0.0064 0.0006  123 ILE   A CA  
912  C C   . ILE   A 117 ? 0.1506 0.1529 0.1697 0.0063  -0.0044 0.0013  123 ILE   A C   
913  O O   . ILE   A 117 ? 0.1617 0.1671 0.1872 0.0073  -0.0037 0.0044  123 ILE   A O   
914  C CB  . ILE   A 117 ? 0.1629 0.1612 0.1799 0.0052  -0.0073 -0.0009 123 ILE   A CB  
915  C CG1 . ILE   A 117 ? 0.1811 0.1799 0.2023 0.0059  -0.0069 0.0004  123 ILE   A CG1 
916  C CG2 . ILE   A 117 ? 0.1976 0.1953 0.2144 0.0043  -0.0085 -0.0015 123 ILE   A CG2 
917  C CD1 . ILE   A 117 ? 0.1888 0.1836 0.2097 0.0057  -0.0073 -0.0017 123 ILE   A CD1 
918  N N   . VAL   A 118 ? 0.1488 0.1479 0.1641 0.0060  -0.0032 -0.0013 124 VAL   A N   
919  C CA  . VAL   A 118 ? 0.1519 0.1500 0.1701 0.0070  0.0007  -0.0022 124 VAL   A CA  
920  C C   . VAL   A 118 ? 0.1713 0.1659 0.1947 0.0082  0.0033  -0.0029 124 VAL   A C   
921  O O   . VAL   A 118 ? 0.1555 0.1463 0.1750 0.0067  0.0022  -0.0052 124 VAL   A O   
922  C CB  . VAL   A 118 ? 0.1619 0.1563 0.1724 0.0045  0.0020  -0.0059 124 VAL   A CB  
923  C CG1 . VAL   A 118 ? 0.1742 0.1662 0.1878 0.0044  0.0082  -0.0086 124 VAL   A CG1 
924  C CG2 . VAL   A 118 ? 0.1750 0.1719 0.1812 0.0033  0.0000  -0.0048 124 VAL   A CG2 
925  N N   . SER   A 119 ? 0.1608 0.1570 0.1944 0.0107  0.0068  -0.0004 125 SER   A N   
926  C CA  . SER   A 119 ? 0.1720 0.1640 0.2135 0.0123  0.0107  -0.0004 125 SER   A CA  
927  C C   . SER   A 119 ? 0.1885 0.1771 0.2387 0.0138  0.0185  -0.0021 125 SER   A C   
928  O O   . SER   A 119 ? 0.2018 0.1831 0.2557 0.0137  0.0243  -0.0054 125 SER   A O   
929  C CB  . SER   A 119 ? 0.1706 0.1680 0.2202 0.0142  0.0075  0.0065  125 SER   A CB  
930  O OG  . SER   A 119 ? 0.2059 0.1991 0.2652 0.0162  0.0113  0.0080  125 SER   A OG  
931  N N   . THR   A 120 ? 0.1899 0.1838 0.2456 0.0151  0.0199  0.0004  126 THR   A N   
932  C CA  . THR   A 120 ? 0.2039 0.1947 0.2713 0.0170  0.0289  -0.0011 126 THR   A CA  
933  C C   . THR   A 120 ? 0.2040 0.1962 0.2654 0.0147  0.0309  -0.0047 126 THR   A C   
934  O O   . THR   A 120 ? 0.1942 0.1908 0.2450 0.0128  0.0246  -0.0040 126 THR   A O   
935  C CB  . THR   A 120 ? 0.2245 0.2222 0.3126 0.0220  0.0297  0.0084  126 THR   A CB  
936  O OG1 . THR   A 120 ? 0.3409 0.3326 0.4444 0.0246  0.0405  0.0067  126 THR   A OG1 
937  C CG2 . THR   A 120 ? 0.1892 0.1992 0.2802 0.0223  0.0242  0.0154  126 THR   A CG2 
938  N N   . GLY   A 121 ? 0.2251 0.2126 0.2929 0.0146  0.0404  -0.0091 127 GLY   A N   
939  C CA  . GLY   A 121 ? 0.2553 0.2439 0.3178 0.0119  0.0433  -0.0129 127 GLY   A CA  
940  C C   . GLY   A 121 ? 0.2873 0.2720 0.3645 0.0131  0.0557  -0.0161 127 GLY   A C   
941  O O   . GLY   A 121 ? 0.3081 0.2871 0.3979 0.0154  0.0629  -0.0168 127 GLY   A O   
942  N N   . GLY   A 122 ? 0.3098 0.2964 0.3847 0.0109  0.0592  -0.0190 128 GLY   A N   
943  C CA  . GLY   A 122 ? 0.3256 0.3090 0.4146 0.0114  0.0723  -0.0230 128 GLY   A CA  
944  C C   . GLY   A 122 ? 0.3464 0.3416 0.4518 0.0160  0.0716  -0.0153 128 GLY   A C   
945  O O   . GLY   A 122 ? 0.3406 0.3467 0.4496 0.0190  0.0615  -0.0057 128 GLY   A O   
946  N N   . ASN   A 123 ? 0.3538 0.3474 0.4691 0.0153  0.0828  -0.0197 129 ASN   A N   
947  C CA  . ASN   A 123 ? 0.3515 0.3572 0.4843 0.0191  0.0833  -0.0125 129 ASN   A CA  
948  C C   . ASN   A 123 ? 0.3368 0.3519 0.4531 0.0161  0.0713  -0.0092 129 ASN   A C   
949  O O   . ASN   A 123 ? 0.3446 0.3725 0.4733 0.0188  0.0677  -0.0007 129 ASN   A O   
950  C CB  . ASN   A 123 ? 0.3556 0.3706 0.5187 0.0275  0.0827  0.0004  129 ASN   A CB  
951  C CG  . ASN   A 123 ? 0.3855 0.3910 0.5702 0.0313  0.0966  -0.0019 129 ASN   A CG  
952  O OD1 . ASN   A 123 ? 0.3945 0.3886 0.5782 0.0280  0.1103  -0.0134 129 ASN   A OD1 
953  N ND2 . ASN   A 123 ? 0.3892 0.3990 0.5945 0.0376  0.0943  0.0089  129 ASN   A ND2 
954  N N   . GLY   A 124 ? 0.3057 0.3148 0.3955 0.0102  0.0658  -0.0153 130 GLY   A N   
955  C CA  . GLY   A 124 ? 0.2652 0.2807 0.3400 0.0073  0.0559  -0.0127 130 GLY   A CA  
956  C C   . GLY   A 124 ? 0.2212 0.2449 0.2964 0.0098  0.0445  -0.0038 130 GLY   A C   
957  O O   . GLY   A 124 ? 0.2111 0.2415 0.2790 0.0078  0.0379  -0.0006 130 GLY   A O   
958  N N   . LEU   A 125 ? 0.1948 0.2169 0.2770 0.0132  0.0430  -0.0007 131 LEU   A N   
959  C CA  . LEU   A 125 ? 0.1897 0.2184 0.2714 0.0144  0.0334  0.0069  131 LEU   A CA  
960  C C   . LEU   A 125 ? 0.2024 0.2219 0.2698 0.0129  0.0301  0.0026  131 LEU   A C   
961  O O   . LEU   A 125 ? 0.2323 0.2417 0.2964 0.0122  0.0357  -0.0040 131 LEU   A O   
962  C CB  . LEU   A 125 ? 0.1983 0.2348 0.3035 0.0195  0.0340  0.0165  131 LEU   A CB  
963  C CG  . LEU   A 125 ? 0.2114 0.2594 0.3361 0.0215  0.0372  0.0230  131 LEU   A CG  
964  C CD1 . LEU   A 125 ? 0.2285 0.2802 0.3808 0.0274  0.0419  0.0311  131 LEU   A CD1 
965  C CD2 . LEU   A 125 ? 0.2042 0.2657 0.3243 0.0180  0.0281  0.0299  131 LEU   A CD2 
966  N N   . VAL   A 126 ? 0.1654 0.1888 0.2253 0.0118  0.0218  0.0062  132 VAL   A N   
967  C CA  . VAL   A 126 ? 0.1678 0.1846 0.2174 0.0109  0.0181  0.0037  132 VAL   A CA  
968  C C   . VAL   A 126 ? 0.1578 0.1811 0.2144 0.0124  0.0131  0.0109  132 VAL   A C   
969  O O   . VAL   A 126 ? 0.1617 0.1948 0.2210 0.0110  0.0092  0.0167  132 VAL   A O   
970  C CB  . VAL   A 126 ? 0.1830 0.1960 0.2150 0.0070  0.0142  -0.0003 132 VAL   A CB  
971  C CG1 . VAL   A 126 ? 0.1851 0.2052 0.2138 0.0049  0.0102  0.0029  132 VAL   A CG1 
972  C CG2 . VAL   A 126 ? 0.1784 0.1861 0.2032 0.0065  0.0105  -0.0018 132 VAL   A CG2 
973  N N   . GLY   A 127 ? 0.1613 0.1799 0.2205 0.0141  0.0133  0.0109  133 GLY   A N   
974  C CA  . GLY   A 127 ? 0.1513 0.1758 0.2158 0.0145  0.0085  0.0178  133 GLY   A CA  
975  C C   . GLY   A 127 ? 0.1695 0.1892 0.2213 0.0123  0.0046  0.0143  133 GLY   A C   
976  O O   . GLY   A 127 ? 0.1855 0.1963 0.2304 0.0122  0.0064  0.0082  133 GLY   A O   
977  N N   . PHE   A 128 ? 0.1483 0.1744 0.1973 0.0095  -0.0005 0.0184  134 PHE   A N   
978  C CA  . PHE   A 128 ? 0.1521 0.1743 0.1911 0.0072  -0.0032 0.0152  134 PHE   A CA  
979  C C   . PHE   A 128 ? 0.1658 0.1915 0.2095 0.0064  -0.0056 0.0202  134 PHE   A C   
980  O O   . PHE   A 128 ? 0.1647 0.1999 0.2142 0.0044  -0.0080 0.0275  134 PHE   A O   
981  C CB  . PHE   A 128 ? 0.1660 0.1909 0.1957 0.0028  -0.0052 0.0137  134 PHE   A CB  
982  C CG  . PHE   A 128 ? 0.1650 0.1878 0.1902 0.0027  -0.0034 0.0103  134 PHE   A CG  
983  C CD1 . PHE   A 128 ? 0.1738 0.1884 0.1923 0.0034  -0.0024 0.0050  134 PHE   A CD1 
984  C CD2 . PHE   A 128 ? 0.1690 0.1990 0.1972 0.0013  -0.0030 0.0133  134 PHE   A CD2 
985  C CE1 . PHE   A 128 ? 0.1620 0.1749 0.1759 0.0025  -0.0011 0.0028  134 PHE   A CE1 
986  C CE2 . PHE   A 128 ? 0.1679 0.1956 0.1912 0.0007  -0.0012 0.0100  134 PHE   A CE2 
987  C CZ  . PHE   A 128 ? 0.1741 0.1928 0.1900 0.0014  -0.0001 0.0047  134 PHE   A CZ  
988  N N   . ALA   A 129 ? 0.1499 0.1690 0.1906 0.0071  -0.0055 0.0169  135 ALA   A N   
989  C CA  . ALA   A 129 ? 0.1516 0.1731 0.1944 0.0055  -0.0077 0.0207  135 ALA   A CA  
990  C C   . ALA   A 129 ? 0.1595 0.1846 0.1931 -0.0003 -0.0101 0.0195  135 ALA   A C   
991  O O   . ALA   A 129 ? 0.1670 0.1867 0.1938 -0.0008 -0.0091 0.0134  135 ALA   A O   
992  C CB  . ALA   A 129 ? 0.1566 0.1696 0.1991 0.0077  -0.0061 0.0167  135 ALA   A CB  
993  N N   . ASP   A 130 ? 0.1511 0.1855 0.1852 -0.0053 -0.0127 0.0255  136 ASP   A N   
994  C CA  . ASP   A 130 ? 0.1683 0.2057 0.1926 -0.0128 -0.0132 0.0233  136 ASP   A CA  
995  C C   . ASP   A 130 ? 0.1612 0.1937 0.1820 -0.0144 -0.0124 0.0197  136 ASP   A C   
996  O O   . ASP   A 130 ? 0.1819 0.2138 0.2078 -0.0123 -0.0136 0.0230  136 ASP   A O   
997  C CB  . ASP   A 130 ? 0.1960 0.2463 0.2207 -0.0201 -0.0168 0.0318  136 ASP   A CB  
998  C CG  . ASP   A 130 ? 0.2485 0.3024 0.2610 -0.0307 -0.0161 0.0286  136 ASP   A CG  
999  O OD1 . ASP   A 130 ? 0.2302 0.2798 0.2363 -0.0323 -0.0128 0.0217  136 ASP   A OD1 
1000 O OD2 . ASP   A 130 ? 0.3030 0.3634 0.3123 -0.0382 -0.0184 0.0329  136 ASP   A OD2 
1001 N N   . VAL   A 131 ? 0.1706 0.1999 0.1837 -0.0187 -0.0097 0.0133  137 VAL   A N   
1002 C CA  . VAL   A 131 ? 0.1744 0.2004 0.1850 -0.0214 -0.0079 0.0097  137 VAL   A CA  
1003 C C   . VAL   A 131 ? 0.1781 0.2077 0.1802 -0.0320 -0.0052 0.0072  137 VAL   A C   
1004 O O   . VAL   A 131 ? 0.1834 0.2102 0.1834 -0.0355 -0.0023 0.0033  137 VAL   A O   
1005 C CB  . VAL   A 131 ? 0.1677 0.1846 0.1808 -0.0158 -0.0053 0.0036  137 VAL   A CB  
1006 C CG1 . VAL   A 131 ? 0.1736 0.1870 0.1923 -0.0082 -0.0074 0.0052  137 VAL   A CG1 
1007 C CG2 . VAL   A 131 ? 0.1801 0.1934 0.1910 -0.0164 -0.0018 -0.0012 137 VAL   A CG2 
1008 N N   . ARG   A 132 ? 0.1786 0.2144 0.1756 -0.0381 -0.0055 0.0088  138 ARG   A N   
1009 C CA  . ARG   A 132 ? 0.1817 0.2202 0.1685 -0.0502 -0.0016 0.0049  138 ARG   A CA  
1010 C C   . ARG   A 132 ? 0.2113 0.2568 0.1927 -0.0597 -0.0033 0.0085  138 ARG   A C   
1011 O O   . ARG   A 132 ? 0.2250 0.2703 0.1971 -0.0705 0.0019  0.0028  138 ARG   A O   
1012 C CB  . ARG   A 132 ? 0.1856 0.2300 0.1673 -0.0557 -0.0019 0.0062  138 ARG   A CB  
1013 C CG  . ARG   A 132 ? 0.1881 0.2241 0.1727 -0.0485 0.0014  0.0010  138 ARG   A CG  
1014 C CD  . ARG   A 132 ? 0.2097 0.2522 0.1890 -0.0546 0.0009  0.0025  138 ARG   A CD  
1015 N NE  . ARG   A 132 ? 0.1975 0.2502 0.1829 -0.0511 -0.0063 0.0125  138 ARG   A NE  
1016 C CZ  . ARG   A 132 ? 0.2283 0.2891 0.2128 -0.0543 -0.0084 0.0164  138 ARG   A CZ  
1017 N NH1 . ARG   A 132 ? 0.2314 0.2914 0.2067 -0.0624 -0.0043 0.0110  138 ARG   A NH1 
1018 N NH2 . ARG   A 132 ? 0.2348 0.3042 0.2289 -0.0496 -0.0139 0.0256  138 ARG   A NH2 
1019 N N   . ASP   A 133 ? 0.1984 0.2497 0.1858 -0.0565 -0.0096 0.0177  139 ASP   A N   
1020 C CA  . ASP   A 133 ? 0.2103 0.2688 0.1930 -0.0658 -0.0121 0.0228  139 ASP   A CA  
1021 C C   . ASP   A 133 ? 0.2056 0.2562 0.1898 -0.0631 -0.0092 0.0180  139 ASP   A C   
1022 O O   . ASP   A 133 ? 0.2363 0.2915 0.2152 -0.0717 -0.0101 0.0208  139 ASP   A O   
1023 C CB  . ASP   A 133 ? 0.2195 0.2887 0.2107 -0.0636 -0.0204 0.0370  139 ASP   A CB  
1024 C CG  . ASP   A 133 ? 0.2564 0.3186 0.2615 -0.0494 -0.0216 0.0395  139 ASP   A CG  
1025 O OD1 . ASP   A 133 ? 0.2432 0.2963 0.2521 -0.0403 -0.0184 0.0328  139 ASP   A OD1 
1026 O OD2 . ASP   A 133 ? 0.2887 0.3543 0.3005 -0.0483 -0.0253 0.0480  139 ASP   A OD2 
1027 N N   . LEU   A 134 ? 0.1895 0.2294 0.1804 -0.0526 -0.0060 0.0117  140 LEU   A N   
1028 C CA  . LEU   A 134 ? 0.1854 0.2188 0.1796 -0.0494 -0.0037 0.0079  140 LEU   A CA  
1029 C C   . LEU   A 134 ? 0.2137 0.2425 0.2026 -0.0560 0.0043  -0.0020 140 LEU   A C   
1030 O O   . LEU   A 134 ? 0.2179 0.2391 0.2124 -0.0500 0.0087  -0.0084 140 LEU   A O   
1031 C CB  . LEU   A 134 ? 0.1876 0.2138 0.1918 -0.0364 -0.0048 0.0070  140 LEU   A CB  
1032 C CG  . LEU   A 134 ? 0.1965 0.2249 0.2075 -0.0297 -0.0101 0.0150  140 LEU   A CG  
1033 C CD1 . LEU   A 134 ? 0.2003 0.2209 0.2178 -0.0197 -0.0095 0.0119  140 LEU   A CD1 
1034 C CD2 . LEU   A 134 ? 0.2210 0.2539 0.2345 -0.0320 -0.0136 0.0229  140 LEU   A CD2 
1035 N N   . LEU   A 135 ? 0.2065 0.2405 0.1851 -0.0692 0.0065  -0.0029 141 LEU   A N   
1036 C CA  . LEU   A 135 ? 0.2241 0.2532 0.1971 -0.0776 0.0165  -0.0135 141 LEU   A CA  
1037 C C   . LEU   A 135 ? 0.2299 0.2516 0.2106 -0.0731 0.0218  -0.0196 141 LEU   A C   
1038 O O   . LEU   A 135 ? 0.2512 0.2660 0.2352 -0.0741 0.0310  -0.0285 141 LEU   A O   
1039 C CB  . LEU   A 135 ? 0.2404 0.2773 0.1981 -0.0956 0.0183  -0.0136 141 LEU   A CB  
1040 C CG  . LEU   A 135 ? 0.2677 0.3157 0.2180 -0.1022 0.0115  -0.0053 141 LEU   A CG  
1041 C CD1 . LEU   A 135 ? 0.2851 0.3410 0.2185 -0.1226 0.0142  -0.0064 141 LEU   A CD1 
1042 C CD2 . LEU   A 135 ? 0.2953 0.3400 0.2474 -0.0979 0.0137  -0.0085 141 LEU   A CD2 
1043 N N   . TRP   A 136 ? 0.2058 0.2286 0.1910 -0.0680 0.0164  -0.0145 142 TRP   A N   
1044 C CA  . TRP   A 136 ? 0.2116 0.2288 0.2047 -0.0639 0.0205  -0.0192 142 TRP   A CA  
1045 C C   . TRP   A 136 ? 0.2120 0.2225 0.2179 -0.0523 0.0224  -0.0225 142 TRP   A C   
1046 O O   . TRP   A 136 ? 0.2234 0.2302 0.2378 -0.0499 0.0271  -0.0269 142 TRP   A O   
1047 C CB  . TRP   A 136 ? 0.2157 0.2356 0.2099 -0.0619 0.0142  -0.0127 142 TRP   A CB  
1048 C CG  . TRP   A 136 ? 0.2043 0.2254 0.2035 -0.0525 0.0058  -0.0044 142 TRP   A CG  
1049 C CD1 . TRP   A 136 ? 0.2103 0.2377 0.2062 -0.0544 -0.0005 0.0046  142 TRP   A CD1 
1050 C CD2 . TRP   A 136 ? 0.2057 0.2217 0.2146 -0.0407 0.0037  -0.0043 142 TRP   A CD2 
1051 N NE1 . TRP   A 136 ? 0.2230 0.2482 0.2274 -0.0438 -0.0050 0.0093  142 TRP   A NE1 
1052 C CE2 . TRP   A 136 ? 0.2147 0.2327 0.2253 -0.0362 -0.0025 0.0034  142 TRP   A CE2 
1053 C CE3 . TRP   A 136 ? 0.2170 0.2278 0.2341 -0.0345 0.0064  -0.0094 142 TRP   A CE3 
1054 C CZ2 . TRP   A 136 ? 0.2298 0.2434 0.2475 -0.0267 -0.0048 0.0042  142 TRP   A CZ2 
1055 C CZ3 . TRP   A 136 ? 0.2284 0.2366 0.2516 -0.0257 0.0024  -0.0071 142 TRP   A CZ3 
1056 C CH2 . TRP   A 136 ? 0.2243 0.2332 0.2466 -0.0224 -0.0025 -0.0013 142 TRP   A CH2 
1057 N N   . LEU   A 137 ? 0.2078 0.2177 0.2161 -0.0455 0.0187  -0.0196 143 LEU   A N   
1058 C CA  . LEU   A 137 ? 0.2213 0.2259 0.2409 -0.0360 0.0200  -0.0215 143 LEU   A CA  
1059 C C   . LEU   A 137 ? 0.2550 0.2548 0.2802 -0.0389 0.0301  -0.0290 143 LEU   A C   
1060 O O   . LEU   A 137 ? 0.2635 0.2599 0.3018 -0.0319 0.0321  -0.0297 143 LEU   A O   
1061 C CB  . LEU   A 137 ? 0.2094 0.2143 0.2285 -0.0303 0.0149  -0.0175 143 LEU   A CB  
1062 C CG  . LEU   A 137 ? 0.2125 0.2199 0.2312 -0.0250 0.0069  -0.0110 143 LEU   A CG  
1063 C CD1 . LEU   A 137 ? 0.2227 0.2310 0.2396 -0.0220 0.0041  -0.0083 143 LEU   A CD1 
1064 C CD2 . LEU   A 137 ? 0.2175 0.2223 0.2442 -0.0183 0.0048  -0.0106 143 LEU   A CD2 
1065 N N   . ASP   A 138 ? 0.2741 0.2738 0.2903 -0.0499 0.0371  -0.0341 144 ASP   A N   
1066 C CA  . ASP   A 138 ? 0.3047 0.2982 0.3259 -0.0543 0.0494  -0.0426 144 ASP   A CA  
1067 C C   . ASP   A 138 ? 0.3553 0.3463 0.3838 -0.0576 0.0579  -0.0485 144 ASP   A C   
1068 O O   . ASP   A 138 ? 0.3681 0.3529 0.4032 -0.0613 0.0701  -0.0562 144 ASP   A O   
1069 C CB  . ASP   A 138 ? 0.3304 0.3245 0.3369 -0.0670 0.0546  -0.0471 144 ASP   A CB  
1070 C CG  . ASP   A 138 ? 0.3688 0.3650 0.3698 -0.0650 0.0489  -0.0428 144 ASP   A CG  
1071 O OD1 . ASP   A 138 ? 0.3585 0.3536 0.3683 -0.0532 0.0430  -0.0378 144 ASP   A OD1 
1072 O OD2 . ASP   A 138 ? 0.4396 0.4394 0.4268 -0.0761 0.0502  -0.0442 144 ASP   A OD2 
1073 N N   . GLU   A 139 ? 0.3800 0.3749 0.4078 -0.0569 0.0528  -0.0455 145 GLU   A N   
1074 C CA  . GLU   A 139 ? 0.4215 0.4147 0.4557 -0.0609 0.0611  -0.0512 145 GLU   A CA  
1075 C C   . GLU   A 139 ? 0.4500 0.4462 0.4925 -0.0532 0.0541  -0.0461 145 GLU   A C   
1076 O O   . GLU   A 139 ? 0.4430 0.4421 0.4842 -0.0462 0.0432  -0.0387 145 GLU   A O   
1077 C CB  . GLU   A 139 ? 0.4666 0.4622 0.4833 -0.0767 0.0657  -0.0558 145 GLU   A CB  
1078 C CG  . GLU   A 139 ? 0.5427 0.5458 0.5466 -0.0794 0.0541  -0.0477 145 GLU   A CG  
1079 C CD  . GLU   A 139 ? 0.6400 0.6488 0.6250 -0.0921 0.0517  -0.0457 145 GLU   A CD  
1080 O OE1 . GLU   A 139 ? 0.6420 0.6576 0.6178 -0.0968 0.0440  -0.0388 145 GLU   A OE1 
1081 O OE2 . GLU   A 139 ? 0.6867 0.6936 0.6667 -0.0976 0.0573  -0.0502 145 GLU   A OE2 
1082 N N   . GLU   A 140 ? 0.4797 0.4750 0.5307 -0.0555 0.0612  -0.0508 146 GLU   A N   
1083 C CA  . GLU   A 140 ? 0.5165 0.5151 0.5740 -0.0510 0.0559  -0.0472 146 GLU   A CA  
1084 C C   . GLU   A 140 ? 0.5410 0.5413 0.6091 -0.0385 0.0464  -0.0397 146 GLU   A C   
1085 O O   . GLU   A 140 ? 0.5536 0.5566 0.6313 -0.0341 0.0435  -0.0373 146 GLU   A O   
1086 C CB  . GLU   A 140 ? 0.5691 0.5715 0.6093 -0.0588 0.0505  -0.0448 146 GLU   A CB  
1087 C CG  . GLU   A 140 ? 0.6699 0.6754 0.7097 -0.0528 0.0396  -0.0372 146 GLU   A CG  
1088 C CD  . GLU   A 140 ? 0.7814 0.7882 0.8258 -0.0546 0.0413  -0.0386 146 GLU   A CD  
1089 O OE1 . GLU   A 140 ? 0.8173 0.8261 0.8532 -0.0569 0.0353  -0.0343 146 GLU   A OE1 
1090 O OE2 . GLU   A 140 ? 0.8086 0.8146 0.8666 -0.0536 0.0490  -0.0436 146 GLU   A OE2 
1091 N N   . SER   B 1   ? 0.2380 0.2492 0.2553 0.0092  -0.0171 0.0416  7   SER   C N   
1092 C CA  . SER   B 1   ? 0.2298 0.2431 0.2564 0.0073  -0.0184 0.0415  7   SER   C CA  
1093 C C   . SER   B 1   ? 0.2329 0.2447 0.2606 0.0050  -0.0187 0.0372  7   SER   C C   
1094 O O   . SER   B 1   ? 0.2560 0.2655 0.2769 0.0047  -0.0193 0.0344  7   SER   C O   
1095 C CB  . SER   B 1   ? 0.2614 0.2774 0.2886 0.0079  -0.0238 0.0433  7   SER   C CB  
1096 O OG  . SER   B 1   ? 0.3256 0.3406 0.3455 0.0074  -0.0284 0.0401  7   SER   C OG  
1097 N N   . GLY   B 2   ? 0.2229 0.2357 0.2590 0.0038  -0.0177 0.0373  8   GLY   C N   
1098 C CA  . GLY   B 2   ? 0.2159 0.2268 0.2530 0.0023  -0.0170 0.0343  8   GLY   C CA  
1099 C C   . GLY   B 2   ? 0.1975 0.2079 0.2411 0.0023  -0.0131 0.0345  8   GLY   C C   
1100 O O   . GLY   B 2   ? 0.2083 0.2191 0.2544 0.0032  -0.0105 0.0355  8   GLY   C O   
1101 N N   . ALA   B 3   ? 0.1942 0.2034 0.2405 0.0014  -0.0122 0.0335  9   ALA   C N   
1102 C CA  . ALA   B 3   ? 0.1919 0.1998 0.2427 0.0021  -0.0080 0.0337  9   ALA   C CA  
1103 C C   . ALA   B 3   ? 0.1750 0.1793 0.2222 0.0024  -0.0060 0.0317  9   ALA   C C   
1104 O O   . ALA   B 3   ? 0.1960 0.1991 0.2401 0.0014  -0.0079 0.0306  9   ALA   C O   
1105 C CB  . ALA   B 3   ? 0.2124 0.2229 0.2735 0.0016  -0.0078 0.0368  9   ALA   C CB  
1106 N N   . ILE   B 4   ? 0.1725 0.1744 0.2195 0.0041  -0.0019 0.0313  10  ILE   C N   
1107 C CA  . ILE   B 4   ? 0.1778 0.1757 0.2212 0.0053  0.0011  0.0305  10  ILE   C CA  
1108 C C   . ILE   B 4   ? 0.1826 0.1803 0.2345 0.0055  0.0048  0.0333  10  ILE   C C   
1109 O O   . ILE   B 4   ? 0.1999 0.1990 0.2567 0.0061  0.0064  0.0345  10  ILE   C O   
1110 C CB  . ILE   B 4   ? 0.1845 0.1795 0.2201 0.0082  0.0030  0.0278  10  ILE   C CB  
1111 C CG1 . ILE   B 4   ? 0.2110 0.2072 0.2416 0.0080  -0.0002 0.0252  10  ILE   C CG1 
1112 C CG2 . ILE   B 4   ? 0.2069 0.1973 0.2369 0.0104  0.0063  0.0278  10  ILE   C CG2 
1113 C CD1 . ILE   B 4   ? 0.2026 0.1973 0.2288 0.0107  0.0006  0.0220  10  ILE   C CD1 
1114 N N   . TYR   B 5   ? 0.1764 0.1724 0.2314 0.0050  0.0066  0.0346  11  TYR   C N   
1115 C CA  . TYR   B 5   ? 0.1844 0.1799 0.2488 0.0052  0.0109  0.0376  11  TYR   C CA  
1116 C C   . TYR   B 5   ? 0.1957 0.1854 0.2544 0.0082  0.0171  0.0381  11  TYR   C C   
1117 O O   . TYR   B 5   ? 0.2069 0.1940 0.2641 0.0079  0.0178  0.0383  11  TYR   C O   
1118 C CB  . TYR   B 5   ? 0.1915 0.1902 0.2675 0.0019  0.0080  0.0391  11  TYR   C CB  
1119 C CG  . TYR   B 5   ? 0.1893 0.1937 0.2701 0.0000  0.0020  0.0391  11  TYR   C CG  
1120 C CD1 . TYR   B 5   ? 0.1915 0.1994 0.2815 0.0002  0.0026  0.0416  11  TYR   C CD1 
1121 C CD2 . TYR   B 5   ? 0.2039 0.2099 0.2790 -0.0014 -0.0040 0.0369  11  TYR   C CD2 
1122 C CE1 . TYR   B 5   ? 0.2203 0.2330 0.3134 -0.0007 -0.0027 0.0423  11  TYR   C CE1 
1123 C CE2 . TYR   B 5   ? 0.2229 0.2333 0.3000 -0.0021 -0.0090 0.0375  11  TYR   C CE2 
1124 C CZ  . TYR   B 5   ? 0.2287 0.2426 0.3148 -0.0017 -0.0085 0.0403  11  TYR   C CZ  
1125 O OH  . TYR   B 5   ? 0.2581 0.2762 0.3456 -0.0018 -0.0133 0.0415  11  TYR   C OH  
1126 N N   . VAL   B 6   ? 0.2073 0.1942 0.2614 0.0116  0.0216  0.0382  12  VAL   C N   
1127 C CA  . VAL   B 6   ? 0.2319 0.2125 0.2777 0.0158  0.0277  0.0389  12  VAL   C CA  
1128 C C   . VAL   B 6   ? 0.2484 0.2271 0.3000 0.0179  0.0345  0.0419  12  VAL   C C   
1129 O O   . VAL   B 6   ? 0.2260 0.2066 0.2804 0.0181  0.0343  0.0413  12  VAL   C O   
1130 C CB  . VAL   B 6   ? 0.2551 0.2332 0.2859 0.0190  0.0258  0.0350  12  VAL   C CB  
1131 C CG1 . VAL   B 6   ? 0.2657 0.2463 0.2966 0.0191  0.0234  0.0323  12  VAL   C CG1 
1132 C CG2 . VAL   B 6   ? 0.2760 0.2475 0.2961 0.0243  0.0315  0.0357  12  VAL   C CG2 
1133 N N   . GLY   B 7   ? 0.2443 0.2193 0.2996 0.0194  0.0410  0.0455  13  GLY   C N   
1134 C CA  . GLY   B 7   ? 0.2529 0.2259 0.3147 0.0217  0.0487  0.0490  13  GLY   C CA  
1135 C C   . GLY   B 7   ? 0.2473 0.2266 0.3254 0.0180  0.0465  0.0503  13  GLY   C C   
1136 O O   . GLY   B 7   ? 0.2581 0.2426 0.3465 0.0136  0.0410  0.0504  13  GLY   C O   
1137 N N   . ASN   B 8   ? 0.2399 0.2188 0.3188 0.0201  0.0495  0.0505  14  ASN   C N   
1138 C CA  . ASN   B 8   ? 0.2371 0.2222 0.3310 0.0172  0.0471  0.0519  14  ASN   C CA  
1139 C C   . ASN   B 8   ? 0.2257 0.2138 0.3147 0.0163  0.0408  0.0483  14  ASN   C C   
1140 O O   . ASN   B 8   ? 0.2237 0.2141 0.3199 0.0164  0.0414  0.0492  14  ASN   C O   
1141 C CB  . ASN   B 8   ? 0.2696 0.2531 0.3732 0.0196  0.0554  0.0556  14  ASN   C CB  
1142 C CG  . ASN   B 8   ? 0.3495 0.3330 0.4665 0.0187  0.0604  0.0601  14  ASN   C CG  
1143 O OD1 . ASN   B 8   ? 0.3588 0.3485 0.4936 0.0149  0.0573  0.0621  14  ASN   C OD1 
1144 N ND2 . ASN   B 8   ? 0.3871 0.3637 0.4960 0.0222  0.0677  0.0616  14  ASN   C ND2 
1145 N N   . TYR   B 9   ? 0.2072 0.1953 0.2852 0.0155  0.0352  0.0447  15  TYR   C N   
1146 C CA  . TYR   B 9   ? 0.1982 0.1888 0.2723 0.0147  0.0299  0.0416  15  TYR   C CA  
1147 C C   . TYR   B 9   ? 0.1843 0.1796 0.2598 0.0110  0.0225  0.0410  15  TYR   C C   
1148 O O   . TYR   B 9   ? 0.1996 0.1943 0.2723 0.0099  0.0209  0.0407  15  TYR   C O   
1149 C CB  . TYR   B 9   ? 0.2197 0.2055 0.2785 0.0179  0.0302  0.0371  15  TYR   C CB  
1150 C CG  . TYR   B 9   ? 0.2513 0.2314 0.3046 0.0225  0.0369  0.0365  15  TYR   C CG  
1151 C CD1 . TYR   B 9   ? 0.2710 0.2513 0.3310 0.0233  0.0398  0.0370  15  TYR   C CD1 
1152 C CD2 . TYR   B 9   ? 0.2869 0.2612 0.3278 0.0265  0.0404  0.0356  15  TYR   C CD2 
1153 C CE1 . TYR   B 9   ? 0.3156 0.2899 0.3693 0.0279  0.0462  0.0360  15  TYR   C CE1 
1154 C CE2 . TYR   B 9   ? 0.3202 0.2885 0.3537 0.0316  0.0465  0.0349  15  TYR   C CE2 
1155 C CZ  . TYR   B 9   ? 0.3527 0.3209 0.3924 0.0322  0.0493  0.0347  15  TYR   C CZ  
1156 O OH  . TYR   B 9   ? 0.4245 0.3863 0.4560 0.0376  0.0557  0.0336  15  TYR   C OH  
1157 N N   . ARG   B 10  ? 0.1821 0.1813 0.2610 0.0096  0.0186  0.0407  16  ARG   C N   
1158 C CA  . ARG   B 10  ? 0.1726 0.1755 0.2504 0.0071  0.0121  0.0400  16  ARG   C CA  
1159 C C   . ARG   B 10  ? 0.1704 0.1725 0.2411 0.0080  0.0109  0.0370  16  ARG   C C   
1160 O O   . ARG   B 10  ? 0.1744 0.1765 0.2489 0.0090  0.0128  0.0372  16  ARG   C O   
1161 C CB  . ARG   B 10  ? 0.1831 0.1916 0.2726 0.0052  0.0090  0.0434  16  ARG   C CB  
1162 C CG  . ARG   B 10  ? 0.2071 0.2190 0.2941 0.0039  0.0031  0.0432  16  ARG   C CG  
1163 C CD  . ARG   B 10  ? 0.1852 0.2023 0.2822 0.0028  -0.0007 0.0465  16  ARG   C CD  
1164 N NE  . ARG   B 10  ? 0.2088 0.2284 0.3044 0.0034  -0.0035 0.0479  16  ARG   C NE  
1165 C CZ  . ARG   B 10  ? 0.2266 0.2479 0.3165 0.0030  -0.0086 0.0477  16  ARG   C CZ  
1166 N NH1 . ARG   B 10  ? 0.2466 0.2674 0.3313 0.0016  -0.0119 0.0454  16  ARG   C NH1 
1167 N NH2 . ARG   B 10  ? 0.2122 0.2350 0.3008 0.0043  -0.0097 0.0499  16  ARG   C NH2 
1168 N N   . VAL   B 11  ? 0.1531 0.1542 0.2149 0.0078  0.0081  0.0342  17  VAL   C N   
1169 C CA  . VAL   B 11  ? 0.1690 0.1697 0.2263 0.0084  0.0069  0.0311  17  VAL   C CA  
1170 C C   . VAL   B 11  ? 0.1654 0.1695 0.2237 0.0066  0.0030  0.0322  17  VAL   C C   
1171 O O   . VAL   B 11  ? 0.1682 0.1731 0.2227 0.0054  0.0002  0.0323  17  VAL   C O   
1172 C CB  . VAL   B 11  ? 0.1955 0.1928 0.2425 0.0101  0.0068  0.0272  17  VAL   C CB  
1173 C CG1 . VAL   B 11  ? 0.2107 0.2080 0.2559 0.0108  0.0054  0.0235  17  VAL   C CG1 
1174 C CG2 . VAL   B 11  ? 0.2072 0.2002 0.2502 0.0129  0.0110  0.0267  17  VAL   C CG2 
1175 N N   . VAL   B 12  ? 0.1620 0.1678 0.2250 0.0065  0.0031  0.0331  18  VAL   C N   
1176 C CA  A VAL   B 12  ? 0.1596 0.1681 0.2229 0.0057  0.0005  0.0350  18  VAL   C CA  
1177 C CA  B VAL   B 12  ? 0.1800 0.1884 0.2431 0.0056  0.0004  0.0350  18  VAL   C CA  
1178 C C   . VAL   B 12  ? 0.1653 0.1733 0.2298 0.0062  0.0017  0.0335  18  VAL   C C   
1179 O O   . VAL   B 12  ? 0.1714 0.1775 0.2388 0.0070  0.0042  0.0310  18  VAL   C O   
1180 C CB  A VAL   B 12  ? 0.1460 0.1578 0.2163 0.0054  -0.0006 0.0398  18  VAL   C CB  
1181 C CB  B VAL   B 12  ? 0.2106 0.2224 0.2808 0.0053  -0.0006 0.0397  18  VAL   C CB  
1182 C CG1 A VAL   B 12  ? 0.1710 0.1844 0.2416 0.0043  -0.0034 0.0410  18  VAL   C CG1 
1183 C CG1 B VAL   B 12  ? 0.2269 0.2409 0.2947 0.0053  -0.0036 0.0421  18  VAL   C CG1 
1184 C CG2 A VAL   B 12  ? 0.1130 0.1248 0.1921 0.0063  0.0030  0.0415  18  VAL   C CG2 
1185 C CG2 B VAL   B 12  ? 0.2354 0.2480 0.3078 0.0045  -0.0018 0.0407  18  VAL   C CG2 
1186 N N   . ASN   B 13  ? 0.1594 0.1687 0.2224 0.0059  0.0004  0.0351  19  ASN   C N   
1187 C CA  . ASN   B 13  ? 0.1423 0.1514 0.2096 0.0064  0.0026  0.0347  19  ASN   C CA  
1188 C C   . ASN   B 13  ? 0.1604 0.1700 0.2369 0.0069  0.0052  0.0379  19  ASN   C C   
1189 O O   . ASN   B 13  ? 0.1628 0.1743 0.2410 0.0072  0.0044  0.0424  19  ASN   C O   
1190 C CB  . ASN   B 13  ? 0.1583 0.1684 0.2224 0.0066  0.0020  0.0373  19  ASN   C CB  
1191 C CG  . ASN   B 13  ? 0.1643 0.1737 0.2201 0.0063  0.0000  0.0344  19  ASN   C CG  
1192 O OD1 . ASN   B 13  ? 0.1866 0.1962 0.2358 0.0060  -0.0028 0.0349  19  ASN   C OD1 
1193 N ND2 . ASN   B 13  ? 0.1724 0.1810 0.2296 0.0063  0.0011  0.0310  19  ASN   C ND2 
1194 N N   . ARG   B 14  ? 0.1657 0.1736 0.2486 0.0072  0.0080  0.0354  20  ARG   C N   
1195 C CA  . ARG   B 14  ? 0.1583 0.1659 0.2506 0.0078  0.0111  0.0381  20  ARG   C CA  
1196 C C   . ARG   B 14  ? 0.1717 0.1813 0.2673 0.0085  0.0119  0.0446  20  ARG   C C   
1197 O O   . ARG   B 14  ? 0.1706 0.1815 0.2706 0.0094  0.0125  0.0490  20  ARG   C O   
1198 C CB  . ARG   B 14  ? 0.1550 0.1600 0.2539 0.0078  0.0137  0.0335  20  ARG   C CB  
1199 C CG  . ARG   B 14  ? 0.1647 0.1685 0.2736 0.0086  0.0174  0.0355  20  ARG   C CG  
1200 C CD  . ARG   B 14  ? 0.1660 0.1668 0.2820 0.0084  0.0195  0.0299  20  ARG   C CD  
1201 N NE  . ARG   B 14  ? 0.1704 0.1689 0.2959 0.0092  0.0233  0.0302  20  ARG   C NE  
1202 C CZ  . ARG   B 14  ? 0.1688 0.1672 0.3047 0.0094  0.0268  0.0347  20  ARG   C CZ  
1203 N NH1 . ARG   B 14  ? 0.1801 0.1806 0.3170 0.0094  0.0272  0.0401  20  ARG   C NH1 
1204 N NH2 . ARG   B 14  ? 0.1804 0.1761 0.3251 0.0102  0.0304  0.0342  20  ARG   C NH2 
1205 N N   . HIS   B 15  ? 0.1596 0.1695 0.2520 0.0086  0.0118  0.0454  21  HIS   C N   
1206 C CA  . HIS   B 15  ? 0.1698 0.1806 0.2631 0.0102  0.0133  0.0520  21  HIS   C CA  
1207 C C   . HIS   B 15  ? 0.1834 0.1968 0.2692 0.0113  0.0092  0.0561  21  HIS   C C   
1208 O O   . HIS   B 15  ? 0.2019 0.2162 0.2876 0.0135  0.0097  0.0619  21  HIS   C O   
1209 C CB  . HIS   B 15  ? 0.1753 0.1850 0.2679 0.0106  0.0156  0.0521  21  HIS   C CB  
1210 C CG  . HIS   B 15  ? 0.1850 0.1951 0.2666 0.0104  0.0127  0.0506  21  HIS   C CG  
1211 N ND1 . HIS   B 15  ? 0.1898 0.1995 0.2687 0.0088  0.0109  0.0444  21  HIS   C ND1 
1212 C CD2 . HIS   B 15  ? 0.1959 0.2066 0.2685 0.0120  0.0115  0.0544  21  HIS   C CD2 
1213 C CE1 . HIS   B 15  ? 0.1940 0.2039 0.2633 0.0092  0.0090  0.0449  21  HIS   C CE1 
1214 N NE2 . HIS   B 15  ? 0.1974 0.2077 0.2624 0.0111  0.0093  0.0505  21  HIS   C NE2 
1215 N N   . LEU   B 16  ? 0.1676 0.1819 0.2476 0.0100  0.0051  0.0531  22  LEU   C N   
1216 C CA  . LEU   B 16  ? 0.1833 0.2002 0.2583 0.0105  0.0004  0.0555  22  LEU   C CA  
1217 C C   . LEU   B 16  ? 0.1959 0.2146 0.2775 0.0099  -0.0008 0.0559  22  LEU   C C   
1218 O O   . LEU   B 16  ? 0.2007 0.2220 0.2808 0.0098  -0.0051 0.0570  22  LEU   C O   
1219 C CB  . LEU   B 16  ? 0.1931 0.2095 0.2578 0.0094  -0.0031 0.0520  22  LEU   C CB  
1220 C CG  . LEU   B 16  ? 0.1899 0.2048 0.2478 0.0105  -0.0018 0.0523  22  LEU   C CG  
1221 C CD1 . LEU   B 16  ? 0.2037 0.2177 0.2521 0.0095  -0.0048 0.0485  22  LEU   C CD1 
1222 C CD2 . LEU   B 16  ? 0.1973 0.2130 0.2522 0.0134  -0.0018 0.0582  22  LEU   C CD2 
1223 N N   . ALA   B 17  ? 0.1855 0.2028 0.2750 0.0095  0.0031  0.0546  23  ALA   C N   
1224 C CA  . ALA   B 17  ? 0.1845 0.2029 0.2808 0.0093  0.0034  0.0551  23  ALA   C CA  
1225 C C   . ALA   B 17  ? 0.2024 0.2244 0.3048 0.0109  0.0017  0.0610  23  ALA   C C   
1226 O O   . ALA   B 17  ? 0.2149 0.2373 0.3193 0.0128  0.0030  0.0650  23  ALA   C O   
1227 C CB  . ALA   B 17  ? 0.1928 0.2080 0.2948 0.0094  0.0084  0.0523  23  ALA   C CB  
1228 N N   . THR   B 18  ? 0.2046 0.2295 0.3111 0.0104  -0.0010 0.0618  24  THR   C N   
1229 C CA  . THR   B 18  ? 0.2078 0.2370 0.3213 0.0120  -0.0039 0.0669  24  THR   C CA  
1230 C C   . THR   B 18  ? 0.1939 0.2232 0.3199 0.0129  0.0009  0.0692  24  THR   C C   
1231 O O   . THR   B 18  ? 0.2019 0.2274 0.3298 0.0122  0.0060  0.0660  24  THR   C O   
1232 C CB  . THR   B 18  ? 0.2234 0.2562 0.3374 0.0107  -0.0098 0.0660  24  THR   C CB  
1233 O OG1 . THR   B 18  ? 0.2298 0.2614 0.3496 0.0090  -0.0068 0.0634  24  THR   C OG1 
1234 C CG2 . THR   B 18  ? 0.2410 0.2732 0.3427 0.0098  -0.0145 0.0631  24  THR   C CG2 
1235 N N   . HIS   B 19  ? 0.2195 0.2529 0.3539 0.0149  -0.0011 0.0745  25  HIS   C N   
1236 C CA  . HIS   B 19  ? 0.2325 0.2661 0.3797 0.0159  0.0035  0.0768  25  HIS   C CA  
1237 C C   . HIS   B 19  ? 0.2105 0.2437 0.3624 0.0140  0.0052  0.0737  25  HIS   C C   
1238 O O   . HIS   B 19  ? 0.2189 0.2485 0.3750 0.0143  0.0115  0.0723  25  HIS   C O   
1239 C CB  . HIS   B 19  ? 0.2529 0.2917 0.4088 0.0185  0.0003  0.0832  25  HIS   C CB  
1240 C CG  . HIS   B 19  ? 0.2766 0.3165 0.4474 0.0194  0.0045  0.0856  25  HIS   C CG  
1241 N ND1 . HIS   B 19  ? 0.2971 0.3328 0.4730 0.0206  0.0119  0.0862  25  HIS   C ND1 
1242 C CD2 . HIS   B 19  ? 0.2889 0.3331 0.4705 0.0191  0.0027  0.0867  25  HIS   C CD2 
1243 C CE1 . HIS   B 19  ? 0.3027 0.3403 0.4915 0.0214  0.0144  0.0884  25  HIS   C CE1 
1244 N NE2 . HIS   B 19  ? 0.2956 0.3384 0.4888 0.0206  0.0093  0.0889  25  HIS   C NE2 
1245 N N   . ASN   B 20  ? 0.2070 0.2431 0.3576 0.0124  0.0002  0.0722  26  ASN   C N   
1246 C CA  . ASN   B 20  ? 0.2136 0.2488 0.3692 0.0109  0.0030  0.0699  26  ASN   C CA  
1247 C C   . ASN   B 20  ? 0.2020 0.2305 0.3487 0.0102  0.0085  0.0652  26  ASN   C C   
1248 O O   . ASN   B 20  ? 0.1921 0.2177 0.3429 0.0108  0.0143  0.0643  26  ASN   C O   
1249 C CB  . ASN   B 20  ? 0.2292 0.2680 0.3856 0.0090  -0.0032 0.0689  26  ASN   C CB  
1250 C CG  . ASN   B 20  ? 0.2938 0.3318 0.4585 0.0077  0.0006  0.0679  26  ASN   C CG  
1251 O OD1 . ASN   B 20  ? 0.3215 0.3621 0.5005 0.0085  0.0031  0.0709  26  ASN   C OD1 
1252 N ND2 . ASN   B 20  ? 0.3218 0.3559 0.4781 0.0061  0.0018  0.0639  26  ASN   C ND2 
1253 N N   . ASP   B 21  ? 0.1791 0.2050 0.3132 0.0096  0.0069  0.0621  27  ASP   C N   
1254 C CA  . ASP   B 21  ? 0.1795 0.1997 0.3057 0.0095  0.0112  0.0573  27  ASP   C CA  
1255 C C   . ASP   B 21  ? 0.1721 0.1889 0.3027 0.0112  0.0171  0.0570  27  ASP   C C   
1256 O O   . ASP   B 21  ? 0.1865 0.1992 0.3155 0.0119  0.0216  0.0541  27  ASP   C O   
1257 C CB  . ASP   B 21  ? 0.1800 0.1987 0.2946 0.0087  0.0084  0.0545  27  ASP   C CB  
1258 C CG  . ASP   B 21  ? 0.1792 0.1993 0.2869 0.0071  0.0035  0.0531  27  ASP   C CG  
1259 O OD1 . ASP   B 21  ? 0.1950 0.2147 0.3037 0.0063  0.0040  0.0520  27  ASP   C OD1 
1260 O OD2 . ASP   B 21  ? 0.1847 0.2060 0.2864 0.0069  -0.0002 0.0534  27  ASP   C OD2 
1261 N N   . TRP   B 22  ? 0.1752 0.1933 0.3110 0.0122  0.0174  0.0600  28  TRP   C N   
1262 C CA  . TRP   B 22  ? 0.1767 0.1911 0.3178 0.0137  0.0231  0.0594  28  TRP   C CA  
1263 C C   . TRP   B 22  ? 0.1773 0.1919 0.3288 0.0151  0.0273  0.0617  28  TRP   C C   
1264 O O   . TRP   B 22  ? 0.1987 0.2084 0.3509 0.0164  0.0328  0.0588  28  TRP   C O   
1265 C CB  . TRP   B 22  ? 0.1812 0.1967 0.3265 0.0146  0.0229  0.0629  28  TRP   C CB  
1266 C CG  . TRP   B 22  ? 0.1900 0.2032 0.3277 0.0138  0.0220  0.0598  28  TRP   C CG  
1267 C CD1 . TRP   B 22  ? 0.2085 0.2239 0.3400 0.0133  0.0180  0.0615  28  TRP   C CD1 
1268 C CD2 . TRP   B 22  ? 0.1743 0.1825 0.3106 0.0135  0.0254  0.0544  28  TRP   C CD2 
1269 N NE1 . TRP   B 22  ? 0.2053 0.2177 0.3330 0.0127  0.0194  0.0580  28  TRP   C NE1 
1270 C CE2 . TRP   B 22  ? 0.1935 0.2017 0.3245 0.0126  0.0233  0.0533  28  TRP   C CE2 
1271 C CE3 . TRP   B 22  ? 0.2036 0.2072 0.3428 0.0142  0.0298  0.0500  28  TRP   C CE3 
1272 C CZ2 . TRP   B 22  ? 0.2054 0.2100 0.3367 0.0120  0.0253  0.0483  28  TRP   C CZ2 
1273 C CZ3 . TRP   B 22  ? 0.2168 0.2165 0.3542 0.0137  0.0309  0.0442  28  TRP   C CZ3 
1274 C CH2 . TRP   B 22  ? 0.2094 0.2100 0.3441 0.0125  0.0285  0.0435  28  TRP   C CH2 
1275 N N   . ALA   B 23  ? 0.1832 0.2029 0.3420 0.0150  0.0247  0.0661  29  ALA   C N   
1276 C CA  . ALA   B 23  ? 0.1815 0.2022 0.3521 0.0163  0.0289  0.0688  29  ALA   C CA  
1277 C C   . ALA   B 23  ? 0.2026 0.2197 0.3697 0.0161  0.0328  0.0656  29  ALA   C C   
1278 O O   . ALA   B 23  ? 0.2060 0.2221 0.3814 0.0176  0.0382  0.0672  29  ALA   C O   
1279 C CB  . ALA   B 23  ? 0.1817 0.2098 0.3628 0.0161  0.0239  0.0742  29  ALA   C CB  
1280 N N   . ASN   B 24  ? 0.2016 0.2166 0.3564 0.0147  0.0305  0.0615  30  ASN   C N   
1281 C CA  . ASN   B 24  ? 0.2096 0.2206 0.3588 0.0151  0.0344  0.0589  30  ASN   C CA  
1282 C C   . ASN   B 24  ? 0.2069 0.2120 0.3406 0.0155  0.0348  0.0529  30  ASN   C C   
1283 O O   . ASN   B 24  ? 0.1956 0.1987 0.3201 0.0152  0.0342  0.0504  30  ASN   C O   
1284 C CB  . ASN   B 24  ? 0.2153 0.2303 0.3667 0.0129  0.0301  0.0604  30  ASN   C CB  
1285 C CG  . ASN   B 24  ? 0.2256 0.2463 0.3939 0.0126  0.0296  0.0655  30  ASN   C CG  
1286 O OD1 . ASN   B 24  ? 0.2466 0.2661 0.4235 0.0139  0.0357  0.0673  30  ASN   C OD1 
1287 N ND2 . ASN   B 24  ? 0.2370 0.2640 0.4107 0.0114  0.0226  0.0679  30  ASN   C ND2 
1288 N N   . LEU   B 25  ? 0.2055 0.2083 0.3374 0.0164  0.0357  0.0506  31  LEU   C N   
1289 C CA  . LEU   B 25  ? 0.2113 0.2097 0.3311 0.0167  0.0349  0.0445  31  LEU   C CA  
1290 C C   . LEU   B 25  ? 0.2237 0.2156 0.3339 0.0193  0.0392  0.0400  31  LEU   C C   
1291 O O   . LEU   B 25  ? 0.2325 0.2212 0.3460 0.0217  0.0450  0.0404  31  LEU   C O   
1292 C CB  . LEU   B 25  ? 0.2165 0.2139 0.3406 0.0169  0.0353  0.0434  31  LEU   C CB  
1293 C CG  . LEU   B 25  ? 0.2181 0.2120 0.3335 0.0168  0.0337  0.0368  31  LEU   C CG  
1294 C CD1 . LEU   B 25  ? 0.2192 0.2161 0.3282 0.0146  0.0280  0.0364  31  LEU   C CD1 
1295 C CD2 . LEU   B 25  ? 0.2273 0.2192 0.3499 0.0172  0.0357  0.0354  31  LEU   C CD2 
1296 N N   . VAL   B 26  ? 0.2039 0.1939 0.3020 0.0193  0.0366  0.0360  32  VAL   C N   
1297 C CA  . VAL   B 26  ? 0.2246 0.2082 0.3107 0.0225  0.0397  0.0313  32  VAL   C CA  
1298 C C   . VAL   B 26  ? 0.2307 0.2115 0.3104 0.0232  0.0370  0.0245  32  VAL   C C   
1299 O O   . VAL   B 26  ? 0.2491 0.2245 0.3244 0.0262  0.0400  0.0201  32  VAL   C O   
1300 C CB  . VAL   B 26  ? 0.2446 0.2279 0.3218 0.0226  0.0385  0.0318  32  VAL   C CB  
1301 C CG1 . VAL   B 26  ? 0.2741 0.2506 0.3364 0.0268  0.0409  0.0271  32  VAL   C CG1 
1302 C CG2 . VAL   B 26  ? 0.2467 0.2322 0.3323 0.0220  0.0416  0.0379  32  VAL   C CG2 
1303 N N   . TRP   B 27  ? 0.2097 0.1940 0.2895 0.0205  0.0315  0.0234  33  TRP   C N   
1304 C CA  . TRP   B 27  ? 0.2223 0.2048 0.2985 0.0207  0.0286  0.0169  33  TRP   C CA  
1305 C C   . TRP   B 27  ? 0.2092 0.1965 0.2910 0.0173  0.0243  0.0185  33  TRP   C C   
1306 O O   . TRP   B 27  ? 0.1982 0.1894 0.2796 0.0155  0.0221  0.0226  33  TRP   C O   
1307 C CB  . TRP   B 27  ? 0.2406 0.2197 0.3022 0.0232  0.0267  0.0119  33  TRP   C CB  
1308 C CG  . TRP   B 27  ? 0.2475 0.2259 0.3053 0.0232  0.0220  0.0050  33  TRP   C CG  
1309 C CD1 . TRP   B 27  ? 0.2752 0.2499 0.3318 0.0253  0.0216  -0.0020 33  TRP   C CD1 
1310 C CD2 . TRP   B 27  ? 0.2346 0.2165 0.2903 0.0213  0.0170  0.0041  33  TRP   C CD2 
1311 N NE1 . TRP   B 27  ? 0.2848 0.2608 0.3397 0.0246  0.0161  -0.0073 33  TRP   C NE1 
1312 C CE2 . TRP   B 27  ? 0.2564 0.2368 0.3107 0.0223  0.0136  -0.0034 33  TRP   C CE2 
1313 C CE3 . TRP   B 27  ? 0.2363 0.2222 0.2920 0.0189  0.0149  0.0085  33  TRP   C CE3 
1314 C CZ2 . TRP   B 27  ? 0.2507 0.2340 0.3045 0.0209  0.0087  -0.0059 33  TRP   C CZ2 
1315 C CZ3 . TRP   B 27  ? 0.2486 0.2364 0.3015 0.0180  0.0104  0.0059  33  TRP   C CZ3 
1316 C CH2 . TRP   B 27  ? 0.2499 0.2369 0.3032 0.0188  0.0076  -0.0008 33  TRP   C CH2 
1317 N N   . GLU   B 28  ? 0.1993 0.1862 0.2864 0.0167  0.0234  0.0150  34  GLU   C N   
1318 C CA  . GLU   B 28  ? 0.2084 0.1990 0.3006 0.0141  0.0204  0.0164  34  GLU   C CA  
1319 C C   . GLU   B 28  ? 0.1951 0.1839 0.2894 0.0140  0.0188  0.0097  34  GLU   C C   
1320 O O   . GLU   B 28  ? 0.2029 0.1879 0.2995 0.0155  0.0204  0.0046  34  GLU   C O   
1321 C CB  . GLU   B 28  ? 0.2124 0.2061 0.3155 0.0127  0.0223  0.0232  34  GLU   C CB  
1322 C CG  . GLU   B 28  ? 0.2331 0.2243 0.3458 0.0137  0.0266  0.0232  34  GLU   C CG  
1323 C CD  . GLU   B 28  ? 0.2424 0.2319 0.3636 0.0130  0.0274  0.0197  34  GLU   C CD  
1324 O OE1 . GLU   B 28  ? 0.2806 0.2663 0.4076 0.0142  0.0307  0.0169  34  GLU   C OE1 
1325 O OE2 . GLU   B 28  ? 0.2284 0.2199 0.3513 0.0114  0.0252  0.0198  34  GLU   C OE2 
1326 N N   . ASP   B 29  ? 0.1798 0.1714 0.2749 0.0122  0.0157  0.0093  35  ASP   C N   
1327 C CA  . ASP   B 29  ? 0.1871 0.1781 0.2876 0.0117  0.0139  0.0031  35  ASP   C CA  
1328 C C   . ASP   B 29  ? 0.1854 0.1799 0.2931 0.0094  0.0136  0.0069  35  ASP   C C   
1329 O O   . ASP   B 29  ? 0.1839 0.1809 0.2853 0.0089  0.0112  0.0086  35  ASP   C O   
1330 C CB  . ASP   B 29  ? 0.2101 0.1994 0.2996 0.0136  0.0098  -0.0038 35  ASP   C CB  
1331 C CG  . ASP   B 29  ? 0.2778 0.2669 0.3730 0.0133  0.0066  -0.0115 35  ASP   C CG  
1332 O OD1 . ASP   B 29  ? 0.2931 0.2844 0.4004 0.0110  0.0072  -0.0104 35  ASP   C OD1 
1333 O OD2 . ASP   B 29  ? 0.3112 0.2977 0.3987 0.0158  0.0034  -0.0186 35  ASP   C OD2 
1334 N N   . SER   B 30  ? 0.1888 0.1831 0.3097 0.0084  0.0168  0.0085  36  SER   C N   
1335 C CA  A SER   B 30  ? 0.1953 0.1922 0.3233 0.0069  0.0180  0.0129  36  SER   C CA  
1336 C CA  B SER   B 30  ? 0.1938 0.1907 0.3215 0.0069  0.0180  0.0130  36  SER   C CA  
1337 C C   . SER   B 30  ? 0.1972 0.1954 0.3263 0.0061  0.0151  0.0080  36  SER   C C   
1338 O O   . SER   B 30  ? 0.2083 0.2089 0.3355 0.0055  0.0150  0.0118  36  SER   C O   
1339 C CB  A SER   B 30  ? 0.2104 0.2058 0.3530 0.0065  0.0229  0.0158  36  SER   C CB  
1340 C CB  B SER   B 30  ? 0.2037 0.1994 0.3456 0.0066  0.0229  0.0164  36  SER   C CB  
1341 O OG  A SER   B 30  ? 0.2336 0.2305 0.3841 0.0055  0.0249  0.0190  36  SER   C OG  
1342 O OG  B SER   B 30  ? 0.2159 0.2083 0.3670 0.0063  0.0236  0.0092  36  SER   C OG  
1343 N N   . SER   B 31  ? 0.1945 0.1909 0.3254 0.0064  0.0124  -0.0007 37  SER   C N   
1344 C CA  . SER   B 31  ? 0.2038 0.2021 0.3372 0.0058  0.0088  -0.0058 37  SER   C CA  
1345 C C   . SER   B 31  ? 0.1966 0.1971 0.3161 0.0065  0.0053  -0.0047 37  SER   C C   
1346 O O   . SER   B 31  ? 0.2053 0.2082 0.3272 0.0059  0.0036  -0.0059 37  SER   C O   
1347 C CB  . SER   B 31  ? 0.2425 0.2388 0.3802 0.0065  0.0053  -0.0161 37  SER   C CB  
1348 O OG  . SER   B 31  ? 0.3206 0.3150 0.4433 0.0090  0.0016  -0.0203 37  SER   C OG  
1349 N N   . ARG   B 32  ? 0.1956 0.1951 0.3018 0.0079  0.0047  -0.0024 38  ARG   C N   
1350 C CA  . ARG   B 32  ? 0.1896 0.1905 0.2831 0.0086  0.0020  -0.0011 38  ARG   C CA  
1351 C C   . ARG   B 32  ? 0.1760 0.1785 0.2658 0.0077  0.0040  0.0070  38  ARG   C C   
1352 O O   . ARG   B 32  ? 0.1847 0.1882 0.2653 0.0080  0.0021  0.0082  38  ARG   C O   
1353 C CB  . ARG   B 32  ? 0.2220 0.2201 0.3031 0.0110  0.0003  -0.0038 38  ARG   C CB  
1354 C CG  . ARG   B 32  ? 0.2445 0.2405 0.3246 0.0131  -0.0028 -0.0124 38  ARG   C CG  
1355 C CD  . ARG   B 32  ? 0.2218 0.2142 0.2878 0.0165  -0.0034 -0.0143 38  ARG   C CD  
1356 N NE  . ARG   B 32  ? 0.2113 0.2044 0.2656 0.0177  -0.0052 -0.0123 38  ARG   C NE  
1357 C CZ  . ARG   B 32  ? 0.2303 0.2207 0.2718 0.0213  -0.0071 -0.0152 38  ARG   C CZ  
1358 N NH1 . ARG   B 32  ? 0.2641 0.2508 0.3013 0.0245  -0.0078 -0.0207 38  ARG   C NH1 
1359 N NH2 . ARG   B 32  ? 0.2233 0.2142 0.2559 0.0223  -0.0081 -0.0126 38  ARG   C NH2 
1360 N N   . ASP   B 33  ? 0.1717 0.1745 0.2684 0.0069  0.0077  0.0123  39  ASP   C N   
1361 C CA  . ASP   B 33  ? 0.1645 0.1688 0.2572 0.0066  0.0088  0.0197  39  ASP   C CA  
1362 C C   . ASP   B 33  ? 0.1648 0.1687 0.2473 0.0072  0.0070  0.0205  39  ASP   C C   
1363 O O   . ASP   B 33  ? 0.1687 0.1741 0.2450 0.0069  0.0057  0.0239  39  ASP   C O   
1364 C CB  . ASP   B 33  ? 0.1726 0.1788 0.2632 0.0062  0.0085  0.0221  39  ASP   C CB  
1365 C CG  . ASP   B 33  ? 0.1886 0.1959 0.2745 0.0064  0.0092  0.0292  39  ASP   C CG  
1366 O OD1 . ASP   B 33  ? 0.1886 0.1961 0.2789 0.0068  0.0112  0.0333  39  ASP   C OD1 
1367 O OD2 . ASP   B 33  ? 0.1776 0.1857 0.2555 0.0065  0.0075  0.0303  39  ASP   C OD2 
1368 N N   . LEU   B 34  ? 0.1557 0.1575 0.2371 0.0082  0.0074  0.0178  40  LEU   C N   
1369 C CA  . LEU   B 34  ? 0.1626 0.1636 0.2363 0.0090  0.0070  0.0193  40  LEU   C CA  
1370 C C   . LEU   B 34  ? 0.1557 0.1559 0.2345 0.0095  0.0101  0.0220  40  LEU   C C   
1371 O O   . LEU   B 34  ? 0.1680 0.1663 0.2532 0.0101  0.0123  0.0200  40  LEU   C O   
1372 C CB  . LEU   B 34  ? 0.1752 0.1735 0.2402 0.0108  0.0055  0.0138  40  LEU   C CB  
1373 C CG  . LEU   B 34  ? 0.1782 0.1774 0.2364 0.0108  0.0023  0.0116  40  LEU   C CG  
1374 C CD1 . LEU   B 34  ? 0.2126 0.2088 0.2615 0.0136  0.0009  0.0067  40  LEU   C CD1 
1375 C CD2 . LEU   B 34  ? 0.1865 0.1875 0.2404 0.0096  0.0015  0.0163  40  LEU   C CD2 
1376 N N   . LEU   B 35  ? 0.1473 0.1485 0.2238 0.0094  0.0102  0.0259  41  LEU   C N   
1377 C CA  . LEU   B 35  ? 0.1766 0.1773 0.2582 0.0102  0.0132  0.0287  41  LEU   C CA  
1378 C C   . LEU   B 35  ? 0.1728 0.1731 0.2490 0.0105  0.0131  0.0299  41  LEU   C C   
1379 O O   . LEU   B 35  ? 0.1832 0.1854 0.2554 0.0093  0.0103  0.0312  41  LEU   C O   
1380 C CB  . LEU   B 35  ? 0.1684 0.1724 0.2588 0.0093  0.0135  0.0345  41  LEU   C CB  
1381 C CG  . LEU   B 35  ? 0.1590 0.1633 0.2572 0.0102  0.0165  0.0379  41  LEU   C CG  
1382 C CD1 . LEU   B 35  ? 0.1790 0.1846 0.2869 0.0105  0.0182  0.0416  41  LEU   C CD1 
1383 C CD2 . LEU   B 35  ? 0.1783 0.1854 0.2764 0.0097  0.0148  0.0417  41  LEU   C CD2 
1384 N N   . VAL   B 36  ? 0.1655 0.1631 0.2423 0.0123  0.0167  0.0295  42  VAL   C N   
1385 C CA  . VAL   B 36  ? 0.1635 0.1601 0.2373 0.0130  0.0184  0.0312  42  VAL   C CA  
1386 C C   . VAL   B 36  ? 0.1670 0.1647 0.2510 0.0132  0.0218  0.0355  42  VAL   C C   
1387 O O   . VAL   B 36  ? 0.1854 0.1811 0.2736 0.0147  0.0253  0.0349  42  VAL   C O   
1388 C CB  . VAL   B 36  ? 0.1836 0.1749 0.2468 0.0159  0.0205  0.0270  42  VAL   C CB  
1389 C CG1 . VAL   B 36  ? 0.2122 0.2018 0.2736 0.0169  0.0237  0.0299  42  VAL   C CG1 
1390 C CG2 . VAL   B 36  ? 0.1933 0.1842 0.2476 0.0159  0.0164  0.0229  42  VAL   C CG2 
1391 N N   . SER   B 37  ? 0.1696 0.1704 0.2586 0.0118  0.0209  0.0396  43  SER   C N   
1392 C CA  . SER   B 37  ? 0.1667 0.1694 0.2672 0.0120  0.0238  0.0440  43  SER   C CA  
1393 C C   . SER   B 37  ? 0.1845 0.1857 0.2855 0.0126  0.0270  0.0453  43  SER   C C   
1394 O O   . SER   B 37  ? 0.1882 0.1874 0.2808 0.0124  0.0260  0.0435  43  SER   C O   
1395 C CB  . SER   B 37  ? 0.1682 0.1771 0.2777 0.0100  0.0193  0.0479  43  SER   C CB  
1396 O OG  . SER   B 37  ? 0.2082 0.2196 0.3145 0.0080  0.0142  0.0480  43  SER   C OG  
1397 N N   . SER   B 38  ? 0.1882 0.1897 0.2996 0.0135  0.0316  0.0486  44  SER   C N   
1398 C CA  . SER   B 38  ? 0.1978 0.1976 0.3123 0.0142  0.0360  0.0507  44  SER   C CA  
1399 C C   . SER   B 38  ? 0.2213 0.2271 0.3477 0.0110  0.0318  0.0540  44  SER   C C   
1400 O O   . SER   B 38  ? 0.2280 0.2394 0.3625 0.0093  0.0267  0.0557  44  SER   C O   
1401 C CB  . SER   B 38  ? 0.2268 0.2235 0.3472 0.0172  0.0441  0.0527  44  SER   C CB  
1402 O OG  . SER   B 38  ? 0.2845 0.2862 0.4197 0.0163  0.0435  0.0561  44  SER   C OG  
1403 N N   . THR   B 39  ? 0.2312 0.2355 0.3583 0.0105  0.0335  0.0546  45  THR   C N   
1404 C CA  . THR   B 39  ? 0.2397 0.2492 0.3788 0.0073  0.0292  0.0565  45  THR   C CA  
1405 C C   . THR   B 39  ? 0.2677 0.2765 0.4205 0.0078  0.0360  0.0601  45  THR   C C   
1406 O O   . THR   B 39  ? 0.2642 0.2668 0.4117 0.0109  0.0443  0.0607  45  THR   C O   
1407 C CB  . THR   B 39  ? 0.2490 0.2571 0.3785 0.0055  0.0248  0.0537  45  THR   C CB  
1408 O OG1 . THR   B 39  ? 0.2664 0.2679 0.3881 0.0077  0.0314  0.0533  45  THR   C OG1 
1409 C CG2 . THR   B 39  ? 0.2710 0.2796 0.3874 0.0051  0.0188  0.0503  45  THR   C CG2 
1410 N N   . THR   B 40  ? 0.2798 0.2946 0.4494 0.0051  0.0322  0.0622  46  THR   C N   
1411 C CA  . THR   B 40  ? 0.2981 0.3129 0.4841 0.0051  0.0386  0.0657  46  THR   C CA  
1412 C C   . THR   B 40  ? 0.3182 0.3289 0.5012 0.0041  0.0406  0.0648  46  THR   C C   
1413 O O   . THR   B 40  ? 0.3403 0.3458 0.5255 0.0063  0.0501  0.0673  46  THR   C O   
1414 C CB  . THR   B 40  ? 0.3482 0.3714 0.5556 0.0029  0.0339  0.0682  46  THR   C CB  
1415 O OG1 . THR   B 40  ? 0.3964 0.4246 0.6039 -0.0004 0.0229  0.0655  46  THR   C OG1 
1416 C CG2 . THR   B 40  ? 0.3415 0.3673 0.5517 0.0049  0.0341  0.0700  46  THR   C CG2 
1417 N N   . ALA   B 41  ? 0.3129 0.3252 0.4900 0.0013  0.0325  0.0615  47  ALA   C N   
1418 C CA  . ALA   B 41  ? 0.3161 0.3243 0.4903 0.0003  0.0341  0.0604  47  ALA   C CA  
1419 C C   . ALA   B 41  ? 0.3095 0.3106 0.4612 0.0031  0.0368  0.0582  47  ALA   C C   
1420 O O   . ALA   B 41  ? 0.2962 0.2974 0.4346 0.0041  0.0332  0.0558  47  ALA   C O   
1421 C CB  . ALA   B 41  ? 0.3285 0.3416 0.5088 -0.0039 0.0241  0.0575  47  ALA   C CB  
1422 N N   . GLN   B 42  ? 0.3092 0.3043 0.4576 0.0043  0.0428  0.0592  48  GLN   C N   
1423 C CA  . GLN   B 42  ? 0.3141 0.3028 0.4416 0.0074  0.0448  0.0572  48  GLN   C CA  
1424 C C   . GLN   B 42  ? 0.2918 0.2820 0.4117 0.0046  0.0362  0.0532  48  GLN   C C   
1425 O O   . GLN   B 42  ? 0.2974 0.2904 0.4277 0.0009  0.0317  0.0524  48  GLN   C O   
1426 C CB  . GLN   B 42  ? 0.3604 0.3416 0.4858 0.0108  0.0551  0.0606  48  GLN   C CB  
1427 C CG  . GLN   B 42  ? 0.4576 0.4355 0.5843 0.0150  0.0646  0.0642  48  GLN   C CG  
1428 C CD  . GLN   B 42  ? 0.5848 0.5550 0.7101 0.0188  0.0756  0.0683  48  GLN   C CD  
1429 O OE1 . GLN   B 42  ? 0.6122 0.5826 0.7539 0.0167  0.0792  0.0715  48  GLN   C OE1 
1430 N NE2 . GLN   B 42  ? 0.6282 0.5912 0.7340 0.0248  0.0811  0.0685  48  GLN   C NE2 
1431 N N   . GLY   B 43  ? 0.2654 0.2535 0.3676 0.0066  0.0338  0.0503  49  GLY   C N   
1432 C CA  . GLY   B 43  ? 0.2529 0.2417 0.3459 0.0048  0.0268  0.0466  49  GLY   C CA  
1433 C C   . GLY   B 43  ? 0.2572 0.2395 0.3400 0.0071  0.0306  0.0464  49  GLY   C C   
1434 O O   . GLY   B 43  ? 0.2794 0.2564 0.3583 0.0110  0.0385  0.0490  49  GLY   C O   
1435 N N   . CYS   B 44  ? 0.2617 0.2442 0.3392 0.0053  0.0254  0.0436  50  CYS   C N   
1436 C CA  . CYS   B 44  ? 0.2854 0.2620 0.3550 0.0072  0.0285  0.0436  50  CYS   C CA  
1437 C C   . CYS   B 44  ? 0.2690 0.2438 0.3217 0.0096  0.0257  0.0407  50  CYS   C C   
1438 O O   . CYS   B 44  ? 0.3110 0.2814 0.3572 0.0112  0.0274  0.0407  50  CYS   C O   
1439 C CB  . CYS   B 44  ? 0.3256 0.3027 0.4055 0.0033  0.0259  0.0429  50  CYS   C CB  
1440 S SG  . CYS   B 44  ? 0.5821 0.5641 0.6589 -0.0005 0.0149  0.0378  50  CYS   C SG  
1441 N N   . ASP   B 45  ? 0.2286 0.2072 0.2761 0.0094  0.0208  0.0381  51  ASP   C N   
1442 C CA  . ASP   B 45  ? 0.2301 0.2078 0.2642 0.0112  0.0178  0.0350  51  ASP   C CA  
1443 C C   . ASP   B 45  ? 0.2455 0.2185 0.2690 0.0166  0.0226  0.0356  51  ASP   C C   
1444 O O   . ASP   B 45  ? 0.2729 0.2446 0.2979 0.0187  0.0272  0.0375  51  ASP   C O   
1445 C CB  . ASP   B 45  ? 0.2330 0.2158 0.2662 0.0096  0.0121  0.0324  51  ASP   C CB  
1446 C CG  . ASP   B 45  ? 0.2847 0.2716 0.3242 0.0055  0.0066  0.0315  51  ASP   C CG  
1447 O OD1 . ASP   B 45  ? 0.3143 0.2998 0.3542 0.0040  0.0052  0.0308  51  ASP   C OD1 
1448 O OD2 . ASP   B 45  ? 0.2468 0.2380 0.2902 0.0041  0.0037  0.0314  51  ASP   C OD2 
1449 N N   . THR   B 46  ? 0.2362 0.2066 0.2487 0.0192  0.0215  0.0339  52  THR   C N   
1450 C CA  . THR   B 46  ? 0.2432 0.2094 0.2433 0.0250  0.0244  0.0336  52  THR   C CA  
1451 C C   . THR   B 46  ? 0.2414 0.2108 0.2351 0.0255  0.0184  0.0290  52  THR   C C   
1452 O O   . THR   B 46  ? 0.2419 0.2140 0.2360 0.0232  0.0137  0.0269  52  THR   C O   
1453 C CB  . THR   B 46  ? 0.2889 0.2498 0.2821 0.0280  0.0271  0.0354  52  THR   C CB  
1454 O OG1 . THR   B 46  ? 0.3058 0.2634 0.3072 0.0273  0.0335  0.0399  52  THR   C OG1 
1455 C CG2 . THR   B 46  ? 0.3310 0.2878 0.3091 0.0348  0.0286  0.0347  52  THR   C CG2 
1456 N N   . ILE   B 47  ? 0.2355 0.2043 0.2238 0.0287  0.0188  0.0271  53  ILE   C N   
1457 C CA  . ILE   B 47  ? 0.2215 0.1932 0.2057 0.0293  0.0134  0.0223  53  ILE   C CA  
1458 C C   . ILE   B 47  ? 0.2325 0.2012 0.2045 0.0343  0.0120  0.0205  53  ILE   C C   
1459 O O   . ILE   B 47  ? 0.2526 0.2161 0.2157 0.0393  0.0160  0.0222  53  ILE   C O   
1460 C CB  . ILE   B 47  ? 0.2324 0.2043 0.2170 0.0307  0.0141  0.0203  53  ILE   C CB  
1461 C CG1 . ILE   B 47  ? 0.2464 0.2209 0.2431 0.0268  0.0162  0.0230  53  ILE   C CG1 
1462 C CG2 . ILE   B 47  ? 0.2374 0.2125 0.2207 0.0308  0.0084  0.0149  53  ILE   C CG2 
1463 C CD1 . ILE   B 47  ? 0.2618 0.2417 0.2680 0.0214  0.0120  0.0231  53  ILE   C CD1 
1464 N N   . ALA   B 48  ? 0.2109 0.1828 0.1823 0.0334  0.0066  0.0173  54  ALA   C N   
1465 C CA  . ALA   B 48  ? 0.2110 0.1812 0.1723 0.0382  0.0043  0.0152  54  ALA   C CA  
1466 C C   . ALA   B 48  ? 0.2276 0.1965 0.1811 0.0430  0.0026  0.0113  54  ALA   C C   
1467 O O   . ALA   B 48  ? 0.2231 0.1947 0.1819 0.0412  0.0008  0.0082  54  ALA   C O   
1468 C CB  . ALA   B 48  ? 0.2096 0.1843 0.1749 0.0357  -0.0010 0.0124  54  ALA   C CB  
1469 N N   . ARG   B 49  ? 0.2294 0.1940 0.1701 0.0495  0.0032  0.0114  55  ARG   C N   
1470 C CA  . ARG   B 49  ? 0.2322 0.1953 0.1632 0.0551  0.0004  0.0067  55  ARG   C CA  
1471 C C   . ARG   B 49  ? 0.2456 0.2094 0.1691 0.0593  -0.0049 0.0042  55  ARG   C C   
1472 O O   . ARG   B 49  ? 0.2778 0.2370 0.1901 0.0647  -0.0026 0.0073  55  ARG   C O   
1473 C CB  . ARG   B 49  ? 0.2533 0.2096 0.1738 0.0603  0.0069  0.0096  55  ARG   C CB  
1474 C CG  . ARG   B 49  ? 0.2490 0.2049 0.1790 0.0561  0.0128  0.0128  55  ARG   C CG  
1475 C CD  . ARG   B 49  ? 0.2582 0.2183 0.1972 0.0524  0.0096  0.0083  55  ARG   C CD  
1476 N NE  . ARG   B 49  ? 0.2650 0.2246 0.2130 0.0490  0.0155  0.0121  55  ARG   C NE  
1477 C CZ  . ARG   B 49  ? 0.2677 0.2312 0.2270 0.0445  0.0142  0.0105  55  ARG   C CZ  
1478 N NH1 . ARG   B 49  ? 0.2447 0.2121 0.2076 0.0429  0.0081  0.0050  55  ARG   C NH1 
1479 N NH2 . ARG   B 49  ? 0.2646 0.2281 0.2325 0.0419  0.0193  0.0145  55  ARG   C NH2 
1480 N N   . CYS   B 50  ? 0.2339 0.2035 0.1645 0.0570  -0.0118 -0.0011 56  CYS   C N   
1481 C CA  . CYS   B 50  ? 0.2387 0.2111 0.1677 0.0593  -0.0175 -0.0035 56  CYS   C CA  
1482 C C   . CYS   B 50  ? 0.2460 0.2251 0.1862 0.0562  -0.0243 -0.0098 56  CYS   C C   
1483 O O   . CYS   B 50  ? 0.2463 0.2277 0.1956 0.0520  -0.0242 -0.0119 56  CYS   C O   
1484 C CB  . CYS   B 50  ? 0.2164 0.1887 0.1494 0.0563  -0.0145 0.0017  56  CYS   C CB  
1485 S SG  . CYS   B 50  ? 0.2280 0.2056 0.1784 0.0469  -0.0138 0.0024  56  CYS   C SG  
1486 N N   . ASP   B 51  ? 0.2502 0.2326 0.1911 0.0583  -0.0299 -0.0125 57  ASP   C N   
1487 C CA  . ASP   B 51  ? 0.2569 0.2460 0.2110 0.0554  -0.0358 -0.0178 57  ASP   C CA  
1488 C C   . ASP   B 51  ? 0.2532 0.2454 0.2152 0.0522  -0.0350 -0.0148 57  ASP   C C   
1489 O O   . ASP   B 51  ? 0.2651 0.2623 0.2356 0.0519  -0.0398 -0.0183 57  ASP   C O   
1490 C CB  . ASP   B 51  ? 0.2920 0.2831 0.2421 0.0610  -0.0439 -0.0248 57  ASP   C CB  
1491 C CG  . ASP   B 51  ? 0.3580 0.3475 0.2962 0.0679  -0.0465 -0.0236 57  ASP   C CG  
1492 O OD1 . ASP   B 51  ? 0.3755 0.3619 0.3089 0.0681  -0.0415 -0.0172 57  ASP   C OD1 
1493 O OD2 . ASP   B 51  ? 0.4326 0.4240 0.3668 0.0732  -0.0541 -0.0294 57  ASP   C OD2 
1494 N N   . CYS   B 52  ? 0.2408 0.2299 0.2012 0.0497  -0.0290 -0.0086 58  CYS   C N   
1495 C CA  . CYS   B 52  ? 0.2206 0.2119 0.1879 0.0466  -0.0279 -0.0062 58  CYS   C CA  
1496 C C   . CYS   B 52  ? 0.2055 0.2026 0.1875 0.0417  -0.0297 -0.0089 58  CYS   C C   
1497 O O   . CYS   B 52  ? 0.2122 0.2107 0.2003 0.0386  -0.0291 -0.0103 58  CYS   C O   
1498 C CB  . CYS   B 52  ? 0.2159 0.2032 0.1812 0.0436  -0.0217 -0.0004 58  CYS   C CB  
1499 S SG  . CYS   B 52  ? 0.2414 0.2216 0.1929 0.0488  -0.0178 0.0043  58  CYS   C SG  
1500 N N   . GLN   B 53  ? 0.1915 0.1917 0.1793 0.0415  -0.0312 -0.0092 59  GLN   C N   
1501 C CA  . GLN   B 53  ? 0.2024 0.2073 0.2041 0.0372  -0.0311 -0.0105 59  GLN   C CA  
1502 C C   . GLN   B 53  ? 0.1890 0.1929 0.1917 0.0349  -0.0271 -0.0063 59  GLN   C C   
1503 O O   . GLN   B 53  ? 0.1934 0.2006 0.2060 0.0327  -0.0264 -0.0067 59  GLN   C O   
1504 C CB  . GLN   B 53  ? 0.2155 0.2259 0.2268 0.0392  -0.0369 -0.0158 59  GLN   C CB  
1505 C CG  . GLN   B 53  ? 0.2547 0.2669 0.2698 0.0397  -0.0410 -0.0212 59  GLN   C CG  
1506 C CD  . GLN   B 53  ? 0.2830 0.3012 0.3109 0.0407  -0.0469 -0.0269 59  GLN   C CD  
1507 O OE1 . GLN   B 53  ? 0.3273 0.3465 0.3511 0.0455  -0.0532 -0.0314 59  GLN   C OE1 
1508 N NE2 . GLN   B 53  ? 0.2530 0.2751 0.2967 0.0366  -0.0448 -0.0268 59  GLN   C NE2 
1509 N N   . THR   B 54  ? 0.1872 0.1861 0.1800 0.0356  -0.0239 -0.0025 60  THR   C N   
1510 C CA  . THR   B 54  ? 0.2039 0.2010 0.1972 0.0331  -0.0202 0.0007  60  THR   C CA  
1511 C C   . THR   B 54  ? 0.1948 0.1875 0.1825 0.0307  -0.0166 0.0039  60  THR   C C   
1512 O O   . THR   B 54  ? 0.2097 0.1994 0.1910 0.0326  -0.0162 0.0047  60  THR   C O   
1513 C CB  . THR   B 54  ? 0.2410 0.2366 0.2310 0.0362  -0.0202 0.0015  60  THR   C CB  
1514 O OG1 . THR   B 54  ? 0.2861 0.2773 0.2660 0.0397  -0.0197 0.0033  60  THR   C OG1 
1515 C CG2 . THR   B 54  ? 0.2311 0.2316 0.2280 0.0389  -0.0241 -0.0016 60  THR   C CG2 
1516 N N   . GLY   B 55  ? 0.1787 0.1710 0.1690 0.0269  -0.0141 0.0056  61  GLY   C N   
1517 C CA  . GLY   B 55  ? 0.1868 0.1757 0.1740 0.0244  -0.0116 0.0081  61  GLY   C CA  
1518 C C   . GLY   B 55  ? 0.1749 0.1637 0.1641 0.0210  -0.0101 0.0091  61  GLY   C C   
1519 O O   . GLY   B 55  ? 0.1790 0.1686 0.1696 0.0214  -0.0098 0.0084  61  GLY   C O   
1520 N N   . VAL   B 56  ? 0.1581 0.1455 0.1469 0.0183  -0.0091 0.0107  62  VAL   C N   
1521 C CA  . VAL   B 56  ? 0.1596 0.1464 0.1484 0.0156  -0.0085 0.0113  62  VAL   C CA  
1522 C C   . VAL   B 56  ? 0.1545 0.1435 0.1467 0.0132  -0.0089 0.0124  62  VAL   C C   
1523 O O   . VAL   B 56  ? 0.1727 0.1615 0.1659 0.0127  -0.0089 0.0132  62  VAL   C O   
1524 C CB  . VAL   B 56  ? 0.1750 0.1569 0.1598 0.0150  -0.0076 0.0119  62  VAL   C CB  
1525 C CG1 . VAL   B 56  ? 0.1918 0.1729 0.1756 0.0124  -0.0080 0.0117  62  VAL   C CG1 
1526 C CG2 . VAL   B 56  ? 0.1822 0.1615 0.1638 0.0178  -0.0067 0.0112  62  VAL   C CG2 
1527 N N   . TYR   B 57  ? 0.1699 0.1607 0.1635 0.0120  -0.0087 0.0129  63  TYR   C N   
1528 C CA  . TYR   B 57  ? 0.1478 0.1406 0.1443 0.0101  -0.0091 0.0145  63  TYR   C CA  
1529 C C   . TYR   B 57  ? 0.1617 0.1533 0.1545 0.0089  -0.0097 0.0155  63  TYR   C C   
1530 O O   . TYR   B 57  ? 0.1714 0.1610 0.1596 0.0096  -0.0092 0.0147  63  TYR   C O   
1531 C CB  . TYR   B 57  ? 0.1611 0.1576 0.1638 0.0105  -0.0082 0.0149  63  TYR   C CB  
1532 C CG  . TYR   B 57  ? 0.1609 0.1581 0.1641 0.0109  -0.0064 0.0158  63  TYR   C CG  
1533 C CD1 . TYR   B 57  ? 0.1686 0.1657 0.1720 0.0124  -0.0051 0.0145  63  TYR   C CD1 
1534 C CD2 . TYR   B 57  ? 0.1723 0.1704 0.1761 0.0102  -0.0055 0.0184  63  TYR   C CD2 
1535 C CE1 . TYR   B 57  ? 0.1853 0.1828 0.1897 0.0131  -0.0023 0.0159  63  TYR   C CE1 
1536 C CE2 . TYR   B 57  ? 0.1855 0.1837 0.1889 0.0113  -0.0027 0.0200  63  TYR   C CE2 
1537 C CZ  . TYR   B 57  ? 0.1862 0.1840 0.1902 0.0127  -0.0008 0.0187  63  TYR   C CZ  
1538 O OH  . TYR   B 57  ? 0.2096 0.2070 0.2139 0.0141  0.0031  0.0207  63  TYR   C OH  
1539 N N   . TYR   B 58  ? 0.1669 0.1596 0.1615 0.0073  -0.0110 0.0170  64  TYR   C N   
1540 C CA  . TYR   B 58  ? 0.1686 0.1607 0.1594 0.0066  -0.0128 0.0176  64  TYR   C CA  
1541 C C   . TYR   B 58  ? 0.1746 0.1689 0.1653 0.0076  -0.0117 0.0199  64  TYR   C C   
1542 O O   . TYR   B 58  ? 0.1784 0.1754 0.1749 0.0074  -0.0109 0.0218  64  TYR   C O   
1543 C CB  . TYR   B 58  ? 0.1856 0.1781 0.1793 0.0047  -0.0154 0.0181  64  TYR   C CB  
1544 C CG  . TYR   B 58  ? 0.1915 0.1836 0.1807 0.0043  -0.0186 0.0178  64  TYR   C CG  
1545 C CD1 . TYR   B 58  ? 0.1969 0.1854 0.1793 0.0047  -0.0198 0.0152  64  TYR   C CD1 
1546 C CD2 . TYR   B 58  ? 0.1881 0.1830 0.1795 0.0041  -0.0208 0.0200  64  TYR   C CD2 
1547 C CE1 . TYR   B 58  ? 0.2114 0.1990 0.1880 0.0049  -0.0234 0.0141  64  TYR   C CE1 
1548 C CE2 . TYR   B 58  ? 0.1973 0.1919 0.1833 0.0045  -0.0247 0.0194  64  TYR   C CE2 
1549 C CZ  . TYR   B 58  ? 0.2210 0.2119 0.1993 0.0049  -0.0262 0.0161  64  TYR   C CZ  
1550 O OH  . TYR   B 58  ? 0.2537 0.2437 0.2248 0.0059  -0.0306 0.0148  64  TYR   C OH  
1551 N N   . CYS   B 59  ? 0.1743 0.1668 0.1581 0.0089  -0.0113 0.0198  65  CYS   C N   
1552 C CA  . CYS   B 59  ? 0.1750 0.1683 0.1566 0.0106  -0.0092 0.0227  65  CYS   C CA  
1553 C C   . CYS   B 59  ? 0.1882 0.1804 0.1621 0.0112  -0.0126 0.0233  65  CYS   C C   
1554 O O   . CYS   B 59  ? 0.2080 0.1969 0.1730 0.0123  -0.0136 0.0212  65  CYS   C O   
1555 C CB  . CYS   B 59  ? 0.1746 0.1662 0.1536 0.0126  -0.0053 0.0223  65  CYS   C CB  
1556 S SG  . CYS   B 59  ? 0.2175 0.2090 0.1935 0.0155  -0.0010 0.0266  65  CYS   C SG  
1557 N N   . SER   B 60  ? 0.2102 0.2050 0.1872 0.0109  -0.0145 0.0257  66  SER   C N   
1558 C CA  . SER   B 60  ? 0.2228 0.2174 0.1934 0.0117  -0.0190 0.0261  66  SER   C CA  
1559 C C   . SER   B 60  ? 0.2324 0.2244 0.1914 0.0153  -0.0177 0.0276  66  SER   C C   
1560 O O   . SER   B 60  ? 0.2573 0.2470 0.2069 0.0163  -0.0218 0.0252  66  SER   C O   
1561 C CB  . SER   B 60  ? 0.2712 0.2696 0.2489 0.0109  -0.0212 0.0289  66  SER   C CB  
1562 O OG  . SER   B 60  ? 0.3813 0.3813 0.3620 0.0127  -0.0173 0.0332  66  SER   C OG  
1563 N N   . SER   B 61  ? 0.2256 0.2175 0.1854 0.0174  -0.0117 0.0309  67  SER   C N   
1564 C CA  . SER   B 61  ? 0.2410 0.2298 0.1896 0.0216  -0.0085 0.0334  67  SER   C CA  
1565 C C   . SER   B 61  ? 0.2603 0.2448 0.1999 0.0228  -0.0072 0.0299  67  SER   C C   
1566 O O   . SER   B 61  ? 0.2945 0.2756 0.2230 0.0267  -0.0046 0.0316  67  SER   C O   
1567 C CB  . SER   B 61  ? 0.2455 0.2354 0.2002 0.0234  -0.0015 0.0384  67  SER   C CB  
1568 O OG  . SER   B 61  ? 0.2546 0.2452 0.2187 0.0217  0.0026  0.0370  67  SER   C OG  
1569 N N   . ARG   B 62  ? 0.2291 0.2129 0.1725 0.0199  -0.0088 0.0254  68  ARG   C N   
1570 C CA  . ARG   B 62  ? 0.2366 0.2159 0.1719 0.0209  -0.0081 0.0218  68  ARG   C CA  
1571 C C   . ARG   B 62  ? 0.2454 0.2232 0.1790 0.0184  -0.0145 0.0167  68  ARG   C C   
1572 O O   . ARG   B 62  ? 0.2641 0.2378 0.1921 0.0187  -0.0144 0.0130  68  ARG   C O   
1573 C CB  . ARG   B 62  ? 0.2391 0.2186 0.1819 0.0204  -0.0030 0.0214  68  ARG   C CB  
1574 C CG  . ARG   B 62  ? 0.2771 0.2579 0.2243 0.0226  0.0038  0.0258  68  ARG   C CG  
1575 C CD  . ARG   B 62  ? 0.2921 0.2683 0.2271 0.0269  0.0080  0.0270  68  ARG   C CD  
1576 N NE  . ARG   B 62  ? 0.3363 0.3132 0.2765 0.0293  0.0157  0.0317  68  ARG   C NE  
1577 C CZ  . ARG   B 62  ? 0.4027 0.3801 0.3419 0.0315  0.0185  0.0368  68  ARG   C CZ  
1578 N NH1 . ARG   B 62  ? 0.3886 0.3664 0.3212 0.0318  0.0136  0.0378  68  ARG   C NH1 
1579 N NH2 . ARG   B 62  ? 0.4198 0.3975 0.3658 0.0335  0.0264  0.0411  68  ARG   C NH2 
1580 N N   . ARG   B 63  ? 0.2473 0.2284 0.1879 0.0157  -0.0193 0.0165  69  ARG   C N   
1581 C CA  . ARG   B 63  ? 0.2546 0.2348 0.1979 0.0127  -0.0244 0.0121  69  ARG   C CA  
1582 C C   . ARG   B 63  ? 0.2637 0.2412 0.2102 0.0113  -0.0217 0.0095  69  ARG   C C   
1583 O O   . ARG   B 63  ? 0.2965 0.2702 0.2397 0.0107  -0.0238 0.0054  69  ARG   C O   
1584 C CB  . ARG   B 63  ? 0.2975 0.2747 0.2304 0.0139  -0.0300 0.0086  69  ARG   C CB  
1585 C CG  . ARG   B 63  ? 0.3827 0.3634 0.3151 0.0147  -0.0349 0.0106  69  ARG   C CG  
1586 C CD  . ARG   B 63  ? 0.4964 0.4754 0.4240 0.0143  -0.0427 0.0054  69  ARG   C CD  
1587 N NE  . ARG   B 63  ? 0.5777 0.5609 0.5060 0.0152  -0.0483 0.0074  69  ARG   C NE  
1588 C CZ  . ARG   B 63  ? 0.6406 0.6229 0.5557 0.0196  -0.0512 0.0082  69  ARG   C CZ  
1589 N NH1 . ARG   B 63  ? 0.6484 0.6251 0.5479 0.0234  -0.0489 0.0068  69  ARG   C NH1 
1590 N NH2 . ARG   B 63  ? 0.6464 0.6329 0.5632 0.0207  -0.0566 0.0104  69  ARG   C NH2 
1591 N N   . LYS   B 64  ? 0.2396 0.2191 0.1927 0.0113  -0.0171 0.0119  70  LYS   C N   
1592 C CA  . LYS   B 64  ? 0.2338 0.2111 0.1893 0.0110  -0.0145 0.0100  70  LYS   C CA  
1593 C C   . LYS   B 64  ? 0.2170 0.1977 0.1825 0.0098  -0.0130 0.0117  70  LYS   C C   
1594 O O   . LYS   B 64  ? 0.2232 0.2077 0.1934 0.0099  -0.0120 0.0144  70  LYS   C O   
1595 C CB  . LYS   B 64  ? 0.2844 0.2596 0.2344 0.0139  -0.0100 0.0104  70  LYS   C CB  
1596 C CG  . LYS   B 64  ? 0.3951 0.3648 0.3341 0.0155  -0.0106 0.0072  70  LYS   C CG  
1597 C CD  . LYS   B 64  ? 0.4841 0.4512 0.4194 0.0184  -0.0049 0.0075  70  LYS   C CD  
1598 C CE  . LYS   B 64  ? 0.5585 0.5199 0.4805 0.0209  -0.0048 0.0049  70  LYS   C CE  
1599 N NZ  . LYS   B 64  ? 0.6118 0.5733 0.5252 0.0227  -0.0067 0.0065  70  LYS   C NZ  
1600 N N   . HIS   B 65  ? 0.2008 0.1796 0.1688 0.0092  -0.0125 0.0100  71  HIS   C N   
1601 C CA  . HIS   B 65  ? 0.1981 0.1789 0.1728 0.0092  -0.0109 0.0110  71  HIS   C CA  
1602 C C   . HIS   B 65  ? 0.2226 0.2028 0.1965 0.0115  -0.0079 0.0106  71  HIS   C C   
1603 O O   . HIS   B 65  ? 0.2610 0.2375 0.2305 0.0125  -0.0070 0.0089  71  HIS   C O   
1604 C CB  . HIS   B 65  ? 0.1994 0.1781 0.1768 0.0079  -0.0118 0.0102  71  HIS   C CB  
1605 C CG  . HIS   B 65  ? 0.1891 0.1689 0.1703 0.0055  -0.0144 0.0107  71  HIS   C CG  
1606 N ND1 . HIS   B 65  ? 0.2163 0.1988 0.2036 0.0049  -0.0140 0.0127  71  HIS   C ND1 
1607 C CD2 . HIS   B 65  ? 0.1947 0.1732 0.1749 0.0039  -0.0176 0.0092  71  HIS   C CD2 
1608 C CE1 . HIS   B 65  ? 0.1970 0.1802 0.1879 0.0029  -0.0165 0.0129  71  HIS   C CE1 
1609 N NE2 . HIS   B 65  ? 0.2261 0.2072 0.2134 0.0021  -0.0192 0.0106  71  HIS   C NE2 
1610 N N   . TYR   B 66  ? 0.1951 0.1792 0.1744 0.0125  -0.0065 0.0119  72  TYR   C N   
1611 C CA  . TYR   B 66  ? 0.1868 0.1713 0.1678 0.0147  -0.0041 0.0113  72  TYR   C CA  
1612 C C   . TYR   B 66  ? 0.1901 0.1764 0.1759 0.0157  -0.0049 0.0107  72  TYR   C C   
1613 O O   . TYR   B 66  ? 0.1830 0.1719 0.1729 0.0150  -0.0062 0.0111  72  TYR   C O   
1614 C CB  . TYR   B 66  ? 0.1981 0.1861 0.1836 0.0153  -0.0019 0.0130  72  TYR   C CB  
1615 C CG  . TYR   B 66  ? 0.2037 0.1897 0.1830 0.0159  0.0000  0.0143  72  TYR   C CG  
1616 C CD1 . TYR   B 66  ? 0.2394 0.2223 0.2139 0.0179  0.0029  0.0137  72  TYR   C CD1 
1617 C CD2 . TYR   B 66  ? 0.2257 0.2126 0.2035 0.0150  -0.0008 0.0163  72  TYR   C CD2 
1618 C CE1 . TYR   B 66  ? 0.2571 0.2375 0.2239 0.0192  0.0050  0.0149  72  TYR   C CE1 
1619 C CE2 . TYR   B 66  ? 0.2353 0.2200 0.2054 0.0164  0.0008  0.0177  72  TYR   C CE2 
1620 C CZ  . TYR   B 66  ? 0.2396 0.2208 0.2035 0.0186  0.0037  0.0169  72  TYR   C CZ  
1621 O OH  . TYR   B 66  ? 0.2853 0.2638 0.2400 0.0208  0.0056  0.0185  72  TYR   C OH  
1622 N N   . PRO   B 67  ? 0.1855 0.1701 0.1703 0.0177  -0.0042 0.0096  73  PRO   C N   
1623 C CA  . PRO   B 67  ? 0.1868 0.1734 0.1752 0.0197  -0.0055 0.0090  73  PRO   C CA  
1624 C C   . PRO   B 67  ? 0.1972 0.1889 0.1937 0.0206  -0.0056 0.0084  73  PRO   C C   
1625 O O   . PRO   B 67  ? 0.2223 0.2149 0.2215 0.0211  -0.0033 0.0086  73  PRO   C O   
1626 C CB  . PRO   B 67  ? 0.2116 0.1948 0.1968 0.0220  -0.0046 0.0084  73  PRO   C CB  
1627 C CG  . PRO   B 67  ? 0.2359 0.2161 0.2176 0.0214  -0.0023 0.0082  73  PRO   C CG  
1628 C CD  . PRO   B 67  ? 0.1956 0.1762 0.1757 0.0187  -0.0024 0.0088  73  PRO   C CD  
1629 N N   . VAL   B 68  ? 0.1729 0.1676 0.1736 0.0210  -0.0079 0.0074  74  VAL   C N   
1630 C CA  . VAL   B 68  ? 0.1784 0.1780 0.1887 0.0214  -0.0085 0.0061  74  VAL   C CA  
1631 C C   . VAL   B 68  ? 0.1832 0.1852 0.1961 0.0238  -0.0123 0.0035  74  VAL   C C   
1632 O O   . VAL   B 68  ? 0.1820 0.1818 0.1886 0.0248  -0.0139 0.0034  74  VAL   C O   
1633 C CB  . VAL   B 68  ? 0.2009 0.2024 0.2158 0.0188  -0.0076 0.0071  74  VAL   C CB  
1634 C CG1 . VAL   B 68  ? 0.2296 0.2297 0.2429 0.0176  -0.0039 0.0097  74  VAL   C CG1 
1635 C CG2 . VAL   B 68  ? 0.2136 0.2137 0.2242 0.0177  -0.0092 0.0075  74  VAL   C CG2 
1636 N N   . SER   B 69  ? 0.1722 0.1786 0.1949 0.0249  -0.0136 0.0014  75  SER   C N   
1637 C CA  . SER   B 69  ? 0.1745 0.1843 0.2021 0.0268  -0.0182 -0.0022 75  SER   C CA  
1638 C C   . SER   B 69  ? 0.1680 0.1802 0.2036 0.0242  -0.0181 -0.0033 75  SER   C C   
1639 O O   . SER   B 69  ? 0.1799 0.1931 0.2224 0.0218  -0.0144 -0.0014 75  SER   C O   
1640 C CB  . SER   B 69  ? 0.2019 0.2158 0.2389 0.0291  -0.0201 -0.0045 75  SER   C CB  
1641 O OG  . SER   B 69  ? 0.2764 0.2876 0.3058 0.0319  -0.0199 -0.0032 75  SER   C OG  
1642 N N   . PHE   B 70  ? 0.1624 0.1747 0.1964 0.0250  -0.0214 -0.0058 76  PHE   C N   
1643 C CA  . PHE   B 70  ? 0.1554 0.1694 0.1971 0.0226  -0.0211 -0.0070 76  PHE   C CA  
1644 C C   . PHE   B 70  ? 0.1722 0.1887 0.2189 0.0245  -0.0263 -0.0125 76  PHE   C C   
1645 O O   . PHE   B 70  ? 0.1824 0.1982 0.2216 0.0282  -0.0303 -0.0148 76  PHE   C O   
1646 C CB  . PHE   B 70  ? 0.1619 0.1722 0.1959 0.0206  -0.0184 -0.0037 76  PHE   C CB  
1647 C CG  . PHE   B 70  ? 0.1642 0.1708 0.1858 0.0227  -0.0197 -0.0035 76  PHE   C CG  
1648 C CD1 . PHE   B 70  ? 0.1752 0.1785 0.1878 0.0233  -0.0181 -0.0006 76  PHE   C CD1 
1649 C CD2 . PHE   B 70  ? 0.1851 0.1912 0.2048 0.0241  -0.0220 -0.0062 76  PHE   C CD2 
1650 C CE1 . PHE   B 70  ? 0.1782 0.1777 0.1809 0.0254  -0.0183 0.0003  76  PHE   C CE1 
1651 C CE2 . PHE   B 70  ? 0.1860 0.1881 0.1942 0.0266  -0.0219 -0.0052 76  PHE   C CE2 
1652 C CZ  . PHE   B 70  ? 0.1812 0.1802 0.1816 0.0272  -0.0198 -0.0017 76  PHE   C CZ  
1653 N N   . SER   B 71  ? 0.1683 0.1873 0.2274 0.0224  -0.0263 -0.0147 77  SER   C N   
1654 C CA  . SER   B 71  ? 0.1771 0.1989 0.2434 0.0241  -0.0319 -0.0213 77  SER   C CA  
1655 C C   . SER   B 71  ? 0.1938 0.2124 0.2500 0.0255  -0.0340 -0.0235 77  SER   C C   
1656 O O   . SER   B 71  ? 0.2012 0.2159 0.2477 0.0247  -0.0304 -0.0194 77  SER   C O   
1657 C CB  . SER   B 71  ? 0.1895 0.2151 0.2752 0.0212  -0.0307 -0.0233 77  SER   C CB  
1658 O OG  . SER   B 71  ? 0.2112 0.2347 0.2990 0.0180  -0.0257 -0.0199 77  SER   C OG  
1659 N N   . LYS   B 72  ? 0.2218 0.2418 0.2806 0.0280  -0.0400 -0.0302 78  LYS   C N   
1660 C CA  . LYS   B 72  ? 0.2254 0.2417 0.2736 0.0301  -0.0416 -0.0326 78  LYS   C CA  
1661 C C   . LYS   B 72  ? 0.2222 0.2376 0.2788 0.0263  -0.0381 -0.0325 78  LYS   C C   
1662 O O   . LYS   B 72  ? 0.2370 0.2555 0.3096 0.0231  -0.0367 -0.0330 78  LYS   C O   
1663 C CB  . LYS   B 72  ? 0.2932 0.3110 0.3399 0.0347  -0.0498 -0.0405 78  LYS   C CB  
1664 C CG  . LYS   B 72  ? 0.3514 0.3698 0.3889 0.0393  -0.0534 -0.0402 78  LYS   C CG  
1665 C CD  . LYS   B 72  ? 0.4560 0.4728 0.4811 0.0456  -0.0604 -0.0459 78  LYS   C CD  
1666 C CE  . LYS   B 72  ? 0.5196 0.5352 0.5314 0.0510  -0.0623 -0.0434 78  LYS   C CE  
1667 N NZ  . LYS   B 72  ? 0.5713 0.5849 0.5693 0.0582  -0.0690 -0.0485 78  LYS   C NZ  
1668 N N   . PRO   B 73  ? 0.2208 0.2318 0.2676 0.0268  -0.0357 -0.0310 79  PRO   C N   
1669 C CA  . PRO   B 73  ? 0.2182 0.2283 0.2735 0.0235  -0.0320 -0.0303 79  PRO   C CA  
1670 C C   . PRO   B 73  ? 0.2213 0.2337 0.2912 0.0227  -0.0354 -0.0374 79  PRO   C C   
1671 O O   . PRO   B 73  ? 0.2514 0.2635 0.3182 0.0260  -0.0413 -0.0444 79  PRO   C O   
1672 C CB  . PRO   B 73  ? 0.2497 0.2548 0.2913 0.0254  -0.0299 -0.0287 79  PRO   C CB  
1673 C CG  . PRO   B 73  ? 0.2756 0.2786 0.3019 0.0288  -0.0306 -0.0263 79  PRO   C CG  
1674 C CD  . PRO   B 73  ? 0.2448 0.2513 0.2732 0.0307  -0.0356 -0.0294 79  PRO   C CD  
1675 N N   . SER   B 74  ? 0.1910 0.2055 0.2771 0.0186  -0.0318 -0.0357 80  SER   C N   
1676 C CA  . SER   B 74  ? 0.2021 0.2191 0.3061 0.0173  -0.0344 -0.0422 80  SER   C CA  
1677 C C   . SER   B 74  ? 0.2031 0.2193 0.3204 0.0134  -0.0281 -0.0388 80  SER   C C   
1678 O O   . SER   B 74  ? 0.1983 0.2127 0.3103 0.0120  -0.0224 -0.0312 80  SER   C O   
1679 C CB  . SER   B 74  ? 0.2271 0.2492 0.3433 0.0169  -0.0371 -0.0441 80  SER   C CB  
1680 O OG  . SER   B 74  ? 0.3020 0.3253 0.4071 0.0205  -0.0420 -0.0454 80  SER   C OG  
1681 N N   . LEU   B 75  ? 0.2149 0.2326 0.3504 0.0118  -0.0295 -0.0445 81  LEU   C N   
1682 C CA  . LEU   B 75  ? 0.2193 0.2362 0.3706 0.0084  -0.0234 -0.0418 81  LEU   C CA  
1683 C C   . LEU   B 75  ? 0.2278 0.2486 0.3941 0.0062  -0.0198 -0.0379 81  LEU   C C   
1684 O O   . LEU   B 75  ? 0.2382 0.2628 0.4174 0.0061  -0.0236 -0.0432 81  LEU   C O   
1685 C CB  . LEU   B 75  ? 0.2344 0.2503 0.3983 0.0080  -0.0268 -0.0509 81  LEU   C CB  
1686 C CG  . LEU   B 75  ? 0.2551 0.2691 0.4355 0.0049  -0.0203 -0.0486 81  LEU   C CG  
1687 C CD1 . LEU   B 75  ? 0.2662 0.2759 0.4344 0.0052  -0.0152 -0.0422 81  LEU   C CD1 
1688 C CD2 . LEU   B 75  ? 0.2810 0.2944 0.4769 0.0043  -0.0247 -0.0592 81  LEU   C CD2 
1689 N N   . ILE   B 76  ? 0.2439 0.2637 0.4071 0.0050  -0.0127 -0.0286 82  ILE   C N   
1690 C CA  . ILE   B 76  ? 0.2585 0.2808 0.4310 0.0039  -0.0081 -0.0234 82  ILE   C CA  
1691 C C   . ILE   B 76  ? 0.2580 0.2787 0.4426 0.0018  0.0002  -0.0173 82  ILE   C C   
1692 O O   . ILE   B 76  ? 0.2440 0.2615 0.4202 0.0018  0.0032  -0.0128 82  ILE   C O   
1693 C CB  . ILE   B 76  ? 0.2912 0.3130 0.4447 0.0054  -0.0071 -0.0172 82  ILE   C CB  
1694 C CG1 . ILE   B 76  ? 0.3171 0.3400 0.4580 0.0079  -0.0143 -0.0220 82  ILE   C CG1 
1695 C CG2 . ILE   B 76  ? 0.3130 0.3361 0.4723 0.0048  -0.0009 -0.0107 82  ILE   C CG2 
1696 C CD1 . ILE   B 76  ? 0.3257 0.3530 0.4773 0.0086  -0.0183 -0.0269 82  ILE   C CD1 
1697 N N   . PHE   B 77  ? 0.2551 0.2778 0.4591 0.0005  0.0044  -0.0163 83  PHE   C N   
1698 C CA  . PHE   B 77  ? 0.2428 0.2634 0.4570 -0.0007 0.0136  -0.0088 83  PHE   C CA  
1699 C C   . PHE   B 77  ? 0.2488 0.2684 0.4478 0.0009  0.0184  0.0005  83  PHE   C C   
1700 O O   . PHE   B 77  ? 0.2755 0.2972 0.4707 0.0018  0.0177  0.0010  83  PHE   C O   
1701 C CB  . PHE   B 77  ? 0.2464 0.2691 0.4874 -0.0023 0.0174  -0.0104 83  PHE   C CB  
1702 C CG  . PHE   B 77  ? 0.2612 0.2808 0.5140 -0.0032 0.0271  -0.0033 83  PHE   C CG  
1703 C CD1 . PHE   B 77  ? 0.2754 0.2920 0.5335 -0.0042 0.0277  -0.0049 83  PHE   C CD1 
1704 C CD2 . PHE   B 77  ? 0.2815 0.3005 0.5384 -0.0024 0.0361  0.0056  83  PHE   C CD2 
1705 C CE1 . PHE   B 77  ? 0.2870 0.3003 0.5556 -0.0045 0.0370  0.0024  83  PHE   C CE1 
1706 C CE2 . PHE   B 77  ? 0.2927 0.3083 0.5592 -0.0023 0.0454  0.0130  83  PHE   C CE2 
1707 C CZ  . PHE   B 77  ? 0.2866 0.2995 0.5593 -0.0035 0.0458  0.0115  83  PHE   C CZ  
1708 N N   . VAL   B 78  ? 0.2134 0.2298 0.4029 0.0014  0.0227  0.0075  84  VAL   C N   
1709 C CA  . VAL   B 78  ? 0.2158 0.2308 0.3897 0.0031  0.0263  0.0157  84  VAL   C CA  
1710 C C   . VAL   B 78  ? 0.2175 0.2303 0.4006 0.0037  0.0357  0.0238  84  VAL   C C   
1711 O O   . VAL   B 78  ? 0.2164 0.2275 0.4085 0.0030  0.0384  0.0250  84  VAL   C O   
1712 C CB  . VAL   B 78  ? 0.2335 0.2467 0.3884 0.0038  0.0226  0.0169  84  VAL   C CB  
1713 C CG1 . VAL   B 78  ? 0.2282 0.2401 0.3673 0.0056  0.0252  0.0244  84  VAL   C CG1 
1714 C CG2 . VAL   B 78  ? 0.2455 0.2599 0.3918 0.0037  0.0145  0.0095  84  VAL   C CG2 
1715 N N   . GLU   B 79  ? 0.2102 0.2225 0.3896 0.0055  0.0410  0.0299  85  GLU   C N   
1716 C CA  . GLU   B 79  ? 0.2098 0.2194 0.3952 0.0071  0.0506  0.0387  85  GLU   C CA  
1717 C C   . GLU   B 79  ? 0.2014 0.2081 0.3723 0.0088  0.0515  0.0449  85  GLU   C C   
1718 O O   . GLU   B 79  ? 0.1952 0.2024 0.3499 0.0089  0.0452  0.0433  85  GLU   C O   
1719 C CB  . GLU   B 79  ? 0.2575 0.2667 0.4402 0.0094  0.0564  0.0436  85  GLU   C CB  
1720 C CG  . GLU   B 79  ? 0.3362 0.3484 0.5382 0.0079  0.0574  0.0388  85  GLU   C CG  
1721 C CD  . GLU   B 79  ? 0.4524 0.4650 0.6815 0.0058  0.0618  0.0373  85  GLU   C CD  
1722 O OE1 . GLU   B 79  ? 0.4836 0.4928 0.7189 0.0070  0.0703  0.0446  85  GLU   C OE1 
1723 O OE2 . GLU   B 79  ? 0.4910 0.5071 0.7352 0.0032  0.0563  0.0286  85  GLU   C OE2 
1724 N N   . ALA   B 80  ? 0.2152 0.2191 0.3929 0.0105  0.0596  0.0524  86  ALA   C N   
1725 C CA  . ALA   B 80  ? 0.2405 0.2421 0.4057 0.0127  0.0604  0.0589  86  ALA   C CA  
1726 C C   . ALA   B 80  ? 0.2559 0.2573 0.3971 0.0153  0.0572  0.0621  86  ALA   C C   
1727 O O   . ALA   B 80  ? 0.2741 0.2752 0.4084 0.0169  0.0590  0.0634  86  ALA   C O   
1728 C CB  . ALA   B 80  ? 0.2609 0.2592 0.4364 0.0151  0.0706  0.0676  86  ALA   C CB  
1729 N N   . SER   B 81  ? 0.2512 0.2527 0.3806 0.0156  0.0521  0.0626  87  SER   C N   
1730 C CA  . SER   B 81  ? 0.2633 0.2647 0.3716 0.0178  0.0481  0.0650  87  SER   C CA  
1731 C C   . SER   B 81  ? 0.2896 0.2894 0.3918 0.0208  0.0499  0.0725  87  SER   C C   
1732 O O   . SER   B 81  ? 0.2884 0.2870 0.4033 0.0212  0.0549  0.0760  87  SER   C O   
1733 C CB  . SER   B 81  ? 0.2350 0.2388 0.3357 0.0152  0.0391  0.0577  87  SER   C CB  
1734 O OG  . SER   B 81  ? 0.2435 0.2479 0.3481 0.0138  0.0363  0.0564  87  SER   C OG  
1735 N N   . GLU   B 82  ? 0.3049 0.3048 0.3887 0.0230  0.0454  0.0746  88  GLU   C N   
1736 C CA  . GLU   B 82  ? 0.3274 0.3264 0.4052 0.0263  0.0458  0.0815  88  GLU   C CA  
1737 C C   . GLU   B 82  ? 0.3078 0.3087 0.3934 0.0241  0.0422  0.0797  88  GLU   C C   
1738 O O   . GLU   B 82  ? 0.3163 0.3165 0.4033 0.0267  0.0442  0.0858  88  GLU   C O   
1739 C CB  . GLU   B 82  ? 0.4001 0.3986 0.4570 0.0297  0.0416  0.0841  88  GLU   C CB  
1740 C CG  . GLU   B 82  ? 0.4943 0.4957 0.5427 0.0272  0.0320  0.0782  88  GLU   C CG  
1741 C CD  . GLU   B 82  ? 0.5852 0.5861 0.6148 0.0307  0.0274  0.0805  88  GLU   C CD  
1742 O OE1 . GLU   B 82  ? 0.5912 0.5891 0.6109 0.0346  0.0313  0.0842  88  GLU   C OE1 
1743 O OE2 . GLU   B 82  ? 0.6107 0.6140 0.6357 0.0297  0.0200  0.0783  88  GLU   C OE2 
1744 N N   . TYR   B 83  ? 0.2662 0.2691 0.3579 0.0198  0.0378  0.0717  89  TYR   C N   
1745 C CA  . TYR   B 83  ? 0.2402 0.2445 0.3379 0.0180  0.0346  0.0694  89  TYR   C CA  
1746 C C   . TYR   B 83  ? 0.2540 0.2578 0.3687 0.0150  0.0368  0.0642  89  TYR   C C   
1747 O O   . TYR   B 83  ? 0.2575 0.2615 0.3775 0.0141  0.0356  0.0631  89  TYR   C O   
1748 C CB  . TYR   B 83  ? 0.2334 0.2399 0.3199 0.0165  0.0266  0.0651  89  TYR   C CB  
1749 C CG  . TYR   B 83  ? 0.2256 0.2325 0.3068 0.0145  0.0236  0.0588  89  TYR   C CG  
1750 C CD1 . TYR   B 83  ? 0.2411 0.2474 0.3105 0.0161  0.0230  0.0599  89  TYR   C CD1 
1751 C CD2 . TYR   B 83  ? 0.2125 0.2199 0.3004 0.0117  0.0220  0.0518  89  TYR   C CD2 
1752 C CE1 . TYR   B 83  ? 0.2359 0.2424 0.3013 0.0145  0.0207  0.0545  89  TYR   C CE1 
1753 C CE2 . TYR   B 83  ? 0.2181 0.2259 0.3012 0.0105  0.0193  0.0466  89  TYR   C CE2 
1754 C CZ  . TYR   B 83  ? 0.2186 0.2260 0.2910 0.0118  0.0188  0.0481  89  TYR   C CZ  
1755 O OH  . TYR   B 83  ? 0.2192 0.2269 0.2883 0.0108  0.0168  0.0433  89  TYR   C OH  
1756 N N   . TYR   B 84  ? 0.2352 0.2382 0.3592 0.0136  0.0400  0.0609  90  TYR   C N   
1757 C CA  . TYR   B 84  ? 0.2173 0.2198 0.3587 0.0111  0.0417  0.0554  90  TYR   C CA  
1758 C C   . TYR   B 84  ? 0.2249 0.2260 0.3797 0.0112  0.0486  0.0571  90  TYR   C C   
1759 O O   . TYR   B 84  ? 0.2308 0.2321 0.3802 0.0124  0.0504  0.0593  90  TYR   C O   
1760 C CB  . TYR   B 84  ? 0.1961 0.2002 0.3363 0.0083  0.0355  0.0456  90  TYR   C CB  
1761 C CG  . TYR   B 84  ? 0.1931 0.1979 0.3249 0.0077  0.0299  0.0425  90  TYR   C CG  
1762 C CD1 . TYR   B 84  ? 0.1977 0.2013 0.3356 0.0077  0.0309  0.0430  90  TYR   C CD1 
1763 C CD2 . TYR   B 84  ? 0.1977 0.2039 0.3163 0.0074  0.0244  0.0394  90  TYR   C CD2 
1764 C CE1 . TYR   B 84  ? 0.2133 0.2173 0.3443 0.0075  0.0268  0.0405  90  TYR   C CE1 
1765 C CE2 . TYR   B 84  ? 0.1870 0.1935 0.2989 0.0071  0.0204  0.0372  90  TYR   C CE2 
1766 C CZ  . TYR   B 84  ? 0.2013 0.2067 0.3194 0.0071  0.0217  0.0377  90  TYR   C CZ  
1767 O OH  . TYR   B 84  ? 0.1944 0.1999 0.3066 0.0071  0.0187  0.0360  90  TYR   C OH  
1768 N N   . PRO   B 85  ? 0.2215 0.2212 0.3951 0.0098  0.0526  0.0553  91  PRO   C N   
1769 C CA  . PRO   B 85  ? 0.2139 0.2127 0.4038 0.0093  0.0590  0.0558  91  PRO   C CA  
1770 C C   . PRO   B 85  ? 0.2134 0.2148 0.4069 0.0067  0.0541  0.0466  91  PRO   C C   
1771 O O   . PRO   B 85  ? 0.2137 0.2172 0.3976 0.0055  0.0462  0.0400  91  PRO   C O   
1772 C CB  . PRO   B 85  ? 0.2300 0.2264 0.4394 0.0081  0.0631  0.0549  91  PRO   C CB  
1773 C CG  . PRO   B 85  ? 0.2294 0.2266 0.4338 0.0065  0.0560  0.0482  91  PRO   C CG  
1774 C CD  . PRO   B 85  ? 0.2231 0.2218 0.4051 0.0084  0.0513  0.0517  91  PRO   C CD  
1775 N N   . ALA   B 86  ? 0.1986 0.2003 0.4078 0.0060  0.0589  0.0461  92  ALA   C N   
1776 C CA  . ALA   B 86  ? 0.2224 0.2271 0.4392 0.0036  0.0541  0.0371  92  ALA   C CA  
1777 C C   . ALA   B 86  ? 0.2406 0.2458 0.4668 0.0010  0.0483  0.0275  92  ALA   C C   
1778 O O   . ALA   B 86  ? 0.2614 0.2641 0.5011 0.0003  0.0520  0.0279  92  ALA   C O   
1779 C CB  . ALA   B 86  ? 0.2267 0.2315 0.4634 0.0033  0.0615  0.0389  92  ALA   C CB  
1780 N N   . ARG   B 87  ? 0.2348 0.2423 0.4514 0.0002  0.0395  0.0196  93  ARG   C N   
1781 C CA  . ARG   B 87  ? 0.2395 0.2466 0.4600 -0.0012 0.0337  0.0107  93  ARG   C CA  
1782 C C   . ARG   B 87  ? 0.2406 0.2505 0.4517 -0.0013 0.0248  0.0024  93  ARG   C C   
1783 O O   . ARG   B 87  ? 0.2331 0.2449 0.4328 -0.0003 0.0231  0.0043  93  ARG   C O   
1784 C CB  . ARG   B 87  ? 0.2495 0.2540 0.4579 -0.0002 0.0337  0.0141  93  ARG   C CB  
1785 C CG  . ARG   B 87  ? 0.2464 0.2518 0.4315 0.0014  0.0298  0.0171  93  ARG   C CG  
1786 C CD  . ARG   B 87  ? 0.2346 0.2381 0.4110 0.0021  0.0288  0.0185  93  ARG   C CD  
1787 N NE  . ARG   B 87  ? 0.2381 0.2427 0.3953 0.0030  0.0237  0.0182  93  ARG   C NE  
1788 C CZ  . ARG   B 87  ? 0.2562 0.2598 0.4043 0.0036  0.0210  0.0172  93  ARG   C CZ  
1789 N NH1 . ARG   B 87  ? 0.2396 0.2410 0.3949 0.0035  0.0227  0.0158  93  ARG   C NH1 
1790 N NH2 . ARG   B 87  ? 0.2577 0.2624 0.3904 0.0043  0.0171  0.0174  93  ARG   C NH2 
1791 N N   . TYR   B 88  ? 0.2568 0.2663 0.4707 -0.0019 0.0191  -0.0066 94  TYR   C N   
1792 C CA  . TYR   B 88  ? 0.2754 0.2866 0.4773 -0.0010 0.0106  -0.0139 94  TYR   C CA  
1793 C C   . TYR   B 88  ? 0.2557 0.2650 0.4359 0.0007  0.0089  -0.0110 94  TYR   C C   
1794 O O   . TYR   B 88  ? 0.2783 0.2847 0.4573 0.0008  0.0111  -0.0093 94  TYR   C O   
1795 C CB  . TYR   B 88  ? 0.3060 0.3170 0.5188 -0.0016 0.0051  -0.0250 94  TYR   C CB  
1796 C CG  . TYR   B 88  ? 0.3278 0.3419 0.5627 -0.0033 0.0046  -0.0297 94  TYR   C CG  
1797 C CD1 . TYR   B 88  ? 0.3324 0.3506 0.5665 -0.0026 -0.0007 -0.0336 94  TYR   C CD1 
1798 C CD2 . TYR   B 88  ? 0.3361 0.3490 0.5940 -0.0055 0.0103  -0.0292 94  TYR   C CD2 
1799 C CE1 . TYR   B 88  ? 0.3428 0.3645 0.5993 -0.0042 -0.0011 -0.0377 94  TYR   C CE1 
1800 C CE2 . TYR   B 88  ? 0.3412 0.3571 0.6220 -0.0072 0.0105  -0.0332 94  TYR   C CE2 
1801 C CZ  . TYR   B 88  ? 0.3516 0.3722 0.6321 -0.0066 0.0045  -0.0376 94  TYR   C CZ  
1802 O OH  . TYR   B 88  ? 0.3745 0.3987 0.6799 -0.0084 0.0047  -0.0415 94  TYR   C OH  
1803 N N   . GLN   B 89  ? 0.2079 0.2186 0.3722 0.0020  0.0053  -0.0105 95  GLN   C N   
1804 C CA  . GLN   B 89  ? 0.1946 0.2038 0.3396 0.0036  0.0033  -0.0084 95  GLN   C CA  
1805 C C   . GLN   B 89  ? 0.1989 0.2084 0.3349 0.0053  -0.0038 -0.0164 95  GLN   C C   
1806 O O   . GLN   B 89  ? 0.2045 0.2167 0.3426 0.0057  -0.0073 -0.0198 95  GLN   C O   
1807 C CB  . GLN   B 89  ? 0.1933 0.2032 0.3271 0.0039  0.0058  -0.0003 95  GLN   C CB  
1808 C CG  . GLN   B 89  ? 0.2189 0.2273 0.3358 0.0051  0.0040  0.0018  95  GLN   C CG  
1809 C CD  . GLN   B 89  ? 0.1942 0.2028 0.3027 0.0052  0.0067  0.0099  95  GLN   C CD  
1810 O OE1 . GLN   B 89  ? 0.2243 0.2329 0.3384 0.0048  0.0112  0.0156  95  GLN   C OE1 
1811 N NE2 . GLN   B 89  ? 0.1998 0.2081 0.2945 0.0060  0.0040  0.0105  95  GLN   C NE2 
1812 N N   . SER   B 90  ? 0.1850 0.1917 0.3111 0.0068  -0.0057 -0.0188 96  SER   C N   
1813 C CA  . SER   B 90  ? 0.1865 0.1925 0.3020 0.0094  -0.0119 -0.0258 96  SER   C CA  
1814 C C   . SER   B 90  ? 0.1923 0.1978 0.2895 0.0113  -0.0127 -0.0218 96  SER   C C   
1815 O O   . SER   B 90  ? 0.1940 0.1990 0.2862 0.0104  -0.0088 -0.0146 96  SER   C O   
1816 C CB  . SER   B 90  ? 0.2018 0.2042 0.3169 0.0108  -0.0132 -0.0317 96  SER   C CB  
1817 O OG  . SER   B 90  ? 0.2228 0.2224 0.3295 0.0112  -0.0090 -0.0262 96  SER   C OG  
1818 N N   . HIS   B 91  ? 0.1787 0.1841 0.2664 0.0141  -0.0180 -0.0269 97  HIS   C N   
1819 C CA  . HIS   B 91  ? 0.1800 0.1842 0.2509 0.0164  -0.0187 -0.0239 97  HIS   C CA  
1820 C C   . HIS   B 91  ? 0.1891 0.1955 0.2594 0.0145  -0.0162 -0.0173 97  HIS   C C   
1821 O O   . HIS   B 91  ? 0.1961 0.2010 0.2560 0.0148  -0.0143 -0.0123 97  HIS   C O   
1822 C CB  . HIS   B 91  ? 0.1965 0.1965 0.2569 0.0178  -0.0160 -0.0217 97  HIS   C CB  
1823 C CG  . HIS   B 91  ? 0.2256 0.2224 0.2833 0.0206  -0.0183 -0.0287 97  HIS   C CG  
1824 N ND1 . HIS   B 91  ? 0.2598 0.2540 0.3030 0.0252  -0.0215 -0.0323 97  HIS   C ND1 
1825 C CD2 . HIS   B 91  ? 0.2279 0.2233 0.2950 0.0198  -0.0175 -0.0325 97  HIS   C CD2 
1826 C CE1 . HIS   B 91  ? 0.2616 0.2528 0.3045 0.0272  -0.0229 -0.0385 97  HIS   C CE1 
1827 N NE2 . HIS   B 91  ? 0.2533 0.2451 0.3110 0.0239  -0.0206 -0.0392 97  HIS   C NE2 
1828 N N   . LEU   B 92  ? 0.1709 0.1806 0.2527 0.0128  -0.0162 -0.0174 98  LEU   C N   
1829 C CA  . LEU   B 92  ? 0.1651 0.1764 0.2464 0.0114  -0.0133 -0.0114 98  LEU   C CA  
1830 C C   . LEU   B 92  ? 0.1764 0.1896 0.2546 0.0131  -0.0168 -0.0137 98  LEU   C C   
1831 O O   . LEU   B 92  ? 0.1780 0.1932 0.2629 0.0141  -0.0208 -0.0197 98  LEU   C O   
1832 C CB  . LEU   B 92  ? 0.1781 0.1911 0.2747 0.0089  -0.0091 -0.0088 98  LEU   C CB  
1833 C CG  . LEU   B 92  ? 0.1966 0.2102 0.2913 0.0080  -0.0051 -0.0020 98  LEU   C CG  
1834 C CD1 . LEU   B 92  ? 0.2084 0.2198 0.2922 0.0078  -0.0030 0.0036  98  LEU   C CD1 
1835 C CD2 . LEU   B 92  ? 0.2169 0.2318 0.3270 0.0065  -0.0005 0.0003  98  LEU   C CD2 
1836 N N   . MET   B 93  ? 0.1629 0.1755 0.2316 0.0133  -0.0154 -0.0092 99  MET   C N   
1837 C CA  . MET   B 93  ? 0.1590 0.1730 0.2245 0.0150  -0.0178 -0.0103 99  MET   C CA  
1838 C C   . MET   B 93  ? 0.1656 0.1808 0.2352 0.0133  -0.0137 -0.0056 99  MET   C C   
1839 O O   . MET   B 93  ? 0.1763 0.1897 0.2414 0.0120  -0.0102 -0.0006 99  MET   C O   
1840 C CB  . MET   B 93  ? 0.1948 0.2060 0.2444 0.0172  -0.0192 -0.0093 99  MET   C CB  
1841 C CG  . MET   B 93  ? 0.2192 0.2283 0.2626 0.0197  -0.0221 -0.0131 99  MET   C CG  
1842 S SD  . MET   B 93  ? 0.2272 0.2318 0.2530 0.0223  -0.0214 -0.0100 99  MET   C SD  
1843 C CE  . MET   B 93  ? 0.2460 0.2490 0.2720 0.0186  -0.0160 -0.0035 99  MET   C CE  
1844 N N   . LEU   B 94  ? 0.1598 0.1777 0.2369 0.0138  -0.0142 -0.0070 100 LEU   C N   
1845 C CA  . LEU   B 94  ? 0.1666 0.1850 0.2468 0.0129  -0.0094 -0.0025 100 LEU   C CA  
1846 C C   . LEU   B 94  ? 0.1543 0.1722 0.2260 0.0147  -0.0102 -0.0018 100 LEU   C C   
1847 O O   . LEU   B 94  ? 0.1701 0.1891 0.2402 0.0168  -0.0146 -0.0056 100 LEU   C O   
1848 C CB  . LEU   B 94  ? 0.1767 0.1985 0.2755 0.0121  -0.0073 -0.0038 100 LEU   C CB  
1849 C CG  . LEU   B 94  ? 0.1989 0.2210 0.3101 0.0101  -0.0050 -0.0039 100 LEU   C CG  
1850 C CD1 . LEU   B 94  ? 0.2324 0.2578 0.3641 0.0093  -0.0022 -0.0049 100 LEU   C CD1 
1851 C CD2 . LEU   B 94  ? 0.2046 0.2236 0.3092 0.0090  -0.0001 0.0024  100 LEU   C CD2 
1852 N N   . ALA   B 95  ? 0.1609 0.1769 0.2278 0.0142  -0.0059 0.0029  101 ALA   C N   
1853 C CA  . ALA   B 95  ? 0.1666 0.1817 0.2272 0.0158  -0.0053 0.0038  101 ALA   C CA  
1854 C C   . ALA   B 95  ? 0.1594 0.1742 0.2240 0.0155  0.0006  0.0077  101 ALA   C C   
1855 O O   . ALA   B 95  ? 0.1630 0.1773 0.2308 0.0143  0.0042  0.0107  101 ALA   C O   
1856 C CB  . ALA   B 95  ? 0.1778 0.1889 0.2226 0.0160  -0.0063 0.0055  101 ALA   C CB  
1857 N N   . VAL   B 96  ? 0.1651 0.1797 0.2288 0.0171  0.0022  0.0080  102 VAL   C N   
1858 C CA  . VAL   B 96  ? 0.1706 0.1837 0.2349 0.0177  0.0085  0.0119  102 VAL   C CA  
1859 C C   . VAL   B 96  ? 0.1863 0.1944 0.2332 0.0177  0.0094  0.0147  102 VAL   C C   
1860 O O   . VAL   B 96  ? 0.1985 0.2043 0.2354 0.0184  0.0067  0.0134  102 VAL   C O   
1861 C CB  . VAL   B 96  ? 0.1839 0.1987 0.2545 0.0196  0.0099  0.0108  102 VAL   C CB  
1862 C CG1 . VAL   B 96  ? 0.1946 0.2067 0.2636 0.0208  0.0174  0.0152  102 VAL   C CG1 
1863 C CG2 . VAL   B 96  ? 0.1919 0.2123 0.2812 0.0195  0.0078  0.0074  102 VAL   C CG2 
1864 N N   . GLY   B 97  ? 0.1979 0.2043 0.2419 0.0172  0.0128  0.0184  103 GLY   C N   
1865 C CA  . GLY   B 97  ? 0.2162 0.2185 0.2448 0.0173  0.0125  0.0204  103 GLY   C CA  
1866 C C   . GLY   B 97  ? 0.2152 0.2164 0.2418 0.0173  0.0155  0.0246  103 GLY   C C   
1867 O O   . GLY   B 97  ? 0.2312 0.2346 0.2688 0.0169  0.0183  0.0264  103 GLY   C O   
1868 N N   . HIS   B 98  ? 0.2152 0.2130 0.2281 0.0178  0.0147  0.0262  104 HIS   C N   
1869 C CA  . HIS   B 98  ? 0.2155 0.2120 0.2240 0.0187  0.0169  0.0305  104 HIS   C CA  
1870 C C   . HIS   B 98  ? 0.2085 0.2067 0.2182 0.0167  0.0128  0.0308  104 HIS   C C   
1871 O O   . HIS   B 98  ? 0.2057 0.2040 0.2118 0.0150  0.0078  0.0280  104 HIS   C O   
1872 C CB  . HIS   B 98  ? 0.2525 0.2446 0.2454 0.0209  0.0174  0.0316  104 HIS   C CB  
1873 C CG  . HIS   B 98  ? 0.2931 0.2836 0.2796 0.0230  0.0197  0.0362  104 HIS   C CG  
1874 N ND1 . HIS   B 98  ? 0.3207 0.3108 0.3120 0.0254  0.0269  0.0409  104 HIS   C ND1 
1875 C CD2 . HIS   B 98  ? 0.3321 0.3216 0.3089 0.0232  0.0156  0.0371  104 HIS   C CD2 
1876 C CE1 . HIS   B 98  ? 0.3535 0.3419 0.3358 0.0275  0.0271  0.0448  104 HIS   C CE1 
1877 N NE2 . HIS   B 98  ? 0.3609 0.3492 0.3344 0.0263  0.0199  0.0425  104 HIS   C NE2 
1878 N N   . SER   B 99  ? 0.2136 0.2128 0.2289 0.0170  0.0156  0.0345  105 SER   C N   
1879 C CA  . SER   B 99  ? 0.2192 0.2199 0.2365 0.0155  0.0126  0.0354  105 SER   C CA  
1880 C C   . SER   B 99  ? 0.2526 0.2529 0.2711 0.0173  0.0167  0.0411  105 SER   C C   
1881 O O   . SER   B 99  ? 0.2751 0.2758 0.3035 0.0181  0.0223  0.0434  105 SER   C O   
1882 C CB  . SER   B 99  ? 0.2287 0.2323 0.2586 0.0132  0.0111  0.0322  105 SER   C CB  
1883 O OG  . SER   B 99  ? 0.2437 0.2484 0.2766 0.0121  0.0095  0.0334  105 SER   C OG  
1884 N N   . GLU   B 100 ? 0.2469 0.2462 0.2557 0.0184  0.0141  0.0435  106 GLU   C N   
1885 C CA  . GLU   B 100 ? 0.2500 0.2487 0.2575 0.0208  0.0168  0.0494  106 GLU   C CA  
1886 C C   . GLU   B 100 ? 0.2311 0.2323 0.2446 0.0189  0.0133  0.0497  106 GLU   C C   
1887 O O   . GLU   B 100 ? 0.2009 0.2035 0.2157 0.0162  0.0085  0.0455  106 GLU   C O   
1888 C CB  . GLU   B 100 ? 0.3027 0.2986 0.2929 0.0240  0.0150  0.0514  106 GLU   C CB  
1889 C CG  . GLU   B 100 ? 0.4033 0.3958 0.3861 0.0266  0.0194  0.0515  106 GLU   C CG  
1890 C CD  . GLU   B 100 ? 0.4790 0.4679 0.4433 0.0303  0.0174  0.0524  106 GLU   C CD  
1891 O OE1 . GLU   B 100 ? 0.5560 0.5450 0.5133 0.0318  0.0136  0.0546  106 GLU   C OE1 
1892 O OE2 . GLU   B 100 ? 0.4752 0.4609 0.4318 0.0319  0.0196  0.0507  106 GLU   C OE2 
1893 N N   . PRO   B 101 ? 0.2329 0.2344 0.2502 0.0205  0.0160  0.0549  107 PRO   C N   
1894 C CA  . PRO   B 101 ? 0.2196 0.2234 0.2436 0.0188  0.0130  0.0552  107 PRO   C CA  
1895 C C   . PRO   B 101 ? 0.2270 0.2320 0.2437 0.0177  0.0056  0.0527  107 PRO   C C   
1896 O O   . PRO   B 101 ? 0.2237 0.2306 0.2472 0.0150  0.0031  0.0499  107 PRO   C O   
1897 C CB  . PRO   B 101 ? 0.2369 0.2401 0.2627 0.0220  0.0172  0.0623  107 PRO   C CB  
1898 C CG  . PRO   B 101 ? 0.2716 0.2723 0.2979 0.0243  0.0243  0.0650  107 PRO   C CG  
1899 C CD  . PRO   B 101 ? 0.2562 0.2555 0.2733 0.0242  0.0230  0.0612  107 PRO   C CD  
1900 N N   . GLY   B 102 ? 0.2220 0.2258 0.2256 0.0197  0.0024  0.0532  108 GLY   C N   
1901 C CA  . GLY   B 102 ? 0.2155 0.2207 0.2144 0.0183  -0.0048 0.0505  108 GLY   C CA  
1902 C C   . GLY   B 102 ? 0.2182 0.2233 0.2191 0.0149  -0.0072 0.0446  108 GLY   C C   
1903 O O   . GLY   B 102 ? 0.2264 0.2325 0.2269 0.0132  -0.0121 0.0421  108 GLY   C O   
1904 N N   . ASP   B 103 ? 0.1997 0.2034 0.2023 0.0143  -0.0036 0.0422  109 ASP   C N   
1905 C CA  . ASP   B 103 ? 0.1844 0.1877 0.1883 0.0118  -0.0055 0.0371  109 ASP   C CA  
1906 C C   . ASP   B 103 ? 0.1828 0.1880 0.1968 0.0097  -0.0056 0.0356  109 ASP   C C   
1907 O O   . ASP   B 103 ? 0.1776 0.1823 0.1918 0.0081  -0.0073 0.0322  109 ASP   C O   
1908 C CB  . ASP   B 103 ? 0.1909 0.1925 0.1933 0.0124  -0.0022 0.0352  109 ASP   C CB  
1909 C CG  . ASP   B 103 ? 0.2374 0.2362 0.2281 0.0146  -0.0021 0.0356  109 ASP   C CG  
1910 O OD1 . ASP   B 103 ? 0.2306 0.2284 0.2136 0.0146  -0.0066 0.0344  109 ASP   C OD1 
1911 O OD2 . ASP   B 103 ? 0.2526 0.2500 0.2423 0.0166  0.0026  0.0370  109 ASP   C OD2 
1912 N N   . CYS   B 104 ? 0.1754 0.1822 0.1976 0.0099  -0.0033 0.0384  110 CYS   C N   
1913 C CA  . CYS   B 104 ? 0.1750 0.1830 0.2060 0.0083  -0.0031 0.0367  110 CYS   C CA  
1914 C C   . CYS   B 104 ? 0.1713 0.1797 0.2009 0.0070  -0.0068 0.0355  110 CYS   C C   
1915 O O   . CYS   B 104 ? 0.1876 0.1968 0.2143 0.0072  -0.0096 0.0375  110 CYS   C O   
1916 C CB  . CYS   B 104 ? 0.1603 0.1694 0.1998 0.0089  -0.0002 0.0401  110 CYS   C CB  
1917 S SG  . CYS   B 104 ? 0.1967 0.2051 0.2439 0.0096  0.0053  0.0405  110 CYS   C SG  
1918 N N   . GLY   B 105 ? 0.1522 0.1599 0.1841 0.0059  -0.0068 0.0322  111 GLY   C N   
1919 C CA  . GLY   B 105 ? 0.1700 0.1776 0.2018 0.0049  -0.0090 0.0315  111 GLY   C CA  
1920 C C   . GLY   B 105 ? 0.1633 0.1689 0.1887 0.0044  -0.0107 0.0288  111 GLY   C C   
1921 O O   . GLY   B 105 ? 0.1752 0.1799 0.2016 0.0036  -0.0112 0.0280  111 GLY   C O   
1922 N N   . GLY   B 106 ? 0.1610 0.1654 0.1803 0.0050  -0.0108 0.0277  112 GLY   C N   
1923 C CA  . GLY   B 106 ? 0.1719 0.1738 0.1853 0.0048  -0.0119 0.0250  112 GLY   C CA  
1924 C C   . GLY   B 106 ? 0.1661 0.1668 0.1808 0.0052  -0.0104 0.0228  112 GLY   C C   
1925 O O   . GLY   B 106 ? 0.1649 0.1664 0.1826 0.0061  -0.0088 0.0219  112 GLY   C O   
1926 N N   . ILE   B 107 ? 0.1693 0.1677 0.1817 0.0048  -0.0110 0.0216  113 ILE   C N   
1927 C CA  . ILE   B 107 ? 0.1603 0.1569 0.1721 0.0061  -0.0094 0.0201  113 ILE   C CA  
1928 C C   . ILE   B 107 ? 0.1586 0.1540 0.1657 0.0077  -0.0093 0.0179  113 ILE   C C   
1929 O O   . ILE   B 107 ? 0.1709 0.1650 0.1742 0.0075  -0.0100 0.0174  113 ILE   C O   
1930 C CB  . ILE   B 107 ? 0.1907 0.1850 0.2029 0.0055  -0.0089 0.0208  113 ILE   C CB  
1931 C CG1 . ILE   B 107 ? 0.2423 0.2382 0.2612 0.0049  -0.0078 0.0229  113 ILE   C CG1 
1932 C CG2 . ILE   B 107 ? 0.1891 0.1800 0.1970 0.0076  -0.0070 0.0197  113 ILE   C CG2 
1933 C CD1 . ILE   B 107 ? 0.2937 0.2881 0.3168 0.0038  -0.0069 0.0245  113 ILE   C CD1 
1934 N N   . LEU   B 108 ? 0.1503 0.1458 0.1577 0.0096  -0.0086 0.0162  114 LEU   C N   
1935 C CA  . LEU   B 108 ? 0.1513 0.1458 0.1551 0.0118  -0.0090 0.0140  114 LEU   C CA  
1936 C C   . LEU   B 108 ? 0.1642 0.1554 0.1636 0.0137  -0.0081 0.0140  114 LEU   C C   
1937 O O   . LEU   B 108 ? 0.1626 0.1534 0.1628 0.0145  -0.0072 0.0142  114 LEU   C O   
1938 C CB  . LEU   B 108 ? 0.1525 0.1497 0.1606 0.0130  -0.0096 0.0117  114 LEU   C CB  
1939 C CG  . LEU   B 108 ? 0.1708 0.1678 0.1765 0.0158  -0.0111 0.0088  114 LEU   C CG  
1940 C CD1 . LEU   B 108 ? 0.1791 0.1761 0.1835 0.0159  -0.0110 0.0089  114 LEU   C CD1 
1941 C CD2 . LEU   B 108 ? 0.1829 0.1829 0.1949 0.0167  -0.0126 0.0057  114 LEU   C CD2 
1942 N N   . ARG   B 109 ? 0.1707 0.1591 0.1654 0.0148  -0.0078 0.0140  115 ARG   C N   
1943 C CA  . ARG   B 109 ? 0.1818 0.1663 0.1720 0.0172  -0.0060 0.0149  115 ARG   C CA  
1944 C C   . ARG   B 109 ? 0.1851 0.1680 0.1699 0.0206  -0.0065 0.0137  115 ARG   C C   
1945 O O   . ARG   B 109 ? 0.1838 0.1677 0.1689 0.0204  -0.0077 0.0126  115 ARG   C O   
1946 C CB  . ARG   B 109 ? 0.2243 0.2060 0.2159 0.0151  -0.0041 0.0173  115 ARG   C CB  
1947 C CG  . ARG   B 109 ? 0.2587 0.2393 0.2496 0.0135  -0.0051 0.0166  115 ARG   C CG  
1948 C CD  . ARG   B 109 ? 0.3300 0.3080 0.3239 0.0111  -0.0041 0.0179  115 ARG   C CD  
1949 N NE  . ARG   B 109 ? 0.4047 0.3857 0.4044 0.0079  -0.0058 0.0184  115 ARG   C NE  
1950 C CZ  . ARG   B 109 ? 0.5165 0.4978 0.5219 0.0068  -0.0045 0.0203  115 ARG   C CZ  
1951 N NH1 . ARG   B 109 ? 0.5337 0.5120 0.5392 0.0088  -0.0008 0.0221  115 ARG   C NH1 
1952 N NH2 . ARG   B 109 ? 0.5367 0.5212 0.5475 0.0043  -0.0067 0.0207  115 ARG   C NH2 
1953 N N   . CYS   B 110 ? 0.1842 0.1644 0.1638 0.0244  -0.0053 0.0142  116 CYS   C N   
1954 C CA  . CYS   B 110 ? 0.1967 0.1749 0.1700 0.0287  -0.0059 0.0137  116 CYS   C CA  
1955 C C   . CYS   B 110 ? 0.2207 0.1930 0.1892 0.0308  -0.0017 0.0171  116 CYS   C C   
1956 O O   . CYS   B 110 ? 0.2208 0.1912 0.1928 0.0282  0.0013  0.0194  116 CYS   C O   
1957 C CB  . CYS   B 110 ? 0.1775 0.1577 0.1477 0.0326  -0.0088 0.0108  116 CYS   C CB  
1958 S SG  . CYS   B 110 ? 0.1975 0.1747 0.1620 0.0357  -0.0067 0.0115  116 CYS   C SG  
1959 N N   . GLN   B 111 ? 0.2276 0.1970 0.1889 0.0358  -0.0012 0.0178  117 GLN   C N   
1960 C CA  . GLN   B 111 ? 0.2488 0.2118 0.2057 0.0384  0.0038  0.0219  117 GLN   C CA  
1961 C C   . GLN   B 111 ? 0.2572 0.2179 0.2117 0.0400  0.0073  0.0240  117 GLN   C C   
1962 O O   . GLN   B 111 ? 0.2830 0.2386 0.2375 0.0407  0.0128  0.0280  117 GLN   C O   
1963 C CB  . GLN   B 111 ? 0.2610 0.2210 0.2096 0.0445  0.0039  0.0229  117 GLN   C CB  
1964 C CG  . GLN   B 111 ? 0.2998 0.2613 0.2402 0.0502  0.0005  0.0209  117 GLN   C CG  
1965 C CD  . GLN   B 111 ? 0.4271 0.3864 0.3594 0.0567  -0.0005 0.0218  117 GLN   C CD  
1966 O OE1 . GLN   B 111 ? 0.4440 0.4071 0.3783 0.0572  -0.0049 0.0191  117 GLN   C OE1 
1967 N NE2 . GLN   B 111 ? 0.4550 0.4081 0.3779 0.0622  0.0039  0.0258  117 GLN   C NE2 
1968 N N   . HIS   B 112 ? 0.2409 0.2048 0.1944 0.0406  0.0047  0.0213  118 HIS   C N   
1969 C CA  . HIS   B 112 ? 0.2463 0.2076 0.1967 0.0428  0.0083  0.0230  118 HIS   C CA  
1970 C C   . HIS   B 112 ? 0.2516 0.2147 0.2119 0.0374  0.0102  0.0239  118 HIS   C C   
1971 O O   . HIS   B 112 ? 0.2804 0.2408 0.2399 0.0389  0.0145  0.0261  118 HIS   C O   
1972 C CB  . HIS   B 112 ? 0.2506 0.2132 0.1934 0.0473  0.0047  0.0193  118 HIS   C CB  
1973 C CG  . HIS   B 112 ? 0.2504 0.2118 0.1835 0.0532  0.0018  0.0182  118 HIS   C CG  
1974 N ND1 . HIS   B 112 ? 0.2478 0.2143 0.1830 0.0531  -0.0048 0.0137  118 HIS   C ND1 
1975 C CD2 . HIS   B 112 ? 0.3070 0.2627 0.2285 0.0599  0.0048  0.0213  118 HIS   C CD2 
1976 C CE1 . HIS   B 112 ? 0.2905 0.2547 0.2160 0.0594  -0.0063 0.0140  118 HIS   C CE1 
1977 N NE2 . HIS   B 112 ? 0.3150 0.2726 0.2313 0.0639  -0.0006 0.0186  118 HIS   C NE2 
1978 N N   . GLY   B 113 ? 0.2317 0.1992 0.2007 0.0319  0.0071  0.0223  119 GLY   C N   
1979 C CA  . GLY   B 113 ? 0.2183 0.1882 0.1967 0.0272  0.0079  0.0232  119 GLY   C CA  
1980 C C   . GLY   B 113 ? 0.2055 0.1812 0.1891 0.0238  0.0033  0.0201  119 GLY   C C   
1981 O O   . GLY   B 113 ? 0.1996 0.1775 0.1821 0.0237  -0.0002 0.0177  119 GLY   C O   
1982 N N   . VAL   B 114 ? 0.2053 0.1832 0.1953 0.0215  0.0038  0.0206  120 VAL   C N   
1983 C CA  . VAL   B 114 ? 0.1929 0.1756 0.1885 0.0185  0.0005  0.0188  120 VAL   C CA  
1984 C C   . VAL   B 114 ? 0.1920 0.1761 0.1848 0.0210  -0.0015 0.0153  120 VAL   C C   
1985 O O   . VAL   B 114 ? 0.2044 0.1866 0.1940 0.0239  0.0001  0.0146  120 VAL   C O   
1986 C CB  . VAL   B 114 ? 0.1920 0.1765 0.1959 0.0155  0.0018  0.0210  120 VAL   C CB  
1987 C CG1 . VAL   B 114 ? 0.2080 0.1969 0.2169 0.0134  -0.0009 0.0197  120 VAL   C CG1 
1988 C CG2 . VAL   B 114 ? 0.2166 0.2005 0.2252 0.0127  0.0025  0.0235  120 VAL   C CG2 
1989 N N   . VAL   B 115 ? 0.1684 0.1555 0.1626 0.0203  -0.0049 0.0128  121 VAL   C N   
1990 C CA  . VAL   B 115 ? 0.1754 0.1646 0.1702 0.0220  -0.0076 0.0087  121 VAL   C CA  
1991 C C   . VAL   B 115 ? 0.1842 0.1765 0.1876 0.0194  -0.0078 0.0081  121 VAL   C C   
1992 O O   . VAL   B 115 ? 0.1831 0.1756 0.1878 0.0208  -0.0085 0.0051  121 VAL   C O   
1993 C CB  . VAL   B 115 ? 0.1713 0.1623 0.1656 0.0226  -0.0105 0.0067  121 VAL   C CB  
1994 C CG1 . VAL   B 115 ? 0.1881 0.1820 0.1862 0.0239  -0.0137 0.0021  121 VAL   C CG1 
1995 C CG2 . VAL   B 115 ? 0.1993 0.1871 0.1852 0.0258  -0.0101 0.0075  121 VAL   C CG2 
1996 N N   . GLY   B 116 ? 0.1705 0.1648 0.1794 0.0159  -0.0072 0.0107  122 GLY   C N   
1997 C CA  . GLY   B 116 ? 0.1884 0.1853 0.2054 0.0138  -0.0069 0.0111  122 GLY   C CA  
1998 C C   . GLY   B 116 ? 0.1606 0.1593 0.1807 0.0109  -0.0066 0.0145  122 GLY   C C   
1999 O O   . GLY   B 116 ? 0.1672 0.1647 0.1834 0.0103  -0.0068 0.0161  122 GLY   C O   
2000 N N   . ILE   B 117 ? 0.1459 0.1469 0.1729 0.0095  -0.0061 0.0156  123 ILE   C N   
2001 C CA  . ILE   B 117 ? 0.1491 0.1515 0.1774 0.0077  -0.0061 0.0190  123 ILE   C CA  
2002 C C   . ILE   B 117 ? 0.1554 0.1597 0.1880 0.0075  -0.0055 0.0190  123 ILE   C C   
2003 O O   . ILE   B 117 ? 0.1604 0.1655 0.1991 0.0079  -0.0048 0.0171  123 ILE   C O   
2004 C CB  . ILE   B 117 ? 0.1599 0.1631 0.1924 0.0066  -0.0053 0.0222  123 ILE   C CB  
2005 C CG1 . ILE   B 117 ? 0.1872 0.1910 0.2266 0.0071  -0.0035 0.0217  123 ILE   C CG1 
2006 C CG2 . ILE   B 117 ? 0.1825 0.1842 0.2124 0.0064  -0.0055 0.0232  123 ILE   C CG2 
2007 C CD1 . ILE   B 117 ? 0.1819 0.1869 0.2271 0.0063  -0.0025 0.0256  123 ILE   C CD1 
2008 N N   . VAL   B 118 ? 0.1497 0.1544 0.1796 0.0070  -0.0055 0.0214  124 VAL   C N   
2009 C CA  . VAL   B 118 ? 0.1546 0.1605 0.1884 0.0073  -0.0036 0.0226  124 VAL   C CA  
2010 C C   . VAL   B 118 ? 0.1619 0.1691 0.2040 0.0070  -0.0016 0.0248  124 VAL   C C   
2011 O O   . VAL   B 118 ? 0.1511 0.1585 0.1933 0.0066  -0.0019 0.0275  124 VAL   C O   
2012 C CB  . VAL   B 118 ? 0.1490 0.1542 0.1760 0.0076  -0.0036 0.0253  124 VAL   C CB  
2013 C CG1 . VAL   B 118 ? 0.1644 0.1702 0.1947 0.0085  -0.0003 0.0277  124 VAL   C CG1 
2014 C CG2 . VAL   B 118 ? 0.1756 0.1790 0.1952 0.0079  -0.0051 0.0229  124 VAL   C CG2 
2015 N N   . SER   B 119 ? 0.1479 0.1558 0.1979 0.0072  0.0006  0.0238  125 SER   C N   
2016 C CA  . SER   B 119 ? 0.1558 0.1643 0.2155 0.0070  0.0032  0.0256  125 SER   C CA  
2017 C C   . SER   B 119 ? 0.1722 0.1812 0.2386 0.0074  0.0071  0.0280  125 SER   C C   
2018 O O   . SER   B 119 ? 0.1622 0.1711 0.2344 0.0077  0.0102  0.0319  125 SER   C O   
2019 C CB  . SER   B 119 ? 0.1651 0.1735 0.2309 0.0067  0.0023  0.0209  125 SER   C CB  
2020 O OG  . SER   B 119 ? 0.1825 0.1909 0.2590 0.0063  0.0052  0.0221  125 SER   C OG  
2021 N N   . THR   B 120 ? 0.1695 0.1789 0.2367 0.0078  0.0076  0.0260  126 THR   C N   
2022 C CA  . THR   B 120 ? 0.1647 0.1744 0.2405 0.0083  0.0124  0.0284  126 THR   C CA  
2023 C C   . THR   B 120 ? 0.1569 0.1659 0.2252 0.0096  0.0137  0.0300  126 THR   C C   
2024 O O   . THR   B 120 ? 0.1667 0.1753 0.2255 0.0097  0.0103  0.0277  126 THR   C O   
2025 C CB  . THR   B 120 ? 0.1748 0.1859 0.2656 0.0074  0.0130  0.0237  126 THR   C CB  
2026 O OG1 . THR   B 120 ? 0.1771 0.1895 0.2665 0.0076  0.0097  0.0188  126 THR   C OG1 
2027 C CG2 . THR   B 120 ? 0.1937 0.2048 0.2916 0.0064  0.0115  0.0207  126 THR   C CG2 
2028 N N   . GLY   B 121 ? 0.1809 0.1893 0.2538 0.0109  0.0193  0.0340  127 GLY   C N   
2029 C CA  . GLY   B 121 ? 0.2116 0.2189 0.2781 0.0126  0.0217  0.0356  127 GLY   C CA  
2030 C C   . GLY   B 121 ? 0.2547 0.2615 0.3316 0.0140  0.0291  0.0394  127 GLY   C C   
2031 O O   . GLY   B 121 ? 0.2741 0.2809 0.3612 0.0138  0.0327  0.0421  127 GLY   C O   
2032 N N   . GLY   B 122 ? 0.2864 0.2924 0.3608 0.0156  0.0322  0.0402  128 GLY   C N   
2033 C CA  . GLY   B 122 ? 0.3084 0.3136 0.3932 0.0172  0.0405  0.0443  128 GLY   C CA  
2034 C C   . GLY   B 122 ? 0.3059 0.3136 0.4030 0.0165  0.0414  0.0403  128 GLY   C C   
2035 O O   . GLY   B 122 ? 0.2910 0.3015 0.3920 0.0146  0.0352  0.0340  128 GLY   C O   
2036 N N   . ASN   B 123 ? 0.2951 0.3017 0.3990 0.0186  0.0494  0.0443  129 ASN   C N   
2037 C CA  . ASN   B 123 ? 0.2951 0.3042 0.4126 0.0184  0.0512  0.0413  129 ASN   C CA  
2038 C C   . ASN   B 123 ? 0.2754 0.2852 0.3815 0.0186  0.0452  0.0367  129 ASN   C C   
2039 O O   . ASN   B 123 ? 0.3077 0.3209 0.4253 0.0179  0.0434  0.0324  129 ASN   C O   
2040 C CB  . ASN   B 123 ? 0.3289 0.3425 0.4706 0.0154  0.0495  0.0366  129 ASN   C CB  
2041 C CG  . ASN   B 123 ? 0.4105 0.4245 0.5739 0.0156  0.0586  0.0402  129 ASN   C CG  
2042 O OD1 . ASN   B 123 ? 0.4265 0.4376 0.5890 0.0185  0.0678  0.0468  129 ASN   C OD1 
2043 N ND2 . ASN   B 123 ? 0.4234 0.4408 0.6076 0.0128  0.0566  0.0359  129 ASN   C ND2 
2044 N N   . GLY   B 124 ? 0.2527 0.2594 0.3377 0.0197  0.0423  0.0375  130 GLY   C N   
2045 C CA  . GLY   B 124 ? 0.2462 0.2526 0.3207 0.0199  0.0373  0.0335  130 GLY   C CA  
2046 C C   . GLY   B 124 ? 0.2097 0.2192 0.2860 0.0175  0.0287  0.0274  130 GLY   C C   
2047 O O   . GLY   B 124 ? 0.2132 0.2230 0.2848 0.0178  0.0250  0.0240  130 GLY   C O   
2048 N N   . LEU   B 125 ? 0.1896 0.2005 0.2714 0.0155  0.0259  0.0263  131 LEU   C N   
2049 C CA  . LEU   B 125 ? 0.1927 0.2057 0.2746 0.0138  0.0184  0.0210  131 LEU   C CA  
2050 C C   . LEU   B 125 ? 0.1882 0.1991 0.2582 0.0130  0.0157  0.0223  131 LEU   C C   
2051 O O   . LEU   B 125 ? 0.2177 0.2270 0.2856 0.0132  0.0191  0.0269  131 LEU   C O   
2052 C CB  . LEU   B 125 ? 0.2016 0.2182 0.3021 0.0124  0.0175  0.0176  131 LEU   C CB  
2053 C CG  . LEU   B 125 ? 0.2438 0.2635 0.3605 0.0129  0.0199  0.0159  131 LEU   C CG  
2054 C CD1 . LEU   B 125 ? 0.2894 0.3116 0.4270 0.0112  0.0218  0.0146  131 LEU   C CD1 
2055 C CD2 . LEU   B 125 ? 0.2535 0.2755 0.3684 0.0137  0.0139  0.0107  131 LEU   C CD2 
2056 N N   . VAL   B 126 ? 0.1608 0.1716 0.2237 0.0124  0.0100  0.0189  132 VAL   C N   
2057 C CA  . VAL   B 126 ? 0.1494 0.1589 0.2041 0.0114  0.0073  0.0197  132 VAL   C CA  
2058 C C   . VAL   B 126 ? 0.1474 0.1587 0.2084 0.0105  0.0033  0.0151  132 VAL   C C   
2059 O O   . VAL   B 126 ? 0.1586 0.1712 0.2215 0.0112  0.0002  0.0108  132 VAL   C O   
2060 C CB  . VAL   B 126 ? 0.1580 0.1648 0.1977 0.0118  0.0049  0.0200  132 VAL   C CB  
2061 C CG1 . VAL   B 126 ? 0.1821 0.1889 0.2191 0.0126  0.0022  0.0163  132 VAL   C CG1 
2062 C CG2 . VAL   B 126 ? 0.1627 0.1686 0.1967 0.0107  0.0020  0.0206  132 VAL   C CG2 
2063 N N   . GLY   B 127 ? 0.1543 0.1655 0.2179 0.0095  0.0034  0.0161  133 GLY   C N   
2064 C CA  . GLY   B 127 ? 0.1502 0.1621 0.2180 0.0090  0.0001  0.0118  133 GLY   C CA  
2065 C C   . GLY   B 127 ? 0.1573 0.1673 0.2151 0.0088  -0.0020 0.0124  133 GLY   C C   
2066 O O   . GLY   B 127 ? 0.1538 0.1628 0.2076 0.0083  -0.0005 0.0166  133 GLY   C O   
2067 N N   . PHE   B 128 ? 0.1355 0.1450 0.1899 0.0097  -0.0055 0.0083  134 PHE   C N   
2068 C CA  . PHE   B 128 ? 0.1524 0.1598 0.1985 0.0099  -0.0067 0.0090  134 PHE   C CA  
2069 C C   . PHE   B 128 ? 0.1603 0.1674 0.2103 0.0103  -0.0075 0.0058  134 PHE   C C   
2070 O O   . PHE   B 128 ? 0.1666 0.1744 0.2202 0.0115  -0.0098 0.0009  134 PHE   C O   
2071 C CB  . PHE   B 128 ? 0.1466 0.1525 0.1827 0.0114  -0.0089 0.0075  134 PHE   C CB  
2072 C CG  . PHE   B 128 ? 0.1530 0.1588 0.1852 0.0113  -0.0083 0.0094  134 PHE   C CG  
2073 C CD1 . PHE   B 128 ? 0.1575 0.1617 0.1838 0.0103  -0.0072 0.0130  134 PHE   C CD1 
2074 C CD2 . PHE   B 128 ? 0.1606 0.1677 0.1955 0.0125  -0.0089 0.0073  134 PHE   C CD2 
2075 C CE1 . PHE   B 128 ? 0.1620 0.1653 0.1838 0.0105  -0.0067 0.0140  134 PHE   C CE1 
2076 C CE2 . PHE   B 128 ? 0.1686 0.1750 0.1996 0.0127  -0.0077 0.0089  134 PHE   C CE2 
2077 C CZ  . PHE   B 128 ? 0.1619 0.1661 0.1859 0.0118  -0.0065 0.0121  134 PHE   C CZ  
2078 N N   . ALA   B 129 ? 0.1493 0.1551 0.1984 0.0097  -0.0060 0.0084  135 ALA   C N   
2079 C CA  . ALA   B 129 ? 0.1557 0.1602 0.2067 0.0105  -0.0062 0.0056  135 ALA   C CA  
2080 C C   . ALA   B 129 ? 0.1697 0.1717 0.2098 0.0128  -0.0079 0.0037  135 ALA   C C   
2081 O O   . ALA   B 129 ? 0.1729 0.1736 0.2068 0.0126  -0.0068 0.0071  135 ALA   C O   
2082 C CB  . ALA   B 129 ? 0.1689 0.1731 0.2236 0.0093  -0.0033 0.0096  135 ALA   C CB  
2083 N N   . ASP   B 130 ? 0.1588 0.1601 0.1971 0.0152  -0.0104 -0.0016 136 ASP   C N   
2084 C CA  . ASP   B 130 ? 0.1763 0.1746 0.2031 0.0184  -0.0115 -0.0030 136 ASP   C CA  
2085 C C   . ASP   B 130 ? 0.1936 0.1888 0.2169 0.0192  -0.0085 -0.0013 136 ASP   C C   
2086 O O   . ASP   B 130 ? 0.1928 0.1879 0.2224 0.0185  -0.0072 -0.0023 136 ASP   C O   
2087 C CB  . ASP   B 130 ? 0.2022 0.2005 0.2276 0.0214  -0.0157 -0.0098 136 ASP   C CB  
2088 C CG  . ASP   B 130 ? 0.2619 0.2570 0.2738 0.0259  -0.0170 -0.0111 136 ASP   C CG  
2089 O OD1 . ASP   B 130 ? 0.2430 0.2372 0.2484 0.0266  -0.0163 -0.0078 136 ASP   C OD1 
2090 O OD2 . ASP   B 130 ? 0.2887 0.2814 0.2959 0.0292  -0.0185 -0.0154 136 ASP   C OD2 
2091 N N   . VAL   B 131 ? 0.1834 0.1757 0.1973 0.0211  -0.0070 0.0010  137 VAL   C N   
2092 C CA  . VAL   B 131 ? 0.1996 0.1884 0.2099 0.0227  -0.0034 0.0027  137 VAL   C CA  
2093 C C   . VAL   B 131 ? 0.2114 0.1958 0.2090 0.0278  -0.0032 0.0008  137 VAL   C C   
2094 O O   . VAL   B 131 ? 0.2164 0.1971 0.2095 0.0301  0.0006  0.0024  137 VAL   C O   
2095 C CB  . VAL   B 131 ? 0.1973 0.1864 0.2108 0.0201  0.0000  0.0087  137 VAL   C CB  
2096 C CG1 . VAL   B 131 ? 0.1974 0.1904 0.2216 0.0162  -0.0004 0.0108  137 VAL   C CG1 
2097 C CG2 . VAL   B 131 ? 0.1937 0.1820 0.2019 0.0201  -0.0002 0.0112  137 VAL   C CG2 
2098 N N   . ARG   B 132 ? 0.2000 0.1847 0.1917 0.0302  -0.0070 -0.0021 138 ARG   C N   
2099 C CA  . ARG   B 132 ? 0.2034 0.1836 0.1813 0.0359  -0.0069 -0.0031 138 ARG   C CA  
2100 C C   . ARG   B 132 ? 0.2283 0.2053 0.1995 0.0403  -0.0074 -0.0076 138 ARG   C C   
2101 O O   . ARG   B 132 ? 0.2543 0.2263 0.2127 0.0456  -0.0053 -0.0069 138 ARG   C O   
2102 C CB  . ARG   B 132 ? 0.2009 0.1829 0.1751 0.0375  -0.0114 -0.0051 138 ARG   C CB  
2103 C CG  . ARG   B 132 ? 0.1998 0.1833 0.1775 0.0342  -0.0101 -0.0004 138 ARG   C CG  
2104 C CD  . ARG   B 132 ? 0.2029 0.1880 0.1777 0.0362  -0.0143 -0.0025 138 ARG   C CD  
2105 N NE  . ARG   B 132 ? 0.1944 0.1844 0.1784 0.0344  -0.0188 -0.0072 138 ARG   C NE  
2106 C CZ  . ARG   B 132 ? 0.2101 0.2030 0.1962 0.0353  -0.0227 -0.0096 138 ARG   C CZ  
2107 N NH1 . ARG   B 132 ? 0.2020 0.1933 0.1800 0.0385  -0.0233 -0.0082 138 ARG   C NH1 
2108 N NH2 . ARG   B 132 ? 0.2097 0.2071 0.2071 0.0331  -0.0257 -0.0133 138 ARG   C NH2 
2109 N N   . ASP   B 133 ? 0.2190 0.1979 0.1983 0.0385  -0.0094 -0.0120 139 ASP   C N   
2110 C CA  . ASP   B 133 ? 0.2241 0.1995 0.1974 0.0427  -0.0102 -0.0174 139 ASP   C CA  
2111 C C   . ASP   B 133 ? 0.2354 0.2071 0.2090 0.0427  -0.0036 -0.0142 139 ASP   C C   
2112 O O   . ASP   B 133 ? 0.2432 0.2107 0.2099 0.0467  -0.0030 -0.0183 139 ASP   C O   
2113 C CB  . ASP   B 133 ? 0.2266 0.2054 0.2101 0.0409  -0.0156 -0.0246 139 ASP   C CB  
2114 C CG  . ASP   B 133 ? 0.2767 0.2586 0.2763 0.0349  -0.0131 -0.0224 139 ASP   C CG  
2115 O OD1 . ASP   B 133 ? 0.2549 0.2394 0.2599 0.0312  -0.0106 -0.0163 139 ASP   C OD1 
2116 O OD2 . ASP   B 133 ? 0.2820 0.2635 0.2885 0.0343  -0.0135 -0.0266 139 ASP   C OD2 
2117 N N   . LEU   B 134 ? 0.2273 0.2005 0.2089 0.0385  0.0011  -0.0075 140 LEU   C N   
2118 C CA  . LEU   B 134 ? 0.2264 0.1971 0.2114 0.0382  0.0072  -0.0042 140 LEU   C CA  
2119 C C   . LEU   B 134 ? 0.2442 0.2100 0.2184 0.0421  0.0126  0.0002  140 LEU   C C   
2120 O O   . LEU   B 134 ? 0.2400 0.2065 0.2187 0.0398  0.0162  0.0064  140 LEU   C O   
2121 C CB  . LEU   B 134 ? 0.2208 0.1964 0.2207 0.0320  0.0085  0.0006  140 LEU   C CB  
2122 C CG  . LEU   B 134 ? 0.2242 0.2044 0.2352 0.0282  0.0044  -0.0023 140 LEU   C CG  
2123 C CD1 . LEU   B 134 ? 0.2378 0.2223 0.2603 0.0233  0.0057  0.0034  140 LEU   C CD1 
2124 C CD2 . LEU   B 134 ? 0.2559 0.2343 0.2702 0.0294  0.0041  -0.0077 140 LEU   C CD2 
2125 N N   . LEU   B 135 ? 0.2572 0.2177 0.2170 0.0486  0.0129  -0.0031 141 LEU   C N   
2126 C CA  . LEU   B 135 ? 0.2737 0.2285 0.2214 0.0536  0.0187  0.0015  141 LEU   C CA  
2127 C C   . LEU   B 135 ? 0.2726 0.2248 0.2254 0.0530  0.0271  0.0073  141 LEU   C C   
2128 O O   . LEU   B 135 ? 0.2783 0.2277 0.2284 0.0545  0.0327  0.0131  141 LEU   C O   
2129 C CB  . LEU   B 135 ? 0.2857 0.2346 0.2146 0.0617  0.0172  -0.0034 141 LEU   C CB  
2130 C CG  . LEU   B 135 ? 0.2860 0.2380 0.2108 0.0628  0.0075  -0.0103 141 LEU   C CG  
2131 C CD1 . LEU   B 135 ? 0.3241 0.2703 0.2289 0.0718  0.0054  -0.0152 141 LEU   C CD1 
2132 C CD2 . LEU   B 135 ? 0.2995 0.2556 0.2275 0.0601  0.0048  -0.0070 141 LEU   C CD2 
2133 N N   . TRP   B 136 ? 0.2625 0.2157 0.2241 0.0510  0.0285  0.0058  142 TRP   C N   
2134 C CA  . TRP   B 136 ? 0.2730 0.2242 0.2414 0.0507  0.0365  0.0111  142 TRP   C CA  
2135 C C   . TRP   B 136 ? 0.2830 0.2390 0.2654 0.0450  0.0381  0.0178  142 TRP   C C   
2136 O O   . TRP   B 136 ? 0.2995 0.2540 0.2880 0.0451  0.0449  0.0230  142 TRP   C O   
2137 C CB  . TRP   B 136 ? 0.2707 0.2221 0.2462 0.0497  0.0370  0.0078  142 TRP   C CB  
2138 C CG  . TRP   B 136 ? 0.2575 0.2154 0.2455 0.0440  0.0305  0.0048  142 TRP   C CG  
2139 C CD1 . TRP   B 136 ? 0.2630 0.2219 0.2493 0.0440  0.0241  -0.0024 142 TRP   C CD1 
2140 C CD2 . TRP   B 136 ? 0.2394 0.2033 0.2441 0.0379  0.0303  0.0093  142 TRP   C CD2 
2141 N NE1 . TRP   B 136 ? 0.2594 0.2243 0.2607 0.0382  0.0209  -0.0021 142 TRP   C NE1 
2142 C CE2 . TRP   B 136 ? 0.2481 0.2159 0.2594 0.0347  0.0245  0.0051  142 TRP   C CE2 
2143 C CE3 . TRP   B 136 ? 0.2492 0.2155 0.2639 0.0350  0.0342  0.0162  142 TRP   C CE3 
2144 C CZ2 . TRP   B 136 ? 0.2480 0.2216 0.2735 0.0294  0.0230  0.0083  142 TRP   C CZ2 
2145 C CZ3 . TRP   B 136 ? 0.2528 0.2253 0.2816 0.0298  0.0316  0.0186  142 TRP   C CZ3 
2146 C CH2 . TRP   B 136 ? 0.2497 0.2254 0.2826 0.0273  0.0263  0.0150  142 TRP   C CH2 
2147 N N   . LEU   B 137 ? 0.2591 0.2205 0.2470 0.0404  0.0321  0.0176  143 LEU   C N   
2148 C CA  . LEU   B 137 ? 0.2597 0.2251 0.2593 0.0356  0.0328  0.0231  143 LEU   C CA  
2149 C C   . LEU   B 137 ? 0.3008 0.2620 0.2961 0.0381  0.0385  0.0279  143 LEU   C C   
2150 O O   . LEU   B 137 ? 0.3238 0.2870 0.3304 0.0349  0.0412  0.0327  143 LEU   C O   
2151 C CB  . LEU   B 137 ? 0.2535 0.2242 0.2564 0.0313  0.0257  0.0214  143 LEU   C CB  
2152 C CG  . LEU   B 137 ? 0.2457 0.2212 0.2571 0.0278  0.0211  0.0187  143 LEU   C CG  
2153 C CD1 . LEU   B 137 ? 0.2569 0.2362 0.2683 0.0252  0.0151  0.0169  143 LEU   C CD1 
2154 C CD2 . LEU   B 137 ? 0.2446 0.2234 0.2699 0.0243  0.0232  0.0228  143 LEU   C CD2 
2155 N N   . ASP   B 138 ? 0.2989 0.2543 0.2783 0.0441  0.0403  0.0267  144 ASP   C N   
2156 C CA  . ASP   B 138 ? 0.3393 0.2898 0.3133 0.0473  0.0464  0.0316  144 ASP   C CA  
2157 C C   . ASP   B 138 ? 0.3793 0.3244 0.3537 0.0510  0.0564  0.0361  144 ASP   C C   
2158 O O   . ASP   B 138 ? 0.3922 0.3325 0.3627 0.0542  0.0628  0.0409  144 ASP   C O   
2159 C CB  . ASP   B 138 ? 0.3464 0.2926 0.3023 0.0531  0.0444  0.0292  144 ASP   C CB  
2160 C CG  . ASP   B 138 ? 0.3780 0.3288 0.3337 0.0501  0.0359  0.0259  144 ASP   C CG  
2161 O OD1 . ASP   B 138 ? 0.3683 0.3247 0.3369 0.0437  0.0326  0.0265  144 ASP   C OD1 
2162 O OD2 . ASP   B 138 ? 0.4111 0.3597 0.3533 0.0548  0.0325  0.0227  144 ASP   C OD2 
2163 N N   . GLU   B 139 ? 0.3963 0.3416 0.3751 0.0511  0.0584  0.0349  145 GLU   C N   
2164 C CA  . GLU   B 139 ? 0.4480 0.3879 0.4270 0.0552  0.0686  0.0391  145 GLU   C CA  
2165 C C   . GLU   B 139 ? 0.4899 0.4335 0.4848 0.0517  0.0704  0.0399  145 GLU   C C   
2166 O O   . GLU   B 139 ? 0.4894 0.4393 0.4932 0.0466  0.0635  0.0370  145 GLU   C O   
2167 C CB  . GLU   B 139 ? 0.5061 0.4381 0.4635 0.0637  0.0712  0.0358  145 GLU   C CB  
2168 C CG  . GLU   B 139 ? 0.6034 0.5364 0.5568 0.0641  0.0655  0.0282  145 GLU   C CG  
2169 C CD  . GLU   B 139 ? 0.7359 0.6662 0.6706 0.0689  0.0591  0.0213  145 GLU   C CD  
2170 O OE1 . GLU   B 139 ? 0.7631 0.6923 0.6932 0.0706  0.0558  0.0148  145 GLU   C OE1 
2171 O OE2 . GLU   B 139 ? 0.7926 0.7218 0.7180 0.0710  0.0570  0.0222  145 GLU   C OE2 
2172 N N   . GLU   B 140 ? 0.5179 0.4571 0.5158 0.0550  0.0803  0.0441  146 GLU   C N   
2173 C CA  . GLU   B 140 ? 0.5390 0.4805 0.5505 0.0531  0.0832  0.0450  146 GLU   C CA  
2174 C C   . GLU   B 140 ? 0.5619 0.5129 0.5942 0.0452  0.0773  0.0463  146 GLU   C C   
2175 O O   . GLU   B 140 ? 0.5727 0.5266 0.6202 0.0432  0.0803  0.0492  146 GLU   C O   
2176 C CB  . GLU   B 140 ? 0.5721 0.5103 0.5717 0.0569  0.0814  0.0383  146 GLU   C CB  
2177 C CG  . GLU   B 140 ? 0.6328 0.5759 0.6451 0.0528  0.0778  0.0358  146 GLU   C CG  
2178 C CD  . GLU   B 140 ? 0.7258 0.6656 0.7443 0.0555  0.0863  0.0379  146 GLU   C CD  
2179 O OE1 . GLU   B 140 ? 0.7370 0.6760 0.7547 0.0562  0.0847  0.0331  146 GLU   C OE1 
2180 O OE2 . GLU   B 140 ? 0.7605 0.6986 0.7857 0.0570  0.0949  0.0443  146 GLU   C OE2 
2181 N N1  . A1B3N C .   ? 0.8696 0.8408 1.0123 0.0280  0.0787  -0.0064 201 A1B3N A N1  
2182 C C4  . A1B3N C .   ? 0.9145 0.8676 0.9518 -0.0109 0.0791  -0.0489 201 A1B3N A C4  
2183 C C5  . A1B3N C .   ? 0.9140 0.8613 0.9597 -0.0086 0.0825  -0.0491 201 A1B3N A C5  
2184 C C6  . A1B3N C .   ? 0.9109 0.8627 0.9581 -0.0038 0.0718  -0.0415 201 A1B3N A C6  
2185 C C7  . A1B3N C .   ? 0.9090 0.8547 0.9678 -0.0008 0.0762  -0.0409 201 A1B3N A C7  
2186 C C8  . A1B3N C .   ? 0.9073 0.8428 0.9805 -0.0014 0.0932  -0.0475 201 A1B3N A C8  
2187 C C10 . A1B3N C .   ? 0.8900 0.8236 1.0140 0.0078  0.1233  -0.0487 201 A1B3N A C10 
2188 C C13 . A1B3N C .   ? 0.8686 0.8406 1.0166 0.0275  0.0861  -0.0100 201 A1B3N A C13 
2189 C C15 . A1B3N C .   ? 0.8875 0.8402 0.9980 0.0147  0.0894  -0.0291 201 A1B3N A C15 
2190 O O1  . A1B3N C .   ? 0.8598 0.8424 1.0249 0.0320  0.0855  -0.0018 201 A1B3N A O1  
2191 C C14 . A1B3N C .   ? 0.8786 0.8364 1.0056 0.0222  0.0834  -0.0174 201 A1B3N A C14 
2192 C C12 . A1B3N C .   ? 0.8790 0.8382 1.0078 0.0190  0.0950  -0.0253 201 A1B3N A C12 
2193 C C11 . A1B3N C .   ? 0.8781 0.8265 1.0231 0.0185  0.1140  -0.0331 201 A1B3N A C11 
2194 C C9  . A1B3N C .   ? 0.8946 0.8228 1.0079 0.0056  0.1180  -0.0493 201 A1B3N A C9  
2195 N N   . A1B3N C .   ? 0.8970 0.8355 0.9946 0.0063  0.0995  -0.0421 201 A1B3N A N   
2196 O O   . A1B3N C .   ? 0.9154 0.8401 0.9793 -0.0092 0.1017  -0.0574 201 A1B3N A O   
2197 C C1  . A1B3N C .   ? 0.9093 0.8707 0.9487 -0.0019 0.0586  -0.0347 201 A1B3N A C1  
2198 S S   . A1B3N C .   ? 0.9082 0.8746 0.9488 0.0026  0.0470  -0.0267 201 A1B3N A S   
2199 C C   . A1B3N C .   ? 0.9061 0.8797 0.9303 0.0003  0.0347  -0.0238 201 A1B3N A C   
2200 C C3  . A1B3N C .   ? 0.9127 0.8751 0.9432 -0.0084 0.0657  -0.0414 201 A1B3N A C3  
2201 C C2  . A1B3N C .   ? 0.9102 0.8764 0.9416 -0.0041 0.0559  -0.0348 201 A1B3N A C2  
# 
