data_7I45
# 
_entry.id   7I45 
# 
_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   7I45         pdb_00007i45 10.2210/pdb7i45/pdb 
WWPDB D_1001408292 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-04-02 ? 
2 'Structure model' 1 1 2025-04-09 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Refinement description' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            pdbx_initial_refinement_model 
# 
_pdbx_database_status.entry_id                        7I45 
_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-[(7-chloro-2,3-dihydro-1,4-benzodioxin-6-yl)acetyl]piperidine-3-carboxamide' 338.786   2   ?         ? ? 
? 
3 non-polymer syn 'ZINC ION'                                                                           65.409    2   ?         ? ? 
? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                                                 78.133    5   ?         ? ? 
? 
5 non-polymer syn GLYCEROL                                                                             92.094    1   ?         ? ? 
? 
6 water       nat water                                                                                18.015    291 ?         ? ? 
? 
# 
_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-[(7-chloro-2,3-dihydro-1,4-benzodioxin-6-yl)acetyl]piperidine-3-carboxamide' A1B2J 
3 'ZINC ION'                                                                           ZN    
4 'DIMETHYL SULFOXIDE'                                                                 DMS   
5 GLYCEROL                                                                             GOL   
6 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 
A1B2J non-polymer         . '(3S)-1-[(7-chloro-2,3-dihydro-1,4-benzodioxin-6-yl)acetyl]piperidine-3-carboxamide' ? 
'C16 H19 Cl N2 O4' 338.786 
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  
GOL   non-polymer         . GLYCEROL                                                                             
'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'         92.094  
HIS   'L-peptide linking' y HISTIDINE                                                                            ? 
'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                                                ? 'H2 O' 18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                           ? 'C6 H13 N O2' 
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                              ? 'C6 H13 N O2' 
131.173 
LYS   'L-peptide linking' y LYSINE                                                                               ? 
'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                                           ? 'C5 H11 N O2 S' 
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                                        ? 'C9 H11 N O2' 
165.189 
PRO   'L-peptide linking' y PROLINE                                                                              ? 'C5 H9 N O2' 
115.130 
SER   'L-peptide linking' y SERINE                                                                               ? 'C3 H7 N O3' 
105.093 
THR   'L-peptide linking' y THREONINE                                                                            ? 'C4 H9 N O3' 
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                                           ? 'C11 H12 N2 O2' 
204.225 
TYR   'L-peptide linking' y TYROSINE                                                                             ? 'C9 H11 N O3' 
181.189 
VAL   'L-peptide linking' y VALINE                                                                               ? 'C5 H11 N O2' 
117.146 
ZN    non-polymer         . 'ZINC ION'                                                                           ? 'Zn 2' 65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   A . n 
A 1 141 ALA 141 147 ?   ?   ?   A . n 
A 1 142 MET 142 148 ?   ?   ?   A . n 
A 1 143 GLU 143 149 ?   ?   ?   A . n 
A 1 144 GLN 144 150 ?   ?   ?   A . n 
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 ?   ?   ?   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        A1B2J 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B2J 
_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 A1B2J 1   201 201 A1B2J LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 6   DMS   DMS A . 
F 4 DMS   1   204 8   DMS   DMS A . 
G 2 A1B2J 1   201 201 A1B2J LIG C . 
H 5 GOL   1   202 202 GOL   GOL C . 
I 4 DMS   1   203 7   DMS   DMS C . 
J 3 ZN    1   204 1   ZN    ZN  C . 
K 4 DMS   1   205 2   DMS   DMS C . 
L 4 DMS   1   206 6   DMS   DMS C . 
M 6 HOH   1   301 76  HOH   HOH A . 
M 6 HOH   2   302 95  HOH   HOH A . 
M 6 HOH   3   303 239 HOH   HOH A . 
M 6 HOH   4   304 61  HOH   HOH A . 
M 6 HOH   5   305 149 HOH   HOH A . 
M 6 HOH   6   306 84  HOH   HOH A . 
M 6 HOH   7   307 24  HOH   HOH A . 
M 6 HOH   8   308 62  HOH   HOH A . 
M 6 HOH   9   309 13  HOH   HOH A . 
M 6 HOH   10  310 22  HOH   HOH A . 
M 6 HOH   11  311 66  HOH   HOH A . 
M 6 HOH   12  312 34  HOH   HOH A . 
M 6 HOH   13  313 190 HOH   HOH A . 
M 6 HOH   14  314 116 HOH   HOH A . 
M 6 HOH   15  315 48  HOH   HOH A . 
M 6 HOH   16  316 32  HOH   HOH A . 
M 6 HOH   17  317 103 HOH   HOH A . 
M 6 HOH   18  318 252 HOH   HOH A . 
M 6 HOH   19  319 5   HOH   HOH A . 
M 6 HOH   20  320 60  HOH   HOH A . 
M 6 HOH   21  321 7   HOH   HOH A . 
M 6 HOH   22  322 64  HOH   HOH A . 
M 6 HOH   23  323 28  HOH   HOH A . 
M 6 HOH   24  324 183 HOH   HOH A . 
M 6 HOH   25  325 236 HOH   HOH A . 
M 6 HOH   26  326 14  HOH   HOH A . 
M 6 HOH   27  327 227 HOH   HOH A . 
M 6 HOH   28  328 63  HOH   HOH A . 
M 6 HOH   29  329 250 HOH   HOH A . 
M 6 HOH   30  330 33  HOH   HOH A . 
M 6 HOH   31  331 59  HOH   HOH A . 
M 6 HOH   32  332 22  HOH   HOH A . 
M 6 HOH   33  333 72  HOH   HOH A . 
M 6 HOH   34  334 19  HOH   HOH A . 
M 6 HOH   35  335 140 HOH   HOH A . 
M 6 HOH   36  336 99  HOH   HOH A . 
M 6 HOH   37  337 49  HOH   HOH A . 
M 6 HOH   38  338 238 HOH   HOH A . 
M 6 HOH   39  339 114 HOH   HOH A . 
M 6 HOH   40  340 88  HOH   HOH A . 
M 6 HOH   41  341 53  HOH   HOH A . 
M 6 HOH   42  342 94  HOH   HOH A . 
M 6 HOH   43  343 113 HOH   HOH A . 
M 6 HOH   44  344 71  HOH   HOH A . 
M 6 HOH   45  345 230 HOH   HOH A . 
M 6 HOH   46  346 130 HOH   HOH A . 
M 6 HOH   47  347 66  HOH   HOH A . 
M 6 HOH   48  348 26  HOH   HOH A . 
M 6 HOH   49  349 128 HOH   HOH A . 
M 6 HOH   50  350 122 HOH   HOH A . 
M 6 HOH   51  351 74  HOH   HOH A . 
M 6 HOH   52  352 171 HOH   HOH A . 
M 6 HOH   53  353 70  HOH   HOH A . 
M 6 HOH   54  354 84  HOH   HOH A . 
M 6 HOH   55  355 53  HOH   HOH A . 
M 6 HOH   56  356 56  HOH   HOH A . 
M 6 HOH   57  357 226 HOH   HOH A . 
M 6 HOH   58  358 119 HOH   HOH A . 
M 6 HOH   59  359 26  HOH   HOH A . 
M 6 HOH   60  360 233 HOH   HOH A . 
M 6 HOH   61  361 79  HOH   HOH A . 
M 6 HOH   62  362 259 HOH   HOH A . 
M 6 HOH   63  363 10  HOH   HOH A . 
M 6 HOH   64  364 73  HOH   HOH A . 
M 6 HOH   65  365 21  HOH   HOH A . 
M 6 HOH   66  366 241 HOH   HOH A . 
M 6 HOH   67  367 256 HOH   HOH A . 
M 6 HOH   68  368 149 HOH   HOH A . 
M 6 HOH   69  369 115 HOH   HOH A . 
M 6 HOH   70  370 102 HOH   HOH A . 
M 6 HOH   71  371 134 HOH   HOH A . 
M 6 HOH   72  372 107 HOH   HOH A . 
M 6 HOH   73  373 111 HOH   HOH A . 
M 6 HOH   74  374 91  HOH   HOH A . 
M 6 HOH   75  375 35  HOH   HOH A . 
M 6 HOH   76  376 242 HOH   HOH A . 
M 6 HOH   77  377 145 HOH   HOH A . 
M 6 HOH   78  378 234 HOH   HOH A . 
M 6 HOH   79  379 85  HOH   HOH A . 
M 6 HOH   80  380 197 HOH   HOH A . 
M 6 HOH   81  381 14  HOH   HOH A . 
M 6 HOH   82  382 152 HOH   HOH A . 
M 6 HOH   83  383 115 HOH   HOH A . 
M 6 HOH   84  384 75  HOH   HOH A . 
M 6 HOH   85  385 150 HOH   HOH A . 
M 6 HOH   86  386 38  HOH   HOH A . 
M 6 HOH   87  387 96  HOH   HOH A . 
M 6 HOH   88  388 151 HOH   HOH A . 
M 6 HOH   89  389 12  HOH   HOH A . 
M 6 HOH   90  390 92  HOH   HOH A . 
M 6 HOH   91  391 23  HOH   HOH A . 
M 6 HOH   92  392 40  HOH   HOH A . 
M 6 HOH   93  393 112 HOH   HOH A . 
M 6 HOH   94  394 102 HOH   HOH A . 
M 6 HOH   95  395 47  HOH   HOH A . 
M 6 HOH   96  396 100 HOH   HOH A . 
M 6 HOH   97  397 228 HOH   HOH A . 
M 6 HOH   98  398 58  HOH   HOH A . 
M 6 HOH   99  399 42  HOH   HOH A . 
M 6 HOH   100 400 36  HOH   HOH A . 
M 6 HOH   101 401 35  HOH   HOH A . 
M 6 HOH   102 402 12  HOH   HOH A . 
M 6 HOH   103 403 106 HOH   HOH A . 
M 6 HOH   104 404 16  HOH   HOH A . 
M 6 HOH   105 405 243 HOH   HOH A . 
M 6 HOH   106 406 208 HOH   HOH A . 
M 6 HOH   107 407 63  HOH   HOH A . 
M 6 HOH   108 408 148 HOH   HOH A . 
M 6 HOH   109 409 19  HOH   HOH A . 
M 6 HOH   110 410 104 HOH   HOH A . 
M 6 HOH   111 411 125 HOH   HOH A . 
M 6 HOH   112 412 157 HOH   HOH A . 
M 6 HOH   113 413 101 HOH   HOH A . 
M 6 HOH   114 414 15  HOH   HOH A . 
M 6 HOH   115 415 60  HOH   HOH A . 
M 6 HOH   116 416 114 HOH   HOH A . 
M 6 HOH   117 417 202 HOH   HOH A . 
M 6 HOH   118 418 127 HOH   HOH A . 
M 6 HOH   119 419 77  HOH   HOH A . 
M 6 HOH   120 420 52  HOH   HOH A . 
M 6 HOH   121 421 209 HOH   HOH A . 
M 6 HOH   122 422 154 HOH   HOH A . 
M 6 HOH   123 423 82  HOH   HOH A . 
M 6 HOH   124 424 178 HOH   HOH A . 
M 6 HOH   125 425 201 HOH   HOH A . 
M 6 HOH   126 426 126 HOH   HOH A . 
M 6 HOH   127 427 181 HOH   HOH A . 
M 6 HOH   128 428 172 HOH   HOH A . 
M 6 HOH   129 429 136 HOH   HOH A . 
M 6 HOH   130 430 23  HOH   HOH A . 
M 6 HOH   131 431 138 HOH   HOH A . 
M 6 HOH   132 432 72  HOH   HOH A . 
M 6 HOH   133 433 129 HOH   HOH A . 
M 6 HOH   134 434 135 HOH   HOH A . 
M 6 HOH   135 435 222 HOH   HOH A . 
M 6 HOH   136 436 132 HOH   HOH A . 
M 6 HOH   137 437 99  HOH   HOH A . 
M 6 HOH   138 438 82  HOH   HOH A . 
M 6 HOH   139 439 136 HOH   HOH A . 
M 6 HOH   140 440 141 HOH   HOH A . 
M 6 HOH   141 441 196 HOH   HOH A . 
M 6 HOH   142 442 224 HOH   HOH A . 
M 6 HOH   143 443 225 HOH   HOH A . 
N 6 HOH   1   301 120 HOH   HOH C . 
N 6 HOH   2   302 147 HOH   HOH C . 
N 6 HOH   3   303 174 HOH   HOH C . 
N 6 HOH   4   304 8   HOH   HOH C . 
N 6 HOH   5   305 235 HOH   HOH C . 
N 6 HOH   6   306 212 HOH   HOH C . 
N 6 HOH   7   307 33  HOH   HOH C . 
N 6 HOH   8   308 103 HOH   HOH C . 
N 6 HOH   9   309 32  HOH   HOH C . 
N 6 HOH   10  310 70  HOH   HOH C . 
N 6 HOH   11  311 2   HOH   HOH C . 
N 6 HOH   12  312 244 HOH   HOH C . 
N 6 HOH   13  313 138 HOH   HOH C . 
N 6 HOH   14  314 28  HOH   HOH C . 
N 6 HOH   15  315 249 HOH   HOH C . 
N 6 HOH   16  316 118 HOH   HOH C . 
N 6 HOH   17  317 43  HOH   HOH C . 
N 6 HOH   18  318 51  HOH   HOH C . 
N 6 HOH   19  319 109 HOH   HOH C . 
N 6 HOH   20  320 111 HOH   HOH C . 
N 6 HOH   21  321 50  HOH   HOH C . 
N 6 HOH   22  322 141 HOH   HOH C . 
N 6 HOH   23  323 133 HOH   HOH C . 
N 6 HOH   24  324 124 HOH   HOH C . 
N 6 HOH   25  325 248 HOH   HOH C . 
N 6 HOH   26  326 254 HOH   HOH C . 
N 6 HOH   27  327 80  HOH   HOH C . 
N 6 HOH   28  328 247 HOH   HOH C . 
N 6 HOH   29  329 122 HOH   HOH C . 
N 6 HOH   30  330 65  HOH   HOH C . 
N 6 HOH   31  331 98  HOH   HOH C . 
N 6 HOH   32  332 237 HOH   HOH C . 
N 6 HOH   33  333 130 HOH   HOH C . 
N 6 HOH   34  334 85  HOH   HOH C . 
N 6 HOH   35  335 39  HOH   HOH C . 
N 6 HOH   36  336 74  HOH   HOH C . 
N 6 HOH   37  337 30  HOH   HOH C . 
N 6 HOH   38  338 20  HOH   HOH C . 
N 6 HOH   39  339 98  HOH   HOH C . 
N 6 HOH   40  340 97  HOH   HOH C . 
N 6 HOH   41  341 31  HOH   HOH C . 
N 6 HOH   42  342 11  HOH   HOH C . 
N 6 HOH   43  343 57  HOH   HOH C . 
N 6 HOH   44  344 126 HOH   HOH C . 
N 6 HOH   45  345 71  HOH   HOH C . 
N 6 HOH   46  346 123 HOH   HOH C . 
N 6 HOH   47  347 46  HOH   HOH C . 
N 6 HOH   48  348 18  HOH   HOH C . 
N 6 HOH   49  349 37  HOH   HOH C . 
N 6 HOH   50  350 258 HOH   HOH C . 
N 6 HOH   51  351 38  HOH   HOH C . 
N 6 HOH   52  352 155 HOH   HOH C . 
N 6 HOH   53  353 137 HOH   HOH C . 
N 6 HOH   54  354 4   HOH   HOH C . 
N 6 HOH   55  355 73  HOH   HOH C . 
N 6 HOH   56  356 198 HOH   HOH C . 
N 6 HOH   57  357 6   HOH   HOH C . 
N 6 HOH   58  358 110 HOH   HOH C . 
N 6 HOH   59  359 83  HOH   HOH C . 
N 6 HOH   60  360 64  HOH   HOH C . 
N 6 HOH   61  361 39  HOH   HOH C . 
N 6 HOH   62  362 29  HOH   HOH C . 
N 6 HOH   63  363 117 HOH   HOH C . 
N 6 HOH   64  364 86  HOH   HOH C . 
N 6 HOH   65  365 229 HOH   HOH C . 
N 6 HOH   66  366 255 HOH   HOH C . 
N 6 HOH   67  367 118 HOH   HOH C . 
N 6 HOH   68  368 79  HOH   HOH C . 
N 6 HOH   69  369 144 HOH   HOH C . 
N 6 HOH   70  370 257 HOH   HOH C . 
N 6 HOH   71  371 37  HOH   HOH C . 
N 6 HOH   72  372 253 HOH   HOH C . 
N 6 HOH   73  373 124 HOH   HOH C . 
N 6 HOH   74  374 52  HOH   HOH C . 
N 6 HOH   75  375 127 HOH   HOH C . 
N 6 HOH   76  376 90  HOH   HOH C . 
N 6 HOH   77  377 170 HOH   HOH C . 
N 6 HOH   78  378 105 HOH   HOH C . 
N 6 HOH   79  379 16  HOH   HOH C . 
N 6 HOH   80  380 205 HOH   HOH C . 
N 6 HOH   81  381 3   HOH   HOH C . 
N 6 HOH   82  382 44  HOH   HOH C . 
N 6 HOH   83  383 13  HOH   HOH C . 
N 6 HOH   84  384 7   HOH   HOH C . 
N 6 HOH   85  385 245 HOH   HOH C . 
N 6 HOH   86  386 91  HOH   HOH C . 
N 6 HOH   87  387 240 HOH   HOH C . 
N 6 HOH   88  388 83  HOH   HOH C . 
N 6 HOH   89  389 1   HOH   HOH C . 
N 6 HOH   90  390 108 HOH   HOH C . 
N 6 HOH   91  391 148 HOH   HOH C . 
N 6 HOH   92  392 50  HOH   HOH C . 
N 6 HOH   93  393 54  HOH   HOH C . 
N 6 HOH   94  394 204 HOH   HOH C . 
N 6 HOH   95  395 40  HOH   HOH C . 
N 6 HOH   96  396 31  HOH   HOH C . 
N 6 HOH   97  397 68  HOH   HOH C . 
N 6 HOH   98  398 231 HOH   HOH C . 
N 6 HOH   99  399 78  HOH   HOH C . 
N 6 HOH   100 400 232 HOH   HOH C . 
N 6 HOH   101 401 78  HOH   HOH C . 
N 6 HOH   102 402 89  HOH   HOH C . 
N 6 HOH   103 403 62  HOH   HOH C . 
N 6 HOH   104 404 87  HOH   HOH C . 
N 6 HOH   105 405 11  HOH   HOH C . 
N 6 HOH   106 406 41  HOH   HOH C . 
N 6 HOH   107 407 144 HOH   HOH C . 
N 6 HOH   108 408 120 HOH   HOH C . 
N 6 HOH   109 409 110 HOH   HOH C . 
N 6 HOH   110 410 162 HOH   HOH C . 
N 6 HOH   111 411 44  HOH   HOH C . 
N 6 HOH   112 412 146 HOH   HOH C . 
N 6 HOH   113 413 41  HOH   HOH C . 
N 6 HOH   114 414 210 HOH   HOH C . 
N 6 HOH   115 415 87  HOH   HOH C . 
N 6 HOH   116 416 106 HOH   HOH C . 
N 6 HOH   117 417 105 HOH   HOH C . 
N 6 HOH   118 418 251 HOH   HOH C . 
N 6 HOH   119 419 54  HOH   HOH C . 
N 6 HOH   120 420 246 HOH   HOH C . 
N 6 HOH   121 421 107 HOH   HOH C . 
N 6 HOH   122 422 69  HOH   HOH C . 
N 6 HOH   123 423 47  HOH   HOH C . 
N 6 HOH   124 424 143 HOH   HOH C . 
N 6 HOH   125 425 104 HOH   HOH C . 
N 6 HOH   126 426 117 HOH   HOH C . 
N 6 HOH   127 427 95  HOH   HOH C . 
N 6 HOH   128 428 260 HOH   HOH C . 
N 6 HOH   129 429 140 HOH   HOH C . 
N 6 HOH   130 430 45  HOH   HOH C . 
N 6 HOH   131 431 211 HOH   HOH C . 
N 6 HOH   132 432 116 HOH   HOH C . 
N 6 HOH   133 433 90  HOH   HOH C . 
N 6 HOH   134 434 135 HOH   HOH C . 
N 6 HOH   135 435 9   HOH   HOH C . 
N 6 HOH   136 436 166 HOH   HOH C . 
N 6 HOH   137 437 185 HOH   HOH C . 
N 6 HOH   138 438 142 HOH   HOH C . 
N 6 HOH   139 439 139 HOH   HOH C . 
N 6 HOH   140 440 216 HOH   HOH C . 
N 6 HOH   141 441 93  HOH   HOH C . 
N 6 HOH   142 442 123 HOH   HOH C . 
N 6 HOH   143 443 176 HOH   HOH C . 
N 6 HOH   144 444 142 HOH   HOH C . 
N 6 HOH   145 445 199 HOH   HOH C . 
N 6 HOH   146 446 218 HOH   HOH C . 
N 6 HOH   147 447 207 HOH   HOH C . 
N 6 HOH   148 448 146 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           7I45 
_cell.length_a           72.493 
_cell.length_b           61.473 
_cell.length_c           65.240 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.47 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I45 
_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          7I45 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.28 
_exptl_crystal.density_percent_sol   46.16 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.pH              6.05 
_exptl_crystal_grow.temp            293.15 
_exptl_crystal_grow.pdbx_details    '0.1 M MES, pH 6.05, 16 % PEG 20,000' 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.crystal_id             1 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS EIGER2 XE 9M' 
_diffrn_detector.pdbx_collection_date   2025-01-17 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.92201 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'DIAMOND BEAMLINE I04-1' 
_diffrn_source.pdbx_wavelength_list        0.92201 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I45 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             46.87 
_reflns.d_resolution_high            1.39 
_reflns.number_obs                   57579 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.074 
_reflns.pdbx_netI_over_sigmaI        9.8 
_reflns.pdbx_redundancy              4.8 
_reflns.pdbx_Rrim_I_all              0.082 
_reflns.pdbx_Rpim_I_all              0.036 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_number_measured_all     279020 
_reflns.pdbx_chi_squared             0.86 
_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                  1.39 
_reflns_shell.d_res_low                   1.46 
_reflns_shell.number_measured_all         28369 
_reflns_shell.number_unique_obs           8305 
_reflns_shell.Rmerge_I_obs                1.163 
_reflns_shell.pdbx_chi_squared            0.70 
_reflns_shell.pdbx_redundancy             3.4 
_reflns_shell.percent_possible_obs        99.3 
_reflns_shell.pdbx_netI_over_sigmaI_obs   1.0 
_reflns_shell.pdbx_Rrim_I_all             1.361 
_reflns_shell.pdbx_Rpim_I_all             0.693 
_reflns_shell.pdbx_CC_half                0.459 
_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                                 7I45 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     57535 
_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                             19.92 
_refine.ls_d_res_high                            1.390 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_R_factor_obs                          0.1825 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1816 
_refine.ls_R_factor_R_free                       0.2001 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.910 
_refine.ls_number_reflns_R_free                  2824 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.966 
_refine.correlation_coeff_Fo_to_Fc_free          0.958 
_refine.B_iso_mean                               22.61 
_refine.aniso_B[1][1]                            -0.61710 
_refine.aniso_B[2][2]                            0.52710 
_refine.aniso_B[3][3]                            0.09000 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            1.02680 
_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             0.058 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.058 
_refine.pdbx_overall_SU_R_Blow_DPI               0.061 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.060 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I45 
_refine_analyze.Luzzati_coordinate_error_obs    0.17 
_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        2148 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         74 
_refine_hist.number_atoms_solvent             291 
_refine_hist.number_atoms_total               2513 
_refine_hist.d_res_high                       1.390 
_refine_hist.d_res_low                        19.92 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
t_bond_d                  0.011 ? 2.00  2282 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               1.03  ? 2.00  3103 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  767  '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 2282 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.65  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.90 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  277  '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  1963 '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                       1.39 
_refine_ls_shell.d_res_low                        1.40 
_refine_ls_shell.number_reflns_R_work             1094 
_refine_ls_shell.R_factor_R_work                  0.3180 
_refine_ls_shell.percent_reflns_obs               97.14 
_refine_ls_shell.R_factor_R_free                  0.3341 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.95 
_refine_ls_shell.number_reflns_R_free             57 
_refine_ls_shell.number_reflns_all                1151 
_refine_ls_shell.R_factor_all                     0.3188 
# 
_struct.entry_id                  7I45 
_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-0036599-001 (A71EV2A-x4669)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I45 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN' 
_struct_keywords.text            
;Diamond Light Source, I04-1, ASAP, A71 2A, enterovirus, protease, crystallographic fragment screening, PanDDA, PanDDa2, XChemExplorer, VIRAL PROTEIN
;
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 2 ? 
H N N 5 ? 
I N N 4 ? 
J N N 3 ? 
K N N 4 ? 
L N N 4 ? 
M N N 6 ? 
N N N 6 ? 
# 
_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 7I45 A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I45 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,E,F,M     
2 1 B,G,H,I,J,K,L,N 
# 
_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 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 ? ? ? ? ? ? ? 2.335 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.343 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.294 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.109 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 J ZN . ZN ? ? C CYS 56  C ZN 204 1_555 ? ? ? ? ? ? ? 2.334 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 J ZN . ZN ? ? C CYS 58  C ZN 204 1_555 ? ? ? ? ? ? ? 2.341 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 J ZN . ZN ? ? C CYS 116 C ZN 204 1_555 ? ? ? ? ? ? ? 2.322 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 J ZN . ZN ? ? C HIS 118 C ZN 204 1_555 ? ? ? ? ? ? ? 2.096 ? ? 
# 
_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_555 110.3 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.5 ? 
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_555 116.1 ? 
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_555 107.2 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.2 ? 
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_555 113.2 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? J ZN . ? C ZN 204 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 109.6 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? J ZN . ? C ZN 204 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.5 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? J ZN . ? C ZN 204 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.1 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? J ZN . ? C ZN 204 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 108.3 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? J ZN . ? C ZN 204 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 101.0 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? J ZN . ? C ZN 204 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 114.1 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
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 
AA1 3 4 ? 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 ILE A 4   ? VAL A 6   ? ILE A 10  VAL A 12  
AA1 2 TYR A 9   ? ASN A 13  ? TYR A 15  ASN A 19  
AA1 3 LEU A 34  ? SER A 38  ? LEU A 40  SER A 44  
AA1 4 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
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 ILE A 4   ? N ILE A 10  O VAL A 11  ? O VAL A 17  
AA1 2 3 N VAL A 12  ? N VAL A 18  O LEU A 35  ? O LEU A 41  
AA1 3 4 O VAL A 36  ? O VAL A 42  N TRP A 27  ? N TRP A 33  
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 GLN A 89  ? O GLN A 95  N ILE A 76  ? N ILE A 82  
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                   7I45 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HOH 
_pdbx_validate_close_contact.auth_seq_id_1    354 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    375 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.79 
# 
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 19.8217 6.7095   18.3072 -0.0196 -0.0237 -0.0026 -0.0029 0.0022  -0.0031 0.7181 0.9825 0.4857 
-0.2450 -0.1282 0.0091 -0.0004 -0.0147 0.0919 0.0131 0.0208 0.0317  0.0224 0.0337  -0.0204 
'X-RAY DIFFRACTION' 2 ? refined 15.3975 -23.8221 14.2355 -0.0120 -0.0171 -0.0067 0.0004  -0.0026 -0.0053 0.5882 0.9732 0.3823 
0.2039  0.1479  0.0403 -0.0249 0.0117  0.0559 0.0333 0.0455 -0.0546 0.0119 -0.0066 -0.0206 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 442 ? 6.66 . 
2 1 O ? A HOH 443 ? 8.25 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLU 146 ? A GLU 140 
2  1 Y 1 A ALA 147 ? A ALA 141 
3  1 Y 1 A MET 148 ? A MET 142 
4  1 Y 1 A GLU 149 ? A GLU 143 
5  1 Y 1 A GLN 150 ? A GLN 144 
6  1 Y 1 C GLU 146 ? B GLU 140 
7  1 Y 1 C ALA 147 ? B ALA 141 
8  1 Y 1 C MET 148 ? B MET 142 
9  1 Y 1 C GLU 149 ? B GLU 143 
10 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 
A1B2J N1   N  N N 1   
A1B2J C4   C  N N 2   
A1B2J C5   C  N N 3   
A1B2J C6   C  N N 4   
A1B2J C7   C  Y N 5   
A1B2J C8   C  Y N 6   
A1B2J C10  C  Y N 7   
A1B2J C13  C  N N 8   
A1B2J C15  C  N N 9   
A1B2J CL   CL N N 10  
A1B2J C12  C  Y N 11  
A1B2J C11  C  Y N 12  
A1B2J O2   O  N N 13  
A1B2J C14  C  N N 14  
A1B2J O3   O  N N 15  
A1B2J C9   C  Y N 16  
A1B2J O1   O  N N 17  
A1B2J C3   C  N N 18  
A1B2J C2   C  N N 19  
A1B2J C1   C  N S 20  
A1B2J C    C  N N 21  
A1B2J O    O  N N 22  
A1B2J N    N  N N 23  
A1B2J H8   H  N N 24  
A1B2J H7   H  N N 25  
A1B2J H10  H  N N 26  
A1B2J H9   H  N N 27  
A1B2J H11  H  N N 28  
A1B2J H13  H  N N 29  
A1B2J H14  H  N N 30  
A1B2J H18  H  N N 31  
A1B2J H17  H  N N 32  
A1B2J H12  H  N N 33  
A1B2J H15  H  N N 34  
A1B2J H16  H  N N 35  
A1B2J H6   H  N N 36  
A1B2J H5   H  N N 37  
A1B2J H4   H  N N 38  
A1B2J H3   H  N N 39  
A1B2J H    H  N N 40  
A1B2J H2   H  N N 41  
A1B2J H1   H  N N 42  
ALA   N    N  N N 43  
ALA   CA   C  N S 44  
ALA   C    C  N N 45  
ALA   O    O  N N 46  
ALA   CB   C  N N 47  
ALA   OXT  O  N N 48  
ALA   H    H  N N 49  
ALA   H2   H  N N 50  
ALA   HA   H  N N 51  
ALA   HB1  H  N N 52  
ALA   HB2  H  N N 53  
ALA   HB3  H  N N 54  
ALA   HXT  H  N N 55  
ARG   N    N  N N 56  
ARG   CA   C  N S 57  
ARG   C    C  N N 58  
ARG   O    O  N N 59  
ARG   CB   C  N N 60  
ARG   CG   C  N N 61  
ARG   CD   C  N N 62  
ARG   NE   N  N N 63  
ARG   CZ   C  N N 64  
ARG   NH1  N  N N 65  
ARG   NH2  N  N N 66  
ARG   OXT  O  N N 67  
ARG   H    H  N N 68  
ARG   H2   H  N N 69  
ARG   HA   H  N N 70  
ARG   HB2  H  N N 71  
ARG   HB3  H  N N 72  
ARG   HG2  H  N N 73  
ARG   HG3  H  N N 74  
ARG   HD2  H  N N 75  
ARG   HD3  H  N N 76  
ARG   HE   H  N N 77  
ARG   HH11 H  N N 78  
ARG   HH12 H  N N 79  
ARG   HH21 H  N N 80  
ARG   HH22 H  N N 81  
ARG   HXT  H  N N 82  
ASN   N    N  N N 83  
ASN   CA   C  N S 84  
ASN   C    C  N N 85  
ASN   O    O  N N 86  
ASN   CB   C  N N 87  
ASN   CG   C  N N 88  
ASN   OD1  O  N N 89  
ASN   ND2  N  N N 90  
ASN   OXT  O  N N 91  
ASN   H    H  N N 92  
ASN   H2   H  N N 93  
ASN   HA   H  N N 94  
ASN   HB2  H  N N 95  
ASN   HB3  H  N N 96  
ASN   HD21 H  N N 97  
ASN   HD22 H  N N 98  
ASN   HXT  H  N N 99  
ASP   N    N  N N 100 
ASP   CA   C  N S 101 
ASP   C    C  N N 102 
ASP   O    O  N N 103 
ASP   CB   C  N N 104 
ASP   CG   C  N N 105 
ASP   OD1  O  N N 106 
ASP   OD2  O  N N 107 
ASP   OXT  O  N N 108 
ASP   H    H  N N 109 
ASP   H2   H  N N 110 
ASP   HA   H  N N 111 
ASP   HB2  H  N N 112 
ASP   HB3  H  N N 113 
ASP   HD2  H  N N 114 
ASP   HXT  H  N N 115 
CYS   N    N  N N 116 
CYS   CA   C  N R 117 
CYS   C    C  N N 118 
CYS   O    O  N N 119 
CYS   CB   C  N N 120 
CYS   SG   S  N N 121 
CYS   OXT  O  N N 122 
CYS   H    H  N N 123 
CYS   H2   H  N N 124 
CYS   HA   H  N N 125 
CYS   HB2  H  N N 126 
CYS   HB3  H  N N 127 
CYS   HG   H  N N 128 
CYS   HXT  H  N N 129 
DMS   S    S  N N 130 
DMS   O    O  N N 131 
DMS   C1   C  N N 132 
DMS   C2   C  N N 133 
DMS   H11  H  N N 134 
DMS   H12  H  N N 135 
DMS   H13  H  N N 136 
DMS   H21  H  N N 137 
DMS   H22  H  N N 138 
DMS   H23  H  N N 139 
GLN   N    N  N N 140 
GLN   CA   C  N S 141 
GLN   C    C  N N 142 
GLN   O    O  N N 143 
GLN   CB   C  N N 144 
GLN   CG   C  N N 145 
GLN   CD   C  N N 146 
GLN   OE1  O  N N 147 
GLN   NE2  N  N N 148 
GLN   OXT  O  N N 149 
GLN   H    H  N N 150 
GLN   H2   H  N N 151 
GLN   HA   H  N N 152 
GLN   HB2  H  N N 153 
GLN   HB3  H  N N 154 
GLN   HG2  H  N N 155 
GLN   HG3  H  N N 156 
GLN   HE21 H  N N 157 
GLN   HE22 H  N N 158 
GLN   HXT  H  N N 159 
GLU   N    N  N N 160 
GLU   CA   C  N S 161 
GLU   C    C  N N 162 
GLU   O    O  N N 163 
GLU   CB   C  N N 164 
GLU   CG   C  N N 165 
GLU   CD   C  N N 166 
GLU   OE1  O  N N 167 
GLU   OE2  O  N N 168 
GLU   OXT  O  N N 169 
GLU   H    H  N N 170 
GLU   H2   H  N N 171 
GLU   HA   H  N N 172 
GLU   HB2  H  N N 173 
GLU   HB3  H  N N 174 
GLU   HG2  H  N N 175 
GLU   HG3  H  N N 176 
GLU   HE2  H  N N 177 
GLU   HXT  H  N N 178 
GLY   N    N  N N 179 
GLY   CA   C  N N 180 
GLY   C    C  N N 181 
GLY   O    O  N N 182 
GLY   OXT  O  N N 183 
GLY   H    H  N N 184 
GLY   H2   H  N N 185 
GLY   HA2  H  N N 186 
GLY   HA3  H  N N 187 
GLY   HXT  H  N N 188 
GOL   C1   C  N N 189 
GOL   O1   O  N N 190 
GOL   C2   C  N N 191 
GOL   O2   O  N N 192 
GOL   C3   C  N N 193 
GOL   O3   O  N N 194 
GOL   H11  H  N N 195 
GOL   H12  H  N N 196 
GOL   HO1  H  N N 197 
GOL   H2   H  N N 198 
GOL   HO2  H  N N 199 
GOL   H31  H  N N 200 
GOL   H32  H  N N 201 
GOL   HO3  H  N N 202 
HIS   N    N  N N 203 
HIS   CA   C  N S 204 
HIS   C    C  N N 205 
HIS   O    O  N N 206 
HIS   CB   C  N N 207 
HIS   CG   C  Y N 208 
HIS   ND1  N  Y N 209 
HIS   CD2  C  Y N 210 
HIS   CE1  C  Y N 211 
HIS   NE2  N  Y N 212 
HIS   OXT  O  N N 213 
HIS   H    H  N N 214 
HIS   H2   H  N N 215 
HIS   HA   H  N N 216 
HIS   HB2  H  N N 217 
HIS   HB3  H  N N 218 
HIS   HD1  H  N N 219 
HIS   HD2  H  N N 220 
HIS   HE1  H  N N 221 
HIS   HE2  H  N N 222 
HIS   HXT  H  N N 223 
HOH   O    O  N N 224 
HOH   H1   H  N N 225 
HOH   H2   H  N N 226 
ILE   N    N  N N 227 
ILE   CA   C  N S 228 
ILE   C    C  N N 229 
ILE   O    O  N N 230 
ILE   CB   C  N S 231 
ILE   CG1  C  N N 232 
ILE   CG2  C  N N 233 
ILE   CD1  C  N N 234 
ILE   OXT  O  N N 235 
ILE   H    H  N N 236 
ILE   H2   H  N N 237 
ILE   HA   H  N N 238 
ILE   HB   H  N N 239 
ILE   HG12 H  N N 240 
ILE   HG13 H  N N 241 
ILE   HG21 H  N N 242 
ILE   HG22 H  N N 243 
ILE   HG23 H  N N 244 
ILE   HD11 H  N N 245 
ILE   HD12 H  N N 246 
ILE   HD13 H  N N 247 
ILE   HXT  H  N N 248 
LEU   N    N  N N 249 
LEU   CA   C  N S 250 
LEU   C    C  N N 251 
LEU   O    O  N N 252 
LEU   CB   C  N N 253 
LEU   CG   C  N N 254 
LEU   CD1  C  N N 255 
LEU   CD2  C  N N 256 
LEU   OXT  O  N N 257 
LEU   H    H  N N 258 
LEU   H2   H  N N 259 
LEU   HA   H  N N 260 
LEU   HB2  H  N N 261 
LEU   HB3  H  N N 262 
LEU   HG   H  N N 263 
LEU   HD11 H  N N 264 
LEU   HD12 H  N N 265 
LEU   HD13 H  N N 266 
LEU   HD21 H  N N 267 
LEU   HD22 H  N N 268 
LEU   HD23 H  N N 269 
LEU   HXT  H  N N 270 
LYS   N    N  N N 271 
LYS   CA   C  N S 272 
LYS   C    C  N N 273 
LYS   O    O  N N 274 
LYS   CB   C  N N 275 
LYS   CG   C  N N 276 
LYS   CD   C  N N 277 
LYS   CE   C  N N 278 
LYS   NZ   N  N N 279 
LYS   OXT  O  N N 280 
LYS   H    H  N N 281 
LYS   H2   H  N N 282 
LYS   HA   H  N N 283 
LYS   HB2  H  N N 284 
LYS   HB3  H  N N 285 
LYS   HG2  H  N N 286 
LYS   HG3  H  N N 287 
LYS   HD2  H  N N 288 
LYS   HD3  H  N N 289 
LYS   HE2  H  N N 290 
LYS   HE3  H  N N 291 
LYS   HZ1  H  N N 292 
LYS   HZ2  H  N N 293 
LYS   HZ3  H  N N 294 
LYS   HXT  H  N N 295 
MET   N    N  N N 296 
MET   CA   C  N S 297 
MET   C    C  N N 298 
MET   O    O  N N 299 
MET   CB   C  N N 300 
MET   CG   C  N N 301 
MET   SD   S  N N 302 
MET   CE   C  N N 303 
MET   OXT  O  N N 304 
MET   H    H  N N 305 
MET   H2   H  N N 306 
MET   HA   H  N N 307 
MET   HB2  H  N N 308 
MET   HB3  H  N N 309 
MET   HG2  H  N N 310 
MET   HG3  H  N N 311 
MET   HE1  H  N N 312 
MET   HE2  H  N N 313 
MET   HE3  H  N N 314 
MET   HXT  H  N N 315 
PHE   N    N  N N 316 
PHE   CA   C  N S 317 
PHE   C    C  N N 318 
PHE   O    O  N N 319 
PHE   CB   C  N N 320 
PHE   CG   C  Y N 321 
PHE   CD1  C  Y N 322 
PHE   CD2  C  Y N 323 
PHE   CE1  C  Y N 324 
PHE   CE2  C  Y N 325 
PHE   CZ   C  Y N 326 
PHE   OXT  O  N N 327 
PHE   H    H  N N 328 
PHE   H2   H  N N 329 
PHE   HA   H  N N 330 
PHE   HB2  H  N N 331 
PHE   HB3  H  N N 332 
PHE   HD1  H  N N 333 
PHE   HD2  H  N N 334 
PHE   HE1  H  N N 335 
PHE   HE2  H  N N 336 
PHE   HZ   H  N N 337 
PHE   HXT  H  N N 338 
PRO   N    N  N N 339 
PRO   CA   C  N S 340 
PRO   C    C  N N 341 
PRO   O    O  N N 342 
PRO   CB   C  N N 343 
PRO   CG   C  N N 344 
PRO   CD   C  N N 345 
PRO   OXT  O  N N 346 
PRO   H    H  N N 347 
PRO   HA   H  N N 348 
PRO   HB2  H  N N 349 
PRO   HB3  H  N N 350 
PRO   HG2  H  N N 351 
PRO   HG3  H  N N 352 
PRO   HD2  H  N N 353 
PRO   HD3  H  N N 354 
PRO   HXT  H  N N 355 
SER   N    N  N N 356 
SER   CA   C  N S 357 
SER   C    C  N N 358 
SER   O    O  N N 359 
SER   CB   C  N N 360 
SER   OG   O  N N 361 
SER   OXT  O  N N 362 
SER   H    H  N N 363 
SER   H2   H  N N 364 
SER   HA   H  N N 365 
SER   HB2  H  N N 366 
SER   HB3  H  N N 367 
SER   HG   H  N N 368 
SER   HXT  H  N N 369 
THR   N    N  N N 370 
THR   CA   C  N S 371 
THR   C    C  N N 372 
THR   O    O  N N 373 
THR   CB   C  N R 374 
THR   OG1  O  N N 375 
THR   CG2  C  N N 376 
THR   OXT  O  N N 377 
THR   H    H  N N 378 
THR   H2   H  N N 379 
THR   HA   H  N N 380 
THR   HB   H  N N 381 
THR   HG1  H  N N 382 
THR   HG21 H  N N 383 
THR   HG22 H  N N 384 
THR   HG23 H  N N 385 
THR   HXT  H  N N 386 
TRP   N    N  N N 387 
TRP   CA   C  N S 388 
TRP   C    C  N N 389 
TRP   O    O  N N 390 
TRP   CB   C  N N 391 
TRP   CG   C  Y N 392 
TRP   CD1  C  Y N 393 
TRP   CD2  C  Y N 394 
TRP   NE1  N  Y N 395 
TRP   CE2  C  Y N 396 
TRP   CE3  C  Y N 397 
TRP   CZ2  C  Y N 398 
TRP   CZ3  C  Y N 399 
TRP   CH2  C  Y N 400 
TRP   OXT  O  N N 401 
TRP   H    H  N N 402 
TRP   H2   H  N N 403 
TRP   HA   H  N N 404 
TRP   HB2  H  N N 405 
TRP   HB3  H  N N 406 
TRP   HD1  H  N N 407 
TRP   HE1  H  N N 408 
TRP   HE3  H  N N 409 
TRP   HZ2  H  N N 410 
TRP   HZ3  H  N N 411 
TRP   HH2  H  N N 412 
TRP   HXT  H  N N 413 
TYR   N    N  N N 414 
TYR   CA   C  N S 415 
TYR   C    C  N N 416 
TYR   O    O  N N 417 
TYR   CB   C  N N 418 
TYR   CG   C  Y N 419 
TYR   CD1  C  Y N 420 
TYR   CD2  C  Y N 421 
TYR   CE1  C  Y N 422 
TYR   CE2  C  Y N 423 
TYR   CZ   C  Y N 424 
TYR   OH   O  N N 425 
TYR   OXT  O  N N 426 
TYR   H    H  N N 427 
TYR   H2   H  N N 428 
TYR   HA   H  N N 429 
TYR   HB2  H  N N 430 
TYR   HB3  H  N N 431 
TYR   HD1  H  N N 432 
TYR   HD2  H  N N 433 
TYR   HE1  H  N N 434 
TYR   HE2  H  N N 435 
TYR   HH   H  N N 436 
TYR   HXT  H  N N 437 
VAL   N    N  N N 438 
VAL   CA   C  N S 439 
VAL   C    C  N N 440 
VAL   O    O  N N 441 
VAL   CB   C  N N 442 
VAL   CG1  C  N N 443 
VAL   CG2  C  N N 444 
VAL   OXT  O  N N 445 
VAL   H    H  N N 446 
VAL   H2   H  N N 447 
VAL   HA   H  N N 448 
VAL   HB   H  N N 449 
VAL   HG11 H  N N 450 
VAL   HG12 H  N N 451 
VAL   HG13 H  N N 452 
VAL   HG21 H  N N 453 
VAL   HG22 H  N N 454 
VAL   HG23 H  N N 455 
VAL   HXT  H  N N 456 
ZN    ZN   ZN N N 457 
# 
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 
A1B2J N   C    sing N N 1   
A1B2J O   C    doub N N 2   
A1B2J C   C1   sing N N 3   
A1B2J C1  C2   sing N N 4   
A1B2J C2  C3   sing N N 5   
A1B2J C3  C4   sing N N 6   
A1B2J C4  N1   sing N N 7   
A1B2J N1  C5   sing N N 8   
A1B2J O1  C5   doub N N 9   
A1B2J C5  C6   sing N N 10  
A1B2J C6  C7   sing N N 11  
A1B2J C7  C8   sing Y N 12  
A1B2J C8  C9   doub Y N 13  
A1B2J C9  C10  sing Y N 14  
A1B2J C10 C11  doub Y N 15  
A1B2J C11 C12  sing Y N 16  
A1B2J C7  C12  doub Y N 17  
A1B2J C12 CL   sing N N 18  
A1B2J O2  C10  sing N N 19  
A1B2J C13 O2   sing N N 20  
A1B2J C14 C13  sing N N 21  
A1B2J O3  C14  sing N N 22  
A1B2J C9  O3   sing N N 23  
A1B2J C15 N1   sing N N 24  
A1B2J C1  C15  sing N N 25  
A1B2J C4  H8   sing N N 26  
A1B2J C4  H7   sing N N 27  
A1B2J C6  H10  sing N N 28  
A1B2J C6  H9   sing N N 29  
A1B2J C8  H11  sing N N 30  
A1B2J C13 H13  sing N N 31  
A1B2J C13 H14  sing N N 32  
A1B2J C15 H18  sing N N 33  
A1B2J C15 H17  sing N N 34  
A1B2J C11 H12  sing N N 35  
A1B2J C14 H15  sing N N 36  
A1B2J C14 H16  sing N N 37  
A1B2J C3  H6   sing N N 38  
A1B2J C3  H5   sing N N 39  
A1B2J C2  H4   sing N N 40  
A1B2J C2  H3   sing N N 41  
A1B2J C1  H    sing N N 42  
A1B2J N   H2   sing N N 43  
A1B2J N   H1   sing N N 44  
ALA   N   CA   sing N N 45  
ALA   N   H    sing N N 46  
ALA   N   H2   sing N N 47  
ALA   CA  C    sing N N 48  
ALA   CA  CB   sing N N 49  
ALA   CA  HA   sing N N 50  
ALA   C   O    doub N N 51  
ALA   C   OXT  sing N N 52  
ALA   CB  HB1  sing N N 53  
ALA   CB  HB2  sing N N 54  
ALA   CB  HB3  sing N N 55  
ALA   OXT HXT  sing N N 56  
ARG   N   CA   sing N N 57  
ARG   N   H    sing N N 58  
ARG   N   H2   sing N N 59  
ARG   CA  C    sing N N 60  
ARG   CA  CB   sing N N 61  
ARG   CA  HA   sing N N 62  
ARG   C   O    doub N N 63  
ARG   C   OXT  sing N N 64  
ARG   CB  CG   sing N N 65  
ARG   CB  HB2  sing N N 66  
ARG   CB  HB3  sing N N 67  
ARG   CG  CD   sing N N 68  
ARG   CG  HG2  sing N N 69  
ARG   CG  HG3  sing N N 70  
ARG   CD  NE   sing N N 71  
ARG   CD  HD2  sing N N 72  
ARG   CD  HD3  sing N N 73  
ARG   NE  CZ   sing N N 74  
ARG   NE  HE   sing N N 75  
ARG   CZ  NH1  sing N N 76  
ARG   CZ  NH2  doub N N 77  
ARG   NH1 HH11 sing N N 78  
ARG   NH1 HH12 sing N N 79  
ARG   NH2 HH21 sing N N 80  
ARG   NH2 HH22 sing N N 81  
ARG   OXT HXT  sing N N 82  
ASN   N   CA   sing N N 83  
ASN   N   H    sing N N 84  
ASN   N   H2   sing N N 85  
ASN   CA  C    sing N N 86  
ASN   CA  CB   sing N N 87  
ASN   CA  HA   sing N N 88  
ASN   C   O    doub N N 89  
ASN   C   OXT  sing N N 90  
ASN   CB  CG   sing N N 91  
ASN   CB  HB2  sing N N 92  
ASN   CB  HB3  sing N N 93  
ASN   CG  OD1  doub N N 94  
ASN   CG  ND2  sing N N 95  
ASN   ND2 HD21 sing N N 96  
ASN   ND2 HD22 sing N N 97  
ASN   OXT HXT  sing N N 98  
ASP   N   CA   sing N N 99  
ASP   N   H    sing N N 100 
ASP   N   H2   sing N N 101 
ASP   CA  C    sing N N 102 
ASP   CA  CB   sing N N 103 
ASP   CA  HA   sing N N 104 
ASP   C   O    doub N N 105 
ASP   C   OXT  sing N N 106 
ASP   CB  CG   sing N N 107 
ASP   CB  HB2  sing N N 108 
ASP   CB  HB3  sing N N 109 
ASP   CG  OD1  doub N N 110 
ASP   CG  OD2  sing N N 111 
ASP   OD2 HD2  sing N N 112 
ASP   OXT HXT  sing N N 113 
CYS   N   CA   sing N N 114 
CYS   N   H    sing N N 115 
CYS   N   H2   sing N N 116 
CYS   CA  C    sing N N 117 
CYS   CA  CB   sing N N 118 
CYS   CA  HA   sing N N 119 
CYS   C   O    doub N N 120 
CYS   C   OXT  sing N N 121 
CYS   CB  SG   sing N N 122 
CYS   CB  HB2  sing N N 123 
CYS   CB  HB3  sing N N 124 
CYS   SG  HG   sing N N 125 
CYS   OXT HXT  sing N N 126 
DMS   S   O    doub N N 127 
DMS   S   C1   sing N N 128 
DMS   S   C2   sing N N 129 
DMS   C1  H11  sing N N 130 
DMS   C1  H12  sing N N 131 
DMS   C1  H13  sing N N 132 
DMS   C2  H21  sing N N 133 
DMS   C2  H22  sing N N 134 
DMS   C2  H23  sing N N 135 
GLN   N   CA   sing N N 136 
GLN   N   H    sing N N 137 
GLN   N   H2   sing N N 138 
GLN   CA  C    sing N N 139 
GLN   CA  CB   sing N N 140 
GLN   CA  HA   sing N N 141 
GLN   C   O    doub N N 142 
GLN   C   OXT  sing N N 143 
GLN   CB  CG   sing N N 144 
GLN   CB  HB2  sing N N 145 
GLN   CB  HB3  sing N N 146 
GLN   CG  CD   sing N N 147 
GLN   CG  HG2  sing N N 148 
GLN   CG  HG3  sing N N 149 
GLN   CD  OE1  doub N N 150 
GLN   CD  NE2  sing N N 151 
GLN   NE2 HE21 sing N N 152 
GLN   NE2 HE22 sing N N 153 
GLN   OXT HXT  sing N N 154 
GLU   N   CA   sing N N 155 
GLU   N   H    sing N N 156 
GLU   N   H2   sing N N 157 
GLU   CA  C    sing N N 158 
GLU   CA  CB   sing N N 159 
GLU   CA  HA   sing N N 160 
GLU   C   O    doub N N 161 
GLU   C   OXT  sing N N 162 
GLU   CB  CG   sing N N 163 
GLU   CB  HB2  sing N N 164 
GLU   CB  HB3  sing N N 165 
GLU   CG  CD   sing N N 166 
GLU   CG  HG2  sing N N 167 
GLU   CG  HG3  sing N N 168 
GLU   CD  OE1  doub N N 169 
GLU   CD  OE2  sing N N 170 
GLU   OE2 HE2  sing N N 171 
GLU   OXT HXT  sing N N 172 
GLY   N   CA   sing N N 173 
GLY   N   H    sing N N 174 
GLY   N   H2   sing N N 175 
GLY   CA  C    sing N N 176 
GLY   CA  HA2  sing N N 177 
GLY   CA  HA3  sing N N 178 
GLY   C   O    doub N N 179 
GLY   C   OXT  sing N N 180 
GLY   OXT HXT  sing N N 181 
GOL   C1  O1   sing N N 182 
GOL   C1  C2   sing N N 183 
GOL   C1  H11  sing N N 184 
GOL   C1  H12  sing N N 185 
GOL   O1  HO1  sing N N 186 
GOL   C2  O2   sing N N 187 
GOL   C2  C3   sing N N 188 
GOL   C2  H2   sing N N 189 
GOL   O2  HO2  sing N N 190 
GOL   C3  O3   sing N N 191 
GOL   C3  H31  sing N N 192 
GOL   C3  H32  sing N N 193 
GOL   O3  HO3  sing N N 194 
HIS   N   CA   sing N N 195 
HIS   N   H    sing N N 196 
HIS   N   H2   sing N N 197 
HIS   CA  C    sing N N 198 
HIS   CA  CB   sing N N 199 
HIS   CA  HA   sing N N 200 
HIS   C   O    doub N N 201 
HIS   C   OXT  sing N N 202 
HIS   CB  CG   sing N N 203 
HIS   CB  HB2  sing N N 204 
HIS   CB  HB3  sing N N 205 
HIS   CG  ND1  sing Y N 206 
HIS   CG  CD2  doub Y N 207 
HIS   ND1 CE1  doub Y N 208 
HIS   ND1 HD1  sing N N 209 
HIS   CD2 NE2  sing Y N 210 
HIS   CD2 HD2  sing N N 211 
HIS   CE1 NE2  sing Y N 212 
HIS   CE1 HE1  sing N N 213 
HIS   NE2 HE2  sing N N 214 
HIS   OXT HXT  sing N N 215 
HOH   O   H1   sing N N 216 
HOH   O   H2   sing N N 217 
ILE   N   CA   sing N N 218 
ILE   N   H    sing N N 219 
ILE   N   H2   sing N N 220 
ILE   CA  C    sing N N 221 
ILE   CA  CB   sing N N 222 
ILE   CA  HA   sing N N 223 
ILE   C   O    doub N N 224 
ILE   C   OXT  sing N N 225 
ILE   CB  CG1  sing N N 226 
ILE   CB  CG2  sing N N 227 
ILE   CB  HB   sing N N 228 
ILE   CG1 CD1  sing N N 229 
ILE   CG1 HG12 sing N N 230 
ILE   CG1 HG13 sing N N 231 
ILE   CG2 HG21 sing N N 232 
ILE   CG2 HG22 sing N N 233 
ILE   CG2 HG23 sing N N 234 
ILE   CD1 HD11 sing N N 235 
ILE   CD1 HD12 sing N N 236 
ILE   CD1 HD13 sing N N 237 
ILE   OXT HXT  sing N N 238 
LEU   N   CA   sing N N 239 
LEU   N   H    sing N N 240 
LEU   N   H2   sing N N 241 
LEU   CA  C    sing N N 242 
LEU   CA  CB   sing N N 243 
LEU   CA  HA   sing N N 244 
LEU   C   O    doub N N 245 
LEU   C   OXT  sing N N 246 
LEU   CB  CG   sing N N 247 
LEU   CB  HB2  sing N N 248 
LEU   CB  HB3  sing N N 249 
LEU   CG  CD1  sing N N 250 
LEU   CG  CD2  sing N N 251 
LEU   CG  HG   sing N N 252 
LEU   CD1 HD11 sing N N 253 
LEU   CD1 HD12 sing N N 254 
LEU   CD1 HD13 sing N N 255 
LEU   CD2 HD21 sing N N 256 
LEU   CD2 HD22 sing N N 257 
LEU   CD2 HD23 sing N N 258 
LEU   OXT HXT  sing N N 259 
LYS   N   CA   sing N N 260 
LYS   N   H    sing N N 261 
LYS   N   H2   sing N N 262 
LYS   CA  C    sing N N 263 
LYS   CA  CB   sing N N 264 
LYS   CA  HA   sing N N 265 
LYS   C   O    doub N N 266 
LYS   C   OXT  sing N N 267 
LYS   CB  CG   sing N N 268 
LYS   CB  HB2  sing N N 269 
LYS   CB  HB3  sing N N 270 
LYS   CG  CD   sing N N 271 
LYS   CG  HG2  sing N N 272 
LYS   CG  HG3  sing N N 273 
LYS   CD  CE   sing N N 274 
LYS   CD  HD2  sing N N 275 
LYS   CD  HD3  sing N N 276 
LYS   CE  NZ   sing N N 277 
LYS   CE  HE2  sing N N 278 
LYS   CE  HE3  sing N N 279 
LYS   NZ  HZ1  sing N N 280 
LYS   NZ  HZ2  sing N N 281 
LYS   NZ  HZ3  sing N N 282 
LYS   OXT HXT  sing N N 283 
MET   N   CA   sing N N 284 
MET   N   H    sing N N 285 
MET   N   H2   sing N N 286 
MET   CA  C    sing N N 287 
MET   CA  CB   sing N N 288 
MET   CA  HA   sing N N 289 
MET   C   O    doub N N 290 
MET   C   OXT  sing N N 291 
MET   CB  CG   sing N N 292 
MET   CB  HB2  sing N N 293 
MET   CB  HB3  sing N N 294 
MET   CG  SD   sing N N 295 
MET   CG  HG2  sing N N 296 
MET   CG  HG3  sing N N 297 
MET   SD  CE   sing N N 298 
MET   CE  HE1  sing N N 299 
MET   CE  HE2  sing N N 300 
MET   CE  HE3  sing N N 301 
MET   OXT HXT  sing N N 302 
PHE   N   CA   sing N N 303 
PHE   N   H    sing N N 304 
PHE   N   H2   sing N N 305 
PHE   CA  C    sing N N 306 
PHE   CA  CB   sing N N 307 
PHE   CA  HA   sing N N 308 
PHE   C   O    doub N N 309 
PHE   C   OXT  sing N N 310 
PHE   CB  CG   sing N N 311 
PHE   CB  HB2  sing N N 312 
PHE   CB  HB3  sing N N 313 
PHE   CG  CD1  doub Y N 314 
PHE   CG  CD2  sing Y N 315 
PHE   CD1 CE1  sing Y N 316 
PHE   CD1 HD1  sing N N 317 
PHE   CD2 CE2  doub Y N 318 
PHE   CD2 HD2  sing N N 319 
PHE   CE1 CZ   doub Y N 320 
PHE   CE1 HE1  sing N N 321 
PHE   CE2 CZ   sing Y N 322 
PHE   CE2 HE2  sing N N 323 
PHE   CZ  HZ   sing N N 324 
PHE   OXT HXT  sing N N 325 
PRO   N   CA   sing N N 326 
PRO   N   CD   sing N N 327 
PRO   N   H    sing N N 328 
PRO   CA  C    sing N N 329 
PRO   CA  CB   sing N N 330 
PRO   CA  HA   sing N N 331 
PRO   C   O    doub N N 332 
PRO   C   OXT  sing N N 333 
PRO   CB  CG   sing N N 334 
PRO   CB  HB2  sing N N 335 
PRO   CB  HB3  sing N N 336 
PRO   CG  CD   sing N N 337 
PRO   CG  HG2  sing N N 338 
PRO   CG  HG3  sing N N 339 
PRO   CD  HD2  sing N N 340 
PRO   CD  HD3  sing N N 341 
PRO   OXT HXT  sing N N 342 
SER   N   CA   sing N N 343 
SER   N   H    sing N N 344 
SER   N   H2   sing N N 345 
SER   CA  C    sing N N 346 
SER   CA  CB   sing N N 347 
SER   CA  HA   sing N N 348 
SER   C   O    doub N N 349 
SER   C   OXT  sing N N 350 
SER   CB  OG   sing N N 351 
SER   CB  HB2  sing N N 352 
SER   CB  HB3  sing N N 353 
SER   OG  HG   sing N N 354 
SER   OXT HXT  sing N N 355 
THR   N   CA   sing N N 356 
THR   N   H    sing N N 357 
THR   N   H2   sing N N 358 
THR   CA  C    sing N N 359 
THR   CA  CB   sing N N 360 
THR   CA  HA   sing N N 361 
THR   C   O    doub N N 362 
THR   C   OXT  sing N N 363 
THR   CB  OG1  sing N N 364 
THR   CB  CG2  sing N N 365 
THR   CB  HB   sing N N 366 
THR   OG1 HG1  sing N N 367 
THR   CG2 HG21 sing N N 368 
THR   CG2 HG22 sing N N 369 
THR   CG2 HG23 sing N N 370 
THR   OXT HXT  sing N N 371 
TRP   N   CA   sing N N 372 
TRP   N   H    sing N N 373 
TRP   N   H2   sing N N 374 
TRP   CA  C    sing N N 375 
TRP   CA  CB   sing N N 376 
TRP   CA  HA   sing N N 377 
TRP   C   O    doub N N 378 
TRP   C   OXT  sing N N 379 
TRP   CB  CG   sing N N 380 
TRP   CB  HB2  sing N N 381 
TRP   CB  HB3  sing N N 382 
TRP   CG  CD1  doub Y N 383 
TRP   CG  CD2  sing Y N 384 
TRP   CD1 NE1  sing Y N 385 
TRP   CD1 HD1  sing N N 386 
TRP   CD2 CE2  doub Y N 387 
TRP   CD2 CE3  sing Y N 388 
TRP   NE1 CE2  sing Y N 389 
TRP   NE1 HE1  sing N N 390 
TRP   CE2 CZ2  sing Y N 391 
TRP   CE3 CZ3  doub Y N 392 
TRP   CE3 HE3  sing N N 393 
TRP   CZ2 CH2  doub Y N 394 
TRP   CZ2 HZ2  sing N N 395 
TRP   CZ3 CH2  sing Y N 396 
TRP   CZ3 HZ3  sing N N 397 
TRP   CH2 HH2  sing N N 398 
TRP   OXT HXT  sing N N 399 
TYR   N   CA   sing N N 400 
TYR   N   H    sing N N 401 
TYR   N   H2   sing N N 402 
TYR   CA  C    sing N N 403 
TYR   CA  CB   sing N N 404 
TYR   CA  HA   sing N N 405 
TYR   C   O    doub N N 406 
TYR   C   OXT  sing N N 407 
TYR   CB  CG   sing N N 408 
TYR   CB  HB2  sing N N 409 
TYR   CB  HB3  sing N N 410 
TYR   CG  CD1  doub Y N 411 
TYR   CG  CD2  sing Y N 412 
TYR   CD1 CE1  sing Y N 413 
TYR   CD1 HD1  sing N N 414 
TYR   CD2 CE2  doub Y N 415 
TYR   CD2 HD2  sing N N 416 
TYR   CE1 CZ   doub Y N 417 
TYR   CE1 HE1  sing N N 418 
TYR   CE2 CZ   sing Y N 419 
TYR   CE2 HE2  sing N N 420 
TYR   CZ  OH   sing N N 421 
TYR   OH  HH   sing N N 422 
TYR   OXT HXT  sing N N 423 
VAL   N   CA   sing N N 424 
VAL   N   H    sing N N 425 
VAL   N   H2   sing N N 426 
VAL   CA  C    sing N N 427 
VAL   CA  CB   sing N N 428 
VAL   CA  HA   sing N N 429 
VAL   C   O    doub N N 430 
VAL   C   OXT  sing N N 431 
VAL   CB  CG1  sing N N 432 
VAL   CB  CG2  sing N N 433 
VAL   CB  HB   sing N N 434 
VAL   CG1 HG11 sing N N 435 
VAL   CG1 HG12 sing N N 436 
VAL   CG1 HG13 sing N N 437 
VAL   CG2 HG21 sing N N 438 
VAL   CG2 HG22 sing N N 439 
VAL   CG2 HG23 sing N N 440 
VAL   OXT HXT  sing N N 441 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171399 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_id            G_1002344 
_pdbx_deposit_group.group_description   
'Crystollographic structure of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitor' 
_pdbx_deposit_group.group_title         
'Group deposition of Coxsackievirus A16 (G-10) 2A protease in complex with inhibitors from the ASAP AViDD centre' 
_pdbx_deposit_group.group_type          'changed state' 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   8POA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    7I45 
_atom_sites.fract_transf_matrix[1][1]   0.013794 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000595 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016267 
_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]   0.015342 
_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  
CL 
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   ? 16.463 6.496   8.211  1.00 20.10 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.236 6.624   9.017  1.00 20.66 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 15.073 5.455   9.996  1.00 20.09 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.713 4.425   9.842  1.00 20.85 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 14.024 6.703   8.084  1.00 24.12 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.841 5.468   7.405  1.00 28.20 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.229 5.625   11.021 1.00 18.56 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.911 4.576   11.973 1.00 18.29 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.502 5.092   13.343 1.00 16.89 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.821 6.236   13.716 1.00 17.47 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.753 4.254   14.091 1.00 15.48 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.309 4.660   15.411 1.00 16.42 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.247 3.457   16.343 1.00 16.64 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.173 2.301   15.878 1.00 17.89 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.902 5.253   15.302 1.00 17.70 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.289 3.737   17.668 1.00 14.73 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.064 2.748   18.708 1.00 14.97 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.655 2.963   19.223 1.00 15.93 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.303 4.078   19.569 1.00 16.60 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.054 2.921   19.881 1.00 15.01 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.514 2.825   19.378 1.00 15.37 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.814 1.868   20.947 1.00 16.91 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.485 3.404   20.399 1.00 17.75 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.844  1.907   19.299 1.00 15.80 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.486  2.028   19.852 1.00 17.27 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.440  1.236   21.136 1.00 17.52 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.518  0.006   21.079 1.00 18.55 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.446  1.478   18.855 1.00 17.66 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.345  2.321   17.609 1.00 19.59 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.467  3.389   17.541 1.00 22.54 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.128  2.046   16.503 1.00 21.48 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.376  4.168   16.394 1.00 23.14 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.067  2.825   15.368 1.00 23.30 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.185  3.878   15.312 1.00 24.29 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.165  4.662   14.182 1.00 27.61 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.372  1.909   22.295 1.00 16.87 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.363  1.264   23.611 1.00 17.75 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.238  1.833   24.433 1.00 19.23 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.133  3.053   24.557 1.00 19.40 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.742  1.412   24.332 1.00 19.39 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.222 2.867   24.325 1.00 19.35 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.678  0.871   25.769 1.00 21.25 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.321  0.985   24.918 1.00 20.86 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.178  1.478   25.686 1.00 21.38 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.365  2.464   24.858 1.00 21.21 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.119  2.195   23.685 1.00 21.68 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 4.068  3.650   25.412 1.00 21.54 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.355  4.665   24.624 1.00 22.56 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.302  5.761   24.153 1.00 19.95 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 3.904  6.931   24.033 1.00 20.00 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.168  5.256   25.378 1.00 26.43 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 1.096  4.230   25.638 1.00 33.78 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.462  3.714   24.716 1.00 37.32 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.910  3.896   26.893 1.00 35.28 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.557  5.385   23.840 1.00 18.25 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.558  6.344   23.379 1.00 17.41 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.150  5.895   22.042 1.00 15.86 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.263  4.685   21.760 1.00 15.99 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.718  6.438   24.386 1.00 18.30 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.305  6.969   25.743 1.00 18.78 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.684  8.205   25.871 1.00 19.69 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.555  6.247   26.897 1.00 20.08 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.358  8.726   27.117 1.00 20.25 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.230  6.758   28.149 1.00 20.55 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.594  7.985   28.249 1.00 21.86 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.285  8.519   29.481 1.00 25.22 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.570  6.897   21.241 1.00 15.18 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.277  6.711   19.995 1.00 16.04 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.607  7.506   20.150 1.00 16.06 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.558  8.700   20.461 1.00 16.28 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.413  7.219   18.824 1.00 18.05 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.152  7.451   17.531 1.00 19.28 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.207  7.803   16.393 1.00 20.17 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.787  8.795   15.490 1.00 21.62 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.157  8.563   14.239 1.00 23.97 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.056  7.340   13.725 1.00 25.52 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.666  9.545   13.497 1.00 23.08 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.769 6.843   19.991 1.00 15.45 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 12.072 7.504   20.087 1.00 15.15 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.644 7.649   18.698 1.00 15.15 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.782 6.640   17.985 1.00 15.22 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 13.070 6.698   20.964 1.00 15.33 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.340 7.528   21.216 1.00 15.65 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.427 6.250   22.286 1.00 15.38 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.977 8.874   18.293 1.00 13.58 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.546 9.095   16.947 1.00 14.31 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.788 10.011  17.056 1.00 13.33 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 15.017 10.695  18.082 1.00 14.35 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.499 9.773   16.008 1.00 16.03 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.345 8.826   15.699 1.00 18.82 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.978 11.093  16.626 1.00 16.61 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.556 10.117  15.947 1.00 12.42 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.606 11.141  15.878 1.00 12.41 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.908 12.496  15.880 1.00 13.57 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.946 12.705  15.109 1.00 14.67 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.381 11.007  14.569 1.00 12.91 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.192 9.754   14.510 1.00 14.85 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.726 8.738   13.969 1.00 16.17 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.433 9.804   15.039 1.00 14.86 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.368 13.419  16.734 1.00 13.05 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.705 14.738  16.807 1.00 12.79 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.698 15.429  15.421 1.00 14.13 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.690 16.049  15.037 1.00 15.32 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.418 15.586  17.854 1.00 13.76 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.673 16.900  18.175 1.00 15.77 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.595 17.743  19.058 1.00 15.55 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.995 18.988  19.576 1.00 17.09 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.956 20.128  18.898 1.00 17.25 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.403 20.184  17.644 1.00 18.18 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.450 21.229  19.462 1.00 17.15 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.813 15.251  14.652 1.00 13.86 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.887 15.933  13.343 1.00 14.73 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.940 15.363  12.295 1.00 15.82 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.744 15.994  11.249 1.00 18.42 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.348 16.018  12.809 1.00 15.02 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.931 14.735  12.305 1.00 16.21 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.506 13.797  13.166 1.00 16.41 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 19.073 14.310  11.028 1.00 16.64 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.944 12.819  12.373 1.00 16.19 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.678 13.079  11.079 1.00 17.12 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.374 14.173  12.561 1.00 14.82 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.415 13.540  11.625 1.00 15.34 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.974 13.560  12.154 1.00 16.53 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 12.073 12.982  11.514 1.00 18.39 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.865 12.096  11.333 1.00 15.56 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.254 11.973  10.675 1.00 16.31 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.606 10.508  10.447 1.00 16.49 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.328 12.767  9.346  1.00 17.27 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.730 14.213  13.316 1.00 15.98 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.389 14.201  13.904 1.00 16.53 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.390 14.885  12.958 1.00 17.25 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.727 15.877  12.323 1.00 16.89 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.398 14.923  15.244 1.00 16.58 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.183  14.332  12.888 1.00 18.09 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.150  14.891  11.992 1.00 20.07 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.322  15.970  12.701 1.00 21.87 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.423  16.134  13.912 1.00 21.46 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.197  13.733  11.567 1.00 21.25 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.470  13.279  12.712 1.00 21.09 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.943  12.574  10.946 1.00 21.92 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.383  16.644  11.962 1.00 22.79 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.472  17.593  12.596 1.00 24.05 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.652  16.881  13.688 1.00 21.48 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.419  17.459  14.750 1.00 22.39 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.497  18.186  11.546 1.00 28.43 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 5.149  18.954  10.426 1.00 36.45 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.920  20.086  10.664 1.00 40.01 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 5.066  18.758  9.087  1.00 39.37 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.317  20.506  9.472  1.00 41.08 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.824  19.739  8.490  1.00 41.10 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.240  15.616  13.439 1.00 21.46 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.476  14.877  14.438 1.00 21.02 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.272  14.567  15.687 1.00 19.48 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.732  14.610  16.791 1.00 20.26 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.907  13.601  13.868 1.00 23.81 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.693  13.881  13.056 1.00 29.88 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.846  14.721  13.411 1.00 30.06 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.600  13.179  11.941 1.00 31.13 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.579  14.267  15.538 1.00 17.56 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.426  14.031  16.720 1.00 17.11 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.457  15.288  17.593 1.00 16.94 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.308  15.211  18.822 1.00 17.49 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.862  13.699  16.265 1.00 15.54 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 8.023  12.288  15.768 1.00 19.04 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.433  11.381  16.379 1.00 20.50 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.713  12.100  14.724 1.00 19.81 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.659  16.460  16.960 1.00 17.78 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.736  17.716  17.711 1.00 18.13 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.393  18.091  18.341 1.00 19.53 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.359  18.637  19.452 1.00 20.27 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.265  18.839  16.812 1.00 17.62 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.782  18.853  16.700 1.00 17.43 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.536  18.400  15.658 1.00 18.45 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.709  19.356  17.672 1.00 17.21 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.886 18.584  15.931 1.00 18.64 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 11.014 19.144  17.169 1.00 18.04 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.569  19.908  18.946 1.00 17.99 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 12.170 19.547  17.880 1.00 17.38 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.713 20.296  19.640 1.00 18.41 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.983 20.106  19.114 1.00 17.98 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.280  17.750  17.673 1.00 19.85 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.935  18.032  18.228 1.00 20.96 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.588  17.117  19.429 1.00 21.68 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.633  17.392  20.185 1.00 22.77 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.899  17.851  17.136 1.00 21.59 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.283  15.970  19.555 1.00 19.52 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 3.076  15.041  20.659 1.00 19.96 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.371  14.903  21.477 1.00 19.59 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.678  13.846  22.013 1.00 18.47 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.653  13.697  20.092 1.00 20.84 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.292  13.785  19.464 1.00 24.50 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.272  13.778  20.178 1.00 26.16 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.253  13.908  18.146 1.00 25.31 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 5.118  16.001  21.601 1.00 19.08 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.424  15.996  22.270 1.00 18.04 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.365  15.610  23.745 1.00 19.43 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.562  16.155  24.508 1.00 20.59 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 7.006  17.402  22.146 1.00 18.43 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.396  17.595  22.791 1.00 19.51 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.467  16.713  22.102 1.00 19.57 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.836  19.070  22.736 1.00 20.02 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.263  14.706  24.164 1.00 18.58 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.413  14.331  25.571 1.00 19.24 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.742  14.927  26.088 1.00 19.33 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.804  15.546  27.167 1.00 20.97 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.402  12.777  25.719 1.00 20.71 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.799  12.351  27.137 1.00 21.28 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 6.021  12.227  25.376 1.00 21.35 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.825  14.760  25.295 1.00 17.81 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 11.149 15.203  25.707 1.00 18.30 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 12.042 15.286  24.477 1.00 16.71 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.917 14.456  23.565 1.00 17.28 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.741 14.173  26.721 1.00 18.78 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.201 14.347  27.053 1.00 20.08 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.752 15.210  27.960 1.00 22.01 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.288 13.607  26.489 1.00 19.76 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 15.127 15.072  27.963 1.00 22.70 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.479 14.101  27.064 1.00 21.07 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.374 12.624  25.503 1.00 19.57 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.729 13.558  26.768 1.00 21.07 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.617 12.115  25.180 1.00 20.02 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.777 12.585  25.811 1.00 20.28 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.933 16.267  24.457 1.00 17.57 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.935 16.338  23.389 1.00 17.63 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.243 16.911  23.932 1.00 17.40 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.232 17.686  24.902 1.00 18.17 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.422 17.098  22.150 1.00 18.38 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.857 18.499  22.419 1.00 17.88 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.876 19.601  22.687 1.00 20.36 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.551 20.500  23.501 1.00 25.01 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 15.008 19.555  22.156 1.00 19.86 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.366 16.546  23.307 1.00 16.70 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.660 17.061  23.732 1.00 16.94 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.532 17.205  22.484 1.00 16.61 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.965 16.198  21.902 1.00 15.78 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.294 16.139  24.797 1.00 18.28 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.577 16.679  25.412 1.00 24.86 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.244 17.521  24.759 1.00 26.57 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.915 16.264  26.538 1.00 25.21 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.757 18.466  22.038 1.00 16.99 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.567 18.738  20.861 0.50 17.66 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.570 18.710  20.848 0.50 17.12 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.999 18.218  21.048 1.00 17.80 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.624 17.773  20.082 1.00 18.10 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.545 20.240  20.573 0.50 19.98 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.544 20.193  20.474 0.50 18.18 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.399 20.593  19.501 0.50 23.43 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.236 20.964  21.441 0.50 19.70 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.530 18.270  22.291 1.00 17.39 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.905 17.778  22.514 1.00 17.98 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 23.017 16.269  22.379 1.00 17.48 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 24.132 15.801  22.237 1.00 18.57 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.464 18.216  23.868 1.00 21.97 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.922 17.446  24.927 1.00 27.83 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.905 15.526  22.395 1.00 16.18 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.953 14.065  22.216 1.00 14.99 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.395 13.620  20.848 1.00 14.83 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.430 12.415  20.557 1.00 14.36 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 21.083 13.389  23.312 1.00 14.97 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.690 13.586  24.706 1.00 15.39 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.879 12.926  25.814 1.00 16.65 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.821 11.451  25.687 1.00 15.61 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.594 10.628  26.704 1.00 17.39 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.378 11.112  27.929 1.00 19.00 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.588 9.311   26.515 1.00 17.80 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.828 14.555  20.056 1.00 14.17 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 20.129 14.214  18.818 1.00 13.46 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.963 13.249  19.091 1.00 13.21 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.670 12.408  18.234 1.00 13.91 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 21.059 13.645  17.716 1.00 14.87 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.364 13.406  16.379 1.00 15.76 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.538 14.266  15.970 1.00 14.86 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.661 12.367  15.735 1.00 15.69 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.246 13.409  20.224 1.00 13.69 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.088 12.563  20.520 1.00 13.13 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.813 13.353  20.698 1.00 12.94 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.829 14.453  21.273 1.00 14.35 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.310 11.745  21.811 1.00 13.25 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.328 10.600  21.714 1.00 15.35 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.350 9.870   23.065 1.00 15.75 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.938 9.573   20.633 1.00 15.54 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.682 12.718  20.327 1.00 12.61 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.356 13.241  20.574 1.00 13.32 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.454 12.068  20.867 1.00 14.55 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.559 11.020  20.207 1.00 14.75 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.839 14.083  19.385 1.00 13.49 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.445 14.752  19.575 1.00 14.48 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.386 16.083  18.833 1.00 16.43 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.299 13.843  19.092 1.00 15.40 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.613 12.210  21.874 1.00 14.58 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.604 11.208  22.240 1.00 15.07 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.226  11.844  22.157 1.00 16.15 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 9.016  12.953  22.690 1.00 17.22 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.838 10.687  23.671 1.00 15.50 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.752  9.653   24.057 1.00 16.89 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.223 10.057  23.772 1.00 15.43 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.320  11.175  21.466 1.00 15.95 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.951  11.641  21.331 1.00 16.36 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.987  10.565  21.875 1.00 18.76 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.366  9.400   22.054 1.00 18.18 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.636  11.968  19.871 1.00 17.01 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.756  10.835  19.025 1.00 18.67 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.745  10.969  22.156 1.00 19.68 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.746  10.014  22.659 1.00 20.78 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 2.951  9.328   21.545 1.00 22.00 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.696  9.912   20.500 1.00 22.44 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.831  10.688  23.672 1.00 23.03 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 2.172  11.753  23.026 1.00 26.74 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.553  8.072   21.767 1.00 23.15 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.781  7.306   20.789 1.00 26.64 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.487  6.783   21.456 1.00 30.60 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.407  6.693   22.686 1.00 30.78 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.605  6.095   20.261 1.00 28.30 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.682  5.113   21.301 1.00 29.19 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.998  6.461   19.807 1.00 28.10 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.489 6.394   20.646 1.00 33.53 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.721 5.805   21.167 1.00 36.63 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.573 4.272   21.239 1.00 38.53 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.065 3.644   22.184 1.00 39.96 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -2.912 6.250   20.315 1.00 39.48 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.631 5.934   18.945 1.00 42.00 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.164 7.739   20.425 1.00 39.89 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -0.880 3.672   20.262 1.00 38.00 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.705 2.225   20.229 1.00 37.42 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.464  1.760   21.120 1.00 36.78 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.421  2.505   21.338 1.00 36.32 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.494 1.765   18.794 1.00 37.57 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.393  0.520   21.607 1.00 35.75 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.454  -0.029  22.451 1.00 35.75 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.648  -0.441  21.592 1.00 34.01 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.458  -1.084  20.560 1.00 34.87 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.923  -1.234  23.231 1.00 39.77 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.926  -1.793  24.235 1.00 46.50 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 1.967  -1.003  25.531 1.00 54.41 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.286  0.022   25.717 1.00 56.83 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 2.763  -1.478  26.475 1.00 56.34 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.850  -0.040  22.004 1.00 31.41 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 5.095  -0.312  21.299 1.00 30.56 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.529  -1.753  21.256 1.00 30.14 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.140  -2.527  22.116 1.00 32.92 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.359  -2.098  20.231 1.00 26.75 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.890  -3.430  19.923 1.00 24.12 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.243  -3.747  20.569 1.00 22.76 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.605  -4.917  20.661 1.00 21.75 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 6.950  -3.637  18.402 1.00 24.36 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 8.009  -2.459  17.499 1.00 26.80 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.985  -2.741  21.015 1.00 21.68 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.372 -2.890  21.525 1.00 20.73 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.555 -2.919  23.089 1.00 21.09 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 9.682  -2.382  23.811 1.00 22.31 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.209 -1.731  20.912 1.00 21.12 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.374 -1.757  19.382 1.00 24.43 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 11.905 -2.769  18.864 1.00 24.92 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 11.070 -0.698  18.702 1.00 21.10 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 11.713 -3.514  23.587 1.00 20.58 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.275 -3.668  24.963 1.00 21.97 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.615 -2.886  25.014 1.00 18.96 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.401 -3.030  24.097 1.00 19.07 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.631 -5.170  25.259 1.00 27.88 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 11.395 -5.838  25.463 1.00 33.65 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 13.583 -5.363  26.511 1.00 30.50 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 13.868 -2.084  26.075 1.00 17.37 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.109 -1.327  26.174 1.00 16.27 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.096 -2.075  27.053 1.00 16.48 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.741 -2.538  28.154 1.00 17.66 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 14.833 0.050   26.827 1.00 16.10 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.725 0.841   26.106 1.00 17.97 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.143 0.893   26.863 1.00 16.30 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 14.036 1.039   24.583 1.00 18.60 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.349 -2.171  26.600 1.00 14.77 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.407 -2.819  27.384 1.00 14.82 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.776 -1.918  28.579 1.00 14.80 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.789 -0.694  28.457 1.00 15.20 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.662 -2.995  26.514 1.00 15.31 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 19.060 -2.538  29.750 1.00 16.19 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.498 -1.794  30.953 1.00 16.37 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.777 -2.518  31.382 1.00 18.14 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.747 -3.453  32.180 1.00 19.22 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.431 -1.826  32.063 1.00 16.81 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.100 -1.250  31.603 1.00 17.10 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.123 0.223   31.226 1.00 17.41 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.771 0.674   30.880 1.00 17.27 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.499 1.810   30.252 1.00 19.52 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.476 2.627   29.890 1.00 18.58 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.243 2.137   29.976 1.00 20.97 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 21.894 -2.126  30.775 1.00 17.58 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 23.139 -2.889  30.884 1.00 18.00 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.349 -2.031  30.511 1.00 18.71 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.208 -0.875  30.108 1.00 18.49 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 23.039 -4.079  29.932 1.00 16.97 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 23.064 -3.576  28.174 1.00 17.16 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.561 -2.668  30.592 1.00 20.05 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.794 -2.005  30.178 1.00 20.40 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.452 -2.724  29.006 1.00 20.79 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.670 -2.616  28.829 1.00 21.36 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 27.784 -1.894  31.358 1.00 24.10 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.279 -3.216  31.910 1.00 30.23 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 27.802 -4.268  31.456 1.00 29.74 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.157 -3.194  32.806 1.00 37.25 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.655 -3.407  28.144 1.00 18.88 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.234 -4.048  26.953 1.00 17.85 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 27.968 -3.061  26.075 1.00 17.03 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.540 -1.899  25.902 1.00 17.04 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.146 -4.743  26.142 1.00 17.25 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.484 -6.262  26.882 1.00 18.92 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 29.061 -3.512  25.494 1.00 15.72 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 29.830 -2.715  24.544 1.00 15.50 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 29.998 -3.471  23.213 1.00 15.31 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 30.857 -3.135  22.413 1.00 16.35 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.205 -2.301  25.094 1.00 17.91 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.173 -1.133  26.072 1.00 23.22 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.598 -0.721  26.444 1.00 27.27 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.007 -0.882  27.603 1.00 28.90 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.381 -0.170  25.481 1.00 25.51 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.189 -4.560  22.999 1.00 14.67 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.098 -5.248  21.716 1.00 14.85 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.599 -5.446  21.431 1.00 14.28 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.759 -5.472  22.347 1.00 15.71 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 29.835 -6.582  21.702 1.00 16.63 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.192 -7.468  22.629 1.00 19.59 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.309 -6.444  22.057 1.00 18.20 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.281 -5.522  20.145 1.00 13.84 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 25.887 -5.660  19.734 1.00 14.16 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 25.806 -5.742  18.218 1.00 13.63 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 26.833 -5.955  17.545 1.00 15.22 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.581 -5.621  17.693 1.00 12.58 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.344 -5.724  16.260 1.00 12.82 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.452 -4.542  15.881 1.00 13.33 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.440 -4.249  16.560 1.00 14.15 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.620 -7.054  15.943 1.00 14.07 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.241 -7.116  14.449 1.00 16.08 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.523 -8.252  16.275 1.00 15.32 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 23.798 -3.867  14.766 1.00 12.98 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 22.962 -2.751  14.304 1.00 12.75 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.455 -2.975  12.892 1.00 12.94 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.077 -3.708  12.113 1.00 12.56 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.678 -1.355  14.406 1.00 12.76 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.694 -1.046  13.319 1.00 12.47 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 25.949 -1.654  13.313 1.00 13.14 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.400 -0.160  12.288 1.00 12.72 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 26.891 -1.364  12.322 1.00 13.64 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.341 0.145   11.301 1.00 14.41 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.577 -0.472  11.313 1.00 14.98 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.532 -0.211  10.353 1.00 18.07 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.335 -2.325  12.561 1.00 13.45 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.795 -2.406  11.217 1.00 13.19 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.331 -1.237  10.388 1.00 13.68 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.195 -0.058  10.775 1.00 14.00 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.241 -2.388  11.238 1.00 13.70 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.697 -2.502  9.844  1.00 14.45 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 18.857 -3.669  9.117  1.00 14.74 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.040 -1.433  9.240  1.00 15.43 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.382 -3.777  7.813  1.00 16.36 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.575 -1.526  7.935  1.00 16.99 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.777 -2.689  7.223  1.00 18.24 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.307 -2.822  5.936  1.00 22.77 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.908 -1.562  9.218  1.00 13.23 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.466 -0.576  8.273  1.00 12.83 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.572 -0.504  7.005  1.00 14.05 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.649 -1.373  6.126  1.00 14.93 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.905 -0.958  7.938  1.00 13.97 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.679 0.099   6.677  1.00 16.53 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.695 0.527   6.937  1.00 14.78 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.759 0.604   5.811  1.00 15.77 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.433 0.747   4.450  1.00 15.12 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.921 0.196   3.455  1.00 15.01 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.744 1.725   6.007  1.00 21.23 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.400 2.965   6.159  1.00 28.60 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.608 1.413   4.396  1.00 14.16 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.352 1.600   3.127  1.00 14.43 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.992 0.314   2.586  1.00 14.51 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.491 0.316   1.455  1.00 16.13 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.393 2.707   3.239  1.00 16.13 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.392 2.326   4.180  1.00 16.84 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.924 -0.790  3.363  1.00 13.93 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.385 -2.093  2.922  1.00 14.47 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.257 -3.145  3.049  1.00 15.88 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.517 -4.316  2.781  1.00 17.79 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.609 -2.520  3.763  1.00 15.37 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.854 -1.655  3.469  1.00 16.47 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.423 -1.976  2.094  1.00 18.22 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.612 -1.166  1.745  1.00 19.28 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.563 0.022   1.148  1.00 20.74 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.400 0.564   0.824  1.00 19.93 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.683 0.675   0.864  1.00 20.84 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.048 -2.752  3.557  1.00 16.44 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 19.969 -3.698  3.859  1.00 18.14 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.478 -4.898  4.672  1.00 18.56 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.184 -6.071  4.342  1.00 20.71 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.299 -4.185  2.567  1.00 21.80 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.225 -3.291  2.136  1.00 28.86 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.292 -4.060  1.201  1.00 30.99 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.674 -3.111  0.310  1.00 31.84 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 16.986 -2.972  -0.973 1.00 31.36 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.851 -3.809  -1.555 1.00 31.81 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.432 -2.009  -1.689 1.00 30.53 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.314 -4.623  5.681  1.00 16.84 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 21.964 -5.714  6.411  1.00 17.56 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.252 -5.317  7.839  1.00 15.94 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.417 -4.129  8.122  1.00 16.43 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.342 -6.029  5.763  1.00 21.35 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.320 -7.200  4.795  1.00 31.92 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 24.701 -7.422  4.167  1.00 39.28 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 24.790 -8.738  3.395  1.00 45.83 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.487 -8.586  2.082  1.00 50.19 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.412 -6.313  8.708  1.00 14.99 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 22.819 -6.089  10.089 1.00 14.62 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.313 -6.415  10.205 1.00 15.57 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 24.834 -7.359  9.565  1.00 18.24 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.052 -7.002  11.047 1.00 14.02 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.570 -6.804  11.037 1.00 15.39 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 19.909 -6.116  12.039 1.00 18.78 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.658 -7.314  10.190 1.00 15.43 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.622 -6.199  11.737 1.00 17.51 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.428 -6.901  10.633 1.00 20.02 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 25.013 -5.639  11.036 1.00 13.57 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.443 -5.874  11.256 1.00 13.44 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.750 -5.925  12.761 1.00 14.35 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.202 -5.150  13.552 1.00 15.14 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.269 -4.675  10.710 1.00 13.61 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.286 -4.576  9.198  1.00 14.92 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 28.075 -5.427  8.431  1.00 17.95 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.608 -3.557  8.542  1.00 16.54 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 28.152 -5.293  7.042  1.00 19.04 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.670 -3.418  7.159  1.00 17.99 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.427 -4.299  6.405  1.00 20.41 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.479 -4.171  5.026  1.00 22.57 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.640 -6.820  13.178 1.00 14.23 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.092 -6.820  14.578 1.00 14.82 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.097 -5.671  14.820 1.00 16.43 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 29.885 -5.318  13.908 1.00 19.22 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.807 -8.185  14.709 1.00 15.52 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.348 -8.436  13.296 1.00 16.29 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.338 -7.840  12.352 1.00 14.68 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.105 -5.093  16.032 1.00 14.14 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 29.983 -3.951  16.331 1.00 15.37 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.492 -4.026  17.764 1.00 14.77 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 29.840 -4.552  18.662 1.00 15.09 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.245 -2.562  16.202 1.00 17.54 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.224 -2.081  14.753 1.00 19.04 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 27.825 -2.611  16.784 1.00 17.42 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.687 -3.478  17.978 1.00 14.94 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.234 -3.178  19.307 1.00 14.98 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.163 -1.641  19.394 1.00 14.63 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.595 -0.966  18.459 1.00 15.66 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.690 -3.615  19.439 1.00 18.78 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 33.724 -5.031  19.441 1.00 25.16 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.550 -1.089  20.461 1.00 13.05 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.368 0.374   20.545 1.00 13.90 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.856 0.922   21.875 1.00 14.95 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.905 0.209   22.903 1.00 15.54 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.876 0.762   20.291 1.00 14.01 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.844 -0.046  21.063 1.00 13.97 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.357 -1.248  20.566 1.00 14.05 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.358 0.402   22.276 1.00 14.25 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.384 -1.975  21.256 1.00 14.40 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.373 -0.335  22.973 1.00 14.75 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.922 -1.527  22.469 1.00 14.47 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.220 2.204   21.858 1.00 14.56 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.660 2.860   23.079 1.00 15.34 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.505 3.154   24.044 1.00 16.63 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.321 3.085   23.680 1.00 16.78 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.452 4.119   22.742 1.00 16.76 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.584 5.053   22.119 1.00 20.05 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 31.840 3.430   25.319 1.00 17.09 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 30.805 3.781   26.300 1.00 17.60 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.228 5.161   25.926 1.00 17.95 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 30.924 5.972   25.287 1.00 18.89 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.426 3.815   27.705 1.00 21.16 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 31.877 2.429   28.145 1.00 24.76 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.382 2.518   29.597 1.00 31.88 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.448 1.133   30.191 1.00 38.69 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 33.343 1.069   31.368 1.00 42.20 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 29.002 5.481   26.372 1.00 17.37 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.411 6.812   26.043 1.00 17.38 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.327 7.945   26.493 1.00 17.32 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.768 7.982   27.655 1.00 18.52 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 27.081 6.836   26.804 1.00 19.06 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 26.767 5.360   27.085 1.00 20.74 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.080 4.635   27.166 1.00 17.67 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.613 8.871   25.561 1.00 16.34 ? 80  SER   A N   1 
ATOM   582  C  CA  A SER   A 1 74  ? 30.549 9.946   25.879 0.50 17.79 ? 80  SER   A CA  1 
ATOM   583  C  CA  B SER   A 1 74  ? 30.601 9.917   25.815 0.50 17.11 ? 80  SER   A CA  1 
ATOM   584  C  C   . SER   A 1 74  ? 30.239 11.234  25.118 1.00 17.42 ? 80  SER   A C   1 
ATOM   585  O  O   . SER   A 1 74  ? 29.330 11.270  24.281 1.00 16.66 ? 80  SER   A O   1 
ATOM   586  C  CB  A SER   A 1 74  ? 31.982 9.486   25.587 0.50 21.23 ? 80  SER   A CB  1 
ATOM   587  C  CB  B SER   A 1 74  ? 31.972 9.460   25.284 0.50 18.40 ? 80  SER   A CB  1 
ATOM   588  O  OG  A SER   A 1 74  ? 32.162 9.215   24.208 0.50 24.67 ? 80  SER   A OG  1 
ATOM   589  O  OG  B SER   A 1 74  ? 32.272 8.094   25.536 0.50 19.61 ? 80  SER   A OG  1 
ATOM   590  N  N   . LEU   A 1 75  ? 31.002 12.321  25.432 1.00 18.30 ? 81  LEU   A N   1 
ATOM   591  C  CA  . LEU   A 1 75  ? 30.837 13.614  24.796 1.00 18.90 ? 81  LEU   A CA  1 
ATOM   592  C  C   . LEU   A 1 75  ? 31.848 13.618  23.624 1.00 20.21 ? 81  LEU   A C   1 
ATOM   593  O  O   . LEU   A 1 75  ? 33.074 13.517  23.856 1.00 21.89 ? 81  LEU   A O   1 
ATOM   594  C  CB  . LEU   A 1 75  ? 31.243 14.660  25.841 1.00 19.78 ? 81  LEU   A CB  1 
ATOM   595  C  CG  . LEU   A 1 75  ? 30.848 16.073  25.609 1.00 23.63 ? 81  LEU   A CG  1 
ATOM   596  C  CD1 . LEU   A 1 75  ? 29.339 16.233  25.409 1.00 24.60 ? 81  LEU   A CD1 1 
ATOM   597  C  CD2 . LEU   A 1 75  ? 31.301 16.957  26.792 1.00 25.96 ? 81  LEU   A CD2 1 
ATOM   598  N  N   . ILE   A 1 76  ? 31.362 13.705  22.387 1.00 18.98 ? 82  ILE   A N   1 
ATOM   599  C  CA  . ILE   A 1 76  ? 32.181 13.592  21.193 1.00 20.56 ? 82  ILE   A CA  1 
ATOM   600  C  C   . ILE   A 1 76  ? 31.933 14.770  20.276 1.00 19.32 ? 82  ILE   A C   1 
ATOM   601  O  O   . ILE   A 1 76  ? 30.776 15.131  20.070 1.00 19.41 ? 82  ILE   A O   1 
ATOM   602  C  CB  . ILE   A 1 76  ? 31.827 12.247  20.489 1.00 22.75 ? 82  ILE   A CB  1 
ATOM   603  C  CG1 . ILE   A 1 76  ? 32.267 11.060  21.364 1.00 25.50 ? 82  ILE   A CG1 1 
ATOM   604  C  CG2 . ILE   A 1 76  ? 32.430 12.167  19.075 1.00 23.84 ? 82  ILE   A CG2 1 
ATOM   605  C  CD1 . ILE   A 1 76  ? 31.816 9.778   20.921 1.00 28.31 ? 82  ILE   A CD1 1 
ATOM   606  N  N   . PHE   A 1 77  ? 33.005 15.370  19.709 1.00 19.22 ? 83  PHE   A N   1 
ATOM   607  C  CA  . PHE   A 1 77  ? 32.822 16.465  18.773 1.00 20.21 ? 83  PHE   A CA  1 
ATOM   608  C  C   . PHE   A 1 77  ? 32.226 15.948  17.462 1.00 20.46 ? 83  PHE   A C   1 
ATOM   609  O  O   . PHE   A 1 77  ? 32.671 14.923  16.926 1.00 21.21 ? 83  PHE   A O   1 
ATOM   610  C  CB  . PHE   A 1 77  ? 34.190 17.135  18.498 1.00 21.87 ? 83  PHE   A CB  1 
ATOM   611  C  CG  . PHE   A 1 77  ? 34.101 18.268  17.501 1.00 24.72 ? 83  PHE   A CG  1 
ATOM   612  C  CD1 . PHE   A 1 77  ? 34.432 18.067  16.169 1.00 25.49 ? 83  PHE   A CD1 1 
ATOM   613  C  CD2 . PHE   A 1 77  ? 33.604 19.501  17.876 1.00 26.89 ? 83  PHE   A CD2 1 
ATOM   614  C  CE1 . PHE   A 1 77  ? 34.330 19.101  15.244 1.00 26.90 ? 83  PHE   A CE1 1 
ATOM   615  C  CE2 . PHE   A 1 77  ? 33.485 20.531  16.943 1.00 27.92 ? 83  PHE   A CE2 1 
ATOM   616  C  CZ  . PHE   A 1 77  ? 33.884 20.330  15.644 1.00 26.95 ? 83  PHE   A CZ  1 
ATOM   617  N  N   . VAL   A 1 78  ? 31.184 16.638  16.969 1.00 20.07 ? 84  VAL   A N   1 
ATOM   618  C  CA  . VAL   A 1 78  ? 30.522 16.310  15.715 1.00 19.83 ? 84  VAL   A CA  1 
ATOM   619  C  C   . VAL   A 1 78  ? 30.575 17.565  14.844 1.00 20.87 ? 84  VAL   A C   1 
ATOM   620  O  O   . VAL   A 1 78  ? 30.122 18.646  15.257 1.00 20.93 ? 84  VAL   A O   1 
ATOM   621  C  CB  . VAL   A 1 78  ? 29.052 15.866  15.940 1.00 19.31 ? 84  VAL   A CB  1 
ATOM   622  C  CG1 . VAL   A 1 78  ? 28.378 15.561  14.599 1.00 19.81 ? 84  VAL   A CG1 1 
ATOM   623  C  CG2 . VAL   A 1 78  ? 28.984 14.637  16.846 1.00 19.14 ? 84  VAL   A CG2 1 
ATOM   624  N  N   . GLU   A 1 79  ? 31.101 17.423  13.630 1.00 21.73 ? 85  GLU   A N   1 
ATOM   625  C  CA  . GLU   A 1 79  ? 31.240 18.573  12.727 1.00 22.99 ? 85  GLU   A CA  1 
ATOM   626  C  C   . GLU   A 1 79  ? 29.894 19.141  12.298 1.00 23.02 ? 85  GLU   A C   1 
ATOM   627  O  O   . GLU   A 1 79  ? 28.880 18.442  12.373 1.00 22.33 ? 85  GLU   A O   1 
ATOM   628  C  CB  . GLU   A 1 79  ? 32.085 18.190  11.505 1.00 27.93 ? 85  GLU   A CB  1 
ATOM   629  C  CG  . GLU   A 1 79  ? 33.353 19.023  11.408 1.00 40.58 ? 85  GLU   A CG  1 
ATOM   630  C  CD  . GLU   A 1 79  ? 33.237 20.403  10.785 1.00 52.56 ? 85  GLU   A CD  1 
ATOM   631  O  OE1 . GLU   A 1 79  ? 32.615 21.300  11.407 1.00 53.42 ? 85  GLU   A OE1 1 
ATOM   632  O  OE2 . GLU   A 1 79  ? 33.796 20.596  9.679  1.00 58.22 ? 85  GLU   A OE2 1 
ATOM   633  N  N   . ALA   A 1 80  ? 29.874 20.424  11.842 1.00 24.00 ? 86  ALA   A N   1 
ATOM   634  C  CA  . ALA   A 1 80  ? 28.638 21.040  11.388 1.00 23.92 ? 86  ALA   A CA  1 
ATOM   635  C  C   . ALA   A 1 80  ? 28.025 20.261  10.230 1.00 23.96 ? 86  ALA   A C   1 
ATOM   636  O  O   . ALA   A 1 80  ? 28.742 19.688  9.394  1.00 24.46 ? 86  ALA   A O   1 
ATOM   637  C  CB  . ALA   A 1 80  ? 28.907 22.470  10.930 1.00 24.22 ? 86  ALA   A CB  1 
ATOM   638  N  N   . SER   A 1 81  ? 26.694 20.211  10.202 1.00 23.20 ? 87  SER   A N   1 
ATOM   639  C  CA  . SER   A 1 81  ? 25.959 19.564  9.113  1.00 22.92 ? 87  SER   A CA  1 
ATOM   640  C  C   . SER   A 1 81  ? 24.816 20.518  8.725  1.00 24.18 ? 87  SER   A C   1 
ATOM   641  O  O   . SER   A 1 81  ? 24.729 21.615  9.278  1.00 24.69 ? 87  SER   A O   1 
ATOM   642  C  CB  . SER   A 1 81  ? 25.411 18.211  9.594  1.00 23.17 ? 87  SER   A CB  1 
ATOM   643  O  OG  . SER   A 1 81  ? 24.384 18.391  10.558 1.00 22.52 ? 87  SER   A OG  1 
ATOM   644  N  N   . GLU   A 1 82  ? 23.930 20.114  7.806  1.00 25.05 ? 88  GLU   A N   1 
ATOM   645  C  CA  . GLU   A 1 82  ? 22.753 20.933  7.509  1.00 26.47 ? 88  GLU   A CA  1 
ATOM   646  C  C   . GLU   A 1 82  ? 21.796 20.985  8.716  1.00 26.33 ? 88  GLU   A C   1 
ATOM   647  O  O   . GLU   A 1 82  ? 20.910 21.839  8.746  1.00 28.03 ? 88  GLU   A O   1 
ATOM   648  C  CB  . GLU   A 1 82  ? 22.019 20.376  6.280  1.00 30.89 ? 88  GLU   A CB  1 
ATOM   649  C  CG  . GLU   A 1 82  ? 22.796 20.528  4.988  1.00 40.22 ? 88  GLU   A CG  1 
ATOM   650  C  CD  . GLU   A 1 82  ? 22.229 19.681  3.869  1.00 52.56 ? 88  GLU   A CD  1 
ATOM   651  O  OE1 . GLU   A 1 82  ? 21.642 20.260  2.927  1.00 54.56 ? 88  GLU   A OE1 1 
ATOM   652  O  OE2 . GLU   A 1 82  ? 22.351 18.435  3.947  1.00 56.75 ? 88  GLU   A OE2 1 
ATOM   653  N  N   . TYR   A 1 83  ? 21.934 20.050  9.704  1.00 24.09 ? 89  TYR   A N   1 
ATOM   654  C  CA  . TYR   A 1 83  ? 21.005 19.975  10.829 1.00 23.05 ? 89  TYR   A CA  1 
ATOM   655  C  C   . TYR   A 1 83  ? 21.486 20.591  12.122 1.00 22.36 ? 89  TYR   A C   1 
ATOM   656  O  O   . TYR   A 1 83  ? 20.655 20.961  12.941 1.00 23.09 ? 89  TYR   A O   1 
ATOM   657  C  CB  . TYR   A 1 83  ? 20.615 18.530  11.119 1.00 22.60 ? 89  TYR   A CB  1 
ATOM   658  C  CG  . TYR   A 1 83  ? 20.049 17.817  9.914  1.00 23.09 ? 89  TYR   A CG  1 
ATOM   659  C  CD1 . TYR   A 1 83  ? 20.875 17.119  9.047  1.00 24.31 ? 89  TYR   A CD1 1 
ATOM   660  C  CD2 . TYR   A 1 83  ? 18.691 17.857  9.629  1.00 22.94 ? 89  TYR   A CD2 1 
ATOM   661  C  CE1 . TYR   A 1 83  ? 20.355 16.422  7.964  1.00 25.48 ? 89  TYR   A CE1 1 
ATOM   662  C  CE2 . TYR   A 1 83  ? 18.162 17.187  8.528  1.00 23.87 ? 89  TYR   A CE2 1 
ATOM   663  C  CZ  . TYR   A 1 83  ? 19.003 16.499  7.682  1.00 26.19 ? 89  TYR   A CZ  1 
ATOM   664  O  OH  . TYR   A 1 83  ? 18.480 15.835  6.594  1.00 29.84 ? 89  TYR   A OH  1 
ATOM   665  N  N   . TYR   A 1 84  ? 22.796 20.695  12.321 1.00 21.30 ? 90  TYR   A N   1 
ATOM   666  C  CA  . TYR   A 1 84  ? 23.324 21.245  13.576 1.00 21.42 ? 90  TYR   A CA  1 
ATOM   667  C  C   . TYR   A 1 84  ? 24.578 22.037  13.331 1.00 23.15 ? 90  TYR   A C   1 
ATOM   668  O  O   . TYR   A 1 84  ? 25.369 21.704  12.442 1.00 22.62 ? 90  TYR   A O   1 
ATOM   669  C  CB  . TYR   A 1 84  ? 23.733 20.093  14.545 1.00 20.07 ? 90  TYR   A CB  1 
ATOM   670  C  CG  . TYR   A 1 84  ? 22.610 19.232  15.074 1.00 17.75 ? 90  TYR   A CG  1 
ATOM   671  C  CD1 . TYR   A 1 84  ? 21.781 19.685  16.077 1.00 18.37 ? 90  TYR   A CD1 1 
ATOM   672  C  CD2 . TYR   A 1 84  ? 22.442 17.936  14.629 1.00 17.27 ? 90  TYR   A CD2 1 
ATOM   673  C  CE1 . TYR   A 1 84  ? 20.767 18.894  16.585 1.00 16.80 ? 90  TYR   A CE1 1 
ATOM   674  C  CE2 . TYR   A 1 84  ? 21.436 17.123  15.140 1.00 16.29 ? 90  TYR   A CE2 1 
ATOM   675  C  CZ  . TYR   A 1 84  ? 20.587 17.607  16.110 1.00 16.70 ? 90  TYR   A CZ  1 
ATOM   676  O  OH  . TYR   A 1 84  ? 19.583 16.822  16.629 1.00 16.56 ? 90  TYR   A OH  1 
ATOM   677  N  N   . PRO   A 1 85  ? 24.851 23.030  14.191 1.00 24.74 ? 91  PRO   A N   1 
ATOM   678  C  CA  . PRO   A 1 85  ? 26.174 23.666  14.130 1.00 24.69 ? 91  PRO   A CA  1 
ATOM   679  C  C   . PRO   A 1 85  ? 27.209 22.663  14.654 1.00 24.12 ? 91  PRO   A C   1 
ATOM   680  O  O   . PRO   A 1 85  ? 26.879 21.652  15.312 1.00 24.00 ? 91  PRO   A O   1 
ATOM   681  C  CB  . PRO   A 1 85  ? 26.028 24.842  15.098 1.00 25.91 ? 91  PRO   A CB  1 
ATOM   682  C  CG  . PRO   A 1 85  ? 25.051 24.330  16.131 1.00 27.16 ? 91  PRO   A CG  1 
ATOM   683  C  CD  . PRO   A 1 85  ? 24.062 23.496  15.353 1.00 25.12 ? 91  PRO   A CD  1 
ATOM   684  N  N   . ALA   A 1 86  ? 28.501 22.969  14.458 1.00 23.41 ? 92  ALA   A N   1 
ATOM   685  C  CA  . ALA   A 1 86  ? 29.583 22.163  15.015 1.00 24.39 ? 92  ALA   A CA  1 
ATOM   686  C  C   . ALA   A 1 86  ? 29.415 22.187  16.558 1.00 23.96 ? 92  ALA   A C   1 
ATOM   687  O  O   . ALA   A 1 86  ? 29.099 23.258  17.110 1.00 25.15 ? 92  ALA   A O   1 
ATOM   688  C  CB  . ALA   A 1 86  ? 30.920 22.805  14.637 1.00 25.61 ? 92  ALA   A CB  1 
ATOM   689  N  N   . ARG   A 1 87  ? 29.455 21.002  17.211 1.00 21.84 ? 93  ARG   A N   1 
ATOM   690  C  CA  . ARG   A 1 87  ? 29.176 20.968  18.651 1.00 20.81 ? 93  ARG   A CA  1 
ATOM   691  C  C   . ARG   A 1 87  ? 29.657 19.651  19.270 1.00 20.97 ? 93  ARG   A C   1 
ATOM   692  O  O   . ARG   A 1 87  ? 30.077 18.758  18.544 1.00 22.05 ? 93  ARG   A O   1 
ATOM   693  C  CB  . ARG   A 1 87  ? 27.640 21.121  18.846 1.00 20.66 ? 93  ARG   A CB  1 
ATOM   694  C  CG  . ARG   A 1 87  ? 26.881 19.805  18.474 1.00 21.37 ? 93  ARG   A CG  1 
ATOM   695  C  CD  . ARG   A 1 87  ? 25.455 20.014  18.025 1.00 21.20 ? 93  ARG   A CD  1 
ATOM   696  N  NE  . ARG   A 1 87  ? 24.559 18.900  18.402 1.00 21.35 ? 93  ARG   A NE  1 
ATOM   697  C  CZ  . ARG   A 1 87  ? 24.521 17.709  17.797 1.00 19.55 ? 93  ARG   A CZ  1 
ATOM   698  N  NH1 . ARG   A 1 87  ? 23.654 16.782  18.194 1.00 17.95 ? 93  ARG   A NH1 1 
ATOM   699  N  NH2 . ARG   A 1 87  ? 25.398 17.412  16.833 1.00 19.78 ? 93  ARG   A NH2 1 
ATOM   700  N  N   . TYR   A 1 88  ? 29.577 19.531  20.593 1.00 20.39 ? 94  TYR   A N   1 
ATOM   701  C  CA  . TYR   A 1 88  ? 29.818 18.244  21.244 1.00 20.97 ? 94  TYR   A CA  1 
ATOM   702  C  C   . TYR   A 1 88  ? 28.461 17.569  21.426 1.00 19.41 ? 94  TYR   A C   1 
ATOM   703  O  O   . TYR   A 1 88  ? 27.519 18.185  21.955 1.00 20.09 ? 94  TYR   A O   1 
ATOM   704  C  CB  . TYR   A 1 88  ? 30.475 18.416  22.616 1.00 21.92 ? 94  TYR   A CB  1 
ATOM   705  C  CG  . TYR   A 1 88  ? 31.904 18.891  22.480 1.00 24.27 ? 94  TYR   A CG  1 
ATOM   706  C  CD1 . TYR   A 1 88  ? 32.952 17.988  22.387 1.00 25.98 ? 94  TYR   A CD1 1 
ATOM   707  C  CD2 . TYR   A 1 88  ? 32.196 20.242  22.367 1.00 26.75 ? 94  TYR   A CD2 1 
ATOM   708  C  CE1 . TYR   A 1 88  ? 34.272 18.428  22.243 1.00 27.91 ? 94  TYR   A CE1 1 
ATOM   709  C  CE2 . TYR   A 1 88  ? 33.497 20.688  22.167 1.00 28.58 ? 94  TYR   A CE2 1 
ATOM   710  C  CZ  . TYR   A 1 88  ? 34.532 19.777  22.108 1.00 30.05 ? 94  TYR   A CZ  1 
ATOM   711  O  OH  . TYR   A 1 88  ? 35.819 20.252  21.946 1.00 33.48 ? 94  TYR   A OH  1 
ATOM   712  N  N   . GLN   A 1 89  ? 28.350 16.331  20.956 1.00 17.35 ? 95  GLN   A N   1 
ATOM   713  C  CA  . GLN   A 1 89  ? 27.137 15.559  21.148 1.00 16.20 ? 95  GLN   A CA  1 
ATOM   714  C  C   . GLN   A 1 89  ? 27.397 14.639  22.349 1.00 16.18 ? 95  GLN   A C   1 
ATOM   715  O  O   . GLN   A 1 89  ? 28.452 13.977  22.424 1.00 17.49 ? 95  GLN   A O   1 
ATOM   716  C  CB  . GLN   A 1 89  ? 26.808 14.743  19.883 1.00 15.78 ? 95  GLN   A CB  1 
ATOM   717  C  CG  . GLN   A 1 89  ? 25.577 13.815  20.089 1.00 16.29 ? 95  GLN   A CG  1 
ATOM   718  C  CD  . GLN   A 1 89  ? 24.928 13.373  18.797 1.00 15.61 ? 95  GLN   A CD  1 
ATOM   719  O  OE1 . GLN   A 1 89  ? 24.854 14.145  17.798 1.00 16.72 ? 95  GLN   A OE1 1 
ATOM   720  N  NE2 . GLN   A 1 89  ? 24.421 12.122  18.794 1.00 14.23 ? 95  GLN   A NE2 1 
ATOM   721  N  N   . SER   A 1 90  ? 26.476 14.610  23.301 1.00 15.03 ? 96  SER   A N   1 
ATOM   722  C  CA  . SER   A 1 90  ? 26.613 13.800  24.491 1.00 14.96 ? 96  SER   A CA  1 
ATOM   723  C  C   . SER   A 1 90  ? 25.930 12.428  24.330 1.00 16.55 ? 96  SER   A C   1 
ATOM   724  O  O   . SER   A 1 90  ? 25.084 12.237  23.429 1.00 15.98 ? 96  SER   A O   1 
ATOM   725  C  CB  . SER   A 1 90  ? 26.025 14.543  25.695 1.00 17.82 ? 96  SER   A CB  1 
ATOM   726  O  OG  . SER   A 1 90  ? 24.627 14.741  25.548 1.00 19.54 ? 96  SER   A OG  1 
ATOM   727  N  N   . HIS   A 1 91  ? 26.310 11.469  25.210 1.00 15.48 ? 97  HIS   A N   1 
ATOM   728  C  CA  . HIS   A 1 91  ? 25.712 10.123  25.242 1.00 15.03 ? 97  HIS   A CA  1 
ATOM   729  C  C   . HIS   A 1 91  ? 25.885 9.408   23.887 1.00 14.49 ? 97  HIS   A C   1 
ATOM   730  O  O   . HIS   A 1 91  ? 25.053 8.576   23.535 1.00 15.09 ? 97  HIS   A O   1 
ATOM   731  C  CB  . HIS   A 1 91  ? 24.212 10.213  25.652 1.00 16.03 ? 97  HIS   A CB  1 
ATOM   732  C  CG  . HIS   A 1 91  ? 24.017 10.777  27.041 1.00 19.12 ? 97  HIS   A CG  1 
ATOM   733  N  ND1 . HIS   A 1 91  ? 23.869 9.941   28.130 1.00 22.09 ? 97  HIS   A ND1 1 
ATOM   734  C  CD2 . HIS   A 1 91  ? 23.956 12.066  27.459 1.00 19.92 ? 97  HIS   A CD2 1 
ATOM   735  C  CE1 . HIS   A 1 91  ? 23.768 10.741  29.193 1.00 22.23 ? 97  HIS   A CE1 1 
ATOM   736  N  NE2 . HIS   A 1 91  ? 23.803 12.031  28.839 1.00 22.39 ? 97  HIS   A NE2 1 
ATOM   737  N  N   . LEU   A 1 92  ? 27.010 9.685   23.188 1.00 13.62 ? 98  LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 92  ? 27.270 9.097   21.873 1.00 13.34 ? 98  LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 92  ? 28.312 7.983   22.012 1.00 14.19 ? 98  LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 92  ? 29.290 8.104   22.759 1.00 15.18 ? 98  LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 92  ? 27.826 10.196  20.923 1.00 14.44 ? 98  LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 92  ? 28.033 9.820   19.422 1.00 16.58 ? 98  LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 92  ? 26.712 9.379   18.751 1.00 17.55 ? 98  LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 92  ? 28.607 11.050  18.649 1.00 18.19 ? 98  LEU   A CD2 1 
ATOM   745  N  N   . MET   A 1 93  ? 28.092 6.889   21.261 1.00 14.06 ? 99  MET   A N   1 
ATOM   746  C  CA  . MET   A 1 93  ? 28.995 5.725   21.294 1.00 14.25 ? 99  MET   A CA  1 
ATOM   747  C  C   . MET   A 1 93  ? 29.509 5.499   19.892 1.00 14.60 ? 99  MET   A C   1 
ATOM   748  O  O   . MET   A 1 93  ? 28.707 5.455   18.948 1.00 15.52 ? 99  MET   A O   1 
ATOM   749  C  CB  . MET   A 1 93  ? 28.205 4.498   21.715 1.00 15.66 ? 99  MET   A CB  1 
ATOM   750  C  CG  . MET   A 1 93  ? 27.608 4.681   23.113 1.00 17.22 ? 99  MET   A CG  1 
ATOM   751  S  SD  . MET   A 1 93  ? 26.520 3.355   23.688 1.00 18.86 ? 99  MET   A SD  1 
ATOM   752  C  CE  . MET   A 1 93  ? 25.167 3.487   22.487 1.00 21.00 ? 99  MET   A CE  1 
ATOM   753  N  N   . LEU   A 1 94  ? 30.833 5.360   19.715 1.00 14.83 ? 100 LEU   A N   1 
ATOM   754  C  CA  . LEU   A 1 94  ? 31.379 5.145   18.369 1.00 15.63 ? 100 LEU   A CA  1 
ATOM   755  C  C   . LEU   A 1 94  ? 31.792 3.719   18.147 1.00 15.32 ? 100 LEU   A C   1 
ATOM   756  O  O   . LEU   A 1 94  ? 32.243 3.033   19.085 1.00 15.53 ? 100 LEU   A O   1 
ATOM   757  C  CB  . LEU   A 1 94  ? 32.626 6.022   18.101 1.00 16.89 ? 100 LEU   A CB  1 
ATOM   758  C  CG  . LEU   A 1 94  ? 32.392 7.501   18.102 1.00 20.46 ? 100 LEU   A CG  1 
ATOM   759  C  CD1 . LEU   A 1 94  ? 33.680 8.258   17.638 1.00 21.66 ? 100 LEU   A CD1 1 
ATOM   760  C  CD2 . LEU   A 1 94  ? 31.250 7.894   17.188 1.00 21.91 ? 100 LEU   A CD2 1 
ATOM   761  N  N   . ALA   A 1 95  ? 31.710 3.309   16.883 1.00 15.37 ? 101 ALA   A N   1 
ATOM   762  C  CA  . ALA   A 1 95  ? 32.162 1.986   16.458 1.00 14.64 ? 101 ALA   A CA  1 
ATOM   763  C  C   . ALA   A 1 95  ? 32.702 2.060   15.048 1.00 14.26 ? 101 ALA   A C   1 
ATOM   764  O  O   . ALA   A 1 95  ? 32.374 2.998   14.319 1.00 14.96 ? 101 ALA   A O   1 
ATOM   765  C  CB  . ALA   A 1 95  ? 30.983 0.995   16.462 1.00 15.73 ? 101 ALA   A CB  1 
ATOM   766  N  N   . VAL   A 1 96  ? 33.531 1.096   14.661 1.00 13.01 ? 102 VAL   A N   1 
ATOM   767  C  CA  . VAL   A 1 96  ? 33.974 0.970   13.286 1.00 14.04 ? 102 VAL   A CA  1 
ATOM   768  C  C   . VAL   A 1 96  ? 32.857 0.202   12.544 1.00 15.44 ? 102 VAL   A C   1 
ATOM   769  O  O   . VAL   A 1 96  ? 32.428 -0.884  12.962 1.00 17.24 ? 102 VAL   A O   1 
ATOM   770  C  CB  . VAL   A 1 96  ? 35.309 0.217   13.220 1.00 14.13 ? 102 VAL   A CB  1 
ATOM   771  C  CG1 . VAL   A 1 96  ? 35.718 -0.047  11.754 1.00 14.78 ? 102 VAL   A CG1 1 
ATOM   772  C  CG2 . VAL   A 1 96  ? 36.367 1.030   13.941 1.00 15.54 ? 102 VAL   A CG2 1 
ATOM   773  N  N   . GLY   A 1 97  ? 32.385 0.794   11.452 1.00 15.16 ? 103 GLY   A N   1 
ATOM   774  C  CA  . GLY   A 1 97  ? 31.339 0.181   10.646 1.00 15.57 ? 103 GLY   A CA  1 
ATOM   775  C  C   . GLY   A 1 97  ? 30.856 1.137   9.572  1.00 15.52 ? 103 GLY   A C   1 
ATOM   776  O  O   . GLY   A 1 97  ? 31.230 2.314   9.528  1.00 15.77 ? 103 GLY   A O   1 
ATOM   777  N  N   . HIS   A 1 98  ? 30.035 0.603   8.676  1.00 15.94 ? 104 HIS   A N   1 
ATOM   778  C  CA  . HIS   A 1 98  ? 29.492 1.384   7.586  1.00 15.16 ? 104 HIS   A CA  1 
ATOM   779  C  C   . HIS   A 1 98  ? 28.319 2.269   7.977  1.00 15.59 ? 104 HIS   A C   1 
ATOM   780  O  O   . HIS   A 1 98  ? 27.453 1.843   8.709  1.00 16.74 ? 104 HIS   A O   1 
ATOM   781  C  CB  . HIS   A 1 98  ? 29.047 0.506   6.402  1.00 16.50 ? 104 HIS   A CB  1 
ATOM   782  C  CG  . HIS   A 1 98  ? 28.623 1.337   5.220  1.00 17.99 ? 104 HIS   A CG  1 
ATOM   783  N  ND1 . HIS   A 1 98  ? 29.521 2.152   4.559  1.00 19.35 ? 104 HIS   A ND1 1 
ATOM   784  C  CD2 . HIS   A 1 98  ? 27.378 1.537   4.700  1.00 18.53 ? 104 HIS   A CD2 1 
ATOM   785  C  CE1 . HIS   A 1 98  ? 28.819 2.777   3.614  1.00 21.02 ? 104 HIS   A CE1 1 
ATOM   786  N  NE2 . HIS   A 1 98  ? 27.512 2.428   3.672  1.00 19.32 ? 104 HIS   A NE2 1 
ATOM   787  N  N   . SER   A 1 99  ? 28.308 3.494   7.490  1.00 15.75 ? 105 SER   A N   1 
ATOM   788  C  CA  . SER   A 1 99  ? 27.235 4.441   7.735  1.00 15.95 ? 105 SER   A CA  1 
ATOM   789  C  C   . SER   A 1 99  ? 27.237 5.451   6.585  1.00 18.62 ? 105 SER   A C   1 
ATOM   790  O  O   . SER   A 1 99  ? 28.299 5.760   6.031  1.00 20.42 ? 105 SER   A O   1 
ATOM   791  C  CB  . SER   A 1 99  ? 27.472 5.185   9.055  1.00 18.66 ? 105 SER   A CB  1 
ATOM   792  O  OG  . SER   A 1 99  ? 28.727 5.872   8.937  1.00 19.74 ? 105 SER   A OG  1 
ATOM   793  N  N   . GLU   A 1 100 ? 26.051 5.873   6.194  1.00 16.43 ? 106 GLU   A N   1 
ATOM   794  C  CA  . GLU   A 1 100 ? 25.724 6.950   5.253  1.00 18.26 ? 106 GLU   A CA  1 
ATOM   795  C  C   . GLU   A 1 100 ? 24.588 7.780   5.869  1.00 20.51 ? 106 GLU   A C   1 
ATOM   796  O  O   . GLU   A 1 100 ? 23.881 7.304   6.739  1.00 20.31 ? 106 GLU   A O   1 
ATOM   797  C  CB  . GLU   A 1 100 ? 25.197 6.361   3.932  1.00 21.50 ? 106 GLU   A CB  1 
ATOM   798  C  CG  . GLU   A 1 100 ? 26.288 5.725   3.166  1.00 21.94 ? 106 GLU   A CG  1 
ATOM   799  C  CD  . GLU   A 1 100 ? 25.815 5.072   1.877  1.00 21.85 ? 106 GLU   A CD  1 
ATOM   800  O  OE1 . GLU   A 1 100 ? 25.020 5.683   1.109  1.00 25.43 ? 106 GLU   A OE1 1 
ATOM   801  O  OE2 . GLU   A 1 100 ? 26.291 3.946   1.623  1.00 20.50 ? 106 GLU   A OE2 1 
ATOM   802  N  N   . PRO   A 1 101 ? 24.418 9.077   5.486  1.00 23.19 ? 107 PRO   A N   1 
ATOM   803  C  CA  . PRO   A 1 101 ? 23.445 9.937   6.233  1.00 23.75 ? 107 PRO   A CA  1 
ATOM   804  C  C   . PRO   A 1 101 ? 22.029 9.346   6.540  1.00 23.47 ? 107 PRO   A C   1 
ATOM   805  O  O   . PRO   A 1 101 ? 21.545 9.391   7.712  1.00 25.35 ? 107 PRO   A O   1 
ATOM   806  C  CB  . PRO   A 1 101 ? 23.363 11.205  5.378  1.00 24.85 ? 107 PRO   A CB  1 
ATOM   807  C  CG  . PRO   A 1 101 ? 24.737 11.256  4.635  1.00 25.52 ? 107 PRO   A CG  1 
ATOM   808  C  CD  . PRO   A 1 101 ? 25.267 9.830   4.537  1.00 23.79 ? 107 PRO   A CD  1 
ATOM   809  N  N   . GLY   A 1 102 ? 21.415 8.725   5.520  1.00 19.96 ? 108 GLY   A N   1 
ATOM   810  C  CA  . GLY   A 1 102 ? 20.118 8.052   5.573  1.00 18.77 ? 108 GLY   A CA  1 
ATOM   811  C  C   . GLY   A 1 102 ? 20.068 6.851   6.511  1.00 16.52 ? 108 GLY   A C   1 
ATOM   812  O  O   . GLY   A 1 102 ? 19.003 6.274   6.757  1.00 17.44 ? 108 GLY   A O   1 
ATOM   813  N  N   . ASP   A 1 103 ? 21.240 6.434   7.038  1.00 14.45 ? 109 ASP   A N   1 
ATOM   814  C  CA  . ASP   A 1 103 ? 21.277 5.340   8.004  1.00 13.80 ? 109 ASP   A CA  1 
ATOM   815  C  C   . ASP   A 1 103 ? 20.834 5.701   9.429  1.00 14.16 ? 109 ASP   A C   1 
ATOM   816  O  O   . ASP   A 1 103 ? 20.582 4.819   10.252 1.00 14.63 ? 109 ASP   A O   1 
ATOM   817  C  CB  . ASP   A 1 103 ? 22.682 4.719   8.079  1.00 14.73 ? 109 ASP   A CB  1 
ATOM   818  C  CG  . ASP   A 1 103 ? 22.962 3.833   6.889  1.00 16.70 ? 109 ASP   A CG  1 
ATOM   819  O  OD1 . ASP   A 1 103 ? 22.007 3.211   6.383  1.00 17.49 ? 109 ASP   A OD1 1 
ATOM   820  O  OD2 . ASP   A 1 103 ? 24.150 3.793   6.433  1.00 15.61 ? 109 ASP   A OD2 1 
ATOM   821  N  N   . CYS   A 1 104 ? 20.697 6.991   9.720  1.00 14.06 ? 110 CYS   A N   1 
ATOM   822  C  CA  . CYS   A 1 104 ? 20.266 7.438   11.056 1.00 13.91 ? 110 CYS   A CA  1 
ATOM   823  C  C   . CYS   A 1 104 ? 18.911 6.842   11.382 1.00 14.33 ? 110 CYS   A C   1 
ATOM   824  O  O   . CYS   A 1 104 ? 18.038 6.822   10.516 1.00 15.31 ? 110 CYS   A O   1 
ATOM   825  C  CB  . CYS   A 1 104 ? 20.228 8.963   11.121 1.00 14.59 ? 110 CYS   A CB  1 
ATOM   826  S  SG  . CYS   A 1 104 ? 21.873 9.722   11.163 1.00 17.33 ? 110 CYS   A SG  1 
ATOM   827  N  N   . GLY   A 1 105 ? 18.769 6.346   12.594 1.00 13.48 ? 111 GLY   A N   1 
ATOM   828  C  CA  . GLY   A 1 105 ? 17.511 5.714   12.995 1.00 13.98 ? 111 GLY   A CA  1 
ATOM   829  C  C   . GLY   A 1 105 ? 17.610 4.196   13.041 1.00 14.49 ? 111 GLY   A C   1 
ATOM   830  O  O   . GLY   A 1 105 ? 16.778 3.542   13.668 1.00 15.15 ? 111 GLY   A O   1 
ATOM   831  N  N   . GLY   A 1 106 ? 18.657 3.614   12.449 1.00 13.31 ? 112 GLY   A N   1 
ATOM   832  C  CA  . GLY   A 1 106 ? 18.858 2.157   12.535 1.00 12.14 ? 112 GLY   A CA  1 
ATOM   833  C  C   . GLY   A 1 106 ? 19.084 1.753   13.987 1.00 12.95 ? 112 GLY   A C   1 
ATOM   834  O  O   . GLY   A 1 106 ? 19.825 2.417   14.706 1.00 14.41 ? 112 GLY   A O   1 
ATOM   835  N  N   . ILE   A 1 107 ? 18.477 0.651   14.415 1.00 12.62 ? 113 ILE   A N   1 
ATOM   836  C  CA  . ILE   A 1 107 ? 18.590 0.231   15.799 1.00 12.07 ? 113 ILE   A CA  1 
ATOM   837  C  C   . ILE   A 1 107 ? 19.844 -0.588  16.082 1.00 12.57 ? 113 ILE   A C   1 
ATOM   838  O  O   . ILE   A 1 107 ? 20.194 -1.488  15.306 1.00 13.74 ? 113 ILE   A O   1 
ATOM   839  C  CB  . ILE   A 1 107 ? 17.290 -0.520  16.231 1.00 14.75 ? 113 ILE   A CB  1 
ATOM   840  C  CG1 . ILE   A 1 107 ? 16.151 0.515   16.390 1.00 16.64 ? 113 ILE   A CG1 1 
ATOM   841  C  CG2 . ILE   A 1 107 ? 17.472 -1.320  17.530 1.00 17.09 ? 113 ILE   A CG2 1 
ATOM   842  C  CD1 . ILE   A 1 107 ? 14.749 -0.187  16.618 1.00 19.79 ? 113 ILE   A CD1 1 
ATOM   843  N  N   . LEU   A 1 108 ? 20.465 -0.323  17.237 1.00 12.23 ? 114 LEU   A N   1 
ATOM   844  C  CA  . LEU   A 1 108 ? 21.579 -1.119  17.788 1.00 12.18 ? 114 LEU   A CA  1 
ATOM   845  C  C   . LEU   A 1 108 ? 20.954 -1.923  18.952 1.00 13.72 ? 114 LEU   A C   1 
ATOM   846  O  O   . LEU   A 1 108 ? 20.283 -1.337  19.823 1.00 13.46 ? 114 LEU   A O   1 
ATOM   847  C  CB  . LEU   A 1 108 ? 22.655 -0.177  18.352 1.00 12.36 ? 114 LEU   A CB  1 
ATOM   848  C  CG  . LEU   A 1 108 ? 23.798 -0.858  19.159 1.00 13.14 ? 114 LEU   A CG  1 
ATOM   849  C  CD1 . LEU   A 1 108 ? 24.625 -1.801  18.280 1.00 15.14 ? 114 LEU   A CD1 1 
ATOM   850  C  CD2 . LEU   A 1 108 ? 24.707 0.222   19.774 1.00 13.81 ? 114 LEU   A CD2 1 
ATOM   851  N  N   . ARG   A 1 109 ? 21.181 -3.266  18.963 1.00 13.04 ? 115 ARG   A N   1 
ATOM   852  C  CA  . ARG   A 1 109 ? 20.662 -4.138  20.007 1.00 13.32 ? 115 ARG   A CA  1 
ATOM   853  C  C   . ARG   A 1 109 ? 21.772 -4.996  20.561 1.00 15.08 ? 115 ARG   A C   1 
ATOM   854  O  O   . ARG   A 1 109 ? 22.685 -5.422  19.846 1.00 14.99 ? 115 ARG   A O   1 
ATOM   855  C  CB  . ARG   A 1 109 ? 19.600 -5.126  19.412 1.00 15.39 ? 115 ARG   A CB  1 
ATOM   856  C  CG  . ARG   A 1 109 ? 18.200 -4.529  19.185 1.00 19.53 ? 115 ARG   A CG  1 
ATOM   857  C  CD  . ARG   A 1 109 ? 17.153 -5.503  18.560 1.00 20.54 ? 115 ARG   A CD  1 
ATOM   858  N  NE  . ARG   A 1 109 ? 15.747 -5.002  18.725 1.00 22.63 ? 115 ARG   A NE  1 
ATOM   859  C  CZ  . ARG   A 1 109 ? 14.930 -5.335  19.718 1.00 22.39 ? 115 ARG   A CZ  1 
ATOM   860  N  NH1 . ARG   A 1 109 ? 15.358 -6.111  20.715 1.00 20.22 ? 115 ARG   A NH1 1 
ATOM   861  N  NH2 . ARG   A 1 109 ? 13.689 -4.857  19.758 1.00 25.32 ? 115 ARG   A NH2 1 
ATOM   862  N  N   . CYS   A 1 110 ? 21.643 -5.339  21.847 1.00 14.90 ? 116 CYS   A N   1 
ATOM   863  C  CA  . CYS   A 1 110 ? 22.526 -6.370  22.453 1.00 15.32 ? 116 CYS   A CA  1 
ATOM   864  C  C   . CYS   A 1 110 ? 21.588 -7.514  22.907 1.00 16.11 ? 116 CYS   A C   1 
ATOM   865  O  O   . CYS   A 1 110 ? 20.380 -7.485  22.625 1.00 16.29 ? 116 CYS   A O   1 
ATOM   866  C  CB  . CYS   A 1 110 ? 23.275 -5.777  23.645 1.00 16.14 ? 116 CYS   A CB  1 
ATOM   867  S  SG  . CYS   A 1 110 ? 22.170 -5.278  25.002 1.00 14.85 ? 116 CYS   A SG  1 
ATOM   868  N  N   . GLN   A 1 111 ? 22.104 -8.503  23.659 1.00 16.58 ? 117 GLN   A N   1 
ATOM   869  C  CA  . GLN   A 1 111 ? 21.254 -9.600  24.125 1.00 16.87 ? 117 GLN   A CA  1 
ATOM   870  C  C   . GLN   A 1 111 ? 20.135 -9.143  25.084 1.00 17.11 ? 117 GLN   A C   1 
ATOM   871  O  O   . GLN   A 1 111 ? 19.201 -9.924  25.345 1.00 18.40 ? 117 GLN   A O   1 
ATOM   872  C  CB  . GLN   A 1 111 ? 22.126 -10.704 24.793 1.00 19.60 ? 117 GLN   A CB  1 
ATOM   873  C  CG  . GLN   A 1 111 ? 22.689 -10.256 26.144 1.00 25.72 ? 117 GLN   A CG  1 
ATOM   874  C  CD  . GLN   A 1 111 ? 23.648 -11.267 26.727 1.00 35.80 ? 117 GLN   A CD  1 
ATOM   875  O  OE1 . GLN   A 1 111 ? 24.881 -11.139 26.648 1.00 40.28 ? 117 GLN   A OE1 1 
ATOM   876  N  NE2 . GLN   A 1 111 ? 23.088 -12.272 27.342 1.00 35.47 ? 117 GLN   A NE2 1 
ATOM   877  N  N   . HIS   A 1 112 ? 20.215 -7.917  25.633 1.00 16.43 ? 118 HIS   A N   1 
ATOM   878  C  CA  . HIS   A 1 112 ? 19.226 -7.432  26.619 1.00 16.43 ? 118 HIS   A CA  1 
ATOM   879  C  C   . HIS   A 1 112 ? 18.123 -6.581  26.026 1.00 15.86 ? 118 HIS   A C   1 
ATOM   880  O  O   . HIS   A 1 112 ? 17.127 -6.341  26.731 1.00 17.01 ? 118 HIS   A O   1 
ATOM   881  C  CB  . HIS   A 1 112 ? 19.924 -6.626  27.744 1.00 16.51 ? 118 HIS   A CB  1 
ATOM   882  C  CG  . HIS   A 1 112 ? 21.024 -7.409  28.401 1.00 17.60 ? 118 HIS   A CG  1 
ATOM   883  N  ND1 . HIS   A 1 112 ? 22.356 -7.084  28.201 1.00 19.16 ? 118 HIS   A ND1 1 
ATOM   884  C  CD2 . HIS   A 1 112 ? 20.957 -8.486  29.233 1.00 19.97 ? 118 HIS   A CD2 1 
ATOM   885  C  CE1 . HIS   A 1 112 ? 23.062 -7.972  28.889 1.00 20.85 ? 118 HIS   A CE1 1 
ATOM   886  N  NE2 . HIS   A 1 112 ? 22.268 -8.846  29.515 1.00 21.65 ? 118 HIS   A NE2 1 
ATOM   887  N  N   . GLY   A 1 113 ? 18.296 -6.128  24.772 1.00 13.88 ? 119 GLY   A N   1 
ATOM   888  C  CA  . GLY   A 1 113 ? 17.287 -5.293  24.152 1.00 14.64 ? 119 GLY   A CA  1 
ATOM   889  C  C   . GLY   A 1 113 ? 17.914 -4.163  23.353 1.00 12.99 ? 119 GLY   A C   1 
ATOM   890  O  O   . GLY   A 1 113 ? 19.086 -4.217  22.937 1.00 14.38 ? 119 GLY   A O   1 
ATOM   891  N  N   . VAL   A 1 114 ? 17.119 -3.118  23.136 1.00 12.52 ? 120 VAL   A N   1 
ATOM   892  C  CA  . VAL   A 1 114 ? 17.568 -1.979  22.350 1.00 12.77 ? 120 VAL   A CA  1 
ATOM   893  C  C   . VAL   A 1 114 ? 18.542 -1.129  23.155 1.00 12.82 ? 120 VAL   A C   1 
ATOM   894  O  O   . VAL   A 1 114 ? 18.249 -0.736  24.303 1.00 13.72 ? 120 VAL   A O   1 
ATOM   895  C  CB  . VAL   A 1 114 ? 16.353 -1.121  21.946 1.00 13.62 ? 120 VAL   A CB  1 
ATOM   896  C  CG1 . VAL   A 1 114 ? 16.823 0.187   21.281 1.00 14.84 ? 120 VAL   A CG1 1 
ATOM   897  C  CG2 . VAL   A 1 114 ? 15.458 -1.916  20.979 1.00 15.11 ? 120 VAL   A CG2 1 
ATOM   898  N  N   . VAL   A 1 115 ? 19.693 -0.812  22.540 1.00 12.86 ? 121 VAL   A N   1 
ATOM   899  C  CA  . VAL   A 1 115 ? 20.741 -0.006  23.167 1.00 12.96 ? 121 VAL   A CA  1 
ATOM   900  C  C   . VAL   A 1 115 ? 20.673 1.463   22.701 1.00 14.25 ? 121 VAL   A C   1 
ATOM   901  O  O   . VAL   A 1 115 ? 20.915 2.395   23.492 1.00 13.73 ? 121 VAL   A O   1 
ATOM   902  C  CB  . VAL   A 1 115 ? 22.108 -0.607  22.782 1.00 14.19 ? 121 VAL   A CB  1 
ATOM   903  C  CG1 . VAL   A 1 115 ? 23.270 0.318   23.213 1.00 15.50 ? 121 VAL   A CG1 1 
ATOM   904  C  CG2 . VAL   A 1 115 ? 22.272 -2.024  23.366 1.00 14.19 ? 121 VAL   A CG2 1 
ATOM   905  N  N   . GLY   A 1 116 ? 20.406 1.669   21.412 1.00 13.44 ? 122 GLY   A N   1 
ATOM   906  C  CA  . GLY   A 1 116 ? 20.375 3.036   20.878 1.00 13.45 ? 122 GLY   A CA  1 
ATOM   907  C  C   . GLY   A 1 116 ? 20.096 3.056   19.394 1.00 13.32 ? 122 GLY   A C   1 
ATOM   908  O  O   . GLY   A 1 116 ? 19.689 2.035   18.827 1.00 13.41 ? 122 GLY   A O   1 
ATOM   909  N  N   . ILE   A 1 117 ? 20.258 4.227   18.775 1.00 13.19 ? 123 ILE   A N   1 
ATOM   910  C  CA  . ILE   A 1 117 ? 19.956 4.358   17.337 1.00 12.72 ? 123 ILE   A CA  1 
ATOM   911  C  C   . ILE   A 1 117 ? 21.122 5.040   16.645 1.00 11.80 ? 123 ILE   A C   1 
ATOM   912  O  O   . ILE   A 1 117 ? 21.760 5.921   17.237 1.00 12.40 ? 123 ILE   A O   1 
ATOM   913  C  CB  . ILE   A 1 117 ? 18.644 5.163   17.086 1.00 14.42 ? 123 ILE   A CB  1 
ATOM   914  C  CG1 . ILE   A 1 117 ? 18.600 6.489   17.876 1.00 14.78 ? 123 ILE   A CG1 1 
ATOM   915  C  CG2 . ILE   A 1 117 ? 17.412 4.295   17.345 1.00 16.82 ? 123 ILE   A CG2 1 
ATOM   916  C  CD1 . ILE   A 1 117 ? 17.407 7.365   17.383 1.00 17.51 ? 123 ILE   A CD1 1 
ATOM   917  N  N   . VAL   A 1 118 ? 21.355 4.724   15.351 1.00 11.64 ? 124 VAL   A N   1 
ATOM   918  C  CA  . VAL   A 1 118 ? 22.403 5.418   14.572 1.00 12.02 ? 124 VAL   A CA  1 
ATOM   919  C  C   . VAL   A 1 118 ? 22.117 6.913   14.564 1.00 12.31 ? 124 VAL   A C   1 
ATOM   920  O  O   . VAL   A 1 118 ? 20.973 7.308   14.328 1.00 12.86 ? 124 VAL   A O   1 
ATOM   921  C  CB  . VAL   A 1 118 ? 22.464 4.894   13.128 1.00 12.54 ? 124 VAL   A CB  1 
ATOM   922  C  CG1 . VAL   A 1 118 ? 23.508 5.684   12.318 1.00 13.67 ? 124 VAL   A CG1 1 
ATOM   923  C  CG2 . VAL   A 1 118 ? 22.823 3.393   13.107 1.00 14.62 ? 124 VAL   A CG2 1 
ATOM   924  N  N   . SER   A 1 119 ? 23.153 7.721   14.834 1.00 12.08 ? 125 SER   A N   1 
ATOM   925  C  CA  . SER   A 1 119 ? 23.005 9.175   14.887 1.00 12.43 ? 125 SER   A CA  1 
ATOM   926  C  C   . SER   A 1 119 ? 24.105 9.893   14.115 1.00 14.26 ? 125 SER   A C   1 
ATOM   927  O  O   . SER   A 1 119 ? 23.886 11.024  13.663 1.00 15.01 ? 125 SER   A O   1 
ATOM   928  C  CB  . SER   A 1 119 ? 23.005 9.622   16.354 1.00 13.99 ? 125 SER   A CB  1 
ATOM   929  O  OG  . SER   A 1 119 ? 22.910 11.039  16.489 1.00 15.10 ? 125 SER   A OG  1 
ATOM   930  N  N   . THR   A 1 120 ? 25.287 9.287   13.965 1.00 13.95 ? 126 THR   A N   1 
ATOM   931  C  CA  . THR   A 1 120 ? 26.389 9.956   13.236 1.00 15.61 ? 126 THR   A CA  1 
ATOM   932  C  C   . THR   A 1 120 ? 27.142 8.935   12.390 1.00 16.33 ? 126 THR   A C   1 
ATOM   933  O  O   . THR   A 1 120 ? 26.981 7.719   12.558 1.00 15.64 ? 126 THR   A O   1 
ATOM   934  C  CB  . THR   A 1 120 ? 27.404 10.659  14.207 1.00 17.91 ? 126 THR   A CB  1 
ATOM   935  O  OG1 . THR   A 1 120 ? 28.206 9.675   14.873 1.00 18.73 ? 126 THR   A OG1 1 
ATOM   936  C  CG2 . THR   A 1 120 ? 26.775 11.612  15.193 1.00 19.02 ? 126 THR   A CG2 1 
ATOM   937  N  N   . GLY   A 1 121 ? 28.010 9.438   11.516 1.00 17.61 ? 127 GLY   A N   1 
ATOM   938  C  CA  . GLY   A 1 121 ? 28.898 8.587   10.763 1.00 19.47 ? 127 GLY   A CA  1 
ATOM   939  C  C   . GLY   A 1 121 ? 30.147 9.321   10.317 1.00 20.62 ? 127 GLY   A C   1 
ATOM   940  O  O   . GLY   A 1 121 ? 30.166 10.546  10.207 1.00 20.98 ? 127 GLY   A O   1 
ATOM   941  N  N   . GLY   A 1 122 ? 31.181 8.549   10.059 1.00 20.34 ? 128 GLY   A N   1 
ATOM   942  C  CA  . GLY   A 1 122 ? 32.454 9.044   9.545  1.00 20.32 ? 128 GLY   A CA  1 
ATOM   943  C  C   . GLY   A 1 122 ? 32.986 8.113   8.479  1.00 20.22 ? 128 GLY   A C   1 
ATOM   944  O  O   . GLY   A 1 122 ? 32.245 7.292   7.942  1.00 21.17 ? 128 GLY   A O   1 
ATOM   945  N  N   . ASN   A 1 123 ? 34.287 8.232   8.150  1.00 18.99 ? 129 ASN   A N   1 
ATOM   946  C  CA  . ASN   A 1 123 ? 34.891 7.386   7.125  1.00 18.77 ? 129 ASN   A CA  1 
ATOM   947  C  C   . ASN   A 1 123 ? 35.210 6.062   7.782  1.00 18.55 ? 129 ASN   A C   1 
ATOM   948  O  O   . ASN   A 1 123 ? 36.334 5.857   8.284  1.00 18.61 ? 129 ASN   A O   1 
ATOM   949  C  CB  . ASN   A 1 123 ? 36.144 8.088   6.566  1.00 20.95 ? 129 ASN   A CB  1 
ATOM   950  C  CG  . ASN   A 1 123 ? 36.681 7.495   5.292  1.00 26.64 ? 129 ASN   A CG  1 
ATOM   951  O  OD1 . ASN   A 1 123 ? 36.052 6.629   4.665  1.00 28.23 ? 129 ASN   A OD1 1 
ATOM   952  N  ND2 . ASN   A 1 123 ? 37.898 7.904   4.902  1.00 27.60 ? 129 ASN   A ND2 1 
ATOM   953  N  N   . GLY   A 1 124 ? 34.244 5.128   7.741  1.00 17.10 ? 130 GLY   A N   1 
ATOM   954  C  CA  . GLY   A 1 124 ? 34.393 3.845   8.399  1.00 16.80 ? 130 GLY   A CA  1 
ATOM   955  C  C   . GLY   A 1 124 ? 34.035 3.886   9.877  1.00 16.44 ? 130 GLY   A C   1 
ATOM   956  O  O   . GLY   A 1 124 ? 34.420 2.971   10.628 1.00 18.03 ? 130 GLY   A O   1 
ATOM   957  N  N   . LEU   A 1 125 ? 33.311 4.924   10.313 1.00 15.19 ? 131 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 125 ? 32.818 5.013   11.683 1.00 14.45 ? 131 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 125 ? 31.289 5.131   11.667 1.00 13.94 ? 131 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 125 ? 30.711 5.683   10.720 1.00 15.04 ? 131 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 125 ? 33.371 6.265   12.406 1.00 14.41 ? 131 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 125 ? 34.896 6.237   12.660 1.00 16.80 ? 131 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 125 ? 35.381 7.651   13.042 1.00 19.49 ? 131 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 125 ? 35.220 5.226   13.780 1.00 16.70 ? 131 LEU   A CD2 1 
ATOM   965  N  N   . VAL   A 1 126 ? 30.665 4.650   12.746 1.00 12.65 ? 132 VAL   A N   1 
ATOM   966  C  CA  . VAL   A 1 126 ? 29.227 4.785   12.954 1.00 11.86 ? 132 VAL   A CA  1 
ATOM   967  C  C   . VAL   A 1 126 ? 29.041 5.177   14.433 1.00 13.44 ? 132 VAL   A C   1 
ATOM   968  O  O   . VAL   A 1 126 ? 29.714 4.613   15.319 1.00 14.31 ? 132 VAL   A O   1 
ATOM   969  C  CB  . VAL   A 1 126 ? 28.409 3.549   12.542 1.00 13.64 ? 132 VAL   A CB  1 
ATOM   970  C  CG1 . VAL   A 1 126 ? 28.895 2.281   13.222 1.00 15.77 ? 132 VAL   A CG1 1 
ATOM   971  C  CG2 . VAL   A 1 126 ? 26.917 3.757   12.812 1.00 14.32 ? 132 VAL   A CG2 1 
ATOM   972  N  N   . GLY   A 1 127 ? 28.197 6.186   14.664 1.00 13.42 ? 133 GLY   A N   1 
ATOM   973  C  CA  . GLY   A 1 127 ? 27.930 6.643   16.023 1.00 13.76 ? 133 GLY   A CA  1 
ATOM   974  C  C   . GLY   A 1 127 ? 26.486 6.400   16.409 1.00 12.90 ? 133 GLY   A C   1 
ATOM   975  O  O   . GLY   A 1 127 ? 25.587 6.581   15.589 1.00 13.69 ? 133 GLY   A O   1 
ATOM   976  N  N   . PHE   A 1 128 ? 26.258 5.961   17.640 1.00 12.73 ? 134 PHE   A N   1 
ATOM   977  C  CA  . PHE   A 1 128 ? 24.924 5.603   18.117 1.00 12.32 ? 134 PHE   A CA  1 
ATOM   978  C  C   . PHE   A 1 128 ? 24.561 6.473   19.342 1.00 12.79 ? 134 PHE   A C   1 
ATOM   979  O  O   . PHE   A 1 128 ? 25.365 6.606   20.275 1.00 13.97 ? 134 PHE   A O   1 
ATOM   980  C  CB  . PHE   A 1 128 ? 24.891 4.134   18.602 1.00 12.88 ? 134 PHE   A CB  1 
ATOM   981  C  CG  . PHE   A 1 128 ? 25.376 3.139   17.576 1.00 13.23 ? 134 PHE   A CG  1 
ATOM   982  C  CD1 . PHE   A 1 128 ? 24.518 2.650   16.614 1.00 13.32 ? 134 PHE   A CD1 1 
ATOM   983  C  CD2 . PHE   A 1 128 ? 26.684 2.671   17.604 1.00 13.81 ? 134 PHE   A CD2 1 
ATOM   984  C  CE1 . PHE   A 1 128 ? 24.965 1.735   15.664 1.00 13.10 ? 134 PHE   A CE1 1 
ATOM   985  C  CE2 . PHE   A 1 128 ? 27.127 1.717   16.689 1.00 13.95 ? 134 PHE   A CE2 1 
ATOM   986  C  CZ  . PHE   A 1 128 ? 26.278 1.281   15.691 1.00 13.57 ? 134 PHE   A CZ  1 
ATOM   987  N  N   . ALA   A 1 129 ? 23.343 7.034   19.318 1.00 12.38 ? 135 ALA   A N   1 
ATOM   988  C  CA  . ALA   A 1 129 ? 22.823 7.758   20.438 1.00 13.07 ? 135 ALA   A CA  1 
ATOM   989  C  C   . ALA   A 1 129 ? 22.313 6.715   21.440 1.00 12.59 ? 135 ALA   A C   1 
ATOM   990  O  O   . ALA   A 1 129 ? 21.373 5.955   21.115 1.00 13.36 ? 135 ALA   A O   1 
ATOM   991  C  CB  . ALA   A 1 129 ? 21.684 8.669   19.991 1.00 12.86 ? 135 ALA   A CB  1 
ATOM   992  N  N   . ASP   A 1 130 ? 22.885 6.707   22.663 1.00 12.65 ? 136 ASP   A N   1 
ATOM   993  C  CA  . ASP   A 1 130 ? 22.461 5.764   23.695 1.00 13.85 ? 136 ASP   A CA  1 
ATOM   994  C  C   . ASP   A 1 130 ? 21.086 6.123   24.228 1.00 14.24 ? 136 ASP   A C   1 
ATOM   995  O  O   . ASP   A 1 130 ? 20.749 7.327   24.387 1.00 14.72 ? 136 ASP   A O   1 
ATOM   996  C  CB  . ASP   A 1 130 ? 23.465 5.782   24.855 1.00 15.26 ? 136 ASP   A CB  1 
ATOM   997  C  CG  . ASP   A 1 130 ? 23.195 4.739   25.916 1.00 20.37 ? 136 ASP   A CG  1 
ATOM   998  O  OD1 . ASP   A 1 130 ? 23.103 3.574   25.574 1.00 21.30 ? 136 ASP   A OD1 1 
ATOM   999  O  OD2 . ASP   A 1 130 ? 23.038 5.113   27.092 1.00 24.52 ? 136 ASP   A OD2 1 
ATOM   1000 N  N   . VAL   A 1 131 ? 20.261 5.083   24.546 1.00 13.59 ? 137 VAL   A N   1 
ATOM   1001 C  CA  . VAL   A 1 131 ? 18.974 5.321   25.203 1.00 13.78 ? 137 VAL   A CA  1 
ATOM   1002 C  C   . VAL   A 1 131 ? 18.855 4.549   26.536 1.00 14.17 ? 137 VAL   A C   1 
ATOM   1003 O  O   . VAL   A 1 131 ? 17.814 4.615   27.175 1.00 15.64 ? 137 VAL   A O   1 
ATOM   1004 C  CB  . VAL   A 1 131 ? 17.743 5.005   24.316 1.00 15.24 ? 137 VAL   A CB  1 
ATOM   1005 C  CG1 . VAL   A 1 131 ? 17.749 5.873   23.041 1.00 15.46 ? 137 VAL   A CG1 1 
ATOM   1006 C  CG2 . VAL   A 1 131 ? 17.705 3.511   23.972 1.00 15.79 ? 137 VAL   A CG2 1 
ATOM   1007 N  N   . ARG   A 1 132 ? 19.899 3.806   26.937 1.00 14.46 ? 138 ARG   A N   1 
ATOM   1008 C  CA  . ARG   A 1 132 ? 19.811 2.936   28.121 1.00 14.65 ? 138 ARG   A CA  1 
ATOM   1009 C  C   . ARG   A 1 132 ? 19.639 3.667   29.433 1.00 16.21 ? 138 ARG   A C   1 
ATOM   1010 O  O   . ARG   A 1 132 ? 19.153 3.056   30.403 1.00 16.59 ? 138 ARG   A O   1 
ATOM   1011 C  CB  . ARG   A 1 132 ? 21.018 1.978   28.196 1.00 13.87 ? 138 ARG   A CB  1 
ATOM   1012 C  CG  . ARG   A 1 132 ? 21.066 1.012   27.009 1.00 14.52 ? 138 ARG   A CG  1 
ATOM   1013 C  CD  . ARG   A 1 132 ? 22.333 0.175   27.092 1.00 15.04 ? 138 ARG   A CD  1 
ATOM   1014 N  NE  . ARG   A 1 132 ? 23.488 1.010   26.779 1.00 14.85 ? 138 ARG   A NE  1 
ATOM   1015 C  CZ  . ARG   A 1 132 ? 24.731 0.545   26.660 1.00 16.89 ? 138 ARG   A CZ  1 
ATOM   1016 N  NH1 . ARG   A 1 132 ? 25.000 -0.734  26.923 1.00 16.26 ? 138 ARG   A NH1 1 
ATOM   1017 N  NH2 . ARG   A 1 132 ? 25.712 1.349   26.255 1.00 17.18 ? 138 ARG   A NH2 1 
ATOM   1018 N  N   . ASP   A 1 133 ? 20.037 4.960   29.474 1.00 15.91 ? 139 ASP   A N   1 
ATOM   1019 C  CA  . ASP   A 1 133 ? 19.868 5.731   30.713 1.00 17.49 ? 139 ASP   A CA  1 
ATOM   1020 C  C   . ASP   A 1 133 ? 18.480 6.331   30.874 1.00 17.28 ? 139 ASP   A C   1 
ATOM   1021 O  O   . ASP   A 1 133 ? 18.196 6.865   31.951 1.00 18.57 ? 139 ASP   A O   1 
ATOM   1022 C  CB  . ASP   A 1 133 ? 20.900 6.872   30.762 1.00 18.56 ? 139 ASP   A CB  1 
ATOM   1023 C  CG  . ASP   A 1 133 ? 20.709 7.894   29.663 1.00 21.49 ? 139 ASP   A CG  1 
ATOM   1024 O  OD1 . ASP   A 1 133 ? 20.499 7.487   28.499 1.00 21.61 ? 139 ASP   A OD1 1 
ATOM   1025 O  OD2 . ASP   A 1 133 ? 20.725 9.115   29.971 1.00 25.49 ? 139 ASP   A OD2 1 
ATOM   1026 N  N   . LEU   A 1 134 ? 17.623 6.255   29.852 1.00 16.87 ? 140 LEU   A N   1 
ATOM   1027 C  CA  . LEU   A 1 134 ? 16.289 6.862   29.905 1.00 15.50 ? 140 LEU   A CA  1 
ATOM   1028 C  C   . LEU   A 1 134 ? 15.320 5.878   30.575 1.00 15.77 ? 140 LEU   A C   1 
ATOM   1029 O  O   . LEU   A 1 134 ? 14.549 5.165   29.904 1.00 15.71 ? 140 LEU   A O   1 
ATOM   1030 C  CB  . LEU   A 1 134 ? 15.842 7.244   28.474 1.00 15.61 ? 140 LEU   A CB  1 
ATOM   1031 C  CG  . LEU   A 1 134 ? 16.820 8.179   27.727 1.00 17.80 ? 140 LEU   A CG  1 
ATOM   1032 C  CD1 . LEU   A 1 134 ? 16.341 8.385   26.291 1.00 18.62 ? 140 LEU   A CD1 1 
ATOM   1033 C  CD2 . LEU   A 1 134 ? 16.979 9.490   28.463 1.00 18.93 ? 140 LEU   A CD2 1 
ATOM   1034 N  N   . LEU   A 1 135 ? 15.405 5.778   31.910 1.00 16.53 ? 141 LEU   A N   1 
ATOM   1035 C  CA  . LEU   A 1 135 ? 14.643 4.728   32.623 1.00 16.63 ? 141 LEU   A CA  1 
ATOM   1036 C  C   . LEU   A 1 135 ? 13.145 4.896   32.523 1.00 17.79 ? 141 LEU   A C   1 
ATOM   1037 O  O   . LEU   A 1 135 ? 12.400 3.902   32.590 1.00 18.77 ? 141 LEU   A O   1 
ATOM   1038 C  CB  . LEU   A 1 135 ? 15.068 4.673   34.091 1.00 16.38 ? 141 LEU   A CB  1 
ATOM   1039 C  CG  . LEU   A 1 135 ? 16.586 4.618   34.323 1.00 18.38 ? 141 LEU   A CG  1 
ATOM   1040 C  CD1 . LEU   A 1 135 ? 16.876 4.334   35.824 1.00 18.80 ? 141 LEU   A CD1 1 
ATOM   1041 C  CD2 . LEU   A 1 135 ? 17.279 3.504   33.455 1.00 19.13 ? 141 LEU   A CD2 1 
ATOM   1042 N  N   . TRP   A 1 136 ? 12.702 6.170   32.383 1.00 17.94 ? 142 TRP   A N   1 
ATOM   1043 C  CA  . TRP   A 1 136 ? 11.279 6.471   32.304 1.00 18.99 ? 142 TRP   A CA  1 
ATOM   1044 C  C   . TRP   A 1 136 ? 10.610 5.901   31.046 1.00 20.47 ? 142 TRP   A C   1 
ATOM   1045 O  O   . TRP   A 1 136 ? 9.371  5.883   30.989 1.00 22.62 ? 142 TRP   A O   1 
ATOM   1046 C  CB  . TRP   A 1 136 ? 11.062 8.000   32.397 1.00 19.10 ? 142 TRP   A CB  1 
ATOM   1047 C  CG  . TRP   A 1 136 ? 11.892 8.815   31.430 1.00 19.49 ? 142 TRP   A CG  1 
ATOM   1048 C  CD1 . TRP   A 1 136 ? 13.128 9.359   31.645 1.00 20.13 ? 142 TRP   A CD1 1 
ATOM   1049 C  CD2 . TRP   A 1 136 ? 11.528 9.165   30.090 1.00 19.80 ? 142 TRP   A CD2 1 
ATOM   1050 N  NE1 . TRP   A 1 136 ? 13.536 10.067  30.530 1.00 20.59 ? 142 TRP   A NE1 1 
ATOM   1051 C  CE2 . TRP   A 1 136 ? 12.564 9.975   29.568 1.00 20.45 ? 142 TRP   A CE2 1 
ATOM   1052 C  CE3 . TRP   A 1 136 ? 10.400 8.919   29.309 1.00 20.35 ? 142 TRP   A CE3 1 
ATOM   1053 C  CZ2 . TRP   A 1 136 ? 12.526 10.497  28.271 1.00 20.35 ? 142 TRP   A CZ2 1 
ATOM   1054 C  CZ3 . TRP   A 1 136 ? 10.347 9.458   28.034 1.00 20.51 ? 142 TRP   A CZ3 1 
ATOM   1055 C  CH2 . TRP   A 1 136 ? 11.371 10.291  27.556 1.00 20.69 ? 142 TRP   A CH2 1 
ATOM   1056 N  N   . LEU   A 1 137 ? 11.385 5.458   30.030 1.00 19.45 ? 143 LEU   A N   1 
ATOM   1057 C  CA  . LEU   A 1 137 ? 10.749 4.890   28.824 1.00 20.20 ? 143 LEU   A CA  1 
ATOM   1058 C  C   . LEU   A 1 137 ? 9.916  3.640   29.163 1.00 23.77 ? 143 LEU   A C   1 
ATOM   1059 O  O   . LEU   A 1 137 ? 8.974  3.335   28.434 1.00 24.30 ? 143 LEU   A O   1 
ATOM   1060 C  CB  . LEU   A 1 137 ? 11.800 4.492   27.778 1.00 18.20 ? 143 LEU   A CB  1 
ATOM   1061 C  CG  . LEU   A 1 137 ? 12.483 5.649   27.071 1.00 18.45 ? 143 LEU   A CG  1 
ATOM   1062 C  CD1 . LEU   A 1 137 ? 13.607 5.150   26.181 1.00 19.99 ? 143 LEU   A CD1 1 
ATOM   1063 C  CD2 . LEU   A 1 137 ? 11.460 6.458   26.188 1.00 18.33 ? 143 LEU   A CD2 1 
ATOM   1064 N  N   . ASP   A 1 138 ? 10.321 2.910   30.239 1.00 26.30 ? 144 ASP   A N   1 
ATOM   1065 C  CA  . ASP   A 1 138 ? 9.801  1.634   30.758 1.00 31.11 ? 144 ASP   A CA  1 
ATOM   1066 C  C   . ASP   A 1 138 ? 8.612  1.742   31.665 1.00 35.25 ? 144 ASP   A C   1 
ATOM   1067 O  O   . ASP   A 1 138 ? 8.104  0.689   32.066 1.00 36.20 ? 144 ASP   A O   1 
ATOM   1068 C  CB  . ASP   A 1 138 ? 10.866 1.013   31.692 1.00 33.75 ? 144 ASP   A CB  1 
ATOM   1069 C  CG  . ASP   A 1 138 ? 12.035 0.361   31.045 1.00 40.93 ? 144 ASP   A CG  1 
ATOM   1070 O  OD1 . ASP   A 1 138 ? 11.944 0.056   29.852 1.00 42.76 ? 144 ASP   A OD1 1 
ATOM   1071 O  OD2 . ASP   A 1 138 ? 13.054 0.134   31.750 1.00 45.62 ? 144 ASP   A OD2 1 
ATOM   1072 N  N   . GLU   A 1 139 ? 8.282  2.943   32.149 1.00 37.72 ? 145 GLU   A N   1 
ATOM   1073 C  CA  . GLU   A 1 139 ? 7.184  3.076   33.110 1.00 41.00 ? 145 GLU   A CA  1 
ATOM   1074 C  C   . GLU   A 1 139 ? 5.994  3.845   32.548 1.00 42.87 ? 145 GLU   A C   1 
ATOM   1075 O  O   . GLU   A 1 139 ? 6.163  4.693   31.675 1.00 44.00 ? 145 GLU   A O   1 
ATOM   1076 C  CB  . GLU   A 1 139 ? 7.687  3.690   34.426 1.00 44.02 ? 145 GLU   A CB  1 
ATOM   1077 C  CG  . GLU   A 1 139 ? 8.385  5.024   34.246 1.00 49.74 ? 145 GLU   A CG  1 
ATOM   1078 C  CD  . GLU   A 1 139 ? 9.409  5.343   35.318 1.00 56.95 ? 145 GLU   A CD  1 
ATOM   1079 O  OE1 . GLU   A 1 139 ? 9.369  6.472   35.860 1.00 57.63 ? 145 GLU   A OE1 1 
ATOM   1080 O  OE2 . GLU   A 1 139 ? 10.265 4.472   35.602 1.00 59.64 ? 145 GLU   A OE2 1 
ATOM   1081 N  N   . SER   B 1 1   ? 19.767 -24.605 23.909 1.00 27.24 ? 7   SER   C N   1 
ATOM   1082 C  CA  . SER   B 1 1   ? 20.878 -24.456 22.948 1.00 27.74 ? 7   SER   C CA  1 
ATOM   1083 C  C   . SER   B 1 1   ? 20.899 -25.600 21.914 1.00 26.67 ? 7   SER   C C   1 
ATOM   1084 O  O   . SER   B 1 1   ? 20.226 -26.623 22.123 1.00 27.26 ? 7   SER   C O   1 
ATOM   1085 C  CB  . SER   B 1 1   ? 22.213 -24.417 23.693 1.00 30.53 ? 7   SER   C CB  1 
ATOM   1086 O  OG  . SER   B 1 1   ? 22.425 -25.659 24.353 1.00 35.02 ? 7   SER   C OG  1 
ATOM   1087 N  N   . GLY   B 1 2   ? 21.650 -25.422 20.814 1.00 24.16 ? 8   GLY   C N   1 
ATOM   1088 C  CA  . GLY   B 1 2   ? 21.790 -26.439 19.780 1.00 22.80 ? 8   GLY   C CA  1 
ATOM   1089 C  C   . GLY   B 1 2   ? 22.102 -25.900 18.396 1.00 20.95 ? 8   GLY   C C   1 
ATOM   1090 O  O   . GLY   B 1 2   ? 21.782 -24.750 18.083 1.00 21.13 ? 8   GLY   C O   1 
ATOM   1091 N  N   . ALA   B 1 3   ? 22.735 -26.713 17.557 1.00 19.36 ? 9   ALA   C N   1 
ATOM   1092 C  CA  . ALA   B 1 3   ? 23.099 -26.300 16.199 1.00 19.17 ? 9   ALA   C CA  1 
ATOM   1093 C  C   . ALA   B 1 3   ? 23.022 -27.466 15.218 1.00 18.87 ? 9   ALA   C C   1 
ATOM   1094 O  O   . ALA   B 1 3   ? 23.129 -28.647 15.610 1.00 20.28 ? 9   ALA   C O   1 
ATOM   1095 C  CB  . ALA   B 1 3   ? 24.518 -25.729 16.175 1.00 20.12 ? 9   ALA   C CB  1 
ATOM   1096 N  N   . ILE   B 1 4   ? 22.886 -27.136 13.924 1.00 17.74 ? 10  ILE   C N   1 
ATOM   1097 C  CA  . ILE   B 1 4   ? 22.954 -28.084 12.824 1.00 16.72 ? 10  ILE   C CA  1 
ATOM   1098 C  C   . ILE   B 1 4   ? 24.309 -27.869 12.138 1.00 18.13 ? 10  ILE   C C   1 
ATOM   1099 O  O   . ILE   B 1 4   ? 24.668 -26.744 11.822 1.00 18.37 ? 10  ILE   C O   1 
ATOM   1100 C  CB  . ILE   B 1 4   ? 21.802 -27.836 11.825 1.00 16.00 ? 10  ILE   C CB  1 
ATOM   1101 C  CG1 . ILE   B 1 4   ? 20.438 -27.922 12.497 1.00 16.84 ? 10  ILE   C CG1 1 
ATOM   1102 C  CG2 . ILE   B 1 4   ? 21.924 -28.793 10.651 1.00 16.24 ? 10  ILE   C CG2 1 
ATOM   1103 C  CD1 . ILE   B 1 4   ? 19.360 -27.255 11.609 1.00 18.55 ? 10  ILE   C CD1 1 
ATOM   1104 N  N   . TYR   B 1 5   ? 25.089 -28.951 11.903 1.00 18.94 ? 11  TYR   C N   1 
ATOM   1105 C  CA  . TYR   B 1 5   ? 26.374 -28.849 11.232 1.00 19.32 ? 11  TYR   C CA  1 
ATOM   1106 C  C   . TYR   B 1 5   ? 26.267 -29.592 9.916  1.00 20.63 ? 11  TYR   C C   1 
ATOM   1107 O  O   . TYR   B 1 5   ? 26.094 -30.811 9.916  1.00 21.56 ? 11  TYR   C O   1 
ATOM   1108 C  CB  . TYR   B 1 5   ? 27.483 -29.490 12.110 1.00 19.69 ? 11  TYR   C CB  1 
ATOM   1109 C  CG  . TYR   B 1 5   ? 27.724 -28.695 13.384 1.00 20.72 ? 11  TYR   C CG  1 
ATOM   1110 C  CD1 . TYR   B 1 5   ? 28.621 -27.640 13.407 1.00 22.49 ? 11  TYR   C CD1 1 
ATOM   1111 C  CD2 . TYR   B 1 5   ? 27.031 -28.980 14.549 1.00 22.92 ? 11  TYR   C CD2 1 
ATOM   1112 C  CE1 . TYR   B 1 5   ? 28.839 -26.895 14.574 1.00 24.46 ? 11  TYR   C CE1 1 
ATOM   1113 C  CE2 . TYR   B 1 5   ? 27.227 -28.237 15.713 1.00 24.24 ? 11  TYR   C CE2 1 
ATOM   1114 C  CZ  . TYR   B 1 5   ? 28.126 -27.191 15.721 1.00 26.06 ? 11  TYR   C CZ  1 
ATOM   1115 O  OH  . TYR   B 1 5   ? 28.261 -26.445 16.875 1.00 30.07 ? 11  TYR   C OH  1 
ATOM   1116 N  N   . VAL   B 1 6   ? 26.328 -28.878 8.792  1.00 20.63 ? 12  VAL   C N   1 
ATOM   1117 C  CA  . VAL   B 1 6   ? 26.181 -29.471 7.465  1.00 22.09 ? 12  VAL   C CA  1 
ATOM   1118 C  C   . VAL   B 1 6   ? 27.238 -28.869 6.537  1.00 23.66 ? 12  VAL   C C   1 
ATOM   1119 O  O   . VAL   B 1 6   ? 27.357 -27.658 6.450  1.00 23.91 ? 12  VAL   C O   1 
ATOM   1120 C  CB  . VAL   B 1 6   ? 24.724 -29.278 6.928  1.00 23.29 ? 12  VAL   C CB  1 
ATOM   1121 C  CG1 . VAL   B 1 6   ? 24.274 -27.824 7.039  1.00 23.86 ? 12  VAL   C CG1 1 
ATOM   1122 C  CG2 . VAL   B 1 6   ? 24.590 -29.804 5.506  1.00 24.43 ? 12  VAL   C CG2 1 
ATOM   1123 N  N   . GLY   B 1 7   ? 28.106 -29.696 5.934  1.00 24.88 ? 13  GLY   C N   1 
ATOM   1124 C  CA  . GLY   B 1 7   ? 29.179 -29.180 5.080  1.00 26.04 ? 13  GLY   C CA  1 
ATOM   1125 C  C   . GLY   B 1 7   ? 30.092 -28.263 5.879  1.00 26.46 ? 13  GLY   C C   1 
ATOM   1126 O  O   . GLY   B 1 7   ? 30.423 -28.594 7.021  1.00 26.54 ? 13  GLY   C O   1 
ATOM   1127 N  N   . ASN   B 1 8   ? 30.384 -27.058 5.371  1.00 26.27 ? 14  ASN   C N   1 
ATOM   1128 C  CA  . ASN   B 1 8   ? 31.176 -26.101 6.149  1.00 26.07 ? 14  ASN   C CA  1 
ATOM   1129 C  C   . ASN   B 1 8   ? 30.292 -25.006 6.748  1.00 23.53 ? 14  ASN   C C   1 
ATOM   1130 O  O   . ASN   B 1 8   ? 30.731 -23.859 6.898  1.00 23.86 ? 14  ASN   C O   1 
ATOM   1131 C  CB  . ASN   B 1 8   ? 32.293 -25.488 5.331  1.00 29.22 ? 14  ASN   C CB  1 
ATOM   1132 C  CG  . ASN   B 1 8   ? 33.324 -26.503 4.924  1.00 36.72 ? 14  ASN   C CG  1 
ATOM   1133 O  OD1 . ASN   B 1 8   ? 34.019 -27.094 5.766  1.00 38.99 ? 14  ASN   C OD1 1 
ATOM   1134 N  ND2 . ASN   B 1 8   ? 33.417 -26.746 3.626  1.00 38.82 ? 14  ASN   C ND2 1 
ATOM   1135 N  N   . TYR   B 1 9   ? 29.067 -25.380 7.147  1.00 21.73 ? 15  TYR   C N   1 
ATOM   1136 C  CA  . TYR   B 1 9   ? 28.119 -24.440 7.748  1.00 19.95 ? 15  TYR   C CA  1 
ATOM   1137 C  C   . TYR   B 1 9   ? 27.660 -24.927 9.118  1.00 19.19 ? 15  TYR   C C   1 
ATOM   1138 O  O   . TYR   B 1 9   ? 27.525 -26.139 9.372  1.00 19.42 ? 15  TYR   C O   1 
ATOM   1139 C  CB  . TYR   B 1 9   ? 26.864 -24.312 6.858  1.00 20.09 ? 15  TYR   C CB  1 
ATOM   1140 C  CG  . TYR   B 1 9   ? 27.121 -23.746 5.481  1.00 21.13 ? 15  TYR   C CG  1 
ATOM   1141 C  CD1 . TYR   B 1 9   ? 27.796 -22.544 5.315  1.00 23.01 ? 15  TYR   C CD1 1 
ATOM   1142 C  CD2 . TYR   B 1 9   ? 26.719 -24.433 4.339  1.00 22.49 ? 15  TYR   C CD2 1 
ATOM   1143 C  CE1 . TYR   B 1 9   ? 28.026 -22.018 4.050  1.00 24.45 ? 15  TYR   C CE1 1 
ATOM   1144 C  CE2 . TYR   B 1 9   ? 26.931 -23.909 3.067  1.00 24.35 ? 15  TYR   C CE2 1 
ATOM   1145 C  CZ  . TYR   B 1 9   ? 27.599 -22.707 2.928  1.00 26.19 ? 15  TYR   C CZ  1 
ATOM   1146 O  OH  . TYR   B 1 9   ? 27.792 -22.162 1.675  1.00 29.43 ? 15  TYR   C OH  1 
ATOM   1147 N  N   . ARG   B 1 10  ? 27.343 -23.939 9.977  1.00 17.28 ? 16  ARG   C N   1 
ATOM   1148 C  CA  . ARG   B 1 10  ? 26.753 -24.155 11.292 1.00 17.20 ? 16  ARG   C CA  1 
ATOM   1149 C  C   . ARG   B 1 10  ? 25.461 -23.324 11.317 1.00 16.94 ? 16  ARG   C C   1 
ATOM   1150 O  O   . ARG   B 1 10  ? 25.527 -22.127 11.041 1.00 18.25 ? 16  ARG   C O   1 
ATOM   1151 C  CB  . ARG   B 1 10  ? 27.730 -23.710 12.395 1.00 18.39 ? 16  ARG   C CB  1 
ATOM   1152 C  CG  . ARG   B 1 10  ? 27.128 -23.499 13.781 1.00 17.98 ? 16  ARG   C CG  1 
ATOM   1153 C  CD  . ARG   B 1 10  ? 28.211 -23.196 14.822 1.00 20.29 ? 16  ARG   C CD  1 
ATOM   1154 N  NE  . ARG   B 1 10  ? 27.789 -22.200 15.806 1.00 22.34 ? 16  ARG   C NE  1 
ATOM   1155 C  CZ  . ARG   B 1 10  ? 27.488 -22.463 17.074 1.00 26.18 ? 16  ARG   C CZ  1 
ATOM   1156 N  NH1 . ARG   B 1 10  ? 27.498 -23.714 17.520 1.00 25.46 ? 16  ARG   C NH1 1 
ATOM   1157 N  NH2 . ARG   B 1 10  ? 27.116 -21.479 17.894 1.00 25.95 ? 16  ARG   C NH2 1 
ATOM   1158 N  N   . VAL   B 1 11  ? 24.300 -23.964 11.558 1.00 16.08 ? 17  VAL   C N   1 
ATOM   1159 C  CA  . VAL   B 1 11  ? 22.994 -23.275 11.610 1.00 15.32 ? 17  VAL   C CA  1 
ATOM   1160 C  C   . VAL   B 1 11  ? 22.556 -23.169 13.065 1.00 15.86 ? 17  VAL   C C   1 
ATOM   1161 O  O   . VAL   B 1 11  ? 22.473 -24.201 13.759 1.00 16.66 ? 17  VAL   C O   1 
ATOM   1162 C  CB  . VAL   B 1 11  ? 21.896 -24.033 10.813 1.00 17.00 ? 17  VAL   C CB  1 
ATOM   1163 C  CG1 . VAL   B 1 11  ? 20.642 -23.165 10.720 1.00 17.35 ? 17  VAL   C CG1 1 
ATOM   1164 C  CG2 . VAL   B 1 11  ? 22.396 -24.434 9.431  1.00 18.19 ? 17  VAL   C CG2 1 
ATOM   1165 N  N   . VAL   B 1 12  ? 22.294 -21.945 13.546 1.00 14.20 ? 18  VAL   C N   1 
ATOM   1166 C  CA  . VAL   B 1 12  ? 21.883 -21.754 14.944 1.00 14.98 ? 18  VAL   C CA  1 
ATOM   1167 C  C   . VAL   B 1 12  ? 20.649 -20.826 14.990 1.00 14.41 ? 18  VAL   C C   1 
ATOM   1168 O  O   . VAL   B 1 12  ? 20.371 -20.080 14.030 1.00 14.34 ? 18  VAL   C O   1 
ATOM   1169 C  CB  . VAL   B 1 12  ? 23.054 -21.128 15.789 1.00 16.61 ? 18  VAL   C CB  1 
ATOM   1170 C  CG1 . VAL   B 1 12  ? 24.185 -22.131 15.943 1.00 19.60 ? 18  VAL   C CG1 1 
ATOM   1171 C  CG2 . VAL   B 1 12  ? 23.555 -19.816 15.167 1.00 16.08 ? 18  VAL   C CG2 1 
ATOM   1172 N  N   . ASN   B 1 13  ? 20.006 -20.737 16.166 1.00 14.41 ? 19  ASN   C N   1 
ATOM   1173 C  CA  . ASN   B 1 13  ? 19.006 -19.687 16.397 1.00 14.09 ? 19  ASN   C CA  1 
ATOM   1174 C  C   . ASN   B 1 13  ? 19.757 -18.343 16.335 1.00 14.90 ? 19  ASN   C C   1 
ATOM   1175 O  O   . ASN   B 1 13  ? 20.793 -18.182 17.015 1.00 15.54 ? 19  ASN   C O   1 
ATOM   1176 C  CB  . ASN   B 1 13  ? 18.386 -19.812 17.792 1.00 14.13 ? 19  ASN   C CB  1 
ATOM   1177 C  CG  . ASN   B 1 13  ? 17.510 -21.034 17.931 1.00 16.20 ? 19  ASN   C CG  1 
ATOM   1178 O  OD1 . ASN   B 1 13  ? 17.978 -22.096 18.377 1.00 16.16 ? 19  ASN   C OD1 1 
ATOM   1179 N  ND2 . ASN   B 1 13  ? 16.236 -20.896 17.554 1.00 15.46 ? 19  ASN   C ND2 1 
ATOM   1180 N  N   . ARG   B 1 14  ? 19.247 -17.391 15.542 1.00 14.00 ? 20  ARG   C N   1 
ATOM   1181 C  CA  . ARG   B 1 14  ? 19.946 -16.087 15.438 1.00 13.99 ? 20  ARG   C CA  1 
ATOM   1182 C  C   . ARG   B 1 14  ? 20.120 -15.421 16.824 1.00 14.85 ? 20  ARG   C C   1 
ATOM   1183 O  O   . ARG   B 1 14  ? 21.186 -14.832 17.103 1.00 15.19 ? 20  ARG   C O   1 
ATOM   1184 C  CB  . ARG   B 1 14  ? 19.150 -15.178 14.494 1.00 14.84 ? 20  ARG   C CB  1 
ATOM   1185 C  CG  . ARG   B 1 14  ? 19.902 -13.882 14.085 1.00 16.86 ? 20  ARG   C CG  1 
ATOM   1186 C  CD  . ARG   B 1 14  ? 18.912 -12.988 13.330 1.00 16.95 ? 20  ARG   C CD  1 
ATOM   1187 N  NE  . ARG   B 1 14  ? 19.478 -11.735 12.786 1.00 16.20 ? 20  ARG   C NE  1 
ATOM   1188 C  CZ  . ARG   B 1 14  ? 19.575 -10.606 13.469 1.00 18.22 ? 20  ARG   C CZ  1 
ATOM   1189 N  NH1 . ARG   B 1 14  ? 19.262 -10.572 14.760 1.00 18.24 ? 20  ARG   C NH1 1 
ATOM   1190 N  NH2 . ARG   B 1 14  ? 20.027 -9.497  12.877 1.00 19.18 ? 20  ARG   C NH2 1 
ATOM   1191 N  N   . HIS   B 1 15  ? 19.085 -15.549 17.700 1.00 14.55 ? 21  HIS   C N   1 
ATOM   1192 C  CA  . HIS   B 1 15  ? 19.178 -14.908 19.018 1.00 15.67 ? 21  HIS   C CA  1 
ATOM   1193 C  C   . HIS   B 1 15  ? 20.200 -15.552 19.945 1.00 16.24 ? 21  HIS   C C   1 
ATOM   1194 O  O   . HIS   B 1 15  ? 20.555 -14.944 20.965 1.00 17.83 ? 21  HIS   C O   1 
ATOM   1195 C  CB  . HIS   B 1 15  ? 17.802 -14.789 19.689 1.00 15.54 ? 21  HIS   C CB  1 
ATOM   1196 C  CG  . HIS   B 1 15  ? 17.235 -16.052 20.255 1.00 16.07 ? 21  HIS   C CG  1 
ATOM   1197 N  ND1 . HIS   B 1 15  ? 16.545 -16.962 19.461 1.00 16.22 ? 21  HIS   C ND1 1 
ATOM   1198 C  CD2 . HIS   B 1 15  ? 17.197 -16.469 21.546 1.00 17.25 ? 21  HIS   C CD2 1 
ATOM   1199 C  CE1 . HIS   B 1 15  ? 16.150 -17.941 20.287 1.00 18.01 ? 21  HIS   C CE1 1 
ATOM   1200 N  NE2 . HIS   B 1 15  ? 16.530 -17.691 21.550 1.00 18.32 ? 21  HIS   C NE2 1 
ATOM   1201 N  N   . LEU   B 1 16  ? 20.683 -16.757 19.606 1.00 15.20 ? 22  LEU   C N   1 
ATOM   1202 C  CA  . LEU   B 1 16  ? 21.701 -17.419 20.434 1.00 15.67 ? 22  LEU   C CA  1 
ATOM   1203 C  C   . LEU   B 1 16  ? 23.093 -17.414 19.759 1.00 17.87 ? 22  LEU   C C   1 
ATOM   1204 O  O   . LEU   B 1 16  ? 24.027 -18.028 20.295 1.00 18.77 ? 22  LEU   C O   1 
ATOM   1205 C  CB  . LEU   B 1 16  ? 21.260 -18.875 20.743 1.00 16.65 ? 22  LEU   C CB  1 
ATOM   1206 C  CG  . LEU   B 1 16  ? 19.926 -18.988 21.531 1.00 18.13 ? 22  LEU   C CG  1 
ATOM   1207 C  CD1 . LEU   B 1 16  ? 19.581 -20.461 21.780 1.00 19.21 ? 22  LEU   C CD1 1 
ATOM   1208 C  CD2 . LEU   B 1 16  ? 20.005 -18.214 22.891 1.00 19.88 ? 22  LEU   C CD2 1 
ATOM   1209 N  N   . ALA   B 1 17  ? 23.236 -16.746 18.587 1.00 17.21 ? 23  ALA   C N   1 
ATOM   1210 C  CA  . ALA   B 1 17  ? 24.515 -16.746 17.876 1.00 17.95 ? 23  ALA   C CA  1 
ATOM   1211 C  C   . ALA   B 1 17  ? 25.590 -16.095 18.714 1.00 18.32 ? 23  ALA   C C   1 
ATOM   1212 O  O   . ALA   B 1 17  ? 25.316 -15.124 19.419 1.00 19.02 ? 23  ALA   C O   1 
ATOM   1213 C  CB  . ALA   B 1 17  ? 24.382 -15.991 16.562 1.00 17.74 ? 23  ALA   C CB  1 
ATOM   1214 N  N   . THR   B 1 18  ? 26.801 -16.657 18.667 1.00 18.01 ? 24  THR   C N   1 
ATOM   1215 C  CA  . THR   B 1 18  ? 27.924 -16.117 19.452 1.00 18.62 ? 24  THR   C CA  1 
ATOM   1216 C  C   . THR   B 1 18  ? 28.682 -15.018 18.693 1.00 18.68 ? 24  THR   C C   1 
ATOM   1217 O  O   . THR   B 1 18  ? 28.453 -14.821 17.498 1.00 18.83 ? 24  THR   C O   1 
ATOM   1218 C  CB  . THR   B 1 18  ? 28.883 -17.292 19.770 1.00 20.52 ? 24  THR   C CB  1 
ATOM   1219 O  OG1 . THR   B 1 18  ? 29.513 -17.699 18.554 1.00 21.93 ? 24  THR   C OG1 1 
ATOM   1220 C  CG2 . THR   B 1 18  ? 28.188 -18.471 20.411 1.00 21.43 ? 24  THR   C CG2 1 
ATOM   1221 N  N   . HIS   B 1 19  ? 29.683 -14.351 19.357 1.00 18.92 ? 25  HIS   C N   1 
ATOM   1222 C  CA  . HIS   B 1 19  ? 30.507 -13.385 18.632 1.00 20.37 ? 25  HIS   C CA  1 
ATOM   1223 C  C   . HIS   B 1 19  ? 31.234 -14.086 17.444 1.00 19.76 ? 25  HIS   C C   1 
ATOM   1224 O  O   . HIS   B 1 19  ? 31.405 -13.484 16.379 1.00 20.46 ? 25  HIS   C O   1 
ATOM   1225 C  CB  . HIS   B 1 19  ? 31.574 -12.788 19.577 1.00 24.16 ? 25  HIS   C CB  1 
ATOM   1226 C  CG  . HIS   B 1 19  ? 31.027 -11.963 20.709 1.00 32.69 ? 25  HIS   C CG  1 
ATOM   1227 N  ND1 . HIS   B 1 19  ? 30.300 -10.797 20.479 1.00 36.63 ? 25  HIS   C ND1 1 
ATOM   1228 C  CD2 . HIS   B 1 19  ? 31.195 -12.109 22.044 1.00 36.22 ? 25  HIS   C CD2 1 
ATOM   1229 C  CE1 . HIS   B 1 19  ? 30.032 -10.291 21.676 1.00 37.34 ? 25  HIS   C CE1 1 
ATOM   1230 N  NE2 . HIS   B 1 19  ? 30.532 -11.051 22.650 1.00 38.27 ? 25  HIS   C NE2 1 
ATOM   1231 N  N   . ASN   B 1 20  ? 31.621 -15.364 17.628 1.00 19.77 ? 26  ASN   C N   1 
ATOM   1232 C  CA  . ASN   B 1 20  ? 32.298 -16.089 16.550 1.00 19.84 ? 26  ASN   C CA  1 
ATOM   1233 C  C   . ASN   B 1 20  ? 31.377 -16.370 15.385 1.00 19.45 ? 26  ASN   C C   1 
ATOM   1234 O  O   . ASN   B 1 20  ? 31.809 -16.314 14.240 1.00 20.06 ? 26  ASN   C O   1 
ATOM   1235 C  CB  . ASN   B 1 20  ? 32.891 -17.381 17.047 1.00 22.95 ? 26  ASN   C CB  1 
ATOM   1236 C  CG  . ASN   B 1 20  ? 34.124 -17.127 17.818 1.00 29.93 ? 26  ASN   C CG  1 
ATOM   1237 O  OD1 . ASN   B 1 20  ? 34.953 -16.304 17.408 1.00 31.97 ? 26  ASN   C OD1 1 
ATOM   1238 N  ND2 . ASN   B 1 20  ? 34.236 -17.805 18.961 1.00 32.51 ? 26  ASN   C ND2 1 
ATOM   1239 N  N   . ASP   B 1 21  ? 30.089 -16.669 15.658 1.00 18.79 ? 27  ASP   C N   1 
ATOM   1240 C  CA  . ASP   B 1 21  ? 29.136 -16.892 14.564 1.00 18.83 ? 27  ASP   C CA  1 
ATOM   1241 C  C   . ASP   B 1 21  ? 29.002 -15.604 13.721 1.00 19.76 ? 27  ASP   C C   1 
ATOM   1242 O  O   . ASP   B 1 21  ? 29.031 -15.646 12.499 1.00 20.97 ? 27  ASP   C O   1 
ATOM   1243 C  CB  . ASP   B 1 21  ? 27.747 -17.234 15.149 1.00 18.57 ? 27  ASP   C CB  1 
ATOM   1244 C  CG  . ASP   B 1 21  ? 27.639 -18.658 15.656 1.00 20.32 ? 27  ASP   C CG  1 
ATOM   1245 O  OD1 . ASP   B 1 21  ? 28.138 -19.563 14.971 1.00 22.47 ? 27  ASP   C OD1 1 
ATOM   1246 O  OD2 . ASP   B 1 21  ? 27.058 -18.855 16.767 1.00 20.06 ? 27  ASP   C OD2 1 
ATOM   1247 N  N   . TRP   B 1 22  ? 28.902 -14.443 14.395 1.00 18.95 ? 28  TRP   C N   1 
ATOM   1248 C  CA  . TRP   B 1 22  ? 28.757 -13.172 13.693 1.00 19.39 ? 28  TRP   C CA  1 
ATOM   1249 C  C   . TRP   B 1 22  ? 30.041 -12.766 12.941 1.00 20.39 ? 28  TRP   C C   1 
ATOM   1250 O  O   . TRP   B 1 22  ? 29.954 -12.187 11.852 1.00 21.52 ? 28  TRP   C O   1 
ATOM   1251 C  CB  . TRP   B 1 22  ? 28.341 -12.071 14.679 1.00 19.10 ? 28  TRP   C CB  1 
ATOM   1252 C  CG  . TRP   B 1 22  ? 26.853 -12.042 14.917 1.00 17.97 ? 28  TRP   C CG  1 
ATOM   1253 C  CD1 . TRP   B 1 22  ? 26.184 -12.511 16.006 1.00 18.47 ? 28  TRP   C CD1 1 
ATOM   1254 C  CD2 . TRP   B 1 22  ? 25.864 -11.481 14.038 1.00 17.16 ? 28  TRP   C CD2 1 
ATOM   1255 N  NE1 . TRP   B 1 22  ? 24.827 -12.278 15.860 1.00 18.94 ? 28  TRP   C NE1 1 
ATOM   1256 C  CE2 . TRP   B 1 22  ? 24.609 -11.647 14.659 1.00 17.78 ? 28  TRP   C CE2 1 
ATOM   1257 C  CE3 . TRP   B 1 22  ? 25.919 -10.862 12.779 1.00 18.41 ? 28  TRP   C CE3 1 
ATOM   1258 C  CZ2 . TRP   B 1 22  ? 23.419 -11.203 14.073 1.00 17.75 ? 28  TRP   C CZ2 1 
ATOM   1259 C  CZ3 . TRP   B 1 22  ? 24.739 -10.413 12.197 1.00 18.59 ? 28  TRP   C CZ3 1 
ATOM   1260 C  CH2 . TRP   B 1 22  ? 23.509 -10.610 12.830 1.00 17.79 ? 28  TRP   C CH2 1 
ATOM   1261 N  N   . ALA   B 1 23  ? 31.205 -13.149 13.468 1.00 20.15 ? 29  ALA   C N   1 
ATOM   1262 C  CA  . ALA   B 1 23  ? 32.466 -12.831 12.796 1.00 21.78 ? 29  ALA   C CA  1 
ATOM   1263 C  C   . ALA   B 1 23  ? 32.692 -13.722 11.547 1.00 23.08 ? 29  ALA   C C   1 
ATOM   1264 O  O   . ALA   B 1 23  ? 33.548 -13.415 10.697 1.00 24.96 ? 29  ALA   C O   1 
ATOM   1265 C  CB  . ALA   B 1 23  ? 33.608 -13.019 13.776 1.00 21.11 ? 29  ALA   C CB  1 
ATOM   1266 N  N   . ASN   B 1 24  ? 32.011 -14.885 11.491 1.00 21.08 ? 30  ASN   C N   1 
ATOM   1267 C  CA  . ASN   B 1 24  ? 32.126 -15.823 10.370 1.00 20.41 ? 30  ASN   C CA  1 
ATOM   1268 C  C   . ASN   B 1 24  ? 30.750 -15.976 9.698  1.00 20.47 ? 30  ASN   C C   1 
ATOM   1269 O  O   . ASN   B 1 24  ? 30.398 -17.043 9.236  1.00 20.27 ? 30  ASN   C O   1 
ATOM   1270 C  CB  . ASN   B 1 24  ? 32.631 -17.177 10.892 1.00 20.84 ? 30  ASN   C CB  1 
ATOM   1271 C  CG  . ASN   B 1 24  ? 34.055 -17.041 11.375 1.00 24.72 ? 30  ASN   C CG  1 
ATOM   1272 O  OD1 . ASN   B 1 24  ? 35.010 -17.007 10.582 1.00 25.46 ? 30  ASN   C OD1 1 
ATOM   1273 N  ND2 . ASN   B 1 24  ? 34.230 -16.871 12.691 1.00 23.59 ? 30  ASN   C ND2 1 
ATOM   1274 N  N   . LEU   B 1 25  ? 30.014 -14.878 9.614  1.00 20.36 ? 31  LEU   C N   1 
ATOM   1275 C  CA  . LEU   B 1 25  ? 28.666 -14.868 9.071  1.00 19.91 ? 31  LEU   C CA  1 
ATOM   1276 C  C   . LEU   B 1 25  ? 28.579 -15.238 7.610  1.00 20.73 ? 31  LEU   C C   1 
ATOM   1277 O  O   . LEU   B 1 25  ? 29.318 -14.692 6.789  1.00 22.17 ? 31  LEU   C O   1 
ATOM   1278 C  CB  . LEU   B 1 25  ? 28.091 -13.457 9.280  1.00 19.94 ? 31  LEU   C CB  1 
ATOM   1279 C  CG  . LEU   B 1 25  ? 26.661 -13.233 8.785  1.00 21.11 ? 31  LEU   C CG  1 
ATOM   1280 C  CD1 . LEU   B 1 25  ? 25.660 -14.116 9.589  1.00 21.49 ? 31  LEU   C CD1 1 
ATOM   1281 C  CD2 . LEU   B 1 25  ? 26.273 -11.781 8.962  1.00 22.31 ? 31  LEU   C CD2 1 
ATOM   1282 N  N   . VAL   B 1 26  ? 27.639 -16.141 7.260  1.00 19.39 ? 32  VAL   C N   1 
ATOM   1283 C  CA  . VAL   B 1 26  ? 27.324 -16.500 5.886  1.00 20.26 ? 32  VAL   C CA  1 
ATOM   1284 C  C   . VAL   B 1 26  ? 25.975 -15.852 5.496  1.00 21.01 ? 32  VAL   C C   1 
ATOM   1285 O  O   . VAL   B 1 26  ? 25.853 -15.206 4.442  1.00 23.03 ? 32  VAL   C O   1 
ATOM   1286 C  CB  . VAL   B 1 26  ? 27.271 -18.028 5.705  1.00 21.64 ? 32  VAL   C CB  1 
ATOM   1287 C  CG1 . VAL   B 1 26  ? 26.732 -18.400 4.309  1.00 21.48 ? 32  VAL   C CG1 1 
ATOM   1288 C  CG2 . VAL   B 1 26  ? 28.669 -18.619 5.942  1.00 22.14 ? 32  VAL   C CG2 1 
ATOM   1289 N  N   . TRP   B 1 27  ? 24.961 -16.005 6.368  1.00 18.94 ? 33  TRP   C N   1 
ATOM   1290 C  CA  . TRP   B 1 27  ? 23.624 -15.510 6.102  1.00 18.49 ? 33  TRP   C CA  1 
ATOM   1291 C  C   . TRP   B 1 27  ? 22.863 -15.431 7.416  1.00 18.34 ? 33  TRP   C C   1 
ATOM   1292 O  O   . TRP   B 1 27  ? 23.041 -16.285 8.291  1.00 18.07 ? 33  TRP   C O   1 
ATOM   1293 C  CB  . TRP   B 1 27  ? 22.907 -16.499 5.135  1.00 19.35 ? 33  TRP   C CB  1 
ATOM   1294 C  CG  . TRP   B 1 27  ? 21.425 -16.270 4.955  1.00 20.09 ? 33  TRP   C CG  1 
ATOM   1295 C  CD1 . TRP   B 1 27  ? 20.815 -15.408 4.086  1.00 22.60 ? 33  TRP   C CD1 1 
ATOM   1296 C  CD2 . TRP   B 1 27  ? 20.366 -16.999 5.607  1.00 19.01 ? 33  TRP   C CD2 1 
ATOM   1297 N  NE1 . TRP   B 1 27  ? 19.435 -15.494 4.231  1.00 23.13 ? 33  TRP   C NE1 1 
ATOM   1298 C  CE2 . TRP   B 1 27  ? 19.139 -16.468 5.151  1.00 20.57 ? 33  TRP   C CE2 1 
ATOM   1299 C  CE3 . TRP   B 1 27  ? 20.341 -17.994 6.599  1.00 19.15 ? 33  TRP   C CE3 1 
ATOM   1300 C  CZ2 . TRP   B 1 27  ? 17.895 -16.987 5.572  1.00 20.04 ? 33  TRP   C CZ2 1 
ATOM   1301 C  CZ3 . TRP   B 1 27  ? 19.113 -18.480 7.032  1.00 20.00 ? 33  TRP   C CZ3 1 
ATOM   1302 C  CH2 . TRP   B 1 27  ? 17.911 -17.975 6.526  1.00 19.79 ? 33  TRP   C CH2 1 
ATOM   1303 N  N   . GLU   B 1 28  ? 21.998 -14.441 7.546  1.00 18.11 ? 34  GLU   C N   1 
ATOM   1304 C  CA  . GLU   B 1 28  ? 21.105 -14.360 8.707  1.00 17.92 ? 34  GLU   C CA  1 
ATOM   1305 C  C   . GLU   B 1 28  ? 19.770 -13.742 8.307  1.00 17.94 ? 34  GLU   C C   1 
ATOM   1306 O  O   . GLU   B 1 28  ? 19.706 -12.949 7.355  1.00 18.59 ? 34  GLU   C O   1 
ATOM   1307 C  CB  . GLU   B 1 28  ? 21.725 -13.650 9.927  1.00 19.65 ? 34  GLU   C CB  1 
ATOM   1308 C  CG  . GLU   B 1 28  ? 22.306 -12.270 9.648  1.00 20.72 ? 34  GLU   C CG  1 
ATOM   1309 C  CD  . GLU   B 1 28  ? 21.310 -11.140 9.502  1.00 24.69 ? 34  GLU   C CD  1 
ATOM   1310 O  OE1 . GLU   B 1 28  ? 21.599 -10.214 8.711  1.00 28.96 ? 34  GLU   C OE1 1 
ATOM   1311 O  OE2 . GLU   B 1 28  ? 20.223 -11.189 10.123 1.00 20.39 ? 34  GLU   C OE2 1 
ATOM   1312 N  N   . ASP   B 1 29  ? 18.692 -14.114 9.018  1.00 16.45 ? 35  ASP   C N   1 
ATOM   1313 C  CA  . ASP   B 1 29  ? 17.388 -13.536 8.731  1.00 15.62 ? 35  ASP   C CA  1 
ATOM   1314 C  C   . ASP   B 1 29  ? 16.655 -13.393 10.075 1.00 15.92 ? 35  ASP   C C   1 
ATOM   1315 O  O   . ASP   B 1 29  ? 16.243 -14.385 10.685 1.00 16.33 ? 35  ASP   C O   1 
ATOM   1316 C  CB  . ASP   B 1 29  ? 16.614 -14.436 7.741  1.00 16.99 ? 35  ASP   C CB  1 
ATOM   1317 C  CG  . ASP   B 1 29  ? 15.283 -13.863 7.283  1.00 23.01 ? 35  ASP   C CG  1 
ATOM   1318 O  OD1 . ASP   B 1 29  ? 14.706 -13.044 8.012  1.00 25.13 ? 35  ASP   C OD1 1 
ATOM   1319 O  OD2 . ASP   B 1 29  ? 14.815 -14.247 6.180  1.00 23.87 ? 35  ASP   C OD2 1 
ATOM   1320 N  N   . SER   B 1 30  ? 16.514 -12.123 10.553 1.00 15.60 ? 36  SER   C N   1 
ATOM   1321 C  CA  A SER   B 1 30  ? 15.843 -11.834 11.807 0.50 16.16 ? 36  SER   C CA  1 
ATOM   1322 C  CA  B SER   B 1 30  ? 15.839 -11.862 11.821 0.50 15.94 ? 36  SER   C CA  1 
ATOM   1323 C  C   . SER   B 1 30  ? 14.387 -12.317 11.783 1.00 16.94 ? 36  SER   C C   1 
ATOM   1324 O  O   . SER   B 1 30  ? 13.885 -12.782 12.807 1.00 18.13 ? 36  SER   C O   1 
ATOM   1325 C  CB  A SER   B 1 30  ? 15.927 -10.336 12.097 0.50 18.67 ? 36  SER   C CB  1 
ATOM   1326 C  CB  B SER   B 1 30  ? 15.925 -10.382 12.195 0.50 17.76 ? 36  SER   C CB  1 
ATOM   1327 O  OG  A SER   B 1 30  ? 15.192 -9.981  13.251 0.50 20.94 ? 36  SER   C OG  1 
ATOM   1328 O  OG  B SER   B 1 30  ? 15.179 -9.585  11.288 0.50 18.76 ? 36  SER   C OG  1 
ATOM   1329 N  N   . SER   B 1 31  ? 13.722 -12.220 10.609 1.00 15.41 ? 37  SER   C N   1 
ATOM   1330 C  CA  . SER   B 1 31  ? 12.323 -12.652 10.540 1.00 15.94 ? 37  SER   C CA  1 
ATOM   1331 C  C   . SER   B 1 31  ? 12.178 -14.163 10.699 1.00 16.32 ? 37  SER   C C   1 
ATOM   1332 O  O   . SER   B 1 31  ? 11.068 -14.595 10.991 1.00 17.98 ? 37  SER   C O   1 
ATOM   1333 C  CB  . SER   B 1 31  ? 11.650 -12.193 9.252  1.00 18.83 ? 37  SER   C CB  1 
ATOM   1334 O  OG  . SER   B 1 31  ? 12.027 -13.004 8.150  1.00 24.18 ? 37  SER   C OG  1 
ATOM   1335 N  N   . ARG   B 1 32  ? 13.240 -14.934 10.535 1.00 14.55 ? 38  ARG   C N   1 
ATOM   1336 C  CA  . ARG   B 1 32  ? 13.167 -16.411 10.713 1.00 14.29 ? 38  ARG   C CA  1 
ATOM   1337 C  C   . ARG   B 1 32  ? 13.842 -16.887 11.994 1.00 14.51 ? 38  ARG   C C   1 
ATOM   1338 O  O   . ARG   B 1 32  ? 13.801 -18.101 12.281 1.00 14.14 ? 38  ARG   C O   1 
ATOM   1339 C  CB  . ARG   B 1 32  ? 13.877 -17.107 9.527  1.00 14.63 ? 38  ARG   C CB  1 
ATOM   1340 C  CG  . ARG   B 1 32  ? 13.137 -16.856 8.207  1.00 14.09 ? 38  ARG   C CG  1 
ATOM   1341 C  CD  . ARG   B 1 32  ? 13.824 -17.503 6.994  1.00 14.01 ? 38  ARG   C CD  1 
ATOM   1342 N  NE  . ARG   B 1 32  ? 13.838 -18.968 7.085  1.00 13.71 ? 38  ARG   C NE  1 
ATOM   1343 C  CZ  . ARG   B 1 32  ? 13.902 -19.772 6.024  1.00 14.69 ? 38  ARG   C CZ  1 
ATOM   1344 N  NH1 . ARG   B 1 32  ? 13.992 -19.267 4.799  1.00 16.90 ? 38  ARG   C NH1 1 
ATOM   1345 N  NH2 . ARG   B 1 32  ? 13.868 -21.088 6.179  1.00 15.30 ? 38  ARG   C NH2 1 
ATOM   1346 N  N   . ASP   B 1 33  ? 14.537 -16.001 12.716 1.00 14.60 ? 39  ASP   C N   1 
ATOM   1347 C  CA  . ASP   B 1 33  ? 15.346 -16.399 13.871 1.00 13.80 ? 39  ASP   C CA  1 
ATOM   1348 C  C   . ASP   B 1 33  ? 16.436 -17.395 13.463 1.00 13.23 ? 39  ASP   C C   1 
ATOM   1349 O  O   . ASP   B 1 33  ? 16.793 -18.265 14.270 1.00 13.79 ? 39  ASP   C O   1 
ATOM   1350 C  CB  . ASP   B 1 33  ? 14.509 -16.962 15.069 1.00 15.07 ? 39  ASP   C CB  1 
ATOM   1351 C  CG  . ASP   B 1 33  ? 15.332 -17.245 16.340 1.00 15.10 ? 39  ASP   C CG  1 
ATOM   1352 O  OD1 . ASP   B 1 33  ? 16.247 -16.417 16.671 1.00 14.94 ? 39  ASP   C OD1 1 
ATOM   1353 O  OD2 . ASP   B 1 33  ? 15.094 -18.288 17.003 1.00 15.38 ? 39  ASP   C OD2 1 
ATOM   1354 N  N   . LEU   B 1 34  ? 17.031 -17.233 12.266 1.00 13.34 ? 40  LEU   C N   1 
ATOM   1355 C  CA  . LEU   B 1 34  ? 18.130 -18.111 11.844 1.00 13.96 ? 40  LEU   C CA  1 
ATOM   1356 C  C   . LEU   B 1 34  ? 19.404 -17.348 11.536 1.00 14.37 ? 40  LEU   C C   1 
ATOM   1357 O  O   . LEU   B 1 34  ? 19.357 -16.263 10.953 1.00 14.83 ? 40  LEU   C O   1 
ATOM   1358 C  CB  . LEU   B 1 34  ? 17.757 -18.894 10.572 1.00 14.09 ? 40  LEU   C CB  1 
ATOM   1359 C  CG  . LEU   B 1 34  ? 16.682 -19.980 10.729 1.00 15.94 ? 40  LEU   C CG  1 
ATOM   1360 C  CD1 . LEU   B 1 34  ? 16.510 -20.684 9.368  1.00 15.98 ? 40  LEU   C CD1 1 
ATOM   1361 C  CD2 . LEU   B 1 34  ? 17.137 -21.063 11.743 1.00 16.26 ? 40  LEU   C CD2 1 
ATOM   1362 N  N   . LEU   B 1 35  ? 20.542 -18.007 11.788 1.00 13.76 ? 41  LEU   C N   1 
ATOM   1363 C  CA  . LEU   B 1 35  ? 21.846 -17.507 11.421 1.00 14.18 ? 41  LEU   C CA  1 
ATOM   1364 C  C   . LEU   B 1 35  ? 22.700 -18.694 11.016 1.00 14.33 ? 41  LEU   C C   1 
ATOM   1365 O  O   . LEU   B 1 35  ? 22.632 -19.749 11.646 1.00 14.83 ? 41  LEU   C O   1 
ATOM   1366 C  CB  . LEU   B 1 35  ? 22.492 -16.701 12.557 1.00 14.88 ? 41  LEU   C CB  1 
ATOM   1367 C  CG  . LEU   B 1 35  ? 23.869 -16.053 12.260 1.00 16.12 ? 41  LEU   C CG  1 
ATOM   1368 C  CD1 . LEU   B 1 35  ? 24.026 -14.722 13.009 1.00 17.22 ? 41  LEU   C CD1 1 
ATOM   1369 C  CD2 . LEU   B 1 35  ? 25.036 -17.001 12.623 1.00 17.25 ? 41  LEU   C CD2 1 
ATOM   1370 N  N   . VAL   B 1 36  ? 23.473 -18.539 9.943  1.00 14.98 ? 42  VAL   C N   1 
ATOM   1371 C  CA  . VAL   B 1 36  ? 24.392 -19.563 9.444  1.00 15.82 ? 42  VAL   C CA  1 
ATOM   1372 C  C   . VAL   B 1 36  ? 25.787 -18.946 9.419  1.00 16.67 ? 42  VAL   C C   1 
ATOM   1373 O  O   . VAL   B 1 36  ? 25.972 -17.834 8.899  1.00 17.26 ? 42  VAL   C O   1 
ATOM   1374 C  CB  . VAL   B 1 36  ? 23.996 -20.035 8.032  1.00 16.74 ? 42  VAL   C CB  1 
ATOM   1375 C  CG1 . VAL   B 1 36  ? 25.010 -21.067 7.506  1.00 18.46 ? 42  VAL   C CG1 1 
ATOM   1376 C  CG2 . VAL   B 1 36  ? 22.572 -20.632 8.062  1.00 16.89 ? 42  VAL   C CG2 1 
ATOM   1377 N  N   . SER   B 1 37  ? 26.740 -19.646 10.023 1.00 16.66 ? 43  SER   C N   1 
ATOM   1378 C  CA  . SER   B 1 37  ? 28.132 -19.218 10.035 1.00 17.53 ? 43  SER   C CA  1 
ATOM   1379 C  C   . SER   B 1 37  ? 29.013 -20.299 9.395  1.00 19.11 ? 43  SER   C C   1 
ATOM   1380 O  O   . SER   B 1 37  ? 28.576 -21.444 9.192  1.00 19.35 ? 43  SER   C O   1 
ATOM   1381 C  CB  . SER   B 1 37  ? 28.589 -18.918 11.455 1.00 17.69 ? 43  SER   C CB  1 
ATOM   1382 O  OG  . SER   B 1 37  ? 28.527 -20.069 12.279 1.00 18.85 ? 43  SER   C OG  1 
ATOM   1383 N  N   . SER   B 1 38  ? 30.247 -19.905 9.016  1.00 20.21 ? 44  SER   C N   1 
ATOM   1384 C  CA  . SER   B 1 38  ? 31.146 -20.858 8.383  1.00 22.64 ? 44  SER   C CA  1 
ATOM   1385 C  C   . SER   B 1 38  ? 32.027 -21.593 9.412  1.00 25.01 ? 44  SER   C C   1 
ATOM   1386 O  O   . SER   B 1 38  ? 32.400 -21.033 10.455 1.00 25.91 ? 44  SER   C O   1 
ATOM   1387 C  CB  . SER   B 1 38  ? 31.992 -20.166 7.327  1.00 25.53 ? 44  SER   C CB  1 
ATOM   1388 O  OG  . SER   B 1 38  ? 32.767 -19.158 7.943  1.00 30.58 ? 44  SER   C OG  1 
ATOM   1389 N  N   . THR   B 1 39  ? 32.324 -22.874 9.121  1.00 26.35 ? 45  THR   C N   1 
ATOM   1390 C  CA  . THR   B 1 39  ? 33.156 -23.714 9.990  1.00 29.59 ? 45  THR   C CA  1 
ATOM   1391 C  C   . THR   B 1 39  ? 34.359 -24.247 9.186  1.00 33.29 ? 45  THR   C C   1 
ATOM   1392 O  O   . THR   B 1 39  ? 34.333 -24.268 7.953  1.00 33.71 ? 45  THR   C O   1 
ATOM   1393 C  CB  . THR   B 1 39  ? 32.333 -24.925 10.508 1.00 31.64 ? 45  THR   C CB  1 
ATOM   1394 O  OG1 . THR   B 1 39  ? 32.121 -25.845 9.434  1.00 33.91 ? 45  THR   C OG1 1 
ATOM   1395 C  CG2 . THR   B 1 39  ? 31.002 -24.519 11.101 1.00 31.63 ? 45  THR   C CG2 1 
ATOM   1396 N  N   . THR   B 1 40  ? 35.384 -24.735 9.889  1.00 35.87 ? 46  THR   C N   1 
ATOM   1397 C  CA  . THR   B 1 40  ? 36.536 -25.345 9.237  1.00 38.76 ? 46  THR   C CA  1 
ATOM   1398 C  C   . THR   B 1 40  ? 36.313 -26.856 9.090  1.00 40.88 ? 46  THR   C C   1 
ATOM   1399 O  O   . THR   B 1 40  ? 36.695 -27.438 8.073  1.00 42.44 ? 46  THR   C O   1 
ATOM   1400 C  CB  . THR   B 1 40  ? 37.811 -25.000 10.011 1.00 40.86 ? 46  THR   C CB  1 
ATOM   1401 O  OG1 . THR   B 1 40  ? 37.624 -25.376 11.376 1.00 43.05 ? 46  THR   C OG1 1 
ATOM   1402 C  CG2 . THR   B 1 40  ? 38.129 -23.513 9.953  1.00 41.36 ? 46  THR   C CG2 1 
ATOM   1403 N  N   . ALA   B 1 41  ? 35.679 -27.495 10.087 1.00 41.02 ? 47  ALA   C N   1 
ATOM   1404 C  CA  . ALA   B 1 41  ? 35.440 -28.937 10.039 1.00 41.23 ? 47  ALA   C CA  1 
ATOM   1405 C  C   . ALA   B 1 41  ? 34.199 -29.304 9.221  1.00 41.15 ? 47  ALA   C C   1 
ATOM   1406 O  O   . ALA   B 1 41  ? 33.264 -28.516 9.115  1.00 41.65 ? 47  ALA   C O   1 
ATOM   1407 C  CB  . ALA   B 1 41  ? 35.311 -29.494 11.449 1.00 41.85 ? 47  ALA   C CB  1 
ATOM   1408 N  N   . GLN   B 1 42  ? 34.186 -30.514 8.665  1.00 40.40 ? 48  GLN   C N   1 
ATOM   1409 C  CA  . GLN   B 1 42  ? 33.073 -30.988 7.854  1.00 39.50 ? 48  GLN   C CA  1 
ATOM   1410 C  C   . GLN   B 1 42  ? 31.933 -31.483 8.739  1.00 36.37 ? 48  GLN   C C   1 
ATOM   1411 O  O   . GLN   B 1 42  ? 32.162 -32.306 9.619  1.00 37.51 ? 48  GLN   C O   1 
ATOM   1412 C  CB  . GLN   B 1 42  ? 33.548 -32.116 6.928  1.00 43.38 ? 48  GLN   C CB  1 
ATOM   1413 C  CG  . GLN   B 1 42  ? 32.490 -32.587 5.940  1.00 49.95 ? 48  GLN   C CG  1 
ATOM   1414 C  CD  . GLN   B 1 42  ? 32.348 -31.695 4.727  1.00 57.02 ? 48  GLN   C CD  1 
ATOM   1415 O  OE1 . GLN   B 1 42  ? 33.027 -30.672 4.576  1.00 59.29 ? 48  GLN   C OE1 1 
ATOM   1416 N  NE2 . GLN   B 1 42  ? 31.454 -32.075 3.825  1.00 58.14 ? 48  GLN   C NE2 1 
ATOM   1417 N  N   . GLY   B 1 43  ? 30.734 -30.948 8.527  1.00 31.84 ? 49  GLY   C N   1 
ATOM   1418 C  CA  . GLY   B 1 43  ? 29.531 -31.313 9.281  1.00 29.57 ? 49  GLY   C CA  1 
ATOM   1419 C  C   . GLY   B 1 43  ? 28.830 -32.454 8.566  1.00 27.22 ? 49  GLY   C C   1 
ATOM   1420 O  O   . GLY   B 1 43  ? 28.840 -32.480 7.327  1.00 27.29 ? 49  GLY   C O   1 
ATOM   1421 N  N   . CYS   B 1 44  ? 28.245 -33.404 9.295  1.00 25.84 ? 50  CYS   C N   1 
ATOM   1422 C  CA  . CYS   B 1 44  ? 27.639 -34.574 8.644  1.00 25.70 ? 50  CYS   C CA  1 
ATOM   1423 C  C   . CYS   B 1 44  ? 26.136 -34.657 8.763  1.00 24.55 ? 50  CYS   C C   1 
ATOM   1424 O  O   . CYS   B 1 44  ? 25.589 -35.752 8.547  1.00 25.39 ? 50  CYS   C O   1 
ATOM   1425 C  CB  . CYS   B 1 44  ? 28.290 -35.866 9.132  1.00 27.74 ? 50  CYS   C CB  1 
ATOM   1426 S  SG  . CYS   B 1 44  ? 30.052 -35.971 8.761  1.00 34.52 ? 50  CYS   C SG  1 
ATOM   1427 N  N   . ASP   B 1 45  ? 25.457 -33.568 9.188  1.00 21.38 ? 51  ASP   C N   1 
ATOM   1428 C  CA  . ASP   B 1 45  ? 23.993 -33.657 9.281  1.00 20.66 ? 51  ASP   C CA  1 
ATOM   1429 C  C   . ASP   B 1 45  ? 23.382 -33.646 7.902  1.00 21.53 ? 51  ASP   C C   1 
ATOM   1430 O  O   . ASP   B 1 45  ? 23.837 -32.938 7.011  1.00 23.49 ? 51  ASP   C O   1 
ATOM   1431 C  CB  . ASP   B 1 45  ? 23.388 -32.492 10.097 1.00 20.22 ? 51  ASP   C CB  1 
ATOM   1432 C  CG  . ASP   B 1 45  ? 23.737 -32.534 11.578 1.00 25.94 ? 51  ASP   C CG  1 
ATOM   1433 O  OD1 . ASP   B 1 45  ? 24.216 -33.590 12.055 1.00 28.24 ? 51  ASP   C OD1 1 
ATOM   1434 O  OD2 . ASP   B 1 45  ? 23.603 -31.501 12.248 1.00 26.09 ? 51  ASP   C OD2 1 
ATOM   1435 N  N   . THR   B 1 46  ? 22.385 -34.481 7.716  1.00 20.24 ? 52  THR   C N   1 
ATOM   1436 C  CA  . THR   B 1 46  ? 21.650 -34.536 6.465  1.00 22.14 ? 52  THR   C CA  1 
ATOM   1437 C  C   . THR   B 1 46  ? 20.412 -33.661 6.634  1.00 19.98 ? 52  THR   C C   1 
ATOM   1438 O  O   . THR   B 1 46  ? 19.687 -33.853 7.596  1.00 20.72 ? 52  THR   C O   1 
ATOM   1439 C  CB  . THR   B 1 46  ? 21.205 -35.978 6.161  1.00 27.35 ? 52  THR   C CB  1 
ATOM   1440 O  OG1 . THR   B 1 46  ? 22.360 -36.735 5.770  1.00 30.83 ? 52  THR   C OG1 1 
ATOM   1441 C  CG2 . THR   B 1 46  ? 20.152 -36.055 5.040  1.00 29.00 ? 52  THR   C CG2 1 
ATOM   1442 N  N   . ILE   B 1 47  ? 20.146 -32.758 5.693  1.00 18.32 ? 53  ILE   C N   1 
ATOM   1443 C  CA  . ILE   B 1 47  ? 18.959 -31.916 5.751  1.00 17.32 ? 53  ILE   C CA  1 
ATOM   1444 C  C   . ILE   B 1 47  ? 17.828 -32.558 4.974  1.00 16.35 ? 53  ILE   C C   1 
ATOM   1445 O  O   . ILE   B 1 47  ? 18.036 -33.032 3.842  1.00 16.58 ? 53  ILE   C O   1 
ATOM   1446 C  CB  . ILE   B 1 47  ? 19.243 -30.528 5.133  1.00 19.15 ? 53  ILE   C CB  1 
ATOM   1447 C  CG1 . ILE   B 1 47  ? 20.491 -29.847 5.749  1.00 21.90 ? 53  ILE   C CG1 1 
ATOM   1448 C  CG2 . ILE   B 1 47  ? 18.000 -29.608 5.255  1.00 19.30 ? 53  ILE   C CG2 1 
ATOM   1449 C  CD1 . ILE   B 1 47  ? 20.368 -29.678 7.250  1.00 24.15 ? 53  ILE   C CD1 1 
ATOM   1450 N  N   . ALA   B 1 48  ? 16.630 -32.609 5.580  1.00 15.50 ? 54  ALA   C N   1 
ATOM   1451 C  CA  . ALA   B 1 48  ? 15.472 -33.172 4.891  1.00 14.32 ? 54  ALA   C CA  1 
ATOM   1452 C  C   . ALA   B 1 48  ? 15.039 -32.239 3.741  1.00 14.03 ? 54  ALA   C C   1 
ATOM   1453 O  O   . ALA   B 1 48  ? 15.087 -31.010 3.877  1.00 14.43 ? 54  ALA   C O   1 
ATOM   1454 C  CB  . ALA   B 1 48  ? 14.329 -33.312 5.889  1.00 14.74 ? 54  ALA   C CB  1 
ATOM   1455 N  N   . ARG   B 1 49  ? 14.598 -32.831 2.610  1.00 13.07 ? 55  ARG   C N   1 
ATOM   1456 C  CA  . ARG   B 1 49  ? 14.092 -32.048 1.450  1.00 13.53 ? 55  ARG   C CA  1 
ATOM   1457 C  C   . ARG   B 1 49  ? 12.741 -32.692 1.144  1.00 14.19 ? 55  ARG   C C   1 
ATOM   1458 O  O   . ARG   B 1 49  ? 12.659 -33.650 0.369  1.00 15.15 ? 55  ARG   C O   1 
ATOM   1459 C  CB  . ARG   B 1 49  ? 15.056 -32.123 0.248  1.00 14.30 ? 55  ARG   C CB  1 
ATOM   1460 C  CG  . ARG   B 1 49  ? 16.460 -31.626 0.579  1.00 15.61 ? 55  ARG   C CG  1 
ATOM   1461 C  CD  . ARG   B 1 49  ? 16.520 -30.146 0.979  1.00 16.86 ? 55  ARG   C CD  1 
ATOM   1462 N  NE  . ARG   B 1 49  ? 17.924 -29.743 1.187  1.00 18.62 ? 55  ARG   C NE  1 
ATOM   1463 C  CZ  . ARG   B 1 49  ? 18.297 -28.639 1.830  1.00 18.57 ? 55  ARG   C CZ  1 
ATOM   1464 N  NH1 . ARG   B 1 49  ? 17.388 -27.811 2.315  1.00 16.04 ? 55  ARG   C NH1 1 
ATOM   1465 N  NH2 . ARG   B 1 49  ? 19.594 -28.360 1.996  1.00 20.48 ? 55  ARG   C NH2 1 
ATOM   1466 N  N   . CYS   B 1 50  ? 11.701 -32.187 1.802  1.00 13.28 ? 56  CYS   C N   1 
ATOM   1467 C  CA  . CYS   B 1 50  ? 10.403 -32.850 1.843  1.00 14.26 ? 56  CYS   C CA  1 
ATOM   1468 C  C   . CYS   B 1 50  ? 9.301  -31.921 2.375  1.00 15.08 ? 56  CYS   C C   1 
ATOM   1469 O  O   . CYS   B 1 50  ? 9.576  -30.814 2.821  1.00 14.34 ? 56  CYS   C O   1 
ATOM   1470 C  CB  . CYS   B 1 50  ? 10.528 -34.067 2.770  1.00 14.83 ? 56  CYS   C CB  1 
ATOM   1471 S  SG  . CYS   B 1 50  ? 10.710 -33.607 4.529  1.00 14.74 ? 56  CYS   C SG  1 
ATOM   1472 N  N   . ASP   B 1 51  ? 8.056  -32.462 2.421  1.00 15.58 ? 57  ASP   C N   1 
ATOM   1473 C  CA  . ASP   B 1 51  ? 6.892  -31.798 2.981  1.00 16.26 ? 57  ASP   C CA  1 
ATOM   1474 C  C   . ASP   B 1 51  ? 6.313  -32.540 4.178  1.00 16.92 ? 57  ASP   C C   1 
ATOM   1475 O  O   . ASP   B 1 51  ? 5.120  -32.413 4.478  1.00 18.15 ? 57  ASP   C O   1 
ATOM   1476 C  CB  . ASP   B 1 51  ? 5.806  -31.511 1.920  1.00 19.20 ? 57  ASP   C CB  1 
ATOM   1477 C  CG  . ASP   B 1 51  ? 5.169  -32.730 1.333  1.00 25.18 ? 57  ASP   C CG  1 
ATOM   1478 O  OD1 . ASP   B 1 51  ? 5.568  -33.867 1.708  1.00 25.80 ? 57  ASP   C OD1 1 
ATOM   1479 O  OD2 . ASP   B 1 51  ? 4.249  -32.564 0.487  1.00 29.75 ? 57  ASP   C OD2 1 
ATOM   1480 N  N   . CYS   B 1 52  ? 7.140  -33.325 4.895  1.00 14.35 ? 58  CYS   C N   1 
ATOM   1481 C  CA  . CYS   B 1 52  ? 6.668  -34.020 6.111  1.00 14.09 ? 58  CYS   C CA  1 
ATOM   1482 C  C   . CYS   B 1 52  ? 6.026  -33.072 7.099  1.00 13.77 ? 58  CYS   C C   1 
ATOM   1483 O  O   . CYS   B 1 52  ? 6.458  -31.918 7.274  1.00 13.50 ? 58  CYS   C O   1 
ATOM   1484 C  CB  . CYS   B 1 52  ? 7.834  -34.739 6.796  1.00 14.05 ? 58  CYS   C CB  1 
ATOM   1485 S  SG  . CYS   B 1 52  ? 8.364  -36.270 5.944  1.00 17.11 ? 58  CYS   C SG  1 
ATOM   1486 N  N   . GLN   B 1 53  ? 5.023  -33.602 7.782  1.00 13.06 ? 59  GLN   C N   1 
ATOM   1487 C  CA  . GLN   B 1 53  ? 4.348  -32.943 8.902  1.00 13.84 ? 59  GLN   C CA  1 
ATOM   1488 C  C   . GLN   B 1 53  ? 4.367  -33.836 10.147 1.00 14.84 ? 59  GLN   C C   1 
ATOM   1489 O  O   . GLN   B 1 53  ? 3.591  -33.591 11.067 1.00 15.31 ? 59  GLN   C O   1 
ATOM   1490 C  CB  . GLN   B 1 53  ? 2.919  -32.528 8.547  1.00 14.95 ? 59  GLN   C CB  1 
ATOM   1491 C  CG  . GLN   B 1 53  ? 2.909  -31.277 7.677  1.00 15.19 ? 59  GLN   C CG  1 
ATOM   1492 C  CD  . GLN   B 1 53  ? 1.496  -30.873 7.375  1.00 18.31 ? 59  GLN   C CD  1 
ATOM   1493 O  OE1 . GLN   B 1 53  ? 0.980  -31.116 6.253  1.00 19.99 ? 59  GLN   C OE1 1 
ATOM   1494 N  NE2 . GLN   B 1 53  ? 0.835  -30.312 8.383  1.00 16.41 ? 59  GLN   C NE2 1 
ATOM   1495 N  N   . THR   B 1 54  ? 5.202  -34.884 10.189 1.00 15.31 ? 60  THR   C N   1 
ATOM   1496 C  CA  . THR   B 1 54  ? 5.380  -35.677 11.415 1.00 15.27 ? 60  THR   C CA  1 
ATOM   1497 C  C   . THR   B 1 54  ? 6.892  -35.856 11.576 1.00 14.71 ? 60  THR   C C   1 
ATOM   1498 O  O   . THR   B 1 54  ? 7.645  -35.964 10.580 1.00 15.44 ? 60  THR   C O   1 
ATOM   1499 C  CB  . THR   B 1 54  ? 4.681  -37.027 11.370 1.00 19.86 ? 60  THR   C CB  1 
ATOM   1500 O  OG1 . THR   B 1 54  ? 5.240  -37.806 10.329 1.00 23.21 ? 60  THR   C OG1 1 
ATOM   1501 C  CG2 . THR   B 1 54  ? 3.196  -36.921 11.126 1.00 21.67 ? 60  THR   C CG2 1 
ATOM   1502 N  N   . GLY   B 1 55  ? 7.323  -35.894 12.827 1.00 13.30 ? 61  GLY   C N   1 
ATOM   1503 C  CA  . GLY   B 1 55  ? 8.745  -36.030 13.111 1.00 14.38 ? 61  GLY   C CA  1 
ATOM   1504 C  C   . GLY   B 1 55  ? 9.005  -36.161 14.594 1.00 13.02 ? 61  GLY   C C   1 
ATOM   1505 O  O   . GLY   B 1 55  ? 8.072  -36.428 15.338 1.00 14.89 ? 61  GLY   C O   1 
ATOM   1506 N  N   . VAL   B 1 56  ? 10.271 -36.063 15.009 1.00 12.73 ? 62  VAL   C N   1 
ATOM   1507 C  CA  . VAL   B 1 56  ? 10.658 -36.237 16.412 1.00 12.86 ? 62  VAL   C CA  1 
ATOM   1508 C  C   . VAL   B 1 56  ? 11.575 -35.070 16.758 1.00 12.91 ? 62  VAL   C C   1 
ATOM   1509 O  O   . VAL   B 1 56  ? 12.517 -34.793 16.003 1.00 13.58 ? 62  VAL   C O   1 
ATOM   1510 C  CB  . VAL   B 1 56  ? 11.431 -37.567 16.602 1.00 13.41 ? 62  VAL   C CB  1 
ATOM   1511 C  CG1 . VAL   B 1 56  ? 11.966 -37.712 18.049 1.00 15.44 ? 62  VAL   C CG1 1 
ATOM   1512 C  CG2 . VAL   B 1 56  ? 10.550 -38.760 16.251 1.00 14.28 ? 62  VAL   C CG2 1 
ATOM   1513 N  N   . TYR   B 1 57  ? 11.350 -34.427 17.924 1.00 13.30 ? 63  TYR   C N   1 
ATOM   1514 C  CA  . TYR   B 1 57  ? 12.263 -33.337 18.330 1.00 12.65 ? 63  TYR   C CA  1 
ATOM   1515 C  C   . TYR   B 1 57  ? 12.874 -33.608 19.697 1.00 13.05 ? 63  TYR   C C   1 
ATOM   1516 O  O   . TYR   B 1 57  ? 12.297 -34.345 20.514 1.00 14.11 ? 63  TYR   C O   1 
ATOM   1517 C  CB  . TYR   B 1 57  ? 11.576 -31.910 18.326 1.00 13.19 ? 63  TYR   C CB  1 
ATOM   1518 C  CG  . TYR   B 1 57  ? 10.666 -31.622 19.516 1.00 13.96 ? 63  TYR   C CG  1 
ATOM   1519 C  CD1 . TYR   B 1 57  ? 9.405  -32.202 19.609 1.00 15.61 ? 63  TYR   C CD1 1 
ATOM   1520 C  CD2 . TYR   B 1 57  ? 11.055 -30.753 20.531 1.00 14.20 ? 63  TYR   C CD2 1 
ATOM   1521 C  CE1 . TYR   B 1 57  ? 8.541  -31.916 20.658 1.00 17.48 ? 63  TYR   C CE1 1 
ATOM   1522 C  CE2 . TYR   B 1 57  ? 10.197 -30.477 21.614 1.00 15.47 ? 63  TYR   C CE2 1 
ATOM   1523 C  CZ  . TYR   B 1 57  ? 8.945  -31.065 21.672 1.00 17.18 ? 63  TYR   C CZ  1 
ATOM   1524 O  OH  . TYR   B 1 57  ? 8.071  -30.797 22.725 1.00 19.01 ? 63  TYR   C OH  1 
ATOM   1525 N  N   . TYR   B 1 58  ? 14.052 -32.999 19.939 1.00 13.61 ? 64  TYR   C N   1 
ATOM   1526 C  CA  . TYR   B 1 58  ? 14.703 -33.112 21.219 1.00 13.61 ? 64  TYR   C CA  1 
ATOM   1527 C  C   . TYR   B 1 58  ? 14.265 -31.976 22.112 1.00 14.43 ? 64  TYR   C C   1 
ATOM   1528 O  O   . TYR   B 1 58  ? 14.407 -30.805 21.758 1.00 14.56 ? 64  TYR   C O   1 
ATOM   1529 C  CB  . TYR   B 1 58  ? 16.238 -33.126 21.075 1.00 15.00 ? 64  TYR   C CB  1 
ATOM   1530 C  CG  . TYR   B 1 58  ? 16.907 -33.299 22.423 1.00 16.29 ? 64  TYR   C CG  1 
ATOM   1531 C  CD1 . TYR   B 1 58  ? 16.784 -34.492 23.133 1.00 17.11 ? 64  TYR   C CD1 1 
ATOM   1532 C  CD2 . TYR   B 1 58  ? 17.618 -32.259 23.008 1.00 18.11 ? 64  TYR   C CD2 1 
ATOM   1533 C  CE1 . TYR   B 1 58  ? 17.350 -34.647 24.403 1.00 18.80 ? 64  TYR   C CE1 1 
ATOM   1534 C  CE2 . TYR   B 1 58  ? 18.168 -32.394 24.283 1.00 19.09 ? 64  TYR   C CE2 1 
ATOM   1535 C  CZ  . TYR   B 1 58  ? 18.025 -33.588 24.974 1.00 19.89 ? 64  TYR   C CZ  1 
ATOM   1536 O  OH  . TYR   B 1 58  ? 18.594 -33.747 26.239 1.00 22.80 ? 64  TYR   C OH  1 
ATOM   1537 N  N   . CYS   B 1 59  ? 13.768 -32.345 23.329 1.00 14.78 ? 65  CYS   C N   1 
ATOM   1538 C  CA  . CYS   B 1 59  ? 13.314 -31.374 24.338 1.00 14.87 ? 65  CYS   C CA  1 
ATOM   1539 C  C   . CYS   B 1 59  ? 14.299 -31.372 25.540 1.00 16.11 ? 65  CYS   C C   1 
ATOM   1540 O  O   . CYS   B 1 59  ? 14.255 -32.280 26.390 1.00 17.03 ? 65  CYS   C O   1 
ATOM   1541 C  CB  . CYS   B 1 59  ? 11.901 -31.739 24.771 1.00 15.06 ? 65  CYS   C CB  1 
ATOM   1542 S  SG  . CYS   B 1 59  ? 11.251 -30.675 26.088 1.00 18.05 ? 65  CYS   C SG  1 
ATOM   1543 N  N   . SER   B 1 60  ? 15.197 -30.361 25.587 1.00 16.13 ? 66  SER   C N   1 
ATOM   1544 C  CA  . SER   B 1 60  ? 16.215 -30.352 26.645 1.00 18.03 ? 66  SER   C CA  1 
ATOM   1545 C  C   . SER   B 1 60  ? 15.644 -30.245 28.038 1.00 17.71 ? 66  SER   C C   1 
ATOM   1546 O  O   . SER   B 1 60  ? 16.171 -30.867 28.956 1.00 19.02 ? 66  SER   C O   1 
ATOM   1547 C  CB  . SER   B 1 60  ? 17.263 -29.266 26.424 1.00 24.35 ? 66  SER   C CB  1 
ATOM   1548 O  OG  . SER   B 1 60  ? 16.660 -28.002 26.317 1.00 32.27 ? 66  SER   C OG  1 
ATOM   1549 N  N   . SER   B 1 61  ? 14.510 -29.534 28.196 1.00 16.89 ? 67  SER   C N   1 
ATOM   1550 C  CA  . SER   B 1 61  ? 13.895 -29.395 29.539 1.00 17.62 ? 67  SER   C CA  1 
ATOM   1551 C  C   . SER   B 1 61  ? 13.229 -30.683 30.063 1.00 18.12 ? 67  SER   C C   1 
ATOM   1552 O  O   . SER   B 1 61  ? 12.797 -30.742 31.232 1.00 18.45 ? 67  SER   C O   1 
ATOM   1553 C  CB  . SER   B 1 61  ? 12.903 -28.243 29.543 1.00 17.75 ? 67  SER   C CB  1 
ATOM   1554 O  OG  . SER   B 1 61  ? 11.816 -28.512 28.674 1.00 18.42 ? 67  SER   C OG  1 
ATOM   1555 N  N   . ARG   B 1 62  ? 13.179 -31.739 29.231 1.00 16.55 ? 68  ARG   C N   1 
ATOM   1556 C  CA  . ARG   B 1 62  ? 12.703 -33.056 29.642 1.00 16.43 ? 68  ARG   C CA  1 
ATOM   1557 C  C   . ARG   B 1 62  ? 13.783 -34.136 29.417 1.00 18.01 ? 68  ARG   C C   1 
ATOM   1558 O  O   . ARG   B 1 62  ? 13.523 -35.315 29.712 1.00 19.58 ? 68  ARG   C O   1 
ATOM   1559 C  CB  . ARG   B 1 62  ? 11.421 -33.418 28.869 1.00 17.19 ? 68  ARG   C CB  1 
ATOM   1560 C  CG  . ARG   B 1 62  ? 10.244 -32.496 29.221 1.00 18.30 ? 68  ARG   C CG  1 
ATOM   1561 C  CD  . ARG   B 1 62  ? 9.694  -32.839 30.608 1.00 19.24 ? 68  ARG   C CD  1 
ATOM   1562 N  NE  . ARG   B 1 62  ? 8.553  -31.986 30.955 1.00 21.20 ? 68  ARG   C NE  1 
ATOM   1563 C  CZ  . ARG   B 1 62  ? 8.652  -30.817 31.576 1.00 25.29 ? 68  ARG   C CZ  1 
ATOM   1564 N  NH1 . ARG   B 1 62  ? 9.840  -30.357 31.961 1.00 24.69 ? 68  ARG   C NH1 1 
ATOM   1565 N  NH2 . ARG   B 1 62  ? 7.560  -30.111 31.850 1.00 26.02 ? 68  ARG   C NH2 1 
ATOM   1566 N  N   . ARG   B 1 63  ? 14.983 -33.758 28.875 1.00 19.09 ? 69  ARG   C N   1 
ATOM   1567 C  CA  . ARG   B 1 63  ? 16.061 -34.704 28.505 1.00 20.26 ? 69  ARG   C CA  1 
ATOM   1568 C  C   . ARG   B 1 63  ? 15.493 -35.852 27.680 1.00 21.00 ? 69  ARG   C C   1 
ATOM   1569 O  O   . ARG   B 1 63  ? 15.786 -37.033 27.935 1.00 23.02 ? 69  ARG   C O   1 
ATOM   1570 C  CB  . ARG   B 1 63  ? 16.787 -35.248 29.755 1.00 22.22 ? 69  ARG   C CB  1 
ATOM   1571 C  CG  . ARG   B 1 63  ? 17.786 -34.294 30.338 1.00 26.61 ? 69  ARG   C CG  1 
ATOM   1572 C  CD  . ARG   B 1 63  ? 18.625 -35.031 31.345 1.00 32.79 ? 69  ARG   C CD  1 
ATOM   1573 N  NE  . ARG   B 1 63  ? 19.131 -34.109 32.355 1.00 39.02 ? 69  ARG   C NE  1 
ATOM   1574 C  CZ  . ARG   B 1 63  ? 18.865 -34.192 33.653 1.00 43.50 ? 69  ARG   C CZ  1 
ATOM   1575 N  NH1 . ARG   B 1 63  ? 18.093 -35.167 34.120 1.00 43.11 ? 69  ARG   C NH1 1 
ATOM   1576 N  NH2 . ARG   B 1 63  ? 19.362 -33.292 34.499 1.00 43.75 ? 69  ARG   C NH2 1 
ATOM   1577 N  N   . LYS   B 1 64  ? 14.577 -35.527 26.724 1.00 19.83 ? 70  LYS   C N   1 
ATOM   1578 C  CA  . LYS   B 1 64  ? 13.868 -36.584 26.002 1.00 19.45 ? 70  LYS   C CA  1 
ATOM   1579 C  C   . LYS   B 1 64  ? 13.485 -36.134 24.618 1.00 17.27 ? 70  LYS   C C   1 
ATOM   1580 O  O   . LYS   B 1 64  ? 13.304 -34.945 24.394 1.00 16.88 ? 70  LYS   C O   1 
ATOM   1581 C  CB  . LYS   B 1 64  ? 12.521 -36.899 26.729 1.00 24.49 ? 70  LYS   C CB  1 
ATOM   1582 C  CG  . LYS   B 1 64  ? 12.569 -38.100 27.660 1.00 34.20 ? 70  LYS   C CG  1 
ATOM   1583 C  CD  . LYS   B 1 64  ? 11.244 -38.310 28.368 1.00 41.19 ? 70  LYS   C CD  1 
ATOM   1584 C  CE  . LYS   B 1 64  ? 10.065 -38.366 27.435 1.00 44.92 ? 70  LYS   C CE  1 
ATOM   1585 N  NZ  . LYS   B 1 64  ? 8.849  -38.816 28.163 1.00 48.26 ? 70  LYS   C NZ  1 
ATOM   1586 N  N   . HIS   B 1 65  ? 13.242 -37.100 23.743 1.00 16.44 ? 71  HIS   C N   1 
ATOM   1587 C  CA  . HIS   B 1 65  ? 12.720 -36.820 22.411 1.00 15.69 ? 71  HIS   C CA  1 
ATOM   1588 C  C   . HIS   B 1 65  ? 11.227 -37.106 22.403 1.00 17.97 ? 71  HIS   C C   1 
ATOM   1589 O  O   . HIS   B 1 65  ? 10.758 -38.070 23.035 1.00 20.05 ? 71  HIS   C O   1 
ATOM   1590 C  CB  . HIS   B 1 65  ? 13.400 -37.729 21.361 1.00 15.81 ? 71  HIS   C CB  1 
ATOM   1591 C  CG  . HIS   B 1 65  ? 14.882 -37.534 21.237 1.00 16.90 ? 71  HIS   C CG  1 
ATOM   1592 N  ND1 . HIS   B 1 65  ? 15.459 -36.788 20.225 1.00 20.31 ? 71  HIS   C ND1 1 
ATOM   1593 C  CD2 . HIS   B 1 65  ? 15.870 -38.050 22.007 1.00 18.32 ? 71  HIS   C CD2 1 
ATOM   1594 C  CE1 . HIS   B 1 65  ? 16.771 -36.886 20.412 1.00 20.12 ? 71  HIS   C CE1 1 
ATOM   1595 N  NE2 . HIS   B 1 65  ? 17.056 -37.623 21.469 1.00 21.86 ? 71  HIS   C NE2 1 
ATOM   1596 N  N   . TYR   B 1 66  ? 10.467 -36.310 21.635 1.00 14.63 ? 72  TYR   C N   1 
ATOM   1597 C  CA  . TYR   B 1 66  ? 9.023  -36.528 21.503 1.00 14.94 ? 72  TYR   C CA  1 
ATOM   1598 C  C   . TYR   B 1 66  ? 8.601  -36.582 20.042 1.00 14.39 ? 72  TYR   C C   1 
ATOM   1599 O  O   . TYR   B 1 66  ? 9.025  -35.743 19.243 1.00 14.63 ? 72  TYR   C O   1 
ATOM   1600 C  CB  . TYR   B 1 66  ? 8.239  -35.347 22.128 1.00 16.18 ? 72  TYR   C CB  1 
ATOM   1601 C  CG  . TYR   B 1 66  ? 8.321  -35.262 23.633 1.00 18.30 ? 72  TYR   C CG  1 
ATOM   1602 C  CD1 . TYR   B 1 66  ? 7.560  -36.098 24.434 1.00 19.58 ? 72  TYR   C CD1 1 
ATOM   1603 C  CD2 . TYR   B 1 66  ? 9.074  -34.273 24.253 1.00 19.46 ? 72  TYR   C CD2 1 
ATOM   1604 C  CE1 . TYR   B 1 66  ? 7.595  -35.996 25.820 1.00 21.44 ? 72  TYR   C CE1 1 
ATOM   1605 C  CE2 . TYR   B 1 66  ? 9.130  -34.176 25.634 1.00 21.62 ? 72  TYR   C CE2 1 
ATOM   1606 C  CZ  . TYR   B 1 66  ? 8.396  -35.046 26.410 1.00 23.63 ? 72  TYR   C CZ  1 
ATOM   1607 O  OH  . TYR   B 1 66  ? 8.433  -34.946 27.784 1.00 25.95 ? 72  TYR   C OH  1 
ATOM   1608 N  N   . PRO   B 1 67  ? 7.739  -37.555 19.690 1.00 14.40 ? 73  PRO   C N   1 
ATOM   1609 C  CA  . PRO   B 1 67  ? 7.173  -37.590 18.325 1.00 15.32 ? 73  PRO   C CA  1 
ATOM   1610 C  C   . PRO   B 1 67  ? 6.046  -36.540 18.251 1.00 16.83 ? 73  PRO   C C   1 
ATOM   1611 O  O   . PRO   B 1 67  ? 5.244  -36.472 19.196 1.00 17.51 ? 73  PRO   C O   1 
ATOM   1612 C  CB  . PRO   B 1 67  ? 6.630  -39.037 18.214 1.00 15.62 ? 73  PRO   C CB  1 
ATOM   1613 C  CG  . PRO   B 1 67  ? 6.284  -39.397 19.610 1.00 16.49 ? 73  PRO   C CG  1 
ATOM   1614 C  CD  . PRO   B 1 67  ? 7.229  -38.661 20.537 1.00 15.32 ? 73  PRO   C CD  1 
ATOM   1615 N  N   . VAL   B 1 68  ? 5.992  -35.737 17.182 1.00 15.14 ? 74  VAL   C N   1 
ATOM   1616 C  CA  . VAL   B 1 68  ? 4.940  -34.713 17.039 1.00 15.53 ? 74  VAL   C CA  1 
ATOM   1617 C  C   . VAL   B 1 68  ? 4.469  -34.610 15.575 1.00 15.27 ? 74  VAL   C C   1 
ATOM   1618 O  O   . VAL   B 1 68  ? 5.229  -34.912 14.653 1.00 16.03 ? 74  VAL   C O   1 
ATOM   1619 C  CB  . VAL   B 1 68  ? 5.419  -33.297 17.464 1.00 18.13 ? 74  VAL   C CB  1 
ATOM   1620 C  CG1 . VAL   B 1 68  ? 5.610  -33.197 18.977 1.00 20.67 ? 74  VAL   C CG1 1 
ATOM   1621 C  CG2 . VAL   B 1 68  ? 6.689  -32.888 16.714 1.00 18.35 ? 74  VAL   C CG2 1 
ATOM   1622 N  N   . SER   B 1 69  ? 3.211  -34.145 15.392 1.00 15.31 ? 75  SER   C N   1 
ATOM   1623 C  CA  . SER   B 1 69  ? 2.730  -33.643 14.116 1.00 14.63 ? 75  SER   C CA  1 
ATOM   1624 C  C   . SER   B 1 69  ? 3.003  -32.096 14.165 1.00 14.21 ? 75  SER   C C   1 
ATOM   1625 O  O   . SER   B 1 69  ? 2.933  -31.444 15.226 1.00 14.95 ? 75  SER   C O   1 
ATOM   1626 C  CB  . SER   B 1 69  ? 1.221  -33.873 13.968 1.00 17.81 ? 75  SER   C CB  1 
ATOM   1627 O  OG  . SER   B 1 69  ? 0.925  -35.263 13.900 1.00 23.39 ? 75  SER   C OG  1 
ATOM   1628 N  N   . PHE   B 1 70  ? 3.364  -31.506 13.014 1.00 13.55 ? 76  PHE   C N   1 
ATOM   1629 C  CA  . PHE   B 1 70  ? 3.675  -30.069 12.984 1.00 13.53 ? 76  PHE   C CA  1 
ATOM   1630 C  C   . PHE   B 1 70  ? 3.102  -29.443 11.726 1.00 13.27 ? 76  PHE   C C   1 
ATOM   1631 O  O   . PHE   B 1 70  ? 2.816  -30.145 10.755 1.00 14.58 ? 76  PHE   C O   1 
ATOM   1632 C  CB  . PHE   B 1 70  ? 5.191  -29.804 13.136 1.00 12.86 ? 76  PHE   C CB  1 
ATOM   1633 C  CG  . PHE   B 1 70  ? 6.082  -30.546 12.161 1.00 12.39 ? 76  PHE   C CG  1 
ATOM   1634 C  CD1 . PHE   B 1 70  ? 6.574  -31.807 12.462 1.00 12.66 ? 76  PHE   C CD1 1 
ATOM   1635 C  CD2 . PHE   B 1 70  ? 6.495  -29.949 10.981 1.00 13.69 ? 76  PHE   C CD2 1 
ATOM   1636 C  CE1 . PHE   B 1 70  ? 7.400  -32.489 11.547 1.00 13.55 ? 76  PHE   C CE1 1 
ATOM   1637 C  CE2 . PHE   B 1 70  ? 7.352  -30.606 10.104 1.00 13.69 ? 76  PHE   C CE2 1 
ATOM   1638 C  CZ  . PHE   B 1 70  ? 7.805  -31.878 10.388 1.00 13.58 ? 76  PHE   C CZ  1 
ATOM   1639 N  N   . SER   B 1 71  ? 2.852  -28.135 11.785 1.00 13.09 ? 77  SER   C N   1 
ATOM   1640 C  CA  . SER   B 1 71  ? 2.207  -27.432 10.687 1.00 14.42 ? 77  SER   C CA  1 
ATOM   1641 C  C   . SER   B 1 71  ? 3.138  -27.161 9.509  1.00 15.06 ? 77  SER   C C   1 
ATOM   1642 O  O   . SER   B 1 71  ? 4.297  -27.583 9.515  1.00 15.29 ? 77  SER   C O   1 
ATOM   1643 C  CB  . SER   B 1 71  ? 1.598  -26.143 11.224 1.00 15.87 ? 77  SER   C CB  1 
ATOM   1644 O  OG  . SER   B 1 71  ? 2.579  -25.179 11.571 1.00 17.12 ? 77  SER   C OG  1 
ATOM   1645 N  N   . LYS   B 1 72  ? 2.597  -26.521 8.452  1.00 14.58 ? 78  LYS   C N   1 
ATOM   1646 C  CA  . LYS   B 1 72  ? 3.457  -26.136 7.330  1.00 15.29 ? 78  LYS   C CA  1 
ATOM   1647 C  C   . LYS   B 1 72  ? 4.141  -24.803 7.672  1.00 15.25 ? 78  LYS   C C   1 
ATOM   1648 O  O   . LYS   B 1 72  ? 3.606  -24.023 8.471  1.00 18.18 ? 78  LYS   C O   1 
ATOM   1649 C  CB  . LYS   B 1 72  ? 2.604  -25.986 6.072  1.00 18.37 ? 78  LYS   C CB  1 
ATOM   1650 C  CG  . LYS   B 1 72  ? 1.975  -27.330 5.686  1.00 21.88 ? 78  LYS   C CG  1 
ATOM   1651 C  CD  . LYS   B 1 72  ? 1.292  -27.206 4.337  1.00 31.01 ? 78  LYS   C CD  1 
ATOM   1652 C  CE  . LYS   B 1 72  ? 0.711  -28.520 3.900  1.00 38.85 ? 78  LYS   C CE  1 
ATOM   1653 N  NZ  . LYS   B 1 72  ? 0.262  -28.453 2.485  1.00 43.82 ? 78  LYS   C NZ  1 
ATOM   1654 N  N   . PRO   B 1 73  ? 5.318  -24.512 7.101  1.00 14.66 ? 79  PRO   C N   1 
ATOM   1655 C  CA  . PRO   B 1 73  ? 5.997  -23.234 7.410  1.00 14.79 ? 79  PRO   C CA  1 
ATOM   1656 C  C   . PRO   B 1 73  ? 5.128  -22.035 7.081  1.00 16.67 ? 79  PRO   C C   1 
ATOM   1657 O  O   . PRO   B 1 73  ? 4.542  -21.944 5.979  1.00 17.32 ? 79  PRO   C O   1 
ATOM   1658 C  CB  . PRO   B 1 73  ? 7.277  -23.253 6.532  1.00 16.13 ? 79  PRO   C CB  1 
ATOM   1659 C  CG  . PRO   B 1 73  ? 7.461  -24.725 6.162  1.00 17.72 ? 79  PRO   C CG  1 
ATOM   1660 C  CD  . PRO   B 1 73  ? 6.089  -25.353 6.161  1.00 15.30 ? 79  PRO   C CD  1 
ATOM   1661 N  N   . SER   B 1 74  ? 5.024  -21.121 8.059  1.00 16.29 ? 80  SER   C N   1 
ATOM   1662 C  CA  . SER   B 1 74  ? 4.136  -19.988 7.852  1.00 18.72 ? 80  SER   C CA  1 
ATOM   1663 C  C   . SER   B 1 74  ? 4.515  -18.802 8.711  1.00 17.24 ? 80  SER   C C   1 
ATOM   1664 O  O   . SER   B 1 74  ? 5.484  -18.847 9.463  1.00 16.15 ? 80  SER   C O   1 
ATOM   1665 C  CB  . SER   B 1 74  ? 2.691  -20.416 8.093  1.00 24.76 ? 80  SER   C CB  1 
ATOM   1666 O  OG  . SER   B 1 74  ? 2.532  -20.697 9.470  1.00 29.09 ? 80  SER   C OG  1 
ATOM   1667 N  N   . LEU   B 1 75  ? 3.774  -17.696 8.510  1.00 17.55 ? 81  LEU   C N   1 
ATOM   1668 C  CA  . LEU   B 1 75  ? 4.014  -16.440 9.195  1.00 18.00 ? 81  LEU   C CA  1 
ATOM   1669 C  C   . LEU   B 1 75  ? 3.152  -16.467 10.477 1.00 17.96 ? 81  LEU   C C   1 
ATOM   1670 O  O   . LEU   B 1 75  ? 1.900  -16.552 10.389 1.00 20.51 ? 81  LEU   C O   1 
ATOM   1671 C  CB  . LEU   B 1 75  ? 3.468  -15.342 8.276  1.00 20.29 ? 81  LEU   C CB  1 
ATOM   1672 C  CG  . LEU   B 1 75  ? 4.379  -14.327 7.602  1.00 25.31 ? 81  LEU   C CG  1 
ATOM   1673 C  CD1 . LEU   B 1 75  ? 3.544  -13.077 7.238  1.00 27.36 ? 81  LEU   C CD1 1 
ATOM   1674 C  CD2 . LEU   B 1 75  ? 5.545  -13.888 8.427  1.00 25.80 ? 81  LEU   C CD2 1 
ATOM   1675 N  N   . ILE   B 1 76  ? 3.785  -16.431 11.656 1.00 16.98 ? 82  ILE   C N   1 
ATOM   1676 C  CA  . ILE   B 1 76  ? 3.113  -16.542 12.935 1.00 18.04 ? 82  ILE   C CA  1 
ATOM   1677 C  C   . ILE   B 1 76  ? 3.514  -15.405 13.865 1.00 18.41 ? 82  ILE   C C   1 
ATOM   1678 O  O   . ILE   B 1 76  ? 4.693  -15.097 13.953 1.00 17.77 ? 82  ILE   C O   1 
ATOM   1679 C  CB  . ILE   B 1 76  ? 3.454  -17.925 13.540 1.00 20.95 ? 82  ILE   C CB  1 
ATOM   1680 C  CG1 . ILE   B 1 76  ? 2.870  -19.063 12.639 1.00 25.08 ? 82  ILE   C CG1 1 
ATOM   1681 C  CG2 . ILE   B 1 76  ? 2.971  -18.030 15.008 1.00 22.75 ? 82  ILE   C CG2 1 
ATOM   1682 C  CD1 . ILE   B 1 76  ? 3.315  -20.391 12.960 1.00 29.54 ? 82  ILE   C CD1 1 
ATOM   1683 N  N   . PHE   B 1 77  ? 2.548  -14.782 14.558 1.00 18.24 ? 83  PHE   C N   1 
ATOM   1684 C  CA  . PHE   B 1 77  ? 2.860  -13.694 15.473 1.00 19.59 ? 83  PHE   C CA  1 
ATOM   1685 C  C   . PHE   B 1 77  ? 3.585  -14.226 16.712 1.00 20.08 ? 83  PHE   C C   1 
ATOM   1686 O  O   . PHE   B 1 77  ? 3.187  -15.247 17.299 1.00 21.22 ? 83  PHE   C O   1 
ATOM   1687 C  CB  . PHE   B 1 77  ? 1.570  -12.956 15.890 1.00 21.14 ? 83  PHE   C CB  1 
ATOM   1688 C  CG  . PHE   B 1 77  ? 1.809  -11.817 16.860 1.00 23.55 ? 83  PHE   C CG  1 
ATOM   1689 C  CD1 . PHE   B 1 77  ? 1.588  -11.982 18.208 1.00 25.49 ? 83  PHE   C CD1 1 
ATOM   1690 C  CD2 . PHE   B 1 77  ? 2.323  -10.613 16.422 1.00 26.31 ? 83  PHE   C CD2 1 
ATOM   1691 C  CE1 . PHE   B 1 77  ? 1.830  -10.934 19.104 1.00 27.29 ? 83  PHE   C CE1 1 
ATOM   1692 C  CE2 . PHE   B 1 77  ? 2.575  -9.568  17.321 1.00 27.13 ? 83  PHE   C CE2 1 
ATOM   1693 C  CZ  . PHE   B 1 77  ? 2.321  -9.741  18.649 1.00 27.18 ? 83  PHE   C CZ  1 
ATOM   1694 N  N   . VAL   B 1 78  ? 4.691  -13.563 17.075 1.00 19.64 ? 84  VAL   C N   1 
ATOM   1695 C  CA  . VAL   B 1 78  ? 5.487  -13.902 18.263 1.00 19.80 ? 84  VAL   C CA  1 
ATOM   1696 C  C   . VAL   B 1 78  ? 5.602  -12.640 19.122 1.00 20.24 ? 84  VAL   C C   1 
ATOM   1697 O  O   . VAL   B 1 78  ? 6.046  -11.588 18.645 1.00 19.79 ? 84  VAL   C O   1 
ATOM   1698 C  CB  . VAL   B 1 78  ? 6.897  -14.402 17.843 1.00 19.69 ? 84  VAL   C CB  1 
ATOM   1699 C  CG1 . VAL   B 1 78  ? 7.737  -14.793 19.067 1.00 20.50 ? 84  VAL   C CG1 1 
ATOM   1700 C  CG2 . VAL   B 1 78  ? 6.782  -15.584 16.867 1.00 19.86 ? 84  VAL   C CG2 1 
ATOM   1701 N  N   . GLU   B 1 79  ? 5.283  -12.765 20.424 1.00 21.33 ? 85  GLU   C N   1 
ATOM   1702 C  CA  . GLU   B 1 79  ? 5.348  -11.644 21.351 1.00 22.33 ? 85  GLU   C CA  1 
ATOM   1703 C  C   . GLU   B 1 79  ? 6.768  -11.101 21.542 1.00 20.74 ? 85  GLU   C C   1 
ATOM   1704 O  O   . GLU   B 1 79  ? 7.717  -11.846 21.352 1.00 19.61 ? 85  GLU   C O   1 
ATOM   1705 C  CB  . GLU   B 1 79  ? 4.846  -12.110 22.717 1.00 26.24 ? 85  GLU   C CB  1 
ATOM   1706 C  CG  . GLU   B 1 79  ? 3.493  -12.787 22.685 1.00 34.52 ? 85  GLU   C CG  1 
ATOM   1707 C  CD  . GLU   B 1 79  ? 2.319  -11.858 22.874 1.00 44.98 ? 85  GLU   C CD  1 
ATOM   1708 O  OE1 . GLU   B 1 79  ? 1.182  -12.377 22.941 1.00 48.12 ? 85  GLU   C OE1 1 
ATOM   1709 O  OE2 . GLU   B 1 79  ? 2.523  -10.623 22.954 1.00 45.94 ? 85  GLU   C OE2 1 
ATOM   1710 N  N   . ALA   B 1 80  ? 6.919  -9.821  21.971 1.00 20.53 ? 86  ALA   C N   1 
ATOM   1711 C  CA  . ALA   B 1 80  ? 8.246  -9.244  22.195 1.00 20.12 ? 86  ALA   C CA  1 
ATOM   1712 C  C   . ALA   B 1 80  ? 9.005  -10.042 23.244 1.00 19.83 ? 86  ALA   C C   1 
ATOM   1713 O  O   . ALA   B 1 80  ? 8.427  -10.622 24.181 1.00 20.86 ? 86  ALA   C O   1 
ATOM   1714 C  CB  . ALA   B 1 80  ? 8.120  -7.791  22.689 1.00 19.69 ? 86  ALA   C CB  1 
ATOM   1715 N  N   . SER   B 1 81  ? 10.307 -10.068 23.083 1.00 18.07 ? 87  SER   C N   1 
ATOM   1716 C  CA  . SER   B 1 81  ? 11.217 -10.666 24.042 1.00 17.75 ? 87  SER   C CA  1 
ATOM   1717 C  C   . SER   B 1 81  ? 12.414 -9.697  24.152 1.00 19.15 ? 87  SER   C C   1 
ATOM   1718 O  O   . SER   B 1 81  ? 12.437 -8.633  23.504 1.00 20.75 ? 87  SER   C O   1 
ATOM   1719 C  CB  . SER   B 1 81  ? 11.696 -12.045 23.574 1.00 18.49 ? 87  SER   C CB  1 
ATOM   1720 O  OG  . SER   B 1 81  ? 12.430 -11.903 22.368 1.00 19.44 ? 87  SER   C OG  1 
ATOM   1721 N  N   . GLU   B 1 82  ? 13.397 -10.054 24.982 1.00 19.47 ? 88  GLU   C N   1 
ATOM   1722 C  CA  . GLU   B 1 82  ? 14.623 -9.228  25.067 1.00 20.62 ? 88  GLU   C CA  1 
ATOM   1723 C  C   . GLU   B 1 82  ? 15.370 -9.247  23.705 1.00 20.98 ? 88  GLU   C C   1 
ATOM   1724 O  O   . GLU   B 1 82  ? 16.154 -8.335  23.408 1.00 20.89 ? 88  GLU   C O   1 
ATOM   1725 C  CB  . GLU   B 1 82  ? 15.609 -9.837  26.093 1.00 26.08 ? 88  GLU   C CB  1 
ATOM   1726 C  CG  . GLU   B 1 82  ? 14.985 -10.316 27.391 1.00 37.17 ? 88  GLU   C CG  1 
ATOM   1727 C  CD  . GLU   B 1 82  ? 14.692 -11.803 27.335 1.00 44.72 ? 88  GLU   C CD  1 
ATOM   1728 O  OE1 . GLU   B 1 82  ? 15.554 -12.600 27.774 1.00 48.95 ? 88  GLU   C OE1 1 
ATOM   1729 O  OE2 . GLU   B 1 82  ? 13.613 -12.173 26.818 1.00 41.55 ? 88  GLU   C OE2 1 
ATOM   1730 N  N   . TYR   B 1 83  ? 15.140 -10.280 22.893 1.00 20.19 ? 89  TYR   C N   1 
ATOM   1731 C  CA  . TYR   B 1 83  ? 15.856 -10.493 21.654 1.00 20.27 ? 89  TYR   C CA  1 
ATOM   1732 C  C   . TYR   B 1 83  ? 15.213 -9.869  20.429 1.00 20.14 ? 89  TYR   C C   1 
ATOM   1733 O  O   . TYR   B 1 83  ? 15.913 -9.626  19.427 1.00 21.82 ? 89  TYR   C O   1 
ATOM   1734 C  CB  . TYR   B 1 83  ? 15.982 -12.006 21.424 1.00 20.07 ? 89  TYR   C CB  1 
ATOM   1735 C  CG  . TYR   B 1 83  ? 16.631 -12.724 22.575 1.00 21.36 ? 89  TYR   C CG  1 
ATOM   1736 C  CD1 . TYR   B 1 83  ? 18.011 -12.722 22.730 1.00 22.77 ? 89  TYR   C CD1 1 
ATOM   1737 C  CD2 . TYR   B 1 83  ? 15.873 -13.422 23.498 1.00 22.13 ? 89  TYR   C CD2 1 
ATOM   1738 C  CE1 . TYR   B 1 83  ? 18.622 -13.385 23.788 1.00 24.91 ? 89  TYR   C CE1 1 
ATOM   1739 C  CE2 . TYR   B 1 83  ? 16.470 -14.078 24.567 1.00 24.77 ? 89  TYR   C CE2 1 
ATOM   1740 C  CZ  . TYR   B 1 83  ? 17.849 -14.079 24.698 1.00 26.65 ? 89  TYR   C CZ  1 
ATOM   1741 O  OH  . TYR   B 1 83  ? 18.456 -14.753 25.741 1.00 31.32 ? 89  TYR   C OH  1 
ATOM   1742 N  N   . TYR   B 1 84  ? 13.898 -9.668  20.448 1.00 18.29 ? 90  TYR   C N   1 
ATOM   1743 C  CA  . TYR   B 1 84  ? 13.174 -9.209  19.268 1.00 18.12 ? 90  TYR   C CA  1 
ATOM   1744 C  C   . TYR   B 1 84  ? 12.013 -8.357  19.661 1.00 20.02 ? 90  TYR   C C   1 
ATOM   1745 O  O   . TYR   B 1 84  ? 11.352 -8.612  20.678 1.00 20.28 ? 90  TYR   C O   1 
ATOM   1746 C  CB  . TYR   B 1 84  ? 12.559 -10.401 18.453 1.00 17.67 ? 90  TYR   C CB  1 
ATOM   1747 C  CG  . TYR   B 1 84  ? 13.549 -11.330 17.810 1.00 17.14 ? 90  TYR   C CG  1 
ATOM   1748 C  CD1 . TYR   B 1 84  ? 13.749 -12.615 18.299 1.00 17.08 ? 90  TYR   C CD1 1 
ATOM   1749 C  CD2 . TYR   B 1 84  ? 14.258 -10.948 16.672 1.00 16.23 ? 90  TYR   C CD2 1 
ATOM   1750 C  CE1 . TYR   B 1 84  ? 14.646 -13.480 17.702 1.00 17.39 ? 90  TYR   C CE1 1 
ATOM   1751 C  CE2 . TYR   B 1 84  ? 15.171 -11.796 16.082 1.00 16.32 ? 90  TYR   C CE2 1 
ATOM   1752 C  CZ  . TYR   B 1 84  ? 15.339 -13.070 16.583 1.00 16.80 ? 90  TYR   C CZ  1 
ATOM   1753 O  OH  . TYR   B 1 84  ? 16.251 -13.889 15.992 1.00 16.81 ? 90  TYR   C OH  1 
ATOM   1754 N  N   . PRO   B 1 85  ? 11.645 -7.391  18.812 1.00 20.27 ? 91  PRO   C N   1 
ATOM   1755 C  CA  . PRO   B 1 85  ? 10.382 -6.717  19.030 1.00 19.31 ? 91  PRO   C CA  1 
ATOM   1756 C  C   . PRO   B 1 85  ? 9.225  -7.704  18.749 1.00 19.27 ? 91  PRO   C C   1 
ATOM   1757 O  O   . PRO   B 1 85  ? 9.403  -8.728  18.053 1.00 18.71 ? 91  PRO   C O   1 
ATOM   1758 C  CB  . PRO   B 1 85  ? 10.386 -5.611  17.938 1.00 20.75 ? 91  PRO   C CB  1 
ATOM   1759 C  CG  . PRO   B 1 85  ? 11.210 -6.202  16.857 1.00 21.77 ? 91  PRO   C CG  1 
ATOM   1760 C  CD  . PRO   B 1 85  ? 12.276 -6.997  17.532 1.00 19.57 ? 91  PRO   C CD  1 
ATOM   1761 N  N   . ALA   B 1 86  ? 8.011  -7.365  19.145 1.00 19.51 ? 92  ALA   C N   1 
ATOM   1762 C  CA  . ALA   B 1 86  ? 6.799  -8.117  18.772 1.00 20.96 ? 92  ALA   C CA  1 
ATOM   1763 C  C   . ALA   B 1 86  ? 6.727  -8.096  17.215 1.00 20.59 ? 92  ALA   C C   1 
ATOM   1764 O  O   . ALA   B 1 86  ? 7.016  -7.034  16.606 1.00 20.41 ? 92  ALA   C O   1 
ATOM   1765 C  CB  . ALA   B 1 86  ? 5.560  -7.421  19.339 1.00 21.52 ? 92  ALA   C CB  1 
ATOM   1766 N  N   . ARG   B 1 87  ? 6.518  -9.266  16.582 1.00 20.01 ? 93  ARG   C N   1 
ATOM   1767 C  CA  . ARG   B 1 87  ? 6.608  -9.301  15.116 1.00 19.65 ? 93  ARG   C CA  1 
ATOM   1768 C  C   . ARG   B 1 87  ? 6.012  -10.599 14.580 1.00 20.15 ? 93  ARG   C C   1 
ATOM   1769 O  O   . ARG   B 1 87  ? 5.698  -11.512 15.357 1.00 20.74 ? 93  ARG   C O   1 
ATOM   1770 C  CB  . ARG   B 1 87  ? 8.115  -9.227  14.710 1.00 19.87 ? 93  ARG   C CB  1 
ATOM   1771 C  CG  . ARG   B 1 87  ? 8.857  -10.584 15.023 1.00 17.85 ? 93  ARG   C CG  1 
ATOM   1772 C  CD  . ARG   B 1 87  ? 10.344 -10.418 15.232 1.00 18.00 ? 93  ARG   C CD  1 
ATOM   1773 N  NE  . ARG   B 1 87  ? 11.156 -11.541 14.763 1.00 16.55 ? 93  ARG   C NE  1 
ATOM   1774 C  CZ  . ARG   B 1 87  ? 11.237 -12.726 15.371 1.00 19.19 ? 93  ARG   C CZ  1 
ATOM   1775 N  NH1 . ARG   B 1 87  ? 12.022 -13.670 14.883 1.00 17.86 ? 93  ARG   C NH1 1 
ATOM   1776 N  NH2 . ARG   B 1 87  ? 10.480 -12.992 16.439 1.00 18.36 ? 93  ARG   C NH2 1 
ATOM   1777 N  N   . TYR   B 1 88  ? 5.923  -10.714 13.250 1.00 19.88 ? 94  TYR   C N   1 
ATOM   1778 C  CA  . TYR   B 1 88  ? 5.550  -11.984 12.644 1.00 20.41 ? 94  TYR   C CA  1 
ATOM   1779 C  C   . TYR   B 1 88  ? 6.859  -12.687 12.274 1.00 18.29 ? 94  TYR   C C   1 
ATOM   1780 O  O   . TYR   B 1 88  ? 7.735  -12.096 11.606 1.00 18.74 ? 94  TYR   C O   1 
ATOM   1781 C  CB  . TYR   B 1 88  ? 4.750  -11.763 11.361 1.00 22.29 ? 94  TYR   C CB  1 
ATOM   1782 C  CG  . TYR   B 1 88  ? 3.364  -11.260 11.657 1.00 25.23 ? 94  TYR   C CG  1 
ATOM   1783 C  CD1 . TYR   B 1 88  ? 2.319  -12.143 11.894 1.00 27.66 ? 94  TYR   C CD1 1 
ATOM   1784 C  CD2 . TYR   B 1 88  ? 3.119  -9.905  11.809 1.00 28.37 ? 94  TYR   C CD2 1 
ATOM   1785 C  CE1 . TYR   B 1 88  ? 1.039  -11.679 12.188 1.00 30.04 ? 94  TYR   C CE1 1 
ATOM   1786 C  CE2 . TYR   B 1 88  ? 1.857  -9.433  12.153 1.00 30.57 ? 94  TYR   C CE2 1 
ATOM   1787 C  CZ  . TYR   B 1 88  ? 0.824  -10.326 12.343 1.00 32.42 ? 94  TYR   C CZ  1 
ATOM   1788 O  OH  . TYR   B 1 88  ? -0.426 -9.845  12.672 1.00 37.64 ? 94  TYR   C OH  1 
ATOM   1789 N  N   . GLN   B 1 89  ? 7.018  -13.926 12.760 1.00 16.06 ? 95  GLN   C N   1 
ATOM   1790 C  CA  . GLN   B 1 89  ? 8.168  -14.744 12.397 1.00 14.99 ? 95  GLN   C CA  1 
ATOM   1791 C  C   . GLN   B 1 89  ? 7.739  -15.603 11.210 1.00 14.95 ? 95  GLN   C C   1 
ATOM   1792 O  O   . GLN   B 1 89  ? 6.686  -16.232 11.254 1.00 17.18 ? 95  GLN   C O   1 
ATOM   1793 C  CB  . GLN   B 1 89  ? 8.610  -15.589 13.604 1.00 15.85 ? 95  GLN   C CB  1 
ATOM   1794 C  CG  . GLN   B 1 89  ? 9.785  -16.547 13.233 1.00 15.73 ? 95  GLN   C CG  1 
ATOM   1795 C  CD  . GLN   B 1 89  ? 10.559 -17.031 14.445 1.00 16.05 ? 95  GLN   C CD  1 
ATOM   1796 O  OE1 . GLN   B 1 89  ? 10.778 -16.289 15.422 1.00 17.05 ? 95  GLN   C OE1 1 
ATOM   1797 N  NE2 . GLN   B 1 89  ? 11.014 -18.285 14.367 1.00 14.30 ? 95  GLN   C NE2 1 
ATOM   1798 N  N   . SER   B 1 90  ? 8.572  -15.643 10.161 1.00 14.05 ? 96  SER   C N   1 
ATOM   1799 C  CA  . SER   B 1 90  ? 8.268  -16.417 8.972  1.00 13.70 ? 96  SER   C CA  1 
ATOM   1800 C  C   . SER   B 1 90  ? 8.922  -17.808 9.033  1.00 14.45 ? 96  SER   C C   1 
ATOM   1801 O  O   . SER   B 1 90  ? 9.851  -18.048 9.849  1.00 15.05 ? 96  SER   C O   1 
ATOM   1802 C  CB  . SER   B 1 90  ? 8.754  -15.677 7.716  1.00 16.11 ? 96  SER   C CB  1 
ATOM   1803 O  OG  . SER   B 1 90  ? 10.170 -15.532 7.736  1.00 18.22 ? 96  SER   C OG  1 
ATOM   1804 N  N   . HIS   B 1 91  ? 8.423  -18.721 8.183  1.00 13.97 ? 97  HIS   C N   1 
ATOM   1805 C  CA  . HIS   B 1 91  ? 8.952  -20.086 8.012  1.00 13.47 ? 97  HIS   C CA  1 
ATOM   1806 C  C   . HIS   B 1 91  ? 8.881  -20.847 9.358  1.00 14.38 ? 97  HIS   C C   1 
ATOM   1807 O  O   . HIS   B 1 91  ? 9.728  -21.709 9.601  1.00 14.73 ? 97  HIS   C O   1 
ATOM   1808 C  CB  . HIS   B 1 91  ? 10.403 -20.047 7.454  1.00 14.80 ? 97  HIS   C CB  1 
ATOM   1809 C  CG  . HIS   B 1 91  ? 10.479 -19.437 6.071  1.00 16.08 ? 97  HIS   C CG  1 
ATOM   1810 N  ND1 . HIS   B 1 91  ? 10.445 -20.236 4.933  1.00 19.16 ? 97  HIS   C ND1 1 
ATOM   1811 C  CD2 . HIS   B 1 91  ? 10.551 -18.135 5.691  1.00 18.04 ? 97  HIS   C CD2 1 
ATOM   1812 C  CE1 . HIS   B 1 91  ? 10.501 -19.404 3.896  1.00 19.50 ? 97  HIS   C CE1 1 
ATOM   1813 N  NE2 . HIS   B 1 91  ? 10.581 -18.126 4.297  1.00 19.43 ? 97  HIS   C NE2 1 
ATOM   1814 N  N   . LEU   B 1 92  ? 7.862  -20.534 10.195 1.00 14.75 ? 98  LEU   C N   1 
ATOM   1815 C  CA  . LEU   B 1 92  ? 7.695  -21.149 11.515 1.00 13.94 ? 98  LEU   C CA  1 
ATOM   1816 C  C   . LEU   B 1 92  ? 6.615  -22.234 11.457 1.00 14.27 ? 98  LEU   C C   1 
ATOM   1817 O  O   . LEU   B 1 92  ? 5.577  -22.074 10.810 1.00 14.38 ? 98  LEU   C O   1 
ATOM   1818 C  CB  . LEU   B 1 92  ? 7.311  -20.072 12.574 1.00 15.37 ? 98  LEU   C CB  1 
ATOM   1819 C  CG  . LEU   B 1 92  ? 7.256  -20.486 14.059 1.00 17.29 ? 98  LEU   C CG  1 
ATOM   1820 C  CD1 . LEU   B 1 92  ? 8.639  -20.935 14.560 1.00 16.83 ? 98  LEU   C CD1 1 
ATOM   1821 C  CD2 . LEU   B 1 92  ? 6.777  -19.302 14.927 1.00 20.34 ? 98  LEU   C CD2 1 
ATOM   1822 N  N   . MET   B 1 93  ? 6.876  -23.368 12.134 1.00 13.80 ? 99  MET   C N   1 
ATOM   1823 C  CA  . MET   B 1 93  ? 5.912  -24.482 12.158 1.00 13.41 ? 99  MET   C CA  1 
ATOM   1824 C  C   . MET   B 1 93  ? 5.536  -24.745 13.605 1.00 14.79 ? 99  MET   C C   1 
ATOM   1825 O  O   . MET   B 1 93  ? 6.424  -24.781 14.451 1.00 15.53 ? 99  MET   C O   1 
ATOM   1826 C  CB  . MET   B 1 93  ? 6.596  -25.742 11.611 1.00 13.10 ? 99  MET   C CB  1 
ATOM   1827 C  CG  . MET   B 1 93  ? 7.021  -25.501 10.176 1.00 15.51 ? 99  MET   C CG  1 
ATOM   1828 S  SD  . MET   B 1 93  ? 7.975  -26.854 9.469  1.00 16.81 ? 99  MET   C SD  1 
ATOM   1829 C  CE  . MET   B 1 93  ? 9.497  -26.778 10.536 1.00 19.82 ? 99  MET   C CE  1 
ATOM   1830 N  N   . LEU   B 1 94  ? 4.257  -24.949 13.900 1.00 13.72 ? 100 LEU   C N   1 
ATOM   1831 C  CA  . LEU   B 1 94  ? 3.816  -25.207 15.280 1.00 13.99 ? 100 LEU   C CA  1 
ATOM   1832 C  C   . LEU   B 1 94  ? 3.445  -26.653 15.501 1.00 13.98 ? 100 LEU   C C   1 
ATOM   1833 O  O   . LEU   B 1 94  ? 2.922  -27.325 14.592 1.00 14.11 ? 100 LEU   C O   1 
ATOM   1834 C  CB  . LEU   B 1 94  ? 2.598  -24.321 15.672 1.00 15.98 ? 100 LEU   C CB  1 
ATOM   1835 C  CG  . LEU   B 1 94  ? 2.850  -22.837 15.619 1.00 17.25 ? 100 LEU   C CG  1 
ATOM   1836 C  CD1 . LEU   B 1 94  ? 1.609  -22.051 16.128 1.00 18.41 ? 100 LEU   C CD1 1 
ATOM   1837 C  CD2 . LEU   B 1 94  ? 4.088  -22.421 16.462 1.00 17.71 ? 100 LEU   C CD2 1 
ATOM   1838 N  N   . ALA   B 1 95  ? 3.680  -27.143 16.736 1.00 14.42 ? 101 ALA   C N   1 
ATOM   1839 C  CA  . ALA   B 1 95  ? 3.207  -28.455 17.190 1.00 14.82 ? 101 ALA   C CA  1 
ATOM   1840 C  C   . ALA   B 1 95  ? 2.645  -28.314 18.603 1.00 15.08 ? 101 ALA   C C   1 
ATOM   1841 O  O   . ALA   B 1 95  ? 3.026  -27.405 19.335 1.00 15.70 ? 101 ALA   C O   1 
ATOM   1842 C  CB  . ALA   B 1 95  ? 4.366  -29.459 17.257 1.00 14.82 ? 101 ALA   C CB  1 
ATOM   1843 N  N   . VAL   B 1 96  ? 1.766  -29.242 19.005 1.00 15.10 ? 102 VAL   C N   1 
ATOM   1844 C  CA  . VAL   B 1 96  ? 1.340  -29.366 20.389 1.00 15.67 ? 102 VAL   C CA  1 
ATOM   1845 C  C   . VAL   B 1 96  ? 2.463  -30.115 21.135 1.00 18.00 ? 102 VAL   C C   1 
ATOM   1846 O  O   . VAL   B 1 96  ? 2.743  -31.277 20.830 1.00 19.71 ? 102 VAL   C O   1 
ATOM   1847 C  CB  . VAL   B 1 96  ? -0.015 -30.127 20.450 1.00 16.61 ? 102 VAL   C CB  1 
ATOM   1848 C  CG1 . VAL   B 1 96  ? -0.428 -30.290 21.922 1.00 17.28 ? 102 VAL   C CG1 1 
ATOM   1849 C  CG2 . VAL   B 1 96  ? -1.071 -29.323 19.651 1.00 17.55 ? 102 VAL   C CG2 1 
ATOM   1850 N  N   . GLY   B 1 97  ? 3.079  -29.452 22.085 1.00 19.30 ? 103 GLY   C N   1 
ATOM   1851 C  CA  . GLY   B 1 97  ? 4.178  -30.081 22.825 1.00 20.23 ? 103 GLY   C CA  1 
ATOM   1852 C  C   . GLY   B 1 97  ? 4.832  -29.126 23.781 1.00 21.36 ? 103 GLY   C C   1 
ATOM   1853 O  O   . GLY   B 1 97  ? 4.494  -27.936 23.842 1.00 22.78 ? 103 GLY   C O   1 
ATOM   1854 N  N   . HIS   B 1 98  ? 5.776  -29.642 24.555 1.00 20.42 ? 104 HIS   C N   1 
ATOM   1855 C  CA  . HIS   B 1 98  ? 6.442  -28.863 25.586 1.00 20.07 ? 104 HIS   C CA  1 
ATOM   1856 C  C   . HIS   B 1 98  ? 7.666  -28.158 25.076 1.00 20.26 ? 104 HIS   C C   1 
ATOM   1857 O  O   . HIS   B 1 98  ? 8.490  -28.766 24.399 1.00 19.84 ? 104 HIS   C O   1 
ATOM   1858 C  CB  . HIS   B 1 98  ? 6.814  -29.787 26.774 1.00 20.62 ? 104 HIS   C CB  1 
ATOM   1859 C  CG  . HIS   B 1 98  ? 7.436  -29.044 27.900 1.00 20.91 ? 104 HIS   C CG  1 
ATOM   1860 N  ND1 . HIS   B 1 98  ? 6.699  -28.137 28.670 1.00 23.19 ? 104 HIS   C ND1 1 
ATOM   1861 C  CD2 . HIS   B 1 98  ? 8.729  -29.029 28.316 1.00 20.90 ? 104 HIS   C CD2 1 
ATOM   1862 C  CE1 . HIS   B 1 98  ? 7.565  -27.627 29.544 1.00 23.48 ? 104 HIS   C CE1 1 
ATOM   1863 N  NE2 . HIS   B 1 98  ? 8.798  -28.141 29.373 1.00 23.20 ? 104 HIS   C NE2 1 
ATOM   1864 N  N   . SER   B 1 99  ? 7.806  -26.859 25.408 1.00 21.07 ? 105 SER   C N   1 
ATOM   1865 C  CA  . SER   B 1 99  ? 8.967  -26.022 25.065 1.00 22.22 ? 105 SER   C CA  1 
ATOM   1866 C  C   . SER   B 1 99  ? 9.048  -24.937 26.120 1.00 24.87 ? 105 SER   C C   1 
ATOM   1867 O  O   . SER   B 1 99  ? 8.060  -24.268 26.386 1.00 27.11 ? 105 SER   C O   1 
ATOM   1868 C  CB  . SER   B 1 99  ? 8.789  -25.400 23.680 1.00 26.18 ? 105 SER   C CB  1 
ATOM   1869 O  OG  . SER   B 1 99  ? 9.910  -24.605 23.310 1.00 31.94 ? 105 SER   C OG  1 
ATOM   1870 N  N   . GLU   B 1 100 ? 10.197 -24.824 26.761 1.00 23.06 ? 106 GLU   C N   1 
ATOM   1871 C  CA  . GLU   B 1 100 ? 10.472 -23.823 27.778 1.00 24.83 ? 106 GLU   C CA  1 
ATOM   1872 C  C   . GLU   B 1 100 ? 11.686 -23.028 27.335 1.00 24.68 ? 106 GLU   C C   1 
ATOM   1873 O  O   . GLU   B 1 100 ? 12.435 -23.481 26.461 1.00 23.88 ? 106 GLU   C O   1 
ATOM   1874 C  CB  . GLU   B 1 100 ? 10.867 -24.576 29.049 1.00 29.02 ? 106 GLU   C CB  1 
ATOM   1875 C  CG  . GLU   B 1 100 ? 9.751  -24.808 30.009 1.00 36.88 ? 106 GLU   C CG  1 
ATOM   1876 C  CD  . GLU   B 1 100 ? 10.415 -25.584 31.120 1.00 39.13 ? 106 GLU   C CD  1 
ATOM   1877 O  OE1 . GLU   B 1 100 ? 11.330 -25.028 31.764 1.00 43.03 ? 106 GLU   C OE1 1 
ATOM   1878 O  OE2 . GLU   B 1 100 ? 10.092 -26.777 31.280 1.00 35.23 ? 106 GLU   C OE2 1 
ATOM   1879 N  N   . PRO   B 1 101 ? 11.974 -21.856 27.966 1.00 26.97 ? 107 PRO   C N   1 
ATOM   1880 C  CA  . PRO   B 1 101 ? 13.231 -21.168 27.673 1.00 28.35 ? 107 PRO   C CA  1 
ATOM   1881 C  C   . PRO   B 1 101 ? 14.360 -22.098 28.136 1.00 27.73 ? 107 PRO   C C   1 
ATOM   1882 O  O   . PRO   B 1 101 ? 14.362 -22.644 29.262 1.00 30.24 ? 107 PRO   C O   1 
ATOM   1883 C  CB  . PRO   B 1 101 ? 13.160 -19.911 28.561 1.00 29.52 ? 107 PRO   C CB  1 
ATOM   1884 C  CG  . PRO   B 1 101 ? 11.710 -19.744 28.876 1.00 29.88 ? 107 PRO   C CG  1 
ATOM   1885 C  CD  . PRO   B 1 101 ? 11.225 -21.165 29.028 1.00 27.36 ? 107 PRO   C CD  1 
ATOM   1886 N  N   . GLY   B 1 102 ? 15.256 -22.301 27.222 1.00 23.50 ? 108 GLY   C N   1 
ATOM   1887 C  CA  . GLY   B 1 102 ? 16.360 -23.231 27.288 1.00 21.45 ? 108 GLY   C CA  1 
ATOM   1888 C  C   . GLY   B 1 102 ? 16.229 -24.301 26.202 1.00 20.07 ? 108 GLY   C C   1 
ATOM   1889 O  O   . GLY   B 1 102 ? 17.222 -24.927 25.835 1.00 19.35 ? 108 GLY   C O   1 
ATOM   1890 N  N   . ASP   B 1 103 ? 15.004 -24.491 25.664 1.00 18.18 ? 109 ASP   C N   1 
ATOM   1891 C  CA  . ASP   B 1 103 ? 14.789 -25.530 24.645 1.00 17.17 ? 109 ASP   C CA  1 
ATOM   1892 C  C   . ASP   B 1 103 ? 15.151 -25.118 23.218 1.00 16.13 ? 109 ASP   C C   1 
ATOM   1893 O  O   . ASP   B 1 103 ? 15.269 -25.986 22.341 1.00 15.72 ? 109 ASP   C O   1 
ATOM   1894 C  CB  . ASP   B 1 103 ? 13.327 -26.065 24.689 1.00 17.84 ? 109 ASP   C CB  1 
ATOM   1895 C  CG  . ASP   B 1 103 ? 13.105 -26.970 25.909 1.00 20.00 ? 109 ASP   C CG  1 
ATOM   1896 O  OD1 . ASP   B 1 103 ? 14.055 -27.644 26.320 1.00 20.45 ? 109 ASP   C OD1 1 
ATOM   1897 O  OD2 . ASP   B 1 103 ? 11.972 -26.987 26.442 1.00 19.53 ? 109 ASP   C OD2 1 
ATOM   1898 N  N   . CYS   B 1 104 ? 15.316 -23.807 22.958 1.00 15.46 ? 110 CYS   C N   1 
ATOM   1899 C  CA  . CYS   B 1 104 ? 15.675 -23.348 21.596 1.00 15.89 ? 110 CYS   C CA  1 
ATOM   1900 C  C   . CYS   B 1 104 ? 16.953 -24.002 21.128 1.00 15.87 ? 110 CYS   C C   1 
ATOM   1901 O  O   . CYS   B 1 104 ? 17.896 -24.135 21.914 1.00 16.99 ? 110 CYS   C O   1 
ATOM   1902 C  CB  . CYS   B 1 104 ? 15.797 -21.824 21.549 1.00 16.72 ? 110 CYS   C CB  1 
ATOM   1903 S  SG  . CYS   B 1 104 ? 14.194 -20.984 21.710 1.00 21.05 ? 110 CYS   C SG  1 
ATOM   1904 N  N   . GLY   B 1 105 ? 16.955 -24.452 19.877 1.00 15.22 ? 111 GLY   C N   1 
ATOM   1905 C  CA  . GLY   B 1 105 ? 18.121 -25.123 19.322 1.00 16.29 ? 111 GLY   C CA  1 
ATOM   1906 C  C   . GLY   B 1 105 ? 17.959 -26.632 19.253 1.00 16.15 ? 111 GLY   C C   1 
ATOM   1907 O  O   . GLY   B 1 105 ? 18.715 -27.305 18.546 1.00 16.72 ? 111 GLY   C O   1 
ATOM   1908 N  N   . GLY   B 1 106 ? 16.946 -27.182 19.946 1.00 14.27 ? 112 GLY   C N   1 
ATOM   1909 C  CA  . GLY   B 1 106 ? 16.652 -28.611 19.840 1.00 13.43 ? 112 GLY   C CA  1 
ATOM   1910 C  C   . GLY   B 1 106 ? 16.267 -28.961 18.410 1.00 14.12 ? 112 GLY   C C   1 
ATOM   1911 O  O   . GLY   B 1 106 ? 15.508 -28.222 17.777 1.00 15.05 ? 112 GLY   C O   1 
ATOM   1912 N  N   . ILE   B 1 107 ? 16.805 -30.075 17.895 1.00 14.38 ? 113 ILE   C N   1 
ATOM   1913 C  CA  . ILE   B 1 107 ? 16.564 -30.438 16.490 1.00 14.35 ? 113 ILE   C CA  1 
ATOM   1914 C  C   . ILE   B 1 107 ? 15.265 -31.218 16.312 1.00 13.50 ? 113 ILE   C C   1 
ATOM   1915 O  O   . ILE   B 1 107 ? 14.979 -32.154 17.093 1.00 14.32 ? 113 ILE   C O   1 
ATOM   1916 C  CB  . ILE   B 1 107 ? 17.805 -31.178 15.881 1.00 16.82 ? 113 ILE   C CB  1 
ATOM   1917 C  CG1 . ILE   B 1 107 ? 18.967 -30.187 15.702 1.00 18.97 ? 113 ILE   C CG1 1 
ATOM   1918 C  CG2 . ILE   B 1 107 ? 17.471 -31.852 14.531 1.00 19.33 ? 113 ILE   C CG2 1 
ATOM   1919 C  CD1 . ILE   B 1 107 ? 20.306 -30.931 15.291 1.00 22.93 ? 113 ILE   C CD1 1 
ATOM   1920 N  N   . LEU   B 1 108 ? 14.519 -30.880 15.238 1.00 12.16 ? 114 LEU   C N   1 
ATOM   1921 C  CA  . LEU   B 1 108 ? 13.338 -31.636 14.780 1.00 12.65 ? 114 LEU   C CA  1 
ATOM   1922 C  C   . LEU   B 1 108 ? 13.816 -32.417 13.542 1.00 13.58 ? 114 LEU   C C   1 
ATOM   1923 O  O   . LEU   B 1 108 ? 14.419 -31.836 12.621 1.00 13.49 ? 114 LEU   C O   1 
ATOM   1924 C  CB  . LEU   B 1 108 ? 12.228 -30.630 14.359 1.00 12.80 ? 114 LEU   C CB  1 
ATOM   1925 C  CG  . LEU   B 1 108 ? 11.012 -31.252 13.650 1.00 13.30 ? 114 LEU   C CG  1 
ATOM   1926 C  CD1 . LEU   B 1 108 ? 10.223 -32.221 14.595 1.00 15.11 ? 114 LEU   C CD1 1 
ATOM   1927 C  CD2 . LEU   B 1 108 ? 10.078 -30.128 13.141 1.00 14.05 ? 114 LEU   C CD2 1 
ATOM   1928 N  N   . ARG   B 1 109 ? 13.554 -33.747 13.523 1.00 13.32 ? 115 ARG   C N   1 
ATOM   1929 C  CA  . ARG   B 1 109 ? 13.946 -34.608 12.404 1.00 14.32 ? 115 ARG   C CA  1 
ATOM   1930 C  C   . ARG   B 1 109 ? 12.747 -35.403 11.926 1.00 15.14 ? 115 ARG   C C   1 
ATOM   1931 O  O   . ARG   B 1 109 ? 11.901 -35.808 12.727 1.00 16.13 ? 115 ARG   C O   1 
ATOM   1932 C  CB  . ARG   B 1 109 ? 15.006 -35.651 12.876 1.00 16.30 ? 115 ARG   C CB  1 
ATOM   1933 C  CG  . ARG   B 1 109 ? 16.412 -35.120 13.048 1.00 21.80 ? 115 ARG   C CG  1 
ATOM   1934 C  CD  . ARG   B 1 109 ? 17.285 -36.155 13.811 1.00 25.22 ? 115 ARG   C CD  1 
ATOM   1935 N  NE  . ARG   B 1 109 ? 18.055 -35.561 14.909 1.00 33.15 ? 115 ARG   C NE  1 
ATOM   1936 C  CZ  . ARG   B 1 109 ? 19.271 -35.040 14.768 1.00 35.73 ? 115 ARG   C CZ  1 
ATOM   1937 N  NH1 . ARG   B 1 109 ? 19.893 -35.096 13.593 1.00 36.67 ? 115 ARG   C NH1 1 
ATOM   1938 N  NH2 . ARG   B 1 109 ? 19.892 -34.500 15.807 1.00 34.58 ? 115 ARG   C NH2 1 
ATOM   1939 N  N   . CYS   B 1 110 ? 12.728 -35.707 10.652 1.00 14.28 ? 116 CYS   C N   1 
ATOM   1940 C  CA  . CYS   B 1 110 ? 11.728 -36.629 10.077 1.00 15.39 ? 116 CYS   C CA  1 
ATOM   1941 C  C   . CYS   B 1 110 ? 12.504 -37.835 9.514  1.00 16.60 ? 116 CYS   C C   1 
ATOM   1942 O  O   . CYS   B 1 110 ? 13.725 -37.917 9.640  1.00 16.30 ? 116 CYS   C O   1 
ATOM   1943 C  CB  . CYS   B 1 110 ? 10.915 -35.935 8.979  1.00 15.31 ? 116 CYS   C CB  1 
ATOM   1944 S  SG  . CYS   B 1 110 ? 11.914 -35.451 7.540  1.00 14.54 ? 116 CYS   C SG  1 
ATOM   1945 N  N   . GLN   B 1 111 ? 11.786 -38.732 8.783  1.00 17.77 ? 117 GLN   C N   1 
ATOM   1946 C  CA  . GLN   B 1 111 ? 12.456 -39.876 8.199  1.00 19.37 ? 117 GLN   C CA  1 
ATOM   1947 C  C   . GLN   B 1 111 ? 13.532 -39.481 7.144  1.00 20.03 ? 117 GLN   C C   1 
ATOM   1948 O  O   . GLN   B 1 111 ? 14.383 -40.301 6.805  1.00 22.22 ? 117 GLN   C O   1 
ATOM   1949 C  CB  . GLN   B 1 111 ? 11.418 -40.834 7.588  1.00 21.36 ? 117 GLN   C CB  1 
ATOM   1950 C  CG  . GLN   B 1 111 ? 10.746 -40.258 6.330  1.00 25.29 ? 117 GLN   C CG  1 
ATOM   1951 C  CD  . GLN   B 1 111 ? 9.734  -41.223 5.747  1.00 34.34 ? 117 GLN   C CD  1 
ATOM   1952 O  OE1 . GLN   B 1 111 ? 8.530  -41.038 5.904  1.00 37.80 ? 117 GLN   C OE1 1 
ATOM   1953 N  NE2 . GLN   B 1 111 ? 10.199 -42.251 5.056  1.00 36.43 ? 117 GLN   C NE2 1 
ATOM   1954 N  N   . HIS   B 1 112 ? 13.527 -38.215 6.650  1.00 17.54 ? 118 HIS   C N   1 
ATOM   1955 C  CA  . HIS   B 1 112 ? 14.469 -37.764 5.607  1.00 17.44 ? 118 HIS   C CA  1 
ATOM   1956 C  C   . HIS   B 1 112 ? 15.663 -36.999 6.131  1.00 18.77 ? 118 HIS   C C   1 
ATOM   1957 O  O   . HIS   B 1 112 ? 16.592 -36.767 5.359  1.00 21.00 ? 118 HIS   C O   1 
ATOM   1958 C  CB  . HIS   B 1 112 ? 13.739 -36.872 4.579  1.00 16.51 ? 118 HIS   C CB  1 
ATOM   1959 C  CG  . HIS   B 1 112 ? 12.531 -37.556 3.995  1.00 16.78 ? 118 HIS   C CG  1 
ATOM   1960 N  ND1 . HIS   B 1 112 ? 11.245 -37.155 4.314  1.00 16.12 ? 118 HIS   C ND1 1 
ATOM   1961 C  CD2 . HIS   B 1 112 ? 12.457 -38.582 3.113  1.00 18.28 ? 118 HIS   C CD2 1 
ATOM   1962 C  CE1 . HIS   B 1 112 ? 10.428 -37.942 3.643  1.00 18.55 ? 118 HIS   C CE1 1 
ATOM   1963 N  NE2 . HIS   B 1 112 ? 11.100 -38.837 2.910  1.00 19.43 ? 118 HIS   C NE2 1 
ATOM   1964 N  N   . GLY   B 1 113 ? 15.658 -36.621 7.401  1.00 16.96 ? 119 GLY   C N   1 
ATOM   1965 C  CA  . GLY   B 1 113 ? 16.769 -35.855 7.953  1.00 16.35 ? 119 GLY   C CA  1 
ATOM   1966 C  C   . GLY   B 1 113 ? 16.319 -34.704 8.841  1.00 14.80 ? 119 GLY   C C   1 
ATOM   1967 O  O   . GLY   B 1 113 ? 15.200 -34.701 9.379  1.00 15.36 ? 119 GLY   C O   1 
ATOM   1968 N  N   . VAL   B 1 114 ? 17.180 -33.718 8.977  1.00 14.40 ? 120 VAL   C N   1 
ATOM   1969 C  CA  . VAL   B 1 114 ? 16.879 -32.535 9.806  1.00 14.38 ? 120 VAL   C CA  1 
ATOM   1970 C  C   . VAL   B 1 114 ? 15.866 -31.623 9.145  1.00 13.71 ? 120 VAL   C C   1 
ATOM   1971 O  O   . VAL   B 1 114 ? 16.049 -31.209 7.976  1.00 14.59 ? 120 VAL   C O   1 
ATOM   1972 C  CB  . VAL   B 1 114 ? 18.188 -31.751 10.084 1.00 15.78 ? 120 VAL   C CB  1 
ATOM   1973 C  CG1 . VAL   B 1 114 ? 17.873 -30.451 10.812 1.00 16.34 ? 120 VAL   C CG1 1 
ATOM   1974 C  CG2 . VAL   B 1 114 ? 19.146 -32.618 10.915 1.00 16.94 ? 120 VAL   C CG2 1 
ATOM   1975 N  N   . VAL   B 1 115 ? 14.798 -31.256 9.884  1.00 13.63 ? 121 VAL   C N   1 
ATOM   1976 C  CA  . VAL   B 1 115 ? 13.737 -30.395 9.394  1.00 12.72 ? 121 VAL   C CA  1 
ATOM   1977 C  C   . VAL   B 1 115 ? 13.919 -28.949 9.874  1.00 13.35 ? 121 VAL   C C   1 
ATOM   1978 O  O   . VAL   B 1 115 ? 13.645 -28.012 9.122  1.00 13.90 ? 121 VAL   C O   1 
ATOM   1979 C  CB  . VAL   B 1 115 ? 12.373 -30.933 9.891  1.00 13.23 ? 121 VAL   C CB  1 
ATOM   1980 C  CG1 . VAL   B 1 115 ? 11.230 -29.959 9.562  1.00 15.05 ? 121 VAL   C CG1 1 
ATOM   1981 C  CG2 . VAL   B 1 115 ? 12.115 -32.309 9.300  1.00 14.11 ? 121 VAL   C CG2 1 
ATOM   1982 N  N   . GLY   B 1 116 ? 14.315 -28.789 11.140 1.00 12.76 ? 122 GLY   C N   1 
ATOM   1983 C  CA  . GLY   B 1 116 ? 14.434 -27.436 11.691 1.00 14.67 ? 122 GLY   C CA  1 
ATOM   1984 C  C   . GLY   B 1 116 ? 14.846 -27.464 13.147 1.00 13.47 ? 122 GLY   C C   1 
ATOM   1985 O  O   . GLY   B 1 116 ? 15.274 -28.512 13.650 1.00 13.61 ? 122 GLY   C O   1 
ATOM   1986 N  N   . ILE   B 1 117 ? 14.784 -26.296 13.810 1.00 13.23 ? 123 ILE   C N   1 
ATOM   1987 C  CA  . ILE   B 1 117 ? 15.221 -26.216 15.194 1.00 13.96 ? 123 ILE   C CA  1 
ATOM   1988 C  C   . ILE   B 1 117 ? 14.167 -25.491 16.034 1.00 13.18 ? 123 ILE   C C   1 
ATOM   1989 O  O   . ILE   B 1 117 ? 13.507 -24.563 15.544 1.00 12.85 ? 123 ILE   C O   1 
ATOM   1990 C  CB  . ILE   B 1 117 ? 16.575 -25.490 15.331 1.00 15.39 ? 123 ILE   C CB  1 
ATOM   1991 C  CG1 . ILE   B 1 117 ? 16.558 -24.137 14.595 1.00 16.56 ? 123 ILE   C CG1 1 
ATOM   1992 C  CG2 . ILE   B 1 117 ? 17.777 -26.388 14.940 1.00 17.67 ? 123 ILE   C CG2 1 
ATOM   1993 C  CD1 . ILE   B 1 117 ? 17.893 -23.342 14.923 1.00 18.91 ? 123 ILE   C CD1 1 
ATOM   1994 N  N   . VAL   B 1 118 ? 14.055 -25.843 17.336 1.00 12.16 ? 124 VAL   C N   1 
ATOM   1995 C  CA  . VAL   B 1 118 ? 13.093 -25.146 18.207 1.00 12.43 ? 124 VAL   C CA  1 
ATOM   1996 C  C   . VAL   B 1 118 ? 13.460 -23.655 18.248 1.00 12.43 ? 124 VAL   C C   1 
ATOM   1997 O  O   . VAL   B 1 118 ? 14.637 -23.305 18.422 1.00 13.86 ? 124 VAL   C O   1 
ATOM   1998 C  CB  . VAL   B 1 118 ? 13.140 -25.716 19.637 1.00 13.11 ? 124 VAL   C CB  1 
ATOM   1999 C  CG1 . VAL   B 1 118 ? 12.233 -24.899 20.578 1.00 14.33 ? 124 VAL   C CG1 1 
ATOM   2000 C  CG2 . VAL   B 1 118 ? 12.713 -27.195 19.648 1.00 14.63 ? 124 VAL   C CG2 1 
ATOM   2001 N  N   . SER   B 1 119 ? 12.443 -22.795 18.092 1.00 12.62 ? 125 SER   C N   1 
ATOM   2002 C  CA  . SER   B 1 119 ? 12.641 -21.352 18.066 1.00 13.60 ? 125 SER   C CA  1 
ATOM   2003 C  C   . SER   B 1 119 ? 11.678 -20.612 18.968 1.00 15.30 ? 125 SER   C C   1 
ATOM   2004 O  O   . SER   B 1 119 ? 12.023 -19.525 19.457 1.00 15.55 ? 125 SER   C O   1 
ATOM   2005 C  CB  . SER   B 1 119 ? 12.513 -20.867 16.618 1.00 14.41 ? 125 SER   C CB  1 
ATOM   2006 O  OG  . SER   B 1 119 ? 12.690 -19.449 16.515 1.00 15.46 ? 125 SER   C OG  1 
ATOM   2007 N  N   . THR   B 1 120 ? 10.500 -21.167 19.256 1.00 15.38 ? 126 THR   C N   1 
ATOM   2008 C  CA  . THR   B 1 120 ? 9.512  -20.484 20.118 1.00 17.00 ? 126 THR   C CA  1 
ATOM   2009 C  C   . THR   B 1 120 ? 8.800  -21.505 21.025 1.00 17.65 ? 126 THR   C C   1 
ATOM   2010 O  O   . THR   B 1 120 ? 8.840  -22.725 20.770 1.00 15.67 ? 126 THR   C O   1 
ATOM   2011 C  CB  . THR   B 1 120 ? 8.424  -19.721 19.262 1.00 18.91 ? 126 THR   C CB  1 
ATOM   2012 O  OG1 . THR   B 1 120 ? 7.517  -20.667 18.657 1.00 20.83 ? 126 THR   C OG1 1 
ATOM   2013 C  CG2 . THR   B 1 120 ? 8.988  -18.764 18.225 1.00 20.22 ? 126 THR   C CG2 1 
ATOM   2014 N  N   . GLY   B 1 121 ? 8.148  -21.020 22.066 1.00 20.00 ? 127 GLY   C N   1 
ATOM   2015 C  CA  . GLY   B 1 121 ? 7.371  -21.896 22.950 1.00 22.51 ? 127 GLY   C CA  1 
ATOM   2016 C  C   . GLY   B 1 121 ? 6.316  -21.127 23.718 1.00 25.46 ? 127 GLY   C C   1 
ATOM   2017 O  O   . GLY   B 1 121 ? 6.338  -19.901 23.746 1.00 24.94 ? 127 GLY   C O   1 
ATOM   2018 N  N   . GLY   B 1 122 ? 5.401  -21.851 24.351 1.00 28.57 ? 128 GLY   C N   1 
ATOM   2019 C  CA  . GLY   B 1 122 ? 4.335  -21.263 25.162 1.00 30.14 ? 128 GLY   C CA  1 
ATOM   2020 C  C   . GLY   B 1 122 ? 2.966  -21.804 24.810 1.00 30.60 ? 128 GLY   C C   1 
ATOM   2021 O  O   . GLY   B 1 122 ? 2.769  -22.280 23.696 1.00 31.03 ? 128 GLY   C O   1 
ATOM   2022 N  N   . ASN   B 1 123 ? 1.993  -21.731 25.768 1.00 29.77 ? 129 ASN   C N   1 
ATOM   2023 C  CA  . ASN   B 1 123 ? 0.625  -22.221 25.578 1.00 29.61 ? 129 ASN   C CA  1 
ATOM   2024 C  C   . ASN   B 1 123 ? 0.520  -23.680 25.213 1.00 27.90 ? 129 ASN   C C   1 
ATOM   2025 O  O   . ASN   B 1 123 ? -0.439 -24.082 24.528 1.00 29.04 ? 129 ASN   C O   1 
ATOM   2026 C  CB  . ASN   B 1 123 ? -0.121 -21.365 24.554 1.00 32.03 ? 129 ASN   C CB  1 
ATOM   2027 C  CG  . ASN   B 1 123 ? -0.738 -20.141 25.165 1.00 34.86 ? 129 ASN   C CG  1 
ATOM   2028 O  OD1 . ASN   B 1 123 ? -0.963 -20.071 26.373 1.00 35.18 ? 129 ASN   C OD1 1 
ATOM   2029 N  ND2 . ASN   B 1 123 ? -1.037 -19.166 24.327 1.00 36.40 ? 129 ASN   C ND2 1 
ATOM   2030 N  N   . GLY   B 1 124 ? 1.499  -24.476 25.645 1.00 24.26 ? 130 GLY   C N   1 
ATOM   2031 C  CA  . GLY   B 1 124 ? 1.512  -25.881 25.279 1.00 22.20 ? 130 GLY   C CA  1 
ATOM   2032 C  C   . GLY   B 1 124 ? 1.767  -26.102 23.795 1.00 19.86 ? 130 GLY   C C   1 
ATOM   2033 O  O   . GLY   B 1 124 ? 1.407  -27.140 23.260 1.00 21.01 ? 130 GLY   C O   1 
ATOM   2034 N  N   . LEU   B 1 125 ? 2.459  -25.161 23.143 1.00 18.94 ? 131 LEU   C N   1 
ATOM   2035 C  CA  . LEU   B 1 125 ? 2.810  -25.256 21.747 1.00 17.77 ? 131 LEU   C CA  1 
ATOM   2036 C  C   . LEU   B 1 125 ? 4.343  -25.137 21.670 1.00 18.19 ? 131 LEU   C C   1 
ATOM   2037 O  O   . LEU   B 1 125 ? 4.975  -24.520 22.537 1.00 20.86 ? 131 LEU   C O   1 
ATOM   2038 C  CB  . LEU   B 1 125 ? 2.173  -24.091 20.950 1.00 19.51 ? 131 LEU   C CB  1 
ATOM   2039 C  CG  . LEU   B 1 125 ? 0.646  -24.057 20.976 1.00 22.38 ? 131 LEU   C CG  1 
ATOM   2040 C  CD1 . LEU   B 1 125 ? 0.142  -22.666 20.563 1.00 23.85 ? 131 LEU   C CD1 1 
ATOM   2041 C  CD2 . LEU   B 1 125 ? 0.061  -25.142 20.071 1.00 23.20 ? 131 LEU   C CD2 1 
ATOM   2042 N  N   . VAL   B 1 126 ? 4.918  -25.712 20.638 1.00 14.86 ? 132 VAL   C N   1 
ATOM   2043 C  CA  . VAL   B 1 126 ? 6.359  -25.568 20.361 1.00 14.32 ? 132 VAL   C CA  1 
ATOM   2044 C  C   . VAL   B 1 126 ? 6.488  -25.105 18.923 1.00 14.41 ? 132 VAL   C C   1 
ATOM   2045 O  O   . VAL   B 1 126 ? 5.761  -25.626 18.049 1.00 15.27 ? 132 VAL   C O   1 
ATOM   2046 C  CB  . VAL   B 1 126 ? 7.152  -26.868 20.658 1.00 16.80 ? 132 VAL   C CB  1 
ATOM   2047 C  CG1 . VAL   B 1 126 ? 6.554  -28.122 20.008 1.00 20.49 ? 132 VAL   C CG1 1 
ATOM   2048 C  CG2 . VAL   B 1 126 ? 8.652  -26.698 20.310 1.00 16.37 ? 132 VAL   C CG2 1 
ATOM   2049 N  N   . GLY   B 1 127 ? 7.356  -24.116 18.682 1.00 13.85 ? 133 GLY   C N   1 
ATOM   2050 C  CA  . GLY   B 1 127 ? 7.541  -23.626 17.322 1.00 13.67 ? 133 GLY   C CA  1 
ATOM   2051 C  C   . GLY   B 1 127 ? 8.929  -23.944 16.796 1.00 13.00 ? 133 GLY   C C   1 
ATOM   2052 O  O   . GLY   B 1 127 ? 9.907  -23.820 17.529 1.00 13.76 ? 133 GLY   C O   1 
ATOM   2053 N  N   . PHE   B 1 128 ? 9.001  -24.392 15.534 1.00 12.20 ? 134 PHE   C N   1 
ATOM   2054 C  CA  . PHE   B 1 128 ? 10.272 -24.787 14.916 1.00 12.91 ? 134 PHE   C CA  1 
ATOM   2055 C  C   . PHE   B 1 128 ? 10.545 -23.921 13.693 1.00 13.22 ? 134 PHE   C C   1 
ATOM   2056 O  O   . PHE   B 1 128 ? 9.666  -23.738 12.847 1.00 13.62 ? 134 PHE   C O   1 
ATOM   2057 C  CB  . PHE   B 1 128 ? 10.186 -26.238 14.392 1.00 13.68 ? 134 PHE   C CB  1 
ATOM   2058 C  CG  . PHE   B 1 128 ? 9.769  -27.225 15.450 1.00 13.44 ? 134 PHE   C CG  1 
ATOM   2059 C  CD1 . PHE   B 1 128 ? 10.696 -27.779 16.308 1.00 13.84 ? 134 PHE   C CD1 1 
ATOM   2060 C  CD2 . PHE   B 1 128 ? 8.447  -27.647 15.549 1.00 14.08 ? 134 PHE   C CD2 1 
ATOM   2061 C  CE1 . PHE   B 1 128 ? 10.310 -28.711 17.269 1.00 13.57 ? 134 PHE   C CE1 1 
ATOM   2062 C  CE2 . PHE   B 1 128 ? 8.064  -28.607 16.490 1.00 14.88 ? 134 PHE   C CE2 1 
ATOM   2063 C  CZ  . PHE   B 1 128 ? 8.995  -29.106 17.373 1.00 14.80 ? 134 PHE   C CZ  1 
ATOM   2064 N  N   . ALA   B 1 129 ? 11.777 -23.403 13.619 1.00 12.66 ? 135 ALA   C N   1 
ATOM   2065 C  CA  . ALA   B 1 129 ? 12.215 -22.669 12.436 1.00 12.01 ? 135 ALA   C CA  1 
ATOM   2066 C  C   . ALA   B 1 129 ? 12.587 -23.694 11.378 1.00 11.74 ? 135 ALA   C C   1 
ATOM   2067 O  O   . ALA   B 1 129 ? 13.535 -24.498 11.574 1.00 12.18 ? 135 ALA   C O   1 
ATOM   2068 C  CB  . ALA   B 1 129 ? 13.432 -21.811 12.796 1.00 12.83 ? 135 ALA   C CB  1 
ATOM   2069 N  N   . ASP   B 1 130 ? 11.882 -23.663 10.221 1.00 11.87 ? 136 ASP   C N   1 
ATOM   2070 C  CA  . ASP   B 1 130 ? 12.180 -24.597 9.135  1.00 12.54 ? 136 ASP   C CA  1 
ATOM   2071 C  C   . ASP   B 1 130 ? 13.515 -24.289 8.477  1.00 13.55 ? 136 ASP   C C   1 
ATOM   2072 O  O   . ASP   B 1 130 ? 13.856 -23.111 8.283  1.00 13.60 ? 136 ASP   C O   1 
ATOM   2073 C  CB  . ASP   B 1 130 ? 11.063 -24.469 8.068  1.00 13.76 ? 136 ASP   C CB  1 
ATOM   2074 C  CG  . ASP   B 1 130 ? 11.165 -25.507 6.968  1.00 20.19 ? 136 ASP   C CG  1 
ATOM   2075 O  OD1 . ASP   B 1 130 ? 11.246 -26.687 7.284  1.00 20.14 ? 136 ASP   C OD1 1 
ATOM   2076 O  OD2 . ASP   B 1 130 ? 11.199 -25.122 5.802  1.00 23.43 ? 136 ASP   C OD2 1 
ATOM   2077 N  N   . VAL   B 1 131 ? 14.243 -25.347 8.043  1.00 12.68 ? 137 VAL   C N   1 
ATOM   2078 C  CA  . VAL   B 1 131 ? 15.470 -25.120 7.243  1.00 13.20 ? 137 VAL   C CA  1 
ATOM   2079 C  C   . VAL   B 1 131 ? 15.420 -25.879 5.910  1.00 14.17 ? 137 VAL   C C   1 
ATOM   2080 O  O   . VAL   B 1 131 ? 16.385 -25.829 5.141  1.00 15.40 ? 137 VAL   C O   1 
ATOM   2081 C  CB  . VAL   B 1 131 ? 16.789 -25.499 7.997  1.00 14.21 ? 137 VAL   C CB  1 
ATOM   2082 C  CG1 . VAL   B 1 131 ? 16.939 -24.661 9.291  1.00 14.07 ? 137 VAL   C CG1 1 
ATOM   2083 C  CG2 . VAL   B 1 131 ? 16.836 -27.007 8.309  1.00 14.91 ? 137 VAL   C CG2 1 
ATOM   2084 N  N   . ARG   B 1 132 ? 14.306 -26.586 5.619  1.00 13.66 ? 138 ARG   C N   1 
ATOM   2085 C  CA  . ARG   B 1 132 ? 14.259 -27.441 4.429  1.00 12.70 ? 138 ARG   C CA  1 
ATOM   2086 C  C   . ARG   B 1 132 ? 14.313 -26.679 3.107  1.00 15.32 ? 138 ARG   C C   1 
ATOM   2087 O  O   . ARG   B 1 132 ? 14.647 -27.293 2.065  1.00 17.00 ? 138 ARG   C O   1 
ATOM   2088 C  CB  . ARG   B 1 132 ? 13.011 -28.329 4.454  1.00 12.79 ? 138 ARG   C CB  1 
ATOM   2089 C  CG  . ARG   B 1 132 ? 13.021 -29.307 5.618  1.00 13.62 ? 138 ARG   C CG  1 
ATOM   2090 C  CD  . ARG   B 1 132 ? 11.709 -30.076 5.662  1.00 13.20 ? 138 ARG   C CD  1 
ATOM   2091 N  NE  . ARG   B 1 132 ? 10.626 -29.171 6.082  1.00 13.52 ? 138 ARG   C NE  1 
ATOM   2092 C  CZ  . ARG   B 1 132 ? 9.382  -29.561 6.337  1.00 14.61 ? 138 ARG   C CZ  1 
ATOM   2093 N  NH1 . ARG   B 1 132 ? 8.998  -30.811 6.081  1.00 13.40 ? 138 ARG   C NH1 1 
ATOM   2094 N  NH2 . ARG   B 1 132 ? 8.499  -28.702 6.829  1.00 14.24 ? 138 ARG   C NH2 1 
ATOM   2095 N  N   . ASP   B 1 133 ? 13.947 -25.396 3.116  1.00 14.38 ? 139 ASP   C N   1 
ATOM   2096 C  CA  . ASP   B 1 133 ? 13.996 -24.600 1.881  1.00 15.29 ? 139 ASP   C CA  1 
ATOM   2097 C  C   . ASP   B 1 133 ? 15.387 -24.042 1.584  1.00 15.98 ? 139 ASP   C C   1 
ATOM   2098 O  O   . ASP   B 1 133 ? 15.589 -23.504 0.474  1.00 17.47 ? 139 ASP   C O   1 
ATOM   2099 C  CB  . ASP   B 1 133 ? 12.982 -23.446 1.954  1.00 16.96 ? 139 ASP   C CB  1 
ATOM   2100 C  CG  . ASP   B 1 133 ? 13.328 -22.435 3.031  1.00 19.94 ? 139 ASP   C CG  1 
ATOM   2101 O  OD1 . ASP   B 1 133 ? 13.657 -22.864 4.157  1.00 19.81 ? 139 ASP   C OD1 1 
ATOM   2102 O  OD2 . ASP   B 1 133 ? 13.331 -21.211 2.722  1.00 20.92 ? 139 ASP   C OD2 1 
ATOM   2103 N  N   . LEU   B 1 134 ? 16.345 -24.161 2.515  1.00 15.53 ? 140 LEU   C N   1 
ATOM   2104 C  CA  . LEU   B 1 134 ? 17.688 -23.606 2.324  1.00 16.60 ? 140 LEU   C CA  1 
ATOM   2105 C  C   . LEU   B 1 134 ? 18.554 -24.596 1.551  1.00 16.70 ? 140 LEU   C C   1 
ATOM   2106 O  O   . LEU   B 1 134 ? 19.401 -25.321 2.111  1.00 17.09 ? 140 LEU   C O   1 
ATOM   2107 C  CB  . LEU   B 1 134 ? 18.303 -23.260 3.700  1.00 16.65 ? 140 LEU   C CB  1 
ATOM   2108 C  CG  . LEU   B 1 134 ? 17.446 -22.315 4.559  1.00 17.86 ? 140 LEU   C CG  1 
ATOM   2109 C  CD1 . LEU   B 1 134 ? 18.111 -22.136 5.953  1.00 19.00 ? 140 LEU   C CD1 1 
ATOM   2110 C  CD2 . LEU   B 1 134 ? 17.235 -20.981 3.881  1.00 18.59 ? 140 LEU   C CD2 1 
ATOM   2111 N  N   . LEU   B 1 135 ? 18.313 -24.673 0.230  1.00 16.43 ? 141 LEU   C N   1 
ATOM   2112 C  CA  . LEU   B 1 135 ? 18.979 -25.712 -0.586 1.00 17.71 ? 141 LEU   C CA  1 
ATOM   2113 C  C   . LEU   B 1 135 ? 20.466 -25.558 -0.655 1.00 19.27 ? 141 LEU   C C   1 
ATOM   2114 O  O   . LEU   B 1 135 ? 21.181 -26.553 -0.813 1.00 21.14 ? 141 LEU   C O   1 
ATOM   2115 C  CB  . LEU   B 1 135 ? 18.369 -25.769 -1.982 1.00 17.57 ? 141 LEU   C CB  1 
ATOM   2116 C  CG  . LEU   B 1 135 ? 16.837 -25.777 -2.046 1.00 17.96 ? 141 LEU   C CG  1 
ATOM   2117 C  CD1 . LEU   B 1 135 ? 16.368 -25.934 -3.481 1.00 18.72 ? 141 LEU   C CD1 1 
ATOM   2118 C  CD2 . LEU   B 1 135 ? 16.216 -26.860 -1.150 1.00 18.57 ? 141 LEU   C CD2 1 
ATOM   2119 N  N   . TRP   B 1 136 ? 20.946 -24.302 -0.549 1.00 19.18 ? 142 TRP   C N   1 
ATOM   2120 C  CA  . TRP   B 1 136 ? 22.376 -24.016 -0.638 1.00 20.29 ? 142 TRP   C CA  1 
ATOM   2121 C  C   . TRP   B 1 136 ? 23.190 -24.617 0.530  1.00 22.23 ? 142 TRP   C C   1 
ATOM   2122 O  O   . TRP   B 1 136 ? 24.410 -24.679 0.435  1.00 23.71 ? 142 TRP   C O   1 
ATOM   2123 C  CB  . TRP   B 1 136 ? 22.603 -22.491 -0.719 1.00 20.72 ? 142 TRP   C CB  1 
ATOM   2124 C  CG  . TRP   B 1 136 ? 21.926 -21.703 0.368  1.00 20.68 ? 142 TRP   C CG  1 
ATOM   2125 C  CD1 . TRP   B 1 136 ? 20.695 -21.118 0.328  1.00 21.26 ? 142 TRP   C CD1 1 
ATOM   2126 C  CD2 . TRP   B 1 136 ? 22.484 -21.385 1.659  1.00 20.54 ? 142 TRP   C CD2 1 
ATOM   2127 N  NE1 . TRP   B 1 136 ? 20.458 -20.440 1.509  1.00 21.57 ? 142 TRP   C NE1 1 
ATOM   2128 C  CE2 . TRP   B 1 136 ? 21.549 -20.585 2.336  1.00 20.94 ? 142 TRP   C CE2 1 
ATOM   2129 C  CE3 . TRP   B 1 136 ? 23.701 -21.689 2.296  1.00 21.44 ? 142 TRP   C CE3 1 
ATOM   2130 C  CZ2 . TRP   B 1 136 ? 21.769 -20.133 3.648  1.00 21.90 ? 142 TRP   C CZ2 1 
ATOM   2131 C  CZ3 . TRP   B 1 136 ? 23.938 -21.176 3.570  1.00 22.99 ? 142 TRP   C CZ3 1 
ATOM   2132 C  CH2 . TRP   B 1 136 ? 23.000 -20.363 4.202  1.00 22.57 ? 142 TRP   C CH2 1 
ATOM   2133 N  N   . LEU   B 1 137 ? 22.526 -25.083 1.617  1.00 21.84 ? 143 LEU   C N   1 
ATOM   2134 C  CA  . LEU   B 1 137 ? 23.279 -25.701 2.728  1.00 22.73 ? 143 LEU   C CA  1 
ATOM   2135 C  C   . LEU   B 1 137 ? 24.034 -26.950 2.264  1.00 26.79 ? 143 LEU   C C   1 
ATOM   2136 O  O   . LEU   B 1 137 ? 25.066 -27.264 2.853  1.00 28.15 ? 143 LEU   C O   1 
ATOM   2137 C  CB  . LEU   B 1 137 ? 22.333 -26.104 3.883  1.00 20.70 ? 143 LEU   C CB  1 
ATOM   2138 C  CG  . LEU   B 1 137 ? 21.775 -24.954 4.712  1.00 20.63 ? 143 LEU   C CG  1 
ATOM   2139 C  CD1 . LEU   B 1 137 ? 20.737 -25.477 5.707  1.00 20.37 ? 143 LEU   C CD1 1 
ATOM   2140 C  CD2 . LEU   B 1 137 ? 22.922 -24.205 5.477  1.00 20.17 ? 143 LEU   C CD2 1 
ATOM   2141 N  N   . ASP   B 1 138 ? 23.489 -27.644 1.235  1.00 29.76 ? 144 ASP   C N   1 
ATOM   2142 C  CA  . ASP   B 1 138 ? 23.910 -28.914 0.620  1.00 34.02 ? 144 ASP   C CA  1 
ATOM   2143 C  C   . ASP   B 1 138 ? 24.996 -28.805 -0.415 1.00 37.06 ? 144 ASP   C C   1 
ATOM   2144 O  O   . ASP   B 1 138 ? 25.446 -29.850 -0.882 1.00 38.04 ? 144 ASP   C O   1 
ATOM   2145 C  CB  . ASP   B 1 138 ? 22.732 -29.506 -0.172 1.00 36.80 ? 144 ASP   C CB  1 
ATOM   2146 C  CG  . ASP   B 1 138 ? 21.620 -30.153 0.603  1.00 42.10 ? 144 ASP   C CG  1 
ATOM   2147 O  OD1 . ASP   B 1 138 ? 21.832 -30.473 1.785  1.00 43.24 ? 144 ASP   C OD1 1 
ATOM   2148 O  OD2 . ASP   B 1 138 ? 20.519 -30.353 0.012  1.00 45.52 ? 144 ASP   C OD2 1 
ATOM   2149 N  N   . GLU   B 1 139 ? 25.280 -27.603 -0.920 1.00 38.09 ? 145 GLU   C N   1 
ATOM   2150 C  CA  . GLU   B 1 139 ? 26.262 -27.457 -1.995 1.00 40.24 ? 145 GLU   C CA  1 
ATOM   2151 C  C   . GLU   B 1 139 ? 27.520 -26.707 -1.572 1.00 41.48 ? 145 GLU   C C   1 
ATOM   2152 O  O   . GLU   B 1 139 ? 27.481 -25.889 -0.657 1.00 42.37 ? 145 GLU   C O   1 
ATOM   2153 C  CB  . GLU   B 1 139 ? 25.612 -26.816 -3.228 1.00 43.75 ? 145 GLU   C CB  1 
ATOM   2154 C  CG  . GLU   B 1 139 ? 24.972 -25.472 -2.945 1.00 50.71 ? 145 GLU   C CG  1 
ATOM   2155 C  CD  . GLU   B 1 139 ? 23.832 -25.117 -3.880 1.00 60.66 ? 145 GLU   C CD  1 
ATOM   2156 O  OE1 . GLU   B 1 139 ? 23.826 -23.982 -4.411 1.00 62.85 ? 145 GLU   C OE1 1 
ATOM   2157 O  OE2 . GLU   B 1 139 ? 22.936 -25.971 -4.070 1.00 63.46 ? 145 GLU   C OE2 1 
HETATM 2158 N  N1  . A1B2J C 2 .   ? 25.238 13.764  10.559 1.00 19.71 ? 201 A1B2J A N1  1 
HETATM 2159 C  C4  . A1B2J C 2 .   ? 24.172 14.456  9.816  1.00 19.89 ? 201 A1B2J A C4  1 
HETATM 2160 C  C5  . A1B2J C 2 .   ? 25.981 12.745  10.074 1.00 20.55 ? 201 A1B2J A C5  1 
HETATM 2161 C  C6  . A1B2J C 2 .   ? 25.609 12.232  8.695  1.00 22.44 ? 201 A1B2J A C6  1 
HETATM 2162 C  C7  . A1B2J C 2 .   ? 26.662 11.313  8.118  1.00 23.96 ? 201 A1B2J A C7  1 
HETATM 2163 C  C8  . A1B2J C 2 .   ? 27.724 11.839  7.384  1.00 25.39 ? 201 A1B2J A C8  1 
HETATM 2164 C  C10 . A1B2J C 2 .   ? 28.562 9.623   6.942  1.00 26.34 ? 201 A1B2J A C10 1 
HETATM 2165 C  C13 . A1B2J C 2 .   ? 30.408 9.332   5.475  1.00 27.83 ? 201 A1B2J A C13 1 
HETATM 2166 C  C15 . A1B2J C 2 .   ? 25.420 14.214  11.944 1.00 18.76 ? 201 A1B2J A C15 1 
HETATM 2167 CL CL  . A1B2J C 2 .   ? 25.383 9.211   9.262  1.00 26.84 ? 201 A1B2J A CL  1 
HETATM 2168 C  C12 . A1B2J C 2 .   ? 26.594 9.929   8.242  1.00 25.21 ? 201 A1B2J A C12 1 
HETATM 2169 C  C11 . A1B2J C 2 .   ? 27.516 9.084   7.654  1.00 25.71 ? 201 A1B2J A C11 1 
HETATM 2170 O  O2  . A1B2J C 2 .   ? 29.530 8.765   6.477  1.00 27.18 ? 201 A1B2J A O2  1 
HETATM 2171 C  C14 . A1B2J C 2 .   ? 30.765 10.790  5.738  1.00 28.71 ? 201 A1B2J A C14 1 
HETATM 2172 O  O3  . A1B2J C 2 .   ? 29.599 11.598  5.982  1.00 27.77 ? 201 A1B2J A O3  1 
HETATM 2173 C  C9  . A1B2J C 2 .   ? 28.656 11.014  6.788  1.00 26.17 ? 201 A1B2J A C9  1 
HETATM 2174 O  O1  . A1B2J C 2 .   ? 26.889 12.244  10.717 1.00 19.50 ? 201 A1B2J A O1  1 
HETATM 2175 C  C3  . A1B2J C 2 .   ? 22.842 14.413  10.565 1.00 19.92 ? 201 A1B2J A C3  1 
HETATM 2176 C  C2  . A1B2J C 2 .   ? 23.012 14.902  12.007 1.00 18.85 ? 201 A1B2J A C2  1 
HETATM 2177 C  C1  . A1B2J C 2 .   ? 24.105 14.088  12.722 1.00 17.92 ? 201 A1B2J A C1  1 
HETATM 2178 C  C   . A1B2J C 2 .   ? 24.307 14.535  14.160 1.00 18.36 ? 201 A1B2J A C   1 
HETATM 2179 O  O   . A1B2J C 2 .   ? 24.825 15.620  14.422 1.00 18.36 ? 201 A1B2J A O   1 
HETATM 2180 N  N   . A1B2J C 2 .   ? 23.952 13.660  15.100 1.00 17.35 ? 201 A1B2J A N   1 
HETATM 2181 ZN ZN  . ZN    D 3 .   ? 23.243 -5.590  27.006 1.00 17.67 2 202 ZN    A ZN  1 
HETATM 2182 S  S   . DMS   E 4 .   ? 15.120 -0.282  12.240 1.00 38.57 ? 203 DMS   A S   1 
HETATM 2183 O  O   . DMS   E 4 .   ? 16.476 -0.608  12.795 1.00 33.70 ? 203 DMS   A O   1 
HETATM 2184 C  C1  . DMS   E 4 .   ? 15.096 0.354   10.549 1.00 39.21 ? 203 DMS   A C1  1 
HETATM 2185 C  C2  . DMS   E 4 .   ? 14.431 1.186   13.049 1.00 38.06 ? 203 DMS   A C2  1 
HETATM 2186 S  S   . DMS   F 4 .   ? 31.774 10.102  14.203 1.00 49.20 ? 204 DMS   A S   1 
HETATM 2187 O  O   . DMS   F 4 .   ? 30.623 9.189   13.838 1.00 48.79 ? 204 DMS   A O   1 
HETATM 2188 C  C1  . DMS   F 4 .   ? 31.218 11.284  15.460 1.00 49.12 ? 204 DMS   A C1  1 
HETATM 2189 C  C2  . DMS   F 4 .   ? 31.867 11.351  12.914 1.00 49.51 ? 204 DMS   A C2  1 
HETATM 2190 N  N1  . A1B2J G 2 .   ? 11.154 -16.666 22.642 1.00 19.30 ? 201 A1B2J C N1  1 
HETATM 2191 C  C4  . A1B2J G 2 .   ? 12.277 -15.930 23.255 1.00 18.70 ? 201 A1B2J C C4  1 
HETATM 2192 C  C5  . A1B2J G 2 .   ? 10.445 -17.667 23.209 1.00 22.28 ? 201 A1B2J C C5  1 
HETATM 2193 C  C6  . A1B2J G 2 .   ? 10.971 -18.146 24.550 1.00 26.20 ? 201 A1B2J C C6  1 
HETATM 2194 C  C7  . A1B2J G 2 .   ? 9.961  -19.005 25.273 1.00 30.24 ? 201 A1B2J C C7  1 
HETATM 2195 C  C8  . A1B2J G 2 .   ? 9.069  -18.414 26.162 1.00 32.63 ? 201 A1B2J C C8  1 
HETATM 2196 C  C10 . A1B2J G 2 .   ? 8.166  -20.572 26.737 1.00 35.92 ? 201 A1B2J C C10 1 
HETATM 2197 C  C13 . A1B2J G 2 .   ? 6.625  -20.717 28.550 1.00 38.48 ? 201 A1B2J C C13 1 
HETATM 2198 C  C15 . A1B2J G 2 .   ? 10.835 -16.254 21.272 1.00 17.80 ? 201 A1B2J C C15 1 
HETATM 2199 CL CL  . A1B2J G 2 .   ? 10.955 -21.165 23.980 1.00 34.63 ? 201 A1B2J C CL  1 
HETATM 2200 C  C12 . A1B2J G 2 .   ? 9.904  -20.385 25.122 1.00 32.90 ? 201 A1B2J C C12 1 
HETATM 2201 C  C11 . A1B2J G 2 .   ? 9.028  -21.175 25.844 1.00 34.29 ? 201 A1B2J C C11 1 
HETATM 2202 O  O2  . A1B2J G 2 .   ? 7.317  -21.377 27.461 1.00 38.09 ? 201 A1B2J C O2  1 
HETATM 2203 C  C14 . A1B2J G 2 .   ? 6.199  -19.302 28.199 1.00 38.32 ? 201 A1B2J C C14 1 
HETATM 2204 O  O3  . A1B2J G 2 .   ? 7.327  -18.517 27.739 1.00 37.60 ? 201 A1B2J C O3  1 
HETATM 2205 C  C9  . A1B2J G 2 .   ? 8.181  -19.175 26.888 1.00 35.51 ? 201 A1B2J C C9  1 
HETATM 2206 O  O1  . A1B2J G 2 .   ? 9.446  -18.163 22.674 1.00 20.68 ? 201 A1B2J C O1  1 
HETATM 2207 C  C3  . A1B2J G 2 .   ? 13.542 -16.059 22.407 1.00 17.22 ? 201 A1B2J C C3  1 
HETATM 2208 C  C2  . A1B2J G 2 .   ? 13.264 -15.628 20.964 1.00 16.32 ? 201 A1B2J C C2  1 
HETATM 2209 C  C1  . A1B2J G 2 .   ? 12.070 -16.412 20.376 1.00 15.85 ? 201 A1B2J C C1  1 
HETATM 2210 C  C   . A1B2J G 2 .   ? 11.746 -15.941 18.969 1.00 15.81 ? 201 A1B2J C C   1 
HETATM 2211 O  O   . A1B2J G 2 .   ? 11.291 -14.809 18.770 1.00 15.01 ? 201 A1B2J C O   1 
HETATM 2212 N  N   . A1B2J G 2 .   ? 11.923 -16.837 18.006 1.00 16.53 ? 201 A1B2J C N   1 
HETATM 2213 C  C1  . GOL   H 5 .   ? 15.214 -18.356 24.397 1.00 35.89 ? 202 GOL   C C1  1 
HETATM 2214 O  O1  . GOL   H 5 .   ? 16.459 -18.917 24.001 1.00 32.82 ? 202 GOL   C O1  1 
HETATM 2215 C  C2  . GOL   H 5 .   ? 15.241 -17.868 25.829 1.00 38.66 ? 202 GOL   C C2  1 
HETATM 2216 O  O2  . GOL   H 5 .   ? 16.498 -17.255 26.144 1.00 39.97 ? 202 GOL   C O2  1 
HETATM 2217 C  C3  . GOL   H 5 .   ? 14.105 -16.922 26.135 1.00 39.92 ? 202 GOL   C C3  1 
HETATM 2218 O  O3  . GOL   H 5 .   ? 14.050 -16.618 27.519 1.00 41.59 ? 202 GOL   C O3  1 
HETATM 2219 S  S   . DMS   I 4 .   ? 4.062  -20.406 19.814 1.00 43.93 ? 203 DMS   C S   1 
HETATM 2220 O  O   . DMS   I 4 .   ? 4.727  -19.397 18.894 1.00 43.75 ? 203 DMS   C O   1 
HETATM 2221 C  C1  . DMS   I 4 .   ? 3.825  -19.626 21.439 1.00 43.94 ? 203 DMS   C C1  1 
HETATM 2222 C  C2  . DMS   I 4 .   ? 5.212  -21.664 20.330 1.00 43.34 ? 203 DMS   C C2  1 
HETATM 2223 ZN ZN  . ZN    J 3 .   ? 10.603 -35.660 5.635  1.00 15.39 2 204 ZN    C ZN  1 
HETATM 2224 S  S   . DMS   K 4 .   ? 14.473 -10.127 7.714  1.00 83.05 ? 205 DMS   C S   1 
HETATM 2225 O  O   . DMS   K 4 .   ? 14.153 -9.076  8.736  1.00 82.94 ? 205 DMS   C O   1 
HETATM 2226 C  C1  . DMS   K 4 .   ? 13.142 -10.137 6.478  1.00 83.06 ? 205 DMS   C C1  1 
HETATM 2227 C  C2  . DMS   K 4 .   ? 15.705 -9.413  6.586  1.00 83.06 ? 205 DMS   C C2  1 
HETATM 2228 S  S   . DMS   L 4 .   ? 20.204 -31.124 19.695 1.00 43.89 ? 206 DMS   C S   1 
HETATM 2229 O  O   . DMS   L 4 .   ? 18.801 -31.490 19.332 1.00 39.77 ? 206 DMS   C O   1 
HETATM 2230 C  C1  . DMS   L 4 .   ? 20.328 -30.394 21.339 1.00 44.39 ? 206 DMS   C C1  1 
HETATM 2231 C  C2  . DMS   L 4 .   ? 20.893 -29.734 18.777 1.00 43.85 ? 206 DMS   C C2  1 
HETATM 2232 O  O   . HOH   M 6 .   ? 30.333 6.362   6.959  1.00 13.75 ? 301 HOH   A O   1 
HETATM 2233 O  O   . HOH   M 6 .   ? 15.105 22.096  24.472 1.00 25.09 ? 302 HOH   A O   1 
HETATM 2234 O  O   . HOH   M 6 .   ? 23.825 7.178   28.222 1.00 24.19 ? 303 HOH   A O   1 
HETATM 2235 O  O   . HOH   M 6 .   ? 11.712 -1.805  28.025 1.00 28.12 ? 304 HOH   A O   1 
HETATM 2236 O  O   . HOH   M 6 .   ? 22.315 8.404   3.080  1.00 28.58 ? 305 HOH   A O   1 
HETATM 2237 O  O   . HOH   M 6 .   ? 11.292 21.312  24.556 1.00 28.18 ? 306 HOH   A O   1 
HETATM 2238 O  O   . HOH   M 6 .   ? 6.402  3.016   28.984 1.00 43.06 ? 307 HOH   A O   1 
HETATM 2239 O  O   . HOH   M 6 .   ? 31.396 12.724  9.315  1.00 44.90 ? 308 HOH   A O   1 
HETATM 2240 O  O   . HOH   M 6 .   ? 34.539 -0.818  16.654 1.00 15.59 ? 309 HOH   A O   1 
HETATM 2241 O  O   . HOH   M 6 .   ? 7.003  15.515  29.124 1.00 40.29 ? 310 HOH   A O   1 
HETATM 2242 O  O   . HOH   M 6 .   ? 21.008 10.169  32.407 1.00 32.34 ? 311 HOH   A O   1 
HETATM 2243 O  O   . HOH   M 6 .   ? 15.066 8.590   13.454 1.00 15.77 ? 312 HOH   A O   1 
HETATM 2244 O  O   . HOH   M 6 .   ? 35.025 13.822  16.278 1.00 32.13 ? 313 HOH   A O   1 
HETATM 2245 O  O   . HOH   M 6 .   ? 16.147 -0.636  4.908  1.00 36.88 ? 314 HOH   A O   1 
HETATM 2246 O  O   . HOH   M 6 .   ? 11.052 -0.138  15.951 1.00 28.86 ? 315 HOH   A O   1 
HETATM 2247 O  O   . HOH   M 6 .   ? 16.249 -3.102  13.790 1.00 33.84 ? 316 HOH   A O   1 
HETATM 2248 O  O   . HOH   M 6 .   ? 22.517 6.542   1.618  1.00 30.31 ? 317 HOH   A O   1 
HETATM 2249 O  O   . HOH   M 6 .   ? 31.150 -5.353  11.525 1.00 36.18 ? 318 HOH   A O   1 
HETATM 2250 O  O   . HOH   M 6 .   ? 7.182  7.292   31.713 1.00 34.69 ? 319 HOH   A O   1 
HETATM 2251 O  O   . HOH   M 6 .   ? 27.161 18.970  15.052 1.00 19.61 ? 320 HOH   A O   1 
HETATM 2252 O  O   . HOH   M 6 .   ? 23.892 3.900   29.369 1.00 35.76 ? 321 HOH   A O   1 
HETATM 2253 O  O   . HOH   M 6 .   ? 24.706 23.989  10.602 1.00 37.97 ? 322 HOH   A O   1 
HETATM 2254 O  O   . HOH   M 6 .   ? 5.326  -2.300  26.079 1.00 54.33 ? 323 HOH   A O   1 
HETATM 2255 O  O   . HOH   M 6 .   ? 31.164 -2.118  29.800 1.00 44.69 ? 324 HOH   A O   1 
HETATM 2256 O  O   . HOH   M 6 .   ? 12.636 17.605  13.208 1.00 35.93 ? 325 HOH   A O   1 
HETATM 2257 O  O   . HOH   M 6 .   ? 25.759 17.691  12.802 1.00 19.38 ? 326 HOH   A O   1 
HETATM 2258 O  O   . HOH   M 6 .   ? 23.654 10.884  21.536 1.00 15.04 ? 327 HOH   A O   1 
HETATM 2259 O  O   . HOH   M 6 .   ? 18.848 -11.556 27.509 1.00 35.73 ? 328 HOH   A O   1 
HETATM 2260 O  O   . HOH   M 6 .   ? 16.761 -7.116  29.327 1.00 32.17 ? 329 HOH   A O   1 
HETATM 2261 O  O   . HOH   M 6 .   ? 4.913  11.045  12.427 1.00 43.79 ? 330 HOH   A O   1 
HETATM 2262 O  O   . HOH   M 6 .   ? 28.624 -6.225  3.620  1.00 32.86 ? 331 HOH   A O   1 
HETATM 2263 O  O   . HOH   M 6 .   ? 23.573 1.772   -0.874 1.00 18.44 ? 332 HOH   A O   1 
HETATM 2264 O  O   . HOH   M 6 .   ? 4.109  10.197  18.158 1.00 37.47 ? 333 HOH   A O   1 
HETATM 2265 O  O   . HOH   M 6 .   ? 20.182 11.876  8.653  1.00 21.74 ? 334 HOH   A O   1 
HETATM 2266 O  O   . HOH   M 6 .   ? 23.961 16.832  27.429 1.00 44.83 ? 335 HOH   A O   1 
HETATM 2267 O  O   . HOH   M 6 .   ? 34.831 -6.640  21.417 1.00 53.45 ? 336 HOH   A O   1 
HETATM 2268 O  O   . HOH   M 6 .   ? 20.324 2.182   9.377  1.00 15.00 ? 337 HOH   A O   1 
HETATM 2269 O  O   . HOH   M 6 .   ? 22.470 -6.033  0.593  1.00 37.14 ? 338 HOH   A O   1 
HETATM 2270 O  O   . HOH   M 6 .   ? 11.847 13.064  8.742  1.00 55.11 ? 339 HOH   A O   1 
HETATM 2271 O  O   . HOH   M 6 .   ? 24.175 14.288  30.429 1.00 51.84 ? 340 HOH   A O   1 
HETATM 2272 O  O   . HOH   M 6 .   ? 23.331 -10.986 30.952 1.00 46.61 ? 341 HOH   A O   1 
HETATM 2273 O  O   . HOH   M 6 .   ? 29.256 13.248  11.819 1.00 31.71 ? 342 HOH   A O   1 
HETATM 2274 O  O   . HOH   M 6 .   ? 18.221 16.360  28.763 1.00 50.12 ? 343 HOH   A O   1 
HETATM 2275 O  O   . HOH   M 6 .   ? 5.051  3.101   21.104 1.00 23.54 ? 344 HOH   A O   1 
HETATM 2276 O  O   . HOH   M 6 .   ? 19.980 -5.100  15.526 1.00 29.64 ? 345 HOH   A O   1 
HETATM 2277 O  O   . HOH   M 6 .   ? 21.694 17.864  28.004 1.00 54.07 ? 346 HOH   A O   1 
HETATM 2278 O  O   . HOH   M 6 .   ? 17.390 2.221   9.386  1.00 24.14 ? 347 HOH   A O   1 
HETATM 2279 O  O   . HOH   M 6 .   ? 4.360  3.942   28.197 1.00 40.84 ? 348 HOH   A O   1 
HETATM 2280 O  O   . HOH   M 6 .   ? 29.737 25.837  16.142 1.00 40.32 ? 349 HOH   A O   1 
HETATM 2281 O  O   . HOH   M 6 .   ? 31.384 4.274   7.493  1.00 21.36 ? 350 HOH   A O   1 
HETATM 2282 O  O   . HOH   M 6 .   ? 35.124 15.120  24.972 1.00 43.10 ? 351 HOH   A O   1 
HETATM 2283 O  O   . HOH   M 6 .   ? 16.480 18.482  27.325 1.00 47.04 ? 352 HOH   A O   1 
HETATM 2284 O  O   . HOH   M 6 .   ? 28.066 3.111   -0.466 1.00 29.12 ? 353 HOH   A O   1 
HETATM 2285 O  O   . HOH   M 6 .   ? 29.397 -6.913  25.410 1.00 38.77 ? 354 HOH   A O   1 
HETATM 2286 O  O   . HOH   M 6 .   ? 17.328 18.383  15.643 1.00 15.88 ? 355 HOH   A O   1 
HETATM 2287 O  O   . HOH   M 6 .   ? 32.200 2.711   5.353  1.00 31.08 ? 356 HOH   A O   1 
HETATM 2288 O  O   . HOH   M 6 .   ? 21.695 9.830   23.407 1.00 14.85 ? 357 HOH   A O   1 
HETATM 2289 O  O   . HOH   M 6 .   ? 16.892 4.520   5.978  1.00 29.37 ? 358 HOH   A O   1 
HETATM 2290 O  O   . HOH   M 6 .   ? 32.942 -2.595  15.190 1.00 22.04 ? 359 HOH   A O   1 
HETATM 2291 O  O   . HOH   M 6 .   ? 29.821 -2.246  8.691  1.00 29.53 ? 360 HOH   A O   1 
HETATM 2292 O  O   . HOH   M 6 .   ? 24.978 4.065   -1.254 1.00 26.28 ? 361 HOH   A O   1 
HETATM 2293 O  O   . HOH   M 6 .   ? 27.175 19.208  24.611 1.00 54.07 ? 362 HOH   A O   1 
HETATM 2294 O  O   . HOH   M 6 .   ? 25.693 1.578   29.962 1.00 26.07 ? 363 HOH   A O   1 
HETATM 2295 O  O   . HOH   M 6 .   ? 29.949 6.371   30.027 1.00 39.39 ? 364 HOH   A O   1 
HETATM 2296 O  O   . HOH   M 6 .   ? 23.092 20.799  20.499 1.00 25.98 ? 365 HOH   A O   1 
HETATM 2297 O  O   . HOH   M 6 .   ? 4.215  20.000  21.724 1.00 32.88 ? 366 HOH   A O   1 
HETATM 2298 O  O   . HOH   M 6 .   ? 29.654 -3.208  1.709  1.00 50.87 ? 367 HOH   A O   1 
HETATM 2299 O  O   . HOH   M 6 .   ? 34.553 3.886   26.204 1.00 27.08 ? 368 HOH   A O   1 
HETATM 2300 O  O   . HOH   M 6 .   ? 16.666 9.047   6.854  1.00 26.12 ? 369 HOH   A O   1 
HETATM 2301 O  O   . HOH   M 6 .   ? 4.318  20.296  15.360 1.00 45.74 ? 370 HOH   A O   1 
HETATM 2302 O  O   . HOH   M 6 .   ? 35.883 9.893   9.918  1.00 31.55 ? 371 HOH   A O   1 
HETATM 2303 O  O   . HOH   M 6 .   ? 28.300 16.063  10.795 1.00 35.29 ? 372 HOH   A O   1 
HETATM 2304 O  O   . HOH   M 6 .   ? 2.890  8.588   26.208 1.00 35.04 ? 373 HOH   A O   1 
HETATM 2305 O  O   . HOH   M 6 .   ? 32.004 14.779  12.792 1.00 32.65 ? 374 HOH   A O   1 
HETATM 2306 O  O   . HOH   M 6 .   ? 30.484 -5.894  26.396 1.00 32.21 ? 375 HOH   A O   1 
HETATM 2307 O  O   . HOH   M 6 .   ? 22.074 -5.590  33.659 1.00 37.48 ? 376 HOH   A O   1 
HETATM 2308 O  O   . HOH   M 6 .   ? 14.714 -3.983  16.188 1.00 30.11 ? 377 HOH   A O   1 
HETATM 2309 O  O   . HOH   M 6 .   ? 28.521 0.728   26.777 1.00 25.67 ? 378 HOH   A O   1 
HETATM 2310 O  O   . HOH   M 6 .   ? 8.904  3.969   11.934 1.00 43.54 ? 379 HOH   A O   1 
HETATM 2311 O  O   . HOH   M 6 .   ? 29.204 25.557  13.278 1.00 34.91 ? 380 HOH   A O   1 
HETATM 2312 O  O   . HOH   M 6 .   ? 17.991 19.836  13.453 1.00 26.08 ? 381 HOH   A O   1 
HETATM 2313 O  O   . HOH   M 6 .   ? 0.023  14.890  22.885 1.00 58.25 ? 382 HOH   A O   1 
HETATM 2314 O  O   . HOH   M 6 .   ? 3.484  18.048  23.617 1.00 39.76 ? 383 HOH   A O   1 
HETATM 2315 O  O   . HOH   M 6 .   ? 35.703 14.455  20.483 1.00 29.06 ? 384 HOH   A O   1 
HETATM 2316 O  O   . HOH   M 6 .   ? 25.668 20.487  21.946 1.00 44.35 ? 385 HOH   A O   1 
HETATM 2317 O  O   . HOH   M 6 .   ? 12.214 -2.685  15.925 1.00 34.97 ? 386 HOH   A O   1 
HETATM 2318 O  O   . HOH   M 6 .   ? 20.110 13.851  29.015 1.00 32.72 ? 387 HOH   A O   1 
HETATM 2319 O  O   . HOH   M 6 .   ? 0.840  17.479  23.041 1.00 55.75 ? 388 HOH   A O   1 
HETATM 2320 O  O   . HOH   M 6 .   ? 18.384 -5.299  30.598 1.00 24.61 ? 389 HOH   A O   1 
HETATM 2321 O  O   . HOH   M 6 .   ? 28.958 21.983  22.156 1.00 28.89 ? 390 HOH   A O   1 
HETATM 2322 O  O   . HOH   M 6 .   ? 30.628 -3.045  11.894 1.00 30.34 ? 391 HOH   A O   1 
HETATM 2323 O  O   . HOH   M 6 .   ? 3.347  2.481   19.006 1.00 36.94 ? 392 HOH   A O   1 
HETATM 2324 O  O   . HOH   M 6 .   ? 6.678  16.120  8.987  1.00 36.79 ? 393 HOH   A O   1 
HETATM 2325 O  O   . HOH   M 6 .   ? 11.173 2.259   12.418 1.00 33.05 ? 394 HOH   A O   1 
HETATM 2326 O  O   . HOH   M 6 .   ? 15.867 11.989  30.934 1.00 35.98 ? 395 HOH   A O   1 
HETATM 2327 O  O   . HOH   M 6 .   ? 32.495 -7.002  17.463 1.00 56.67 ? 396 HOH   A O   1 
HETATM 2328 O  O   . HOH   M 6 .   ? 28.070 11.866  27.678 1.00 25.64 ? 397 HOH   A O   1 
HETATM 2329 O  O   . HOH   M 6 .   ? 24.278 17.557  6.164  1.00 46.16 ? 398 HOH   A O   1 
HETATM 2330 O  O   . HOH   M 6 .   ? 24.956 -8.678  24.831 1.00 27.62 ? 399 HOH   A O   1 
HETATM 2331 O  O   . HOH   M 6 .   ? 13.409 8.584   11.167 1.00 21.18 ? 400 HOH   A O   1 
HETATM 2332 O  O   . HOH   M 6 .   ? 3.941  14.675  10.510 1.00 30.10 ? 401 HOH   A O   1 
HETATM 2333 O  O   . HOH   M 6 .   ? 12.402 18.394  26.641 1.00 31.31 ? 402 HOH   A O   1 
HETATM 2334 O  O   . HOH   M 6 .   ? 26.007 -8.484  22.654 1.00 42.12 ? 403 HOH   A O   1 
HETATM 2335 O  O   . HOH   M 6 .   ? 15.465 23.119  16.955 1.00 24.66 ? 404 HOH   A O   1 
HETATM 2336 O  O   . HOH   M 6 .   ? 26.549 -6.722  29.906 1.00 38.17 ? 405 HOH   A O   1 
HETATM 2337 O  O   . HOH   M 6 .   ? 19.804 -9.820  20.565 1.00 41.41 ? 406 HOH   A O   1 
HETATM 2338 O  O   . HOH   M 6 .   ? 11.600 10.455  9.602  1.00 50.25 ? 407 HOH   A O   1 
HETATM 2339 O  O   . HOH   M 6 .   ? 16.657 7.108   4.647  1.00 38.66 ? 408 HOH   A O   1 
HETATM 2340 O  O   . HOH   M 6 .   ? 33.265 8.140   3.850  1.00 46.44 ? 409 HOH   A O   1 
HETATM 2341 O  O   . HOH   M 6 .   ? 5.203  3.143   12.046 1.00 61.56 ? 410 HOH   A O   1 
HETATM 2342 O  O   . HOH   M 6 .   ? 4.500  10.429  15.232 1.00 54.08 ? 411 HOH   A O   1 
HETATM 2343 O  O   . HOH   M 6 .   ? 24.901 -5.175  32.726 1.00 38.06 ? 412 HOH   A O   1 
HETATM 2344 O  O   . HOH   M 6 .   ? 22.539 -8.716  19.538 1.00 42.15 ? 413 HOH   A O   1 
HETATM 2345 O  O   . HOH   M 6 .   ? 15.639 8.200   34.161 1.00 35.88 ? 414 HOH   A O   1 
HETATM 2346 O  O   . HOH   M 6 .   ? 28.285 16.634  8.178  1.00 61.19 ? 415 HOH   A O   1 
HETATM 2347 O  O   . HOH   M 6 .   ? 20.362 13.101  6.250  1.00 51.89 ? 416 HOH   A O   1 
HETATM 2348 O  O   . HOH   M 6 .   ? 2.512  14.537  24.843 1.00 50.69 ? 417 HOH   A O   1 
HETATM 2349 O  O   . HOH   M 6 .   ? 16.033 -5.898  5.587  1.00 52.57 ? 418 HOH   A O   1 
HETATM 2350 O  O   . HOH   M 6 .   ? 31.383 6.113   4.768  1.00 32.21 ? 419 HOH   A O   1 
HETATM 2351 O  O   . HOH   M 6 .   ? 30.091 -2.086  3.849  1.00 51.54 ? 420 HOH   A O   1 
HETATM 2352 O  O   . HOH   M 6 .   ? 10.960 6.475   11.315 1.00 49.25 ? 421 HOH   A O   1 
HETATM 2353 O  O   . HOH   M 6 .   ? 8.889  17.901  9.016  1.00 54.64 ? 422 HOH   A O   1 
HETATM 2354 O  O   . HOH   M 6 .   ? 1.646  15.825  9.264  1.00 65.87 ? 423 HOH   A O   1 
HETATM 2355 O  O   . HOH   M 6 .   ? 6.719  -1.030  28.080 1.00 51.18 ? 424 HOH   A O   1 
HETATM 2356 O  O   . HOH   M 6 .   ? 26.127 18.330  26.711 1.00 56.84 ? 425 HOH   A O   1 
HETATM 2357 O  O   . HOH   M 6 .   ? 18.262 11.066  6.669  1.00 41.00 ? 426 HOH   A O   1 
HETATM 2358 O  O   . HOH   M 6 .   ? 6.545  18.617  27.755 1.00 68.82 ? 427 HOH   A O   1 
HETATM 2359 O  O   . HOH   M 6 .   ? 2.176  20.993  8.893  1.00 55.48 ? 428 HOH   A O   1 
HETATM 2360 O  O   . HOH   M 6 .   ? 13.998 21.610  14.756 1.00 32.81 ? 429 HOH   A O   1 
HETATM 2361 O  O   . HOH   M 6 .   ? 29.971 6.769   2.492  1.00 51.52 ? 430 HOH   A O   1 
HETATM 2362 O  O   . HOH   M 6 .   ? 33.775 -2.234  9.162  1.00 36.08 ? 431 HOH   A O   1 
HETATM 2363 O  O   . HOH   M 6 .   ? 28.212 1.498   29.437 1.00 37.37 ? 432 HOH   A O   1 
HETATM 2364 O  O   . HOH   M 6 .   ? 9.006  -2.356  27.836 1.00 48.49 ? 433 HOH   A O   1 
HETATM 2365 O  O   . HOH   M 6 .   ? 25.153 -9.241  19.816 1.00 42.36 ? 434 HOH   A O   1 
HETATM 2366 O  O   . HOH   M 6 .   ? 31.842 25.480  11.936 1.00 47.44 ? 435 HOH   A O   1 
HETATM 2367 O  O   . HOH   M 6 .   ? 9.437  21.860  12.375 1.00 38.33 ? 436 HOH   A O   1 
HETATM 2368 O  O   . HOH   M 6 .   ? 25.427 14.848  6.295  1.00 51.32 ? 437 HOH   A O   1 
HETATM 2369 O  O   . HOH   M 6 .   ? 31.551 -3.955  9.712  1.00 45.31 ? 438 HOH   A O   1 
HETATM 2370 O  O   . HOH   M 6 .   ? 28.706 4.191   30.757 1.00 47.94 ? 439 HOH   A O   1 
HETATM 2371 O  O   . HOH   M 6 .   ? 31.141 -7.674  10.098 1.00 47.91 ? 440 HOH   A O   1 
HETATM 2372 O  O   . HOH   M 6 .   ? 36.165 11.775  17.284 1.00 61.40 ? 441 HOH   A O   1 
HETATM 2373 O  O   . HOH   M 6 .   ? 0.745  18.614  28.403 1.00 59.76 ? 442 HOH   A O   1 
HETATM 2374 O  O   . HOH   M 6 .   ? -0.379 16.819  30.197 1.00 78.60 ? 443 HOH   A O   1 
HETATM 2375 O  O   . HOH   N 6 .   ? 20.241 -8.452  7.719  1.00 24.59 ? 301 HOH   C O   1 
HETATM 2376 O  O   . HOH   N 6 .   ? 2.545  -22.935 10.619 1.00 33.43 ? 302 HOH   C O   1 
HETATM 2377 O  O   . HOH   N 6 .   ? 35.883 -14.865 15.551 1.00 38.51 ? 303 HOH   C O   1 
HETATM 2378 O  O   . HOH   N 6 .   ? 10.306 -22.955 4.783  1.00 21.82 ? 304 HOH   C O   1 
HETATM 2379 O  O   . HOH   N 6 .   ? 23.822 -9.240  7.892  1.00 22.77 ? 305 HOH   C O   1 
HETATM 2380 O  O   . HOH   N 6 .   ? 20.886 -27.455 -4.591 1.00 48.79 ? 306 HOH   C O   1 
HETATM 2381 O  O   . HOH   N 6 .   ? 17.044 -37.575 2.940  1.00 32.07 ? 307 HOH   C O   1 
HETATM 2382 O  O   . HOH   N 6 .   ? 10.512 -27.806 33.637 1.00 55.43 ? 308 HOH   C O   1 
HETATM 2383 O  O   . HOH   N 6 .   ? 20.723 -22.400 18.543 1.00 16.92 ? 309 HOH   C O   1 
HETATM 2384 O  O   . HOH   N 6 .   ? 5.682  -17.690 25.002 1.00 45.62 ? 310 HOH   C O   1 
HETATM 2385 O  O   . HOH   N 6 .   ? 23.786 -31.284 14.860 1.00 31.44 ? 311 HOH   C O   1 
HETATM 2386 O  O   . HOH   N 6 .   ? 4.594  -36.212 21.745 1.00 36.00 ? 312 HOH   C O   1 
HETATM 2387 O  O   . HOH   N 6 .   ? 23.787 -13.007 18.998 1.00 36.62 ? 313 HOH   C O   1 
HETATM 2388 O  O   . HOH   N 6 .   ? 12.428 -29.418 33.496 1.00 23.04 ? 314 HOH   C O   1 
HETATM 2389 O  O   . HOH   N 6 .   ? 12.361 -14.188 5.149  1.00 49.39 ? 315 HOH   C O   1 
HETATM 2390 O  O   . HOH   N 6 .   ? 19.224 -34.037 18.657 1.00 42.71 ? 316 HOH   C O   1 
HETATM 2391 O  O   . HOH   N 6 .   ? 10.655 -12.644 20.514 1.00 16.85 ? 317 HOH   C O   1 
HETATM 2392 O  O   . HOH   N 6 .   ? 26.599 -23.372 -0.490 1.00 40.51 ? 318 HOH   C O   1 
HETATM 2393 O  O   . HOH   N 6 .   ? 17.894 -7.605  21.504 1.00 21.83 ? 319 HOH   C O   1 
HETATM 2394 O  O   . HOH   N 6 .   ? 34.389 -10.908 10.242 1.00 47.58 ? 320 HOH   C O   1 
HETATM 2395 O  O   . HOH   N 6 .   ? 9.940  -26.222 3.695  1.00 20.86 ? 321 HOH   C O   1 
HETATM 2396 O  O   . HOH   N 6 .   ? 15.544 -21.421 24.685 1.00 33.65 ? 322 HOH   C O   1 
HETATM 2397 O  O   . HOH   N 6 .   ? 27.573 -27.513 1.861  1.00 43.63 ? 323 HOH   C O   1 
HETATM 2398 O  O   . HOH   N 6 .   ? 4.070  -23.436 3.759  1.00 41.76 ? 324 HOH   C O   1 
HETATM 2399 O  O   . HOH   N 6 .   ? 12.026 -20.287 0.522  1.00 36.80 ? 325 HOH   C O   1 
HETATM 2400 O  O   . HOH   N 6 .   ? 26.971 -27.261 19.127 1.00 43.67 ? 326 HOH   C O   1 
HETATM 2401 O  O   . HOH   N 6 .   ? 7.154  -36.956 29.205 1.00 37.04 ? 327 HOH   C O   1 
HETATM 2402 O  O   . HOH   N 6 .   ? 2.692  -31.278 3.977  1.00 36.53 ? 328 HOH   C O   1 
HETATM 2403 O  O   . HOH   N 6 .   ? 17.947 -10.003 9.195  1.00 20.66 ? 329 HOH   C O   1 
HETATM 2404 O  O   . HOH   N 6 .   ? 30.997 -21.036 12.927 1.00 37.45 ? 330 HOH   C O   1 
HETATM 2405 O  O   . HOH   N 6 .   ? 22.295 -12.334 17.259 1.00 26.76 ? 331 HOH   C O   1 
HETATM 2406 O  O   . HOH   N 6 .   ? 29.623 -27.873 9.673  1.00 29.87 ? 332 HOH   C O   1 
HETATM 2407 O  O   . HOH   N 6 .   ? 0.903  -16.609 17.963 1.00 32.12 ? 333 HOH   C O   1 
HETATM 2408 O  O   . HOH   N 6 .   ? -3.089 -18.773 27.528 1.00 33.61 ? 334 HOH   C O   1 
HETATM 2409 O  O   . HOH   N 6 .   ? 11.451 -19.486 11.560 1.00 14.62 ? 335 HOH   C O   1 
HETATM 2410 O  O   . HOH   N 6 .   ? 15.525 -28.709 23.141 1.00 16.96 ? 336 HOH   C O   1 
HETATM 2411 O  O   . HOH   N 6 .   ? 8.952  -11.416 18.410 1.00 18.36 ? 337 HOH   C O   1 
HETATM 2412 O  O   . HOH   N 6 .   ? 8.305  -28.394 3.137  1.00 23.65 ? 338 HOH   C O   1 
HETATM 2413 O  O   . HOH   N 6 .   ? 27.599 -15.288 2.313  1.00 44.39 ? 339 HOH   C O   1 
HETATM 2414 O  O   . HOH   N 6 .   ? 5.151  -25.483 25.126 1.00 34.08 ? 340 HOH   C O   1 
HETATM 2415 O  O   . HOH   N 6 .   ? 9.927  -40.717 1.246  1.00 43.72 ? 341 HOH   C O   1 
HETATM 2416 O  O   . HOH   N 6 .   ? 10.982 -35.711 -0.440 1.00 30.07 ? 342 HOH   C O   1 
HETATM 2417 O  O   . HOH   N 6 .   ? 34.669 -17.147 7.703  1.00 60.70 ? 343 HOH   C O   1 
HETATM 2418 O  O   . HOH   N 6 .   ? 18.141 -11.937 5.293  1.00 40.14 ? 344 HOH   C O   1 
HETATM 2419 O  O   . HOH   N 6 .   ? 20.063 -31.496 26.962 1.00 32.16 ? 345 HOH   C O   1 
HETATM 2420 O  O   . HOH   N 6 .   ? 22.237 -32.495 3.661  1.00 29.87 ? 346 HOH   C O   1 
HETATM 2421 O  O   . HOH   N 6 .   ? 0.985  -31.409 17.221 1.00 16.44 ? 347 HOH   C O   1 
HETATM 2422 O  O   . HOH   N 6 .   ? 26.710 -34.855 12.109 1.00 63.16 ? 348 HOH   C O   1 
HETATM 2423 O  O   . HOH   N 6 .   ? 18.594 -12.384 16.800 1.00 18.11 ? 349 HOH   C O   1 
HETATM 2424 O  O   . HOH   N 6 .   ? 4.939  -30.892 -1.673 1.00 37.91 ? 350 HOH   C O   1 
HETATM 2425 O  O   . HOH   N 6 .   ? 31.012 -20.075 18.812 1.00 39.52 ? 351 HOH   C O   1 
HETATM 2426 O  O   . HOH   N 6 .   ? 14.885 -20.007 0.693  1.00 46.85 ? 352 HOH   C O   1 
HETATM 2427 O  O   . HOH   N 6 .   ? 29.917 -9.995  10.070 1.00 43.07 ? 353 HOH   C O   1 
HETATM 2428 O  O   . HOH   N 6 .   ? 13.125 -20.619 9.413  1.00 13.92 ? 354 HOH   C O   1 
HETATM 2429 O  O   . HOH   N 6 .   ? 18.372 -28.625 22.904 1.00 27.25 ? 355 HOH   C O   1 
HETATM 2430 O  O   . HOH   N 6 .   ? 3.981  -27.658 27.987 1.00 40.33 ? 356 HOH   C O   1 
HETATM 2431 O  O   . HOH   N 6 .   ? 12.643 -6.145  22.131 1.00 22.52 ? 357 HOH   C O   1 
HETATM 2432 O  O   . HOH   N 6 .   ? 31.340 -10.646 16.096 1.00 29.90 ? 358 HOH   C O   1 
HETATM 2433 O  O   . HOH   N 6 .   ? 8.065  -5.404  14.512 1.00 40.66 ? 359 HOH   C O   1 
HETATM 2434 O  O   . HOH   N 6 .   ? 26.350 -32.885 5.650  1.00 46.89 ? 360 HOH   C O   1 
HETATM 2435 O  O   . HOH   N 6 .   ? 29.474 -33.883 4.821  1.00 60.96 ? 361 HOH   C O   1 
HETATM 2436 O  O   . HOH   N 6 .   ? 0.875  -29.299 25.064 1.00 48.10 ? 362 HOH   C O   1 
HETATM 2437 O  O   . HOH   N 6 .   ? 18.415 -10.924 18.913 1.00 28.98 ? 363 HOH   C O   1 
HETATM 2438 O  O   . HOH   N 6 .   ? 15.070 -35.697 16.938 1.00 25.79 ? 364 HOH   C O   1 
HETATM 2439 O  O   . HOH   N 6 .   ? 5.662  -29.151 7.402  1.00 16.48 ? 365 HOH   C O   1 
HETATM 2440 O  O   . HOH   N 6 .   ? 29.726 -26.569 2.600  1.00 44.72 ? 366 HOH   C O   1 
HETATM 2441 O  O   . HOH   N 6 .   ? 0.331  -18.852 21.796 1.00 48.98 ? 367 HOH   C O   1 
HETATM 2442 O  O   . HOH   N 6 .   ? 19.743 -22.045 25.267 1.00 37.73 ? 368 HOH   C O   1 
HETATM 2443 O  O   . HOH   N 6 .   ? 18.984 -36.567 11.265 1.00 36.25 ? 369 HOH   C O   1 
HETATM 2444 O  O   . HOH   N 6 .   ? 19.607 -27.012 25.526 1.00 46.47 ? 370 HOH   C O   1 
HETATM 2445 O  O   . HOH   N 6 .   ? -0.210 -15.653 14.163 1.00 28.01 ? 371 HOH   C O   1 
HETATM 2446 O  O   . HOH   N 6 .   ? 7.065  -38.935 7.304  1.00 46.30 ? 372 HOH   C O   1 
HETATM 2447 O  O   . HOH   N 6 .   ? 18.191 -18.603 1.224  1.00 35.45 ? 373 HOH   C O   1 
HETATM 2448 O  O   . HOH   N 6 .   ? 31.457 -28.515 11.429 1.00 48.92 ? 374 HOH   C O   1 
HETATM 2449 O  O   . HOH   N 6 .   ? 16.441 -7.624  14.490 1.00 46.65 ? 375 HOH   C O   1 
HETATM 2450 O  O   . HOH   N 6 .   ? -1.253 -35.345 15.880 1.00 48.69 ? 376 HOH   C O   1 
HETATM 2451 O  O   . HOH   N 6 .   ? 5.904  -38.850 28.084 1.00 55.07 ? 377 HOH   C O   1 
HETATM 2452 O  O   . HOH   N 6 .   ? 22.427 -14.851 23.239 1.00 56.18 ? 378 HOH   C O   1 
HETATM 2453 O  O   . HOH   N 6 .   ? 9.796  -10.028 11.190 1.00 41.11 ? 379 HOH   C O   1 
HETATM 2454 O  O   . HOH   N 6 .   ? 4.792  -30.523 30.918 1.00 51.44 ? 380 HOH   C O   1 
HETATM 2455 O  O   . HOH   N 6 .   ? 12.343 -9.720  12.533 1.00 30.55 ? 381 HOH   C O   1 
HETATM 2456 O  O   . HOH   N 6 .   ? 15.075 -35.578 1.647  1.00 24.33 ? 382 HOH   C O   1 
HETATM 2457 O  O   . HOH   N 6 .   ? 4.426  -8.377  22.766 1.00 32.34 ? 383 HOH   C O   1 
HETATM 2458 O  O   . HOH   N 6 .   ? 3.842  -36.212 7.067  1.00 28.87 ? 384 HOH   C O   1 
HETATM 2459 O  O   . HOH   N 6 .   ? 6.972  -16.552 22.599 1.00 41.13 ? 385 HOH   C O   1 
HETATM 2460 O  O   . HOH   N 6 .   ? 16.502 -38.138 10.634 1.00 35.70 ? 386 HOH   C O   1 
HETATM 2461 O  O   . HOH   N 6 .   ? 19.183 -30.171 -2.621 1.00 39.37 ? 387 HOH   C O   1 
HETATM 2462 O  O   . HOH   N 6 .   ? 14.328 -16.501 3.800  1.00 28.86 ? 388 HOH   C O   1 
HETATM 2463 O  O   . HOH   N 6 .   ? 8.036  -34.973 0.502  1.00 24.45 ? 389 HOH   C O   1 
HETATM 2464 O  O   . HOH   N 6 .   ? 28.877 -33.179 12.180 1.00 47.39 ? 390 HOH   C O   1 
HETATM 2465 O  O   . HOH   N 6 .   ? 8.491  -39.495 24.342 1.00 47.56 ? 391 HOH   C O   1 
HETATM 2466 O  O   . HOH   N 6 .   ? 1.647  -17.848 6.422  1.00 33.87 ? 392 HOH   C O   1 
HETATM 2467 O  O   . HOH   N 6 .   ? 6.317  -8.281  11.563 1.00 30.25 ? 393 HOH   C O   1 
HETATM 2468 O  O   . HOH   N 6 .   ? 21.817 -36.624 9.722  1.00 31.23 ? 394 HOH   C O   1 
HETATM 2469 O  O   . HOH   N 6 .   ? 26.574 -32.895 13.757 1.00 38.19 ? 395 HOH   C O   1 
HETATM 2470 O  O   . HOH   N 6 .   ? 19.449 -7.599  15.128 1.00 26.80 ? 396 HOH   C O   1 
HETATM 2471 O  O   . HOH   N 6 .   ? 29.470 -14.725 22.330 1.00 41.40 ? 397 HOH   C O   1 
HETATM 2472 O  O   . HOH   N 6 .   ? 18.948 -30.140 29.844 1.00 36.31 ? 398 HOH   C O   1 
HETATM 2473 O  O   . HOH   N 6 .   ? 4.130  -24.210 27.093 1.00 39.11 ? 399 HOH   C O   1 
HETATM 2474 O  O   . HOH   N 6 .   ? 8.377  -14.250 23.051 1.00 30.74 ? 400 HOH   C O   1 
HETATM 2475 O  O   . HOH   N 6 .   ? 1.048  -33.765 20.583 1.00 43.44 ? 401 HOH   C O   1 
HETATM 2476 O  O   . HOH   N 6 .   ? -2.184 -30.424 8.351  1.00 24.23 ? 402 HOH   C O   1 
HETATM 2477 O  O   . HOH   N 6 .   ? 6.523  -18.259 5.878  1.00 24.38 ? 403 HOH   C O   1 
HETATM 2478 O  O   . HOH   N 6 .   ? 8.802  -38.584 9.612  1.00 28.07 ? 404 HOH   C O   1 
HETATM 2479 O  O   . HOH   N 6 .   ? 5.946  -32.665 24.492 1.00 26.49 ? 405 HOH   C O   1 
HETATM 2480 O  O   . HOH   N 6 .   ? 4.729  -15.585 21.412 1.00 30.54 ? 406 HOH   C O   1 
HETATM 2481 O  O   . HOH   N 6 .   ? 17.073 -8.507  16.837 1.00 48.10 ? 407 HOH   C O   1 
HETATM 2482 O  O   . HOH   N 6 .   ? 10.714 -15.217 3.364  1.00 46.19 ? 408 HOH   C O   1 
HETATM 2483 O  O   . HOH   N 6 .   ? 1.814  -33.837 18.095 1.00 27.27 ? 409 HOH   C O   1 
HETATM 2484 O  O   . HOH   N 6 .   ? 17.123 -34.284 17.608 1.00 41.58 ? 410 HOH   C O   1 
HETATM 2485 O  O   . HOH   N 6 .   ? 24.367 -29.042 18.705 1.00 35.35 ? 411 HOH   C O   1 
HETATM 2486 O  O   . HOH   N 6 .   ? 21.733 -12.129 21.433 1.00 40.10 ? 412 HOH   C O   1 
HETATM 2487 O  O   . HOH   N 6 .   ? 22.459 -12.185 5.482  1.00 34.45 ? 413 HOH   C O   1 
HETATM 2488 O  O   . HOH   N 6 .   ? 17.932 -13.148 2.876  1.00 56.81 ? 414 HOH   C O   1 
HETATM 2489 O  O   . HOH   N 6 .   ? 32.520 -16.505 6.350  1.00 57.48 ? 415 HOH   C O   1 
HETATM 2490 O  O   . HOH   N 6 .   ? 28.066 -9.725  18.607 1.00 55.55 ? 416 HOH   C O   1 
HETATM 2491 O  O   . HOH   N 6 .   ? 22.575 -22.459 20.545 1.00 25.11 ? 417 HOH   C O   1 
HETATM 2492 O  O   . HOH   N 6 .   ? 4.455  -33.468 22.318 1.00 36.51 ? 418 HOH   C O   1 
HETATM 2493 O  O   . HOH   N 6 .   ? 5.908  -32.849 29.403 1.00 55.03 ? 419 HOH   C O   1 
HETATM 2494 O  O   . HOH   N 6 .   ? -0.461 -7.384  14.728 1.00 51.80 ? 420 HOH   C O   1 
HETATM 2495 O  O   . HOH   N 6 .   ? 30.722 -8.840  17.969 1.00 61.86 ? 421 HOH   C O   1 
HETATM 2496 O  O   . HOH   N 6 .   ? 21.493 -37.401 11.958 1.00 43.46 ? 422 HOH   C O   1 
HETATM 2497 O  O   . HOH   N 6 .   ? 12.218 -39.059 12.991 1.00 37.52 ? 423 HOH   C O   1 
HETATM 2498 O  O   . HOH   N 6 .   ? 7.020  -36.488 3.046  1.00 28.29 ? 424 HOH   C O   1 
HETATM 2499 O  O   . HOH   N 6 .   ? 32.886 -9.020  19.454 1.00 67.09 ? 425 HOH   C O   1 
HETATM 2500 O  O   . HOH   N 6 .   ? 13.931 -42.205 4.133  1.00 52.22 ? 426 HOH   C O   1 
HETATM 2501 O  O   . HOH   N 6 .   ? 20.798 -9.617  17.628 1.00 38.95 ? 427 HOH   C O   1 
HETATM 2502 O  O   . HOH   N 6 .   ? 1.920  -33.852 4.437  1.00 62.77 ? 428 HOH   C O   1 
HETATM 2503 O  O   . HOH   N 6 .   ? 24.785 -24.253 20.065 1.00 50.14 ? 429 HOH   C O   1 
HETATM 2504 O  O   . HOH   N 6 .   ? 31.551 -21.717 4.191  1.00 56.23 ? 430 HOH   C O   1 
HETATM 2505 O  O   . HOH   N 6 .   ? 29.398 -28.806 19.346 1.00 86.65 ? 431 HOH   C O   1 
HETATM 2506 O  O   . HOH   N 6 .   ? 5.585  -28.571 4.669  1.00 30.21 ? 432 HOH   C O   1 
HETATM 2507 O  O   . HOH   N 6 .   ? 22.289 -35.281 35.357 1.00 61.00 ? 433 HOH   C O   1 
HETATM 2508 O  O   . HOH   N 6 .   ? 17.248 -14.619 30.419 1.00 53.85 ? 434 HOH   C O   1 
HETATM 2509 O  O   . HOH   N 6 .   ? 17.754 -9.833  29.344 1.00 61.12 ? 435 HOH   C O   1 
HETATM 2510 O  O   . HOH   N 6 .   ? 17.208 -42.045 4.711  1.00 66.20 ? 436 HOH   C O   1 
HETATM 2511 O  O   . HOH   N 6 .   ? 30.796 -30.935 13.223 1.00 53.27 ? 437 HOH   C O   1 
HETATM 2512 O  O   . HOH   N 6 .   ? 16.039 -17.391 1.728  1.00 59.27 ? 438 HOH   C O   1 
HETATM 2513 O  O   . HOH   N 6 .   ? -0.610 -34.690 10.093 1.00 65.64 ? 439 HOH   C O   1 
HETATM 2514 O  O   . HOH   N 6 .   ? 31.685 -24.813 15.053 1.00 59.96 ? 440 HOH   C O   1 
HETATM 2515 O  O   . HOH   N 6 .   ? 8.689  -23.658 2.700  1.00 38.55 ? 441 HOH   C O   1 
HETATM 2516 O  O   . HOH   N 6 .   ? 32.463 -27.137 13.500 1.00 53.11 ? 442 HOH   C O   1 
HETATM 2517 O  O   . HOH   N 6 .   ? -1.966 -16.629 28.871 1.00 48.57 ? 443 HOH   C O   1 
HETATM 2518 O  O   . HOH   N 6 .   ? -1.259 -19.417 11.880 1.00 41.16 ? 444 HOH   C O   1 
HETATM 2519 O  O   . HOH   N 6 .   ? 33.121 -8.965  11.620 1.00 44.17 ? 445 HOH   C O   1 
HETATM 2520 O  O   . HOH   N 6 .   ? 5.477  -39.454 23.379 1.00 39.16 ? 446 HOH   C O   1 
HETATM 2521 O  O   . HOH   N 6 .   ? 35.565 -9.315  8.308  1.00 67.25 ? 447 HOH   C O   1 
HETATM 2522 O  O   . HOH   N 6 .   ? 35.578 -10.237 15.420 1.00 37.00 ? 448 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   ? 0.2596 0.2469 0.2571 -0.0003 -0.0130 0.0125  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.2630 0.2524 0.2696 -0.0016 -0.0147 0.0117  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.2551 0.2447 0.2634 -0.0031 -0.0143 0.0085  7   SER   A C   
4    O  O   . SER   A 1   ? 0.2675 0.2551 0.2694 -0.0030 -0.0140 0.0068  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.3066 0.2963 0.3135 -0.0010 -0.0199 0.0130  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.3611 0.3490 0.3613 -0.0011 -0.0233 0.0108  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.2324 0.2239 0.2491 -0.0042 -0.0137 0.0078  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.2284 0.2196 0.2471 -0.0056 -0.0127 0.0055  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.2076 0.2006 0.2338 -0.0061 -0.0095 0.0052  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.2136 0.2076 0.2425 -0.0055 -0.0075 0.0060  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.1885 0.1814 0.2182 -0.0073 -0.0088 0.0041  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.1981 0.1922 0.2336 -0.0075 -0.0052 0.0038  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.2021 0.1943 0.2360 -0.0082 -0.0027 0.0027  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.2194 0.2096 0.2507 -0.0091 -0.0044 0.0022  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.2100 0.2069 0.2557 -0.0080 -0.0062 0.0048  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.1776 0.1698 0.2123 -0.0076 0.0013  0.0023  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.1817 0.1718 0.2151 -0.0079 0.0046  0.0021  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.1901 0.1820 0.2330 -0.0088 0.0069  0.0028  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.1964 0.1904 0.2438 -0.0081 0.0083  0.0028  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.1850 0.1737 0.2115 -0.0061 0.0076  0.0012  10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.1922 0.1803 0.2114 -0.0051 0.0053  0.0005  10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.2111 0.1968 0.2346 -0.0058 0.0111  0.0017  10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.2236 0.2121 0.2386 -0.0034 0.0069  -0.0009 10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.1876 0.1785 0.2344 -0.0104 0.0077  0.0034  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.2018 0.1950 0.2592 -0.0114 0.0108  0.0042  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.2071 0.1971 0.2614 -0.0112 0.0166  0.0050  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.2220 0.2087 0.2740 -0.0123 0.0167  0.0054  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.2029 0.1982 0.2698 -0.0139 0.0070  0.0044  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.2254 0.2240 0.2951 -0.0136 0.0012  0.0042  11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2580 0.2611 0.3375 -0.0130 0.0010  0.0050  11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2524 0.2493 0.3144 -0.0135 -0.0037 0.0035  11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2641 0.2696 0.3454 -0.0122 -0.0044 0.0055  11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2745 0.2737 0.3372 -0.0127 -0.0086 0.0038  11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2824 0.2858 0.3546 -0.0121 -0.0091 0.0050  11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.3240 0.3291 0.3959 -0.0109 -0.0139 0.0060  11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.1994 0.1894 0.2524 -0.0094 0.0215  0.0051  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.2135 0.1998 0.2612 -0.0084 0.0275  0.0061  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2289 0.2173 0.2845 -0.0080 0.0332  0.0068  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2294 0.2203 0.2873 -0.0066 0.0334  0.0056  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2399 0.2232 0.2735 -0.0056 0.0278  0.0050  12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2389 0.2247 0.2717 -0.0042 0.0261  0.0028  12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.2672 0.2465 0.2939 -0.0038 0.0340  0.0063  12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2480 0.2353 0.3092 -0.0093 0.0380  0.0089  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2508 0.2405 0.3209 -0.0089 0.0443  0.0099  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2421 0.2380 0.3259 -0.0097 0.0411  0.0090  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2447 0.2434 0.3357 -0.0120 0.0353  0.0089  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2448 0.2426 0.3308 -0.0074 0.0443  0.0082  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2516 0.2551 0.3504 -0.0076 0.0411  0.0077  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2211 0.2240 0.3130 -0.0059 0.0363  0.0057  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2186 0.2241 0.3171 -0.0044 0.0363  0.0051  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2960 0.3024 0.4059 -0.0063 0.0479  0.0083  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3848 0.3931 0.5056 -0.0086 0.0524  0.0107  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.4244 0.4366 0.5571 -0.0114 0.0481  0.0115  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.4063 0.4113 0.5227 -0.0073 0.0611  0.0118  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.2046 0.2042 0.2843 -0.0061 0.0323  0.0048  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.1963 0.1953 0.2699 -0.0049 0.0282  0.0031  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.1773 0.1767 0.2489 -0.0065 0.0213  0.0036  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.1801 0.1783 0.2491 -0.0080 0.0200  0.0043  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.2135 0.2083 0.2734 -0.0031 0.0304  0.0012  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.2206 0.2139 0.2790 -0.0009 0.0370  0.0001  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2290 0.2240 0.2950 0.0004  0.0388  -0.0009 15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.2416 0.2312 0.2903 0.0003  0.0415  0.0002  15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.2377 0.2306 0.3010 0.0027  0.0451  -0.0025 15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.2494 0.2371 0.2945 0.0028  0.0476  -0.0011 15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.2628 0.2522 0.3155 0.0039  0.0496  -0.0026 15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.3077 0.2946 0.3561 0.0066  0.0559  -0.0044 15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.1680 0.1686 0.2401 -0.0058 0.0174  0.0032  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1803 0.1807 0.2484 -0.0066 0.0116  0.0036  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1840 0.1823 0.2438 -0.0053 0.0114  0.0022  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1857 0.1842 0.2485 -0.0041 0.0128  0.0015  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.2014 0.2054 0.2791 -0.0069 0.0074  0.0051  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.2188 0.2222 0.2914 -0.0068 0.0020  0.0058  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.2262 0.2330 0.3071 -0.0067 -0.0027 0.0075  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.2460 0.2520 0.3235 -0.0052 -0.0055 0.0089  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.2777 0.2831 0.3497 -0.0052 -0.0103 0.0099  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.2985 0.3037 0.3673 -0.0066 -0.0134 0.0091  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.2678 0.2721 0.3369 -0.0036 -0.0117 0.0118  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.1802 0.1763 0.2305 -0.0055 0.0098  0.0016  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.1788 0.1738 0.2230 -0.0047 0.0093  0.0002  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.1790 0.1745 0.2220 -0.0051 0.0052  0.0015  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.1812 0.1763 0.2208 -0.0058 0.0029  0.0022  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.1849 0.1778 0.2198 -0.0041 0.0106  -0.0013 17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.1904 0.1831 0.2213 -0.0033 0.0100  -0.0033 17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.1863 0.1779 0.2201 -0.0034 0.0149  -0.0017 17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.1583 0.1541 0.2037 -0.0046 0.0046  0.0017  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.1681 0.1639 0.2116 -0.0047 0.0016  0.0035  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.1565 0.1515 0.1983 -0.0045 0.0026  0.0027  18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.1690 0.1635 0.2126 -0.0043 0.0049  0.0005  18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.1873 0.1842 0.2375 -0.0043 -0.0005 0.0061  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.2211 0.2197 0.2743 -0.0049 -0.0026 0.0067  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.1921 0.1891 0.2498 -0.0035 0.0019  0.0059  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.1461 0.1408 0.1850 -0.0045 0.0011  0.0044  19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.1458 0.1399 0.1857 -0.0046 0.0023  0.0043  19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.1584 0.1516 0.2057 -0.0043 0.0032  0.0053  19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.1714 0.1645 0.2214 -0.0036 0.0017  0.0081  19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.1536 0.1474 0.1895 -0.0045 0.0014  0.0068  19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.1802 0.1747 0.2093 -0.0044 0.0009  0.0056  19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.1986 0.1926 0.2234 -0.0041 -0.0009 0.0063  19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.1802 0.1757 0.2088 -0.0047 0.0023  0.0038  19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.1508 0.1431 0.2017 -0.0047 0.0053  0.0030  20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.1458 0.1362 0.2041 -0.0042 0.0066  0.0036  20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.1625 0.1516 0.2228 -0.0037 0.0058  0.0082  20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.1762 0.1645 0.2413 -0.0024 0.0054  0.0107  20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.1576 0.1466 0.2186 -0.0049 0.0087  -0.0003 20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.1815 0.1677 0.2501 -0.0042 0.0105  -0.0007 20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.1787 0.1628 0.2493 -0.0054 0.0120  -0.0051 20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.1971 0.1777 0.2745 -0.0047 0.0141  -0.0068 20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.1980 0.1753 0.2821 -0.0047 0.0151  -0.0043 20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.2097 0.1871 0.2940 -0.0052 0.0143  0.0005  20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.1960 0.1694 0.2861 -0.0039 0.0172  -0.0064 20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.1605 0.1495 0.2166 -0.0044 0.0057  0.0097  21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.1721 0.1591 0.2285 -0.0036 0.0057  0.0146  21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.1871 0.1746 0.2394 -0.0019 0.0025  0.0180  21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.2208 0.2064 0.2728 -0.0006 0.0020  0.0224  21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.1768 0.1634 0.2306 -0.0046 0.0075  0.0155  21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.1939 0.1826 0.2394 -0.0045 0.0064  0.0155  21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.1963 0.1875 0.2395 -0.0053 0.0061  0.0115  21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.2019 0.1898 0.2407 -0.0033 0.0057  0.0191  21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.1957 0.1876 0.2318 -0.0047 0.0054  0.0127  21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.2093 0.1992 0.2421 -0.0035 0.0052  0.0170  21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.1746 0.1646 0.2238 -0.0020 0.0003  0.0161  22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.1819 0.1728 0.2282 -0.0008 -0.0036 0.0184  22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.1939 0.1868 0.2475 -0.0003 -0.0050 0.0177  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.2170 0.2115 0.2702 0.0004  -0.0088 0.0189  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.1872 0.1790 0.2251 -0.0014 -0.0051 0.0169  22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.1995 0.1899 0.2303 -0.0014 -0.0035 0.0178  22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.2042 0.1951 0.2273 -0.0016 -0.0049 0.0160  22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.2134 0.2015 0.2414 0.0002  -0.0038 0.0226  22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.1846 0.1774 0.2452 -0.0006 -0.0021 0.0156  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.1883 0.1833 0.2565 0.0000  -0.0023 0.0148  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.1953 0.1909 0.2690 0.0021  -0.0052 0.0187  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.1917 0.1846 0.2654 0.0033  -0.0050 0.0217  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.1876 0.1815 0.2609 -0.0001 0.0019  0.0119  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.2032 0.2023 0.2818 0.0025  -0.0078 0.0189  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.2258 0.2266 0.3104 0.0048  -0.0116 0.0225  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.2445 0.2457 0.3407 0.0064  -0.0089 0.0227  24  THR   A C   
137  O  O   . THR   A 18  ? 0.2386 0.2391 0.3378 0.0056  -0.0042 0.0196  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.2386 0.2438 0.3249 0.0042  -0.0164 0.0220  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.2329 0.2411 0.3273 0.0029  -0.0137 0.0192  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.2513 0.2555 0.3261 0.0026  -0.0189 0.0210  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.2533 0.2560 0.3565 0.0092  -0.0121 0.0263  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.2649 0.2685 0.3805 0.0112  -0.0096 0.0266  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.2284 0.2364 0.3515 0.0100  -0.0072 0.0231  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.2381 0.2452 0.3673 0.0106  -0.0020 0.0210  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.3175 0.3232 0.4396 0.0147  -0.0146 0.0313  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.4231 0.4240 0.5379 0.0166  -0.0165 0.0359  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.4704 0.4652 0.5845 0.0172  -0.0118 0.0369  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.4620 0.4633 0.5705 0.0183  -0.0225 0.0397  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.4873 0.4788 0.5947 0.0190  -0.0144 0.0418  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 0.4878 0.4829 0.5907 0.0199  -0.0209 0.0437  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.2270 0.2392 0.3493 0.0082  -0.0106 0.0222  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.2176 0.2337 0.3473 0.0068  -0.0077 0.0194  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.2014 0.2142 0.3246 0.0050  -0.0015 0.0158  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.2089 0.2228 0.3382 0.0052  0.0035  0.0139  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.2511 0.2717 0.3819 0.0050  -0.0126 0.0193  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.3224 0.3483 0.4647 0.0069  -0.0181 0.0218  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.3197 0.3482 0.4743 0.0093  -0.0162 0.0229  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.3390 0.3667 0.4773 0.0063  -0.0252 0.0226  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.1826 0.1915 0.2932 0.0035  -0.0017 0.0149  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.1801 0.1859 0.2840 0.0022  0.0033  0.0115  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.1775 0.1806 0.2853 0.0039  0.0080  0.0101  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.1846 0.1871 0.2929 0.0039  0.0128  0.0072  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.1654 0.1680 0.2570 0.0009  0.0017  0.0112  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.2113 0.2153 0.2969 -0.0008 -0.0014 0.0111  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.2284 0.2343 0.3164 -0.0019 -0.0002 0.0097  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.2237 0.2265 0.3023 -0.0010 -0.0049 0.0125  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.1883 0.1891 0.2983 0.0054  0.0069  0.0121  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.1926 0.1897 0.3066 0.0069  0.0112  0.0105  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.2058 0.2052 0.3312 0.0091  0.0142  0.0101  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.2156 0.2124 0.3423 0.0099  0.0193  0.0068  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.1874 0.1807 0.3016 0.0080  0.0096  0.0133  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.1894 0.1790 0.2939 0.0059  0.0096  0.0122  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.2047 0.1943 0.3021 0.0049  0.0063  0.0147  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.1889 0.1746 0.2906 0.0048  0.0132  0.0079  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.2100 0.1966 0.3017 0.0031  0.0081  0.0126  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.2022 0.1866 0.2965 0.0028  0.0117  0.0083  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.1986 0.1821 0.3029 0.0053  0.0173  0.0035  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.1959 0.1773 0.2873 0.0012  0.0138  0.0044  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.2066 0.1865 0.3064 0.0038  0.0189  -0.0006 28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.2033 0.1825 0.2974 0.0016  0.0169  -0.0001 28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.2052 0.2099 0.3390 0.0101  0.0111  0.0131  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.2137 0.2219 0.3606 0.0122  0.0141  0.0131  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.2223 0.2325 0.3690 0.0108  0.0190  0.0099  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.2323 0.2445 0.3884 0.0126  0.0238  0.0091  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.2165 0.2306 0.3731 0.0134  0.0085  0.0170  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.1985 0.2084 0.3349 0.0080  0.0181  0.0087  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.2044 0.2151 0.3387 0.0067  0.0229  0.0064  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.2065 0.2117 0.3263 0.0058  0.0253  0.0031  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.1947 0.1997 0.3075 0.0042  0.0267  0.0020  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.2136 0.2287 0.3496 0.0044  0.0194  0.0080  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.2526 0.2740 0.4043 0.0053  0.0170  0.0105  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.2689 0.2936 0.4313 0.0061  0.0217  0.0103  30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.2617 0.2850 0.4150 0.0054  0.0097  0.0130  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.2026 0.2034 0.3188 0.0068  0.0258  0.0015  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.1951 0.1914 0.2990 0.0059  0.0269  -0.0019 31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.2151 0.2097 0.3135 0.0065  0.0325  -0.0054 31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.2283 0.2224 0.3319 0.0086  0.0374  -0.0067 31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.2012 0.1932 0.3060 0.0069  0.0267  -0.0032 31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.2198 0.2075 0.3141 0.0058  0.0271  -0.0072 31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.2228 0.2116 0.3091 0.0034  0.0227  -0.0059 31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.2267 0.2097 0.3243 0.0065  0.0276  -0.0088 31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.2086 0.2020 0.2956 0.0051  0.0318  -0.0068 32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.2206 0.2114 0.2991 0.0060  0.0366  -0.0099 32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.2264 0.2130 0.2951 0.0061  0.0353  -0.0141 32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.2496 0.2329 0.3144 0.0078  0.0389  -0.0180 32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.2405 0.2330 0.3134 0.0047  0.0367  -0.0081 32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.2528 0.2419 0.3140 0.0060  0.0409  -0.0108 32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.2435 0.2401 0.3276 0.0043  0.0385  -0.0047 32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.2082 0.1952 0.2735 0.0042  0.0302  -0.0134 33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.2178 0.2019 0.2755 0.0038  0.0284  -0.0172 33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.1967 0.1821 0.2561 0.0018  0.0235  -0.0152 33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.2028 0.1909 0.2629 0.0008  0.0212  -0.0114 33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.2281 0.2116 0.2737 0.0043  0.0290  -0.0192 33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.2476 0.2298 0.2857 0.0037  0.0257  -0.0228 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.2743 0.2534 0.3086 0.0046  0.0260  -0.0281 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.2442 0.2284 0.2783 0.0022  0.0215  -0.0216 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.2844 0.2642 0.3138 0.0034  0.0217  -0.0302 33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.2627 0.2457 0.2922 0.0022  0.0192  -0.0260 33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.2407 0.2275 0.2754 0.0010  0.0193  -0.0174 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.2631 0.2482 0.2890 0.0012  0.0153  -0.0261 33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.2475 0.2355 0.2777 0.0002  0.0158  -0.0176 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.2522 0.2397 0.2786 0.0003  0.0139  -0.0217 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.2082 0.1913 0.2681 0.0012  0.0222  -0.0177 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.2084 0.1924 0.2691 -0.0006 0.0185  -0.0158 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.2070 0.1893 0.2648 -0.0016 0.0173  -0.0203 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.2178 0.1971 0.2754 -0.0009 0.0190  -0.0249 34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.2150 0.1989 0.2846 -0.0007 0.0178  -0.0117 34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.2073 0.1877 0.2845 0.0004  0.0203  -0.0131 34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.2395 0.2161 0.3181 -0.0007 0.0204  -0.0167 34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.2987 0.2717 0.3800 0.0004  0.0229  -0.0204 34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.2334 0.2105 0.3105 -0.0026 0.0181  -0.0162 34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.1982 0.1823 0.2542 -0.0032 0.0144  -0.0193 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.2015 0.1851 0.2570 -0.0045 0.0128  -0.0234 35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.1954 0.1805 0.2551 -0.0064 0.0111  -0.0202 35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.1851 0.1733 0.2411 -0.0066 0.0096  -0.0176 35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.2211 0.2063 0.2671 -0.0038 0.0113  -0.0269 35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.3044 0.2897 0.3503 -0.0048 0.0088  -0.0321 35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.3235 0.3087 0.3772 -0.0070 0.0080  -0.0322 35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.3114 0.2968 0.3495 -0.0036 0.0075  -0.0361 35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.1984 0.1809 0.2662 -0.0077 0.0119  -0.0201 36  SER   A N   
241  C  CA  A SER   A 30  ? 0.2051 0.1884 0.2773 -0.0094 0.0114  -0.0166 36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.1984 0.1818 0.2705 -0.0094 0.0114  -0.0166 36  SER   A CA  
243  C  C   . SER   A 30  ? 0.2065 0.1933 0.2766 -0.0108 0.0094  -0.0190 36  SER   A C   
244  O  O   . SER   A 30  ? 0.2094 0.1987 0.2796 -0.0115 0.0091  -0.0154 36  SER   A O   
245  C  CB  A SER   A 30  ? 0.2330 0.2119 0.3144 -0.0104 0.0133  -0.0165 36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.2101 0.1892 0.2914 -0.0103 0.0133  -0.0160 36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.2751 0.2542 0.3610 -0.0121 0.0137  -0.0130 36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.2289 0.2061 0.3136 -0.0118 0.0131  -0.0222 36  SER   A OG  
249  N  N   . SER   A 31  ? 0.2017 0.1891 0.2700 -0.0110 0.0079  -0.0250 37  SER   A N   
250  C  CA  . SER   A 31  ? 0.2081 0.1996 0.2755 -0.0121 0.0052  -0.0274 37  SER   A CA  
251  C  C   . SER   A 31  ? 0.2032 0.1985 0.2624 -0.0105 0.0039  -0.0251 37  SER   A C   
252  O  O   . SER   A 31  ? 0.2156 0.2147 0.2753 -0.0111 0.0022  -0.0255 37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2588 0.2501 0.3259 -0.0125 0.0029  -0.0348 37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.3365 0.3276 0.3932 -0.0099 0.0021  -0.0371 37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.1893 0.1835 0.2421 -0.0086 0.0049  -0.0227 38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.1758 0.1724 0.2212 -0.0072 0.0040  -0.0203 38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.1738 0.1703 0.2195 -0.0072 0.0051  -0.0146 38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.1692 0.1671 0.2092 -0.0062 0.0043  -0.0128 38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.1787 0.1739 0.2163 -0.0051 0.0044  -0.0219 38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.1853 0.1805 0.2191 -0.0044 0.0027  -0.0275 38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.2049 0.1982 0.2297 -0.0019 0.0040  -0.0285 38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.1935 0.1879 0.2115 -0.0005 0.0038  -0.0253 38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.2196 0.2128 0.2285 0.0018  0.0043  -0.0259 38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.2423 0.2333 0.2463 0.0032  0.0049  -0.0298 38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.2264 0.2199 0.2301 0.0028  0.0043  -0.0227 38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.1642 0.1585 0.2157 -0.0079 0.0066  -0.0121 39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.1557 0.1495 0.2064 -0.0074 0.0069  -0.0070 39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.1541 0.1479 0.2001 -0.0061 0.0066  -0.0063 39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.1637 0.1581 0.2066 -0.0057 0.0057  -0.0033 39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.1735 0.1692 0.2222 -0.0078 0.0064  -0.0042 39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.1859 0.1805 0.2326 -0.0071 0.0064  0.0007  39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.1739 0.1663 0.2245 -0.0069 0.0070  0.0028  39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.1864 0.1822 0.2274 -0.0065 0.0056  0.0021  39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.1605 0.1532 0.2065 -0.0054 0.0076  -0.0089 40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.1543 0.1469 0.1976 -0.0044 0.0082  -0.0080 40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.1504 0.1417 0.1997 -0.0037 0.0101  -0.0075 40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.1676 0.1570 0.2206 -0.0036 0.0116  -0.0099 40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.1581 0.1508 0.1947 -0.0034 0.0087  -0.0109 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.1862 0.1805 0.2164 -0.0033 0.0069  -0.0108 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.1939 0.1874 0.2170 -0.0018 0.0076  -0.0131 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.1890 0.1836 0.2178 -0.0035 0.0060  -0.0071 40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.1455 0.1377 0.1960 -0.0033 0.0101  -0.0049 41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.1524 0.1443 0.2094 -0.0024 0.0120  -0.0044 41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.1678 0.1612 0.2237 -0.0022 0.0128  -0.0035 41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.1710 0.1656 0.2239 -0.0030 0.0106  -0.0017 41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.1521 0.1442 0.2163 -0.0022 0.0106  -0.0010 41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.1616 0.1539 0.2345 -0.0007 0.0124  -0.0002 41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.1848 0.1754 0.2641 0.0000  0.0119  0.0019  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.1712 0.1668 0.2473 -0.0006 0.0109  0.0024  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.1675 0.1605 0.2258 -0.0012 0.0163  -0.0049 42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.1728 0.1673 0.2324 -0.0012 0.0183  -0.0037 42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.1823 0.1784 0.2528 -0.0003 0.0202  -0.0024 42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.1951 0.1899 0.2691 0.0011  0.0228  -0.0041 42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.1815 0.1739 0.2334 -0.0003 0.0220  -0.0062 42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.1981 0.1914 0.2521 -0.0004 0.0250  -0.0043 42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.1845 0.1757 0.2263 -0.0006 0.0196  -0.0073 42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.1768 0.1759 0.2534 -0.0011 0.0186  0.0002  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.1769 0.1790 0.2657 -0.0003 0.0198  0.0017  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.2052 0.2094 0.2980 -0.0011 0.0229  0.0024  43  SER   A C   
300  O  O   . SER   A 37  ? 0.2005 0.2036 0.2867 -0.0025 0.0228  0.0024  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.1823 0.1868 0.2772 -0.0005 0.0144  0.0045  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.2039 0.2097 0.2957 -0.0023 0.0101  0.0058  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.2121 0.2191 0.3165 0.0000  0.0259  0.0031  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.2232 0.2327 0.3338 -0.0010 0.0296  0.0041  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.2336 0.2480 0.3543 -0.0030 0.0246  0.0063  44  SER   A C   
306  O  O   . SER   A 38  ? 0.2363 0.2533 0.3630 -0.0025 0.0194  0.0075  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.2487 0.2591 0.3670 0.0012  0.0366  0.0035  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.2909 0.3045 0.4207 0.0027  0.0345  0.0044  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.2473 0.2625 0.3697 -0.0051 0.0261  0.0069  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.2868 0.3062 0.4191 -0.0075 0.0212  0.0083  45  THR   A CA  
311  C  C   . THR   A 39  ? 0.3311 0.3543 0.4772 -0.0085 0.0266  0.0093  45  THR   A C   
312  O  O   . THR   A 39  ? 0.3350 0.3559 0.4786 -0.0077 0.0345  0.0092  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.3124 0.3286 0.4344 -0.0098 0.0172  0.0079  45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.3260 0.3391 0.4438 -0.0109 0.0231  0.0078  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.3159 0.3281 0.4236 -0.0088 0.0137  0.0070  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.3618 0.3906 0.5218 -0.0104 0.0223  0.0102  46  THR   A N   
317  C  CA  . THR   A 40  ? 0.3944 0.4275 0.5699 -0.0120 0.0271  0.0112  46  THR   A CA  
318  C  C   . THR   A 40  ? 0.4204 0.4507 0.5927 -0.0157 0.0275  0.0112  46  THR   A C   
319  O  O   . THR   A 40  ? 0.4374 0.4670 0.6142 -0.0168 0.0351  0.0122  46  THR   A O   
320  C  CB  . THR   A 40  ? 0.4213 0.4628 0.6158 -0.0121 0.0221  0.0119  46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.4538 0.4961 0.6457 -0.0135 0.0118  0.0113  46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.4243 0.4680 0.6233 -0.0081 0.0233  0.0124  46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.4173 0.4451 0.5814 -0.0173 0.0200  0.0101  47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.4122 0.4365 0.5733 -0.0207 0.0199  0.0098  47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.4126 0.4289 0.5558 -0.0197 0.0250  0.0099  47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.4120 0.4255 0.5426 -0.0169 0.0252  0.0093  47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.4143 0.4391 0.5740 -0.0225 0.0098  0.0082  47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.4010 0.4136 0.5436 -0.0220 0.0289  0.0107  48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.4091 0.4141 0.5350 -0.0207 0.0333  0.0112  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.3928 0.3938 0.5057 -0.0208 0.0264  0.0096  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.4020 0.4036 0.5193 -0.0233 0.0205  0.0084  48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.4597 0.4615 0.5900 -0.0229 0.0401  0.0133  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.5533 0.5472 0.6664 -0.0208 0.0454  0.0146  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.6557 0.6489 0.7627 -0.0172 0.0530  0.0156  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6816 0.6799 0.7976 -0.0162 0.0554  0.0155  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.6876 0.6742 0.7788 -0.0149 0.0570  0.0167  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.3662 0.3634 0.4637 -0.0179 0.0271  0.0091  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.3607 0.3545 0.4458 -0.0173 0.0217  0.0077  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.3593 0.3474 0.4386 -0.0188 0.0217  0.0079  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.3949 0.3801 0.4759 -0.0195 0.0275  0.0097  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.3193 0.3056 0.3915 -0.0189 0.0156  0.0063  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.2899 0.2704 0.3561 -0.0200 0.0144  0.0058  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.2794 0.2547 0.3308 -0.0171 0.0166  0.0063  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.2700 0.2397 0.3169 -0.0174 0.0176  0.0067  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.2924 0.2737 0.3594 -0.0215 0.0066  0.0033  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.3256 0.3094 0.3833 -0.0186 0.0014  0.0021  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.2674 0.2444 0.3119 -0.0142 0.0173  0.0062  51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.2609 0.2346 0.2922 -0.0113 0.0180  0.0062  51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.2684 0.2396 0.2936 -0.0089 0.0242  0.0080  51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.2813 0.2544 0.3119 -0.0090 0.0283  0.0089  51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.2658 0.2431 0.2935 -0.0098 0.0140  0.0045  51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.3069 0.2855 0.3358 -0.0110 0.0082  0.0031  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.3160 0.2908 0.3399 -0.0111 0.0064  0.0025  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.2618 0.2446 0.2953 -0.0113 0.0054  0.0026  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.2671 0.2342 0.2808 -0.0063 0.0245  0.0085  52  THR   A N   
356  C  CA  . THR   A 46  ? 0.2890 0.2529 0.2927 -0.0030 0.0286  0.0100  52  THR   A CA  
357  C  C   . THR   A 46  ? 0.2528 0.2191 0.2485 -0.0002 0.0250  0.0078  52  THR   A C   
358  O  O   . THR   A 46  ? 0.2543 0.2214 0.2489 -0.0003 0.0207  0.0065  52  THR   A O   
359  C  CB  . THR   A 46  ? 0.3681 0.3252 0.3659 -0.0021 0.0304  0.0123  52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.4396 0.3941 0.4450 -0.0046 0.0349  0.0145  52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.4068 0.3607 0.3914 0.0024  0.0325  0.0138  52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.2341 0.2015 0.2246 0.0021  0.0269  0.0072  53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.2211 0.1912 0.2058 0.0043  0.0233  0.0048  53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.2287 0.1954 0.2020 0.0078  0.0234  0.0057  53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.2470 0.2098 0.2143 0.0097  0.0276  0.0078  53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.2177 0.1906 0.2033 0.0048  0.0245  0.0027  53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.2364 0.2126 0.2337 0.0020  0.0249  0.0023  53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.2207 0.1966 0.2022 0.0064  0.0203  -0.0003 53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.2415 0.2205 0.2447 -0.0001 0.0199  0.0016  53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.2075 0.1757 0.1778 0.0091  0.0190  0.0044  54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.2122 0.1783 0.1726 0.0130  0.0181  0.0051  54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.2135 0.1813 0.1675 0.0156  0.0179  0.0032  54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.2158 0.1878 0.1739 0.0143  0.0164  0.0002  54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.2173 0.1860 0.1784 0.0137  0.0134  0.0038  54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.2359 0.2000 0.1792 0.0193  0.0193  0.0050  55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.2407 0.2058 0.1755 0.0224  0.0184  0.0027  55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.2660 0.2307 0.1924 0.0266  0.0145  0.0034  55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.2847 0.2441 0.2016 0.0299  0.0168  0.0068  55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.2499 0.2104 0.1784 0.0236  0.0245  0.0047  55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.2499 0.2113 0.1886 0.0197  0.0286  0.0045  55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.2497 0.2164 0.1954 0.0177  0.0261  0.0000  55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.2446 0.2117 0.1998 0.0147  0.0304  0.0006  55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.2687 0.2398 0.2330 0.0124  0.0289  -0.0021 55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.2553 0.2298 0.2207 0.0122  0.0238  -0.0056 55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.2840 0.2556 0.2572 0.0102  0.0327  -0.0012 55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.2557 0.2258 0.1865 0.0264  0.0090  0.0005  56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.2622 0.2331 0.1886 0.0301  0.0051  0.0013  56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.2667 0.2453 0.1988 0.0298  -0.0008 -0.0030 56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.2603 0.2428 0.1996 0.0266  -0.0016 -0.0063 56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.2490 0.2166 0.1792 0.0292  0.0067  0.0047  56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.2453 0.2175 0.1892 0.0243  0.0053  0.0025  56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.2837 0.2643 0.2136 0.0333  -0.0048 -0.0026 57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.2831 0.2716 0.2204 0.0331  -0.0101 -0.0062 57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.2851 0.2753 0.2294 0.0330  -0.0106 -0.0047 57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.2889 0.2850 0.2377 0.0345  -0.0146 -0.0064 57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.3313 0.3228 0.2617 0.0376  -0.0154 -0.0083 57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.4129 0.4011 0.3346 0.0431  -0.0164 -0.0045 57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 0.4090 0.3916 0.3294 0.0433  -0.0124 -0.0002 57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 0.5026 0.4938 0.4188 0.0473  -0.0216 -0.0059 57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.2620 0.2472 0.2080 0.0309  -0.0063 -0.0019 58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.2467 0.2329 0.1986 0.0307  -0.0064 -0.0010 58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.2306 0.2242 0.1924 0.0283  -0.0086 -0.0041 58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.2284 0.2245 0.1946 0.0249  -0.0083 -0.0063 58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.2410 0.2208 0.1934 0.0282  -0.0021 0.0014  58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.2686 0.2387 0.2117 0.0310  0.0012  0.0059  58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.2116 0.2085 0.1773 0.0303  -0.0101 -0.0041 59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.2031 0.2068 0.1788 0.0282  -0.0110 -0.0063 59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.2005 0.2023 0.1788 0.0281  -0.0084 -0.0047 59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.2096 0.2166 0.1951 0.0278  -0.0086 -0.0057 59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.2294 0.2412 0.2099 0.0306  -0.0155 -0.0086 59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.2954 0.3106 0.2763 0.0293  -0.0185 -0.0119 59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.3414 0.3654 0.3294 0.0311  -0.0235 -0.0147 59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.3632 0.3886 0.3461 0.0345  -0.0278 -0.0158 59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.3129 0.3432 0.3131 0.0289  -0.0232 -0.0159 59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.1971 0.1910 0.1693 0.0286  -0.0058 -0.0023 60  THR   A N   
416  C  CA  . THR   A 54  ? 0.2002 0.1908 0.1734 0.0280  -0.0034 -0.0015 60  THR   A CA  
417  C  C   . THR   A 54  ? 0.1963 0.1800 0.1662 0.0247  -0.0010 -0.0006 60  THR   A C   
418  O  O   . THR   A 54  ? 0.2167 0.1973 0.1828 0.0242  -0.0006 0.0004  60  THR   A O   
419  C  CB  . THR   A 54  ? 0.2246 0.2122 0.1949 0.0325  -0.0031 -0.0001 60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.2669 0.2475 0.2298 0.0343  -0.0026 0.0022  60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.2405 0.2357 0.2153 0.0362  -0.0058 -0.0009 60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.1907 0.1727 0.1624 0.0226  0.0004  -0.0010 61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.1971 0.1738 0.1674 0.0193  0.0018  -0.0005 61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.1903 0.1659 0.1617 0.0177  0.0023  -0.0015 61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.2097 0.1871 0.1816 0.0198  0.0026  -0.0021 61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.1779 0.1504 0.1495 0.0144  0.0025  -0.0016 62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.1819 0.1525 0.1528 0.0131  0.0024  -0.0026 62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.1861 0.1596 0.1606 0.0097  0.0015  -0.0027 62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.1960 0.1691 0.1727 0.0077  0.0013  -0.0021 62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.2016 0.1642 0.1690 0.0127  0.0027  -0.0030 62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.2282 0.1887 0.1939 0.0112  0.0017  -0.0047 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.2197 0.1786 0.1837 0.0165  0.0039  -0.0026 62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.1807 0.1567 0.1556 0.0092  0.0013  -0.0031 63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.1762 0.1543 0.1541 0.0065  0.0003  -0.0027 63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.1807 0.1558 0.1551 0.0057  -0.0009 -0.0033 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.1784 0.1509 0.1478 0.0075  -0.0003 -0.0041 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.1727 0.1570 0.1552 0.0064  0.0009  -0.0021 63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.1687 0.1550 0.1503 0.0076  0.0022  -0.0018 63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.1771 0.1645 0.1576 0.0103  0.0037  -0.0023 63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.1716 0.1585 0.1533 0.0064  0.0023  -0.0008 63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.1829 0.1723 0.1632 0.0115  0.0059  -0.0018 63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.1930 0.1813 0.1732 0.0077  0.0045  0.0000  63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.2000 0.1896 0.1798 0.0101  0.0065  -0.0006 63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.2388 0.2300 0.2179 0.0116  0.0096  0.0003  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.1862 0.1617 0.1630 0.0033  -0.0026 -0.0028 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.1850 0.1581 0.1580 0.0028  -0.0047 -0.0034 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.1903 0.1667 0.1626 0.0034  -0.0040 -0.0018 64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.1913 0.1715 0.1690 0.0025  -0.0036 -0.0003 64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.1905 0.1627 0.1673 0.0001  -0.0076 -0.0036 64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.2022 0.1722 0.1746 -0.0002 -0.0108 -0.0045 64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.2099 0.1747 0.1755 0.0006  -0.0118 -0.0069 64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.2131 0.1858 0.1875 -0.0010 -0.0130 -0.0031 64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.2331 0.1955 0.1930 0.0006  -0.0154 -0.0083 64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.2354 0.2060 0.2042 -0.0007 -0.0166 -0.0039 64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.2554 0.2210 0.2165 0.0001  -0.0178 -0.0067 64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.3159 0.2790 0.2702 0.0005  -0.0219 -0.0081 64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.1877 0.1619 0.1529 0.0052  -0.0035 -0.0023 65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.1828 0.1590 0.1457 0.0062  -0.0020 -0.0003 65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.2014 0.1745 0.1578 0.0060  -0.0052 -0.0002 65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.2168 0.1856 0.1647 0.0074  -0.0060 -0.0021 65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.1983 0.1747 0.1578 0.0088  0.0018  -0.0005 65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.2314 0.2093 0.1873 0.0103  0.0051  0.0024  65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.2086 0.1837 0.1691 0.0046  -0.0073 0.0017  66  SER   A N   
464  C  CA  . SER   A 60  ? 0.2239 0.1966 0.1788 0.0047  -0.0113 0.0018  66  SER   A CA  
465  C  C   . SER   A 60  ? 0.2201 0.1904 0.1641 0.0074  -0.0100 0.0029  66  SER   A C   
466  O  O   . SER   A 60  ? 0.2229 0.1894 0.1581 0.0083  -0.0135 0.0013  66  SER   A O   
467  C  CB  . SER   A 60  ? 0.2896 0.2653 0.2515 0.0032  -0.0137 0.0041  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.3808 0.3594 0.3464 0.0037  -0.0101 0.0073  66  SER   A OG  
469  N  N   . SER   A 61  ? 0.2072 0.1795 0.1515 0.0087  -0.0048 0.0054  67  SER   A N   
470  C  CA  . SER   A 61  ? 0.2147 0.1847 0.1488 0.0115  -0.0019 0.0071  67  SER   A CA  
471  C  C   . SER   A 61  ? 0.2203 0.1862 0.1449 0.0137  -0.0005 0.0040  67  SER   A C   
472  O  O   . SER   A 61  ? 0.2451 0.2083 0.1594 0.0164  0.0018  0.0049  67  SER   A O   
473  C  CB  . SER   A 61  ? 0.2334 0.2069 0.1726 0.0119  0.0038  0.0109  67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.2390 0.2155 0.1852 0.0115  0.0072  0.0094  67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.2121 0.1771 0.1398 0.0128  -0.0018 0.0004  68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.2233 0.1835 0.1429 0.0149  -0.0010 -0.0031 68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.2431 0.1990 0.1613 0.0132  -0.0066 -0.0070 68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.2708 0.2218 0.1832 0.0145  -0.0065 -0.0105 68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.2320 0.1946 0.1573 0.0159  0.0038  -0.0034 68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.2440 0.2107 0.1710 0.0177  0.0098  -0.0001 68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 0.2718 0.2343 0.1862 0.0211  0.0130  -0.0003 68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 0.2832 0.2496 0.1999 0.0228  0.0196  0.0032  68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 0.3015 0.2692 0.2171 0.0225  0.0214  0.0073  68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 0.2932 0.2589 0.2052 0.0211  0.0166  0.0083  68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 0.3007 0.2716 0.2195 0.0238  0.0281  0.0104  68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.2470 0.2050 0.1725 0.0102  -0.0111 -0.0066 69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.2688 0.2238 0.1966 0.0079  -0.0159 -0.0100 69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.2743 0.2265 0.2043 0.0080  -0.0135 -0.0124 69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.3050 0.2514 0.2306 0.0079  -0.0155 -0.0162 69  ARG   A O   
490  C  CB  . ARG   A 63  ? 0.3203 0.2703 0.2378 0.0085  -0.0208 -0.0130 69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 0.4082 0.3610 0.3273 0.0073  -0.0257 -0.0114 69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 0.4390 0.3872 0.3514 0.0069  -0.0326 -0.0157 69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 0.4505 0.4006 0.3585 0.0079  -0.0368 -0.0136 69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 0.4506 0.3972 0.3439 0.0111  -0.0378 -0.0136 69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 0.4620 0.4030 0.3436 0.0135  -0.0350 -0.0166 69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 0.4406 0.3891 0.3302 0.0124  -0.0414 -0.0107 69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.2492 0.2051 0.1854 0.0085  -0.0092 -0.0102 70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.2588 0.2121 0.1961 0.0095  -0.0067 -0.0118 70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.2336 0.1917 0.1803 0.0088  -0.0046 -0.0095 70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.2364 0.2001 0.1877 0.0083  -0.0037 -0.0069 70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.3095 0.2616 0.2400 0.0134  -0.0025 -0.0121 70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.4493 0.3938 0.3698 0.0151  -0.0032 -0.0159 70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.5445 0.4887 0.4591 0.0193  0.0020  -0.0158 70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 0.6342 0.5704 0.5368 0.0214  0.0015  -0.0199 70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 0.6922 0.6287 0.5860 0.0250  0.0056  -0.0191 70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.2218 0.1773 0.1706 0.0092  -0.0036 -0.0104 71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.2136 0.1729 0.1690 0.0093  -0.0017 -0.0085 71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.2258 0.1862 0.1796 0.0130  0.0016  -0.0083 71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.2630 0.2188 0.2112 0.0153  0.0027  -0.0100 71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.2064 0.1618 0.1646 0.0079  -0.0025 -0.0089 71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.2227 0.1775 0.1847 0.0043  -0.0053 -0.0092 71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.2621 0.2207 0.2309 0.0023  -0.0052 -0.0073 71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.2251 0.1758 0.1853 0.0024  -0.0084 -0.0115 71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.2453 0.2025 0.2173 -0.0005 -0.0078 -0.0081 71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.2802 0.2329 0.2475 -0.0007 -0.0102 -0.0107 71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.1965 0.1632 0.1558 0.0135  0.0030  -0.0064 72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.1936 0.1630 0.1539 0.0169  0.0057  -0.0061 72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.2026 0.1749 0.1679 0.0176  0.0054  -0.0051 72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.2102 0.1855 0.1795 0.0154  0.0041  -0.0042 72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.1927 0.1685 0.1559 0.0172  0.0076  -0.0049 72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.2123 0.1856 0.1691 0.0178  0.0089  -0.0052 72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.2534 0.2237 0.2048 0.0210  0.0115  -0.0065 72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.2328 0.2070 0.1887 0.0155  0.0079  -0.0041 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.2705 0.2384 0.2144 0.0220  0.0132  -0.0068 72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.2544 0.2262 0.2029 0.0166  0.0091  -0.0040 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.2884 0.2569 0.2303 0.0198  0.0118  -0.0054 72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.3198 0.2853 0.2526 0.0212  0.0133  -0.0054 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.2015 0.1728 0.1662 0.0210  0.0065  -0.0053 73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.2067 0.1814 0.1752 0.0225  0.0058  -0.0042 73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.2218 0.2055 0.1968 0.0229  0.0059  -0.0038 73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.2554 0.2424 0.2324 0.0237  0.0079  -0.0040 73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.2178 0.1883 0.1834 0.0266  0.0069  -0.0043 73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.2289 0.1981 0.1920 0.0280  0.0091  -0.0057 73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.2100 0.1773 0.1704 0.0243  0.0085  -0.0065 73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.1903 0.1780 0.1689 0.0223  0.0041  -0.0034 74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.2007 0.1968 0.1866 0.0221  0.0036  -0.0037 74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.1913 0.1907 0.1791 0.0241  0.0012  -0.0038 74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.1984 0.1936 0.1814 0.0247  0.0000  -0.0033 74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.2264 0.2246 0.2154 0.0179  0.0032  -0.0037 74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.2453 0.2434 0.2345 0.0165  0.0055  -0.0033 74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.2277 0.2212 0.2130 0.0158  0.0020  -0.0035 74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.1886 0.1957 0.1835 0.0254  0.0004  -0.0046 75  SER   A N   
543  C  CA  . SER   A 69  ? 0.1865 0.1985 0.1843 0.0268  -0.0030 -0.0055 75  SER   A CA  
544  C  C   . SER   A 69  ? 0.1782 0.1953 0.1825 0.0230  -0.0038 -0.0070 75  SER   A C   
545  O  O   . SER   A 69  ? 0.1880 0.2085 0.1986 0.0212  -0.0018 -0.0071 75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2307 0.2487 0.2340 0.0308  -0.0040 -0.0058 75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3155 0.3279 0.3126 0.0347  -0.0033 -0.0043 75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.1589 0.1755 0.1613 0.0217  -0.0062 -0.0080 76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.1666 0.1866 0.1748 0.0180  -0.0067 -0.0097 76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.1778 0.2022 0.1882 0.0187  -0.0108 -0.0124 76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.1877 0.2108 0.1918 0.0219  -0.0133 -0.0125 76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.1715 0.1856 0.1754 0.0149  -0.0050 -0.0088 76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.1759 0.1838 0.1709 0.0160  -0.0051 -0.0079 76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.1807 0.1830 0.1701 0.0172  -0.0034 -0.0059 76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.1805 0.1879 0.1729 0.0158  -0.0066 -0.0091 76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.1893 0.1857 0.1719 0.0177  -0.0029 -0.0047 76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.1916 0.1930 0.1760 0.0168  -0.0057 -0.0077 76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.1911 0.1873 0.1713 0.0176  -0.0038 -0.0053 76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.1683 0.1976 0.1873 0.0159  -0.0116 -0.0146 77  SER   A N   
560  C  CA  . SER   A 71  ? 0.1760 0.2093 0.1974 0.0161  -0.0160 -0.0181 77  SER   A CA  
561  C  C   . SER   A 71  ? 0.1970 0.2250 0.2099 0.0155  -0.0167 -0.0191 77  SER   A C   
562  O  O   . SER   A 71  ? 0.2025 0.2246 0.2105 0.0140  -0.0135 -0.0171 77  SER   A O   
563  C  CB  . SER   A 71  ? 0.1875 0.2272 0.2220 0.0129  -0.0164 -0.0205 77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.2299 0.2660 0.2659 0.0091  -0.0132 -0.0198 77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.2029 0.2330 0.2136 0.0170  -0.0210 -0.0223 78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.2138 0.2389 0.2160 0.0168  -0.0212 -0.0236 78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.2162 0.2407 0.2249 0.0123  -0.0193 -0.0254 78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.2230 0.2521 0.2428 0.0097  -0.0195 -0.0268 78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.2595 0.2873 0.2573 0.0197  -0.0266 -0.0270 78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.3078 0.3351 0.2979 0.0248  -0.0284 -0.0245 78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.3995 0.4288 0.3830 0.0282  -0.0343 -0.0278 78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.4905 0.5167 0.4629 0.0337  -0.0351 -0.0242 78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.5351 0.5653 0.5029 0.0379  -0.0420 -0.0270 78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.2129 0.2318 0.2154 0.0115  -0.0173 -0.0255 79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.2112 0.2290 0.2200 0.0078  -0.0154 -0.0271 79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.2063 0.2287 0.2230 0.0062  -0.0190 -0.0321 79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.2225 0.2463 0.2349 0.0082  -0.0231 -0.0359 79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.2375 0.2493 0.2375 0.0084  -0.0133 -0.0270 79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.2630 0.2719 0.2531 0.0116  -0.0123 -0.0236 79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.2226 0.2359 0.2128 0.0142  -0.0159 -0.0237 79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.1895 0.2139 0.2176 0.0027  -0.0174 -0.0322 80  SER   A N   
582  C  CA  A SER   A 74  ? 0.2030 0.2318 0.2410 0.0006  -0.0206 -0.0369 80  SER   A CA  
583  C  CA  B SER   A 74  ? 0.1942 0.2233 0.2327 0.0006  -0.0205 -0.0367 80  SER   A CA  
584  C  C   . SER   A 74  ? 0.1956 0.2227 0.2434 -0.0035 -0.0174 -0.0369 80  SER   A C   
585  O  O   . SER   A 74  ? 0.1878 0.2108 0.2343 -0.0043 -0.0132 -0.0328 80  SER   A O   
586  C  CB  A SER   A 74  ? 0.2417 0.2780 0.2871 0.0014  -0.0232 -0.0370 80  SER   A CB  
587  C  CB  B SER   A 74  ? 0.2054 0.2416 0.2520 0.0010  -0.0222 -0.0360 80  SER   A CB  
588  O  OG  A SER   A 74  ? 0.2830 0.3203 0.3341 0.0003  -0.0191 -0.0324 80  SER   A OG  
589  O  OG  B SER   A 74  ? 0.2228 0.2604 0.2619 0.0050  -0.0237 -0.0340 80  SER   A OG  
590  N  N   . LEU   A 75  ? 0.2025 0.2325 0.2603 -0.0060 -0.0199 -0.0415 81  LEU   A N   
591  C  CA  . LEU   A 75  ? 0.2073 0.2352 0.2755 -0.0099 -0.0170 -0.0416 81  LEU   A CA  
592  C  C   . LEU   A 75  ? 0.2184 0.2514 0.2981 -0.0117 -0.0150 -0.0385 81  LEU   A C   
593  O  O   . LEU   A 75  ? 0.2349 0.2746 0.3223 -0.0120 -0.0181 -0.0410 81  LEU   A O   
594  C  CB  . LEU   A 75  ? 0.2166 0.2450 0.2898 -0.0116 -0.0210 -0.0489 81  LEU   A CB  
595  C  CG  . LEU   A 75  ? 0.2642 0.2882 0.3455 -0.0151 -0.0185 -0.0505 81  LEU   A CG  
596  C  CD1 . LEU   A 75  ? 0.2815 0.2980 0.3551 -0.0142 -0.0142 -0.0474 81  LEU   A CD1 
597  C  CD2 . LEU   A 75  ? 0.2925 0.3167 0.3773 -0.0164 -0.0234 -0.0589 81  LEU   A CD2 
598  N  N   . ILE   A 76  ? 0.2034 0.2335 0.2843 -0.0127 -0.0098 -0.0330 82  ILE   A N   
599  C  CA  . ILE   A 76  ? 0.2195 0.2533 0.3084 -0.0137 -0.0067 -0.0291 82  ILE   A CA  
600  C  C   . ILE   A 76  ? 0.2023 0.2326 0.2993 -0.0169 -0.0022 -0.0265 82  ILE   A C   
601  O  O   . ILE   A 76  ? 0.2073 0.2314 0.2989 -0.0168 -0.0002 -0.0246 82  ILE   A O   
602  C  CB  . ILE   A 76  ? 0.2509 0.2839 0.3297 -0.0105 -0.0048 -0.0243 82  ILE   A CB  
603  C  CG1 . ILE   A 76  ? 0.2866 0.3232 0.3590 -0.0072 -0.0089 -0.0264 82  ILE   A CG1 
604  C  CG2 . ILE   A 76  ? 0.2623 0.2971 0.3466 -0.0112 -0.0002 -0.0196 82  ILE   A CG2 
605  C  CD1 . ILE   A 76  ? 0.3263 0.3607 0.3884 -0.0042 -0.0075 -0.0227 82  ILE   A CD1 
606  N  N   . PHE   A 77  ? 0.1952 0.2295 0.3055 -0.0195 -0.0002 -0.0260 83  PHE   A N   
607  C  CA  . PHE   A 77  ? 0.2067 0.2369 0.3243 -0.0223 0.0048  -0.0226 83  PHE   A CA  
608  C  C   . PHE   A 77  ? 0.2136 0.2405 0.3231 -0.0204 0.0095  -0.0154 83  PHE   A C   
609  O  O   . PHE   A 77  ? 0.2234 0.2536 0.3289 -0.0183 0.0105  -0.0130 83  PHE   A O   
610  C  CB  . PHE   A 77  ? 0.2202 0.2559 0.3547 -0.0256 0.0064  -0.0235 83  PHE   A CB  
611  C  CG  . PHE   A 77  ? 0.2552 0.2863 0.3978 -0.0284 0.0124  -0.0191 83  PHE   A CG  
612  C  CD1 . PHE   A 77  ? 0.2645 0.2959 0.4080 -0.0280 0.0183  -0.0125 83  PHE   A CD1 
613  C  CD2 . PHE   A 77  ? 0.2829 0.3084 0.4306 -0.0310 0.0124  -0.0213 83  PHE   A CD2 
614  C  CE1 . PHE   A 77  ? 0.2820 0.3085 0.4315 -0.0302 0.0242  -0.0078 83  PHE   A CE1 
615  C  CE2 . PHE   A 77  ? 0.2953 0.3156 0.4500 -0.0333 0.0182  -0.0166 83  PHE   A CE2 
616  C  CZ  . PHE   A 77  ? 0.2824 0.3035 0.4381 -0.0329 0.0240  -0.0097 83  PHE   A CZ  
617  N  N   . VAL   A 78  ? 0.2120 0.2320 0.3186 -0.0209 0.0121  -0.0124 84  VAL   A N   
618  C  CA  . VAL   A 78  ? 0.2128 0.2291 0.3115 -0.0191 0.0157  -0.0059 84  VAL   A CA  
619  C  C   . VAL   A 78  ? 0.2246 0.2370 0.3312 -0.0213 0.0205  -0.0019 84  VAL   A C   
620  O  O   . VAL   A 78  ? 0.2250 0.2334 0.3369 -0.0232 0.0204  -0.0035 84  VAL   A O   
621  C  CB  . VAL   A 78  ? 0.2118 0.2235 0.2985 -0.0168 0.0137  -0.0055 84  VAL   A CB  
622  C  CG1 . VAL   A 78  ? 0.2218 0.2299 0.3009 -0.0151 0.0165  0.0008  84  VAL   A CG1 
623  C  CG2 . VAL   A 78  ? 0.2113 0.2259 0.2902 -0.0147 0.0096  -0.0089 84  VAL   A CG2 
624  N  N   . GLU   A 79  ? 0.2352 0.2482 0.3421 -0.0209 0.0251  0.0034  85  GLU   A N   
625  C  CA  . GLU   A 79  ? 0.2503 0.2592 0.3641 -0.0228 0.0305  0.0082  85  GLU   A CA  
626  C  C   . GLU   A 79  ? 0.2554 0.2566 0.3625 -0.0215 0.0310  0.0118  85  GLU   A C   
627  O  O   . GLU   A 79  ? 0.2510 0.2508 0.3468 -0.0190 0.0279  0.0118  85  GLU   A O   
628  C  CB  . GLU   A 79  ? 0.3123 0.3233 0.4258 -0.0219 0.0360  0.0135  85  GLU   A CB  
629  C  CG  . GLU   A 79  ? 0.4659 0.4800 0.5960 -0.0254 0.0403  0.0136  85  GLU   A CG  
630  C  CD  . GLU   A 79  ? 0.6172 0.6250 0.7546 -0.0277 0.0455  0.0182  85  GLU   A CD  
631  O  OE1 . GLU   A 79  ? 0.6283 0.6317 0.7696 -0.0294 0.0434  0.0159  85  GLU   A OE1 
632  O  OE2 . GLU   A 79  ? 0.6886 0.6957 0.8280 -0.0276 0.0522  0.0242  85  GLU   A OE2 
633  N  N   . ALA   A 80  ? 0.2670 0.2632 0.3817 -0.0234 0.0349  0.0151  86  ALA   A N   
634  C  CA  . ALA   A 80  ? 0.2702 0.2592 0.3796 -0.0218 0.0354  0.0191  86  ALA   A CA  
635  C  C   . ALA   A 80  ? 0.2759 0.2633 0.3712 -0.0181 0.0361  0.0249  86  ALA   A C   
636  O  O   . ALA   A 80  ? 0.2827 0.2723 0.3743 -0.0172 0.0391  0.0280  86  ALA   A O   
637  C  CB  . ALA   A 80  ? 0.2721 0.2558 0.3921 -0.0241 0.0404  0.0228  86  ALA   A CB  
638  N  N   . SER   A 81  ? 0.2700 0.2538 0.3576 -0.0158 0.0331  0.0259  87  SER   A N   
639  C  CA  . SER   A 81  ? 0.2714 0.2533 0.3460 -0.0123 0.0326  0.0308  87  SER   A CA  
640  C  C   . SER   A 81  ? 0.2896 0.2653 0.3637 -0.0109 0.0324  0.0349  87  SER   A C   
641  O  O   . SER   A 81  ? 0.2938 0.2665 0.3777 -0.0127 0.0335  0.0339  87  SER   A O   
642  C  CB  . SER   A 81  ? 0.2764 0.2619 0.3421 -0.0107 0.0275  0.0269  87  SER   A CB  
643  O  OG  . SER   A 81  ? 0.2678 0.2526 0.3354 -0.0108 0.0238  0.0234  87  SER   A OG  
644  N  N   . GLU   A 82  ? 0.3051 0.2786 0.3681 -0.0076 0.0307  0.0392  88  GLU   A N   
645  C  CA  . GLU   A 82  ? 0.3248 0.2932 0.3877 -0.0056 0.0295  0.0428  88  GLU   A CA  
646  C  C   . GLU   A 82  ? 0.3211 0.2907 0.3888 -0.0060 0.0254  0.0375  88  GLU   A C   
647  O  O   . GLU   A 82  ? 0.3426 0.3084 0.4140 -0.0049 0.0249  0.0394  88  GLU   A O   
648  C  CB  . GLU   A 82  ? 0.3857 0.3526 0.4353 -0.0018 0.0274  0.0479  88  GLU   A CB  
649  C  CG  . GLU   A 82  ? 0.5070 0.4712 0.5501 -0.0005 0.0322  0.0541  88  GLU   A CG  
650  C  CD  . GLU   A 82  ? 0.6686 0.6321 0.6962 0.0033  0.0293  0.0574  88  GLU   A CD  
651  O  OE1 . GLU   A 82  ? 0.6975 0.6562 0.7196 0.0062  0.0292  0.0635  88  GLU   A OE1 
652  O  OE2 . GLU   A 82  ? 0.7227 0.6901 0.7435 0.0035  0.0267  0.0536  88  GLU   A OE2 
653  N  N   . TYR   A 83  ? 0.2911 0.2658 0.3584 -0.0073 0.0227  0.0311  89  TYR   A N   
654  C  CA  . TYR   A 83  ? 0.2767 0.2523 0.3467 -0.0073 0.0194  0.0264  89  TYR   A CA  
655  C  C   . TYR   A 83  ? 0.2647 0.2406 0.3442 -0.0099 0.0203  0.0207  89  TYR   A C   
656  O  O   . TYR   A 83  ? 0.2733 0.2480 0.3561 -0.0095 0.0190  0.0179  89  TYR   A O   
657  C  CB  . TYR   A 83  ? 0.2722 0.2522 0.3344 -0.0064 0.0157  0.0235  89  TYR   A CB  
658  C  CG  . TYR   A 83  ? 0.2816 0.2614 0.3341 -0.0039 0.0137  0.0278  89  TYR   A CG  
659  C  CD1 . TYR   A 83  ? 0.2993 0.2800 0.3444 -0.0035 0.0149  0.0297  89  TYR   A CD1 
660  C  CD2 . TYR   A 83  ? 0.2807 0.2594 0.3316 -0.0018 0.0107  0.0297  89  TYR   A CD2 
661  C  CE1 . TYR   A 83  ? 0.3178 0.2978 0.3527 -0.0011 0.0126  0.0328  89  TYR   A CE1 
662  C  CE2 . TYR   A 83  ? 0.2954 0.2741 0.3373 0.0005  0.0079  0.0330  89  TYR   A CE2 
663  C  CZ  . TYR   A 83  ? 0.3276 0.3065 0.3609 0.0008  0.0088  0.0345  89  TYR   A CZ  
664  O  OH  . TYR   A 83  ? 0.3774 0.3558 0.4007 0.0032  0.0057  0.0370  89  TYR   A OH  
665  N  N   . TYR   A 84  ? 0.2493 0.2270 0.3332 -0.0124 0.0224  0.0188  90  TYR   A N   
666  C  CA  . TYR   A 84  ? 0.2477 0.2259 0.3402 -0.0150 0.0224  0.0125  90  TYR   A CA  
667  C  C   . TYR   A 84  ? 0.2668 0.2443 0.3685 -0.0179 0.0259  0.0131  90  TYR   A C   
668  O  O   . TYR   A 84  ? 0.2600 0.2393 0.3602 -0.0181 0.0283  0.0168  90  TYR   A O   
669  C  CB  . TYR   A 84  ? 0.2301 0.2141 0.3186 -0.0154 0.0192  0.0067  90  TYR   A CB  
670  C  CG  . TYR   A 84  ? 0.2029 0.1879 0.2837 -0.0132 0.0161  0.0050  90  TYR   A CG  
671  C  CD1 . TYR   A 84  ? 0.2107 0.1937 0.2936 -0.0128 0.0152  0.0014  90  TYR   A CD1 
672  C  CD2 . TYR   A 84  ? 0.1989 0.1868 0.2706 -0.0116 0.0145  0.0066  90  TYR   A CD2 
673  C  CE1 . TYR   A 84  ? 0.1924 0.1765 0.2693 -0.0110 0.0132  0.0001  90  TYR   A CE1 
674  C  CE2 . TYR   A 84  ? 0.1881 0.1768 0.2542 -0.0100 0.0120  0.0051  90  TYR   A CE2 
675  C  CZ  . TYR   A 84  ? 0.1928 0.1799 0.2618 -0.0097 0.0116  0.0021  90  TYR   A CZ  
676  O  OH  . TYR   A 84  ? 0.1923 0.1803 0.2567 -0.0083 0.0100  0.0010  90  TYR   A OH  
677  N  N   . PRO   A 85  ? 0.2843 0.2596 0.3960 -0.0203 0.0263  0.0087  91  PRO   A N   
678  C  CA  . PRO   A 85  ? 0.2798 0.2558 0.4023 -0.0238 0.0291  0.0078  91  PRO   A CA  
679  C  C   . PRO   A 85  ? 0.2703 0.2540 0.3921 -0.0250 0.0268  0.0034  91  PRO   A C   
680  O  O   . PRO   A 85  ? 0.2702 0.2576 0.3840 -0.0232 0.0228  -0.0001 91  PRO   A O   
681  C  CB  . PRO   A 85  ? 0.2935 0.2650 0.4257 -0.0260 0.0288  0.0027  91  PRO   A CB  
682  C  CG  . PRO   A 85  ? 0.3116 0.2840 0.4365 -0.0238 0.0246  -0.0023 91  PRO   A CG  
683  C  CD  . PRO   A 85  ? 0.2893 0.2622 0.4031 -0.0201 0.0241  0.0033  91  PRO   A CD  
684  N  N   . ALA   A 86  ? 0.2571 0.2436 0.3887 -0.0279 0.0292  0.0031  92  ALA   A N   
685  C  CA  . ALA   A 86  ? 0.2662 0.2606 0.4000 -0.0290 0.0267  -0.0014 92  ALA   A CA  
686  C  C   . ALA   A 86  ? 0.2600 0.2557 0.3947 -0.0296 0.0213  -0.0100 92  ALA   A C   
687  O  O   . ALA   A 86  ? 0.2747 0.2655 0.4155 -0.0313 0.0211  -0.0132 92  ALA   A O   
688  C  CB  . ALA   A 86  ? 0.2761 0.2727 0.4242 -0.0326 0.0305  -0.0007 92  ALA   A CB  
689  N  N   . ARG   A 87  ? 0.2342 0.2350 0.3605 -0.0276 0.0171  -0.0134 93  ARG   A N   
690  C  CA  . ARG   A 87  ? 0.2218 0.2230 0.3458 -0.0274 0.0122  -0.0208 93  ARG   A CA  
691  C  C   . ARG   A 87  ? 0.2240 0.2319 0.3410 -0.0255 0.0082  -0.0237 93  ARG   A C   
692  O  O   . ARG   A 87  ? 0.2374 0.2491 0.3513 -0.0242 0.0093  -0.0199 93  ARG   A O   
693  C  CB  . ARG   A 87  ? 0.2248 0.2198 0.3402 -0.0250 0.0123  -0.0199 93  ARG   A CB  
694  C  CG  . ARG   A 87  ? 0.2377 0.2343 0.3400 -0.0215 0.0117  -0.0161 93  ARG   A CG  
695  C  CD  . ARG   A 87  ? 0.2390 0.2302 0.3362 -0.0195 0.0133  -0.0122 93  ARG   A CD  
696  N  NE  . ARG   A 87  ? 0.2442 0.2366 0.3305 -0.0167 0.0112  -0.0124 93  ARG   A NE  
697  C  CZ  . ARG   A 87  ? 0.2230 0.2181 0.3018 -0.0151 0.0107  -0.0091 93  ARG   A CZ  
698  N  NH1 . ARG   A 87  ? 0.2054 0.2008 0.2758 -0.0130 0.0091  -0.0095 93  ARG   A NH1 
699  N  NH2 . ARG   A 87  ? 0.2247 0.2222 0.3046 -0.0156 0.0121  -0.0058 93  ARG   A NH2 
700  N  N   . TYR   A 88  ? 0.2175 0.2262 0.3312 -0.0250 0.0036  -0.0303 94  TYR   A N   
701  C  CA  . TYR   A 88  ? 0.2261 0.2398 0.3309 -0.0223 -0.0002 -0.0323 94  TYR   A CA  
702  C  C   . TYR   A 88  ? 0.2122 0.2220 0.3035 -0.0191 0.0000  -0.0304 94  TYR   A C   
703  O  O   . TYR   A 88  ? 0.2231 0.2279 0.3123 -0.0189 0.0003  -0.0323 94  TYR   A O   
704  C  CB  . TYR   A 88  ? 0.2364 0.2531 0.3434 -0.0229 -0.0056 -0.0403 94  TYR   A CB  
705  C  CG  . TYR   A 88  ? 0.2594 0.2817 0.3811 -0.0261 -0.0067 -0.0426 94  TYR   A CG  
706  C  CD1 . TYR   A 88  ? 0.2778 0.3079 0.4014 -0.0252 -0.0087 -0.0423 94  TYR   A CD1 
707  C  CD2 . TYR   A 88  ? 0.2873 0.3070 0.4220 -0.0301 -0.0051 -0.0447 94  TYR   A CD2 
708  C  CE1 . TYR   A 88  ? 0.2950 0.3313 0.4341 -0.0282 -0.0094 -0.0443 94  TYR   A CE1 
709  C  CE2 . TYR   A 88  ? 0.3036 0.3287 0.4537 -0.0335 -0.0055 -0.0464 94  TYR   A CE2 
710  C  CZ  . TYR   A 88  ? 0.3185 0.3523 0.4711 -0.0326 -0.0077 -0.0463 94  TYR   A CZ  
711  O  OH  . TYR   A 88  ? 0.3540 0.3940 0.5240 -0.0361 -0.0080 -0.0482 94  TYR   A OH  
712  N  N   . GLN   A 89  ? 0.1879 0.1999 0.2713 -0.0168 0.0003  -0.0266 95  GLN   A N   
713  C  CA  . GLN   A 89  ? 0.1782 0.1873 0.2502 -0.0141 0.0003  -0.0249 95  GLN   A CA  
714  C  C   . GLN   A 89  ? 0.1795 0.1912 0.2439 -0.0119 -0.0034 -0.0289 95  GLN   A C   
715  O  O   . GLN   A 89  ? 0.1942 0.2110 0.2594 -0.0113 -0.0056 -0.0296 95  GLN   A O   
716  C  CB  . GLN   A 89  ? 0.1743 0.1832 0.2419 -0.0129 0.0027  -0.0186 95  GLN   A CB  
717  C  CG  . GLN   A 89  ? 0.1852 0.1915 0.2421 -0.0104 0.0024  -0.0171 95  GLN   A CG  
718  C  CD  . GLN   A 89  ? 0.1782 0.1828 0.2319 -0.0098 0.0045  -0.0116 95  GLN   A CD  
719  O  OE1 . GLN   A 89  ? 0.1913 0.1942 0.2497 -0.0108 0.0067  -0.0083 95  GLN   A OE1 
720  N  NE2 . GLN   A 89  ? 0.1636 0.1681 0.2090 -0.0078 0.0037  -0.0103 95  GLN   A NE2 
721  N  N   . SER   A 90  ? 0.1685 0.1768 0.2257 -0.0104 -0.0041 -0.0312 96  SER   A N   
722  C  CA  . SER   A 90  ? 0.1701 0.1797 0.2185 -0.0080 -0.0072 -0.0345 96  SER   A CA  
723  C  C   . SER   A 90  ? 0.1939 0.2026 0.2323 -0.0053 -0.0061 -0.0304 96  SER   A C   
724  O  O   . SER   A 90  ? 0.1875 0.1940 0.2256 -0.0056 -0.0031 -0.0259 96  SER   A O   
725  C  CB  . SER   A 90  ? 0.2086 0.2145 0.2538 -0.0076 -0.0079 -0.0395 96  SER   A CB  
726  O  OG  . SER   A 90  ? 0.2330 0.2339 0.2754 -0.0070 -0.0042 -0.0371 96  SER   A OG  
727  N  N   . HIS   A 91  ? 0.1824 0.1928 0.2129 -0.0028 -0.0087 -0.0319 97  HIS   A N   
728  C  CA  . HIS   A 91  ? 0.1805 0.1892 0.2014 -0.0002 -0.0076 -0.0284 97  HIS   A CA  
729  C  C   . HIS   A 91  ? 0.1724 0.1825 0.1957 -0.0006 -0.0061 -0.0237 97  HIS   A C   
730  O  O   . HIS   A 91  ? 0.1826 0.1899 0.2007 0.0003  -0.0042 -0.0204 97  HIS   A O   
731  C  CB  . HIS   A 91  ? 0.1966 0.2001 0.2123 0.0003  -0.0046 -0.0276 97  HIS   A CB  
732  C  CG  . HIS   A 91  ? 0.2380 0.2395 0.2490 0.0015  -0.0054 -0.0324 97  HIS   A CG  
733  N  ND1 . HIS   A 91  ? 0.2798 0.2799 0.2797 0.0046  -0.0060 -0.0331 97  HIS   A ND1 
734  C  CD2 . HIS   A 91  ? 0.2470 0.2473 0.2624 0.0001  -0.0056 -0.0366 97  HIS   A CD2 
735  C  CE1 . HIS   A 91  ? 0.2832 0.2814 0.2800 0.0052  -0.0067 -0.0379 97  HIS   A CE1 
736  N  NE2 . HIS   A 91  ? 0.2822 0.2803 0.2883 0.0025  -0.0066 -0.0405 97  HIS   A NE2 
737  N  N   . LEU   A 92  ? 0.1574 0.1716 0.1884 -0.0019 -0.0069 -0.0236 98  LEU   A N   
738  C  CA  . LEU   A 92  ? 0.1530 0.1682 0.1856 -0.0020 -0.0050 -0.0195 98  LEU   A CA  
739  C  C   . LEU   A 92  ? 0.1633 0.1822 0.1936 0.0004  -0.0069 -0.0195 98  LEU   A C   
740  O  O   . LEU   A 92  ? 0.1735 0.1966 0.2067 0.0010  -0.0100 -0.0227 98  LEU   A O   
741  C  CB  . LEU   A 92  ? 0.1629 0.1799 0.2060 -0.0048 -0.0033 -0.0188 98  LEU   A CB  
742  C  CG  . LEU   A 92  ? 0.1895 0.2067 0.2337 -0.0049 -0.0005 -0.0142 98  LEU   A CG  
743  C  CD1 . LEU   A 92  ? 0.2058 0.2181 0.2431 -0.0043 0.0011  -0.0108 98  LEU   A CD1 
744  C  CD2 . LEU   A 92  ? 0.2060 0.2246 0.2607 -0.0076 0.0017  -0.0133 98  LEU   A CD2 
745  N  N   . MET   A 93  ? 0.1639 0.1812 0.1893 0.0018  -0.0053 -0.0160 99  MET   A N   
746  C  CA  . MET   A 93  ? 0.1663 0.1861 0.1891 0.0046  -0.0066 -0.0155 99  MET   A CA  
747  C  C   . MET   A 93  ? 0.1690 0.1901 0.1955 0.0042  -0.0040 -0.0128 99  MET   A C   
748  O  O   . MET   A 93  ? 0.1828 0.2001 0.2067 0.0033  -0.0015 -0.0102 99  MET   A O   
749  C  CB  . MET   A 93  ? 0.1892 0.2043 0.2017 0.0069  -0.0065 -0.0140 99  MET   A CB  
750  C  CG  . MET   A 93  ? 0.2112 0.2244 0.2185 0.0077  -0.0080 -0.0161 99  MET   A CG  
751  S  SD  . MET   A 93  ? 0.2379 0.2448 0.2339 0.0100  -0.0066 -0.0137 99  MET   A SD  
752  C  CE  . MET   A 93  ? 0.2658 0.2687 0.2636 0.0071  -0.0032 -0.0110 99  MET   A CE  
753  N  N   . LEU   A 94  ? 0.1681 0.1947 0.2006 0.0052  -0.0045 -0.0134 100 LEU   A N   
754  C  CA  . LEU   A 94  ? 0.1768 0.2046 0.2123 0.0053  -0.0011 -0.0108 100 LEU   A CA  
755  C  C   . LEU   A 94  ? 0.1748 0.2022 0.2049 0.0088  -0.0009 -0.0096 100 LEU   A C   
756  O  O   . LEU   A 94  ? 0.1775 0.2067 0.2059 0.0114  -0.0038 -0.0111 100 LEU   A O   
757  C  CB  . LEU   A 94  ? 0.1865 0.2209 0.2345 0.0037  -0.0003 -0.0118 100 LEU   A CB  
758  C  CG  . LEU   A 94  ? 0.2293 0.2637 0.2845 0.0000  0.0003  -0.0126 100 LEU   A CG  
759  C  CD1 . LEU   A 94  ? 0.2378 0.2785 0.3068 -0.0018 0.0022  -0.0128 100 LEU   A CD1 
760  C  CD2 . LEU   A 94  ? 0.2513 0.2795 0.3017 -0.0014 0.0034  -0.0095 100 LEU   A CD2 
761  N  N   . ALA   A 95  ? 0.1772 0.2022 0.2048 0.0091  0.0026  -0.0071 101 ALA   A N   
762  C  CA  . ALA   A 95  ? 0.1698 0.1936 0.1927 0.0125  0.0036  -0.0062 101 ALA   A CA  
763  C  C   . ALA   A 95  ? 0.1641 0.1886 0.1890 0.0126  0.0079  -0.0042 101 ALA   A C   
764  O  O   . ALA   A 95  ? 0.1727 0.1964 0.1994 0.0101  0.0101  -0.0029 101 ALA   A O   
765  C  CB  . ALA   A 95  ? 0.1898 0.2061 0.2017 0.0134  0.0031  -0.0053 101 ALA   A CB  
766  N  N   . VAL   A 96  ? 0.1481 0.1738 0.1724 0.0159  0.0095  -0.0039 102 VAL   A N   
767  C  CA  . VAL   A 96  ? 0.1616 0.1867 0.1851 0.0167  0.0144  -0.0021 102 VAL   A CA  
768  C  C   . VAL   A 96  ? 0.1865 0.2029 0.1973 0.0173  0.0149  -0.0013 102 VAL   A C   
769  O  O   . VAL   A 96  ? 0.2128 0.2250 0.2171 0.0191  0.0128  -0.0022 102 VAL   A O   
770  C  CB  . VAL   A 96  ? 0.1595 0.1895 0.1881 0.0204  0.0161  -0.0025 102 VAL   A CB  
771  C  CG1 . VAL   A 96  ? 0.1692 0.1975 0.1949 0.0220  0.0219  -0.0007 102 VAL   A CG1 
772  C  CG2 . VAL   A 96  ? 0.1694 0.2088 0.2121 0.0195  0.0148  -0.0037 102 VAL   A CG2 
773  N  N   . GLY   A 97  ? 0.1849 0.1985 0.1924 0.0157  0.0174  0.0004  103 GLY   A N   
774  C  CA  . GLY   A 97  ? 0.1965 0.2024 0.1925 0.0159  0.0172  0.0008  103 GLY   A CA  
775  C  C   . GLY   A 97  ? 0.1973 0.2014 0.1908 0.0141  0.0191  0.0030  103 GLY   A C   
776  O  O   . GLY   A 97  ? 0.1968 0.2048 0.1977 0.0123  0.0209  0.0045  103 GLY   A O   
777  N  N   . HIS   A 98  ? 0.2084 0.2061 0.1913 0.0147  0.0187  0.0032  104 HIS   A N   
778  C  CA  . HIS   A 98  ? 0.2009 0.1961 0.1792 0.0138  0.0199  0.0055  104 HIS   A CA  
779  C  C   . HIS   A 98  ? 0.2058 0.2003 0.1862 0.0108  0.0165  0.0063  104 HIS   A C   
780  O  O   . HIS   A 98  ? 0.2211 0.2139 0.2010 0.0098  0.0127  0.0046  104 HIS   A O   
781  C  CB  . HIS   A 98  ? 0.2244 0.2129 0.1895 0.0158  0.0200  0.0050  104 HIS   A CB  
782  C  CG  . HIS   A 98  ? 0.2461 0.2322 0.2053 0.0156  0.0213  0.0078  104 HIS   A CG  
783  N  ND1 . HIS   A 98  ? 0.2618 0.2503 0.2230 0.0163  0.0267  0.0109  104 HIS   A ND1 
784  C  CD2 . HIS   A 98  ? 0.2566 0.2385 0.2090 0.0147  0.0176  0.0083  104 HIS   A CD2 
785  C  CE1 . HIS   A 98  ? 0.2866 0.2715 0.2405 0.0162  0.0264  0.0134  104 HIS   A CE1 
786  N  NE2 . HIS   A 98  ? 0.2681 0.2492 0.2166 0.0153  0.0205  0.0118  104 HIS   A NE2 
787  N  N   . SER   A 99  ? 0.2066 0.2021 0.1898 0.0095  0.0183  0.0091  105 SER   A N   
788  C  CA  . SER   A 99  ? 0.2086 0.2033 0.1943 0.0071  0.0157  0.0102  105 SER   A CA  
789  C  C   . SER   A 99  ? 0.2436 0.2367 0.2269 0.0073  0.0185  0.0142  105 SER   A C   
790  O  O   . SER   A 99  ? 0.2655 0.2602 0.2503 0.0082  0.0234  0.0161  105 SER   A O   
791  C  CB  . SER   A 99  ? 0.2376 0.2368 0.2347 0.0050  0.0150  0.0091  105 SER   A CB  
792  O  OG  . SER   A 99  ? 0.2473 0.2506 0.2519 0.0048  0.0191  0.0103  105 SER   A OG  
793  N  N   . GLU   A 100 ? 0.2184 0.2083 0.1978 0.0067  0.0156  0.0156  106 GLU   A N   
794  C  CA  . GLU   A 100 ? 0.2430 0.2307 0.2201 0.0069  0.0170  0.0198  106 GLU   A CA  
795  C  C   . GLU   A 100 ? 0.2695 0.2572 0.2526 0.0049  0.0134  0.0202  106 GLU   A C   
796  O  O   . GLU   A 100 ? 0.2660 0.2544 0.2514 0.0039  0.0097  0.0173  106 GLU   A O   
797  C  CB  . GLU   A 100 ? 0.2904 0.2731 0.2532 0.0094  0.0156  0.0209  106 GLU   A CB  
798  C  CG  . GLU   A 100 ? 0.2986 0.2805 0.2546 0.0118  0.0202  0.0210  106 GLU   A CG  
799  C  CD  . GLU   A 100 ? 0.3045 0.2809 0.2447 0.0146  0.0187  0.0211  106 GLU   A CD  
800  O  OE1 . GLU   A 100 ? 0.3529 0.3263 0.2869 0.0153  0.0166  0.0240  106 GLU   A OE1 
801  O  OE2 . GLU   A 100 ? 0.2901 0.2650 0.2239 0.0164  0.0196  0.0183  106 GLU   A OE2 
802  N  N   . PRO   A 101 ? 0.3028 0.2895 0.2890 0.0045  0.0150  0.0241  107 PRO   A N   
803  C  CA  . PRO   A 101 ? 0.3071 0.2941 0.3011 0.0027  0.0123  0.0241  107 PRO   A CA  
804  C  C   . PRO   A 101 ? 0.3046 0.2909 0.2964 0.0027  0.0065  0.0220  107 PRO   A C   
805  O  O   . PRO   A 101 ? 0.3253 0.3135 0.3243 0.0011  0.0048  0.0194  107 PRO   A O   
806  C  CB  . PRO   A 101 ? 0.3219 0.3063 0.3161 0.0034  0.0147  0.0294  107 PRO   A CB  
807  C  CG  . PRO   A 101 ? 0.3312 0.3156 0.3229 0.0042  0.0207  0.0318  107 PRO   A CG  
808  C  CD  . PRO   A 101 ? 0.3112 0.2967 0.2961 0.0054  0.0205  0.0285  107 PRO   A CD  
809  N  N   . GLY   A 102 ? 0.2644 0.2479 0.2460 0.0045  0.0036  0.0228  108 GLY   A N   
810  C  CA  . GLY   A 102 ? 0.2503 0.2332 0.2298 0.0045  -0.0020 0.0208  108 GLY   A CA  
811  C  C   . GLY   A 102 ? 0.2208 0.2050 0.2019 0.0032  -0.0033 0.0162  108 GLY   A C   
812  O  O   . GLY   A 102 ? 0.2322 0.2163 0.2141 0.0025  -0.0074 0.0143  108 GLY   A O   
813  N  N   . ASP   A 103 ? 0.1938 0.1794 0.1759 0.0031  0.0001  0.0146  109 ASP   A N   
814  C  CA  . ASP   A 103 ? 0.1848 0.1712 0.1683 0.0023  -0.0008 0.0108  109 ASP   A CA  
815  C  C   . ASP   A 103 ? 0.1855 0.1744 0.1782 0.0005  -0.0012 0.0094  109 ASP   A C   
816  O  O   . ASP   A 103 ? 0.1913 0.1801 0.1846 0.0000  -0.0023 0.0069  109 ASP   A O   
817  C  CB  . ASP   A 103 ? 0.1970 0.1842 0.1784 0.0034  0.0026  0.0097  109 ASP   A CB  
818  C  CG  . ASP   A 103 ? 0.2267 0.2105 0.1974 0.0055  0.0027  0.0095  109 ASP   A CG  
819  O  OD1 . ASP   A 103 ? 0.2396 0.2203 0.2046 0.0057  -0.0010 0.0085  109 ASP   A OD1 
820  O  OD2 . ASP   A 103 ? 0.2134 0.1979 0.1818 0.0070  0.0067  0.0103  109 ASP   A OD2 
821  N  N   . CYS   A 104 ? 0.1815 0.1717 0.1808 -0.0003 -0.0002 0.0111  110 CYS   A N   
822  C  CA  . CYS   A 104 ? 0.1764 0.1684 0.1836 -0.0017 -0.0003 0.0094  110 CYS   A CA  
823  C  C   . CYS   A 104 ? 0.1819 0.1732 0.1895 -0.0022 -0.0032 0.0084  110 CYS   A C   
824  O  O   . CYS   A 104 ? 0.1953 0.1854 0.2011 -0.0019 -0.0058 0.0098  110 CYS   A O   
825  C  CB  . CYS   A 104 ? 0.1827 0.1752 0.1966 -0.0023 0.0012  0.0113  110 CYS   A CB  
826  S  SG  . CYS   A 104 ? 0.2156 0.2098 0.2331 -0.0028 0.0052  0.0117  110 CYS   A SG  
827  N  N   . GLY   A 105 ? 0.1700 0.1621 0.1800 -0.0029 -0.0028 0.0060  111 GLY   A N   
828  C  CA  . GLY   A 105 ? 0.1759 0.1674 0.1876 -0.0036 -0.0046 0.0052  111 GLY   A CA  
829  C  C   . GLY   A 105 ? 0.1849 0.1745 0.1913 -0.0034 -0.0053 0.0036  111 GLY   A C   
830  O  O   . GLY   A 105 ? 0.1927 0.1817 0.2012 -0.0043 -0.0057 0.0027  111 GLY   A O   
831  N  N   . GLY   A 106 ? 0.1724 0.1608 0.1725 -0.0023 -0.0049 0.0033  112 GLY   A N   
832  C  CA  . GLY   A 106 ? 0.1600 0.1459 0.1552 -0.0019 -0.0052 0.0017  112 GLY   A CA  
833  C  C   . GLY   A 106 ? 0.1695 0.1558 0.1666 -0.0018 -0.0033 0.0006  112 GLY   A C   
834  O  O   . GLY   A 106 ? 0.1865 0.1752 0.1856 -0.0013 -0.0017 0.0004  112 GLY   A O   
835  N  N   . ILE   A 107 ? 0.1666 0.1501 0.1627 -0.0023 -0.0036 -0.0002 113 ILE   A N   
836  C  CA  . ILE   A 107 ? 0.1596 0.1427 0.1562 -0.0018 -0.0017 -0.0006 113 ILE   A CA  
837  C  C   . ILE   A 107 ? 0.1682 0.1501 0.1595 0.0004  -0.0007 -0.0012 113 ILE   A C   
838  O  O   . ILE   A 107 ? 0.1853 0.1644 0.1724 0.0011  -0.0013 -0.0016 113 ILE   A O   
839  C  CB  . ILE   A 107 ? 0.1936 0.1741 0.1927 -0.0033 -0.0015 -0.0005 113 ILE   A CB  
840  C  CG1 . ILE   A 107 ? 0.2142 0.1975 0.2206 -0.0049 -0.0016 0.0002  113 ILE   A CG1 
841  C  CG2 . ILE   A 107 ? 0.2247 0.2030 0.2216 -0.0023 0.0010  -0.0004 113 ILE   A CG2 
842  C  CD1 . ILE   A 107 ? 0.2529 0.2346 0.2643 -0.0068 -0.0015 0.0004  113 ILE   A CD1 
843  N  N   . LEU   A 108 ? 0.1631 0.1469 0.1546 0.0016  0.0006  -0.0015 114 LEU   A N   
844  C  CA  . LEU   A 108 ? 0.1641 0.1473 0.1514 0.0041  0.0011  -0.0018 114 LEU   A CA  
845  C  C   . LEU   A 108 ? 0.1855 0.1652 0.1706 0.0046  0.0023  -0.0012 114 LEU   A C   
846  O  O   . LEU   A 108 ? 0.1813 0.1618 0.1684 0.0038  0.0033  -0.0010 114 LEU   A O   
847  C  CB  . LEU   A 108 ? 0.1641 0.1522 0.1534 0.0052  0.0009  -0.0026 114 LEU   A CB  
848  C  CG  . LEU   A 108 ? 0.1748 0.1636 0.1609 0.0082  0.0007  -0.0031 114 LEU   A CG  
849  C  CD1 . LEU   A 108 ? 0.2013 0.1889 0.1851 0.0100  0.0008  -0.0028 114 LEU   A CD1 
850  C  CD2 . LEU   A 108 ? 0.1802 0.1745 0.1700 0.0086  -0.0003 -0.0046 114 LEU   A CD2 
851  N  N   . ARG   A 109 ? 0.1798 0.1551 0.1606 0.0061  0.0028  -0.0007 115 ARG   A N   
852  C  CA  . ARG   A 109 ? 0.1855 0.1565 0.1638 0.0067  0.0047  0.0006  115 ARG   A CA  
853  C  C   . ARG   A 109 ? 0.2102 0.1795 0.1832 0.0104  0.0048  0.0012  115 ARG   A C   
854  O  O   . ARG   A 109 ? 0.2095 0.1789 0.1812 0.0120  0.0039  0.0006  115 ARG   A O   
855  C  CB  . ARG   A 109 ? 0.2132 0.1788 0.1927 0.0046  0.0052  0.0011  115 ARG   A CB  
856  C  CG  . ARG   A 109 ? 0.2632 0.2299 0.2490 0.0012  0.0053  0.0011  115 ARG   A CG  
857  C  CD  . ARG   A 109 ? 0.2766 0.2387 0.2653 -0.0013 0.0050  0.0010  115 ARG   A CD  
858  N  NE  . ARG   A 109 ? 0.2998 0.2638 0.2962 -0.0043 0.0056  0.0015  115 ARG   A NE  
859  C  CZ  . ARG   A 109 ? 0.2964 0.2586 0.2958 -0.0051 0.0090  0.0031  115 ARG   A CZ  
860  N  NH1 . ARG   A 109 ? 0.2721 0.2300 0.2661 -0.0031 0.0122  0.0048  115 ARG   A NH1 
861  N  NH2 . ARG   A 109 ? 0.3299 0.2945 0.3375 -0.0076 0.0097  0.0034  115 ARG   A NH2 
862  N  N   . CYS   A 110 ? 0.2099 0.1770 0.1793 0.0121  0.0064  0.0027  116 CYS   A N   
863  C  CA  . CYS   A 110 ? 0.2181 0.1822 0.1817 0.0161  0.0066  0.0040  116 CYS   A CA  
864  C  C   . CYS   A 110 ? 0.2316 0.1878 0.1927 0.0157  0.0096  0.0066  116 CYS   A C   
865  O  O   . CYS   A 110 ? 0.2332 0.1875 0.1983 0.0122  0.0112  0.0067  116 CYS   A O   
866  C  CB  . CYS   A 110 ? 0.2283 0.1963 0.1886 0.0189  0.0054  0.0039  116 CYS   A CB  
867  S  SG  . CYS   A 110 ? 0.2135 0.1799 0.1709 0.0182  0.0080  0.0050  116 CYS   A SG  
868  N  N   . GLN   A 111 ? 0.2411 0.1928 0.1962 0.0194  0.0107  0.0088  117 GLN   A N   
869  C  CA  . GLN   A 111 ? 0.2481 0.1916 0.2011 0.0191  0.0143  0.0118  117 GLN   A CA  
870  C  C   . GLN   A 111 ? 0.2514 0.1944 0.2045 0.0174  0.0175  0.0134  117 GLN   A C   
871  O  O   . GLN   A 111 ? 0.2695 0.2062 0.2234 0.0160  0.0213  0.0158  117 GLN   A O   
872  C  CB  . GLN   A 111 ? 0.2867 0.2252 0.2327 0.0242  0.0148  0.0144  117 GLN   A CB  
873  C  CG  . GLN   A 111 ? 0.3657 0.3069 0.3048 0.0281  0.0142  0.0159  117 GLN   A CG  
874  C  CD  . GLN   A 111 ? 0.4970 0.4341 0.4292 0.0338  0.0138  0.0186  117 GLN   A CD  
875  O  OE1 . GLN   A 111 ? 0.5523 0.4942 0.4838 0.0372  0.0101  0.0173  117 GLN   A OE1 
876  N  NE2 . GLN   A 111 ? 0.4972 0.4257 0.4249 0.0349  0.0177  0.0226  117 GLN   A NE2 
877  N  N   . HIS   A 112 ? 0.2409 0.1900 0.1935 0.0176  0.0165  0.0121  118 HIS   A N   
878  C  CA  . HIS   A 112 ? 0.2414 0.1899 0.1931 0.0168  0.0201  0.0134  118 HIS   A CA  
879  C  C   . HIS   A 112 ? 0.2301 0.1819 0.1908 0.0122  0.0207  0.0117  118 HIS   A C   
880  O  O   . HIS   A 112 ? 0.2446 0.1954 0.2064 0.0112  0.0246  0.0130  118 HIS   A O   
881  C  CB  . HIS   A 112 ? 0.2436 0.1956 0.1881 0.0203  0.0188  0.0126  118 HIS   A CB  
882  C  CG  . HIS   A 112 ? 0.2612 0.2107 0.1967 0.0253  0.0173  0.0144  118 HIS   A CG  
883  N  ND1 . HIS   A 112 ? 0.2794 0.2342 0.2143 0.0278  0.0123  0.0121  118 HIS   A ND1 
884  C  CD2 . HIS   A 112 ? 0.2962 0.2387 0.2239 0.0285  0.0203  0.0185  118 HIS   A CD2 
885  C  CE1 . HIS   A 112 ? 0.3046 0.2560 0.2316 0.0325  0.0118  0.0146  118 HIS   A CE1 
886  N  NE2 . HIS   A 112 ? 0.3191 0.2625 0.2410 0.0333  0.0165  0.0187  118 HIS   A NE2 
887  N  N   . GLY   A 113 ? 0.2015 0.1573 0.1684 0.0099  0.0173  0.0090  119 GLY   A N   
888  C  CA  . GLY   A 113 ? 0.2072 0.1664 0.1826 0.0061  0.0172  0.0077  119 GLY   A CA  
889  C  C   . GLY   A 113 ? 0.1833 0.1487 0.1615 0.0056  0.0133  0.0049  119 GLY   A C   
890  O  O   . GLY   A 113 ? 0.2014 0.1683 0.1767 0.0073  0.0106  0.0038  119 GLY   A O   
891  N  N   . VAL   A 114 ? 0.1741 0.1431 0.1585 0.0033  0.0133  0.0039  120 VAL   A N   
892  C  CA  . VAL   A 114 ? 0.1745 0.1485 0.1622 0.0025  0.0103  0.0018  120 VAL   A CA  
893  C  C   . VAL   A 114 ? 0.1753 0.1524 0.1594 0.0048  0.0095  0.0004  120 VAL   A C   
894  O  O   . VAL   A 114 ? 0.1875 0.1644 0.1693 0.0058  0.0116  0.0003  120 VAL   A O   
895  C  CB  . VAL   A 114 ? 0.1817 0.1581 0.1776 -0.0002 0.0106  0.0016  120 VAL   A CB  
896  C  CG1 . VAL   A 114 ? 0.1947 0.1757 0.1935 -0.0006 0.0081  0.0001  120 VAL   A CG1 
897  C  CG2 . VAL   A 114 ? 0.1996 0.1741 0.2002 -0.0027 0.0099  0.0024  120 VAL   A CG2 
898  N  N   . VAL   A 115 ? 0.1748 0.1549 0.1587 0.0055  0.0067  -0.0009 121 VAL   A N   
899  C  CA  . VAL   A 115 ? 0.1755 0.1592 0.1578 0.0072  0.0052  -0.0028 121 VAL   A CA  
900  C  C   . VAL   A 115 ? 0.1883 0.1760 0.1771 0.0052  0.0043  -0.0045 121 VAL   A C   
901  O  O   . VAL   A 115 ? 0.1810 0.1707 0.1701 0.0056  0.0040  -0.0064 121 VAL   A O   
902  C  CB  . VAL   A 115 ? 0.1913 0.1763 0.1713 0.0092  0.0030  -0.0030 121 VAL   A CB  
903  C  CG1 . VAL   A 115 ? 0.2059 0.1960 0.1872 0.0104  0.0007  -0.0054 121 VAL   A CG1 
904  C  CG2 . VAL   A 115 ? 0.1951 0.1757 0.1684 0.0119  0.0039  -0.0012 121 VAL   A CG2 
905  N  N   . GLY   A 116 ? 0.1763 0.1647 0.1697 0.0032  0.0036  -0.0038 122 GLY   A N   
906  C  CA  . GLY   A 116 ? 0.1734 0.1648 0.1727 0.0016  0.0030  -0.0046 122 GLY   A CA  
907  C  C   . GLY   A 116 ? 0.1709 0.1623 0.1730 0.0002  0.0022  -0.0032 122 GLY   A C   
908  O  O   . GLY   A 116 ? 0.1736 0.1624 0.1735 0.0000  0.0019  -0.0021 122 GLY   A O   
909  N  N   . ILE   A 117 ? 0.1669 0.1605 0.1736 -0.0008 0.0018  -0.0032 123 ILE   A N   
910  C  CA  . ILE   A 117 ? 0.1606 0.1539 0.1687 -0.0018 0.0009  -0.0015 123 ILE   A CA  
911  C  C   . ILE   A 117 ? 0.1478 0.1434 0.1572 -0.0016 0.0009  -0.0013 123 ILE   A C   
912  O  O   . ILE   A 117 ? 0.1535 0.1512 0.1664 -0.0018 0.0015  -0.0026 123 ILE   A O   
913  C  CB  . ILE   A 117 ? 0.1805 0.1736 0.1937 -0.0031 0.0008  -0.0005 123 ILE   A CB  
914  C  CG1 . ILE   A 117 ? 0.1830 0.1775 0.2012 -0.0034 0.0020  -0.0015 123 ILE   A CG1 
915  C  CG2 . ILE   A 117 ? 0.2115 0.2027 0.2248 -0.0036 0.0007  -0.0001 123 ILE   A CG2 
916  C  CD1 . ILE   A 117 ? 0.2156 0.2101 0.2397 -0.0042 0.0019  0.0000  123 ILE   A CD1 
917  N  N   . VAL   A 118 ? 0.1469 0.1416 0.1536 -0.0013 0.0006  0.0002  124 VAL   A N   
918  C  CA  . VAL   A 118 ? 0.1507 0.1473 0.1589 -0.0012 0.0017  0.0011  124 VAL   A CA  
919  C  C   . VAL   A 118 ? 0.1519 0.1494 0.1664 -0.0025 0.0023  0.0020  124 VAL   A C   
920  O  O   . VAL   A 118 ? 0.1589 0.1549 0.1747 -0.0031 0.0015  0.0031  124 VAL   A O   
921  C  CB  . VAL   A 118 ? 0.1596 0.1543 0.1625 -0.0004 0.0016  0.0029  124 VAL   A CB  
922  C  CG1 . VAL   A 118 ? 0.1729 0.1693 0.1774 -0.0001 0.0039  0.0045  124 VAL   A CG1 
923  C  CG2 . VAL   A 118 ? 0.1886 0.1816 0.1855 0.0011  0.0013  0.0017  124 VAL   A CG2 
924  N  N   . SER   A 119 ? 0.1465 0.1466 0.1658 -0.0029 0.0036  0.0013  125 SER   A N   
925  C  CA  . SER   A 119 ? 0.1486 0.1488 0.1747 -0.0043 0.0046  0.0018  125 SER   A CA  
926  C  C   . SER   A 119 ? 0.1701 0.1717 0.2000 -0.0049 0.0068  0.0034  125 SER   A C   
927  O  O   . SER   A 119 ? 0.1786 0.1788 0.2129 -0.0058 0.0081  0.0054  125 SER   A O   
928  C  CB  . SER   A 119 ? 0.1668 0.1680 0.1967 -0.0049 0.0041  -0.0017 125 SER   A CB  
929  O  OG  . SER   A 119 ? 0.1787 0.1794 0.2156 -0.0063 0.0050  -0.0019 125 SER   A OG  
930  N  N   . THR   A 120 ? 0.1656 0.1697 0.1947 -0.0042 0.0077  0.0029  126 THR   A N   
931  C  CA  . THR   A 120 ? 0.1844 0.1903 0.2185 -0.0048 0.0107  0.0046  126 THR   A CA  
932  C  C   . THR   A 120 ? 0.1949 0.2017 0.2237 -0.0029 0.0122  0.0059  126 THR   A C   
933  O  O   . THR   A 120 ? 0.1885 0.1948 0.2109 -0.0013 0.0105  0.0046  126 THR   A O   
934  C  CB  . THR   A 120 ? 0.2088 0.2188 0.2528 -0.0064 0.0108  0.0015  126 THR   A CB  
935  O  OG1 . THR   A 120 ? 0.2183 0.2320 0.2613 -0.0051 0.0092  -0.0012 126 THR   A OG1 
936  C  CG2 . THR   A 120 ? 0.2217 0.2305 0.2704 -0.0080 0.0093  -0.0009 126 THR   A CG2 
937  N  N   . GLY   A 121 ? 0.2097 0.2177 0.2418 -0.0031 0.0159  0.0084  127 GLY   A N   
938  C  CA  . GLY   A 121 ? 0.2341 0.2434 0.2624 -0.0011 0.0183  0.0093  127 GLY   A CA  
939  C  C   . GLY   A 121 ? 0.2447 0.2574 0.2816 -0.0020 0.0229  0.0110  127 GLY   A C   
940  O  O   . GLY   A 121 ? 0.2471 0.2594 0.2909 -0.0041 0.0248  0.0127  127 GLY   A O   
941  N  N   . GLY   A 122 ? 0.2399 0.2558 0.2770 -0.0002 0.0250  0.0106  128 GLY   A N   
942  C  CA  . GLY   A 122 ? 0.2354 0.2554 0.2813 -0.0007 0.0302  0.0124  128 GLY   A CA  
943  C  C   . GLY   A 122 ? 0.2369 0.2562 0.2752 0.0025  0.0341  0.0143  128 GLY   A C   
944  O  O   . GLY   A 122 ? 0.2548 0.2692 0.2803 0.0046  0.0328  0.0147  128 GLY   A O   
945  N  N   . ASN   A 123 ? 0.2168 0.2411 0.2636 0.0028  0.0391  0.0153  129 ASN   A N   
946  C  CA  . ASN   A 123 ? 0.2164 0.2402 0.2567 0.0061  0.0438  0.0170  129 ASN   A CA  
947  C  C   . ASN   A 123 ? 0.2133 0.2397 0.2519 0.0087  0.0406  0.0132  129 ASN   A C   
948  O  O   . ASN   A 123 ? 0.2080 0.2414 0.2575 0.0092  0.0415  0.0116  129 ASN   A O   
949  C  CB  . ASN   A 123 ? 0.2385 0.2670 0.2903 0.0054  0.0512  0.0199  129 ASN   A CB  
950  C  CG  . ASN   A 123 ? 0.3139 0.3406 0.3577 0.0089  0.0579  0.0228  129 ASN   A CG  
951  O  OD1 . ASN   A 123 ? 0.3412 0.3621 0.3692 0.0119  0.0571  0.0227  129 ASN   A OD1 
952  N  ND2 . ASN   A 123 ? 0.3205 0.3525 0.3757 0.0087  0.0649  0.0249  129 ASN   A ND2 
953  N  N   . GLY   A 124 ? 0.2012 0.2219 0.2266 0.0104  0.0369  0.0119  130 GLY   A N   
954  C  CA  . GLY   A 124 ? 0.1981 0.2195 0.2208 0.0128  0.0337  0.0087  130 GLY   A CA  
955  C  C   . GLY   A 124 ? 0.1910 0.2147 0.2188 0.0112  0.0276  0.0057  130 GLY   A C   
956  O  O   . GLY   A 124 ? 0.2102 0.2360 0.2388 0.0132  0.0251  0.0033  130 GLY   A O   
957  N  N   . LEU   A 125 ? 0.1745 0.1974 0.2052 0.0080  0.0253  0.0058  131 LEU   A N   
958  C  CA  . LEU   A 125 ? 0.1639 0.1878 0.1973 0.0066  0.0200  0.0030  131 LEU   A CA  
959  C  C   . LEU   A 125 ? 0.1624 0.1799 0.1872 0.0054  0.0174  0.0034  131 LEU   A C   
960  O  O   . LEU   A 125 ? 0.1788 0.1927 0.1999 0.0046  0.0193  0.0061  131 LEU   A O   
961  C  CB  . LEU   A 125 ? 0.1572 0.1864 0.2038 0.0037  0.0194  0.0019  131 LEU   A CB  
962  C  CG  . LEU   A 125 ? 0.1809 0.2182 0.2394 0.0043  0.0207  0.0007  131 LEU   A CG  
963  C  CD1 . LEU   A 125 ? 0.2088 0.2505 0.2812 0.0006  0.0210  -0.0001 131 LEU   A CD1 
964  C  CD2 . LEU   A 125 ? 0.1788 0.2191 0.2366 0.0068  0.0161  -0.0026 131 LEU   A CD2 
965  N  N   . VAL   A 126 ? 0.1472 0.1636 0.1696 0.0055  0.0132  0.0011  132 VAL   A N   
966  C  CA  . VAL   A 126 ? 0.1407 0.1522 0.1576 0.0042  0.0108  0.0012  132 VAL   A CA  
967  C  C   . VAL   A 126 ? 0.1585 0.1721 0.1801 0.0031  0.0077  -0.0014 132 VAL   A C   
968  O  O   . VAL   A 126 ? 0.1680 0.1846 0.1910 0.0045  0.0060  -0.0035 132 VAL   A O   
969  C  CB  . VAL   A 126 ? 0.1685 0.1747 0.1750 0.0059  0.0097  0.0013  132 VAL   A CB  
970  C  CG1 . VAL   A 126 ? 0.1962 0.2028 0.2003 0.0083  0.0085  -0.0005 132 VAL   A CG1 
971  C  CG2 . VAL   A 126 ? 0.1794 0.1818 0.1830 0.0042  0.0072  0.0014  132 VAL   A CG2 
972  N  N   . GLY   A 127 ? 0.1580 0.1700 0.1817 0.0008  0.0071  -0.0013 133 GLY   A N   
973  C  CA  . GLY   A 127 ? 0.1609 0.1740 0.1878 -0.0001 0.0046  -0.0041 133 GLY   A CA  
974  C  C   . GLY   A 127 ? 0.1534 0.1620 0.1746 -0.0003 0.0033  -0.0040 133 GLY   A C   
975  O  O   . GLY   A 127 ? 0.1652 0.1708 0.1843 -0.0009 0.0040  -0.0018 133 GLY   A O   
976  N  N   . PHE   A 128 ? 0.1521 0.1607 0.1710 0.0005  0.0014  -0.0062 134 PHE   A N   
977  C  CA  . PHE   A 128 ? 0.1498 0.1545 0.1640 0.0005  0.0008  -0.0060 134 PHE   A CA  
978  C  C   . PHE   A 128 ? 0.1547 0.1597 0.1714 -0.0002 0.0002  -0.0084 134 PHE   A C   
979  O  O   . PHE   A 128 ? 0.1686 0.1761 0.1862 0.0005  -0.0013 -0.0110 134 PHE   A O   
980  C  CB  . PHE   A 128 ? 0.1598 0.1626 0.1671 0.0027  0.0001  -0.0061 134 PHE   A CB  
981  C  CG  . PHE   A 128 ? 0.1656 0.1675 0.1696 0.0040  0.0007  -0.0046 134 PHE   A CG  
982  C  CD1 . PHE   A 128 ? 0.1691 0.1673 0.1697 0.0035  0.0012  -0.0029 134 PHE   A CD1 
983  C  CD2 . PHE   A 128 ? 0.1717 0.1767 0.1764 0.0059  0.0006  -0.0052 134 PHE   A CD2 
984  C  CE1 . PHE   A 128 ? 0.1682 0.1648 0.1648 0.0048  0.0018  -0.0022 134 PHE   A CE1 
985  C  CE2 . PHE   A 128 ? 0.1750 0.1786 0.1763 0.0076  0.0017  -0.0041 134 PHE   A CE2 
986  C  CZ  . PHE   A 128 ? 0.1733 0.1724 0.1701 0.0070  0.0024  -0.0027 134 PHE   A CZ  
987  N  N   . ALA   A 129 ? 0.1502 0.1525 0.1678 -0.0014 0.0010  -0.0078 135 ALA   A N   
988  C  CA  . ALA   A 129 ? 0.1586 0.1603 0.1775 -0.0017 0.0010  -0.0101 135 ALA   A CA  
989  C  C   . ALA   A 129 ? 0.1555 0.1553 0.1674 0.0000  0.0010  -0.0105 135 ALA   A C   
990  O  O   . ALA   A 129 ? 0.1670 0.1643 0.1763 0.0001  0.0020  -0.0083 135 ALA   A O   
991  C  CB  . ALA   A 129 ? 0.1553 0.1550 0.1784 -0.0031 0.0024  -0.0087 135 ALA   A CB  
992  N  N   . ASP   A 130 ? 0.1571 0.1577 0.1659 0.0014  -0.0001 -0.0133 136 ASP   A N   
993  C  CA  . ASP   A 130 ? 0.1757 0.1739 0.1767 0.0035  0.0004  -0.0133 136 ASP   A CA  
994  C  C   . ASP   A 130 ? 0.1817 0.1769 0.1823 0.0030  0.0030  -0.0131 136 ASP   A C   
995  O  O   . ASP   A 130 ? 0.1862 0.1816 0.1913 0.0019  0.0036  -0.0149 136 ASP   A O   
996  C  CB  . ASP   A 130 ? 0.1942 0.1943 0.1912 0.0055  -0.0020 -0.0163 136 ASP   A CB  
997  C  CG  . ASP   A 130 ? 0.2632 0.2603 0.2505 0.0084  -0.0015 -0.0156 136 ASP   A CG  
998  O  OD1 . ASP   A 130 ? 0.2766 0.2720 0.2607 0.0094  -0.0007 -0.0127 136 ASP   A OD1 
999  O  OD2 . ASP   A 130 ? 0.3177 0.3138 0.3002 0.0097  -0.0016 -0.0180 136 ASP   A OD2 
1000 N  N   . VAL   A 131 ? 0.1761 0.1683 0.1718 0.0040  0.0050  -0.0110 137 VAL   A N   
1001 C  CA  . VAL   A 131 ? 0.1794 0.1691 0.1750 0.0039  0.0083  -0.0107 137 VAL   A CA  
1002 C  C   . VAL   A 131 ? 0.1884 0.1752 0.1747 0.0065  0.0101  -0.0107 137 VAL   A C   
1003 O  O   . VAL   A 131 ? 0.2081 0.1926 0.1935 0.0068  0.0137  -0.0101 137 VAL   A O   
1004 C  CB  . VAL   A 131 ? 0.1965 0.1852 0.1975 0.0021  0.0100  -0.0078 137 VAL   A CB  
1005 C  CG1 . VAL   A 131 ? 0.1959 0.1869 0.2046 0.0001  0.0083  -0.0075 137 VAL   A CG1 
1006 C  CG2 . VAL   A 131 ? 0.2052 0.1920 0.2027 0.0023  0.0101  -0.0053 137 VAL   A CG2 
1007 N  N   . ARG   A 132 ? 0.1943 0.1812 0.1739 0.0086  0.0079  -0.0108 138 ARG   A N   
1008 C  CA  . ARG   A 132 ? 0.2013 0.1847 0.1708 0.0116  0.0097  -0.0098 138 ARG   A CA  
1009 C  C   . ARG   A 132 ? 0.2234 0.2057 0.1870 0.0134  0.0108  -0.0125 138 ARG   A C   
1010 O  O   . ARG   A 132 ? 0.2323 0.2106 0.1874 0.0157  0.0140  -0.0109 138 ARG   A O   
1011 C  CB  . ARG   A 132 ? 0.1931 0.1770 0.1571 0.0140  0.0065  -0.0090 138 ARG   A CB  
1012 C  CG  . ARG   A 132 ? 0.2002 0.1835 0.1679 0.0128  0.0064  -0.0062 138 ARG   A CG  
1013 C  CD  . ARG   A 132 ? 0.2080 0.1921 0.1713 0.0157  0.0035  -0.0058 138 ARG   A CD  
1014 N  NE  . ARG   A 132 ? 0.2022 0.1920 0.1700 0.0155  -0.0004 -0.0088 138 ARG   A NE  
1015 C  CZ  . ARG   A 132 ? 0.2273 0.2198 0.1947 0.0176  -0.0035 -0.0091 138 ARG   A CZ  
1016 N  NH1 . ARG   A 132 ? 0.2223 0.2119 0.1836 0.0206  -0.0033 -0.0066 138 ARG   A NH1 
1017 N  NH2 . ARG   A 132 ? 0.2268 0.2251 0.2009 0.0167  -0.0064 -0.0118 138 ARG   A NH2 
1018 N  N   . ASP   A 133 ? 0.2173 0.2023 0.1848 0.0125  0.0086  -0.0166 139 ASP   A N   
1019 C  CA  . ASP   A 133 ? 0.2399 0.2233 0.2013 0.0143  0.0095  -0.0202 139 ASP   A CA  
1020 C  C   . ASP   A 133 ? 0.2370 0.2179 0.2017 0.0133  0.0147  -0.0199 139 ASP   A C   
1021 O  O   . ASP   A 133 ? 0.2562 0.2348 0.2145 0.0152  0.0167  -0.0227 139 ASP   A O   
1022 C  CB  . ASP   A 133 ? 0.2512 0.2380 0.2160 0.0136  0.0047  -0.0254 139 ASP   A CB  
1023 C  CG  . ASP   A 133 ? 0.2833 0.2722 0.2609 0.0099  0.0047  -0.0260 139 ASP   A CG  
1024 O  OD1 . ASP   A 133 ? 0.2823 0.2724 0.2663 0.0081  0.0053  -0.0224 139 ASP   A OD1 
1025 O  OD2 . ASP   A 133 ? 0.3329 0.3217 0.3137 0.0091  0.0043  -0.0301 139 ASP   A OD2 
1026 N  N   . LEU   A 134 ? 0.2284 0.2099 0.2025 0.0107  0.0169  -0.0169 140 LEU   A N   
1027 C  CA  . LEU   A 134 ? 0.2096 0.1900 0.1893 0.0099  0.0216  -0.0165 140 LEU   A CA  
1028 C  C   . LEU   A 134 ? 0.2158 0.1929 0.1906 0.0113  0.0271  -0.0132 140 LEU   A C   
1029 O  O   . LEU   A 134 ? 0.2130 0.1902 0.1938 0.0096  0.0290  -0.0094 140 LEU   A O   
1030 C  CB  . LEU   A 134 ? 0.2059 0.1890 0.1984 0.0067  0.0206  -0.0148 140 LEU   A CB  
1031 C  CG  . LEU   A 134 ? 0.2310 0.2168 0.2287 0.0052  0.0161  -0.0172 140 LEU   A CG  
1032 C  CD1 . LEU   A 134 ? 0.2373 0.2250 0.2452 0.0027  0.0154  -0.0145 140 LEU   A CD1 
1033 C  CD2 . LEU   A 134 ? 0.2455 0.2305 0.2433 0.0058  0.0162  -0.0218 140 LEU   A CD2 
1034 N  N   . LEU   A 135 ? 0.2303 0.2042 0.1934 0.0145  0.0294  -0.0145 141 LEU   A N   
1035 C  CA  . LEU   A 135 ? 0.2351 0.2051 0.1918 0.0162  0.0351  -0.0106 141 LEU   A CA  
1036 C  C   . LEU   A 135 ? 0.2469 0.2167 0.2124 0.0149  0.0414  -0.0085 141 LEU   A C   
1037 O  O   . LEU   A 135 ? 0.2596 0.2275 0.2261 0.0146  0.0459  -0.0042 141 LEU   A O   
1038 C  CB  . LEU   A 135 ? 0.2385 0.2047 0.1792 0.0205  0.0363  -0.0123 141 LEU   A CB  
1039 C  CG  . LEU   A 135 ? 0.2662 0.2335 0.1987 0.0223  0.0293  -0.0150 141 LEU   A CG  
1040 C  CD1 . LEU   A 135 ? 0.2788 0.2419 0.1937 0.0272  0.0305  -0.0158 141 LEU   A CD1 
1041 C  CD2 . LEU   A 135 ? 0.2743 0.2432 0.2094 0.0213  0.0256  -0.0116 141 LEU   A CD2 
1042 N  N   . TRP   A 136 ? 0.2457 0.2173 0.2185 0.0141  0.0420  -0.0116 142 TRP   A N   
1043 C  CA  . TRP   A 136 ? 0.2555 0.2277 0.2382 0.0132  0.0479  -0.0100 142 TRP   A CA  
1044 C  C   . TRP   A 136 ? 0.2687 0.2440 0.2649 0.0098  0.0470  -0.0062 142 TRP   A C   
1045 O  O   . TRP   A 136 ? 0.2926 0.2690 0.2980 0.0090  0.0518  -0.0042 142 TRP   A O   
1046 C  CB  . TRP   A 136 ? 0.2551 0.2281 0.2427 0.0136  0.0481  -0.0143 142 TRP   A CB  
1047 C  CG  . TRP   A 136 ? 0.2571 0.2329 0.2506 0.0116  0.0412  -0.0168 142 TRP   A CG  
1048 C  CD1 . TRP   A 136 ? 0.2675 0.2428 0.2546 0.0122  0.0363  -0.0209 142 TRP   A CD1 
1049 C  CD2 . TRP   A 136 ? 0.2553 0.2346 0.2625 0.0088  0.0387  -0.0151 142 TRP   A CD2 
1050 N  NE1 . TRP   A 136 ? 0.2690 0.2472 0.2659 0.0097  0.0319  -0.0216 142 TRP   A NE1 
1051 C  CE2 . TRP   A 136 ? 0.2628 0.2432 0.2710 0.0078  0.0333  -0.0179 142 TRP   A CE2 
1052 C  CE3 . TRP   A 136 ? 0.2574 0.2393 0.2764 0.0071  0.0406  -0.0116 142 TRP   A CE3 
1053 C  CZ2 . TRP   A 136 ? 0.2571 0.2402 0.2761 0.0056  0.0301  -0.0167 142 TRP   A CZ2 
1054 C  CZ3 . TRP   A 136 ? 0.2550 0.2400 0.2844 0.0050  0.0365  -0.0108 142 TRP   A CZ3 
1055 C  CH2 . TRP   A 136 ? 0.2574 0.2426 0.2863 0.0045  0.0318  -0.0132 142 TRP   A CH2 
1056 N  N   . LEU   A 137 ? 0.2547 0.2318 0.2526 0.0079  0.0410  -0.0055 143 LEU   A N   
1057 C  CA  . LEU   A 137 ? 0.2596 0.2392 0.2688 0.0048  0.0396  -0.0026 143 LEU   A CA  
1058 C  C   . LEU   A 137 ? 0.3053 0.2828 0.3152 0.0044  0.0445  0.0012  143 LEU   A C   
1059 O  O   . LEU   A 137 ? 0.3073 0.2871 0.3289 0.0019  0.0451  0.0032  143 LEU   A O   
1060 C  CB  . LEU   A 137 ? 0.2342 0.2150 0.2423 0.0035  0.0330  -0.0026 143 LEU   A CB  
1061 C  CG  . LEU   A 137 ? 0.2355 0.2190 0.2468 0.0029  0.0284  -0.0052 143 LEU   A CG  
1062 C  CD1 . LEU   A 137 ? 0.2555 0.2398 0.2642 0.0021  0.0231  -0.0050 143 LEU   A CD1 
1063 C  CD2 . LEU   A 137 ? 0.2285 0.2150 0.2529 0.0011  0.0283  -0.0046 143 LEU   A CD2 
1064 N  N   . ASP   A 138 ? 0.3429 0.3160 0.3404 0.0068  0.0476  0.0023  144 ASP   A N   
1065 C  CA  . ASP   A 138 ? 0.4059 0.3752 0.4008 0.0070  0.0528  0.0063  144 ASP   A CA  
1066 C  C   . ASP   A 138 ? 0.4579 0.4261 0.4554 0.0079  0.0613  0.0080  144 ASP   A C   
1067 O  O   . ASP   A 138 ? 0.4713 0.4362 0.4681 0.0076  0.0664  0.0118  144 ASP   A O   
1068 C  CB  . ASP   A 138 ? 0.4466 0.4111 0.4246 0.0104  0.0526  0.0067  144 ASP   A CB  
1069 C  CG  . ASP   A 138 ? 0.5391 0.5033 0.5130 0.0102  0.0462  0.0067  144 ASP   A CG  
1070 O  OD1 . ASP   A 138 ? 0.5583 0.5248 0.5415 0.0072  0.0428  0.0071  144 ASP   A OD1 
1071 O  OD2 . ASP   A 138 ? 0.6035 0.5654 0.5646 0.0134  0.0445  0.0061  144 ASP   A OD2 
1072 N  N   . GLU   A 139 ? 0.4885 0.4581 0.4867 0.0094  0.0636  0.0052  145 GLU   A N   
1073 C  CA  . GLU   A 139 ? 0.5301 0.4982 0.5295 0.0109  0.0727  0.0067  145 GLU   A CA  
1074 C  C   . GLU   A 139 ? 0.5461 0.5194 0.5633 0.0090  0.0747  0.0063  145 GLU   A C   
1075 O  O   . GLU   A 139 ? 0.5566 0.5338 0.5812 0.0077  0.0689  0.0037  145 GLU   A O   
1076 C  CB  . GLU   A 139 ? 0.5750 0.5392 0.5582 0.0155  0.0755  0.0039  145 GLU   A CB  
1077 C  CG  . GLU   A 139 ? 0.6474 0.6135 0.6291 0.0162  0.0697  -0.0017 145 GLU   A CG  
1078 C  CD  . GLU   A 139 ? 0.7462 0.7082 0.7094 0.0201  0.0684  -0.0051 145 GLU   A CD  
1079 O  OE1 . GLU   A 139 ? 0.7560 0.7174 0.7163 0.0220  0.0695  -0.0094 145 GLU   A OE1 
1080 O  OE2 . GLU   A 139 ? 0.7849 0.7443 0.7368 0.0213  0.0657  -0.0037 145 GLU   A OE2 
1081 N  N   . SER   B 1   ? 0.3635 0.3291 0.3423 0.0079  -0.0273 -0.0164 7   SER   C N   
1082 C  CA  . SER   B 1   ? 0.3644 0.3342 0.3552 0.0082  -0.0286 -0.0168 7   SER   C CA  
1083 C  C   . SER   B 1   ? 0.3484 0.3214 0.3437 0.0082  -0.0266 -0.0153 7   SER   C C   
1084 O  O   . SER   B 1   ? 0.3587 0.3295 0.3475 0.0080  -0.0259 -0.0137 7   SER   C O   
1085 C  CB  . SER   B 1   ? 0.3997 0.3669 0.3933 0.0089  -0.0350 -0.0183 7   SER   C CB  
1086 O  OG  . SER   B 1   ? 0.4598 0.4229 0.4480 0.0093  -0.0387 -0.0171 7   SER   C OG  
1087 N  N   . GLY   B 2   ? 0.3115 0.2892 0.3172 0.0082  -0.0254 -0.0158 8   GLY   C N   
1088 C  CA  . GLY   B 2   ? 0.2920 0.2725 0.3020 0.0081  -0.0233 -0.0151 8   GLY   C CA  
1089 C  C   . GLY   B 2   ? 0.2639 0.2499 0.2822 0.0072  -0.0194 -0.0154 8   GLY   C C   
1090 O  O   . GLY   B 2   ? 0.2654 0.2530 0.2846 0.0063  -0.0175 -0.0152 8   GLY   C O   
1091 N  N   . ALA   B 3   ? 0.2410 0.2294 0.2652 0.0074  -0.0182 -0.0160 9   ALA   C N   
1092 C  CA  . ALA   B 3   ? 0.2347 0.2280 0.2656 0.0061  -0.0140 -0.0164 9   ALA   C CA  
1093 C  C   . ALA   B 3   ? 0.2304 0.2249 0.2617 0.0059  -0.0110 -0.0167 9   ALA   C C   
1094 O  O   . ALA   B 3   ? 0.2494 0.2414 0.2796 0.0072  -0.0131 -0.0171 9   ALA   C O   
1095 C  CB  . ALA   B 3   ? 0.2422 0.2383 0.2840 0.0063  -0.0154 -0.0182 9   ALA   C CB  
1096 N  N   . ILE   B 4   ? 0.2145 0.2123 0.2470 0.0041  -0.0064 -0.0165 10  ILE   C N   
1097 C  CA  . ILE   B 4   ? 0.2011 0.2002 0.2340 0.0036  -0.0030 -0.0174 10  ILE   C CA  
1098 C  C   . ILE   B 4   ? 0.2141 0.2174 0.2573 0.0033  -0.0005 -0.0197 10  ILE   C C   
1099 O  O   . ILE   B 4   ? 0.2151 0.2210 0.2618 0.0019  0.0009  -0.0192 10  ILE   C O   
1100 C  CB  . ILE   B 4   ? 0.1942 0.1937 0.2199 0.0012  0.0005  -0.0155 10  ILE   C CB  
1101 C  CG1 . ILE   B 4   ? 0.2086 0.2050 0.2263 0.0013  -0.0015 -0.0133 10  ILE   C CG1 
1102 C  CG2 . ILE   B 4   ? 0.1974 0.1975 0.2224 0.0003  0.0040  -0.0170 10  ILE   C CG2 
1103 C  CD1 . ILE   B 4   ? 0.2315 0.2290 0.2445 -0.0009 0.0009  -0.0111 10  ILE   C CD1 
1104 N  N   . TYR   B 5   ? 0.2223 0.2262 0.2711 0.0047  0.0001  -0.0222 11  TYR   C N   
1105 C  CA  . TYR   B 5   ? 0.2219 0.2304 0.2816 0.0046  0.0032  -0.0248 11  TYR   C CA  
1106 C  C   . TYR   B 5   ? 0.2390 0.2484 0.2964 0.0034  0.0089  -0.0265 11  TYR   C C   
1107 O  O   . TYR   B 5   ? 0.2523 0.2590 0.3079 0.0049  0.0083  -0.0279 11  TYR   C O   
1108 C  CB  . TYR   B 5   ? 0.2231 0.2316 0.2933 0.0076  -0.0010 -0.0270 11  TYR   C CB  
1109 C  CG  . TYR   B 5   ? 0.2359 0.2433 0.3081 0.0084  -0.0070 -0.0257 11  TYR   C CG  
1110 C  CD1 . TYR   B 5   ? 0.2540 0.2653 0.3353 0.0076  -0.0070 -0.0262 11  TYR   C CD1 
1111 C  CD2 . TYR   B 5   ? 0.2683 0.2702 0.3324 0.0096  -0.0123 -0.0240 11  TYR   C CD2 
1112 C  CE1 . TYR   B 5   ? 0.2791 0.2887 0.3616 0.0081  -0.0128 -0.0254 11  TYR   C CE1 
1113 C  CE2 . TYR   B 5   ? 0.2856 0.2858 0.3498 0.0101  -0.0176 -0.0231 11  TYR   C CE2 
1114 C  CZ  . TYR   B 5   ? 0.3044 0.3082 0.3776 0.0094  -0.0181 -0.0240 11  TYR   C CZ  
1115 O  OH  . TYR   B 5   ? 0.3565 0.3577 0.4285 0.0097  -0.0236 -0.0235 11  TYR   C OH  
1116 N  N   . VAL   B 6   ? 0.2383 0.2507 0.2946 0.0005  0.0142  -0.0262 12  VAL   C N   
1117 C  CA  . VAL   B 6   ? 0.2583 0.2711 0.3101 -0.0012 0.0199  -0.0279 12  VAL   C CA  
1118 C  C   . VAL   B 6   ? 0.2741 0.2919 0.3329 -0.0032 0.0258  -0.0295 12  VAL   C C   
1119 O  O   . VAL   B 6   ? 0.2762 0.2960 0.3361 -0.0053 0.0265  -0.0273 12  VAL   C O   
1120 C  CB  . VAL   B 6   ? 0.2792 0.2888 0.3170 -0.0037 0.0201  -0.0248 12  VAL   C CB  
1121 C  CG1 . VAL   B 6   ? 0.2870 0.2972 0.3222 -0.0056 0.0190  -0.0211 12  VAL   C CG1 
1122 C  CG2 . VAL   B 6   ? 0.2958 0.3051 0.3274 -0.0060 0.0256  -0.0265 12  VAL   C CG2 
1123 N  N   . GLY   B 7   ? 0.2867 0.3067 0.3520 -0.0025 0.0303  -0.0337 13  GLY   C N   
1124 C  CA  . GLY   B 7   ? 0.2970 0.3225 0.3701 -0.0045 0.0368  -0.0357 13  GLY   C CA  
1125 C  C   . GLY   B 7   ? 0.2966 0.3261 0.3827 -0.0039 0.0342  -0.0349 13  GLY   C C   
1126 O  O   . GLY   B 7   ? 0.2952 0.3242 0.3889 -0.0005 0.0283  -0.0355 13  GLY   C O   
1127 N  N   . ASN   B 8   ? 0.2928 0.3253 0.3799 -0.0073 0.0376  -0.0330 14  ASN   C N   
1128 C  CA  . ASN   B 8   ? 0.2852 0.3210 0.3843 -0.0071 0.0345  -0.0320 14  ASN   C CA  
1129 C  C   . ASN   B 8   ? 0.2568 0.2890 0.3481 -0.0082 0.0294  -0.0275 14  ASN   C C   
1130 O  O   . ASN   B 8   ? 0.2585 0.2927 0.3553 -0.0100 0.0289  -0.0258 14  ASN   C O   
1131 C  CB  . ASN   B 8   ? 0.3197 0.3616 0.4288 -0.0100 0.0413  -0.0332 14  ASN   C CB  
1132 C  CG  . ASN   B 8   ? 0.4094 0.4559 0.5300 -0.0083 0.0462  -0.0384 14  ASN   C CG  
1133 O  OD1 . ASN   B 8   ? 0.4333 0.4815 0.5666 -0.0045 0.0422  -0.0410 14  ASN   C OD1 
1134 N  ND2 . ASN   B 8   ? 0.4370 0.4849 0.5529 -0.0110 0.0549  -0.0402 14  ASN   C ND2 
1135 N  N   . TYR   B 9   ? 0.2398 0.2667 0.3192 -0.0069 0.0254  -0.0257 15  TYR   C N   
1136 C  CA  . TYR   B 9   ? 0.2208 0.2442 0.2931 -0.0075 0.0209  -0.0220 15  TYR   C CA  
1137 C  C   . TYR   B 9   ? 0.2128 0.2327 0.2836 -0.0040 0.0140  -0.0221 15  TYR   C C   
1138 O  O   . TYR   B 9   ? 0.2168 0.2350 0.2861 -0.0017 0.0128  -0.0238 15  TYR   C O   
1139 C  CB  . TYR   B 9   ? 0.2282 0.2485 0.2864 -0.0099 0.0231  -0.0192 15  TYR   C CB  
1140 C  CG  . TYR   B 9   ? 0.2416 0.2639 0.2975 -0.0140 0.0294  -0.0182 15  TYR   C CG  
1141 C  CD1 . TYR   B 9   ? 0.2625 0.2872 0.3246 -0.0165 0.0309  -0.0167 15  TYR   C CD1 
1142 C  CD2 . TYR   B 9   ? 0.2621 0.2834 0.3091 -0.0158 0.0339  -0.0188 15  TYR   C CD2 
1143 C  CE1 . TYR   B 9   ? 0.2814 0.3073 0.3403 -0.0207 0.0368  -0.0152 15  TYR   C CE1 
1144 C  CE2 . TYR   B 9   ? 0.2867 0.3090 0.3294 -0.0201 0.0396  -0.0176 15  TYR   C CE2 
1145 C  CZ  . TYR   B 9   ? 0.3073 0.3320 0.3559 -0.0226 0.0413  -0.0157 15  TYR   C CZ  
1146 O  OH  . TYR   B 9   ? 0.3499 0.3750 0.3932 -0.0273 0.0471  -0.0139 15  TYR   C OH  
1147 N  N   . ARG   B 10  ? 0.1896 0.2075 0.2594 -0.0039 0.0097  -0.0200 16  ARG   C N   
1148 C  CA  . ARG   B 10  ? 0.1913 0.2052 0.2571 -0.0013 0.0036  -0.0196 16  ARG   C CA  
1149 C  C   . ARG   B 10  ? 0.1923 0.2031 0.2482 -0.0025 0.0030  -0.0166 16  ARG   C C   
1150 O  O   . ARG   B 10  ? 0.2081 0.2196 0.2657 -0.0045 0.0038  -0.0151 16  ARG   C O   
1151 C  CB  . ARG   B 10  ? 0.2031 0.2175 0.2782 0.0001  -0.0012 -0.0209 16  ARG   C CB  
1152 C  CG  . ARG   B 10  ? 0.2014 0.2110 0.2707 0.0018  -0.0073 -0.0202 16  ARG   C CG  
1153 C  CD  . ARG   B 10  ? 0.2277 0.2374 0.3059 0.0031  -0.0127 -0.0218 16  ARG   C CD  
1154 N  NE  . ARG   B 10  ? 0.2565 0.2624 0.3300 0.0030  -0.0168 -0.0210 16  ARG   C NE  
1155 C  CZ  . ARG   B 10  ? 0.3087 0.3099 0.3761 0.0048  -0.0222 -0.0214 16  ARG   C CZ  
1156 N  NH1 . ARG   B 10  ? 0.3010 0.3003 0.3659 0.0067  -0.0245 -0.0218 16  ARG   C NH1 
1157 N  NH2 . ARG   B 10  ? 0.3085 0.3062 0.3714 0.0045  -0.0251 -0.0212 16  ARG   C NH2 
1158 N  N   . VAL   B 11  ? 0.1856 0.1932 0.2322 -0.0016 0.0019  -0.0156 17  VAL   C N   
1159 C  CA  . VAL   B 11  ? 0.1794 0.1846 0.2181 -0.0024 0.0014  -0.0129 17  VAL   C CA  
1160 C  C   . VAL   B 11  ? 0.1882 0.1901 0.2243 -0.0002 -0.0032 -0.0131 17  VAL   C C   
1161 O  O   . VAL   B 11  ? 0.1998 0.1998 0.2334 0.0016  -0.0052 -0.0141 17  VAL   C O   
1162 C  CB  . VAL   B 11  ? 0.2037 0.2080 0.2341 -0.0032 0.0036  -0.0116 17  VAL   C CB  
1163 C  CG1 . VAL   B 11  ? 0.2104 0.2133 0.2354 -0.0042 0.0030  -0.0087 17  VAL   C CG1 
1164 C  CG2 . VAL   B 11  ? 0.2177 0.2244 0.2488 -0.0053 0.0081  -0.0122 17  VAL   C CG2 
1165 N  N   . VAL   B 12  ? 0.1675 0.1682 0.2038 -0.0004 -0.0047 -0.0123 18  VAL   C N   
1166 C  CA  . VAL   B 12  ? 0.1798 0.1770 0.2125 0.0014  -0.0084 -0.0130 18  VAL   C CA  
1167 C  C   . VAL   B 12  ? 0.1745 0.1702 0.2028 0.0011  -0.0078 -0.0113 18  VAL   C C   
1168 O  O   . VAL   B 12  ? 0.1727 0.1697 0.2025 -0.0006 -0.0057 -0.0095 18  VAL   C O   
1169 C  CB  . VAL   B 12  ? 0.1984 0.1951 0.2376 0.0020  -0.0120 -0.0149 18  VAL   C CB  
1170 C  CG1 . VAL   B 12  ? 0.2340 0.2320 0.2786 0.0030  -0.0136 -0.0166 18  VAL   C CG1 
1171 C  CG2 . VAL   B 12  ? 0.1890 0.1874 0.2347 0.0001  -0.0108 -0.0144 18  VAL   C CG2 
1172 N  N   . ASN   B 13  ? 0.1773 0.1697 0.2006 0.0026  -0.0098 -0.0120 19  ASN   C N   
1173 C  CA  . ASN   B 13  ? 0.1743 0.1653 0.1957 0.0028  -0.0094 -0.0113 19  ASN   C CA  
1174 C  C   . ASN   B 13  ? 0.1827 0.1733 0.2104 0.0021  -0.0106 -0.0119 19  ASN   C C   
1175 O  O   . ASN   B 13  ? 0.1901 0.1796 0.2208 0.0025  -0.0133 -0.0140 19  ASN   C O   
1176 C  CB  . ASN   B 13  ? 0.1782 0.1656 0.1933 0.0045  -0.0108 -0.0129 19  ASN   C CB  
1177 C  CG  . ASN   B 13  ? 0.2064 0.1938 0.2154 0.0048  -0.0095 -0.0119 19  ASN   C CG  
1178 O  OD1 . ASN   B 13  ? 0.2072 0.1934 0.2134 0.0051  -0.0109 -0.0125 19  ASN   C OD1 
1179 N  ND2 . ASN   B 13  ? 0.1971 0.1857 0.2046 0.0045  -0.0070 -0.0104 19  ASN   C ND2 
1180 N  N   . ARG   B 14  ? 0.1703 0.1614 0.2003 0.0010  -0.0090 -0.0100 20  ARG   C N   
1181 C  CA  . ARG   B 14  ? 0.1684 0.1587 0.2046 0.0001  -0.0102 -0.0101 20  ARG   C CA  
1182 C  C   . ARG   B 14  ? 0.1807 0.1670 0.2166 0.0017  -0.0134 -0.0132 20  ARG   C C   
1183 O  O   . ARG   B 14  ? 0.1835 0.1690 0.2245 0.0010  -0.0156 -0.0146 20  ARG   C O   
1184 C  CB  . ARG   B 14  ? 0.1787 0.1689 0.2162 -0.0011 -0.0087 -0.0072 20  ARG   C CB  
1185 C  CG  . ARG   B 14  ? 0.2024 0.1916 0.2466 -0.0030 -0.0096 -0.0063 20  ARG   C CG  
1186 C  CD  . ARG   B 14  ? 0.2039 0.1917 0.2484 -0.0037 -0.0090 -0.0031 20  ARG   C CD  
1187 N  NE  . ARG   B 14  ? 0.1930 0.1791 0.2433 -0.0058 -0.0098 -0.0013 20  ARG   C NE  
1188 C  CZ  . ARG   B 14  ? 0.2186 0.2009 0.2729 -0.0051 -0.0121 -0.0028 20  ARG   C CZ  
1189 N  NH1 . ARG   B 14  ? 0.2202 0.2002 0.2728 -0.0022 -0.0137 -0.0066 20  ARG   C NH1 
1190 N  NH2 . ARG   B 14  ? 0.2296 0.2100 0.2892 -0.0074 -0.0128 -0.0006 20  ARG   C NH2 
1191 N  N   . HIS   B 15  ? 0.1798 0.1637 0.2094 0.0036  -0.0133 -0.0144 21  HIS   C N   
1192 C  CA  . HIS   B 15  ? 0.1962 0.1756 0.2235 0.0049  -0.0158 -0.0177 21  HIS   C CA  
1193 C  C   . HIS   B 15  ? 0.2047 0.1826 0.2298 0.0052  -0.0192 -0.0200 21  HIS   C C   
1194 O  O   . HIS   B 15  ? 0.2266 0.2005 0.2502 0.0058  -0.0222 -0.0228 21  HIS   C O   
1195 C  CB  . HIS   B 15  ? 0.1972 0.1745 0.2187 0.0067  -0.0141 -0.0187 21  HIS   C CB  
1196 C  CG  . HIS   B 15  ? 0.2065 0.1841 0.2201 0.0074  -0.0129 -0.0188 21  HIS   C CG  
1197 N  ND1 . HIS   B 15  ? 0.2074 0.1885 0.2202 0.0070  -0.0103 -0.0160 21  HIS   C ND1 
1198 C  CD2 . HIS   B 15  ? 0.2251 0.1992 0.2310 0.0084  -0.0139 -0.0213 21  HIS   C CD2 
1199 C  CE1 . HIS   B 15  ? 0.2330 0.2130 0.2385 0.0076  -0.0098 -0.0168 21  HIS   C CE1 
1200 N  NE2 . HIS   B 15  ? 0.2400 0.2156 0.2406 0.0084  -0.0119 -0.0197 21  HIS   C NE2 
1201 N  N   . LEU   B 16  ? 0.1906 0.1712 0.2156 0.0049  -0.0191 -0.0189 22  LEU   C N   
1202 C  CA  . LEU   B 16  ? 0.1974 0.1766 0.2216 0.0053  -0.0231 -0.0207 22  LEU   C CA  
1203 C  C   . LEU   B 16  ? 0.2206 0.2033 0.2551 0.0040  -0.0244 -0.0205 22  LEU   C C   
1204 O  O   . LEU   B 16  ? 0.2314 0.2139 0.2678 0.0045  -0.0280 -0.0217 22  LEU   C O   
1205 C  CB  . LEU   B 16  ? 0.2122 0.1912 0.2292 0.0061  -0.0226 -0.0199 22  LEU   C CB  
1206 C  CG  . LEU   B 16  ? 0.2354 0.2112 0.2423 0.0070  -0.0209 -0.0202 22  LEU   C CG  
1207 C  CD1 . LEU   B 16  ? 0.2513 0.2267 0.2517 0.0073  -0.0205 -0.0190 22  LEU   C CD1 
1208 C  CD2 . LEU   B 16  ? 0.2612 0.2315 0.2626 0.0077  -0.0238 -0.0232 22  LEU   C CD2 
1209 N  N   . ALA   B 17  ? 0.2087 0.1948 0.2503 0.0024  -0.0216 -0.0188 23  ALA   C N   
1210 C  CA  . ALA   B 17  ? 0.2135 0.2035 0.2652 0.0009  -0.0215 -0.0186 23  ALA   C CA  
1211 C  C   . ALA   B 17  ? 0.2167 0.2050 0.2742 0.0007  -0.0264 -0.0210 23  ALA   C C   
1212 O  O   . ALA   B 17  ? 0.2278 0.2119 0.2829 0.0008  -0.0287 -0.0222 23  ALA   C O   
1213 C  CB  . ALA   B 17  ? 0.2084 0.2011 0.2646 -0.0014 -0.0175 -0.0161 23  ALA   C CB  
1214 N  N   . THR   B 18  ? 0.2091 0.2006 0.2746 0.0004  -0.0282 -0.0218 24  THR   C N   
1215 C  CA  . THR   B 18  ? 0.2149 0.2052 0.2874 0.0000  -0.0337 -0.0240 24  THR   C CA  
1216 C  C   . THR   B 18  ? 0.2108 0.2042 0.2949 -0.0027 -0.0323 -0.0234 24  THR   C C   
1217 O  O   . THR   B 18  ? 0.2109 0.2075 0.2972 -0.0043 -0.0269 -0.0211 24  THR   C O   
1218 C  CB  . THR   B 18  ? 0.2365 0.2292 0.3141 0.0012  -0.0369 -0.0250 24  THR   C CB  
1219 O  OG1 . THR   B 18  ? 0.2487 0.2480 0.3363 0.0001  -0.0324 -0.0241 24  THR   C OG1 
1220 C  CG2 . THR   B 18  ? 0.2528 0.2423 0.3193 0.0034  -0.0381 -0.0249 24  THR   C CG2 
1221 N  N   . HIS   B 19  ? 0.2115 0.2039 0.3033 -0.0035 -0.0375 -0.0254 25  HIS   C N   
1222 C  CA  . HIS   B 19  ? 0.2248 0.2205 0.3288 -0.0065 -0.0361 -0.0247 25  HIS   C CA  
1223 C  C   . HIS   B 19  ? 0.2112 0.2147 0.3249 -0.0078 -0.0310 -0.0233 25  HIS   C C   
1224 O  O   . HIS   B 19  ? 0.2172 0.2237 0.3363 -0.0105 -0.0262 -0.0213 25  HIS   C O   
1225 C  CB  . HIS   B 19  ? 0.2706 0.2647 0.3827 -0.0072 -0.0431 -0.0273 25  HIS   C CB  
1226 C  CG  . HIS   B 19  ? 0.3842 0.3702 0.4875 -0.0065 -0.0479 -0.0293 25  HIS   C CG  
1227 N  ND1 . HIS   B 19  ? 0.4364 0.4188 0.5366 -0.0075 -0.0458 -0.0287 25  HIS   C ND1 
1228 C  CD2 . HIS   B 19  ? 0.4324 0.4134 0.5303 -0.0051 -0.0548 -0.0322 25  HIS   C CD2 
1229 C  CE1 . HIS   B 19  ? 0.4501 0.4254 0.5432 -0.0065 -0.0509 -0.0316 25  HIS   C CE1 
1230 N  NE2 . HIS   B 19  ? 0.4632 0.4373 0.5537 -0.0051 -0.0563 -0.0338 25  HIS   C NE2 
1231 N  N   . ASN   B 20  ? 0.2100 0.2162 0.3251 -0.0058 -0.0319 -0.0244 26  ASN   C N   
1232 C  CA  . ASN   B 20  ? 0.2055 0.2187 0.3297 -0.0066 -0.0267 -0.0239 26  ASN   C CA  
1233 C  C   . ASN   B 20  ? 0.2028 0.2171 0.3191 -0.0073 -0.0194 -0.0215 26  ASN   C C   
1234 O  O   . ASN   B 20  ? 0.2068 0.2259 0.3293 -0.0096 -0.0137 -0.0205 26  ASN   C O   
1235 C  CB  . ASN   B 20  ? 0.2429 0.2580 0.3710 -0.0039 -0.0298 -0.0258 26  ASN   C CB  
1236 C  CG  . ASN   B 20  ? 0.3267 0.3432 0.4674 -0.0040 -0.0362 -0.0278 26  ASN   C CG  
1237 O  OD1 . ASN   B 20  ? 0.3471 0.3675 0.5001 -0.0066 -0.0351 -0.0279 26  ASN   C OD1 
1238 N  ND2 . ASN   B 20  ? 0.3616 0.3745 0.4991 -0.0014 -0.0433 -0.0292 26  ASN   C ND2 
1239 N  N   . ASP   B 21  ? 0.2006 0.2103 0.3030 -0.0056 -0.0195 -0.0206 27  ASP   C N   
1240 C  CA  . ASP   B 21  ? 0.2036 0.2138 0.2983 -0.0064 -0.0135 -0.0182 27  ASP   C CA  
1241 C  C   . ASP   B 21  ? 0.2147 0.2249 0.3110 -0.0097 -0.0104 -0.0157 27  ASP   C C   
1242 O  O   . ASP   B 21  ? 0.2289 0.2421 0.3258 -0.0120 -0.0049 -0.0139 27  ASP   C O   
1243 C  CB  . ASP   B 21  ? 0.2064 0.2116 0.2876 -0.0042 -0.0150 -0.0177 27  ASP   C CB  
1244 C  CG  . ASP   B 21  ? 0.2301 0.2348 0.3071 -0.0016 -0.0165 -0.0190 27  ASP   C CG  
1245 O  OD1 . ASP   B 21  ? 0.2547 0.2633 0.3360 -0.0016 -0.0137 -0.0194 27  ASP   C OD1 
1246 O  OD2 . ASP   B 21  ? 0.2308 0.2310 0.3002 0.0003  -0.0205 -0.0197 27  ASP   C OD2 
1247 N  N   . TRP   B 22  ? 0.2056 0.2119 0.3025 -0.0101 -0.0142 -0.0158 28  TRP   C N   
1248 C  CA  . TRP   B 22  ? 0.2110 0.2162 0.3097 -0.0132 -0.0122 -0.0132 28  TRP   C CA  
1249 C  C   . TRP   B 22  ? 0.2178 0.2279 0.3290 -0.0167 -0.0094 -0.0126 28  TRP   C C   
1250 O  O   . TRP   B 22  ? 0.2318 0.2427 0.3431 -0.0199 -0.0050 -0.0096 28  TRP   C O   
1251 C  CB  . TRP   B 22  ? 0.2099 0.2091 0.3067 -0.0124 -0.0171 -0.0141 28  TRP   C CB  
1252 C  CG  . TRP   B 22  ? 0.2009 0.1957 0.2861 -0.0103 -0.0171 -0.0133 28  TRP   C CG  
1253 C  CD1 . TRP   B 22  ? 0.2109 0.2024 0.2884 -0.0071 -0.0200 -0.0155 28  TRP   C CD1 
1254 C  CD2 . TRP   B 22  ? 0.1927 0.1859 0.2734 -0.0114 -0.0142 -0.0099 28  TRP   C CD2 
1255 N  NE1 . TRP   B 22  ? 0.2204 0.2091 0.2900 -0.0061 -0.0185 -0.0140 28  TRP   C NE1 
1256 C  CE2 . TRP   B 22  ? 0.2047 0.1943 0.2765 -0.0085 -0.0153 -0.0105 28  TRP   C CE2 
1257 C  CE3 . TRP   B 22  ? 0.2074 0.2016 0.2905 -0.0147 -0.0108 -0.0062 28  TRP   C CE3 
1258 C  CZ2 . TRP   B 22  ? 0.2065 0.1941 0.2736 -0.0085 -0.0137 -0.0078 28  TRP   C CZ2 
1259 C  CZ3 . TRP   B 22  ? 0.2127 0.2040 0.2896 -0.0149 -0.0096 -0.0031 28  TRP   C CZ3 
1260 C  CH2 . TRP   B 22  ? 0.2059 0.1944 0.2757 -0.0117 -0.0112 -0.0040 28  TRP   C CH2 
1261 N  N   . ALA   B 23  ? 0.2102 0.2238 0.3317 -0.0162 -0.0118 -0.0154 29  ALA   C N   
1262 C  CA  . ALA   B 23  ? 0.2243 0.2437 0.3595 -0.0195 -0.0087 -0.0152 29  ALA   C CA  
1263 C  C   . ALA   B 23  ? 0.2387 0.2637 0.3746 -0.0207 -0.0011 -0.0144 29  ALA   C C   
1264 O  O   . ALA   B 23  ? 0.2578 0.2877 0.4029 -0.0242 0.0037  -0.0136 29  ALA   C O   
1265 C  CB  . ALA   B 23  ? 0.2111 0.2327 0.3582 -0.0183 -0.0142 -0.0185 29  ALA   C CB  
1266 N  N   . ASN   B 24  ? 0.2165 0.2411 0.3434 -0.0179 0.0000  -0.0151 30  ASN   C N   
1267 C  CA  . ASN   B 24  ? 0.2069 0.2359 0.3327 -0.0186 0.0068  -0.0151 30  ASN   C CA  
1268 C  C   . ASN   B 24  ? 0.2142 0.2393 0.3244 -0.0188 0.0094  -0.0124 30  ASN   C C   
1269 O  O   . ASN   B 24  ? 0.2132 0.2392 0.3176 -0.0177 0.0123  -0.0131 30  ASN   C O   
1270 C  CB  . ASN   B 24  ? 0.2098 0.2416 0.3404 -0.0151 0.0053  -0.0187 30  ASN   C CB  
1271 C  CG  . ASN   B 24  ? 0.2516 0.2882 0.3994 -0.0152 0.0029  -0.0211 30  ASN   C CG  
1272 O  OD1 . ASN   B 24  ? 0.2552 0.2979 0.4141 -0.0176 0.0083  -0.0217 30  ASN   C OD1 
1273 N  ND2 . ASN   B 24  ? 0.2374 0.2711 0.3878 -0.0130 -0.0051 -0.0225 30  ASN   C ND2 
1274 N  N   . LEU   B 25  ? 0.2162 0.2369 0.3207 -0.0204 0.0082  -0.0094 31  LEU   C N   
1275 C  CA  . LEU   B 25  ? 0.2162 0.2330 0.3074 -0.0205 0.0093  -0.0065 31  LEU   C CA  
1276 C  C   . LEU   B 25  ? 0.2276 0.2465 0.3137 -0.0235 0.0159  -0.0046 31  LEU   C C   
1277 O  O   . LEU   B 25  ? 0.2434 0.2647 0.3343 -0.0274 0.0201  -0.0031 31  LEU   C O   
1278 C  CB  . LEU   B 25  ? 0.2188 0.2307 0.3082 -0.0218 0.0063  -0.0038 31  LEU   C CB  
1279 C  CG  . LEU   B 25  ? 0.2389 0.2466 0.3167 -0.0218 0.0063  -0.0005 31  LEU   C CG  
1280 C  CD1 . LEU   B 25  ? 0.2467 0.2526 0.3172 -0.0176 0.0035  -0.0023 31  LEU   C CD1 
1281 C  CD2 . LEU   B 25  ? 0.2553 0.2583 0.3340 -0.0229 0.0034  0.0020  31  LEU   C CD2 
1282 N  N   . VAL   B 26  ? 0.2145 0.2320 0.2901 -0.0221 0.0169  -0.0044 32  VAL   C N   
1283 C  CA  . VAL   B 26  ? 0.2280 0.2460 0.2956 -0.0250 0.0223  -0.0025 32  VAL   C CA  
1284 C  C   . VAL   B 26  ? 0.2429 0.2558 0.2997 -0.0260 0.0203  0.0018  32  VAL   C C   
1285 O  O   . VAL   B 26  ? 0.2703 0.2819 0.3227 -0.0299 0.0230  0.0054  32  VAL   C O   
1286 C  CB  . VAL   B 26  ? 0.2460 0.2660 0.3102 -0.0229 0.0245  -0.0056 32  VAL   C CB  
1287 C  CG1 . VAL   B 26  ? 0.2480 0.2670 0.3011 -0.0259 0.0294  -0.0037 32  VAL   C CG1 
1288 C  CG2 . VAL   B 26  ? 0.2466 0.2718 0.3230 -0.0220 0.0268  -0.0096 32  VAL   C CG2 
1289 N  N   . TRP   B 27  ? 0.2189 0.2288 0.2719 -0.0226 0.0155  0.0015  33  TRP   C N   
1290 C  CA  . TRP   B 27  ? 0.2174 0.2231 0.2621 -0.0228 0.0132  0.0050  33  TRP   C CA  
1291 C  C   . TRP   B 27  ? 0.2160 0.2194 0.2613 -0.0188 0.0081  0.0037  33  TRP   C C   
1292 O  O   . TRP   B 27  ? 0.2117 0.2164 0.2585 -0.0159 0.0070  0.0003  33  TRP   C O   
1293 C  CB  . TRP   B 27  ? 0.2317 0.2374 0.2663 -0.0237 0.0156  0.0059  33  TRP   C CB  
1294 C  CG  . TRP   B 27  ? 0.2447 0.2468 0.2716 -0.0233 0.0125  0.0090  33  TRP   C CG  
1295 C  CD1 . TRP   B 27  ? 0.2791 0.2782 0.3013 -0.0262 0.0117  0.0136  33  TRP   C CD1 
1296 C  CD2 . TRP   B 27  ? 0.2325 0.2338 0.2559 -0.0201 0.0097  0.0079  33  TRP   C CD2 
1297 N  NE1 . TRP   B 27  ? 0.2881 0.2850 0.3057 -0.0244 0.0081  0.0152  33  TRP   C NE1 
1298 C  CE2 . TRP   B 27  ? 0.2549 0.2534 0.2733 -0.0209 0.0072  0.0117  33  TRP   C CE2 
1299 C  CE3 . TRP   B 27  ? 0.2334 0.2360 0.2582 -0.0167 0.0087  0.0043  33  TRP   C CE3 
1300 C  CZ2 . TRP   B 27  ? 0.2494 0.2473 0.2647 -0.0185 0.0046  0.0116  33  TRP   C CZ2 
1301 C  CZ3 . TRP   B 27  ? 0.2460 0.2473 0.2665 -0.0146 0.0063  0.0045  33  TRP   C CZ3 
1302 C  CH2 . TRP   B 27  ? 0.2454 0.2447 0.2617 -0.0155 0.0045  0.0080  33  TRP   C CH2 
1303 N  N   . GLU   B 28  ? 0.2149 0.2147 0.2587 -0.0187 0.0053  0.0063  34  GLU   C N   
1304 C  CA  . GLU   B 28  ? 0.2133 0.2109 0.2565 -0.0150 0.0014  0.0049  34  GLU   C CA  
1305 C  C   . GLU   B 28  ? 0.2160 0.2106 0.2551 -0.0151 -0.0003 0.0083  34  GLU   C C   
1306 O  O   . GLU   B 28  ? 0.2249 0.2179 0.2634 -0.0180 0.0001  0.0121  34  GLU   C O   
1307 C  CB  . GLU   B 28  ? 0.2334 0.2297 0.2836 -0.0133 -0.0014 0.0022  34  GLU   C CB  
1308 C  CG  . GLU   B 28  ? 0.2455 0.2400 0.3018 -0.0158 -0.0020 0.0041  34  GLU   C CG  
1309 C  CD  . GLU   B 28  ? 0.2976 0.2877 0.3528 -0.0159 -0.0042 0.0071  34  GLU   C CD  
1310 O  OE1 . GLU   B 28  ? 0.3515 0.3399 0.4089 -0.0190 -0.0037 0.0104  34  GLU   C OE1 
1311 O  OE2 . GLU   B 28  ? 0.2448 0.2330 0.2970 -0.0129 -0.0062 0.0063  34  GLU   C OE2 
1312 N  N   . ASP   B 29  ? 0.1983 0.1921 0.2348 -0.0121 -0.0021 0.0073  35  ASP   C N   
1313 C  CA  . ASP   B 29  ? 0.1891 0.1807 0.2238 -0.0117 -0.0040 0.0102  35  ASP   C CA  
1314 C  C   . ASP   B 29  ? 0.1926 0.1831 0.2293 -0.0078 -0.0060 0.0075  35  ASP   C C   
1315 O  O   . ASP   B 29  ? 0.1983 0.1902 0.2319 -0.0059 -0.0055 0.0053  35  ASP   C O   
1316 C  CB  . ASP   B 29  ? 0.2082 0.2011 0.2361 -0.0130 -0.0030 0.0125  35  ASP   C CB  
1317 C  CG  . ASP   B 29  ? 0.2853 0.2764 0.3124 -0.0130 -0.0056 0.0160  35  ASP   C CG  
1318 O  OD1 . ASP   B 29  ? 0.3112 0.3006 0.3432 -0.0106 -0.0078 0.0157  35  ASP   C OD1 
1319 O  OD2 . ASP   B 29  ? 0.2980 0.2892 0.3197 -0.0153 -0.0056 0.0190  35  ASP   C OD2 
1320 N  N   . SER   B 30  ? 0.1879 0.1752 0.2296 -0.0069 -0.0080 0.0074  36  SER   C N   
1321 C  CA  A SER   B 30  ? 0.1951 0.1807 0.2384 -0.0034 -0.0093 0.0044  36  SER   C CA  
1322 C  CA  B SER   B 30  ? 0.1923 0.1780 0.2355 -0.0034 -0.0093 0.0043  36  SER   C CA  
1323 C  C   . SER   B 30  ? 0.2052 0.1922 0.2463 -0.0017 -0.0091 0.0053  36  SER   C C   
1324 O  O   . SER   B 30  ? 0.2206 0.2080 0.2602 0.0008  -0.0085 0.0023  36  SER   C O   
1325 C  CB  A SER   B 30  ? 0.2261 0.2077 0.2754 -0.0030 -0.0114 0.0043  36  SER   C CB  
1326 C  CB  B SER   B 30  ? 0.2148 0.1963 0.2639 -0.0027 -0.0114 0.0040  36  SER   C CB  
1327 O  OG  A SER   B 30  ? 0.2551 0.2347 0.3057 0.0004  -0.0121 0.0010  36  SER   C OG  
1328 O  OG  B SER   B 30  ? 0.2272 0.2070 0.2787 -0.0037 -0.0126 0.0081  36  SER   C OG  
1329 N  N   . SER   B 31  ? 0.1859 0.1733 0.2265 -0.0034 -0.0097 0.0095  37  SER   C N   
1330 C  CA  . SER   B 31  ? 0.1922 0.1813 0.2323 -0.0020 -0.0101 0.0106  37  SER   C CA  
1331 C  C   . SER   B 31  ? 0.1978 0.1901 0.2322 -0.0020 -0.0081 0.0091  37  SER   C C   
1332 O  O   . SER   B 31  ? 0.2182 0.2122 0.2529 -0.0006 -0.0080 0.0089  37  SER   C O   
1333 C  CB  . SER   B 31  ? 0.2288 0.2171 0.2695 -0.0040 -0.0123 0.0157  37  SER   C CB  
1334 O  OG  . SER   B 31  ? 0.2983 0.2880 0.3325 -0.0073 -0.0115 0.0180  37  SER   C OG  
1335 N  N   . ARG   B 32  ? 0.1765 0.1696 0.2068 -0.0035 -0.0066 0.0081  38  ARG   C N   
1336 C  CA  . ARG   B 32  ? 0.1741 0.1695 0.1994 -0.0034 -0.0051 0.0066  38  ARG   C CA  
1337 C  C   . ARG   B 32  ? 0.1772 0.1723 0.2018 -0.0016 -0.0043 0.0026  38  ARG   C C   
1338 O  O   . ARG   B 32  ? 0.1734 0.1697 0.1940 -0.0013 -0.0034 0.0014  38  ARG   C O   
1339 C  CB  . ARG   B 32  ? 0.1793 0.1758 0.2006 -0.0064 -0.0039 0.0080  38  ARG   C CB  
1340 C  CG  . ARG   B 32  ? 0.1733 0.1696 0.1925 -0.0088 -0.0050 0.0122  38  ARG   C CG  
1341 C  CD  . ARG   B 32  ? 0.1741 0.1707 0.1876 -0.0121 -0.0033 0.0133  38  ARG   C CD  
1342 N  NE  . ARG   B 32  ? 0.1711 0.1694 0.1804 -0.0118 -0.0018 0.0110  38  ARG   C NE  
1343 C  CZ  . ARG   B 32  ? 0.1856 0.1840 0.1888 -0.0143 -0.0007 0.0117  38  ARG   C CZ  
1344 N  NH1 . ARG   B 32  ? 0.2151 0.2123 0.2148 -0.0175 -0.0007 0.0147  38  ARG   C NH1 
1345 N  NH2 . ARG   B 32  ? 0.1939 0.1932 0.1941 -0.0138 0.0004  0.0094  38  ARG   C NH2 
1346 N  N   . ASP   B 33  ? 0.1780 0.1710 0.2058 -0.0006 -0.0052 0.0007  39  ASP   C N   
1347 C  CA  . ASP   B 33  ? 0.1685 0.1606 0.1951 0.0007  -0.0054 -0.0029 39  ASP   C CA  
1348 C  C   . ASP   B 33  ? 0.1612 0.1550 0.1864 -0.0006 -0.0047 -0.0033 39  ASP   C C   
1349 O  O   . ASP   B 33  ? 0.1693 0.1628 0.1919 0.0005  -0.0051 -0.0055 39  ASP   C O   
1350 C  CB  . ASP   B 33  ? 0.1861 0.1775 0.2088 0.0030  -0.0050 -0.0050 39  ASP   C CB  
1351 C  CG  . ASP   B 33  ? 0.1882 0.1774 0.2083 0.0042  -0.0061 -0.0084 39  ASP   C CG  
1352 O  OD1 . ASP   B 33  ? 0.1857 0.1730 0.2089 0.0042  -0.0078 -0.0100 39  ASP   C OD1 
1353 O  OD2 . ASP   B 33  ? 0.1935 0.1825 0.2084 0.0048  -0.0056 -0.0094 39  ASP   C OD2 
1354 N  N   . LEU   B 34  ? 0.1615 0.1567 0.1886 -0.0030 -0.0038 -0.0013 40  LEU   C N   
1355 C  CA  . LEU   B 34  ? 0.1687 0.1658 0.1958 -0.0041 -0.0025 -0.0023 40  LEU   C CA  
1356 C  C   . LEU   B 34  ? 0.1717 0.1694 0.2047 -0.0057 -0.0022 -0.0025 40  LEU   C C   
1357 O  O   . LEU   B 34  ? 0.1772 0.1740 0.2124 -0.0073 -0.0022 -0.0003 40  LEU   C O   
1358 C  CB  . LEU   B 34  ? 0.1712 0.1700 0.1942 -0.0061 -0.0003 -0.0003 40  LEU   C CB  
1359 C  CG  . LEU   B 34  ? 0.1964 0.1952 0.2141 -0.0052 -0.0003 -0.0002 40  LEU   C CG  
1360 C  CD1 . LEU   B 34  ? 0.1978 0.1978 0.2115 -0.0076 0.0015  0.0013  40  LEU   C CD1 
1361 C  CD2 . LEU   B 34  ? 0.2008 0.1994 0.2176 -0.0033 -0.0008 -0.0032 40  LEU   C CD2 
1362 N  N   . LEU   B 35  ? 0.1625 0.1618 0.1984 -0.0055 -0.0019 -0.0049 41  LEU   C N   
1363 C  CA  . LEU   B 35  ? 0.1650 0.1660 0.2079 -0.0072 -0.0011 -0.0053 41  LEU   C CA  
1364 C  C   . LEU   B 35  ? 0.1653 0.1694 0.2097 -0.0074 0.0011  -0.0070 41  LEU   C C   
1365 O  O   . LEU   B 35  ? 0.1724 0.1763 0.2149 -0.0053 -0.0001 -0.0089 41  LEU   C O   
1366 C  CB  . LEU   B 35  ? 0.1725 0.1718 0.2208 -0.0061 -0.0045 -0.0073 41  LEU   C CB  
1367 C  CG  . LEU   B 35  ? 0.1846 0.1859 0.2421 -0.0081 -0.0041 -0.0078 41  LEU   C CG  
1368 C  CD1 . LEU   B 35  ? 0.1981 0.1964 0.2597 -0.0081 -0.0074 -0.0082 41  LEU   C CD1 
1369 C  CD2 . LEU   B 35  ? 0.1961 0.2004 0.2590 -0.0073 -0.0045 -0.0106 41  LEU   C CD2 
1370 N  N   . VAL   B 36  ? 0.1715 0.1783 0.2195 -0.0101 0.0046  -0.0063 42  VAL   C N   
1371 C  CA  . VAL   B 36  ? 0.1799 0.1901 0.2311 -0.0104 0.0076  -0.0084 42  VAL   C CA  
1372 C  C   . VAL   B 36  ? 0.1861 0.1993 0.2481 -0.0118 0.0086  -0.0095 42  VAL   C C   
1373 O  O   . VAL   B 36  ? 0.1928 0.2060 0.2569 -0.0145 0.0099  -0.0074 42  VAL   C O   
1374 C  CB  . VAL   B 36  ? 0.1935 0.2045 0.2382 -0.0129 0.0122  -0.0070 42  VAL   C CB  
1375 C  CG1 . VAL   B 36  ? 0.2128 0.2272 0.2614 -0.0130 0.0161  -0.0099 42  VAL   C CG1 
1376 C  CG2 . VAL   B 36  ? 0.1995 0.2077 0.2345 -0.0117 0.0107  -0.0057 42  VAL   C CG2 
1377 N  N   . SER   B 37  ? 0.1828 0.1982 0.2521 -0.0099 0.0074  -0.0127 43  SER   C N   
1378 C  CA  . SER   B 37  ? 0.1884 0.2077 0.2702 -0.0110 0.0081  -0.0142 43  SER   C CA  
1379 C  C   . SER   B 37  ? 0.2049 0.2287 0.2925 -0.0109 0.0124  -0.0167 43  SER   C C   
1380 O  O   . SER   B 37  ? 0.2100 0.2332 0.2921 -0.0093 0.0135  -0.0178 43  SER   C O   
1381 C  CB  . SER   B 37  ? 0.1888 0.2067 0.2766 -0.0087 0.0018  -0.0159 43  SER   C CB  
1382 O  OG  . SER   B 37  ? 0.2045 0.2212 0.2905 -0.0054 -0.0015 -0.0180 43  SER   C OG  
1383 N  N   . SER   B 38  ? 0.2133 0.2419 0.3128 -0.0128 0.0152  -0.0178 44  SER   C N   
1384 C  CA  . SER   B 38  ? 0.2399 0.2734 0.3468 -0.0126 0.0201  -0.0207 44  SER   C CA  
1385 C  C   . SER   B 38  ? 0.2654 0.3009 0.3839 -0.0090 0.0156  -0.0241 44  SER   C C   
1386 O  O   . SER   B 38  ? 0.2751 0.3099 0.3996 -0.0080 0.0096  -0.0242 44  SER   C O   
1387 C  CB  . SER   B 38  ? 0.2727 0.3108 0.3864 -0.0168 0.0267  -0.0202 44  SER   C CB  
1388 O  OG  . SER   B 38  ? 0.3323 0.3722 0.4573 -0.0177 0.0236  -0.0199 44  SER   C OG  
1389 N  N   . THR   B 39  ? 0.2809 0.3183 0.4018 -0.0070 0.0180  -0.0270 45  THR   C N   
1390 C  CA  . THR   B 39  ? 0.3177 0.3567 0.4500 -0.0034 0.0135  -0.0300 45  THR   C CA  
1391 C  C   . THR   B 39  ? 0.3576 0.4035 0.5040 -0.0036 0.0197  -0.0335 45  THR   C C   
1392 O  O   . THR   B 39  ? 0.3631 0.4113 0.5065 -0.0062 0.0278  -0.0338 45  THR   C O   
1393 C  CB  . THR   B 39  ? 0.3484 0.3824 0.4712 0.0000  0.0100  -0.0305 45  THR   C CB  
1394 O  OG1 . THR   B 39  ? 0.3784 0.4131 0.4972 -0.0003 0.0163  -0.0320 45  THR   C OG1 
1395 C  CG2 . THR   B 39  ? 0.3554 0.3831 0.4632 -0.0001 0.0059  -0.0273 45  THR   C CG2 
1396 N  N   . THR   B 40  ? 0.3841 0.4331 0.5457 -0.0008 0.0158  -0.0362 46  THR   C N   
1397 C  CA  . THR   B 40  ? 0.4132 0.4691 0.5904 -0.0003 0.0214  -0.0400 46  THR   C CA  
1398 C  C   . THR   B 40  ? 0.4416 0.4955 0.6163 0.0032  0.0222  -0.0428 46  THR   C C   
1399 O  O   . THR   B 40  ? 0.4588 0.5163 0.6375 0.0029  0.0301  -0.0458 46  THR   C O   
1400 C  CB  . THR   B 40  ? 0.4315 0.4924 0.6288 0.0008  0.0166  -0.0414 46  THR   C CB  
1401 O  OG1 . THR   B 40  ? 0.4613 0.5172 0.6573 0.0043  0.0060  -0.0409 46  THR   C OG1 
1402 C  CG2 . THR   B 40  ? 0.4357 0.4990 0.6369 -0.0033 0.0172  -0.0391 46  THR   C CG2 
1403 N  N   . ALA   B 41  ? 0.4478 0.4954 0.6153 0.0064  0.0143  -0.0418 47  ALA   C N   
1404 C  CA  . ALA   B 41  ? 0.4523 0.4970 0.6174 0.0096  0.0141  -0.0440 47  ALA   C CA  
1405 C  C   . ALA   B 41  ? 0.4589 0.4990 0.6056 0.0081  0.0188  -0.0430 47  ALA   C C   
1406 O  O   . ALA   B 41  ? 0.4705 0.5079 0.6040 0.0054  0.0189  -0.0396 47  ALA   C O   
1407 C  CB  . ALA   B 41  ? 0.4619 0.5013 0.6268 0.0132  0.0036  -0.0430 47  ALA   C CB  
1408 N  N   . GLN   B 42  ? 0.4497 0.4889 0.5962 0.0098  0.0222  -0.0461 48  GLN   C N   
1409 C  CA  . GLN   B 42  ? 0.4453 0.4801 0.5753 0.0083  0.0263  -0.0457 48  GLN   C CA  
1410 C  C   . GLN   B 42  ? 0.4123 0.4396 0.5299 0.0099  0.0191  -0.0429 48  GLN   C C   
1411 O  O   . GLN   B 42  ? 0.4260 0.4506 0.5487 0.0133  0.0132  -0.0436 48  GLN   C O   
1412 C  CB  . GLN   B 42  ? 0.4923 0.5287 0.6273 0.0096  0.0327  -0.0508 48  GLN   C CB  
1413 C  CG  . GLN   B 42  ? 0.5826 0.6146 0.7007 0.0074  0.0375  -0.0509 48  GLN   C CG  
1414 C  CD  . GLN   B 42  ? 0.6737 0.7085 0.7844 0.0026  0.0453  -0.0501 48  GLN   C CD  
1415 O  OE1 . GLN   B 42  ? 0.6980 0.7383 0.8166 0.0006  0.0482  -0.0495 48  GLN   C OE1 
1416 N  NE2 . GLN   B 42  ? 0.6945 0.7251 0.7893 0.0004  0.0484  -0.0498 48  GLN   C NE2 
1417 N  N   . GLY   B 43  ? 0.3612 0.3852 0.4634 0.0072  0.0194  -0.0394 49  GLY   C N   
1418 C  CA  . GLY   B 43  ? 0.3387 0.3562 0.4285 0.0080  0.0138  -0.0366 49  GLY   C CA  
1419 C  C   . GLY   B 43  ? 0.3131 0.3269 0.3944 0.0081  0.0165  -0.0380 49  GLY   C C   
1420 O  O   . GLY   B 43  ? 0.3142 0.3299 0.3927 0.0059  0.0233  -0.0398 49  GLY   C O   
1421 N  N   . CYS   B 44  ? 0.2988 0.3072 0.3756 0.0101  0.0115  -0.0373 50  CYS   C N   
1422 C  CA  . CYS   B 44  ? 0.3007 0.3051 0.3706 0.0101  0.0137  -0.0390 50  CYS   C CA  
1423 C  C   . CYS   B 44  ? 0.2928 0.2924 0.3478 0.0083  0.0116  -0.0355 50  CYS   C C   
1424 O  O   . CYS   B 44  ? 0.3065 0.3017 0.3565 0.0087  0.0114  -0.0365 50  CYS   C O   
1425 C  CB  . CYS   B 44  ? 0.3244 0.3263 0.4032 0.0139  0.0106  -0.0418 50  CYS   C CB  
1426 S  SG  . CYS   B 44  ? 0.4015 0.4099 0.5002 0.0163  0.0141  -0.0469 50  CYS   C SG  
1427 N  N   . ASP   B 45  ? 0.2544 0.2545 0.3035 0.0066  0.0098  -0.0316 51  ASP   C N   
1428 C  CA  . ASP   B 45  ? 0.2508 0.2469 0.2873 0.0050  0.0082  -0.0285 51  ASP   C CA  
1429 C  C   . ASP   B 45  ? 0.2641 0.2607 0.2931 0.0020  0.0131  -0.0290 51  ASP   C C   
1430 O  O   . ASP   B 45  ? 0.2874 0.2876 0.3177 0.0002  0.0176  -0.0298 51  ASP   C O   
1431 C  CB  . ASP   B 45  ? 0.2463 0.2429 0.2792 0.0042  0.0052  -0.0247 51  ASP   C CB  
1432 C  CG  . ASP   B 45  ? 0.3181 0.3127 0.3547 0.0067  -0.0005 -0.0238 51  ASP   C CG  
1433 O  OD1 . ASP   B 45  ? 0.3469 0.3389 0.3873 0.0089  -0.0032 -0.0252 51  ASP   C OD1 
1434 O  OD2 . ASP   B 45  ? 0.3200 0.3154 0.3558 0.0064  -0.0025 -0.0218 51  ASP   C OD2 
1435 N  N   . THR   B 46  ? 0.2518 0.2443 0.2728 0.0013  0.0122  -0.0284 52  THR   C N   
1436 C  CA  . THR   B 46  ? 0.2791 0.2710 0.2913 -0.0018 0.0156  -0.0286 52  THR   C CA  
1437 C  C   . THR   B 46  ? 0.2542 0.2460 0.2590 -0.0039 0.0135  -0.0240 52  THR   C C   
1438 O  O   . THR   B 46  ? 0.2648 0.2545 0.2680 -0.0031 0.0096  -0.0217 52  THR   C O   
1439 C  CB  . THR   B 46  ? 0.3480 0.3350 0.3561 -0.0016 0.0152  -0.0307 52  THR   C CB  
1440 O  OG1 . THR   B 46  ? 0.3897 0.3768 0.4050 0.0002  0.0181  -0.0356 52  THR   C OG1 
1441 C  CG2 . THR   B 46  ? 0.3731 0.3583 0.3702 -0.0052 0.0169  -0.0301 52  THR   C CG2 
1442 N  N   . ILE   B 47  ? 0.2340 0.2279 0.2344 -0.0067 0.0162  -0.0227 53  ILE   C N   
1443 C  CA  . ILE   B 47  ? 0.2232 0.2171 0.2178 -0.0086 0.0140  -0.0184 53  ILE   C CA  
1444 C  C   . ILE   B 47  ? 0.2148 0.2059 0.2006 -0.0109 0.0135  -0.0178 53  ILE   C C   
1445 O  O   . ILE   B 47  ? 0.2195 0.2095 0.2009 -0.0127 0.0165  -0.0201 53  ILE   C O   
1446 C  CB  . ILE   B 47  ? 0.2453 0.2423 0.2400 -0.0105 0.0162  -0.0167 53  ILE   C CB  
1447 C  CG1 . ILE   B 47  ? 0.2758 0.2760 0.2801 -0.0087 0.0170  -0.0177 53  ILE   C CG1 
1448 C  CG2 . ILE   B 47  ? 0.2486 0.2455 0.2390 -0.0119 0.0134  -0.0123 53  ILE   C CG2 
1449 C  CD1 . ILE   B 47  ? 0.3031 0.3028 0.3118 -0.0060 0.0126  -0.0165 53  ILE   C CD1 
1450 N  N   . ALA   B 48  ? 0.2053 0.1952 0.1886 -0.0110 0.0099  -0.0149 54  ALA   C N   
1451 C  CA  . ALA   B 48  ? 0.1935 0.1811 0.1696 -0.0135 0.0087  -0.0139 54  ALA   C CA  
1452 C  C   . ALA   B 48  ? 0.1912 0.1799 0.1617 -0.0167 0.0095  -0.0119 54  ALA   C C   
1453 O  O   . ALA   B 48  ? 0.1947 0.1860 0.1675 -0.0167 0.0094  -0.0094 54  ALA   C O   
1454 C  CB  . ALA   B 48  ? 0.1988 0.1858 0.1753 -0.0130 0.0051  -0.0111 54  ALA   C CB  
1455 N  N   . ARG   B 49  ? 0.1825 0.1686 0.1453 -0.0194 0.0098  -0.0128 55  ARG   C N   
1456 C  CA  . ARG   B 49  ? 0.1907 0.1768 0.1464 -0.0229 0.0097  -0.0104 55  ARG   C CA  
1457 C  C   . ARG   B 49  ? 0.2017 0.1854 0.1523 -0.0249 0.0058  -0.0090 55  ARG   C C   
1458 O  O   . ARG   B 49  ? 0.2170 0.1973 0.1612 -0.0268 0.0062  -0.0116 55  ARG   C O   
1459 C  CB  . ARG   B 49  ? 0.2027 0.1877 0.1528 -0.0250 0.0143  -0.0134 55  ARG   C CB  
1460 C  CG  . ARG   B 49  ? 0.2160 0.2040 0.1732 -0.0230 0.0185  -0.0152 55  ARG   C CG  
1461 C  CD  . ARG   B 49  ? 0.2293 0.2205 0.1909 -0.0228 0.0176  -0.0113 55  ARG   C CD  
1462 N  NE  . ARG   B 49  ? 0.2483 0.2423 0.2170 -0.0215 0.0217  -0.0134 55  ARG   C NE  
1463 C  CZ  . ARG   B 49  ? 0.2445 0.2412 0.2199 -0.0204 0.0211  -0.0112 55  ARG   C CZ  
1464 N  NH1 . ARG   B 49  ? 0.2123 0.2092 0.1880 -0.0203 0.0171  -0.0072 55  ARG   C NH1 
1465 N  NH2 . ARG   B 49  ? 0.2654 0.2648 0.2480 -0.0195 0.0245  -0.0134 55  ARG   C NH2 
1466 N  N   . CYS   B 50  ? 0.1882 0.1738 0.1424 -0.0245 0.0021  -0.0052 56  CYS   C N   
1467 C  CA  . CYS   B 50  ? 0.2014 0.1858 0.1544 -0.0258 -0.0017 -0.0038 56  CYS   C CA  
1468 C  C   . CYS   B 50  ? 0.2092 0.1968 0.1671 -0.0256 -0.0049 0.0007  56  CYS   C C   
1469 O  O   . CYS   B 50  ? 0.1974 0.1876 0.1597 -0.0240 -0.0042 0.0024  56  CYS   C O   
1470 C  CB  . CYS   B 50  ? 0.2081 0.1909 0.1646 -0.0238 -0.0014 -0.0062 56  CYS   C CB  
1471 S  SG  . CYS   B 50  ? 0.2029 0.1887 0.1686 -0.0199 -0.0012 -0.0048 56  CYS   C SG  
1472 N  N   . ASP   B 51  ? 0.2153 0.2028 0.1738 -0.0270 -0.0083 0.0022  57  ASP   C N   
1473 C  CA  . ASP   B 51  ? 0.2207 0.2117 0.1856 -0.0266 -0.0111 0.0059  57  ASP   C CA  
1474 C  C   . ASP   B 51  ? 0.2268 0.2188 0.1974 -0.0252 -0.0111 0.0057  57  ASP   C C   
1475 O  O   . ASP   B 51  ? 0.2398 0.2345 0.2154 -0.0259 -0.0134 0.0082  57  ASP   C O   
1476 C  CB  . ASP   B 51  ? 0.2587 0.2498 0.2211 -0.0298 -0.0156 0.0088  57  ASP   C CB  
1477 C  CG  . ASP   B 51  ? 0.3369 0.3251 0.2948 -0.0327 -0.0181 0.0077  57  ASP   C CG  
1478 O  OD1 . ASP   B 51  ? 0.3459 0.3318 0.3026 -0.0322 -0.0162 0.0046  57  ASP   C OD1 
1479 O  OD2 . ASP   B 51  ? 0.3955 0.3836 0.3514 -0.0356 -0.0226 0.0100  57  ASP   C OD2 
1480 N  N   . CYS   B 52  ? 0.1949 0.1849 0.1653 -0.0234 -0.0086 0.0030  58  CYS   C N   
1481 C  CA  . CYS   B 52  ? 0.1902 0.1803 0.1647 -0.0224 -0.0084 0.0032  58  CYS   C CA  
1482 C  C   . CYS   B 52  ? 0.1826 0.1769 0.1636 -0.0208 -0.0081 0.0057  58  CYS   C C   
1483 O  O   . CYS   B 52  ? 0.1779 0.1742 0.1609 -0.0190 -0.0071 0.0062  58  CYS   C O   
1484 C  CB  . CYS   B 52  ? 0.1911 0.1782 0.1646 -0.0202 -0.0062 0.0004  58  CYS   C CB  
1485 S  SG  . CYS   B 52  ? 0.2337 0.2151 0.2014 -0.0217 -0.0064 -0.0032 58  CYS   C SG  
1486 N  N   . GLN   B 53  ? 0.1721 0.1676 0.1566 -0.0215 -0.0086 0.0070  59  GLN   C N   
1487 C  CA  . GLN   B 53  ? 0.1787 0.1778 0.1692 -0.0200 -0.0073 0.0088  59  GLN   C CA  
1488 C  C   . GLN   B 53  ? 0.1922 0.1894 0.1822 -0.0195 -0.0055 0.0083  59  GLN   C C   
1489 O  O   . GLN   B 53  ? 0.1958 0.1957 0.1900 -0.0192 -0.0040 0.0097  59  GLN   C O   
1490 C  CB  . GLN   B 53  ? 0.1893 0.1928 0.1859 -0.0217 -0.0093 0.0114  59  GLN   C CB  
1491 C  CG  . GLN   B 53  ? 0.1912 0.1967 0.1893 -0.0214 -0.0111 0.0126  59  GLN   C CG  
1492 C  CD  . GLN   B 53  ? 0.2267 0.2365 0.2323 -0.0227 -0.0137 0.0153  59  GLN   C CD  
1493 O  OE1 . GLN   B 53  ? 0.2487 0.2581 0.2530 -0.0254 -0.0176 0.0165  59  GLN   C OE1 
1494 N  NE2 . GLN   B 53  ? 0.1987 0.2125 0.2122 -0.0209 -0.0117 0.0160  59  GLN   C NE2 
1495 N  N   . THR   B 54  ? 0.2014 0.1938 0.1865 -0.0195 -0.0055 0.0065  60  THR   C N   
1496 C  CA  . THR   B 54  ? 0.2024 0.1918 0.1861 -0.0189 -0.0043 0.0065  60  THR   C CA  
1497 C  C   . THR   B 54  ? 0.1977 0.1833 0.1780 -0.0166 -0.0042 0.0040  60  THR   C C   
1498 O  O   . THR   B 54  ? 0.2080 0.1922 0.1865 -0.0165 -0.0048 0.0020  60  THR   C O   
1499 C  CB  . THR   B 54  ? 0.2617 0.2483 0.2445 -0.0217 -0.0055 0.0072  60  THR   C CB  
1500 O  OG1 . THR   B 54  ? 0.3065 0.2894 0.2859 -0.0226 -0.0073 0.0052  60  THR   C OG1 
1501 C  CG2 . THR   B 54  ? 0.2815 0.2725 0.2693 -0.0243 -0.0060 0.0095  60  THR   C CG2 
1502 N  N   . GLY   B 55  ? 0.1808 0.1646 0.1600 -0.0149 -0.0033 0.0042  61  GLY   C N   
1503 C  CA  . GLY   B 55  ? 0.1962 0.1767 0.1736 -0.0125 -0.0038 0.0021  61  GLY   C CA  
1504 C  C   . GLY   B 55  ? 0.1805 0.1584 0.1558 -0.0113 -0.0037 0.0029  61  GLY   C C   
1505 O  O   . GLY   B 55  ? 0.2048 0.1824 0.1787 -0.0127 -0.0029 0.0050  61  GLY   C O   
1506 N  N   . VAL   B 56  ? 0.1779 0.1534 0.1525 -0.0089 -0.0048 0.0013  62  VAL   C N   
1507 C  CA  . VAL   B 56  ? 0.1818 0.1536 0.1531 -0.0078 -0.0058 0.0021  62  VAL   C CA  
1508 C  C   . VAL   B 56  ? 0.1813 0.1549 0.1542 -0.0053 -0.0060 0.0006  62  VAL   C C   
1509 O  O   . VAL   B 56  ? 0.1882 0.1631 0.1647 -0.0040 -0.0065 -0.0015 62  VAL   C O   
1510 C  CB  . VAL   B 56  ? 0.1913 0.1570 0.1611 -0.0073 -0.0086 0.0016  62  VAL   C CB  
1511 C  CG1 . VAL   B 56  ? 0.2200 0.1811 0.1856 -0.0062 -0.0107 0.0028  62  VAL   C CG1 
1512 C  CG2 . VAL   B 56  ? 0.2037 0.1668 0.1722 -0.0100 -0.0087 0.0030  62  VAL   C CG2 
1513 N  N   . TYR   B 57  ? 0.1874 0.1607 0.1572 -0.0049 -0.0055 0.0014  63  TYR   C N   
1514 C  CA  . TYR   B 57  ? 0.1785 0.1526 0.1495 -0.0027 -0.0063 -0.0002 63  TYR   C CA  
1515 C  C   . TYR   B 57  ? 0.1871 0.1560 0.1528 -0.0018 -0.0088 0.0000  63  TYR   C C   
1516 O  O   . TYR   B 57  ? 0.2038 0.1689 0.1634 -0.0032 -0.0089 0.0020  63  TYR   C O   
1517 C  CB  . TYR   B 57  ? 0.1831 0.1619 0.1561 -0.0026 -0.0036 -0.0004 63  TYR   C CB  
1518 C  CG  . TYR   B 57  ? 0.1947 0.1727 0.1630 -0.0031 -0.0017 0.0006  63  TYR   C CG  
1519 C  CD1 . TYR   B 57  ? 0.2158 0.1946 0.1828 -0.0052 0.0006  0.0025  63  TYR   C CD1 
1520 C  CD2 . TYR   B 57  ? 0.1992 0.1757 0.1646 -0.0018 -0.0019 -0.0006 63  TYR   C CD2 
1521 C  CE1 . TYR   B 57  ? 0.2407 0.2194 0.2040 -0.0059 0.0035  0.0032  63  TYR   C CE1 
1522 C  CE2 . TYR   B 57  ? 0.2172 0.1929 0.1775 -0.0024 0.0007  -0.0002 63  TYR   C CE2 
1523 C  CZ  . TYR   B 57  ? 0.2388 0.2158 0.1981 -0.0045 0.0037  0.0017  63  TYR   C CZ  
1524 O  OH  . TYR   B 57  ? 0.2636 0.2402 0.2184 -0.0053 0.0073  0.0018  63  TYR   C OH  
1525 N  N   . TYR   B 58  ? 0.1936 0.1621 0.1614 0.0002  -0.0111 -0.0018 64  TYR   C N   
1526 C  CA  . TYR   B 58  ? 0.1970 0.1604 0.1596 0.0011  -0.0145 -0.0016 64  TYR   C CA  
1527 C  C   . TYR   B 58  ? 0.2088 0.1726 0.1669 0.0010  -0.0130 -0.0020 64  TYR   C C   
1528 O  O   . TYR   B 58  ? 0.2076 0.1753 0.1702 0.0019  -0.0118 -0.0037 64  TYR   C O   
1529 C  CB  . TYR   B 58  ? 0.2131 0.1757 0.1813 0.0032  -0.0185 -0.0035 64  TYR   C CB  
1530 C  CG  . TYR   B 58  ? 0.2332 0.1899 0.1957 0.0039  -0.0232 -0.0030 64  TYR   C CG  
1531 C  CD1 . TYR   B 58  ? 0.2478 0.1983 0.2040 0.0031  -0.0259 -0.0007 64  TYR   C CD1 
1532 C  CD2 . TYR   B 58  ? 0.2560 0.2129 0.2191 0.0050  -0.0254 -0.0046 64  TYR   C CD2 
1533 C  CE1 . TYR   B 58  ? 0.2735 0.2177 0.2229 0.0034  -0.0308 0.0003  64  TYR   C CE1 
1534 C  CE2 . TYR   B 58  ? 0.2727 0.2235 0.2291 0.0053  -0.0303 -0.0041 64  TYR   C CE2 
1535 C  CZ  . TYR   B 58  ? 0.2874 0.2318 0.2366 0.0045  -0.0331 -0.0015 64  TYR   C CZ  
1536 O  OH  . TYR   B 58  ? 0.3290 0.2667 0.2705 0.0046  -0.0387 -0.0006 64  TYR   C OH  
1537 N  N   . CYS   B 59  ? 0.2179 0.1770 0.1666 -0.0001 -0.0132 -0.0005 65  CYS   C N   
1538 C  CA  . CYS   B 59  ? 0.2214 0.1797 0.1639 -0.0003 -0.0113 -0.0013 65  CYS   C CA  
1539 C  C   . CYS   B 59  ? 0.2417 0.1935 0.1768 0.0003  -0.0162 -0.0017 65  CYS   C C   
1540 O  O   . CYS   B 59  ? 0.2582 0.2041 0.1846 -0.0009 -0.0182 0.0004  65  CYS   C O   
1541 C  CB  . CYS   B 59  ? 0.2257 0.1840 0.1626 -0.0026 -0.0067 0.0006  65  CYS   C CB  
1542 S  SG  . CYS   B 59  ? 0.2669 0.2238 0.1952 -0.0029 -0.0032 -0.0009 65  CYS   C SG  
1543 N  N   . SER   B 60  ? 0.2405 0.1932 0.1793 0.0021  -0.0186 -0.0043 66  SER   C N   
1544 C  CA  . SER   B 60  ? 0.2684 0.2151 0.2013 0.0026  -0.0244 -0.0048 66  SER   C CA  
1545 C  C   . SER   B 60  ? 0.2711 0.2120 0.1898 0.0011  -0.0238 -0.0044 66  SER   C C   
1546 O  O   . SER   B 60  ? 0.2928 0.2269 0.2031 0.0005  -0.0286 -0.0030 66  SER   C O   
1547 C  CB  . SER   B 60  ? 0.3453 0.2943 0.2857 0.0044  -0.0272 -0.0077 66  SER   C CB  
1548 O  OG  . SER   B 60  ? 0.4441 0.3964 0.3856 0.0045  -0.0230 -0.0097 66  SER   C OG  
1549 N  N   . SER   B 61  ? 0.2608 0.2042 0.1766 0.0003  -0.0176 -0.0053 67  SER   C N   
1550 C  CA  . SER   B 61  ? 0.2766 0.2147 0.1782 -0.0013 -0.0156 -0.0055 67  SER   C CA  
1551 C  C   . SER   B 61  ? 0.2875 0.2213 0.1796 -0.0039 -0.0144 -0.0017 67  SER   C C   
1552 O  O   . SER   B 61  ? 0.2980 0.2264 0.1765 -0.0059 -0.0129 -0.0013 67  SER   C O   
1553 C  CB  . SER   B 61  ? 0.2763 0.2187 0.1793 -0.0011 -0.0090 -0.0081 67  SER   C CB  
1554 O  OG  . SER   B 61  ? 0.2804 0.2290 0.1906 -0.0017 -0.0036 -0.0067 67  SER   C OG  
1555 N  N   . ARG   B 62  ? 0.2649 0.2005 0.1634 -0.0043 -0.0151 0.0009  68  ARG   C N   
1556 C  CA  . ARG   B 62  ? 0.2674 0.1983 0.1584 -0.0068 -0.0151 0.0048  68  ARG   C CA  
1557 C  C   . ARG   B 62  ? 0.2882 0.2146 0.1816 -0.0060 -0.0224 0.0069  68  ARG   C C   
1558 O  O   . ARG   B 62  ? 0.3115 0.2330 0.1994 -0.0080 -0.0235 0.0104  68  ARG   C O   
1559 C  CB  . ARG   B 62  ? 0.2732 0.2099 0.1700 -0.0083 -0.0086 0.0061  68  ARG   C CB  
1560 C  CG  . ARG   B 62  ? 0.2865 0.2273 0.1814 -0.0092 -0.0012 0.0044  68  ARG   C CG  
1561 C  CD  . ARG   B 62  ? 0.3057 0.2402 0.1851 -0.0121 0.0013  0.0060  68  ARG   C CD  
1562 N  NE  . ARG   B 62  ? 0.3294 0.2681 0.2078 -0.0128 0.0092  0.0039  68  ARG   C NE  
1563 C  CZ  . ARG   B 62  ? 0.3828 0.3210 0.2572 -0.0115 0.0109  0.0001  68  ARG   C CZ  
1564 N  NH1 . ARG   B 62  ? 0.3782 0.3117 0.2482 -0.0099 0.0048  -0.0016 68  ARG   C NH1 
1565 N  NH2 . ARG   B 62  ? 0.3905 0.3328 0.2653 -0.0120 0.0185  -0.0020 68  ARG   C NH2 
1566 N  N   . ARG   B 63  ? 0.2982 0.2265 0.2008 -0.0032 -0.0272 0.0047  69  ARG   C N   
1567 C  CA  . ARG   B 63  ? 0.3119 0.2374 0.2204 -0.0018 -0.0336 0.0059  69  ARG   C CA  
1568 C  C   . ARG   B 63  ? 0.3193 0.2460 0.2324 -0.0028 -0.0315 0.0080  69  ARG   C C   
1569 O  O   . ARG   B 63  ? 0.3479 0.2685 0.2583 -0.0033 -0.0356 0.0107  69  ARG   C O   
1570 C  CB  . ARG   B 63  ? 0.3435 0.2594 0.2414 -0.0023 -0.0408 0.0080  69  ARG   C CB  
1571 C  CG  . ARG   B 63  ? 0.3998 0.3144 0.2969 -0.0008 -0.0456 0.0055  69  ARG   C CG  
1572 C  CD  . ARG   B 63  ? 0.4837 0.3890 0.3730 -0.0010 -0.0543 0.0080  69  ARG   C CD  
1573 N  NE  . ARG   B 63  ? 0.5667 0.4682 0.4475 -0.0012 -0.0581 0.0063  69  ARG   C NE  
1574 C  CZ  . ARG   B 63  ? 0.6322 0.5253 0.4953 -0.0036 -0.0600 0.0081  69  ARG   C CZ  
1575 N  NH1 . ARG   B 63  ? 0.6328 0.5203 0.4847 -0.0063 -0.0583 0.0121  69  ARG   C NH1 
1576 N  NH2 . ARG   B 63  ? 0.6390 0.5286 0.4946 -0.0037 -0.0637 0.0059  69  ARG   C NH2 
1577 N  N   . LYS   B 64  ? 0.3001 0.2339 0.2194 -0.0032 -0.0252 0.0070  70  LYS   C N   
1578 C  CA  . LYS   B 64  ? 0.2940 0.2286 0.2163 -0.0047 -0.0230 0.0090  70  LYS   C CA  
1579 C  C   . LYS   B 64  ? 0.2602 0.2029 0.1932 -0.0040 -0.0190 0.0069  70  LYS   C C   
1580 O  O   . LYS   B 64  ? 0.2525 0.2005 0.1885 -0.0033 -0.0162 0.0048  70  LYS   C O   
1581 C  CB  . LYS   B 64  ? 0.3617 0.2944 0.2744 -0.0082 -0.0184 0.0117  70  LYS   C CB  
1582 C  CG  . LYS   B 64  ? 0.4911 0.4147 0.3936 -0.0104 -0.0216 0.0156  70  LYS   C CG  
1583 C  CD  . LYS   B 64  ? 0.5829 0.5058 0.4765 -0.0141 -0.0159 0.0180  70  LYS   C CD  
1584 C  CE  . LYS   B 64  ? 0.6257 0.5543 0.5266 -0.0158 -0.0107 0.0187  70  LYS   C CE  
1585 N  NZ  . LYS   B 64  ? 0.6716 0.5983 0.5639 -0.0199 -0.0059 0.0217  70  LYS   C NZ  
1586 N  N   . HIS   B 65  ? 0.2480 0.1911 0.1857 -0.0047 -0.0187 0.0078  71  HIS   C N   
1587 C  CA  . HIS   B 65  ? 0.2334 0.1834 0.1793 -0.0048 -0.0151 0.0063  71  HIS   C CA  
1588 C  C   . HIS   B 65  ? 0.2626 0.2142 0.2059 -0.0078 -0.0108 0.0084  71  HIS   C C   
1589 O  O   . HIS   B 65  ? 0.2926 0.2392 0.2300 -0.0100 -0.0112 0.0112  71  HIS   C O   
1590 C  CB  . HIS   B 65  ? 0.2329 0.1822 0.1856 -0.0038 -0.0175 0.0053  71  HIS   C CB  
1591 C  CG  . HIS   B 65  ? 0.2452 0.1940 0.2031 -0.0009 -0.0212 0.0029  71  HIS   C CG  
1592 N  ND1 . HIS   B 65  ? 0.2838 0.2382 0.2497 0.0007  -0.0199 0.0000  71  HIS   C ND1 
1593 C  CD2 . HIS   B 65  ? 0.2655 0.2085 0.2220 0.0006  -0.0263 0.0034  71  HIS   C CD2 
1594 C  CE1 . HIS   B 65  ? 0.2806 0.2332 0.2507 0.0030  -0.0237 -0.0015 71  HIS   C CE1 
1595 N  NE2 . HIS   B 65  ? 0.3065 0.2524 0.2715 0.0032  -0.0280 0.0005  71  HIS   C NE2 
1596 N  N   . TYR   B 66  ? 0.2163 0.1748 0.1649 -0.0081 -0.0070 0.0074  72  TYR   C N   
1597 C  CA  . TYR   B 66  ? 0.2192 0.1805 0.1680 -0.0108 -0.0031 0.0092  72  TYR   C CA  
1598 C  C   . TYR   B 66  ? 0.2079 0.1742 0.1647 -0.0113 -0.0024 0.0084  72  TYR   C C   
1599 O  O   . TYR   B 66  ? 0.2079 0.1782 0.1697 -0.0096 -0.0025 0.0063  72  TYR   C O   
1600 C  CB  . TYR   B 66  ? 0.2338 0.1993 0.1817 -0.0109 0.0011  0.0088  72  TYR   C CB  
1601 C  CG  . TYR   B 66  ? 0.2655 0.2262 0.2035 -0.0114 0.0016  0.0095  72  TYR   C CG  
1602 C  CD1 . TYR   B 66  ? 0.2852 0.2423 0.2164 -0.0143 0.0035  0.0123  72  TYR   C CD1 
1603 C  CD2 . TYR   B 66  ? 0.2815 0.2411 0.2166 -0.0092 0.0005  0.0074  72  TYR   C CD2 
1604 C  CE1 . TYR   B 66  ? 0.3140 0.2662 0.2345 -0.0152 0.0044  0.0131  72  TYR   C CE1 
1605 C  CE2 . TYR   B 66  ? 0.3141 0.2687 0.2386 -0.0099 0.0008  0.0078  72  TYR   C CE2 
1606 C  CZ  . TYR   B 66  ? 0.3434 0.2942 0.2601 -0.0129 0.0028  0.0107  72  TYR   C CZ  
1607 O  OH  . TYR   B 66  ? 0.3788 0.3240 0.2832 -0.0140 0.0034  0.0113  72  TYR   C OH  
1608 N  N   . PRO   B 67  ? 0.2080 0.1738 0.1654 -0.0140 -0.0018 0.0102  73  PRO   C N   
1609 C  CA  . PRO   B 67  ? 0.2160 0.1862 0.1799 -0.0150 -0.0013 0.0096  73  PRO   C CA  
1610 C  C   . PRO   B 67  ? 0.2314 0.2085 0.1994 -0.0156 0.0021  0.0101  73  PRO   C C   
1611 O  O   . PRO   B 67  ? 0.2405 0.2182 0.2065 -0.0170 0.0050  0.0116  73  PRO   C O   
1612 C  CB  . PRO   B 67  ? 0.2216 0.1878 0.1841 -0.0179 -0.0023 0.0115  73  PRO   C CB  
1613 C  CG  . PRO   B 67  ? 0.2358 0.1983 0.1922 -0.0193 -0.0011 0.0141  73  PRO   C CG  
1614 C  CD  . PRO   B 67  ? 0.2233 0.1839 0.1751 -0.0166 -0.0017 0.0131  73  PRO   C CD  
1615 N  N   . VAL   B 68  ? 0.2066 0.1885 0.1801 -0.0148 0.0020  0.0088  74  VAL   C N   
1616 C  CA  . VAL   B 68  ? 0.2076 0.1959 0.1865 -0.0150 0.0045  0.0092  74  VAL   C CA  
1617 C  C   . VAL   B 68  ? 0.2013 0.1933 0.1858 -0.0161 0.0030  0.0093  74  VAL   C C   
1618 O  O   . VAL   B 68  ? 0.2119 0.2018 0.1953 -0.0158 0.0006  0.0081  74  VAL   C O   
1619 C  CB  . VAL   B 68  ? 0.2397 0.2300 0.2194 -0.0122 0.0056  0.0076  74  VAL   C CB  
1620 C  CG1 . VAL   B 68  ? 0.2748 0.2620 0.2485 -0.0115 0.0075  0.0075  74  VAL   C CG1 
1621 C  CG2 . VAL   B 68  ? 0.2427 0.2319 0.2226 -0.0102 0.0031  0.0058  74  VAL   C CG2 
1622 N  N   . SER   B 69  ? 0.1979 0.1952 0.1886 -0.0173 0.0044  0.0106  75  SER   C N   
1623 C  CA  . SER   B 69  ? 0.1861 0.1874 0.1824 -0.0179 0.0025  0.0109  75  SER   C CA  
1624 C  C   . SER   B 69  ? 0.1788 0.1831 0.1781 -0.0151 0.0033  0.0100  75  SER   C C   
1625 O  O   . SER   B 69  ? 0.1877 0.1929 0.1875 -0.0134 0.0061  0.0095  75  SER   C O   
1626 C  CB  . SER   B 69  ? 0.2227 0.2285 0.2257 -0.0204 0.0029  0.0130  75  SER   C CB  
1627 O  OG  . SER   B 69  ? 0.2951 0.2979 0.2959 -0.0233 0.0020  0.0139  75  SER   C OG  
1628 N  N   . PHE   B 70  ? 0.1697 0.1749 0.1702 -0.0147 0.0009  0.0098  76  PHE   C N   
1629 C  CA  . PHE   B 70  ? 0.1678 0.1750 0.1713 -0.0123 0.0012  0.0093  76  PHE   C CA  
1630 C  C   . PHE   B 70  ? 0.1619 0.1721 0.1701 -0.0133 -0.0014 0.0108  76  PHE   C C   
1631 O  O   . PHE   B 70  ? 0.1792 0.1888 0.1861 -0.0157 -0.0039 0.0117  76  PHE   C O   
1632 C  CB  . PHE   B 70  ? 0.1623 0.1658 0.1606 -0.0105 0.0011  0.0073  76  PHE   C CB  
1633 C  CG  . PHE   B 70  ? 0.1588 0.1593 0.1527 -0.0115 -0.0008 0.0065  76  PHE   C CG  
1634 C  CD1 . PHE   B 70  ? 0.1649 0.1616 0.1543 -0.0121 -0.0009 0.0056  76  PHE   C CD1 
1635 C  CD2 . PHE   B 70  ? 0.1750 0.1760 0.1690 -0.0119 -0.0022 0.0066  76  PHE   C CD2 
1636 C  CE1 . PHE   B 70  ? 0.1782 0.1721 0.1644 -0.0127 -0.0022 0.0043  76  PHE   C CE1 
1637 C  CE2 . PHE   B 70  ? 0.1774 0.1757 0.1670 -0.0128 -0.0030 0.0053  76  PHE   C CE2 
1638 C  CZ  . PHE   B 70  ? 0.1783 0.1732 0.1644 -0.0131 -0.0028 0.0039  76  PHE   C CZ  
1639 N  N   . SER   B 71  ? 0.1570 0.1699 0.1706 -0.0115 -0.0012 0.0112  77  SER   C N   
1640 C  CA  . SER   B 71  ? 0.1712 0.1866 0.1900 -0.0122 -0.0043 0.0132  77  SER   C CA  
1641 C  C   . SER   B 71  ? 0.1821 0.1946 0.1955 -0.0130 -0.0069 0.0135  77  SER   C C   
1642 O  O   . SER   B 71  ? 0.1884 0.1975 0.1952 -0.0129 -0.0059 0.0118  77  SER   C O   
1643 C  CB  . SER   B 71  ? 0.1856 0.2044 0.2129 -0.0099 -0.0032 0.0135  77  SER   C CB  
1644 O  OG  . SER   B 71  ? 0.2028 0.2195 0.2283 -0.0075 -0.0022 0.0120  77  SER   C OG  
1645 N  N   . LYS   B 72  ? 0.1745 0.1884 0.1910 -0.0141 -0.0103 0.0159  78  LYS   C N   
1646 C  CA  . LYS   B 72  ? 0.1866 0.1975 0.1971 -0.0152 -0.0122 0.0165  78  LYS   C CA  
1647 C  C   . LYS   B 72  ? 0.1854 0.1959 0.1982 -0.0128 -0.0111 0.0163  78  LYS   C C   
1648 O  O   . LYS   B 72  ? 0.2192 0.2320 0.2394 -0.0106 -0.0102 0.0163  78  LYS   C O   
1649 C  CB  . LYS   B 72  ? 0.2251 0.2366 0.2364 -0.0178 -0.0169 0.0195  78  LYS   C CB  
1650 C  CG  . LYS   B 72  ? 0.2703 0.2817 0.2791 -0.0205 -0.0185 0.0195  78  LYS   C CG  
1651 C  CD  . LYS   B 72  ? 0.3866 0.3975 0.3940 -0.0235 -0.0239 0.0223  78  LYS   C CD  
1652 C  CE  . LYS   B 72  ? 0.4873 0.4974 0.4916 -0.0265 -0.0259 0.0219  78  LYS   C CE  
1653 N  NZ  . LYS   B 72  ? 0.5525 0.5605 0.5521 -0.0298 -0.0316 0.0242  78  LYS   C NZ  
1654 N  N   . PRO   B 73  ? 0.1807 0.1883 0.1878 -0.0134 -0.0108 0.0158  79  PRO   C N   
1655 C  CA  . PRO   B 73  ? 0.1817 0.1887 0.1914 -0.0115 -0.0100 0.0157  79  PRO   C CA  
1656 C  C   . PRO   B 73  ? 0.2029 0.2112 0.2195 -0.0110 -0.0128 0.0186  79  PRO   C C   
1657 O  O   . PRO   B 73  ? 0.2114 0.2194 0.2271 -0.0132 -0.0165 0.0216  79  PRO   C O   
1658 C  CB  . PRO   B 73  ? 0.2020 0.2061 0.2046 -0.0132 -0.0094 0.0153  79  PRO   C CB  
1659 C  CG  . PRO   B 73  ? 0.2247 0.2278 0.2208 -0.0150 -0.0087 0.0138  79  PRO   C CG  
1660 C  CD  . PRO   B 73  ? 0.1927 0.1976 0.1911 -0.0158 -0.0108 0.0150  79  PRO   C CD  
1661 N  N   . SER   B 74  ? 0.1955 0.2047 0.2188 -0.0081 -0.0115 0.0176  80  SER   C N   
1662 C  CA  . SER   B 74  ? 0.2231 0.2335 0.2547 -0.0070 -0.0142 0.0200  80  SER   C CA  
1663 C  C   . SER   B 74  ? 0.2030 0.2124 0.2396 -0.0041 -0.0127 0.0185  80  SER   C C   
1664 O  O   . SER   B 74  ? 0.1908 0.1987 0.2241 -0.0031 -0.0098 0.0156  80  SER   C O   
1665 C  CB  . SER   B 74  ? 0.2959 0.3103 0.3345 -0.0066 -0.0151 0.0207  80  SER   C CB  
1666 O  OG  . SER   B 74  ? 0.3492 0.3654 0.3905 -0.0044 -0.0108 0.0175  80  SER   C OG  
1667 N  N   . LEU   B 75  ? 0.2040 0.2138 0.2490 -0.0028 -0.0153 0.0205  81  LEU   C N   
1668 C  CA  . LEU   B 75  ? 0.2083 0.2165 0.2591 0.0000  -0.0145 0.0191  81  LEU   C CA  
1669 C  C   . LEU   B 75  ? 0.2043 0.2158 0.2623 0.0031  -0.0113 0.0159  81  LEU   C C   
1670 O  O   . LEU   B 75  ? 0.2328 0.2479 0.2985 0.0036  -0.0123 0.0171  81  LEU   C O   
1671 C  CB  . LEU   B 75  ? 0.2357 0.2426 0.2927 -0.0002 -0.0193 0.0232  81  LEU   C CB  
1672 C  CG  . LEU   B 75  ? 0.3017 0.3039 0.3563 -0.0014 -0.0215 0.0254  81  LEU   C CG  
1673 C  CD1 . LEU   B 75  ? 0.3246 0.3256 0.3893 0.0000  -0.0258 0.0286  81  LEU   C CD1 
1674 C  CD2 . LEU   B 75  ? 0.3093 0.3090 0.3618 -0.0002 -0.0182 0.0220  81  LEU   C CD2 
1675 N  N   . ILE   B 76  ? 0.1932 0.2033 0.2485 0.0048  -0.0075 0.0119  82  ILE   C N   
1676 C  CA  . ILE   B 76  ? 0.2046 0.2170 0.2637 0.0072  -0.0035 0.0084  82  ILE   C CA  
1677 C  C   . ILE   B 76  ? 0.2094 0.2189 0.2711 0.0100  -0.0018 0.0051  82  ILE   C C   
1678 O  O   . ILE   B 76  ? 0.2045 0.2101 0.2606 0.0097  -0.0023 0.0041  82  ILE   C O   
1679 C  CB  . ILE   B 76  ? 0.2443 0.2572 0.2946 0.0059  -0.0005 0.0067  82  ILE   C CB  
1680 C  CG1 . ILE   B 76  ? 0.2960 0.3117 0.3450 0.0031  -0.0023 0.0097  82  ILE   C CG1 
1681 C  CG2 . ILE   B 76  ? 0.2664 0.2804 0.3176 0.0079  0.0042  0.0029  82  ILE   C CG2 
1682 C  CD1 . ILE   B 76  ? 0.3556 0.3707 0.3961 0.0015  -0.0005 0.0087  82  ILE   C CD1 
1683 N  N   . PHE   B 77  ? 0.2038 0.2151 0.2742 0.0128  0.0002  0.0030  83  PHE   C N   
1684 C  CA  . PHE   B 77  ? 0.2212 0.2292 0.2938 0.0156  0.0020  -0.0008 83  PHE   C CA  
1685 C  C   . PHE   B 77  ? 0.2316 0.2374 0.2942 0.0157  0.0058  -0.0050 83  PHE   C C   
1686 O  O   . PHE   B 77  ? 0.2466 0.2548 0.3050 0.0150  0.0091  -0.0060 83  PHE   C O   
1687 C  CB  . PHE   B 77  ? 0.2358 0.2466 0.3210 0.0187  0.0038  -0.0025 83  PHE   C CB  
1688 C  CG  . PHE   B 77  ? 0.2668 0.2736 0.3543 0.0218  0.0060  -0.0072 83  PHE   C CG  
1689 C  CD1 . PHE   B 77  ? 0.2924 0.2993 0.3769 0.0233  0.0117  -0.0124 83  PHE   C CD1 
1690 C  CD2 . PHE   B 77  ? 0.3019 0.3043 0.3934 0.0227  0.0023  -0.0065 83  PHE   C CD2 
1691 C  CE1 . PHE   B 77  ? 0.3163 0.3189 0.4018 0.0260  0.0136  -0.0173 83  PHE   C CE1 
1692 C  CE2 . PHE   B 77  ? 0.3131 0.3111 0.4066 0.0254  0.0040  -0.0112 83  PHE   C CE2 
1693 C  CZ  . PHE   B 77  ? 0.3148 0.3129 0.4051 0.0271  0.0096  -0.0168 83  PHE   C CZ  
1694 N  N   . VAL   B 78  ? 0.2290 0.2298 0.2875 0.0161  0.0049  -0.0071 84  VAL   C N   
1695 C  CA  . VAL   B 78  ? 0.2353 0.2330 0.2842 0.0162  0.0073  -0.0110 84  VAL   C CA  
1696 C  C   . VAL   B 78  ? 0.2413 0.2349 0.2929 0.0188  0.0082  -0.0154 84  VAL   C C   
1697 O  O   . VAL   B 78  ? 0.2349 0.2257 0.2913 0.0194  0.0052  -0.0148 84  VAL   C O   
1698 C  CB  . VAL   B 78  ? 0.2372 0.2325 0.2783 0.0139  0.0045  -0.0096 84  VAL   C CB  
1699 C  CG1 . VAL   B 78  ? 0.2517 0.2436 0.2834 0.0139  0.0058  -0.0133 84  VAL   C CG1 
1700 C  CG2 . VAL   B 78  ? 0.2389 0.2377 0.2778 0.0114  0.0035  -0.0057 84  VAL   C CG2 
1701 N  N   . GLU   B 79  ? 0.2569 0.2495 0.3041 0.0202  0.0125  -0.0199 85  GLU   C N   
1702 C  CA  . GLU   B 79  ? 0.2706 0.2589 0.3189 0.0226  0.0140  -0.0249 85  GLU   C CA  
1703 C  C   . GLU   B 79  ? 0.2543 0.2365 0.2971 0.0220  0.0104  -0.0263 85  GLU   C C   
1704 O  O   . GLU   B 79  ? 0.2426 0.2243 0.2783 0.0197  0.0081  -0.0245 85  GLU   C O   
1705 C  CB  . GLU   B 79  ? 0.3226 0.3106 0.3638 0.0233  0.0196  -0.0293 85  GLU   C CB  
1706 C  CG  . GLU   B 79  ? 0.4238 0.4181 0.4698 0.0234  0.0240  -0.0282 85  GLU   C CG  
1707 C  CD  . GLU   B 79  ? 0.5513 0.5479 0.6096 0.0266  0.0274  -0.0308 85  GLU   C CD  
1708 O  OE1 . GLU   B 79  ? 0.5875 0.5898 0.6512 0.0267  0.0314  -0.0303 85  GLU   C OE1 
1709 O  OE2 . GLU   B 79  ? 0.5632 0.5559 0.6265 0.0289  0.0261  -0.0336 85  GLU   C OE2 
1710 N  N   . ALA   B 80  ? 0.2520 0.2296 0.2985 0.0240  0.0098  -0.0299 86  ALA   C N   
1711 C  CA  . ALA   B 80  ? 0.2501 0.2220 0.2925 0.0231  0.0062  -0.0315 86  ALA   C CA  
1712 C  C   . ALA   B 80  ? 0.2516 0.2210 0.2808 0.0219  0.0067  -0.0342 86  ALA   C C   
1713 O  O   . ALA   B 80  ? 0.2669 0.2366 0.2893 0.0224  0.0108  -0.0368 86  ALA   C O   
1714 C  CB  . ALA   B 80  ? 0.2445 0.2112 0.2925 0.0257  0.0061  -0.0359 86  ALA   C CB  
1715 N  N   . SER   B 81  ? 0.2313 0.1981 0.2572 0.0201  0.0025  -0.0333 87  SER   C N   
1716 C  CA  . SER   B 81  ? 0.2321 0.1955 0.2467 0.0189  0.0012  -0.0357 87  SER   C CA  
1717 C  C   . SER   B 81  ? 0.2511 0.2094 0.2673 0.0184  -0.0034 -0.0376 87  SER   C C   
1718 O  O   . SER   B 81  ? 0.2685 0.2259 0.2940 0.0189  -0.0049 -0.0369 87  SER   C O   
1719 C  CB  . SER   B 81  ? 0.2418 0.2088 0.2521 0.0167  0.0001  -0.0317 87  SER   C CB  
1720 O  OG  . SER   B 81  ? 0.2509 0.2200 0.2680 0.0153  -0.0031 -0.0279 87  SER   C OG  
1721 N  N   . GLU   B 82  ? 0.2592 0.2138 0.2667 0.0172  -0.0060 -0.0398 88  GLU   C N   
1722 C  CA  . GLU   B 82  ? 0.2744 0.2247 0.2843 0.0163  -0.0110 -0.0414 88  GLU   C CA  
1723 C  C   . GLU   B 82  ? 0.2746 0.2289 0.2936 0.0144  -0.0136 -0.0363 88  GLU   C C   
1724 O  O   . GLU   B 82  ? 0.2722 0.2241 0.2973 0.0135  -0.0168 -0.0365 88  GLU   C O   
1725 C  CB  . GLU   B 82  ? 0.3482 0.2949 0.3476 0.0151  -0.0143 -0.0437 88  GLU   C CB  
1726 C  CG  . GLU   B 82  ? 0.4941 0.4375 0.4806 0.0159  -0.0115 -0.0473 88  GLU   C CG  
1727 C  CD  . GLU   B 82  ? 0.5904 0.5379 0.5710 0.0151  -0.0096 -0.0439 88  GLU   C CD  
1728 O  OE1 . GLU   B 82  ? 0.6467 0.5926 0.6206 0.0137  -0.0133 -0.0432 88  GLU   C OE1 
1729 O  OE2 . GLU   B 82  ? 0.5477 0.4998 0.5313 0.0158  -0.0050 -0.0417 88  GLU   C OE2 
1730 N  N   . TYR   B 83  ? 0.2626 0.2226 0.2821 0.0136  -0.0120 -0.0320 89  TYR   C N   
1731 C  CA  . TYR   B 83  ? 0.2602 0.2240 0.2859 0.0115  -0.0137 -0.0276 89  TYR   C CA  
1732 C  C   . TYR   B 83  ? 0.2550 0.2211 0.2891 0.0114  -0.0125 -0.0239 89  TYR   C C   
1733 O  O   . TYR   B 83  ? 0.2740 0.2415 0.3135 0.0094  -0.0141 -0.0208 89  TYR   C O   
1734 C  CB  . TYR   B 83  ? 0.2580 0.2259 0.2788 0.0106  -0.0128 -0.0252 89  TYR   C CB  
1735 C  CG  . TYR   B 83  ? 0.2780 0.2432 0.2904 0.0106  -0.0147 -0.0279 89  TYR   C CG  
1736 C  CD1 . TYR   B 83  ? 0.2958 0.2597 0.3096 0.0094  -0.0189 -0.0286 89  TYR   C CD1 
1737 C  CD2 . TYR   B 83  ? 0.2912 0.2552 0.2945 0.0116  -0.0126 -0.0295 89  TYR   C CD2 
1738 C  CE1 . TYR   B 83  ? 0.3263 0.2874 0.3326 0.0093  -0.0218 -0.0308 89  TYR   C CE1 
1739 C  CE2 . TYR   B 83  ? 0.3288 0.2893 0.3230 0.0113  -0.0150 -0.0315 89  TYR   C CE2 
1740 C  CZ  . TYR   B 83  ? 0.3526 0.3116 0.3484 0.0102  -0.0200 -0.0320 89  TYR   C CZ  
1741 O  OH  . TYR   B 83  ? 0.4158 0.3712 0.4030 0.0099  -0.0233 -0.0336 89  TYR   C OH  
1742 N  N   . TYR   B 84  ? 0.2309 0.1977 0.2662 0.0133  -0.0097 -0.0241 90  TYR   C N   
1743 C  CA  . TYR   B 84  ? 0.2255 0.1946 0.2685 0.0132  -0.0093 -0.0201 90  TYR   C CA  
1744 C  C   . TYR   B 84  ? 0.2486 0.2160 0.2960 0.0160  -0.0077 -0.0222 90  TYR   C C   
1745 O  O   . TYR   B 84  ? 0.2535 0.2204 0.2967 0.0179  -0.0048 -0.0260 90  TYR   C O   
1746 C  CB  . TYR   B 84  ? 0.2184 0.1933 0.2597 0.0123  -0.0074 -0.0161 90  TYR   C CB  
1747 C  CG  . TYR   B 84  ? 0.2119 0.1893 0.2501 0.0097  -0.0084 -0.0136 90  TYR   C CG  
1748 C  CD1 . TYR   B 84  ? 0.2129 0.1920 0.2441 0.0095  -0.0074 -0.0145 90  TYR   C CD1 
1749 C  CD2 . TYR   B 84  ? 0.1988 0.1768 0.2412 0.0074  -0.0101 -0.0102 90  TYR   C CD2 
1750 C  CE1 . TYR   B 84  ? 0.2166 0.1979 0.2461 0.0075  -0.0081 -0.0127 90  TYR   C CE1 
1751 C  CE2 . TYR   B 84  ? 0.1999 0.1803 0.2401 0.0051  -0.0101 -0.0085 90  TYR   C CE2 
1752 C  CZ  . TYR   B 84  ? 0.2073 0.1896 0.2415 0.0054  -0.0092 -0.0099 90  TYR   C CZ  
1753 O  OH  . TYR   B 84  ? 0.2070 0.1916 0.2403 0.0035  -0.0092 -0.0086 90  TYR   C OH  
1754 N  N   . PRO   B 85  ? 0.2491 0.2157 0.3052 0.0162  -0.0091 -0.0196 91  PRO   C N   
1755 C  CA  . PRO   B 85  ? 0.2351 0.2011 0.2974 0.0192  -0.0075 -0.0211 91  PRO   C CA  
1756 C  C   . PRO   B 85  ? 0.2327 0.2048 0.2948 0.0198  -0.0046 -0.0190 91  PRO   C C   
1757 O  O   . PRO   B 85  ? 0.2255 0.2015 0.2839 0.0176  -0.0049 -0.0153 91  PRO   C O   
1758 C  CB  . PRO   B 85  ? 0.2509 0.2148 0.3226 0.0186  -0.0109 -0.0171 91  PRO   C CB  
1759 C  CG  . PRO   B 85  ? 0.2640 0.2303 0.3329 0.0149  -0.0127 -0.0119 91  PRO   C CG  
1760 C  CD  . PRO   B 85  ? 0.2387 0.2054 0.2994 0.0136  -0.0120 -0.0145 91  PRO   C CD  
1761 N  N   . ALA   B 86  ? 0.2335 0.2066 0.3011 0.0227  -0.0021 -0.0211 92  ALA   C N   
1762 C  CA  . ALA   B 86  ? 0.2489 0.2280 0.3196 0.0232  0.0002  -0.0188 92  ALA   C CA  
1763 C  C   . ALA   B 86  ? 0.2418 0.2230 0.3176 0.0212  -0.0038 -0.0121 92  ALA   C C   
1764 O  O   . ALA   B 86  ? 0.2387 0.2163 0.3203 0.0211  -0.0073 -0.0101 92  ALA   C O   
1765 C  CB  . ALA   B 86  ? 0.2529 0.2324 0.3323 0.0269  0.0031  -0.0222 92  ALA   C CB  
1766 N  N   . ARG   B 87  ? 0.2341 0.2200 0.3061 0.0191  -0.0036 -0.0086 93  ARG   C N   
1767 C  CA  . ARG   B 87  ? 0.2285 0.2155 0.3025 0.0167  -0.0074 -0.0025 93  ARG   C CA  
1768 C  C   . ARG   B 87  ? 0.2341 0.2264 0.3050 0.0150  -0.0066 0.0002  93  ARG   C C   
1769 O  O   . ARG   B 87  ? 0.2421 0.2371 0.3089 0.0155  -0.0031 -0.0024 93  ARG   C O   
1770 C  CB  . ARG   B 87  ? 0.2345 0.2182 0.3023 0.0138  -0.0093 -0.0013 93  ARG   C CB  
1771 C  CG  . ARG   B 87  ? 0.2115 0.1974 0.2693 0.0120  -0.0073 -0.0024 93  ARG   C CG  
1772 C  CD  . ARG   B 87  ? 0.2159 0.1987 0.2694 0.0105  -0.0082 -0.0038 93  ARG   C CD  
1773 N  NE  . ARG   B 87  ? 0.1989 0.1839 0.2459 0.0079  -0.0079 -0.0023 93  ARG   C NE  
1774 C  CZ  . ARG   B 87  ? 0.2337 0.2207 0.2746 0.0081  -0.0060 -0.0042 93  ARG   C CZ  
1775 N  NH1 . ARG   B 87  ? 0.2179 0.2064 0.2542 0.0059  -0.0060 -0.0030 93  ARG   C NH1 
1776 N  NH2 . ARG   B 87  ? 0.2236 0.2109 0.2629 0.0102  -0.0038 -0.0072 93  ARG   C NH2 
1777 N  N   . TYR   B 88  ? 0.2301 0.2234 0.3018 0.0127  -0.0099 0.0055  94  TYR   C N   
1778 C  CA  . TYR   B 88  ? 0.2370 0.2344 0.3042 0.0106  -0.0098 0.0079  94  TYR   C CA  
1779 C  C   . TYR   B 88  ? 0.2138 0.2100 0.2710 0.0076  -0.0096 0.0085  94  TYR   C C   
1780 O  O   . TYR   B 88  ? 0.2210 0.2141 0.2769 0.0059  -0.0117 0.0105  94  TYR   C O   
1781 C  CB  . TYR   B 88  ? 0.2586 0.2573 0.3309 0.0093  -0.0139 0.0132  94  TYR   C CB  
1782 C  CG  . TYR   B 88  ? 0.2912 0.2923 0.3752 0.0123  -0.0142 0.0128  94  TYR   C CG  
1783 C  CD1 . TYR   B 88  ? 0.3193 0.3258 0.4060 0.0128  -0.0124 0.0123  94  TYR   C CD1 
1784 C  CD2 . TYR   B 88  ? 0.3289 0.3271 0.4221 0.0149  -0.0159 0.0124  94  TYR   C CD2 
1785 C  CE1 . TYR   B 88  ? 0.3441 0.3537 0.4434 0.0156  -0.0122 0.0116  94  TYR   C CE1 
1786 C  CE2 . TYR   B 88  ? 0.3517 0.3525 0.4572 0.0181  -0.0157 0.0114  94  TYR   C CE2 
1787 C  CZ  . TYR   B 88  ? 0.3721 0.3790 0.4809 0.0185  -0.0137 0.0109  94  TYR   C CZ  
1788 O  OH  . TYR   B 88  ? 0.4323 0.4426 0.5551 0.0218  -0.0131 0.0097  94  TYR   C OH  
1789 N  N   . GLN   B 89  ? 0.1871 0.1855 0.2378 0.0070  -0.0070 0.0066  95  GLN   C N   
1790 C  CA  . GLN   B 89  ? 0.1764 0.1742 0.2190 0.0046  -0.0068 0.0069  95  GLN   C CA  
1791 C  C   . GLN   B 89  ? 0.1761 0.1762 0.2159 0.0020  -0.0081 0.0105  95  GLN   C C   
1792 O  O   . GLN   B 89  ? 0.2029 0.2059 0.2442 0.0023  -0.0077 0.0110  95  GLN   C O   
1793 C  CB  . GLN   B 89  ? 0.1891 0.1869 0.2263 0.0055  -0.0040 0.0029  95  GLN   C CB  
1794 C  CG  . GLN   B 89  ? 0.1900 0.1875 0.2202 0.0033  -0.0039 0.0031  95  GLN   C CG  
1795 C  CD  . GLN   B 89  ? 0.1960 0.1920 0.2218 0.0043  -0.0025 -0.0006 95  GLN   C CD  
1796 O  OE1 . GLN   B 89  ? 0.2091 0.2028 0.2361 0.0061  -0.0024 -0.0034 95  GLN   C OE1 
1797 N  NE2 . GLN   B 89  ? 0.1754 0.1722 0.1960 0.0032  -0.0020 -0.0007 95  GLN   C NE2 
1798 N  N   . SER   B 90  ? 0.1665 0.1652 0.2021 -0.0007 -0.0093 0.0128  96  SER   C N   
1799 C  CA  . SER   B 90  ? 0.1631 0.1630 0.1943 -0.0035 -0.0106 0.0159  96  SER   C CA  
1800 C  C   . SER   B 90  ? 0.1747 0.1755 0.1987 -0.0047 -0.0083 0.0139  96  SER   C C   
1801 O  O   . SER   B 90  ? 0.1831 0.1833 0.2055 -0.0037 -0.0063 0.0108  96  SER   C O   
1802 C  CB  . SER   B 90  ? 0.1950 0.1924 0.2246 -0.0062 -0.0129 0.0196  96  SER   C CB  
1803 O  OG  . SER   B 90  ? 0.2234 0.2190 0.2498 -0.0073 -0.0110 0.0182  96  SER   C OG  
1804 N  N   . HIS   B 91  ? 0.1696 0.1715 0.1895 -0.0069 -0.0092 0.0156  97  HIS   C N   
1805 C  CA  . HIS   B 91  ? 0.1654 0.1677 0.1787 -0.0083 -0.0074 0.0140  97  HIS   C CA  
1806 C  C   . HIS   B 91  ? 0.1765 0.1798 0.1902 -0.0060 -0.0053 0.0108  97  HIS   C C   
1807 O  O   . HIS   B 91  ? 0.1826 0.1851 0.1921 -0.0062 -0.0037 0.0086  97  HIS   C O   
1808 C  CB  . HIS   B 91  ? 0.1843 0.1848 0.1933 -0.0099 -0.0060 0.0134  97  HIS   C CB  
1809 C  CG  . HIS   B 91  ? 0.2020 0.2010 0.2082 -0.0129 -0.0075 0.0169  97  HIS   C CG  
1810 N  ND1 . HIS   B 91  ? 0.2435 0.2420 0.2425 -0.0158 -0.0076 0.0179  97  HIS   C ND1 
1811 C  CD2 . HIS   B 91  ? 0.2264 0.2237 0.2354 -0.0134 -0.0091 0.0195  97  HIS   C CD2 
1812 C  CE1 . HIS   B 91  ? 0.2493 0.2457 0.2459 -0.0183 -0.0092 0.0214  97  HIS   C CE1 
1813 N  NE2 . HIS   B 91  ? 0.2466 0.2423 0.2494 -0.0170 -0.0102 0.0227  97  HIS   C NE2 
1814 N  N   . LEU   B 92  ? 0.1789 0.1837 0.1978 -0.0041 -0.0052 0.0105  98  LEU   C N   
1815 C  CA  . LEU   B 92  ? 0.1687 0.1740 0.1871 -0.0023 -0.0029 0.0077  98  LEU   C CA  
1816 C  C   . LEU   B 92  ? 0.1723 0.1797 0.1902 -0.0034 -0.0027 0.0086  98  LEU   C C   
1817 O  O   . LEU   B 92  ? 0.1716 0.1813 0.1936 -0.0042 -0.0044 0.0109  98  LEU   C O   
1818 C  CB  . LEU   B 92  ? 0.1850 0.1903 0.2088 0.0004  -0.0019 0.0062  98  LEU   C CB  
1819 C  CG  . LEU   B 92  ? 0.2103 0.2150 0.2319 0.0021  0.0008  0.0031  98  LEU   C CG  
1820 C  CD1 . LEU   B 92  ? 0.2075 0.2092 0.2228 0.0021  0.0009  0.0010  98  LEU   C CD1 
1821 C  CD2 . LEU   B 92  ? 0.2471 0.2517 0.2740 0.0046  0.0020  0.0013  98  LEU   C CD2 
1822 N  N   . MET   B 93  ? 0.1681 0.1748 0.1814 -0.0035 -0.0011 0.0069  99  MET   C N   
1823 C  CA  . MET   B 93  ? 0.1628 0.1711 0.1756 -0.0048 -0.0007 0.0077  99  MET   C CA  
1824 C  C   . MET   B 93  ? 0.1802 0.1887 0.1929 -0.0035 0.0021  0.0060  99  MET   C C   
1825 O  O   . MET   B 93  ? 0.1919 0.1977 0.2005 -0.0023 0.0031  0.0040  99  MET   C O   
1826 C  CB  . MET   B 93  ? 0.1618 0.1679 0.1680 -0.0067 -0.0013 0.0074  99  MET   C CB  
1827 C  CG  . MET   B 93  ? 0.1930 0.1986 0.1976 -0.0084 -0.0033 0.0086  99  MET   C CG  
1828 S  SD  . MET   B 93  ? 0.2128 0.2156 0.2101 -0.0102 -0.0032 0.0072  99  MET   C SD  
1829 C  CE  . MET   B 93  ? 0.2520 0.2527 0.2483 -0.0078 -0.0014 0.0043  99  MET   C CE  
1830 N  N   . LEU   B 94  ? 0.1643 0.1758 0.1814 -0.0038 0.0033  0.0068  100 LEU   C N   
1831 C  CA  . LEU   B 94  ? 0.1679 0.1796 0.1841 -0.0030 0.0069  0.0053  100 LEU   C CA  
1832 C  C   . LEU   B 94  ? 0.1691 0.1804 0.1815 -0.0052 0.0077  0.0061  100 LEU   C C   
1833 O  O   . LEU   B 94  ? 0.1697 0.1826 0.1840 -0.0073 0.0058  0.0080  100 LEU   C O   
1834 C  CB  . LEU   B 94  ? 0.1887 0.2046 0.2139 -0.0016 0.0090  0.0052  100 LEU   C CB  
1835 C  CG  . LEU   B 94  ? 0.2033 0.2189 0.2331 0.0008  0.0084  0.0042  100 LEU   C CG  
1836 C  CD1 . LEU   B 94  ? 0.2135 0.2331 0.2531 0.0026  0.0110  0.0035  100 LEU   C CD1 
1837 C  CD2 . LEU   B 94  ? 0.2129 0.2240 0.2360 0.0024  0.0092  0.0014  100 LEU   C CD2 
1838 N  N   . ALA   B 95  ? 0.1775 0.1862 0.1842 -0.0050 0.0103  0.0048  101 ALA   C N   
1839 C  CA  . ALA   B 95  ? 0.1841 0.1919 0.1872 -0.0072 0.0116  0.0059  101 ALA   C CA  
1840 C  C   . ALA   B 95  ? 0.1878 0.1958 0.1893 -0.0068 0.0161  0.0049  101 ALA   C C   
1841 O  O   . ALA   B 95  ? 0.1967 0.2035 0.1965 -0.0046 0.0176  0.0027  101 ALA   C O   
1842 C  CB  . ALA   B 95  ? 0.1887 0.1911 0.1834 -0.0078 0.0095  0.0056  101 ALA   C CB  
1843 N  N   . VAL   B 96  ? 0.1878 0.1969 0.1891 -0.0091 0.0185  0.0063  102 VAL   C N   
1844 C  CA  . VAL   B 96  ? 0.1967 0.2048 0.1937 -0.0096 0.0233  0.0056  102 VAL   C CA  
1845 C  C   . VAL   B 96  ? 0.2328 0.2336 0.2174 -0.0100 0.0218  0.0054  102 VAL   C C   
1846 O  O   . VAL   B 96  ? 0.2567 0.2545 0.2377 -0.0119 0.0194  0.0072  102 VAL   C O   
1847 C  CB  . VAL   B 96  ? 0.2055 0.2178 0.2077 -0.0125 0.0263  0.0076  102 VAL   C CB  
1848 C  CG1 . VAL   B 96  ? 0.2164 0.2273 0.2127 -0.0135 0.0321  0.0070  102 VAL   C CG1 
1849 C  CG2 . VAL   B 96  ? 0.2102 0.2301 0.2265 -0.0118 0.0266  0.0078  102 VAL   C CG2 
1850 N  N   . GLY   B 97  ? 0.2525 0.2500 0.2309 -0.0082 0.0229  0.0033  103 GLY   C N   
1851 C  CA  . GLY   B 97  ? 0.2705 0.2607 0.2375 -0.0084 0.0206  0.0032  103 GLY   C CA  
1852 C  C   . GLY   B 97  ? 0.2878 0.2748 0.2489 -0.0063 0.0211  0.0004  103 GLY   C C   
1853 O  O   . GLY   B 97  ? 0.3031 0.2933 0.2692 -0.0045 0.0233  -0.0018 103 GLY   C O   
1854 N  N   . HIS   B 98  ? 0.2816 0.2619 0.2324 -0.0066 0.0185  0.0005  104 HIS   C N   
1855 C  CA  . HIS   B 98  ? 0.2810 0.2571 0.2243 -0.0051 0.0182  -0.0021 104 HIS   C CA  
1856 C  C   . HIS   B 98  ? 0.2827 0.2580 0.2292 -0.0027 0.0134  -0.0039 104 HIS   C C   
1857 O  O   . HIS   B 98  ? 0.2772 0.2514 0.2254 -0.0026 0.0091  -0.0027 104 HIS   C O   
1858 C  CB  . HIS   B 98  ? 0.2951 0.2637 0.2247 -0.0070 0.0172  -0.0007 104 HIS   C CB  
1859 C  CG  . HIS   B 98  ? 0.3036 0.2671 0.2238 -0.0060 0.0165  -0.0034 104 HIS   C CG  
1860 N  ND1 . HIS   B 98  ? 0.3330 0.2975 0.2504 -0.0058 0.0220  -0.0061 104 HIS   C ND1 
1861 C  CD2 . HIS   B 98  ? 0.3076 0.2652 0.2215 -0.0051 0.0108  -0.0041 104 HIS   C CD2 
1862 C  CE1 . HIS   B 98  ? 0.3418 0.3003 0.2499 -0.0049 0.0193  -0.0084 104 HIS   C CE1 
1863 N  NE2 . HIS   B 98  ? 0.3404 0.2947 0.2464 -0.0045 0.0122  -0.0071 104 HIS   C NE2 
1864 N  N   . SER   B 99  ? 0.2924 0.2681 0.2401 -0.0008 0.0143  -0.0069 105 SER   C N   
1865 C  CA  . SER   B 99  ? 0.3062 0.2809 0.2570 0.0013  0.0101  -0.0088 105 SER   C CA  
1866 C  C   . SER   B 99  ? 0.3425 0.3142 0.2882 0.0025  0.0115  -0.0123 105 SER   C C   
1867 O  O   . SER   B 99  ? 0.3694 0.3435 0.3172 0.0029  0.0163  -0.0139 105 SER   C O   
1868 C  CB  . SER   B 99  ? 0.3504 0.3310 0.3134 0.0023  0.0100  -0.0085 105 SER   C CB  
1869 O  OG  . SER   B 99  ? 0.4225 0.4022 0.3888 0.0038  0.0064  -0.0100 105 SER   C OG  
1870 N  N   . GLU   B 100 ? 0.3236 0.2898 0.2627 0.0029  0.0071  -0.0136 106 GLU   C N   
1871 C  CA  . GLU   B 100 ? 0.3494 0.3115 0.2824 0.0038  0.0071  -0.0173 106 GLU   C CA  
1872 C  C   . GLU   B 100 ? 0.3458 0.3074 0.2846 0.0054  0.0020  -0.0188 106 GLU   C C   
1873 O  O   . GLU   B 100 ? 0.3330 0.2964 0.2778 0.0055  -0.0015 -0.0169 106 GLU   C O   
1874 C  CB  . GLU   B 100 ? 0.4100 0.3647 0.3281 0.0023  0.0051  -0.0169 106 GLU   C CB  
1875 C  CG  . GLU   B 100 ? 0.5133 0.4662 0.4217 0.0006  0.0110  -0.0173 106 GLU   C CG  
1876 C  CD  . GLU   B 100 ? 0.5496 0.4943 0.4428 -0.0012 0.0072  -0.0161 106 GLU   C CD  
1877 O  OE1 . GLU   B 100 ? 0.6027 0.5421 0.4900 -0.0005 0.0024  -0.0183 106 GLU   C OE1 
1878 O  OE2 . GLU   B 100 ? 0.5025 0.4458 0.3904 -0.0034 0.0081  -0.0126 106 GLU   C OE2 
1879 N  N   . PRO   B 101 ? 0.3764 0.3351 0.3132 0.0065  0.0015  -0.0226 107 PRO   C N   
1880 C  CA  . PRO   B 101 ? 0.3926 0.3501 0.3344 0.0075  -0.0039 -0.0239 107 PRO   C CA  
1881 C  C   . PRO   B 101 ? 0.3884 0.3415 0.3237 0.0066  -0.0097 -0.0226 107 PRO   C C   
1882 O  O   . PRO   B 101 ? 0.4263 0.3737 0.3491 0.0056  -0.0107 -0.0227 107 PRO   C O   
1883 C  CB  . PRO   B 101 ? 0.4100 0.3637 0.3479 0.0084  -0.0030 -0.0284 107 PRO   C CB  
1884 C  CG  . PRO   B 101 ? 0.4148 0.3701 0.3506 0.0086  0.0041  -0.0294 107 PRO   C CG  
1885 C  CD  . PRO   B 101 ? 0.3846 0.3405 0.3142 0.0068  0.0058  -0.0260 107 PRO   C CD  
1886 N  N   . GLY   B 102 ? 0.3310 0.2868 0.2753 0.0070  -0.0133 -0.0212 108 GLY   C N   
1887 C  CA  . GLY   B 102 ? 0.3060 0.2596 0.2493 0.0066  -0.0189 -0.0196 108 GLY   C CA  
1888 C  C   . GLY   B 102 ? 0.2850 0.2430 0.2345 0.0063  -0.0177 -0.0164 108 GLY   C C   
1889 O  O   . GLY   B 102 ? 0.2745 0.2326 0.2283 0.0065  -0.0217 -0.0155 108 GLY   C O   
1890 N  N   . ASP   B 103 ? 0.2595 0.2211 0.2103 0.0058  -0.0123 -0.0150 109 ASP   C N   
1891 C  CA  . ASP   B 103 ? 0.2438 0.2090 0.1995 0.0052  -0.0113 -0.0123 109 ASP   C CA  
1892 C  C   . ASP   B 103 ? 0.2250 0.1956 0.1922 0.0057  -0.0110 -0.0121 109 ASP   C C   
1893 O  O   . ASP   B 103 ? 0.2179 0.1906 0.1888 0.0052  -0.0110 -0.0104 109 ASP   C O   
1894 C  CB  . ASP   B 103 ? 0.2531 0.2197 0.2051 0.0040  -0.0064 -0.0106 109 ASP   C CB  
1895 C  CG  . ASP   B 103 ? 0.2864 0.2472 0.2264 0.0027  -0.0068 -0.0095 109 ASP   C CG  
1896 O  OD1 . ASP   B 103 ? 0.2948 0.2512 0.2309 0.0026  -0.0117 -0.0089 109 ASP   C OD1 
1897 O  OD2 . ASP   B 103 ? 0.2822 0.2430 0.2170 0.0016  -0.0023 -0.0092 109 ASP   C OD2 
1898 N  N   . CYS   B 104 ? 0.2142 0.1866 0.1867 0.0064  -0.0106 -0.0138 110 CYS   C N   
1899 C  CA  . CYS   B 104 ? 0.2148 0.1918 0.1973 0.0064  -0.0102 -0.0132 110 CYS   C CA  
1900 C  C   . CYS   B 104 ? 0.2131 0.1905 0.1996 0.0064  -0.0133 -0.0130 110 CYS   C C   
1901 O  O   . CYS   B 104 ? 0.2288 0.2030 0.2137 0.0069  -0.0172 -0.0142 110 CYS   C O   
1902 C  CB  . CYS   B 104 ? 0.2236 0.2012 0.2106 0.0070  -0.0100 -0.0149 110 CYS   C CB  
1903 S  SG  . CYS   B 104 ? 0.2782 0.2569 0.2646 0.0075  -0.0056 -0.0152 110 CYS   C SG  
1904 N  N   . GLY   B 105 ? 0.2019 0.1830 0.1935 0.0057  -0.0116 -0.0116 111 GLY   C N   
1905 C  CA  . GLY   B 105 ? 0.2134 0.1955 0.2099 0.0058  -0.0135 -0.0119 111 GLY   C CA  
1906 C  C   . GLY   B 105 ? 0.2132 0.1939 0.2064 0.0056  -0.0137 -0.0108 111 GLY   C C   
1907 O  O   . GLY   B 105 ? 0.2185 0.2005 0.2165 0.0057  -0.0142 -0.0111 111 GLY   C O   
1908 N  N   . GLY   B 106 ? 0.1928 0.1709 0.1785 0.0052  -0.0130 -0.0096 112 GLY   C N   
1909 C  CA  . GLY   B 106 ? 0.1837 0.1602 0.1663 0.0047  -0.0131 -0.0083 112 GLY   C CA  
1910 C  C   . GLY   B 106 ? 0.1898 0.1700 0.1765 0.0037  -0.0103 -0.0076 112 GLY   C C   
1911 O  O   . GLY   B 106 ? 0.2001 0.1835 0.1883 0.0029  -0.0076 -0.0070 112 GLY   C O   
1912 N  N   . ILE   B 107 ? 0.1929 0.1722 0.1814 0.0037  -0.0112 -0.0078 113 ILE   C N   
1913 C  CA  . ILE   B 107 ? 0.1905 0.1728 0.1820 0.0026  -0.0087 -0.0077 113 ILE   C CA  
1914 C  C   . ILE   B 107 ? 0.1816 0.1630 0.1684 0.0010  -0.0072 -0.0059 113 ILE   C C   
1915 O  O   . ILE   B 107 ? 0.1946 0.1722 0.1771 0.0009  -0.0086 -0.0050 113 ILE   C O   
1916 C  CB  . ILE   B 107 ? 0.2200 0.2022 0.2168 0.0035  -0.0096 -0.0097 113 ILE   C CB  
1917 C  CG1 . ILE   B 107 ? 0.2440 0.2290 0.2477 0.0044  -0.0098 -0.0114 113 ILE   C CG1 
1918 C  CG2 . ILE   B 107 ? 0.2512 0.2347 0.2484 0.0022  -0.0069 -0.0100 113 ILE   C CG2 
1919 C  CD1 . ILE   B 107 ? 0.2917 0.2771 0.3025 0.0057  -0.0106 -0.0137 113 ILE   C CD1 
1920 N  N   . LEU   B 108 ? 0.1632 0.1479 0.1511 -0.0004 -0.0048 -0.0052 114 LEU   C N   
1921 C  CA  . LEU   B 108 ? 0.1703 0.1550 0.1555 -0.0023 -0.0038 -0.0037 114 LEU   C CA  
1922 C  C   . LEU   B 108 ? 0.1817 0.1662 0.1682 -0.0031 -0.0034 -0.0050 114 LEU   C C   
1923 O  O   . LEU   B 108 ? 0.1788 0.1657 0.1681 -0.0031 -0.0023 -0.0061 114 LEU   C O   
1924 C  CB  . LEU   B 108 ? 0.1706 0.1590 0.1568 -0.0034 -0.0021 -0.0022 114 LEU   C CB  
1925 C  CG  . LEU   B 108 ? 0.1769 0.1664 0.1621 -0.0056 -0.0015 -0.0006 114 LEU   C CG  
1926 C  CD1 . LEU   B 108 ? 0.2017 0.1888 0.1837 -0.0064 -0.0015 0.0006  114 LEU   C CD1 
1927 C  CD2 . LEU   B 108 ? 0.1841 0.1775 0.1722 -0.0063 -0.0006 0.0009  114 LEU   C CD2 
1928 N  N   . ARG   B 109 ? 0.1802 0.1615 0.1643 -0.0038 -0.0042 -0.0049 115 ARG   C N   
1929 C  CA  . ARG   B 109 ? 0.1931 0.1734 0.1778 -0.0045 -0.0038 -0.0068 115 ARG   C CA  
1930 C  C   . ARG   B 109 ? 0.2050 0.1841 0.1863 -0.0069 -0.0038 -0.0055 115 ARG   C C   
1931 O  O   . ARG   B 109 ? 0.2186 0.1962 0.1979 -0.0077 -0.0046 -0.0034 115 ARG   C O   
1932 C  CB  . ARG   B 109 ? 0.2190 0.1952 0.2053 -0.0026 -0.0056 -0.0086 115 ARG   C CB  
1933 C  CG  . ARG   B 109 ? 0.2865 0.2639 0.2780 -0.0003 -0.0059 -0.0107 115 ARG   C CG  
1934 C  CD  . ARG   B 109 ? 0.3305 0.3034 0.3243 0.0018  -0.0089 -0.0117 115 ARG   C CD  
1935 N  NE  . ARG   B 109 ? 0.4302 0.4029 0.4263 0.0038  -0.0115 -0.0114 115 ARG   C NE  
1936 C  CZ  . ARG   B 109 ? 0.4597 0.4350 0.4628 0.0054  -0.0117 -0.0135 115 ARG   C CZ  
1937 N  NH1 . ARG   B 109 ? 0.4690 0.4472 0.4773 0.0055  -0.0088 -0.0162 115 ARG   C NH1 
1938 N  NH2 . ARG   B 109 ? 0.4448 0.4196 0.4496 0.0069  -0.0147 -0.0132 115 ARG   C NH2 
1939 N  N   . CYS   B 110 ? 0.1942 0.1735 0.1748 -0.0083 -0.0029 -0.0069 116 CYS   C N   
1940 C  CA  . CYS   B 110 ? 0.2100 0.1873 0.1874 -0.0109 -0.0035 -0.0063 116 CYS   C CA  
1941 C  C   . CYS   B 110 ? 0.2269 0.2000 0.2038 -0.0105 -0.0036 -0.0095 116 CYS   C C   
1942 O  O   . CYS   B 110 ? 0.2224 0.1947 0.2022 -0.0082 -0.0031 -0.0119 116 CYS   C O   
1943 C  CB  . CYS   B 110 ? 0.2084 0.1891 0.1844 -0.0132 -0.0030 -0.0052 116 CYS   C CB  
1944 S  SG  . CYS   B 110 ? 0.1987 0.1804 0.1733 -0.0135 -0.0010 -0.0080 116 CYS   C SG  
1945 N  N   . GLN   B 111 ? 0.2437 0.2142 0.2175 -0.0129 -0.0043 -0.0100 117 GLN   C N   
1946 C  CA  . GLN   B 111 ? 0.2656 0.2315 0.2387 -0.0126 -0.0042 -0.0136 117 GLN   C CA  
1947 C  C   . GLN   B 111 ? 0.2734 0.2409 0.2469 -0.0118 -0.0013 -0.0173 117 GLN   C C   
1948 O  O   . GLN   B 111 ? 0.3017 0.2661 0.2766 -0.0105 -0.0003 -0.0210 117 GLN   C O   
1949 C  CB  . GLN   B 111 ? 0.2933 0.2559 0.2626 -0.0157 -0.0057 -0.0135 117 GLN   C CB  
1950 C  CG  . GLN   B 111 ? 0.3434 0.3087 0.3087 -0.0186 -0.0052 -0.0134 117 GLN   C CG  
1951 C  CD  . GLN   B 111 ? 0.4604 0.4221 0.4221 -0.0219 -0.0074 -0.0135 117 GLN   C CD  
1952 O  OE1 . GLN   B 111 ? 0.5035 0.4672 0.4655 -0.0241 -0.0093 -0.0102 117 GLN   C OE1 
1953 N  NE2 . GLN   B 111 ? 0.4895 0.4460 0.4486 -0.0222 -0.0072 -0.0175 117 GLN   C NE2 
1954 N  N   . HIS   B 112 ? 0.2404 0.2127 0.2132 -0.0125 0.0004  -0.0162 118 HIS   C N   
1955 C  CA  . HIS   B 112 ? 0.2388 0.2127 0.2112 -0.0126 0.0037  -0.0192 118 HIS   C CA  
1956 C  C   . HIS   B 112 ? 0.2525 0.2296 0.2311 -0.0099 0.0054  -0.0198 118 HIS   C C   
1957 O  O   . HIS   B 112 ? 0.2800 0.2584 0.2596 -0.0097 0.0087  -0.0226 118 HIS   C O   
1958 C  CB  . HIS   B 112 ? 0.2281 0.2044 0.1949 -0.0157 0.0043  -0.0173 118 HIS   C CB  
1959 C  CG  . HIS   B 112 ? 0.2344 0.2079 0.1954 -0.0187 0.0019  -0.0165 118 HIS   C CG  
1960 N  ND1 . HIS   B 112 ? 0.2255 0.2008 0.1864 -0.0202 -0.0010 -0.0124 118 HIS   C ND1 
1961 C  CD2 . HIS   B 112 ? 0.2565 0.2257 0.2124 -0.0205 0.0021  -0.0196 118 HIS   C CD2 
1962 C  CE1 . HIS   B 112 ? 0.2588 0.2311 0.2151 -0.0230 -0.0029 -0.0128 118 HIS   C CE1 
1963 N  NE2 . HIS   B 112 ? 0.2725 0.2406 0.2250 -0.0233 -0.0014 -0.0171 118 HIS   C NE2 
1964 N  N   . GLY   B 113 ? 0.2279 0.2060 0.2104 -0.0080 0.0033  -0.0175 119 GLY   C N   
1965 C  CA  . GLY   B 113 ? 0.2173 0.1982 0.2059 -0.0056 0.0041  -0.0181 119 GLY   C CA  
1966 C  C   . GLY   B 113 ? 0.1965 0.1799 0.1858 -0.0053 0.0025  -0.0146 119 GLY   C C   
1967 O  O   . GLY   B 113 ? 0.2048 0.1876 0.1911 -0.0061 0.0007  -0.0119 119 GLY   C O   
1968 N  N   . VAL   B 114 ? 0.1889 0.1754 0.1826 -0.0042 0.0035  -0.0150 120 VAL   C N   
1969 C  CA  . VAL   B 114 ? 0.1876 0.1762 0.1824 -0.0037 0.0022  -0.0124 120 VAL   C CA  
1970 C  C   . VAL   B 114 ? 0.1796 0.1703 0.1709 -0.0060 0.0030  -0.0099 120 VAL   C C   
1971 O  O   . VAL   B 114 ? 0.1907 0.1828 0.1807 -0.0078 0.0052  -0.0102 120 VAL   C O   
1972 C  CB  . VAL   B 114 ? 0.2024 0.1934 0.2038 -0.0021 0.0028  -0.0138 120 VAL   C CB  
1973 C  CG1 . VAL   B 114 ? 0.2088 0.2013 0.2108 -0.0019 0.0015  -0.0116 120 VAL   C CG1 
1974 C  CG2 . VAL   B 114 ? 0.2162 0.2051 0.2223 0.0005  0.0007  -0.0159 120 VAL   C CG2 
1975 N  N   . VAL   B 115 ? 0.1791 0.1699 0.1689 -0.0061 0.0013  -0.0073 121 VAL   C N   
1976 C  CA  . VAL   B 115 ? 0.1675 0.1603 0.1557 -0.0078 0.0013  -0.0048 121 VAL   C CA  
1977 C  C   . VAL   B 115 ? 0.1735 0.1684 0.1652 -0.0068 0.0012  -0.0037 121 VAL   C C   
1978 O  O   . VAL   B 115 ? 0.1799 0.1765 0.1718 -0.0081 0.0016  -0.0022 121 VAL   C O   
1979 C  CB  . VAL   B 115 ? 0.1749 0.1669 0.1610 -0.0085 -0.0001 -0.0029 121 VAL   C CB  
1980 C  CG1 . VAL   B 115 ? 0.1967 0.1914 0.1835 -0.0097 -0.0006 -0.0002 121 VAL   C CG1 
1981 C  CG2 . VAL   B 115 ? 0.1879 0.1774 0.1707 -0.0099 -0.0004 -0.0038 121 VAL   C CG2 
1982 N  N   . GLY   B 116 ? 0.1656 0.1598 0.1595 -0.0046 0.0003  -0.0044 122 GLY   C N   
1983 C  CA  . GLY   B 116 ? 0.1884 0.1839 0.1852 -0.0037 0.0000  -0.0038 122 GLY   C CA  
1984 C  C   . GLY   B 116 ? 0.1736 0.1673 0.1710 -0.0015 -0.0014 -0.0049 122 GLY   C C   
1985 O  O   . GLY   B 116 ? 0.1766 0.1680 0.1726 -0.0008 -0.0024 -0.0060 122 GLY   C O   
1986 N  N   . ILE   B 117 ? 0.1699 0.1640 0.1690 -0.0006 -0.0019 -0.0048 123 ILE   C N   
1987 C  CA  . ILE   B 117 ? 0.1801 0.1718 0.1783 0.0011  -0.0035 -0.0061 123 ILE   C CA  
1988 C  C   . ILE   B 117 ? 0.1711 0.1624 0.1673 0.0016  -0.0031 -0.0055 123 ILE   C C   
1989 O  O   . ILE   B 117 ? 0.1653 0.1587 0.1642 0.0012  -0.0020 -0.0045 123 ILE   C O   
1990 C  CB  . ILE   B 117 ? 0.1967 0.1885 0.1995 0.0019  -0.0048 -0.0078 123 ILE   C CB  
1991 C  CG1 . ILE   B 117 ? 0.2095 0.2036 0.2163 0.0011  -0.0037 -0.0071 123 ILE   C CG1 
1992 C  CG2 . ILE   B 117 ? 0.2246 0.2165 0.2303 0.0021  -0.0054 -0.0092 123 ILE   C CG2 
1993 C  CD1 . ILE   B 117 ? 0.2374 0.2314 0.2494 0.0017  -0.0052 -0.0087 123 ILE   C CD1 
1994 N  N   . VAL   B 118 ? 0.1607 0.1490 0.1525 0.0025  -0.0039 -0.0062 124 VAL   C N   
1995 C  CA  . VAL   B 118 ? 0.1648 0.1528 0.1545 0.0030  -0.0026 -0.0064 124 VAL   C CA  
1996 C  C   . VAL   B 118 ? 0.1633 0.1517 0.1571 0.0040  -0.0029 -0.0076 124 VAL   C C   
1997 O  O   . VAL   B 118 ? 0.1814 0.1685 0.1768 0.0045  -0.0051 -0.0090 124 VAL   C O   
1998 C  CB  . VAL   B 118 ? 0.1773 0.1611 0.1599 0.0035  -0.0034 -0.0072 124 VAL   C CB  
1999 C  CG1 . VAL   B 118 ? 0.1937 0.1769 0.1736 0.0040  -0.0012 -0.0081 124 VAL   C CG1 
2000 C  CG2 . VAL   B 118 ? 0.1983 0.1809 0.1768 0.0023  -0.0031 -0.0055 124 VAL   C CG2 
2001 N  N   . SER   B 119 ? 0.1642 0.1545 0.1606 0.0042  -0.0011 -0.0071 125 SER   C N   
2002 C  CA  . SER   B 119 ? 0.1752 0.1654 0.1760 0.0050  -0.0014 -0.0081 125 SER   C CA  
2003 C  C   . SER   B 119 ? 0.1972 0.1866 0.1975 0.0063  0.0004  -0.0095 125 SER   C C   
2004 O  O   . SER   B 119 ? 0.2005 0.1879 0.2023 0.0074  -0.0003 -0.0115 125 SER   C O   
2005 C  CB  . SER   B 119 ? 0.1826 0.1758 0.1892 0.0040  -0.0014 -0.0059 125 SER   C CB  
2006 O  OG  . SER   B 119 ? 0.1944 0.1870 0.2058 0.0046  -0.0020 -0.0063 125 SER   C OG  
2007 N  N   . THR   B 120 ? 0.1983 0.1892 0.1968 0.0061  0.0029  -0.0088 126 THR   C N   
2008 C  CA  . THR   B 120 ? 0.2188 0.2095 0.2176 0.0074  0.0057  -0.0106 126 THR   C CA  
2009 C  C   . THR   B 120 ? 0.2293 0.2196 0.2216 0.0068  0.0085  -0.0107 126 THR   C C   
2010 O  O   . THR   B 120 ? 0.2053 0.1958 0.1944 0.0052  0.0079  -0.0087 126 THR   C O   
2011 C  CB  . THR   B 120 ? 0.2386 0.2333 0.2465 0.0079  0.0070  -0.0091 126 THR   C CB  
2012 O  OG1 . THR   B 120 ? 0.2612 0.2596 0.2705 0.0065  0.0080  -0.0064 126 THR   C OG1 
2013 C  CG2 . THR   B 120 ? 0.2531 0.2481 0.2671 0.0080  0.0043  -0.0079 126 THR   C CG2 
2014 N  N   . GLY   B 121 ? 0.2602 0.2494 0.2502 0.0077  0.0116  -0.0130 127 GLY   C N   
2015 C  CA  . GLY   B 121 ? 0.2943 0.2831 0.2779 0.0067  0.0151  -0.0130 127 GLY   C CA  
2016 C  C   . GLY   B 121 ? 0.3308 0.3206 0.3160 0.0079  0.0200  -0.0156 127 GLY   C C   
2017 O  O   . GLY   B 121 ? 0.3227 0.3122 0.3128 0.0098  0.0201  -0.0180 127 GLY   C O   
2018 N  N   . GLY   B 122 ? 0.3710 0.3620 0.3527 0.0066  0.0243  -0.0152 128 GLY   C N   
2019 C  CA  . GLY   B 122 ? 0.3899 0.3823 0.3730 0.0075  0.0302  -0.0180 128 GLY   C CA  
2020 C  C   . GLY   B 122 ? 0.3910 0.3898 0.3817 0.0064  0.0342  -0.0159 128 GLY   C C   
2021 O  O   . GLY   B 122 ? 0.3929 0.3955 0.3905 0.0055  0.0316  -0.0125 128 GLY   C O   
2022 N  N   . ASN   B 123 ? 0.3805 0.3806 0.3700 0.0063  0.0409  -0.0181 129 ASN   C N   
2023 C  CA  . ASN   B 123 ? 0.3735 0.3803 0.3714 0.0050  0.0455  -0.0164 129 ASN   C CA  
2024 C  C   . ASN   B 123 ? 0.3526 0.3602 0.3474 0.0017  0.0441  -0.0121 129 ASN   C C   
2025 O  O   . ASN   B 123 ? 0.3616 0.3752 0.3665 0.0006  0.0451  -0.0097 129 ASN   C O   
2026 C  CB  . ASN   B 123 ? 0.3962 0.4094 0.4113 0.0072  0.0447  -0.0161 129 ASN   C CB  
2027 C  CG  . ASN   B 123 ? 0.4294 0.4441 0.4510 0.0101  0.0496  -0.0206 129 ASN   C CG  
2028 O  OD1 . ASN   B 123 ? 0.4367 0.4492 0.4509 0.0100  0.0554  -0.0240 129 ASN   C OD1 
2029 N  ND2 . ASN   B 123 ? 0.4433 0.4612 0.4785 0.0126  0.0472  -0.0207 129 ASN   C ND2 
2030 N  N   . GLY   B 124 ? 0.3131 0.3143 0.2945 0.0001  0.0413  -0.0110 130 GLY   C N   
2031 C  CA  . GLY   B 124 ? 0.2881 0.2890 0.2664 -0.0029 0.0393  -0.0070 130 GLY   C CA  
2032 C  C   . GLY   B 124 ? 0.2548 0.2584 0.2415 -0.0028 0.0338  -0.0044 130 GLY   C C   
2033 O  O   . GLY   B 124 ? 0.2683 0.2735 0.2566 -0.0051 0.0329  -0.0014 130 GLY   C O   
2034 N  N   . LEU   B 125 ? 0.2417 0.2452 0.2326 -0.0004 0.0301  -0.0056 131 LEU   C N   
2035 C  CA  . LEU   B 125 ? 0.2243 0.2296 0.2214 -0.0004 0.0252  -0.0035 131 LEU   C CA  
2036 C  C   . LEU   B 125 ? 0.2336 0.2335 0.2240 0.0006  0.0207  -0.0043 131 LEU   C C   
2037 O  O   . LEU   B 125 ? 0.2705 0.2667 0.2554 0.0019  0.0210  -0.0069 131 LEU   C O   
2038 C  CB  . LEU   B 125 ? 0.2404 0.2508 0.2501 0.0015  0.0250  -0.0038 131 LEU   C CB  
2039 C  CG  . LEU   B 125 ? 0.2714 0.2880 0.2908 0.0011  0.0290  -0.0033 131 LEU   C CG  
2040 C  CD1 . LEU   B 125 ? 0.2849 0.3051 0.3161 0.0039  0.0290  -0.0046 131 LEU   C CD1 
2041 C  CD2 . LEU   B 125 ? 0.2794 0.2993 0.3027 -0.0016 0.0271  0.0003  131 LEU   C CD2 
2042 N  N   . VAL   B 126 ? 0.1912 0.1910 0.1825 -0.0003 0.0168  -0.0023 132 VAL   C N   
2043 C  CA  . VAL   B 126 ? 0.1867 0.1829 0.1746 0.0006  0.0128  -0.0030 132 VAL   C CA  
2044 C  C   . VAL   B 126 ? 0.1843 0.1835 0.1797 0.0007  0.0103  -0.0018 132 VAL   C C   
2045 O  O   . VAL   B 126 ? 0.1929 0.1951 0.1922 -0.0008 0.0101  0.0003  132 VAL   C O   
2046 C  CB  . VAL   B 126 ? 0.2223 0.2140 0.2021 -0.0007 0.0107  -0.0022 132 VAL   C CB  
2047 C  CG1 . VAL   B 126 ? 0.2682 0.2613 0.2489 -0.0030 0.0106  0.0004  132 VAL   C CG1 
2048 C  CG2 . VAL   B 126 ? 0.2181 0.2071 0.1969 0.0003  0.0067  -0.0031 132 VAL   C CG2 
2049 N  N   . GLY   B 127 ? 0.1770 0.1751 0.1741 0.0022  0.0084  -0.0031 133 GLY   C N   
2050 C  CA  . GLY   B 127 ? 0.1720 0.1723 0.1750 0.0019  0.0063  -0.0017 133 GLY   C CA  
2051 C  C   . GLY   B 127 ? 0.1652 0.1632 0.1653 0.0015  0.0037  -0.0018 133 GLY   C C   
2052 O  O   . GLY   B 127 ? 0.1771 0.1720 0.1738 0.0025  0.0029  -0.0037 133 GLY   C O   
2053 N  N   . PHE   B 128 ? 0.1542 0.1536 0.1556 0.0000  0.0024  0.0000  134 PHE   C N   
2054 C  CA  . PHE   B 128 ? 0.1644 0.1623 0.1640 -0.0006 0.0009  -0.0005 134 PHE   C CA  
2055 C  C   . PHE   B 128 ? 0.1666 0.1659 0.1699 -0.0013 0.0000  0.0007  134 PHE   C C   
2056 O  O   . PHE   B 128 ? 0.1702 0.1716 0.1756 -0.0024 -0.0003 0.0028  134 PHE   C O   
2057 C  CB  . PHE   B 128 ? 0.1754 0.1728 0.1717 -0.0022 0.0006  0.0003  134 PHE   C CB  
2058 C  CG  . PHE   B 128 ? 0.1742 0.1698 0.1665 -0.0022 0.0013  0.0001  134 PHE   C CG  
2059 C  CD1 . PHE   B 128 ? 0.1818 0.1739 0.1701 -0.0014 0.0004  -0.0013 134 PHE   C CD1 
2060 C  CD2 . PHE   B 128 ? 0.1817 0.1790 0.1745 -0.0034 0.0026  0.0016  134 PHE   C CD2 
2061 C  CE1 . PHE   B 128 ? 0.1809 0.1704 0.1644 -0.0018 0.0008  -0.0009 134 PHE   C CE1 
2062 C  CE2 . PHE   B 128 ? 0.1938 0.1891 0.1825 -0.0039 0.0035  0.0018  134 PHE   C CE2 
2063 C  CZ  . PHE   B 128 ? 0.1959 0.1870 0.1793 -0.0032 0.0027  0.0007  134 PHE   C CZ  
2064 N  N   . ALA   B 129 ? 0.1595 0.1577 0.1636 -0.0008 -0.0006 -0.0005 135 ALA   C N   
2065 C  CA  . ALA   B 129 ? 0.1502 0.1493 0.1568 -0.0021 -0.0010 0.0008  135 ALA   C CA  
2066 C  C   . ALA   B 129 ? 0.1477 0.1470 0.1512 -0.0040 -0.0006 0.0012  135 ALA   C C   
2067 O  O   . ALA   B 129 ? 0.1541 0.1525 0.1562 -0.0037 -0.0002 -0.0007 135 ALA   C O   
2068 C  CB  . ALA   B 129 ? 0.1601 0.1580 0.1693 -0.0013 -0.0014 -0.0008 135 ALA   C CB  
2069 N  N   . ASP   B 130 ? 0.1493 0.1497 0.1519 -0.0060 -0.0009 0.0035  136 ASP   C N   
2070 C  CA  . ASP   B 130 ? 0.1593 0.1594 0.1578 -0.0081 -0.0004 0.0035  136 ASP   C CA  
2071 C  C   . ASP   B 130 ? 0.1722 0.1720 0.1707 -0.0090 0.0010  0.0026  136 ASP   C C   
2072 O  O   . ASP   B 130 ? 0.1718 0.1719 0.1730 -0.0093 0.0009  0.0037  136 ASP   C O   
2073 C  CB  . ASP   B 130 ? 0.1751 0.1758 0.1718 -0.0103 -0.0018 0.0064  136 ASP   C CB  
2074 C  CG  . ASP   B 130 ? 0.2588 0.2586 0.2498 -0.0127 -0.0014 0.0061  136 ASP   C CG  
2075 O  OD1 . ASP   B 130 ? 0.2591 0.2580 0.2481 -0.0124 -0.0008 0.0042  136 ASP   C OD1 
2076 O  OD2 . ASP   B 130 ? 0.3010 0.3003 0.2889 -0.0151 -0.0018 0.0078  136 ASP   C OD2 
2077 N  N   . VAL   B 131 ? 0.1622 0.1615 0.1581 -0.0097 0.0025  0.0006  137 VAL   C N   
2078 C  CA  . VAL   B 131 ? 0.1685 0.1683 0.1649 -0.0109 0.0048  -0.0005 137 VAL   C CA  
2079 C  C   . VAL   B 131 ? 0.1830 0.1820 0.1733 -0.0135 0.0065  -0.0007 137 VAL   C C   
2080 O  O   . VAL   B 131 ? 0.1987 0.1981 0.1885 -0.0150 0.0093  -0.0019 137 VAL   C O   
2081 C  CB  . VAL   B 131 ? 0.1796 0.1797 0.1806 -0.0089 0.0058  -0.0037 137 VAL   C CB  
2082 C  CG1 . VAL   B 131 ? 0.1763 0.1764 0.1821 -0.0067 0.0038  -0.0037 137 VAL   C CG1 
2083 C  CG2 . VAL   B 131 ? 0.1895 0.1883 0.1888 -0.0078 0.0057  -0.0060 137 VAL   C CG2 
2084 N  N   . ARG   B 132 ? 0.1784 0.1763 0.1642 -0.0145 0.0049  0.0002  138 ARG   C N   
2085 C  CA  . ARG   B 132 ? 0.1690 0.1654 0.1481 -0.0170 0.0061  -0.0007 138 ARG   C CA  
2086 C  C   . ARG   B 132 ? 0.2041 0.2000 0.1781 -0.0203 0.0070  0.0014  138 ARG   C C   
2087 O  O   . ARG   B 132 ? 0.2280 0.2223 0.1955 -0.0226 0.0092  -0.0002 138 ARG   C O   
2088 C  CB  . ARG   B 132 ? 0.1717 0.1667 0.1475 -0.0175 0.0035  0.0000  138 ARG   C CB  
2089 C  CG  . ARG   B 132 ? 0.1814 0.1759 0.1603 -0.0150 0.0031  -0.0020 138 ARG   C CG  
2090 C  CD  . ARG   B 132 ? 0.1771 0.1707 0.1537 -0.0160 0.0007  -0.0007 138 ARG   C CD  
2091 N  NE  . ARG   B 132 ? 0.1794 0.1751 0.1591 -0.0158 -0.0014 0.0025  138 ARG   C NE  
2092 C  CZ  . ARG   B 132 ? 0.1928 0.1891 0.1734 -0.0164 -0.0034 0.0041  138 ARG   C CZ  
2093 N  NH1 . ARG   B 132 ? 0.1792 0.1735 0.1565 -0.0178 -0.0041 0.0031  138 ARG   C NH1 
2094 N  NH2 . ARG   B 132 ? 0.1857 0.1845 0.1710 -0.0157 -0.0047 0.0065  138 ARG   C NH2 
2095 N  N   . ASP   B 133 ? 0.1912 0.1878 0.1672 -0.0207 0.0052  0.0048  139 ASP   C N   
2096 C  CA  . ASP   B 133 ? 0.2050 0.2003 0.1756 -0.0241 0.0055  0.0076  139 ASP   C CA  
2097 C  C   . ASP   B 133 ? 0.2131 0.2091 0.1852 -0.0249 0.0097  0.0065  139 ASP   C C   
2098 O  O   . ASP   B 133 ? 0.2343 0.2289 0.2005 -0.0284 0.0109  0.0086  139 ASP   C O   
2099 C  CB  . ASP   B 133 ? 0.2255 0.2206 0.1984 -0.0242 0.0014  0.0121  139 ASP   C CB  
2100 C  CG  . ASP   B 133 ? 0.2597 0.2564 0.2415 -0.0215 0.0013  0.0123  139 ASP   C CG  
2101 O  OD1 . ASP   B 133 ? 0.2560 0.2541 0.2428 -0.0185 0.0021  0.0094  139 ASP   C OD1 
2102 O  OD2 . ASP   B 133 ? 0.2719 0.2678 0.2551 -0.0225 0.0001  0.0154  139 ASP   C OD2 
2103 N  N   . LEU   B 134 ? 0.2041 0.2022 0.1837 -0.0223 0.0116  0.0035  140 LEU   C N   
2104 C  CA  . LEU   B 134 ? 0.2159 0.2155 0.1993 -0.0230 0.0154  0.0024  140 LEU   C CA  
2105 C  C   . LEU   B 134 ? 0.2181 0.2181 0.1982 -0.0243 0.0202  -0.0012 140 LEU   C C   
2106 O  O   . LEU   B 134 ? 0.2206 0.2222 0.2066 -0.0220 0.0221  -0.0052 140 LEU   C O   
2107 C  CB  . LEU   B 134 ? 0.2125 0.2141 0.2062 -0.0196 0.0145  0.0009  140 LEU   C CB  
2108 C  CG  . LEU   B 134 ? 0.2269 0.2279 0.2239 -0.0179 0.0103  0.0035  140 LEU   C CG  
2109 C  CD1 . LEU   B 134 ? 0.2382 0.2404 0.2434 -0.0147 0.0094  0.0012  140 LEU   C CD1 
2110 C  CD2 . LEU   B 134 ? 0.2368 0.2367 0.2327 -0.0204 0.0096  0.0075  140 LEU   C CD2 
2111 N  N   . LEU   B 135 ? 0.2187 0.2165 0.1889 -0.0281 0.0219  -0.0001 141 LEU   C N   
2112 C  CA  . LEU   B 135 ? 0.2367 0.2341 0.2020 -0.0295 0.0269  -0.0042 141 LEU   C CA  
2113 C  C   . LEU   B 135 ? 0.2532 0.2538 0.2252 -0.0295 0.0326  -0.0070 141 LEU   C C   
2114 O  O   . LEU   B 135 ? 0.2760 0.2775 0.2496 -0.0286 0.0365  -0.0118 141 LEU   C O   
2115 C  CB  . LEU   B 135 ? 0.2407 0.2345 0.1923 -0.0339 0.0273  -0.0023 141 LEU   C CB  
2116 C  CG  . LEU   B 135 ? 0.2485 0.2395 0.1942 -0.0345 0.0210  0.0012  141 LEU   C CG  
2117 C  CD1 . LEU   B 135 ? 0.2643 0.2512 0.1957 -0.0392 0.0211  0.0026  141 LEU   C CD1 
2118 C  CD2 . LEU   B 135 ? 0.2550 0.2462 0.2046 -0.0311 0.0180  -0.0011 141 LEU   C CD2 
2119 N  N   . TRP   B 136 ? 0.2499 0.2521 0.2267 -0.0306 0.0331  -0.0043 142 TRP   C N   
2120 C  CA  . TRP   B 136 ? 0.2601 0.2659 0.2447 -0.0311 0.0385  -0.0065 142 TRP   C CA  
2121 C  C   . TRP   B 136 ? 0.2792 0.2885 0.2768 -0.0266 0.0383  -0.0107 142 TRP   C C   
2122 O  O   . TRP   B 136 ? 0.2942 0.3070 0.2996 -0.0267 0.0429  -0.0136 142 TRP   C O   
2123 C  CB  . TRP   B 136 ? 0.2646 0.2708 0.2517 -0.0335 0.0382  -0.0021 142 TRP   C CB  
2124 C  CG  . TRP   B 136 ? 0.2626 0.2681 0.2550 -0.0310 0.0317  0.0009  142 TRP   C CG  
2125 C  CD1 . TRP   B 136 ? 0.2730 0.2751 0.2597 -0.0315 0.0268  0.0052  142 TRP   C CD1 
2126 C  CD2 . TRP   B 136 ? 0.2559 0.2639 0.2606 -0.0276 0.0296  -0.0006 142 TRP   C CD2 
2127 N  NE1 . TRP   B 136 ? 0.2740 0.2766 0.2689 -0.0285 0.0225  0.0061  142 TRP   C NE1 
2128 C  CE2 . TRP   B 136 ? 0.2616 0.2675 0.2666 -0.0263 0.0241  0.0026  142 TRP   C CE2 
2129 C  CE3 . TRP   B 136 ? 0.2624 0.2742 0.2781 -0.0255 0.0317  -0.0045 142 TRP   C CE3 
2130 C  CZ2 . TRP   B 136 ? 0.2704 0.2772 0.2846 -0.0231 0.0208  0.0018  142 TRP   C CZ2 
2131 C  CZ3 . TRP   B 136 ? 0.2785 0.2913 0.3036 -0.0227 0.0277  -0.0047 142 TRP   C CZ3 
2132 C  CH2 . TRP   B 136 ? 0.2746 0.2846 0.2982 -0.0217 0.0226  -0.0016 142 TRP   C CH2 
2133 N  N   . LEU   B 137 ? 0.2739 0.2821 0.2739 -0.0230 0.0329  -0.0110 143 LEU   C N   
2134 C  CA  . LEU   B 137 ? 0.2807 0.2912 0.2917 -0.0189 0.0319  -0.0145 143 LEU   C CA  
2135 C  C   . LEU   B 137 ? 0.3312 0.3426 0.3440 -0.0182 0.0363  -0.0195 143 LEU   C C   
2136 O  O   . LEU   B 137 ? 0.3437 0.3581 0.3677 -0.0157 0.0371  -0.0226 143 LEU   C O   
2137 C  CB  . LEU   B 137 ? 0.2559 0.2641 0.2664 -0.0157 0.0258  -0.0137 143 LEU   C CB  
2138 C  CG  . LEU   B 137 ? 0.2546 0.2623 0.2669 -0.0151 0.0214  -0.0101 143 LEU   C CG  
2139 C  CD1 . LEU   B 137 ? 0.2529 0.2582 0.2629 -0.0125 0.0167  -0.0096 143 LEU   C CD1 
2140 C  CD2 . LEU   B 137 ? 0.2442 0.2547 0.2677 -0.0139 0.0212  -0.0111 143 LEU   C CD2 
2141 N  N   . ASP   B 138 ? 0.3733 0.3821 0.3754 -0.0202 0.0387  -0.0204 144 ASP   C N   
2142 C  CA  . ASP   B 138 ? 0.4280 0.4361 0.4285 -0.0199 0.0428  -0.0254 144 ASP   C CA  
2143 C  C   . ASP   B 138 ? 0.4651 0.4759 0.4669 -0.0223 0.0507  -0.0282 144 ASP   C C   
2144 O  O   . ASP   B 138 ? 0.4776 0.4882 0.4796 -0.0216 0.0548  -0.0331 144 ASP   C O   
2145 C  CB  . ASP   B 138 ? 0.4695 0.4728 0.4557 -0.0220 0.0418  -0.0247 144 ASP   C CB  
2146 C  CG  . ASP   B 138 ? 0.5385 0.5387 0.5225 -0.0199 0.0355  -0.0235 144 ASP   C CG  
2147 O  OD1 . ASP   B 138 ? 0.5497 0.5508 0.5425 -0.0162 0.0324  -0.0241 144 ASP   C OD1 
2148 O  OD2 . ASP   B 138 ? 0.5866 0.5832 0.5596 -0.0221 0.0336  -0.0217 144 ASP   C OD2 
2149 N  N   . GLU   B 139 ? 0.4780 0.4906 0.4786 -0.0257 0.0533  -0.0252 145 GLU   C N   
2150 C  CA  . GLU   B 139 ? 0.5045 0.5196 0.5047 -0.0289 0.0617  -0.0275 145 GLU   C CA  
2151 C  C   . GLU   B 139 ? 0.5132 0.5343 0.5286 -0.0285 0.0645  -0.0279 145 GLU   C C   
2152 O  O   . GLU   B 139 ? 0.5218 0.5440 0.5442 -0.0273 0.0596  -0.0248 145 GLU   C O   
2153 C  CB  . GLU   B 139 ? 0.5555 0.5670 0.5396 -0.0345 0.0637  -0.0238 145 GLU   C CB  
2154 C  CG  . GLU   B 139 ? 0.6448 0.6551 0.6268 -0.0361 0.0586  -0.0171 145 GLU   C CG  
2155 C  CD  . GLU   B 139 ? 0.7783 0.7831 0.7433 -0.0402 0.0564  -0.0127 145 GLU   C CD  
2156 O  OE1 . GLU   B 139 ? 0.8078 0.8118 0.7685 -0.0440 0.0571  -0.0081 145 GLU   C OE1 
2157 O  OE2 . GLU   B 139 ? 0.8178 0.8191 0.7744 -0.0396 0.0536  -0.0136 145 GLU   C OE2 
2158 N  N1  . A1B2J C .   ? 0.2368 0.2327 0.2793 -0.0069 0.0178  0.0172  201 A1B2J A N1  
2159 C  C4  . A1B2J C .   ? 0.2414 0.2329 0.2814 -0.0060 0.0176  0.0212  201 A1B2J A C4  
2160 C  C5  . A1B2J C .   ? 0.2486 0.2466 0.2856 -0.0057 0.0188  0.0172  201 A1B2J A C5  
2161 C  C6  . A1B2J C .   ? 0.2773 0.2721 0.3034 -0.0033 0.0194  0.0212  201 A1B2J A C6  
2162 C  C7  . A1B2J C .   ? 0.2974 0.2941 0.3188 -0.0019 0.0219  0.0213  201 A1B2J A C7  
2163 C  C8  . A1B2J C .   ? 0.3143 0.3116 0.3387 -0.0020 0.0273  0.0244  201 A1B2J A C8  
2164 C  C10 . A1B2J C .   ? 0.3296 0.3291 0.3422 0.0015  0.0275  0.0215  201 A1B2J A C10 
2165 C  C13 . A1B2J C .   ? 0.3487 0.3498 0.3590 0.0041  0.0371  0.0253  201 A1B2J A C13 
2166 C  C15 . A1B2J C .   ? 0.2213 0.2193 0.2723 -0.0089 0.0166  0.0125  201 A1B2J A C15 
2167 CL CL  . A1B2J C .   ? 0.3369 0.3338 0.3491 -0.0007 0.0138  0.0149  201 A1B2J A CL  
2168 C  C12 . A1B2J C .   ? 0.3154 0.3129 0.3297 -0.0004 0.0195  0.0186  201 A1B2J A C12 
2169 C  C11 . A1B2J C .   ? 0.3229 0.3214 0.3326 0.0013  0.0221  0.0186  201 A1B2J A C11 
2170 O  O2  . A1B2J C .   ? 0.3407 0.3419 0.3501 0.0035  0.0305  0.0212  201 A1B2J A O2  
2171 C  C14 . A1B2J C .   ? 0.3550 0.3577 0.3780 0.0012  0.0399  0.0276  201 A1B2J A C14 
2172 O  O3  . A1B2J C .   ? 0.3443 0.3435 0.3673 -0.0002 0.0365  0.0284  201 A1B2J A O3  
2173 C  C9  . A1B2J C .   ? 0.3251 0.3240 0.3452 -0.0003 0.0303  0.0247  201 A1B2J A C9  
2174 O  O1  . A1B2J C .   ? 0.2330 0.2349 0.2732 -0.0062 0.0188  0.0141  201 A1B2J A O1  
2175 C  C3  . A1B2J C .   ? 0.2421 0.2327 0.2822 -0.0058 0.0138  0.0190  201 A1B2J A C3  
2176 C  C2  . A1B2J C .   ? 0.2251 0.2174 0.2738 -0.0077 0.0134  0.0144  201 A1B2J A C2  
2177 C  C1  . A1B2J C .   ? 0.2118 0.2083 0.2606 -0.0084 0.0132  0.0104  201 A1B2J A C1  
2178 C  C   . A1B2J C .   ? 0.2147 0.2126 0.2702 -0.0099 0.0121  0.0054  201 A1B2J A C   
2179 O  O   . A1B2J C .   ? 0.2120 0.2096 0.2759 -0.0118 0.0137  0.0045  201 A1B2J A O   
2180 N  N   . A1B2J C .   ? 0.2029 0.2023 0.2542 -0.0092 0.0095  0.0020  201 A1B2J A N   
2190 N  N1  . A1B2J G .   ? 0.2526 0.2308 0.2498 0.0121  0.0030  -0.0217 201 A1B2J C N1  
2191 C  C4  . A1B2J G .   ? 0.2474 0.2208 0.2425 0.0125  -0.0003 -0.0246 201 A1B2J C C4  
2192 C  C5  . A1B2J G .   ? 0.2922 0.2711 0.2832 0.0116  0.0058  -0.0214 201 A1B2J C C5  
2193 C  C6  . A1B2J G .   ? 0.3475 0.3212 0.3267 0.0112  0.0052  -0.0238 201 A1B2J C C6  
2194 C  C7  . A1B2J G .   ? 0.4009 0.3750 0.3731 0.0106  0.0094  -0.0236 201 A1B2J C C7  
2195 C  C8  . A1B2J G .   ? 0.4325 0.4053 0.4020 0.0115  0.0140  -0.0268 201 A1B2J C C8  
2196 C  C10 . A1B2J G .   ? 0.4774 0.4514 0.4359 0.0084  0.0180  -0.0231 201 A1B2J C C10 
2197 C  C13 . A1B2J G .   ? 0.5143 0.4865 0.4612 0.0075  0.0280  -0.0264 201 A1B2J C C13 
2198 C  C15 . A1B2J G .   ? 0.2290 0.2113 0.2361 0.0120  0.0026  -0.0187 201 A1B2J C C15 
2199 CL CL  . A1B2J G .   ? 0.4557 0.4323 0.4278 0.0079  0.0045  -0.0173 201 A1B2J C CL  
2200 C  C12 . A1B2J G .   ? 0.4357 0.4107 0.4038 0.0089  0.0093  -0.0205 201 A1B2J C C12 
2201 C  C11 . A1B2J G .   ? 0.4555 0.4303 0.4169 0.0078  0.0132  -0.0201 201 A1B2J C C11 
2202 O  O2  . A1B2J G .   ? 0.5072 0.4811 0.4588 0.0069  0.0226  -0.0225 201 A1B2J C O2  
2203 C  C14 . A1B2J G .   ? 0.5077 0.4826 0.4656 0.0102  0.0297  -0.0295 201 A1B2J C C14 
2204 O  O3  . A1B2J G .   ? 0.4984 0.4707 0.4593 0.0115  0.0238  -0.0304 201 A1B2J C O3  
2205 C  C9  . A1B2J G .   ? 0.4711 0.4442 0.4339 0.0105  0.0186  -0.0267 201 A1B2J C C9  
2206 O  O1  . A1B2J G .   ? 0.2694 0.2525 0.2637 0.0113  0.0084  -0.0191 201 A1B2J C O1  
2207 C  C3  . A1B2J G .   ? 0.2270 0.2012 0.2260 0.0112  -0.0043 -0.0225 201 A1B2J C C3  
2208 C  C2  . A1B2J G .   ? 0.2111 0.1894 0.2196 0.0107  -0.0039 -0.0194 201 A1B2J C C2  
2209 C  C1  . A1B2J G .   ? 0.2035 0.1861 0.2127 0.0105  -0.0009 -0.0166 201 A1B2J C C1  
2210 C  C   . A1B2J G .   ? 0.1992 0.1850 0.2164 0.0098  -0.0012 -0.0133 201 A1B2J C C   
2211 O  O   . A1B2J G .   ? 0.1873 0.1726 0.2105 0.0108  -0.0012 -0.0135 201 A1B2J C O   
2212 N  N   . A1B2J G .   ? 0.2075 0.1961 0.2244 0.0081  -0.0016 -0.0103 201 A1B2J C N   
2213 C  C1  . GOL   H .   ? 0.4725 0.4398 0.4515 0.0097  -0.0100 -0.0240 202 GOL   C C1  
2214 O  O1  . GOL   H .   ? 0.4325 0.4003 0.4142 0.0090  -0.0140 -0.0228 202 GOL   C O1  
2215 C  C2  . GOL   H .   ? 0.5126 0.4738 0.4826 0.0102  -0.0108 -0.0277 202 GOL   C C2  
2216 O  O2  . GOL   H .   ? 0.5298 0.4877 0.5010 0.0101  -0.0161 -0.0297 202 GOL   C O2  
2217 C  C3  . GOL   H .   ? 0.5285 0.4894 0.4988 0.0113  -0.0064 -0.0301 202 GOL   C C3  
2218 O  O3  . GOL   H .   ? 0.5553 0.5101 0.5148 0.0116  -0.0062 -0.0339 202 GOL   C O3  
# 
