data_7I67
# 
_entry.id   7I67 
# 
_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   7I67         pdb_00007i67 10.2210/pdb7i67/pdb 
WWPDB D_1001408366 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-02 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.entry_id                        7I67 
_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 '(3S)-1-[(5-fluoro-2-methyl-1H-1,3-benzimidazol-4-yl)methyl]-6-oxopiperidine-3-carboxamide' 304.319   1   ? ? ? 
? 
3 non-polymer syn 'ZINC ION'                                                                                  65.409    2   ? ? ? 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                        78.133    1   ? ? ? 
? 
5 water       nat water                                                                                       18.015    362 ? ? ? 
? 
# 
_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 '(3S)-1-[(5-fluoro-2-methyl-1H-1,3-benzimidazol-4-yl)methyl]-6-oxopiperidine-3-carboxamide' A1B4G 
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 
A1B4G non-polymer         . '(3S)-1-[(5-fluoro-2-methyl-1H-1,3-benzimidazol-4-yl)methyl]-6-oxopiperidine-3-carboxamide' ? 
'C15 H17 F N4 O2' 304.319 
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        A1B4G 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B4G 
_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 A1B4G 1   201 201 A1B4G LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 3 ZN    1   201 1   ZN    ZN  C . 
F 4 DMS   1   202 1   DMS   DMS C . 
G 5 HOH   1   301 351 HOH   HOH A . 
G 5 HOH   2   302 354 HOH   HOH A . 
G 5 HOH   3   303 66  HOH   HOH A . 
G 5 HOH   4   304 118 HOH   HOH A . 
G 5 HOH   5   305 355 HOH   HOH A . 
G 5 HOH   6   306 320 HOH   HOH A . 
G 5 HOH   7   307 359 HOH   HOH A . 
G 5 HOH   8   308 79  HOH   HOH A . 
G 5 HOH   9   309 207 HOH   HOH A . 
G 5 HOH   10  310 293 HOH   HOH A . 
G 5 HOH   11  311 301 HOH   HOH A . 
G 5 HOH   12  312 108 HOH   HOH A . 
G 5 HOH   13  313 342 HOH   HOH A . 
G 5 HOH   14  314 121 HOH   HOH A . 
G 5 HOH   15  315 274 HOH   HOH A . 
G 5 HOH   16  316 303 HOH   HOH A . 
G 5 HOH   17  317 132 HOH   HOH A . 
G 5 HOH   18  318 298 HOH   HOH A . 
G 5 HOH   19  319 179 HOH   HOH A . 
G 5 HOH   20  320 111 HOH   HOH A . 
G 5 HOH   21  321 16  HOH   HOH A . 
G 5 HOH   22  322 360 HOH   HOH A . 
G 5 HOH   23  323 190 HOH   HOH A . 
G 5 HOH   24  324 156 HOH   HOH A . 
G 5 HOH   25  325 197 HOH   HOH A . 
G 5 HOH   26  326 210 HOH   HOH A . 
G 5 HOH   27  327 239 HOH   HOH A . 
G 5 HOH   28  328 95  HOH   HOH A . 
G 5 HOH   29  329 259 HOH   HOH A . 
G 5 HOH   30  330 99  HOH   HOH A . 
G 5 HOH   31  331 310 HOH   HOH A . 
G 5 HOH   32  332 89  HOH   HOH A . 
G 5 HOH   33  333 9   HOH   HOH A . 
G 5 HOH   34  334 232 HOH   HOH A . 
G 5 HOH   35  335 11  HOH   HOH A . 
G 5 HOH   36  336 81  HOH   HOH A . 
G 5 HOH   37  337 115 HOH   HOH A . 
G 5 HOH   38  338 169 HOH   HOH A . 
G 5 HOH   39  339 318 HOH   HOH A . 
G 5 HOH   40  340 33  HOH   HOH A . 
G 5 HOH   41  341 271 HOH   HOH A . 
G 5 HOH   42  342 119 HOH   HOH A . 
G 5 HOH   43  343 266 HOH   HOH A . 
G 5 HOH   44  344 106 HOH   HOH A . 
G 5 HOH   45  345 312 HOH   HOH A . 
G 5 HOH   46  346 204 HOH   HOH A . 
G 5 HOH   47  347 183 HOH   HOH A . 
G 5 HOH   48  348 42  HOH   HOH A . 
G 5 HOH   49  349 211 HOH   HOH A . 
G 5 HOH   50  350 335 HOH   HOH A . 
G 5 HOH   51  351 26  HOH   HOH A . 
G 5 HOH   52  352 164 HOH   HOH A . 
G 5 HOH   53  353 243 HOH   HOH A . 
G 5 HOH   54  354 4   HOH   HOH A . 
G 5 HOH   55  355 47  HOH   HOH A . 
G 5 HOH   56  356 104 HOH   HOH A . 
G 5 HOH   57  357 40  HOH   HOH A . 
G 5 HOH   58  358 238 HOH   HOH A . 
G 5 HOH   59  359 6   HOH   HOH A . 
G 5 HOH   60  360 116 HOH   HOH A . 
G 5 HOH   61  361 291 HOH   HOH A . 
G 5 HOH   62  362 70  HOH   HOH A . 
G 5 HOH   63  363 258 HOH   HOH A . 
G 5 HOH   64  364 325 HOH   HOH A . 
G 5 HOH   65  365 36  HOH   HOH A . 
G 5 HOH   66  366 234 HOH   HOH A . 
G 5 HOH   67  367 307 HOH   HOH A . 
G 5 HOH   68  368 2   HOH   HOH A . 
G 5 HOH   69  369 120 HOH   HOH A . 
G 5 HOH   70  370 346 HOH   HOH A . 
G 5 HOH   71  371 18  HOH   HOH A . 
G 5 HOH   72  372 219 HOH   HOH A . 
G 5 HOH   73  373 194 HOH   HOH A . 
G 5 HOH   74  374 180 HOH   HOH A . 
G 5 HOH   75  375 220 HOH   HOH A . 
G 5 HOH   76  376 345 HOH   HOH A . 
G 5 HOH   77  377 86  HOH   HOH A . 
G 5 HOH   78  378 28  HOH   HOH A . 
G 5 HOH   79  379 64  HOH   HOH A . 
G 5 HOH   80  380 215 HOH   HOH A . 
G 5 HOH   81  381 165 HOH   HOH A . 
G 5 HOH   82  382 23  HOH   HOH A . 
G 5 HOH   83  383 221 HOH   HOH A . 
G 5 HOH   84  384 216 HOH   HOH A . 
G 5 HOH   85  385 112 HOH   HOH A . 
G 5 HOH   86  386 53  HOH   HOH A . 
G 5 HOH   87  387 175 HOH   HOH A . 
G 5 HOH   88  388 228 HOH   HOH A . 
G 5 HOH   89  389 56  HOH   HOH A . 
G 5 HOH   90  390 24  HOH   HOH A . 
G 5 HOH   91  391 37  HOH   HOH A . 
G 5 HOH   92  392 131 HOH   HOH A . 
G 5 HOH   93  393 240 HOH   HOH A . 
G 5 HOH   94  394 110 HOH   HOH A . 
G 5 HOH   95  395 152 HOH   HOH A . 
G 5 HOH   96  396 170 HOH   HOH A . 
G 5 HOH   97  397 159 HOH   HOH A . 
G 5 HOH   98  398 150 HOH   HOH A . 
G 5 HOH   99  399 92  HOH   HOH A . 
G 5 HOH   100 400 226 HOH   HOH A . 
G 5 HOH   101 401 289 HOH   HOH A . 
G 5 HOH   102 402 54  HOH   HOH A . 
G 5 HOH   103 403 45  HOH   HOH A . 
G 5 HOH   104 404 224 HOH   HOH A . 
G 5 HOH   105 405 60  HOH   HOH A . 
G 5 HOH   106 406 290 HOH   HOH A . 
G 5 HOH   107 407 122 HOH   HOH A . 
G 5 HOH   108 408 147 HOH   HOH A . 
G 5 HOH   109 409 280 HOH   HOH A . 
G 5 HOH   110 410 198 HOH   HOH A . 
G 5 HOH   111 411 98  HOH   HOH A . 
G 5 HOH   112 412 362 HOH   HOH A . 
G 5 HOH   113 413 272 HOH   HOH A . 
G 5 HOH   114 414 146 HOH   HOH A . 
G 5 HOH   115 415 209 HOH   HOH A . 
G 5 HOH   116 416 358 HOH   HOH A . 
G 5 HOH   117 417 254 HOH   HOH A . 
G 5 HOH   118 418 255 HOH   HOH A . 
G 5 HOH   119 419 163 HOH   HOH A . 
G 5 HOH   120 420 323 HOH   HOH A . 
G 5 HOH   121 421 244 HOH   HOH A . 
G 5 HOH   122 422 326 HOH   HOH A . 
G 5 HOH   123 423 62  HOH   HOH A . 
G 5 HOH   124 424 168 HOH   HOH A . 
G 5 HOH   125 425 68  HOH   HOH A . 
G 5 HOH   126 426 191 HOH   HOH A . 
G 5 HOH   127 427 299 HOH   HOH A . 
G 5 HOH   128 428 337 HOH   HOH A . 
G 5 HOH   129 429 126 HOH   HOH A . 
G 5 HOH   130 430 15  HOH   HOH A . 
G 5 HOH   131 431 29  HOH   HOH A . 
G 5 HOH   132 432 13  HOH   HOH A . 
G 5 HOH   133 433 80  HOH   HOH A . 
G 5 HOH   134 434 161 HOH   HOH A . 
G 5 HOH   135 435 19  HOH   HOH A . 
G 5 HOH   136 436 134 HOH   HOH A . 
G 5 HOH   137 437 341 HOH   HOH A . 
G 5 HOH   138 438 300 HOH   HOH A . 
G 5 HOH   139 439 20  HOH   HOH A . 
G 5 HOH   140 440 5   HOH   HOH A . 
G 5 HOH   141 441 304 HOH   HOH A . 
G 5 HOH   142 442 166 HOH   HOH A . 
G 5 HOH   143 443 75  HOH   HOH A . 
G 5 HOH   144 444 287 HOH   HOH A . 
G 5 HOH   145 445 185 HOH   HOH A . 
G 5 HOH   146 446 270 HOH   HOH A . 
G 5 HOH   147 447 59  HOH   HOH A . 
G 5 HOH   148 448 296 HOH   HOH A . 
G 5 HOH   149 449 46  HOH   HOH A . 
G 5 HOH   150 450 87  HOH   HOH A . 
G 5 HOH   151 451 344 HOH   HOH A . 
G 5 HOH   152 452 107 HOH   HOH A . 
G 5 HOH   153 453 365 HOH   HOH A . 
G 5 HOH   154 454 138 HOH   HOH A . 
G 5 HOH   155 455 245 HOH   HOH A . 
G 5 HOH   156 456 314 HOH   HOH A . 
G 5 HOH   157 457 313 HOH   HOH A . 
G 5 HOH   158 458 278 HOH   HOH A . 
G 5 HOH   159 459 94  HOH   HOH A . 
G 5 HOH   160 460 218 HOH   HOH A . 
G 5 HOH   161 461 343 HOH   HOH A . 
G 5 HOH   162 462 174 HOH   HOH A . 
G 5 HOH   163 463 277 HOH   HOH A . 
G 5 HOH   164 464 361 HOH   HOH A . 
G 5 HOH   165 465 363 HOH   HOH A . 
G 5 HOH   166 466 279 HOH   HOH A . 
G 5 HOH   167 467 201 HOH   HOH A . 
G 5 HOH   168 468 177 HOH   HOH A . 
G 5 HOH   169 469 248 HOH   HOH A . 
G 5 HOH   170 470 275 HOH   HOH A . 
G 5 HOH   171 471 350 HOH   HOH A . 
G 5 HOH   172 472 212 HOH   HOH A . 
G 5 HOH   173 473 182 HOH   HOH A . 
G 5 HOH   174 474 282 HOH   HOH A . 
G 5 HOH   175 475 109 HOH   HOH A . 
G 5 HOH   176 476 184 HOH   HOH A . 
G 5 HOH   177 477 143 HOH   HOH A . 
G 5 HOH   178 478 366 HOH   HOH A . 
G 5 HOH   179 479 283 HOH   HOH A . 
G 5 HOH   180 480 285 HOH   HOH A . 
G 5 HOH   181 481 334 HOH   HOH A . 
G 5 HOH   182 482 329 HOH   HOH A . 
G 5 HOH   183 483 241 HOH   HOH A . 
G 5 HOH   184 484 247 HOH   HOH A . 
H 5 HOH   1   301 367 HOH   HOH C . 
H 5 HOH   2   302 257 HOH   HOH C . 
H 5 HOH   3   303 223 HOH   HOH C . 
H 5 HOH   4   304 105 HOH   HOH C . 
H 5 HOH   5   305 61  HOH   HOH C . 
H 5 HOH   6   306 288 HOH   HOH C . 
H 5 HOH   7   307 368 HOH   HOH C . 
H 5 HOH   8   308 315 HOH   HOH C . 
H 5 HOH   9   309 196 HOH   HOH C . 
H 5 HOH   10  310 127 HOH   HOH C . 
H 5 HOH   11  311 349 HOH   HOH C . 
H 5 HOH   12  312 63  HOH   HOH C . 
H 5 HOH   13  313 322 HOH   HOH C . 
H 5 HOH   14  314 90  HOH   HOH C . 
H 5 HOH   15  315 205 HOH   HOH C . 
H 5 HOH   16  316 309 HOH   HOH C . 
H 5 HOH   17  317 330 HOH   HOH C . 
H 5 HOH   18  318 102 HOH   HOH C . 
H 5 HOH   19  319 38  HOH   HOH C . 
H 5 HOH   20  320 136 HOH   HOH C . 
H 5 HOH   21  321 130 HOH   HOH C . 
H 5 HOH   22  322 3   HOH   HOH C . 
H 5 HOH   23  323 338 HOH   HOH C . 
H 5 HOH   24  324 88  HOH   HOH C . 
H 5 HOH   25  325 233 HOH   HOH C . 
H 5 HOH   26  326 34  HOH   HOH C . 
H 5 HOH   27  327 142 HOH   HOH C . 
H 5 HOH   28  328 160 HOH   HOH C . 
H 5 HOH   29  329 30  HOH   HOH C . 
H 5 HOH   30  330 246 HOH   HOH C . 
H 5 HOH   31  331 203 HOH   HOH C . 
H 5 HOH   32  332 154 HOH   HOH C . 
H 5 HOH   33  333 137 HOH   HOH C . 
H 5 HOH   34  334 123 HOH   HOH C . 
H 5 HOH   35  335 58  HOH   HOH C . 
H 5 HOH   36  336 200 HOH   HOH C . 
H 5 HOH   37  337 1   HOH   HOH C . 
H 5 HOH   38  338 331 HOH   HOH C . 
H 5 HOH   39  339 176 HOH   HOH C . 
H 5 HOH   40  340 267 HOH   HOH C . 
H 5 HOH   41  341 276 HOH   HOH C . 
H 5 HOH   42  342 21  HOH   HOH C . 
H 5 HOH   43  343 113 HOH   HOH C . 
H 5 HOH   44  344 256 HOH   HOH C . 
H 5 HOH   45  345 12  HOH   HOH C . 
H 5 HOH   46  346 262 HOH   HOH C . 
H 5 HOH   47  347 103 HOH   HOH C . 
H 5 HOH   48  348 336 HOH   HOH C . 
H 5 HOH   49  349 85  HOH   HOH C . 
H 5 HOH   50  350 55  HOH   HOH C . 
H 5 HOH   51  351 51  HOH   HOH C . 
H 5 HOH   52  352 222 HOH   HOH C . 
H 5 HOH   53  353 8   HOH   HOH C . 
H 5 HOH   54  354 97  HOH   HOH C . 
H 5 HOH   55  355 348 HOH   HOH C . 
H 5 HOH   56  356 67  HOH   HOH C . 
H 5 HOH   57  357 52  HOH   HOH C . 
H 5 HOH   58  358 25  HOH   HOH C . 
H 5 HOH   59  359 173 HOH   HOH C . 
H 5 HOH   60  360 114 HOH   HOH C . 
H 5 HOH   61  361 269 HOH   HOH C . 
H 5 HOH   62  362 82  HOH   HOH C . 
H 5 HOH   63  363 100 HOH   HOH C . 
H 5 HOH   64  364 72  HOH   HOH C . 
H 5 HOH   65  365 135 HOH   HOH C . 
H 5 HOH   66  366 206 HOH   HOH C . 
H 5 HOH   67  367 153 HOH   HOH C . 
H 5 HOH   68  368 324 HOH   HOH C . 
H 5 HOH   69  369 141 HOH   HOH C . 
H 5 HOH   70  370 74  HOH   HOH C . 
H 5 HOH   71  371 229 HOH   HOH C . 
H 5 HOH   72  372 292 HOH   HOH C . 
H 5 HOH   73  373 27  HOH   HOH C . 
H 5 HOH   74  374 208 HOH   HOH C . 
H 5 HOH   75  375 193 HOH   HOH C . 
H 5 HOH   76  376 319 HOH   HOH C . 
H 5 HOH   77  377 195 HOH   HOH C . 
H 5 HOH   78  378 128 HOH   HOH C . 
H 5 HOH   79  379 71  HOH   HOH C . 
H 5 HOH   80  380 297 HOH   HOH C . 
H 5 HOH   81  381 327 HOH   HOH C . 
H 5 HOH   82  382 311 HOH   HOH C . 
H 5 HOH   83  383 332 HOH   HOH C . 
H 5 HOH   84  384 84  HOH   HOH C . 
H 5 HOH   85  385 181 HOH   HOH C . 
H 5 HOH   86  386 96  HOH   HOH C . 
H 5 HOH   87  387 22  HOH   HOH C . 
H 5 HOH   88  388 39  HOH   HOH C . 
H 5 HOH   89  389 17  HOH   HOH C . 
H 5 HOH   90  390 7   HOH   HOH C . 
H 5 HOH   91  391 14  HOH   HOH C . 
H 5 HOH   92  392 251 HOH   HOH C . 
H 5 HOH   93  393 140 HOH   HOH C . 
H 5 HOH   94  394 192 HOH   HOH C . 
H 5 HOH   95  395 93  HOH   HOH C . 
H 5 HOH   96  396 73  HOH   HOH C . 
H 5 HOH   97  397 230 HOH   HOH C . 
H 5 HOH   98  398 48  HOH   HOH C . 
H 5 HOH   99  399 91  HOH   HOH C . 
H 5 HOH   100 400 213 HOH   HOH C . 
H 5 HOH   101 401 83  HOH   HOH C . 
H 5 HOH   102 402 117 HOH   HOH C . 
H 5 HOH   103 403 157 HOH   HOH C . 
H 5 HOH   104 404 78  HOH   HOH C . 
H 5 HOH   105 405 167 HOH   HOH C . 
H 5 HOH   106 406 43  HOH   HOH C . 
H 5 HOH   107 407 148 HOH   HOH C . 
H 5 HOH   108 408 50  HOH   HOH C . 
H 5 HOH   109 409 32  HOH   HOH C . 
H 5 HOH   110 410 49  HOH   HOH C . 
H 5 HOH   111 411 250 HOH   HOH C . 
H 5 HOH   112 412 263 HOH   HOH C . 
H 5 HOH   113 413 69  HOH   HOH C . 
H 5 HOH   114 414 265 HOH   HOH C . 
H 5 HOH   115 415 101 HOH   HOH C . 
H 5 HOH   116 416 235 HOH   HOH C . 
H 5 HOH   117 417 77  HOH   HOH C . 
H 5 HOH   118 418 340 HOH   HOH C . 
H 5 HOH   119 419 333 HOH   HOH C . 
H 5 HOH   120 420 186 HOH   HOH C . 
H 5 HOH   121 421 151 HOH   HOH C . 
H 5 HOH   122 422 217 HOH   HOH C . 
H 5 HOH   123 423 162 HOH   HOH C . 
H 5 HOH   124 424 305 HOH   HOH C . 
H 5 HOH   125 425 124 HOH   HOH C . 
H 5 HOH   126 426 172 HOH   HOH C . 
H 5 HOH   127 427 227 HOH   HOH C . 
H 5 HOH   128 428 125 HOH   HOH C . 
H 5 HOH   129 429 41  HOH   HOH C . 
H 5 HOH   130 430 65  HOH   HOH C . 
H 5 HOH   131 431 202 HOH   HOH C . 
H 5 HOH   132 432 35  HOH   HOH C . 
H 5 HOH   133 433 171 HOH   HOH C . 
H 5 HOH   134 434 295 HOH   HOH C . 
H 5 HOH   135 435 302 HOH   HOH C . 
H 5 HOH   136 436 10  HOH   HOH C . 
H 5 HOH   137 437 321 HOH   HOH C . 
H 5 HOH   138 438 44  HOH   HOH C . 
H 5 HOH   139 439 149 HOH   HOH C . 
H 5 HOH   140 440 31  HOH   HOH C . 
H 5 HOH   141 441 145 HOH   HOH C . 
H 5 HOH   142 442 284 HOH   HOH C . 
H 5 HOH   143 443 178 HOH   HOH C . 
H 5 HOH   144 444 155 HOH   HOH C . 
H 5 HOH   145 445 286 HOH   HOH C . 
H 5 HOH   146 446 231 HOH   HOH C . 
H 5 HOH   147 447 144 HOH   HOH C . 
H 5 HOH   148 448 139 HOH   HOH C . 
H 5 HOH   149 449 264 HOH   HOH C . 
H 5 HOH   150 450 364 HOH   HOH C . 
H 5 HOH   151 451 353 HOH   HOH C . 
H 5 HOH   152 452 133 HOH   HOH C . 
H 5 HOH   153 453 294 HOH   HOH C . 
H 5 HOH   154 454 249 HOH   HOH C . 
H 5 HOH   155 455 281 HOH   HOH C . 
H 5 HOH   156 456 76  HOH   HOH C . 
H 5 HOH   157 457 352 HOH   HOH C . 
H 5 HOH   158 458 268 HOH   HOH C . 
H 5 HOH   159 459 189 HOH   HOH C . 
H 5 HOH   160 460 188 HOH   HOH C . 
H 5 HOH   161 461 225 HOH   HOH C . 
H 5 HOH   162 462 273 HOH   HOH C . 
H 5 HOH   163 463 236 HOH   HOH C . 
H 5 HOH   164 464 158 HOH   HOH C . 
H 5 HOH   165 465 339 HOH   HOH C . 
H 5 HOH   166 466 316 HOH   HOH C . 
H 5 HOH   167 467 357 HOH   HOH C . 
H 5 HOH   168 468 214 HOH   HOH C . 
H 5 HOH   169 469 242 HOH   HOH C . 
H 5 HOH   170 470 252 HOH   HOH C . 
H 5 HOH   171 471 356 HOH   HOH C . 
H 5 HOH   172 472 199 HOH   HOH C . 
H 5 HOH   173 473 187 HOH   HOH C . 
H 5 HOH   174 474 261 HOH   HOH C . 
H 5 HOH   175 475 328 HOH   HOH C . 
H 5 HOH   176 476 253 HOH   HOH C . 
H 5 HOH   177 477 347 HOH   HOH C . 
H 5 HOH   178 478 260 HOH   HOH C . 
# 
loop_
_software.classification 
_software.name 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
refinement       BUSTER  '2.10.4 (23-JAN-2024)' ? 1 
'data scaling'   Aimless .                      ? 2 
phasing          PHASER  .                      ? 3 
'data reduction' XDS     .                      ? 4 
# 
_cell.entry_id           7I67 
_cell.length_a           86.389 
_cell.length_b           57.015 
_cell.length_c           64.664 
_cell.angle_alpha        90.00 
_cell.angle_beta         94.84 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I67 
_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          7I67 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.50 
_exptl_crystal.density_percent_sol   50.72 
_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   2025-01-24 
_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   0.92204 
_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        0.92204 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I67 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             64.43 
_reflns.d_resolution_high            1.35 
_reflns.number_obs                   66277 
_reflns.percent_possible_obs         96.4 
_reflns.pdbx_Rmerge_I_obs            0.038 
_reflns.pdbx_netI_over_sigmaI        30.3 
_reflns.pdbx_redundancy              6.2 
_reflns.pdbx_Rrim_I_all              0.041 
_reflns.pdbx_Rpim_I_all              0.016 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     409529 
_reflns.pdbx_chi_squared             0.87 
_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                  1.35 
_reflns_shell.d_res_low                   1.37 
_reflns_shell.number_measured_all         9228 
_reflns_shell.number_unique_obs           2460 
_reflns_shell.Rmerge_I_obs                0.220 
_reflns_shell.pdbx_chi_squared            0.17 
_reflns_shell.pdbx_redundancy             3.8 
_reflns_shell.percent_possible_obs        72.7 
_reflns_shell.pdbx_netI_over_sigmaI_obs   2.5 
_reflns_shell.pdbx_Rrim_I_all             0.257 
_reflns_shell.pdbx_Rpim_I_all             0.128 
_reflns_shell.pdbx_CC_half                0.951 
_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                                 7I67 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     66225 
_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                             19.57 
_refine.ls_d_res_high                            1.349 
_refine.ls_percent_reflns_obs                    96.2 
_refine.ls_R_factor_obs                          0.1755 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1746 
_refine.ls_R_factor_R_free                       0.1925 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.980 
_refine.ls_number_reflns_R_free                  3296 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.962 
_refine.B_iso_mean                               18.54 
_refine.aniso_B[1][1]                            -0.93800 
_refine.aniso_B[2][2]                            -0.25430 
_refine.aniso_B[3][3]                            1.19230 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -1.72160 
_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             0.051 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.052 
_refine.pdbx_overall_SU_R_Blow_DPI               0.054 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.054 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I67 
_refine_analyze.Luzzati_coordinate_error_obs    0.16 
_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         28 
_refine_hist.number_atoms_solvent             362 
_refine_hist.number_atoms_total               2556 
_refine_hist.d_res_high                       1.349 
_refine_hist.d_res_low                        19.57 
# 
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  2264 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.06  ? 2.00  3086 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  757  '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  412  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2264 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.88  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.19 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  279  '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  2125 '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                       1.35 
_refine_ls_shell.d_res_low                        1.36 
_refine_ls_shell.number_reflns_R_work             1246 
_refine_ls_shell.R_factor_R_work                  0.2006 
_refine_ls_shell.percent_reflns_obs               67.70 
_refine_ls_shell.R_factor_R_free                  0.1971 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            5.96 
_refine_ls_shell.number_reflns_R_free             79 
_refine_ls_shell.number_reflns_all                1325 
_refine_ls_shell.R_factor_all                     0.2004 
# 
_struct.entry_id                  7I67 
_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-0037647-001 (A71EV2A-x4926)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I67 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I67 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I67 C 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.397 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.302 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.211 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 56  C ZN 201 1_555 ? ? ? ? ? ? ? 2.330 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 58  C ZN 201 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 E ZN . ZN ? ? C CYS 116 C ZN 201 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 E ZN . ZN ? ? C HIS 118 C ZN 201 1_555 ? ? ? ? ? ? ? 2.092 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 52  ? A CYS 58  ? 1_555 107.8 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 104.7 ? 
3  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 116.9 ? 
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_555 107.8 ? 
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_555 102.8 ? 
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_555 116.4 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.4 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 107.0 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 118.4 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 106.6 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.2 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? E ZN . ? C ZN 201 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.7 ? 
# 
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 VAL A 26  ? N VAL A 32  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O ARG A 87  ? O ARG A 93  N VAL A 78  ? N VAL A 84  
AA3 1 2 N TRP B 27  ? N TRP C 33  O VAL B 36  ? O VAL C 42  
AA3 2 3 N LEU B 35  ? N LEU C 41  O VAL B 12  ? O VAL C 18  
AA4 1 2 O LYS B 64  ? O LYS C 70  N CYS B 59  ? N CYS C 65  
AA4 2 3 N VAL B 56  ? N VAL C 62  O ARG B 109 ? O ARG C 115 
AA4 3 4 N LEU B 108 ? N LEU C 114 O VAL B 115 ? O VAL C 121 
AA4 4 5 N SER B 119 ? N SER C 125 O GLY B 127 ? O GLY C 133 
AA4 5 6 O PHE B 128 ? O PHE C 134 N MET B 93  ? N MET C 99  
AA4 6 7 O ARG B 87  ? O ARG C 93  N VAL B 78  ? N VAL C 84  
# 
_pdbx_entry_details.entry_id                   7I67 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O C HOH 318 ? ? O C HOH 376 ? ? 1.90 
2 1 O A HOH 339 ? ? O C HOH 468 ? ? 1.91 
3 1 O A HOH 473 ? ? O A HOH 483 ? ? 2.01 
4 1 O A HOH 403 ? ? O A HOH 456 ? ? 2.07 
5 1 O C HOH 368 ? ? O C HOH 394 ? ? 2.17 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    O 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    HOH 
_pdbx_validate_symm_contact.auth_seq_id_1     454 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    C 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     313 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_455 
_pdbx_validate_symm_contact.dist              1.97 
# 
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 14.8347 8.1640   14.3861 -0.0175 -0.0197 -0.0027 0.0064 -0.0034 0.0036 1.0536 0.7085 0.6703 0.6476 
-0.4761 -0.2426 -0.0097 0.0403 0.0798 0.0182 0.0413 0.0102 -0.0113 -0.0592 -0.0316 
'X-RAY DIFFRACTION' 2 ? refined 25.6940 -20.1772 17.6870 -0.0209 -0.0216 0.0139  0.0062 0.0002  0.0139 0.6033 0.9037 0.2429 
-0.1724 -0.1598 -0.0625 0.0145  0.0101 0.1110 0.0255 0.0401 0.0308 0.0299  0.0180  -0.0547 
# 
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 
A1B4G N1   N  N N 1   
A1B4G N3   N  Y N 2   
A1B4G C4   C  N N 3   
A1B4G C5   C  N N 4   
A1B4G C6   C  N S 5   
A1B4G C7   C  N N 6   
A1B4G C8   C  N N 7   
A1B4G C10  C  N N 8   
A1B4G C13  C  Y N 9   
A1B4G F    F  N N 10  
A1B4G C11  C  Y N 11  
A1B4G C12  C  Y N 12  
A1B4G C14  C  Y N 13  
A1B4G C2   C  Y N 14  
A1B4G N    N  Y N 15  
A1B4G C1   C  Y N 16  
A1B4G C    C  N N 17  
A1B4G C3   C  Y N 18  
A1B4G O1   O  N N 19  
A1B4G C9   C  N N 20  
A1B4G O    O  N N 21  
A1B4G N2   N  N N 22  
A1B4G H1   H  N N 23  
A1B4G H6   H  N N 24  
A1B4G H5   H  N N 25  
A1B4G H8   H  N N 26  
A1B4G H7   H  N N 27  
A1B4G H    H  N N 28  
A1B4G H12  H  N N 29  
A1B4G H11  H  N N 30  
A1B4G H16  H  N N 31  
A1B4G H15  H  N N 32  
A1B4G H3   H  N N 33  
A1B4G H4   H  N N 34  
A1B4G H2   H  N N 35  
A1B4G H14  H  N N 36  
A1B4G H13  H  N N 37  
A1B4G H10  H  N N 38  
A1B4G H9   H  N N 39  
ALA   N    N  N N 40  
ALA   CA   C  N S 41  
ALA   C    C  N N 42  
ALA   O    O  N N 43  
ALA   CB   C  N N 44  
ALA   OXT  O  N N 45  
ALA   H    H  N N 46  
ALA   H2   H  N N 47  
ALA   HA   H  N N 48  
ALA   HB1  H  N N 49  
ALA   HB2  H  N N 50  
ALA   HB3  H  N N 51  
ALA   HXT  H  N N 52  
ARG   N    N  N N 53  
ARG   CA   C  N S 54  
ARG   C    C  N N 55  
ARG   O    O  N N 56  
ARG   CB   C  N N 57  
ARG   CG   C  N N 58  
ARG   CD   C  N N 59  
ARG   NE   N  N N 60  
ARG   CZ   C  N N 61  
ARG   NH1  N  N N 62  
ARG   NH2  N  N N 63  
ARG   OXT  O  N N 64  
ARG   H    H  N N 65  
ARG   H2   H  N N 66  
ARG   HA   H  N N 67  
ARG   HB2  H  N N 68  
ARG   HB3  H  N N 69  
ARG   HG2  H  N N 70  
ARG   HG3  H  N N 71  
ARG   HD2  H  N N 72  
ARG   HD3  H  N N 73  
ARG   HE   H  N N 74  
ARG   HH11 H  N N 75  
ARG   HH12 H  N N 76  
ARG   HH21 H  N N 77  
ARG   HH22 H  N N 78  
ARG   HXT  H  N N 79  
ASN   N    N  N N 80  
ASN   CA   C  N S 81  
ASN   C    C  N N 82  
ASN   O    O  N N 83  
ASN   CB   C  N N 84  
ASN   CG   C  N N 85  
ASN   OD1  O  N N 86  
ASN   ND2  N  N N 87  
ASN   OXT  O  N N 88  
ASN   H    H  N N 89  
ASN   H2   H  N N 90  
ASN   HA   H  N N 91  
ASN   HB2  H  N N 92  
ASN   HB3  H  N N 93  
ASN   HD21 H  N N 94  
ASN   HD22 H  N N 95  
ASN   HXT  H  N N 96  
ASP   N    N  N N 97  
ASP   CA   C  N S 98  
ASP   C    C  N N 99  
ASP   O    O  N N 100 
ASP   CB   C  N N 101 
ASP   CG   C  N N 102 
ASP   OD1  O  N N 103 
ASP   OD2  O  N N 104 
ASP   OXT  O  N N 105 
ASP   H    H  N N 106 
ASP   H2   H  N N 107 
ASP   HA   H  N N 108 
ASP   HB2  H  N N 109 
ASP   HB3  H  N N 110 
ASP   HD2  H  N N 111 
ASP   HXT  H  N N 112 
CYS   N    N  N N 113 
CYS   CA   C  N R 114 
CYS   C    C  N N 115 
CYS   O    O  N N 116 
CYS   CB   C  N N 117 
CYS   SG   S  N N 118 
CYS   OXT  O  N N 119 
CYS   H    H  N N 120 
CYS   H2   H  N N 121 
CYS   HA   H  N N 122 
CYS   HB2  H  N N 123 
CYS   HB3  H  N N 124 
CYS   HG   H  N N 125 
CYS   HXT  H  N N 126 
DMS   S    S  N N 127 
DMS   O    O  N N 128 
DMS   C1   C  N N 129 
DMS   C2   C  N N 130 
DMS   H11  H  N N 131 
DMS   H12  H  N N 132 
DMS   H13  H  N N 133 
DMS   H21  H  N N 134 
DMS   H22  H  N N 135 
DMS   H23  H  N N 136 
GLN   N    N  N N 137 
GLN   CA   C  N S 138 
GLN   C    C  N N 139 
GLN   O    O  N N 140 
GLN   CB   C  N N 141 
GLN   CG   C  N N 142 
GLN   CD   C  N N 143 
GLN   OE1  O  N N 144 
GLN   NE2  N  N N 145 
GLN   OXT  O  N N 146 
GLN   H    H  N N 147 
GLN   H2   H  N N 148 
GLN   HA   H  N N 149 
GLN   HB2  H  N N 150 
GLN   HB3  H  N N 151 
GLN   HG2  H  N N 152 
GLN   HG3  H  N N 153 
GLN   HE21 H  N N 154 
GLN   HE22 H  N N 155 
GLN   HXT  H  N N 156 
GLU   N    N  N N 157 
GLU   CA   C  N S 158 
GLU   C    C  N N 159 
GLU   O    O  N N 160 
GLU   CB   C  N N 161 
GLU   CG   C  N N 162 
GLU   CD   C  N N 163 
GLU   OE1  O  N N 164 
GLU   OE2  O  N N 165 
GLU   OXT  O  N N 166 
GLU   H    H  N N 167 
GLU   H2   H  N N 168 
GLU   HA   H  N N 169 
GLU   HB2  H  N N 170 
GLU   HB3  H  N N 171 
GLU   HG2  H  N N 172 
GLU   HG3  H  N N 173 
GLU   HE2  H  N N 174 
GLU   HXT  H  N N 175 
GLY   N    N  N N 176 
GLY   CA   C  N N 177 
GLY   C    C  N N 178 
GLY   O    O  N N 179 
GLY   OXT  O  N N 180 
GLY   H    H  N N 181 
GLY   H2   H  N N 182 
GLY   HA2  H  N N 183 
GLY   HA3  H  N N 184 
GLY   HXT  H  N N 185 
HIS   N    N  N N 186 
HIS   CA   C  N S 187 
HIS   C    C  N N 188 
HIS   O    O  N N 189 
HIS   CB   C  N N 190 
HIS   CG   C  Y N 191 
HIS   ND1  N  Y N 192 
HIS   CD2  C  Y N 193 
HIS   CE1  C  Y N 194 
HIS   NE2  N  Y N 195 
HIS   OXT  O  N N 196 
HIS   H    H  N N 197 
HIS   H2   H  N N 198 
HIS   HA   H  N N 199 
HIS   HB2  H  N N 200 
HIS   HB3  H  N N 201 
HIS   HD1  H  N N 202 
HIS   HD2  H  N N 203 
HIS   HE1  H  N N 204 
HIS   HE2  H  N N 205 
HIS   HXT  H  N N 206 
HOH   O    O  N N 207 
HOH   H1   H  N N 208 
HOH   H2   H  N N 209 
ILE   N    N  N N 210 
ILE   CA   C  N S 211 
ILE   C    C  N N 212 
ILE   O    O  N N 213 
ILE   CB   C  N S 214 
ILE   CG1  C  N N 215 
ILE   CG2  C  N N 216 
ILE   CD1  C  N N 217 
ILE   OXT  O  N N 218 
ILE   H    H  N N 219 
ILE   H2   H  N N 220 
ILE   HA   H  N N 221 
ILE   HB   H  N N 222 
ILE   HG12 H  N N 223 
ILE   HG13 H  N N 224 
ILE   HG21 H  N N 225 
ILE   HG22 H  N N 226 
ILE   HG23 H  N N 227 
ILE   HD11 H  N N 228 
ILE   HD12 H  N N 229 
ILE   HD13 H  N N 230 
ILE   HXT  H  N N 231 
LEU   N    N  N N 232 
LEU   CA   C  N S 233 
LEU   C    C  N N 234 
LEU   O    O  N N 235 
LEU   CB   C  N N 236 
LEU   CG   C  N N 237 
LEU   CD1  C  N N 238 
LEU   CD2  C  N N 239 
LEU   OXT  O  N N 240 
LEU   H    H  N N 241 
LEU   H2   H  N N 242 
LEU   HA   H  N N 243 
LEU   HB2  H  N N 244 
LEU   HB3  H  N N 245 
LEU   HG   H  N N 246 
LEU   HD11 H  N N 247 
LEU   HD12 H  N N 248 
LEU   HD13 H  N N 249 
LEU   HD21 H  N N 250 
LEU   HD22 H  N N 251 
LEU   HD23 H  N N 252 
LEU   HXT  H  N N 253 
LYS   N    N  N N 254 
LYS   CA   C  N S 255 
LYS   C    C  N N 256 
LYS   O    O  N N 257 
LYS   CB   C  N N 258 
LYS   CG   C  N N 259 
LYS   CD   C  N N 260 
LYS   CE   C  N N 261 
LYS   NZ   N  N N 262 
LYS   OXT  O  N N 263 
LYS   H    H  N N 264 
LYS   H2   H  N N 265 
LYS   HA   H  N N 266 
LYS   HB2  H  N N 267 
LYS   HB3  H  N N 268 
LYS   HG2  H  N N 269 
LYS   HG3  H  N N 270 
LYS   HD2  H  N N 271 
LYS   HD3  H  N N 272 
LYS   HE2  H  N N 273 
LYS   HE3  H  N N 274 
LYS   HZ1  H  N N 275 
LYS   HZ2  H  N N 276 
LYS   HZ3  H  N N 277 
LYS   HXT  H  N N 278 
MET   N    N  N N 279 
MET   CA   C  N S 280 
MET   C    C  N N 281 
MET   O    O  N N 282 
MET   CB   C  N N 283 
MET   CG   C  N N 284 
MET   SD   S  N N 285 
MET   CE   C  N N 286 
MET   OXT  O  N N 287 
MET   H    H  N N 288 
MET   H2   H  N N 289 
MET   HA   H  N N 290 
MET   HB2  H  N N 291 
MET   HB3  H  N N 292 
MET   HG2  H  N N 293 
MET   HG3  H  N N 294 
MET   HE1  H  N N 295 
MET   HE2  H  N N 296 
MET   HE3  H  N N 297 
MET   HXT  H  N N 298 
PHE   N    N  N N 299 
PHE   CA   C  N S 300 
PHE   C    C  N N 301 
PHE   O    O  N N 302 
PHE   CB   C  N N 303 
PHE   CG   C  Y N 304 
PHE   CD1  C  Y N 305 
PHE   CD2  C  Y N 306 
PHE   CE1  C  Y N 307 
PHE   CE2  C  Y N 308 
PHE   CZ   C  Y N 309 
PHE   OXT  O  N N 310 
PHE   H    H  N N 311 
PHE   H2   H  N N 312 
PHE   HA   H  N N 313 
PHE   HB2  H  N N 314 
PHE   HB3  H  N N 315 
PHE   HD1  H  N N 316 
PHE   HD2  H  N N 317 
PHE   HE1  H  N N 318 
PHE   HE2  H  N N 319 
PHE   HZ   H  N N 320 
PHE   HXT  H  N N 321 
PRO   N    N  N N 322 
PRO   CA   C  N S 323 
PRO   C    C  N N 324 
PRO   O    O  N N 325 
PRO   CB   C  N N 326 
PRO   CG   C  N N 327 
PRO   CD   C  N N 328 
PRO   OXT  O  N N 329 
PRO   H    H  N N 330 
PRO   HA   H  N N 331 
PRO   HB2  H  N N 332 
PRO   HB3  H  N N 333 
PRO   HG2  H  N N 334 
PRO   HG3  H  N N 335 
PRO   HD2  H  N N 336 
PRO   HD3  H  N N 337 
PRO   HXT  H  N N 338 
SER   N    N  N N 339 
SER   CA   C  N S 340 
SER   C    C  N N 341 
SER   O    O  N N 342 
SER   CB   C  N N 343 
SER   OG   O  N N 344 
SER   OXT  O  N N 345 
SER   H    H  N N 346 
SER   H2   H  N N 347 
SER   HA   H  N N 348 
SER   HB2  H  N N 349 
SER   HB3  H  N N 350 
SER   HG   H  N N 351 
SER   HXT  H  N N 352 
THR   N    N  N N 353 
THR   CA   C  N S 354 
THR   C    C  N N 355 
THR   O    O  N N 356 
THR   CB   C  N R 357 
THR   OG1  O  N N 358 
THR   CG2  C  N N 359 
THR   OXT  O  N N 360 
THR   H    H  N N 361 
THR   H2   H  N N 362 
THR   HA   H  N N 363 
THR   HB   H  N N 364 
THR   HG1  H  N N 365 
THR   HG21 H  N N 366 
THR   HG22 H  N N 367 
THR   HG23 H  N N 368 
THR   HXT  H  N N 369 
TRP   N    N  N N 370 
TRP   CA   C  N S 371 
TRP   C    C  N N 372 
TRP   O    O  N N 373 
TRP   CB   C  N N 374 
TRP   CG   C  Y N 375 
TRP   CD1  C  Y N 376 
TRP   CD2  C  Y N 377 
TRP   NE1  N  Y N 378 
TRP   CE2  C  Y N 379 
TRP   CE3  C  Y N 380 
TRP   CZ2  C  Y N 381 
TRP   CZ3  C  Y N 382 
TRP   CH2  C  Y N 383 
TRP   OXT  O  N N 384 
TRP   H    H  N N 385 
TRP   H2   H  N N 386 
TRP   HA   H  N N 387 
TRP   HB2  H  N N 388 
TRP   HB3  H  N N 389 
TRP   HD1  H  N N 390 
TRP   HE1  H  N N 391 
TRP   HE3  H  N N 392 
TRP   HZ2  H  N N 393 
TRP   HZ3  H  N N 394 
TRP   HH2  H  N N 395 
TRP   HXT  H  N N 396 
TYR   N    N  N N 397 
TYR   CA   C  N S 398 
TYR   C    C  N N 399 
TYR   O    O  N N 400 
TYR   CB   C  N N 401 
TYR   CG   C  Y N 402 
TYR   CD1  C  Y N 403 
TYR   CD2  C  Y N 404 
TYR   CE1  C  Y N 405 
TYR   CE2  C  Y N 406 
TYR   CZ   C  Y N 407 
TYR   OH   O  N N 408 
TYR   OXT  O  N N 409 
TYR   H    H  N N 410 
TYR   H2   H  N N 411 
TYR   HA   H  N N 412 
TYR   HB2  H  N N 413 
TYR   HB3  H  N N 414 
TYR   HD1  H  N N 415 
TYR   HD2  H  N N 416 
TYR   HE1  H  N N 417 
TYR   HE2  H  N N 418 
TYR   HH   H  N N 419 
TYR   HXT  H  N N 420 
VAL   N    N  N N 421 
VAL   CA   C  N S 422 
VAL   C    C  N N 423 
VAL   O    O  N N 424 
VAL   CB   C  N N 425 
VAL   CG1  C  N N 426 
VAL   CG2  C  N N 427 
VAL   OXT  O  N N 428 
VAL   H    H  N N 429 
VAL   H2   H  N N 430 
VAL   HA   H  N N 431 
VAL   HB   H  N N 432 
VAL   HG11 H  N N 433 
VAL   HG12 H  N N 434 
VAL   HG13 H  N N 435 
VAL   HG21 H  N N 436 
VAL   HG22 H  N N 437 
VAL   HG23 H  N N 438 
VAL   HXT  H  N N 439 
ZN    ZN   ZN N N 440 
# 
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 
A1B4G C   C1   sing N N 1   
A1B4G C1  N    doub Y N 2   
A1B4G N   C2   sing Y N 3   
A1B4G C2  C3   doub Y N 4   
A1B4G C4  C3   sing N N 5   
A1B4G N1  C4   sing N N 6   
A1B4G N1  C5   sing N N 7   
A1B4G C5  C6   sing N N 8   
A1B4G C7  C6   sing N N 9   
A1B4G N2  C7   sing N N 10  
A1B4G O   C7   doub N N 11  
A1B4G C6  C8   sing N N 12  
A1B4G C8  C9   sing N N 13  
A1B4G C9  C10  sing N N 14  
A1B4G C10 N1   sing N N 15  
A1B4G O1  C10  doub N N 16  
A1B4G C3  C11  sing Y N 17  
A1B4G C11 F    sing N N 18  
A1B4G C12 C11  doub Y N 19  
A1B4G C13 C12  sing Y N 20  
A1B4G C14 C13  doub Y N 21  
A1B4G C2  C14  sing Y N 22  
A1B4G N3  C14  sing Y N 23  
A1B4G C1  N3   sing Y N 24  
A1B4G N3  H1   sing N N 25  
A1B4G C4  H6   sing N N 26  
A1B4G C4  H5   sing N N 27  
A1B4G C5  H8   sing N N 28  
A1B4G C5  H7   sing N N 29  
A1B4G C6  H    sing N N 30  
A1B4G C8  H12  sing N N 31  
A1B4G C8  H11  sing N N 32  
A1B4G C13 H16  sing N N 33  
A1B4G C12 H15  sing N N 34  
A1B4G C   H3   sing N N 35  
A1B4G C   H4   sing N N 36  
A1B4G C   H2   sing N N 37  
A1B4G C9  H14  sing N N 38  
A1B4G C9  H13  sing N N 39  
A1B4G N2  H10  sing N N 40  
A1B4G N2  H9   sing N N 41  
ALA   N   CA   sing N N 42  
ALA   N   H    sing N N 43  
ALA   N   H2   sing N N 44  
ALA   CA  C    sing N N 45  
ALA   CA  CB   sing N N 46  
ALA   CA  HA   sing N N 47  
ALA   C   O    doub N N 48  
ALA   C   OXT  sing N N 49  
ALA   CB  HB1  sing N N 50  
ALA   CB  HB2  sing N N 51  
ALA   CB  HB3  sing N N 52  
ALA   OXT HXT  sing N N 53  
ARG   N   CA   sing N N 54  
ARG   N   H    sing N N 55  
ARG   N   H2   sing N N 56  
ARG   CA  C    sing N N 57  
ARG   CA  CB   sing N N 58  
ARG   CA  HA   sing N N 59  
ARG   C   O    doub N N 60  
ARG   C   OXT  sing N N 61  
ARG   CB  CG   sing N N 62  
ARG   CB  HB2  sing N N 63  
ARG   CB  HB3  sing N N 64  
ARG   CG  CD   sing N N 65  
ARG   CG  HG2  sing N N 66  
ARG   CG  HG3  sing N N 67  
ARG   CD  NE   sing N N 68  
ARG   CD  HD2  sing N N 69  
ARG   CD  HD3  sing N N 70  
ARG   NE  CZ   sing N N 71  
ARG   NE  HE   sing N N 72  
ARG   CZ  NH1  sing N N 73  
ARG   CZ  NH2  doub N N 74  
ARG   NH1 HH11 sing N N 75  
ARG   NH1 HH12 sing N N 76  
ARG   NH2 HH21 sing N N 77  
ARG   NH2 HH22 sing N N 78  
ARG   OXT HXT  sing N N 79  
ASN   N   CA   sing N N 80  
ASN   N   H    sing N N 81  
ASN   N   H2   sing N N 82  
ASN   CA  C    sing N N 83  
ASN   CA  CB   sing N N 84  
ASN   CA  HA   sing N N 85  
ASN   C   O    doub N N 86  
ASN   C   OXT  sing N N 87  
ASN   CB  CG   sing N N 88  
ASN   CB  HB2  sing N N 89  
ASN   CB  HB3  sing N N 90  
ASN   CG  OD1  doub N N 91  
ASN   CG  ND2  sing N N 92  
ASN   ND2 HD21 sing N N 93  
ASN   ND2 HD22 sing N N 94  
ASN   OXT HXT  sing N N 95  
ASP   N   CA   sing N N 96  
ASP   N   H    sing N N 97  
ASP   N   H2   sing N N 98  
ASP   CA  C    sing N N 99  
ASP   CA  CB   sing N N 100 
ASP   CA  HA   sing N N 101 
ASP   C   O    doub N N 102 
ASP   C   OXT  sing N N 103 
ASP   CB  CG   sing N N 104 
ASP   CB  HB2  sing N N 105 
ASP   CB  HB3  sing N N 106 
ASP   CG  OD1  doub N N 107 
ASP   CG  OD2  sing N N 108 
ASP   OD2 HD2  sing N N 109 
ASP   OXT HXT  sing N N 110 
CYS   N   CA   sing N N 111 
CYS   N   H    sing N N 112 
CYS   N   H2   sing N N 113 
CYS   CA  C    sing N N 114 
CYS   CA  CB   sing N N 115 
CYS   CA  HA   sing N N 116 
CYS   C   O    doub N N 117 
CYS   C   OXT  sing N N 118 
CYS   CB  SG   sing N N 119 
CYS   CB  HB2  sing N N 120 
CYS   CB  HB3  sing N N 121 
CYS   SG  HG   sing N N 122 
CYS   OXT HXT  sing N N 123 
DMS   S   O    doub N N 124 
DMS   S   C1   sing N N 125 
DMS   S   C2   sing N N 126 
DMS   C1  H11  sing N N 127 
DMS   C1  H12  sing N N 128 
DMS   C1  H13  sing N N 129 
DMS   C2  H21  sing N N 130 
DMS   C2  H22  sing N N 131 
DMS   C2  H23  sing N N 132 
GLN   N   CA   sing N N 133 
GLN   N   H    sing N N 134 
GLN   N   H2   sing N N 135 
GLN   CA  C    sing N N 136 
GLN   CA  CB   sing N N 137 
GLN   CA  HA   sing N N 138 
GLN   C   O    doub N N 139 
GLN   C   OXT  sing N N 140 
GLN   CB  CG   sing N N 141 
GLN   CB  HB2  sing N N 142 
GLN   CB  HB3  sing N N 143 
GLN   CG  CD   sing N N 144 
GLN   CG  HG2  sing N N 145 
GLN   CG  HG3  sing N N 146 
GLN   CD  OE1  doub N N 147 
GLN   CD  NE2  sing N N 148 
GLN   NE2 HE21 sing N N 149 
GLN   NE2 HE22 sing N N 150 
GLN   OXT HXT  sing N N 151 
GLU   N   CA   sing N N 152 
GLU   N   H    sing N N 153 
GLU   N   H2   sing N N 154 
GLU   CA  C    sing N N 155 
GLU   CA  CB   sing N N 156 
GLU   CA  HA   sing N N 157 
GLU   C   O    doub N N 158 
GLU   C   OXT  sing N N 159 
GLU   CB  CG   sing N N 160 
GLU   CB  HB2  sing N N 161 
GLU   CB  HB3  sing N N 162 
GLU   CG  CD   sing N N 163 
GLU   CG  HG2  sing N N 164 
GLU   CG  HG3  sing N N 165 
GLU   CD  OE1  doub N N 166 
GLU   CD  OE2  sing N N 167 
GLU   OE2 HE2  sing N N 168 
GLU   OXT HXT  sing N N 169 
GLY   N   CA   sing N N 170 
GLY   N   H    sing N N 171 
GLY   N   H2   sing N N 172 
GLY   CA  C    sing N N 173 
GLY   CA  HA2  sing N N 174 
GLY   CA  HA3  sing N N 175 
GLY   C   O    doub N N 176 
GLY   C   OXT  sing N N 177 
GLY   OXT HXT  sing N N 178 
HIS   N   CA   sing N N 179 
HIS   N   H    sing N N 180 
HIS   N   H2   sing N N 181 
HIS   CA  C    sing N N 182 
HIS   CA  CB   sing N N 183 
HIS   CA  HA   sing N N 184 
HIS   C   O    doub N N 185 
HIS   C   OXT  sing N N 186 
HIS   CB  CG   sing N N 187 
HIS   CB  HB2  sing N N 188 
HIS   CB  HB3  sing N N 189 
HIS   CG  ND1  sing Y N 190 
HIS   CG  CD2  doub Y N 191 
HIS   ND1 CE1  doub Y N 192 
HIS   ND1 HD1  sing N N 193 
HIS   CD2 NE2  sing Y N 194 
HIS   CD2 HD2  sing N N 195 
HIS   CE1 NE2  sing Y N 196 
HIS   CE1 HE1  sing N N 197 
HIS   NE2 HE2  sing N N 198 
HIS   OXT HXT  sing N N 199 
HOH   O   H1   sing N N 200 
HOH   O   H2   sing N N 201 
ILE   N   CA   sing N N 202 
ILE   N   H    sing N N 203 
ILE   N   H2   sing N N 204 
ILE   CA  C    sing N N 205 
ILE   CA  CB   sing N N 206 
ILE   CA  HA   sing N N 207 
ILE   C   O    doub N N 208 
ILE   C   OXT  sing N N 209 
ILE   CB  CG1  sing N N 210 
ILE   CB  CG2  sing N N 211 
ILE   CB  HB   sing N N 212 
ILE   CG1 CD1  sing N N 213 
ILE   CG1 HG12 sing N N 214 
ILE   CG1 HG13 sing N N 215 
ILE   CG2 HG21 sing N N 216 
ILE   CG2 HG22 sing N N 217 
ILE   CG2 HG23 sing N N 218 
ILE   CD1 HD11 sing N N 219 
ILE   CD1 HD12 sing N N 220 
ILE   CD1 HD13 sing N N 221 
ILE   OXT HXT  sing N N 222 
LEU   N   CA   sing N N 223 
LEU   N   H    sing N N 224 
LEU   N   H2   sing N N 225 
LEU   CA  C    sing N N 226 
LEU   CA  CB   sing N N 227 
LEU   CA  HA   sing N N 228 
LEU   C   O    doub N N 229 
LEU   C   OXT  sing N N 230 
LEU   CB  CG   sing N N 231 
LEU   CB  HB2  sing N N 232 
LEU   CB  HB3  sing N N 233 
LEU   CG  CD1  sing N N 234 
LEU   CG  CD2  sing N N 235 
LEU   CG  HG   sing N N 236 
LEU   CD1 HD11 sing N N 237 
LEU   CD1 HD12 sing N N 238 
LEU   CD1 HD13 sing N N 239 
LEU   CD2 HD21 sing N N 240 
LEU   CD2 HD22 sing N N 241 
LEU   CD2 HD23 sing N N 242 
LEU   OXT HXT  sing N N 243 
LYS   N   CA   sing N N 244 
LYS   N   H    sing N N 245 
LYS   N   H2   sing N N 246 
LYS   CA  C    sing N N 247 
LYS   CA  CB   sing N N 248 
LYS   CA  HA   sing N N 249 
LYS   C   O    doub N N 250 
LYS   C   OXT  sing N N 251 
LYS   CB  CG   sing N N 252 
LYS   CB  HB2  sing N N 253 
LYS   CB  HB3  sing N N 254 
LYS   CG  CD   sing N N 255 
LYS   CG  HG2  sing N N 256 
LYS   CG  HG3  sing N N 257 
LYS   CD  CE   sing N N 258 
LYS   CD  HD2  sing N N 259 
LYS   CD  HD3  sing N N 260 
LYS   CE  NZ   sing N N 261 
LYS   CE  HE2  sing N N 262 
LYS   CE  HE3  sing N N 263 
LYS   NZ  HZ1  sing N N 264 
LYS   NZ  HZ2  sing N N 265 
LYS   NZ  HZ3  sing N N 266 
LYS   OXT HXT  sing N N 267 
MET   N   CA   sing N N 268 
MET   N   H    sing N N 269 
MET   N   H2   sing N N 270 
MET   CA  C    sing N N 271 
MET   CA  CB   sing N N 272 
MET   CA  HA   sing N N 273 
MET   C   O    doub N N 274 
MET   C   OXT  sing N N 275 
MET   CB  CG   sing N N 276 
MET   CB  HB2  sing N N 277 
MET   CB  HB3  sing N N 278 
MET   CG  SD   sing N N 279 
MET   CG  HG2  sing N N 280 
MET   CG  HG3  sing N N 281 
MET   SD  CE   sing N N 282 
MET   CE  HE1  sing N N 283 
MET   CE  HE2  sing N N 284 
MET   CE  HE3  sing N N 285 
MET   OXT HXT  sing N N 286 
PHE   N   CA   sing N N 287 
PHE   N   H    sing N N 288 
PHE   N   H2   sing N N 289 
PHE   CA  C    sing N N 290 
PHE   CA  CB   sing N N 291 
PHE   CA  HA   sing N N 292 
PHE   C   O    doub N N 293 
PHE   C   OXT  sing N N 294 
PHE   CB  CG   sing N N 295 
PHE   CB  HB2  sing N N 296 
PHE   CB  HB3  sing N N 297 
PHE   CG  CD1  doub Y N 298 
PHE   CG  CD2  sing Y N 299 
PHE   CD1 CE1  sing Y N 300 
PHE   CD1 HD1  sing N N 301 
PHE   CD2 CE2  doub Y N 302 
PHE   CD2 HD2  sing N N 303 
PHE   CE1 CZ   doub Y N 304 
PHE   CE1 HE1  sing N N 305 
PHE   CE2 CZ   sing Y N 306 
PHE   CE2 HE2  sing N N 307 
PHE   CZ  HZ   sing N N 308 
PHE   OXT HXT  sing N N 309 
PRO   N   CA   sing N N 310 
PRO   N   CD   sing N N 311 
PRO   N   H    sing N N 312 
PRO   CA  C    sing N N 313 
PRO   CA  CB   sing N N 314 
PRO   CA  HA   sing N N 315 
PRO   C   O    doub N N 316 
PRO   C   OXT  sing N N 317 
PRO   CB  CG   sing N N 318 
PRO   CB  HB2  sing N N 319 
PRO   CB  HB3  sing N N 320 
PRO   CG  CD   sing N N 321 
PRO   CG  HG2  sing N N 322 
PRO   CG  HG3  sing N N 323 
PRO   CD  HD2  sing N N 324 
PRO   CD  HD3  sing N N 325 
PRO   OXT HXT  sing N N 326 
SER   N   CA   sing N N 327 
SER   N   H    sing N N 328 
SER   N   H2   sing N N 329 
SER   CA  C    sing N N 330 
SER   CA  CB   sing N N 331 
SER   CA  HA   sing N N 332 
SER   C   O    doub N N 333 
SER   C   OXT  sing N N 334 
SER   CB  OG   sing N N 335 
SER   CB  HB2  sing N N 336 
SER   CB  HB3  sing N N 337 
SER   OG  HG   sing N N 338 
SER   OXT HXT  sing N N 339 
THR   N   CA   sing N N 340 
THR   N   H    sing N N 341 
THR   N   H2   sing N N 342 
THR   CA  C    sing N N 343 
THR   CA  CB   sing N N 344 
THR   CA  HA   sing N N 345 
THR   C   O    doub N N 346 
THR   C   OXT  sing N N 347 
THR   CB  OG1  sing N N 348 
THR   CB  CG2  sing N N 349 
THR   CB  HB   sing N N 350 
THR   OG1 HG1  sing N N 351 
THR   CG2 HG21 sing N N 352 
THR   CG2 HG22 sing N N 353 
THR   CG2 HG23 sing N N 354 
THR   OXT HXT  sing N N 355 
TRP   N   CA   sing N N 356 
TRP   N   H    sing N N 357 
TRP   N   H2   sing N N 358 
TRP   CA  C    sing N N 359 
TRP   CA  CB   sing N N 360 
TRP   CA  HA   sing N N 361 
TRP   C   O    doub N N 362 
TRP   C   OXT  sing N N 363 
TRP   CB  CG   sing N N 364 
TRP   CB  HB2  sing N N 365 
TRP   CB  HB3  sing N N 366 
TRP   CG  CD1  doub Y N 367 
TRP   CG  CD2  sing Y N 368 
TRP   CD1 NE1  sing Y N 369 
TRP   CD1 HD1  sing N N 370 
TRP   CD2 CE2  doub Y N 371 
TRP   CD2 CE3  sing Y N 372 
TRP   NE1 CE2  sing Y N 373 
TRP   NE1 HE1  sing N N 374 
TRP   CE2 CZ2  sing Y N 375 
TRP   CE3 CZ3  doub Y N 376 
TRP   CE3 HE3  sing N N 377 
TRP   CZ2 CH2  doub Y N 378 
TRP   CZ2 HZ2  sing N N 379 
TRP   CZ3 CH2  sing Y N 380 
TRP   CZ3 HZ3  sing N N 381 
TRP   CH2 HH2  sing N N 382 
TRP   OXT HXT  sing N N 383 
TYR   N   CA   sing N N 384 
TYR   N   H    sing N N 385 
TYR   N   H2   sing N N 386 
TYR   CA  C    sing N N 387 
TYR   CA  CB   sing N N 388 
TYR   CA  HA   sing N N 389 
TYR   C   O    doub N N 390 
TYR   C   OXT  sing N N 391 
TYR   CB  CG   sing N N 392 
TYR   CB  HB2  sing N N 393 
TYR   CB  HB3  sing N N 394 
TYR   CG  CD1  doub Y N 395 
TYR   CG  CD2  sing Y N 396 
TYR   CD1 CE1  sing Y N 397 
TYR   CD1 HD1  sing N N 398 
TYR   CD2 CE2  doub Y N 399 
TYR   CD2 HD2  sing N N 400 
TYR   CE1 CZ   doub Y N 401 
TYR   CE1 HE1  sing N N 402 
TYR   CE2 CZ   sing Y N 403 
TYR   CE2 HE2  sing N N 404 
TYR   CZ  OH   sing N N 405 
TYR   OH  HH   sing N N 406 
TYR   OXT HXT  sing N N 407 
VAL   N   CA   sing N N 408 
VAL   N   H    sing N N 409 
VAL   N   H2   sing N N 410 
VAL   CA  C    sing N N 411 
VAL   CA  CB   sing N N 412 
VAL   CA  HA   sing N N 413 
VAL   C   O    doub N N 414 
VAL   C   OXT  sing N N 415 
VAL   CB  CG1  sing N N 416 
VAL   CB  CG2  sing N N 417 
VAL   CB  HB   sing N N 418 
VAL   CG1 HG11 sing N N 419 
VAL   CG1 HG12 sing N N 420 
VAL   CG1 HG13 sing N N 421 
VAL   CG2 HG21 sing N N 422 
VAL   CG2 HG22 sing N N 423 
VAL   CG2 HG23 sing N N 424 
VAL   OXT HXT  sing N N 425 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_atom_sites.entry_id                    7I67 
_atom_sites.fract_transf_matrix[1][1]   0.011576 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000980 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.017539 
_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]   0.015520 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 1   ? 17.603 8.183   24.746 1.00 15.41 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 18.852 8.260   23.984 1.00 15.57 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 18.989 7.048   23.066 1.00 14.94 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 18.247 6.067   23.230 1.00 15.67 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 20.047 8.307   24.939 1.00 18.41 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 20.131 7.095   25.666 1.00 21.75 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 19.930 7.098   22.124 1.00 13.59 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 20.187 5.973   21.230 1.00 12.94 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 20.610 6.436   19.852 1.00 11.90 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 20.306 7.561   19.451 1.00 13.09 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 21.295 5.559   19.144 1.00 10.77 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 21.778 5.909   17.811 1.00 11.38 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 21.765 4.692   16.907 1.00 11.19 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 21.650 3.557   17.383 1.00 11.81 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 23.223 6.441   17.935 1.00 12.61 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 21.846 4.937   15.593 1.00 10.54 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 22.074 3.880   14.590 1.00 9.72  ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 23.536 3.970   14.206 1.00 10.81 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 24.031 5.078   13.909 1.00 11.38 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 21.205 4.077   13.330 1.00 10.36 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 19.719 4.237   13.677 1.00 11.69 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 21.427 2.907   12.349 1.00 12.02 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 18.932 4.779   12.451 1.00 12.84 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 24.257 2.827   14.174 1.00 10.74 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 25.671 2.807   13.785 1.00 11.81 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 25.760 1.965   12.505 1.00 12.65 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 25.736 0.728   12.565 1.00 12.62 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 26.523 2.194   14.917 1.00 12.94 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 26.568 3.098   16.126 1.00 12.62 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 27.437 4.193   16.177 1.00 13.53 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 25.724 2.890   17.212 1.00 14.07 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 27.435 5.072   17.261 1.00 14.50 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 25.750 3.745   18.323 1.00 14.62 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 26.595 4.843   18.327 1.00 15.36 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 26.613 5.719   19.403 1.00 17.55 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 25.833 2.631   11.351 1.00 13.45 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 25.917 1.966   10.053 1.00 13.52 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 27.161 2.462   9.337  1.00 14.26 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 27.386 3.683   9.244  1.00 13.80 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 24.632 2.233   9.208  1.00 14.85 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 24.284 3.725   9.107  1.00 14.87 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 24.764 1.604   7.825  1.00 16.38 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 28.030 1.553   8.881  1.00 15.15 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 29.267 1.971   8.215  1.00 15.56 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 30.084 2.871   9.127  1.00 14.52 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 30.185 2.575   10.317 1.00 14.68 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 30.548 4.020   8.605  1.00 13.79 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 31.239 5.007   9.442  1.00 13.63 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 30.339 6.201   9.766  1.00 12.66 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 30.822 7.335   9.896  1.00 13.46 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 32.566 5.445   8.844  1.00 14.32 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 33.647 4.398   8.976  1.00 18.17 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 34.379 4.330   9.973  1.00 21.22 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 33.710 3.517   8.010  1.00 17.41 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 29.056 5.916   9.989  1.00 11.90 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 28.092 6.937   10.355 1.00 11.78 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 27.414 6.613   11.677 1.00 11.53 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 27.138 5.431   12.000 1.00 12.31 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 26.987 7.012   9.263  1.00 13.07 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 27.477 7.409   7.892  1.00 13.96 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 28.120 8.625   7.681  1.00 14.91 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 27.317 6.559   6.806  1.00 15.40 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 28.590 8.986   6.421  1.00 15.38 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 27.727 6.939   5.533  1.00 16.73 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 28.350 8.155   5.345  1.00 16.91 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 28.795 8.546   4.091  1.00 21.65 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 27.062 7.671   12.418 1.00 11.03 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 26.265 7.612   13.646 1.00 10.96 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 25.036 8.486   13.402 1.00 10.50 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 25.196 9.689   13.113 1.00 11.26 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 27.083 8.170   14.853 1.00 11.69 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 26.287 8.501   16.103 1.00 13.56 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 27.226 8.868   17.276 1.00 13.86 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 26.680 9.942   18.122 1.00 14.55 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 25.986 9.750   19.246 1.00 16.35 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 25.725 8.514   19.674 1.00 16.44 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 25.539 10.793  19.946 1.00 15.66 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 23.831 7.885   13.447 1.00 9.95  ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 22.576 8.627   13.212 1.00 10.17 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 21.887 8.827   14.543 1.00 11.24 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 21.594 7.834   15.252 1.00 10.90 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 21.632 7.815   12.286 1.00 10.44 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 20.401 8.662   11.933 1.00 11.15 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 22.343 7.305   11.029 1.00 11.92 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 21.640 10.096  14.905 1.00 9.89  ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 21.018 10.425  16.188 1.00 10.89 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 19.900 11.420  15.988 1.00 10.20 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 19.765 12.057  14.900 1.00 11.64 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 22.051 11.045  17.195 1.00 12.60 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 23.036 9.991   17.663 1.00 15.55 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 22.743 12.303  16.625 1.00 12.86 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 19.060 11.588  17.020 1.00 9.94  ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 18.080 12.688  16.992 1.00 10.37 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 18.882 14.008  16.995 1.00 11.04 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 19.811 14.177  17.804 1.00 11.37 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.217 12.671  18.254 1.00 10.60 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 16.356 11.435  18.354 1.00 11.32 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 16.771 10.423  18.966 1.00 12.00 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 15.183 11.473  17.703 1.00 12.49 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 18.502 14.952  16.113 1.00 10.59 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 19.239 16.228  16.069 1.00 10.88 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 19.212 16.904  17.427 1.00 12.08 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 20.229 17.463  17.855 1.00 13.15 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 18.637 17.121  14.993 1.00 11.50 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 19.434 18.424  14.734 1.00 12.25 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 18.679 19.294  13.741 1.00 13.38 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 19.430 20.499  13.300 1.00 13.82 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 19.386 21.662  13.932 1.00 16.39 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 18.800 21.760  15.121 1.00 16.63 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 19.986 22.733  13.410 1.00 17.53 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 18.053 16.805  18.139 1.00 11.10 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 17.950 17.518  19.418 1.00 12.50 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 18.794 16.907  20.539 1.00 13.27 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 18.949 17.542  21.591 1.00 14.74 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 16.471 17.688  19.855 1.00 14.00 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 15.784 16.436  20.344 1.00 13.55 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 15.166 15.549  19.464 1.00 13.58 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 15.609 15.975  21.605 1.00 14.49 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 14.643 14.574  20.219 1.00 13.69 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 14.896 14.785  21.513 1.00 14.20 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 19.347 15.697  20.331 1.00 13.17 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 20.215 15.006  21.310 1.00 12.70 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 21.681 14.964  20.866 1.00 14.33 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 22.490 14.340  21.526 1.00 15.29 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 19.699 13.597  21.628 1.00 12.84 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 18.296 13.593  22.210 1.00 13.22 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 17.818 12.160  22.433 1.00 13.71 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 18.241 14.362  23.559 1.00 15.52 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 22.016 15.577  19.705 1.00 13.42 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 23.391 15.534  19.211 1.00 13.41 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 24.369 16.180  20.202 1.00 14.43 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 24.053 17.216  20.819 1.00 14.87 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 23.455 16.253  17.872 1.00 13.27 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 25.550 15.565  20.329 1.00 13.94 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 26.605 16.081  21.250 1.00 13.87 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 27.535 17.068  20.529 1.00 14.47 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 27.463 17.227  19.280 1.00 13.91 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 27.455 14.906  21.768 1.00 16.25 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 28.178 14.364  20.642 1.00 16.57 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 26.597 13.799  22.413 1.00 16.25 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 28.455 17.737  21.266 1.00 14.40 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 29.450 18.574  20.636 1.00 14.68 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 30.304 17.757  19.671 1.00 13.92 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 30.577 18.230  18.573 1.00 14.70 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 30.371 19.253  21.697 1.00 16.86 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 31.613 19.875  21.076 1.00 23.50 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 31.543 21.034  20.317 1.00 26.81 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 32.884 19.392  21.003 1.00 27.11 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 32.781 21.305  19.931 1.00 27.91 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 33.629 20.326  20.282 1.00 29.26 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 30.666 16.511  20.044 1.00 14.05 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 31.472 15.700  19.132 1.00 14.50 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 30.703 15.422  17.835 1.00 13.04 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 31.285 15.457  16.748 1.00 14.01 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 31.907 14.376  19.761 1.00 16.89 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 32.881 13.642  18.862 1.00 24.59 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 34.034 14.078  18.675 1.00 28.10 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 32.428 12.564  18.221 1.00 26.28 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 29.357 15.201  17.948 1.00 12.30 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 28.577 15.014  16.710 1.00 12.25 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 28.644 16.262  15.810 1.00 11.54 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 28.849 16.156  14.598 1.00 12.13 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 27.121 14.753  17.048 1.00 12.27 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 26.846 13.388  17.639 1.00 13.53 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 27.488 12.402  17.188 1.00 13.71 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 26.017 13.308  18.566 1.00 13.40 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 28.435 17.446  16.392 1.00 11.50 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 28.478 18.696  15.603 1.00 11.68 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 29.883 18.968  15.023 1.00 12.69 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 29.972 19.531  13.929 1.00 13.41 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 28.013 19.888  16.479 1.00 12.39 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 26.511 19.964  16.600 1.00 12.82 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 25.754 19.636  17.688 1.00 14.42 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 25.595 20.422  15.595 1.00 12.88 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 24.416 19.925  17.450 1.00 13.48 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 24.287 20.337  16.136 1.00 12.88 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 25.753 20.869  14.272 1.00 14.46 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 23.153 20.733  15.398 1.00 14.12 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 24.632 21.189  13.533 1.00 14.84 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 23.368 21.186  14.106 1.00 14.73 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 30.944 18.567  15.737 1.00 12.57 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 32.311 18.783  15.274 1.00 13.32 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 32.735 17.776  14.205 1.00 14.42 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 33.783 17.945  13.585 1.00 15.17 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 33.261 18.728  16.474 1.00 14.63 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 31.942 16.701  14.009 1.00 13.81 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 32.223 15.656  12.998 1.00 13.72 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 30.960 15.463  12.150 1.00 14.29 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 30.590 14.342  11.802 1.00 13.91 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 32.621 14.326  13.694 1.00 14.54 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 33.966 14.505  14.362 1.00 16.52 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 35.016 14.428  13.700 1.00 19.57 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 33.973 14.821  15.668 1.00 16.95 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 30.316 16.552  11.786 1.00 13.76 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 29.020 16.531  11.117 1.00 13.10 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 29.075 16.087  9.664  1.00 13.48 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 29.922 16.559  8.893  1.00 15.01 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 28.425 17.954  11.199 1.00 13.21 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 27.019 18.106  10.603 1.00 13.77 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 25.976 17.323  11.411 1.00 13.81 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 26.608 19.568  10.563 1.00 16.04 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 28.161 15.212  9.266  1.00 12.42 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 27.989 14.805  7.870  1.00 12.61 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 26.736 15.506  7.298  1.00 13.46 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 26.785 16.055  6.192  1.00 15.12 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 27.859 13.267  7.774  1.00 12.79 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 27.500 12.842  6.333  1.00 14.82 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 29.166 12.600  8.256  1.00 13.89 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 25.602 15.447  8.022  1.00 12.60 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 24.341 15.995  7.526  1.00 13.09 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 23.381 16.220  8.666  1.00 13.36 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 23.405 15.453  9.642  1.00 12.67 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 23.733 15.012  6.484  1.00 14.03 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 22.318 15.275  6.040  1.00 14.91 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 21.908 16.120  5.038  1.00 16.97 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 21.131 14.657  6.549  1.00 14.02 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 20.535 16.070  4.912  1.00 18.28 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 20.038 15.136  5.791  1.00 15.68 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 20.884 13.741  7.567  1.00 14.02 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 18.717 14.701  6.024  1.00 16.76 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 19.597 13.260  7.742  1.00 15.39 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 18.522 13.788  7.027  1.00 16.41 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 22.560 17.273  8.596  1.00 13.43 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 21.538 17.478  9.611  1.00 13.52 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 20.314 18.098  8.994  1.00 14.69 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 20.423 18.903  8.051  1.00 15.00 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 22.036 18.332  10.787 1.00 14.67 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 22.653 19.675  10.380 1.00 15.43 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 21.695 20.846  10.199 1.00 16.80 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 22.028 21.804  9.449  1.00 17.70 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 20.596 20.825  10.802 1.00 15.48 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 19.145 17.813  9.562  1.00 13.83 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.891 18.379  9.059  1.00 13.43 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 16.914 18.544  10.218 1.00 13.27 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 16.386 17.554  10.755 1.00 13.31 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 17.314 17.457  7.965  1.00 15.37 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 16.047 17.942  7.302  1.00 18.97 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 15.214 18.526  7.991  1.00 21.32 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 15.869 17.676  6.096  1.00 21.36 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 16.700 19.799  10.635 1.00 13.26 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 15.823 20.111  11.751 0.50 14.06 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 15.829 20.067  11.769 0.50 14.97 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 14.383 19.666  11.481 1.00 15.07 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 13.704 19.178  12.398 1.00 15.33 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 15.881 21.608  12.034 0.50 15.19 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 15.930 21.531  12.180 0.50 18.74 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 14.900 21.985  12.979 0.50 15.01 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 15.661 22.358  11.062 0.50 23.76 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 13.913 19.818  10.216 1.00 14.95 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 12.526 19.409  9.915  1.00 15.21 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 12.275 17.919  10.106 1.00 14.36 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 11.132 17.522  10.306 1.00 15.54 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 12.117 19.825  8.506  1.00 17.76 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 12.689 19.003  7.509  1.00 23.41 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 13.335 17.093  10.078 1.00 12.72 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 13.235 15.637  10.277 1.00 12.52 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 13.696 15.187  11.687 1.00 12.53 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 13.603 13.997  12.002 1.00 12.36 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 14.110 14.910  9.226  1.00 12.67 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 13.606 15.112  7.803  1.00 14.49 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 14.466 14.414  6.766  1.00 14.41 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 14.375 12.952  6.914  1.00 12.74 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 14.540 12.092  5.911  1.00 14.85 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 14.802 12.534  4.680  1.00 15.98 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 14.389 10.781  6.114  1.00 14.41 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 14.270 16.111  12.494 1.00 11.82 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 14.896 15.771  13.763 1.00 10.93 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 16.034 14.756  13.605 1.00 10.18 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 16.257 13.929  14.492 1.00 11.09 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 13.880 15.292  14.823 1.00 11.89 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 14.504 15.057  16.193 1.00 11.88 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 15.339 15.899  16.643 1.00 13.44 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 14.107 14.078  16.877 1.00 13.27 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 16.837 14.881  12.522 1.00 10.85 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.935 13.932  12.327 1.00 10.23 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 19.288 14.642  12.199 1.00 10.81 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 19.379 15.749  11.630 1.00 11.56 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.721 13.123  11.044 1.00 10.98 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 16.641 12.016  11.092 1.00 12.06 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 16.541 11.305  9.747  1.00 13.30 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 16.904 11.004  12.213 1.00 12.70 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 20.337 13.967  12.663 1.00 10.35 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 21.714 14.438  12.480 1.00 9.78  ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 22.564 13.197  12.330 1.00 10.57 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 22.359 12.174  13.038 1.00 10.97 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 22.168 15.278  13.685 1.00 10.29 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 23.616 15.865  13.598 1.00 11.15 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 23.707 17.226  14.295 1.00 12.75 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 24.647 14.917  14.250 1.00 12.00 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 23.544 13.266  11.416 1.00 10.72 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 24.481 12.184  11.149 1.00 9.58  ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 25.889 12.701  11.295 1.00 10.01 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 26.221 13.759  10.732 1.00 11.34 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 24.264 11.585  9.741  1.00 10.01 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 25.291 10.486  9.463  1.00 11.91 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 22.821 11.058  9.600  1.00 11.82 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 26.703 12.021  12.108 1.00 10.44 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 28.114 12.346  12.267 1.00 10.29 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 28.996 11.174  11.835 1.00 11.75 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 28.515 10.040  11.622 1.00 11.85 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 28.411 12.718  13.717 1.00 12.16 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 28.093 11.649  14.594 1.00 12.93 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 30.298 11.439  11.632 1.00 12.14 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 31.228 10.398  11.207 1.00 13.47 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 31.838 9.690   12.417 1.00 15.61 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 32.001 10.301  13.499 1.00 17.30 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 32.315 11.006  10.329 1.00 16.62 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 33.013 11.973  11.093 1.00 19.63 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 32.187 8.398   12.238 1.00 15.49 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 32.773 7.594   13.309 1.00 17.32 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 34.112 7.007   12.864 1.00 19.07 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 34.328 6.766   11.663 1.00 18.22 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 31.844 6.424   13.694 1.00 18.49 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 31.688 5.523   12.591 1.00 19.35 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 30.472 6.889   14.125 1.00 18.93 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? 34.968 6.713   13.843 1.00 20.09 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? 36.239 6.086   13.526 1.00 21.98 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? 36.032 4.582   13.311 1.00 22.10 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? 36.607 4.013   12.368 1.00 24.36 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? 37.288 6.440   14.590 1.00 25.90 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? 36.780 6.059   15.855 1.00 29.89 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? 37.581 7.923   14.615 1.00 26.62 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? 35.221 3.950   14.171 1.00 21.61 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? 34.939 2.515   14.071 1.00 22.51 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 33.717 2.224   13.182 1.00 21.73 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 32.765 3.013   13.185 1.00 20.91 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? 34.666 1.958   15.457 1.00 24.68 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 33.692 1.064   12.511 1.00 20.61 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 32.571 0.669   11.659 1.00 20.65 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 31.478 0.080   12.511 1.00 20.42 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 31.748 -0.692  13.433 1.00 21.63 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 32.995 -0.352  10.593 1.00 22.42 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 33.846 0.246   9.463  1.00 27.68 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 34.188 -0.823  8.459  1.00 33.82 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 35.046 -1.674  8.701  1.00 34.29 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 33.492 -0.821  7.324  1.00 35.61 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 30.243 0.423   12.181 1.00 17.89 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 29.078 -0.059  12.917 1.00 17.80 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 28.472 -1.304  12.325 1.00 16.92 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 28.768 -1.668  11.189 1.00 17.28 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 27.520 -1.909  13.087 1.00 16.11 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 26.918 -3.203  12.727 1.00 17.04 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 25.473 -3.170  12.268 1.00 16.57 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 24.926 -4.226  11.910 1.00 17.07 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 27.077 -4.179  13.883 1.00 18.20 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 28.790 -4.637  14.190 1.00 22.92 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 24.825 -2.024  12.383 1.00 14.04 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 23.443 -1.924  11.953 1.00 13.30 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 23.379 -1.891  10.420 1.00 15.32 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 24.254 -1.306  9.763  1.00 16.89 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 22.815 -0.661  12.557 1.00 12.75 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 22.698 -0.712  14.072 1.00 14.33 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 22.335 -1.810  14.605 1.00 15.18 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 22.914 0.335   14.732 1.00 14.27 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 22.341 -2.450  9.873  1.00 15.79 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 22.036 -2.419  8.425  1.00 17.08 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 20.723 -1.622  8.284  1.00 15.91 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 19.810 -1.788  9.102  1.00 16.56 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 21.834 -3.854  7.916  1.00 22.57 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 23.127 -4.515  7.910  1.00 26.40 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 21.172 -3.924  6.545  1.00 25.70 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 20.622 -0.769  7.248  1.00 14.65 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 19.394 -0.004  7.041  1.00 13.39 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 18.425 -0.793  6.155  1.00 13.65 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 18.801 -1.346  5.100  1.00 15.16 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 19.706 1.358   6.398  1.00 13.25 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 20.800 2.134   7.169  1.00 14.59 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 18.419 2.200   6.256  1.00 13.54 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 20.447 2.419   8.646  1.00 14.62 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.151 -0.835  6.561  1.00 12.37 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 16.111 -1.455  5.758  1.00 13.16 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 15.865 -0.613  4.490  1.00 13.48 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 15.834 0.634   4.513  1.00 13.89 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 14.818 -1.490  6.547  1.00 12.59 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 15.667 -1.318  3.347  1.00 15.33 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 15.351 -0.664  2.080  1.00 16.83 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 14.108 -1.418  1.598  1.00 18.64 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 14.185 -2.357  0.798  1.00 19.80 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 16.544 -0.773  1.098  1.00 17.36 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.867 -0.167  1.620  1.00 17.81 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.817 1.351   1.865  1.00 16.70 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 19.128 1.844   2.338  1.00 15.19 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 19.295 3.001   2.976  1.00 16.00 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 18.278 3.840   3.122  1.00 15.16 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 20.493 3.342   3.457  1.00 17.85 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 12.976 -0.982  2.091  1.00 18.15 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 11.715 -1.707  1.947  1.00 18.52 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 10.520 -0.798  2.126  1.00 19.15 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 10.609 0.376   2.460  1.00 20.43 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 11.672 -2.819  2.987  1.00 18.85 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 11.553 -2.173  4.670  1.00 18.42 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 9.316  -1.485  2.030  1.00 21.96 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 8.014  -0.878  2.190  1.00 24.24 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 7.276  -1.348  3.450  1.00 23.44 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 6.057  -1.194  3.515  1.00 24.05 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 7.131  -1.228  0.960  1.00 29.26 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 7.104  -2.697  0.565  1.00 40.18 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 6.793  -2.994  -0.625 1.00 43.43 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 7.368  -3.554  1.438  1.00 44.63 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 7.983  -1.902  4.443  1.00 20.80 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 7.300  -2.416  5.642  1.00 18.47 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 6.542  -1.336  6.424  1.00 18.62 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 7.000  -0.200  6.585  1.00 20.05 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 8.290  -3.143  6.553  1.00 19.40 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 9.009  -4.706  5.906  1.00 18.97 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 5.369  -1.701  6.920  1.00 16.12 ? 59  GLN   A N   1 
ATOM   407  C  CA  A GLN   A 1 53  ? 4.622  -0.827  7.798  0.50 15.66 ? 59  GLN   A CA  1 
ATOM   408  C  CA  B GLN   A 1 53  ? 4.510  -0.863  7.784  0.50 15.75 ? 59  GLN   A CA  1 
ATOM   409  C  C   . GLN   A 1 53  ? 4.255  -1.577  9.135  1.00 13.75 ? 59  GLN   A C   1 
ATOM   410  O  O   . GLN   A 1 53  ? 3.403  -1.155  9.917  1.00 14.45 ? 59  GLN   A O   1 
ATOM   411  C  CB  A GLN   A 1 53  ? 3.474  -0.159  7.039  0.50 17.75 ? 59  GLN   A CB  1 
ATOM   412  C  CB  B GLN   A 1 53  ? 3.162  -0.438  7.126  0.50 17.81 ? 59  GLN   A CB  1 
ATOM   413  C  CG  A GLN   A 1 53  ? 3.997  0.643   5.801  0.50 16.53 ? 59  GLN   A CG  1 
ATOM   414  C  CG  B GLN   A 1 53  ? 3.161  0.914   6.339  0.50 17.00 ? 59  GLN   A CG  1 
ATOM   415  C  CD  A GLN   A 1 53  ? 4.914  1.797   6.227  0.50 16.29 ? 59  GLN   A CD  1 
ATOM   416  C  CD  B GLN   A 1 53  ? 1.752  1.392   5.981  0.50 19.55 ? 59  GLN   A CD  1 
ATOM   417  O  OE1 A GLN   A 1 53  ? 4.736  2.345   7.329  0.50 17.24 ? 59  GLN   A OE1 1 
ATOM   418  O  OE1 B GLN   A 1 53  ? 1.249  1.197   4.863  0.50 21.03 ? 59  GLN   A OE1 1 
ATOM   419  N  NE2 A GLN   A 1 53  ? 5.938  2.180   5.432  0.50 15.57 ? 59  GLN   A NE2 1 
ATOM   420  N  NE2 B GLN   A 1 53  ? 1.066  2.024   6.916  0.50 16.21 ? 59  GLN   A NE2 1 
ATOM   421  N  N   . THR   A 1 54  ? 5.003  -2.685  9.407  1.00 12.39 ? 60  THR   A N   1 
ATOM   422  C  CA  . THR   A 1 54  ? 4.980  -3.390  10.677 1.00 13.15 ? 60  THR   A CA  1 
ATOM   423  C  C   . THR   A 1 54  ? 6.441  -3.652  11.082 1.00 12.47 ? 60  THR   A C   1 
ATOM   424  O  O   . THR   A 1 54  ? 7.316  -3.861  10.230 1.00 14.45 ? 60  THR   A O   1 
ATOM   425  C  CB  . THR   A 1 54  ? 4.200  -4.676  10.677 1.00 15.97 ? 60  THR   A CB  1 
ATOM   426  O  OG1 . THR   A 1 54  ? 4.819  -5.593  9.805  1.00 22.04 ? 60  THR   A OG1 1 
ATOM   427  C  CG2 . THR   A 1 54  ? 2.761  -4.482  10.283 1.00 16.20 ? 60  THR   A CG2 1 
ATOM   428  N  N   . GLY   A 1 55  ? 6.689  -3.578  12.377 1.00 11.50 ? 61  GLY   A N   1 
ATOM   429  C  CA  . GLY   A 1 55  ? 8.051  -3.793  12.864 1.00 11.70 ? 61  GLY   A CA  1 
ATOM   430  C  C   . GLY   A 1 55  ? 8.068  -3.813  14.369 1.00 10.55 ? 61  GLY   A C   1 
ATOM   431  O  O   . GLY   A 1 55  ? 7.037  -4.052  14.988 1.00 11.16 ? 61  GLY   A O   1 
ATOM   432  N  N   . VAL   A 1 56  ? 9.248  -3.593  14.963 1.00 9.69  ? 62  VAL   A N   1 
ATOM   433  C  CA  . VAL   A 1 56  ? 9.397  -3.653  16.395 1.00 9.10  ? 62  VAL   A CA  1 
ATOM   434  C  C   . VAL   A 1 56  ? 10.250 -2.476  16.818 1.00 9.37  ? 62  VAL   A C   1 
ATOM   435  O  O   . VAL   A 1 56  ? 11.235 -2.159  16.146 1.00 10.81 ? 62  VAL   A O   1 
ATOM   436  C  CB  . VAL   A 1 56  ? 10.100 -5.000  16.759 1.00 11.52 ? 62  VAL   A CB  1 
ATOM   437  C  CG1 . VAL   A 1 56  ? 10.456 -5.061  18.228 1.00 14.12 ? 62  VAL   A CG1 1 
ATOM   438  C  CG2 . VAL   A 1 56  ? 9.208  -6.201  16.413 1.00 12.46 ? 62  VAL   A CG2 1 
ATOM   439  N  N   . TYR   A 1 57  ? 9.896  -1.804  17.928 1.00 9.27  ? 63  TYR   A N   1 
ATOM   440  C  CA  . TYR   A 1 57  ? 10.755 -0.706  18.422 1.00 9.03  ? 63  TYR   A CA  1 
ATOM   441  C  C   . TYR   A 1 57  ? 11.184 -0.915  19.874 1.00 9.41  ? 63  TYR   A C   1 
ATOM   442  O  O   . TYR   A 1 57  ? 10.481 -1.559  20.648 1.00 10.25 ? 63  TYR   A O   1 
ATOM   443  C  CB  . TYR   A 1 57  ? 10.073 0.689   18.280 1.00 9.30  ? 63  TYR   A CB  1 
ATOM   444  C  CG  . TYR   A 1 57  ? 9.080  1.075   19.348 1.00 9.33  ? 63  TYR   A CG  1 
ATOM   445  C  CD1 . TYR   A 1 57  ? 7.801  0.539   19.360 1.00 10.90 ? 63  TYR   A CD1 1 
ATOM   446  C  CD2 . TYR   A 1 57  ? 9.413  1.985   20.347 1.00 10.11 ? 63  TYR   A CD2 1 
ATOM   447  C  CE1 . TYR   A 1 57  ? 6.886  0.888   20.333 1.00 11.68 ? 63  TYR   A CE1 1 
ATOM   448  C  CE2 . TYR   A 1 57  ? 8.485  2.360   21.316 1.00 10.65 ? 63  TYR   A CE2 1 
ATOM   449  C  CZ  . TYR   A 1 57  ? 7.239  1.779   21.319 1.00 12.33 ? 63  TYR   A CZ  1 
ATOM   450  O  OH  . TYR   A 1 57  ? 6.300  2.101   22.284 1.00 14.56 ? 63  TYR   A OH  1 
ATOM   451  N  N   . TYR   A 1 58  ? 12.317 -0.303  20.232 1.00 9.00  ? 64  TYR   A N   1 
ATOM   452  C  CA  . TYR   A 1 58  ? 12.783 -0.345  21.614 1.00 9.20  ? 64  TYR   A CA  1 
ATOM   453  C  C   . TYR   A 1 58  ? 12.310 0.860   22.402 1.00 9.79  ? 64  TYR   A C   1 
ATOM   454  O  O   . TYR   A 1 58  ? 12.541 2.011   22.013 1.00 10.12 ? 64  TYR   A O   1 
ATOM   455  C  CB  . TYR   A 1 58  ? 14.340 -0.400  21.660 1.00 9.80  ? 64  TYR   A CB  1 
ATOM   456  C  CG  . TYR   A 1 58  ? 14.811 -0.553  23.085 1.00 11.19 ? 64  TYR   A CG  1 
ATOM   457  C  CD1 . TYR   A 1 58  ? 14.474 -1.669  23.822 1.00 11.29 ? 64  TYR   A CD1 1 
ATOM   458  C  CD2 . TYR   A 1 58  ? 15.554 0.452   23.710 1.00 11.46 ? 64  TYR   A CD2 1 
ATOM   459  C  CE1 . TYR   A 1 58  ? 14.867 -1.798  25.144 1.00 12.93 ? 64  TYR   A CE1 1 
ATOM   460  C  CE2 . TYR   A 1 58  ? 15.924 0.345   25.038 1.00 12.21 ? 64  TYR   A CE2 1 
ATOM   461  C  CZ  . TYR   A 1 58  ? 15.638 -0.815  25.723 1.00 12.95 ? 64  TYR   A CZ  1 
ATOM   462  O  OH  . TYR   A 1 58  ? 15.974 -0.946  27.067 1.00 15.81 ? 64  TYR   A OH  1 
ATOM   463  N  N   . CYS   A 1 59  ? 11.695 0.573   23.536 1.00 9.42  ? 65  CYS   A N   1 
ATOM   464  C  CA  . CYS   A 1 59  ? 11.164 1.583   24.472 1.00 9.98  ? 65  CYS   A CA  1 
ATOM   465  C  C   . CYS   A 1 59  ? 11.992 1.573   25.778 1.00 10.94 ? 65  CYS   A C   1 
ATOM   466  O  O   . CYS   A 1 59  ? 11.781 0.667   26.623 1.00 10.80 ? 65  CYS   A O   1 
ATOM   467  C  CB  . CYS   A 1 59  ? 9.706  1.257   24.767 1.00 10.32 ? 65  CYS   A CB  1 
ATOM   468  S  SG  . CYS   A 1 59  ? 8.936  2.388   25.956 1.00 12.21 ? 65  CYS   A SG  1 
ATOM   469  N  N   . SER   A 1 60  ? 12.908 2.541   25.953 1.00 10.39 ? 66  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 60  ? 13.770 2.535   27.154 1.00 11.48 ? 66  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 60  ? 12.996 2.732   28.464 1.00 12.00 ? 66  SER   A C   1 
ATOM   472  O  O   . SER   A 1 60  ? 13.389 2.165   29.488 1.00 13.41 ? 66  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 60  ? 14.908 3.545   27.010 1.00 13.72 ? 66  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 60  ? 14.438 4.872   27.100 1.00 16.03 ? 66  SER   A OG  1 
ATOM   475  N  N   . SER   A 1 61  ? 11.849 3.443   28.431 1.00 10.91 ? 67  SER   A N   1 
ATOM   476  C  CA  . SER   A 1 61  ? 11.029 3.660   29.621 1.00 11.24 ? 67  SER   A CA  1 
ATOM   477  C  C   . SER   A 1 61  ? 10.222 2.437   30.068 1.00 11.20 ? 67  SER   A C   1 
ATOM   478  O  O   . SER   A 1 61  ? 9.574  2.470   31.107 1.00 12.10 ? 67  SER   A O   1 
ATOM   479  C  CB  . SER   A 1 61  ? 10.103 4.866   29.476 1.00 11.77 ? 67  SER   A CB  1 
ATOM   480  O  OG  . SER   A 1 61  ? 9.153  4.677   28.456 1.00 13.26 ? 67  SER   A OG  1 
ATOM   481  N  N   . ARG   A 1 62  ? 10.337 1.329   29.288 1.00 11.41 ? 68  ARG   A N   1 
ATOM   482  C  CA  . ARG   A 1 62  ? 9.749  0.041   29.687 1.00 11.94 ? 68  ARG   A CA  1 
ATOM   483  C  C   . ARG   A 1 62  ? 10.795 -1.094  29.631 1.00 12.97 ? 68  ARG   A C   1 
ATOM   484  O  O   . ARG   A 1 62  ? 10.450 -2.257  29.902 1.00 13.48 ? 68  ARG   A O   1 
ATOM   485  C  CB  . ARG   A 1 62  ? 8.583  -0.301  28.737 1.00 12.63 ? 68  ARG   A CB  1 
ATOM   486  C  CG  . ARG   A 1 62  ? 7.401  0.655   28.879 1.00 13.82 ? 68  ARG   A CG  1 
ATOM   487  C  CD  . ARG   A 1 62  ? 6.621  0.364   30.134 1.00 13.68 ? 68  ARG   A CD  1 
ATOM   488  N  NE  . ARG   A 1 62  ? 5.470  1.264   30.285 1.00 14.84 ? 68  ARG   A NE  1 
ATOM   489  C  CZ  . ARG   A 1 62  ? 5.500  2.422   30.925 1.00 14.65 ? 68  ARG   A CZ  1 
ATOM   490  N  NH1 . ARG   A 1 62  ? 6.635  2.866   31.461 1.00 15.13 ? 68  ARG   A NH1 1 
ATOM   491  N  NH2 . ARG   A 1 62  ? 4.380  3.146   31.065 1.00 16.41 ? 68  ARG   A NH2 1 
ATOM   492  N  N   . ARG   A 1 63  ? 12.034 -0.811  29.210 1.00 13.07 ? 69  ARG   A N   1 
ATOM   493  C  CA  . ARG   A 1 63  ? 13.047 -1.861  28.952 1.00 14.63 ? 69  ARG   A CA  1 
ATOM   494  C  C   . ARG   A 1 63  ? 12.480 -2.988  28.079 1.00 17.01 ? 69  ARG   A C   1 
ATOM   495  O  O   . ARG   A 1 63  ? 12.698 -4.194  28.353 1.00 19.62 ? 69  ARG   A O   1 
ATOM   496  C  CB  . ARG   A 1 63  ? 13.563 -2.454  30.251 1.00 18.19 ? 69  ARG   A CB  1 
ATOM   497  C  CG  . ARG   A 1 63  ? 14.592 -1.630  30.793 1.00 19.99 ? 69  ARG   A CG  1 
ATOM   498  C  CD  . ARG   A 1 63  ? 15.404 -2.491  31.754 1.00 20.71 ? 69  ARG   A CD  1 
ATOM   499  N  NE  . ARG   A 1 63  ? 16.162 -1.553  32.548 1.00 22.04 ? 69  ARG   A NE  1 
ATOM   500  C  CZ  . ARG   A 1 63  ? 15.815 -1.143  33.759 1.00 19.05 ? 69  ARG   A CZ  1 
ATOM   501  N  NH1 . ARG   A 1 63  ? 14.746 -1.658  34.367 1.00 18.93 ? 69  ARG   A NH1 1 
ATOM   502  N  NH2 . ARG   A 1 63  ? 16.545 -0.236  34.389 1.00 19.62 ? 69  ARG   A NH2 1 
ATOM   503  N  N   . LYS   A 1 64  ? 11.739 -2.620  27.045 1.00 14.18 ? 70  LYS   A N   1 
ATOM   504  C  CA  . LYS   A 1 64  ? 11.064 -3.625  26.235 1.00 14.86 ? 70  LYS   A CA  1 
ATOM   505  C  C   . LYS   A 1 64  ? 10.998 -3.247  24.794 1.00 13.64 ? 70  LYS   A C   1 
ATOM   506  O  O   . LYS   A 1 64  ? 10.927 -2.056  24.448 1.00 13.72 ? 70  LYS   A O   1 
ATOM   507  C  CB  . LYS   A 1 64  ? 9.611  -3.777  26.729 1.00 17.95 ? 70  LYS   A CB  1 
ATOM   508  C  CG  . LYS   A 1 64  ? 9.474  -4.702  27.944 1.00 26.19 ? 70  LYS   A CG  1 
ATOM   509  C  CD  . LYS   A 1 64  ? 8.049  -5.139  28.173 1.00 34.54 ? 70  LYS   A CD  1 
ATOM   510  C  CE  . LYS   A 1 64  ? 7.945  -5.868  29.498 1.00 40.25 ? 70  LYS   A CE  1 
ATOM   511  N  NZ  . LYS   A 1 64  ? 8.410  -5.010  30.627 1.00 43.87 ? 70  LYS   A NZ  1 
ATOM   512  N  N   . HIS   A 1 65  ? 11.013 -4.257  23.931 1.00 12.61 ? 71  HIS   A N   1 
ATOM   513  C  CA  . HIS   A 1 65  ? 10.767 -4.118  22.500 1.00 11.71 ? 71  HIS   A CA  1 
ATOM   514  C  C   . HIS   A 1 65  ? 9.291  -4.455  22.232 1.00 13.42 ? 71  HIS   A C   1 
ATOM   515  O  O   . HIS   A 1 65  ? 8.783  -5.498  22.697 1.00 17.21 ? 71  HIS   A O   1 
ATOM   516  C  CB  . HIS   A 1 65  ? 11.662 -5.067  21.678 1.00 11.00 ? 71  HIS   A CB  1 
ATOM   517  C  CG  . HIS   A 1 65  ? 13.125 -4.751  21.778 1.00 12.49 ? 71  HIS   A CG  1 
ATOM   518  N  ND1 . HIS   A 1 65  ? 13.812 -4.063  20.811 1.00 15.64 ? 71  HIS   A ND1 1 
ATOM   519  C  CD2 . HIS   A 1 65  ? 13.975 -5.057  22.789 1.00 12.13 ? 71  HIS   A CD2 1 
ATOM   520  C  CE1 . HIS   A 1 65  ? 15.083 -4.022  21.231 1.00 14.36 ? 71  HIS   A CE1 1 
ATOM   521  N  NE2 . HIS   A 1 65  ? 15.208 -4.589  22.414 1.00 16.35 ? 71  HIS   A NE2 1 
ATOM   522  N  N   . TYR   A 1 66  ? 8.600  -3.590  21.473 1.00 11.12 ? 72  TYR   A N   1 
ATOM   523  C  CA  . TYR   A 1 66  ? 7.157  -3.793  21.211 1.00 11.74 ? 72  TYR   A CA  1 
ATOM   524  C  C   . TYR   A 1 66  ? 6.903  -3.908  19.733 1.00 10.56 ? 72  TYR   A C   1 
ATOM   525  O  O   . TYR   A 1 66  ? 7.427  -3.095  18.942 1.00 10.44 ? 72  TYR   A O   1 
ATOM   526  C  CB  . TYR   A 1 66  ? 6.336  -2.555  21.688 1.00 11.76 ? 72  TYR   A CB  1 
ATOM   527  C  CG  . TYR   A 1 66  ? 6.264  -2.392  23.190 1.00 12.46 ? 72  TYR   A CG  1 
ATOM   528  C  CD1 . TYR   A 1 66  ? 5.414  -3.192  23.960 1.00 14.12 ? 72  TYR   A CD1 1 
ATOM   529  C  CD2 . TYR   A 1 66  ? 6.971  -1.393  23.829 1.00 12.81 ? 72  TYR   A CD2 1 
ATOM   530  C  CE1 . TYR   A 1 66  ? 5.305  -3.019  25.335 1.00 15.25 ? 72  TYR   A CE1 1 
ATOM   531  C  CE2 . TYR   A 1 66  ? 6.879  -1.215  25.209 1.00 13.78 ? 72  TYR   A CE2 1 
ATOM   532  C  CZ  . TYR   A 1 66  ? 6.022  -2.014  25.953 1.00 14.66 ? 72  TYR   A CZ  1 
ATOM   533  O  OH  . TYR   A 1 66  ? 5.936  -1.837  27.325 1.00 17.53 ? 72  TYR   A OH  1 
ATOM   534  N  N   . PRO   A 1 67  ? 6.081  -4.874  19.323 1.00 10.99 ? 73  PRO   A N   1 
ATOM   535  C  CA  . PRO   A 1 67  ? 5.679  -4.919  17.900 1.00 11.11 ? 73  PRO   A CA  1 
ATOM   536  C  C   . PRO   A 1 67  ? 4.669  -3.797  17.627 1.00 12.78 ? 73  PRO   A C   1 
ATOM   537  O  O   . PRO   A 1 67  ? 3.723  -3.592  18.429 1.00 15.75 ? 73  PRO   A O   1 
ATOM   538  C  CB  . PRO   A 1 67  ? 4.997  -6.299  17.728 1.00 12.95 ? 73  PRO   A CB  1 
ATOM   539  C  CG  . PRO   A 1 67  ? 4.688  -6.752  19.105 1.00 14.63 ? 73  PRO   A CG  1 
ATOM   540  C  CD  . PRO   A 1 67  ? 5.487  -5.958  20.129 1.00 11.47 ? 73  PRO   A CD  1 
ATOM   541  N  N   . VAL   A 1 68  ? 4.785  -3.177  16.474 1.00 11.09 ? 74  VAL   A N   1 
ATOM   542  C  CA  . VAL   A 1 68  ? 3.871  -2.073  16.114 1.00 12.73 ? 74  VAL   A CA  1 
ATOM   543  C  C   . VAL   A 1 68  ? 3.555  -2.059  14.647 1.00 12.00 ? 74  VAL   A C   1 
ATOM   544  O  O   . VAL   A 1 68  ? 4.349  -2.443  13.821 1.00 13.13 ? 74  VAL   A O   1 
ATOM   545  C  CB  . VAL   A 1 68  ? 4.442  -0.695  16.492 1.00 15.59 ? 74  VAL   A CB  1 
ATOM   546  C  CG1 . VAL   A 1 68  ? 4.376  -0.477  17.992 1.00 16.62 ? 74  VAL   A CG1 1 
ATOM   547  C  CG2 . VAL   A 1 68  ? 5.847  -0.507  15.966 1.00 16.20 ? 74  VAL   A CG2 1 
ATOM   548  N  N   . SER   A 1 69  ? 2.361  -1.499  14.327 1.00 12.01 ? 75  SER   A N   1 
ATOM   549  C  CA  . SER   A 1 69  ? 1.983  -1.094  12.962 1.00 12.16 ? 75  SER   A CA  1 
ATOM   550  C  C   . SER   A 1 69  ? 2.197  0.419   12.906 1.00 11.48 ? 75  SER   A C   1 
ATOM   551  O  O   . SER   A 1 69  ? 1.819  1.127   13.867 1.00 12.80 ? 75  SER   A O   1 
ATOM   552  C  CB  . SER   A 1 69  ? 0.496  -1.356  12.747 1.00 16.77 ? 75  SER   A CB  1 
ATOM   553  O  OG  . SER   A 1 69  ? 0.287  -2.758  12.767 1.00 23.83 ? 75  SER   A OG  1 
ATOM   554  N  N   . PHE   A 1 70  ? 2.813  0.926   11.847 1.00 12.12 ? 76  PHE   A N   1 
ATOM   555  C  CA  . PHE   A 1 70  ? 3.134  2.354   11.768 1.00 12.02 ? 76  PHE   A CA  1 
ATOM   556  C  C   . PHE   A 1 70  ? 2.733  2.925   10.426 1.00 12.51 ? 76  PHE   A C   1 
ATOM   557  O  O   . PHE   A 1 70  ? 2.662  2.202   9.425  1.00 14.32 ? 76  PHE   A O   1 
ATOM   558  C  CB  . PHE   A 1 70  ? 4.642  2.611   12.112 1.00 13.10 ? 76  PHE   A CB  1 
ATOM   559  C  CG  . PHE   A 1 70  ? 5.646  1.788   11.318 1.00 12.03 ? 76  PHE   A CG  1 
ATOM   560  C  CD1 . PHE   A 1 70  ? 6.058  0.537   11.763 1.00 11.30 ? 76  PHE   A CD1 1 
ATOM   561  C  CD2 . PHE   A 1 70  ? 6.223  2.289   10.162 1.00 12.16 ? 76  PHE   A CD2 1 
ATOM   562  C  CE1 . PHE   A 1 70  ? 6.989  -0.202  11.044 1.00 12.32 ? 76  PHE   A CE1 1 
ATOM   563  C  CE2 . PHE   A 1 70  ? 7.181  1.551   9.456  1.00 12.61 ? 76  PHE   A CE2 1 
ATOM   564  C  CZ  . PHE   A 1 70  ? 7.535  0.303   9.900  1.00 12.76 ? 76  PHE   A CZ  1 
ATOM   565  N  N   . SER   A 1 71  ? 2.453  4.224   10.391 1.00 12.54 ? 77  SER   A N   1 
ATOM   566  C  CA  . SER   A 1 71  ? 2.032  4.888   9.168  1.00 13.61 ? 77  SER   A CA  1 
ATOM   567  C  C   . SER   A 1 71  ? 3.186  5.124   8.202  1.00 14.04 ? 77  SER   A C   1 
ATOM   568  O  O   . SER   A 1 71  ? 4.360  5.001   8.588  1.00 14.04 ? 77  SER   A O   1 
ATOM   569  C  CB  . SER   A 1 71  ? 1.321  6.206   9.502  1.00 15.66 ? 77  SER   A CB  1 
ATOM   570  O  OG  . SER   A 1 71  ? 2.171  7.148   10.157 1.00 17.32 ? 77  SER   A OG  1 
ATOM   571  N  N   . LYS   A 1 72  ? 2.896  5.444   6.951  1.00 14.30 ? 78  LYS   A N   1 
ATOM   572  C  CA  . LYS   A 1 72  ? 3.946  5.762   5.992  1.00 14.52 ? 78  LYS   A CA  1 
ATOM   573  C  C   . LYS   A 1 72  ? 4.575  7.135   6.324  1.00 15.62 ? 78  LYS   A C   1 
ATOM   574  O  O   . LYS   A 1 72  ? 3.898  7.996   6.891  1.00 15.97 ? 78  LYS   A O   1 
ATOM   575  C  CB  . LYS   A 1 72  ? 3.364  5.745   4.567  1.00 16.82 ? 78  LYS   A CB  1 
ATOM   576  C  CG  . LYS   A 1 72  ? 2.904  4.357   4.162  1.00 20.87 ? 78  LYS   A CG  1 
ATOM   577  C  CD  . LYS   A 1 72  ? 2.575  4.291   2.677  1.00 26.56 ? 78  LYS   A CD  1 
ATOM   578  C  CE  . LYS   A 1 72  ? 2.322  2.870   2.246  1.00 32.99 ? 78  LYS   A CE  1 
ATOM   579  N  NZ  . LYS   A 1 72  ? 2.497  2.748   0.785  1.00 37.37 ? 78  LYS   A NZ  1 
ATOM   580  N  N   . PRO   A 1 73  ? 5.842  7.376   5.974  1.00 14.86 ? 79  PRO   A N   1 
ATOM   581  C  CA  . PRO   A 1 73  ? 6.480  8.667   6.309  1.00 15.35 ? 79  PRO   A CA  1 
ATOM   582  C  C   . PRO   A 1 73  ? 5.685  9.840   5.759  1.00 15.74 ? 79  PRO   A C   1 
ATOM   583  O  O   . PRO   A 1 73  ? 5.314  9.845   4.588  1.00 17.95 ? 79  PRO   A O   1 
ATOM   584  C  CB  . PRO   A 1 73  ? 7.899  8.555   5.711  1.00 17.68 ? 79  PRO   A CB  1 
ATOM   585  C  CG  . PRO   A 1 73  ? 8.022  7.187   5.153  1.00 19.95 ? 79  PRO   A CG  1 
ATOM   586  C  CD  . PRO   A 1 73  ? 6.762  6.439   5.282  1.00 16.25 ? 79  PRO   A CD  1 
ATOM   587  N  N   . SER   A 1 74  ? 5.403  10.805  6.614  1.00 15.23 ? 80  SER   A N   1 
ATOM   588  C  CA  . SER   A 1 74  ? 4.526  11.907  6.246  1.00 17.14 ? 80  SER   A CA  1 
ATOM   589  C  C   . SER   A 1 74  ? 4.920  13.193  6.978  1.00 15.82 ? 80  SER   A C   1 
ATOM   590  O  O   . SER   A 1 74  ? 5.724  13.184  7.915  1.00 15.33 ? 80  SER   A O   1 
ATOM   591  C  CB  . SER   A 1 74  ? 3.071  11.554  6.615  1.00 22.52 ? 80  SER   A CB  1 
ATOM   592  O  OG  . SER   A 1 74  ? 2.708  10.222  6.285  1.00 31.73 ? 80  SER   A OG  1 
ATOM   593  N  N   . LEU   A 1 75  ? 4.201  14.292  6.630  1.00 17.35 ? 81  LEU   A N   1 
ATOM   594  C  CA  . LEU   A 1 75  ? 4.376  15.585  7.266  1.00 19.09 ? 81  LEU   A CA  1 
ATOM   595  C  C   . LEU   A 1 75  ? 3.284  15.671  8.331  1.00 20.70 ? 81  LEU   A C   1 
ATOM   596  O  O   . LEU   A 1 75  ? 2.080  15.728  8.005  1.00 22.95 ? 81  LEU   A O   1 
ATOM   597  C  CB  . LEU   A 1 75  ? 4.168  16.672  6.188  1.00 20.33 ? 81  LEU   A CB  1 
ATOM   598  C  CG  . LEU   A 1 75  ? 4.492  18.097  6.591  1.00 23.17 ? 81  LEU   A CG  1 
ATOM   599  C  CD1 . LEU   A 1 75  ? 5.980  18.283  6.786  1.00 23.46 ? 81  LEU   A CD1 1 
ATOM   600  C  CD2 . LEU   A 1 75  ? 4.029  19.084  5.513  1.00 24.91 ? 81  LEU   A CD2 1 
ATOM   601  N  N   . ILE   A 1 76  ? 3.683  15.641  9.615  1.00 19.58 ? 82  ILE   A N   1 
ATOM   602  C  CA  . ILE   A 1 76  ? 2.786  15.595  10.768 1.00 21.53 ? 82  ILE   A CA  1 
ATOM   603  C  C   . ILE   A 1 76  ? 3.018  16.747  11.708 1.00 22.29 ? 82  ILE   A C   1 
ATOM   604  O  O   . ILE   A 1 76  ? 4.168  17.118  12.004 1.00 21.14 ? 82  ILE   A O   1 
ATOM   605  C  CB  . ILE   A 1 76  ? 3.048  14.270  11.518 1.00 23.39 ? 82  ILE   A CB  1 
ATOM   606  C  CG1 . ILE   A 1 76  ? 2.840  13.053  10.575 1.00 25.49 ? 82  ILE   A CG1 1 
ATOM   607  C  CG2 . ILE   A 1 76  ? 2.247  14.181  12.853 1.00 25.15 ? 82  ILE   A CG2 1 
ATOM   608  C  CD1 . ILE   A 1 76  ? 2.752  11.790  11.141 1.00 26.80 ? 82  ILE   A CD1 1 
ATOM   609  N  N   . PHE   A 1 77  ? 1.921  17.304  12.235 1.00 23.04 ? 83  PHE   A N   1 
ATOM   610  C  CA  . PHE   A 1 77  ? 2.034  18.399  13.187 1.00 23.11 ? 83  PHE   A CA  1 
ATOM   611  C  C   . PHE   A 1 77  ? 2.375  17.811  14.548 1.00 23.68 ? 83  PHE   A C   1 
ATOM   612  O  O   . PHE   A 1 77  ? 1.760  16.837  14.990 1.00 25.90 ? 83  PHE   A O   1 
ATOM   613  C  CB  . PHE   A 1 77  ? 0.718  19.194  13.271 1.00 24.30 ? 83  PHE   A CB  1 
ATOM   614  C  CG  . PHE   A 1 77  ? 0.920  20.506  13.970 1.00 27.07 ? 83  PHE   A CG  1 
ATOM   615  C  CD1 . PHE   A 1 77  ? 1.587  21.545  13.347 1.00 29.13 ? 83  PHE   A CD1 1 
ATOM   616  C  CD2 . PHE   A 1 77  ? 0.483  20.684  15.269 1.00 29.55 ? 83  PHE   A CD2 1 
ATOM   617  C  CE1 . PHE   A 1 77  ? 1.795  22.746  13.999 1.00 31.08 ? 83  PHE   A CE1 1 
ATOM   618  C  CE2 . PHE   A 1 77  ? 0.674  21.894  15.915 1.00 30.07 ? 83  PHE   A CE2 1 
ATOM   619  C  CZ  . PHE   A 1 77  ? 1.318  22.919  15.274 1.00 30.71 ? 83  PHE   A CZ  1 
ATOM   620  N  N   . VAL   A 1 78  ? 3.472  18.306  15.147 1.00 21.22 ? 84  VAL   A N   1 
ATOM   621  C  CA  . VAL   A 1 78  ? 3.960  17.838  16.427 1.00 19.53 ? 84  VAL   A CA  1 
ATOM   622  C  C   . VAL   A 1 78  ? 3.861  19.000  17.420 1.00 18.76 ? 84  VAL   A C   1 
ATOM   623  O  O   . VAL   A 1 78  ? 4.343  20.087  17.115 1.00 19.08 ? 84  VAL   A O   1 
ATOM   624  C  CB  . VAL   A 1 78  ? 5.433  17.345  16.308 1.00 17.37 ? 84  VAL   A CB  1 
ATOM   625  C  CG1 . VAL   A 1 78  ? 5.952  16.863  17.667 1.00 17.93 ? 84  VAL   A CG1 1 
ATOM   626  C  CG2 . VAL   A 1 78  ? 5.526  16.224  15.259 1.00 18.42 ? 84  VAL   A CG2 1 
ATOM   627  N  N   . GLU   A 1 79  ? 3.318  18.725  18.604 1.00 18.62 ? 85  GLU   A N   1 
ATOM   628  C  CA  . GLU   A 1 79  ? 3.159  19.740  19.654 1.00 19.94 ? 85  GLU   A CA  1 
ATOM   629  C  C   . GLU   A 1 79  ? 4.509  20.225  20.160 1.00 19.78 ? 85  GLU   A C   1 
ATOM   630  O  O   . GLU   A 1 79  ? 5.509  19.510  20.073 1.00 19.46 ? 85  GLU   A O   1 
ATOM   631  C  CB  . GLU   A 1 79  ? 2.338  19.178  20.821 1.00 24.10 ? 85  GLU   A CB  1 
ATOM   632  C  CG  . GLU   A 1 79  ? 0.867  18.967  20.483 1.00 32.36 ? 85  GLU   A CG  1 
ATOM   633  C  CD  . GLU   A 1 79  ? 0.192  20.218  19.949 1.00 44.10 ? 85  GLU   A CD  1 
ATOM   634  O  OE1 . GLU   A 1 79  ? 0.276  21.275  20.616 1.00 47.26 ? 85  GLU   A OE1 1 
ATOM   635  O  OE2 . GLU   A 1 79  ? -0.389 20.154  18.842 1.00 48.36 ? 85  GLU   A OE2 1 
ATOM   636  N  N   . ALA   A 1 80  ? 4.518  21.432  20.754 1.00 20.51 ? 86  ALA   A N   1 
ATOM   637  C  CA  . ALA   A 1 80  ? 5.728  22.007  21.332 1.00 21.87 ? 86  ALA   A CA  1 
ATOM   638  C  C   . ALA   A 1 80  ? 6.294  21.112  22.401 1.00 22.57 ? 86  ALA   A C   1 
ATOM   639  O  O   . ALA   A 1 80  ? 5.550  20.455  23.150 1.00 24.17 ? 86  ALA   A O   1 
ATOM   640  C  CB  . ALA   A 1 80  ? 5.412  23.357  21.955 1.00 22.60 ? 86  ALA   A CB  1 
ATOM   641  N  N   . SER   A 1 81  ? 7.616  21.033  22.439 1.00 22.09 ? 87  SER   A N   1 
ATOM   642  C  CA  . SER   A 1 81  ? 8.314  20.252  23.458 1.00 21.68 ? 87  SER   A CA  1 
ATOM   643  C  C   . SER   A 1 81  ? 9.443  21.138  24.030 1.00 22.95 ? 87  SER   A C   1 
ATOM   644  O  O   . SER   A 1 81  ? 9.538  22.313  23.684 1.00 23.47 ? 87  SER   A O   1 
ATOM   645  C  CB  . SER   A 1 81  ? 8.926  18.995  22.838 1.00 21.45 ? 87  SER   A CB  1 
ATOM   646  O  OG  . SER   A 1 81  ? 9.981  19.350  21.946 1.00 20.43 ? 87  SER   A OG  1 
ATOM   647  N  N   . GLU   A 1 82  ? 10.360 20.541  24.829 1.00 23.74 ? 88  GLU   A N   1 
ATOM   648  C  CA  . GLU   A 1 82  ? 11.508 21.314  25.312 1.00 23.90 ? 88  GLU   A CA  1 
ATOM   649  C  C   . GLU   A 1 82  ? 12.500 21.625  24.175 1.00 21.36 ? 88  GLU   A C   1 
ATOM   650  O  O   . GLU   A 1 82  ? 13.300 22.557  24.295 1.00 22.08 ? 88  GLU   A O   1 
ATOM   651  C  CB  . GLU   A 1 82  ? 12.236 20.539  26.419 1.00 28.59 ? 88  GLU   A CB  1 
ATOM   652  C  CG  . GLU   A 1 82  ? 11.424 20.492  27.699 1.00 37.48 ? 88  GLU   A CG  1 
ATOM   653  C  CD  . GLU   A 1 82  ? 12.035 19.668  28.818 1.00 47.43 ? 88  GLU   A CD  1 
ATOM   654  O  OE1 . GLU   A 1 82  ? 13.184 19.190  28.658 1.00 47.76 ? 88  GLU   A OE1 1 
ATOM   655  O  OE2 . GLU   A 1 82  ? 11.351 19.486  29.851 1.00 51.66 ? 88  GLU   A OE2 1 
ATOM   656  N  N   . TYR   A 1 83  ? 12.436 20.884  23.046 1.00 19.33 ? 89  TYR   A N   1 
ATOM   657  C  CA  . TYR   A 1 83  ? 13.436 21.029  21.986 1.00 18.29 ? 89  TYR   A CA  1 
ATOM   658  C  C   . TYR   A 1 83  ? 12.966 21.691  20.708 1.00 17.53 ? 89  TYR   A C   1 
ATOM   659  O  O   . TYR   A 1 83  ? 13.800 22.183  19.961 1.00 17.66 ? 89  TYR   A O   1 
ATOM   660  C  CB  . TYR   A 1 83  ? 14.042 19.661  21.664 1.00 19.07 ? 89  TYR   A CB  1 
ATOM   661  C  CG  . TYR   A 1 83  ? 14.828 19.132  22.837 1.00 21.38 ? 89  TYR   A CG  1 
ATOM   662  C  CD1 . TYR   A 1 83  ? 16.149 19.505  23.039 1.00 24.51 ? 89  TYR   A CD1 1 
ATOM   663  C  CD2 . TYR   A 1 83  ? 14.247 18.287  23.762 1.00 23.65 ? 89  TYR   A CD2 1 
ATOM   664  C  CE1 . TYR   A 1 83  ? 16.889 18.994  24.100 1.00 26.90 ? 89  TYR   A CE1 1 
ATOM   665  C  CE2 . TYR   A 1 83  ? 14.966 17.802  24.850 1.00 26.31 ? 89  TYR   A CE2 1 
ATOM   666  C  CZ  . TYR   A 1 83  ? 16.278 18.179  25.028 1.00 29.47 ? 89  TYR   A CZ  1 
ATOM   667  O  OH  . TYR   A 1 83  ? 16.984 17.668  26.099 1.00 34.76 ? 89  TYR   A OH  1 
ATOM   668  N  N   . TYR   A 1 84  ? 11.649 21.724  20.444 1.00 17.79 ? 90  TYR   A N   1 
ATOM   669  C  CA  . TYR   A 1 84  ? 11.123 22.392  19.246 1.00 17.11 ? 90  TYR   A CA  1 
ATOM   670  C  C   . TYR   A 1 84  ? 9.790  23.079  19.588 1.00 18.30 ? 90  TYR   A C   1 
ATOM   671  O  O   . TYR   A 1 84  ? 9.017  22.496  20.364 1.00 18.75 ? 90  TYR   A O   1 
ATOM   672  C  CB  . TYR   A 1 84  ? 10.814 21.363  18.130 1.00 17.08 ? 90  TYR   A CB  1 
ATOM   673  C  CG  . TYR   A 1 84  ? 12.009 20.598  17.588 1.00 14.84 ? 90  TYR   A CG  1 
ATOM   674  C  CD1 . TYR   A 1 84  ? 12.908 21.196  16.708 1.00 14.93 ? 90  TYR   A CD1 1 
ATOM   675  C  CD2 . TYR   A 1 84  ? 12.237 19.280  17.953 1.00 14.83 ? 90  TYR   A CD2 1 
ATOM   676  C  CE1 . TYR   A 1 84  ? 13.988 20.487  16.184 1.00 14.01 ? 90  TYR   A CE1 1 
ATOM   677  C  CE2 . TYR   A 1 84  ? 13.328 18.572  17.460 1.00 14.71 ? 90  TYR   A CE2 1 
ATOM   678  C  CZ  . TYR   A 1 84  ? 14.198 19.179  16.573 1.00 14.11 ? 90  TYR   A CZ  1 
ATOM   679  O  OH  . TYR   A 1 84  ? 15.291 18.465  16.096 1.00 13.86 ? 90  TYR   A OH  1 
ATOM   680  N  N   . PRO   A 1 85  ? 9.473  24.200  18.922 1.00 19.84 ? 91  PRO   A N   1 
ATOM   681  C  CA  . PRO   A 1 85  ? 8.107  24.755  19.056 1.00 20.60 ? 91  PRO   A CA  1 
ATOM   682  C  C   . PRO   A 1 85  ? 7.140  23.799  18.330 1.00 22.27 ? 91  PRO   A C   1 
ATOM   683  O  O   . PRO   A 1 85  ? 7.567  22.878  17.589 1.00 21.98 ? 91  PRO   A O   1 
ATOM   684  C  CB  . PRO   A 1 85  ? 8.199  26.107  18.307 1.00 22.96 ? 91  PRO   A CB  1 
ATOM   685  C  CG  . PRO   A 1 85  ? 9.253  25.907  17.294 1.00 23.33 ? 91  PRO   A CG  1 
ATOM   686  C  CD  . PRO   A 1 85  ? 10.276 24.950  17.927 1.00 20.77 ? 91  PRO   A CD  1 
ATOM   687  N  N   . ALA   A 1 86  ? 5.822  24.050  18.433 1.00 22.97 ? 92  ALA   A N   1 
ATOM   688  C  CA  . ALA   A 1 86  ? 4.829  23.244  17.707 1.00 22.98 ? 92  ALA   A CA  1 
ATOM   689  C  C   . ALA   A 1 86  ? 5.074  23.538  16.215 1.00 23.25 ? 92  ALA   A C   1 
ATOM   690  O  O   . ALA   A 1 86  ? 5.305  24.692  15.831 1.00 25.11 ? 92  ALA   A O   1 
ATOM   691  C  CB  . ALA   A 1 86  ? 3.408  23.662  18.120 1.00 23.53 ? 92  ALA   A CB  1 
ATOM   692  N  N   . ARG   A 1 87  ? 5.189  22.484  15.406 1.00 22.65 ? 93  ARG   A N   1 
ATOM   693  C  CA  . ARG   A 1 87  ? 5.571  22.650  14.011 1.00 21.88 ? 93  ARG   A CA  1 
ATOM   694  C  C   . ARG   A 1 87  ? 5.229  21.377  13.252 1.00 21.49 ? 93  ARG   A C   1 
ATOM   695  O  O   . ARG   A 1 87  ? 4.878  20.361  13.859 1.00 22.21 ? 93  ARG   A O   1 
ATOM   696  C  CB  . ARG   A 1 87  ? 7.107  22.873  13.931 1.00 22.12 ? 93  ARG   A CB  1 
ATOM   697  C  CG  . ARG   A 1 87  ? 7.942  21.544  14.025 1.00 21.98 ? 93  ARG   A CG  1 
ATOM   698  C  CD  . ARG   A 1 87  ? 9.302  21.723  14.616 1.00 22.07 ? 93  ARG   A CD  1 
ATOM   699  N  NE  . ARG   A 1 87  ? 10.257 20.672  14.218 1.00 21.03 ? 93  ARG   A NE  1 
ATOM   700  C  CZ  . ARG   A 1 87  ? 10.334 19.444  14.695 1.00 24.35 ? 93  ARG   A CZ  1 
ATOM   701  N  NH1 . ARG   A 1 87  ? 9.424  18.998  15.576 1.00 24.47 ? 93  ARG   A NH1 1 
ATOM   702  N  NH2 . ARG   A 1 87  ? 11.304 18.629  14.276 1.00 18.77 ? 93  ARG   A NH2 1 
ATOM   703  N  N   . TYR   A 1 88  ? 5.426  21.407  11.932 1.00 21.80 ? 94  TYR   A N   1 
ATOM   704  C  CA  . TYR   A 1 88  ? 5.297  20.229  11.110 1.00 22.28 ? 94  TYR   A CA  1 
ATOM   705  C  C   . TYR   A 1 88  ? 6.668  19.551  10.998 1.00 19.87 ? 94  TYR   A C   1 
ATOM   706  O  O   . TYR   A 1 88  ? 7.654  20.187  10.625 1.00 20.31 ? 94  TYR   A O   1 
ATOM   707  C  CB  . TYR   A 1 88  ? 4.840  20.615  9.715  1.00 23.52 ? 94  TYR   A CB  1 
ATOM   708  C  CG  . TYR   A 1 88  ? 3.366  20.932  9.686  1.00 24.85 ? 94  TYR   A CG  1 
ATOM   709  C  CD1 . TYR   A 1 88  ? 2.424  19.922  9.606  1.00 25.79 ? 94  TYR   A CD1 1 
ATOM   710  C  CD2 . TYR   A 1 88  ? 2.911  22.237  9.800  1.00 26.55 ? 94  TYR   A CD2 1 
ATOM   711  C  CE1 . TYR   A 1 88  ? 1.065  20.197  9.622  1.00 28.03 ? 94  TYR   A CE1 1 
ATOM   712  C  CE2 . TYR   A 1 88  ? 1.552  22.526  9.804  1.00 28.30 ? 94  TYR   A CE2 1 
ATOM   713  C  CZ  . TYR   A 1 88  ? 0.631  21.499  9.727  1.00 29.16 ? 94  TYR   A CZ  1 
ATOM   714  O  OH  . TYR   A 1 88  ? -0.723 21.742  9.737  1.00 32.54 ? 94  TYR   A OH  1 
ATOM   715  N  N   . GLN   A 1 89  ? 6.721  18.242  11.325 1.00 17.41 ? 95  GLN   A N   1 
ATOM   716  C  CA  . GLN   A 1 89  ? 7.932  17.421  11.198 1.00 15.27 ? 95  GLN   A CA  1 
ATOM   717  C  C   . GLN   A 1 89  ? 7.730  16.528  9.960  1.00 14.83 ? 95  GLN   A C   1 
ATOM   718  O  O   . GLN   A 1 89  ? 6.655  15.927  9.777  1.00 15.76 ? 95  GLN   A O   1 
ATOM   719  C  CB  . GLN   A 1 89  ? 8.153  16.585  12.466 1.00 15.74 ? 95  GLN   A CB  1 
ATOM   720  C  CG  . GLN   A 1 89  ? 9.412  15.776  12.374 1.00 15.22 ? 95  GLN   A CG  1 
ATOM   721  C  CD  . GLN   A 1 89  ? 9.969  15.311  13.722 1.00 15.17 ? 95  GLN   A CD  1 
ATOM   722  O  OE1 . GLN   A 1 89  ? 9.984  16.016  14.734 1.00 17.18 ? 95  GLN   A OE1 1 
ATOM   723  N  NE2 . GLN   A 1 89  ? 10.486 14.090  13.727 1.00 14.57 ? 95  GLN   A NE2 1 
ATOM   724  N  N   . SER   A 1 90  ? 8.749  16.452  9.091  1.00 13.52 ? 96  SER   A N   1 
ATOM   725  C  CA  . SER   A 1 90  ? 8.635  15.658  7.881  1.00 14.06 ? 96  SER   A CA  1 
ATOM   726  C  C   . SER   A 1 90  ? 9.247  14.263  8.081  1.00 13.76 ? 96  SER   A C   1 
ATOM   727  O  O   . SER   A 1 90  ? 10.009 14.034  9.043  1.00 13.44 ? 96  SER   A O   1 
ATOM   728  C  CB  . SER   A 1 90  ? 9.318  16.397  6.734  1.00 17.65 ? 96  SER   A CB  1 
ATOM   729  O  OG  . SER   A 1 90  ? 10.713 16.491  6.983  1.00 20.32 ? 96  SER   A OG  1 
ATOM   730  N  N   . HIS   A 1 91  ? 8.857  13.343  7.188  1.00 13.83 ? 97  HIS   A N   1 
ATOM   731  C  CA  . HIS   A 1 91  ? 9.353  11.973  7.142  1.00 13.24 ? 97  HIS   A CA  1 
ATOM   732  C  C   . HIS   A 1 91  ? 9.108  11.269  8.487  1.00 12.63 ? 97  HIS   A C   1 
ATOM   733  O  O   . HIS   A 1 91  ? 9.918  10.426  8.908  1.00 13.32 ? 97  HIS   A O   1 
ATOM   734  C  CB  . HIS   A 1 91  ? 10.874 11.948  6.758  1.00 14.44 ? 97  HIS   A CB  1 
ATOM   735  C  CG  . HIS   A 1 91  ? 11.152 12.515  5.383  1.00 16.07 ? 97  HIS   A CG  1 
ATOM   736  N  ND1 . HIS   A 1 91  ? 11.280 11.692  4.284  1.00 18.49 ? 97  HIS   A ND1 1 
ATOM   737  C  CD2 . HIS   A 1 91  ? 11.312 13.800  4.984  1.00 18.51 ? 97  HIS   A CD2 1 
ATOM   738  C  CE1 . HIS   A 1 91  ? 11.518 12.496  3.248  1.00 19.32 ? 97  HIS   A CE1 1 
ATOM   739  N  NE2 . HIS   A 1 91  ? 11.533 13.769  3.615  1.00 20.08 ? 97  HIS   A NE2 1 
ATOM   740  N  N   . LEU   A 1 92  ? 7.970  11.547  9.105  1.00 12.02 ? 98  LEU   A N   1 
ATOM   741  C  CA  . LEU   A 1 92  ? 7.625  10.998  10.418 1.00 12.44 ? 98  LEU   A CA  1 
ATOM   742  C  C   . LEU   A 1 92  ? 6.564  9.906   10.234 1.00 12.26 ? 98  LEU   A C   1 
ATOM   743  O  O   . LEU   A 1 92  ? 5.643  10.061  9.435  1.00 12.87 ? 98  LEU   A O   1 
ATOM   744  C  CB  . LEU   A 1 92  ? 7.066  12.134  11.307 1.00 13.61 ? 98  LEU   A CB  1 
ATOM   745  C  CG  . LEU   A 1 92  ? 6.800  11.723  12.781 1.00 15.87 ? 98  LEU   A CG  1 
ATOM   746  C  CD1 . LEU   A 1 92  ? 8.083  11.452  13.509 1.00 15.90 ? 98  LEU   A CD1 1 
ATOM   747  C  CD2 . LEU   A 1 92  ? 6.075  12.856  13.556 1.00 18.42 ? 98  LEU   A CD2 1 
ATOM   748  N  N   . MET   A 1 93  ? 6.702  8.815   10.991 1.00 12.40 ? 99  MET   A N   1 
ATOM   749  C  CA  . MET   A 1 93  ? 5.722  7.707   10.974 1.00 12.23 ? 99  MET   A CA  1 
ATOM   750  C  C   . MET   A 1 93  ? 5.144  7.561   12.372 1.00 12.71 ? 99  MET   A C   1 
ATOM   751  O  O   . MET   A 1 93  ? 5.895  7.581   13.358 1.00 13.60 ? 99  MET   A O   1 
ATOM   752  C  CB  . MET   A 1 93  ? 6.468  6.429   10.601 1.00 13.39 ? 99  MET   A CB  1 
ATOM   753  C  CG  . MET   A 1 93  ? 7.105  6.518   9.216  1.00 14.85 ? 99  MET   A CG  1 
ATOM   754  S  SD  . MET   A 1 93  ? 8.211  5.149   8.748  1.00 16.63 ? 99  MET   A SD  1 
ATOM   755  C  CE  . MET   A 1 93  ? 9.466  5.326   10.062 1.00 21.79 ? 99  MET   A CE  1 
ATOM   756  N  N   . LEU   A 1 94  ? 3.814  7.403   12.508 1.00 12.43 ? 100 LEU   A N   1 
ATOM   757  C  CA  . LEU   A 1 94  ? 3.201  7.258   13.825 1.00 13.67 ? 100 LEU   A CA  1 
ATOM   758  C  C   . LEU   A 1 94  ? 2.701  5.846   14.108 1.00 12.69 ? 100 LEU   A C   1 
ATOM   759  O  O   . LEU   A 1 94  ? 2.274  5.141   13.172 1.00 14.10 ? 100 LEU   A O   1 
ATOM   760  C  CB  . LEU   A 1 94  ? 1.977  8.193   14.045 1.00 15.89 ? 100 LEU   A CB  1 
ATOM   761  C  CG  . LEU   A 1 94  ? 2.221  9.663   14.000 1.00 20.15 ? 100 LEU   A CG  1 
ATOM   762  C  CD1 . LEU   A 1 94  ? 0.926  10.454  14.252 1.00 21.99 ? 100 LEU   A CD1 1 
ATOM   763  C  CD2 . LEU   A 1 94  ? 3.239  10.091  15.061 1.00 21.28 ? 100 LEU   A CD2 1 
ATOM   764  N  N   . ALA   A 1 95  ? 2.760  5.445   15.362 1.00 12.60 ? 101 ALA   A N   1 
ATOM   765  C  CA  . ALA   A 1 95  ? 2.218  4.162   15.828 1.00 12.27 ? 101 ALA   A CA  1 
ATOM   766  C  C   . ALA   A 1 95  ? 1.586  4.363   17.213 1.00 12.00 ? 101 ALA   A C   1 
ATOM   767  O  O   . ALA   A 1 95  ? 1.868  5.369   17.908 1.00 12.62 ? 101 ALA   A O   1 
ATOM   768  C  CB  . ALA   A 1 95  ? 3.354  3.109   15.951 1.00 13.50 ? 101 ALA   A CB  1 
ATOM   769  N  N   . VAL   A 1 96  ? 0.761  3.395   17.646 1.00 11.81 ? 102 VAL   A N   1 
ATOM   770  C  CA  . VAL   A 1 96  ? 0.257  3.379   18.981 1.00 11.86 ? 102 VAL   A CA  1 
ATOM   771  C  C   . VAL   A 1 96  ? 1.288  2.626   19.838 1.00 13.97 ? 102 VAL   A C   1 
ATOM   772  O  O   . VAL   A 1 96  ? 1.620  1.485   19.558 1.00 15.74 ? 102 VAL   A O   1 
ATOM   773  C  CB  . VAL   A 1 96  ? -1.093 2.674   19.007 1.00 11.90 ? 102 VAL   A CB  1 
ATOM   774  C  CG1 . VAL   A 1 96  ? -1.570 2.484   20.441 1.00 13.71 ? 102 VAL   A CG1 1 
ATOM   775  C  CG2 . VAL   A 1 96  ? -2.089 3.485   18.171 1.00 12.34 ? 102 VAL   A CG2 1 
ATOM   776  N  N   . GLY   A 1 97  ? 1.792  3.314   20.847 1.00 13.99 ? 103 GLY   A N   1 
ATOM   777  C  CA  . GLY   A 1 97  ? 2.797  2.724   21.727 1.00 14.91 ? 103 GLY   A CA  1 
ATOM   778  C  C   . GLY   A 1 97  ? 3.246  3.730   22.740 1.00 15.07 ? 103 GLY   A C   1 
ATOM   779  O  O   . GLY   A 1 97  ? 3.006  4.918   22.618 1.00 16.49 ? 103 GLY   A O   1 
ATOM   780  N  N   . HIS   A 1 98  ? 3.849  3.210   23.833 1.00 16.04 ? 104 HIS   A N   1 
ATOM   781  C  CA  . HIS   A 1 98  ? 4.337  4.076   24.865 1.00 17.20 ? 104 HIS   A CA  1 
ATOM   782  C  C   . HIS   A 1 98  ? 5.645  4.798   24.490 1.00 16.45 ? 104 HIS   A C   1 
ATOM   783  O  O   . HIS   A 1 98  ? 6.568  4.173   23.929 1.00 15.68 ? 104 HIS   A O   1 
ATOM   784  C  CB  . HIS   A 1 98  ? 4.549  3.254   26.165 1.00 17.89 ? 104 HIS   A CB  1 
ATOM   785  C  CG  . HIS   A 1 98  ? 4.939  4.129   27.305 1.00 19.02 ? 104 HIS   A CG  1 
ATOM   786  N  ND1 . HIS   A 1 98  ? 4.028  4.984   27.882 1.00 20.04 ? 104 HIS   A ND1 1 
ATOM   787  C  CD2 . HIS   A 1 98  ? 6.141  4.296   27.908 1.00 19.34 ? 104 HIS   A CD2 1 
ATOM   788  C  CE1 . HIS   A 1 98  ? 4.702  5.647   28.824 1.00 19.68 ? 104 HIS   A CE1 1 
ATOM   789  N  NE2 . HIS   A 1 98  ? 5.974  5.244   28.880 1.00 19.50 ? 104 HIS   A NE2 1 
ATOM   790  N  N   . SER   A 1 99  ? 5.757  6.078   24.778 1.00 16.95 ? 105 SER   A N   1 
ATOM   791  C  CA  A SER   A 1 99  ? 6.956  6.830   24.616 0.50 16.78 ? 105 SER   A CA  1 
ATOM   792  C  CA  B SER   A 1 99  ? 6.944  6.905   24.524 0.50 17.19 ? 105 SER   A CA  1 
ATOM   793  C  C   . SER   A 1 99  ? 6.948  8.015   25.586 1.00 19.17 ? 105 SER   A C   1 
ATOM   794  O  O   . SER   A 1 99  ? 5.861  8.535   25.951 1.00 22.26 ? 105 SER   A O   1 
ATOM   795  C  CB  A SER   A 1 99  ? 7.139  7.266   23.170 0.50 15.82 ? 105 SER   A CB  1 
ATOM   796  C  CB  B SER   A 1 99  ? 6.976  7.479   23.081 0.50 17.12 ? 105 SER   A CB  1 
ATOM   797  O  OG  A SER   A 1 99  ? 6.038  8.099   22.862 0.50 14.59 ? 105 SER   A OG  1 
ATOM   798  O  OG  B SER   A 1 99  ? 8.107  8.243   22.630 0.50 17.08 ? 105 SER   A OG  1 
ATOM   799  N  N   . GLU   A 1 100 ? 8.100  8.289   26.122 1.00 15.79 ? 106 GLU   A N   1 
ATOM   800  C  CA  . GLU   A 1 100 ? 8.440  9.400   27.015 1.00 15.42 ? 106 GLU   A CA  1 
ATOM   801  C  C   . GLU   A 1 100 ? 9.599  10.130  26.332 1.00 16.31 ? 106 GLU   A C   1 
ATOM   802  O  O   . GLU   A 1 100 ? 10.263 9.584   25.425 1.00 14.92 ? 106 GLU   A O   1 
ATOM   803  C  CB  . GLU   A 1 100 ? 8.882  8.892   28.398 1.00 16.82 ? 106 GLU   A CB  1 
ATOM   804  C  CG  . GLU   A 1 100 ? 7.698  8.213   29.064 1.00 18.24 ? 106 GLU   A CG  1 
ATOM   805  C  CD  . GLU   A 1 100 ? 7.900  7.631   30.450 1.00 21.94 ? 106 GLU   A CD  1 
ATOM   806  O  OE1 . GLU   A 1 100 ? 8.727  8.162   31.225 1.00 26.36 ? 106 GLU   A OE1 1 
ATOM   807  O  OE2 . GLU   A 1 100 ? 7.219  6.631   30.758 1.00 20.50 ? 106 GLU   A OE2 1 
ATOM   808  N  N   . PRO   A 1 101 ? 9.837  11.404  26.656 1.00 16.59 ? 107 PRO   A N   1 
ATOM   809  C  CA  . PRO   A 1 101 ? 10.877 12.168  25.913 1.00 17.10 ? 107 PRO   A CA  1 
ATOM   810  C  C   . PRO   A 1 101 ? 12.247 11.467  25.796 1.00 16.78 ? 107 PRO   A C   1 
ATOM   811  O  O   . PRO   A 1 101 ? 12.820 11.400  24.695 1.00 17.17 ? 107 PRO   A O   1 
ATOM   812  C  CB  . PRO   A 1 101 ? 10.917 13.505  26.678 1.00 19.00 ? 107 PRO   A CB  1 
ATOM   813  C  CG  . PRO   A 1 101 ? 9.489  13.656  27.141 1.00 20.15 ? 107 PRO   A CG  1 
ATOM   814  C  CD  . PRO   A 1 101 ? 9.088  12.273  27.600 1.00 17.48 ? 107 PRO   A CD  1 
ATOM   815  N  N   . GLY   A 1 102 ? 12.731 10.851  26.881 1.00 15.21 ? 108 GLY   A N   1 
ATOM   816  C  CA  . GLY   A 1 102 ? 13.998 10.122  26.896 1.00 14.01 ? 108 GLY   A CA  1 
ATOM   817  C  C   . GLY   A 1 102 ? 14.006 8.820   26.085 1.00 12.79 ? 108 GLY   A C   1 
ATOM   818  O  O   . GLY   A 1 102 ? 15.061 8.191   25.947 1.00 13.35 ? 108 GLY   A O   1 
ATOM   819  N  N   . ASP   A 1 103 ? 12.852 8.378   25.586 1.00 12.14 ? 109 ASP   A N   1 
ATOM   820  C  CA  . ASP   A 1 103 ? 12.804 7.230   24.671 1.00 11.74 ? 109 ASP   A CA  1 
ATOM   821  C  C   . ASP   A 1 103 ? 13.333 7.575   23.279 1.00 11.40 ? 109 ASP   A C   1 
ATOM   822  O  O   . ASP   A 1 103 ? 13.602 6.649   22.474 1.00 11.20 ? 109 ASP   A O   1 
ATOM   823  C  CB  . ASP   A 1 103 ? 11.380 6.650   24.545 1.00 11.39 ? 109 ASP   A CB  1 
ATOM   824  C  CG  . ASP   A 1 103 ? 10.985 5.926   25.812 1.00 12.21 ? 109 ASP   A CG  1 
ATOM   825  O  OD1 . ASP   A 1 103 ? 11.848 5.271   26.396 1.00 12.72 ? 109 ASP   A OD1 1 
ATOM   826  O  OD2 . ASP   A 1 103 ? 9.797  6.034   26.221 1.00 12.43 ? 109 ASP   A OD2 1 
ATOM   827  N  N   . CYS   A 1 104 ? 13.520 8.884   22.957 1.00 11.48 ? 110 CYS   A N   1 
ATOM   828  C  CA  . CYS   A 1 104 ? 14.079 9.242   21.641 1.00 11.58 ? 110 CYS   A CA  1 
ATOM   829  C  C   . CYS   A 1 104 ? 15.412 8.546   21.392 1.00 11.16 ? 110 CYS   A C   1 
ATOM   830  O  O   . CYS   A 1 104 ? 16.248 8.445   22.293 1.00 12.34 ? 110 CYS   A O   1 
ATOM   831  C  CB  . CYS   A 1 104 ? 14.237 10.751  21.532 1.00 12.77 ? 110 CYS   A CB  1 
ATOM   832  S  SG  . CYS   A 1 104 ? 12.665 11.622  21.266 1.00 13.76 ? 110 CYS   A SG  1 
ATOM   833  N  N   . GLY   A 1 105 ? 15.575 7.993   20.194 1.00 10.29 ? 111 GLY   A N   1 
ATOM   834  C  CA  . GLY   A 1 105 ? 16.793 7.288   19.850 1.00 10.84 ? 111 GLY   A CA  1 
ATOM   835  C  C   . GLY   A 1 105 ? 16.617 5.782   19.779 1.00 10.59 ? 111 GLY   A C   1 
ATOM   836  O  O   . GLY   A 1 105 ? 17.477 5.081   19.223 1.00 11.66 ? 111 GLY   A O   1 
ATOM   837  N  N   . GLY   A 1 106 ? 15.544 5.261   20.379 1.00 10.24 ? 112 GLY   A N   1 
ATOM   838  C  CA  . GLY   A 1 106 ? 15.282 3.830   20.287 1.00 10.00 ? 112 GLY   A CA  1 
ATOM   839  C  C   . GLY   A 1 106 ? 15.042 3.402   18.849 1.00 9.23  ? 112 GLY   A C   1 
ATOM   840  O  O   . GLY   A 1 106 ? 14.382 4.123   18.086 1.00 9.96  ? 112 GLY   A O   1 
ATOM   841  N  N   . ILE   A 1 107 ? 15.562 2.245   18.457 1.00 9.51  ? 113 ILE   A N   1 
ATOM   842  C  CA  . ILE   A 1 107 ? 15.425 1.813   17.054 1.00 8.94  ? 113 ILE   A CA  1 
ATOM   843  C  C   . ILE   A 1 107 ? 14.089 1.173   16.770 1.00 8.36  ? 113 ILE   A C   1 
ATOM   844  O  O   . ILE   A 1 107 ? 13.627 0.337   17.550 1.00 9.29  ? 113 ILE   A O   1 
ATOM   845  C  CB  . ILE   A 1 107 ? 16.586 0.847   16.710 1.00 9.76  ? 113 ILE   A CB  1 
ATOM   846  C  CG1 . ILE   A 1 107 ? 17.870 1.697   16.465 1.00 11.30 ? 113 ILE   A CG1 1 
ATOM   847  C  CG2 . ILE   A 1 107 ? 16.322 -0.036  15.489 1.00 10.52 ? 113 ILE   A CG2 1 
ATOM   848  C  CD1 . ILE   A 1 107 ? 19.147 0.849   16.335 1.00 14.50 ? 113 ILE   A CD1 1 
ATOM   849  N  N   . LEU   A 1 108 ? 13.512 1.511   15.592 1.00 8.74  ? 114 LEU   A N   1 
ATOM   850  C  CA  . LEU   A 1 108 ? 12.402 0.782   14.974 1.00 8.90  ? 114 LEU   A CA  1 
ATOM   851  C  C   . LEU   A 1 108 ? 13.041 -0.073  13.865 1.00 9.56  ? 114 LEU   A C   1 
ATOM   852  O  O   . LEU   A 1 108 ? 13.822 0.459   13.041 1.00 9.80  ? 114 LEU   A O   1 
ATOM   853  C  CB  . LEU   A 1 108 ? 11.409 1.785   14.349 1.00 9.35  ? 114 LEU   A CB  1 
ATOM   854  C  CG  . LEU   A 1 108 ? 10.318 1.151   13.448 1.00 10.53 ? 114 LEU   A CG  1 
ATOM   855  C  CD1 . LEU   A 1 108 ? 9.335  0.342   14.312 1.00 11.94 ? 114 LEU   A CD1 1 
ATOM   856  C  CD2 . LEU   A 1 108 ? 9.535  2.267   12.710 1.00 11.79 ? 114 LEU   A CD2 1 
ATOM   857  N  N   . ARG   A 1 109 ? 12.704 -1.343  13.813 1.00 9.40  ? 115 ARG   A N   1 
ATOM   858  C  CA  . ARG   A 1 109 ? 13.284 -2.237  12.784 1.00 9.67  ? 115 ARG   A CA  1 
ATOM   859  C  C   . ARG   A 1 109 ? 12.235 -3.188  12.254 1.00 10.42 ? 115 ARG   A C   1 
ATOM   860  O  O   . ARG   A 1 109 ? 11.202 -3.468  12.888 1.00 10.44 ? 115 ARG   A O   1 
ATOM   861  C  CB  . ARG   A 1 109 ? 14.481 -3.044  13.402 1.00 11.05 ? 115 ARG   A CB  1 
ATOM   862  C  CG  . ARG   A 1 109 ? 14.005 -4.030  14.490 1.00 11.81 ? 115 ARG   A CG  1 
ATOM   863  C  CD  . ARG   A 1 109 ? 15.231 -4.772  15.049 1.00 13.34 ? 115 ARG   A CD  1 
ATOM   864  N  NE  . ARG   A 1 109 ? 16.039 -3.913  15.904 1.00 13.95 ? 115 ARG   A NE  1 
ATOM   865  C  CZ  . ARG   A 1 109 ? 17.334 -3.685  15.748 1.00 14.07 ? 115 ARG   A CZ  1 
ATOM   866  N  NH1 . ARG   A 1 109 ? 17.972 -4.129  14.667 1.00 14.89 ? 115 ARG   A NH1 1 
ATOM   867  N  NH2 . ARG   A 1 109 ? 17.996 -2.946  16.634 1.00 14.87 ? 115 ARG   A NH2 1 
ATOM   868  N  N   . CYS   A 1 110 ? 12.550 -3.761  11.084 1.00 12.66 ? 116 CYS   A N   1 
ATOM   869  C  CA  . CYS   A 1 110 ? 11.729 -4.814  10.456 1.00 15.49 ? 116 CYS   A CA  1 
ATOM   870  C  C   . CYS   A 1 110 ? 12.711 -5.977  10.091 1.00 18.68 ? 116 CYS   A C   1 
ATOM   871  O  O   . CYS   A 1 110 ? 13.886 -5.944  10.454 1.00 18.45 ? 116 CYS   A O   1 
ATOM   872  C  CB  . CYS   A 1 110 ? 11.029 -4.235  9.241  1.00 15.29 ? 116 CYS   A CB  1 
ATOM   873  S  SG  . CYS   A 1 110 ? 12.172 -3.779  7.889  1.00 15.83 ? 116 CYS   A SG  1 
ATOM   874  N  N   . GLN   A 1 111 ? 12.212 -7.049  9.379  1.00 21.97 ? 117 GLN   A N   1 
ATOM   875  C  CA  . GLN   A 1 111 ? 13.115 -8.139  8.973  1.00 24.40 ? 117 GLN   A CA  1 
ATOM   876  C  C   . GLN   A 1 111 ? 14.253 -7.684  8.056  1.00 24.14 ? 117 GLN   A C   1 
ATOM   877  O  O   . GLN   A 1 111 ? 15.274 -8.371  7.973  1.00 26.81 ? 117 GLN   A O   1 
ATOM   878  C  CB  . GLN   A 1 111 ? 12.375 -9.286  8.245  1.00 26.86 ? 117 GLN   A CB  1 
ATOM   879  C  CG  . GLN   A 1 111 ? 11.728 -8.847  6.941  1.00 31.91 ? 117 GLN   A CG  1 
ATOM   880  C  CD  . GLN   A 1 111 ? 10.264 -8.623  7.151  1.00 37.34 ? 117 GLN   A CD  1 
ATOM   881  O  OE1 . GLN   A 1 111 ? 9.822  -8.142  8.212  1.00 38.48 ? 117 GLN   A OE1 1 
ATOM   882  N  NE2 . GLN   A 1 111 ? 9.477  -8.980  6.143  1.00 37.90 ? 117 GLN   A NE2 1 
ATOM   883  N  N   . HIS   A 1 112 ? 14.106 -6.516  7.389  1.00 20.78 ? 118 HIS   A N   1 
ATOM   884  C  CA  . HIS   A 1 112 ? 15.133 -6.007  6.458  1.00 19.15 ? 118 HIS   A CA  1 
ATOM   885  C  C   . HIS   A 1 112 ? 16.242 -5.194  7.118  1.00 18.86 ? 118 HIS   A C   1 
ATOM   886  O  O   . HIS   A 1 112 ? 17.286 -4.923  6.515  1.00 21.14 ? 118 HIS   A O   1 
ATOM   887  C  CB  . HIS   A 1 112 ? 14.486 -5.209  5.323  1.00 18.96 ? 118 HIS   A CB  1 
ATOM   888  C  CG  . HIS   A 1 112 ? 13.398 -5.987  4.632  1.00 20.30 ? 118 HIS   A CG  1 
ATOM   889  N  ND1 . HIS   A 1 112 ? 12.067 -5.712  4.849  1.00 22.53 ? 118 HIS   A ND1 1 
ATOM   890  C  CD2 . HIS   A 1 112 ? 13.484 -7.031  3.763  1.00 22.62 ? 118 HIS   A CD2 1 
ATOM   891  C  CE1 . HIS   A 1 112 ? 11.382 -6.597  4.132  1.00 24.51 ? 118 HIS   A CE1 1 
ATOM   892  N  NE2 . HIS   A 1 112 ? 12.200 -7.385  3.440  1.00 24.40 ? 118 HIS   A NE2 1 
ATOM   893  N  N   . GLY   A 1 113 ? 15.991 -4.734  8.358  1.00 16.81 ? 119 GLY   A N   1 
ATOM   894  C  CA  . GLY   A 1 113 ? 16.967 -3.932  9.058  1.00 15.67 ? 119 GLY   A CA  1 
ATOM   895  C  C   . GLY   A 1 113 ? 16.329 -2.764  9.798  1.00 12.79 ? 119 GLY   A C   1 
ATOM   896  O  O   . GLY   A 1 113 ? 15.139 -2.766  10.113 1.00 12.81 ? 119 GLY   A O   1 
ATOM   897  N  N   . VAL   A 1 114 ? 17.146 -1.738  10.037 1.00 11.74 ? 120 VAL   A N   1 
ATOM   898  C  CA  . VAL   A 1 114 ? 16.701 -0.541  10.770 1.00 11.58 ? 120 VAL   A CA  1 
ATOM   899  C  C   . VAL   A 1 114 ? 15.855 0.374   9.896  1.00 10.45 ? 120 VAL   A C   1 
ATOM   900  O  O   . VAL   A 1 114 ? 16.249 0.721   8.781  1.00 11.06 ? 120 VAL   A O   1 
ATOM   901  C  CB  . VAL   A 1 114 ? 17.920 0.231   11.345 1.00 11.79 ? 120 VAL   A CB  1 
ATOM   902  C  CG1 . VAL   A 1 114 ? 17.471 1.542   12.014 1.00 12.91 ? 120 VAL   A CG1 1 
ATOM   903  C  CG2 . VAL   A 1 114 ? 18.680 -0.653  12.344 1.00 13.42 ? 120 VAL   A CG2 1 
ATOM   904  N  N   . VAL   A 1 115 ? 14.686 0.765   10.392 1.00 9.92  ? 121 VAL   A N   1 
ATOM   905  C  CA  . VAL   A 1 115 ? 13.729 1.588   9.668  1.00 10.61 ? 121 VAL   A CA  1 
ATOM   906  C  C   . VAL   A 1 115 ? 13.836 3.054   10.095 1.00 10.37 ? 121 VAL   A C   1 
ATOM   907  O  O   . VAL   A 1 115 ? 13.698 3.962   9.285  1.00 11.18 ? 121 VAL   A O   1 
ATOM   908  C  CB  . VAL   A 1 115 ? 12.282 1.067   9.954  1.00 11.95 ? 121 VAL   A CB  1 
ATOM   909  C  CG1 . VAL   A 1 115 ? 11.206 2.017   9.372  1.00 14.15 ? 121 VAL   A CG1 1 
ATOM   910  C  CG2 . VAL   A 1 115 ? 12.090 -0.352  9.429  1.00 13.13 ? 121 VAL   A CG2 1 
ATOM   911  N  N   . GLY   A 1 116 ? 14.045 3.307   11.390 1.00 10.22 ? 122 GLY   A N   1 
ATOM   912  C  CA  . GLY   A 1 116 ? 14.152 4.677   11.909 1.00 10.66 ? 122 GLY   A CA  1 
ATOM   913  C  C   . GLY   A 1 116 ? 14.375 4.700   13.399 1.00 9.74  ? 122 GLY   A C   1 
ATOM   914  O  O   . GLY   A 1 116 ? 14.690 3.641   13.983 1.00 9.88  ? 122 GLY   A O   1 
ATOM   915  N  N   . ILE   A 1 117 ? 14.236 5.882   14.018 1.00 9.05  ? 123 ILE   A N   1 
ATOM   916  C  CA  . ILE   A 1 117 ? 14.449 6.019   15.469 1.00 9.36  ? 123 ILE   A CA  1 
ATOM   917  C  C   . ILE   A 1 117 ? 13.310 6.787   16.080 1.00 9.51  ? 123 ILE   A C   1 
ATOM   918  O  O   . ILE   A 1 117 ? 12.701 7.654   15.429 1.00 10.76 ? 123 ILE   A O   1 
ATOM   919  C  CB  . ILE   A 1 117 ? 15.798 6.717   15.832 1.00 10.70 ? 123 ILE   A CB  1 
ATOM   920  C  CG1 . ILE   A 1 117 ? 15.952 8.039   15.094 1.00 12.19 ? 123 ILE   A CG1 1 
ATOM   921  C  CG2 . ILE   A 1 117 ? 16.954 5.771   15.626 1.00 12.45 ? 123 ILE   A CG2 1 
ATOM   922  C  CD1 . ILE   A 1 117 ? 17.215 8.847   15.607 1.00 13.62 ? 123 ILE   A CD1 1 
ATOM   923  N  N   . VAL   A 1 118 ? 13.010 6.511   17.351 1.00 9.36  ? 124 VAL   A N   1 
ATOM   924  C  CA  . VAL   A 1 118 ? 11.953 7.249   18.065 1.00 8.97  ? 124 VAL   A CA  1 
ATOM   925  C  C   . VAL   A 1 118 ? 12.311 8.735   18.080 1.00 10.03 ? 124 VAL   A C   1 
ATOM   926  O  O   . VAL   A 1 118 ? 13.480 9.085   18.369 1.00 10.06 ? 124 VAL   A O   1 
ATOM   927  C  CB  . VAL   A 1 118 ? 11.835 6.761   19.527 1.00 9.50  ? 124 VAL   A CB  1 
ATOM   928  C  CG1 . VAL   A 1 118 ? 10.851 7.615   20.334 1.00 11.70 ? 124 VAL   A CG1 1 
ATOM   929  C  CG2 . VAL   A 1 118 ? 11.398 5.297   19.603 1.00 9.79  ? 124 VAL   A CG2 1 
ATOM   930  N  N   . SER   A 1 119 ? 11.337 9.604   17.744 1.00 9.99  ? 125 SER   A N   1 
ATOM   931  C  CA  . SER   A 1 119 ? 11.532 11.053  17.680 1.00 10.59 ? 125 SER   A CA  1 
ATOM   932  C  C   . SER   A 1 119 ? 10.430 11.826  18.370 1.00 12.58 ? 125 SER   A C   1 
ATOM   933  O  O   . SER   A 1 119 ? 10.713 12.947  18.821 1.00 14.70 ? 125 SER   A O   1 
ATOM   934  C  CB  . SER   A 1 119 ? 11.659 11.483  16.226 1.00 11.92 ? 125 SER   A CB  1 
ATOM   935  O  OG  . SER   A 1 119 ? 11.776 12.888  16.050 1.00 13.14 ? 125 SER   A OG  1 
ATOM   936  N  N   . THR   A 1 120 ? 9.176  11.301  18.447 1.00 12.17 ? 126 THR   A N   1 
ATOM   937  C  CA  . THR   A 1 120 ? 8.091  12.083  19.078 1.00 13.63 ? 126 THR   A CA  1 
ATOM   938  C  C   . THR   A 1 120 ? 7.257  11.142  19.973 1.00 15.69 ? 126 THR   A C   1 
ATOM   939  O  O   . THR   A 1 120 ? 7.412  9.899   19.904 1.00 13.97 ? 126 THR   A O   1 
ATOM   940  C  CB  . THR   A 1 120 ? 7.197  12.756  17.996 1.00 15.40 ? 126 THR   A CB  1 
ATOM   941  O  OG1 . THR   A 1 120 ? 6.369  11.766  17.363 1.00 16.55 ? 126 THR   A OG1 1 
ATOM   942  C  CG2 . THR   A 1 120 ? 7.976  13.564  16.995 1.00 15.50 ? 126 THR   A CG2 1 
ATOM   943  N  N   . GLY   A 1 121 ? 6.337  11.714  20.757 1.00 18.03 ? 127 GLY   A N   1 
ATOM   944  C  CA  . GLY   A 1 121 ? 5.458  10.887  21.558 1.00 20.48 ? 127 GLY   A CA  1 
ATOM   945  C  C   . GLY   A 1 121 ? 4.443  11.654  22.360 1.00 21.26 ? 127 GLY   A C   1 
ATOM   946  O  O   . GLY   A 1 121 ? 4.395  12.878  22.299 1.00 22.38 ? 127 GLY   A O   1 
ATOM   947  N  N   . GLY   A 1 122 ? 3.677  10.876  23.122 1.00 21.39 ? 128 GLY   A N   1 
ATOM   948  C  CA  . GLY   A 1 122 ? 2.649  11.376  24.030 1.00 20.93 ? 128 GLY   A CA  1 
ATOM   949  C  C   . GLY   A 1 122 ? 1.325  10.675  23.807 1.00 22.05 ? 128 GLY   A C   1 
ATOM   950  O  O   . GLY   A 1 122 ? 1.000  10.285  22.669 1.00 22.05 ? 128 GLY   A O   1 
ATOM   951  N  N   . ASN   A 1 123 ? 0.552  10.512  24.906 1.00 21.67 ? 129 ASN   A N   1 
ATOM   952  C  CA  . ASN   A 1 123 ? -0.805 9.975   24.891 1.00 22.83 ? 129 ASN   A CA  1 
ATOM   953  C  C   . ASN   A 1 123 ? -0.991 8.678   24.154 1.00 21.62 ? 129 ASN   A C   1 
ATOM   954  O  O   . ASN   A 1 123 ? -2.060 8.444   23.557 1.00 21.87 ? 129 ASN   A O   1 
ATOM   955  C  CB  . ASN   A 1 123 ? -1.715 11.042  24.325 1.00 25.01 ? 129 ASN   A CB  1 
ATOM   956  C  CG  . ASN   A 1 123 ? -1.773 12.249  25.222 1.00 29.15 ? 129 ASN   A CG  1 
ATOM   957  O  OD1 . ASN   A 1 123 ? -2.039 12.126  26.429 1.00 31.49 ? 129 ASN   A OD1 1 
ATOM   958  N  ND2 . ASN   A 1 123 ? -1.532 13.424  24.634 1.00 29.96 ? 129 ASN   A ND2 1 
ATOM   959  N  N   . GLY   A 1 124 ? -0.070 7.755   24.373 1.00 18.69 ? 130 GLY   A N   1 
ATOM   960  C  CA  . GLY   A 1 124 ? -0.169 6.443   23.791 1.00 17.48 ? 130 GLY   A CA  1 
ATOM   961  C  C   . GLY   A 1 124 ? 0.212  6.423   22.333 1.00 14.38 ? 130 GLY   A C   1 
ATOM   962  O  O   . GLY   A 1 124 ? 0.051  5.374   21.735 1.00 16.42 ? 130 GLY   A O   1 
ATOM   963  N  N   . LEU   A 1 125 ? 0.860  7.516   21.809 1.00 14.09 ? 131 LEU   A N   1 
ATOM   964  C  CA  . LEU   A 1 125 ? 1.412  7.478   20.447 1.00 14.03 ? 131 LEU   A CA  1 
ATOM   965  C  C   . LEU   A 1 125 ? 2.949  7.550   20.505 1.00 14.77 ? 131 LEU   A C   1 
ATOM   966  O  O   . LEU   A 1 125 ? 3.529  8.139   21.459 1.00 16.69 ? 131 LEU   A O   1 
ATOM   967  C  CB  . LEU   A 1 125 ? 0.915  8.642   19.592 1.00 14.74 ? 131 LEU   A CB  1 
ATOM   968  C  CG  . LEU   A 1 125 ? -0.599 8.650   19.381 1.00 15.52 ? 131 LEU   A CG  1 
ATOM   969  C  CD1 . LEU   A 1 125 ? -1.082 10.015  18.912 1.00 17.85 ? 131 LEU   A CD1 1 
ATOM   970  C  CD2 . LEU   A 1 125 ? -1.008 7.537   18.387 1.00 16.62 ? 131 LEU   A CD2 1 
ATOM   971  N  N   . VAL   A 1 126 ? 3.598  6.976   19.507 1.00 11.77 ? 132 VAL   A N   1 
ATOM   972  C  CA  . VAL   A 1 126 ? 5.048  7.091   19.370 1.00 11.95 ? 132 VAL   A CA  1 
ATOM   973  C  C   . VAL   A 1 126 ? 5.297  7.459   17.887 1.00 11.44 ? 132 VAL   A C   1 
ATOM   974  O  O   . VAL   A 1 126 ? 4.675  6.865   16.993 1.00 12.54 ? 132 VAL   A O   1 
ATOM   975  C  CB  . VAL   A 1 126 ? 5.769  5.797   19.826 1.00 11.69 ? 132 VAL   A CB  1 
ATOM   976  C  CG1 . VAL   A 1 126 ? 5.227  4.568   19.108 1.00 12.34 ? 132 VAL   A CG1 1 
ATOM   977  C  CG2 . VAL   A 1 126 ? 7.293  5.928   19.637 1.00 12.11 ? 132 VAL   A CG2 1 
ATOM   978  N  N   . GLY   A 1 127 ? 6.214  8.393   17.625 1.00 11.20 ? 133 GLY   A N   1 
ATOM   979  C  CA  . GLY   A 1 127 ? 6.549  8.792   16.262 1.00 11.34 ? 133 GLY   A CA  1 
ATOM   980  C  C   . GLY   A 1 127 ? 7.995  8.460   15.988 1.00 11.81 ? 133 GLY   A C   1 
ATOM   981  O  O   . GLY   A 1 127 ? 8.853  8.619   16.876 1.00 12.56 ? 133 GLY   A O   1 
ATOM   982  N  N   . PHE   A 1 128 ? 8.257  7.981   14.780 1.00 9.89  ? 134 PHE   A N   1 
ATOM   983  C  CA  . PHE   A 1 128 ? 9.613  7.575   14.364 1.00 10.43 ? 134 PHE   A CA  1 
ATOM   984  C  C   . PHE   A 1 128 ? 10.071 8.388   13.177 1.00 11.01 ? 134 PHE   A C   1 
ATOM   985  O  O   . PHE   A 1 128 ? 9.330  8.532   12.179 1.00 11.67 ? 134 PHE   A O   1 
ATOM   986  C  CB  . PHE   A 1 128 ? 9.586  6.082   13.923 1.00 10.94 ? 134 PHE   A CB  1 
ATOM   987  C  CG  . PHE   A 1 128 ? 8.971  5.149   14.951 1.00 10.70 ? 134 PHE   A CG  1 
ATOM   988  C  CD1 . PHE   A 1 128 ? 9.712  4.684   16.035 1.00 10.23 ? 134 PHE   A CD1 1 
ATOM   989  C  CD2 . PHE   A 1 128 ? 7.641  4.756   14.848 1.00 11.80 ? 134 PHE   A CD2 1 
ATOM   990  C  CE1 . PHE   A 1 128 ? 9.148  3.811   16.960 1.00 10.13 ? 134 PHE   A CE1 1 
ATOM   991  C  CE2 . PHE   A 1 128 ? 7.092  3.873   15.765 1.00 11.70 ? 134 PHE   A CE2 1 
ATOM   992  C  CZ  . PHE   A 1 128 ? 7.841  3.423   16.838 1.00 11.00 ? 134 PHE   A CZ  1 
ATOM   993  N  N   . ALA   A 1 129 ? 11.335 8.843   13.248 1.00 10.15 ? 135 ALA   A N   1 
ATOM   994  C  CA  . ALA   A 1 129 ? 11.963 9.508   12.093 1.00 10.52 ? 135 ALA   A CA  1 
ATOM   995  C  C   . ALA   A 1 129 ? 12.453 8.427   11.136 1.00 10.73 ? 135 ALA   A C   1 
ATOM   996  O  O   . ALA   A 1 129 ? 13.340 7.638   11.501 1.00 11.26 ? 135 ALA   A O   1 
ATOM   997  C  CB  . ALA   A 1 129 ? 13.111 10.380  12.582 1.00 11.17 ? 135 ALA   A CB  1 
ATOM   998  N  N   . ASP   A 1 130 ? 11.910 8.380   9.906  1.00 10.90 ? 136 ASP   A N   1 
ATOM   999  C  CA  . ASP   A 1 130 ? 12.325 7.392   8.922  1.00 11.50 ? 136 ASP   A CA  1 
ATOM   1000 C  C   . ASP   A 1 130 ? 13.735 7.686   8.450  1.00 11.24 ? 136 ASP   A C   1 
ATOM   1001 O  O   . ASP   A 1 130 ? 14.118 8.856   8.263  1.00 12.76 ? 136 ASP   A O   1 
ATOM   1002 C  CB  . ASP   A 1 130 ? 11.377 7.465   7.694  1.00 13.19 ? 136 ASP   A CB  1 
ATOM   1003 C  CG  . ASP   A 1 130 ? 11.641 6.435   6.629  1.00 19.97 ? 136 ASP   A CG  1 
ATOM   1004 O  OD1 . ASP   A 1 130 ? 11.762 5.254   6.973  1.00 17.67 ? 136 ASP   A OD1 1 
ATOM   1005 O  OD2 . ASP   A 1 130 ? 11.793 6.840   5.432  1.00 27.01 ? 136 ASP   A OD2 1 
ATOM   1006 N  N   . VAL   A 1 131 ? 14.500 6.609   8.140  1.00 10.25 ? 137 VAL   A N   1 
ATOM   1007 C  CA  . VAL   A 1 131 ? 15.823 6.761   7.518  1.00 10.51 ? 137 VAL   A CA  1 
ATOM   1008 C  C   . VAL   A 1 131 ? 15.941 5.939   6.220  1.00 10.93 ? 137 VAL   A C   1 
ATOM   1009 O  O   . VAL   A 1 131 ? 17.021 5.945   5.607  1.00 11.10 ? 137 VAL   A O   1 
ATOM   1010 C  CB  . VAL   A 1 131 ? 16.993 6.403   8.475  1.00 10.59 ? 137 VAL   A CB  1 
ATOM   1011 C  CG1 . VAL   A 1 131 ? 17.011 7.314   9.706  1.00 11.16 ? 137 VAL   A CG1 1 
ATOM   1012 C  CG2 . VAL   A 1 131 ? 16.985 4.930   8.883  1.00 11.66 ? 137 VAL   A CG2 1 
ATOM   1013 N  N   . ARG   A 1 132 ? 14.876 5.242   5.795  1.00 11.16 ? 138 ARG   A N   1 
ATOM   1014 C  CA  . ARG   A 1 132 ? 14.963 4.321   4.656  1.00 11.26 ? 138 ARG   A CA  1 
ATOM   1015 C  C   . ARG   A 1 132 ? 15.238 5.012   3.337  1.00 12.75 ? 138 ARG   A C   1 
ATOM   1016 O  O   . ARG   A 1 132 ? 15.687 4.348   2.380  1.00 13.72 ? 138 ARG   A O   1 
ATOM   1017 C  CB  . ARG   A 1 132 ? 13.712 3.443   4.560  1.00 11.77 ? 138 ARG   A CB  1 
ATOM   1018 C  CG  . ARG   A 1 132 ? 13.578 2.493   5.764  1.00 11.95 ? 138 ARG   A CG  1 
ATOM   1019 C  CD  . ARG   A 1 132 ? 12.293 1.708   5.616  1.00 12.78 ? 138 ARG   A CD  1 
ATOM   1020 N  NE  . ARG   A 1 132 ? 11.146 2.597   5.851  1.00 13.60 ? 138 ARG   A NE  1 
ATOM   1021 C  CZ  . ARG   A 1 132 ? 9.883  2.193   5.951  1.00 16.04 ? 138 ARG   A CZ  1 
ATOM   1022 N  NH1 . ARG   A 1 132 ? 9.564  0.923   5.697  1.00 16.55 ? 138 ARG   A NH1 1 
ATOM   1023 N  NH2 . ARG   A 1 132 ? 8.923  3.077   6.232  1.00 17.15 ? 138 ARG   A NH2 1 
ATOM   1024 N  N   . ASP   A 1 133 ? 14.937 6.329   3.221  1.00 12.60 ? 139 ASP   A N   1 
ATOM   1025 C  CA  . ASP   A 1 133 ? 15.209 7.040   1.966  1.00 13.23 ? 139 ASP   A CA  1 
ATOM   1026 C  C   . ASP   A 1 133 ? 16.651 7.555   1.876  1.00 13.42 ? 139 ASP   A C   1 
ATOM   1027 O  O   . ASP   A 1 133 ? 17.044 8.072   0.825  1.00 15.27 ? 139 ASP   A O   1 
ATOM   1028 C  CB  . ASP   A 1 133 ? 14.201 8.213   1.830  1.00 15.02 ? 139 ASP   A CB  1 
ATOM   1029 C  CG  . ASP   A 1 133 ? 14.404 9.269   2.916  1.00 17.35 ? 139 ASP   A CG  1 
ATOM   1030 O  OD1 . ASP   A 1 133 ? 14.507 8.896   4.112  1.00 16.96 ? 139 ASP   A OD1 1 
ATOM   1031 O  OD2 . ASP   A 1 133 ? 14.436 10.472  2.583  1.00 20.18 ? 139 ASP   A OD2 1 
ATOM   1032 N  N   . LEU   A 1 134 ? 17.437 7.481   2.984  1.00 12.00 ? 140 LEU   A N   1 
ATOM   1033 C  CA  . LEU   A 1 134 ? 18.797 8.034   3.026  1.00 11.83 ? 140 LEU   A CA  1 
ATOM   1034 C  C   . LEU   A 1 134 ? 19.767 7.007   2.490  1.00 12.53 ? 140 LEU   A C   1 
ATOM   1035 O  O   . LEU   A 1 134 ? 20.457 6.309   3.234  1.00 13.27 ? 140 LEU   A O   1 
ATOM   1036 C  CB  . LEU   A 1 134 ? 19.148 8.454   4.466  1.00 12.59 ? 140 LEU   A CB  1 
ATOM   1037 C  CG  . LEU   A 1 134 ? 18.177 9.474   5.107  1.00 13.32 ? 140 LEU   A CG  1 
ATOM   1038 C  CD1 . LEU   A 1 134 ? 18.563 9.726   6.570  1.00 13.36 ? 140 LEU   A CD1 1 
ATOM   1039 C  CD2 . LEU   A 1 134 ? 18.176 10.792  4.347  1.00 15.51 ? 140 LEU   A CD2 1 
ATOM   1040 N  N   . LEU   A 1 135 ? 19.756 6.844   1.158  1.00 12.10 ? 141 LEU   A N   1 
ATOM   1041 C  CA  . LEU   A 1 135 ? 20.522 5.765   0.526  1.00 12.66 ? 141 LEU   A CA  1 
ATOM   1042 C  C   . LEU   A 1 135 ? 22.002 5.891   0.723  1.00 13.03 ? 141 LEU   A C   1 
ATOM   1043 O  O   . LEU   A 1 135 ? 22.712 4.863   0.754  1.00 14.71 ? 141 LEU   A O   1 
ATOM   1044 C  CB  . LEU   A 1 135 ? 20.164 5.626   -0.995 1.00 13.63 ? 141 LEU   A CB  1 
ATOM   1045 C  CG  . LEU   A 1 135 ? 18.650 5.603   -1.292 1.00 16.37 ? 141 LEU   A CG  1 
ATOM   1046 C  CD1 . LEU   A 1 135 ? 18.386 5.307   -2.761 1.00 17.85 ? 141 LEU   A CD1 1 
ATOM   1047 C  CD2 . LEU   A 1 135 ? 17.877 4.592   -0.460 1.00 17.31 ? 141 LEU   A CD2 1 
ATOM   1048 N  N   . TRP   A 1 136 ? 22.487 7.128   0.881  1.00 12.59 ? 142 TRP   A N   1 
ATOM   1049 C  CA  . TRP   A 1 136 ? 23.915 7.376   1.043  1.00 13.18 ? 142 TRP   A CA  1 
ATOM   1050 C  C   . TRP   A 1 136 ? 24.470 6.786   2.335  1.00 14.05 ? 142 TRP   A C   1 
ATOM   1051 O  O   . TRP   A 1 136 ? 25.695 6.646   2.449  1.00 15.29 ? 142 TRP   A O   1 
ATOM   1052 C  CB  . TRP   A 1 136 ? 24.212 8.883   0.924  1.00 13.88 ? 142 TRP   A CB  1 
ATOM   1053 C  CG  . TRP   A 1 136 ? 23.393 9.724   1.857  1.00 13.27 ? 142 TRP   A CG  1 
ATOM   1054 C  CD1 . TRP   A 1 136 ? 22.234 10.380  1.566  1.00 14.15 ? 142 TRP   A CD1 1 
ATOM   1055 C  CD2 . TRP   A 1 136 ? 23.725 10.065  3.213  1.00 13.48 ? 142 TRP   A CD2 1 
ATOM   1056 N  NE1 . TRP   A 1 136 ? 21.791 11.071  2.680  1.00 15.32 ? 142 TRP   A NE1 1 
ATOM   1057 C  CE2 . TRP   A 1 136 ? 22.692 10.889  3.703  1.00 14.36 ? 142 TRP   A CE2 1 
ATOM   1058 C  CE3 . TRP   A 1 136 ? 24.789 9.728   4.065  1.00 14.54 ? 142 TRP   A CE3 1 
ATOM   1059 C  CZ2 . TRP   A 1 136 ? 22.711 11.404  5.005  1.00 15.65 ? 142 TRP   A CZ2 1 
ATOM   1060 C  CZ3 . TRP   A 1 136 ? 24.823 10.266  5.341  1.00 15.86 ? 142 TRP   A CZ3 1 
ATOM   1061 C  CH2 . TRP   A 1 136 ? 23.786 11.080  5.798  1.00 15.41 ? 142 TRP   A CH2 1 
ATOM   1062 N  N   . LEU   A 1 137 ? 23.609 6.420   3.313  1.00 12.46 ? 143 LEU   A N   1 
ATOM   1063 C  CA  . LEU   A 1 137 ? 24.123 5.775   4.538  1.00 14.21 ? 143 LEU   A CA  1 
ATOM   1064 C  C   . LEU   A 1 137 ? 24.832 4.453   4.216  1.00 16.26 ? 143 LEU   A C   1 
ATOM   1065 O  O   . LEU   A 1 137 ? 25.632 3.977   5.041  1.00 17.09 ? 143 LEU   A O   1 
ATOM   1066 C  CB  . LEU   A 1 137 ? 22.991 5.521   5.532  1.00 13.57 ? 143 LEU   A CB  1 
ATOM   1067 C  CG  . LEU   A 1 137 ? 22.417 6.751   6.211  1.00 13.29 ? 143 LEU   A CG  1 
ATOM   1068 C  CD1 . LEU   A 1 137 ? 21.140 6.387   6.961  1.00 15.08 ? 143 LEU   A CD1 1 
ATOM   1069 C  CD2 . LEU   A 1 137 ? 23.486 7.419   7.147  1.00 13.86 ? 143 LEU   A CD2 1 
ATOM   1070 N  N   . ASP   A 1 138 ? 24.492 3.821   3.075  1.00 17.58 ? 144 ASP   A N   1 
ATOM   1071 C  CA  . ASP   A 1 138 ? 25.043 2.507   2.695  1.00 19.82 ? 144 ASP   A CA  1 
ATOM   1072 C  C   . ASP   A 1 138 ? 26.391 2.570   1.992  1.00 23.67 ? 144 ASP   A C   1 
ATOM   1073 O  O   . ASP   A 1 138 ? 26.920 1.517   1.619  1.00 24.89 ? 144 ASP   A O   1 
ATOM   1074 C  CB  . ASP   A 1 138 ? 24.046 1.753   1.755  1.00 19.54 ? 144 ASP   A CB  1 
ATOM   1075 C  CG  . ASP   A 1 138 ? 22.707 1.396   2.356  1.00 23.47 ? 144 ASP   A CG  1 
ATOM   1076 O  OD1 . ASP   A 1 138 ? 22.555 1.534   3.588  1.00 23.77 ? 144 ASP   A OD1 1 
ATOM   1077 O  OD2 . ASP   A 1 138 ? 21.800 0.999   1.599  1.00 29.24 ? 144 ASP   A OD2 1 
ATOM   1078 N  N   . GLU   A 1 139 ? 26.950 3.767   1.761  1.00 25.55 ? 145 GLU   A N   1 
ATOM   1079 C  CA  . GLU   A 1 139 ? 28.217 3.878   1.017  1.00 29.19 ? 145 GLU   A CA  1 
ATOM   1080 C  C   . GLU   A 1 139 ? 29.151 4.973   1.573  1.00 31.86 ? 145 GLU   A C   1 
ATOM   1081 O  O   . GLU   A 1 139 ? 28.781 5.667   2.517  1.00 31.38 ? 145 GLU   A O   1 
ATOM   1082 C  CB  . GLU   A 1 139 ? 27.848 4.213   -0.440 1.00 33.69 ? 145 GLU   A CB  1 
ATOM   1083 C  CG  . GLU   A 1 139 ? 27.166 5.567   -0.548 1.00 40.66 ? 145 GLU   A CG  1 
ATOM   1084 C  CD  . GLU   A 1 139 ? 26.296 5.813   -1.766 1.00 47.74 ? 145 GLU   A CD  1 
ATOM   1085 O  OE1 . GLU   A 1 139 ? 25.951 6.993   -2.014 1.00 48.50 ? 145 GLU   A OE1 1 
ATOM   1086 O  OE2 . GLU   A 1 139 ? 25.957 4.832   -2.469 1.00 50.48 ? 145 GLU   A OE2 1 
ATOM   1087 N  N   . GLU   A 1 140 ? 30.335 5.157   0.930  1.00 35.09 ? 146 GLU   A N   1 
ATOM   1088 C  CA  . GLU   A 1 140 ? 31.317 6.233   1.120  1.00 37.84 ? 146 GLU   A CA  1 
ATOM   1089 C  C   . GLU   A 1 140 ? 31.714 6.438   2.562  1.00 39.49 ? 146 GLU   A C   1 
ATOM   1090 O  O   . GLU   A 1 140 ? 31.644 7.557   3.085  1.00 39.99 ? 146 GLU   A O   1 
ATOM   1091 C  CB  . GLU   A 1 140 ? 30.781 7.532   0.472  1.00 41.17 ? 146 GLU   A CB  1 
ATOM   1092 C  CG  . GLU   A 1 140 ? 31.578 8.817   0.668  1.00 48.28 ? 146 GLU   A CG  1 
ATOM   1093 C  CD  . GLU   A 1 140 ? 32.966 8.893   0.058  1.00 56.81 ? 146 GLU   A CD  1 
ATOM   1094 O  OE1 . GLU   A 1 140 ? 33.810 9.626   0.621  1.00 58.01 ? 146 GLU   A OE1 1 
ATOM   1095 O  OE2 . GLU   A 1 140 ? 33.211 8.232   -0.978 1.00 59.37 ? 146 GLU   A OE2 1 
ATOM   1096 N  N   . SER   B 1 1   ? 21.746 -21.321 7.547  1.00 17.77 ? 7   SER   C N   1 
ATOM   1097 C  CA  . SER   B 1 1   ? 20.613 -21.100 8.459  1.00 18.32 ? 7   SER   C CA  1 
ATOM   1098 C  C   . SER   B 1 1   ? 20.592 -22.201 9.546  1.00 18.21 ? 7   SER   C C   1 
ATOM   1099 O  O   . SER   B 1 1   ? 21.277 -23.229 9.406  1.00 19.60 ? 7   SER   C O   1 
ATOM   1100 C  CB  . SER   B 1 1   ? 19.308 -21.167 7.667  1.00 21.68 ? 7   SER   C CB  1 
ATOM   1101 O  OG  . SER   B 1 1   ? 19.178 -22.456 7.089  1.00 25.84 ? 7   SER   C OG  1 
ATOM   1102 N  N   . GLY   B 1 2   ? 19.794 -22.008 10.599 1.00 16.99 ? 8   GLY   C N   1 
ATOM   1103 C  CA  . GLY   B 1 2   ? 19.656 -23.013 11.646 1.00 15.92 ? 8   GLY   C CA  1 
ATOM   1104 C  C   . GLY   B 1 2   ? 19.368 -22.391 12.994 1.00 14.35 ? 8   GLY   C C   1 
ATOM   1105 O  O   . GLY   B 1 2   ? 19.755 -21.255 13.259 1.00 14.43 ? 8   GLY   C O   1 
ATOM   1106 N  N   . ALA   B 1 3   ? 18.707 -23.133 13.862 1.00 13.04 ? 9   ALA   C N   1 
ATOM   1107 C  CA  . ALA   B 1 3   ? 18.370 -22.642 15.207 1.00 13.36 ? 9   ALA   C CA  1 
ATOM   1108 C  C   . ALA   B 1 3   ? 18.506 -23.741 16.250 1.00 12.00 ? 9   ALA   C C   1 
ATOM   1109 O  O   . ALA   B 1 3   ? 18.580 -24.931 15.878 1.00 13.10 ? 9   ALA   C O   1 
ATOM   1110 C  CB  . ALA   B 1 3   ? 16.929 -22.106 15.217 1.00 16.08 ? 9   ALA   C CB  1 
ATOM   1111 N  N   . ILE   B 1 4   ? 18.540 -23.348 17.527 1.00 11.80 ? 10  ILE   C N   1 
ATOM   1112 C  CA  . ILE   B 1 4   ? 18.454 -24.286 18.660 1.00 11.80 ? 10  ILE   C CA  1 
ATOM   1113 C  C   . ILE   B 1 4   ? 17.050 -24.111 19.268 1.00 11.90 ? 10  ILE   C C   1 
ATOM   1114 O  O   . ILE   B 1 4   ? 16.613 -22.963 19.472 1.00 12.77 ? 10  ILE   C O   1 
ATOM   1115 C  CB  . ILE   B 1 4   ? 19.497 -23.974 19.745 1.00 12.31 ? 10  ILE   C CB  1 
ATOM   1116 C  CG1 . ILE   B 1 4   ? 20.934 -23.840 19.161 1.00 13.58 ? 10  ILE   C CG1 1 
ATOM   1117 C  CG2 . ILE   B 1 4   ? 19.427 -25.033 20.869 1.00 13.32 ? 10  ILE   C CG2 1 
ATOM   1118 C  CD1 . ILE   B 1 4   ? 21.892 -23.235 20.171 1.00 14.17 ? 10  ILE   C CD1 1 
ATOM   1119 N  N   . TYR   B 1 5   ? 16.346 -25.222 19.554 1.00 11.71 ? 11  TYR   C N   1 
ATOM   1120 C  CA  . TYR   B 1 5   ? 15.007 -25.156 20.148 1.00 12.70 ? 11  TYR   C CA  1 
ATOM   1121 C  C   . TYR   B 1 5   ? 15.074 -25.829 21.521 1.00 13.94 ? 11  TYR   C C   1 
ATOM   1122 O  O   . TYR   B 1 5   ? 15.150 -27.059 21.603 1.00 14.80 ? 11  TYR   C O   1 
ATOM   1123 C  CB  . TYR   B 1 5   ? 13.964 -25.868 19.238 1.00 13.41 ? 11  TYR   C CB  1 
ATOM   1124 C  CG  . TYR   B 1 5   ? 13.761 -25.127 17.932 1.00 14.16 ? 11  TYR   C CG  1 
ATOM   1125 C  CD1 . TYR   B 1 5   ? 12.925 -24.012 17.862 1.00 14.85 ? 11  TYR   C CD1 1 
ATOM   1126 C  CD2 . TYR   B 1 5   ? 14.477 -25.473 16.796 1.00 14.86 ? 11  TYR   C CD2 1 
ATOM   1127 C  CE1 . TYR   B 1 5   ? 12.796 -23.288 16.683 1.00 16.04 ? 11  TYR   C CE1 1 
ATOM   1128 C  CE2 . TYR   B 1 5   ? 14.336 -24.773 15.606 1.00 16.47 ? 11  TYR   C CE2 1 
ATOM   1129 C  CZ  . TYR   B 1 5   ? 13.504 -23.676 15.557 1.00 16.89 ? 11  TYR   C CZ  1 
ATOM   1130 O  OH  . TYR   B 1 5   ? 13.418 -22.957 14.379 1.00 19.42 ? 11  TYR   C OH  1 
ATOM   1131 N  N   . VAL   B 1 6   ? 15.114 -25.063 22.607 1.00 14.22 ? 12  VAL   C N   1 
ATOM   1132 C  CA  . VAL   B 1 6   ? 15.189 -25.602 23.980 1.00 15.29 ? 12  VAL   C CA  1 
ATOM   1133 C  C   . VAL   B 1 6   ? 14.054 -24.978 24.813 1.00 15.85 ? 12  VAL   C C   1 
ATOM   1134 O  O   . VAL   B 1 6   ? 13.870 -23.768 24.807 1.00 14.63 ? 12  VAL   C O   1 
ATOM   1135 C  CB  . VAL   B 1 6   ? 16.595 -25.329 24.574 1.00 16.14 ? 12  VAL   C CB  1 
ATOM   1136 C  CG1 . VAL   B 1 6   ? 16.965 -23.836 24.474 1.00 16.93 ? 12  VAL   C CG1 1 
ATOM   1137 C  CG2 . VAL   B 1 6   ? 16.671 -25.826 26.005 1.00 17.98 ? 12  VAL   C CG2 1 
ATOM   1138 N  N   . GLY   B 1 7   ? 13.230 -25.801 25.499 1.00 16.53 ? 13  GLY   C N   1 
ATOM   1139 C  CA  . GLY   B 1 7   ? 12.112 -25.253 26.274 1.00 16.54 ? 13  GLY   C CA  1 
ATOM   1140 C  C   . GLY   B 1 7   ? 11.181 -24.423 25.400 1.00 16.85 ? 13  GLY   C C   1 
ATOM   1141 O  O   . GLY   B 1 7   ? 10.917 -24.820 24.257 1.00 17.95 ? 13  GLY   C O   1 
ATOM   1142 N  N   . ASN   B 1 8   ? 10.839 -23.222 25.831 1.00 15.94 ? 14  ASN   C N   1 
ATOM   1143 C  CA  . ASN   B 1 8   ? 10.048 -22.328 24.984 1.00 16.55 ? 14  ASN   C CA  1 
ATOM   1144 C  C   . ASN   B 1 8   ? 10.923 -21.229 24.401 1.00 15.45 ? 14  ASN   C C   1 
ATOM   1145 O  O   . ASN   B 1 8   ? 10.447 -20.107 24.224 1.00 15.77 ? 14  ASN   C O   1 
ATOM   1146 C  CB  . ASN   B 1 8   ? 8.819  -21.753 25.717 1.00 18.83 ? 14  ASN   C CB  1 
ATOM   1147 C  CG  . ASN   B 1 8   ? 7.727  -22.795 25.876 1.00 25.36 ? 14  ASN   C CG  1 
ATOM   1148 O  OD1 . ASN   B 1 8   ? 6.858  -22.958 25.005 1.00 28.72 ? 14  ASN   C OD1 1 
ATOM   1149 N  ND2 . ASN   B 1 8   ? 7.813  -23.567 26.935 1.00 26.61 ? 14  ASN   C ND2 1 
ATOM   1150 N  N   . TYR   B 1 9   ? 12.153 -21.590 24.007 1.00 13.12 ? 15  TYR   C N   1 
ATOM   1151 C  CA  . TYR   B 1 9   ? 13.101 -20.627 23.423 1.00 13.53 ? 15  TYR   C CA  1 
ATOM   1152 C  C   . TYR   B 1 9   ? 13.582 -21.128 22.060 1.00 13.04 ? 15  TYR   C C   1 
ATOM   1153 O  O   . TYR   B 1 9   ? 13.774 -22.342 21.843 1.00 14.61 ? 15  TYR   C O   1 
ATOM   1154 C  CB  . TYR   B 1 9   ? 14.339 -20.474 24.334 1.00 14.43 ? 15  TYR   C CB  1 
ATOM   1155 C  CG  . TYR   B 1 9   ? 14.035 -19.955 25.731 1.00 15.63 ? 15  TYR   C CG  1 
ATOM   1156 C  CD1 . TYR   B 1 9   ? 13.461 -18.703 25.920 1.00 17.95 ? 15  TYR   C CD1 1 
ATOM   1157 C  CD2 . TYR   B 1 9   ? 14.328 -20.718 26.859 1.00 17.94 ? 15  TYR   C CD2 1 
ATOM   1158 C  CE1 . TYR   B 1 9   ? 13.173 -18.232 27.199 1.00 20.51 ? 15  TYR   C CE1 1 
ATOM   1159 C  CE2 . TYR   B 1 9   ? 14.085 -20.236 28.143 1.00 20.58 ? 15  TYR   C CE2 1 
ATOM   1160 C  CZ  . TYR   B 1 9   ? 13.515 -18.990 28.302 1.00 23.07 ? 15  TYR   C CZ  1 
ATOM   1161 O  OH  . TYR   B 1 9   ? 13.247 -18.496 29.561 1.00 28.52 ? 15  TYR   C OH  1 
ATOM   1162 N  N   . ARG   B 1 10  ? 13.830 -20.179 21.154 1.00 12.53 ? 16  ARG   C N   1 
ATOM   1163 C  CA  . ARG   B 1 10  ? 14.442 -20.406 19.830 1.00 12.43 ? 16  ARG   C CA  1 
ATOM   1164 C  C   . ARG   B 1 10  ? 15.707 -19.531 19.807 1.00 11.99 ? 16  ARG   C C   1 
ATOM   1165 O  O   . ARG   B 1 10  ? 15.608 -18.312 20.015 1.00 12.65 ? 16  ARG   C O   1 
ATOM   1166 C  CB  . ARG   B 1 10  ? 13.471 -19.978 18.691 1.00 14.32 ? 16  ARG   C CB  1 
ATOM   1167 C  CG  . ARG   B 1 10  ? 14.111 -19.802 17.308 1.00 15.51 ? 16  ARG   C CG  1 
ATOM   1168 C  CD  . ARG   B 1 10  ? 13.044 -19.549 16.254 1.00 14.83 ? 16  ARG   C CD  1 
ATOM   1169 N  NE  . ARG   B 1 10  ? 13.466 -18.595 15.227 1.00 15.85 ? 16  ARG   C NE  1 
ATOM   1170 C  CZ  . ARG   B 1 10  ? 13.984 -18.907 14.039 1.00 17.64 ? 16  ARG   C CZ  1 
ATOM   1171 N  NH1 . ARG   B 1 10  ? 14.239 -20.180 13.726 1.00 18.39 ? 16  ARG   C NH1 1 
ATOM   1172 N  NH2 . ARG   B 1 10  ? 14.312 -17.946 13.175 1.00 17.32 ? 16  ARG   C NH2 1 
ATOM   1173 N  N   . VAL   B 1 11  ? 16.889 -20.145 19.601 1.00 11.28 ? 17  VAL   C N   1 
ATOM   1174 C  CA  . VAL   B 1 11  ? 18.165 -19.407 19.573 1.00 11.20 ? 17  VAL   C CA  1 
ATOM   1175 C  C   . VAL   B 1 11  ? 18.644 -19.356 18.139 1.00 11.38 ? 17  VAL   C C   1 
ATOM   1176 O  O   . VAL   B 1 11  ? 18.822 -20.432 17.505 1.00 11.83 ? 17  VAL   C O   1 
ATOM   1177 C  CB  . VAL   B 1 11  ? 19.237 -20.134 20.435 1.00 12.39 ? 17  VAL   C CB  1 
ATOM   1178 C  CG1 . VAL   B 1 11  ? 20.505 -19.287 20.503 1.00 14.06 ? 17  VAL   C CG1 1 
ATOM   1179 C  CG2 . VAL   B 1 11  ? 18.705 -20.487 21.840 1.00 13.81 ? 17  VAL   C CG2 1 
ATOM   1180 N  N   . VAL   B 1 12  ? 18.887 -18.141 17.593 1.00 10.96 ? 18  VAL   C N   1 
ATOM   1181 C  CA  . VAL   B 1 12  ? 19.337 -17.982 16.212 1.00 11.79 ? 18  VAL   C CA  1 
ATOM   1182 C  C   . VAL   B 1 12  ? 20.481 -16.979 16.141 1.00 11.45 ? 18  VAL   C C   1 
ATOM   1183 O  O   . VAL   B 1 12  ? 20.720 -16.206 17.092 1.00 11.94 ? 18  VAL   C O   1 
ATOM   1184 C  CB  . VAL   B 1 12  ? 18.168 -17.456 15.304 1.00 13.83 ? 18  VAL   C CB  1 
ATOM   1185 C  CG1 . VAL   B 1 12  ? 17.146 -18.565 15.111 1.00 16.65 ? 18  VAL   C CG1 1 
ATOM   1186 C  CG2 . VAL   B 1 12  ? 17.557 -16.122 15.832 1.00 14.01 ? 18  VAL   C CG2 1 
ATOM   1187 N  N   . ASN   B 1 13  ? 21.178 -16.946 14.981 1.00 10.94 ? 19  ASN   C N   1 
ATOM   1188 C  CA  . ASN   B 1 13  ? 22.149 -15.866 14.763 1.00 10.85 ? 19  ASN   C CA  1 
ATOM   1189 C  C   . ASN   B 1 13  ? 21.339 -14.534 14.711 1.00 11.99 ? 19  ASN   C C   1 
ATOM   1190 O  O   . ASN   B 1 13  ? 20.326 -14.448 14.008 1.00 11.84 ? 19  ASN   C O   1 
ATOM   1191 C  CB  . ASN   B 1 13  ? 22.859 -16.033 13.403 1.00 11.57 ? 19  ASN   C CB  1 
ATOM   1192 C  CG  . ASN   B 1 13  ? 23.717 -17.285 13.322 1.00 11.46 ? 19  ASN   C CG  1 
ATOM   1193 O  OD1 . ASN   B 1 13  ? 23.254 -18.359 12.912 1.00 12.92 ? 19  ASN   C OD1 1 
ATOM   1194 N  ND2 . ASN   B 1 13  ? 24.947 -17.160 13.798 1.00 11.93 ? 19  ASN   C ND2 1 
ATOM   1195 N  N   . ARG   B 1 14  ? 21.843 -13.494 15.415 1.00 11.53 ? 20  ARG   C N   1 
ATOM   1196 C  CA  . ARG   B 1 14  ? 21.104 -12.210 15.440 1.00 10.89 ? 20  ARG   C CA  1 
ATOM   1197 C  C   . ARG   B 1 14  ? 20.949 -11.673 14.003 1.00 12.11 ? 20  ARG   C C   1 
ATOM   1198 O  O   . ARG   B 1 14  ? 19.895 -11.129 13.653 1.00 12.85 ? 20  ARG   C O   1 
ATOM   1199 C  CB  . ARG   B 1 14  ? 21.857 -11.215 16.315 1.00 10.92 ? 20  ARG   C CB  1 
ATOM   1200 C  CG  . ARG   B 1 14  ? 21.078 -9.877  16.538 1.00 11.64 ? 20  ARG   C CG  1 
ATOM   1201 C  CD  . ARG   B 1 14  ? 21.945 -8.922  17.327 1.00 12.20 ? 20  ARG   C CD  1 
ATOM   1202 N  NE  . ARG   B 1 14  ? 21.271 -7.677  17.772 1.00 13.01 ? 20  ARG   C NE  1 
ATOM   1203 C  CZ  . ARG   B 1 14  ? 21.193 -6.570  17.044 1.00 13.47 ? 20  ARG   C CZ  1 
ATOM   1204 N  NH1 . ARG   B 1 14  ? 21.591 -6.566  15.781 1.00 14.68 ? 20  ARG   C NH1 1 
ATOM   1205 N  NH2 . ARG   B 1 14  ? 20.675 -5.461  17.566 1.00 13.41 ? 20  ARG   C NH2 1 
ATOM   1206 N  N   . HIS   B 1 15  ? 21.997 -11.867 13.150 1.00 11.67 ? 21  HIS   C N   1 
ATOM   1207 C  CA  . HIS   B 1 15  ? 21.905 -11.320 11.781 1.00 12.88 ? 21  HIS   C CA  1 
ATOM   1208 C  C   . HIS   B 1 15  ? 20.906 -12.064 10.873 1.00 13.00 ? 21  HIS   C C   1 
ATOM   1209 O  O   . HIS   B 1 15  ? 20.580 -11.539 9.815  1.00 15.19 ? 21  HIS   C O   1 
ATOM   1210 C  CB  . HIS   B 1 15  ? 23.304 -11.215 11.133 1.00 12.50 ? 21  HIS   C CB  1 
ATOM   1211 C  CG  . HIS   B 1 15  ? 23.912 -12.527 10.694 1.00 13.04 ? 21  HIS   C CG  1 
ATOM   1212 N  ND1 . HIS   B 1 15  ? 24.637 -13.333 11.574 1.00 13.43 ? 21  HIS   C ND1 1 
ATOM   1213 C  CD2 . HIS   B 1 15  ? 23.913 -13.112 9.467  1.00 14.10 ? 21  HIS   C CD2 1 
ATOM   1214 C  CE1 . HIS   B 1 15  ? 25.032 -14.396 10.860 1.00 14.43 ? 21  HIS   C CE1 1 
ATOM   1215 N  NE2 . HIS   B 1 15  ? 24.613 -14.291 9.579  1.00 14.30 ? 21  HIS   C NE2 1 
ATOM   1216 N  N   . LEU   B 1 16  ? 20.378 -13.210 11.318 1.00 12.33 ? 22  LEU   C N   1 
ATOM   1217 C  CA  . LEU   B 1 16  ? 19.374 -13.975 10.562 1.00 13.51 ? 22  LEU   C CA  1 
ATOM   1218 C  C   . LEU   B 1 16  ? 17.985 -13.932 11.225 1.00 14.42 ? 22  LEU   C C   1 
ATOM   1219 O  O   . LEU   B 1 16  ? 17.060 -14.653 10.789 1.00 15.21 ? 22  LEU   C O   1 
ATOM   1220 C  CB  . LEU   B 1 16  ? 19.845 -15.431 10.359 1.00 13.71 ? 22  LEU   C CB  1 
ATOM   1221 C  CG  . LEU   B 1 16  ? 21.138 -15.561 9.579  1.00 13.89 ? 22  LEU   C CG  1 
ATOM   1222 C  CD1 . LEU   B 1 16  ? 21.602 -17.042 9.525  1.00 14.51 ? 22  LEU   C CD1 1 
ATOM   1223 C  CD2 . LEU   B 1 16  ? 21.011 -14.953 8.176  1.00 14.49 ? 22  LEU   C CD2 1 
ATOM   1224 N  N   . ALA   B 1 17  ? 17.828 -13.166 12.335 1.00 14.19 ? 23  ALA   C N   1 
ATOM   1225 C  CA  . ALA   B 1 17  ? 16.544 -13.124 13.057 1.00 13.63 ? 23  ALA   C CA  1 
ATOM   1226 C  C   . ALA   B 1 17  ? 15.425 -12.584 12.178 1.00 15.20 ? 23  ALA   C C   1 
ATOM   1227 O  O   . ALA   B 1 17  ? 15.646 -11.638 11.400 1.00 16.84 ? 23  ALA   C O   1 
ATOM   1228 C  CB  . ALA   B 1 17  ? 16.687 -12.251 14.309 1.00 15.46 ? 23  ALA   C CB  1 
ATOM   1229 N  N   . THR   B 1 18  ? 14.237 -13.172 12.313 1.00 16.21 ? 24  THR   C N   1 
ATOM   1230 C  CA  . THR   B 1 18  ? 13.063 -12.765 11.530 1.00 16.80 ? 24  THR   C CA  1 
ATOM   1231 C  C   . THR   B 1 18  ? 12.243 -11.696 12.290 1.00 16.70 ? 24  THR   C C   1 
ATOM   1232 O  O   . THR   B 1 18  ? 12.506 -11.384 13.459 1.00 17.58 ? 24  THR   C O   1 
ATOM   1233 C  CB  . THR   B 1 18  ? 12.163 -14.009 11.284 1.00 18.76 ? 24  THR   C CB  1 
ATOM   1234 O  OG1 . THR   B 1 18  ? 11.629 -14.422 12.537 1.00 18.39 ? 24  THR   C OG1 1 
ATOM   1235 C  CG2 . THR   B 1 18  ? 12.911 -15.177 10.616 1.00 20.10 ? 24  THR   C CG2 1 
ATOM   1236 N  N   . HIS   B 1 19  ? 11.206 -11.113 11.610 1.00 18.49 ? 25  HIS   C N   1 
ATOM   1237 C  CA  . HIS   B 1 19  ? 10.311 -10.190 12.306 1.00 19.77 ? 25  HIS   C CA  1 
ATOM   1238 C  C   . HIS   B 1 19  ? 9.610  -10.921 13.449 1.00 17.55 ? 25  HIS   C C   1 
ATOM   1239 O  O   . HIS   B 1 19  ? 9.530  -10.348 14.535 1.00 18.51 ? 25  HIS   C O   1 
ATOM   1240 C  CB  . HIS   B 1 19  ? 9.230  -9.639  11.359 1.00 21.80 ? 25  HIS   C CB  1 
ATOM   1241 C  CG  . HIS   B 1 19  ? 8.104  -8.930  12.077 1.00 24.83 ? 25  HIS   C CG  1 
ATOM   1242 N  ND1 . HIS   B 1 19  ? 8.298  -7.698  12.688 1.00 26.93 ? 25  HIS   C ND1 1 
ATOM   1243 C  CD2 . HIS   B 1 19  ? 6.868  -9.382  12.399 1.00 27.27 ? 25  HIS   C CD2 1 
ATOM   1244 C  CE1 . HIS   B 1 19  ? 7.126  -7.369  13.221 1.00 27.51 ? 25  HIS   C CE1 1 
ATOM   1245 N  NE2 . HIS   B 1 19  ? 6.242  -8.365  13.106 1.00 27.81 ? 25  HIS   C NE2 1 
ATOM   1246 N  N   . ASN   B 1 20  ? 9.204  -12.187 13.254 1.00 17.88 ? 26  ASN   C N   1 
ATOM   1247 C  CA  . ASN   B 1 20  ? 8.569  -12.916 14.348 1.00 17.97 ? 26  ASN   C CA  1 
ATOM   1248 C  C   . ASN   B 1 20  ? 9.505  -13.079 15.538 1.00 16.31 ? 26  ASN   C C   1 
ATOM   1249 O  O   . ASN   B 1 20  ? 9.086  -12.942 16.682 1.00 16.41 ? 26  ASN   C O   1 
ATOM   1250 C  CB  . ASN   B 1 20  ? 8.027  -14.276 13.903 1.00 20.01 ? 26  ASN   C CB  1 
ATOM   1251 C  CG  . ASN   B 1 20  ? 7.227  -14.954 15.011 1.00 26.39 ? 26  ASN   C CG  1 
ATOM   1252 O  OD1 . ASN   B 1 20  ? 6.114  -14.523 15.345 1.00 29.96 ? 26  ASN   C OD1 1 
ATOM   1253 N  ND2 . ASN   B 1 20  ? 7.795  -15.967 15.661 1.00 27.92 ? 26  ASN   C ND2 1 
ATOM   1254 N  N   . ASP   B 1 21  ? 10.830 -13.281 15.264 1.00 15.51 ? 27  ASP   C N   1 
ATOM   1255 C  CA  . ASP   B 1 21  ? 11.773 -13.357 16.372 1.00 15.08 ? 27  ASP   C CA  1 
ATOM   1256 C  C   . ASP   B 1 21  ? 11.821 -12.037 17.157 1.00 14.23 ? 27  ASP   C C   1 
ATOM   1257 O  O   . ASP   B 1 21  ? 11.774 -12.046 18.378 1.00 15.79 ? 27  ASP   C O   1 
ATOM   1258 C  CB  . ASP   B 1 21  ? 13.187 -13.659 15.853 1.00 14.35 ? 27  ASP   C CB  1 
ATOM   1259 C  CG  . ASP   B 1 21  ? 13.402 -15.088 15.384 1.00 14.75 ? 27  ASP   C CG  1 
ATOM   1260 O  OD1 . ASP   B 1 21  ? 12.822 -16.015 16.006 1.00 15.89 ? 27  ASP   C OD1 1 
ATOM   1261 O  OD2 . ASP   B 1 21  ? 14.081 -15.280 14.355 1.00 15.19 ? 27  ASP   C OD2 1 
ATOM   1262 N  N   . TRP   B 1 22  ? 11.898 -10.893 16.438 1.00 14.70 ? 28  TRP   C N   1 
ATOM   1263 C  CA  . TRP   B 1 22  ? 11.958 -9.604  17.122 1.00 15.19 ? 28  TRP   C CA  1 
ATOM   1264 C  C   . TRP   B 1 22  ? 10.630 -9.260  17.858 1.00 15.49 ? 28  TRP   C C   1 
ATOM   1265 O  O   . TRP   B 1 22  ? 10.664 -8.636  18.929 1.00 16.83 ? 28  TRP   C O   1 
ATOM   1266 C  CB  . TRP   B 1 22  ? 12.332 -8.494  16.146 1.00 16.01 ? 28  TRP   C CB  1 
ATOM   1267 C  CG  . TRP   B 1 22  ? 13.815 -8.447  15.860 1.00 16.07 ? 28  TRP   C CG  1 
ATOM   1268 C  CD1 . TRP   B 1 22  ? 14.457 -8.940  14.761 1.00 17.65 ? 28  TRP   C CD1 1 
ATOM   1269 C  CD2 . TRP   B 1 22  ? 14.831 -7.868  16.695 1.00 15.19 ? 28  TRP   C CD2 1 
ATOM   1270 N  NE1 . TRP   B 1 22  ? 15.812 -8.664  14.841 1.00 17.77 ? 28  TRP   C NE1 1 
ATOM   1271 C  CE2 . TRP   B 1 22  ? 16.071 -8.045  16.036 1.00 17.09 ? 28  TRP   C CE2 1 
ATOM   1272 C  CE3 . TRP   B 1 22  ? 14.819 -7.213  17.924 1.00 17.55 ? 28  TRP   C CE3 1 
ATOM   1273 C  CZ2 . TRP   B 1 22  ? 17.249 -7.503  16.516 1.00 17.15 ? 28  TRP   C CZ2 1 
ATOM   1274 C  CZ3 . TRP   B 1 22  ? 16.014 -6.718  18.423 1.00 18.29 ? 28  TRP   C CZ3 1 
ATOM   1275 C  CH2 . TRP   B 1 22  ? 17.214 -6.894  17.720 1.00 17.31 ? 28  TRP   C CH2 1 
ATOM   1276 N  N   . ALA   B 1 23  ? 9.514  -9.718  17.306 1.00 16.05 ? 29  ALA   C N   1 
ATOM   1277 C  CA  . ALA   B 1 23  ? 8.190  -9.469  17.923 1.00 16.63 ? 29  ALA   C CA  1 
ATOM   1278 C  C   . ALA   B 1 23  ? 7.948  -10.347 19.155 1.00 18.46 ? 29  ALA   C C   1 
ATOM   1279 O  O   . ALA   B 1 23  ? 7.000  -10.121 19.906 1.00 18.62 ? 29  ALA   C O   1 
ATOM   1280 C  CB  . ALA   B 1 23  ? 7.083  -9.723  16.905 1.00 17.14 ? 29  ALA   C CB  1 
ATOM   1281 N  N   . ASN   B 1 24  ? 8.780  -11.407 19.345 1.00 17.70 ? 30  ASN   C N   1 
ATOM   1282 C  CA  . ASN   B 1 24  ? 8.675  -12.313 20.494 1.00 16.64 ? 30  ASN   C CA  1 
ATOM   1283 C  C   . ASN   B 1 24  ? 10.054 -12.367 21.182 1.00 16.38 ? 30  ASN   C C   1 
ATOM   1284 O  O   . ASN   B 1 24  ? 10.480 -13.426 21.638 1.00 15.92 ? 30  ASN   C O   1 
ATOM   1285 C  CB  . ASN   B 1 24  ? 8.211  -13.696 20.009 1.00 18.41 ? 30  ASN   C CB  1 
ATOM   1286 C  CG  . ASN   B 1 24  ? 6.781  -13.626 19.526 1.00 20.49 ? 30  ASN   C CG  1 
ATOM   1287 O  OD1 . ASN   B 1 24  ? 5.822  -13.635 20.332 1.00 22.17 ? 30  ASN   C OD1 1 
ATOM   1288 N  ND2 . ASN   B 1 24  ? 6.605  -13.499 18.222 1.00 21.29 ? 30  ASN   C ND2 1 
ATOM   1289 N  N   . LEU   B 1 25  ? 10.749 -11.234 21.274 1.00 16.56 ? 31  LEU   C N   1 
ATOM   1290 C  CA  . LEU   B 1 25  ? 12.121 -11.202 21.781 1.00 16.42 ? 31  LEU   C CA  1 
ATOM   1291 C  C   . LEU   B 1 25  ? 12.265 -11.507 23.253 1.00 17.56 ? 31  LEU   C C   1 
ATOM   1292 O  O   . LEU   B 1 25  ? 11.502 -10.977 24.064 1.00 18.44 ? 31  LEU   C O   1 
ATOM   1293 C  CB  . LEU   B 1 25  ? 12.701 -9.809  21.473 1.00 16.29 ? 31  LEU   C CB  1 
ATOM   1294 C  CG  . LEU   B 1 25  ? 14.162 -9.629  21.861 1.00 16.20 ? 31  LEU   C CG  1 
ATOM   1295 C  CD1 . LEU   B 1 25  ? 15.099 -10.506 20.998 1.00 15.99 ? 31  LEU   C CD1 1 
ATOM   1296 C  CD2 . LEU   B 1 25  ? 14.553 -8.176  21.750 1.00 17.24 ? 31  LEU   C CD2 1 
ATOM   1297 N  N   . VAL   B 1 26  ? 13.238 -12.351 23.613 1.00 16.20 ? 32  VAL   C N   1 
ATOM   1298 C  CA  . VAL   B 1 26  ? 13.583 -12.616 25.005 1.00 16.52 ? 32  VAL   C CA  1 
ATOM   1299 C  C   . VAL   B 1 26  ? 14.909 -11.901 25.320 1.00 17.00 ? 32  VAL   C C   1 
ATOM   1300 O  O   . VAL   B 1 26  ? 15.016 -11.200 26.338 1.00 17.97 ? 32  VAL   C O   1 
ATOM   1301 C  CB  . VAL   B 1 26  ? 13.724 -14.135 25.237 1.00 17.32 ? 32  VAL   C CB  1 
ATOM   1302 C  CG1 . VAL   B 1 26  ? 14.269 -14.448 26.631 1.00 18.79 ? 32  VAL   C CG1 1 
ATOM   1303 C  CG2 . VAL   B 1 26  ? 12.382 -14.831 25.032 1.00 17.81 ? 32  VAL   C CG2 1 
ATOM   1304 N  N   . TRP   B 1 27  ? 15.934 -12.050 24.444 1.00 15.36 ? 33  TRP   C N   1 
ATOM   1305 C  CA  . TRP   B 1 27  ? 17.248 -11.473 24.722 1.00 15.31 ? 33  TRP   C CA  1 
ATOM   1306 C  C   . TRP   B 1 27  ? 18.045 -11.422 23.426 1.00 14.78 ? 33  TRP   C C   1 
ATOM   1307 O  O   . TRP   B 1 27  ? 17.860 -12.291 22.561 1.00 14.37 ? 33  TRP   C O   1 
ATOM   1308 C  CB  . TRP   B 1 27  ? 17.978 -12.355 25.785 1.00 16.36 ? 33  TRP   C CB  1 
ATOM   1309 C  CG  . TRP   B 1 27  ? 19.455 -12.092 25.980 1.00 16.48 ? 33  TRP   C CG  1 
ATOM   1310 C  CD1 . TRP   B 1 27  ? 20.034 -11.150 26.794 1.00 18.39 ? 33  TRP   C CD1 1 
ATOM   1311 C  CD2 . TRP   B 1 27  ? 20.542 -12.790 25.342 1.00 14.69 ? 33  TRP   C CD2 1 
ATOM   1312 N  NE1 . TRP   B 1 27  ? 21.419 -11.239 26.716 1.00 18.88 ? 33  TRP   C NE1 1 
ATOM   1313 C  CE2 . TRP   B 1 27  ? 21.749 -12.254 25.849 1.00 16.25 ? 33  TRP   C CE2 1 
ATOM   1314 C  CE3 . TRP   B 1 27  ? 20.610 -13.818 24.385 1.00 14.66 ? 33  TRP   C CE3 1 
ATOM   1315 C  CZ2 . TRP   B 1 27  ? 23.000 -12.733 25.456 1.00 16.51 ? 33  TRP   C CZ2 1 
ATOM   1316 C  CZ3 . TRP   B 1 27  ? 21.858 -14.317 24.037 1.00 16.30 ? 33  TRP   C CZ3 1 
ATOM   1317 C  CH2 . TRP   B 1 27  ? 23.026 -13.734 24.523 1.00 16.34 ? 33  TRP   C CH2 1 
ATOM   1318 N  N   . GLU   B 1 28  ? 18.894 -10.427 23.272 1.00 14.76 ? 34  GLU   C N   1 
ATOM   1319 C  CA  . GLU   B 1 28  ? 19.757 -10.335 22.097 1.00 15.20 ? 34  GLU   C CA  1 
ATOM   1320 C  C   . GLU   B 1 28  ? 21.050 -9.655  22.445 1.00 14.63 ? 34  GLU   C C   1 
ATOM   1321 O  O   . GLU   B 1 28  ? 21.074 -8.774  23.347 1.00 14.88 ? 34  GLU   C O   1 
ATOM   1322 C  CB  . GLU   B 1 28  ? 19.102 -9.634  20.892 1.00 15.03 ? 34  GLU   C CB  1 
ATOM   1323 C  CG  . GLU   B 1 28  ? 18.511 -8.282  21.227 1.00 16.12 ? 34  GLU   C CG  1 
ATOM   1324 C  CD  . GLU   B 1 28  ? 19.467 -7.103  21.144 1.00 18.69 ? 34  GLU   C CD  1 
ATOM   1325 O  OE1 . GLU   B 1 28  ? 19.219 -6.086  21.834 1.00 21.43 ? 34  GLU   C OE1 1 
ATOM   1326 O  OE2 . GLU   B 1 28  ? 20.475 -7.189  20.406 1.00 16.87 ? 34  GLU   C OE2 1 
ATOM   1327 N  N   . ASP   B 1 29  ? 22.124 -10.010 21.738 1.00 13.18 ? 35  ASP   C N   1 
ATOM   1328 C  CA  . ASP   B 1 29  ? 23.417 -9.366  21.969 1.00 13.67 ? 35  ASP   C CA  1 
ATOM   1329 C  C   . ASP   B 1 29  ? 24.195 -9.327  20.653 1.00 13.56 ? 35  ASP   C C   1 
ATOM   1330 O  O   . ASP   B 1 29  ? 24.642 -10.367 20.147 1.00 13.59 ? 35  ASP   C O   1 
ATOM   1331 C  CB  . ASP   B 1 29  ? 24.150 -10.150 23.076 1.00 14.90 ? 35  ASP   C CB  1 
ATOM   1332 C  CG  . ASP   B 1 29  ? 25.493 -9.584  23.469 1.00 19.62 ? 35  ASP   C CG  1 
ATOM   1333 O  OD1 . ASP   B 1 29  ? 26.211 -9.088  22.584 1.00 20.62 ? 35  ASP   C OD1 1 
ATOM   1334 O  OD2 . ASP   B 1 29  ? 25.864 -9.720  24.651 1.00 22.36 ? 35  ASP   C OD2 1 
ATOM   1335 N  N   . SER   B 1 30  ? 24.341 -8.122  20.078 1.00 13.70 ? 36  SER   C N   1 
ATOM   1336 C  CA  A SER   B 1 30  ? 25.050 -7.939  18.814 0.50 14.23 ? 36  SER   C CA  1 
ATOM   1337 C  CA  B SER   B 1 30  ? 25.039 -7.986  18.805 0.50 14.23 ? 36  SER   C CA  1 
ATOM   1338 C  C   . SER   B 1 30  ? 26.518 -8.376  18.900 1.00 14.61 ? 36  SER   C C   1 
ATOM   1339 O  O   . SER   B 1 30  ? 27.040 -8.976  17.940 1.00 14.95 ? 36  SER   C O   1 
ATOM   1340 C  CB  A SER   B 1 30  ? 24.965 -6.485  18.360 0.50 16.44 ? 36  SER   C CB  1 
ATOM   1341 C  CB  B SER   B 1 30  ? 24.879 -6.579  18.249 0.50 16.33 ? 36  SER   C CB  1 
ATOM   1342 O  OG  A SER   B 1 30  ? 25.878 -6.228  17.301 0.50 17.18 ? 36  SER   C OG  1 
ATOM   1343 O  OG  B SER   B 1 30  ? 25.318 -5.638  19.207 0.50 16.74 ? 36  SER   C OG  1 
ATOM   1344 N  N   . SER   B 1 31  ? 27.167 -8.121  20.062 1.00 14.35 ? 37  SER   C N   1 
ATOM   1345 C  CA  . SER   B 1 31  ? 28.589 -8.516  20.154 1.00 15.01 ? 37  SER   C CA  1 
ATOM   1346 C  C   . SER   B 1 31  ? 28.777 -10.021 20.091 1.00 14.06 ? 37  SER   C C   1 
ATOM   1347 O  O   . SER   B 1 31  ? 29.871 -10.467 19.727 1.00 14.98 ? 37  SER   C O   1 
ATOM   1348 C  CB  . SER   B 1 31  ? 29.228 -7.966  21.417 1.00 18.32 ? 37  SER   C CB  1 
ATOM   1349 O  OG  . SER   B 1 31  ? 28.790 -8.637  22.578 1.00 24.63 ? 37  SER   C OG  1 
ATOM   1350 N  N   . ARG   B 1 32  ? 27.724 -10.817 20.419 1.00 13.03 ? 38  ARG   C N   1 
ATOM   1351 C  CA  . ARG   B 1 32  ? 27.800 -12.289 20.363 1.00 12.73 ? 38  ARG   C CA  1 
ATOM   1352 C  C   . ARG   B 1 32  ? 27.168 -12.861 19.082 1.00 12.87 ? 38  ARG   C C   1 
ATOM   1353 O  O   . ARG   B 1 32  ? 27.230 -14.072 18.862 1.00 12.63 ? 38  ARG   C O   1 
ATOM   1354 C  CB  . ARG   B 1 32  ? 27.048 -12.874 21.591 1.00 13.95 ? 38  ARG   C CB  1 
ATOM   1355 C  CG  . ARG   B 1 32  ? 27.709 -12.496 22.912 1.00 15.26 ? 38  ARG   C CG  1 
ATOM   1356 C  CD  . ARG   B 1 32  ? 26.972 -13.080 24.115 1.00 13.95 ? 38  ARG   C CD  1 
ATOM   1357 N  NE  . ARG   B 1 32  ? 27.031 -14.557 24.142 1.00 13.90 ? 38  ARG   C NE  1 
ATOM   1358 C  CZ  . ARG   B 1 32  ? 27.009 -15.298 25.255 1.00 14.14 ? 38  ARG   C CZ  1 
ATOM   1359 N  NH1 . ARG   B 1 32  ? 26.898 -14.720 26.451 1.00 15.43 ? 38  ARG   C NH1 1 
ATOM   1360 N  NH2 . ARG   B 1 32  ? 27.161 -16.616 25.183 1.00 13.64 ? 38  ARG   C NH2 1 
ATOM   1361 N  N   . ASP   B 1 33  ? 26.492 -12.014 18.268 1.00 11.44 ? 39  ASP   C N   1 
ATOM   1362 C  CA  . ASP   B 1 33  ? 25.720 -12.487 17.128 1.00 11.33 ? 39  ASP   C CA  1 
ATOM   1363 C  C   . ASP   B 1 33  ? 24.612 -13.456 17.571 1.00 11.06 ? 39  ASP   C C   1 
ATOM   1364 O  O   . ASP   B 1 33  ? 24.303 -14.388 16.812 1.00 11.96 ? 39  ASP   C O   1 
ATOM   1365 C  CB  . ASP   B 1 33  ? 26.579 -13.104 16.015 1.00 11.70 ? 39  ASP   C CB  1 
ATOM   1366 C  CG  . ASP   B 1 33  ? 25.780 -13.429 14.746 1.00 12.28 ? 39  ASP   C CG  1 
ATOM   1367 O  OD1 . ASP   B 1 33  ? 24.882 -12.617 14.365 1.00 13.38 ? 39  ASP   C OD1 1 
ATOM   1368 O  OD2 . ASP   B 1 33  ? 26.088 -14.451 14.100 1.00 12.68 ? 39  ASP   C OD2 1 
ATOM   1369 N  N   . LEU   B 1 34  ? 23.946 -13.229 18.738 1.00 10.74 ? 40  LEU   C N   1 
ATOM   1370 C  CA  . LEU   B 1 34  ? 22.867 -14.132 19.169 1.00 11.06 ? 40  LEU   C CA  1 
ATOM   1371 C  C   . LEU   B 1 34  ? 21.570 -13.376 19.427 1.00 11.11 ? 40  LEU   C C   1 
ATOM   1372 O  O   . LEU   B 1 34  ? 21.583 -12.222 19.898 1.00 12.14 ? 40  LEU   C O   1 
ATOM   1373 C  CB  . LEU   B 1 34  ? 23.254 -14.836 20.481 1.00 11.39 ? 40  LEU   C CB  1 
ATOM   1374 C  CG  . LEU   B 1 34  ? 24.322 -15.927 20.388 1.00 11.92 ? 40  LEU   C CG  1 
ATOM   1375 C  CD1 . LEU   B 1 34  ? 24.601 -16.508 21.805 1.00 13.58 ? 40  LEU   C CD1 1 
ATOM   1376 C  CD2 . LEU   B 1 34  ? 23.910 -17.041 19.427 1.00 13.21 ? 40  LEU   C CD2 1 
ATOM   1377 N  N   . LEU   B 1 35  ? 20.465 -14.072 19.194 1.00 10.48 ? 41  LEU   C N   1 
ATOM   1378 C  CA  . LEU   B 1 35  ? 19.137 -13.564 19.551 1.00 11.74 ? 41  LEU   C CA  1 
ATOM   1379 C  C   . LEU   B 1 35  ? 18.314 -14.785 19.959 1.00 11.83 ? 41  LEU   C C   1 
ATOM   1380 O  O   . LEU   B 1 35  ? 18.425 -15.860 19.348 1.00 12.40 ? 41  LEU   C O   1 
ATOM   1381 C  CB  . LEU   B 1 35  ? 18.500 -12.852 18.325 1.00 12.46 ? 41  LEU   C CB  1 
ATOM   1382 C  CG  . LEU   B 1 35  ? 17.100 -12.250 18.589 1.00 12.06 ? 41  LEU   C CG  1 
ATOM   1383 C  CD1 . LEU   B 1 35  ? 16.904 -10.945 17.812 1.00 14.74 ? 41  LEU   C CD1 1 
ATOM   1384 C  CD2 . LEU   B 1 35  ? 15.996 -13.276 18.225 1.00 13.35 ? 41  LEU   C CD2 1 
ATOM   1385 N  N   . VAL   B 1 36  ? 17.518 -14.617 21.021 1.00 11.93 ? 42  VAL   C N   1 
ATOM   1386 C  CA  . VAL   B 1 36  ? 16.608 -15.637 21.537 1.00 11.82 ? 42  VAL   C CA  1 
ATOM   1387 C  C   . VAL   B 1 36  ? 15.191 -15.089 21.526 1.00 11.80 ? 42  VAL   C C   1 
ATOM   1388 O  O   . VAL   B 1 36  ? 14.955 -13.966 22.022 1.00 13.77 ? 42  VAL   C O   1 
ATOM   1389 C  CB  . VAL   B 1 36  ? 17.009 -16.075 22.954 1.00 12.85 ? 42  VAL   C CB  1 
ATOM   1390 C  CG1 . VAL   B 1 36  ? 16.036 -17.121 23.507 1.00 13.69 ? 42  VAL   C CG1 1 
ATOM   1391 C  CG2 . VAL   B 1 36  ? 18.458 -16.626 22.960 1.00 13.56 ? 42  VAL   C CG2 1 
ATOM   1392 N  N   . SER   B 1 37  ? 14.273 -15.853 20.954 1.00 12.08 ? 43  SER   C N   1 
ATOM   1393 C  CA  . SER   B 1 37  ? 12.862 -15.499 20.949 1.00 12.42 ? 43  SER   C CA  1 
ATOM   1394 C  C   . SER   B 1 37  ? 12.047 -16.596 21.644 1.00 13.85 ? 43  SER   C C   1 
ATOM   1395 O  O   . SER   B 1 37  ? 12.536 -17.716 21.886 1.00 13.65 ? 43  SER   C O   1 
ATOM   1396 C  CB  . SER   B 1 37  ? 12.371 -15.304 19.527 1.00 13.39 ? 43  SER   C CB  1 
ATOM   1397 O  OG  . SER   B 1 37  ? 12.552 -16.462 18.727 1.00 15.22 ? 43  SER   C OG  1 
ATOM   1398 N  N   . SER   B 1 38  ? 10.789 -16.273 22.024 1.00 14.67 ? 44  SER   C N   1 
ATOM   1399 C  CA  . SER   B 1 38  ? 9.931  -17.241 22.685 1.00 15.27 ? 44  SER   C CA  1 
ATOM   1400 C  C   . SER   B 1 38  ? 9.120  -18.039 21.649 1.00 17.42 ? 44  SER   C C   1 
ATOM   1401 O  O   . SER   B 1 38  ? 8.833  -17.549 20.557 1.00 18.93 ? 44  SER   C O   1 
ATOM   1402 C  CB  . SER   B 1 38  ? 9.015  -16.518 23.665 1.00 18.13 ? 44  SER   C CB  1 
ATOM   1403 O  OG  . SER   B 1 38  ? 8.190  -15.616 22.955 1.00 23.26 ? 44  SER   C OG  1 
ATOM   1404 N  N   . THR   B 1 39  ? 8.763  -19.279 21.991 1.00 17.24 ? 45  THR   C N   1 
ATOM   1405 C  CA  . THR   B 1 39  ? 8.009  -20.167 21.101 1.00 18.18 ? 45  THR   C CA  1 
ATOM   1406 C  C   . THR   B 1 39  ? 6.717  -20.637 21.800 1.00 20.81 ? 45  THR   C C   1 
ATOM   1407 O  O   . THR   B 1 39  ? 6.662  -20.722 23.019 1.00 20.19 ? 45  THR   C O   1 
ATOM   1408 C  CB  . THR   B 1 39  ? 8.853  -21.423 20.730 1.00 18.58 ? 45  THR   C CB  1 
ATOM   1409 O  OG1 . THR   B 1 39  ? 9.129  -22.172 21.908 1.00 19.40 ? 45  THR   C OG1 1 
ATOM   1410 C  CG2 . THR   B 1 39  ? 10.187 -21.063 20.059 1.00 19.71 ? 45  THR   C CG2 1 
ATOM   1411 N  N   . THR   B 1 40  ? 5.730  -21.027 21.003 1.00 22.56 ? 46  THR   C N   1 
ATOM   1412 C  CA  . THR   B 1 40  ? 4.489  -21.580 21.561 1.00 24.75 ? 46  THR   C CA  1 
ATOM   1413 C  C   . THR   B 1 40  ? 4.698  -23.049 21.924 1.00 25.27 ? 46  THR   C C   1 
ATOM   1414 O  O   . THR   B 1 40  ? 4.275  -23.491 22.993 1.00 27.64 ? 46  THR   C O   1 
ATOM   1415 C  CB  . THR   B 1 40  ? 3.322  -21.309 20.612 1.00 29.34 ? 46  THR   C CB  1 
ATOM   1416 O  OG1 . THR   B 1 40  ? 3.645  -21.873 19.345 1.00 33.71 ? 46  THR   C OG1 1 
ATOM   1417 C  CG2 . THR   B 1 40  ? 3.085  -19.824 20.426 1.00 29.27 ? 46  THR   C CG2 1 
ATOM   1418 N  N   . ALA   B 1 41  ? 5.386  -23.805 21.052 1.00 23.23 ? 47  ALA   C N   1 
ATOM   1419 C  CA  . ALA   B 1 41  ? 5.640  -25.217 21.290 1.00 23.49 ? 47  ALA   C CA  1 
ATOM   1420 C  C   . ALA   B 1 41  ? 6.970  -25.445 22.023 1.00 21.83 ? 47  ALA   C C   1 
ATOM   1421 O  O   . ALA   B 1 41  ? 7.908  -24.679 21.818 1.00 20.86 ? 47  ALA   C O   1 
ATOM   1422 C  CB  . ALA   B 1 41  ? 5.675  -25.958 19.958 1.00 24.76 ? 47  ALA   C CB  1 
ATOM   1423 N  N   . GLN   B 1 42  ? 7.080  -26.509 22.812 1.00 21.27 ? 48  GLN   C N   1 
ATOM   1424 C  CA  . GLN   B 1 42  ? 8.315  -26.832 23.511 1.00 21.21 ? 48  GLN   C CA  1 
ATOM   1425 C  C   . GLN   B 1 42  ? 9.290  -27.498 22.543 1.00 20.53 ? 48  GLN   C C   1 
ATOM   1426 O  O   . GLN   B 1 42  ? 8.887  -28.305 21.698 1.00 21.56 ? 48  GLN   C O   1 
ATOM   1427 C  CB  . GLN   B 1 42  ? 8.058  -27.751 24.720 1.00 25.13 ? 48  GLN   C CB  1 
ATOM   1428 C  CG  . GLN   B 1 42  ? 7.426  -27.009 25.901 1.00 33.42 ? 48  GLN   C CG  1 
ATOM   1429 C  CD  . GLN   B 1 42  ? 7.263  -27.954 27.056 1.00 42.66 ? 48  GLN   C CD  1 
ATOM   1430 O  OE1 . GLN   B 1 42  ? 6.367  -28.807 27.067 1.00 46.45 ? 48  GLN   C OE1 1 
ATOM   1431 N  NE2 . GLN   B 1 42  ? 8.126  -27.836 28.054 1.00 44.86 ? 48  GLN   C NE2 1 
ATOM   1432 N  N   . GLY   B 1 43  ? 10.562 -27.129 22.652 1.00 18.36 ? 49  GLY   C N   1 
ATOM   1433 C  CA  . GLY   B 1 43  ? 11.648 -27.696 21.855 1.00 17.66 ? 49  GLY   C CA  1 
ATOM   1434 C  C   . GLY   B 1 43  ? 12.331 -28.819 22.618 1.00 17.51 ? 49  GLY   C C   1 
ATOM   1435 O  O   . GLY   B 1 43  ? 12.136 -28.963 23.828 1.00 19.86 ? 49  GLY   C O   1 
ATOM   1436 N  N   . CYS   B 1 44  ? 13.164 -29.577 21.938 1.00 15.54 ? 50  CYS   C N   1 
ATOM   1437 C  CA  . CYS   B 1 44  ? 13.750 -30.776 22.531 1.00 16.74 ? 50  CYS   C CA  1 
ATOM   1438 C  C   . CYS   B 1 44  ? 15.247 -30.821 22.564 1.00 16.87 ? 50  CYS   C C   1 
ATOM   1439 O  O   . CYS   B 1 44  ? 15.805 -31.874 22.921 1.00 19.14 ? 50  CYS   C O   1 
ATOM   1440 C  CB  . CYS   B 1 44  ? 13.200 -31.993 21.802 1.00 17.44 ? 50  CYS   C CB  1 
ATOM   1441 S  SG  . CYS   B 1 44  ? 11.386 -32.092 21.860 1.00 22.76 ? 50  CYS   C SG  1 
ATOM   1442 N  N   . ASP   B 1 45  ? 15.929 -29.765 22.145 1.00 14.18 ? 51  ASP   C N   1 
ATOM   1443 C  CA  . ASP   B 1 45  ? 17.382 -29.758 22.179 1.00 13.90 ? 51  ASP   C CA  1 
ATOM   1444 C  C   . ASP   B 1 45  ? 17.793 -29.566 23.648 1.00 15.32 ? 51  ASP   C C   1 
ATOM   1445 O  O   . ASP   B 1 45  ? 17.093 -28.889 24.428 1.00 17.65 ? 51  ASP   C O   1 
ATOM   1446 C  CB  . ASP   B 1 45  ? 17.945 -28.601 21.327 1.00 14.99 ? 51  ASP   C CB  1 
ATOM   1447 C  CG  . ASP   B 1 45  ? 17.747 -28.779 19.838 1.00 17.74 ? 51  ASP   C CG  1 
ATOM   1448 O  OD1 . ASP   B 1 45  ? 17.740 -29.933 19.368 1.00 18.81 ? 51  ASP   C OD1 1 
ATOM   1449 O  OD2 . ASP   B 1 45  ? 17.612 -27.758 19.124 1.00 15.92 ? 51  ASP   C OD2 1 
ATOM   1450 N  N   . THR   B 1 46  ? 18.923 -30.167 24.004 1.00 13.82 ? 52  THR   C N   1 
ATOM   1451 C  CA  . THR   B 1 46  ? 19.530 -30.011 25.314 1.00 13.84 ? 52  THR   C CA  1 
ATOM   1452 C  C   . THR   B 1 46  ? 20.793 -29.157 25.131 1.00 13.44 ? 52  THR   C C   1 
ATOM   1453 O  O   . THR   B 1 46  ? 21.616 -29.449 24.244 1.00 14.08 ? 52  THR   C O   1 
ATOM   1454 C  CB  . THR   B 1 46  ? 19.928 -31.381 25.880 1.00 16.45 ? 52  THR   C CB  1 
ATOM   1455 O  OG1 . THR   B 1 46  ? 18.727 -32.161 26.090 1.00 18.58 ? 52  THR   C OG1 1 
ATOM   1456 C  CG2 . THR   B 1 46  ? 20.706 -31.252 27.211 1.00 18.46 ? 52  THR   C CG2 1 
ATOM   1457 N  N   . ILE   B 1 47  ? 20.963 -28.128 25.979 1.00 13.07 ? 53  ILE   C N   1 
ATOM   1458 C  CA  . ILE   B 1 47  ? 22.175 -27.312 25.923 1.00 12.98 ? 53  ILE   C CA  1 
ATOM   1459 C  C   . ILE   B 1 47  ? 23.272 -27.975 26.754 1.00 12.19 ? 53  ILE   C C   1 
ATOM   1460 O  O   . ILE   B 1 47  ? 23.040 -28.407 27.899 1.00 13.37 ? 53  ILE   C O   1 
ATOM   1461 C  CB  . ILE   B 1 47  ? 21.912 -25.925 26.528 1.00 14.18 ? 53  ILE   C CB  1 
ATOM   1462 C  CG1 . ILE   B 1 47  ? 20.720 -25.234 25.868 1.00 15.51 ? 53  ILE   C CG1 1 
ATOM   1463 C  CG2 . ILE   B 1 47  ? 23.173 -25.067 26.422 1.00 14.91 ? 53  ILE   C CG2 1 
ATOM   1464 C  CD1 . ILE   B 1 47  ? 20.867 -25.111 24.309 1.00 17.57 ? 53  ILE   C CD1 1 
ATOM   1465 N  N   . ALA   B 1 48  ? 24.497 -28.045 26.184 1.00 11.44 ? 54  ALA   C N   1 
ATOM   1466 C  CA  . ALA   B 1 48  ? 25.621 -28.590 26.939 1.00 11.56 ? 54  ALA   C CA  1 
ATOM   1467 C  C   . ALA   B 1 48  ? 25.980 -27.664 28.105 1.00 11.52 ? 54  ALA   C C   1 
ATOM   1468 O  O   . ALA   B 1 48  ? 25.949 -26.434 27.959 1.00 11.95 ? 54  ALA   C O   1 
ATOM   1469 C  CB  . ALA   B 1 48  ? 26.822 -28.682 26.032 1.00 11.37 ? 54  ALA   C CB  1 
ATOM   1470 N  N   . ARG   B 1 49  ? 26.345 -28.252 29.266 1.00 11.46 ? 55  ARG   C N   1 
ATOM   1471 C  CA  . ARG   B 1 49  ? 26.785 -27.494 30.438 1.00 11.98 ? 55  ARG   C CA  1 
ATOM   1472 C  C   . ARG   B 1 49  ? 28.112 -28.147 30.820 1.00 12.06 ? 55  ARG   C C   1 
ATOM   1473 O  O   . ARG   B 1 49  ? 28.148 -29.179 31.510 1.00 13.33 ? 55  ARG   C O   1 
ATOM   1474 C  CB  . ARG   B 1 49  ? 25.749 -27.531 31.568 1.00 13.21 ? 55  ARG   C CB  1 
ATOM   1475 C  CG  . ARG   B 1 49  ? 24.373 -26.990 31.143 1.00 12.64 ? 55  ARG   C CG  1 
ATOM   1476 C  CD  . ARG   B 1 49  ? 24.388 -25.507 30.775 1.00 14.14 ? 55  ARG   C CD  1 
ATOM   1477 N  NE  . ARG   B 1 49  ? 23.032 -25.069 30.417 1.00 13.91 ? 55  ARG   C NE  1 
ATOM   1478 C  CZ  . ARG   B 1 49  ? 22.773 -23.971 29.701 1.00 14.40 ? 55  ARG   C CZ  1 
ATOM   1479 N  NH1 . ARG   B 1 49  ? 23.749 -23.141 29.369 1.00 13.52 ? 55  ARG   C NH1 1 
ATOM   1480 N  NH2 . ARG   B 1 49  ? 21.516 -23.673 29.348 1.00 15.80 ? 55  ARG   C NH2 1 
ATOM   1481 N  N   . CYS   B 1 50  ? 29.185 -27.569 30.294 1.00 12.01 ? 56  CYS   C N   1 
ATOM   1482 C  CA  . CYS   B 1 50  ? 30.517 -28.200 30.336 1.00 11.64 ? 56  CYS   C CA  1 
ATOM   1483 C  C   . CYS   B 1 50  ? 31.583 -27.226 29.842 1.00 11.86 ? 56  CYS   C C   1 
ATOM   1484 O  O   . CYS   B 1 50  ? 31.274 -26.118 29.362 1.00 12.73 ? 56  CYS   C O   1 
ATOM   1485 C  CB  . CYS   B 1 50  ? 30.490 -29.419 29.405 1.00 11.38 ? 56  CYS   C CB  1 
ATOM   1486 S  SG  . CYS   B 1 50  ? 30.354 -28.984 27.629 1.00 12.19 ? 56  CYS   C SG  1 
ATOM   1487 N  N   . ASP   B 1 51  ? 32.870 -27.687 29.859 1.00 12.83 ? 57  ASP   C N   1 
ATOM   1488 C  CA  . ASP   B 1 51  ? 33.985 -26.941 29.261 1.00 13.57 ? 57  ASP   C CA  1 
ATOM   1489 C  C   . ASP   B 1 51  ? 34.668 -27.806 28.164 1.00 14.00 ? 57  ASP   C C   1 
ATOM   1490 O  O   . ASP   B 1 51  ? 35.876 -27.645 27.894 1.00 15.24 ? 57  ASP   C O   1 
ATOM   1491 C  CB  . ASP   B 1 51  ? 35.007 -26.505 30.326 1.00 16.43 ? 57  ASP   C CB  1 
ATOM   1492 C  CG  . ASP   B 1 51  ? 35.701 -27.632 31.038 1.00 21.20 ? 57  ASP   C CG  1 
ATOM   1493 O  OD1 . ASP   B 1 51  ? 35.349 -28.799 30.791 1.00 20.39 ? 57  ASP   C OD1 1 
ATOM   1494 O  OD2 . ASP   B 1 51  ? 36.637 -27.339 31.856 1.00 27.93 ? 57  ASP   C OD2 1 
ATOM   1495 N  N   . CYS   B 1 52  ? 33.902 -28.670 27.465 1.00 12.93 ? 58  CYS   C N   1 
ATOM   1496 C  CA  . CYS   B 1 52  ? 34.476 -29.458 26.343 1.00 12.34 ? 58  CYS   C CA  1 
ATOM   1497 C  C   . CYS   B 1 52  ? 35.146 -28.555 25.316 1.00 11.90 ? 58  CYS   C C   1 
ATOM   1498 O  O   . CYS   B 1 52  ? 34.695 -27.420 25.082 1.00 12.47 ? 58  CYS   C O   1 
ATOM   1499 C  CB  . CYS   B 1 52  ? 33.396 -30.277 25.628 1.00 13.03 ? 58  CYS   C CB  1 
ATOM   1500 S  SG  . CYS   B 1 52  ? 32.795 -31.699 26.551 1.00 12.88 ? 58  CYS   C SG  1 
ATOM   1501 N  N   . GLN   B 1 53  ? 36.209 -29.072 24.711 1.00 11.38 ? 59  GLN   C N   1 
ATOM   1502 C  CA  . GLN   B 1 53  ? 36.883 -28.450 23.572 1.00 12.56 ? 59  GLN   C CA  1 
ATOM   1503 C  C   . GLN   B 1 53  ? 36.929 -29.402 22.389 1.00 12.18 ? 59  GLN   C C   1 
ATOM   1504 O  O   . GLN   B 1 53  ? 37.693 -29.153 21.444 1.00 12.49 ? 59  GLN   C O   1 
ATOM   1505 C  CB  . GLN   B 1 53  ? 38.311 -27.975 23.917 1.00 13.28 ? 59  GLN   C CB  1 
ATOM   1506 C  CG  . GLN   B 1 53  ? 38.262 -26.761 24.841 1.00 16.43 ? 59  GLN   C CG  1 
ATOM   1507 C  CD  . GLN   B 1 53  ? 39.637 -26.186 25.033 1.00 20.10 ? 59  GLN   C CD  1 
ATOM   1508 O  OE1 . GLN   B 1 53  ? 40.158 -26.207 26.164 1.00 21.39 ? 59  GLN   C OE1 1 
ATOM   1509 N  NE2 . GLN   B 1 53  ? 40.240 -25.651 23.956 1.00 17.61 ? 59  GLN   C NE2 1 
ATOM   1510 N  N   . THR   B 1 54  ? 36.144 -30.503 22.398 1.00 11.53 ? 60  THR   C N   1 
ATOM   1511 C  CA  . THR   B 1 54  ? 36.041 -31.344 21.211 1.00 12.31 ? 60  THR   C CA  1 
ATOM   1512 C  C   . THR   B 1 54  ? 34.566 -31.624 20.978 1.00 12.09 ? 60  THR   C C   1 
ATOM   1513 O  O   . THR   B 1 54  ? 33.777 -31.727 21.920 1.00 12.30 ? 60  THR   C O   1 
ATOM   1514 C  CB  . THR   B 1 54  ? 36.798 -32.647 21.298 1.00 15.61 ? 60  THR   C CB  1 
ATOM   1515 O  OG1 . THR   B 1 54  ? 36.240 -33.412 22.340 1.00 19.39 ? 60  THR   C OG1 1 
ATOM   1516 C  CG2 . THR   B 1 54  ? 38.284 -32.423 21.561 1.00 15.37 ? 60  THR   C CG2 1 
ATOM   1517 N  N   . GLY   B 1 55  ? 34.181 -31.694 19.701 1.00 11.24 ? 61  GLY   C N   1 
ATOM   1518 C  CA  . GLY   B 1 55  ? 32.776 -31.937 19.355 1.00 11.50 ? 61  GLY   C CA  1 
ATOM   1519 C  C   . GLY   B 1 55  ? 32.639 -32.125 17.859 1.00 10.45 ? 61  GLY   C C   1 
ATOM   1520 O  O   . GLY   B 1 55  ? 33.630 -32.438 17.185 1.00 11.29 ? 61  GLY   C O   1 
ATOM   1521 N  N   . VAL   B 1 56  ? 31.400 -32.015 17.383 1.00 9.80  ? 62  VAL   C N   1 
ATOM   1522 C  CA  . VAL   B 1 56  ? 31.112 -32.223 15.957 1.00 8.54  ? 62  VAL   C CA  1 
ATOM   1523 C  C   . VAL   B 1 56  ? 30.211 -31.100 15.513 1.00 8.59  ? 62  VAL   C C   1 
ATOM   1524 O  O   . VAL   B 1 56  ? 29.251 -30.786 16.212 1.00 10.21 ? 62  VAL   C O   1 
ATOM   1525 C  CB  . VAL   B 1 56  ? 30.387 -33.586 15.788 1.00 9.34  ? 62  VAL   C CB  1 
ATOM   1526 C  CG1 . VAL   B 1 56  ? 29.916 -33.775 14.333 1.00 11.52 ? 62  VAL   C CG1 1 
ATOM   1527 C  CG2 . VAL   B 1 56  ? 31.316 -34.749 16.208 1.00 10.88 ? 62  VAL   C CG2 1 
ATOM   1528 N  N   . TYR   B 1 57  ? 30.470 -30.514 14.323 1.00 9.34  ? 63  TYR   C N   1 
ATOM   1529 C  CA  . TYR   B 1 57  ? 29.566 -29.444 13.820 1.00 8.11  ? 63  TYR   C CA  1 
ATOM   1530 C  C   . TYR   B 1 57  ? 29.019 -29.792 12.440 1.00 8.95  ? 63  TYR   C C   1 
ATOM   1531 O  O   . TYR   B 1 57  ? 29.666 -30.500 11.683 1.00 10.29 ? 63  TYR   C O   1 
ATOM   1532 C  CB  . TYR   B 1 57  ? 30.241 -28.035 13.794 1.00 9.22  ? 63  TYR   C CB  1 
ATOM   1533 C  CG  . TYR   B 1 57  ? 31.114 -27.724 12.589 1.00 9.24  ? 63  TYR   C CG  1 
ATOM   1534 C  CD1 . TYR   B 1 57  ? 32.403 -28.221 12.495 1.00 10.98 ? 63  TYR   C CD1 1 
ATOM   1535 C  CD2 . TYR   B 1 57  ? 30.651 -26.901 11.561 1.00 9.94  ? 63  TYR   C CD2 1 
ATOM   1536 C  CE1 . TYR   B 1 57  ? 33.222 -27.917 11.411 1.00 11.46 ? 63  TYR   C CE1 1 
ATOM   1537 C  CE2 . TYR   B 1 57  ? 31.471 -26.568 10.481 1.00 10.72 ? 63  TYR   C CE2 1 
ATOM   1538 C  CZ  . TYR   B 1 57  ? 32.745 -27.098 10.399 1.00 11.49 ? 63  TYR   C CZ  1 
ATOM   1539 O  OH  . TYR   B 1 57  ? 33.594 -26.777 9.339  1.00 13.45 ? 63  TYR   C OH  1 
ATOM   1540 N  N   . TYR   B 1 58  ? 27.836 -29.227 12.155 1.00 9.47  ? 64  TYR   C N   1 
ATOM   1541 C  CA  . TYR   B 1 58  ? 27.227 -29.408 10.837 1.00 9.68  ? 64  TYR   C CA  1 
ATOM   1542 C  C   . TYR   B 1 58  ? 27.617 -28.273 9.909  1.00 10.51 ? 64  TYR   C C   1 
ATOM   1543 O  O   . TYR   B 1 58  ? 27.375 -27.086 10.224 1.00 10.82 ? 64  TYR   C O   1 
ATOM   1544 C  CB  . TYR   B 1 58  ? 25.694 -29.504 10.930 1.00 10.42 ? 64  TYR   C CB  1 
ATOM   1545 C  CG  . TYR   B 1 58  ? 25.106 -29.783 9.558  1.00 11.52 ? 64  TYR   C CG  1 
ATOM   1546 C  CD1 . TYR   B 1 58  ? 25.441 -30.938 8.863  1.00 12.13 ? 64  TYR   C CD1 1 
ATOM   1547 C  CD2 . TYR   B 1 58  ? 24.220 -28.899 8.965  1.00 11.92 ? 64  TYR   C CD2 1 
ATOM   1548 C  CE1 . TYR   B 1 58  ? 24.924 -31.199 7.590  1.00 12.57 ? 64  TYR   C CE1 1 
ATOM   1549 C  CE2 . TYR   B 1 58  ? 23.700 -29.150 7.690  1.00 12.64 ? 64  TYR   C CE2 1 
ATOM   1550 C  CZ  . TYR   B 1 58  ? 24.054 -30.309 7.026  1.00 13.09 ? 64  TYR   C CZ  1 
ATOM   1551 O  OH  . TYR   B 1 58  ? 23.592 -30.587 5.746  1.00 15.81 ? 64  TYR   C OH  1 
ATOM   1552 N  N   . CYS   B 1 59  ? 28.139 -28.637 8.735  1.00 9.99  ? 65  CYS   C N   1 
ATOM   1553 C  CA  . CYS   B 1 59  ? 28.528 -27.689 7.682  1.00 9.91  ? 65  CYS   C CA  1 
ATOM   1554 C  C   . CYS   B 1 59  ? 27.579 -27.884 6.456  1.00 11.19 ? 65  CYS   C C   1 
ATOM   1555 O  O   . CYS   B 1 59  ? 27.757 -28.830 5.674  1.00 11.97 ? 65  CYS   C O   1 
ATOM   1556 C  CB  . CYS   B 1 59  ? 29.965 -27.963 7.281  1.00 10.28 ? 65  CYS   C CB  1 
ATOM   1557 S  SG  . CYS   B 1 59  ? 30.549 -26.910 5.933  1.00 13.32 ? 65  CYS   C SG  1 
ATOM   1558 N  N   . SER   B 1 60  ? 26.555 -27.036 6.336  1.00 12.46 ? 66  SER   C N   1 
ATOM   1559 C  CA  . SER   B 1 60  ? 25.573 -27.186 5.261  1.00 13.17 ? 66  SER   C CA  1 
ATOM   1560 C  C   . SER   B 1 60  ? 26.180 -27.129 3.860  1.00 13.21 ? 66  SER   C C   1 
ATOM   1561 O  O   . SER   B 1 60  ? 25.767 -27.906 2.983  1.00 14.71 ? 66  SER   C O   1 
ATOM   1562 C  CB  . SER   B 1 60  ? 24.452 -26.164 5.419  1.00 15.99 ? 66  SER   C CB  1 
ATOM   1563 O  OG  . SER   B 1 60  ? 23.511 -26.398 4.382  1.00 20.81 ? 66  SER   C OG  1 
ATOM   1564 N  N   . SER   B 1 61  ? 27.200 -26.282 3.676  1.00 12.44 ? 67  SER   C N   1 
ATOM   1565 C  CA  . SER   B 1 61  ? 27.834 -26.143 2.349  1.00 13.34 ? 67  SER   C CA  1 
ATOM   1566 C  C   . SER   B 1 61  ? 28.645 -27.354 1.901  1.00 15.16 ? 67  SER   C C   1 
ATOM   1567 O  O   . SER   B 1 61  ? 28.987 -27.464 0.713  1.00 17.35 ? 67  SER   C O   1 
ATOM   1568 C  CB  . SER   B 1 61  ? 28.689 -24.888 2.266  1.00 14.76 ? 67  SER   C CB  1 
ATOM   1569 O  OG  . SER   B 1 61  ? 29.795 -24.955 3.137  1.00 15.45 ? 67  SER   C OG  1 
ATOM   1570 N  N   . ARG   B 1 62  ? 28.887 -28.312 2.817  1.00 13.33 ? 68  ARG   C N   1 
ATOM   1571 C  CA  . ARG   B 1 62  ? 29.537 -29.575 2.455  1.00 14.16 ? 68  ARG   C CA  1 
ATOM   1572 C  C   . ARG   B 1 62  ? 28.585 -30.760 2.694  1.00 14.05 ? 68  ARG   C C   1 
ATOM   1573 O  O   . ARG   B 1 62  ? 28.981 -31.923 2.506  1.00 15.06 ? 68  ARG   C O   1 
ATOM   1574 C  CB  . ARG   B 1 62  ? 30.809 -29.752 3.305  1.00 15.10 ? 68  ARG   C CB  1 
ATOM   1575 C  CG  . ARG   B 1 62  ? 31.864 -28.676 3.039  1.00 18.31 ? 68  ARG   C CG  1 
ATOM   1576 C  CD  . ARG   B 1 62  ? 32.537 -28.915 1.720  1.00 18.67 ? 68  ARG   C CD  1 
ATOM   1577 N  NE  . ARG   B 1 62  ? 33.561 -27.889 1.423  1.00 22.48 ? 68  ARG   C NE  1 
ATOM   1578 C  CZ  . ARG   B 1 62  ? 33.339 -26.749 0.767  1.00 26.80 ? 68  ARG   C CZ  1 
ATOM   1579 N  NH1 . ARG   B 1 62  ? 32.118 -26.442 0.341  1.00 28.29 ? 68  ARG   C NH1 1 
ATOM   1580 N  NH2 . ARG   B 1 62  ? 34.347 -25.917 0.501  1.00 27.00 ? 68  ARG   C NH2 1 
ATOM   1581 N  N   . ARG   B 1 63  ? 27.360 -30.513 3.214  1.00 13.90 ? 69  ARG   C N   1 
ATOM   1582 C  CA  . ARG   B 1 63  ? 26.425 -31.576 3.655  1.00 14.87 ? 69  ARG   C CA  1 
ATOM   1583 C  C   . ARG   B 1 63  ? 27.126 -32.599 4.543  1.00 15.63 ? 69  ARG   C C   1 
ATOM   1584 O  O   . ARG   B 1 63  ? 26.968 -33.824 4.363  1.00 17.69 ? 69  ARG   C O   1 
ATOM   1585 C  CB  . ARG   B 1 63  ? 25.791 -32.265 2.434  1.00 16.45 ? 69  ARG   C CB  1 
ATOM   1586 C  CG  . ARG   B 1 63  ? 24.897 -31.362 1.621  1.00 18.88 ? 69  ARG   C CG  1 
ATOM   1587 C  CD  . ARG   B 1 63  ? 23.643 -30.984 2.330  1.00 23.57 ? 69  ARG   C CD  1 
ATOM   1588 N  NE  . ARG   B 1 63  ? 22.642 -30.510 1.374  1.00 27.20 ? 69  ARG   C NE  1 
ATOM   1589 C  CZ  . ARG   B 1 63  ? 22.459 -29.236 1.057  1.00 28.92 ? 69  ARG   C CZ  1 
ATOM   1590 N  NH1 . ARG   B 1 63  ? 23.224 -28.290 1.596  1.00 26.93 ? 69  ARG   C NH1 1 
ATOM   1591 N  NH2 . ARG   B 1 63  ? 21.503 -28.891 0.205  1.00 29.49 ? 69  ARG   C NH2 1 
ATOM   1592 N  N   . LYS   B 1 64  ? 27.933 -32.087 5.490  1.00 14.24 ? 70  LYS   C N   1 
ATOM   1593 C  CA  . LYS   B 1 64  ? 28.730 -32.998 6.305  1.00 14.51 ? 70  LYS   C CA  1 
ATOM   1594 C  C   . LYS   B 1 64  ? 28.861 -32.519 7.716  1.00 13.06 ? 70  LYS   C C   1 
ATOM   1595 O  O   . LYS   B 1 64  ? 28.876 -31.311 7.980  1.00 13.03 ? 70  LYS   C O   1 
ATOM   1596 C  CB  . LYS   B 1 64  ? 30.147 -33.073 5.715  1.00 18.96 ? 70  LYS   C CB  1 
ATOM   1597 C  CG  . LYS   B 1 64  ? 30.264 -34.089 4.573  1.00 28.42 ? 70  LYS   C CG  1 
ATOM   1598 C  CD  . LYS   B 1 64  ? 31.707 -34.468 4.296  1.00 36.87 ? 70  LYS   C CD  1 
ATOM   1599 C  CE  . LYS   B 1 64  ? 31.801 -35.275 3.026  1.00 42.54 ? 70  LYS   C CE  1 
ATOM   1600 N  NZ  . LYS   B 1 64  ? 31.204 -34.548 1.872  1.00 46.52 ? 70  LYS   C NZ  1 
ATOM   1601 N  N   . HIS   B 1 65  ? 28.950 -33.477 8.629  1.00 11.83 ? 71  HIS   C N   1 
ATOM   1602 C  CA  . HIS   B 1 65  ? 29.268 -33.213 10.035 1.00 11.53 ? 71  HIS   C CA  1 
ATOM   1603 C  C   . HIS   B 1 65  ? 30.750 -33.480 10.217 1.00 13.29 ? 71  HIS   C C   1 
ATOM   1604 O  O   . HIS   B 1 65  ? 31.260 -34.557 9.844  1.00 16.23 ? 71  HIS   C O   1 
ATOM   1605 C  CB  . HIS   B 1 65  ? 28.448 -34.104 10.986 1.00 12.18 ? 71  HIS   C CB  1 
ATOM   1606 C  CG  . HIS   B 1 65  ? 26.977 -33.823 10.946 1.00 11.71 ? 71  HIS   C CG  1 
ATOM   1607 N  ND1 . HIS   B 1 65  ? 26.333 -33.039 11.885 1.00 14.78 ? 71  HIS   C ND1 1 
ATOM   1608 C  CD2 . HIS   B 1 65  ? 26.062 -34.248 10.037 1.00 11.59 ? 71  HIS   C CD2 1 
ATOM   1609 C  CE1 . HIS   B 1 65  ? 25.040 -33.058 11.559 1.00 13.16 ? 71  HIS   C CE1 1 
ATOM   1610 N  NE2 . HIS   B 1 65  ? 24.824 -33.772 10.464 1.00 14.63 ? 71  HIS   C NE2 1 
ATOM   1611 N  N   . TYR   B 1 66  ? 31.492 -32.495 10.792 1.00 11.07 ? 72  TYR   C N   1 
ATOM   1612 C  CA  . TYR   B 1 66  ? 32.940 -32.676 10.955 1.00 10.75 ? 72  TYR   C CA  1 
ATOM   1613 C  C   . TYR   B 1 66  ? 33.321 -32.721 12.427 1.00 10.52 ? 72  TYR   C C   1 
ATOM   1614 O  O   . TYR   B 1 66  ? 32.879 -31.856 13.201 1.00 10.62 ? 72  TYR   C O   1 
ATOM   1615 C  CB  . TYR   B 1 66  ? 33.695 -31.453 10.377 1.00 11.99 ? 72  TYR   C CB  1 
ATOM   1616 C  CG  . TYR   B 1 66  ? 33.657 -31.365 8.861  1.00 12.72 ? 72  TYR   C CG  1 
ATOM   1617 C  CD1 . TYR   B 1 66  ? 34.530 -32.108 8.084  1.00 14.80 ? 72  TYR   C CD1 1 
ATOM   1618 C  CD2 . TYR   B 1 66  ? 32.856 -30.431 8.210  1.00 13.72 ? 72  TYR   C CD2 1 
ATOM   1619 C  CE1 . TYR   B 1 66  ? 34.531 -32.002 6.691  1.00 15.63 ? 72  TYR   C CE1 1 
ATOM   1620 C  CE2 . TYR   B 1 66  ? 32.840 -30.322 6.825  1.00 14.42 ? 72  TYR   C CE2 1 
ATOM   1621 C  CZ  . TYR   B 1 66  ? 33.705 -31.084 6.072  1.00 15.10 ? 72  TYR   C CZ  1 
ATOM   1622 O  OH  . TYR   B 1 66  ? 33.676 -30.935 4.696  1.00 17.78 ? 72  TYR   C OH  1 
ATOM   1623 N  N   . PRO   B 1 67  ? 34.139 -33.699 12.837 1.00 10.93 ? 73  PRO   C N   1 
ATOM   1624 C  CA  . PRO   B 1 67  ? 34.650 -33.672 14.225 1.00 10.83 ? 73  PRO   C CA  1 
ATOM   1625 C  C   . PRO   B 1 67  ? 35.739 -32.580 14.317 1.00 11.99 ? 73  PRO   C C   1 
ATOM   1626 O  O   . PRO   B 1 67  ? 36.629 -32.507 13.439 1.00 14.42 ? 73  PRO   C O   1 
ATOM   1627 C  CB  . PRO   B 1 67  ? 35.277 -35.071 14.425 1.00 12.93 ? 73  PRO   C CB  1 
ATOM   1628 C  CG  . PRO   B 1 67  ? 35.458 -35.616 13.051 1.00 14.94 ? 73  PRO   C CG  1 
ATOM   1629 C  CD  . PRO   B 1 67  ? 34.638 -34.855 12.051 1.00 11.57 ? 73  PRO   C CD  1 
ATOM   1630 N  N   . VAL   B 1 68  ? 35.719 -31.789 15.381 1.00 10.43 ? 74  VAL   C N   1 
ATOM   1631 C  CA  . VAL   B 1 68  ? 36.693 -30.698 15.519 1.00 10.72 ? 74  VAL   C CA  1 
ATOM   1632 C  C   . VAL   B 1 68  ? 37.076 -30.513 16.969 1.00 10.98 ? 74  VAL   C C   1 
ATOM   1633 O  O   . VAL   B 1 68  ? 36.322 -30.790 17.893 1.00 11.49 ? 74  VAL   C O   1 
ATOM   1634 C  CB  . VAL   B 1 68  ? 36.084 -29.329 15.017 1.00 12.53 ? 74  VAL   C CB  1 
ATOM   1635 C  CG1 . VAL   B 1 68  ? 36.030 -29.254 13.475 1.00 14.89 ? 74  VAL   C CG1 1 
ATOM   1636 C  CG2 . VAL   B 1 68  ? 34.710 -29.044 15.679 1.00 13.39 ? 74  VAL   C CG2 1 
ATOM   1637 N  N   . SER   B 1 69  ? 38.286 -29.949 17.139 1.00 10.60 ? 75  SER   C N   1 
ATOM   1638 C  CA  . SER   B 1 69  ? 38.739 -29.318 18.391 1.00 11.53 ? 75  SER   C CA  1 
ATOM   1639 C  C   . SER   B 1 69  ? 38.432 -27.818 18.259 1.00 10.79 ? 75  SER   C C   1 
ATOM   1640 O  O   . SER   B 1 69  ? 38.556 -27.219 17.167 1.00 11.05 ? 75  SER   C O   1 
ATOM   1641 C  CB  . SER   B 1 69  ? 40.250 -29.479 18.538 1.00 14.36 ? 75  SER   C CB  1 
ATOM   1642 O  OG  . SER   B 1 69  ? 40.529 -30.857 18.684 1.00 18.59 ? 75  SER   C OG  1 
ATOM   1643 N  N   . PHE   B 1 70  ? 37.962 -27.208 19.330 1.00 10.49 ? 76  PHE   C N   1 
ATOM   1644 C  CA  . PHE   B 1 70  ? 37.589 -25.788 19.300 1.00 10.47 ? 76  PHE   C CA  1 
ATOM   1645 C  C   . PHE   B 1 70  ? 38.070 -25.059 20.550 1.00 10.81 ? 76  PHE   C C   1 
ATOM   1646 O  O   . PHE   B 1 70  ? 38.258 -25.679 21.601 1.00 11.80 ? 76  PHE   C O   1 
ATOM   1647 C  CB  . PHE   B 1 70  ? 36.067 -25.565 19.061 1.00 11.32 ? 76  PHE   C CB  1 
ATOM   1648 C  CG  . PHE   B 1 70  ? 35.177 -26.284 20.056 1.00 10.65 ? 76  PHE   C CG  1 
ATOM   1649 C  CD1 . PHE   B 1 70  ? 34.758 -27.584 19.828 1.00 11.02 ? 76  PHE   C CD1 1 
ATOM   1650 C  CD2 . PHE   B 1 70  ? 34.729 -25.636 21.191 1.00 11.16 ? 76  PHE   C CD2 1 
ATOM   1651 C  CE1 . PHE   B 1 70  ? 33.953 -28.241 20.758 1.00 11.45 ? 76  PHE   C CE1 1 
ATOM   1652 C  CE2 . PHE   B 1 70  ? 33.867 -26.281 22.080 1.00 11.39 ? 76  PHE   C CE2 1 
ATOM   1653 C  CZ  . PHE   B 1 70  ? 33.509 -27.574 21.870 1.00 11.37 ? 76  PHE   C CZ  1 
ATOM   1654 N  N   . SER   B 1 71  ? 38.341 -23.775 20.409 1.00 10.76 ? 77  SER   C N   1 
ATOM   1655 C  CA  . SER   B 1 71  ? 38.939 -22.996 21.496 1.00 11.76 ? 77  SER   C CA  1 
ATOM   1656 C  C   . SER   B 1 71  ? 37.951 -22.603 22.577 1.00 12.60 ? 77  SER   C C   1 
ATOM   1657 O  O   . SER   B 1 71  ? 36.754 -22.875 22.486 1.00 13.56 ? 77  SER   C O   1 
ATOM   1658 C  CB  . SER   B 1 71  ? 39.656 -21.783 20.904 1.00 12.40 ? 77  SER   C CB  1 
ATOM   1659 O  OG  . SER   B 1 71  ? 38.755 -20.887 20.258 1.00 14.68 ? 77  SER   C OG  1 
ATOM   1660 N  N   . LYS   B 1 72  ? 38.453 -21.983 23.656 1.00 14.03 ? 78  LYS   C N   1 
ATOM   1661 C  CA  . LYS   B 1 72  ? 37.579 -21.543 24.753 1.00 14.00 ? 78  LYS   C CA  1 
ATOM   1662 C  C   . LYS   B 1 72  ? 36.855 -20.248 24.342 1.00 14.26 ? 78  LYS   C C   1 
ATOM   1663 O  O   . LYS   B 1 72  ? 37.430 -19.431 23.609 1.00 15.52 ? 78  LYS   C O   1 
ATOM   1664 C  CB  . LYS   B 1 72  ? 38.442 -21.263 26.008 1.00 17.75 ? 78  LYS   C CB  1 
ATOM   1665 C  CG  . LYS   B 1 72  ? 39.137 -22.514 26.502 1.00 21.15 ? 78  LYS   C CG  1 
ATOM   1666 C  CD  . LYS   B 1 72  ? 39.768 -22.280 27.890 1.00 31.50 ? 78  LYS   C CD  1 
ATOM   1667 C  CE  . LYS   B 1 72  ? 40.434 -23.539 28.422 1.00 39.99 ? 78  LYS   C CE  1 
ATOM   1668 N  NZ  . LYS   B 1 72  ? 39.724 -24.124 29.621 1.00 44.62 ? 78  LYS   C NZ  1 
ATOM   1669 N  N   . PRO   B 1 73  ? 35.615 -20.006 24.808 1.00 13.58 ? 79  PRO   C N   1 
ATOM   1670 C  CA  . PRO   B 1 73  ? 34.879 -18.770 24.388 1.00 14.32 ? 79  PRO   C CA  1 
ATOM   1671 C  C   . PRO   B 1 73  ? 35.647 -17.520 24.753 1.00 14.94 ? 79  PRO   C C   1 
ATOM   1672 O  O   . PRO   B 1 73  ? 36.092 -17.376 25.907 1.00 17.08 ? 79  PRO   C O   1 
ATOM   1673 C  CB  . PRO   B 1 73  ? 33.558 -18.818 25.150 1.00 16.15 ? 79  PRO   C CB  1 
ATOM   1674 C  CG  . PRO   B 1 73  ? 33.524 -20.140 25.811 1.00 18.22 ? 79  PRO   C CG  1 
ATOM   1675 C  CD  . PRO   B 1 73  ? 34.837 -20.866 25.725 1.00 14.68 ? 79  PRO   C CD  1 
ATOM   1676 N  N   . SER   B 1 74  ? 35.876 -16.648 23.776 1.00 13.26 ? 80  SER   C N   1 
ATOM   1677 C  CA  . SER   B 1 74  ? 36.739 -15.488 23.986 1.00 14.91 ? 80  SER   C CA  1 
ATOM   1678 C  C   . SER   B 1 74  ? 36.334 -14.328 23.090 1.00 14.83 ? 80  SER   C C   1 
ATOM   1679 O  O   . SER   B 1 74  ? 35.481 -14.471 22.217 1.00 14.23 ? 80  SER   C O   1 
ATOM   1680 C  CB  . SER   B 1 74  ? 38.189 -15.862 23.656 1.00 19.13 ? 80  SER   C CB  1 
ATOM   1681 O  OG  . SER   B 1 74  ? 38.590 -17.091 24.242 1.00 26.59 ? 80  SER   C OG  1 
ATOM   1682 N  N   . LEU   B 1 75  ? 37.009 -13.182 23.275 1.00 15.09 ? 81  LEU   C N   1 
ATOM   1683 C  CA  . LEU   B 1 75  ? 36.825 -11.978 22.465 1.00 16.61 ? 81  LEU   C CA  1 
ATOM   1684 C  C   . LEU   B 1 75  ? 37.837 -12.078 21.309 1.00 17.47 ? 81  LEU   C C   1 
ATOM   1685 O  O   . LEU   B 1 75  ? 39.069 -12.009 21.531 1.00 19.50 ? 81  LEU   C O   1 
ATOM   1686 C  CB  . LEU   B 1 75  ? 37.090 -10.731 23.330 1.00 18.04 ? 81  LEU   C CB  1 
ATOM   1687 C  CG  . LEU   B 1 75  ? 36.793 -9.393  22.677 1.00 20.38 ? 81  LEU   C CG  1 
ATOM   1688 C  CD1 . LEU   B 1 75  ? 35.301 -9.187  22.531 1.00 20.41 ? 81  LEU   C CD1 1 
ATOM   1689 C  CD2 . LEU   B 1 75  ? 37.383 -8.253  23.543 1.00 22.25 ? 81  LEU   C CD2 1 
ATOM   1690 N  N   . ILE   B 1 76  ? 37.341 -12.345 20.100 1.00 16.88 ? 82  ILE   C N   1 
ATOM   1691 C  CA  . ILE   B 1 76  ? 38.176 -12.646 18.920 1.00 18.02 ? 82  ILE   C CA  1 
ATOM   1692 C  C   . ILE   B 1 76  ? 37.951 -11.571 17.846 1.00 18.27 ? 82  ILE   C C   1 
ATOM   1693 O  O   . ILE   B 1 76  ? 36.782 -11.192 17.620 1.00 17.22 ? 82  ILE   C O   1 
ATOM   1694 C  CB  . ILE   B 1 76  ? 37.750 -14.040 18.367 1.00 20.18 ? 82  ILE   C CB  1 
ATOM   1695 C  CG1 . ILE   B 1 76  ? 38.025 -15.197 19.371 1.00 22.72 ? 82  ILE   C CG1 1 
ATOM   1696 C  CG2 . ILE   B 1 76  ? 38.364 -14.361 16.957 1.00 21.56 ? 82  ILE   C CG2 1 
ATOM   1697 C  CD1 . ILE   B 1 76  ? 39.502 -15.607 19.456 1.00 24.99 ? 82  ILE   C CD1 1 
ATOM   1698 N  N   . PHE   B 1 77  ? 39.027 -11.072 17.194 1.00 18.52 ? 83  PHE   C N   1 
ATOM   1699 C  CA  . PHE   B 1 77  ? 38.847 -10.116 16.097 1.00 18.64 ? 83  PHE   C CA  1 
ATOM   1700 C  C   . PHE   B 1 77  ? 38.463 -10.966 14.858 1.00 19.37 ? 83  PHE   C C   1 
ATOM   1701 O  O   . PHE   B 1 77  ? 39.149 -11.949 14.507 1.00 21.50 ? 83  PHE   C O   1 
ATOM   1702 C  CB  . PHE   B 1 77  ? 40.145 -9.324  15.812 1.00 19.11 ? 83  PHE   C CB  1 
ATOM   1703 C  CG  . PHE   B 1 77  ? 39.876 -8.161  14.878 1.00 20.41 ? 83  PHE   C CG  1 
ATOM   1704 C  CD1 . PHE   B 1 77  ? 39.209 -7.032  15.325 1.00 21.65 ? 83  PHE   C CD1 1 
ATOM   1705 C  CD2 . PHE   B 1 77  ? 40.235 -8.225  13.533 1.00 21.77 ? 83  PHE   C CD2 1 
ATOM   1706 C  CE1 . PHE   B 1 77  ? 38.910 -5.979  14.452 1.00 23.41 ? 83  PHE   C CE1 1 
ATOM   1707 C  CE2 . PHE   B 1 77  ? 39.956 -7.165  12.673 1.00 22.45 ? 83  PHE   C CE2 1 
ATOM   1708 C  CZ  . PHE   B 1 77  ? 39.306 -6.046  13.135 1.00 22.75 ? 83  PHE   C CZ  1 
ATOM   1709 N  N   . VAL   B 1 78  ? 37.351 -10.591 14.210 1.00 16.89 ? 84  VAL   C N   1 
ATOM   1710 C  CA  . VAL   B 1 78  ? 36.824 -11.304 13.054 1.00 16.70 ? 84  VAL   C CA  1 
ATOM   1711 C  C   . VAL   B 1 78  ? 36.915 -10.367 11.840 1.00 16.52 ? 84  VAL   C C   1 
ATOM   1712 O  O   . VAL   B 1 78  ? 36.459 -9.233  11.933 1.00 16.59 ? 84  VAL   C O   1 
ATOM   1713 C  CB  . VAL   B 1 78  ? 35.343 -11.686 13.339 1.00 17.39 ? 84  VAL   C CB  1 
ATOM   1714 C  CG1 . VAL   B 1 78  ? 34.774 -12.456 12.158 1.00 18.13 ? 84  VAL   C CG1 1 
ATOM   1715 C  CG2 . VAL   B 1 78  ? 35.206 -12.512 14.630 1.00 17.83 ? 84  VAL   C CG2 1 
ATOM   1716 N  N   . GLU   B 1 79  ? 37.412 -10.848 10.697 1.00 15.57 ? 85  GLU   C N   1 
ATOM   1717 C  CA  . GLU   B 1 79  ? 37.452 -10.047 9.468  1.00 15.67 ? 85  GLU   C CA  1 
ATOM   1718 C  C   . GLU   B 1 79  ? 36.038 -9.774  8.938  1.00 15.41 ? 85  GLU   C C   1 
ATOM   1719 O  O   . GLU   B 1 79  ? 35.074 -10.450 9.313  1.00 14.90 ? 85  GLU   C O   1 
ATOM   1720 C  CB  . GLU   B 1 79  ? 38.280 -10.751 8.378  1.00 18.98 ? 85  GLU   C CB  1 
ATOM   1721 C  CG  . GLU   B 1 79  ? 39.773 -10.757 8.676  1.00 25.22 ? 85  GLU   C CG  1 
ATOM   1722 C  CD  . GLU   B 1 79  ? 40.372 -9.381  8.914  1.00 35.35 ? 85  GLU   C CD  1 
ATOM   1723 O  OE1 . GLU   B 1 79  ? 40.140 -8.465  8.089  1.00 37.88 ? 85  GLU   C OE1 1 
ATOM   1724 O  OE2 . GLU   B 1 79  ? 41.047 -9.204  9.953  1.00 38.82 ? 85  GLU   C OE2 1 
ATOM   1725 N  N   . ALA   B 1 80  ? 35.902 -8.759  8.081  1.00 16.92 ? 86  ALA   C N   1 
ATOM   1726 C  CA  . ALA   B 1 80  ? 34.604 -8.412  7.523  1.00 17.91 ? 86  ALA   C CA  1 
ATOM   1727 C  C   . ALA   B 1 80  ? 33.987 -9.593  6.774  1.00 19.02 ? 86  ALA   C C   1 
ATOM   1728 O  O   . ALA   B 1 80  ? 34.693 -10.369 6.136  1.00 21.03 ? 86  ALA   C O   1 
ATOM   1729 C  CB  . ALA   B 1 80  ? 34.779 -7.247  6.552  1.00 19.24 ? 86  ALA   C CB  1 
ATOM   1730 N  N   . SER   B 1 81  ? 32.682 -9.747  6.929  1.00 18.47 ? 87  SER   C N   1 
ATOM   1731 C  CA  . SER   B 1 81  ? 31.949 -10.780 6.239  1.00 19.17 ? 87  SER   C CA  1 
ATOM   1732 C  C   . SER   B 1 81  ? 30.825 -10.099 5.436  1.00 20.84 ? 87  SER   C C   1 
ATOM   1733 O  O   . SER   B 1 81  ? 30.684 -8.849  5.455  1.00 20.80 ? 87  SER   C O   1 
ATOM   1734 C  CB  . SER   B 1 81  ? 31.368 -11.754 7.262  1.00 18.37 ? 87  SER   C CB  1 
ATOM   1735 O  OG  . SER   B 1 81  ? 30.332 -11.101 7.991  1.00 17.99 ? 87  SER   C OG  1 
ATOM   1736 N  N   . GLU   B 1 82  ? 29.997 -10.909 4.778  1.00 22.25 ? 88  GLU   C N   1 
ATOM   1737 C  CA  . GLU   B 1 82  ? 28.893 -10.304 4.040  1.00 23.06 ? 88  GLU   C CA  1 
ATOM   1738 C  C   . GLU   B 1 82  ? 27.842 -9.668  4.974  1.00 22.45 ? 88  GLU   C C   1 
ATOM   1739 O  O   . GLU   B 1 82  ? 27.080 -8.811  4.528  1.00 23.77 ? 88  GLU   C O   1 
ATOM   1740 C  CB  . GLU   B 1 82  ? 28.288 -11.288 3.034  1.00 27.81 ? 88  GLU   C CB  1 
ATOM   1741 C  CG  . GLU   B 1 82  ? 27.469 -12.413 3.621  1.00 35.06 ? 88  GLU   C CG  1 
ATOM   1742 C  CD  . GLU   B 1 82  ? 26.770 -13.191 2.522  1.00 41.43 ? 88  GLU   C CD  1 
ATOM   1743 O  OE1 . GLU   B 1 82  ? 27.409 -13.424 1.470  1.00 42.07 ? 88  GLU   C OE1 1 
ATOM   1744 O  OE2 . GLU   B 1 82  ? 25.582 -13.547 2.703  1.00 43.58 ? 88  GLU   C OE2 1 
ATOM   1745 N  N   . TYR   B 1 83  ? 27.858 -9.996  6.290  1.00 19.77 ? 89  TYR   C N   1 
ATOM   1746 C  CA  . TYR   B 1 83  ? 26.834 -9.503  7.199  1.00 18.69 ? 89  TYR   C CA  1 
ATOM   1747 C  C   . TYR   B 1 83  ? 27.343 -8.631  8.380  1.00 19.75 ? 89  TYR   C C   1 
ATOM   1748 O  O   . TYR   B 1 83  ? 26.521 -8.043  9.076  1.00 21.04 ? 89  TYR   C O   1 
ATOM   1749 C  CB  . TYR   B 1 83  ? 25.975 -10.699 7.718  1.00 17.65 ? 89  TYR   C CB  1 
ATOM   1750 C  CG  . TYR   B 1 83  ? 26.802 -11.908 8.164  1.00 16.79 ? 89  TYR   C CG  1 
ATOM   1751 C  CD1 . TYR   B 1 83  ? 27.207 -12.883 7.251  1.00 17.01 ? 89  TYR   C CD1 1 
ATOM   1752 C  CD2 . TYR   B 1 83  ? 27.227 -12.039 9.477  1.00 16.25 ? 89  TYR   C CD2 1 
ATOM   1753 C  CE1 . TYR   B 1 83  ? 27.979 -13.977 7.647  1.00 15.82 ? 89  TYR   C CE1 1 
ATOM   1754 C  CE2 . TYR   B 1 83  ? 28.009 -13.116 9.884  1.00 16.86 ? 89  TYR   C CE2 1 
ATOM   1755 C  CZ  . TYR   B 1 83  ? 28.390 -14.087 8.965  1.00 16.00 ? 89  TYR   C CZ  1 
ATOM   1756 O  OH  . TYR   B 1 83  ? 29.182 -15.167 9.332  1.00 17.05 ? 89  TYR   C OH  1 
ATOM   1757 N  N   . TYR   B 1 84  ? 28.669 -8.525  8.615  1.00 17.46 ? 90  TYR   C N   1 
ATOM   1758 C  CA  . TYR   B 1 84  ? 29.208 -7.616  9.665  1.00 16.75 ? 90  TYR   C CA  1 
ATOM   1759 C  C   . TYR   B 1 84  ? 30.533 -6.994  9.163  1.00 16.41 ? 90  TYR   C C   1 
ATOM   1760 O  O   . TYR   B 1 84  ? 31.244 -7.641  8.401  1.00 16.67 ? 90  TYR   C O   1 
ATOM   1761 C  CB  . TYR   B 1 84  ? 29.569 -8.381  10.979 1.00 16.05 ? 90  TYR   C CB  1 
ATOM   1762 C  CG  . TYR   B 1 84  ? 28.398 -8.804  11.836 1.00 14.87 ? 90  TYR   C CG  1 
ATOM   1763 C  CD1 . TYR   B 1 84  ? 27.480 -7.872  12.313 1.00 15.16 ? 90  TYR   C CD1 1 
ATOM   1764 C  CD2 . TYR   B 1 84  ? 28.207 -10.128 12.165 1.00 14.49 ? 90  TYR   C CD2 1 
ATOM   1765 C  CE1 . TYR   B 1 84  ? 26.410 -8.259  13.122 1.00 15.07 ? 90  TYR   C CE1 1 
ATOM   1766 C  CE2 . TYR   B 1 84  ? 27.136 -10.534 12.954 1.00 13.62 ? 90  TYR   C CE2 1 
ATOM   1767 C  CZ  . TYR   B 1 84  ? 26.236 -9.599  13.431 1.00 13.90 ? 90  TYR   C CZ  1 
ATOM   1768 O  OH  . TYR   B 1 84  ? 25.165 -10.010 14.192 1.00 13.62 ? 90  TYR   C OH  1 
ATOM   1769 N  N   . PRO   B 1 85  ? 30.931 -5.808  9.643  1.00 17.07 ? 91  PRO   C N   1 
ATOM   1770 C  CA  . PRO   B 1 85  ? 32.282 -5.298  9.313  1.00 16.30 ? 91  PRO   C CA  1 
ATOM   1771 C  C   . PRO   B 1 85  ? 33.329 -6.083  10.135 1.00 16.66 ? 91  PRO   C C   1 
ATOM   1772 O  O   . PRO   B 1 85  ? 32.977 -6.877  11.033 1.00 16.69 ? 91  PRO   C O   1 
ATOM   1773 C  CB  . PRO   B 1 85  ? 32.205 -3.833  9.806  1.00 17.62 ? 91  PRO   C CB  1 
ATOM   1774 C  CG  . PRO   B 1 85  ? 31.285 -3.913  10.989 1.00 18.57 ? 91  PRO   C CG  1 
ATOM   1775 C  CD  . PRO   B 1 85  ? 30.222 -4.947  10.621 1.00 17.90 ? 91  PRO   C CD  1 
ATOM   1776 N  N   . ALA   B 1 86  ? 34.628 -5.804  9.919  1.00 16.47 ? 92  ALA   C N   1 
ATOM   1777 C  CA  . ALA   B 1 86  ? 35.689 -6.377  10.754 1.00 17.94 ? 92  ALA   C CA  1 
ATOM   1778 C  C   . ALA   B 1 86  ? 35.500 -5.816  12.170 1.00 18.89 ? 92  ALA   C C   1 
ATOM   1779 O  O   . ALA   B 1 86  ? 35.249 -4.608  12.327 1.00 20.49 ? 92  ALA   C O   1 
ATOM   1780 C  CB  . ALA   B 1 86  ? 37.053 -5.960  10.206 1.00 17.62 ? 92  ALA   C CB  1 
ATOM   1781 N  N   . ARG   B 1 87  ? 35.506 -6.698  13.179 1.00 17.72 ? 93  ARG   C N   1 
ATOM   1782 C  CA  . ARG   B 1 87  ? 35.207 -6.255  14.542 1.00 17.96 ? 93  ARG   C CA  1 
ATOM   1783 C  C   . ARG   B 1 87  ? 35.546 -7.344  15.549 1.00 17.32 ? 93  ARG   C C   1 
ATOM   1784 O  O   . ARG   B 1 87  ? 35.792 -8.489  15.168 1.00 16.98 ? 93  ARG   C O   1 
ATOM   1785 C  CB  . ARG   B 1 87  ? 33.690 -5.968  14.669 1.00 18.84 ? 93  ARG   C CB  1 
ATOM   1786 C  CG  . ARG   B 1 87  ? 32.857 -7.238  14.506 1.00 17.43 ? 93  ARG   C CG  1 
ATOM   1787 C  CD  . ARG   B 1 87  ? 31.390 -6.978  14.786 1.00 17.33 ? 93  ARG   C CD  1 
ATOM   1788 N  NE  . ARG   B 1 87  ? 30.669 -8.240  14.967 1.00 17.30 ? 93  ARG   C NE  1 
ATOM   1789 C  CZ  . ARG   B 1 87  ? 29.558 -8.383  15.681 1.00 18.83 ? 93  ARG   C CZ  1 
ATOM   1790 N  NH1 . ARG   B 1 87  ? 28.997 -7.329  16.274 1.00 17.85 ? 93  ARG   C NH1 1 
ATOM   1791 N  NH2 . ARG   B 1 87  ? 29.024 -9.588  15.849 1.00 19.49 ? 93  ARG   C NH2 1 
ATOM   1792 N  N   . TYR   B 1 88  ? 35.499 -6.998  16.845 1.00 18.26 ? 94  TYR   C N   1 
ATOM   1793 C  CA  . TYR   B 1 88  ? 35.638 -8.003  17.890 1.00 19.42 ? 94  TYR   C CA  1 
ATOM   1794 C  C   . TYR   B 1 88  ? 34.266 -8.635  18.164 1.00 17.72 ? 94  TYR   C C   1 
ATOM   1795 O  O   . TYR   B 1 88  ? 33.270 -7.922  18.325 1.00 18.89 ? 94  TYR   C O   1 
ATOM   1796 C  CB  . TYR   B 1 88  ? 36.125 -7.359  19.202 1.00 21.92 ? 94  TYR   C CB  1 
ATOM   1797 C  CG  . TYR   B 1 88  ? 37.589 -7.006  19.122 1.00 24.80 ? 94  TYR   C CG  1 
ATOM   1798 C  CD1 . TYR   B 1 88  ? 38.564 -7.966  19.331 1.00 26.46 ? 94  TYR   C CD1 1 
ATOM   1799 C  CD2 . TYR   B 1 88  ? 37.994 -5.725  18.762 1.00 26.67 ? 94  TYR   C CD2 1 
ATOM   1800 C  CE1 . TYR   B 1 88  ? 39.914 -7.656  19.210 1.00 27.96 ? 94  TYR   C CE1 1 
ATOM   1801 C  CE2 . TYR   B 1 88  ? 39.332 -5.405  18.633 1.00 28.17 ? 94  TYR   C CE2 1 
ATOM   1802 C  CZ  . TYR   B 1 88  ? 40.291 -6.368  18.870 1.00 29.52 ? 94  TYR   C CZ  1 
ATOM   1803 O  OH  . TYR   B 1 88  ? 41.614 -6.009  18.731 1.00 32.42 ? 94  TYR   C OH  1 
ATOM   1804 N  N   . GLN   B 1 89  ? 34.210 -9.960  18.203 1.00 15.67 ? 95  GLN   C N   1 
ATOM   1805 C  CA  . GLN   B 1 89  ? 32.997 -10.686 18.563 1.00 14.31 ? 95  GLN   C CA  1 
ATOM   1806 C  C   . GLN   B 1 89  ? 33.302 -11.400 19.883 1.00 13.46 ? 95  GLN   C C   1 
ATOM   1807 O  O   . GLN   B 1 89  ? 34.392 -11.986 20.038 1.00 14.38 ? 95  GLN   C O   1 
ATOM   1808 C  CB  . GLN   B 1 89  ? 32.636 -11.666 17.442 1.00 15.44 ? 95  GLN   C CB  1 
ATOM   1809 C  CG  . GLN   B 1 89  ? 31.341 -12.397 17.731 1.00 15.79 ? 95  GLN   C CG  1 
ATOM   1810 C  CD  . GLN   B 1 89  ? 30.655 -12.986 16.518 1.00 14.60 ? 95  GLN   C CD  1 
ATOM   1811 O  OE1 . GLN   B 1 89  ? 30.616 -12.393 15.415 1.00 15.78 ? 95  GLN   C OE1 1 
ATOM   1812 N  NE2 . GLN   B 1 89  ? 30.099 -14.152 16.725 1.00 14.68 ? 95  GLN   C NE2 1 
ATOM   1813 N  N   . SER   B 1 90  ? 32.384 -11.357 20.830 1.00 12.89 ? 96  SER   C N   1 
ATOM   1814 C  CA  . SER   B 1 90  ? 32.597 -11.970 22.136 1.00 13.41 ? 96  SER   C CA  1 
ATOM   1815 C  C   . SER   B 1 90  ? 31.978 -13.377 22.200 1.00 12.70 ? 96  SER   C C   1 
ATOM   1816 O  O   . SER   B 1 90  ? 31.145 -13.735 21.366 1.00 13.14 ? 96  SER   C O   1 
ATOM   1817 C  CB  . SER   B 1 90  ? 32.050 -11.078 23.261 1.00 14.86 ? 96  SER   C CB  1 
ATOM   1818 O  OG  . SER   B 1 90  ? 30.643 -11.045 23.158 1.00 15.94 ? 96  SER   C OG  1 
ATOM   1819 N  N   . HIS   B 1 91  ? 32.433 -14.167 23.181 1.00 11.98 ? 97  HIS   C N   1 
ATOM   1820 C  CA  . HIS   B 1 91  ? 31.952 -15.521 23.450 1.00 11.53 ? 97  HIS   C CA  1 
ATOM   1821 C  C   . HIS   B 1 91  ? 32.042 -16.391 22.178 1.00 11.52 ? 97  HIS   C C   1 
ATOM   1822 O  O   . HIS   B 1 91  ? 31.154 -17.222 21.940 1.00 12.72 ? 97  HIS   C O   1 
ATOM   1823 C  CB  . HIS   B 1 91  ? 30.505 -15.490 24.015 1.00 12.63 ? 97  HIS   C CB  1 
ATOM   1824 C  CG  . HIS   B 1 91  ? 30.381 -14.738 25.324 1.00 14.55 ? 97  HIS   C CG  1 
ATOM   1825 N  ND1 . HIS   B 1 91  ? 30.399 -15.396 26.543 1.00 16.92 ? 97  HIS   C ND1 1 
ATOM   1826 C  CD2 . HIS   B 1 91  ? 30.272 -13.399 25.558 1.00 15.91 ? 97  HIS   C CD2 1 
ATOM   1827 C  CE1 . HIS   B 1 91  ? 30.272 -14.453 27.477 1.00 16.83 ? 97  HIS   C CE1 1 
ATOM   1828 N  NE2 . HIS   B 1 91  ? 30.202 -13.232 26.935 1.00 17.32 ? 97  HIS   C NE2 1 
ATOM   1829 N  N   . LEU   B 1 92  ? 33.139 -16.234 21.439 1.00 11.40 ? 98  LEU   C N   1 
ATOM   1830 C  CA  . LEU   B 1 92  ? 33.334 -16.937 20.186 1.00 11.00 ? 98  LEU   C CA  1 
ATOM   1831 C  C   . LEU   B 1 92  ? 34.419 -17.996 20.387 1.00 11.54 ? 98  LEU   C C   1 
ATOM   1832 O  O   . LEU   B 1 92  ? 35.397 -17.787 21.099 1.00 12.26 ? 98  LEU   C O   1 
ATOM   1833 C  CB  . LEU   B 1 92  ? 33.796 -15.926 19.090 1.00 12.59 ? 98  LEU   C CB  1 
ATOM   1834 C  CG  . LEU   B 1 92  ? 33.874 -16.504 17.670 1.00 13.97 ? 98  LEU   C CG  1 
ATOM   1835 C  CD1 . LEU   B 1 92  ? 32.496 -16.808 17.125 1.00 14.19 ? 98  LEU   C CD1 1 
ATOM   1836 C  CD2 . LEU   B 1 92  ? 34.542 -15.503 16.700 1.00 15.49 ? 98  LEU   C CD2 1 
ATOM   1837 N  N   . MET   B 1 93  ? 34.216 -19.155 19.750 1.00 10.92 ? 99  MET   C N   1 
ATOM   1838 C  CA  . MET   B 1 93  ? 35.181 -20.267 19.803 1.00 10.57 ? 99  MET   C CA  1 
ATOM   1839 C  C   . MET   B 1 93  ? 35.585 -20.585 18.366 1.00 11.13 ? 99  MET   C C   1 
ATOM   1840 O  O   . MET   B 1 93  ? 34.716 -20.634 17.487 1.00 12.29 ? 99  MET   C O   1 
ATOM   1841 C  CB  . MET   B 1 93  ? 34.492 -21.503 20.399 1.00 11.92 ? 99  MET   C CB  1 
ATOM   1842 C  CG  . MET   B 1 93  ? 34.013 -21.241 21.812 1.00 14.02 ? 99  MET   C CG  1 
ATOM   1843 S  SD  . MET   B 1 93  ? 32.980 -22.553 22.438 1.00 14.07 ? 99  MET   C SD  1 
ATOM   1844 C  CE  . MET   B 1 93  ? 31.564 -22.467 21.305 1.00 16.37 ? 99  MET   C CE  1 
ATOM   1845 N  N   . LEU   B 1 94  ? 36.871 -20.827 18.082 1.00 10.59 ? 100 LEU   C N   1 
ATOM   1846 C  CA  . LEU   B 1 94  ? 37.309 -21.134 16.721 1.00 11.52 ? 100 LEU   C CA  1 
ATOM   1847 C  C   . LEU   B 1 94  ? 37.760 -22.589 16.591 1.00 10.91 ? 100 LEU   C C   1 
ATOM   1848 O  O   . LEU   B 1 94  ? 38.265 -23.194 17.539 1.00 12.21 ? 100 LEU   C O   1 
ATOM   1849 C  CB  . LEU   B 1 94  ? 38.552 -20.285 16.299 1.00 12.30 ? 100 LEU   C CB  1 
ATOM   1850 C  CG  . LEU   B 1 94  ? 38.387 -18.789 16.246 1.00 13.87 ? 100 LEU   C CG  1 
ATOM   1851 C  CD1 . LEU   B 1 94  ? 39.688 -18.129 15.826 1.00 16.88 ? 100 LEU   C CD1 1 
ATOM   1852 C  CD2 . LEU   B 1 94  ? 37.240 -18.356 15.326 1.00 14.94 ? 100 LEU   C CD2 1 
ATOM   1853 N  N   . ALA   B 1 95  ? 37.601 -23.122 15.383 1.00 10.42 ? 101 ALA   C N   1 
ATOM   1854 C  CA  . ALA   B 1 95  ? 38.151 -24.417 14.984 1.00 10.76 ? 101 ALA   C CA  1 
ATOM   1855 C  C   . ALA   B 1 95  ? 38.719 -24.286 13.555 1.00 10.93 ? 101 ALA   C C   1 
ATOM   1856 O  O   . ALA   B 1 95  ? 38.347 -23.357 12.819 1.00 10.94 ? 101 ALA   C O   1 
ATOM   1857 C  CB  . ALA   B 1 95  ? 37.048 -25.491 15.001 1.00 11.53 ? 101 ALA   C CB  1 
ATOM   1858 N  N   . VAL   B 1 96  ? 39.573 -25.235 13.145 1.00 11.65 ? 102 VAL   C N   1 
ATOM   1859 C  CA  . VAL   B 1 96  ? 40.036 -25.295 11.764 1.00 12.66 ? 102 VAL   C CA  1 
ATOM   1860 C  C   . VAL   B 1 96  ? 38.964 -26.048 10.977 1.00 12.85 ? 102 VAL   C C   1 
ATOM   1861 O  O   . VAL   B 1 96  ? 38.652 -27.219 11.273 1.00 13.61 ? 102 VAL   C O   1 
ATOM   1862 C  CB  . VAL   B 1 96  ? 41.393 -26.036 11.721 1.00 13.49 ? 102 VAL   C CB  1 
ATOM   1863 C  CG1 . VAL   B 1 96  ? 41.858 -26.184 10.277 1.00 15.26 ? 102 VAL   C CG1 1 
ATOM   1864 C  CG2 . VAL   B 1 96  ? 42.414 -25.262 12.541 1.00 14.64 ? 102 VAL   C CG2 1 
ATOM   1865 N  N   . GLY   B 1 97  ? 38.368 -25.353 10.009 1.00 13.05 ? 103 GLY   C N   1 
ATOM   1866 C  CA  . GLY   B 1 97  ? 37.302 -25.981 9.238  1.00 14.11 ? 103 GLY   C CA  1 
ATOM   1867 C  C   . GLY   B 1 97  ? 36.617 -25.023 8.313  1.00 14.61 ? 103 GLY   C C   1 
ATOM   1868 O  O   . GLY   B 1 97  ? 36.898 -23.810 8.313  1.00 16.32 ? 103 GLY   C O   1 
ATOM   1869 N  N   . HIS   B 1 98  ? 35.765 -25.569 7.444  1.00 14.46 ? 104 HIS   C N   1 
ATOM   1870 C  CA  . HIS   B 1 98  ? 35.082 -24.773 6.464  1.00 13.97 ? 104 HIS   C CA  1 
ATOM   1871 C  C   . HIS   B 1 98  ? 33.809 -24.099 6.973  1.00 13.40 ? 104 HIS   C C   1 
ATOM   1872 O  O   . HIS   B 1 98  ? 33.005 -24.729 7.680  1.00 13.33 ? 104 HIS   C O   1 
ATOM   1873 C  CB  . HIS   B 1 98  ? 34.751 -25.667 5.285  1.00 16.94 ? 104 HIS   C CB  1 
ATOM   1874 C  CG  . HIS   B 1 98  ? 34.232 -24.879 4.143  1.00 20.08 ? 104 HIS   C CG  1 
ATOM   1875 N  ND1 . HIS   B 1 98  ? 35.026 -23.957 3.466  1.00 22.14 ? 104 HIS   C ND1 1 
ATOM   1876 C  CD2 . HIS   B 1 98  ? 32.981 -24.833 3.648  1.00 22.78 ? 104 HIS   C CD2 1 
ATOM   1877 C  CE1 . HIS   B 1 98  ? 34.239 -23.415 2.552  1.00 24.51 ? 104 HIS   C CE1 1 
ATOM   1878 N  NE2 . HIS   B 1 98  ? 33.000 -23.909 2.624  1.00 25.15 ? 104 HIS   C NE2 1 
ATOM   1879 N  N   . SER   B 1 99  ? 33.594 -22.828 6.594  1.00 13.45 ? 105 SER   C N   1 
ATOM   1880 C  CA  . SER   B 1 99  ? 32.363 -22.106 6.992  1.00 14.03 ? 105 SER   C CA  1 
ATOM   1881 C  C   . SER   B 1 99  ? 32.121 -20.987 5.972  1.00 16.33 ? 105 SER   C C   1 
ATOM   1882 O  O   . SER   B 1 99  ? 32.989 -20.114 5.845  1.00 18.28 ? 105 SER   C O   1 
ATOM   1883 C  CB  . SER   B 1 99  ? 32.579 -21.501 8.381  1.00 15.65 ? 105 SER   C CB  1 
ATOM   1884 O  OG  . SER   B 1 99  ? 31.507 -20.651 8.783  1.00 16.89 ? 105 SER   C OG  1 
ATOM   1885 N  N   . GLU   B 1 100 ? 30.977 -21.006 5.277  1.00 16.34 ? 106 GLU   C N   1 
ATOM   1886 C  CA  . GLU   B 1 100 ? 30.505 -19.994 4.291  1.00 16.17 ? 106 GLU   C CA  1 
ATOM   1887 C  C   . GLU   B 1 100 ? 29.382 -19.238 5.032  1.00 14.70 ? 106 GLU   C C   1 
ATOM   1888 O  O   . GLU   B 1 100 ? 28.814 -19.747 6.011  1.00 13.87 ? 106 GLU   C O   1 
ATOM   1889 C  CB  . GLU   B 1 100 ? 29.834 -20.674 3.052  1.00 18.78 ? 106 GLU   C CB  1 
ATOM   1890 C  CG  . GLU   B 1 100 ? 30.581 -21.739 2.308  1.00 25.65 ? 106 GLU   C CG  1 
ATOM   1891 C  CD  . GLU   B 1 100 ? 31.396 -21.285 1.129  1.00 32.66 ? 106 GLU   C CD  1 
ATOM   1892 O  OE1 . GLU   B 1 100 ? 32.052 -22.148 0.513  1.00 34.20 ? 106 GLU   C OE1 1 
ATOM   1893 O  OE2 . GLU   B 1 100 ? 31.440 -20.061 0.868  1.00 33.89 ? 106 GLU   C OE2 1 
ATOM   1894 N  N   . PRO   B 1 101 ? 28.981 -18.056 4.539  1.00 15.04 ? 107 PRO   C N   1 
ATOM   1895 C  CA  . PRO   B 1 101 ? 27.883 -17.343 5.218  1.00 13.98 ? 107 PRO   C CA  1 
ATOM   1896 C  C   . PRO   B 1 101 ? 26.618 -18.205 5.409  1.00 14.86 ? 107 PRO   C C   1 
ATOM   1897 O  O   . PRO   B 1 101 ? 25.997 -18.162 6.475  1.00 14.96 ? 107 PRO   C O   1 
ATOM   1898 C  CB  . PRO   B 1 101 ? 27.597 -16.139 4.292  1.00 16.00 ? 107 PRO   C CB  1 
ATOM   1899 C  CG  . PRO   B 1 101 ? 28.878 -15.953 3.524  1.00 18.79 ? 107 PRO   C CG  1 
ATOM   1900 C  CD  . PRO   B 1 101 ? 29.587 -17.269 3.433  1.00 17.11 ? 107 PRO   C CD  1 
ATOM   1901 N  N   . GLY   B 1 102 ? 26.293 -19.058 4.428  1.00 13.61 ? 108 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 102 ? 25.072 -19.869 4.531  1.00 13.38 ? 108 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 102 ? 25.151 -20.960 5.597  1.00 12.57 ? 108 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 102 ? 24.168 -21.645 5.896  1.00 14.45 ? 108 GLY   C O   1 
ATOM   1905 N  N   . ASP   B 1 103 ? 26.379 -21.249 6.091  1.00 11.53 ? 109 ASP   C N   1 
ATOM   1906 C  CA  . ASP   B 1 103 ? 26.546 -22.242 7.132  1.00 11.15 ? 109 ASP   C CA  1 
ATOM   1907 C  C   . ASP   B 1 103 ? 26.180 -21.751 8.519  1.00 11.53 ? 109 ASP   C C   1 
ATOM   1908 O  O   . ASP   B 1 103 ? 26.065 -22.563 9.456  1.00 11.22 ? 109 ASP   C O   1 
ATOM   1909 C  CB  . ASP   B 1 103 ? 28.008 -22.736 7.162  1.00 12.62 ? 109 ASP   C CB  1 
ATOM   1910 C  CG  . ASP   B 1 103 ? 28.339 -23.539 5.937  1.00 13.79 ? 109 ASP   C CG  1 
ATOM   1911 O  OD1 . ASP   B 1 103 ? 27.489 -24.295 5.497  1.00 14.13 ? 109 ASP   C OD1 1 
ATOM   1912 O  OD2 . ASP   B 1 103 ? 29.472 -23.382 5.404  1.00 15.72 ? 109 ASP   C OD2 1 
ATOM   1913 N  N   . CYS   B 1 104 ? 25.986 -20.414 8.710  1.00 11.32 ? 110 CYS   C N   1 
ATOM   1914 C  CA  . CYS   B 1 104 ? 25.580 -19.881 10.026 1.00 11.06 ? 110 CYS   C CA  1 
ATOM   1915 C  C   . CYS   B 1 104 ? 24.333 -20.580 10.525 1.00 11.40 ? 110 CYS   C C   1 
ATOM   1916 O  O   . CYS   B 1 104 ? 23.388 -20.806 9.749  1.00 12.73 ? 110 CYS   C O   1 
ATOM   1917 C  CB  . CYS   B 1 104 ? 25.352 -18.372 9.959  1.00 12.00 ? 110 CYS   C CB  1 
ATOM   1918 S  SG  . CYS   B 1 104 ? 26.874 -17.405 9.828  1.00 13.21 ? 110 CYS   C SG  1 
ATOM   1919 N  N   . GLY   B 1 105 ? 24.345 -20.946 11.790 1.00 9.53  ? 111 GLY   C N   1 
ATOM   1920 C  CA  . GLY   B 1 105 ? 23.189 -21.618 12.394 1.00 11.03 ? 111 GLY   C CA  1 
ATOM   1921 C  C   . GLY   B 1 105 ? 23.410 -23.112 12.574 1.00 11.12 ? 111 GLY   C C   1 
ATOM   1922 O  O   . GLY   B 1 105 ? 22.638 -23.777 13.277 1.00 12.03 ? 111 GLY   C O   1 
ATOM   1923 N  N   . GLY   B 1 106 ? 24.433 -23.680 11.907 1.00 10.58 ? 112 GLY   C N   1 
ATOM   1924 C  CA  . GLY   B 1 106 ? 24.753 -25.114 12.080 1.00 10.82 ? 112 GLY   C CA  1 
ATOM   1925 C  C   . GLY   B 1 106 ? 25.144 -25.405 13.518 1.00 10.07 ? 112 GLY   C C   1 
ATOM   1926 O  O   . GLY   B 1 106 ? 25.847 -24.600 14.152 1.00 10.23 ? 112 GLY   C O   1 
ATOM   1927 N  N   . ILE   B 1 107 ? 24.699 -26.538 14.038 1.00 9.61  ? 113 ILE   C N   1 
ATOM   1928 C  CA  . ILE   B 1 107 ? 24.969 -26.839 15.444 1.00 9.48  ? 113 ILE   C CA  1 
ATOM   1929 C  C   . ILE   B 1 107 ? 26.358 -27.448 15.628 1.00 9.35  ? 113 ILE   C C   1 
ATOM   1930 O  O   . ILE   B 1 107 ? 26.776 -28.337 14.865 1.00 10.16 ? 113 ILE   C O   1 
ATOM   1931 C  CB  . ILE   B 1 107 ? 23.844 -27.796 15.972 1.00 11.97 ? 113 ILE   C CB  1 
ATOM   1932 C  CG1 . ILE   B 1 107 ? 22.610 -26.855 16.384 1.00 15.55 ? 113 ILE   C CG1 1 
ATOM   1933 C  CG2 . ILE   B 1 107 ? 24.288 -28.643 17.181 1.00 12.12 ? 113 ILE   C CG2 1 
ATOM   1934 C  CD1 . ILE   B 1 107 ? 21.285 -27.558 16.800 1.00 20.24 ? 113 ILE   C CD1 1 
ATOM   1935 N  N   . LEU   B 1 108 ? 27.027 -27.013 16.732 1.00 9.08  ? 114 LEU   C N   1 
ATOM   1936 C  CA  . LEU   B 1 108 ? 28.213 -27.674 17.280 1.00 8.62  ? 114 LEU   C CA  1 
ATOM   1937 C  C   . LEU   B 1 108 ? 27.706 -28.447 18.542 1.00 9.60  ? 114 LEU   C C   1 
ATOM   1938 O  O   . LEU   B 1 108 ? 27.070 -27.844 19.406 1.00 9.54  ? 114 LEU   C O   1 
ATOM   1939 C  CB  . LEU   B 1 108 ? 29.248 -26.611 17.677 1.00 8.77  ? 114 LEU   C CB  1 
ATOM   1940 C  CG  . LEU   B 1 108 ? 30.456 -27.124 18.482 1.00 9.90  ? 114 LEU   C CG  1 
ATOM   1941 C  CD1 . LEU   B 1 108 ? 31.342 -28.038 17.612 1.00 11.83 ? 114 LEU   C CD1 1 
ATOM   1942 C  CD2 . LEU   B 1 108 ? 31.280 -25.953 18.972 1.00 10.47 ? 114 LEU   C CD2 1 
ATOM   1943 N  N   . ARG   B 1 109 ? 27.981 -29.765 18.610 1.00 9.62  ? 115 ARG   C N   1 
ATOM   1944 C  CA  . ARG   B 1 109 ? 27.514 -30.585 19.747 1.00 10.03 ? 115 ARG   C CA  1 
ATOM   1945 C  C   . ARG   B 1 109 ? 28.664 -31.407 20.326 1.00 10.61 ? 115 ARG   C C   1 
ATOM   1946 O  O   . ARG   B 1 109 ? 29.591 -31.813 19.613 1.00 10.85 ? 115 ARG   C O   1 
ATOM   1947 C  CB  . ARG   B 1 109 ? 26.400 -31.547 19.262 1.00 13.12 ? 115 ARG   C CB  1 
ATOM   1948 C  CG  . ARG   B 1 109 ? 26.876 -32.480 18.178 1.00 16.00 ? 115 ARG   C CG  1 
ATOM   1949 C  CD  . ARG   B 1 109 ? 25.787 -33.438 17.716 1.00 20.91 ? 115 ARG   C CD  1 
ATOM   1950 N  NE  . ARG   B 1 109 ? 24.876 -32.755 16.806 1.00 25.88 ? 115 ARG   C NE  1 
ATOM   1951 C  CZ  . ARG   B 1 109 ? 23.554 -32.856 16.848 1.00 31.11 ? 115 ARG   C CZ  1 
ATOM   1952 N  NH1 . ARG   B 1 109 ? 22.967 -33.611 17.771 1.00 33.00 ? 115 ARG   C NH1 1 
ATOM   1953 N  NH2 . ARG   B 1 109 ? 22.806 -32.210 15.963 1.00 31.94 ? 115 ARG   C NH2 1 
ATOM   1954 N  N   . CYS   B 1 110 ? 28.605 -31.629 21.629 1.00 10.60 ? 116 CYS   C N   1 
ATOM   1955 C  CA  . CYS   B 1 110 ? 29.559 -32.515 22.338 1.00 10.89 ? 116 CYS   C CA  1 
ATOM   1956 C  C   . CYS   B 1 110 ? 28.709 -33.623 23.020 1.00 12.30 ? 116 CYS   C C   1 
ATOM   1957 O  O   . CYS   B 1 110 ? 27.482 -33.701 22.815 1.00 12.31 ? 116 CYS   C O   1 
ATOM   1958 C  CB  . CYS   B 1 110 ? 30.367 -31.724 23.367 1.00 10.20 ? 116 CYS   C CB  1 
ATOM   1959 S  SG  . CYS   B 1 110 ? 29.337 -31.045 24.714 1.00 11.27 ? 116 CYS   C SG  1 
ATOM   1960 N  N   . GLN   B 1 111 ? 29.353 -34.491 23.864 1.00 13.74 ? 117 GLN   C N   1 
ATOM   1961 C  CA  . GLN   B 1 111 ? 28.574 -35.524 24.567 1.00 15.00 ? 117 GLN   C CA  1 
ATOM   1962 C  C   . GLN   B 1 111 ? 27.493 -34.959 25.500 1.00 15.46 ? 117 GLN   C C   1 
ATOM   1963 O  O   . GLN   B 1 111 ? 26.534 -35.661 25.851 1.00 17.16 ? 117 GLN   C O   1 
ATOM   1964 C  CB  . GLN   B 1 111 ? 29.492 -36.488 25.381 1.00 16.12 ? 117 GLN   C CB  1 
ATOM   1965 C  CG  . GLN   B 1 111 ? 30.150 -35.810 26.566 1.00 19.00 ? 117 GLN   C CG  1 
ATOM   1966 C  CD  . GLN   B 1 111 ? 31.084 -36.706 27.345 1.00 29.13 ? 117 GLN   C CD  1 
ATOM   1967 O  OE1 . GLN   B 1 111 ? 32.283 -36.743 27.067 1.00 32.79 ? 117 GLN   C OE1 1 
ATOM   1968 N  NE2 . GLN   B 1 111 ? 30.574 -37.405 28.350 1.00 31.41 ? 117 GLN   C NE2 1 
ATOM   1969 N  N   . HIS   B 1 112 ? 27.608 -33.688 25.901 1.00 13.21 ? 118 HIS   C N   1 
ATOM   1970 C  CA  . HIS   B 1 112 ? 26.651 -33.077 26.820 1.00 13.27 ? 118 HIS   C CA  1 
ATOM   1971 C  C   . HIS   B 1 112 ? 25.459 -32.399 26.149 1.00 13.49 ? 118 HIS   C C   1 
ATOM   1972 O  O   . HIS   B 1 112 ? 24.497 -32.032 26.839 1.00 14.98 ? 118 HIS   C O   1 
ATOM   1973 C  CB  . HIS   B 1 112 ? 27.363 -32.095 27.761 1.00 13.83 ? 118 HIS   C CB  1 
ATOM   1974 C  CG  . HIS   B 1 112 ? 28.539 -32.716 28.457 1.00 12.72 ? 118 HIS   C CG  1 
ATOM   1975 N  ND1 . HIS   B 1 112 ? 29.856 -32.469 28.077 1.00 12.95 ? 118 HIS   C ND1 1 
ATOM   1976 C  CD2 . HIS   B 1 112 ? 28.554 -33.506 29.557 1.00 15.88 ? 118 HIS   C CD2 1 
ATOM   1977 C  CE1 . HIS   B 1 112 ? 30.610 -33.163 28.907 1.00 15.25 ? 118 HIS   C CE1 1 
ATOM   1978 N  NE2 . HIS   B 1 112 ? 29.868 -33.787 29.822 1.00 16.94 ? 118 HIS   C NE2 1 
ATOM   1979 N  N   . GLY   B 1 113 ? 25.540 -32.155 24.841 1.00 12.27 ? 119 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 113 ? 24.465 -31.479 24.128 1.00 12.50 ? 119 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 113 ? 24.966 -30.407 23.177 1.00 11.31 ? 119 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 113 ? 26.080 -30.498 22.665 1.00 11.13 ? 119 GLY   C O   1 
ATOM   1983 N  N   . VAL   B 1 114 ? 24.111 -29.401 22.912 1.00 10.98 ? 120 VAL   C N   1 
ATOM   1984 C  CA  . VAL   B 1 114 ? 24.425 -28.330 21.985 1.00 10.79 ? 120 VAL   C CA  1 
ATOM   1985 C  C   . VAL   B 1 114 ? 25.359 -27.323 22.662 1.00 10.57 ? 120 VAL   C C   1 
ATOM   1986 O  O   . VAL   B 1 114 ? 25.064 -26.765 23.717 1.00 11.35 ? 120 VAL   C O   1 
ATOM   1987 C  CB  . VAL   B 1 114 ? 23.126 -27.636 21.504 1.00 12.10 ? 120 VAL   C CB  1 
ATOM   1988 C  CG1 . VAL   B 1 114 ? 23.483 -26.452 20.621 1.00 13.05 ? 120 VAL   C CG1 1 
ATOM   1989 C  CG2 . VAL   B 1 114 ? 22.218 -28.620 20.744 1.00 14.02 ? 120 VAL   C CG2 1 
ATOM   1990 N  N   . VAL   B 1 115 ? 26.522 -27.063 22.032 1.00 9.41  ? 121 VAL   C N   1 
ATOM   1991 C  CA  . VAL   B 1 115 ? 27.538 -26.124 22.538 1.00 10.09 ? 121 VAL   C CA  1 
ATOM   1992 C  C   . VAL   B 1 115 ? 27.309 -24.723 22.002 1.00 10.93 ? 121 VAL   C C   1 
ATOM   1993 O  O   . VAL   B 1 115 ? 27.536 -23.745 22.717 1.00 11.29 ? 121 VAL   C O   1 
ATOM   1994 C  CB  . VAL   B 1 115 ? 28.937 -26.641 22.134 1.00 9.92  ? 121 VAL   C CB  1 
ATOM   1995 C  CG1 . VAL   B 1 115 ? 30.015 -25.640 22.523 1.00 11.49 ? 121 VAL   C CG1 1 
ATOM   1996 C  CG2 . VAL   B 1 115 ? 29.207 -28.004 22.779 1.00 11.34 ? 121 VAL   C CG2 1 
ATOM   1997 N  N   . GLY   B 1 116 ? 26.954 -24.631 20.727 1.00 10.07 ? 122 GLY   C N   1 
ATOM   1998 C  CA  . GLY   B 1 116 ? 26.736 -23.336 20.104 1.00 11.42 ? 122 GLY   C CA  1 
ATOM   1999 C  C   . GLY   B 1 116 ? 26.387 -23.511 18.640 1.00 10.28 ? 122 GLY   C C   1 
ATOM   2000 O  O   . GLY   B 1 116 ? 26.081 -24.631 18.201 1.00 10.49 ? 122 GLY   C O   1 
ATOM   2001 N  N   . ILE   B 1 117 ? 26.375 -22.364 17.897 1.00 9.21  ? 123 ILE   C N   1 
ATOM   2002 C  CA  . ILE   B 1 117 ? 26.032 -22.406 16.483 1.00 9.55  ? 123 ILE   C CA  1 
ATOM   2003 C  C   . ILE   B 1 117 ? 27.076 -21.663 15.678 1.00 9.51  ? 123 ILE   C C   1 
ATOM   2004 O  O   . ILE   B 1 117 ? 27.700 -20.695 16.153 1.00 10.70 ? 123 ILE   C O   1 
ATOM   2005 C  CB  . ILE   B 1 117 ? 24.620 -21.770 16.222 1.00 10.34 ? 123 ILE   C CB  1 
ATOM   2006 C  CG1 . ILE   B 1 117 ? 24.505 -20.363 16.848 1.00 11.89 ? 123 ILE   C CG1 1 
ATOM   2007 C  CG2 . ILE   B 1 117 ? 23.499 -22.705 16.664 1.00 12.41 ? 123 ILE   C CG2 1 
ATOM   2008 C  CD1 . ILE   B 1 117 ? 23.165 -19.593 16.412 1.00 12.34 ? 123 ILE   C CD1 1 
ATOM   2009 N  N   . VAL   B 1 118 ? 27.247 -22.084 14.418 1.00 9.25  ? 124 VAL   C N   1 
ATOM   2010 C  CA  . VAL   B 1 118 ? 28.192 -21.409 13.508 1.00 9.47  ? 124 VAL   C CA  1 
ATOM   2011 C  C   . VAL   B 1 118 ? 27.803 -19.934 13.374 1.00 10.39 ? 124 VAL   C C   1 
ATOM   2012 O  O   . VAL   B 1 118 ? 26.599 -19.608 13.197 1.00 9.99  ? 124 VAL   C O   1 
ATOM   2013 C  CB  . VAL   B 1 118 ? 28.172 -22.083 12.115 1.00 9.35  ? 124 VAL   C CB  1 
ATOM   2014 C  CG1 . VAL   B 1 118 ? 29.031 -21.322 11.105 1.00 10.15 ? 124 VAL   C CG1 1 
ATOM   2015 C  CG2 . VAL   B 1 118 ? 28.625 -23.534 12.184 1.00 11.00 ? 124 VAL   C CG2 1 
ATOM   2016 N  N   . SER   B 1 119 ? 28.822 -19.048 13.474 1.00 9.90  ? 125 SER   C N   1 
ATOM   2017 C  CA  . SER   B 1 119 ? 28.626 -17.592 13.360 1.00 10.27 ? 125 SER   C CA  1 
ATOM   2018 C  C   . SER   B 1 119 ? 29.632 -16.906 12.451 1.00 11.82 ? 125 SER   C C   1 
ATOM   2019 O  O   . SER   B 1 119 ? 29.273 -15.855 11.883 1.00 11.59 ? 125 SER   C O   1 
ATOM   2020 C  CB  . SER   B 1 119 ? 28.660 -16.987 14.765 1.00 11.53 ? 125 SER   C CB  1 
ATOM   2021 O  OG  . SER   B 1 119 ? 28.532 -15.559 14.708 1.00 12.96 ? 125 SER   C OG  1 
ATOM   2022 N  N   . THR   B 1 120 ? 30.870 -17.445 12.321 1.00 11.34 ? 126 THR   C N   1 
ATOM   2023 C  CA  . THR   B 1 120 ? 31.882 -16.768 11.513 1.00 11.01 ? 126 THR   C CA  1 
ATOM   2024 C  C   . THR   B 1 120 ? 32.593 -17.781 10.617 1.00 11.04 ? 126 THR   C C   1 
ATOM   2025 O  O   . THR   B 1 120 ? 32.517 -19.011 10.856 1.00 11.25 ? 126 THR   C O   1 
ATOM   2026 C  CB  . THR   B 1 120 ? 32.935 -16.011 12.409 1.00 11.81 ? 126 THR   C CB  1 
ATOM   2027 O  OG1 . THR   B 1 120 ? 33.809 -16.960 13.054 1.00 12.50 ? 126 THR   C OG1 1 
ATOM   2028 C  CG2 . THR   B 1 120 ? 32.298 -15.088 13.390 1.00 13.42 ? 126 THR   C CG2 1 
ATOM   2029 N  N   . GLY   B 1 121 ? 33.307 -17.280 9.624  1.00 12.32 ? 127 GLY   C N   1 
ATOM   2030 C  CA  . GLY   B 1 121 ? 34.131 -18.147 8.786  1.00 13.93 ? 127 GLY   C CA  1 
ATOM   2031 C  C   . GLY   B 1 121 ? 35.124 -17.336 7.975  1.00 17.79 ? 127 GLY   C C   1 
ATOM   2032 O  O   . GLY   B 1 121 ? 34.913 -16.158 7.699  1.00 19.27 ? 127 GLY   C O   1 
ATOM   2033 N  N   . GLY   B 1 122 ? 36.166 -17.976 7.518  1.00 21.51 ? 128 GLY   C N   1 
ATOM   2034 C  CA  . GLY   B 1 122 ? 37.212 -17.318 6.731  1.00 24.04 ? 128 GLY   C CA  1 
ATOM   2035 C  C   . GLY   B 1 122 ? 38.595 -17.738 7.183  1.00 23.11 ? 128 GLY   C C   1 
ATOM   2036 O  O   . GLY   B 1 122 ? 38.784 -18.167 8.318  1.00 22.86 ? 128 GLY   C O   1 
ATOM   2037 N  N   . ASN   B 1 123 ? 39.588 -17.575 6.303  1.00 21.97 ? 129 ASN   C N   1 
ATOM   2038 C  CA  . ASN   B 1 123 ? 40.985 -17.951 6.538  1.00 22.52 ? 129 ASN   C CA  1 
ATOM   2039 C  C   . ASN   B 1 123 ? 41.098 -19.431 6.952  1.00 20.53 ? 129 ASN   C C   1 
ATOM   2040 O  O   . ASN   B 1 123 ? 42.039 -19.786 7.667  1.00 23.14 ? 129 ASN   C O   1 
ATOM   2041 C  CB  . ASN   B 1 123 ? 41.677 -17.042 7.598  1.00 26.72 ? 129 ASN   C CB  1 
ATOM   2042 C  CG  . ASN   B 1 123 ? 42.464 -15.898 7.011  1.00 32.95 ? 129 ASN   C CG  1 
ATOM   2043 O  OD1 . ASN   B 1 123 ? 42.780 -15.878 5.817  1.00 33.64 ? 129 ASN   C OD1 1 
ATOM   2044 N  ND2 . ASN   B 1 123 ? 42.803 -14.914 7.836  1.00 35.48 ? 129 ASN   C ND2 1 
ATOM   2045 N  N   . GLY   B 1 124 ? 40.144 -20.276 6.537  1.00 18.10 ? 130 GLY   C N   1 
ATOM   2046 C  CA  . GLY   B 1 124 ? 40.182 -21.696 6.910  1.00 17.05 ? 130 GLY   C CA  1 
ATOM   2047 C  C   . GLY   B 1 124 ? 39.766 -21.988 8.338  1.00 15.23 ? 130 GLY   C C   1 
ATOM   2048 O  O   . GLY   B 1 124 ? 40.011 -23.081 8.852  1.00 15.11 ? 130 GLY   C O   1 
ATOM   2049 N  N   . LEU   B 1 125 ? 39.095 -21.046 8.967  1.00 13.96 ? 131 LEU   C N   1 
ATOM   2050 C  CA  . LEU   B 1 125 ? 38.614 -21.166 10.336 1.00 13.85 ? 131 LEU   C CA  1 
ATOM   2051 C  C   . LEU   B 1 125 ? 37.099 -21.075 10.356 1.00 13.83 ? 131 LEU   C C   1 
ATOM   2052 O  O   . LEU   B 1 125 ? 36.474 -20.456 9.457  1.00 16.10 ? 131 LEU   C O   1 
ATOM   2053 C  CB  . LEU   B 1 125 ? 39.220 -20.071 11.236 1.00 15.72 ? 131 LEU   C CB  1 
ATOM   2054 C  CG  . LEU   B 1 125 ? 40.772 -20.082 11.279 1.00 18.00 ? 131 LEU   C CG  1 
ATOM   2055 C  CD1 . LEU   B 1 125 ? 41.368 -18.738 11.741 1.00 21.22 ? 131 LEU   C CD1 1 
ATOM   2056 C  CD2 . LEU   B 1 125 ? 41.298 -21.215 12.080 1.00 19.02 ? 131 LEU   C CD2 1 
ATOM   2057 N  N   . VAL   B 1 126 ? 36.494 -21.729 11.320 1.00 11.09 ? 132 VAL   C N   1 
ATOM   2058 C  CA  . VAL   B 1 126 ? 35.048 -21.625 11.572 1.00 10.76 ? 132 VAL   C CA  1 
ATOM   2059 C  C   . VAL   B 1 126 ? 34.892 -21.147 13.012 1.00 10.18 ? 132 VAL   C C   1 
ATOM   2060 O  O   . VAL   B 1 126 ? 35.562 -21.659 13.922 1.00 10.87 ? 132 VAL   C O   1 
ATOM   2061 C  CB  . VAL   B 1 126 ? 34.308 -22.966 11.337 1.00 10.94 ? 132 VAL   C CB  1 
ATOM   2062 C  CG1 . VAL   B 1 126 ? 34.947 -24.130 12.045 1.00 13.09 ? 132 VAL   C CG1 1 
ATOM   2063 C  CG2 . VAL   B 1 126 ? 32.797 -22.862 11.665 1.00 11.45 ? 132 VAL   C CG2 1 
ATOM   2064 N  N   . GLY   B 1 127 ? 33.999 -20.175 13.217 1.00 10.21 ? 133 GLY   C N   1 
ATOM   2065 C  CA  . GLY   B 1 127 ? 33.753 -19.665 14.554 1.00 9.97  ? 133 GLY   C CA  1 
ATOM   2066 C  C   . GLY   B 1 127 ? 32.334 -19.997 14.999 1.00 10.48 ? 133 GLY   C C   1 
ATOM   2067 O  O   . GLY   B 1 127 ? 31.389 -19.889 14.204 1.00 10.54 ? 133 GLY   C O   1 
ATOM   2068 N  N   . PHE   B 1 128 ? 32.213 -20.373 16.271 1.00 8.68  ? 134 PHE   C N   1 
ATOM   2069 C  CA  . PHE   B 1 128 ? 30.919 -20.742 16.874 1.00 9.66  ? 134 PHE   C CA  1 
ATOM   2070 C  C   . PHE   B 1 128 ? 30.592 -19.805 18.009 1.00 9.72  ? 134 PHE   C C   1 
ATOM   2071 O  O   . PHE   B 1 128 ? 31.447 -19.557 18.896 1.00 10.48 ? 134 PHE   C O   1 
ATOM   2072 C  CB  . PHE   B 1 128 ? 30.992 -22.175 17.466 1.00 9.59  ? 134 PHE   C CB  1 
ATOM   2073 C  CG  . PHE   B 1 128 ? 31.527 -23.195 16.478 1.00 9.64  ? 134 PHE   C CG  1 
ATOM   2074 C  CD1 . PHE   B 1 128 ? 30.689 -23.783 15.531 1.00 9.51  ? 134 PHE   C CD1 1 
ATOM   2075 C  CD2 . PHE   B 1 128 ? 32.867 -23.567 16.492 1.00 10.34 ? 134 PHE   C CD2 1 
ATOM   2076 C  CE1 . PHE   B 1 128 ? 31.173 -24.750 14.672 1.00 10.39 ? 134 PHE   C CE1 1 
ATOM   2077 C  CE2 . PHE   B 1 128 ? 33.362 -24.527 15.606 1.00 10.45 ? 134 PHE   C CE2 1 
ATOM   2078 C  CZ  . PHE   B 1 128 ? 32.523 -25.111 14.695 1.00 10.56 ? 134 PHE   C CZ  1 
ATOM   2079 N  N   . ALA   B 1 129 ? 29.330 -19.333 18.030 1.00 9.58  ? 135 ALA   C N   1 
ATOM   2080 C  CA  . ALA   B 1 129 ? 28.830 -18.534 19.145 1.00 9.82  ? 135 ALA   C CA  1 
ATOM   2081 C  C   . ALA   B 1 129 ? 28.442 -19.514 20.281 1.00 11.01 ? 135 ALA   C C   1 
ATOM   2082 O  O   . ALA   B 1 129 ? 27.536 -20.349 20.122 1.00 11.08 ? 135 ALA   C O   1 
ATOM   2083 C  CB  . ALA   B 1 129 ? 27.606 -17.733 18.695 1.00 10.70 ? 135 ALA   C CB  1 
ATOM   2084 N  N   . ASP   B 1 130 ? 29.116 -19.405 21.430 1.00 10.80 ? 136 ASP   C N   1 
ATOM   2085 C  CA  . ASP   B 1 130 ? 28.861 -20.300 22.568 1.00 10.95 ? 136 ASP   C CA  1 
ATOM   2086 C  C   . ASP   B 1 130 ? 27.507 -19.962 23.161 1.00 10.79 ? 136 ASP   C C   1 
ATOM   2087 O  O   . ASP   B 1 130 ? 27.131 -18.778 23.264 1.00 11.49 ? 136 ASP   C O   1 
ATOM   2088 C  CB  . ASP   B 1 130 ? 29.925 -20.052 23.661 1.00 12.25 ? 136 ASP   C CB  1 
ATOM   2089 C  CG  . ASP   B 1 130 ? 29.827 -20.974 24.853 1.00 15.53 ? 136 ASP   C CG  1 
ATOM   2090 O  OD1 . ASP   B 1 130 ? 29.689 -22.189 24.656 1.00 14.85 ? 136 ASP   C OD1 1 
ATOM   2091 O  OD2 . ASP   B 1 130 ? 29.809 -20.463 25.995 1.00 18.65 ? 136 ASP   C OD2 1 
ATOM   2092 N  N   . VAL   B 1 131 ? 26.797 -20.982 23.666 1.00 10.79 ? 137 VAL   C N   1 
ATOM   2093 C  CA  . VAL   B 1 131 ? 25.554 -20.772 24.439 1.00 10.97 ? 137 VAL   C CA  1 
ATOM   2094 C  C   . VAL   B 1 131 ? 25.613 -21.447 25.832 1.00 12.05 ? 137 VAL   C C   1 
ATOM   2095 O  O   . VAL   B 1 131 ? 24.637 -21.399 26.575 1.00 12.37 ? 137 VAL   C O   1 
ATOM   2096 C  CB  . VAL   B 1 131 ? 24.275 -21.246 23.689 1.00 11.82 ? 137 VAL   C CB  1 
ATOM   2097 C  CG1 . VAL   B 1 131 ? 24.115 -20.446 22.376 1.00 11.63 ? 137 VAL   C CG1 1 
ATOM   2098 C  CG2 . VAL   B 1 131 ? 24.309 -22.738 23.395 1.00 12.11 ? 137 VAL   C CG2 1 
ATOM   2099 N  N   . ARG   B 1 132 ? 26.732 -22.097 26.177 1.00 11.58 ? 138 ARG   C N   1 
ATOM   2100 C  CA  . ARG   B 1 132 ? 26.826 -22.876 27.420 1.00 11.34 ? 138 ARG   C CA  1 
ATOM   2101 C  C   . ARG   B 1 132 ? 26.751 -22.045 28.686 1.00 11.93 ? 138 ARG   C C   1 
ATOM   2102 O  O   . ARG   B 1 132 ? 26.451 -22.609 29.758 1.00 13.45 ? 138 ARG   C O   1 
ATOM   2103 C  CB  . ARG   B 1 132 ? 28.080 -23.732 27.418 1.00 10.39 ? 138 ARG   C CB  1 
ATOM   2104 C  CG  . ARG   B 1 132 ? 28.086 -24.778 26.293 1.00 11.27 ? 138 ARG   C CG  1 
ATOM   2105 C  CD  . ARG   B 1 132 ? 29.395 -25.540 26.309 1.00 11.64 ? 138 ARG   C CD  1 
ATOM   2106 N  NE  . ARG   B 1 132 ? 30.484 -24.650 25.905 1.00 11.35 ? 138 ARG   C NE  1 
ATOM   2107 C  CZ  . ARG   B 1 132 ? 31.739 -25.037 25.750 1.00 12.62 ? 138 ARG   C CZ  1 
ATOM   2108 N  NH1 . ARG   B 1 132 ? 32.115 -26.278 26.088 1.00 12.47 ? 138 ARG   C NH1 1 
ATOM   2109 N  NH2 . ARG   B 1 132 ? 32.643 -24.188 25.278 1.00 12.79 ? 138 ARG   C NH2 1 
ATOM   2110 N  N   . ASP   B 1 133 ? 27.027 -20.743 28.607 1.00 12.10 ? 139 ASP   C N   1 
ATOM   2111 C  CA  . ASP   B 1 133 ? 26.964 -19.885 29.792 1.00 12.92 ? 139 ASP   C CA  1 
ATOM   2112 C  C   . ASP   B 1 133 ? 25.541 -19.337 30.028 1.00 14.19 ? 139 ASP   C C   1 
ATOM   2113 O  O   . ASP   B 1 133 ? 25.315 -18.722 31.087 1.00 14.92 ? 139 ASP   C O   1 
ATOM   2114 C  CB  . ASP   B 1 133 ? 27.940 -18.700 29.640 1.00 14.41 ? 139 ASP   C CB  1 
ATOM   2115 C  CG  . ASP   B 1 133 ? 27.585 -17.772 28.492 1.00 16.92 ? 139 ASP   C CG  1 
ATOM   2116 O  OD1 . ASP   B 1 133 ? 27.268 -18.280 27.390 1.00 14.61 ? 139 ASP   C OD1 1 
ATOM   2117 O  OD2 . ASP   B 1 133 ? 27.589 -16.502 28.700 1.00 18.47 ? 139 ASP   C OD2 1 
ATOM   2118 N  N   . LEU   B 1 134 ? 24.592 -19.551 29.060 1.00 13.25 ? 140 LEU   C N   1 
ATOM   2119 C  CA  . LEU   B 1 134 ? 23.240 -18.982 29.158 1.00 12.72 ? 140 LEU   C CA  1 
ATOM   2120 C  C   . LEU   B 1 134 ? 22.384 -19.953 29.933 1.00 13.07 ? 140 LEU   C C   1 
ATOM   2121 O  O   . LEU   B 1 134 ? 21.574 -20.692 29.376 1.00 13.53 ? 140 LEU   C O   1 
ATOM   2122 C  CB  . LEU   B 1 134 ? 22.688 -18.742 27.738 1.00 12.61 ? 140 LEU   C CB  1 
ATOM   2123 C  CG  . LEU   B 1 134 ? 23.543 -17.788 26.881 1.00 13.16 ? 140 LEU   C CG  1 
ATOM   2124 C  CD1 . LEU   B 1 134 ? 22.973 -17.704 25.425 1.00 14.70 ? 140 LEU   C CD1 1 
ATOM   2125 C  CD2 . LEU   B 1 134 ? 23.650 -16.392 27.499 1.00 15.66 ? 140 LEU   C CD2 1 
ATOM   2126 N  N   . LEU   B 1 135 ? 22.596 -19.988 31.269 1.00 13.02 ? 141 LEU   C N   1 
ATOM   2127 C  CA  . LEU   B 1 135 ? 21.954 -21.014 32.108 1.00 14.40 ? 141 LEU   C CA  1 
ATOM   2128 C  C   . LEU   B 1 135 ? 20.449 -20.913 32.138 1.00 14.34 ? 141 LEU   C C   1 
ATOM   2129 O  O   . LEU   B 1 135 ? 19.768 -21.923 32.332 1.00 15.41 ? 141 LEU   C O   1 
ATOM   2130 C  CB  . LEU   B 1 135 ? 22.536 -21.044 33.550 1.00 14.56 ? 141 LEU   C CB  1 
ATOM   2131 C  CG  . LEU   B 1 135 ? 24.082 -21.014 33.616 1.00 14.54 ? 141 LEU   C CG  1 
ATOM   2132 C  CD1 . LEU   B 1 135 ? 24.593 -21.045 35.094 1.00 15.79 ? 141 LEU   C CD1 1 
ATOM   2133 C  CD2 . LEU   B 1 135 ? 24.720 -22.151 32.830 1.00 15.17 ? 141 LEU   C CD2 1 
ATOM   2134 N  N   . TRP   B 1 136 ? 19.932 -19.700 31.934 1.00 14.87 ? 142 TRP   C N   1 
ATOM   2135 C  CA  . TRP   B 1 136 ? 18.485 -19.449 31.968 1.00 15.26 ? 142 TRP   C CA  1 
ATOM   2136 C  C   . TRP   B 1 136 ? 17.749 -20.149 30.827 1.00 16.21 ? 142 TRP   C C   1 
ATOM   2137 O  O   . TRP   B 1 136 ? 16.528 -20.321 30.910 1.00 17.49 ? 142 TRP   C O   1 
ATOM   2138 C  CB  . TRP   B 1 136 ? 18.225 -17.936 31.959 1.00 15.30 ? 142 TRP   C CB  1 
ATOM   2139 C  CG  . TRP   B 1 136 ? 18.898 -17.192 30.855 1.00 15.00 ? 142 TRP   C CG  1 
ATOM   2140 C  CD1 . TRP   B 1 136 ? 20.083 -16.521 30.916 1.00 15.67 ? 142 TRP   C CD1 1 
ATOM   2141 C  CD2 . TRP   B 1 136 ? 18.377 -16.969 29.523 1.00 15.44 ? 142 TRP   C CD2 1 
ATOM   2142 N  NE1 . TRP   B 1 136 ? 20.356 -15.926 29.696 1.00 16.44 ? 142 TRP   C NE1 1 
ATOM   2143 C  CE2 . TRP   B 1 136 ? 19.326 -16.194 28.826 1.00 16.20 ? 142 TRP   C CE2 1 
ATOM   2144 C  CE3 . TRP   B 1 136 ? 17.227 -17.382 28.863 1.00 15.92 ? 142 TRP   C CE3 1 
ATOM   2145 C  CZ2 . TRP   B 1 136 ? 19.140 -15.802 27.491 1.00 16.21 ? 142 TRP   C CZ2 1 
ATOM   2146 C  CZ3 . TRP   B 1 136 ? 17.024 -16.964 27.558 1.00 16.39 ? 142 TRP   C CZ3 1 
ATOM   2147 C  CH2 . TRP   B 1 136 ? 17.984 -16.208 26.882 1.00 16.19 ? 142 TRP   C CH2 1 
ATOM   2148 N  N   . LEU   B 1 137 ? 18.459 -20.620 29.785 1.00 15.06 ? 143 LEU   C N   1 
ATOM   2149 C  CA  . LEU   B 1 137 ? 17.783 -21.383 28.726 1.00 15.07 ? 143 LEU   C CA  1 
ATOM   2150 C  C   . LEU   B 1 137 ? 17.159 -22.683 29.290 1.00 17.40 ? 143 LEU   C C   1 
ATOM   2151 O  O   . LEU   B 1 137 ? 16.265 -23.246 28.662 1.00 19.33 ? 143 LEU   C O   1 
ATOM   2152 C  CB  . LEU   B 1 137 ? 18.743 -21.741 27.579 1.00 15.01 ? 143 LEU   C CB  1 
ATOM   2153 C  CG  . LEU   B 1 137 ? 19.196 -20.569 26.702 1.00 14.33 ? 143 LEU   C CG  1 
ATOM   2154 C  CD1 . LEU   B 1 137 ? 20.359 -21.001 25.783 1.00 14.70 ? 143 LEU   C CD1 1 
ATOM   2155 C  CD2 . LEU   B 1 137 ? 18.049 -20.013 25.859 1.00 16.10 ? 143 LEU   C CD2 1 
ATOM   2156 N  N   . ASP   B 1 138 ? 17.691 -23.186 30.436 1.00 16.47 ? 144 ASP   C N   1 
ATOM   2157 C  CA  . ASP   B 1 138 ? 17.247 -24.458 31.024 1.00 18.30 ? 144 ASP   C CA  1 
ATOM   2158 C  C   . ASP   B 1 138 ? 16.007 -24.324 31.911 1.00 21.83 ? 144 ASP   C C   1 
ATOM   2159 O  O   . ASP   B 1 138 ? 15.580 -25.336 32.488 1.00 22.86 ? 144 ASP   C O   1 
ATOM   2160 C  CB  . ASP   B 1 138 ? 18.368 -25.104 31.868 1.00 18.29 ? 144 ASP   C CB  1 
ATOM   2161 C  CG  . ASP   B 1 138 ? 19.597 -25.553 31.080 1.00 19.78 ? 144 ASP   C CG  1 
ATOM   2162 O  OD1 . ASP   B 1 138 ? 19.540 -25.564 29.844 1.00 19.75 ? 144 ASP   C OD1 1 
ATOM   2163 O  OD2 . ASP   B 1 138 ? 20.614 -25.900 31.722 1.00 22.35 ? 144 ASP   C OD2 1 
ATOM   2164 N  N   . GLU   B 1 139 ? 15.444 -23.125 32.061 1.00 23.07 ? 145 GLU   C N   1 
ATOM   2165 C  CA  . GLU   B 1 139 ? 14.296 -22.929 32.958 1.00 27.78 ? 145 GLU   C CA  1 
ATOM   2166 C  C   . GLU   B 1 139 ? 13.275 -21.897 32.430 1.00 32.08 ? 145 GLU   C C   1 
ATOM   2167 O  O   . GLU   B 1 139 ? 13.496 -21.284 31.383 1.00 32.76 ? 145 GLU   C O   1 
ATOM   2168 C  CB  . GLU   B 1 139 ? 14.864 -22.443 34.312 1.00 32.41 ? 145 GLU   C CB  1 
ATOM   2169 C  CG  . GLU   B 1 139 ? 15.521 -21.076 34.183 1.00 39.96 ? 145 GLU   C CG  1 
ATOM   2170 C  CD  . GLU   B 1 139 ? 16.548 -20.685 35.229 1.00 49.00 ? 145 GLU   C CD  1 
ATOM   2171 O  OE1 . GLU   B 1 139 ? 16.901 -19.484 35.288 1.00 49.08 ? 145 GLU   C OE1 1 
ATOM   2172 O  OE2 . GLU   B 1 139 ? 16.999 -21.575 35.986 1.00 53.00 ? 145 GLU   C OE2 1 
ATOM   2173 N  N   . GLU   B 1 140 ? 12.193 -21.651 33.222 1.00 34.81 ? 146 GLU   C N   1 
ATOM   2174 C  CA  . GLU   B 1 140 ? 11.181 -20.592 33.055 1.00 37.29 ? 146 GLU   C CA  1 
ATOM   2175 C  C   . GLU   B 1 140 ? 10.584 -20.536 31.667 1.00 39.44 ? 146 GLU   C C   1 
ATOM   2176 O  O   . GLU   B 1 140 ? 10.562 -19.482 31.028 1.00 40.68 ? 146 GLU   C O   1 
ATOM   2177 C  CB  . GLU   B 1 140 ? 11.787 -19.234 33.483 1.00 39.67 ? 146 GLU   C CB  1 
ATOM   2178 C  CG  . GLU   B 1 140 ? 10.957 -17.968 33.266 1.00 48.33 ? 146 GLU   C CG  1 
ATOM   2179 C  CD  . GLU   B 1 140 ? 9.679  -17.826 34.068 1.00 58.02 ? 146 GLU   C CD  1 
ATOM   2180 O  OE1 . GLU   B 1 140 ? 8.748  -17.153 33.570 1.00 60.96 ? 146 GLU   C OE1 1 
ATOM   2181 O  OE2 . GLU   B 1 140 ? 9.607  -18.371 35.193 1.00 61.19 ? 146 GLU   C OE2 1 
HETATM 2182 N  N1  . A1B4G C 2 .   ? 9.348  15.618  21.915 1.00 26.57 ? 201 A1B4G A N1  1 
HETATM 2183 N  N3  . A1B4G C 2 .   ? 5.708  12.403  25.486 1.00 30.18 ? 201 A1B4G A N3  1 
HETATM 2184 C  C4  . A1B4G C 2 .   ? 8.095  15.301  22.599 1.00 27.87 ? 201 A1B4G A C4  1 
HETATM 2185 C  C5  . A1B4G C 2 .   ? 9.157  15.852  20.477 1.00 25.16 ? 201 A1B4G A C5  1 
HETATM 2186 C  C6  . A1B4G C 2 .   ? 10.495 15.838  19.729 1.00 24.26 ? 201 A1B4G A C6  1 
HETATM 2187 C  C7  . A1B4G C 2 .   ? 10.348 16.243  18.273 1.00 22.21 ? 201 A1B4G A C7  1 
HETATM 2188 C  C8  . A1B4G C 2 .   ? 11.453 16.775  20.483 1.00 24.57 ? 201 A1B4G A C8  1 
HETATM 2189 C  C10 . A1B4G C 2 .   ? 10.488 15.783  22.631 1.00 26.70 ? 201 A1B4G A C10 1 
HETATM 2190 C  C13 . A1B4G C 2 .   ? 7.497  11.242  24.108 1.00 28.78 ? 201 A1B4G A C13 1 
HETATM 2191 F  F   . A1B4G C 2 .   ? 9.520  12.976  21.672 1.00 28.95 ? 201 A1B4G A F   1 
HETATM 2192 C  C11 . A1B4G C 2 .   ? 8.651  12.796  22.700 1.00 28.80 ? 201 A1B4G A C11 1 
HETATM 2193 C  C12 . A1B4G C 2 .   ? 8.480  11.505  23.166 1.00 28.77 ? 201 A1B4G A C12 1 
HETATM 2194 C  C14 . A1B4G C 2 .   ? 6.751  12.314  24.573 1.00 29.34 ? 201 A1B4G A C14 1 
HETATM 2195 C  C2  . A1B4G C 2 .   ? 6.948  13.617  24.115 1.00 29.29 ? 201 A1B4G A C2  1 
HETATM 2196 N  N   . A1B4G C 2 .   ? 6.054  14.482  24.733 1.00 30.10 ? 201 A1B4G A N   1 
HETATM 2197 C  C1  . A1B4G C 2 .   ? 5.335  13.712  25.548 1.00 30.42 ? 201 A1B4G A C1  1 
HETATM 2198 C  C   . A1B4G C 2 .   ? 4.244  14.196  26.436 1.00 31.05 ? 201 A1B4G A C   1 
HETATM 2199 C  C3  . A1B4G C 2 .   ? 7.926  13.897  23.146 1.00 28.67 ? 201 A1B4G A C3  1 
HETATM 2200 O  O1  . A1B4G C 2 .   ? 10.531 15.623  23.841 1.00 27.97 ? 201 A1B4G A O1  1 
HETATM 2201 C  C9  . A1B4G C 2 .   ? 11.717 16.246  21.890 1.00 25.58 ? 201 A1B4G A C9  1 
HETATM 2202 O  O   . A1B4G C 2 .   ? 9.731  17.268  17.953 1.00 23.05 ? 201 A1B4G A O   1 
HETATM 2203 N  N2  . A1B4G C 2 .   ? 10.958 15.466  17.391 1.00 18.12 ? 201 A1B4G A N2  1 
HETATM 2204 ZN ZN  . ZN    D 3 .   ? 11.254 -4.196  5.921  1.00 19.55 2 202 ZN    A ZN  1 
HETATM 2205 ZN ZN  . ZN    E 3 .   ? 30.543 -31.094 26.658 1.00 12.32 2 201 ZN    C ZN  1 
HETATM 2206 S  S   . DMS   F 4 .   ? 20.669 -32.231 9.087  1.00 87.75 ? 202 DMS   C S   1 
HETATM 2207 O  O   . DMS   F 4 .   ? 21.874 -32.643 8.298  1.00 87.90 ? 202 DMS   C O   1 
HETATM 2208 C  C1  . DMS   F 4 .   ? 21.149 -32.149 10.824 1.00 87.70 ? 202 DMS   C C1  1 
HETATM 2209 C  C2  . DMS   F 4 .   ? 20.444 -30.444 8.875  1.00 87.70 ? 202 DMS   C C2  1 
HETATM 2210 O  O   . HOH   G 5 .   ? 11.267 8.877   4.312  1.00 21.48 ? 301 HOH   A O   1 
HETATM 2211 O  O   . HOH   G 5 .   ? 1.971  22.896  21.237 1.00 28.08 ? 302 HOH   A O   1 
HETATM 2212 O  O   . HOH   G 5 .   ? 35.267 -3.917  7.720  1.00 22.31 ? 303 HOH   A O   1 
HETATM 2213 O  O   . HOH   G 5 .   ? 8.330  -2.818  31.757 1.00 23.73 ? 304 HOH   A O   1 
HETATM 2214 O  O   . HOH   G 5 .   ? 31.863 6.989   5.486  1.00 30.35 ? 305 HOH   A O   1 
HETATM 2215 O  O   . HOH   G 5 .   ? 12.679 15.755  25.191 1.00 31.19 ? 306 HOH   A O   1 
HETATM 2216 O  O   . HOH   G 5 .   ? 14.101 17.313  4.294  1.00 41.74 ? 307 HOH   A O   1 
HETATM 2217 O  O   . HOH   G 5 .   ? 7.307  20.305  17.377 1.00 21.54 ? 308 HOH   A O   1 
HETATM 2218 O  O   . HOH   G 5 .   ? 3.059  9.489   8.857  1.00 26.50 ? 309 HOH   A O   1 
HETATM 2219 O  O   . HOH   G 5 .   ? 10.526 17.392  25.767 1.00 34.03 ? 310 HOH   A O   1 
HETATM 2220 O  O   . HOH   G 5 .   ? 8.460  -6.410  9.651  1.00 30.81 ? 311 HOH   A O   1 
HETATM 2221 O  O   . HOH   G 5 .   ? 17.343 0.948   28.284 1.00 24.35 ? 312 HOH   A O   1 
HETATM 2222 O  O   . HOH   G 5 .   ? 38.362 4.970   10.647 1.00 47.12 ? 313 HOH   A O   1 
HETATM 2223 O  O   . HOH   G 5 .   ? 30.452 10.563  15.618 1.00 26.79 ? 314 HOH   A O   1 
HETATM 2224 O  O   . HOH   G 5 .   ? 31.207 -2.311  15.446 1.00 50.57 ? 315 HOH   A O   1 
HETATM 2225 O  O   . HOH   G 5 .   ? 12.257 22.073  12.891 1.00 36.98 ? 316 HOH   A O   1 
HETATM 2226 O  O   . HOH   G 5 .   ? 28.083 2.966   5.000  1.00 30.02 ? 317 HOH   A O   1 
HETATM 2227 O  O   . HOH   G 5 .   ? 35.401 7.968   9.557  1.00 50.30 ? 318 HOH   A O   1 
HETATM 2228 O  O   . HOH   G 5 .   ? 29.403 22.256  19.322 1.00 24.89 ? 319 HOH   A O   1 
HETATM 2229 O  O   . HOH   G 5 .   ? 0.453  -0.899  19.378 1.00 22.70 ? 320 HOH   A O   1 
HETATM 2230 O  O   . HOH   G 5 .   ? 19.334 10.102  19.603 1.00 12.05 ? 321 HOH   A O   1 
HETATM 2231 O  O   . HOH   G 5 .   ? 19.609 20.107  21.862 1.00 36.53 ? 322 HOH   A O   1 
HETATM 2232 O  O   . HOH   G 5 .   ? 14.809 11.384  0.108  1.00 30.88 ? 323 HOH   A O   1 
HETATM 2233 O  O   . HOH   G 5 .   ? 2.586  -2.797  20.707 1.00 26.97 ? 324 HOH   A O   1 
HETATM 2234 O  O   . HOH   G 5 .   ? 19.902 20.057  5.699  1.00 42.12 ? 325 HOH   A O   1 
HETATM 2235 O  O   . HOH   G 5 .   ? 27.785 8.105   1.630  1.00 32.80 ? 326 HOH   A O   1 
HETATM 2236 O  O   . HOH   G 5 .   ? 12.605 -5.885  30.427 1.00 40.56 ? 327 HOH   A O   1 
HETATM 2237 O  O   . HOH   G 5 .   ? 23.365 21.668  7.132  1.00 22.81 ? 328 HOH   A O   1 
HETATM 2238 O  O   . HOH   G 5 .   ? 36.347 -2.503  10.895 1.00 27.54 ? 329 HOH   A O   1 
HETATM 2239 O  O   . HOH   G 5 .   ? 4.599  -3.583  28.861 1.00 26.85 ? 330 HOH   A O   1 
HETATM 2240 O  O   . HOH   G 5 .   ? 19.500 16.729  26.219 1.00 45.93 ? 331 HOH   A O   1 
HETATM 2241 O  O   . HOH   G 5 .   ? 10.494 10.186  31.364 1.00 21.88 ? 332 HOH   A O   1 
HETATM 2242 O  O   . HOH   G 5 .   ? -0.086 1.335   15.758 1.00 12.66 ? 333 HOH   A O   1 
HETATM 2243 O  O   . HOH   G 5 .   ? 4.524  10.458  27.291 1.00 31.06 ? 334 HOH   A O   1 
HETATM 2244 O  O   . HOH   G 5 .   ? 22.627 0.884   17.365 1.00 16.08 ? 335 HOH   A O   1 
HETATM 2245 O  O   . HOH   G 5 .   ? 8.590  19.072  19.627 1.00 20.24 ? 336 HOH   A O   1 
HETATM 2246 O  O   . HOH   G 5 .   ? 33.632 11.022  15.561 1.00 37.09 ? 337 HOH   A O   1 
HETATM 2247 O  O   . HOH   G 5 .   ? 33.770 14.135  9.604  1.00 32.58 ? 338 HOH   A O   1 
HETATM 2248 O  O   . HOH   G 5 .   ? 23.172 -6.324  11.889 1.00 31.64 ? 339 HOH   A O   1 
HETATM 2249 O  O   . HOH   G 5 .   ? 14.156 13.741  23.930 1.00 18.44 ? 340 HOH   A O   1 
HETATM 2250 O  O   . HOH   G 5 .   ? -1.124 -4.316  11.016 1.00 58.19 ? 341 HOH   A O   1 
HETATM 2251 O  O   . HOH   G 5 .   ? 24.883 5.162   21.448 1.00 28.35 ? 342 HOH   A O   1 
HETATM 2252 O  O   . HOH   G 5 .   ? 3.070  20.860  24.248 1.00 38.95 ? 343 HOH   A O   1 
HETATM 2253 O  O   . HOH   G 5 .   ? 10.734 5.455   3.312  1.00 27.01 ? 344 HOH   A O   1 
HETATM 2254 O  O   . HOH   G 5 .   ? 1.481  5.569   27.018 1.00 32.91 ? 345 HOH   A O   1 
HETATM 2255 O  O   . HOH   G 5 .   ? 35.232 10.877  12.302 1.00 48.01 ? 346 HOH   A O   1 
HETATM 2256 O  O   . HOH   G 5 .   ? 4.985  14.593  20.224 1.00 28.46 ? 347 HOH   A O   1 
HETATM 2257 O  O   . HOH   G 5 .   ? 20.893 -4.112  14.139 1.00 15.99 ? 348 HOH   A O   1 
HETATM 2258 O  O   . HOH   G 5 .   ? 20.788 -1.283  3.190  1.00 31.08 ? 349 HOH   A O   1 
HETATM 2259 O  O   . HOH   G 5 .   ? 15.762 23.998  14.657 1.00 38.62 ? 350 HOH   A O   1 
HETATM 2260 O  O   . HOH   G 5 .   ? 11.311 12.694  11.076 1.00 14.89 ? 351 HOH   A O   1 
HETATM 2261 O  O   . HOH   G 5 .   ? 8.292  24.778  23.737 1.00 25.05 ? 352 HOH   A O   1 
HETATM 2262 O  O   . HOH   G 5 .   ? 21.453 4.889   24.654 1.00 42.67 ? 353 HOH   A O   1 
HETATM 2263 O  O   . HOH   G 5 .   ? 13.724 4.037   23.480 1.00 11.59 ? 354 HOH   A O   1 
HETATM 2264 O  O   . HOH   G 5 .   ? 16.552 3.911   23.657 1.00 16.46 ? 355 HOH   A O   1 
HETATM 2265 O  O   . HOH   G 5 .   ? 31.578 19.896  11.694 1.00 20.84 ? 356 HOH   A O   1 
HETATM 2266 O  O   . HOH   G 5 .   ? 30.549 2.956   14.858 1.00 21.47 ? 357 HOH   A O   1 
HETATM 2267 O  O   . HOH   G 5 .   ? 33.967 -2.363  13.502 1.00 34.76 ? 358 HOH   A O   1 
HETATM 2268 O  O   . HOH   G 5 .   ? 28.949 3.385   12.676 1.00 15.68 ? 359 HOH   A O   1 
HETATM 2269 O  O   . HOH   G 5 .   ? 3.851  12.883  17.783 1.00 30.20 ? 360 HOH   A O   1 
HETATM 2270 O  O   . HOH   G 5 .   ? 29.830 11.596  18.524 1.00 25.99 ? 361 HOH   A O   1 
HETATM 2271 O  O   . HOH   G 5 .   ? 18.359 21.909  9.534  1.00 18.32 ? 362 HOH   A O   1 
HETATM 2272 O  O   . HOH   G 5 .   ? 29.945 -1.407  8.668  1.00 33.29 ? 363 HOH   A O   1 
HETATM 2273 O  O   . HOH   G 5 .   ? 20.380 17.924  23.970 1.00 40.01 ? 364 HOH   A O   1 
HETATM 2274 O  O   . HOH   G 5 .   ? 20.806 -2.549  16.835 1.00 14.88 ? 365 HOH   A O   1 
HETATM 2275 O  O   . HOH   G 5 .   ? 36.797 2.365   10.108 1.00 36.13 ? 366 HOH   A O   1 
HETATM 2276 O  O   . HOH   G 5 .   ? 4.994  8.232   2.316  1.00 29.46 ? 367 HOH   A O   1 
HETATM 2277 O  O   . HOH   G 5 .   ? 29.381 11.921  21.317 1.00 30.18 ? 368 HOH   A O   1 
HETATM 2278 O  O   . HOH   G 5 .   ? 6.599  -6.881  23.793 1.00 23.09 ? 369 HOH   A O   1 
HETATM 2279 O  O   . HOH   G 5 .   ? 12.103 11.187  29.603 1.00 21.46 ? 370 HOH   A O   1 
HETATM 2280 O  O   . HOH   G 5 .   ? 9.504  4.050   33.436 1.00 13.29 ? 371 HOH   A O   1 
HETATM 2281 O  O   . HOH   G 5 .   ? 11.597 18.013  4.781  1.00 36.64 ? 372 HOH   A O   1 
HETATM 2282 O  O   . HOH   G 5 .   ? 23.439 11.707  21.879 1.00 28.87 ? 373 HOH   A O   1 
HETATM 2283 O  O   . HOH   G 5 .   ? 0.703  -0.969  9.117  1.00 32.57 ? 374 HOH   A O   1 
HETATM 2284 O  O   . HOH   G 5 .   ? 16.939 -3.512  27.739 1.00 33.12 ? 375 HOH   A O   1 
HETATM 2285 O  O   . HOH   G 5 .   ? 12.605 16.525  27.917 1.00 33.84 ? 376 HOH   A O   1 
HETATM 2286 O  O   . HOH   G 5 .   ? 16.309 9.367   -1.586 1.00 20.62 ? 377 HOH   A O   1 
HETATM 2287 O  O   . HOH   G 5 .   ? 17.543 20.007  16.973 1.00 15.11 ? 378 HOH   A O   1 
HETATM 2288 O  O   . HOH   G 5 .   ? 22.893 -0.633  5.407  1.00 20.75 ? 379 HOH   A O   1 
HETATM 2289 O  O   . HOH   G 5 .   ? 32.215 2.069   6.061  1.00 33.32 ? 380 HOH   A O   1 
HETATM 2290 O  O   . HOH   G 5 .   ? 26.971 -1.254  8.895  1.00 26.08 ? 381 HOH   A O   1 
HETATM 2291 O  O   . HOH   G 5 .   ? 14.436 -2.371  17.943 1.00 17.73 ? 382 HOH   A O   1 
HETATM 2292 O  O   . HOH   G 5 .   ? 25.375 19.596  21.677 1.00 27.19 ? 383 HOH   A O   1 
HETATM 2293 O  O   . HOH   G 5 .   ? 21.840 2.406   -0.885 1.00 31.09 ? 384 HOH   A O   1 
HETATM 2294 O  O   . HOH   G 5 .   ? 5.621  16.969  21.372 1.00 27.56 ? 385 HOH   A O   1 
HETATM 2295 O  O   . HOH   G 5 .   ? 3.925  -4.011  6.047  1.00 27.75 ? 386 HOH   A O   1 
HETATM 2296 O  O   . HOH   G 5 .   ? 30.913 15.637  22.759 1.00 23.26 ? 387 HOH   A O   1 
HETATM 2297 O  O   . HOH   G 5 .   ? 32.779 16.487  9.107  1.00 32.98 ? 388 HOH   A O   1 
HETATM 2298 O  O   . HOH   G 5 .   ? 19.403 2.966   19.402 1.00 19.19 ? 389 HOH   A O   1 
HETATM 2299 O  O   . HOH   G 5 .   ? 13.223 11.426  9.170  1.00 12.98 ? 390 HOH   A O   1 
HETATM 2300 O  O   . HOH   G 5 .   ? 4.096  0.352   23.979 1.00 18.69 ? 391 HOH   A O   1 
HETATM 2301 O  O   . HOH   G 5 .   ? 5.395  5.453   32.639 1.00 22.31 ? 392 HOH   A O   1 
HETATM 2302 O  O   . HOH   G 5 .   ? 36.494 18.125  14.525 1.00 29.38 ? 393 HOH   A O   1 
HETATM 2303 O  O   . HOH   G 5 .   ? 16.959 6.252   27.022 1.00 26.09 ? 394 HOH   A O   1 
HETATM 2304 O  O   . HOH   G 5 .   ? 31.976 8.728   7.660  1.00 23.98 ? 395 HOH   A O   1 
HETATM 2305 O  O   . HOH   G 5 .   ? 2.593  15.990  19.122 1.00 28.42 ? 396 HOH   A O   1 
HETATM 2306 O  O   . HOH   G 5 .   ? 15.210 -5.025  0.472  1.00 40.58 ? 397 HOH   A O   1 
HETATM 2307 O  O   . HOH   G 5 .   ? 28.834 15.725  4.188  1.00 32.45 ? 398 HOH   A O   1 
HETATM 2308 O  O   . HOH   G 5 .   ? 11.438 -6.982  24.782 1.00 28.86 ? 399 HOH   A O   1 
HETATM 2309 O  O   . HOH   G 5 .   ? 16.408 21.307  19.087 1.00 26.98 ? 400 HOH   A O   1 
HETATM 2310 O  O   . HOH   G 5 .   ? 0.200  5.918   6.007  1.00 26.98 ? 401 HOH   A O   1 
HETATM 2311 O  O   . HOH   G 5 .   ? 30.407 4.523   5.748  1.00 22.37 ? 402 HOH   A O   1 
HETATM 2312 O  O   . HOH   G 5 .   ? 27.252 -1.315  15.923 1.00 26.87 ? 403 HOH   A O   1 
HETATM 2313 O  O   . HOH   G 5 .   ? 1.760  10.911  27.527 1.00 40.92 ? 404 HOH   A O   1 
HETATM 2314 O  O   . HOH   G 5 .   ? 17.680 10.758  26.120 1.00 21.28 ? 405 HOH   A O   1 
HETATM 2315 O  O   . HOH   G 5 .   ? 7.064  26.430  14.272 1.00 37.34 ? 406 HOH   A O   1 
HETATM 2316 O  O   . HOH   G 5 .   ? 15.135 15.047  3.216  1.00 30.81 ? 407 HOH   A O   1 
HETATM 2317 O  O   . HOH   G 5 .   ? 5.062  26.447  19.932 1.00 25.17 ? 408 HOH   A O   1 
HETATM 2318 O  O   . HOH   G 5 .   ? 33.910 18.636  10.743 1.00 27.03 ? 409 HOH   A O   1 
HETATM 2319 O  O   . HOH   G 5 .   ? 5.959  -3.608  31.417 1.00 28.72 ? 410 HOH   A O   1 
HETATM 2320 O  O   . HOH   G 5 .   ? 19.872 13.238  2.202  1.00 31.33 ? 411 HOH   A O   1 
HETATM 2321 O  O   . HOH   G 5 .   ? 2.962  0.555   28.936 1.00 42.27 ? 412 HOH   A O   1 
HETATM 2322 O  O   . HOH   G 5 .   ? 19.929 24.981  15.298 1.00 43.24 ? 413 HOH   A O   1 
HETATM 2323 O  O   . HOH   G 5 .   ? 22.468 19.413  19.683 1.00 29.29 ? 414 HOH   A O   1 
HETATM 2324 O  O   . HOH   G 5 .   ? 36.232 -0.417  12.587 1.00 32.12 ? 415 HOH   A O   1 
HETATM 2325 O  O   . HOH   G 5 .   ? 17.679 24.447  10.515 1.00 33.98 ? 416 HOH   A O   1 
HETATM 2326 O  O   . HOH   G 5 .   ? 9.148  2.924   2.818  1.00 31.24 ? 417 HOH   A O   1 
HETATM 2327 O  O   . HOH   G 5 .   ? 30.965 19.323  8.726  1.00 41.29 ? 418 HOH   A O   1 
HETATM 2328 O  O   . HOH   G 5 .   ? 27.851 17.614  24.172 1.00 22.32 ? 419 HOH   A O   1 
HETATM 2329 O  O   . HOH   G 5 .   ? 35.584 11.886  17.402 1.00 42.93 ? 420 HOH   A O   1 
HETATM 2330 O  O   . HOH   G 5 .   ? 25.105 17.899  4.576  1.00 34.41 ? 421 HOH   A O   1 
HETATM 2331 O  O   . HOH   G 5 .   ? 35.862 15.244  10.969 1.00 40.43 ? 422 HOH   A O   1 
HETATM 2332 O  O   . HOH   G 5 .   ? 8.179  6.651   33.732 1.00 19.42 ? 423 HOH   A O   1 
HETATM 2333 O  O   . HOH   G 5 .   ? 18.126 17.781  4.152  1.00 32.62 ? 424 HOH   A O   1 
HETATM 2334 O  O   . HOH   G 5 .   ? 3.153  7.800   24.398 1.00 23.03 ? 425 HOH   A O   1 
HETATM 2335 O  O   . HOH   G 5 .   ? 6.145  23.951  10.551 1.00 33.19 ? 426 HOH   A O   1 
HETATM 2336 O  O   . HOH   G 5 .   ? 24.270 -3.455  16.180 1.00 34.98 ? 427 HOH   A O   1 
HETATM 2337 O  O   . HOH   G 5 .   ? 25.065 10.600  22.891 1.00 37.98 ? 428 HOH   A O   1 
HETATM 2338 O  O   . HOH   G 5 .   ? 33.969 5.180   16.599 1.00 31.55 ? 429 HOH   A O   1 
HETATM 2339 O  O   . HOH   G 5 .   ? 17.461 0.746   20.246 1.00 18.60 ? 430 HOH   A O   1 
HETATM 2340 O  O   . HOH   G 5 .   ? 23.199 19.093  6.282  1.00 19.53 ? 431 HOH   A O   1 
HETATM 2341 O  O   . HOH   G 5 .   ? 7.340  13.825  4.630  1.00 22.79 ? 432 HOH   A O   1 
HETATM 2342 O  O   . HOH   G 5 .   ? 2.105  14.453  16.801 1.00 28.20 ? 433 HOH   A O   1 
HETATM 2343 O  O   . HOH   G 5 .   ? 3.339  -0.297  21.285 1.00 25.72 ? 434 HOH   A O   1 
HETATM 2344 O  O   . HOH   G 5 .   ? 0.485  -1.221  16.677 1.00 19.52 ? 435 HOH   A O   1 
HETATM 2345 O  O   . HOH   G 5 .   ? 16.758 -4.100  2.880  1.00 26.10 ? 436 HOH   A O   1 
HETATM 2346 O  O   . HOH   G 5 .   ? -1.065 16.375  14.008 1.00 38.98 ? 437 HOH   A O   1 
HETATM 2347 O  O   . HOH   G 5 .   ? 2.085  13.850  4.469  1.00 36.12 ? 438 HOH   A O   1 
HETATM 2348 O  O   . HOH   G 5 .   ? 15.272 21.725  8.088  1.00 31.48 ? 439 HOH   A O   1 
HETATM 2349 O  O   . HOH   G 5 .   ? 20.990 9.979   21.896 1.00 15.54 ? 440 HOH   A O   1 
HETATM 2350 O  O   . HOH   G 5 .   ? 36.579 16.144  16.638 1.00 34.56 ? 441 HOH   A O   1 
HETATM 2351 O  O   . HOH   G 5 .   ? 16.924 -5.598  12.170 1.00 28.76 ? 442 HOH   A O   1 
HETATM 2352 O  O   . HOH   G 5 .   ? 22.704 3.436   20.879 1.00 21.47 ? 443 HOH   A O   1 
HETATM 2353 O  O   . HOH   G 5 .   ? 19.744 9.216   -0.901 1.00 27.30 ? 444 HOH   A O   1 
HETATM 2354 O  O   . HOH   G 5 .   ? 34.079 7.867   16.627 1.00 33.34 ? 445 HOH   A O   1 
HETATM 2355 O  O   . HOH   G 5 .   ? 5.233  17.454  24.060 1.00 47.79 ? 446 HOH   A O   1 
HETATM 2356 O  O   . HOH   G 5 .   ? 23.318 8.269   21.696 1.00 25.19 ? 447 HOH   A O   1 
HETATM 2357 O  O   . HOH   G 5 .   ? 1.071  -5.013  17.466 1.00 36.17 ? 448 HOH   A O   1 
HETATM 2358 O  O   . HOH   G 5 .   ? 17.168 -2.376  19.641 1.00 17.59 ? 449 HOH   A O   1 
HETATM 2359 O  O   . HOH   G 5 .   ? 20.907 -4.824  11.463 1.00 28.81 ? 450 HOH   A O   1 
HETATM 2360 O  O   . HOH   G 5 .   ? 22.966 16.762  23.806 1.00 47.53 ? 451 HOH   A O   1 
HETATM 2361 O  O   . HOH   G 5 .   ? 8.047  11.354  31.523 1.00 37.03 ? 452 HOH   A O   1 
HETATM 2362 O  O   . HOH   G 5 .   ? 8.600  21.009  7.588  1.00 43.89 ? 453 HOH   A O   1 
HETATM 2363 O  O   . HOH   G 5 .   ? -0.761 15.475  11.605 1.00 28.97 ? 454 HOH   A O   1 
HETATM 2364 O  O   . HOH   G 5 .   ? 1.960  12.384  20.013 1.00 44.70 ? 455 HOH   A O   1 
HETATM 2365 O  O   . HOH   G 5 .   ? 25.358 -1.038  16.716 1.00 38.54 ? 456 HOH   A O   1 
HETATM 2366 O  O   . HOH   G 5 .   ? 0.625  7.838   27.923 1.00 39.31 ? 457 HOH   A O   1 
HETATM 2367 O  O   . HOH   G 5 .   ? 0.858  3.641   25.951 1.00 35.52 ? 458 HOH   A O   1 
HETATM 2368 O  O   . HOH   G 5 .   ? 15.955 13.042  26.037 1.00 25.71 ? 459 HOH   A O   1 
HETATM 2369 O  O   . HOH   G 5 .   ? 16.671 -5.017  34.251 1.00 31.12 ? 460 HOH   A O   1 
HETATM 2370 O  O   . HOH   G 5 .   ? 11.679 24.267  14.555 1.00 36.40 ? 461 HOH   A O   1 
HETATM 2371 O  O   . HOH   G 5 .   ? 18.540 2.212   22.605 1.00 32.27 ? 462 HOH   A O   1 
HETATM 2372 O  O   . HOH   G 5 .   ? 13.841 -6.836  25.644 1.00 48.34 ? 463 HOH   A O   1 
HETATM 2373 O  O   . HOH   G 5 .   ? 7.092  21.389  26.903 1.00 42.09 ? 464 HOH   A O   1 
HETATM 2374 O  O   . HOH   G 5 .   ? 2.490  -0.075  26.279 1.00 33.81 ? 465 HOH   A O   1 
HETATM 2375 O  O   . HOH   G 5 .   ? 0.076  0.157   23.063 1.00 29.97 ? 466 HOH   A O   1 
HETATM 2376 O  O   . HOH   G 5 .   ? 29.655 0.729   16.615 1.00 29.09 ? 467 HOH   A O   1 
HETATM 2377 O  O   . HOH   G 5 .   ? 23.764 1.059   19.805 1.00 37.64 ? 468 HOH   A O   1 
HETATM 2378 O  O   . HOH   G 5 .   ? 21.438 11.494  24.343 1.00 47.41 ? 469 HOH   A O   1 
HETATM 2379 O  O   . HOH   G 5 .   ? 27.513 10.383  -0.031 1.00 53.59 ? 470 HOH   A O   1 
HETATM 2380 O  O   . HOH   G 5 .   ? 21.179 2.985   23.077 1.00 33.47 ? 471 HOH   A O   1 
HETATM 2381 O  O   . HOH   G 5 .   ? 30.387 7.039   17.850 1.00 39.15 ? 472 HOH   A O   1 
HETATM 2382 O  O   . HOH   G 5 .   ? -0.400 13.819  17.148 1.00 36.42 ? 473 HOH   A O   1 
HETATM 2383 O  O   . HOH   G 5 .   ? 12.266 -4.993  33.045 1.00 29.96 ? 474 HOH   A O   1 
HETATM 2384 O  O   . HOH   G 5 .   ? 31.278 4.587   17.015 1.00 24.19 ? 475 HOH   A O   1 
HETATM 2385 O  O   . HOH   G 5 .   ? 37.587 -4.600  6.597  1.00 28.95 ? 476 HOH   A O   1 
HETATM 2386 O  O   . HOH   G 5 .   ? 21.282 -0.961  18.933 1.00 29.53 ? 477 HOH   A O   1 
HETATM 2387 O  O   . HOH   G 5 .   ? 8.869  24.685  10.897 1.00 41.83 ? 478 HOH   A O   1 
HETATM 2388 O  O   . HOH   G 5 .   ? 39.258 -2.602  10.687 1.00 39.74 ? 479 HOH   A O   1 
HETATM 2389 O  O   . HOH   G 5 .   ? 29.011 1.422   19.098 1.00 51.96 ? 480 HOH   A O   1 
HETATM 2390 O  O   . HOH   G 5 .   ? 1.274  16.506  3.167  1.00 45.78 ? 481 HOH   A O   1 
HETATM 2391 O  O   . HOH   G 5 .   ? 9.750  26.010  13.894 1.00 44.57 ? 482 HOH   A O   1 
HETATM 2392 O  O   . HOH   G 5 .   ? 0.133  14.009  19.072 1.00 32.16 ? 483 HOH   A O   1 
HETATM 2393 O  O   . HOH   G 5 .   ? 26.626 0.350   19.917 1.00 47.75 ? 484 HOH   A O   1 
HETATM 2394 O  O   . HOH   H 5 .   ? 9.927  -19.960 28.742 1.00 36.86 ? 301 HOH   C O   1 
HETATM 2395 O  O   . HOH   H 5 .   ? 31.448 -17.788 -0.008 1.00 40.77 ? 302 HOH   C O   1 
HETATM 2396 O  O   . HOH   H 5 .   ? 17.504 -33.339 24.021 1.00 36.44 ? 303 HOH   C O   1 
HETATM 2397 O  O   . HOH   H 5 .   ? 38.491 -18.568 21.493 1.00 23.85 ? 304 HOH   C O   1 
HETATM 2398 O  O   . HOH   H 5 .   ? 38.162 -7.361  6.888  1.00 20.83 ? 305 HOH   C O   1 
HETATM 2399 O  O   . HOH   H 5 .   ? 29.226 -25.787 -1.213 1.00 27.17 ? 306 HOH   C O   1 
HETATM 2400 O  O   . HOH   H 5 .   ? 14.521 -18.666 31.793 1.00 37.24 ? 307 HOH   C O   1 
HETATM 2401 O  O   . HOH   H 5 .   ? 16.545 -15.609 8.435  1.00 53.19 ? 308 HOH   C O   1 
HETATM 2402 O  O   . HOH   H 5 .   ? 24.493 -9.881  26.862 1.00 36.94 ? 309 HOH   C O   1 
HETATM 2403 O  O   . HOH   H 5 .   ? 10.112 -17.513 18.279 1.00 25.75 ? 310 HOH   C O   1 
HETATM 2404 O  O   . HOH   H 5 .   ? 17.795 -6.022  24.030 1.00 25.05 ? 311 HOH   C O   1 
HETATM 2405 O  O   . HOH   H 5 .   ? 30.631 -18.101 26.791 1.00 17.66 ? 312 HOH   C O   1 
HETATM 2406 O  O   . HOH   H 5 .   ? 42.495 -11.166 10.988 1.00 33.05 ? 313 HOH   C O   1 
HETATM 2407 O  O   . HOH   H 5 .   ? 19.646 -4.116  20.108 1.00 20.52 ? 314 HOH   C O   1 
HETATM 2408 O  O   . HOH   H 5 .   ? 16.241 -17.187 10.858 1.00 35.42 ? 315 HOH   C O   1 
HETATM 2409 O  O   . HOH   H 5 .   ? 24.503 -5.880  15.046 1.00 33.69 ? 316 HOH   C O   1 
HETATM 2410 O  O   . HOH   H 5 .   ? 18.935 -32.299 19.740 1.00 36.82 ? 317 HOH   C O   1 
HETATM 2411 O  O   . HOH   H 5 .   ? 35.928 -17.641 11.557 1.00 26.86 ? 318 HOH   C O   1 
HETATM 2412 O  O   . HOH   H 5 .   ? 22.769 -5.929  21.002 1.00 18.78 ? 319 HOH   C O   1 
HETATM 2413 O  O   . HOH   H 5 .   ? 36.048 -26.066 34.145 1.00 31.96 ? 320 HOH   C O   1 
HETATM 2414 O  O   . HOH   H 5 .   ? 18.465 -8.857  13.605 1.00 27.94 ? 321 HOH   C O   1 
HETATM 2415 O  O   . HOH   H 5 .   ? 20.591 -18.762 12.711 1.00 12.94 ? 322 HOH   C O   1 
HETATM 2416 O  O   . HOH   H 5 .   ? 44.073 -19.145 9.304  1.00 35.45 ? 323 HOH   C O   1 
HETATM 2417 O  O   . HOH   H 5 .   ? 21.871 -28.779 4.733  1.00 24.05 ? 324 HOH   C O   1 
HETATM 2418 O  O   . HOH   H 5 .   ? 28.014 -5.133  18.536 1.00 37.02 ? 325 HOH   C O   1 
HETATM 2419 O  O   . HOH   H 5 .   ? 37.333 -31.890 10.906 1.00 23.17 ? 326 HOH   C O   1 
HETATM 2420 O  O   . HOH   H 5 .   ? 14.670 -23.968 12.199 1.00 33.14 ? 327 HOH   C O   1 
HETATM 2421 O  O   . HOH   H 5 .   ? 7.123  -30.353 21.919 1.00 26.95 ? 328 HOH   C O   1 
HETATM 2422 O  O   . HOH   H 5 .   ? 17.792 -27.577 16.423 1.00 16.87 ? 329 HOH   C O   1 
HETATM 2423 O  O   . HOH   H 5 .   ? 35.791 -28.387 2.891  1.00 38.49 ? 330 HOH   C O   1 
HETATM 2424 O  O   . HOH   H 5 .   ? 35.262 -32.622 3.272  1.00 35.15 ? 331 HOH   C O   1 
HETATM 2425 O  O   . HOH   H 5 .   ? 26.493 -5.471  9.956  1.00 25.14 ? 332 HOH   C O   1 
HETATM 2426 O  O   . HOH   H 5 .   ? 21.593 -26.058 34.253 1.00 25.79 ? 333 HOH   C O   1 
HETATM 2427 O  O   . HOH   H 5 .   ? 30.957 -23.880 -1.292 1.00 23.71 ? 334 HOH   C O   1 
HETATM 2428 O  O   . HOH   H 5 .   ? 24.661 -15.715 7.246  1.00 18.26 ? 335 HOH   C O   1 
HETATM 2429 O  O   . HOH   H 5 .   ? 37.098 -18.644 28.110 1.00 24.99 ? 336 HOH   C O   1 
HETATM 2430 O  O   . HOH   H 5 .   ? 40.383 -27.198 15.133 1.00 12.17 ? 337 HOH   C O   1 
HETATM 2431 O  O   . HOH   H 5 .   ? 38.196 -25.965 28.282 1.00 31.76 ? 338 HOH   C O   1 
HETATM 2432 O  O   . HOH   H 5 .   ? 13.781 -24.238 29.267 1.00 31.82 ? 339 HOH   C O   1 
HETATM 2433 O  O   . HOH   H 5 .   ? 14.627 -28.801 25.634 1.00 43.53 ? 340 HOH   C O   1 
HETATM 2434 O  O   . HOH   H 5 .   ? 40.013 -29.523 11.895 1.00 22.24 ? 341 HOH   C O   1 
HETATM 2435 O  O   . HOH   H 5 .   ? 30.851 -21.443 28.345 1.00 16.38 ? 342 HOH   C O   1 
HETATM 2436 O  O   . HOH   H 5 .   ? 10.277 -17.001 15.063 1.00 29.97 ? 343 HOH   C O   1 
HETATM 2437 O  O   . HOH   H 5 .   ? 37.091 -10.672 4.812  1.00 35.82 ? 344 HOH   C O   1 
HETATM 2438 O  O   . HOH   H 5 .   ? 29.735 -15.214 19.516 1.00 15.38 ? 345 HOH   C O   1 
HETATM 2439 O  O   . HOH   H 5 .   ? 21.184 -24.967 4.000  1.00 37.35 ? 346 HOH   C O   1 
HETATM 2440 O  O   . HOH   H 5 .   ? 9.875  -8.772  23.742 1.00 28.28 ? 347 HOH   C O   1 
HETATM 2441 O  O   . HOH   H 5 .   ? 16.805 -9.591  27.696 1.00 35.61 ? 348 HOH   C O   1 
HETATM 2442 O  O   . HOH   H 5 .   ? 23.780 -8.132  9.430  1.00 24.33 ? 349 HOH   C O   1 
HETATM 2443 O  O   . HOH   H 5 .   ? 35.020 -13.113 8.570  1.00 18.87 ? 350 HOH   C O   1 
HETATM 2444 O  O   . HOH   H 5 .   ? 32.382 -23.604 29.040 1.00 16.94 ? 351 HOH   C O   1 
HETATM 2445 O  O   . HOH   H 5 .   ? 5.723  -16.740 22.403 1.00 55.73 ? 352 HOH   C O   1 
HETATM 2446 O  O   . HOH   H 5 .   ? 25.904 -25.287 8.712  1.00 12.23 ? 353 HOH   C O   1 
HETATM 2447 O  O   . HOH   H 5 .   ? 25.689 -37.790 24.267 1.00 29.88 ? 354 HOH   C O   1 
HETATM 2448 O  O   . HOH   H 5 .   ? 31.065 -6.097  5.681  1.00 36.12 ? 355 HOH   C O   1 
HETATM 2449 O  O   . HOH   H 5 .   ? 20.656 -25.676 13.790 1.00 20.28 ? 356 HOH   C O   1 
HETATM 2450 O  O   . HOH   H 5 .   ? 19.053 -27.667 28.062 1.00 18.41 ? 357 HOH   C O   1 
HETATM 2451 O  O   . HOH   H 5 .   ? 11.773 -24.285 21.596 1.00 16.31 ? 358 HOH   C O   1 
HETATM 2452 O  O   . HOH   H 5 .   ? 6.775  -9.185  22.536 1.00 33.29 ? 359 HOH   C O   1 
HETATM 2453 O  O   . HOH   H 5 .   ? 36.185 -21.263 6.790  1.00 23.59 ? 360 HOH   C O   1 
HETATM 2454 O  O   . HOH   H 5 .   ? 17.421 -24.113 8.521  1.00 37.71 ? 361 HOH   C O   1 
HETATM 2455 O  O   . HOH   H 5 .   ? 31.912 -10.418 13.702 1.00 20.27 ? 362 HOH   C O   1 
HETATM 2456 O  O   . HOH   H 5 .   ? 13.034 -29.573 19.123 1.00 28.88 ? 363 HOH   C O   1 
HETATM 2457 O  O   . HOH   H 5 .   ? 9.055  -7.939  21.139 1.00 23.37 ? 364 HOH   C O   1 
HETATM 2458 O  O   . HOH   H 5 .   ? 41.142 -25.017 7.139  1.00 30.36 ? 365 HOH   C O   1 
HETATM 2459 O  O   . HOH   H 5 .   ? 10.940 -21.870 13.577 1.00 43.24 ? 366 HOH   C O   1 
HETATM 2460 O  O   . HOH   H 5 .   ? 27.084 -35.614 20.770 1.00 24.48 ? 367 HOH   C O   1 
HETATM 2461 O  O   . HOH   H 5 .   ? 34.028 -33.643 24.088 1.00 36.09 ? 368 HOH   C O   1 
HETATM 2462 O  O   . HOH   H 5 .   ? 26.136 -15.182 30.741 1.00 32.99 ? 369 HOH   C O   1 
HETATM 2463 O  O   . HOH   H 5 .   ? 29.572 -13.076 12.872 1.00 15.99 ? 370 HOH   C O   1 
HETATM 2464 O  O   . HOH   H 5 .   ? 33.252 -32.907 0.799  1.00 40.24 ? 371 HOH   C O   1 
HETATM 2465 O  O   . HOH   H 5 .   ? 23.695 -3.341  18.790 1.00 38.03 ? 372 HOH   C O   1 
HETATM 2466 O  O   . HOH   H 5 .   ? 22.752 -8.532  13.911 1.00 15.14 ? 373 HOH   C O   1 
HETATM 2467 O  O   . HOH   H 5 .   ? 34.379 -23.132 -0.796 1.00 39.83 ? 374 HOH   C O   1 
HETATM 2468 O  O   . HOH   H 5 .   ? 34.859 -34.851 18.064 1.00 28.04 ? 375 HOH   C O   1 
HETATM 2469 O  O   . HOH   H 5 .   ? 36.479 -16.104 12.525 1.00 31.86 ? 376 HOH   C O   1 
HETATM 2470 O  O   . HOH   H 5 .   ? 10.428 -16.999 12.274 1.00 33.57 ? 377 HOH   C O   1 
HETATM 2471 O  O   . HOH   H 5 .   ? 13.038 -11.254 28.398 1.00 37.82 ? 378 HOH   C O   1 
HETATM 2472 O  O   . HOH   H 5 .   ? 23.063 -25.397 8.874  1.00 18.54 ? 379 HOH   C O   1 
HETATM 2473 O  O   . HOH   H 5 .   ? 29.766 -15.871 30.443 1.00 29.82 ? 380 HOH   C O   1 
HETATM 2474 O  O   . HOH   H 5 .   ? 4.310  -16.186 16.816 1.00 44.71 ? 381 HOH   C O   1 
HETATM 2475 O  O   . HOH   H 5 .   ? 22.668 -7.595  25.410 1.00 42.44 ? 382 HOH   C O   1 
HETATM 2476 O  O   . HOH   H 5 .   ? 22.777 -32.664 20.471 1.00 37.65 ? 383 HOH   C O   1 
HETATM 2477 O  O   . HOH   H 5 .   ? 37.598 -31.369 25.720 1.00 27.51 ? 384 HOH   C O   1 
HETATM 2478 O  O   . HOH   H 5 .   ? 22.212 -13.743 29.550 1.00 33.06 ? 385 HOH   C O   1 
HETATM 2479 O  O   . HOH   H 5 .   ? 4.170  -10.355 19.481 1.00 28.67 ? 386 HOH   C O   1 
HETATM 2480 O  O   . HOH   H 5 .   ? 32.830 -9.805  11.003 1.00 14.58 ? 387 HOH   C O   1 
HETATM 2481 O  O   . HOH   H 5 .   ? 31.115 -12.151 10.565 1.00 14.87 ? 388 HOH   C O   1 
HETATM 2482 O  O   . HOH   H 5 .   ? 28.864 -36.250 7.824  1.00 18.35 ? 389 HOH   C O   1 
HETATM 2483 O  O   . HOH   H 5 .   ? 27.965 -16.324 21.987 1.00 13.31 ? 390 HOH   C O   1 
HETATM 2484 O  O   . HOH   H 5 .   ? 22.816 -28.148 12.548 1.00 19.22 ? 391 HOH   C O   1 
HETATM 2485 O  O   . HOH   H 5 .   ? 30.824 -35.762 31.705 1.00 39.80 ? 392 HOH   C O   1 
HETATM 2486 O  O   . HOH   H 5 .   ? 8.670  -13.431 10.691 1.00 24.70 ? 393 HOH   C O   1 
HETATM 2487 O  O   . HOH   H 5 .   ? 32.111 -34.417 24.754 1.00 27.01 ? 394 HOH   C O   1 
HETATM 2488 O  O   . HOH   H 5 .   ? 22.851 -33.371 5.411  1.00 33.48 ? 395 HOH   C O   1 
HETATM 2489 O  O   . HOH   H 5 .   ? 26.316 -31.205 14.813 1.00 18.86 ? 396 HOH   C O   1 
HETATM 2490 O  O   . HOH   H 5 .   ? 10.617 -11.994 8.904  1.00 29.39 ? 397 HOH   C O   1 
HETATM 2491 O  O   . HOH   H 5 .   ? 35.456 -24.588 24.653 1.00 17.82 ? 398 HOH   C O   1 
HETATM 2492 O  O   . HOH   H 5 .   ? 26.498 -12.010 27.437 1.00 25.58 ? 399 HOH   C O   1 
HETATM 2493 O  O   . HOH   H 5 .   ? 33.531 -36.055 8.802  1.00 41.85 ? 400 HOH   C O   1 
HETATM 2494 O  O   . HOH   H 5 .   ? 30.137 -18.115 8.344  1.00 25.12 ? 401 HOH   C O   1 
HETATM 2495 O  O   . HOH   H 5 .   ? 11.381 -22.572 28.623 1.00 28.27 ? 402 HOH   C O   1 
HETATM 2496 O  O   . HOH   H 5 .   ? 3.760  -8.192  14.631 1.00 27.29 ? 403 HOH   C O   1 
HETATM 2497 O  O   . HOH   H 5 .   ? 36.869 -29.200 10.072 1.00 19.10 ? 404 HOH   C O   1 
HETATM 2498 O  O   . HOH   H 5 .   ? 23.473 -33.676 29.029 1.00 28.50 ? 405 HOH   C O   1 
HETATM 2499 O  O   . HOH   H 5 .   ? 9.933  -24.905 19.720 1.00 21.23 ? 406 HOH   C O   1 
HETATM 2500 O  O   . HOH   H 5 .   ? 26.463 -6.025  21.980 1.00 30.81 ? 407 HOH   C O   1 
HETATM 2501 O  O   . HOH   H 5 .   ? 32.925 -30.208 31.633 1.00 18.36 ? 408 HOH   C O   1 
HETATM 2502 O  O   . HOH   H 5 .   ? 34.124 -13.396 25.446 1.00 19.48 ? 409 HOH   C O   1 
HETATM 2503 O  O   . HOH   H 5 .   ? 25.960 -30.972 30.719 1.00 18.40 ? 410 HOH   C O   1 
HETATM 2504 O  O   . HOH   H 5 .   ? 22.160 -23.791 5.999  1.00 31.77 ? 411 HOH   C O   1 
HETATM 2505 O  O   . HOH   H 5 .   ? 10.892 -6.430  13.259 1.00 25.29 ? 412 HOH   C O   1 
HETATM 2506 O  O   . HOH   H 5 .   ? 35.686 -28.504 7.708  1.00 17.16 ? 413 HOH   C O   1 
HETATM 2507 O  O   . HOH   H 5 .   ? 37.688 -20.281 4.903  1.00 33.95 ? 414 HOH   C O   1 
HETATM 2508 O  O   . HOH   H 5 .   ? 31.368 -13.457 4.203  1.00 31.05 ? 415 HOH   C O   1 
HETATM 2509 O  O   . HOH   H 5 .   ? 4.558  -27.994 23.184 1.00 34.85 ? 416 HOH   C O   1 
HETATM 2510 O  O   . HOH   H 5 .   ? 43.174 -25.439 23.644 1.00 23.98 ? 417 HOH   C O   1 
HETATM 2511 O  O   . HOH   H 5 .   ? 37.780 -23.538 4.466  1.00 38.66 ? 418 HOH   C O   1 
HETATM 2512 O  O   . HOH   H 5 .   ? 4.496  -25.095 25.482 1.00 46.49 ? 419 HOH   C O   1 
HETATM 2513 O  O   . HOH   H 5 .   ? 34.898 -4.204  17.655 1.00 29.70 ? 420 HOH   C O   1 
HETATM 2514 O  O   . HOH   H 5 .   ? 38.666 -12.925 25.728 1.00 26.84 ? 421 HOH   C O   1 
HETATM 2515 O  O   . HOH   H 5 .   ? 20.267 -23.626 34.717 1.00 29.62 ? 422 HOH   C O   1 
HETATM 2516 O  O   . HOH   H 5 .   ? 34.999 -13.728 5.980  1.00 34.49 ? 423 HOH   C O   1 
HETATM 2517 O  O   . HOH   H 5 .   ? 14.563 -18.544 10.265 1.00 37.18 ? 424 HOH   C O   1 
HETATM 2518 O  O   . HOH   H 5 .   ? 21.579 -18.864 5.863  1.00 26.64 ? 425 HOH   C O   1 
HETATM 2519 O  O   . HOH   H 5 .   ? 29.889 -10.334 27.572 1.00 40.91 ? 426 HOH   C O   1 
HETATM 2520 O  O   . HOH   H 5 .   ? 10.258 -30.842 25.229 1.00 30.58 ? 427 HOH   C O   1 
HETATM 2521 O  O   . HOH   H 5 .   ? 20.196 -32.207 22.192 1.00 27.22 ? 428 HOH   C O   1 
HETATM 2522 O  O   . HOH   H 5 .   ? 32.640 -14.359 9.285  1.00 15.54 ? 429 HOH   C O   1 
HETATM 2523 O  O   . HOH   H 5 .   ? 41.572 -12.453 18.049 1.00 22.48 ? 430 HOH   C O   1 
HETATM 2524 O  O   . HOH   H 5 .   ? 6.321  -23.019 18.287 1.00 33.12 ? 431 HOH   C O   1 
HETATM 2525 O  O   . HOH   H 5 .   ? 17.044 -25.334 12.615 1.00 24.16 ? 432 HOH   C O   1 
HETATM 2526 O  O   . HOH   H 5 .   ? 3.896  -12.728 17.111 1.00 36.98 ? 433 HOH   C O   1 
HETATM 2527 O  O   . HOH   H 5 .   ? 23.265 -31.079 13.187 1.00 30.97 ? 434 HOH   C O   1 
HETATM 2528 O  O   . HOH   H 5 .   ? 9.554  -18.436 26.598 1.00 29.83 ? 435 HOH   C O   1 
HETATM 2529 O  O   . HOH   H 5 .   ? 39.960 -29.873 14.594 1.00 16.78 ? 436 HOH   C O   1 
HETATM 2530 O  O   . HOH   H 5 .   ? 6.617  -17.248 18.170 1.00 44.17 ? 437 HOH   C O   1 
HETATM 2531 O  O   . HOH   H 5 .   ? 18.487 -8.323  25.459 1.00 20.47 ? 438 HOH   C O   1 
HETATM 2532 O  O   . HOH   H 5 .   ? 16.296 -20.515 11.462 1.00 26.89 ? 439 HOH   C O   1 
HETATM 2533 O  O   . HOH   H 5 .   ? 18.669 -19.142 10.731 1.00 18.50 ? 440 HOH   C O   1 
HETATM 2534 O  O   . HOH   H 5 .   ? 33.836 -15.562 27.035 1.00 32.97 ? 441 HOH   C O   1 
HETATM 2535 O  O   . HOH   H 5 .   ? 6.383  -20.130 18.078 1.00 35.11 ? 442 HOH   C O   1 
HETATM 2536 O  O   . HOH   H 5 .   ? 37.379 -13.882 9.806  1.00 30.55 ? 443 HOH   C O   1 
HETATM 2537 O  O   . HOH   H 5 .   ? 14.940 -29.774 17.860 1.00 39.14 ? 444 HOH   C O   1 
HETATM 2538 O  O   . HOH   H 5 .   ? 23.160 -17.500 33.214 1.00 22.33 ? 445 HOH   C O   1 
HETATM 2539 O  O   . HOH   H 5 .   ? 36.398 -24.476 27.218 1.00 31.76 ? 446 HOH   C O   1 
HETATM 2540 O  O   . HOH   H 5 .   ? 31.445 -15.696 7.011  1.00 28.62 ? 447 HOH   C O   1 
HETATM 2541 O  O   . HOH   H 5 .   ? 41.844 -31.402 15.714 1.00 32.02 ? 448 HOH   C O   1 
HETATM 2542 O  O   . HOH   H 5 .   ? 20.193 -19.645 35.978 1.00 30.42 ? 449 HOH   C O   1 
HETATM 2543 O  O   . HOH   H 5 .   ? 34.524 -30.154 33.767 1.00 36.44 ? 450 HOH   C O   1 
HETATM 2544 O  O   . HOH   H 5 .   ? 33.445 -20.456 -2.084 1.00 38.51 ? 451 HOH   C O   1 
HETATM 2545 O  O   . HOH   H 5 .   ? 34.192 -31.759 29.529 1.00 25.03 ? 452 HOH   C O   1 
HETATM 2546 O  O   . HOH   H 5 .   ? 8.821  -12.967 25.061 1.00 52.69 ? 453 HOH   C O   1 
HETATM 2547 O  O   . HOH   H 5 .   ? 24.100 -16.639 3.112  1.00 44.49 ? 454 HOH   C O   1 
HETATM 2548 O  O   . HOH   H 5 .   ? 23.612 -15.632 31.461 1.00 31.34 ? 455 HOH   C O   1 
HETATM 2549 O  O   . HOH   H 5 .   ? 26.151 -35.413 7.430  1.00 24.78 ? 456 HOH   C O   1 
HETATM 2550 O  O   . HOH   H 5 .   ? 20.986 -17.443 34.500 1.00 26.37 ? 457 HOH   C O   1 
HETATM 2551 O  O   . HOH   H 5 .   ? 8.814  -19.200 16.823 1.00 36.16 ? 458 HOH   C O   1 
HETATM 2552 O  O   . HOH   H 5 .   ? 22.670 -16.735 5.404  1.00 36.75 ? 459 HOH   C O   1 
HETATM 2553 O  O   . HOH   H 5 .   ? 21.375 -27.003 10.157 1.00 32.89 ? 460 HOH   C O   1 
HETATM 2554 O  O   . HOH   H 5 .   ? 16.330 -27.506 14.064 1.00 34.10 ? 461 HOH   C O   1 
HETATM 2555 O  O   . HOH   H 5 .   ? 13.362 -26.981 29.371 1.00 56.99 ? 462 HOH   C O   1 
HETATM 2556 O  O   . HOH   H 5 .   ? 18.417 -26.092 10.136 1.00 41.38 ? 463 HOH   C O   1 
HETATM 2557 O  O   . HOH   H 5 .   ? 32.375 -19.255 28.986 1.00 27.95 ? 464 HOH   C O   1 
HETATM 2558 O  O   . HOH   H 5 .   ? 35.269 -2.275  15.783 1.00 56.83 ? 465 HOH   C O   1 
HETATM 2559 O  O   . HOH   H 5 .   ? 22.097 -3.081  20.703 1.00 49.69 ? 466 HOH   C O   1 
HETATM 2560 O  O   . HOH   H 5 .   ? 9.899  -21.442 16.193 1.00 31.27 ? 467 HOH   C O   1 
HETATM 2561 O  O   . HOH   H 5 .   ? 22.200 -7.864  11.315 1.00 28.50 ? 468 HOH   C O   1 
HETATM 2562 O  O   . HOH   H 5 .   ? 18.022 -17.917 8.088  1.00 37.97 ? 469 HOH   C O   1 
HETATM 2563 O  O   . HOH   H 5 .   ? 17.886 -16.381 38.229 1.00 36.88 ? 470 HOH   C O   1 
HETATM 2564 O  O   . HOH   H 5 .   ? 36.979 -23.094 -1.643 1.00 32.95 ? 471 HOH   C O   1 
HETATM 2565 O  O   . HOH   H 5 .   ? 8.830  -23.550 17.610 1.00 32.37 ? 472 HOH   C O   1 
HETATM 2566 O  O   . HOH   H 5 .   ? 35.005 -22.930 28.977 1.00 26.02 ? 473 HOH   C O   1 
HETATM 2567 O  O   . HOH   H 5 .   ? 35.301 -20.251 29.395 1.00 38.99 ? 474 HOH   C O   1 
HETATM 2568 O  O   . HOH   H 5 .   ? 9.740  -15.870 27.422 1.00 36.54 ? 475 HOH   C O   1 
HETATM 2569 O  O   . HOH   H 5 .   ? 5.553  -24.387 15.723 1.00 52.40 ? 476 HOH   C O   1 
HETATM 2570 O  O   . HOH   H 5 .   ? 19.448 -15.158 34.489 1.00 36.43 ? 477 HOH   C O   1 
HETATM 2571 O  O   . HOH   H 5 .   ? 19.178 -17.529 5.655  1.00 40.42 ? 478 HOH   C O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER   A 1   ? 0.2025 0.1946 0.1883 -0.0082 -0.0086 -0.0082 7   SER   A N   
2    C CA  . SER   A 1   ? 0.2022 0.1961 0.1931 -0.0070 -0.0111 -0.0064 7   SER   A CA  
3    C C   . SER   A 1   ? 0.1921 0.1872 0.1882 -0.0030 -0.0128 -0.0024 7   SER   A C   
4    O O   . SER   A 1   ? 0.2019 0.1967 0.1966 -0.0021 -0.0128 -0.0007 7   SER   A O   
5    C CB  . SER   A 1   ? 0.2377 0.2362 0.2257 -0.0115 -0.0148 -0.0054 7   SER   A CB  
6    O OG  . SER   A 1   ? 0.2794 0.2817 0.2654 -0.0123 -0.0182 -0.0011 7   SER   A OG  
7    N N   . GLY   A 2   ? 0.1729 0.1689 0.1746 -0.0012 -0.0137 -0.0013 8   GLY   A N   
8    C CA  . GLY   A 2   ? 0.1628 0.1592 0.1697 0.0018  -0.0141 0.0016  8   GLY   A CA  
9    C C   . GLY   A 2   ? 0.1484 0.1437 0.1600 0.0035  -0.0125 0.0006  8   GLY   A C   
10   O O   . GLY   A 2   ? 0.1643 0.1580 0.1753 0.0032  -0.0108 -0.0017 8   GLY   A O   
11   N N   . ALA   A 3   ? 0.1322 0.1283 0.1489 0.0052  -0.0125 0.0025  9   ALA   A N   
12   C CA  . ALA   A 3   ? 0.1387 0.1342 0.1593 0.0060  -0.0107 0.0014  9   ALA   A CA  
13   C C   . ALA   A 3   ? 0.1358 0.1299 0.1594 0.0073  -0.0085 0.0021  9   ALA   A C   
14   O O   . ALA   A 3   ? 0.1436 0.1371 0.1681 0.0081  -0.0086 0.0040  9   ALA   A O   
15   C CB  . ALA   A 3   ? 0.1518 0.1504 0.1767 0.0053  -0.0123 0.0019  9   ALA   A CB  
16   N N   . ILE   A 4   ? 0.1274 0.1207 0.1523 0.0070  -0.0061 0.0006  10  ILE   A N   
17   C CA  . ILE   A 4   ? 0.1166 0.1083 0.1443 0.0071  -0.0029 0.0000  10  ILE   A CA  
18   C C   . ILE   A 4   ? 0.1277 0.1208 0.1622 0.0077  -0.0021 0.0002  10  ILE   A C   
19   O O   . ILE   A 4   ? 0.1343 0.1291 0.1690 0.0068  -0.0029 -0.0006 10  ILE   A O   
20   C CB  . ILE   A 4   ? 0.1264 0.1173 0.1500 0.0050  -0.0006 -0.0018 10  ILE   A CB  
21   C CG1 . ILE   A 4   ? 0.1450 0.1361 0.1631 0.0044  -0.0017 -0.0014 10  ILE   A CG1 
22   C CG2 . ILE   A 4   ? 0.1477 0.1364 0.1728 0.0036  0.0037  -0.0035 10  ILE   A CG2 
23   C CD1 . ILE   A 4   ? 0.1599 0.1528 0.1751 0.0021  -0.0007 -0.0017 10  ILE   A CD1 
24   N N   . TYR   A 5   ? 0.1249 0.1174 0.1659 0.0091  0.0000  0.0013  11  TYR   A N   
25   C CA  . TYR   A 5   ? 0.1349 0.1295 0.1845 0.0100  0.0015  0.0017  11  TYR   A CA  
26   C C   . TYR   A 5   ? 0.1460 0.1368 0.1978 0.0091  0.0077  -0.0012 11  TYR   A C   
27   O O   . TYR   A 5   ? 0.1455 0.1330 0.2012 0.0104  0.0109  -0.0007 11  TYR   A O   
28   C CB  . TYR   A 5   ? 0.1453 0.1432 0.2030 0.0126  -0.0010 0.0062  11  TYR   A CB  
29   C CG  . TYR   A 5   ? 0.1409 0.1434 0.1952 0.0117  -0.0068 0.0083  11  TYR   A CG  
30   C CD1 . TYR   A 5   ? 0.1505 0.1573 0.2064 0.0104  -0.0089 0.0080  11  TYR   A CD1 
31   C CD2 . TYR   A 5   ? 0.1613 0.1634 0.2098 0.0114  -0.0097 0.0100  11  TYR   A CD2 
32   C CE1 . TYR   A 5   ? 0.1631 0.1734 0.2145 0.0082  -0.0134 0.0088  11  TYR   A CE1 
33   C CE2 . TYR   A 5   ? 0.1684 0.1744 0.2125 0.0093  -0.0142 0.0110  11  TYR   A CE2 
34   C CZ  . TYR   A 5   ? 0.1762 0.1860 0.2215 0.0076  -0.0158 0.0100  11  TYR   A CZ  
35   O OH  . TYR   A 5   ? 0.2046 0.2175 0.2446 0.0044  -0.0194 0.0099  11  TYR   A OH  
36   N N   . VAL   A 6   ? 0.1572 0.1479 0.2060 0.0065  0.0099  -0.0043 12  VAL   A N   
37   C CA  . VAL   A 6   ? 0.1591 0.1466 0.2080 0.0039  0.0162  -0.0079 12  VAL   A CA  
38   C C   . VAL   A 6   ? 0.1659 0.1556 0.2205 0.0033  0.0186  -0.0092 12  VAL   A C   
39   O O   . VAL   A 6   ? 0.1597 0.1526 0.2121 0.0024  0.0155  -0.0087 12  VAL   A O   
40   C CB  . VAL   A 6   ? 0.1800 0.1665 0.2179 -0.0004 0.0167  -0.0102 12  VAL   A CB  
41   C CG1 . VAL   A 6   ? 0.1807 0.1707 0.2136 -0.0014 0.0123  -0.0089 12  VAL   A CG1 
42   C CG2 . VAL   A 6   ? 0.2007 0.1846 0.2369 -0.0048 0.0233  -0.0144 12  VAL   A CG2 
43   N N   . GLY   A 7   ? 0.1750 0.1628 0.2380 0.0040  0.0245  -0.0107 13  GLY   A N   
44   C CA  . GLY   A 7   ? 0.1771 0.1673 0.2467 0.0035  0.0274  -0.0120 13  GLY   A CA  
45   C C   . GLY   A 7   ? 0.1599 0.1564 0.2352 0.0062  0.0216  -0.0081 13  GLY   A C   
46   O O   . GLY   A 7   ? 0.1597 0.1583 0.2397 0.0096  0.0177  -0.0040 13  GLY   A O   
47   N N   . ASN   A 8   ? 0.1505 0.1498 0.2237 0.0038  0.0206  -0.0092 14  ASN   A N   
48   C CA  . ASN   A 8   ? 0.1455 0.1504 0.2222 0.0050  0.0151  -0.0062 14  ASN   A CA  
49   C C   . ASN   A 8   ? 0.1369 0.1413 0.2029 0.0032  0.0101  -0.0059 14  ASN   A C   
50   O O   . ASN   A 8   ? 0.1463 0.1534 0.2119 0.0019  0.0077  -0.0056 14  ASN   A O   
51   C CB  . ASN   A 8   ? 0.1502 0.1590 0.2347 0.0040  0.0177  -0.0071 14  ASN   A CB  
52   C CG  . ASN   A 8   ? 0.1933 0.2047 0.2925 0.0073  0.0215  -0.0056 14  ASN   A CG  
53   O OD1 . ASN   A 8   ? 0.2268 0.2443 0.3353 0.0100  0.0177  -0.0012 14  ASN   A OD1 
54   N ND2 . ASN   A 8   ? 0.1842 0.1912 0.2861 0.0067  0.0291  -0.0090 14  ASN   A ND2 
55   N N   . TYR   A 9   ? 0.1309 0.1320 0.1894 0.0033  0.0089  -0.0059 15  TYR   A N   
56   C CA  . TYR   A 9   ? 0.1325 0.1327 0.1825 0.0023  0.0051  -0.0053 15  TYR   A CA  
57   C C   . TYR   A 9   ? 0.1300 0.1300 0.1783 0.0044  0.0015  -0.0033 15  TYR   A C   
58   O O   . TYR   A 9   ? 0.1396 0.1385 0.1897 0.0060  0.0024  -0.0025 15  TYR   A O   
59   C CB  . TYR   A 9   ? 0.1524 0.1498 0.1944 -0.0003 0.0072  -0.0068 15  TYR   A CB  
60   C CG  . TYR   A 9   ? 0.1639 0.1616 0.2050 -0.0037 0.0106  -0.0085 15  TYR   A CG  
61   C CD1 . TYR   A 9   ? 0.1751 0.1743 0.2170 -0.0048 0.0095  -0.0081 15  TYR   A CD1 
62   C CD2 . TYR   A 9   ? 0.1833 0.1796 0.2223 -0.0065 0.0153  -0.0110 15  TYR   A CD2 
63   C CE1 . TYR   A 9   ? 0.1814 0.1811 0.2221 -0.0083 0.0127  -0.0094 15  TYR   A CE1 
64   C CE2 . TYR   A 9   ? 0.2007 0.1976 0.2374 -0.0106 0.0186  -0.0128 15  TYR   A CE2 
65   C CZ  . TYR   A 9   ? 0.2020 0.2008 0.2396 -0.0114 0.0170  -0.0116 15  TYR   A CZ  
66   O OH  . TYR   A 9   ? 0.2626 0.2623 0.2976 -0.0159 0.0203  -0.0130 15  TYR   A OH  
67   N N   . ARG   A 10  ? 0.1247 0.1253 0.1690 0.0038  -0.0020 -0.0027 16  ARG   A N   
68   C CA  . ARG   A 10  ? 0.1253 0.1254 0.1658 0.0047  -0.0050 -0.0015 16  ARG   A CA  
69   C C   . ARG   A 10  ? 0.1227 0.1198 0.1563 0.0038  -0.0049 -0.0024 16  ARG   A C   
70   O O   . ARG   A 10  ? 0.1329 0.1294 0.1657 0.0025  -0.0047 -0.0031 16  ARG   A O   
71   C CB  . ARG   A 10  ? 0.1326 0.1365 0.1751 0.0039  -0.0085 -0.0004 16  ARG   A CB  
72   C CG  . ARG   A 10  ? 0.1585 0.1617 0.1951 0.0031  -0.0110 -0.0003 16  ARG   A CG  
73   C CD  . ARG   A 10  ? 0.1602 0.1685 0.1981 0.0009  -0.0145 0.0008  16  ARG   A CD  
74   N NE  . ARG   A 10  ? 0.1719 0.1783 0.2027 -0.0020 -0.0152 -0.0015 16  ARG   A NE  
75   C CZ  . ARG   A 10  ? 0.1965 0.2026 0.2219 -0.0032 -0.0166 -0.0014 16  ARG   A CZ  
76   N NH1 . ARG   A 10  ? 0.1969 0.2048 0.2231 -0.0015 -0.0181 0.0016  16  ARG   A NH1 
77   N NH2 . ARG   A 10  ? 0.1906 0.1943 0.2100 -0.0064 -0.0159 -0.0045 16  ARG   A NH2 
78   N N   . VAL   A 11  ? 0.1176 0.1130 0.1474 0.0044  -0.0045 -0.0021 17  VAL   A N   
79   C CA  . VAL   A 11  ? 0.1224 0.1163 0.1477 0.0041  -0.0043 -0.0020 17  VAL   A CA  
80   C C   . VAL   A 11  ? 0.1371 0.1302 0.1599 0.0048  -0.0059 -0.0019 17  VAL   A C   
81   O O   . VAL   A 11  ? 0.1330 0.1264 0.1548 0.0054  -0.0067 -0.0015 17  VAL   A O   
82   C CB  . VAL   A 11  ? 0.1267 0.1205 0.1495 0.0034  -0.0027 -0.0017 17  VAL   A CB  
83   C CG1 . VAL   A 11  ? 0.1364 0.1307 0.1565 0.0031  -0.0029 -0.0001 17  VAL   A CG1 
84   C CG2 . VAL   A 11  ? 0.1448 0.1391 0.1690 0.0016  -0.0002 -0.0027 17  VAL   A CG2 
85   N N   . VAL   A 12  ? 0.1208 0.1124 0.1426 0.0044  -0.0058 -0.0025 18  VAL   A N   
86   C CA  . VAL   A 12  ? 0.1349 0.1251 0.1539 0.0042  -0.0061 -0.0035 18  VAL   A CA  
87   C C   . VAL   A 12  ? 0.1270 0.1148 0.1458 0.0050  -0.0039 -0.0034 18  VAL   A C   
88   O O   . VAL   A 12  ? 0.1445 0.1319 0.1657 0.0055  -0.0028 -0.0018 18  VAL   A O   
89   C CB  . VAL   A 12  ? 0.1566 0.1471 0.1750 0.0020  -0.0072 -0.0052 18  VAL   A CB  
90   C CG1 . VAL   A 12  ? 0.1921 0.1867 0.2121 0.0016  -0.0100 -0.0039 18  VAL   A CG1 
91   C CG2 . VAL   A 12  ? 0.1597 0.1486 0.1803 0.0008  -0.0059 -0.0063 18  VAL   A CG2 
92   N N   . ASN   A 13  ? 0.1250 0.1113 0.1416 0.0050  -0.0030 -0.0045 19  ASN   A N   
93   C CA  . ASN   A 13  ? 0.1306 0.1141 0.1492 0.0061  0.0001  -0.0045 19  ASN   A CA  
94   C C   . ASN   A 13  ? 0.1398 0.1195 0.1600 0.0048  0.0019  -0.0061 19  ASN   A C   
95   O O   . ASN   A 13  ? 0.1452 0.1242 0.1627 0.0020  0.0013  -0.0090 19  ASN   A O   
96   C CB  . ASN   A 13  ? 0.1350 0.1169 0.1509 0.0057  0.0018  -0.0066 19  ASN   A CB  
97   C CG  . ASN   A 13  ? 0.1437 0.1288 0.1577 0.0066  0.0005  -0.0051 19  ASN   A CG  
98   O OD1 . ASN   A 13  ? 0.1530 0.1396 0.1633 0.0053  -0.0018 -0.0056 19  ASN   A OD1 
99   N ND2 . ASN   A 13  ? 0.1568 0.1435 0.1742 0.0086  0.0017  -0.0026 19  ASN   A ND2 
100  N N   . ARG   A 14  ? 0.1333 0.1111 0.1581 0.0064  0.0041  -0.0038 20  ARG   A N   
101  C CA  . ARG   A 14  ? 0.1378 0.1111 0.1645 0.0050  0.0064  -0.0053 20  ARG   A CA  
102  C C   . ARG   A 14  ? 0.1555 0.1238 0.1798 0.0028  0.0097  -0.0101 20  ARG   A C   
103  O O   . ARG   A 14  ? 0.1704 0.1365 0.1926 -0.0006 0.0102  -0.0133 20  ARG   A O   
104  C CB  . ARG   A 14  ? 0.1442 0.1159 0.1769 0.0075  0.0086  -0.0010 20  ARG   A CB  
105  C CG  . ARG   A 14  ? 0.1547 0.1210 0.1899 0.0061  0.0112  -0.0016 20  ARG   A CG  
106  C CD  . ARG   A 14  ? 0.1671 0.1320 0.2093 0.0090  0.0134  0.0041  20  ARG   A CD  
107  N NE  . ARG   A 14  ? 0.1734 0.1330 0.2185 0.0078  0.0159  0.0046  20  ARG   A NE  
108  C CZ  . ARG   A 14  ? 0.2078 0.1592 0.2560 0.0075  0.0213  0.0021  20  ARG   A CZ  
109  N NH1 . ARG   A 14  ? 0.2122 0.1599 0.2598 0.0076  0.0248  -0.0022 20  ARG   A NH1 
110  N NH2 . ARG   A 14  ? 0.2229 0.1692 0.2741 0.0065  0.0238  0.0033  20  ARG   A NH2 
111  N N   . HIS   A 15  ? 0.1434 0.1106 0.1675 0.0040  0.0121  -0.0110 21  HIS   A N   
112  C CA  . HIS   A 15  ? 0.1639 0.1257 0.1852 0.0010  0.0165  -0.0163 21  HIS   A CA  
113  C C   . HIS   A 15  ? 0.1756 0.1400 0.1886 -0.0040 0.0136  -0.0202 21  HIS   A C   
114  O O   . HIS   A 15  ? 0.1969 0.1574 0.2057 -0.0084 0.0169  -0.0253 21  HIS   A O   
115  C CB  . HIS   A 15  ? 0.1826 0.1422 0.2070 0.0035  0.0210  -0.0164 21  HIS   A CB  
116  C CG  . HIS   A 15  ? 0.1765 0.1413 0.1972 0.0039  0.0183  -0.0159 21  HIS   A CG  
117  N ND1 . HIS   A 15  ? 0.1740 0.1445 0.1975 0.0074  0.0149  -0.0108 21  HIS   A ND1 
118  C CD2 . HIS   A 15  ? 0.1905 0.1554 0.2045 0.0007  0.0189  -0.0198 21  HIS   A CD2 
119  C CE1 . HIS   A 15  ? 0.1760 0.1491 0.1950 0.0065  0.0138  -0.0118 21  HIS   A CE1 
120  N NE2 . HIS   A 15  ? 0.1854 0.1555 0.1985 0.0026  0.0159  -0.0169 21  HIS   A NE2 
121  N N   . LEU   A 16  ? 0.1729 0.1438 0.1838 -0.0038 0.0078  -0.0176 22  LEU   A N   
122  C CA  . LEU   A 16  ? 0.1675 0.1426 0.1723 -0.0080 0.0041  -0.0191 22  LEU   A CA  
123  C C   . LEU   A 16  ? 0.1865 0.1652 0.1927 -0.0096 0.0005  -0.0180 22  LEU   A C   
124  O O   . LEU   A 16  ? 0.1979 0.1818 0.2012 -0.0125 -0.0033 -0.0176 22  LEU   A O   
125  C CB  . LEU   A 16  ? 0.1686 0.1482 0.1712 -0.0065 0.0009  -0.0166 22  LEU   A CB  
126  C CG  . LEU   A 16  ? 0.1749 0.1519 0.1757 -0.0058 0.0043  -0.0180 22  LEU   A CG  
127  C CD1 . LEU   A 16  ? 0.1803 0.1616 0.1789 -0.0045 0.0012  -0.0153 22  LEU   A CD1 
128  C CD2 . LEU   A 16  ? 0.2071 0.1808 0.2019 -0.0111 0.0080  -0.0235 22  LEU   A CD2 
129  N N   . ALA   A 17  ? 0.1739 0.1507 0.1852 -0.0076 0.0016  -0.0168 23  ALA   A N   
130  C CA  . ALA   A 17  ? 0.1719 0.1523 0.1852 -0.0090 -0.0012 -0.0158 23  ALA   A CA  
131  C C   . ALA   A 17  ? 0.1857 0.1670 0.1954 -0.0151 -0.0015 -0.0194 23  ALA   A C   
132  O O   . ALA   A 17  ? 0.1943 0.1700 0.2009 -0.0184 0.0026  -0.0235 23  ALA   A O   
133  C CB  . ALA   A 17  ? 0.1695 0.1468 0.1877 -0.0068 0.0009  -0.0143 23  ALA   A CB  
134  N N   . THR   A 18  ? 0.1768 0.1654 0.1875 -0.0170 -0.0060 -0.0177 24  THR   A N   
135  C CA  . THR   A 18  ? 0.1757 0.1680 0.1832 -0.0238 -0.0075 -0.0202 24  THR   A CA  
136  C C   . THR   A 18  ? 0.1827 0.1735 0.1937 -0.0257 -0.0059 -0.0215 24  THR   A C   
137  O O   . THR   A 18  ? 0.1749 0.1627 0.1909 -0.0214 -0.0043 -0.0198 24  THR   A O   
138  C CB  . THR   A 18  ? 0.2020 0.2047 0.2108 -0.0248 -0.0135 -0.0162 24  THR   A CB  
139  O OG1 . THR   A 18  ? 0.2021 0.2082 0.2191 -0.0206 -0.0151 -0.0126 24  THR   A OG1 
140  C CG2 . THR   A 18  ? 0.2024 0.2066 0.2083 -0.0227 -0.0153 -0.0139 24  THR   A CG2 
141  N N   . HIS   A 19  ? 0.1820 0.1754 0.1898 -0.0327 -0.0065 -0.0244 25  HIS   A N   
142  C CA  . HIS   A 19  ? 0.1844 0.1776 0.1956 -0.0351 -0.0054 -0.0255 25  HIS   A CA  
143  C C   . HIS   A 19  ? 0.1697 0.1703 0.1890 -0.0312 -0.0090 -0.0207 25  HIS   A C   
144  O O   . HIS   A 19  ? 0.1792 0.1767 0.2027 -0.0294 -0.0068 -0.0204 25  HIS   A O   
145  C CB  . HIS   A 19  ? 0.2124 0.2096 0.2185 -0.0446 -0.0063 -0.0293 25  HIS   A CB  
146  C CG  . HIS   A 19  ? 0.2941 0.2942 0.3048 -0.0474 -0.0065 -0.0295 25  HIS   A CG  
147  N ND1 . HIS   A 19  ? 0.3389 0.3293 0.3507 -0.0475 -0.0010 -0.0324 25  HIS   A ND1 
148  C CD2 . HIS   A 19  ? 0.3342 0.3458 0.3499 -0.0493 -0.0115 -0.0263 25  HIS   A CD2 
149  C CE1 . HIS   A 19  ? 0.3496 0.3456 0.3652 -0.0507 -0.0026 -0.0319 25  HIS   A CE1 
150  N NE2 . HIS   A 19  ? 0.3613 0.3705 0.3800 -0.0516 -0.0089 -0.0282 25  HIS   A NE2 
151  N N   . ASN   A 20  ? 0.1675 0.1771 0.1893 -0.0298 -0.0140 -0.0167 26  ASN   A N   
152  C CA  . ASN   A 20  ? 0.1682 0.1839 0.1989 -0.0259 -0.0160 -0.0125 26  ASN   A CA  
153  C C   . ASN   A 20  ? 0.1510 0.1602 0.1841 -0.0197 -0.0128 -0.0116 26  ASN   A C   
154  O O   . ASN   A 20  ? 0.1614 0.1712 0.1998 -0.0182 -0.0116 -0.0108 26  ASN   A O   
155  C CB  . ASN   A 20  ? 0.1938 0.2193 0.2285 -0.0247 -0.0210 -0.0077 26  ASN   A CB  
156  C CG  . ASN   A 20  ? 0.2857 0.3172 0.3312 -0.0212 -0.0218 -0.0039 26  ASN   A CG  
157  O OD1 . ASN   A 20  ? 0.3266 0.3639 0.3772 -0.0240 -0.0226 -0.0038 26  ASN   A OD1 
158  N ND2 . ASN   A 20  ? 0.3064 0.3362 0.3559 -0.0152 -0.0208 -0.0015 26  ASN   A ND2 
159  N N   . ASP   A 21  ? 0.1451 0.1485 0.1739 -0.0168 -0.0113 -0.0120 27  ASP   A N   
160  C CA  . ASP   A 21  ? 0.1456 0.1440 0.1760 -0.0121 -0.0087 -0.0108 27  ASP   A CA  
161  C C   . ASP   A 21  ? 0.1382 0.1311 0.1691 -0.0130 -0.0052 -0.0122 27  ASP   A C   
162  O O   . ASP   A 21  ? 0.1445 0.1375 0.1788 -0.0112 -0.0041 -0.0106 27  ASP   A O   
163  C CB  . ASP   A 21  ? 0.1486 0.1427 0.1748 -0.0097 -0.0076 -0.0109 27  ASP   A CB  
164  C CG  . ASP   A 21  ? 0.1634 0.1615 0.1891 -0.0079 -0.0104 -0.0087 27  ASP   A CG  
165  O OD1 . ASP   A 21  ? 0.1625 0.1652 0.1932 -0.0060 -0.0120 -0.0062 27  ASP   A OD1 
166  O OD2 . ASP   A 21  ? 0.1639 0.1604 0.1849 -0.0085 -0.0105 -0.0096 27  ASP   A OD2 
167  N N   . TRP   A 22  ? 0.1406 0.1284 0.1681 -0.0162 -0.0029 -0.0152 28  TRP   A N   
168  C CA  . TRP   A 22  ? 0.1446 0.1261 0.1733 -0.0170 0.0009  -0.0160 28  TRP   A CA  
169  C C   . TRP   A 22  ? 0.1548 0.1403 0.1870 -0.0198 0.0002  -0.0160 28  TRP   A C   
170  O O   . TRP   A 22  ? 0.1643 0.1465 0.1986 -0.0191 0.0025  -0.0147 28  TRP   A O   
171  C CB  . TRP   A 22  ? 0.1573 0.1312 0.1821 -0.0202 0.0046  -0.0198 28  TRP   A CB  
172  C CG  . TRP   A 22  ? 0.1651 0.1332 0.1890 -0.0165 0.0073  -0.0192 28  TRP   A CG  
173  C CD1 . TRP   A 22  ? 0.1868 0.1543 0.2069 -0.0168 0.0076  -0.0212 28  TRP   A CD1 
174  C CD2 . TRP   A 22  ? 0.1663 0.1293 0.1938 -0.0123 0.0102  -0.0159 28  TRP   A CD2 
175  N NE1 . TRP   A 22  ? 0.1762 0.1381 0.1980 -0.0128 0.0110  -0.0199 28  TRP   A NE1 
176  C CE2 . TRP   A 22  ? 0.1675 0.1274 0.1944 -0.0097 0.0121  -0.0160 28  TRP   A CE2 
177  C CE3 . TRP   A 22  ? 0.1854 0.1471 0.2169 -0.0107 0.0111  -0.0123 28  TRP   A CE3 
178  C CZ2 . TRP   A 22  ? 0.1830 0.1392 0.2143 -0.0054 0.0148  -0.0120 28  TRP   A CZ2 
179  C CZ3 . TRP   A 22  ? 0.1903 0.1487 0.2250 -0.0068 0.0130  -0.0080 28  TRP   A CZ3 
180  C CH2 . TRP   A 22  ? 0.1895 0.1453 0.2248 -0.0041 0.0149  -0.0077 28  TRP   A CH2 
181  N N   . ALA   A 23  ? 0.1504 0.1434 0.1836 -0.0230 -0.0030 -0.0168 29  ALA   A N   
182  C CA  . ALA   A 23  ? 0.1566 0.1549 0.1944 -0.0258 -0.0036 -0.0167 29  ALA   A CA  
183  C C   . ALA   A 23  ? 0.1669 0.1702 0.2108 -0.0220 -0.0045 -0.0135 29  ALA   A C   
184  O O   . ALA   A 23  ? 0.1736 0.1807 0.2222 -0.0236 -0.0040 -0.0133 29  ALA   A O   
185  C CB  . ALA   A 23  ? 0.1707 0.1769 0.2082 -0.0311 -0.0070 -0.0180 29  ALA   A CB  
186  N N   . ASN   A 24  ? 0.1591 0.1625 0.2030 -0.0174 -0.0052 -0.0114 30  ASN   A N   
187  C CA  . ASN   A 24  ? 0.1551 0.1619 0.2041 -0.0142 -0.0047 -0.0093 30  ASN   A CA  
188  C C   . ASN   A 24  ? 0.1656 0.1665 0.2108 -0.0112 -0.0026 -0.0084 30  ASN   A C   
189  O O   . ASN   A 24  ? 0.1601 0.1623 0.2063 -0.0085 -0.0026 -0.0072 30  ASN   A O   
190  C CB  . ASN   A 24  ? 0.1615 0.1756 0.2152 -0.0123 -0.0076 -0.0073 30  ASN   A CB  
191  C CG  . ASN   A 24  ? 0.1821 0.2044 0.2412 -0.0155 -0.0102 -0.0068 30  ASN   A CG  
192  O OD1 . ASN   A 24  ? 0.2168 0.2437 0.2831 -0.0160 -0.0091 -0.0063 30  ASN   A OD1 
193  N ND2 . ASN   A 24  ? 0.1879 0.2127 0.2434 -0.0187 -0.0134 -0.0072 30  ASN   A ND2 
194  N N   . LEU   A 25  ? 0.1622 0.1568 0.2037 -0.0120 -0.0006 -0.0086 31  LEU   A N   
195  C CA  . LEU   A 25  ? 0.1563 0.1467 0.1947 -0.0096 0.0007  -0.0067 31  LEU   A CA  
196  C C   . LEU   A 25  ? 0.1604 0.1523 0.1994 -0.0095 0.0021  -0.0050 31  LEU   A C   
197  O O   . LEU   A 25  ? 0.1790 0.1716 0.2198 -0.0118 0.0036  -0.0051 31  LEU   A O   
198  C CB  . LEU   A 25  ? 0.1606 0.1443 0.1971 -0.0104 0.0027  -0.0065 31  LEU   A CB  
199  C CG  . LEU   A 25  ? 0.1693 0.1496 0.2043 -0.0078 0.0037  -0.0033 31  LEU   A CG  
200  C CD1 . LEU   A 25  ? 0.1702 0.1511 0.2033 -0.0051 0.0024  -0.0034 31  LEU   A CD1 
201  C CD2 . LEU   A 25  ? 0.2000 0.1735 0.2358 -0.0082 0.0065  -0.0022 31  LEU   A CD2 
202  N N   . VAL   A 26  ? 0.1475 0.1399 0.1845 -0.0076 0.0020  -0.0036 32  VAL   A N   
203  C CA  . VAL   A 26  ? 0.1500 0.1436 0.1854 -0.0087 0.0037  -0.0023 32  VAL   A CA  
204  C C   . VAL   A 26  ? 0.1628 0.1541 0.1947 -0.0086 0.0036  0.0013  32  VAL   A C   
205  O O   . VAL   A 26  ? 0.1841 0.1755 0.2147 -0.0110 0.0048  0.0037  32  VAL   A O   
206  C CB  . VAL   A 26  ? 0.1513 0.1476 0.1869 -0.0077 0.0040  -0.0034 32  VAL   A CB  
207  C CG1 . VAL   A 26  ? 0.1779 0.1753 0.2099 -0.0103 0.0063  -0.0028 32  VAL   A CG1 
208  C CG2 . VAL   A 26  ? 0.1622 0.1616 0.2039 -0.0072 0.0044  -0.0056 32  VAL   A CG2 
209  N N   . TRP   A 27  ? 0.1527 0.1425 0.1835 -0.0061 0.0023  0.0024  33  TRP   A N   
210  C CA  . TRP   A 27  ? 0.1596 0.1486 0.1892 -0.0053 0.0022  0.0068  33  TRP   A CA  
211  C C   . TRP   A 27  ? 0.1636 0.1500 0.1942 -0.0023 0.0017  0.0069  33  TRP   A C   
212  O O   . TRP   A 27  ? 0.1549 0.1417 0.1848 -0.0011 0.0008  0.0039  33  TRP   A O   
213  C CB  . TRP   A 27  ? 0.1712 0.1648 0.1973 -0.0070 0.0017  0.0086  33  TRP   A CB  
214  C CG  . TRP   A 27  ? 0.1819 0.1776 0.2071 -0.0065 0.0006  0.0139  33  TRP   A CG  
215  C CD1 . TRP   A 27  ? 0.2074 0.2048 0.2328 -0.0081 0.0003  0.0196  33  TRP   A CD1 
216  C CD2 . TRP   A 27  ? 0.1702 0.1676 0.1949 -0.0045 -0.0007 0.0147  33  TRP   A CD2 
217  N NE1 . TRP   A 27  ? 0.2225 0.2235 0.2485 -0.0070 -0.0013 0.0244  33  TRP   A NE1 
218  C CE2 . TRP   A 27  ? 0.1898 0.1910 0.2151 -0.0050 -0.0018 0.0210  33  TRP   A CE2 
219  C CE3 . TRP   A 27  ? 0.1706 0.1673 0.1948 -0.0026 -0.0010 0.0112  33  TRP   A CE3 
220  C CZ2 . TRP   A 27  ? 0.2022 0.2069 0.2279 -0.0037 -0.0031 0.0235  33  TRP   A CZ2 
221  C CZ3 . TRP   A 27  ? 0.1874 0.1867 0.2108 -0.0016 -0.0021 0.0132  33  TRP   A CZ3 
222  C CH2 . TRP   A 27  ? 0.1986 0.2018 0.2231 -0.0020 -0.0030 0.0190  33  TRP   A CH2 
223  N N   . GLU   A 28  ? 0.1645 0.1482 0.1975 -0.0009 0.0026  0.0105  34  GLU   A N   
224  C CA  . GLU   A 28  ? 0.1660 0.1472 0.2006 0.0020  0.0032  0.0105  34  GLU   A CA  
225  C C   . GLU   A 28  ? 0.1793 0.1613 0.2175 0.0039  0.0037  0.0168  34  GLU   A C   
226  O O   . GLU   A 28  ? 0.1826 0.1644 0.2230 0.0031  0.0043  0.0213  34  GLU   A O   
227  C CB  . GLU   A 28  ? 0.1821 0.1572 0.2180 0.0020  0.0055  0.0064  34  GLU   A CB  
228  C CG  . GLU   A 28  ? 0.1924 0.1626 0.2311 0.0007  0.0080  0.0074  34  GLU   A CG  
229  C CD  . GLU   A 28  ? 0.2097 0.1750 0.2538 0.0030  0.0111  0.0119  34  GLU   A CD  
230  O OE1 . GLU   A 28  ? 0.2211 0.1835 0.2680 0.0022  0.0127  0.0151  34  GLU   A OE1 
231  O OE2 . GLU   A 28  ? 0.1924 0.1568 0.2388 0.0059  0.0123  0.0125  34  GLU   A OE2 
232  N N   . ASP   A 29  ? 0.1676 0.1507 0.2074 0.0064  0.0037  0.0178  35  ASP   A N   
233  C CA  . ASP   A 29  ? 0.1598 0.1451 0.2052 0.0087  0.0041  0.0247  35  ASP   A CA  
234  C C   . ASP   A 29  ? 0.1575 0.1400 0.2067 0.0121  0.0065  0.0234  35  ASP   A C   
235  O O   . ASP   A 29  ? 0.1579 0.1435 0.2042 0.0124  0.0052  0.0212  35  ASP   A O   
236  C CB  . ASP   A 29  ? 0.1824 0.1767 0.2249 0.0068  0.0007  0.0290  35  ASP   A CB  
237  C CG  . ASP   A 29  ? 0.2242 0.2240 0.2727 0.0083  -0.0002 0.0377  35  ASP   A CG  
238  O OD1 . ASP   A 29  ? 0.2523 0.2498 0.3078 0.0123  0.0020  0.0395  35  ASP   A OD1 
239  O OD2 . ASP   A 29  ? 0.2527 0.2598 0.2990 0.0052  -0.0029 0.0428  35  ASP   A OD2 
240  N N   . SER   A 30  ? 0.1573 0.1334 0.2131 0.0144  0.0107  0.0244  36  SER   A N   
241  C CA  A SER   A 30  ? 0.1674 0.1395 0.2275 0.0172  0.0145  0.0224  36  SER   A CA  
242  C CA  B SER   A 30  ? 0.1789 0.1512 0.2388 0.0171  0.0144  0.0222  36  SER   A CA  
243  C C   . SER   A 30  ? 0.1761 0.1555 0.2411 0.0199  0.0133  0.0281  36  SER   A C   
244  O O   . SER   A 30  ? 0.1794 0.1591 0.2440 0.0210  0.0145  0.0249  36  SER   A O   
245  C CB  A SER   A 30  ? 0.1822 0.1453 0.2496 0.0188  0.0204  0.0227  36  SER   A CB  
246  C CB  B SER   A 30  ? 0.2276 0.1904 0.2941 0.0185  0.0204  0.0216  36  SER   A CB  
247  O OG  A SER   A 30  ? 0.1793 0.1385 0.2524 0.0217  0.0254  0.0213  36  SER   A OG  
248  O OG  B SER   A 30  ? 0.2883 0.2520 0.3625 0.0204  0.0207  0.0301  36  SER   A OG  
249  N N   . SER   A 31  ? 0.1708 0.1571 0.2402 0.0204  0.0106  0.0367  37  SER   A N   
250  C CA  . SER   A 31  ? 0.1694 0.1645 0.2441 0.0224  0.0089  0.0430  37  SER   A CA  
251  C C   . SER   A 31  ? 0.1593 0.1605 0.2258 0.0199  0.0054  0.0393  37  SER   A C   
252  O O   . SER   A 31  ? 0.1712 0.1781 0.2413 0.0214  0.0050  0.0418  37  SER   A O   
253  C CB  . SER   A 31  ? 0.1972 0.2002 0.2773 0.0222  0.0059  0.0537  37  SER   A CB  
254  O OG  . SER   A 31  ? 0.2699 0.2791 0.3405 0.0170  0.0010  0.0541  37  SER   A OG  
255  N N   . ARG   A 32  ? 0.1424 0.1423 0.1987 0.0163  0.0032  0.0335  38  ARG   A N   
256  C CA  . ARG   A 32  ? 0.1411 0.1450 0.1897 0.0139  0.0007  0.0297  38  ARG   A CA  
257  C C   . ARG   A 32  ? 0.1448 0.1424 0.1890 0.0142  0.0025  0.0217  38  ARG   A C   
258  O O   . ARG   A 32  ? 0.1437 0.1436 0.1825 0.0127  0.0008  0.0188  38  ARG   A O   
259  C CB  . ARG   A 32  ? 0.1444 0.1514 0.1856 0.0094  -0.0023 0.0291  38  ARG   A CB  
260  C CG  . ARG   A 32  ? 0.1642 0.1794 0.2070 0.0072  -0.0047 0.0368  38  ARG   A CG  
261  C CD  . ARG   A 32  ? 0.1650 0.1827 0.1998 0.0019  -0.0065 0.0353  38  ARG   A CD  
262  N NE  . ARG   A 32  ? 0.1454 0.1651 0.1734 -0.0008 -0.0071 0.0305  38  ARG   A NE  
263  C CZ  . ARG   A 32  ? 0.1728 0.1971 0.1942 -0.0063 -0.0081 0.0299  38  ARG   A CZ  
264  N NH1 . ARG   A 32  ? 0.1864 0.2147 0.2060 -0.0101 -0.0092 0.0339  38  ARG   A NH1 
265  N NH2 . ARG   A 32  ? 0.1689 0.1936 0.1851 -0.0086 -0.0078 0.0254  38  ARG   A NH2 
266  N N   . ASP   A 33  ? 0.1378 0.1276 0.1837 0.0154  0.0057  0.0182  39  ASP   A N   
267  C CA  . ASP   A 33  ? 0.1300 0.1149 0.1706 0.0142  0.0068  0.0112  39  ASP   A CA  
268  C C   . ASP   A 33  ? 0.1222 0.1086 0.1558 0.0114  0.0035  0.0082  39  ASP   A C   
269  O O   . ASP   A 33  ? 0.1354 0.1214 0.1645 0.0104  0.0026  0.0045  39  ASP   A O   
270  C CB  . ASP   A 33  ? 0.1420 0.1273 0.1823 0.0153  0.0082  0.0092  39  ASP   A CB  
271  C CG  . ASP   A 33  ? 0.1455 0.1262 0.1797 0.0133  0.0093  0.0026  39  ASP   A CG  
272  O OD1 . ASP   A 33  ? 0.1672 0.1425 0.2008 0.0119  0.0113  -0.0007 39  ASP   A OD1 
273  O OD2 . ASP   A 33  ? 0.1637 0.1466 0.1938 0.0125  0.0082  0.0008  39  ASP   A OD2 
274  N N   . LEU   A 34  ? 0.1304 0.1180 0.1637 0.0100  0.0020  0.0100  40  LEU   A N   
275  C CA  . LEU   A 34  ? 0.1237 0.1126 0.1523 0.0076  -0.0001 0.0072  40  LEU   A CA  
276  C C   . LEU   A 34  ? 0.1320 0.1178 0.1610 0.0062  0.0005  0.0054  40  LEU   A C   
277  O O   . LEU   A 34  ? 0.1411 0.1249 0.1732 0.0063  0.0019  0.0078  40  LEU   A O   
278  C CB  . LEU   A 34  ? 0.1321 0.1263 0.1589 0.0060  -0.0017 0.0100  40  LEU   A CB  
279  C CG  . LEU   A 34  ? 0.1451 0.1434 0.1699 0.0058  -0.0027 0.0107  40  LEU   A CG  
280  C CD1 . LEU   A 34  ? 0.1600 0.1633 0.1819 0.0025  -0.0037 0.0126  40  LEU   A CD1 
281  C CD2 . LEU   A 34  ? 0.1549 0.1511 0.1766 0.0061  -0.0029 0.0065  40  LEU   A CD2 
282  N N   . LEU   A 35  ? 0.1268 0.1129 0.1534 0.0048  -0.0007 0.0020  41  LEU   A N   
283  C CA  . LEU   A 35  ? 0.1197 0.1047 0.1471 0.0030  -0.0006 0.0004  41  LEU   A CA  
284  C C   . LEU   A 35  ? 0.1288 0.1173 0.1554 0.0022  -0.0022 -0.0009 41  LEU   A C   
285  O O   . LEU   A 35  ? 0.1339 0.1237 0.1591 0.0029  -0.0033 -0.0017 41  LEU   A O   
286  C CB  . LEU   A 35  ? 0.1275 0.1088 0.1548 0.0020  0.0004  -0.0028 41  LEU   A CB  
287  C CG  . LEU   A 35  ? 0.1381 0.1190 0.1664 -0.0006 0.0005  -0.0046 41  LEU   A CG  
288  C CD1 . LEU   A 35  ? 0.1602 0.1355 0.1886 -0.0023 0.0032  -0.0069 41  LEU   A CD1 
289  C CD2 . LEU   A 35  ? 0.1477 0.1330 0.1754 -0.0020 -0.0022 -0.0064 41  LEU   A CD2 
290  N N   . VAL   A 36  ? 0.1299 0.1196 0.1579 0.0006  -0.0017 -0.0008 42  VAL   A N   
291  C CA  . VAL   A 36  ? 0.1140 0.1066 0.1434 0.0000  -0.0019 -0.0021 42  VAL   A CA  
292  C C   . VAL   A 36  ? 0.1181 0.1115 0.1508 -0.0014 -0.0019 -0.0035 42  VAL   A C   
293  O O   . VAL   A 36  ? 0.1352 0.1272 0.1684 -0.0029 -0.0008 -0.0032 42  VAL   A O   
294  C CB  . VAL   A 36  ? 0.1193 0.1135 0.1475 -0.0013 -0.0003 -0.0012 42  VAL   A CB  
295  C CG1 . VAL   A 36  ? 0.1420 0.1379 0.1729 -0.0019 0.0011  -0.0031 42  VAL   A CG1 
296  C CG2 . VAL   A 36  ? 0.1432 0.1379 0.1679 -0.0008 -0.0007 0.0004  42  VAL   A CG2 
297  N N   . SER   A 37  ? 0.1216 0.1178 0.1571 -0.0011 -0.0033 -0.0044 43  SER   A N   
298  C CA  . SER   A 37  ? 0.1172 0.1164 0.1572 -0.0026 -0.0037 -0.0051 43  SER   A CA  
299  C C   . SER   A 37  ? 0.1326 0.1356 0.1784 -0.0017 -0.0028 -0.0048 43  SER   A C   
300  O O   . SER   A 37  ? 0.1339 0.1365 0.1799 0.0000  -0.0018 -0.0043 43  SER   A O   
301  C CB  . SER   A 37  ? 0.1406 0.1413 0.1801 -0.0037 -0.0063 -0.0057 43  SER   A CB  
302  O OG  . SER   A 37  ? 0.1497 0.1524 0.1890 -0.0022 -0.0084 -0.0045 43  SER   A OG  
303  N N   . SER   A 38  ? 0.1343 0.1410 0.1858 -0.0031 -0.0024 -0.0051 44  SER   A N   
304  C CA  . SER   A 38  ? 0.1473 0.1578 0.2067 -0.0019 -0.0005 -0.0047 44  SER   A CA  
305  C C   . SER   A 38  ? 0.1705 0.1863 0.2362 -0.0003 -0.0036 -0.0023 44  SER   A C   
306  O O   . SER   A 38  ? 0.1916 0.2101 0.2558 -0.0018 -0.0074 -0.0014 44  SER   A O   
307  C CB  . SER   A 38  ? 0.1852 0.1977 0.2486 -0.0042 0.0019  -0.0059 44  SER   A CB  
308  O OG  . SER   A 38  ? 0.2217 0.2374 0.2865 -0.0062 -0.0009 -0.0057 44  SER   A OG  
309  N N   . THR   A 39  ? 0.1659 0.1834 0.2390 0.0024  -0.0016 -0.0008 45  THR   A N   
310  C CA  . THR   A 39  ? 0.1846 0.2079 0.2656 0.0045  -0.0045 0.0031  45  THR   A CA  
311  C C   . THR   A 39  ? 0.2004 0.2290 0.2950 0.0061  -0.0018 0.0047  45  THR   A C   
312  O O   . THR   A 39  ? 0.1898 0.2155 0.2869 0.0062  0.0039  0.0020  45  THR   A O   
313  C CB  . THR   A 39  ? 0.2012 0.2209 0.2805 0.0073  -0.0042 0.0047  45  THR   A CB  
314  O OG1 . THR   A 39  ? 0.2127 0.2278 0.2946 0.0088  0.0016  0.0028  45  THR   A OG1 
315  C CG2 . THR   A 39  ? 0.2124 0.2273 0.2795 0.0061  -0.0063 0.0032  45  THR   A CG2 
316  N N   . THR   A 40  ? 0.2075 0.2445 0.3112 0.0071  -0.0055 0.0095  46  THR   A N   
317  C CA  . THR   A 40  ? 0.2242 0.2675 0.3435 0.0093  -0.0029 0.0122  46  THR   A CA  
318  C C   . THR   A 40  ? 0.2243 0.2640 0.3513 0.0140  0.0014  0.0141  46  THR   A C   
319  O O   . THR   A 40  ? 0.2503 0.2886 0.3866 0.0157  0.0080  0.0126  46  THR   A O   
320  C CB  . THR   A 40  ? 0.2672 0.3226 0.3943 0.0080  -0.0090 0.0174  46  THR   A CB  
321  O OG1 . THR   A 40  ? 0.3180 0.3758 0.4418 0.0083  -0.0145 0.0218  46  THR   A OG1 
322  C CG2 . THR   A 40  ? 0.2779 0.3356 0.3978 0.0026  -0.0114 0.0143  46  THR   A CG2 
323  N N   . ALA   A 41  ? 0.2202 0.2578 0.3433 0.0156  -0.0015 0.0170  47  ALA   A N   
324  C CA  . ALA   A 41  ? 0.2307 0.2638 0.3606 0.0197  0.0027  0.0190  47  ALA   A CA  
325  C C   . ALA   A 41  ? 0.2284 0.2502 0.3471 0.0187  0.0078  0.0129  47  ALA   A C   
326  O O   . ALA   A 41  ? 0.2238 0.2423 0.3284 0.0158  0.0052  0.0098  47  ALA   A O   
327  C CB  . ALA   A 41  ? 0.2567 0.2935 0.3876 0.0213  -0.0031 0.0257  47  ALA   A CB  
328  N N   . GLN   A 42  ? 0.2140 0.2299 0.3390 0.0210  0.0150  0.0117  48  GLN   A N   
329  C CA  . GLN   A 42  ? 0.2212 0.2274 0.3358 0.0190  0.0200  0.0060  48  GLN   A CA  
330  C C   . GLN   A 42  ? 0.2216 0.2243 0.3299 0.0200  0.0170  0.0083  48  GLN   A C   
331  O O   . GLN   A 42  ? 0.2334 0.2382 0.3501 0.0235  0.0152  0.0142  48  GLN   A O   
332  C CB  . GLN   A 42  ? 0.2426 0.2433 0.3658 0.0198  0.0300  0.0026  48  GLN   A CB  
333  C CG  . GLN   A 42  ? 0.3078 0.3102 0.4337 0.0173  0.0347  -0.0017 48  GLN   A CG  
334  C CD  . GLN   A 42  ? 0.3852 0.3812 0.5187 0.0173  0.0457  -0.0060 48  GLN   A CD  
335  O OE1 . GLN   A 42  ? 0.3853 0.3822 0.5355 0.0217  0.0500  -0.0028 48  GLN   A OE1 
336  N NE2 . GLN   A 42  ? 0.4141 0.4036 0.5355 0.0120  0.0509  -0.0130 48  GLN   A NE2 
337  N N   . GLY   A 43  ? 0.1959 0.1939 0.2899 0.0168  0.0165  0.0043  49  GLY   A N   
338  C CA  . GLY   A 43  ? 0.1984 0.1930 0.2850 0.0171  0.0140  0.0057  49  GLY   A CA  
339  C C   . GLY   A 43  ? 0.1899 0.1766 0.2763 0.0169  0.0207  0.0031  49  GLY   A C   
340  O O   . GLY   A 43  ? 0.1949 0.1778 0.2837 0.0154  0.0278  -0.0012 49  GLY   A O   
341  N N   . CYS   A 44  ? 0.1821 0.1659 0.2639 0.0174  0.0187  0.0052  50  CYS   A N   
342  C CA  . CYS   A 44  ? 0.1966 0.1724 0.2784 0.0171  0.0250  0.0032  50  CYS   A CA  
343  C C   . CYS   A 44  ? 0.1966 0.1685 0.2644 0.0126  0.0256  -0.0013 50  CYS   A C   
344  O O   . CYS   A 44  ? 0.2055 0.1708 0.2721 0.0111  0.0311  -0.0036 50  CYS   A O   
345  C CB  . CYS   A 44  ? 0.2087 0.1839 0.2988 0.0212  0.0237  0.0098  50  CYS   A CB  
346  S SG  . CYS   A 44  ? 0.2602 0.2398 0.3709 0.0266  0.0253  0.0161  50  CYS   A SG  
347  N N   . ASP   A 45  ? 0.1665 0.1425 0.2246 0.0107  0.0201  -0.0018 51  ASP   A N   
348  C CA  . ASP   A 45  ? 0.1615 0.1358 0.2079 0.0067  0.0201  -0.0050 51  ASP   A CA  
349  C C   . ASP   A 45  ? 0.1891 0.1615 0.2315 0.0020  0.0255  -0.0104 51  ASP   A C   
350  O O   . ASP   A 45  ? 0.2073 0.1818 0.2528 0.0015  0.0268  -0.0117 51  ASP   A O   
351  C CB  . ASP   A 45  ? 0.1551 0.1345 0.1947 0.0066  0.0132  -0.0034 51  ASP   A CB  
352  C CG  . ASP   A 45  ? 0.1742 0.1554 0.2149 0.0094  0.0083  0.0011  51  ASP   A CG  
353  O OD1 . ASP   A 45  ? 0.1857 0.1635 0.2275 0.0103  0.0096  0.0028  51  ASP   A OD1 
354  O OD2 . ASP   A 45  ? 0.1723 0.1579 0.2119 0.0101  0.0035  0.0027  51  ASP   A OD2 
355  N N   . THR   A 46  ? 0.1985 0.1680 0.2334 -0.0022 0.0283  -0.0135 52  THR   A N   
356  C CA  . THR   A 46  ? 0.2173 0.1863 0.2454 -0.0087 0.0328  -0.0185 52  THR   A CA  
357  C C   . THR   A 46  ? 0.2042 0.1784 0.2219 -0.0119 0.0275  -0.0176 52  THR   A C   
358  O O   . THR   A 46  ? 0.2130 0.1877 0.2283 -0.0106 0.0243  -0.0154 52  THR   A O   
359  C CB  . THR   A 46  ? 0.2894 0.2510 0.3172 -0.0122 0.0409  -0.0228 52  THR   A CB  
360  O OG1 . THR   A 46  ? 0.3356 0.2924 0.3752 -0.0088 0.0468  -0.0235 52  THR   A OG1 
361  C CG2 . THR   A 46  ? 0.3324 0.2943 0.3497 -0.0209 0.0448  -0.0282 52  THR   A CG2 
362  N N   . ILE   A 47  ? 0.1886 0.1670 0.2010 -0.0160 0.0269  -0.0187 53  ILE   A N   
363  C CA  . ILE   A 47  ? 0.1732 0.1575 0.1780 -0.0187 0.0222  -0.0166 53  ILE   A CA  
364  C C   . ILE   A 47  ? 0.1791 0.1638 0.1758 -0.0262 0.0255  -0.0197 53  ILE   A C   
365  O O   . ILE   A 47  ? 0.1999 0.1823 0.1937 -0.0319 0.0313  -0.0242 53  ILE   A O   
366  C CB  . ILE   A 47  ? 0.1701 0.1597 0.1738 -0.0195 0.0193  -0.0148 53  ILE   A CB  
367  C CG1 . ILE   A 47  ? 0.1847 0.1737 0.1960 -0.0135 0.0169  -0.0128 53  ILE   A CG1 
368  C CG2 . ILE   A 47  ? 0.1733 0.1693 0.1717 -0.0212 0.0143  -0.0111 53  ILE   A CG2 
369  C CD1 . ILE   A 47  ? 0.1841 0.1732 0.1982 -0.0081 0.0122  -0.0095 53  ILE   A CD1 
370  N N   . ALA   A 48  ? 0.1632 0.1511 0.1558 -0.0270 0.0221  -0.0175 54  ALA   A N   
371  C CA  . ALA   A 48  ? 0.1750 0.1654 0.1595 -0.0349 0.0240  -0.0197 54  ALA   A CA  
372  C C   . ALA   A 48  ? 0.1784 0.1768 0.1570 -0.0410 0.0223  -0.0186 54  ALA   A C   
373  O O   . ALA   A 48  ? 0.1811 0.1850 0.1616 -0.0381 0.0172  -0.0139 54  ALA   A O   
374  C CB  . ALA   A 48  ? 0.1671 0.1611 0.1502 -0.0337 0.0199  -0.0165 54  ALA   A CB  
375  N N   . ARG   A 49  ? 0.2043 0.2031 0.1752 -0.0503 0.0270  -0.0230 55  ARG   A N   
376  C CA  . ARG   A 49  ? 0.2228 0.2303 0.1863 -0.0580 0.0253  -0.0216 55  ARG   A CA  
377  C C   . ARG   A 49  ? 0.2470 0.2594 0.2020 -0.0669 0.0258  -0.0229 55  ARG   A C   
378  O O   . ARG   A 49  ? 0.2650 0.2744 0.2129 -0.0756 0.0322  -0.0291 55  ARG   A O   
379  C CB  . ARG   A 49  ? 0.2315 0.2351 0.1931 -0.0622 0.0313  -0.0265 55  ARG   A CB  
380  C CG  . ARG   A 49  ? 0.2356 0.2344 0.2067 -0.0537 0.0314  -0.0258 55  ARG   A CG  
381  C CD  . ARG   A 49  ? 0.2183 0.2236 0.1927 -0.0487 0.0239  -0.0187 55  ARG   A CD  
382  N NE  . ARG   A 49  ? 0.1980 0.1986 0.1806 -0.0420 0.0246  -0.0189 55  ARG   A NE  
383  C CZ  . ARG   A 49  ? 0.2057 0.2085 0.1935 -0.0357 0.0193  -0.0140 55  ARG   A CZ  
384  N NH1 . ARG   A 49  ? 0.1935 0.2024 0.1800 -0.0350 0.0136  -0.0084 55  ARG   A NH1 
385  N NH2 . ARG   A 49  ? 0.2280 0.2270 0.2231 -0.0305 0.0201  -0.0146 55  ARG   A NH2 
386  N N   . CYS   A 50  ? 0.2379 0.2578 0.1939 -0.0649 0.0196  -0.0171 56  CYS   A N   
387  C CA  . CYS   A 50  ? 0.2428 0.2679 0.1929 -0.0717 0.0193  -0.0175 56  CYS   A CA  
388  C C   . CYS   A 50  ? 0.2460 0.2836 0.1982 -0.0703 0.0114  -0.0092 56  CYS   A C   
389  O O   . CYS   A 50  ? 0.2588 0.2998 0.2176 -0.0634 0.0066  -0.0032 56  CYS   A O   
390  C CB  . CYS   A 50  ? 0.2494 0.2644 0.2023 -0.0680 0.0232  -0.0216 56  CYS   A CB  
391  S SG  . CYS   A 50  ? 0.2410 0.2543 0.2047 -0.0547 0.0178  -0.0160 56  CYS   A SG  
392  N N   . ASP   A 51  ? 0.2811 0.3248 0.2285 -0.0768 0.0108  -0.0092 57  ASP   A N   
393  C CA  . ASP   A 51  ? 0.3047 0.3613 0.2549 -0.0765 0.0042  -0.0016 57  ASP   A CA  
394  C C   . ASP   A 51  ? 0.2940 0.3478 0.2490 -0.0712 0.0039  -0.0016 57  ASP   A C   
395  O O   . ASP   A 51  ? 0.2976 0.3623 0.2539 -0.0731 0.0000  0.0032  57  ASP   A O   
396  C CB  . ASP   A 51  ? 0.3672 0.4367 0.3080 -0.0899 0.0029  -0.0005 57  ASP   A CB  
397  C CG  . ASP   A 51  ? 0.5109 0.5748 0.4409 -0.1006 0.0097  -0.0097 57  ASP   A CG  
398  O OD1 . ASP   A 51  ? 0.5519 0.6260 0.4724 -0.1133 0.0093  -0.0098 57  ASP   A OD1 
399  O OD2 . ASP   A 51  ? 0.5716 0.6213 0.5029 -0.0969 0.0157  -0.0164 57  ASP   A OD2 
400  N N   . CYS   A 52  ? 0.2639 0.3044 0.2220 -0.0646 0.0078  -0.0061 58  CYS   A N   
401  C CA  . CYS   A 52  ? 0.2342 0.2719 0.1957 -0.0605 0.0077  -0.0061 58  CYS   A CA  
402  C C   . CYS   A 52  ? 0.2309 0.2762 0.2005 -0.0533 0.0021  0.0010  58  CYS   A C   
403  O O   . CYS   A 52  ? 0.2468 0.2928 0.2221 -0.0470 -0.0005 0.0047  58  CYS   A O   
404  C CB  . CYS   A 52  ? 0.2503 0.2729 0.2140 -0.0548 0.0124  -0.0110 58  CYS   A CB  
405  S SG  . CYS   A 52  ? 0.2510 0.2621 0.2079 -0.0623 0.0213  -0.0199 58  CYS   A SG  
406  N N   . GLN   A 53  ? 0.1973 0.2477 0.1676 -0.0545 0.0010  0.0025  59  GLN   A N   
407  C CA  A GLN   A 53  ? 0.1868 0.2428 0.1655 -0.0476 -0.0027 0.0081  59  GLN   A CA  
408  C CA  B GLN   A 53  ? 0.1876 0.2445 0.1662 -0.0481 -0.0028 0.0083  59  GLN   A CA  
409  C C   . GLN   A 53  ? 0.1645 0.2137 0.1442 -0.0443 -0.0005 0.0054  59  GLN   A C   
410  O O   . GLN   A 53  ? 0.1699 0.2239 0.1553 -0.0405 -0.0023 0.0087  59  GLN   A O   
411  C CB  A GLN   A 53  ? 0.2067 0.2794 0.1883 -0.0515 -0.0072 0.0151  59  GLN   A CB  
412  C CB  B GLN   A 53  ? 0.2073 0.2811 0.1882 -0.0529 -0.0070 0.0147  59  GLN   A CB  
413  C CG  A GLN   A 53  ? 0.1897 0.2681 0.1702 -0.0543 -0.0096 0.0186  59  GLN   A CG  
414  C CG  B GLN   A 53  ? 0.1920 0.2757 0.1783 -0.0514 -0.0113 0.0222  59  GLN   A CG  
415  C CD  A GLN   A 53  ? 0.1865 0.2586 0.1738 -0.0450 -0.0102 0.0205  59  GLN   A CD  
416  C CD  B GLN   A 53  ? 0.2164 0.3176 0.2087 -0.0539 -0.0158 0.0304  59  GLN   A CD  
417  O OE1 A GLN   A 53  ? 0.1970 0.2661 0.1919 -0.0369 -0.0104 0.0221  59  GLN   A OE1 
418  O OE1 B GLN   A 53  ? 0.2327 0.3458 0.2205 -0.0630 -0.0183 0.0334  59  GLN   A OE1 
419  N NE2 A GLN   A 53  ? 0.1792 0.2486 0.1636 -0.0463 -0.0099 0.0198  59  GLN   A NE2 
420  N NE2 B GLN   A 53  ? 0.1697 0.2736 0.1727 -0.0464 -0.0167 0.0345  59  GLN   A NE2 
421  N N   . THR   A 54  ? 0.1530 0.1901 0.1277 -0.0454 0.0039  -0.0006 60  THR   A N   
422  C CA  . THR   A 54  ? 0.1652 0.1938 0.1405 -0.0418 0.0061  -0.0027 60  THR   A CA  
423  C C   . THR   A 54  ? 0.1607 0.1766 0.1366 -0.0372 0.0088  -0.0057 60  THR   A C   
424  O O   . THR   A 54  ? 0.1878 0.1999 0.1615 -0.0397 0.0110  -0.0083 60  THR   A O   
425  C CB  . THR   A 54  ? 0.2030 0.2308 0.1731 -0.0485 0.0091  -0.0057 60  THR   A CB  
426  O OG1 . THR   A 54  ? 0.2840 0.3053 0.2479 -0.0547 0.0135  -0.0107 60  THR   A OG1 
427  C CG2 . THR   A 54  ? 0.2013 0.2430 0.1714 -0.0536 0.0063  -0.0025 60  THR   A CG2 
428  N N   . GLY   A 55  ? 0.1491 0.1596 0.1283 -0.0309 0.0084  -0.0048 61  GLY   A N   
429  C CA  . GLY   A 55  ? 0.1544 0.1548 0.1354 -0.0264 0.0100  -0.0062 61  GLY   A CA  
430  C C   . GLY   A 55  ? 0.1404 0.1370 0.1236 -0.0212 0.0090  -0.0046 61  GLY   A C   
431  O O   . GLY   A 55  ? 0.1477 0.1469 0.1296 -0.0223 0.0086  -0.0038 61  GLY   A O   
432  N N   . VAL   A 56  ? 0.1303 0.1214 0.1166 -0.0164 0.0085  -0.0041 62  VAL   A N   
433  C CA  . VAL   A 56  ? 0.1235 0.1114 0.1107 -0.0126 0.0073  -0.0023 62  VAL   A CA  
434  C C   . VAL   A 56  ? 0.1255 0.1144 0.1160 -0.0081 0.0045  -0.0009 62  VAL   A C   
435  O O   . VAL   A 56  ? 0.1434 0.1312 0.1363 -0.0071 0.0046  -0.0014 62  VAL   A O   
436  C CB  . VAL   A 56  ? 0.1571 0.1362 0.1445 -0.0126 0.0102  -0.0025 62  VAL   A CB  
437  C CG1 . VAL   A 56  ? 0.1905 0.1672 0.1789 -0.0091 0.0083  0.0005  62  VAL   A CG1 
438  C CG2 . VAL   A 56  ? 0.1710 0.1478 0.1547 -0.0178 0.0139  -0.0045 62  VAL   A CG2 
439  N N   . TYR   A 57  ? 0.1236 0.1145 0.1140 -0.0059 0.0025  0.0005  63  TYR   A N   
440  C CA  . TYR   A 57  ? 0.1197 0.1108 0.1125 -0.0026 0.0004  0.0011  63  TYR   A CA  
441  C C   . TYR   A 57  ? 0.1260 0.1144 0.1173 -0.0014 -0.0008 0.0024  63  TYR   A C   
442  O O   . TYR   A 57  ? 0.1378 0.1255 0.1260 -0.0027 -0.0002 0.0030  63  TYR   A O   
443  C CB  . TYR   A 57  ? 0.1208 0.1173 0.1154 -0.0016 -0.0004 0.0012  63  TYR   A CB  
444  C CG  . TYR   A 57  ? 0.1208 0.1192 0.1144 -0.0013 0.0001  0.0012  63  TYR   A CG  
445  C CD1 . TYR   A 57  ? 0.1400 0.1416 0.1326 -0.0034 0.0013  0.0014  63  TYR   A CD1 
446  C CD2 . TYR   A 57  ? 0.1311 0.1284 0.1246 0.0003  -0.0002 0.0006  63  TYR   A CD2 
447  C CE1 . TYR   A 57  ? 0.1493 0.1528 0.1416 -0.0033 0.0024  0.0011  63  TYR   A CE1 
448  C CE2 . TYR   A 57  ? 0.1379 0.1366 0.1304 -0.0001 0.0013  -0.0002 63  TYR   A CE2 
449  C CZ  . TYR   A 57  ? 0.1582 0.1599 0.1504 -0.0016 0.0027  0.0002  63  TYR   A CZ  
450  O OH  . TYR   A 57  ? 0.1861 0.1893 0.1777 -0.0021 0.0050  -0.0009 63  TYR   A OH  
451  N N   . TYR   A 58  ? 0.1204 0.1082 0.1135 0.0005  -0.0026 0.0031  64  TYR   A N   
452  C CA  . TYR   A 58  ? 0.1239 0.1109 0.1148 0.0006  -0.0045 0.0047  64  TYR   A CA  
453  C C   . TYR   A 58  ? 0.1314 0.1209 0.1197 0.0000  -0.0048 0.0031  64  TYR   A C   
454  O O   . TYR   A 58  ? 0.1345 0.1252 0.1249 0.0010  -0.0047 0.0015  64  TYR   A O   
455  C CB  . TYR   A 58  ? 0.1305 0.1167 0.1252 0.0021  -0.0064 0.0068  64  TYR   A CB  
456  C CG  . TYR   A 58  ? 0.1486 0.1358 0.1408 0.0012  -0.0091 0.0096  64  TYR   A CG  
457  C CD1 . TYR   A 58  ? 0.1512 0.1368 0.1411 0.0001  -0.0092 0.0126  64  TYR   A CD1 
458  C CD2 . TYR   A 58  ? 0.1514 0.1414 0.1427 0.0005  -0.0115 0.0095  64  TYR   A CD2 
459  C CE1 . TYR   A 58  ? 0.1724 0.1600 0.1591 -0.0016 -0.0121 0.0161  64  TYR   A CE1 
460  C CE2 . TYR   A 58  ? 0.1614 0.1537 0.1489 -0.0018 -0.0143 0.0122  64  TYR   A CE2 
461  C CZ  . TYR   A 58  ? 0.1717 0.1632 0.1573 -0.0027 -0.0149 0.0160  64  TYR   A CZ  
462  O OH  . TYR   A 58  ? 0.2084 0.2030 0.1894 -0.0059 -0.0181 0.0196  64  TYR   A OH  
463  N N   . CYS   A 59  ? 0.1283 0.1179 0.1119 -0.0019 -0.0046 0.0034  65  CYS   A N   
464  C CA  . CYS   A 59  ? 0.1359 0.1270 0.1162 -0.0033 -0.0036 0.0011  65  CYS   A CA  
465  C C   . CYS   A 59  ? 0.1497 0.1409 0.1251 -0.0058 -0.0059 0.0023  65  CYS   A C   
466  O O   . CYS   A 59  ? 0.1494 0.1404 0.1204 -0.0080 -0.0067 0.0046  65  CYS   A O   
467  C CB  . CYS   A 59  ? 0.1406 0.1327 0.1188 -0.0046 -0.0010 0.0001  65  CYS   A CB  
468  S SG  . CYS   A 59  ? 0.1653 0.1585 0.1401 -0.0067 0.0022  -0.0035 65  CYS   A SG  
469  N N   . SER   A 60  ? 0.1424 0.1344 0.1181 -0.0062 -0.0072 0.0012  66  SER   A N   
470  C CA  . SER   A 60  ? 0.1573 0.1510 0.1279 -0.0098 -0.0101 0.0028  66  SER   A CA  
471  C C   . SER   A 60  ? 0.1664 0.1607 0.1287 -0.0144 -0.0084 0.0007  66  SER   A C   
472  O O   . SER   A 60  ? 0.1853 0.1818 0.1422 -0.0181 -0.0112 0.0038  66  SER   A O   
473  C CB  . SER   A 60  ? 0.1846 0.1796 0.1572 -0.0101 -0.0116 0.0016  66  SER   A CB  
474  O OG  . SER   A 60  ? 0.2148 0.2084 0.1860 -0.0113 -0.0080 -0.0037 66  SER   A OG  
475  N N   . SER   A 61  ? 0.1532 0.1461 0.1151 -0.0144 -0.0036 -0.0039 67  SER   A N   
476  C CA  . SER   A 61  ? 0.1599 0.1528 0.1144 -0.0190 -0.0006 -0.0068 67  SER   A CA  
477  C C   . SER   A 61  ? 0.1604 0.1538 0.1114 -0.0202 -0.0007 -0.0041 67  SER   A C   
478  O O   . SER   A 61  ? 0.1740 0.1678 0.1181 -0.0245 0.0017  -0.0061 67  SER   A O   
479  C CB  . SER   A 61  ? 0.1663 0.1574 0.1236 -0.0182 0.0055  -0.0125 67  SER   A CB  
480  O OG  . SER   A 61  ? 0.1827 0.1739 0.1474 -0.0136 0.0074  -0.0117 67  SER   A OG  
481  N N   . ARG   A 62  ? 0.1617 0.1547 0.1172 -0.0169 -0.0031 0.0002  68  ARG   A N   
482  C CA  . ARG   A 62  ? 0.1696 0.1621 0.1219 -0.0182 -0.0034 0.0035  68  ARG   A CA  
483  C C   . ARG   A 62  ? 0.1823 0.1743 0.1363 -0.0173 -0.0079 0.0099  68  ARG   A C   
484  O O   . ARG   A 62  ? 0.1897 0.1803 0.1421 -0.0180 -0.0081 0.0135  68  ARG   A O   
485  C CB  . ARG   A 62  ? 0.1770 0.1687 0.1341 -0.0155 -0.0003 0.0021  68  ARG   A CB  
486  C CG  . ARG   A 62  ? 0.1914 0.1847 0.1490 -0.0161 0.0045  -0.0028 68  ARG   A CG  
487  C CD  . ARG   A 62  ? 0.1920 0.1858 0.1421 -0.0206 0.0068  -0.0038 68  ARG   A CD  
488  N NE  . ARG   A 62  ? 0.2055 0.2007 0.1577 -0.0209 0.0123  -0.0086 68  ARG   A NE  
489  C CZ  . ARG   A 62  ? 0.2039 0.1986 0.1543 -0.0227 0.0157  -0.0129 68  ARG   A CZ  
490  N NH1 . ARG   A 62  ? 0.2120 0.2054 0.1573 -0.0252 0.0134  -0.0134 68  ARG   A NH1 
491  N NH2 . ARG   A 62  ? 0.2245 0.2201 0.1787 -0.0224 0.0218  -0.0169 68  ARG   A NH2 
492  N N   . ARG   A 63  ? 0.1818 0.1745 0.1401 -0.0152 -0.0108 0.0116  69  ARG   A N   
493  C CA  . ARG   A 63  ? 0.2001 0.1923 0.1635 -0.0130 -0.0140 0.0179  69  ARG   A CA  
494  C C   . ARG   A 63  ? 0.2302 0.2180 0.1980 -0.0103 -0.0116 0.0189  69  ARG   A C   
495  O O   . ARG   A 63  ? 0.2636 0.2494 0.2326 -0.0101 -0.0124 0.0242  69  ARG   A O   
496  C CB  . ARG   A 63  ? 0.2458 0.2409 0.2044 -0.0167 -0.0178 0.0239  69  ARG   A CB  
497  C CG  . ARG   A 63  ? 0.2675 0.2675 0.2245 -0.0191 -0.0213 0.0246  69  ARG   A CG  
498  C CD  . ARG   A 63  ? 0.2755 0.2797 0.2316 -0.0214 -0.0263 0.0334  69  ARG   A CD  
499  N NE  . ARG   A 63  ? 0.2919 0.3026 0.2428 -0.0264 -0.0297 0.0332  69  ARG   A NE  
500  C CZ  . ARG   A 63  ? 0.2568 0.2708 0.1963 -0.0336 -0.0303 0.0318  69  ARG   A CZ  
501  N NH1 . ARG   A 63  ? 0.2583 0.2701 0.1907 -0.0363 -0.0280 0.0315  69  ARG   A NH1 
502  N NH2 . ARG   A 63  ? 0.2637 0.2835 0.1981 -0.0390 -0.0329 0.0306  69  ARG   A NH2 
503  N N   . LYS   A 64  ? 0.1940 0.1805 0.1642 -0.0086 -0.0084 0.0143  70  LYS   A N   
504  C CA  . LYS   A 64  ? 0.2030 0.1860 0.1755 -0.0077 -0.0057 0.0142  70  LYS   A CA  
505  C C   . LYS   A 64  ? 0.1860 0.1688 0.1636 -0.0055 -0.0039 0.0109  70  LYS   A C   
506  O O   . LYS   A 64  ? 0.1857 0.1713 0.1642 -0.0047 -0.0039 0.0079  70  LYS   A O   
507  C CB  . LYS   A 64  ? 0.2437 0.2274 0.2108 -0.0106 -0.0032 0.0122  70  LYS   A CB  
508  C CG  . LYS   A 64  ? 0.3504 0.3328 0.3121 -0.0134 -0.0040 0.0162  70  LYS   A CG  
509  C CD  . LYS   A 64  ? 0.4574 0.4396 0.4153 -0.0161 -0.0009 0.0144  70  LYS   A CD  
510  C CE  . LYS   A 64  ? 0.5322 0.5133 0.4837 -0.0195 -0.0018 0.0186  70  LYS   A CE  
511  N NZ  . LYS   A 64  ? 0.5787 0.5636 0.5245 -0.0220 -0.0043 0.0191  70  LYS   A NZ  
512  N N   . HIS   A 65  ? 0.1731 0.1522 0.1538 -0.0050 -0.0019 0.0115  71  HIS   A N   
513  C CA  . HIS   A 65  ? 0.1607 0.1398 0.1444 -0.0046 0.0003  0.0083  71  HIS   A CA  
514  C C   . HIS   A 65  ? 0.1829 0.1634 0.1636 -0.0074 0.0027  0.0062  71  HIS   A C   
515  O O   . HIS   A 65  ? 0.2328 0.2104 0.2107 -0.0094 0.0042  0.0073  71  HIS   A O   
516  C CB  . HIS   A 65  ? 0.1517 0.1259 0.1402 -0.0035 0.0021  0.0092  71  HIS   A CB  
517  C CG  . HIS   A 65  ? 0.1689 0.1430 0.1625 -0.0005 -0.0001 0.0115  71  HIS   A CG  
518  N ND1 . HIS   A 65  ? 0.2071 0.1825 0.2045 0.0009  0.0000  0.0095  71  HIS   A ND1 
519  C CD2 . HIS   A 65  ? 0.1638 0.1377 0.1593 0.0008  -0.0026 0.0163  71  HIS   A CD2 
520  C CE1 . HIS   A 65  ? 0.1893 0.1649 0.1913 0.0032  -0.0020 0.0127  71  HIS   A CE1 
521  N NE2 . HIS   A 65  ? 0.2149 0.1902 0.2162 0.0032  -0.0039 0.0171  71  HIS   A NE2 
522  N N   . TYR   A 66  ? 0.1518 0.1372 0.1333 -0.0077 0.0030  0.0036  72  TYR   A N   
523  C CA  . TYR   A 66  ? 0.1590 0.1481 0.1388 -0.0106 0.0048  0.0023  72  TYR   A CA  
524  C C   . TYR   A 66  ? 0.1428 0.1342 0.1243 -0.0124 0.0059  0.0009  72  TYR   A C   
525  O O   . TYR   A 66  ? 0.1396 0.1331 0.1241 -0.0109 0.0048  0.0005  72  TYR   A O   
526  C CB  . TYR   A 66  ? 0.1570 0.1521 0.1377 -0.0097 0.0044  0.0017  72  TYR   A CB  
527  C CG  . TYR   A 66  ? 0.1675 0.1615 0.1447 -0.0097 0.0042  0.0021  72  TYR   A CG  
528  C CD1 . TYR   A 66  ? 0.1899 0.1835 0.1631 -0.0124 0.0057  0.0024  72  TYR   A CD1 
529  C CD2 . TYR   A 66  ? 0.1719 0.1656 0.1491 -0.0079 0.0030  0.0017  72  TYR   A CD2 
530  C CE1 . TYR   A 66  ? 0.2059 0.1989 0.1748 -0.0135 0.0059  0.0026  72  TYR   A CE1 
531  C CE2 . TYR   A 66  ? 0.1859 0.1791 0.1585 -0.0093 0.0032  0.0015  72  TYR   A CE2 
532  C CZ  . TYR   A 66  ? 0.1985 0.1916 0.1668 -0.0122 0.0047  0.0019  72  TYR   A CZ  
533  O OH  . TYR   A 66  ? 0.2369 0.2297 0.1994 -0.0146 0.0051  0.0016  72  TYR   A OH  
534  N N   . PRO   A 67  ? 0.1489 0.1404 0.1282 -0.0165 0.0081  -0.0001 73  PRO   A N   
535  C CA  . PRO   A 67  ? 0.1489 0.1446 0.1284 -0.0200 0.0089  -0.0016 73  PRO   A CA  
536  C C   . PRO   A 67  ? 0.1658 0.1719 0.1481 -0.0199 0.0070  -0.0005 73  PRO   A C   
537  O O   . PRO   A 67  ? 0.2019 0.2118 0.1847 -0.0196 0.0070  0.0004  73  PRO   A O   
538  C CB  . PRO   A 67  ? 0.1746 0.1675 0.1501 -0.0254 0.0121  -0.0032 73  PRO   A CB  
539  C CG  . PRO   A 67  ? 0.1975 0.1870 0.1713 -0.0244 0.0125  -0.0018 73  PRO   A CG  
540  C CD  . PRO   A 67  ? 0.1574 0.1454 0.1330 -0.0190 0.0099  0.0003  73  PRO   A CD  
541  N N   . VAL   A 68  ? 0.1419 0.1530 0.1263 -0.0206 0.0059  -0.0001 74  VAL   A N   
542  C CA  . VAL   A 68  ? 0.1577 0.1793 0.1468 -0.0200 0.0039  0.0025  74  VAL   A CA  
543  C C   . VAL   A 68  ? 0.1461 0.1749 0.1349 -0.0247 0.0030  0.0033  74  VAL   A C   
544  O O   . VAL   A 68  ? 0.1627 0.1879 0.1483 -0.0271 0.0037  0.0015  74  VAL   A O   
545  C CB  . VAL   A 68  ? 0.1924 0.2138 0.1863 -0.0142 0.0025  0.0039  74  VAL   A CB  
546  C CG1 . VAL   A 68  ? 0.2065 0.2242 0.2006 -0.0110 0.0034  0.0033  74  VAL   A CG1 
547  C CG2 . VAL   A 68  ? 0.2021 0.2180 0.1954 -0.0127 0.0019  0.0030  74  VAL   A CG2 
548  N N   . SER   A 69  ? 0.1410 0.1814 0.1340 -0.0259 0.0014  0.0067  75  SER   A N   
549  C CA  . SER   A 69  ? 0.1389 0.1896 0.1334 -0.0299 -0.0009 0.0097  75  SER   A CA  
550  C C   . SER   A 69  ? 0.1264 0.1808 0.1289 -0.0239 -0.0030 0.0139  75  SER   A C   
551  O O   . SER   A 69  ? 0.1411 0.1956 0.1497 -0.0185 -0.0024 0.0153  75  SER   A O   
552  C CB  . SER   A 69  ? 0.1926 0.2555 0.1891 -0.0345 -0.0018 0.0124  75  SER   A CB  
553  O OG  . SER   A 69  ? 0.2860 0.3449 0.2747 -0.0407 0.0007  0.0082  75  SER   A OG  
554  N N   . PHE   A 70  ? 0.1339 0.1903 0.1362 -0.0249 -0.0046 0.0155  76  PHE   A N   
555  C CA  . PHE   A 70  ? 0.1296 0.1877 0.1393 -0.0193 -0.0062 0.0195  76  PHE   A CA  
556  C C   . PHE   A 70  ? 0.1310 0.2008 0.1435 -0.0227 -0.0093 0.0252  76  PHE   A C   
557  O O   . PHE   A 70  ? 0.1546 0.2288 0.1605 -0.0302 -0.0101 0.0246  76  PHE   A O   
558  C CB  . PHE   A 70  ? 0.1481 0.1941 0.1554 -0.0155 -0.0050 0.0158  76  PHE   A CB  
559  C CG  . PHE   A 70  ? 0.1389 0.1797 0.1386 -0.0198 -0.0042 0.0121  76  PHE   A CG  
560  C CD1 . PHE   A 70  ? 0.1342 0.1668 0.1281 -0.0217 -0.0016 0.0071  76  PHE   A CD1 
561  C CD2 . PHE   A 70  ? 0.1398 0.1832 0.1389 -0.0219 -0.0054 0.0136  76  PHE   A CD2 
562  C CE1 . PHE   A 70  ? 0.1507 0.1778 0.1395 -0.0253 0.0004  0.0036  76  PHE   A CE1 
563  C CE2 . PHE   A 70  ? 0.1495 0.1876 0.1421 -0.0260 -0.0035 0.0095  76  PHE   A CE2 
564  C CZ  . PHE   A 70  ? 0.1556 0.1854 0.1436 -0.0275 -0.0003 0.0044  76  PHE   A CZ  
565  N N   . SER   A 71  ? 0.1264 0.2013 0.1486 -0.0178 -0.0107 0.0311  77  SER   A N   
566  C CA  . SER   A 71  ? 0.1345 0.2217 0.1610 -0.0205 -0.0142 0.0386  77  SER   A CA  
567  C C   . SER   A 71  ? 0.1429 0.2266 0.1640 -0.0228 -0.0151 0.0379  77  SER   A C   
568  O O   . SER   A 71  ? 0.1485 0.2199 0.1650 -0.0205 -0.0128 0.0322  77  SER   A O   
569  C CB  . SER   A 71  ? 0.1536 0.2469 0.1946 -0.0137 -0.0145 0.0458  77  SER   A CB  
570  O OG  . SER   A 71  ? 0.1770 0.2594 0.2218 -0.0067 -0.0121 0.0440  77  SER   A OG  
571  N N   . LYS   A 72  ? 0.1425 0.2374 0.1636 -0.0277 -0.0185 0.0441  78  LYS   A N   
572  C CA  . LYS   A 72  ? 0.1478 0.2402 0.1639 -0.0303 -0.0192 0.0440  78  LYS   A CA  
573  C C   . LYS   A 72  ? 0.1607 0.2474 0.1852 -0.0221 -0.0189 0.0471  78  LYS   A C   
574  O O   . LYS   A 72  ? 0.1604 0.2501 0.1963 -0.0160 -0.0190 0.0522  78  LYS   A O   
575  C CB  . LYS   A 72  ? 0.1728 0.2803 0.1860 -0.0390 -0.0233 0.0505  78  LYS   A CB  
576  C CG  . LYS   A 72  ? 0.2262 0.3378 0.2289 -0.0488 -0.0228 0.0458  78  LYS   A CG  
577  C CD  . LYS   A 72  ? 0.2956 0.4212 0.2922 -0.0595 -0.0265 0.0508  78  LYS   A CD  
578  C CE  . LYS   A 72  ? 0.3808 0.5078 0.3649 -0.0705 -0.0246 0.0441  78  LYS   A CE  
579  N NZ  . LYS   A 72  ? 0.4368 0.5722 0.4109 -0.0820 -0.0263 0.0453  78  LYS   A NZ  
580  N N   . PRO   A 73  ? 0.1554 0.2340 0.1753 -0.0221 -0.0178 0.0439  79  PRO   A N   
581  C CA  . PRO   A 73  ? 0.1611 0.2337 0.1885 -0.0150 -0.0171 0.0462  79  PRO   A CA  
582  C C   . PRO   A 73  ? 0.1590 0.2421 0.1971 -0.0130 -0.0198 0.0570  79  PRO   A C   
583  O O   . PRO   A 73  ? 0.1838 0.2782 0.2202 -0.0189 -0.0233 0.0632  79  PRO   A O   
584  C CB  . PRO   A 73  ? 0.1956 0.2610 0.2151 -0.0178 -0.0161 0.0417  79  PRO   A CB  
585  C CG  . PRO   A 73  ? 0.2278 0.2940 0.2363 -0.0256 -0.0154 0.0364  79  PRO   A CG  
586  C CD  . PRO   A 73  ? 0.1784 0.2526 0.1865 -0.0288 -0.0165 0.0376  79  PRO   A CD  
587  N N   . SER   A 74  ? 0.1499 0.2295 0.1992 -0.0052 -0.0178 0.0595  80  SER   A N   
588  C CA  . SER   A 74  ? 0.1666 0.2556 0.2293 -0.0019 -0.0194 0.0705  80  SER   A CA  
589  C C   . SER   A 74  ? 0.1499 0.2288 0.2225 0.0063  -0.0156 0.0710  80  SER   A C   
590  O O   . SER   A 74  ? 0.1492 0.2152 0.2181 0.0091  -0.0119 0.0625  80  SER   A O   
591  C CB  . SER   A 74  ? 0.2288 0.3281 0.2986 -0.0014 -0.0201 0.0743  80  SER   A CB  
592  O OG  . SER   A 74  ? 0.3468 0.4524 0.4064 -0.0090 -0.0223 0.0709  80  SER   A OG  
593  N N   . LEU   A 75  ? 0.1621 0.2481 0.2489 0.0102  -0.0160 0.0816  81  LEU   A N   
594  C CA  . LEU   A 75  ? 0.1833 0.2602 0.2817 0.0178  -0.0113 0.0830  81  LEU   A CA  
595  C C   . LEU   A 75  ? 0.1999 0.2776 0.3090 0.0229  -0.0075 0.0828  81  LEU   A C   
596  O O   . LEU   A 75  ? 0.2205 0.3113 0.3402 0.0237  -0.0093 0.0916  81  LEU   A O   
597  C CB  . LEU   A 75  ? 0.1931 0.2775 0.3019 0.0189  -0.0137 0.0958  81  LEU   A CB  
598  C CG  . LEU   A 75  ? 0.2285 0.3026 0.3493 0.0260  -0.0085 0.0981  81  LEU   A CG  
599  C CD1 . LEU   A 75  ? 0.2405 0.3003 0.3507 0.0249  -0.0064 0.0893  81  LEU   A CD1 
600  C CD2 . LEU   A 75  ? 0.2430 0.3268 0.3765 0.0275  -0.0112 0.1131  81  LEU   A CD2 
601  N N   . ILE   A 76  ? 0.1909 0.2557 0.2972 0.0259  -0.0022 0.0729  82  ILE   A N   
602  C CA  . ILE   A 76  ? 0.2137 0.2773 0.3272 0.0296  0.0025  0.0701  82  ILE   A CA  
603  C C   . ILE   A 76  ? 0.2246 0.2758 0.3466 0.0355  0.0099  0.0670  82  ILE   A C   
604  O O   . ILE   A 76  ? 0.2163 0.2555 0.3314 0.0352  0.0119  0.0609  82  ILE   A O   
605  C CB  . ILE   A 76  ? 0.2433 0.3030 0.3423 0.0256  0.0021  0.0599  82  ILE   A CB  
606  C CG1 . ILE   A 76  ? 0.2694 0.3400 0.3593 0.0189  -0.0042 0.0618  82  ILE   A CG1 
607  C CG2 . ILE   A 76  ? 0.2650 0.3218 0.3689 0.0287  0.0074  0.0554  82  ILE   A CG2 
608  C CD1 . ILE   A 76  ? 0.2898 0.3592 0.3695 0.0153  -0.0045 0.0547  82  ILE   A CD1 
609  N N   . PHE   A 77  ? 0.2282 0.2820 0.3651 0.0405  0.0147  0.0707  83  PHE   A N   
610  C CA  . PHE   A 77  ? 0.2305 0.2717 0.3759 0.0456  0.0234  0.0668  83  PHE   A CA  
611  C C   . PHE   A 77  ? 0.2449 0.2762 0.3787 0.0434  0.0273  0.0540  83  PHE   A C   
612  O O   . PHE   A 77  ? 0.2726 0.3093 0.4020 0.0414  0.0261  0.0513  83  PHE   A O   
613  C CB  . PHE   A 77  ? 0.2362 0.2836 0.4034 0.0518  0.0284  0.0752  83  PHE   A CB  
614  C CG  . PHE   A 77  ? 0.2724 0.3059 0.4501 0.0569  0.0381  0.0725  83  PHE   A CG  
615  C CD1 . PHE   A 77  ? 0.2989 0.3264 0.4817 0.0589  0.0390  0.0771  83  PHE   A CD1 
616  C CD2 . PHE   A 77  ? 0.3053 0.3309 0.4865 0.0588  0.0470  0.0646  83  PHE   A CD2 
617  C CE1 . PHE   A 77  ? 0.3251 0.3386 0.5171 0.0630  0.0489  0.0739  83  PHE   A CE1 
618  C CE2 . PHE   A 77  ? 0.3135 0.3254 0.5037 0.0625  0.0571  0.0611  83  PHE   A CE2 
619  C CZ  . PHE   A 77  ? 0.3218 0.3275 0.5176 0.0647  0.0581  0.0658  83  PHE   A CZ  
620  N N   . VAL   A 78  ? 0.2206 0.2381 0.3474 0.0427  0.0310  0.0462  84  VAL   A N   
621  C CA  . VAL   A 78  ? 0.2063 0.2148 0.3210 0.0398  0.0341  0.0347  84  VAL   A CA  
622  C C   . VAL   A 78  ? 0.1978 0.1949 0.3203 0.0426  0.0442  0.0300  84  VAL   A C   
623  O O   . VAL   A 78  ? 0.2019 0.1923 0.3306 0.0447  0.0474  0.0317  84  VAL   A O   
624  C CB  . VAL   A 78  ? 0.1861 0.1892 0.2846 0.0351  0.0294  0.0291  84  VAL   A CB  
625  C CG1 . VAL   A 78  ? 0.1998 0.1951 0.2864 0.0317  0.0319  0.0186  84  VAL   A CG1 
626  C CG2 . VAL   A 78  ? 0.1984 0.2116 0.2900 0.0321  0.0208  0.0333  84  VAL   A CG2 
627  N N   . GLU   A 79  ? 0.1975 0.1918 0.3182 0.0418  0.0494  0.0233  85  GLU   A N   
628  C CA  . GLU   A 79  ? 0.2159 0.1991 0.3426 0.0432  0.0603  0.0172  85  GLU   A CA  
629  C C   . GLU   A 79  ? 0.2218 0.1924 0.3372 0.0392  0.0624  0.0090  85  GLU   A C   
630  O O   . GLU   A 79  ? 0.2225 0.1935 0.3233 0.0348  0.0555  0.0061  85  GLU   A O   
631  C CB  . GLU   A 79  ? 0.2692 0.2531 0.3935 0.0416  0.0650  0.0111  85  GLU   A CB  
632  C CG  . GLU   A 79  ? 0.3650 0.3605 0.5042 0.0459  0.0656  0.0188  85  GLU   A CG  
633  C CD  . GLU   A 79  ? 0.5061 0.5020 0.6677 0.0529  0.0717  0.0268  85  GLU   A CD  
634  O OE1 . GLU   A 79  ? 0.5478 0.5319 0.7160 0.0545  0.0820  0.0219  85  GLU   A OE1 
635  O OE2 . GLU   A 79  ? 0.5522 0.5603 0.7250 0.0564  0.0662  0.0382  85  GLU   A OE2 
636  N N   . ALA   A 80  ? 0.2324 0.1919 0.3550 0.0404  0.0725  0.0048  86  ALA   A N   
637  C CA  . ALA   A 80  ? 0.2571 0.2045 0.3693 0.0356  0.0757  -0.0037 86  ALA   A CA  
638  C C   . ALA   A 80  ? 0.2725 0.2188 0.3661 0.0285  0.0734  -0.0130 86  ALA   A C   
639  O O   . ALA   A 80  ? 0.2926 0.2422 0.3834 0.0273  0.0749  -0.0159 86  ALA   A O   
640  C CB  . ALA   A 80  ? 0.2669 0.2021 0.3898 0.0372  0.0888  -0.0080 86  ALA   A CB  
641  N N   . SER   A 81  ? 0.2718 0.2145 0.3528 0.0237  0.0691  -0.0168 87  SER   A N   
642  C CA  . SER   A 81  ? 0.2726 0.2148 0.3363 0.0166  0.0663  -0.0246 87  SER   A CA  
643  C C   . SER   A 81  ? 0.2945 0.2265 0.3512 0.0111  0.0704  -0.0320 87  SER   A C   
644  O O   . SER   A 81  ? 0.3006 0.2250 0.3662 0.0132  0.0764  -0.0317 87  SER   A O   
645  C CB  . SER   A 81  ? 0.2696 0.2208 0.3247 0.0157  0.0546  -0.0204 87  SER   A CB  
646  O OG  . SER   A 81  ? 0.2571 0.2072 0.3119 0.0159  0.0505  -0.0177 87  SER   A OG  
647  N N   . GLU   A 82  ? 0.3096 0.2421 0.3505 0.0039  0.0665  -0.0377 88  GLU   A N   
648  C CA  . GLU   A 82  ? 0.3166 0.2415 0.3500 -0.0024 0.0691  -0.0443 88  GLU   A CA  
649  C C   . GLU   A 82  ? 0.2832 0.2087 0.3195 -0.0004 0.0637  -0.0394 88  GLU   A C   
650  O O   . GLU   A 82  ? 0.2954 0.2135 0.3302 -0.0040 0.0674  -0.0435 88  GLU   A O   
651  C CB  . GLU   A 82  ? 0.3806 0.3086 0.3971 -0.0108 0.0649  -0.0499 88  GLU   A CB  
652  C CG  . GLU   A 82  ? 0.4957 0.4211 0.5071 -0.0152 0.0720  -0.0566 88  GLU   A CG  
653  C CD  . GLU   A 82  ? 0.6255 0.5561 0.6205 -0.0234 0.0669  -0.0602 88  GLU   A CD  
654  O OE1 . GLU   A 82  ? 0.6308 0.5655 0.6183 -0.0268 0.0590  -0.0588 88  GLU   A OE1 
655  O OE2 . GLU   A 82  ? 0.6805 0.6115 0.6706 -0.0264 0.0706  -0.0638 88  GLU   A OE2 
656  N N   . TYR   A 83  ? 0.2535 0.1873 0.2938 0.0047  0.0556  -0.0311 89  TYR   A N   
657  C CA  . TYR   A 83  ? 0.2394 0.1747 0.2807 0.0056  0.0502  -0.0269 89  TYR   A CA  
658  C C   . TYR   A 83  ? 0.2255 0.1605 0.2802 0.0121  0.0513  -0.0192 89  TYR   A C   
659  O O   . TYR   A 83  ? 0.2272 0.1605 0.2831 0.0120  0.0495  -0.0170 89  TYR   A O   
660  C CB  . TYR   A 83  ? 0.2489 0.1936 0.2822 0.0046  0.0401  -0.0241 89  TYR   A CB  
661  C CG  . TYR   A 83  ? 0.2821 0.2276 0.3028 -0.0022 0.0380  -0.0302 89  TYR   A CG  
662  C CD1 . TYR   A 83  ? 0.3243 0.2680 0.3391 -0.0073 0.0365  -0.0334 89  TYR   A CD1 
663  C CD2 . TYR   A 83  ? 0.3117 0.2604 0.3264 -0.0042 0.0375  -0.0323 89  TYR   A CD2 
664  C CE1 . TYR   A 83  ? 0.3572 0.3038 0.3610 -0.0141 0.0336  -0.0377 89  TYR   A CE1 
665  C CE2 . TYR   A 83  ? 0.3487 0.2992 0.3518 -0.0109 0.0350  -0.0367 89  TYR   A CE2 
666  C CZ  . TYR   A 83  ? 0.3907 0.3404 0.3885 -0.0160 0.0330  -0.0392 89  TYR   A CZ  
667  O OH  . TYR   A 83  ? 0.4602 0.4136 0.4470 -0.0230 0.0298  -0.0422 89  TYR   A OH  
668  N N   . TYR   A 84  ? 0.2245 0.1619 0.2897 0.0175  0.0540  -0.0144 90  TYR   A N   
669  C CA  . TYR   A 84  ? 0.2108 0.1493 0.2901 0.0236  0.0548  -0.0055 90  TYR   A CA  
670  C C   . TYR   A 84  ? 0.2223 0.1577 0.3152 0.0282  0.0636  -0.0040 90  TYR   A C   
671  O O   . TYR   A 84  ? 0.2277 0.1657 0.3189 0.0278  0.0653  -0.0070 90  TYR   A O   
672  C CB  . TYR   A 84  ? 0.2060 0.1569 0.2859 0.0262  0.0457  0.0028  90  TYR   A CB  
673  C CG  . TYR   A 84  ? 0.1800 0.1348 0.2491 0.0227  0.0376  0.0026  90  TYR   A CG  
674  C CD1 . TYR   A 84  ? 0.1815 0.1343 0.2516 0.0223  0.0360  0.0053  90  TYR   A CD1 
675  C CD2 . TYR   A 84  ? 0.1814 0.1419 0.2402 0.0199  0.0321  -0.0001 90  TYR   A CD2 
676  C CE1 . TYR   A 84  ? 0.1713 0.1282 0.2328 0.0193  0.0293  0.0050  90  TYR   A CE1 
677  C CE2 . TYR   A 84  ? 0.1814 0.1453 0.2323 0.0172  0.0257  -0.0002 90  TYR   A CE2 
678  C CZ  . TYR   A 84  ? 0.1738 0.1360 0.2263 0.0170  0.0245  0.0021  90  TYR   A CZ  
679  O OH  . TYR   A 84  ? 0.1718 0.1375 0.2174 0.0143  0.0190  0.0017  90  TYR   A OH  
680  N N   . PRO   A 85  ? 0.2385 0.1695 0.3457 0.0328  0.0684  0.0018  91  PRO   A N   
681  C CA  . PRO   A 85  ? 0.2428 0.1733 0.3666 0.0386  0.0761  0.0058  91  PRO   A CA  
682  C C   . PRO   A 85  ? 0.2573 0.2027 0.3861 0.0424  0.0687  0.0149  91  PRO   A C   
683  O O   . PRO   A 85  ? 0.2535 0.2079 0.3738 0.0406  0.0587  0.0184  91  PRO   A O   
684  C CB  . PRO   A 85  ? 0.2703 0.1937 0.4083 0.0428  0.0812  0.0120  91  PRO   A CB  
685  C CG  . PRO   A 85  ? 0.2763 0.2034 0.4068 0.0407  0.0722  0.0160  91  PRO   A CG  
686  C CD  . PRO   A 85  ? 0.2503 0.1782 0.3607 0.0335  0.0668  0.0066  91  PRO   A CD  
687  N N   . ALA   A 86  ? 0.2601 0.2088 0.4040 0.0476  0.0739  0.0195  92  ALA   A N   
688  C CA  . ALA   A 86  ? 0.2529 0.2169 0.4032 0.0507  0.0673  0.0289  92  ALA   A CA  
689  C C   . ALA   A 86  ? 0.2521 0.2226 0.4086 0.0531  0.0606  0.0405  92  ALA   A C   
690  O O   . ALA   A 86  ? 0.2746 0.2382 0.4412 0.0560  0.0651  0.0445  92  ALA   A O   
691  C CB  . ALA   A 86  ? 0.2533 0.2192 0.4215 0.0562  0.0753  0.0322  92  ALA   A CB  
692  N N   . ARG   A 87  ? 0.2434 0.2257 0.3914 0.0506  0.0502  0.0448  93  ARG   A N   
693  C CA  . ARG   A 87  ? 0.2310 0.2196 0.3808 0.0508  0.0435  0.0543  93  ARG   A CA  
694  C C   . ARG   A 87  ? 0.2234 0.2269 0.3663 0.0480  0.0338  0.0589  93  ARG   A C   
695  O O   . ARG   A 87  ? 0.2338 0.2408 0.3693 0.0458  0.0324  0.0536  93  ARG   A O   
696  C CB  . ARG   A 87  ? 0.2414 0.2204 0.3785 0.0466  0.0422  0.0481  93  ARG   A CB  
697  C CG  . ARG   A 87  ? 0.2450 0.2272 0.3628 0.0406  0.0351  0.0412  93  ARG   A CG  
698  C CD  . ARG   A 87  ? 0.2536 0.2250 0.3599 0.0367  0.0366  0.0317  93  ARG   A CD  
699  N NE  . ARG   A 87  ? 0.2437 0.2193 0.3359 0.0320  0.0291  0.0291  93  ARG   A NE  
700  C CZ  . ARG   A 87  ? 0.2880 0.2673 0.3700 0.0292  0.0255  0.0243  93  ARG   A CZ  
701  N NH1 . ARG   A 87  ? 0.2887 0.2695 0.3716 0.0300  0.0279  0.0217  93  ARG   A NH1 
702  N NH2 . ARG   A 87  ? 0.2200 0.2018 0.2915 0.0255  0.0199  0.0223  93  ARG   A NH2 
703  N N   . TYR   A 88  ? 0.2243 0.2358 0.3680 0.0470  0.0274  0.0679  94  TYR   A N   
704  C CA  . TYR   A 88  ? 0.2291 0.2535 0.3638 0.0426  0.0187  0.0710  94  TYR   A CA  
705  C C   . TYR   A 88  ? 0.2064 0.2256 0.3230 0.0370  0.0150  0.0629  94  TYR   A C   
706  O O   . TYR   A 88  ? 0.2149 0.2276 0.3292 0.0363  0.0154  0.0626  94  TYR   A O   
707  C CB  . TYR   A 88  ? 0.2379 0.2742 0.3817 0.0432  0.0138  0.0849  94  TYR   A CB  
708  C CG  . TYR   A 88  ? 0.2453 0.2918 0.4070 0.0479  0.0152  0.0945  94  TYR   A CG  
709  C CD1 . TYR   A 88  ? 0.2531 0.3130 0.4139 0.0458  0.0110  0.0966  94  TYR   A CD1 
710  C CD2 . TYR   A 88  ? 0.2619 0.3045 0.4425 0.0546  0.0214  0.1014  94  TYR   A CD2 
711  C CE1 . TYR   A 88  ? 0.2722 0.3426 0.4504 0.0501  0.0124  0.1056  94  TYR   A CE1 
712  C CE2 . TYR   A 88  ? 0.2744 0.3270 0.4738 0.0596  0.0232  0.1109  94  TYR   A CE2 
713  C CZ  . TYR   A 88  ? 0.2809 0.3480 0.4791 0.0573  0.0185  0.1130  94  TYR   A CZ  
714  O OH  . TYR   A 88  ? 0.3133 0.3920 0.5309 0.0620  0.0200  0.1226  94  TYR   A OH  
715  N N   . GLN   A 89  ? 0.1782 0.2005 0.2828 0.0332  0.0118  0.0568  95  GLN   A N   
716  C CA  . GLN   A 89  ? 0.1574 0.1764 0.2465 0.0282  0.0083  0.0499  95  GLN   A CA  
717  C C   . GLN   A 89  ? 0.1495 0.1804 0.2335 0.0238  0.0017  0.0551  95  GLN   A C   
718  O O   . GLN   A 89  ? 0.1572 0.1981 0.2437 0.0231  -0.0005 0.0589  95  GLN   A O   
719  C CB  . GLN   A 89  ? 0.1681 0.1815 0.2484 0.0269  0.0100  0.0399  95  GLN   A CB  
720  C CG  . GLN   A 89  ? 0.1671 0.1773 0.2341 0.0226  0.0069  0.0339  95  GLN   A CG  
721  C CD  . GLN   A 89  ? 0.1714 0.1740 0.2309 0.0216  0.0090  0.0247  95  GLN   A CD  
722  O OE1 . GLN   A 89  ? 0.1984 0.1938 0.2604 0.0233  0.0138  0.0208  95  GLN   A OE1 
723  N NE2 . GLN   A 89  ? 0.1666 0.1705 0.2164 0.0183  0.0057  0.0212  95  GLN   A NE2 
724  N N   . SER   A 90  ? 0.1356 0.1659 0.2122 0.0202  -0.0012 0.0550  96  SER   A N   
725  C CA  . SER   A 90  ? 0.1410 0.1817 0.2114 0.0148  -0.0065 0.0590  96  SER   A CA  
726  C C   . SER   A 90  ? 0.1424 0.1811 0.1995 0.0103  -0.0077 0.0503  96  SER   A C   
727  O O   . SER   A 90  ? 0.1429 0.1721 0.1956 0.0115  -0.0053 0.0423  96  SER   A O   
728  C CB  . SER   A 90  ? 0.1862 0.2279 0.2566 0.0129  -0.0083 0.0644  96  SER   A CB  
729  O OG  . SER   A 90  ? 0.2258 0.2570 0.2894 0.0121  -0.0064 0.0570  96  SER   A OG  
730  N N   . HIS   A 91  ? 0.1421 0.1902 0.1934 0.0049  -0.0113 0.0525  97  HIS   A N   
731  C CA  . HIS   A 91  ? 0.1389 0.1856 0.1786 0.0000  -0.0119 0.0453  97  HIS   A CA  
732  C C   . HIS   A 91  ? 0.1334 0.1748 0.1719 0.0024  -0.0097 0.0388  97  HIS   A C   
733  O O   . HIS   A 91  ? 0.1467 0.1817 0.1778 0.0010  -0.0087 0.0318  97  HIS   A O   
734  C CB  . HIS   A 91  ? 0.1588 0.1983 0.1916 -0.0022 -0.0111 0.0405  97  HIS   A CB  
735  C CG  . HIS   A 91  ? 0.1778 0.2228 0.2098 -0.0059 -0.0132 0.0463  97  HIS   A CG  
736  N ND1 . HIS   A 91  ? 0.2095 0.2604 0.2328 -0.0133 -0.0148 0.0459  97  HIS   A ND1 
737  C CD2 . HIS   A 91  ? 0.2066 0.2515 0.2452 -0.0036 -0.0134 0.0525  97  HIS   A CD2 
738  C CE1 . HIS   A 91  ? 0.2183 0.2733 0.2424 -0.0156 -0.0164 0.0520  97  HIS   A CE1 
739  N NE2 . HIS   A 91  ? 0.2259 0.2775 0.2594 -0.0097 -0.0158 0.0566  97  HIS   A NE2 
740  N N   . LEU   A 92  ? 0.1219 0.1668 0.1679 0.0057  -0.0089 0.0418  98  LEU   A N   
741  C CA  . LEU   A 92  ? 0.1290 0.1693 0.1742 0.0078  -0.0065 0.0363  98  LEU   A CA  
742  C C   . LEU   A 92  ? 0.1248 0.1737 0.1675 0.0042  -0.0082 0.0374  98  LEU   A C   
743  O O   . LEU   A 92  ? 0.1272 0.1871 0.1746 0.0025  -0.0106 0.0443  98  LEU   A O   
744  C CB  . LEU   A 92  ? 0.1413 0.1787 0.1971 0.0137  -0.0030 0.0381  98  LEU   A CB  
745  C CG  . LEU   A 92  ? 0.1724 0.2041 0.2266 0.0155  0.0002  0.0318  98  LEU   A CG  
746  C CD1 . LEU   A 92  ? 0.1788 0.2005 0.2246 0.0147  0.0012  0.0244  98  LEU   A CD1 
747  C CD2 . LEU   A 92  ? 0.2016 0.2313 0.2671 0.0205  0.0049  0.0335  98  LEU   A CD2 
748  N N   . MET   A 93  ? 0.1303 0.1746 0.1661 0.0028  -0.0072 0.0309  99  MET   A N   
749  C CA  . MET   A 93  ? 0.1270 0.1778 0.1598 -0.0010 -0.0080 0.0308  99  MET   A CA  
750  C C   . MET   A 93  ? 0.1336 0.1808 0.1687 0.0023  -0.0053 0.0279  99  MET   A C   
751  O O   . MET   A 93  ? 0.1490 0.1866 0.1812 0.0046  -0.0032 0.0228  99  MET   A O   
752  C CB  . MET   A 93  ? 0.1467 0.1936 0.1685 -0.0062 -0.0083 0.0255  99  MET   A CB  
753  C CG  . MET   A 93  ? 0.1654 0.2152 0.1835 -0.0104 -0.0100 0.0272  99  MET   A CG  
754  S SD  . MET   A 93  ? 0.1941 0.2370 0.2009 -0.0160 -0.0084 0.0200  99  MET   A SD  
755  C CE  . MET   A 93  ? 0.2633 0.2932 0.2713 -0.0096 -0.0061 0.0150  99  MET   A CE  
756  N N   . LEU   A 94  ? 0.1255 0.1811 0.1657 0.0020  -0.0053 0.0311  100 LEU   A N   
757  C CA  . LEU   A 94  ? 0.1415 0.1942 0.1837 0.0045  -0.0022 0.0281  100 LEU   A CA  
758  C C   . LEU   A 94  ? 0.1309 0.1852 0.1659 0.0001  -0.0024 0.0250  100 LEU   A C   
759  O O   . LEU   A 94  ? 0.1472 0.2091 0.1793 -0.0050 -0.0049 0.0271  100 LEU   A O   
760  C CB  . LEU   A 94  ? 0.1627 0.2229 0.2183 0.0084  -0.0003 0.0336  100 LEU   A CB  
761  C CG  . LEU   A 94  ? 0.2142 0.2719 0.2795 0.0137  0.0016  0.0368  100 LEU   A CG  
762  C CD1 . LEU   A 94  ? 0.2300 0.2951 0.3104 0.0178  0.0044  0.0425  100 LEU   A CD1 
763  C CD2 . LEU   A 94  ? 0.2344 0.2784 0.2956 0.0162  0.0053  0.0299  100 LEU   A CD2 
764  N N   . ALA   A 95  ? 0.1333 0.1806 0.1649 0.0012  0.0002  0.0202  101 ALA   A N   
765  C CA  . ALA   A 95  ? 0.1310 0.1786 0.1566 -0.0025 0.0007  0.0175  101 ALA   A CA  
766  C C   . ALA   A 95  ? 0.1275 0.1729 0.1557 0.0001  0.0042  0.0156  101 ALA   A C   
767  O O   . ALA   A 95  ? 0.1355 0.1763 0.1677 0.0042  0.0066  0.0145  101 ALA   A O   
768  C CB  . ALA   A 95  ? 0.1533 0.1916 0.1683 -0.0050 0.0003  0.0128  101 ALA   A CB  
769  N N   . VAL   A 96  ? 0.1251 0.1731 0.1504 -0.0030 0.0050  0.0144  102 VAL   A N   
770  C CA  . VAL   A 96  ? 0.1266 0.1719 0.1520 -0.0018 0.0085  0.0118  102 VAL   A CA  
771  C C   . VAL   A 96  ? 0.1607 0.1949 0.1753 -0.0031 0.0086  0.0071  102 VAL   A C   
772  O O   . VAL   A 96  ? 0.1861 0.2180 0.1938 -0.0065 0.0070  0.0062  102 VAL   A O   
773  C CB  . VAL   A 96  ? 0.1237 0.1774 0.1510 -0.0050 0.0091  0.0132  102 VAL   A CB  
774  C CG1 . VAL   A 96  ? 0.1484 0.1985 0.1739 -0.0048 0.0131  0.0098  102 VAL   A CG1 
775  C CG2 . VAL   A 96  ? 0.1208 0.1873 0.1607 -0.0034 0.0085  0.0193  102 VAL   A CG2 
776  N N   . GLY   A 97  ? 0.1631 0.1912 0.1771 -0.0007 0.0107  0.0046  103 GLY   A N   
777  C CA  . GLY   A 97  ? 0.1808 0.2001 0.1854 -0.0020 0.0103  0.0014  103 GLY   A CA  
778  C C   . GLY   A 97  ? 0.1844 0.1991 0.1889 -0.0002 0.0127  -0.0012 103 GLY   A C   
779  O O   . GLY   A 97  ? 0.1997 0.2157 0.2113 0.0026  0.0150  -0.0010 103 GLY   A O   
780  N N   . HIS   A 98  ? 0.2015 0.2105 0.1975 -0.0024 0.0125  -0.0035 104 HIS   A N   
781  C CA  . HIS   A 98  ? 0.2184 0.2232 0.2120 -0.0025 0.0147  -0.0066 104 HIS   A CA  
782  C C   . HIS   A 98  ? 0.2099 0.2112 0.2039 -0.0009 0.0127  -0.0068 104 HIS   A C   
783  O O   . HIS   A 98  ? 0.2013 0.2014 0.1931 -0.0009 0.0087  -0.0051 104 HIS   A O   
784  C CB  . HIS   A 98  ? 0.2314 0.2331 0.2151 -0.0065 0.0146  -0.0080 104 HIS   A CB  
785  C CG  . HIS   A 98  ? 0.2483 0.2466 0.2278 -0.0084 0.0172  -0.0117 104 HIS   A CG  
786  N ND1 . HIS   A 98  ? 0.2601 0.2589 0.2425 -0.0087 0.0231  -0.0151 104 HIS   A ND1 
787  C CD2 . HIS   A 98  ? 0.2556 0.2506 0.2288 -0.0105 0.0150  -0.0126 104 HIS   A CD2 
788  C CE1 . HIS   A 98  ? 0.2588 0.2536 0.2352 -0.0116 0.0248  -0.0187 104 HIS   A CE1 
789  N NE2 . HIS   A 98  ? 0.2591 0.2522 0.2295 -0.0131 0.0195  -0.0171 104 HIS   A NE2 
790  N N   . SER   A 99  ? 0.2158 0.2151 0.2130 0.0002  0.0158  -0.0091 105 SER   A N   
791  C CA  A SER   A 99  ? 0.2150 0.2108 0.2119 0.0008  0.0145  -0.0100 105 SER   A CA  
792  C CA  B SER   A 99  ? 0.2199 0.2157 0.2175 0.0011  0.0146  -0.0099 105 SER   A CA  
793  C C   . SER   A 99  ? 0.2468 0.2386 0.2431 -0.0004 0.0196  -0.0145 105 SER   A C   
794  O O   . SER   A 99  ? 0.2842 0.2766 0.2850 0.0002  0.0251  -0.0163 105 SER   A O   
795  C CB  A SER   A 99  ? 0.1996 0.1974 0.2042 0.0043  0.0129  -0.0069 105 SER   A CB  
796  C CB  B SER   A 99  ? 0.2153 0.2135 0.2216 0.0049  0.0136  -0.0068 105 SER   A CB  
797  O OG  A SER   A 99  ? 0.1801 0.1807 0.1936 0.0069  0.0168  -0.0060 105 SER   A OG  
798  O OG  B SER   A 99  ? 0.2155 0.2106 0.2230 0.0059  0.0123  -0.0070 105 SER   A OG  
799  N N   . GLU   A 100 ? 0.2071 0.1955 0.1974 -0.0031 0.0182  -0.0167 106 GLU   A N   
800  C CA  . GLU   A 100 ? 0.2049 0.1888 0.1924 -0.0060 0.0226  -0.0218 106 GLU   A CA  
801  C C   . GLU   A 100 ? 0.2161 0.1978 0.2061 -0.0047 0.0206  -0.0214 106 GLU   A C   
802  O O   . GLU   A 100 ? 0.1971 0.1811 0.1887 -0.0026 0.0153  -0.0175 106 GLU   A O   
803  C CB  . GLU   A 100 ? 0.2268 0.2101 0.2022 -0.0123 0.0216  -0.0243 106 GLU   A CB  
804  C CG  . GLU   A 100 ? 0.2451 0.2302 0.2178 -0.0139 0.0242  -0.0248 106 GLU   A CG  
805  C CD  . GLU   A 100 ? 0.2959 0.2813 0.2563 -0.0207 0.0235  -0.0266 106 GLU   A CD  
806  O OE1 . GLU   A 100 ? 0.3549 0.3386 0.3081 -0.0257 0.0237  -0.0296 106 GLU   A OE1 
807  O OE2 . GLU   A 100 ? 0.2778 0.2657 0.2354 -0.0215 0.0227  -0.0246 106 GLU   A OE2 
808  N N   . PRO   A 101 ? 0.2207 0.1976 0.2119 -0.0060 0.0254  -0.0255 107 PRO   A N   
809  C CA  . PRO   A 101 ? 0.2268 0.2016 0.2214 -0.0047 0.0238  -0.0250 107 PRO   A CA  
810  C C   . PRO   A 101 ? 0.2238 0.2011 0.2127 -0.0067 0.0167  -0.0229 107 PRO   A C   
811  O O   . PRO   A 101 ? 0.2267 0.2053 0.2203 -0.0036 0.0133  -0.0195 107 PRO   A O   
812  C CB  . PRO   A 101 ? 0.2532 0.2215 0.2471 -0.0078 0.0311  -0.0312 107 PRO   A CB  
813  C CG  . PRO   A 101 ? 0.2669 0.2342 0.2645 -0.0067 0.0377  -0.0331 107 PRO   A CG  
814  C CD  . PRO   A 101 ? 0.2335 0.2062 0.2245 -0.0083 0.0336  -0.0312 107 PRO   A CD  
815  N N   . GLY   A 102 ? 0.2065 0.1854 0.1860 -0.0118 0.0142  -0.0241 108 GLY   A N   
816  C CA  . GLY   A 102 ? 0.1913 0.1738 0.1671 -0.0136 0.0076  -0.0210 108 GLY   A CA  
817  C C   . GLY   A 102 ? 0.1736 0.1596 0.1527 -0.0096 0.0029  -0.0154 108 GLY   A C   
818  O O   . GLY   A 102 ? 0.1801 0.1686 0.1587 -0.0099 -0.0019 -0.0124 108 GLY   A O   
819  N N   . ASP   A 103 ? 0.1641 0.1503 0.1467 -0.0064 0.0046  -0.0141 109 ASP   A N   
820  C CA  . ASP   A 103 ? 0.1573 0.1459 0.1430 -0.0033 0.0013  -0.0098 109 ASP   A CA  
821  C C   . ASP   A 103 ? 0.1508 0.1394 0.1430 0.0000  0.0002  -0.0082 109 ASP   A C   
822  O O   . ASP   A 103 ? 0.1471 0.1372 0.1412 0.0015  -0.0023 -0.0054 109 ASP   A O   
823  C CB  . ASP   A 103 ? 0.1520 0.1418 0.1388 -0.0020 0.0034  -0.0091 109 ASP   A CB  
824  C CG  . ASP   A 103 ? 0.1647 0.1548 0.1443 -0.0055 0.0035  -0.0096 109 ASP   A CG  
825  O OD1 . ASP   A 103 ? 0.1726 0.1632 0.1474 -0.0078 0.0000  -0.0079 109 ASP   A OD1 
826  O OD2 . ASP   A 103 ? 0.1675 0.1579 0.1468 -0.0060 0.0072  -0.0113 109 ASP   A OD2 
827  N N   . CYS   A 104 ? 0.1513 0.1378 0.1469 0.0007  0.0026  -0.0101 110 CYS   A N   
828  C CA  . CYS   A 104 ? 0.1506 0.1375 0.1518 0.0032  0.0014  -0.0082 110 CYS   A CA  
829  C C   . CYS   A 104 ? 0.1452 0.1334 0.1453 0.0025  -0.0026 -0.0067 110 CYS   A C   
830  O O   . CYS   A 104 ? 0.1613 0.1499 0.1578 -0.0001 -0.0044 -0.0074 110 CYS   A O   
831  C CB  . CYS   A 104 ? 0.1657 0.1493 0.1701 0.0034  0.0047  -0.0103 110 CYS   A CB  
832  S SG  . CYS   A 104 ? 0.1764 0.1589 0.1875 0.0064  0.0100  -0.0099 110 CYS   A SG  
833  N N   . GLY   A 105 ? 0.1326 0.1222 0.1362 0.0045  -0.0038 -0.0043 111 GLY   A N   
834  C CA  . GLY   A 105 ? 0.1390 0.1295 0.1434 0.0044  -0.0064 -0.0029 111 GLY   A CA  
835  C C   . GLY   A 105 ? 0.1357 0.1270 0.1394 0.0047  -0.0074 -0.0010 111 GLY   A C   
836  O O   . GLY   A 105 ? 0.1483 0.1399 0.1548 0.0053  -0.0083 0.0003  111 GLY   A O   
837  N N   . GLY   A 106 ? 0.1325 0.1237 0.1330 0.0042  -0.0067 -0.0009 112 GLY   A N   
838  C CA  . GLY   A 106 ? 0.1297 0.1207 0.1296 0.0041  -0.0069 0.0008  112 GLY   A CA  
839  C C   . GLY   A 106 ? 0.1191 0.1102 0.1216 0.0047  -0.0056 0.0009  112 GLY   A C   
840  O O   . GLY   A 106 ? 0.1275 0.1202 0.1310 0.0048  -0.0045 0.0004  112 GLY   A O   
841  N N   . ILE   A 107 ? 0.1227 0.1121 0.1264 0.0047  -0.0052 0.0018  113 ILE   A N   
842  C CA  . ILE   A 107 ? 0.1151 0.1043 0.1201 0.0038  -0.0031 0.0010  113 ILE   A CA  
843  C C   . ILE   A 107 ? 0.1086 0.0986 0.1105 0.0018  -0.0017 0.0006  113 ILE   A C   
844  O O   . ILE   A 107 ? 0.1217 0.1100 0.1214 0.0013  -0.0014 0.0011  113 ILE   A O   
845  C CB  . ILE   A 107 ? 0.1254 0.1117 0.1339 0.0043  -0.0019 0.0013  113 ILE   A CB  
846  C CG1 . ILE   A 107 ? 0.1430 0.1305 0.1557 0.0056  -0.0030 0.0014  113 ILE   A CG1 
847  C CG2 . ILE   A 107 ? 0.1357 0.1201 0.1439 0.0021  0.0017  -0.0004 113 ILE   A CG2 
848  C CD1 . ILE   A 107 ? 0.1822 0.1678 0.2007 0.0069  -0.0018 0.0024  113 ILE   A CD1 
849  N N   . LEU   A 108 ? 0.1125 0.1055 0.1141 0.0001  -0.0008 0.0000  114 LEU   A N   
850  C CA  . LEU   A 108 ? 0.1148 0.1097 0.1136 -0.0032 0.0006  -0.0004 114 LEU   A CA  
851  C C   . LEU   A 108 ? 0.1242 0.1165 0.1224 -0.0060 0.0033  -0.0023 114 LEU   A C   
852  O O   . LEU   A 108 ? 0.1266 0.1194 0.1264 -0.0061 0.0035  -0.0028 114 LEU   A O   
853  C CB  . LEU   A 108 ? 0.1180 0.1196 0.1175 -0.0040 -0.0005 0.0012  114 LEU   A CB  
854  C CG  . LEU   A 108 ? 0.1323 0.1387 0.1291 -0.0087 0.0003  0.0013  114 LEU   A CG  
855  C CD1 . LEU   A 108 ? 0.1509 0.1571 0.1457 -0.0096 0.0010  0.0011  114 LEU   A CD1 
856  C CD2 . LEU   A 108 ? 0.1446 0.1592 0.1440 -0.0092 -0.0015 0.0046  114 LEU   A CD2 
857  N N   . ARG   A 109 ? 0.1240 0.1133 0.1199 -0.0086 0.0059  -0.0037 115 ARG   A N   
858  C CA  . ARG   A 109 ? 0.1289 0.1142 0.1242 -0.0119 0.0100  -0.0065 115 ARG   A CA  
859  C C   . ARG   A 109 ? 0.1400 0.1256 0.1302 -0.0175 0.0128  -0.0086 115 ARG   A C   
860  O O   . ARG   A 109 ? 0.1404 0.1277 0.1286 -0.0182 0.0118  -0.0076 115 ARG   A O   
861  C CB  . ARG   A 109 ? 0.1473 0.1253 0.1474 -0.0086 0.0122  -0.0065 115 ARG   A CB  
862  C CG  . ARG   A 109 ? 0.1583 0.1324 0.1579 -0.0078 0.0128  -0.0051 115 ARG   A CG  
863  C CD  . ARG   A 109 ? 0.1776 0.1456 0.1837 -0.0043 0.0145  -0.0034 115 ARG   A CD  
864  N NE  . ARG   A 109 ? 0.1831 0.1541 0.1929 0.0001  0.0101  -0.0001 115 ARG   A NE  
865  C CZ  . ARG   A 109 ? 0.1826 0.1533 0.1987 0.0027  0.0101  0.0008  115 ARG   A CZ  
866  N NH1 . ARG   A 109 ? 0.1929 0.1605 0.2125 0.0016  0.0148  -0.0018 115 ARG   A NH1 
867  N NH2 . ARG   A 109 ? 0.1906 0.1648 0.2094 0.0056  0.0057  0.0039  115 ARG   A NH2 
868  N N   . CYS   A 110 ? 0.1698 0.1534 0.1579 -0.0224 0.0169  -0.0120 116 CYS   A N   
869  C CA  . CYS   A 110 ? 0.2079 0.1905 0.1903 -0.0295 0.0208  -0.0152 116 CYS   A CA  
870  C C   . CYS   A 110 ? 0.2512 0.2235 0.2352 -0.0309 0.0279  -0.0194 116 CYS   A C   
871  O O   . CYS   A 110 ? 0.2476 0.2151 0.2382 -0.0256 0.0288  -0.0186 116 CYS   A O   
872  C CB  . CYS   A 110 ? 0.2041 0.1957 0.1812 -0.0358 0.0193  -0.0155 116 CYS   A CB  
873  S SG  . CYS   A 110 ? 0.2111 0.2028 0.1875 -0.0385 0.0216  -0.0179 116 CYS   A SG  
874  N N   . GLN   A 111 ? 0.2958 0.2646 0.2744 -0.0384 0.0335  -0.0239 117 GLN   A N   
875  C CA  . GLN   A 111 ? 0.3294 0.2873 0.3105 -0.0399 0.0418  -0.0285 117 GLN   A CA  
876  C C   . GLN   A 111 ? 0.3254 0.2829 0.3088 -0.0401 0.0443  -0.0308 117 GLN   A C   
877  O O   . GLN   A 111 ? 0.3602 0.3088 0.3497 -0.0383 0.0507  -0.0332 117 GLN   A O   
878  C CB  . GLN   A 111 ? 0.3643 0.3182 0.3381 -0.0495 0.0485  -0.0342 117 GLN   A CB  
879  C CG  . GLN   A 111 ? 0.4285 0.3913 0.3928 -0.0590 0.0478  -0.0371 117 GLN   A CG  
880  C CD  . GLN   A 111 ? 0.4958 0.4683 0.4545 -0.0626 0.0424  -0.0344 117 GLN   A CD  
881  O OE1 . GLN   A 111 ? 0.5077 0.4840 0.4703 -0.0562 0.0365  -0.0291 117 GLN   A OE1 
882  N NE2 . GLN   A 111 ? 0.5044 0.4817 0.4540 -0.0736 0.0445  -0.0381 117 GLN   A NE2 
883  N N   . HIS   A 112 ? 0.2809 0.2479 0.2606 -0.0420 0.0396  -0.0295 118 HIS   A N   
884  C CA  . HIS   A 112 ? 0.2599 0.2272 0.2407 -0.0430 0.0417  -0.0316 118 HIS   A CA  
885  C C   . HIS   A 112 ? 0.2531 0.2204 0.2430 -0.0341 0.0383  -0.0278 118 HIS   A C   
886  O O   . HIS   A 112 ? 0.2814 0.2473 0.2744 -0.0338 0.0411  -0.0295 118 HIS   A O   
887  C CB  . HIS   A 112 ? 0.2569 0.2344 0.2291 -0.0504 0.0387  -0.0317 118 HIS   A CB  
888  C CG  . HIS   A 112 ? 0.2764 0.2560 0.2390 -0.0606 0.0416  -0.0353 118 HIS   A CG  
889  N ND1 . HIS   A 112 ? 0.3031 0.2915 0.2615 -0.0628 0.0359  -0.0316 118 HIS   A ND1 
890  C CD2 . HIS   A 112 ? 0.3096 0.2834 0.2664 -0.0694 0.0500  -0.0424 118 HIS   A CD2 
891  C CE1 . HIS   A 112 ? 0.3308 0.3195 0.2809 -0.0730 0.0402  -0.0362 118 HIS   A CE1 
892  N NE2 . HIS   A 112 ? 0.3332 0.3128 0.2812 -0.0777 0.0489  -0.0431 118 HIS   A NE2 
893  N N   . GLY   A 113 ? 0.2252 0.1947 0.2189 -0.0274 0.0323  -0.0226 119 GLY   A N   
894  C CA  . GLY   A 113 ? 0.2080 0.1783 0.2091 -0.0201 0.0286  -0.0191 119 GLY   A CA  
895  C C   . GLY   A 113 ? 0.1696 0.1469 0.1696 -0.0168 0.0210  -0.0145 119 GLY   A C   
896  O O   . GLY   A 113 ? 0.1701 0.1507 0.1659 -0.0183 0.0186  -0.0133 119 GLY   A O   
897  N N   . VAL   A 114 ? 0.1541 0.1337 0.1584 -0.0127 0.0178  -0.0123 120 VAL   A N   
898  C CA  . VAL   A 114 ? 0.1504 0.1352 0.1546 -0.0095 0.0119  -0.0087 120 VAL   A CA  
899  C C   . VAL   A 114 ? 0.1354 0.1268 0.1350 -0.0129 0.0097  -0.0078 120 VAL   A C   
900  O O   . VAL   A 114 ? 0.1430 0.1362 0.1412 -0.0161 0.0110  -0.0089 120 VAL   A O   
901  C CB  . VAL   A 114 ? 0.1510 0.1356 0.1612 -0.0047 0.0097  -0.0070 120 VAL   A CB  
902  C CG1 . VAL   A 114 ? 0.1640 0.1528 0.1736 -0.0024 0.0049  -0.0043 120 VAL   A CG1 
903  C CG2 . VAL   A 114 ? 0.1713 0.1515 0.1871 -0.0012 0.0106  -0.0060 120 VAL   A CG2 
904  N N   . VAL   A 115 ? 0.1278 0.1233 0.1257 -0.0125 0.0066  -0.0054 121 VAL   A N   
905  C CA  . VAL   A 115 ? 0.1349 0.1379 0.1304 -0.0151 0.0043  -0.0029 121 VAL   A CA  
906  C C   . VAL   A 115 ? 0.1296 0.1351 0.1294 -0.0107 0.0010  0.0004  121 VAL   A C   
907  O O   . VAL   A 115 ? 0.1382 0.1484 0.1383 -0.0119 -0.0004 0.0029  121 VAL   A O   
908  C CB  . VAL   A 115 ? 0.1515 0.1582 0.1443 -0.0173 0.0036  -0.0020 121 VAL   A CB  
909  C CG1 . VAL   A 115 ? 0.1760 0.1923 0.1691 -0.0190 0.0005  0.0023  121 VAL   A CG1 
910  C CG2 . VAL   A 115 ? 0.1689 0.1729 0.1569 -0.0230 0.0075  -0.0057 121 VAL   A CG2 
911  N N   . GLY   A 116 ? 0.1277 0.1300 0.1304 -0.0060 -0.0001 0.0006  122 GLY   A N   
912  C CA  . GLY   A 116 ? 0.1318 0.1350 0.1381 -0.0023 -0.0021 0.0027  122 GLY   A CA  
913  C C   . GLY   A 116 ? 0.1210 0.1205 0.1285 0.0010  -0.0026 0.0019  122 GLY   A C   
914  O O   . GLY   A 116 ? 0.1244 0.1207 0.1305 0.0010  -0.0019 0.0005  122 GLY   A O   
915  N N   . ILE   A 117 ? 0.1115 0.1112 0.1213 0.0034  -0.0034 0.0029  123 ILE   A N   
916  C CA  . ILE   A 117 ? 0.1165 0.1132 0.1260 0.0052  -0.0037 0.0016  123 ILE   A CA  
917  C C   . ILE   A 117 ? 0.1175 0.1156 0.1281 0.0063  -0.0030 0.0023  123 ILE   A C   
918  O O   . ILE   A 117 ? 0.1313 0.1321 0.1455 0.0070  -0.0024 0.0044  123 ILE   A O   
919  C CB  . ILE   A 117 ? 0.1338 0.1280 0.1448 0.0061  -0.0044 0.0006  123 ILE   A CB  
920  C CG1 . ILE   A 117 ? 0.1515 0.1462 0.1654 0.0066  -0.0039 0.0014  123 ILE   A CG1 
921  C CG2 . ILE   A 117 ? 0.1563 0.1493 0.1676 0.0056  -0.0048 0.0000  123 ILE   A CG2 
922  C CD1 . ILE   A 117 ? 0.1701 0.1622 0.1851 0.0068  -0.0042 -0.0002 123 ILE   A CD1 
923  N N   . VAL   A 118 ? 0.1170 0.1134 0.1253 0.0065  -0.0026 0.0009  124 VAL   A N   
924  C CA  . VAL   A 118 ? 0.1114 0.1084 0.1211 0.0074  -0.0007 0.0007  124 VAL   A CA  
925  C C   . VAL   A 118 ? 0.1243 0.1192 0.1378 0.0088  0.0008  0.0002  124 VAL   A C   
926  O O   . VAL   A 118 ? 0.1261 0.1180 0.1381 0.0082  0.0001  -0.0015 124 VAL   A O   
927  C CB  . VAL   A 118 ? 0.1203 0.1152 0.1255 0.0062  -0.0002 -0.0014 124 VAL   A CB  
928  C CG1 . VAL   A 118 ? 0.1477 0.1424 0.1544 0.0067  0.0030  -0.0028 124 VAL   A CG1 
929  C CG2 . VAL   A 118 ? 0.1247 0.1207 0.1265 0.0049  -0.0011 -0.0006 124 VAL   A CG2 
930  N N   . SER   A 119 ? 0.1212 0.1180 0.1403 0.0105  0.0030  0.0021  125 SER   A N   
931  C CA  . SER   A 119 ? 0.1281 0.1220 0.1523 0.0122  0.0054  0.0022  125 SER   A CA  
932  C C   . SER   A 119 ? 0.1519 0.1449 0.1811 0.0140  0.0099  0.0018  125 SER   A C   
933  O O   . SER   A 119 ? 0.1797 0.1676 0.2114 0.0145  0.0134  -0.0003 125 SER   A O   
934  C CB  . SER   A 119 ? 0.1425 0.1394 0.1712 0.0131  0.0040  0.0066  125 SER   A CB  
935  O OG  . SER   A 119 ? 0.1568 0.1507 0.1916 0.0150  0.0066  0.0077  125 SER   A OG  
936  N N   . THR   A 120 ? 0.1444 0.1422 0.1759 0.0146  0.0105  0.0037  126 THR   A N   
937  C CA  . THR   A 120 ? 0.1609 0.1581 0.1991 0.0167  0.0157  0.0034  126 THR   A CA  
938  C C   . THR   A 120 ? 0.1875 0.1869 0.2218 0.0151  0.0165  0.0014  126 THR   A C   
939  O O   . THR   A 120 ? 0.1671 0.1689 0.1946 0.0128  0.0127  0.0014  126 THR   A O   
940  C CB  . THR   A 120 ? 0.1774 0.1804 0.2273 0.0201  0.0162  0.0101  126 THR   A CB  
941  O OG1 . THR   A 120 ? 0.1890 0.2008 0.2391 0.0192  0.0128  0.0140  126 THR   A OG1 
942  C CG2 . THR   A 120 ? 0.1780 0.1796 0.2312 0.0212  0.0149  0.0133  126 THR   A CG2 
943  N N   . GLY   A 121 ? 0.2158 0.2142 0.2550 0.0163  0.0219  -0.0002 127 GLY   A N   
944  C CA  . GLY   A 121 ? 0.2470 0.2480 0.2831 0.0147  0.0232  -0.0019 127 GLY   A CA  
945  C C   . GLY   A 121 ? 0.2550 0.2548 0.2981 0.0161  0.0304  -0.0039 127 GLY   A C   
946  O O   . GLY   A 121 ? 0.2675 0.2638 0.3189 0.0188  0.0351  -0.0039 127 GLY   A O   
947  N N   . GLY   A 122 ? 0.2571 0.2593 0.2966 0.0141  0.0317  -0.0057 128 GLY   A N   
948  C CA  . GLY   A 122 ? 0.2496 0.2510 0.2945 0.0146  0.0392  -0.0085 128 GLY   A CA  
949  C C   . GLY   A 122 ? 0.2589 0.2694 0.3095 0.0155  0.0390  -0.0049 128 GLY   A C   
950  O O   . GLY   A 122 ? 0.2546 0.2729 0.3103 0.0171  0.0342  0.0013  128 GLY   A O   
951  N N   . ASN   A 123 ? 0.2547 0.2646 0.3039 0.0136  0.0444  -0.0089 129 ASN   A N   
952  C CA  . ASN   A 123 ? 0.2644 0.2828 0.3202 0.0141  0.0459  -0.0062 129 ASN   A CA  
953  C C   . ASN   A 123 ? 0.2480 0.2740 0.2995 0.0123  0.0385  -0.0020 129 ASN   A C   
954  O O   . ASN   A 123 ? 0.2449 0.2806 0.3056 0.0136  0.0380  0.0029  129 ASN   A O   
955  C CB  . ASN   A 123 ? 0.2841 0.3074 0.3588 0.0197  0.0505  -0.0017 129 ASN   A CB  
956  C CG  . ASN   A 123 ? 0.3375 0.3525 0.4175 0.0211  0.0603  -0.0070 129 ASN   A CG  
957  O OD1 . ASN   A 123 ? 0.3706 0.3814 0.4446 0.0177  0.0661  -0.0136 129 ASN   A OD1 
958  N ND2 . ASN   A 123 ? 0.3451 0.3572 0.4362 0.0256  0.0628  -0.0043 129 ASN   A ND2 
959  N N   . GLY   A 124 ? 0.2170 0.2387 0.2545 0.0085  0.0338  -0.0042 130 GLY   A N   
960  C CA  . GLY   A 124 ? 0.2019 0.2284 0.2341 0.0060  0.0281  -0.0014 130 GLY   A CA  
961  C C   . GLY   A 124 ? 0.1600 0.1906 0.1958 0.0075  0.0229  0.0035  130 GLY   A C   
962  O O   . GLY   A 124 ? 0.1858 0.2205 0.2178 0.0049  0.0190  0.0055  130 GLY   A O   
963  N N   . LEU   A 125 ? 0.1555 0.1835 0.1965 0.0108  0.0229  0.0048  131 LEU   A N   
964  C CA  . LEU   A 125 ? 0.1532 0.1843 0.1954 0.0112  0.0178  0.0090  131 LEU   A CA  
965  C C   . LEU   A 125 ? 0.1683 0.1906 0.2022 0.0106  0.0156  0.0060  131 LEU   A C   
966  O O   . LEU   A 125 ? 0.1960 0.2110 0.2270 0.0109  0.0186  0.0018  131 LEU   A O   
967  C CB  . LEU   A 125 ? 0.1558 0.1926 0.2117 0.0153  0.0187  0.0146  131 LEU   A CB  
968  C CG  . LEU   A 125 ? 0.1583 0.2062 0.2253 0.0164  0.0202  0.0194  131 LEU   A CG  
969  C CD1 . LEU   A 125 ? 0.1810 0.2330 0.2641 0.0216  0.0228  0.0251  131 LEU   A CD1 
970  C CD2 . LEU   A 125 ? 0.1701 0.2276 0.2338 0.0123  0.0146  0.0231  131 LEU   A CD2 
971  N N   . VAL   A 126 ? 0.1311 0.1547 0.1613 0.0092  0.0110  0.0079  132 VAL   A N   
972  C CA  . VAL   A 126 ? 0.1374 0.1543 0.1621 0.0090  0.0090  0.0060  132 VAL   A CA  
973  C C   . VAL   A 126 ? 0.1281 0.1493 0.1572 0.0097  0.0062  0.0103  132 VAL   A C   
974  O O   . VAL   A 126 ? 0.1394 0.1677 0.1694 0.0078  0.0041  0.0135  132 VAL   A O   
975  C CB  . VAL   A 126 ? 0.1390 0.1517 0.1534 0.0059  0.0068  0.0032  132 VAL   A CB  
976  C CG1 . VAL   A 126 ? 0.1464 0.1638 0.1586 0.0032  0.0048  0.0050  132 VAL   A CG1 
977  C CG2 . VAL   A 126 ? 0.1473 0.1546 0.1581 0.0060  0.0047  0.0020  132 VAL   A CG2 
978  N N   . GLY   A 127 ? 0.1258 0.1429 0.1567 0.0115  0.0063  0.0102  133 GLY   A N   
979  C CA  . GLY   A 127 ? 0.1254 0.1460 0.1595 0.0117  0.0038  0.0143  133 GLY   A CA  
980  C C   . GLY   A 127 ? 0.1355 0.1506 0.1628 0.0101  0.0017  0.0117  133 GLY   A C   
981  O O   . GLY   A 127 ? 0.1483 0.1567 0.1721 0.0105  0.0027  0.0078  133 GLY   A O   
982  N N   . PHE   A 128 ? 0.1105 0.1293 0.1359 0.0078  -0.0009 0.0138  134 PHE   A N   
983  C CA  . PHE   A 128 ? 0.1206 0.1351 0.1407 0.0062  -0.0022 0.0114  134 PHE   A CA  
984  C C   . PHE   A 128 ? 0.1263 0.1429 0.1492 0.0060  -0.0033 0.0145  134 PHE   A C   
985  O O   . PHE   A 128 ? 0.1313 0.1552 0.1568 0.0046  -0.0046 0.0191  134 PHE   A O   
986  C CB  . PHE   A 128 ? 0.1286 0.1444 0.1426 0.0023  -0.0032 0.0101  134 PHE   A CB  
987  C CG  . PHE   A 128 ? 0.1270 0.1415 0.1380 0.0018  -0.0022 0.0080  134 PHE   A CG  
988  C CD1 . PHE   A 128 ? 0.1244 0.1324 0.1320 0.0026  -0.0017 0.0049  134 PHE   A CD1 
989  C CD2 . PHE   A 128 ? 0.1386 0.1592 0.1506 0.0001  -0.0021 0.0098  134 PHE   A CD2 
990  C CE1 . PHE   A 128 ? 0.1245 0.1314 0.1290 0.0017  -0.0010 0.0037  134 PHE   A CE1 
991  C CE2 . PHE   A 128 ? 0.1388 0.1580 0.1477 -0.0008 -0.0010 0.0079  134 PHE   A CE2 
992  C CZ  . PHE   A 128 ? 0.1337 0.1457 0.1387 0.0001  -0.0004 0.0049  134 PHE   A CZ  
993  N N   . ALA   A 129 ? 0.1176 0.1286 0.1395 0.0068  -0.0030 0.0124  135 ALA   A N   
994  C CA  . ALA   A 129 ? 0.1213 0.1335 0.1447 0.0060  -0.0039 0.0148  135 ALA   A CA  
995  C C   . ALA   A 129 ? 0.1253 0.1392 0.1430 0.0019  -0.0050 0.0136  135 ALA   A C   
996  O O   . ALA   A 129 ? 0.1348 0.1442 0.1490 0.0013  -0.0043 0.0096  135 ALA   A O   
997  C CB  . ALA   A 129 ? 0.1314 0.1371 0.1560 0.0079  -0.0028 0.0125  135 ALA   A CB  
998  N N   . ASP   A 130 ? 0.1255 0.1462 0.1426 -0.0014 -0.0062 0.0173  136 ASP   A N   
999  C CA  . ASP   A 130 ? 0.1347 0.1568 0.1456 -0.0067 -0.0061 0.0154  136 ASP   A CA  
1000 C C   . ASP   A 130 ? 0.1332 0.1510 0.1431 -0.0071 -0.0052 0.0133  136 ASP   A C   
1001 O O   . ASP   A 130 ? 0.1514 0.1687 0.1649 -0.0052 -0.0057 0.0159  136 ASP   A O   
1002 C CB  . ASP   A 130 ? 0.1531 0.1851 0.1631 -0.0113 -0.0080 0.0204  136 ASP   A CB  
1003 C CG  . ASP   A 130 ? 0.2409 0.2748 0.2430 -0.0184 -0.0071 0.0178  136 ASP   A CG  
1004 O OD1 . ASP   A 130 ? 0.2144 0.2443 0.2126 -0.0201 -0.0050 0.0128  136 ASP   A OD1 
1005 O OD2 . ASP   A 130 ? 0.3291 0.3681 0.3291 -0.0227 -0.0082 0.0207  136 ASP   A OD2 
1006 N N   . VAL   A 131 ? 0.1230 0.1377 0.1285 -0.0101 -0.0033 0.0089  137 VAL   A N   
1007 C CA  . VAL   A 131 ? 0.1276 0.1393 0.1325 -0.0113 -0.0018 0.0068  137 VAL   A CA  
1008 C C   . VAL   A 131 ? 0.1341 0.1481 0.1332 -0.0180 0.0003  0.0048  137 VAL   A C   
1009 O O   . VAL   A 131 ? 0.1373 0.1490 0.1356 -0.0197 0.0025  0.0025  137 VAL   A O   
1010 C CB  . VAL   A 131 ? 0.1300 0.1349 0.1374 -0.0078 -0.0003 0.0029  137 VAL   A CB  
1011 C CG1 . VAL   A 131 ? 0.1366 0.1394 0.1481 -0.0028 -0.0021 0.0041  137 VAL   A CG1 
1012 C CG2 . VAL   A 131 ? 0.1452 0.1470 0.1508 -0.0085 0.0018  -0.0004 137 VAL   A CG2 
1013 N N   . ARG   A 132 ? 0.1369 0.1556 0.1316 -0.0224 0.0002  0.0053  138 ARG   A N   
1014 C CA  . ARG   A 132 ? 0.1401 0.1601 0.1278 -0.0302 0.0031  0.0021  138 ARG   A CA  
1015 C C   . ARG   A 132 ? 0.1582 0.1834 0.1426 -0.0353 0.0026  0.0044  138 ARG   A C   
1016 O O   . ARG   A 132 ? 0.1728 0.1975 0.1511 -0.0421 0.0063  0.0004  138 ARG   A O   
1017 C CB  . ARG   A 132 ? 0.1465 0.1708 0.1298 -0.0347 0.0030  0.0020  138 ARG   A CB  
1018 C CG  . ARG   A 132 ? 0.1503 0.1681 0.1356 -0.0309 0.0047  -0.0013 138 ARG   A CG  
1019 C CD  . ARG   A 132 ? 0.1608 0.1834 0.1415 -0.0360 0.0045  -0.0012 138 ARG   A CD  
1020 N NE  . ARG   A 132 ? 0.1672 0.1985 0.1511 -0.0340 -0.0004 0.0052  138 ARG   A NE  
1021 C CZ  . ARG   A 132 ? 0.1964 0.2340 0.1791 -0.0368 -0.0017 0.0070  138 ARG   A CZ  
1022 N NH1 . ARG   A 132 ? 0.2054 0.2416 0.1817 -0.0430 0.0012  0.0027  138 ARG   A NH1 
1023 N NH2 . ARG   A 132 ? 0.2060 0.2514 0.1942 -0.0338 -0.0057 0.0133  138 ARG   A NH2 
1024 N N   . ASP   A 133 ? 0.1535 0.1837 0.1416 -0.0329 -0.0014 0.0110  139 ASP   A N   
1025 C CA  . ASP   A 133 ? 0.1608 0.1962 0.1457 -0.0379 -0.0022 0.0143  139 ASP   A CA  
1026 C C   . ASP   A 133 ? 0.1645 0.1937 0.1515 -0.0358 0.0001  0.0118  139 ASP   A C   
1027 O O   . ASP   A 133 ? 0.1880 0.2204 0.1717 -0.0404 0.0001  0.0137  139 ASP   A O   
1028 C CB  . ASP   A 133 ? 0.1791 0.2229 0.1685 -0.0362 -0.0073 0.0237  139 ASP   A CB  
1029 C CG  . ASP   A 133 ? 0.2073 0.2459 0.2061 -0.0270 -0.0083 0.0260  139 ASP   A CG  
1030 O OD1 . ASP   A 133 ? 0.2035 0.2358 0.2053 -0.0218 -0.0070 0.0220  139 ASP   A OD1 
1031 O OD2 . ASP   A 133 ? 0.2410 0.2818 0.2440 -0.0253 -0.0101 0.0320  139 ASP   A OD2 
1032 N N   . LEU   A 134 ? 0.1474 0.1686 0.1400 -0.0292 0.0016  0.0081  140 LEU   A N   
1033 C CA  . LEU   A 134 ? 0.1458 0.1622 0.1416 -0.0269 0.0033  0.0062  140 LEU   A CA  
1034 C C   . LEU   A 134 ? 0.1567 0.1696 0.1497 -0.0308 0.0084  -0.0003 140 LEU   A C   
1035 O O   . LEU   A 134 ? 0.1667 0.1740 0.1636 -0.0273 0.0110  -0.0045 140 LEU   A O   
1036 C CB  . LEU   A 134 ? 0.1547 0.1659 0.1578 -0.0191 0.0021  0.0058  140 LEU   A CB  
1037 C CG  . LEU   A 134 ? 0.1620 0.1752 0.1688 -0.0150 -0.0014 0.0112  140 LEU   A CG  
1038 C CD1 . LEU   A 134 ? 0.1628 0.1704 0.1746 -0.0090 -0.0016 0.0092  140 LEU   A CD1 
1039 C CD2 . LEU   A 134 ? 0.1884 0.2044 0.1966 -0.0158 -0.0029 0.0166  140 LEU   A CD2 
1040 N N   . LEU   A 135 ? 0.1524 0.1691 0.1384 -0.0386 0.0104  -0.0009 141 LEU   A N   
1041 C CA  . LEU   A 135 ? 0.1617 0.1749 0.1443 -0.0436 0.0168  -0.0079 141 LEU   A CA  
1042 C C   . LEU   A 135 ? 0.1662 0.1741 0.1550 -0.0403 0.0202  -0.0112 141 LEU   A C   
1043 O O   . LEU   A 135 ? 0.1884 0.1912 0.1793 -0.0406 0.0259  -0.0170 141 LEU   A O   
1044 C CB  . LEU   A 135 ? 0.1756 0.1946 0.1477 -0.0545 0.0185  -0.0082 141 LEU   A CB  
1045 C CG  . LEU   A 135 ? 0.2096 0.2368 0.1757 -0.0588 0.0141  -0.0034 141 LEU   A CG  
1046 C CD1 . LEU   A 135 ? 0.2300 0.2635 0.1846 -0.0710 0.0160  -0.0044 141 LEU   A CD1 
1047 C CD2 . LEU   A 135 ? 0.2219 0.2467 0.1889 -0.0567 0.0145  -0.0058 141 LEU   A CD2 
1048 N N   . TRP   A 136 ? 0.1589 0.1678 0.1516 -0.0369 0.0171  -0.0075 142 TRP   A N   
1049 C CA  . TRP   A 136 ? 0.1655 0.1708 0.1644 -0.0343 0.0198  -0.0101 142 TRP   A CA  
1050 C C   . TRP   A 136 ? 0.1752 0.1759 0.1826 -0.0274 0.0204  -0.0123 142 TRP   A C   
1051 O O   . TRP   A 136 ? 0.1895 0.1882 0.2032 -0.0257 0.0235  -0.0149 142 TRP   A O   
1052 C CB  . TRP   A 136 ? 0.1732 0.1805 0.1736 -0.0331 0.0164  -0.0054 142 TRP   A CB  
1053 C CG  . TRP   A 136 ? 0.1643 0.1722 0.1676 -0.0278 0.0109  -0.0001 142 TRP   A CG  
1054 C CD1 . TRP   A 136 ? 0.1752 0.1872 0.1755 -0.0288 0.0071  0.0057  142 TRP   A CD1 
1055 C CD2 . TRP   A 136 ? 0.1658 0.1702 0.1761 -0.0210 0.0090  -0.0002 142 TRP   A CD2 
1056 N NE1 . TRP   A 136 ? 0.1888 0.1989 0.1944 -0.0226 0.0040  0.0086  142 TRP   A NE1 
1057 C CE2 . TRP   A 136 ? 0.1766 0.1819 0.1873 -0.0183 0.0051  0.0046  142 TRP   A CE2 
1058 C CE3 . TRP   A 136 ? 0.1782 0.1794 0.1947 -0.0174 0.0103  -0.0036 142 TRP   A CE3 
1059 C CZ2 . TRP   A 136 ? 0.1922 0.1944 0.2080 -0.0128 0.0032  0.0050  142 TRP   A CZ2 
1060 C CZ3 . TRP   A 136 ? 0.1940 0.1935 0.2150 -0.0124 0.0074  -0.0024 142 TRP   A CZ3 
1061 C CH2 . TRP   A 136 ? 0.1887 0.1882 0.2086 -0.0106 0.0043  0.0012  142 TRP   A CH2 
1062 N N   . LEU   A 137 ? 0.1551 0.1550 0.1634 -0.0237 0.0175  -0.0108 143 LEU   A N   
1063 C CA  . LEU   A 137 ? 0.1759 0.1722 0.1916 -0.0179 0.0178  -0.0122 143 LEU   A CA  
1064 C C   . LEU   A 137 ? 0.2021 0.1949 0.2209 -0.0192 0.0243  -0.0170 143 LEU   A C   
1065 O O   . LEU   A 137 ? 0.2105 0.2011 0.2378 -0.0146 0.0252  -0.0174 143 LEU   A O   
1066 C CB  . LEU   A 137 ? 0.1683 0.1644 0.1828 -0.0149 0.0142  -0.0100 143 LEU   A CB  
1067 C CG  . LEU   A 137 ? 0.1641 0.1622 0.1788 -0.0119 0.0089  -0.0058 143 LEU   A CG  
1068 C CD1 . LEU   A 137 ? 0.1874 0.1858 0.2000 -0.0103 0.0065  -0.0042 143 LEU   A CD1 
1069 C CD2 . LEU   A 137 ? 0.1695 0.1663 0.1908 -0.0077 0.0074  -0.0055 143 LEU   A CD2 
1070 N N   . ASP   A 138 ? 0.2211 0.2135 0.2333 -0.0258 0.0289  -0.0203 144 ASP   A N   
1071 C CA  . ASP   A 138 ? 0.2502 0.2377 0.2650 -0.0278 0.0368  -0.0258 144 ASP   A CA  
1072 C C   . ASP   A 138 ? 0.2977 0.2843 0.3175 -0.0292 0.0425  -0.0290 144 ASP   A C   
1073 O O   . ASP   A 138 ? 0.3134 0.2956 0.3368 -0.0309 0.0503  -0.0339 144 ASP   A O   
1074 C CB  . ASP   A 138 ? 0.2503 0.2374 0.2546 -0.0359 0.0403  -0.0291 144 ASP   A CB  
1075 C CG  . ASP   A 138 ? 0.3014 0.2892 0.3013 -0.0353 0.0364  -0.0269 144 ASP   A CG  
1076 O OD1 . ASP   A 138 ? 0.3035 0.2907 0.3090 -0.0283 0.0319  -0.0234 144 ASP   A OD1 
1077 O OD2 . ASP   A 138 ? 0.3768 0.3664 0.3675 -0.0425 0.0378  -0.0287 144 ASP   A OD2 
1078 N N   . GLU   A 139 ? 0.3200 0.3104 0.3405 -0.0290 0.0395  -0.0267 145 GLU   A N   
1079 C CA  . GLU   A 139 ? 0.3646 0.3549 0.3896 -0.0310 0.0451  -0.0299 145 GLU   A CA  
1080 C C   . GLU   A 139 ? 0.3949 0.3883 0.4272 -0.0264 0.0410  -0.0265 145 GLU   A C   
1081 O O   . GLU   A 139 ? 0.3881 0.3832 0.4211 -0.0222 0.0340  -0.0221 145 GLU   A O   
1082 C CB  . GLU   A 139 ? 0.4248 0.4171 0.4380 -0.0404 0.0480  -0.0323 145 GLU   A CB  
1083 C CG  . GLU   A 139 ? 0.5138 0.5113 0.5199 -0.0418 0.0404  -0.0265 145 GLU   A CG  
1084 C CD  . GLU   A 139 ? 0.6065 0.6079 0.5995 -0.0508 0.0402  -0.0260 145 GLU   A CD  
1085 O OE1 . GLU   A 139 ? 0.6160 0.6221 0.6048 -0.0520 0.0346  -0.0204 145 GLU   A OE1 
1086 O OE2 . GLU   A 139 ? 0.6438 0.6435 0.6308 -0.0571 0.0459  -0.0310 145 GLU   A OE2 
1087 N N   . GLU   A 140 ? 0.4339 0.4281 0.4711 -0.0282 0.0458  -0.0291 146 GLU   A N   
1088 C CA  . GLU   A 140 ? 0.4658 0.4634 0.5087 -0.0262 0.0433  -0.0268 146 GLU   A CA  
1089 C C   . GLU   A 140 ? 0.4830 0.4821 0.5352 -0.0189 0.0378  -0.0231 146 GLU   A C   
1090 O O   . GLU   A 140 ? 0.4890 0.4904 0.5399 -0.0176 0.0320  -0.0197 146 GLU   A O   
1091 C CB  . GLU   A 140 ? 0.5106 0.5106 0.5431 -0.0308 0.0394  -0.0242 146 GLU   A CB  
1092 C CG  . GLU   A 140 ? 0.5986 0.6012 0.6348 -0.0291 0.0357  -0.0212 146 GLU   A CG  
1093 C CD  . GLU   A 140 ? 0.7042 0.7085 0.7458 -0.0316 0.0407  -0.0238 146 GLU   A CD  
1094 O OE1 . GLU   A 140 ? 0.7177 0.7240 0.7624 -0.0306 0.0377  -0.0215 146 GLU   A OE1 
1095 O OE2 . GLU   A 140 ? 0.7366 0.7400 0.7792 -0.0350 0.0480  -0.0285 146 GLU   A OE2 
1096 N N   . SER   B 1   ? 0.2177 0.2210 0.2363 0.0038  -0.0165 0.0357  7   SER   C N   
1097 C CA  . SER   B 1   ? 0.2211 0.2260 0.2489 0.0026  -0.0170 0.0362  7   SER   C CA  
1098 C C   . SER   B 1   ? 0.2205 0.2236 0.2478 0.0017  -0.0166 0.0325  7   SER   C C   
1099 O O   . SER   B 1   ? 0.2414 0.2421 0.2612 0.0019  -0.0171 0.0298  7   SER   C O   
1100 C CB  . SER   B 1   ? 0.2626 0.2689 0.2922 0.0019  -0.0217 0.0390  7   SER   C CB  
1101 O OG  . SER   B 1   ? 0.3186 0.3229 0.3405 0.0011  -0.0256 0.0368  7   SER   C OG  
1102 N N   . GLY   B 2   ? 0.2022 0.2059 0.2373 0.0010  -0.0154 0.0326  8   GLY   C N   
1103 C CA  . GLY   B 2   ? 0.1896 0.1913 0.2242 0.0004  -0.0146 0.0299  8   GLY   C CA  
1104 C C   . GLY   B 2   ? 0.1673 0.1692 0.2087 0.0006  -0.0109 0.0296  8   GLY   C C   
1105 O O   . GLY   B 2   ? 0.1669 0.1699 0.2115 0.0013  -0.0084 0.0302  8   GLY   C O   
1106 N N   . ALA   B 3   ? 0.1507 0.1511 0.1939 0.0000  -0.0102 0.0288  9   ALA   C N   
1107 C CA  . ALA   B 3   ? 0.1533 0.1530 0.2014 0.0004  -0.0062 0.0284  9   ALA   C CA  
1108 C C   . ALA   B 3   ? 0.1387 0.1350 0.1824 0.0007  -0.0046 0.0262  9   ALA   C C   
1109 O O   . ALA   B 3   ? 0.1545 0.1493 0.1939 0.0002  -0.0068 0.0254  9   ALA   C O   
1110 C CB  . ALA   B 3   ? 0.1837 0.1853 0.2421 -0.0004 -0.0059 0.0314  9   ALA   C CB  
1111 N N   . ILE   B 4   ? 0.1363 0.1312 0.1809 0.0017  -0.0008 0.0252  10  ILE   C N   
1112 C CA  . ILE   B 4   ? 0.1388 0.1301 0.1795 0.0024  0.0014  0.0239  10  ILE   C CA  
1113 C C   . ILE   B 4   ? 0.1376 0.1285 0.1863 0.0018  0.0044  0.0260  10  ILE   C C   
1114 O O   . ILE   B 4   ? 0.1461 0.1384 0.2008 0.0020  0.0065  0.0270  10  ILE   C O   
1115 C CB  . ILE   B 4   ? 0.1479 0.1372 0.1825 0.0042  0.0037  0.0211  10  ILE   C CB  
1116 C CG1 . ILE   B 4   ? 0.1653 0.1559 0.1949 0.0048  0.0013  0.0192  10  ILE   C CG1 
1117 C CG2 . ILE   B 4   ? 0.1639 0.1491 0.1931 0.0053  0.0057  0.0204  10  ILE   C CG2 
1118 C CD1 . ILE   B 4   ? 0.1740 0.1638 0.2004 0.0063  0.0028  0.0164  10  ILE   C CD1 
1119 N N   . TYR   B 5   ? 0.1356 0.1244 0.1851 0.0013  0.0050  0.0268  11  TYR   C N   
1120 C CA  . TYR   B 5   ? 0.1454 0.1337 0.2035 0.0008  0.0084  0.0291  11  TYR   C CA  
1121 C C   . TYR   B 5   ? 0.1646 0.1480 0.2172 0.0023  0.0130  0.0283  11  TYR   C C   
1122 O O   . TYR   B 5   ? 0.1775 0.1585 0.2265 0.0022  0.0124  0.0282  11  TYR   C O   
1123 C CB  . TYR   B 5   ? 0.1511 0.1413 0.2172 -0.0014 0.0052  0.0312  11  TYR   C CB  
1124 C CG  . TYR   B 5   ? 0.1573 0.1521 0.2284 -0.0026 0.0006  0.0325  11  TYR   C CG  
1125 C CD1 . TYR   B 5   ? 0.1618 0.1597 0.2429 -0.0027 0.0018  0.0349  11  TYR   C CD1 
1126 C CD2 . TYR   B 5   ? 0.1679 0.1637 0.2331 -0.0031 -0.0044 0.0313  11  TYR   C CD2 
1127 C CE1 . TYR   B 5   ? 0.1742 0.1761 0.2591 -0.0033 -0.0023 0.0366  11  TYR   C CE1 
1128 C CE2 . TYR   B 5   ? 0.1861 0.1856 0.2541 -0.0037 -0.0083 0.0328  11  TYR   C CE2 
1129 C CZ  . TYR   B 5   ? 0.1872 0.1898 0.2649 -0.0037 -0.0075 0.0356  11  TYR   C CZ  
1130 O OH  . TYR   B 5   ? 0.2173 0.2233 0.2971 -0.0039 -0.0114 0.0375  11  TYR   C OH  
1131 N N   . VAL   B 6   ? 0.1693 0.1509 0.2201 0.0041  0.0175  0.0277  12  VAL   C N   
1132 C CA  . VAL   B 6   ? 0.1870 0.1634 0.2307 0.0061  0.0221  0.0272  12  VAL   C CA  
1133 C C   . VAL   B 6   ? 0.1923 0.1673 0.2426 0.0066  0.0281  0.0290  12  VAL   C C   
1134 O O   . VAL   B 6   ? 0.1747 0.1516 0.2296 0.0067  0.0293  0.0287  12  VAL   C O   
1135 C CB  . VAL   B 6   ? 0.2021 0.1768 0.2341 0.0081  0.0213  0.0238  12  VAL   C CB  
1136 C CG1 . VAL   B 6   ? 0.2106 0.1878 0.2447 0.0083  0.0210  0.0221  12  VAL   C CG1 
1137 C CG2 . VAL   B 6   ? 0.2302 0.1994 0.2534 0.0106  0.0256  0.0233  12  VAL   C CG2 
1138 N N   . GLY   B 7   ? 0.2015 0.1732 0.2535 0.0070  0.0325  0.0311  13  GLY   C N   
1139 C CA  . GLY   B 7   ? 0.1998 0.1699 0.2587 0.0077  0.0391  0.0331  13  GLY   C CA  
1140 C C   . GLY   B 7   ? 0.1970 0.1723 0.2709 0.0057  0.0380  0.0351  13  GLY   C C   
1141 O O   . GLY   B 7   ? 0.2073 0.1866 0.2882 0.0034  0.0328  0.0363  13  GLY   C O   
1142 N N   . ASN   B 8   ? 0.1842 0.1596 0.2619 0.0067  0.0418  0.0350  14  ASN   C N   
1143 C CA  . ASN   B 8   ? 0.1855 0.1660 0.2773 0.0053  0.0404  0.0371  14  ASN   C CA  
1144 C C   . ASN   B 8   ? 0.1716 0.1547 0.2607 0.0053  0.0366  0.0350  14  ASN   C C   
1145 O O   . ASN   B 8   ? 0.1721 0.1574 0.2699 0.0054  0.0381  0.0361  14  ASN   C O   
1146 C CB  . ASN   B 8   ? 0.2114 0.1907 0.3135 0.0061  0.0477  0.0395  14  ASN   C CB  
1147 C CG  . ASN   B 8   ? 0.2913 0.2701 0.4021 0.0052  0.0506  0.0428  14  ASN   C CG  
1148 O OD1 . ASN   B 8   ? 0.3275 0.3112 0.4524 0.0031  0.0476  0.0455  14  ASN   C OD1 
1149 N ND2 . ASN   B 8   ? 0.3119 0.2850 0.4143 0.0068  0.0557  0.0425  14  ASN   C ND2 
1150 N N   . TYR   B 9   ? 0.1455 0.1288 0.2243 0.0052  0.0317  0.0325  15  TYR   C N   
1151 C CA  . TYR   B 9   ? 0.1507 0.1363 0.2270 0.0052  0.0283  0.0305  15  TYR   C CA  
1152 C C   . TYR   B 9   ? 0.1434 0.1328 0.2192 0.0035  0.0215  0.0310  15  TYR   C C   
1153 O O   . TYR   B 9   ? 0.1652 0.1537 0.2364 0.0029  0.0190  0.0308  15  TYR   C O   
1154 C CB  . TYR   B 9   ? 0.1677 0.1495 0.2311 0.0070  0.0293  0.0263  15  TYR   C CB  
1155 C CG  . TYR   B 9   ? 0.1854 0.1625 0.2458 0.0090  0.0358  0.0249  15  TYR   C CG  
1156 C CD1 . TYR   B 9   ? 0.2122 0.1896 0.2804 0.0093  0.0394  0.0252  15  TYR   C CD1 
1157 C CD2 . TYR   B 9   ? 0.2200 0.1921 0.2695 0.0108  0.0384  0.0233  15  TYR   C CD2 
1158 C CE1 . TYR   B 9   ? 0.2474 0.2198 0.3121 0.0113  0.0457  0.0235  15  TYR   C CE1 
1159 C CE2 . TYR   B 9   ? 0.2567 0.2239 0.3014 0.0129  0.0444  0.0218  15  TYR   C CE2 
1160 C CZ  . TYR   B 9   ? 0.2858 0.2530 0.3380 0.0131  0.0481  0.0216  15  TYR   C CZ  
1161 O OH  . TYR   B 9   ? 0.3583 0.3200 0.4053 0.0153  0.0543  0.0198  15  TYR   C OH  
1162 N N   . ARG   B 10  ? 0.1344 0.1273 0.2143 0.0030  0.0187  0.0316  16  ARG   C N   
1163 C CA  . ARG   B 10  ? 0.1328 0.1288 0.2105 0.0019  0.0127  0.0319  16  ARG   C CA  
1164 C C   . ARG   B 10  ? 0.1291 0.1250 0.2014 0.0028  0.0125  0.0295  16  ARG   C C   
1165 O O   . ARG   B 10  ? 0.1357 0.1320 0.2131 0.0033  0.0150  0.0296  16  ARG   C O   
1166 C CB  . ARG   B 10  ? 0.1517 0.1521 0.2403 0.0007  0.0099  0.0357  16  ARG   C CB  
1167 C CG  . ARG   B 10  ? 0.1667 0.1700 0.2526 0.0002  0.0045  0.0364  16  ARG   C CG  
1168 C CD  . ARG   B 10  ? 0.1536 0.1608 0.2490 -0.0008 0.0011  0.0403  16  ARG   C CD  
1169 N NE  . ARG   B 10  ? 0.1656 0.1753 0.2613 -0.0004 -0.0013 0.0421  16  ARG   C NE  
1170 C CZ  . ARG   B 10  ? 0.1899 0.2009 0.2796 -0.0007 -0.0061 0.0425  16  ARG   C CZ  
1171 N NH1 . ARG   B 10  ? 0.2021 0.2119 0.2846 -0.0015 -0.0093 0.0406  16  ARG   C NH1 
1172 N NH2 . ARG   B 10  ? 0.1850 0.1978 0.2753 0.0001  -0.0073 0.0447  16  ARG   C NH2 
1173 N N   . VAL   B 11  ? 0.1235 0.1187 0.1865 0.0030  0.0099  0.0271  17  VAL   C N   
1174 C CA  . VAL   B 11  ? 0.1237 0.1191 0.1827 0.0037  0.0095  0.0246  17  VAL   C CA  
1175 C C   . VAL   B 11  ? 0.1250 0.1235 0.1841 0.0030  0.0056  0.0261  17  VAL   C C   
1176 O O   . VAL   B 11  ? 0.1322 0.1307 0.1864 0.0025  0.0025  0.0263  17  VAL   C O   
1177 C CB  . VAL   B 11  ? 0.1432 0.1357 0.1920 0.0048  0.0095  0.0209  17  VAL   C CB  
1178 C CG1 . VAL   B 11  ? 0.1648 0.1579 0.2117 0.0054  0.0092  0.0182  17  VAL   C CG1 
1179 C CG2 . VAL   B 11  ? 0.1634 0.1521 0.2094 0.0059  0.0132  0.0199  17  VAL   C CG2 
1180 N N   . VAL   B 12  ? 0.1173 0.1178 0.1812 0.0030  0.0060  0.0272  18  VAL   C N   
1181 C CA  . VAL   B 12  ? 0.1273 0.1302 0.1907 0.0027  0.0030  0.0292  18  VAL   C CA  
1182 C C   . VAL   B 12  ? 0.1226 0.1259 0.1864 0.0033  0.0045  0.0279  18  VAL   C C   
1183 O O   . VAL   B 12  ? 0.1283 0.1303 0.1949 0.0037  0.0074  0.0257  18  VAL   C O   
1184 C CB  . VAL   B 12  ? 0.1496 0.1551 0.2208 0.0022  0.0018  0.0337  18  VAL   C CB  
1185 C CG1 . VAL   B 12  ? 0.1852 0.1909 0.2566 0.0013  -0.0008 0.0349  18  VAL   C CG1 
1186 C CG2 . VAL   B 12  ? 0.1485 0.1544 0.2295 0.0026  0.0054  0.0351  18  VAL   C CG2 
1187 N N   . ASN   B 13  ? 0.1165 0.1213 0.1780 0.0033  0.0026  0.0292  19  ASN   C N   
1188 C CA  . ASN   B 13  ? 0.1141 0.1195 0.1785 0.0037  0.0045  0.0289  19  ASN   C CA  
1189 C C   . ASN   B 13  ? 0.1251 0.1313 0.1992 0.0037  0.0067  0.0318  19  ASN   C C   
1190 O O   . ASN   B 13  ? 0.1216 0.1292 0.1989 0.0036  0.0054  0.0358  19  ASN   C O   
1191 C CB  . ASN   B 13  ? 0.1242 0.1308 0.1847 0.0040  0.0029  0.0309  19  ASN   C CB  
1192 C CG  . ASN   B 13  ? 0.1260 0.1318 0.1777 0.0042  0.0011  0.0283  19  ASN   C CG  
1193 O OD1 . ASN   B 13  ? 0.1466 0.1517 0.1927 0.0040  -0.0015 0.0288  19  ASN   C OD1 
1194 N ND2 . ASN   B 13  ? 0.1323 0.1378 0.1833 0.0046  0.0024  0.0253  19  ASN   C ND2 
1195 N N   . ARG   B 14  ? 0.1178 0.1232 0.1970 0.0039  0.0099  0.0297  20  ARG   C N   
1196 C CA  . ARG   B 14  ? 0.1063 0.1119 0.1954 0.0040  0.0126  0.0321  20  ARG   C CA  
1197 C C   . ARG   B 14  ? 0.1200 0.1277 0.2123 0.0043  0.0118  0.0376  20  ARG   C C   
1198 O O   . ARG   B 14  ? 0.1269 0.1356 0.2256 0.0046  0.0120  0.0415  20  ARG   C O   
1199 C CB  . ARG   B 14  ? 0.1059 0.1098 0.1993 0.0040  0.0158  0.0284  20  ARG   C CB  
1200 C CG  . ARG   B 14  ? 0.1117 0.1148 0.2157 0.0042  0.0193  0.0302  20  ARG   C CG  
1201 C CD  . ARG   B 14  ? 0.1182 0.1193 0.2261 0.0039  0.0221  0.0257  20  ARG   C CD  
1202 N NE  . ARG   B 14  ? 0.1258 0.1251 0.2434 0.0041  0.0261  0.0261  20  ARG   C NE  
1203 C CZ  . ARG   B 14  ? 0.1284 0.1282 0.2551 0.0043  0.0282  0.0298  20  ARG   C CZ  
1204 N NH1 . ARG   B 14  ? 0.1429 0.1452 0.2698 0.0044  0.0268  0.0341  20  ARG   C NH1 
1205 N NH2 . ARG   B 14  ? 0.1254 0.1230 0.2610 0.0045  0.0321  0.0293  20  ARG   C NH2 
1206 N N   . HIS   B 15  ? 0.1158 0.1242 0.2033 0.0046  0.0108  0.0380  21  HIS   C N   
1207 C CA  . HIS   B 15  ? 0.1303 0.1400 0.2193 0.0053  0.0105  0.0435  21  HIS   C CA  
1208 C C   . HIS   B 15  ? 0.1327 0.1438 0.2173 0.0055  0.0064  0.0472  21  HIS   C C   
1209 O O   . HIS   B 15  ? 0.1596 0.1717 0.2456 0.0064  0.0057  0.0521  21  HIS   C O   
1210 C CB  . HIS   B 15  ? 0.1265 0.1361 0.2123 0.0057  0.0117  0.0432  21  HIS   C CB  
1211 C CG  . HIS   B 15  ? 0.1369 0.1464 0.2119 0.0057  0.0090  0.0416  21  HIS   C CG  
1212 N ND1 . HIS   B 15  ? 0.1435 0.1523 0.2145 0.0052  0.0085  0.0364  21  HIS   C ND1 
1213 C CD2 . HIS   B 15  ? 0.1529 0.1627 0.2203 0.0065  0.0068  0.0446  21  HIS   C CD2 
1214 C CE1 . HIS   B 15  ? 0.1592 0.1678 0.2212 0.0056  0.0064  0.0364  21  HIS   C CE1 
1215 N NE2 . HIS   B 15  ? 0.1584 0.1674 0.2176 0.0063  0.0054  0.0410  21  HIS   C NE2 
1216 N N   . LEU   B 16  ? 0.1258 0.1367 0.2060 0.0048  0.0037  0.0449  22  LEU   C N   
1217 C CA  . LEU   B 16  ? 0.1413 0.1535 0.2185 0.0047  -0.0007 0.0476  22  LEU   C CA  
1218 C C   . LEU   B 16  ? 0.1499 0.1630 0.2350 0.0041  -0.0010 0.0485  22  LEU   C C   
1219 O O   . LEU   B 16  ? 0.1597 0.1740 0.2442 0.0037  -0.0050 0.0501  22  LEU   C O   
1220 C CB  . LEU   B 16  ? 0.1478 0.1589 0.2142 0.0042  -0.0037 0.0447  22  LEU   C CB  
1221 C CG  . LEU   B 16  ? 0.1530 0.1632 0.2117 0.0049  -0.0033 0.0443  22  LEU   C CG  
1222 C CD1 . LEU   B 16  ? 0.1645 0.1733 0.2133 0.0045  -0.0057 0.0409  22  LEU   C CD1 
1223 C CD2 . LEU   B 16  ? 0.1606 0.1718 0.2180 0.0060  -0.0043 0.0494  22  LEU   C CD2 
1224 N N   . ALA   B 17  ? 0.1448 0.1570 0.2375 0.0042  0.0032  0.0470  23  ALA   C N   
1225 C CA  . ALA   B 17  ? 0.1349 0.1475 0.2354 0.0039  0.0040  0.0477  23  ALA   C CA  
1226 C C   . ALA   B 17  ? 0.1513 0.1667 0.2597 0.0044  0.0019  0.0534  23  ALA   C C   
1227 O O   . ALA   B 17  ? 0.1708 0.1872 0.2819 0.0054  0.0023  0.0568  23  ALA   C O   
1228 C CB  . ALA   B 17  ? 0.1570 0.1674 0.2631 0.0042  0.0095  0.0450  23  ALA   C CB  
1229 N N   . THR   B 18  ? 0.1620 0.1790 0.2749 0.0038  -0.0001 0.0545  24  THR   C N   
1230 C CA  . THR   B 18  ? 0.1654 0.1857 0.2871 0.0042  -0.0030 0.0599  24  THR   C CA  
1231 C C   . THR   B 18  ? 0.1596 0.1802 0.2948 0.0050  0.0017  0.0617  24  THR   C C   
1232 O O   . THR   B 18  ? 0.1712 0.1890 0.3078 0.0050  0.0070  0.0583  24  THR   C O   
1233 C CB  . THR   B 18  ? 0.1898 0.2119 0.3111 0.0030  -0.0081 0.0600  24  THR   C CB  
1234 O OG1 . THR   B 18  ? 0.1839 0.2047 0.3101 0.0022  -0.0045 0.0575  24  THR   C OG1 
1235 C CG2 . THR   B 18  ? 0.2116 0.2327 0.3196 0.0022  -0.0124 0.0576  24  THR   C CG2 
1236 N N   . HIS   B 19  ? 0.1778 0.2017 0.3230 0.0058  -0.0005 0.0671  25  HIS   C N   
1237 C CA  . HIS   B 19  ? 0.1892 0.2135 0.3484 0.0066  0.0041  0.0690  25  HIS   C CA  
1238 C C   . HIS   B 19  ? 0.1602 0.1836 0.3231 0.0056  0.0066  0.0661  25  HIS   C C   
1239 O O   . HIS   B 19  ? 0.1717 0.1924 0.3393 0.0061  0.0129  0.0642  25  HIS   C O   
1240 C CB  . HIS   B 19  ? 0.2099 0.2385 0.3798 0.0077  0.0004  0.0756  25  HIS   C CB  
1241 C CG  . HIS   B 19  ? 0.2426 0.2722 0.4285 0.0085  0.0047  0.0777  25  HIS   C CG  
1242 N ND1 . HIS   B 19  ? 0.2679 0.2950 0.4603 0.0098  0.0114  0.0777  25  HIS   C ND1 
1243 C CD2 . HIS   B 19  ? 0.2692 0.3014 0.4655 0.0081  0.0039  0.0791  25  HIS   C CD2 
1244 C CE1 . HIS   B 19  ? 0.2702 0.2985 0.4765 0.0104  0.0142  0.0798  25  HIS   C CE1 
1245 N NE2 . HIS   B 19  ? 0.2719 0.3035 0.4814 0.0094  0.0101  0.0807  25  HIS   C NE2 
1246 N N   . ASN   B 20  ? 0.1649 0.1898 0.3246 0.0043  0.0022  0.0654  26  ASN   C N   
1247 C CA  . ASN   B 20  ? 0.1653 0.1889 0.3285 0.0034  0.0053  0.0630  26  ASN   C CA  
1248 C C   . ASN   B 20  ? 0.1491 0.1675 0.3030 0.0034  0.0107  0.0576  26  ASN   C C   
1249 O O   . ASN   B 20  ? 0.1498 0.1658 0.3079 0.0038  0.0165  0.0561  26  ASN   C O   
1250 C CB  . ASN   B 20  ? 0.1910 0.2166 0.3528 0.0018  -0.0003 0.0631  26  ASN   C CB  
1251 C CG  . ASN   B 20  ? 0.2702 0.2946 0.4381 0.0010  0.0036  0.0617  26  ASN   C CG  
1252 O OD1 . ASN   B 20  ? 0.3100 0.3363 0.4921 0.0015  0.0063  0.0645  26  ASN   C OD1 
1253 N ND2 . ASN   B 20  ? 0.2940 0.3148 0.4519 0.0002  0.0050  0.0576  26  ASN   C ND2 
1254 N N   . ASP   B 21  ? 0.1438 0.1604 0.2849 0.0033  0.0091  0.0547  27  ASP   C N   
1255 C CA  . ASP   B 21  ? 0.1427 0.1549 0.2755 0.0035  0.0135  0.0496  27  ASP   C CA  
1256 C C   . ASP   B 21  ? 0.1307 0.1406 0.2693 0.0047  0.0195  0.0488  27  ASP   C C   
1257 O O   . ASP   B 21  ? 0.1520 0.1584 0.2894 0.0050  0.0244  0.0457  27  ASP   C O   
1258 C CB  . ASP   B 21  ? 0.1378 0.1492 0.2584 0.0032  0.0106  0.0472  27  ASP   C CB  
1259 C CG  . ASP   B 21  ? 0.1456 0.1573 0.2575 0.0021  0.0059  0.0461  27  ASP   C CG  
1260 O OD1 . ASP   B 21  ? 0.1603 0.1711 0.2722 0.0015  0.0064  0.0451  27  ASP   C OD1 
1261 O OD2 . ASP   B 21  ? 0.1528 0.1657 0.2585 0.0020  0.0020  0.0467  27  ASP   C OD2 
1262 N N   . TRP   B 22  ? 0.1341 0.1456 0.2789 0.0054  0.0194  0.0518  28  TRP   C N   
1263 C CA  . TRP   B 22  ? 0.1391 0.1481 0.2902 0.0064  0.0252  0.0509  28  TRP   C CA  
1264 C C   . TRP   B 22  ? 0.1391 0.1478 0.3018 0.0072  0.0298  0.0525  28  TRP   C C   
1265 O O   . TRP   B 22  ? 0.1569 0.1616 0.3211 0.0079  0.0357  0.0494  28  TRP   C O   
1266 C CB  . TRP   B 22  ? 0.1474 0.1580 0.3031 0.0071  0.0244  0.0542  28  TRP   C CB  
1267 C CG  . TRP   B 22  ? 0.1518 0.1610 0.2978 0.0067  0.0232  0.0514  28  TRP   C CG  
1268 C CD1 . TRP   B 22  ? 0.1735 0.1847 0.3124 0.0063  0.0185  0.0530  28  TRP   C CD1 
1269 C CD2 . TRP   B 22  ? 0.1429 0.1483 0.2860 0.0066  0.0270  0.0464  28  TRP   C CD2 
1270 N NE1 . TRP   B 22  ? 0.1776 0.1869 0.3107 0.0061  0.0196  0.0497  28  TRP   C NE1 
1271 C CE2 . TRP   B 22  ? 0.1693 0.1753 0.3049 0.0061  0.0243  0.0454  28  TRP   C CE2 
1272 C CE3 . TRP   B 22  ? 0.1731 0.1747 0.3191 0.0069  0.0323  0.0424  28  TRP   C CE3 
1273 C CZ2 . TRP   B 22  ? 0.1716 0.1751 0.3050 0.0059  0.0266  0.0411  28  TRP   C CZ2 
1274 C CZ3 . TRP   B 22  ? 0.1847 0.1834 0.3268 0.0066  0.0339  0.0375  28  TRP   C CZ3 
1275 C CH2 . TRP   B 22  ? 0.1737 0.1737 0.3102 0.0060  0.0309  0.0370  28  TRP   C CH2 
1276 N N   . ALA   B 23  ? 0.1423 0.1548 0.3126 0.0070  0.0269  0.0568  29  ALA   C N   
1277 C CA  . ALA   B 23  ? 0.1453 0.1582 0.3285 0.0077  0.0313  0.0589  29  ALA   C CA  
1278 C C   . ALA   B 23  ? 0.1711 0.1806 0.3498 0.0074  0.0352  0.0553  29  ALA   C C   
1279 O O   . ALA   B 23  ? 0.1705 0.1788 0.3582 0.0082  0.0406  0.0561  29  ALA   C O   
1280 C CB  . ALA   B 23  ? 0.1461 0.1648 0.3401 0.0075  0.0262  0.0648  29  ALA   C CB  
1281 N N   . ASN   B 24  ? 0.1666 0.1743 0.3315 0.0064  0.0328  0.0516  30  ASN   C N   
1282 C CA  . ASN   B 24  ? 0.1566 0.1605 0.3152 0.0063  0.0364  0.0484  30  ASN   C CA  
1283 C C   . ASN   B 24  ? 0.1597 0.1591 0.3034 0.0066  0.0374  0.0428  30  ASN   C C   
1284 O O   . ASN   B 24  ? 0.1580 0.1553 0.2914 0.0062  0.0366  0.0402  30  ASN   C O   
1285 C CB  . ASN   B 24  ? 0.1782 0.1849 0.3364 0.0048  0.0317  0.0501  30  ASN   C CB  
1286 C CG  . ASN   B 24  ? 0.1976 0.2087 0.3721 0.0046  0.0310  0.0552  30  ASN   C CG  
1287 O OD1 . ASN   B 24  ? 0.2164 0.2264 0.3995 0.0052  0.0365  0.0562  30  ASN   C OD1 
1288 N ND2 . ASN   B 24  ? 0.2045 0.2206 0.3837 0.0039  0.0243  0.0586  30  ASN   C ND2 
1289 N N   . LEU   B 25  ? 0.1628 0.1606 0.3059 0.0073  0.0391  0.0409  31  LEU   C N   
1290 C CA  . LEU   B 25  ? 0.1663 0.1606 0.2968 0.0073  0.0389  0.0356  31  LEU   C CA  
1291 C C   . LEU   B 25  ? 0.1854 0.1742 0.3075 0.0083  0.0436  0.0310  31  LEU   C C   
1292 O O   . LEU   B 25  ? 0.1958 0.1817 0.3229 0.0095  0.0495  0.0308  31  LEU   C O   
1293 C CB  . LEU   B 25  ? 0.1632 0.1574 0.2982 0.0076  0.0399  0.0350  31  LEU   C CB  
1294 C CG  . LEU   B 25  ? 0.1664 0.1579 0.2913 0.0075  0.0390  0.0296  31  LEU   C CG  
1295 C CD1 . LEU   B 25  ? 0.1654 0.1598 0.2823 0.0064  0.0329  0.0298  31  LEU   C CD1 
1296 C CD2 . LEU   B 25  ? 0.1776 0.1682 0.3093 0.0077  0.0413  0.0288  31  LEU   C CD2 
1297 N N   . VAL   B 26  ? 0.1731 0.1602 0.2822 0.0081  0.0411  0.0274  32  VAL   C N   
1298 C CA  . VAL   B 26  ? 0.1825 0.1639 0.2811 0.0094  0.0447  0.0228  32  VAL   C CA  
1299 C C   . VAL   B 26  ? 0.1915 0.1709 0.2834 0.0096  0.0435  0.0176  32  VAL   C C   
1300 O O   . VAL   B 26  ? 0.2062 0.1810 0.2954 0.0107  0.0476  0.0137  32  VAL   C O   
1301 C CB  . VAL   B 26  ? 0.1961 0.1769 0.2851 0.0093  0.0426  0.0227  32  VAL   C CB  
1302 C CG1 . VAL   B 26  ? 0.2210 0.1960 0.2970 0.0110  0.0453  0.0181  32  VAL   C CG1 
1303 C CG2 . VAL   B 26  ? 0.1992 0.1816 0.2961 0.0089  0.0442  0.0273  32  VAL   C CG2 
1304 N N   . TRP   B 27  ? 0.1704 0.1531 0.2601 0.0085  0.0380  0.0174  33  TRP   C N   
1305 C CA  . TRP   B 27  ? 0.1719 0.1532 0.2565 0.0084  0.0365  0.0125  33  TRP   C CA  
1306 C C   . TRP   B 27  ? 0.1627 0.1486 0.2501 0.0071  0.0318  0.0144  33  TRP   C C   
1307 O O   . TRP   B 27  ? 0.1567 0.1458 0.2435 0.0065  0.0286  0.0179  33  TRP   C O   
1308 C CB  . TRP   B 27  ? 0.1910 0.1689 0.2616 0.0094  0.0355  0.0080  33  TRP   C CB  
1309 C CG  . TRP   B 27  ? 0.1945 0.1722 0.2594 0.0092  0.0321  0.0031  33  TRP   C CG  
1310 C CD1 . TRP   B 27  ? 0.2203 0.1947 0.2839 0.0096  0.0334  -0.0021 33  TRP   C CD1 
1311 C CD2 . TRP   B 27  ? 0.1721 0.1529 0.2329 0.0085  0.0268  0.0029  33  TRP   C CD2 
1312 N NE1 . TRP   B 27  ? 0.2274 0.2032 0.2869 0.0092  0.0288  -0.0056 33  TRP   C NE1 
1313 C CE2 . TRP   B 27  ? 0.1933 0.1730 0.2510 0.0086  0.0251  -0.0024 33  TRP   C CE2 
1314 C CE3 . TRP   B 27  ? 0.1710 0.1553 0.2307 0.0079  0.0235  0.0064  33  TRP   C CE3 
1315 C CZ2 . TRP   B 27  ? 0.1967 0.1791 0.2512 0.0082  0.0204  -0.0038 33  TRP   C CZ2 
1316 C CZ3 . TRP   B 27  ? 0.1927 0.1789 0.2477 0.0077  0.0193  0.0047  33  TRP   C CZ3 
1317 C CH2 . TRP   B 27  ? 0.1940 0.1795 0.2474 0.0078  0.0179  0.0000  33  TRP   C CH2 
1318 N N   . GLU   B 28  ? 0.1614 0.1474 0.2520 0.0067  0.0315  0.0121  34  GLU   C N   
1319 C CA  . GLU   B 28  ? 0.1649 0.1547 0.2577 0.0058  0.0279  0.0138  34  GLU   C CA  
1320 C C   . GLU   B 28  ? 0.1584 0.1471 0.2505 0.0054  0.0274  0.0089  34  GLU   C C   
1321 O O   . GLU   B 28  ? 0.1620 0.1472 0.2561 0.0057  0.0303  0.0050  34  GLU   C O   
1322 C CB  . GLU   B 28  ? 0.1582 0.1510 0.2618 0.0054  0.0284  0.0195  34  GLU   C CB  
1323 C CG  . GLU   B 28  ? 0.1693 0.1603 0.2829 0.0058  0.0330  0.0197  34  GLU   C CG  
1324 C CD  . GLU   B 28  ? 0.2005 0.1906 0.3191 0.0053  0.0341  0.0173  34  GLU   C CD  
1325 O OE1 . GLU   B 28  ? 0.2345 0.2213 0.3586 0.0056  0.0381  0.0149  34  GLU   C OE1 
1326 O OE2 . GLU   B 28  ? 0.1771 0.1694 0.2944 0.0046  0.0313  0.0176  34  GLU   C OE2 
1327 N N   . ASP   B 29  ? 0.1398 0.1312 0.2298 0.0048  0.0238  0.0089  35  ASP   C N   
1328 C CA  . ASP   B 29  ? 0.1457 0.1368 0.2371 0.0043  0.0230  0.0045  35  ASP   C CA  
1329 C C   . ASP   B 29  ? 0.1417 0.1367 0.2370 0.0036  0.0212  0.0077  35  ASP   C C   
1330 O O   . ASP   B 29  ? 0.1434 0.1405 0.2326 0.0037  0.0182  0.0088  35  ASP   C O   
1331 C CB  . ASP   B 29  ? 0.1654 0.1546 0.2463 0.0049  0.0206  -0.0010 35  ASP   C CB  
1332 C CG  . ASP   B 29  ? 0.2246 0.2138 0.3071 0.0043  0.0188  -0.0062 35  ASP   C CG  
1333 O OD1 . ASP   B 29  ? 0.2339 0.2259 0.3238 0.0034  0.0184  -0.0049 35  ASP   C OD1 
1334 O OD2 . ASP   B 29  ? 0.2625 0.2489 0.3383 0.0050  0.0177  -0.0116 35  ASP   C OD2 
1335 N N   . SER   B 30  ? 0.1399 0.1354 0.2453 0.0030  0.0235  0.0093  36  SER   C N   
1336 C CA  A SER   B 30  ? 0.1442 0.1427 0.2537 0.0026  0.0228  0.0128  36  SER   C CA  
1337 C CA  B SER   B 30  ? 0.1443 0.1429 0.2535 0.0026  0.0227  0.0129  36  SER   C CA  
1338 C C   . SER   B 30  ? 0.1496 0.1494 0.2560 0.0022  0.0203  0.0091  36  SER   C C   
1339 O O   . SER   B 30  ? 0.1540 0.1562 0.2578 0.0023  0.0189  0.0119  36  SER   C O   
1340 C CB  A SER   B 30  ? 0.1684 0.1664 0.2899 0.0022  0.0264  0.0150  36  SER   C CB  
1341 C CB  B SER   B 30  ? 0.1671 0.1653 0.2880 0.0023  0.0263  0.0157  36  SER   C CB  
1342 O OG  A SER   B 30  ? 0.1757 0.1759 0.3010 0.0019  0.0265  0.0176  36  SER   C OG  
1343 O OG  B SER   B 30  ? 0.1713 0.1669 0.2978 0.0016  0.0282  0.0103  36  SER   C OG  
1344 N N   . SER   B 31  ? 0.1470 0.1450 0.2532 0.0018  0.0197  0.0027  37  SER   C N   
1345 C CA  . SER   B 31  ? 0.1552 0.1550 0.2600 0.0015  0.0169  -0.0008 37  SER   C CA  
1346 C C   . SER   B 31  ? 0.1464 0.1476 0.2404 0.0024  0.0135  -0.0003 37  SER   C C   
1347 O O   . SER   B 31  ? 0.1574 0.1609 0.2511 0.0024  0.0116  -0.0010 37  SER   C O   
1348 C CB  . SER   B 31  ? 0.1973 0.1950 0.3037 0.0010  0.0158  -0.0080 37  SER   C CB  
1349 O OG  . SER   B 31  ? 0.2815 0.2766 0.3776 0.0020  0.0141  -0.0114 37  SER   C OG  
1350 N N   . ARG   B 32  ? 0.1365 0.1362 0.2224 0.0032  0.0131  0.0010  38  ARG   C N   
1351 C CA  . ARG   B 32  ? 0.1358 0.1361 0.2117 0.0041  0.0103  0.0017  38  ARG   C CA  
1352 C C   . ARG   B 32  ? 0.1376 0.1395 0.2121 0.0041  0.0105  0.0075  38  ARG   C C   
1353 O O   . ARG   B 32  ? 0.1368 0.1391 0.2039 0.0046  0.0083  0.0083  38  ARG   C O   
1354 C CB  . ARG   B 32  ? 0.1550 0.1521 0.2228 0.0050  0.0100  -0.0006 38  ARG   C CB  
1355 C CG  . ARG   B 32  ? 0.1730 0.1680 0.2388 0.0053  0.0090  -0.0069 38  ARG   C CG  
1356 C CD  . ARG   B 32  ? 0.1608 0.1520 0.2172 0.0067  0.0093  -0.0087 38  ARG   C CD  
1357 N NE  . ARG   B 32  ? 0.1633 0.1547 0.2104 0.0078  0.0070  -0.0073 38  ARG   C NE  
1358 C CZ  . ARG   B 32  ? 0.1705 0.1590 0.2077 0.0093  0.0060  -0.0097 38  ARG   C CZ  
1359 N NH1 . ARG   B 32  ? 0.1891 0.1740 0.2230 0.0101  0.0069  -0.0138 38  ARG   C NH1 
1360 N NH2 . ARG   B 32  ? 0.1665 0.1552 0.1965 0.0103  0.0040  -0.0082 38  ARG   C NH2 
1361 N N   . ASP   B 33  ? 0.1169 0.1194 0.1983 0.0037  0.0128  0.0116  39  ASP   C N   
1362 C CA  . ASP   B 33  ? 0.1157 0.1195 0.1953 0.0038  0.0123  0.0170  39  ASP   C CA  
1363 C C   . ASP   B 33  ? 0.1146 0.1172 0.1883 0.0041  0.0111  0.0176  39  ASP   C C   
1364 O O   . ASP   B 33  ? 0.1273 0.1308 0.1962 0.0042  0.0091  0.0202  39  ASP   C O   
1365 C CB  . ASP   B 33  ? 0.1209 0.1266 0.1970 0.0040  0.0108  0.0188  39  ASP   C CB  
1366 C CG  . ASP   B 33  ? 0.1287 0.1353 0.2026 0.0042  0.0101  0.0242  39  ASP   C CG  
1367 O OD1 . ASP   B 33  ? 0.1407 0.1475 0.2202 0.0042  0.0114  0.0278  39  ASP   C OD1 
1368 O OD2 . ASP   B 33  ? 0.1360 0.1430 0.2028 0.0046  0.0081  0.0249  39  ASP   C OD2 
1369 N N   . LEU   B 34  ? 0.1112 0.1114 0.1853 0.0043  0.0127  0.0153  40  LEU   C N   
1370 C CA  . LEU   B 34  ? 0.1172 0.1161 0.1868 0.0046  0.0124  0.0163  40  LEU   C CA  
1371 C C   . LEU   B 34  ? 0.1158 0.1139 0.1925 0.0045  0.0154  0.0184  40  LEU   C C   
1372 O O   . LEU   B 34  ? 0.1273 0.1241 0.2097 0.0046  0.0181  0.0169  40  LEU   C O   
1373 C CB  . LEU   B 34  ? 0.1248 0.1211 0.1867 0.0053  0.0120  0.0118  40  LEU   C CB  
1374 C CG  . LEU   B 34  ? 0.1340 0.1308 0.1881 0.0057  0.0088  0.0100  40  LEU   C CG  
1375 C CD1 . LEU   B 34  ? 0.1586 0.1524 0.2050 0.0069  0.0085  0.0060  40  LEU   C CD1 
1376 C CD2 . LEU   B 34  ? 0.1510 0.1490 0.2019 0.0055  0.0069  0.0135  40  LEU   C CD2 
1377 N N   . LEU   B 35  ? 0.1079 0.1063 0.1842 0.0045  0.0149  0.0215  41  LEU   C N   
1378 C CA  . LEU   B 35  ? 0.1217 0.1194 0.2050 0.0046  0.0178  0.0236  41  LEU   C CA  
1379 C C   . LEU   B 35  ? 0.1245 0.1212 0.2038 0.0047  0.0174  0.0242  41  LEU   C C   
1380 O O   . LEU   B 35  ? 0.1329 0.1309 0.2075 0.0042  0.0140  0.0253  41  LEU   C O   
1381 C CB  . LEU   B 35  ? 0.1267 0.1275 0.2190 0.0043  0.0173  0.0287  41  LEU   C CB  
1382 C CG  . LEU   B 35  ? 0.1186 0.1193 0.2203 0.0046  0.0202  0.0315  41  LEU   C CG  
1383 C CD1 . LEU   B 35  ? 0.1487 0.1512 0.2602 0.0048  0.0213  0.0351  41  LEU   C CD1 
1384 C CD2 . LEU   B 35  ? 0.1341 0.1366 0.2366 0.0041  0.0180  0.0347  41  LEU   C CD2 
1385 N N   . VAL   B 36  ? 0.1260 0.1201 0.2072 0.0053  0.0213  0.0234  42  VAL   C N   
1386 C CA  . VAL   B 36  ? 0.1257 0.1183 0.2050 0.0054  0.0223  0.0244  42  VAL   C CA  
1387 C C   . VAL   B 36  ? 0.1215 0.1149 0.2119 0.0054  0.0255  0.0279  42  VAL   C C   
1388 O O   . VAL   B 36  ? 0.1451 0.1371 0.2408 0.0061  0.0294  0.0273  42  VAL   C O   
1389 C CB  . VAL   B 36  ? 0.1434 0.1315 0.2134 0.0067  0.0248  0.0203  42  VAL   C CB  
1390 C CG1 . VAL   B 36  ? 0.1552 0.1413 0.2237 0.0070  0.0269  0.0220  42  VAL   C CG1 
1391 C CG2 . VAL   B 36  ? 0.1557 0.1436 0.2158 0.0069  0.0212  0.0170  42  VAL   C CG2 
1392 N N   . SER   B 37  ? 0.1229 0.1186 0.2176 0.0046  0.0237  0.0314  43  SER   C N   
1393 C CA  . SER   B 37  ? 0.1228 0.1198 0.2294 0.0046  0.0263  0.0350  43  SER   C CA  
1394 C C   . SER   B 37  ? 0.1416 0.1367 0.2478 0.0045  0.0284  0.0356  43  SER   C C   
1395 O O   . SER   B 37  ? 0.1427 0.1361 0.2397 0.0044  0.0269  0.0338  43  SER   C O   
1396 C CB  . SER   B 37  ? 0.1307 0.1327 0.2454 0.0036  0.0217  0.0394  43  SER   C CB  
1397 O OG  . SER   B 37  ? 0.1549 0.1587 0.2646 0.0024  0.0163  0.0399  43  SER   C OG  
1398 N N   . SER   B 38  ? 0.1484 0.1436 0.2654 0.0049  0.0327  0.0381  44  SER   C N   
1399 C CA  . SER   B 38  ? 0.1560 0.1495 0.2747 0.0049  0.0357  0.0392  44  SER   C CA  
1400 C C   . SER   B 38  ? 0.1788 0.1769 0.3061 0.0030  0.0309  0.0428  44  SER   C C   
1401 O O   . SER   B 38  ? 0.1939 0.1965 0.3289 0.0022  0.0266  0.0454  44  SER   C O   
1402 C CB  . SER   B 38  ? 0.1905 0.1815 0.3169 0.0063  0.0434  0.0400  44  SER   C CB  
1403 O OG  . SER   B 38  ? 0.2492 0.2444 0.3902 0.0060  0.0430  0.0436  44  SER   C OG  
1404 N N   . THR   B 39  ? 0.1776 0.1741 0.3033 0.0023  0.0314  0.0430  45  THR   C N   
1405 C CA  . THR   B 39  ? 0.1857 0.1859 0.3193 0.0003  0.0266  0.0456  45  THR   C CA  
1406 C C   . THR   B 39  ? 0.2155 0.2148 0.3602 0.0001  0.0318  0.0481  45  THR   C C   
1407 O O   . THR   B 39  ? 0.2106 0.2051 0.3514 0.0017  0.0388  0.0472  45  THR   C O   
1408 C CB  . THR   B 39  ? 0.1951 0.1939 0.3171 -0.0007 0.0219  0.0434  45  THR   C CB  
1409 O OG1 . THR   B 39  ? 0.2099 0.2034 0.3238 0.0003  0.0267  0.0416  45  THR   C OG1 
1410 C CG2 . THR   B 39  ? 0.2128 0.2122 0.3240 -0.0004 0.0174  0.0410  45  THR   C CG2 
1411 N N   . THR   B 40  ? 0.2318 0.2357 0.3896 -0.0017 0.0280  0.0511  46  THR   C N   
1412 C CA  . THR   B 40  ? 0.2555 0.2591 0.4258 -0.0022 0.0325  0.0536  46  THR   C CA  
1413 C C   . THR   B 40  ? 0.2655 0.2655 0.4290 -0.0031 0.0328  0.0522  46  THR   C C   
1414 O O   . THR   B 40  ? 0.2965 0.2925 0.4612 -0.0023 0.0400  0.0529  46  THR   C O   
1415 C CB  . THR   B 40  ? 0.3052 0.3155 0.4941 -0.0038 0.0282  0.0573  46  THR   C CB  
1416 O OG1 . THR   B 40  ? 0.3604 0.3740 0.5464 -0.0058 0.0186  0.0567  46  THR   C OG1 
1417 C CG2 . THR   B 40  ? 0.3009 0.3140 0.4971 -0.0023 0.0294  0.0592  46  THR   C CG2 
1418 N N   . ALA   B 41  ? 0.2420 0.2429 0.3978 -0.0047 0.0254  0.0504  47  ALA   C N   
1419 C CA  . ALA   B 41  ? 0.2486 0.2459 0.3981 -0.0056 0.0252  0.0490  47  ALA   C CA  
1420 C C   . ALA   B 41  ? 0.2356 0.2274 0.3663 -0.0036 0.0276  0.0458  47  ALA   C C   
1421 O O   . ALA   B 41  ? 0.2262 0.2184 0.3479 -0.0025 0.0256  0.0439  47  ALA   C O   
1422 C CB  . ALA   B 41  ? 0.2630 0.2637 0.4141 -0.0082 0.0160  0.0484  47  ALA   C CB  
1423 N N   . GLN   B 42  ? 0.2320 0.2188 0.3572 -0.0031 0.0313  0.0454  48  GLN   C N   
1424 C CA  . GLN   B 42  ? 0.2388 0.2206 0.3466 -0.0011 0.0329  0.0427  48  GLN   C CA  
1425 C C   . GLN   B 42  ? 0.2326 0.2153 0.3320 -0.0023 0.0254  0.0403  48  GLN   C C   
1426 O O   . GLN   B 42  ? 0.2431 0.2276 0.3485 -0.0046 0.0209  0.0407  48  GLN   C O   
1427 C CB  . GLN   B 42  ? 0.2915 0.2673 0.3961 0.0002  0.0399  0.0438  48  GLN   C CB  
1428 C CG  . GLN   B 42  ? 0.3966 0.3696 0.5035 0.0024  0.0487  0.0454  48  GLN   C CG  
1429 C CD  . GLN   B 42  ? 0.5177 0.4842 0.6191 0.0041  0.0557  0.0467  48  GLN   C CD  
1430 O OE1 . GLN   B 42  ? 0.5625 0.5284 0.6739 0.0028  0.0580  0.0494  48  GLN   C OE1 
1431 N NE2 . GLN   B 42  ? 0.5526 0.5139 0.6379 0.0072  0.0590  0.0449  48  GLN   C NE2 
1432 N N   . GLY   B 43  ? 0.2099 0.1914 0.2963 -0.0006 0.0241  0.0376  49  GLY   C N   
1433 C CA  . GLY   B 43  ? 0.2040 0.1858 0.2812 -0.0011 0.0182  0.0351  49  GLY   C CA  
1434 C C   . GLY   B 43  ? 0.2074 0.1838 0.2740 0.0002  0.0202  0.0340  49  GLY   C C   
1435 O O   . GLY   B 43  ? 0.2394 0.2118 0.3033 0.0020  0.0262  0.0348  49  GLY   C O   
1436 N N   . CYS   B 44  ? 0.1848 0.1609 0.2448 -0.0003 0.0156  0.0321  50  CYS   C N   
1437 C CA  . CYS   B 44  ? 0.2044 0.1756 0.2560 0.0010  0.0170  0.0314  50  CYS   C CA  
1438 C C   . CYS   B 44  ? 0.2107 0.1808 0.2496 0.0028  0.0148  0.0287  50  CYS   C C   
1439 O O   . CYS   B 44  ? 0.2429 0.2092 0.2750 0.0039  0.0153  0.0282  50  CYS   C O   
1440 C CB  . CYS   B 44  ? 0.2115 0.1821 0.2689 -0.0014 0.0144  0.0319  50  CYS   C CB  
1441 S SG  . CYS   B 44  ? 0.2727 0.2446 0.3475 -0.0038 0.0172  0.0352  50  CYS   C SG  
1442 N N   . ASP   B 45  ? 0.1762 0.1497 0.2127 0.0032  0.0123  0.0271  51  ASP   C N   
1443 C CA  . ASP   B 45  ? 0.1763 0.1493 0.2025 0.0049  0.0103  0.0245  51  ASP   C CA  
1444 C C   . ASP   B 45  ? 0.1979 0.1674 0.2167 0.0077  0.0144  0.0241  51  ASP   C C   
1445 O O   . ASP   B 45  ? 0.2269 0.1956 0.2483 0.0083  0.0185  0.0251  51  ASP   C O   
1446 C CB  . ASP   B 45  ? 0.1883 0.1658 0.2154 0.0044  0.0071  0.0232  51  ASP   C CB  
1447 C CG  . ASP   B 45  ? 0.2208 0.2013 0.2520 0.0022  0.0025  0.0235  51  ASP   C CG  
1448 O OD1 . ASP   B 45  ? 0.2354 0.2141 0.2651 0.0014  0.0006  0.0232  51  ASP   C OD1 
1449 O OD2 . ASP   B 45  ? 0.1950 0.1792 0.2305 0.0014  0.0009  0.0240  51  ASP   C OD2 
1450 N N   . THR   B 46  ? 0.1828 0.1502 0.1922 0.0096  0.0132  0.0225  52  THR   C N   
1451 C CA  . THR   B 46  ? 0.1870 0.1513 0.1875 0.0126  0.0156  0.0216  52  THR   C CA  
1452 C C   . THR   B 46  ? 0.1822 0.1495 0.1788 0.0134  0.0122  0.0185  52  THR   C C   
1453 O O   . THR   B 46  ? 0.1897 0.1593 0.1859 0.0129  0.0084  0.0173  52  THR   C O   
1454 C CB  . THR   B 46  ? 0.2240 0.1837 0.2172 0.0145  0.0164  0.0224  52  THR   C CB  
1455 O OG1 . THR   B 46  ? 0.2504 0.2071 0.2486 0.0137  0.0202  0.0254  52  THR   C OG1 
1456 C CG2 . THR   B 46  ? 0.2541 0.2108 0.2364 0.0181  0.0177  0.0214  52  THR   C CG2 
1457 N N   . ILE   B 47  ? 0.1785 0.1456 0.1725 0.0147  0.0138  0.0170  53  ILE   C N   
1458 C CA  . ILE   B 47  ? 0.1774 0.1472 0.1687 0.0154  0.0107  0.0138  53  ILE   C CA  
1459 C C   . ILE   B 47  ? 0.1715 0.1388 0.1527 0.0182  0.0091  0.0123  53  ILE   C C   
1460 O O   . ILE   B 47  ? 0.1903 0.1531 0.1644 0.0205  0.0117  0.0130  53  ILE   C O   
1461 C CB  . ILE   B 47  ? 0.1919 0.1620 0.1848 0.0156  0.0128  0.0123  53  ILE   C CB  
1462 C CG1 . ILE   B 47  ? 0.2046 0.1767 0.2079 0.0133  0.0149  0.0143  53  ILE   C CG1 
1463 C CG2 . ILE   B 47  ? 0.2005 0.1735 0.1924 0.0159  0.0094  0.0088  53  ILE   C CG2 
1464 C CD1 . ILE   B 47  ? 0.2267 0.2036 0.2372 0.0110  0.0112  0.0151  53  ILE   C CD1 
1465 N N   . ALA   B 48  ? 0.1613 0.1316 0.1419 0.0184  0.0050  0.0104  54  ALA   C N   
1466 C CA  . ALA   B 48  ? 0.1659 0.1347 0.1384 0.0212  0.0028  0.0089  54  ALA   C CA  
1467 C C   . ALA   B 48  ? 0.1675 0.1354 0.1349 0.0230  0.0027  0.0062  54  ALA   C C   
1468 O O   . ALA   B 48  ? 0.1705 0.1408 0.1426 0.0217  0.0027  0.0042  54  ALA   C O   
1469 C CB  . ALA   B 48  ? 0.1614 0.1342 0.1365 0.0209  -0.0012 0.0074  54  ALA   C CB  
1470 N N   . ARG   B 49  ? 0.1713 0.1354 0.1287 0.0261  0.0025  0.0060  55  ARG   C N   
1471 C CA  . ARG   B 49  ? 0.1807 0.1433 0.1311 0.0282  0.0016  0.0029  55  ARG   C CA  
1472 C C   . ARG   B 49  ? 0.1835 0.1467 0.1278 0.0308  -0.0032 0.0016  55  ARG   C C   
1473 O O   . ARG   B 49  ? 0.2037 0.1630 0.1396 0.0336  -0.0027 0.0037  55  ARG   C O   
1474 C CB  . ARG   B 49  ? 0.2008 0.1575 0.1437 0.0299  0.0066  0.0043  55  ARG   C CB  
1475 C CG  . ARG   B 49  ? 0.1910 0.1475 0.1419 0.0273  0.0116  0.0062  55  ARG   C CG  
1476 C CD  . ARG   B 49  ? 0.2064 0.1664 0.1645 0.0253  0.0110  0.0031  55  ARG   C CD  
1477 N NE  . ARG   B 49  ? 0.2010 0.1607 0.1669 0.0233  0.0159  0.0055  55  ARG   C NE  
1478 C CZ  . ARG   B 49  ? 0.2027 0.1660 0.1783 0.0209  0.0160  0.0046  55  ARG   C CZ  
1479 N NH1 . ARG   B 49  ? 0.1896 0.1563 0.1678 0.0202  0.0122  0.0013  55  ARG   C NH1 
1480 N NH2 . ARG   B 49  ? 0.2179 0.1812 0.2014 0.0193  0.0200  0.0072  55  ARG   C NH2 
1481 N N   . CYS   B 50  ? 0.1794 0.1477 0.1293 0.0300  -0.0075 -0.0013 56  CYS   C N   
1482 C CA  . CYS   B 50  ? 0.1746 0.1449 0.1226 0.0320  -0.0124 -0.0023 56  CYS   C CA  
1483 C C   . CYS   B 50  ? 0.1728 0.1489 0.1290 0.0306  -0.0164 -0.0060 56  CYS   C C   
1484 O O   . CYS   B 50  ? 0.1808 0.1591 0.1440 0.0280  -0.0151 -0.0075 56  CYS   C O   
1485 C CB  . CYS   B 50  ? 0.1702 0.1407 0.1213 0.0316  -0.0115 0.0011  56  CYS   C CB  
1486 S SG  . CYS   B 50  ? 0.1747 0.1500 0.1385 0.0275  -0.0107 0.0014  56  CYS   C SG  
1487 N N   . ASP   B 51  ? 0.1840 0.1629 0.1407 0.0323  -0.0210 -0.0071 57  ASP   C N   
1488 C CA  . ASP   B 51  ? 0.1881 0.1729 0.1545 0.0310  -0.0244 -0.0101 57  ASP   C CA  
1489 C C   . ASP   B 51  ? 0.1906 0.1784 0.1631 0.0309  -0.0249 -0.0080 57  ASP   C C   
1490 O O   . ASP   B 51  ? 0.2027 0.1949 0.1816 0.0313  -0.0283 -0.0099 57  ASP   C O   
1491 C CB  . ASP   B 51  ? 0.2249 0.2110 0.1884 0.0331  -0.0299 -0.0141 57  ASP   C CB  
1492 C CG  . ASP   B 51  ? 0.2882 0.2732 0.2442 0.0369  -0.0335 -0.0131 57  ASP   C CG  
1493 O OD1 . ASP   B 51  ? 0.2800 0.2623 0.2323 0.0381  -0.0311 -0.0091 57  ASP   C OD1 
1494 O OD2 . ASP   B 51  ? 0.3734 0.3602 0.3276 0.0388  -0.0390 -0.0164 57  ASP   C OD2 
1495 N N   . CYS   B 52  ? 0.1782 0.1635 0.1496 0.0302  -0.0213 -0.0044 58  CYS   C N   
1496 C CA  . CYS   B 52  ? 0.1684 0.1557 0.1449 0.0300  -0.0212 -0.0029 58  CYS   C CA  
1497 C C   . CYS   B 52  ? 0.1575 0.1501 0.1445 0.0278  -0.0216 -0.0045 58  CYS   C C   
1498 O O   . CYS   B 52  ? 0.1629 0.1568 0.1540 0.0255  -0.0203 -0.0056 58  CYS   C O   
1499 C CB  . CYS   B 52  ? 0.1789 0.1627 0.1537 0.0288  -0.0173 0.0004  58  CYS   C CB  
1500 S SG  . CYS   B 52  ? 0.1824 0.1599 0.1471 0.0315  -0.0160 0.0033  58  CYS   C SG  
1501 N N   . GLN   B 53  ? 0.1485 0.1437 0.1400 0.0288  -0.0228 -0.0045 59  GLN   C N   
1502 C CA  . GLN   B 53  ? 0.1587 0.1584 0.1601 0.0271  -0.0220 -0.0051 59  GLN   C CA  
1503 C C   . GLN   B 53  ? 0.1541 0.1528 0.1560 0.0270  -0.0195 -0.0028 59  GLN   C C   
1504 O O   . GLN   B 53  ? 0.1546 0.1565 0.1636 0.0265  -0.0186 -0.0030 59  GLN   C O   
1505 C CB  . GLN   B 53  ? 0.1638 0.1683 0.1724 0.0282  -0.0257 -0.0078 59  GLN   C CB  
1506 C CG  . GLN   B 53  ? 0.2030 0.2087 0.2127 0.0274  -0.0281 -0.0110 59  GLN   C CG  
1507 C CD  . GLN   B 53  ? 0.2445 0.2556 0.2637 0.0279  -0.0318 -0.0140 59  GLN   C CD  
1508 O OE1 . GLN   B 53  ? 0.2615 0.2732 0.2781 0.0298  -0.0366 -0.0164 59  GLN   C OE1 
1509 N NE2 . GLN   B 53  ? 0.2080 0.2229 0.2382 0.0262  -0.0298 -0.0139 59  GLN   C NE2 
1510 N N   . THR   B 54  ? 0.1498 0.1438 0.1445 0.0276  -0.0181 -0.0007 60  THR   C N   
1511 C CA  . THR   B 54  ? 0.1602 0.1525 0.1549 0.0271  -0.0157 0.0009  60  THR   C CA  
1512 C C   . THR   B 54  ? 0.1605 0.1487 0.1503 0.0253  -0.0135 0.0026  60  THR   C C   
1513 O O   . THR   B 54  ? 0.1656 0.1511 0.1508 0.0255  -0.0136 0.0032  60  THR   C O   
1514 C CB  . THR   B 54  ? 0.2032 0.1940 0.1961 0.0299  -0.0163 0.0016  60  THR   C CB  
1515 O OG1 . THR   B 54  ? 0.2548 0.2415 0.2405 0.0315  -0.0170 0.0027  60  THR   C OG1 
1516 C CG2 . THR   B 54  ? 0.1965 0.1919 0.1956 0.0319  -0.0188 0.0000  60  THR   C CG2 
1517 N N   . GLY   B 55  ? 0.1494 0.1372 0.1405 0.0234  -0.0115 0.0034  61  GLY   C N   
1518 C CA  . GLY   B 55  ? 0.1548 0.1394 0.1429 0.0214  -0.0101 0.0048  61  GLY   C CA  
1519 C C   . GLY   B 55  ? 0.1414 0.1256 0.1301 0.0199  -0.0089 0.0052  61  GLY   C C   
1520 O O   . GLY   B 55  ? 0.1514 0.1364 0.1411 0.0210  -0.0084 0.0046  61  GLY   C O   
1521 N N   . VAL   B 56  ? 0.1340 0.1167 0.1218 0.0176  -0.0084 0.0063  62  VAL   C N   
1522 C CA  . VAL   B 56  ? 0.1186 0.1003 0.1054 0.0162  -0.0079 0.0065  62  VAL   C CA  
1523 C C   . VAL   B 56  ? 0.1177 0.1015 0.1071 0.0140  -0.0079 0.0076  62  VAL   C C   
1524 O O   . VAL   B 56  ? 0.1379 0.1215 0.1287 0.0130  -0.0081 0.0084  62  VAL   C O   
1525 C CB  . VAL   B 56  ? 0.1318 0.1086 0.1145 0.0158  -0.0080 0.0067  62  VAL   C CB  
1526 C CG1 . VAL   B 56  ? 0.1606 0.1360 0.1412 0.0141  -0.0083 0.0065  62  VAL   C CG1 
1527 C CG2 . VAL   B 56  ? 0.1529 0.1271 0.1332 0.0184  -0.0076 0.0059  62  VAL   C CG2 
1528 N N   . TYR   B 57  ? 0.1264 0.1120 0.1166 0.0133  -0.0074 0.0079  63  TYR   C N   
1529 C CA  . TYR   B 57  ? 0.1093 0.0967 0.1020 0.0114  -0.0077 0.0095  63  TYR   C CA  
1530 C C   . TYR   B 57  ? 0.1218 0.1075 0.1107 0.0103  -0.0084 0.0102  63  TYR   C C   
1531 O O   . TYR   B 57  ? 0.1408 0.1246 0.1254 0.0112  -0.0079 0.0093  63  TYR   C O   
1532 C CB  . TYR   B 57  ? 0.1202 0.1117 0.1183 0.0116  -0.0064 0.0099  63  TYR   C CB  
1533 C CG  . TYR   B 57  ? 0.1202 0.1128 0.1180 0.0122  -0.0049 0.0104  63  TYR   C CG  
1534 C CD1 . TYR   B 57  ? 0.1424 0.1350 0.1398 0.0140  -0.0037 0.0090  63  TYR   C CD1 
1535 C CD2 . TYR   B 57  ? 0.1286 0.1222 0.1268 0.0112  -0.0043 0.0125  63  TYR   C CD2 
1536 C CE1 . TYR   B 57  ? 0.1481 0.1416 0.1457 0.0147  -0.0014 0.0097  63  TYR   C CE1 
1537 C CE2 . TYR   B 57  ? 0.1386 0.1327 0.1359 0.0120  -0.0022 0.0133  63  TYR   C CE2 
1538 C CZ  . TYR   B 57  ? 0.1486 0.1425 0.1455 0.0138  -0.0004 0.0119  63  TYR   C CZ  
1539 O OH  . TYR   B 57  ? 0.1734 0.1676 0.1699 0.0148  0.0026  0.0129  63  TYR   C OH  
1540 N N   . TYR   B 58  ? 0.1276 0.1140 0.1183 0.0086  -0.0096 0.0119  64  TYR   C N   
1541 C CA  . TYR   B 58  ? 0.1318 0.1171 0.1188 0.0075  -0.0113 0.0126  64  TYR   C CA  
1542 C C   . TYR   B 58  ? 0.1415 0.1292 0.1288 0.0079  -0.0103 0.0144  64  TYR   C C   
1543 O O   . TYR   B 58  ? 0.1425 0.1333 0.1356 0.0075  -0.0096 0.0161  64  TYR   C O   
1544 C CB  . TYR   B 58  ? 0.1405 0.1255 0.1300 0.0055  -0.0137 0.0137  64  TYR   C CB  
1545 C CG  . TYR   B 58  ? 0.1564 0.1400 0.1414 0.0045  -0.0165 0.0140  64  TYR   C CG  
1546 C CD1 . TYR   B 58  ? 0.1678 0.1476 0.1457 0.0048  -0.0174 0.0118  64  TYR   C CD1 
1547 C CD2 . TYR   B 58  ? 0.1597 0.1458 0.1474 0.0034  -0.0184 0.0164  64  TYR   C CD2 
1548 C CE1 . TYR   B 58  ? 0.1757 0.1538 0.1481 0.0039  -0.0204 0.0115  64  TYR   C CE1 
1549 C CE2 . TYR   B 58  ? 0.1709 0.1557 0.1535 0.0027  -0.0217 0.0166  64  TYR   C CE2 
1550 C CZ  . TYR   B 58  ? 0.1807 0.1614 0.1552 0.0030  -0.0228 0.0139  64  TYR   C CZ  
1551 O OH  . TYR   B 58  ? 0.2179 0.1969 0.1858 0.0024  -0.0264 0.0135  64  TYR   C OH  
1552 N N   . CYS   B 59  ? 0.1376 0.1235 0.1185 0.0086  -0.0099 0.0140  65  CYS   C N   
1553 C CA  . CYS   B 59  ? 0.1367 0.1240 0.1161 0.0093  -0.0085 0.0161  65  CYS   C CA  
1554 C C   . CYS   B 59  ? 0.1557 0.1410 0.1284 0.0085  -0.0115 0.0171  65  CYS   C C   
1555 O O   . CYS   B 59  ? 0.1695 0.1512 0.1340 0.0090  -0.0122 0.0154  65  CYS   C O   
1556 C CB  . CYS   B 59  ? 0.1427 0.1290 0.1191 0.0113  -0.0051 0.0150  65  CYS   C CB  
1557 S SG  . CYS   B 59  ? 0.1817 0.1688 0.1556 0.0125  -0.0020 0.0179  65  CYS   C SG  
1558 N N   . SER   B 60  ? 0.1698 0.1574 0.1463 0.0074  -0.0135 0.0197  66  SER   C N   
1559 C CA  . SER   B 60  ? 0.1809 0.1673 0.1520 0.0066  -0.0175 0.0208  66  SER   C CA  
1560 C C   . SER   B 60  ? 0.1855 0.1697 0.1466 0.0082  -0.0166 0.0215  66  SER   C C   
1561 O O   . SER   B 60  ? 0.2085 0.1894 0.1609 0.0080  -0.0198 0.0201  66  SER   C O   
1562 C CB  . SER   B 60  ? 0.2130 0.2029 0.1915 0.0055  -0.0195 0.0240  66  SER   C CB  
1563 O OG  . SER   B 60  ? 0.2761 0.2650 0.2496 0.0048  -0.0242 0.0249  66  SER   C OG  
1564 N N   . SER   B 61  ? 0.1751 0.1605 0.1372 0.0099  -0.0120 0.0233  67  SER   C N   
1565 C CA  . SER   B 61  ? 0.1905 0.1735 0.1429 0.0118  -0.0100 0.0246  67  SER   C CA  
1566 C C   . SER   B 61  ? 0.2182 0.1966 0.1614 0.0130  -0.0084 0.0211  67  SER   C C   
1567 O O   . SER   B 61  ? 0.2504 0.2256 0.1832 0.0146  -0.0072 0.0216  67  SER   C O   
1568 C CB  . SER   B 61  ? 0.2061 0.1915 0.1634 0.0133  -0.0048 0.0279  67  SER   C CB  
1569 O OG  . SER   B 61  ? 0.2121 0.1988 0.1760 0.0137  -0.0009 0.0261  67  SER   C OG  
1570 N N   . ARG   B 62  ? 0.1942 0.1719 0.1406 0.0124  -0.0086 0.0177  68  ARG   C N   
1571 C CA  . ARG   B 62  ? 0.2088 0.1818 0.1474 0.0134  -0.0074 0.0142  68  ARG   C CA  
1572 C C   . ARG   B 62  ? 0.2090 0.1792 0.1454 0.0115  -0.0122 0.0110  68  ARG   C C   
1573 O O   . ARG   B 62  ? 0.2251 0.1910 0.1559 0.0121  -0.0117 0.0077  68  ARG   C O   
1574 C CB  . ARG   B 62  ? 0.2182 0.1924 0.1631 0.0147  -0.0029 0.0130  68  ARG   C CB  
1575 C CG  . ARG   B 62  ? 0.2568 0.2335 0.2052 0.0164  0.0022  0.0157  68  ARG   C CG  
1576 C CD  . ARG   B 62  ? 0.2662 0.2390 0.2043 0.0185  0.0057  0.0158  68  ARG   C CD  
1577 N NE  . ARG   B 62  ? 0.3122 0.2873 0.2546 0.0202  0.0114  0.0188  68  ARG   C NE  
1578 C CZ  . ARG   B 62  ? 0.3667 0.3430 0.3085 0.0205  0.0126  0.0228  68  ARG   C CZ  
1579 N NH1 . ARG   B 62  ? 0.3874 0.3633 0.3243 0.0194  0.0081  0.0244  68  ARG   C NH1 
1580 N NH2 . ARG   B 62  ? 0.3671 0.3451 0.3137 0.0221  0.0185  0.0254  68  ARG   C NH2 
1581 N N   . ARG   B 63  ? 0.2044 0.1770 0.1467 0.0093  -0.0164 0.0120  69  ARG   C N   
1582 C CA  . ARG   B 63  ? 0.2169 0.1875 0.1605 0.0073  -0.0205 0.0094  69  ARG   C CA  
1583 C C   . ARG   B 63  ? 0.2266 0.1951 0.1723 0.0078  -0.0180 0.0067  69  ARG   C C   
1584 O O   . ARG   B 63  ? 0.2556 0.2195 0.1970 0.0073  -0.0194 0.0035  69  ARG   C O   
1585 C CB  . ARG   B 63  ? 0.2417 0.2081 0.1753 0.0066  -0.0247 0.0074  69  ARG   C CB  
1586 C CG  . ARG   B 63  ? 0.2723 0.2409 0.2041 0.0061  -0.0286 0.0102  69  ARG   C CG  
1587 C CD  . ARG   B 63  ? 0.3268 0.2994 0.2693 0.0038  -0.0323 0.0119  69  ARG   C CD  
1588 N NE  . ARG   B 63  ? 0.3734 0.3471 0.3130 0.0031  -0.0376 0.0137  69  ARG   C NE  
1589 C CZ  . ARG   B 63  ? 0.3933 0.3707 0.3349 0.0040  -0.0375 0.0181  69  ARG   C CZ  
1590 N NH1 . ARG   B 63  ? 0.3656 0.3456 0.3121 0.0053  -0.0321 0.0208  69  ARG   C NH1 
1591 N NH2 . ARG   B 63  ? 0.4010 0.3794 0.3401 0.0035  -0.0430 0.0198  69  ARG   C NH2 
1592 N N   . LYS   B 64  ? 0.2058 0.1773 0.1581 0.0089  -0.0144 0.0078  70  LYS   C N   
1593 C CA  . LYS   B 64  ? 0.2093 0.1790 0.1631 0.0100  -0.0121 0.0057  70  LYS   C CA  
1594 C C   . LYS   B 64  ? 0.1867 0.1601 0.1495 0.0100  -0.0110 0.0069  70  LYS   C C   
1595 O O   . LYS   B 64  ? 0.1832 0.1608 0.1511 0.0100  -0.0103 0.0091  70  LYS   C O   
1596 C CB  . LYS   B 64  ? 0.2674 0.2359 0.2170 0.0125  -0.0080 0.0050  70  LYS   C CB  
1597 C CG  . LYS   B 64  ? 0.3927 0.3553 0.3318 0.0131  -0.0081 0.0024  70  LYS   C CG  
1598 C CD  . LYS   B 64  ? 0.5011 0.4619 0.4378 0.0159  -0.0032 0.0013  70  LYS   C CD  
1599 C CE  . LYS   B 64  ? 0.5789 0.5335 0.5041 0.0166  -0.0027 -0.0014 70  LYS   C CE  
1600 N NZ  . LYS   B 64  ? 0.6321 0.5860 0.5493 0.0162  -0.0044 -0.0002 70  LYS   C NZ  
1601 N N   . HIS   B 65  ? 0.1711 0.1426 0.1357 0.0103  -0.0109 0.0054  71  HIS   C N   
1602 C CA  . HIS   B 65  ? 0.1644 0.1384 0.1354 0.0110  -0.0098 0.0061  71  HIS   C CA  
1603 C C   . HIS   B 65  ? 0.1867 0.1608 0.1575 0.0135  -0.0070 0.0051  71  HIS   C C   
1604 O O   . HIS   B 65  ? 0.2266 0.1970 0.1933 0.0146  -0.0061 0.0034  71  HIS   C O   
1605 C CB  . HIS   B 65  ? 0.1729 0.1444 0.1456 0.0101  -0.0111 0.0057  71  HIS   C CB  
1606 C CG  . HIS   B 65  ? 0.1658 0.1379 0.1411 0.0075  -0.0135 0.0068  71  HIS   C CG  
1607 N ND1 . HIS   B 65  ? 0.2017 0.1767 0.1830 0.0068  -0.0134 0.0087  71  HIS   C ND1 
1608 C CD2 . HIS   B 65  ? 0.1658 0.1357 0.1387 0.0057  -0.0162 0.0062  71  HIS   C CD2 
1609 C CE1 . HIS   B 65  ? 0.1806 0.1553 0.1640 0.0046  -0.0156 0.0094  71  HIS   C CE1 
1610 N NE2 . HIS   B 65  ? 0.2016 0.1736 0.1805 0.0038  -0.0178 0.0080  71  HIS   C NE2 
1611 N N   . TYR   B 66  ? 0.1553 0.1337 0.1315 0.0145  -0.0056 0.0061  72  TYR   C N   
1612 C CA  . TYR   B 66  ? 0.1504 0.1298 0.1283 0.0168  -0.0034 0.0052  72  TYR   C CA  
1613 C C   . TYR   B 66  ? 0.1453 0.1265 0.1279 0.0179  -0.0041 0.0050  72  TYR   C C   
1614 O O   . TYR   B 66  ? 0.1444 0.1283 0.1308 0.0170  -0.0051 0.0057  72  TYR   C O   
1615 C CB  . TYR   B 66  ? 0.1636 0.1469 0.1451 0.0173  -0.0012 0.0063  72  TYR   C CB  
1616 C CG  . TYR   B 66  ? 0.1755 0.1568 0.1511 0.0172  0.0004  0.0069  72  TYR   C CG  
1617 C CD1 . TYR   B 66  ? 0.2041 0.1826 0.1756 0.0190  0.0030  0.0058  72  TYR   C CD1 
1618 C CD2 . TYR   B 66  ? 0.1881 0.1704 0.1627 0.0157  -0.0003 0.0088  72  TYR   C CD2 
1619 C CE1 . TYR   B 66  ? 0.2177 0.1938 0.1822 0.0192  0.0048  0.0063  72  TYR   C CE1 
1620 C CE2 . TYR   B 66  ? 0.1999 0.1802 0.1678 0.0160  0.0009  0.0096  72  TYR   C CE2 
1621 C CZ  . TYR   B 66  ? 0.2114 0.1885 0.1738 0.0178  0.0037  0.0083  72  TYR   C CZ  
1622 O OH  . TYR   B 66  ? 0.2489 0.2234 0.2032 0.0184  0.0052  0.0091  72  TYR   C OH  
1623 N N   . PRO   B 67  ? 0.1511 0.1308 0.1334 0.0200  -0.0036 0.0039  73  PRO   C N   
1624 C CA  . PRO   B 67  ? 0.1478 0.1295 0.1340 0.0215  -0.0047 0.0038  73  PRO   C CA  
1625 C C   . PRO   B 67  ? 0.1586 0.1456 0.1514 0.0223  -0.0040 0.0037  73  PRO   C C   
1626 O O   . PRO   B 67  ? 0.1884 0.1764 0.1830 0.0232  -0.0018 0.0035  73  PRO   C O   
1627 C CB  . PRO   B 67  ? 0.1763 0.1546 0.1602 0.0238  -0.0042 0.0031  73  PRO   C CB  
1628 C CG  . PRO   B 67  ? 0.2039 0.1793 0.1843 0.0238  -0.0021 0.0024  73  PRO   C CG  
1629 C CD  . PRO   B 67  ? 0.1620 0.1376 0.1399 0.0213  -0.0020 0.0028  73  PRO   C CD  
1630 N N   . VAL   B 68  ? 0.1365 0.1266 0.1332 0.0221  -0.0058 0.0036  74  VAL   C N   
1631 C CA  . VAL   B 68  ? 0.1360 0.1311 0.1403 0.0225  -0.0056 0.0030  74  VAL   C CA  
1632 C C   . VAL   B 68  ? 0.1377 0.1348 0.1446 0.0236  -0.0084 0.0019  74  VAL   C C   
1633 O O   . VAL   B 68  ? 0.1463 0.1413 0.1490 0.0236  -0.0101 0.0019  74  VAL   C O   
1634 C CB  . VAL   B 68  ? 0.1573 0.1544 0.1643 0.0201  -0.0046 0.0039  74  VAL   C CB  
1635 C CG1 . VAL   B 68  ? 0.1882 0.1842 0.1932 0.0194  -0.0018 0.0052  74  VAL   C CG1 
1636 C CG2 . VAL   B 68  ? 0.1697 0.1653 0.1737 0.0184  -0.0062 0.0044  74  VAL   C CG2 
1637 N N   . SER   B 69  ? 0.1289 0.1303 0.1435 0.0246  -0.0089 0.0008  75  SER   C N   
1638 C CA  . SER   B 69  ? 0.1382 0.1428 0.1570 0.0252  -0.0121 -0.0009 75  SER   C CA  
1639 C C   . SER   B 69  ? 0.1263 0.1334 0.1502 0.0228  -0.0114 -0.0014 75  SER   C C   
1640 O O   . SER   B 69  ? 0.1279 0.1363 0.1559 0.0216  -0.0085 -0.0004 75  SER   C O   
1641 C CB  . SER   B 69  ? 0.1703 0.1787 0.1966 0.0273  -0.0132 -0.0021 75  SER   C CB  
1642 O OG  . SER   B 69  ? 0.2262 0.2320 0.2482 0.0298  -0.0137 -0.0014 75  SER   C OG  
1643 N N   . PHE   B 70  ? 0.1227 0.1300 0.1458 0.0223  -0.0137 -0.0027 76  PHE   C N   
1644 C CA  . PHE   B 70  ? 0.1203 0.1293 0.1483 0.0201  -0.0130 -0.0033 76  PHE   C CA  
1645 C C   . PHE   B 70  ? 0.1226 0.1338 0.1542 0.0204  -0.0163 -0.0065 76  PHE   C C   
1646 O O   . PHE   B 70  ? 0.1371 0.1473 0.1639 0.0223  -0.0195 -0.0077 76  PHE   C O   
1647 C CB  . PHE   B 70  ? 0.1339 0.1396 0.1564 0.0183  -0.0112 -0.0015 76  PHE   C CB  
1648 C CG  . PHE   B 70  ? 0.1294 0.1315 0.1436 0.0190  -0.0126 -0.0015 76  PHE   C CG  
1649 C CD1 . PHE   B 70  ? 0.1375 0.1361 0.1451 0.0199  -0.0122 0.0001  76  PHE   C CD1 
1650 C CD2 . PHE   B 70  ? 0.1366 0.1380 0.1495 0.0188  -0.0138 -0.0030 76  PHE   C CD2 
1651 C CE1 . PHE   B 70  ? 0.1464 0.1414 0.1471 0.0206  -0.0128 0.0006  76  PHE   C CE1 
1652 C CE2 . PHE   B 70  ? 0.1434 0.1409 0.1484 0.0197  -0.0141 -0.0025 76  PHE   C CE2 
1653 C CZ  . PHE   B 70  ? 0.1460 0.1405 0.1453 0.0206  -0.0135 -0.0005 76  PHE   C CZ  
1654 N N   . SER   B 71  ? 0.1182 0.1322 0.1582 0.0187  -0.0157 -0.0077 77  SER   C N   
1655 C CA  . SER   B 71  ? 0.1286 0.1449 0.1735 0.0188  -0.0192 -0.0114 77  SER   C CA  
1656 C C   . SER   B 71  ? 0.1425 0.1556 0.1805 0.0185  -0.0205 -0.0130 77  SER   C C   
1657 O O   . SER   B 71  ? 0.1583 0.1678 0.1891 0.0180  -0.0184 -0.0108 77  SER   C O   
1658 C CB  . SER   B 71  ? 0.1310 0.1512 0.1889 0.0171  -0.0177 -0.0124 77  SER   C CB  
1659 O OG  . SER   B 71  ? 0.1599 0.1788 0.2191 0.0149  -0.0140 -0.0106 77  SER   C OG  
1660 N N   . LYS   B 72  ? 0.1596 0.1739 0.1998 0.0188  -0.0242 -0.0169 78  LYS   C N   
1661 C CA  . LYS   B 72  ? 0.1627 0.1736 0.1957 0.0187  -0.0251 -0.0189 78  LYS   C CA  
1662 C C   . LYS   B 72  ? 0.1643 0.1746 0.2028 0.0160  -0.0216 -0.0189 78  LYS   C C   
1663 O O   . LYS   B 72  ? 0.1755 0.1891 0.2251 0.0144  -0.0204 -0.0192 78  LYS   C O   
1664 C CB  . LYS   B 72  ? 0.2098 0.2219 0.2428 0.0200  -0.0307 -0.0237 78  LYS   C CB  
1665 C CG  . LYS   B 72  ? 0.2545 0.2670 0.2820 0.0231  -0.0345 -0.0233 78  LYS   C CG  
1666 C CD  . LYS   B 72  ? 0.3859 0.3994 0.4117 0.0247  -0.0409 -0.0280 78  LYS   C CD  
1667 C CE  . LYS   B 72  ? 0.4947 0.5090 0.5156 0.0280  -0.0450 -0.0272 78  LYS   C CE  
1668 N NZ  . LYS   B 72  ? 0.5605 0.5693 0.5654 0.0308  -0.0466 -0.0269 78  LYS   C NZ  
1669 N N   . PRO   B 73  ? 0.1593 0.1656 0.1911 0.0157  -0.0197 -0.0185 79  PRO   C N   
1670 C CA  . PRO   B 73  ? 0.1668 0.1726 0.2047 0.0133  -0.0161 -0.0181 79  PRO   C CA  
1671 C C   . PRO   B 73  ? 0.1709 0.1787 0.2180 0.0122  -0.0177 -0.0224 79  PRO   C C   
1672 O O   . PRO   B 73  ? 0.1992 0.2063 0.2434 0.0131  -0.0215 -0.0269 79  PRO   C O   
1673 C CB  . PRO   B 73  ? 0.1945 0.1956 0.2235 0.0138  -0.0144 -0.0177 79  PRO   C CB  
1674 C CG  . PRO   B 73  ? 0.2251 0.2239 0.2431 0.0161  -0.0164 -0.0171 79  PRO   C CG  
1675 C CD  . PRO   B 73  ? 0.1789 0.1808 0.1981 0.0175  -0.0201 -0.0179 79  PRO   C CD  
1676 N N   . SER   B 74  ? 0.1450 0.1554 0.2034 0.0102  -0.0150 -0.0211 80  SER   C N   
1677 C CA  . SER   B 74  ? 0.1613 0.1740 0.2311 0.0088  -0.0163 -0.0251 80  SER   C CA  
1678 C C   . SER   B 74  ? 0.1570 0.1699 0.2365 0.0067  -0.0115 -0.0229 80  SER   C C   
1679 O O   . SER   B 74  ? 0.1504 0.1623 0.2278 0.0064  -0.0078 -0.0181 80  SER   C O   
1680 C CB  . SER   B 74  ? 0.2107 0.2281 0.2879 0.0093  -0.0189 -0.0259 80  SER   C CB  
1681 O OG  . SER   B 74  ? 0.3080 0.3256 0.3767 0.0116  -0.0229 -0.0266 80  SER   C OG  
1682 N N   . LEU   B 75  ? 0.1561 0.1705 0.2470 0.0051  -0.0119 -0.0264 81  LEU   C N   
1683 C CA  . LEU   B 75  ? 0.1714 0.1861 0.2736 0.0031  -0.0074 -0.0244 81  LEU   C CA  
1684 C C   . LEU   B 75  ? 0.1777 0.1966 0.2894 0.0028  -0.0058 -0.0215 81  LEU   C C   
1685 O O   . LEU   B 75  ? 0.1997 0.2218 0.3196 0.0026  -0.0084 -0.0247 81  LEU   C O   
1686 C CB  . LEU   B 75  ? 0.1873 0.2009 0.2973 0.0016  -0.0086 -0.0302 81  LEU   C CB  
1687 C CG  . LEU   B 75  ? 0.2132 0.2261 0.3350 -0.0004 -0.0037 -0.0285 81  LEU   C CG  
1688 C CD1 . LEU   B 75  ? 0.2170 0.2260 0.3325 -0.0001 0.0001  -0.0251 81  LEU   C CD1 
1689 C CD2 . LEU   B 75  ? 0.2340 0.2462 0.3654 -0.0020 -0.0056 -0.0353 81  LEU   C CD2 
1690 N N   . ILE   B 76  ? 0.1709 0.1897 0.2809 0.0030  -0.0017 -0.0155 82  ILE   C N   
1691 C CA  . ILE   B 76  ? 0.1824 0.2042 0.2979 0.0033  0.0007  -0.0120 82  ILE   C CA  
1692 C C   . ILE   B 76  ? 0.1828 0.2043 0.3071 0.0021  0.0063  -0.0078 82  ILE   C C   
1693 O O   . ILE   B 76  ? 0.1718 0.1906 0.2921 0.0018  0.0084  -0.0051 82  ILE   C O   
1694 C CB  . ILE   B 76  ? 0.2142 0.2352 0.3172 0.0051  0.0006  -0.0084 82  ILE   C CB  
1695 C CG1 . ILE   B 76  ? 0.2493 0.2703 0.3437 0.0067  -0.0044 -0.0117 82  ILE   C CG1 
1696 C CG2 . ILE   B 76  ? 0.2301 0.2529 0.3362 0.0057  0.0042  -0.0039 82  ILE   C CG2 
1697 C CD1 . ILE   B 76  ? 0.2746 0.2994 0.3756 0.0074  -0.0068 -0.0138 82  ILE   C CD1 
1698 N N   . PHE   B 77  ? 0.1809 0.2052 0.3175 0.0015  0.0088  -0.0070 83  PHE   C N   
1699 C CA  . PHE   B 77  ? 0.1801 0.2038 0.3242 0.0008  0.0147  -0.0022 83  PHE   C CA  
1700 C C   . PHE   B 77  ? 0.1930 0.2159 0.3272 0.0024  0.0174  0.0039  83  PHE   C C   
1701 O O   . PHE   B 77  ? 0.2205 0.2451 0.3513 0.0037  0.0168  0.0043  83  PHE   C O   
1702 C CB  . PHE   B 77  ? 0.1795 0.2060 0.3404 -0.0004 0.0172  -0.0030 83  PHE   C CB  
1703 C CG  . PHE   B 77  ? 0.1937 0.2188 0.3631 -0.0012 0.0235  0.0018  83  PHE   C CG  
1704 C CD1 . PHE   B 77  ? 0.2085 0.2312 0.3830 -0.0026 0.0243  0.0006  83  PHE   C CD1 
1705 C CD2 . PHE   B 77  ? 0.2102 0.2357 0.3811 -0.0002 0.0289  0.0078  83  PHE   C CD2 
1706 C CE1 . PHE   B 77  ? 0.2288 0.2498 0.4109 -0.0031 0.0302  0.0056  83  PHE   C CE1 
1707 C CE2 . PHE   B 77  ? 0.2172 0.2410 0.3947 -0.0005 0.0347  0.0129  83  PHE   C CE2 
1708 C CZ  . PHE   B 77  ? 0.2197 0.2414 0.4033 -0.0020 0.0353  0.0119  83  PHE   C CZ  
1709 N N   . VAL   B 78  ? 0.1639 0.1843 0.2935 0.0025  0.0200  0.0084  84  VAL   C N   
1710 C CA  . VAL   B 78  ? 0.1653 0.1845 0.2846 0.0040  0.0218  0.0138  84  VAL   C CA  
1711 C C   . VAL   B 78  ? 0.1611 0.1798 0.2868 0.0041  0.0276  0.0194  84  VAL   C C   
1712 O O   . VAL   B 78  ? 0.1600 0.1776 0.2928 0.0031  0.0295  0.0204  84  VAL   C O   
1713 C CB  . VAL   B 78  ? 0.1785 0.1953 0.2869 0.0042  0.0193  0.0146  84  VAL   C CB  
1714 C CG1 . VAL   B 78  ? 0.1919 0.2074 0.2896 0.0055  0.0202  0.0196  84  VAL   C CG1 
1715 C CG2 . VAL   B 78  ? 0.1861 0.2027 0.2884 0.0042  0.0143  0.0094  84  VAL   C CG2 
1716 N N   . GLU   B 79  ? 0.1502 0.1690 0.2723 0.0055  0.0307  0.0232  85  GLU   C N   
1717 C CA  . GLU   B 79  ? 0.1506 0.1683 0.2763 0.0062  0.0365  0.0293  85  GLU   C CA  
1718 C C   . GLU   B 79  ? 0.1510 0.1660 0.2686 0.0067  0.0364  0.0338  85  GLU   C C   
1719 O O   . GLU   B 79  ? 0.1479 0.1622 0.2559 0.0067  0.0321  0.0326  85  GLU   C O   
1720 C CB  . GLU   B 79  ? 0.1941 0.2118 0.3153 0.0080  0.0399  0.0323  85  GLU   C CB  
1721 C CG  . GLU   B 79  ? 0.2682 0.2889 0.4013 0.0076  0.0417  0.0292  85  GLU   C CG  
1722 C CD  . GLU   B 79  ? 0.3900 0.4120 0.5410 0.0060  0.0451  0.0290  85  GLU   C CD  
1723 O OE1 . GLU   B 79  ? 0.4215 0.4417 0.5761 0.0062  0.0503  0.0343  85  GLU   C OE1 
1724 O OE2 . GLU   B 79  ? 0.4296 0.4543 0.5913 0.0044  0.0423  0.0235  85  GLU   C OE2 
1725 N N   . ALA   B 80  ? 0.1689 0.1827 0.2914 0.0071  0.0412  0.0392  86  ALA   C N   
1726 C CA  . ALA   B 80  ? 0.1842 0.1959 0.3004 0.0079  0.0410  0.0440  86  ALA   C CA  
1727 C C   . ALA   B 80  ? 0.2041 0.2147 0.3038 0.0095  0.0382  0.0462  86  ALA   C C   
1728 O O   . ALA   B 80  ? 0.2317 0.2421 0.3250 0.0107  0.0394  0.0466  86  ALA   C O   
1729 C CB  . ALA   B 80  ? 0.1992 0.2095 0.3224 0.0087  0.0471  0.0503  86  ALA   C CB  
1730 N N   . SER   B 81  ? 0.1994 0.2093 0.2930 0.0094  0.0344  0.0469  87  SER   C N   
1731 C CA  . SER   B 81  ? 0.2135 0.2222 0.2926 0.0106  0.0312  0.0488  87  SER   C CA  
1732 C C   . SER   B 81  ? 0.2358 0.2433 0.3127 0.0115  0.0313  0.0549  87  SER   C C   
1733 O O   . SER   B 81  ? 0.2319 0.2394 0.3189 0.0114  0.0344  0.0577  87  SER   C O   
1734 C CB  . SER   B 81  ? 0.2048 0.2141 0.2792 0.0095  0.0257  0.0437  87  SER   C CB  
1735 O OG  . SER   B 81  ? 0.1980 0.2076 0.2779 0.0084  0.0241  0.0435  87  SER   C OG  
1736 N N   . GLU   B 82  ? 0.2581 0.2647 0.3227 0.0125  0.0276  0.0567  88  GLU   C N   
1737 C CA  . GLU   B 82  ? 0.2692 0.2752 0.3320 0.0136  0.0266  0.0625  88  GLU   C CA  
1738 C C   . GLU   B 82  ? 0.2580 0.2652 0.3298 0.0122  0.0246  0.0618  88  GLU   C C   
1739 O O   . GLU   B 82  ? 0.2736 0.2806 0.3489 0.0131  0.0252  0.0668  88  GLU   C O   
1740 C CB  . GLU   B 82  ? 0.3348 0.3395 0.3823 0.0149  0.0227  0.0644  88  GLU   C CB  
1741 C CG  . GLU   B 82  ? 0.4282 0.4336 0.4704 0.0136  0.0165  0.0603  88  GLU   C CG  
1742 C CD  . GLU   B 82  ? 0.5138 0.5178 0.5425 0.0148  0.0123  0.0626  88  GLU   C CD  
1743 O OE1 . GLU   B 82  ? 0.5258 0.5276 0.5452 0.0166  0.0143  0.0647  88  GLU   C OE1 
1744 O OE2 . GLU   B 82  ? 0.5411 0.5460 0.5687 0.0140  0.0071  0.0624  88  GLU   C OE2 
1745 N N   . TYR   B 83  ? 0.2222 0.2305 0.2985 0.0104  0.0230  0.0558  89  TYR   C N   
1746 C CA  . TYR   B 83  ? 0.2060 0.2148 0.2894 0.0094  0.0215  0.0548  89  TYR   C CA  
1747 C C   . TYR   B 83  ? 0.2153 0.2242 0.3109 0.0080  0.0244  0.0509  89  TYR   C C   
1748 O O   . TYR   B 83  ? 0.2295 0.2383 0.3316 0.0074  0.0243  0.0504  89  TYR   C O   
1749 C CB  . TYR   B 83  ? 0.1950 0.2043 0.2713 0.0086  0.0163  0.0518  89  TYR   C CB  
1750 C CG  . TYR   B 83  ? 0.1864 0.1955 0.2559 0.0081  0.0148  0.0465  89  TYR   C CG  
1751 C CD1 . TYR   B 83  ? 0.1931 0.2015 0.2519 0.0090  0.0135  0.0472  89  TYR   C CD1 
1752 C CD2 . TYR   B 83  ? 0.1781 0.1875 0.2518 0.0069  0.0149  0.0410  89  TYR   C CD2 
1753 C CE1 . TYR   B 83  ? 0.1799 0.1880 0.2333 0.0087  0.0125  0.0427  89  TYR   C CE1 
1754 C CE2 . TYR   B 83  ? 0.1878 0.1971 0.2558 0.0068  0.0135  0.0368  89  TYR   C CE2 
1755 C CZ  . TYR   B 83  ? 0.1803 0.1890 0.2387 0.0077  0.0125  0.0377  89  TYR   C CZ  
1756 O OH  . TYR   B 83  ? 0.1953 0.2038 0.2487 0.0077  0.0114  0.0338  89  TYR   C OH  
1757 N N   . TYR   B 84  ? 0.1850 0.1941 0.2843 0.0075  0.0270  0.0479  90  TYR   C N   
1758 C CA  . TYR   B 84  ? 0.1720 0.1810 0.2833 0.0061  0.0294  0.0439  90  TYR   C CA  
1759 C C   . TYR   B 84  ? 0.1652 0.1744 0.2837 0.0062  0.0339  0.0448  90  TYR   C C   
1760 O O   . TYR   B 84  ? 0.1704 0.1800 0.2829 0.0071  0.0345  0.0462  90  TYR   C O   
1761 C CB  . TYR   B 84  ? 0.1636 0.1731 0.2730 0.0049  0.0264  0.0365  90  TYR   C CB  
1762 C CG  . TYR   B 84  ? 0.1502 0.1591 0.2557 0.0045  0.0232  0.0344  90  TYR   C CG  
1763 C CD1 . TYR   B 84  ? 0.1519 0.1598 0.2644 0.0042  0.0245  0.0351  90  TYR   C CD1 
1764 C CD2 . TYR   B 84  ? 0.1486 0.1577 0.2442 0.0046  0.0195  0.0320  90  TYR   C CD2 
1765 C CE1 . TYR   B 84  ? 0.1519 0.1591 0.2615 0.0040  0.0224  0.0334  90  TYR   C CE1 
1766 C CE2 . TYR   B 84  ? 0.1389 0.1473 0.2315 0.0044  0.0172  0.0304  90  TYR   C CE2 
1767 C CZ  . TYR   B 84  ? 0.1404 0.1479 0.2400 0.0041  0.0188  0.0312  90  TYR   C CZ  
1768 O OH  . TYR   B 84  ? 0.1379 0.1446 0.2352 0.0039  0.0174  0.0300  90  TYR   C OH  
1769 N N   . PRO   B 85  ? 0.1694 0.1781 0.3011 0.0051  0.0372  0.0436  91  PRO   C N   
1770 C CA  . PRO   B 85  ? 0.1566 0.1658 0.2969 0.0048  0.0414  0.0437  91  PRO   C CA  
1771 C C   . PRO   B 85  ? 0.1606 0.1716 0.3007 0.0037  0.0389  0.0368  91  PRO   C C   
1772 O O   . PRO   B 85  ? 0.1630 0.1744 0.2967 0.0033  0.0342  0.0321  91  PRO   C O   
1773 C CB  . PRO   B 85  ? 0.1689 0.1767 0.3240 0.0036  0.0447  0.0432  91  PRO   C CB  
1774 C CG  . PRO   B 85  ? 0.1815 0.1887 0.3352 0.0027  0.0410  0.0386  91  PRO   C CG  
1775 C CD  . PRO   B 85  ? 0.1775 0.1851 0.3173 0.0040  0.0373  0.0412  91  PRO   C CD  
1776 N N   . ALA   B 86  ? 0.1551 0.1672 0.3036 0.0033  0.0420  0.0361  92  ALA   C N   
1777 C CA  . ALA   B 86  ? 0.1719 0.1863 0.3233 0.0023  0.0395  0.0296  92  ALA   C CA  
1778 C C   . ALA   B 86  ? 0.1818 0.1958 0.3401 0.0005  0.0367  0.0232  92  ALA   C C   
1779 O O   . ALA   B 86  ? 0.1992 0.2117 0.3677 -0.0005 0.0394  0.0237  92  ALA   C O   
1780 C CB  . ALA   B 86  ? 0.1638 0.1795 0.3262 0.0021  0.0441  0.0307  92  ALA   C CB  
1781 N N   . ARG   B 87  ? 0.1689 0.1838 0.3205 0.0002  0.0314  0.0176  93  ARG   C N   
1782 C CA  . ARG   B 87  ? 0.1712 0.1851 0.3261 -0.0011 0.0286  0.0116  93  ARG   C CA  
1783 C C   . ARG   B 87  ? 0.1654 0.1804 0.3124 -0.0010 0.0231  0.0058  93  ARG   C C   
1784 O O   . ARG   B 87  ? 0.1634 0.1798 0.3018 0.0002  0.0215  0.0070  93  ARG   C O   
1785 C CB  . ARG   B 87  ? 0.1850 0.1961 0.3346 -0.0008 0.0288  0.0138  93  ARG   C CB  
1786 C CG  . ARG   B 87  ? 0.1722 0.1832 0.3067 0.0006  0.0258  0.0157  93  ARG   C CG  
1787 C CD  . ARG   B 87  ? 0.1728 0.1816 0.3040 0.0008  0.0257  0.0172  93  ARG   C CD  
1788 N NE  . ARG   B 87  ? 0.1767 0.1855 0.2951 0.0017  0.0222  0.0173  93  ARG   C NE  
1789 C CZ  . ARG   B 87  ? 0.1980 0.2051 0.3123 0.0018  0.0210  0.0162  93  ARG   C CZ  
1790 N NH1 . ARG   B 87  ? 0.1839 0.1890 0.3052 0.0012  0.0230  0.0151  93  ARG   C NH1 
1791 N NH2 . ARG   B 87  ? 0.2099 0.2169 0.3136 0.0025  0.0181  0.0161  93  ARG   C NH2 
1792 N N   . TYR   B 88  ? 0.1769 0.1909 0.3260 -0.0020 0.0202  -0.0004 94  TYR   C N   
1793 C CA  . TYR   B 88  ? 0.1945 0.2089 0.3344 -0.0014 0.0149  -0.0054 94  TYR   C CA  
1794 C C   . TYR   B 88  ? 0.1781 0.1900 0.3050 -0.0004 0.0138  -0.0039 94  TYR   C C   
1795 O O   . TYR   B 88  ? 0.1934 0.2027 0.3214 -0.0007 0.0158  -0.0029 94  TYR   C O   
1796 C CB  . TYR   B 88  ? 0.2245 0.2383 0.3703 -0.0027 0.0120  -0.0129 94  TYR   C CB  
1797 C CG  . TYR   B 88  ? 0.2555 0.2726 0.4141 -0.0038 0.0114  -0.0156 94  TYR   C CG  
1798 C CD1 . TYR   B 88  ? 0.2762 0.2965 0.4326 -0.0030 0.0075  -0.0178 94  TYR   C CD1 
1799 C CD2 . TYR   B 88  ? 0.2741 0.2911 0.4480 -0.0055 0.0151  -0.0154 94  TYR   C CD2 
1800 C CE1 . TYR   B 88  ? 0.2895 0.3134 0.4594 -0.0040 0.0071  -0.0199 94  TYR   C CE1 
1801 C CE2 . TYR   B 88  ? 0.2875 0.3078 0.4749 -0.0066 0.0150  -0.0175 94  TYR   C CE2 
1802 C CZ  . TYR   B 88  ? 0.3040 0.3279 0.4896 -0.0059 0.0108  -0.0199 94  TYR   C CZ  
1803 O OH  . TYR   B 88  ? 0.3344 0.3620 0.5354 -0.0071 0.0109  -0.0218 94  TYR   C OH  
1804 N N   . GLN   B 89  ? 0.1557 0.1682 0.2714 0.0009  0.0110  -0.0035 95  GLN   C N   
1805 C CA  . GLN   B 89  ? 0.1431 0.1533 0.2472 0.0018  0.0098  -0.0025 95  GLN   C CA  
1806 C C   . GLN   B 89  ? 0.1350 0.1445 0.2321 0.0025  0.0055  -0.0080 95  GLN   C C   
1807 O O   . GLN   B 89  ? 0.1459 0.1577 0.2429 0.0029  0.0028  -0.0103 95  GLN   C O   
1808 C CB  . GLN   B 89  ? 0.1597 0.1706 0.2565 0.0028  0.0103  0.0029  95  GLN   C CB  
1809 C CG  . GLN   B 89  ? 0.1681 0.1769 0.2550 0.0035  0.0092  0.0042  95  GLN   C CG  
1810 C CD  . GLN   B 89  ? 0.1546 0.1635 0.2365 0.0040  0.0100  0.0098  95  GLN   C CD  
1811 O OE1 . GLN   B 89  ? 0.1678 0.1776 0.2542 0.0039  0.0125  0.0139  95  GLN   C OE1 
1812 N NE2 . GLN   B 89  ? 0.1590 0.1670 0.2316 0.0047  0.0078  0.0099  95  GLN   C NE2 
1813 N N   . SER   B 90  ? 0.1307 0.1371 0.2221 0.0028  0.0050  -0.0100 96  SER   C N   
1814 C CA  . SER   B 90  ? 0.1404 0.1454 0.2238 0.0037  0.0013  -0.0149 96  SER   C CA  
1815 C C   . SER   B 90  ? 0.1358 0.1398 0.2069 0.0053  0.0001  -0.0125 96  SER   C C   
1816 O O   . SER   B 90  ? 0.1421 0.1459 0.2112 0.0053  0.0022  -0.0077 96  SER   C O   
1817 C CB  . SER   B 90  ? 0.1599 0.1613 0.2434 0.0034  0.0019  -0.0191 96  SER   C CB  
1818 O OG  . SER   B 90  ? 0.1756 0.1744 0.2556 0.0037  0.0051  -0.0157 96  SER   C OG  
1819 N N   . HIS   B 91  ? 0.1295 0.1327 0.1928 0.0066  -0.0035 -0.0160 97  HIS   C N   
1820 C CA  . HIS   B 91  ? 0.1282 0.1298 0.1800 0.0082  -0.0047 -0.0143 97  HIS   C CA  
1821 C C   . HIS   B 91  ? 0.1274 0.1313 0.1790 0.0083  -0.0041 -0.0097 97  HIS   C C   
1822 O O   . HIS   B 91  ? 0.1454 0.1476 0.1904 0.0088  -0.0033 -0.0066 97  HIS   C O   
1823 C CB  . HIS   B 91  ? 0.1455 0.1431 0.1915 0.0085  -0.0021 -0.0132 97  HIS   C CB  
1824 C CG  . HIS   B 91  ? 0.1715 0.1659 0.2155 0.0089  -0.0022 -0.0181 97  HIS   C CG  
1825 N ND1 . HIS   B 91  ? 0.2061 0.1975 0.2391 0.0107  -0.0043 -0.0209 97  HIS   C ND1 
1826 C CD2 . HIS   B 91  ? 0.1866 0.1800 0.2378 0.0077  -0.0005 -0.0206 97  HIS   C CD2 
1827 C CE1 . HIS   B 91  ? 0.2060 0.1946 0.2389 0.0107  -0.0038 -0.0252 97  HIS   C CE1 
1828 N NE2 . HIS   B 91  ? 0.2082 0.1978 0.2522 0.0088  -0.0015 -0.0254 97  HIS   C NE2 
1829 N N   . LEU   B 92  ? 0.1225 0.1298 0.1809 0.0079  -0.0046 -0.0096 98  LEU   C N   
1830 C CA  . LEU   B 92  ? 0.1170 0.1258 0.1750 0.0081  -0.0035 -0.0056 98  LEU   C CA  
1831 C C   . LEU   B 92  ? 0.1244 0.1347 0.1793 0.0095  -0.0065 -0.0072 98  LEU   C C   
1832 O O   . LEU   B 92  ? 0.1317 0.1438 0.1902 0.0099  -0.0091 -0.0110 98  LEU   C O   
1833 C CB  . LEU   B 92  ? 0.1329 0.1441 0.2015 0.0068  -0.0007 -0.0036 98  LEU   C CB  
1834 C CG  . LEU   B 92  ? 0.1505 0.1627 0.2176 0.0071  0.0012  0.0008  98  LEU   C CG  
1835 C CD1 . LEU   B 92  ? 0.1561 0.1661 0.2170 0.0070  0.0022  0.0046  98  LEU   C CD1 
1836 C CD2 . LEU   B 92  ? 0.1657 0.1800 0.2430 0.0063  0.0043  0.0027  98  LEU   C CD2 
1837 N N   . MET   B 93  ? 0.1189 0.1286 0.1674 0.0104  -0.0063 -0.0044 99  MET   C N   
1838 C CA  . MET   B 93  ? 0.1151 0.1258 0.1608 0.0121  -0.0085 -0.0052 99  MET   C CA  
1839 C C   . MET   B 93  ? 0.1210 0.1331 0.1689 0.0120  -0.0060 -0.0021 99  MET   C C   
1840 O O   . MET   B 93  ? 0.1372 0.1477 0.1821 0.0113  -0.0039 0.0011  99  MET   C O   
1841 C CB  . MET   B 93  ? 0.1369 0.1443 0.1716 0.0134  -0.0099 -0.0047 99  MET   C CB  
1842 C CG  . MET   B 93  ? 0.1656 0.1708 0.1962 0.0139  -0.0115 -0.0073 99  MET   C CG  
1843 S SD  . MET   B 93  ? 0.1717 0.1725 0.1904 0.0153  -0.0117 -0.0057 99  MET   C SD  
1844 C CE  . MET   B 93  ? 0.2011 0.2005 0.2204 0.0133  -0.0081 -0.0015 99  MET   C CE  
1845 N N   . LEU   B 94  ? 0.1115 0.1263 0.1644 0.0129  -0.0064 -0.0030 100 LEU   C N   
1846 C CA  . LEU   B 94  ? 0.1227 0.1382 0.1769 0.0132  -0.0033 -0.0001 100 LEU   C CA  
1847 C C   . LEU   B 94  ? 0.1173 0.1319 0.1654 0.0151  -0.0043 0.0000  100 LEU   C C   
1848 O O   . LEU   B 94  ? 0.1340 0.1490 0.1810 0.0165  -0.0074 -0.0023 100 LEU   C O   
1849 C CB  . LEU   B 94  ? 0.1272 0.1464 0.1936 0.0129  -0.0014 -0.0006 100 LEU   C CB  
1850 C CG  . LEU   B 94  ? 0.1439 0.1642 0.2190 0.0110  0.0004  -0.0006 100 LEU   C CG  
1851 C CD1 . LEU   B 94  ? 0.1765 0.2004 0.2645 0.0108  0.0025  -0.0009 100 LEU   C CD1 
1852 C CD2 . LEU   B 94  ? 0.1594 0.1774 0.2307 0.0101  0.0035  0.0034  100 LEU   C CD2 
1853 N N   . ALA   B 95  ? 0.1129 0.1259 0.1570 0.0154  -0.0016 0.0027  101 ALA   C N   
1854 C CA  . ALA   B 95  ? 0.1192 0.1310 0.1588 0.0172  -0.0013 0.0029  101 ALA   C CA  
1855 C C   . ALA   B 95  ? 0.1204 0.1325 0.1622 0.0175  0.0030  0.0051  101 ALA   C C   
1856 O O   . ALA   B 95  ? 0.1199 0.1322 0.1636 0.0163  0.0056  0.0072  101 ALA   C O   
1857 C CB  . ALA   B 95  ? 0.1340 0.1415 0.1625 0.0174  -0.0025 0.0037  101 ALA   C CB  
1858 N N   . VAL   B 96  ? 0.1299 0.1417 0.1708 0.0194  0.0042  0.0050  102 VAL   C N   
1859 C CA  . VAL   B 96  ? 0.1432 0.1542 0.1837 0.0201  0.0090  0.0071  102 VAL   C CA  
1860 C C   . VAL   B 96  ? 0.1514 0.1575 0.1792 0.0199  0.0092  0.0085  102 VAL   C C   
1861 O O   . VAL   B 96  ? 0.1643 0.1675 0.1853 0.0206  0.0072  0.0073  102 VAL   C O   
1862 C CB  . VAL   B 96  ? 0.1516 0.1640 0.1968 0.0223  0.0103  0.0061  102 VAL   C CB  
1863 C CG1 . VAL   B 96  ? 0.1753 0.1860 0.2186 0.0234  0.0160  0.0082  102 VAL   C CG1 
1864 C CG2 . VAL   B 96  ? 0.1598 0.1777 0.2188 0.0223  0.0091  0.0044  102 VAL   C CG2 
1865 N N   . GLY   B 97  ? 0.1553 0.1602 0.1803 0.0189  0.0115  0.0109  103 GLY   C N   
1866 C CA  . GLY   B 97  ? 0.1741 0.1746 0.1875 0.0186  0.0109  0.0120  103 GLY   C CA  
1867 C C   . GLY   B 97  ? 0.1812 0.1812 0.1926 0.0175  0.0124  0.0150  103 GLY   C C   
1868 O O   . GLY   B 97  ? 0.1992 0.2021 0.2186 0.0170  0.0144  0.0165  103 GLY   C O   
1869 N N   . HIS   B 98  ? 0.1841 0.1804 0.1850 0.0174  0.0117  0.0159  104 HIS   C N   
1870 C CA  . HIS   B 98  ? 0.1793 0.1749 0.1768 0.0169  0.0126  0.0191  104 HIS   C CA  
1871 C C   . HIS   B 98  ? 0.1710 0.1678 0.1705 0.0149  0.0092  0.0202  104 HIS   C C   
1872 O O   . HIS   B 98  ? 0.1710 0.1669 0.1686 0.0139  0.0055  0.0185  104 HIS   C O   
1873 C CB  . HIS   B 98  ? 0.2227 0.2136 0.2075 0.0177  0.0127  0.0193  104 HIS   C CB  
1874 C CG  . HIS   B 98  ? 0.2645 0.2543 0.2443 0.0178  0.0138  0.0229  104 HIS   C CG  
1875 N ND1 . HIS   B 98  ? 0.2892 0.2799 0.2721 0.0191  0.0190  0.0258  104 HIS   C ND1 
1876 C CD2 . HIS   B 98  ? 0.3014 0.2897 0.2746 0.0169  0.0103  0.0242  104 HIS   C CD2 
1877 C CE1 . HIS   B 98  ? 0.3218 0.3111 0.2983 0.0191  0.0185  0.0290  104 HIS   C CE1 
1878 N NE2 . HIS   B 98  ? 0.3323 0.3203 0.3030 0.0178  0.0129  0.0281  104 HIS   C NE2 
1879 N N   . SER   B 99  ? 0.1695 0.1680 0.1734 0.0145  0.0109  0.0232  105 SER   C N   
1880 C CA  . SER   B 99  ? 0.1757 0.1752 0.1823 0.0129  0.0082  0.0246  105 SER   C CA  
1881 C C   . SER   B 99  ? 0.2046 0.2043 0.2116 0.0132  0.0105  0.0290  105 SER   C C   
1882 O O   . SER   B 99  ? 0.2265 0.2278 0.2404 0.0137  0.0145  0.0304  105 SER   C O   
1883 C CB  . SER   B 99  ? 0.1917 0.1942 0.2088 0.0119  0.0078  0.0227  105 SER   C CB  
1884 O OG  . SER   B 99  ? 0.2057 0.2093 0.2269 0.0106  0.0064  0.0241  105 SER   C OG  
1885 N N   . GLU   B 100 ? 0.2074 0.2057 0.2079 0.0129  0.0078  0.0313  106 GLU   C N   
1886 C CA  . GLU   B 100 ? 0.2055 0.2038 0.2051 0.0134  0.0090  0.0361  106 GLU   C CA  
1887 C C   . GLU   B 100 ? 0.1836 0.1841 0.1909 0.0118  0.0064  0.0372  106 GLU   C C   
1888 O O   . GLU   B 100 ? 0.1722 0.1732 0.1816 0.0105  0.0034  0.0344  106 GLU   C O   
1889 C CB  . GLU   B 100 ? 0.2441 0.2391 0.2303 0.0142  0.0063  0.0376  106 GLU   C CB  
1890 C CG  . GLU   B 100 ? 0.3359 0.3274 0.3114 0.0157  0.0076  0.0357  106 GLU   C CG  
1891 C CD  . GLU   B 100 ? 0.4271 0.4167 0.3972 0.0179  0.0127  0.0388  106 GLU   C CD  
1892 O OE1 . GLU   B 100 ? 0.4506 0.4369 0.4118 0.0193  0.0145  0.0371  106 GLU   C OE1 
1893 O OE2 . GLU   B 100 ? 0.4404 0.4315 0.4157 0.0184  0.0155  0.0430  106 GLU   C OE2 
1894 N N   . PRO   B 101 ? 0.1864 0.1878 0.1974 0.0122  0.0077  0.0415  107 PRO   C N   
1895 C CA  . PRO   B 101 ? 0.1696 0.1729 0.1885 0.0109  0.0056  0.0426  107 PRO   C CA  
1896 C C   . PRO   B 101 ? 0.1823 0.1852 0.1969 0.0098  0.0002  0.0414  107 PRO   C C   
1897 O O   . PRO   B 101 ? 0.1811 0.1853 0.2022 0.0085  -0.0012 0.0397  107 PRO   C O   
1898 C CB  . PRO   B 101 ? 0.1945 0.1981 0.2153 0.0120  0.0076  0.0483  107 PRO   C CB  
1899 C CG  . PRO   B 101 ? 0.2312 0.2335 0.2492 0.0136  0.0125  0.0497  107 PRO   C CG  
1900 C CD  . PRO   B 101 ? 0.2133 0.2139 0.2228 0.0139  0.0120  0.0458  107 PRO   C CD  
1901 N N   . GLY   B 102 ? 0.1708 0.1717 0.1747 0.0103  -0.0028 0.0419  108 GLY   C N   
1902 C CA  . GLY   B 102 ? 0.1688 0.1695 0.1701 0.0091  -0.0082 0.0408  108 GLY   C CA  
1903 C C   . GLY   B 102 ? 0.1586 0.1586 0.1604 0.0079  -0.0092 0.0359  108 GLY   C C   
1904 O O   . GLY   B 102 ? 0.1825 0.1823 0.1844 0.0066  -0.0130 0.0348  108 GLY   C O   
1905 N N   . ASP   B 103 ? 0.1457 0.1451 0.1474 0.0084  -0.0060 0.0332  109 ASP   C N   
1906 C CA  . ASP   B 103 ? 0.1410 0.1396 0.1430 0.0077  -0.0067 0.0291  109 ASP   C CA  
1907 C C   . ASP   B 103 ? 0.1421 0.1426 0.1533 0.0067  -0.0062 0.0282  109 ASP   C C   
1908 O O   . ASP   B 103 ? 0.1386 0.1382 0.1497 0.0062  -0.0071 0.0254  109 ASP   C O   
1909 C CB  . ASP   B 103 ? 0.1610 0.1585 0.1601 0.0090  -0.0038 0.0267  109 ASP   C CB  
1910 C CG  . ASP   B 103 ? 0.1803 0.1748 0.1688 0.0100  -0.0041 0.0266  109 ASP   C CG  
1911 O OD1 . ASP   B 103 ? 0.1872 0.1798 0.1698 0.0093  -0.0077 0.0261  109 ASP   C OD1 
1912 O OD2 . ASP   B 103 ? 0.2055 0.1995 0.1921 0.0115  -0.0005 0.0269  109 ASP   C OD2 
1913 N N   . CYS   B 104 ? 0.1362 0.1388 0.1552 0.0066  -0.0044 0.0305  110 CYS   C N   
1914 C CA  . CYS   B 104 ? 0.1298 0.1336 0.1569 0.0058  -0.0036 0.0293  110 CYS   C CA  
1915 C C   . CYS   B 104 ? 0.1344 0.1376 0.1613 0.0048  -0.0063 0.0289  110 CYS   C C   
1916 O O   . CYS   B 104 ? 0.1517 0.1549 0.1770 0.0043  -0.0091 0.0311  110 CYS   C O   
1917 C CB  . CYS   B 104 ? 0.1383 0.1439 0.1736 0.0059  -0.0014 0.0322  110 CYS   C CB  
1918 S SG  . CYS   B 104 ? 0.1520 0.1585 0.1915 0.0067  0.0029  0.0320  110 CYS   C SG  
1919 N N   . GLY   B 105 ? 0.1104 0.1129 0.1390 0.0045  -0.0057 0.0261  111 GLY   C N   
1920 C CA  . GLY   B 105 ? 0.1294 0.1309 0.1588 0.0036  -0.0072 0.0259  111 GLY   C CA  
1921 C C   . GLY   B 105 ? 0.1336 0.1327 0.1562 0.0036  -0.0087 0.0234  111 GLY   C C   
1922 O O   . GLY   B 105 ? 0.1453 0.1431 0.1688 0.0030  -0.0092 0.0228  111 GLY   C O   
1923 N N   . GLY   B 106 ? 0.1292 0.1273 0.1455 0.0044  -0.0091 0.0222  112 GLY   C N   
1924 C CA  . GLY   B 106 ? 0.1352 0.1306 0.1454 0.0047  -0.0101 0.0198  112 GLY   C CA  
1925 C C   . GLY   B 106 ? 0.1257 0.1202 0.1368 0.0053  -0.0086 0.0177  112 GLY   C C   
1926 O O   . GLY   B 106 ? 0.1263 0.1222 0.1403 0.0061  -0.0068 0.0169  112 GLY   C O   
1927 N N   . ILE   B 107 ? 0.1215 0.1134 0.1301 0.0051  -0.0093 0.0167  113 ILE   C N   
1928 C CA  . ILE   B 107 ? 0.1205 0.1110 0.1288 0.0061  -0.0079 0.0152  113 ILE   C CA  
1929 C C   . ILE   B 107 ? 0.1206 0.1103 0.1244 0.0078  -0.0077 0.0130  113 ILE   C C   
1930 O O   . ILE   B 107 ? 0.1327 0.1209 0.1323 0.0081  -0.0086 0.0125  113 ILE   C O   
1931 C CB  . ILE   B 107 ? 0.1530 0.1408 0.1612 0.0053  -0.0081 0.0157  113 ILE   C CB  
1932 C CG1 . ILE   B 107 ? 0.1954 0.1847 0.2106 0.0042  -0.0069 0.0177  113 ILE   C CG1 
1933 C CG2 . ILE   B 107 ? 0.1571 0.1420 0.1616 0.0068  -0.0068 0.0143  113 ILE   C CG2 
1934 C CD1 . ILE   B 107 ? 0.2545 0.2419 0.2727 0.0031  -0.0066 0.0190  113 ILE   C CD1 
1935 N N   . LEU   B 108 ? 0.1166 0.1070 0.1213 0.0091  -0.0067 0.0116  114 LEU   C N   
1936 C CA  . LEU   B 108 ? 0.1122 0.1018 0.1135 0.0110  -0.0069 0.0097  114 LEU   C CA  
1937 C C   . LEU   B 108 ? 0.1267 0.1132 0.1248 0.0118  -0.0066 0.0095  114 LEU   C C   
1938 O O   . LEU   B 108 ? 0.1255 0.1118 0.1251 0.0117  -0.0056 0.0098  114 LEU   C O   
1939 C CB  . LEU   B 108 ? 0.1119 0.1046 0.1168 0.0118  -0.0067 0.0082  114 LEU   C CB  
1940 C CG  . LEU   B 108 ? 0.1268 0.1195 0.1297 0.0139  -0.0076 0.0061  114 LEU   C CG  
1941 C CD1 . LEU   B 108 ? 0.1520 0.1445 0.1530 0.0149  -0.0079 0.0060  114 LEU   C CD1 
1942 C CD2 . LEU   B 108 ? 0.1314 0.1272 0.1393 0.0142  -0.0079 0.0043  114 LEU   C CD2 
1943 N N   . ARG   B 109 ? 0.1294 0.1131 0.1231 0.0129  -0.0071 0.0093  115 ARG   C N   
1944 C CA  . ARG   B 109 ? 0.1370 0.1170 0.1272 0.0140  -0.0063 0.0098  115 ARG   C CA  
1945 C C   . ARG   B 109 ? 0.1461 0.1249 0.1321 0.0166  -0.0071 0.0087  115 ARG   C C   
1946 O O   . ARG   B 109 ? 0.1490 0.1285 0.1347 0.0173  -0.0079 0.0079  115 ARG   C O   
1947 C CB  . ARG   B 109 ? 0.1772 0.1541 0.1673 0.0124  -0.0059 0.0113  115 ARG   C CB  
1948 C CG  . ARG   B 109 ? 0.2147 0.1904 0.2028 0.0123  -0.0071 0.0106  115 ARG   C CG  
1949 C CD  . ARG   B 109 ? 0.2778 0.2503 0.2664 0.0106  -0.0072 0.0114  115 ARG   C CD  
1950 N NE  . ARG   B 109 ? 0.3387 0.3134 0.3313 0.0081  -0.0083 0.0121  115 ARG   C NE  
1951 C CZ  . ARG   B 109 ? 0.4038 0.3777 0.4004 0.0062  -0.0083 0.0135  115 ARG   C CZ  
1952 N NH1 . ARG   B 109 ? 0.4286 0.3993 0.4259 0.0064  -0.0065 0.0144  115 ARG   C NH1 
1953 N NH2 . ARG   B 109 ? 0.4122 0.3886 0.4126 0.0042  -0.0100 0.0142  115 ARG   C NH2 
1954 N N   . CYS   B 110 ? 0.1478 0.1244 0.1303 0.0184  -0.0065 0.0089  116 CYS   C N   
1955 C CA  . CYS   B 110 ? 0.1538 0.1286 0.1316 0.0213  -0.0075 0.0085  116 CYS   C CA  
1956 C C   . CYS   B 110 ? 0.1747 0.1442 0.1483 0.0221  -0.0056 0.0107  116 CYS   C C   
1957 O O   . CYS   B 110 ? 0.1749 0.1426 0.1504 0.0201  -0.0037 0.0121  116 CYS   C O   
1958 C CB  . CYS   B 110 ? 0.1447 0.1217 0.1211 0.0232  -0.0091 0.0068  116 CYS   C CB  
1959 S SG  . CYS   B 110 ? 0.1602 0.1349 0.1331 0.0234  -0.0073 0.0072  116 CYS   C SG  
1960 N N   . GLN   B 111 ? 0.1956 0.1625 0.1640 0.0251  -0.0060 0.0112  117 GLN   C N   
1961 C CA  . GLN   B 111 ? 0.2147 0.1761 0.1792 0.0261  -0.0035 0.0137  117 GLN   C CA  
1962 C C   . GLN   B 111 ? 0.2217 0.1812 0.1845 0.0258  -0.0009 0.0150  117 GLN   C C   
1963 O O   . GLN   B 111 ? 0.2450 0.2002 0.2070 0.0257  0.0022  0.0174  117 GLN   C O   
1964 C CB  . GLN   B 111 ? 0.2317 0.1904 0.1905 0.0300  -0.0043 0.0146  117 GLN   C CB  
1965 C CG  . GLN   B 111 ? 0.2693 0.2294 0.2230 0.0327  -0.0062 0.0137  117 GLN   C CG  
1966 C CD  . GLN   B 111 ? 0.4002 0.3582 0.3483 0.0368  -0.0079 0.0148  117 GLN   C CD  
1967 O OE1 . GLN   B 111 ? 0.4449 0.4061 0.3951 0.0381  -0.0110 0.0134  117 GLN   C OE1 
1968 N NE2 . GLN   B 111 ? 0.4332 0.3858 0.3744 0.0391  -0.0057 0.0177  117 GLN   C NE2 
1969 N N   . HIS   B 112 ? 0.1921 0.1547 0.1550 0.0257  -0.0016 0.0133  118 HIS   C N   
1970 C CA  . HIS   B 112 ? 0.1943 0.1548 0.1552 0.0257  0.0013  0.0141  118 HIS   C CA  
1971 C C   . HIS   B 112 ? 0.1941 0.1561 0.1624 0.0223  0.0033  0.0147  118 HIS   C C   
1972 O O   . HIS   B 112 ? 0.2137 0.1736 0.1817 0.0223  0.0067  0.0159  118 HIS   C O   
1973 C CB  . HIS   B 112 ? 0.2024 0.1644 0.1587 0.0277  -0.0005 0.0117  118 HIS   C CB  
1974 C CG  . HIS   B 112 ? 0.1909 0.1520 0.1403 0.0312  -0.0034 0.0112  118 HIS   C CG  
1975 N ND1 . HIS   B 112 ? 0.1916 0.1571 0.1433 0.0317  -0.0077 0.0087  118 HIS   C ND1 
1976 C CD2 . HIS   B 112 ? 0.2355 0.1918 0.1760 0.0345  -0.0024 0.0131  118 HIS   C CD2 
1977 C CE1 . HIS   B 112 ? 0.2237 0.1873 0.1686 0.0353  -0.0097 0.0092  118 HIS   C CE1 
1978 N NE2 . HIS   B 112 ? 0.2494 0.2073 0.1868 0.0371  -0.0067 0.0118  118 HIS   C NE2 
1979 N N   . GLY   B 113 ? 0.1753 0.1410 0.1501 0.0198  0.0014  0.0139  119 GLY   C N   
1980 C CA  . GLY   B 113 ? 0.1751 0.1427 0.1571 0.0169  0.0026  0.0146  119 GLY   C CA  
1981 C C   . GLY   B 113 ? 0.1568 0.1294 0.1434 0.0154  0.0002  0.0128  119 GLY   C C   
1982 O O   . GLY   B 113 ? 0.1542 0.1288 0.1398 0.0160  -0.0023 0.0113  119 GLY   C O   
1983 N N   . VAL   B 114 ? 0.1500 0.1246 0.1423 0.0135  0.0013  0.0134  120 VAL   C N   
1984 C CA  . VAL   B 114 ? 0.1446 0.1236 0.1419 0.0121  -0.0004 0.0124  120 VAL   C CA  
1985 C C   . VAL   B 114 ? 0.1416 0.1222 0.1376 0.0134  -0.0008 0.0100  120 VAL   C C   
1986 O O   . VAL   B 114 ? 0.1526 0.1317 0.1470 0.0143  0.0010  0.0094  120 VAL   C O   
1987 C CB  . VAL   B 114 ? 0.1583 0.1386 0.1627 0.0099  0.0010  0.0143  120 VAL   C CB  
1988 C CG1 . VAL   B 114 ? 0.1674 0.1519 0.1765 0.0088  -0.0004 0.0139  120 VAL   C CG1 
1989 C CG2 . VAL   B 114 ? 0.1822 0.1614 0.1891 0.0082  0.0004  0.0163  120 VAL   C CG2 
1990 N N   . VAL   B 115 ? 0.1258 0.1093 0.1226 0.0136  -0.0031 0.0085  121 VAL   C N   
1991 C CA  . VAL   B 115 ? 0.1334 0.1191 0.1309 0.0145  -0.0042 0.0058  121 VAL   C CA  
1992 C C   . VAL   B 115 ? 0.1407 0.1293 0.1454 0.0128  -0.0034 0.0057  121 VAL   C C   
1993 O O   . VAL   B 115 ? 0.1446 0.1336 0.1507 0.0131  -0.0030 0.0036  121 VAL   C O   
1994 C CB  . VAL   B 115 ? 0.1310 0.1184 0.1274 0.0157  -0.0066 0.0045  121 VAL   C CB  
1995 C CG1 . VAL   B 115 ? 0.1489 0.1392 0.1483 0.0162  -0.0081 0.0016  121 VAL   C CG1 
1996 C CG2 . VAL   B 115 ? 0.1523 0.1366 0.1419 0.0178  -0.0074 0.0048  121 VAL   C CG2 
1997 N N   . GLY   B 116 ? 0.1278 0.1181 0.1366 0.0111  -0.0033 0.0077  122 GLY   C N   
1998 C CA  . GLY   B 116 ? 0.1418 0.1348 0.1575 0.0097  -0.0025 0.0083  122 GLY   C CA  
1999 C C   . GLY   B 116 ? 0.1261 0.1205 0.1438 0.0084  -0.0030 0.0109  122 GLY   C C   
2000 O O   . GLY   B 116 ? 0.1305 0.1234 0.1445 0.0083  -0.0040 0.0119  122 GLY   C O   
2001 N N   . ILE   B 117 ? 0.1098 0.1067 0.1334 0.0075  -0.0023 0.0121  123 ILE   C N   
2002 C CA  . ILE   B 117 ? 0.1135 0.1115 0.1380 0.0066  -0.0030 0.0148  123 ILE   C CA  
2003 C C   . ILE   B 117 ? 0.1114 0.1117 0.1384 0.0068  -0.0025 0.0149  123 ILE   C C   
2004 O O   . ILE   B 117 ? 0.1244 0.1261 0.1562 0.0070  -0.0013 0.0136  123 ILE   C O   
2005 C CB  . ILE   B 117 ? 0.1217 0.1202 0.1511 0.0054  -0.0025 0.0176  123 ILE   C CB  
2006 C CG1 . ILE   B 117 ? 0.1388 0.1383 0.1748 0.0053  -0.0002 0.0174  123 ILE   C CG1 
2007 C CG2 . ILE   B 117 ? 0.1491 0.1455 0.1769 0.0049  -0.0029 0.0183  123 ILE   C CG2 
2008 C CD1 . ILE   B 117 ? 0.1419 0.1424 0.1846 0.0043  0.0006  0.0208  123 ILE   C CD1 
2009 N N   . VAL   B 118 ? 0.1089 0.1094 0.1331 0.0068  -0.0032 0.0166  124 VAL   C N   
2010 C CA  . VAL   B 118 ? 0.1104 0.1127 0.1366 0.0072  -0.0019 0.0175  124 VAL   C CA  
2011 C C   . VAL   B 118 ? 0.1190 0.1230 0.1527 0.0065  -0.0002 0.0195  124 VAL   C C   
2012 O O   . VAL   B 118 ? 0.1134 0.1173 0.1488 0.0057  -0.0006 0.0218  124 VAL   C O   
2013 C CB  . VAL   B 118 ? 0.1112 0.1126 0.1316 0.0074  -0.0026 0.0193  124 VAL   C CB  
2014 C CG1 . VAL   B 118 ? 0.1203 0.1230 0.1423 0.0080  -0.0004 0.0211  124 VAL   C CG1 
2015 C CG2 . VAL   B 118 ? 0.1351 0.1343 0.1486 0.0081  -0.0039 0.0172  124 VAL   C CG2 
2016 N N   . SER   B 119 ? 0.1105 0.1160 0.1497 0.0068  0.0018  0.0186  125 SER   C N   
2017 C CA  . SER   B 119 ? 0.1120 0.1189 0.1594 0.0062  0.0040  0.0204  125 SER   C CA  
2018 C C   . SER   B 119 ? 0.1299 0.1381 0.1811 0.0066  0.0065  0.0220  125 SER   C C   
2019 O O   . SER   B 119 ? 0.1252 0.1339 0.1814 0.0064  0.0084  0.0251  125 SER   C O   
2020 C CB  . SER   B 119 ? 0.1263 0.1330 0.1787 0.0058  0.0044  0.0171  125 SER   C CB  
2021 O OG  . SER   B 119 ? 0.1413 0.1488 0.2024 0.0053  0.0068  0.0182  125 SER   C OG  
2022 N N   . THR   B 120 ? 0.1242 0.1329 0.1739 0.0074  0.0069  0.0201  126 THR   C N   
2023 C CA  . THR   B 120 ? 0.1179 0.1279 0.1726 0.0078  0.0101  0.0218  126 THR   C CA  
2024 C C   . THR   B 120 ? 0.1208 0.1301 0.1686 0.0091  0.0105  0.0223  126 THR   C C   
2025 O O   . THR   B 120 ? 0.1263 0.1345 0.1668 0.0095  0.0081  0.0204  126 THR   C O   
2026 C CB  . THR   B 120 ? 0.1241 0.1359 0.1889 0.0074  0.0112  0.0184  126 THR   C CB  
2027 O OG1 . THR   B 120 ? 0.1332 0.1457 0.1958 0.0080  0.0092  0.0147  126 THR   C OG1 
2028 C CG2 . THR   B 120 ? 0.1426 0.1543 0.2132 0.0063  0.0107  0.0169  126 THR   C CG2 
2029 N N   . GLY   B 121 ? 0.1361 0.1458 0.1863 0.0098  0.0141  0.0249  127 GLY   C N   
2030 C CA  . GLY   B 121 ? 0.1587 0.1675 0.2030 0.0112  0.0157  0.0253  127 GLY   C CA  
2031 C C   . GLY   B 121 ? 0.2053 0.2150 0.2558 0.0120  0.0208  0.0279  127 GLY   C C   
2032 O O   . GLY   B 121 ? 0.2219 0.2320 0.2785 0.0115  0.0232  0.0307  127 GLY   C O   
2033 N N   . GLY   B 122 ? 0.2530 0.2626 0.3018 0.0133  0.0231  0.0273  128 GLY   C N   
2034 C CA  . GLY   B 122 ? 0.2827 0.2929 0.3378 0.0143  0.0288  0.0299  128 GLY   C CA  
2035 C C   . GLY   B 122 ? 0.2676 0.2801 0.3301 0.0148  0.0302  0.0268  128 GLY   C C   
2036 O O   . GLY   B 122 ? 0.2629 0.2772 0.3286 0.0142  0.0263  0.0226  128 GLY   C O   
2037 N N   . ASN   B 123 ? 0.2521 0.2646 0.3180 0.0162  0.0358  0.0291  129 ASN   C N   
2038 C CA  . ASN   B 123 ? 0.2555 0.2704 0.3299 0.0170  0.0380  0.0269  129 ASN   C CA  
2039 C C   . ASN   B 123 ? 0.2331 0.2473 0.2997 0.0180  0.0343  0.0234  129 ASN   C C   
2040 O O   . ASN   B 123 ? 0.2624 0.2796 0.3372 0.0183  0.0332  0.0204  129 ASN   C O   
2041 C CB  . ASN   B 123 ? 0.3013 0.3208 0.3931 0.0153  0.0371  0.0242  129 ASN   C CB  
2042 C CG  . ASN   B 123 ? 0.3755 0.3963 0.4801 0.0152  0.0434  0.0272  129 ASN   C CG  
2043 O OD1 . ASN   B 123 ? 0.3860 0.4048 0.4875 0.0168  0.0495  0.0313  129 ASN   C OD1 
2044 N ND2 . ASN   B 123 ? 0.4015 0.4256 0.5209 0.0133  0.0424  0.0251  129 ASN   C ND2 
2045 N N   . GLY   B 124 ? 0.2085 0.2190 0.2603 0.0185  0.0320  0.0238  130 GLY   C N   
2046 C CA  . GLY   B 124 ? 0.1981 0.2072 0.2426 0.0194  0.0288  0.0208  130 GLY   C CA  
2047 C C   . GLY   B 124 ? 0.1738 0.1846 0.2203 0.0181  0.0227  0.0172  130 GLY   C C   
2048 O O   . GLY   B 124 ? 0.1734 0.1837 0.2169 0.0190  0.0203  0.0146  130 GLY   C O   
2049 N N   . LEU   B 125 ? 0.1557 0.1679 0.2066 0.0163  0.0206  0.0172  131 LEU   C N   
2050 C CA  . LEU   B 125 ? 0.1536 0.1669 0.2057 0.0152  0.0154  0.0140  131 LEU   C CA  
2051 C C   . LEU   B 125 ? 0.1567 0.1676 0.2011 0.0140  0.0130  0.0152  131 LEU   C C   
2052 O O   . LEU   B 125 ? 0.1867 0.1964 0.2288 0.0136  0.0150  0.0185  131 LEU   C O   
2053 C CB  . LEU   B 125 ? 0.1715 0.1886 0.2371 0.0142  0.0149  0.0121  131 LEU   C CB  
2054 C CG  . LEU   B 125 ? 0.1958 0.2163 0.2719 0.0151  0.0168  0.0108  131 LEU   C CG  
2055 C CD1 . LEU   B 125 ? 0.2303 0.2544 0.3215 0.0137  0.0178  0.0099  131 LEU   C CD1 
2056 C CD2 . LEU   B 125 ? 0.2090 0.2303 0.2835 0.0164  0.0132  0.0077  131 LEU   C CD2 
2057 N N   . VAL   B 126 ? 0.1237 0.1337 0.1640 0.0137  0.0090  0.0129  132 VAL   C N   
2058 C CA  . VAL   B 126 ? 0.1217 0.1300 0.1570 0.0125  0.0067  0.0137  132 VAL   C CA  
2059 C C   . VAL   B 126 ? 0.1122 0.1219 0.1528 0.0117  0.0043  0.0110  132 VAL   C C   
2060 O O   . VAL   B 126 ? 0.1203 0.1308 0.1619 0.0124  0.0024  0.0081  132 VAL   C O   
2061 C CB  . VAL   B 126 ? 0.1287 0.1336 0.1532 0.0128  0.0046  0.0136  132 VAL   C CB  
2062 C CG1 . VAL   B 126 ? 0.1569 0.1612 0.1791 0.0141  0.0030  0.0108  132 VAL   C CG1 
2063 C CG2 . VAL   B 126 ? 0.1368 0.1403 0.1581 0.0114  0.0022  0.0145  132 VAL   C CG2 
2064 N N   . GLY   B 127 ? 0.1116 0.1213 0.1549 0.0103  0.0044  0.0120  133 GLY   C N   
2065 C CA  . GLY   B 127 ? 0.1071 0.1174 0.1542 0.0096  0.0026  0.0093  133 GLY   C CA  
2066 C C   . GLY   B 127 ? 0.1163 0.1242 0.1575 0.0091  0.0010  0.0099  133 GLY   C C   
2067 O O   . GLY   B 127 ? 0.1182 0.1251 0.1572 0.0085  0.0017  0.0130  133 GLY   C O   
2068 N N   . PHE   B 128 ? 0.0946 0.1016 0.1337 0.0094  -0.0011 0.0071  134 PHE   C N   
2069 C CA  . PHE   B 128 ? 0.1095 0.1140 0.1436 0.0091  -0.0020 0.0075  134 PHE   C CA  
2070 C C   . PHE   B 128 ? 0.1091 0.1133 0.1469 0.0087  -0.0018 0.0055  134 PHE   C C   
2071 O O   . PHE   B 128 ? 0.1179 0.1228 0.1575 0.0092  -0.0029 0.0021  134 PHE   C O   
2072 C CB  . PHE   B 128 ? 0.1118 0.1142 0.1382 0.0103  -0.0040 0.0062  134 PHE   C CB  
2073 C CG  . PHE   B 128 ? 0.1138 0.1160 0.1365 0.0110  -0.0041 0.0072  134 PHE   C CG  
2074 C CD1 . PHE   B 128 ? 0.1142 0.1147 0.1326 0.0104  -0.0040 0.0096  134 PHE   C CD1 
2075 C CD2 . PHE   B 128 ? 0.1219 0.1255 0.1456 0.0123  -0.0045 0.0056  134 PHE   C CD2 
2076 C CE1 . PHE   B 128 ? 0.1271 0.1265 0.1411 0.0112  -0.0040 0.0100  134 PHE   C CE1 
2077 C CE2 . PHE   B 128 ? 0.1246 0.1274 0.1448 0.0132  -0.0041 0.0064  134 PHE   C CE2 
2078 C CZ  . PHE   B 128 ? 0.1286 0.1291 0.1434 0.0126  -0.0037 0.0084  134 PHE   C CZ  
2079 N N   . ALA   B 129 ? 0.1074 0.1104 0.1460 0.0078  -0.0006 0.0073  135 ALA   C N   
2080 C CA  . ALA   B 129 ? 0.1101 0.1120 0.1511 0.0075  0.0003  0.0054  135 ALA   C CA  
2081 C C   . ALA   B 129 ? 0.1288 0.1278 0.1619 0.0086  -0.0009 0.0038  135 ALA   C C   
2082 O O   . ALA   B 129 ? 0.1315 0.1289 0.1605 0.0086  -0.0007 0.0060  135 ALA   C O   
2083 C CB  . ALA   B 129 ? 0.1198 0.1214 0.1654 0.0065  0.0024  0.0085  135 ALA   C CB  
2084 N N   . ASP   B 130 ? 0.1270 0.1253 0.1582 0.0096  -0.0020 0.0000  136 ASP   C N   
2085 C CA  . ASP   B 130 ? 0.1327 0.1279 0.1553 0.0111  -0.0029 -0.0013 136 ASP   C CA  
2086 C C   . ASP   B 130 ? 0.1321 0.1243 0.1537 0.0109  -0.0002 -0.0004 136 ASP   C C   
2087 O O   . ASP   B 130 ? 0.1390 0.1313 0.1662 0.0100  0.0017  -0.0010 136 ASP   C O   
2088 C CB  . ASP   B 130 ? 0.1498 0.1450 0.1705 0.0124  -0.0053 -0.0058 136 ASP   C CB  
2089 C CG  . ASP   B 130 ? 0.1959 0.1876 0.2064 0.0145  -0.0065 -0.0070 136 ASP   C CG  
2090 O OD1 . ASP   B 130 ? 0.1893 0.1801 0.1948 0.0154  -0.0068 -0.0048 136 ASP   C OD1 
2091 O OD2 . ASP   B 130 ? 0.2373 0.2269 0.2445 0.0154  -0.0067 -0.0101 136 ASP   C OD2 
2092 N N   . VAL   B 131 ? 0.1353 0.1246 0.1502 0.0118  0.0005  0.0009  137 VAL   C N   
2093 C CA  . VAL   B 131 ? 0.1391 0.1251 0.1527 0.0120  0.0037  0.0017  137 VAL   C CA  
2094 C C   . VAL   B 131 ? 0.1574 0.1393 0.1611 0.0142  0.0039  -0.0001 137 VAL   C C   
2095 O O   . VAL   B 131 ? 0.1634 0.1420 0.1646 0.0148  0.0072  0.0006  137 VAL   C O   
2096 C CB  . VAL   B 131 ? 0.1488 0.1348 0.1656 0.0108  0.0055  0.0060  137 VAL   C CB  
2097 C CG1 . VAL   B 131 ? 0.1422 0.1319 0.1679 0.0089  0.0052  0.0080  137 VAL   C CG1 
2098 C CG2 . VAL   B 131 ? 0.1544 0.1395 0.1661 0.0112  0.0040  0.0076  137 VAL   C CG2 
2099 N N   . ARG   B 132 ? 0.1533 0.1354 0.1512 0.0157  0.0007  -0.0020 138 ARG   C N   
2100 C CA  . ARG   B 132 ? 0.1552 0.1332 0.1425 0.0183  0.0005  -0.0029 138 ARG   C CA  
2101 C C   . ARG   B 132 ? 0.1653 0.1403 0.1479 0.0196  0.0015  -0.0062 138 ARG   C C   
2102 O O   . ARG   B 132 ? 0.1893 0.1598 0.1621 0.0218  0.0028  -0.0062 138 ARG   C O   
2103 C CB  . ARG   B 132 ? 0.1440 0.1234 0.1274 0.0198  -0.0037 -0.0039 138 ARG   C CB  
2104 C CG  . ARG   B 132 ? 0.1539 0.1347 0.1396 0.0190  -0.0041 -0.0007 138 ARG   C CG  
2105 C CD  . ARG   B 132 ? 0.1591 0.1414 0.1420 0.0207  -0.0078 -0.0019 138 ARG   C CD  
2106 N NE  . ARG   B 132 ? 0.1518 0.1384 0.1411 0.0200  -0.0104 -0.0046 138 ARG   C NE  
2107 C CZ  . ARG   B 132 ? 0.1666 0.1558 0.1569 0.0211  -0.0136 -0.0059 138 ARG   C CZ  
2108 N NH1 . ARG   B 132 ? 0.1674 0.1549 0.1516 0.0233  -0.0151 -0.0048 138 ARG   C NH1 
2109 N NH2 . ARG   B 132 ? 0.1648 0.1583 0.1630 0.0201  -0.0152 -0.0080 138 ARG   C NH2 
2110 N N   . ASP   B 133 ? 0.1648 0.1416 0.1534 0.0183  0.0012  -0.0092 139 ASP   C N   
2111 C CA  . ASP   B 133 ? 0.1778 0.1512 0.1618 0.0194  0.0021  -0.0131 139 ASP   C CA  
2112 C C   . ASP   B 133 ? 0.1944 0.1646 0.1803 0.0189  0.0080  -0.0115 139 ASP   C C   
2113 O O   . ASP   B 133 ? 0.2068 0.1729 0.1873 0.0202  0.0099  -0.0145 139 ASP   C O   
2114 C CB  . ASP   B 133 ? 0.1934 0.1699 0.1843 0.0182  -0.0008 -0.0175 139 ASP   C CB  
2115 C CG  . ASP   B 133 ? 0.2198 0.1995 0.2237 0.0154  0.0013  -0.0158 139 ASP   C CG  
2116 O OD1 . ASP   B 133 ? 0.1881 0.1704 0.1966 0.0143  0.0020  -0.0115 139 ASP   C OD1 
2117 O OD2 . ASP   B 133 ? 0.2377 0.2170 0.2470 0.0145  0.0024  -0.0188 139 ASP   C OD2 
2118 N N   . LEU   B 134 ? 0.1794 0.1513 0.1728 0.0173  0.0107  -0.0068 140 LEU   C N   
2119 C CA  . LEU   B 134 ? 0.1719 0.1416 0.1697 0.0167  0.0161  -0.0049 140 LEU   C CA  
2120 C C   . LEU   B 134 ? 0.1804 0.1457 0.1705 0.0185  0.0196  -0.0025 140 LEU   C C   
2121 O O   . LEU   B 134 ? 0.1848 0.1507 0.1786 0.0177  0.0213  0.0018  140 LEU   C O   
2122 C CB  . LEU   B 134 ? 0.1650 0.1392 0.1750 0.0142  0.0165  -0.0011 140 LEU   C CB  
2123 C CG  . LEU   B 134 ? 0.1679 0.1463 0.1858 0.0126  0.0137  -0.0026 140 LEU   C CG  
2124 C CD1 . LEU   B 134 ? 0.1828 0.1652 0.2105 0.0106  0.0138  0.0019  140 LEU   C CD1 
2125 C CD2 . LEU   B 134 ? 0.1992 0.1760 0.2200 0.0126  0.0154  -0.0064 140 LEU   C CD2 
2126 N N   . LEU   B 135 ? 0.1853 0.1456 0.1639 0.0210  0.0206  -0.0054 141 LEU   C N   
2127 C CA  . LEU   B 135 ? 0.2076 0.1629 0.1769 0.0233  0.0241  -0.0029 141 LEU   C CA  
2128 C C   . LEU   B 135 ? 0.2057 0.1589 0.1805 0.0228  0.0308  0.0007  141 LEU   C C   
2129 O O   . LEU   B 135 ? 0.2207 0.1715 0.1932 0.0236  0.0338  0.0044  141 LEU   C O   
2130 C CB  . LEU   B 135 ? 0.2163 0.1663 0.1704 0.0266  0.0236  -0.0066 141 LEU   C CB  
2131 C CG  . LEU   B 135 ? 0.2167 0.1693 0.1665 0.0271  0.0163  -0.0107 141 LEU   C CG  
2132 C CD1 . LEU   B 135 ? 0.2396 0.1867 0.1735 0.0306  0.0152  -0.0144 141 LEU   C CD1 
2133 C CD2 . LEU   B 135 ? 0.2228 0.1791 0.1743 0.0267  0.0122  -0.0080 141 LEU   C CD2 
2134 N N   . TRP   B 136 ? 0.2092 0.1633 0.1925 0.0215  0.0333  -0.0003 142 TRP   C N   
2135 C CA  . TRP   B 136 ? 0.2123 0.1648 0.2029 0.0212  0.0399  0.0030  142 TRP   C CA  
2136 C C   . TRP   B 136 ? 0.2192 0.1759 0.2208 0.0190  0.0396  0.0082  142 TRP   C C   
2137 O O   . TRP   B 136 ? 0.2339 0.1894 0.2413 0.0189  0.0447  0.0116  142 TRP   C O   
2138 C CB  . TRP   B 136 ? 0.2102 0.1630 0.2082 0.0204  0.0422  0.0005  142 TRP   C CB  
2139 C CG  . TRP   B 136 ? 0.2014 0.1598 0.2087 0.0180  0.0373  -0.0006 142 TRP   C CG  
2140 C CD1 . TRP   B 136 ? 0.2103 0.1697 0.2153 0.0178  0.0332  -0.0052 142 TRP   C CD1 
2141 C CD2 . TRP   B 136 ? 0.2005 0.1644 0.2217 0.0156  0.0365  0.0033  142 TRP   C CD2 
2142 N NE1 . TRP   B 136 ? 0.2144 0.1793 0.2309 0.0155  0.0305  -0.0042 142 TRP   C NE1 
2143 C CE2 . TRP   B 136 ? 0.2075 0.1750 0.2331 0.0142  0.0323  0.0011  142 TRP   C CE2 
2144 C CE3 . TRP   B 136 ? 0.2029 0.1688 0.2331 0.0145  0.0386  0.0084  142 TRP   C CE3 
2145 C CZ2 . TRP   B 136 ? 0.2020 0.1746 0.2394 0.0121  0.0306  0.0042  142 TRP   C CZ2 
2146 C CZ3 . TRP   B 136 ? 0.2031 0.1744 0.2451 0.0124  0.0362  0.0111  142 TRP   C CZ3 
2147 C CH2 . TRP   B 136 ? 0.1988 0.1732 0.2434 0.0114  0.0324  0.0091  142 TRP   C CH2 
2148 N N   . LEU   B 137 ? 0.2022 0.1636 0.2065 0.0174  0.0338  0.0087  143 LEU   C N   
2149 C CA  . LEU   B 137 ? 0.1984 0.1631 0.2112 0.0154  0.0329  0.0131  143 LEU   C CA  
2150 C C   . LEU   B 137 ? 0.2306 0.1916 0.2389 0.0165  0.0359  0.0159  143 LEU   C C   
2151 O O   . LEU   B 137 ? 0.2517 0.2143 0.2684 0.0150  0.0368  0.0196  143 LEU   C O   
2152 C CB  . LEU   B 137 ? 0.1956 0.1650 0.2097 0.0139  0.0264  0.0128  143 LEU   C CB  
2153 C CG  . LEU   B 137 ? 0.1831 0.1568 0.2046 0.0124  0.0238  0.0115  143 LEU   C CG  
2154 C CD1 . LEU   B 137 ? 0.1872 0.1644 0.2070 0.0116  0.0182  0.0107  143 LEU   C CD1 
2155 C CD2 . LEU   B 137 ? 0.2004 0.1770 0.2344 0.0106  0.0254  0.0149  143 LEU   C CD2 
2156 N N   . ASP   B 138 ? 0.2249 0.1809 0.2200 0.0193  0.0371  0.0143  144 ASP   C N   
2157 C CA  . ASP   B 138 ? 0.2513 0.2031 0.2408 0.0207  0.0402  0.0172  144 ASP   C CA  
2158 C C   . ASP   B 138 ? 0.2972 0.2444 0.2878 0.0220  0.0483  0.0195  144 ASP   C C   
2159 O O   . ASP   B 138 ? 0.3131 0.2561 0.2993 0.0234  0.0520  0.0223  144 ASP   C O   
2160 C CB  . ASP   B 138 ? 0.2574 0.2057 0.2317 0.0236  0.0379  0.0152  144 ASP   C CB  
2161 C CG  . ASP   B 138 ? 0.2754 0.2277 0.2486 0.0228  0.0307  0.0137  144 ASP   C CG  
2162 O OD1 . ASP   B 138 ? 0.2701 0.2271 0.2530 0.0201  0.0278  0.0146  144 ASP   C OD1 
2163 O OD2 . ASP   B 138 ? 0.3123 0.2625 0.2744 0.0251  0.0280  0.0116  144 ASP   C OD2 
2164 N N   . GLU   B 139 ? 0.3109 0.2583 0.3073 0.0217  0.0516  0.0185  145 GLU   C N   
2165 C CA  . GLU   B 139 ? 0.3718 0.3145 0.3693 0.0232  0.0601  0.0206  145 GLU   C CA  
2166 C C   . GLU   B 139 ? 0.4200 0.3659 0.4329 0.0214  0.0631  0.0217  145 GLU   C C   
2167 O O   . GLU   B 139 ? 0.4238 0.3754 0.4455 0.0191  0.0582  0.0210  145 GLU   C O   
2168 C CB  . GLU   B 139 ? 0.4380 0.3742 0.4193 0.0267  0.0628  0.0169  145 GLU   C CB  
2169 C CG  . GLU   B 139 ? 0.5331 0.4711 0.5142 0.0263  0.0598  0.0118  145 GLU   C CG  
2170 C CD  . GLU   B 139 ? 0.6546 0.5883 0.6190 0.0290  0.0576  0.0067  145 GLU   C CD  
2171 O OE1 . GLU   B 139 ? 0.6553 0.5895 0.6200 0.0286  0.0559  0.0022  145 GLU   C OE1 
2172 O OE2 . GLU   B 139 ? 0.7109 0.6405 0.6622 0.0315  0.0575  0.0072  145 GLU   C OE2 
2173 N N   . GLU   B 140 ? 0.4551 0.3969 0.4705 0.0228  0.0715  0.0236  146 GLU   C N   
2174 C CA  . GLU   B 140 ? 0.4815 0.4248 0.5103 0.0221  0.0760  0.0246  146 GLU   C CA  
2175 C C   . GLU   B 140 ? 0.5003 0.4512 0.5471 0.0188  0.0721  0.0277  146 GLU   C C   
2176 O O   . GLU   B 140 ? 0.5118 0.4665 0.5672 0.0176  0.0702  0.0269  146 GLU   C O   
2177 C CB  . GLU   B 140 ? 0.5144 0.4557 0.5373 0.0233  0.0762  0.0195  146 GLU   C CB  
2178 C CG  . GLU   B 140 ? 0.6187 0.5621 0.6556 0.0224  0.0793  0.0198  146 GLU   C CG  
2179 C CD  . GLU   B 140 ? 0.7413 0.6803 0.7829 0.0243  0.0894  0.0217  146 GLU   C CD  
2180 O OE1 . GLU   B 140 ? 0.7739 0.7147 0.8278 0.0237  0.0920  0.0221  146 GLU   C OE1 
2181 O OE2 . GLU   B 140 ? 0.7862 0.7195 0.8192 0.0264  0.0951  0.0231  146 GLU   C OE2 
2182 N N1  . A1B4G C .   ? 0.3332 0.3045 0.3716 0.0140  0.0336  -0.0127 201 A1B4G A N1  
2183 N N3  . A1B4G C .   ? 0.3804 0.3627 0.4034 0.0067  0.0397  -0.0206 201 A1B4G A N3  
2184 C C4  . A1B4G C .   ? 0.3483 0.3218 0.3890 0.0145  0.0373  -0.0136 201 A1B4G A C4  
2185 C C5  . A1B4G C .   ? 0.3109 0.2865 0.3585 0.0183  0.0309  -0.0054 201 A1B4G A C5  
2186 C C6  . A1B4G C .   ? 0.3013 0.2762 0.3445 0.0169  0.0259  -0.0045 201 A1B4G A C6  
2187 C C7  . A1B4G C .   ? 0.2712 0.2499 0.3229 0.0203  0.0239  0.0028  201 A1B4G A C7  
2188 C C8  . A1B4G C .   ? 0.3092 0.2756 0.3488 0.0139  0.0297  -0.0104 201 A1B4G A C8  
2189 C C10 . A1B4G C .   ? 0.3395 0.3060 0.3689 0.0094  0.0333  -0.0180 201 A1B4G A C10 
2190 C C13 . A1B4G C .   ? 0.3640 0.3499 0.3795 0.0066  0.0261  -0.0149 201 A1B4G A C13 
2191 F F   . A1B4G C .   ? 0.3640 0.3463 0.3899 0.0115  0.0219  -0.0095 201 A1B4G A F   
2192 C C11 . A1B4G C .   ? 0.3627 0.3446 0.3870 0.0102  0.0257  -0.0124 201 A1B4G A C11 
2193 C C12 . A1B4G C .   ? 0.3636 0.3489 0.3806 0.0079  0.0224  -0.0126 201 A1B4G A C12 
2194 C C14 . A1B4G C .   ? 0.3700 0.3527 0.3919 0.0077  0.0336  -0.0175 201 A1B4G A C14 
2195 C C2  . A1B4G C .   ? 0.3680 0.3466 0.3981 0.0103  0.0374  -0.0174 201 A1B4G A C2  
2196 N N   . A1B4G C .   ? 0.3771 0.3524 0.4141 0.0113  0.0460  -0.0204 201 A1B4G A N   
2197 C C1  . A1B4G C .   ? 0.3819 0.3598 0.4142 0.0090  0.0471  -0.0225 201 A1B4G A C1  
2198 C C   . A1B4G C .   ? 0.3890 0.3648 0.4260 0.0087  0.0562  -0.0264 201 A1B4G A C   
2199 C C3  . A1B4G C .   ? 0.3600 0.3381 0.3912 0.0116  0.0332  -0.0146 201 A1B4G A C3  
2200 O O1  . A1B4G C .   ? 0.3590 0.3230 0.3807 0.0051  0.0356  -0.0235 201 A1B4G A O1  
2201 C C9  . A1B4G C .   ? 0.3261 0.2907 0.3552 0.0090  0.0303  -0.0169 201 A1B4G A C9  
2202 O O   . A1B4G C .   ? 0.2787 0.2559 0.3410 0.0236  0.0281  0.0062  201 A1B4G A O   
2203 N N2  . A1B4G C .   ? 0.2193 0.2026 0.2665 0.0191  0.0178  0.0054  201 A1B4G A N2  
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