data_7I6Y
# 
_entry.id   7I6Y 
# 
_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   7I6Y         pdb_00007i6y 10.2210/pdb7i6y/pdb 
WWPDB D_1001408393 ?            ?                   
# 
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                        7I6Y 
_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-[(2-chloropyridin-3-yl)acetyl]piperidine-3-carboxamide' 281.738   2   ?         ? ? ? 
3 non-polymer syn 'ZINC ION'                                                      65.409    2   ?         ? ? ? 
4 non-polymer syn 'DIMETHYL SULFOXIDE'                                            78.133    3   ?         ? ? ? 
5 water       nat water                                                           18.015    335 ?         ? ? ? 
# 
_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-[(2-chloropyridin-3-yl)acetyl]piperidine-3-carboxamide' A1B5J 
3 'ZINC ION'                                                      ZN    
4 'DIMETHYL SULFOXIDE'                                            DMS   
5 water                                                           HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   GLY n 
1 3   ALA n 
1 4   ILE n 
1 5   TYR n 
1 6   VAL n 
1 7   GLY n 
1 8   ASN n 
1 9   TYR n 
1 10  ARG n 
1 11  VAL n 
1 12  VAL n 
1 13  ASN n 
1 14  ARG n 
1 15  HIS n 
1 16  LEU n 
1 17  ALA n 
1 18  THR n 
1 19  HIS n 
1 20  ASN n 
1 21  ASP n 
1 22  TRP n 
1 23  ALA n 
1 24  ASN n 
1 25  LEU n 
1 26  VAL n 
1 27  TRP n 
1 28  GLU n 
1 29  ASP n 
1 30  SER n 
1 31  SER n 
1 32  ARG n 
1 33  ASP n 
1 34  LEU n 
1 35  LEU n 
1 36  VAL n 
1 37  SER n 
1 38  SER n 
1 39  THR n 
1 40  THR n 
1 41  ALA n 
1 42  GLN n 
1 43  GLY n 
1 44  CYS n 
1 45  ASP n 
1 46  THR n 
1 47  ILE n 
1 48  ALA n 
1 49  ARG n 
1 50  CYS n 
1 51  ASP n 
1 52  CYS n 
1 53  GLN n 
1 54  THR n 
1 55  GLY n 
1 56  VAL n 
1 57  TYR n 
1 58  TYR n 
1 59  CYS n 
1 60  SER n 
1 61  SER n 
1 62  ARG n 
1 63  ARG n 
1 64  LYS n 
1 65  HIS n 
1 66  TYR n 
1 67  PRO n 
1 68  VAL n 
1 69  SER n 
1 70  PHE n 
1 71  SER n 
1 72  LYS n 
1 73  PRO n 
1 74  SER n 
1 75  LEU n 
1 76  ILE n 
1 77  PHE n 
1 78  VAL n 
1 79  GLU n 
1 80  ALA n 
1 81  SER n 
1 82  GLU n 
1 83  TYR n 
1 84  TYR n 
1 85  PRO n 
1 86  ALA n 
1 87  ARG n 
1 88  TYR n 
1 89  GLN n 
1 90  SER n 
1 91  HIS n 
1 92  LEU n 
1 93  MET n 
1 94  LEU n 
1 95  ALA n 
1 96  VAL n 
1 97  GLY n 
1 98  HIS n 
1 99  SER n 
1 100 GLU n 
1 101 PRO n 
1 102 GLY n 
1 103 ASP n 
1 104 CYS n 
1 105 GLY n 
1 106 GLY n 
1 107 ILE n 
1 108 LEU n 
1 109 ARG n 
1 110 CYS n 
1 111 GLN n 
1 112 HIS n 
1 113 GLY n 
1 114 VAL n 
1 115 VAL n 
1 116 GLY n 
1 117 ILE n 
1 118 VAL n 
1 119 SER n 
1 120 THR n 
1 121 GLY n 
1 122 GLY n 
1 123 ASN n 
1 124 GLY n 
1 125 LEU n 
1 126 VAL n 
1 127 GLY n 
1 128 PHE n 
1 129 ALA n 
1 130 ASP n 
1 131 VAL n 
1 132 ARG n 
1 133 ASP n 
1 134 LEU n 
1 135 LEU n 
1 136 TRP n 
1 137 LEU n 
1 138 ASP n 
1 139 GLU n 
1 140 GLU n 
1 141 ALA n 
1 142 MET n 
1 143 GLU n 
1 144 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   144 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Coxsackievirus A16' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     31704 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1B5J non-polymer         . '(3S)-1-[(2-chloropyridin-3-yl)acetyl]piperidine-3-carboxamide' ? 'C13 H16 Cl N3 O2' 281.738 
ALA   'L-peptide linking' y ALANINE                                                         ? 'C3 H7 N O2'       89.093  
ARG   'L-peptide linking' y ARGININE                                                        ? 'C6 H15 N4 O2 1'   175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                      ? 'C4 H8 N2 O3'      132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                 ? 'C4 H7 N O4'       133.103 
CYS   'L-peptide linking' y CYSTEINE                                                        ? 'C3 H7 N O2 S'     121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                            ? 'C2 H6 O S'        78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                       ? 'C5 H10 N2 O3'     146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                 ? 'C5 H9 N O4'       147.129 
GLY   'peptide linking'   y GLYCINE                                                         ? 'C2 H5 N O2'       75.067  
HIS   'L-peptide linking' y HISTIDINE                                                       ? 'C6 H10 N3 O2 1'   156.162 
HOH   non-polymer         . WATER                                                           ? 'H2 O'             18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                      ? 'C6 H13 N O2'      131.173 
LEU   'L-peptide linking' y LEUCINE                                                         ? 'C6 H13 N O2'      131.173 
LYS   'L-peptide linking' y LYSINE                                                          ? 'C6 H15 N2 O2 1'   147.195 
MET   'L-peptide linking' y METHIONINE                                                      ? 'C5 H11 N O2 S'    149.211 
PHE   'L-peptide linking' y PHENYLALANINE                                                   ? 'C9 H11 N O2'      165.189 
PRO   'L-peptide linking' y PROLINE                                                         ? 'C5 H9 N O2'       115.130 
SER   'L-peptide linking' y SERINE                                                          ? 'C3 H7 N O3'       105.093 
THR   'L-peptide linking' y THREONINE                                                       ? 'C4 H9 N O3'       119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                                                      ? 'C11 H12 N2 O2'    204.225 
TYR   'L-peptide linking' y TYROSINE                                                        ? 'C9 H11 N O3'      181.189 
VAL   'L-peptide linking' y VALINE                                                          ? 'C5 H11 N O2'      117.146 
ZN    non-polymer         . 'ZINC ION'                                                      ? 'Zn 2'             65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   SER 1   7   7   SER SER A . n 
A 1 2   GLY 2   8   8   GLY GLY A . n 
A 1 3   ALA 3   9   9   ALA ALA A . n 
A 1 4   ILE 4   10  10  ILE ILE A . n 
A 1 5   TYR 5   11  11  TYR TYR A . n 
A 1 6   VAL 6   12  12  VAL VAL A . n 
A 1 7   GLY 7   13  13  GLY GLY A . n 
A 1 8   ASN 8   14  14  ASN ASN A . n 
A 1 9   TYR 9   15  15  TYR TYR A . n 
A 1 10  ARG 10  16  16  ARG ARG A . n 
A 1 11  VAL 11  17  17  VAL VAL A . n 
A 1 12  VAL 12  18  18  VAL VAL A . n 
A 1 13  ASN 13  19  19  ASN ASN A . n 
A 1 14  ARG 14  20  20  ARG ARG A . n 
A 1 15  HIS 15  21  21  HIS HIS A . n 
A 1 16  LEU 16  22  22  LEU LEU A . n 
A 1 17  ALA 17  23  23  ALA ALA A . n 
A 1 18  THR 18  24  24  THR THR A . n 
A 1 19  HIS 19  25  25  HIS HIS A . n 
A 1 20  ASN 20  26  26  ASN ASN A . n 
A 1 21  ASP 21  27  27  ASP ASP A . n 
A 1 22  TRP 22  28  28  TRP TRP A . n 
A 1 23  ALA 23  29  29  ALA ALA A . n 
A 1 24  ASN 24  30  30  ASN ASN A . n 
A 1 25  LEU 25  31  31  LEU LEU A . n 
A 1 26  VAL 26  32  32  VAL VAL A . n 
A 1 27  TRP 27  33  33  TRP TRP A . n 
A 1 28  GLU 28  34  34  GLU GLU A . n 
A 1 29  ASP 29  35  35  ASP ASP A . n 
A 1 30  SER 30  36  36  SER SER A . n 
A 1 31  SER 31  37  37  SER SER A . n 
A 1 32  ARG 32  38  38  ARG ARG A . n 
A 1 33  ASP 33  39  39  ASP ASP A . n 
A 1 34  LEU 34  40  40  LEU LEU A . n 
A 1 35  LEU 35  41  41  LEU LEU A . n 
A 1 36  VAL 36  42  42  VAL VAL A . n 
A 1 37  SER 37  43  43  SER SER A . n 
A 1 38  SER 38  44  44  SER SER A . n 
A 1 39  THR 39  45  45  THR THR A . n 
A 1 40  THR 40  46  46  THR THR A . n 
A 1 41  ALA 41  47  47  ALA ALA A . n 
A 1 42  GLN 42  48  48  GLN GLN A . n 
A 1 43  GLY 43  49  49  GLY GLY A . n 
A 1 44  CYS 44  50  50  CYS CYS A . n 
A 1 45  ASP 45  51  51  ASP ASP A . n 
A 1 46  THR 46  52  52  THR THR A . n 
A 1 47  ILE 47  53  53  ILE ILE A . n 
A 1 48  ALA 48  54  54  ALA ALA A . n 
A 1 49  ARG 49  55  55  ARG ARG A . n 
A 1 50  CYS 50  56  56  CYS CYS A . n 
A 1 51  ASP 51  57  57  ASP ASP A . n 
A 1 52  CYS 52  58  58  CYS CYS A . n 
A 1 53  GLN 53  59  59  GLN GLN A . n 
A 1 54  THR 54  60  60  THR THR A . n 
A 1 55  GLY 55  61  61  GLY GLY A . n 
A 1 56  VAL 56  62  62  VAL VAL A . n 
A 1 57  TYR 57  63  63  TYR TYR A . n 
A 1 58  TYR 58  64  64  TYR TYR A . n 
A 1 59  CYS 59  65  65  CYS CYS A . n 
A 1 60  SER 60  66  66  SER SER A . n 
A 1 61  SER 61  67  67  SER SER A . n 
A 1 62  ARG 62  68  68  ARG ARG A . n 
A 1 63  ARG 63  69  69  ARG ARG A . n 
A 1 64  LYS 64  70  70  LYS LYS A . n 
A 1 65  HIS 65  71  71  HIS HIS A . n 
A 1 66  TYR 66  72  72  TYR TYR A . n 
A 1 67  PRO 67  73  73  PRO PRO A . n 
A 1 68  VAL 68  74  74  VAL VAL A . n 
A 1 69  SER 69  75  75  SER SER A . n 
A 1 70  PHE 70  76  76  PHE PHE A . n 
A 1 71  SER 71  77  77  SER SER A . n 
A 1 72  LYS 72  78  78  LYS LYS A . n 
A 1 73  PRO 73  79  79  PRO PRO A . n 
A 1 74  SER 74  80  80  SER SER A . n 
A 1 75  LEU 75  81  81  LEU LEU A . n 
A 1 76  ILE 76  82  82  ILE ILE A . n 
A 1 77  PHE 77  83  83  PHE PHE A . n 
A 1 78  VAL 78  84  84  VAL VAL A . n 
A 1 79  GLU 79  85  85  GLU GLU A . n 
A 1 80  ALA 80  86  86  ALA ALA A . n 
A 1 81  SER 81  87  87  SER SER A . n 
A 1 82  GLU 82  88  88  GLU GLU A . n 
A 1 83  TYR 83  89  89  TYR TYR A . n 
A 1 84  TYR 84  90  90  TYR TYR A . n 
A 1 85  PRO 85  91  91  PRO PRO A . n 
A 1 86  ALA 86  92  92  ALA ALA A . n 
A 1 87  ARG 87  93  93  ARG ARG A . n 
A 1 88  TYR 88  94  94  TYR TYR A . n 
A 1 89  GLN 89  95  95  GLN GLN A . n 
A 1 90  SER 90  96  96  SER SER A . n 
A 1 91  HIS 91  97  97  HIS HIS A . n 
A 1 92  LEU 92  98  98  LEU LEU A . n 
A 1 93  MET 93  99  99  MET MET A . n 
A 1 94  LEU 94  100 100 LEU LEU A . n 
A 1 95  ALA 95  101 101 ALA ALA A . n 
A 1 96  VAL 96  102 102 VAL VAL A . n 
A 1 97  GLY 97  103 103 GLY GLY A . n 
A 1 98  HIS 98  104 104 HIS HIS A . n 
A 1 99  SER 99  105 105 SER SER A . n 
A 1 100 GLU 100 106 106 GLU GLU A . n 
A 1 101 PRO 101 107 107 PRO PRO A . n 
A 1 102 GLY 102 108 108 GLY GLY A . n 
A 1 103 ASP 103 109 109 ASP ASP A . n 
A 1 104 CYS 104 110 110 CYS CYS A . n 
A 1 105 GLY 105 111 111 GLY GLY A . n 
A 1 106 GLY 106 112 112 GLY GLY A . n 
A 1 107 ILE 107 113 113 ILE ILE A . n 
A 1 108 LEU 108 114 114 LEU LEU A . n 
A 1 109 ARG 109 115 115 ARG ARG A . n 
A 1 110 CYS 110 116 116 CYS CYS A . n 
A 1 111 GLN 111 117 117 GLN GLN A . n 
A 1 112 HIS 112 118 118 HIS HIS A . n 
A 1 113 GLY 113 119 119 GLY GLY A . n 
A 1 114 VAL 114 120 120 VAL VAL A . n 
A 1 115 VAL 115 121 121 VAL VAL A . n 
A 1 116 GLY 116 122 122 GLY GLY A . n 
A 1 117 ILE 117 123 123 ILE ILE A . n 
A 1 118 VAL 118 124 124 VAL VAL A . n 
A 1 119 SER 119 125 125 SER SER A . n 
A 1 120 THR 120 126 126 THR THR A . n 
A 1 121 GLY 121 127 127 GLY GLY A . n 
A 1 122 GLY 122 128 128 GLY GLY A . n 
A 1 123 ASN 123 129 129 ASN ASN A . n 
A 1 124 GLY 124 130 130 GLY GLY A . n 
A 1 125 LEU 125 131 131 LEU LEU A . n 
A 1 126 VAL 126 132 132 VAL VAL A . n 
A 1 127 GLY 127 133 133 GLY GLY A . n 
A 1 128 PHE 128 134 134 PHE PHE A . n 
A 1 129 ALA 129 135 135 ALA ALA A . n 
A 1 130 ASP 130 136 136 ASP ASP A . n 
A 1 131 VAL 131 137 137 VAL VAL A . n 
A 1 132 ARG 132 138 138 ARG ARG A . n 
A 1 133 ASP 133 139 139 ASP ASP A . n 
A 1 134 LEU 134 140 140 LEU LEU A . n 
A 1 135 LEU 135 141 141 LEU LEU A . n 
A 1 136 TRP 136 142 142 TRP TRP A . n 
A 1 137 LEU 137 143 143 LEU LEU A . n 
A 1 138 ASP 138 144 144 ASP ASP A . n 
A 1 139 GLU 139 145 145 GLU GLU A . n 
A 1 140 GLU 140 146 ?   ?   ?   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        A1B5J 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1B5J 
_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 A1B5J 1   201 201 A1B5J LIG A . 
D 3 ZN    1   202 1   ZN    ZN  A . 
E 4 DMS   1   203 8   DMS   DMS A . 
F 2 A1B5J 1   201 201 A1B5J LIG C . 
G 4 DMS   1   202 7   DMS   DMS C . 
H 3 ZN    1   203 1   ZN    ZN  C . 
I 4 DMS   1   204 2   DMS   DMS C . 
J 5 HOH   1   301 95  HOH   HOH A . 
J 5 HOH   2   302 285 HOH   HOH A . 
J 5 HOH   3   303 247 HOH   HOH A . 
J 5 HOH   4   304 103 HOH   HOH A . 
J 5 HOH   5   305 61  HOH   HOH A . 
J 5 HOH   6   306 311 HOH   HOH A . 
J 5 HOH   7   307 295 HOH   HOH A . 
J 5 HOH   8   308 337 HOH   HOH A . 
J 5 HOH   9   309 279 HOH   HOH A . 
J 5 HOH   10  310 116 HOH   HOH A . 
J 5 HOH   11  311 146 HOH   HOH A . 
J 5 HOH   12  312 84  HOH   HOH A . 
J 5 HOH   13  313 225 HOH   HOH A . 
J 5 HOH   14  314 270 HOH   HOH A . 
J 5 HOH   15  315 93  HOH   HOH A . 
J 5 HOH   16  316 5   HOH   HOH A . 
J 5 HOH   17  317 303 HOH   HOH A . 
J 5 HOH   18  318 7   HOH   HOH A . 
J 5 HOH   19  319 72  HOH   HOH A . 
J 5 HOH   20  320 176 HOH   HOH A . 
J 5 HOH   21  321 171 HOH   HOH A . 
J 5 HOH   22  322 56  HOH   HOH A . 
J 5 HOH   23  323 159 HOH   HOH A . 
J 5 HOH   24  324 178 HOH   HOH A . 
J 5 HOH   25  325 63  HOH   HOH A . 
J 5 HOH   26  326 13  HOH   HOH A . 
J 5 HOH   27  327 160 HOH   HOH A . 
J 5 HOH   28  328 140 HOH   HOH A . 
J 5 HOH   29  329 6   HOH   HOH A . 
J 5 HOH   30  330 66  HOH   HOH A . 
J 5 HOH   31  331 228 HOH   HOH A . 
J 5 HOH   32  332 70  HOH   HOH A . 
J 5 HOH   33  333 308 HOH   HOH A . 
J 5 HOH   34  334 71  HOH   HOH A . 
J 5 HOH   35  335 14  HOH   HOH A . 
J 5 HOH   36  336 22  HOH   HOH A . 
J 5 HOH   37  337 230 HOH   HOH A . 
J 5 HOH   38  338 190 HOH   HOH A . 
J 5 HOH   39  339 48  HOH   HOH A . 
J 5 HOH   40  340 157 HOH   HOH A . 
J 5 HOH   41  341 22  HOH   HOH A . 
J 5 HOH   42  342 339 HOH   HOH A . 
J 5 HOH   43  343 85  HOH   HOH A . 
J 5 HOH   44  344 336 HOH   HOH A . 
J 5 HOH   45  345 63  HOH   HOH A . 
J 5 HOH   46  346 49  HOH   HOH A . 
J 5 HOH   47  347 99  HOH   HOH A . 
J 5 HOH   48  348 271 HOH   HOH A . 
J 5 HOH   49  349 59  HOH   HOH A . 
J 5 HOH   50  350 115 HOH   HOH A . 
J 5 HOH   51  351 62  HOH   HOH A . 
J 5 HOH   52  352 10  HOH   HOH A . 
J 5 HOH   53  353 287 HOH   HOH A . 
J 5 HOH   54  354 309 HOH   HOH A . 
J 5 HOH   55  355 88  HOH   HOH A . 
J 5 HOH   56  356 23  HOH   HOH A . 
J 5 HOH   57  357 128 HOH   HOH A . 
J 5 HOH   58  358 274 HOH   HOH A . 
J 5 HOH   59  359 66  HOH   HOH A . 
J 5 HOH   60  360 102 HOH   HOH A . 
J 5 HOH   61  361 254 HOH   HOH A . 
J 5 HOH   62  362 242 HOH   HOH A . 
J 5 HOH   63  363 299 HOH   HOH A . 
J 5 HOH   64  364 27  HOH   HOH A . 
J 5 HOH   65  365 26  HOH   HOH A . 
J 5 HOH   66  366 318 HOH   HOH A . 
J 5 HOH   67  367 332 HOH   HOH A . 
J 5 HOH   68  368 21  HOH   HOH A . 
J 5 HOH   69  369 241 HOH   HOH A . 
J 5 HOH   70  370 60  HOH   HOH A . 
J 5 HOH   71  371 333 HOH   HOH A . 
J 5 HOH   72  372 227 HOH   HOH A . 
J 5 HOH   73  373 329 HOH   HOH A . 
J 5 HOH   74  374 19  HOH   HOH A . 
J 5 HOH   75  375 288 HOH   HOH A . 
J 5 HOH   76  376 259 HOH   HOH A . 
J 5 HOH   77  377 75  HOH   HOH A . 
J 5 HOH   78  378 14  HOH   HOH A . 
J 5 HOH   79  379 53  HOH   HOH A . 
J 5 HOH   80  380 119 HOH   HOH A . 
J 5 HOH   81  381 115 HOH   HOH A . 
J 5 HOH   82  382 325 HOH   HOH A . 
J 5 HOH   83  383 235 HOH   HOH A . 
J 5 HOH   84  384 233 HOH   HOH A . 
J 5 HOH   85  385 35  HOH   HOH A . 
J 5 HOH   86  386 272 HOH   HOH A . 
J 5 HOH   87  387 327 HOH   HOH A . 
J 5 HOH   88  388 149 HOH   HOH A . 
J 5 HOH   89  389 89  HOH   HOH A . 
J 5 HOH   90  390 165 HOH   HOH A . 
J 5 HOH   91  391 293 HOH   HOH A . 
J 5 HOH   92  392 12  HOH   HOH A . 
J 5 HOH   93  393 197 HOH   HOH A . 
J 5 HOH   94  394 284 HOH   HOH A . 
J 5 HOH   95  395 91  HOH   HOH A . 
J 5 HOH   96  396 92  HOH   HOH A . 
J 5 HOH   97  397 312 HOH   HOH A . 
J 5 HOH   98  398 320 HOH   HOH A . 
J 5 HOH   99  399 96  HOH   HOH A . 
J 5 HOH   100 400 263 HOH   HOH A . 
J 5 HOH   101 401 40  HOH   HOH A . 
J 5 HOH   102 402 148 HOH   HOH A . 
J 5 HOH   103 403 101 HOH   HOH A . 
J 5 HOH   104 404 252 HOH   HOH A . 
J 5 HOH   105 405 73  HOH   HOH A . 
J 5 HOH   106 406 26  HOH   HOH A . 
J 5 HOH   107 407 251 HOH   HOH A . 
J 5 HOH   108 408 250 HOH   HOH A . 
J 5 HOH   109 409 319 HOH   HOH A . 
J 5 HOH   110 410 315 HOH   HOH A . 
J 5 HOH   111 411 307 HOH   HOH A . 
J 5 HOH   112 412 49  HOH   HOH A . 
J 5 HOH   113 413 265 HOH   HOH A . 
J 5 HOH   114 414 300 HOH   HOH A . 
J 5 HOH   115 415 85  HOH   HOH A . 
J 5 HOH   116 416 112 HOH   HOH A . 
J 5 HOH   117 417 113 HOH   HOH A . 
J 5 HOH   118 418 19  HOH   HOH A . 
J 5 HOH   119 419 35  HOH   HOH A . 
J 5 HOH   120 420 12  HOH   HOH A . 
J 5 HOH   121 421 127 HOH   HOH A . 
J 5 HOH   122 422 102 HOH   HOH A . 
J 5 HOH   123 423 16  HOH   HOH A . 
J 5 HOH   124 424 283 HOH   HOH A . 
J 5 HOH   125 425 323 HOH   HOH A . 
J 5 HOH   126 426 331 HOH   HOH A . 
J 5 HOH   127 427 231 HOH   HOH A . 
J 5 HOH   128 428 202 HOH   HOH A . 
J 5 HOH   129 429 52  HOH   HOH A . 
J 5 HOH   130 430 38  HOH   HOH A . 
J 5 HOH   131 431 100 HOH   HOH A . 
J 5 HOH   132 432 208 HOH   HOH A . 
J 5 HOH   133 433 297 HOH   HOH A . 
J 5 HOH   134 434 114 HOH   HOH A . 
J 5 HOH   135 435 155 HOH   HOH A . 
J 5 HOH   136 436 15  HOH   HOH A . 
J 5 HOH   137 437 157 HOH   HOH A . 
J 5 HOH   138 438 294 HOH   HOH A . 
J 5 HOH   139 439 104 HOH   HOH A . 
J 5 HOH   140 440 126 HOH   HOH A . 
J 5 HOH   141 441 194 HOH   HOH A . 
J 5 HOH   142 442 129 HOH   HOH A . 
J 5 HOH   143 443 201 HOH   HOH A . 
J 5 HOH   144 444 24  HOH   HOH A . 
J 5 HOH   145 445 177 HOH   HOH A . 
J 5 HOH   146 446 291 HOH   HOH A . 
J 5 HOH   147 447 154 HOH   HOH A . 
J 5 HOH   148 448 156 HOH   HOH A . 
J 5 HOH   149 449 136 HOH   HOH A . 
J 5 HOH   150 450 150 HOH   HOH A . 
J 5 HOH   151 451 253 HOH   HOH A . 
J 5 HOH   152 452 168 HOH   HOH A . 
J 5 HOH   153 453 101 HOH   HOH A . 
J 5 HOH   154 454 82  HOH   HOH A . 
J 5 HOH   155 455 221 HOH   HOH A . 
J 5 HOH   156 456 138 HOH   HOH A . 
J 5 HOH   157 457 154 HOH   HOH A . 
J 5 HOH   158 458 32  HOH   HOH A . 
J 5 HOH   159 459 99  HOH   HOH A . 
J 5 HOH   160 460 187 HOH   HOH A . 
J 5 HOH   161 461 163 HOH   HOH A . 
J 5 HOH   162 462 317 HOH   HOH A . 
J 5 HOH   163 463 269 HOH   HOH A . 
J 5 HOH   164 464 164 HOH   HOH A . 
K 5 HOH   1   301 8   HOH   HOH C . 
K 5 HOH   2   302 64  HOH   HOH C . 
K 5 HOH   3   303 306 HOH   HOH C . 
K 5 HOH   4   304 137 HOH   HOH C . 
K 5 HOH   5   305 103 HOH   HOH C . 
K 5 HOH   6   306 33  HOH   HOH C . 
K 5 HOH   7   307 174 HOH   HOH C . 
K 5 HOH   8   308 249 HOH   HOH C . 
K 5 HOH   9   309 278 HOH   HOH C . 
K 5 HOH   10  310 65  HOH   HOH C . 
K 5 HOH   11  311 98  HOH   HOH C . 
K 5 HOH   12  312 2   HOH   HOH C . 
K 5 HOH   13  313 28  HOH   HOH C . 
K 5 HOH   14  314 155 HOH   HOH C . 
K 5 HOH   15  315 51  HOH   HOH C . 
K 5 HOH   16  316 124 HOH   HOH C . 
K 5 HOH   17  317 50  HOH   HOH C . 
K 5 HOH   18  318 261 HOH   HOH C . 
K 5 HOH   19  319 298 HOH   HOH C . 
K 5 HOH   20  320 130 HOH   HOH C . 
K 5 HOH   21  321 123 HOH   HOH C . 
K 5 HOH   22  322 223 HOH   HOH C . 
K 5 HOH   23  323 310 HOH   HOH C . 
K 5 HOH   24  324 91  HOH   HOH C . 
K 5 HOH   25  325 43  HOH   HOH C . 
K 5 HOH   26  326 276 HOH   HOH C . 
K 5 HOH   27  327 80  HOH   HOH C . 
K 5 HOH   28  328 122 HOH   HOH C . 
K 5 HOH   29  329 69  HOH   HOH C . 
K 5 HOH   30  330 226 HOH   HOH C . 
K 5 HOH   31  331 243 HOH   HOH C . 
K 5 HOH   32  332 280 HOH   HOH C . 
K 5 HOH   33  333 109 HOH   HOH C . 
K 5 HOH   34  334 260 HOH   HOH C . 
K 5 HOH   35  335 313 HOH   HOH C . 
K 5 HOH   36  336 1   HOH   HOH C . 
K 5 HOH   37  337 224 HOH   HOH C . 
K 5 HOH   38  338 39  HOH   HOH C . 
K 5 HOH   39  339 111 HOH   HOH C . 
K 5 HOH   40  340 314 HOH   HOH C . 
K 5 HOH   41  341 20  HOH   HOH C . 
K 5 HOH   42  342 64  HOH   HOH C . 
K 5 HOH   43  343 262 HOH   HOH C . 
K 5 HOH   44  344 289 HOH   HOH C . 
K 5 HOH   45  345 292 HOH   HOH C . 
K 5 HOH   46  346 97  HOH   HOH C . 
K 5 HOH   47  347 244 HOH   HOH C . 
K 5 HOH   48  348 245 HOH   HOH C . 
K 5 HOH   49  349 31  HOH   HOH C . 
K 5 HOH   50  350 78  HOH   HOH C . 
K 5 HOH   51  351 54  HOH   HOH C . 
K 5 HOH   52  352 30  HOH   HOH C . 
K 5 HOH   53  353 70  HOH   HOH C . 
K 5 HOH   54  354 41  HOH   HOH C . 
K 5 HOH   55  355 110 HOH   HOH C . 
K 5 HOH   56  356 67  HOH   HOH C . 
K 5 HOH   57  357 204 HOH   HOH C . 
K 5 HOH   58  358 205 HOH   HOH C . 
K 5 HOH   59  359 38  HOH   HOH C . 
K 5 HOH   60  360 290 HOH   HOH C . 
K 5 HOH   61  361 302 HOH   HOH C . 
K 5 HOH   62  362 322 HOH   HOH C . 
K 5 HOH   63  363 240 HOH   HOH C . 
K 5 HOH   64  364 296 HOH   HOH C . 
K 5 HOH   65  365 237 HOH   HOH C . 
K 5 HOH   66  366 304 HOH   HOH C . 
K 5 HOH   67  367 338 HOH   HOH C . 
K 5 HOH   68  368 71  HOH   HOH C . 
K 5 HOH   69  369 334 HOH   HOH C . 
K 5 HOH   70  370 4   HOH   HOH C . 
K 5 HOH   71  371 29  HOH   HOH C . 
K 5 HOH   72  372 324 HOH   HOH C . 
K 5 HOH   73  373 139 HOH   HOH C . 
K 5 HOH   74  374 40  HOH   HOH C . 
K 5 HOH   75  375 78  HOH   HOH C . 
K 5 HOH   76  376 118 HOH   HOH C . 
K 5 HOH   77  377 37  HOH   HOH C . 
K 5 HOH   78  378 239 HOH   HOH C . 
K 5 HOH   79  379 7   HOH   HOH C . 
K 5 HOH   80  380 79  HOH   HOH C . 
K 5 HOH   81  381 248 HOH   HOH C . 
K 5 HOH   82  382 48  HOH   HOH C . 
K 5 HOH   83  383 286 HOH   HOH C . 
K 5 HOH   84  384 275 HOH   HOH C . 
K 5 HOH   85  385 273 HOH   HOH C . 
K 5 HOH   86  386 83  HOH   HOH C . 
K 5 HOH   87  387 37  HOH   HOH C . 
K 5 HOH   88  388 146 HOH   HOH C . 
K 5 HOH   89  389 87  HOH   HOH C . 
K 5 HOH   90  390 124 HOH   HOH C . 
K 5 HOH   91  391 232 HOH   HOH C . 
K 5 HOH   92  392 256 HOH   HOH C . 
K 5 HOH   93  393 282 HOH   HOH C . 
K 5 HOH   94  394 13  HOH   HOH C . 
K 5 HOH   95  395 62  HOH   HOH C . 
K 5 HOH   96  396 68  HOH   HOH C . 
K 5 HOH   97  397 267 HOH   HOH C . 
K 5 HOH   98  398 3   HOH   HOH C . 
K 5 HOH   99  399 41  HOH   HOH C . 
K 5 HOH   100 400 43  HOH   HOH C . 
K 5 HOH   101 401 31  HOH   HOH C . 
K 5 HOH   102 402 11  HOH   HOH C . 
K 5 HOH   103 403 50  HOH   HOH C . 
K 5 HOH   104 404 147 HOH   HOH C . 
K 5 HOH   105 405 148 HOH   HOH C . 
K 5 HOH   106 406 340 HOH   HOH C . 
K 5 HOH   107 407 16  HOH   HOH C . 
K 5 HOH   108 408 108 HOH   HOH C . 
K 5 HOH   109 409 266 HOH   HOH C . 
K 5 HOH   110 410 258 HOH   HOH C . 
K 5 HOH   111 411 236 HOH   HOH C . 
K 5 HOH   112 412 169 HOH   HOH C . 
K 5 HOH   113 413 44  HOH   HOH C . 
K 5 HOH   114 414 45  HOH   HOH C . 
K 5 HOH   115 415 47  HOH   HOH C . 
K 5 HOH   116 416 120 HOH   HOH C . 
K 5 HOH   117 417 54  HOH   HOH C . 
K 5 HOH   118 418 268 HOH   HOH C . 
K 5 HOH   119 419 167 HOH   HOH C . 
K 5 HOH   120 420 153 HOH   HOH C . 
K 5 HOH   121 421 90  HOH   HOH C . 
K 5 HOH   122 422 117 HOH   HOH C . 
K 5 HOH   123 423 142 HOH   HOH C . 
K 5 HOH   124 424 234 HOH   HOH C . 
K 5 HOH   125 425 52  HOH   HOH C . 
K 5 HOH   126 426 83  HOH   HOH C . 
K 5 HOH   127 427 132 HOH   HOH C . 
K 5 HOH   128 428 17  HOH   HOH C . 
K 5 HOH   129 429 95  HOH   HOH C . 
K 5 HOH   130 430 264 HOH   HOH C . 
K 5 HOH   131 431 257 HOH   HOH C . 
K 5 HOH   132 432 116 HOH   HOH C . 
K 5 HOH   133 433 151 HOH   HOH C . 
K 5 HOH   134 434 135 HOH   HOH C . 
K 5 HOH   135 435 107 HOH   HOH C . 
K 5 HOH   136 436 321 HOH   HOH C . 
K 5 HOH   137 437 140 HOH   HOH C . 
K 5 HOH   138 438 162 HOH   HOH C . 
K 5 HOH   139 439 81  HOH   HOH C . 
K 5 HOH   140 440 167 HOH   HOH C . 
K 5 HOH   141 441 141 HOH   HOH C . 
K 5 HOH   142 442 139 HOH   HOH C . 
K 5 HOH   143 443 335 HOH   HOH C . 
K 5 HOH   144 444 161 HOH   HOH C . 
K 5 HOH   145 445 281 HOH   HOH C . 
K 5 HOH   146 446 152 HOH   HOH C . 
K 5 HOH   147 447 166 HOH   HOH C . 
K 5 HOH   148 448 185 HOH   HOH C . 
K 5 HOH   149 449 277 HOH   HOH C . 
K 5 HOH   150 450 27  HOH   HOH C . 
K 5 HOH   151 451 143 HOH   HOH C . 
K 5 HOH   152 452 93  HOH   HOH C . 
K 5 HOH   153 453 198 HOH   HOH C . 
K 5 HOH   154 454 301 HOH   HOH C . 
K 5 HOH   155 455 9   HOH   HOH C . 
K 5 HOH   156 456 326 HOH   HOH C . 
K 5 HOH   157 457 153 HOH   HOH C . 
K 5 HOH   158 458 158 HOH   HOH C . 
K 5 HOH   159 459 61  HOH   HOH C . 
K 5 HOH   160 460 199 HOH   HOH C . 
K 5 HOH   161 461 132 HOH   HOH C . 
K 5 HOH   162 462 145 HOH   HOH C . 
K 5 HOH   163 463 170 HOH   HOH C . 
K 5 HOH   164 464 123 HOH   HOH C . 
K 5 HOH   165 465 222 HOH   HOH C . 
K 5 HOH   166 466 189 HOH   HOH C . 
K 5 HOH   167 467 144 HOH   HOH C . 
K 5 HOH   168 468 141 HOH   HOH C . 
K 5 HOH   169 469 218 HOH   HOH C . 
K 5 HOH   170 470 203 HOH   HOH C . 
K 5 HOH   171 471 149 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           7I6Y 
_cell.length_a           72.718 
_cell.length_b           61.401 
_cell.length_c           65.205 
_cell.angle_alpha        90.00 
_cell.angle_beta         92.30 
_cell.angle_gamma        90.00 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7I6Y 
_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          7I6Y 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.29 
_exptl_crystal.density_percent_sol   46.24 
_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   2025-02-10 
_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   0.92205 
_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        0.92205 
_diffrn_source.pdbx_synchrotron_site       Diamond 
_diffrn_source.pdbx_synchrotron_beamline   I04-1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7I6Y 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.d_resolution_low             65.15 
_reflns.d_resolution_high            1.48 
_reflns.number_obs                   47984 
_reflns.percent_possible_obs         100.0 
_reflns.pdbx_Rmerge_I_obs            0.122 
_reflns.pdbx_netI_over_sigmaI        7.9 
_reflns.pdbx_redundancy              5.7 
_reflns.pdbx_Rrim_I_all              0.135 
_reflns.pdbx_Rpim_I_all              0.056 
_reflns.pdbx_CC_half                 0.998 
_reflns.pdbx_number_measured_all     273489 
_reflns.pdbx_chi_squared             0.75 
_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                  1.48 
_reflns_shell.d_res_low                   1.56 
_reflns_shell.number_measured_all         31384 
_reflns_shell.number_unique_obs           6948 
_reflns_shell.Rmerge_I_obs                1.579 
_reflns_shell.pdbx_chi_squared            0.60 
_reflns_shell.pdbx_redundancy             4.5 
_reflns_shell.percent_possible_obs        99.9 
_reflns_shell.pdbx_netI_over_sigmaI_obs   0.9 
_reflns_shell.pdbx_Rrim_I_all             1.790 
_reflns_shell.pdbx_Rpim_I_all             0.832 
_reflns_shell.pdbx_CC_half                0.369 
_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                                 7I6Y 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     47754 
_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                             65.15 
_refine.ls_d_res_high                            1.478 
_refine.ls_percent_reflns_obs                    99.4 
_refine.ls_R_factor_obs                          0.1939 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1924 
_refine.ls_R_factor_R_free                       0.2239 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 4.930 
_refine.ls_number_reflns_R_free                  2355 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.958 
_refine.correlation_coeff_Fo_to_Fc_free          0.948 
_refine.B_iso_mean                               20.30 
_refine.aniso_B[1][1]                            -1.45910 
_refine.aniso_B[2][2]                            2.04880 
_refine.aniso_B[3][3]                            -0.58970 
_refine.aniso_B[1][2]                            0.00000 
_refine.aniso_B[1][3]                            -0.09050 
_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             0.074 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   0.076 
_refine.pdbx_overall_SU_R_Blow_DPI               0.078 
_refine.pdbx_overall_SU_R_free_Blow_DPI          0.080 
# 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
_refine_analyze.entry_id                        7I6Y 
_refine_analyze.Luzzati_coordinate_error_obs    0.20 
_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         52 
_refine_hist.number_atoms_solvent             335 
_refine_hist.number_atoms_total               2535 
_refine_hist.d_res_high                       1.478 
_refine_hist.d_res_low                        65.15 
# 
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  2257 'X-RAY DIFFRACTION' HARMONIC     
t_angle_deg               0.98  ? 2.00  3069 'X-RAY DIFFRACTION' HARMONIC     
t_dihedral_angle_d        ?     ? 2.00  752  '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  406  'X-RAY DIFFRACTION' HARMONIC     
t_it                      ?     ? 10.00 2257 'X-RAY DIFFRACTION' HARMONIC     
t_nbd                     ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_omega_torsion           4.33  ? ?     ?    'X-RAY DIFFRACTION' ?            
t_other_torsion           14.01 ? ?     ?    'X-RAY DIFFRACTION' ?            
t_improper_torsion        ?     ? ?     ?    'X-RAY DIFFRACTION' ?            
t_chiral_improper_torsion ?     ? 5.00  276  '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  2072 '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                       1.48 
_refine_ls_shell.d_res_low                        1.49 
_refine_ls_shell.number_reflns_R_work             916 
_refine_ls_shell.R_factor_R_work                  0.3221 
_refine_ls_shell.percent_reflns_obs               91.71 
_refine_ls_shell.R_factor_R_free                  0.3499 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            4.18 
_refine_ls_shell.number_reflns_R_free             40 
_refine_ls_shell.number_reflns_all                956 
_refine_ls_shell.R_factor_all                     0.3233 
# 
_struct.entry_id                  7I6Y 
_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-0037793-001 (A71EV2A-x5079)
;
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7I6Y 
_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 2 ? 
G N N 4 ? 
H N N 3 ? 
I N N 4 ? 
J N N 5 ? 
K N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    POLG_CX16G 
_struct_ref.pdbx_db_accession          Q65900 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SGAIYVGNYRVVNRHLATHNDWANLVWEDSSRDLLVSSTTAQGCDTIARCDCQTGVYYCSSRRKHYPVSFSKPSLIFVEA
SEYYPARYQSHLMLAVGHSEPGDCGGILRCQHGVVGIVSTGGNGLVGFADVRDLLWLDEEAMEQ
;
_struct_ref.pdbx_align_begin           869 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 7I6Y A 1 ? 144 ? Q65900 869 ? 1012 ? 7 150 
2 1 7I6Y 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,J   
2 1 B,F,G,H,I,K 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 HIS A 15  ? ALA A 17  ? HIS A 21  ALA A 23  5 ? 3 
HELX_P HELX_P2  AA2 THR A 18  ? ASN A 24  ? THR A 24  ASN A 30  1 ? 7 
HELX_P HELX_P3  AA3 SER A 30  ? ARG A 32  ? SER A 36  ARG A 38  5 ? 3 
HELX_P HELX_P4  AA4 SER A 60  ? ARG A 63  ? SER A 66  ARG A 69  5 ? 4 
HELX_P HELX_P5  AA5 GLU A 100 ? CYS A 104 ? GLU A 106 CYS A 110 5 ? 5 
HELX_P HELX_P6  AA6 LEU A 134 ? GLU A 139 ? LEU A 140 GLU A 145 5 ? 6 
HELX_P HELX_P7  AA7 HIS B 15  ? ALA B 17  ? HIS C 21  ALA C 23  5 ? 3 
HELX_P HELX_P8  AA8 THR B 18  ? ASN B 24  ? THR C 24  ASN C 30  1 ? 7 
HELX_P HELX_P9  AA9 SER B 30  ? ARG B 32  ? SER C 36  ARG C 38  5 ? 3 
HELX_P HELX_P10 AB1 SER B 60  ? ARG B 63  ? SER C 66  ARG C 69  5 ? 4 
HELX_P HELX_P11 AB2 GLU B 100 ? CYS B 104 ? GLU C 106 CYS C 110 5 ? 5 
HELX_P HELX_P12 AB3 LEU B 134 ? GLU B 139 ? LEU C 140 GLU C 145 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 50  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 56  A ZN 202 1_555 ? ? ? ? ? ? ? 2.373 ? ? 
metalc2 metalc ? ? A CYS 52  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 58  A ZN 202 1_555 ? ? ? ? ? ? ? 2.379 ? ? 
metalc3 metalc ? ? A CYS 110 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 116 A ZN 202 1_555 ? ? ? ? ? ? ? 2.323 ? ? 
metalc4 metalc ? ? A HIS 112 ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 118 A ZN 202 1_555 ? ? ? ? ? ? ? 2.081 ? ? 
metalc5 metalc ? ? B CYS 50  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 56  C ZN 203 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc6 metalc ? ? B CYS 52  SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 58  C ZN 203 1_555 ? ? ? ? ? ? ? 2.360 ? ? 
metalc7 metalc ? ? B CYS 110 SG  ? ? ? 1_555 H ZN . ZN ? ? C CYS 116 C ZN 203 1_555 ? ? ? ? ? ? ? 2.327 ? ? 
metalc8 metalc ? ? B HIS 112 ND1 ? ? ? 1_555 H ZN . ZN ? ? C HIS 118 C ZN 203 1_555 ? ? ? ? ? ? ? 2.119 ? ? 
# 
_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_555 108.8 ? 
2  SG ? A CYS 50  ? A CYS 56  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 SG  ? A CYS 110 ? A CYS 116 ? 1_555 106.1 ? 
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_555 115.3 ? 
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_555 108.7 ? 
5  SG ? A CYS 52  ? A CYS 58  ? 1_555 ZN ? D ZN . ? A ZN 202 ? 1_555 ND1 ? A HIS 112 ? A HIS 118 ? 1_555 103.9 ? 
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_555 113.9 ? 
7  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 52  ? C CYS 58  ? 1_555 108.3 ? 
8  SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 106.2 ? 
9  SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 SG  ? B CYS 110 ? C CYS 116 ? 1_555 117.6 ? 
10 SG ? B CYS 50  ? C CYS 56  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 107.8 ? 
11 SG ? B CYS 52  ? C CYS 58  ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 100.6 ? 
12 SG ? B CYS 110 ? C CYS 116 ? 1_555 ZN ? H ZN . ? C ZN 203 ? 1_555 ND1 ? B HIS 112 ? C HIS 118 ? 1_555 115.9 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 3 ? 
AA2 ? 7 ? 
AA3 ? 3 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 LEU A 25  ? ASP A 29  ? LEU A 31  ASP A 35  
AA1 2 LEU A 34  ? CYS A 44  ? LEU A 40  CYS A 50  
AA1 3 ILE A 4   ? ASN A 13  ? ILE A 10  ASN A 19  
AA2 1 LYS A 64  ? SER A 69  ? LYS A 70  SER A 75  
AA2 2 THR A 54  ? CYS A 59  ? THR A 60  CYS A 65  
AA2 3 ILE A 107 ? CYS A 110 ? ILE A 113 CYS A 116 
AA2 4 GLY A 113 ? GLY A 122 ? GLY A 119 GLY A 128 
AA2 5 LEU A 125 ? ASP A 130 ? LEU A 131 ASP A 136 
AA2 6 ARG A 87  ? VAL A 96  ? ARG A 93  VAL A 102 
AA2 7 SER A 74  ? VAL A 78  ? SER A 80  VAL A 84  
AA3 1 LEU B 25  ? ASP B 29  ? LEU C 31  ASP C 35  
AA3 2 LEU B 34  ? CYS B 44  ? LEU C 40  CYS C 50  
AA3 3 ILE B 4   ? ASN B 13  ? ILE C 10  ASN C 19  
AA4 1 LYS B 64  ? SER B 69  ? LYS C 70  SER C 75  
AA4 2 THR B 54  ? CYS B 59  ? THR C 60  CYS C 65  
AA4 3 ILE B 107 ? CYS B 110 ? ILE C 113 CYS C 116 
AA4 4 GLY B 113 ? GLY B 122 ? GLY C 119 GLY C 128 
AA4 5 LEU B 125 ? ASP B 130 ? LEU C 131 ASP C 136 
AA4 6 ARG B 87  ? VAL B 96  ? ARG C 93  VAL C 102 
AA4 7 SER B 74  ? VAL B 78  ? SER C 80  VAL C 84  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N TRP A 27  ? N TRP A 33  O VAL A 36  ? O VAL A 42  
AA1 2 3 N LEU A 35  ? N LEU A 41  O VAL A 12  ? O VAL A 18  
AA2 1 2 O LYS A 64  ? O LYS A 70  N CYS A 59  ? N CYS A 65  
AA2 2 3 N VAL A 56  ? N VAL A 62  O ARG A 109 ? O ARG A 115 
AA2 3 4 N LEU A 108 ? N LEU A 114 O VAL A 115 ? O VAL A 121 
AA2 4 5 N SER A 119 ? N SER A 125 O GLY A 127 ? O GLY A 133 
AA2 5 6 O PHE A 128 ? O PHE A 134 N MET A 93  ? N MET A 99  
AA2 6 7 O 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 GLY B 43  ? N GLY C 49  O GLY B 7   ? O GLY C 13  
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 GLN B 89  ? O GLN C 95  N ILE B 76  ? N ILE C 82  
# 
_pdbx_entry_details.entry_id                   7I6Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 366 ? ? O A HOH 386 ? ? 2.03 
2 1 O A HOH 333 ? ? O A HOH 369 ? ? 2.18 
3 1 O A HOH 366 ? ? O A HOH 387 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 14  ? ? -99.92  35.96  
2 1 ASP A 144 ? ? -140.41 34.93  
3 1 SER C 125 ? ? -132.52 -30.52 
# 
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 19.7884 6.7153   18.3377 -0.0260 -0.0100 -0.0175 0.0005  -0.0016 0.0019  0.7914 1.3648 0.4257 
-0.5618 -0.1509 0.2313 -0.0144 0.0020 0.0951 0.0217 0.0337 0.0433  0.0406  0.0313  -0.0193 
'X-RAY DIFFRACTION' 2 ? refined 15.4047 -23.8567 14.1658 -0.0138 -0.0039 -0.0209 -0.0007 -0.0131 -0.0046 0.6826 0.9658 0.3373 
0.4292  0.1031  0.0576 -0.0272 0.0269 0.0382 0.0143 0.0315 -0.0335 -0.0181 -0.0245 -0.0044 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '{ A|* }' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '{ C|* }' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A 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 
A1B5J N1   N  N N 1   
A1B5J C4   C  N N 2   
A1B5J C5   C  N N 3   
A1B5J C6   C  N N 4   
A1B5J C7   C  Y N 5   
A1B5J C8   C  Y N 6   
A1B5J C10  C  Y N 7   
A1B5J CL   CL N N 8   
A1B5J C11  C  Y N 9   
A1B5J N2   N  Y N 10  
A1B5J C9   C  Y N 11  
A1B5J O1   O  N N 12  
A1B5J C3   C  N N 13  
A1B5J C2   C  N N 14  
A1B5J C12  C  N N 15  
A1B5J C1   C  N S 16  
A1B5J C    C  N N 17  
A1B5J O    O  N N 18  
A1B5J N    N  N N 19  
A1B5J H8   H  N N 20  
A1B5J H7   H  N N 21  
A1B5J H10  H  N N 22  
A1B5J H9   H  N N 23  
A1B5J H11  H  N N 24  
A1B5J H13  H  N N 25  
A1B5J H12  H  N N 26  
A1B5J H6   H  N N 27  
A1B5J H5   H  N N 28  
A1B5J H4   H  N N 29  
A1B5J H3   H  N N 30  
A1B5J H15  H  N N 31  
A1B5J H14  H  N N 32  
A1B5J H    H  N N 33  
A1B5J H2   H  N N 34  
A1B5J H1   H  N N 35  
ALA   N    N  N N 36  
ALA   CA   C  N S 37  
ALA   C    C  N N 38  
ALA   O    O  N N 39  
ALA   CB   C  N N 40  
ALA   OXT  O  N N 41  
ALA   H    H  N N 42  
ALA   H2   H  N N 43  
ALA   HA   H  N N 44  
ALA   HB1  H  N N 45  
ALA   HB2  H  N N 46  
ALA   HB3  H  N N 47  
ALA   HXT  H  N N 48  
ARG   N    N  N N 49  
ARG   CA   C  N S 50  
ARG   C    C  N N 51  
ARG   O    O  N N 52  
ARG   CB   C  N N 53  
ARG   CG   C  N N 54  
ARG   CD   C  N N 55  
ARG   NE   N  N N 56  
ARG   CZ   C  N N 57  
ARG   NH1  N  N N 58  
ARG   NH2  N  N N 59  
ARG   OXT  O  N N 60  
ARG   H    H  N N 61  
ARG   H2   H  N N 62  
ARG   HA   H  N N 63  
ARG   HB2  H  N N 64  
ARG   HB3  H  N N 65  
ARG   HG2  H  N N 66  
ARG   HG3  H  N N 67  
ARG   HD2  H  N N 68  
ARG   HD3  H  N N 69  
ARG   HE   H  N N 70  
ARG   HH11 H  N N 71  
ARG   HH12 H  N N 72  
ARG   HH21 H  N N 73  
ARG   HH22 H  N N 74  
ARG   HXT  H  N N 75  
ASN   N    N  N N 76  
ASN   CA   C  N S 77  
ASN   C    C  N N 78  
ASN   O    O  N N 79  
ASN   CB   C  N N 80  
ASN   CG   C  N N 81  
ASN   OD1  O  N N 82  
ASN   ND2  N  N N 83  
ASN   OXT  O  N N 84  
ASN   H    H  N N 85  
ASN   H2   H  N N 86  
ASN   HA   H  N N 87  
ASN   HB2  H  N N 88  
ASN   HB3  H  N N 89  
ASN   HD21 H  N N 90  
ASN   HD22 H  N N 91  
ASN   HXT  H  N N 92  
ASP   N    N  N N 93  
ASP   CA   C  N S 94  
ASP   C    C  N N 95  
ASP   O    O  N N 96  
ASP   CB   C  N N 97  
ASP   CG   C  N N 98  
ASP   OD1  O  N N 99  
ASP   OD2  O  N N 100 
ASP   OXT  O  N N 101 
ASP   H    H  N N 102 
ASP   H2   H  N N 103 
ASP   HA   H  N N 104 
ASP   HB2  H  N N 105 
ASP   HB3  H  N N 106 
ASP   HD2  H  N N 107 
ASP   HXT  H  N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
DMS   S    S  N N 123 
DMS   O    O  N N 124 
DMS   C1   C  N N 125 
DMS   C2   C  N N 126 
DMS   H11  H  N N 127 
DMS   H12  H  N N 128 
DMS   H13  H  N N 129 
DMS   H21  H  N N 130 
DMS   H22  H  N N 131 
DMS   H23  H  N N 132 
GLN   N    N  N N 133 
GLN   CA   C  N S 134 
GLN   C    C  N N 135 
GLN   O    O  N N 136 
GLN   CB   C  N N 137 
GLN   CG   C  N N 138 
GLN   CD   C  N N 139 
GLN   OE1  O  N N 140 
GLN   NE2  N  N N 141 
GLN   OXT  O  N N 142 
GLN   H    H  N N 143 
GLN   H2   H  N N 144 
GLN   HA   H  N N 145 
GLN   HB2  H  N N 146 
GLN   HB3  H  N N 147 
GLN   HG2  H  N N 148 
GLN   HG3  H  N N 149 
GLN   HE21 H  N N 150 
GLN   HE22 H  N N 151 
GLN   HXT  H  N N 152 
GLU   N    N  N N 153 
GLU   CA   C  N S 154 
GLU   C    C  N N 155 
GLU   O    O  N N 156 
GLU   CB   C  N N 157 
GLU   CG   C  N N 158 
GLU   CD   C  N N 159 
GLU   OE1  O  N N 160 
GLU   OE2  O  N N 161 
GLU   OXT  O  N N 162 
GLU   H    H  N N 163 
GLU   H2   H  N N 164 
GLU   HA   H  N N 165 
GLU   HB2  H  N N 166 
GLU   HB3  H  N N 167 
GLU   HG2  H  N N 168 
GLU   HG3  H  N N 169 
GLU   HE2  H  N N 170 
GLU   HXT  H  N N 171 
GLY   N    N  N N 172 
GLY   CA   C  N N 173 
GLY   C    C  N N 174 
GLY   O    O  N N 175 
GLY   OXT  O  N N 176 
GLY   H    H  N N 177 
GLY   H2   H  N N 178 
GLY   HA2  H  N N 179 
GLY   HA3  H  N N 180 
GLY   HXT  H  N N 181 
HIS   N    N  N N 182 
HIS   CA   C  N S 183 
HIS   C    C  N N 184 
HIS   O    O  N N 185 
HIS   CB   C  N N 186 
HIS   CG   C  Y N 187 
HIS   ND1  N  Y N 188 
HIS   CD2  C  Y N 189 
HIS   CE1  C  Y N 190 
HIS   NE2  N  Y N 191 
HIS   OXT  O  N N 192 
HIS   H    H  N N 193 
HIS   H2   H  N N 194 
HIS   HA   H  N N 195 
HIS   HB2  H  N N 196 
HIS   HB3  H  N N 197 
HIS   HD1  H  N N 198 
HIS   HD2  H  N N 199 
HIS   HE1  H  N N 200 
HIS   HE2  H  N N 201 
HIS   HXT  H  N N 202 
HOH   O    O  N N 203 
HOH   H1   H  N N 204 
HOH   H2   H  N N 205 
ILE   N    N  N N 206 
ILE   CA   C  N S 207 
ILE   C    C  N N 208 
ILE   O    O  N N 209 
ILE   CB   C  N S 210 
ILE   CG1  C  N N 211 
ILE   CG2  C  N N 212 
ILE   CD1  C  N N 213 
ILE   OXT  O  N N 214 
ILE   H    H  N N 215 
ILE   H2   H  N N 216 
ILE   HA   H  N N 217 
ILE   HB   H  N N 218 
ILE   HG12 H  N N 219 
ILE   HG13 H  N N 220 
ILE   HG21 H  N N 221 
ILE   HG22 H  N N 222 
ILE   HG23 H  N N 223 
ILE   HD11 H  N N 224 
ILE   HD12 H  N N 225 
ILE   HD13 H  N N 226 
ILE   HXT  H  N N 227 
LEU   N    N  N N 228 
LEU   CA   C  N S 229 
LEU   C    C  N N 230 
LEU   O    O  N N 231 
LEU   CB   C  N N 232 
LEU   CG   C  N N 233 
LEU   CD1  C  N N 234 
LEU   CD2  C  N N 235 
LEU   OXT  O  N N 236 
LEU   H    H  N N 237 
LEU   H2   H  N N 238 
LEU   HA   H  N N 239 
LEU   HB2  H  N N 240 
LEU   HB3  H  N N 241 
LEU   HG   H  N N 242 
LEU   HD11 H  N N 243 
LEU   HD12 H  N N 244 
LEU   HD13 H  N N 245 
LEU   HD21 H  N N 246 
LEU   HD22 H  N N 247 
LEU   HD23 H  N N 248 
LEU   HXT  H  N N 249 
LYS   N    N  N N 250 
LYS   CA   C  N S 251 
LYS   C    C  N N 252 
LYS   O    O  N N 253 
LYS   CB   C  N N 254 
LYS   CG   C  N N 255 
LYS   CD   C  N N 256 
LYS   CE   C  N N 257 
LYS   NZ   N  N N 258 
LYS   OXT  O  N N 259 
LYS   H    H  N N 260 
LYS   H2   H  N N 261 
LYS   HA   H  N N 262 
LYS   HB2  H  N N 263 
LYS   HB3  H  N N 264 
LYS   HG2  H  N N 265 
LYS   HG3  H  N N 266 
LYS   HD2  H  N N 267 
LYS   HD3  H  N N 268 
LYS   HE2  H  N N 269 
LYS   HE3  H  N N 270 
LYS   HZ1  H  N N 271 
LYS   HZ2  H  N N 272 
LYS   HZ3  H  N N 273 
LYS   HXT  H  N N 274 
MET   N    N  N N 275 
MET   CA   C  N S 276 
MET   C    C  N N 277 
MET   O    O  N N 278 
MET   CB   C  N N 279 
MET   CG   C  N N 280 
MET   SD   S  N N 281 
MET   CE   C  N N 282 
MET   OXT  O  N N 283 
MET   H    H  N N 284 
MET   H2   H  N N 285 
MET   HA   H  N N 286 
MET   HB2  H  N N 287 
MET   HB3  H  N N 288 
MET   HG2  H  N N 289 
MET   HG3  H  N N 290 
MET   HE1  H  N N 291 
MET   HE2  H  N N 292 
MET   HE3  H  N N 293 
MET   HXT  H  N N 294 
PHE   N    N  N N 295 
PHE   CA   C  N S 296 
PHE   C    C  N N 297 
PHE   O    O  N N 298 
PHE   CB   C  N N 299 
PHE   CG   C  Y N 300 
PHE   CD1  C  Y N 301 
PHE   CD2  C  Y N 302 
PHE   CE1  C  Y N 303 
PHE   CE2  C  Y N 304 
PHE   CZ   C  Y N 305 
PHE   OXT  O  N N 306 
PHE   H    H  N N 307 
PHE   H2   H  N N 308 
PHE   HA   H  N N 309 
PHE   HB2  H  N N 310 
PHE   HB3  H  N N 311 
PHE   HD1  H  N N 312 
PHE   HD2  H  N N 313 
PHE   HE1  H  N N 314 
PHE   HE2  H  N N 315 
PHE   HZ   H  N N 316 
PHE   HXT  H  N N 317 
PRO   N    N  N N 318 
PRO   CA   C  N S 319 
PRO   C    C  N N 320 
PRO   O    O  N N 321 
PRO   CB   C  N N 322 
PRO   CG   C  N N 323 
PRO   CD   C  N N 324 
PRO   OXT  O  N N 325 
PRO   H    H  N N 326 
PRO   HA   H  N N 327 
PRO   HB2  H  N N 328 
PRO   HB3  H  N N 329 
PRO   HG2  H  N N 330 
PRO   HG3  H  N N 331 
PRO   HD2  H  N N 332 
PRO   HD3  H  N N 333 
PRO   HXT  H  N N 334 
SER   N    N  N N 335 
SER   CA   C  N S 336 
SER   C    C  N N 337 
SER   O    O  N N 338 
SER   CB   C  N N 339 
SER   OG   O  N N 340 
SER   OXT  O  N N 341 
SER   H    H  N N 342 
SER   H2   H  N N 343 
SER   HA   H  N N 344 
SER   HB2  H  N N 345 
SER   HB3  H  N N 346 
SER   HG   H  N N 347 
SER   HXT  H  N N 348 
THR   N    N  N N 349 
THR   CA   C  N S 350 
THR   C    C  N N 351 
THR   O    O  N N 352 
THR   CB   C  N R 353 
THR   OG1  O  N N 354 
THR   CG2  C  N N 355 
THR   OXT  O  N N 356 
THR   H    H  N N 357 
THR   H2   H  N N 358 
THR   HA   H  N N 359 
THR   HB   H  N N 360 
THR   HG1  H  N N 361 
THR   HG21 H  N N 362 
THR   HG22 H  N N 363 
THR   HG23 H  N N 364 
THR   HXT  H  N N 365 
TRP   N    N  N N 366 
TRP   CA   C  N S 367 
TRP   C    C  N N 368 
TRP   O    O  N N 369 
TRP   CB   C  N N 370 
TRP   CG   C  Y N 371 
TRP   CD1  C  Y N 372 
TRP   CD2  C  Y N 373 
TRP   NE1  N  Y N 374 
TRP   CE2  C  Y N 375 
TRP   CE3  C  Y N 376 
TRP   CZ2  C  Y N 377 
TRP   CZ3  C  Y N 378 
TRP   CH2  C  Y N 379 
TRP   OXT  O  N N 380 
TRP   H    H  N N 381 
TRP   H2   H  N N 382 
TRP   HA   H  N N 383 
TRP   HB2  H  N N 384 
TRP   HB3  H  N N 385 
TRP   HD1  H  N N 386 
TRP   HE1  H  N N 387 
TRP   HE3  H  N N 388 
TRP   HZ2  H  N N 389 
TRP   HZ3  H  N N 390 
TRP   HH2  H  N N 391 
TRP   HXT  H  N N 392 
TYR   N    N  N N 393 
TYR   CA   C  N S 394 
TYR   C    C  N N 395 
TYR   O    O  N N 396 
TYR   CB   C  N N 397 
TYR   CG   C  Y N 398 
TYR   CD1  C  Y N 399 
TYR   CD2  C  Y N 400 
TYR   CE1  C  Y N 401 
TYR   CE2  C  Y N 402 
TYR   CZ   C  Y N 403 
TYR   OH   O  N N 404 
TYR   OXT  O  N N 405 
TYR   H    H  N N 406 
TYR   H2   H  N N 407 
TYR   HA   H  N N 408 
TYR   HB2  H  N N 409 
TYR   HB3  H  N N 410 
TYR   HD1  H  N N 411 
TYR   HD2  H  N N 412 
TYR   HE1  H  N N 413 
TYR   HE2  H  N N 414 
TYR   HH   H  N N 415 
TYR   HXT  H  N N 416 
VAL   N    N  N N 417 
VAL   CA   C  N S 418 
VAL   C    C  N N 419 
VAL   O    O  N N 420 
VAL   CB   C  N N 421 
VAL   CG1  C  N N 422 
VAL   CG2  C  N N 423 
VAL   OXT  O  N N 424 
VAL   H    H  N N 425 
VAL   H2   H  N N 426 
VAL   HA   H  N N 427 
VAL   HB   H  N N 428 
VAL   HG11 H  N N 429 
VAL   HG12 H  N N 430 
VAL   HG13 H  N N 431 
VAL   HG21 H  N N 432 
VAL   HG22 H  N N 433 
VAL   HG23 H  N N 434 
VAL   HXT  H  N N 435 
ZN    ZN   ZN N N 436 
# 
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 
A1B5J N   C    sing N N 1   
A1B5J O   C    doub N N 2   
A1B5J C   C1   sing N N 3   
A1B5J C1  C2   sing N N 4   
A1B5J C2  C3   sing N N 5   
A1B5J C3  C4   sing N N 6   
A1B5J C4  N1   sing N N 7   
A1B5J N1  C5   sing N N 8   
A1B5J O1  C5   doub N N 9   
A1B5J C5  C6   sing N N 10  
A1B5J C6  C7   sing N N 11  
A1B5J C7  C8   doub Y N 12  
A1B5J C8  C9   sing Y N 13  
A1B5J C9  C10  doub Y N 14  
A1B5J C10 N2   sing Y N 15  
A1B5J N2  C11  doub Y N 16  
A1B5J C7  C11  sing Y N 17  
A1B5J C11 CL   sing N N 18  
A1B5J C12 N1   sing N N 19  
A1B5J C1  C12  sing N N 20  
A1B5J C4  H8   sing N N 21  
A1B5J C4  H7   sing N N 22  
A1B5J C6  H10  sing N N 23  
A1B5J C6  H9   sing N N 24  
A1B5J C8  H11  sing N N 25  
A1B5J C10 H13  sing N N 26  
A1B5J C9  H12  sing N N 27  
A1B5J C3  H6   sing N N 28  
A1B5J C3  H5   sing N N 29  
A1B5J C2  H4   sing N N 30  
A1B5J C2  H3   sing N N 31  
A1B5J C12 H15  sing N N 32  
A1B5J C12 H14  sing N N 33  
A1B5J C1  H    sing N N 34  
A1B5J N   H2   sing N N 35  
A1B5J N   H1   sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
DMS   S   O    doub N N 119 
DMS   S   C1   sing N N 120 
DMS   S   C2   sing N N 121 
DMS   C1  H11  sing N N 122 
DMS   C1  H12  sing N N 123 
DMS   C1  H13  sing N N 124 
DMS   C2  H21  sing N N 125 
DMS   C2  H22  sing N N 126 
DMS   C2  H23  sing N N 127 
GLN   N   CA   sing N N 128 
GLN   N   H    sing N N 129 
GLN   N   H2   sing N N 130 
GLN   CA  C    sing N N 131 
GLN   CA  CB   sing N N 132 
GLN   CA  HA   sing N N 133 
GLN   C   O    doub N N 134 
GLN   C   OXT  sing N N 135 
GLN   CB  CG   sing N N 136 
GLN   CB  HB2  sing N N 137 
GLN   CB  HB3  sing N N 138 
GLN   CG  CD   sing N N 139 
GLN   CG  HG2  sing N N 140 
GLN   CG  HG3  sing N N 141 
GLN   CD  OE1  doub N N 142 
GLN   CD  NE2  sing N N 143 
GLN   NE2 HE21 sing N N 144 
GLN   NE2 HE22 sing N N 145 
GLN   OXT HXT  sing N N 146 
GLU   N   CA   sing N N 147 
GLU   N   H    sing N N 148 
GLU   N   H2   sing N N 149 
GLU   CA  C    sing N N 150 
GLU   CA  CB   sing N N 151 
GLU   CA  HA   sing N N 152 
GLU   C   O    doub N N 153 
GLU   C   OXT  sing N N 154 
GLU   CB  CG   sing N N 155 
GLU   CB  HB2  sing N N 156 
GLU   CB  HB3  sing N N 157 
GLU   CG  CD   sing N N 158 
GLU   CG  HG2  sing N N 159 
GLU   CG  HG3  sing N N 160 
GLU   CD  OE1  doub N N 161 
GLU   CD  OE2  sing N N 162 
GLU   OE2 HE2  sing N N 163 
GLU   OXT HXT  sing N N 164 
GLY   N   CA   sing N N 165 
GLY   N   H    sing N N 166 
GLY   N   H2   sing N N 167 
GLY   CA  C    sing N N 168 
GLY   CA  HA2  sing N N 169 
GLY   CA  HA3  sing N N 170 
GLY   C   O    doub N N 171 
GLY   C   OXT  sing N N 172 
GLY   OXT HXT  sing N N 173 
HIS   N   CA   sing N N 174 
HIS   N   H    sing N N 175 
HIS   N   H2   sing N N 176 
HIS   CA  C    sing N N 177 
HIS   CA  CB   sing N N 178 
HIS   CA  HA   sing N N 179 
HIS   C   O    doub N N 180 
HIS   C   OXT  sing N N 181 
HIS   CB  CG   sing N N 182 
HIS   CB  HB2  sing N N 183 
HIS   CB  HB3  sing N N 184 
HIS   CG  ND1  sing Y N 185 
HIS   CG  CD2  doub Y N 186 
HIS   ND1 CE1  doub Y N 187 
HIS   ND1 HD1  sing N N 188 
HIS   CD2 NE2  sing Y N 189 
HIS   CD2 HD2  sing N N 190 
HIS   CE1 NE2  sing Y N 191 
HIS   CE1 HE1  sing N N 192 
HIS   NE2 HE2  sing N N 193 
HIS   OXT HXT  sing N N 194 
HOH   O   H1   sing N N 195 
HOH   O   H2   sing N N 196 
ILE   N   CA   sing N N 197 
ILE   N   H    sing N N 198 
ILE   N   H2   sing N N 199 
ILE   CA  C    sing N N 200 
ILE   CA  CB   sing N N 201 
ILE   CA  HA   sing N N 202 
ILE   C   O    doub N N 203 
ILE   C   OXT  sing N N 204 
ILE   CB  CG1  sing N N 205 
ILE   CB  CG2  sing N N 206 
ILE   CB  HB   sing N N 207 
ILE   CG1 CD1  sing N N 208 
ILE   CG1 HG12 sing N N 209 
ILE   CG1 HG13 sing N N 210 
ILE   CG2 HG21 sing N N 211 
ILE   CG2 HG22 sing N N 212 
ILE   CG2 HG23 sing N N 213 
ILE   CD1 HD11 sing N N 214 
ILE   CD1 HD12 sing N N 215 
ILE   CD1 HD13 sing N N 216 
ILE   OXT HXT  sing N N 217 
LEU   N   CA   sing N N 218 
LEU   N   H    sing N N 219 
LEU   N   H2   sing N N 220 
LEU   CA  C    sing N N 221 
LEU   CA  CB   sing N N 222 
LEU   CA  HA   sing N N 223 
LEU   C   O    doub N N 224 
LEU   C   OXT  sing N N 225 
LEU   CB  CG   sing N N 226 
LEU   CB  HB2  sing N N 227 
LEU   CB  HB3  sing N N 228 
LEU   CG  CD1  sing N N 229 
LEU   CG  CD2  sing N N 230 
LEU   CG  HG   sing N N 231 
LEU   CD1 HD11 sing N N 232 
LEU   CD1 HD12 sing N N 233 
LEU   CD1 HD13 sing N N 234 
LEU   CD2 HD21 sing N N 235 
LEU   CD2 HD22 sing N N 236 
LEU   CD2 HD23 sing N N 237 
LEU   OXT HXT  sing N N 238 
LYS   N   CA   sing N N 239 
LYS   N   H    sing N N 240 
LYS   N   H2   sing N N 241 
LYS   CA  C    sing N N 242 
LYS   CA  CB   sing N N 243 
LYS   CA  HA   sing N N 244 
LYS   C   O    doub N N 245 
LYS   C   OXT  sing N N 246 
LYS   CB  CG   sing N N 247 
LYS   CB  HB2  sing N N 248 
LYS   CB  HB3  sing N N 249 
LYS   CG  CD   sing N N 250 
LYS   CG  HG2  sing N N 251 
LYS   CG  HG3  sing N N 252 
LYS   CD  CE   sing N N 253 
LYS   CD  HD2  sing N N 254 
LYS   CD  HD3  sing N N 255 
LYS   CE  NZ   sing N N 256 
LYS   CE  HE2  sing N N 257 
LYS   CE  HE3  sing N N 258 
LYS   NZ  HZ1  sing N N 259 
LYS   NZ  HZ2  sing N N 260 
LYS   NZ  HZ3  sing N N 261 
LYS   OXT HXT  sing N N 262 
MET   N   CA   sing N N 263 
MET   N   H    sing N N 264 
MET   N   H2   sing N N 265 
MET   CA  C    sing N N 266 
MET   CA  CB   sing N N 267 
MET   CA  HA   sing N N 268 
MET   C   O    doub N N 269 
MET   C   OXT  sing N N 270 
MET   CB  CG   sing N N 271 
MET   CB  HB2  sing N N 272 
MET   CB  HB3  sing N N 273 
MET   CG  SD   sing N N 274 
MET   CG  HG2  sing N N 275 
MET   CG  HG3  sing N N 276 
MET   SD  CE   sing N N 277 
MET   CE  HE1  sing N N 278 
MET   CE  HE2  sing N N 279 
MET   CE  HE3  sing N N 280 
MET   OXT HXT  sing N N 281 
PHE   N   CA   sing N N 282 
PHE   N   H    sing N N 283 
PHE   N   H2   sing N N 284 
PHE   CA  C    sing N N 285 
PHE   CA  CB   sing N N 286 
PHE   CA  HA   sing N N 287 
PHE   C   O    doub N N 288 
PHE   C   OXT  sing N N 289 
PHE   CB  CG   sing N N 290 
PHE   CB  HB2  sing N N 291 
PHE   CB  HB3  sing N N 292 
PHE   CG  CD1  doub Y N 293 
PHE   CG  CD2  sing Y N 294 
PHE   CD1 CE1  sing Y N 295 
PHE   CD1 HD1  sing N N 296 
PHE   CD2 CE2  doub Y N 297 
PHE   CD2 HD2  sing N N 298 
PHE   CE1 CZ   doub Y N 299 
PHE   CE1 HE1  sing N N 300 
PHE   CE2 CZ   sing Y N 301 
PHE   CE2 HE2  sing N N 302 
PHE   CZ  HZ   sing N N 303 
PHE   OXT HXT  sing N N 304 
PRO   N   CA   sing N N 305 
PRO   N   CD   sing N N 306 
PRO   N   H    sing N N 307 
PRO   CA  C    sing N N 308 
PRO   CA  CB   sing N N 309 
PRO   CA  HA   sing N N 310 
PRO   C   O    doub N N 311 
PRO   C   OXT  sing N N 312 
PRO   CB  CG   sing N N 313 
PRO   CB  HB2  sing N N 314 
PRO   CB  HB3  sing N N 315 
PRO   CG  CD   sing N N 316 
PRO   CG  HG2  sing N N 317 
PRO   CG  HG3  sing N N 318 
PRO   CD  HD2  sing N N 319 
PRO   CD  HD3  sing N N 320 
PRO   OXT HXT  sing N N 321 
SER   N   CA   sing N N 322 
SER   N   H    sing N N 323 
SER   N   H2   sing N N 324 
SER   CA  C    sing N N 325 
SER   CA  CB   sing N N 326 
SER   CA  HA   sing N N 327 
SER   C   O    doub N N 328 
SER   C   OXT  sing N N 329 
SER   CB  OG   sing N N 330 
SER   CB  HB2  sing N N 331 
SER   CB  HB3  sing N N 332 
SER   OG  HG   sing N N 333 
SER   OXT HXT  sing N N 334 
THR   N   CA   sing N N 335 
THR   N   H    sing N N 336 
THR   N   H2   sing N N 337 
THR   CA  C    sing N N 338 
THR   CA  CB   sing N N 339 
THR   CA  HA   sing N N 340 
THR   C   O    doub N N 341 
THR   C   OXT  sing N N 342 
THR   CB  OG1  sing N N 343 
THR   CB  CG2  sing N N 344 
THR   CB  HB   sing N N 345 
THR   OG1 HG1  sing N N 346 
THR   CG2 HG21 sing N N 347 
THR   CG2 HG22 sing N N 348 
THR   CG2 HG23 sing N N 349 
THR   OXT HXT  sing N N 350 
TRP   N   CA   sing N N 351 
TRP   N   H    sing N N 352 
TRP   N   H2   sing N N 353 
TRP   CA  C    sing N N 354 
TRP   CA  CB   sing N N 355 
TRP   CA  HA   sing N N 356 
TRP   C   O    doub N N 357 
TRP   C   OXT  sing N N 358 
TRP   CB  CG   sing N N 359 
TRP   CB  HB2  sing N N 360 
TRP   CB  HB3  sing N N 361 
TRP   CG  CD1  doub Y N 362 
TRP   CG  CD2  sing Y N 363 
TRP   CD1 NE1  sing Y N 364 
TRP   CD1 HD1  sing N N 365 
TRP   CD2 CE2  doub Y N 366 
TRP   CD2 CE3  sing Y N 367 
TRP   NE1 CE2  sing Y N 368 
TRP   NE1 HE1  sing N N 369 
TRP   CE2 CZ2  sing Y N 370 
TRP   CE3 CZ3  doub Y N 371 
TRP   CE3 HE3  sing N N 372 
TRP   CZ2 CH2  doub Y N 373 
TRP   CZ2 HZ2  sing N N 374 
TRP   CZ3 CH2  sing Y N 375 
TRP   CZ3 HZ3  sing N N 376 
TRP   CH2 HH2  sing N N 377 
TRP   OXT HXT  sing N N 378 
TYR   N   CA   sing N N 379 
TYR   N   H    sing N N 380 
TYR   N   H2   sing N N 381 
TYR   CA  C    sing N N 382 
TYR   CA  CB   sing N N 383 
TYR   CA  HA   sing N N 384 
TYR   C   O    doub N N 385 
TYR   C   OXT  sing N N 386 
TYR   CB  CG   sing N N 387 
TYR   CB  HB2  sing N N 388 
TYR   CB  HB3  sing N N 389 
TYR   CG  CD1  doub Y N 390 
TYR   CG  CD2  sing Y N 391 
TYR   CD1 CE1  sing Y N 392 
TYR   CD1 HD1  sing N N 393 
TYR   CD2 CE2  doub Y N 394 
TYR   CD2 HD2  sing N N 395 
TYR   CE1 CZ   doub Y N 396 
TYR   CE1 HE1  sing N N 397 
TYR   CE2 CZ   sing Y N 398 
TYR   CE2 HE2  sing N N 399 
TYR   CZ  OH   sing N N 400 
TYR   OH  HH   sing N N 401 
TYR   OXT HXT  sing N N 402 
VAL   N   CA   sing N N 403 
VAL   N   H    sing N N 404 
VAL   N   H2   sing N N 405 
VAL   CA  C    sing N N 406 
VAL   CA  CB   sing N N 407 
VAL   CA  HA   sing N N 408 
VAL   C   O    doub N N 409 
VAL   C   OXT  sing N N 410 
VAL   CB  CG1  sing N N 411 
VAL   CB  CG2  sing N N 412 
VAL   CB  HB   sing N N 413 
VAL   CG1 HG11 sing N N 414 
VAL   CG1 HG12 sing N N 415 
VAL   CG1 HG13 sing N N 416 
VAL   CG2 HG21 sing N N 417 
VAL   CG2 HG22 sing N N 418 
VAL   CG2 HG23 sing N N 419 
VAL   OXT HXT  sing N N 420 
# 
_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                    7I6Y 
_atom_sites.fract_transf_matrix[1][1]   0.013752 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000552 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016286 
_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]   0.015349 
_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   ? 16.332 6.372   8.259  1.00 18.53 ? 7   SER   A N   1 
ATOM   2    C  CA  . SER   A 1 1   ? 15.112 6.451   9.059  1.00 19.33 ? 7   SER   A CA  1 
ATOM   3    C  C   . SER   A 1 1   ? 15.009 5.298   10.056 1.00 18.79 ? 7   SER   A C   1 
ATOM   4    O  O   . SER   A 1 1   ? 15.714 4.297   9.910  1.00 19.20 ? 7   SER   A O   1 
ATOM   5    C  CB  . SER   A 1 1   ? 13.885 6.494   8.143  1.00 22.90 ? 7   SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 1   ? 13.794 5.296   7.389  1.00 26.23 ? 7   SER   A OG  1 
ATOM   7    N  N   . GLY   A 1 2   ? 14.166 5.451   11.076 1.00 17.62 ? 8   GLY   A N   1 
ATOM   8    C  CA  . GLY   A 1 2   ? 13.955 4.406   12.063 1.00 16.87 ? 8   GLY   A CA  1 
ATOM   9    C  C   . GLY   A 1 2   ? 13.572 4.968   13.422 1.00 16.05 ? 8   GLY   A C   1 
ATOM   10   O  O   . GLY   A 1 2   ? 13.939 6.098   13.753 1.00 15.39 ? 8   GLY   A O   1 
ATOM   11   N  N   . ALA   A 1 3   ? 12.834 4.191   14.198 1.00 14.76 ? 9   ALA   A N   1 
ATOM   12   C  CA  . ALA   A 1 3   ? 12.395 4.623   15.515 1.00 16.12 ? 9   ALA   A CA  1 
ATOM   13   C  C   . ALA   A 1 3   ? 12.367 3.413   16.463 1.00 15.91 ? 9   ALA   A C   1 
ATOM   14   O  O   . ALA   A 1 3   ? 12.352 2.252   15.996 1.00 16.15 ? 9   ALA   A O   1 
ATOM   15   C  CB  . ALA   A 1 3   ? 10.990 5.215   15.401 1.00 17.41 ? 9   ALA   A CB  1 
ATOM   16   N  N   . ILE   A 1 4   ? 12.321 3.689   17.782 1.00 13.93 ? 10  ILE   A N   1 
ATOM   17   C  CA  . ILE   A 1 4   ? 12.145 2.679   18.823 1.00 13.80 ? 10  ILE   A CA  1 
ATOM   18   C  C   . ILE   A 1 4   ? 10.748 2.902   19.368 1.00 14.49 ? 10  ILE   A C   1 
ATOM   19   O  O   . ILE   A 1 4   ? 10.390 4.045   19.681 1.00 14.48 ? 10  ILE   A O   1 
ATOM   20   C  CB  . ILE   A 1 4   ? 13.157 2.870   19.973 1.00 13.33 ? 10  ILE   A CB  1 
ATOM   21   C  CG1 . ILE   A 1 4   ? 14.619 2.860   19.433 1.00 13.22 ? 10  ILE   A CG1 1 
ATOM   22   C  CG2 . ILE   A 1 4   ? 12.942 1.823   21.054 1.00 14.76 ? 10  ILE   A CG2 1 
ATOM   23   C  CD1 . ILE   A 1 4   ? 15.646 3.437   20.481 1.00 13.50 ? 10  ILE   A CD1 1 
ATOM   24   N  N   . TYR   A 1 5   ? 9.959  1.825   19.491 1.00 14.92 ? 11  TYR   A N   1 
ATOM   25   C  CA  . TYR   A 1 5   ? 8.593  1.905   20.028 1.00 16.52 ? 11  TYR   A CA  1 
ATOM   26   C  C   . TYR   A 1 5   ? 8.525  1.172   21.344 1.00 17.06 ? 11  TYR   A C   1 
ATOM   27   O  O   . TYR   A 1 5   ? 8.608  -0.046  21.336 1.00 18.33 ? 11  TYR   A O   1 
ATOM   28   C  CB  . TYR   A 1 5   ? 7.619  1.294   19.011 1.00 16.87 ? 11  TYR   A CB  1 
ATOM   29   C  CG  . TYR   A 1 5   ? 7.530  2.130   17.761 1.00 17.93 ? 11  TYR   A CG  1 
ATOM   30   C  CD1 . TYR   A 1 5   ? 6.720  3.256   17.713 1.00 19.17 ? 11  TYR   A CD1 1 
ATOM   31   C  CD2 . TYR   A 1 5   ? 8.311  1.841   16.653 1.00 19.25 ? 11  TYR   A CD2 1 
ATOM   32   C  CE1 . TYR   A 1 5   ? 6.648  4.041   16.572 1.00 19.88 ? 11  TYR   A CE1 1 
ATOM   33   C  CE2 . TYR   A 1 5   ? 8.262  2.627   15.514 1.00 20.37 ? 11  TYR   A CE2 1 
ATOM   34   C  CZ  . TYR   A 1 5   ? 7.411  3.712   15.469 1.00 20.94 ? 11  TYR   A CZ  1 
ATOM   35   O  OH  . TYR   A 1 5   ? 7.384  4.504   14.352 1.00 23.87 ? 11  TYR   A OH  1 
ATOM   36   N  N   . VAL   A 1 6   ? 8.499  1.898   22.481 1.00 16.25 ? 12  VAL   A N   1 
ATOM   37   C  CA  . VAL   A 1 6   ? 8.480  1.260   23.803 1.00 17.79 ? 12  VAL   A CA  1 
ATOM   38   C  C   . VAL   A 1 6   ? 7.357  1.866   24.633 1.00 18.74 ? 12  VAL   A C   1 
ATOM   39   O  O   . VAL   A 1 6   ? 7.273  3.079   24.733 1.00 19.46 ? 12  VAL   A O   1 
ATOM   40   C  CB  . VAL   A 1 6   ? 9.865  1.368   24.501 1.00 19.85 ? 12  VAL   A CB  1 
ATOM   41   C  CG1 . VAL   A 1 6   ? 10.352 2.822   24.552 1.00 19.77 ? 12  VAL   A CG1 1 
ATOM   42   C  CG2 . VAL   A 1 6   ? 9.821  0.754   25.898 1.00 21.80 ? 12  VAL   A CG2 1 
ATOM   43   N  N   . GLY   A 1 7   ? 6.445  1.040   25.173 1.00 19.07 ? 13  GLY   A N   1 
ATOM   44   C  CA  . GLY   A 1 7   ? 5.300  1.551   25.929 1.00 19.22 ? 13  GLY   A CA  1 
ATOM   45   C  C   . GLY   A 1 7   ? 4.475  2.510   25.084 1.00 20.12 ? 13  GLY   A C   1 
ATOM   46   O  O   . GLY   A 1 7   ? 4.257  2.235   23.901 1.00 20.46 ? 13  GLY   A O   1 
ATOM   47   N  N   . ASN   A 1 8   ? 4.128  3.684   25.617 1.00 20.39 ? 14  ASN   A N   1 
ATOM   48   C  CA  . ASN   A 1 8   ? 3.426  4.688   24.821 1.00 20.83 ? 14  ASN   A CA  1 
ATOM   49   C  C   . ASN   A 1 8   ? 4.397  5.759   24.320 1.00 19.68 ? 14  ASN   A C   1 
ATOM   50   O  O   . ASN   A 1 8   ? 4.005  6.924   24.182 1.00 19.57 ? 14  ASN   A O   1 
ATOM   51   C  CB  . ASN   A 1 8   ? 2.270  5.317   25.582 1.00 24.58 ? 14  ASN   A CB  1 
ATOM   52   C  CG  . ASN   A 1 8   ? 1.122  4.361   25.743 1.00 32.51 ? 14  ASN   A CG  1 
ATOM   53   O  OD1 . ASN   A 1 8   ? 0.595  3.810   24.763 1.00 35.32 ? 14  ASN   A OD1 1 
ATOM   54   N  ND2 . ASN   A 1 8   ? 0.728  4.154   26.985 1.00 34.59 ? 14  ASN   A ND2 1 
ATOM   55   N  N   . TYR   A 1 9   ? 5.639  5.357   23.981 1.00 18.33 ? 15  TYR   A N   1 
ATOM   56   C  CA  . TYR   A 1 9   ? 6.663  6.277   23.503 1.00 17.07 ? 15  TYR   A CA  1 
ATOM   57   C  C   . TYR   A 1 9   ? 7.237  5.852   22.144 1.00 15.89 ? 15  TYR   A C   1 
ATOM   58   O  O   . TYR   A 1 9   ? 7.360  4.649   21.861 1.00 15.42 ? 15  TYR   A O   1 
ATOM   59   C  CB  . TYR   A 1 9   ? 7.841  6.355   24.511 1.00 17.72 ? 15  TYR   A CB  1 
ATOM   60   C  CG  . TYR   A 1 9   ? 7.453  6.909   25.867 1.00 17.62 ? 15  TYR   A CG  1 
ATOM   61   C  CD1 . TYR   A 1 9   ? 6.830  8.142   25.983 1.00 19.00 ? 15  TYR   A CD1 1 
ATOM   62   C  CD2 . TYR   A 1 9   ? 7.747  6.216   27.034 1.00 19.18 ? 15  TYR   A CD2 1 
ATOM   63   C  CE1 . TYR   A 1 9   ? 6.472  8.660   27.228 1.00 20.52 ? 15  TYR   A CE1 1 
ATOM   64   C  CE2 . TYR   A 1 9   ? 7.403  6.729   28.286 1.00 21.00 ? 15  TYR   A CE2 1 
ATOM   65   C  CZ  . TYR   A 1 9   ? 6.757  7.953   28.373 1.00 22.59 ? 15  TYR   A CZ  1 
ATOM   66   O  OH  . TYR   A 1 9   ? 6.405  8.486   29.590 1.00 24.55 ? 15  TYR   A OH  1 
ATOM   67   N  N   . ARG   A 1 10  ? 7.634  6.866   21.334 1.00 13.78 ? 16  ARG   A N   1 
ATOM   68   C  CA  . ARG   A 1 10  ? 8.322  6.675   20.058 1.00 13.69 ? 16  ARG   A CA  1 
ATOM   69   C  C   . ARG   A 1 10  ? 9.638  7.472   20.174 1.00 14.56 ? 16  ARG   A C   1 
ATOM   70   O  O   . ARG   A 1 10  ? 9.600  8.663   20.464 1.00 15.19 ? 16  ARG   A O   1 
ATOM   71   C  CB  . ARG   A 1 10  ? 7.473  7.202   18.889 1.00 15.60 ? 16  ARG   A CB  1 
ATOM   72   C  CG  . ARG   A 1 10  ? 8.218  7.409   17.572 1.00 17.93 ? 16  ARG   A CG  1 
ATOM   73   C  CD  . ARG   A 1 10  ? 7.289  7.758   16.419 1.00 18.22 ? 16  ARG   A CD  1 
ATOM   74   N  NE  . ARG   A 1 10  ? 7.848  8.768   15.515 1.00 21.20 ? 16  ARG   A NE  1 
ATOM   75   C  CZ  . ARG   A 1 10  ? 8.313  8.529   14.294 1.00 23.84 ? 16  ARG   A CZ  1 
ATOM   76   N  NH1 . ARG   A 1 10  ? 8.395  7.281   13.836 1.00 22.23 ? 16  ARG   A NH1 1 
ATOM   77   N  NH2 . ARG   A 1 10  ? 8.760  9.529   13.542 1.00 23.81 ? 16  ARG   A NH2 1 
ATOM   78   N  N   . VAL   A 1 11  ? 10.790 6.805   19.996 1.00 13.39 ? 17  VAL   A N   1 
ATOM   79   C  CA  . VAL   A 1 11  ? 12.091 7.487   20.101 1.00 13.22 ? 17  VAL   A CA  1 
ATOM   80   C  C   . VAL   A 1 11  ? 12.659 7.612   18.692 1.00 14.05 ? 17  VAL   A C   1 
ATOM   81   O  O   . VAL   A 1 11  ? 12.812 6.599   18.009 1.00 13.34 ? 17  VAL   A O   1 
ATOM   82   C  CB  . VAL   A 1 11  ? 13.101 6.670   20.973 1.00 13.80 ? 17  VAL   A CB  1 
ATOM   83   C  CG1 . VAL   A 1 11  ? 14.401 7.497   21.194 1.00 13.25 ? 17  VAL   A CG1 1 
ATOM   84   C  CG2 . VAL   A 1 11  ? 12.472 6.226   22.301 1.00 14.76 ? 17  VAL   A CG2 1 
ATOM   85   N  N   . VAL   A 1 12  ? 12.985 8.836   18.264 1.00 12.71 ? 18  VAL   A N   1 
ATOM   86   C  CA  . VAL   A 1 12  ? 13.527 9.060   16.919 1.00 12.36 ? 18  VAL   A CA  1 
ATOM   87   C  C   . VAL   A 1 12  ? 14.751 9.998   17.012 1.00 11.36 ? 18  VAL   A C   1 
ATOM   88   O  O   . VAL   A 1 12  ? 14.962 10.704  18.020 1.00 12.57 ? 18  VAL   A O   1 
ATOM   89   C  CB  . VAL   A 1 12  ? 12.458 9.727   16.002 1.00 14.07 ? 18  VAL   A CB  1 
ATOM   90   C  CG1 . VAL   A 1 12  ? 11.326 8.767   15.695 1.00 16.77 ? 18  VAL   A CG1 1 
ATOM   91   C  CG2 . VAL   A 1 12  ? 11.943 11.033  16.636 1.00 14.01 ? 18  VAL   A CG2 1 
ATOM   92   N  N   . ASN   A 1 13  ? 15.526 10.088  15.909 1.00 11.14 ? 19  ASN   A N   1 
ATOM   93   C  CA  . ASN   A 1 13  ? 16.583 11.116  15.844 1.00 10.75 ? 19  ASN   A CA  1 
ATOM   94   C  C   . ASN   A 1 13  ? 15.867 12.469  15.838 1.00 11.92 ? 19  ASN   A C   1 
ATOM   95   O  O   . ASN   A 1 13  ? 14.914 12.679  15.060 1.00 12.98 ? 19  ASN   A O   1 
ATOM   96   C  CB  . ASN   A 1 13  ? 17.370 11.015  14.519 1.00 11.58 ? 19  ASN   A CB  1 
ATOM   97   C  CG  . ASN   A 1 13  ? 18.176 9.753   14.446 1.00 14.02 ? 19  ASN   A CG  1 
ATOM   98   O  OD1 . ASN   A 1 13  ? 17.724 8.740   13.880 1.00 15.38 ? 19  ASN   A OD1 1 
ATOM   99   N  ND2 . ASN   A 1 13  ? 19.392 9.815   14.968 1.00 12.92 ? 19  ASN   A ND2 1 
ATOM   100  N  N   . ARG   A 1 14  ? 16.322 13.397  16.686 1.00 10.86 ? 20  ARG   A N   1 
ATOM   101  C  CA  . ARG   A 1 14  ? 15.640 14.717  16.753 1.00 10.34 ? 20  ARG   A CA  1 
ATOM   102  C  C   . ARG   A 1 14  ? 15.624 15.409  15.373 1.00 11.39 ? 20  ARG   A C   1 
ATOM   103  O  O   . ARG   A 1 14  ? 14.620 16.025  14.999 1.00 13.64 ? 20  ARG   A O   1 
ATOM   104  C  CB  . ARG   A 1 14  ? 16.344 15.602  17.772 1.00 11.08 ? 20  ARG   A CB  1 
ATOM   105  C  CG  . ARG   A 1 14  ? 15.572 16.881  18.136 1.00 12.82 ? 20  ARG   A CG  1 
ATOM   106  C  CD  . ARG   A 1 14  ? 16.516 17.773  18.921 1.00 13.09 ? 20  ARG   A CD  1 
ATOM   107  N  NE  . ARG   A 1 14  ? 15.889 18.992  19.444 1.00 14.97 ? 20  ARG   A NE  1 
ATOM   108  C  CZ  . ARG   A 1 14  ? 15.836 20.143  18.778 1.00 15.85 ? 20  ARG   A CZ  1 
ATOM   109  N  NH1 . ARG   A 1 14  ? 16.299 20.222  17.528 1.00 14.14 ? 20  ARG   A NH1 1 
ATOM   110  N  NH2 . ARG   A 1 14  ? 15.338 21.233  19.362 1.00 15.64 ? 20  ARG   A NH2 1 
ATOM   111  N  N   . HIS   A 1 15  ? 16.738 15.272  14.595 1.00 11.59 ? 21  HIS   A N   1 
ATOM   112  C  CA  . HIS   A 1 15  ? 16.793 15.947  13.283 1.00 12.89 ? 21  HIS   A CA  1 
ATOM   113  C  C   . HIS   A 1 15  ? 15.829 15.368  12.233 1.00 14.47 ? 21  HIS   A C   1 
ATOM   114  O  O   . HIS   A 1 15  ? 15.582 16.017  11.190 1.00 16.81 ? 21  HIS   A O   1 
ATOM   115  C  CB  . HIS   A 1 15  ? 18.246 16.000  12.739 1.00 14.06 ? 21  HIS   A CB  1 
ATOM   116  C  CG  . HIS   A 1 15  ? 18.804 14.695  12.248 1.00 14.06 ? 21  HIS   A CG  1 
ATOM   117  N  ND1 . HIS   A 1 15  ? 19.426 13.789  13.111 1.00 13.98 ? 21  HIS   A ND1 1 
ATOM   118  C  CD2 . HIS   A 1 15  ? 18.915 14.230  10.976 1.00 15.70 ? 21  HIS   A CD2 1 
ATOM   119  C  CE1 . HIS   A 1 15  ? 19.877 12.803  12.334 1.00 14.70 ? 21  HIS   A CE1 1 
ATOM   120  N  NE2 . HIS   A 1 15  ? 19.591 13.023  11.041 1.00 15.01 ? 21  HIS   A NE2 1 
ATOM   121  N  N   . LEU   A 1 16  ? 15.279 14.169  12.499 1.00 13.70 ? 22  LEU   A N   1 
ATOM   122  C  CA  . LEU   A 1 16  ? 14.334 13.515  11.589 1.00 13.98 ? 22  LEU   A CA  1 
ATOM   123  C  C   . LEU   A 1 16  ? 12.887 13.541  12.144 1.00 14.25 ? 22  LEU   A C   1 
ATOM   124  O  O   . LEU   A 1 16  ? 11.983 12.936  11.538 1.00 14.44 ? 22  LEU   A O   1 
ATOM   125  C  CB  . LEU   A 1 16  ? 14.789 12.080  11.305 1.00 14.53 ? 22  LEU   A CB  1 
ATOM   126  C  CG  . LEU   A 1 16  ? 16.161 11.943  10.631 1.00 15.80 ? 22  LEU   A CG  1 
ATOM   127  C  CD1 . LEU   A 1 16  ? 16.507 10.468  10.391 1.00 16.16 ? 22  LEU   A CD1 1 
ATOM   128  C  CD2 . LEU   A 1 16  ? 16.201 12.695  9.296  1.00 15.04 ? 22  LEU   A CD2 1 
ATOM   129  N  N   . ALA   A 1 17  ? 12.669 14.172  13.323 1.00 14.20 ? 23  ALA   A N   1 
ATOM   130  C  CA  . ALA   A 1 17  ? 11.322 14.192  13.918 1.00 14.24 ? 23  ALA   A CA  1 
ATOM   131  C  C   . ALA   A 1 17  ? 10.320 14.857  12.974 1.00 15.52 ? 23  ALA   A C   1 
ATOM   132  O  O   . ALA   A 1 17  ? 10.674 15.812  12.306 1.00 16.06 ? 23  ALA   A O   1 
ATOM   133  C  CB  . ALA   A 1 17  ? 11.351 14.956  15.234 1.00 14.25 ? 23  ALA   A CB  1 
ATOM   134  N  N   . THR   A 1 18  ? 9.102  14.328  12.917 1.00 15.77 ? 24  THR   A N   1 
ATOM   135  C  CA  . THR   A 1 18  ? 8.063  14.863  12.026 1.00 17.10 ? 24  THR   A CA  1 
ATOM   136  C  C   . THR   A 1 18  ? 7.223  15.965  12.735 1.00 18.17 ? 24  THR   A C   1 
ATOM   137  O  O   . THR   A 1 18  ? 7.348  16.170  13.952 1.00 17.79 ? 24  THR   A O   1 
ATOM   138  C  CB  . THR   A 1 18  ? 7.104  13.692  11.643 1.00 19.20 ? 24  THR   A CB  1 
ATOM   139  O  OG1 . THR   A 1 18  ? 6.411  13.279  12.833 1.00 20.08 ? 24  THR   A OG1 1 
ATOM   140  C  CG2 . THR   A 1 18  ? 7.816  12.520  11.016 1.00 19.70 ? 24  THR   A CG2 1 
ATOM   141  N  N   . HIS   A 1 19  ? 6.264  16.605  11.995 1.00 18.92 ? 25  HIS   A N   1 
ATOM   142  C  CA  . HIS   A 1 19  ? 5.345  17.554  12.628 1.00 21.10 ? 25  HIS   A CA  1 
ATOM   143  C  C   . HIS   A 1 19  ? 4.539  16.850  13.744 1.00 19.43 ? 25  HIS   A C   1 
ATOM   144  O  O   . HIS   A 1 19  ? 4.354  17.413  14.830 1.00 19.59 ? 25  HIS   A O   1 
ATOM   145  C  CB  . HIS   A 1 19  ? 4.338  18.089  11.575 1.00 24.90 ? 25  HIS   A CB  1 
ATOM   146  C  CG  . HIS   A 1 19  ? 4.965  18.901  10.491 1.00 33.46 ? 25  HIS   A CG  1 
ATOM   147  N  ND1 . HIS   A 1 19  ? 5.842  19.936  10.775 1.00 37.17 ? 25  HIS   A ND1 1 
ATOM   148  C  CD2 . HIS   A 1 19  ? 4.776  18.842  9.148  1.00 36.19 ? 25  HIS   A CD2 1 
ATOM   149  C  CE1 . HIS   A 1 19  ? 6.181  20.451  9.601  1.00 37.99 ? 25  HIS   A CE1 1 
ATOM   150  N  NE2 . HIS   A 1 19  ? 5.565  19.823  8.592  1.00 37.84 ? 25  HIS   A NE2 1 
ATOM   151  N  N   . ASN   A 1 20  ? 4.107  15.589  13.486 1.00 18.91 ? 26  ASN   A N   1 
ATOM   152  C  CA  . ASN   A 1 20  ? 3.361  14.819  14.474 1.00 18.67 ? 26  ASN   A CA  1 
ATOM   153  C  C   . ASN   A 1 20  ? 4.189  14.514  15.727 1.00 17.73 ? 26  ASN   A C   1 
ATOM   154  O  O   . ASN   A 1 20  ? 3.670  14.586  16.850 1.00 18.13 ? 26  ASN   A O   1 
ATOM   155  C  CB  . ASN   A 1 20  ? 2.814  13.541  13.880 1.00 21.62 ? 26  ASN   A CB  1 
ATOM   156  C  CG  . ASN   A 1 20  ? 1.528  13.787  13.148 1.00 28.77 ? 26  ASN   A CG  1 
ATOM   157  O  OD1 . ASN   A 1 20  ? 0.705  14.630  13.558 1.00 29.41 ? 26  ASN   A OD1 1 
ATOM   158  N  ND2 . ASN   A 1 20  ? 1.356  13.102  12.026 1.00 30.46 ? 26  ASN   A ND2 1 
ATOM   159  N  N   . ASP   A 1 21  ? 5.491  14.213  15.563 1.00 15.63 ? 27  ASP   A N   1 
ATOM   160  C  CA  . ASP   A 1 21  ? 6.366  13.988  16.722 1.00 14.76 ? 27  ASP   A CA  1 
ATOM   161  C  C   . ASP   A 1 21  ? 6.398  15.245  17.603 1.00 14.64 ? 27  ASP   A C   1 
ATOM   162  O  O   . ASP   A 1 21  ? 6.257  15.140  18.815 1.00 15.41 ? 27  ASP   A O   1 
ATOM   163  C  CB  . ASP   A 1 21  ? 7.804  13.677  16.266 1.00 14.79 ? 27  ASP   A CB  1 
ATOM   164  C  CG  . ASP   A 1 21  ? 7.951  12.267  15.746 1.00 18.98 ? 27  ASP   A CG  1 
ATOM   165  O  OD1 . ASP   A 1 21  ? 7.372  11.354  16.357 1.00 19.35 ? 27  ASP   A OD1 1 
ATOM   166  O  OD2 . ASP   A 1 21  ? 8.655  12.082  14.707 1.00 19.45 ? 27  ASP   A OD2 1 
ATOM   167  N  N   . TRP   A 1 22  ? 6.571  16.432  16.980 1.00 14.54 ? 28  TRP   A N   1 
ATOM   168  C  CA  . TRP   A 1 22  ? 6.649  17.677  17.761 1.00 15.00 ? 28  TRP   A CA  1 
ATOM   169  C  C   . TRP   A 1 22  ? 5.296  18.040  18.386 1.00 16.53 ? 28  TRP   A C   1 
ATOM   170  O  O   . TRP   A 1 22  ? 5.268  18.584  19.492 1.00 16.75 ? 28  TRP   A O   1 
ATOM   171  C  CB  . TRP   A 1 22  ? 7.174  18.806  16.885 1.00 15.11 ? 28  TRP   A CB  1 
ATOM   172  C  CG  . TRP   A 1 22  ? 8.671  18.798  16.760 1.00 15.06 ? 28  TRP   A CG  1 
ATOM   173  C  CD1 . TRP   A 1 22  ? 9.414  18.400  15.682 1.00 16.41 ? 28  TRP   A CD1 1 
ATOM   174  C  CD2 . TRP   A 1 22  ? 9.595  19.338  17.711 1.00 15.16 ? 28  TRP   A CD2 1 
ATOM   175  N  NE1 . TRP   A 1 22  ? 10.760 18.607  15.932 1.00 15.75 ? 28  TRP   A NE1 1 
ATOM   176  C  CE2 . TRP   A 1 22  ? 10.895 19.183  17.176 1.00 15.69 ? 28  TRP   A CE2 1 
ATOM   177  C  CE3 . TRP   A 1 22  ? 9.453  19.887  18.985 1.00 16.05 ? 28  TRP   A CE3 1 
ATOM   178  C  CZ2 . TRP   A 1 22  ? 12.040 19.620  17.858 1.00 15.45 ? 28  TRP   A CZ2 1 
ATOM   179  C  CZ3 . TRP   A 1 22  ? 10.590 20.306  19.663 1.00 16.55 ? 28  TRP   A CZ3 1 
ATOM   180  C  CH2 . TRP   A 1 22  ? 11.862 20.149  19.107 1.00 16.22 ? 28  TRP   A CH2 1 
ATOM   181  N  N   . ALA   A 1 23  ? 4.167  17.680  17.728 1.00 16.88 ? 29  ALA   A N   1 
ATOM   182  C  CA  . ALA   A 1 23  ? 2.832  17.969  18.300 1.00 18.94 ? 29  ALA   A CA  1 
ATOM   183  C  C   . ALA   A 1 23  ? 2.506  17.047  19.510 1.00 19.05 ? 29  ALA   A C   1 
ATOM   184  O  O   . ALA   A 1 23  ? 1.611  17.342  20.312 1.00 19.77 ? 29  ALA   A O   1 
ATOM   185  C  CB  . ALA   A 1 23  ? 1.781  17.791  17.232 1.00 20.45 ? 29  ALA   A CB  1 
ATOM   186  N  N   . ASN   A 1 24  ? 3.232  15.917  19.639 1.00 17.63 ? 30  ASN   A N   1 
ATOM   187  C  CA  . ASN   A 1 24  ? 3.035  14.978  20.745 1.00 17.63 ? 30  ASN   A CA  1 
ATOM   188  C  C   . ASN   A 1 24  ? 4.362  14.827  21.546 1.00 17.13 ? 30  ASN   A C   1 
ATOM   189  O  O   . ASN   A 1 24  ? 4.665  13.756  22.077 1.00 15.67 ? 30  ASN   A O   1 
ATOM   190  C  CB  . ASN   A 1 24  ? 2.601  13.633  20.172 1.00 19.21 ? 30  ASN   A CB  1 
ATOM   191  C  CG  . ASN   A 1 24  ? 1.246  13.694  19.517 1.00 22.05 ? 30  ASN   A CG  1 
ATOM   192  O  OD1 . ASN   A 1 24  ? 0.218  13.684  20.208 1.00 23.37 ? 30  ASN   A OD1 1 
ATOM   193  N  ND2 . ASN   A 1 24  ? 1.215  13.742  18.185 1.00 21.49 ? 30  ASN   A ND2 1 
ATOM   194  N  N   . LEU   A 1 25  ? 5.131  15.930  21.645 1.00 17.11 ? 31  LEU   A N   1 
ATOM   195  C  CA  . LEU   A 1 25  ? 6.425  15.961  22.304 1.00 16.78 ? 31  LEU   A CA  1 
ATOM   196  C  C   . LEU   A 1 25  ? 6.372  15.584  23.774 1.00 16.96 ? 31  LEU   A C   1 
ATOM   197  O  O   . LEU   A 1 25  ? 5.558  16.121  24.537 1.00 17.82 ? 31  LEU   A O   1 
ATOM   198  C  CB  . LEU   A 1 25  ? 7.025  17.358  22.155 1.00 16.80 ? 31  LEU   A CB  1 
ATOM   199  C  CG  . LEU   A 1 25  ? 8.394  17.553  22.802 1.00 17.08 ? 31  LEU   A CG  1 
ATOM   200  C  CD1 . LEU   A 1 25  ? 9.451  16.653  22.116 1.00 17.81 ? 31  LEU   A CD1 1 
ATOM   201  C  CD2 . LEU   A 1 25  ? 8.826  19.036  22.740 1.00 17.12 ? 31  LEU   A CD2 1 
ATOM   202  N  N   . VAL   A 1 26  ? 7.269  14.666  24.192 1.00 15.92 ? 32  VAL   A N   1 
ATOM   203  C  CA  . VAL   A 1 26  ? 7.413  14.281  25.598 1.00 16.39 ? 32  VAL   A CA  1 
ATOM   204  C  C   . VAL   A 1 26  ? 8.741  14.879  26.113 1.00 17.23 ? 32  VAL   A C   1 
ATOM   205  O  O   . VAL   A 1 26  ? 8.807  15.479  27.196 1.00 19.37 ? 32  VAL   A O   1 
ATOM   206  C  CB  . VAL   A 1 26  ? 7.435  12.731  25.729 1.00 17.94 ? 32  VAL   A CB  1 
ATOM   207  C  CG1 . VAL   A 1 26  ? 7.858  12.313  27.139 1.00 19.02 ? 32  VAL   A CG1 1 
ATOM   208  C  CG2 . VAL   A 1 26  ? 6.060  12.146  25.385 1.00 18.77 ? 32  VAL   A CG2 1 
ATOM   209  N  N   . TRP   A 1 27  ? 9.811  14.725  25.322 1.00 15.51 ? 33  TRP   A N   1 
ATOM   210  C  CA  . TRP   A 1 27  ? 11.142 15.182  25.709 1.00 15.65 ? 33  TRP   A CA  1 
ATOM   211  C  C   . TRP   A 1 27  ? 12.030 15.268  24.452 1.00 14.43 ? 33  TRP   A C   1 
ATOM   212  O  O   . TRP   A 1 27  ? 11.904 14.440  23.558 1.00 14.31 ? 33  TRP   A O   1 
ATOM   213  C  CB  . TRP   A 1 27  ? 11.768 14.167  26.705 1.00 16.62 ? 33  TRP   A CB  1 
ATOM   214  C  CG  . TRP   A 1 27  ? 13.234 14.367  27.023 1.00 18.16 ? 33  TRP   A CG  1 
ATOM   215  C  CD1 . TRP   A 1 27  ? 13.773 15.232  27.933 1.00 19.99 ? 33  TRP   A CD1 1 
ATOM   216  C  CD2 . TRP   A 1 27  ? 14.331 13.645  26.457 1.00 18.08 ? 33  TRP   A CD2 1 
ATOM   217  N  NE1 . TRP   A 1 27  ? 15.150 15.133  27.922 1.00 20.71 ? 33  TRP   A NE1 1 
ATOM   218  C  CE2 . TRP   A 1 27  ? 15.518 14.172  27.012 1.00 19.20 ? 33  TRP   A CE2 1 
ATOM   219  C  CE3 . TRP   A 1 27  ? 14.428 12.640  25.490 1.00 17.82 ? 33  TRP   A CE3 1 
ATOM   220  C  CZ2 . TRP   A 1 27  ? 16.774 13.633  26.729 1.00 18.95 ? 33  TRP   A CZ2 1 
ATOM   221  C  CZ3 . TRP   A 1 27  ? 15.682 12.156  25.161 1.00 18.30 ? 33  TRP   A CZ3 1 
ATOM   222  C  CH2 . TRP   A 1 27  ? 16.836 12.652  25.782 1.00 18.26 ? 33  TRP   A CH2 1 
ATOM   223  N  N   . GLU   A 1 28  ? 12.912 16.256  24.404 1.00 13.99 ? 34  GLU   A N   1 
ATOM   224  C  CA  . GLU   A 1 28  ? 13.890 16.348  23.322 1.00 13.98 ? 34  GLU   A CA  1 
ATOM   225  C  C   . GLU   A 1 28  ? 15.194 16.921  23.840 1.00 13.92 ? 34  GLU   A C   1 
ATOM   226  O  O   . GLU   A 1 28  ? 15.202 17.692  24.816 1.00 14.45 ? 34  GLU   A O   1 
ATOM   227  C  CB  . GLU   A 1 28  ? 13.360 17.132  22.106 1.00 15.68 ? 34  GLU   A CB  1 
ATOM   228  C  CG  . GLU   A 1 28  ? 12.815 18.531  22.413 1.00 17.52 ? 34  GLU   A CG  1 
ATOM   229  C  CD  . GLU   A 1 28  ? 13.837 19.635  22.633 1.00 19.17 ? 34  GLU   A CD  1 
ATOM   230  O  OE1 . GLU   A 1 28  ? 13.543 20.547  23.448 1.00 23.46 ? 34  GLU   A OE1 1 
ATOM   231  O  OE2 . GLU   A 1 28  ? 14.938 19.571  22.039 1.00 17.11 ? 34  GLU   A OE2 1 
ATOM   232  N  N   . ASP   A 1 29  ? 16.307 16.545  23.206 1.00 13.34 ? 35  ASP   A N   1 
ATOM   233  C  CA  . ASP   A 1 29  ? 17.611 17.054  23.625 1.00 13.38 ? 35  ASP   A CA  1 
ATOM   234  C  C   . ASP   A 1 29  ? 18.481 17.191  22.372 1.00 13.72 ? 35  ASP   A C   1 
ATOM   235  O  O   . ASP   A 1 29  ? 18.930 16.195  21.801 1.00 13.55 ? 35  ASP   A O   1 
ATOM   236  C  CB  . ASP   A 1 29  ? 18.248 16.156  24.705 1.00 16.15 ? 35  ASP   A CB  1 
ATOM   237  C  CG  . ASP   A 1 29  ? 19.522 16.730  25.301 1.00 21.83 ? 35  ASP   A CG  1 
ATOM   238  O  OD1 . ASP   A 1 29  ? 20.182 17.541  24.619 1.00 21.91 ? 35  ASP   A OD1 1 
ATOM   239  O  OD2 . ASP   A 1 29  ? 19.892 16.317  26.433 1.00 22.86 ? 35  ASP   A OD2 1 
ATOM   240  N  N   . SER   A 1 30  ? 18.686 18.457  21.932 1.00 13.94 ? 36  SER   A N   1 
ATOM   241  C  CA  A SER   A 1 30  ? 19.471 18.757  20.749 0.50 14.91 ? 36  SER   A CA  1 
ATOM   242  C  CA  B SER   A 1 30  ? 19.466 18.716  20.729 0.50 14.64 ? 36  SER   A CA  1 
ATOM   243  C  C   . SER   A 1 30  ? 20.901 18.238  20.913 1.00 14.64 ? 36  SER   A C   1 
ATOM   244  O  O   . SER   A 1 30  ? 21.501 17.765  19.958 1.00 15.66 ? 36  SER   A O   1 
ATOM   245  C  CB  A SER   A 1 30  ? 19.484 20.265  20.504 0.50 16.82 ? 36  SER   A CB  1 
ATOM   246  C  CB  B SER   A 1 30  ? 19.438 20.199  20.357 0.50 15.77 ? 36  SER   A CB  1 
ATOM   247  O  OG  A SER   A 1 30  ? 20.291 20.577  19.386 0.50 19.33 ? 36  SER   A OG  1 
ATOM   248  O  OG  B SER   A 1 30  ? 20.163 20.971  21.294 0.50 16.71 ? 36  SER   A OG  1 
ATOM   249  N  N   . SER   A 1 31  ? 21.455 18.341  22.143 1.00 14.27 ? 37  SER   A N   1 
ATOM   250  C  CA  . SER   A 1 31  ? 22.828 17.878  22.374 1.00 15.92 ? 37  SER   A CA  1 
ATOM   251  C  C   . SER   A 1 31  ? 22.973 16.364  22.213 1.00 15.50 ? 37  SER   A C   1 
ATOM   252  O  O   . SER   A 1 31  ? 24.094 15.893  22.015 1.00 17.03 ? 37  SER   A O   1 
ATOM   253  C  CB  . SER   A 1 31  ? 23.345 18.319  23.744 1.00 18.74 ? 37  SER   A CB  1 
ATOM   254  O  OG  . SER   A 1 31  ? 22.875 17.502  24.804 1.00 23.26 ? 37  SER   A OG  1 
ATOM   255  N  N   . ARG   A 1 32  ? 21.854 15.602  22.272 1.00 13.69 ? 38  ARG   A N   1 
ATOM   256  C  CA  . ARG   A 1 32  ? 21.921 14.127  22.118 1.00 13.09 ? 38  ARG   A CA  1 
ATOM   257  C  C   . ARG   A 1 32  ? 21.361 13.660  20.749 1.00 13.22 ? 38  ARG   A C   1 
ATOM   258  O  O   . ARG   A 1 32  ? 21.420 12.459  20.439 1.00 13.96 ? 38  ARG   A O   1 
ATOM   259  C  CB  . ARG   A 1 32  ? 21.115 13.433  23.244 1.00 13.61 ? 38  ARG   A CB  1 
ATOM   260  C  CG  . ARG   A 1 32  ? 21.697 13.686  24.634 1.00 14.55 ? 38  ARG   A CG  1 
ATOM   261  C  CD  . ARG   A 1 32  ? 20.869 13.007  25.732 1.00 15.83 ? 38  ARG   A CD  1 
ATOM   262  N  NE  . ARG   A 1 32  ? 20.892 11.539  25.593 1.00 14.78 ? 38  ARG   A NE  1 
ATOM   263  C  CZ  . ARG   A 1 32  ? 20.713 10.692  26.612 1.00 16.29 ? 38  ARG   A CZ  1 
ATOM   264  N  NH1 . ARG   A 1 32  ? 20.549 11.156  27.856 1.00 16.71 ? 38  ARG   A NH1 1 
ATOM   265  N  NH2 . ARG   A 1 32  ? 20.748 9.371   26.405 1.00 14.69 ? 38  ARG   A NH2 1 
ATOM   266  N  N   . ASP   A 1 33  ? 20.779 14.602  19.953 1.00 13.32 ? 39  ASP   A N   1 
ATOM   267  C  CA  . ASP   A 1 33  ? 20.091 14.257  18.703 1.00 12.24 ? 39  ASP   A CA  1 
ATOM   268  C  C   . ASP   A 1 33  ? 18.930 13.297  18.983 1.00 11.43 ? 39  ASP   A C   1 
ATOM   269  O  O   . ASP   A 1 33  ? 18.626 12.468  18.114 1.00 12.51 ? 39  ASP   A O   1 
ATOM   270  C  CB  . ASP   A 1 33  ? 21.011 13.697  17.601 1.00 13.56 ? 39  ASP   A CB  1 
ATOM   271  C  CG  . ASP   A 1 33  ? 20.295 13.441  16.280 1.00 12.91 ? 39  ASP   A CG  1 
ATOM   272  O  OD1 . ASP   A 1 33  ? 19.469 14.303  15.869 1.00 12.98 ? 39  ASP   A OD1 1 
ATOM   273  O  OD2 . ASP   A 1 33  ? 20.575 12.388  15.641 1.00 12.83 ? 39  ASP   A OD2 1 
ATOM   274  N  N   . LEU   A 1 34  ? 18.242 13.428  20.167 1.00 11.40 ? 40  LEU   A N   1 
ATOM   275  C  CA  . LEU   A 1 34  ? 17.087 12.577  20.442 1.00 10.58 ? 40  LEU   A CA  1 
ATOM   276  C  C   . LEU   A 1 34  ? 15.796 13.376  20.623 1.00 10.56 ? 40  LEU   A C   1 
ATOM   277  O  O   . LEU   A 1 34  ? 15.804 14.455  21.207 1.00 12.04 ? 40  LEU   A O   1 
ATOM   278  C  CB  . LEU   A 1 34  ? 17.279 11.748  21.730 1.00 10.45 ? 40  LEU   A CB  1 
ATOM   279  C  CG  . LEU   A 1 34  ? 18.320 10.619  21.664 1.00 12.21 ? 40  LEU   A CG  1 
ATOM   280  C  CD1 . LEU   A 1 34  ? 18.422 9.928   23.034 1.00 13.73 ? 40  LEU   A CD1 1 
ATOM   281  C  CD2 . LEU   A 1 34  ? 17.956 9.554   20.607 1.00 12.38 ? 40  LEU   A CD2 1 
ATOM   282  N  N   . LEU   A 1 35  ? 14.669 12.722  20.283 1.00 10.09 ? 41  LEU   A N   1 
ATOM   283  C  CA  . LEU   A 1 35  ? 13.346 13.276  20.542 1.00 11.35 ? 41  LEU   A CA  1 
ATOM   284  C  C   . LEU   A 1 35  ? 12.436 12.085  20.850 1.00 12.38 ? 41  LEU   A C   1 
ATOM   285  O  O   . LEU   A 1 35  ? 12.519 11.039  20.183 1.00 12.80 ? 41  LEU   A O   1 
ATOM   286  C  CB  . LEU   A 1 35  ? 12.817 14.100  19.351 1.00 11.76 ? 41  LEU   A CB  1 
ATOM   287  C  CG  . LEU   A 1 35  ? 11.429 14.748  19.552 1.00 13.13 ? 41  LEU   A CG  1 
ATOM   288  C  CD1 . LEU   A 1 35  ? 11.328 16.096  18.811 1.00 15.60 ? 41  LEU   A CD1 1 
ATOM   289  C  CD2 . LEU   A 1 35  ? 10.320 13.849  19.041 1.00 13.29 ? 41  LEU   A CD2 1 
ATOM   290  N  N   . VAL   A 1 36  ? 11.585 12.233  21.877 1.00 12.24 ? 42  VAL   A N   1 
ATOM   291  C  CA  . VAL   A 1 36  ? 10.608 11.200  22.245 1.00 12.76 ? 42  VAL   A CA  1 
ATOM   292  C  C   . VAL   A 1 36  ? 9.225  11.822  22.158 1.00 13.69 ? 42  VAL   A C   1 
ATOM   293  O  O   . VAL   A 1 36  ? 9.003  12.915  22.709 1.00 14.32 ? 42  VAL   A O   1 
ATOM   294  C  CB  . VAL   A 1 36  ? 10.860 10.633  23.671 1.00 14.40 ? 42  VAL   A CB  1 
ATOM   295  C  CG1 . VAL   A 1 36  ? 9.786  9.603   24.069 1.00 15.58 ? 42  VAL   A CG1 1 
ATOM   296  C  CG2 . VAL   A 1 36  ? 12.261 10.018  23.743 1.00 13.93 ? 42  VAL   A CG2 1 
ATOM   297  N  N   . SER   A 1 37  ? 8.313  11.129  21.451 1.00 12.90 ? 43  SER   A N   1 
ATOM   298  C  CA  . SER   A 1 37  ? 6.926  11.583  21.332 1.00 14.35 ? 43  SER   A CA  1 
ATOM   299  C  C   . SER   A 1 37  ? 5.996  10.489  21.916 1.00 16.70 ? 43  SER   A C   1 
ATOM   300  O  O   . SER   A 1 37  ? 6.424  9.342   22.113 1.00 16.62 ? 43  SER   A O   1 
ATOM   301  C  CB  . SER   A 1 37  ? 6.560  11.902  19.874 1.00 15.40 ? 43  SER   A CB  1 
ATOM   302  O  OG  . SER   A 1 37  ? 6.698  10.768  19.030 1.00 18.24 ? 43  SER   A OG  1 
ATOM   303  N  N   . SER   A 1 38  ? 4.739  10.865  22.225 1.00 16.72 ? 44  SER   A N   1 
ATOM   304  C  CA  . SER   A 1 38  ? 3.786  9.896   22.760 1.00 18.13 ? 44  SER   A CA  1 
ATOM   305  C  C   . SER   A 1 38  ? 3.019  9.187   21.629 1.00 19.36 ? 44  SER   A C   1 
ATOM   306  O  O   . SER   A 1 38  ? 2.830  9.743   20.549 1.00 20.16 ? 44  SER   A O   1 
ATOM   307  C  CB  . SER   A 1 38  ? 2.814  10.595  23.712 1.00 20.73 ? 44  SER   A CB  1 
ATOM   308  O  OG  . SER   A 1 38  ? 2.193  11.658  23.016 1.00 23.33 ? 44  SER   A OG  1 
ATOM   309  N  N   . THR   A 1 39  ? 2.574  7.944   21.877 1.00 20.08 ? 45  THR   A N   1 
ATOM   310  C  CA  . THR   A 1 39  ? 1.828  7.184   20.877 1.00 21.97 ? 45  THR   A CA  1 
ATOM   311  C  C   . THR   A 1 39  ? 0.514  6.709   21.494 1.00 25.99 ? 45  THR   A C   1 
ATOM   312  O  O   . THR   A 1 39  ? 0.406  6.579   22.725 1.00 27.12 ? 45  THR   A O   1 
ATOM   313  C  CB  . THR   A 1 39  ? 2.637  5.949   20.409 1.00 22.71 ? 45  THR   A CB  1 
ATOM   314  O  OG1 . THR   A 1 39  ? 2.794  5.082   21.528 1.00 23.46 ? 45  THR   A OG1 1 
ATOM   315  C  CG2 . THR   A 1 39  ? 3.997  6.307   19.859 1.00 22.79 ? 45  THR   A CG2 1 
ATOM   316  N  N   . THR   A 1 40  ? -0.467 6.408   20.642 1.00 28.00 ? 46  THR   A N   1 
ATOM   317  C  CA  . THR   A 1 40  ? -1.730 5.864   21.119 1.00 30.75 ? 46  THR   A CA  1 
ATOM   318  C  C   . THR   A 1 40  ? -1.592 4.327   21.253 1.00 32.09 ? 46  THR   A C   1 
ATOM   319  O  O   . THR   A 1 40  ? -2.110 3.743   22.211 1.00 33.21 ? 46  THR   A O   1 
ATOM   320  C  CB  . THR   A 1 40  ? -2.872 6.261   20.166 1.00 33.69 ? 46  THR   A CB  1 
ATOM   321  O  OG1 . THR   A 1 40  ? -2.495 5.918   18.822 1.00 35.23 ? 46  THR   A OG1 1 
ATOM   322  C  CG2 . THR   A 1 40  ? -3.204 7.743   20.240 1.00 34.67 ? 46  THR   A CG2 1 
ATOM   323  N  N   . ALA   A 1 41  ? -0.870 3.688   20.312 1.00 31.80 ? 47  ALA   A N   1 
ATOM   324  C  CA  . ALA   A 1 41  ? -0.665 2.242   20.308 1.00 32.49 ? 47  ALA   A CA  1 
ATOM   325  C  C   . ALA   A 1 41  ? 0.488  1.845   21.225 1.00 32.85 ? 47  ALA   A C   1 
ATOM   326  O  O   . ALA   A 1 41  ? 1.437  2.602   21.407 1.00 32.19 ? 47  ALA   A O   1 
ATOM   327  C  CB  . ALA   A 1 41  ? -0.383 1.754   18.893 1.00 32.60 ? 47  ALA   A CB  1 
ATOM   328  N  N   . GLN   A 1 42  ? 0.384  0.672   21.810 1.00 33.27 ? 48  GLN   A N   1 
ATOM   329  C  CA  . GLN   A 1 42  ? 1.395  0.159   22.705 1.00 34.10 ? 48  GLN   A CA  1 
ATOM   330  C  C   . GLN   A 1 42  ? 2.557  -0.381  21.888 1.00 33.69 ? 48  GLN   A C   1 
ATOM   331  O  O   . GLN   A 1 42  ? 2.365  -1.111  20.921 1.00 33.46 ? 48  GLN   A O   1 
ATOM   332  C  CB  . GLN   A 1 42  ? 0.791  -0.956  23.583 1.00 37.30 ? 48  GLN   A CB  1 
ATOM   333  C  CG  . GLN   A 1 42  ? 1.822  -1.752  24.385 1.00 42.82 ? 48  GLN   A CG  1 
ATOM   334  C  CD  . GLN   A 1 42  ? 2.296  -1.020  25.615 1.00 49.94 ? 48  GLN   A CD  1 
ATOM   335  O  OE1 . GLN   A 1 42  ? 1.644  -0.084  26.115 1.00 52.57 ? 48  GLN   A OE1 1 
ATOM   336  N  NE2 . GLN   A 1 42  ? 3.443  -1.446  26.139 1.00 51.07 ? 48  GLN   A NE2 1 
ATOM   337  N  N   . GLY   A 1 43  ? 3.753  0.015   22.270 1.00 33.58 ? 49  GLY   A N   1 
ATOM   338  C  CA  . GLY   A 1 43  ? 4.972  -0.491  21.675 1.00 34.78 ? 49  GLY   A CA  1 
ATOM   339  C  C   . GLY   A 1 43  ? 5.559  -1.526  22.623 1.00 35.75 ? 49  GLY   A C   1 
ATOM   340  O  O   . GLY   A 1 43  ? 5.423  -1.408  23.857 1.00 36.76 ? 49  GLY   A O   1 
ATOM   341  N  N   . CYS   A 1 44  ? 6.222  -2.526  22.070 1.00 34.58 ? 50  CYS   A N   1 
ATOM   342  C  CA  . CYS   A 1 44  ? 6.837  -3.528  22.930 1.00 34.39 ? 50  CYS   A CA  1 
ATOM   343  C  C   . CYS   A 1 44  ? 8.239  -3.863  22.530 1.00 32.53 ? 50  CYS   A C   1 
ATOM   344  O  O   . CYS   A 1 44  ? 8.712  -4.951  22.875 1.00 33.24 ? 50  CYS   A O   1 
ATOM   345  C  CB  . CYS   A 1 44  ? 5.972  -4.766  23.068 1.00 35.95 ? 50  CYS   A CB  1 
ATOM   346  S  SG  . CYS   A 1 44  ? 5.468  -5.438  21.487 1.00 43.11 ? 50  CYS   A SG  1 
ATOM   347  N  N   . ASP   A 1 45  ? 8.998  -2.856  21.966 1.00 29.80 ? 51  ASP   A N   1 
ATOM   348  C  CA  . ASP   A 1 45  ? 10.461 -2.954  21.825 1.00 26.72 ? 51  ASP   A CA  1 
ATOM   349  C  C   . ASP   A 1 45  ? 10.904 -2.897  23.340 1.00 25.25 ? 51  ASP   A C   1 
ATOM   350  O  O   . ASP   A 1 45  ? 10.130 -2.382  24.187 1.00 27.25 ? 51  ASP   A O   1 
ATOM   351  C  CB  . ASP   A 1 45  ? 11.103 -1.725  21.073 1.00 25.49 ? 51  ASP   A CB  1 
ATOM   352  C  CG  . ASP   A 1 45  ? 11.455 -1.819  19.572 1.00 27.48 ? 51  ASP   A CG  1 
ATOM   353  O  OD1 . ASP   A 1 45  ? 12.132 -2.819  19.175 1.00 25.85 ? 51  ASP   A OD1 1 
ATOM   354  O  OD2 . ASP   A 1 45  ? 11.121 -0.828  18.790 1.00 24.37 ? 51  ASP   A OD2 1 
ATOM   355  N  N   . THR   A 1 46  ? 12.006 -3.524  23.697 1.00 22.07 ? 52  THR   A N   1 
ATOM   356  C  CA  . THR   A 1 46  ? 12.462 -3.503  25.072 1.00 22.56 ? 52  THR   A CA  1 
ATOM   357  C  C   . THR   A 1 46  ? 13.841 -2.831  25.120 1.00 19.83 ? 52  THR   A C   1 
ATOM   358  O  O   . THR   A 1 46  ? 14.673 -3.041  24.243 1.00 19.32 ? 52  THR   A O   1 
ATOM   359  C  CB  . THR   A 1 46  ? 12.339 -4.885  25.694 1.00 27.07 ? 52  THR   A CB  1 
ATOM   360  O  OG1 . THR   A 1 46  ? 13.143 -5.781  24.970 1.00 29.74 ? 52  THR   A OG1 1 
ATOM   361  C  CG2 . THR   A 1 46  ? 10.906 -5.394  25.690 1.00 27.41 ? 52  THR   A CG2 1 
ATOM   362  N  N   . ILE   A 1 47  ? 14.049 -1.976  26.136 1.00 17.27 ? 53  ILE   A N   1 
ATOM   363  C  CA  . ILE   A 1 47  ? 15.296 -1.244  26.248 1.00 15.82 ? 53  ILE   A CA  1 
ATOM   364  C  C   . ILE   A 1 47  ? 16.302 -2.012  27.096 1.00 16.05 ? 53  ILE   A C   1 
ATOM   365  O  O   . ILE   A 1 47  ? 15.945 -2.501  28.187 1.00 16.87 ? 53  ILE   A O   1 
ATOM   366  C  CB  . ILE   A 1 47  ? 15.043 0.169   26.858 1.00 15.07 ? 53  ILE   A CB  1 
ATOM   367  C  CG1 . ILE   A 1 47  ? 13.919 0.955   26.118 1.00 15.62 ? 53  ILE   A CG1 1 
ATOM   368  C  CG2 . ILE   A 1 47  ? 16.341 0.994   26.909 1.00 14.61 ? 53  ILE   A CG2 1 
ATOM   369  C  CD1 . ILE   A 1 47  ? 14.264 1.199   24.622 1.00 16.65 ? 53  ILE   A CD1 1 
ATOM   370  N  N   . ALA   A 1 48  ? 17.558 -2.092  26.628 1.00 14.71 ? 54  ALA   A N   1 
ATOM   371  C  CA  . ALA   A 1 48  ? 18.630 -2.738  27.388 1.00 14.07 ? 54  ALA   A CA  1 
ATOM   372  C  C   . ALA   A 1 48  ? 18.966 -1.870  28.610 1.00 14.53 ? 54  ALA   A C   1 
ATOM   373  O  O   . ALA   A 1 48  ? 18.998 -0.652  28.509 1.00 14.98 ? 54  ALA   A O   1 
ATOM   374  C  CB  . ALA   A 1 48  ? 19.888 -2.885  26.511 1.00 13.64 ? 54  ALA   A CB  1 
ATOM   375  N  N   . ARG   A 1 49  ? 19.273 -2.515  29.765 1.00 14.89 ? 55  ARG   A N   1 
ATOM   376  C  CA  . ARG   A 1 49  ? 19.710 -1.763  30.964 1.00 15.37 ? 55  ARG   A CA  1 
ATOM   377  C  C   . ARG   A 1 49  ? 20.996 -2.506  31.352 1.00 17.24 ? 55  ARG   A C   1 
ATOM   378  O  O   . ARG   A 1 49  ? 20.951 -3.517  32.071 1.00 18.06 ? 55  ARG   A O   1 
ATOM   379  C  CB  . ARG   A 1 49  ? 18.644 -1.837  32.081 1.00 15.70 ? 55  ARG   A CB  1 
ATOM   380  C  CG  . ARG   A 1 49  ? 17.290 -1.249  31.675 1.00 16.30 ? 55  ARG   A CG  1 
ATOM   381  C  CD  . ARG   A 1 49  ? 17.328 0.259   31.300 1.00 18.55 ? 55  ARG   A CD  1 
ATOM   382  N  NE  . ARG   A 1 49  ? 15.991 0.732   30.937 1.00 18.00 ? 55  ARG   A NE  1 
ATOM   383  C  CZ  . ARG   A 1 49  ? 15.740 1.882   30.315 1.00 20.59 ? 55  ARG   A CZ  1 
ATOM   384  N  NH1 . ARG   A 1 49  ? 16.735 2.703   29.991 1.00 20.12 ? 55  ARG   A NH1 1 
ATOM   385  N  NH2 . ARG   A 1 49  ? 14.493 2.220   30.012 1.00 20.94 ? 55  ARG   A NH2 1 
ATOM   386  N  N   . CYS   A 1 50  ? 22.126 -2.062  30.793 1.00 16.91 ? 56  CYS   A N   1 
ATOM   387  C  CA  . CYS   A 1 50  ? 23.382 -2.804  30.894 1.00 17.18 ? 56  CYS   A CA  1 
ATOM   388  C  C   . CYS   A 1 50  ? 24.569 -1.911  30.539 1.00 18.65 ? 56  CYS   A C   1 
ATOM   389  O  O   . CYS   A 1 50  ? 24.385 -0.767  30.096 1.00 20.07 ? 56  CYS   A O   1 
ATOM   390  C  CB  . CYS   A 1 50  ? 23.311 -3.978  29.909 1.00 16.94 ? 56  CYS   A CB  1 
ATOM   391  S  SG  . CYS   A 1 50  ? 23.275 -3.456  28.173 1.00 16.90 ? 56  CYS   A SG  1 
ATOM   392  N  N   . ASP   A 1 51  ? 25.796 -2.499  30.602 1.00 19.64 ? 57  ASP   A N   1 
ATOM   393  C  CA  . ASP   A 1 51  ? 26.993 -1.792  30.157 1.00 20.83 ? 57  ASP   A CA  1 
ATOM   394  C  C   . ASP   A 1 51  ? 27.658 -2.503  28.982 1.00 21.30 ? 57  ASP   A C   1 
ATOM   395  O  O   . ASP   A 1 51  ? 28.876 -2.401  28.822 1.00 22.12 ? 57  ASP   A O   1 
ATOM   396  C  CB  . ASP   A 1 51  ? 28.004 -1.604  31.305 1.00 23.96 ? 57  ASP   A CB  1 
ATOM   397  C  CG  . ASP   A 1 51  ? 28.514 -2.895  31.932 1.00 29.89 ? 57  ASP   A CG  1 
ATOM   398  O  OD1 . ASP   A 1 51  ? 28.034 -3.986  31.540 1.00 29.91 ? 57  ASP   A OD1 1 
ATOM   399  O  OD2 . ASP   A 1 51  ? 29.405 -2.818  32.796 1.00 35.25 ? 57  ASP   A OD2 1 
ATOM   400  N  N   . CYS   A 1 52  ? 26.879 -3.201  28.126 1.00 19.55 ? 58  CYS   A N   1 
ATOM   401  C  CA  . CYS   A 1 52  ? 27.467 -3.864  26.946 1.00 17.93 ? 58  CYS   A CA  1 
ATOM   402  C  C   . CYS   A 1 52  ? 28.212 -2.880  26.061 1.00 17.79 ? 58  CYS   A C   1 
ATOM   403  O  O   . CYS   A 1 52  ? 27.786 -1.728  25.913 1.00 17.81 ? 58  CYS   A O   1 
ATOM   404  C  CB  . CYS   A 1 52  ? 26.384 -4.561  26.131 1.00 17.74 ? 58  CYS   A CB  1 
ATOM   405  S  SG  . CYS   A 1 52  ? 25.761 -6.102  26.849 1.00 18.76 ? 58  CYS   A SG  1 
ATOM   406  N  N   . GLN   A 1 53  ? 29.316 -3.340  25.472 1.00 16.17 ? 59  GLN   A N   1 
ATOM   407  C  CA  . GLN   A 1 53  ? 30.101 -2.605  24.483 1.00 14.83 ? 59  GLN   A CA  1 
ATOM   408  C  C   . GLN   A 1 53  ? 30.246 -3.391  23.184 1.00 13.79 ? 59  GLN   A C   1 
ATOM   409  O  O   . GLN   A 1 53  ? 31.127 -3.078  22.370 1.00 14.97 ? 59  GLN   A O   1 
ATOM   410  C  CB  . GLN   A 1 53  ? 31.465 -2.178  25.011 1.00 16.38 ? 59  GLN   A CB  1 
ATOM   411  C  CG  . GLN   A 1 53  ? 31.407 -1.011  25.958 1.00 21.52 ? 59  GLN   A CG  1 
ATOM   412  C  CD  . GLN   A 1 53  ? 32.823 -0.623  26.346 1.00 26.51 ? 59  GLN   A CD  1 
ATOM   413  O  OE1 . GLN   A 1 53  ? 33.273 -0.856  27.483 1.00 26.25 ? 59  GLN   A OE1 1 
ATOM   414  N  NE2 . GLN   A 1 53  ? 33.569 -0.028  25.399 1.00 24.77 ? 59  GLN   A NE2 1 
ATOM   415  N  N   . THR   A 1 54  ? 29.398 -4.440  22.986 1.00 11.62 ? 60  THR   A N   1 
ATOM   416  C  CA  . THR   A 1 54  ? 29.298 -5.168  21.721 1.00 12.67 ? 60  THR   A CA  1 
ATOM   417  C  C   . THR   A 1 54  ? 27.789 -5.342  21.437 1.00 12.63 ? 60  THR   A C   1 
ATOM   418  O  O   . THR   A 1 54  ? 26.959 -5.463  22.350 1.00 14.28 ? 60  THR   A O   1 
ATOM   419  C  CB  . THR   A 1 54  ? 30.008 -6.553  21.760 1.00 14.64 ? 60  THR   A CB  1 
ATOM   420  O  OG1 . THR   A 1 54  ? 29.313 -7.389  22.694 1.00 15.91 ? 60  THR   A OG1 1 
ATOM   421  C  CG2 . THR   A 1 54  ? 31.467 -6.454  22.171 1.00 15.93 ? 60  THR   A CG2 1 
ATOM   422  N  N   . GLY   A 1 55  ? 27.462 -5.358  20.175 1.00 12.03 ? 61  GLY   A N   1 
ATOM   423  C  CA  . GLY   A 1 55  ? 26.075 -5.550  19.755 1.00 11.48 ? 61  GLY   A CA  1 
ATOM   424  C  C   . GLY   A 1 55  ? 26.001 -5.649  18.242 1.00 11.73 ? 61  GLY   A C   1 
ATOM   425  O  O   . GLY   A 1 55  ? 27.015 -5.854  17.581 1.00 11.85 ? 61  GLY   A O   1 
ATOM   426  N  N   . VAL   A 1 56  ? 24.793 -5.528  17.718 1.00 10.88 ? 62  VAL   A N   1 
ATOM   427  C  CA  . VAL   A 1 56  ? 24.536 -5.636  16.277 1.00 10.68 ? 62  VAL   A CA  1 
ATOM   428  C  C   . VAL   A 1 56  ? 23.665 -4.448  15.872 1.00 11.16 ? 62  VAL   A C   1 
ATOM   429  O  O   . VAL   A 1 56  ? 22.681 -4.174  16.544 1.00 11.65 ? 62  VAL   A O   1 
ATOM   430  C  CB  . VAL   A 1 56  ? 23.829 -6.969  15.960 1.00 12.07 ? 62  VAL   A CB  1 
ATOM   431  C  CG1 . VAL   A 1 56  ? 23.482 -7.054  14.471 1.00 14.10 ? 62  VAL   A CG1 1 
ATOM   432  C  CG2 . VAL   A 1 56  ? 24.733 -8.144  16.358 1.00 13.11 ? 62  VAL   A CG2 1 
ATOM   433  N  N   . TYR   A 1 57  ? 24.006 -3.791  14.741 1.00 11.20 ? 63  TYR   A N   1 
ATOM   434  C  CA  . TYR   A 1 57  ? 23.159 -2.682  14.273 1.00 10.90 ? 63  TYR   A CA  1 
ATOM   435  C  C   . TYR   A 1 57  ? 22.615 -2.928  12.881 1.00 11.57 ? 63  TYR   A C   1 
ATOM   436  O  O   . TYR   A 1 57  ? 23.235 -3.637  12.090 1.00 12.27 ? 63  TYR   A O   1 
ATOM   437  C  CB  . TYR   A 1 57  ? 23.880 -1.299  14.344 1.00 10.84 ? 63  TYR   A CB  1 
ATOM   438  C  CG  . TYR   A 1 57  ? 24.873 -1.019  13.225 1.00 10.65 ? 63  TYR   A CG  1 
ATOM   439  C  CD1 . TYR   A 1 57  ? 26.157 -1.560  13.252 1.00 11.53 ? 63  TYR   A CD1 1 
ATOM   440  C  CD2 . TYR   A 1 57  ? 24.565 -0.132  12.199 1.00 11.58 ? 63  TYR   A CD2 1 
ATOM   441  C  CE1 . TYR   A 1 57  ? 27.090 -1.254  12.261 1.00 11.78 ? 63  TYR   A CE1 1 
ATOM   442  C  CE2 . TYR   A 1 57  ? 25.479 0.150   11.179 1.00 11.88 ? 63  TYR   A CE2 1 
ATOM   443  C  CZ  . TYR   A 1 57  ? 26.738 -0.413  11.215 1.00 12.46 ? 63  TYR   A CZ  1 
ATOM   444  O  OH  . TYR   A 1 57  ? 27.668 -0.158  10.228 1.00 13.85 ? 63  TYR   A OH  1 
ATOM   445  N  N   . TYR   A 1 58  ? 21.471 -2.299  12.577 1.00 11.32 ? 64  TYR   A N   1 
ATOM   446  C  CA  . TYR   A 1 58  ? 20.908 -2.411  11.232 1.00 11.68 ? 64  TYR   A CA  1 
ATOM   447  C  C   . TYR   A 1 58  ? 21.386 -1.226  10.352 1.00 12.22 ? 64  TYR   A C   1 
ATOM   448  O  O   . TYR   A 1 58  ? 21.256 -0.063  10.737 1.00 12.12 ? 64  TYR   A O   1 
ATOM   449  C  CB  . TYR   A 1 58  ? 19.369 -2.445  11.279 1.00 11.60 ? 64  TYR   A CB  1 
ATOM   450  C  CG  . TYR   A 1 58  ? 18.797 -2.578  9.891  1.00 13.12 ? 64  TYR   A CG  1 
ATOM   451  C  CD1 . TYR   A 1 58  ? 19.071 -3.692  9.115  1.00 13.64 ? 64  TYR   A CD1 1 
ATOM   452  C  CD2 . TYR   A 1 58  ? 18.078 -1.539  9.314  1.00 13.96 ? 64  TYR   A CD2 1 
ATOM   453  C  CE1 . TYR   A 1 58  ? 18.592 -3.802  7.817  1.00 15.67 ? 64  TYR   A CE1 1 
ATOM   454  C  CE2 . TYR   A 1 58  ? 17.614 -1.622  8.013  1.00 15.60 ? 64  TYR   A CE2 1 
ATOM   455  C  CZ  . TYR   A 1 58  ? 17.875 -2.755  7.266  1.00 17.11 ? 64  TYR   A CZ  1 
ATOM   456  O  OH  . TYR   A 1 58  ? 17.407 -2.876  5.990  1.00 19.63 ? 64  TYR   A OH  1 
ATOM   457  N  N   . CYS   A 1 59  ? 21.950 -1.567  9.177  1.00 12.04 ? 65  CYS   A N   1 
ATOM   458  C  CA  . CYS   A 1 59  ? 22.468 -0.567  8.234  1.00 11.84 ? 65  CYS   A CA  1 
ATOM   459  C  C   . CYS   A 1 59  ? 21.569 -0.561  6.967  1.00 13.70 ? 65  CYS   A C   1 
ATOM   460  O  O   . CYS   A 1 59  ? 21.699 -1.443  6.108  1.00 14.35 ? 65  CYS   A O   1 
ATOM   461  C  CB  . CYS   A 1 59  ? 23.916 -0.901  7.887  1.00 12.56 ? 65  CYS   A CB  1 
ATOM   462  S  SG  . CYS   A 1 59  ? 24.649 0.165   6.590  1.00 15.03 ? 65  CYS   A SG  1 
ATOM   463  N  N   . SER   A 1 60  ? 20.632 0.432   6.875  1.00 14.35 ? 66  SER   A N   1 
ATOM   464  C  CA  . SER   A 1 60  ? 19.709 0.425   5.753  1.00 14.62 ? 66  SER   A CA  1 
ATOM   465  C  C   . SER   A 1 60  ? 20.384 0.577   4.392  1.00 14.25 ? 66  SER   A C   1 
ATOM   466  O  O   . SER   A 1 60  ? 19.920 -0.017  3.397  1.00 15.45 ? 66  SER   A O   1 
ATOM   467  C  CB  . SER   A 1 60  ? 18.595 1.456   5.914  1.00 18.98 ? 66  SER   A CB  1 
ATOM   468  O  OG  . SER   A 1 60  ? 19.138 2.758   5.823  1.00 24.44 ? 66  SER   A OG  1 
ATOM   469  N  N   . SER   A 1 61  ? 21.527 1.295   4.335  1.00 12.65 ? 67  SER   A N   1 
ATOM   470  C  CA  . SER   A 1 61  ? 22.247 1.477   3.058  1.00 13.22 ? 67  SER   A CA  1 
ATOM   471  C  C   . SER   A 1 61  ? 22.929 0.226   2.526  1.00 12.78 ? 67  SER   A C   1 
ATOM   472  O  O   . SER   A 1 61  ? 23.481 0.257   1.412  1.00 14.07 ? 67  SER   A O   1 
ATOM   473  C  CB  . SER   A 1 61  ? 23.276 2.593   3.137  1.00 14.57 ? 67  SER   A CB  1 
ATOM   474  O  OG  . SER   A 1 61  ? 24.311 2.324   4.073  1.00 16.09 ? 67  SER   A OG  1 
ATOM   475  N  N   . ARG   A 1 62  ? 22.892 -0.861  3.286  1.00 12.78 ? 68  ARG   A N   1 
ATOM   476  C  CA  . ARG   A 1 62  ? 23.407 -2.160  2.879  1.00 13.47 ? 68  ARG   A CA  1 
ATOM   477  C  C   . ARG   A 1 62  ? 22.324 -3.273  3.053  1.00 15.30 ? 68  ARG   A C   1 
ATOM   478  O  O   . ARG   A 1 62  ? 22.605 -4.438  2.752  1.00 16.47 ? 68  ARG   A O   1 
ATOM   479  C  CB  . ARG   A 1 62  ? 24.648 -2.516  3.713  1.00 14.18 ? 68  ARG   A CB  1 
ATOM   480  C  CG  . ARG   A 1 62  ? 25.855 -1.595  3.475  1.00 14.66 ? 68  ARG   A CG  1 
ATOM   481  C  CD  . ARG   A 1 62  ? 26.472 -1.902  2.108  1.00 16.42 ? 68  ARG   A CD  1 
ATOM   482  N  NE  . ARG   A 1 62  ? 27.655 -1.070  1.834  1.00 18.05 ? 68  ARG   A NE  1 
ATOM   483  C  CZ  . ARG   A 1 62  ? 27.616 0.122   1.249  1.00 18.20 ? 68  ARG   A CZ  1 
ATOM   484  N  NH1 . ARG   A 1 62  ? 26.459 0.646   0.868  1.00 17.30 ? 68  ARG   A NH1 1 
ATOM   485  N  NH2 . ARG   A 1 62  ? 28.743 0.805   1.041  1.00 18.13 ? 68  ARG   A NH2 1 
ATOM   486  N  N   . ARG   A 1 63  ? 21.125 -2.942  3.599  1.00 15.37 ? 69  ARG   A N   1 
ATOM   487  C  CA  . ARG   A 1 63  ? 20.078 -3.931  3.916  1.00 17.07 ? 69  ARG   A CA  1 
ATOM   488  C  C   . ARG   A 1 63  ? 20.679 -5.105  4.733  1.00 17.20 ? 69  ARG   A C   1 
ATOM   489  O  O   . ARG   A 1 63  ? 20.422 -6.274  4.444  1.00 18.49 ? 69  ARG   A O   1 
ATOM   490  C  CB  . ARG   A 1 63  ? 19.411 -4.464  2.646  1.00 20.76 ? 69  ARG   A CB  1 
ATOM   491  C  CG  . ARG   A 1 63  ? 18.610 -3.431  1.925  1.00 26.18 ? 69  ARG   A CG  1 
ATOM   492  C  CD  . ARG   A 1 63  ? 17.525 -4.126  1.109  1.00 28.47 ? 69  ARG   A CD  1 
ATOM   493  N  NE  . ARG   A 1 63  ? 16.855 -3.147  0.272  1.00 31.06 ? 69  ARG   A NE  1 
ATOM   494  C  CZ  . ARG   A 1 63  ? 17.056 -3.019  -1.041 1.00 32.93 ? 69  ARG   A CZ  1 
ATOM   495  N  NH1 . ARG   A 1 63  ? 17.891 -3.842  -1.678 1.00 34.03 ? 69  ARG   A NH1 1 
ATOM   496  N  NH2 . ARG   A 1 63  ? 16.445 -2.058  -1.720 1.00 30.88 ? 69  ARG   A NH2 1 
ATOM   497  N  N   . LYS   A 1 64  ? 21.550 -4.770  5.709  1.00 15.58 ? 70  LYS   A N   1 
ATOM   498  C  CA  . LYS   A 1 64  ? 22.269 -5.803  6.453  1.00 15.51 ? 70  LYS   A CA  1 
ATOM   499  C  C   . LYS   A 1 64  ? 22.456 -5.369  7.888  1.00 14.02 ? 70  LYS   A C   1 
ATOM   500  O  O   . LYS   A 1 64  ? 22.557 -4.180  8.173  1.00 14.09 ? 70  LYS   A O   1 
ATOM   501  C  CB  . LYS   A 1 64  ? 23.711 -5.925  5.883  1.00 19.00 ? 70  LYS   A CB  1 
ATOM   502  C  CG  . LYS   A 1 64  ? 23.908 -6.870  4.699  1.00 27.89 ? 70  LYS   A CG  1 
ATOM   503  C  CD  . LYS   A 1 64  ? 25.403 -6.967  4.382  1.00 35.28 ? 70  LYS   A CD  1 
ATOM   504  C  CE  . LYS   A 1 64  ? 25.768 -8.163  3.525  1.00 42.58 ? 70  LYS   A CE  1 
ATOM   505  N  NZ  . LYS   A 1 64  ? 25.133 -8.118  2.174  1.00 47.41 ? 70  LYS   A NZ  1 
ATOM   506  N  N   . HIS   A 1 65  ? 22.650 -6.361  8.760  1.00 12.87 ? 71  HIS   A N   1 
ATOM   507  C  CA  . HIS   A 1 65  ? 23.007 -6.091  10.148 1.00 12.90 ? 71  HIS   A CA  1 
ATOM   508  C  C   . HIS   A 1 65  ? 24.516 -6.401  10.279 1.00 14.80 ? 71  HIS   A C   1 
ATOM   509  O  O   . HIS   A 1 65  ? 25.025 -7.363  9.682  1.00 15.78 ? 71  HIS   A O   1 
ATOM   510  C  CB  . HIS   A 1 65  ? 22.262 -7.056  11.065 1.00 12.22 ? 71  HIS   A CB  1 
ATOM   511  C  CG  . HIS   A 1 65  ? 20.773 -6.848  11.075 1.00 13.20 ? 71  HIS   A CG  1 
ATOM   512  N  ND1 . HIS   A 1 65  ? 20.138 -6.128  12.081 1.00 17.61 ? 71  HIS   A ND1 1 
ATOM   513  C  CD2 . HIS   A 1 65  ? 19.833 -7.353  10.247 1.00 13.33 ? 71  HIS   A CD2 1 
ATOM   514  C  CE1 . HIS   A 1 65  ? 18.848 -6.211  11.814 1.00 16.14 ? 71  HIS   A CE1 1 
ATOM   515  N  NE2 . HIS   A 1 65  ? 18.619 -6.875  10.701 1.00 16.52 ? 71  HIS   A NE2 1 
ATOM   516  N  N   . TYR   A 1 66  ? 25.221 -5.605  11.094 1.00 13.08 ? 72  TYR   A N   1 
ATOM   517  C  CA  . TYR   A 1 66  ? 26.657 -5.813  11.296 1.00 12.96 ? 72  TYR   A CA  1 
ATOM   518  C  C   . TYR   A 1 66  ? 26.955 -5.882  12.784 1.00 12.64 ? 72  TYR   A C   1 
ATOM   519  O  O   . TYR   A 1 66  ? 26.430 -5.083  13.573 1.00 12.37 ? 72  TYR   A O   1 
ATOM   520  C  CB  . TYR   A 1 66  ? 27.442 -4.588  10.755 1.00 13.38 ? 72  TYR   A CB  1 
ATOM   521  C  CG  . TYR   A 1 66  ? 27.431 -4.467  9.249  1.00 13.89 ? 72  TYR   A CG  1 
ATOM   522  C  CD1 . TYR   A 1 66  ? 28.219 -5.299  8.454  1.00 15.67 ? 72  TYR   A CD1 1 
ATOM   523  C  CD2 . TYR   A 1 66  ? 26.662 -3.499  8.614  1.00 14.92 ? 72  TYR   A CD2 1 
ATOM   524  C  CE1 . TYR   A 1 66  ? 28.200 -5.209  7.054  1.00 16.56 ? 72  TYR   A CE1 1 
ATOM   525  C  CE2 . TYR   A 1 66  ? 26.651 -3.382  7.220  1.00 16.32 ? 72  TYR   A CE2 1 
ATOM   526  C  CZ  . TYR   A 1 66  ? 27.420 -4.242  6.442  1.00 17.76 ? 72  TYR   A CZ  1 
ATOM   527  O  OH  . TYR   A 1 66  ? 27.416 -4.131  5.056  1.00 19.37 ? 72  TYR   A OH  1 
ATOM   528  N  N   . PRO   A 1 67  ? 27.855 -6.787  13.191 1.00 12.40 ? 73  PRO   A N   1 
ATOM   529  C  CA  . PRO   A 1 67  ? 28.279 -6.805  14.606 1.00 12.95 ? 73  PRO   A CA  1 
ATOM   530  C  C   . PRO   A 1 67  ? 29.323 -5.695  14.869 1.00 15.00 ? 73  PRO   A C   1 
ATOM   531  O  O   . PRO   A 1 67  ? 30.219 -5.474  14.025 1.00 17.49 ? 73  PRO   A O   1 
ATOM   532  C  CB  . PRO   A 1 67  ? 28.935 -8.194  14.758 1.00 13.46 ? 73  PRO   A CB  1 
ATOM   533  C  CG  . PRO   A 1 67  ? 29.432 -8.510  13.348 1.00 13.41 ? 73  PRO   A CG  1 
ATOM   534  C  CD  . PRO   A 1 67  ? 28.561 -7.804  12.363 1.00 11.91 ? 73  PRO   A CD  1 
ATOM   535  N  N   . VAL   A 1 68  ? 29.282 -5.043  16.062 1.00 13.14 ? 74  VAL   A N   1 
ATOM   536  C  CA  . VAL   A 1 68  ? 30.202 -3.952  16.326 1.00 14.14 ? 74  VAL   A CA  1 
ATOM   537  C  C   . VAL   A 1 68  ? 30.708 -3.984  17.746 1.00 14.05 ? 74  VAL   A C   1 
ATOM   538  O  O   . VAL   A 1 68  ? 30.008 -4.427  18.656 1.00 14.33 ? 74  VAL   A O   1 
ATOM   539  C  CB  . VAL   A 1 68  ? 29.540 -2.556  16.090 1.00 15.99 ? 74  VAL   A CB  1 
ATOM   540  C  CG1 . VAL   A 1 68  ? 29.492 -2.205  14.593 1.00 17.50 ? 74  VAL   A CG1 1 
ATOM   541  C  CG2 . VAL   A 1 68  ? 28.163 -2.459  16.739 1.00 16.80 ? 74  VAL   A CG2 1 
ATOM   542  N  N   . SER   A 1 69  ? 31.932 -3.442  17.934 1.00 13.13 ? 75  SER   A N   1 
ATOM   543  C  CA  . SER   A 1 69  ? 32.430 -3.136  19.275 1.00 14.42 ? 75  SER   A CA  1 
ATOM   544  C  C   . SER   A 1 69  ? 32.284 -1.595  19.363 1.00 13.58 ? 75  SER   A C   1 
ATOM   545  O  O   . SER   A 1 69  ? 32.676 -0.901  18.416 1.00 13.91 ? 75  SER   A O   1 
ATOM   546  C  CB  . SER   A 1 69  ? 33.903 -3.503  19.391 1.00 18.00 ? 75  SER   A CB  1 
ATOM   547  O  OG  . SER   A 1 69  ? 34.034 -4.917  19.418 1.00 24.10 ? 75  SER   A OG  1 
ATOM   548  N  N   . PHE   A 1 70  ? 31.674 -1.073  20.441 1.00 12.34 ? 76  PHE   A N   1 
ATOM   549  C  CA  . PHE   A 1 70  ? 31.436 0.373   20.523 1.00 12.53 ? 76  PHE   A CA  1 
ATOM   550  C  C   . PHE   A 1 70  ? 31.915 0.995   21.832 1.00 13.79 ? 76  PHE   A C   1 
ATOM   551  O  O   . PHE   A 1 70  ? 31.995 0.330   22.879 1.00 15.59 ? 76  PHE   A O   1 
ATOM   552  C  CB  . PHE   A 1 70  ? 29.946 0.741   20.233 1.00 12.30 ? 76  PHE   A CB  1 
ATOM   553  C  CG  . PHE   A 1 70  ? 28.910 -0.016  21.064 1.00 12.34 ? 76  PHE   A CG  1 
ATOM   554  C  CD1 . PHE   A 1 70  ? 28.391 -1.238  20.628 1.00 12.44 ? 76  PHE   A CD1 1 
ATOM   555  C  CD2 . PHE   A 1 70  ? 28.419 0.516   22.254 1.00 13.76 ? 76  PHE   A CD2 1 
ATOM   556  C  CE1 . PHE   A 1 70  ? 27.451 -1.937  21.416 1.00 14.27 ? 76  PHE   A CE1 1 
ATOM   557  C  CE2 . PHE   A 1 70  ? 27.462 -0.172  23.021 1.00 14.13 ? 76  PHE   A CE2 1 
ATOM   558  C  CZ  . PHE   A 1 70  ? 26.971 -1.384  22.586 1.00 14.68 ? 76  PHE   A CZ  1 
ATOM   559  N  N   . SER   A 1 71  ? 32.330 2.286   21.756 1.00 13.87 ? 77  SER   A N   1 
ATOM   560  C  CA  . SER   A 1 71  ? 32.819 2.985   22.957 1.00 14.41 ? 77  SER   A CA  1 
ATOM   561  C  C   . SER   A 1 71  ? 31.674 3.326   23.935 1.00 14.41 ? 77  SER   A C   1 
ATOM   562  O  O   . SER   A 1 71  ? 30.502 3.290   23.565 1.00 14.84 ? 77  SER   A O   1 
ATOM   563  C  CB  . SER   A 1 71  ? 33.561 4.259   22.558 1.00 15.92 ? 77  SER   A CB  1 
ATOM   564  O  OG  . SER   A 1 71  ? 32.644 5.139   21.915 1.00 17.52 ? 77  SER   A OG  1 
ATOM   565  N  N   . LYS   A 1 72  ? 32.016 3.627   25.199 1.00 14.52 ? 78  LYS   A N   1 
ATOM   566  C  CA  . LYS   A 1 72  ? 31.043 4.036   26.202 1.00 16.10 ? 78  LYS   A CA  1 
ATOM   567  C  C   . LYS   A 1 72  ? 30.446 5.390   25.778 1.00 16.23 ? 78  LYS   A C   1 
ATOM   568  O  O   . LYS   A 1 72  ? 31.126 6.196   25.136 1.00 17.19 ? 78  LYS   A O   1 
ATOM   569  C  CB  . LYS   A 1 72  ? 31.745 4.164   27.559 1.00 18.36 ? 78  LYS   A CB  1 
ATOM   570  C  CG  . LYS   A 1 72  ? 32.194 2.806   28.056 1.00 23.90 ? 78  LYS   A CG  1 
ATOM   571  C  CD  . LYS   A 1 72  ? 32.753 2.892   29.483 1.00 27.78 ? 78  LYS   A CD  1 
ATOM   572  C  CE  . LYS   A 1 72  ? 32.523 1.558   30.127 1.00 33.93 ? 78  LYS   A CE  1 
ATOM   573  N  NZ  . LYS   A 1 72  ? 33.424 1.315   31.286 1.00 38.04 ? 78  LYS   A NZ  1 
ATOM   574  N  N   . PRO   A 1 73  ? 29.200 5.679   26.189 1.00 15.50 ? 79  PRO   A N   1 
ATOM   575  C  CA  . PRO   A 1 73  ? 28.594 6.970   25.817 1.00 16.03 ? 79  PRO   A CA  1 
ATOM   576  C  C   . PRO   A 1 73  ? 29.434 8.141   26.308 1.00 16.28 ? 79  PRO   A C   1 
ATOM   577  O  O   . PRO   A 1 73  ? 29.851 8.167   27.467 1.00 16.77 ? 79  PRO   A O   1 
ATOM   578  C  CB  . PRO   A 1 73  ? 27.225 6.971   26.512 1.00 17.51 ? 79  PRO   A CB  1 
ATOM   579  C  CG  . PRO   A 1 73  ? 27.107 5.659   27.251 1.00 19.23 ? 79  PRO   A CG  1 
ATOM   580  C  CD  . PRO   A 1 73  ? 28.306 4.822   27.006 1.00 16.24 ? 79  PRO   A CD  1 
ATOM   581  N  N   . SER   A 1 74  ? 29.724 9.075   25.396 1.00 16.19 ? 80  SER   A N   1 
ATOM   582  C  CA  . SER   A 1 74  ? 30.587 10.208  25.765 1.00 17.69 ? 80  SER   A CA  1 
ATOM   583  C  C   . SER   A 1 74  ? 30.291 11.439  24.905 1.00 17.36 ? 80  SER   A C   1 
ATOM   584  O  O   . SER   A 1 74  ? 29.423 11.401  24.022 1.00 16.93 ? 80  SER   A O   1 
ATOM   585  C  CB  . SER   A 1 74  ? 32.061 9.786   25.685 1.00 22.20 ? 80  SER   A CB  1 
ATOM   586  O  OG  . SER   A 1 74  ? 32.487 9.631   24.347 1.00 27.27 ? 80  SER   A OG  1 
ATOM   587  N  N   . LEU   A 1 75  ? 30.974 12.572  25.231 1.00 17.04 ? 81  LEU   A N   1 
ATOM   588  C  CA  . LEU   A 1 75  ? 30.836 13.838  24.511 1.00 17.63 ? 81  LEU   A CA  1 
ATOM   589  C  C   . LEU   A 1 75  ? 31.826 13.783  23.371 1.00 17.96 ? 81  LEU   A C   1 
ATOM   590  O  O   . LEU   A 1 75  ? 33.050 13.701  23.619 1.00 18.60 ? 81  LEU   A O   1 
ATOM   591  C  CB  . LEU   A 1 75  ? 31.276 14.972  25.461 1.00 18.90 ? 81  LEU   A CB  1 
ATOM   592  C  CG  . LEU   A 1 75  ? 30.209 15.618  26.264 1.00 23.85 ? 81  LEU   A CG  1 
ATOM   593  C  CD1 . LEU   A 1 75  ? 30.846 16.536  27.337 1.00 26.16 ? 81  LEU   A CD1 1 
ATOM   594  C  CD2 . LEU   A 1 75  ? 29.276 16.448  25.358 1.00 23.84 ? 81  LEU   A CD2 1 
ATOM   595  N  N   . ILE   A 1 76  ? 31.328 13.823  22.124 1.00 17.93 ? 82  ILE   A N   1 
ATOM   596  C  CA  . ILE   A 1 76  ? 32.159 13.693  20.924 1.00 18.79 ? 82  ILE   A CA  1 
ATOM   597  C  C   . ILE   A 1 76  ? 31.912 14.861  19.996 1.00 19.38 ? 82  ILE   A C   1 
ATOM   598  O  O   . ILE   A 1 76  ? 30.754 15.221  19.766 1.00 18.64 ? 82  ILE   A O   1 
ATOM   599  C  CB  . ILE   A 1 76  ? 31.821 12.330  20.223 1.00 19.69 ? 82  ILE   A CB  1 
ATOM   600  C  CG1 . ILE   A 1 76  ? 32.302 11.176  21.130 1.00 22.07 ? 82  ILE   A CG1 1 
ATOM   601  C  CG2 . ILE   A 1 76  ? 32.450 12.238  18.825 1.00 20.71 ? 82  ILE   A CG2 1 
ATOM   602  C  CD1 . ILE   A 1 76  ? 32.071 9.851   20.662 1.00 25.00 ? 82  ILE   A CD1 1 
ATOM   603  N  N   . PHE   A 1 77  ? 32.986 15.463  19.464 1.00 19.60 ? 83  PHE   A N   1 
ATOM   604  C  CA  . PHE   A 1 77  ? 32.832 16.559  18.522 1.00 21.49 ? 83  PHE   A CA  1 
ATOM   605  C  C   . PHE   A 1 77  ? 32.240 16.058  17.198 1.00 21.58 ? 83  PHE   A C   1 
ATOM   606  O  O   . PHE   A 1 77  ? 32.678 15.040  16.661 1.00 22.88 ? 83  PHE   A O   1 
ATOM   607  C  CB  . PHE   A 1 77  ? 34.178 17.272  18.287 1.00 22.93 ? 83  PHE   A CB  1 
ATOM   608  C  CG  . PHE   A 1 77  ? 34.032 18.497  17.425 1.00 25.74 ? 83  PHE   A CG  1 
ATOM   609  C  CD1 . PHE   A 1 77  ? 34.323 18.449  16.076 1.00 27.67 ? 83  PHE   A CD1 1 
ATOM   610  C  CD2 . PHE   A 1 77  ? 33.542 19.673  17.948 1.00 27.67 ? 83  PHE   A CD2 1 
ATOM   611  C  CE1 . PHE   A 1 77  ? 34.159 19.567  15.276 1.00 28.95 ? 83  PHE   A CE1 1 
ATOM   612  C  CE2 . PHE   A 1 77  ? 33.396 20.806  17.142 1.00 29.11 ? 83  PHE   A CE2 1 
ATOM   613  C  CZ  . PHE   A 1 77  ? 33.722 20.741  15.815 1.00 28.76 ? 83  PHE   A CZ  1 
ATOM   614  N  N   . VAL   A 1 78  ? 31.182 16.742  16.712 1.00 19.99 ? 84  VAL   A N   1 
ATOM   615  C  CA  . VAL   A 1 78  ? 30.514 16.399  15.469 1.00 19.84 ? 84  VAL   A CA  1 
ATOM   616  C  C   . VAL   A 1 78  ? 30.531 17.619  14.554 1.00 20.91 ? 84  VAL   A C   1 
ATOM   617  O  O   . VAL   A 1 78  ? 30.016 18.689  14.939 1.00 20.55 ? 84  VAL   A O   1 
ATOM   618  C  CB  . VAL   A 1 78  ? 29.037 15.942  15.728 1.00 20.10 ? 84  VAL   A CB  1 
ATOM   619  C  CG1 . VAL   A 1 78  ? 28.339 15.569  14.416 1.00 20.53 ? 84  VAL   A CG1 1 
ATOM   620  C  CG2 . VAL   A 1 78  ? 28.996 14.759  16.705 1.00 19.89 ? 84  VAL   A CG2 1 
ATOM   621  N  N   . GLU   A 1 79  ? 30.997 17.415  13.317 1.00 20.82 ? 85  GLU   A N   1 
ATOM   622  C  CA  . GLU   A 1 79  ? 31.085 18.473  12.308 1.00 21.81 ? 85  GLU   A CA  1 
ATOM   623  C  C   . GLU   A 1 79  ? 29.713 19.067  12.006 1.00 21.05 ? 85  GLU   A C   1 
ATOM   624  O  O   . GLU   A 1 79  ? 28.697 18.375  12.129 1.00 20.03 ? 85  GLU   A O   1 
ATOM   625  C  CB  . GLU   A 1 79  ? 31.611 17.875  11.001 1.00 26.95 ? 85  GLU   A CB  1 
ATOM   626  C  CG  . GLU   A 1 79  ? 33.098 17.667  10.985 1.00 38.73 ? 85  GLU   A CG  1 
ATOM   627  C  CD  . GLU   A 1 79  ? 33.568 17.881  9.562  1.00 52.66 ? 85  GLU   A CD  1 
ATOM   628  O  OE1 . GLU   A 1 79  ? 34.011 19.007  9.221  1.00 56.26 ? 85  GLU   A OE1 1 
ATOM   629  O  OE2 . GLU   A 1 79  ? 33.462 16.917  8.772  1.00 56.64 ? 85  GLU   A OE2 1 
ATOM   630  N  N   . ALA   A 1 80  ? 29.697 20.328  11.516 1.00 21.20 ? 86  ALA   A N   1 
ATOM   631  C  CA  . ALA   A 1 80  ? 28.443 20.975  11.144 1.00 21.54 ? 86  ALA   A CA  1 
ATOM   632  C  C   . ALA   A 1 80  ? 27.769 20.227  10.007 1.00 21.79 ? 86  ALA   A C   1 
ATOM   633  O  O   . ALA   A 1 80  ? 28.446 19.657  9.144  1.00 22.56 ? 86  ALA   A O   1 
ATOM   634  C  CB  . ALA   A 1 80  ? 28.711 22.420  10.702 1.00 21.79 ? 86  ALA   A CB  1 
ATOM   635  N  N   . SER   A 1 81  ? 26.435 20.205  10.025 1.00 21.45 ? 87  SER   A N   1 
ATOM   636  C  CA  . SER   A 1 81  ? 25.607 19.622  8.970  1.00 21.52 ? 87  SER   A CA  1 
ATOM   637  C  C   . SER   A 1 81  ? 24.488 20.639  8.659  1.00 22.34 ? 87  SER   A C   1 
ATOM   638  O  O   . SER   A 1 81  ? 24.463 21.725  9.258  1.00 22.38 ? 87  SER   A O   1 
ATOM   639  C  CB  . SER   A 1 81  ? 24.979 18.301  9.455  1.00 21.60 ? 87  SER   A CB  1 
ATOM   640  O  OG  . SER   A 1 81  ? 24.047 18.526  10.506 1.00 20.57 ? 87  SER   A OG  1 
ATOM   641  N  N   . GLU   A 1 82  ? 23.562 20.297  7.742  1.00 22.62 ? 88  GLU   A N   1 
ATOM   642  C  CA  . GLU   A 1 82  ? 22.416 21.185  7.493  1.00 24.45 ? 88  GLU   A CA  1 
ATOM   643  C  C   . GLU   A 1 82  ? 21.466 21.221  8.716  1.00 23.16 ? 88  GLU   A C   1 
ATOM   644  O  O   . GLU   A 1 82  ? 20.665 22.140  8.848  1.00 23.65 ? 88  GLU   A O   1 
ATOM   645  C  CB  . GLU   A 1 82  ? 21.651 20.738  6.234  1.00 30.56 ? 88  GLU   A CB  1 
ATOM   646  C  CG  . GLU   A 1 82  ? 21.137 19.314  6.346  1.00 40.98 ? 88  GLU   A CG  1 
ATOM   647  C  CD  . GLU   A 1 82  ? 20.764 18.621  5.050  1.00 56.22 ? 88  GLU   A CD  1 
ATOM   648  O  OE1 . GLU   A 1 82  ? 21.620 18.533  4.137  1.00 60.15 ? 88  GLU   A OE1 1 
ATOM   649  O  OE2 . GLU   A 1 82  ? 19.620 18.117  4.964  1.00 60.75 ? 88  GLU   A OE2 1 
ATOM   650  N  N   . TYR   A 1 83  ? 21.598 20.234  9.645  1.00 21.43 ? 89  TYR   A N   1 
ATOM   651  C  CA  . TYR   A 1 83  ? 20.729 20.146  10.812 1.00 20.35 ? 89  TYR   A CA  1 
ATOM   652  C  C   . TYR   A 1 83  ? 21.268 20.790  12.074 1.00 19.84 ? 89  TYR   A C   1 
ATOM   653  O  O   . TYR   A 1 83  ? 20.477 21.187  12.914 1.00 20.05 ? 89  TYR   A O   1 
ATOM   654  C  CB  . TYR   A 1 83  ? 20.382 18.684  11.103 1.00 19.78 ? 89  TYR   A CB  1 
ATOM   655  C  CG  . TYR   A 1 83  ? 19.822 17.934  9.912  1.00 19.80 ? 89  TYR   A CG  1 
ATOM   656  C  CD1 . TYR   A 1 83  ? 20.629 17.108  9.142  1.00 21.42 ? 89  TYR   A CD1 1 
ATOM   657  C  CD2 . TYR   A 1 83  ? 18.477 18.018  9.584  1.00 20.91 ? 89  TYR   A CD2 1 
ATOM   658  C  CE1 . TYR   A 1 83  ? 20.097 16.349  8.098  1.00 22.41 ? 89  TYR   A CE1 1 
ATOM   659  C  CE2 . TYR   A 1 83  ? 17.950 17.320  8.499  1.00 21.91 ? 89  TYR   A CE2 1 
ATOM   660  C  CZ  . TYR   A 1 83  ? 18.761 16.480  7.766  1.00 23.30 ? 89  TYR   A CZ  1 
ATOM   661  O  OH  . TYR   A 1 83  ? 18.244 15.776  6.693  1.00 25.02 ? 89  TYR   A OH  1 
ATOM   662  N  N   . TYR   A 1 84  ? 22.598 20.837  12.245 1.00 19.11 ? 90  TYR   A N   1 
ATOM   663  C  CA  . TYR   A 1 84  ? 23.182 21.407  13.469 1.00 18.21 ? 90  TYR   A CA  1 
ATOM   664  C  C   . TYR   A 1 84  ? 24.492 22.133  13.154 1.00 19.91 ? 90  TYR   A C   1 
ATOM   665  O  O   . TYR   A 1 84  ? 25.238 21.707  12.259 1.00 20.01 ? 90  TYR   A O   1 
ATOM   666  C  CB  . TYR   A 1 84  ? 23.578 20.278  14.469 1.00 16.83 ? 90  TYR   A CB  1 
ATOM   667  C  CG  . TYR   A 1 84  ? 22.463 19.386  14.961 1.00 15.04 ? 90  TYR   A CG  1 
ATOM   668  C  CD1 . TYR   A 1 84  ? 21.574 19.822  15.935 1.00 15.02 ? 90  TYR   A CD1 1 
ATOM   669  C  CD2 . TYR   A 1 84  ? 22.337 18.083  14.499 1.00 15.66 ? 90  TYR   A CD2 1 
ATOM   670  C  CE1 . TYR   A 1 84  ? 20.596 18.977  16.453 1.00 15.09 ? 90  TYR   A CE1 1 
ATOM   671  C  CE2 . TYR   A 1 84  ? 21.358 17.226  15.006 1.00 15.29 ? 90  TYR   A CE2 1 
ATOM   672  C  CZ  . TYR   A 1 84  ? 20.508 17.672  15.999 1.00 15.19 ? 90  TYR   A CZ  1 
ATOM   673  O  OH  . TYR   A 1 84  ? 19.511 16.854  16.493 1.00 14.59 ? 90  TYR   A OH  1 
ATOM   674  N  N   . PRO   A 1 85  ? 24.856 23.154  13.949 1.00 21.17 ? 91  PRO   A N   1 
ATOM   675  C  CA  . PRO   A 1 85  ? 26.210 23.731  13.793 1.00 21.55 ? 91  PRO   A CA  1 
ATOM   676  C  C   . PRO   A 1 85  ? 27.237 22.726  14.364 1.00 21.67 ? 91  PRO   A C   1 
ATOM   677  O  O   . PRO   A 1 85  ? 26.856 21.738  15.034 1.00 21.64 ? 91  PRO   A O   1 
ATOM   678  C  CB  . PRO   A 1 85  ? 26.150 24.987  14.672 1.00 22.14 ? 91  PRO   A CB  1 
ATOM   679  C  CG  . PRO   A 1 85  ? 25.174 24.639  15.745 1.00 23.47 ? 91  PRO   A CG  1 
ATOM   680  C  CD  . PRO   A 1 85  ? 24.126 23.754  15.089 1.00 21.42 ? 91  PRO   A CD  1 
ATOM   681  N  N   . ALA   A 1 86  ? 28.551 22.990  14.183 1.00 21.61 ? 92  ALA   A N   1 
ATOM   682  C  CA  . ALA   A 1 86  ? 29.589 22.130  14.778 1.00 22.07 ? 92  ALA   A CA  1 
ATOM   683  C  C   . ALA   A 1 86  ? 29.428 22.187  16.316 1.00 21.35 ? 92  ALA   A C   1 
ATOM   684  O  O   . ALA   A 1 86  ? 29.211 23.273  16.859 1.00 20.79 ? 92  ALA   A O   1 
ATOM   685  C  CB  . ALA   A 1 86  ? 30.971 22.646  14.387 1.00 22.61 ? 92  ALA   A CB  1 
ATOM   686  N  N   . ARG   A 1 87  ? 29.398 21.022  16.985 1.00 20.35 ? 93  ARG   A N   1 
ATOM   687  C  CA  . ARG   A 1 87  ? 29.140 21.006  18.430 1.00 19.56 ? 93  ARG   A CA  1 
ATOM   688  C  C   . ARG   A 1 87  ? 29.591 19.687  19.064 1.00 19.76 ? 93  ARG   A C   1 
ATOM   689  O  O   . ARG   A 1 87  ? 29.926 18.749  18.337 1.00 20.77 ? 93  ARG   A O   1 
ATOM   690  C  CB  . ARG   A 1 87  ? 27.616 21.188  18.656 1.00 19.83 ? 93  ARG   A CB  1 
ATOM   691  C  CG  . ARG   A 1 87  ? 26.829 19.884  18.328 1.00 20.54 ? 93  ARG   A CG  1 
ATOM   692  C  CD  . ARG   A 1 87  ? 25.429 20.082  17.826 1.00 21.53 ? 93  ARG   A CD  1 
ATOM   693  N  NE  . ARG   A 1 87  ? 24.519 18.993  18.205 1.00 20.23 ? 93  ARG   A NE  1 
ATOM   694  C  CZ  . ARG   A 1 87  ? 24.481 17.808  17.612 1.00 19.57 ? 93  ARG   A CZ  1 
ATOM   695  N  NH1 . ARG   A 1 87  ? 23.579 16.899  17.984 1.00 18.48 ? 93  ARG   A NH1 1 
ATOM   696  N  NH2 . ARG   A 1 87  ? 25.343 17.516  16.641 1.00 18.77 ? 93  ARG   A NH2 1 
ATOM   697  N  N   . TYR   A 1 88  ? 29.555 19.598  20.402 1.00 18.59 ? 94  TYR   A N   1 
ATOM   698  C  CA  . TYR   A 1 88  ? 29.778 18.311  21.056 1.00 18.73 ? 94  TYR   A CA  1 
ATOM   699  C  C   . TYR   A 1 88  ? 28.430 17.647  21.224 1.00 18.29 ? 94  TYR   A C   1 
ATOM   700  O  O   . TYR   A 1 88  ? 27.500 18.250  21.764 1.00 19.45 ? 94  TYR   A O   1 
ATOM   701  C  CB  . TYR   A 1 88  ? 30.428 18.450  22.441 1.00 19.15 ? 94  TYR   A CB  1 
ATOM   702  C  CG  . TYR   A 1 88  ? 31.870 18.884  22.350 1.00 21.00 ? 94  TYR   A CG  1 
ATOM   703  C  CD1 . TYR   A 1 88  ? 32.890 17.953  22.234 1.00 22.31 ? 94  TYR   A CD1 1 
ATOM   704  C  CD2 . TYR   A 1 88  ? 32.208 20.230  22.314 1.00 23.35 ? 94  TYR   A CD2 1 
ATOM   705  C  CE1 . TYR   A 1 88  ? 34.220 18.350  22.127 1.00 24.94 ? 94  TYR   A CE1 1 
ATOM   706  C  CE2 . TYR   A 1 88  ? 33.527 20.640  22.195 1.00 25.00 ? 94  TYR   A CE2 1 
ATOM   707  C  CZ  . TYR   A 1 88  ? 34.535 19.696  22.111 1.00 26.72 ? 94  TYR   A CZ  1 
ATOM   708  O  OH  . TYR   A 1 88  ? 35.843 20.126  22.031 1.00 30.32 ? 94  TYR   A OH  1 
ATOM   709  N  N   . GLN   A 1 89  ? 28.302 16.434  20.714 1.00 16.61 ? 95  GLN   A N   1 
ATOM   710  C  CA  . GLN   A 1 89  ? 27.093 15.652  20.898 1.00 14.98 ? 95  GLN   A CA  1 
ATOM   711  C  C   . GLN   A 1 89  ? 27.364 14.748  22.096 1.00 15.04 ? 95  GLN   A C   1 
ATOM   712  O  O   . GLN   A 1 89  ? 28.416 14.091  22.148 1.00 16.31 ? 95  GLN   A O   1 
ATOM   713  C  CB  . GLN   A 1 89  ? 26.732 14.831  19.647 1.00 15.22 ? 95  GLN   A CB  1 
ATOM   714  C  CG  . GLN   A 1 89  ? 25.505 13.924  19.888 1.00 14.35 ? 95  GLN   A CG  1 
ATOM   715  C  CD  . GLN   A 1 89  ? 24.865 13.451  18.602 1.00 15.82 ? 95  GLN   A CD  1 
ATOM   716  O  OE1 . GLN   A 1 89  ? 24.756 14.221  17.627 1.00 15.34 ? 95  GLN   A OE1 1 
ATOM   717  N  NE2 . GLN   A 1 89  ? 24.351 12.187  18.604 1.00 13.96 ? 95  GLN   A NE2 1 
ATOM   718  N  N   . SER   A 1 90  ? 26.468 14.752  23.076 1.00 13.33 ? 96  SER   A N   1 
ATOM   719  C  CA  . SER   A 1 90  ? 26.653 13.938  24.268 1.00 14.15 ? 96  SER   A CA  1 
ATOM   720  C  C   . SER   A 1 90  ? 25.993 12.562  24.139 1.00 14.64 ? 96  SER   A C   1 
ATOM   721  O  O   . SER   A 1 90  ? 25.158 12.349  23.237 1.00 15.45 ? 96  SER   A O   1 
ATOM   722  C  CB  . SER   A 1 90  ? 26.086 14.660  25.483 1.00 15.83 ? 96  SER   A CB  1 
ATOM   723  O  OG  . SER   A 1 90  ? 24.696 14.911  25.315 1.00 17.69 ? 96  SER   A OG  1 
ATOM   724  N  N   . HIS   A 1 91  ? 26.380 11.623  25.035 1.00 14.43 ? 97  HIS   A N   1 
ATOM   725  C  CA  . HIS   A 1 91  ? 25.804 10.270  25.095 1.00 13.99 ? 97  HIS   A CA  1 
ATOM   726  C  C   . HIS   A 1 91  ? 25.949 9.517   23.758 1.00 13.34 ? 97  HIS   A C   1 
ATOM   727  O  O   . HIS   A 1 91  ? 25.097 8.686   23.440 1.00 13.33 ? 97  HIS   A O   1 
ATOM   728  C  CB  . HIS   A 1 91  ? 24.319 10.330  25.538 1.00 15.61 ? 97  HIS   A CB  1 
ATOM   729  C  CG  . HIS   A 1 91  ? 24.137 10.952  26.891 1.00 16.58 ? 97  HIS   A CG  1 
ATOM   730  N  ND1 . HIS   A 1 91  ? 24.061 10.177  28.040 1.00 20.19 ? 97  HIS   A ND1 1 
ATOM   731  C  CD2 . HIS   A 1 91  ? 24.032 12.260  27.237 1.00 17.71 ? 97  HIS   A CD2 1 
ATOM   732  C  CE1 . HIS   A 1 91  ? 23.916 11.037  29.050 1.00 20.66 ? 97  HIS   A CE1 1 
ATOM   733  N  NE2 . HIS   A 1 91  ? 23.871 12.301  28.611 1.00 19.53 ? 97  HIS   A NE2 1 
ATOM   734  N  N   . LEU   A 1 92  ? 27.060 9.778   23.025 1.00 13.60 ? 98  LEU   A N   1 
ATOM   735  C  CA  . LEU   A 1 92  ? 27.327 9.187   21.708 1.00 13.32 ? 98  LEU   A CA  1 
ATOM   736  C  C   . LEU   A 1 92  ? 28.363 8.064   21.854 1.00 13.51 ? 98  LEU   A C   1 
ATOM   737  O  O   . LEU   A 1 92  ? 29.335 8.198   22.600 1.00 13.40 ? 98  LEU   A O   1 
ATOM   738  C  CB  . LEU   A 1 92  ? 27.881 10.269  20.755 1.00 13.50 ? 98  LEU   A CB  1 
ATOM   739  C  CG  . LEU   A 1 92  ? 28.012 9.900   19.273 1.00 15.70 ? 98  LEU   A CG  1 
ATOM   740  C  CD1 . LEU   A 1 92  ? 26.646 9.492   18.665 1.00 16.64 ? 98  LEU   A CD1 1 
ATOM   741  C  CD2 . LEU   A 1 92  ? 28.610 11.102  18.473 1.00 17.24 ? 98  LEU   A CD2 1 
ATOM   742  N  N   . MET   A 1 93  ? 28.137 6.979   21.115 1.00 12.69 ? 99  MET   A N   1 
ATOM   743  C  CA  . MET   A 1 93  ? 29.004 5.799   21.151 1.00 12.59 ? 99  MET   A CA  1 
ATOM   744  C  C   . MET   A 1 93  ? 29.509 5.527   19.755 1.00 13.68 ? 99  MET   A C   1 
ATOM   745  O  O   . MET   A 1 93  ? 28.684 5.472   18.842 1.00 13.83 ? 99  MET   A O   1 
ATOM   746  C  CB  . MET   A 1 93  ? 28.178 4.592   21.608 1.00 12.94 ? 99  MET   A CB  1 
ATOM   747  C  CG  . MET   A 1 93  ? 27.672 4.759   23.057 1.00 15.93 ? 99  MET   A CG  1 
ATOM   748  S  SD  . MET   A 1 93  ? 26.520 3.451   23.551 1.00 17.73 ? 99  MET   A SD  1 
ATOM   749  C  CE  . MET   A 1 93  ? 25.172 3.726   22.385 1.00 19.10 ? 99  MET   A CE  1 
ATOM   750  N  N   . LEU   A 1 94  ? 30.832 5.417   19.554 1.00 13.07 ? 100 LEU   A N   1 
ATOM   751  C  CA  . LEU   A 1 94  ? 31.354 5.183   18.207 1.00 13.50 ? 100 LEU   A CA  1 
ATOM   752  C  C   . LEU   A 1 94  ? 31.799 3.743   18.029 1.00 13.82 ? 100 LEU   A C   1 
ATOM   753  O  O   . LEU   A 1 94  ? 32.294 3.091   18.971 1.00 13.69 ? 100 LEU   A O   1 
ATOM   754  C  CB  . LEU   A 1 94  ? 32.622 6.035   17.947 1.00 15.23 ? 100 LEU   A CB  1 
ATOM   755  C  CG  . LEU   A 1 94  ? 32.422 7.531   17.932 1.00 18.50 ? 100 LEU   A CG  1 
ATOM   756  C  CD1 . LEU   A 1 94  ? 33.698 8.253   17.398 1.00 20.15 ? 100 LEU   A CD1 1 
ATOM   757  C  CD2 . LEU   A 1 94  ? 31.229 7.949   17.082 1.00 19.31 ? 100 LEU   A CD2 1 
ATOM   758  N  N   . ALA   A 1 95  ? 31.739 3.315   16.774 1.00 12.78 ? 101 ALA   A N   1 
ATOM   759  C  CA  . ALA   A 1 95  ? 32.206 1.988   16.373 1.00 12.63 ? 101 ALA   A CA  1 
ATOM   760  C  C   . ALA   A 1 95  ? 32.746 2.074   14.940 1.00 12.78 ? 101 ALA   A C   1 
ATOM   761  O  O   . ALA   A 1 95  ? 32.396 2.993   14.197 1.00 12.81 ? 101 ALA   A O   1 
ATOM   762  C  CB  . ALA   A 1 95  ? 31.041 1.004   16.384 1.00 13.62 ? 101 ALA   A CB  1 
ATOM   763  N  N   . VAL   A 1 96  ? 33.576 1.089   14.553 1.00 11.93 ? 102 VAL   A N   1 
ATOM   764  C  CA  . VAL   A 1 96  ? 34.017 1.017   13.176 1.00 11.92 ? 102 VAL   A CA  1 
ATOM   765  C  C   . VAL   A 1 96  ? 32.918 0.275   12.384 1.00 14.23 ? 102 VAL   A C   1 
ATOM   766  O  O   . VAL   A 1 96  ? 32.554 -0.857  12.712 1.00 14.98 ? 102 VAL   A O   1 
ATOM   767  C  CB  . VAL   A 1 96  ? 35.362 0.272   13.128 1.00 13.11 ? 102 VAL   A CB  1 
ATOM   768  C  CG1 . VAL   A 1 96  ? 35.802 0.045   11.677 1.00 13.44 ? 102 VAL   A CG1 1 
ATOM   769  C  CG2 . VAL   A 1 96  ? 36.394 1.073   13.909 1.00 15.17 ? 102 VAL   A CG2 1 
ATOM   770  N  N   . GLY   A 1 97  ? 32.380 0.950   11.378 1.00 14.75 ? 103 GLY   A N   1 
ATOM   771  C  CA  . GLY   A 1 97  ? 31.339 0.368   10.538 1.00 15.14 ? 103 GLY   A CA  1 
ATOM   772  C  C   . GLY   A 1 97  ? 30.819 1.363   9.520  1.00 14.58 ? 103 GLY   A C   1 
ATOM   773  O  O   . GLY   A 1 97  ? 31.116 2.563   9.580  1.00 14.78 ? 103 GLY   A O   1 
ATOM   774  N  N   . HIS   A 1 98  ? 30.079 0.856   8.535  1.00 13.74 ? 104 HIS   A N   1 
ATOM   775  C  CA  . HIS   A 1 98  ? 29.537 1.682   7.479  1.00 13.51 ? 104 HIS   A CA  1 
ATOM   776  C  C   . HIS   A 1 98  ? 28.264 2.417   7.875  1.00 13.50 ? 104 HIS   A C   1 
ATOM   777  O  O   . HIS   A 1 98  ? 27.367 1.850   8.491  1.00 13.16 ? 104 HIS   A O   1 
ATOM   778  C  CB  . HIS   A 1 98  ? 29.273 0.828   6.220  1.00 13.54 ? 104 HIS   A CB  1 
ATOM   779  C  CG  . HIS   A 1 98  ? 28.695 1.632   5.085  1.00 13.53 ? 104 HIS   A CG  1 
ATOM   780  N  ND1 . HIS   A 1 98  ? 29.456 2.577   4.407  1.00 14.89 ? 104 HIS   A ND1 1 
ATOM   781  C  CD2 . HIS   A 1 98  ? 27.421 1.675   4.611  1.00 15.01 ? 104 HIS   A CD2 1 
ATOM   782  C  CE1 . HIS   A 1 98  ? 28.635 3.139   3.517  1.00 16.06 ? 104 HIS   A CE1 1 
ATOM   783  N  NE2 . HIS   A 1 98  ? 27.395 2.619   3.607  1.00 15.86 ? 104 HIS   A NE2 1 
ATOM   784  N  N   . SER   A 1 99  ? 28.128 3.643   7.403  1.00 13.68 ? 105 SER   A N   1 
ATOM   785  C  CA  . SER   A 1 99  ? 26.901 4.406   7.521  1.00 14.72 ? 105 SER   A CA  1 
ATOM   786  C  C   . SER   A 1 99  ? 26.909 5.545   6.477  1.00 16.38 ? 105 SER   A C   1 
ATOM   787  O  O   . SER   A 1 99  ? 27.985 5.975   6.044  1.00 18.49 ? 105 SER   A O   1 
ATOM   788  C  CB  . SER   A 1 99  ? 26.712 4.973   8.920  1.00 17.34 ? 105 SER   A CB  1 
ATOM   789  O  OG  . SER   A 1 99  ? 27.605 6.051   9.102  1.00 21.58 ? 105 SER   A OG  1 
ATOM   790  N  N   . GLU   A 1 100 ? 25.718 5.927   6.043  1.00 15.51 ? 106 GLU   A N   1 
ATOM   791  C  CA  . GLU   A 1 100 ? 25.377 7.051   5.178  1.00 15.91 ? 106 GLU   A CA  1 
ATOM   792  C  C   . GLU   A 1 100 ? 24.262 7.865   5.911  1.00 16.82 ? 106 GLU   A C   1 
ATOM   793  O  O   . GLU   A 1 100 ? 23.627 7.350   6.841  1.00 17.32 ? 106 GLU   A O   1 
ATOM   794  C  CB  . GLU   A 1 100 ? 24.898 6.539   3.800  1.00 18.00 ? 106 GLU   A CB  1 
ATOM   795  C  CG  . GLU   A 1 100 ? 26.032 5.848   3.079  1.00 20.88 ? 106 GLU   A CG  1 
ATOM   796  C  CD  . GLU   A 1 100 ? 25.656 5.119   1.802  1.00 22.85 ? 106 GLU   A CD  1 
ATOM   797  O  OE1 . GLU   A 1 100 ? 24.843 5.665   1.016  1.00 22.81 ? 106 GLU   A OE1 1 
ATOM   798  O  OE2 . GLU   A 1 100 ? 26.205 4.016   1.569  1.00 21.50 ? 106 GLU   A OE2 1 
ATOM   799  N  N   . PRO   A 1 101 ? 24.018 9.157   5.568  1.00 18.10 ? 107 PRO   A N   1 
ATOM   800  C  CA  . PRO   A 1 101 ? 23.013 9.953   6.345  1.00 17.99 ? 107 PRO   A CA  1 
ATOM   801  C  C   . PRO   A 1 101 ? 21.643 9.288   6.575  1.00 18.04 ? 107 PRO   A C   1 
ATOM   802  O  O   . PRO   A 1 101 ? 21.087 9.312   7.694  1.00 18.40 ? 107 PRO   A O   1 
ATOM   803  C  CB  . PRO   A 1 101 ? 22.882 11.243  5.520  1.00 18.64 ? 107 PRO   A CB  1 
ATOM   804  C  CG  . PRO   A 1 101 ? 24.275 11.398  4.882  1.00 19.52 ? 107 PRO   A CG  1 
ATOM   805  C  CD  . PRO   A 1 101 ? 24.714 9.966   4.547  1.00 17.98 ? 107 PRO   A CD  1 
ATOM   806  N  N   . GLY   A 1 102 ? 21.131 8.661   5.526  1.00 17.27 ? 108 GLY   A N   1 
ATOM   807  C  CA  . GLY   A 1 102 ? 19.861 7.943   5.566  1.00 16.26 ? 108 GLY   A CA  1 
ATOM   808  C  C   . GLY   A 1 102 ? 19.841 6.759   6.515  1.00 14.81 ? 108 GLY   A C   1 
ATOM   809  O  O   . GLY   A 1 102 ? 18.781 6.194   6.774  1.00 15.72 ? 108 GLY   A O   1 
ATOM   810  N  N   . ASP   A 1 103 ? 21.018 6.343   7.026  1.00 14.14 ? 109 ASP   A N   1 
ATOM   811  C  CA  . ASP   A 1 103 ? 21.061 5.237   7.967  1.00 12.57 ? 109 ASP   A CA  1 
ATOM   812  C  C   . ASP   A 1 103 ? 20.642 5.631   9.387  1.00 12.28 ? 109 ASP   A C   1 
ATOM   813  O  O   . ASP   A 1 103 ? 20.440 4.736   10.224 1.00 12.19 ? 109 ASP   A O   1 
ATOM   814  C  CB  . ASP   A 1 103 ? 22.453 4.594   8.026  1.00 13.77 ? 109 ASP   A CB  1 
ATOM   815  C  CG  . ASP   A 1 103 ? 22.721 3.767   6.797  1.00 15.45 ? 109 ASP   A CG  1 
ATOM   816  O  OD1 . ASP   A 1 103 ? 21.778 3.111   6.314  1.00 15.62 ? 109 ASP   A OD1 1 
ATOM   817  O  OD2 . ASP   A 1 103 ? 23.887 3.750   6.341  1.00 16.14 ? 109 ASP   A OD2 1 
ATOM   818  N  N   . CYS   A 1 104 ? 20.517 6.949   9.680  1.00 12.30 ? 110 CYS   A N   1 
ATOM   819  C  CA  . CYS   A 1 104 ? 20.126 7.381   11.032 1.00 12.82 ? 110 CYS   A CA  1 
ATOM   820  C  C   . CYS   A 1 104 ? 18.786 6.771   11.403 1.00 12.81 ? 110 CYS   A C   1 
ATOM   821  O  O   . CYS   A 1 104 ? 17.886 6.705   10.545 1.00 13.48 ? 110 CYS   A O   1 
ATOM   822  C  CB  . CYS   A 1 104 ? 20.078 8.903   11.140 1.00 13.51 ? 110 CYS   A CB  1 
ATOM   823  S  SG  . CYS   A 1 104 ? 21.713 9.696   11.083 1.00 15.81 ? 110 CYS   A SG  1 
ATOM   824  N  N   . GLY   A 1 105 ? 18.700 6.276   12.627 1.00 11.03 ? 111 GLY   A N   1 
ATOM   825  C  CA  . GLY   A 1 105 ? 17.475 5.636   13.096 1.00 12.69 ? 111 GLY   A CA  1 
ATOM   826  C  C   . GLY   A 1 105 ? 17.588 4.117   13.166 1.00 13.30 ? 111 GLY   A C   1 
ATOM   827  O  O   . GLY   A 1 105 ? 16.747 3.479   13.800 1.00 13.56 ? 111 GLY   A O   1 
ATOM   828  N  N   . GLY   A 1 106 ? 18.613 3.531   12.522 1.00 13.13 ? 112 GLY   A N   1 
ATOM   829  C  CA  . GLY   A 1 106 ? 18.838 2.079   12.584 1.00 12.08 ? 112 GLY   A CA  1 
ATOM   830  C  C   . GLY   A 1 106 ? 19.151 1.689   14.022 1.00 11.65 ? 112 GLY   A C   1 
ATOM   831  O  O   . GLY   A 1 106 ? 19.905 2.395   14.692 1.00 12.11 ? 112 GLY   A O   1 
ATOM   832  N  N   . ILE   A 1 107 ? 18.536 0.617   14.501 1.00 10.93 ? 113 ILE   A N   1 
ATOM   833  C  CA  . ILE   A 1 107 ? 18.720 0.200   15.871 1.00 10.87 ? 113 ILE   A CA  1 
ATOM   834  C  C   . ILE   A 1 107 ? 20.016 -0.574  16.097 1.00 11.17 ? 113 ILE   A C   1 
ATOM   835  O  O   . ILE   A 1 107 ? 20.400 -1.447  15.285 1.00 12.35 ? 113 ILE   A O   1 
ATOM   836  C  CB  . ILE   A 1 107 ? 17.468 -0.620  16.314 1.00 12.46 ? 113 ILE   A CB  1 
ATOM   837  C  CG1 . ILE   A 1 107 ? 16.288 0.334   16.587 1.00 13.90 ? 113 ILE   A CG1 1 
ATOM   838  C  CG2 . ILE   A 1 107 ? 17.725 -1.552  17.501 1.00 13.76 ? 113 ILE   A CG2 1 
ATOM   839  C  CD1 . ILE   A 1 107 ? 14.957 -0.438  16.931 1.00 15.78 ? 113 ILE   A CD1 1 
ATOM   840  N  N   . LEU   A 1 108 ? 20.641 -0.277  17.253 1.00 10.53 ? 114 LEU   A N   1 
ATOM   841  C  CA  . LEU   A 1 108 ? 21.781 -1.049  17.776 1.00 10.15 ? 114 LEU   A CA  1 
ATOM   842  C  C   . LEU   A 1 108 ? 21.187 -1.860  18.954 1.00 11.52 ? 114 LEU   A C   1 
ATOM   843  O  O   . LEU   A 1 108 ? 20.536 -1.276  19.827 1.00 11.93 ? 114 LEU   A O   1 
ATOM   844  C  CB  . LEU   A 1 108 ? 22.873 -0.092  18.316 1.00 11.32 ? 114 LEU   A CB  1 
ATOM   845  C  CG  . LEU   A 1 108 ? 24.011 -0.782  19.124 1.00 12.01 ? 114 LEU   A CG  1 
ATOM   846  C  CD1 . LEU   A 1 108 ? 24.824 -1.706  18.220 1.00 12.32 ? 114 LEU   A CD1 1 
ATOM   847  C  CD2 . LEU   A 1 108 ? 24.953 0.278   19.748 1.00 14.47 ? 114 LEU   A CD2 1 
ATOM   848  N  N   . ARG   A 1 109 ? 21.391 -3.194  18.946 1.00 11.52 ? 115 ARG   A N   1 
ATOM   849  C  CA  . ARG   A 1 109 ? 20.862 -4.056  20.007 1.00 12.80 ? 115 ARG   A CA  1 
ATOM   850  C  C   . ARG   A 1 109 ? 21.968 -4.954  20.540 1.00 13.10 ? 115 ARG   A C   1 
ATOM   851  O  O   . ARG   A 1 109 ? 22.838 -5.424  19.803 1.00 13.19 ? 115 ARG   A O   1 
ATOM   852  C  CB  . ARG   A 1 109 ? 19.815 -5.061  19.427 1.00 16.32 ? 115 ARG   A CB  1 
ATOM   853  C  CG  . ARG   A 1 109 ? 18.644 -4.498  18.684 1.00 23.19 ? 115 ARG   A CG  1 
ATOM   854  C  CD  . ARG   A 1 109 ? 17.747 -5.642  18.191 1.00 24.91 ? 115 ARG   A CD  1 
ATOM   855  N  NE  . ARG   A 1 109 ? 17.106 -6.248  19.351 1.00 25.99 ? 115 ARG   A NE  1 
ATOM   856  C  CZ  . ARG   A 1 109 ? 15.932 -5.861  19.839 1.00 25.04 ? 115 ARG   A CZ  1 
ATOM   857  N  NH1 . ARG   A 1 109 ? 15.205 -4.965  19.197 1.00 21.79 ? 115 ARG   A NH1 1 
ATOM   858  N  NH2 . ARG   A 1 109 ? 15.471 -6.386  20.961 1.00 22.74 ? 115 ARG   A NH2 1 
ATOM   859  N  N   . CYS   A 1 110 ? 21.865 -5.268  21.825 1.00 12.49 ? 116 CYS   A N   1 
ATOM   860  C  CA  . CYS   A 1 110 ? 22.715 -6.303  22.428 1.00 13.43 ? 116 CYS   A CA  1 
ATOM   861  C  C   . CYS   A 1 110 ? 21.753 -7.436  22.893 1.00 15.15 ? 116 CYS   A C   1 
ATOM   862  O  O   . CYS   A 1 110 ? 20.525 -7.370  22.672 1.00 16.49 ? 116 CYS   A O   1 
ATOM   863  C  CB  . CYS   A 1 110 ? 23.474 -5.710  23.612 1.00 14.81 ? 116 CYS   A CB  1 
ATOM   864  S  SG  . CYS   A 1 110 ? 22.376 -5.200  24.975 1.00 13.94 ? 116 CYS   A SG  1 
ATOM   865  N  N   . GLN   A 1 111 ? 22.272 -8.458  23.606 1.00 15.54 ? 117 GLN   A N   1 
ATOM   866  C  CA  . GLN   A 1 111 ? 21.426 -9.563  24.086 1.00 17.35 ? 117 GLN   A CA  1 
ATOM   867  C  C   . GLN   A 1 111 ? 20.323 -9.106  25.079 1.00 17.41 ? 117 GLN   A C   1 
ATOM   868  O  O   . GLN   A 1 111 ? 19.388 -9.879  25.352 1.00 18.08 ? 117 GLN   A O   1 
ATOM   869  C  CB  . GLN   A 1 111 ? 22.298 -10.669 24.733 1.00 20.03 ? 117 GLN   A CB  1 
ATOM   870  C  CG  . GLN   A 1 111 ? 22.931 -10.202 26.051 1.00 26.86 ? 117 GLN   A CG  1 
ATOM   871  C  CD  . GLN   A 1 111 ? 23.959 -11.166 26.594 1.00 36.56 ? 117 GLN   A CD  1 
ATOM   872  O  OE1 . GLN   A 1 111 ? 25.186 -10.941 26.527 1.00 39.22 ? 117 GLN   A OE1 1 
ATOM   873  N  NE2 . GLN   A 1 111 ? 23.462 -12.249 27.170 1.00 37.03 ? 117 GLN   A NE2 1 
ATOM   874  N  N   . HIS   A 1 112 ? 20.434 -7.903  25.644 1.00 15.74 ? 118 HIS   A N   1 
ATOM   875  C  CA  . HIS   A 1 112 ? 19.471 -7.397  26.653 1.00 16.47 ? 118 HIS   A CA  1 
ATOM   876  C  C   . HIS   A 1 112 ? 18.345 -6.555  26.084 1.00 15.77 ? 118 HIS   A C   1 
ATOM   877  O  O   . HIS   A 1 112 ? 17.345 -6.304  26.773 1.00 15.61 ? 118 HIS   A O   1 
ATOM   878  C  CB  . HIS   A 1 112 ? 20.181 -6.610  27.769 1.00 16.59 ? 118 HIS   A CB  1 
ATOM   879  C  CG  . HIS   A 1 112 ? 21.308 -7.368  28.401 1.00 18.64 ? 118 HIS   A CG  1 
ATOM   880  N  ND1 . HIS   A 1 112 ? 22.636 -7.022  28.176 1.00 20.73 ? 118 HIS   A ND1 1 
ATOM   881  C  CD2 . HIS   A 1 112 ? 21.276 -8.438  29.246 1.00 20.78 ? 118 HIS   A CD2 1 
ATOM   882  C  CE1 . HIS   A 1 112 ? 23.367 -7.892  28.857 1.00 21.77 ? 118 HIS   A CE1 1 
ATOM   883  N  NE2 . HIS   A 1 112 ? 22.597 -8.772  29.506 1.00 21.73 ? 118 HIS   A NE2 1 
ATOM   884  N  N   . GLY   A 1 113 ? 18.537 -6.074  24.847 1.00 14.65 ? 119 GLY   A N   1 
ATOM   885  C  CA  . GLY   A 1 113 ? 17.523 -5.251  24.224 1.00 14.69 ? 119 GLY   A CA  1 
ATOM   886  C  C   . GLY   A 1 113 ? 18.131 -4.119  23.434 1.00 13.07 ? 119 GLY   A C   1 
ATOM   887  O  O   . GLY   A 1 113 ? 19.302 -4.189  23.032 1.00 14.00 ? 119 GLY   A O   1 
ATOM   888  N  N   . VAL   A 1 114 ? 17.307 -3.113  23.139 1.00 12.40 ? 120 VAL   A N   1 
ATOM   889  C  CA  . VAL   A 1 114 ? 17.750 -1.962  22.363 1.00 12.27 ? 120 VAL   A CA  1 
ATOM   890  C  C   . VAL   A 1 114 ? 18.722 -1.106  23.173 1.00 12.49 ? 120 VAL   A C   1 
ATOM   891  O  O   . VAL   A 1 114 ? 18.391 -0.697  24.301 1.00 12.52 ? 120 VAL   A O   1 
ATOM   892  C  CB  . VAL   A 1 114 ? 16.524 -1.105  21.949 1.00 13.34 ? 120 VAL   A CB  1 
ATOM   893  C  CG1 . VAL   A 1 114 ? 17.000 0.167   21.242 1.00 13.33 ? 120 VAL   A CG1 1 
ATOM   894  C  CG2 . VAL   A 1 114 ? 15.606 -1.927  21.038 1.00 13.23 ? 120 VAL   A CG2 1 
ATOM   895  N  N   . VAL   A 1 115 ? 19.853 -0.765  22.552 1.00 12.42 ? 121 VAL   A N   1 
ATOM   896  C  CA  . VAL   A 1 115 ? 20.898 0.057   23.145 1.00 12.88 ? 121 VAL   A CA  1 
ATOM   897  C  C   . VAL   A 1 115 ? 20.783 1.537   22.703 1.00 12.76 ? 121 VAL   A C   1 
ATOM   898  O  O   . VAL   A 1 115 ? 21.003 2.464   23.496 1.00 12.70 ? 121 VAL   A O   1 
ATOM   899  C  CB  . VAL   A 1 115 ? 22.283 -0.527  22.776 1.00 14.23 ? 121 VAL   A CB  1 
ATOM   900  C  CG1 . VAL   A 1 115 ? 23.409 0.415   23.215 1.00 14.59 ? 121 VAL   A CG1 1 
ATOM   901  C  CG2 . VAL   A 1 115 ? 22.494 -1.938  23.363 1.00 14.34 ? 121 VAL   A CG2 1 
ATOM   902  N  N   . GLY   A 1 116 ? 20.553 1.729   21.401 1.00 11.96 ? 122 GLY   A N   1 
ATOM   903  C  CA  . GLY   A 1 116 ? 20.497 3.083   20.853 1.00 12.27 ? 122 GLY   A CA  1 
ATOM   904  C  C   . GLY   A 1 116 ? 20.183 3.096   19.372 1.00 11.99 ? 122 GLY   A C   1 
ATOM   905  O  O   . GLY   A 1 116 ? 19.785 2.069   18.814 1.00 11.88 ? 122 GLY   A O   1 
ATOM   906  N  N   . ILE   A 1 117 ? 20.323 4.265   18.734 1.00 11.67 ? 123 ILE   A N   1 
ATOM   907  C  CA  . ILE   A 1 117 ? 20.019 4.365   17.295 1.00 10.76 ? 123 ILE   A CA  1 
ATOM   908  C  C   . ILE   A 1 117 ? 21.167 5.069   16.575 1.00 10.08 ? 123 ILE   A C   1 
ATOM   909  O  O   . ILE   A 1 117 ? 21.828 5.930   17.152 1.00 10.53 ? 123 ILE   A O   1 
ATOM   910  C  CB  . ILE   A 1 117 ? 18.696 5.146   17.023 1.00 12.14 ? 123 ILE   A CB  1 
ATOM   911  C  CG1 . ILE   A 1 117 ? 18.671 6.481   17.777 1.00 12.98 ? 123 ILE   A CG1 1 
ATOM   912  C  CG2 . ILE   A 1 117 ? 17.463 4.279   17.351 1.00 13.56 ? 123 ILE   A CG2 1 
ATOM   913  C  CD1 . ILE   A 1 117 ? 17.369 7.300   17.324 1.00 14.94 ? 123 ILE   A CD1 1 
ATOM   914  N  N   . VAL   A 1 118 ? 21.402 4.739   15.301 1.00 9.37  ? 124 VAL   A N   1 
ATOM   915  C  CA  . VAL   A 1 118 ? 22.429 5.424   14.500 1.00 10.40 ? 124 VAL   A CA  1 
ATOM   916  C  C   . VAL   A 1 118 ? 22.121 6.927   14.483 1.00 11.17 ? 124 VAL   A C   1 
ATOM   917  O  O   . VAL   A 1 118 ? 20.973 7.322   14.250 1.00 10.73 ? 124 VAL   A O   1 
ATOM   918  C  CB  . VAL   A 1 118 ? 22.464 4.899   13.050 1.00 10.82 ? 124 VAL   A CB  1 
ATOM   919  C  CG1 . VAL   A 1 118 ? 23.420 5.745   12.203 1.00 11.53 ? 124 VAL   A CG1 1 
ATOM   920  C  CG2 . VAL   A 1 118 ? 22.872 3.419   13.011 1.00 11.86 ? 124 VAL   A CG2 1 
ATOM   921  N  N   . SER   A 1 119 ? 23.140 7.728   14.748 1.00 11.07 ? 125 SER   A N   1 
ATOM   922  C  CA  . SER   A 1 119 ? 22.973 9.189   14.775 1.00 11.27 ? 125 SER   A CA  1 
ATOM   923  C  C   . SER   A 1 119 ? 24.042 9.927   13.972 1.00 13.19 ? 125 SER   A C   1 
ATOM   924  O  O   . SER   A 1 119 ? 23.772 11.011  13.479 1.00 14.47 ? 125 SER   A O   1 
ATOM   925  C  CB  . SER   A 1 119 ? 22.977 9.667   16.230 1.00 13.43 ? 125 SER   A CB  1 
ATOM   926  O  OG  . SER   A 1 119 ? 22.805 11.068  16.399 1.00 14.32 ? 125 SER   A OG  1 
ATOM   927  N  N   . THR   A 1 120 ? 25.262 9.374   13.864 1.00 12.80 ? 126 THR   A N   1 
ATOM   928  C  CA  . THR   A 1 120 ? 26.344 10.050  13.114 1.00 13.24 ? 126 THR   A CA  1 
ATOM   929  C  C   . THR   A 1 120 ? 27.150 9.016   12.299 1.00 14.33 ? 126 THR   A C   1 
ATOM   930  O  O   . THR   A 1 120 ? 27.039 7.817   12.541 1.00 13.50 ? 126 THR   A O   1 
ATOM   931  C  CB  . THR   A 1 120 ? 27.310 10.789  14.114 1.00 15.62 ? 126 THR   A CB  1 
ATOM   932  O  OG1 . THR   A 1 120 ? 28.137 9.832   14.800 1.00 17.09 ? 126 THR   A OG1 1 
ATOM   933  C  CG2 . THR   A 1 120 ? 26.608 11.715  15.098 1.00 15.71 ? 126 THR   A CG2 1 
ATOM   934  N  N   . GLY   A 1 121 ? 28.027 9.502   11.417 1.00 14.51 ? 127 GLY   A N   1 
ATOM   935  C  CA  . GLY   A 1 121 ? 28.925 8.614   10.717 1.00 15.73 ? 127 GLY   A CA  1 
ATOM   936  C  C   . GLY   A 1 121 ? 29.905 9.334   9.841  1.00 16.92 ? 127 GLY   A C   1 
ATOM   937  O  O   . GLY   A 1 121 ? 29.833 10.549  9.699  1.00 16.93 ? 127 GLY   A O   1 
ATOM   938  N  N   . GLY   A 1 122 ? 30.782 8.549   9.229  1.00 18.54 ? 128 GLY   A N   1 
ATOM   939  C  CA  . GLY   A 1 122 ? 31.708 9.074   8.241  1.00 20.34 ? 128 GLY   A CA  1 
ATOM   940  C  C   . GLY   A 1 122 ? 33.037 8.398   8.355  1.00 21.11 ? 128 GLY   A C   1 
ATOM   941  O  O   . GLY   A 1 122 ? 33.438 8.039   9.469  1.00 21.60 ? 128 GLY   A O   1 
ATOM   942  N  N   . ASN   A 1 123 ? 33.726 8.231   7.210  1.00 20.78 ? 129 ASN   A N   1 
ATOM   943  C  CA  . ASN   A 1 123 ? 35.063 7.668   7.154  1.00 21.74 ? 129 ASN   A CA  1 
ATOM   944  C  C   . ASN   A 1 123 ? 35.211 6.323   7.838  1.00 20.28 ? 129 ASN   A C   1 
ATOM   945  O  O   . ASN   A 1 123 ? 36.244 6.046   8.465  1.00 21.27 ? 129 ASN   A O   1 
ATOM   946  C  CB  . ASN   A 1 123 ? 36.045 8.682   7.706  1.00 25.15 ? 129 ASN   A CB  1 
ATOM   947  C  CG  . ASN   A 1 123 ? 36.028 9.953   6.876  1.00 33.16 ? 129 ASN   A CG  1 
ATOM   948  O  OD1 . ASN   A 1 123 ? 36.044 9.895   5.639  1.00 35.73 ? 129 ASN   A OD1 1 
ATOM   949  N  ND2 . ASN   A 1 123 ? 35.974 11.113  7.536  1.00 35.48 ? 129 ASN   A ND2 1 
ATOM   950  N  N   . GLY   A 1 124 ? 34.205 5.483   7.684  1.00 17.73 ? 130 GLY   A N   1 
ATOM   951  C  CA  . GLY   A 1 124 ? 34.254 4.143   8.242  1.00 17.09 ? 130 GLY   A CA  1 
ATOM   952  C  C   . GLY   A 1 124 ? 33.945 4.082   9.722  1.00 16.62 ? 130 GLY   A C   1 
ATOM   953  O  O   . GLY   A 1 124 ? 34.138 3.027   10.331 1.00 17.57 ? 130 GLY   A O   1 
ATOM   954  N  N   . LEU   A 1 125 ? 33.371 5.140   10.278 1.00 15.26 ? 131 LEU   A N   1 
ATOM   955  C  CA  . LEU   A 1 125 ? 32.930 5.130   11.672 1.00 15.64 ? 131 LEU   A CA  1 
ATOM   956  C  C   . LEU   A 1 125 ? 31.403 5.282   11.672 1.00 16.58 ? 131 LEU   A C   1 
ATOM   957  O  O   . LEU   A 1 125 ? 30.832 5.900   10.756 1.00 18.40 ? 131 LEU   A O   1 
ATOM   958  C  CB  . LEU   A 1 125 ? 33.527 6.308   12.414 1.00 16.83 ? 131 LEU   A CB  1 
ATOM   959  C  CG  . LEU   A 1 125 ? 35.010 6.220   12.719 1.00 20.19 ? 131 LEU   A CG  1 
ATOM   960  C  CD1 . LEU   A 1 125 ? 35.521 7.558   13.188 1.00 21.88 ? 131 LEU   A CD1 1 
ATOM   961  C  CD2 . LEU   A 1 125 ? 35.266 5.145   13.825 1.00 19.64 ? 131 LEU   A CD2 1 
ATOM   962  N  N   . VAL   A 1 126 ? 30.748 4.752   12.697 1.00 13.13 ? 132 VAL   A N   1 
ATOM   963  C  CA  . VAL   A 1 126 ? 29.325 4.964   12.866 1.00 12.34 ? 132 VAL   A CA  1 
ATOM   964  C  C   . VAL   A 1 126 ? 29.097 5.332   14.345 1.00 12.33 ? 132 VAL   A C   1 
ATOM   965  O  O   . VAL   A 1 126 ? 29.740 4.753   15.229 1.00 12.68 ? 132 VAL   A O   1 
ATOM   966  C  CB  . VAL   A 1 126 ? 28.498 3.761   12.397 1.00 13.69 ? 132 VAL   A CB  1 
ATOM   967  C  CG1 . VAL   A 1 126 ? 28.960 2.483   13.063 1.00 15.32 ? 132 VAL   A CG1 1 
ATOM   968  C  CG2 . VAL   A 1 126 ? 27.012 3.989   12.645 1.00 13.72 ? 132 VAL   A CG2 1 
ATOM   969  N  N   . GLY   A 1 127 ? 28.229 6.318   14.580 1.00 12.28 ? 133 GLY   A N   1 
ATOM   970  C  CA  . GLY   A 1 127 ? 27.954 6.741   15.946 1.00 11.83 ? 133 GLY   A CA  1 
ATOM   971  C  C   . GLY   A 1 127 ? 26.511 6.483   16.318 1.00 12.19 ? 133 GLY   A C   1 
ATOM   972  O  O   . GLY   A 1 127 ? 25.616 6.709   15.499 1.00 12.07 ? 133 GLY   A O   1 
ATOM   973  N  N   . PHE   A 1 128 ? 26.272 6.021   17.565 1.00 11.36 ? 134 PHE   A N   1 
ATOM   974  C  CA  . PHE   A 1 128 ? 24.937 5.652   18.043 1.00 11.52 ? 134 PHE   A CA  1 
ATOM   975  C  C   . PHE   A 1 128 ? 24.591 6.529   19.268 1.00 12.76 ? 134 PHE   A C   1 
ATOM   976  O  O   . PHE   A 1 128 ? 25.411 6.679   20.186 1.00 12.00 ? 134 PHE   A O   1 
ATOM   977  C  CB  . PHE   A 1 128 ? 24.933 4.174   18.521 1.00 11.06 ? 134 PHE   A CB  1 
ATOM   978  C  CG  . PHE   A 1 128 ? 25.427 3.198   17.476 1.00 11.33 ? 134 PHE   A CG  1 
ATOM   979  C  CD1 . PHE   A 1 128 ? 24.578 2.727   16.489 1.00 11.92 ? 134 PHE   A CD1 1 
ATOM   980  C  CD2 . PHE   A 1 128 ? 26.742 2.734   17.494 1.00 11.99 ? 134 PHE   A CD2 1 
ATOM   981  C  CE1 . PHE   A 1 128 ? 25.043 1.846   15.514 1.00 12.33 ? 134 PHE   A CE1 1 
ATOM   982  C  CE2 . PHE   A 1 128 ? 27.204 1.838   16.525 1.00 12.92 ? 134 PHE   A CE2 1 
ATOM   983  C  CZ  . PHE   A 1 128 ? 26.349 1.382   15.549 1.00 11.57 ? 134 PHE   A CZ  1 
ATOM   984  N  N   . ALA   A 1 129 ? 23.364 7.074   19.255 1.00 12.42 ? 135 ALA   A N   1 
ATOM   985  C  CA  . ALA   A 1 129 ? 22.835 7.836   20.380 1.00 11.73 ? 135 ALA   A CA  1 
ATOM   986  C  C   . ALA   A 1 129 ? 22.356 6.781   21.383 1.00 11.36 ? 135 ALA   A C   1 
ATOM   987  O  O   . ALA   A 1 129 ? 21.446 5.988   21.070 1.00 11.17 ? 135 ALA   A O   1 
ATOM   988  C  CB  . ALA   A 1 129 ? 21.645 8.686   19.929 1.00 11.48 ? 135 ALA   A CB  1 
ATOM   989  N  N   . ASP   A 1 130 ? 22.939 6.767   22.585 1.00 10.99 ? 136 ASP   A N   1 
ATOM   990  C  CA  . ASP   A 1 130 ? 22.556 5.792   23.624 1.00 11.71 ? 136 ASP   A CA  1 
ATOM   991  C  C   . ASP   A 1 130 ? 21.170 6.161   24.174 1.00 12.72 ? 136 ASP   A C   1 
ATOM   992  O  O   . ASP   A 1 130 ? 20.858 7.367   24.327 1.00 12.97 ? 136 ASP   A O   1 
ATOM   993  C  CB  . ASP   A 1 130 ? 23.562 5.898   24.784 1.00 14.13 ? 136 ASP   A CB  1 
ATOM   994  C  CG  . ASP   A 1 130 ? 23.354 4.869   25.878 1.00 18.77 ? 136 ASP   A CG  1 
ATOM   995  O  OD1 . ASP   A 1 130 ? 23.105 3.698   25.554 1.00 17.02 ? 136 ASP   A OD1 1 
ATOM   996  O  OD2 . ASP   A 1 130 ? 23.361 5.258   27.060 1.00 21.45 ? 136 ASP   A OD2 1 
ATOM   997  N  N   . VAL   A 1 131 ? 20.353 5.133   24.524 1.00 11.43 ? 137 VAL   A N   1 
ATOM   998  C  CA  . VAL   A 1 131 ? 19.064 5.392   25.197 1.00 12.95 ? 137 VAL   A CA  1 
ATOM   999  C  C   . VAL   A 1 131 ? 18.971 4.614   26.538 1.00 13.52 ? 137 VAL   A C   1 
ATOM   1000 O  O   . VAL   A 1 131 ? 17.935 4.672   27.194 1.00 14.92 ? 137 VAL   A O   1 
ATOM   1001 C  CB  . VAL   A 1 131 ? 17.835 5.056   24.312 1.00 14.49 ? 137 VAL   A CB  1 
ATOM   1002 C  CG1 . VAL   A 1 131 ? 17.835 5.903   23.029 1.00 14.23 ? 137 VAL   A CG1 1 
ATOM   1003 C  CG2 . VAL   A 1 131 ? 17.809 3.563   23.960 1.00 14.50 ? 137 VAL   A CG2 1 
ATOM   1004 N  N   . ARG   A 1 132 ? 20.025 3.828   26.911 1.00 13.01 ? 138 ARG   A N   1 
ATOM   1005 C  CA  . ARG   A 1 132 ? 19.964 2.983   28.109 1.00 13.21 ? 138 ARG   A CA  1 
ATOM   1006 C  C   . ARG   A 1 132 ? 19.823 3.735   29.391 1.00 15.05 ? 138 ARG   A C   1 
ATOM   1007 O  O   . ARG   A 1 132 ? 19.347 3.152   30.367 1.00 16.09 ? 138 ARG   A O   1 
ATOM   1008 C  CB  . ARG   A 1 132 ? 21.175 2.026   28.193 1.00 13.38 ? 138 ARG   A CB  1 
ATOM   1009 C  CG  . ARG   A 1 132 ? 21.264 1.079   27.005 1.00 14.33 ? 138 ARG   A CG  1 
ATOM   1010 C  CD  . ARG   A 1 132 ? 22.564 0.280   27.077 1.00 13.39 ? 138 ARG   A CD  1 
ATOM   1011 N  NE  . ARG   A 1 132 ? 23.687 1.115   26.698 1.00 12.96 ? 138 ARG   A NE  1 
ATOM   1012 C  CZ  . ARG   A 1 132 ? 24.943 0.689   26.604 1.00 16.98 ? 138 ARG   A CZ  1 
ATOM   1013 N  NH1 . ARG   A 1 132 ? 25.244 -0.583  26.888 1.00 15.58 ? 138 ARG   A NH1 1 
ATOM   1014 N  NH2 . ARG   A 1 132 ? 25.901 1.522   26.198 1.00 17.35 ? 138 ARG   A NH2 1 
ATOM   1015 N  N   . ASP   A 1 133 ? 20.250 5.022   29.429 1.00 15.14 ? 139 ASP   A N   1 
ATOM   1016 C  CA  . ASP   A 1 133 ? 20.119 5.793   30.664 1.00 15.71 ? 139 ASP   A CA  1 
ATOM   1017 C  C   . ASP   A 1 133 ? 18.712 6.387   30.864 1.00 16.43 ? 139 ASP   A C   1 
ATOM   1018 O  O   . ASP   A 1 133 ? 18.446 6.936   31.941 1.00 17.92 ? 139 ASP   A O   1 
ATOM   1019 C  CB  . ASP   A 1 133 ? 21.166 6.916   30.717 1.00 17.20 ? 139 ASP   A CB  1 
ATOM   1020 C  CG  . ASP   A 1 133 ? 20.974 7.938   29.611 1.00 20.24 ? 139 ASP   A CG  1 
ATOM   1021 O  OD1 . ASP   A 1 133 ? 20.748 7.518   28.443 1.00 19.12 ? 139 ASP   A OD1 1 
ATOM   1022 O  OD2 . ASP   A 1 133 ? 21.035 9.173   29.914 1.00 22.45 ? 139 ASP   A OD2 1 
ATOM   1023 N  N   . LEU   A 1 134 ? 17.841 6.332   29.850 1.00 15.03 ? 140 LEU   A N   1 
ATOM   1024 C  CA  . LEU   A 1 134 ? 16.492 6.926   29.928 1.00 14.10 ? 140 LEU   A CA  1 
ATOM   1025 C  C   . LEU   A 1 134 ? 15.551 5.956   30.626 1.00 14.46 ? 140 LEU   A C   1 
ATOM   1026 O  O   . LEU   A 1 134 ? 14.770 5.231   29.985 1.00 14.77 ? 140 LEU   A O   1 
ATOM   1027 C  CB  . LEU   A 1 134 ? 15.991 7.298   28.514 1.00 14.37 ? 140 LEU   A CB  1 
ATOM   1028 C  CG  . LEU   A 1 134 ? 16.938 8.223   27.736 1.00 15.44 ? 140 LEU   A CG  1 
ATOM   1029 C  CD1 . LEU   A 1 134 ? 16.459 8.439   26.299 1.00 15.14 ? 140 LEU   A CD1 1 
ATOM   1030 C  CD2 . LEU   A 1 134 ? 17.129 9.566   28.452 1.00 16.51 ? 140 LEU   A CD2 1 
ATOM   1031 N  N   . LEU   A 1 135 ? 15.677 5.874   31.963 1.00 14.59 ? 141 LEU   A N   1 
ATOM   1032 C  CA  . LEU   A 1 135 ? 14.910 4.862   32.709 1.00 16.01 ? 141 LEU   A CA  1 
ATOM   1033 C  C   . LEU   A 1 135 ? 13.402 5.031   32.609 1.00 17.07 ? 141 LEU   A C   1 
ATOM   1034 O  O   . LEU   A 1 135 ? 12.650 4.036   32.677 1.00 18.32 ? 141 LEU   A O   1 
ATOM   1035 C  CB  . LEU   A 1 135 ? 15.362 4.804   34.177 1.00 16.30 ? 141 LEU   A CB  1 
ATOM   1036 C  CG  . LEU   A 1 135 ? 16.888 4.725   34.379 1.00 18.21 ? 141 LEU   A CG  1 
ATOM   1037 C  CD1 . LEU   A 1 135 ? 17.220 4.603   35.873 1.00 18.90 ? 141 LEU   A CD1 1 
ATOM   1038 C  CD2 . LEU   A 1 135 ? 17.538 3.573   33.540 1.00 19.57 ? 141 LEU   A CD2 1 
ATOM   1039 N  N   . TRP   A 1 136 ? 12.961 6.289   32.445 1.00 16.98 ? 142 TRP   A N   1 
ATOM   1040 C  CA  . TRP   A 1 136 ? 11.539 6.606   32.363 1.00 18.02 ? 142 TRP   A CA  1 
ATOM   1041 C  C   . TRP   A 1 136 ? 10.863 6.014   31.123 1.00 18.73 ? 142 TRP   A C   1 
ATOM   1042 O  O   . TRP   A 1 136 ? 9.633  5.934   31.095 1.00 19.77 ? 142 TRP   A O   1 
ATOM   1043 C  CB  . TRP   A 1 136 ? 11.332 8.120   32.457 1.00 18.18 ? 142 TRP   A CB  1 
ATOM   1044 C  CG  . TRP   A 1 136 ? 12.140 8.902   31.457 1.00 18.10 ? 142 TRP   A CG  1 
ATOM   1045 C  CD1 . TRP   A 1 136 ? 13.391 9.440   31.625 1.00 18.63 ? 142 TRP   A CD1 1 
ATOM   1046 C  CD2 . TRP   A 1 136 ? 11.740 9.219   30.124 1.00 18.05 ? 142 TRP   A CD2 1 
ATOM   1047 N  NE1 . TRP   A 1 136 ? 13.759 10.134  30.492 1.00 18.96 ? 142 TRP   A NE1 1 
ATOM   1048 C  CE2 . TRP   A 1 136 ? 12.759 10.017  29.554 1.00 18.46 ? 142 TRP   A CE2 1 
ATOM   1049 C  CE3 . TRP   A 1 136 ? 10.575 8.987   29.386 1.00 18.18 ? 142 TRP   A CE3 1 
ATOM   1050 C  CZ2 . TRP   A 1 136 ? 12.680 10.504  28.243 1.00 18.50 ? 142 TRP   A CZ2 1 
ATOM   1051 C  CZ3 . TRP   A 1 136 ? 10.487 9.496   28.104 1.00 18.31 ? 142 TRP   A CZ3 1 
ATOM   1052 C  CH2 . TRP   A 1 136 ? 11.516 10.276  27.562 1.00 18.50 ? 142 TRP   A CH2 1 
ATOM   1053 N  N   . LEU   A 1 137 ? 11.646 5.581   30.092 1.00 17.58 ? 143 LEU   A N   1 
ATOM   1054 C  CA  . LEU   A 1 137 ? 11.028 4.987   28.893 1.00 19.25 ? 143 LEU   A CA  1 
ATOM   1055 C  C   . LEU   A 1 137 ? 10.157 3.748   29.241 1.00 23.21 ? 143 LEU   A C   1 
ATOM   1056 O  O   . LEU   A 1 137 ? 9.257  3.401   28.478 1.00 22.62 ? 143 LEU   A O   1 
ATOM   1057 C  CB  . LEU   A 1 137 ? 12.085 4.579   27.856 1.00 18.71 ? 143 LEU   A CB  1 
ATOM   1058 C  CG  . LEU   A 1 137 ? 12.705 5.709   27.053 1.00 18.84 ? 143 LEU   A CG  1 
ATOM   1059 C  CD1 . LEU   A 1 137 ? 13.804 5.172   26.131 1.00 19.46 ? 143 LEU   A CD1 1 
ATOM   1060 C  CD2 . LEU   A 1 137 ? 11.637 6.443   26.217 1.00 19.33 ? 143 LEU   A CD2 1 
ATOM   1061 N  N   . ASP   A 1 138 ? 10.449 3.066   30.368 1.00 26.91 ? 144 ASP   A N   1 
ATOM   1062 C  CA  . ASP   A 1 138 ? 9.645  1.895   30.754 1.00 32.37 ? 144 ASP   A CA  1 
ATOM   1063 C  C   . ASP   A 1 138 ? 9.411  1.862   32.250 1.00 37.54 ? 144 ASP   A C   1 
ATOM   1064 O  O   . ASP   A 1 138 ? 9.386  0.779   32.839 1.00 39.13 ? 144 ASP   A O   1 
ATOM   1065 C  CB  . ASP   A 1 138 ? 10.302 0.598   30.262 1.00 35.05 ? 144 ASP   A CB  1 
ATOM   1066 C  CG  . ASP   A 1 138 ? 11.768 0.513   30.608 1.00 40.02 ? 144 ASP   A CG  1 
ATOM   1067 O  OD1 . ASP   A 1 138 ? 12.572 0.209   29.702 1.00 41.38 ? 144 ASP   A OD1 1 
ATOM   1068 O  OD2 . ASP   A 1 138 ? 12.121 0.807   31.763 1.00 41.18 ? 144 ASP   A OD2 1 
ATOM   1069 N  N   . GLU   A 1 139 ? 9.259  3.055   32.871 1.00 39.74 ? 145 GLU   A N   1 
ATOM   1070 C  CA  . GLU   A 1 139 ? 9.131  3.328   34.307 1.00 42.53 ? 145 GLU   A CA  1 
ATOM   1071 C  C   . GLU   A 1 139 ? 8.929  2.106   35.217 1.00 44.42 ? 145 GLU   A C   1 
ATOM   1072 O  O   . GLU   A 1 139 ? 8.030  1.294   34.986 1.00 45.62 ? 145 GLU   A O   1 
ATOM   1073 C  CB  . GLU   A 1 139 ? 8.024  4.350   34.563 1.00 45.81 ? 145 GLU   A CB  1 
ATOM   1074 C  CG  . GLU   A 1 139 ? 8.291  5.192   35.796 1.00 52.75 ? 145 GLU   A CG  1 
ATOM   1075 C  CD  . GLU   A 1 139 ? 9.507  6.093   35.686 1.00 60.10 ? 145 GLU   A CD  1 
ATOM   1076 O  OE1 . GLU   A 1 139 ? 9.368  7.211   35.137 1.00 61.26 ? 145 GLU   A OE1 1 
ATOM   1077 O  OE2 . GLU   A 1 139 ? 10.593 5.688   36.161 1.00 62.61 ? 145 GLU   A OE2 1 
ATOM   1078 N  N   . SER   B 1 1   ? 19.702 -24.620 23.972 1.00 20.19 ? 7   SER   C N   1 
ATOM   1079 C  CA  . SER   B 1 1   ? 20.838 -24.460 23.037 1.00 20.12 ? 7   SER   C CA  1 
ATOM   1080 C  C   . SER   B 1 1   ? 20.833 -25.621 22.008 1.00 19.29 ? 7   SER   C C   1 
ATOM   1081 O  O   . SER   B 1 1   ? 20.126 -26.620 22.205 1.00 19.81 ? 7   SER   C O   1 
ATOM   1082 C  CB  . SER   B 1 1   ? 22.162 -24.447 23.807 1.00 23.10 ? 7   SER   C CB  1 
ATOM   1083 O  OG  . SER   B 1 1   ? 22.350 -25.682 24.484 1.00 26.85 ? 7   SER   C OG  1 
ATOM   1084 N  N   . GLY   B 1 2   ? 21.574 -25.461 20.916 1.00 17.91 ? 8   GLY   C N   1 
ATOM   1085 C  CA  . GLY   B 1 2   ? 21.676 -26.500 19.896 1.00 17.00 ? 8   GLY   C CA  1 
ATOM   1086 C  C   . GLY   B 1 2   ? 21.965 -25.922 18.531 1.00 16.71 ? 8   GLY   C C   1 
ATOM   1087 O  O   . GLY   B 1 2   ? 21.610 -24.771 18.253 1.00 16.72 ? 8   GLY   C O   1 
ATOM   1088 N  N   . ALA   B 1 3   ? 22.602 -26.701 17.682 1.00 15.65 ? 9   ALA   C N   1 
ATOM   1089 C  CA  . ALA   B 1 3   ? 22.943 -26.244 16.330 1.00 15.46 ? 9   ALA   C CA  1 
ATOM   1090 C  C   . ALA   B 1 3   ? 22.847 -27.411 15.332 1.00 15.12 ? 9   ALA   C C   1 
ATOM   1091 O  O   . ALA   B 1 3   ? 22.843 -28.565 15.740 1.00 15.45 ? 9   ALA   C O   1 
ATOM   1092 C  CB  . ALA   B 1 3   ? 24.378 -25.686 16.327 1.00 16.29 ? 9   ALA   C CB  1 
ATOM   1093 N  N   . ILE   B 1 4   ? 22.800 -27.094 14.034 1.00 14.64 ? 10  ILE   C N   1 
ATOM   1094 C  CA  . ILE   B 1 4   ? 22.871 -28.066 12.945 1.00 14.55 ? 10  ILE   C CA  1 
ATOM   1095 C  C   . ILE   B 1 4   ? 24.233 -27.850 12.261 1.00 15.42 ? 10  ILE   C C   1 
ATOM   1096 O  O   . ILE   B 1 4   ? 24.601 -26.715 11.978 1.00 15.38 ? 10  ILE   C O   1 
ATOM   1097 C  CB  . ILE   B 1 4   ? 21.753 -27.818 11.900 1.00 14.37 ? 10  ILE   C CB  1 
ATOM   1098 C  CG1 . ILE   B 1 4   ? 20.385 -27.869 12.551 1.00 14.99 ? 10  ILE   C CG1 1 
ATOM   1099 C  CG2 . ILE   B 1 4   ? 21.867 -28.841 10.764 1.00 15.14 ? 10  ILE   C CG2 1 
ATOM   1100 C  CD1 . ILE   B 1 4   ? 19.286 -27.247 11.650 1.00 16.55 ? 10  ILE   C CD1 1 
ATOM   1101 N  N   . TYR   B 1 5   ? 24.981 -28.935 12.016 1.00 15.52 ? 11  TYR   C N   1 
ATOM   1102 C  CA  . TYR   B 1 5   ? 26.291 -28.873 11.399 1.00 16.33 ? 11  TYR   C CA  1 
ATOM   1103 C  C   . TYR   B 1 5   ? 26.217 -29.592 10.052 1.00 17.12 ? 11  TYR   C C   1 
ATOM   1104 O  O   . TYR   B 1 5   ? 26.036 -30.808 10.023 1.00 18.57 ? 11  TYR   C O   1 
ATOM   1105 C  CB  . TYR   B 1 5   ? 27.313 -29.558 12.326 1.00 16.34 ? 11  TYR   C CB  1 
ATOM   1106 C  CG  . TYR   B 1 5   ? 27.521 -28.771 13.601 1.00 17.45 ? 11  TYR   C CG  1 
ATOM   1107 C  CD1 . TYR   B 1 5   ? 28.372 -27.674 13.634 1.00 18.00 ? 11  TYR   C CD1 1 
ATOM   1108 C  CD2 . TYR   B 1 5   ? 26.806 -29.071 14.753 1.00 18.30 ? 11  TYR   C CD2 1 
ATOM   1109 C  CE1 . TYR   B 1 5   ? 28.534 -26.917 14.795 1.00 19.33 ? 11  TYR   C CE1 1 
ATOM   1110 C  CE2 . TYR   B 1 5   ? 26.960 -28.324 15.918 1.00 19.48 ? 11  TYR   C CE2 1 
ATOM   1111 C  CZ  . TYR   B 1 5   ? 27.836 -27.251 15.940 1.00 19.87 ? 11  TYR   C CZ  1 
ATOM   1112 O  OH  . TYR   B 1 5   ? 27.961 -26.479 17.077 1.00 21.37 ? 11  TYR   C OH  1 
ATOM   1113 N  N   . VAL   B 1 6   ? 26.369 -28.866 8.945  1.00 16.69 ? 12  VAL   C N   1 
ATOM   1114 C  CA  . VAL   B 1 6   ? 26.248 -29.467 7.623  1.00 18.32 ? 12  VAL   C CA  1 
ATOM   1115 C  C   . VAL   B 1 6   ? 27.301 -28.824 6.737  1.00 19.55 ? 12  VAL   C C   1 
ATOM   1116 O  O   . VAL   B 1 6   ? 27.373 -27.601 6.651  1.00 19.50 ? 12  VAL   C O   1 
ATOM   1117 C  CB  . VAL   B 1 6   ? 24.810 -29.311 7.033  1.00 20.07 ? 12  VAL   C CB  1 
ATOM   1118 C  CG1 . VAL   B 1 6   ? 24.257 -27.899 7.237  1.00 20.64 ? 12  VAL   C CG1 1 
ATOM   1119 C  CG2 . VAL   B 1 6   ? 24.787 -29.704 5.550  1.00 20.68 ? 12  VAL   C CG2 1 
ATOM   1120 N  N   . GLY   B 1 7   ? 28.194 -29.641 6.163  1.00 20.08 ? 13  GLY   C N   1 
ATOM   1121 C  CA  . GLY   B 1 7   ? 29.277 -29.138 5.325  1.00 20.99 ? 13  GLY   C CA  1 
ATOM   1122 C  C   . GLY   B 1 7   ? 30.160 -28.209 6.138  1.00 21.98 ? 13  GLY   C C   1 
ATOM   1123 O  O   . GLY   B 1 7   ? 30.419 -28.489 7.311  1.00 23.05 ? 13  GLY   C O   1 
ATOM   1124 N  N   . ASN   B 1 8   ? 30.450 -27.032 5.612  1.00 22.47 ? 14  ASN   C N   1 
ATOM   1125 C  CA  . ASN   B 1 8   ? 31.230 -26.053 6.373  1.00 22.45 ? 14  ASN   C CA  1 
ATOM   1126 C  C   . ASN   B 1 8   ? 30.323 -24.982 6.982  1.00 20.92 ? 14  ASN   C C   1 
ATOM   1127 O  O   . ASN   B 1 8   ? 30.751 -23.839 7.138  1.00 21.41 ? 14  ASN   C O   1 
ATOM   1128 C  CB  . ASN   B 1 8   ? 32.325 -25.423 5.533  1.00 25.86 ? 14  ASN   C CB  1 
ATOM   1129 C  CG  . ASN   B 1 8   ? 33.430 -26.397 5.236  1.00 33.87 ? 14  ASN   C CG  1 
ATOM   1130 O  OD1 . ASN   B 1 8   ? 34.035 -26.995 6.144  1.00 36.17 ? 14  ASN   C OD1 1 
ATOM   1131 N  ND2 . ASN   B 1 8   ? 33.727 -26.575 3.966  1.00 35.63 ? 14  ASN   C ND2 1 
ATOM   1132 N  N   . TYR   B 1 9   ? 29.101 -25.369 7.393  1.00 18.73 ? 15  TYR   C N   1 
ATOM   1133 C  CA  . TYR   B 1 9   ? 28.140 -24.449 7.993  1.00 17.08 ? 15  TYR   C CA  1 
ATOM   1134 C  C   . TYR   B 1 9   ? 27.661 -24.909 9.367  1.00 16.10 ? 15  TYR   C C   1 
ATOM   1135 O  O   . TYR   B 1 9   ? 27.498 -26.117 9.618  1.00 15.72 ? 15  TYR   C O   1 
ATOM   1136 C  CB  . TYR   B 1 9   ? 26.885 -24.331 7.090  1.00 16.65 ? 15  TYR   C CB  1 
ATOM   1137 C  CG  . TYR   B 1 9   ? 27.163 -23.756 5.717  1.00 17.95 ? 15  TYR   C CG  1 
ATOM   1138 C  CD1 . TYR   B 1 9   ? 27.828 -22.543 5.571  1.00 19.68 ? 15  TYR   C CD1 1 
ATOM   1139 C  CD2 . TYR   B 1 9   ? 26.753 -24.419 4.567  1.00 19.38 ? 15  TYR   C CD2 1 
ATOM   1140 C  CE1 . TYR   B 1 9   ? 28.103 -22.018 4.314  1.00 21.36 ? 15  TYR   C CE1 1 
ATOM   1141 C  CE2 . TYR   B 1 9   ? 27.006 -23.891 3.302  1.00 20.94 ? 15  TYR   C CE2 1 
ATOM   1142 C  CZ  . TYR   B 1 9   ? 27.666 -22.679 3.182  1.00 22.68 ? 15  TYR   C CZ  1 
ATOM   1143 O  OH  . TYR   B 1 9   ? 27.939 -22.125 1.946  1.00 25.33 ? 15  TYR   C OH  1 
ATOM   1144 N  N   . ARG   B 1 10  ? 27.333 -23.906 10.230 1.00 14.24 ? 16  ARG   C N   1 
ATOM   1145 C  CA  . ARG   B 1 10  ? 26.742 -24.125 11.546 1.00 14.59 ? 16  ARG   C CA  1 
ATOM   1146 C  C   . ARG   B 1 10  ? 25.443 -23.292 11.557 1.00 14.77 ? 16  ARG   C C   1 
ATOM   1147 O  O   . ARG   B 1 10  ? 25.508 -22.089 11.306 1.00 15.26 ? 16  ARG   C O   1 
ATOM   1148 C  CB  . ARG   B 1 10  ? 27.689 -23.659 12.666 1.00 15.62 ? 16  ARG   C CB  1 
ATOM   1149 C  CG  . ARG   B 1 10  ? 27.045 -23.461 14.030 1.00 16.93 ? 16  ARG   C CG  1 
ATOM   1150 C  CD  . ARG   B 1 10  ? 28.080 -23.168 15.127 1.00 18.51 ? 16  ARG   C CD  1 
ATOM   1151 N  NE  . ARG   B 1 10  ? 27.668 -22.150 16.105 1.00 19.93 ? 16  ARG   C NE  1 
ATOM   1152 C  CZ  . ARG   B 1 10  ? 27.247 -22.413 17.340 1.00 22.28 ? 16  ARG   C CZ  1 
ATOM   1153 N  NH1 . ARG   B 1 10  ? 27.117 -23.674 17.752 1.00 21.60 ? 16  ARG   C NH1 1 
ATOM   1154 N  NH2 . ARG   B 1 10  ? 26.904 -21.416 18.162 1.00 20.70 ? 16  ARG   C NH2 1 
ATOM   1155 N  N   . VAL   B 1 11  ? 24.282 -23.938 11.774 1.00 13.39 ? 17  VAL   C N   1 
ATOM   1156 C  CA  . VAL   B 1 11  ? 22.991 -23.238 11.797 1.00 13.40 ? 17  VAL   C CA  1 
ATOM   1157 C  C   . VAL   B 1 11  ? 22.547 -23.136 13.258 1.00 13.49 ? 17  VAL   C C   1 
ATOM   1158 O  O   . VAL   B 1 11  ? 22.430 -24.166 13.942 1.00 14.22 ? 17  VAL   C O   1 
ATOM   1159 C  CB  . VAL   B 1 11  ? 21.898 -24.010 10.992 1.00 14.72 ? 17  VAL   C CB  1 
ATOM   1160 C  CG1 . VAL   B 1 11  ? 20.615 -23.154 10.888 1.00 15.14 ? 17  VAL   C CG1 1 
ATOM   1161 C  CG2 . VAL   B 1 11  ? 22.411 -24.414 9.604  1.00 14.90 ? 17  VAL   C CG2 1 
ATOM   1162 N  N   . VAL   B 1 12  ? 22.303 -21.921 13.740 1.00 12.11 ? 18  VAL   C N   1 
ATOM   1163 C  CA  . VAL   B 1 12  ? 21.879 -21.724 15.134 1.00 12.83 ? 18  VAL   C CA  1 
ATOM   1164 C  C   . VAL   B 1 12  ? 20.672 -20.765 15.168 1.00 11.98 ? 18  VAL   C C   1 
ATOM   1165 O  O   . VAL   B 1 12  ? 20.406 -20.018 14.202 1.00 11.34 ? 18  VAL   C O   1 
ATOM   1166 C  CB  . VAL   B 1 12  ? 23.036 -21.105 15.987 1.00 15.53 ? 18  VAL   C CB  1 
ATOM   1167 C  CG1 . VAL   B 1 12  ? 24.161 -22.103 16.163 1.00 18.52 ? 18  VAL   C CG1 1 
ATOM   1168 C  CG2 . VAL   B 1 12  ? 23.533 -19.793 15.363 1.00 15.44 ? 18  VAL   C CG2 1 
ATOM   1169 N  N   . ASN   B 1 13  ? 19.979 -20.703 16.322 1.00 11.62 ? 19  ASN   C N   1 
ATOM   1170 C  CA  . ASN   B 1 13  ? 18.948 -19.660 16.518 1.00 11.64 ? 19  ASN   C CA  1 
ATOM   1171 C  C   . ASN   B 1 13  ? 19.723 -18.308 16.487 1.00 12.27 ? 19  ASN   C C   1 
ATOM   1172 O  O   . ASN   B 1 13  ? 20.739 -18.149 17.194 1.00 12.93 ? 19  ASN   C O   1 
ATOM   1173 C  CB  . ASN   B 1 13  ? 18.310 -19.779 17.901 1.00 12.41 ? 19  ASN   C CB  1 
ATOM   1174 C  CG  . ASN   B 1 13  ? 17.455 -21.018 18.033 1.00 15.11 ? 19  ASN   C CG  1 
ATOM   1175 O  OD1 . ASN   B 1 13  ? 17.918 -22.054 18.536 1.00 14.97 ? 19  ASN   C OD1 1 
ATOM   1176 N  ND2 . ASN   B 1 13  ? 16.200 -20.916 17.602 1.00 13.40 ? 19  ASN   C ND2 1 
ATOM   1177 N  N   . ARG   B 1 14  ? 19.241 -17.358 15.694 1.00 11.66 ? 20  ARG   C N   1 
ATOM   1178 C  CA  . ARG   B 1 14  ? 19.927 -16.051 15.605 1.00 11.42 ? 20  ARG   C CA  1 
ATOM   1179 C  C   . ARG   B 1 14  ? 20.068 -15.388 16.983 1.00 12.13 ? 20  ARG   C C   1 
ATOM   1180 O  O   . ARG   B 1 14  ? 21.127 -14.812 17.271 1.00 13.65 ? 20  ARG   C O   1 
ATOM   1181 C  CB  . ARG   B 1 14  ? 19.166 -15.111 14.664 1.00 12.53 ? 20  ARG   C CB  1 
ATOM   1182 C  CG  . ARG   B 1 14  ? 19.938 -13.840 14.254 1.00 14.29 ? 20  ARG   C CG  1 
ATOM   1183 C  CD  . ARG   B 1 14  ? 18.950 -12.924 13.560 1.00 13.90 ? 20  ARG   C CD  1 
ATOM   1184 N  NE  . ARG   B 1 14  ? 19.543 -11.691 13.005 1.00 14.32 ? 20  ARG   C NE  1 
ATOM   1185 C  CZ  . ARG   B 1 14  ? 19.661 -10.557 13.683 1.00 16.75 ? 20  ARG   C CZ  1 
ATOM   1186 N  NH1 . ARG   B 1 14  ? 19.343 -10.509 14.974 1.00 14.90 ? 20  ARG   C NH1 1 
ATOM   1187 N  NH2 . ARG   B 1 14  ? 20.141 -9.467  13.087 1.00 18.12 ? 20  ARG   C NH2 1 
ATOM   1188 N  N   . HIS   B 1 15  ? 19.035 -15.516 17.849 1.00 11.40 ? 21  HIS   C N   1 
ATOM   1189 C  CA  . HIS   B 1 15  ? 19.111 -14.888 19.179 1.00 12.12 ? 21  HIS   C CA  1 
ATOM   1190 C  C   . HIS   B 1 15  ? 20.137 -15.525 20.126 1.00 12.85 ? 21  HIS   C C   1 
ATOM   1191 O  O   . HIS   B 1 15  ? 20.498 -14.907 21.144 1.00 14.09 ? 21  HIS   C O   1 
ATOM   1192 C  CB  . HIS   B 1 15  ? 17.718 -14.810 19.847 1.00 13.03 ? 21  HIS   C CB  1 
ATOM   1193 C  CG  . HIS   B 1 15  ? 17.161 -16.111 20.356 1.00 12.02 ? 21  HIS   C CG  1 
ATOM   1194 N  ND1 . HIS   B 1 15  ? 16.443 -16.983 19.534 1.00 13.40 ? 21  HIS   C ND1 1 
ATOM   1195 C  CD2 . HIS   B 1 15  ? 17.139 -16.596 21.625 1.00 14.10 ? 21  HIS   C CD2 1 
ATOM   1196 C  CE1 . HIS   B 1 15  ? 16.035 -17.972 20.321 1.00 15.04 ? 21  HIS   C CE1 1 
ATOM   1197 N  NE2 . HIS   B 1 15  ? 16.431 -17.784 21.592 1.00 14.93 ? 21  HIS   C NE2 1 
ATOM   1198 N  N   . LEU   B 1 16  ? 20.631 -16.719 19.784 1.00 12.52 ? 22  LEU   C N   1 
ATOM   1199 C  CA  . LEU   B 1 16  ? 21.629 -17.402 20.619 1.00 14.00 ? 22  LEU   C CA  1 
ATOM   1200 C  C   . LEU   B 1 16  ? 23.024 -17.395 19.958 1.00 15.35 ? 22  LEU   C C   1 
ATOM   1201 O  O   . LEU   B 1 16  ? 23.967 -18.000 20.508 1.00 15.56 ? 22  LEU   C O   1 
ATOM   1202 C  CB  . LEU   B 1 16  ? 21.175 -18.862 20.894 1.00 14.61 ? 22  LEU   C CB  1 
ATOM   1203 C  CG  . LEU   B 1 16  ? 19.852 -18.975 21.677 1.00 15.77 ? 22  LEU   C CG  1 
ATOM   1204 C  CD1 . LEU   B 1 16  ? 19.492 -20.457 21.919 1.00 16.87 ? 22  LEU   C CD1 1 
ATOM   1205 C  CD2 . LEU   B 1 16  ? 19.919 -18.242 23.047 1.00 16.30 ? 22  LEU   C CD2 1 
ATOM   1206 N  N   . ALA   B 1 17  ? 23.164 -16.738 18.775 1.00 14.26 ? 23  ALA   C N   1 
ATOM   1207 C  CA  . ALA   B 1 17  ? 24.454 -16.693 18.083 1.00 15.38 ? 23  ALA   C CA  1 
ATOM   1208 C  C   . ALA   B 1 17  ? 25.537 -16.061 18.966 1.00 15.30 ? 23  ALA   C C   1 
ATOM   1209 O  O   . ALA   B 1 17  ? 25.246 -15.145 19.734 1.00 15.46 ? 23  ALA   C O   1 
ATOM   1210 C  CB  . ALA   B 1 17  ? 24.324 -15.898 16.792 1.00 14.18 ? 23  ALA   C CB  1 
ATOM   1211 N  N   . THR   B 1 18  ? 26.756 -16.607 18.912 1.00 15.68 ? 24  THR   C N   1 
ATOM   1212 C  CA  . THR   B 1 18  ? 27.876 -16.108 19.729 1.00 16.13 ? 24  THR   C CA  1 
ATOM   1213 C  C   . THR   B 1 18  ? 28.665 -14.994 18.970 1.00 16.34 ? 24  THR   C C   1 
ATOM   1214 O  O   . THR   B 1 18  ? 28.445 -14.783 17.765 1.00 15.64 ? 24  THR   C O   1 
ATOM   1215 C  CB  . THR   B 1 18  ? 28.836 -17.295 20.014 1.00 17.55 ? 24  THR   C CB  1 
ATOM   1216 O  OG1 . THR   B 1 18  ? 29.397 -17.691 18.754 1.00 19.25 ? 24  THR   C OG1 1 
ATOM   1217 C  CG2 . THR   B 1 18  ? 28.143 -18.465 20.691 1.00 18.05 ? 24  THR   C CG2 1 
ATOM   1218 N  N   . HIS   B 1 19  ? 29.693 -14.378 19.627 1.00 17.06 ? 25  HIS   C N   1 
ATOM   1219 C  CA  . HIS   B 1 19  ? 30.571 -13.430 18.940 1.00 17.75 ? 25  HIS   C CA  1 
ATOM   1220 C  C   . HIS   B 1 19  ? 31.266 -14.143 17.752 1.00 17.18 ? 25  HIS   C C   1 
ATOM   1221 O  O   . HIS   B 1 19  ? 31.378 -13.569 16.664 1.00 18.13 ? 25  HIS   C O   1 
ATOM   1222 C  CB  . HIS   B 1 19  ? 31.655 -12.921 19.910 1.00 21.46 ? 25  HIS   C CB  1 
ATOM   1223 C  CG  . HIS   B 1 19  ? 31.125 -12.078 21.026 1.00 30.23 ? 25  HIS   C CG  1 
ATOM   1224 N  ND1 . HIS   B 1 19  ? 30.259 -11.013 20.786 1.00 34.07 ? 25  HIS   C ND1 1 
ATOM   1225 C  CD2 . HIS   B 1 19  ? 31.386 -12.135 22.354 1.00 33.31 ? 25  HIS   C CD2 1 
ATOM   1226 C  CE1 . HIS   B 1 19  ? 30.036 -10.453 21.970 1.00 35.06 ? 25  HIS   C CE1 1 
ATOM   1227 N  NE2 . HIS   B 1 19  ? 30.691 -11.092 22.943 1.00 35.29 ? 25  HIS   C NE2 1 
ATOM   1228 N  N   . ASN   B 1 20  ? 31.688 -15.408 17.958 1.00 16.86 ? 26  ASN   C N   1 
ATOM   1229 C  CA  . ASN   B 1 20  ? 32.354 -16.182 16.899 1.00 17.46 ? 26  ASN   C CA  1 
ATOM   1230 C  C   . ASN   B 1 20  ? 31.410 -16.416 15.716 1.00 16.87 ? 26  ASN   C C   1 
ATOM   1231 O  O   . ASN   B 1 20  ? 31.831 -16.312 14.557 1.00 17.32 ? 26  ASN   C O   1 
ATOM   1232 C  CB  . ASN   B 1 20  ? 32.874 -17.518 17.419 1.00 21.19 ? 26  ASN   C CB  1 
ATOM   1233 C  CG  . ASN   B 1 20  ? 33.730 -18.234 16.392 1.00 29.12 ? 26  ASN   C CG  1 
ATOM   1234 O  OD1 . ASN   B 1 20  ? 34.736 -17.700 15.930 1.00 30.36 ? 26  ASN   C OD1 1 
ATOM   1235 N  ND2 . ASN   B 1 20  ? 33.348 -19.450 15.991 1.00 31.43 ? 26  ASN   C ND2 1 
ATOM   1236 N  N   . ASP   B 1 21  ? 30.114 -16.708 15.991 1.00 15.62 ? 27  ASP   C N   1 
ATOM   1237 C  CA  . ASP   B 1 21  ? 29.150 -16.895 14.888 1.00 15.52 ? 27  ASP   C CA  1 
ATOM   1238 C  C   . ASP   B 1 21  ? 29.058 -15.606 14.045 1.00 15.72 ? 27  ASP   C C   1 
ATOM   1239 O  O   . ASP   B 1 21  ? 29.107 -15.674 12.825 1.00 17.77 ? 27  ASP   C O   1 
ATOM   1240 C  CB  . ASP   B 1 21  ? 27.756 -17.203 15.449 1.00 15.37 ? 27  ASP   C CB  1 
ATOM   1241 C  CG  . ASP   B 1 21  ? 27.633 -18.630 15.968 1.00 18.10 ? 27  ASP   C CG  1 
ATOM   1242 O  OD1 . ASP   B 1 21  ? 28.171 -19.543 15.308 1.00 17.67 ? 27  ASP   C OD1 1 
ATOM   1243 O  OD2 . ASP   B 1 21  ? 26.992 -18.819 17.037 1.00 18.21 ? 27  ASP   C OD2 1 
ATOM   1244 N  N   . TRP   B 1 22  ? 28.967 -14.441 14.703 1.00 15.27 ? 28  TRP   C N   1 
ATOM   1245 C  CA  . TRP   B 1 22  ? 28.844 -13.183 13.961 1.00 15.61 ? 28  TRP   C CA  1 
ATOM   1246 C  C   . TRP   B 1 22  ? 30.158 -12.808 13.233 1.00 16.72 ? 28  TRP   C C   1 
ATOM   1247 O  O   . TRP   B 1 22  ? 30.102 -12.199 12.160 1.00 17.42 ? 28  TRP   C O   1 
ATOM   1248 C  CB  . TRP   B 1 22  ? 28.409 -12.066 14.911 1.00 15.87 ? 28  TRP   C CB  1 
ATOM   1249 C  CG  . TRP   B 1 22  ? 26.932 -12.032 15.138 1.00 15.34 ? 28  TRP   C CG  1 
ATOM   1250 C  CD1 . TRP   B 1 22  ? 26.250 -12.481 16.231 1.00 16.07 ? 28  TRP   C CD1 1 
ATOM   1251 C  CD2 . TRP   B 1 22  ? 25.959 -11.463 14.252 1.00 14.27 ? 28  TRP   C CD2 1 
ATOM   1252 N  NE1 . TRP   B 1 22  ? 24.904 -12.238 16.078 1.00 16.41 ? 28  TRP   C NE1 1 
ATOM   1253 C  CE2 . TRP   B 1 22  ? 24.698 -11.612 14.867 1.00 15.54 ? 28  TRP   C CE2 1 
ATOM   1254 C  CE3 . TRP   B 1 22  ? 26.034 -10.852 12.997 1.00 14.61 ? 28  TRP   C CE3 1 
ATOM   1255 C  CZ2 . TRP   B 1 22  ? 23.525 -11.146 14.277 1.00 15.63 ? 28  TRP   C CZ2 1 
ATOM   1256 C  CZ3 . TRP   B 1 22  ? 24.859 -10.410 12.401 1.00 15.33 ? 28  TRP   C CZ3 1 
ATOM   1257 C  CH2 . TRP   B 1 22  ? 23.623 -10.593 13.032 1.00 15.66 ? 28  TRP   C CH2 1 
ATOM   1258 N  N   . ALA   B 1 23  ? 31.323 -13.189 13.792 1.00 16.20 ? 29  ALA   C N   1 
ATOM   1259 C  CA  . ALA   B 1 23  ? 32.603 -12.879 13.135 1.00 17.75 ? 29  ALA   C CA  1 
ATOM   1260 C  C   . ALA   B 1 23  ? 32.828 -13.771 11.880 1.00 18.33 ? 29  ALA   C C   1 
ATOM   1261 O  O   . ALA   B 1 23  ? 33.719 -13.472 11.068 1.00 18.86 ? 29  ALA   C O   1 
ATOM   1262 C  CB  . ALA   B 1 23  ? 33.748 -13.105 14.113 1.00 17.27 ? 29  ALA   C CB  1 
ATOM   1263 N  N   . ASN   B 1 24  ? 32.083 -14.914 11.783 1.00 17.69 ? 30  ASN   C N   1 
ATOM   1264 C  CA  . ASN   B 1 24  ? 32.185 -15.861 10.660 1.00 17.49 ? 30  ASN   C CA  1 
ATOM   1265 C  C   . ASN   B 1 24  ? 30.817 -15.990 9.969  1.00 17.68 ? 30  ASN   C C   1 
ATOM   1266 O  O   . ASN   B 1 24  ? 30.442 -17.060 9.506  1.00 17.17 ? 30  ASN   C O   1 
ATOM   1267 C  CB  . ASN   B 1 24  ? 32.664 -17.211 11.175 1.00 18.65 ? 30  ASN   C CB  1 
ATOM   1268 C  CG  . ASN   B 1 24  ? 34.081 -17.133 11.715 1.00 23.95 ? 30  ASN   C CG  1 
ATOM   1269 O  OD1 . ASN   B 1 24  ? 35.057 -17.086 10.956 1.00 23.87 ? 30  ASN   C OD1 1 
ATOM   1270 N  ND2 . ASN   B 1 24  ? 34.217 -17.068 13.043 1.00 24.11 ? 30  ASN   C ND2 1 
ATOM   1271 N  N   . LEU   B 1 25  ? 30.077 -14.866 9.907  1.00 17.42 ? 31  LEU   C N   1 
ATOM   1272 C  CA  . LEU   B 1 25  ? 28.734 -14.817 9.365  1.00 17.50 ? 31  LEU   C CA  1 
ATOM   1273 C  C   . LEU   B 1 25  ? 28.657 -15.184 7.888  1.00 17.85 ? 31  LEU   C C   1 
ATOM   1274 O  O   . LEU   B 1 25  ? 29.416 -14.658 7.067  1.00 19.65 ? 31  LEU   C O   1 
ATOM   1275 C  CB  . LEU   B 1 25  ? 28.160 -13.415 9.594  1.00 17.30 ? 31  LEU   C CB  1 
ATOM   1276 C  CG  . LEU   B 1 25  ? 26.741 -13.198 9.061  1.00 17.87 ? 31  LEU   C CG  1 
ATOM   1277 C  CD1 . LEU   B 1 25  ? 25.737 -14.096 9.818  1.00 18.20 ? 31  LEU   C CD1 1 
ATOM   1278 C  CD2 . LEU   B 1 25  ? 26.332 -11.736 9.225  1.00 17.39 ? 31  LEU   C CD2 1 
ATOM   1279 N  N   . VAL   B 1 26  ? 27.706 -16.064 7.537  1.00 16.10 ? 32  VAL   C N   1 
ATOM   1280 C  CA  . VAL   B 1 26  ? 27.441 -16.440 6.146  1.00 16.66 ? 32  VAL   C CA  1 
ATOM   1281 C  C   . VAL   B 1 26  ? 26.109 -15.809 5.727  1.00 16.67 ? 32  VAL   C C   1 
ATOM   1282 O  O   . VAL   B 1 26  ? 26.007 -15.186 4.659  1.00 18.41 ? 32  VAL   C O   1 
ATOM   1283 C  CB  . VAL   B 1 26  ? 27.371 -17.985 5.998  1.00 17.78 ? 32  VAL   C CB  1 
ATOM   1284 C  CG1 . VAL   B 1 26  ? 26.820 -18.376 4.619  1.00 18.43 ? 32  VAL   C CG1 1 
ATOM   1285 C  CG2 . VAL   B 1 26  ? 28.756 -18.609 6.258  1.00 18.44 ? 32  VAL   C CG2 1 
ATOM   1286 N  N   . TRP   B 1 27  ? 25.087 -15.948 6.590  1.00 14.97 ? 33  TRP   C N   1 
ATOM   1287 C  CA  . TRP   B 1 27  ? 23.739 -15.463 6.321  1.00 15.34 ? 33  TRP   C CA  1 
ATOM   1288 C  C   . TRP   B 1 27  ? 22.953 -15.374 7.637  1.00 15.69 ? 33  TRP   C C   1 
ATOM   1289 O  O   . TRP   B 1 27  ? 23.126 -16.207 8.518  1.00 16.54 ? 33  TRP   C O   1 
ATOM   1290 C  CB  . TRP   B 1 27  ? 23.026 -16.445 5.351  1.00 16.39 ? 33  TRP   C CB  1 
ATOM   1291 C  CG  . TRP   B 1 27  ? 21.546 -16.213 5.155  1.00 18.16 ? 33  TRP   C CG  1 
ATOM   1292 C  CD1 . TRP   B 1 27  ? 20.954 -15.324 4.300  1.00 20.62 ? 33  TRP   C CD1 1 
ATOM   1293 C  CD2 . TRP   B 1 27  ? 20.472 -16.926 5.799  1.00 18.24 ? 33  TRP   C CD2 1 
ATOM   1294 N  NE1 . TRP   B 1 27  ? 19.575 -15.406 4.414  1.00 21.02 ? 33  TRP   C NE1 1 
ATOM   1295 C  CE2 . TRP   B 1 27  ? 19.258 -16.381 5.329  1.00 19.46 ? 33  TRP   C CE2 1 
ATOM   1296 C  CE3 . TRP   B 1 27  ? 20.423 -17.952 6.758  1.00 18.37 ? 33  TRP   C CE3 1 
ATOM   1297 C  CZ2 . TRP   B 1 27  ? 18.008 -16.902 5.710  1.00 19.11 ? 33  TRP   C CZ2 1 
ATOM   1298 C  CZ3 . TRP   B 1 27  ? 19.186 -18.431 7.162  1.00 18.32 ? 33  TRP   C CZ3 1 
ATOM   1299 C  CH2 . TRP   B 1 27  ? 17.999 -17.904 6.643  1.00 18.04 ? 33  TRP   C CH2 1 
ATOM   1300 N  N   . GLU   B 1 28  ? 22.101 -14.363 7.768  1.00 15.06 ? 34  GLU   C N   1 
ATOM   1301 C  CA  . GLU   B 1 28  ? 21.212 -14.281 8.925  1.00 15.48 ? 34  GLU   C CA  1 
ATOM   1302 C  C   . GLU   B 1 28  ? 19.880 -13.682 8.510  1.00 15.86 ? 34  GLU   C C   1 
ATOM   1303 O  O   . GLU   B 1 28  ? 19.817 -12.874 7.564  1.00 15.80 ? 34  GLU   C O   1 
ATOM   1304 C  CB  . GLU   B 1 28  ? 21.830 -13.517 10.112 1.00 15.96 ? 34  GLU   C CB  1 
ATOM   1305 C  CG  . GLU   B 1 28  ? 22.371 -12.123 9.782  1.00 17.56 ? 34  GLU   C CG  1 
ATOM   1306 C  CD  . GLU   B 1 28  ? 21.348 -11.000 9.684  1.00 19.21 ? 34  GLU   C CD  1 
ATOM   1307 O  OE1 . GLU   B 1 28  ? 21.591 -10.035 8.919  1.00 22.17 ? 34  GLU   C OE1 1 
ATOM   1308 O  OE2 . GLU   B 1 28  ? 20.303 -11.068 10.377 1.00 16.68 ? 34  GLU   C OE2 1 
ATOM   1309 N  N   . ASP   B 1 29  ? 18.814 -14.064 9.217  1.00 15.32 ? 35  ASP   C N   1 
ATOM   1310 C  CA  . ASP   B 1 29  ? 17.486 -13.523 8.921  1.00 14.82 ? 35  ASP   C CA  1 
ATOM   1311 C  C   . ASP   B 1 29  ? 16.716 -13.387 10.239 1.00 14.18 ? 35  ASP   C C   1 
ATOM   1312 O  O   . ASP   B 1 29  ? 16.291 -14.377 10.839 1.00 13.66 ? 35  ASP   C O   1 
ATOM   1313 C  CB  . ASP   B 1 29  ? 16.753 -14.390 7.880  1.00 15.91 ? 35  ASP   C CB  1 
ATOM   1314 C  CG  . ASP   B 1 29  ? 15.437 -13.801 7.406  1.00 20.72 ? 35  ASP   C CG  1 
ATOM   1315 O  OD1 . ASP   B 1 29  ? 14.857 -12.987 8.142  1.00 21.45 ? 35  ASP   C OD1 1 
ATOM   1316 O  OD2 . ASP   B 1 29  ? 14.974 -14.184 6.294  1.00 22.11 ? 35  ASP   C OD2 1 
ATOM   1317 N  N   . SER   B 1 30  ? 16.575 -12.131 10.708 1.00 13.96 ? 36  SER   C N   1 
ATOM   1318 C  CA  A SER   B 1 30  ? 15.893 -11.832 11.953 0.50 14.51 ? 36  SER   C CA  1 
ATOM   1319 C  CA  B SER   B 1 30  ? 15.898 -11.871 11.971 0.50 14.50 ? 36  SER   C CA  1 
ATOM   1320 C  C   . SER   B 1 30  ? 14.440 -12.309 11.904 1.00 14.66 ? 36  SER   C C   1 
ATOM   1321 O  O   . SER   B 1 30  ? 13.920 -12.789 12.899 1.00 16.19 ? 36  SER   C O   1 
ATOM   1322 C  CB  A SER   B 1 30  ? 15.929 -10.328 12.214 0.50 15.94 ? 36  SER   C CB  1 
ATOM   1323 C  CB  B SER   B 1 30  ? 15.981 -10.390 12.345 0.50 16.01 ? 36  SER   C CB  1 
ATOM   1324 O  OG  A SER   B 1 30  ? 15.203 -10.006 13.385 0.50 17.54 ? 36  SER   C OG  1 
ATOM   1325 O  OG  B SER   B 1 30  ? 15.220 -9.594  11.451 0.50 17.43 ? 36  SER   C OG  1 
ATOM   1326 N  N   . SER   B 1 31  ? 13.797 -12.181 10.720 1.00 13.29 ? 37  SER   C N   1 
ATOM   1327 C  CA  . SER   B 1 31  ? 12.394 -12.588 10.599 1.00 14.44 ? 37  SER   C CA  1 
ATOM   1328 C  C   . SER   B 1 31  ? 12.231 -14.107 10.778 1.00 14.52 ? 37  SER   C C   1 
ATOM   1329 O  O   . SER   B 1 31  ? 11.120 -14.535 11.096 1.00 15.99 ? 37  SER   C O   1 
ATOM   1330 C  CB  . SER   B 1 31  ? 11.805 -12.121 9.267  1.00 17.46 ? 37  SER   C CB  1 
ATOM   1331 O  OG  . SER   B 1 31  ? 12.168 -12.963 8.178  1.00 22.29 ? 37  SER   C OG  1 
ATOM   1332 N  N   . ARG   B 1 32  ? 13.324 -14.904 10.602 1.00 12.93 ? 38  ARG   C N   1 
ATOM   1333 C  CA  . ARG   B 1 32  ? 13.233 -16.373 10.753 1.00 12.95 ? 38  ARG   C CA  1 
ATOM   1334 C  C   . ARG   B 1 32  ? 13.889 -16.875 12.056 1.00 13.24 ? 38  ARG   C C   1 
ATOM   1335 O  O   . ARG   B 1 32  ? 13.843 -18.078 12.345 1.00 13.61 ? 38  ARG   C O   1 
ATOM   1336 C  CB  . ARG   B 1 32  ? 13.930 -17.068 9.557  1.00 13.44 ? 38  ARG   C CB  1 
ATOM   1337 C  CG  . ARG   B 1 32  ? 13.246 -16.769 8.223  1.00 14.71 ? 38  ARG   C CG  1 
ATOM   1338 C  CD  . ARG   B 1 32  ? 13.965 -17.447 7.041  1.00 14.73 ? 38  ARG   C CD  1 
ATOM   1339 N  NE  . ARG   B 1 32  ? 13.929 -18.913 7.153  1.00 13.64 ? 38  ARG   C NE  1 
ATOM   1340 C  CZ  . ARG   B 1 32  ? 13.982 -19.742 6.105  1.00 14.19 ? 38  ARG   C CZ  1 
ATOM   1341 N  NH1 . ARG   B 1 32  ? 14.054 -19.255 4.862  1.00 15.61 ? 38  ARG   C NH1 1 
ATOM   1342 N  NH2 . ARG   B 1 32  ? 13.907 -21.062 6.290  1.00 15.26 ? 38  ARG   C NH2 1 
ATOM   1343 N  N   . ASP   B 1 33  ? 14.554 -15.963 12.812 1.00 13.67 ? 39  ASP   C N   1 
ATOM   1344 C  CA  . ASP   B 1 33  ? 15.336 -16.348 13.996 1.00 13.08 ? 39  ASP   C CA  1 
ATOM   1345 C  C   . ASP   B 1 33  ? 16.433 -17.330 13.615 1.00 12.64 ? 39  ASP   C C   1 
ATOM   1346 O  O   . ASP   B 1 33  ? 16.794 -18.184 14.434 1.00 12.71 ? 39  ASP   C O   1 
ATOM   1347 C  CB  . ASP   B 1 33  ? 14.494 -16.890 15.178 1.00 13.29 ? 39  ASP   C CB  1 
ATOM   1348 C  CG  . ASP   B 1 33  ? 15.317 -17.216 16.422 1.00 13.04 ? 39  ASP   C CG  1 
ATOM   1349 O  OD1 . ASP   B 1 33  ? 16.199 -16.390 16.787 1.00 13.38 ? 39  ASP   C OD1 1 
ATOM   1350 O  OD2 . ASP   B 1 33  ? 15.063 -18.286 17.069 1.00 13.36 ? 39  ASP   C OD2 1 
ATOM   1351 N  N   . LEU   B 1 34  ? 17.040 -17.185 12.386 1.00 12.01 ? 40  LEU   C N   1 
ATOM   1352 C  CA  . LEU   B 1 34  ? 18.144 -18.073 11.997 1.00 11.62 ? 40  LEU   C CA  1 
ATOM   1353 C  C   . LEU   B 1 34  ? 19.433 -17.287 11.716 1.00 12.62 ? 40  LEU   C C   1 
ATOM   1354 O  O   . LEU   B 1 34  ? 19.394 -16.205 11.140 1.00 13.65 ? 40  LEU   C O   1 
ATOM   1355 C  CB  . LEU   B 1 34  ? 17.821 -18.853 10.712 1.00 11.80 ? 40  LEU   C CB  1 
ATOM   1356 C  CG  . LEU   B 1 34  ? 16.746 -19.954 10.848 1.00 13.16 ? 40  LEU   C CG  1 
ATOM   1357 C  CD1 . LEU   B 1 34  ? 16.529 -20.632 9.475  1.00 13.28 ? 40  LEU   C CD1 1 
ATOM   1358 C  CD2 . LEU   B 1 34  ? 17.167 -21.043 11.855 1.00 13.65 ? 40  LEU   C CD2 1 
ATOM   1359 N  N   . LEU   B 1 35  ? 20.569 -17.957 11.965 1.00 12.50 ? 41  LEU   C N   1 
ATOM   1360 C  CA  . LEU   B 1 35  ? 21.868 -17.405 11.601 1.00 13.07 ? 41  LEU   C CA  1 
ATOM   1361 C  C   . LEU   B 1 35  ? 22.747 -18.618 11.202 1.00 13.08 ? 41  LEU   C C   1 
ATOM   1362 O  O   . LEU   B 1 35  ? 22.677 -19.683 11.832 1.00 13.53 ? 41  LEU   C O   1 
ATOM   1363 C  CB  . LEU   B 1 35  ? 22.511 -16.620 12.763 1.00 13.28 ? 41  LEU   C CB  1 
ATOM   1364 C  CG  . LEU   B 1 35  ? 23.885 -16.002 12.478 1.00 14.48 ? 41  LEU   C CG  1 
ATOM   1365 C  CD1 . LEU   B 1 35  ? 24.080 -14.668 13.238 1.00 15.05 ? 41  LEU   C CD1 1 
ATOM   1366 C  CD2 . LEU   B 1 35  ? 25.017 -16.949 12.895 1.00 15.42 ? 41  LEU   C CD2 1 
ATOM   1367 N  N   . VAL   B 1 36  ? 23.518 -18.469 10.119 1.00 12.06 ? 42  VAL   C N   1 
ATOM   1368 C  CA  . VAL   B 1 36  ? 24.441 -19.502 9.658  1.00 13.22 ? 42  VAL   C CA  1 
ATOM   1369 C  C   . VAL   B 1 36  ? 25.840 -18.902 9.669  1.00 14.35 ? 42  VAL   C C   1 
ATOM   1370 O  O   . VAL   B 1 36  ? 26.051 -17.804 9.103  1.00 13.60 ? 42  VAL   C O   1 
ATOM   1371 C  CB  . VAL   B 1 36  ? 24.066 -20.025 8.242  1.00 14.07 ? 42  VAL   C CB  1 
ATOM   1372 C  CG1 . VAL   B 1 36  ? 25.085 -21.058 7.749  1.00 15.48 ? 42  VAL   C CG1 1 
ATOM   1373 C  CG2 . VAL   B 1 36  ? 22.665 -20.623 8.261  1.00 13.27 ? 42  VAL   C CG2 1 
ATOM   1374 N  N   . SER   B 1 37  ? 26.786 -19.617 10.323 1.00 14.63 ? 43  SER   C N   1 
ATOM   1375 C  CA  . SER   B 1 37  ? 28.192 -19.204 10.333 1.00 14.92 ? 43  SER   C CA  1 
ATOM   1376 C  C   . SER   B 1 37  ? 29.062 -20.312 9.670  1.00 16.13 ? 43  SER   C C   1 
ATOM   1377 O  O   . SER   B 1 37  ? 28.588 -21.444 9.454  1.00 15.95 ? 43  SER   C O   1 
ATOM   1378 C  CB  . SER   B 1 37  ? 28.672 -18.918 11.751 1.00 16.32 ? 43  SER   C CB  1 
ATOM   1379 O  OG  . SER   B 1 37  ? 28.565 -20.070 12.580 1.00 18.66 ? 43  SER   C OG  1 
ATOM   1380 N  N   . SER   B 1 38  ? 30.301 -19.955 9.299  1.00 16.75 ? 44  SER   C N   1 
ATOM   1381 C  CA  . SER   B 1 38  ? 31.176 -20.929 8.644  1.00 18.81 ? 44  SER   C CA  1 
ATOM   1382 C  C   . SER   B 1 38  ? 32.016 -21.687 9.699  1.00 20.74 ? 44  SER   C C   1 
ATOM   1383 O  O   . SER   B 1 38  ? 32.326 -21.148 10.773 1.00 21.04 ? 44  SER   C O   1 
ATOM   1384 C  CB  . SER   B 1 38  ? 32.097 -20.221 7.655  1.00 20.28 ? 44  SER   C CB  1 
ATOM   1385 O  OG  . SER   B 1 38  ? 32.817 -19.211 8.329  1.00 24.38 ? 44  SER   C OG  1 
ATOM   1386 N  N   . THR   B 1 39  ? 32.382 -22.949 9.385  1.00 22.26 ? 45  THR   C N   1 
ATOM   1387 C  CA  . THR   B 1 39  ? 33.186 -23.771 10.290 1.00 24.41 ? 45  THR   C CA  1 
ATOM   1388 C  C   . THR   B 1 39  ? 34.423 -24.291 9.534  1.00 26.86 ? 45  THR   C C   1 
ATOM   1389 O  O   . THR   B 1 39  ? 34.419 -24.365 8.297  1.00 27.33 ? 45  THR   C O   1 
ATOM   1390 C  CB  . THR   B 1 39  ? 32.366 -24.995 10.758 1.00 26.21 ? 45  THR   C CB  1 
ATOM   1391 O  OG1 . THR   B 1 39  ? 32.084 -25.813 9.619  1.00 27.68 ? 45  THR   C OG1 1 
ATOM   1392 C  CG2 . THR   B 1 39  ? 31.056 -24.619 11.437 1.00 26.89 ? 45  THR   C CG2 1 
ATOM   1393 N  N   . THR   B 1 40  ? 35.453 -24.698 10.273 1.00 28.47 ? 46  THR   C N   1 
ATOM   1394 C  CA  . THR   B 1 40  ? 36.630 -25.317 9.657  1.00 30.79 ? 46  THR   C CA  1 
ATOM   1395 C  C   . THR   B 1 40  ? 36.376 -26.840 9.519  1.00 31.70 ? 46  THR   C C   1 
ATOM   1396 O  O   . THR   B 1 40  ? 36.778 -27.449 8.525  1.00 32.60 ? 46  THR   C O   1 
ATOM   1397 C  CB  . THR   B 1 40  ? 37.888 -25.019 10.482 1.00 33.86 ? 46  THR   C CB  1 
ATOM   1398 O  OG1 . THR   B 1 40  ? 37.621 -25.325 11.860 1.00 37.18 ? 46  THR   C OG1 1 
ATOM   1399 C  CG2 . THR   B 1 40  ? 38.331 -23.567 10.352 1.00 34.00 ? 46  THR   C CG2 1 
ATOM   1400 N  N   . ALA   B 1 41  ? 35.699 -27.446 10.509 1.00 31.16 ? 47  ALA   C N   1 
ATOM   1401 C  CA  . ALA   B 1 41  ? 35.387 -28.874 10.495 1.00 31.39 ? 47  ALA   C CA  1 
ATOM   1402 C  C   . ALA   B 1 41  ? 34.172 -29.200 9.618  1.00 31.41 ? 47  ALA   C C   1 
ATOM   1403 O  O   . ALA   B 1 41  ? 33.277 -28.374 9.467  1.00 31.56 ? 47  ALA   C O   1 
ATOM   1404 C  CB  . ALA   B 1 41  ? 35.156 -29.371 11.918 1.00 31.80 ? 47  ALA   C CB  1 
ATOM   1405 N  N   . GLN   B 1 42  ? 34.122 -30.429 9.091  1.00 31.01 ? 48  GLN   C N   1 
ATOM   1406 C  CA  . GLN   B 1 42  ? 33.046 -30.897 8.219  1.00 31.10 ? 48  GLN   C CA  1 
ATOM   1407 C  C   . GLN   B 1 42  ? 31.851 -31.408 9.013  1.00 29.45 ? 48  GLN   C C   1 
ATOM   1408 O  O   . GLN   B 1 42  ? 31.998 -32.331 9.815  1.00 29.57 ? 48  GLN   C O   1 
ATOM   1409 C  CB  . GLN   B 1 42  ? 33.574 -32.011 7.298  1.00 34.50 ? 48  GLN   C CB  1 
ATOM   1410 C  CG  . GLN   B 1 42  ? 32.516 -32.639 6.391  1.00 40.67 ? 48  GLN   C CG  1 
ATOM   1411 C  CD  . GLN   B 1 42  ? 32.187 -31.782 5.185  1.00 48.07 ? 48  GLN   C CD  1 
ATOM   1412 O  OE1 . GLN   B 1 42  ? 32.878 -30.799 4.857  1.00 49.99 ? 48  GLN   C OE1 1 
ATOM   1413 N  NE2 . GLN   B 1 42  ? 31.129 -32.161 4.479  1.00 49.88 ? 48  GLN   C NE2 1 
ATOM   1414 N  N   . GLY   B 1 43  ? 30.678 -30.841 8.747  1.00 26.90 ? 49  GLY   C N   1 
ATOM   1415 C  CA  . GLY   B 1 43  ? 29.436 -31.241 9.395  1.00 25.53 ? 49  GLY   C CA  1 
ATOM   1416 C  C   . GLY   B 1 43  ? 28.804 -32.412 8.676  1.00 23.89 ? 49  GLY   C C   1 
ATOM   1417 O  O   . GLY   B 1 43  ? 28.822 -32.470 7.442  1.00 24.24 ? 49  GLY   C O   1 
ATOM   1418 N  N   . CYS   B 1 44  ? 28.235 -33.340 9.437  1.00 21.84 ? 50  CYS   C N   1 
ATOM   1419 C  CA  . CYS   B 1 44  ? 27.649 -34.533 8.868  1.00 22.14 ? 50  CYS   C CA  1 
ATOM   1420 C  C   . CYS   B 1 44  ? 26.130 -34.655 9.052  1.00 20.56 ? 50  CYS   C C   1 
ATOM   1421 O  O   . CYS   B 1 44  ? 25.590 -35.749 8.777  1.00 20.78 ? 50  CYS   C O   1 
ATOM   1422 C  CB  . CYS   B 1 44  ? 28.365 -35.777 9.376  1.00 23.99 ? 50  CYS   C CB  1 
ATOM   1423 S  SG  . CYS   B 1 44  ? 30.119 -35.831 8.941  1.00 28.52 ? 50  CYS   C SG  1 
ATOM   1424 N  N   . ASP   B 1 45  ? 25.424 -33.581 9.483  1.00 17.64 ? 51  ASP   C N   1 
ATOM   1425 C  CA  . ASP   B 1 45  ? 23.956 -33.704 9.586  1.00 17.50 ? 51  ASP   C CA  1 
ATOM   1426 C  C   . ASP   B 1 45  ? 23.363 -33.739 8.184  1.00 18.80 ? 51  ASP   C C   1 
ATOM   1427 O  O   . ASP   B 1 45  ? 23.875 -33.067 7.278  1.00 20.68 ? 51  ASP   C O   1 
ATOM   1428 C  CB  . ASP   B 1 45  ? 23.334 -32.530 10.377 1.00 17.39 ? 51  ASP   C CB  1 
ATOM   1429 C  CG  . ASP   B 1 45  ? 23.722 -32.515 11.845 1.00 22.97 ? 51  ASP   C CG  1 
ATOM   1430 O  OD1 . ASP   B 1 45  ? 24.084 -33.590 12.378 1.00 23.84 ? 51  ASP   C OD1 1 
ATOM   1431 O  OD2 . ASP   B 1 45  ? 23.673 -31.427 12.466 1.00 22.78 ? 51  ASP   C OD2 1 
ATOM   1432 N  N   . THR   B 1 46  ? 22.286 -34.515 7.991  1.00 18.50 ? 52  THR   C N   1 
ATOM   1433 C  CA  . THR   B 1 46  ? 21.623 -34.556 6.699  1.00 19.13 ? 52  THR   C CA  1 
ATOM   1434 C  C   . THR   B 1 46  ? 20.389 -33.666 6.798  1.00 16.47 ? 52  THR   C C   1 
ATOM   1435 O  O   . THR   B 1 46  ? 19.619 -33.850 7.728  1.00 16.64 ? 52  THR   C O   1 
ATOM   1436 C  CB  . THR   B 1 46  ? 21.168 -35.996 6.388  1.00 23.05 ? 52  THR   C CB  1 
ATOM   1437 O  OG1 . THR   B 1 46  ? 22.335 -36.811 6.230  1.00 25.83 ? 52  THR   C OG1 1 
ATOM   1438 C  CG2 . THR   B 1 46  ? 20.298 -36.068 5.116  1.00 24.65 ? 52  THR   C CG2 1 
ATOM   1439 N  N   . ILE   B 1 47  ? 20.174 -32.757 5.836  1.00 14.81 ? 53  ILE   C N   1 
ATOM   1440 C  CA  . ILE   B 1 47  ? 18.991 -31.892 5.854  1.00 14.20 ? 53  ILE   C CA  1 
ATOM   1441 C  C   . ILE   B 1 47  ? 17.860 -32.557 5.061  1.00 14.18 ? 53  ILE   C C   1 
ATOM   1442 O  O   . ILE   B 1 47  ? 18.081 -33.035 3.933  1.00 14.82 ? 53  ILE   C O   1 
ATOM   1443 C  CB  . ILE   B 1 47  ? 19.296 -30.500 5.244  1.00 14.97 ? 53  ILE   C CB  1 
ATOM   1444 C  CG1 . ILE   B 1 47  ? 20.544 -29.844 5.888  1.00 16.77 ? 53  ILE   C CG1 1 
ATOM   1445 C  CG2 . ILE   B 1 47  ? 18.060 -29.560 5.318  1.00 15.32 ? 53  ILE   C CG2 1 
ATOM   1446 C  CD1 . ILE   B 1 47  ? 20.358 -29.605 7.411  1.00 18.03 ? 53  ILE   C CD1 1 
ATOM   1447 N  N   . ALA   B 1 48  ? 16.651 -32.572 5.632  1.00 12.73 ? 54  ALA   C N   1 
ATOM   1448 C  CA  . ALA   B 1 48  ? 15.498 -33.134 4.938  1.00 13.24 ? 54  ALA   C CA  1 
ATOM   1449 C  C   . ALA   B 1 48  ? 15.117 -32.209 3.771  1.00 13.05 ? 54  ALA   C C   1 
ATOM   1450 O  O   . ALA   B 1 48  ? 15.167 -30.990 3.937  1.00 13.01 ? 54  ALA   C O   1 
ATOM   1451 C  CB  . ALA   B 1 48  ? 14.333 -33.204 5.918  1.00 13.28 ? 54  ALA   C CB  1 
ATOM   1452 N  N   . ARG   B 1 49  ? 14.655 -32.773 2.629  1.00 12.38 ? 55  ARG   C N   1 
ATOM   1453 C  CA  . ARG   B 1 49  ? 14.166 -31.990 1.478  1.00 12.89 ? 55  ARG   C CA  1 
ATOM   1454 C  C   . ARG   B 1 49  ? 12.826 -32.658 1.192  1.00 13.43 ? 55  ARG   C C   1 
ATOM   1455 O  O   . ARG   B 1 49  ? 12.762 -33.655 0.459  1.00 13.64 ? 55  ARG   C O   1 
ATOM   1456 C  CB  . ARG   B 1 49  ? 15.144 -32.103 0.284  1.00 14.49 ? 55  ARG   C CB  1 
ATOM   1457 C  CG  . ARG   B 1 49  ? 16.565 -31.606 0.603  1.00 16.09 ? 55  ARG   C CG  1 
ATOM   1458 C  CD  . ARG   B 1 49  ? 16.643 -30.118 0.995  1.00 17.99 ? 55  ARG   C CD  1 
ATOM   1459 N  NE  . ARG   B 1 49  ? 18.035 -29.718 1.282  1.00 19.01 ? 55  ARG   C NE  1 
ATOM   1460 C  CZ  . ARG   B 1 49  ? 18.381 -28.598 1.912  1.00 19.74 ? 55  ARG   C CZ  1 
ATOM   1461 N  NH1 . ARG   B 1 49  ? 17.452 -27.751 2.330  1.00 16.34 ? 55  ARG   C NH1 1 
ATOM   1462 N  NH2 . ARG   B 1 49  ? 19.663 -28.325 2.145  1.00 19.12 ? 55  ARG   C NH2 1 
ATOM   1463 N  N   . CYS   B 1 50  ? 11.752 -32.112 1.805  1.00 13.70 ? 56  CYS   C N   1 
ATOM   1464 C  CA  . CYS   B 1 50  ? 10.454 -32.771 1.800  1.00 13.84 ? 56  CYS   C CA  1 
ATOM   1465 C  C   . CYS   B 1 50  ? 9.338  -31.828 2.293  1.00 14.65 ? 56  CYS   C C   1 
ATOM   1466 O  O   . CYS   B 1 50  ? 9.617  -30.712 2.739  1.00 14.38 ? 56  CYS   C O   1 
ATOM   1467 C  CB  . CYS   B 1 50  ? 10.542 -33.972 2.741  1.00 13.89 ? 56  CYS   C CB  1 
ATOM   1468 S  SG  . CYS   B 1 50  ? 10.742 -33.486 4.484  1.00 13.55 ? 56  CYS   C SG  1 
ATOM   1469 N  N   . ASP   B 1 51  ? 8.082  -32.347 2.306  1.00 15.16 ? 57  ASP   C N   1 
ATOM   1470 C  CA  . ASP   B 1 51  ? 6.966  -31.625 2.894  1.00 15.38 ? 57  ASP   C CA  1 
ATOM   1471 C  C   . ASP   B 1 51  ? 6.352  -32.404 4.069  1.00 15.41 ? 57  ASP   C C   1 
ATOM   1472 O  O   . ASP   B 1 51  ? 5.162  -32.248 4.344  1.00 15.59 ? 57  ASP   C O   1 
ATOM   1473 C  CB  . ASP   B 1 51  ? 5.888  -31.261 1.871  1.00 17.41 ? 57  ASP   C CB  1 
ATOM   1474 C  CG  . ASP   B 1 51  ? 5.242  -32.442 1.196  1.00 21.92 ? 57  ASP   C CG  1 
ATOM   1475 O  OD1 . ASP   B 1 51  ? 5.624  -33.599 1.508  1.00 22.65 ? 57  ASP   C OD1 1 
ATOM   1476 O  OD2 . ASP   B 1 51  ? 4.314  -32.221 0.380  1.00 26.17 ? 57  ASP   C OD2 1 
ATOM   1477 N  N   . CYS   B 1 52  ? 7.148  -33.211 4.804  1.00 13.69 ? 58  CYS   C N   1 
ATOM   1478 C  CA  . CYS   B 1 52  ? 6.659  -33.946 5.991  1.00 12.62 ? 58  CYS   C CA  1 
ATOM   1479 C  C   . CYS   B 1 52  ? 6.025  -33.029 6.971  1.00 12.56 ? 58  CYS   C C   1 
ATOM   1480 O  O   . CYS   B 1 52  ? 6.472  -31.875 7.144  1.00 12.42 ? 58  CYS   C O   1 
ATOM   1481 C  CB  . CYS   B 1 52  ? 7.803  -34.677 6.689  1.00 12.86 ? 58  CYS   C CB  1 
ATOM   1482 S  SG  . CYS   B 1 52  ? 8.342  -36.161 5.834  1.00 15.24 ? 58  CYS   C SG  1 
ATOM   1483 N  N   . GLN   B 1 53  ? 4.998  -33.561 7.645  1.00 11.82 ? 59  GLN   C N   1 
ATOM   1484 C  CA  . GLN   B 1 53  ? 4.325  -32.905 8.751  1.00 11.67 ? 59  GLN   C CA  1 
ATOM   1485 C  C   . GLN   B 1 53  ? 4.302  -33.781 9.999  1.00 12.64 ? 59  GLN   C C   1 
ATOM   1486 O  O   . GLN   B 1 53  ? 3.496  -33.523 10.901 1.00 12.99 ? 59  GLN   C O   1 
ATOM   1487 C  CB  . GLN   B 1 53  ? 2.916  -32.437 8.369  1.00 13.00 ? 59  GLN   C CB  1 
ATOM   1488 C  CG  . GLN   B 1 53  ? 2.913  -31.144 7.499  1.00 15.74 ? 59  GLN   C CG  1 
ATOM   1489 C  CD  . GLN   B 1 53  ? 1.492  -30.724 7.238  1.00 18.38 ? 59  GLN   C CD  1 
ATOM   1490 O  OE1 . GLN   B 1 53  ? 0.957  -30.928 6.121  1.00 18.74 ? 59  GLN   C OE1 1 
ATOM   1491 N  NE2 . GLN   B 1 53  ? 0.834  -30.172 8.275  1.00 17.61 ? 59  GLN   C NE2 1 
ATOM   1492 N  N   . THR   B 1 54  ? 5.164  -34.820 10.073 1.00 12.10 ? 60  THR   C N   1 
ATOM   1493 C  CA  . THR   B 1 54  ? 5.319  -35.636 11.285 1.00 13.30 ? 60  THR   C CA  1 
ATOM   1494 C  C   . THR   B 1 54  ? 6.834  -35.836 11.475 1.00 13.20 ? 60  THR   C C   1 
ATOM   1495 O  O   . THR   B 1 54  ? 7.596  -35.954 10.501 1.00 12.84 ? 60  THR   C O   1 
ATOM   1496 C  CB  . THR   B 1 54  ? 4.636  -37.004 11.176 1.00 17.82 ? 60  THR   C CB  1 
ATOM   1497 O  OG1 . THR   B 1 54  ? 5.276  -37.796 10.163 1.00 20.72 ? 60  THR   C OG1 1 
ATOM   1498 C  CG2 . THR   B 1 54  ? 3.158  -36.899 10.860 1.00 18.18 ? 60  THR   C CG2 1 
ATOM   1499 N  N   . GLY   B 1 55  ? 7.249  -35.854 12.727 1.00 11.61 ? 61  GLY   C N   1 
ATOM   1500 C  CA  . GLY   B 1 55  ? 8.671  -36.010 13.040 1.00 11.23 ? 61  GLY   C CA  1 
ATOM   1501 C  C   . GLY   B 1 55  ? 8.892  -36.153 14.530 1.00 11.87 ? 61  GLY   C C   1 
ATOM   1502 O  O   . GLY   B 1 55  ? 7.943  -36.373 15.271 1.00 12.18 ? 61  GLY   C O   1 
ATOM   1503 N  N   . VAL   B 1 56  ? 10.132 -36.032 14.947 1.00 10.87 ? 62  VAL   C N   1 
ATOM   1504 C  CA  . VAL   B 1 56  ? 10.481 -36.169 16.369 1.00 10.37 ? 62  VAL   C CA  1 
ATOM   1505 C  C   . VAL   B 1 56  ? 11.383 -34.976 16.743 1.00 10.73 ? 62  VAL   C C   1 
ATOM   1506 O  O   . VAL   B 1 56  ? 12.352 -34.730 16.031 1.00 11.39 ? 62  VAL   C O   1 
ATOM   1507 C  CB  . VAL   B 1 56  ? 11.256 -37.495 16.587 1.00 11.18 ? 62  VAL   C CB  1 
ATOM   1508 C  CG1 . VAL   B 1 56  ? 11.730 -37.617 18.048 1.00 12.13 ? 62  VAL   C CG1 1 
ATOM   1509 C  CG2 . VAL   B 1 56  ? 10.373 -38.677 16.208 1.00 11.38 ? 62  VAL   C CG2 1 
ATOM   1510 N  N   . TYR   B 1 57  ? 11.154 -34.352 17.922 1.00 10.26 ? 63  TYR   C N   1 
ATOM   1511 C  CA  . TYR   B 1 57  ? 12.057 -33.270 18.360 1.00 10.68 ? 63  TYR   C CA  1 
ATOM   1512 C  C   . TYR   B 1 57  ? 12.690 -33.544 19.702 1.00 10.87 ? 63  TYR   C C   1 
ATOM   1513 O  O   . TYR   B 1 57  ? 12.104 -34.265 20.516 1.00 11.62 ? 63  TYR   C O   1 
ATOM   1514 C  CB  . TYR   B 1 57  ? 11.371 -31.856 18.364 1.00 11.14 ? 63  TYR   C CB  1 
ATOM   1515 C  CG  . TYR   B 1 57  ? 10.454 -31.578 19.547 1.00 11.54 ? 63  TYR   C CG  1 
ATOM   1516 C  CD1 . TYR   B 1 57  ? 9.159  -32.090 19.593 1.00 12.85 ? 63  TYR   C CD1 1 
ATOM   1517 C  CD2 . TYR   B 1 57  ? 10.851 -30.728 20.570 1.00 11.51 ? 63  TYR   C CD2 1 
ATOM   1518 C  CE1 . TYR   B 1 57  ? 8.291  -31.782 20.650 1.00 13.34 ? 63  TYR   C CE1 1 
ATOM   1519 C  CE2 . TYR   B 1 57  ? 10.007 -30.434 21.641 1.00 11.91 ? 63  TYR   C CE2 1 
ATOM   1520 C  CZ  . TYR   B 1 57  ? 8.718  -30.951 21.671 1.00 14.18 ? 63  TYR   C CZ  1 
ATOM   1521 O  OH  . TYR   B 1 57  ? 7.891  -30.681 22.737 1.00 16.48 ? 63  TYR   C OH  1 
ATOM   1522 N  N   . TYR   B 1 58  ? 13.859 -32.942 19.944 1.00 11.06 ? 64  TYR   C N   1 
ATOM   1523 C  CA  . TYR   B 1 58  ? 14.537 -33.102 21.230 1.00 11.55 ? 64  TYR   C CA  1 
ATOM   1524 C  C   . TYR   B 1 58  ? 14.129 -31.945 22.151 1.00 12.59 ? 64  TYR   C C   1 
ATOM   1525 O  O   . TYR   B 1 58  ? 14.275 -30.776 21.790 1.00 11.86 ? 64  TYR   C O   1 
ATOM   1526 C  CB  . TYR   B 1 58  ? 16.062 -33.168 21.079 1.00 12.01 ? 64  TYR   C CB  1 
ATOM   1527 C  CG  . TYR   B 1 58  ? 16.716 -33.353 22.436 1.00 13.14 ? 64  TYR   C CG  1 
ATOM   1528 C  CD1 . TYR   B 1 58  ? 16.488 -34.500 23.190 1.00 14.59 ? 64  TYR   C CD1 1 
ATOM   1529 C  CD2 . TYR   B 1 58  ? 17.501 -32.353 22.991 1.00 15.11 ? 64  TYR   C CD2 1 
ATOM   1530 C  CE1 . TYR   B 1 58  ? 17.038 -34.658 24.469 1.00 15.84 ? 64  TYR   C CE1 1 
ATOM   1531 C  CE2 . TYR   B 1 58  ? 18.046 -32.492 24.274 1.00 16.24 ? 64  TYR   C CE2 1 
ATOM   1532 C  CZ  . TYR   B 1 58  ? 17.813 -33.648 25.004 1.00 17.44 ? 64  TYR   C CZ  1 
ATOM   1533 O  OH  . TYR   B 1 58  ? 18.385 -33.813 26.264 1.00 20.59 ? 64  TYR   C OH  1 
ATOM   1534 N  N   . CYS   B 1 59  ? 13.638 -32.308 23.369 1.00 12.56 ? 65  CYS   C N   1 
ATOM   1535 C  CA  . CYS   B 1 59  ? 13.223 -31.320 24.365 1.00 12.66 ? 65  CYS   C CA  1 
ATOM   1536 C  C   . CYS   B 1 59  ? 14.211 -31.385 25.572 1.00 14.22 ? 65  CYS   C C   1 
ATOM   1537 O  O   . CYS   B 1 59  ? 14.086 -32.288 26.417 1.00 15.92 ? 65  CYS   C O   1 
ATOM   1538 C  CB  . CYS   B 1 59  ? 11.788 -31.603 24.794 1.00 14.57 ? 65  CYS   C CB  1 
ATOM   1539 S  SG  . CYS   B 1 59  ? 11.188 -30.526 26.128 1.00 16.56 ? 65  CYS   C SG  1 
ATOM   1540 N  N   . SER   B 1 60  ? 15.185 -30.434 25.638 1.00 13.43 ? 66  SER   C N   1 
ATOM   1541 C  CA  . SER   B 1 60  ? 16.177 -30.510 26.711 1.00 15.18 ? 66  SER   C CA  1 
ATOM   1542 C  C   . SER   B 1 60  ? 15.586 -30.372 28.096 1.00 14.81 ? 66  SER   C C   1 
ATOM   1543 O  O   . SER   B 1 60  ? 16.075 -31.024 29.038 1.00 15.42 ? 66  SER   C O   1 
ATOM   1544 C  CB  . SER   B 1 60  ? 17.321 -29.518 26.515 1.00 19.75 ? 66  SER   C CB  1 
ATOM   1545 O  OG  . SER   B 1 60  ? 16.869 -28.193 26.669 1.00 24.37 ? 66  SER   C OG  1 
ATOM   1546 N  N   . SER   B 1 61  ? 14.494 -29.611 28.233 1.00 14.34 ? 67  SER   C N   1 
ATOM   1547 C  CA  . SER   B 1 61  ? 13.874 -29.438 29.571 1.00 14.27 ? 67  SER   C CA  1 
ATOM   1548 C  C   . SER   B 1 61  ? 13.173 -30.675 30.116 1.00 14.84 ? 67  SER   C C   1 
ATOM   1549 O  O   . SER   B 1 61  ? 12.724 -30.665 31.278 1.00 15.97 ? 67  SER   C O   1 
ATOM   1550 C  CB  . SER   B 1 61  ? 12.907 -28.264 29.573 1.00 15.48 ? 67  SER   C CB  1 
ATOM   1551 O  OG  . SER   B 1 61  ? 11.803 -28.464 28.713 1.00 16.92 ? 67  SER   C OG  1 
ATOM   1552 N  N   . ARG   B 1 62  ? 13.079 -31.729 29.307 1.00 14.23 ? 68  ARG   C N   1 
ATOM   1553 C  CA  . ARG   B 1 62  ? 12.529 -33.003 29.715 1.00 14.70 ? 68  ARG   C CA  1 
ATOM   1554 C  C   . ARG   B 1 62  ? 13.555 -34.156 29.464 1.00 16.53 ? 68  ARG   C C   1 
ATOM   1555 O  O   . ARG   B 1 62  ? 13.248 -35.315 29.774 1.00 18.05 ? 68  ARG   C O   1 
ATOM   1556 C  CB  . ARG   B 1 62  ? 11.228 -33.278 28.927 1.00 15.65 ? 68  ARG   C CB  1 
ATOM   1557 C  CG  . ARG   B 1 62  ? 10.090 -32.293 29.232 1.00 16.36 ? 68  ARG   C CG  1 
ATOM   1558 C  CD  . ARG   B 1 62  ? 9.522  -32.581 30.624 1.00 17.95 ? 68  ARG   C CD  1 
ATOM   1559 N  NE  . ARG   B 1 62  ? 8.417  -31.682 30.980 1.00 21.48 ? 68  ARG   C NE  1 
ATOM   1560 C  CZ  . ARG   B 1 62  ? 8.563  -30.525 31.612 1.00 26.10 ? 68  ARG   C CZ  1 
ATOM   1561 N  NH1 . ARG   B 1 62  ? 9.771  -30.098 31.960 1.00 25.21 ? 68  ARG   C NH1 1 
ATOM   1562 N  NH2 . ARG   B 1 62  ? 7.503  -29.788 31.911 1.00 28.40 ? 68  ARG   C NH2 1 
ATOM   1563 N  N   . ARG   B 1 63  ? 14.751 -33.863 28.870 1.00 16.29 ? 69  ARG   C N   1 
ATOM   1564 C  CA  . ARG   B 1 63  ? 15.764 -34.871 28.471 1.00 16.52 ? 69  ARG   C CA  1 
ATOM   1565 C  C   . ARG   B 1 63  ? 15.084 -35.997 27.678 1.00 17.08 ? 69  ARG   C C   1 
ATOM   1566 O  O   . ARG   B 1 63  ? 15.317 -37.174 27.948 1.00 18.09 ? 69  ARG   C O   1 
ATOM   1567 C  CB  . ARG   B 1 63  ? 16.506 -35.437 29.709 1.00 19.53 ? 69  ARG   C CB  1 
ATOM   1568 C  CG  . ARG   B 1 63  ? 17.282 -34.393 30.484 1.00 25.58 ? 69  ARG   C CG  1 
ATOM   1569 C  CD  . ARG   B 1 63  ? 18.591 -33.994 29.848 1.00 31.92 ? 69  ARG   C CD  1 
ATOM   1570 N  NE  . ARG   B 1 63  ? 19.431 -33.208 30.759 1.00 36.11 ? 69  ARG   C NE  1 
ATOM   1571 C  CZ  . ARG   B 1 63  ? 19.475 -31.879 30.780 1.00 39.15 ? 69  ARG   C CZ  1 
ATOM   1572 N  NH1 . ARG   B 1 63  ? 18.742 -31.167 29.930 1.00 36.36 ? 69  ARG   C NH1 1 
ATOM   1573 N  NH2 . ARG   B 1 63  ? 20.264 -31.249 31.642 1.00 40.97 ? 69  ARG   C NH2 1 
ATOM   1574 N  N   . LYS   B 1 64  ? 14.164 -35.616 26.752 1.00 16.68 ? 70  LYS   C N   1 
ATOM   1575 C  CA  . LYS   B 1 64  ? 13.374 -36.601 26.030 1.00 17.27 ? 70  LYS   C CA  1 
ATOM   1576 C  C   . LYS   B 1 64  ? 13.141 -36.119 24.608 1.00 15.56 ? 70  LYS   C C   1 
ATOM   1577 O  O   . LYS   B 1 64  ? 13.064 -34.914 24.362 1.00 15.25 ? 70  LYS   C O   1 
ATOM   1578 C  CB  . LYS   B 1 64  ? 11.949 -36.680 26.668 1.00 21.36 ? 70  LYS   C CB  1 
ATOM   1579 C  CG  . LYS   B 1 64  ? 11.765 -37.647 27.833 1.00 31.40 ? 70  LYS   C CG  1 
ATOM   1580 C  CD  . LYS   B 1 64  ? 10.281 -37.676 28.207 1.00 38.09 ? 70  LYS   C CD  1 
ATOM   1581 C  CE  . LYS   B 1 64  ? 9.860  -38.849 29.073 1.00 44.94 ? 70  LYS   C CE  1 
ATOM   1582 N  NZ  . LYS   B 1 64  ? 10.497 -38.822 30.422 1.00 48.11 ? 70  LYS   C NZ  1 
ATOM   1583 N  N   . HIS   B 1 65  ? 12.876 -37.083 23.721 1.00 14.32 ? 71  HIS   C N   1 
ATOM   1584 C  CA  . HIS   B 1 65  ? 12.443 -36.779 22.363 1.00 12.95 ? 71  HIS   C CA  1 
ATOM   1585 C  C   . HIS   B 1 65  ? 10.929 -37.029 22.332 1.00 14.41 ? 71  HIS   C C   1 
ATOM   1586 O  O   . HIS   B 1 65  ? 10.440 -38.007 22.938 1.00 17.11 ? 71  HIS   C O   1 
ATOM   1587 C  CB  . HIS   B 1 65  ? 13.104 -37.733 21.369 1.00 13.32 ? 71  HIS   C CB  1 
ATOM   1588 C  CG  . HIS   B 1 65  ? 14.594 -37.550 21.264 1.00 14.70 ? 71  HIS   C CG  1 
ATOM   1589 N  ND1 . HIS   B 1 65  ? 15.176 -36.813 20.230 1.00 17.12 ? 71  HIS   C ND1 1 
ATOM   1590 C  CD2 . HIS   B 1 65  ? 15.580 -38.054 22.045 1.00 15.73 ? 71  HIS   C CD2 1 
ATOM   1591 C  CE1 . HIS   B 1 65  ? 16.487 -36.906 20.418 1.00 15.41 ? 71  HIS   C CE1 1 
ATOM   1592 N  NE2 . HIS   B 1 65  ? 16.778 -37.614 21.496 1.00 17.09 ? 71  HIS   C NE2 1 
ATOM   1593 N  N   . TYR   B 1 66  ? 10.185 -36.202 21.574 1.00 11.90 ? 72  TYR   C N   1 
ATOM   1594 C  CA  . TYR   B 1 66  ? 8.735  -36.390 21.464 1.00 12.82 ? 72  TYR   C CA  1 
ATOM   1595 C  C   . TYR   B 1 66  ? 8.342  -36.486 20.002 1.00 12.71 ? 72  TYR   C C   1 
ATOM   1596 O  O   . TYR   B 1 66  ? 8.753  -35.634 19.193 1.00 12.73 ? 72  TYR   C O   1 
ATOM   1597 C  CB  . TYR   B 1 66  ? 7.991  -35.177 22.044 1.00 13.86 ? 72  TYR   C CB  1 
ATOM   1598 C  CG  . TYR   B 1 66  ? 8.090  -35.059 23.551 1.00 14.76 ? 72  TYR   C CG  1 
ATOM   1599 C  CD1 . TYR   B 1 66  ? 7.338  -35.876 24.382 1.00 16.46 ? 72  TYR   C CD1 1 
ATOM   1600 C  CD2 . TYR   B 1 66  ? 8.921  -34.109 24.146 1.00 15.88 ? 72  TYR   C CD2 1 
ATOM   1601 C  CE1 . TYR   B 1 66  ? 7.412  -35.758 25.772 1.00 17.15 ? 72  TYR   C CE1 1 
ATOM   1602 C  CE2 . TYR   B 1 66  ? 9.027  -34.007 25.528 1.00 16.72 ? 72  TYR   C CE2 1 
ATOM   1603 C  CZ  . TYR   B 1 66  ? 8.257  -34.825 26.333 1.00 17.94 ? 72  TYR   C CZ  1 
ATOM   1604 O  OH  . TYR   B 1 66  ? 8.296  -34.684 27.706 1.00 19.83 ? 72  TYR   C OH  1 
ATOM   1605 N  N   . PRO   B 1 67  ? 7.496  -37.488 19.660 1.00 12.13 ? 73  PRO   C N   1 
ATOM   1606 C  CA  . PRO   B 1 67  ? 6.988  -37.558 18.275 1.00 12.82 ? 73  PRO   C CA  1 
ATOM   1607 C  C   . PRO   B 1 67  ? 5.824  -36.554 18.136 1.00 13.59 ? 73  PRO   C C   1 
ATOM   1608 O  O   . PRO   B 1 67  ? 4.965  -36.506 19.039 1.00 14.81 ? 73  PRO   C O   1 
ATOM   1609 C  CB  . PRO   B 1 67  ? 6.455  -39.003 18.163 1.00 13.60 ? 73  PRO   C CB  1 
ATOM   1610 C  CG  . PRO   B 1 67  ? 6.129  -39.398 19.580 1.00 14.65 ? 73  PRO   C CG  1 
ATOM   1611 C  CD  . PRO   B 1 67  ? 6.961  -38.568 20.531 1.00 13.08 ? 73  PRO   C CD  1 
ATOM   1612 N  N   . VAL   B 1 68  ? 5.797  -35.751 17.076 1.00 12.39 ? 74  VAL   C N   1 
ATOM   1613 C  CA  . VAL   B 1 68  ? 4.706  -34.786 16.900 1.00 12.48 ? 74  VAL   C CA  1 
ATOM   1614 C  C   . VAL   B 1 68  ? 4.280  -34.630 15.451 1.00 12.22 ? 74  VAL   C C   1 
ATOM   1615 O  O   . VAL   B 1 68  ? 5.061  -34.879 14.534 1.00 13.75 ? 74  VAL   C O   1 
ATOM   1616 C  CB  . VAL   B 1 68  ? 5.162  -33.391 17.368 1.00 13.80 ? 74  VAL   C CB  1 
ATOM   1617 C  CG1 . VAL   B 1 68  ? 5.282  -33.310 18.901 1.00 14.69 ? 74  VAL   C CG1 1 
ATOM   1618 C  CG2 . VAL   B 1 68  ? 6.437  -32.922 16.631 1.00 14.15 ? 74  VAL   C CG2 1 
ATOM   1619 N  N   . SER   B 1 69  ? 3.026  -34.147 15.258 1.00 10.89 ? 75  SER   C N   1 
ATOM   1620 C  CA  . SER   B 1 69  ? 2.580  -33.626 13.963 1.00 12.14 ? 75  SER   C CA  1 
ATOM   1621 C  C   . SER   B 1 69  ? 2.904  -32.083 14.009 1.00 12.15 ? 75  SER   C C   1 
ATOM   1622 O  O   . SER   B 1 69  ? 2.818  -31.449 15.083 1.00 12.46 ? 75  SER   C O   1 
ATOM   1623 C  CB  . SER   B 1 69  ? 1.070  -33.792 13.795 1.00 15.87 ? 75  SER   C CB  1 
ATOM   1624 O  OG  . SER   B 1 69  ? 0.759  -35.168 13.700 1.00 19.20 ? 75  SER   C OG  1 
ATOM   1625 N  N   . PHE   B 1 70  ? 3.284  -31.490 12.876 1.00 11.04 ? 76  PHE   C N   1 
ATOM   1626 C  CA  . PHE   B 1 70  ? 3.590  -30.053 12.847 1.00 11.97 ? 76  PHE   C CA  1 
ATOM   1627 C  C   . PHE   B 1 70  ? 3.038  -29.374 11.604 1.00 12.09 ? 76  PHE   C C   1 
ATOM   1628 O  O   . PHE   B 1 70  ? 2.785  -30.045 10.599 1.00 13.62 ? 76  PHE   C O   1 
ATOM   1629 C  CB  . PHE   B 1 70  ? 5.087  -29.758 13.030 1.00 11.90 ? 76  PHE   C CB  1 
ATOM   1630 C  CG  . PHE   B 1 70  ? 6.004  -30.502 12.079 1.00 11.46 ? 76  PHE   C CG  1 
ATOM   1631 C  CD1 . PHE   B 1 70  ? 6.500  -31.749 12.402 1.00 11.78 ? 76  PHE   C CD1 1 
ATOM   1632 C  CD2 . PHE   B 1 70  ? 6.417  -29.922 10.896 1.00 11.41 ? 76  PHE   C CD2 1 
ATOM   1633 C  CE1 . PHE   B 1 70  ? 7.351  -32.437 11.521 1.00 12.98 ? 76  PHE   C CE1 1 
ATOM   1634 C  CE2 . PHE   B 1 70  ? 7.251  -30.599 10.018 1.00 11.13 ? 76  PHE   C CE2 1 
ATOM   1635 C  CZ  . PHE   B 1 70  ? 7.757  -31.840 10.347 1.00 11.47 ? 76  PHE   C CZ  1 
ATOM   1636 N  N   . SER   B 1 71  ? 2.808  -28.063 11.686 1.00 11.41 ? 77  SER   C N   1 
ATOM   1637 C  CA  . SER   B 1 71  ? 2.170  -27.364 10.593 1.00 12.27 ? 77  SER   C CA  1 
ATOM   1638 C  C   . SER   B 1 71  ? 3.107  -27.071 9.421  1.00 13.48 ? 77  SER   C C   1 
ATOM   1639 O  O   . SER   B 1 71  ? 4.266  -27.459 9.412  1.00 14.37 ? 77  SER   C O   1 
ATOM   1640 C  CB  . SER   B 1 71  ? 1.494  -26.102 11.120 1.00 13.62 ? 77  SER   C CB  1 
ATOM   1641 O  OG  . SER   B 1 71  ? 2.443  -25.196 11.654 1.00 15.13 ? 77  SER   C OG  1 
ATOM   1642 N  N   . LYS   B 1 72  ? 2.569  -26.426 8.378  1.00 13.38 ? 78  LYS   C N   1 
ATOM   1643 C  CA  . LYS   B 1 72  ? 3.385  -26.029 7.232  1.00 14.80 ? 78  LYS   C CA  1 
ATOM   1644 C  C   . LYS   B 1 72  ? 4.090  -24.711 7.580  1.00 15.20 ? 78  LYS   C C   1 
ATOM   1645 O  O   . LYS   B 1 72  ? 3.519  -23.870 8.298  1.00 17.65 ? 78  LYS   C O   1 
ATOM   1646 C  CB  . LYS   B 1 72  ? 2.462  -25.812 6.025  1.00 16.53 ? 78  LYS   C CB  1 
ATOM   1647 C  CG  . LYS   B 1 72  ? 1.734  -27.107 5.681  1.00 20.62 ? 78  LYS   C CG  1 
ATOM   1648 C  CD  . LYS   B 1 72  ? 0.990  -27.030 4.352  1.00 29.52 ? 78  LYS   C CD  1 
ATOM   1649 C  CE  . LYS   B 1 72  ? 1.285  -28.286 3.560  1.00 37.24 ? 78  LYS   C CE  1 
ATOM   1650 N  NZ  . LYS   B 1 72  ? 2.715  -28.312 3.126  1.00 41.27 ? 78  LYS   C NZ  1 
ATOM   1651 N  N   . PRO   B 1 73  ? 5.299  -24.456 7.049  1.00 13.88 ? 79  PRO   C N   1 
ATOM   1652 C  CA  . PRO   B 1 73  ? 6.011  -23.205 7.402  1.00 15.21 ? 79  PRO   C CA  1 
ATOM   1653 C  C   . PRO   B 1 73  ? 5.197  -21.978 7.034  1.00 16.37 ? 79  PRO   C C   1 
ATOM   1654 O  O   . PRO   B 1 73  ? 4.652  -21.882 5.923  1.00 17.38 ? 79  PRO   C O   1 
ATOM   1655 C  CB  . PRO   B 1 73  ? 7.312  -23.247 6.605  1.00 16.35 ? 79  PRO   C CB  1 
ATOM   1656 C  CG  . PRO   B 1 73  ? 7.347  -24.561 5.938  1.00 17.60 ? 79  PRO   C CG  1 
ATOM   1657 C  CD  . PRO   B 1 73  ? 6.087  -25.325 6.155  1.00 14.11 ? 79  PRO   C CD  1 
ATOM   1658 N  N   . SER   B 1 74  ? 5.071  -21.060 7.988  1.00 15.79 ? 80  SER   C N   1 
ATOM   1659 C  CA  . SER   B 1 74  ? 4.227  -19.887 7.746  1.00 17.57 ? 80  SER   C CA  1 
ATOM   1660 C  C   . SER   B 1 74  ? 4.610  -18.712 8.644  1.00 17.08 ? 80  SER   C C   1 
ATOM   1661 O  O   . SER   B 1 74  ? 5.529  -18.825 9.460  1.00 15.77 ? 80  SER   C O   1 
ATOM   1662 C  CB  . SER   B 1 74  ? 2.752  -20.268 7.921  1.00 22.13 ? 80  SER   C CB  1 
ATOM   1663 O  OG  . SER   B 1 74  ? 2.399  -20.472 9.282  1.00 27.09 ? 80  SER   C OG  1 
ATOM   1664 N  N   . LEU   B 1 75  ? 3.946  -17.566 8.434  1.00 16.16 ? 81  LEU   C N   1 
ATOM   1665 C  CA  . LEU   B 1 75  ? 4.123  -16.355 9.214  1.00 16.85 ? 81  LEU   C CA  1 
ATOM   1666 C  C   . LEU   B 1 75  ? 3.226  -16.482 10.441 1.00 18.26 ? 81  LEU   C C   1 
ATOM   1667 O  O   . LEU   B 1 75  ? 1.985  -16.542 10.294 1.00 19.82 ? 81  LEU   C O   1 
ATOM   1668 C  CB  . LEU   B 1 75  ? 3.595  -15.176 8.371  1.00 18.86 ? 81  LEU   C CB  1 
ATOM   1669 C  CG  . LEU   B 1 75  ? 4.593  -14.520 7.466  1.00 22.52 ? 81  LEU   C CG  1 
ATOM   1670 C  CD1 . LEU   B 1 75  ? 3.852  -13.617 6.427  1.00 24.96 ? 81  LEU   C CD1 1 
ATOM   1671 C  CD2 . LEU   B 1 75  ? 5.613  -13.742 8.274  1.00 24.05 ? 81  LEU   C CD2 1 
ATOM   1672 N  N   . ILE   B 1 76  ? 3.818  -16.483 11.640 1.00 16.95 ? 82  ILE   C N   1 
ATOM   1673 C  CA  . ILE   B 1 76  ? 3.116  -16.654 12.905 1.00 18.22 ? 82  ILE   C CA  1 
ATOM   1674 C  C   . ILE   B 1 76  ? 3.487  -15.562 13.884 1.00 18.46 ? 82  ILE   C C   1 
ATOM   1675 O  O   . ILE   B 1 76  ? 4.664  -15.216 14.010 1.00 16.82 ? 82  ILE   C O   1 
ATOM   1676 C  CB  . ILE   B 1 76  ? 3.449  -18.056 13.484 1.00 20.33 ? 82  ILE   C CB  1 
ATOM   1677 C  CG1 . ILE   B 1 76  ? 2.856  -19.148 12.555 1.00 23.03 ? 82  ILE   C CG1 1 
ATOM   1678 C  CG2 . ILE   B 1 76  ? 2.969  -18.208 14.949 1.00 22.31 ? 82  ILE   C CG2 1 
ATOM   1679 C  CD1 . ILE   B 1 76  ? 3.093  -20.513 12.934 1.00 26.10 ? 82  ILE   C CD1 1 
ATOM   1680 N  N   . PHE   B 1 77  ? 2.488  -14.993 14.574 1.00 19.98 ? 83  PHE   C N   1 
ATOM   1681 C  CA  . PHE   B 1 77  ? 2.744  -13.931 15.531 1.00 21.61 ? 83  PHE   C CA  1 
ATOM   1682 C  C   . PHE   B 1 77  ? 3.489  -14.464 16.759 1.00 21.03 ? 83  PHE   C C   1 
ATOM   1683 O  O   . PHE   B 1 77  ? 3.137  -15.519 17.298 1.00 21.56 ? 83  PHE   C O   1 
ATOM   1684 C  CB  . PHE   B 1 77  ? 1.424  -13.242 15.940 1.00 23.64 ? 83  PHE   C CB  1 
ATOM   1685 C  CG  . PHE   B 1 77  ? 1.655  -12.036 16.818 1.00 26.17 ? 83  PHE   C CG  1 
ATOM   1686 C  CD1 . PHE   B 1 77  ? 1.523  -12.125 18.195 1.00 28.67 ? 83  PHE   C CD1 1 
ATOM   1687 C  CD2 . PHE   B 1 77  ? 2.088  -10.843 16.276 1.00 28.30 ? 83  PHE   C CD2 1 
ATOM   1688 C  CE1 . PHE   B 1 77  ? 1.775  -11.023 19.007 1.00 29.64 ? 83  PHE   C CE1 1 
ATOM   1689 C  CE2 . PHE   B 1 77  ? 2.320  -9.737  17.086 1.00 30.02 ? 83  PHE   C CE2 1 
ATOM   1690 C  CZ  . PHE   B 1 77  ? 2.158  -9.833  18.444 1.00 29.67 ? 83  PHE   C CZ  1 
ATOM   1691 N  N   . VAL   B 1 78  ? 4.548  -13.753 17.164 1.00 20.12 ? 84  VAL   C N   1 
ATOM   1692 C  CA  . VAL   B 1 78  ? 5.379  -14.116 18.314 1.00 20.08 ? 84  VAL   C CA  1 
ATOM   1693 C  C   . VAL   B 1 78  ? 5.475  -12.909 19.247 1.00 21.23 ? 84  VAL   C C   1 
ATOM   1694 O  O   . VAL   B 1 78  ? 5.901  -11.828 18.825 1.00 20.87 ? 84  VAL   C O   1 
ATOM   1695 C  CB  . VAL   B 1 78  ? 6.812  -14.514 17.872 1.00 18.99 ? 84  VAL   C CB  1 
ATOM   1696 C  CG1 . VAL   B 1 78  ? 7.677  -14.848 19.094 1.00 18.67 ? 84  VAL   C CG1 1 
ATOM   1697 C  CG2 . VAL   B 1 78  ? 6.767  -15.683 16.886 1.00 17.54 ? 84  VAL   C CG2 1 
ATOM   1698 N  N   . GLU   B 1 79  ? 5.176  -13.129 20.543 1.00 22.16 ? 85  GLU   C N   1 
ATOM   1699 C  CA  . GLU   B 1 79  ? 5.250  -12.093 21.573 1.00 22.71 ? 85  GLU   C CA  1 
ATOM   1700 C  C   . GLU   B 1 79  ? 6.632  -11.474 21.696 1.00 21.91 ? 85  GLU   C C   1 
ATOM   1701 O  O   . GLU   B 1 79  ? 7.630  -12.142 21.420 1.00 20.91 ? 85  GLU   C O   1 
ATOM   1702 C  CB  . GLU   B 1 79  ? 4.898  -12.701 22.942 1.00 25.58 ? 85  GLU   C CB  1 
ATOM   1703 C  CG  . GLU   B 1 79  ? 3.497  -13.270 23.048 1.00 31.25 ? 85  GLU   C CG  1 
ATOM   1704 C  CD  . GLU   B 1 79  ? 2.338  -12.291 23.067 1.00 40.40 ? 85  GLU   C CD  1 
ATOM   1705 O  OE1 . GLU   B 1 79  ? 1.194  -12.732 22.812 1.00 42.22 ? 85  GLU   C OE1 1 
ATOM   1706 O  OE2 . GLU   B 1 79  ? 2.571  -11.086 23.322 1.00 41.47 ? 85  GLU   C OE2 1 
ATOM   1707 N  N   . ALA   B 1 80  ? 6.702  -10.231 22.186 1.00 21.42 ? 86  ALA   C N   1 
ATOM   1708 C  CA  . ALA   B 1 80  ? 7.989  -9.561  22.396 1.00 20.85 ? 86  ALA   C CA  1 
ATOM   1709 C  C   . ALA   B 1 80  ? 8.826  -10.316 23.432 1.00 20.16 ? 86  ALA   C C   1 
ATOM   1710 O  O   . ALA   B 1 80  ? 8.294  -10.903 24.378 1.00 20.89 ? 86  ALA   C O   1 
ATOM   1711 C  CB  . ALA   B 1 80  ? 7.780  -8.117  22.881 1.00 21.29 ? 86  ALA   C CB  1 
ATOM   1712 N  N   . SER   B 1 81  ? 10.142 -10.270 23.262 1.00 18.46 ? 87  SER   C N   1 
ATOM   1713 C  CA  . SER   B 1 81  ? 11.109 -10.840 24.193 1.00 16.84 ? 87  SER   C CA  1 
ATOM   1714 C  C   . SER   B 1 81  ? 12.260 -9.793  24.319 1.00 18.45 ? 87  SER   C C   1 
ATOM   1715 O  O   . SER   B 1 81  ? 12.209 -8.718  23.701 1.00 19.46 ? 87  SER   C O   1 
ATOM   1716 C  CB  . SER   B 1 81  ? 11.654 -12.184 23.668 1.00 14.80 ? 87  SER   C CB  1 
ATOM   1717 O  OG  . SER   B 1 81  ? 12.411 -11.986 22.485 1.00 16.05 ? 87  SER   C OG  1 
ATOM   1718 N  N   . GLU   B 1 82  ? 13.305 -10.103 25.099 1.00 18.87 ? 88  GLU   C N   1 
ATOM   1719 C  CA  . GLU   B 1 82  ? 14.468 -9.212  25.177 1.00 19.77 ? 88  GLU   C CA  1 
ATOM   1720 C  C   . GLU   B 1 82  ? 15.256 -9.240  23.826 1.00 20.10 ? 88  GLU   C C   1 
ATOM   1721 O  O   . GLU   B 1 82  ? 16.025 -8.328  23.547 1.00 20.67 ? 88  GLU   C O   1 
ATOM   1722 C  CB  . GLU   B 1 82  ? 15.366 -9.618  26.348 1.00 23.65 ? 88  GLU   C CB  1 
ATOM   1723 C  CG  . GLU   B 1 82  ? 15.869 -11.042 26.223 1.00 30.95 ? 88  GLU   C CG  1 
ATOM   1724 C  CD  . GLU   B 1 82  ? 15.105 -12.141 26.957 1.00 40.32 ? 88  GLU   C CD  1 
ATOM   1725 O  OE1 . GLU   B 1 82  ? 15.767 -12.907 27.695 1.00 42.52 ? 88  GLU   C OE1 1 
ATOM   1726 O  OE2 . GLU   B 1 82  ? 13.862 -12.245 26.788 1.00 39.42 ? 88  GLU   C OE2 1 
ATOM   1727 N  N   . TYR   B 1 83  ? 15.005 -10.252 22.964 1.00 19.45 ? 89  TYR   C N   1 
ATOM   1728 C  CA  . TYR   B 1 83  ? 15.687 -10.438 21.700 1.00 19.78 ? 89  TYR   C CA  1 
ATOM   1729 C  C   . TYR   B 1 83  ? 14.972 -9.777  20.501 1.00 20.70 ? 89  TYR   C C   1 
ATOM   1730 O  O   . TYR   B 1 83  ? 15.640 -9.401  19.536 1.00 22.74 ? 89  TYR   C O   1 
ATOM   1731 C  CB  . TYR   B 1 83  ? 15.875 -11.949 21.446 1.00 19.30 ? 89  TYR   C CB  1 
ATOM   1732 C  CG  . TYR   B 1 83  ? 16.523 -12.689 22.594 1.00 19.28 ? 89  TYR   C CG  1 
ATOM   1733 C  CD1 . TYR   B 1 83  ? 17.896 -12.630 22.803 1.00 20.99 ? 89  TYR   C CD1 1 
ATOM   1734 C  CD2 . TYR   B 1 83  ? 15.766 -13.453 23.465 1.00 20.00 ? 89  TYR   C CD2 1 
ATOM   1735 C  CE1 . TYR   B 1 83  ? 18.499 -13.333 23.839 1.00 22.84 ? 89  TYR   C CE1 1 
ATOM   1736 C  CE2 . TYR   B 1 83  ? 16.362 -14.206 24.469 1.00 21.66 ? 89  TYR   C CE2 1 
ATOM   1737 C  CZ  . TYR   B 1 83  ? 17.730 -14.138 24.664 1.00 24.21 ? 89  TYR   C CZ  1 
ATOM   1738 O  OH  . TYR   B 1 83  ? 18.324 -14.858 25.683 1.00 26.67 ? 89  TYR   C OH  1 
ATOM   1739 N  N   . TYR   B 1 84  ? 13.635 -9.680  20.516 1.00 19.95 ? 90  TYR   C N   1 
ATOM   1740 C  CA  . TYR   B 1 84  ? 12.886 -9.117  19.393 1.00 19.49 ? 90  TYR   C CA  1 
ATOM   1741 C  C   . TYR   B 1 84  ? 11.641 -8.376  19.877 1.00 20.82 ? 90  TYR   C C   1 
ATOM   1742 O  O   . TYR   B 1 84  ? 11.024 -8.799  20.852 1.00 20.34 ? 90  TYR   C O   1 
ATOM   1743 C  CB  . TYR   B 1 84  ? 12.352 -10.244 18.482 1.00 18.21 ? 90  TYR   C CB  1 
ATOM   1744 C  CG  . TYR   B 1 84  ? 13.378 -11.186 17.892 1.00 17.20 ? 90  TYR   C CG  1 
ATOM   1745 C  CD1 . TYR   B 1 84  ? 13.573 -12.457 18.426 1.00 16.55 ? 90  TYR   C CD1 1 
ATOM   1746 C  CD2 . TYR   B 1 84  ? 14.153 -10.814 16.796 1.00 16.95 ? 90  TYR   C CD2 1 
ATOM   1747 C  CE1 . TYR   B 1 84  ? 14.481 -13.342 17.869 1.00 16.28 ? 90  TYR   C CE1 1 
ATOM   1748 C  CE2 . TYR   B 1 84  ? 15.067 -11.696 16.228 1.00 16.79 ? 90  TYR   C CE2 1 
ATOM   1749 C  CZ  . TYR   B 1 84  ? 15.196 -12.983 16.739 1.00 16.03 ? 90  TYR   C CZ  1 
ATOM   1750 O  OH  . TYR   B 1 84  ? 16.139 -13.814 16.201 1.00 14.82 ? 90  TYR   C OH  1 
ATOM   1751 N  N   . PRO   B 1 85  ? 11.165 -7.329  19.150 1.00 22.39 ? 91  PRO   C N   1 
ATOM   1752 C  CA  . PRO   B 1 85  ? 9.843  -6.776  19.472 1.00 22.54 ? 91  PRO   C CA  1 
ATOM   1753 C  C   . PRO   B 1 85  ? 8.756  -7.785  19.060 1.00 22.80 ? 91  PRO   C C   1 
ATOM   1754 O  O   . PRO   B 1 85  ? 9.056  -8.767  18.341 1.00 22.60 ? 91  PRO   C O   1 
ATOM   1755 C  CB  . PRO   B 1 85  ? 9.759  -5.524  18.579 1.00 23.70 ? 91  PRO   C CB  1 
ATOM   1756 C  CG  . PRO   B 1 85  ? 10.620 -5.865  17.407 1.00 24.43 ? 91  PRO   C CG  1 
ATOM   1757 C  CD  . PRO   B 1 85  ? 11.737 -6.746  17.916 1.00 22.91 ? 91  PRO   C CD  1 
ATOM   1758 N  N   . ALA   B 1 86  ? 7.479  -7.550  19.420 1.00 23.02 ? 92  ALA   C N   1 
ATOM   1759 C  CA  . ALA   B 1 86  ? 6.369  -8.409  18.960 1.00 23.39 ? 92  ALA   C CA  1 
ATOM   1760 C  C   . ALA   B 1 86  ? 6.333  -8.333  17.418 1.00 22.87 ? 92  ALA   C C   1 
ATOM   1761 O  O   . ALA   B 1 86  ? 6.488  -7.239  16.870 1.00 24.30 ? 92  ALA   C O   1 
ATOM   1762 C  CB  . ALA   B 1 86  ? 5.041  -7.914  19.524 1.00 23.96 ? 92  ALA   C CB  1 
ATOM   1763 N  N   . ARG   B 1 87  ? 6.289  -9.484  16.738 1.00 21.10 ? 93  ARG   C N   1 
ATOM   1764 C  CA  . ARG   B 1 87  ? 6.392  -9.477  15.276 1.00 20.20 ? 93  ARG   C CA  1 
ATOM   1765 C  C   . ARG   B 1 87  ? 5.881  -10.777 14.688 1.00 20.67 ? 93  ARG   C C   1 
ATOM   1766 O  O   . ARG   B 1 87  ? 5.626  -11.735 15.423 1.00 20.33 ? 93  ARG   C O   1 
ATOM   1767 C  CB  . ARG   B 1 87  ? 7.877  -9.290  14.879 1.00 19.88 ? 93  ARG   C CB  1 
ATOM   1768 C  CG  . ARG   B 1 87  ? 8.707  -10.593 15.088 1.00 17.43 ? 93  ARG   C CG  1 
ATOM   1769 C  CD  . ARG   B 1 87  ? 10.168 -10.403 15.374 1.00 18.34 ? 93  ARG   C CD  1 
ATOM   1770 N  NE  . ARG   B 1 87  ? 11.023 -11.499 14.904 1.00 17.33 ? 93  ARG   C NE  1 
ATOM   1771 C  CZ  . ARG   B 1 87  ? 11.111 -12.694 15.485 1.00 19.43 ? 93  ARG   C CZ  1 
ATOM   1772 N  NH1 . ARG   B 1 87  ? 11.963 -13.610 15.015 1.00 15.73 ? 93  ARG   C NH1 1 
ATOM   1773 N  NH2 . ARG   B 1 87  ? 10.364 -12.980 16.559 1.00 17.91 ? 93  ARG   C NH2 1 
ATOM   1774 N  N   . TYR   B 1 88  ? 5.790  -10.836 13.347 1.00 20.99 ? 94  TYR   C N   1 
ATOM   1775 C  CA  . TYR   B 1 88  ? 5.486  -12.093 12.691 1.00 21.87 ? 94  TYR   C CA  1 
ATOM   1776 C  C   . TYR   B 1 88  ? 6.823  -12.745 12.355 1.00 18.96 ? 94  TYR   C C   1 
ATOM   1777 O  O   . TYR   B 1 88  ? 7.679  -12.137 11.696 1.00 18.91 ? 94  TYR   C O   1 
ATOM   1778 C  CB  . TYR   B 1 88  ? 4.695  -11.886 11.396 1.00 24.27 ? 94  TYR   C CB  1 
ATOM   1779 C  CG  . TYR   B 1 88  ? 3.275  -11.470 11.668 1.00 28.13 ? 94  TYR   C CG  1 
ATOM   1780 C  CD1 . TYR   B 1 88  ? 2.283  -12.415 11.879 1.00 30.19 ? 94  TYR   C CD1 1 
ATOM   1781 C  CD2 . TYR   B 1 88  ? 2.936  -10.131 11.793 1.00 31.14 ? 94  TYR   C CD2 1 
ATOM   1782 C  CE1 . TYR   B 1 88  ? 0.972  -12.036 12.149 1.00 33.24 ? 94  TYR   C CE1 1 
ATOM   1783 C  CE2 . TYR   B 1 88  ? 1.635  -9.743  12.083 1.00 32.85 ? 94  TYR   C CE2 1 
ATOM   1784 C  CZ  . TYR   B 1 88  ? 0.658  -10.699 12.264 1.00 34.97 ? 94  TYR   C CZ  1 
ATOM   1785 O  OH  . TYR   B 1 88  ? -0.643 -10.327 12.504 1.00 38.67 ? 94  TYR   C OH  1 
ATOM   1786 N  N   . GLN   B 1 89  ? 7.007  -13.977 12.826 1.00 15.91 ? 95  GLN   C N   1 
ATOM   1787 C  CA  . GLN   B 1 89  ? 8.192  -14.738 12.475 1.00 14.93 ? 95  GLN   C CA  1 
ATOM   1788 C  C   . GLN   B 1 89  ? 7.806  -15.602 11.284 1.00 15.22 ? 95  GLN   C C   1 
ATOM   1789 O  O   . GLN   B 1 89  ? 6.734  -16.238 11.298 1.00 16.16 ? 95  GLN   C O   1 
ATOM   1790 C  CB  . GLN   B 1 89  ? 8.659  -15.596 13.672 1.00 13.99 ? 95  GLN   C CB  1 
ATOM   1791 C  CG  . GLN   B 1 89  ? 9.847  -16.511 13.286 1.00 14.35 ? 95  GLN   C CG  1 
ATOM   1792 C  CD  . GLN   B 1 89  ? 10.594 -17.023 14.498 1.00 14.16 ? 95  GLN   C CD  1 
ATOM   1793 O  OE1 . GLN   B 1 89  ? 10.797 -16.286 15.470 1.00 15.13 ? 95  GLN   C OE1 1 
ATOM   1794 N  NE2 . GLN   B 1 89  ? 11.073 -18.295 14.411 1.00 13.39 ? 95  GLN   C NE2 1 
ATOM   1795 N  N   . SER   B 1 90  ? 8.624  -15.575 10.231 1.00 13.78 ? 96  SER   C N   1 
ATOM   1796 C  CA  . SER   B 1 90  ? 8.321  -16.361 9.041  1.00 12.99 ? 96  SER   C CA  1 
ATOM   1797 C  C   . SER   B 1 90  ? 8.966  -17.770 9.082  1.00 12.96 ? 96  SER   C C   1 
ATOM   1798 O  O   . SER   B 1 90  ? 9.857  -18.040 9.913  1.00 13.21 ? 96  SER   C O   1 
ATOM   1799 C  CB  . SER   B 1 90  ? 8.797  -15.634 7.779  1.00 15.35 ? 96  SER   C CB  1 
ATOM   1800 O  OG  . SER   B 1 90  ? 10.203 -15.432 7.861  1.00 18.13 ? 96  SER   C OG  1 
ATOM   1801 N  N   . HIS   B 1 91  ? 8.483  -18.659 8.175  1.00 12.52 ? 97  HIS   C N   1 
ATOM   1802 C  CA  . HIS   B 1 91  ? 9.014  -20.025 8.024  1.00 12.64 ? 97  HIS   C CA  1 
ATOM   1803 C  C   . HIS   B 1 91  ? 8.937  -20.824 9.351  1.00 13.53 ? 97  HIS   C C   1 
ATOM   1804 O  O   . HIS   B 1 91  ? 9.796  -21.680 9.607  1.00 13.91 ? 97  HIS   C O   1 
ATOM   1805 C  CB  . HIS   B 1 91  ? 10.459 -19.990 7.477  1.00 12.94 ? 97  HIS   C CB  1 
ATOM   1806 C  CG  . HIS   B 1 91  ? 10.566 -19.344 6.124  1.00 15.92 ? 97  HIS   C CG  1 
ATOM   1807 N  ND1 . HIS   B 1 91  ? 10.502 -20.090 4.959  1.00 19.10 ? 97  HIS   C ND1 1 
ATOM   1808 C  CD2 . HIS   B 1 91  ? 10.663 -18.029 5.800  1.00 17.80 ? 97  HIS   C CD2 1 
ATOM   1809 C  CE1 . HIS   B 1 91  ? 10.605 -19.216 3.956  1.00 20.04 ? 97  HIS   C CE1 1 
ATOM   1810 N  NE2 . HIS   B 1 91  ? 10.713 -17.962 4.409  1.00 19.25 ? 97  HIS   C NE2 1 
ATOM   1811 N  N   . LEU   B 1 92  ? 7.907  -20.543 10.169 1.00 13.19 ? 98  LEU   C N   1 
ATOM   1812 C  CA  . LEU   B 1 92  ? 7.714  -21.182 11.486 1.00 12.53 ? 98  LEU   C CA  1 
ATOM   1813 C  C   . LEU   B 1 92  ? 6.636  -22.283 11.389 1.00 13.13 ? 98  LEU   C C   1 
ATOM   1814 O  O   . LEU   B 1 92  ? 5.625  -22.101 10.723 1.00 14.19 ? 98  LEU   C O   1 
ATOM   1815 C  CB  . LEU   B 1 92  ? 7.297  -20.106 12.521 1.00 13.44 ? 98  LEU   C CB  1 
ATOM   1816 C  CG  . LEU   B 1 92  ? 7.261  -20.514 13.981 1.00 15.49 ? 98  LEU   C CG  1 
ATOM   1817 C  CD1 . LEU   B 1 92  ? 8.679  -20.912 14.466 1.00 16.27 ? 98  LEU   C CD1 1 
ATOM   1818 C  CD2 . LEU   B 1 92  ? 6.792  -19.339 14.860 1.00 17.69 ? 98  LEU   C CD2 1 
ATOM   1819 N  N   . MET   B 1 93  ? 6.835  -23.389 12.126 1.00 11.97 ? 99  MET   C N   1 
ATOM   1820 C  CA  . MET   B 1 93  ? 5.876  -24.503 12.103 1.00 12.80 ? 99  MET   C CA  1 
ATOM   1821 C  C   . MET   B 1 93  ? 5.538  -24.815 13.552 1.00 13.58 ? 99  MET   C C   1 
ATOM   1822 O  O   . MET   B 1 93  ? 6.458  -24.826 14.389 1.00 14.13 ? 99  MET   C O   1 
ATOM   1823 C  CB  . MET   B 1 93  ? 6.558  -25.725 11.485 1.00 12.18 ? 99  MET   C CB  1 
ATOM   1824 C  CG  . MET   B 1 93  ? 6.995  -25.457 10.067 1.00 15.53 ? 99  MET   C CG  1 
ATOM   1825 S  SD  . MET   B 1 93  ? 8.026  -26.779 9.441  1.00 16.76 ? 99  MET   C SD  1 
ATOM   1826 C  CE  . MET   B 1 93  ? 9.437  -26.717 10.538 1.00 15.66 ? 99  MET   C CE  1 
ATOM   1827 N  N   . LEU   B 1 94  ? 4.251  -24.998 13.858 1.00 12.38 ? 100 LEU   C N   1 
ATOM   1828 C  CA  . LEU   B 1 94  ? 3.857  -25.268 15.243 1.00 12.39 ? 100 LEU   C CA  1 
ATOM   1829 C  C   . LEU   B 1 94  ? 3.434  -26.724 15.425 1.00 11.87 ? 100 LEU   C C   1 
ATOM   1830 O  O   . LEU   B 1 94  ? 2.948  -27.368 14.507 1.00 11.37 ? 100 LEU   C O   1 
ATOM   1831 C  CB  . LEU   B 1 94  ? 2.628  -24.422 15.652 1.00 13.66 ? 100 LEU   C CB  1 
ATOM   1832 C  CG  . LEU   B 1 94  ? 2.822  -22.906 15.612 1.00 16.29 ? 100 LEU   C CG  1 
ATOM   1833 C  CD1 . LEU   B 1 94  ? 1.568  -22.190 16.221 1.00 18.52 ? 100 LEU   C CD1 1 
ATOM   1834 C  CD2 . LEU   B 1 94  ? 4.099  -22.469 16.351 1.00 18.05 ? 100 LEU   C CD2 1 
ATOM   1835 N  N   . ALA   B 1 95  ? 3.605  -27.205 16.658 1.00 11.80 ? 101 ALA   C N   1 
ATOM   1836 C  CA  . ALA   B 1 95  ? 3.158  -28.537 17.096 1.00 11.49 ? 101 ALA   C CA  1 
ATOM   1837 C  C   . ALA   B 1 95  ? 2.626  -28.398 18.531 1.00 11.78 ? 101 ALA   C C   1 
ATOM   1838 O  O   . ALA   B 1 95  ? 3.012  -27.481 19.258 1.00 12.92 ? 101 ALA   C O   1 
ATOM   1839 C  CB  . ALA   B 1 95  ? 4.336  -29.507 17.100 1.00 11.85 ? 101 ALA   C CB  1 
ATOM   1840 N  N   . VAL   B 1 96  ? 1.785  -29.350 18.940 1.00 11.63 ? 102 VAL   C N   1 
ATOM   1841 C  CA  . VAL   B 1 96  ? 1.363  -29.409 20.324 1.00 12.21 ? 102 VAL   C CA  1 
ATOM   1842 C  C   . VAL   B 1 96  ? 2.461  -30.122 21.093 1.00 13.60 ? 102 VAL   C C   1 
ATOM   1843 O  O   . VAL   B 1 96  ? 2.713  -31.311 20.859 1.00 14.03 ? 102 VAL   C O   1 
ATOM   1844 C  CB  . VAL   B 1 96  ? 0.008  -30.150 20.429 1.00 13.86 ? 102 VAL   C CB  1 
ATOM   1845 C  CG1 . VAL   B 1 96  ? -0.400 -30.266 21.890 1.00 14.40 ? 102 VAL   C CG1 1 
ATOM   1846 C  CG2 . VAL   B 1 96  ? -1.052 -29.411 19.606 1.00 15.21 ? 102 VAL   C CG2 1 
ATOM   1847 N  N   . GLY   B 1 97  ? 3.130  -29.387 21.974 1.00 13.78 ? 103 GLY   C N   1 
ATOM   1848 C  CA  . GLY   B 1 97  ? 4.209  -29.988 22.746 1.00 15.00 ? 103 GLY   C CA  1 
ATOM   1849 C  C   . GLY   B 1 97  ? 4.827  -29.002 23.704 1.00 16.11 ? 103 GLY   C C   1 
ATOM   1850 O  O   . GLY   B 1 97  ? 4.578  -27.793 23.635 1.00 16.38 ? 103 GLY   C O   1 
ATOM   1851 N  N   . HIS   B 1 98  ? 5.640  -29.521 24.611 1.00 14.61 ? 104 HIS   C N   1 
ATOM   1852 C  CA  . HIS   B 1 98  ? 6.273  -28.710 25.623 1.00 14.65 ? 104 HIS   C CA  1 
ATOM   1853 C  C   . HIS   B 1 98  ? 7.566  -28.071 25.146 1.00 14.96 ? 104 HIS   C C   1 
ATOM   1854 O  O   . HIS   B 1 98  ? 8.374  -28.698 24.450 1.00 14.45 ? 104 HIS   C O   1 
ATOM   1855 C  CB  . HIS   B 1 98  ? 6.615  -29.598 26.857 1.00 14.63 ? 104 HIS   C CB  1 
ATOM   1856 C  CG  . HIS   B 1 98  ? 7.317  -28.846 27.946 1.00 16.73 ? 104 HIS   C CG  1 
ATOM   1857 N  ND1 . HIS   B 1 98  ? 6.660  -27.861 28.683 1.00 17.76 ? 104 HIS   C ND1 1 
ATOM   1858 C  CD2 . HIS   B 1 98  ? 8.623  -28.890 28.330 1.00 18.63 ? 104 HIS   C CD2 1 
ATOM   1859 C  CE1 . HIS   B 1 98  ? 7.572  -27.380 29.531 1.00 19.60 ? 104 HIS   C CE1 1 
ATOM   1860 N  NE2 . HIS   B 1 98  ? 8.775  -27.967 29.345 1.00 20.61 ? 104 HIS   C NE2 1 
ATOM   1861 N  N   . SER   B 1 99  ? 7.811  -26.859 25.652 1.00 14.05 ? 105 SER   C N   1 
ATOM   1862 C  CA  . SER   B 1 99  ? 9.076  -26.176 25.478 1.00 14.32 ? 105 SER   C CA  1 
ATOM   1863 C  C   . SER   B 1 99  ? 9.221  -25.099 26.528 1.00 15.51 ? 105 SER   C C   1 
ATOM   1864 O  O   . SER   B 1 99  ? 8.236  -24.612 27.090 1.00 15.92 ? 105 SER   C O   1 
ATOM   1865 C  CB  . SER   B 1 99  ? 9.220  -25.566 24.079 1.00 15.56 ? 105 SER   C CB  1 
ATOM   1866 O  OG  . SER   B 1 99  ? 8.318  -24.490 23.878 1.00 17.69 ? 105 SER   C OG  1 
ATOM   1867 N  N   . GLU   B 1 100 ? 10.468 -24.766 26.801 1.00 15.58 ? 106 GLU   C N   1 
ATOM   1868 C  CA  . GLU   B 1 100 ? 10.908 -23.666 27.656 1.00 16.50 ? 106 GLU   C CA  1 
ATOM   1869 C  C   . GLU   B 1 100 ? 11.975 -22.891 26.872 1.00 16.30 ? 106 GLU   C C   1 
ATOM   1870 O  O   . GLU   B 1 100 ? 12.499 -23.406 25.863 1.00 15.27 ? 106 GLU   C O   1 
ATOM   1871 C  CB  . GLU   B 1 100 ? 11.450 -24.189 28.981 1.00 17.96 ? 106 GLU   C CB  1 
ATOM   1872 C  CG  . GLU   B 1 100 ? 10.315 -24.767 29.788 1.00 25.40 ? 106 GLU   C CG  1 
ATOM   1873 C  CD  . GLU   B 1 100 ? 10.766 -25.548 31.001 1.00 29.84 ? 106 GLU   C CD  1 
ATOM   1874 O  OE1 . GLU   B 1 100 ? 11.874 -25.272 31.513 1.00 33.32 ? 106 GLU   C OE1 1 
ATOM   1875 O  OE2 . GLU   B 1 100 ? 10.013 -26.450 31.427 1.00 28.37 ? 106 GLU   C OE2 1 
ATOM   1876 N  N   . PRO   B 1 101 ? 12.280 -21.632 27.248 1.00 17.10 ? 107 PRO   C N   1 
ATOM   1877 C  CA  . PRO   B 1 101 ? 13.260 -20.859 26.451 1.00 17.40 ? 107 PRO   C CA  1 
ATOM   1878 C  C   . PRO   B 1 101 ? 14.586 -21.580 26.138 1.00 16.66 ? 107 PRO   C C   1 
ATOM   1879 O  O   . PRO   B 1 101 ? 15.070 -21.551 24.989 1.00 16.13 ? 107 PRO   C O   1 
ATOM   1880 C  CB  . PRO   B 1 101 ? 13.488 -19.603 27.302 1.00 19.00 ? 107 PRO   C CB  1 
ATOM   1881 C  CG  . PRO   B 1 101 ? 12.147 -19.411 28.024 1.00 19.36 ? 107 PRO   C CG  1 
ATOM   1882 C  CD  . PRO   B 1 101 ? 11.697 -20.828 28.347 1.00 17.52 ? 107 PRO   C CD  1 
ATOM   1883 N  N   . GLY   B 1 102 ? 15.156 -22.263 27.153 1.00 16.48 ? 108 GLY   C N   1 
ATOM   1884 C  CA  . GLY   B 1 102 ? 16.403 -23.013 27.006 1.00 16.14 ? 108 GLY   C CA  1 
ATOM   1885 C  C   . GLY   B 1 102 ? 16.328 -24.183 26.038 1.00 15.42 ? 108 GLY   C C   1 
ATOM   1886 O  O   . GLY   B 1 102 ? 17.350 -24.804 25.703 1.00 15.16 ? 108 GLY   C O   1 
ATOM   1887 N  N   . ASP   B 1 103 ? 15.098 -24.537 25.613 1.00 13.06 ? 109 ASP   C N   1 
ATOM   1888 C  CA  . ASP   B 1 103 ? 14.929 -25.616 24.627 1.00 12.89 ? 109 ASP   C CA  1 
ATOM   1889 C  C   . ASP   B 1 103 ? 15.265 -25.200 23.210 1.00 12.57 ? 109 ASP   C C   1 
ATOM   1890 O  O   . ASP   B 1 103 ? 15.362 -26.080 22.335 1.00 12.68 ? 109 ASP   C O   1 
ATOM   1891 C  CB  . ASP   B 1 103 ? 13.499 -26.186 24.663 1.00 13.70 ? 109 ASP   C CB  1 
ATOM   1892 C  CG  . ASP   B 1 103 ? 13.270 -27.031 25.910 1.00 16.20 ? 109 ASP   C CG  1 
ATOM   1893 O  OD1 . ASP   B 1 103 ? 14.219 -27.718 26.347 1.00 16.16 ? 109 ASP   C OD1 1 
ATOM   1894 O  OD2 . ASP   B 1 103 ? 12.151 -27.006 26.447 1.00 16.38 ? 109 ASP   C OD2 1 
ATOM   1895 N  N   . CYS   B 1 104 ? 15.392 -23.865 22.929 1.00 12.51 ? 110 CYS   C N   1 
ATOM   1896 C  CA  . CYS   B 1 104 ? 15.707 -23.407 21.570 1.00 12.90 ? 110 CYS   C CA  1 
ATOM   1897 C  C   . CYS   B 1 104 ? 16.982 -24.052 21.071 1.00 13.24 ? 110 CYS   C C   1 
ATOM   1898 O  O   . CYS   B 1 104 ? 17.932 -24.181 21.839 1.00 13.37 ? 110 CYS   C O   1 
ATOM   1899 C  CB  . CYS   B 1 104 ? 15.787 -21.883 21.486 1.00 14.15 ? 110 CYS   C CB  1 
ATOM   1900 S  SG  . CYS   B 1 104 ? 14.175 -21.043 21.687 1.00 16.48 ? 110 CYS   C SG  1 
ATOM   1901 N  N   . GLY   B 1 105 ? 16.956 -24.528 19.839 1.00 11.54 ? 111 GLY   C N   1 
ATOM   1902 C  CA  . GLY   B 1 105 ? 18.112 -25.185 19.263 1.00 13.14 ? 111 GLY   C CA  1 
ATOM   1903 C  C   . GLY   B 1 105 ? 17.953 -26.698 19.153 1.00 14.02 ? 111 GLY   C C   1 
ATOM   1904 O  O   . GLY   B 1 105 ? 18.722 -27.348 18.440 1.00 14.30 ? 111 GLY   C O   1 
ATOM   1905 N  N   . GLY   B 1 106 ? 16.970 -27.269 19.876 1.00 12.26 ? 112 GLY   C N   1 
ATOM   1906 C  CA  . GLY   B 1 106 ? 16.672 -28.703 19.809 1.00 12.22 ? 112 GLY   C CA  1 
ATOM   1907 C  C   . GLY   B 1 106 ? 16.234 -29.050 18.387 1.00 12.17 ? 112 GLY   C C   1 
ATOM   1908 O  O   . GLY   B 1 106 ? 15.453 -28.305 17.783 1.00 12.35 ? 112 GLY   C O   1 
ATOM   1909 N  N   . ILE   B 1 107 ? 16.763 -30.151 17.843 1.00 12.18 ? 113 ILE   C N   1 
ATOM   1910 C  CA  . ILE   B 1 107 ? 16.464 -30.503 16.460 1.00 12.67 ? 113 ILE   C CA  1 
ATOM   1911 C  C   . ILE   B 1 107 ? 15.130 -31.218 16.328 1.00 11.92 ? 113 ILE   C C   1 
ATOM   1912 O  O   . ILE   B 1 107 ? 14.778 -32.088 17.153 1.00 12.99 ? 113 ILE   C O   1 
ATOM   1913 C  CB  . ILE   B 1 107 ? 17.648 -31.350 15.898 1.00 14.16 ? 113 ILE   C CB  1 
ATOM   1914 C  CG1 . ILE   B 1 107 ? 18.867 -30.425 15.562 1.00 16.34 ? 113 ILE   C CG1 1 
ATOM   1915 C  CG2 . ILE   B 1 107 ? 17.281 -32.255 14.707 1.00 16.08 ? 113 ILE   C CG2 1 
ATOM   1916 C  CD1 . ILE   B 1 107 ? 20.145 -31.243 15.088 1.00 18.06 ? 113 ILE   C CD1 1 
ATOM   1917 N  N   . LEU   B 1 108 ? 14.424 -30.888 15.233 1.00 11.42 ? 114 LEU   C N   1 
ATOM   1918 C  CA  . LEU   B 1 108 ? 13.227 -31.615 14.792 1.00 11.81 ? 114 LEU   C CA  1 
ATOM   1919 C  C   . LEU   B 1 108 ? 13.703 -32.417 13.554 1.00 12.42 ? 114 LEU   C C   1 
ATOM   1920 O  O   . LEU   B 1 108 ? 14.307 -31.849 12.629 1.00 12.46 ? 114 LEU   C O   1 
ATOM   1921 C  CB  . LEU   B 1 108 ? 12.114 -30.617 14.357 1.00 11.10 ? 114 LEU   C CB  1 
ATOM   1922 C  CG  . LEU   B 1 108 ? 10.927 -31.248 13.638 1.00 11.25 ? 114 LEU   C CG  1 
ATOM   1923 C  CD1 . LEU   B 1 108 ? 10.139 -32.178 14.580 1.00 12.22 ? 114 LEU   C CD1 1 
ATOM   1924 C  CD2 . LEU   B 1 108 ? 9.983  -30.122 13.104 1.00 12.57 ? 114 LEU   C CD2 1 
ATOM   1925 N  N   . ARG   B 1 109 ? 13.448 -33.750 13.547 1.00 12.39 ? 115 ARG   C N   1 
ATOM   1926 C  CA  . ARG   B 1 109 ? 13.866 -34.600 12.425 1.00 13.08 ? 115 ARG   C CA  1 
ATOM   1927 C  C   . ARG   B 1 109 ? 12.693 -35.409 11.932 1.00 13.62 ? 115 ARG   C C   1 
ATOM   1928 O  O   . ARG   B 1 109 ? 11.877 -35.878 12.725 1.00 14.13 ? 115 ARG   C O   1 
ATOM   1929 C  CB  . ARG   B 1 109 ? 14.901 -35.666 12.890 1.00 15.96 ? 115 ARG   C CB  1 
ATOM   1930 C  CG  . ARG   B 1 109 ? 16.145 -35.162 13.564 1.00 23.39 ? 115 ARG   C CG  1 
ATOM   1931 C  CD  . ARG   B 1 109 ? 17.037 -36.341 13.993 1.00 27.88 ? 115 ARG   C CD  1 
ATOM   1932 N  NE  . ARG   B 1 109 ? 17.525 -36.990 12.784 1.00 32.24 ? 115 ARG   C NE  1 
ATOM   1933 C  CZ  . ARG   B 1 109 ? 18.661 -36.664 12.173 1.00 34.77 ? 115 ARG   C CZ  1 
ATOM   1934 N  NH1 . ARG   B 1 109 ? 19.509 -35.810 12.741 1.00 36.28 ? 115 ARG   C NH1 1 
ATOM   1935 N  NH2 . ARG   B 1 109 ? 18.981 -37.228 11.022 1.00 35.12 ? 115 ARG   C NH2 1 
ATOM   1936 N  N   . CYS   B 1 110 ? 12.672 -35.653 10.635 1.00 12.36 ? 116 CYS   C N   1 
ATOM   1937 C  CA  . CYS   B 1 110 ? 11.684 -36.565 10.051 1.00 14.06 ? 116 CYS   C CA  1 
ATOM   1938 C  C   . CYS   B 1 110 ? 12.449 -37.782 9.473  1.00 15.47 ? 116 CYS   C C   1 
ATOM   1939 O  O   . CYS   B 1 110 ? 13.676 -37.881 9.618  1.00 15.12 ? 116 CYS   C O   1 
ATOM   1940 C  CB  . CYS   B 1 110 ? 10.877 -35.855 8.966  1.00 14.01 ? 116 CYS   C CB  1 
ATOM   1941 S  SG  . CYS   B 1 110 ? 11.885 -35.369 7.533  1.00 13.10 ? 116 CYS   C SG  1 
ATOM   1942 N  N   . GLN   B 1 111 ? 11.721 -38.684 8.739  1.00 16.85 ? 117 GLN   C N   1 
ATOM   1943 C  CA  . GLN   B 1 111 ? 12.392 -39.836 8.155  1.00 17.87 ? 117 GLN   C CA  1 
ATOM   1944 C  C   . GLN   B 1 111 ? 13.490 -39.448 7.098  1.00 18.29 ? 117 GLN   C C   1 
ATOM   1945 O  O   . GLN   B 1 111 ? 14.332 -40.269 6.738  1.00 20.98 ? 117 GLN   C O   1 
ATOM   1946 C  CB  . GLN   B 1 111 ? 11.348 -40.779 7.521  1.00 20.66 ? 117 GLN   C CB  1 
ATOM   1947 C  CG  . GLN   B 1 111 ? 10.695 -40.186 6.272  1.00 23.47 ? 117 GLN   C CG  1 
ATOM   1948 C  CD  . GLN   B 1 111 ? 9.675  -41.127 5.646  1.00 32.34 ? 117 GLN   C CD  1 
ATOM   1949 O  OE1 . GLN   B 1 111 ? 8.464  -40.866 5.688  1.00 34.43 ? 117 GLN   C OE1 1 
ATOM   1950 N  NE2 . GLN   B 1 111 ? 10.134 -42.224 5.028  1.00 34.06 ? 117 GLN   C NE2 1 
ATOM   1951 N  N   . HIS   B 1 112 ? 13.490 -38.192 6.618  1.00 15.99 ? 118 HIS   C N   1 
ATOM   1952 C  CA  . HIS   B 1 112 ? 14.442 -37.741 5.587  1.00 16.13 ? 118 HIS   C CA  1 
ATOM   1953 C  C   . HIS   B 1 112 ? 15.654 -36.992 6.144  1.00 16.56 ? 118 HIS   C C   1 
ATOM   1954 O  O   . HIS   B 1 112 ? 16.600 -36.745 5.402  1.00 18.39 ? 118 HIS   C O   1 
ATOM   1955 C  CB  . HIS   B 1 112 ? 13.737 -36.839 4.557  1.00 16.24 ? 118 HIS   C CB  1 
ATOM   1956 C  CG  . HIS   B 1 112 ? 12.539 -37.486 3.932  1.00 16.06 ? 118 HIS   C CG  1 
ATOM   1957 N  ND1 . HIS   B 1 112 ? 11.257 -37.076 4.230  1.00 15.36 ? 118 HIS   C ND1 1 
ATOM   1958 C  CD2 . HIS   B 1 112 ? 12.476 -38.486 3.014  1.00 18.08 ? 118 HIS   C CD2 1 
ATOM   1959 C  CE1 . HIS   B 1 112 ? 10.445 -37.836 3.512  1.00 17.47 ? 118 HIS   C CE1 1 
ATOM   1960 N  NE2 . HIS   B 1 112 ? 11.125 -38.700 2.756  1.00 19.13 ? 118 HIS   C NE2 1 
ATOM   1961 N  N   . GLY   B 1 113 ? 15.614 -36.627 7.427  1.00 14.80 ? 119 GLY   C N   1 
ATOM   1962 C  CA  . GLY   B 1 113 ? 16.709 -35.864 8.028  1.00 13.74 ? 119 GLY   C CA  1 
ATOM   1963 C  C   . GLY   B 1 113 ? 16.252 -34.699 8.903  1.00 12.76 ? 119 GLY   C C   1 
ATOM   1964 O  O   . GLY   B 1 113 ? 15.121 -34.679 9.412  1.00 13.44 ? 119 GLY   C O   1 
ATOM   1965 N  N   . VAL   B 1 114 ? 17.151 -33.733 9.088  1.00 12.22 ? 120 VAL   C N   1 
ATOM   1966 C  CA  . VAL   B 1 114 ? 16.859 -32.554 9.892  1.00 12.21 ? 120 VAL   C CA  1 
ATOM   1967 C  C   . VAL   B 1 114 ? 15.870 -31.624 9.195  1.00 11.57 ? 120 VAL   C C   1 
ATOM   1968 O  O   . VAL   B 1 114 ? 16.113 -31.209 8.053  1.00 12.12 ? 120 VAL   C O   1 
ATOM   1969 C  CB  . VAL   B 1 114 ? 18.154 -31.777 10.219 1.00 13.46 ? 120 VAL   C CB  1 
ATOM   1970 C  CG1 . VAL   B 1 114 ? 17.815 -30.482 10.979 1.00 14.24 ? 120 VAL   C CG1 1 
ATOM   1971 C  CG2 . VAL   B 1 114 ? 19.114 -32.669 11.036 1.00 13.72 ? 120 VAL   C CG2 1 
ATOM   1972 N  N   . VAL   B 1 115 ? 14.787 -31.256 9.901  1.00 11.15 ? 121 VAL   C N   1 
ATOM   1973 C  CA  . VAL   B 1 115 ? 13.745 -30.378 9.400  1.00 10.92 ? 121 VAL   C CA  1 
ATOM   1974 C  C   . VAL   B 1 115 ? 13.948 -28.918 9.864  1.00 11.58 ? 121 VAL   C C   1 
ATOM   1975 O  O   . VAL   B 1 115 ? 13.677 -27.965 9.120  1.00 11.83 ? 121 VAL   C O   1 
ATOM   1976 C  CB  . VAL   B 1 115 ? 12.363 -30.898 9.885  1.00 12.54 ? 121 VAL   C CB  1 
ATOM   1977 C  CG1 . VAL   B 1 115 ? 11.260 -29.902 9.549  1.00 13.11 ? 121 VAL   C CG1 1 
ATOM   1978 C  CG2 . VAL   B 1 115 ? 12.051 -32.255 9.262  1.00 12.95 ? 121 VAL   C CG2 1 
ATOM   1979 N  N   . GLY   B 1 116 ? 14.305 -28.767 11.140 1.00 11.28 ? 122 GLY   C N   1 
ATOM   1980 C  CA  . GLY   B 1 116 ? 14.463 -27.432 11.709 1.00 12.70 ? 122 GLY   C CA  1 
ATOM   1981 C  C   . GLY   B 1 116 ? 14.859 -27.480 13.165 1.00 12.27 ? 122 GLY   C C   1 
ATOM   1982 O  O   . GLY   B 1 116 ? 15.275 -28.531 13.658 1.00 12.60 ? 122 GLY   C O   1 
ATOM   1983 N  N   . ILE   B 1 117 ? 14.815 -26.322 13.845 1.00 11.16 ? 123 ILE   C N   1 
ATOM   1984 C  CA  . ILE   B 1 117 ? 15.207 -26.274 15.250 1.00 11.28 ? 123 ILE   C CA  1 
ATOM   1985 C  C   . ILE   B 1 117 ? 14.145 -25.543 16.060 1.00 10.98 ? 123 ILE   C C   1 
ATOM   1986 O  O   . ILE   B 1 117 ? 13.483 -24.640 15.555 1.00 10.60 ? 123 ILE   C O   1 
ATOM   1987 C  CB  . ILE   B 1 117 ? 16.570 -25.536 15.433 1.00 11.90 ? 123 ILE   C CB  1 
ATOM   1988 C  CG1 . ILE   B 1 117 ? 16.582 -24.183 14.687 1.00 13.04 ? 123 ILE   C CG1 1 
ATOM   1989 C  CG2 . ILE   B 1 117 ? 17.752 -26.428 14.980 1.00 13.24 ? 123 ILE   C CG2 1 
ATOM   1990 C  CD1 . ILE   B 1 117 ? 17.940 -23.407 15.037 1.00 14.34 ? 123 ILE   C CD1 1 
ATOM   1991 N  N   . VAL   B 1 118 ? 13.993 -25.904 17.357 1.00 10.77 ? 124 VAL   C N   1 
ATOM   1992 C  CA  . VAL   B 1 118 ? 13.054 -25.202 18.226 1.00 11.10 ? 124 VAL   C CA  1 
ATOM   1993 C  C   . VAL   B 1 118 ? 13.414 -23.705 18.262 1.00 11.19 ? 124 VAL   C C   1 
ATOM   1994 O  O   . VAL   B 1 118 ? 14.593 -23.344 18.407 1.00 11.47 ? 124 VAL   C O   1 
ATOM   1995 C  CB  . VAL   B 1 118 ? 13.113 -25.748 19.671 1.00 11.79 ? 124 VAL   C CB  1 
ATOM   1996 C  CG1 . VAL   B 1 118 ? 12.260 -24.888 20.612 1.00 11.91 ? 124 VAL   C CG1 1 
ATOM   1997 C  CG2 . VAL   B 1 118 ? 12.668 -27.214 19.730 1.00 12.00 ? 124 VAL   C CG2 1 
ATOM   1998 N  N   . SER   B 1 119 ? 12.408 -22.870 18.109 1.00 11.20 ? 125 SER   C N   1 
ATOM   1999 C  CA  . SER   B 1 119 ? 12.623 -21.412 18.076 1.00 11.91 ? 125 SER   C CA  1 
ATOM   2000 C  C   . SER   B 1 119 ? 11.660 -20.636 18.971 1.00 13.01 ? 125 SER   C C   1 
ATOM   2001 O  O   . SER   B 1 119 ? 12.026 -19.569 19.479 1.00 13.47 ? 125 SER   C O   1 
ATOM   2002 C  CB  . SER   B 1 119 ? 12.541 -20.901 16.626 1.00 13.15 ? 125 SER   C CB  1 
ATOM   2003 O  OG  . SER   B 1 119 ? 12.720 -19.492 16.481 1.00 14.26 ? 125 SER   C OG  1 
ATOM   2004 N  N   . THR   B 1 120 ? 10.442 -21.140 19.166 1.00 13.34 ? 126 THR   C N   1 
ATOM   2005 C  CA  . THR   B 1 120 ? 9.432  -20.435 19.987 1.00 13.76 ? 126 THR   C CA  1 
ATOM   2006 C  C   . THR   B 1 120 ? 8.635  -21.435 20.832 1.00 14.21 ? 126 THR   C C   1 
ATOM   2007 O  O   . THR   B 1 120 ? 8.632  -22.643 20.547 1.00 14.09 ? 126 THR   C O   1 
ATOM   2008 C  CB  . THR   B 1 120 ? 8.430  -19.663 19.071 1.00 15.18 ? 126 THR   C CB  1 
ATOM   2009 O  OG1 . THR   B 1 120 ? 7.535  -20.586 18.410 1.00 16.07 ? 126 THR   C OG1 1 
ATOM   2010 C  CG2 . THR   B 1 120 ? 9.089  -18.736 18.069 1.00 15.33 ? 126 THR   C CG2 1 
ATOM   2011 N  N   . GLY   B 1 121 ? 7.861  -20.924 21.783 1.00 14.49 ? 127 GLY   C N   1 
ATOM   2012 C  CA  . GLY   B 1 121 ? 6.944  -21.771 22.531 1.00 16.14 ? 127 GLY   C CA  1 
ATOM   2013 C  C   . GLY   B 1 121 ? 6.022  -20.964 23.416 1.00 16.97 ? 127 GLY   C C   1 
ATOM   2014 O  O   . GLY   B 1 121 ? 6.222  -19.771 23.626 1.00 16.41 ? 127 GLY   C O   1 
ATOM   2015 N  N   . GLY   B 1 122 ? 5.035  -21.633 23.964 1.00 17.95 ? 128 GLY   C N   1 
ATOM   2016 C  CA  . GLY   B 1 122 ? 4.054  -20.994 24.851 1.00 18.74 ? 128 GLY   C CA  1 
ATOM   2017 C  C   . GLY   B 1 122 ? 2.692  -21.645 24.678 1.00 18.29 ? 128 GLY   C C   1 
ATOM   2018 O  O   . GLY   B 1 122 ? 2.381  -22.135 23.594 1.00 18.06 ? 128 GLY   C O   1 
ATOM   2019 N  N   . ASN   B 1 123 ? 1.899  -21.705 25.768 1.00 19.52 ? 129 ASN   C N   1 
ATOM   2020 C  CA  . ASN   B 1 123 ? 0.559  -22.299 25.763 1.00 20.11 ? 129 ASN   C CA  1 
ATOM   2021 C  C   . ASN   B 1 123 ? 0.541  -23.762 25.246 1.00 19.15 ? 129 ASN   C C   1 
ATOM   2022 O  O   . ASN   B 1 123 ? -0.458 -24.176 24.650 1.00 20.10 ? 129 ASN   C O   1 
ATOM   2023 C  CB  . ASN   B 1 123 ? -0.378 -21.456 24.902 1.00 22.88 ? 129 ASN   C CB  1 
ATOM   2024 C  CG  . ASN   B 1 123 ? -0.595 -20.091 25.453 1.00 29.01 ? 129 ASN   C CG  1 
ATOM   2025 O  OD1 . ASN   B 1 123 ? -0.655 -19.891 26.672 1.00 30.63 ? 129 ASN   C OD1 1 
ATOM   2026 N  ND2 . ASN   B 1 123 ? -0.727 -19.128 24.556 1.00 31.42 ? 129 ASN   C ND2 1 
ATOM   2027 N  N   . GLY   B 1 124 ? 1.607  -24.528 25.493 1.00 17.16 ? 130 GLY   C N   1 
ATOM   2028 C  CA  . GLY   B 1 124 ? 1.653  -25.920 25.041 1.00 16.81 ? 130 GLY   C CA  1 
ATOM   2029 C  C   . GLY   B 1 124 ? 1.797  -26.108 23.540 1.00 15.45 ? 130 GLY   C C   1 
ATOM   2030 O  O   . GLY   B 1 124 ? 1.500  -27.189 23.033 1.00 16.21 ? 130 GLY   C O   1 
ATOM   2031 N  N   . LEU   B 1 125 ? 2.247  -25.039 22.831 1.00 13.53 ? 131 LEU   C N   1 
ATOM   2032 C  CA  . LEU   B 1 125 ? 2.522  -25.074 21.391 1.00 14.32 ? 131 LEU   C CA  1 
ATOM   2033 C  C   . LEU   B 1 125 ? 4.006  -24.717 21.189 1.00 16.42 ? 131 LEU   C C   1 
ATOM   2034 O  O   . LEU   B 1 125 ? 4.427  -23.627 21.598 1.00 19.18 ? 131 LEU   C O   1 
ATOM   2035 C  CB  . LEU   B 1 125 ? 1.647  -24.033 20.677 1.00 15.26 ? 131 LEU   C CB  1 
ATOM   2036 C  CG  . LEU   B 1 125 ? 0.160  -24.378 20.667 1.00 17.14 ? 131 LEU   C CG  1 
ATOM   2037 C  CD1 . LEU   B 1 125 ? -0.711 -23.114 20.411 1.00 18.46 ? 131 LEU   C CD1 1 
ATOM   2038 C  CD2 . LEU   B 1 125 ? -0.135 -25.403 19.618 1.00 17.65 ? 131 LEU   C CD2 1 
ATOM   2039 N  N   . VAL   B 1 126 ? 4.795  -25.618 20.584 1.00 13.15 ? 132 VAL   C N   1 
ATOM   2040 C  CA  . VAL   B 1 126 ? 6.221  -25.387 20.345 1.00 12.66 ? 132 VAL   C CA  1 
ATOM   2041 C  C   . VAL   B 1 126 ? 6.392  -25.028 18.869 1.00 12.55 ? 132 VAL   C C   1 
ATOM   2042 O  O   . VAL   B 1 126 ? 5.706  -25.619 17.996 1.00 12.91 ? 132 VAL   C O   1 
ATOM   2043 C  CB  . VAL   B 1 126 ? 7.040  -26.648 20.722 1.00 13.44 ? 132 VAL   C CB  1 
ATOM   2044 C  CG1 . VAL   B 1 126 ? 6.475  -27.914 20.058 1.00 14.35 ? 132 VAL   C CG1 1 
ATOM   2045 C  CG2 . VAL   B 1 126 ? 8.553  -26.467 20.415 1.00 13.36 ? 132 VAL   C CG2 1 
ATOM   2046 N  N   . GLY   B 1 127 ? 7.265  -24.056 18.591 1.00 11.52 ? 133 GLY   C N   1 
ATOM   2047 C  CA  . GLY   B 1 127 ? 7.469  -23.638 17.207 1.00 11.62 ? 133 GLY   C CA  1 
ATOM   2048 C  C   . GLY   B 1 127 ? 8.887  -23.954 16.750 1.00 12.33 ? 133 GLY   C C   1 
ATOM   2049 O  O   . GLY   B 1 127 ? 9.838  -23.788 17.517 1.00 11.79 ? 133 GLY   C O   1 
ATOM   2050 N  N   . PHE   B 1 128 ? 9.019  -24.394 15.477 1.00 11.63 ? 134 PHE   C N   1 
ATOM   2051 C  CA  . PHE   B 1 128 ? 10.292 -24.810 14.886 1.00 12.14 ? 134 PHE   C CA  1 
ATOM   2052 C  C   . PHE   B 1 128 ? 10.571 -23.934 13.664 1.00 12.66 ? 134 PHE   C C   1 
ATOM   2053 O  O   . PHE   B 1 128 ? 9.686  -23.737 12.824 1.00 12.70 ? 134 PHE   C O   1 
ATOM   2054 C  CB  . PHE   B 1 128 ? 10.206 -26.275 14.379 1.00 12.62 ? 134 PHE   C CB  1 
ATOM   2055 C  CG  . PHE   B 1 128 ? 9.753  -27.257 15.446 1.00 12.70 ? 134 PHE   C CG  1 
ATOM   2056 C  CD1 . PHE   B 1 128 ? 10.654 -27.777 16.357 1.00 12.33 ? 134 PHE   C CD1 1 
ATOM   2057 C  CD2 . PHE   B 1 128 ? 8.431  -27.667 15.518 1.00 13.48 ? 134 PHE   C CD2 1 
ATOM   2058 C  CE1 . PHE   B 1 128 ? 10.225 -28.644 17.364 1.00 12.79 ? 134 PHE   C CE1 1 
ATOM   2059 C  CE2 . PHE   B 1 128 ? 8.009  -28.574 16.499 1.00 13.69 ? 134 PHE   C CE2 1 
ATOM   2060 C  CZ  . PHE   B 1 128 ? 8.907  -29.054 17.419 1.00 13.38 ? 134 PHE   C CZ  1 
ATOM   2061 N  N   . ALA   B 1 129 ? 11.812 -23.417 13.598 1.00 11.42 ? 135 ALA   C N   1 
ATOM   2062 C  CA  . ALA   B 1 129 ? 12.284 -22.644 12.443 1.00 11.44 ? 135 ALA   C CA  1 
ATOM   2063 C  C   . ALA   B 1 129 ? 12.647 -23.682 11.396 1.00 11.48 ? 135 ALA   C C   1 
ATOM   2064 O  O   . ALA   B 1 129 ? 13.566 -24.496 11.616 1.00 11.58 ? 135 ALA   C O   1 
ATOM   2065 C  CB  . ALA   B 1 129 ? 13.531 -21.846 12.826 1.00 11.33 ? 135 ALA   C CB  1 
ATOM   2066 N  N   . ASP   B 1 130 ? 11.961 -23.649 10.240 1.00 11.20 ? 136 ASP   C N   1 
ATOM   2067 C  CA  . ASP   B 1 130 ? 12.233 -24.605 9.159  1.00 11.84 ? 136 ASP   C CA  1 
ATOM   2068 C  C   . ASP   B 1 130 ? 13.583 -24.283 8.504  1.00 12.67 ? 136 ASP   C C   1 
ATOM   2069 O  O   . ASP   B 1 130 ? 13.908 -23.092 8.334  1.00 12.58 ? 136 ASP   C O   1 
ATOM   2070 C  CB  . ASP   B 1 130 ? 11.137 -24.423 8.077  1.00 12.41 ? 136 ASP   C CB  1 
ATOM   2071 C  CG  . ASP   B 1 130 ? 11.207 -25.436 6.954  1.00 18.02 ? 136 ASP   C CG  1 
ATOM   2072 O  OD1 . ASP   B 1 130 ? 11.428 -26.613 7.237  1.00 17.87 ? 136 ASP   C OD1 1 
ATOM   2073 O  OD2 . ASP   B 1 130 ? 11.114 -25.027 5.785  1.00 21.12 ? 136 ASP   C OD2 1 
ATOM   2074 N  N   . VAL   B 1 131 ? 14.338 -25.320 8.069  1.00 11.24 ? 137 VAL   C N   1 
ATOM   2075 C  CA  . VAL   B 1 131 ? 15.578 -25.096 7.284  1.00 12.13 ? 137 VAL   C CA  1 
ATOM   2076 C  C   . VAL   B 1 131 ? 15.535 -25.873 5.942  1.00 13.03 ? 137 VAL   C C   1 
ATOM   2077 O  O   . VAL   B 1 131 ? 16.501 -25.845 5.191  1.00 13.56 ? 137 VAL   C O   1 
ATOM   2078 C  CB  . VAL   B 1 131 ? 16.852 -25.487 8.070  1.00 13.40 ? 137 VAL   C CB  1 
ATOM   2079 C  CG1 . VAL   B 1 131 ? 16.990 -24.670 9.372  1.00 13.57 ? 137 VAL   C CG1 1 
ATOM   2080 C  CG2 . VAL   B 1 131 ? 16.881 -27.003 8.366  1.00 12.73 ? 137 VAL   C CG2 1 
ATOM   2081 N  N   . ARG   B 1 132 ? 14.422 -26.602 5.647  1.00 12.40 ? 138 ARG   C N   1 
ATOM   2082 C  CA  . ARG   B 1 132 ? 14.344 -27.428 4.449  1.00 10.88 ? 138 ARG   C CA  1 
ATOM   2083 C  C   . ARG   B 1 132 ? 14.423 -26.653 3.166  1.00 12.71 ? 138 ARG   C C   1 
ATOM   2084 O  O   . ARG   B 1 132 ? 14.799 -27.243 2.158  1.00 14.27 ? 138 ARG   C O   1 
ATOM   2085 C  CB  . ARG   B 1 132 ? 13.066 -28.294 4.445  1.00 11.17 ? 138 ARG   C CB  1 
ATOM   2086 C  CG  . ARG   B 1 132 ? 13.035 -29.246 5.624  1.00 11.18 ? 138 ARG   C CG  1 
ATOM   2087 C  CD  . ARG   B 1 132 ? 11.702 -29.976 5.674  1.00 11.96 ? 138 ARG   C CD  1 
ATOM   2088 N  NE  . ARG   B 1 132 ? 10.624 -29.094 6.123  1.00 11.84 ? 138 ARG   C NE  1 
ATOM   2089 C  CZ  . ARG   B 1 132 ? 9.372  -29.480 6.337  1.00 14.31 ? 138 ARG   C CZ  1 
ATOM   2090 N  NH1 . ARG   B 1 132 ? 8.991  -30.719 6.045  1.00 13.25 ? 138 ARG   C NH1 1 
ATOM   2091 N  NH2 . ARG   B 1 132 ? 8.476  -28.618 6.824  1.00 14.36 ? 138 ARG   C NH2 1 
ATOM   2092 N  N   . ASP   B 1 133 ? 14.017 -25.367 3.168  1.00 12.51 ? 139 ASP   C N   1 
ATOM   2093 C  CA  . ASP   B 1 133 ? 14.091 -24.571 1.947  1.00 12.84 ? 139 ASP   C CA  1 
ATOM   2094 C  C   . ASP   B 1 133 ? 15.482 -24.010 1.656  1.00 14.43 ? 139 ASP   C C   1 
ATOM   2095 O  O   . ASP   B 1 133 ? 15.682 -23.487 0.546  1.00 15.43 ? 139 ASP   C O   1 
ATOM   2096 C  CB  . ASP   B 1 133 ? 13.080 -23.419 1.987  1.00 14.87 ? 139 ASP   C CB  1 
ATOM   2097 C  CG  . ASP   B 1 133 ? 13.377 -22.422 3.085  1.00 19.03 ? 139 ASP   C CG  1 
ATOM   2098 O  OD1 . ASP   B 1 133 ? 13.680 -22.869 4.225  1.00 18.69 ? 139 ASP   C OD1 1 
ATOM   2099 O  OD2 . ASP   B 1 133 ? 13.324 -21.176 2.802  1.00 20.62 ? 139 ASP   C OD2 1 
ATOM   2100 N  N   . LEU   B 1 134 ? 16.441 -24.114 2.599  1.00 14.30 ? 140 LEU   C N   1 
ATOM   2101 C  CA  . LEU   B 1 134 ? 17.791 -23.559 2.421  1.00 14.45 ? 140 LEU   C CA  1 
ATOM   2102 C  C   . LEU   B 1 134 ? 18.654 -24.540 1.639  1.00 14.63 ? 140 LEU   C C   1 
ATOM   2103 O  O   . LEU   B 1 134 ? 19.485 -25.271 2.203  1.00 15.09 ? 140 LEU   C O   1 
ATOM   2104 C  CB  . LEU   B 1 134 ? 18.426 -23.218 3.795  1.00 15.14 ? 140 LEU   C CB  1 
ATOM   2105 C  CG  . LEU   B 1 134 ? 17.570 -22.290 4.665  1.00 16.36 ? 140 LEU   C CG  1 
ATOM   2106 C  CD1 . LEU   B 1 134 ? 18.187 -22.104 6.057  1.00 15.85 ? 140 LEU   C CD1 1 
ATOM   2107 C  CD2 . LEU   B 1 134 ? 17.364 -20.936 3.990  1.00 17.09 ? 140 LEU   C CD2 1 
ATOM   2108 N  N   . LEU   B 1 135 ? 18.414 -24.604 0.323  1.00 14.42 ? 141 LEU   C N   1 
ATOM   2109 C  CA  . LEU   B 1 135 ? 19.090 -25.623 -0.496 1.00 15.35 ? 141 LEU   C CA  1 
ATOM   2110 C  C   . LEU   B 1 135 ? 20.604 -25.473 -0.537 1.00 16.55 ? 141 LEU   C C   1 
ATOM   2111 O  O   . LEU   B 1 135 ? 21.323 -26.473 -0.708 1.00 18.47 ? 141 LEU   C O   1 
ATOM   2112 C  CB  . LEU   B 1 135 ? 18.499 -25.660 -1.918 1.00 15.17 ? 141 LEU   C CB  1 
ATOM   2113 C  CG  . LEU   B 1 135 ? 16.973 -25.698 -2.014 1.00 16.80 ? 141 LEU   C CG  1 
ATOM   2114 C  CD1 . LEU   B 1 135 ? 16.552 -25.853 -3.480 1.00 17.75 ? 141 LEU   C CD1 1 
ATOM   2115 C  CD2 . LEU   B 1 135 ? 16.364 -26.815 -1.154 1.00 17.54 ? 141 LEU   C CD2 1 
ATOM   2116 N  N   . TRP   B 1 136 ? 21.090 -24.226 -0.388 1.00 16.83 ? 142 TRP   C N   1 
ATOM   2117 C  CA  . TRP   B 1 136 ? 22.517 -23.930 -0.456 1.00 17.33 ? 142 TRP   C CA  1 
ATOM   2118 C  C   . TRP   B 1 136 ? 23.301 -24.536 0.741  1.00 18.88 ? 142 TRP   C C   1 
ATOM   2119 O  O   . TRP   B 1 136 ? 24.534 -24.615 0.668  1.00 20.29 ? 142 TRP   C O   1 
ATOM   2120 C  CB  . TRP   B 1 136 ? 22.726 -22.410 -0.535 1.00 17.81 ? 142 TRP   C CB  1 
ATOM   2121 C  CG  . TRP   B 1 136 ? 22.035 -21.632 0.554  1.00 17.78 ? 142 TRP   C CG  1 
ATOM   2122 C  CD1 . TRP   B 1 136 ? 20.789 -21.067 0.514  1.00 18.54 ? 142 TRP   C CD1 1 
ATOM   2123 C  CD2 . TRP   B 1 136 ? 22.572 -21.338 1.859  1.00 17.10 ? 142 TRP   C CD2 1 
ATOM   2124 N  NE1 . TRP   B 1 136 ? 20.533 -20.410 1.710  1.00 18.96 ? 142 TRP   C NE1 1 
ATOM   2125 C  CE2 . TRP   B 1 136 ? 21.629 -20.541 2.534  1.00 18.31 ? 142 TRP   C CE2 1 
ATOM   2126 C  CE3 . TRP   B 1 136 ? 23.819 -21.579 2.472  1.00 17.60 ? 142 TRP   C CE3 1 
ATOM   2127 C  CZ2 . TRP   B 1 136 ? 21.842 -20.087 3.841  1.00 18.92 ? 142 TRP   C CZ2 1 
ATOM   2128 C  CZ3 . TRP   B 1 136 ? 24.035 -21.090 3.753  1.00 18.23 ? 142 TRP   C CZ3 1 
ATOM   2129 C  CH2 . TRP   B 1 136 ? 23.066 -20.324 4.407  1.00 18.33 ? 142 TRP   C CH2 1 
ATOM   2130 N  N   . LEU   B 1 137 ? 22.621 -25.014 1.805  1.00 18.64 ? 143 LEU   C N   1 
ATOM   2131 C  CA  . LEU   B 1 137 ? 23.345 -25.640 2.943  1.00 19.58 ? 143 LEU   C CA  1 
ATOM   2132 C  C   . LEU   B 1 137 ? 24.196 -26.860 2.492  1.00 23.00 ? 143 LEU   C C   1 
ATOM   2133 O  O   . LEU   B 1 137 ? 25.202 -27.165 3.135  1.00 22.94 ? 143 LEU   C O   1 
ATOM   2134 C  CB  . LEU   B 1 137 ? 22.376 -26.065 4.063  1.00 18.70 ? 143 LEU   C CB  1 
ATOM   2135 C  CG  . LEU   B 1 137 ? 21.794 -24.935 4.881  1.00 18.33 ? 143 LEU   C CG  1 
ATOM   2136 C  CD1 . LEU   B 1 137 ? 20.710 -25.461 5.830  1.00 17.46 ? 143 LEU   C CD1 1 
ATOM   2137 C  CD2 . LEU   B 1 137 ? 22.897 -24.183 5.681  1.00 17.25 ? 143 LEU   C CD2 1 
ATOM   2138 N  N   . ASP   B 1 138 ? 23.788 -27.520 1.391  1.00 25.86 ? 144 ASP   C N   1 
ATOM   2139 C  CA  . ASP   B 1 138 ? 24.461 -28.688 0.810  1.00 30.54 ? 144 ASP   C CA  1 
ATOM   2140 C  C   . ASP   B 1 138 ? 25.355 -28.401 -0.373 1.00 35.02 ? 144 ASP   C C   1 
ATOM   2141 O  O   . ASP   B 1 138 ? 25.804 -29.361 -1.007 1.00 36.80 ? 144 ASP   C O   1 
ATOM   2142 C  CB  . ASP   B 1 138 ? 23.423 -29.692 0.326  1.00 33.65 ? 144 ASP   C CB  1 
ATOM   2143 C  CG  . ASP   B 1 138 ? 22.712 -30.318 1.476  1.00 38.19 ? 144 ASP   C CG  1 
ATOM   2144 O  OD1 . ASP   B 1 138 ? 23.391 -30.640 2.486  1.00 39.15 ? 144 ASP   C OD1 1 
ATOM   2145 O  OD2 . ASP   B 1 138 ? 21.488 -30.466 1.391  1.00 39.23 ? 144 ASP   C OD2 1 
ATOM   2146 N  N   . GLU   B 1 139 ? 25.610 -27.134 -0.694 1.00 36.76 ? 145 GLU   C N   1 
ATOM   2147 C  CA  . GLU   B 1 139 ? 26.493 -26.815 -1.817 1.00 39.58 ? 145 GLU   C CA  1 
ATOM   2148 C  C   . GLU   B 1 139 ? 27.651 -25.909 -1.372 1.00 41.51 ? 145 GLU   C C   1 
ATOM   2149 O  O   . GLU   B 1 139 ? 28.399 -25.381 -2.206 1.00 42.38 ? 145 GLU   C O   1 
ATOM   2150 C  CB  . GLU   B 1 139 ? 25.702 -26.212 -2.990 1.00 42.97 ? 145 GLU   C CB  1 
ATOM   2151 C  CG  . GLU   B 1 139 ? 24.963 -24.933 -2.648 1.00 49.29 ? 145 GLU   C CG  1 
ATOM   2152 C  CD  . GLU   B 1 139 ? 24.207 -24.312 -3.811 1.00 56.86 ? 145 GLU   C CD  1 
ATOM   2153 O  OE1 . GLU   B 1 139 ? 24.397 -23.099 -4.062 1.00 57.29 ? 145 GLU   C OE1 1 
ATOM   2154 O  OE2 . GLU   B 1 139 ? 23.428 -25.039 -4.472 1.00 59.40 ? 145 GLU   C OE2 1 
HETATM 2155 N  N1  . A1B5J C 2 .   ? 25.141 13.710  10.376 1.00 16.44 ? 201 A1B5J A N1  1 
HETATM 2156 C  C4  . A1B5J C 2 .   ? 24.103 14.421  9.609  1.00 15.59 ? 201 A1B5J A C4  1 
HETATM 2157 C  C5  . A1B5J C 2 .   ? 25.855 12.652  9.932  1.00 17.42 ? 201 A1B5J A C5  1 
HETATM 2158 C  C6  . A1B5J C 2 .   ? 25.451 12.071  8.588  1.00 18.21 ? 201 A1B5J A C6  1 
HETATM 2159 C  C7  . A1B5J C 2 .   ? 26.376 10.965  8.138  1.00 18.80 ? 201 A1B5J A C7  1 
HETATM 2160 C  C8  . A1B5J C 2 .   ? 27.361 11.207  7.187  1.00 19.69 ? 201 A1B5J A C8  1 
HETATM 2161 C  C10 . A1B5J C 2 .   ? 27.900 8.886   7.200  1.00 18.76 ? 201 A1B5J A C10 1 
HETATM 2162 CL CL  . A1B5J C 2 .   ? 24.960 9.235   9.666  1.00 20.14 ? 201 A1B5J A CL  1 
HETATM 2163 C  C11 . A1B5J C 2 .   ? 26.242 9.616   8.552  1.00 19.21 ? 201 A1B5J A C11 1 
HETATM 2164 N  N2  . A1B5J C 2 .   ? 26.966 8.604   8.127  1.00 18.85 ? 201 A1B5J A N2  1 
HETATM 2165 C  C9  . A1B5J C 2 .   ? 28.128 10.160  6.701  1.00 19.20 ? 201 A1B5J A C9  1 
HETATM 2166 O  O1  . A1B5J C 2 .   ? 26.769 12.170  10.582 1.00 17.07 ? 201 A1B5J A O1  1 
HETATM 2167 C  C3  . A1B5J C 2 .   ? 22.770 14.368  10.339 1.00 15.62 ? 201 A1B5J A C3  1 
HETATM 2168 C  C2  . A1B5J C 2 .   ? 22.918 14.874  11.787 1.00 16.01 ? 201 A1B5J A C2  1 
HETATM 2169 C  C12 . A1B5J C 2 .   ? 25.333 14.224  11.735 1.00 16.77 ? 201 A1B5J A C12 1 
HETATM 2170 C  C1  . A1B5J C 2 .   ? 24.023 14.103  12.529 1.00 16.28 ? 201 A1B5J A C1  1 
HETATM 2171 C  C   . A1B5J C 2 .   ? 24.170 14.578  13.965 1.00 17.00 ? 201 A1B5J A C   1 
HETATM 2172 O  O   . A1B5J C 2 .   ? 24.636 15.695  14.224 1.00 16.87 ? 201 A1B5J A O   1 
HETATM 2173 N  N   . A1B5J C 2 .   ? 23.829 13.703  14.907 1.00 16.32 ? 201 A1B5J A N   1 
HETATM 2174 ZN ZN  . ZN    D 3 .   ? 23.461 -5.513  27.005 1.00 17.32 2 202 ZN    A ZN  1 
HETATM 2175 S  S   . DMS   E 4 .   ? 31.735 10.660  14.152 1.00 83.79 ? 203 DMS   A S   1 
HETATM 2176 O  O   . DMS   E 4 .   ? 31.212 11.051  15.499 1.00 83.79 ? 203 DMS   A O   1 
HETATM 2177 C  C1  . DMS   E 4 .   ? 30.683 11.475  12.958 1.00 83.74 ? 203 DMS   A C1  1 
HETATM 2178 C  C2  . DMS   E 4 .   ? 31.166 8.989   13.726 1.00 83.70 ? 203 DMS   A C2  1 
HETATM 2179 N  N1  . A1B5J F 2 .   ? 10.999 -16.864 22.717 1.00 14.84 ? 201 A1B5J C N1  1 
HETATM 2180 C  C4  . A1B5J F 2 .   ? 12.091 -16.170 23.424 1.00 15.47 ? 201 A1B5J C C4  1 
HETATM 2181 C  C5  . A1B5J F 2 .   ? 10.274 -17.914 23.181 1.00 15.75 ? 201 A1B5J C C5  1 
HETATM 2182 C  C6  . A1B5J F 2 .   ? 10.740 -18.554 24.476 1.00 16.37 ? 201 A1B5J C C6  1 
HETATM 2183 C  C7  . A1B5J F 2 .   ? 9.790  -19.627 24.966 1.00 16.41 ? 201 A1B5J C C7  1 
HETATM 2184 C  C8  . A1B5J F 2 .   ? 8.877  -19.352 25.982 1.00 16.32 ? 201 A1B5J C C8  1 
HETATM 2185 C  C10 . A1B5J F 2 .   ? 8.174  -21.630 25.940 1.00 17.75 ? 201 A1B5J C C10 1 
HETATM 2186 CL CL  . A1B5J F 2 .   ? 10.974 -21.393 23.295 1.00 19.10 ? 201 A1B5J C CL  1 
HETATM 2187 C  C11 . A1B5J F 2 .   ? 9.803  -20.968 24.508 1.00 17.53 ? 201 A1B5J C C11 1 
HETATM 2188 N  N2  . A1B5J F 2 .   ? 9.027  -21.944 24.949 1.00 17.50 ? 201 A1B5J C N2  1 
HETATM 2189 C  C9  . A1B5J F 2 .   ? 8.065  -20.364 26.482 1.00 17.24 ? 201 A1B5J C C9  1 
HETATM 2190 O  O1  . A1B5J F 2 .   ? 9.289  -18.344 22.585 1.00 15.78 ? 201 A1B5J C O1  1 
HETATM 2191 C  C3  . A1B5J F 2 .   ? 13.378 -16.236 22.596 1.00 14.90 ? 201 A1B5J C C3  1 
HETATM 2192 C  C2  . A1B5J F 2 .   ? 13.141 -15.725 21.161 1.00 14.06 ? 201 A1B5J C C2  1 
HETATM 2193 C  C12 . A1B5J F 2 .   ? 10.736 -16.328 21.377 1.00 14.19 ? 201 A1B5J C C12 1 
HETATM 2194 C  C1  . A1B5J F 2 .   ? 11.978 -16.487 20.489 1.00 13.86 ? 201 A1B5J C C1  1 
HETATM 2195 C  C   . A1B5J F 2 .   ? 11.722 -15.971 19.082 1.00 14.41 ? 201 A1B5J C C   1 
HETATM 2196 O  O   . A1B5J F 2 .   ? 11.275 -14.828 18.892 1.00 14.03 ? 201 A1B5J C O   1 
HETATM 2197 N  N   . A1B5J F 2 .   ? 11.955 -16.840 18.096 1.00 14.59 ? 201 A1B5J C N   1 
HETATM 2198 S  S   . DMS   G 4 .   ? 4.186  -19.270 18.808 1.00 71.75 ? 202 DMS   C S   1 
HETATM 2199 O  O   . DMS   G 4 .   ? 4.298  -17.851 19.310 1.00 71.61 ? 202 DMS   C O   1 
HETATM 2200 C  C1  . DMS   G 4 .   ? 2.421  -19.700 18.836 1.00 71.86 ? 202 DMS   C C1  1 
HETATM 2201 C  C2  . DMS   G 4 .   ? 4.595  -20.399 20.153 1.00 71.59 ? 202 DMS   C C2  1 
HETATM 2202 ZN ZN  . ZN    H 3 .   ? 10.618 -35.585 5.593  1.00 14.07 2 203 ZN    C ZN  1 
HETATM 2203 S  S   . DMS   I 4 .   ? 14.441 -10.469 7.029  1.00 69.55 ? 204 DMS   C S   1 
HETATM 2204 O  O   . DMS   I 4 .   ? 14.353 -9.984  8.457  1.00 69.17 ? 204 DMS   C O   1 
HETATM 2205 C  C1  . DMS   I 4 .   ? 12.840 -10.185 6.212  1.00 69.51 ? 204 DMS   C C1  1 
HETATM 2206 C  C2  . DMS   I 4 .   ? 15.346 -9.203  6.090  1.00 69.52 ? 204 DMS   C C2  1 
HETATM 2207 O  O   . HOH   J 5 .   ? 15.070 22.067  24.603 1.00 29.39 ? 301 HOH   A O   1 
HETATM 2208 O  O   . HOH   J 5 .   ? 30.408 5.260   8.383  1.00 30.23 ? 302 HOH   A O   1 
HETATM 2209 O  O   . HOH   J 5 .   ? 24.054 7.421   28.159 1.00 23.87 ? 303 HOH   A O   1 
HETATM 2210 O  O   . HOH   J 5 .   ? 22.501 6.510   1.535  1.00 24.49 ? 304 HOH   A O   1 
HETATM 2211 O  O   . HOH   J 5 .   ? 11.906 -1.704  28.114 1.00 24.99 ? 305 HOH   A O   1 
HETATM 2212 O  O   . HOH   J 5 .   ? 30.631 19.903  7.774  1.00 38.21 ? 306 HOH   A O   1 
HETATM 2213 O  O   . HOH   J 5 .   ? 32.052 7.434   23.043 1.00 30.97 ? 307 HOH   A O   1 
HETATM 2214 O  O   . HOH   J 5 .   ? 28.532 17.322  7.991  1.00 44.87 ? 308 HOH   A O   1 
HETATM 2215 O  O   . HOH   J 5 .   ? 31.283 -5.275  11.629 1.00 24.98 ? 309 HOH   A O   1 
HETATM 2216 O  O   . HOH   J 5 .   ? 16.090 -0.868  4.910  1.00 29.34 ? 310 HOH   A O   1 
HETATM 2217 O  O   . HOH   J 5 .   ? 14.642 -5.444  27.124 1.00 31.27 ? 311 HOH   A O   1 
HETATM 2218 O  O   . HOH   J 5 .   ? 11.269 21.260  24.610 1.00 26.32 ? 312 HOH   A O   1 
HETATM 2219 O  O   . HOH   J 5 .   ? 15.073 8.499   13.452 1.00 12.74 ? 313 HOH   A O   1 
HETATM 2220 O  O   . HOH   J 5 .   ? -1.735 15.498  20.448 1.00 27.47 ? 314 HOH   A O   1 
HETATM 2221 O  O   . HOH   J 5 .   ? 17.178 20.629  23.057 1.00 20.15 ? 315 HOH   A O   1 
HETATM 2222 O  O   . HOH   J 5 .   ? 7.492  7.358   31.859 1.00 33.17 ? 316 HOH   A O   1 
HETATM 2223 O  O   . HOH   J 5 .   ? 13.019 -4.582  20.994 1.00 33.85 ? 317 HOH   A O   1 
HETATM 2224 O  O   . HOH   J 5 .   ? 24.240 3.947   29.233 1.00 20.94 ? 318 HOH   A O   1 
HETATM 2225 O  O   . HOH   J 5 .   ? 4.204  9.836   18.242 1.00 34.97 ? 319 HOH   A O   1 
HETATM 2226 O  O   . HOH   J 5 .   ? 35.152 14.889  24.811 1.00 28.75 ? 320 HOH   A O   1 
HETATM 2227 O  O   . HOH   J 5 .   ? 16.564 18.528  26.984 1.00 42.43 ? 321 HOH   A O   1 
HETATM 2228 O  O   . HOH   J 5 .   ? 31.949 3.289   5.139  1.00 28.36 ? 322 HOH   A O   1 
HETATM 2229 O  O   . HOH   J 5 .   ? 33.143 10.121  11.156 1.00 41.98 ? 323 HOH   A O   1 
HETATM 2230 O  O   . HOH   J 5 .   ? 6.676  3.091   29.233 1.00 38.14 ? 324 HOH   A O   1 
HETATM 2231 O  O   . HOH   J 5 .   ? 18.932 -11.556 27.428 1.00 32.65 ? 325 HOH   A O   1 
HETATM 2232 O  O   . HOH   J 5 .   ? 34.591 -0.769  16.501 1.00 13.62 ? 326 HOH   A O   1 
HETATM 2233 O  O   . HOH   J 5 .   ? 37.116 7.802   4.283  1.00 46.40 ? 327 HOH   A O   1 
HETATM 2234 O  O   . HOH   J 5 .   ? 24.156 16.670  27.318 1.00 36.47 ? 328 HOH   A O   1 
HETATM 2235 O  O   . HOH   J 5 .   ? 12.806 -6.351  22.331 1.00 28.28 ? 329 HOH   A O   1 
HETATM 2236 O  O   . HOH   J 5 .   ? 21.331 10.533  32.255 1.00 44.32 ? 330 HOH   A O   1 
HETATM 2237 O  O   . HOH   J 5 .   ? 23.695 10.978  21.386 1.00 12.91 ? 331 HOH   A O   1 
HETATM 2238 O  O   . HOH   J 5 .   ? 27.964 3.194   -0.352 1.00 23.02 ? 332 HOH   A O   1 
HETATM 2239 O  O   . HOH   J 5 .   ? 12.398 17.755  13.176 1.00 34.71 ? 333 HOH   A O   1 
HETATM 2240 O  O   . HOH   J 5 .   ? 5.286  2.946   21.309 1.00 22.42 ? 334 HOH   A O   1 
HETATM 2241 O  O   . HOH   J 5 .   ? 25.562 17.767  12.687 1.00 17.88 ? 335 HOH   A O   1 
HETATM 2242 O  O   . HOH   J 5 .   ? 23.569 1.736   -0.897 1.00 15.85 ? 336 HOH   A O   1 
HETATM 2243 O  O   . HOH   J 5 .   ? 27.113 19.011  14.832 1.00 17.53 ? 337 HOH   A O   1 
HETATM 2244 O  O   . HOH   J 5 .   ? 35.097 13.774  16.351 1.00 25.45 ? 338 HOH   A O   1 
HETATM 2245 O  O   . HOH   J 5 .   ? 11.438 -0.339  15.917 1.00 23.99 ? 339 HOH   A O   1 
HETATM 2246 O  O   . HOH   J 5 .   ? 2.686  1.397   28.189 1.00 35.51 ? 340 HOH   A O   1 
HETATM 2247 O  O   . HOH   J 5 .   ? 7.334  15.354  29.524 1.00 39.32 ? 341 HOH   A O   1 
HETATM 2248 O  O   . HOH   J 5 .   ? 14.153 -1.953  30.365 1.00 32.30 ? 342 HOH   A O   1 
HETATM 2249 O  O   . HOH   J 5 .   ? 8.973  3.792   12.207 1.00 35.50 ? 343 HOH   A O   1 
HETATM 2250 O  O   . HOH   J 5 .   ? 16.851 -7.367  29.277 1.00 32.55 ? 344 HOH   A O   1 
HETATM 2251 O  O   . HOH   J 5 .   ? 11.464 10.836  9.816  1.00 43.41 ? 345 HOH   A O   1 
HETATM 2252 O  O   . HOH   J 5 .   ? 20.211 2.107   9.373  1.00 15.08 ? 346 HOH   A O   1 
HETATM 2253 O  O   . HOH   J 5 .   ? 35.064 -6.338  21.561 1.00 36.25 ? 347 HOH   A O   1 
HETATM 2254 O  O   . HOH   J 5 .   ? 29.085 13.546  11.235 1.00 30.41 ? 348 HOH   A O   1 
HETATM 2255 O  O   . HOH   J 5 .   ? 28.634 -6.069  3.488  1.00 25.40 ? 349 HOH   A O   1 
HETATM 2256 O  O   . HOH   J 5 .   ? 3.710  18.061  23.814 1.00 32.86 ? 350 HOH   A O   1 
HETATM 2257 O  O   . HOH   J 5 .   ? 30.433 12.699  8.047  1.00 38.25 ? 351 HOH   A O   1 
HETATM 2258 O  O   . HOH   J 5 .   ? 25.737 1.643   29.800 1.00 23.84 ? 352 HOH   A O   1 
HETATM 2259 O  O   . HOH   J 5 .   ? 31.357 0.207   1.775  1.00 34.33 ? 353 HOH   A O   1 
HETATM 2260 O  O   . HOH   J 5 .   ? 19.557 13.339  6.411  1.00 33.91 ? 354 HOH   A O   1 
HETATM 2261 O  O   . HOH   J 5 .   ? 24.000 14.774  29.880 1.00 57.03 ? 355 HOH   A O   1 
HETATM 2262 O  O   . HOH   J 5 .   ? 29.509 7.348   4.162  1.00 34.48 ? 356 HOH   A O   1 
HETATM 2263 O  O   . HOH   J 5 .   ? 29.920 25.786  15.890 1.00 40.43 ? 357 HOH   A O   1 
HETATM 2264 O  O   . HOH   J 5 .   ? 5.134  10.802  12.646 1.00 30.58 ? 358 HOH   A O   1 
HETATM 2265 O  O   . HOH   J 5 .   ? 17.349 2.086   9.397  1.00 17.21 ? 359 HOH   A O   1 
HETATM 2266 O  O   . HOH   J 5 .   ? 4.124  20.137  15.425 1.00 31.17 ? 360 HOH   A O   1 
HETATM 2267 O  O   . HOH   J 5 .   ? 17.211 0.117   2.680  1.00 32.22 ? 361 HOH   A O   1 
HETATM 2268 O  O   . HOH   J 5 .   ? 24.986 4.119   -1.322 1.00 20.95 ? 362 HOH   A O   1 
HETATM 2269 O  O   . HOH   J 5 .   ? 35.565 1.751   26.264 1.00 33.05 ? 363 HOH   A O   1 
HETATM 2270 O  O   . HOH   J 5 .   ? 21.911 8.767   2.824  1.00 23.89 ? 364 HOH   A O   1 
HETATM 2271 O  O   . HOH   J 5 .   ? 4.665  4.058   28.358 1.00 33.91 ? 365 HOH   A O   1 
HETATM 2272 O  O   . HOH   J 5 .   ? 25.168 -8.694  24.824 1.00 34.66 ? 366 HOH   A O   1 
HETATM 2273 O  O   . HOH   J 5 .   ? 22.854 -11.258 30.814 1.00 49.12 ? 367 HOH   A O   1 
HETATM 2274 O  O   . HOH   J 5 .   ? 22.976 20.775  20.238 1.00 25.56 ? 368 HOH   A O   1 
HETATM 2275 O  O   . HOH   J 5 .   ? 13.619 18.660  14.738 1.00 26.38 ? 369 HOH   A O   1 
HETATM 2276 O  O   . HOH   J 5 .   ? 28.088 16.159  10.462 1.00 27.40 ? 370 HOH   A O   1 
HETATM 2277 O  O   . HOH   J 5 .   ? -0.213 10.508  22.036 1.00 48.00 ? 371 HOH   A O   1 
HETATM 2278 O  O   . HOH   J 5 .   ? 21.760 9.866   23.320 1.00 12.63 ? 372 HOH   A O   1 
HETATM 2279 O  O   . HOH   J 5 .   ? 22.429 -6.159  0.492  1.00 40.93 ? 373 HOH   A O   1 
HETATM 2280 O  O   . HOH   J 5 .   ? 20.059 11.845  8.487  1.00 19.00 ? 374 HOH   A O   1 
HETATM 2281 O  O   . HOH   J 5 .   ? 27.200 -8.625  8.342  1.00 35.62 ? 375 HOH   A O   1 
HETATM 2282 O  O   . HOH   J 5 .   ? 4.080  19.832  21.762 1.00 23.35 ? 376 HOH   A O   1 
HETATM 2283 O  O   . HOH   J 5 .   ? 35.588 14.549  20.194 1.00 23.85 ? 377 HOH   A O   1 
HETATM 2284 O  O   . HOH   J 5 .   ? 17.926 20.109  13.599 1.00 22.33 ? 378 HOH   A O   1 
HETATM 2285 O  O   . HOH   J 5 .   ? 17.275 18.361  15.540 1.00 15.24 ? 379 HOH   A O   1 
HETATM 2286 O  O   . HOH   J 5 .   ? 16.704 4.227   6.139  1.00 27.78 ? 380 HOH   A O   1 
HETATM 2287 O  O   . HOH   J 5 .   ? 16.324 8.844   6.804  1.00 23.87 ? 381 HOH   A O   1 
HETATM 2288 O  O   . HOH   J 5 .   ? 31.687 5.843   6.356  1.00 46.96 ? 382 HOH   A O   1 
HETATM 2289 O  O   . HOH   J 5 .   ? 29.815 -2.004  8.460  1.00 21.37 ? 383 HOH   A O   1 
HETATM 2290 O  O   . HOH   J 5 .   ? 28.689 0.936   26.583 1.00 22.52 ? 384 HOH   A O   1 
HETATM 2291 O  O   . HOH   J 5 .   ? 30.684 -5.742  26.266 1.00 28.80 ? 385 HOH   A O   1 
HETATM 2292 O  O   . HOH   J 5 .   ? 26.807 -7.689  24.182 1.00 34.30 ? 386 HOH   A O   1 
HETATM 2293 O  O   . HOH   J 5 .   ? 24.929 -9.128  22.691 1.00 39.53 ? 387 HOH   A O   1 
HETATM 2294 O  O   . HOH   J 5 .   ? 34.757 3.971   26.046 1.00 23.20 ? 388 HOH   A O   1 
HETATM 2295 O  O   . HOH   J 5 .   ? 34.255 0.759   8.543  1.00 20.30 ? 389 HOH   A O   1 
HETATM 2296 O  O   . HOH   J 5 .   ? 20.529 20.392  24.289 1.00 36.30 ? 390 HOH   A O   1 
HETATM 2297 O  O   . HOH   J 5 .   ? 33.965 -3.199  22.916 1.00 37.38 ? 391 HOH   A O   1 
HETATM 2298 O  O   . HOH   J 5 .   ? 18.359 -5.181  30.530 1.00 26.07 ? 392 HOH   A O   1 
HETATM 2299 O  O   . HOH   J 5 .   ? 29.397 25.642  13.227 1.00 28.42 ? 393 HOH   A O   1 
HETATM 2300 O  O   . HOH   J 5 .   ? 2.952  8.535   26.421 1.00 34.18 ? 394 HOH   A O   1 
HETATM 2301 O  O   . HOH   J 5 .   ? 31.892 14.655  12.663 1.00 28.20 ? 395 HOH   A O   1 
HETATM 2302 O  O   . HOH   J 5 .   ? 29.056 22.142  21.864 1.00 29.00 ? 396 HOH   A O   1 
HETATM 2303 O  O   . HOH   J 5 .   ? 26.995 19.320  24.502 1.00 43.69 ? 397 HOH   A O   1 
HETATM 2304 O  O   . HOH   J 5 .   ? 25.553 20.510  21.748 1.00 38.75 ? 398 HOH   A O   1 
HETATM 2305 O  O   . HOH   J 5 .   ? 20.133 13.879  29.001 1.00 26.80 ? 399 HOH   A O   1 
HETATM 2306 O  O   . HOH   J 5 .   ? 15.989 12.105  30.697 1.00 32.17 ? 400 HOH   A O   1 
HETATM 2307 O  O   . HOH   J 5 .   ? 3.538  2.180   19.329 1.00 30.25 ? 401 HOH   A O   1 
HETATM 2308 O  O   . HOH   J 5 .   ? 16.401 -0.713  12.885 1.00 22.00 ? 402 HOH   A O   1 
HETATM 2309 O  O   . HOH   J 5 .   ? 22.441 -8.380  19.434 1.00 28.69 ? 403 HOH   A O   1 
HETATM 2310 O  O   . HOH   J 5 .   ? 30.718 -2.909  11.465 1.00 29.30 ? 404 HOH   A O   1 
HETATM 2311 O  O   . HOH   J 5 .   ? 29.986 6.495   29.983 1.00 32.97 ? 405 HOH   A O   1 
HETATM 2312 O  O   . HOH   J 5 .   ? 33.212 -2.741  15.282 1.00 26.41 ? 406 HOH   A O   1 
HETATM 2313 O  O   . HOH   J 5 .   ? 20.016 -4.669  15.190 1.00 24.95 ? 407 HOH   A O   1 
HETATM 2314 O  O   . HOH   J 5 .   ? 28.060 11.987  27.539 1.00 22.71 ? 408 HOH   A O   1 
HETATM 2315 O  O   . HOH   J 5 .   ? 4.873  10.334  14.960 1.00 40.30 ? 409 HOH   A O   1 
HETATM 2316 O  O   . HOH   J 5 .   ? 15.121 -4.199  16.257 1.00 29.13 ? 410 HOH   A O   1 
HETATM 2317 O  O   . HOH   J 5 .   ? 1.029  17.772  23.278 1.00 53.09 ? 411 HOH   A O   1 
HETATM 2318 O  O   . HOH   J 5 .   ? 32.174 22.094  11.072 1.00 29.77 ? 412 HOH   A O   1 
HETATM 2319 O  O   . HOH   J 5 .   ? 23.920 17.699  6.003  1.00 41.69 ? 413 HOH   A O   1 
HETATM 2320 O  O   . HOH   J 5 .   ? 27.391 -6.433  29.786 1.00 45.82 ? 414 HOH   A O   1 
HETATM 2321 O  O   . HOH   J 5 .   ? 33.032 12.476  27.533 1.00 35.41 ? 415 HOH   A O   1 
HETATM 2322 O  O   . HOH   J 5 .   ? 6.641  16.115  8.967  1.00 29.29 ? 416 HOH   A O   1 
HETATM 2323 O  O   . HOH   J 5 .   ? 17.808 16.715  28.684 1.00 47.74 ? 417 HOH   A O   1 
HETATM 2324 O  O   . HOH   J 5 .   ? 31.933 8.604   4.715  1.00 42.11 ? 418 HOH   A O   1 
HETATM 2325 O  O   . HOH   J 5 .   ? 3.832  14.526  10.591 1.00 30.54 ? 419 HOH   A O   1 
HETATM 2326 O  O   . HOH   J 5 .   ? 12.440 18.393  26.597 1.00 25.03 ? 420 HOH   A O   1 
HETATM 2327 O  O   . HOH   J 5 .   ? 16.075 -5.584  5.250  1.00 51.69 ? 421 HOH   A O   1 
HETATM 2328 O  O   . HOH   J 5 .   ? 11.252 2.001   12.647 1.00 23.36 ? 422 HOH   A O   1 
HETATM 2329 O  O   . HOH   J 5 .   ? 15.210 23.100  16.868 1.00 20.45 ? 423 HOH   A O   1 
HETATM 2330 O  O   . HOH   J 5 .   ? 19.737 -6.307  32.803 1.00 36.18 ? 424 HOH   A O   1 
HETATM 2331 O  O   . HOH   J 5 .   ? -1.273 10.955  19.675 1.00 44.55 ? 425 HOH   A O   1 
HETATM 2332 O  O   . HOH   J 5 .   ? 32.932 -6.784  14.971 1.00 38.06 ? 426 HOH   A O   1 
HETATM 2333 O  O   . HOH   J 5 .   ? 13.244 8.467   11.251 1.00 19.52 ? 427 HOH   A O   1 
HETATM 2334 O  O   . HOH   J 5 .   ? 2.661  14.091  25.066 1.00 57.53 ? 428 HOH   A O   1 
HETATM 2335 O  O   . HOH   J 5 .   ? 30.308 -1.927  3.525  1.00 36.23 ? 429 HOH   A O   1 
HETATM 2336 O  O   . HOH   J 5 .   ? 12.269 -2.855  15.898 1.00 47.21 ? 430 HOH   A O   1 
HETATM 2337 O  O   . HOH   J 5 .   ? 32.004 -7.019  17.904 1.00 33.01 ? 431 HOH   A O   1 
HETATM 2338 O  O   . HOH   J 5 .   ? 19.847 -9.780  20.515 1.00 26.65 ? 432 HOH   A O   1 
HETATM 2339 O  O   . HOH   J 5 .   ? 10.809 6.756   11.587 1.00 36.75 ? 433 HOH   A O   1 
HETATM 2340 O  O   . HOH   J 5 .   ? 11.944 15.094  8.976  1.00 57.60 ? 434 HOH   A O   1 
HETATM 2341 O  O   . HOH   J 5 .   ? 16.270 -5.251  12.457 1.00 32.26 ? 435 HOH   A O   1 
HETATM 2342 O  O   . HOH   J 5 .   ? 16.025 8.404   34.202 1.00 32.20 ? 436 HOH   A O   1 
HETATM 2343 O  O   . HOH   J 5 .   ? 25.142 -5.275  32.778 1.00 38.47 ? 437 HOH   A O   1 
HETATM 2344 O  O   . HOH   J 5 .   ? 18.856 23.348  17.977 1.00 53.32 ? 438 HOH   A O   1 
HETATM 2345 O  O   . HOH   J 5 .   ? 5.547  2.555   11.964 1.00 54.38 ? 439 HOH   A O   1 
HETATM 2346 O  O   . HOH   J 5 .   ? 17.921 10.777  6.764  1.00 29.47 ? 440 HOH   A O   1 
HETATM 2347 O  O   . HOH   J 5 .   ? 23.825 9.407   32.208 1.00 54.06 ? 441 HOH   A O   1 
HETATM 2348 O  O   . HOH   J 5 .   ? 8.980  -2.782  27.638 1.00 54.65 ? 442 HOH   A O   1 
HETATM 2349 O  O   . HOH   J 5 .   ? 26.002 18.367  26.498 1.00 43.53 ? 443 HOH   A O   1 
HETATM 2350 O  O   . HOH   J 5 .   ? 2.728  21.183  12.337 1.00 63.12 ? 444 HOH   A O   1 
HETATM 2351 O  O   . HOH   J 5 .   ? 26.457 21.977  6.092  1.00 39.93 ? 445 HOH   A O   1 
HETATM 2352 O  O   . HOH   J 5 .   ? 17.145 10.470  32.177 1.00 36.18 ? 446 HOH   A O   1 
HETATM 2353 O  O   . HOH   J 5 .   ? 8.817  17.803  8.713  1.00 51.11 ? 447 HOH   A O   1 
HETATM 2354 O  O   . HOH   J 5 .   ? 23.371 22.761  18.439 1.00 30.17 ? 448 HOH   A O   1 
HETATM 2355 O  O   . HOH   J 5 .   ? 13.850 21.522  14.772 1.00 24.75 ? 449 HOH   A O   1 
HETATM 2356 O  O   . HOH   J 5 .   ? 33.136 1.191   6.078  1.00 26.69 ? 450 HOH   A O   1 
HETATM 2357 O  O   . HOH   J 5 .   ? 28.376 1.595   29.342 1.00 30.15 ? 451 HOH   A O   1 
HETATM 2358 O  O   . HOH   J 5 .   ? 4.672  -0.511  17.676 1.00 45.10 ? 452 HOH   A O   1 
HETATM 2359 O  O   . HOH   J 5 .   ? 21.381 23.842  17.213 1.00 31.84 ? 453 HOH   A O   1 
HETATM 2360 O  O   . HOH   J 5 .   ? 2.012  16.293  9.537  1.00 41.51 ? 454 HOH   A O   1 
HETATM 2361 O  O   . HOH   J 5 .   ? 35.277 11.533  15.155 1.00 38.73 ? 455 HOH   A O   1 
HETATM 2362 O  O   . HOH   J 5 .   ? 33.885 -2.098  9.008  1.00 27.71 ? 456 HOH   A O   1 
HETATM 2363 O  O   . HOH   J 5 .   ? 2.243  21.454  20.384 1.00 30.57 ? 457 HOH   A O   1 
HETATM 2364 O  O   . HOH   J 5 .   ? 16.936 -3.530  14.001 1.00 27.53 ? 458 HOH   A O   1 
HETATM 2365 O  O   . HOH   J 5 .   ? 25.661 14.572  6.066  1.00 35.15 ? 459 HOH   A O   1 
HETATM 2366 O  O   . HOH   J 5 .   ? 2.908  3.737   17.273 1.00 32.53 ? 460 HOH   A O   1 
HETATM 2367 O  O   . HOH   J 5 .   ? 13.427 9.784   8.276  1.00 45.04 ? 461 HOH   A O   1 
HETATM 2368 O  O   . HOH   J 5 .   ? 22.806 11.023  1.606  1.00 35.53 ? 462 HOH   A O   1 
HETATM 2369 O  O   . HOH   J 5 .   ? 28.682 4.035   30.444 1.00 40.69 ? 463 HOH   A O   1 
HETATM 2370 O  O   . HOH   J 5 .   ? 25.163 24.504  19.459 1.00 30.26 ? 464 HOH   A O   1 
HETATM 2371 O  O   . HOH   K 5 .   ? 10.325 -22.775 4.866  1.00 22.13 ? 301 HOH   C O   1 
HETATM 2372 O  O   . HOH   K 5 .   ? 24.247 -37.247 10.375 1.00 39.96 ? 302 HOH   C O   1 
HETATM 2373 O  O   . HOH   K 5 .   ? 2.560  -22.880 10.481 1.00 30.19 ? 303 HOH   C O   1 
HETATM 2374 O  O   . HOH   K 5 .   ? 31.043 -10.580 10.378 1.00 33.01 ? 304 HOH   C O   1 
HETATM 2375 O  O   . HOH   K 5 .   ? 10.867 -27.372 33.686 1.00 27.98 ? 305 HOH   C O   1 
HETATM 2376 O  O   . HOH   K 5 .   ? 17.183 -37.796 3.110  1.00 39.91 ? 306 HOH   C O   1 
HETATM 2377 O  O   . HOH   K 5 .   ? 35.801 -15.342 15.829 1.00 38.53 ? 307 HOH   C O   1 
HETATM 2378 O  O   . HOH   K 5 .   ? 23.780 -9.235  7.787  1.00 21.73 ? 308 HOH   C O   1 
HETATM 2379 O  O   . HOH   K 5 .   ? 0.334  -15.175 22.544 1.00 34.45 ? 309 HOH   C O   1 
HETATM 2380 O  O   . HOH   K 5 .   ? 31.160 -21.296 13.099 1.00 29.56 ? 310 HOH   C O   1 
HETATM 2381 O  O   . HOH   K 5 .   ? 27.519 -15.250 2.524  1.00 36.51 ? 311 HOH   C O   1 
HETATM 2382 O  O   . HOH   K 5 .   ? 23.634 -31.222 15.080 1.00 24.83 ? 312 HOH   C O   1 
HETATM 2383 O  O   . HOH   K 5 .   ? 12.630 -29.348 33.565 1.00 20.02 ? 313 HOH   C O   1 
HETATM 2384 O  O   . HOH   K 5 .   ? 14.319 -19.620 0.901  1.00 30.89 ? 314 HOH   C O   1 
HETATM 2385 O  O   . HOH   K 5 .   ? 26.551 -22.966 -0.154 1.00 38.08 ? 315 HOH   C O   1 
HETATM 2386 O  O   . HOH   K 5 .   ? 3.819  -23.200 3.766  1.00 28.97 ? 316 HOH   C O   1 
HETATM 2387 O  O   . HOH   K 5 .   ? 10.066 -26.121 3.592  1.00 16.38 ? 317 HOH   C O   1 
HETATM 2388 O  O   . HOH   K 5 .   ? 4.325  -35.804 21.533 1.00 22.35 ? 318 HOH   C O   1 
HETATM 2389 O  O   . HOH   K 5 .   ? -0.342 -16.906 11.563 1.00 41.43 ? 319 HOH   C O   1 
HETATM 2390 O  O   . HOH   K 5 .   ? 0.795  -16.701 17.876 1.00 29.30 ? 320 HOH   C O   1 
HETATM 2391 O  O   . HOH   K 5 .   ? 22.247 -32.679 3.812  1.00 28.28 ? 321 HOH   C O   1 
HETATM 2392 O  O   . HOH   K 5 .   ? 20.614 -22.313 18.700 1.00 12.66 ? 322 HOH   C O   1 
HETATM 2393 O  O   . HOH   K 5 .   ? 6.134  -10.644 25.965 1.00 38.94 ? 323 HOH   C O   1 
HETATM 2394 O  O   . HOH   K 5 .   ? 16.158 -38.760 10.223 1.00 46.88 ? 324 HOH   C O   1 
HETATM 2395 O  O   . HOH   K 5 .   ? 10.660 -12.750 20.574 1.00 16.03 ? 325 HOH   C O   1 
HETATM 2396 O  O   . HOH   K 5 .   ? 2.689  -31.248 3.874  1.00 30.44 ? 326 HOH   C O   1 
HETATM 2397 O  O   . HOH   K 5 .   ? 7.146  -36.575 29.274 1.00 33.52 ? 327 HOH   C O   1 
HETATM 2398 O  O   . HOH   K 5 .   ? 18.040 -9.971  9.360  1.00 20.40 ? 328 HOH   C O   1 
HETATM 2399 O  O   . HOH   K 5 .   ? 22.881 -36.020 12.275 1.00 39.19 ? 329 HOH   C O   1 
HETATM 2400 O  O   . HOH   K 5 .   ? 0.947  -31.403 17.060 1.00 13.49 ? 330 HOH   C O   1 
HETATM 2401 O  O   . HOH   K 5 .   ? 22.191 -12.307 17.184 1.00 22.88 ? 331 HOH   C O   1 
HETATM 2402 O  O   . HOH   K 5 .   ? 11.215 -14.001 5.776  1.00 54.44 ? 332 HOH   C O   1 
HETATM 2403 O  O   . HOH   K 5 .   ? 17.950 -7.717  21.718 1.00 22.14 ? 333 HOH   C O   1 
HETATM 2404 O  O   . HOH   K 5 .   ? 18.418 -11.852 5.451  1.00 37.79 ? 334 HOH   C O   1 
HETATM 2405 O  O   . HOH   K 5 .   ? 11.725 -20.493 0.693  1.00 36.70 ? 335 HOH   C O   1 
HETATM 2406 O  O   . HOH   K 5 .   ? 7.934  -34.816 0.660  1.00 18.98 ? 336 HOH   C O   1 
HETATM 2407 O  O   . HOH   K 5 .   ? 15.578 -28.765 23.131 1.00 14.56 ? 337 HOH   C O   1 
HETATM 2408 O  O   . HOH   K 5 .   ? 11.534 -19.464 11.558 1.00 15.00 ? 338 HOH   C O   1 
HETATM 2409 O  O   . HOH   K 5 .   ? 34.808 -10.958 10.721 1.00 38.95 ? 339 HOH   C O   1 
HETATM 2410 O  O   . HOH   K 5 .   ? 7.320  -38.933 7.299  1.00 45.30 ? 340 HOH   C O   1 
HETATM 2411 O  O   . HOH   K 5 .   ? 8.438  -28.227 3.040  1.00 19.46 ? 341 HOH   C O   1 
HETATM 2412 O  O   . HOH   K 5 .   ? 26.246 -33.006 5.844  1.00 39.83 ? 342 HOH   C O   1 
HETATM 2413 O  O   . HOH   K 5 .   ? 11.458 -35.808 -0.702 1.00 28.15 ? 343 HOH   C O   1 
HETATM 2414 O  O   . HOH   K 5 .   ? -1.485 -31.250 4.842  1.00 32.02 ? 344 HOH   C O   1 
HETATM 2415 O  O   . HOH   K 5 .   ? 27.780 -27.521 2.170  1.00 31.03 ? 345 HOH   C O   1 
HETATM 2416 O  O   . HOH   K 5 .   ? 5.617  -24.944 24.337 1.00 22.32 ? 346 HOH   C O   1 
HETATM 2417 O  O   . HOH   K 5 .   ? 14.803 -22.199 29.907 1.00 22.62 ? 347 HOH   C O   1 
HETATM 2418 O  O   . HOH   K 5 .   ? 29.541 -27.970 9.984  1.00 22.44 ? 348 HOH   C O   1 
HETATM 2419 O  O   . HOH   K 5 .   ? 9.853  -40.634 1.211  1.00 41.58 ? 349 HOH   C O   1 
HETATM 2420 O  O   . HOH   K 5 .   ? 7.167  -23.074 29.149 1.00 28.21 ? 350 HOH   C O   1 
HETATM 2421 O  O   . HOH   K 5 .   ? 6.117  -32.536 29.653 1.00 38.88 ? 351 HOH   C O   1 
HETATM 2422 O  O   . HOH   K 5 .   ? 8.759  -11.533 18.583 1.00 17.57 ? 352 HOH   C O   1 
HETATM 2423 O  O   . HOH   K 5 .   ? 5.673  -17.590 25.295 1.00 28.04 ? 353 HOH   C O   1 
HETATM 2424 O  O   . HOH   K 5 .   ? 4.689  -16.141 21.495 1.00 28.83 ? 354 HOH   C O   1 
HETATM 2425 O  O   . HOH   K 5 .   ? 31.472 -10.770 16.529 1.00 21.93 ? 355 HOH   C O   1 
HETATM 2426 O  O   . HOH   K 5 .   ? 16.094 -18.911 24.143 1.00 17.01 ? 356 HOH   C O   1 
HETATM 2427 O  O   . HOH   K 5 .   ? 21.503 -36.486 10.009 1.00 27.04 ? 357 HOH   C O   1 
HETATM 2428 O  O   . HOH   K 5 .   ? 4.826  -30.301 31.185 1.00 41.83 ? 358 HOH   C O   1 
HETATM 2429 O  O   . HOH   K 5 .   ? 30.653 -20.195 19.094 1.00 27.23 ? 359 HOH   C O   1 
HETATM 2430 O  O   . HOH   K 5 .   ? 4.156  -26.700 28.087 1.00 30.21 ? 360 HOH   C O   1 
HETATM 2431 O  O   . HOH   K 5 .   ? 11.169 -36.298 31.495 1.00 30.19 ? 361 HOH   C O   1 
HETATM 2432 O  O   . HOH   K 5 .   ? 33.176 -34.896 9.942  1.00 41.96 ? 362 HOH   C O   1 
HETATM 2433 O  O   . HOH   K 5 .   ? 18.402 -28.744 22.942 1.00 19.67 ? 363 HOH   C O   1 
HETATM 2434 O  O   . HOH   K 5 .   ? 26.574 -27.311 19.405 1.00 39.59 ? 364 HOH   C O   1 
HETATM 2435 O  O   . HOH   K 5 .   ? 23.689 -12.853 19.132 1.00 27.11 ? 365 HOH   C O   1 
HETATM 2436 O  O   . HOH   K 5 .   ? 29.810 -26.350 2.932  1.00 33.42 ? 366 HOH   C O   1 
HETATM 2437 O  O   . HOH   K 5 .   ? 24.883 -20.686 20.348 1.00 36.81 ? 367 HOH   C O   1 
HETATM 2438 O  O   . HOH   K 5 .   ? 20.054 -31.626 27.002 1.00 28.81 ? 368 HOH   C O   1 
HETATM 2439 O  O   . HOH   K 5 .   ? 30.687 -20.402 16.436 1.00 42.42 ? 369 HOH   C O   1 
HETATM 2440 O  O   . HOH   K 5 .   ? 13.194 -20.562 9.468  1.00 13.80 ? 370 HOH   C O   1 
HETATM 2441 O  O   . HOH   K 5 .   ? 1.482  -29.307 24.960 1.00 27.95 ? 371 HOH   C O   1 
HETATM 2442 O  O   . HOH   K 5 .   ? 21.142 -15.163 26.114 1.00 40.53 ? 372 HOH   C O   1 
HETATM 2443 O  O   . HOH   K 5 .   ? 35.462 -29.078 4.784  1.00 46.93 ? 373 HOH   C O   1 
HETATM 2444 O  O   . HOH   K 5 .   ? 26.471 -32.955 13.848 1.00 27.14 ? 374 HOH   C O   1 
HETATM 2445 O  O   . HOH   K 5 .   ? 1.155  -33.704 20.504 1.00 24.40 ? 375 HOH   C O   1 
HETATM 2446 O  O   . HOH   K 5 .   ? 1.097  -19.306 22.331 1.00 53.11 ? 376 HOH   C O   1 
HETATM 2447 O  O   . HOH   K 5 .   ? 18.532 -12.367 17.026 1.00 16.02 ? 377 HOH   C O   1 
HETATM 2448 O  O   . HOH   K 5 .   ? 15.221 -35.438 1.665  1.00 21.04 ? 378 HOH   C O   1 
HETATM 2449 O  O   . HOH   K 5 .   ? 3.769  -36.058 6.863  1.00 22.88 ? 379 HOH   C O   1 
HETATM 2450 O  O   . HOH   K 5 .   ? 19.882 -22.167 25.497 1.00 21.61 ? 380 HOH   C O   1 
HETATM 2451 O  O   . HOH   K 5 .   ? 14.937 -35.573 17.026 1.00 22.28 ? 381 HOH   C O   1 
HETATM 2452 O  O   . HOH   K 5 .   ? 36.555 -32.028 8.977  1.00 53.40 ? 382 HOH   C O   1 
HETATM 2453 O  O   . HOH   K 5 .   ? 7.022  -16.522 22.781 1.00 29.54 ? 383 HOH   C O   1 
HETATM 2454 O  O   . HOH   K 5 .   ? 18.222 -10.579 18.862 1.00 33.15 ? 384 HOH   C O   1 
HETATM 2455 O  O   . HOH   K 5 .   ? 19.448 -27.079 25.527 1.00 30.04 ? 385 HOH   C O   1 
HETATM 2456 O  O   . HOH   K 5 .   ? 14.490 -16.575 3.785  1.00 26.74 ? 386 HOH   C O   1 
HETATM 2457 O  O   . HOH   K 5 .   ? -0.257 -15.932 14.225 1.00 28.93 ? 387 HOH   C O   1 
HETATM 2458 O  O   . HOH   K 5 .   ? 21.091 -12.047 21.253 1.00 29.57 ? 388 HOH   C O   1 
HETATM 2459 O  O   . HOH   K 5 .   ? 8.728  -38.463 9.509  1.00 25.62 ? 389 HOH   C O   1 
HETATM 2460 O  O   . HOH   K 5 .   ? 18.556 -18.249 1.609  1.00 37.96 ? 390 HOH   C O   1 
HETATM 2461 O  O   . HOH   K 5 .   ? 5.622  -29.062 7.325  1.00 14.46 ? 391 HOH   C O   1 
HETATM 2462 O  O   . HOH   K 5 .   ? 8.451  -14.357 23.171 1.00 27.28 ? 392 HOH   C O   1 
HETATM 2463 O  O   . HOH   K 5 .   ? 22.108 -14.779 23.602 1.00 31.33 ? 393 HOH   C O   1 
HETATM 2464 O  O   . HOH   K 5 .   ? 4.273  -8.709  22.950 1.00 28.14 ? 394 HOH   C O   1 
HETATM 2465 O  O   . HOH   K 5 .   ? 6.758  -18.142 5.836  1.00 19.46 ? 395 HOH   C O   1 
HETATM 2466 O  O   . HOH   K 5 .   ? 29.234 -14.588 22.541 1.00 30.56 ? 396 HOH   C O   1 
HETATM 2467 O  O   . HOH   K 5 .   ? 4.381  -24.174 26.483 1.00 26.09 ? 397 HOH   C O   1 
HETATM 2468 O  O   . HOH   K 5 .   ? 12.339 -9.706  12.659 1.00 32.12 ? 398 HOH   C O   1 
HETATM 2469 O  O   . HOH   K 5 .   ? 22.557 -12.199 5.784  1.00 24.00 ? 399 HOH   C O   1 
HETATM 2470 O  O   . HOH   K 5 .   ? 31.250 -26.087 -2.703 1.00 56.50 ? 400 HOH   C O   1 
HETATM 2471 O  O   . HOH   K 5 .   ? 19.677 -7.354  15.137 1.00 19.43 ? 401 HOH   C O   1 
HETATM 2472 O  O   . HOH   K 5 .   ? 5.836  -32.496 24.494 1.00 19.30 ? 402 HOH   C O   1 
HETATM 2473 O  O   . HOH   K 5 .   ? 1.986  -17.539 6.184  1.00 31.20 ? 403 HOH   C O   1 
HETATM 2474 O  O   . HOH   K 5 .   ? 19.033 -31.483 19.252 1.00 18.50 ? 404 HOH   C O   1 
HETATM 2475 O  O   . HOH   K 5 .   ? 8.356  -39.528 24.483 1.00 34.86 ? 405 HOH   C O   1 
HETATM 2476 O  O   . HOH   K 5 .   ? 2.163  -37.637 14.734 1.00 40.98 ? 406 HOH   C O   1 
HETATM 2477 O  O   . HOH   K 5 .   ? 9.780  -9.985  11.307 1.00 39.37 ? 407 HOH   C O   1 
HETATM 2478 O  O   . HOH   K 5 .   ? 28.743 -33.245 12.429 1.00 28.70 ? 408 HOH   C O   1 
HETATM 2479 O  O   . HOH   K 5 .   ? 16.904 -7.848  14.705 1.00 33.11 ? 409 HOH   C O   1 
HETATM 2480 O  O   . HOH   K 5 .   ? 4.477  -33.310 22.340 1.00 27.65 ? 410 HOH   C O   1 
HETATM 2481 O  O   . HOH   K 5 .   ? 1.417  -34.083 17.848 1.00 18.31 ? 411 HOH   C O   1 
HETATM 2482 O  O   . HOH   K 5 .   ? 35.030 -24.442 13.286 1.00 63.25 ? 412 HOH   C O   1 
HETATM 2483 O  O   . HOH   K 5 .   ? 24.217 -28.972 18.969 1.00 26.04 ? 413 HOH   C O   1 
HETATM 2484 O  O   . HOH   K 5 .   ? 31.616 -22.026 4.815  1.00 31.82 ? 414 HOH   C O   1 
HETATM 2485 O  O   . HOH   K 5 .   ? 12.115 -38.927 13.037 1.00 29.42 ? 415 HOH   C O   1 
HETATM 2486 O  O   . HOH   K 5 .   ? 10.744 -15.043 3.420  1.00 36.06 ? 416 HOH   C O   1 
HETATM 2487 O  O   . HOH   K 5 .   ? 6.304  -8.226  11.760 1.00 33.89 ? 417 HOH   C O   1 
HETATM 2488 O  O   . HOH   K 5 .   ? 32.258 -16.695 20.738 1.00 24.02 ? 418 HOH   C O   1 
HETATM 2489 O  O   . HOH   K 5 .   ? 34.196 -21.296 13.590 1.00 50.89 ? 419 HOH   C O   1 
HETATM 2490 O  O   . HOH   K 5 .   ? 17.433 -40.189 7.305  1.00 54.39 ? 420 HOH   C O   1 
HETATM 2491 O  O   . HOH   K 5 .   ? -0.402 -35.655 16.609 1.00 31.38 ? 421 HOH   C O   1 
HETATM 2492 O  O   . HOH   K 5 .   ? 13.543 -42.183 4.328  1.00 47.81 ? 422 HOH   C O   1 
HETATM 2493 O  O   . HOH   K 5 .   ? 19.746 -24.244 27.733 1.00 33.90 ? 423 HOH   C O   1 
HETATM 2494 O  O   . HOH   K 5 .   ? 22.648 -22.460 20.734 1.00 19.35 ? 424 HOH   C O   1 
HETATM 2495 O  O   . HOH   K 5 .   ? 31.271 -28.902 11.895 1.00 27.83 ? 425 HOH   C O   1 
HETATM 2496 O  O   . HOH   K 5 .   ? 8.028  -5.360  14.735 1.00 36.58 ? 426 HOH   C O   1 
HETATM 2497 O  O   . HOH   K 5 .   ? 4.797  -38.487 7.037  1.00 66.81 ? 427 HOH   C O   1 
HETATM 2498 O  O   . HOH   K 5 .   ? 24.709 -15.402 22.922 1.00 53.69 ? 428 HOH   C O   1 
HETATM 2499 O  O   . HOH   K 5 .   ? 20.613 -9.036  17.587 1.00 33.67 ? 429 HOH   C O   1 
HETATM 2500 O  O   . HOH   K 5 .   ? 24.865 -24.185 20.081 1.00 36.70 ? 430 HOH   C O   1 
HETATM 2501 O  O   . HOH   K 5 .   ? 32.423 -16.476 6.546  1.00 49.57 ? 431 HOH   C O   1 
HETATM 2502 O  O   . HOH   K 5 .   ? 5.760  -28.524 4.352  1.00 37.28 ? 432 HOH   C O   1 
HETATM 2503 O  O   . HOH   K 5 .   ? 6.902  -36.279 2.928  1.00 23.75 ? 433 HOH   C O   1 
HETATM 2504 O  O   . HOH   K 5 .   ? 28.350 -9.255  18.753 1.00 42.20 ? 434 HOH   C O   1 
HETATM 2505 O  O   . HOH   K 5 .   ? 30.948 -8.997  18.262 1.00 42.50 ? 435 HOH   C O   1 
HETATM 2506 O  O   . HOH   K 5 .   ? 30.779 -23.806 2.114  1.00 42.59 ? 436 HOH   C O   1 
HETATM 2507 O  O   . HOH   K 5 .   ? 15.961 -17.217 26.038 1.00 34.99 ? 437 HOH   C O   1 
HETATM 2508 O  O   . HOH   K 5 .   ? 20.240 -23.745 -4.601 1.00 36.92 ? 438 HOH   C O   1 
HETATM 2509 O  O   . HOH   K 5 .   ? 9.321  -13.924 25.707 1.00 43.08 ? 439 HOH   C O   1 
HETATM 2510 O  O   . HOH   K 5 .   ? 34.792 -13.874 17.947 1.00 32.92 ? 440 HOH   C O   1 
HETATM 2511 O  O   . HOH   K 5 .   ? 18.202 -20.103 25.807 1.00 28.59 ? 441 HOH   C O   1 
HETATM 2512 O  O   . HOH   K 5 .   ? 0.118  -34.099 9.931  1.00 50.39 ? 442 HOH   C O   1 
HETATM 2513 O  O   . HOH   K 5 .   ? 32.200 -22.748 15.259 1.00 36.61 ? 443 HOH   C O   1 
HETATM 2514 O  O   . HOH   K 5 .   ? 19.463 -21.932 -2.728 1.00 33.23 ? 444 HOH   C O   1 
HETATM 2515 O  O   . HOH   K 5 .   ? 8.961  -11.821 6.775  1.00 36.52 ? 445 HOH   C O   1 
HETATM 2516 O  O   . HOH   K 5 .   ? 12.491 -7.608  14.244 1.00 33.35 ? 446 HOH   C O   1 
HETATM 2517 O  O   . HOH   K 5 .   ? 29.195 -22.109 21.070 1.00 35.06 ? 447 HOH   C O   1 
HETATM 2518 O  O   . HOH   K 5 .   ? 30.639 -31.334 13.190 1.00 33.46 ? 448 HOH   C O   1 
HETATM 2519 O  O   . HOH   K 5 .   ? 17.422 -34.675 18.064 1.00 34.98 ? 449 HOH   C O   1 
HETATM 2520 O  O   . HOH   K 5 .   ? 10.371 -9.955  27.582 1.00 62.28 ? 450 HOH   C O   1 
HETATM 2521 O  O   . HOH   K 5 .   ? 5.057  -22.067 27.991 1.00 32.38 ? 451 HOH   C O   1 
HETATM 2522 O  O   . HOH   K 5 .   ? 8.824  -23.728 2.771  1.00 25.91 ? 452 HOH   C O   1 
HETATM 2523 O  O   . HOH   K 5 .   ? 2.764  -28.762 27.306 1.00 31.61 ? 453 HOH   C O   1 
HETATM 2524 O  O   . HOH   K 5 .   ? 2.444  -17.127 22.800 1.00 33.19 ? 454 HOH   C O   1 
HETATM 2525 O  O   . HOH   K 5 .   ? 17.931 -9.900  29.250 1.00 42.16 ? 455 HOH   C O   1 
HETATM 2526 O  O   . HOH   K 5 .   ? 32.482 -19.329 20.908 1.00 35.19 ? 456 HOH   C O   1 
HETATM 2527 O  O   . HOH   K 5 .   ? 33.076 -9.503  14.621 1.00 29.29 ? 457 HOH   C O   1 
HETATM 2528 O  O   . HOH   K 5 .   ? 16.350 -17.430 1.899  1.00 41.78 ? 458 HOH   C O   1 
HETATM 2529 O  O   . HOH   K 5 .   ? 20.276 -35.427 22.122 1.00 55.02 ? 459 HOH   C O   1 
HETATM 2530 O  O   . HOH   K 5 .   ? 33.118 -9.240  11.777 1.00 37.46 ? 460 HOH   C O   1 
HETATM 2531 O  O   . HOH   K 5 .   ? 9.550  -39.613 12.367 1.00 32.93 ? 461 HOH   C O   1 
HETATM 2532 O  O   . HOH   K 5 .   ? 3.182  -17.198 25.323 1.00 35.17 ? 462 HOH   C O   1 
HETATM 2533 O  O   . HOH   K 5 .   ? 10.635 -16.015 26.950 1.00 39.79 ? 463 HOH   C O   1 
HETATM 2534 O  O   . HOH   K 5 .   ? 32.063 -27.174 13.824 1.00 33.34 ? 464 HOH   C O   1 
HETATM 2535 O  O   . HOH   K 5 .   ? 31.967 -36.149 12.205 1.00 34.26 ? 465 HOH   C O   1 
HETATM 2536 O  O   . HOH   K 5 .   ? 26.685 -21.090 22.652 1.00 40.81 ? 466 HOH   C O   1 
HETATM 2537 O  O   . HOH   K 5 .   ? 8.746  -21.257 30.090 1.00 31.63 ? 467 HOH   C O   1 
HETATM 2538 O  O   . HOH   K 5 .   ? 29.841 -8.700  9.244  1.00 36.15 ? 468 HOH   C O   1 
HETATM 2539 O  O   . HOH   K 5 .   ? 5.496  -39.629 23.482 1.00 30.65 ? 469 HOH   C O   1 
HETATM 2540 O  O   . HOH   K 5 .   ? 30.493 -30.644 16.069 1.00 50.58 ? 470 HOH   C O   1 
HETATM 2541 O  O   . HOH   K 5 .   ? 35.717 -10.317 15.600 1.00 29.01 ? 471 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   ? 0.2377 0.2453 0.2212 0.0093  -0.0230 0.0141  7   SER   A N   
2    C  CA  . SER   A 1   ? 0.2429 0.2532 0.2383 0.0070  -0.0253 0.0120  7   SER   A CA  
3    C  C   . SER   A 1   ? 0.2340 0.2456 0.2345 0.0040  -0.0241 0.0084  7   SER   A C   
4    O  O   . SER   A 1   ? 0.2419 0.2519 0.2357 0.0042  -0.0235 0.0071  7   SER   A O   
5    C  CB  . SER   A 1   ? 0.2881 0.2979 0.2842 0.0096  -0.0325 0.0109  7   SER   A CB  
6    O  OG  . SER   A 1   ? 0.3329 0.3411 0.3225 0.0111  -0.0370 0.0076  7   SER   A OG  
7    N  N   . GLY   A 2   ? 0.2147 0.2285 0.2264 0.0016  -0.0231 0.0073  8   GLY   A N   
8    C  CA  . GLY   A 2   ? 0.2037 0.2174 0.2198 -0.0008 -0.0209 0.0048  8   GLY   A CA  
9    C  C   . GLY   A 2   ? 0.1900 0.2052 0.2147 -0.0026 -0.0164 0.0052  8   GLY   A C   
10   O  O   . GLY   A 2   ? 0.1813 0.1973 0.2063 -0.0023 -0.0143 0.0070  8   GLY   A O   
11   N  N   . ALA   A 3   ? 0.1715 0.1863 0.2029 -0.0043 -0.0146 0.0034  9   ALA   A N   
12   C  CA  . ALA   A 3   ? 0.1865 0.2016 0.2244 -0.0054 -0.0096 0.0037  9   ALA   A CA  
13   C  C   . ALA   A 3   ? 0.1851 0.1971 0.2225 -0.0064 -0.0051 0.0028  9   ALA   A C   
14   O  O   . ALA   A 3   ? 0.1890 0.1992 0.2252 -0.0069 -0.0068 0.0015  9   ALA   A O   
15   C  CB  . ALA   A 3   ? 0.1976 0.2155 0.2485 -0.0060 -0.0111 0.0033  9   ALA   A CB  
16   N  N   . ILE   A 4   ? 0.1602 0.1708 0.1981 -0.0063 0.0005  0.0035  10  ILE   A N   
17   C  CA  . ILE   A 4   ? 0.1604 0.1667 0.1973 -0.0065 0.0061  0.0035  10  ILE   A CA  
18   C  C   . ILE   A 4   ? 0.1647 0.1716 0.2144 -0.0078 0.0099  0.0036  10  ILE   A C   
19   O  O   . ILE   A 4   ? 0.1623 0.1716 0.2162 -0.0073 0.0107  0.0039  10  ILE   A O   
20   C  CB  . ILE   A 4   ? 0.1591 0.1624 0.1848 -0.0041 0.0098  0.0042  10  ILE   A CB  
21   C  CG1 . ILE   A 4   ? 0.1608 0.1650 0.1766 -0.0028 0.0060  0.0039  10  ILE   A CG1 
22   C  CG2 . ILE   A 4   ? 0.1803 0.1777 0.2026 -0.0032 0.0161  0.0051  10  ILE   A CG2 
23   C  CD1 . ILE   A 4   ? 0.1673 0.1705 0.1750 -0.0002 0.0076  0.0034  10  ILE   A CD1 
24   N  N   . TYR   A 5   ? 0.1683 0.1730 0.2255 -0.0094 0.0127  0.0031  11  TYR   A N   
25   C  CA  . TYR   A 5   ? 0.1834 0.1888 0.2556 -0.0109 0.0176  0.0031  11  TYR   A CA  
26   C  C   . TYR   A 5   ? 0.1937 0.1924 0.2621 -0.0101 0.0272  0.0051  11  TYR   A C   
27   O  O   . TYR   A 5   ? 0.2115 0.2059 0.2790 -0.0109 0.0291  0.0053  11  TYR   A O   
28   C  CB  . TYR   A 5   ? 0.1817 0.1901 0.2692 -0.0135 0.0131  0.0006  11  TYR   A CB  
29   C  CG  . TYR   A 5   ? 0.1923 0.2066 0.2824 -0.0131 0.0037  -0.0010 11  TYR   A CG  
30   C  CD1 . TYR   A 5   ? 0.2031 0.2219 0.3034 -0.0127 0.0025  -0.0012 11  TYR   A CD1 
31   C  CD2 . TYR   A 5   ? 0.2121 0.2264 0.2927 -0.0122 -0.0034 -0.0021 11  TYR   A CD2 
32   C  CE1 . TYR   A 5   ? 0.2104 0.2334 0.3115 -0.0115 -0.0059 -0.0021 11  TYR   A CE1 
33   C  CE2 . TYR   A 5   ? 0.2252 0.2434 0.3054 -0.0108 -0.0112 -0.0028 11  TYR   A CE2 
34   C  CZ  . TYR   A 5   ? 0.2276 0.2499 0.3180 -0.0104 -0.0126 -0.0027 11  TYR   A CZ  
35   O  OH  . TYR   A 5   ? 0.2646 0.2895 0.3529 -0.0082 -0.0200 -0.0028 11  TYR   A OH  
36   N  N   . VAL   A 6   ? 0.1856 0.1824 0.2495 -0.0079 0.0331  0.0066  12  VAL   A N   
37   C  CA  . VAL   A 6   ? 0.2102 0.1992 0.2668 -0.0058 0.0428  0.0090  12  VAL   A CA  
38   C  C   . VAL   A 6   ? 0.2190 0.2078 0.2852 -0.0055 0.0505  0.0098  12  VAL   A C   
39   O  O   . VAL   A 6   ? 0.2265 0.2191 0.2937 -0.0045 0.0487  0.0089  12  VAL   A O   
40   C  CB  . VAL   A 6   ? 0.2447 0.2294 0.2801 -0.0016 0.0424  0.0096  12  VAL   A CB  
41   C  CG1 . VAL   A 6   ? 0.2435 0.2325 0.2750 0.0000  0.0381  0.0080  12  VAL   A CG1 
42   C  CG2 . VAL   A 6   ? 0.2759 0.2513 0.3010 0.0018  0.0522  0.0123  12  VAL   A CG2 
43   N  N   . GLY   A 7   ? 0.2216 0.2061 0.2968 -0.0066 0.0595  0.0116  13  GLY   A N   
44   C  CA  . GLY   A 7   ? 0.2197 0.2043 0.3063 -0.0064 0.0681  0.0125  13  GLY   A CA  
45   C  C   . GLY   A 7   ? 0.2216 0.2160 0.3268 -0.0090 0.0621  0.0097  13  GLY   A C   
46   O  O   . GLY   A 7   ? 0.2204 0.2202 0.3368 -0.0121 0.0541  0.0074  13  GLY   A O   
47   N  N   . ASN   A 8   ? 0.2241 0.2203 0.3304 -0.0070 0.0645  0.0095  14  ASN   A N   
48   C  CA  . ASN   A 8   ? 0.2213 0.2264 0.3438 -0.0086 0.0582  0.0071  14  ASN   A CA  
49   C  C   . ASN   A 8   ? 0.2097 0.2176 0.3204 -0.0069 0.0490  0.0059  14  ASN   A C   
50   O  O   . ASN   A 8   ? 0.2046 0.2168 0.3220 -0.0062 0.0467  0.0048  14  ASN   A O   
51   C  CB  . ASN   A 8   ? 0.2640 0.2701 0.3999 -0.0078 0.0667  0.0074  14  ASN   A CB  
52   C  CG  . ASN   A 8   ? 0.3581 0.3639 0.5134 -0.0105 0.0746  0.0080  14  ASN   A CG  
53   O  OD1 . ASN   A 8   ? 0.3862 0.3972 0.5584 -0.0142 0.0690  0.0059  14  ASN   A OD1 
54   N  ND2 . ASN   A 8   ? 0.3872 0.3866 0.5405 -0.0085 0.0879  0.0107  14  ASN   A ND2 
55   N  N   . TYR   A 9   ? 0.1987 0.2043 0.2935 -0.0064 0.0438  0.0060  15  TYR   A N   
56   C  CA  . TYR   A 9   ? 0.1855 0.1933 0.2700 -0.0051 0.0362  0.0051  15  TYR   A CA  
57   C  C   . TYR   A 9   ? 0.1699 0.1807 0.2532 -0.0069 0.0271  0.0045  15  TYR   A C   
58   O  O   . TYR   A 9   ? 0.1649 0.1737 0.2471 -0.0082 0.0270  0.0046  15  TYR   A O   
59   C  CB  . TYR   A 9   ? 0.2021 0.2041 0.2670 -0.0018 0.0389  0.0055  15  TYR   A CB  
60   C  CG  . TYR   A 9   ? 0.2034 0.2014 0.2648 0.0013  0.0469  0.0057  15  TYR   A CG  
61   C  CD1 . TYR   A 9   ? 0.2168 0.2181 0.2868 0.0018  0.0473  0.0045  15  TYR   A CD1 
62   C  CD2 . TYR   A 9   ? 0.2301 0.2203 0.2782 0.0045  0.0542  0.0070  15  TYR   A CD2 
63   C  CE1 . TYR   A 9   ? 0.2389 0.2360 0.3049 0.0052  0.0549  0.0043  15  TYR   A CE1 
64   C  CE2 . TYR   A 9   ? 0.2566 0.2421 0.2990 0.0083  0.0618  0.0070  15  TYR   A CE2 
65   C  CZ  . TYR   A 9   ? 0.2725 0.2616 0.3241 0.0085  0.0622  0.0055  15  TYR   A CZ  
66   O  OH  . TYR   A 9   ? 0.3010 0.2852 0.3466 0.0127  0.0698  0.0051  15  TYR   A OH  
67   N  N   . ARG   A 10  ? 0.1421 0.1568 0.2246 -0.0065 0.0202  0.0039  16  ARG   A N   
68   C  CA  . ARG   A 10  ? 0.1419 0.1585 0.2198 -0.0071 0.0122  0.0037  16  ARG   A CA  
69   C  C   . ARG   A 10  ? 0.1575 0.1731 0.2226 -0.0054 0.0106  0.0042  16  ARG   A C   
70   O  O   . ARG   A 10  ? 0.1646 0.1812 0.2316 -0.0044 0.0111  0.0041  16  ARG   A O   
71   C  CB  . ARG   A 10  ? 0.1604 0.1821 0.2503 -0.0077 0.0058  0.0030  16  ARG   A CB  
72   C  CG  . ARG   A 10  ? 0.1920 0.2148 0.2745 -0.0070 -0.0019 0.0034  16  ARG   A CG  
73   C  CD  . ARG   A 10  ? 0.1910 0.2178 0.2836 -0.0065 -0.0088 0.0026  16  ARG   A CD  
74   N  NE  . ARG   A 10  ? 0.2310 0.2580 0.3166 -0.0043 -0.0136 0.0044  16  ARG   A NE  
75   C  CZ  . ARG   A 10  ? 0.2672 0.2936 0.3449 -0.0029 -0.0196 0.0047  16  ARG   A CZ  
76   N  NH1 . ARG   A 10  ? 0.2480 0.2737 0.3229 -0.0037 -0.0220 0.0029  16  ARG   A NH1 
77   N  NH2 . ARG   A 10  ? 0.2693 0.2948 0.3407 -0.0006 -0.0224 0.0072  16  ARG   A NH2 
78   N  N   . VAL   A 11  ? 0.1472 0.1607 0.2007 -0.0051 0.0091  0.0043  17  VAL   A N   
79   C  CA  . VAL   A 11  ? 0.1483 0.1615 0.1924 -0.0036 0.0077  0.0042  17  VAL   A CA  
80   C  C   . VAL   A 11  ? 0.1587 0.1741 0.2010 -0.0041 0.0020  0.0050  17  VAL   A C   
81   O  O   . VAL   A 11  ? 0.1509 0.1658 0.1901 -0.0046 -0.0002 0.0050  17  VAL   A O   
82   C  CB  . VAL   A 11  ? 0.1609 0.1703 0.1931 -0.0021 0.0102  0.0035  17  VAL   A CB  
83   C  CG1 . VAL   A 11  ? 0.1559 0.1658 0.1817 -0.0006 0.0084  0.0024  17  VAL   A CG1 
84   C  CG2 . VAL   A 11  ? 0.1749 0.1801 0.2059 -0.0009 0.0167  0.0035  17  VAL   A CG2 
85   N  N   . VAL   A 12  ? 0.1408 0.1578 0.1844 -0.0037 0.0001  0.0057  18  VAL   A N   
86   C  CA  . VAL   A 12  ? 0.1369 0.1549 0.1777 -0.0034 -0.0041 0.0073  18  VAL   A CA  
87   C  C   . VAL   A 12  ? 0.1255 0.1433 0.1629 -0.0029 -0.0032 0.0077  18  VAL   A C   
88   O  O   . VAL   A 12  ? 0.1401 0.1576 0.1797 -0.0027 -0.0008 0.0063  18  VAL   A O   
89   C  CB  . VAL   A 12  ? 0.1557 0.1752 0.2038 -0.0030 -0.0074 0.0086  18  VAL   A CB  
90   C  CG1 . VAL   A 12  ? 0.1877 0.2083 0.2413 -0.0036 -0.0097 0.0074  18  VAL   A CG1 
91   C  CG2 . VAL   A 12  ? 0.1521 0.1723 0.2081 -0.0027 -0.0054 0.0088  18  VAL   A CG2 
92   N  N   . ASN   A 13  ? 0.1241 0.1418 0.1572 -0.0025 -0.0050 0.0095  19  ASN   A N   
93   C  CA  . ASN   A 13  ? 0.1190 0.1367 0.1526 -0.0023 -0.0035 0.0103  19  ASN   A CA  
94   C  C   . ASN   A 13  ? 0.1314 0.1488 0.1727 -0.0022 -0.0032 0.0116  19  ASN   A C   
95   O  O   . ASN   A 13  ? 0.1443 0.1614 0.1876 -0.0014 -0.0055 0.0136  19  ASN   A O   
96   C  CB  . ASN   A 13  ? 0.1317 0.1486 0.1597 -0.0016 -0.0042 0.0130  19  ASN   A CB  
97   C  CG  . ASN   A 13  ? 0.1649 0.1821 0.1857 -0.0014 -0.0042 0.0117  19  ASN   A CG  
98   O  OD1 . ASN   A 13  ? 0.1840 0.2004 0.1999 -0.0008 -0.0064 0.0117  19  ASN   A OD1 
99   N  ND2 . ASN   A 13  ? 0.1507 0.1688 0.1716 -0.0017 -0.0022 0.0103  19  ASN   A ND2 
100  N  N   . ARG   A 14  ? 0.1165 0.1338 0.1625 -0.0027 -0.0011 0.0099  20  ARG   A N   
101  C  CA  . ARG   A 14  ? 0.1076 0.1240 0.1615 -0.0024 -0.0006 0.0108  20  ARG   A CA  
102  C  C   . ARG   A 14  ? 0.1214 0.1360 0.1756 -0.0015 -0.0014 0.0155  20  ARG   A C   
103  O  O   . ARG   A 14  ? 0.1487 0.1625 0.2070 -0.0003 -0.0027 0.0174  20  ARG   A O   
104  C  CB  . ARG   A 14  ? 0.1154 0.1314 0.1741 -0.0029 0.0015  0.0077  20  ARG   A CB  
105  C  CG  . ARG   A 14  ? 0.1352 0.1498 0.2023 -0.0025 0.0024  0.0075  20  ARG   A CG  
106  C  CD  . ARG   A 14  ? 0.1372 0.1510 0.2091 -0.0031 0.0037  0.0040  20  ARG   A CD  
107  N  NE  . ARG   A 14  ? 0.1591 0.1710 0.2389 -0.0026 0.0047  0.0026  20  ARG   A NE  
108  C  CZ  . ARG   A 14  ? 0.1685 0.1781 0.2555 -0.0028 0.0056  0.0054  20  ARG   A CZ  
109  N  NH1 . ARG   A 14  ? 0.1477 0.1561 0.2335 -0.0032 0.0060  0.0103  20  ARG   A NH1 
110  N  NH2 . ARG   A 14  ? 0.1641 0.1716 0.2586 -0.0022 0.0065  0.0035  20  ARG   A NH2 
111  N  N   . HIS   A 15  ? 0.1258 0.1394 0.1750 -0.0015 -0.0003 0.0175  21  HIS   A N   
112  C  CA  . HIS   A 15  ? 0.1441 0.1545 0.1912 0.0002  0.0001  0.0226  21  HIS   A CA  
113  C  C   . HIS   A 15  ? 0.1667 0.1763 0.2070 0.0028  -0.0040 0.0250  21  HIS   A C   
114  O  O   . HIS   A 15  ? 0.1984 0.2044 0.2358 0.0054  -0.0046 0.0294  21  HIS   A O   
115  C  CB  . HIS   A 15  ? 0.1602 0.1694 0.2046 -0.0002 0.0038  0.0244  21  HIS   A CB  
116  C  CG  . HIS   A 15  ? 0.1630 0.1733 0.1979 0.0003  0.0030  0.0241  21  HIS   A CG  
117  N  ND1 . HIS   A 15  ? 0.1609 0.1746 0.1956 -0.0012 0.0028  0.0198  21  HIS   A ND1 
118  C  CD2 . HIS   A 15  ? 0.1878 0.1957 0.2129 0.0027  0.0027  0.0276  21  HIS   A CD2 
119  C  CE1 . HIS   A 15  ? 0.1731 0.1864 0.1990 -0.0001 0.0025  0.0208  21  HIS   A CE1 
120  N  NE2 . HIS   A 15  ? 0.1803 0.1902 0.1999 0.0022  0.0025  0.0253  21  HIS   A NE2 
121  N  N   . LEU   A 16  ? 0.1568 0.1690 0.1947 0.0023  -0.0070 0.0221  22  LEU   A N   
122  C  CA  . LEU   A 16  ? 0.1619 0.1739 0.1954 0.0045  -0.0121 0.0227  22  LEU   A CA  
123  C  C   . LEU   A 16  ? 0.1613 0.1759 0.2042 0.0043  -0.0149 0.0204  22  LEU   A C   
124  O  O   . LEU   A 16  ? 0.1634 0.1790 0.2062 0.0057  -0.0198 0.0196  22  LEU   A O   
125  C  CB  . LEU   A 16  ? 0.1713 0.1840 0.1966 0.0042  -0.0133 0.0209  22  LEU   A CB  
126  C  CG  . LEU   A 16  ? 0.1912 0.2016 0.2074 0.0050  -0.0105 0.0231  22  LEU   A CG  
127  C  CD1 . LEU   A 16  ? 0.1981 0.2091 0.2067 0.0050  -0.0120 0.0207  22  LEU   A CD1 
128  C  CD2 . LEU   A 16  ? 0.1852 0.1913 0.1947 0.0086  -0.0107 0.0279  22  LEU   A CD2 
129  N  N   . ALA   A 17  ? 0.1573 0.1731 0.2090 0.0026  -0.0117 0.0188  23  ALA   A N   
130  C  CA  . ALA   A 17  ? 0.1536 0.1720 0.2153 0.0024  -0.0129 0.0167  23  ALA   A CA  
131  C  C   . ALA   A 17  ? 0.1686 0.1867 0.2342 0.0053  -0.0175 0.0188  23  ALA   A C   
132  O  O   . ALA   A 17  ? 0.1776 0.1925 0.2401 0.0073  -0.0175 0.0224  23  ALA   A O   
133  C  CB  . ALA   A 17  ? 0.1515 0.1700 0.2199 0.0011  -0.0084 0.0150  23  ALA   A CB  
134  N  N   . THR   A 18  ? 0.1684 0.1896 0.2413 0.0057  -0.0211 0.0167  24  THR   A N   
135  C  CA  . THR   A 18  ? 0.1834 0.2051 0.2611 0.0092  -0.0269 0.0179  24  THR   A CA  
136  C  C   . THR   A 18  ? 0.1922 0.2153 0.2828 0.0096  -0.0250 0.0177  24  THR   A C   
137  O  O   . THR   A 18  ? 0.1856 0.2092 0.2812 0.0071  -0.0192 0.0161  24  THR   A O   
138  C  CB  . THR   A 18  ? 0.2072 0.2326 0.2898 0.0093  -0.0326 0.0144  24  THR   A CB  
139  O  OG1 . THR   A 18  ? 0.2127 0.2419 0.3082 0.0062  -0.0288 0.0111  24  THR   A OG1 
140  C  CG2 . THR   A 18  ? 0.2179 0.2420 0.2888 0.0090  -0.0347 0.0136  24  THR   A CG2 
141  N  N   . HIS   A 19  ? 0.1997 0.2232 0.2960 0.0133  -0.0303 0.0189  25  HIS   A N   
142  C  CA  . HIS   A 19  ? 0.2221 0.2473 0.3321 0.0140  -0.0289 0.0184  25  HIS   A CA  
143  C  C   . HIS   A 19  ? 0.1950 0.2254 0.3179 0.0110  -0.0258 0.0139  25  HIS   A C   
144  O  O   . HIS   A 19  ? 0.1945 0.2253 0.3246 0.0098  -0.0200 0.0129  25  HIS   A O   
145  C  CB  . HIS   A 19  ? 0.2686 0.2944 0.3831 0.0191  -0.0366 0.0197  25  HIS   A CB  
146  C  CG  . HIS   A 19  ? 0.3835 0.4027 0.4851 0.0233  -0.0388 0.0250  25  HIS   A CG  
147  N  ND1 . HIS   A 19  ? 0.4337 0.4475 0.5311 0.0228  -0.0327 0.0286  25  HIS   A ND1 
148  C  CD2 . HIS   A 19  ? 0.4220 0.4387 0.5144 0.0284  -0.0462 0.0271  25  HIS   A CD2 
149  C  CE1 . HIS   A 19  ? 0.4497 0.4577 0.5359 0.0272  -0.0353 0.0335  25  HIS   A CE1 
150  N  NE2 . HIS   A 19  ? 0.4491 0.4582 0.5305 0.0311  -0.0435 0.0330  25  HIS   A NE2 
151  N  N   . ASN   A 20  ? 0.1864 0.2203 0.3118 0.0098  -0.0291 0.0111  26  ASN   A N   
152  C  CA  . ASN   A 20  ? 0.1778 0.2158 0.3158 0.0069  -0.0250 0.0075  26  ASN   A CA  
153  C  C   . ASN   A 20  ? 0.1688 0.2043 0.3004 0.0037  -0.0163 0.0073  26  ASN   A C   
154  O  O   . ASN   A 20  ? 0.1707 0.2072 0.3109 0.0026  -0.0100 0.0057  26  ASN   A O   
155  C  CB  . ASN   A 20  ? 0.2125 0.2538 0.3552 0.0061  -0.0302 0.0046  26  ASN   A CB  
156  C  CG  . ASN   A 20  ? 0.2967 0.3426 0.4539 0.0090  -0.0380 0.0027  26  ASN   A CG  
157  O  OD1 . ASN   A 20  ? 0.2995 0.3480 0.4699 0.0103  -0.0366 0.0025  26  ASN   A OD1 
158  N  ND2 . ASN   A 20  ? 0.3185 0.3654 0.4732 0.0107  -0.0468 0.0009  26  ASN   A ND2 
159  N  N   . ASP   A 21  ? 0.1486 0.1805 0.2648 0.0029  -0.0156 0.0087  27  ASP   A N   
160  C  CA  . ASP   A 21  ? 0.1408 0.1702 0.2500 0.0008  -0.0086 0.0081  27  ASP   A CA  
161  C  C   . ASP   A 21  ? 0.1388 0.1665 0.2509 0.0016  -0.0041 0.0082  27  ASP   A C   
162  O  O   . ASP   A 21  ? 0.1481 0.1752 0.2621 0.0009  0.0018  0.0063  27  ASP   A O   
163  C  CB  . ASP   A 21  ? 0.1472 0.1735 0.2412 0.0004  -0.0096 0.0096  27  ASP   A CB  
164  C  CG  . ASP   A 21  ? 0.2017 0.2285 0.2907 -0.0006 -0.0121 0.0087  27  ASP   A CG  
165  O  OD1 . ASP   A 21  ? 0.2041 0.2322 0.2987 -0.0022 -0.0098 0.0066  27  ASP   A OD1 
166  O  OD2 . ASP   A 21  ? 0.2114 0.2368 0.2909 0.0003  -0.0161 0.0102  27  ASP   A OD2 
167  N  N   . TRP   A 22  ? 0.1380 0.1643 0.2501 0.0035  -0.0067 0.0104  28  TRP   A N   
168  C  CA  . TRP   A 22  ? 0.1434 0.1675 0.2589 0.0042  -0.0029 0.0100  28  TRP   A CA  
169  C  C   . TRP   A 22  ? 0.1572 0.1840 0.2868 0.0053  -0.0006 0.0083  28  TRP   A C   
170  O  O   . TRP   A 22  ? 0.1598 0.1850 0.2914 0.0054  0.0047  0.0064  28  TRP   A O   
171  C  CB  . TRP   A 22  ? 0.1468 0.1678 0.2596 0.0059  -0.0056 0.0132  28  TRP   A CB  
172  C  CG  . TRP   A 22  ? 0.1509 0.1687 0.2526 0.0046  -0.0044 0.0142  28  TRP   A CG  
173  C  CD1 . TRP   A 22  ? 0.1715 0.1880 0.2641 0.0048  -0.0071 0.0170  28  TRP   A CD1 
174  C  CD2 . TRP   A 22  ? 0.1536 0.1690 0.2534 0.0034  -0.0002 0.0122  28  TRP   A CD2 
175  N  NE1 . TRP   A 22  ? 0.1658 0.1800 0.2526 0.0033  -0.0042 0.0170  28  TRP   A NE1 
176  C  CE2 . TRP   A 22  ? 0.1637 0.1773 0.2552 0.0024  -0.0006 0.0137  28  TRP   A CE2 
177  C  CE3 . TRP   A 22  ? 0.1637 0.1784 0.2679 0.0033  0.0036  0.0086  28  TRP   A CE3 
178  C  CZ2 . TRP   A 22  ? 0.1617 0.1735 0.2518 0.0011  0.0021  0.0115  28  TRP   A CZ2 
179  C  CZ3 . TRP   A 22  ? 0.1721 0.1843 0.2726 0.0025  0.0057  0.0062  28  TRP   A CZ3 
180  C  CH2 . TRP   A 22  ? 0.1701 0.1814 0.2646 0.0012  0.0046  0.0074  28  TRP   A CH2 
181  N  N   . ALA   A 23  ? 0.1569 0.1878 0.2966 0.0061  -0.0046 0.0083  29  ALA   A N   
182  C  CA  . ALA   A 23  ? 0.1765 0.2107 0.3322 0.0071  -0.0021 0.0065  29  ALA   A CA  
183  C  C   . ALA   A 23  ? 0.1766 0.2118 0.3353 0.0050  0.0053  0.0039  29  ALA   A C   
184  O  O   . ALA   A 23  ? 0.1815 0.2182 0.3515 0.0057  0.0105  0.0024  29  ALA   A O   
185  C  CB  . ALA   A 23  ? 0.1904 0.2293 0.3574 0.0087  -0.0093 0.0066  29  ALA   A CB  
186  N  N   . ASN   A 24  ? 0.1626 0.1964 0.3109 0.0028  0.0065  0.0038  30  ASN   A N   
187  C  CA  . ASN   A 24  ? 0.1628 0.1957 0.3112 0.0013  0.0140  0.0023  30  ASN   A CA  
188  C  C   . ASN   A 24  ? 0.1642 0.1918 0.2948 0.0011  0.0177  0.0022  30  ASN   A C   
189  O  O   . ASN   A 24  ? 0.1487 0.1743 0.2726 0.0000  0.0213  0.0020  30  ASN   A O   
190  C  CB  . ASN   A 24  ? 0.1802 0.2160 0.3339 -0.0008 0.0116  0.0019  30  ASN   A CB  
191  C  CG  . ASN   A 24  ? 0.2075 0.2493 0.3809 -0.0004 0.0077  0.0008  30  ASN   A CG  
192  O  OD1 . ASN   A 24  ? 0.2186 0.2627 0.4067 -0.0005 0.0134  -0.0005 30  ASN   A OD1 
193  N  ND2 . ASN   A 24  ? 0.1994 0.2436 0.3735 0.0005  -0.0020 0.0010  30  ASN   A ND2 
194  N  N   . LEU   A 25  ? 0.1670 0.1920 0.2911 0.0024  0.0165  0.0023  31  LEU   A N   
195  C  CA  . LEU   A 25  ? 0.1691 0.1899 0.2787 0.0026  0.0182  0.0013  31  LEU   A CA  
196  C  C   . LEU   A 25  ? 0.1744 0.1918 0.2784 0.0038  0.0256  -0.0008 31  LEU   A C   
197  O  O   . LEU   A 25  ? 0.1833 0.2000 0.2936 0.0055  0.0306  -0.0020 31  LEU   A O   
198  C  CB  . LEU   A 25  ? 0.1701 0.1891 0.2789 0.0036  0.0159  0.0010  31  LEU   A CB  
199  C  CG  . LEU   A 25  ? 0.1788 0.1943 0.2759 0.0038  0.0165  -0.0011 31  LEU   A CG  
200  C  CD1 . LEU   A 25  ? 0.1910 0.2068 0.2789 0.0022  0.0131  0.0003  31  LEU   A CD1 
201  C  CD2 . LEU   A 25  ? 0.1789 0.1924 0.2792 0.0046  0.0151  -0.0020 31  LEU   A CD2 
202  N  N   . VAL   A 26  ? 0.1664 0.1811 0.2575 0.0036  0.0266  -0.0012 32  VAL   A N   
203  C  CA  . VAL   A 26  ? 0.1772 0.1871 0.2586 0.0060  0.0332  -0.0028 32  VAL   A CA  
204  C  C   . VAL   A 26  ? 0.1930 0.1997 0.2621 0.0078  0.0307  -0.0056 32  VAL   A C   
205  O  O   . VAL   A 26  ? 0.2230 0.2260 0.2869 0.0108  0.0339  -0.0085 32  VAL   A O   
206  C  CB  . VAL   A 26  ? 0.1992 0.2075 0.2749 0.0051  0.0359  -0.0012 32  VAL   A CB  
207  C  CG1 . VAL   A 26  ? 0.2200 0.2218 0.2810 0.0086  0.0420  -0.0024 32  VAL   A CG1 
208  C  CG2 . VAL   A 26  ? 0.2038 0.2150 0.2943 0.0033  0.0392  0.0005  32  VAL   A CG2 
209  N  N   . TRP   A 27  ? 0.1720 0.1802 0.2370 0.0061  0.0248  -0.0051 33  TRP   A N   
210  C  CA  . TRP   A 27  ? 0.1774 0.1836 0.2337 0.0073  0.0219  -0.0081 33  TRP   A CA  
211  C  C   . TRP   A 27  ? 0.1602 0.1695 0.2186 0.0047  0.0161  -0.0065 33  TRP   A C   
212  O  O   . TRP   A 27  ? 0.1577 0.1692 0.2168 0.0028  0.0146  -0.0035 33  TRP   A O   
213  C  CB  . TRP   A 27  ? 0.1958 0.1982 0.2376 0.0099  0.0239  -0.0097 33  TRP   A CB  
214  C  CG  . TRP   A 27  ? 0.2185 0.2198 0.2517 0.0113  0.0195  -0.0132 33  TRP   A CG  
215  C  CD1 . TRP   A 27  ? 0.2437 0.2426 0.2732 0.0142  0.0183  -0.0182 33  TRP   A CD1 
216  C  CD2 . TRP   A 27  ? 0.2184 0.2215 0.2472 0.0101  0.0155  -0.0127 33  TRP   A CD2 
217  N  NE1 . TRP   A 27  ? 0.2542 0.2539 0.2790 0.0146  0.0133  -0.0210 33  TRP   A NE1 
218  C  CE2 . TRP   A 27  ? 0.2342 0.2366 0.2586 0.0121  0.0118  -0.0174 33  TRP   A CE2 
219  C  CE3 . TRP   A 27  ? 0.2143 0.2195 0.2432 0.0076  0.0144  -0.0091 33  TRP   A CE3 
220  C  CZ2 . TRP   A 27  ? 0.2319 0.2360 0.2523 0.0119  0.0077  -0.0184 33  TRP   A CZ2 
221  C  CZ3 . TRP   A 27  ? 0.2217 0.2281 0.2455 0.0075  0.0106  -0.0098 33  TRP   A CZ3 
222  C  CH2 . TRP   A 27  ? 0.2225 0.2285 0.2426 0.0096  0.0076  -0.0143 33  TRP   A CH2 
223  N  N   . GLU   A 28  ? 0.1542 0.1633 0.2139 0.0047  0.0134  -0.0087 34  GLU   A N   
224  C  CA  . GLU   A 28  ? 0.1529 0.1642 0.2140 0.0025  0.0094  -0.0070 34  GLU   A CA  
225  C  C   . GLU   A 28  ? 0.1531 0.1635 0.2124 0.0031  0.0075  -0.0112 34  GLU   A C   
226  O  O   . GLU   A 28  ? 0.1602 0.1684 0.2203 0.0050  0.0081  -0.0155 34  GLU   A O   
227  C  CB  . GLU   A 28  ? 0.1708 0.1835 0.2415 0.0010  0.0081  -0.0032 34  GLU   A CB  
228  C  CG  . GLU   A 28  ? 0.1917 0.2029 0.2711 0.0018  0.0093  -0.0044 34  GLU   A CG  
229  C  CD  . GLU   A 28  ? 0.2121 0.2215 0.2947 0.0016  0.0083  -0.0073 34  GLU   A CD  
230  O  OE1 . GLU   A 28  ? 0.2658 0.2730 0.3524 0.0029  0.0096  -0.0107 34  GLU   A OE1 
231  O  OE2 . GLU   A 28  ? 0.1861 0.1962 0.2679 0.0001  0.0066  -0.0066 34  GLU   A OE2 
232  N  N   . ASP   A 29  ? 0.1457 0.1579 0.2033 0.0018  0.0051  -0.0106 35  ASP   A N   
233  C  CA  . ASP   A 29  ? 0.1457 0.1581 0.2047 0.0021  0.0028  -0.0151 35  ASP   A CA  
234  C  C   . ASP   A 29  ? 0.1474 0.1621 0.2119 -0.0006 0.0018  -0.0120 35  ASP   A C   
235  O  O   . ASP   A 29  ? 0.1465 0.1628 0.2057 -0.0010 0.0013  -0.0099 35  ASP   A O   
236  C  CB  . ASP   A 29  ? 0.1846 0.1962 0.2329 0.0049  0.0014  -0.0193 35  ASP   A CB  
237  C  CG  . ASP   A 29  ? 0.2554 0.2677 0.3065 0.0059  -0.0022 -0.0255 35  ASP   A CG  
238  O  OD1 . ASP   A 29  ? 0.2520 0.2663 0.3142 0.0033  -0.0031 -0.0256 35  ASP   A OD1 
239  O  OD2 . ASP   A 29  ? 0.2720 0.2826 0.3141 0.0096  -0.0041 -0.0303 35  ASP   A OD2 
240  N  N   . SER   A 30  ? 0.1469 0.1609 0.2219 -0.0021 0.0023  -0.0117 36  SER   A N   
241  C  CA  A SER   A 30  ? 0.1569 0.1718 0.2377 -0.0042 0.0031  -0.0081 36  SER   A CA  
242  C  CA  B SER   A 30  ? 0.1536 0.1685 0.2340 -0.0042 0.0031  -0.0080 36  SER   A CA  
243  C  C   . SER   A 30  ? 0.1527 0.1703 0.2333 -0.0046 0.0016  -0.0114 36  SER   A C   
244  O  O   . SER   A 30  ? 0.1654 0.1845 0.2452 -0.0056 0.0026  -0.0079 36  SER   A O   
245  C  CB  A SER   A 30  ? 0.1779 0.1904 0.2706 -0.0054 0.0047  -0.0078 36  SER   A CB  
246  C  CB  B SER   A 30  ? 0.1649 0.1774 0.2571 -0.0055 0.0048  -0.0070 36  SER   A CB  
247  O  OG  A SER   A 30  ? 0.2080 0.2203 0.3061 -0.0072 0.0067  -0.0038 36  SER   A OG  
248  O  OG  B SER   A 30  ? 0.1742 0.1865 0.2742 -0.0056 0.0037  -0.0135 36  SER   A OG  
249  N  N   . SER   A 31  ? 0.1476 0.1659 0.2289 -0.0031 -0.0010 -0.0184 37  SER   A N   
250  C  CA  . SER   A 31  ? 0.1669 0.1883 0.2495 -0.0029 -0.0035 -0.0224 37  SER   A CA  
251  C  C   . SER   A 31  ? 0.1651 0.1881 0.2357 -0.0016 -0.0042 -0.0204 37  SER   A C   
252  O  O   . SER   A 31  ? 0.1830 0.2089 0.2554 -0.0017 -0.0054 -0.0219 37  SER   A O   
253  C  CB  . SER   A 31  ? 0.2018 0.2233 0.2869 -0.0007 -0.0076 -0.0312 37  SER   A CB  
254  O  OG  . SER   A 31  ? 0.2644 0.2842 0.3352 0.0032  -0.0096 -0.0338 37  SER   A OG  
255  N  N   . ARG   A 32  ? 0.1465 0.1674 0.2064 -0.0004 -0.0031 -0.0172 38  ARG   A N   
256  C  CA  . ARG   A 32  ? 0.1424 0.1637 0.1913 0.0008  -0.0035 -0.0153 38  ARG   A CA  
257  C  C   . ARG   A 32  ? 0.1446 0.1659 0.1919 -0.0011 -0.0013 -0.0087 38  ARG   A C   
258  O  O   . ARG   A 32  ? 0.1565 0.1780 0.1960 -0.0005 -0.0015 -0.0071 38  ARG   A O   
259  C  CB  . ARG   A 32  ? 0.1536 0.1718 0.1916 0.0038  -0.0035 -0.0169 38  ARG   A CB  
260  C  CG  . ARG   A 32  ? 0.1669 0.1842 0.2019 0.0072  -0.0064 -0.0236 38  ARG   A CG  
261  C  CD  . ARG   A 32  ? 0.1889 0.2016 0.2110 0.0109  -0.0049 -0.0242 38  ARG   A CD  
262  N  NE  . ARG   A 32  ? 0.1792 0.1909 0.1914 0.0120  -0.0040 -0.0212 38  ARG   A NE  
263  C  CZ  . ARG   A 32  ? 0.2042 0.2114 0.2034 0.0162  -0.0032 -0.0221 38  ARG   A CZ  
264  N  NH1 . ARG   A 32  ? 0.2127 0.2163 0.2058 0.0202  -0.0035 -0.0261 38  ARG   A NH1 
265  N  NH2 . ARG   A 32  ? 0.1870 0.1927 0.1785 0.0168  -0.0021 -0.0190 38  ARG   A NH2 
266  N  N   . ASP   A 33  ? 0.1439 0.1643 0.1977 -0.0028 0.0004  -0.0052 39  ASP   A N   
267  C  CA  . ASP   A 33  ? 0.1314 0.1511 0.1824 -0.0035 0.0014  0.0004  39  ASP   A CA  
268  C  C   . ASP   A 33  ? 0.1238 0.1425 0.1679 -0.0026 0.0008  0.0011  39  ASP   A C   
269  O  O   . ASP   A 33  ? 0.1391 0.1578 0.1785 -0.0027 0.0003  0.0040  39  ASP   A O   
270  C  CB  . ASP   A 33  ? 0.1487 0.1695 0.1970 -0.0040 0.0020  0.0031  39  ASP   A CB  
271  C  CG  . ASP   A 33  ? 0.1426 0.1617 0.1863 -0.0037 0.0023  0.0084  39  ASP   A CG  
272  O  OD1 . ASP   A 33  ? 0.1429 0.1602 0.1901 -0.0037 0.0026  0.0110  39  ASP   A OD1 
273  O  OD2 . ASP   A 33  ? 0.1438 0.1632 0.1803 -0.0031 0.0018  0.0096  39  ASP   A OD2 
274  N  N   . LEU   A 34  ? 0.1238 0.1414 0.1678 -0.0016 0.0013  -0.0017 40  LEU   A N   
275  C  CA  . LEU   A 34  ? 0.1152 0.1317 0.1553 -0.0010 0.0022  -0.0007 40  LEU   A CA  
276  C  C   . LEU   A 34  ? 0.1128 0.1287 0.1596 -0.0011 0.0035  0.0000  40  LEU   A C   
277  O  O   . LEU   A 34  ? 0.1303 0.1454 0.1817 -0.0006 0.0042  -0.0021 40  LEU   A O   
278  C  CB  . LEU   A 34  ? 0.1167 0.1314 0.1490 0.0010  0.0032  -0.0038 40  LEU   A CB  
279  C  CG  . LEU   A 34  ? 0.1415 0.1564 0.1661 0.0018  0.0019  -0.0044 40  LEU   A CG  
280  C  CD1 . LEU   A 34  ? 0.1648 0.1765 0.1804 0.0049  0.0029  -0.0070 40  LEU   A CD1 
281  C  CD2 . LEU   A 34  ? 0.1443 0.1594 0.1666 0.0005  0.0016  -0.0010 40  LEU   A CD2 
282  N  N   . LEU   A 35  ? 0.1066 0.1226 0.1543 -0.0014 0.0039  0.0020  41  LEU   A N   
283  C  CA  . LEU   A 35  ? 0.1200 0.1361 0.1752 -0.0012 0.0055  0.0023  41  LEU   A CA  
284  C  C   . LEU   A 35  ? 0.1333 0.1492 0.1879 -0.0013 0.0074  0.0026  41  LEU   A C   
285  O  O   . LEU   A 35  ? 0.1395 0.1559 0.1911 -0.0022 0.0057  0.0038  41  LEU   A O   
286  C  CB  . LEU   A 35  ? 0.1223 0.1397 0.1848 -0.0017 0.0029  0.0052  41  LEU   A CB  
287  C  CG  . LEU   A 35  ? 0.1361 0.1542 0.2084 -0.0010 0.0039  0.0054  41  LEU   A CG  
288  C  CD1 . LEU   A 35  ? 0.1656 0.1833 0.2439 -0.0004 0.0021  0.0074  41  LEU   A CD1 
289  C  CD2 . LEU   A 35  ? 0.1361 0.1563 0.2125 -0.0014 0.0026  0.0064  41  LEU   A CD2 
290  N  N   . VAL   A 36  ? 0.1310 0.1455 0.1887 -0.0003 0.0116  0.0013  42  VAL   A N   
291  C  CA  . VAL   A 36  ? 0.1370 0.1509 0.1970 -0.0006 0.0151  0.0019  42  VAL   A CA  
292  C  C   . VAL   A 36  ? 0.1436 0.1597 0.2169 -0.0009 0.0165  0.0023  42  VAL   A C   
293  O  O   . VAL   A 36  ? 0.1507 0.1663 0.2272 0.0005  0.0183  0.0012  42  VAL   A O   
294  C  CB  . VAL   A 36  ? 0.1625 0.1718 0.2130 0.0016  0.0206  0.0005  42  VAL   A CB  
295  C  CG1 . VAL   A 36  ? 0.1767 0.1843 0.2310 0.0012  0.0261  0.0018  42  VAL   A CG1 
296  C  CG2 . VAL   A 36  ? 0.1612 0.1688 0.1993 0.0024  0.0182  -0.0002 42  VAL   A CG2 
297  N  N   . SER   A 37  ? 0.1299 0.1485 0.2118 -0.0024 0.0153  0.0033  43  SER   A N   
298  C  CA  . SER   A 37  ? 0.1422 0.1638 0.2392 -0.0025 0.0161  0.0032  43  SER   A CA  
299  C  C   . SER   A 37  ? 0.1698 0.1910 0.2737 -0.0035 0.0218  0.0030  43  SER   A C   
300  O  O   . SER   A 37  ? 0.1721 0.1905 0.2688 -0.0043 0.0236  0.0033  43  SER   A O   
301  C  CB  . SER   A 37  ? 0.1517 0.1773 0.2560 -0.0030 0.0084  0.0041  43  SER   A CB  
302  O  OG  . SER   A 37  ? 0.1882 0.2146 0.2902 -0.0043 0.0045  0.0042  43  SER   A OG  
303  N  N   . SER   A 38  ? 0.1643 0.1879 0.2830 -0.0034 0.0253  0.0025  44  SER   A N   
304  C  CA  . SER   A 38  ? 0.1790 0.2023 0.3075 -0.0046 0.0319  0.0024  44  SER   A CA  
305  C  C   . SER   A 38  ? 0.1881 0.2163 0.3312 -0.0070 0.0263  0.0016  44  SER   A C   
306  O  O   . SER   A 38  ? 0.1949 0.2275 0.3436 -0.0068 0.0180  0.0009  44  SER   A O   
307  C  CB  . SER   A 38  ? 0.2087 0.2320 0.3470 -0.0031 0.0396  0.0021  44  SER   A CB  
308  O  OG  . SER   A 38  ? 0.2356 0.2643 0.3864 -0.0026 0.0343  0.0012  44  SER   A OG  
309  N  N   . THR   A 39  ? 0.1956 0.2226 0.3448 -0.0090 0.0308  0.0014  45  THR   A N   
310  C  CA  . THR   A 39  ? 0.2129 0.2444 0.3776 -0.0115 0.0253  -0.0006 45  THR   A CA  
311  C  C   . THR   A 39  ? 0.2563 0.2894 0.4419 -0.0131 0.0334  -0.0013 45  THR   A C   
312  O  O   . THR   A 39  ? 0.2731 0.3014 0.4559 -0.0125 0.0447  0.0006  45  THR   A O   
313  C  CB  . THR   A 39  ? 0.2269 0.2551 0.3810 -0.0129 0.0224  -0.0006 45  THR   A CB  
314  O  OG1 . THR   A 39  ? 0.2401 0.2621 0.3891 -0.0134 0.0326  0.0011  45  THR   A OG1 
315  C  CG2 . THR   A 39  ? 0.2351 0.2615 0.3692 -0.0113 0.0160  0.0003  45  THR   A CG2 
316  N  N   . THR   A 40  ? 0.2728 0.3121 0.4791 -0.0149 0.0277  -0.0043 46  THR   A N   
317  C  CA  . THR   A 40  ? 0.2989 0.3405 0.5291 -0.0171 0.0351  -0.0056 46  THR   A CA  
318  C  C   . THR   A 40  ? 0.3171 0.3542 0.5481 -0.0202 0.0394  -0.0055 46  THR   A C   
319  O  O   . THR   A 40  ? 0.3295 0.3632 0.5690 -0.0215 0.0515  -0.0039 46  THR   A O   
320  C  CB  . THR   A 40  ? 0.3248 0.3759 0.5795 -0.0174 0.0263  -0.0096 46  THR   A CB  
321  O  OG1 . THR   A 40  ? 0.3449 0.3982 0.5954 -0.0175 0.0129  -0.0123 46  THR   A OG1 
322  C  CG2 . THR   A 40  ? 0.3352 0.3899 0.5923 -0.0143 0.0247  -0.0092 46  THR   A CG2 
323  N  N   . ALA   A 41  ? 0.3168 0.3532 0.5382 -0.0209 0.0302  -0.0070 47  ALA   A N   
324  C  CA  . ALA   A 41  ? 0.3271 0.3587 0.5485 -0.0236 0.0329  -0.0073 47  ALA   A CA  
325  C  C   . ALA   A 41  ? 0.3430 0.3653 0.5397 -0.0222 0.0408  -0.0029 47  ALA   A C   
326  O  O   . ALA   A 41  ? 0.3421 0.3625 0.5186 -0.0193 0.0390  -0.0009 47  ALA   A O   
327  C  CB  . ALA   A 41  ? 0.3278 0.3623 0.5486 -0.0242 0.0194  -0.0113 47  ALA   A CB  
328  N  N   . GLN   A 42  ? 0.3495 0.3656 0.5488 -0.0240 0.0494  -0.0015 48  GLN   A N   
329  C  CA  . GLN   A 42  ? 0.3709 0.3774 0.5475 -0.0220 0.0568  0.0027  48  GLN   A CA  
330  C  C   . GLN   A 42  ? 0.3717 0.3765 0.5321 -0.0217 0.0476  0.0016  48  GLN   A C   
331  O  O   . GLN   A 42  ? 0.3648 0.3717 0.5347 -0.0242 0.0408  -0.0017 48  GLN   A O   
332  C  CB  . GLN   A 42  ? 0.4105 0.4100 0.5966 -0.0237 0.0702  0.0051  48  GLN   A CB  
333  C  CG  . GLN   A 42  ? 0.4919 0.4802 0.6547 -0.0213 0.0769  0.0093  48  GLN   A CG  
334  C  CD  . GLN   A 42  ? 0.5907 0.5734 0.7333 -0.0164 0.0846  0.0133  48  GLN   A CD  
335  O  OE1 . GLN   A 42  ? 0.6210 0.6065 0.7698 -0.0152 0.0890  0.0136  48  GLN   A OE1 
336  N  NE2 . GLN   A 42  ? 0.6158 0.5905 0.7340 -0.0131 0.0859  0.0159  48  GLN   A NE2 
337  N  N   . GLY   A 43  ? 0.3795 0.3805 0.5160 -0.0184 0.0471  0.0040  49  GLY   A N   
338  C  CA  . GLY   A 43  ? 0.4010 0.3997 0.5208 -0.0176 0.0404  0.0036  49  GLY   A CA  
339  C  C   . GLY   A 43  ? 0.4208 0.4097 0.5278 -0.0163 0.0490  0.0069  49  GLY   A C   
340  O  O   . GLY   A 43  ? 0.4372 0.4206 0.5388 -0.0141 0.0591  0.0101  49  GLY   A O   
341  N  N   . CYS   A 44  ? 0.4091 0.3949 0.5098 -0.0168 0.0452  0.0061  50  CYS   A N   
342  C  CA  . CYS   A 44  ? 0.4143 0.3902 0.5019 -0.0149 0.0527  0.0094  50  CYS   A CA  
343  C  C   . CYS   A 44  ? 0.3978 0.3717 0.4667 -0.0126 0.0464  0.0092  50  CYS   A C   
344  O  O   . CYS   A 44  ? 0.4120 0.3781 0.4729 -0.0115 0.0503  0.0109  50  CYS   A O   
345  C  CB  . CYS   A 44  ? 0.4307 0.4015 0.5336 -0.0180 0.0598  0.0099  50  CYS   A CB  
346  S  SG  . CYS   A 44  ? 0.5130 0.4898 0.6352 -0.0227 0.0493  0.0039  50  CYS   A SG  
347  N  N   . ASP   A 45  ? 0.3639 0.3440 0.4243 -0.0112 0.0380  0.0076  51  ASP   A N   
348  C  CA  . ASP   A 45  ? 0.3316 0.3101 0.3734 -0.0083 0.0336  0.0078  51  ASP   A CA  
349  C  C   . ASP   A 45  ? 0.3201 0.2916 0.3479 -0.0041 0.0416  0.0111  51  ASP   A C   
350  O  O   . ASP   A 45  ? 0.3443 0.3147 0.3764 -0.0036 0.0482  0.0126  51  ASP   A O   
351  C  CB  . ASP   A 45  ? 0.3149 0.3009 0.3525 -0.0076 0.0252  0.0060  51  ASP   A CB  
352  C  CG  . ASP   A 45  ? 0.3381 0.3288 0.3771 -0.0089 0.0161  0.0033  51  ASP   A CG  
353  O  OD1 . ASP   A 45  ? 0.3208 0.3081 0.3532 -0.0085 0.0144  0.0027  51  ASP   A OD1 
354  O  OD2 . ASP   A 45  ? 0.2947 0.2916 0.3396 -0.0097 0.0108  0.0020  51  ASP   A OD2 
355  N  N   . THR   A 46  ? 0.2867 0.2529 0.2989 -0.0008 0.0417  0.0122  52  THR   A N   
356  C  CA  . THR   A 46  ? 0.3003 0.2595 0.2975 0.0042  0.0477  0.0149  52  THR   A CA  
357  C  C   . THR   A 46  ? 0.2694 0.2316 0.2526 0.0078  0.0410  0.0132  52  THR   A C   
358  O  O   . THR   A 46  ? 0.2623 0.2280 0.2438 0.0071  0.0343  0.0114  52  THR   A O   
359  C  CB  . THR   A 46  ? 0.3625 0.3111 0.3550 0.0058  0.0555  0.0182  52  THR   A CB  
360  O  OG1 . THR   A 46  ? 0.3979 0.3455 0.3866 0.0056  0.0504  0.0172  52  THR   A OG1 
361  C  CG2 . THR   A 46  ? 0.3617 0.3080 0.3718 0.0017  0.0630  0.0196  52  THR   A CG2 
362  N  N   . ILE   A 47  ? 0.2402 0.2013 0.2146 0.0116  0.0429  0.0133  53  ILE   A N   
363  C  CA  . ILE   A 47  ? 0.2240 0.1886 0.1884 0.0147  0.0363  0.0108  53  ILE   A CA  
364  C  C   . ILE   A 47  ? 0.2351 0.1924 0.1822 0.0207  0.0370  0.0116  53  ILE   A C   
365  O  O   . ILE   A 47  ? 0.2516 0.1999 0.1894 0.0246  0.0442  0.0144  53  ILE   A O   
366  C  CB  . ILE   A 47  ? 0.2134 0.1809 0.1783 0.0159  0.0366  0.0092  53  ILE   A CB  
367  C  CG1 . ILE   A 47  ? 0.2124 0.1864 0.1947 0.0108  0.0365  0.0088  53  ILE   A CG1 
368  C  CG2 . ILE   A 47  ? 0.2084 0.1802 0.1664 0.0185  0.0292  0.0058  53  ILE   A CG2 
369  C  CD1 . ILE   A 47  ? 0.2199 0.2018 0.2111 0.0068  0.0287  0.0071  53  ILE   A CD1 
370  N  N   . ALA   A 48  ? 0.2185 0.1793 0.1610 0.0219  0.0299  0.0094  54  ALA   A N   
371  C  CA  . ALA   A 48  ? 0.2176 0.1727 0.1444 0.0282  0.0287  0.0094  54  ALA   A CA  
372  C  C   . ALA   A 48  ? 0.2277 0.1810 0.1436 0.0338  0.0282  0.0076  54  ALA   A C   
373  O  O   . ALA   A 48  ? 0.2291 0.1891 0.1510 0.0323  0.0248  0.0046  54  ALA   A O   
374  C  CB  . ALA   A 48  ? 0.2098 0.1709 0.1376 0.0279  0.0209  0.0067  54  ALA   A CB  
375  N  N   . ARG   A 49  ? 0.2411 0.1847 0.1401 0.0409  0.0312  0.0092  55  ARG   A N   
376  C  CA  . ARG   A 49  ? 0.2524 0.1935 0.1382 0.0477  0.0293  0.0066  55  ARG   A CA  
377  C  C   . ARG   A 49  ? 0.2819 0.2194 0.1539 0.0543  0.0241  0.0055  55  ARG   A C   
378  O  O   . ARG   A 49  ? 0.3006 0.2273 0.1584 0.0598  0.0288  0.0092  55  ARG   A O   
379  C  CB  . ARG   A 49  ? 0.2631 0.1940 0.1394 0.0512  0.0392  0.0103  55  ARG   A CB  
380  C  CG  . ARG   A 49  ? 0.2643 0.1987 0.1563 0.0446  0.0451  0.0117  55  ARG   A CG  
381  C  CD  . ARG   A 49  ? 0.2858 0.2305 0.1886 0.0414  0.0392  0.0069  55  ARG   A CD  
382  N  NE  . ARG   A 49  ? 0.2729 0.2204 0.1905 0.0359  0.0448  0.0085  55  ARG   A NE  
383  C  CZ  . ARG   A 49  ? 0.2984 0.2546 0.2294 0.0315  0.0410  0.0057  55  ARG   A CZ  
384  N  NH1 . ARG   A 49  ? 0.2899 0.2527 0.2220 0.0316  0.0324  0.0013  55  ARG   A NH1 
385  N  NH2 . ARG   A 49  ? 0.2976 0.2559 0.2421 0.0273  0.0461  0.0074  55  ARG   A NH2 
386  N  N   . CYS   A 50  ? 0.2727 0.2194 0.1506 0.0537  0.0148  0.0007  56  CYS   A N   
387  C  CA  . CYS   A 50  ? 0.2790 0.2248 0.1489 0.0589  0.0091  -0.0009 56  CYS   A CA  
388  C  C   . CYS   A 50  ? 0.2912 0.2479 0.1693 0.0586  -0.0007 -0.0074 56  CYS   A C   
389  O  O   . CYS   A 50  ? 0.3024 0.2670 0.1930 0.0536  -0.0024 -0.0101 56  CYS   A O   
390  C  CB  . CYS   A 50  ? 0.2744 0.2192 0.1500 0.0549  0.0117  0.0027  56  CYS   A CB  
391  S  SG  . CYS   A 50  ? 0.2623 0.2198 0.1600 0.0449  0.0087  0.0010  56  CYS   A SG  
392  N  N   . ASP   A 51  ? 0.3051 0.2627 0.1786 0.0634  -0.0067 -0.0097 57  ASP   A N   
393  C  CA  . ASP   A 51  ? 0.3126 0.2813 0.1974 0.0626  -0.0153 -0.0159 57  ASP   A CA  
394  C  C   . ASP   A 51  ? 0.3137 0.2875 0.2081 0.0592  -0.0166 -0.0151 57  ASP   A C   
395  O  O   . ASP   A 51  ? 0.3201 0.3005 0.2198 0.0613  -0.0232 -0.0195 57  ASP   A O   
396  C  CB  . ASP   A 51  ? 0.3562 0.3237 0.2303 0.0718  -0.0231 -0.0214 57  ASP   A CB  
397  C  CG  . ASP   A 51  ? 0.4398 0.3986 0.2973 0.0802  -0.0241 -0.0194 57  ASP   A CG  
398  O  OD1 . ASP   A 51  ? 0.4434 0.3959 0.2972 0.0787  -0.0177 -0.0133 57  ASP   A OD1 
399  O  OD2 . ASP   A 51  ? 0.5108 0.4689 0.3595 0.0884  -0.0317 -0.0242 57  ASP   A OD2 
400  N  N   . CYS   A 52  ? 0.2912 0.2625 0.1889 0.0540  -0.0105 -0.0101 58  CYS   A N   
401  C  CA  . CYS   A 52  ? 0.2665 0.2422 0.1723 0.0510  -0.0114 -0.0097 58  CYS   A CA  
402  C  C   . CYS   A 52  ? 0.2557 0.2433 0.1770 0.0468  -0.0156 -0.0136 58  CYS   A C   
403  O  O   . CYS   A 52  ? 0.2518 0.2439 0.1810 0.0429  -0.0154 -0.0147 58  CYS   A O   
404  C  CB  . CYS   A 52  ? 0.2646 0.2363 0.1730 0.0455  -0.0049 -0.0048 58  CYS   A CB  
405  S  SG  . CYS   A 52  ? 0.2873 0.2446 0.1810 0.0498  0.0011  0.0004  58  CYS   A SG  
406  N  N   . GLN   A 53  ? 0.2321 0.2243 0.1581 0.0479  -0.0188 -0.0155 59  GLN   A N   
407  C  CA  . GLN   A 53  ? 0.2065 0.2092 0.1479 0.0440  -0.0210 -0.0183 59  GLN   A CA  
408  C  C   . GLN   A 53  ? 0.1917 0.1953 0.1368 0.0410  -0.0182 -0.0159 59  GLN   A C   
409  O  O   . GLN   A 53  ? 0.2006 0.2118 0.1563 0.0395  -0.0194 -0.0179 59  GLN   A O   
410  C  CB  . GLN   A 53  ? 0.2222 0.2313 0.1690 0.0485  -0.0277 -0.0242 59  GLN   A CB  
411  C  CG  . GLN   A 53  ? 0.2861 0.2971 0.2344 0.0498  -0.0313 -0.0281 59  GLN   A CG  
412  C  CD  . GLN   A 53  ? 0.3439 0.3623 0.3009 0.0538  -0.0388 -0.0350 59  GLN   A CD  
413  O  OE1 . GLN   A 53  ? 0.3446 0.3602 0.2925 0.0612  -0.0445 -0.0386 59  GLN   A OE1 
414  N  NE2 . GLN   A 53  ? 0.3127 0.3406 0.2879 0.0495  -0.0389 -0.0371 59  GLN   A NE2 
415  N  N   . THR   A 54  ? 0.1697 0.1654 0.1066 0.0404  -0.0143 -0.0118 60  THR   A N   
416  C  CA  . THR   A 54  ? 0.1822 0.1777 0.1217 0.0373  -0.0117 -0.0099 60  THR   A CA  
417  C  C   . THR   A 54  ? 0.1841 0.1740 0.1216 0.0329  -0.0074 -0.0064 60  THR   A C   
418  O  O   . THR   A 54  ? 0.2092 0.1929 0.1406 0.0339  -0.0053 -0.0046 60  THR   A O   
419  C  CB  . THR   A 54  ? 0.2107 0.2017 0.1437 0.0420  -0.0123 -0.0099 60  THR   A CB  
420  O  OG1 . THR   A 54  ? 0.2342 0.2148 0.1556 0.0450  -0.0102 -0.0072 60  THR   A OG1 
421  C  CG2 . THR   A 54  ? 0.2243 0.2209 0.1600 0.0471  -0.0171 -0.0138 60  THR   A CG2 
422  N  N   . GLY   A 55  ? 0.1741 0.1662 0.1169 0.0286  -0.0061 -0.0057 61  GLY   A N   
423  C  CA  . GLY   A 55  ? 0.1683 0.1562 0.1116 0.0246  -0.0033 -0.0033 61  GLY   A CA  
424  C  C   . GLY   A 55  ? 0.1692 0.1598 0.1168 0.0214  -0.0035 -0.0035 61  GLY   A C   
425  O  O   . GLY   A 55  ? 0.1695 0.1632 0.1174 0.0229  -0.0045 -0.0049 61  GLY   A O   
426  N  N   . VAL   A 56  ? 0.1579 0.1471 0.1084 0.0176  -0.0025 -0.0024 62  VAL   A N   
427  C  CA  . VAL   A 56  ? 0.1543 0.1448 0.1068 0.0153  -0.0035 -0.0029 62  VAL   A CA  
428  C  C   . VAL   A 56  ? 0.1572 0.1513 0.1155 0.0120  -0.0040 -0.0021 62  VAL   A C   
429  O  O   . VAL   A 56  ? 0.1630 0.1556 0.1242 0.0103  -0.0030 -0.0012 62  VAL   A O   
430  C  CB  . VAL   A 56  ? 0.1748 0.1584 0.1252 0.0148  -0.0030 -0.0032 62  VAL   A CB  
431  C  CG1 . VAL   A 56  ? 0.2000 0.1845 0.1513 0.0131  -0.0052 -0.0046 62  VAL   A CG1 
432  C  CG2 . VAL   A 56  ? 0.1916 0.1706 0.1359 0.0186  -0.0023 -0.0037 62  VAL   A CG2 
433  N  N   . TYR   A 57  ? 0.1559 0.1543 0.1155 0.0113  -0.0051 -0.0022 63  TYR   A N   
434  C  CA  . TYR   A 57  ? 0.1497 0.1506 0.1139 0.0088  -0.0058 -0.0010 63  TYR   A CA  
435  C  C   . TYR   A 57  ? 0.1593 0.1590 0.1214 0.0083  -0.0079 -0.0014 63  TYR   A C   
436  O  O   . TYR   A 57  ? 0.1705 0.1687 0.1271 0.0101  -0.0083 -0.0024 63  TYR   A O   
437  C  CB  . TYR   A 57  ? 0.1457 0.1522 0.1139 0.0088  -0.0049 -0.0002 63  TYR   A CB  
438  C  CG  . TYR   A 57  ? 0.1429 0.1519 0.1096 0.0099  -0.0041 0.0003  63  TYR   A CG  
439  C  CD1 . TYR   A 57  ? 0.1543 0.1645 0.1194 0.0123  -0.0029 -0.0009 63  TYR   A CD1 
440  C  CD2 . TYR   A 57  ? 0.1542 0.1643 0.1214 0.0091  -0.0038 0.0022  63  TYR   A CD2 
441  C  CE1 . TYR   A 57  ? 0.1566 0.1692 0.1217 0.0134  -0.0007 -0.0002 63  TYR   A CE1 
442  C  CE2 . TYR   A 57  ? 0.1583 0.1697 0.1234 0.0107  -0.0015 0.0033  63  TYR   A CE2 
443  C  CZ  . TYR   A 57  ? 0.1654 0.1782 0.1299 0.0126  0.0005  0.0021  63  TYR   A CZ  
444  O  OH  . TYR   A 57  ? 0.1830 0.1970 0.1463 0.0142  0.0040  0.0034  63  TYR   A OH  
445  N  N   . TYR   A 58  ? 0.1545 0.1548 0.1207 0.0063  -0.0096 -0.0008 64  TYR   A N   
446  C  CA  . TYR   A 58  ? 0.1604 0.1595 0.1239 0.0067  -0.0129 -0.0016 64  TYR   A CA  
447  C  C   . TYR   A 58  ? 0.1672 0.1691 0.1279 0.0080  -0.0125 0.0007  64  TYR   A C   
448  O  O   . TYR   A 58  ? 0.1633 0.1680 0.1291 0.0069  -0.0113 0.0027  64  TYR   A O   
449  C  CB  . TYR   A 58  ? 0.1574 0.1556 0.1277 0.0045  -0.0158 -0.0026 64  TYR   A CB  
450  C  CG  . TYR   A 58  ? 0.1782 0.1752 0.1452 0.0058  -0.0207 -0.0044 64  TYR   A CG  
451  C  CD1 . TYR   A 58  ? 0.1882 0.1815 0.1485 0.0076  -0.0229 -0.0072 64  TYR   A CD1 
452  C  CD2 . TYR   A 58  ? 0.1873 0.1865 0.1565 0.0060  -0.0236 -0.0033 64  TYR   A CD2 
453  C  CE1 . TYR   A 58  ? 0.2162 0.2079 0.1715 0.0097  -0.0282 -0.0095 64  TYR   A CE1 
454  C  CE2 . TYR   A 58  ? 0.2104 0.2079 0.1743 0.0083  -0.0289 -0.0051 64  TYR   A CE2 
455  C  CZ  . TYR   A 58  ? 0.2332 0.2270 0.1897 0.0103  -0.0314 -0.0083 64  TYR   A CZ  
456  O  OH  . TYR   A 58  ? 0.2681 0.2597 0.2179 0.0134  -0.0376 -0.0108 64  TYR   A OH  
457  N  N   . CYS   A 59  ? 0.1683 0.1684 0.1206 0.0106  -0.0130 0.0004  65  CYS   A N   
458  C  CA  . CYS   A 59  ? 0.1670 0.1681 0.1148 0.0126  -0.0112 0.0032  65  CYS   A CA  
459  C  C   . CYS   A 59  ? 0.1940 0.1918 0.1347 0.0147  -0.0158 0.0027  65  CYS   A C   
460  O  O   . CYS   A 59  ? 0.2064 0.2006 0.1381 0.0174  -0.0177 0.0005  65  CYS   A O   
461  C  CB  . CYS   A 59  ? 0.1778 0.1790 0.1205 0.0149  -0.0070 0.0036  65  CYS   A CB  
462  S  SG  . CYS   A 59  ? 0.2113 0.2121 0.1476 0.0178  -0.0026 0.0077  65  CYS   A SG  
463  N  N   . SER   A 60  ? 0.2007 0.1994 0.1452 0.0141  -0.0180 0.0044  66  SER   A N   
464  C  CA  . SER   A 60  ? 0.2071 0.2030 0.1454 0.0168  -0.0238 0.0033  66  SER   A CA  
465  C  C   . SER   A 60  ? 0.2086 0.2006 0.1320 0.0218  -0.0227 0.0052  66  SER   A C   
466  O  O   . SER   A 60  ? 0.2284 0.2165 0.1423 0.0253  -0.0279 0.0024  66  SER   A O   
467  C  CB  . SER   A 60  ? 0.2593 0.2570 0.2049 0.0157  -0.0267 0.0047  66  SER   A CB  
468  O  OG  . SER   A 60  ? 0.3285 0.3269 0.2734 0.0164  -0.0222 0.0096  66  SER   A OG  
469  N  N   . SER   A 61  ? 0.1889 0.1815 0.1103 0.0225  -0.0155 0.0094  67  SER   A N   
470  C  CA  . SER   A 61  ? 0.2024 0.1906 0.1094 0.0275  -0.0123 0.0121  67  SER   A CA  
471  C  C   . SER   A 61  ? 0.2010 0.1863 0.0983 0.0302  -0.0117 0.0090  67  SER   A C   
472  O  O   . SER   A 61  ? 0.2233 0.2042 0.1070 0.0351  -0.0089 0.0108  67  SER   A O   
473  C  CB  . SER   A 61  ? 0.2181 0.2076 0.1281 0.0272  -0.0037 0.0175  67  SER   A CB  
474  O  OG  . SER   A 61  ? 0.2325 0.2265 0.1523 0.0241  0.0011  0.0166  67  SER   A OG  
475  N  N   . ARG   A 62  ? 0.1983 0.1854 0.1019 0.0275  -0.0139 0.0046  68  ARG   A N   
476  C  CA  . ARG   A 62  ? 0.2105 0.1946 0.1065 0.0297  -0.0143 0.0009  68  ARG   A CA  
477  C  C   . ARG   A 62  ? 0.2335 0.2158 0.1320 0.0284  -0.0222 -0.0049 68  ARG   A C   
478  O  O   . ARG   A 62  ? 0.2512 0.2303 0.1443 0.0300  -0.0234 -0.0088 68  ARG   A O   
479  C  CB  . ARG   A 62  ? 0.2163 0.2037 0.1189 0.0279  -0.0081 0.0013  68  ARG   A CB  
480  C  CG  . ARG   A 62  ? 0.2217 0.2112 0.1242 0.0291  0.0001  0.0060  68  ARG   A CG  
481  C  CD  . ARG   A 62  ? 0.2508 0.2352 0.1380 0.0348  0.0033  0.0067  68  ARG   A CD  
482  N  NE  . ARG   A 62  ? 0.2705 0.2564 0.1591 0.0359  0.0127  0.0114  68  ARG   A NE  
483  C  CZ  . ARG   A 62  ? 0.2739 0.2581 0.1594 0.0373  0.0166  0.0166  68  ARG   A CZ  
484  N  NH1 . ARG   A 62  ? 0.2655 0.2466 0.1453 0.0383  0.0113  0.0176  68  ARG   A NH1 
485  N  NH2 . ARG   A 62  ? 0.2714 0.2569 0.1606 0.0380  0.0262  0.0207  68  ARG   A NH2 
486  N  N   . ARG   A 63  ? 0.2305 0.2149 0.1389 0.0252  -0.0269 -0.0057 69  ARG   A N   
487  C  CA  . ARG   A 63  ? 0.2500 0.2334 0.1654 0.0230  -0.0331 -0.0110 69  ARG   A CA  
488  C  C   . ARG   A 63  ? 0.2505 0.2331 0.1700 0.0209  -0.0301 -0.0131 69  ARG   A C   
489  O  O   . ARG   A 63  ? 0.2686 0.2474 0.1865 0.0215  -0.0335 -0.0178 69  ARG   A O   
490  C  CB  . ARG   A 63  ? 0.3014 0.2802 0.2072 0.0271  -0.0407 -0.0156 69  ARG   A CB  
491  C  CG  . ARG   A 63  ? 0.3711 0.3501 0.2735 0.0297  -0.0454 -0.0143 69  ARG   A CG  
492  C  CD  . ARG   A 63  ? 0.4018 0.3777 0.3021 0.0321  -0.0558 -0.0210 69  ARG   A CD  
493  N  NE  . ARG   A 63  ? 0.4370 0.4122 0.3307 0.0363  -0.0610 -0.0197 69  ARG   A NE  
494  C  CZ  . ARG   A 63  ? 0.4690 0.4388 0.3435 0.0435  -0.0641 -0.0201 69  ARG   A CZ  
495  N  NH1 . ARG   A 63  ? 0.4892 0.4540 0.3498 0.0470  -0.0623 -0.0221 69  ARG   A NH1 
496  N  NH2 . ARG   A 63  ? 0.4456 0.4142 0.3136 0.0478  -0.0686 -0.0181 69  ARG   A NH2 
497  N  N   . LYS   A 64  ? 0.2273 0.2133 0.1516 0.0191  -0.0238 -0.0096 70  LYS   A N   
498  C  CA  . LYS   A 64  ? 0.2261 0.2110 0.1522 0.0184  -0.0208 -0.0110 70  LYS   A CA  
499  C  C   . LYS   A 64  ? 0.2027 0.1913 0.1385 0.0153  -0.0172 -0.0084 70  LYS   A C   
500  O  O   . LYS   A 64  ? 0.2013 0.1938 0.1405 0.0144  -0.0152 -0.0052 70  LYS   A O   
501  C  CB  . LYS   A 64  ? 0.2734 0.2579 0.1905 0.0220  -0.0164 -0.0099 70  LYS   A CB  
502  C  CG  . LYS   A 64  ? 0.3916 0.3709 0.2972 0.0260  -0.0185 -0.0135 70  LYS   A CG  
503  C  CD  . LYS   A 64  ? 0.4870 0.4668 0.3864 0.0292  -0.0124 -0.0119 70  LYS   A CD  
504  C  CE  . LYS   A 64  ? 0.5848 0.5590 0.4739 0.0331  -0.0133 -0.0160 70  LYS   A CE  
505  N  NZ  . LYS   A 64  ? 0.6517 0.6212 0.5286 0.0367  -0.0178 -0.0182 70  LYS   A NZ  
506  N  N   . HIS   A 65  ? 0.1880 0.1745 0.1267 0.0145  -0.0159 -0.0097 71  HIS   A N   
507  C  CA  . HIS   A 65  ? 0.1855 0.1744 0.1301 0.0130  -0.0125 -0.0076 71  HIS   A CA  
508  C  C   . HIS   A 65  ? 0.2106 0.2005 0.1511 0.0158  -0.0094 -0.0073 71  HIS   A C   
509  O  O   . HIS   A 65  ? 0.2261 0.2128 0.1608 0.0182  -0.0095 -0.0093 71  HIS   A O   
510  C  CB  . HIS   A 65  ? 0.1768 0.1615 0.1260 0.0112  -0.0126 -0.0088 71  HIS   A CB  
511  C  CG  . HIS   A 65  ? 0.1870 0.1711 0.1436 0.0082  -0.0150 -0.0094 71  HIS   A CG  
512  N  ND1 . HIS   A 65  ? 0.2397 0.2260 0.2036 0.0059  -0.0132 -0.0073 71  HIS   A ND1 
513  C  CD2 . HIS   A 65  ? 0.1887 0.1704 0.1473 0.0074  -0.0193 -0.0126 71  HIS   A CD2 
514  C  CE1 . HIS   A 65  ? 0.2189 0.2044 0.1899 0.0037  -0.0158 -0.0089 71  HIS   A CE1 
515  N  NE2 . HIS   A 65  ? 0.2253 0.2085 0.1939 0.0044  -0.0200 -0.0122 71  HIS   A NE2 
516  N  N   . TYR   A 66  ? 0.1861 0.1805 0.1306 0.0158  -0.0069 -0.0053 72  TYR   A N   
517  C  CA  . TYR   A 66  ? 0.1841 0.1807 0.1277 0.0185  -0.0045 -0.0056 72  TYR   A CA  
518  C  C   . TYR   A 66  ? 0.1785 0.1759 0.1259 0.0187  -0.0041 -0.0055 72  TYR   A C   
519  O  O   . TYR   A 66  ? 0.1730 0.1722 0.1247 0.0169  -0.0044 -0.0044 72  TYR   A O   
520  C  CB  . TYR   A 66  ? 0.1866 0.1889 0.1329 0.0187  -0.0020 -0.0039 72  TYR   A CB  
521  C  CG  . TYR   A 66  ? 0.1956 0.1965 0.1355 0.0200  -0.0012 -0.0033 72  TYR   A CG  
522  C  CD1 . TYR   A 66  ? 0.2210 0.2199 0.1544 0.0232  0.0005  -0.0047 72  TYR   A CD1 
523  C  CD2 . TYR   A 66  ? 0.2089 0.2099 0.1480 0.0188  -0.0018 -0.0013 72  TYR   A CD2 
524  C  CE1 . TYR   A 66  ? 0.2360 0.2324 0.1609 0.0254  0.0015  -0.0042 72  TYR   A CE1 
525  C  CE2 . TYR   A 66  ? 0.2304 0.2289 0.1608 0.0211  -0.0012 -0.0005 72  TYR   A CE2 
526  C  CZ  . TYR   A 66  ? 0.2521 0.2481 0.1747 0.0246  0.0006  -0.0020 72  TYR   A CZ  
527  O  OH  . TYR   A 66  ? 0.2774 0.2698 0.1890 0.0278  0.0015  -0.0012 72  TYR   A OH  
528  N  N   . PRO   A 67  ? 0.1767 0.1727 0.1218 0.0218  -0.0037 -0.0067 73  PRO   A N   
529  C  CA  . PRO   A 67  ? 0.1829 0.1795 0.1297 0.0235  -0.0040 -0.0068 73  PRO   A CA  
530  C  C   . PRO   A 67  ? 0.2040 0.2084 0.1575 0.0242  -0.0038 -0.0073 73  PRO   A C   
531  O  O   . PRO   A 67  ? 0.2333 0.2418 0.1895 0.0250  -0.0023 -0.0078 73  PRO   A O   
532  C  CB  . PRO   A 67  ? 0.1924 0.1846 0.1343 0.0272  -0.0040 -0.0081 73  PRO   A CB  
533  C  CG  . PRO   A 67  ? 0.1921 0.1851 0.1323 0.0279  -0.0031 -0.0092 73  PRO   A CG  
534  C  CD  . PRO   A 67  ? 0.1729 0.1666 0.1131 0.0246  -0.0031 -0.0083 73  PRO   A CD  
535  N  N   . VAL   A 68  ? 0.1788 0.1850 0.1353 0.0243  -0.0051 -0.0075 74  VAL   A N   
536  C  CA  . VAL   A 68  ? 0.1862 0.1998 0.1511 0.0246  -0.0056 -0.0089 74  VAL   A CA  
537  C  C   . VAL   A 68  ? 0.1850 0.1991 0.1499 0.0280  -0.0085 -0.0111 74  VAL   A C   
538  O  O   . VAL   A 68  ? 0.1928 0.2011 0.1505 0.0292  -0.0093 -0.0103 74  VAL   A O   
539  C  CB  . VAL   A 68  ? 0.2068 0.2234 0.1774 0.0206  -0.0047 -0.0076 74  VAL   A CB  
540  C  CG1 . VAL   A 68  ? 0.2252 0.2430 0.1969 0.0186  -0.0020 -0.0057 74  VAL   A CG1 
541  C  CG2 . VAL   A 68  ? 0.2198 0.2319 0.1867 0.0189  -0.0053 -0.0062 74  VAL   A CG2 
542  N  N   . SER   A 69  ? 0.1681 0.1891 0.1415 0.0298  -0.0100 -0.0139 75  SER   A N   
543  C  CA  . SER   A 69  ? 0.1834 0.2062 0.1584 0.0331  -0.0142 -0.0171 75  SER   A CA  
544  C  C   . SER   A 69  ? 0.1677 0.1958 0.1526 0.0297  -0.0143 -0.0180 75  SER   A C   
545  O  O   . SER   A 69  ? 0.1669 0.2001 0.1616 0.0267  -0.0117 -0.0177 75  SER   A O   
546  C  CB  . SER   A 69  ? 0.2249 0.2530 0.2060 0.0374  -0.0168 -0.0206 75  SER   A CB  
547  O  OG  . SER   A 69  ? 0.3073 0.3297 0.2788 0.0412  -0.0169 -0.0198 75  SER   A OG  
548  N  N   . PHE   A 70  ? 0.1538 0.1797 0.1355 0.0302  -0.0166 -0.0189 76  PHE   A N   
549  C  CA  . PHE   A 70  ? 0.1518 0.1816 0.1427 0.0268  -0.0165 -0.0199 76  PHE   A CA  
550  C  C   . PHE   A 70  ? 0.1661 0.1981 0.1597 0.0301  -0.0217 -0.0250 76  PHE   A C   
551  O  O   . PHE   A 70  ? 0.1937 0.2216 0.1772 0.0353  -0.0251 -0.0266 76  PHE   A O   
552  C  CB  . PHE   A 70  ? 0.1519 0.1772 0.1383 0.0229  -0.0133 -0.0159 76  PHE   A CB  
553  C  CG  . PHE   A 70  ? 0.1593 0.1767 0.1330 0.0247  -0.0131 -0.0142 76  PHE   A CG  
554  C  CD1 . PHE   A 70  ? 0.1650 0.1769 0.1307 0.0248  -0.0108 -0.0112 76  PHE   A CD1 
555  C  CD2 . PHE   A 70  ? 0.1791 0.1942 0.1494 0.0263  -0.0144 -0.0156 76  PHE   A CD2 
556  C  CE1 . PHE   A 70  ? 0.1940 0.1982 0.1500 0.0263  -0.0094 -0.0093 76  PHE   A CE1 
557  C  CE2 . PHE   A 70  ? 0.1903 0.1974 0.1490 0.0282  -0.0126 -0.0133 76  PHE   A CE2 
558  C  CZ  . PHE   A 70  ? 0.2011 0.2029 0.1537 0.0279  -0.0097 -0.0100 76  PHE   A CZ  
559  N  N   . SER   A 71  ? 0.1605 0.1987 0.1680 0.0276  -0.0224 -0.0278 77  SER   A N   
560  C  CA  . SER   A 71  ? 0.1649 0.2057 0.1768 0.0306  -0.0283 -0.0339 77  SER   A CA  
561  C  C   . SER   A 71  ? 0.1708 0.2051 0.1716 0.0316  -0.0289 -0.0335 77  SER   A C   
562  O  O   . SER   A 71  ? 0.1798 0.2095 0.1745 0.0285  -0.0243 -0.0285 77  SER   A O   
563  C  CB  . SER   A 71  ? 0.1748 0.2234 0.2067 0.0271  -0.0284 -0.0372 77  SER   A CB  
564  O  OG  . SER   A 71  ? 0.1946 0.2417 0.2294 0.0217  -0.0234 -0.0332 77  SER   A OG  
565  N  N   . LYS   A 72  ? 0.1732 0.2072 0.1712 0.0364  -0.0348 -0.0390 78  LYS   A N   
566  C  CA  . LYS   A 72  ? 0.1988 0.2267 0.1862 0.0382  -0.0352 -0.0393 78  LYS   A CA  
567  C  C   . LYS   A 72  ? 0.1959 0.2263 0.1946 0.0323  -0.0324 -0.0389 78  LYS   A C   
568  O  O   . LYS   A 72  ? 0.2001 0.2373 0.2156 0.0287  -0.0327 -0.0410 78  LYS   A O   
569  C  CB  . LYS   A 72  ? 0.2293 0.2568 0.2117 0.0454  -0.0431 -0.0465 78  LYS   A CB  
570  C  CG  . LYS   A 72  ? 0.3056 0.3287 0.2738 0.0522  -0.0456 -0.0459 78  LYS   A CG  
571  C  CD  . LYS   A 72  ? 0.3587 0.3794 0.3174 0.0610  -0.0539 -0.0526 78  LYS   A CD  
572  C  CE  . LYS   A 72  ? 0.4468 0.4582 0.3842 0.0678  -0.0533 -0.0489 78  LYS   A CE  
573  N  NZ  . LYS   A 72  ? 0.5024 0.5123 0.4306 0.0778  -0.0626 -0.0552 78  LYS   A NZ  
574  N  N   . PRO   A 73  ? 0.1913 0.2159 0.1816 0.0317  -0.0293 -0.0364 79  PRO   A N   
575  C  CA  . PRO   A 73  ? 0.1940 0.2204 0.1948 0.0267  -0.0269 -0.0360 79  PRO   A CA  
576  C  C   . PRO   A 73  ? 0.1912 0.2225 0.2047 0.0272  -0.0320 -0.0433 79  PRO   A C   
577  O  O   . PRO   A 73  ? 0.1997 0.2298 0.2075 0.0327  -0.0378 -0.0493 79  PRO   A O   
578  C  CB  . PRO   A 73  ? 0.2193 0.2384 0.2077 0.0278  -0.0238 -0.0335 79  PRO   A CB  
579  C  CG  . PRO   A 73  ? 0.2489 0.2616 0.2200 0.0334  -0.0238 -0.0321 79  PRO   A CG  
580  C  CD  . PRO   A 73  ? 0.2099 0.2256 0.1815 0.0357  -0.0273 -0.0335 79  PRO   A CD  
581  N  N   . SER   A 74  ? 0.1827 0.2192 0.2133 0.0218  -0.0300 -0.0430 80  SER   A N   
582  C  CA  . SER   A 74  ? 0.1946 0.2361 0.2412 0.0214  -0.0344 -0.0503 80  SER   A CA  
583  C  C   . SER   A 74  ? 0.1848 0.2281 0.2466 0.0152  -0.0297 -0.0479 80  SER   A C   
584  O  O   . SER   A 74  ? 0.1813 0.2220 0.2399 0.0118  -0.0237 -0.0407 80  SER   A O   
585  C  CB  . SER   A 74  ? 0.2464 0.2944 0.3026 0.0233  -0.0388 -0.0548 80  SER   A CB  
586  O  OG  . SER   A 74  ? 0.3058 0.3578 0.3725 0.0189  -0.0334 -0.0501 80  SER   A OG  
587  N  N   . LEU   A 75  ? 0.1740 0.2211 0.2523 0.0142  -0.0330 -0.0545 81  LEU   A N   
588  C  CA  . LEU   A 75  ? 0.1758 0.2239 0.2703 0.0087  -0.0286 -0.0529 81  LEU   A CA  
589  C  C   . LEU   A 75  ? 0.1732 0.2266 0.2825 0.0053  -0.0248 -0.0504 81  LEU   A C   
590  O  O   . LEU   A 75  ? 0.1754 0.2346 0.2967 0.0065  -0.0288 -0.0564 81  LEU   A O   
591  C  CB  . LEU   A 75  ? 0.1871 0.2367 0.2941 0.0095  -0.0342 -0.0622 81  LEU   A CB  
592  C  CG  . LEU   A 75  ? 0.2546 0.2984 0.3532 0.0109  -0.0351 -0.0637 81  LEU   A CG  
593  C  CD1 . LEU   A 75  ? 0.2798 0.3252 0.3890 0.0132  -0.0426 -0.0749 81  LEU   A CD1 
594  C  CD2 . LEU   A 75  ? 0.2537 0.2946 0.3575 0.0057  -0.0276 -0.0567 81  LEU   A CD2 
595  N  N   . ILE   A 76  ? 0.1737 0.2253 0.2824 0.0016  -0.0172 -0.0419 82  ILE   A N   
596  C  CA  . ILE   A 76  ? 0.1799 0.2350 0.2991 -0.0010 -0.0119 -0.0382 82  ILE   A CA  
597  C  C   . ILE   A 76  ? 0.1843 0.2374 0.3148 -0.0056 -0.0050 -0.0334 82  ILE   A C   
598  O  O   . ILE   A 76  ? 0.1795 0.2273 0.3015 -0.0064 -0.0027 -0.0287 82  ILE   A O   
599  C  CB  . ILE   A 76  ? 0.1976 0.2508 0.2999 0.0005  -0.0093 -0.0319 82  ILE   A CB  
600  C  CG1 . ILE   A 76  ? 0.2301 0.2851 0.3235 0.0052  -0.0157 -0.0367 82  ILE   A CG1 
601  C  CG2 . ILE   A 76  ? 0.2075 0.2625 0.3169 -0.0019 -0.0023 -0.0267 82  ILE   A CG2 
602  C  CD1 . ILE   A 76  ? 0.2728 0.3257 0.3515 0.0070  -0.0142 -0.0322 82  ILE   A CD1 
603  N  N   . PHE   A 77  ? 0.1791 0.2362 0.3295 -0.0082 -0.0013 -0.0344 83  PHE   A N   
604  C  CA  . PHE   A 77  ? 0.2005 0.2545 0.3615 -0.0121 0.0066  -0.0289 83  PHE   A CA  
605  C  C   . PHE   A 77  ? 0.2079 0.2574 0.3546 -0.0122 0.0135  -0.0187 83  PHE   A C   
606  O  O   . PHE   A 77  ? 0.2260 0.2773 0.3660 -0.0107 0.0150  -0.0166 83  PHE   A O   
607  C  CB  . PHE   A 77  ? 0.2084 0.2673 0.3956 -0.0149 0.0100  -0.0323 83  PHE   A CB  
608  C  CG  . PHE   A 77  ? 0.2416 0.2961 0.4405 -0.0187 0.0187  -0.0266 83  PHE   A CG  
609  C  CD1 . PHE   A 77  ? 0.2665 0.3187 0.4659 -0.0199 0.0287  -0.0181 83  PHE   A CD1 
610  C  CD2 . PHE   A 77  ? 0.2644 0.3156 0.4713 -0.0204 0.0173  -0.0291 83  PHE   A CD2 
611  C  CE1 . PHE   A 77  ? 0.2819 0.3284 0.4898 -0.0226 0.0373  -0.0119 83  PHE   A CE1 
612  C  CE2 . PHE   A 77  ? 0.2810 0.3269 0.4982 -0.0236 0.0257  -0.0233 83  PHE   A CE2 
613  C  CZ  . PHE   A 77  ? 0.2771 0.3206 0.4948 -0.0246 0.0358  -0.0145 83  PHE   A CZ  
614  N  N   . VAL   A 78  ? 0.1918 0.2351 0.3326 -0.0132 0.0168  -0.0129 84  VAL   A N   
615  C  CA  . VAL   A 78  ? 0.1963 0.2347 0.3230 -0.0126 0.0221  -0.0039 84  VAL   A CA  
616  C  C   . VAL   A 78  ? 0.2081 0.2419 0.3444 -0.0148 0.0300  0.0019  84  VAL   A C   
617  O  O   . VAL   A 78  ? 0.2022 0.2332 0.3453 -0.0162 0.0295  0.0012  84  VAL   A O   
618  C  CB  . VAL   A 78  ? 0.2070 0.2416 0.3152 -0.0107 0.0177  -0.0021 84  VAL   A CB  
619  C  CG1 . VAL   A 78  ? 0.2187 0.2485 0.3130 -0.0096 0.0217  0.0062  84  VAL   A CG1 
620  C  CG2 . VAL   A 78  ? 0.2065 0.2442 0.3052 -0.0084 0.0110  -0.0073 84  VAL   A CG2 
621  N  N   . GLU   A 79  ? 0.2084 0.2403 0.3424 -0.0144 0.0375  0.0084  85  GLU   A N   
622  C  CA  . GLU   A 79  ? 0.2206 0.2467 0.3614 -0.0156 0.0466  0.0153  85  GLU   A CA  
623  C  C   . GLU   A 79  ? 0.2173 0.2361 0.3464 -0.0144 0.0460  0.0206  85  GLU   A C   
624  O  O   . GLU   A 79  ? 0.2102 0.2282 0.3226 -0.0122 0.0402  0.0209  85  GLU   A O   
625  C  CB  . GLU   A 79  ? 0.2887 0.3129 0.4226 -0.0139 0.0546  0.0218  85  GLU   A CB  
626  C  CG  . GLU   A 79  ? 0.4303 0.4560 0.5851 -0.0162 0.0638  0.0226  85  GLU   A CG  
627  C  CD  . GLU   A 79  ? 0.6116 0.6325 0.7567 -0.0138 0.0739  0.0311  85  GLU   A CD  
628  O  OE1 . GLU   A 79  ? 0.6543 0.6715 0.8119 -0.0151 0.0847  0.0359  85  GLU   A OE1 
629  O  OE2 . GLU   A 79  ? 0.6690 0.6892 0.7938 -0.0104 0.0714  0.0329  85  GLU   A OE2 
630  N  N   . ALA   A 80  ? 0.2180 0.2310 0.3564 -0.0157 0.0526  0.0252  86  ALA   A N   
631  C  CA  . ALA   A 80  ? 0.2280 0.2338 0.3565 -0.0141 0.0524  0.0307  86  ALA   A CA  
632  C  C   . ALA   A 80  ? 0.2403 0.2415 0.3461 -0.0099 0.0531  0.0378  86  ALA   A C   
633  O  O   . ALA   A 80  ? 0.2522 0.2528 0.3522 -0.0084 0.0583  0.0414  86  ALA   A O   
634  C  CB  . ALA   A 80  ? 0.2286 0.2279 0.3713 -0.0157 0.0606  0.0353  86  ALA   A CB  
635  N  N   . SER   A 81  ? 0.2410 0.2395 0.3346 -0.0077 0.0476  0.0392  87  SER   A N   
636  C  CA  . SER   A 81  ? 0.2503 0.2441 0.3232 -0.0034 0.0465  0.0451  87  SER   A CA  
637  C  C   . SER   A 81  ? 0.2639 0.2510 0.3339 -0.0014 0.0460  0.0498  87  SER   A C   
638  O  O   . SER   A 81  ? 0.2601 0.2461 0.3442 -0.0038 0.0473  0.0485  87  SER   A O   
639  C  CB  . SER   A 81  ? 0.2533 0.2523 0.3151 -0.0025 0.0379  0.0402  87  SER   A CB  
640  O  OG  . SER   A 81  ? 0.2382 0.2395 0.3039 -0.0037 0.0315  0.0357  87  SER   A OG  
641  N  N   . GLU   A 82  ? 0.2749 0.2574 0.3272 0.0032  0.0435  0.0546  88  GLU   A N   
642  C  CA  . GLU   A 82  ? 0.3010 0.2777 0.3501 0.0058  0.0414  0.0585  88  GLU   A CA  
643  C  C   . GLU   A 82  ? 0.2805 0.2625 0.3368 0.0037  0.0336  0.0519  88  GLU   A C   
644  O  O   . GLU   A 82  ? 0.2866 0.2653 0.3465 0.0047  0.0324  0.0535  88  GLU   A O   
645  C  CB  . GLU   A 82  ? 0.3871 0.3586 0.4153 0.0119  0.0389  0.0639  88  GLU   A CB  
646  C  CG  . GLU   A 82  ? 0.5205 0.4979 0.5388 0.0125  0.0312  0.0589  88  GLU   A CG  
647  C  CD  . GLU   A 82  ? 0.7217 0.6950 0.7196 0.0181  0.0292  0.0625  88  GLU   A CD  
648  O  OE1 . GLU   A 82  ? 0.7751 0.7453 0.7652 0.0198  0.0353  0.0657  88  GLU   A OE1 
649  O  OE2 . GLU   A 82  ? 0.7815 0.7550 0.7717 0.0209  0.0211  0.0612  88  GLU   A OE2 
650  N  N   . TYR   A 83  ? 0.2554 0.2452 0.3138 0.0011  0.0291  0.0448  89  TYR   A N   
651  C  CA  . TYR   A 83  ? 0.2385 0.2327 0.3019 -0.0003 0.0229  0.0389  89  TYR   A CA  
652  C  C   . TYR   A 83  ? 0.2259 0.2231 0.3050 -0.0040 0.0238  0.0331  89  TYR   A C   
653  O  O   . TYR   A 83  ? 0.2267 0.2248 0.3104 -0.0044 0.0205  0.0298  89  TYR   A O   
654  C  CB  . TYR   A 83  ? 0.2326 0.2319 0.2870 0.0000  0.0174  0.0350  89  TYR   A CB  
655  C  CG  . TYR   A 83  ? 0.2388 0.2356 0.2781 0.0037  0.0150  0.0390  89  TYR   A CG  
656  C  CD1 . TYR   A 83  ? 0.2625 0.2589 0.2926 0.0048  0.0170  0.0405  89  TYR   A CD1 
657  C  CD2 . TYR   A 83  ? 0.2548 0.2500 0.2896 0.0064  0.0102  0.0405  89  TYR   A CD2 
658  C  CE1 . TYR   A 83  ? 0.2807 0.2747 0.2960 0.0087  0.0139  0.0430  89  TYR   A CE1 
659  C  CE2 . TYR   A 83  ? 0.2727 0.2656 0.2940 0.0103  0.0067  0.0431  89  TYR   A CE2 
660  C  CZ  . TYR   A 83  ? 0.2940 0.2862 0.3050 0.0114  0.0084  0.0441  89  TYR   A CZ  
661  O  OH  . TYR   A 83  ? 0.3215 0.3110 0.3182 0.0158  0.0043  0.0458  89  TYR   A OH  
662  N  N   . TYR   A 84  ? 0.2132 0.2123 0.3005 -0.0064 0.0277  0.0312  90  TYR   A N   
663  C  CA  . TYR   A 84  ? 0.1957 0.1980 0.2983 -0.0095 0.0272  0.0243  90  TYR   A CA  
664  C  C   . TYR   A 84  ? 0.2130 0.2141 0.3294 -0.0118 0.0338  0.0252  90  TYR   A C   
665  O  O   . TYR   A 84  ? 0.2156 0.2162 0.3286 -0.0114 0.0384  0.0292  90  TYR   A O   
666  C  CB  . TYR   A 84  ? 0.1766 0.1858 0.2770 -0.0102 0.0223  0.0170  90  TYR   A CB  
667  C  CG  . TYR   A 84  ? 0.1573 0.1682 0.2460 -0.0085 0.0167  0.0152  90  TYR   A CG  
668  C  CD1 . TYR   A 84  ? 0.1562 0.1670 0.2476 -0.0084 0.0137  0.0117  90  TYR   A CD1 
669  C  CD2 . TYR   A 84  ? 0.1687 0.1812 0.2449 -0.0071 0.0150  0.0167  90  TYR   A CD2 
670  C  CE1 . TYR   A 84  ? 0.1595 0.1719 0.2420 -0.0070 0.0099  0.0100  90  TYR   A CE1 
671  C  CE2 . TYR   A 84  ? 0.1664 0.1804 0.2342 -0.0060 0.0105  0.0147  90  TYR   A CE2 
672  C  CZ  . TYR   A 84  ? 0.1639 0.1779 0.2354 -0.0060 0.0084  0.0115  90  TYR   A CZ  
673  O  OH  . TYR   A 84  ? 0.1581 0.1732 0.2229 -0.0050 0.0054  0.0101  90  TYR   A OH  
674  N  N   . PRO   A 85  ? 0.2234 0.2246 0.3566 -0.0144 0.0344  0.0206  91  PRO   A N   
675  C  CA  . PRO   A 85  ? 0.2224 0.2239 0.3725 -0.0172 0.0403  0.0198  91  PRO   A CA  
676  C  C   . PRO   A 85  ? 0.2203 0.2299 0.3733 -0.0183 0.0373  0.0132  91  PRO   A C   
677  O  O   . PRO   A 85  ? 0.2220 0.2359 0.3642 -0.0168 0.0305  0.0089  91  PRO   A O   
678  C  CB  . PRO   A 85  ? 0.2248 0.2247 0.3918 -0.0194 0.0394  0.0146  91  PRO   A CB  
679  C  CG  . PRO   A 85  ? 0.2435 0.2460 0.4023 -0.0179 0.0312  0.0089  91  PRO   A CG  
680  C  CD  . PRO   A 85  ? 0.2248 0.2262 0.3631 -0.0147 0.0296  0.0149  91  PRO   A CD  
681  N  N   . ALA   A 86  ? 0.2135 0.2252 0.3825 -0.0207 0.0422  0.0118  92  ALA   A N   
682  C  CA  . ALA   A 86  ? 0.2147 0.2347 0.3892 -0.0214 0.0387  0.0047  92  ALA   A CA  
683  C  C   . ALA   A 86  ? 0.2027 0.2269 0.3817 -0.0214 0.0294  -0.0057 92  ALA   A C   
684  O  O   . ALA   A 86  ? 0.1927 0.2144 0.3829 -0.0229 0.0286  -0.0090 92  ALA   A O   
685  C  CB  . ALA   A 86  ? 0.2138 0.2355 0.4097 -0.0243 0.0458  0.0044  92  ALA   A CB  
686  N  N   . ARG   A 87  ? 0.1921 0.2212 0.3597 -0.0192 0.0227  -0.0102 93  ARG   A N   
687  C  CA  . ARG   A 87  ? 0.1816 0.2130 0.3486 -0.0180 0.0143  -0.0192 93  ARG   A CA  
688  C  C   . ARG   A 87  ? 0.1853 0.2223 0.3432 -0.0154 0.0084  -0.0241 93  ARG   A C   
689  O  O   . ARG   A 87  ? 0.2000 0.2386 0.3507 -0.0148 0.0108  -0.0199 93  ARG   A O   
690  C  CB  . ARG   A 87  ? 0.1913 0.2177 0.3445 -0.0164 0.0127  -0.0164 93  ARG   A CB  
691  C  CG  . ARG   A 87  ? 0.2074 0.2337 0.3393 -0.0138 0.0114  -0.0119 93  ARG   A CG  
692  C  CD  . ARG   A 87  ? 0.2251 0.2462 0.3466 -0.0129 0.0129  -0.0056 93  ARG   A CD  
693  N  NE  . ARG   A 87  ? 0.2139 0.2356 0.3192 -0.0105 0.0091  -0.0056 93  ARG   A NE  
694  C  CZ  . ARG   A 87  ? 0.2090 0.2318 0.3028 -0.0094 0.0091  -0.0023 93  ARG   A CZ  
695  N  NH1 . ARG   A 87  ? 0.1994 0.2220 0.2809 -0.0076 0.0062  -0.0024 93  ARG   A NH1 
696  N  NH2 . ARG   A 87  ? 0.1981 0.2218 0.2932 -0.0100 0.0125  0.0010  93  ARG   A NH2 
697  N  N   . TYR   A 88  ? 0.1704 0.2093 0.3267 -0.0133 0.0009  -0.0325 94  TYR   A N   
698  C  CA  . TYR   A 88  ? 0.1752 0.2174 0.3190 -0.0098 -0.0047 -0.0361 94  TYR   A CA  
699  C  C   . TYR   A 88  ? 0.1781 0.2161 0.3008 -0.0075 -0.0054 -0.0320 94  TYR   A C   
700  O  O   . TYR   A 88  ? 0.1951 0.2294 0.3147 -0.0070 -0.0064 -0.0329 94  TYR   A O   
701  C  CB  . TYR   A 88  ? 0.1774 0.2229 0.3272 -0.0074 -0.0128 -0.0472 94  TYR   A CB  
702  C  CG  . TYR   A 88  ? 0.1914 0.2427 0.3639 -0.0094 -0.0135 -0.0526 94  TYR   A CG  
703  C  CD1 . TYR   A 88  ? 0.2054 0.2624 0.3800 -0.0080 -0.0152 -0.0545 94  TYR   A CD1 
704  C  CD2 . TYR   A 88  ? 0.2142 0.2652 0.4078 -0.0128 -0.0117 -0.0557 94  TYR   A CD2 
705  C  CE1 . TYR   A 88  ? 0.2287 0.2919 0.4269 -0.0100 -0.0155 -0.0597 94  TYR   A CE1 
706  C  CE2 . TYR   A 88  ? 0.2252 0.2819 0.4429 -0.0152 -0.0116 -0.0609 94  TYR   A CE2 
707  C  CZ  . TYR   A 88  ? 0.2439 0.3071 0.4644 -0.0137 -0.0136 -0.0631 94  TYR   A CZ  
708  O  OH  . TYR   A 88  ? 0.2784 0.3480 0.5255 -0.0161 -0.0135 -0.0688 94  TYR   A OH  
709  N  N   . GLN   A 89  ? 0.1610 0.1994 0.2708 -0.0062 -0.0044 -0.0276 95  GLN   A N   
710  C  CA  . GLN   A 89  ? 0.1475 0.1824 0.2393 -0.0042 -0.0051 -0.0243 95  GLN   A CA  
711  C  C   . GLN   A 89  ? 0.1510 0.1870 0.2335 -0.0003 -0.0107 -0.0301 95  GLN   A C   
712  O  O   . GLN   A 89  ? 0.1653 0.2050 0.2495 0.0010  -0.0129 -0.0328 95  GLN   A O   
713  C  CB  . GLN   A 89  ? 0.1539 0.1877 0.2369 -0.0048 -0.0012 -0.0166 95  GLN   A CB  
714  C  CG  . GLN   A 89  ? 0.1492 0.1798 0.2161 -0.0030 -0.0023 -0.0142 95  GLN   A CG  
715  C  CD  . GLN   A 89  ? 0.1708 0.1994 0.2310 -0.0038 0.0008  -0.0071 95  GLN   A CD  
716  O  OE1 . GLN   A 89  ? 0.1634 0.1908 0.2288 -0.0055 0.0042  -0.0029 95  GLN   A OE1 
717  N  NE2 . GLN   A 89  ? 0.1516 0.1792 0.1996 -0.0023 -0.0003 -0.0058 95  GLN   A NE2 
718  N  N   . SER   A 90  ? 0.1336 0.1661 0.2067 0.0021  -0.0128 -0.0321 96  SER   A N   
719  C  CA  . SER   A 90  ? 0.1481 0.1798 0.2097 0.0068  -0.0175 -0.0370 96  SER   A CA  
720  C  C   . SER   A 90  ? 0.1606 0.1896 0.2061 0.0086  -0.0158 -0.0320 96  SER   A C   
721  O  O   . SER   A 90  ? 0.1721 0.1996 0.2152 0.0061  -0.0116 -0.0256 96  SER   A O   
722  C  CB  . SER   A 90  ? 0.1715 0.1999 0.2302 0.0094  -0.0200 -0.0420 96  SER   A CB  
723  O  OG  . SER   A 90  ? 0.1981 0.2224 0.2518 0.0082  -0.0156 -0.0372 96  SER   A OG  
724  N  N   . HIS   A 91  ? 0.1619 0.1899 0.1964 0.0132  -0.0193 -0.0352 97  HIS   A N   
725  C  CA  . HIS   A 91  ? 0.1627 0.1869 0.1820 0.0153  -0.0174 -0.0311 97  HIS   A CA  
726  C  C   . HIS   A 91  ? 0.1533 0.1794 0.1741 0.0123  -0.0145 -0.0256 97  HIS   A C   
727  O  O   . HIS   A 91  ? 0.1572 0.1800 0.1694 0.0120  -0.0117 -0.0210 97  HIS   A O   
728  C  CB  . HIS   A 91  ? 0.1878 0.2065 0.1988 0.0156  -0.0139 -0.0282 97  HIS   A CB  
729  C  CG  . HIS   A 91  ? 0.2027 0.2182 0.2090 0.0195  -0.0160 -0.0335 97  HIS   A CG  
730  N  ND1 . HIS   A 91  ? 0.2554 0.2658 0.2460 0.0253  -0.0170 -0.0352 97  HIS   A ND1 
731  C  CD2 . HIS   A 91  ? 0.2141 0.2302 0.2287 0.0188  -0.0171 -0.0374 97  HIS   A CD2 
732  C  CE1 . HIS   A 91  ? 0.2628 0.2709 0.2515 0.0283  -0.0189 -0.0403 97  HIS   A CE1 
733  N  NE2 . HIS   A 91  ? 0.2424 0.2538 0.2457 0.0244  -0.0192 -0.0420 97  HIS   A NE2 
734  N  N   . LEU   A 92  ? 0.1511 0.1825 0.1831 0.0105  -0.0152 -0.0266 98  LEU   A N   
735  C  CA  . LEU   A 92  ? 0.1466 0.1796 0.1800 0.0082  -0.0121 -0.0218 98  LEU   A CA  
736  C  C   . LEU   A 92  ? 0.1496 0.1846 0.1792 0.0113  -0.0146 -0.0239 98  LEU   A C   
737  O  O   . LEU   A 92  ? 0.1457 0.1837 0.1799 0.0138  -0.0188 -0.0295 98  LEU   A O   
738  C  CB  . LEU   A 92  ? 0.1426 0.1793 0.1911 0.0045  -0.0096 -0.0209 98  LEU   A CB  
739  C  CG  . LEU   A 92  ? 0.1702 0.2074 0.2190 0.0025  -0.0052 -0.0152 98  LEU   A CG  
740  C  CD1 . LEU   A 92  ? 0.1872 0.2197 0.2252 0.0017  -0.0032 -0.0097 98  LEU   A CD1 
741  C  CD2 . LEU   A 92  ? 0.1839 0.2234 0.2476 -0.0005 -0.0015 -0.0140 98  LEU   A CD2 
742  N  N   . MET   A 93  ? 0.1425 0.1756 0.1642 0.0112  -0.0123 -0.0196 99  MET   A N   
743  C  CA  . MET   A 93  ? 0.1425 0.1764 0.1594 0.0142  -0.0140 -0.0208 99  MET   A CA  
744  C  C   . MET   A 93  ? 0.1540 0.1905 0.1755 0.0121  -0.0106 -0.0176 99  MET   A C   
745  O  O   . MET   A 93  ? 0.1580 0.1918 0.1758 0.0097  -0.0072 -0.0129 99  MET   A O   
746  C  CB  . MET   A 93  ? 0.1541 0.1818 0.1557 0.0167  -0.0138 -0.0186 99  MET   A CB  
747  C  CG  . MET   A 93  ? 0.1958 0.2195 0.1900 0.0199  -0.0160 -0.0212 99  MET   A CG  
748  S  SD  . MET   A 93  ? 0.2270 0.2419 0.2047 0.0221  -0.0133 -0.0172 99  MET   A SD  
749  C  CE  . MET   A 93  ? 0.2430 0.2573 0.2252 0.0163  -0.0086 -0.0121 99  MET   A CE  
750  N  N   . LEU   A 94  ? 0.1417 0.1833 0.1716 0.0132  -0.0113 -0.0203 100 LEU   A N   
751  C  CA  . LEU   A 94  ? 0.1453 0.1888 0.1790 0.0116  -0.0068 -0.0171 100 LEU   A CA  
752  C  C   . LEU   A 94  ? 0.1524 0.1949 0.1777 0.0147  -0.0074 -0.0169 100 LEU   A C   
753  O  O   . LEU   A 94  ? 0.1516 0.1945 0.1740 0.0184  -0.0117 -0.0206 100 LEU   A O   
754  C  CB  . LEU   A 94  ? 0.1589 0.2091 0.2106 0.0104  -0.0054 -0.0198 100 LEU   A CB  
755  C  CG  . LEU   A 94  ? 0.1961 0.2474 0.2595 0.0070  -0.0037 -0.0199 100 LEU   A CG  
756  C  CD1 . LEU   A 94  ? 0.2085 0.2658 0.2914 0.0052  -0.0002 -0.0214 100 LEU   A CD1 
757  C  CD2 . LEU   A 94  ? 0.2103 0.2565 0.2668 0.0043  0.0005  -0.0136 100 LEU   A CD2 
758  N  N   . ALA   A 95  ? 0.1408 0.1819 0.1628 0.0136  -0.0031 -0.0130 101 ALA   A N   
759  C  CA  . ALA   A 95  ? 0.1416 0.1816 0.1566 0.0163  -0.0028 -0.0128 101 ALA   A CA  
760  C  C   . ALA   A 95  ? 0.1419 0.1834 0.1604 0.0153  0.0028  -0.0100 101 ALA   A C   
761  O  O   . ALA   A 95  ? 0.1413 0.1824 0.1629 0.0126  0.0065  -0.0069 101 ALA   A O   
762  C  CB  . ALA   A 95  ? 0.1615 0.1944 0.1617 0.0168  -0.0037 -0.0104 101 ALA   A CB  
763  N  N   . VAL   A 96  ? 0.1313 0.1738 0.1483 0.0180  0.0038  -0.0108 102 VAL   A N   
764  C  CA  . VAL   A 96  ? 0.1311 0.1736 0.1481 0.0179  0.0099  -0.0080 102 VAL   A CA  
765  C  C   . VAL   A 96  ? 0.1682 0.2034 0.1690 0.0180  0.0102  -0.0047 102 VAL   A C   
766  O  O   . VAL   A 96  ? 0.1821 0.2135 0.1736 0.0199  0.0070  -0.0059 102 VAL   A O   
767  C  CB  . VAL   A 96  ? 0.1428 0.1895 0.1657 0.0210  0.0108  -0.0108 102 VAL   A CB  
768  C  CG1 . VAL   A 96  ? 0.1481 0.1939 0.1687 0.0218  0.0179  -0.0077 102 VAL   A CG1 
769  C  CG2 . VAL   A 96  ? 0.1600 0.2148 0.2016 0.0208  0.0094  -0.0149 102 VAL   A CG2 
770  N  N   . GLY   A 97  ? 0.1767 0.2094 0.1744 0.0164  0.0138  -0.0009 103 GLY   A N   
771  C  CA  . GLY   A 97  ? 0.1885 0.2147 0.1720 0.0169  0.0132  0.0014  103 GLY   A CA  
772  C  C   . GLY   A 97  ? 0.1829 0.2069 0.1640 0.0157  0.0166  0.0055  103 GLY   A C   
773  O  O   . GLY   A 97  ? 0.1813 0.2081 0.1721 0.0140  0.0196  0.0071  103 GLY   A O   
774  N  N   . HIS   A 98  ? 0.1786 0.1970 0.1466 0.0173  0.0160  0.0071  104 HIS   A N   
775  C  CA  . HIS   A 98  ? 0.1787 0.1936 0.1411 0.0176  0.0184  0.0112  104 HIS   A CA  
776  C  C   . HIS   A 98  ? 0.1786 0.1924 0.1422 0.0152  0.0143  0.0122  104 HIS   A C   
777  O  O   . HIS   A 98  ? 0.1752 0.1880 0.1370 0.0141  0.0089  0.0099  104 HIS   A O   
778  C  CB  . HIS   A 98  ? 0.1862 0.1953 0.1329 0.0212  0.0183  0.0117  104 HIS   A CB  
779  C  CG  . HIS   A 98  ? 0.1906 0.1950 0.1285 0.0229  0.0201  0.0159  104 HIS   A CG  
780  N  ND1 . HIS   A 98  ? 0.2074 0.2114 0.1468 0.0241  0.0279  0.0203  104 HIS   A ND1 
781  C  CD2 . HIS   A 98  ? 0.2139 0.2139 0.1427 0.0238  0.0148  0.0163  104 HIS   A CD2 
782  C  CE1 . HIS   A 98  ? 0.2278 0.2261 0.1565 0.0263  0.0273  0.0238  104 HIS   A CE1 
783  N  NE2 . HIS   A 98  ? 0.2280 0.2243 0.1503 0.0262  0.0188  0.0211  104 HIS   A NE2 
784  N  N   . SER   A 99  ? 0.1803 0.1934 0.1462 0.0147  0.0175  0.0160  105 SER   A N   
785  C  CA  . SER   A 99  ? 0.1940 0.2053 0.1599 0.0133  0.0141  0.0175  105 SER   A CA  
786  C  C   . SER   A 99  ? 0.2171 0.2250 0.1802 0.0148  0.0188  0.0228  105 SER   A C   
787  O  O   . SER   A 99  ? 0.2426 0.2509 0.2089 0.0155  0.0258  0.0253  105 SER   A O   
788  C  CB  . SER   A 99  ? 0.2216 0.2371 0.2001 0.0098  0.0121  0.0154  105 SER   A CB  
789  O  OG  . SER   A 99  ? 0.2706 0.2891 0.2603 0.0085  0.0170  0.0168  105 SER   A OG  
790  N  N   . GLU   A 100 ? 0.2094 0.2136 0.1661 0.0157  0.0151  0.0246  106 GLU   A N   
791  C  CA  . GLU   A 100 ? 0.2173 0.2172 0.1700 0.0176  0.0178  0.0299  106 GLU   A CA  
792  C  C   . GLU   A 100 ? 0.2258 0.2269 0.1864 0.0151  0.0134  0.0297  106 GLU   A C   
793  O  O   . GLU   A 100 ? 0.2294 0.2337 0.1949 0.0127  0.0081  0.0256  106 GLU   A O   
794  C  CB  . GLU   A 100 ? 0.2521 0.2455 0.1862 0.0229  0.0158  0.0315  106 GLU   A CB  
795  C  CG  . GLU   A 100 ? 0.2919 0.2835 0.2179 0.0258  0.0214  0.0320  106 GLU   A CG  
796  C  CD  . GLU   A 100 ? 0.3257 0.3107 0.2318 0.0316  0.0188  0.0321  106 GLU   A CD  
797  O  OE1 . GLU   A 100 ? 0.3304 0.3100 0.2262 0.0351  0.0162  0.0350  106 GLU   A OE1 
798  O  OE2 . GLU   A 100 ? 0.3107 0.2955 0.2109 0.0331  0.0191  0.0291  106 GLU   A OE2 
799  N  N   . PRO   A 101 ? 0.2421 0.2405 0.2050 0.0156  0.0161  0.0343  107 PRO   A N   
800  C  CA  . PRO   A 101 ? 0.2373 0.2372 0.2092 0.0132  0.0123  0.0337  107 PRO   A CA  
801  C  C   . PRO   A 101 ? 0.2387 0.2393 0.2076 0.0134  0.0039  0.0303  107 PRO   A C   
802  O  O   . PRO   A 101 ? 0.2387 0.2430 0.2173 0.0103  0.0011  0.0272  107 PRO   A O   
803  C  CB  . PRO   A 101 ? 0.2481 0.2425 0.2176 0.0156  0.0162  0.0399  107 PRO   A CB  
804  C  CG  . PRO   A 101 ? 0.2605 0.2528 0.2284 0.0167  0.0253  0.0434  107 PRO   A CG  
805  C  CD  . PRO   A 101 ? 0.2439 0.2372 0.2022 0.0183  0.0239  0.0403  107 PRO   A CD  
806  N  N   . GLY   A 102 ? 0.2346 0.2313 0.1903 0.0173  0.0001  0.0307  108 GLY   A N   
807  C  CA  . GLY   A 102 ? 0.2221 0.2195 0.1762 0.0177  -0.0081 0.0270  108 GLY   A CA  
808  C  C   . GLY   A 102 ? 0.2006 0.2019 0.1600 0.0145  -0.0103 0.0217  108 GLY   A C   
809  O  O   . GLY   A 102 ? 0.2109 0.2133 0.1731 0.0137  -0.0159 0.0184  108 GLY   A O   
810  N  N   . ASP   A 103 ? 0.1909 0.1942 0.1523 0.0128  -0.0057 0.0208  109 ASP   A N   
811  C  CA  . ASP   A 103 ? 0.1688 0.1748 0.1340 0.0105  -0.0073 0.0164  109 ASP   A CA  
812  C  C   . ASP   A 103 ? 0.1601 0.1695 0.1371 0.0070  -0.0073 0.0148  109 ASP   A C   
813  O  O   . ASP   A 103 ? 0.1577 0.1682 0.1371 0.0055  -0.0087 0.0117  109 ASP   A O   
814  C  CB  . ASP   A 103 ? 0.1847 0.1914 0.1473 0.0108  -0.0031 0.0156  109 ASP   A CB  
815  C  CG  . ASP   A 103 ? 0.2114 0.2143 0.1612 0.0144  -0.0037 0.0156  109 ASP   A CG  
816  O  OD1 . ASP   A 103 ? 0.2163 0.2168 0.1605 0.0157  -0.0092 0.0135  109 ASP   A OD1 
817  O  OD2 . ASP   A 103 ? 0.2214 0.2240 0.1678 0.0160  0.0014  0.0171  109 ASP   A OD2 
818  N  N   . CYS   A 104 ? 0.1577 0.1680 0.1416 0.0060  -0.0055 0.0171  110 CYS   A N   
819  C  CA  . CYS   A 104 ? 0.1601 0.1731 0.1541 0.0034  -0.0053 0.0153  110 CYS   A CA  
820  C  C   . CYS   A 104 ? 0.1593 0.1723 0.1552 0.0026  -0.0093 0.0131  110 CYS   A C   
821  O  O   . CYS   A 104 ? 0.1690 0.1805 0.1625 0.0040  -0.0130 0.0137  110 CYS   A O   
822  C  CB  . CYS   A 104 ? 0.1664 0.1796 0.1673 0.0028  -0.0032 0.0177  110 CYS   A CB  
823  S  SG  . CYS   A 104 ? 0.1939 0.2080 0.1987 0.0024  0.0027  0.0193  110 CYS   A SG  
824  N  N   . GLY   A 105 ? 0.1350 0.1493 0.1349 0.0010  -0.0086 0.0106  111 GLY   A N   
825  C  CA  . GLY   A 105 ? 0.1550 0.1689 0.1584 0.0000  -0.0106 0.0087  111 GLY   A CA  
826  C  C   . GLY   A 105 ? 0.1648 0.1770 0.1637 0.0000  -0.0113 0.0066  111 GLY   A C   
827  O  O   . GLY   A 105 ? 0.1669 0.1783 0.1700 -0.0012 -0.0113 0.0051  111 GLY   A O   
828  N  N   . GLY   A 106 ? 0.1656 0.1767 0.1567 0.0014  -0.0111 0.0066  112 GLY   A N   
829  C  CA  . GLY   A 106 ? 0.1545 0.1635 0.1411 0.0018  -0.0116 0.0045  112 GLY   A CA  
830  C  C   . GLY   A 106 ? 0.1485 0.1571 0.1369 0.0011  -0.0086 0.0036  112 GLY   A C   
831  O  O   . GLY   A 106 ? 0.1535 0.1640 0.1428 0.0014  -0.0065 0.0039  112 GLY   A O   
832  N  N   . ILE   A 107 ? 0.1402 0.1459 0.1292 0.0005  -0.0083 0.0022  113 ILE   A N   
833  C  CA  . ILE   A 107 ? 0.1402 0.1439 0.1287 0.0008  -0.0051 0.0020  113 ILE   A CA  
834  C  C   . ILE   A 107 ? 0.1471 0.1493 0.1280 0.0030  -0.0043 0.0013  113 ILE   A C   
835  O  O   . ILE   A 107 ? 0.1639 0.1646 0.1407 0.0038  -0.0057 0.0006  113 ILE   A O   
836  C  CB  . ILE   A 107 ? 0.1599 0.1602 0.1532 -0.0007 -0.0037 0.0016  113 ILE   A CB  
837  C  CG1 . ILE   A 107 ? 0.1744 0.1769 0.1769 -0.0024 -0.0032 0.0021  113 ILE   A CG1 
838  C  CG2 . ILE   A 107 ? 0.1794 0.1748 0.1684 0.0005  0.0002  0.0018  113 ILE   A CG2 
839  C  CD1 . ILE   A 107 ? 0.1963 0.1961 0.2072 -0.0044 -0.0013 0.0016  113 ILE   A CD1 
840  N  N   . LEU   A 108 ? 0.1395 0.1420 0.1188 0.0045  -0.0025 0.0012  114 LEU   A N   
841  C  CA  . LEU   A 108 ? 0.1374 0.1382 0.1101 0.0074  -0.0021 0.0003  114 LEU   A CA  
842  C  C   . LEU   A 108 ? 0.1578 0.1526 0.1271 0.0086  0.0006  0.0008  114 LEU   A C   
843  O  O   . LEU   A 108 ? 0.1627 0.1568 0.1339 0.0084  0.0026  0.0013  114 LEU   A O   
844  C  CB  . LEU   A 108 ? 0.1505 0.1555 0.1241 0.0091  -0.0028 -0.0009 114 LEU   A CB  
845  C  CG  . LEU   A 108 ? 0.1616 0.1654 0.1294 0.0129  -0.0033 -0.0026 114 LEU   A CG  
846  C  CD1 . LEU   A 108 ? 0.1663 0.1701 0.1315 0.0140  -0.0040 -0.0029 114 LEU   A CD1 
847  C  CD2 . LEU   A 108 ? 0.1900 0.1984 0.1613 0.0144  -0.0050 -0.0049 114 LEU   A CD2 
848  N  N   . ARG   A 109 ? 0.1611 0.1511 0.1254 0.0100  0.0014  0.0009  115 ARG   A N   
849  C  CA  . ARG   A 109 ? 0.1810 0.1638 0.1414 0.0114  0.0051  0.0022  115 ARG   A CA  
850  C  C   . ARG   A 109 ? 0.1892 0.1682 0.1403 0.0159  0.0051  0.0020  115 ARG   A C   
851  O  O   . ARG   A 109 ? 0.1904 0.1709 0.1399 0.0168  0.0026  0.0008  115 ARG   A O   
852  C  CB  . ARG   A 109 ? 0.2255 0.2040 0.1905 0.0087  0.0067  0.0027  115 ARG   A CB  
853  C  CG  . ARG   A 109 ? 0.3080 0.2898 0.2832 0.0046  0.0056  0.0023  115 ARG   A CG  
854  C  CD  . ARG   A 109 ? 0.3294 0.3068 0.3102 0.0023  0.0063  0.0016  115 ARG   A CD  
855  N  NE  . ARG   A 109 ? 0.3450 0.3157 0.3268 0.0026  0.0126  0.0037  115 ARG   A NE  
856  C  CZ  . ARG   A 109 ? 0.3302 0.3007 0.3206 0.0004  0.0162  0.0048  115 ARG   A CZ  
857  N  NH1 . ARG   A 109 ? 0.2837 0.2605 0.2837 -0.0023 0.0132  0.0034  115 ARG   A NH1 
858  N  NH2 . ARG   A 109 ? 0.3037 0.2672 0.2932 0.0014  0.0233  0.0074  115 ARG   A NH2 
859  N  N   . CYS   A 110 ? 0.1858 0.1588 0.1301 0.0192  0.0082  0.0034  116 CYS   A N   
860  C  CA  . CYS   A 110 ? 0.2030 0.1701 0.1373 0.0242  0.0085  0.0039  116 CYS   A CA  
861  C  C   . CYS   A 110 ? 0.2289 0.1859 0.1607 0.0242  0.0144  0.0070  116 CYS   A C   
862  O  O   . CYS   A 110 ? 0.2435 0.1995 0.1833 0.0199  0.0177  0.0081  116 CYS   A O   
863  C  CB  . CYS   A 110 ? 0.2229 0.1904 0.1494 0.0294  0.0069  0.0029  116 CYS   A CB  
864  S  SG  . CYS   A 110 ? 0.2154 0.1770 0.1371 0.0308  0.0121  0.0051  116 CYS   A SG  
865  N  N   . GLN   A 111 ? 0.2401 0.1890 0.1615 0.0292  0.0163  0.0086  117 GLN   A N   
866  C  CA  . GLN   A 111 ? 0.2674 0.2052 0.1865 0.0294  0.0231  0.0122  117 GLN   A CA  
867  C  C   . GLN   A 111 ? 0.2698 0.2033 0.1886 0.0292  0.0296  0.0151  117 GLN   A C   
868  O  O   . GLN   A 111 ? 0.2801 0.2054 0.2015 0.0279  0.0366  0.0182  117 GLN   A O   
869  C  CB  . GLN   A 111 ? 0.3086 0.2377 0.2148 0.0360  0.0239  0.0139  117 GLN   A CB  
870  C  CG  . GLN   A 111 ? 0.4005 0.3272 0.2930 0.0432  0.0232  0.0146  117 GLN   A CG  
871  C  CD  . GLN   A 111 ? 0.5300 0.4497 0.4095 0.0507  0.0219  0.0156  117 GLN   A CD  
872  O  OE1 . GLN   A 111 ? 0.5628 0.4882 0.4393 0.0544  0.0150  0.0123  117 GLN   A OE1 
873  N  NE2 . GLN   A 111 ? 0.5427 0.4494 0.4149 0.0532  0.0288  0.0202  117 GLN   A NE2 
874  N  N   . HIS   A 112 ? 0.2478 0.1862 0.1641 0.0307  0.0279  0.0140  118 HIS   A N   
875  C  CA  . HIS   A 112 ? 0.2592 0.1932 0.1735 0.0314  0.0342  0.0164  118 HIS   A CA  
876  C  C   . HIS   A 112 ? 0.2430 0.1836 0.1726 0.0249  0.0353  0.0155  118 HIS   A C   
877  O  O   . HIS   A 112 ? 0.2416 0.1785 0.1730 0.0246  0.0420  0.0178  118 HIS   A O   
878  C  CB  . HIS   A 112 ? 0.2651 0.1989 0.1661 0.0379  0.0320  0.0153  118 HIS   A CB  
879  C  CG  . HIS   A 112 ? 0.2984 0.2260 0.1839 0.0454  0.0297  0.0156  118 HIS   A CG  
880  N  ND1 . HIS   A 112 ? 0.3231 0.2578 0.2065 0.0481  0.0210  0.0114  118 HIS   A ND1 
881  C  CD2 . HIS   A 112 ? 0.3341 0.2491 0.2064 0.0510  0.0353  0.0198  118 HIS   A CD2 
882  C  CE1 . HIS   A 112 ? 0.3436 0.2706 0.2131 0.0552  0.0205  0.0127  118 HIS   A CE1 
883  N  NE2 . HIS   A 112 ? 0.3500 0.2645 0.2113 0.0574  0.0290  0.0180  118 HIS   A NE2 
884  N  N   . GLY   A 113 ? 0.2221 0.1724 0.1621 0.0205  0.0290  0.0124  119 GLY   A N   
885  C  CA  . GLY   A 113 ? 0.2159 0.1725 0.1698 0.0151  0.0287  0.0114  119 GLY   A CA  
886  C  C   . GLY   A 113 ? 0.1907 0.1573 0.1484 0.0135  0.0215  0.0083  119 GLY   A C   
887  O  O   . GLY   A 113 ? 0.2032 0.1727 0.1560 0.0153  0.0167  0.0066  119 GLY   A O   
888  N  N   . VAL   A 114 ? 0.1773 0.1491 0.1448 0.0102  0.0213  0.0077  120 VAL   A N   
889  C  CA  . VAL   A 114 ? 0.1713 0.1517 0.1433 0.0086  0.0155  0.0055  120 VAL   A CA  
890  C  C   . VAL   A 114 ? 0.1759 0.1580 0.1405 0.0123  0.0138  0.0041  120 VAL   A C   
891  O  O   . VAL   A 114 ? 0.1787 0.1577 0.1392 0.0147  0.0170  0.0045  120 VAL   A O   
892  C  CB  . VAL   A 114 ? 0.1794 0.1638 0.1637 0.0048  0.0160  0.0055  120 VAL   A CB  
893  C  CG1 . VAL   A 114 ? 0.1757 0.1675 0.1633 0.0039  0.0109  0.0040  120 VAL   A CG1 
894  C  CG2 . VAL   A 114 ? 0.1750 0.1589 0.1685 0.0013  0.0159  0.0056  120 VAL   A CG2 
895  N  N   . VAL   A 115 ? 0.1735 0.1607 0.1376 0.0127  0.0087  0.0021  121 VAL   A N   
896  C  CA  . VAL   A 115 ? 0.1796 0.1697 0.1401 0.0157  0.0058  -0.0003 121 VAL   A CA  
897  C  C   . VAL   A 115 ? 0.1729 0.1695 0.1426 0.0129  0.0038  -0.0016 121 VAL   A C   
898  O  O   . VAL   A 115 ? 0.1719 0.1696 0.1412 0.0147  0.0030  -0.0036 121 VAL   A O   
899  C  CB  . VAL   A 115 ? 0.1974 0.1892 0.1540 0.0179  0.0022  -0.0018 121 VAL   A CB  
900  C  CG1 . VAL   A 115 ? 0.2001 0.1968 0.1575 0.0202  -0.0017 -0.0053 121 VAL   A CG1 
901  C  CG2 . VAL   A 115 ? 0.2047 0.1892 0.1511 0.0216  0.0040  -0.0006 121 VAL   A CG2 
902  N  N   . GLY   A 116 ? 0.1590 0.1595 0.1361 0.0093  0.0025  -0.0007 122 GLY   A N   
903  C  CA  . GLY   A 116 ? 0.1584 0.1641 0.1436 0.0070  0.0009  -0.0011 122 GLY   A CA  
904  C  C   . GLY   A 116 ? 0.1525 0.1606 0.1425 0.0042  -0.0003 0.0005  122 GLY   A C   
905  O  O   . GLY   A 116 ? 0.1524 0.1583 0.1406 0.0035  -0.0003 0.0014  122 GLY   A O   
906  N  N   . ILE   A 117 ? 0.1452 0.1571 0.1412 0.0028  -0.0015 0.0009  123 ILE   A N   
907  C  CA  . ILE   A 117 ? 0.1324 0.1456 0.1306 0.0012  -0.0028 0.0028  123 ILE   A CA  
908  C  C   . ILE   A 117 ? 0.1225 0.1387 0.1219 0.0014  -0.0032 0.0031  123 ILE   A C   
909  O  O   . ILE   A 117 ? 0.1262 0.1444 0.1296 0.0016  -0.0026 0.0019  123 ILE   A O   
910  C  CB  . ILE   A 117 ? 0.1477 0.1613 0.1523 -0.0005 -0.0031 0.0041  123 ILE   A CB  
911  C  CG1 . ILE   A 117 ? 0.1561 0.1712 0.1661 -0.0006 -0.0019 0.0036  123 ILE   A CG1 
912  C  CG2 . ILE   A 117 ? 0.1660 0.1771 0.1720 -0.0012 -0.0024 0.0039  123 ILE   A CG2 
913  C  CD1 . ILE   A 117 ? 0.1783 0.1940 0.1955 -0.0019 -0.0024 0.0052  123 ILE   A CD1 
914  N  N   . VAL   A 118 ? 0.1145 0.1306 0.1110 0.0015  -0.0038 0.0047  124 VAL   A N   
915  C  CA  . VAL   A 118 ? 0.1264 0.1445 0.1242 0.0018  -0.0025 0.0059  124 VAL   A CA  
916  C  C   . VAL   A 118 ? 0.1334 0.1526 0.1385 0.0006  -0.0015 0.0074  124 VAL   A C   
917  O  O   . VAL   A 118 ? 0.1278 0.1457 0.1341 0.0001  -0.0026 0.0089  124 VAL   A O   
918  C  CB  . VAL   A 118 ? 0.1345 0.1509 0.1258 0.0029  -0.0028 0.0079  124 VAL   A CB  
919  C  CG1 . VAL   A 118 ? 0.1427 0.1601 0.1353 0.0035  0.0003  0.0103  124 VAL   A CG1 
920  C  CG2 . VAL   A 118 ? 0.1503 0.1652 0.1350 0.0042  -0.0035 0.0061  124 VAL   A CG2 
921  N  N   . SER   A 119 ? 0.1294 0.1509 0.1404 0.0004  0.0004  0.0067  125 SER   A N   
922  C  CA  . SER   A 119 ? 0.1290 0.1509 0.1482 -0.0009 0.0017  0.0079  125 SER   A CA  
923  C  C   . SER   A 119 ? 0.1515 0.1743 0.1755 -0.0011 0.0053  0.0099  125 SER   A C   
924  O  O   . SER   A 119 ? 0.1667 0.1880 0.1950 -0.0017 0.0072  0.0128  125 SER   A O   
925  C  CB  . SER   A 119 ? 0.1541 0.1774 0.1790 -0.0013 0.0007  0.0040  125 SER   A CB  
926  O  OG  . SER   A 119 ? 0.1624 0.1857 0.1960 -0.0025 0.0018  0.0042  125 SER   A OG  
927  N  N   . THR   A 120 ? 0.1457 0.1707 0.1701 -0.0005 0.0067  0.0086  126 THR   A N   
928  C  CA  . THR   A 120 ? 0.1487 0.1746 0.1798 -0.0009 0.0115  0.0106  126 THR   A CA  
929  C  C   . THR   A 120 ? 0.1645 0.1907 0.1891 0.0009  0.0135  0.0115  126 THR   A C   
930  O  O   . THR   A 120 ? 0.1566 0.1829 0.1736 0.0022  0.0105  0.0095  126 THR   A O   
931  C  CB  . THR   A 120 ? 0.1726 0.2028 0.2182 -0.0024 0.0117  0.0063  126 THR   A CB  
932  O  OG1 . THR   A 120 ? 0.1901 0.2238 0.2356 -0.0011 0.0092  0.0017  126 THR   A OG1 
933  C  CG2 . THR   A 120 ? 0.1718 0.2017 0.2233 -0.0036 0.0093  0.0040  126 THR   A CG2 
934  N  N   . GLY   A 121 ? 0.1654 0.1916 0.1942 0.0011  0.0192  0.0144  127 GLY   A N   
935  C  CA  . GLY   A 121 ? 0.1822 0.2089 0.2065 0.0030  0.0221  0.0149  127 GLY   A CA  
936  C  C   . GLY   A 121 ? 0.1951 0.2216 0.2264 0.0030  0.0300  0.0183  127 GLY   A C   
937  O  O   . GLY   A 121 ? 0.1930 0.2181 0.2321 0.0014  0.0335  0.0210  127 GLY   A O   
938  N  N   . GLY   A 122 ? 0.2164 0.2437 0.2445 0.0049  0.0335  0.0186  128 GLY   A N   
939  C  CA  . GLY   A 122 ? 0.2380 0.2642 0.2709 0.0056  0.0427  0.0227  128 GLY   A CA  
940  C  C   . GLY   A 122 ? 0.2431 0.2747 0.2842 0.0062  0.0455  0.0195  128 GLY   A C   
941  O  O   . GLY   A 122 ? 0.2443 0.2818 0.2946 0.0051  0.0403  0.0136  128 GLY   A O   
942  N  N   . ASN   A 123 ? 0.2409 0.2701 0.2784 0.0085  0.0537  0.0235  129 ASN   A N   
943  C  CA  . ASN   A 123 ? 0.2483 0.2826 0.2953 0.0093  0.0581  0.0210  129 ASN   A CA  
944  C  C   . ASN   A 123 ? 0.2298 0.2681 0.2728 0.0108  0.0507  0.0153  129 ASN   A C   
945  O  O   . ASN   A 123 ? 0.2352 0.2804 0.2924 0.0106  0.0503  0.0107  129 ASN   A O   
946  C  CB  . ASN   A 123 ? 0.2809 0.3214 0.3534 0.0060  0.0622  0.0191  129 ASN   A CB  
947  C  CG  . ASN   A 123 ? 0.3826 0.4179 0.4594 0.0049  0.0718  0.0259  129 ASN   A CG  
948  O  OD1 . ASN   A 123 ? 0.4215 0.4503 0.4857 0.0079  0.0797  0.0322  129 ASN   A OD1 
949  N  ND2 . ASN   A 123 ? 0.4060 0.4430 0.4991 0.0011  0.0713  0.0248  129 ASN   A ND2 
950  N  N   . GLY   A 124 ? 0.2053 0.2388 0.2294 0.0127  0.0451  0.0155  130 GLY   A N   
951  C  CA  . GLY   A 124 ? 0.1986 0.2338 0.2170 0.0144  0.0390  0.0109  130 GLY   A CA  
952  C  C   . GLY   A 124 ? 0.1892 0.2281 0.2140 0.0126  0.0308  0.0060  130 GLY   A C   
953  O  O   . GLY   A 124 ? 0.2018 0.2422 0.2237 0.0143  0.0262  0.0022  130 GLY   A O   
954  N  N   . LEU   A 125 ? 0.1698 0.2091 0.2009 0.0098  0.0289  0.0063  131 LEU   A N   
955  C  CA  . LEU   A 125 ? 0.1729 0.2142 0.2070 0.0087  0.0214  0.0019  131 LEU   A CA  
956  C  C   . LEU   A 125 ? 0.1905 0.2264 0.2132 0.0078  0.0182  0.0043  131 LEU   A C   
957  O  O   . LEU   A 125 ? 0.2163 0.2483 0.2346 0.0072  0.0215  0.0089  131 LEU   A O   
958  C  CB  . LEU   A 125 ? 0.1801 0.2266 0.2327 0.0063  0.0216  -0.0007 131 LEU   A CB  
959  C  CG  . LEU   A 125 ? 0.2150 0.2686 0.2835 0.0070  0.0228  -0.0049 131 LEU   A CG  
960  C  CD1 . LEU   A 125 ? 0.2283 0.2862 0.3168 0.0041  0.0239  -0.0073 131 LEU   A CD1 
961  C  CD2 . LEU   A 125 ? 0.2083 0.2644 0.2734 0.0099  0.0151  -0.0105 131 LEU   A CD2 
962  N  N   . VAL   A 126 ? 0.1485 0.1837 0.1667 0.0079  0.0122  0.0015  132 VAL   A N   
963  C  CA  . VAL   A 126 ? 0.1421 0.1732 0.1534 0.0068  0.0095  0.0030  132 VAL   A CA  
964  C  C   . VAL   A 126 ? 0.1395 0.1725 0.1564 0.0060  0.0054  -0.0007 132 VAL   A C   
965  O  O   . VAL   A 126 ? 0.1428 0.1781 0.1611 0.0077  0.0027  -0.0045 132 VAL   A O   
966  C  CB  . VAL   A 126 ? 0.1654 0.1919 0.1627 0.0082  0.0074  0.0040  132 VAL   A CB  
967  C  CG1 . VAL   A 126 ? 0.1872 0.2140 0.1810 0.0102  0.0049  0.0007  132 VAL   A CG1 
968  C  CG2 . VAL   A 126 ? 0.1682 0.1915 0.1617 0.0068  0.0045  0.0051  132 VAL   A CG2 
969  N  N   . GLY   A 127 ? 0.1385 0.1703 0.1580 0.0041  0.0050  0.0005  133 GLY   A N   
970  C  CA  . GLY   A 127 ? 0.1311 0.1638 0.1546 0.0038  0.0016  -0.0031 133 GLY   A CA  
971  C  C   . GLY   A 127 ? 0.1397 0.1684 0.1551 0.0036  -0.0003 -0.0019 133 GLY   A C   
972  O  O   . GLY   A 127 ? 0.1400 0.1662 0.1526 0.0024  0.0009  0.0016  133 GLY   A O   
973  N  N   . PHE   A 128 ? 0.1307 0.1583 0.1425 0.0051  -0.0031 -0.0049 134 PHE   A N   
974  C  CA  . PHE   A 128 ? 0.1363 0.1598 0.1415 0.0050  -0.0037 -0.0039 134 PHE   A CA  
975  C  C   . PHE   A 128 ? 0.1510 0.1744 0.1596 0.0053  -0.0047 -0.0064 134 PHE   A C   
976  O  O   . PHE   A 128 ? 0.1402 0.1652 0.1503 0.0074  -0.0067 -0.0104 134 PHE   A O   
977  C  CB  . PHE   A 128 ? 0.1346 0.1551 0.1303 0.0074  -0.0046 -0.0046 134 PHE   A CB  
978  C  CG  . PHE   A 128 ? 0.1394 0.1596 0.1313 0.0079  -0.0041 -0.0033 134 PHE   A CG  
979  C  CD1 . PHE   A 128 ? 0.1490 0.1667 0.1372 0.0066  -0.0034 -0.0006 134 PHE   A CD1 
980  C  CD2 . PHE   A 128 ? 0.1468 0.1695 0.1392 0.0100  -0.0046 -0.0052 134 PHE   A CD2 
981  C  CE1 . PHE   A 128 ? 0.1561 0.1729 0.1397 0.0075  -0.0031 0.0000  134 PHE   A CE1 
982  C  CE2 . PHE   A 128 ? 0.1600 0.1822 0.1486 0.0108  -0.0036 -0.0042 134 PHE   A CE2 
983  C  CZ  . PHE   A 128 ? 0.1458 0.1647 0.1292 0.0096  -0.0028 -0.0016 134 PHE   A CZ  
984  N  N   . ALA   A 129 ? 0.1470 0.1685 0.1565 0.0038  -0.0036 -0.0046 135 ALA   A N   
985  C  CA  . ALA   A 129 ? 0.1380 0.1584 0.1494 0.0043  -0.0038 -0.0067 135 ALA   A CA  
986  C  C   . ALA   A 129 ? 0.1379 0.1542 0.1395 0.0069  -0.0036 -0.0074 135 ALA   A C   
987  O  O   . ALA   A 129 ? 0.1376 0.1512 0.1355 0.0062  -0.0019 -0.0047 135 ALA   A O   
988  C  CB  . ALA   A 129 ? 0.1334 0.1531 0.1498 0.0021  -0.0023 -0.0041 135 ALA   A CB  
989  N  N   . ASP   A 130 ? 0.1350 0.1503 0.1324 0.0102  -0.0052 -0.0112 136 ASP   A N   
990  C  CA  . ASP   A 130 ? 0.1496 0.1596 0.1356 0.0137  -0.0042 -0.0113 136 ASP   A CA  
991  C  C   . ASP   A 130 ? 0.1639 0.1703 0.1492 0.0133  -0.0006 -0.0098 136 ASP   A C   
992  O  O   . ASP   A 130 ? 0.1643 0.1724 0.1562 0.0122  -0.0007 -0.0112 136 ASP   A O   
993  C  CB  . ASP   A 130 ? 0.1820 0.1916 0.1630 0.0185  -0.0077 -0.0161 136 ASP   A CB  
994  C  CG  . ASP   A 130 ? 0.2480 0.2508 0.2144 0.0234  -0.0066 -0.0159 136 ASP   A CG  
995  O  OD1 . ASP   A 130 ? 0.2286 0.2282 0.1898 0.0234  -0.0042 -0.0124 136 ASP   A OD1 
996  O  OD2 . ASP   A 130 ? 0.2851 0.2849 0.2450 0.0276  -0.0076 -0.0189 136 ASP   A OD2 
997  N  N   . VAL   A 131 ? 0.1517 0.1529 0.1299 0.0143  0.0030  -0.0072 137 VAL   A N   
998  C  CA  . VAL   A 131 ? 0.1722 0.1697 0.1503 0.0144  0.0075  -0.0060 137 VAL   A CA  
999  C  C   . VAL   A 131 ? 0.1863 0.1764 0.1509 0.0195  0.0107  -0.0059 137 VAL   A C   
1000 O  O   . VAL   A 131 ? 0.2060 0.1919 0.1689 0.0203  0.0159  -0.0044 137 VAL   A O   
1001 C  CB  . VAL   A 131 ? 0.1889 0.1869 0.1748 0.0103  0.0104  -0.0023 137 VAL   A CB  
1002 C  CG1 . VAL   A 131 ? 0.1800 0.1840 0.1766 0.0066  0.0072  -0.0020 137 VAL   A CG1 
1003 C  CG2 . VAL   A 131 ? 0.1915 0.1864 0.1730 0.0101  0.0116  -0.0001 137 VAL   A CG2 
1004 N  N   . ARG   A 132 ? 0.1840 0.1718 0.1386 0.0234  0.0082  -0.0070 138 ARG   A N   
1005 C  CA  . ARG   A 132 ? 0.1942 0.1736 0.1339 0.0290  0.0115  -0.0061 138 ARG   A CA  
1006 C  C   . ARG   A 132 ? 0.2217 0.1972 0.1531 0.0339  0.0123  -0.0087 138 ARG   A C   
1007 O  O   . ARG   A 132 ? 0.2418 0.2088 0.1608 0.0383  0.0176  -0.0067 138 ARG   A O   
1008 C  CB  . ARG   A 132 ? 0.1998 0.1777 0.1307 0.0328  0.0077  -0.0070 138 ARG   A CB  
1009 C  CG  . ARG   A 132 ? 0.2095 0.1892 0.1459 0.0290  0.0078  -0.0043 138 ARG   A CG  
1010 C  CD  . ARG   A 132 ? 0.2001 0.1793 0.1293 0.0330  0.0036  -0.0057 138 ARG   A CD  
1011 N  NE  . ARG   A 132 ? 0.1895 0.1770 0.1259 0.0325  -0.0029 -0.0102 138 ARG   A NE  
1012 C  CZ  . ARG   A 132 ? 0.2401 0.2300 0.1750 0.0354  -0.0076 -0.0126 138 ARG   A CZ  
1013 N  NH1 . ARG   A 132 ? 0.2277 0.2119 0.1524 0.0393  -0.0069 -0.0108 138 ARG   A NH1 
1014 N  NH2 . ARG   A 132 ? 0.2388 0.2368 0.1837 0.0342  -0.0124 -0.0166 138 ARG   A NH2 
1015 N  N   . ASP   A 133 ? 0.2189 0.1998 0.1566 0.0334  0.0076  -0.0134 139 ASP   A N   
1016 C  CA  . ASP   A 133 ? 0.2301 0.2070 0.1596 0.0384  0.0077  -0.0169 139 ASP   A CA  
1017 C  C   . ASP   A 133 ? 0.2385 0.2134 0.1724 0.0364  0.0145  -0.0147 139 ASP   A C   
1018 O  O   . ASP   A 133 ? 0.2618 0.2320 0.1872 0.0411  0.0162  -0.0172 139 ASP   A O   
1019 C  CB  . ASP   A 133 ? 0.2451 0.2280 0.1806 0.0390  -0.0003 -0.0236 139 ASP   A CB  
1020 C  CG  . ASP   A 133 ? 0.2747 0.2653 0.2290 0.0320  -0.0012 -0.0237 139 ASP   A CG  
1021 O  OD1 . ASP   A 133 ? 0.2566 0.2506 0.2192 0.0269  0.0003  -0.0195 139 ASP   A OD1 
1022 O  OD2 . ASP   A 133 ? 0.3001 0.2927 0.2603 0.0320  -0.0035 -0.0280 139 ASP   A OD2 
1023 N  N   . LEU   A 134 ? 0.2153 0.1937 0.1623 0.0302  0.0179  -0.0109 140 LEU   A N   
1024 C  CA  . LEU   A 134 ? 0.2011 0.1789 0.1556 0.0280  0.0238  -0.0091 140 LEU   A CA  
1025 C  C   . LEU   A 134 ? 0.2110 0.1809 0.1576 0.0304  0.0327  -0.0049 140 LEU   A C   
1026 O  O   . LEU   A 134 ? 0.2121 0.1824 0.1668 0.0264  0.0368  -0.0008 140 LEU   A O   
1027 C  CB  . LEU   A 134 ? 0.1961 0.1814 0.1685 0.0210  0.0224  -0.0072 140 LEU   A CB  
1028 C  CG  . LEU   A 134 ? 0.2048 0.1969 0.1851 0.0186  0.0152  -0.0103 140 LEU   A CG  
1029 C  CD1 . LEU   A 134 ? 0.1944 0.1921 0.1887 0.0129  0.0142  -0.0075 140 LEU   A CD1 
1030 C  CD2 . LEU   A 134 ? 0.2179 0.2102 0.1991 0.0208  0.0134  -0.0149 140 LEU   A CD2 
1031 N  N   . LEU   A 135 ? 0.2209 0.1828 0.1508 0.0373  0.0357  -0.0060 141 LEU   A N   
1032 C  CA  . LEU   A 135 ? 0.2453 0.1978 0.1653 0.0405  0.0454  -0.0012 141 LEU   A CA  
1033 C  C   . LEU   A 135 ? 0.2547 0.2070 0.1869 0.0370  0.0543  0.0020  141 LEU   A C   
1034 O  O   . LEU   A 135 ? 0.2718 0.2192 0.2052 0.0362  0.0625  0.0069  141 LEU   A O   
1035 C  CB  . LEU   A 135 ? 0.2597 0.2026 0.1568 0.0500  0.0469  -0.0029 141 LEU   A CB  
1036 C  CG  . LEU   A 135 ? 0.2875 0.2311 0.1732 0.0544  0.0368  -0.0074 141 LEU   A CG  
1037 C  CD1 . LEU   A 135 ? 0.3081 0.2409 0.1692 0.0650  0.0381  -0.0090 141 LEU   A CD1 
1038 C  CD2 . LEU   A 135 ? 0.3032 0.2488 0.1915 0.0517  0.0338  -0.0047 141 LEU   A CD2 
1039 N  N   . TRP   A 136 ? 0.2482 0.2059 0.1910 0.0349  0.0529  -0.0007 142 TRP   A N   
1040 C  CA  . TRP   A 136 ? 0.2565 0.2153 0.2129 0.0319  0.0605  0.0015  142 TRP   A CA  
1041 C  C   . TRP   A 136 ? 0.2573 0.2219 0.2323 0.0248  0.0608  0.0046  142 TRP   A C   
1042 O  O   . TRP   A 136 ? 0.2665 0.2312 0.2535 0.0226  0.0679  0.0070  142 TRP   A O   
1043 C  CB  . TRP   A 136 ? 0.2549 0.2179 0.2179 0.0319  0.0578  -0.0026 142 TRP   A CB  
1044 C  CG  . TRP   A 136 ? 0.2481 0.2196 0.2202 0.0281  0.0472  -0.0059 142 TRP   A CG  
1045 C  CD1 . TRP   A 136 ? 0.2569 0.2295 0.2215 0.0304  0.0393  -0.0105 142 TRP   A CD1 
1046 C  CD2 . TRP   A 136 ? 0.2385 0.2182 0.2292 0.0216  0.0438  -0.0047 142 TRP   A CD2 
1047 N  NE1 . TRP   A 136 ? 0.2538 0.2344 0.2322 0.0254  0.0326  -0.0117 142 TRP   A NE1 
1048 C  CE2 . TRP   A 136 ? 0.2413 0.2259 0.2342 0.0204  0.0351  -0.0080 142 TRP   A CE2 
1049 C  CE3 . TRP   A 136 ? 0.2338 0.2169 0.2401 0.0173  0.0472  -0.0015 142 TRP   A CE3 
1050 C  CZ2 . TRP   A 136 ? 0.2345 0.2263 0.2421 0.0153  0.0305  -0.0072 142 TRP   A CZ2 
1051 C  CZ3 . TRP   A 136 ? 0.2282 0.2188 0.2486 0.0126  0.0412  -0.0016 142 TRP   A CZ3 
1052 C  CH2 . TRP   A 136 ? 0.2296 0.2239 0.2495 0.0119  0.0334  -0.0040 142 TRP   A CH2 
1053 N  N   . LEU   A 137 ? 0.2402 0.2095 0.2182 0.0215  0.0530  0.0043  143 LEU   A N   
1054 C  CA  . LEU   A 137 ? 0.2543 0.2285 0.2484 0.0155  0.0523  0.0065  143 LEU   A CA  
1055 C  C   . LEU   A 137 ? 0.3058 0.2739 0.3019 0.0152  0.0616  0.0105  143 LEU   A C   
1056 O  O   . LEU   A 137 ? 0.2916 0.2634 0.3044 0.0104  0.0629  0.0116  143 LEU   A O   
1057 C  CB  . LEU   A 137 ? 0.2465 0.2248 0.2396 0.0133  0.0436  0.0056  143 LEU   A CB  
1058 C  CG  . LEU   A 137 ? 0.2439 0.2297 0.2424 0.0114  0.0353  0.0027  143 LEU   A CG  
1059 C  CD1 . LEU   A 137 ? 0.2517 0.2402 0.2474 0.0101  0.0286  0.0023  143 LEU   A CD1 
1060 C  CD2 . LEU   A 137 ? 0.2422 0.2339 0.2581 0.0074  0.0346  0.0030  143 LEU   A CD2 
1061 N  N   . ASP   A 138 ? 0.3615 0.3199 0.3408 0.0204  0.0679  0.0125  144 ASP   A N   
1062 C  CA  . ASP   A 138 ? 0.4326 0.3837 0.4137 0.0203  0.0783  0.0169  144 ASP   A CA  
1063 C  C   . ASP   A 138 ? 0.5068 0.4474 0.4721 0.0270  0.0886  0.0193  144 ASP   A C   
1064 O  O   . ASP   A 138 ? 0.5335 0.4644 0.4890 0.0299  0.0962  0.0233  144 ASP   A O   
1065 C  CB  . ASP   A 138 ? 0.4688 0.4171 0.4456 0.0193  0.0758  0.0186  144 ASP   A CB  
1066 C  CG  . ASP   A 138 ? 0.5395 0.4850 0.4961 0.0244  0.0694  0.0171  144 ASP   A CG  
1067 O  OD1 . ASP   A 138 ? 0.5547 0.5048 0.5129 0.0221  0.0612  0.0155  144 ASP   A OD1 
1068 O  OD2 . ASP   A 138 ? 0.5620 0.5010 0.5016 0.0309  0.0721  0.0170  144 ASP   A OD2 
1069 N  N   . GLU   A 139 ? 0.5357 0.4771 0.4973 0.0300  0.0891  0.0168  145 GLU   A N   
1070 C  CA  . GLU   A 139 ? 0.5801 0.5119 0.5239 0.0376  0.0973  0.0176  145 GLU   A CA  
1071 C  C   . GLU   A 139 ? 0.6132 0.5318 0.5427 0.0424  0.1089  0.0232  145 GLU   A C   
1072 O  O   . GLU   A 139 ? 0.6247 0.5413 0.5673 0.0386  0.1177  0.0275  145 GLU   A O   
1073 C  CB  . GLU   A 139 ? 0.6168 0.5514 0.5726 0.0368  0.1031  0.0166  145 GLU   A CB  
1074 C  CG  . GLU   A 139 ? 0.7132 0.6414 0.6497 0.0447  0.1053  0.0141  145 GLU   A CG  
1075 C  CD  . GLU   A 139 ? 0.8077 0.7404 0.7354 0.0466  0.0919  0.0080  145 GLU   A CD  
1076 O  OE1 . GLU   A 139 ? 0.8149 0.7562 0.7564 0.0430  0.0861  0.0042  145 GLU   A OE1 
1077 O  OE2 . GLU   A 139 ? 0.8478 0.7752 0.7558 0.0519  0.0874  0.0068  145 GLU   A OE2 
1078 N  N   . SER   B 1   ? 0.2711 0.2544 0.2415 -0.0041 -0.0331 -0.0075 7   SER   C N   
1079 C  CA  . SER   B 1   ? 0.2660 0.2519 0.2467 -0.0029 -0.0344 -0.0074 7   SER   C CA  
1080 C  C   . SER   B 1   ? 0.2522 0.2416 0.2392 -0.0019 -0.0329 -0.0064 7   SER   C C   
1081 O  O   . SER   B 1   ? 0.2602 0.2490 0.2436 -0.0023 -0.0324 -0.0054 7   SER   C O   
1082 C  CB  . SER   B 1   ? 0.3040 0.2870 0.2865 -0.0040 -0.0402 -0.0068 7   SER   C CB  
1083 O  OG  . SER   B 1   ? 0.3531 0.3337 0.3336 -0.0051 -0.0440 -0.0046 7   SER   C OG  
1084 N  N   . GLY   B 2   ? 0.2307 0.2233 0.2265 -0.0010 -0.0319 -0.0070 8   GLY   C N   
1085 C  CA  . GLY   B 2   ? 0.2161 0.2118 0.2181 -0.0004 -0.0300 -0.0070 8   GLY   C CA  
1086 C  C   . GLY   B 2   ? 0.2092 0.2088 0.2169 -0.0001 -0.0265 -0.0081 8   GLY   C C   
1087 O  O   . GLY   B 2   ? 0.2100 0.2101 0.2154 -0.0002 -0.0248 -0.0084 8   GLY   C O   
1088 N  N   . ALA   B 3   ? 0.1926 0.1946 0.2076 0.0000  -0.0252 -0.0089 9   ALA   C N   
1089 C  CA  . ALA   B 3   ? 0.1875 0.1930 0.2069 -0.0006 -0.0213 -0.0102 9   ALA   C CA  
1090 C  C   . ALA   B 3   ? 0.1814 0.1892 0.2040 -0.0008 -0.0182 -0.0115 9   ALA   C C   
1091 O  O   . ALA   B 3   ? 0.1854 0.1919 0.2097 -0.0002 -0.0197 -0.0115 9   ALA   C O   
1092 C  CB  . ALA   B 3   ? 0.1949 0.2014 0.2228 -0.0008 -0.0225 -0.0111 9   ALA   C CB  
1093 N  N   . ILE   B 4   ? 0.1744 0.1848 0.1972 -0.0021 -0.0140 -0.0126 10  ILE   C N   
1094 C  CA  . ILE   B 4   ? 0.1716 0.1840 0.1971 -0.0031 -0.0104 -0.0147 10  ILE   C CA  
1095 C  C   . ILE   B 4   ? 0.1788 0.1938 0.2132 -0.0041 -0.0078 -0.0170 10  ILE   C C   
1096 O  O   . ILE   B 4   ? 0.1781 0.1940 0.2123 -0.0052 -0.0070 -0.0165 10  ILE   C O   
1097 C  CB  . ILE   B 4   ? 0.1717 0.1852 0.1892 -0.0048 -0.0073 -0.0142 10  ILE   C CB  
1098 C  CG1 . ILE   B 4   ? 0.1825 0.1944 0.1928 -0.0039 -0.0095 -0.0120 10  ILE   C CG1 
1099 C  CG2 . ILE   B 4   ? 0.1803 0.1954 0.1995 -0.0064 -0.0034 -0.0169 10  ILE   C CG2 
1100 C  CD1 . ILE   B 4   ? 0.2039 0.2170 0.2077 -0.0054 -0.0079 -0.0107 10  ILE   C CD1 
1101 N  N   . TYR   B 5   ? 0.1768 0.1929 0.2198 -0.0038 -0.0064 -0.0196 11  TYR   C N   
1102 C  CA  . TYR   B 5   ? 0.1826 0.2017 0.2361 -0.0046 -0.0033 -0.0225 11  TYR   C CA  
1103 C  C   . TYR   B 5   ? 0.1920 0.2130 0.2454 -0.0067 0.0029  -0.0260 11  TYR   C C   
1104 O  O   . TYR   B 5   ? 0.2098 0.2299 0.2659 -0.0058 0.0033  -0.0278 11  TYR   C O   
1105 C  CB  . TYR   B 5   ? 0.1787 0.1974 0.2447 -0.0023 -0.0071 -0.0232 11  TYR   C CB  
1106 C  CG  . TYR   B 5   ? 0.1937 0.2103 0.2589 -0.0012 -0.0133 -0.0200 11  TYR   C CG  
1107 C  CD1 . TYR   B 5   ? 0.1988 0.2170 0.2683 -0.0020 -0.0135 -0.0200 11  TYR   C CD1 
1108 C  CD2 . TYR   B 5   ? 0.2079 0.2206 0.2666 0.0001  -0.0185 -0.0172 11  TYR   C CD2 
1109 C  CE1 . TYR   B 5   ? 0.2169 0.2327 0.2847 -0.0014 -0.0192 -0.0175 11  TYR   C CE1 
1110 C  CE2 . TYR   B 5   ? 0.2246 0.2348 0.2807 0.0005  -0.0237 -0.0148 11  TYR   C CE2 
1111 C  CZ  . TYR   B 5   ? 0.2275 0.2392 0.2882 -0.0002 -0.0243 -0.0151 11  TYR   C CZ  
1112 O  OH  . TYR   B 5   ? 0.2486 0.2575 0.3058 -0.0002 -0.0294 -0.0131 11  TYR   C OH  
1113 N  N   . VAL   B 6   ? 0.1870 0.2101 0.2370 -0.0098 0.0077  -0.0271 12  VAL   C N   
1114 C  CA  . VAL   B 6   ? 0.2081 0.2326 0.2555 -0.0127 0.0138  -0.0305 12  VAL   C CA  
1115 C  C   . VAL   B 6   ? 0.2212 0.2488 0.2729 -0.0158 0.0192  -0.0330 12  VAL   C C   
1116 O  O   . VAL   B 6   ? 0.2218 0.2497 0.2695 -0.0173 0.0187  -0.0304 12  VAL   C O   
1117 C  CB  . VAL   B 6   ? 0.2358 0.2586 0.2684 -0.0147 0.0139  -0.0283 12  VAL   C CB  
1118 C  CG1 . VAL   B 6   ? 0.2458 0.2677 0.2706 -0.0151 0.0109  -0.0237 12  VAL   C CG1 
1119 C  CG2 . VAL   B 6   ? 0.2446 0.2685 0.2724 -0.0189 0.0202  -0.0318 12  VAL   C CG2 
1120 N  N   . GLY   B 7   ? 0.2238 0.2538 0.2853 -0.0165 0.0245  -0.0382 13  GLY   C N   
1121 C  CA  . GLY   B 7   ? 0.2323 0.2659 0.2995 -0.0198 0.0307  -0.0413 13  GLY   C CA  
1122 C  C   . GLY   B 7   ? 0.2413 0.2764 0.3175 -0.0183 0.0273  -0.0391 13  GLY   C C   
1123 O  O   . GLY   B 7   ? 0.2522 0.2865 0.3369 -0.0143 0.0215  -0.0378 13  GLY   C O   
1124 N  N   . ASN   B 8   ? 0.2485 0.2848 0.3206 -0.0217 0.0296  -0.0377 14  ASN   C N   
1125 C  CA  . ASN   B 8   ? 0.2453 0.2826 0.3250 -0.0206 0.0261  -0.0355 14  ASN   C CA  
1126 C  C   . ASN   B 8   ? 0.2311 0.2646 0.2993 -0.0199 0.0201  -0.0298 14  ASN   C C   
1127 O  O   . ASN   B 8   ? 0.2370 0.2706 0.3060 -0.0211 0.0189  -0.0277 14  ASN   C O   
1128 C  CB  . ASN   B 8   ? 0.2852 0.3264 0.3710 -0.0247 0.0325  -0.0379 14  ASN   C CB  
1129 C  CG  . ASN   B 8   ? 0.3797 0.4254 0.4819 -0.0245 0.0379  -0.0440 14  ASN   C CG  
1130 O  OD1 . ASN   B 8   ? 0.4036 0.4504 0.5204 -0.0204 0.0341  -0.0451 14  ASN   C OD1 
1131 N  ND2 . ASN   B 8   ? 0.4017 0.4498 0.5022 -0.0290 0.0469  -0.0482 14  ASN   C ND2 
1132 N  N   . TYR   B 9   ? 0.2075 0.2377 0.2664 -0.0178 0.0162  -0.0276 15  TYR   C N   
1133 C  CA  . TYR   B 9   ? 0.1911 0.2178 0.2402 -0.0168 0.0110  -0.0229 15  TYR   C CA  
1134 C  C   . TYR   B 9   ? 0.1792 0.2034 0.2292 -0.0125 0.0048  -0.0213 15  TYR   C C   
1135 O  O   . TYR   B 9   ? 0.1735 0.1976 0.2262 -0.0107 0.0043  -0.0230 15  TYR   C O   
1136 C  CB  . TYR   B 9   ? 0.1908 0.2158 0.2259 -0.0191 0.0126  -0.0211 15  TYR   C CB  
1137 C  CG  . TYR   B 9   ? 0.2085 0.2347 0.2388 -0.0243 0.0180  -0.0215 15  TYR   C CG  
1138 C  CD1 . TYR   B 9   ? 0.2298 0.2562 0.2616 -0.0265 0.0185  -0.0198 15  TYR   C CD1 
1139 C  CD2 . TYR   B 9   ? 0.2289 0.2555 0.2521 -0.0275 0.0225  -0.0234 15  TYR   C CD2 
1140 C  CE1 . TYR   B 9   ? 0.2527 0.2798 0.2792 -0.0319 0.0235  -0.0198 15  TYR   C CE1 
1141 C  CE2 . TYR   B 9   ? 0.2505 0.2777 0.2674 -0.0331 0.0275  -0.0236 15  TYR   C CE2 
1142 C  CZ  . TYR   B 9   ? 0.2720 0.2994 0.2902 -0.0354 0.0279  -0.0215 15  TYR   C CZ  
1143 O  OH  . TYR   B 9   ? 0.3080 0.3355 0.3191 -0.0416 0.0328  -0.0212 15  TYR   C OH  
1144 N  N   . ARG   B 10  ? 0.1578 0.1794 0.2040 -0.0113 0.0001  -0.0182 16  ARG   C N   
1145 C  CA  . ARG   B 10  ? 0.1640 0.1826 0.2079 -0.0082 -0.0055 -0.0165 16  ARG   C CA  
1146 C  C   . ARG   B 10  ? 0.1709 0.1869 0.2034 -0.0083 -0.0067 -0.0136 16  ARG   C C   
1147 O  O   . ARG   B 10  ? 0.1779 0.1933 0.2084 -0.0097 -0.0066 -0.0121 16  ARG   C O   
1148 C  CB  . ARG   B 10  ? 0.1747 0.1926 0.2260 -0.0069 -0.0100 -0.0161 16  ARG   C CB  
1149 C  CG  . ARG   B 10  ? 0.1946 0.2085 0.2401 -0.0049 -0.0156 -0.0140 16  ARG   C CG  
1150 C  CD  . ARG   B 10  ? 0.2126 0.2255 0.2651 -0.0042 -0.0205 -0.0140 16  ARG   C CD  
1151 N  NE  . ARG   B 10  ? 0.2343 0.2433 0.2798 -0.0040 -0.0243 -0.0123 16  ARG   C NE  
1152 C  CZ  . ARG   B 10  ? 0.2670 0.2724 0.3073 -0.0029 -0.0287 -0.0114 16  ARG   C CZ  
1153 N  NH1 . ARG   B 10  ? 0.2582 0.2632 0.2992 -0.0018 -0.0304 -0.0112 16  ARG   C NH1 
1154 N  NH2 . ARG   B 10  ? 0.2502 0.2521 0.2841 -0.0031 -0.0312 -0.0108 16  ARG   C NH2 
1155 N  N   . VAL   B 11  ? 0.1560 0.1708 0.1821 -0.0071 -0.0077 -0.0128 17  VAL   C N   
1156 C  CA  . VAL   B 11  ? 0.1596 0.1725 0.1770 -0.0069 -0.0087 -0.0104 17  VAL   C CA  
1157 C  C   . VAL   B 11  ? 0.1622 0.1724 0.1779 -0.0044 -0.0128 -0.0096 17  VAL   C C   
1158 O  O   . VAL   B 11  ? 0.1715 0.1811 0.1876 -0.0031 -0.0142 -0.0101 17  VAL   C O   
1159 C  CB  . VAL   B 11  ? 0.1780 0.1917 0.1896 -0.0077 -0.0067 -0.0102 17  VAL   C CB  
1160 C  CG1 . VAL   B 11  ? 0.1859 0.1985 0.1909 -0.0076 -0.0080 -0.0075 17  VAL   C CG1 
1161 C  CG2 . VAL   B 11  ? 0.1791 0.1953 0.1916 -0.0107 -0.0023 -0.0119 17  VAL   C CG2 
1162 N  N   . VAL   B 12  ? 0.1462 0.1543 0.1596 -0.0040 -0.0145 -0.0084 18  VAL   C N   
1163 C  CA  . VAL   B 12  ? 0.1574 0.1625 0.1678 -0.0022 -0.0176 -0.0082 18  VAL   C CA  
1164 C  C   . VAL   B 12  ? 0.1488 0.1523 0.1542 -0.0017 -0.0174 -0.0070 18  VAL   C C   
1165 O  O   . VAL   B 12  ? 0.1404 0.1446 0.1457 -0.0026 -0.0161 -0.0058 18  VAL   C O   
1166 C  CB  . VAL   B 12  ? 0.1908 0.1941 0.2053 -0.0023 -0.0205 -0.0089 18  VAL   C CB  
1167 C  CG1 . VAL   B 12  ? 0.2259 0.2306 0.2471 -0.0024 -0.0217 -0.0099 18  VAL   C CG1 
1168 C  CG2 . VAL   B 12  ? 0.1888 0.1920 0.2058 -0.0036 -0.0196 -0.0085 18  VAL   C CG2 
1169 N  N   . ASN   B 13  ? 0.1462 0.1475 0.1479 -0.0003 -0.0188 -0.0075 19  ASN   C N   
1170 C  CA  . ASN   B 13  ? 0.1478 0.1475 0.1470 0.0006  -0.0185 -0.0071 19  ASN   C CA  
1171 C  C   . ASN   B 13  ? 0.1556 0.1531 0.1576 0.0001  -0.0196 -0.0072 19  ASN   C C   
1172 O  O   . ASN   B 13  ? 0.1641 0.1598 0.1675 -0.0004 -0.0215 -0.0083 19  ASN   C O   
1173 C  CB  . ASN   B 13  ? 0.1597 0.1570 0.1546 0.0015  -0.0192 -0.0085 19  ASN   C CB  
1174 C  CG  . ASN   B 13  ? 0.1944 0.1934 0.1863 0.0017  -0.0181 -0.0083 19  ASN   C CG  
1175 O  OD1 . ASN   B 13  ? 0.1932 0.1919 0.1838 0.0012  -0.0192 -0.0084 19  ASN   C OD1 
1176 N  ND2 . ASN   B 13  ? 0.1723 0.1731 0.1639 0.0024  -0.0162 -0.0077 19  ASN   C ND2 
1177 N  N   . ARG   B 14  ? 0.1476 0.1449 0.1507 -0.0001 -0.0189 -0.0057 20  ARG   C N   
1178 C  CA  . ARG   B 14  ? 0.1444 0.1391 0.1504 -0.0008 -0.0199 -0.0055 20  ARG   C CA  
1179 C  C   . ARG   B 14  ? 0.1551 0.1458 0.1601 0.0002  -0.0216 -0.0078 20  ARG   C C   
1180 O  O   . ARG   B 14  ? 0.1741 0.1630 0.1814 -0.0009 -0.0232 -0.0085 20  ARG   C O   
1181 C  CB  . ARG   B 14  ? 0.1584 0.1525 0.1653 -0.0009 -0.0196 -0.0031 20  ARG   C CB  
1182 C  CG  . ARG   B 14  ? 0.1806 0.1720 0.1905 -0.0024 -0.0206 -0.0019 20  ARG   C CG  
1183 C  CD  . ARG   B 14  ? 0.1758 0.1656 0.1867 -0.0021 -0.0213 0.0008  20  ARG   C CD  
1184 N  NE  . ARG   B 14  ? 0.1814 0.1680 0.1948 -0.0039 -0.0225 0.0029  20  ARG   C NE  
1185 C  CZ  . ARG   B 14  ? 0.2126 0.1947 0.2289 -0.0030 -0.0240 0.0018  20  ARG   C CZ  
1186 N  NH1 . ARG   B 14  ? 0.1899 0.1702 0.2061 -0.0005 -0.0241 -0.0018 20  ARG   C NH1 
1187 N  NH2 . ARG   B 14  ? 0.2302 0.2092 0.2490 -0.0049 -0.0252 0.0042  20  ARG   C NH2 
1188 N  N   . HIS   B 15  ? 0.1473 0.1369 0.1489 0.0018  -0.0211 -0.0093 21  HIS   C N   
1189 C  CA  . HIS   B 15  ? 0.1587 0.1440 0.1578 0.0021  -0.0221 -0.0122 21  HIS   C CA  
1190 C  C   . HIS   B 15  ? 0.1694 0.1535 0.1655 0.0008  -0.0244 -0.0134 21  HIS   C C   
1191 O  O   . HIS   B 15  ? 0.1872 0.1673 0.1809 0.0002  -0.0260 -0.0156 21  HIS   C O   
1192 C  CB  . HIS   B 15  ? 0.1715 0.1559 0.1677 0.0037  -0.0200 -0.0140 21  HIS   C CB  
1193 C  CG  . HIS   B 15  ? 0.1595 0.1460 0.1509 0.0036  -0.0188 -0.0144 21  HIS   C CG  
1194 N  ND1 . HIS   B 15  ? 0.1753 0.1660 0.1678 0.0041  -0.0174 -0.0123 21  HIS   C ND1 
1195 C  CD2 . HIS   B 15  ? 0.1888 0.1731 0.1738 0.0028  -0.0190 -0.0165 21  HIS   C CD2 
1196 C  CE1 . HIS   B 15  ? 0.1975 0.1886 0.1852 0.0038  -0.0166 -0.0133 21  HIS   C CE1 
1197 N  NE2 . HIS   B 15  ? 0.1991 0.1863 0.1817 0.0028  -0.0175 -0.0155 21  HIS   C NE2 
1198 N  N   . LEU   B 16  ? 0.1638 0.1511 0.1608 0.0002  -0.0249 -0.0121 22  LEU   C N   
1199 C  CA  . LEU   B 16  ? 0.1832 0.1695 0.1792 -0.0009 -0.0280 -0.0126 22  LEU   C CA  
1200 C  C   . LEU   B 16  ? 0.1972 0.1855 0.2007 -0.0019 -0.0295 -0.0117 22  LEU   C C   
1201 O  O   . LEU   B 16  ? 0.1992 0.1875 0.2047 -0.0027 -0.0326 -0.0118 22  LEU   C O   
1202 C  CB  . LEU   B 16  ? 0.1915 0.1794 0.1841 -0.0007 -0.0278 -0.0120 22  LEU   C CB  
1203 C  CG  . LEU   B 16  ? 0.2093 0.1955 0.1944 -0.0002 -0.0260 -0.0130 22  LEU   C CG  
1204 C  CD1 . LEU   B 16  ? 0.2239 0.2113 0.2058 -0.0005 -0.0260 -0.0119 22  LEU   C CD1 
1205 C  CD2 . LEU   B 16  ? 0.2197 0.2008 0.1987 -0.0013 -0.0275 -0.0154 22  LEU   C CD2 
1206 N  N   . ALA   B 17  ? 0.1811 0.1713 0.1893 -0.0022 -0.0274 -0.0107 23  ALA   C N   
1207 C  CA  . ALA   B 17  ? 0.1920 0.1847 0.2076 -0.0037 -0.0277 -0.0101 23  ALA   C CA  
1208 C  C   . ALA   B 17  ? 0.1910 0.1811 0.2094 -0.0048 -0.0315 -0.0112 23  ALA   C C   
1209 O  O   . ALA   B 17  ? 0.1958 0.1816 0.2102 -0.0048 -0.0329 -0.0123 23  ALA   C O   
1210 C  CB  . ALA   B 17  ? 0.1758 0.1696 0.1936 -0.0046 -0.0249 -0.0087 23  ALA   C CB  
1211 N  N   . THR   B 18  ? 0.1926 0.1852 0.2181 -0.0057 -0.0332 -0.0113 24  THR   C N   
1212 C  CA  . THR   B 18  ? 0.1976 0.1882 0.2269 -0.0071 -0.0375 -0.0121 24  THR   C CA  
1213 C  C   . THR   B 18  ? 0.1977 0.1893 0.2339 -0.0088 -0.0363 -0.0119 24  THR   C C   
1214 O  O   . THR   B 18  ? 0.1875 0.1814 0.2253 -0.0093 -0.0321 -0.0108 24  THR   C O   
1215 C  CB  . THR   B 18  ? 0.2124 0.2059 0.2486 -0.0071 -0.0404 -0.0120 24  THR   C CB  
1216 O  OG1 . THR   B 18  ? 0.2291 0.2279 0.2742 -0.0074 -0.0366 -0.0118 24  THR   C OG1 
1217 C  CG2 . THR   B 18  ? 0.2212 0.2135 0.2511 -0.0058 -0.0418 -0.0115 24  THR   C CG2 
1218 N  N   . HIS   B 19  ? 0.2058 0.1958 0.2465 -0.0104 -0.0403 -0.0126 25  HIS   C N   
1219 C  CA  . HIS   B 19  ? 0.2116 0.2028 0.2600 -0.0126 -0.0393 -0.0124 25  HIS   C CA  
1220 C  C   . HIS   B 19  ? 0.1991 0.1969 0.2567 -0.0133 -0.0355 -0.0118 25  HIS   C C   
1221 O  O   . HIS   B 19  ? 0.2098 0.2092 0.2697 -0.0150 -0.0315 -0.0109 25  HIS   C O   
1222 C  CB  . HIS   B 19  ? 0.2577 0.2469 0.3107 -0.0143 -0.0448 -0.0134 25  HIS   C CB  
1223 C  CG  . HIS   B 19  ? 0.3741 0.3564 0.4180 -0.0144 -0.0480 -0.0147 25  HIS   C CG  
1224 N  ND1 . HIS   B 19  ? 0.4259 0.4042 0.4644 -0.0141 -0.0454 -0.0150 25  HIS   C ND1 
1225 C  CD2 . HIS   B 19  ? 0.4157 0.3943 0.4555 -0.0150 -0.0535 -0.0160 25  HIS   C CD2 
1226 C  CE1 . HIS   B 19  ? 0.4426 0.4151 0.4745 -0.0145 -0.0487 -0.0171 25  HIS   C CE1 
1227 N  NE2 . HIS   B 19  ? 0.4457 0.4180 0.4770 -0.0153 -0.0536 -0.0178 25  HIS   C NE2 
1228 N  N   . ASN   B 20  ? 0.1923 0.1935 0.2547 -0.0123 -0.0366 -0.0123 26  ASN   C N   
1229 C  CA  . ASN   B 20  ? 0.1947 0.2020 0.2667 -0.0129 -0.0324 -0.0127 26  ASN   C CA  
1230 C  C   . ASN   B 20  ? 0.1889 0.1975 0.2547 -0.0128 -0.0264 -0.0121 26  ASN   C C   
1231 O  O   . ASN   B 20  ? 0.1919 0.2040 0.2621 -0.0148 -0.0216 -0.0122 26  ASN   C O   
1232 C  CB  . ASN   B 20  ? 0.2389 0.2487 0.3177 -0.0113 -0.0352 -0.0135 26  ASN   C CB  
1233 C  CG  . ASN   B 20  ? 0.3330 0.3492 0.4243 -0.0120 -0.0308 -0.0149 26  ASN   C CG  
1234 O  OD1 . ASN   B 20  ? 0.3443 0.3637 0.4455 -0.0141 -0.0292 -0.0156 26  ASN   C OD1 
1235 N  ND2 . ASN   B 20  ? 0.3615 0.3798 0.4530 -0.0104 -0.0282 -0.0156 26  ASN   C ND2 
1236 N  N   . ASP   B 21  ? 0.1775 0.1832 0.2327 -0.0108 -0.0266 -0.0114 27  ASP   C N   
1237 C  CA  . ASP   B 21  ? 0.1779 0.1846 0.2271 -0.0109 -0.0218 -0.0105 27  ASP   C CA  
1238 C  C   . ASP   B 21  ? 0.1815 0.1870 0.2287 -0.0133 -0.0195 -0.0090 27  ASP   C C   
1239 O  O   . ASP   B 21  ? 0.2065 0.2145 0.2539 -0.0154 -0.0152 -0.0083 27  ASP   C O   
1240 C  CB  . ASP   B 21  ? 0.1804 0.1840 0.2197 -0.0086 -0.0231 -0.0099 27  ASP   C CB  
1241 C  CG  . ASP   B 21  ? 0.2145 0.2193 0.2540 -0.0068 -0.0243 -0.0107 27  ASP   C CG  
1242 O  OD1 . ASP   B 21  ? 0.2057 0.2144 0.2513 -0.0072 -0.0219 -0.0116 27  ASP   C OD1 
1243 O  OD2 . ASP   B 21  ? 0.2189 0.2205 0.2525 -0.0053 -0.0274 -0.0106 27  ASP   C OD2 
1244 N  N   . TRP   B 22  ? 0.1780 0.1791 0.2232 -0.0133 -0.0226 -0.0084 28  TRP   C N   
1245 C  CA  . TRP   B 22  ? 0.1835 0.1824 0.2272 -0.0155 -0.0211 -0.0065 28  TRP   C CA  
1246 C  C   . TRP   B 22  ? 0.1938 0.1957 0.2458 -0.0190 -0.0189 -0.0064 28  TRP   C C   
1247 O  O   . TRP   B 22  ? 0.2032 0.2050 0.2535 -0.0218 -0.0159 -0.0044 28  TRP   C O   
1248 C  CB  . TRP   B 22  ? 0.1899 0.1829 0.2303 -0.0144 -0.0249 -0.0064 28  TRP   C CB  
1249 C  CG  . TRP   B 22  ? 0.1867 0.1768 0.2192 -0.0119 -0.0251 -0.0059 28  TRP   C CG  
1250 C  CD1 . TRP   B 22  ? 0.1980 0.1864 0.2261 -0.0093 -0.0270 -0.0076 28  TRP   C CD1 
1251 C  CD2 . TRP   B 22  ? 0.1749 0.1635 0.2036 -0.0121 -0.0234 -0.0034 28  TRP   C CD2 
1252 N  NE1 . TRP   B 22  ? 0.2047 0.1912 0.2276 -0.0076 -0.0260 -0.0067 28  TRP   C NE1 
1253 C  CE2 . TRP   B 22  ? 0.1934 0.1800 0.2170 -0.0091 -0.0242 -0.0040 28  TRP   C CE2 
1254 C  CE3 . TRP   B 22  ? 0.1792 0.1678 0.2082 -0.0148 -0.0215 -0.0005 28  TRP   C CE3 
1255 C  CZ2 . TRP   B 22  ? 0.1960 0.1810 0.2168 -0.0083 -0.0236 -0.0019 28  TRP   C CZ2 
1256 C  CZ3 . TRP   B 22  ? 0.1905 0.1769 0.2151 -0.0143 -0.0214 0.0021  28  TRP   C CZ3 
1257 C  CH2 . TRP   B 22  ? 0.1963 0.1812 0.2176 -0.0108 -0.0226 0.0014  28  TRP   C CH2 
1258 N  N   . ALA   B 23  ? 0.1832 0.1879 0.2443 -0.0193 -0.0205 -0.0084 29  ALA   C N   
1259 C  CA  . ALA   B 23  ? 0.1983 0.2068 0.2692 -0.0227 -0.0179 -0.0088 29  ALA   C CA  
1260 C  C   . ALA   B 23  ? 0.2030 0.2170 0.2763 -0.0244 -0.0115 -0.0095 29  ALA   C C   
1261 O  O   . ALA   B 23  ? 0.2067 0.2238 0.2862 -0.0280 -0.0076 -0.0098 29  ALA   C O   
1262 C  CB  . ALA   B 23  ? 0.1882 0.1984 0.2697 -0.0223 -0.0219 -0.0107 29  ALA   C CB  
1263 N  N   . ASN   B 24  ? 0.1961 0.2112 0.2648 -0.0220 -0.0104 -0.0102 30  ASN   C N   
1264 C  CA  . ASN   B 24  ? 0.1918 0.2113 0.2615 -0.0235 -0.0044 -0.0116 30  ASN   C CA  
1265 C  C   . ASN   B 24  ? 0.1993 0.2165 0.2562 -0.0235 -0.0027 -0.0097 30  ASN   C C   
1266 O  O   . ASN   B 24  ? 0.1928 0.2122 0.2475 -0.0229 0.0000  -0.0111 30  ASN   C O   
1267 C  CB  . ASN   B 24  ? 0.2025 0.2256 0.2807 -0.0209 -0.0051 -0.0146 30  ASN   C CB  
1268 C  CG  . ASN   B 24  ? 0.2637 0.2898 0.3565 -0.0213 -0.0069 -0.0163 30  ASN   C CG  
1269 O  OD1 . ASN   B 24  ? 0.2580 0.2888 0.3601 -0.0241 -0.0022 -0.0179 30  ASN   C OD1 
1270 N  ND2 . ASN   B 24  ? 0.2657 0.2895 0.3609 -0.0188 -0.0138 -0.0158 30  ASN   C ND2 
1271 N  N   . LEU   B 25  ? 0.2001 0.2127 0.2492 -0.0241 -0.0047 -0.0066 31  LEU   C N   
1272 C  CA  . LEU   B 25  ? 0.2056 0.2156 0.2439 -0.0239 -0.0045 -0.0042 31  LEU   C CA  
1273 C  C   . LEU   B 25  ? 0.2107 0.2231 0.2443 -0.0278 0.0008  -0.0037 31  LEU   C C   
1274 O  O   . LEU   B 25  ? 0.2327 0.2461 0.2678 -0.0321 0.0042  -0.0032 31  LEU   C O   
1275 C  CB  . LEU   B 25  ? 0.2062 0.2109 0.2403 -0.0239 -0.0080 -0.0010 31  LEU   C CB  
1276 C  CG  . LEU   B 25  ? 0.2175 0.2193 0.2423 -0.0235 -0.0087 0.0020  31  LEU   C CG  
1277 C  CD1 . LEU   B 25  ? 0.2225 0.2246 0.2445 -0.0192 -0.0106 0.0007  31  LEU   C CD1 
1278 C  CD2 . LEU   B 25  ? 0.2137 0.2101 0.2371 -0.0237 -0.0120 0.0050  31  LEU   C CD2 
1279 N  N   . VAL   B 26  ? 0.1906 0.2035 0.2178 -0.0267 0.0016  -0.0038 32  VAL   C N   
1280 C  CA  . VAL   B 26  ? 0.1996 0.2137 0.2198 -0.0307 0.0061  -0.0033 32  VAL   C CA  
1281 C  C   . VAL   B 26  ? 0.2045 0.2145 0.2144 -0.0312 0.0031  0.0011  32  VAL   C C   
1282 O  O   . VAL   B 26  ? 0.2291 0.2376 0.2327 -0.0357 0.0045  0.0040  32  VAL   C O   
1283 C  CB  . VAL   B 26  ? 0.2123 0.2298 0.2334 -0.0295 0.0090  -0.0070 32  VAL   C CB  
1284 C  CG1 . VAL   B 26  ? 0.2236 0.2415 0.2350 -0.0337 0.0128  -0.0065 32  VAL   C CG1 
1285 C  CG2 . VAL   B 26  ? 0.2152 0.2370 0.2485 -0.0293 0.0121  -0.0113 32  VAL   C CG2 
1286 N  N   . TRP   B 27  ? 0.1839 0.1922 0.1926 -0.0267 -0.0011 0.0017  33  TRP   C N   
1287 C  CA  . TRP   B 27  ? 0.1920 0.1971 0.1936 -0.0263 -0.0043 0.0055  33  TRP   C CA  
1288 C  C   . TRP   B 27  ? 0.1962 0.1996 0.2003 -0.0209 -0.0084 0.0051  33  TRP   C C   
1289 O  O   . TRP   B 27  ? 0.2052 0.2104 0.2127 -0.0180 -0.0084 0.0020  33  TRP   C O   
1290 C  CB  . TRP   B 27  ? 0.2072 0.2141 0.2015 -0.0282 -0.0023 0.0055  33  TRP   C CB  
1291 C  CG  . TRP   B 27  ? 0.2322 0.2369 0.2208 -0.0272 -0.0061 0.0090  33  TRP   C CG  
1292 C  CD1 . TRP   B 27  ? 0.2662 0.2680 0.2493 -0.0302 -0.0085 0.0138  33  TRP   C CD1 
1293 C  CD2 . TRP   B 27  ? 0.2330 0.2385 0.2217 -0.0233 -0.0083 0.0082  33  TRP   C CD2 
1294 N  NE1 . TRP   B 27  ? 0.2722 0.2731 0.2533 -0.0278 -0.0122 0.0159  33  TRP   C NE1 
1295 C  CE2 . TRP   B 27  ? 0.2505 0.2539 0.2350 -0.0237 -0.0118 0.0123  33  TRP   C CE2 
1296 C  CE3 . TRP   B 27  ? 0.2327 0.2403 0.2250 -0.0196 -0.0077 0.0047  33  TRP   C CE3 
1297 C  CZ2 . TRP   B 27  ? 0.2459 0.2502 0.2302 -0.0207 -0.0140 0.0125  33  TRP   C CZ2 
1298 C  CZ3 . TRP   B 27  ? 0.2325 0.2404 0.2233 -0.0170 -0.0099 0.0051  33  TRP   C CZ3 
1299 C  CH2 . TRP   B 27  ? 0.2305 0.2371 0.2179 -0.0175 -0.0127 0.0087  33  TRP   C CH2 
1300 N  N   . GLU   B 28  ? 0.1900 0.1897 0.1924 -0.0199 -0.0119 0.0082  34  GLU   C N   
1301 C  CA  . GLU   B 28  ? 0.1953 0.1935 0.1995 -0.0153 -0.0148 0.0074  34  GLU   C CA  
1302 C  C   . GLU   B 28  ? 0.2017 0.1977 0.2032 -0.0147 -0.0175 0.0109  34  GLU   C C   
1303 O  O   . GLU   B 28  ? 0.2023 0.1961 0.2018 -0.0177 -0.0186 0.0146  34  GLU   C O   
1304 C  CB  . GLU   B 28  ? 0.2004 0.1961 0.2098 -0.0132 -0.0165 0.0056  34  GLU   C CB  
1305 C  CG  . GLU   B 28  ? 0.2212 0.2133 0.2326 -0.0155 -0.0176 0.0079  34  GLU   C CG  
1306 C  CD  . GLU   B 28  ? 0.2437 0.2314 0.2547 -0.0145 -0.0206 0.0110  34  GLU   C CD  
1307 O  OE1 . GLU   B 28  ? 0.2822 0.2671 0.2930 -0.0174 -0.0215 0.0143  34  GLU   C OE1 
1308 O  OE2 . GLU   B 28  ? 0.2118 0.1988 0.2233 -0.0109 -0.0221 0.0101  34  GLU   C OE2 
1309 N  N   . ASP   B 29  ? 0.1945 0.1910 0.1966 -0.0111 -0.0188 0.0099  35  ASP   C N   
1310 C  CA  . ASP   B 29  ? 0.1886 0.1836 0.1907 -0.0100 -0.0215 0.0129  35  ASP   C CA  
1311 C  C   . ASP   B 29  ? 0.1795 0.1737 0.1857 -0.0055 -0.0224 0.0104  35  ASP   C C   
1312 O  O   . ASP   B 29  ? 0.1723 0.1692 0.1776 -0.0037 -0.0211 0.0079  35  ASP   C O   
1313 C  CB  . ASP   B 29  ? 0.2031 0.2009 0.2003 -0.0120 -0.0214 0.0148  35  ASP   C CB  
1314 C  CG  . ASP   B 29  ? 0.2642 0.2607 0.2623 -0.0115 -0.0252 0.0187  35  ASP   C CG  
1315 O  OD1 . ASP   B 29  ? 0.2722 0.2666 0.2762 -0.0082 -0.0271 0.0187  35  ASP   C OD1 
1316 O  OD2 . ASP   B 29  ? 0.2831 0.2807 0.2763 -0.0145 -0.0262 0.0216  35  ASP   C OD2 
1317 N  N   . SER   B 30  ? 0.1765 0.1668 0.1871 -0.0040 -0.0242 0.0108  36  SER   C N   
1318 C  CA  A SER   B 30  ? 0.1826 0.1716 0.1970 -0.0001 -0.0243 0.0078  36  SER   C CA  
1319 C  CA  B SER   B 30  ? 0.1826 0.1716 0.1969 -0.0001 -0.0243 0.0077  36  SER   C CA  
1320 C  C   . SER   B 30  ? 0.1832 0.1748 0.1990 0.0019  -0.0246 0.0083  36  SER   C C   
1321 O  O   . SER   B 30  ? 0.2019 0.1949 0.2184 0.0042  -0.0229 0.0050  36  SER   C O   
1322 C  CB  A SER   B 30  ? 0.2008 0.1845 0.2202 0.0008  -0.0263 0.0083  36  SER   C CB  
1323 C  CB  B SER   B 30  ? 0.2017 0.1855 0.2209 0.0009  -0.0260 0.0078  36  SER   C CB  
1324 O  OG  A SER   B 30  ? 0.2203 0.2026 0.2435 0.0043  -0.0257 0.0047  36  SER   C OG  
1325 O  OG  B SER   B 30  ? 0.2193 0.2013 0.2419 0.0007  -0.0288 0.0121  36  SER   C OG  
1326 N  N   . SER   B 31  ? 0.1656 0.1579 0.1816 0.0004  -0.0268 0.0126  37  SER   C N   
1327 C  CA  . SER   B 31  ? 0.1782 0.1734 0.1971 0.0021  -0.0278 0.0135  37  SER   C CA  
1328 C  C   . SER   B 31  ? 0.1793 0.1790 0.1935 0.0018  -0.0252 0.0114  37  SER   C C   
1329 O  O   . SER   B 31  ? 0.1960 0.1984 0.2131 0.0037  -0.0250 0.0106  37  SER   C O   
1330 C  CB  . SER   B 31  ? 0.2164 0.2110 0.2360 0.0001  -0.0318 0.0191  37  SER   C CB  
1331 O  OG  . SER   B 31  ? 0.2795 0.2762 0.2912 -0.0040 -0.0317 0.0213  37  SER   C OG  
1332 N  N   . ARG   B 32  ? 0.1607 0.1614 0.1690 -0.0005 -0.0233 0.0102  38  ARG   C N   
1333 C  CA  . ARG   B 32  ? 0.1610 0.1653 0.1656 -0.0009 -0.0211 0.0082  38  ARG   C CA  
1334 C  C   . ARG   B 32  ? 0.1650 0.1690 0.1689 0.0007  -0.0189 0.0041  38  ARG   C C   
1335 O  O   . ARG   B 32  ? 0.1699 0.1761 0.1712 0.0006  -0.0174 0.0025  38  ARG   C O   
1336 C  CB  . ARG   B 32  ? 0.1686 0.1743 0.1677 -0.0047 -0.0205 0.0096  38  ARG   C CB  
1337 C  CG  . ARG   B 32  ? 0.1853 0.1911 0.1824 -0.0073 -0.0231 0.0139  38  ARG   C CG  
1338 C  CD  . ARG   B 32  ? 0.1876 0.1943 0.1777 -0.0118 -0.0216 0.0146  38  ARG   C CD  
1339 N  NE  . ARG   B 32  ? 0.1736 0.1834 0.1612 -0.0119 -0.0191 0.0116  38  ARG   C NE  
1340 C  CZ  . ARG   B 32  ? 0.1821 0.1932 0.1639 -0.0155 -0.0180 0.0118  38  ARG   C CZ  
1341 N  NH1 . ARG   B 32  ? 0.2022 0.2120 0.1788 -0.0197 -0.0192 0.0149  38  ARG   C NH1 
1342 N  NH2 . ARG   B 32  ? 0.1954 0.2087 0.1760 -0.0153 -0.0159 0.0089  38  ARG   C NH2 
1343 N  N   . ASP   B 33  ? 0.1710 0.1717 0.1768 0.0017  -0.0191 0.0027  39  ASP   C N   
1344 C  CA  . ASP   B 33  ? 0.1644 0.1640 0.1686 0.0023  -0.0179 -0.0007 39  ASP   C CA  
1345 C  C   . ASP   B 33  ? 0.1591 0.1604 0.1609 0.0003  -0.0172 -0.0009 39  ASP   C C   
1346 O  O   . ASP   B 33  ? 0.1603 0.1619 0.1606 0.0008  -0.0167 -0.0030 39  ASP   C O   
1347 C  CB  . ASP   B 33  ? 0.1673 0.1674 0.1704 0.0043  -0.0167 -0.0032 39  ASP   C CB  
1348 C  CG  . ASP   B 33  ? 0.1657 0.1638 0.1659 0.0043  -0.0164 -0.0061 39  ASP   C CG  
1349 O  OD1 . ASP   B 33  ? 0.1708 0.1659 0.1717 0.0040  -0.0175 -0.0070 39  ASP   C OD1 
1350 O  OD2 . ASP   B 33  ? 0.1705 0.1698 0.1674 0.0043  -0.0155 -0.0073 39  ASP   C OD2 
1351 N  N   . LEU   B 34  ? 0.1509 0.1530 0.1526 -0.0022 -0.0170 0.0011  40  LEU   C N   
1352 C  CA  . LEU   B 34  ? 0.1455 0.1494 0.1465 -0.0041 -0.0155 0.0000  40  LEU   C CA  
1353 C  C   . LEU   B 34  ? 0.1578 0.1604 0.1613 -0.0059 -0.0154 0.0002  40  LEU   C C   
1354 O  O   . LEU   B 34  ? 0.1714 0.1722 0.1752 -0.0071 -0.0162 0.0024  40  LEU   C O   
1355 C  CB  . LEU   B 34  ? 0.1479 0.1545 0.1459 -0.0064 -0.0141 0.0013  40  LEU   C CB  
1356 C  CG  . LEU   B 34  ? 0.1651 0.1737 0.1611 -0.0054 -0.0138 0.0009  40  LEU   C CG  
1357 C  CD1 . LEU   B 34  ? 0.1673 0.1779 0.1596 -0.0083 -0.0126 0.0019  40  LEU   C CD1 
1358 C  CD2 . LEU   B 34  ? 0.1709 0.1799 0.1677 -0.0039 -0.0131 -0.0019 40  LEU   C CD2 
1359 N  N   . LEU   B 35  ? 0.1551 0.1590 0.1609 -0.0065 -0.0144 -0.0019 41  LEU   C N   
1360 C  CA  . LEU   B 35  ? 0.1610 0.1649 0.1705 -0.0086 -0.0137 -0.0021 41  LEU   C CA  
1361 C  C   . LEU   B 35  ? 0.1591 0.1664 0.1713 -0.0098 -0.0111 -0.0041 41  LEU   C C   
1362 O  O   . LEU   B 35  ? 0.1643 0.1726 0.1773 -0.0081 -0.0115 -0.0058 41  LEU   C O   
1363 C  CB  . LEU   B 35  ? 0.1634 0.1646 0.1764 -0.0074 -0.0161 -0.0032 41  LEU   C CB  
1364 C  CG  . LEU   B 35  ? 0.1769 0.1783 0.1950 -0.0097 -0.0157 -0.0034 41  LEU   C CG  
1365 C  CD1 . LEU   B 35  ? 0.1850 0.1822 0.2046 -0.0092 -0.0184 -0.0032 41  LEU   C CD1 
1366 C  CD2 . LEU   B 35  ? 0.1860 0.1901 0.2097 -0.0096 -0.0154 -0.0058 41  LEU   C CD2 
1367 N  N   . VAL   B 36  ? 0.1452 0.1542 0.1588 -0.0130 -0.0083 -0.0040 42  VAL   C N   
1368 C  CA  . VAL   B 36  ? 0.1574 0.1698 0.1752 -0.0144 -0.0050 -0.0067 42  VAL   C CA  
1369 C  C   . VAL   B 36  ? 0.1689 0.1823 0.1941 -0.0160 -0.0040 -0.0076 42  VAL   C C   
1370 O  O   . VAL   B 36  ? 0.1603 0.1725 0.1841 -0.0186 -0.0034 -0.0057 42  VAL   C O   
1371 C  CB  . VAL   B 36  ? 0.1693 0.1835 0.1818 -0.0175 -0.0011 -0.0065 42  VAL   C CB  
1372 C  CG1 . VAL   B 36  ? 0.1843 0.2019 0.2022 -0.0190 0.0033  -0.0102 42  VAL   C CG1 
1373 C  CG2 . VAL   B 36  ? 0.1615 0.1750 0.1677 -0.0160 -0.0026 -0.0055 42  VAL   C CG2 
1374 N  N   . SER   B 37  ? 0.1690 0.1844 0.2025 -0.0146 -0.0044 -0.0103 43  SER   C N   
1375 C  CA  . SER   B 37  ? 0.1689 0.1862 0.2118 -0.0162 -0.0035 -0.0116 43  SER   C CA  
1376 C  C   . SER   B 37  ? 0.1801 0.2020 0.2308 -0.0173 0.0011  -0.0150 43  SER   C C   
1377 O  O   . SER   B 37  ? 0.1781 0.2008 0.2270 -0.0163 0.0025  -0.0164 43  SER   C O   
1378 C  CB  . SER   B 37  ? 0.1854 0.2010 0.2336 -0.0137 -0.0087 -0.0117 43  SER   C CB  
1379 O  OG  . SER   B 37  ? 0.2143 0.2301 0.2645 -0.0109 -0.0112 -0.0130 43  SER   C OG  
1380 N  N   . SER   B 38  ? 0.1840 0.2088 0.2436 -0.0197 0.0038  -0.0165 44  SER   C N   
1381 C  CA  . SER   B 38  ? 0.2055 0.2350 0.2742 -0.0209 0.0091  -0.0204 44  SER   C CA  
1382 C  C   . SER   B 38  ? 0.2249 0.2561 0.3070 -0.0175 0.0055  -0.0224 44  SER   C C   
1383 O  O   . SER   B 38  ? 0.2281 0.2577 0.3137 -0.0159 -0.0002 -0.0209 44  SER   C O   
1384 C  CB  . SER   B 38  ? 0.2220 0.2543 0.2944 -0.0256 0.0146  -0.0213 44  SER   C CB  
1385 O  OG  . SER   B 38  ? 0.2719 0.3038 0.3507 -0.0256 0.0112  -0.0199 44  SER   C OG  
1386 N  N   . THR   B 39  ? 0.2406 0.2748 0.3303 -0.0167 0.0086  -0.0259 45  THR   C N   
1387 C  CA  . THR   B 39  ? 0.2626 0.2984 0.3665 -0.0136 0.0049  -0.0276 45  THR   C CA  
1388 C  C   . THR   B 39  ? 0.2866 0.3281 0.4061 -0.0151 0.0111  -0.0322 45  THR   C C   
1389 O  O   . THR   B 39  ? 0.2927 0.3363 0.4092 -0.0183 0.0188  -0.0347 45  THR   C O   
1390 C  CB  . THR   B 39  ? 0.2875 0.3208 0.3877 -0.0105 0.0022  -0.0275 45  THR   C CB  
1391 O  OG1 . THR   B 39  ? 0.3061 0.3410 0.4044 -0.0119 0.0090  -0.0306 45  THR   C OG1 
1392 C  CG2 . THR   B 39  ? 0.3029 0.3310 0.3880 -0.0092 -0.0025 -0.0236 45  THR   C CG2 
1393 N  N   . THR   B 40  ? 0.3006 0.3444 0.4367 -0.0129 0.0076  -0.0334 46  THR   C N   
1394 C  CA  . THR   B 40  ? 0.3220 0.3718 0.4761 -0.0136 0.0132  -0.0383 46  THR   C CA  
1395 C  C   . THR   B 40  ? 0.3321 0.3817 0.4906 -0.0111 0.0147  -0.0414 46  THR   C C   
1396 O  O   . THR   B 40  ? 0.3400 0.3931 0.5054 -0.0125 0.0226  -0.0463 46  THR   C O   
1397 C  CB  . THR   B 40  ? 0.3539 0.4066 0.5260 -0.0125 0.0083  -0.0382 46  THR   C CB  
1398 O  OG1 . THR   B 40  ? 0.3976 0.4461 0.5691 -0.0089 -0.0018 -0.0348 46  THR   C OG1 
1399 C  CG2 . THR   B 40  ? 0.3559 0.4097 0.5262 -0.0159 0.0089  -0.0365 46  THR   C CG2 
1400 N  N   . ALA   B 41  ? 0.3283 0.3733 0.4823 -0.0076 0.0073  -0.0385 47  ALA   C N   
1401 C  CA  . ALA   B 41  ? 0.3305 0.3743 0.4881 -0.0051 0.0075  -0.0406 47  ALA   C CA  
1402 C  C   . ALA   B 41  ? 0.3370 0.3785 0.4780 -0.0067 0.0126  -0.0414 47  ALA   C C   
1403 O  O   . ALA   B 41  ? 0.3452 0.3842 0.4696 -0.0085 0.0124  -0.0383 47  ALA   C O   
1404 C  CB  . ALA   B 41  ? 0.3368 0.3762 0.4954 -0.0015 -0.0027 -0.0367 47  ALA   C CB  
1405 N  N   . GLN   B 42  ? 0.3302 0.3720 0.4762 -0.0060 0.0166  -0.0454 48  GLN   C N   
1406 C  CA  . GLN   B 42  ? 0.3367 0.3764 0.4685 -0.0078 0.0213  -0.0468 48  GLN   C CA  
1407 C  C   . GLN   B 42  ? 0.3213 0.3556 0.4422 -0.0054 0.0148  -0.0428 48  GLN   C C   
1408 O  O   . GLN   B 42  ? 0.3206 0.3530 0.4501 -0.0022 0.0100  -0.0424 48  GLN   C O   
1409 C  CB  . GLN   B 42  ? 0.3753 0.4175 0.5181 -0.0084 0.0289  -0.0536 48  GLN   C CB  
1410 C  CG  . GLN   B 42  ? 0.4589 0.4986 0.5877 -0.0105 0.0337  -0.0557 48  GLN   C CG  
1411 C  CD  . GLN   B 42  ? 0.5570 0.5980 0.6716 -0.0159 0.0405  -0.0565 48  GLN   C CD  
1412 O  OE1 . GLN   B 42  ? 0.5796 0.6238 0.6962 -0.0184 0.0434  -0.0565 48  GLN   C OE1 
1413 N  NE2 . GLN   B 42  ? 0.5857 0.6240 0.6856 -0.0182 0.0430  -0.0571 48  GLN   C NE2 
1414 N  N   . GLY   B 43  ? 0.2957 0.3277 0.3986 -0.0072 0.0149  -0.0400 49  GLY   C N   
1415 C  CA  . GLY   B 43  ? 0.2836 0.3111 0.3754 -0.0056 0.0099  -0.0365 49  GLY   C CA  
1416 C  C   . GLY   B 43  ? 0.2642 0.2906 0.3528 -0.0062 0.0136  -0.0395 49  GLY   C C   
1417 O  O   . GLY   B 43  ? 0.2691 0.2973 0.3547 -0.0093 0.0207  -0.0432 49  GLY   C O   
1418 N  N   . CYS   B 44  ? 0.2396 0.2624 0.3279 -0.0038 0.0090  -0.0379 50  CYS   C N   
1419 C  CA  . CYS   B 44  ? 0.2446 0.2658 0.3310 -0.0042 0.0118  -0.0407 50  CYS   C CA  
1420 C  C   . CYS   B 44  ? 0.2308 0.2487 0.3018 -0.0047 0.0092  -0.0373 50  CYS   C C   
1421 O  O   . CYS   B 44  ? 0.2346 0.2503 0.3045 -0.0049 0.0102  -0.0391 50  CYS   C O   
1422 C  CB  . CYS   B 44  ? 0.2632 0.2831 0.3653 -0.0013 0.0098  -0.0429 50  CYS   C CB  
1423 S  SG  . CYS   B 44  ? 0.3119 0.3365 0.4353 -0.0007 0.0142  -0.0483 50  CYS   C SG  
1424 N  N   . ASP   B 45  ? 0.1975 0.2150 0.2577 -0.0051 0.0061  -0.0327 51  ASP   C N   
1425 C  CA  . ASP   B 45  ? 0.2008 0.2159 0.2481 -0.0057 0.0042  -0.0299 51  ASP   C CA  
1426 C  C   . ASP   B 45  ? 0.2195 0.2359 0.2588 -0.0092 0.0096  -0.0323 51  ASP   C C   
1427 O  O   . ASP   B 45  ? 0.2428 0.2616 0.2812 -0.0116 0.0139  -0.0341 51  ASP   C O   
1428 C  CB  . ASP   B 45  ? 0.2023 0.2169 0.2416 -0.0051 0.0001  -0.0251 51  ASP   C CB  
1429 C  CG  . ASP   B 45  ? 0.2721 0.2846 0.3160 -0.0024 -0.0057 -0.0225 51  ASP   C CG  
1430 O  OD1 . ASP   B 45  ? 0.2815 0.2920 0.3324 -0.0009 -0.0080 -0.0230 51  ASP   C OD1 
1431 O  OD2 . ASP   B 45  ? 0.2710 0.2833 0.3112 -0.0021 -0.0083 -0.0199 51  ASP   C OD2 
1432 N  N   . THR   B 46  ? 0.2186 0.2331 0.2513 -0.0099 0.0093  -0.0322 52  THR   C N   
1433 C  CA  . THR   B 46  ? 0.2294 0.2446 0.2530 -0.0137 0.0133  -0.0340 52  THR   C CA  
1434 C  C   . THR   B 46  ? 0.1995 0.2147 0.2118 -0.0145 0.0102  -0.0292 52  THR   C C   
1435 O  O   . THR   B 46  ? 0.2026 0.2164 0.2134 -0.0125 0.0061  -0.0262 52  THR   C O   
1436 C  CB  . THR   B 46  ? 0.2796 0.2926 0.3036 -0.0143 0.0145  -0.0370 52  THR   C CB  
1437 O  OG1 . THR   B 46  ? 0.3108 0.3237 0.3470 -0.0133 0.0177  -0.0419 52  THR   C OG1 
1438 C  CG2 . THR   B 46  ? 0.3036 0.3168 0.3163 -0.0186 0.0175  -0.0384 52  THR   C CG2 
1439 N  N   . ILE   B 47  ? 0.1805 0.1972 0.1851 -0.0177 0.0122  -0.0285 53  ILE   C N   
1440 C  CA  . ILE   B 47  ? 0.1757 0.1925 0.1714 -0.0183 0.0090  -0.0240 53  ILE   C CA  
1441 C  C   . ILE   B 47  ? 0.1782 0.1945 0.1661 -0.0211 0.0092  -0.0243 53  ILE   C C   
1442 O  O   . ILE   B 47  ? 0.1875 0.2037 0.1721 -0.0247 0.0131  -0.0277 53  ILE   C O   
1443 C  CB  . ILE   B 47  ? 0.1863 0.2043 0.1781 -0.0204 0.0099  -0.0221 53  ILE   C CB  
1444 C  CG1 . ILE   B 47  ? 0.2061 0.2249 0.2061 -0.0184 0.0102  -0.0224 53  ILE   C CG1 
1445 C  CG2 . ILE   B 47  ? 0.1932 0.2111 0.1779 -0.0206 0.0059  -0.0172 53  ILE   C CG2 
1446 C  CD1 . ILE   B 47  ? 0.2211 0.2387 0.2252 -0.0141 0.0053  -0.0197 53  ILE   C CD1 
1447 N  N   . ALA   B 48  ? 0.1609 0.1769 0.1459 -0.0198 0.0053  -0.0210 54  ALA   C N   
1448 C  CA  . ALA   B 48  ? 0.1697 0.1855 0.1480 -0.0226 0.0047  -0.0208 54  ALA   C CA  
1449 C  C   . ALA   B 48  ? 0.1698 0.1865 0.1396 -0.0265 0.0047  -0.0190 54  ALA   C C   
1450 O  O   . ALA   B 48  ? 0.1691 0.1866 0.1385 -0.0257 0.0030  -0.0158 54  ALA   C O   
1451 C  CB  . ALA   B 48  ? 0.1699 0.1859 0.1487 -0.0202 0.0006  -0.0174 54  ALA   C CB  
1452 N  N   . ARG   B 49  ? 0.1638 0.1800 0.1265 -0.0308 0.0059  -0.0207 55  ARG   C N   
1453 C  CA  . ARG   B 49  ? 0.1734 0.1899 0.1265 -0.0354 0.0048  -0.0183 55  ARG   C CA  
1454 C  C   . ARG   B 49  ? 0.1817 0.1981 0.1305 -0.0371 0.0017  -0.0172 55  ARG   C C   
1455 O  O   . ARG   B 49  ? 0.1862 0.2013 0.1308 -0.0405 0.0038  -0.0209 55  ARG   C O   
1456 C  CB  . ARG   B 49  ? 0.1959 0.2113 0.1435 -0.0402 0.0101  -0.0223 55  ARG   C CB  
1457 C  CG  . ARG   B 49  ? 0.2137 0.2298 0.1679 -0.0384 0.0139  -0.0241 55  ARG   C CG  
1458 C  CD  . ARG   B 49  ? 0.2372 0.2540 0.1922 -0.0369 0.0110  -0.0191 55  ARG   C CD  
1459 N  NE  . ARG   B 49  ? 0.2477 0.2652 0.2095 -0.0356 0.0146  -0.0211 55  ARG   C NE  
1460 C  CZ  . ARG   B 49  ? 0.2554 0.2733 0.2211 -0.0332 0.0125  -0.0179 55  ARG   C CZ  
1461 N  NH1 . ARG   B 49  ? 0.2132 0.2307 0.1770 -0.0316 0.0074  -0.0129 55  ARG   C NH1 
1462 N  NH2 . ARG   B 49  ? 0.2451 0.2639 0.2176 -0.0324 0.0157  -0.0201 55  ARG   C NH2 
1463 N  N   . CYS   B 50  ? 0.1840 0.2019 0.1348 -0.0349 -0.0033 -0.0125 56  CYS   C N   
1464 C  CA  . CYS   B 50  ? 0.1857 0.2044 0.1356 -0.0356 -0.0064 -0.0114 56  CYS   C CA  
1465 C  C   . CYS   B 50  ? 0.1943 0.2153 0.1471 -0.0336 -0.0115 -0.0060 56  CYS   C C   
1466 O  O   . CYS   B 50  ? 0.1897 0.2112 0.1454 -0.0311 -0.0123 -0.0035 56  CYS   C O   
1467 C  CB  . CYS   B 50  ? 0.1844 0.2025 0.1407 -0.0327 -0.0048 -0.0143 56  CYS   C CB  
1468 S  SG  . CYS   B 50  ? 0.1768 0.1957 0.1424 -0.0264 -0.0057 -0.0122 56  CYS   C SG  
1469 N  N   . ASP   B 51  ? 0.1999 0.2225 0.1534 -0.0343 -0.0145 -0.0046 57  ASP   C N   
1470 C  CA  . ASP   B 51  ? 0.2000 0.2254 0.1590 -0.0319 -0.0186 -0.0004 57  ASP   C CA  
1471 C  C   . ASP   B 51  ? 0.1975 0.2244 0.1634 -0.0288 -0.0181 -0.0012 57  ASP   C C   
1472 O  O   . ASP   B 51  ? 0.1974 0.2273 0.1677 -0.0282 -0.0210 0.0013  57  ASP   C O   
1473 C  CB  . ASP   B 51  ? 0.2264 0.2532 0.1818 -0.0356 -0.0236 0.0031  57  ASP   C CB  
1474 C  CG  . ASP   B 51  ? 0.2849 0.3117 0.2361 -0.0396 -0.0246 0.0014  57  ASP   C CG  
1475 O  OD1 . ASP   B 51  ? 0.2947 0.3201 0.2460 -0.0395 -0.0210 -0.0027 57  ASP   C OD1 
1476 O  OD2 . ASP   B 51  ? 0.3394 0.3674 0.2877 -0.0430 -0.0295 0.0044  57  ASP   C OD2 
1477 N  N   . CYS   B 52  ? 0.1758 0.2008 0.1435 -0.0270 -0.0146 -0.0044 58  CYS   C N   
1478 C  CA  . CYS   B 52  ? 0.1603 0.1859 0.1334 -0.0246 -0.0140 -0.0048 58  CYS   C CA  
1479 C  C   . CYS   B 52  ? 0.1569 0.1850 0.1353 -0.0214 -0.0153 -0.0020 58  CYS   C C   
1480 O  O   . CYS   B 52  ? 0.1549 0.1829 0.1342 -0.0195 -0.0155 -0.0007 58  CYS   C O   
1481 C  CB  . CYS   B 52  ? 0.1640 0.1863 0.1383 -0.0228 -0.0109 -0.0077 58  CYS   C CB  
1482 S  SG  . CYS   B 52  ? 0.1963 0.2155 0.1675 -0.0261 -0.0087 -0.0121 58  CYS   C SG  
1483 N  N   . GLN   B 53  ? 0.1456 0.1756 0.1278 -0.0210 -0.0157 -0.0013 59  GLN   C N   
1484 C  CA  . GLN   B 53  ? 0.1411 0.1736 0.1290 -0.0182 -0.0157 0.0004  59  GLN   C CA  
1485 C  C   . GLN   B 53  ? 0.1533 0.1846 0.1425 -0.0172 -0.0133 -0.0008 59  GLN   C C   
1486 O  O   . GLN   B 53  ? 0.1555 0.1891 0.1488 -0.0160 -0.0126 0.0002  59  GLN   C O   
1487 C  CB  . GLN   B 53  ? 0.1547 0.1918 0.1473 -0.0190 -0.0184 0.0028  59  GLN   C CB  
1488 C  CG  . GLN   B 53  ? 0.1891 0.2271 0.1819 -0.0189 -0.0215 0.0052  59  GLN   C CG  
1489 C  CD  . GLN   B 53  ? 0.2186 0.2613 0.2184 -0.0193 -0.0248 0.0079  59  GLN   C CD  
1490 O  OE1 . GLN   B 53  ? 0.2235 0.2672 0.2215 -0.0226 -0.0286 0.0094  59  GLN   C OE1 
1491 N  NE2 . GLN   B 53  ? 0.2053 0.2507 0.2133 -0.0162 -0.0236 0.0082  59  GLN   C NE2 
1492 N  N   . THR   B 54  ? 0.1488 0.1762 0.1348 -0.0180 -0.0121 -0.0027 60  THR   C N   
1493 C  CA  . THR   B 54  ? 0.1647 0.1896 0.1512 -0.0173 -0.0106 -0.0032 60  THR   C CA  
1494 C  C   . THR   B 54  ? 0.1654 0.1860 0.1501 -0.0160 -0.0099 -0.0048 60  THR   C C   
1495 O  O   . THR   B 54  ? 0.1617 0.1810 0.1450 -0.0168 -0.0098 -0.0065 60  THR   C O   
1496 C  CB  . THR   B 54  ? 0.2220 0.2465 0.2086 -0.0199 -0.0107 -0.0036 60  THR   C CB  
1497 O  OG1 . THR   B 54  ? 0.2604 0.2821 0.2446 -0.0217 -0.0110 -0.0058 60  THR   C OG1 
1498 C  CG2 . THR   B 54  ? 0.2239 0.2532 0.2135 -0.0216 -0.0118 -0.0021 60  THR   C CG2 
1499 N  N   . GLY   B 55  ? 0.1460 0.1643 0.1308 -0.0143 -0.0095 -0.0043 61  GLY   C N   
1500 C  CA  . GLY   B 55  ? 0.1426 0.1569 0.1272 -0.0130 -0.0096 -0.0054 61  GLY   C CA  
1501 C  C   . GLY   B 55  ? 0.1520 0.1635 0.1357 -0.0120 -0.0101 -0.0041 61  GLY   C C   
1502 O  O   . GLY   B 55  ? 0.1560 0.1682 0.1385 -0.0129 -0.0096 -0.0028 61  GLY   C O   
1503 N  N   . VAL   B 56  ? 0.1401 0.1486 0.1244 -0.0105 -0.0110 -0.0045 62  VAL   C N   
1504 C  CA  . VAL   B 56  ? 0.1356 0.1405 0.1178 -0.0101 -0.0123 -0.0030 62  VAL   C CA  
1505 C  C   . VAL   B 56  ? 0.1403 0.1450 0.1225 -0.0081 -0.0130 -0.0033 62  VAL   C C   
1506 O  O   . VAL   B 56  ? 0.1475 0.1524 0.1330 -0.0071 -0.0132 -0.0047 62  VAL   C O   
1507 C  CB  . VAL   B 56  ? 0.1468 0.1470 0.1310 -0.0106 -0.0143 -0.0030 62  VAL   C CB  
1508 C  CG1 . VAL   B 56  ? 0.1613 0.1571 0.1426 -0.0106 -0.0169 -0.0007 62  VAL   C CG1 
1509 C  CG2 . VAL   B 56  ? 0.1494 0.1493 0.1337 -0.0127 -0.0137 -0.0029 62  VAL   C CG2 
1510 N  N   . TYR   B 57  ? 0.1359 0.1396 0.1143 -0.0080 -0.0132 -0.0022 63  TYR   C N   
1511 C  CA  . TYR   B 57  ? 0.1417 0.1444 0.1197 -0.0064 -0.0143 -0.0025 63  TYR   C CA  
1512 C  C   . TYR   B 57  ? 0.1469 0.1448 0.1213 -0.0070 -0.0169 -0.0012 63  TYR   C C   
1513 O  O   . TYR   B 57  ? 0.1587 0.1544 0.1287 -0.0089 -0.0172 0.0003  63  TYR   C O   
1514 C  CB  . TYR   B 57  ? 0.1468 0.1526 0.1240 -0.0056 -0.0122 -0.0031 63  TYR   C CB  
1515 C  CG  . TYR   B 57  ? 0.1536 0.1590 0.1261 -0.0064 -0.0108 -0.0028 63  TYR   C CG  
1516 C  CD1 . TYR   B 57  ? 0.1694 0.1772 0.1415 -0.0079 -0.0086 -0.0024 63  TYR   C CD1 
1517 C  CD2 . TYR   B 57  ? 0.1552 0.1582 0.1240 -0.0061 -0.0111 -0.0033 63  TYR   C CD2 
1518 C  CE1 . TYR   B 57  ? 0.1768 0.1847 0.1452 -0.0089 -0.0061 -0.0026 63  TYR   C CE1 
1519 C  CE2 . TYR   B 57  ? 0.1620 0.1645 0.1259 -0.0074 -0.0088 -0.0037 63  TYR   C CE2 
1520 C  CZ  . TYR   B 57  ? 0.1899 0.1951 0.1539 -0.0088 -0.0060 -0.0035 63  TYR   C CZ  
1521 O  OH  . TYR   B 57  ? 0.2206 0.2256 0.1801 -0.0103 -0.0028 -0.0044 63  TYR   C OH  
1522 N  N   . TYR   B 58  ? 0.1493 0.1456 0.1252 -0.0058 -0.0191 -0.0016 64  TYR   C N   
1523 C  CA  . TYR   B 58  ? 0.1585 0.1499 0.1305 -0.0067 -0.0226 -0.0001 64  TYR   C CA  
1524 C  C   . TYR   B 58  ? 0.1740 0.1649 0.1393 -0.0072 -0.0216 -0.0005 64  TYR   C C   
1525 O  O   . TYR   B 58  ? 0.1633 0.1565 0.1307 -0.0057 -0.0203 -0.0021 64  TYR   C O   
1526 C  CB  . TYR   B 58  ? 0.1628 0.1526 0.1410 -0.0054 -0.0262 -0.0002 64  TYR   C CB  
1527 C  CG  . TYR   B 58  ? 0.1803 0.1648 0.1543 -0.0067 -0.0310 0.0019  64  TYR   C CG  
1528 C  CD1 . TYR   B 58  ? 0.2013 0.1815 0.1714 -0.0087 -0.0336 0.0046  64  TYR   C CD1 
1529 C  CD2 . TYR   B 58  ? 0.2060 0.1893 0.1789 -0.0064 -0.0333 0.0016  64  TYR   C CD2 
1530 C  CE1 . TYR   B 58  ? 0.2208 0.1955 0.1854 -0.0106 -0.0387 0.0072  64  TYR   C CE1 
1531 C  CE2 . TYR   B 58  ? 0.2237 0.2018 0.1914 -0.0082 -0.0383 0.0038  64  TYR   C CE2 
1532 C  CZ  . TYR   B 58  ? 0.2419 0.2156 0.2050 -0.0104 -0.0411 0.0067  64  TYR   C CZ  
1533 O  OH  . TYR   B 58  ? 0.2858 0.2537 0.2427 -0.0128 -0.0470 0.0095  64  TYR   C OH  
1534 N  N   . CYS   B 59  ? 0.1775 0.1650 0.1347 -0.0097 -0.0221 0.0009  65  CYS   C N   
1535 C  CA  . CYS   B 59  ? 0.1817 0.1680 0.1314 -0.0108 -0.0204 -0.0002 65  CYS   C CA  
1536 C  C   . CYS   B 59  ? 0.2055 0.1858 0.1488 -0.0128 -0.0253 0.0013  65  CYS   C C   
1537 O  O   . CYS   B 59  ? 0.2308 0.2069 0.1674 -0.0157 -0.0274 0.0038  65  CYS   C O   
1538 C  CB  . CYS   B 59  ? 0.2071 0.1947 0.1518 -0.0129 -0.0162 -0.0003 65  CYS   C CB  
1539 S  SG  . CYS   B 59  ? 0.2361 0.2219 0.1710 -0.0150 -0.0129 -0.0025 65  CYS   C SG  
1540 N  N   . SER   B 60  ? 0.1952 0.1747 0.1404 -0.0115 -0.0276 0.0002  66  SER   C N   
1541 C  CA  . SER   B 60  ? 0.2210 0.1948 0.1608 -0.0135 -0.0332 0.0019  66  SER   C CA  
1542 C  C   . SER   B 60  ? 0.2224 0.1918 0.1485 -0.0174 -0.0327 0.0021  66  SER   C C   
1543 O  O   . SER   B 60  ? 0.2343 0.1982 0.1535 -0.0204 -0.0377 0.0050  66  SER   C O   
1544 C  CB  . SER   B 60  ? 0.2771 0.2512 0.2221 -0.0117 -0.0359 0.0005  66  SER   C CB  
1545 O  OG  . SER   B 60  ? 0.3363 0.3115 0.2780 -0.0114 -0.0323 -0.0024 66  SER   C OG  
1546 N  N   . SER   B 61  ? 0.2170 0.1887 0.1391 -0.0177 -0.0266 -0.0008 67  SER   C N   
1547 C  CA  . SER   B 61  ? 0.2220 0.1897 0.1304 -0.0219 -0.0247 -0.0015 67  SER   C CA  
1548 C  C   . SER   B 61  ? 0.2324 0.1979 0.1337 -0.0255 -0.0241 0.0013  67  SER   C C   
1549 O  O   . SER   B 61  ? 0.2522 0.2137 0.1407 -0.0299 -0.0226 0.0012  67  SER   C O   
1550 C  CB  . SER   B 61  ? 0.2364 0.2073 0.1444 -0.0210 -0.0177 -0.0060 67  SER   C CB  
1551 O  OG  . SER   B 61  ? 0.2503 0.2272 0.1656 -0.0191 -0.0126 -0.0068 67  SER   C OG  
1552 N  N   . ARG   B 62  ? 0.2215 0.1890 0.1303 -0.0241 -0.0251 0.0037  68  ARG   C N   
1553 C  CA  . ARG   B 62  ? 0.2299 0.1950 0.1335 -0.0274 -0.0255 0.0070  68  ARG   C CA  
1554 C  C   . ARG   B 62  ? 0.2526 0.2141 0.1613 -0.0269 -0.0328 0.0111  68  ARG   C C   
1555 O  O   . ARG   B 62  ? 0.2740 0.2324 0.1793 -0.0296 -0.0343 0.0145  68  ARG   C O   
1556 C  CB  . ARG   B 62  ? 0.2380 0.2092 0.1473 -0.0263 -0.0191 0.0056  68  ARG   C CB  
1557 C  CG  . ARG   B 62  ? 0.2469 0.2217 0.1530 -0.0269 -0.0118 0.0016  68  ARG   C CG  
1558 C  CD  . ARG   B 62  ? 0.2734 0.2436 0.1651 -0.0326 -0.0096 0.0022  68  ARG   C CD  
1559 N  NE  . ARG   B 62  ? 0.3175 0.2913 0.2071 -0.0334 -0.0017 -0.0022 68  ARG   C NE  
1560 C  CZ  . ARG   B 62  ? 0.3784 0.3507 0.2628 -0.0338 0.0003  -0.0059 68  ARG   C CZ  
1561 N  NH1 . ARG   B 62  ? 0.3701 0.3376 0.2503 -0.0337 -0.0053 -0.0053 68  ARG   C NH1 
1562 N  NH2 . ARG   B 62  ? 0.4064 0.3820 0.2905 -0.0344 0.0080  -0.0103 68  ARG   C NH2 
1563 N  N   . ARG   B 63  ? 0.2462 0.2085 0.1642 -0.0235 -0.0370 0.0108  69  ARG   C N   
1564 C  CA  . ARG   B 63  ? 0.2470 0.2071 0.1736 -0.0221 -0.0432 0.0138  69  ARG   C CA  
1565 C  C   . ARG   B 63  ? 0.2515 0.2136 0.1839 -0.0215 -0.0408 0.0146  69  ARG   C C   
1566 O  O   . ARG   B 63  ? 0.2658 0.2234 0.1984 -0.0230 -0.0450 0.0181  69  ARG   C O   
1567 C  CB  . ARG   B 63  ? 0.2905 0.2426 0.2092 -0.0257 -0.0509 0.0182  69  ARG   C CB  
1568 C  CG  . ARG   B 63  ? 0.3698 0.3194 0.2829 -0.0267 -0.0543 0.0175  69  ARG   C CG  
1569 C  CD  . ARG   B 63  ? 0.4451 0.3967 0.3711 -0.0229 -0.0583 0.0166  69  ARG   C CD  
1570 N  NE  . ARG   B 63  ? 0.5013 0.4492 0.4215 -0.0248 -0.0635 0.0170  69  ARG   C NE  
1571 C  CZ  . ARG   B 63  ? 0.5398 0.4898 0.4578 -0.0242 -0.0606 0.0133  69  ARG   C CZ  
1572 N  NH1 . ARG   B 63  ? 0.5012 0.4571 0.4231 -0.0214 -0.0529 0.0093  69  ARG   C NH1 
1573 N  NH2 . ARG   B 63  ? 0.5660 0.5120 0.4784 -0.0263 -0.0658 0.0137  69  ARG   C NH2 
1574 N  N   . LYS   B 64  ? 0.2431 0.2115 0.1794 -0.0196 -0.0343 0.0114  70  LYS   C N   
1575 C  CA  . LYS   B 64  ? 0.2484 0.2188 0.1888 -0.0196 -0.0318 0.0118  70  LYS   C CA  
1576 C  C   . LYS   B 64  ? 0.2214 0.1986 0.1713 -0.0161 -0.0278 0.0084  70  LYS   C C   
1577 O  O   . LYS   B 64  ? 0.2160 0.1969 0.1665 -0.0145 -0.0252 0.0059  70  LYS   C O   
1578 C  CB  . LYS   B 64  ? 0.3031 0.2740 0.2343 -0.0231 -0.0271 0.0121  70  LYS   C CB  
1579 C  CG  . LYS   B 64  ? 0.4358 0.4002 0.3572 -0.0278 -0.0298 0.0161  70  LYS   C CG  
1580 C  CD  . LYS   B 64  ? 0.5219 0.4886 0.4366 -0.0311 -0.0235 0.0155  70  LYS   C CD  
1581 C  CE  . LYS   B 64  ? 0.6135 0.5745 0.5196 -0.0362 -0.0250 0.0196  70  LYS   C CE  
1582 N  NZ  . LYS   B 64  ? 0.6603 0.6137 0.5540 -0.0401 -0.0295 0.0227  70  LYS   C NZ  
1583 N  N   . HIS   B 65  ? 0.2032 0.1817 0.1593 -0.0156 -0.0271 0.0085  71  HIS   C N   
1584 C  CA  . HIS   B 65  ? 0.1815 0.1661 0.1444 -0.0134 -0.0233 0.0056  71  HIS   C CA  
1585 C  C   . HIS   B 65  ? 0.2002 0.1875 0.1599 -0.0154 -0.0193 0.0057  71  HIS   C C   
1586 O  O   . HIS   B 65  ? 0.2367 0.2209 0.1924 -0.0182 -0.0199 0.0079  71  HIS   C O   
1587 C  CB  . HIS   B 65  ? 0.1834 0.1675 0.1550 -0.0121 -0.0249 0.0051  71  HIS   C CB  
1588 C  CG  . HIS   B 65  ? 0.1995 0.1819 0.1770 -0.0099 -0.0283 0.0046  71  HIS   C CG  
1589 N  ND1 . HIS   B 65  ? 0.2267 0.2132 0.2106 -0.0076 -0.0265 0.0017  71  HIS   C ND1 
1590 C  CD2 . HIS   B 65  ? 0.2138 0.1911 0.1927 -0.0101 -0.0335 0.0068  71  HIS   C CD2 
1591 C  CE1 . HIS   B 65  ? 0.2039 0.1881 0.1934 -0.0063 -0.0301 0.0018  71  HIS   C CE1 
1592 N  NE2 . HIS   B 65  ? 0.2278 0.2066 0.2150 -0.0076 -0.0347 0.0049  71  HIS   C NE2 
1593 N  N   . TYR   B 66  ? 0.1656 0.1588 0.1279 -0.0141 -0.0155 0.0035  72  TYR   C N   
1594 C  CA  . TYR   B 66  ? 0.1763 0.1730 0.1378 -0.0158 -0.0119 0.0033  72  TYR   C CA  
1595 C  C   . TYR   B 66  ? 0.1711 0.1725 0.1395 -0.0146 -0.0107 0.0019  72  TYR   C C   
1596 O  O   . TYR   B 66  ? 0.1692 0.1732 0.1412 -0.0123 -0.0106 0.0003  72  TYR   C O   
1597 C  CB  . TYR   B 66  ? 0.1894 0.1892 0.1481 -0.0157 -0.0084 0.0021  72  TYR   C CB  
1598 C  CG  . TYR   B 66  ? 0.2053 0.2007 0.1550 -0.0180 -0.0084 0.0030  72  TYR   C CG  
1599 C  CD1 . TYR   B 66  ? 0.2293 0.2227 0.1732 -0.0218 -0.0070 0.0047  72  TYR   C CD1 
1600 C  CD2 . TYR   B 66  ? 0.2214 0.2144 0.1677 -0.0170 -0.0097 0.0022  72  TYR   C CD2 
1601 C  CE1 . TYR   B 66  ? 0.2430 0.2319 0.1767 -0.0248 -0.0067 0.0056  72  TYR   C CE1 
1602 C  CE2 . TYR   B 66  ? 0.2368 0.2252 0.1732 -0.0198 -0.0100 0.0029  72  TYR   C CE2 
1603 C  CZ  . TYR   B 66  ? 0.2551 0.2415 0.1849 -0.0238 -0.0084 0.0046  72  TYR   C CZ  
1604 O  OH  . TYR   B 66  ? 0.2845 0.2661 0.2027 -0.0274 -0.0081 0.0052  72  TYR   C OH  
1605 N  N   . PRO   B 67  ? 0.1631 0.1653 0.1327 -0.0166 -0.0099 0.0025  73  PRO   C N   
1606 C  CA  . PRO   B 67  ? 0.1685 0.1751 0.1434 -0.0162 -0.0090 0.0011  73  PRO   C CA  
1607 C  C   . PRO   B 67  ? 0.1757 0.1883 0.1523 -0.0159 -0.0063 0.0005  73  PRO   C C   
1608 O  O   . PRO   B 67  ? 0.1915 0.2051 0.1661 -0.0174 -0.0041 0.0012  73  PRO   C O   
1609 C  CB  . PRO   B 67  ? 0.1789 0.1837 0.1541 -0.0188 -0.0094 0.0020  73  PRO   C CB  
1610 C  CG  . PRO   B 67  ? 0.1950 0.1966 0.1649 -0.0211 -0.0091 0.0043  73  PRO   C CG  
1611 C  CD  . PRO   B 67  ? 0.1775 0.1765 0.1431 -0.0198 -0.0099 0.0047  73  PRO   C CD  
1612 N  N   . VAL   B 68  ? 0.1581 0.1743 0.1384 -0.0142 -0.0064 -0.0006 74  VAL   C N   
1613 C  CA  . VAL   B 68  ? 0.1563 0.1779 0.1400 -0.0137 -0.0047 -0.0008 74  VAL   C CA  
1614 C  C   . VAL   B 68  ? 0.1504 0.1758 0.1383 -0.0137 -0.0060 -0.0009 74  VAL   C C   
1615 O  O   . VAL   B 68  ? 0.1705 0.1943 0.1577 -0.0137 -0.0076 -0.0015 74  VAL   C O   
1616 C  CB  . VAL   B 68  ? 0.1731 0.1947 0.1565 -0.0112 -0.0041 -0.0015 74  VAL   C CB  
1617 C  CG1 . VAL   B 68  ? 0.1870 0.2056 0.1655 -0.0117 -0.0025 -0.0016 74  VAL   C CG1 
1618 C  CG2 . VAL   B 68  ? 0.1783 0.1979 0.1615 -0.0095 -0.0063 -0.0020 74  VAL   C CG2 
1619 N  N   . SER   B 69  ? 0.1301 0.1608 0.1229 -0.0139 -0.0052 -0.0005 75  SER   C N   
1620 C  CA  . SER   B 69  ? 0.1433 0.1777 0.1402 -0.0138 -0.0072 0.0000  75  SER   C CA  
1621 C  C   . SER   B 69  ? 0.1426 0.1776 0.1414 -0.0110 -0.0074 0.0000  75  SER   C C   
1622 O  O   . SER   B 69  ? 0.1464 0.1813 0.1460 -0.0094 -0.0052 -0.0007 75  SER   C O   
1623 C  CB  . SER   B 69  ? 0.1868 0.2265 0.1898 -0.0153 -0.0071 0.0008  75  SER   C CB  
1624 O  OG  . SER   B 69  ? 0.2297 0.2686 0.2311 -0.0182 -0.0071 0.0008  75  SER   C OG  
1625 N  N   . PHE   B 70  ? 0.1284 0.1637 0.1275 -0.0106 -0.0098 0.0006  76  PHE   C N   
1626 C  CA  . PHE   B 70  ? 0.1394 0.1747 0.1405 -0.0082 -0.0104 0.0010  76  PHE   C CA  
1627 C  C   . PHE   B 70  ? 0.1388 0.1769 0.1435 -0.0087 -0.0136 0.0029  76  PHE   C C   
1628 O  O   . PHE   B 70  ? 0.1585 0.1975 0.1615 -0.0113 -0.0156 0.0038  76  PHE   C O   
1629 C  CB  . PHE   B 70  ? 0.1417 0.1725 0.1379 -0.0072 -0.0101 0.0001  76  PHE   C CB  
1630 C  CG  . PHE   B 70  ? 0.1384 0.1670 0.1302 -0.0090 -0.0112 -0.0003 76  PHE   C CG  
1631 C  CD1 . PHE   B 70  ? 0.1442 0.1702 0.1331 -0.0100 -0.0103 -0.0016 76  PHE   C CD1 
1632 C  CD2 . PHE   B 70  ? 0.1380 0.1666 0.1287 -0.0097 -0.0128 0.0004  76  PHE   C CD2 
1633 C  CE1 . PHE   B 70  ? 0.1610 0.1850 0.1473 -0.0115 -0.0106 -0.0027 76  PHE   C CE1 
1634 C  CE2 . PHE   B 70  ? 0.1366 0.1632 0.1232 -0.0117 -0.0127 -0.0007 76  PHE   C CE2 
1635 C  CZ  . PHE   B 70  ? 0.1421 0.1665 0.1271 -0.0124 -0.0114 -0.0026 76  PHE   C CZ  
1636 N  N   . SER   B 71  ? 0.1282 0.1674 0.1379 -0.0065 -0.0143 0.0038  77  SER   C N   
1637 C  CA  . SER   B 71  ? 0.1368 0.1784 0.1509 -0.0069 -0.0182 0.0064  77  SER   C CA  
1638 C  C   . SER   B 71  ? 0.1552 0.1939 0.1630 -0.0086 -0.0208 0.0078  77  SER   C C   
1639 O  O   . SER   B 71  ? 0.1699 0.2051 0.1709 -0.0092 -0.0192 0.0063  77  SER   C O   
1640 C  CB  . SER   B 71  ? 0.1501 0.1938 0.1735 -0.0039 -0.0182 0.0068  77  SER   C CB  
1641 O  OG  . SER   B 71  ? 0.1712 0.2112 0.1926 -0.0017 -0.0168 0.0057  77  SER   C OG  
1642 N  N   . LYS   B 72  ? 0.1528 0.1928 0.1629 -0.0097 -0.0251 0.0109  78  LYS   C N   
1643 C  CA  . LYS   B 72  ? 0.1740 0.2111 0.1774 -0.0120 -0.0275 0.0126  78  LYS   C CA  
1644 C  C   . LYS   B 72  ? 0.1794 0.2138 0.1844 -0.0094 -0.0272 0.0131  78  LYS   C C   
1645 O  O   . LYS   B 72  ? 0.2072 0.2429 0.2206 -0.0063 -0.0272 0.0134  78  LYS   C O   
1646 C  CB  . LYS   B 72  ? 0.1949 0.2338 0.1995 -0.0147 -0.0330 0.0164  78  LYS   C CB  
1647 C  CG  . LYS   B 72  ? 0.2464 0.2878 0.2494 -0.0176 -0.0335 0.0157  78  LYS   C CG  
1648 C  CD  . LYS   B 72  ? 0.3588 0.4016 0.3613 -0.0212 -0.0397 0.0194  78  LYS   C CD  
1649 C  CE  . LYS   B 72  ? 0.4600 0.5017 0.4531 -0.0258 -0.0394 0.0178  78  LYS   C CE  
1650 N  NZ  . LYS   B 72  ? 0.5164 0.5534 0.4983 -0.0278 -0.0366 0.0158  78  LYS   C NZ  
1651 N  N   . PRO   B 73  ? 0.1662 0.1971 0.1642 -0.0109 -0.0267 0.0131  79  PRO   C N   
1652 C  CA  . PRO   B 73  ? 0.1833 0.2115 0.1830 -0.0088 -0.0265 0.0136  79  PRO   C CA  
1653 C  C   . PRO   B 73  ? 0.1957 0.2243 0.2021 -0.0078 -0.0308 0.0173  79  PRO   C C   
1654 O  O   . PRO   B 73  ? 0.2086 0.2378 0.2138 -0.0106 -0.0351 0.0208  79  PRO   C O   
1655 C  CB  . PRO   B 73  ? 0.2016 0.2266 0.1928 -0.0117 -0.0256 0.0135  79  PRO   C CB  
1656 C  CG  . PRO   B 73  ? 0.2193 0.2451 0.2043 -0.0150 -0.0247 0.0121  79  PRO   C CG  
1657 C  CD  . PRO   B 73  ? 0.1728 0.2020 0.1615 -0.0147 -0.0258 0.0121  79  PRO   C CD  
1658 N  N   . SER   B 74  ? 0.1860 0.2141 0.1998 -0.0040 -0.0298 0.0165  80  SER   C N   
1659 C  CA  . SER   B 74  ? 0.2055 0.2339 0.2283 -0.0025 -0.0339 0.0197  80  SER   C CA  
1660 C  C   . SER   B 74  ? 0.1984 0.2241 0.2267 0.0011  -0.0323 0.0182  80  SER   C C   
1661 O  O   . SER   B 74  ? 0.1837 0.2074 0.2080 0.0020  -0.0284 0.0148  80  SER   C O   
1662 C  CB  . SER   B 74  ? 0.2585 0.2919 0.2903 -0.0014 -0.0351 0.0200  80  SER   C CB  
1663 O  OG  . SER   B 74  ? 0.3188 0.3543 0.3562 0.0018  -0.0304 0.0158  80  SER   C OG  
1664 N  N   . LEU   B 75  ? 0.1837 0.2089 0.2212 0.0028  -0.0360 0.0209  81  LEU   C N   
1665 C  CA  . LEU   B 75  ? 0.1912 0.2135 0.2356 0.0063  -0.0349 0.0194  81  LEU   C CA  
1666 C  C   . LEU   B 75  ? 0.2049 0.2305 0.2583 0.0098  -0.0311 0.0152  81  LEU   C C   
1667 O  O   . LEU   B 75  ? 0.2200 0.2498 0.2831 0.0108  -0.0328 0.0163  81  LEU   C O   
1668 C  CB  . LEU   B 75  ? 0.2146 0.2351 0.2668 0.0065  -0.0411 0.0245  81  LEU   C CB  
1669 C  CG  . LEU   B 75  ? 0.2653 0.2806 0.3100 0.0036  -0.0442 0.0283  81  LEU   C CG  
1670 C  CD1 . LEU   B 75  ? 0.2944 0.3082 0.3457 0.0028  -0.0518 0.0347  81  LEU   C CD1 
1671 C  CD2 . LEU   B 75  ? 0.2863 0.2973 0.3304 0.0054  -0.0410 0.0254  81  LEU   C CD2 
1672 N  N   . ILE   B 76  ? 0.1897 0.2137 0.2406 0.0114  -0.0259 0.0105  82  ILE   C N   
1673 C  CA  . ILE   B 76  ? 0.2032 0.2296 0.2596 0.0138  -0.0211 0.0058  82  ILE   C CA  
1674 C  C   . ILE   B 76  ? 0.2064 0.2289 0.2661 0.0164  -0.0185 0.0023  82  ILE   C C   
1675 O  O   . ILE   B 76  ? 0.1896 0.2075 0.2421 0.0157  -0.0184 0.0019  82  ILE   C O   
1676 C  CB  . ILE   B 76  ? 0.2326 0.2606 0.2794 0.0119  -0.0172 0.0033  82  ILE   C CB  
1677 C  CG1 . ILE   B 76  ? 0.2658 0.2979 0.3111 0.0094  -0.0196 0.0062  82  ILE   C CG1 
1678 C  CG2 . ILE   B 76  ? 0.2564 0.2856 0.3055 0.0135  -0.0115 -0.0018 82  ILE   C CG2 
1679 C  CD1 . ILE   B 76  ? 0.3070 0.3403 0.3444 0.0075  -0.0167 0.0044  82  ILE   C CD1 
1680 N  N   . PHE   B 77  ? 0.2213 0.2456 0.2925 0.0193  -0.0161 -0.0006 83  PHE   C N   
1681 C  CA  . PHE   B 77  ? 0.2421 0.2623 0.3168 0.0217  -0.0132 -0.0047 83  PHE   C CA  
1682 C  C   . PHE   B 77  ? 0.2392 0.2573 0.3026 0.0205  -0.0079 -0.0095 83  PHE   C C   
1683 O  O   . PHE   B 77  ? 0.2461 0.2676 0.3054 0.0193  -0.0045 -0.0114 83  PHE   C O   
1684 C  CB  . PHE   B 77  ? 0.2613 0.2844 0.3524 0.0250  -0.0113 -0.0072 83  PHE   C CB  
1685 C  CG  . PHE   B 77  ? 0.2935 0.3117 0.3892 0.0275  -0.0084 -0.0118 83  PHE   C CG  
1686 C  CD1 . PHE   B 77  ? 0.3259 0.3439 0.4195 0.0279  -0.0013 -0.0187 83  PHE   C CD1 
1687 C  CD2 . PHE   B 77  ? 0.3206 0.3338 0.4210 0.0288  -0.0128 -0.0094 83  PHE   C CD2 
1688 C  CE1 . PHE   B 77  ? 0.3388 0.3518 0.4355 0.0297  0.0016  -0.0235 83  PHE   C CE1 
1689 C  CE2 . PHE   B 77  ? 0.3426 0.3508 0.4473 0.0309  -0.0101 -0.0140 83  PHE   C CE2 
1690 C  CZ  . PHE   B 77  ? 0.3388 0.3469 0.4416 0.0314  -0.0029 -0.0213 83  PHE   C CZ  
1691 N  N   . VAL   B 78  ? 0.2312 0.2437 0.2895 0.0206  -0.0078 -0.0111 84  VAL   C N   
1692 C  CA  . VAL   B 78  ? 0.2354 0.2449 0.2828 0.0192  -0.0041 -0.0152 84  VAL   C CA  
1693 C  C   . VAL   B 78  ? 0.2503 0.2553 0.3012 0.0209  -0.0015 -0.0199 84  VAL   C C   
1694 O  O   . VAL   B 78  ? 0.2455 0.2466 0.3007 0.0221  -0.0044 -0.0187 84  VAL   C O   
1695 C  CB  . VAL   B 78  ? 0.2260 0.2327 0.2627 0.0167  -0.0071 -0.0125 84  VAL   C CB  
1696 C  CG1 . VAL   B 78  ? 0.2265 0.2299 0.2529 0.0153  -0.0044 -0.0163 84  VAL   C CG1 
1697 C  CG2 . VAL   B 78  ? 0.2075 0.2181 0.2407 0.0148  -0.0093 -0.0084 84  VAL   C CG2 
1698 N  N   . GLU   B 79  ? 0.2633 0.2680 0.3106 0.0206  0.0041  -0.0255 85  GLU   C N   
1699 C  CA  . GLU   B 79  ? 0.2714 0.2714 0.3202 0.0216  0.0075  -0.0312 85  GLU   C CA  
1700 C  C   . GLU   B 79  ? 0.2659 0.2594 0.3072 0.0205  0.0047  -0.0311 85  GLU   C C   
1701 O  O   . GLU   B 79  ? 0.2566 0.2494 0.2885 0.0183  0.0017  -0.0280 85  GLU   C O   
1702 C  CB  . GLU   B 79  ? 0.3101 0.3106 0.3514 0.0198  0.0140  -0.0367 85  GLU   C CB  
1703 C  CG  . GLU   B 79  ? 0.3774 0.3843 0.4257 0.0203  0.0182  -0.0379 85  GLU   C CG  
1704 C  CD  . GLU   B 79  ? 0.4869 0.4958 0.5522 0.0238  0.0211  -0.0412 85  GLU   C CD  
1705 O  OE1 . GLU   B 79  ? 0.5045 0.5198 0.5799 0.0248  0.0225  -0.0404 85  GLU   C OE1 
1706 O  OE2 . GLU   B 79  ? 0.5007 0.5047 0.5701 0.0255  0.0219  -0.0447 85  GLU   C OE2 
1707 N  N   . ALA   B 80  ? 0.2598 0.2484 0.3058 0.0220  0.0059  -0.0350 86  ALA   C N   
1708 C  CA  . ALA   B 80  ? 0.2568 0.2390 0.2966 0.0208  0.0033  -0.0355 86  ALA   C CA  
1709 C  C   . ALA   B 80  ? 0.2537 0.2338 0.2783 0.0174  0.0047  -0.0379 86  ALA   C C   
1710 O  O   . ALA   B 80  ? 0.2644 0.2457 0.2835 0.0162  0.0093  -0.0417 86  ALA   C O   
1711 C  CB  . ALA   B 80  ? 0.2613 0.2383 0.3091 0.0229  0.0051  -0.0403 86  ALA   C CB  
1712 N  N   . SER   B 81  ? 0.2356 0.2124 0.2536 0.0156  0.0007  -0.0357 87  SER   C N   
1713 C  CA  . SER   B 81  ? 0.2203 0.1943 0.2252 0.0124  0.0003  -0.0373 87  SER   C CA  
1714 C  C   . SER   B 81  ? 0.2430 0.2109 0.2470 0.0117  -0.0028 -0.0382 87  SER   C C   
1715 O  O   . SER   B 81  ? 0.2534 0.2194 0.2665 0.0136  -0.0041 -0.0375 87  SER   C O   
1716 C  CB  . SER   B 81  ? 0.1950 0.1729 0.1943 0.0107  -0.0024 -0.0325 87  SER   C CB  
1717 O  OG  . SER   B 81  ? 0.2093 0.1878 0.2127 0.0111  -0.0068 -0.0278 87  SER   C OG  
1718 N  N   . GLU   B 82  ? 0.2529 0.2176 0.2464 0.0087  -0.0045 -0.0394 88  GLU   C N   
1719 C  CA  . GLU   B 82  ? 0.2662 0.2257 0.2592 0.0075  -0.0080 -0.0398 88  GLU   C CA  
1720 C  C   . GLU   B 82  ? 0.2676 0.2296 0.2664 0.0079  -0.0124 -0.0337 88  GLU   C C   
1721 O  O   . GLU   B 82  ? 0.2750 0.2335 0.2771 0.0075  -0.0150 -0.0332 88  GLU   C O   
1722 C  CB  . GLU   B 82  ? 0.3207 0.2767 0.3013 0.0039  -0.0094 -0.0421 88  GLU   C CB  
1723 C  CG  . GLU   B 82  ? 0.4136 0.3737 0.3886 0.0024  -0.0117 -0.0381 88  GLU   C CG  
1724 C  CD  . GLU   B 82  ? 0.5345 0.4963 0.5013 0.0011  -0.0087 -0.0392 88  GLU   C CD  
1725 O  OE1 . GLU   B 82  ? 0.5660 0.5263 0.5234 -0.0019 -0.0114 -0.0385 88  GLU   C OE1 
1726 O  OE2 . GLU   B 82  ? 0.5209 0.4857 0.4913 0.0028  -0.0042 -0.0404 88  GLU   C OE2 
1727 N  N   . TYR   B 83  ? 0.2571 0.2249 0.2572 0.0084  -0.0128 -0.0294 89  TYR   C N   
1728 C  CA  . TYR   B 83  ? 0.2592 0.2296 0.2629 0.0080  -0.0159 -0.0241 89  TYR   C CA  
1729 C  C   . TYR   B 83  ? 0.2672 0.2390 0.2802 0.0100  -0.0162 -0.0210 89  TYR   C C   
1730 O  O   . TYR   B 83  ? 0.2921 0.2637 0.3082 0.0092  -0.0188 -0.0174 89  TYR   C O   
1731 C  CB  . TYR   B 83  ? 0.2530 0.2283 0.2522 0.0069  -0.0163 -0.0215 89  TYR   C CB  
1732 C  CG  . TYR   B 83  ? 0.2561 0.2299 0.2467 0.0049  -0.0169 -0.0236 89  TYR   C CG  
1733 C  CD1 . TYR   B 83  ? 0.2792 0.2508 0.2678 0.0029  -0.0204 -0.0232 89  TYR   C CD1 
1734 C  CD2 . TYR   B 83  ? 0.2670 0.2414 0.2515 0.0046  -0.0144 -0.0257 89  TYR   C CD2 
1735 C  CE1 . TYR   B 83  ? 0.3057 0.2756 0.2867 0.0008  -0.0221 -0.0245 89  TYR   C CE1 
1736 C  CE2 . TYR   B 83  ? 0.2916 0.2641 0.2673 0.0021  -0.0158 -0.0266 89  TYR   C CE2 
1737 C  CZ  . TYR   B 83  ? 0.3253 0.2954 0.2992 0.0004  -0.0200 -0.0259 89  TYR   C CZ  
1738 O  OH  . TYR   B 83  ? 0.3600 0.3278 0.3256 -0.0022 -0.0225 -0.0264 89  TYR   C OH  
1739 N  N   . TYR   B 84  ? 0.2557 0.2291 0.2732 0.0123  -0.0137 -0.0221 90  TYR   C N   
1740 C  CA  . TYR   B 84  ? 0.2464 0.2211 0.2732 0.0141  -0.0149 -0.0186 90  TYR   C CA  
1741 C  C   . TYR   B 84  ? 0.2610 0.2346 0.2957 0.0170  -0.0124 -0.0220 90  TYR   C C   
1742 O  O   . TYR   B 84  ? 0.2553 0.2300 0.2875 0.0175  -0.0084 -0.0264 90  TYR   C O   
1743 C  CB  . TYR   B 84  ? 0.2282 0.2092 0.2547 0.0139  -0.0153 -0.0146 90  TYR   C CB  
1744 C  CG  . TYR   B 84  ? 0.2168 0.2000 0.2368 0.0113  -0.0169 -0.0115 90  TYR   C CG  
1745 C  CD1 . TYR   B 84  ? 0.2100 0.1957 0.2231 0.0102  -0.0155 -0.0128 90  TYR   C CD1 
1746 C  CD2 . TYR   B 84  ? 0.2135 0.1960 0.2346 0.0097  -0.0197 -0.0075 90  TYR   C CD2 
1747 C  CE1 . TYR   B 84  ? 0.2072 0.1951 0.2163 0.0082  -0.0168 -0.0104 90  TYR   C CE1 
1748 C  CE2 . TYR   B 84  ? 0.2123 0.1972 0.2286 0.0073  -0.0203 -0.0055 90  TYR   C CE2 
1749 C  CZ  . TYR   B 84  ? 0.2034 0.1912 0.2145 0.0069  -0.0188 -0.0070 90  TYR   C CZ  
1750 O  OH  . TYR   B 84  ? 0.1883 0.1783 0.1964 0.0048  -0.0193 -0.0055 90  TYR   C OH  
1751 N  N   . PRO   B 85  ? 0.2780 0.2498 0.3230 0.0189  -0.0144 -0.0199 91  PRO   C N   
1752 C  CA  . PRO   B 85  ? 0.2763 0.2484 0.3317 0.0222  -0.0119 -0.0229 91  PRO   C CA  
1753 C  C   . PRO   B 85  ? 0.2764 0.2556 0.3343 0.0230  -0.0108 -0.0209 91  PRO   C C   
1754 O  O   . PRO   B 85  ? 0.2746 0.2575 0.3265 0.0211  -0.0128 -0.0166 91  PRO   C O   
1755 C  CB  . PRO   B 85  ? 0.2888 0.2571 0.3547 0.0236  -0.0161 -0.0193 91  PRO   C CB  
1756 C  CG  . PRO   B 85  ? 0.2994 0.2686 0.3600 0.0208  -0.0205 -0.0125 91  PRO   C CG  
1757 C  CD  . PRO   B 85  ? 0.2841 0.2541 0.3321 0.0180  -0.0191 -0.0141 91  PRO   C CD  
1758 N  N   . ALA   B 86  ? 0.2752 0.2564 0.3429 0.0257  -0.0079 -0.0239 92  ALA   C N   
1759 C  CA  . ALA   B 86  ? 0.2761 0.2643 0.3484 0.0265  -0.0073 -0.0218 92  ALA   C CA  
1760 C  C   . ALA   B 86  ? 0.2675 0.2571 0.3442 0.0262  -0.0137 -0.0140 92  ALA   C C   
1761 O  O   . ALA   B 86  ? 0.2848 0.2702 0.3682 0.0272  -0.0174 -0.0116 92  ALA   C O   
1762 C  CB  . ALA   B 86  ? 0.2783 0.2683 0.3637 0.0298  -0.0034 -0.0263 92  ALA   C CB  
1763 N  N   . ARG   B 87  ? 0.2455 0.2399 0.3163 0.0243  -0.0151 -0.0102 93  ARG   C N   
1764 C  CA  . ARG   B 87  ? 0.2336 0.2287 0.3052 0.0229  -0.0210 -0.0031 93  ARG   C CA  
1765 C  C   . ARG   B 87  ? 0.2386 0.2399 0.3067 0.0213  -0.0215 -0.0004 93  ARG   C C   
1766 O  O   . ARG   B 87  ? 0.2346 0.2393 0.2986 0.0210  -0.0173 -0.0038 93  ARG   C O   
1767 C  CB  . ARG   B 87  ? 0.2342 0.2250 0.2961 0.0200  -0.0231 -0.0008 93  ARG   C CB  
1768 C  CG  . ARG   B 87  ? 0.2067 0.1999 0.2557 0.0173  -0.0209 -0.0017 93  ARG   C CG  
1769 C  CD  . ARG   B 87  ? 0.2221 0.2114 0.2634 0.0154  -0.0208 -0.0027 93  ARG   C CD  
1770 N  NE  . ARG   B 87  ? 0.2116 0.2031 0.2437 0.0124  -0.0210 -0.0009 93  ARG   C NE  
1771 C  CZ  . ARG   B 87  ? 0.2392 0.2337 0.2653 0.0118  -0.0184 -0.0032 93  ARG   C CZ  
1772 N  NH1 . ARG   B 87  ? 0.1940 0.1901 0.2135 0.0093  -0.0188 -0.0017 93  ARG   C NH1 
1773 N  NH2 . ARG   B 87  ? 0.2193 0.2149 0.2463 0.0134  -0.0153 -0.0071 93  ARG   C NH2 
1774 N  N   . TYR   B 88  ? 0.2423 0.2445 0.3107 0.0196  -0.0267 0.0058  94  TYR   C N   
1775 C  CA  . TYR   B 88  ? 0.2535 0.2608 0.3166 0.0173  -0.0274 0.0083  94  TYR   C CA  
1776 C  C   . TYR   B 88  ? 0.2217 0.2274 0.2712 0.0139  -0.0271 0.0091  94  TYR   C C   
1777 O  O   . TYR   B 88  ? 0.2235 0.2254 0.2697 0.0121  -0.0297 0.0120  94  TYR   C O   
1778 C  CB  . TYR   B 88  ? 0.2814 0.2902 0.3505 0.0166  -0.0334 0.0143  94  TYR   C CB  
1779 C  CG  . TYR   B 88  ? 0.3242 0.3360 0.4086 0.0200  -0.0340 0.0136  94  TYR   C CG  
1780 C  CD1 . TYR   B 88  ? 0.3471 0.3652 0.4350 0.0204  -0.0321 0.0122  94  TYR   C CD1 
1781 C  CD2 . TYR   B 88  ? 0.3593 0.3678 0.4560 0.0230  -0.0360 0.0138  94  TYR   C CD2 
1782 C  CE1 . TYR   B 88  ? 0.3791 0.4008 0.4830 0.0235  -0.0321 0.0111  94  TYR   C CE1 
1783 C  CE2 . TYR   B 88  ? 0.3746 0.3861 0.4876 0.0265  -0.0361 0.0125  94  TYR   C CE2 
1784 C  CZ  . TYR   B 88  ? 0.3978 0.4164 0.5146 0.0267  -0.0340 0.0111  94  TYR   C CZ  
1785 O  OH  . TYR   B 88  ? 0.4374 0.4598 0.5720 0.0301  -0.0340 0.0098  94  TYR   C OH  
1786 N  N   . GLN   B 89  ? 0.1845 0.1931 0.2269 0.0128  -0.0237 0.0066  95  GLN   C N   
1787 C  CA  . GLN   B 89  ? 0.1758 0.1838 0.2074 0.0098  -0.0233 0.0072  95  GLN   C CA  
1788 C  C   . GLN   B 89  ? 0.1794 0.1908 0.2080 0.0072  -0.0256 0.0108  95  GLN   C C   
1789 O  O   . GLN   B 89  ? 0.1889 0.2043 0.2208 0.0078  -0.0255 0.0107  95  GLN   C O   
1790 C  CB  . GLN   B 89  ? 0.1657 0.1741 0.1917 0.0100  -0.0191 0.0026  95  GLN   C CB  
1791 C  CG  . GLN   B 89  ? 0.1733 0.1816 0.1903 0.0072  -0.0188 0.0031  95  GLN   C CG  
1792 C  CD  . GLN   B 89  ? 0.1729 0.1799 0.1852 0.0075  -0.0161 -0.0007 95  GLN   C CD  
1793 O  OE1 . GLN   B 89  ? 0.1858 0.1899 0.1993 0.0089  -0.0151 -0.0033 95  GLN   C OE1 
1794 N  NE2 . GLN   B 89  ? 0.1645 0.1731 0.1712 0.0058  -0.0153 -0.0009 95  GLN   C NE2 
1795 N  N   . SER   B 90  ? 0.1638 0.1734 0.1863 0.0041  -0.0277 0.0139  96  SER   C N   
1796 C  CA  . SER   B 90  ? 0.1545 0.1666 0.1724 0.0009  -0.0297 0.0170  96  SER   C CA  
1797 C  C   . SER   B 90  ? 0.1562 0.1702 0.1661 -0.0011 -0.0265 0.0145  96  SER   C C   
1798 O  O   . SER   B 90  ? 0.1605 0.1734 0.1680 -0.0003 -0.0234 0.0111  96  SER   C O   
1799 C  CB  . SER   B 90  ? 0.1866 0.1956 0.2010 -0.0023 -0.0334 0.0216  96  SER   C CB  
1800 O  OG  . SER   B 90  ? 0.2244 0.2306 0.2336 -0.0037 -0.0311 0.0203  96  SER   C OG  
1801 N  N   . HIS   B 91  ? 0.1510 0.1675 0.1571 -0.0037 -0.0277 0.0161  97  HIS   C N   
1802 C  CA  . HIS   B 91  ? 0.1544 0.1723 0.1536 -0.0058 -0.0250 0.0139  97  HIS   C CA  
1803 C  C   . HIS   B 91  ? 0.1646 0.1839 0.1655 -0.0033 -0.0216 0.0099  97  HIS   C C   
1804 O  O   . HIS   B 91  ? 0.1710 0.1899 0.1677 -0.0040 -0.0191 0.0075  97  HIS   C O   
1805 C  CB  . HIS   B 91  ? 0.1612 0.1766 0.1540 -0.0085 -0.0234 0.0135  97  HIS   C CB  
1806 C  CG  . HIS   B 91  ? 0.2008 0.2145 0.1896 -0.0122 -0.0262 0.0175  97  HIS   C CG  
1807 N  ND1 . HIS   B 91  ? 0.2432 0.2578 0.2249 -0.0165 -0.0266 0.0185  97  HIS   C ND1 
1808 C  CD2 . HIS   B 91  ? 0.2249 0.2358 0.2157 -0.0125 -0.0290 0.0208  97  HIS   C CD2 
1809 C  CE1 . HIS   B 91  ? 0.2571 0.2692 0.2352 -0.0197 -0.0295 0.0226  97  HIS   C CE1 
1810 N  NE2 . HIS   B 91  ? 0.2459 0.2557 0.2296 -0.0174 -0.0312 0.0243  97  HIS   C NE2 
1811 N  N   . LEU   B 92  ? 0.1576 0.1785 0.1651 -0.0005 -0.0216 0.0092  98  LEU   C N   
1812 C  CA  . LEU   B 92  ? 0.1487 0.1705 0.1570 0.0014  -0.0183 0.0058  98  LEU   C CA  
1813 C  C   . LEU   B 92  ? 0.1547 0.1804 0.1639 0.0006  -0.0180 0.0058  98  LEU   C C   
1814 O  O   . LEU   B 92  ? 0.1657 0.1940 0.1794 0.0002  -0.0205 0.0081  98  LEU   C O   
1815 C  CB  . LEU   B 92  ? 0.1584 0.1792 0.1730 0.0046  -0.0173 0.0043  98  LEU   C CB  
1816 C  CG  . LEU   B 92  ? 0.1847 0.2053 0.1983 0.0059  -0.0137 0.0005  98  LEU   C CG  
1817 C  CD1 . LEU   B 92  ? 0.1982 0.2155 0.2046 0.0050  -0.0127 -0.0011 98  LEU   C CD1 
1818 C  CD2 . LEU   B 92  ? 0.2109 0.2303 0.2307 0.0086  -0.0123 -0.0015 98  LEU   C CD2 
1819 N  N   . MET   B 93  ? 0.1411 0.1670 0.1467 0.0002  -0.0153 0.0034  99  MET   C N   
1820 C  CA  . MET   B 93  ? 0.1503 0.1795 0.1566 -0.0009 -0.0148 0.0033  99  MET   C CA  
1821 C  C   . MET   B 93  ? 0.1598 0.1891 0.1670 0.0004  -0.0115 0.0008  99  MET   C C   
1822 O  O   . MET   B 93  ? 0.1693 0.1954 0.1723 0.0010  -0.0100 -0.0009 99  MET   C O   
1823 C  CB  . MET   B 93  ? 0.1449 0.1732 0.1446 -0.0036 -0.0148 0.0031  99  MET   C CB  
1824 C  CG  . MET   B 93  ? 0.1885 0.2161 0.1854 -0.0057 -0.0171 0.0050  99  MET   C CG  
1825 S  SD  . MET   B 93  ? 0.2070 0.2330 0.1968 -0.0086 -0.0157 0.0032  99  MET   C SD  
1826 C  CE  . MET   B 93  ? 0.1944 0.2171 0.1835 -0.0066 -0.0134 0.0008  99  MET   C CE  
1827 N  N   . LEU   B 94  ? 0.1416 0.1746 0.1542 0.0007  -0.0105 0.0007  100 LEU   C N   
1828 C  CA  . LEU   B 94  ? 0.1416 0.1749 0.1543 0.0013  -0.0066 -0.0019 100 LEU   C CA  
1829 C  C   . LEU   B 94  ? 0.1356 0.1703 0.1453 -0.0010 -0.0054 -0.0019 100 LEU   C C   
1830 O  O   . LEU   B 94  ? 0.1279 0.1650 0.1390 -0.0026 -0.0074 -0.0003 100 LEU   C O   
1831 C  CB  . LEU   B 94  ? 0.1533 0.1901 0.1756 0.0032  -0.0050 -0.0028 100 LEU   C CB  
1832 C  CG  . LEU   B 94  ? 0.1855 0.2206 0.2128 0.0058  -0.0059 -0.0030 100 LEU   C CG  
1833 C  CD1 . LEU   B 94  ? 0.2089 0.2475 0.2473 0.0079  -0.0032 -0.0050 100 LEU   C CD1 
1834 C  CD2 . LEU   B 94  ? 0.2119 0.2417 0.2321 0.0063  -0.0048 -0.0049 100 LEU   C CD2 
1835 N  N   . ALA   B 95  ? 0.1368 0.1695 0.1420 -0.0015 -0.0024 -0.0037 101 ALA   C N   
1836 C  CA  . ALA   B 95  ? 0.1336 0.1669 0.1359 -0.0039 -0.0008 -0.0037 101 ALA   C CA  
1837 C  C   . ALA   B 95  ? 0.1376 0.1709 0.1390 -0.0042 0.0035  -0.0058 101 ALA   C C   
1838 O  O   . ALA   B 95  ? 0.1533 0.1843 0.1532 -0.0028 0.0050  -0.0076 101 ALA   C O   
1839 C  CB  . ALA   B 95  ? 0.1423 0.1711 0.1368 -0.0053 -0.0024 -0.0032 101 ALA   C CB  
1840 N  N   . VAL   B 96  ? 0.1351 0.1705 0.1364 -0.0065 0.0057  -0.0058 102 VAL   C N   
1841 C  CA  . VAL   B 96  ? 0.1437 0.1783 0.1417 -0.0079 0.0103  -0.0077 102 VAL   C CA  
1842 C  C   . VAL   B 96  ? 0.1674 0.1955 0.1539 -0.0098 0.0094  -0.0071 102 VAL   C C   
1843 O  O   . VAL   B 96  ? 0.1746 0.2010 0.1576 -0.0117 0.0075  -0.0052 102 VAL   C O   
1844 C  CB  . VAL   B 96  ? 0.1613 0.2009 0.1643 -0.0102 0.0132  -0.0076 102 VAL   C CB  
1845 C  CG1 . VAL   B 96  ? 0.1702 0.2088 0.1683 -0.0125 0.0188  -0.0097 102 VAL   C CG1 
1846 C  CG2 . VAL   B 96  ? 0.1717 0.2181 0.1880 -0.0081 0.0130  -0.0078 102 VAL   C CG2 
1847 N  N   . GLY   B 97  ? 0.1727 0.1970 0.1538 -0.0092 0.0104  -0.0088 103 GLY   C N   
1848 C  CA  . GLY   B 97  ? 0.1938 0.2117 0.1644 -0.0110 0.0085  -0.0078 103 GLY   C CA  
1849 C  C   . GLY   B 97  ? 0.2110 0.2250 0.1761 -0.0106 0.0094  -0.0100 103 GLY   C C   
1850 O  O   . GLY   B 97  ? 0.2122 0.2281 0.1822 -0.0084 0.0112  -0.0123 103 GLY   C O   
1851 N  N   . HIS   B 98  ? 0.1973 0.2055 0.1524 -0.0130 0.0077  -0.0091 104 HIS   C N   
1852 C  CA  . HIS   B 98  ? 0.2017 0.2055 0.1497 -0.0135 0.0079  -0.0110 104 HIS   C CA  
1853 C  C   . HIS   B 98  ? 0.2058 0.2072 0.1553 -0.0109 0.0034  -0.0107 104 HIS   C C   
1854 O  O   . HIS   B 98  ? 0.1991 0.1996 0.1505 -0.0102 -0.0008 -0.0082 104 HIS   C O   
1855 C  CB  . HIS   B 98  ? 0.2076 0.2055 0.1429 -0.0179 0.0071  -0.0094 104 HIS   C CB  
1856 C  CG  . HIS   B 98  ? 0.2390 0.2315 0.1651 -0.0193 0.0065  -0.0112 104 HIS   C CG  
1857 N  ND1 . HIS   B 98  ? 0.2527 0.2457 0.1763 -0.0200 0.0120  -0.0154 104 HIS   C ND1 
1858 C  CD2 . HIS   B 98  ? 0.2669 0.2538 0.1870 -0.0199 0.0010  -0.0096 104 HIS   C CD2 
1859 C  CE1 . HIS   B 98  ? 0.2810 0.2681 0.1954 -0.0216 0.0097  -0.0163 104 HIS   C CE1 
1860 N  NE2 . HIS   B 98  ? 0.2958 0.2792 0.2081 -0.0215 0.0027  -0.0126 104 HIS   C NE2 
1861 N  N   . SER   B 99  ? 0.1953 0.1950 0.1435 -0.0101 0.0045  -0.0134 105 SER   C N   
1862 C  CA  . SER   B 99  ? 0.1998 0.1964 0.1480 -0.0085 0.0005  -0.0134 105 SER   C CA  
1863 C  C   . SER   B 99  ? 0.2180 0.2110 0.1605 -0.0092 0.0023  -0.0168 105 SER   C C   
1864 O  O   . SER   B 99  ? 0.2229 0.2171 0.1647 -0.0099 0.0075  -0.0199 105 SER   C O   
1865 C  CB  . SER   B 99  ? 0.2106 0.2111 0.1694 -0.0049 -0.0008 -0.0130 105 SER   C CB  
1866 O  OG  . SER   B 99  ? 0.2346 0.2381 0.1996 -0.0030 0.0027  -0.0154 105 SER   C OG  
1867 N  N   . GLU   B 100 ? 0.2214 0.2101 0.1603 -0.0094 -0.0020 -0.0164 106 GLU   C N   
1868 C  CA  . GLU   B 100 ? 0.2361 0.2207 0.1700 -0.0101 -0.0018 -0.0195 106 GLU   C CA  
1869 C  C   . GLU   B 100 ? 0.2314 0.2158 0.1721 -0.0074 -0.0057 -0.0190 106 GLU   C C   
1870 O  O   . GLU   B 100 ? 0.2155 0.2022 0.1623 -0.0058 -0.0087 -0.0161 106 GLU   C O   
1871 C  CB  . GLU   B 100 ? 0.2612 0.2396 0.1814 -0.0145 -0.0040 -0.0190 106 GLU   C CB  
1872 C  CG  . GLU   B 100 ? 0.3580 0.3364 0.2707 -0.0177 0.0009  -0.0200 106 GLU   C CG  
1873 C  CD  . GLU   B 100 ? 0.4212 0.3933 0.3193 -0.0229 -0.0018 -0.0181 106 GLU   C CD  
1874 O  OE1 . GLU   B 100 ? 0.4688 0.4359 0.3612 -0.0241 -0.0070 -0.0175 106 GLU   C OE1 
1875 O  OE2 . GLU   B 100 ? 0.4044 0.3766 0.2969 -0.0259 0.0007  -0.0169 106 GLU   C OE2 
1876 N  N   . PRO   B 101 ? 0.2426 0.2243 0.1828 -0.0069 -0.0053 -0.0221 107 PRO   C N   
1877 C  CA  . PRO   B 101 ? 0.2441 0.2258 0.1913 -0.0046 -0.0088 -0.0214 107 PRO   C CA  
1878 C  C   . PRO   B 101 ? 0.2348 0.2156 0.1824 -0.0051 -0.0146 -0.0180 107 PRO   C C   
1879 O  O   . PRO   B 101 ? 0.2245 0.2081 0.1804 -0.0031 -0.0161 -0.0162 107 PRO   C O   
1880 C  CB  . PRO   B 101 ? 0.2671 0.2443 0.2106 -0.0053 -0.0080 -0.0254 107 PRO   C CB  
1881 C  CG  . PRO   B 101 ? 0.2727 0.2502 0.2127 -0.0061 -0.0017 -0.0291 107 PRO   C CG  
1882 C  CD  . PRO   B 101 ? 0.2509 0.2297 0.1849 -0.0084 -0.0011 -0.0267 107 PRO   C CD  
1883 N  N   . GLY   B 102 ? 0.2370 0.2136 0.1757 -0.0081 -0.0177 -0.0171 108 GLY   C N   
1884 C  CA  . GLY   B 102 ? 0.2325 0.2079 0.1728 -0.0086 -0.0236 -0.0140 108 GLY   C CA  
1885 C  C   . GLY   B 102 ? 0.2200 0.1994 0.1665 -0.0073 -0.0239 -0.0110 108 GLY   C C   
1886 O  O   . GLY   B 102 ? 0.2153 0.1946 0.1662 -0.0071 -0.0281 -0.0089 108 GLY   C O   
1887 N  N   . ASP   B 103 ? 0.1886 0.1714 0.1362 -0.0067 -0.0195 -0.0112 109 ASP   C N   
1888 C  CA  . ASP   B 103 ? 0.1834 0.1697 0.1366 -0.0057 -0.0194 -0.0089 109 ASP   C CA  
1889 C  C   . ASP   B 103 ? 0.1748 0.1651 0.1377 -0.0031 -0.0191 -0.0088 109 ASP   C C   
1890 O  O   . ASP   B 103 ? 0.1739 0.1667 0.1414 -0.0026 -0.0194 -0.0073 109 ASP   C O   
1891 C  CB  . ASP   B 103 ? 0.1937 0.1823 0.1447 -0.0064 -0.0153 -0.0090 109 ASP   C CB  
1892 C  CG  . ASP   B 103 ? 0.2299 0.2146 0.1710 -0.0097 -0.0159 -0.0080 109 ASP   C CG  
1893 O  OD1 . ASP   B 103 ? 0.2316 0.2125 0.1698 -0.0111 -0.0207 -0.0058 109 ASP   C OD1 
1894 O  OD2 . ASP   B 103 ? 0.2335 0.2188 0.1701 -0.0112 -0.0117 -0.0093 109 ASP   C OD2 
1895 N  N   . CYS   B 104 ? 0.1729 0.1637 0.1389 -0.0018 -0.0182 -0.0104 110 CYS   C N   
1896 C  CA  . CYS   B 104 ? 0.1741 0.1681 0.1480 -0.0001 -0.0179 -0.0099 110 CYS   C CA  
1897 C  C   . CYS   B 104 ? 0.1770 0.1712 0.1549 -0.0003 -0.0209 -0.0086 110 CYS   C C   
1898 O  O   . CYS   B 104 ? 0.1801 0.1713 0.1566 -0.0012 -0.0242 -0.0085 110 CYS   C O   
1899 C  CB  . CYS   B 104 ? 0.1894 0.1826 0.1655 0.0009  -0.0173 -0.0114 110 CYS   C CB  
1900 S  SG  . CYS   B 104 ? 0.2186 0.2128 0.1946 0.0020  -0.0132 -0.0133 110 CYS   C SG  
1901 N  N   . GLY   B 105 ? 0.1526 0.1502 0.1355 0.0002  -0.0197 -0.0078 111 GLY   C N   
1902 C  CA  . GLY   B 105 ? 0.1709 0.1693 0.1589 0.0001  -0.0213 -0.0073 111 GLY   C CA  
1903 C  C   . GLY   B 105 ? 0.1819 0.1807 0.1702 -0.0004 -0.0215 -0.0066 111 GLY   C C   
1904 O  O   . GLY   B 105 ? 0.1832 0.1832 0.1770 -0.0003 -0.0218 -0.0068 111 GLY   C O   
1905 N  N   . GLY   B 106 ? 0.1620 0.1595 0.1445 -0.0010 -0.0211 -0.0060 112 GLY   C N   
1906 C  CA  . GLY   B 106 ? 0.1615 0.1589 0.1439 -0.0017 -0.0213 -0.0050 112 GLY   C CA  
1907 C  C   . GLY   B 106 ? 0.1584 0.1596 0.1446 -0.0014 -0.0186 -0.0055 112 GLY   C C   
1908 O  O   . GLY   B 106 ? 0.1599 0.1636 0.1456 -0.0011 -0.0163 -0.0058 112 GLY   C O   
1909 N  N   . ILE   B 107 ? 0.1570 0.1583 0.1474 -0.0016 -0.0190 -0.0057 113 ILE   C N   
1910 C  CA  . ILE   B 107 ? 0.1613 0.1657 0.1544 -0.0020 -0.0163 -0.0067 113 ILE   C CA  
1911 C  C   . ILE   B 107 ? 0.1527 0.1579 0.1423 -0.0029 -0.0150 -0.0060 113 ILE   C C   
1912 O  O   . ILE   B 107 ? 0.1677 0.1707 0.1550 -0.0035 -0.0161 -0.0050 113 ILE   C O   
1913 C  CB  . ILE   B 107 ? 0.1781 0.1821 0.1779 -0.0019 -0.0166 -0.0081 113 ILE   C CB  
1914 C  CG1 . ILE   B 107 ? 0.2037 0.2088 0.2084 -0.0013 -0.0166 -0.0092 113 ILE   C CG1 
1915 C  CG2 . ILE   B 107 ? 0.2014 0.2071 0.2026 -0.0029 -0.0140 -0.0095 113 ILE   C CG2 
1916 C  CD1 . ILE   B 107 ? 0.2224 0.2277 0.2362 -0.0011 -0.0164 -0.0111 113 ILE   C CD1 
1917 N  N   . LEU   B 108 ? 0.1453 0.1537 0.1347 -0.0034 -0.0128 -0.0064 114 LEU   C N   
1918 C  CA  . LEU   B 108 ? 0.1504 0.1604 0.1380 -0.0047 -0.0117 -0.0060 114 LEU   C CA  
1919 C  C   . LEU   B 108 ? 0.1572 0.1677 0.1472 -0.0058 -0.0106 -0.0077 114 LEU   C C   
1920 O  O   . LEU   B 108 ? 0.1568 0.1685 0.1480 -0.0062 -0.0095 -0.0087 114 LEU   C O   
1921 C  CB  . LEU   B 108 ? 0.1407 0.1538 0.1270 -0.0047 -0.0108 -0.0051 114 LEU   C CB  
1922 C  CG  . LEU   B 108 ? 0.1420 0.1575 0.1277 -0.0063 -0.0101 -0.0047 114 LEU   C CG  
1923 C  CD1 . LEU   B 108 ? 0.1550 0.1698 0.1395 -0.0069 -0.0100 -0.0041 114 LEU   C CD1 
1924 C  CD2 . LEU   B 108 ? 0.1575 0.1763 0.1440 -0.0061 -0.0101 -0.0035 114 LEU   C CD2 
1925 N  N   . ARG   B 109 ? 0.1571 0.1662 0.1475 -0.0068 -0.0106 -0.0082 115 ARG   C N   
1926 C  CA  . ARG   B 109 ? 0.1651 0.1742 0.1577 -0.0081 -0.0091 -0.0106 115 ARG   C CA  
1927 C  C   . ARG   B 109 ? 0.1725 0.1823 0.1626 -0.0101 -0.0086 -0.0105 115 ARG   C C   
1928 O  O   . ARG   B 109 ? 0.1796 0.1888 0.1684 -0.0102 -0.0096 -0.0089 115 ARG   C O   
1929 C  CB  . ARG   B 109 ? 0.2009 0.2066 0.1988 -0.0073 -0.0101 -0.0118 115 ARG   C CB  
1930 C  CG  . ARG   B 109 ? 0.2941 0.2986 0.2962 -0.0054 -0.0116 -0.0117 115 ARG   C CG  
1931 C  CD  . ARG   B 109 ? 0.3499 0.3509 0.3585 -0.0046 -0.0134 -0.0125 115 ARG   C CD  
1932 N  NE  . ARG   B 109 ? 0.4031 0.4049 0.4168 -0.0053 -0.0103 -0.0163 115 ARG   C NE  
1933 C  CZ  . ARG   B 109 ? 0.4327 0.4359 0.4524 -0.0048 -0.0083 -0.0190 115 ARG   C CZ  
1934 N  NH1 . ARG   B 109 ? 0.4507 0.4545 0.4735 -0.0034 -0.0100 -0.0180 115 ARG   C NH1 
1935 N  NH2 . ARG   B 109 ? 0.4358 0.4399 0.4587 -0.0061 -0.0045 -0.0229 115 ARG   C NH2 
1936 N  N   . CYS   B 110 ? 0.1564 0.1674 0.1457 -0.0120 -0.0069 -0.0126 116 CYS   C N   
1937 C  CA  . CYS   B 110 ? 0.1786 0.1898 0.1658 -0.0144 -0.0066 -0.0131 116 CYS   C CA  
1938 C  C   . CYS   B 110 ? 0.1965 0.2049 0.1865 -0.0154 -0.0050 -0.0168 116 CYS   C C   
1939 O  O   . CYS   B 110 ? 0.1910 0.1978 0.1856 -0.0139 -0.0042 -0.0186 116 CYS   C O   
1940 C  CB  . CYS   B 110 ? 0.1783 0.1928 0.1613 -0.0165 -0.0065 -0.0125 116 CYS   C CB  
1941 S  SG  . CYS   B 110 ? 0.1674 0.1822 0.1482 -0.0184 -0.0041 -0.0151 116 CYS   C SG  
1942 N  N   . GLN   B 111 ? 0.2148 0.2229 0.2027 -0.0181 -0.0044 -0.0182 117 GLN   C N   
1943 C  CA  . GLN   B 111 ? 0.2278 0.2328 0.2186 -0.0191 -0.0024 -0.0224 117 GLN   C CA  
1944 C  C   . GLN   B 111 ? 0.2327 0.2383 0.2239 -0.0199 0.0010  -0.0263 117 GLN   C C   
1945 O  O   . GLN   B 111 ? 0.2660 0.2693 0.2619 -0.0201 0.0035  -0.0304 117 GLN   C O   
1946 C  CB  . GLN   B 111 ? 0.2644 0.2687 0.2519 -0.0223 -0.0025 -0.0235 117 GLN   C CB  
1947 C  CG  . GLN   B 111 ? 0.3013 0.3086 0.2818 -0.0257 -0.0020 -0.0239 117 GLN   C CG  
1948 C  CD  . GLN   B 111 ? 0.4150 0.4215 0.3923 -0.0292 -0.0026 -0.0251 117 GLN   C CD  
1949 O  OE1 . GLN   B 111 ? 0.4415 0.4506 0.4162 -0.0305 -0.0051 -0.0220 117 GLN   C OE1 
1950 N  NE2 . GLN   B 111 ? 0.4377 0.4406 0.4157 -0.0310 -0.0003 -0.0298 117 GLN   C NE2 
1951 N  N   . HIS   B 112 ? 0.2040 0.2127 0.1909 -0.0206 0.0014  -0.0249 118 HIS   C N   
1952 C  CA  . HIS   B 112 ? 0.2059 0.2153 0.1918 -0.0223 0.0050  -0.0281 118 HIS   C CA  
1953 C  C   . HIS   B 112 ? 0.2091 0.2191 0.2008 -0.0194 0.0056  -0.0278 118 HIS   C C   
1954 O  O   . HIS   B 112 ? 0.2318 0.2424 0.2247 -0.0207 0.0092  -0.0309 118 HIS   C O   
1955 C  CB  . HIS   B 112 ? 0.2095 0.2212 0.1862 -0.0257 0.0048  -0.0264 118 HIS   C CB  
1956 C  CG  . HIS   B 112 ? 0.2093 0.2208 0.1802 -0.0290 0.0035  -0.0264 118 HIS   C CG  
1957 N  ND1 . HIS   B 112 ? 0.2007 0.2140 0.1690 -0.0289 -0.0005 -0.0221 118 HIS   C ND1 
1958 C  CD2 . HIS   B 112 ? 0.2366 0.2461 0.2044 -0.0325 0.0057  -0.0306 118 HIS   C CD2 
1959 C  CE1 . HIS   B 112 ? 0.2290 0.2418 0.1931 -0.0324 -0.0011 -0.0232 118 HIS   C CE1 
1960 N  NE2 . HIS   B 112 ? 0.2513 0.2615 0.2141 -0.0348 0.0025  -0.0284 118 HIS   C NE2 
1961 N  N   . GLY   B 113 ? 0.1858 0.1957 0.1808 -0.0161 0.0023  -0.0244 119 GLY   C N   
1962 C  CA  . GLY   B 113 ? 0.1704 0.1808 0.1707 -0.0137 0.0021  -0.0238 119 GLY   C CA  
1963 C  C   . GLY   B 113 ? 0.1585 0.1700 0.1562 -0.0120 -0.0010 -0.0194 119 GLY   C C   
1964 O  O   . GLY   B 113 ? 0.1684 0.1800 0.1624 -0.0118 -0.0033 -0.0167 119 GLY   C O   
1965 N  N   . VAL   B 114 ? 0.1505 0.1629 0.1509 -0.0109 -0.0009 -0.0191 120 VAL   C N   
1966 C  CA  . VAL   B 114 ? 0.1509 0.1637 0.1493 -0.0093 -0.0034 -0.0157 120 VAL   C CA  
1967 C  C   . VAL   B 114 ? 0.1444 0.1591 0.1362 -0.0110 -0.0035 -0.0137 120 VAL   C C   
1968 O  O   . VAL   B 114 ? 0.1518 0.1676 0.1411 -0.0134 -0.0014 -0.0145 120 VAL   C O   
1969 C  CB  . VAL   B 114 ? 0.1650 0.1780 0.1685 -0.0080 -0.0034 -0.0161 120 VAL   C CB  
1970 C  CG1 . VAL   B 114 ? 0.1756 0.1887 0.1766 -0.0067 -0.0059 -0.0131 120 VAL   C CG1 
1971 C  CG2 . VAL   B 114 ? 0.1663 0.1774 0.1777 -0.0061 -0.0047 -0.0175 120 VAL   C CG2 
1972 N  N   . VAL   B 115 ? 0.1397 0.1548 0.1293 -0.0099 -0.0058 -0.0109 121 VAL   C N   
1973 C  CA  . VAL   B 115 ? 0.1375 0.1543 0.1231 -0.0108 -0.0067 -0.0086 121 VAL   C CA  
1974 C  C   . VAL   B 115 ? 0.1455 0.1624 0.1320 -0.0092 -0.0079 -0.0067 121 VAL   C C   
1975 O  O   . VAL   B 115 ? 0.1491 0.1668 0.1336 -0.0104 -0.0084 -0.0051 121 VAL   C O   
1976 C  CB  . VAL   B 115 ? 0.1581 0.1757 0.1426 -0.0106 -0.0081 -0.0072 121 VAL   C CB  
1977 C  CG1 . VAL   B 115 ? 0.1651 0.1849 0.1482 -0.0109 -0.0097 -0.0046 121 VAL   C CG1 
1978 C  CG2 . VAL   B 115 ? 0.1638 0.1812 0.1471 -0.0127 -0.0073 -0.0089 121 VAL   C CG2 
1979 N  N   . GLY   B 116 ? 0.1414 0.1569 0.1304 -0.0068 -0.0088 -0.0067 122 GLY   C N   
1980 C  CA  . GLY   B 116 ? 0.1592 0.1742 0.1490 -0.0053 -0.0099 -0.0055 122 GLY   C CA  
1981 C  C   . GLY   B 116 ? 0.1542 0.1670 0.1452 -0.0033 -0.0110 -0.0059 122 GLY   C C   
1982 O  O   . GLY   B 116 ? 0.1585 0.1700 0.1504 -0.0032 -0.0113 -0.0068 122 GLY   C O   
1983 N  N   . ILE   B 117 ? 0.1404 0.1523 0.1314 -0.0021 -0.0119 -0.0053 123 ILE   C N   
1984 C  CA  . ILE   B 117 ? 0.1429 0.1522 0.1334 -0.0009 -0.0132 -0.0058 123 ILE   C CA  
1985 C  C   . ILE   B 117 ? 0.1400 0.1489 0.1284 0.0001  -0.0130 -0.0055 123 ILE   C C   
1986 O  O   . ILE   B 117 ? 0.1343 0.1446 0.1238 0.0005  -0.0125 -0.0048 123 ILE   C O   
1987 C  CB  . ILE   B 117 ? 0.1504 0.1581 0.1435 -0.0006 -0.0143 -0.0064 123 ILE   C CB  
1988 C  CG1 . ILE   B 117 ? 0.1643 0.1727 0.1585 -0.0007 -0.0138 -0.0058 123 ILE   C CG1 
1989 C  CG2 . ILE   B 117 ? 0.1660 0.1740 0.1630 -0.0012 -0.0143 -0.0074 123 ILE   C CG2 
1990 C  CD1 . ILE   B 117 ? 0.1804 0.1870 0.1775 -0.0006 -0.0150 -0.0064 123 ILE   C CD1 
1991 N  N   . VAL   B 118 ? 0.1390 0.1458 0.1243 0.0002  -0.0134 -0.0060 124 VAL   C N   
1992 C  CA  . VAL   B 118 ? 0.1441 0.1504 0.1273 0.0008  -0.0123 -0.0066 124 VAL   C CA  
1993 C  C   . VAL   B 118 ? 0.1450 0.1501 0.1300 0.0019  -0.0126 -0.0073 124 VAL   C C   
1994 O  O   . VAL   B 118 ? 0.1491 0.1521 0.1345 0.0018  -0.0143 -0.0076 124 VAL   C O   
1995 C  CB  . VAL   B 118 ? 0.1557 0.1588 0.1333 -0.0001 -0.0127 -0.0072 124 VAL   C CB  
1996 C  CG1 . VAL   B 118 ? 0.1584 0.1608 0.1334 0.0001  -0.0106 -0.0087 124 VAL   C CG1 
1997 C  CG2 . VAL   B 118 ? 0.1589 0.1625 0.1347 -0.0015 -0.0125 -0.0061 124 VAL   C CG2 
1998 N  N   . SER   B 119 ? 0.1440 0.1505 0.1312 0.0029  -0.0112 -0.0075 125 SER   C N   
1999 C  CA  . SER   B 119 ? 0.1525 0.1575 0.1425 0.0040  -0.0115 -0.0081 125 SER   C CA  
2000 C  C   . SER   B 119 ? 0.1665 0.1707 0.1570 0.0051  -0.0095 -0.0101 125 SER   C C   
2001 O  O   . SER   B 119 ? 0.1732 0.1744 0.1641 0.0058  -0.0097 -0.0118 125 SER   C O   
2002 C  CB  . SER   B 119 ? 0.1660 0.1731 0.1604 0.0041  -0.0124 -0.0059 125 SER   C CB  
2003 O  OG  . SER   B 119 ? 0.1797 0.1849 0.1773 0.0051  -0.0132 -0.0058 125 SER   C OG  
2004 N  N   . THR   B 120 ? 0.1696 0.1765 0.1608 0.0052  -0.0073 -0.0105 126 THR   C N   
2005 C  CA  . THR   B 120 ? 0.1742 0.1811 0.1674 0.0063  -0.0043 -0.0131 126 THR   C CA  
2006 C  C   . THR   B 120 ? 0.1807 0.1890 0.1700 0.0049  -0.0014 -0.0142 126 THR   C C   
2007 O  O   . THR   B 120 ? 0.1797 0.1895 0.1664 0.0035  -0.0021 -0.0124 126 THR   C O   
2008 C  CB  . THR   B 120 ? 0.1880 0.1981 0.1907 0.0082  -0.0042 -0.0121 126 THR   C CB  
2009 O  OG1 . THR   B 120 ? 0.1969 0.2117 0.2020 0.0076  -0.0041 -0.0101 126 THR   C OG1 
2010 C  CG2 . THR   B 120 ? 0.1892 0.1980 0.1955 0.0090  -0.0074 -0.0099 126 THR   C CG2 
2011 N  N   . GLY   B 121 ? 0.1844 0.1923 0.1739 0.0051  0.0023  -0.0174 127 GLY   C N   
2012 C  CA  . GLY   B 121 ? 0.2056 0.2154 0.1921 0.0034  0.0059  -0.0186 127 GLY   C CA  
2013 C  C   . GLY   B 121 ? 0.2153 0.2253 0.2043 0.0039  0.0110  -0.0228 127 GLY   C C   
2014 O  O   . GLY   B 121 ? 0.2080 0.2157 0.1998 0.0054  0.0114  -0.0253 127 GLY   C O   
2015 N  N   . GLY   B 122 ? 0.2271 0.2398 0.2153 0.0022  0.0150  -0.0240 128 GLY   C N   
2016 C  CA  . GLY   B 122 ? 0.2357 0.2494 0.2268 0.0023  0.0212  -0.0288 128 GLY   C CA  
2017 C  C   . GLY   B 122 ? 0.2256 0.2457 0.2237 0.0018  0.0247  -0.0286 128 GLY   C C   
2018 O  O   . GLY   B 122 ? 0.2192 0.2433 0.2238 0.0028  0.0217  -0.0250 128 GLY   C O   
2019 N  N   . ASN   B 123 ? 0.2417 0.2625 0.2376 -0.0002 0.0313  -0.0326 129 ASN   C N   
2020 C  CA  . ASN   B 123 ? 0.2446 0.2718 0.2477 -0.0012 0.0357  -0.0332 129 ASN   C CA  
2021 C  C   . ASN   B 123 ? 0.2330 0.2622 0.2324 -0.0034 0.0326  -0.0283 129 ASN   C C   
2022 O  O   . ASN   B 123 ? 0.2397 0.2750 0.2489 -0.0030 0.0334  -0.0271 129 ASN   C O   
2023 C  CB  . ASN   B 123 ? 0.2715 0.3046 0.2931 0.0029  0.0360  -0.0338 129 ASN   C CB  
2024 C  CG  . ASN   B 123 ? 0.3477 0.3794 0.3754 0.0052  0.0400  -0.0392 129 ASN   C CG  
2025 O  OD1 . ASN   B 123 ? 0.3714 0.4004 0.3919 0.0029  0.0460  -0.0441 129 ASN   C OD1 
2026 N  ND2 . ASN   B 123 ? 0.3733 0.4064 0.4142 0.0093  0.0367  -0.0383 129 ASN   C ND2 
2027 N  N   . GLY   B 124 ? 0.2140 0.2379 0.2003 -0.0058 0.0291  -0.0257 130 GLY   C N   
2028 C  CA  . GLY   B 124 ? 0.2104 0.2351 0.1934 -0.0078 0.0262  -0.0215 130 GLY   C CA  
2029 C  C   . GLY   B 124 ? 0.1894 0.2171 0.1806 -0.0053 0.0208  -0.0179 130 GLY   C C   
2030 O  O   . GLY   B 124 ? 0.1982 0.2280 0.1899 -0.0068 0.0194  -0.0153 130 GLY   C O   
2031 N  N   . LEU   B 125 ? 0.1632 0.1907 0.1602 -0.0019 0.0180  -0.0180 131 LEU   C N   
2032 C  CA  . LEU   B 125 ? 0.1708 0.2000 0.1734 -0.0001 0.0128  -0.0147 131 LEU   C CA  
2033 C  C   . LEU   B 125 ? 0.2012 0.2251 0.1976 0.0006  0.0089  -0.0137 131 LEU   C C   
2034 O  O   . LEU   B 125 ? 0.2371 0.2584 0.2335 0.0021  0.0094  -0.0158 131 LEU   C O   
2035 C  CB  . LEU   B 125 ? 0.1767 0.2105 0.1927 0.0028  0.0128  -0.0151 131 LEU   C CB  
2036 C  CG  . LEU   B 125 ? 0.1952 0.2355 0.2205 0.0023  0.0159  -0.0157 131 LEU   C CG  
2037 C  CD1 . LEU   B 125 ? 0.2059 0.2499 0.2456 0.0056  0.0169  -0.0173 131 LEU   C CD1 
2038 C  CD2 . LEU   B 125 ? 0.2001 0.2435 0.2270 0.0010  0.0124  -0.0120 131 LEU   C CD2 
2039 N  N   . VAL   B 126 ? 0.1617 0.1842 0.1538 -0.0004 0.0052  -0.0110 132 VAL   C N   
2040 C  CA  . VAL   B 126 ? 0.1584 0.1766 0.1462 0.0001  0.0018  -0.0102 132 VAL   C CA  
2041 C  C   . VAL   B 126 ? 0.1542 0.1746 0.1480 0.0015  -0.0013 -0.0081 132 VAL   C C   
2042 O  O   . VAL   B 126 ? 0.1564 0.1804 0.1538 0.0010  -0.0020 -0.0065 132 VAL   C O   
2043 C  CB  . VAL   B 126 ? 0.1719 0.1868 0.1518 -0.0021 0.0001  -0.0089 132 VAL   C CB  
2044 C  CG1 . VAL   B 126 ? 0.1821 0.1998 0.1635 -0.0035 -0.0003 -0.0070 132 VAL   C CG1 
2045 C  CG2 . VAL   B 126 ? 0.1728 0.1841 0.1505 -0.0015 -0.0035 -0.0082 132 VAL   C CG2 
2046 N  N   . GLY   B 127 ? 0.1418 0.1598 0.1361 0.0029  -0.0031 -0.0082 133 GLY   C N   
2047 C  CA  . GLY   B 127 ? 0.1412 0.1606 0.1398 0.0035  -0.0059 -0.0060 133 GLY   C CA  
2048 C  C   . GLY   B 127 ? 0.1525 0.1692 0.1468 0.0027  -0.0080 -0.0052 133 GLY   C C   
2049 O  O   . GLY   B 127 ? 0.1480 0.1613 0.1387 0.0027  -0.0082 -0.0063 133 GLY   C O   
2050 N  N   . PHE   B 128 ? 0.1429 0.1612 0.1379 0.0017  -0.0097 -0.0033 134 PHE   C N   
2051 C  CA  . PHE   B 128 ? 0.1508 0.1674 0.1430 0.0006  -0.0108 -0.0030 134 PHE   C CA  
2052 C  C   . PHE   B 128 ? 0.1566 0.1736 0.1507 0.0002  -0.0123 -0.0014 134 PHE   C C   
2053 O  O   . PHE   B 128 ? 0.1557 0.1750 0.1519 -0.0003 -0.0133 0.0004  134 PHE   C O   
2054 C  CB  . PHE   B 128 ? 0.1571 0.1749 0.1474 -0.0012 -0.0107 -0.0027 134 PHE   C CB  
2055 C  CG  . PHE   B 128 ? 0.1589 0.1763 0.1472 -0.0015 -0.0096 -0.0035 134 PHE   C CG  
2056 C  CD1 . PHE   B 128 ? 0.1565 0.1704 0.1416 -0.0017 -0.0099 -0.0043 134 PHE   C CD1 
2057 C  CD2 . PHE   B 128 ? 0.1675 0.1876 0.1570 -0.0021 -0.0085 -0.0031 134 PHE   C CD2 
2058 C  CE1 . PHE   B 128 ? 0.1637 0.1765 0.1459 -0.0025 -0.0092 -0.0044 134 PHE   C CE1 
2059 C  CE2 . PHE   B 128 ? 0.1712 0.1906 0.1583 -0.0030 -0.0072 -0.0036 134 PHE   C CE2 
2060 C  CZ  . PHE   B 128 ? 0.1700 0.1855 0.1528 -0.0033 -0.0076 -0.0041 134 PHE   C CZ  
2061 N  N   . ALA   B 129 ? 0.1420 0.1566 0.1354 0.0002  -0.0127 -0.0017 135 ALA   C N   
2062 C  CA  . ALA   B 129 ? 0.1420 0.1565 0.1361 -0.0010 -0.0138 -0.0001 135 ALA   C CA  
2063 C  C   . ALA   B 129 ? 0.1431 0.1588 0.1344 -0.0035 -0.0132 0.0000  135 ALA   C C   
2064 O  O   . ALA   B 129 ? 0.1448 0.1599 0.1353 -0.0039 -0.0121 -0.0018 135 ALA   C O   
2065 C  CB  . ALA   B 129 ? 0.1414 0.1531 0.1360 -0.0005 -0.0140 -0.0009 135 ALA   C CB  
2066 N  N   . ASP   B 130 ? 0.1394 0.1567 0.1295 -0.0053 -0.0142 0.0020  136 ASP   C N   
2067 C  CA  . ASP   B 130 ? 0.1484 0.1667 0.1347 -0.0083 -0.0133 0.0016  136 ASP   C CA  
2068 C  C   . ASP   B 130 ? 0.1600 0.1768 0.1447 -0.0102 -0.0119 0.0009  136 ASP   C C   
2069 O  O   . ASP   B 130 ? 0.1590 0.1746 0.1445 -0.0102 -0.0128 0.0026  136 ASP   C O   
2070 C  CB  . ASP   B 130 ? 0.1557 0.1755 0.1402 -0.0104 -0.0154 0.0043  136 ASP   C CB  
2071 C  CG  . ASP   B 130 ? 0.2283 0.2487 0.2076 -0.0141 -0.0146 0.0036  136 ASP   C CG  
2072 O  OD1 . ASP   B 130 ? 0.2265 0.2471 0.2054 -0.0141 -0.0126 0.0009  136 ASP   C OD1 
2073 O  OD2 . ASP   B 130 ? 0.2690 0.2892 0.2442 -0.0172 -0.0159 0.0056  136 ASP   C OD2 
2074 N  N   . VAL   B 131 ? 0.1422 0.1593 0.1254 -0.0119 -0.0095 -0.0015 137 VAL   C N   
2075 C  CA  . VAL   B 131 ? 0.1540 0.1705 0.1362 -0.0143 -0.0072 -0.0026 137 VAL   C CA  
2076 C  C   . VAL   B 131 ? 0.1670 0.1842 0.1439 -0.0184 -0.0052 -0.0037 137 VAL   C C   
2077 O  O   . VAL   B 131 ? 0.1742 0.1913 0.1497 -0.0210 -0.0023 -0.0053 137 VAL   C O   
2078 C  CB  . VAL   B 131 ? 0.1685 0.1846 0.1559 -0.0126 -0.0055 -0.0055 137 VAL   C CB  
2079 C  CG1 . VAL   B 131 ? 0.1700 0.1847 0.1610 -0.0094 -0.0077 -0.0047 137 VAL   C CG1 
2080 C  CG2 . VAL   B 131 ? 0.1594 0.1758 0.1483 -0.0120 -0.0043 -0.0082 137 VAL   C CG2 
2081 N  N   . ARG   B 132 ? 0.1597 0.1778 0.1336 -0.0192 -0.0064 -0.0033 138 ARG   C N   
2082 C  CA  . ARG   B 132 ? 0.1424 0.1607 0.1105 -0.0233 -0.0046 -0.0049 138 ARG   C CA  
2083 C  C   . ARG   B 132 ? 0.1681 0.1856 0.1292 -0.0278 -0.0047 -0.0029 138 ARG   C C   
2084 O  O   . ARG   B 132 ? 0.1899 0.2071 0.1454 -0.0320 -0.0018 -0.0052 138 ARG   C O   
2085 C  CB  . ARG   B 132 ? 0.1462 0.1653 0.1128 -0.0235 -0.0066 -0.0045 138 ARG   C CB  
2086 C  CG  . ARG   B 132 ? 0.1445 0.1637 0.1166 -0.0201 -0.0060 -0.0066 138 ARG   C CG  
2087 C  CD  . ARG   B 132 ? 0.1543 0.1747 0.1255 -0.0205 -0.0080 -0.0057 138 ARG   C CD  
2088 N  NE  . ARG   B 132 ? 0.1516 0.1734 0.1247 -0.0187 -0.0114 -0.0020 138 ARG   C NE  
2089 C  CZ  . ARG   B 132 ? 0.1819 0.2055 0.1564 -0.0185 -0.0133 -0.0008 138 ARG   C CZ  
2090 N  NH1 . ARG   B 132 ? 0.1690 0.1927 0.1417 -0.0204 -0.0128 -0.0025 138 ARG   C NH1 
2091 N  NH2 . ARG   B 132 ? 0.1806 0.2060 0.1590 -0.0166 -0.0157 0.0020  138 ARG   C NH2 
2092 N  N   . ASP   B 133 ? 0.1658 0.1828 0.1267 -0.0275 -0.0081 0.0015  139 ASP   C N   
2093 C  CA  . ASP   B 133 ? 0.1729 0.1884 0.1265 -0.0322 -0.0089 0.0043  139 ASP   C CA  
2094 C  C   . ASP   B 133 ? 0.1935 0.2081 0.1467 -0.0341 -0.0052 0.0031  139 ASP   C C   
2095 O  O   . ASP   B 133 ? 0.2093 0.2223 0.1548 -0.0391 -0.0049 0.0051  139 ASP   C O   
2096 C  CB  . ASP   B 133 ? 0.1985 0.2134 0.1531 -0.0313 -0.0146 0.0099  139 ASP   C CB  
2097 C  CG  . ASP   B 133 ? 0.2487 0.2630 0.2113 -0.0267 -0.0155 0.0108  139 ASP   C CG  
2098 O  OD1 . ASP   B 133 ? 0.2421 0.2574 0.2107 -0.0227 -0.0137 0.0078  139 ASP   C OD1 
2099 O  OD2 . ASP   B 133 ? 0.2696 0.2819 0.2320 -0.0274 -0.0183 0.0147  139 ASP   C OD2 
2100 N  N   . LEU   B 134 ? 0.1891 0.2043 0.1499 -0.0306 -0.0026 0.0001  140 LEU   C N   
2101 C  CA  . LEU   B 134 ? 0.1905 0.2053 0.1530 -0.0321 0.0008  -0.0011 140 LEU   C CA  
2102 C  C   . LEU   B 134 ? 0.1932 0.2091 0.1535 -0.0356 0.0067  -0.0059 140 LEU   C C   
2103 O  O   . LEU   B 134 ? 0.1960 0.2134 0.1638 -0.0333 0.0098  -0.0102 140 LEU   C O   
2104 C  CB  . LEU   B 134 ? 0.1959 0.2111 0.1683 -0.0271 0.0003  -0.0021 140 LEU   C CB  
2105 C  CG  . LEU   B 134 ? 0.2110 0.2249 0.1859 -0.0235 -0.0046 0.0016  140 LEU   C CG  
2106 C  CD1 . LEU   B 134 ? 0.2018 0.2156 0.1847 -0.0191 -0.0050 -0.0001 140 LEU   C CD1 
2107 C  CD2 . LEU   B 134 ? 0.2221 0.2339 0.1934 -0.0259 -0.0070 0.0060  140 LEU   C CD2 
2108 N  N   . LEU   B 135 ? 0.1942 0.2092 0.1443 -0.0414 0.0081  -0.0054 141 LEU   C N   
2109 C  CA  . LEU   B 135 ? 0.2068 0.2226 0.1538 -0.0452 0.0143  -0.0108 141 LEU   C CA  
2110 C  C   . LEU   B 135 ? 0.2197 0.2368 0.1725 -0.0461 0.0202  -0.0145 141 LEU   C C   
2111 O  O   . LEU   B 135 ? 0.2422 0.2607 0.1989 -0.0466 0.0256  -0.0203 141 LEU   C O   
2112 C  CB  . LEU   B 135 ? 0.2099 0.2239 0.1427 -0.0522 0.0145  -0.0095 141 LEU   C CB  
2113 C  CG  . LEU   B 135 ? 0.2327 0.2456 0.1601 -0.0520 0.0079  -0.0053 141 LEU   C CG  
2114 C  CD1 . LEU   B 135 ? 0.2503 0.2612 0.1629 -0.0598 0.0081  -0.0045 141 LEU   C CD1 
2115 C  CD2 . LEU   B 135 ? 0.2393 0.2537 0.1733 -0.0472 0.0067  -0.0078 141 LEU   C CD2 
2116 N  N   . TRP   B 136 ? 0.2228 0.2394 0.1773 -0.0464 0.0191  -0.0112 142 TRP   C N   
2117 C  CA  . TRP   B 136 ? 0.2266 0.2448 0.1872 -0.0477 0.0244  -0.0141 142 TRP   C CA  
2118 C  C   . TRP   B 136 ? 0.2404 0.2611 0.2158 -0.0419 0.0253  -0.0179 142 TRP   C C   
2119 O  O   . TRP   B 136 ? 0.2551 0.2779 0.2380 -0.0427 0.0302  -0.0216 142 TRP   C O   
2120 C  CB  . TRP   B 136 ? 0.2339 0.2504 0.1926 -0.0494 0.0221  -0.0090 142 TRP   C CB  
2121 C  CG  . TRP   B 136 ? 0.2325 0.2475 0.1955 -0.0441 0.0150  -0.0044 142 TRP   C CG  
2122 C  CD1 . TRP   B 136 ? 0.2449 0.2574 0.2021 -0.0436 0.0091  0.0007  142 TRP   C CD1 
2123 C  CD2 . TRP   B 136 ? 0.2198 0.2356 0.1944 -0.0387 0.0133  -0.0051 142 TRP   C CD2 
2124 N  NE1 . TRP   B 136 ? 0.2480 0.2598 0.2127 -0.0382 0.0046  0.0028  142 TRP   C NE1 
2125 C  CE2 . TRP   B 136 ? 0.2359 0.2495 0.2102 -0.0355 0.0071  -0.0007 142 TRP   C CE2 
2126 C  CE3 . TRP   B 136 ? 0.2217 0.2399 0.2070 -0.0368 0.0164  -0.0090 142 TRP   C CE3 
2127 C  CZ2 . TRP   B 136 ? 0.2409 0.2542 0.2237 -0.0306 0.0043  -0.0005 142 TRP   C CZ2 
2128 C  CZ3 . TRP   B 136 ? 0.2270 0.2449 0.2207 -0.0321 0.0126  -0.0081 142 TRP   C CZ3 
2129 C  CH2 . TRP   B 136 ? 0.2300 0.2451 0.2214 -0.0293 0.0069  -0.0040 142 TRP   C CH2 
2130 N  N   . LEU   B 137 ? 0.2361 0.2564 0.2159 -0.0364 0.0207  -0.0172 143 LEU   C N   
2131 C  CA  . LEU   B 137 ? 0.2431 0.2650 0.2359 -0.0314 0.0207  -0.0203 143 LEU   C CA  
2132 C  C   . LEU   B 137 ? 0.2838 0.3078 0.2824 -0.0326 0.0267  -0.0266 143 LEU   C C   
2133 O  O   . LEU   B 137 ? 0.2783 0.3040 0.2892 -0.0299 0.0278  -0.0293 143 LEU   C O   
2134 C  CB  . LEU   B 137 ? 0.2319 0.2526 0.2260 -0.0265 0.0151  -0.0184 143 LEU   C CB  
2135 C  CG  . LEU   B 137 ? 0.2280 0.2472 0.2212 -0.0240 0.0097  -0.0137 143 LEU   C CG  
2136 C  CD1 . LEU   B 137 ? 0.2174 0.2356 0.2103 -0.0202 0.0056  -0.0124 143 LEU   C CD1 
2137 C  CD2 . LEU   B 137 ? 0.2115 0.2310 0.2132 -0.0221 0.0091  -0.0137 143 LEU   C CD2 
2138 N  N   . ASP   B 138 ? 0.3229 0.3465 0.3132 -0.0366 0.0304  -0.0290 144 ASP   C N   
2139 C  CA  . ASP   B 138 ? 0.3803 0.4052 0.3748 -0.0383 0.0369  -0.0357 144 ASP   C CA  
2140 C  C   . ASP   B 138 ? 0.4375 0.4639 0.4293 -0.0442 0.0444  -0.0391 144 ASP   C C   
2141 O  O   . ASP   B 138 ? 0.4590 0.4863 0.4528 -0.0463 0.0507  -0.0452 144 ASP   C O   
2142 C  CB  . ASP   B 138 ? 0.4231 0.4461 0.4093 -0.0396 0.0366  -0.0370 144 ASP   C CB  
2143 C  CG  . ASP   B 138 ? 0.4793 0.5013 0.4705 -0.0341 0.0309  -0.0353 144 ASP   C CG  
2144 O  OD1 . ASP   B 138 ? 0.4870 0.5098 0.4907 -0.0295 0.0298  -0.0365 144 ASP   C OD1 
2145 O  OD2 . ASP   B 138 ? 0.4958 0.5161 0.4785 -0.0345 0.0273  -0.0326 144 ASP   C OD2 
2146 N  N   . GLU   B 139 ? 0.4610 0.4874 0.4484 -0.0471 0.0444  -0.0355 145 GLU   C N   
2147 C  CA  . GLU   B 139 ? 0.4973 0.5251 0.4814 -0.0535 0.0521  -0.0385 145 GLU   C CA  
2148 C  C   . GLU   B 139 ? 0.5173 0.5476 0.5123 -0.0526 0.0533  -0.0378 145 GLU   C C   
2149 O  O   . GLU   B 139 ? 0.5287 0.5602 0.5212 -0.0581 0.0591  -0.0390 145 GLU   C O   
2150 C  CB  . GLU   B 139 ? 0.5477 0.5724 0.5127 -0.0604 0.0520  -0.0349 145 GLU   C CB  
2151 C  CG  . GLU   B 139 ? 0.6306 0.6528 0.5895 -0.0595 0.0441  -0.0266 145 GLU   C CG  
2152 C  CD  . GLU   B 139 ? 0.7336 0.7523 0.6745 -0.0664 0.0429  -0.0223 145 GLU   C CD  
2153 O  OE1 . GLU   B 139 ? 0.7408 0.7581 0.6779 -0.0692 0.0415  -0.0175 145 GLU   C OE1 
2154 O  OE2 . GLU   B 139 ? 0.7696 0.7868 0.7005 -0.0693 0.0430  -0.0234 145 GLU   C OE2 
2155 N  N1  . A1B5J C .   ? 0.1921 0.2049 0.2276 -0.0007 0.0230  0.0273  201 A1B5J A N1  
2156 C  C4  . A1B5J C .   ? 0.1851 0.1924 0.2149 0.0011  0.0230  0.0324  201 A1B5J A C4  
2157 C  C5  . A1B5J C .   ? 0.2063 0.2204 0.2352 0.0006  0.0241  0.0269  201 A1B5J A C5  
2158 C  C6  . A1B5J C .   ? 0.2233 0.2325 0.2360 0.0042  0.0246  0.0314  201 A1B5J A C6  
2159 C  C7  . A1B5J C .   ? 0.2325 0.2429 0.2391 0.0057  0.0267  0.0305  201 A1B5J A C7  
2160 C  C8  . A1B5J C .   ? 0.2447 0.2529 0.2505 0.0072  0.0344  0.0344  201 A1B5J A C8  
2161 C  C10 . A1B5J C .   ? 0.2358 0.2474 0.2297 0.0094  0.0302  0.0288  201 A1B5J A C10 
2162 CL CL  . A1B5J C .   ? 0.2498 0.2645 0.2510 0.0045  0.0136  0.0220  201 A1B5J A CL  
2163 C  C11 . A1B5J C .   ? 0.2388 0.2518 0.2395 0.0061  0.0216  0.0261  201 A1B5J A C11 
2164 N  N2  . A1B5J C .   ? 0.2359 0.2494 0.2307 0.0078  0.0229  0.0252  201 A1B5J A N2  
2165 C  C9  . A1B5J C .   ? 0.2405 0.2493 0.2396 0.0092  0.0364  0.0336  201 A1B5J A C9  
2166 O  O1  . A1B5J C .   ? 0.1982 0.2170 0.2335 -0.0006 0.0241  0.0227  201 A1B5J A O1  
2167 C  C3  . A1B5J C .   ? 0.1854 0.1936 0.2145 0.0008  0.0165  0.0298  201 A1B5J A C3  
2168 C  C2  . A1B5J C .   ? 0.1847 0.1968 0.2270 -0.0022 0.0154  0.0247  201 A1B5J A C2  
2169 C  C12 . A1B5J C .   ? 0.1905 0.2074 0.2394 -0.0035 0.0211  0.0221  201 A1B5J A C12 
2170 C  C1  . A1B5J C .   ? 0.1853 0.2023 0.2310 -0.0035 0.0153  0.0197  201 A1B5J A C1  
2171 C  C   . A1B5J C .   ? 0.1899 0.2099 0.2462 -0.0054 0.0132  0.0140  201 A1B5J A C   
2172 O  O   . A1B5J C .   ? 0.1843 0.2043 0.2525 -0.0069 0.0156  0.0132  201 A1B5J A O   
2173 N  N   . A1B5J C .   ? 0.1820 0.2042 0.2337 -0.0049 0.0089  0.0098  201 A1B5J A N   
2179 N  N1  . A1B5J F .   ? 0.1946 0.1867 0.1825 0.0072  -0.0030 -0.0229 201 A1B5J C N1  
2180 C  C4  . A1B5J F .   ? 0.2059 0.1926 0.1892 0.0062  -0.0047 -0.0249 201 A1B5J C C4  
2181 C  C5  . A1B5J F .   ? 0.2066 0.2011 0.1906 0.0060  -0.0005 -0.0232 201 A1B5J C C5  
2182 C  C6  . A1B5J F .   ? 0.2195 0.2103 0.1920 0.0031  -0.0001 -0.0249 201 A1B5J C C6  
2183 C  C7  . A1B5J F .   ? 0.2205 0.2138 0.1891 0.0015  0.0031  -0.0250 201 A1B5J C C7  
2184 C  C8  . A1B5J F .   ? 0.2206 0.2133 0.1864 0.0004  0.0083  -0.0291 201 A1B5J C C8  
2185 C  C10 . A1B5J F .   ? 0.2390 0.2359 0.1994 -0.0026 0.0089  -0.0249 201 A1B5J C C10 
2186 CL CL  . A1B5J F .   ? 0.2529 0.2495 0.2233 0.0013  -0.0039 -0.0174 201 A1B5J C CL  
2187 C  C11 . A1B5J F .   ? 0.2343 0.2302 0.2015 0.0005  0.0015  -0.0215 201 A1B5J C C11 
2188 N  N2  . A1B5J F .   ? 0.2347 0.2322 0.1982 -0.0014 0.0040  -0.0213 201 A1B5J C N2  
2189 C  C9  . A1B5J F .   ? 0.2330 0.2277 0.1944 -0.0017 0.0115  -0.0291 201 A1B5J C C9  
2190 O  O1  . A1B5J F .   ? 0.2037 0.2028 0.1929 0.0069  0.0010  -0.0219 201 A1B5J C O1  
2191 C  C3  . A1B5J F .   ? 0.1984 0.1848 0.1828 0.0058  -0.0092 -0.0215 201 A1B5J C C3  
2192 C  C2  . A1B5J F .   ? 0.1839 0.1730 0.1772 0.0076  -0.0102 -0.0186 201 A1B5J C C2  
2193 C  C12 . A1B5J F .   ? 0.1824 0.1771 0.1797 0.0093  -0.0046 -0.0201 201 A1B5J C C12 
2194 C  C1  . A1B5J F .   ? 0.1786 0.1728 0.1751 0.0084  -0.0086 -0.0167 201 A1B5J C C1  
2195 C  C   . A1B5J F .   ? 0.1823 0.1787 0.1864 0.0096  -0.0103 -0.0134 201 A1B5J C C   
2196 O  O   . A1B5J F .   ? 0.1758 0.1710 0.1862 0.0112  -0.0103 -0.0138 201 A1B5J C O   
2197 N  N   . A1B5J F .   ? 0.1839 0.1833 0.1872 0.0085  -0.0117 -0.0102 201 A1B5J C N   
# 
