data_8XR5
# 
_entry.id   8XR5 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8XR5         pdb_00008xr5 10.2210/pdb8xr5/pdb 
WWPDB D_1300043980 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-02-26 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8XR5 
_pdbx_database_status.recvd_initial_deposition_date   2024-01-06 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              yhl@cpu.edu.cn 
_pdbx_contact_author.name_first         Haoliang 
_pdbx_contact_author.name_last          Yuan 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-0248-4347 
# 
_audit_author.name               'Liu, L.' 
_audit_author.pdbx_ordinal       1 
_audit_author.identifier_ORCID   ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            J.Med.Chem. 
_citation.journal_id_ASTM           JMCMAR 
_citation.journal_id_CSD            0151 
_citation.journal_id_ISSN           0022-2623 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            67 
_citation.language                  ? 
_citation.page_first                4977 
_citation.page_last                 4997 
_citation.title                     
'Discovery of Novel PD-L1 Small-Molecular Inhibitors with Potent In Vivo Anti-tumor Immune Activity.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c00102 
_citation.pdbx_database_id_PubMed   38465588 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Liu, L.'   1  ?                   
primary 'Zhang, H.' 2  ?                   
primary 'Hou, J.'   3  ?                   
primary 'Zhang, Y.' 4  ?                   
primary 'Wang, L.'  5  ?                   
primary 'Wang, S.'  6  ?                   
primary 'Yao, Z.'   7  ?                   
primary 'Xie, T.'   8  ?                   
primary 'Wen, X.'   9  0000-0001-7852-1154 
primary 'Xu, Q.'    10 0000-0003-4450-6866 
primary 'Dai, L.'   11 0000-0003-0172-4759 
primary 'Feng, Z.'  12 ?                   
primary 'Zhang, P.' 13 ?                   
primary 'Wu, Y.'    14 ?                   
primary 'Sun, H.'   15 0000-0002-3452-7674 
primary 'Liu, J.'   16 ?                   
primary 'Yuan, H.'  17 0000-0003-0248-4347 
# 
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 'Programmed cell death 1 ligand 1' 14436.488 2   ? ? ? ? 
2 non-polymer syn 
;(2~{R})-2-[[2-(2,1,3-benzoxadiazol-5-ylmethoxy)-5-chloranyl-4-[[2-fluoranyl-3-[3-[3-(4-oxidanylpiperidin-1-yl)propoxy]phenyl]phenyl]methoxy]phenyl]methylamino]-3-oxidanyl-propanoic acid
;
735.198   1   ? ? ? ? 
3 water       nat water 18.015    121 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PD-L1,PDCD1 ligand 1,Programmed death ligand 1,hPD-L1,B7 homolog 1,B7-H1' 
# 
_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       
;FTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAA
LQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYAAHHHHHHAA
;
_entity_poly.pdbx_seq_one_letter_code_can   
;FTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAA
LQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYAAHHHHHHAA
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
;(2~{R})-2-[[2-(2,1,3-benzoxadiazol-5-ylmethoxy)-5-chloranyl-4-[[2-fluoranyl-3-[3-[3-(4-oxidanylpiperidin-1-yl)propoxy]phenyl]phenyl]methoxy]phenyl]methylamino]-3-oxidanyl-propanoic acid
;
A1LV3 
3 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   PHE n 
1 2   THR n 
1 3   VAL n 
1 4   THR n 
1 5   VAL n 
1 6   PRO n 
1 7   LYS n 
1 8   ASP n 
1 9   LEU n 
1 10  TYR n 
1 11  VAL n 
1 12  VAL n 
1 13  GLU n 
1 14  TYR n 
1 15  GLY n 
1 16  SER n 
1 17  ASN n 
1 18  MET n 
1 19  THR n 
1 20  ILE n 
1 21  GLU n 
1 22  CYS n 
1 23  LYS n 
1 24  PHE n 
1 25  PRO n 
1 26  VAL n 
1 27  GLU n 
1 28  LYS n 
1 29  GLN n 
1 30  LEU n 
1 31  ASP n 
1 32  LEU n 
1 33  ALA n 
1 34  ALA n 
1 35  LEU n 
1 36  ILE n 
1 37  VAL n 
1 38  TYR n 
1 39  TRP n 
1 40  GLU n 
1 41  MET n 
1 42  GLU n 
1 43  ASP n 
1 44  LYS n 
1 45  ASN n 
1 46  ILE n 
1 47  ILE n 
1 48  GLN n 
1 49  PHE n 
1 50  VAL n 
1 51  HIS n 
1 52  GLY n 
1 53  GLU n 
1 54  GLU n 
1 55  ASP n 
1 56  LEU n 
1 57  LYS n 
1 58  VAL n 
1 59  GLN n 
1 60  HIS n 
1 61  SER n 
1 62  SER n 
1 63  TYR n 
1 64  ARG n 
1 65  GLN n 
1 66  ARG n 
1 67  ALA n 
1 68  ARG n 
1 69  LEU n 
1 70  LEU n 
1 71  LYS n 
1 72  ASP n 
1 73  GLN n 
1 74  LEU n 
1 75  SER n 
1 76  LEU n 
1 77  GLY n 
1 78  ASN n 
1 79  ALA n 
1 80  ALA n 
1 81  LEU n 
1 82  GLN n 
1 83  ILE n 
1 84  THR n 
1 85  ASP n 
1 86  VAL n 
1 87  LYS n 
1 88  LEU n 
1 89  GLN n 
1 90  ASP n 
1 91  ALA n 
1 92  GLY n 
1 93  VAL n 
1 94  TYR n 
1 95  ARG n 
1 96  CYS n 
1 97  MET n 
1 98  ILE n 
1 99  SER n 
1 100 TYR n 
1 101 GLY n 
1 102 GLY n 
1 103 ALA n 
1 104 ASP n 
1 105 TYR n 
1 106 LYS n 
1 107 ARG n 
1 108 ILE n 
1 109 THR n 
1 110 VAL n 
1 111 LYS n 
1 112 VAL n 
1 113 ASN n 
1 114 ALA n 
1 115 PRO n 
1 116 TYR n 
1 117 ALA n 
1 118 ALA n 
1 119 HIS n 
1 120 HIS n 
1 121 HIS n 
1 122 HIS n 
1 123 HIS n 
1 124 HIS n 
1 125 ALA n 
1 126 ALA 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                   126 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'CD274, B7H1, PDCD1L1, PDCD1LG1, PDL1' 
_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      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
A1LV3 non-polymer         . 
;(2~{R})-2-[[2-(2,1,3-benzoxadiazol-5-ylmethoxy)-5-chloranyl-4-[[2-fluoranyl-3-[3-[3-(4-oxidanylpiperidin-1-yl)propoxy]phenyl]phenyl]methoxy]phenyl]methylamino]-3-oxidanyl-propanoic acid
;
? 'C38 H40 Cl F N4 O8' 735.198 
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 
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 
# 
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   PHE 1   1   1   PHE PHE A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   THR 4   4   4   THR THR A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   PRO 6   6   6   PRO PRO A . n 
A 1 7   LYS 7   7   7   LYS LYS A . n 
A 1 8   ASP 8   8   8   ASP ASP A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  TYR 10  10  10  TYR TYR A . n 
A 1 11  VAL 11  11  11  VAL VAL A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  GLU 13  13  13  GLU GLU A . n 
A 1 14  TYR 14  14  14  TYR TYR A . n 
A 1 15  GLY 15  15  15  GLY GLY A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ASN 17  17  17  ASN ASN A . n 
A 1 18  MET 18  18  18  MET MET A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  ILE 20  20  20  ILE ILE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  CYS 22  22  22  CYS CYS A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  PHE 24  24  24  PHE PHE A . n 
A 1 25  PRO 25  25  25  PRO PRO A . n 
A 1 26  VAL 26  26  26  VAL VAL A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  GLN 29  29  29  GLN GLN A . n 
A 1 30  LEU 30  30  30  LEU LEU A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  ALA 33  33  33  ALA ALA A . n 
A 1 34  ALA 34  34  34  ALA ALA A . n 
A 1 35  LEU 35  35  35  LEU LEU A . n 
A 1 36  ILE 36  36  36  ILE ILE A . n 
A 1 37  VAL 37  37  37  VAL VAL A . n 
A 1 38  TYR 38  38  38  TYR TYR A . n 
A 1 39  TRP 39  39  39  TRP TRP A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  MET 41  41  41  MET MET A . n 
A 1 42  GLU 42  42  42  GLU GLU A . n 
A 1 43  ASP 43  43  43  ASP ASP A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  ASN 45  45  45  ASN ASN A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  ILE 47  47  47  ILE ILE A . n 
A 1 48  GLN 48  48  48  GLN GLN A . n 
A 1 49  PHE 49  49  49  PHE PHE A . n 
A 1 50  VAL 50  50  50  VAL VAL A . n 
A 1 51  HIS 51  51  51  HIS HIS A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  GLU 53  53  53  GLU GLU A . n 
A 1 54  GLU 54  54  54  GLU GLU A . n 
A 1 55  ASP 55  55  55  ASP ASP A . n 
A 1 56  LEU 56  56  56  LEU LEU A . n 
A 1 57  LYS 57  57  57  LYS LYS A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  GLN 59  59  59  GLN GLN A . n 
A 1 60  HIS 60  60  60  HIS HIS A . n 
A 1 61  SER 61  61  61  SER SER A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  TYR 63  63  63  TYR TYR A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  GLN 65  65  65  GLN GLN A . n 
A 1 66  ARG 66  66  66  ARG ARG A . n 
A 1 67  ALA 67  67  67  ALA ALA A . n 
A 1 68  ARG 68  68  68  ARG ARG A . n 
A 1 69  LEU 69  69  69  LEU LEU A . n 
A 1 70  LEU 70  70  70  LEU LEU A . n 
A 1 71  LYS 71  71  71  LYS LYS A . n 
A 1 72  ASP 72  72  72  ASP ASP A . n 
A 1 73  GLN 73  73  73  GLN GLN A . n 
A 1 74  LEU 74  74  74  LEU LEU A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  ASN 78  78  78  ASN ASN A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  ALA 80  80  80  ALA ALA A . n 
A 1 81  LEU 81  81  81  LEU LEU A . n 
A 1 82  GLN 82  82  82  GLN GLN A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  THR 84  84  84  THR THR A . n 
A 1 85  ASP 85  85  85  ASP ASP A . n 
A 1 86  VAL 86  86  86  VAL VAL A . n 
A 1 87  LYS 87  87  87  LYS LYS A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  GLN 89  89  89  GLN GLN A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  ALA 91  91  91  ALA ALA A . n 
A 1 92  GLY 92  92  92  GLY GLY A . n 
A 1 93  VAL 93  93  93  VAL VAL A . n 
A 1 94  TYR 94  94  94  TYR TYR A . n 
A 1 95  ARG 95  95  95  ARG ARG A . n 
A 1 96  CYS 96  96  96  CYS CYS A . n 
A 1 97  MET 97  97  97  MET MET A . n 
A 1 98  ILE 98  98  98  ILE ILE A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 TYR 100 100 100 TYR TYR A . n 
A 1 101 GLY 101 101 101 GLY GLY A . n 
A 1 102 GLY 102 102 102 GLY GLY A . n 
A 1 103 ALA 103 103 103 ALA ALA A . n 
A 1 104 ASP 104 104 104 ASP ASP A . n 
A 1 105 TYR 105 105 105 TYR TYR A . n 
A 1 106 LYS 106 106 106 LYS LYS A . n 
A 1 107 ARG 107 107 107 ARG ARG A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 THR 109 109 109 THR THR A . n 
A 1 110 VAL 110 110 110 VAL VAL A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 VAL 112 112 112 VAL VAL A . n 
A 1 113 ASN 113 113 113 ASN ASN A . n 
A 1 114 ALA 114 114 114 ALA ALA A . n 
A 1 115 PRO 115 115 115 PRO PRO A . n 
A 1 116 TYR 116 116 116 TYR TYR A . n 
A 1 117 ALA 117 117 117 ALA ALA A . n 
A 1 118 ALA 118 118 118 ALA ALA A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 HIS 121 121 121 HIS HIS A . n 
A 1 122 HIS 122 122 122 HIS HIS A . n 
A 1 123 HIS 123 123 123 HIS HIS A . n 
A 1 124 HIS 124 124 124 HIS HIS A . n 
A 1 125 ALA 125 125 125 ALA ALA A . n 
A 1 126 ALA 126 126 126 ALA ALA A . n 
B 1 1   PHE 1   1   1   PHE PHE B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   THR 4   4   4   THR THR B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   PRO 6   6   6   PRO PRO B . n 
B 1 7   LYS 7   7   7   LYS LYS B . n 
B 1 8   ASP 8   8   8   ASP ASP B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  TYR 10  10  10  TYR TYR B . n 
B 1 11  VAL 11  11  11  VAL VAL B . n 
B 1 12  VAL 12  12  12  VAL VAL B . n 
B 1 13  GLU 13  13  13  GLU GLU B . n 
B 1 14  TYR 14  14  14  TYR TYR B . n 
B 1 15  GLY 15  15  15  GLY GLY B . n 
B 1 16  SER 16  16  16  SER SER B . n 
B 1 17  ASN 17  17  17  ASN ASN B . n 
B 1 18  MET 18  18  18  MET MET B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  ILE 20  20  20  ILE ILE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  CYS 22  22  22  CYS CYS B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  PHE 24  24  24  PHE PHE B . n 
B 1 25  PRO 25  25  25  PRO PRO B . n 
B 1 26  VAL 26  26  26  VAL VAL B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  GLN 29  29  29  GLN GLN B . n 
B 1 30  LEU 30  30  30  LEU LEU B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  ALA 33  33  33  ALA ALA B . n 
B 1 34  ALA 34  34  34  ALA ALA B . n 
B 1 35  LEU 35  35  35  LEU LEU B . n 
B 1 36  ILE 36  36  36  ILE ILE B . n 
B 1 37  VAL 37  37  37  VAL VAL B . n 
B 1 38  TYR 38  38  38  TYR TYR B . n 
B 1 39  TRP 39  39  39  TRP TRP B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  MET 41  41  41  MET MET B . n 
B 1 42  GLU 42  42  42  GLU GLU B . n 
B 1 43  ASP 43  43  43  ASP ASP B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  ASN 45  45  45  ASN ASN B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  ILE 47  47  47  ILE ILE B . n 
B 1 48  GLN 48  48  48  GLN GLN B . n 
B 1 49  PHE 49  49  49  PHE PHE B . n 
B 1 50  VAL 50  50  50  VAL VAL B . n 
B 1 51  HIS 51  51  51  HIS HIS B . n 
B 1 52  GLY 52  52  52  GLY GLY B . n 
B 1 53  GLU 53  53  53  GLU GLU B . n 
B 1 54  GLU 54  54  54  GLU GLU B . n 
B 1 55  ASP 55  55  55  ASP ASP B . n 
B 1 56  LEU 56  56  56  LEU LEU B . n 
B 1 57  LYS 57  57  57  LYS LYS B . n 
B 1 58  VAL 58  58  58  VAL VAL B . n 
B 1 59  GLN 59  59  59  GLN GLN B . n 
B 1 60  HIS 60  60  60  HIS HIS B . n 
B 1 61  SER 61  61  61  SER SER B . n 
B 1 62  SER 62  62  62  SER SER B . n 
B 1 63  TYR 63  63  63  TYR TYR B . n 
B 1 64  ARG 64  64  64  ARG ARG B . n 
B 1 65  GLN 65  65  65  GLN GLN B . n 
B 1 66  ARG 66  66  66  ARG ARG B . n 
B 1 67  ALA 67  67  67  ALA ALA B . n 
B 1 68  ARG 68  68  68  ARG ARG B . n 
B 1 69  LEU 69  69  69  LEU LEU B . n 
B 1 70  LEU 70  70  70  LEU LEU B . n 
B 1 71  LYS 71  71  71  LYS LYS B . n 
B 1 72  ASP 72  72  72  ASP ASP B . n 
B 1 73  GLN 73  73  73  GLN GLN B . n 
B 1 74  LEU 74  74  74  LEU LEU B . n 
B 1 75  SER 75  75  75  SER SER B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  ASN 78  78  78  ASN ASN B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  ALA 80  80  80  ALA ALA B . n 
B 1 81  LEU 81  81  81  LEU LEU B . n 
B 1 82  GLN 82  82  82  GLN GLN B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  THR 84  84  84  THR THR B . n 
B 1 85  ASP 85  85  85  ASP ASP B . n 
B 1 86  VAL 86  86  86  VAL VAL B . n 
B 1 87  LYS 87  87  87  LYS LYS B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  GLN 89  89  89  GLN GLN B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  ALA 91  91  91  ALA ALA B . n 
B 1 92  GLY 92  92  92  GLY GLY B . n 
B 1 93  VAL 93  93  93  VAL VAL B . n 
B 1 94  TYR 94  94  94  TYR TYR B . n 
B 1 95  ARG 95  95  95  ARG ARG B . n 
B 1 96  CYS 96  96  96  CYS CYS B . n 
B 1 97  MET 97  97  97  MET MET B . n 
B 1 98  ILE 98  98  98  ILE ILE B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 TYR 100 100 100 TYR TYR B . n 
B 1 101 GLY 101 101 101 GLY GLY B . n 
B 1 102 GLY 102 102 102 GLY GLY B . n 
B 1 103 ALA 103 103 103 ALA ALA B . n 
B 1 104 ASP 104 104 104 ASP ASP B . n 
B 1 105 TYR 105 105 105 TYR TYR B . n 
B 1 106 LYS 106 106 106 LYS LYS B . n 
B 1 107 ARG 107 107 107 ARG ARG B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 THR 109 109 109 THR THR B . n 
B 1 110 VAL 110 110 110 VAL VAL B . n 
B 1 111 LYS 111 111 111 LYS LYS B . n 
B 1 112 VAL 112 112 112 VAL VAL B . n 
B 1 113 ASN 113 113 113 ASN ASN B . n 
B 1 114 ALA 114 114 114 ALA ALA B . n 
B 1 115 PRO 115 115 115 PRO PRO B . n 
B 1 116 TYR 116 116 116 TYR TYR B . n 
B 1 117 ALA 117 117 117 ALA ALA B . n 
B 1 118 ALA 118 118 118 ALA ALA B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 HIS 121 121 121 HIS HIS B . n 
B 1 122 HIS 122 122 ?   ?   ?   B . n 
B 1 123 HIS 123 123 ?   ?   ?   B . n 
B 1 124 HIS 124 124 ?   ?   ?   B . n 
B 1 125 ALA 125 125 ?   ?   ?   B . n 
B 1 126 ALA 126 126 ?   ?   ?   B . n 
# 
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 A1LV3 1  201 201 A1LV3 LIG B . 
D 3 HOH   1  201 92  HOH   HOH A . 
D 3 HOH   2  202 111 HOH   HOH A . 
D 3 HOH   3  203 4   HOH   HOH A . 
D 3 HOH   4  204 94  HOH   HOH A . 
D 3 HOH   5  205 24  HOH   HOH A . 
D 3 HOH   6  206 115 HOH   HOH A . 
D 3 HOH   7  207 3   HOH   HOH A . 
D 3 HOH   8  208 23  HOH   HOH A . 
D 3 HOH   9  209 2   HOH   HOH A . 
D 3 HOH   10 210 80  HOH   HOH A . 
D 3 HOH   11 211 18  HOH   HOH A . 
D 3 HOH   12 212 104 HOH   HOH A . 
D 3 HOH   13 213 96  HOH   HOH A . 
D 3 HOH   14 214 65  HOH   HOH A . 
D 3 HOH   15 215 114 HOH   HOH A . 
D 3 HOH   16 216 8   HOH   HOH A . 
D 3 HOH   17 217 117 HOH   HOH A . 
D 3 HOH   18 218 71  HOH   HOH A . 
D 3 HOH   19 219 33  HOH   HOH A . 
D 3 HOH   20 220 109 HOH   HOH A . 
D 3 HOH   21 221 59  HOH   HOH A . 
D 3 HOH   22 222 48  HOH   HOH A . 
D 3 HOH   23 223 85  HOH   HOH A . 
D 3 HOH   24 224 76  HOH   HOH A . 
D 3 HOH   25 225 17  HOH   HOH A . 
D 3 HOH   26 226 11  HOH   HOH A . 
D 3 HOH   27 227 10  HOH   HOH A . 
D 3 HOH   28 228 13  HOH   HOH A . 
D 3 HOH   29 229 103 HOH   HOH A . 
D 3 HOH   30 230 26  HOH   HOH A . 
D 3 HOH   31 231 108 HOH   HOH A . 
D 3 HOH   32 232 27  HOH   HOH A . 
D 3 HOH   33 233 12  HOH   HOH A . 
D 3 HOH   34 234 105 HOH   HOH A . 
D 3 HOH   35 235 32  HOH   HOH A . 
D 3 HOH   36 236 45  HOH   HOH A . 
D 3 HOH   37 237 70  HOH   HOH A . 
D 3 HOH   38 238 102 HOH   HOH A . 
D 3 HOH   39 239 99  HOH   HOH A . 
D 3 HOH   40 240 15  HOH   HOH A . 
D 3 HOH   41 241 41  HOH   HOH A . 
D 3 HOH   42 242 72  HOH   HOH A . 
D 3 HOH   43 243 57  HOH   HOH A . 
D 3 HOH   44 244 25  HOH   HOH A . 
D 3 HOH   45 245 100 HOH   HOH A . 
D 3 HOH   46 246 106 HOH   HOH A . 
D 3 HOH   47 247 119 HOH   HOH A . 
D 3 HOH   48 248 81  HOH   HOH A . 
D 3 HOH   49 249 91  HOH   HOH A . 
D 3 HOH   50 250 90  HOH   HOH A . 
D 3 HOH   51 251 50  HOH   HOH A . 
D 3 HOH   52 252 107 HOH   HOH A . 
D 3 HOH   53 253 46  HOH   HOH A . 
D 3 HOH   54 254 118 HOH   HOH A . 
D 3 HOH   55 255 38  HOH   HOH A . 
D 3 HOH   56 256 58  HOH   HOH A . 
D 3 HOH   57 257 31  HOH   HOH A . 
D 3 HOH   58 258 30  HOH   HOH A . 
D 3 HOH   59 259 101 HOH   HOH A . 
E 3 HOH   1  301 121 HOH   HOH B . 
E 3 HOH   2  302 78  HOH   HOH B . 
E 3 HOH   3  303 83  HOH   HOH B . 
E 3 HOH   4  304 63  HOH   HOH B . 
E 3 HOH   5  305 98  HOH   HOH B . 
E 3 HOH   6  306 86  HOH   HOH B . 
E 3 HOH   7  307 67  HOH   HOH B . 
E 3 HOH   8  308 68  HOH   HOH B . 
E 3 HOH   9  309 62  HOH   HOH B . 
E 3 HOH   10 310 88  HOH   HOH B . 
E 3 HOH   11 311 60  HOH   HOH B . 
E 3 HOH   12 312 97  HOH   HOH B . 
E 3 HOH   13 313 74  HOH   HOH B . 
E 3 HOH   14 314 69  HOH   HOH B . 
E 3 HOH   15 315 6   HOH   HOH B . 
E 3 HOH   16 316 116 HOH   HOH B . 
E 3 HOH   17 317 112 HOH   HOH B . 
E 3 HOH   18 318 34  HOH   HOH B . 
E 3 HOH   19 319 77  HOH   HOH B . 
E 3 HOH   20 320 9   HOH   HOH B . 
E 3 HOH   21 321 14  HOH   HOH B . 
E 3 HOH   22 322 75  HOH   HOH B . 
E 3 HOH   23 323 110 HOH   HOH B . 
E 3 HOH   24 324 64  HOH   HOH B . 
E 3 HOH   25 325 54  HOH   HOH B . 
E 3 HOH   26 326 93  HOH   HOH B . 
E 3 HOH   27 327 21  HOH   HOH B . 
E 3 HOH   28 328 16  HOH   HOH B . 
E 3 HOH   29 329 1   HOH   HOH B . 
E 3 HOH   30 330 22  HOH   HOH B . 
E 3 HOH   31 331 53  HOH   HOH B . 
E 3 HOH   32 332 73  HOH   HOH B . 
E 3 HOH   33 333 28  HOH   HOH B . 
E 3 HOH   34 334 66  HOH   HOH B . 
E 3 HOH   35 335 36  HOH   HOH B . 
E 3 HOH   36 336 35  HOH   HOH B . 
E 3 HOH   37 337 37  HOH   HOH B . 
E 3 HOH   38 338 19  HOH   HOH B . 
E 3 HOH   39 339 43  HOH   HOH B . 
E 3 HOH   40 340 7   HOH   HOH B . 
E 3 HOH   41 341 44  HOH   HOH B . 
E 3 HOH   42 342 29  HOH   HOH B . 
E 3 HOH   43 343 61  HOH   HOH B . 
E 3 HOH   44 344 42  HOH   HOH B . 
E 3 HOH   45 345 120 HOH   HOH B . 
E 3 HOH   46 346 95  HOH   HOH B . 
E 3 HOH   47 347 84  HOH   HOH B . 
E 3 HOH   48 348 51  HOH   HOH B . 
E 3 HOH   49 349 40  HOH   HOH B . 
E 3 HOH   50 350 5   HOH   HOH B . 
E 3 HOH   51 351 47  HOH   HOH B . 
E 3 HOH   52 352 113 HOH   HOH B . 
E 3 HOH   53 353 87  HOH   HOH B . 
E 3 HOH   54 354 56  HOH   HOH B . 
E 3 HOH   55 355 20  HOH   HOH B . 
E 3 HOH   56 356 39  HOH   HOH B . 
E 3 HOH   57 357 52  HOH   HOH B . 
E 3 HOH   58 358 79  HOH   HOH B . 
E 3 HOH   59 359 82  HOH   HOH B . 
E 3 HOH   60 360 49  HOH   HOH B . 
E 3 HOH   61 361 89  HOH   HOH B . 
E 3 HOH   62 362 55  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 27  ? OE2 ? A GLU 27  OE2 
2  1 Y 1 A ARG 64  ? CZ  ? A ARG 64  CZ  
3  1 Y 1 A ARG 64  ? NH1 ? A ARG 64  NH1 
4  1 Y 1 A ARG 64  ? NH2 ? A ARG 64  NH2 
5  1 Y 1 A ARG 107 ? CZ  ? A ARG 107 CZ  
6  1 Y 1 A ARG 107 ? NH1 ? A ARG 107 NH1 
7  1 Y 1 A ARG 107 ? NH2 ? A ARG 107 NH2 
8  1 Y 1 A LYS 111 ? CD  ? A LYS 111 CD  
9  1 Y 1 A LYS 111 ? CE  ? A LYS 111 CE  
10 1 Y 1 A LYS 111 ? NZ  ? A LYS 111 NZ  
11 1 Y 1 B GLU 27  ? OE2 ? B GLU 27  OE2 
12 1 Y 1 B LYS 28  ? CD  ? B LYS 28  CD  
13 1 Y 1 B LYS 28  ? NZ  ? B LYS 28  NZ  
14 1 Y 1 B ARG 64  ? CZ  ? B ARG 64  CZ  
15 1 Y 1 B ARG 64  ? NH1 ? B ARG 64  NH1 
16 1 Y 1 B ARG 64  ? NH2 ? B ARG 64  NH2 
17 1 Y 1 B ARG 107 ? CZ  ? B ARG 107 CZ  
18 1 Y 1 B ARG 107 ? NH1 ? B ARG 107 NH1 
19 1 Y 1 B ARG 107 ? NH2 ? B ARG 107 NH2 
20 1 Y 1 B LYS 111 ? CD  ? B LYS 111 CD  
21 1 Y 1 B LYS 111 ? CE  ? B LYS 111 CE  
22 1 Y 1 B LYS 111 ? NZ  ? B LYS 111 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8XR5 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     109.171 
_cell.length_a_esd                 ? 
_cell.length_b                     49.090 
_cell.length_b_esd                 ? 
_cell.length_c                     51.849 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8XR5 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8XR5 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.45 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.71 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '19% PEG3350 and 0.2 M Ammonium tartrate dibasic' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER2 S 9M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-01-12 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9790 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'SSRF BEAMLINE BL02U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9790 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL02U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8XR5 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               50.00 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     20788 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          6.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               2.592 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.125 
_reflns.pdbx_Rpim_I_all                                0.037 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.120 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.95 1.98  ? ? ? ? ? ? 1008 ? ? ? ? ? ? ? ? ? ? ? 9.5  0.652 ? ? 0.726 0.226 ? 1  1 0.879 0.967 ? 98.6  ? 0.688 ? ? ? ? ? ? ? ? ? 
1.98 2.02  ? ? ? ? ? ? 987  ? ? ? ? ? ? ? ? ? ? ? 11.0 0.701 ? ? 0.582 0.170 ? 2  1 0.929 0.981 ? 98.0  ? 0.556 ? ? ? ? ? ? ? ? ? 
2.02 2.06  ? ? ? ? ? ? 1028 ? ? ? ? ? ? ? ? ? ? ? 11.5 0.790 ? ? 0.568 0.163 ? 3  1 0.940 0.984 ? 99.2  ? 0.544 ? ? ? ? ? ? ? ? ? 
2.06 2.10  ? ? ? ? ? ? 1008 ? ? ? ? ? ? ? ? ? ? ? 11.7 0.732 ? ? 0.553 0.158 ? 4  1 0.933 0.983 ? 100.0 ? 0.529 ? ? ? ? ? ? ? ? ? 
2.10 2.15  ? ? ? ? ? ? 1019 ? ? ? ? ? ? ? ? ? ? ? 12.1 0.919 ? ? 0.483 0.137 ? 5  1 0.960 0.990 ? 99.7  ? 0.463 ? ? ? ? ? ? ? ? ? 
2.15 2.20  ? ? ? ? ? ? 1016 ? ? ? ? ? ? ? ? ? ? ? 12.2 1.022 ? ? 0.411 0.118 ? 6  1 0.919 0.979 ? 100.0 ? 0.393 ? ? ? ? ? ? ? ? ? 
2.20 2.25  ? ? ? ? ? ? 1043 ? ? ? ? ? ? ? ? ? ? ? 11.9 1.216 ? ? 0.377 0.109 ? 7  1 0.945 0.986 ? 100.0 ? 0.360 ? ? ? ? ? ? ? ? ? 
2.25 2.31  ? ? ? ? ? ? 1018 ? ? ? ? ? ? ? ? ? ? ? 12.3 1.181 ? ? 0.332 0.094 ? 8  1 0.977 0.994 ? 100.0 ? 0.318 ? ? ? ? ? ? ? ? ? 
2.31 2.38  ? ? ? ? ? ? 1029 ? ? ? ? ? ? ? ? ? ? ? 13.2 1.459 ? ? 0.309 0.086 ? 9  1 0.979 0.995 ? 100.0 ? 0.297 ? ? ? ? ? ? ? ? ? 
2.38 2.46  ? ? ? ? ? ? 1047 ? ? ? ? ? ? ? ? ? ? ? 13.3 1.459 ? ? 0.269 0.074 ? 10 1 0.979 0.995 ? 100.0 ? 0.258 ? ? ? ? ? ? ? ? ? 
2.46 2.54  ? ? ? ? ? ? 1025 ? ? ? ? ? ? ? ? ? ? ? 13.1 1.627 ? ? 0.235 0.065 ? 11 1 0.984 0.996 ? 100.0 ? 0.226 ? ? ? ? ? ? ? ? ? 
2.54 2.65  ? ? ? ? ? ? 1025 ? ? ? ? ? ? ? ? ? ? ? 12.8 2.056 ? ? 0.216 0.061 ? 12 1 0.981 0.995 ? 100.0 ? 0.206 ? ? ? ? ? ? ? ? ? 
2.65 2.77  ? ? ? ? ? ? 1036 ? ? ? ? ? ? ? ? ? ? ? 12.1 2.541 ? ? 0.189 0.055 ? 13 1 0.988 0.997 ? 100.0 ? 0.180 ? ? ? ? ? ? ? ? ? 
2.77 2.91  ? ? ? ? ? ? 1036 ? ? ? ? ? ? ? ? ? ? ? 12.6 3.095 ? ? 0.170 0.048 ? 14 1 0.992 0.998 ? 100.0 ? 0.163 ? ? ? ? ? ? ? ? ? 
2.91 3.10  ? ? ? ? ? ? 1057 ? ? ? ? ? ? ? ? ? ? ? 13.2 3.586 ? ? 0.155 0.044 ? 15 1 0.992 0.998 ? 100.0 ? 0.149 ? ? ? ? ? ? ? ? ? 
3.10 3.33  ? ? ? ? ? ? 1044 ? ? ? ? ? ? ? ? ? ? ? 12.9 4.322 ? ? 0.141 0.040 ? 16 1 0.993 0.998 ? 100.0 ? 0.135 ? ? ? ? ? ? ? ? ? 
3.33 3.67  ? ? ? ? ? ? 1050 ? ? ? ? ? ? ? ? ? ? ? 12.1 5.409 ? ? 0.135 0.040 ? 17 1 0.968 0.992 ? 100.0 ? 0.129 ? ? ? ? ? ? ? ? ? 
3.67 4.20  ? ? ? ? ? ? 1066 ? ? ? ? ? ? ? ? ? ? ? 12.9 5.418 ? ? 0.115 0.033 ? 18 1 0.991 0.998 ? 100.0 ? 0.110 ? ? ? ? ? ? ? ? ? 
4.20 5.29  ? ? ? ? ? ? 1077 ? ? ? ? ? ? ? ? ? ? ? 12.2 5.711 ? ? 0.097 0.028 ? 19 1 0.991 0.998 ? 99.9  ? 0.092 ? ? ? ? ? ? ? ? ? 
5.29 50.00 ? ? ? ? ? ? 1169 ? ? ? ? ? ? ? ? ? ? ? 11.3 6.288 ? ? 0.101 0.032 ? 20 1 0.981 0.995 ? 99.5  ? 0.095 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8XR5 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             37.59 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     20635 
_refine.ls_number_reflns_R_free                  2005 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.94 
_refine.ls_percent_reflns_R_free                 9.72 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2302 
_refine.ls_R_factor_R_free                       0.2569 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2273 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.36 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      4Z18 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.24 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.24 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        37.59 
_refine_hist.number_atoms_solvent             121 
_refine_hist.number_atoms_total               2141 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2020 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.004  ? 2067 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.605  ? 2800 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 20.306 ? 743  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.061  ? 307  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009  ? 349  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.95 2.00  . . 134 1209 92.00  . . . . 0.3208 . . . . . . . . . . . 0.3507 
'X-RAY DIFFRACTION' 2.00 2.06  . . 140 1280 97.00  . . . . 0.2758 . . . . . . . . . . . 0.3044 
'X-RAY DIFFRACTION' 2.06 2.12  . . 136 1303 99.00  . . . . 0.2795 . . . . . . . . . . . 0.2976 
'X-RAY DIFFRACTION' 2.12 2.19  . . 145 1306 99.00  . . . . 0.2740 . . . . . . . . . . . 0.2855 
'X-RAY DIFFRACTION' 2.19 2.26  . . 138 1330 99.00  . . . . 0.2731 . . . . . . . . . . . 0.2981 
'X-RAY DIFFRACTION' 2.26 2.36  . . 138 1330 100.00 . . . . 0.2620 . . . . . . . . . . . 0.2987 
'X-RAY DIFFRACTION' 2.36 2.46  . . 146 1329 100.00 . . . . 0.2724 . . . . . . . . . . . 0.2848 
'X-RAY DIFFRACTION' 2.46 2.59  . . 141 1323 100.00 . . . . 0.2732 . . . . . . . . . . . 0.2912 
'X-RAY DIFFRACTION' 2.59 2.75  . . 142 1331 100.00 . . . . 0.2642 . . . . . . . . . . . 0.3280 
'X-RAY DIFFRACTION' 2.76 2.97  . . 146 1334 100.00 . . . . 0.2523 . . . . . . . . . . . 0.2441 
'X-RAY DIFFRACTION' 2.97 3.27  . . 144 1368 100.00 . . . . 0.2464 . . . . . . . . . . . 0.2641 
'X-RAY DIFFRACTION' 3.27 3.74  . . 150 1359 100.00 . . . . 0.2120 . . . . . . . . . . . 0.2583 
'X-RAY DIFFRACTION' 3.74 4.71  . . 153 1368 100.00 . . . . 0.1819 . . . . . . . . . . . 0.1936 
'X-RAY DIFFRACTION' 4.71 37.59 . . 152 1460 100.00 . . . . 0.2120 . . . . . . . . . . . 0.2674 
# 
_struct.entry_id                     8XR5 
_struct.title                        'Crystal structure of PD-L1 complexed with small molecule inhibitor X18' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        8XR5 
_struct_keywords.text            'Programmed death-ligand 1, inhibitor, IMMUNOSUPPRESSANT, IMMUNOSUPPRESSANT-INHIBITOR complex' 
_struct_keywords.pdbx_keywords   IMMUNOSUPPRESSANT/INHIBITOR 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PD1L1_HUMAN 
_struct_ref.pdbx_db_accession          Q9NZQ7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;FTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNAA
LQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPY
;
_struct_ref.pdbx_align_begin           19 
# 
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 8XR5 A 1 ? 116 ? Q9NZQ7 19 ? 134 ? 1 116 
2 1 8XR5 B 1 ? 116 ? Q9NZQ7 19 ? 134 ? 1 116 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8XR5 ALA A 117 ? UNP Q9NZQ7 ? ? 'expression tag' 117 1  
1 8XR5 ALA A 118 ? UNP Q9NZQ7 ? ? 'expression tag' 118 2  
1 8XR5 HIS A 119 ? UNP Q9NZQ7 ? ? 'expression tag' 119 3  
1 8XR5 HIS A 120 ? UNP Q9NZQ7 ? ? 'expression tag' 120 4  
1 8XR5 HIS A 121 ? UNP Q9NZQ7 ? ? 'expression tag' 121 5  
1 8XR5 HIS A 122 ? UNP Q9NZQ7 ? ? 'expression tag' 122 6  
1 8XR5 HIS A 123 ? UNP Q9NZQ7 ? ? 'expression tag' 123 7  
1 8XR5 HIS A 124 ? UNP Q9NZQ7 ? ? 'expression tag' 124 8  
1 8XR5 ALA A 125 ? UNP Q9NZQ7 ? ? 'expression tag' 125 9  
1 8XR5 ALA A 126 ? UNP Q9NZQ7 ? ? 'expression tag' 126 10 
2 8XR5 ALA B 117 ? UNP Q9NZQ7 ? ? 'expression tag' 117 11 
2 8XR5 ALA B 118 ? UNP Q9NZQ7 ? ? 'expression tag' 118 12 
2 8XR5 HIS B 119 ? UNP Q9NZQ7 ? ? 'expression tag' 119 13 
2 8XR5 HIS B 120 ? UNP Q9NZQ7 ? ? 'expression tag' 120 14 
2 8XR5 HIS B 121 ? UNP Q9NZQ7 ? ? 'expression tag' 121 15 
2 8XR5 HIS B 122 ? UNP Q9NZQ7 ? ? 'expression tag' 122 16 
2 8XR5 HIS B 123 ? UNP Q9NZQ7 ? ? 'expression tag' 123 17 
2 8XR5 HIS B 124 ? UNP Q9NZQ7 ? ? 'expression tag' 124 18 
2 8XR5 ALA B 125 ? UNP Q9NZQ7 ? ? 'expression tag' 125 19 
2 8XR5 ALA B 126 ? UNP Q9NZQ7 ? ? 'expression tag' 126 20 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'surface plasmon resonance' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 ASP A 31  ? ALA A 33  ? ASP A 31  ALA A 33  5 ? 3  
HELX_P HELX_P2  AA2 HIS A 60  ? ARG A 64  ? HIS A 60  ARG A 64  5 ? 5  
HELX_P HELX_P3  AA3 LYS A 71  ? LEU A 76  ? LYS A 71  LEU A 76  5 ? 6  
HELX_P HELX_P4  AA4 LYS A 87  ? ALA A 91  ? LYS A 87  ALA A 91  5 ? 5  
HELX_P HELX_P5  AA5 PRO A 115 ? ALA A 126 ? PRO A 115 ALA A 126 1 ? 12 
HELX_P HELX_P6  AA6 ASP B 31  ? ALA B 33  ? ASP B 31  ALA B 33  5 ? 3  
HELX_P HELX_P7  AA7 HIS B 60  ? ARG B 64  ? HIS B 60  ARG B 64  5 ? 5  
HELX_P HELX_P8  AA8 LYS B 71  ? GLY B 77  ? LYS B 71  GLY B 77  5 ? 7  
HELX_P HELX_P9  AA9 LYS B 87  ? ALA B 91  ? LYS B 87  ALA B 91  5 ? 5  
HELX_P HELX_P10 AB1 PRO B 115 ? HIS B 121 ? PRO B 115 HIS B 121 1 ? 7  
# 
_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 
disulf1 disulf ? ? A CYS 22 SG ? ? ? 1_555 A CYS 96 SG ? ? A CYS 22 A CYS 96 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
disulf2 disulf ? ? B CYS 22 SG ? ? ? 1_555 B CYS 96 SG ? ? B CYS 22 B CYS 96 1_555 ? ? ? ? ? ? ? 2.039 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 CYS A 22 ? CYS A 96 ? CYS A 22 ? 1_555 CYS A 96 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 22 ? CYS B 96 ? CYS B 22 ? 1_555 CYS B 96 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 3 ? 
AA3 ? 6 ? 
AA4 ? 3 ? 
# 
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 ? parallel      
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA3 4 5 ? anti-parallel 
AA3 5 6 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? 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 9   ? GLU A 13  ? LEU A 9   GLU A 13  
AA1 2 ALA A 103 ? ASN A 113 ? ALA A 103 ASN A 113 
AA1 3 GLY A 92  ? TYR A 100 ? GLY A 92  TYR A 100 
AA1 4 LEU A 35  ? MET A 41  ? LEU A 35  MET A 41  
AA1 5 LYS A 44  ? VAL A 50  ? LYS A 44  VAL A 50  
AA1 6 GLU A 53  ? GLU A 54  ? GLU A 53  GLU A 54  
AA2 1 MET A 18  ? LYS A 23  ? MET A 18  LYS A 23  
AA2 2 ASN A 78  ? ILE A 83  ? ASN A 78  ILE A 83  
AA2 3 ALA A 67  ? LEU A 69  ? ALA A 67  LEU A 69  
AA3 1 LEU B 9   ? GLU B 13  ? LEU B 9   GLU B 13  
AA3 2 ALA B 103 ? ASN B 113 ? ALA B 103 ASN B 113 
AA3 3 GLY B 92  ? TYR B 100 ? GLY B 92  TYR B 100 
AA3 4 LEU B 35  ? MET B 41  ? LEU B 35  MET B 41  
AA3 5 LYS B 44  ? VAL B 50  ? LYS B 44  VAL B 50  
AA3 6 GLU B 53  ? GLU B 54  ? GLU B 53  GLU B 54  
AA4 1 MET B 18  ? ILE B 20  ? MET B 18  ILE B 20  
AA4 2 LEU B 81  ? ILE B 83  ? LEU B 81  ILE B 83  
AA4 3 ALA B 67  ? LEU B 69  ? ALA B 67  LEU B 69  
# 
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 TYR A 10  ? N TYR A 10  O LYS A 111 ? O LYS A 111 
AA1 2 3 O ILE A 108 ? O ILE A 108 N TYR A 94  ? N TYR A 94  
AA1 3 4 O ARG A 95  ? O ARG A 95  N GLU A 40  ? N GLU A 40  
AA1 4 5 N VAL A 37  ? N VAL A 37  O PHE A 49  ? O PHE A 49  
AA1 5 6 N VAL A 50  ? N VAL A 50  O GLU A 53  ? O GLU A 53  
AA2 1 2 N ILE A 20  ? N ILE A 20  O LEU A 81  ? O LEU A 81  
AA2 2 3 O GLN A 82  ? O GLN A 82  N ARG A 68  ? N ARG A 68  
AA3 1 2 N TYR B 10  ? N TYR B 10  O LYS B 111 ? O LYS B 111 
AA3 2 3 O ILE B 108 ? O ILE B 108 N TYR B 94  ? N TYR B 94  
AA3 3 4 O ARG B 95  ? O ARG B 95  N GLU B 40  ? N GLU B 40  
AA3 4 5 N VAL B 37  ? N VAL B 37  O PHE B 49  ? O PHE B 49  
AA3 5 6 N VAL B 50  ? N VAL B 50  O GLU B 53  ? O GLU B 53  
AA4 1 2 N MET B 18  ? N MET B 18  O ILE B 83  ? O ILE B 83  
AA4 2 3 O GLN B 82  ? O GLN B 82  N ARG B 68  ? N ARG B 68  
# 
_pdbx_entry_details.entry_id                   8XR5 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
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   B HOH 346 ? ? O   B HOH 351 ? ? 1.80 
2  1 O   B ALA 33  ? ? O   B HOH 301 ? ? 1.85 
3  1 O   B HOH 316 ? ? O   B HOH 326 ? ? 1.86 
4  1 OH  A TYR 105 ? ? O   A HOH 201 ? ? 1.88 
5  1 O   B HOH 324 ? ? O   B HOH 356 ? ? 1.94 
6  1 N   B GLY 52  ? ? O   B HOH 302 ? ? 1.95 
7  1 O   B HOH 322 ? ? O   B HOH 349 ? ? 1.96 
8  1 OG  A SER 99  ? ? O   A HOH 202 ? ? 1.99 
9  1 OH  A TYR 38  ? ? O   A HOH 203 ? ? 2.01 
10 1 OH  B TYR 14  ? ? O   B HOH 303 ? ? 2.02 
11 1 CA  B ALA 33  ? ? O   B HOH 301 ? ? 2.05 
12 1 O   B HOH 351 ? ? O   B HOH 356 ? ? 2.06 
13 1 NZ  B LYS 23  ? ? OD1 B ASN 78  ? ? 2.07 
14 1 NZ  A LYS 87  ? ? O   A HOH 204 ? ? 2.07 
15 1 O   A HOH 237 ? ? O   A HOH 249 ? ? 2.13 
16 1 NE2 B GLN 29  ? ? O   B HOH 304 ? ? 2.15 
17 1 C   B ALA 33  ? ? O   B HOH 301 ? ? 2.17 
18 1 O   B HOH 358 ? ? O   B HOH 359 ? ? 2.19 
19 1 O   B ALA 34  ? ? O   B HOH 305 ? ? 2.19 
20 1 O   B HOH 313 ? ? O   B HOH 346 ? ? 2.19 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OE1 
_pdbx_validate_symm_contact.auth_asym_id_1    B 
_pdbx_validate_symm_contact.auth_comp_id_1    GLN 
_pdbx_validate_symm_contact.auth_seq_id_1     65 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    CB 
_pdbx_validate_symm_contact.auth_asym_id_2    B 
_pdbx_validate_symm_contact.auth_comp_id_2    SER 
_pdbx_validate_symm_contact.auth_seq_id_2     75 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   3_446 
_pdbx_validate_symm_contact.dist              1.87 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            A 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             53 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            ? 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            A 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             53 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            ? 
_pdbx_validate_rmsd_bond.bond_value                1.180 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            -0.072 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 N   A GLU 27 ? ? CA A GLU 27 ? ? C   A GLU 27 ? ? 93.40  111.00 -17.60 2.70 N 
2 1 OE1 A GLU 53 ? ? CD A GLU 53 ? ? OE2 A GLU 53 ? ? 86.43  123.30 -36.87 1.20 N 
3 1 CG  A GLU 53 ? ? CD A GLU 53 ? ? OE1 A GLU 53 ? ? 80.07  118.30 -38.23 2.00 N 
4 1 CG  A GLU 53 ? ? CD A GLU 53 ? ? OE2 A GLU 53 ? ? 162.11 118.30 43.81  2.00 N 
5 1 CA  B CYS 22 ? ? CB B CYS 22 ? ? SG  B CYS 22 ? ? 121.38 114.20 7.18   1.10 N 
# 
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 GLU A 27 ? ? 52.60 -119.05 
2 1 GLU A 42 ? ? 59.38 -110.40 
3 1 ASP A 85 ? ? 61.35 62.44   
4 1 GLU B 42 ? ? 56.78 -109.21 
5 1 ASP B 85 ? ? 61.81 62.12   
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     347 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   E 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 B HIS 122 ? B HIS 122 
2 1 Y 1 B HIS 123 ? B HIS 123 
3 1 Y 1 B HIS 124 ? B HIS 124 
4 1 Y 1 B ALA 125 ? B ALA 125 
5 1 Y 1 B ALA 126 ? B ALA 126 
# 
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 
A1LV3 C10  C  Y N 1   
A1LV3 C13  C  Y N 2   
A1LV3 C15  C  N N 3   
A1LV3 C21  C  N N 4   
A1LV3 C24  C  N N 5   
A1LV3 C26  C  Y N 6   
A1LV3 C28  C  Y N 7   
A1LV3 C01  C  Y N 8   
A1LV3 C02  C  Y N 9   
A1LV3 C03  C  Y N 10  
A1LV3 C04  C  Y N 11  
A1LV3 C05  C  Y N 12  
A1LV3 C06  C  Y N 13  
A1LV3 C08  C  Y N 14  
A1LV3 C09  C  Y N 15  
A1LV3 C11  C  Y N 16  
A1LV3 C12  C  Y N 17  
A1LV3 C18  C  N R 18  
A1LV3 C19  C  N N 19  
A1LV3 C25  C  Y N 20  
A1LV3 C27  C  Y N 21  
A1LV3 C29  C  Y N 22  
A1LV3 C30  C  Y N 23  
A1LV3 C31  C  Y N 24  
A1LV3 C33  C  Y N 25  
A1LV3 C34  C  Y N 26  
A1LV3 C35  C  Y N 27  
A1LV3 C36  C  Y N 28  
A1LV3 C37  C  Y N 29  
A1LV3 C39  C  N N 30  
A1LV3 C40  C  N N 31  
A1LV3 C41  C  N N 32  
A1LV3 C43  C  N N 33  
A1LV3 C44  C  N N 34  
A1LV3 C45  C  N N 35  
A1LV3 C46  C  N N 36  
A1LV3 C47  C  N N 37  
A1LV3 C52  C  N N 38  
A1LV3 F32  F  N N 39  
A1LV3 N16  N  N N 40  
A1LV3 N42  N  N N 41  
A1LV3 N49  N  Y N 42  
A1LV3 N50  N  Y N 43  
A1LV3 O07  O  N N 44  
A1LV3 O17  O  N N 45  
A1LV3 O20  O  N N 46  
A1LV3 O22  O  N N 47  
A1LV3 O23  O  N N 48  
A1LV3 O38  O  N N 49  
A1LV3 O48  O  N N 50  
A1LV3 O51  O  Y N 51  
A1LV3 CL14 CL N N 52  
A1LV3 H131 H  N N 53  
A1LV3 H152 H  N N 54  
A1LV3 H151 H  N N 55  
A1LV3 H242 H  N N 56  
A1LV3 H241 H  N N 57  
A1LV3 H281 H  N N 58  
A1LV3 H011 H  N N 59  
A1LV3 H041 H  N N 60  
A1LV3 H091 H  N N 61  
A1LV3 H121 H  N N 62  
A1LV3 H181 H  N N 63  
A1LV3 H191 H  N N 64  
A1LV3 H192 H  N N 65  
A1LV3 H291 H  N N 66  
A1LV3 H301 H  N N 67  
A1LV3 H331 H  N N 68  
A1LV3 H341 H  N N 69  
A1LV3 H351 H  N N 70  
A1LV3 H371 H  N N 71  
A1LV3 H391 H  N N 72  
A1LV3 H392 H  N N 73  
A1LV3 H401 H  N N 74  
A1LV3 H402 H  N N 75  
A1LV3 H411 H  N N 76  
A1LV3 H412 H  N N 77  
A1LV3 H431 H  N N 78  
A1LV3 H432 H  N N 79  
A1LV3 H441 H  N N 80  
A1LV3 H442 H  N N 81  
A1LV3 H451 H  N N 82  
A1LV3 H462 H  N N 83  
A1LV3 H461 H  N N 84  
A1LV3 H472 H  N N 85  
A1LV3 H471 H  N N 86  
A1LV3 H521 H  N N 87  
A1LV3 H522 H  N N 88  
A1LV3 H1   H  N N 89  
A1LV3 H201 H  N N 90  
A1LV3 H3   H  N N 91  
A1LV3 H481 H  N N 92  
ALA   N    N  N N 93  
ALA   CA   C  N S 94  
ALA   C    C  N N 95  
ALA   O    O  N N 96  
ALA   CB   C  N N 97  
ALA   OXT  O  N N 98  
ALA   H    H  N N 99  
ALA   H2   H  N N 100 
ALA   HA   H  N N 101 
ALA   HB1  H  N N 102 
ALA   HB2  H  N N 103 
ALA   HB3  H  N N 104 
ALA   HXT  H  N N 105 
ARG   N    N  N N 106 
ARG   CA   C  N S 107 
ARG   C    C  N N 108 
ARG   O    O  N N 109 
ARG   CB   C  N N 110 
ARG   CG   C  N N 111 
ARG   CD   C  N N 112 
ARG   NE   N  N N 113 
ARG   CZ   C  N N 114 
ARG   NH1  N  N N 115 
ARG   NH2  N  N N 116 
ARG   OXT  O  N N 117 
ARG   H    H  N N 118 
ARG   H2   H  N N 119 
ARG   HA   H  N N 120 
ARG   HB2  H  N N 121 
ARG   HB3  H  N N 122 
ARG   HG2  H  N N 123 
ARG   HG3  H  N N 124 
ARG   HD2  H  N N 125 
ARG   HD3  H  N N 126 
ARG   HE   H  N N 127 
ARG   HH11 H  N N 128 
ARG   HH12 H  N N 129 
ARG   HH21 H  N N 130 
ARG   HH22 H  N N 131 
ARG   HXT  H  N N 132 
ASN   N    N  N N 133 
ASN   CA   C  N S 134 
ASN   C    C  N N 135 
ASN   O    O  N N 136 
ASN   CB   C  N N 137 
ASN   CG   C  N N 138 
ASN   OD1  O  N N 139 
ASN   ND2  N  N N 140 
ASN   OXT  O  N N 141 
ASN   H    H  N N 142 
ASN   H2   H  N N 143 
ASN   HA   H  N N 144 
ASN   HB2  H  N N 145 
ASN   HB3  H  N N 146 
ASN   HD21 H  N N 147 
ASN   HD22 H  N N 148 
ASN   HXT  H  N N 149 
ASP   N    N  N N 150 
ASP   CA   C  N S 151 
ASP   C    C  N N 152 
ASP   O    O  N N 153 
ASP   CB   C  N N 154 
ASP   CG   C  N N 155 
ASP   OD1  O  N N 156 
ASP   OD2  O  N N 157 
ASP   OXT  O  N N 158 
ASP   H    H  N N 159 
ASP   H2   H  N N 160 
ASP   HA   H  N N 161 
ASP   HB2  H  N N 162 
ASP   HB3  H  N N 163 
ASP   HD2  H  N N 164 
ASP   HXT  H  N N 165 
CYS   N    N  N N 166 
CYS   CA   C  N R 167 
CYS   C    C  N N 168 
CYS   O    O  N N 169 
CYS   CB   C  N N 170 
CYS   SG   S  N N 171 
CYS   OXT  O  N N 172 
CYS   H    H  N N 173 
CYS   H2   H  N N 174 
CYS   HA   H  N N 175 
CYS   HB2  H  N N 176 
CYS   HB3  H  N N 177 
CYS   HG   H  N N 178 
CYS   HXT  H  N N 179 
GLN   N    N  N N 180 
GLN   CA   C  N S 181 
GLN   C    C  N N 182 
GLN   O    O  N N 183 
GLN   CB   C  N N 184 
GLN   CG   C  N N 185 
GLN   CD   C  N N 186 
GLN   OE1  O  N N 187 
GLN   NE2  N  N N 188 
GLN   OXT  O  N N 189 
GLN   H    H  N N 190 
GLN   H2   H  N N 191 
GLN   HA   H  N N 192 
GLN   HB2  H  N N 193 
GLN   HB3  H  N N 194 
GLN   HG2  H  N N 195 
GLN   HG3  H  N N 196 
GLN   HE21 H  N N 197 
GLN   HE22 H  N N 198 
GLN   HXT  H  N N 199 
GLU   N    N  N N 200 
GLU   CA   C  N S 201 
GLU   C    C  N N 202 
GLU   O    O  N N 203 
GLU   CB   C  N N 204 
GLU   CG   C  N N 205 
GLU   CD   C  N N 206 
GLU   OE1  O  N N 207 
GLU   OE2  O  N N 208 
GLU   OXT  O  N N 209 
GLU   H    H  N N 210 
GLU   H2   H  N N 211 
GLU   HA   H  N N 212 
GLU   HB2  H  N N 213 
GLU   HB3  H  N N 214 
GLU   HG2  H  N N 215 
GLU   HG3  H  N N 216 
GLU   HE2  H  N N 217 
GLU   HXT  H  N N 218 
GLY   N    N  N N 219 
GLY   CA   C  N N 220 
GLY   C    C  N N 221 
GLY   O    O  N N 222 
GLY   OXT  O  N N 223 
GLY   H    H  N N 224 
GLY   H2   H  N N 225 
GLY   HA2  H  N N 226 
GLY   HA3  H  N N 227 
GLY   HXT  H  N N 228 
HIS   N    N  N N 229 
HIS   CA   C  N S 230 
HIS   C    C  N N 231 
HIS   O    O  N N 232 
HIS   CB   C  N N 233 
HIS   CG   C  Y N 234 
HIS   ND1  N  Y N 235 
HIS   CD2  C  Y N 236 
HIS   CE1  C  Y N 237 
HIS   NE2  N  Y N 238 
HIS   OXT  O  N N 239 
HIS   H    H  N N 240 
HIS   H2   H  N N 241 
HIS   HA   H  N N 242 
HIS   HB2  H  N N 243 
HIS   HB3  H  N N 244 
HIS   HD1  H  N N 245 
HIS   HD2  H  N N 246 
HIS   HE1  H  N N 247 
HIS   HE2  H  N N 248 
HIS   HXT  H  N N 249 
HOH   O    O  N N 250 
HOH   H1   H  N N 251 
HOH   H2   H  N N 252 
ILE   N    N  N N 253 
ILE   CA   C  N S 254 
ILE   C    C  N N 255 
ILE   O    O  N N 256 
ILE   CB   C  N S 257 
ILE   CG1  C  N N 258 
ILE   CG2  C  N N 259 
ILE   CD1  C  N N 260 
ILE   OXT  O  N N 261 
ILE   H    H  N N 262 
ILE   H2   H  N N 263 
ILE   HA   H  N N 264 
ILE   HB   H  N N 265 
ILE   HG12 H  N N 266 
ILE   HG13 H  N N 267 
ILE   HG21 H  N N 268 
ILE   HG22 H  N N 269 
ILE   HG23 H  N N 270 
ILE   HD11 H  N N 271 
ILE   HD12 H  N N 272 
ILE   HD13 H  N N 273 
ILE   HXT  H  N N 274 
LEU   N    N  N N 275 
LEU   CA   C  N S 276 
LEU   C    C  N N 277 
LEU   O    O  N N 278 
LEU   CB   C  N N 279 
LEU   CG   C  N N 280 
LEU   CD1  C  N N 281 
LEU   CD2  C  N N 282 
LEU   OXT  O  N N 283 
LEU   H    H  N N 284 
LEU   H2   H  N N 285 
LEU   HA   H  N N 286 
LEU   HB2  H  N N 287 
LEU   HB3  H  N N 288 
LEU   HG   H  N N 289 
LEU   HD11 H  N N 290 
LEU   HD12 H  N N 291 
LEU   HD13 H  N N 292 
LEU   HD21 H  N N 293 
LEU   HD22 H  N N 294 
LEU   HD23 H  N N 295 
LEU   HXT  H  N N 296 
LYS   N    N  N N 297 
LYS   CA   C  N S 298 
LYS   C    C  N N 299 
LYS   O    O  N N 300 
LYS   CB   C  N N 301 
LYS   CG   C  N N 302 
LYS   CD   C  N N 303 
LYS   CE   C  N N 304 
LYS   NZ   N  N N 305 
LYS   OXT  O  N N 306 
LYS   H    H  N N 307 
LYS   H2   H  N N 308 
LYS   HA   H  N N 309 
LYS   HB2  H  N N 310 
LYS   HB3  H  N N 311 
LYS   HG2  H  N N 312 
LYS   HG3  H  N N 313 
LYS   HD2  H  N N 314 
LYS   HD3  H  N N 315 
LYS   HE2  H  N N 316 
LYS   HE3  H  N N 317 
LYS   HZ1  H  N N 318 
LYS   HZ2  H  N N 319 
LYS   HZ3  H  N N 320 
LYS   HXT  H  N N 321 
MET   N    N  N N 322 
MET   CA   C  N S 323 
MET   C    C  N N 324 
MET   O    O  N N 325 
MET   CB   C  N N 326 
MET   CG   C  N N 327 
MET   SD   S  N N 328 
MET   CE   C  N N 329 
MET   OXT  O  N N 330 
MET   H    H  N N 331 
MET   H2   H  N N 332 
MET   HA   H  N N 333 
MET   HB2  H  N N 334 
MET   HB3  H  N N 335 
MET   HG2  H  N N 336 
MET   HG3  H  N N 337 
MET   HE1  H  N N 338 
MET   HE2  H  N N 339 
MET   HE3  H  N N 340 
MET   HXT  H  N N 341 
PHE   N    N  N N 342 
PHE   CA   C  N S 343 
PHE   C    C  N N 344 
PHE   O    O  N N 345 
PHE   CB   C  N N 346 
PHE   CG   C  Y N 347 
PHE   CD1  C  Y N 348 
PHE   CD2  C  Y N 349 
PHE   CE1  C  Y N 350 
PHE   CE2  C  Y N 351 
PHE   CZ   C  Y N 352 
PHE   OXT  O  N N 353 
PHE   H    H  N N 354 
PHE   H2   H  N N 355 
PHE   HA   H  N N 356 
PHE   HB2  H  N N 357 
PHE   HB3  H  N N 358 
PHE   HD1  H  N N 359 
PHE   HD2  H  N N 360 
PHE   HE1  H  N N 361 
PHE   HE2  H  N N 362 
PHE   HZ   H  N N 363 
PHE   HXT  H  N N 364 
PRO   N    N  N N 365 
PRO   CA   C  N S 366 
PRO   C    C  N N 367 
PRO   O    O  N N 368 
PRO   CB   C  N N 369 
PRO   CG   C  N N 370 
PRO   CD   C  N N 371 
PRO   OXT  O  N N 372 
PRO   H    H  N N 373 
PRO   HA   H  N N 374 
PRO   HB2  H  N N 375 
PRO   HB3  H  N N 376 
PRO   HG2  H  N N 377 
PRO   HG3  H  N N 378 
PRO   HD2  H  N N 379 
PRO   HD3  H  N N 380 
PRO   HXT  H  N N 381 
SER   N    N  N N 382 
SER   CA   C  N S 383 
SER   C    C  N N 384 
SER   O    O  N N 385 
SER   CB   C  N N 386 
SER   OG   O  N N 387 
SER   OXT  O  N N 388 
SER   H    H  N N 389 
SER   H2   H  N N 390 
SER   HA   H  N N 391 
SER   HB2  H  N N 392 
SER   HB3  H  N N 393 
SER   HG   H  N N 394 
SER   HXT  H  N N 395 
THR   N    N  N N 396 
THR   CA   C  N S 397 
THR   C    C  N N 398 
THR   O    O  N N 399 
THR   CB   C  N R 400 
THR   OG1  O  N N 401 
THR   CG2  C  N N 402 
THR   OXT  O  N N 403 
THR   H    H  N N 404 
THR   H2   H  N N 405 
THR   HA   H  N N 406 
THR   HB   H  N N 407 
THR   HG1  H  N N 408 
THR   HG21 H  N N 409 
THR   HG22 H  N N 410 
THR   HG23 H  N N 411 
THR   HXT  H  N N 412 
TRP   N    N  N N 413 
TRP   CA   C  N S 414 
TRP   C    C  N N 415 
TRP   O    O  N N 416 
TRP   CB   C  N N 417 
TRP   CG   C  Y N 418 
TRP   CD1  C  Y N 419 
TRP   CD2  C  Y N 420 
TRP   NE1  N  Y N 421 
TRP   CE2  C  Y N 422 
TRP   CE3  C  Y N 423 
TRP   CZ2  C  Y N 424 
TRP   CZ3  C  Y N 425 
TRP   CH2  C  Y N 426 
TRP   OXT  O  N N 427 
TRP   H    H  N N 428 
TRP   H2   H  N N 429 
TRP   HA   H  N N 430 
TRP   HB2  H  N N 431 
TRP   HB3  H  N N 432 
TRP   HD1  H  N N 433 
TRP   HE1  H  N N 434 
TRP   HE3  H  N N 435 
TRP   HZ2  H  N N 436 
TRP   HZ3  H  N N 437 
TRP   HH2  H  N N 438 
TRP   HXT  H  N N 439 
TYR   N    N  N N 440 
TYR   CA   C  N S 441 
TYR   C    C  N N 442 
TYR   O    O  N N 443 
TYR   CB   C  N N 444 
TYR   CG   C  Y N 445 
TYR   CD1  C  Y N 446 
TYR   CD2  C  Y N 447 
TYR   CE1  C  Y N 448 
TYR   CE2  C  Y N 449 
TYR   CZ   C  Y N 450 
TYR   OH   O  N N 451 
TYR   OXT  O  N N 452 
TYR   H    H  N N 453 
TYR   H2   H  N N 454 
TYR   HA   H  N N 455 
TYR   HB2  H  N N 456 
TYR   HB3  H  N N 457 
TYR   HD1  H  N N 458 
TYR   HD2  H  N N 459 
TYR   HE1  H  N N 460 
TYR   HE2  H  N N 461 
TYR   HH   H  N N 462 
TYR   HXT  H  N N 463 
VAL   N    N  N N 464 
VAL   CA   C  N S 465 
VAL   C    C  N N 466 
VAL   O    O  N N 467 
VAL   CB   C  N N 468 
VAL   CG1  C  N N 469 
VAL   CG2  C  N N 470 
VAL   OXT  O  N N 471 
VAL   H    H  N N 472 
VAL   H2   H  N N 473 
VAL   HA   H  N N 474 
VAL   HB   H  N N 475 
VAL   HG11 H  N N 476 
VAL   HG12 H  N N 477 
VAL   HG13 H  N N 478 
VAL   HG21 H  N N 479 
VAL   HG22 H  N N 480 
VAL   HG23 H  N N 481 
VAL   HXT  H  N N 482 
# 
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 
A1LV3 C29  C30  doub Y N 1   
A1LV3 C29  C28  sing Y N 2   
A1LV3 CL14 C03  sing N N 3   
A1LV3 C30  C25  sing Y N 4   
A1LV3 O48  C45  sing N N 5   
A1LV3 C28  C27  doub Y N 6   
A1LV3 O17  C02  sing N N 7   
A1LV3 O17  C24  sing N N 8   
A1LV3 C03  C02  doub Y N 9   
A1LV3 C03  C04  sing Y N 10  
A1LV3 C02  C01  sing Y N 11  
A1LV3 C46  C45  sing N N 12  
A1LV3 C46  C47  sing N N 13  
A1LV3 C04  C05  doub Y N 14  
A1LV3 C43  N42  sing N N 15  
A1LV3 C43  C44  sing N N 16  
A1LV3 C25  C24  sing N N 17  
A1LV3 C25  C26  doub Y N 18  
A1LV3 C45  C44  sing N N 19  
A1LV3 N42  C47  sing N N 20  
A1LV3 N42  C41  sing N N 21  
A1LV3 C01  C06  doub Y N 22  
A1LV3 C27  C26  sing Y N 23  
A1LV3 C27  C31  sing N N 24  
A1LV3 C05  C06  sing Y N 25  
A1LV3 C05  C15  sing N N 26  
A1LV3 C52  C08  sing N N 27  
A1LV3 C52  O07  sing N N 28  
A1LV3 C06  O07  sing N N 29  
A1LV3 C15  N16  sing N N 30  
A1LV3 C37  C31  doub Y N 31  
A1LV3 C37  C36  sing Y N 32  
A1LV3 C26  F32  sing N N 33  
A1LV3 C40  C41  sing N N 34  
A1LV3 C40  C39  sing N N 35  
A1LV3 O22  C21  doub N N 36  
A1LV3 C09  C08  doub Y N 37  
A1LV3 C09  C10  sing Y N 38  
A1LV3 O38  C36  sing N N 39  
A1LV3 O38  C39  sing N N 40  
A1LV3 C31  C33  sing Y N 41  
A1LV3 C08  C13  sing Y N 42  
A1LV3 C36  C35  doub Y N 43  
A1LV3 N16  C18  sing N N 44  
A1LV3 C21  O23  sing N N 45  
A1LV3 C21  C18  sing N N 46  
A1LV3 C10  N50  doub Y N 47  
A1LV3 C10  C11  sing Y N 48  
A1LV3 C13  C12  doub Y N 49  
A1LV3 N50  O51  sing Y N 50  
A1LV3 C18  C19  sing N N 51  
A1LV3 C33  C34  doub Y N 52  
A1LV3 C11  C12  sing Y N 53  
A1LV3 C11  N49  doub Y N 54  
A1LV3 O51  N49  sing Y N 55  
A1LV3 C35  C34  sing Y N 56  
A1LV3 C19  O20  sing N N 57  
A1LV3 C13  H131 sing N N 58  
A1LV3 C15  H152 sing N N 59  
A1LV3 C15  H151 sing N N 60  
A1LV3 C24  H242 sing N N 61  
A1LV3 C24  H241 sing N N 62  
A1LV3 C28  H281 sing N N 63  
A1LV3 C01  H011 sing N N 64  
A1LV3 C04  H041 sing N N 65  
A1LV3 C09  H091 sing N N 66  
A1LV3 C12  H121 sing N N 67  
A1LV3 C18  H181 sing N N 68  
A1LV3 C19  H191 sing N N 69  
A1LV3 C19  H192 sing N N 70  
A1LV3 C29  H291 sing N N 71  
A1LV3 C30  H301 sing N N 72  
A1LV3 C33  H331 sing N N 73  
A1LV3 C34  H341 sing N N 74  
A1LV3 C35  H351 sing N N 75  
A1LV3 C37  H371 sing N N 76  
A1LV3 C39  H391 sing N N 77  
A1LV3 C39  H392 sing N N 78  
A1LV3 C40  H401 sing N N 79  
A1LV3 C40  H402 sing N N 80  
A1LV3 C41  H411 sing N N 81  
A1LV3 C41  H412 sing N N 82  
A1LV3 C43  H431 sing N N 83  
A1LV3 C43  H432 sing N N 84  
A1LV3 C44  H441 sing N N 85  
A1LV3 C44  H442 sing N N 86  
A1LV3 C45  H451 sing N N 87  
A1LV3 C46  H462 sing N N 88  
A1LV3 C46  H461 sing N N 89  
A1LV3 C47  H472 sing N N 90  
A1LV3 C47  H471 sing N N 91  
A1LV3 C52  H521 sing N N 92  
A1LV3 C52  H522 sing N N 93  
A1LV3 N16  H1   sing N N 94  
A1LV3 O20  H201 sing N N 95  
A1LV3 O23  H3   sing N N 96  
A1LV3 O48  H481 sing N N 97  
ALA   N    CA   sing N N 98  
ALA   N    H    sing N N 99  
ALA   N    H2   sing N N 100 
ALA   CA   C    sing N N 101 
ALA   CA   CB   sing N N 102 
ALA   CA   HA   sing N N 103 
ALA   C    O    doub N N 104 
ALA   C    OXT  sing N N 105 
ALA   CB   HB1  sing N N 106 
ALA   CB   HB2  sing N N 107 
ALA   CB   HB3  sing N N 108 
ALA   OXT  HXT  sing N N 109 
ARG   N    CA   sing N N 110 
ARG   N    H    sing N N 111 
ARG   N    H2   sing N N 112 
ARG   CA   C    sing N N 113 
ARG   CA   CB   sing N N 114 
ARG   CA   HA   sing N N 115 
ARG   C    O    doub N N 116 
ARG   C    OXT  sing N N 117 
ARG   CB   CG   sing N N 118 
ARG   CB   HB2  sing N N 119 
ARG   CB   HB3  sing N N 120 
ARG   CG   CD   sing N N 121 
ARG   CG   HG2  sing N N 122 
ARG   CG   HG3  sing N N 123 
ARG   CD   NE   sing N N 124 
ARG   CD   HD2  sing N N 125 
ARG   CD   HD3  sing N N 126 
ARG   NE   CZ   sing N N 127 
ARG   NE   HE   sing N N 128 
ARG   CZ   NH1  sing N N 129 
ARG   CZ   NH2  doub N N 130 
ARG   NH1  HH11 sing N N 131 
ARG   NH1  HH12 sing N N 132 
ARG   NH2  HH21 sing N N 133 
ARG   NH2  HH22 sing N N 134 
ARG   OXT  HXT  sing N N 135 
ASN   N    CA   sing N N 136 
ASN   N    H    sing N N 137 
ASN   N    H2   sing N N 138 
ASN   CA   C    sing N N 139 
ASN   CA   CB   sing N N 140 
ASN   CA   HA   sing N N 141 
ASN   C    O    doub N N 142 
ASN   C    OXT  sing N N 143 
ASN   CB   CG   sing N N 144 
ASN   CB   HB2  sing N N 145 
ASN   CB   HB3  sing N N 146 
ASN   CG   OD1  doub N N 147 
ASN   CG   ND2  sing N N 148 
ASN   ND2  HD21 sing N N 149 
ASN   ND2  HD22 sing N N 150 
ASN   OXT  HXT  sing N N 151 
ASP   N    CA   sing N N 152 
ASP   N    H    sing N N 153 
ASP   N    H2   sing N N 154 
ASP   CA   C    sing N N 155 
ASP   CA   CB   sing N N 156 
ASP   CA   HA   sing N N 157 
ASP   C    O    doub N N 158 
ASP   C    OXT  sing N N 159 
ASP   CB   CG   sing N N 160 
ASP   CB   HB2  sing N N 161 
ASP   CB   HB3  sing N N 162 
ASP   CG   OD1  doub N N 163 
ASP   CG   OD2  sing N N 164 
ASP   OD2  HD2  sing N N 165 
ASP   OXT  HXT  sing N N 166 
CYS   N    CA   sing N N 167 
CYS   N    H    sing N N 168 
CYS   N    H2   sing N N 169 
CYS   CA   C    sing N N 170 
CYS   CA   CB   sing N N 171 
CYS   CA   HA   sing N N 172 
CYS   C    O    doub N N 173 
CYS   C    OXT  sing N N 174 
CYS   CB   SG   sing N N 175 
CYS   CB   HB2  sing N N 176 
CYS   CB   HB3  sing N N 177 
CYS   SG   HG   sing N N 178 
CYS   OXT  HXT  sing N N 179 
GLN   N    CA   sing N N 180 
GLN   N    H    sing N N 181 
GLN   N    H2   sing N N 182 
GLN   CA   C    sing N N 183 
GLN   CA   CB   sing N N 184 
GLN   CA   HA   sing N N 185 
GLN   C    O    doub N N 186 
GLN   C    OXT  sing N N 187 
GLN   CB   CG   sing N N 188 
GLN   CB   HB2  sing N N 189 
GLN   CB   HB3  sing N N 190 
GLN   CG   CD   sing N N 191 
GLN   CG   HG2  sing N N 192 
GLN   CG   HG3  sing N N 193 
GLN   CD   OE1  doub N N 194 
GLN   CD   NE2  sing N N 195 
GLN   NE2  HE21 sing N N 196 
GLN   NE2  HE22 sing N N 197 
GLN   OXT  HXT  sing N N 198 
GLU   N    CA   sing N N 199 
GLU   N    H    sing N N 200 
GLU   N    H2   sing N N 201 
GLU   CA   C    sing N N 202 
GLU   CA   CB   sing N N 203 
GLU   CA   HA   sing N N 204 
GLU   C    O    doub N N 205 
GLU   C    OXT  sing N N 206 
GLU   CB   CG   sing N N 207 
GLU   CB   HB2  sing N N 208 
GLU   CB   HB3  sing N N 209 
GLU   CG   CD   sing N N 210 
GLU   CG   HG2  sing N N 211 
GLU   CG   HG3  sing N N 212 
GLU   CD   OE1  doub N N 213 
GLU   CD   OE2  sing N N 214 
GLU   OE2  HE2  sing N N 215 
GLU   OXT  HXT  sing N N 216 
GLY   N    CA   sing N N 217 
GLY   N    H    sing N N 218 
GLY   N    H2   sing N N 219 
GLY   CA   C    sing N N 220 
GLY   CA   HA2  sing N N 221 
GLY   CA   HA3  sing N N 222 
GLY   C    O    doub N N 223 
GLY   C    OXT  sing N N 224 
GLY   OXT  HXT  sing N N 225 
HIS   N    CA   sing N N 226 
HIS   N    H    sing N N 227 
HIS   N    H2   sing N N 228 
HIS   CA   C    sing N N 229 
HIS   CA   CB   sing N N 230 
HIS   CA   HA   sing N N 231 
HIS   C    O    doub N N 232 
HIS   C    OXT  sing N N 233 
HIS   CB   CG   sing N N 234 
HIS   CB   HB2  sing N N 235 
HIS   CB   HB3  sing N N 236 
HIS   CG   ND1  sing Y N 237 
HIS   CG   CD2  doub Y N 238 
HIS   ND1  CE1  doub Y N 239 
HIS   ND1  HD1  sing N N 240 
HIS   CD2  NE2  sing Y N 241 
HIS   CD2  HD2  sing N N 242 
HIS   CE1  NE2  sing Y N 243 
HIS   CE1  HE1  sing N N 244 
HIS   NE2  HE2  sing N N 245 
HIS   OXT  HXT  sing N N 246 
HOH   O    H1   sing N N 247 
HOH   O    H2   sing N N 248 
ILE   N    CA   sing N N 249 
ILE   N    H    sing N N 250 
ILE   N    H2   sing N N 251 
ILE   CA   C    sing N N 252 
ILE   CA   CB   sing N N 253 
ILE   CA   HA   sing N N 254 
ILE   C    O    doub N N 255 
ILE   C    OXT  sing N N 256 
ILE   CB   CG1  sing N N 257 
ILE   CB   CG2  sing N N 258 
ILE   CB   HB   sing N N 259 
ILE   CG1  CD1  sing N N 260 
ILE   CG1  HG12 sing N N 261 
ILE   CG1  HG13 sing N N 262 
ILE   CG2  HG21 sing N N 263 
ILE   CG2  HG22 sing N N 264 
ILE   CG2  HG23 sing N N 265 
ILE   CD1  HD11 sing N N 266 
ILE   CD1  HD12 sing N N 267 
ILE   CD1  HD13 sing N N 268 
ILE   OXT  HXT  sing N N 269 
LEU   N    CA   sing N N 270 
LEU   N    H    sing N N 271 
LEU   N    H2   sing N N 272 
LEU   CA   C    sing N N 273 
LEU   CA   CB   sing N N 274 
LEU   CA   HA   sing N N 275 
LEU   C    O    doub N N 276 
LEU   C    OXT  sing N N 277 
LEU   CB   CG   sing N N 278 
LEU   CB   HB2  sing N N 279 
LEU   CB   HB3  sing N N 280 
LEU   CG   CD1  sing N N 281 
LEU   CG   CD2  sing N N 282 
LEU   CG   HG   sing N N 283 
LEU   CD1  HD11 sing N N 284 
LEU   CD1  HD12 sing N N 285 
LEU   CD1  HD13 sing N N 286 
LEU   CD2  HD21 sing N N 287 
LEU   CD2  HD22 sing N N 288 
LEU   CD2  HD23 sing N N 289 
LEU   OXT  HXT  sing N N 290 
LYS   N    CA   sing N N 291 
LYS   N    H    sing N N 292 
LYS   N    H2   sing N N 293 
LYS   CA   C    sing N N 294 
LYS   CA   CB   sing N N 295 
LYS   CA   HA   sing N N 296 
LYS   C    O    doub N N 297 
LYS   C    OXT  sing N N 298 
LYS   CB   CG   sing N N 299 
LYS   CB   HB2  sing N N 300 
LYS   CB   HB3  sing N N 301 
LYS   CG   CD   sing N N 302 
LYS   CG   HG2  sing N N 303 
LYS   CG   HG3  sing N N 304 
LYS   CD   CE   sing N N 305 
LYS   CD   HD2  sing N N 306 
LYS   CD   HD3  sing N N 307 
LYS   CE   NZ   sing N N 308 
LYS   CE   HE2  sing N N 309 
LYS   CE   HE3  sing N N 310 
LYS   NZ   HZ1  sing N N 311 
LYS   NZ   HZ2  sing N N 312 
LYS   NZ   HZ3  sing N N 313 
LYS   OXT  HXT  sing N N 314 
MET   N    CA   sing N N 315 
MET   N    H    sing N N 316 
MET   N    H2   sing N N 317 
MET   CA   C    sing N N 318 
MET   CA   CB   sing N N 319 
MET   CA   HA   sing N N 320 
MET   C    O    doub N N 321 
MET   C    OXT  sing N N 322 
MET   CB   CG   sing N N 323 
MET   CB   HB2  sing N N 324 
MET   CB   HB3  sing N N 325 
MET   CG   SD   sing N N 326 
MET   CG   HG2  sing N N 327 
MET   CG   HG3  sing N N 328 
MET   SD   CE   sing N N 329 
MET   CE   HE1  sing N N 330 
MET   CE   HE2  sing N N 331 
MET   CE   HE3  sing N N 332 
MET   OXT  HXT  sing N N 333 
PHE   N    CA   sing N N 334 
PHE   N    H    sing N N 335 
PHE   N    H2   sing N N 336 
PHE   CA   C    sing N N 337 
PHE   CA   CB   sing N N 338 
PHE   CA   HA   sing N N 339 
PHE   C    O    doub N N 340 
PHE   C    OXT  sing N N 341 
PHE   CB   CG   sing N N 342 
PHE   CB   HB2  sing N N 343 
PHE   CB   HB3  sing N N 344 
PHE   CG   CD1  doub Y N 345 
PHE   CG   CD2  sing Y N 346 
PHE   CD1  CE1  sing Y N 347 
PHE   CD1  HD1  sing N N 348 
PHE   CD2  CE2  doub Y N 349 
PHE   CD2  HD2  sing N N 350 
PHE   CE1  CZ   doub Y N 351 
PHE   CE1  HE1  sing N N 352 
PHE   CE2  CZ   sing Y N 353 
PHE   CE2  HE2  sing N N 354 
PHE   CZ   HZ   sing N N 355 
PHE   OXT  HXT  sing N N 356 
PRO   N    CA   sing N N 357 
PRO   N    CD   sing N N 358 
PRO   N    H    sing N N 359 
PRO   CA   C    sing N N 360 
PRO   CA   CB   sing N N 361 
PRO   CA   HA   sing N N 362 
PRO   C    O    doub N N 363 
PRO   C    OXT  sing N N 364 
PRO   CB   CG   sing N N 365 
PRO   CB   HB2  sing N N 366 
PRO   CB   HB3  sing N N 367 
PRO   CG   CD   sing N N 368 
PRO   CG   HG2  sing N N 369 
PRO   CG   HG3  sing N N 370 
PRO   CD   HD2  sing N N 371 
PRO   CD   HD3  sing N N 372 
PRO   OXT  HXT  sing N N 373 
SER   N    CA   sing N N 374 
SER   N    H    sing N N 375 
SER   N    H2   sing N N 376 
SER   CA   C    sing N N 377 
SER   CA   CB   sing N N 378 
SER   CA   HA   sing N N 379 
SER   C    O    doub N N 380 
SER   C    OXT  sing N N 381 
SER   CB   OG   sing N N 382 
SER   CB   HB2  sing N N 383 
SER   CB   HB3  sing N N 384 
SER   OG   HG   sing N N 385 
SER   OXT  HXT  sing N N 386 
THR   N    CA   sing N N 387 
THR   N    H    sing N N 388 
THR   N    H2   sing N N 389 
THR   CA   C    sing N N 390 
THR   CA   CB   sing N N 391 
THR   CA   HA   sing N N 392 
THR   C    O    doub N N 393 
THR   C    OXT  sing N N 394 
THR   CB   OG1  sing N N 395 
THR   CB   CG2  sing N N 396 
THR   CB   HB   sing N N 397 
THR   OG1  HG1  sing N N 398 
THR   CG2  HG21 sing N N 399 
THR   CG2  HG22 sing N N 400 
THR   CG2  HG23 sing N N 401 
THR   OXT  HXT  sing N N 402 
TRP   N    CA   sing N N 403 
TRP   N    H    sing N N 404 
TRP   N    H2   sing N N 405 
TRP   CA   C    sing N N 406 
TRP   CA   CB   sing N N 407 
TRP   CA   HA   sing N N 408 
TRP   C    O    doub N N 409 
TRP   C    OXT  sing N N 410 
TRP   CB   CG   sing N N 411 
TRP   CB   HB2  sing N N 412 
TRP   CB   HB3  sing N N 413 
TRP   CG   CD1  doub Y N 414 
TRP   CG   CD2  sing Y N 415 
TRP   CD1  NE1  sing Y N 416 
TRP   CD1  HD1  sing N N 417 
TRP   CD2  CE2  doub Y N 418 
TRP   CD2  CE3  sing Y N 419 
TRP   NE1  CE2  sing Y N 420 
TRP   NE1  HE1  sing N N 421 
TRP   CE2  CZ2  sing Y N 422 
TRP   CE3  CZ3  doub Y N 423 
TRP   CE3  HE3  sing N N 424 
TRP   CZ2  CH2  doub Y N 425 
TRP   CZ2  HZ2  sing N N 426 
TRP   CZ3  CH2  sing Y N 427 
TRP   CZ3  HZ3  sing N N 428 
TRP   CH2  HH2  sing N N 429 
TRP   OXT  HXT  sing N N 430 
TYR   N    CA   sing N N 431 
TYR   N    H    sing N N 432 
TYR   N    H2   sing N N 433 
TYR   CA   C    sing N N 434 
TYR   CA   CB   sing N N 435 
TYR   CA   HA   sing N N 436 
TYR   C    O    doub N N 437 
TYR   C    OXT  sing N N 438 
TYR   CB   CG   sing N N 439 
TYR   CB   HB2  sing N N 440 
TYR   CB   HB3  sing N N 441 
TYR   CG   CD1  doub Y N 442 
TYR   CG   CD2  sing Y N 443 
TYR   CD1  CE1  sing Y N 444 
TYR   CD1  HD1  sing N N 445 
TYR   CD2  CE2  doub Y N 446 
TYR   CD2  HD2  sing N N 447 
TYR   CE1  CZ   doub Y N 448 
TYR   CE1  HE1  sing N N 449 
TYR   CE2  CZ   sing Y N 450 
TYR   CE2  HE2  sing N N 451 
TYR   CZ   OH   sing N N 452 
TYR   OH   HH   sing N N 453 
TYR   OXT  HXT  sing N N 454 
VAL   N    CA   sing N N 455 
VAL   N    H    sing N N 456 
VAL   N    H2   sing N N 457 
VAL   CA   C    sing N N 458 
VAL   CA   CB   sing N N 459 
VAL   CA   HA   sing N N 460 
VAL   C    O    doub N N 461 
VAL   C    OXT  sing N N 462 
VAL   CB   CG1  sing N N 463 
VAL   CB   CG2  sing N N 464 
VAL   CB   HB   sing N N 465 
VAL   CG1  HG11 sing N N 466 
VAL   CG1  HG12 sing N N 467 
VAL   CG1  HG13 sing N N 468 
VAL   CG2  HG21 sing N N 469 
VAL   CG2  HG22 sing N N 470 
VAL   CG2  HG23 sing N N 471 
VAL   OXT  HXT  sing N N 472 
# 
_pdbx_audit_support.funding_organization   'National Natural Science Foundation of China (NSFC)' 
_pdbx_audit_support.country                China 
_pdbx_audit_support.grant_number           82204216 
_pdbx_audit_support.ordinal                1 
# 
_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   4Z18 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8XR5 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.009160 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020371 
_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]   0.019287 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
F  
H  
N  
O  
S  
# 
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    . PHE   A 1 1   ? -31.377 11.499  3.115   1.00 55.32  ?  1   PHE   A N    1 
ATOM   2    C  CA   . PHE   A 1 1   ? -30.283 12.024  2.303   1.00 63.68  ?  1   PHE   A CA   1 
ATOM   3    C  C    . PHE   A 1 1   ? -29.154 11.016  2.121   1.00 54.96  ?  1   PHE   A C    1 
ATOM   4    O  O    . PHE   A 1 1   ? -28.609 10.497  3.095   1.00 58.43  ?  1   PHE   A O    1 
ATOM   5    C  CB   . PHE   A 1 1   ? -29.715 13.299  2.919   1.00 62.67  ?  1   PHE   A CB   1 
ATOM   6    C  CG   . PHE   A 1 1   ? -28.667 13.951  2.070   1.00 51.31  ?  1   PHE   A CG   1 
ATOM   7    C  CD1  . PHE   A 1 1   ? -29.008 14.578  0.885   1.00 52.04  ?  1   PHE   A CD1  1 
ATOM   8    C  CD2  . PHE   A 1 1   ? -27.333 13.903  2.438   1.00 53.01  ?  1   PHE   A CD2  1 
ATOM   9    C  CE1  . PHE   A 1 1   ? -28.042 15.169  0.095   1.00 50.45  ?  1   PHE   A CE1  1 
ATOM   10   C  CE2  . PHE   A 1 1   ? -26.362 14.489  1.652   1.00 50.85  ?  1   PHE   A CE2  1 
ATOM   11   C  CZ   . PHE   A 1 1   ? -26.716 15.123  0.479   1.00 46.56  ?  1   PHE   A CZ   1 
ATOM   12   N  N    . THR   A 1 2   ? -28.800 10.747  0.867   1.00 44.09  ?  2   THR   A N    1 
ATOM   13   C  CA   . THR   A 1 2   ? -27.805 9.730   0.558   1.00 45.06  ?  2   THR   A CA   1 
ATOM   14   C  C    . THR   A 1 2   ? -26.862 10.210  -0.534  1.00 44.78  ?  2   THR   A C    1 
ATOM   15   O  O    . THR   A 1 2   ? -27.310 10.686  -1.582  1.00 41.18  ?  2   THR   A O    1 
ATOM   16   C  CB   . THR   A 1 2   ? -28.475 8.424   0.127   1.00 56.42  ?  2   THR   A CB   1 
ATOM   17   O  OG1  . THR   A 1 2   ? -29.605 8.168   0.971   1.00 70.73  ?  2   THR   A OG1  1 
ATOM   18   C  CG2  . THR   A 1 2   ? -27.498 7.282   0.236   1.00 57.54  ?  2   THR   A CG2  1 
ATOM   19   N  N    . VAL   A 1 3   ? -25.562 10.085  -0.282  1.00 51.73  ?  3   VAL   A N    1 
ATOM   20   C  CA   . VAL   A 1 3   ? -24.538 10.228  -1.310  1.00 48.07  ?  3   VAL   A CA   1 
ATOM   21   C  C    . VAL   A 1 3   ? -24.211 8.848   -1.858  1.00 43.75  ?  3   VAL   A C    1 
ATOM   22   O  O    . VAL   A 1 3   ? -24.066 7.883   -1.099  1.00 37.54  ?  3   VAL   A O    1 
ATOM   23   C  CB   . VAL   A 1 3   ? -23.281 10.918  -0.749  1.00 43.16  ?  3   VAL   A CB   1 
ATOM   24   C  CG1  . VAL   A 1 3   ? -22.153 10.876  -1.771  1.00 47.70  ?  3   VAL   A CG1  1 
ATOM   25   C  CG2  . VAL   A 1 3   ? -23.598 12.351  -0.360  1.00 44.50  ?  3   VAL   A CG2  1 
ATOM   26   N  N    . THR   A 1 4   ? -24.108 8.746   -3.181  1.00 42.09  ?  4   THR   A N    1 
ATOM   27   C  CA   . THR   A 1 4   ? -23.753 7.503   -3.847  1.00 43.30  ?  4   THR   A CA   1 
ATOM   28   C  C    . THR   A 1 4   ? -22.620 7.761   -4.831  1.00 43.44  ?  4   THR   A C    1 
ATOM   29   O  O    . THR   A 1 4   ? -22.468 8.872   -5.346  1.00 45.24  ?  4   THR   A O    1 
ATOM   30   C  CB   . THR   A 1 4   ? -24.951 6.890   -4.587  1.00 42.47  ?  4   THR   A CB   1 
ATOM   31   O  OG1  . THR   A 1 4   ? -25.659 7.920   -5.286  1.00 48.50  ?  4   THR   A OG1  1 
ATOM   32   C  CG2  . THR   A 1 4   ? -25.896 6.217   -3.601  1.00 55.53  ?  4   THR   A CG2  1 
ATOM   33   N  N    . VAL   A 1 5   ? -21.828 6.728   -5.090  1.00 39.82  ?  5   VAL   A N    1 
ATOM   34   C  CA   . VAL   A 1 5   ? -20.762 6.771   -6.085  1.00 49.35  ?  5   VAL   A CA   1 
ATOM   35   C  C    . VAL   A 1 5   ? -21.091 5.758   -7.162  1.00 45.06  ?  5   VAL   A C    1 
ATOM   36   O  O    . VAL   A 1 5   ? -21.311 4.583   -6.853  1.00 51.02  ?  5   VAL   A O    1 
ATOM   37   C  CB   . VAL   A 1 5   ? -19.373 6.481   -5.482  1.00 44.88  ?  5   VAL   A CB   1 
ATOM   38   C  CG1  . VAL   A 1 5   ? -18.931 7.629   -4.592  1.00 38.57  ?  5   VAL   A CG1  1 
ATOM   39   C  CG2  . VAL   A 1 5   ? -19.380 5.167   -4.716  1.00 56.15  ?  5   VAL   A CG2  1 
ATOM   40   N  N    . PRO   A 1 6   ? -21.144 6.153   -8.439  1.00 51.79  ?  6   PRO   A N    1 
ATOM   41   C  CA   . PRO   A 1 6   ? -21.368 5.151   -9.494  1.00 58.63  ?  6   PRO   A CA   1 
ATOM   42   C  C    . PRO   A 1 6   ? -20.281 4.093   -9.535  1.00 43.76  ?  6   PRO   A C    1 
ATOM   43   O  O    . PRO   A 1 6   ? -20.567 2.927   -9.833  1.00 54.59  ?  6   PRO   A O    1 
ATOM   44   C  CB   . PRO   A 1 6   ? -21.411 5.983   -10.786 1.00 58.30  ?  6   PRO   A CB   1 
ATOM   45   C  CG   . PRO   A 1 6   ? -20.928 7.347   -10.435 1.00 63.37  ?  6   PRO   A CG   1 
ATOM   46   C  CD   . PRO   A 1 6   ? -20.852 7.501   -8.955  1.00 48.64  ?  6   PRO   A CD   1 
ATOM   47   N  N    . LYS   A 1 7   ? -19.033 4.470   -9.270  1.00 43.87  ?  7   LYS   A N    1 
ATOM   48   C  CA   . LYS   A 1 7   ? -17.959 3.498   -9.124  1.00 37.70  ?  7   LYS   A CA   1 
ATOM   49   C  C    . LYS   A 1 7   ? -17.089 3.910   -7.946  1.00 43.18  ?  7   LYS   A C    1 
ATOM   50   O  O    . LYS   A 1 7   ? -16.750 5.088   -7.800  1.00 45.87  ?  7   LYS   A O    1 
ATOM   51   C  CB   . LYS   A 1 7   ? -17.159 3.343   -10.426 1.00 57.30  ?  7   LYS   A CB   1 
ATOM   52   C  CG   . LYS   A 1 7   ? -16.442 4.564   -10.953 1.00 57.75  ?  7   LYS   A CG   1 
ATOM   53   C  CD   . LYS   A 1 7   ? -15.980 4.274   -12.377 1.00 59.03  ?  7   LYS   A CD   1 
ATOM   54   C  CE   . LYS   A 1 7   ? -15.013 3.100   -12.433 1.00 52.59  ?  7   LYS   A CE   1 
ATOM   55   N  NZ   . LYS   A 1 7   ? -13.760 3.432   -13.156 1.00 48.75  ?  7   LYS   A NZ   1 
ATOM   56   N  N    . ASP   A 1 8   ? -16.753 2.940   -7.099  1.00 42.80  ?  8   ASP   A N    1 
ATOM   57   C  CA   . ASP   A 1 8   ? -15.913 3.158   -5.930  1.00 40.18  ?  8   ASP   A CA   1 
ATOM   58   C  C    . ASP   A 1 8   ? -14.467 2.741   -6.159  1.00 45.81  ?  8   ASP   A C    1 
ATOM   59   O  O    . ASP   A 1 8   ? -13.678 2.721   -5.210  1.00 32.31  ?  8   ASP   A O    1 
ATOM   60   C  CB   . ASP   A 1 8   ? -16.497 2.418   -4.723  1.00 47.14  ?  8   ASP   A CB   1 
ATOM   61   C  CG   . ASP   A 1 8   ? -16.371 0.908   -4.843  1.00 51.53  ?  8   ASP   A CG   1 
ATOM   62   O  OD1  . ASP   A 1 8   ? -16.017 0.419   -5.937  1.00 52.37  ?  8   ASP   A OD1  1 
ATOM   63   O  OD2  . ASP   A 1 8   ? -16.635 0.207   -3.844  1.00 74.99  ?  8   ASP   A OD2  1 
ATOM   64   N  N    . LEU   A 1 9   ? -14.107 2.402   -7.395  1.00 38.20  ?  9   LEU   A N    1 
ATOM   65   C  CA   . LEU   A 1 9   ? -12.731 2.097   -7.758  1.00 37.67  ?  9   LEU   A CA   1 
ATOM   66   C  C    . LEU   A 1 9   ? -12.416 2.736   -9.099  1.00 41.67  ?  9   LEU   A C    1 
ATOM   67   O  O    . LEU   A 1 9   ? -13.188 2.598   -10.053 1.00 37.06  ?  9   LEU   A O    1 
ATOM   68   C  CB   . LEU   A 1 9   ? -12.494 0.584   -7.831  1.00 39.82  ?  9   LEU   A CB   1 
ATOM   69   C  CG   . LEU   A 1 9   ? -11.095 0.144   -8.273  1.00 42.53  ?  9   LEU   A CG   1 
ATOM   70   C  CD1  . LEU   A 1 9   ? -10.076 0.331   -7.155  1.00 45.75  ?  9   LEU   A CD1  1 
ATOM   71   C  CD2  . LEU   A 1 9   ? -11.114 -1.300  -8.759  1.00 47.30  ?  9   LEU   A CD2  1 
ATOM   72   N  N    . TYR   A 1 10  ? -11.280 3.426   -9.168  1.00 33.47  ?  10  TYR   A N    1 
ATOM   73   C  CA   . TYR   A 1 10  ? -10.768 3.995   -10.407 1.00 39.88  ?  10  TYR   A CA   1 
ATOM   74   C  C    . TYR   A 1 10  ? -9.337  3.519   -10.587 1.00 38.16  ?  10  TYR   A C    1 
ATOM   75   O  O    . TYR   A 1 10  ? -8.547  3.549   -9.638  1.00 32.25  ?  10  TYR   A O    1 
ATOM   76   C  CB   . TYR   A 1 10  ? -10.808 5.529   -10.398 1.00 41.97  ?  10  TYR   A CB   1 
ATOM   77   C  CG   . TYR   A 1 10  ? -12.190 6.140   -10.454 1.00 40.16  ?  10  TYR   A CG   1 
ATOM   78   C  CD1  . TYR   A 1 10  ? -13.011 6.156   -9.336  1.00 36.22  ?  10  TYR   A CD1  1 
ATOM   79   C  CD2  . TYR   A 1 10  ? -12.662 6.724   -11.623 1.00 34.55  ?  10  TYR   A CD2  1 
ATOM   80   C  CE1  . TYR   A 1 10  ? -14.271 6.723   -9.384  1.00 34.80  ?  10  TYR   A CE1  1 
ATOM   81   C  CE2  . TYR   A 1 10  ? -13.920 7.294   -11.682 1.00 43.53  ?  10  TYR   A CE2  1 
ATOM   82   C  CZ   . TYR   A 1 10  ? -14.720 7.291   -10.559 1.00 48.13  ?  10  TYR   A CZ   1 
ATOM   83   O  OH   . TYR   A 1 10  ? -15.973 7.855   -10.610 1.00 40.40  ?  10  TYR   A OH   1 
ATOM   84   N  N    . VAL   A 1 11  ? -9.008  3.074   -11.795 1.00 32.43  ?  11  VAL   A N    1 
ATOM   85   C  CA   . VAL   A 1 11  ? -7.655  2.667   -12.152 1.00 36.02  ?  11  VAL   A CA   1 
ATOM   86   C  C    . VAL   A 1 11  ? -7.191  3.618   -13.244 1.00 42.48  ?  11  VAL   A C    1 
ATOM   87   O  O    . VAL   A 1 11  ? -7.751  3.625   -14.348 1.00 44.01  ?  11  VAL   A O    1 
ATOM   88   C  CB   . VAL   A 1 11  ? -7.594  1.207   -12.618 1.00 39.37  ?  11  VAL   A CB   1 
ATOM   89   C  CG1  . VAL   A 1 11  ? -6.215  0.881   -13.172 1.00 44.74  ?  11  VAL   A CG1  1 
ATOM   90   C  CG2  . VAL   A 1 11  ? -7.955  0.269   -11.473 1.00 42.20  ?  11  VAL   A CG2  1 
ATOM   91   N  N    . VAL   A 1 12  ? -6.176  4.424   -12.942 1.00 32.07  ?  12  VAL   A N    1 
ATOM   92   C  CA   . VAL   A 1 12  ? -5.772  5.518   -13.813 1.00 32.09  ?  12  VAL   A CA   1 
ATOM   93   C  C    . VAL   A 1 12  ? -4.279  5.440   -14.096 1.00 39.77  ?  12  VAL   A C    1 
ATOM   94   O  O    . VAL   A 1 12  ? -3.494  4.945   -13.281 1.00 36.50  ?  12  VAL   A O    1 
ATOM   95   C  CB   . VAL   A 1 12  ? -6.139  6.883   -13.194 1.00 44.78  ?  12  VAL   A CB   1 
ATOM   96   C  CG1  . VAL   A 1 12  ? -7.581  6.868   -12.723 1.00 44.78  ?  12  VAL   A CG1  1 
ATOM   97   C  CG2  . VAL   A 1 12  ? -5.209  7.200   -12.036 1.00 55.26  ?  12  VAL   A CG2  1 
ATOM   98   N  N    . GLU   A 1 13  ? -3.890  5.952   -15.261 1.00 35.62  ?  13  GLU   A N    1 
ATOM   99   C  CA   . GLU   A 1 13  ? -2.501  5.940   -15.694 1.00 39.77  ?  13  GLU   A CA   1 
ATOM   100  C  C    . GLU   A 1 13  ? -1.799  7.210   -15.234 1.00 38.70  ?  13  GLU   A C    1 
ATOM   101  O  O    . GLU   A 1 13  ? -2.350  8.310   -15.328 1.00 38.82  ?  13  GLU   A O    1 
ATOM   102  C  CB   . GLU   A 1 13  ? -2.406  5.819   -17.218 1.00 33.82  ?  13  GLU   A CB   1 
ATOM   103  C  CG   . GLU   A 1 13  ? -3.172  4.643   -17.812 1.00 43.22  ?  13  GLU   A CG   1 
ATOM   104  C  CD   . GLU   A 1 13  ? -2.739  3.308   -17.238 1.00 45.18  ?  13  GLU   A CD   1 
ATOM   105  O  OE1  . GLU   A 1 13  ? -1.521  3.038   -17.216 1.00 48.97  ?  13  GLU   A OE1  1 
ATOM   106  O  OE2  . GLU   A 1 13  ? -3.617  2.530   -16.807 1.00 43.94  ?  13  GLU   A OE2  1 
ATOM   107  N  N    . TYR   A 1 14  ? -0.584  7.045   -14.719 1.00 42.36  ?  14  TYR   A N    1 
ATOM   108  C  CA   . TYR   A 1 14  ? 0.273   8.182   -14.407 1.00 38.78  ?  14  TYR   A CA   1 
ATOM   109  C  C    . TYR   A 1 14  ? 0.344   9.144   -15.588 1.00 37.94  ?  14  TYR   A C    1 
ATOM   110  O  O    . TYR   A 1 14  ? 0.532   8.730   -16.735 1.00 41.28  ?  14  TYR   A O    1 
ATOM   111  C  CB   . TYR   A 1 14  ? 1.666   7.674   -14.030 1.00 34.28  ?  14  TYR   A CB   1 
ATOM   112  C  CG   . TYR   A 1 14  ? 2.714   8.740   -13.810 1.00 38.53  ?  14  TYR   A CG   1 
ATOM   113  C  CD1  . TYR   A 1 14  ? 3.456   9.241   -14.873 1.00 43.42  ?  14  TYR   A CD1  1 
ATOM   114  C  CD2  . TYR   A 1 14  ? 2.975   9.234   -12.539 1.00 40.35  ?  14  TYR   A CD2  1 
ATOM   115  C  CE1  . TYR   A 1 14  ? 4.423   10.208  -14.676 1.00 45.72  ?  14  TYR   A CE1  1 
ATOM   116  C  CE2  . TYR   A 1 14  ? 3.940   10.202  -12.333 1.00 47.51  ?  14  TYR   A CE2  1 
ATOM   117  C  CZ   . TYR   A 1 14  ? 4.661   10.685  -13.405 1.00 42.84  ?  14  TYR   A CZ   1 
ATOM   118  O  OH   . TYR   A 1 14  ? 5.621   11.650  -13.208 1.00 52.69  ?  14  TYR   A OH   1 
ATOM   119  N  N    . GLY   A 1 15  ? 0.186   10.436  -15.299 1.00 39.41  ?  15  GLY   A N    1 
ATOM   120  C  CA   . GLY   A 1 15  ? 0.254   11.470  -16.308 1.00 39.82  ?  15  GLY   A CA   1 
ATOM   121  C  C    . GLY   A 1 15  ? -1.067  11.818  -16.960 1.00 41.50  ?  15  GLY   A C    1 
ATOM   122  O  O    . GLY   A 1 15  ? -1.154  12.852  -17.635 1.00 43.63  ?  15  GLY   A O    1 
ATOM   123  N  N    . SER   A 1 16  ? -2.095  10.993  -16.784 1.00 45.01  ?  16  SER   A N    1 
ATOM   124  C  CA   . SER   A 1 16  ? -3.399  11.261  -17.365 1.00 40.77  ?  16  SER   A CA   1 
ATOM   125  C  C    . SER   A 1 16  ? -4.216  12.172  -16.449 1.00 50.17  ?  16  SER   A C    1 
ATOM   126  O  O    . SER   A 1 16  ? -3.755  12.625  -15.398 1.00 43.99  ?  16  SER   A O    1 
ATOM   127  C  CB   . SER   A 1 16  ? -4.136  9.952   -17.635 1.00 43.86  ?  16  SER   A CB   1 
ATOM   128  O  OG   . SER   A 1 16  ? -4.697  9.432   -16.443 1.00 51.61  ?  16  SER   A OG   1 
ATOM   129  N  N    . ASN   A 1 17  ? -5.447  12.452  -16.861 1.00 48.48  ?  17  ASN   A N    1 
ATOM   130  C  CA   . ASN   A 1 17  ? -6.410  13.189  -16.059 1.00 48.41  ?  17  ASN   A CA   1 
ATOM   131  C  C    . ASN   A 1 17  ? -7.483  12.230  -15.563 1.00 50.11  ?  17  ASN   A C    1 
ATOM   132  O  O    . ASN   A 1 17  ? -7.834  11.268  -16.251 1.00 48.43  ?  17  ASN   A O    1 
ATOM   133  C  CB   . ASN   A 1 17  ? -7.059  14.313  -16.873 1.00 48.91  ?  17  ASN   A CB   1 
ATOM   134  C  CG   . ASN   A 1 17  ? -6.052  15.327  -17.377 1.00 38.34  ?  17  ASN   A CG   1 
ATOM   135  O  OD1  . ASN   A 1 17  ? -4.990  15.513  -16.786 1.00 47.56  ?  17  ASN   A OD1  1 
ATOM   136  N  ND2  . ASN   A 1 17  ? -6.379  15.982  -18.486 1.00 54.71  ?  17  ASN   A ND2  1 
ATOM   137  N  N    . MET   A 1 18  ? -7.993  12.474  -14.356 1.00 51.95  ?  18  MET   A N    1 
ATOM   138  C  CA   . MET   A 1 18  ? -9.062  11.632  -13.836 1.00 48.26  ?  18  MET   A CA   1 
ATOM   139  C  C    . MET   A 1 18  ? -10.179 12.487  -13.255 1.00 42.31  ?  18  MET   A C    1 
ATOM   140  O  O    . MET   A 1 18  ? -9.931  13.549  -12.678 1.00 44.44  ?  18  MET   A O    1 
ATOM   141  C  CB   . MET   A 1 18  ? -8.552  10.645  -12.774 1.00 43.97  ?  18  MET   A CB   1 
ATOM   142  C  CG   . MET   A 1 18  ? -8.225  11.251  -11.423 1.00 63.34  ?  18  MET   A CG   1 
ATOM   143  S  SD   . MET   A 1 18  ? -8.207  9.967   -10.154 1.00 58.23  ?  18  MET   A SD   1 
ATOM   144  C  CE   . MET   A 1 18  ? -7.718  10.904  -8.710  1.00 59.71  ?  18  MET   A CE   1 
ATOM   145  N  N    . THR   A 1 19  ? -11.413 12.022  -13.430 1.00 41.55  ?  19  THR   A N    1 
ATOM   146  C  CA   . THR   A 1 19  ? -12.592 12.648  -12.844 1.00 43.51  ?  19  THR   A CA   1 
ATOM   147  C  C    . THR   A 1 19  ? -13.332 11.592  -12.034 1.00 46.09  ?  19  THR   A C    1 
ATOM   148  O  O    . THR   A 1 19  ? -13.819 10.605  -12.596 1.00 51.32  ?  19  THR   A O    1 
ATOM   149  C  CB   . THR   A 1 19  ? -13.499 13.247  -13.922 1.00 43.20  ?  19  THR   A CB   1 
ATOM   150  O  OG1  . THR   A 1 19  ? -12.853 14.381  -14.515 1.00 47.97  ?  19  THR   A OG1  1 
ATOM   151  C  CG2  . THR   A 1 19  ? -14.821 13.695  -13.317 1.00 43.93  ?  19  THR   A CG2  1 
ATOM   152  N  N    . ILE   A 1 20  ? -13.400 11.788  -10.720 1.00 42.01  ?  20  ILE   A N    1 
ATOM   153  C  CA   . ILE   A 1 20  ? -14.109 10.881  -9.822  1.00 39.44  ?  20  ILE   A CA   1 
ATOM   154  C  C    . ILE   A 1 20  ? -15.372 11.574  -9.332  1.00 41.46  ?  20  ILE   A C    1 
ATOM   155  O  O    . ILE   A 1 20  ? -15.358 12.770  -9.023  1.00 49.10  ?  20  ILE   A O    1 
ATOM   156  C  CB   . ILE   A 1 20  ? -13.228 10.424  -8.644  1.00 39.55  ?  20  ILE   A CB   1 
ATOM   157  C  CG1  . ILE   A 1 20  ? -12.627 11.624  -7.916  1.00 52.71  ?  20  ILE   A CG1  1 
ATOM   158  C  CG2  . ILE   A 1 20  ? -12.120 9.510   -9.149  1.00 47.05  ?  20  ILE   A CG2  1 
ATOM   159  C  CD1  . ILE   A 1 20  ? -11.704 11.235  -6.779  1.00 59.11  ?  20  ILE   A CD1  1 
ATOM   160  N  N    . GLU   A 1 21  ? -16.462 10.823  -9.259  1.00 46.80  ?  21  GLU   A N    1 
ATOM   161  C  CA   . GLU   A 1 21  ? -17.793 11.399  -9.160  1.00 51.24  ?  21  GLU   A CA   1 
ATOM   162  C  C    . GLU   A 1 21  ? -18.485 10.965  -7.875  1.00 56.35  ?  21  GLU   A C    1 
ATOM   163  O  O    . GLU   A 1 21  ? -18.289 9.846   -7.392  1.00 40.10  ?  21  GLU   A O    1 
ATOM   164  C  CB   . GLU   A 1 21  ? -18.635 10.991  -10.368 1.00 44.80  ?  21  GLU   A CB   1 
ATOM   165  C  CG   . GLU   A 1 21  ? -18.377 11.854  -11.593 1.00 77.73  ?  21  GLU   A CG   1 
ATOM   166  C  CD   . GLU   A 1 21  ? -19.421 11.672  -12.676 1.00 65.00  ?  21  GLU   A CD   1 
ATOM   167  O  OE1  . GLU   A 1 21  ? -19.775 10.511  -12.965 1.00 74.00  ?  21  GLU   A OE1  1 
ATOM   168  O  OE2  . GLU   A 1 21  ? -19.901 12.686  -13.224 1.00 72.21  ?  21  GLU   A OE2  1 
ATOM   169  N  N    . CYS   A 1 22  ? -19.297 11.867  -7.321  1.00 51.38  ?  22  CYS   A N    1 
ATOM   170  C  CA   . CYS   A 1 22  ? -20.222 11.502  -6.257  1.00 42.11  ?  22  CYS   A CA   1 
ATOM   171  C  C    . CYS   A 1 22  ? -21.590 12.095  -6.561  1.00 38.90  ?  22  CYS   A C    1 
ATOM   172  O  O    . CYS   A 1 22  ? -21.693 13.239  -7.014  1.00 50.62  ?  22  CYS   A O    1 
ATOM   173  C  CB   . CYS   A 1 22  ? -19.720 11.988  -4.888  1.00 50.05  ?  22  CYS   A CB   1 
ATOM   174  S  SG   . CYS   A 1 22  ? -18.562 10.844  -4.099  1.00 64.83  ?  22  CYS   A SG   1 
ATOM   175  N  N    . LYS   A 1 23  ? -22.637 11.308  -6.314  1.00 51.82  ?  23  LYS   A N    1 
ATOM   176  C  CA   . LYS   A 1 23  ? -24.007 11.676  -6.649  1.00 46.76  ?  23  LYS   A CA   1 
ATOM   177  C  C    . LYS   A 1 23  ? -24.746 12.065  -5.379  1.00 46.20  ?  23  LYS   A C    1 
ATOM   178  O  O    . LYS   A 1 23  ? -24.606 11.403  -4.346  1.00 48.22  ?  23  LYS   A O    1 
ATOM   179  C  CB   . LYS   A 1 23  ? -24.752 10.509  -7.319  1.00 53.86  ?  23  LYS   A CB   1 
ATOM   180  C  CG   . LYS   A 1 23  ? -24.029 9.857   -8.489  1.00 63.71  ?  23  LYS   A CG   1 
ATOM   181  C  CD   . LYS   A 1 23  ? -23.906 10.837  -9.627  1.00 67.67  ?  23  LYS   A CD   1 
ATOM   182  C  CE   . LYS   A 1 23  ? -24.058 10.220  -11.009 1.00 64.92  ?  23  LYS   A CE   1 
ATOM   183  N  NZ   . LYS   A 1 23  ? -25.002 9.076   -11.047 1.00 75.98  ?  23  LYS   A NZ   1 
ATOM   184  N  N    . PHE   A 1 24  ? -25.545 13.125  -5.456  1.00 48.33  ?  24  PHE   A N    1 
ATOM   185  C  CA   . PHE   A 1 24  ? -26.468 13.467  -4.385  1.00 46.21  ?  24  PHE   A CA   1 
ATOM   186  C  C    . PHE   A 1 24  ? -27.783 13.947  -4.978  1.00 39.08  ?  24  PHE   A C    1 
ATOM   187  O  O    . PHE   A 1 24  ? -27.804 14.510  -6.079  1.00 43.99  ?  24  PHE   A O    1 
ATOM   188  C  CB   . PHE   A 1 24  ? -25.878 14.524  -3.434  1.00 53.81  ?  24  PHE   A CB   1 
ATOM   189  C  CG   . PHE   A 1 24  ? -25.616 15.858  -4.074  1.00 47.97  ?  24  PHE   A CG   1 
ATOM   190  C  CD1  . PHE   A 1 24  ? -24.515 16.038  -4.896  1.00 41.21  ?  24  PHE   A CD1  1 
ATOM   191  C  CD2  . PHE   A 1 24  ? -26.443 16.940  -3.825  1.00 49.81  ?  24  PHE   A CD2  1 
ATOM   192  C  CE1  . PHE   A 1 24  ? -24.258 17.265  -5.476  1.00 45.77  ?  24  PHE   A CE1  1 
ATOM   193  C  CE2  . PHE   A 1 24  ? -26.190 18.172  -4.402  1.00 41.60  ?  24  PHE   A CE2  1 
ATOM   194  C  CZ   . PHE   A 1 24  ? -25.095 18.334  -5.229  1.00 42.44  ?  24  PHE   A CZ   1 
ATOM   195  N  N    . PRO   A 1 25  ? -28.896 13.734  -4.275  1.00 48.44  ?  25  PRO   A N    1 
ATOM   196  C  CA   . PRO   A 1 25  ? -30.205 14.064  -4.851  1.00 47.44  ?  25  PRO   A CA   1 
ATOM   197  C  C    . PRO   A 1 25  ? -30.416 15.570  -4.912  1.00 49.17  ?  25  PRO   A C    1 
ATOM   198  O  O    . PRO   A 1 25  ? -30.181 16.288  -3.939  1.00 48.63  ?  25  PRO   A O    1 
ATOM   199  C  CB   . PRO   A 1 25  ? -31.191 13.390  -3.891  1.00 62.08  ?  25  PRO   A CB   1 
ATOM   200  C  CG   . PRO   A 1 25  ? -30.472 13.420  -2.583  1.00 50.91  ?  25  PRO   A CG   1 
ATOM   201  C  CD   . PRO   A 1 25  ? -29.026 13.151  -2.928  1.00 48.21  ?  25  PRO   A CD   1 
ATOM   202  N  N    . VAL   A 1 26  ? -30.879 16.043  -6.055  1.00 45.46  ?  26  VAL   A N    1 
ATOM   203  C  CA   . VAL   A 1 26  ? -31.161 17.497  -6.201  1.00 55.83  ?  26  VAL   A CA   1 
ATOM   204  C  C    . VAL   A 1 26  ? -32.606 17.636  -6.688  1.00 66.73  ?  26  VAL   A C    1 
ATOM   205  O  O    . VAL   A 1 26  ? -33.009 18.747  -7.051  1.00 78.77  ?  26  VAL   A O    1 
ATOM   206  C  CB   . VAL   A 1 26  ? -30.117 18.141  -7.133  1.00 55.31  ?  26  VAL   A CB   1 
ATOM   207  C  CG1  . VAL   A 1 26  ? -30.392 19.602  -7.429  1.00 58.39  ?  26  VAL   A CG1  1 
ATOM   208  C  CG2  . VAL   A 1 26  ? -28.720 17.993  -6.564  1.00 53.73  ?  26  VAL   A CG2  1 
ATOM   209  N  N    . GLU   A 1 27  ? -33.368 16.545  -6.636  1.00 76.14  ?  27  GLU   A N    1 
ATOM   210  C  CA   . GLU   A 1 27  ? -34.758 16.565  -7.136  1.00 86.82  ?  27  GLU   A CA   1 
ATOM   211  C  C    . GLU   A 1 27  ? -34.359 17.130  -8.489  1.00 86.35  ?  27  GLU   A C    1 
ATOM   212  O  O    . GLU   A 1 27  ? -33.559 16.484  -9.187  1.00 102.63 ?  27  GLU   A O    1 
ATOM   213  C  CB   . GLU   A 1 27  ? -35.625 17.545  -6.354  1.00 85.40  ?  27  GLU   A CB   1 
ATOM   214  C  CG   . GLU   A 1 27  ? -35.743 17.219  -4.880  1.00 90.95  ?  27  GLU   A CG   1 
ATOM   215  C  CD   . GLU   A 1 27  ? -36.158 18.408  -4.032  1.00 93.89  ?  27  GLU   A CD   1 
ATOM   216  O  OE1  . GLU   A 1 27  ? -35.949 19.554  -4.482  1.00 99.60  ?  27  GLU   A OE1  1 
ATOM   217  N  N    . LYS   A 1 28  ? -34.870 18.309  -8.822  1.00 87.91  ?  28  LYS   A N    1 
ATOM   218  C  CA   . LYS   A 1 28  ? -34.698 18.825  -10.195 1.00 72.14  ?  28  LYS   A CA   1 
ATOM   219  C  C    . LYS   A 1 28  ? -34.058 20.206  -10.134 1.00 68.50  ?  28  LYS   A C    1 
ATOM   220  O  O    . LYS   A 1 28  ? -33.844 20.791  -11.207 1.00 68.02  ?  28  LYS   A O    1 
ATOM   221  C  CB   . LYS   A 1 28  ? -36.057 18.915  -10.884 1.00 79.59  ?  28  LYS   A CB   1 
ATOM   222  C  CG   . LYS   A 1 28  ? -36.970 17.712  -10.703 1.00 91.25  ?  28  LYS   A CG   1 
ATOM   223  C  CD   . LYS   A 1 28  ? -37.042 16.838  -11.932 1.00 91.95  ?  28  LYS   A CD   1 
ATOM   224  C  CE   . LYS   A 1 28  ? -38.459 16.633  -12.422 1.00 108.57 ?  28  LYS   A CE   1 
ATOM   225  N  NZ   . LYS   A 1 28  ? -39.435 16.682  -11.309 1.00 119.59 ?  28  LYS   A NZ   1 
ATOM   226  N  N    . GLN   A 1 29  ? -33.758 20.707  -8.932  1.00 63.41  ?  29  GLN   A N    1 
ATOM   227  C  CA   . GLN   A 1 29  ? -33.254 22.075  -8.936  1.00 68.16  ?  29  GLN   A CA   1 
ATOM   228  C  C    . GLN   A 1 29  ? -32.292 22.218  -7.763  1.00 63.29  ?  29  GLN   A C    1 
ATOM   229  O  O    . GLN   A 1 29  ? -32.630 21.831  -6.640  1.00 65.49  ?  29  GLN   A O    1 
ATOM   230  C  CB   . GLN   A 1 29  ? -34.418 23.062  -8.788  1.00 52.75  ?  29  GLN   A CB   1 
ATOM   231  C  CG   . GLN   A 1 29  ? -34.037 24.443  -8.275  1.00 53.39  ?  29  GLN   A CG   1 
ATOM   232  C  CD   . GLN   A 1 29  ? -34.653 25.560  -9.094  1.00 70.19  ?  29  GLN   A CD   1 
ATOM   233  O  OE1  . GLN   A 1 29  ? -35.734 25.404  -9.662  1.00 64.69  ?  29  GLN   A OE1  1 
ATOM   234  N  NE2  . GLN   A 1 29  ? -33.980 26.703  -9.138  1.00 76.77  ?  29  GLN   A NE2  1 
ATOM   235  N  N    . LEU   A 1 30  ? -31.109 22.778  -8.014  1.00 61.22  ?  30  LEU   A N    1 
ATOM   236  C  CA   . LEU   A 1 30  ? -30.107 22.955  -6.966  1.00 59.39  ?  30  LEU   A CA   1 
ATOM   237  C  C    . LEU   A 1 30  ? -30.341 24.211  -6.129  1.00 59.05  ?  30  LEU   A C    1 
ATOM   238  O  O    . LEU   A 1 30  ? -30.655 25.280  -6.660  1.00 66.59  ?  30  LEU   A O    1 
ATOM   239  C  CB   . LEU   A 1 30  ? -28.703 22.988  -7.570  1.00 43.51  ?  30  LEU   A CB   1 
ATOM   240  C  CG   . LEU   A 1 30  ? -27.578 23.182  -6.554  1.00 53.73  ?  30  LEU   A CG   1 
ATOM   241  C  CD1  . LEU   A 1 30  ? -27.605 22.062  -5.528  1.00 47.82  ?  30  LEU   A CD1  1 
ATOM   242  C  CD2  . LEU   A 1 30  ? -26.239 23.212  -7.262  1.00 50.81  ?  30  LEU   A CD2  1 
ATOM   243  N  N    . ASP   A 1 31  ? -30.180 24.075  -4.813  1.00 58.32  ?  31  ASP   A N    1 
ATOM   244  C  CA   . ASP   A 1 31  ? -30.184 25.203  -3.877  1.00 62.07  ?  31  ASP   A CA   1 
ATOM   245  C  C    . ASP   A 1 31  ? -28.739 25.403  -3.418  1.00 62.90  ?  31  ASP   A C    1 
ATOM   246  O  O    . ASP   A 1 31  ? -28.310 24.843  -2.408  1.00 64.62  ?  31  ASP   A O    1 
ATOM   247  C  CB   . ASP   A 1 31  ? -31.121 24.961  -2.692  1.00 64.87  ?  31  ASP   A CB   1 
ATOM   248  C  CG   . ASP   A 1 31  ? -30.998 26.037  -1.619  1.00 75.04  ?  31  ASP   A CG   1 
ATOM   249  O  OD1  . ASP   A 1 31  ? -30.392 27.092  -1.899  1.00 66.30  ?  31  ASP   A OD1  1 
ATOM   250  O  OD2  . ASP   A 1 31  ? -31.508 25.832  -0.496  1.00 77.78  ?  31  ASP   A OD2  1 
ATOM   251  N  N    . LEU   A 1 32  ? -27.992 26.216  -4.171  1.00 63.68  ?  32  LEU   A N    1 
ATOM   252  C  CA   . LEU   A 1 32  ? -26.576 26.425  -3.878  1.00 65.11  ?  32  LEU   A CA   1 
ATOM   253  C  C    . LEU   A 1 32  ? -26.346 26.890  -2.446  1.00 58.58  ?  32  LEU   A C    1 
ATOM   254  O  O    . LEU   A 1 32  ? -25.322 26.554  -1.840  1.00 72.92  ?  32  LEU   A O    1 
ATOM   255  C  CB   . LEU   A 1 32  ? -25.986 27.445  -4.854  1.00 68.40  ?  32  LEU   A CB   1 
ATOM   256  C  CG   . LEU   A 1 32  ? -24.678 27.109  -5.576  1.00 68.67  ?  32  LEU   A CG   1 
ATOM   257  C  CD1  . LEU   A 1 32  ? -24.736 25.737  -6.225  1.00 63.43  ?  32  LEU   A CD1  1 
ATOM   258  C  CD2  . LEU   A 1 32  ? -24.354 28.180  -6.608  1.00 68.06  ?  32  LEU   A CD2  1 
ATOM   259  N  N    . ALA   A 1 33  ? -27.286 27.654  -1.888  1.00 56.13  ?  33  ALA   A N    1 
ATOM   260  C  CA   . ALA   A 1 33  ? -27.097 28.211  -0.552  1.00 65.02  ?  33  ALA   A CA   1 
ATOM   261  C  C    . ALA   A 1 33  ? -26.920 27.116  0.491   1.00 57.73  ?  33  ALA   A C    1 
ATOM   262  O  O    . ALA   A 1 33  ? -26.131 27.265  1.432   1.00 58.74  ?  33  ALA   A O    1 
ATOM   263  C  CB   . ALA   A 1 33  ? -28.285 29.099  -0.188  1.00 73.79  ?  33  ALA   A CB   1 
ATOM   264  N  N    . ALA   A 1 34  ? -27.643 26.011  0.342   1.00 59.75  ?  34  ALA   A N    1 
ATOM   265  C  CA   . ALA   A 1 34  ? -27.662 24.941  1.327   1.00 61.47  ?  34  ALA   A CA   1 
ATOM   266  C  C    . ALA   A 1 34  ? -26.633 23.853  1.048   1.00 66.12  ?  34  ALA   A C    1 
ATOM   267  O  O    . ALA   A 1 34  ? -26.707 22.780  1.655   1.00 72.82  ?  34  ALA   A O    1 
ATOM   268  C  CB   . ALA   A 1 34  ? -29.060 24.322  1.400   1.00 66.30  ?  34  ALA   A CB   1 
ATOM   269  N  N    . LEU   A 1 35  ? -25.682 24.099  0.150   1.00 52.28  ?  35  LEU   A N    1 
ATOM   270  C  CA   . LEU   A 1 35  ? -24.755 23.077  -0.316  1.00 44.14  ?  35  LEU   A CA   1 
ATOM   271  C  C    . LEU   A 1 35  ? -23.346 23.329  0.199   1.00 52.72  ?  35  LEU   A C    1 
ATOM   272  O  O    . LEU   A 1 35  ? -22.823 24.443  0.086   1.00 51.37  ?  35  LEU   A O    1 
ATOM   273  C  CB   . LEU   A 1 35  ? -24.729 23.013  -1.843  1.00 48.90  ?  35  LEU   A CB   1 
ATOM   274  C  CG   . LEU   A 1 35  ? -23.717 22.012  -2.406  1.00 43.62  ?  35  LEU   A CG   1 
ATOM   275  C  CD1  . LEU   A 1 35  ? -24.064 20.590  -1.993  1.00 42.38  ?  35  LEU   A CD1  1 
ATOM   276  C  CD2  . LEU   A 1 35  ? -23.616 22.132  -3.920  1.00 44.28  ?  35  LEU   A CD2  1 
ATOM   277  N  N    . ILE   A 1 36  ? -22.744 22.289  0.769   1.00 44.28  ?  36  ILE   A N    1 
ATOM   278  C  CA   . ILE   A 1 36  ? -21.313 22.233  1.026   1.00 40.57  ?  36  ILE   A CA   1 
ATOM   279  C  C    . ILE   A 1 36  ? -20.783 20.937  0.433   1.00 40.46  ?  36  ILE   A C    1 
ATOM   280  O  O    . ILE   A 1 36  ? -21.304 19.855  0.732   1.00 42.89  ?  36  ILE   A O    1 
ATOM   281  C  CB   . ILE   A 1 36  ? -20.979 22.311  2.526   1.00 50.05  ?  36  ILE   A CB   1 
ATOM   282  C  CG1  . ILE   A 1 36  ? -21.532 23.599  3.140   1.00 50.96  ?  36  ILE   A CG1  1 
ATOM   283  C  CG2  . ILE   A 1 36  ? -19.489 22.214  2.718   1.00 57.28  ?  36  ILE   A CG2  1 
ATOM   284  C  CD1  . ILE   A 1 36  ? -21.287 23.716  4.632   1.00 51.30  ?  36  ILE   A CD1  1 
ATOM   285  N  N    . VAL   A 1 37  ? -19.745 21.046  -0.391  1.00 41.14  ?  37  VAL   A N    1 
ATOM   286  C  CA   . VAL   A 1 37  ? -19.073 19.890  -0.978  1.00 36.84  ?  37  VAL   A CA   1 
ATOM   287  C  C    . VAL   A 1 37  ? -17.616 19.916  -0.548  1.00 45.22  ?  37  VAL   A C    1 
ATOM   288  O  O    . VAL   A 1 37  ? -16.931 20.930  -0.717  1.00 46.35  ?  37  VAL   A O    1 
ATOM   289  C  CB   . VAL   A 1 37  ? -19.183 19.881  -2.514  1.00 44.37  ?  37  VAL   A CB   1 
ATOM   290  C  CG1  . VAL   A 1 37  ? -18.292 18.794  -3.097  1.00 40.53  ?  37  VAL   A CG1  1 
ATOM   291  C  CG2  . VAL   A 1 37  ? -20.627 19.680  -2.945  1.00 38.23  ?  37  VAL   A CG2  1 
ATOM   292  N  N    . TYR   A 1 38  ? -17.128 18.797  -0.023  1.00 41.05  ?  38  TYR   A N    1 
ATOM   293  C  CA   . TYR   A 1 38  ? -15.770 18.743  0.494   1.00 37.63  ?  38  TYR   A CA   1 
ATOM   294  C  C    . TYR   A 1 38  ? -15.111 17.451  0.035   1.00 39.18  ?  38  TYR   A C    1 
ATOM   295  O  O    . TYR   A 1 38  ? -15.610 16.360  0.318   1.00 40.56  ?  38  TYR   A O    1 
ATOM   296  C  CB   . TYR   A 1 38  ? -15.765 18.850  2.022   1.00 44.37  ?  38  TYR   A CB   1 
ATOM   297  C  CG   . TYR   A 1 38  ? -14.376 18.877  2.589   1.00 39.24  ?  38  TYR   A CG   1 
ATOM   298  C  CD1  . TYR   A 1 38  ? -13.661 20.064  2.658   1.00 50.48  ?  38  TYR   A CD1  1 
ATOM   299  C  CD2  . TYR   A 1 38  ? -13.765 17.714  3.027   1.00 43.14  ?  38  TYR   A CD2  1 
ATOM   300  C  CE1  . TYR   A 1 38  ? -12.383 20.092  3.158   1.00 63.17  ?  38  TYR   A CE1  1 
ATOM   301  C  CE2  . TYR   A 1 38  ? -12.487 17.732  3.531   1.00 46.51  ?  38  TYR   A CE2  1 
ATOM   302  C  CZ   . TYR   A 1 38  ? -11.799 18.921  3.589   1.00 53.86  ?  38  TYR   A CZ   1 
ATOM   303  O  OH   . TYR   A 1 38  ? -10.520 18.939  4.091   1.00 54.04  ?  38  TYR   A OH   1 
ATOM   304  N  N    . TRP   A 1 39  ? -13.984 17.578  -0.654  1.00 39.15  ?  39  TRP   A N    1 
ATOM   305  C  CA   . TRP   A 1 39  ? -13.185 16.446  -1.104  1.00 38.20  ?  39  TRP   A CA   1 
ATOM   306  C  C    . TRP   A 1 39  ? -11.876 16.410  -0.338  1.00 42.29  ?  39  TRP   A C    1 
ATOM   307  O  O    . TRP   A 1 39  ? -11.162 17.424  -0.289  1.00 43.15  ?  39  TRP   A O    1 
ATOM   308  C  CB   . TRP   A 1 39  ? -12.873 16.535  -2.598  1.00 37.11  ?  39  TRP   A CB   1 
ATOM   309  C  CG   . TRP   A 1 39  ? -13.968 16.138  -3.520  1.00 41.35  ?  39  TRP   A CG   1 
ATOM   310  C  CD1  . TRP   A 1 39  ? -14.840 16.964  -4.164  1.00 42.81  ?  39  TRP   A CD1  1 
ATOM   311  C  CD2  . TRP   A 1 39  ? -14.271 14.810  -3.960  1.00 38.18  ?  39  TRP   A CD2  1 
ATOM   312  N  NE1  . TRP   A 1 39  ? -15.689 16.229  -4.956  1.00 43.68  ?  39  TRP   A NE1  1 
ATOM   313  C  CE2  . TRP   A 1 39  ? -15.358 14.903  -4.850  1.00 43.41  ?  39  TRP   A CE2  1 
ATOM   314  C  CE3  . TRP   A 1 39  ? -13.736 13.549  -3.678  1.00 41.44  ?  39  TRP   A CE3  1 
ATOM   315  C  CZ2  . TRP   A 1 39  ? -15.920 13.784  -5.460  1.00 42.31  ?  39  TRP   A CZ2  1 
ATOM   316  C  CZ3  . TRP   A 1 39  ? -14.296 12.439  -4.283  1.00 42.87  ?  39  TRP   A CZ3  1 
ATOM   317  C  CH2  . TRP   A 1 39  ? -15.377 12.564  -5.164  1.00 43.61  ?  39  TRP   A CH2  1 
ATOM   318  N  N    . GLU   A 1 40  ? -11.545 15.234  0.207   1.00 38.45  ?  40  GLU   A N    1 
ATOM   319  C  CA   . GLU   A 1 40  ? -10.276 15.036  0.899   1.00 39.78  ?  40  GLU   A CA   1 
ATOM   320  C  C    . GLU   A 1 40  ? -9.712  13.660  0.563   1.00 37.84  ?  40  GLU   A C    1 
ATOM   321  O  O    . GLU   A 1 40  ? -10.439 12.750  0.169   1.00 44.43  ?  40  GLU   A O    1 
ATOM   322  C  CB   . GLU   A 1 40  ? -10.437 15.203  2.421   1.00 39.13  ?  40  GLU   A CB   1 
ATOM   323  C  CG   . GLU   A 1 40  ? -11.334 14.169  3.101   1.00 56.15  ?  40  GLU   A CG   1 
ATOM   324  C  CD   . GLU   A 1 40  ? -10.578 12.936  3.559   1.00 48.12  ?  40  GLU   A CD   1 
ATOM   325  O  OE1  . GLU   A 1 40  ? -9.332  12.977  3.581   1.00 60.20  ?  40  GLU   A OE1  1 
ATOM   326  O  OE2  . GLU   A 1 40  ? -11.232 11.929  3.904   1.00 59.00  ?  40  GLU   A OE2  1 
ATOM   327  N  N    . MET   A 1 41  ? -8.391  13.525  0.677   1.00 40.58  ?  41  MET   A N    1 
ATOM   328  C  CA   . MET   A 1 41  ? -7.736  12.226  0.557   1.00 42.32  ?  41  MET   A CA   1 
ATOM   329  C  C    . MET   A 1 41  ? -6.674  12.137  1.641   1.00 52.26  ?  41  MET   A C    1 
ATOM   330  O  O    . MET   A 1 41  ? -5.894  13.076  1.830   1.00 38.62  ?  41  MET   A O    1 
ATOM   331  C  CB   . MET   A 1 41  ? -7.147  12.004  -0.849  1.00 39.45  ?  41  MET   A CB   1 
ATOM   332  C  CG   . MET   A 1 41  ? -5.692  12.410  -1.054  1.00 58.72  ?  41  MET   A CG   1 
ATOM   333  S  SD   . MET   A 1 41  ? -4.506  11.053  -0.895  1.00 64.50  ?  41  MET   A SD   1 
ATOM   334  C  CE   . MET   A 1 41  ? -4.862  10.078  -2.362  1.00 57.51  ?  41  MET   A CE   1 
ATOM   335  N  N    . GLU   A 1 42  ? -6.647  11.005  2.346   1.00 52.66  ?  42  GLU   A N    1 
ATOM   336  C  CA   . GLU   A 1 42  ? -5.886  10.919  3.583   1.00 63.09  ?  42  GLU   A CA   1 
ATOM   337  C  C    . GLU   A 1 42  ? -6.477  11.991  4.496   1.00 68.57  ?  42  GLU   A C    1 
ATOM   338  O  O    . GLU   A 1 42  ? -7.611  11.806  4.946   1.00 77.44  ?  42  GLU   A O    1 
ATOM   339  C  CB   . GLU   A 1 42  ? -4.387  10.973  3.270   1.00 63.84  ?  42  GLU   A CB   1 
ATOM   340  C  CG   . GLU   A 1 42  ? -4.018  9.578   2.701   1.00 62.79  ?  42  GLU   A CG   1 
ATOM   341  C  CD   . GLU   A 1 42  ? -2.773  9.490   1.836   1.00 77.45  ?  42  GLU   A CD   1 
ATOM   342  O  OE1  . GLU   A 1 42  ? -2.016  10.474  1.722   1.00 65.73  ?  42  GLU   A OE1  1 
ATOM   343  O  OE2  . GLU   A 1 42  ? -2.571  8.405   1.245   1.00 72.05  ?  42  GLU   A OE2  1 
ATOM   344  N  N    . ASP   A 1 43  ? -5.798  13.084  4.817   1.00 61.30  ?  43  ASP   A N    1 
ATOM   345  C  CA   . ASP   A 1 43  ? -6.551  14.179  5.436   1.00 73.27  ?  43  ASP   A CA   1 
ATOM   346  C  C    . ASP   A 1 43  ? -6.110  15.523  4.869   1.00 67.77  ?  43  ASP   A C    1 
ATOM   347  O  O    . ASP   A 1 43  ? -5.947  16.511  5.587   1.00 74.50  ?  43  ASP   A O    1 
ATOM   348  C  CB   . ASP   A 1 43  ? -6.461  14.120  6.959   1.00 52.19  ?  43  ASP   A CB   1 
ATOM   349  C  CG   . ASP   A 1 43  ? -7.396  13.071  7.546   1.00 58.54  ?  43  ASP   A CG   1 
ATOM   350  O  OD1  . ASP   A 1 43  ? -8.614  13.339  7.649   1.00 54.74  ?  43  ASP   A OD1  1 
ATOM   351  O  OD2  . ASP   A 1 43  ? -6.913  11.976  7.898   1.00 56.54  ?  43  ASP   A OD2  1 
ATOM   352  N  N    . LYS   A 1 44  ? -5.992  15.580  3.547   1.00 54.23  ?  44  LYS   A N    1 
ATOM   353  C  CA   . LYS   A 1 44  ? -5.605  16.785  2.830   1.00 52.30  ?  44  LYS   A CA   1 
ATOM   354  C  C    . LYS   A 1 44  ? -6.841  17.414  2.208   1.00 51.00  ?  44  LYS   A C    1 
ATOM   355  O  O    . LYS   A 1 44  ? -7.645  16.722  1.573   1.00 45.76  ?  44  LYS   A O    1 
ATOM   356  C  CB   . LYS   A 1 44  ? -4.581  16.478  1.736   1.00 47.95  ?  44  LYS   A CB   1 
ATOM   357  C  CG   . LYS   A 1 44  ? -3.467  15.530  2.136   1.00 53.42  ?  44  LYS   A CG   1 
ATOM   358  C  CD   . LYS   A 1 44  ? -2.858  14.894  0.893   1.00 50.48  ?  44  LYS   A CD   1 
ATOM   359  C  CE   . LYS   A 1 44  ? -1.390  15.247  0.732   1.00 61.13  ?  44  LYS   A CE   1 
ATOM   360  N  NZ   . LYS   A 1 44  ? -0.527  14.540  1.715   1.00 72.44  ?  44  LYS   A NZ   1 
ATOM   361  N  N    . ASN   A 1 45  ? -6.990  18.721  2.393   1.00 42.83  ?  45  ASN   A N    1 
ATOM   362  C  CA   . ASN   A 1 45  ? -8.081  19.457  1.770   1.00 43.86  ?  45  ASN   A CA   1 
ATOM   363  C  C    . ASN   A 1 45  ? -7.846  19.525  0.265   1.00 44.11  ?  45  ASN   A C    1 
ATOM   364  O  O    . ASN   A 1 45  ? -6.935  20.220  -0.197  1.00 44.25  ?  45  ASN   A O    1 
ATOM   365  C  CB   . ASN   A 1 45  ? -8.154  20.853  2.385   1.00 49.41  ?  45  ASN   A CB   1 
ATOM   366  C  CG   . ASN   A 1 45  ? -9.385  21.627  1.962   1.00 63.26  ?  45  ASN   A CG   1 
ATOM   367  O  OD1  . ASN   A 1 45  ? -9.708  21.712  0.777   1.00 57.21  ?  45  ASN   A OD1  1 
ATOM   368  N  ND2  . ASN   A 1 45  ? -10.073 22.215  2.936   1.00 69.82  ?  45  ASN   A ND2  1 
ATOM   369  N  N    . ILE   A 1 46  ? -8.667  18.814  -0.503  1.00 38.21  ?  46  ILE   A N    1 
ATOM   370  C  CA   . ILE   A 1 46  ? -8.630  18.925  -1.959  1.00 35.31  ?  46  ILE   A CA   1 
ATOM   371  C  C    . ILE   A 1 46  ? -9.597  19.984  -2.443  1.00 46.78  ?  46  ILE   A C    1 
ATOM   372  O  O    . ILE   A 1 46  ? -9.248  20.838  -3.263  1.00 47.19  ?  46  ILE   A O    1 
ATOM   373  C  CB   . ILE   A 1 46  ? -8.924  17.569  -2.635  1.00 38.87  ?  46  ILE   A CB   1 
ATOM   374  C  CG1  . ILE   A 1 46  ? -7.940  16.496  -2.176  1.00 43.28  ?  46  ILE   A CG1  1 
ATOM   375  C  CG2  . ILE   A 1 46  ? -8.891  17.722  -4.151  1.00 39.00  ?  46  ILE   A CG2  1 
ATOM   376  C  CD1  . ILE   A 1 46  ? -8.378  15.094  -2.540  1.00 41.99  ?  46  ILE   A CD1  1 
ATOM   377  N  N    . ILE   A 1 47  ? -10.824 19.960  -1.934  1.00 43.97  ?  47  ILE   A N    1 
ATOM   378  C  CA   . ILE   A 1 47  ? -11.800 20.949  -2.373  1.00 39.81  ?  47  ILE   A CA   1 
ATOM   379  C  C    . ILE   A 1 47  ? -12.760 21.243  -1.235  1.00 42.28  ?  47  ILE   A C    1 
ATOM   380  O  O    . ILE   A 1 47  ? -13.210 20.340  -0.527  1.00 55.56  ?  47  ILE   A O    1 
ATOM   381  C  CB   . ILE   A 1 47  ? -12.558 20.479  -3.633  1.00 49.46  ?  47  ILE   A CB   1 
ATOM   382  C  CG1  . ILE   A 1 47  ? -11.621 20.463  -4.842  1.00 49.44  ?  47  ILE   A CG1  1 
ATOM   383  C  CG2  . ILE   A 1 47  ? -13.779 21.355  -3.888  1.00 51.32  ?  47  ILE   A CG2  1 
ATOM   384  C  CD1  . ILE   A 1 47  ? -12.321 20.638  -6.159  1.00 70.76  ?  47  ILE   A CD1  1 
ATOM   385  N  N    . GLN   A 1 48  ? -13.081 22.523  -1.094  1.00 39.01  ?  48  GLN   A N    1 
ATOM   386  C  CA   . GLN   A 1 48  ? -14.033 23.030  -0.116  1.00 50.74  ?  48  GLN   A CA   1 
ATOM   387  C  C    . GLN   A 1 48  ? -14.907 24.028  -0.855  1.00 54.26  ?  48  GLN   A C    1 
ATOM   388  O  O    . GLN   A 1 48  ? -14.471 25.148  -1.139  1.00 59.64  ?  48  GLN   A O    1 
ATOM   389  C  CB   . GLN   A 1 48  ? -13.302 23.683  1.054   1.00 45.59  ?  48  GLN   A CB   1 
ATOM   390  C  CG   . GLN   A 1 48  ? -14.159 24.126  2.214   1.00 59.44  ?  48  GLN   A CG   1 
ATOM   391  C  CD   . GLN   A 1 48  ? -13.309 24.617  3.364   1.00 76.78  ?  48  GLN   A CD   1 
ATOM   392  O  OE1  . GLN   A 1 48  ? -12.111 24.340  3.422   1.00 61.81  ?  48  GLN   A OE1  1 
ATOM   393  N  NE2  . GLN   A 1 48  ? -13.883 25.477  4.195   1.00 69.50  ?  48  GLN   A NE2  1 
ATOM   394  N  N    . PHE   A 1 49  ? -16.136 23.630  -1.148  1.00 46.91  ?  49  PHE   A N    1 
ATOM   395  C  CA   . PHE   A 1 49  ? -17.087 24.440  -1.889  1.00 42.67  ?  49  PHE   A CA   1 
ATOM   396  C  C    . PHE   A 1 49  ? -18.230 24.779  -0.942  1.00 44.87  ?  49  PHE   A C    1 
ATOM   397  O  O    . PHE   A 1 49  ? -19.007 23.896  -0.556  1.00 46.70  ?  49  PHE   A O    1 
ATOM   398  C  CB   . PHE   A 1 49  ? -17.549 23.682  -3.133  1.00 55.26  ?  49  PHE   A CB   1 
ATOM   399  C  CG   . PHE   A 1 49  ? -18.535 24.424  -3.979  1.00 56.11  ?  49  PHE   A CG   1 
ATOM   400  C  CD1  . PHE   A 1 49  ? -19.889 24.386  -3.696  1.00 58.33  ?  49  PHE   A CD1  1 
ATOM   401  C  CD2  . PHE   A 1 49  ? -18.102 25.167  -5.063  1.00 61.70  ?  49  PHE   A CD2  1 
ATOM   402  C  CE1  . PHE   A 1 49  ? -20.791 25.067  -4.487  1.00 67.90  ?  49  PHE   A CE1  1 
ATOM   403  C  CE2  . PHE   A 1 49  ? -18.997 25.853  -5.853  1.00 66.86  ?  49  PHE   A CE2  1 
ATOM   404  C  CZ   . PHE   A 1 49  ? -20.343 25.802  -5.567  1.00 49.87  ?  49  PHE   A CZ   1 
ATOM   405  N  N    . VAL   A 1 50  ? -18.311 26.053  -0.561  1.00 47.26  ?  50  VAL   A N    1 
ATOM   406  C  CA   . VAL   A 1 50  ? -19.320 26.555  0.358   1.00 65.63  ?  50  VAL   A CA   1 
ATOM   407  C  C    . VAL   A 1 50  ? -19.838 27.864  -0.209  1.00 66.77  ?  50  VAL   A C    1 
ATOM   408  O  O    . VAL   A 1 50  ? -19.128 28.578  -0.923  1.00 64.41  ?  50  VAL   A O    1 
ATOM   409  C  CB   . VAL   A 1 50  ? -18.760 26.775  1.779   1.00 66.08  ?  50  VAL   A CB   1 
ATOM   410  C  CG1  . VAL   A 1 50  ? -18.736 25.468  2.549   1.00 67.81  ?  50  VAL   A CG1  1 
ATOM   411  C  CG2  . VAL   A 1 50  ? -17.374 27.396  1.704   1.00 64.12  ?  50  VAL   A CG2  1 
ATOM   412  N  N    . HIS   A 1 51  ? -21.090 28.175  0.105   1.00 76.52  ?  51  HIS   A N    1 
ATOM   413  C  CA   . HIS   A 1 51  ? -21.719 29.380  -0.420  1.00 85.99  ?  51  HIS   A CA   1 
ATOM   414  C  C    . HIS   A 1 51  ? -21.549 29.471  -1.934  1.00 79.11  ?  51  HIS   A C    1 
ATOM   415  O  O    . HIS   A 1 51  ? -21.437 30.561  -2.497  1.00 83.45  ?  51  HIS   A O    1 
ATOM   416  C  CB   . HIS   A 1 51  ? -21.174 30.640  0.261   1.00 96.60  ?  51  HIS   A CB   1 
ATOM   417  C  CG   . HIS   A 1 51  ? -21.016 30.515  1.747   1.00 100.19 ?  51  HIS   A CG   1 
ATOM   418  N  ND1  . HIS   A 1 51  ? -19.840 30.823  2.395   1.00 96.69  ?  51  HIS   A ND1  1 
ATOM   419  C  CD2  . HIS   A 1 51  ? -21.881 30.115  2.711   1.00 100.16 ?  51  HIS   A CD2  1 
ATOM   420  C  CE1  . HIS   A 1 51  ? -19.985 30.620  3.692   1.00 108.26 ?  51  HIS   A CE1  1 
ATOM   421  N  NE2  . HIS   A 1 51  ? -21.214 30.189  3.911   1.00 101.06 ?  51  HIS   A NE2  1 
ATOM   422  N  N    . GLY   A 1 52  ? -21.553 28.324  -2.605  1.00 62.01  ?  52  GLY   A N    1 
ATOM   423  C  CA   . GLY   A 1 52  ? -21.386 28.332  -4.048  1.00 79.93  ?  52  GLY   A CA   1 
ATOM   424  C  C    . GLY   A 1 52  ? -20.092 28.953  -4.522  1.00 71.46  ?  52  GLY   A C    1 
ATOM   425  O  O    . GLY   A 1 52  ? -20.044 29.520  -5.615  1.00 74.43  ?  52  GLY   A O    1 
ATOM   426  N  N    . GLU   A 1 53  ? -19.031 28.799  -3.765  1.00 74.27  ?  53  GLU   A N    1 
ATOM   427  C  CA   . GLU   A 1 53  ? -17.787 29.484  -4.024  1.00 92.31  ?  53  GLU   A CA   1 
ATOM   428  C  C    . GLU   A 1 53  ? -16.775 28.355  -3.879  1.00 88.67  ?  53  GLU   A C    1 
ATOM   429  O  O    . GLU   A 1 53  ? -16.920 27.577  -2.931  1.00 84.08  ?  53  GLU   A O    1 
ATOM   430  C  CB   . GLU   A 1 53  ? -17.547 30.481  -2.817  1.00 92.95  ?  53  GLU   A CB   1 
ATOM   431  C  CG   . GLU   A 1 53  ? -16.482 31.618  -2.936  1.00 101.86 ?  53  GLU   A CG   1 
ATOM   432  C  CD   . GLU   A 1 53  ? -16.927 32.751  -3.835  1.00 112.94 ?  53  GLU   A CD   1 
ATOM   433  O  OE1  . GLU   A 1 53  ? -16.591 33.365  -2.885  1.00 116.51 ?  53  GLU   A OE1  1 
ATOM   434  O  OE2  . GLU   A 1 53  ? -16.972 33.838  -4.426  1.00 117.94 ?  53  GLU   A OE2  1 
ATOM   435  N  N    . GLU   A 1 54  ? -15.775 28.202  -4.759  1.00 84.67  ?  54  GLU   A N    1 
ATOM   436  C  CA   . GLU   A 1 54  ? -14.648 27.383  -4.345  1.00 76.69  ?  54  GLU   A CA   1 
ATOM   437  C  C    . GLU   A 1 54  ? -13.775 28.181  -3.394  1.00 81.35  ?  54  GLU   A C    1 
ATOM   438  O  O    . GLU   A 1 54  ? -13.509 29.367  -3.613  1.00 94.93  ?  54  GLU   A O    1 
ATOM   439  C  CB   . GLU   A 1 54  ? -13.817 26.820  -5.495  1.00 72.92  ?  54  GLU   A CB   1 
ATOM   440  C  CG   . GLU   A 1 54  ? -14.166 25.360  -5.898  1.00 69.02  ?  54  GLU   A CG   1 
ATOM   441  C  CD   . GLU   A 1 54  ? -13.228 24.816  -6.967  1.00 92.85  ?  54  GLU   A CD   1 
ATOM   442  O  OE1  . GLU   A 1 54  ? -12.062 24.535  -6.590  1.00 85.92  ?  54  GLU   A OE1  1 
ATOM   443  O  OE2  . GLU   A 1 54  ? -13.623 24.642  -8.133  1.00 93.93  ?  54  GLU   A OE2  1 
ATOM   444  N  N    . ASP   A 1 55  ? -13.389 27.544  -2.301  1.00 81.56  ?  55  ASP   A N    1 
ATOM   445  C  CA   . ASP   A 1 55  ? -12.532 28.172  -1.304  1.00 83.91  ?  55  ASP   A CA   1 
ATOM   446  C  C    . ASP   A 1 55  ? -11.134 27.593  -1.488  1.00 93.40  ?  55  ASP   A C    1 
ATOM   447  O  O    . ASP   A 1 55  ? -10.858 26.464  -1.072  1.00 87.28  ?  55  ASP   A O    1 
ATOM   448  C  CB   . ASP   A 1 55  ? -13.060 27.934  0.106   1.00 93.11  ?  55  ASP   A CB   1 
ATOM   449  C  CG   . ASP   A 1 55  ? -12.391 28.825  1.130   1.00 111.01 ?  55  ASP   A CG   1 
ATOM   450  O  OD1  . ASP   A 1 55  ? -11.151 28.946  1.078   1.00 110.16 ?  55  ASP   A OD1  1 
ATOM   451  O  OD2  . ASP   A 1 55  ? -13.096 29.390  1.994   1.00 102.29 ?  55  ASP   A OD2  1 
ATOM   452  N  N    . LEU   A 1 56  ? -10.244 28.382  -2.095  1.00 89.93  ?  56  LEU   A N    1 
ATOM   453  C  CA   . LEU   A 1 56  ? -8.970  27.873  -2.589  1.00 90.03  ?  56  LEU   A CA   1 
ATOM   454  C  C    . LEU   A 1 56  ? -7.792  28.087  -1.646  1.00 90.55  ?  56  LEU   A C    1 
ATOM   455  O  O    . LEU   A 1 56  ? -6.748  27.456  -1.844  1.00 81.99  ?  56  LEU   A O    1 
ATOM   456  C  CB   . LEU   A 1 56  ? -8.642  28.514  -3.943  1.00 72.73  ?  56  LEU   A CB   1 
ATOM   457  C  CG   . LEU   A 1 56  ? -7.801  27.676  -4.908  1.00 88.49  ?  56  LEU   A CG   1 
ATOM   458  C  CD1  . LEU   A 1 56  ? -8.698  26.761  -5.723  1.00 78.24  ?  56  LEU   A CD1  1 
ATOM   459  C  CD2  . LEU   A 1 56  ? -6.970  28.568  -5.819  1.00 95.45  ?  56  LEU   A CD2  1 
ATOM   460  N  N    . LYS   A 1 57  ? -7.917  28.955  -0.640  1.00 101.42 ?  57  LYS   A N    1 
ATOM   461  C  CA   . LYS   A 1 57  ? -6.757  29.298  0.180   1.00 102.11 ?  57  LYS   A CA   1 
ATOM   462  C  C    . LYS   A 1 57  ? -6.317  28.127  1.048   1.00 96.48  ?  57  LYS   A C    1 
ATOM   463  O  O    . LYS   A 1 57  ? -5.118  27.954  1.298   1.00 79.64  ?  57  LYS   A O    1 
ATOM   464  C  CB   . LYS   A 1 57  ? -7.083  30.501  1.059   1.00 111.83 ?  57  LYS   A CB   1 
ATOM   465  C  CG   . LYS   A 1 57  ? -8.296  30.256  1.939   1.00 107.14 ?  57  LYS   A CG   1 
ATOM   466  C  CD   . LYS   A 1 57  ? -9.125  31.509  2.131   1.00 116.76 ?  57  LYS   A CD   1 
ATOM   467  C  CE   . LYS   A 1 57  ? -10.280 31.256  3.089   1.00 114.17 ?  57  LYS   A CE   1 
ATOM   468  N  NZ   . LYS   A 1 57  ? -11.285 32.355  3.057   1.00 113.38 ?  57  LYS   A NZ   1 
ATOM   469  N  N    . VAL   A 1 58  ? -7.271  27.299  1.491   1.00 88.32  ?  58  VAL   A N    1 
ATOM   470  C  CA   . VAL   A 1 58  ? -6.964  26.116  2.292   1.00 88.65  ?  58  VAL   A CA   1 
ATOM   471  C  C    . VAL   A 1 58  ? -6.652  24.900  1.439   1.00 70.85  ?  58  VAL   A C    1 
ATOM   472  O  O    . VAL   A 1 58  ? -6.333  23.837  1.988   1.00 65.40  ?  58  VAL   A O    1 
ATOM   473  C  CB   . VAL   A 1 58  ? -8.135  25.832  3.259   1.00 92.45  ?  58  VAL   A CB   1 
ATOM   474  C  CG1  . VAL   A 1 58  ? -7.956  24.500  3.996   1.00 85.99  ?  58  VAL   A CG1  1 
ATOM   475  C  CG2  . VAL   A 1 58  ? -8.266  26.967  4.261   1.00 88.66  ?  58  VAL   A CG2  1 
ATOM   476  N  N    . GLN   A 1 59  ? -6.704  25.019  0.115   1.00 72.41  ?  59  GLN   A N    1 
ATOM   477  C  CA   . GLN   A 1 59  ? -6.437  23.853  -0.709  1.00 55.75  ?  59  GLN   A CA   1 
ATOM   478  C  C    . GLN   A 1 59  ? -5.005  23.394  -0.468  1.00 51.16  ?  59  GLN   A C    1 
ATOM   479  O  O    . GLN   A 1 59  ? -4.068  24.198  -0.488  1.00 52.96  ?  59  GLN   A O    1 
ATOM   480  C  CB   . GLN   A 1 59  ? -6.665  24.159  -2.188  1.00 54.88  ?  59  GLN   A CB   1 
ATOM   481  C  CG   . GLN   A 1 59  ? -6.259  23.010  -3.095  1.00 46.98  ?  59  GLN   A CG   1 
ATOM   482  C  CD   . GLN   A 1 59  ? -6.756  23.175  -4.513  1.00 65.60  ?  59  GLN   A CD   1 
ATOM   483  O  OE1  . GLN   A 1 59  ? -6.262  24.015  -5.264  1.00 70.08  ?  59  GLN   A OE1  1 
ATOM   484  N  NE2  . GLN   A 1 59  ? -7.741  22.368  -4.890  1.00 61.18  ?  59  GLN   A NE2  1 
ATOM   485  N  N    . HIS   A 1 60  ? -4.846  22.097  -0.235  1.00 54.96  ?  60  HIS   A N    1 
ATOM   486  C  CA   . HIS   A 1 60  ? -3.551  21.543  0.128   1.00 48.27  ?  60  HIS   A CA   1 
ATOM   487  C  C    . HIS   A 1 60  ? -2.552  21.663  -1.019  1.00 61.63  ?  60  HIS   A C    1 
ATOM   488  O  O    . HIS   A 1 60  ? -2.909  21.596  -2.198  1.00 58.43  ?  60  HIS   A O    1 
ATOM   489  C  CB   . HIS   A 1 60  ? -3.693  20.085  0.558   1.00 55.65  ?  60  HIS   A CB   1 
ATOM   490  C  CG   . HIS   A 1 60  ? -2.422  19.487  1.072   1.00 58.42  ?  60  HIS   A CG   1 
ATOM   491  N  ND1  . HIS   A 1 60  ? -1.422  19.038  0.238   1.00 56.16  ?  60  HIS   A ND1  1 
ATOM   492  C  CD2  . HIS   A 1 60  ? -1.976  19.292  2.335   1.00 55.50  ?  60  HIS   A CD2  1 
ATOM   493  C  CE1  . HIS   A 1 60  ? -0.421  18.575  0.964   1.00 68.63  ?  60  HIS   A CE1  1 
ATOM   494  N  NE2  . HIS   A 1 60  ? -0.731  18.718  2.240   1.00 58.47  ?  60  HIS   A NE2  1 
ATOM   495  N  N    . SER   A 1 61  ? -1.281  21.845  -0.649  1.00 54.29  ?  61  SER   A N    1 
ATOM   496  C  CA   . SER   A 1 61  ? -0.245  22.177  -1.621  1.00 62.09  ?  61  SER   A CA   1 
ATOM   497  C  C    . SER   A 1 61  ? -0.172  21.157  -2.751  1.00 54.70  ?  61  SER   A C    1 
ATOM   498  O  O    . SER   A 1 61  ? -0.009  21.527  -3.919  1.00 60.54  ?  61  SER   A O    1 
ATOM   499  C  CB   . SER   A 1 61  ? 1.109   22.272  -0.912  1.00 66.83  ?  61  SER   A CB   1 
ATOM   500  O  OG   . SER   A 1 61  ? 2.084   22.897  -1.726  1.00 72.73  ?  61  SER   A OG   1 
ATOM   501  N  N    . SER   A 1 62  ? -0.303  19.870  -2.429  1.00 53.58  ?  62  SER   A N    1 
ATOM   502  C  CA   . SER   A 1 62  ? -0.136  18.840  -3.447  1.00 66.18  ?  62  SER   A CA   1 
ATOM   503  C  C    . SER   A 1 62  ? -1.228  18.872  -4.509  1.00 67.73  ?  62  SER   A C    1 
ATOM   504  O  O    . SER   A 1 62  ? -1.065  18.241  -5.559  1.00 61.70  ?  62  SER   A O    1 
ATOM   505  C  CB   . SER   A 1 62  ? -0.086  17.459  -2.791  1.00 54.27  ?  62  SER   A CB   1 
ATOM   506  O  OG   . SER   A 1 62  ? -1.379  17.025  -2.411  1.00 67.50  ?  62  SER   A OG   1 
ATOM   507  N  N    . TYR   A 1 63  ? -2.330  19.579  -4.268  1.00 56.75  ?  63  TYR   A N    1 
ATOM   508  C  CA   . TYR   A 1 63  ? -3.445  19.604  -5.202  1.00 52.82  ?  63  TYR   A CA   1 
ATOM   509  C  C    . TYR   A 1 63  ? -3.697  20.982  -5.797  1.00 64.12  ?  63  TYR   A C    1 
ATOM   510  O  O    . TYR   A 1 63  ? -4.620  21.131  -6.607  1.00 55.71  ?  63  TYR   A O    1 
ATOM   511  C  CB   . TYR   A 1 63  ? -4.710  19.080  -4.511  1.00 52.72  ?  63  TYR   A CB   1 
ATOM   512  C  CG   . TYR   A 1 63  ? -4.671  17.582  -4.318  1.00 57.78  ?  63  TYR   A CG   1 
ATOM   513  C  CD1  . TYR   A 1 63  ? -4.851  16.718  -5.389  1.00 50.66  ?  63  TYR   A CD1  1 
ATOM   514  C  CD2  . TYR   A 1 63  ? -4.412  17.032  -3.069  1.00 54.30  ?  63  TYR   A CD2  1 
ATOM   515  C  CE1  . TYR   A 1 63  ? -4.799  15.346  -5.217  1.00 42.14  ?  63  TYR   A CE1  1 
ATOM   516  C  CE2  . TYR   A 1 63  ? -4.357  15.663  -2.887  1.00 52.10  ?  63  TYR   A CE2  1 
ATOM   517  C  CZ   . TYR   A 1 63  ? -4.551  14.824  -3.965  1.00 66.32  ?  63  TYR   A CZ   1 
ATOM   518  O  OH   . TYR   A 1 63  ? -4.498  13.460  -3.788  1.00 50.99  ?  63  TYR   A OH   1 
ATOM   519  N  N    . ARG   A 1 64  ? -2.915  21.990  -5.420  1.00 57.72  ?  64  ARG   A N    1 
ATOM   520  C  CA   . ARG   A 1 64  ? -3.114  23.330  -5.954  1.00 59.70  ?  64  ARG   A CA   1 
ATOM   521  C  C    . ARG   A 1 64  ? -2.719  23.364  -7.429  1.00 55.38  ?  64  ARG   A C    1 
ATOM   522  O  O    . ARG   A 1 64  ? -1.727  22.757  -7.840  1.00 52.40  ?  64  ARG   A O    1 
ATOM   523  C  CB   . ARG   A 1 64  ? -2.318  24.338  -5.116  1.00 63.53  ?  64  ARG   A CB   1 
ATOM   524  C  CG   . ARG   A 1 64  ? -2.129  25.736  -5.693  1.00 67.91  ?  64  ARG   A CG   1 
ATOM   525  C  CD   . ARG   A 1 64  ? -0.773  25.901  -6.358  1.00 81.23  ?  64  ARG   A CD   1 
ATOM   526  N  NE   . ARG   A 1 64  ? -0.516  27.285  -6.742  1.00 70.92  ?  64  ARG   A NE   1 
ATOM   527  N  N    . GLN   A 1 65  ? -3.517  24.073  -8.228  1.00 64.05  ?  65  GLN   A N    1 
ATOM   528  C  CA   . GLN   A 1 65  ? -3.364  24.131  -9.682  1.00 62.92  ?  65  GLN   A CA   1 
ATOM   529  C  C    . GLN   A 1 65  ? -3.519  22.764  -10.342 1.00 59.61  ?  65  GLN   A C    1 
ATOM   530  O  O    . GLN   A 1 65  ? -3.089  22.573  -11.484 1.00 78.07  ?  65  GLN   A O    1 
ATOM   531  C  CB   . GLN   A 1 65  ? -2.028  24.762  -10.096 1.00 61.50  ?  65  GLN   A CB   1 
ATOM   532  C  CG   . GLN   A 1 65  ? -1.668  26.025  -9.342  1.00 67.69  ?  65  GLN   A CG   1 
ATOM   533  C  CD   . GLN   A 1 65  ? -1.998  27.276  -10.135 1.00 72.79  ?  65  GLN   A CD   1 
ATOM   534  O  OE1  . GLN   A 1 65  ? -3.120  27.780  -10.077 1.00 78.40  ?  65  GLN   A OE1  1 
ATOM   535  N  NE2  . GLN   A 1 65  ? -1.025  27.776  -10.890 1.00 75.83  ?  65  GLN   A NE2  1 
ATOM   536  N  N    . ARG   A 1 66  ? -4.125  21.800  -9.649  1.00 55.09  ?  66  ARG   A N    1 
ATOM   537  C  CA   . ARG   A 1 66  ? -4.332  20.478  -10.235 1.00 56.48  ?  66  ARG   A CA   1 
ATOM   538  C  C    . ARG   A 1 66  ? -5.711  19.887  -9.986  1.00 57.37  ?  66  ARG   A C    1 
ATOM   539  O  O    . ARG   A 1 66  ? -6.101  18.971  -10.719 1.00 61.78  ?  66  ARG   A O    1 
ATOM   540  C  CB   . ARG   A 1 66  ? -3.280  19.492  -9.711  1.00 55.96  ?  66  ARG   A CB   1 
ATOM   541  C  CG   . ARG   A 1 66  ? -1.917  19.600  -10.380 1.00 70.06  ?  66  ARG   A CG   1 
ATOM   542  C  CD   . ARG   A 1 66  ? -1.135  18.305  -10.226 1.00 65.84  ?  66  ARG   A CD   1 
ATOM   543  N  NE   . ARG   A 1 66  ? -1.280  17.750  -8.885  1.00 52.35  ?  66  ARG   A NE   1 
ATOM   544  C  CZ   . ARG   A 1 66  ? -1.678  16.512  -8.627  1.00 49.50  ?  66  ARG   A CZ   1 
ATOM   545  N  NH1  . ARG   A 1 66  ? -1.874  15.632  -9.596  1.00 51.70  ?  66  ARG   A NH1  1 
ATOM   546  N  NH2  . ARG   A 1 66  ? -1.862  16.139  -7.363  1.00 46.34  ?  66  ARG   A NH2  1 
ATOM   547  N  N    . ALA   A 1 67  ? -6.467  20.358  -8.998  1.00 51.95  ?  67  ALA   A N    1 
ATOM   548  C  CA   . ALA   A 1 67  ? -7.767  19.795  -8.661  1.00 43.40  ?  67  ALA   A CA   1 
ATOM   549  C  C    . ALA   A 1 67  ? -8.833  20.875  -8.753  1.00 57.05  ?  67  ALA   A C    1 
ATOM   550  O  O    . ALA   A 1 67  ? -8.639  21.987  -8.250  1.00 55.05  ?  67  ALA   A O    1 
ATOM   551  C  CB   . ALA   A 1 67  ? -7.754  19.183  -7.257  1.00 48.65  ?  67  ALA   A CB   1 
ATOM   552  N  N    . ARG   A 1 68  ? -9.960  20.547  -9.380  1.00 47.22  ?  68  ARG   A N    1 
ATOM   553  C  CA   . ARG   A 1 68  ? -11.108 21.442  -9.329  1.00 51.58  ?  68  ARG   A CA   1 
ATOM   554  C  C    . ARG   A 1 68  ? -12.396 20.638  -9.337  1.00 49.14  ?  68  ARG   A C    1 
ATOM   555  O  O    . ARG   A 1 68  ? -12.446 19.490  -9.787  1.00 45.59  ?  68  ARG   A O    1 
ATOM   556  C  CB   . ARG   A 1 68  ? -11.158 22.451  -10.483 1.00 51.24  ?  68  ARG   A CB   1 
ATOM   557  C  CG   . ARG   A 1 68  ? -11.161 21.828  -11.854 1.00 72.33  ?  68  ARG   A CG   1 
ATOM   558  C  CD   . ARG   A 1 68  ? -10.360 22.666  -12.820 1.00 76.27  ?  68  ARG   A CD   1 
ATOM   559  N  NE   . ARG   A 1 68  ? -8.956  22.709  -12.440 1.00 95.39  ?  68  ARG   A NE   1 
ATOM   560  C  CZ   . ARG   A 1 68  ? -8.078  21.752  -12.699 1.00 85.91  ?  68  ARG   A CZ   1 
ATOM   561  N  NH1  . ARG   A 1 68  ? -8.462  20.561  -13.126 1.00 79.75  ?  68  ARG   A NH1  1 
ATOM   562  N  NH2  . ARG   A 1 68  ? -6.790  21.971  -12.453 1.00 80.39  ?  68  ARG   A NH2  1 
ATOM   563  N  N    . LEU   A 1 69  ? -13.445 21.278  -8.839  1.00 49.41  ?  69  LEU   A N    1 
ATOM   564  C  CA   . LEU   A 1 69  ? -14.789 20.733  -8.894  1.00 42.78  ?  69  LEU   A CA   1 
ATOM   565  C  C    . LEU   A 1 69  ? -15.438 21.210  -10.185 1.00 42.39  ?  69  LEU   A C    1 
ATOM   566  O  O    . LEU   A 1 69  ? -15.360 22.396  -10.522 1.00 50.15  ?  69  LEU   A O    1 
ATOM   567  C  CB   . LEU   A 1 69  ? -15.602 21.199  -7.685  1.00 50.14  ?  69  LEU   A CB   1 
ATOM   568  C  CG   . LEU   A 1 69  ? -16.925 20.521  -7.327  1.00 55.98  ?  69  LEU   A CG   1 
ATOM   569  C  CD1  . LEU   A 1 69  ? -16.709 19.080  -6.895  1.00 47.04  ?  69  LEU   A CD1  1 
ATOM   570  C  CD2  . LEU   A 1 69  ? -17.632 21.316  -6.240  1.00 59.47  ?  69  LEU   A CD2  1 
ATOM   571  N  N    . LEU   A 1 70  ? -16.054 20.288  -10.915 1.00 47.24  ?  70  LEU   A N    1 
ATOM   572  C  CA   . LEU   A 1 70  ? -16.768 20.646  -12.137 1.00 53.16  ?  70  LEU   A CA   1 
ATOM   573  C  C    . LEU   A 1 70  ? -18.130 21.185  -11.714 1.00 44.96  ?  70  LEU   A C    1 
ATOM   574  O  O    . LEU   A 1 70  ? -19.061 20.422  -11.446 1.00 52.27  ?  70  LEU   A O    1 
ATOM   575  C  CB   . LEU   A 1 70  ? -16.875 19.444  -13.069 1.00 58.30  ?  70  LEU   A CB   1 
ATOM   576  C  CG   . LEU   A 1 70  ? -15.532 18.779  -13.410 1.00 50.40  ?  70  LEU   A CG   1 
ATOM   577  C  CD1  . LEU   A 1 70  ? -15.726 17.362  -13.939 1.00 61.54  ?  70  LEU   A CD1  1 
ATOM   578  C  CD2  . LEU   A 1 70  ? -14.720 19.616  -14.388 1.00 64.29  ?  70  LEU   A CD2  1 
ATOM   579  N  N    . LYS   A 1 71  ? -18.250 22.517  -11.661 1.00 54.91  ?  71  LYS   A N    1 
ATOM   580  C  CA   . LYS   A 1 71  ? -19.393 23.144  -11.001 1.00 57.05  ?  71  LYS   A CA   1 
ATOM   581  C  C    . LYS   A 1 71  ? -20.674 22.978  -11.804 1.00 69.32  ?  71  LYS   A C    1 
ATOM   582  O  O    . LYS   A 1 71  ? -21.757 22.847  -11.223 1.00 58.46  ?  71  LYS   A O    1 
ATOM   583  C  CB   . LYS   A 1 71  ? -19.131 24.635  -10.785 1.00 65.20  ?  71  LYS   A CB   1 
ATOM   584  C  CG   . LYS   A 1 71  ? -17.671 25.013  -10.624 1.00 67.40  ?  71  LYS   A CG   1 
ATOM   585  C  CD   . LYS   A 1 71  ? -17.462 26.039  -9.522  1.00 66.22  ?  71  LYS   A CD   1 
ATOM   586  C  CE   . LYS   A 1 71  ? -16.055 25.938  -8.958  1.00 81.05  ?  71  LYS   A CE   1 
ATOM   587  N  NZ   . LYS   A 1 71  ? -15.743 27.029  -7.995  1.00 89.52  ?  71  LYS   A NZ   1 
ATOM   588  N  N    . ASP   A 1 72  ? -20.572 22.994  -13.134 1.00 60.89  ?  72  ASP   A N    1 
ATOM   589  C  CA   . ASP   A 1 72  ? -21.760 22.919  -13.977 1.00 65.93  ?  72  ASP   A CA   1 
ATOM   590  C  C    . ASP   A 1 72  ? -22.584 21.674  -13.680 1.00 67.06  ?  72  ASP   A C    1 
ATOM   591  O  O    . ASP   A 1 72  ? -23.816 21.709  -13.766 1.00 64.06  ?  72  ASP   A O    1 
ATOM   592  C  CB   . ASP   A 1 72  ? -21.347 22.937  -15.447 1.00 57.12  ?  72  ASP   A CB   1 
ATOM   593  C  CG   . ASP   A 1 72  ? -20.403 21.802  -15.794 1.00 78.80  ?  72  ASP   A CG   1 
ATOM   594  O  OD1  . ASP   A 1 72  ? -19.193 21.926  -15.506 1.00 83.33  ?  72  ASP   A OD1  1 
ATOM   595  O  OD2  . ASP   A 1 72  ? -20.870 20.784  -16.346 1.00 80.14  ?  72  ASP   A OD2  1 
ATOM   596  N  N    . GLN   A 1 73  ? -21.926 20.568  -13.335 1.00 63.99  ?  73  GLN   A N    1 
ATOM   597  C  CA   . GLN   A 1 73  ? -22.620 19.317  -13.064 1.00 74.28  ?  73  GLN   A CA   1 
ATOM   598  C  C    . GLN   A 1 73  ? -23.316 19.300  -11.708 1.00 58.57  ?  73  GLN   A C    1 
ATOM   599  O  O    . GLN   A 1 73  ? -24.108 18.387  -11.451 1.00 59.00  ?  73  GLN   A O    1 
ATOM   600  C  CB   . GLN   A 1 73  ? -21.631 18.155  -13.170 1.00 61.77  ?  73  GLN   A CB   1 
ATOM   601  C  CG   . GLN   A 1 73  ? -20.837 18.177  -14.467 1.00 84.74  ?  73  GLN   A CG   1 
ATOM   602  C  CD   . GLN   A 1 73  ? -20.189 16.849  -14.786 1.00 87.35  ?  73  GLN   A CD   1 
ATOM   603  O  OE1  . GLN   A 1 73  ? -19.109 16.799  -15.375 1.00 96.27  ?  73  GLN   A OE1  1 
ATOM   604  N  NE2  . GLN   A 1 73  ? -20.846 15.762  -14.401 1.00 83.69  ?  73  GLN   A NE2  1 
ATOM   605  N  N    . LEU   A 1 74  ? -23.051 20.285  -10.846 1.00 48.16  ?  74  LEU   A N    1 
ATOM   606  C  CA   . LEU   A 1 74  ? -23.745 20.351  -9.563  1.00 55.75  ?  74  LEU   A CA   1 
ATOM   607  C  C    . LEU   A 1 74  ? -25.256 20.388  -9.756  1.00 62.25  ?  74  LEU   A C    1 
ATOM   608  O  O    . LEU   A 1 74  ? -26.004 19.783  -8.979  1.00 51.96  ?  74  LEU   A O    1 
ATOM   609  C  CB   . LEU   A 1 74  ? -23.270 21.566  -8.764  1.00 56.06  ?  74  LEU   A CB   1 
ATOM   610  C  CG   . LEU   A 1 74  ? -21.829 21.512  -8.249  1.00 52.59  ?  74  LEU   A CG   1 
ATOM   611  C  CD1  . LEU   A 1 74  ? -21.586 22.603  -7.216  1.00 62.61  ?  74  LEU   A CD1  1 
ATOM   612  C  CD2  . LEU   A 1 74  ? -21.523 20.140  -7.668  1.00 53.61  ?  74  LEU   A CD2  1 
ATOM   613  N  N    . SER   A 1 75  ? -25.725 21.092  -10.792 1.00 62.24  ?  75  SER   A N    1 
ATOM   614  C  CA   . SER   A 1 75  ? -27.160 21.166  -11.046 1.00 44.97  ?  75  SER   A CA   1 
ATOM   615  C  C    . SER   A 1 75  ? -27.768 19.784  -11.226 1.00 57.28  ?  75  SER   A C    1 
ATOM   616  O  O    . SER   A 1 75  ? -28.956 19.585  -10.946 1.00 48.43  ?  75  SER   A O    1 
ATOM   617  C  CB   . SER   A 1 75  ? -27.435 22.013  -12.290 1.00 75.96  ?  75  SER   A CB   1 
ATOM   618  O  OG   . SER   A 1 75  ? -26.743 21.509  -13.419 1.00 50.20  ?  75  SER   A OG   1 
ATOM   619  N  N    . LEU   A 1 76  ? -26.975 18.823  -11.682 1.00 63.28  ?  76  LEU   A N    1 
ATOM   620  C  CA   . LEU   A 1 76  ? -27.441 17.464  -11.908 1.00 50.27  ?  76  LEU   A CA   1 
ATOM   621  C  C    . LEU   A 1 76  ? -27.343 16.597  -10.662 1.00 58.56  ?  76  LEU   A C    1 
ATOM   622  O  O    . LEU   A 1 76  ? -27.741 15.428  -10.702 1.00 54.47  ?  76  LEU   A O    1 
ATOM   623  C  CB   . LEU   A 1 76  ? -26.633 16.828  -13.041 1.00 55.23  ?  76  LEU   A CB   1 
ATOM   624  C  CG   . LEU   A 1 76  ? -26.742 17.535  -14.393 1.00 59.26  ?  76  LEU   A CG   1 
ATOM   625  C  CD1  . LEU   A 1 76  ? -25.946 16.799  -15.459 1.00 74.31  ?  76  LEU   A CD1  1 
ATOM   626  C  CD2  . LEU   A 1 76  ? -28.195 17.686  -14.808 1.00 66.10  ?  76  LEU   A CD2  1 
ATOM   627  N  N    . GLY   A 1 77  ? -26.832 17.139  -9.561  1.00 51.08  ?  77  GLY   A N    1 
ATOM   628  C  CA   . GLY   A 1 77  ? -26.569 16.335  -8.385  1.00 54.14  ?  77  GLY   A CA   1 
ATOM   629  C  C    . GLY   A 1 77  ? -25.280 15.555  -8.488  1.00 47.73  ?  77  GLY   A C    1 
ATOM   630  O  O    . GLY   A 1 77  ? -25.198 14.425  -7.991  1.00 44.87  ?  77  GLY   A O    1 
ATOM   631  N  N    . ASN   A 1 78  ? -24.258 16.142  -9.105  1.00 41.59  ?  78  ASN   A N    1 
ATOM   632  C  CA   . ASN   A 1 78  ? -22.981 15.483  -9.353  1.00 45.85  ?  78  ASN   A CA   1 
ATOM   633  C  C    . ASN   A 1 78  ? -21.831 16.369  -8.909  1.00 45.37  ?  78  ASN   A C    1 
ATOM   634  O  O    . ASN   A 1 78  ? -21.548 17.390  -9.543  1.00 49.72  ?  78  ASN   A O    1 
ATOM   635  C  CB   . ASN   A 1 78  ? -22.806 15.130  -10.825 1.00 54.05  ?  78  ASN   A CB   1 
ATOM   636  C  CG   . ASN   A 1 78  ? -21.938 13.921  -11.013 1.00 66.11  ?  78  ASN   A CG   1 
ATOM   637  O  OD1  . ASN   A 1 78  ? -20.838 14.021  -11.547 1.00 70.47  ?  78  ASN   A OD1  1 
ATOM   638  N  ND2  . ASN   A 1 78  ? -22.405 12.779  -10.554 1.00 74.20  ?  78  ASN   A ND2  1 
ATOM   639  N  N    . ALA   A 1 79  ? -21.158 15.959  -7.839  1.00 46.36  ?  79  ALA   A N    1 
ATOM   640  C  CA   . ALA   A 1 79  ? -19.919 16.586  -7.395  1.00 40.53  ?  79  ALA   A CA   1 
ATOM   641  C  C    . ALA   A 1 79  ? -18.784 15.767  -7.995  1.00 43.24  ?  79  ALA   A C    1 
ATOM   642  O  O    . ALA   A 1 79  ? -18.414 14.703  -7.486  1.00 51.80  ?  79  ALA   A O    1 
ATOM   643  C  CB   . ALA   A 1 79  ? -19.846 16.649  -5.875  1.00 47.34  ?  79  ALA   A CB   1 
ATOM   644  N  N    . ALA   A 1 80  ? -18.319 16.199  -9.164  1.00 43.96  ?  80  ALA   A N    1 
ATOM   645  C  CA   . ALA   A 1 80  ? -17.221 15.547  -9.861  1.00 45.17  ?  80  ALA   A CA   1 
ATOM   646  C  C    . ALA   A 1 80  ? -15.937 16.308  -9.560  1.00 37.09  ?  80  ALA   A C    1 
ATOM   647  O  O    . ALA   A 1 80  ? -15.852 17.514  -9.816  1.00 41.38  ?  80  ALA   A O    1 
ATOM   648  C  CB   . ALA   A 1 80  ? -17.479 15.494  -11.366 1.00 46.05  ?  80  ALA   A CB   1 
ATOM   649  N  N    . LEU   A 1 81  ? -14.942 15.603  -9.036  1.00 37.06  ?  81  LEU   A N    1 
ATOM   650  C  CA   . LEU   A 1 81  ? -13.618 16.157  -8.796  1.00 34.28  ?  81  LEU   A CA   1 
ATOM   651  C  C    . LEU   A 1 81  ? -12.717 15.742  -9.947  1.00 40.58  ?  81  LEU   A C    1 
ATOM   652  O  O    . LEU   A 1 81  ? -12.572 14.544  -10.224 1.00 34.85  ?  81  LEU   A O    1 
ATOM   653  C  CB   . LEU   A 1 81  ? -13.055 15.665  -7.463  1.00 36.55  ?  81  LEU   A CB   1 
ATOM   654  C  CG   . LEU   A 1 81  ? -11.559 15.863  -7.197  1.00 45.21  ?  81  LEU   A CG   1 
ATOM   655  C  CD1  . LEU   A 1 81  ? -11.228 17.327  -6.936  1.00 40.20  ?  81  LEU   A CD1  1 
ATOM   656  C  CD2  . LEU   A 1 81  ? -11.105 14.989  -6.033  1.00 42.39  ?  81  LEU   A CD2  1 
ATOM   657  N  N    . GLN   A 1 82  ? -12.117 16.721  -10.616 1.00 39.53  ?  82  GLN   A N    1 
ATOM   658  C  CA   . GLN   A 1 82  ? -11.169 16.458  -11.685 1.00 46.70  ?  82  GLN   A CA   1 
ATOM   659  C  C    . GLN   A 1 82  ? -9.771  16.826  -11.216 1.00 43.44  ?  82  GLN   A C    1 
ATOM   660  O  O    . GLN   A 1 82  ? -9.547  17.932  -10.705 1.00 42.34  ?  82  GLN   A O    1 
ATOM   661  C  CB   . GLN   A 1 82  ? -11.529 17.231  -12.955 1.00 51.88  ?  82  GLN   A CB   1 
ATOM   662  C  CG   . GLN   A 1 82  ? -10.490 17.099  -14.057 1.00 51.96  ?  82  GLN   A CG   1 
ATOM   663  C  CD   . GLN   A 1 82  ? -10.862 17.862  -15.309 1.00 65.55  ?  82  GLN   A CD   1 
ATOM   664  O  OE1  . GLN   A 1 82  ? -10.667 19.075  -15.393 1.00 73.11  ?  82  GLN   A OE1  1 
ATOM   665  N  NE2  . GLN   A 1 82  ? -11.402 17.154  -16.294 1.00 67.12  ?  82  GLN   A NE2  1 
ATOM   666  N  N    . ILE   A 1 83  ? -8.843  15.891  -11.397 1.00 45.86  ?  83  ILE   A N    1 
ATOM   667  C  CA   . ILE   A 1 83  ? -7.439  16.061  -11.059 1.00 37.39  ?  83  ILE   A CA   1 
ATOM   668  C  C    . ILE   A 1 83  ? -6.632  15.836  -12.329 1.00 39.33  ?  83  ILE   A C    1 
ATOM   669  O  O    . ILE   A 1 83  ? -6.801  14.812  -13.005 1.00 48.91  ?  83  ILE   A O    1 
ATOM   670  C  CB   . ILE   A 1 83  ? -6.999  15.091  -9.948  1.00 46.63  ?  83  ILE   A CB   1 
ATOM   671  C  CG1  . ILE   A 1 83  ? -7.748  15.397  -8.649  1.00 47.46  ?  83  ILE   A CG1  1 
ATOM   672  C  CG2  . ILE   A 1 83  ? -5.494  15.168  -9.736  1.00 45.10  ?  83  ILE   A CG2  1 
ATOM   673  C  CD1  . ILE   A 1 83  ? -7.303  14.557  -7.474  1.00 52.29  ?  83  ILE   A CD1  1 
ATOM   674  N  N    . THR   A 1 84  ? -5.775  16.797  -12.655 1.00 49.43  ?  84  THR   A N    1 
ATOM   675  C  CA   . THR   A 1 84  ? -4.991  16.776  -13.881 1.00 46.61  ?  84  THR   A CA   1 
ATOM   676  C  C    . THR   A 1 84  ? -3.584  16.280  -13.584 1.00 40.62  ?  84  THR   A C    1 
ATOM   677  O  O    . THR   A 1 84  ? -3.021  16.575  -12.526 1.00 48.26  ?  84  THR   A O    1 
ATOM   678  C  CB   . THR   A 1 84  ? -4.912  18.169  -14.511 1.00 48.70  ?  84  THR   A CB   1 
ATOM   679  O  OG1  . THR   A 1 84  ? -4.399  19.100  -13.550 1.00 56.29  ?  84  THR   A OG1  1 
ATOM   680  C  CG2  . THR   A 1 84  ? -6.286  18.631  -14.970 1.00 52.97  ?  84  THR   A CG2  1 
ATOM   681  N  N    . ASP   A 1 85  ? -3.020  15.520  -14.522 1.00 42.94  ?  85  ASP   A N    1 
ATOM   682  C  CA   . ASP   A 1 85  ? -1.629  15.090  -14.430 1.00 42.34  ?  85  ASP   A CA   1 
ATOM   683  C  C    . ASP   A 1 85  ? -1.414  14.234  -13.179 1.00 41.05  ?  85  ASP   A C    1 
ATOM   684  O  O    . ASP   A 1 85  ? -0.669  14.587  -12.264 1.00 46.51  ?  85  ASP   A O    1 
ATOM   685  C  CB   . ASP   A 1 85  ? -0.697  16.306  -14.453 1.00 47.02  ?  85  ASP   A CB   1 
ATOM   686  C  CG   . ASP   A 1 85  ? 0.752   15.930  -14.669 1.00 50.79  ?  85  ASP   A CG   1 
ATOM   687  O  OD1  . ASP   A 1 85  ? 1.015   14.785  -15.091 1.00 59.13  ?  85  ASP   A OD1  1 
ATOM   688  O  OD2  . ASP   A 1 85  ? 1.630   16.786  -14.427 1.00 64.78  ?  85  ASP   A OD2  1 
ATOM   689  N  N    . VAL   A 1 86  ? -2.113  13.097  -13.153 1.00 36.90  ?  86  VAL   A N    1 
ATOM   690  C  CA   . VAL   A 1 86  ? -2.101  12.233  -11.980 1.00 41.86  ?  86  VAL   A CA   1 
ATOM   691  C  C    . VAL   A 1 86  ? -0.689  11.751  -11.675 1.00 52.56  ?  86  VAL   A C    1 
ATOM   692  O  O    . VAL   A 1 86  ? 0.068   11.352  -12.571 1.00 38.92  ?  86  VAL   A O    1 
ATOM   693  C  CB   . VAL   A 1 86  ? -3.059  11.046  -12.182 1.00 47.15  ?  86  VAL   A CB   1 
ATOM   694  C  CG1  . VAL   A 1 86  ? -2.782  9.956   -11.154 1.00 42.70  ?  86  VAL   A CG1  1 
ATOM   695  C  CG2  . VAL   A 1 86  ? -4.502  11.514  -12.087 1.00 47.67  ?  86  VAL   A CG2  1 
ATOM   696  N  N    . LYS   A 1 87  ? -0.336  11.788  -10.395 1.00 41.20  ?  87  LYS   A N    1 
ATOM   697  C  CA   . LYS   A 1 87  ? 0.933   11.310  -9.866  1.00 41.30  ?  87  LYS   A CA   1 
ATOM   698  C  C    . LYS   A 1 87  ? 0.711   10.000  -9.123  1.00 47.17  ?  87  LYS   A C    1 
ATOM   699  O  O    . LYS   A 1 87  ? -0.420  9.613   -8.819  1.00 40.12  ?  87  LYS   A O    1 
ATOM   700  C  CB   . LYS   A 1 87  ? 1.553   12.339  -8.912  1.00 48.11  ?  87  LYS   A CB   1 
ATOM   701  C  CG   . LYS   A 1 87  ? 1.813   13.712  -9.498  1.00 47.40  ?  87  LYS   A CG   1 
ATOM   702  C  CD   . LYS   A 1 87  ? 2.009   13.645  -10.993 1.00 66.69  ?  87  LYS   A CD   1 
ATOM   703  C  CE   . LYS   A 1 87  ? 3.425   13.194  -11.305 1.00 62.93  ?  87  LYS   A CE   1 
ATOM   704  N  NZ   . LYS   A 1 87  ? 3.853   13.618  -12.663 1.00 71.96  ?  87  LYS   A NZ   1 
ATOM   705  N  N    . LEU   A 1 88  ? 1.812   9.309   -8.823  1.00 38.16  ?  88  LEU   A N    1 
ATOM   706  C  CA   . LEU   A 1 88  ? 1.689   8.114   -7.997  1.00 51.54  ?  88  LEU   A CA   1 
ATOM   707  C  C    . LEU   A 1 88  ? 1.182   8.462   -6.604  1.00 42.21  ?  88  LEU   A C    1 
ATOM   708  O  O    . LEU   A 1 88  ? 0.476   7.659   -5.985  1.00 37.08  ?  88  LEU   A O    1 
ATOM   709  C  CB   . LEU   A 1 88  ? 3.022   7.368   -7.921  1.00 44.92  ?  88  LEU   A CB   1 
ATOM   710  C  CG   . LEU   A 1 88  ? 3.304   6.462   -9.123  1.00 46.69  ?  88  LEU   A CG   1 
ATOM   711  C  CD1  . LEU   A 1 88  ? 4.774   6.078   -9.196  1.00 57.10  ?  88  LEU   A CD1  1 
ATOM   712  C  CD2  . LEU   A 1 88  ? 2.422   5.222   -9.069  1.00 43.75  ?  88  LEU   A CD2  1 
ATOM   713  N  N    . GLN   A 1 89  ? 1.519   9.652   -6.099  1.00 37.83  ?  89  GLN   A N    1 
ATOM   714  C  CA   . GLN   A 1 89  ? 1.040   10.059  -4.782  1.00 45.12  ?  89  GLN   A CA   1 
ATOM   715  C  C    . GLN   A 1 89  ? -0.454  10.354  -4.762  1.00 47.07  ?  89  GLN   A C    1 
ATOM   716  O  O    . GLN   A 1 89  ? -1.014  10.539  -3.676  1.00 34.68  ?  89  GLN   A O    1 
ATOM   717  C  CB   . GLN   A 1 89  ? 1.810   11.285  -4.278  1.00 47.62  ?  89  GLN   A CB   1 
ATOM   718  C  CG   . GLN   A 1 89  ? 1.889   12.453  -5.249  1.00 61.73  ?  89  GLN   A CG   1 
ATOM   719  C  CD   . GLN   A 1 89  ? 3.146   12.423  -6.101  1.00 69.27  ?  89  GLN   A CD   1 
ATOM   720  O  OE1  . GLN   A 1 89  ? 3.837   11.407  -6.178  1.00 54.14  ?  89  GLN   A OE1  1 
ATOM   721  N  NE2  . GLN   A 1 89  ? 3.455   13.548  -6.735  1.00 72.20  ?  89  GLN   A NE2  1 
ATOM   722  N  N    . ASP   A 1 90  ? -1.111  10.406  -5.920  1.00 34.68  ?  90  ASP   A N    1 
ATOM   723  C  CA   . ASP   A 1 90  ? -2.559  10.563  -5.956  1.00 40.13  ?  90  ASP   A CA   1 
ATOM   724  C  C    . ASP   A 1 90  ? -3.297  9.266   -5.651  1.00 41.81  ?  90  ASP   A C    1 
ATOM   725  O  O    . ASP   A 1 90  ? -4.518  9.298   -5.462  1.00 40.64  ?  90  ASP   A O    1 
ATOM   726  C  CB   . ASP   A 1 90  ? -3.000  11.108  -7.317  1.00 40.36  ?  90  ASP   A CB   1 
ATOM   727  C  CG   . ASP   A 1 90  ? -2.527  12.528  -7.556  1.00 48.55  ?  90  ASP   A CG   1 
ATOM   728  O  OD1  . ASP   A 1 90  ? -2.492  13.314  -6.586  1.00 40.02  ?  90  ASP   A OD1  1 
ATOM   729  O  OD2  . ASP   A 1 90  ? -2.187  12.862  -8.711  1.00 50.81  ?  90  ASP   A OD2  1 
ATOM   730  N  N    . ALA   A 1 91  ? -2.596  8.136   -5.611  1.00 33.68  ?  91  ALA   A N    1 
ATOM   731  C  CA   . ALA   A 1 91  ? -3.223  6.875   -5.243  1.00 35.93  ?  91  ALA   A CA   1 
ATOM   732  C  C    . ALA   A 1 91  ? -3.617  6.888   -3.772  1.00 37.79  ?  91  ALA   A C    1 
ATOM   733  O  O    . ALA   A 1 91  ? -2.887  7.402   -2.920  1.00 34.74  ?  91  ALA   A O    1 
ATOM   734  C  CB   . ALA   A 1 91  ? -2.278  5.707   -5.522  1.00 37.93  ?  91  ALA   A CB   1 
ATOM   735  N  N    . GLY   A 1 92  ? -4.776  6.329   -3.474  1.00 37.48  ?  92  GLY   A N    1 
ATOM   736  C  CA   . GLY   A 1 92  ? -5.250  6.277   -2.108  1.00 40.86  ?  92  GLY   A CA   1 
ATOM   737  C  C    . GLY   A 1 92  ? -6.763  6.313   -2.067  1.00 37.68  ?  92  GLY   A C    1 
ATOM   738  O  O    . GLY   A 1 92  ? -7.436  6.129   -3.073  1.00 35.66  ?  92  GLY   A O    1 
ATOM   739  N  N    . VAL   A 1 93  ? -7.289  6.579   -0.878  1.00 36.66  ?  93  VAL   A N    1 
ATOM   740  C  CA   . VAL   A 1 93  ? -8.727  6.567   -0.647  1.00 37.26  ?  93  VAL   A CA   1 
ATOM   741  C  C    . VAL   A 1 93  ? -9.202  8.006   -0.508  1.00 31.97  ?  93  VAL   A C    1 
ATOM   742  O  O    . VAL   A 1 93  ? -8.768  8.734   0.393   1.00 34.43  ?  93  VAL   A O    1 
ATOM   743  C  CB   . VAL   A 1 93  ? -9.095  5.730   0.586   1.00 48.20  ?  93  VAL   A CB   1 
ATOM   744  C  CG1  . VAL   A 1 93  ? -10.600 5.712   0.784   1.00 45.84  ?  93  VAL   A CG1  1 
ATOM   745  C  CG2  . VAL   A 1 93  ? -8.557  4.315   0.431   1.00 42.56  ?  93  VAL   A CG2  1 
ATOM   746  N  N    . TYR   A 1 94  ? -10.091 8.407   -1.407  1.00 35.48  ?  94  TYR   A N    1 
ATOM   747  C  CA   . TYR   A 1 94  ? -10.690 9.727   -1.431  1.00 32.15  ?  94  TYR   A CA   1 
ATOM   748  C  C    . TYR   A 1 94  ? -12.047 9.653   -0.743  1.00 33.34  ?  94  TYR   A C    1 
ATOM   749  O  O    . TYR   A 1 94  ? -12.726 8.627   -0.794  1.00 36.60  ?  94  TYR   A O    1 
ATOM   750  C  CB   . TYR   A 1 94  ? -10.871 10.222  -2.872  1.00 32.77  ?  94  TYR   A CB   1 
ATOM   751  C  CG   . TYR   A 1 94  ? -9.582  10.548  -3.592  1.00 36.14  ?  94  TYR   A CG   1 
ATOM   752  C  CD1  . TYR   A 1 94  ? -8.677  9.545   -3.912  1.00 34.63  ?  94  TYR   A CD1  1 
ATOM   753  C  CD2  . TYR   A 1 94  ? -9.275  11.850  -3.963  1.00 39.21  ?  94  TYR   A CD2  1 
ATOM   754  C  CE1  . TYR   A 1 94  ? -7.499  9.828   -4.572  1.00 33.64  ?  94  TYR   A CE1  1 
ATOM   755  C  CE2  . TYR   A 1 94  ? -8.095  12.144  -4.624  1.00 36.35  ?  94  TYR   A CE2  1 
ATOM   756  C  CZ   . TYR   A 1 94  ? -7.212  11.128  -4.925  1.00 37.41  ?  94  TYR   A CZ   1 
ATOM   757  O  OH   . TYR   A 1 94  ? -6.037  11.411  -5.581  1.00 38.00  ?  94  TYR   A OH   1 
ATOM   758  N  N    . ARG   A 1 95  ? -12.439 10.754  -0.105  1.00 35.22  ?  95  ARG   A N    1 
ATOM   759  C  CA   . ARG   A 1 95  ? -13.757 10.909  0.493   1.00 43.26  ?  95  ARG   A CA   1 
ATOM   760  C  C    . ARG   A 1 95  ? -14.429 12.153  -0.055  1.00 40.83  ?  95  ARG   A C    1 
ATOM   761  O  O    . ARG   A 1 95  ? -13.834 13.244  -0.076  1.00 41.20  ?  95  ARG   A O    1 
ATOM   762  C  CB   . ARG   A 1 95  ? -13.699 10.973  2.027   1.00 36.17  ?  95  ARG   A CB   1 
ATOM   763  C  CG   . ARG   A 1 95  ? -13.666 9.594   2.656   1.00 52.44  ?  95  ARG   A CG   1 
ATOM   764  C  CD   . ARG   A 1 95  ? -12.977 9.567   4.010   1.00 47.45  ?  95  ARG   A CD   1 
ATOM   765  N  NE   . ARG   A 1 95  ? -13.959 9.369   5.080   1.00 72.57  ?  95  ARG   A NE   1 
ATOM   766  C  CZ   . ARG   A 1 95  ? -13.679 9.488   6.379   1.00 73.91  ?  95  ARG   A CZ   1 
ATOM   767  N  NH1  . ARG   A 1 95  ? -12.458 9.669   6.815   1.00 72.03  ?  95  ARG   A NH1  1 
ATOM   768  N  NH2  . ARG   A 1 95  ? -14.651 9.464   7.274   1.00 83.03  ?  95  ARG   A NH2  1 
ATOM   769  N  N    . CYS   A 1 96  ? -15.677 11.970  -0.482  1.00 30.22  ?  96  CYS   A N    1 
ATOM   770  C  CA   . CYS   A 1 96  ? -16.545 13.065  -0.881  1.00 35.56  ?  96  CYS   A CA   1 
ATOM   771  C  C    . CYS   A 1 96  ? -17.588 13.228  0.213   1.00 36.07  ?  96  CYS   A C    1 
ATOM   772  O  O    . CYS   A 1 96  ? -18.299 12.272  0.548   1.00 40.88  ?  96  CYS   A O    1 
ATOM   773  C  CB   . CYS   A 1 96  ? -17.224 12.801  -2.223  1.00 41.11  ?  96  CYS   A CB   1 
ATOM   774  S  SG   . CYS   A 1 96  ? -18.437 11.473  -2.175  1.00 51.57  ?  96  CYS   A SG   1 
ATOM   775  N  N    . MET   A 1 97  ? -17.655 14.427  0.777   1.00 42.99  ?  97  MET   A N    1 
ATOM   776  C  CA   . MET   A 1 97  ? -18.477 14.729  1.936   1.00 34.16  ?  97  MET   A CA   1 
ATOM   777  C  C    . MET   A 1 97  ? -19.411 15.856  1.536   1.00 41.25  ?  97  MET   A C    1 
ATOM   778  O  O    . MET   A 1 97  ? -18.952 16.937  1.158   1.00 43.92  ?  97  MET   A O    1 
ATOM   779  C  CB   . MET   A 1 97  ? -17.592 15.144  3.108   1.00 36.88  ?  97  MET   A CB   1 
ATOM   780  C  CG   . MET   A 1 97  ? -16.494 14.139  3.408   1.00 43.49  ?  97  MET   A CG   1 
ATOM   781  S  SD   . MET   A 1 97  ? -15.537 14.592  4.858   1.00 55.58  ?  97  MET   A SD   1 
ATOM   782  C  CE   . MET   A 1 97  ? -16.670 14.087  6.139   1.00 54.89  ?  97  MET   A CE   1 
ATOM   783  N  N    . ILE   A 1 98  ? -20.712 15.623  1.631   1.00 39.90  ?  98  ILE   A N    1 
ATOM   784  C  CA   . ILE   A 1 98  ? -21.685 16.574  1.124   1.00 37.46  ?  98  ILE   A CA   1 
ATOM   785  C  C    . ILE   A 1 98  ? -22.711 16.854  2.207   1.00 48.71  ?  98  ILE   A C    1 
ATOM   786  O  O    . ILE   A 1 98  ? -23.288 15.924  2.788   1.00 42.13  ?  98  ILE   A O    1 
ATOM   787  C  CB   . ILE   A 1 98  ? -22.357 16.068  -0.166  1.00 39.32  ?  98  ILE   A CB   1 
ATOM   788  C  CG1  . ILE   A 1 98  ? -21.292 15.869  -1.247  1.00 38.90  ?  98  ILE   A CG1  1 
ATOM   789  C  CG2  . ILE   A 1 98  ? -23.400 17.060  -0.643  1.00 38.14  ?  98  ILE   A CG2  1 
ATOM   790  C  CD1  . ILE   A 1 98  ? -21.693 14.917  -2.343  1.00 49.07  ?  98  ILE   A CD1  1 
ATOM   791  N  N    . SER   A 1 99  ? -22.896 18.138  2.501   1.00 45.62  ?  99  SER   A N    1 
ATOM   792  C  CA   . SER   A 1 99  ? -24.007 18.629  3.299   1.00 48.46  ?  99  SER   A CA   1 
ATOM   793  C  C    . SER   A 1 99  ? -24.979 19.336  2.367   1.00 44.78  ?  99  SER   A C    1 
ATOM   794  O  O    . SER   A 1 99  ? -24.626 20.339  1.738   1.00 45.64  ?  99  SER   A O    1 
ATOM   795  C  CB   . SER   A 1 99  ? -23.526 19.577  4.397   1.00 46.26  ?  99  SER   A CB   1 
ATOM   796  O  OG   . SER   A 1 99  ? -24.623 20.136  5.100   1.00 57.43  ?  99  SER   A OG   1 
ATOM   797  N  N    . TYR   A 1 100 ? -26.191 18.805  2.273   1.00 44.99  ?  100 TYR   A N    1 
ATOM   798  C  CA   . TYR   A 1 100 ? -27.246 19.423  1.473   1.00 38.55  ?  100 TYR   A CA   1 
ATOM   799  C  C    . TYR   A 1 100 ? -28.540 19.068  2.202   1.00 54.67  ?  100 TYR   A C    1 
ATOM   800  O  O    . TYR   A 1 100 ? -29.147 18.024  1.953   1.00 52.79  ?  100 TYR   A O    1 
ATOM   801  C  CB   . TYR   A 1 100 ? -27.215 18.905  0.041   1.00 44.51  ?  100 TYR   A CB   1 
ATOM   802  C  CG   . TYR   A 1 100 ? -28.139 19.602  -0.932  1.00 42.37  ?  100 TYR   A CG   1 
ATOM   803  C  CD1  . TYR   A 1 100 ? -27.956 20.939  -1.258  1.00 54.47  ?  100 TYR   A CD1  1 
ATOM   804  C  CD2  . TYR   A 1 100 ? -29.164 18.909  -1.563  1.00 50.73  ?  100 TYR   A CD2  1 
ATOM   805  C  CE1  . TYR   A 1 100 ? -28.788 21.575  -2.161  1.00 55.16  ?  100 TYR   A CE1  1 
ATOM   806  C  CE2  . TYR   A 1 100 ? -29.999 19.535  -2.468  1.00 53.97  ?  100 TYR   A CE2  1 
ATOM   807  C  CZ   . TYR   A 1 100 ? -29.807 20.868  -2.763  1.00 47.82  ?  100 TYR   A CZ   1 
ATOM   808  O  OH   . TYR   A 1 100 ? -30.636 21.496  -3.663  1.00 55.85  ?  100 TYR   A OH   1 
ATOM   809  N  N    . GLY   A 1 101 ? -28.926 19.923  3.141   1.00 53.54  ?  101 GLY   A N    1 
ATOM   810  C  CA   . GLY   A 1 101 ? -29.923 19.461  4.077   1.00 62.10  ?  101 GLY   A CA   1 
ATOM   811  C  C    . GLY   A 1 101 ? -29.228 18.509  5.026   1.00 70.45  ?  101 GLY   A C    1 
ATOM   812  O  O    . GLY   A 1 101 ? -28.542 18.929  5.964   1.00 61.19  ?  101 GLY   A O    1 
ATOM   813  N  N    . GLY   A 1 102 ? -29.404 17.214  4.781   1.00 61.77  ?  102 GLY   A N    1 
ATOM   814  C  CA   . GLY   A 1 102 ? -28.681 16.192  5.505   1.00 48.23  ?  102 GLY   A CA   1 
ATOM   815  C  C    . GLY   A 1 102 ? -27.191 16.223  5.193   1.00 50.41  ?  102 GLY   A C    1 
ATOM   816  O  O    . GLY   A 1 102 ? -26.658 17.159  4.596   1.00 45.60  ?  102 GLY   A O    1 
ATOM   817  N  N    . ALA   A 1 103 ? -26.508 15.160  5.615   1.00 43.39  ?  103 ALA   A N    1 
ATOM   818  C  CA   . ALA   A 1 103 ? -25.075 15.047  5.382   1.00 45.26  ?  103 ALA   A CA   1 
ATOM   819  C  C    . ALA   A 1 103 ? -24.698 13.591  5.159   1.00 41.66  ?  103 ALA   A C    1 
ATOM   820  O  O    . ALA   A 1 103 ? -25.301 12.682  5.736   1.00 44.48  ?  103 ALA   A O    1 
ATOM   821  C  CB   . ALA   A 1 103 ? -24.271 15.622  6.554   1.00 48.25  ?  103 ALA   A CB   1 
ATOM   822  N  N    . ASP   A 1 104 ? -23.689 13.381  4.317   1.00 45.96  ?  104 ASP   A N    1 
ATOM   823  C  CA   . ASP   A 1 104 ? -23.248 12.025  3.999   1.00 38.54  ?  104 ASP   A CA   1 
ATOM   824  C  C    . ASP   A 1 104 ? -21.871 12.114  3.356   1.00 38.10  ?  104 ASP   A C    1 
ATOM   825  O  O    . ASP   A 1 104 ? -21.418 13.197  2.983   1.00 39.33  ?  104 ASP   A O    1 
ATOM   826  C  CB   . ASP   A 1 104 ? -24.245 11.310  3.074   1.00 38.73  ?  104 ASP   A CB   1 
ATOM   827  C  CG   . ASP   A 1 104 ? -24.119 9.796   3.130   1.00 49.10  ?  104 ASP   A CG   1 
ATOM   828  O  OD1  . ASP   A 1 104 ? -23.275 9.290   3.900   1.00 51.85  ?  104 ASP   A OD1  1 
ATOM   829  O  OD2  . ASP   A 1 104 ? -24.871 9.111   2.404   1.00 51.95  ?  104 ASP   A OD2  1 
ATOM   830  N  N    . TYR   A 1 105 ? -21.183 10.976  3.286   1.00 43.09  ?  105 TYR   A N    1 
ATOM   831  C  CA   . TYR   A 1 105 ? -19.940 10.920  2.530   1.00 33.98  ?  105 TYR   A CA   1 
ATOM   832  C  C    . TYR   A 1 105 ? -19.750 9.514   1.984   1.00 42.17  ?  105 TYR   A C    1 
ATOM   833  O  O    . TYR   A 1 105 ? -20.324 8.545   2.487   1.00 40.66  ?  105 TYR   A O    1 
ATOM   834  C  CB   . TYR   A 1 105 ? -18.720 11.336  3.368   1.00 42.36  ?  105 TYR   A CB   1 
ATOM   835  C  CG   . TYR   A 1 105 ? -18.286 10.336  4.417   1.00 42.85  ?  105 TYR   A CG   1 
ATOM   836  C  CD1  . TYR   A 1 105 ? -17.487 9.248   4.081   1.00 48.93  ?  105 TYR   A CD1  1 
ATOM   837  C  CD2  . TYR   A 1 105 ? -18.644 10.495  5.746   1.00 55.52  ?  105 TYR   A CD2  1 
ATOM   838  C  CE1  . TYR   A 1 105 ? -17.083 8.336   5.035   1.00 64.87  ?  105 TYR   A CE1  1 
ATOM   839  C  CE2  . TYR   A 1 105 ? -18.239 9.590   6.708   1.00 54.87  ?  105 TYR   A CE2  1 
ATOM   840  C  CZ   . TYR   A 1 105 ? -17.461 8.513   6.346   1.00 51.44  ?  105 TYR   A CZ   1 
ATOM   841  O  OH   . TYR   A 1 105 ? -17.058 7.612   7.303   1.00 65.25  ?  105 TYR   A OH   1 
ATOM   842  N  N    . LYS   A 1 106 ? -18.931 9.421   0.941   1.00 39.06  ?  106 LYS   A N    1 
ATOM   843  C  CA   . LYS   A 1 106 ? -18.582 8.136   0.353   1.00 40.87  ?  106 LYS   A CA   1 
ATOM   844  C  C    . LYS   A 1 106 ? -17.086 8.061   0.075   1.00 38.93  ?  106 LYS   A C    1 
ATOM   845  O  O    . LYS   A 1 106 ? -16.412 9.083   -0.121  1.00 44.61  ?  106 LYS   A O    1 
ATOM   846  C  CB   . LYS   A 1 106 ? -19.374 7.871   -0.940  1.00 40.60  ?  106 LYS   A CB   1 
ATOM   847  C  CG   . LYS   A 1 106 ? -20.818 7.400   -0.715  1.00 42.57  ?  106 LYS   A CG   1 
ATOM   848  C  CD   . LYS   A 1 106 ? -20.907 6.248   0.280   1.00 33.94  ?  106 LYS   A CD   1 
ATOM   849  C  CE   . LYS   A 1 106 ? -22.348 5.776   0.462   1.00 61.79  ?  106 LYS   A CE   1 
ATOM   850  N  NZ   . LYS   A 1 106 ? -23.151 6.685   1.329   1.00 57.21  ?  106 LYS   A NZ   1 
ATOM   851  N  N    . ARG   A 1 107 ? -16.588 6.823   0.048   1.00 38.37  ?  107 ARG   A N    1 
ATOM   852  C  CA   . ARG   A 1 107 ? -15.187 6.504   -0.193  1.00 39.90  ?  107 ARG   A CA   1 
ATOM   853  C  C    . ARG   A 1 107 ? -14.987 6.028   -1.628  1.00 36.43  ?  107 ARG   A C    1 
ATOM   854  O  O    . ARG   A 1 107 ? -15.818 5.295   -2.172  1.00 36.57  ?  107 ARG   A O    1 
ATOM   855  C  CB   . ARG   A 1 107 ? -14.715 5.414   0.772   1.00 47.26  ?  107 ARG   A CB   1 
ATOM   856  C  CG   . ARG   A 1 107 ? -14.664 5.836   2.228   1.00 61.12  ?  107 ARG   A CG   1 
ATOM   857  C  CD   . ARG   A 1 107 ? -13.933 4.799   3.066   1.00 68.96  ?  107 ARG   A CD   1 
ATOM   858  N  NE   . ARG   A 1 107 ? -13.760 3.535   2.359   1.00 73.12  ?  107 ARG   A NE   1 
ATOM   859  N  N    . ILE   A 1 108 ? -13.873 6.440   -2.230  1.00 35.88  ?  108 ILE   A N    1 
ATOM   860  C  CA   . ILE   A 1 108 ? -13.477 6.029   -3.575  1.00 35.75  ?  108 ILE   A CA   1 
ATOM   861  C  C    . ILE   A 1 108 ? -12.001 5.655   -3.544  1.00 34.11  ?  108 ILE   A C    1 
ATOM   862  O  O    . ILE   A 1 108 ? -11.165 6.467   -3.139  1.00 36.50  ?  108 ILE   A O    1 
ATOM   863  C  CB   . ILE   A 1 108 ? -13.718 7.141   -4.611  1.00 36.30  ?  108 ILE   A CB   1 
ATOM   864  C  CG1  . ILE   A 1 108 ? -15.186 7.572   -4.614  1.00 37.21  ?  108 ILE   A CG1  1 
ATOM   865  C  CG2  . ILE   A 1 108 ? -13.270 6.692   -5.996  1.00 36.17  ?  108 ILE   A CG2  1 
ATOM   866  C  CD1  . ILE   A 1 108 ? -15.428 8.886   -5.335  1.00 48.50  ?  108 ILE   A CD1  1 
ATOM   867  N  N    . THR   A 1 109 ? -11.674 4.444   -3.982  1.00 35.05  ?  109 THR   A N    1 
ATOM   868  C  CA   . THR   A 1 109 ? -10.280 4.024   -4.073  1.00 34.28  ?  109 THR   A CA   1 
ATOM   869  C  C    . THR   A 1 109 ? -9.716  4.376   -5.444  1.00 38.95  ?  109 THR   A C    1 
ATOM   870  O  O    . THR   A 1 109 ? -10.315 4.046   -6.473  1.00 37.01  ?  109 THR   A O    1 
ATOM   871  C  CB   . THR   A 1 109 ? -10.138 2.525   -3.817  1.00 45.65  ?  109 THR   A CB   1 
ATOM   872  O  OG1  . THR   A 1 109 ? -10.650 2.212   -2.516  1.00 42.24  ?  109 THR   A OG1  1 
ATOM   873  C  CG2  . THR   A 1 109 ? -8.674  2.114   -3.894  1.00 39.48  ?  109 THR   A CG2  1 
ATOM   874  N  N    . VAL   A 1 110 ? -8.557  5.032   -5.455  1.00 32.78  ?  110 VAL   A N    1 
ATOM   875  C  CA   . VAL   A 1 110 ? -7.844  5.378   -6.677  1.00 37.97  ?  110 VAL   A CA   1 
ATOM   876  C  C    . VAL   A 1 110 ? -6.531  4.609   -6.683  1.00 42.06  ?  110 VAL   A C    1 
ATOM   877  O  O    . VAL   A 1 110 ? -5.727  4.726   -5.747  1.00 36.06  ?  110 VAL   A O    1 
ATOM   878  C  CB   . VAL   A 1 110 ? -7.590  6.890   -6.780  1.00 39.10  ?  110 VAL   A CB   1 
ATOM   879  C  CG1  . VAL   A 1 110 ? -6.709  7.199   -7.983  1.00 44.45  ?  110 VAL   A CG1  1 
ATOM   880  C  CG2  . VAL   A 1 110 ? -8.904  7.651   -6.864  1.00 40.32  ?  110 VAL   A CG2  1 
ATOM   881  N  N    . LYS   A 1 111 ? -6.321  3.826   -7.737  1.00 31.42  ?  111 LYS   A N    1 
ATOM   882  C  CA   . LYS   A 1 111 ? -5.081  3.106   -7.979  1.00 37.20  ?  111 LYS   A CA   1 
ATOM   883  C  C    . LYS   A 1 111 ? -4.402  3.705   -9.204  1.00 41.24  ?  111 LYS   A C    1 
ATOM   884  O  O    . LYS   A 1 111 ? -5.069  4.053   -10.183 1.00 37.79  ?  111 LYS   A O    1 
ATOM   885  C  CB   . LYS   A 1 111 ? -5.353  1.614   -8.190  1.00 36.64  ?  111 LYS   A CB   1 
ATOM   886  C  CG   . LYS   A 1 111 ? -4.107  0.755   -8.287  1.00 69.41  ?  111 LYS   A CG   1 
ATOM   887  N  N    . VAL   A 1 112 ? -3.079  3.836   -9.150  1.00 35.84  ?  112 VAL   A N    1 
ATOM   888  C  CA   . VAL   A 1 112 ? -2.320  4.483   -10.216 1.00 33.19  ?  112 VAL   A CA   1 
ATOM   889  C  C    . VAL   A 1 112 ? -1.321  3.489   -10.796 1.00 48.08  ?  112 VAL   A C    1 
ATOM   890  O  O    . VAL   A 1 112 ? -0.453  2.980   -10.076 1.00 33.90  ?  112 VAL   A O    1 
ATOM   891  C  CB   . VAL   A 1 112 ? -1.602  5.746   -9.713  1.00 33.09  ?  112 VAL   A CB   1 
ATOM   892  C  CG1  . VAL   A 1 112 ? -0.793  6.375   -10.834 1.00 41.84  ?  112 VAL   A CG1  1 
ATOM   893  C  CG2  . VAL   A 1 112 ? -2.611  6.739   -9.150  1.00 32.42  ?  112 VAL   A CG2  1 
ATOM   894  N  N    . ASN   A 1 113 ? -1.442  3.224   -12.097 1.00 37.43  ?  113 ASN   A N    1 
ATOM   895  C  CA   . ASN   A 1 113 ? -0.401  2.525   -12.841 1.00 36.05  ?  113 ASN   A CA   1 
ATOM   896  C  C    . ASN   A 1 113 ? 0.645   3.526   -13.311 1.00 38.49  ?  113 ASN   A C    1 
ATOM   897  O  O    . ASN   A 1 113 ? 0.315   4.647   -13.708 1.00 43.81  ?  113 ASN   A O    1 
ATOM   898  C  CB   . ASN   A 1 113 ? -0.980  1.794   -14.055 1.00 40.92  ?  113 ASN   A CB   1 
ATOM   899  C  CG   . ASN   A 1 113 ? -1.931  0.678   -13.679 1.00 44.36  ?  113 ASN   A CG   1 
ATOM   900  O  OD1  . ASN   A 1 113 ? -1.681  -0.085  -12.747 1.00 41.93  ?  113 ASN   A OD1  1 
ATOM   901  N  ND2  . ASN   A 1 113 ? -3.019  0.556   -14.433 1.00 39.76  ?  113 ASN   A ND2  1 
ATOM   902  N  N    . ALA   A 1 114 ? 1.912   3.121   -13.266 1.00 37.93  ?  114 ALA   A N    1 
ATOM   903  C  CA   . ALA   A 1 114 ? 2.986   3.990   -13.723 1.00 41.44  ?  114 ALA   A CA   1 
ATOM   904  C  C    . ALA   A 1 114 ? 4.124   3.147   -14.276 1.00 42.03  ?  114 ALA   A C    1 
ATOM   905  O  O    . ALA   A 1 114 ? 4.400   2.060   -13.754 1.00 48.50  ?  114 ALA   A O    1 
ATOM   906  C  CB   . ALA   A 1 114 ? 3.500   4.888   -12.588 1.00 41.65  ?  114 ALA   A CB   1 
ATOM   907  N  N    . PRO   A 1 115 ? 4.803   3.620   -15.318 1.00 47.51  ?  115 PRO   A N    1 
ATOM   908  C  CA   . PRO   A 1 115 ? 5.969   2.899   -15.843 1.00 53.86  ?  115 PRO   A CA   1 
ATOM   909  C  C    . PRO   A 1 115 ? 7.143   2.947   -14.875 1.00 40.60  ?  115 PRO   A C    1 
ATOM   910  O  O    . PRO   A 1 115 ? 7.169   3.701   -13.901 1.00 43.84  ?  115 PRO   A O    1 
ATOM   911  C  CB   . PRO   A 1 115 ? 6.289   3.624   -17.155 1.00 46.32  ?  115 PRO   A CB   1 
ATOM   912  C  CG   . PRO   A 1 115 ? 5.048   4.395   -17.491 1.00 43.98  ?  115 PRO   A CG   1 
ATOM   913  C  CD   . PRO   A 1 115 ? 4.421   4.751   -16.178 1.00 43.54  ?  115 PRO   A CD   1 
ATOM   914  N  N    . TYR   A 1 116 ? 8.138   2.111   -15.180 1.00 48.91  ?  116 TYR   A N    1 
ATOM   915  C  CA   . TYR   A 1 116 ? 9.310   1.975   -14.320 1.00 44.87  ?  116 TYR   A CA   1 
ATOM   916  C  C    . TYR   A 1 116 ? 9.921   3.317   -13.933 1.00 42.79  ?  116 TYR   A C    1 
ATOM   917  O  O    . TYR   A 1 116 ? 10.248  3.534   -12.766 1.00 40.34  ?  116 TYR   A O    1 
ATOM   918  C  CB   . TYR   A 1 116 ? 10.367  1.102   -14.993 1.00 46.70  ?  116 TYR   A CB   1 
ATOM   919  C  CG   . TYR   A 1 116 ? 11.581  0.908   -14.117 1.00 49.67  ?  116 TYR   A CG   1 
ATOM   920  C  CD1  . TYR   A 1 116 ? 11.518  0.127   -12.969 1.00 39.17  ?  116 TYR   A CD1  1 
ATOM   921  C  CD2  . TYR   A 1 116 ? 12.783  1.534   -14.417 1.00 52.25  ?  116 TYR   A CD2  1 
ATOM   922  C  CE1  . TYR   A 1 116 ? 12.623  -0.042  -12.159 1.00 48.41  ?  116 TYR   A CE1  1 
ATOM   923  C  CE2  . TYR   A 1 116 ? 13.894  1.372   -13.611 1.00 55.33  ?  116 TYR   A CE2  1 
ATOM   924  C  CZ   . TYR   A 1 116 ? 13.808  0.582   -12.484 1.00 44.17  ?  116 TYR   A CZ   1 
ATOM   925  O  OH   . TYR   A 1 116 ? 14.910  0.415   -11.677 1.00 50.83  ?  116 TYR   A OH   1 
ATOM   926  N  N    . ALA   A 1 117 ? 10.140  4.213   -14.898 1.00 38.79  ?  117 ALA   A N    1 
ATOM   927  C  CA   . ALA   A 1 117 ? 10.876  5.440   -14.590 1.00 55.02  ?  117 ALA   A CA   1 
ATOM   928  C  C    . ALA   A 1 117 ? 10.161  6.269   -13.524 1.00 42.56  ?  117 ALA   A C    1 
ATOM   929  O  O    . ALA   A 1 117 ? 10.778  6.727   -12.548 1.00 52.26  ?  117 ALA   A O    1 
ATOM   930  C  CB   . ALA   A 1 117 ? 11.080  6.259   -15.865 1.00 54.50  ?  117 ALA   A CB   1 
ATOM   931  N  N    . ALA   A 1 118 ? 8.847   6.443   -13.676 1.00 46.72  ?  118 ALA   A N    1 
ATOM   932  C  CA   . ALA   A 1 118 ? 8.088   7.220   -12.703 1.00 55.22  ?  118 ALA   A CA   1 
ATOM   933  C  C    . ALA   A 1 118 ? 8.105   6.545   -11.339 1.00 40.60  ?  118 ALA   A C    1 
ATOM   934  O  O    . ALA   A 1 118 ? 8.404   7.182   -10.322 1.00 49.21  ?  118 ALA   A O    1 
ATOM   935  C  CB   . ALA   A 1 118 ? 6.654   7.419   -13.196 1.00 44.54  ?  118 ALA   A CB   1 
ATOM   936  N  N    . HIS   A 1 119 ? 7.785   5.249   -11.299 1.00 38.51  ?  119 HIS   A N    1 
ATOM   937  C  CA   . HIS   A 1 119 ? 7.823   4.511   -10.042 1.00 40.68  ?  119 HIS   A CA   1 
ATOM   938  C  C    . HIS   A 1 119 ? 9.189   4.642   -9.392  1.00 47.05  ?  119 HIS   A C    1 
ATOM   939  O  O    . HIS   A 1 119 ? 9.311   4.716   -8.164  1.00 45.36  ?  119 HIS   A O    1 
ATOM   940  C  CB   . HIS   A 1 119 ? 7.504   3.038   -10.300 1.00 45.22  ?  119 HIS   A CB   1 
ATOM   941  C  CG   . HIS   A 1 119 ? 6.062   2.689   -10.119 1.00 85.58  ?  119 HIS   A CG   1 
ATOM   942  N  ND1  . HIS   A 1 119 ? 5.268   2.258   -11.160 1.00 70.74  ?  119 HIS   A ND1  1 
ATOM   943  C  CD2  . HIS   A 1 119 ? 5.270   2.704   -9.022  1.00 73.80  ?  119 HIS   A CD2  1 
ATOM   944  C  CE1  . HIS   A 1 119 ? 4.048   2.024   -10.712 1.00 54.95  ?  119 HIS   A CE1  1 
ATOM   945  N  NE2  . HIS   A 1 119 ? 4.022   2.286   -9.417  1.00 82.69  ?  119 HIS   A NE2  1 
ATOM   946  N  N    . HIS   A 1 120 ? 10.229  4.674   -10.220 1.00 46.32  ?  120 HIS   A N    1 
ATOM   947  C  CA   . HIS   A 1 120 ? 11.596  4.752   -9.738  1.00 42.60  ?  120 HIS   A CA   1 
ATOM   948  C  C    . HIS   A 1 120 ? 11.811  6.070   -9.015  1.00 48.80  ?  120 HIS   A C    1 
ATOM   949  O  O    . HIS   A 1 120 ? 12.394  6.113   -7.925  1.00 52.69  ?  120 HIS   A O    1 
ATOM   950  C  CB   . HIS   A 1 120 ? 12.545  4.625   -10.926 1.00 53.16  ?  120 HIS   A CB   1 
ATOM   951  C  CG   . HIS   A 1 120 ? 13.985  4.519   -10.549 1.00 55.05  ?  120 HIS   A CG   1 
ATOM   952  N  ND1  . HIS   A 1 120 ? 14.996  4.563   -11.483 1.00 68.64  ?  120 HIS   A ND1  1 
ATOM   953  C  CD2  . HIS   A 1 120 ? 14.575  4.221   -9.368  1.00 63.14  ?  120 HIS   A CD2  1 
ATOM   954  C  CE1  . HIS   A 1 120 ? 16.156  4.385   -10.877 1.00 97.43  ?  120 HIS   A CE1  1 
ATOM   955  N  NE2  . HIS   A 1 120 ? 15.927  4.171   -9.595  1.00 103.37 ?  120 HIS   A NE2  1 
ATOM   956  N  N    . HIS   A 1 121 ? 11.339  7.165   -9.617  1.00 48.96  ?  121 HIS   A N    1 
ATOM   957  C  CA   . HIS   A 1 121 ? 11.432  8.453   -8.938  1.00 59.09  ?  121 HIS   A CA   1 
ATOM   958  C  C    . HIS   A 1 121 ? 10.636  8.436   -7.640  1.00 59.69  ?  121 HIS   A C    1 
ATOM   959  O  O    . HIS   A 1 121 ? 11.057  9.017   -6.632  1.00 70.59  ?  121 HIS   A O    1 
ATOM   960  C  CB   . HIS   A 1 121 ? 10.936  9.577   -9.845  1.00 66.25  ?  121 HIS   A CB   1 
ATOM   961  C  CG   . HIS   A 1 121 ? 11.100  10.940  -9.249  1.00 78.95  ?  121 HIS   A CG   1 
ATOM   962  N  ND1  . HIS   A 1 121 ? 12.263  11.344  -8.628  1.00 94.42  ?  121 HIS   A ND1  1 
ATOM   963  C  CD2  . HIS   A 1 121 ? 10.240  11.981  -9.150  1.00 86.48  ?  121 HIS   A CD2  1 
ATOM   964  C  CE1  . HIS   A 1 121 ? 12.118  12.581  -8.188  1.00 95.44  ?  121 HIS   A CE1  1 
ATOM   965  N  NE2  . HIS   A 1 121 ? 10.899  12.990  -8.490  1.00 100.10 ?  121 HIS   A NE2  1 
ATOM   966  N  N    . HIS   A 1 122 ? 9.478   7.773   -7.649  1.00 57.32  ?  122 HIS   A N    1 
ATOM   967  C  CA   . HIS   A 1 122 ? 8.651   7.670   -6.452  1.00 61.98  ?  122 HIS   A CA   1 
ATOM   968  C  C    . HIS   A 1 122 ? 9.318   6.806   -5.387  1.00 72.95  ?  122 HIS   A C    1 
ATOM   969  O  O    . HIS   A 1 122 ? 9.112   7.026   -4.188  1.00 61.83  ?  122 HIS   A O    1 
ATOM   970  C  CB   . HIS   A 1 122 ? 7.285   7.100   -6.837  1.00 66.73  ?  122 HIS   A CB   1 
ATOM   971  C  CG   . HIS   A 1 122 ? 6.268   7.140   -5.740  1.00 64.45  ?  122 HIS   A CG   1 
ATOM   972  N  ND1  . HIS   A 1 122 ? 5.915   8.306   -5.095  1.00 61.30  ?  122 HIS   A ND1  1 
ATOM   973  C  CD2  . HIS   A 1 122 ? 5.508   6.162   -5.193  1.00 56.11  ?  122 HIS   A CD2  1 
ATOM   974  C  CE1  . HIS   A 1 122 ? 4.989   8.042   -4.190  1.00 65.84  ?  122 HIS   A CE1  1 
ATOM   975  N  NE2  . HIS   A 1 122 ? 4.725   6.749   -4.228  1.00 64.53  ?  122 HIS   A NE2  1 
ATOM   976  N  N    . HIS   A 1 123 ? 10.115  5.822   -5.812  1.00 60.03  ?  123 HIS   A N    1 
ATOM   977  C  CA   . HIS   A 1 123 ? 10.777  4.919   -4.877  1.00 62.15  ?  123 HIS   A CA   1 
ATOM   978  C  C    . HIS   A 1 123 ? 11.911  5.628   -4.148  1.00 72.67  ?  123 HIS   A C    1 
ATOM   979  O  O    . HIS   A 1 123 ? 12.137  5.391   -2.955  1.00 62.21  ?  123 HIS   A O    1 
ATOM   980  C  CB   . HIS   A 1 123 ? 11.292  3.698   -5.643  1.00 65.14  ?  123 HIS   A CB   1 
ATOM   981  C  CG   . HIS   A 1 123 ? 11.686  2.542   -4.776  1.00 63.18  ?  123 HIS   A CG   1 
ATOM   982  N  ND1  . HIS   A 1 123 ? 12.927  1.946   -4.853  1.00 67.01  ?  123 HIS   A ND1  1 
ATOM   983  C  CD2  . HIS   A 1 123 ? 10.993  1.849   -3.842  1.00 54.61  ?  123 HIS   A CD2  1 
ATOM   984  C  CE1  . HIS   A 1 123 ? 12.987  0.945   -3.993  1.00 65.80  ?  123 HIS   A CE1  1 
ATOM   985  N  NE2  . HIS   A 1 123 ? 11.827  0.866   -3.366  1.00 66.25  ?  123 HIS   A NE2  1 
ATOM   986  N  N    . HIS   A 1 124 ? 12.638  6.503   -4.851  1.00 86.33  ?  124 HIS   A N    1 
ATOM   987  C  CA   . HIS   A 1 124 ? 13.688  7.281   -4.202  1.00 92.60  ?  124 HIS   A CA   1 
ATOM   988  C  C    . HIS   A 1 124 ? 13.153  8.443   -3.385  1.00 103.67 ?  124 HIS   A C    1 
ATOM   989  O  O    . HIS   A 1 124 ? 13.770  8.815   -2.382  1.00 111.90 ?  124 HIS   A O    1 
ATOM   990  C  CB   . HIS   A 1 124 ? 14.693  7.831   -5.212  1.00 85.54  ?  124 HIS   A CB   1 
ATOM   991  C  CG   . HIS   A 1 124 ? 15.396  6.779   -5.998  1.00 93.85  ?  124 HIS   A CG   1 
ATOM   992  N  ND1  . HIS   A 1 124 ? 16.122  7.061   -7.133  1.00 92.80  ?  124 HIS   A ND1  1 
ATOM   993  C  CD2  . HIS   A 1 124 ? 15.476  5.441   -5.818  1.00 91.28  ?  124 HIS   A CD2  1 
ATOM   994  C  CE1  . HIS   A 1 124 ? 16.639  5.944   -7.607  1.00 97.86  ?  124 HIS   A CE1  1 
ATOM   995  N  NE2  . HIS   A 1 124 ? 16.260  4.945   -6.830  1.00 98.91  ?  124 HIS   A NE2  1 
ATOM   996  N  N    . ALA   A 1 125 ? 12.058  9.065   -3.818  1.00 101.95 ?  125 ALA   A N    1 
ATOM   997  C  CA   . ALA   A 1 125 ? 11.496  10.171  -3.055  1.00 109.76 ?  125 ALA   A CA   1 
ATOM   998  C  C    . ALA   A 1 125 ? 11.058  9.701   -1.674  1.00 119.14 ?  125 ALA   A C    1 
ATOM   999  O  O    . ALA   A 1 125 ? 11.522  10.212  -0.648  1.00 137.26 ?  125 ALA   A O    1 
ATOM   1000 C  CB   . ALA   A 1 125 ? 10.327  10.787  -3.823  1.00 109.15 ?  125 ALA   A CB   1 
ATOM   1001 N  N    . ALA   A 1 126 ? 10.179  8.705   -1.631  1.00 118.23 ?  126 ALA   A N    1 
ATOM   1002 C  CA   . ALA   A 1 126 ? 9.721   8.143   -0.368  1.00 128.69 ?  126 ALA   A CA   1 
ATOM   1003 C  C    . ALA   A 1 126 ? 10.805  7.267   0.252   1.00 125.27 ?  126 ALA   A C    1 
ATOM   1004 O  O    . ALA   A 1 126 ? 11.285  7.541   1.352   1.00 111.43 ?  126 ALA   A O    1 
ATOM   1005 C  CB   . ALA   A 1 126 ? 8.443   7.345   -0.572  1.00 120.26 ?  126 ALA   A CB   1 
ATOM   1006 N  N    . PHE   B 1 1   ? -17.188 28.424  10.425  1.00 57.86  ?  1   PHE   B N    1 
ATOM   1007 C  CA   . PHE   B 1 1   ? -17.605 27.343  11.311  1.00 69.10  ?  1   PHE   B CA   1 
ATOM   1008 C  C    . PHE   B 1 1   ? -16.432 26.421  11.612  1.00 63.96  ?  1   PHE   B C    1 
ATOM   1009 O  O    . PHE   B 1 1   ? -15.793 25.909  10.694  1.00 68.77  ?  1   PHE   B O    1 
ATOM   1010 C  CB   . PHE   B 1 1   ? -18.744 26.537  10.694  1.00 53.99  ?  1   PHE   B CB   1 
ATOM   1011 C  CG   . PHE   B 1 1   ? -19.213 25.408  11.561  1.00 65.73  ?  1   PHE   B CG   1 
ATOM   1012 C  CD1  . PHE   B 1 1   ? -19.977 25.661  12.687  1.00 58.38  ?  1   PHE   B CD1  1 
ATOM   1013 C  CD2  . PHE   B 1 1   ? -18.857 24.101  11.276  1.00 43.63  ?  1   PHE   B CD2  1 
ATOM   1014 C  CE1  . PHE   B 1 1   ? -20.406 24.630  13.496  1.00 62.02  ?  1   PHE   B CE1  1 
ATOM   1015 C  CE2  . PHE   B 1 1   ? -19.280 23.063  12.085  1.00 45.02  ?  1   PHE   B CE2  1 
ATOM   1016 C  CZ   . PHE   B 1 1   ? -20.056 23.329  13.197  1.00 48.96  ?  1   PHE   B CZ   1 
ATOM   1017 N  N    . THR   B 1 2   ? -16.155 26.188  12.893  1.00 59.26  ?  2   THR   B N    1 
ATOM   1018 C  CA   . THR   B 1 2   ? -14.979 25.425  13.287  1.00 55.60  ?  2   THR   B CA   1 
ATOM   1019 C  C    . THR   B 1 2   ? -15.325 24.408  14.361  1.00 54.64  ?  2   THR   B C    1 
ATOM   1020 O  O    . THR   B 1 2   ? -15.946 24.748  15.374  1.00 64.06  ?  2   THR   B O    1 
ATOM   1021 C  CB   . THR   B 1 2   ? -13.865 26.342  13.801  1.00 61.20  ?  2   THR   B CB   1 
ATOM   1022 O  OG1  . THR   B 1 2   ? -13.699 27.446  12.904  1.00 63.25  ?  2   THR   B OG1  1 
ATOM   1023 C  CG2  . THR   B 1 2   ? -12.557 25.573  13.904  1.00 57.91  ?  2   THR   B CG2  1 
ATOM   1024 N  N    . VAL   B 1 3   ? -14.917 23.171  14.131  1.00 46.95  ?  3   VAL   B N    1 
ATOM   1025 C  CA   . VAL   B 1 3   ? -14.897 22.136  15.154  1.00 45.95  ?  3   VAL   B CA   1 
ATOM   1026 C  C    . VAL   B 1 3   ? -13.514 22.145  15.784  1.00 62.73  ?  3   VAL   B C    1 
ATOM   1027 O  O    . VAL   B 1 3   ? -12.500 22.232  15.080  1.00 47.82  ?  3   VAL   B O    1 
ATOM   1028 C  CB   . VAL   B 1 3   ? -15.230 20.757  14.554  1.00 51.42  ?  3   VAL   B CB   1 
ATOM   1029 C  CG1  . VAL   B 1 3   ? -14.955 19.654  15.566  1.00 50.90  ?  3   VAL   B CG1  1 
ATOM   1030 C  CG2  . VAL   B 1 3   ? -16.675 20.715  14.083  1.00 45.18  ?  3   VAL   B CG2  1 
ATOM   1031 N  N    . THR   B 1 4   ? -13.461 22.070  17.110  1.00 53.69  ?  4   THR   B N    1 
ATOM   1032 C  CA   . THR   B 1 4   ? -12.194 22.033  17.820  1.00 60.74  ?  4   THR   B CA   1 
ATOM   1033 C  C    . THR   B 1 4   ? -12.182 20.859  18.785  1.00 50.87  ?  4   THR   B C    1 
ATOM   1034 O  O    . THR   B 1 4   ? -13.225 20.438  19.292  1.00 61.77  ?  4   THR   B O    1 
ATOM   1035 C  CB   . THR   B 1 4   ? -11.936 23.336  18.595  1.00 67.64  ?  4   THR   B CB   1 
ATOM   1036 O  OG1  . THR   B 1 4   ? -13.061 23.626  19.434  1.00 77.81  ?  4   THR   B OG1  1 
ATOM   1037 C  CG2  . THR   B 1 4   ? -11.708 24.496  17.637  1.00 56.53  ?  4   THR   B CG2  1 
ATOM   1038 N  N    . VAL   B 1 5   ? -10.990 20.326  19.023  1.00 52.03  ?  5   VAL   B N    1 
ATOM   1039 C  CA   . VAL   B 1 5   ? -10.773 19.275  20.006  1.00 61.11  ?  5   VAL   B CA   1 
ATOM   1040 C  C    . VAL   B 1 5   ? -9.778  19.793  21.037  1.00 57.18  ?  5   VAL   B C    1 
ATOM   1041 O  O    . VAL   B 1 5   ? -8.681  20.225  20.673  1.00 51.18  ?  5   VAL   B O    1 
ATOM   1042 C  CB   . VAL   B 1 5   ? -10.264 17.975  19.362  1.00 64.08  ?  5   VAL   B CB   1 
ATOM   1043 C  CG1  . VAL   B 1 5   ? -11.386 17.286  18.598  1.00 52.21  ?  5   VAL   B CG1  1 
ATOM   1044 C  CG2  . VAL   B 1 5   ? -9.092  18.268  18.440  1.00 46.36  ?  5   VAL   B CG2  1 
ATOM   1045 N  N    . PRO   B 1 6   ? -10.115 19.789  22.328  1.00 54.82  ?  6   PRO   B N    1 
ATOM   1046 C  CA   . PRO   B 1 6   ? -9.115  20.155  23.344  1.00 52.73  ?  6   PRO   B CA   1 
ATOM   1047 C  C    . PRO   B 1 6   ? -7.926  19.213  23.374  1.00 45.67  ?  6   PRO   B C    1 
ATOM   1048 O  O    . PRO   B 1 6   ? -6.796  19.654  23.619  1.00 59.53  ?  6   PRO   B O    1 
ATOM   1049 C  CB   . PRO   B 1 6   ? -9.911  20.107  24.654  1.00 46.46  ?  6   PRO   B CB   1 
ATOM   1050 C  CG   . PRO   B 1 6   ? -11.030 19.166  24.381  1.00 50.68  ?  6   PRO   B CG   1 
ATOM   1051 C  CD   . PRO   B 1 6   ? -11.380 19.333  22.928  1.00 57.69  ?  6   PRO   B CD   1 
ATOM   1052 N  N    . LYS   B 1 7   ? -8.148  17.928  23.106  1.00 44.32  ?  7   LYS   B N    1 
ATOM   1053 C  CA   . LYS   B 1 7   ? -7.089  16.934  23.032  1.00 46.58  ?  7   LYS   B CA   1 
ATOM   1054 C  C    . LYS   B 1 7   ? -7.250  16.140  21.748  1.00 52.25  ?  7   LYS   B C    1 
ATOM   1055 O  O    . LYS   B 1 7   ? -8.346  15.658  21.448  1.00 50.12  ?  7   LYS   B O    1 
ATOM   1056 C  CB   . LYS   B 1 7   ? -7.151  15.958  24.217  1.00 53.66  ?  7   LYS   B CB   1 
ATOM   1057 C  CG   . LYS   B 1 7   ? -6.742  16.498  25.573  1.00 44.68  ?  7   LYS   B CG   1 
ATOM   1058 C  CD   . LYS   B 1 7   ? -6.812  15.385  26.619  1.00 60.38  ?  7   LYS   B CD   1 
ATOM   1059 C  CE   . LYS   B 1 7   ? -5.816  14.268  26.330  1.00 67.20  ?  7   LYS   B CE   1 
ATOM   1060 N  NZ   . LYS   B 1 7   ? -6.212  12.972  26.962  1.00 59.51  ?  7   LYS   B NZ   1 
ATOM   1061 N  N    . ASP   B 1 8   ? -6.163  16.006  20.995  1.00 45.29  ?  8   ASP   B N    1 
ATOM   1062 C  CA   . ASP   B 1 8   ? -6.156  15.161  19.813  1.00 47.05  ?  8   ASP   B CA   1 
ATOM   1063 C  C    . ASP   B 1 8   ? -5.439  13.845  20.070  1.00 40.48  ?  8   ASP   B C    1 
ATOM   1064 O  O    . ASP   B 1 8   ? -5.235  13.065  19.135  1.00 36.49  ?  8   ASP   B O    1 
ATOM   1065 C  CB   . ASP   B 1 8   ? -5.535  15.896  18.622  1.00 49.88  ?  8   ASP   B CB   1 
ATOM   1066 C  CG   . ASP   B 1 8   ? -4.073  16.234  18.833  1.00 52.66  ?  8   ASP   B CG   1 
ATOM   1067 O  OD1  . ASP   B 1 8   ? -3.534  15.934  19.918  1.00 51.98  ?  8   ASP   B OD1  1 
ATOM   1068 O  OD2  . ASP   B 1 8   ? -3.461  16.801  17.902  1.00 61.46  ?  8   ASP   B OD2  1 
ATOM   1069 N  N    . LEU   B 1 9   ? -5.049  13.587  21.319  1.00 36.78  ?  9   LEU   B N    1 
ATOM   1070 C  CA   . LEU   B 1 9   ? -4.449  12.319  21.703  1.00 34.35  ?  9   LEU   B CA   1 
ATOM   1071 C  C    . LEU   B 1 9   ? -4.985  11.878  23.055  1.00 38.48  ?  9   LEU   B C    1 
ATOM   1072 O  O    . LEU   B 1 9   ? -5.014  12.665  24.007  1.00 36.83  ?  9   LEU   B O    1 
ATOM   1073 C  CB   . LEU   B 1 9   ? -2.921  12.422  21.748  1.00 32.10  ?  9   LEU   B CB   1 
ATOM   1074 C  CG   . LEU   B 1 9   ? -2.205  11.116  22.089  1.00 38.28  ?  9   LEU   B CG   1 
ATOM   1075 C  CD1  . LEU   B 1 9   ? -2.159  10.208  20.874  1.00 45.54  ?  9   LEU   B CD1  1 
ATOM   1076 C  CD2  . LEU   B 1 9   ? -0.800  11.404  22.590  1.00 49.11  ?  9   LEU   B CD2  1 
ATOM   1077 N  N    . TYR   B 1 10  ? -5.403  10.618  23.131  1.00 35.48  ?  10  TYR   B N    1 
ATOM   1078 C  CA   . TYR   B 1 10  ? -5.849  9.985   24.363  1.00 39.21  ?  10  TYR   B CA   1 
ATOM   1079 C  C    . TYR   B 1 10  ? -5.101  8.672   24.526  1.00 34.62  ?  10  TYR   B C    1 
ATOM   1080 O  O    . TYR   B 1 10  ? -4.966  7.909   23.565  1.00 40.98  ?  10  TYR   B O    1 
ATOM   1081 C  CB   . TYR   B 1 10  ? -7.358  9.712   24.339  1.00 34.10  ?  10  TYR   B CB   1 
ATOM   1082 C  CG   . TYR   B 1 10  ? -8.233  10.942  24.414  1.00 34.79  ?  10  TYR   B CG   1 
ATOM   1083 C  CD1  . TYR   B 1 10  ? -8.426  11.745  23.298  1.00 33.41  ?  10  TYR   B CD1  1 
ATOM   1084 C  CD2  . TYR   B 1 10  ? -8.895  11.280  25.586  1.00 44.22  ?  10  TYR   B CD2  1 
ATOM   1085 C  CE1  . TYR   B 1 10  ? -9.233  12.864  23.353  1.00 41.32  ?  10  TYR   B CE1  1 
ATOM   1086 C  CE2  . TYR   B 1 10  ? -9.708  12.397  25.651  1.00 42.18  ?  10  TYR   B CE2  1 
ATOM   1087 C  CZ   . TYR   B 1 10  ? -9.873  13.185  24.532  1.00 43.95  ?  10  TYR   B CZ   1 
ATOM   1088 O  OH   . TYR   B 1 10  ? -10.680 14.298  24.593  1.00 41.92  ?  10  TYR   B OH   1 
ATOM   1089 N  N    . VAL   B 1 11  ? -4.608  8.411   25.732  1.00 31.09  ?  11  VAL   B N    1 
ATOM   1090 C  CA   . VAL   B 1 11  ? -3.965  7.142   26.055  1.00 31.51  ?  11  VAL   B CA   1 
ATOM   1091 C  C    . VAL   B 1 11  ? -4.815  6.485   27.130  1.00 42.87  ?  11  VAL   B C    1 
ATOM   1092 O  O    . VAL   B 1 11  ? -4.887  6.982   28.262  1.00 39.09  ?  11  VAL   B O    1 
ATOM   1093 C  CB   . VAL   B 1 11  ? -2.517  7.327   26.529  1.00 46.32  ?  11  VAL   B CB   1 
ATOM   1094 C  CG1  . VAL   B 1 11  ? -1.951  6.008   27.037  1.00 42.64  ?  11  VAL   B CG1  1 
ATOM   1095 C  CG2  . VAL   B 1 11  ? -1.658  7.889   25.406  1.00 44.24  ?  11  VAL   B CG2  1 
ATOM   1096 N  N    . VAL   B 1 12  ? -5.446  5.363   26.793  1.00 35.86  ?  12  VAL   B N    1 
ATOM   1097 C  CA   . VAL   B 1 12  ? -6.436  4.753   27.669  1.00 38.53  ?  12  VAL   B CA   1 
ATOM   1098 C  C    . VAL   B 1 12  ? -6.079  3.296   27.907  1.00 41.09  ?  12  VAL   B C    1 
ATOM   1099 O  O    . VAL   B 1 12  ? -5.442  2.641   27.075  1.00 35.91  ?  12  VAL   B O    1 
ATOM   1100 C  CB   . VAL   B 1 12  ? -7.869  4.869   27.101  1.00 43.68  ?  12  VAL   B CB   1 
ATOM   1101 C  CG1  . VAL   B 1 12  ? -8.172  6.305   26.708  1.00 49.24  ?  12  VAL   B CG1  1 
ATOM   1102 C  CG2  . VAL   B 1 12  ? -8.055  3.927   25.924  1.00 54.72  ?  12  VAL   B CG2  1 
ATOM   1103 N  N    . GLU   B 1 13  ? -6.497  2.794   29.064  1.00 39.17  ?  13  GLU   B N    1 
ATOM   1104 C  CA   . GLU   B 1 13  ? -6.223  1.429   29.478  1.00 38.42  ?  13  GLU   B CA   1 
ATOM   1105 C  C    . GLU   B 1 13  ? -7.342  0.508   29.016  1.00 33.30  ?  13  GLU   B C    1 
ATOM   1106 O  O    . GLU   B 1 13  ? -8.524  0.853   29.103  1.00 35.04  ?  13  GLU   B O    1 
ATOM   1107 C  CB   . GLU   B 1 13  ? -6.078  1.350   30.999  1.00 35.48  ?  13  GLU   B CB   1 
ATOM   1108 C  CG   . GLU   B 1 13  ? -5.047  2.309   31.573  1.00 39.10  ?  13  GLU   B CG   1 
ATOM   1109 C  CD   . GLU   B 1 13  ? -3.675  2.137   30.952  1.00 44.66  ?  13  GLU   B CD   1 
ATOM   1110 O  OE1  . GLU   B 1 13  ? -3.189  0.988   30.890  1.00 45.70  ?  13  GLU   B OE1  1 
ATOM   1111 O  OE2  . GLU   B 1 13  ? -3.087  3.152   30.521  1.00 44.69  ?  13  GLU   B OE2  1 
ATOM   1112 N  N    . TYR   B 1 14  ? -6.959  -0.658  28.502  1.00 38.46  ?  14  TYR   B N    1 
ATOM   1113 C  CA   . TYR   B 1 14  ? -7.927  -1.702  28.199  1.00 40.42  ?  14  TYR   B CA   1 
ATOM   1114 C  C    . TYR   B 1 14  ? -8.861  -1.913  29.383  1.00 43.94  ?  14  TYR   B C    1 
ATOM   1115 O  O    . TYR   B 1 14  ? -8.420  -1.988  30.533  1.00 40.05  ?  14  TYR   B O    1 
ATOM   1116 C  CB   . TYR   B 1 14  ? -7.185  -2.997  27.856  1.00 37.81  ?  14  TYR   B CB   1 
ATOM   1117 C  CG   . TYR   B 1 14  ? -8.054  -4.226  27.694  1.00 39.69  ?  14  TYR   B CG   1 
ATOM   1118 C  CD1  . TYR   B 1 14  ? -8.484  -4.948  28.800  1.00 46.32  ?  14  TYR   B CD1  1 
ATOM   1119 C  CD2  . TYR   B 1 14  ? -8.421  -4.679  26.434  1.00 42.23  ?  14  TYR   B CD2  1 
ATOM   1120 C  CE1  . TYR   B 1 14  ? -9.267  -6.073  28.657  1.00 47.83  ?  14  TYR   B CE1  1 
ATOM   1121 C  CE2  . TYR   B 1 14  ? -9.205  -5.807  26.283  1.00 41.60  ?  14  TYR   B CE2  1 
ATOM   1122 C  CZ   . TYR   B 1 14  ? -9.625  -6.498  27.398  1.00 57.23  ?  14  TYR   B CZ   1 
ATOM   1123 O  OH   . TYR   B 1 14  ? -10.405 -7.622  27.256  1.00 55.46  ?  14  TYR   B OH   1 
ATOM   1124 N  N    . GLY   B 1 15  ? -10.161 -1.989  29.098  1.00 42.09  ?  15  GLY   B N    1 
ATOM   1125 C  CA   . GLY   B 1 15  ? -11.154 -2.227  30.121  1.00 40.84  ?  15  GLY   B CA   1 
ATOM   1126 C  C    . GLY   B 1 15  ? -11.728 -0.986  30.768  1.00 47.00  ?  15  GLY   B C    1 
ATOM   1127 O  O    . GLY   B 1 15  ? -12.730 -1.090  31.487  1.00 45.32  ?  15  GLY   B O    1 
ATOM   1128 N  N    . SER   B 1 16  ? -11.123 0.179   30.557  1.00 39.43  ?  16  SER   B N    1 
ATOM   1129 C  CA   . SER   B 1 16  ? -11.628 1.409   31.140  1.00 45.32  ?  16  SER   B CA   1 
ATOM   1130 C  C    . SER   B 1 16  ? -12.714 2.010   30.252  1.00 47.48  ?  16  SER   B C    1 
ATOM   1131 O  O    . SER   B 1 16  ? -13.063 1.478   29.196  1.00 38.83  ?  16  SER   B O    1 
ATOM   1132 C  CB   . SER   B 1 16  ? -10.490 2.407   31.345  1.00 50.54  ?  16  SER   B CB   1 
ATOM   1133 O  OG   . SER   B 1 16  ? -10.116 3.004   30.113  1.00 56.51  ?  16  SER   B OG   1 
ATOM   1134 N  N    . ASN   B 1 17  ? -13.246 3.146   30.686  1.00 46.14  ?  17  ASN   B N    1 
ATOM   1135 C  CA   . ASN   B 1 17  ? -14.164 3.943   29.890  1.00 45.16  ?  17  ASN   B CA   1 
ATOM   1136 C  C    . ASN   B 1 17  ? -13.415 5.180   29.428  1.00 48.32  ?  17  ASN   B C    1 
ATOM   1137 O  O    . ASN   B 1 17  ? -12.585 5.720   30.166  1.00 44.85  ?  17  ASN   B O    1 
ATOM   1138 C  CB   . ASN   B 1 17  ? -15.402 4.352   30.696  1.00 38.20  ?  17  ASN   B CB   1 
ATOM   1139 C  CG   . ASN   B 1 17  ? -16.139 3.166   31.282  1.00 49.47  ?  17  ASN   B CG   1 
ATOM   1140 O  OD1  . ASN   B 1 17  ? -16.160 2.082   30.699  1.00 47.46  ?  17  ASN   B OD1  1 
ATOM   1141 N  ND2  . ASN   B 1 17  ? -16.745 3.364   32.447  1.00 56.34  ?  17  ASN   B ND2  1 
ATOM   1142 N  N    . MET   B 1 18  ? -13.701 5.635   28.216  1.00 47.17  ?  18  MET   B N    1 
ATOM   1143 C  CA   . MET   B 1 18  ? -13.053 6.837   27.721  1.00 40.74  ?  18  MET   B CA   1 
ATOM   1144 C  C    . MET   B 1 18  ? -14.094 7.776   27.144  1.00 42.90  ?  18  MET   B C    1 
ATOM   1145 O  O    . MET   B 1 18  ? -15.063 7.345   26.514  1.00 44.15  ?  18  MET   B O    1 
ATOM   1146 C  CB   . MET   B 1 18  ? -11.983 6.521   26.666  1.00 45.64  ?  18  MET   B CB   1 
ATOM   1147 C  CG   . MET   B 1 18  ? -12.503 5.923   25.374  1.00 62.03  ?  18  MET   B CG   1 
ATOM   1148 S  SD   . MET   B 1 18  ? -11.214 5.920   24.111  1.00 50.36  ?  18  MET   B SD   1 
ATOM   1149 C  CE   . MET   B 1 18  ? -12.146 5.458   22.655  1.00 43.89  ?  18  MET   B CE   1 
ATOM   1150 N  N    . THR   B 1 19  ? -13.881 9.065   27.362  1.00 40.85  ?  19  THR   B N    1 
ATOM   1151 C  CA   . THR   B 1 19  ? -14.726 10.107  26.802  1.00 48.73  ?  19  THR   B CA   1 
ATOM   1152 C  C    . THR   B 1 19  ? -13.816 11.023  26.002  1.00 40.30  ?  19  THR   B C    1 
ATOM   1153 O  O    . THR   B 1 19  ? -12.946 11.693  26.570  1.00 41.99  ?  19  THR   B O    1 
ATOM   1154 C  CB   . THR   B 1 19  ? -15.461 10.874  27.901  1.00 57.13  ?  19  THR   B CB   1 
ATOM   1155 O  OG1  . THR   B 1 19  ? -16.440 10.022  28.510  1.00 44.62  ?  19  THR   B OG1  1 
ATOM   1156 C  CG2  . THR   B 1 19  ? -16.152 12.101  27.324  1.00 49.71  ?  19  THR   B CG2  1 
ATOM   1157 N  N    . ILE   B 1 20  ? -14.007 11.046  24.689  1.00 47.96  ?  20  ILE   B N    1 
ATOM   1158 C  CA   . ILE   B 1 20  ? -13.247 11.926  23.815  1.00 41.80  ?  20  ILE   B CA   1 
ATOM   1159 C  C    . ILE   B 1 20  ? -14.186 13.028  23.362  1.00 47.88  ?  20  ILE   B C    1 
ATOM   1160 O  O    . ILE   B 1 20  ? -15.347 12.774  23.016  1.00 41.11  ?  20  ILE   B O    1 
ATOM   1161 C  CB   . ILE   B 1 20  ? -12.626 11.185  22.614  1.00 46.41  ?  20  ILE   B CB   1 
ATOM   1162 C  CG1  . ILE   B 1 20  ? -13.693 10.445  21.810  1.00 49.16  ?  20  ILE   B CG1  1 
ATOM   1163 C  CG2  . ILE   B 1 20  ? -11.548 10.218  23.087  1.00 50.84  ?  20  ILE   B CG2  1 
ATOM   1164 C  CD1  . ILE   B 1 20  ? -13.119 9.616   20.677  1.00 58.93  ?  20  ILE   B CD1  1 
ATOM   1165 N  N    . GLU   B 1 21  ? -13.682 14.253  23.375  1.00 51.40  ?  21  GLU   B N    1 
ATOM   1166 C  CA   . GLU   B 1 21  ? -14.519 15.435  23.309  1.00 61.92  ?  21  GLU   B CA   1 
ATOM   1167 C  C    . GLU   B 1 21  ? -14.153 16.251  22.082  1.00 50.22  ?  21  GLU   B C    1 
ATOM   1168 O  O    . GLU   B 1 21  ? -12.974 16.370  21.733  1.00 54.49  ?  21  GLU   B O    1 
ATOM   1169 C  CB   . GLU   B 1 21  ? -14.326 16.259  24.580  1.00 64.21  ?  21  GLU   B CB   1 
ATOM   1170 C  CG   . GLU   B 1 21  ? -14.575 15.440  25.837  1.00 66.65  ?  21  GLU   B CG   1 
ATOM   1171 C  CD   . GLU   B 1 21  ? -14.620 16.275  27.094  1.00 61.51  ?  21  GLU   B CD   1 
ATOM   1172 O  OE1  . GLU   B 1 21  ? -14.656 17.518  26.987  1.00 75.77  ?  21  GLU   B OE1  1 
ATOM   1173 O  OE2  . GLU   B 1 21  ? -14.608 15.683  28.194  1.00 83.20  ?  21  GLU   B OE2  1 
ATOM   1174 N  N    . CYS   B 1 22  ? -15.164 16.791  21.411  1.00 59.56  ?  22  CYS   B N    1 
ATOM   1175 C  CA   . CYS   B 1 22  ? -14.924 17.807  20.400  1.00 57.82  ?  22  CYS   B CA   1 
ATOM   1176 C  C    . CYS   B 1 22  ? -16.015 18.864  20.485  1.00 59.08  ?  22  CYS   B C    1 
ATOM   1177 O  O    . CYS   B 1 22  ? -17.182 18.555  20.743  1.00 50.02  ?  22  CYS   B O    1 
ATOM   1178 C  CB   . CYS   B 1 22  ? -14.771 17.181  19.002  1.00 69.30  ?  22  CYS   B CB   1 
ATOM   1179 S  SG   . CYS   B 1 22  ? -16.195 16.853  17.966  1.00 64.76  ?  22  CYS   B SG   1 
ATOM   1180 N  N    . LYS   B 1 23  ? -15.606 20.114  20.301  1.00 55.27  ?  23  LYS   B N    1 
ATOM   1181 C  CA   . LYS   B 1 23  ? -16.434 21.291  20.506  1.00 57.41  ?  23  LYS   B CA   1 
ATOM   1182 C  C    . LYS   B 1 23  ? -16.868 21.881  19.172  1.00 53.79  ?  23  LYS   B C    1 
ATOM   1183 O  O    . LYS   B 1 23  ? -16.130 21.835  18.184  1.00 57.88  ?  23  LYS   B O    1 
ATOM   1184 C  CB   . LYS   B 1 23  ? -15.670 22.364  21.289  1.00 62.90  ?  23  LYS   B CB   1 
ATOM   1185 C  CG   . LYS   B 1 23  ? -14.864 21.862  22.478  1.00 63.96  ?  23  LYS   B CG   1 
ATOM   1186 C  CD   . LYS   B 1 23  ? -15.728 21.299  23.589  1.00 75.12  ?  23  LYS   B CD   1 
ATOM   1187 C  CE   . LYS   B 1 23  ? -15.019 21.469  24.925  1.00 68.31  ?  23  LYS   B CE   1 
ATOM   1188 N  NZ   . LYS   B 1 23  ? -15.485 20.515  25.964  1.00 68.18  ?  23  LYS   B NZ   1 
ATOM   1189 N  N    . PHE   B 1 24  ? -18.081 22.421  19.145  1.00 66.55  ?  24  PHE   B N    1 
ATOM   1190 C  CA   . PHE   B 1 24  ? -18.523 23.236  18.027  1.00 65.57  ?  24  PHE   B CA   1 
ATOM   1191 C  C    . PHE   B 1 24  ? -19.234 24.458  18.583  1.00 66.38  ?  24  PHE   B C    1 
ATOM   1192 O  O    . PHE   B 1 24  ? -19.834 24.395  19.663  1.00 57.59  ?  24  PHE   B O    1 
ATOM   1193 C  CB   . PHE   B 1 24  ? -19.455 22.476  17.069  1.00 67.58  ?  24  PHE   B CB   1 
ATOM   1194 C  CG   . PHE   B 1 24  ? -20.720 21.980  17.707  1.00 59.02  ?  24  PHE   B CG   1 
ATOM   1195 C  CD1  . PHE   B 1 24  ? -20.720 20.829  18.475  1.00 53.30  ?  24  PHE   B CD1  1 
ATOM   1196 C  CD2  . PHE   B 1 24  ? -21.913 22.660  17.526  1.00 51.82  ?  24  PHE   B CD2  1 
ATOM   1197 C  CE1  . PHE   B 1 24  ? -21.887 20.368  19.056  1.00 59.65  ?  24  PHE   B CE1  1 
ATOM   1198 C  CE2  . PHE   B 1 24  ? -23.082 22.204  18.104  1.00 48.28  ?  24  PHE   B CE2  1 
ATOM   1199 C  CZ   . PHE   B 1 24  ? -23.069 21.057  18.870  1.00 62.31  ?  24  PHE   B CZ   1 
ATOM   1200 N  N    . PRO   B 1 25  ? -19.180 25.584  17.874  1.00 59.39  ?  25  PRO   B N    1 
ATOM   1201 C  CA   . PRO   B 1 25  ? -19.724 26.829  18.429  1.00 62.76  ?  25  PRO   B CA   1 
ATOM   1202 C  C    . PRO   B 1 25  ? -21.245 26.818  18.456  1.00 72.10  ?  25  PRO   B C    1 
ATOM   1203 O  O    . PRO   B 1 25  ? -21.898 26.442  17.479  1.00 75.31  ?  25  PRO   B O    1 
ATOM   1204 C  CB   . PRO   B 1 25  ? -19.184 27.901  17.477  1.00 58.61  ?  25  PRO   B CB   1 
ATOM   1205 C  CG   . PRO   B 1 25  ? -19.065 27.184  16.172  1.00 72.56  ?  25  PRO   B CG   1 
ATOM   1206 C  CD   . PRO   B 1 25  ? -18.613 25.785  16.527  1.00 64.21  ?  25  PRO   B CD   1 
ATOM   1207 N  N    . VAL   B 1 26  ? -21.806 27.226  19.592  1.00 64.85  ?  26  VAL   B N    1 
ATOM   1208 C  CA   . VAL   B 1 26  ? -23.243 27.412  19.739  1.00 83.63  ?  26  VAL   B CA   1 
ATOM   1209 C  C    . VAL   B 1 26  ? -23.451 28.826  20.269  1.00 84.95  ?  26  VAL   B C    1 
ATOM   1210 O  O    . VAL   B 1 26  ? -23.159 29.108  21.438  1.00 66.70  ?  26  VAL   B O    1 
ATOM   1211 C  CB   . VAL   B 1 26  ? -23.869 26.363  20.671  1.00 77.19  ?  26  VAL   B CB   1 
ATOM   1212 C  CG1  . VAL   B 1 26  ? -23.585 24.967  20.150  1.00 74.01  ?  26  VAL   B CG1  1 
ATOM   1213 C  CG2  . VAL   B 1 26  ? -23.313 26.494  22.086  1.00 87.07  ?  26  VAL   B CG2  1 
ATOM   1214 N  N    . GLU   B 1 27  ? -23.955 29.716  19.413  1.00 93.39  ?  27  GLU   B N    1 
ATOM   1215 C  CA   . GLU   B 1 27  ? -24.114 31.118  19.804  1.00 85.07  ?  27  GLU   B CA   1 
ATOM   1216 C  C    . GLU   B 1 27  ? -25.384 31.317  20.622  1.00 91.90  ?  27  GLU   B C    1 
ATOM   1217 O  O    . GLU   B 1 27  ? -25.335 31.641  21.813  1.00 94.31  ?  27  GLU   B O    1 
ATOM   1218 C  CB   . GLU   B 1 27  ? -24.128 32.013  18.561  1.00 96.82  ?  27  GLU   B CB   1 
ATOM   1219 C  CG   . GLU   B 1 27  ? -22.756 32.333  17.999  1.00 95.10  ?  27  GLU   B CG   1 
ATOM   1220 C  CD   . GLU   B 1 27  ? -22.032 31.102  17.492  1.00 91.75  ?  27  GLU   B CD   1 
ATOM   1221 O  OE1  . GLU   B 1 27  ? -20.899 31.248  16.989  1.00 89.68  ?  27  GLU   B OE1  1 
ATOM   1222 N  N    . LYS   B 1 28  ? -26.530 31.108  19.987  1.00 100.51 ?  28  LYS   B N    1 
ATOM   1223 C  CA   . LYS   B 1 28  ? -27.825 31.198  20.635  1.00 90.18  ?  28  LYS   B CA   1 
ATOM   1224 C  C    . LYS   B 1 28  ? -28.184 29.818  21.179  1.00 90.34  ?  28  LYS   B C    1 
ATOM   1225 O  O    . LYS   B 1 28  ? -27.339 28.924  21.271  1.00 94.98  ?  28  LYS   B O    1 
ATOM   1226 C  CB   . LYS   B 1 28  ? -28.873 31.729  19.657  1.00 99.13  ?  28  LYS   B CB   1 
ATOM   1227 C  CG   . LYS   B 1 28  ? -28.460 32.994  18.916  1.00 95.66  ?  28  LYS   B CG   1 
ATOM   1228 C  CE   . LYS   B 1 28  ? -31.515 36.185  20.290  1.00 73.67  ?  28  LYS   B CE   1 
ATOM   1229 N  N    . GLN   B 1 29  ? -29.444 29.638  21.562  1.00 73.64  ?  29  GLN   B N    1 
ATOM   1230 C  CA   . GLN   B 1 29  ? -29.938 28.317  21.924  1.00 87.31  ?  29  GLN   B CA   1 
ATOM   1231 C  C    . GLN   B 1 29  ? -29.611 27.299  20.838  1.00 84.21  ?  29  GLN   B C    1 
ATOM   1232 O  O    . GLN   B 1 29  ? -29.618 27.614  19.645  1.00 74.43  ?  29  GLN   B O    1 
ATOM   1233 C  CB   . GLN   B 1 29  ? -31.448 28.353  22.168  1.00 83.62  ?  29  GLN   B CB   1 
ATOM   1234 C  CG   . GLN   B 1 29  ? -32.049 26.988  22.484  1.00 74.51  ?  29  GLN   B CG   1 
ATOM   1235 C  CD   . GLN   B 1 29  ? -31.907 26.604  23.946  1.00 76.93  ?  29  GLN   B CD   1 
ATOM   1236 O  OE1  . GLN   B 1 29  ? -31.370 25.544  24.271  1.00 83.58  ?  29  GLN   B OE1  1 
ATOM   1237 N  NE2  . GLN   B 1 29  ? -32.387 27.465  24.835  1.00 73.69  ?  29  GLN   B NE2  1 
ATOM   1238 N  N    . LEU   B 1 30  ? -29.311 26.074  21.262  1.00 92.78  ?  30  LEU   B N    1 
ATOM   1239 C  CA   . LEU   B 1 30  ? -29.011 25.022  20.303  1.00 84.90  ?  30  LEU   B CA   1 
ATOM   1240 C  C    . LEU   B 1 30  ? -30.251 24.731  19.472  1.00 84.07  ?  30  LEU   B C    1 
ATOM   1241 O  O    . LEU   B 1 30  ? -31.368 24.658  19.992  1.00 91.32  ?  30  LEU   B O    1 
ATOM   1242 C  CB   . LEU   B 1 30  ? -28.559 23.752  21.030  1.00 82.23  ?  30  LEU   B CB   1 
ATOM   1243 C  CG   . LEU   B 1 30  ? -28.221 22.520  20.183  1.00 80.29  ?  30  LEU   B CG   1 
ATOM   1244 C  CD1  . LEU   B 1 30  ? -26.987 22.740  19.317  1.00 77.54  ?  30  LEU   B CD1  1 
ATOM   1245 C  CD2  . LEU   B 1 30  ? -28.063 21.285  21.065  1.00 79.92  ?  30  LEU   B CD2  1 
ATOM   1246 N  N    . ASP   B 1 31  ? -30.050 24.578  18.169  1.00 89.04  ?  31  ASP   B N    1 
ATOM   1247 C  CA   . ASP   B 1 31  ? -31.116 24.250  17.227  1.00 82.87  ?  31  ASP   B CA   1 
ATOM   1248 C  C    . ASP   B 1 31  ? -30.954 22.784  16.830  1.00 78.48  ?  31  ASP   B C    1 
ATOM   1249 O  O    . ASP   B 1 31  ? -30.273 22.459  15.855  1.00 86.74  ?  31  ASP   B O    1 
ATOM   1250 C  CB   . ASP   B 1 31  ? -31.065 25.183  16.020  1.00 79.88  ?  31  ASP   B CB   1 
ATOM   1251 C  CG   . ASP   B 1 31  ? -32.028 24.779  14.927  1.00 84.27  ?  31  ASP   B CG   1 
ATOM   1252 O  OD1  . ASP   B 1 31  ? -32.998 24.053  15.228  1.00 84.32  ?  31  ASP   B OD1  1 
ATOM   1253 O  OD2  . ASP   B 1 31  ? -31.818 25.192  13.767  1.00 85.54  ?  31  ASP   B OD2  1 
ATOM   1254 N  N    . LEU   B 1 32  ? -31.595 21.899  17.599  1.00 82.81  ?  32  LEU   B N    1 
ATOM   1255 C  CA   . LEU   B 1 32  ? -31.445 20.464  17.378  1.00 80.31  ?  32  LEU   B CA   1 
ATOM   1256 C  C    . LEU   B 1 32  ? -31.772 20.065  15.946  1.00 84.70  ?  32  LEU   B C    1 
ATOM   1257 O  O    . LEU   B 1 32  ? -31.182 19.117  15.417  1.00 83.23  ?  32  LEU   B O    1 
ATOM   1258 C  CB   . LEU   B 1 32  ? -32.333 19.689  18.352  1.00 67.03  ?  32  LEU   B CB   1 
ATOM   1259 C  CG   . LEU   B 1 32  ? -31.624 19.080  19.562  1.00 73.18  ?  32  LEU   B CG   1 
ATOM   1260 C  CD1  . LEU   B 1 32  ? -32.423 17.915  20.120  1.00 86.19  ?  32  LEU   B CD1  1 
ATOM   1261 C  CD2  . LEU   B 1 32  ? -30.222 18.636  19.183  1.00 76.33  ?  32  LEU   B CD2  1 
ATOM   1262 N  N    . ALA   B 1 33  ? -32.712 20.762  15.307  1.00 74.50  ?  33  ALA   B N    1 
ATOM   1263 C  CA   . ALA   B 1 33  ? -33.108 20.390  13.953  1.00 80.62  ?  33  ALA   B CA   1 
ATOM   1264 C  C    . ALA   B 1 33  ? -31.938 20.497  12.983  1.00 72.51  ?  33  ALA   B C    1 
ATOM   1265 O  O    . ALA   B 1 33  ? -31.800 19.673  12.071  1.00 69.58  ?  33  ALA   B O    1 
ATOM   1266 C  CB   . ALA   B 1 33  ? -34.273 21.263  13.486  1.00 81.09  ?  33  ALA   B CB   1 
ATOM   1267 N  N    . ALA   B 1 34  ? -31.085 21.503  13.162  1.00 75.89  ?  34  ALA   B N    1 
ATOM   1268 C  CA   . ALA   B 1 34  ? -30.000 21.785  12.232  1.00 73.26  ?  34  ALA   B CA   1 
ATOM   1269 C  C    . ALA   B 1 34  ? -28.689 21.108  12.614  1.00 71.78  ?  34  ALA   B C    1 
ATOM   1270 O  O    . ALA   B 1 34  ? -27.648 21.438  12.036  1.00 81.72  ?  34  ALA   B O    1 
ATOM   1271 C  CB   . ALA   B 1 34  ? -29.785 23.296  12.118  1.00 74.53  ?  34  ALA   B CB   1 
ATOM   1272 N  N    . LEU   B 1 35  ? -28.710 20.173  13.558  1.00 63.55  ?  35  LEU   B N    1 
ATOM   1273 C  CA   . LEU   B 1 35  ? -27.494 19.574  14.091  1.00 64.30  ?  35  LEU   B CA   1 
ATOM   1274 C  C    . LEU   B 1 35  ? -27.373 18.132  13.624  1.00 56.00  ?  35  LEU   B C    1 
ATOM   1275 O  O    . LEU   B 1 35  ? -28.310 17.341  13.782  1.00 63.84  ?  35  LEU   B O    1 
ATOM   1276 C  CB   . LEU   B 1 35  ? -27.478 19.627  15.620  1.00 57.52  ?  35  LEU   B CB   1 
ATOM   1277 C  CG   . LEU   B 1 35  ? -26.257 18.973  16.270  1.00 50.85  ?  35  LEU   B CG   1 
ATOM   1278 C  CD1  . LEU   B 1 35  ? -24.973 19.646  15.810  1.00 59.01  ?  35  LEU   B CD1  1 
ATOM   1279 C  CD2  . LEU   B 1 35  ? -26.372 18.999  17.787  1.00 55.70  ?  35  LEU   B CD2  1 
ATOM   1280 N  N    . ILE   B 1 36  ? -26.217 17.794  13.059  1.00 49.57  ?  36  ILE   B N    1 
ATOM   1281 C  CA   . ILE   B 1 36  ? -25.831 16.412  12.810  1.00 54.53  ?  36  ILE   B CA   1 
ATOM   1282 C  C    . ILE   B 1 36  ? -24.449 16.196  13.405  1.00 55.52  ?  36  ILE   B C    1 
ATOM   1283 O  O    . ILE   B 1 36  ? -23.518 16.959  13.119  1.00 51.06  ?  36  ILE   B O    1 
ATOM   1284 C  CB   . ILE   B 1 36  ? -25.826 16.066  11.309  1.00 59.01  ?  36  ILE   B CB   1 
ATOM   1285 C  CG1  . ILE   B 1 36  ? -27.216 16.265  10.705  1.00 62.25  ?  36  ILE   B CG1  1 
ATOM   1286 C  CG2  . ILE   B 1 36  ? -25.359 14.634  11.097  1.00 60.68  ?  36  ILE   B CG2  1 
ATOM   1287 C  CD1  . ILE   B 1 36  ? -27.188 16.807  9.292   1.00 56.80  ?  36  ILE   B CD1  1 
ATOM   1288 N  N    . VAL   B 1 37  ? -24.319 15.158  14.227  1.00 46.80  ?  37  VAL   B N    1 
ATOM   1289 C  CA   . VAL   B 1 37  ? -23.041 14.755  14.800  1.00 47.89  ?  37  VAL   B CA   1 
ATOM   1290 C  C    . VAL   B 1 37  ? -22.764 13.323  14.374  1.00 41.64  ?  37  VAL   B C    1 
ATOM   1291 O  O    . VAL   B 1 37  ? -23.641 12.459  14.474  1.00 45.64  ?  37  VAL   B O    1 
ATOM   1292 C  CB   . VAL   B 1 37  ? -23.025 14.881  16.334  1.00 41.23  ?  37  VAL   B CB   1 
ATOM   1293 C  CG1  . VAL   B 1 37  ? -21.723 14.324  16.892  1.00 40.06  ?  37  VAL   B CG1  1 
ATOM   1294 C  CG2  . VAL   B 1 37  ? -23.197 16.332  16.745  1.00 49.23  ?  37  VAL   B CG2  1 
ATOM   1295 N  N    . TYR   B 1 38  ? -21.561 13.073  13.875  1.00 41.23  ?  38  TYR   B N    1 
ATOM   1296 C  CA   . TYR   B 1 38  ? -21.208 11.753  13.379  1.00 49.30  ?  38  TYR   B CA   1 
ATOM   1297 C  C    . TYR   B 1 38  ? -19.815 11.394  13.869  1.00 42.63  ?  38  TYR   B C    1 
ATOM   1298 O  O    . TYR   B 1 38  ? -18.857 12.133  13.624  1.00 44.84  ?  38  TYR   B O    1 
ATOM   1299 C  CB   . TYR   B 1 38  ? -21.283 11.715  11.855  1.00 43.13  ?  38  TYR   B CB   1 
ATOM   1300 C  CG   . TYR   B 1 38  ? -21.035 10.353  11.288  1.00 48.16  ?  38  TYR   B CG   1 
ATOM   1301 C  CD1  . TYR   B 1 38  ? -22.068 9.441   11.155  1.00 62.13  ?  38  TYR   B CD1  1 
ATOM   1302 C  CD2  . TYR   B 1 38  ? -19.765 9.979   10.874  1.00 50.73  ?  38  TYR   B CD2  1 
ATOM   1303 C  CE1  . TYR   B 1 38  ? -21.839 8.195   10.637  1.00 65.97  ?  38  TYR   B CE1  1 
ATOM   1304 C  CE2  . TYR   B 1 38  ? -19.527 8.738   10.350  1.00 44.81  ?  38  TYR   B CE2  1 
ATOM   1305 C  CZ   . TYR   B 1 38  ? -20.563 7.846   10.240  1.00 58.00  ?  38  TYR   B CZ   1 
ATOM   1306 O  OH   . TYR   B 1 38  ? -20.327 6.601   9.711   1.00 72.20  ?  38  TYR   B OH   1 
ATOM   1307 N  N    . TRP   B 1 39  ? -19.708 10.265  14.560  1.00 43.10  ?  39  TRP   B N    1 
ATOM   1308 C  CA   . TRP   B 1 39  ? -18.443 9.740   15.051  1.00 49.19  ?  39  TRP   B CA   1 
ATOM   1309 C  C    . TRP   B 1 39  ? -18.098 8.465   14.303  1.00 36.29  ?  39  TRP   B C    1 
ATOM   1310 O  O    . TRP   B 1 39  ? -18.912 7.526   14.272  1.00 40.17  ?  39  TRP   B O    1 
ATOM   1311 C  CB   . TRP   B 1 39  ? -18.528 9.449   16.550  1.00 52.45  ?  39  TRP   B CB   1 
ATOM   1312 C  CG   . TRP   B 1 39  ? -18.370 10.650  17.404  1.00 46.12  ?  39  TRP   B CG   1 
ATOM   1313 C  CD1  . TRP   B 1 39  ? -19.364 11.422  17.928  1.00 51.19  ?  39  TRP   B CD1  1 
ATOM   1314 C  CD2  . TRP   B 1 39  ? -17.139 11.201  17.878  1.00 43.93  ?  39  TRP   B CD2  1 
ATOM   1315 N  NE1  . TRP   B 1 39  ? -18.826 12.438  18.679  1.00 44.61  ?  39  TRP   B NE1  1 
ATOM   1316 C  CE2  . TRP   B 1 39  ? -17.461 12.322  18.667  1.00 45.36  ?  39  TRP   B CE2  1 
ATOM   1317 C  CE3  . TRP   B 1 39  ? -15.794 10.861  17.704  1.00 42.58  ?  39  TRP   B CE3  1 
ATOM   1318 C  CZ2  . TRP   B 1 39  ? -16.487 13.106  19.282  1.00 54.83  ?  39  TRP   B CZ2  1 
ATOM   1319 C  CZ3  . TRP   B 1 39  ? -14.829 11.639  18.314  1.00 49.45  ?  39  TRP   B CZ3  1 
ATOM   1320 C  CH2  . TRP   B 1 39  ? -15.180 12.748  19.094  1.00 51.85  ?  39  TRP   B CH2  1 
ATOM   1321 N  N    . GLU   B 1 40  ? -16.873 8.417   13.765  1.00 42.33  ?  40  GLU   B N    1 
ATOM   1322 C  CA   . GLU   B 1 40  ? -16.370 7.237   13.068  1.00 38.59  ?  40  GLU   B CA   1 
ATOM   1323 C  C    . GLU   B 1 40  ? -14.902 7.027   13.417  1.00 49.81  ?  40  GLU   B C    1 
ATOM   1324 O  O    . GLU   B 1 40  ? -14.209 7.953   13.834  1.00 46.25  ?  40  GLU   B O    1 
ATOM   1325 C  CB   . GLU   B 1 40  ? -16.576 7.358   11.546  1.00 38.97  ?  40  GLU   B CB   1 
ATOM   1326 C  CG   . GLU   B 1 40  ? -15.822 8.497   10.852  1.00 53.52  ?  40  GLU   B CG   1 
ATOM   1327 C  CD   . GLU   B 1 40  ? -14.485 8.074   10.269  1.00 71.25  ?  40  GLU   B CD   1 
ATOM   1328 O  OE1  . GLU   B 1 40  ? -14.169 6.867   10.311  1.00 71.30  ?  40  GLU   B OE1  1 
ATOM   1329 O  OE2  . GLU   B 1 40  ? -13.760 8.947   9.746   1.00 68.96  ?  40  GLU   B OE2  1 
ATOM   1330 N  N    . MET   B 1 41  ? -14.437 5.785   13.280  1.00 46.22  ?  41  MET   B N    1 
ATOM   1331 C  CA   . MET   B 1 41  ? -13.024 5.461   13.446  1.00 43.28  ?  41  MET   B CA   1 
ATOM   1332 C  C    . MET   B 1 41  ? -12.596 4.536   12.321  1.00 46.54  ?  41  MET   B C    1 
ATOM   1333 O  O    . MET   B 1 41  ? -13.260 3.528   12.056  1.00 48.16  ?  41  MET   B O    1 
ATOM   1334 C  CB   . MET   B 1 41  ? -12.747 4.798   14.802  1.00 39.90  ?  41  MET   B CB   1 
ATOM   1335 C  CG   . MET   B 1 41  ? -11.274 4.485   15.058  1.00 61.25  ?  41  MET   B CG   1 
ATOM   1336 S  SD   . MET   B 1 41  ? -10.717 2.889   14.421  1.00 61.94  ?  41  MET   B SD   1 
ATOM   1337 C  CE   . MET   B 1 41  ? -12.092 1.836   14.878  1.00 49.46  ?  41  MET   B CE   1 
ATOM   1338 N  N    . GLU   B 1 42  ? -11.474 4.869   11.679  1.00 54.40  ?  42  GLU   B N    1 
ATOM   1339 C  CA   . GLU   B 1 42  ? -11.109 4.195   10.443  1.00 63.39  ?  42  GLU   B CA   1 
ATOM   1340 C  C    . GLU   B 1 42  ? -12.285 4.395   9.495   1.00 73.93  ?  42  GLU   B C    1 
ATOM   1341 O  O    . GLU   B 1 42  ? -12.490 5.521   9.032   1.00 89.92  ?  42  GLU   B O    1 
ATOM   1342 C  CB   . GLU   B 1 42  ? -10.696 2.748   10.721  1.00 67.86  ?  42  GLU   B CB   1 
ATOM   1343 C  CG   . GLU   B 1 42  ? -9.198  2.730   11.080  1.00 61.55  ?  42  GLU   B CG   1 
ATOM   1344 C  CD   . GLU   B 1 42  ? -8.752  1.578   11.958  1.00 70.26  ?  42  GLU   B CD   1 
ATOM   1345 O  OE1  . GLU   B 1 42  ? -9.324  0.474   11.863  1.00 82.02  ?  42  GLU   B OE1  1 
ATOM   1346 O  OE2  . GLU   B 1 42  ? -7.808  1.790   12.751  1.00 79.41  ?  42  GLU   B OE2  1 
ATOM   1347 N  N    . ASP   B 1 43  ? -13.069 3.372   9.179   1.00 53.41  ?  43  ASP   B N    1 
ATOM   1348 C  CA   . ASP   B 1 43  ? -14.331 3.663   8.500   1.00 71.03  ?  43  ASP   B CA   1 
ATOM   1349 C  C    . ASP   B 1 43  ? -15.470 2.848   9.104   1.00 71.95  ?  43  ASP   B C    1 
ATOM   1350 O  O    . ASP   B 1 43  ? -16.261 2.210   8.408   1.00 75.53  ?  43  ASP   B O    1 
ATOM   1351 C  CB   . ASP   B 1 43  ? -14.192 3.482   6.993   1.00 68.20  ?  43  ASP   B CB   1 
ATOM   1352 C  CG   . ASP   B 1 43  ? -14.027 4.813   6.279   1.00 72.10  ?  43  ASP   B CG   1 
ATOM   1353 O  OD1  . ASP   B 1 43  ? -14.929 5.672   6.395   1.00 79.99  ?  43  ASP   B OD1  1 
ATOM   1354 O  OD2  . ASP   B 1 43  ? -12.973 5.021   5.647   1.00 91.71  ?  43  ASP   B OD2  1 
ATOM   1355 N  N    . LYS   B 1 44  ? -15.539 2.861   10.432  1.00 57.29  ?  44  LYS   B N    1 
ATOM   1356 C  CA   . LYS   B 1 44  ? -16.613 2.244   11.195  1.00 53.99  ?  44  LYS   B CA   1 
ATOM   1357 C  C    . LYS   B 1 44  ? -17.500 3.346   11.760  1.00 60.54  ?  44  LYS   B C    1 
ATOM   1358 O  O    . LYS   B 1 44  ? -16.996 4.289   12.380  1.00 60.82  ?  44  LYS   B O    1 
ATOM   1359 C  CB   . LYS   B 1 44  ? -16.049 1.400   12.339  1.00 55.20  ?  44  LYS   B CB   1 
ATOM   1360 C  CG   . LYS   B 1 44  ? -14.962 0.428   11.926  1.00 49.72  ?  44  LYS   B CG   1 
ATOM   1361 C  CD   . LYS   B 1 44  ? -14.110 0.047   13.125  1.00 46.52  ?  44  LYS   B CD   1 
ATOM   1362 C  CE   . LYS   B 1 44  ? -13.293 -1.205  12.860  1.00 65.42  ?  44  LYS   B CE   1 
ATOM   1363 N  NZ   . LYS   B 1 44  ? -12.164 -0.948  11.923  1.00 74.36  ?  44  LYS   B NZ   1 
ATOM   1364 N  N    . ASN   B 1 45  ? -18.810 3.236   11.553  1.00 43.26  ?  45  ASN   B N    1 
ATOM   1365 C  CA   . ASN   B 1 45  ? -19.733 4.169   12.190  1.00 42.33  ?  45  ASN   B CA   1 
ATOM   1366 C  C    . ASN   B 1 45  ? -19.825 3.869   13.678  1.00 45.85  ?  45  ASN   B C    1 
ATOM   1367 O  O    . ASN   B 1 45  ? -20.282 2.790   14.071  1.00 45.51  ?  45  ASN   B O    1 
ATOM   1368 C  CB   . ASN   B 1 45  ? -21.126 4.106   11.578  1.00 44.52  ?  45  ASN   B CB   1 
ATOM   1369 C  CG   . ASN   B 1 45  ? -22.160 4.829   12.439  1.00 68.74  ?  45  ASN   B CG   1 
ATOM   1370 O  OD1  . ASN   B 1 45  ? -22.319 6.044   12.351  1.00 79.44  ?  45  ASN   B OD1  1 
ATOM   1371 N  ND2  . ASN   B 1 45  ? -22.832 4.087   13.304  1.00 69.61  ?  45  ASN   B ND2  1 
ATOM   1372 N  N    . ILE   B 1 46  ? -19.401 4.813   14.508  1.00 46.20  ?  46  ILE   B N    1 
ATOM   1373 C  CA   . ILE   B 1 46  ? -19.600 4.660   15.941  1.00 43.38  ?  46  ILE   B CA   1 
ATOM   1374 C  C    . ILE   B 1 46  ? -20.932 5.245   16.373  1.00 51.86  ?  46  ILE   B C    1 
ATOM   1375 O  O    . ILE   B 1 46  ? -21.702 4.593   17.083  1.00 55.46  ?  46  ILE   B O    1 
ATOM   1376 C  CB   . ILE   B 1 46  ? -18.435 5.297   16.723  1.00 53.09  ?  46  ILE   B CB   1 
ATOM   1377 C  CG1  . ILE   B 1 46  ? -17.108 4.674   16.298  1.00 43.14  ?  46  ILE   B CG1  1 
ATOM   1378 C  CG2  . ILE   B 1 46  ? -18.657 5.136   18.222  1.00 37.87  ?  46  ILE   B CG2  1 
ATOM   1379 C  CD1  . ILE   B 1 46  ? -15.915 5.525   16.628  1.00 39.66  ?  46  ILE   B CD1  1 
ATOM   1380 N  N    . ILE   B 1 47  ? -21.247 6.473   15.959  1.00 48.86  ?  47  ILE   B N    1 
ATOM   1381 C  CA   . ILE   B 1 47  ? -22.516 7.059   16.386  1.00 57.12  ?  47  ILE   B CA   1 
ATOM   1382 C  C    . ILE   B 1 47  ? -22.974 8.111   15.389  1.00 43.28  ?  47  ILE   B C    1 
ATOM   1383 O  O    . ILE   B 1 47  ? -22.162 8.823   14.797  1.00 58.67  ?  47  ILE   B O    1 
ATOM   1384 C  CB   . ILE   B 1 47  ? -22.414 7.622   17.826  1.00 64.13  ?  47  ILE   B CB   1 
ATOM   1385 C  CG1  . ILE   B 1 47  ? -23.757 7.454   18.527  1.00 76.22  ?  47  ILE   B CG1  1 
ATOM   1386 C  CG2  . ILE   B 1 47  ? -21.963 9.070   17.822  1.00 58.29  ?  47  ILE   B CG2  1 
ATOM   1387 C  CD1  . ILE   B 1 47  ? -23.876 6.091   19.138  1.00 74.63  ?  47  ILE   B CD1  1 
ATOM   1388 N  N    . GLN   B 1 48  ? -24.291 8.200   15.199  1.00 47.11  ?  48  GLN   B N    1 
ATOM   1389 C  CA   . GLN   B 1 48  ? -24.907 9.184   14.316  1.00 61.38  ?  48  GLN   B CA   1 
ATOM   1390 C  C    . GLN   B 1 48  ? -26.098 9.820   15.016  1.00 70.07  ?  48  GLN   B C    1 
ATOM   1391 O  O    . GLN   B 1 48  ? -27.085 9.138   15.311  1.00 68.10  ?  48  GLN   B O    1 
ATOM   1392 C  CB   . GLN   B 1 48  ? -25.354 8.563   12.991  1.00 61.60  ?  48  GLN   B CB   1 
ATOM   1393 C  CG   . GLN   B 1 48  ? -26.195 9.517   12.153  1.00 71.03  ?  48  GLN   B CG   1 
ATOM   1394 C  CD   . GLN   B 1 48  ? -26.218 9.157   10.686  1.00 76.09  ?  48  GLN   B CD   1 
ATOM   1395 O  OE1  . GLN   B 1 48  ? -26.697 8.090   10.303  1.00 89.17  ?  48  GLN   B OE1  1 
ATOM   1396 N  NE2  . GLN   B 1 48  ? -25.700 10.050  9.851   1.00 90.87  ?  48  GLN   B NE2  1 
ATOM   1397 N  N    . PHE   B 1 49  ? -25.998 11.118  15.293  1.00 58.08  ?  49  PHE   B N    1 
ATOM   1398 C  CA   . PHE   B 1 49  ? -27.062 11.892  15.916  1.00 55.34  ?  49  PHE   B CA   1 
ATOM   1399 C  C    . PHE   B 1 49  ? -27.605 12.836  14.850  1.00 53.84  ?  49  PHE   B C    1 
ATOM   1400 O  O    . PHE   B 1 49  ? -26.926 13.789  14.446  1.00 61.07  ?  49  PHE   B O    1 
ATOM   1401 C  CB   . PHE   B 1 49  ? -26.543 12.655  17.133  1.00 52.53  ?  49  PHE   B CB   1 
ATOM   1402 C  CG   . PHE   B 1 49  ? -27.614 13.373  17.907  1.00 56.57  ?  49  PHE   B CG   1 
ATOM   1403 C  CD1  . PHE   B 1 49  ? -28.407 12.691  18.814  1.00 69.47  ?  49  PHE   B CD1  1 
ATOM   1404 C  CD2  . PHE   B 1 49  ? -27.810 14.734  17.744  1.00 59.71  ?  49  PHE   B CD2  1 
ATOM   1405 C  CE1  . PHE   B 1 49  ? -29.385 13.349  19.533  1.00 69.99  ?  49  PHE   B CE1  1 
ATOM   1406 C  CE2  . PHE   B 1 49  ? -28.786 15.398  18.461  1.00 63.89  ?  49  PHE   B CE2  1 
ATOM   1407 C  CZ   . PHE   B 1 49  ? -29.574 14.706  19.356  1.00 71.25  ?  49  PHE   B CZ   1 
ATOM   1408 N  N    . VAL   B 1 50  ? -28.816 12.533  14.384  1.00 59.54  ?  50  VAL   B N    1 
ATOM   1409 C  CA   . VAL   B 1 50  ? -29.532 13.280  13.359  1.00 67.19  ?  50  VAL   B CA   1 
ATOM   1410 C  C    . VAL   B 1 50  ? -30.986 13.335  13.805  1.00 77.89  ?  50  VAL   B C    1 
ATOM   1411 O  O    . VAL   B 1 50  ? -31.439 12.489  14.580  1.00 76.46  ?  50  VAL   B O    1 
ATOM   1412 C  CB   . VAL   B 1 50  ? -29.391 12.632  11.961  1.00 67.37  ?  50  VAL   B CB   1 
ATOM   1413 C  CG1  . VAL   B 1 50  ? -29.647 11.133  12.040  1.00 77.88  ?  50  VAL   B CG1  1 
ATOM   1414 C  CG2  . VAL   B 1 50  ? -30.324 13.294  10.957  1.00 65.85  ?  50  VAL   B CG2  1 
ATOM   1415 N  N    . HIS   B 1 51  ? -31.715 14.352  13.341  1.00 65.24  ?  51  HIS   B N    1 
ATOM   1416 C  CA   . HIS   B 1 51  ? -33.118 14.531  13.727  1.00 91.32  ?  51  HIS   B CA   1 
ATOM   1417 C  C    . HIS   B 1 51  ? -33.269 14.530  15.248  1.00 84.67  ?  51  HIS   B C    1 
ATOM   1418 O  O    . HIS   B 1 51  ? -34.263 14.064  15.810  1.00 88.45  ?  51  HIS   B O    1 
ATOM   1419 C  CB   . HIS   B 1 51  ? -34.007 13.472  13.053  1.00 83.10  ?  51  HIS   B CB   1 
ATOM   1420 C  CG   . HIS   B 1 51  ? -34.280 12.259  13.893  1.00 106.22 ?  51  HIS   B CG   1 
ATOM   1421 N  ND1  . HIS   B 1 51  ? -35.329 12.193  14.785  1.00 101.03 ?  51  HIS   B ND1  1 
ATOM   1422 C  CD2  . HIS   B 1 51  ? -33.669 11.050  13.944  1.00 99.96  ?  51  HIS   B CD2  1 
ATOM   1423 C  CE1  . HIS   B 1 51  ? -35.334 11.008  15.370  1.00 104.33 ?  51  HIS   B CE1  1 
ATOM   1424 N  NE2  . HIS   B 1 51  ? -34.336 10.296  14.878  1.00 103.16 ?  51  HIS   B NE2  1 
ATOM   1425 N  N    . GLY   B 1 52  ? -32.271 15.093  15.918  1.00 78.68  ?  52  GLY   B N    1 
ATOM   1426 C  CA   . GLY   B 1 52  ? -32.242 15.127  17.364  1.00 87.08  ?  52  GLY   B CA   1 
ATOM   1427 C  C    . GLY   B 1 52  ? -32.310 13.763  17.990  1.00 88.24  ?  52  GLY   B C    1 
ATOM   1428 O  O    . GLY   B 1 52  ? -32.691 13.640  19.157  1.00 84.89  ?  52  GLY   B O    1 
ATOM   1429 N  N    . GLU   B 1 53  ? -31.970 12.719  17.238  1.00 83.33  ?  53  GLU   B N    1 
ATOM   1430 C  CA   . GLU   B 1 53  ? -31.922 11.385  17.901  1.00 90.66  ?  53  GLU   B CA   1 
ATOM   1431 C  C    . GLU   B 1 53  ? -30.800 10.514  17.326  1.00 77.50  ?  53  GLU   B C    1 
ATOM   1432 O  O    . GLU   B 1 53  ? -30.448 10.688  16.154  1.00 66.61  ?  53  GLU   B O    1 
ATOM   1433 C  CB   . GLU   B 1 53  ? -33.264 10.663  17.807  1.00 96.80  ?  53  GLU   B CB   1 
ATOM   1434 C  CG   . GLU   B 1 53  ? -33.970 10.526  19.138  1.00 96.37  ?  53  GLU   B CG   1 
ATOM   1435 C  CD   . GLU   B 1 53  ? -35.326 11.206  19.180  1.00 108.47 ?  53  GLU   B CD   1 
ATOM   1436 O  OE1  . GLU   B 1 53  ? -35.358 12.449  19.220  1.00 112.94 ?  53  GLU   B OE1  1 
ATOM   1437 O  OE2  . GLU   B 1 53  ? -36.344 10.491  19.166  1.00 117.50 ?  53  GLU   B OE2  1 
ATOM   1438 N  N    . GLU   B 1 54  ? -30.281 9.607   18.148  1.00 80.78  ?  54  GLU   B N    1 
ATOM   1439 C  CA   . GLU   B 1 54  ? -29.208 8.695   17.690  1.00 84.96  ?  54  GLU   B CA   1 
ATOM   1440 C  C    . GLU   B 1 54  ? -29.791 7.700   16.689  1.00 80.80  ?  54  GLU   B C    1 
ATOM   1441 O  O    . GLU   B 1 54  ? -30.927 7.260   16.901  1.00 93.87  ?  54  GLU   B O    1 
ATOM   1442 C  CB   . GLU   B 1 54  ? -28.600 7.972   18.887  1.00 95.59  ?  54  GLU   B CB   1 
ATOM   1443 C  CG   . GLU   B 1 54  ? -27.629 8.817   19.691  1.00 100.41 ?  54  GLU   B CG   1 
ATOM   1444 C  CD   . GLU   B 1 54  ? -26.988 8.092   20.865  1.00 107.05 ?  54  GLU   B CD   1 
ATOM   1445 O  OE1  . GLU   B 1 54  ? -27.228 6.879   21.009  1.00 109.35 ?  54  GLU   B OE1  1 
ATOM   1446 O  OE2  . GLU   B 1 54  ? -26.253 8.742   21.633  1.00 90.96  ?  54  GLU   B OE2  1 
ATOM   1447 N  N    . ASP   B 1 55  ? -29.047 7.387   15.631  1.00 78.43  ?  55  ASP   B N    1 
ATOM   1448 C  CA   . ASP   B 1 55  ? -29.488 6.391   14.625  1.00 70.10  ?  55  ASP   B CA   1 
ATOM   1449 C  C    . ASP   B 1 55  ? -28.585 5.174   14.751  1.00 76.50  ?  55  ASP   B C    1 
ATOM   1450 O  O    . ASP   B 1 55  ? -27.473 5.215   14.222  1.00 85.32  ?  55  ASP   B O    1 
ATOM   1451 C  CB   . ASP   B 1 55  ? -29.424 6.941   13.206  1.00 73.46  ?  55  ASP   B CB   1 
ATOM   1452 C  CG   . ASP   B 1 55  ? -30.012 5.983   12.188  1.00 85.20  ?  55  ASP   B CG   1 
ATOM   1453 O  OD1  . ASP   B 1 55  ? -30.563 4.955   12.612  1.00 87.31  ?  55  ASP   B OD1  1 
ATOM   1454 O  OD2  . ASP   B 1 55  ? -29.917 6.274   10.984  1.00 96.26  ?  55  ASP   B OD2  1 
ATOM   1455 N  N    . LEU   B 1 56  ? -29.072 4.117   15.383  1.00 75.55  ?  56  LEU   B N    1 
ATOM   1456 C  CA   . LEU   B 1 56  ? -28.238 2.953   15.639  1.00 65.94  ?  56  LEU   B CA   1 
ATOM   1457 C  C    . LEU   B 1 56  ? -28.161 1.974   14.471  1.00 66.32  ?  56  LEU   B C    1 
ATOM   1458 O  O    . LEU   B 1 56  ? -27.298 1.090   14.487  1.00 74.10  ?  56  LEU   B O    1 
ATOM   1459 C  CB   . LEU   B 1 56  ? -28.755 2.213   16.874  1.00 80.61  ?  56  LEU   B CB   1 
ATOM   1460 C  CG   . LEU   B 1 56  ? -28.630 2.971   18.196  1.00 71.56  ?  56  LEU   B CG   1 
ATOM   1461 C  CD1  . LEU   B 1 56  ? -27.216 3.493   18.378  1.00 73.10  ?  56  LEU   B CD1  1 
ATOM   1462 C  CD2  . LEU   B 1 56  ? -29.648 4.102   18.282  1.00 81.28  ?  56  LEU   B CD2  1 
ATOM   1463 N  N    . LYS   B 1 57  ? -29.025 2.103   13.462  1.00 67.87  ?  57  LYS   B N    1 
ATOM   1464 C  CA   . LYS   B 1 57  ? -29.130 1.049   12.455  1.00 71.41  ?  57  LYS   B CA   1 
ATOM   1465 C  C    . LYS   B 1 57  ? -27.880 0.938   11.583  1.00 58.30  ?  57  LYS   B C    1 
ATOM   1466 O  O    . LYS   B 1 57  ? -27.595 -0.146  11.064  1.00 65.41  ?  57  LYS   B O    1 
ATOM   1467 C  CB   . LYS   B 1 57  ? -30.404 1.242   11.625  1.00 84.28  ?  57  LYS   B CB   1 
ATOM   1468 C  CG   . LYS   B 1 57  ? -30.546 2.547   10.865  1.00 74.66  ?  57  LYS   B CG   1 
ATOM   1469 C  CD   . LYS   B 1 57  ? -32.010 2.708   10.456  1.00 74.93  ?  57  LYS   B CD   1 
ATOM   1470 C  CE   . LYS   B 1 57  ? -32.292 4.029   9.766   1.00 77.69  ?  57  LYS   B CE   1 
ATOM   1471 N  NZ   . LYS   B 1 57  ? -33.313 3.870   8.693   1.00 90.89  ?  57  LYS   B NZ   1 
ATOM   1472 N  N    . VAL   B 1 58  ? -27.143 2.032   11.366  1.00 62.07  ?  58  VAL   B N    1 
ATOM   1473 C  CA   . VAL   B 1 58  ? -25.877 1.937   10.639  1.00 60.90  ?  58  VAL   B CA   1 
ATOM   1474 C  C    . VAL   B 1 58  ? -24.679 1.702   11.559  1.00 57.31  ?  58  VAL   B C    1 
ATOM   1475 O  O    . VAL   B 1 58  ? -23.544 1.604   11.071  1.00 56.85  ?  58  VAL   B O    1 
ATOM   1476 C  CB   . VAL   B 1 58  ? -25.637 3.189   9.767   1.00 61.46  ?  58  VAL   B CB   1 
ATOM   1477 C  CG1  . VAL   B 1 58  ? -25.311 4.393   10.631  1.00 65.01  ?  58  VAL   B CG1  1 
ATOM   1478 C  CG2  . VAL   B 1 58  ? -24.533 2.926   8.746   1.00 74.87  ?  58  VAL   B CG2  1 
ATOM   1479 N  N    . GLN   B 1 59  ? -24.892 1.608   12.872  1.00 58.31  ?  59  GLN   B N    1 
ATOM   1480 C  CA   . GLN   B 1 59  ? -23.783 1.498   13.817  1.00 57.63  ?  59  GLN   B CA   1 
ATOM   1481 C  C    . GLN   B 1 59  ? -22.978 0.215   13.633  1.00 51.91  ?  59  GLN   B C    1 
ATOM   1482 O  O    . GLN   B 1 59  ? -23.536 -0.881  13.530  1.00 66.96  ?  59  GLN   B O    1 
ATOM   1483 C  CB   . GLN   B 1 59  ? -24.304 1.590   15.250  1.00 61.56  ?  59  GLN   B CB   1 
ATOM   1484 C  CG   . GLN   B 1 59  ? -23.230 1.365   16.300  1.00 65.93  ?  59  GLN   B CG   1 
ATOM   1485 C  CD   . GLN   B 1 59  ? -23.786 1.373   17.705  1.00 66.36  ?  59  GLN   B CD   1 
ATOM   1486 O  OE1  . GLN   B 1 59  ? -23.794 0.351   18.386  1.00 80.90  ?  59  GLN   B OE1  1 
ATOM   1487 N  NE2  . GLN   B 1 59  ? -24.247 2.535   18.153  1.00 72.36  ?  59  GLN   B NE2  1 
ATOM   1488 N  N    . HIS   B 1 60  ? -21.653 0.364   13.613  1.00 58.26  ?  60  HIS   B N    1 
ATOM   1489 C  CA   . HIS   B 1 60  ? -20.751 -0.757  13.387  1.00 56.29  ?  60  HIS   B CA   1 
ATOM   1490 C  C    . HIS   B 1 60  ? -20.832 -1.736  14.556  1.00 57.47  ?  60  HIS   B C    1 
ATOM   1491 O  O    . HIS   B 1 60  ? -20.933 -1.333  15.718  1.00 65.90  ?  60  HIS   B O    1 
ATOM   1492 C  CB   . HIS   B 1 60  ? -19.326 -0.221  13.207  1.00 63.65  ?  60  HIS   B CB   1 
ATOM   1493 C  CG   . HIS   B 1 60  ? -18.306 -1.259  12.850  1.00 57.48  ?  60  HIS   B CG   1 
ATOM   1494 N  ND1  . HIS   B 1 60  ? -17.812 -2.170  13.760  1.00 66.23  ?  60  HIS   B ND1  1 
ATOM   1495 C  CD2  . HIS   B 1 60  ? -17.661 -1.504  11.685  1.00 62.11  ?  60  HIS   B CD2  1 
ATOM   1496 C  CE1  . HIS   B 1 60  ? -16.919 -2.941  13.166  1.00 51.81  ?  60  HIS   B CE1  1 
ATOM   1497 N  NE2  . HIS   B 1 60  ? -16.809 -2.559  11.906  1.00 58.67  ?  60  HIS   B NE2  1 
ATOM   1498 N  N    . SER   B 1 61  ? -20.779 -3.035  14.240  1.00 58.63  ?  61  SER   B N    1 
ATOM   1499 C  CA   . SER   B 1 61  ? -21.067 -4.061  15.242  1.00 58.21  ?  61  SER   B CA   1 
ATOM   1500 C  C    . SER   B 1 61  ? -20.117 -3.981  16.434  1.00 71.38  ?  61  SER   B C    1 
ATOM   1501 O  O    . SER   B 1 61  ? -20.528 -4.210  17.577  1.00 61.62  ?  61  SER   B O    1 
ATOM   1502 C  CB   . SER   B 1 61  ? -21.027 -5.452  14.606  1.00 61.14  ?  61  SER   B CB   1 
ATOM   1503 O  OG   . SER   B 1 61  ? -19.700 -5.878  14.365  1.00 75.61  ?  61  SER   B OG   1 
ATOM   1504 N  N    . SER   B 1 62  ? -18.839 -3.678  16.192  1.00 60.17  ?  62  SER   B N    1 
ATOM   1505 C  CA   . SER   B 1 62  ? -17.854 -3.697  17.271  1.00 65.34  ?  62  SER   B CA   1 
ATOM   1506 C  C    . SER   B 1 62  ? -18.115 -2.638  18.327  1.00 62.99  ?  62  SER   B C    1 
ATOM   1507 O  O    . SER   B 1 62  ? -17.540 -2.716  19.421  1.00 57.75  ?  62  SER   B O    1 
ATOM   1508 C  CB   . SER   B 1 62  ? -16.449 -3.498  16.714  1.00 63.50  ?  62  SER   B CB   1 
ATOM   1509 O  OG   . SER   B 1 62  ? -16.268 -2.167  16.260  1.00 64.67  ?  62  SER   B OG   1 
ATOM   1510 N  N    . TYR   B 1 63  ? -18.982 -1.673  18.035  1.00 60.52  ?  63  TYR   B N    1 
ATOM   1511 C  CA   . TYR   B 1 63  ? -19.283 -0.588  18.952  1.00 64.01  ?  63  TYR   B CA   1 
ATOM   1512 C  C    . TYR   B 1 63  ? -20.690 -0.687  19.510  1.00 63.78  ?  63  TYR   B C    1 
ATOM   1513 O  O    . TYR   B 1 63  ? -21.083 0.176   20.299  1.00 66.43  ?  63  TYR   B O    1 
ATOM   1514 C  CB   . TYR   B 1 63  ? -19.087 0.760   18.241  1.00 51.92  ?  63  TYR   B CB   1 
ATOM   1515 C  CG   . TYR   B 1 63  ? -17.643 1.111   18.068  1.00 57.92  ?  63  TYR   B CG   1 
ATOM   1516 C  CD1  . TYR   B 1 63  ? -16.906 1.624   19.118  1.00 44.18  ?  63  TYR   B CD1  1 
ATOM   1517 C  CD2  . TYR   B 1 63  ? -17.006 0.886   16.859  1.00 58.41  ?  63  TYR   B CD2  1 
ATOM   1518 C  CE1  . TYR   B 1 63  ? -15.577 1.934   18.964  1.00 63.88  ?  63  TYR   B CE1  1 
ATOM   1519 C  CE2  . TYR   B 1 63  ? -15.677 1.191   16.691  1.00 49.36  ?  63  TYR   B CE2  1 
ATOM   1520 C  CZ   . TYR   B 1 63  ? -14.965 1.716   17.749  1.00 54.27  ?  63  TYR   B CZ   1 
ATOM   1521 O  OH   . TYR   B 1 63  ? -13.635 2.027   17.596  1.00 50.46  ?  63  TYR   B OH   1 
ATOM   1522 N  N    . ARG   B 1 64  ? -21.375 -1.790  19.235  1.00 68.21  ?  64  ARG   B N    1 
ATOM   1523 C  CA   . ARG   B 1 64  ? -22.780 -1.916  19.694  1.00 78.34  ?  64  ARG   B CA   1 
ATOM   1524 C  C    . ARG   B 1 64  ? -22.806 -2.101  21.211  1.00 72.86  ?  64  ARG   B C    1 
ATOM   1525 O  O    . ARG   B 1 64  ? -21.965 -2.859  21.718  1.00 59.22  ?  64  ARG   B O    1 
ATOM   1526 C  CB   . ARG   B 1 64  ? -23.506 -3.039  18.947  1.00 78.39  ?  64  ARG   B CB   1 
ATOM   1527 C  CG   . ARG   B 1 64  ? -23.046 -4.442  19.311  1.00 90.00  ?  64  ARG   B CG   1 
ATOM   1528 C  CD   . ARG   B 1 64  ? -23.429 -5.441  18.237  1.00 91.32  ?  64  ARG   B CD   1 
ATOM   1529 N  NE   . ARG   B 1 64  ? -24.490 -4.937  17.377  1.00 89.41  ?  64  ARG   B NE   1 
ATOM   1530 N  N    . GLN   B 1 65  ? -23.721 -1.407  21.885  1.00 68.47  ?  65  GLN   B N    1 
ATOM   1531 C  CA   . GLN   B 1 65  ? -23.877 -1.516  23.358  1.00 69.98  ?  65  GLN   B CA   1 
ATOM   1532 C  C    . GLN   B 1 65  ? -22.673 -0.911  24.091  1.00 68.68  ?  65  GLN   B C    1 
ATOM   1533 O  O    . GLN   B 1 65  ? -22.550 -1.177  25.290  1.00 72.16  ?  65  GLN   B O    1 
ATOM   1534 C  CB   . GLN   B 1 65  ? -24.091 -2.975  23.759  1.00 78.81  ?  65  GLN   B CB   1 
ATOM   1535 C  CG   . GLN   B 1 65  ? -25.392 -3.564  23.242  1.00 95.29  ?  65  GLN   B CG   1 
ATOM   1536 C  CD   . GLN   B 1 65  ? -26.589 -2.840  23.806  1.00 112.22 ?  65  GLN   B CD   1 
ATOM   1537 O  OE1  . GLN   B 1 65  ? -26.843 -2.863  25.009  1.00 118.74 ?  65  GLN   B OE1  1 
ATOM   1538 N  NE2  . GLN   B 1 65  ? -27.334 -2.181  22.934  1.00 119.97 ?  65  GLN   B NE2  1 
ATOM   1539 N  N    . ARG   B 1 66  ? -21.846 -0.104  23.422  1.00 50.05  ?  66  ARG   B N    1 
ATOM   1540 C  CA   . ARG   B 1 66  ? -20.615 0.405   24.085  1.00 54.55  ?  66  ARG   B CA   1 
ATOM   1541 C  C    . ARG   B 1 66  ? -20.409 1.900   23.815  1.00 50.41  ?  66  ARG   B C    1 
ATOM   1542 O  O    . ARG   B 1 66  ? -19.582 2.500   24.506  1.00 45.93  ?  66  ARG   B O    1 
ATOM   1543 C  CB   . ARG   B 1 66  ? -19.404 -0.412  23.626  1.00 50.55  ?  66  ARG   B CB   1 
ATOM   1544 C  CG   . ARG   B 1 66  ? -19.175 -1.695  24.408  1.00 54.10  ?  66  ARG   B CG   1 
ATOM   1545 C  CD   . ARG   B 1 66  ? -17.771 -2.243  24.234  1.00 53.34  ?  66  ARG   B CD   1 
ATOM   1546 N  NE   . ARG   B 1 66  ? -17.239 -2.007  22.902  1.00 52.87  ?  66  ARG   B NE   1 
ATOM   1547 C  CZ   . ARG   B 1 66  ? -16.116 -1.349  22.648  1.00 56.11  ?  66  ARG   B CZ   1 
ATOM   1548 N  NH1  . ARG   B 1 66  ? -15.395 -0.858  23.640  1.00 40.02  ?  66  ARG   B NH1  1 
ATOM   1549 N  NH2  . ARG   B 1 66  ? -15.718 -1.184  21.400  1.00 51.94  ?  66  ARG   B NH2  1 
ATOM   1550 N  N    . ALA   B 1 67  ? -21.134 2.481   22.861  1.00 45.74  ?  67  ALA   B N    1 
ATOM   1551 C  CA   . ALA   B 1 67  ? -20.895 3.867   22.521  1.00 44.20  ?  67  ALA   B CA   1 
ATOM   1552 C  C    . ALA   B 1 67  ? -22.144 4.686   22.798  1.00 46.24  ?  67  ALA   B C    1 
ATOM   1553 O  O    . ALA   B 1 67  ? -23.264 4.243   22.519  1.00 52.15  ?  67  ALA   B O    1 
ATOM   1554 C  CB   . ALA   B 1 67  ? -20.505 3.997   21.049  1.00 43.78  ?  67  ALA   B CB   1 
ATOM   1555 N  N    . ARG   B 1 68  ? -21.952 5.870   23.375  1.00 44.65  ?  68  ARG   B N    1 
ATOM   1556 C  CA   . ARG   B 1 68  ? -23.060 6.800   23.512  1.00 48.25  ?  68  ARG   B CA   1 
ATOM   1557 C  C    . ARG   B 1 68  ? -22.565 8.228   23.339  1.00 57.67  ?  68  ARG   B C    1 
ATOM   1558 O  O    . ARG   B 1 68  ? -21.390 8.537   23.563  1.00 47.15  ?  68  ARG   B O    1 
ATOM   1559 C  CB   . ARG   B 1 68  ? -23.770 6.623   24.861  1.00 52.74  ?  68  ARG   B CB   1 
ATOM   1560 C  CG   . ARG   B 1 68  ? -22.898 6.816   26.091  1.00 74.34  ?  68  ARG   B CG   1 
ATOM   1561 C  CD   . ARG   B 1 68  ? -23.648 6.379   27.346  1.00 71.47  ?  68  ARG   B CD   1 
ATOM   1562 N  NE   . ARG   B 1 68  ? -25.046 6.795   27.321  1.00 82.00  ?  68  ARG   B NE   1 
ATOM   1563 C  CZ   . ARG   B 1 68  ? -25.458 8.053   27.386  1.00 94.01  ?  68  ARG   B CZ   1 
ATOM   1564 N  NH1  . ARG   B 1 68  ? -24.634 9.035   27.714  1.00 89.92  ?  68  ARG   B NH1  1 
ATOM   1565 N  NH2  . ARG   B 1 68  ? -26.744 8.325   27.184  1.00 104.80 ?  68  ARG   B NH2  1 
ATOM   1566 N  N    . LEU   B 1 69  ? -23.475 9.085   22.892  1.00 53.08  ?  69  LEU   B N    1 
ATOM   1567 C  CA   . LEU   B 1 69  ? -23.234 10.514  22.778  1.00 49.62  ?  69  LEU   B CA   1 
ATOM   1568 C  C    . LEU   B 1 69  ? -23.774 11.194  24.030  1.00 65.83  ?  69  LEU   B C    1 
ATOM   1569 O  O    . LEU   B 1 69  ? -24.895 10.904  24.460  1.00 69.35  ?  69  LEU   B O    1 
ATOM   1570 C  CB   . LEU   B 1 69  ? -23.897 11.072  21.516  1.00 59.69  ?  69  LEU   B CB   1 
ATOM   1571 C  CG   . LEU   B 1 69  ? -23.346 12.381  20.948  1.00 56.23  ?  69  LEU   B CG   1 
ATOM   1572 C  CD1  . LEU   B 1 69  ? -23.606 13.547  21.884  1.00 81.48  ?  69  LEU   B CD1  1 
ATOM   1573 C  CD2  . LEU   B 1 69  ? -21.858 12.238  20.664  1.00 61.59  ?  69  LEU   B CD2  1 
ATOM   1574 N  N    . LEU   B 1 70  ? -22.982 12.088  24.617  1.00 56.92  ?  70  LEU   B N    1 
ATOM   1575 C  CA   . LEU   B 1 70  ? -23.416 12.827  25.802  1.00 68.75  ?  70  LEU   B CA   1 
ATOM   1576 C  C    . LEU   B 1 70  ? -24.316 13.972  25.350  1.00 70.42  ?  70  LEU   B C    1 
ATOM   1577 O  O    . LEU   B 1 70  ? -23.838 15.033  24.943  1.00 82.05  ?  70  LEU   B O    1 
ATOM   1578 C  CB   . LEU   B 1 70  ? -22.212 13.328  26.593  1.00 67.44  ?  70  LEU   B CB   1 
ATOM   1579 C  CG   . LEU   B 1 70  ? -21.103 12.313  26.893  1.00 69.32  ?  70  LEU   B CG   1 
ATOM   1580 C  CD1  . LEU   B 1 70  ? -20.320 12.717  28.136  1.00 56.02  ?  70  LEU   B CD1  1 
ATOM   1581 C  CD2  . LEU   B 1 70  ? -21.667 10.907  27.052  1.00 72.75  ?  70  LEU   B CD2  1 
ATOM   1582 N  N    . LYS   B 1 71  ? -25.632 13.753  25.427  1.00 73.06  ?  71  LYS   B N    1 
ATOM   1583 C  CA   . LYS   B 1 71  ? -26.588 14.650  24.782  1.00 78.57  ?  71  LYS   B CA   1 
ATOM   1584 C  C    . LYS   B 1 71  ? -26.748 15.969  25.526  1.00 87.72  ?  71  LYS   B C    1 
ATOM   1585 O  O    . LYS   B 1 71  ? -26.913 17.020  24.896  1.00 94.39  ?  71  LYS   B O    1 
ATOM   1586 C  CB   . LYS   B 1 71  ? -27.947 13.962  24.654  1.00 82.83  ?  71  LYS   B CB   1 
ATOM   1587 C  CG   . LYS   B 1 71  ? -27.955 12.763  23.728  1.00 84.40  ?  71  LYS   B CG   1 
ATOM   1588 C  CD   . LYS   B 1 71  ? -29.159 11.878  24.002  1.00 102.76 ?  71  LYS   B CD   1 
ATOM   1589 C  CE   . LYS   B 1 71  ? -28.962 11.054  25.264  1.00 100.10 ?  71  LYS   B CE   1 
ATOM   1590 N  NZ   . LYS   B 1 71  ? -30.107 10.135  25.509  1.00 113.00 ?  71  LYS   B NZ   1 
ATOM   1591 N  N    . ASP   B 1 72  ? -26.712 15.945  26.860  1.00 87.02  ?  72  ASP   B N    1 
ATOM   1592 C  CA   . ASP   B 1 72  ? -26.930 17.182  27.600  1.00 105.48 ?  72  ASP   B CA   1 
ATOM   1593 C  C    . ASP   B 1 72  ? -25.898 18.236  27.210  1.00 107.42 ?  72  ASP   B C    1 
ATOM   1594 O  O    . ASP   B 1 72  ? -26.206 19.431  27.168  1.00 117.69 ?  72  ASP   B O    1 
ATOM   1595 C  CB   . ASP   B 1 72  ? -26.907 16.916  29.109  1.00 106.70 ?  72  ASP   B CB   1 
ATOM   1596 C  CG   . ASP   B 1 72  ? -25.504 16.765  29.661  1.00 119.87 ?  72  ASP   B CG   1 
ATOM   1597 O  OD1  . ASP   B 1 72  ? -24.802 17.792  29.789  1.00 110.04 ?  72  ASP   B OD1  1 
ATOM   1598 O  OD2  . ASP   B 1 72  ? -25.102 15.625  29.970  1.00 130.32 ?  72  ASP   B OD2  1 
ATOM   1599 N  N    . GLN   B 1 73  ? -24.671 17.811  26.913  1.00 102.30 ?  73  GLN   B N    1 
ATOM   1600 C  CA   . GLN   B 1 73  ? -23.586 18.740  26.618  1.00 98.22  ?  73  GLN   B CA   1 
ATOM   1601 C  C    . GLN   B 1 73  ? -23.680 19.367  25.231  1.00 79.03  ?  73  GLN   B C    1 
ATOM   1602 O  O    . GLN   B 1 73  ? -22.944 20.320  24.954  1.00 74.93  ?  73  GLN   B O    1 
ATOM   1603 C  CB   . GLN   B 1 73  ? -22.250 18.015  26.761  1.00 97.77  ?  73  GLN   B CB   1 
ATOM   1604 C  CG   . GLN   B 1 73  ? -21.077 18.896  27.165  1.00 105.90 ?  73  GLN   B CG   1 
ATOM   1605 C  CD   . GLN   B 1 73  ? -20.955 19.071  28.668  1.00 92.11  ?  73  GLN   B CD   1 
ATOM   1606 O  OE1  . GLN   B 1 73  ? -21.669 18.433  29.442  1.00 103.47 ?  73  GLN   B OE1  1 
ATOM   1607 N  NE2  . GLN   B 1 73  ? -20.024 19.919  29.087  1.00 92.93  ?  73  GLN   B NE2  1 
ATOM   1608 N  N    . LEU   B 1 74  ? -24.555 18.862  24.359  1.00 77.88  ?  74  LEU   B N    1 
ATOM   1609 C  CA   . LEU   B 1 74  ? -24.680 19.437  23.024  1.00 75.50  ?  74  LEU   B CA   1 
ATOM   1610 C  C    . LEU   B 1 74  ? -24.988 20.922  23.116  1.00 85.38  ?  74  LEU   B C    1 
ATOM   1611 O  O    . LEU   B 1 74  ? -24.421 21.738  22.380  1.00 67.60  ?  74  LEU   B O    1 
ATOM   1612 C  CB   . LEU   B 1 74  ? -25.799 18.724  22.270  1.00 58.44  ?  74  LEU   B CB   1 
ATOM   1613 C  CG   . LEU   B 1 74  ? -25.573 17.239  22.016  1.00 63.57  ?  74  LEU   B CG   1 
ATOM   1614 C  CD1  . LEU   B 1 74  ? -26.650 16.693  21.092  1.00 62.22  ?  74  LEU   B CD1  1 
ATOM   1615 C  CD2  . LEU   B 1 74  ? -24.179 16.980  21.476  1.00 71.31  ?  74  LEU   B CD2  1 
ATOM   1616 N  N    . SER   B 1 75  ? -25.870 21.283  24.046  1.00 79.14  ?  75  SER   B N    1 
ATOM   1617 C  CA   . SER   B 1 75  ? -26.264 22.670  24.257  1.00 81.48  ?  75  SER   B CA   1 
ATOM   1618 C  C    . SER   B 1 75  ? -25.087 23.561  24.596  1.00 89.56  ?  75  SER   B C    1 
ATOM   1619 O  O    . SER   B 1 75  ? -25.123 24.764  24.318  1.00 92.20  ?  75  SER   B O    1 
ATOM   1620 C  CB   . SER   B 1 75  ? -27.328 22.714  25.341  1.00 91.90  ?  75  SER   B CB   1 
ATOM   1621 O  OG   . SER   B 1 75  ? -27.321 23.932  26.065  1.00 94.69  ?  75  SER   B OG   1 
ATOM   1622 N  N    . LEU   B 1 76  ? -24.046 22.996  25.186  1.00 82.13  ?  76  LEU   B N    1 
ATOM   1623 C  CA   . LEU   B 1 76  ? -22.855 23.745  25.532  1.00 84.68  ?  76  LEU   B CA   1 
ATOM   1624 C  C    . LEU   B 1 76  ? -21.854 23.790  24.385  1.00 81.72  ?  76  LEU   B C    1 
ATOM   1625 O  O    . LEU   B 1 76  ? -20.796 24.411  24.524  1.00 86.77  ?  76  LEU   B O    1 
ATOM   1626 C  CB   . LEU   B 1 76  ? -22.216 23.136  26.782  1.00 85.91  ?  76  LEU   B CB   1 
ATOM   1627 C  CG   . LEU   B 1 76  ? -23.024 23.351  28.065  1.00 86.77  ?  76  LEU   B CG   1 
ATOM   1628 C  CD1  . LEU   B 1 76  ? -22.709 22.275  29.102  1.00 89.06  ?  76  LEU   B CD1  1 
ATOM   1629 C  CD2  . LEU   B 1 76  ? -22.795 24.744  28.630  1.00 73.34  ?  76  LEU   B CD2  1 
ATOM   1630 N  N    . GLY   B 1 77  ? -22.169 23.154  23.260  1.00 63.51  ?  77  GLY   B N    1 
ATOM   1631 C  CA   . GLY   B 1 77  ? -21.231 23.033  22.161  1.00 63.60  ?  77  GLY   B CA   1 
ATOM   1632 C  C    . GLY   B 1 77  ? -20.214 21.927  22.321  1.00 68.51  ?  77  GLY   B C    1 
ATOM   1633 O  O    . GLY   B 1 77  ? -19.056 22.093  21.919  1.00 65.97  ?  77  GLY   B O    1 
ATOM   1634 N  N    . ASN   B 1 78  ? -20.611 20.795  22.901  1.00 69.85  ?  78  ASN   B N    1 
ATOM   1635 C  CA   . ASN   B 1 78  ? -19.702 19.681  23.152  1.00 73.47  ?  78  ASN   B CA   1 
ATOM   1636 C  C    . ASN   B 1 78  ? -20.370 18.389  22.700  1.00 74.89  ?  78  ASN   B C    1 
ATOM   1637 O  O    . ASN   B 1 78  ? -21.319 17.923  23.339  1.00 67.93  ?  78  ASN   B O    1 
ATOM   1638 C  CB   . ASN   B 1 78  ? -19.323 19.608  24.630  1.00 73.55  ?  78  ASN   B CB   1 
ATOM   1639 C  CG   . ASN   B 1 78  ? -17.939 19.039  24.851  1.00 89.28  ?  78  ASN   B CG   1 
ATOM   1640 O  OD1  . ASN   B 1 78  ? -17.238 19.430  25.783  1.00 92.53  ?  78  ASN   B OD1  1 
ATOM   1641 N  ND2  . ASN   B 1 78  ? -17.533 18.114  23.989  1.00 78.34  ?  78  ASN   B ND2  1 
ATOM   1642 N  N    . ALA   B 1 79  ? -19.880 17.815  21.603  1.00 63.93  ?  79  ALA   B N    1 
ATOM   1643 C  CA   . ALA   B 1 79  ? -20.311 16.496  21.140  1.00 62.89  ?  79  ALA   B CA   1 
ATOM   1644 C  C    . ALA   B 1 79  ? -19.289 15.491  21.658  1.00 69.23  ?  79  ALA   B C    1 
ATOM   1645 O  O    . ALA   B 1 79  ? -18.312 15.163  20.984  1.00 80.96  ?  79  ALA   B O    1 
ATOM   1646 C  CB   . ALA   B 1 79  ? -20.435 16.458  19.622  1.00 62.35  ?  79  ALA   B CB   1 
ATOM   1647 N  N    . ALA   B 1 80  ? -19.537 14.980  22.859  1.00 56.33  ?  80  ALA   B N    1 
ATOM   1648 C  CA   . ALA   B 1 80  ? -18.623 14.058  23.516  1.00 54.83  ?  80  ALA   B CA   1 
ATOM   1649 C  C    . ALA   B 1 80  ? -19.040 12.619  23.248  1.00 48.10  ?  80  ALA   B C    1 
ATOM   1650 O  O    . ALA   B 1 80  ? -20.205 12.256  23.437  1.00 52.68  ?  80  ALA   B O    1 
ATOM   1651 C  CB   . ALA   B 1 80  ? -18.579 14.324  25.021  1.00 56.10  ?  80  ALA   B CB   1 
ATOM   1652 N  N    . LEU   B 1 81  ? -18.091 11.811  22.788  1.00 44.07  ?  81  LEU   B N    1 
ATOM   1653 C  CA   . LEU   B 1 81  ? -18.309 10.385  22.590  1.00 47.74  ?  81  LEU   B CA   1 
ATOM   1654 C  C    . LEU   B 1 81  ? -17.766 9.628   23.794  1.00 46.27  ?  81  LEU   B C    1 
ATOM   1655 O  O    . LEU   B 1 81  ? -16.591 9.781   24.152  1.00 37.62  ?  81  LEU   B O    1 
ATOM   1656 C  CB   . LEU   B 1 81  ? -17.634 9.894   21.310  1.00 39.95  ?  81  LEU   B CB   1 
ATOM   1657 C  CG   . LEU   B 1 81  ? -17.601 8.370   21.166  1.00 44.34  ?  81  LEU   B CG   1 
ATOM   1658 C  CD1  . LEU   B 1 81  ? -18.997 7.811   20.921  1.00 47.79  ?  81  LEU   B CD1  1 
ATOM   1659 C  CD2  . LEU   B 1 81  ? -16.647 7.949   20.060  1.00 43.90  ?  81  LEU   B CD2  1 
ATOM   1660 N  N    . GLN   B 1 82  ? -18.620 8.823   24.420  1.00 37.14  ?  82  GLN   B N    1 
ATOM   1661 C  CA   . GLN   B 1 82  ? -18.218 7.955   25.514  1.00 47.29  ?  82  GLN   B CA   1 
ATOM   1662 C  C    . GLN   B 1 82  ? -18.241 6.514   25.028  1.00 42.69  ?  82  GLN   B C    1 
ATOM   1663 O  O    . GLN   B 1 82  ? -19.235 6.065   24.443  1.00 45.81  ?  82  GLN   B O    1 
ATOM   1664 C  CB   . GLN   B 1 82  ? -19.138 8.121   26.723  1.00 51.49  ?  82  GLN   B CB   1 
ATOM   1665 C  CG   . GLN   B 1 82  ? -18.810 7.184   27.873  1.00 48.40  ?  82  GLN   B CG   1 
ATOM   1666 C  CD   . GLN   B 1 82  ? -19.818 7.273   28.998  1.00 70.51  ?  82  GLN   B CD   1 
ATOM   1667 O  OE1  . GLN   B 1 82  ? -20.953 6.816   28.865  1.00 73.05  ?  82  GLN   B OE1  1 
ATOM   1668 N  NE2  . GLN   B 1 82  ? -19.407 7.858   30.117  1.00 74.84  ?  82  GLN   B NE2  1 
ATOM   1669 N  N    . ILE   B 1 83  ? -17.145 5.802   25.264  1.00 42.43  ?  83  ILE   B N    1 
ATOM   1670 C  CA   . ILE   B 1 83  ? -17.014 4.395   24.918  1.00 37.24  ?  83  ILE   B CA   1 
ATOM   1671 C  C    . ILE   B 1 83  ? -16.682 3.633   26.191  1.00 46.96  ?  83  ILE   B C    1 
ATOM   1672 O  O    . ILE   B 1 83  ? -15.725 3.977   26.897  1.00 44.10  ?  83  ILE   B O    1 
ATOM   1673 C  CB   . ILE   B 1 83  ? -15.939 4.173   23.839  1.00 47.51  ?  83  ILE   B CB   1 
ATOM   1674 C  CG1  . ILE   B 1 83  ? -16.481 4.567   22.464  1.00 49.46  ?  83  ILE   B CG1  1 
ATOM   1675 C  CG2  . ILE   B 1 83  ? -15.468 2.725   23.844  1.00 50.72  ?  83  ILE   B CG2  1 
ATOM   1676 C  CD1  . ILE   B 1 83  ? -15.499 5.348   21.620  1.00 66.39  ?  83  ILE   B CD1  1 
ATOM   1677 N  N    . THR   B 1 84  ? -17.475 2.608   26.482  1.00 41.44  ?  84  THR   B N    1 
ATOM   1678 C  CA   . THR   B 1 84  ? -17.351 1.824   27.701  1.00 42.59  ?  84  THR   B CA   1 
ATOM   1679 C  C    . THR   B 1 84  ? -16.612 0.528   27.402  1.00 48.87  ?  84  THR   B C    1 
ATOM   1680 O  O    . THR   B 1 84  ? -16.786 -0.063  26.333  1.00 48.91  ?  84  THR   B O    1 
ATOM   1681 C  CB   . THR   B 1 84  ? -18.729 1.511   28.289  1.00 48.07  ?  84  THR   B CB   1 
ATOM   1682 O  OG1  . THR   B 1 84  ? -19.352 2.725   28.726  1.00 55.72  ?  84  THR   B OG1  1 
ATOM   1683 C  CG2  . THR   B 1 84  ? -18.603 0.555   29.466  1.00 55.69  ?  84  THR   B CG2  1 
ATOM   1684 N  N    . ASP   B 1 85  ? -15.787 0.087   28.351  1.00 46.56  ?  85  ASP   B N    1 
ATOM   1685 C  CA   . ASP   B 1 85  ? -15.111 -1.201  28.235  1.00 39.07  ?  85  ASP   B CA   1 
ATOM   1686 C  C    . ASP   B 1 85  ? -14.194 -1.207  27.009  1.00 37.40  ?  85  ASP   B C    1 
ATOM   1687 O  O    . ASP   B 1 85  ? -14.362 -1.985  26.068  1.00 48.15  ?  85  ASP   B O    1 
ATOM   1688 C  CB   . ASP   B 1 85  ? -16.146 -2.331  28.177  1.00 48.70  ?  85  ASP   B CB   1 
ATOM   1689 C  CG   . ASP   B 1 85  ? -15.541 -3.699  28.409  1.00 59.63  ?  85  ASP   B CG   1 
ATOM   1690 O  OD1  . ASP   B 1 85  ? -14.571 -3.801  29.189  1.00 58.95  ?  85  ASP   B OD1  1 
ATOM   1691 O  OD2  . ASP   B 1 85  ? -16.053 -4.676  27.823  1.00 66.32  ?  85  ASP   B OD2  1 
ATOM   1692 N  N    . VAL   B 1 86  ? -13.207 -0.308  27.043  1.00 36.88  ?  86  VAL   B N    1 
ATOM   1693 C  CA   . VAL   B 1 86  ? -12.333 -0.096  25.894  1.00 33.33  ?  86  VAL   B CA   1 
ATOM   1694 C  C    . VAL   B 1 86  ? -11.606 -1.384  25.534  1.00 45.24  ?  86  VAL   B C    1 
ATOM   1695 O  O    . VAL   B 1 86  ? -11.070 -2.085  26.403  1.00 44.33  ?  86  VAL   B O    1 
ATOM   1696 C  CB   . VAL   B 1 86  ? -11.342 1.040   26.188  1.00 37.17  ?  86  VAL   B CB   1 
ATOM   1697 C  CG1  . VAL   B 1 86  ? -10.230 1.064   25.149  1.00 37.23  ?  86  VAL   B CG1  1 
ATOM   1698 C  CG2  . VAL   B 1 86  ? -12.065 2.375   26.232  1.00 36.38  ?  86  VAL   B CG2  1 
ATOM   1699 N  N    . LYS   B 1 87  ? -11.575 -1.690  24.240  1.00 36.77  ?  87  LYS   B N    1 
ATOM   1700 C  CA   . LYS   B 1 87  ? -10.886 -2.847  23.687  1.00 39.09  ?  87  LYS   B CA   1 
ATOM   1701 C  C    . LYS   B 1 87  ? -9.641  -2.399  22.931  1.00 38.42  ?  87  LYS   B C    1 
ATOM   1702 O  O    . LYS   B 1 87  ? -9.457  -1.217  22.627  1.00 37.54  ?  87  LYS   B O    1 
ATOM   1703 C  CB   . LYS   B 1 87  ? -11.813 -3.638  22.755  1.00 43.29  ?  87  LYS   B CB   1 
ATOM   1704 C  CG   . LYS   B 1 87  ? -13.099 -4.134  23.399  1.00 55.41  ?  87  LYS   B CG   1 
ATOM   1705 C  CD   . LYS   B 1 87  ? -12.835 -4.853  24.712  1.00 56.65  ?  87  LYS   B CD   1 
ATOM   1706 C  CE   . LYS   B 1 87  ? -14.016 -5.731  25.099  1.00 66.73  ?  87  LYS   B CE   1 
ATOM   1707 N  NZ   . LYS   B 1 87  ? -13.604 -6.886  25.943  1.00 70.46  ?  87  LYS   B NZ   1 
ATOM   1708 N  N    . LEU   B 1 88  ? -8.777  -3.369  22.617  1.00 33.49  ?  88  LEU   B N    1 
ATOM   1709 C  CA   . LEU   B 1 88  ? -7.597  -3.063  21.816  1.00 39.70  ?  88  LEU   B CA   1 
ATOM   1710 C  C    . LEU   B 1 88  ? -7.973  -2.603  20.414  1.00 37.19  ?  88  LEU   B C    1 
ATOM   1711 O  O    . LEU   B 1 88  ? -7.280  -1.760  19.833  1.00 35.61  ?  88  LEU   B O    1 
ATOM   1712 C  CB   . LEU   B 1 88  ? -6.673  -4.278  21.744  1.00 47.43  ?  88  LEU   B CB   1 
ATOM   1713 C  CG   . LEU   B 1 88  ? -5.707  -4.442  22.919  1.00 52.04  ?  88  LEU   B CG   1 
ATOM   1714 C  CD1  . LEU   B 1 88  ? -5.144  -5.854  22.961  1.00 44.93  ?  88  LEU   B CD1  1 
ATOM   1715 C  CD2  . LEU   B 1 88  ? -4.591  -3.409  22.839  1.00 49.22  ?  88  LEU   B CD2  1 
ATOM   1716 N  N    . GLN   B 1 89  ? -9.065  -3.130  19.860  1.00 37.36  ?  89  GLN   B N    1 
ATOM   1717 C  CA   . GLN   B 1 89  ? -9.496  -2.720  18.528  1.00 39.86  ?  89  GLN   B CA   1 
ATOM   1718 C  C    . GLN   B 1 89  ? -10.033 -1.297  18.502  1.00 48.23  ?  89  GLN   B C    1 
ATOM   1719 O  O    . GLN   B 1 89  ? -10.278 -0.767  17.413  1.00 36.12  ?  89  GLN   B O    1 
ATOM   1720 C  CB   . GLN   B 1 89  ? -10.553 -3.687  17.993  1.00 39.70  ?  89  GLN   B CB   1 
ATOM   1721 C  CG   . GLN   B 1 89  ? -11.662 -4.001  18.979  1.00 54.34  ?  89  GLN   B CG   1 
ATOM   1722 C  CD   . GLN   B 1 89  ? -11.412 -5.286  19.743  1.00 71.58  ?  89  GLN   B CD   1 
ATOM   1723 O  OE1  . GLN   B 1 89  ? -10.291 -5.556  20.177  1.00 49.50  ?  89  GLN   B OE1  1 
ATOM   1724 N  NE2  . GLN   B 1 89  ? -12.457 -6.088  19.911  1.00 61.35  ?  89  GLN   B NE2  1 
ATOM   1725 N  N    . ASP   B 1 90  ? -10.222 -0.673  19.666  1.00 39.37  ?  90  ASP   B N    1 
ATOM   1726 C  CA   . ASP   B 1 90  ? -10.636 0.721   19.733  1.00 34.16  ?  90  ASP   B CA   1 
ATOM   1727 C  C    . ASP   B 1 90  ? -9.496  1.690   19.449  1.00 39.70  ?  90  ASP   B C    1 
ATOM   1728 O  O    . ASP   B 1 90  ? -9.755  2.882   19.252  1.00 38.78  ?  90  ASP   B O    1 
ATOM   1729 C  CB   . ASP   B 1 90  ? -11.225 1.032   21.115  1.00 37.43  ?  90  ASP   B CB   1 
ATOM   1730 C  CG   . ASP   B 1 90  ? -12.545 0.326   21.365  1.00 42.18  ?  90  ASP   B CG   1 
ATOM   1731 O  OD1  . ASP   B 1 90  ? -13.302 0.109   20.397  1.00 43.88  ?  90  ASP   B OD1  1 
ATOM   1732 O  OD2  . ASP   B 1 90  ? -12.829 -0.006  22.536  1.00 44.38  ?  90  ASP   B OD2  1 
ATOM   1733 N  N    . ALA   B 1 91  ? -8.251  1.216   19.423  1.00 30.53  ?  91  ALA   B N    1 
ATOM   1734 C  CA   . ALA   B 1 91  ? -7.130  2.079   19.083  1.00 30.52  ?  91  ALA   B CA   1 
ATOM   1735 C  C    . ALA   B 1 91  ? -7.194  2.475   17.614  1.00 36.81  ?  91  ALA   B C    1 
ATOM   1736 O  O    . ALA   B 1 91  ? -7.533  1.662   16.750  1.00 41.10  ?  91  ALA   B O    1 
ATOM   1737 C  CB   . ALA   B 1 91  ? -5.804  1.379   19.377  1.00 35.76  ?  91  ALA   B CB   1 
ATOM   1738 N  N    . GLY   B 1 92  ? -6.866  3.725   17.333  1.00 36.53  ?  92  GLY   B N    1 
ATOM   1739 C  CA   . GLY   B 1 92  ? -6.890  4.208   15.969  1.00 49.10  ?  92  GLY   B CA   1 
ATOM   1740 C  C    . GLY   B 1 92  ? -7.209  5.688   15.927  1.00 39.94  ?  92  GLY   B C    1 
ATOM   1741 O  O    . GLY   B 1 92  ? -7.142  6.385   16.934  1.00 37.69  ?  92  GLY   B O    1 
ATOM   1742 N  N    . VAL   B 1 93  ? -7.575  6.150   14.736  1.00 33.19  ?  93  VAL   B N    1 
ATOM   1743 C  CA   . VAL   B 1 93  ? -7.848  7.559   14.490  1.00 40.03  ?  93  VAL   B CA   1 
ATOM   1744 C  C    . VAL   B 1 93  ? -9.354  7.738   14.378  1.00 42.66  ?  93  VAL   B C    1 
ATOM   1745 O  O    . VAL   B 1 93  ? -9.998  7.156   13.496  1.00 36.93  ?  93  VAL   B O    1 
ATOM   1746 C  CB   . VAL   B 1 93  ? -7.136  8.063   13.226  1.00 48.71  ?  93  VAL   B CB   1 
ATOM   1747 C  CG1  . VAL   B 1 93  ? -7.525  9.506   12.940  1.00 35.19  ?  93  VAL   B CG1  1 
ATOM   1748 C  CG2  . VAL   B 1 93  ? -5.628  7.930   13.380  1.00 48.52  ?  93  VAL   B CG2  1 
ATOM   1749 N  N    . TYR   B 1 94  ? -9.909  8.545   15.272  1.00 36.86  ?  94  TYR   B N    1 
ATOM   1750 C  CA   . TYR   B 1 94  ? -11.321 8.867   15.311  1.00 41.45  ?  94  TYR   B CA   1 
ATOM   1751 C  C    . TYR   B 1 94  ? -11.537 10.195  14.607  1.00 35.04  ?  94  TYR   B C    1 
ATOM   1752 O  O    . TYR   B 1 94  ? -10.673 11.073  14.622  1.00 40.54  ?  94  TYR   B O    1 
ATOM   1753 C  CB   . TYR   B 1 94  ? -11.816 8.970   16.757  1.00 49.61  ?  94  TYR   B CB   1 
ATOM   1754 C  CG   . TYR   B 1 94  ? -11.899 7.644   17.467  1.00 38.83  ?  94  TYR   B CG   1 
ATOM   1755 C  CD1  . TYR   B 1 94  ? -10.751 6.916   17.748  1.00 33.04  ?  94  TYR   B CD1  1 
ATOM   1756 C  CD2  . TYR   B 1 94  ? -13.122 7.117   17.855  1.00 41.87  ?  94  TYR   B CD2  1 
ATOM   1757 C  CE1  . TYR   B 1 94  ? -10.818 5.699   18.390  1.00 35.76  ?  94  TYR   B CE1  1 
ATOM   1758 C  CE2  . TYR   B 1 94  ? -13.201 5.903   18.500  1.00 39.94  ?  94  TYR   B CE2  1 
ATOM   1759 C  CZ   . TYR   B 1 94  ? -12.047 5.197   18.765  1.00 37.92  ?  94  TYR   B CZ   1 
ATOM   1760 O  OH   . TYR   B 1 94  ? -12.124 3.986   19.408  1.00 43.06  ?  94  TYR   B OH   1 
ATOM   1761 N  N    . ARG   B 1 95  ? -12.695 10.334  13.981  1.00 35.15  ?  95  ARG   B N    1 
ATOM   1762 C  CA   . ARG   B 1 95  ? -13.104 11.594  13.394  1.00 33.57  ?  95  ARG   B CA   1 
ATOM   1763 C  C    . ARG   B 1 95  ? -14.473 11.947  13.940  1.00 46.87  ?  95  ARG   B C    1 
ATOM   1764 O  O    . ARG   B 1 95  ? -15.389 11.106  13.948  1.00 43.39  ?  95  ARG   B O    1 
ATOM   1765 C  CB   . ARG   B 1 95  ? -13.123 11.533  11.863  1.00 37.11  ?  95  ARG   B CB   1 
ATOM   1766 C  CG   . ARG   B 1 95  ? -11.737 11.417  11.263  1.00 43.30  ?  95  ARG   B CG   1 
ATOM   1767 C  CD   . ARG   B 1 95  ? -11.770 11.199  9.763   1.00 51.36  ?  95  ARG   B CD   1 
ATOM   1768 N  NE   . ARG   B 1 95  ? -10.427 10.959  9.252   1.00 53.57  ?  95  ARG   B NE   1 
ATOM   1769 C  CZ   . ARG   B 1 95  ? -9.691  9.900   9.560   1.00 53.25  ?  95  ARG   B CZ   1 
ATOM   1770 N  NH1  . ARG   B 1 95  ? -10.126 8.976   10.401  1.00 62.37  ?  95  ARG   B NH1  1 
ATOM   1771 N  NH2  . ARG   B 1 95  ? -8.476  9.778   9.032   1.00 47.71  ?  95  ARG   B NH2  1 
ATOM   1772 N  N    . CYS   B 1 96  ? -14.590 13.184  14.416  1.00 36.96  ?  96  CYS   B N    1 
ATOM   1773 C  CA   . CYS   B 1 96  ? -15.868 13.745  14.825  1.00 38.02  ?  96  CYS   B CA   1 
ATOM   1774 C  C    . CYS   B 1 96  ? -16.241 14.768  13.765  1.00 49.08  ?  96  CYS   B C    1 
ATOM   1775 O  O    . CYS   B 1 96  ? -15.454 15.677  13.464  1.00 43.27  ?  96  CYS   B O    1 
ATOM   1776 C  CB   . CYS   B 1 96  ? -15.816 14.378  16.218  1.00 48.65  ?  96  CYS   B CB   1 
ATOM   1777 S  SG   . CYS   B 1 96  ? -15.288 16.106  16.299  1.00 82.98  ?  96  CYS   B SG   1 
ATOM   1778 N  N    . MET   B 1 97  ? -17.419 14.582  13.178  1.00 43.68  ?  97  MET   B N    1 
ATOM   1779 C  CA   . MET   B 1 97  ? -17.888 15.326  12.022  1.00 36.53  ?  97  MET   B CA   1 
ATOM   1780 C  C    . MET   B 1 97  ? -19.187 16.003  12.418  1.00 44.14  ?  97  MET   B C    1 
ATOM   1781 O  O    . MET   B 1 97  ? -20.118 15.336  12.876  1.00 49.87  ?  97  MET   B O    1 
ATOM   1782 C  CB   . MET   B 1 97  ? -18.112 14.376  10.848  1.00 48.07  ?  97  MET   B CB   1 
ATOM   1783 C  CG   . MET   B 1 97  ? -16.857 13.644  10.427  1.00 55.58  ?  97  MET   B CG   1 
ATOM   1784 S  SD   . MET   B 1 97  ? -17.071 12.706  8.913   1.00 61.78  ?  97  MET   B SD   1 
ATOM   1785 C  CE   . MET   B 1 97  ? -15.390 12.157  8.630   1.00 65.44  ?  97  MET   B CE   1 
ATOM   1786 N  N    . ILE   B 1 98  ? -19.251 17.317  12.268  1.00 43.63  ?  98  ILE   B N    1 
ATOM   1787 C  CA   . ILE   B 1 98  ? -20.399 18.073  12.739  1.00 42.93  ?  98  ILE   B CA   1 
ATOM   1788 C  C    . ILE   B 1 98  ? -20.894 18.969  11.616  1.00 53.10  ?  98  ILE   B C    1 
ATOM   1789 O  O    . ILE   B 1 98  ? -20.108 19.712  11.010  1.00 44.60  ?  98  ILE   B O    1 
ATOM   1790 C  CB   . ILE   B 1 98  ? -20.060 18.889  13.998  1.00 37.49  ?  98  ILE   B CB   1 
ATOM   1791 C  CG1  . ILE   B 1 98  ? -19.614 17.937  15.110  1.00 46.43  ?  98  ILE   B CG1  1 
ATOM   1792 C  CG2  . ILE   B 1 98  ? -21.266 19.693  14.446  1.00 48.35  ?  98  ILE   B CG2  1 
ATOM   1793 C  CD1  . ILE   B 1 98  ? -18.903 18.608  16.253  1.00 57.13  ?  98  ILE   B CD1  1 
ATOM   1794 N  N    . SER   B 1 99  ? -22.186 18.853  11.312  1.00 52.04  ?  99  SER   B N    1 
ATOM   1795 C  CA   . SER   B 1 99  ? -22.909 19.805  10.479  1.00 51.76  ?  99  SER   B CA   1 
ATOM   1796 C  C    . SER   B 1 99  ? -23.840 20.611  11.371  1.00 56.17  ?  99  SER   B C    1 
ATOM   1797 O  O    . SER   B 1 99  ? -24.769 20.057  11.969  1.00 60.67  ?  99  SER   B O    1 
ATOM   1798 C  CB   . SER   B 1 99  ? -23.703 19.094  9.384   1.00 54.41  ?  99  SER   B CB   1 
ATOM   1799 O  OG   . SER   B 1 99  ? -24.470 20.019  8.632   1.00 60.86  ?  99  SER   B OG   1 
ATOM   1800 N  N    . TYR   B 1 100 ? -23.590 21.914  11.458  1.00 52.12  ?  100 TYR   B N    1 
ATOM   1801 C  CA   . TYR   B 1 100 ? -24.444 22.826  12.220  1.00 57.63  ?  100 TYR   B CA   1 
ATOM   1802 C  C    . TYR   B 1 100 ? -24.342 24.170  11.500  1.00 59.67  ?  100 TYR   B C    1 
ATOM   1803 O  O    . TYR   B 1 100 ? -23.453 24.976  11.784  1.00 61.72  ?  100 TYR   B O    1 
ATOM   1804 C  CB   . TYR   B 1 100 ? -23.996 22.912  13.672  1.00 60.32  ?  100 TYR   B CB   1 
ATOM   1805 C  CG   . TYR   B 1 100 ? -24.937 23.654  14.591  1.00 65.67  ?  100 TYR   B CG   1 
ATOM   1806 C  CD1  . TYR   B 1 100 ? -26.254 23.244  14.745  1.00 57.72  ?  100 TYR   B CD1  1 
ATOM   1807 C  CD2  . TYR   B 1 100 ? -24.502 24.751  15.320  1.00 71.13  ?  100 TYR   B CD2  1 
ATOM   1808 C  CE1  . TYR   B 1 100 ? -27.115 23.916  15.590  1.00 74.38  ?  100 TYR   B CE1  1 
ATOM   1809 C  CE2  . TYR   B 1 100 ? -25.354 25.428  16.167  1.00 69.22  ?  100 TYR   B CE2  1 
ATOM   1810 C  CZ   . TYR   B 1 100 ? -26.659 25.007  16.299  1.00 77.64  ?  100 TYR   B CZ   1 
ATOM   1811 O  OH   . TYR   B 1 100 ? -27.513 25.678  17.143  1.00 83.99  ?  100 TYR   B OH   1 
ATOM   1812 N  N    . GLY   B 1 101 ? -25.228 24.385  10.537  1.00 69.87  ?  101 GLY   B N    1 
ATOM   1813 C  CA   . GLY   B 1 101 ? -24.946 25.473  9.631   1.00 64.19  ?  101 GLY   B CA   1 
ATOM   1814 C  C    . GLY   B 1 101 ? -23.846 25.005  8.705   1.00 70.47  ?  101 GLY   B C    1 
ATOM   1815 O  O    . GLY   B 1 101 ? -24.093 24.272  7.741   1.00 67.18  ?  101 GLY   B O    1 
ATOM   1816 N  N    . GLY   B 1 102 ? -22.622 25.433  8.992   1.00 50.88  ?  102 GLY   B N    1 
ATOM   1817 C  CA   . GLY   B 1 102 ? -21.462 24.935  8.286   1.00 54.13  ?  102 GLY   B CA   1 
ATOM   1818 C  C    . GLY   B 1 102 ? -21.202 23.468  8.597   1.00 52.71  ?  102 GLY   B C    1 
ATOM   1819 O  O    . GLY   B 1 102 ? -22.020 22.757  9.182   1.00 53.97  ?  102 GLY   B O    1 
ATOM   1820 N  N    . ALA   B 1 103 ? -20.020 23.014  8.187   1.00 56.86  ?  103 ALA   B N    1 
ATOM   1821 C  CA   . ALA   B 1 103 ? -19.613 21.638  8.428   1.00 42.67  ?  103 ALA   B CA   1 
ATOM   1822 C  C    . ALA   B 1 103 ? -18.111 21.587  8.655   1.00 48.55  ?  103 ALA   B C    1 
ATOM   1823 O  O    . ALA   B 1 103 ? -17.350 22.352  8.055   1.00 50.65  ?  103 ALA   B O    1 
ATOM   1824 C  CB   . ALA   B 1 103 ? -20.000 20.723  7.261   1.00 41.92  ?  103 ALA   B CB   1 
ATOM   1825 N  N    . ASP   B 1 104 ? -17.691 20.665  9.517   1.00 51.58  ?  104 ASP   B N    1 
ATOM   1826 C  CA   . ASP   B 1 104 ? -16.276 20.532  9.842   1.00 47.83  ?  104 ASP   B CA   1 
ATOM   1827 C  C    . ASP   B 1 104 ? -16.056 19.186  10.512  1.00 49.23  ?  104 ASP   B C    1 
ATOM   1828 O  O    . ASP   B 1 104 ? -17.005 18.526  10.938  1.00 46.91  ?  104 ASP   B O    1 
ATOM   1829 C  CB   . ASP   B 1 104 ? -15.792 21.668  10.750  1.00 44.80  ?  104 ASP   B CB   1 
ATOM   1830 C  CG   . ASP   B 1 104 ? -14.280 21.808  10.760  1.00 55.45  ?  104 ASP   B CG   1 
ATOM   1831 O  OD1  . ASP   B 1 104 ? -13.618 21.256  9.854   1.00 50.76  ?  104 ASP   B OD1  1 
ATOM   1832 O  OD2  . ASP   B 1 104 ? -13.754 22.459  11.687  1.00 54.27  ?  104 ASP   B OD2  1 
ATOM   1833 N  N    . TYR   B 1 105 ? -14.795 18.763  10.573  1.00 50.02  ?  105 TYR   B N    1 
ATOM   1834 C  CA   . TYR   B 1 105 ? -14.485 17.578  11.357  1.00 39.04  ?  105 TYR   B CA   1 
ATOM   1835 C  C    . TYR   B 1 105 ? -13.068 17.690  11.892  1.00 47.30  ?  105 TYR   B C    1 
ATOM   1836 O  O    . TYR   B 1 105 ? -12.239 18.442  11.372  1.00 43.42  ?  105 TYR   B O    1 
ATOM   1837 C  CB   . TYR   B 1 105 ? -14.695 16.287  10.545  1.00 45.02  ?  105 TYR   B CB   1 
ATOM   1838 C  CG   . TYR   B 1 105 ? -13.625 15.908  9.535   1.00 44.72  ?  105 TYR   B CG   1 
ATOM   1839 C  CD1  . TYR   B 1 105 ? -12.511 15.168  9.917   1.00 47.66  ?  105 TYR   B CD1  1 
ATOM   1840 C  CD2  . TYR   B 1 105 ? -13.740 16.274  8.200   1.00 50.20  ?  105 TYR   B CD2  1 
ATOM   1841 C  CE1  . TYR   B 1 105 ? -11.545 14.795  8.995   1.00 52.90  ?  105 TYR   B CE1  1 
ATOM   1842 C  CE2  . TYR   B 1 105 ? -12.771 15.918  7.273   1.00 56.36  ?  105 TYR   B CE2  1 
ATOM   1843 C  CZ   . TYR   B 1 105 ? -11.676 15.181  7.676   1.00 63.38  ?  105 TYR   B CZ   1 
ATOM   1844 O  OH   . TYR   B 1 105 ? -10.713 14.827  6.755   1.00 57.93  ?  105 TYR   B OH   1 
ATOM   1845 N  N    . LYS   B 1 106 ? -12.813 16.940  12.960  1.00 39.89  ?  106 LYS   B N    1 
ATOM   1846 C  CA   . LYS   B 1 106 ? -11.488 16.881  13.557  1.00 40.37  ?  106 LYS   B CA   1 
ATOM   1847 C  C    . LYS   B 1 106 ? -11.106 15.436  13.855  1.00 42.92  ?  106 LYS   B C    1 
ATOM   1848 O  O    . LYS   B 1 106 ? -11.964 14.559  14.033  1.00 51.99  ?  106 LYS   B O    1 
ATOM   1849 C  CB   . LYS   B 1 106 ? -11.401 17.735  14.835  1.00 46.17  ?  106 LYS   B CB   1 
ATOM   1850 C  CG   . LYS   B 1 106 ? -11.326 19.250  14.594  1.00 46.78  ?  106 LYS   B CG   1 
ATOM   1851 C  CD   . LYS   B 1 106 ? -9.999  19.664  13.961  1.00 49.90  ?  106 LYS   B CD   1 
ATOM   1852 C  CE   . LYS   B 1 106 ? -9.794  21.178  13.999  1.00 63.70  ?  106 LYS   B CE   1 
ATOM   1853 N  NZ   . LYS   B 1 106 ? -10.834 21.934  13.249  1.00 57.96  ?  106 LYS   B NZ   1 
ATOM   1854 N  N    . ARG   B 1 107 ? -9.792  15.211  13.903  1.00 39.10  ?  107 ARG   B N    1 
ATOM   1855 C  CA   . ARG   B 1 107 ? -9.186  13.910  14.156  1.00 33.45  ?  107 ARG   B CA   1 
ATOM   1856 C  C    . ARG   B 1 107 ? -8.711  13.812  15.601  1.00 33.39  ?  107 ARG   B C    1 
ATOM   1857 O  O    . ARG   B 1 107 ? -8.205  14.786  16.166  1.00 41.98  ?  107 ARG   B O    1 
ATOM   1858 C  CB   . ARG   B 1 107 ? -7.995  13.678  13.224  1.00 37.89  ?  107 ARG   B CB   1 
ATOM   1859 C  CG   . ARG   B 1 107 ? -8.343  13.469  11.766  1.00 51.76  ?  107 ARG   B CG   1 
ATOM   1860 C  CD   . ARG   B 1 107 ? -7.085  13.150  10.976  1.00 57.50  ?  107 ARG   B CD   1 
ATOM   1861 N  NE   . ARG   B 1 107 ? -6.049  14.154  11.189  1.00 53.50  ?  107 ARG   B NE   1 
ATOM   1862 N  N    . ILE   B 1 108 ? -8.874  12.630  16.192  1.00 39.74  ?  108 ILE   B N    1 
ATOM   1863 C  CA   . ILE   B 1 108 ? -8.411  12.329  17.544  1.00 36.03  ?  108 ILE   B CA   1 
ATOM   1864 C  C    . ILE   B 1 108 ? -7.721  10.971  17.515  1.00 39.20  ?  108 ILE   B C    1 
ATOM   1865 O  O    . ILE   B 1 108 ? -8.327  9.977   17.107  1.00 39.74  ?  108 ILE   B O    1 
ATOM   1866 C  CB   . ILE   B 1 108 ? -9.568  12.314  18.556  1.00 37.68  ?  108 ILE   B CB   1 
ATOM   1867 C  CG1  . ILE   B 1 108 ? -10.173 13.710  18.707  1.00 39.05  ?  108 ILE   B CG1  1 
ATOM   1868 C  CG2  . ILE   B 1 108 ? -9.089  11.792  19.908  1.00 32.41  ?  108 ILE   B CG2  1 
ATOM   1869 C  CD1  . ILE   B 1 108 ? -11.148 13.819  19.861  1.00 56.95  ?  108 ILE   B CD1  1 
ATOM   1870 N  N    . THR   B 1 109 ? -6.475  10.914  17.971  1.00 33.64  ?  109 THR   B N    1 
ATOM   1871 C  CA   . THR   B 1 109 ? -5.757  9.648   18.056  1.00 33.54  ?  109 THR   B CA   1 
ATOM   1872 C  C    . THR   B 1 109 ? -6.001  8.995   19.412  1.00 35.42  ?  109 THR   B C    1 
ATOM   1873 O  O    . THR   B 1 109 ? -5.836  9.638   20.453  1.00 36.01  ?  109 THR   B O    1 
ATOM   1874 C  CB   . THR   B 1 109 ? -4.259  9.858   17.841  1.00 39.55  ?  109 THR   B CB   1 
ATOM   1875 O  OG1  . THR   B 1 109 ? -4.041  10.496  16.577  1.00 42.93  ?  109 THR   B OG1  1 
ATOM   1876 C  CG2  . THR   B 1 109 ? -3.529  8.526   17.870  1.00 38.87  ?  109 THR   B CG2  1 
ATOM   1877 N  N    . VAL   B 1 110 ? -6.397  7.723   19.398  1.00 36.77  ?  110 VAL   B N    1 
ATOM   1878 C  CA   . VAL   B 1 110 ? -6.589  6.940   20.614  1.00 33.87  ?  110 VAL   B CA   1 
ATOM   1879 C  C    . VAL   B 1 110 ? -5.600  5.783   20.599  1.00 39.08  ?  110 VAL   B C    1 
ATOM   1880 O  O    . VAL   B 1 110 ? -5.581  4.986   19.650  1.00 33.98  ?  110 VAL   B O    1 
ATOM   1881 C  CB   . VAL   B 1 110 ? -8.028  6.419   20.744  1.00 40.19  ?  110 VAL   B CB   1 
ATOM   1882 C  CG1  . VAL   B 1 110 ? -8.144  5.493   21.947  1.00 44.90  ?  110 VAL   B CG1  1 
ATOM   1883 C  CG2  . VAL   B 1 110 ? -9.002  7.578   20.861  1.00 38.65  ?  110 VAL   B CG2  1 
ATOM   1884 N  N    . LYS   B 1 111 ? -4.789  5.691   21.649  1.00 37.69  ?  111 LYS   B N    1 
ATOM   1885 C  CA   . LYS   B 1 111 ? -3.880  4.577   21.872  1.00 32.37  ?  111 LYS   B CA   1 
ATOM   1886 C  C    . LYS   B 1 111 ? -4.362  3.794   23.086  1.00 38.00  ?  111 LYS   B C    1 
ATOM   1887 O  O    . LYS   B 1 111 ? -4.820  4.382   24.070  1.00 34.96  ?  111 LYS   B O    1 
ATOM   1888 C  CB   . LYS   B 1 111 ? -2.446  5.069   22.090  1.00 44.37  ?  111 LYS   B CB   1 
ATOM   1889 C  CG   . LYS   B 1 111 ? -1.748  5.539   20.819  1.00 45.06  ?  111 LYS   B CG   1 
ATOM   1890 N  N    . VAL   B 1 112 ? -4.272  2.468   23.016  1.00 35.35  ?  112 VAL   B N    1 
ATOM   1891 C  CA   . VAL   B 1 112 ? -4.783  1.595   24.069  1.00 40.09  ?  112 VAL   B CA   1 
ATOM   1892 C  C    . VAL   B 1 112 ? -3.635  0.769   24.636  1.00 33.54  ?  112 VAL   B C    1 
ATOM   1893 O  O    . VAL   B 1 112 ? -2.976  0.023   23.900  1.00 38.53  ?  112 VAL   B O    1 
ATOM   1894 C  CB   . VAL   B 1 112 ? -5.906  0.682   23.553  1.00 42.51  ?  112 VAL   B CB   1 
ATOM   1895 C  CG1  . VAL   B 1 112 ? -6.364  -0.261  24.652  1.00 39.43  ?  112 VAL   B CG1  1 
ATOM   1896 C  CG2  . VAL   B 1 112 ? -7.069  1.512   23.033  1.00 39.88  ?  112 VAL   B CG2  1 
ATOM   1897 N  N    . ASN   B 1 113 ? -3.400  0.902   25.941  1.00 41.47  ?  113 ASN   B N    1 
ATOM   1898 C  CA   . ASN   B 1 113 ? -2.527  -0.002  26.679  1.00 31.70  ?  113 ASN   B CA   1 
ATOM   1899 C  C    . ASN   B 1 113 ? -3.326  -1.216  27.140  1.00 32.70  ?  113 ASN   B C    1 
ATOM   1900 O  O    . ASN   B 1 113 ? -4.482  -1.088  27.551  1.00 45.99  ?  113 ASN   B O    1 
ATOM   1901 C  CB   . ASN   B 1 113 ? -1.909  0.704   27.888  1.00 34.38  ?  113 ASN   B CB   1 
ATOM   1902 C  CG   . ASN   B 1 113 ? -1.028  1.874   27.496  1.00 35.23  ?  113 ASN   B CG   1 
ATOM   1903 O  OD1  . ASN   B 1 113 ? -0.230  1.784   26.563  1.00 37.57  ?  113 ASN   B OD1  1 
ATOM   1904 N  ND2  . ASN   B 1 113 ? -1.163  2.981   28.218  1.00 33.03  ?  113 ASN   B ND2  1 
ATOM   1905 N  N    . ALA   B 1 114 ? -2.707  -2.395  27.080  1.00 45.17  ?  114 ALA   B N    1 
ATOM   1906 C  CA   . ALA   B 1 114 ? -3.389  -3.608  27.514  1.00 38.05  ?  114 ALA   B CA   1 
ATOM   1907 C  C    . ALA   B 1 114 ? -2.383  -4.607  28.064  1.00 48.64  ?  114 ALA   B C    1 
ATOM   1908 O  O    . ALA   B 1 114 ? -1.252  -4.685  27.569  1.00 42.98  ?  114 ALA   B O    1 
ATOM   1909 C  CB   . ALA   B 1 114 ? -4.186  -4.244  26.366  1.00 44.40  ?  114 ALA   B CB   1 
ATOM   1910 N  N    . PRO   B 1 115 ? -2.766  -5.387  29.073  1.00 39.09  ?  115 PRO   B N    1 
ATOM   1911 C  CA   . PRO   B 1 115 ? -1.871  -6.421  29.605  1.00 40.01  ?  115 PRO   B CA   1 
ATOM   1912 C  C    . PRO   B 1 115 ? -1.671  -7.567  28.622  1.00 40.47  ?  115 PRO   B C    1 
ATOM   1913 O  O    . PRO   B 1 115 ? -2.374  -7.710  27.620  1.00 38.48  ?  115 PRO   B O    1 
ATOM   1914 C  CB   . PRO   B 1 115 ? -2.587  -6.902  30.874  1.00 43.50  ?  115 PRO   B CB   1 
ATOM   1915 C  CG   . PRO   B 1 115 ? -3.624  -5.858  31.167  1.00 48.27  ?  115 PRO   B CG   1 
ATOM   1916 C  CD   . PRO   B 1 115 ? -4.019  -5.299  29.839  1.00 46.25  ?  115 PRO   B CD   1 
ATOM   1917 N  N    . TYR   B 1 116 ? -0.673  -8.396  28.942  1.00 36.68  ?  116 TYR   B N    1 
ATOM   1918 C  CA   . TYR   B 1 116 ? -0.332  -9.549  28.113  1.00 43.39  ?  116 TYR   B CA   1 
ATOM   1919 C  C    . TYR   B 1 116 ? -1.554  -10.389 27.767  1.00 52.12  ?  116 TYR   B C    1 
ATOM   1920 O  O    . TYR   B 1 116 ? -1.741  -10.781 26.611  1.00 38.75  ?  116 TYR   B O    1 
ATOM   1921 C  CB   . TYR   B 1 116 ? 0.705   -10.415 28.827  1.00 44.70  ?  116 TYR   B CB   1 
ATOM   1922 C  CG   . TYR   B 1 116 ? 1.130   -11.634 28.039  1.00 40.40  ?  116 TYR   B CG   1 
ATOM   1923 C  CD1  . TYR   B 1 116 ? 1.894   -11.519 26.885  1.00 38.28  ?  116 TYR   B CD1  1 
ATOM   1924 C  CD2  . TYR   B 1 116 ? 0.743   -12.905 28.443  1.00 47.86  ?  116 TYR   B CD2  1 
ATOM   1925 C  CE1  . TYR   B 1 116 ? 2.275   -12.642 26.167  1.00 44.42  ?  116 TYR   B CE1  1 
ATOM   1926 C  CE2  . TYR   B 1 116 ? 1.116   -14.027 27.734  1.00 53.71  ?  116 TYR   B CE2  1 
ATOM   1927 C  CZ   . TYR   B 1 116 ? 1.881   -13.892 26.598  1.00 51.26  ?  116 TYR   B CZ   1 
ATOM   1928 O  OH   . TYR   B 1 116 ? 2.250   -15.016 25.895  1.00 54.50  ?  116 TYR   B OH   1 
ATOM   1929 N  N    . ALA   B 1 117 ? -2.373  -10.720 28.767  1.00 42.79  ?  117 ALA   B N    1 
ATOM   1930 C  CA   . ALA   B 1 117 ? -3.479  -11.642 28.527  1.00 49.62  ?  117 ALA   B CA   1 
ATOM   1931 C  C    . ALA   B 1 117 ? -4.436  -11.096 27.474  1.00 40.56  ?  117 ALA   B C    1 
ATOM   1932 O  O    . ALA   B 1 117 ? -4.879  -11.832 26.584  1.00 54.55  ?  117 ALA   B O    1 
ATOM   1933 C  CB   . ALA   B 1 117 ? -4.218  -11.929 29.834  1.00 54.04  ?  117 ALA   B CB   1 
ATOM   1934 N  N    . ALA   B 1 118 ? -4.777  -9.809  27.566  1.00 38.07  ?  118 ALA   B N    1 
ATOM   1935 C  CA   . ALA   B 1 118 ? -5.665  -9.205  26.577  1.00 52.31  ?  118 ALA   B CA   1 
ATOM   1936 C  C    . ALA   B 1 118 ? -5.015  -9.169  25.197  1.00 45.63  ?  118 ALA   B C    1 
ATOM   1937 O  O    . ALA   B 1 118 ? -5.613  -9.601  24.206  1.00 46.19  ?  118 ALA   B O    1 
ATOM   1938 C  CB   . ALA   B 1 118 ? -6.066  -7.800  27.025  1.00 43.22  ?  118 ALA   B CB   1 
ATOM   1939 N  N    . HIS   B 1 119 ? -3.782  -8.657  25.117  1.00 44.93  ?  119 HIS   B N    1 
ATOM   1940 C  CA   . HIS   B 1 119 ? -3.070  -8.599  23.843  1.00 53.20  ?  119 HIS   B CA   1 
ATOM   1941 C  C    . HIS   B 1 119 ? -2.988  -9.969  23.184  1.00 44.71  ?  119 HIS   B C    1 
ATOM   1942 O  O    . HIS   B 1 119 ? -3.030  -10.078 21.954  1.00 49.11  ?  119 HIS   B O    1 
ATOM   1943 C  CB   . HIS   B 1 119 ? -1.659  -8.048  24.065  1.00 54.01  ?  119 HIS   B CB   1 
ATOM   1944 C  CG   . HIS   B 1 119 ? -1.533  -6.574  23.830  1.00 90.05  ?  119 HIS   B CG   1 
ATOM   1945 N  ND1  . HIS   B 1 119 ? -1.212  -5.689  24.837  1.00 84.83  ?  119 HIS   B ND1  1 
ATOM   1946 C  CD2  . HIS   B 1 119 ? -1.672  -5.832  22.706  1.00 77.43  ?  119 HIS   B CD2  1 
ATOM   1947 C  CE1  . HIS   B 1 119 ? -1.164  -4.464  24.344  1.00 68.20  ?  119 HIS   B CE1  1 
ATOM   1948 N  NE2  . HIS   B 1 119 ? -1.439  -4.523  23.054  1.00 91.75  ?  119 HIS   B NE2  1 
ATOM   1949 N  N    . HIS   B 1 120 ? -2.860  -11.019 23.993  1.00 44.93  ?  120 HIS   B N    1 
ATOM   1950 C  CA   . HIS   B 1 120 ? -2.705  -12.376 23.483  1.00 48.43  ?  120 HIS   B CA   1 
ATOM   1951 C  C    . HIS   B 1 120 ? -3.936  -12.827 22.708  1.00 57.80  ?  120 HIS   B C    1 
ATOM   1952 O  O    . HIS   B 1 120 ? -3.827  -13.365 21.600  1.00 56.55  ?  120 HIS   B O    1 
ATOM   1953 C  CB   . HIS   B 1 120 ? -2.437  -13.310 24.664  1.00 65.85  ?  120 HIS   B CB   1 
ATOM   1954 C  CG   . HIS   B 1 120 ? -1.836  -14.627 24.290  1.00 61.99  ?  120 HIS   B CG   1 
ATOM   1955 N  ND1  . HIS   B 1 120 ? -2.004  -15.758 25.058  1.00 68.75  ?  120 HIS   B ND1  1 
ATOM   1956 C  CD2  . HIS   B 1 120 ? -1.056  -14.992 23.246  1.00 67.57  ?  120 HIS   B CD2  1 
ATOM   1957 C  CE1  . HIS   B 1 120 ? -1.361  -16.767 24.499  1.00 82.59  ?  120 HIS   B CE1  1 
ATOM   1958 N  NE2  . HIS   B 1 120 ? -0.777  -16.329 23.398  1.00 90.66  ?  120 HIS   B NE2  1 
ATOM   1959 N  N    . HIS   B 1 121 ? -5.118  -12.613 23.276  1.00 53.85  ?  121 HIS   B N    1 
ATOM   1960 C  CA   . HIS   B 1 121 ? -6.375  -13.004 22.648  1.00 67.97  ?  121 HIS   B CA   1 
ATOM   1961 C  C    . HIS   B 1 121 ? -6.623  -12.258 21.338  1.00 56.98  ?  121 HIS   B C    1 
ATOM   1962 O  O    . HIS   B 1 121 ? -6.041  -11.202 21.089  1.00 56.65  ?  121 HIS   B O    1 
ATOM   1963 C  CB   . HIS   B 1 121 ? -7.530  -12.785 23.633  1.00 72.81  ?  121 HIS   B CB   1 
ATOM   1964 C  CG   . HIS   B 1 121 ? -8.832  -12.426 22.987  1.00 97.00  ?  121 HIS   B CG   1 
ATOM   1965 N  ND1  . HIS   B 1 121 ? -9.100  -11.169 22.488  1.00 104.39 ?  121 HIS   B ND1  1 
ATOM   1966 C  CD2  . HIS   B 1 121 ? -9.952  -13.159 22.777  1.00 113.06 ?  121 HIS   B CD2  1 
ATOM   1967 C  CE1  . HIS   B 1 121 ? -10.323 -11.146 21.990  1.00 108.26 ?  121 HIS   B CE1  1 
ATOM   1968 N  NE2  . HIS   B 1 121 ? -10.862 -12.341 22.153  1.00 113.92 ?  121 HIS   B NE2  1 
HETATM 1969 C  C10  . A1LV3 C 2 .   ? -7.755  18.488  8.263   1.00 59.42  ?  201 A1LV3 B C10  1 
HETATM 1970 C  C13  . A1LV3 C 2 .   ? -10.780 18.550  8.316   1.00 62.66  ?  201 A1LV3 B C13  1 
HETATM 1971 C  C15  . A1LV3 C 2 .   ? -12.401 23.894  6.872   1.00 73.35  ?  201 A1LV3 B C15  1 
HETATM 1972 C  C21  . A1LV3 C 2 .   ? -11.419 26.071  8.100   1.00 78.95  ?  201 A1LV3 B C21  1 
HETATM 1973 C  C24  . A1LV3 C 2 .   ? -16.701 18.755  6.435   1.00 50.83  ?  201 A1LV3 B C24  1 
HETATM 1974 C  C26  . A1LV3 C 2 .   ? -18.700 17.112  6.937   1.00 48.16  ?  201 A1LV3 B C26  1 
HETATM 1975 C  C28  . A1LV3 C 2 .   ? -20.655 16.796  5.163   1.00 49.01  ?  201 A1LV3 B C28  1 
HETATM 1976 C  C01  . A1LV3 C 2 .   ? -14.101 20.192  6.458   1.00 52.56  ?  201 A1LV3 B C01  1 
HETATM 1977 C  C02  . A1LV3 C 2 .   ? -15.387 20.583  5.731   1.00 63.03  ?  201 A1LV3 B C02  1 
HETATM 1978 C  C03  . A1LV3 C 2 .   ? -15.669 22.044  5.400   1.00 68.42  ?  201 A1LV3 B C03  1 
HETATM 1979 C  C04  . A1LV3 C 2 .   ? -14.667 23.125  5.790   1.00 64.15  ?  201 A1LV3 B C04  1 
HETATM 1980 C  C05  . A1LV3 C 2 .   ? -13.378 22.752  6.513   1.00 65.33  ?  201 A1LV3 B C05  1 
HETATM 1981 C  C06  . A1LV3 C 2 .   ? -13.097 21.286  6.844   1.00 64.12  ?  201 A1LV3 B C06  1 
HETATM 1982 C  C08  . A1LV3 C 2 .   ? -10.056 19.531  7.464   1.00 68.97  ?  201 A1LV3 B C08  1 
HETATM 1983 C  C09  . A1LV3 C 2 .   ? -8.549  19.532  7.420   1.00 69.54  ?  201 A1LV3 B C09  1 
HETATM 1984 C  C11  . A1LV3 C 2 .   ? -8.438  17.554  9.066   1.00 74.44  ?  201 A1LV3 B C11  1 
HETATM 1985 C  C12  . A1LV3 C 2 .   ? -9.996  17.551  9.127   1.00 66.50  ?  201 A1LV3 B C12  1 
HETATM 1986 C  C18  . A1LV3 C 2 .   ? -11.292 24.727  8.812   1.00 74.27  ?  201 A1LV3 B C18  1 
HETATM 1987 C  C19  . A1LV3 C 2 .   ? -12.386 24.600  9.877   1.00 72.09  ?  201 A1LV3 B C19  1 
HETATM 1988 C  C25  . A1LV3 C 2 .   ? -18.027 18.103  6.001   1.00 49.58  ?  201 A1LV3 B C25  1 
HETATM 1989 C  C27  . A1LV3 C 2 .   ? -20.011 16.459  6.507   1.00 43.49  ?  201 A1LV3 B C27  1 
HETATM 1990 C  C29  . A1LV3 C 2 .   ? -19.970 17.796  4.228   1.00 41.91  ?  201 A1LV3 B C29  1 
HETATM 1991 C  C30  . A1LV3 C 2 .   ? -18.650 18.451  4.651   1.00 41.32  ?  201 A1LV3 B C30  1 
HETATM 1992 C  C31  . A1LV3 C 2 .   ? -20.704 15.467  7.456   1.00 44.52  ?  201 A1LV3 B C31  1 
HETATM 1993 C  C33  . A1LV3 C 2 .   ? -20.782 15.824  8.939   1.00 40.28  ?  201 A1LV3 B C33  1 
HETATM 1994 C  C34  . A1LV3 C 2 .   ? -21.471 14.873  9.916   1.00 46.40  ?  201 A1LV3 B C34  1 
HETATM 1995 C  C35  . A1LV3 C 2 .   ? -22.086 13.574  9.394   1.00 48.17  ?  201 A1LV3 B C35  1 
HETATM 1996 C  C36  . A1LV3 C 2 .   ? -22.005 13.225  7.906   1.00 43.20  ?  201 A1LV3 B C36  1 
HETATM 1997 C  C37  . A1LV3 C 2 .   ? -21.320 14.173  6.925   1.00 51.99  ?  201 A1LV3 B C37  1 
HETATM 1998 C  C39  . A1LV3 C 2 .   ? -22.275 10.861  8.171   1.00 68.30  ?  201 A1LV3 B C39  1 
HETATM 1999 C  C40  . A1LV3 C 2 .   ? -21.899 9.796   7.110   1.00 63.64  ?  201 A1LV3 B C40  1 
HETATM 2000 C  C41  . A1LV3 C 2 .   ? -22.556 8.448   7.489   1.00 62.63  ?  201 A1LV3 B C41  1 
HETATM 2001 C  C43  . A1LV3 C 2 .   ? -21.546 7.050   5.824   1.00 66.02  ?  201 A1LV3 B C43  1 
HETATM 2002 C  C44  . A1LV3 C 2 .   ? -21.371 5.664   6.428   1.00 67.98  ?  201 A1LV3 B C44  1 
HETATM 2003 C  C45  . A1LV3 C 2 .   ? -22.471 4.717   6.047   1.00 69.82  ?  201 A1LV3 B C45  1 
HETATM 2004 C  C46  . A1LV3 C 2 .   ? -23.763 5.404   5.744   1.00 74.95  ?  201 A1LV3 B C46  1 
HETATM 2005 C  C47  . A1LV3 C 2 .   ? -23.928 6.716   6.509   1.00 69.61  ?  201 A1LV3 B C47  1 
HETATM 2006 C  C52  . A1LV3 C 2 .   ? -10.875 20.547  6.663   1.00 68.95  ?  201 A1LV3 B C52  1 
HETATM 2007 F  F32  . A1LV3 C 2 .   ? -18.117 16.822  8.138   1.00 68.26  ?  201 A1LV3 B F32  1 
HETATM 2008 N  N16  . A1LV3 C 2 .   ? -11.455 23.562  7.930   1.00 86.35  ?  201 A1LV3 B N16  1 
HETATM 2009 N  N42  . A1LV3 C 2 .   ? -22.814 7.691   6.276   1.00 63.79  ?  201 A1LV3 B N42  1 
HETATM 2010 N  N49  . A1LV3 C 2 .   ? -7.532  16.793  9.668   1.00 75.11  ?  201 A1LV3 B N49  1 
HETATM 2011 N  N50  . A1LV3 C 2 .   ? -6.451  18.270  8.398   1.00 73.31  ?  201 A1LV3 B N50  1 
HETATM 2012 O  O07  . A1LV3 C 2 .   ? -11.913 20.944  7.512   1.00 65.77  ?  201 A1LV3 B O07  1 
HETATM 2013 O  O17  . A1LV3 C 2 .   ? -16.331 19.587  5.360   1.00 52.05  ?  201 A1LV3 B O17  1 
HETATM 2014 O  O20  . A1LV3 C 2 .   ? -12.303 25.650  10.805  1.00 78.74  ?  201 A1LV3 B O20  1 
HETATM 2015 O  O22  . A1LV3 C 2 .   ? -10.473 26.503  7.396   1.00 85.73  -1 201 A1LV3 B O22  1 
HETATM 2016 O  O23  . A1LV3 C 2 .   ? -12.482 26.739  8.207   1.00 80.40  ?  201 A1LV3 B O23  1 
HETATM 2017 O  O38  . A1LV3 C 2 .   ? -22.589 12.027  7.434   1.00 58.08  ?  201 A1LV3 B O38  1 
HETATM 2018 O  O48  . A1LV3 C 2 .   ? -22.064 3.965   4.875   1.00 80.64  ?  201 A1LV3 B O48  1 
HETATM 2019 O  O51  . A1LV3 C 2 .   ? -6.285  17.220  9.270   1.00 78.49  ?  201 A1LV3 B O51  1 
HETATM 2020 CL CL14 . A1LV3 C 2 .   ? -17.162 22.512  4.560   1.00 101.41 ?  201 A1LV3 B CL14 1 
HETATM 2021 H  H131 . A1LV3 C 2 .   ? -11.865 18.554  8.354   1.00 75.25  ?  201 A1LV3 B H131 1 
HETATM 2022 H  H152 . A1LV3 C 2 .   ? -12.982 24.750  7.193   1.00 88.08  ?  201 A1LV3 B H152 1 
HETATM 2023 H  H151 . A1LV3 C 2 .   ? -11.839 24.153  5.983   1.00 88.08  ?  201 A1LV3 B H151 1 
HETATM 2024 H  H242 . A1LV3 C 2 .   ? -16.842 19.339  7.336   1.00 61.06  ?  201 A1LV3 B H242 1 
HETATM 2025 H  H241 . A1LV3 C 2 .   ? -15.945 18.000  6.609   1.00 61.06  ?  201 A1LV3 B H241 1 
HETATM 2026 H  H281 . A1LV3 C 2 .   ? -21.590 16.331  4.873   1.00 58.87  ?  201 A1LV3 B H281 1 
HETATM 2027 H  H011 . A1LV3 C 2 .   ? -13.901 19.156  6.697   1.00 63.13  ?  201 A1LV3 B H011 1 
HETATM 2028 H  H041 . A1LV3 C 2 .   ? -14.873 24.165  5.551   1.00 77.05  ?  201 A1LV3 B H041 1 
HETATM 2029 H  H091 . A1LV3 C 2 .   ? -8.023  20.252  6.809   1.00 83.52  ?  201 A1LV3 B H091 1 
HETATM 2030 H  H121 . A1LV3 C 2 .   ? -10.512 16.835  9.749   1.00 79.87  ?  201 A1LV3 B H121 1 
HETATM 2031 H  H181 . A1LV3 C 2 .   ? -10.290 24.721  9.222   1.00 89.19  ?  201 A1LV3 B H181 1 
HETATM 2032 H  H191 . A1LV3 C 2 .   ? -12.266 23.653  10.400  1.00 86.57  ?  201 A1LV3 B H191 1 
HETATM 2033 H  H192 . A1LV3 C 2 .   ? -13.360 24.627  9.394   1.00 86.57  ?  201 A1LV3 B H192 1 
HETATM 2034 H  H291 . A1LV3 C 2 .   ? -20.416 18.040  3.272   1.00 50.35  ?  201 A1LV3 B H291 1 
HETATM 2035 H  H301 . A1LV3 C 2 .   ? -18.160 19.159  3.994   1.00 49.64  ?  201 A1LV3 B H301 1 
HETATM 2036 H  H331 . A1LV3 C 2 .   ? -20.350 16.749  9.297   1.00 48.40  ?  201 A1LV3 B H331 1 
HETATM 2037 H  H341 . A1LV3 C 2 .   ? -21.523 15.116  10.970  1.00 55.74  ?  201 A1LV3 B H341 1 
HETATM 2038 H  H351 . A1LV3 C 2 .   ? -22.581 12.899  10.080  1.00 57.87  ?  201 A1LV3 B H351 1 
HETATM 2039 H  H371 . A1LV3 C 2 .   ? -21.271 13.933  5.871   1.00 62.45  ?  201 A1LV3 B H371 1 
HETATM 2040 H  H391 . A1LV3 C 2 .   ? -21.437 11.046  8.838   1.00 82.02  ?  201 A1LV3 B H391 1 
HETATM 2041 H  H392 . A1LV3 C 2 .   ? -23.134 10.533  8.751   1.00 82.02  ?  201 A1LV3 B H392 1 
HETATM 2042 H  H401 . A1LV3 C 2 .   ? -22.255 10.112  6.137   1.00 76.44  ?  201 A1LV3 B H401 1 
HETATM 2043 H  H402 . A1LV3 C 2 .   ? -20.823 9.679   7.080   1.00 76.44  ?  201 A1LV3 B H402 1 
HETATM 2044 H  H411 . A1LV3 C 2 .   ? -21.889 7.887   8.133   1.00 75.22  ?  201 A1LV3 B H411 1 
HETATM 2045 H  H412 . A1LV3 C 2 .   ? -23.490 8.632   8.008   1.00 75.22  ?  201 A1LV3 B H412 1 
HETATM 2046 H  H431 . A1LV3 C 2 .   ? -20.710 7.673   6.124   1.00 79.29  ?  201 A1LV3 B H431 1 
HETATM 2047 H  H432 . A1LV3 C 2 .   ? -21.559 6.965   4.743   1.00 79.29  ?  201 A1LV3 B H432 1 
HETATM 2048 H  H441 . A1LV3 C 2 .   ? -21.353 5.756   7.507   1.00 81.64  ?  201 A1LV3 B H441 1 
HETATM 2049 H  H442 . A1LV3 C 2 .   ? -20.428 5.254   6.089   1.00 81.64  ?  201 A1LV3 B H442 1 
HETATM 2050 H  H451 . A1LV3 C 2 .   ? -22.629 4.041   6.879   1.00 83.85  ?  201 A1LV3 B H451 1 
HETATM 2051 H  H462 . A1LV3 C 2 .   ? -24.580 4.741   6.009   1.00 90.00  ?  201 A1LV3 B H462 1 
HETATM 2052 H  H461 . A1LV3 C 2 .   ? -23.804 5.614   4.680   1.00 90.00  ?  201 A1LV3 B H461 1 
HETATM 2053 H  H472 . A1LV3 C 2 .   ? -23.973 6.492   7.572   1.00 83.59  ?  201 A1LV3 B H472 1 
HETATM 2054 H  H471 . A1LV3 C 2 .   ? -24.862 7.179   6.201   1.00 83.59  ?  201 A1LV3 B H471 1 
HETATM 2055 H  H521 . A1LV3 C 2 .   ? -11.273 20.089  5.767   1.00 82.80  ?  201 A1LV3 B H521 1 
HETATM 2056 H  H522 . A1LV3 C 2 .   ? -10.262 21.396  6.392   1.00 82.80  ?  201 A1LV3 B H522 1 
HETATM 2057 H  H1   . A1LV3 C 2 .   ? -11.803 22.781  8.461   1.00 103.69 ?  201 A1LV3 B H1   1 
HETATM 2058 H  H201 . A1LV3 C 2 .   ? -11.398 25.798  11.024  1.00 94.55  ?  201 A1LV3 B H201 1 
HETATM 2059 H  H481 . A1LV3 C 2 .   ? -21.731 4.559   4.219   1.00 96.83  ?  201 A1LV3 B H481 1 
HETATM 2060 O  O    . HOH   D 3 .   ? -18.295 7.004   8.585   1.00 63.63  ?  201 HOH   A O    1 
HETATM 2061 O  O    . HOH   D 3 .   ? -23.883 21.259  6.570   1.00 57.52  ?  202 HOH   A O    1 
HETATM 2062 O  O    . HOH   D 3 .   ? -9.638  17.382  4.999   1.00 46.07  ?  203 HOH   A O    1 
HETATM 2063 O  O    . HOH   D 3 .   ? 2.371   13.119  -14.024 1.00 57.52  ?  204 HOH   A O    1 
HETATM 2064 O  O    . HOH   D 3 .   ? -7.473  8.849   2.684   1.00 43.95  ?  205 HOH   A O    1 
HETATM 2065 O  O    . HOH   D 3 .   ? -32.990 23.854  -5.529  1.00 57.52  ?  206 HOH   A O    1 
HETATM 2066 O  O    . HOH   D 3 .   ? 1.793   6.694   -17.625 1.00 40.75  ?  207 HOH   A O    1 
HETATM 2067 O  O    . HOH   D 3 .   ? 0.680   4.225   -17.845 1.00 56.31  ?  208 HOH   A O    1 
HETATM 2068 O  O    . HOH   D 3 .   ? -17.630 7.469   -8.672  1.00 50.80  ?  209 HOH   A O    1 
HETATM 2069 O  O    . HOH   D 3 .   ? -10.091 10.559  5.775   1.00 57.41  ?  210 HOH   A O    1 
HETATM 2070 O  O    . HOH   D 3 .   ? 13.178  7.588   -13.052 1.00 46.95  ?  211 HOH   A O    1 
HETATM 2071 O  O    . HOH   D 3 .   ? -12.515 24.380  -2.848  1.00 57.52  ?  212 HOH   A O    1 
HETATM 2072 O  O    . HOH   D 3 .   ? -32.984 20.321  -4.521  1.00 57.52  ?  213 HOH   A O    1 
HETATM 2073 O  O    . HOH   D 3 .   ? -31.320 17.193  0.731   1.00 51.72  ?  214 HOH   A O    1 
HETATM 2074 O  O    . HOH   D 3 .   ? 1.513   1.158   -10.031 1.00 57.52  ?  215 HOH   A O    1 
HETATM 2075 O  O    . HOH   D 3 .   ? -11.193 3.186   -13.893 1.00 38.33  ?  216 HOH   A O    1 
HETATM 2076 O  O    . HOH   D 3 .   ? -4.890  10.250  7.499   1.00 57.52  ?  217 HOH   A O    1 
HETATM 2077 O  O    . HOH   D 3 .   ? 0.914   4.999   -5.855  1.00 49.52  ?  218 HOH   A O    1 
HETATM 2078 O  O    . HOH   D 3 .   ? -0.428  9.259   -19.221 1.00 38.74  ?  219 HOH   A O    1 
HETATM 2079 O  O    . HOH   D 3 .   ? 1.325   16.287  -11.450 1.00 57.52  ?  220 HOH   A O    1 
HETATM 2080 O  O    . HOH   D 3 .   ? -6.345  2.915   -16.750 1.00 49.00  ?  221 HOH   A O    1 
HETATM 2081 O  O    . HOH   D 3 .   ? 1.196   14.732  -17.870 1.00 59.74  ?  222 HOH   A O    1 
HETATM 2082 O  O    . HOH   D 3 .   ? -0.486  13.906  -4.722  1.00 56.17  ?  223 HOH   A O    1 
HETATM 2083 O  O    . HOH   D 3 .   ? 4.458   10.298  -9.057  1.00 54.71  ?  224 HOH   A O    1 
HETATM 2084 O  O    . HOH   D 3 .   ? 7.227   9.743   -9.866  1.00 50.84  ?  225 HOH   A O    1 
HETATM 2085 O  O    . HOH   D 3 .   ? 7.273   -0.035  -16.862 1.00 38.84  ?  226 HOH   A O    1 
HETATM 2086 O  O    . HOH   D 3 .   ? 7.049   3.612   -6.793  1.00 47.10  ?  227 HOH   A O    1 
HETATM 2087 O  O    . HOH   D 3 .   ? -1.810  2.537   -6.930  1.00 43.36  ?  228 HOH   A O    1 
HETATM 2088 O  O    . HOH   D 3 .   ? -7.730  9.037   5.696   1.00 57.52  ?  229 HOH   A O    1 
HETATM 2089 O  O    . HOH   D 3 .   ? -5.484  6.565   1.366   1.00 44.87  ?  230 HOH   A O    1 
HETATM 2090 O  O    . HOH   D 3 .   ? 8.140   11.514  -11.816 1.00 57.52  ?  231 HOH   A O    1 
HETATM 2091 O  O    . HOH   D 3 .   ? 15.929  -0.408  -9.106  1.00 47.44  ?  232 HOH   A O    1 
HETATM 2092 O  O    . HOH   D 3 .   ? 10.104  3.543   -17.730 1.00 36.06  ?  233 HOH   A O    1 
HETATM 2093 O  O    . HOH   D 3 .   ? -4.056  12.332  8.430   1.00 57.52  ?  234 HOH   A O    1 
HETATM 2094 O  O    . HOH   D 3 .   ? -4.878  2.657   -3.842  1.00 45.19  ?  235 HOH   A O    1 
HETATM 2095 O  O    . HOH   D 3 .   ? -6.017  6.733   -17.135 1.00 40.49  ?  236 HOH   A O    1 
HETATM 2096 O  O    . HOH   D 3 .   ? -32.072 16.648  -1.715  1.00 68.55  ?  237 HOH   A O    1 
HETATM 2097 O  O    . HOH   D 3 .   ? -9.718  0.810   -0.096  1.00 57.52  ?  238 HOH   A O    1 
HETATM 2098 O  O    . HOH   D 3 .   ? -13.589 1.995   -2.239  1.00 57.52  ?  239 HOH   A O    1 
HETATM 2099 O  O    . HOH   D 3 .   ? -17.983 4.538   1.340   1.00 48.24  ?  240 HOH   A O    1 
HETATM 2100 O  O    . HOH   D 3 .   ? -6.438  11.785  -19.590 1.00 49.09  ?  241 HOH   A O    1 
HETATM 2101 O  O    . HOH   D 3 .   ? 1.292   13.081  -19.380 1.00 59.38  ?  242 HOH   A O    1 
HETATM 2102 O  O    . HOH   D 3 .   ? -33.320 9.530   4.421   1.00 67.92  ?  243 HOH   A O    1 
HETATM 2103 O  O    . HOH   D 3 .   ? -4.882  20.030  4.205   1.00 47.97  ?  244 HOH   A O    1 
HETATM 2104 O  O    . HOH   D 3 .   ? -22.845 4.426   -3.293  1.00 57.52  ?  245 HOH   A O    1 
HETATM 2105 O  O    . HOH   D 3 .   ? -15.595 28.162  4.434   1.00 57.52  ?  246 HOH   A O    1 
HETATM 2106 O  O    . HOH   D 3 .   ? -26.680 7.027   4.322   1.00 57.52  ?  247 HOH   A O    1 
HETATM 2107 O  O    . HOH   D 3 .   ? 2.205   2.124   -16.870 1.00 51.87  ?  248 HOH   A O    1 
HETATM 2108 O  O    . HOH   D 3 .   ? -33.673 17.792  -2.535  1.00 62.24  ?  249 HOH   A O    1 
HETATM 2109 O  O    . HOH   D 3 .   ? 7.955   11.088  -7.242  1.00 71.25  ?  250 HOH   A O    1 
HETATM 2110 O  O    . HOH   D 3 .   ? 1.580   0.088   -7.639  1.00 52.03  ?  251 HOH   A O    1 
HETATM 2111 O  O    . HOH   D 3 .   ? 9.238   10.750  -14.179 1.00 57.52  ?  252 HOH   A O    1 
HETATM 2112 O  O    . HOH   D 3 .   ? 7.251   7.325   -17.109 1.00 47.02  ?  253 HOH   A O    1 
HETATM 2113 O  O    . HOH   D 3 .   ? 4.082   12.813  -16.625 1.00 57.52  ?  254 HOH   A O    1 
HETATM 2114 O  O    . HOH   D 3 .   ? -10.986 5.982   -14.976 1.00 47.22  ?  255 HOH   A O    1 
HETATM 2115 O  O    . HOH   D 3 .   ? 8.309   9.531   -16.273 1.00 58.53  ?  256 HOH   A O    1 
HETATM 2116 O  O    . HOH   D 3 .   ? 4.540   7.657   -17.926 1.00 45.38  ?  257 HOH   A O    1 
HETATM 2117 O  O    . HOH   D 3 .   ? 4.187   9.861   -18.898 1.00 48.81  ?  258 HOH   A O    1 
HETATM 2118 O  O    . HOH   D 3 .   ? -5.579  -0.178  -4.390  1.00 57.52  ?  259 HOH   A O    1 
HETATM 2119 O  O    . HOH   E 3 .   ? -32.918 18.561  13.043  1.00 57.52  ?  301 HOH   B O    1 
HETATM 2120 O  O    . HOH   E 3 .   ? -30.797 16.363  15.964  1.00 76.08  ?  302 HOH   B O    1 
HETATM 2121 O  O    . HOH   E 3 .   ? -9.499  -9.122  26.244  1.00 62.62  ?  303 HOH   B O    1 
HETATM 2122 O  O    . HOH   E 3 .   ? -33.801 29.086  24.943  1.00 53.58  ?  304 HOH   B O    1 
HETATM 2123 O  O    . HOH   E 3 .   ? -26.784 21.088  10.054  1.00 57.52  ?  305 HOH   B O    1 
HETATM 2124 O  O    . HOH   E 3 .   ? -5.358  -10.685 19.017  1.00 74.17  ?  306 HOH   B O    1 
HETATM 2125 O  O    . HOH   E 3 .   ? -24.944 12.001  8.903   1.00 58.72  ?  307 HOH   B O    1 
HETATM 2126 O  O    . HOH   E 3 .   ? -4.193  12.899  16.443  1.00 53.56  ?  308 HOH   B O    1 
HETATM 2127 O  O    . HOH   E 3 .   ? -4.082  5.440   30.337  1.00 50.98  ?  309 HOH   B O    1 
HETATM 2128 O  O    . HOH   E 3 .   ? -7.234  17.027  15.476  1.00 47.66  ?  310 HOH   B O    1 
HETATM 2129 O  O    . HOH   E 3 .   ? -15.342 0.016   31.994  1.00 54.77  ?  311 HOH   B O    1 
HETATM 2130 O  O    . HOH   E 3 .   ? -12.173 2.519   5.569   1.00 57.52  ?  312 HOH   B O    1 
HETATM 2131 O  O    . HOH   E 3 .   ? -5.298  10.591  27.642  1.00 37.07  ?  313 HOH   B O    1 
HETATM 2132 O  O    . HOH   E 3 .   ? -15.322 24.606  8.447   1.00 56.98  ?  314 HOH   B O    1 
HETATM 2133 O  O    . HOH   E 3 .   ? -6.717  4.192   12.633  1.00 47.93  ?  315 HOH   B O    1 
HETATM 2134 O  O    . HOH   E 3 .   ? -3.034  -0.437  21.298  1.00 57.52  ?  316 HOH   B O    1 
HETATM 2135 O  O    . HOH   E 3 .   ? -24.407 1.418   20.729  1.00 57.52  ?  317 HOH   B O    1 
HETATM 2136 O  O    . HOH   E 3 .   ? -5.298  -14.454 27.055  1.00 52.09  ?  318 HOH   B O    1 
HETATM 2137 O  O    . HOH   E 3 .   ? -2.152  -7.863  20.595  1.00 51.16  ?  319 HOH   B O    1 
HETATM 2138 O  O    . HOH   E 3 .   ? -9.239  -1.171  33.029  1.00 40.41  ?  320 HOH   B O    1 
HETATM 2139 O  O    . HOH   E 3 .   ? -9.805  6.133   30.367  1.00 44.72  ?  321 HOH   B O    1 
HETATM 2140 O  O    . HOH   E 3 .   ? -3.726  -1.768  31.298  1.00 47.81  ?  322 HOH   B O    1 
HETATM 2141 O  O    . HOH   E 3 .   ? -24.519 -2.039  11.128  1.00 57.52  ?  323 HOH   B O    1 
HETATM 2142 O  O    . HOH   E 3 .   ? -8.230  13.595  28.899  1.00 67.45  ?  324 HOH   B O    1 
HETATM 2143 O  O    . HOH   E 3 .   ? -10.833 20.743  10.335  1.00 52.36  ?  325 HOH   B O    1 
HETATM 2144 O  O    . HOH   E 3 .   ? -2.849  1.342   20.785  1.00 57.52  ?  326 HOH   B O    1 
HETATM 2145 O  O    . HOH   E 3 .   ? -1.795  -10.688 31.590  1.00 41.79  ?  327 HOH   B O    1 
HETATM 2146 O  O    . HOH   E 3 .   ? -7.529  4.733   30.930  1.00 36.78  ?  328 HOH   B O    1 
HETATM 2147 O  O    . HOH   E 3 .   ? -5.925  -3.153  31.403  1.00 41.50  ?  329 HOH   B O    1 
HETATM 2148 O  O    . HOH   E 3 .   ? -9.266  -6.354  22.760  1.00 46.93  ?  330 HOH   B O    1 
HETATM 2149 O  O    . HOH   E 3 .   ? 0.465   1.510   23.767  1.00 46.25  ?  331 HOH   B O    1 
HETATM 2150 O  O    . HOH   E 3 .   ? -7.240  -1.411  11.169  1.00 72.65  ?  332 HOH   B O    1 
HETATM 2151 O  O    . HOH   E 3 .   ? 1.341   -7.313  30.747  1.00 44.50  ?  333 HOH   B O    1 
HETATM 2152 O  O    . HOH   E 3 .   ? -12.586 4.154   33.347  1.00 45.62  ?  334 HOH   B O    1 
HETATM 2153 O  O    . HOH   E 3 .   ? -0.639  4.470   31.442  1.00 46.41  ?  335 HOH   B O    1 
HETATM 2154 O  O    . HOH   E 3 .   ? -8.394  -8.527  23.554  1.00 50.23  ?  336 HOH   B O    1 
HETATM 2155 O  O    . HOH   E 3 .   ? -8.979  21.518  17.248  1.00 67.20  ?  337 HOH   B O    1 
HETATM 2156 O  O    . HOH   E 3 .   ? -12.227 -4.738  27.685  1.00 51.75  ?  338 HOH   B O    1 
HETATM 2157 O  O    . HOH   E 3 .   ? -18.350 25.024  6.835   1.00 57.39  ?  339 HOH   B O    1 
HETATM 2158 O  O    . HOH   E 3 .   ? -7.967  17.100  12.567  1.00 54.27  ?  340 HOH   B O    1 
HETATM 2159 O  O    . HOH   E 3 .   ? -2.234  9.471   14.484  1.00 47.85  ?  341 HOH   B O    1 
HETATM 2160 O  O    . HOH   E 3 .   ? -3.305  4.508   17.789  1.00 48.03  ?  342 HOH   B O    1 
HETATM 2161 O  O    . HOH   E 3 .   ? -4.296  -1.781  19.745  1.00 53.36  ?  343 HOH   B O    1 
HETATM 2162 O  O    . HOH   E 3 .   ? -16.583 28.763  14.443  1.00 58.13  ?  344 HOH   B O    1 
HETATM 2163 O  O    . HOH   E 3 .   ? -13.725 -1.822  18.086  1.00 57.52  ?  345 HOH   B O    1 
HETATM 2164 O  O    . HOH   E 3 .   ? -6.860  9.308   28.488  1.00 57.52  ?  346 HOH   B O    1 
HETATM 2165 O  O    . HOH   E 3 .   ? 0.000   0.000   30.504  0.50 56.35  ?  347 HOH   B O    1 
HETATM 2166 O  O    . HOH   E 3 .   ? -12.926 -3.658  33.758  1.00 50.31  ?  348 HOH   B O    1 
HETATM 2167 O  O    . HOH   E 3 .   ? -1.971  -2.351  30.660  1.00 52.01  ?  349 HOH   B O    1 
HETATM 2168 O  O    . HOH   E 3 .   ? -18.056 15.580  17.223  1.00 62.05  ?  350 HOH   B O    1 
HETATM 2169 O  O    . HOH   E 3 .   ? -8.120  10.542  28.859  1.00 54.99  ?  351 HOH   B O    1 
HETATM 2170 O  O    . HOH   E 3 .   ? -3.535  -13.019 17.990  1.00 57.52  ?  352 HOH   B O    1 
HETATM 2171 O  O    . HOH   E 3 .   ? 0.117   -1.664  21.400  1.00 47.35  ?  353 HOH   B O    1 
HETATM 2172 O  O    . HOH   E 3 .   ? -5.470  7.171   32.073  1.00 42.46  ?  354 HOH   B O    1 
HETATM 2173 O  O    . HOH   E 3 .   ? -7.990  4.076   33.417  1.00 41.87  ?  355 HOH   B O    1 
HETATM 2174 O  O    . HOH   E 3 .   ? -9.356  12.092  29.403  1.00 54.25  ?  356 HOH   B O    1 
HETATM 2175 O  O    . HOH   E 3 .   ? -7.968  -13.904 28.264  1.00 64.61  ?  357 HOH   B O    1 
HETATM 2176 O  O    . HOH   E 3 .   ? -6.869  -5.629  31.689  1.00 47.72  ?  358 HOH   B O    1 
HETATM 2177 O  O    . HOH   E 3 .   ? -8.708  -5.594  32.873  1.00 52.61  ?  359 HOH   B O    1 
HETATM 2178 O  O    . HOH   E 3 .   ? -6.895  9.260   31.495  1.00 48.37  ?  360 HOH   B O    1 
HETATM 2179 O  O    . HOH   E 3 .   ? -10.571 4.986   34.138  1.00 47.92  ?  361 HOH   B O    1 
HETATM 2180 O  O    . HOH   E 3 .   ? -6.873  20.034  16.434  1.00 61.48  ?  362 HOH   B 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   . PHE A 1   ? 0.6668 0.6817 0.7533 0.0917  -0.0713 0.0530  1   PHE A N   
2    C CA  . PHE A 1   ? 0.7742 0.7962 0.8491 0.0868  -0.0854 0.0529  1   PHE A CA  
3    C C   . PHE A 1   ? 0.6719 0.6793 0.7370 0.0854  -0.0719 0.0482  1   PHE A C   
4    O O   . PHE A 1   ? 0.7252 0.7113 0.7834 0.0996  -0.0593 0.0513  1   PHE A O   
5    C CB  . PHE A 1   ? 0.7653 0.7857 0.8302 0.1027  -0.1027 0.0639  1   PHE A CB  
6    C CG  . PHE A 1   ? 0.6214 0.6509 0.6771 0.0976  -0.1183 0.0648  1   PHE A CG  
7    C CD1 . PHE A 1   ? 0.6214 0.6741 0.6816 0.0821  -0.1333 0.0620  1   PHE A CD1 
8    C CD2 . PHE A 1   ? 0.6523 0.6667 0.6951 0.1083  -0.1174 0.0685  1   PHE A CD2 
9    C CE1 . PHE A 1   ? 0.6014 0.6621 0.6533 0.0778  -0.1466 0.0633  1   PHE A CE1 
10   C CE2 . PHE A 1   ? 0.6244 0.6471 0.6605 0.1036  -0.1308 0.0698  1   PHE A CE2 
11   C CZ  . PHE A 1   ? 0.5610 0.6067 0.6015 0.0885  -0.1450 0.0675  1   PHE A CZ  
12   N N   . THR A 2   ? 0.5311 0.5494 0.5949 0.0686  -0.0746 0.0407  2   THR A N   
13   C CA  . THR A 2   ? 0.5502 0.5561 0.6058 0.0651  -0.0611 0.0351  2   THR A CA  
14   C C   . THR A 2   ? 0.5463 0.5627 0.5926 0.0565  -0.0741 0.0342  2   THR A C   
15   O O   . THR A 2   ? 0.4929 0.5290 0.5429 0.0426  -0.0863 0.0308  2   THR A O   
16   C CB  . THR A 2   ? 0.6913 0.6958 0.7566 0.0515  -0.0431 0.0242  2   THR A CB  
17   O OG1 . THR A 2   ? 0.8697 0.8700 0.9476 0.0570  -0.0340 0.0253  2   THR A OG1 
18   C CG2 . THR A 2   ? 0.7145 0.7003 0.7714 0.0532  -0.0253 0.0201  2   THR A CG2 
19   N N   . VAL A 3   ? 0.6427 0.6455 0.6773 0.0651  -0.0712 0.0375  3   VAL A N   
20   C CA  . VAL A 3   ? 0.5972 0.6060 0.6233 0.0568  -0.0778 0.0358  3   VAL A CA  
21   C C   . VAL A 3   ? 0.5460 0.5464 0.5699 0.0463  -0.0590 0.0259  3   VAL A C   
22   O O   . VAL A 3   ? 0.4736 0.4556 0.4972 0.0532  -0.0412 0.0242  3   VAL A O   
23   C CB  . VAL A 3   ? 0.5414 0.5407 0.5578 0.0721  -0.0862 0.0454  3   VAL A CB  
24   C CG1 . VAL A 3   ? 0.6002 0.6031 0.6090 0.0639  -0.0890 0.0435  3   VAL A CG1 
25   C CG2 . VAL A 3   ? 0.5542 0.5638 0.5728 0.0808  -0.1068 0.0546  3   VAL A CG2 
26   N N   . THR A 4   ? 0.5214 0.5347 0.5433 0.0300  -0.0629 0.0192  4   THR A N   
27   C CA  . THR A 4   ? 0.5402 0.5466 0.5585 0.0191  -0.0468 0.0094  4   THR A CA  
28   C C   . THR A 4   ? 0.5443 0.5550 0.5514 0.0135  -0.0533 0.0096  4   THR A C   
29   O O   . THR A 4   ? 0.5630 0.5881 0.5678 0.0121  -0.0714 0.0147  4   THR A O   
30   C CB  . THR A 4   ? 0.5231 0.5399 0.5508 0.0025  -0.0423 -0.0014 4   THR A CB  
31   O OG1 . THR A 4   ? 0.5908 0.6293 0.6225 -0.0053 -0.0615 -0.0006 4   THR A OG1 
32   C CG2 . THR A 4   ? 0.6876 0.6950 0.7273 0.0075  -0.0286 -0.0030 4   THR A CG2 
33   N N   . VAL A 5   ? 0.5047 0.5029 0.5053 0.0105  -0.0380 0.0044  5   VAL A N   
34   C CA  . VAL A 5   ? 0.6281 0.6287 0.6181 0.0043  -0.0406 0.0036  5   VAL A CA  
35   C C   . VAL A 5   ? 0.5735 0.5768 0.5616 -0.0128 -0.0302 -0.0090 5   VAL A C   
36   O O   . VAL A 5   ? 0.6523 0.6432 0.6432 -0.0146 -0.0125 -0.0159 5   VAL A O   
37   C CB  . VAL A 5   ? 0.5800 0.5625 0.5629 0.0166  -0.0323 0.0090  5   VAL A CB  
38   C CG1 . VAL A 5   ? 0.5002 0.4815 0.4839 0.0329  -0.0462 0.0214  5   VAL A CG1 
39   C CG2 . VAL A 5   ? 0.7288 0.6915 0.7130 0.0208  -0.0104 0.0041  5   VAL A CG2 
40   N N   . PRO A 6   ? 0.6554 0.6740 0.6384 -0.0255 -0.0406 -0.0125 6   PRO A N   
41   C CA  . PRO A 6   ? 0.7432 0.7624 0.7222 -0.0412 -0.0309 -0.0249 6   PRO A CA  
42   C C   . PRO A 6   ? 0.5635 0.5651 0.5339 -0.0400 -0.0131 -0.0281 6   PRO A C   
43   O O   . PRO A 6   ? 0.7030 0.6975 0.6735 -0.0485 0.0014  -0.0385 6   PRO A O   
44   C CB  . PRO A 6   ? 0.7351 0.7728 0.7072 -0.0516 -0.0475 -0.0255 6   PRO A CB  
45   C CG  . PRO A 6   ? 0.7971 0.8419 0.7687 -0.0410 -0.0638 -0.0127 6   PRO A CG  
46   C CD  . PRO A 6   ? 0.6117 0.6455 0.5909 -0.0249 -0.0609 -0.0048 6   PRO A CD  
47   N N   . LYS A 7   ? 0.5696 0.5642 0.5332 -0.0299 -0.0141 -0.0195 7   LYS A N   
48   C CA  . LYS A 7   ? 0.4996 0.4762 0.4565 -0.0265 0.0030  -0.0211 7   LYS A CA  
49   C C   . LYS A 7   ? 0.5725 0.5373 0.5307 -0.0085 0.0026  -0.0099 7   LYS A C   
50   O O   . LYS A 7   ? 0.6039 0.5765 0.5626 -0.0013 -0.0133 -0.0002 7   LYS A O   
51   C CB  . LYS A 7   ? 0.7510 0.7307 0.6956 -0.0363 0.0038  -0.0246 7   LYS A CB  
52   C CG  . LYS A 7   ? 0.7547 0.7455 0.6941 -0.0338 -0.0126 -0.0154 7   LYS A CG  
53   C CD  . LYS A 7   ? 0.7736 0.7686 0.7006 -0.0460 -0.0103 -0.0211 7   LYS A CD  
54   C CE  . LYS A 7   ? 0.7003 0.6774 0.6203 -0.0456 0.0094  -0.0252 7   LYS A CE  
55   N NZ  . LYS A 7   ? 0.6550 0.6319 0.5654 -0.0449 0.0081  -0.0197 7   LYS A NZ  
56   N N   . ASP A 8   ? 0.5737 0.5196 0.5328 -0.0011 0.0198  -0.0113 8   ASP A N   
57   C CA  . ASP A 8   ? 0.5452 0.4768 0.5046 0.0165  0.0212  -0.0019 8   ASP A CA  
58   C C   . ASP A 8   ? 0.6230 0.5430 0.5745 0.0195  0.0294  -0.0001 8   ASP A C   
59   O O   . ASP A 8   ? 0.4568 0.3624 0.4083 0.0338  0.0329  0.0065  8   ASP A O   
60   C CB  . ASP A 8   ? 0.6362 0.5533 0.6016 0.0249  0.0344  -0.0035 8   ASP A CB  
61   C CG  . ASP A 8   ? 0.6972 0.6002 0.6604 0.0190  0.0568  -0.0130 8   ASP A CG  
62   O OD1 . ASP A 8   ? 0.7088 0.6149 0.6661 0.0067  0.0615  -0.0197 8   ASP A OD1 
63   O OD2 . ASP A 8   ? 0.9980 0.8863 0.9651 0.0270  0.0700  -0.0137 8   ASP A OD2 
64   N N   . LEU A 9   ? 0.5272 0.4525 0.4717 0.0067  0.0326  -0.0058 9   LEU A N   
65   C CA  . LEU A 9   ? 0.5259 0.4422 0.4632 0.0085  0.0395  -0.0036 9   LEU A CA  
66   C C   . LEU A 9   ? 0.5735 0.5052 0.5046 -0.0017 0.0289  -0.0031 9   LEU A C   
67   O O   . LEU A 9   ? 0.5125 0.4554 0.4403 -0.0155 0.0272  -0.0110 9   LEU A O   
68   C CB  . LEU A 9   ? 0.5597 0.4604 0.4928 0.0039  0.0621  -0.0129 9   LEU A CB  
69   C CG  . LEU A 9   ? 0.5999 0.4907 0.5254 0.0047  0.0712  -0.0116 9   LEU A CG  
70   C CD1 . LEU A 9   ? 0.6443 0.5209 0.5730 0.0220  0.0723  -0.0018 9   LEU A CD1 
71   C CD2 . LEU A 9   ? 0.6655 0.5461 0.5854 -0.0051 0.0915  -0.0231 9   LEU A CD2 
72   N N   . TYR A 10  ? 0.4701 0.4016 0.3999 0.0054  0.0219  0.0063  10  TYR A N   
73   C CA  . TYR A 10  ? 0.5495 0.4929 0.4729 -0.0025 0.0140  0.0083  10  TYR A CA  
74   C C   . TYR A 10  ? 0.5334 0.4642 0.4524 0.0013  0.0252  0.0112  10  TYR A C   
75   O O   . TYR A 10  ? 0.4608 0.3794 0.3851 0.0145  0.0273  0.0181  10  TYR A O   
76   C CB  . TYR A 10  ? 0.5692 0.5278 0.4978 0.0024  -0.0081 0.0186  10  TYR A CB  
77   C CG  . TYR A 10  ? 0.5399 0.5139 0.4721 -0.0028 -0.0210 0.0162  10  TYR A CG  
78   C CD1 . TYR A 10  ? 0.4884 0.4591 0.4286 0.0043  -0.0224 0.0165  10  TYR A CD1 
79   C CD2 . TYR A 10  ? 0.4645 0.4562 0.3921 -0.0144 -0.0319 0.0142  10  TYR A CD2 
80   C CE1 . TYR A 10  ? 0.4642 0.4492 0.4089 -0.0004 -0.0340 0.0147  10  TYR A CE1 
81   C CE2 . TYR A 10  ? 0.5720 0.5781 0.5037 -0.0192 -0.0441 0.0121  10  TYR A CE2 
82   C CZ  . TYR A 10  ? 0.6284 0.6312 0.5692 -0.0123 -0.0450 0.0124  10  TYR A CZ  
83   O OH  . TYR A 10  ? 0.5239 0.5411 0.4699 -0.0170 -0.0569 0.0106  10  TYR A OH  
84   N N   . VAL A 11  ? 0.4633 0.3964 0.3725 -0.0099 0.0321  0.0059  11  VAL A N   
85   C CA  . VAL A 11  ? 0.5137 0.4365 0.4183 -0.0077 0.0426  0.0087  11  VAL A CA  
86   C C   . VAL A 11  ? 0.5923 0.5290 0.4928 -0.0121 0.0311  0.0147  11  VAL A C   
87   O O   . VAL A 11  ? 0.6112 0.5584 0.5025 -0.0243 0.0289  0.0085  11  VAL A O   
88   C CB  . VAL A 11  ? 0.5632 0.4740 0.4586 -0.0162 0.0635  -0.0027 11  VAL A CB  
89   C CG1 . VAL A 11  ? 0.6359 0.5383 0.5257 -0.0152 0.0734  0.0006  11  VAL A CG1 
90   C CG2 . VAL A 11  ? 0.6022 0.4982 0.5029 -0.0106 0.0759  -0.0074 11  VAL A CG2 
91   N N   . VAL A 12  ? 0.4582 0.3946 0.3656 -0.0018 0.0235  0.0267  12  VAL A N   
92   C CA  . VAL A 12  ? 0.4541 0.4045 0.3606 -0.0039 0.0103  0.0345  12  VAL A CA  
93   C C   . VAL A 12  ? 0.5539 0.4960 0.4612 0.0010  0.0178  0.0416  12  VAL A C   
94   O O   . VAL A 12  ? 0.5155 0.4425 0.4289 0.0103  0.0267  0.0443  12  VAL A O   
95   C CB  . VAL A 12  ? 0.6072 0.5694 0.5249 0.0040  -0.0109 0.0438  12  VAL A CB  
96   C CG1 . VAL A 12  ? 0.6050 0.5729 0.5237 0.0009  -0.0165 0.0372  12  VAL A CG1 
97   C CG2 . VAL A 12  ? 0.7394 0.6908 0.6693 0.0198  -0.0135 0.0537  12  VAL A CG2 
98   N N   . GLU A 13  ? 0.5000 0.4519 0.4015 -0.0051 0.0140  0.0451  13  GLU A N   
99   C CA  . GLU A 13  ? 0.5543 0.5001 0.4567 -0.0015 0.0212  0.0523  13  GLU A CA  
100  C C   . GLU A 13  ? 0.5337 0.4853 0.4515 0.0095  0.0056  0.0668  13  GLU A C   
101  O O   . GLU A 13  ? 0.5290 0.4955 0.4506 0.0094  -0.0119 0.0714  13  GLU A O   
102  C CB  . GLU A 13  ? 0.4818 0.4340 0.3693 -0.0131 0.0264  0.0490  13  GLU A CB  
103  C CG  . GLU A 13  ? 0.6077 0.5555 0.4791 -0.0250 0.0395  0.0341  13  GLU A CG  
104  C CD  . GLU A 13  ? 0.6391 0.5676 0.5099 -0.0226 0.0590  0.0279  13  GLU A CD  
105  O OE1 . GLU A 13  ? 0.6897 0.6079 0.5632 -0.0170 0.0689  0.0335  13  GLU A OE1 
106  O OE2 . GLU A 13  ? 0.6258 0.5495 0.4942 -0.0263 0.0646  0.0176  13  GLU A OE2 
107  N N   . TYR A 14  ? 0.5809 0.5203 0.5082 0.0192  0.0119  0.0737  14  TYR A N   
108  C CA  . TYR A 14  ? 0.5290 0.4726 0.4720 0.0295  -0.0016 0.0876  14  TYR A CA  
109  C C   . TYR A 14  ? 0.5136 0.4737 0.4542 0.0233  -0.0110 0.0936  14  TYR A C   
110  O O   . TYR A 14  ? 0.5596 0.5210 0.4878 0.0142  -0.0006 0.0903  14  TYR A O   
111  C CB  . TYR A 14  ? 0.4744 0.4022 0.4260 0.0379  0.0100  0.0928  14  TYR A CB  
112  C CG  . TYR A 14  ? 0.5212 0.4519 0.4907 0.0481  -0.0019 0.1072  14  TYR A CG  
113  C CD1 . TYR A 14  ? 0.5802 0.5184 0.5513 0.0447  -0.0017 0.1146  14  TYR A CD1 
114  C CD2 . TYR A 14  ? 0.5411 0.4662 0.5260 0.0615  -0.0132 0.1134  14  TYR A CD2 
115  C CE1 . TYR A 14  ? 0.6022 0.5430 0.5919 0.0538  -0.0124 0.1279  14  TYR A CE1 
116  C CE2 . TYR A 14  ? 0.6250 0.5524 0.6278 0.0708  -0.0249 0.1261  14  TYR A CE2 
117  C CZ  . TYR A 14  ? 0.5621 0.4976 0.5682 0.0667  -0.0244 0.1335  14  TYR A CZ  
118  O OH  . TYR A 14  ? 0.6793 0.6172 0.7054 0.0758  -0.0359 0.1464  14  TYR A OH  
119  N N   . GLY A 15  ? 0.5245 0.4966 0.4764 0.0287  -0.0308 0.1026  15  GLY A N   
120  C CA  . GLY A 15  ? 0.5245 0.5125 0.4761 0.0243  -0.0415 0.1096  15  GLY A CA  
121  C C   . GLY A 15  ? 0.5448 0.5480 0.4840 0.0138  -0.0502 0.1032  15  GLY A C   
122  O O   . GLY A 15  ? 0.5666 0.5843 0.5067 0.0116  -0.0625 0.1098  15  GLY A O   
123  N N   . SER A 16  ? 0.5939 0.5941 0.5223 0.0075  -0.0442 0.0908  16  SER A N   
124  C CA  . SER A 16  ? 0.5390 0.5531 0.4568 -0.0025 -0.0525 0.0839  16  SER A CA  
125  C C   . SER A 16  ? 0.6515 0.6746 0.5802 0.0032  -0.0711 0.0872  16  SER A C   
126  O O   . SER A 16  ? 0.5699 0.5881 0.5133 0.0152  -0.0779 0.0948  16  SER A O   
127  C CB  . SER A 16  ? 0.5855 0.5925 0.4884 -0.0122 -0.0377 0.0689  16  SER A CB  
128  O OG  . SER A 16  ? 0.6845 0.6832 0.5934 -0.0077 -0.0357 0.0638  16  SER A OG  
129  N N   . ASN A 17  ? 0.6283 0.6641 0.5496 -0.0052 -0.0797 0.0812  17  ASN A N   
130  C CA  . ASN A 17  ? 0.6218 0.6662 0.5513 -0.0014 -0.0958 0.0824  17  ASN A CA  
131  C C   . ASN A 17  ? 0.6469 0.6856 0.5714 -0.0057 -0.0881 0.0701  17  ASN A C   
132  O O   . ASN A 17  ? 0.6307 0.6664 0.5429 -0.0160 -0.0755 0.0595  17  ASN A O   
133  C CB  . ASN A 17  ? 0.6224 0.6868 0.5493 -0.0074 -0.1125 0.0856  17  ASN A CB  
134  C CG  . ASN A 17  ? 0.4842 0.5551 0.4173 -0.0031 -0.1206 0.0985  17  ASN A CG  
135  O OD1 . ASN A 17  ? 0.5998 0.6625 0.5449 0.0072  -0.1196 0.1071  17  ASN A OD1 
136  N ND2 . ASN A 17  ? 0.6893 0.7749 0.6146 -0.0108 -0.1285 0.0999  17  ASN A ND2 
137  N N   . MET A 18  ? 0.6136 0.6894 0.6708 0.0488  0.0469  0.0159  18  MET A N   
138  C CA  . MET A 18  ? 0.5659 0.6481 0.6197 0.0559  0.0328  0.0210  18  MET A CA  
139  C C   . MET A 18  ? 0.4898 0.5703 0.5473 0.0535  0.0252  0.0171  18  MET A C   
140  O O   . MET A 18  ? 0.5078 0.6002 0.5804 0.0463  0.0294  0.0081  18  MET A O   
141  C CB  . MET A 18  ? 0.4929 0.6137 0.5641 0.0585  0.0282  0.0199  18  MET A CB  
142  C CG  . MET A 18  ? 0.7179 0.8741 0.8147 0.0522  0.0278  0.0098  18  MET A CG  
143  S SD  . MET A 18  ? 0.6350 0.8309 0.7466 0.0567  0.0166  0.0111  18  MET A SD  
144  C CE  . MET A 18  ? 0.6317 0.8649 0.7720 0.0472  0.0184  -0.0015 18  MET A CE  
145  N N   . THR A 19  ? 0.4900 0.5550 0.5337 0.0597  0.0143  0.0239  19  THR A N   
146  C CA  . THR A 19  ? 0.5138 0.5783 0.5609 0.0588  0.0055  0.0210  19  THR A CA  
147  C C   . THR A 19  ? 0.5392 0.6230 0.5889 0.0651  -0.0075 0.0247  19  THR A C   
148  O O   . THR A 19  ? 0.6159 0.6851 0.6490 0.0725  -0.0135 0.0342  19  THR A O   
149  C CB  . THR A 19  ? 0.5306 0.5534 0.5574 0.0595  0.0044  0.0257  19  THR A CB  
150  O OG1 . THR A 19  ? 0.5962 0.6036 0.6228 0.0522  0.0158  0.0208  19  THR A OG1 
151  C CG2 . THR A 19  ? 0.5389 0.5614 0.5690 0.0601  -0.0063 0.0236  19  THR A CG2 
152  N N   . ILE A 20  ? 0.4698 0.5865 0.5400 0.0619  -0.0117 0.0171  20  ILE A N   
153  C CA  . ILE A 20  ? 0.4287 0.5666 0.5031 0.0666  -0.0242 0.0195  20  ILE A CA  
154  C C   . ILE A 20  ? 0.4548 0.5891 0.5314 0.0653  -0.0320 0.0159  20  ILE A C   
155  O O   . ILE A 20  ? 0.5473 0.6834 0.6347 0.0586  -0.0275 0.0073  20  ILE A O   
156  C CB  . ILE A 20  ? 0.4091 0.5890 0.5048 0.0639  -0.0241 0.0141  20  ILE A CB  
157  C CG1 . ILE A 20  ? 0.5627 0.7612 0.6787 0.0544  -0.0166 0.0023  20  ILE A CG1 
158  C CG2 . ILE A 20  ? 0.5040 0.6869 0.5966 0.0669  -0.0185 0.0191  20  ILE A CG2 
159  C CD1 . ILE A 20  ? 0.6231 0.8624 0.7603 0.0509  -0.0161 -0.0030 20  ILE A CD1 
160  N N   . GLU A 21  ? 0.5274 0.6567 0.5941 0.0718  -0.0437 0.0224  21  GLU A N   
161  C CA  . GLU A 21  ? 0.5892 0.7051 0.6525 0.0722  -0.0511 0.0214  21  GLU A CA  
162  C C   . GLU A 21  ? 0.6401 0.7856 0.7155 0.0729  -0.0619 0.0184  21  GLU A C   
163  O O   . GLU A 21  ? 0.4270 0.5929 0.5039 0.0764  -0.0673 0.0221  21  GLU A O   
164  C CB  . GLU A 21  ? 0.5288 0.6065 0.5670 0.0792  -0.0557 0.0324  21  GLU A CB  
165  C CG  . GLU A 21  ? 0.9614 1.0042 0.9876 0.0766  -0.0465 0.0336  21  GLU A CG  
166  C CD  . GLU A 21  ? 0.8210 0.8252 0.8236 0.0822  -0.0523 0.0434  21  GLU A CD  
167  O OE1 . GLU A 21  ? 0.9451 0.9240 0.9427 0.0793  -0.0505 0.0419  21  GLU A OE1 
168  O OE2 . GLU A 21  ? 0.9185 0.9176 0.9077 0.0894  -0.0591 0.0526  21  GLU A OE2 
169  N N   . CYS A 22  ? 0.5735 0.7212 0.6576 0.0692  -0.0649 0.0114  22  CYS A N   
170  C CA  . CYS A 22  ? 0.4463 0.6154 0.5382 0.0702  -0.0760 0.0093  22  CYS A CA  
171  C C   . CYS A 22  ? 0.4160 0.5614 0.5007 0.0720  -0.0820 0.0098  22  CYS A C   
172  O O   . CYS A 22  ? 0.5705 0.6968 0.6560 0.0684  -0.0763 0.0055  22  CYS A O   
173  C CB  . CYS A 22  ? 0.5260 0.7331 0.6424 0.0623  -0.0738 -0.0025 22  CYS A CB  
174  S SG  . CYS A 22  ? 0.6975 0.9417 0.8239 0.0619  -0.0739 -0.0016 22  CYS A SG  
175  N N   . LYS A 23  ? 0.5815 0.7281 0.6594 0.0776  -0.0936 0.0151  23  LYS A N   
176  C CA  . LYS A 23  ? 0.5278 0.6513 0.5975 0.0805  -0.1007 0.0172  23  LYS A CA  
177  C C   . LYS A 23  ? 0.5064 0.6554 0.5935 0.0768  -0.1065 0.0079  23  LYS A C   
178  O O   . LYS A 23  ? 0.5180 0.6992 0.6148 0.0757  -0.1109 0.0055  23  LYS A O   
179  C CB  . LYS A 23  ? 0.6309 0.7359 0.6796 0.0896  -0.1100 0.0301  23  LYS A CB  
180  C CG  . LYS A 23  ? 0.7690 0.8523 0.7995 0.0940  -0.1053 0.0401  23  LYS A CG  
181  C CD  . LYS A 23  ? 0.8338 0.8823 0.8552 0.0921  -0.0974 0.0407  23  LYS A CD  
182  C CE  . LYS A 23  ? 0.8194 0.8321 0.8152 0.0984  -0.0981 0.0533  23  LYS A CE  
183  N NZ  . LYS A 23  ? 0.9651 0.9739 0.9479 0.1063  -0.1102 0.0627  23  LYS A NZ  
184  N N   . PHE A 24  ? 0.5370 0.6714 0.6281 0.0745  -0.1068 0.0027  24  PHE A N   
185  C CA  . PHE A 24  ? 0.4991 0.6525 0.6043 0.0720  -0.1133 -0.0053 24  PHE A CA  
186  C C   . PHE A 24  ? 0.4212 0.5452 0.5184 0.0755  -0.1191 -0.0029 24  PHE A C   
187  O O   . PHE A 24  ? 0.4981 0.5889 0.5846 0.0767  -0.1152 0.0009  24  PHE A O   
188  C CB  . PHE A 24  ? 0.5794 0.7576 0.7075 0.0626  -0.1058 -0.0194 24  PHE A CB  
189  C CG  . PHE A 24  ? 0.5120 0.6679 0.6427 0.0585  -0.0968 -0.0244 24  PHE A CG  
190  C CD1 . PHE A 24  ? 0.4331 0.5755 0.5573 0.0573  -0.0873 -0.0215 24  PHE A CD1 
191  C CD2 . PHE A 24  ? 0.5342 0.6838 0.6747 0.0554  -0.0978 -0.0324 24  PHE A CD2 
192  C CE1 . PHE A 24  ? 0.4969 0.6190 0.6231 0.0531  -0.0792 -0.0260 24  PHE A CE1 
193  C CE2 . PHE A 24  ? 0.4361 0.5652 0.5792 0.0514  -0.0900 -0.0369 24  PHE A CE2 
194  C CZ  . PHE A 24  ? 0.4539 0.5691 0.5894 0.0501  -0.0808 -0.0336 24  PHE A CZ  
195  N N   . PRO A 25  ? 0.5345 0.6694 0.6365 0.0770  -0.1285 -0.0048 25  PRO A N   
196  C CA  . PRO A 25  ? 0.5339 0.6407 0.6279 0.0812  -0.1352 -0.0015 25  PRO A CA  
197  C C   . PRO A 25  ? 0.5557 0.6509 0.6618 0.0759  -0.1298 -0.0111 25  PRO A C   
198  O O   . PRO A 25  ? 0.5341 0.6537 0.6600 0.0690  -0.1258 -0.0233 25  PRO A O   
199  C CB  . PRO A 25  ? 0.7103 0.8390 0.8093 0.0831  -0.1460 -0.0025 25  PRO A CB  
200  C CG  . PRO A 25  ? 0.5488 0.7186 0.6669 0.0761  -0.1424 -0.0128 25  PRO A CG  
201  C CD  . PRO A 25  ? 0.5146 0.6879 0.6292 0.0747  -0.1339 -0.0100 25  PRO A CD  
202  N N   . VAL A 26  ? 0.5255 0.5827 0.6190 0.0790  -0.1301 -0.0054 26  VAL A N   
203  C CA  . VAL A 26  ? 0.6596 0.6996 0.7619 0.0750  -0.1265 -0.0127 26  VAL A CA  
204  C C   . VAL A 26  ? 0.8090 0.8233 0.9033 0.0804  -0.1363 -0.0075 26  VAL A C   
205  O O   . VAL A 26  ? 0.9759 0.9669 1.0500 0.0871  -0.1417 0.0049  26  VAL A O   
206  C CB  . VAL A 26  ? 0.6633 0.6797 0.7586 0.0721  -0.1164 -0.0112 26  VAL A CB  
207  C CG1 . VAL A 26  ? 0.7108 0.6989 0.8087 0.0702  -0.1159 -0.0146 26  VAL A CG1 
208  C CG2 . VAL A 26  ? 0.6288 0.6736 0.7392 0.0648  -0.1062 -0.0204 26  VAL A CG2 
209  N N   . GLU A 27  ? 0.9213 0.9398 1.0319 0.0775  -0.1385 -0.0172 27  GLU A N   
210  C CA  . GLU A 27  ? 1.0593 1.0703 1.1692 0.0823  -0.1494 -0.0152 27  GLU A CA  
211  C C   . GLU A 27  ? 1.0743 1.0471 1.1596 0.0893  -0.1543 -0.0004 27  GLU A C   
212  O O   . GLU A 27  ? 1.2857 1.2573 1.3564 0.0954  -0.1611 0.0097  27  GLU A O   
213  C CB  . GLU A 27  ? 1.0395 1.0405 1.1648 0.0789  -0.1493 -0.0248 27  GLU A CB  
214  C CG  . GLU A 27  ? 1.0922 1.1208 1.2425 0.0706  -0.1424 -0.0410 27  GLU A CG  
215  C CD  . GLU A 27  ? 1.1106 1.1824 1.2744 0.0677  -0.1433 -0.0484 27  GLU A CD  
216  O OE1 . GLU A 27  ? 1.1821 1.2662 1.3361 0.0716  -0.1486 -0.0411 27  GLU A OE1 
217  N N   . LYS A 28  ? 1.1059 1.0471 1.1872 0.0879  -0.1506 0.0004  28  LYS A N   
218  C CA  . LYS A 28  ? 0.9227 0.8339 0.9845 0.0889  -0.1457 0.0099  28  LYS A CA  
219  C C   . LYS A 28  ? 0.8781 0.7757 0.9487 0.0824  -0.1371 0.0023  28  LYS A C   
220  O O   . LYS A 28  ? 0.8883 0.7506 0.9454 0.0826  -0.1355 0.0085  28  LYS A O   
221  C CB  . LYS A 28  ? 1.0358 0.9131 1.0750 0.0964  -0.1546 0.0240  28  LYS A CB  
222  C CG  . LYS A 28  ? 1.1805 1.0606 1.2259 0.1002  -0.1658 0.0232  28  LYS A CG  
223  C CD  . LYS A 28  ? 1.2079 1.0533 1.2326 0.1071  -0.1750 0.0366  28  LYS A CD  
224  C CE  . LYS A 28  ? 1.4124 1.2677 1.4452 0.1109  -0.1860 0.0350  28  LYS A CE  
225  N NZ  . LYS A 28  ? 1.5689 1.3927 1.5821 0.1179  -0.1960 0.0483  28  LYS A NZ  
226  N N   . GLN A 29  ? 0.7965 0.7225 0.8902 0.0761  -0.1319 -0.0115 29  GLN A N   
227  C CA  . GLN A 29  ? 0.8539 0.7753 0.9604 0.0689  -0.1236 -0.0213 29  GLN A CA  
228  C C   . GLN A 29  ? 0.7729 0.7343 0.8977 0.0626  -0.1157 -0.0326 29  GLN A C   
229  O O   . GLN A 29  ? 0.7861 0.7786 0.9236 0.0624  -0.1194 -0.0385 29  GLN A O   
230  C CB  . GLN A 29  ? 0.6585 0.5683 0.7776 0.0683  -0.1289 -0.0278 29  GLN A CB  
231  C CG  . GLN A 29  ? 0.6567 0.5751 0.7966 0.0604  -0.1214 -0.0417 29  GLN A CG  
232  C CD  . GLN A 29  ? 0.8815 0.7643 1.0212 0.0597  -0.1232 -0.0419 29  GLN A CD  
233  O OE1 . GLN A 29  ? 0.8225 0.6814 0.9539 0.0650  -0.1323 -0.0349 29  GLN A OE1 
234  N NE2 . GLN A 29  ? 0.9628 0.8420 1.1121 0.0529  -0.1148 -0.0498 29  GLN A NE2 
235  N N   . LEU A 30  ? 0.7465 0.7070 0.8726 0.0571  -0.1052 -0.0357 30  LEU A N   
236  C CA  . LEU A 30  ? 0.7056 0.7025 0.8485 0.0507  -0.0973 -0.0460 30  LEU A CA  
237  C C   . LEU A 30  ? 0.6890 0.6992 0.8554 0.0442  -0.0946 -0.0607 30  LEU A C   
238  O O   . LEU A 30  ? 0.7919 0.7777 0.9604 0.0421  -0.0933 -0.0634 30  LEU A O   
239  C CB  . LEU A 30  ? 0.5089 0.5006 0.6438 0.0475  -0.0869 -0.0431 30  LEU A CB  
240  C CG  . LEU A 30  ? 0.6204 0.6486 0.7724 0.0406  -0.0784 -0.0532 30  LEU A CG  
241  C CD1 . LEU A 30  ? 0.5322 0.5953 0.6893 0.0427  -0.0831 -0.0533 30  LEU A CD1 
242  C CD2 . LEU A 30  ? 0.5891 0.6091 0.7323 0.0380  -0.0683 -0.0497 30  LEU A CD2 
243  N N   . ASP A 31  ? 0.6612 0.7099 0.8448 0.0405  -0.0938 -0.0701 31  ASP A N   
244  C CA  . ASP A 31  ? 0.6948 0.7620 0.9016 0.0332  -0.0896 -0.0851 31  ASP A CA  
245  C C   . ASP A 31  ? 0.6952 0.7852 0.9097 0.0263  -0.0789 -0.0909 31  ASP A C   
246  O O   . ASP A 31  ? 0.7024 0.8271 0.9257 0.0238  -0.0782 -0.0949 31  ASP A O   
247  C CB  . ASP A 31  ? 0.7165 0.8105 0.9377 0.0334  -0.0965 -0.0923 31  ASP A CB  
248  C CG  . ASP A 31  ? 0.8295 0.9467 1.0749 0.0251  -0.0913 -0.1085 31  ASP A CG  
249  O OD1 . ASP A 31  ? 0.7202 0.8276 0.9714 0.0200  -0.0835 -0.1138 31  ASP A OD1 
250  O OD2 . ASP A 31  ? 0.8505 0.9958 1.1090 0.0234  -0.0949 -0.1159 31  ASP A OD2 
251  N N   . LEU A 32  ? 0.8203 0.6789 0.9205 0.0659  -0.0714 -0.0595 32  LEU A N   
252  C CA  . LEU A 32  ? 0.8355 0.6961 0.9424 0.0585  -0.0797 -0.0650 32  LEU A CA  
253  C C   . LEU A 32  ? 0.7445 0.6354 0.8458 0.0725  -0.0896 -0.0889 32  LEU A C   
254  O O   . LEU A 32  ? 0.9200 0.8310 1.0196 0.0713  -0.0910 -0.0896 32  LEU A O   
255  C CB  . LEU A 32  ? 0.8851 0.7040 1.0099 0.0444  -0.0909 -0.0703 32  LEU A CB  
256  C CG  . LEU A 32  ? 0.8902 0.6944 1.0245 0.0265  -0.0899 -0.0555 32  LEU A CG  
257  C CD1 . LEU A 32  ? 0.8244 0.6331 0.9527 0.0195  -0.0726 -0.0257 32  LEU A CD1 
258  C CD2 . LEU A 32  ? 0.8912 0.6519 1.0428 0.0136  -0.1001 -0.0607 32  LEU A CD2 
259  N N   . ALA A 33  ? 0.7129 0.6086 0.8113 0.0862  -0.0965 -0.1089 33  ALA A N   
260  C CA  . ALA A 33  ? 0.8177 0.7408 0.9120 0.0997  -0.1071 -0.1338 33  ALA A CA  
261  C C   . ALA A 33  ? 0.7156 0.6835 0.7945 0.1091  -0.0978 -0.1267 33  ALA A C   
262  O O   . ALA A 33  ? 0.7211 0.7121 0.7985 0.1140  -0.1049 -0.1398 33  ALA A O   
263  C CB  . ALA A 33  ? 0.9300 0.8514 1.0224 0.1135  -0.1142 -0.1541 33  ALA A CB  
264  N N   . ALA A 34  ? 0.7408 0.7216 0.8079 0.1119  -0.0818 -0.1063 34  ALA A N   
265  C CA  . ALA A 34  ? 0.7539 0.7767 0.8048 0.1222  -0.0715 -0.0985 34  ALA A CA  
266  C C   . ALA A 34  ? 0.8116 0.8401 0.8607 0.1114  -0.0618 -0.0757 34  ALA A C   
267  O O   . ALA A 34  ? 0.8908 0.9502 0.9259 0.1182  -0.0501 -0.0634 34  ALA A O   
268  C CB  . ALA A 34  ? 0.8150 0.8508 0.8534 0.1320  -0.0589 -0.0895 34  ALA A CB  
269  N N   . LEU A 35  ? 0.6413 0.6411 0.7040 0.0950  -0.0662 -0.0697 35  LEU A N   
270  C CA  . LEU A 35  ? 0.5382 0.5384 0.6004 0.0831  -0.0566 -0.0464 35  LEU A CA  
271  C C   . LEU A 35  ? 0.6418 0.6523 0.7089 0.0796  -0.0663 -0.0560 35  LEU A C   
272  O O   . LEU A 35  ? 0.6264 0.6188 0.7065 0.0748  -0.0810 -0.0742 35  LEU A O   
273  C CB  . LEU A 35  ? 0.6079 0.5684 0.6817 0.0658  -0.0523 -0.0288 35  LEU A CB  
274  C CG  . LEU A 35  ? 0.5414 0.4999 0.6161 0.0525  -0.0433 -0.0052 35  LEU A CG  
275  C CD1 . LEU A 35  ? 0.5215 0.5092 0.5796 0.0591  -0.0263 0.0145  35  LEU A CD1 
276  C CD2 . LEU A 35  ? 0.5588 0.4766 0.6469 0.0351  -0.0416 0.0090  35  LEU A CD2 
277  N N   . ILE A 36  ? 0.5288 0.5685 0.5852 0.0824  -0.0579 -0.0438 36  ILE A N   
278  C CA  . ILE A 36  ? 0.4775 0.5257 0.5382 0.0762  -0.0635 -0.0456 36  ILE A CA  
279  C C   . ILE A 36  ? 0.4774 0.5262 0.5337 0.0665  -0.0491 -0.0164 36  ILE A C   
280  O O   . ILE A 36  ? 0.5061 0.5757 0.5479 0.0736  -0.0350 -0.0004 36  ILE A O   
281  C CB  . ILE A 36  ? 0.5872 0.6763 0.6382 0.0918  -0.0693 -0.0634 36  ILE A CB  
282  C CG1 . ILE A 36  ? 0.5971 0.6867 0.6526 0.1021  -0.0836 -0.0933 36  ILE A CG1 
283  C CG2 . ILE A 36  ? 0.6744 0.7721 0.7300 0.0848  -0.0745 -0.0643 36  ILE A CG2 
284  C CD1 . ILE A 36  ? 0.5906 0.7217 0.6368 0.1184  -0.0896 -0.1121 36  ILE A CD1 
285  N N   . VAL A 37  ? 0.4894 0.5157 0.5580 0.0503  -0.0527 -0.0096 37  VAL A N   
286  C CA  . VAL A 37  ? 0.4360 0.4618 0.5021 0.0400  -0.0408 0.0167  37  VAL A CA  
287  C C   . VAL A 37  ? 0.5364 0.5760 0.6057 0.0362  -0.0481 0.0112  37  VAL A C   
288  O O   . VAL A 37  ? 0.5513 0.5753 0.6344 0.0289  -0.0620 -0.0052 37  VAL A O   
289  C CB  . VAL A 37  ? 0.5407 0.5261 0.6189 0.0228  -0.0368 0.0331  37  VAL A CB  
290  C CG1 . VAL A 37  ? 0.4925 0.4774 0.5699 0.0115  -0.0268 0.0577  37  VAL A CG1 
291  C CG2 . VAL A 37  ? 0.4680 0.4431 0.5416 0.0270  -0.0276 0.0410  37  VAL A CG2 
292  N N   . TYR A 38  ? 0.4783 0.5463 0.5350 0.0408  -0.0384 0.0251  38  TYR A N   
293  C CA  . TYR A 38  ? 0.4287 0.5148 0.4864 0.0393  -0.0446 0.0197  38  TYR A CA  
294  C C   . TYR A 38  ? 0.4487 0.5390 0.5008 0.0318  -0.0317 0.0470  38  TYR A C   
295  O O   . TYR A 38  ? 0.4652 0.5736 0.5023 0.0396  -0.0175 0.0638  38  TYR A O   
296  C CB  . TYR A 38  ? 0.5043 0.6312 0.5502 0.0579  -0.0492 0.0016  38  TYR A CB  
297  C CG  . TYR A 38  ? 0.4322 0.5790 0.4797 0.0570  -0.0566 -0.0062 38  TYR A CG  
298  C CD1 . TYR A 38  ? 0.5727 0.7104 0.6348 0.0516  -0.0733 -0.0294 38  TYR A CD1 
299  C CD2 . TYR A 38  ? 0.4767 0.6509 0.5114 0.0612  -0.0468 0.0098  38  TYR A CD2 
300  C CE1 . TYR A 38  ? 0.7264 0.8831 0.7905 0.0504  -0.0801 -0.0371 38  TYR A CE1 
301  C CE2 . TYR A 38  ? 0.5126 0.7059 0.5485 0.0607  -0.0536 0.0025  38  TYR A CE2 
302  C CZ  . TYR A 38  ? 0.6035 0.7884 0.6544 0.0551  -0.0702 -0.0211 38  TYR A CZ  
303  O OH  . TYR A 38  ? 0.5986 0.8037 0.6510 0.0544  -0.0769 -0.0289 38  TYR A OH  
304  N N   . TRP A 39  ? 0.4498 0.5239 0.5138 0.0168  -0.0365 0.0510  39  TRP A N   
305  C CA  . TRP A 39  ? 0.4379 0.5153 0.4981 0.0089  -0.0262 0.0749  39  TRP A CA  
306  C C   . TRP A 39  ? 0.4816 0.5850 0.5402 0.0113  -0.0331 0.0663  39  TRP A C   
307  O O   . TRP A 39  ? 0.4905 0.5872 0.5618 0.0058  -0.0476 0.0469  39  TRP A O   
308  C CB  . TRP A 39  ? 0.4321 0.4706 0.5075 -0.0112 -0.0255 0.0885  39  TRP A CB  
309  C CG  . TRP A 39  ? 0.4935 0.5089 0.5688 -0.0154 -0.0144 0.1056  39  TRP A CG  
310  C CD1 . TRP A 39  ? 0.5182 0.5052 0.6030 -0.0194 -0.0185 0.0987  39  TRP A CD1 
311  C CD2 . TRP A 39  ? 0.4556 0.4735 0.5214 -0.0169 0.0029  0.1329  39  TRP A CD2 
312  N NE1 . TRP A 39  ? 0.5349 0.5082 0.6165 -0.0227 -0.0050 0.1195  39  TRP A NE1 
313  C CE2 . TRP A 39  ? 0.5292 0.5208 0.5995 -0.0217 0.0084  0.1407  39  TRP A CE2 
314  C CE3 . TRP A 39  ? 0.4936 0.5335 0.5473 -0.0144 0.0142  0.1514  39  TRP A CE3 
315  C CZ2 . TRP A 39  ? 0.5188 0.5060 0.5826 -0.0244 0.0248  0.1655  39  TRP A CZ2 
316  C CZ3 . TRP A 39  ? 0.5159 0.5501 0.5629 -0.0170 0.0306  0.1764  39  TRP A CZ3 
317  C CH2 . TRP A 39  ? 0.5321 0.5405 0.5845 -0.0222 0.0358  0.1830  39  TRP A CH2 
318  N N   . GLU A 40  ? 0.4285 0.5604 0.4719 0.0189  -0.0223 0.0813  40  GLU A N   
319  C CA  . GLU A 40  ? 0.4376 0.5961 0.4778 0.0216  -0.0271 0.0761  40  GLU A CA  
320  C C   . GLU A 40  ? 0.4136 0.5794 0.4448 0.0179  -0.0133 0.1036  40  GLU A C   
321  O O   . GLU A 40  ? 0.5016 0.6620 0.5244 0.0186  0.0011  0.1248  40  GLU A O   
322  C CB  . GLU A 40  ? 0.4205 0.6182 0.4482 0.0415  -0.0313 0.0577  40  GLU A CB  
323  C CG  . GLU A 40  ? 0.6346 0.8571 0.6419 0.0572  -0.0167 0.0711  40  GLU A CG  
324  C CD  . GLU A 40  ? 0.5284 0.7786 0.5212 0.0626  -0.0066 0.0883  40  GLU A CD  
325  O OE1 . GLU A 40  ? 0.6776 0.9344 0.6753 0.0571  -0.0129 0.0854  40  GLU A OE1 
326  O OE2 . GLU A 40  ? 0.6666 0.9321 0.6432 0.0724  0.0076  0.1046  40  GLU A OE2 
327  N N   . MET A 41  ? 0.4436 0.6208 0.4775 0.0133  -0.0181 0.1028  41  MET A N   
328  C CA  . MET A 41  ? 0.4648 0.6546 0.4885 0.0124  -0.0062 0.1265  41  MET A CA  
329  C C   . MET A 41  ? 0.5810 0.8073 0.5975 0.0220  -0.0121 0.1155  41  MET A C   
330  O O   . MET A 41  ? 0.4038 0.6317 0.4317 0.0180  -0.0267 0.0949  41  MET A O   
331  C CB  . MET A 41  ? 0.4348 0.5927 0.4715 -0.0078 -0.0039 0.1433  41  MET A CB  
332  C CG  . MET A 41  ? 0.6751 0.8327 0.7232 -0.0185 -0.0148 0.1356  41  MET A CG  
333  S SD  . MET A 41  ? 0.7440 0.9262 0.7805 -0.0174 -0.0056 0.1560  41  MET A SD  
334  C CE  . MET A 41  ? 0.6653 0.8156 0.7042 -0.0316 0.0094  0.1883  41  MET A CE  
335  N N   . GLU A 42  ? 0.5825 0.8381 0.5801 0.0348  -0.0006 0.1294  42  GLU A N   
336  C CA  . GLU A 42  ? 0.7047 1.0002 0.6923 0.0485  -0.0054 0.1175  42  GLU A CA  
337  C C   . GLU A 42  ? 0.7694 1.0776 0.7582 0.0598  -0.0166 0.0896  42  GLU A C   
338  O O   . GLU A 42  ? 0.8829 1.1983 0.8613 0.0713  -0.0099 0.0909  42  GLU A O   
339  C CB  . GLU A 42  ? 0.7108 1.0075 0.7072 0.0378  -0.0127 0.1163  42  GLU A CB  
340  C CG  . GLU A 42  ? 0.7012 0.9960 0.6885 0.0337  0.0024  0.1470  42  GLU A CG  
341  C CD  . GLU A 42  ? 0.8875 1.1687 0.8865 0.0173  -0.0012 0.1542  42  GLU A CD  
342  O OE1 . GLU A 42  ? 0.7359 1.0119 0.7498 0.0088  -0.0157 0.1353  42  GLU A OE1 
343  O OE2 . GLU A 42  ? 0.8230 1.0983 0.8162 0.0127  0.0110  0.1793  42  GLU A OE2 
344  N N   . ASP A 43  ? 0.6721 0.9844 0.6728 0.0576  -0.0329 0.0643  43  ASP A N   
345  C CA  . ASP A 43  ? 0.8214 1.1367 0.8260 0.0658  -0.0431 0.0388  43  ASP A CA  
346  C C   . ASP A 43  ? 0.7530 1.0420 0.7798 0.0516  -0.0592 0.0182  43  ASP A C   
347  O O   . ASP A 43  ? 0.8324 1.1336 0.8647 0.0572  -0.0725 -0.0086 43  ASP A O   
348  C CB  . ASP A 43  ? 0.5439 0.9047 0.5343 0.0864  -0.0458 0.0241  43  ASP A CB  
349  C CG  . ASP A 43  ? 0.6247 1.0059 0.5938 0.1020  -0.0304 0.0405  43  ASP A CG  
350  O OD1 . ASP A 43  ? 0.5795 0.9540 0.5462 0.1078  -0.0281 0.0368  43  ASP A OD1 
351  O OD2 . ASP A 43  ? 0.5965 1.0003 0.5514 0.1084  -0.0205 0.0572  43  ASP A OD2 
352  N N   . LYS A 44  ? 0.5899 0.8411 0.6295 0.0330  -0.0576 0.0309  44  LYS A N   
353  C CA  . LYS A 44  ? 0.5683 0.7894 0.6294 0.0175  -0.0712 0.0152  44  LYS A CA  
354  C C   . LYS A 44  ? 0.5603 0.7490 0.6284 0.0139  -0.0715 0.0130  44  LYS A C   
355  O O   . LYS A 44  ? 0.5008 0.6743 0.5635 0.0120  -0.0590 0.0341  44  LYS A O   
356  C CB  . LYS A 44  ? 0.5166 0.7170 0.5881 -0.0013 -0.0700 0.0305  44  LYS A CB  
357  C CG  . LYS A 44  ? 0.5794 0.8089 0.6414 0.0017  -0.0654 0.0410  44  LYS A CG  
358  C CD  . LYS A 44  ? 0.5479 0.7537 0.6163 -0.0156 -0.0587 0.0645  44  LYS A CD  
359  C CE  . LYS A 44  ? 0.6778 0.8872 0.7576 -0.0266 -0.0688 0.0560  44  LYS A CE  
360  N NZ  . LYS A 44  ? 0.8117 1.0627 0.8781 -0.0148 -0.0670 0.0561  44  LYS A NZ  
361  N N   . ASN A 45  ? 0.4562 0.6348 0.5363 0.0131  -0.0856 -0.0128 45  ASN A N   
362  C CA  . ASN A 45  ? 0.4774 0.6234 0.5658 0.0091  -0.0877 -0.0172 45  ASN A CA  
363  C C   . ASN A 45  ? 0.4896 0.5940 0.5924 -0.0117 -0.0860 -0.0021 45  ASN A C   
364  O O   . ASN A 45  ? 0.4915 0.5801 0.6096 -0.0251 -0.0962 -0.0111 45  ASN A O   
365  C CB  . ASN A 45  ? 0.5443 0.6909 0.6423 0.0134  -0.1041 -0.0496 45  ASN A CB  
366  C CG  . ASN A 45  ? 0.7272 0.8454 0.8310 0.0134  -0.1065 -0.0567 45  ASN A CG  
367  O OD1 . ASN A 45  ? 0.6598 0.7417 0.7724 0.0003  -0.1033 -0.0440 45  ASN A OD1 
368  N ND2 . ASN A 45  ? 0.8062 0.9415 0.9052 0.0286  -0.1125 -0.0774 45  ASN A ND2 
369  N N   . ILE A 46  ? 0.4222 0.5093 0.5202 -0.0146 -0.0731 0.0207  46  ILE A N   
370  C CA  . ILE A 46  ? 0.3945 0.4411 0.5061 -0.0333 -0.0712 0.0347  46  ILE A CA  
371  C C   . ILE A 46  ? 0.5466 0.5624 0.6684 -0.0360 -0.0775 0.0230  46  ILE A C   
372  O O   . ILE A 46  ? 0.5565 0.5414 0.6951 -0.0503 -0.0862 0.0169  46  ILE A O   
373  C CB  . ILE A 46  ? 0.4439 0.4869 0.5462 -0.0364 -0.0538 0.0663  46  ILE A CB  
374  C CG1 . ILE A 46  ? 0.4934 0.5660 0.5852 -0.0334 -0.0474 0.0787  46  ILE A CG1 
375  C CG2 . ILE A 46  ? 0.4543 0.4562 0.5713 -0.0555 -0.0524 0.0800  46  ILE A CG2 
376  C CD1 . ILE A 46  ? 0.4802 0.5561 0.5593 -0.0318 -0.0294 0.1077  46  ILE A CD1 
377  N N   . ILE A 47  ? 0.5116 0.5356 0.6234 -0.0221 -0.0734 0.0195  47  ILE A N   
378  C CA  . ILE A 47  ? 0.4655 0.4612 0.5860 -0.0234 -0.0792 0.0083  47  ILE A CA  
379  C C   . ILE A 47  ? 0.4926 0.5114 0.6023 -0.0042 -0.0812 -0.0085 47  ILE A C   
380  O O   . ILE A 47  ? 0.6567 0.7044 0.7498 0.0090  -0.0710 0.0001  47  ILE A O   
381  C CB  . ILE A 47  ? 0.5970 0.5624 0.7197 -0.0327 -0.0681 0.0313  47  ILE A CB  
382  C CG1 . ILE A 47  ? 0.6013 0.5391 0.7381 -0.0530 -0.0689 0.0441  47  ILE A CG1 
383  C CG2 . ILE A 47  ? 0.6265 0.5696 0.7538 -0.0293 -0.0721 0.0203  47  ILE A CG2 
384  C CD1 . ILE A 47  ? 0.8812 0.7804 1.0270 -0.0641 -0.0649 0.0565  47  ILE A CD1 
385  N N   . GLN A 48  ? 0.4527 0.4575 0.5721 -0.0028 -0.0942 -0.0322 48  GLN A N   
386  C CA  . GLN A 48  ? 0.5980 0.6197 0.7101 0.0144  -0.0984 -0.0513 48  GLN A CA  
387  C C   . GLN A 48  ? 0.6512 0.6362 0.7742 0.0098  -0.1042 -0.0596 48  GLN A C   
388  O O   . GLN A 48  ? 0.7217 0.6846 0.8597 0.0017  -0.1173 -0.0763 48  GLN A O   
389  C CB  . GLN A 48  ? 0.5237 0.5720 0.6367 0.0227  -0.1114 -0.0774 48  GLN A CB  
390  C CG  . GLN A 48  ? 0.6940 0.7663 0.7982 0.0418  -0.1158 -0.0978 48  GLN A CG  
391  C CD  . GLN A 48  ? 0.9035 1.0057 1.0082 0.0495  -0.1275 -0.1215 48  GLN A CD  
392  O OE1 . GLN A 48  ? 0.7095 0.8220 0.8169 0.0429  -0.1291 -0.1189 48  GLN A OE1 
393  N NE2 . GLN A 48  ? 0.8078 0.9207 0.9121 0.0622  -0.1369 -0.1464 48  GLN A NE2 
394  N N   . PHE A 49  ? 0.5626 0.5416 0.6780 0.0153  -0.0943 -0.0482 49  PHE A N   
395  C CA  . PHE A 49  ? 0.5173 0.4628 0.6411 0.0122  -0.0978 -0.0531 49  PHE A CA  
396  C C   . PHE A 49  ? 0.5422 0.5064 0.6562 0.0309  -0.0996 -0.0693 49  PHE A C   
397  O O   . PHE A 49  ? 0.5632 0.5488 0.6623 0.0415  -0.0877 -0.0579 49  PHE A O   
398  C CB  . PHE A 49  ? 0.6845 0.6063 0.8087 0.0019  -0.0846 -0.0256 49  PHE A CB  
399  C CG  . PHE A 49  ? 0.7041 0.5915 0.8363 -0.0014 -0.0869 -0.0282 49  PHE A CG  
400  C CD1 . PHE A 49  ? 0.7332 0.6268 0.8562 0.0114  -0.0820 -0.0305 49  PHE A CD1 
401  C CD2 . PHE A 49  ? 0.7821 0.6311 0.9311 -0.0173 -0.0939 -0.0283 49  PHE A CD2 
402  C CE1 . PHE A 49  ? 0.8625 0.7249 0.9926 0.0089  -0.0842 -0.0329 49  PHE A CE1 
403  C CE2 . PHE A 49  ? 0.8558 0.6729 1.0118 -0.0198 -0.0960 -0.0303 49  PHE A CE2 
404  C CZ  . PHE A 49  ? 0.6415 0.4655 0.7880 -0.0065 -0.0912 -0.0327 49  PHE A CZ  
405  N N   . VAL A 50  ? 0.5723 0.5287 0.6946 0.0348  -0.1144 -0.0960 50  VAL A N   
406  C CA  . VAL A 50  ? 0.8019 0.7750 0.9168 0.0523  -0.1187 -0.1151 50  VAL A CA  
407  C C   . VAL A 50  ? 0.8238 0.7611 0.9519 0.0487  -0.1299 -0.1312 50  VAL A C   
408  O O   . VAL A 50  ? 0.7988 0.7062 0.9422 0.0346  -0.1384 -0.1354 50  VAL A O   
409  C CB  . VAL A 50  ? 0.7967 0.8078 0.9062 0.0648  -0.1270 -0.1362 50  VAL A CB  
410  C CG1 . VAL A 50  ? 0.8111 0.8626 0.9026 0.0751  -0.1144 -0.1217 50  VAL A CG1 
411  C CG2 . VAL A 50  ? 0.7701 0.7729 0.8934 0.0533  -0.1387 -0.1475 50  VAL A CG2 
412  N N   . HIS A 51  ? 0.9485 0.8885 1.0703 0.0616  -0.1298 -0.1400 51  HIS A N   
413  C CA  . HIS A 51  ? 1.0760 0.9825 1.2087 0.0600  -0.1396 -0.1545 51  HIS A CA  
414  C C   . HIS A 51  ? 0.9993 0.8625 1.1441 0.0417  -0.1369 -0.1377 51  HIS A C   
415  O O   . HIS A 51  ? 1.0607 0.8909 1.2193 0.0342  -0.1476 -0.1494 51  HIS A O   
416  C CB  . HIS A 51  ? 1.2073 1.1134 1.3495 0.0630  -0.1573 -0.1851 51  HIS A CB  
417  C CG  . HIS A 51  ? 1.2413 1.1921 1.3732 0.0789  -0.1607 -0.2015 51  HIS A CG  
418  N ND1 . HIS A 51  ? 1.1902 1.1564 1.3273 0.0770  -0.1700 -0.2158 51  HIS A ND1 
419  C CD2 . HIS A 51  ? 1.2349 1.2192 1.3516 0.0970  -0.1560 -0.2058 51  HIS A CD2 
420  C CE1 . HIS A 51  ? 1.3268 1.3343 1.4524 0.0936  -0.1709 -0.2282 51  HIS A CE1 
421  N NE2 . HIS A 51  ? 1.2360 1.2550 1.3490 0.1059  -0.1625 -0.2223 51  HIS A NE2 
422  N N   . GLY A 52  ? 0.7845 0.6474 0.9242 0.0345  -0.1224 -0.1099 52  GLY A N   
423  C CA  . GLY A 52  ? 1.0206 0.8448 1.1715 0.0173  -0.1192 -0.0928 52  GLY A CA  
424  C C   . GLY A 52  ? 0.9153 0.7179 1.0818 0.0017  -0.1291 -0.0975 52  GLY A C   
425  O O   . GLY A 52  ? 0.9615 0.7261 1.1404 -0.0108 -0.1323 -0.0936 52  GLY A O   
426  N N   . GLU A 53  ? 0.9433 0.7697 1.1090 0.0016  -0.1332 -0.1045 53  GLU A N   
427  C CA  . GLU A 53  ? 1.1722 0.9826 1.3527 -0.0117 -0.1441 -0.1134 53  GLU A CA  
428  C C   . GLU A 53  ? 1.1198 0.9541 1.2950 -0.0171 -0.1361 -0.0967 53  GLU A C   
429  O O   . GLU A 53  ? 1.0540 0.9257 1.2148 -0.0044 -0.1298 -0.0949 53  GLU A O   
430  C CB  . GLU A 53  ? 1.1739 1.0014 1.3563 -0.0011 -0.1589 -0.1457 53  GLU A CB  
431  C CG  . GLU A 53  ? 1.2876 1.0953 1.4872 -0.0124 -0.1741 -0.1644 53  GLU A CG  
432  C CD  . GLU A 53  ? 1.4386 1.2011 1.6516 -0.0200 -0.1817 -0.1717 53  GLU A CD  
433  O OE1 . GLU A 53  ? 1.4913 1.2183 1.7172 -0.0272 -0.1910 -0.1823 53  GLU A OE1 
434  O OE2 . GLU A 53  ? 1.4959 1.2749 1.7103 -0.0130 -0.1920 -0.1950 53  GLU A OE2 
435  N N   . GLU A 54  ? 1.0721 0.8875 1.2576 -0.0347 -0.1355 -0.0840 54  GLU A N   
436  C CA  . GLU A 54  ? 0.9634 0.8057 1.1448 -0.0377 -0.1321 -0.0761 54  GLU A CA  
437  C C   . GLU A 54  ? 1.0153 0.8735 1.2020 -0.0348 -0.1461 -0.1023 54  GLU A C   
438  O O   . GLU A 54  ? 1.1906 1.0250 1.3914 -0.0414 -0.1588 -0.1202 54  GLU A O   
439  C CB  . GLU A 54  ? 0.9196 0.7425 1.1086 -0.0563 -0.1261 -0.0533 54  GLU A CB  
440  C CG  . GLU A 54  ? 0.8706 0.7041 1.0477 -0.0560 -0.1084 -0.0238 54  GLU A CG  
441  C CD  . GLU A 54  ? 1.1753 0.9922 1.3603 -0.0742 -0.1035 -0.0028 54  GLU A CD  
442  O OE1 . GLU A 54  ? 1.0951 0.8839 1.2854 -0.0840 -0.0972 0.0141  54  GLU A OE1 
443  O OE2 . GLU A 54  ? 1.1828 1.0176 1.3685 -0.0780 -0.1059 -0.0037 54  GLU A OE2 
444  N N   . ASP A 55  ? 1.0082 0.9075 1.1833 -0.0239 -0.1438 -0.1053 55  ASP A N   
445  C CA  . ASP A 55  ? 1.0296 0.9503 1.2084 -0.0199 -0.1562 -0.1298 55  ASP A CA  
446  C C   . ASP A 55  ? 1.1455 1.0756 1.3275 -0.0315 -0.1546 -0.1194 55  ASP A C   
447  O O   . ASP A 55  ? 1.0624 1.0221 1.2318 -0.0260 -0.1449 -0.1050 55  ASP A O   
448  C CB  . ASP A 55  ? 1.1374 1.0996 1.3009 0.0014  -0.1557 -0.1424 55  ASP A CB  
449  C CG  . ASP A 55  ? 1.3560 1.3368 1.5249 0.0070  -0.1704 -0.1722 55  ASP A CG  
450  O OD1 . ASP A 55  ? 1.3418 1.3246 1.5193 -0.0033 -0.1758 -0.1758 55  ASP A OD1 
451  O OD2 . ASP A 55  ? 1.2425 1.2371 1.4070 0.0218  -0.1764 -0.1923 55  ASP A OD2 
452  N N   . LEU A 56  ? 1.1042 1.0093 1.3033 -0.0473 -0.1643 -0.1270 56  LEU A N   
453  C CA  . LEU A 56  ? 1.1036 1.0090 1.3083 -0.0618 -0.1622 -0.1141 56  LEU A CA  
454  C C   . LEU A 56  ? 1.0996 1.0344 1.3063 -0.0600 -0.1712 -0.1321 56  LEU A C   
455  O O   . LEU A 56  ? 0.9877 0.9325 1.1951 -0.0686 -0.1679 -0.1206 56  LEU A O   
456  C CB  . LEU A 56  ? 0.8938 0.7534 1.1162 -0.0821 -0.1660 -0.1085 56  LEU A CB  
457  C CG  . LEU A 56  ? 1.0952 0.9462 1.3209 -0.0979 -0.1579 -0.0833 56  LEU A CG  
458  C CD1 . LEU A 56  ? 0.9721 0.8107 1.1898 -0.0982 -0.1433 -0.0560 56  LEU A CD1 
459  C CD2 . LEU A 56  ? 1.1881 1.0049 1.4336 -0.1177 -0.1671 -0.0884 56  LEU A CD2 
460  N N   . LYS A 57  ? 1.2321 1.1815 1.4400 -0.0492 -0.1824 -0.1602 57  LYS A N   
461  C CA  . LYS A 57  ? 1.2309 1.2055 1.4434 -0.0491 -0.1922 -0.1796 57  LYS A CA  
462  C C   . LYS A 57  ? 1.1496 1.1702 1.3459 -0.0379 -0.1843 -0.1706 57  LYS A C   
463  O O   . LYS A 57  ? 0.9294 0.9678 1.1287 -0.0431 -0.1876 -0.1737 57  LYS A O   
464  C CB  . LYS A 57  ? 1.3507 1.3303 1.5681 -0.0392 -0.2058 -0.2122 57  LYS A CB  
465  C CG  . LYS A 57  ? 1.2888 1.2914 1.4905 -0.0180 -0.2018 -0.2166 57  LYS A CG  
466  C CD  . LYS A 57  ? 1.4146 1.3985 1.6234 -0.0125 -0.2124 -0.2402 57  LYS A CD  
467  C CE  . LYS A 57  ? 1.3781 1.3889 1.5710 0.0093  -0.2088 -0.2458 57  LYS A CE  
468  N NZ  . LYS A 57  ? 1.3740 1.3614 1.5726 0.0143  -0.2168 -0.2636 57  LYS A NZ  
469  N N   . VAL A 58  ? 1.0456 1.0855 1.2245 -0.0228 -0.1737 -0.1590 58  VAL A N   
470  C CA  . VAL A 58  ? 1.0414 1.1236 1.2032 -0.0112 -0.1646 -0.1480 58  VAL A CA  
471  C C   . VAL A 58  ? 0.8197 0.8958 0.9763 -0.0205 -0.1508 -0.1159 58  VAL A C   
472  O O   . VAL A 58  ? 0.7447 0.8530 0.8872 -0.0122 -0.1423 -0.1038 58  VAL A O   
473  C CB  . VAL A 58  ? 1.0866 1.1944 1.2318 0.0102  -0.1599 -0.1521 58  VAL A CB  
474  C CG1 . VAL A 58  ? 0.9975 1.1462 1.1235 0.0224  -0.1483 -0.1367 58  VAL A CG1 
475  C CG2 . VAL A 58  ? 1.0326 1.1538 1.1822 0.0207  -0.1741 -0.1855 58  VAL A CG2 
476  N N   . GLN A 59  ? 0.8492 0.8853 1.0169 -0.0372 -0.1484 -0.1017 59  GLN A N   
477  C CA  . GLN A 59  ? 0.6417 0.6721 0.8046 -0.0458 -0.1352 -0.0713 59  GLN A CA  
478  C C   . GLN A 59  ? 0.5760 0.6285 0.7394 -0.0510 -0.1366 -0.0691 59  GLN A C   
479  O O   . GLN A 59  ? 0.5959 0.6435 0.7729 -0.0604 -0.1484 -0.0856 59  GLN A O   
480  C CB  . GLN A 59  ? 0.6418 0.6254 0.8181 -0.0635 -0.1337 -0.0583 59  GLN A CB  
481  C CG  . GLN A 59  ? 0.5448 0.5219 0.7183 -0.0740 -0.1212 -0.0281 59  GLN A CG  
482  C CD  . GLN A 59  ? 0.7917 0.7254 0.9754 -0.0884 -0.1174 -0.0130 59  GLN A CD  
483  O OE1 . GLN A 59  ? 0.8525 0.7574 1.0529 -0.1033 -0.1259 -0.0193 59  GLN A OE1 
484  N NE2 . GLN A 59  ? 0.7405 0.6699 0.9143 -0.0838 -0.1043 0.0070  59  GLN A NE2 
485  N N   . HIS A 60  ? 0.6208 0.6981 0.7692 -0.0447 -0.1243 -0.0489 60  HIS A N   
486  C CA  . HIS A 60  ? 0.5282 0.6319 0.6739 -0.0464 -0.1246 -0.0464 60  HIS A CA  
487  C C   . HIS A 60  ? 0.7011 0.7785 0.8622 -0.0679 -0.1271 -0.0375 60  HIS A C   
488  O O   . HIS A 60  ? 0.6697 0.7126 0.8377 -0.0804 -0.1221 -0.0213 60  HIS A O   
489  C CB  . HIS A 60  ? 0.6187 0.7515 0.7442 -0.0346 -0.1098 -0.0245 60  HIS A CB  
490  C CG  . HIS A 60  ? 0.6451 0.8091 0.7655 -0.0332 -0.1100 -0.0228 60  HIS A CG  
491  N ND1 . HIS A 60  ? 0.6178 0.7715 0.7447 -0.0483 -0.1076 -0.0077 60  HIS A ND1 
492  C CD2 . HIS A 60  ? 0.5977 0.8036 0.7074 -0.0183 -0.1127 -0.0350 60  HIS A CD2 
493  C CE1 . HIS A 60  ? 0.7666 0.9544 0.8866 -0.0425 -0.1086 -0.0104 60  HIS A CE1 
494  N NE2 . HIS A 60  ? 0.6307 0.8507 0.7402 -0.0243 -0.1117 -0.0268 60  HIS A NE2 
495  N N   . SER A 61  ? 0.4961 0.8403 0.7263 -0.1885 0.0257  0.2043  61  SER A N   
496  C CA  . SER A 61  ? 0.6007 0.9427 0.8157 -0.1892 0.0352  0.2173  61  SER A CA  
497  C C   . SER A 61  ? 0.5108 0.8511 0.7163 -0.1838 0.0424  0.2281  61  SER A C   
498  O O   . SER A 61  ? 0.5956 0.9220 0.7828 -0.1849 0.0451  0.2371  61  SER A O   
499  C CB  . SER A 61  ? 0.6579 1.0085 0.8727 -0.1851 0.0434  0.2159  61  SER A CB  
500  O OG  . SER A 61  ? 0.7387 1.0855 0.9391 -0.1871 0.0505  0.2258  61  SER A OG  
501  N N   . SER A 62  ? 0.4910 0.8400 0.7047 -0.1755 0.0450  0.2251  62  SER A N   
502  C CA  . SER A 62  ? 0.6545 1.0018 0.8582 -0.1685 0.0536  0.2349  62  SER A CA  
503  C C   . SER A 62  ? 0.6940 1.0050 0.8745 -0.1598 0.0434  0.2255  62  SER A C   
504  O O   . SER A 62  ? 0.6292 0.9246 0.7904 -0.1498 0.0484  0.2282  62  SER A O   
505  C CB  . SER A 62  ? 0.4961 0.8551 0.7110 -0.1588 0.0569  0.2292  62  SER A CB  
506  O OG  . SER A 62  ? 0.6595 1.0189 0.8864 -0.1595 0.0472  0.2212  62  SER A OG  
507  N N   . TYR A 63  ? 0.5590 0.8561 0.7411 -0.1634 0.0293  0.2144  63  TYR A N   
508  C CA  . TYR A 63  ? 0.5273 0.7906 0.6890 -0.1554 0.0187  0.2048  63  TYR A CA  
509  C C   . TYR A 63  ? 0.6828 0.9241 0.8294 -0.1606 0.0110  0.2036  63  TYR A C   
510  O O   . TYR A 63  ? 0.5919 0.8041 0.7208 -0.1547 0.0015  0.1960  63  TYR A O   
511  C CB  . TYR A 63  ? 0.5220 0.7844 0.6969 -0.1528 0.0075  0.1913  63  TYR A CB  
512  C CG  . TYR A 63  ? 0.5801 0.8540 0.7614 -0.1439 0.0136  0.1910  63  TYR A CG  
513  C CD1 . TYR A 63  ? 0.5032 0.7576 0.6640 -0.1315 0.0163  0.1906  63  TYR A CD1 
514  C CD2 . TYR A 63  ? 0.5169 0.8215 0.7248 -0.1483 0.0173  0.1916  63  TYR A CD2 
515  C CE1 . TYR A 63  ? 0.3900 0.6547 0.5565 -0.1234 0.0223  0.1905  63  TYR A CE1 
516  C CE2 . TYR A 63  ? 0.4835 0.7987 0.6975 -0.1403 0.0230  0.1916  63  TYR A CE2 
517  C CZ  . TYR A 63  ? 0.6772 0.9723 0.8704 -0.1277 0.0256  0.1910  63  TYR A CZ  
518  O OH  . TYR A 63  ? 0.4777 0.7830 0.6767 -0.1196 0.0315  0.1910  63  TYR A OH  
519  N N   . ARG A 64  ? 0.5954 0.8495 0.7482 -0.1716 0.0148  0.2108  64  ARG A N   
520  C CA  . ARG A 64  ? 0.6319 0.8658 0.7708 -0.1771 0.0079  0.2100  64  ARG A CA  
521  C C   . ARG A 64  ? 0.5950 0.8050 0.7043 -0.1701 0.0122  0.2159  64  ARG A C   
522  O O   . ARG A 64  ? 0.5565 0.7750 0.6596 -0.1664 0.0248  0.2257  64  ARG A O   
523  C CB  . ARG A 64  ? 0.6680 0.9240 0.8219 -0.1910 0.0119  0.2166  64  ARG A CB  
524  C CG  . ARG A 64  ? 0.7340 0.9735 0.8728 -0.1977 0.0088  0.2195  64  ARG A CG  
525  C CD  . ARG A 64  ? 0.9058 1.1497 1.0310 -0.1987 0.0219  0.2334  64  ARG A CD  
526  N NE  . ARG A 64  ? 0.7830 1.0151 0.8965 -0.2067 0.0194  0.2366  64  ARG A NE  
527  N N   . GLN A 65  ? 0.7209 0.9007 0.8119 -0.1684 0.0015  0.2099  65  GLN A N   
528  C CA  . GLN A 65  ? 0.7254 0.8784 0.7869 -0.1617 0.0032  0.2136  65  GLN A CA  
529  C C   . GLN A 65  ? 0.6896 0.8348 0.7405 -0.1489 0.0076  0.2127  65  GLN A C   
530  O O   . GLN A 65  ? 0.9362 1.0656 0.9646 -0.1433 0.0132  0.2183  65  GLN A O   
531  C CB  . GLN A 65  ? 0.7084 0.8677 0.7606 -0.1674 0.0142  0.2267  65  GLN A CB  
532  C CG  . GLN A 65  ? 0.7785 0.9506 0.8429 -0.1808 0.0126  0.2293  65  GLN A CG  
533  C CD  . GLN A 65  ? 0.8585 1.0035 0.9035 -0.1842 0.0043  0.2278  65  GLN A CD  
534  O OE1 . GLN A 65  ? 0.9352 1.0634 0.9802 -0.1847 -0.0091 0.2177  65  GLN A OE1 
535  N NE2 . GLN A 65  ? 0.9042 1.0446 0.9323 -0.1866 0.0121  0.2378  65  GLN A NE2 
536  N N   . ARG A 66  ? 0.6236 0.7793 0.6901 -0.1444 0.0053  0.2057  66  ARG A N   
537  C CA  . ARG A 66  ? 0.6470 0.7952 0.7039 -0.1322 0.0092  0.2042  66  ARG A CA  
538  C C   . ARG A 66  ? 0.6602 0.7980 0.7215 -0.1262 -0.0024 0.1908  66  ARG A C   
539  O O   . ARG A 66  ? 0.7257 0.8486 0.7729 -0.1157 -0.0017 0.1881  66  ARG A O   
540  C CB  . ARG A 66  ? 0.6261 0.8034 0.6969 -0.1309 0.0239  0.2129  66  ARG A CB  
541  C CG  . ARG A 66  ? 0.8071 0.9889 0.8660 -0.1317 0.0377  0.2265  66  ARG A CG  
542  C CD  . ARG A 66  ? 0.7446 0.9462 0.8108 -0.1256 0.0514  0.2331  66  ARG A CD  
543  N NE  . ARG A 66  ? 0.5553 0.7841 0.6498 -0.1280 0.0512  0.2300  66  ARG A NE  
544  C CZ  . ARG A 66  ? 0.5149 0.7492 0.6167 -0.1200 0.0525  0.2256  66  ARG A CZ  
545  N NH1 . ARG A 66  ? 0.5547 0.7712 0.6383 -0.1089 0.0555  0.2247  66  ARG A NH1 
546  N NH2 . ARG A 66  ? 0.4581 0.7166 0.5860 -0.1236 0.0509  0.2222  66  ARG A NH2 
547  N N   . ALA A 67  ? 0.5831 0.7280 0.6628 -0.1323 -0.0127 0.1823  67  ALA A N   
548  C CA  . ALA A 67  ? 0.4753 0.6127 0.5611 -0.1271 -0.0236 0.1693  67  ALA A CA  
549  C C   . ALA A 67  ? 0.6565 0.7729 0.7381 -0.1310 -0.0390 0.1599  67  ALA A C   
550  O O   . ALA A 67  ? 0.6260 0.7490 0.7168 -0.1412 -0.0419 0.1613  67  ALA A O   
551  C CB  . ALA A 67  ? 0.5219 0.6897 0.6369 -0.1306 -0.0218 0.1665  67  ALA A CB  
552  N N   . ARG A 68  ? 0.5449 0.6365 0.6129 -0.1229 -0.0487 0.1506  68  ARG A N   
553  C CA  . ARG A 68  ? 0.6062 0.6799 0.6737 -0.1259 -0.0642 0.1403  68  ARG A CA  
554  C C   . ARG A 68  ? 0.5797 0.6412 0.6463 -0.1176 -0.0739 0.1279  68  ARG A C   
555  O O   . ARG A 68  ? 0.5389 0.5967 0.5965 -0.1081 -0.0692 0.1279  68  ARG A O   
556  C CB  . ARG A 68  ? 0.6193 0.6650 0.6627 -0.1264 -0.0686 0.1430  68  ARG A CB  
557  C CG  . ARG A 68  ? 0.9033 0.9259 0.9191 -0.1161 -0.0655 0.1457  68  ARG A CG  
558  C CD  . ARG A 68  ? 0.9641 0.9738 0.9602 -0.1190 -0.0608 0.1556  68  ARG A CD  
559  N NE  . ARG A 68  ? 1.1951 1.2295 1.1998 -0.1246 -0.0468 0.1673  68  ARG A NE  
560  C CZ  . ARG A 68  ? 1.0725 1.1179 1.0736 -0.1197 -0.0334 0.1751  68  ARG A CZ  
561  N NH1 . ARG A 68  ? 0.9995 1.0378 0.9928 -0.1093 -0.0316 0.1719  68  ARG A NH1 
562  N NH2 . ARG A 68  ? 0.9940 1.0595 1.0009 -0.1255 -0.0214 0.1863  68  ARG A NH2 
563  N N   . LEU A 69  ? 0.5823 0.6371 0.6580 -0.1214 -0.0874 0.1174  69  LEU A N   
564  C CA  . LEU A 69  ? 0.5040 0.5439 0.5774 -0.1144 -0.0988 0.1047  69  LEU A CA  
565  C C   . LEU A 69  ? 0.5195 0.5246 0.5664 -0.1093 -0.1069 0.1024  69  LEU A C   
566  O O   . LEU A 69  ? 0.6239 0.6175 0.6642 -0.1150 -0.1111 0.1048  69  LEU A O   
567  C CB  . LEU A 69  ? 0.5856 0.6363 0.6831 -0.1215 -0.1094 0.0942  69  LEU A CB  
568  C CG  . LEU A 69  ? 0.6596 0.7044 0.7630 -0.1160 -0.1202 0.0803  69  LEU A CG  
569  C CD1 . LEU A 69  ? 0.5377 0.6004 0.6492 -0.1101 -0.1123 0.0802  69  LEU A CD1 
570  C CD2 . LEU A 69  ? 0.6937 0.7466 0.8191 -0.1249 -0.1309 0.0710  69  LEU A CD2 
571  N N   . LEU A 70  ? 0.5917 0.5803 0.6229 -0.0987 -0.1088 0.0981  70  LEU A N   
572  C CA  . LEU A 70  ? 0.6863 0.6415 0.6922 -0.0935 -0.1172 0.0952  70  LEU A CA  
573  C C   . LEU A 70  ? 0.5833 0.5277 0.5972 -0.0952 -0.1336 0.0822  70  LEU A C   
574  O O   . LEU A 70  ? 0.6752 0.6175 0.6932 -0.0896 -0.1398 0.0724  70  LEU A O   
575  C CB  . LEU A 70  ? 0.7623 0.7046 0.7483 -0.0821 -0.1123 0.0959  70  LEU A CB  
576  C CG  . LEU A 70  ? 0.6599 0.6149 0.6401 -0.0800 -0.0953 0.1083  70  LEU A CG  
577  C CD1 . LEU A 70  ? 0.8069 0.7562 0.7753 -0.0690 -0.0900 0.1068  70  LEU A CD1 
578  C CD2 . LEU A 70  ? 0.8464 0.7886 0.8078 -0.0830 -0.0904 0.1186  70  LEU A CD2 
579  N N   . LYS A 71  ? 0.7111 0.6483 0.7271 -0.1029 -0.1408 0.0820  71  LYS A N   
580  C CA  . LYS A 71  ? 0.7350 0.6679 0.7646 -0.1066 -0.1552 0.0703  71  LYS A CA  
581  C C   . LYS A 71  ? 0.9057 0.8097 0.9185 -0.0986 -0.1674 0.0612  71  LYS A C   
582  O O   . LYS A 71  ? 0.7647 0.6678 0.7889 -0.0977 -0.1780 0.0495  71  LYS A O   
583  C CB  . LYS A 71  ? 0.8366 0.7687 0.8720 -0.1171 -0.1589 0.0732  71  LYS A CB  
584  C CG  . LYS A 71  ? 0.8573 0.8076 0.8961 -0.1240 -0.1456 0.0861  71  LYS A CG  
585  C CD  . LYS A 71  ? 0.8288 0.7966 0.8905 -0.1361 -0.1475 0.0855  71  LYS A CD  
586  C CE  . LYS A 71  ? 1.0036 0.9995 1.0763 -0.1423 -0.1328 0.0965  71  LYS A CE  
587  N NZ  . LYS A 71  ? 1.0991 1.1109 1.1913 -0.1550 -0.1337 0.0974  71  LYS A NZ  
588  N N   . ASP A 72  ? 0.8158 0.6962 0.8016 -0.0931 -0.1663 0.0664  72  ASP A N   
589  C CA  . ASP A 72  ? 0.8950 0.7467 0.8632 -0.0860 -0.1780 0.0587  72  ASP A CA  
590  C C   . ASP A 72  ? 0.9072 0.7615 0.8792 -0.0781 -0.1807 0.0493  72  ASP A C   
591  O O   . ASP A 72  ? 0.8751 0.7140 0.8450 -0.0749 -0.1935 0.0388  72  ASP A O   
592  C CB  . ASP A 72  ? 0.8010 0.6301 0.7393 -0.0813 -0.1737 0.0671  72  ASP A CB  
593  C CG  . ASP A 72  ? 1.0750 0.9141 1.0050 -0.0761 -0.1586 0.0752  72  ASP A CG  
594  O OD1 . ASP A 72  ? 1.1240 0.9815 1.0606 -0.0809 -0.1469 0.0848  72  ASP A OD1 
595  O OD2 . ASP A 72  ? 1.0997 0.9284 1.0167 -0.0671 -0.1582 0.0720  72  ASP A OD2 
596  N N   . GLN A 73  ? 0.8600 0.7336 0.8376 -0.0750 -0.1690 0.0529  73  GLN A N   
597  C CA  . GLN A 73  ? 0.9882 0.8653 0.9687 -0.0675 -0.1703 0.0446  73  GLN A CA  
598  C C   . GLN A 73  ? 0.7745 0.6689 0.7820 -0.0716 -0.1780 0.0338  73  GLN A C   
599  O O   . GLN A 73  ? 0.7790 0.6737 0.7892 -0.0657 -0.1820 0.0249  73  GLN A O   
600  C CB  . GLN A 73  ? 0.8259 0.7177 0.8032 -0.0628 -0.1547 0.0527  73  GLN A CB  
601  C CG  . GLN A 73  ? 1.1304 1.0070 1.0822 -0.0596 -0.1460 0.0638  73  GLN A CG  
602  C CD  . GLN A 73  ? 1.1636 1.0477 1.1077 -0.0524 -0.1325 0.0692  73  GLN A CD  
603  O OE1 . GLN A 73  ? 1.2796 1.1653 1.2131 -0.0524 -0.1208 0.0804  73  GLN A OE1 
604  N NE2 . GLN A 73  ? 1.1139 1.0027 1.0632 -0.0462 -0.1341 0.0612  73  GLN A NE2 
605  N N   . LEU A 74  ? 0.6314 0.5399 0.6585 -0.0817 -0.1800 0.0342  74  LEU A N   
606  C CA  . LEU A 74  ? 0.7138 0.6379 0.7666 -0.0865 -0.1878 0.0235  74  LEU A CA  
607  C C   . LEU A 74  ? 0.8046 0.7081 0.8527 -0.0820 -0.2032 0.0104  74  LEU A C   
608  O O   . LEU A 74  ? 0.6666 0.5791 0.7286 -0.0806 -0.2085 0.0001  74  LEU A O   
609  C CB  . LEU A 74  ? 0.7068 0.6450 0.7784 -0.0985 -0.1883 0.0262  74  LEU A CB  
610  C CG  . LEU A 74  ? 0.6504 0.6149 0.7330 -0.1046 -0.1736 0.0378  74  LEU A CG  
611  C CD1 . LEU A 74  ? 0.7642 0.7452 0.8694 -0.1170 -0.1757 0.0375  74  LEU A CD1 
612  C CD2 . LEU A 74  ? 0.6529 0.6387 0.7454 -0.1004 -0.1650 0.0377  74  LEU A CD2 
613  N N   . SER A 75  ? 0.8202 0.6959 0.8486 -0.0797 -0.2108 0.0106  75  SER A N   
614  C CA  . SER A 75  ? 0.6103 0.4652 0.6330 -0.0753 -0.2256 -0.0014 75  SER A CA  
615  C C   . SER A 75  ? 0.7698 0.6218 0.7849 -0.0655 -0.2257 -0.0076 75  SER A C   
616  O O   . SER A 75  ? 0.6585 0.5038 0.6780 -0.0628 -0.2370 -0.0197 75  SER A O   
617  C CB  . SER A 75  ? 1.0206 0.8456 1.0201 -0.0736 -0.2320 0.0018  75  SER A CB  
618  O OG  . SER A 75  ? 0.7058 0.5202 0.6812 -0.0678 -0.2225 0.0117  75  SER A OG  
619  N N   . LEU A 76  ? 0.8479 0.7048 0.8517 -0.0602 -0.2131 0.0003  76  LEU A N   
620  C CA  . LEU A 76  ? 0.6870 0.5412 0.6820 -0.0508 -0.2114 -0.0045 76  LEU A CA  
621  C C   . LEU A 76  ? 0.7749 0.6570 0.7930 -0.0519 -0.2072 -0.0092 76  LEU A C   
622  O O   . LEU A 76  ? 0.7247 0.6069 0.7380 -0.0445 -0.2058 -0.0139 76  LEU A O   
623  C CB  . LEU A 76  ? 0.7608 0.6059 0.7319 -0.0444 -0.1995 0.0062  76  LEU A CB  
624  C CG  . LEU A 76  ? 0.8301 0.6461 0.7753 -0.0425 -0.2033 0.0110  76  LEU A CG  
625  C CD1 . LEU A 76  ? 1.0309 0.8393 0.9533 -0.0364 -0.1908 0.0210  76  LEU A CD1 
626  C CD2 . LEU A 76  ? 0.9279 0.7202 0.8635 -0.0383 -0.2187 0.0000  76  LEU A CD2 
627  N N   . GLY A 77  ? 0.6614 0.6095 0.6700 0.0089  -0.0492 0.0550  77  GLY A N   
628  C CA  . GLY A 77  ? 0.6983 0.6507 0.7081 0.0185  -0.0385 0.0538  77  GLY A CA  
629  C C   . GLY A 77  ? 0.6191 0.5718 0.6226 0.0111  -0.0349 0.0491  77  GLY A C   
630  O O   . GLY A 77  ? 0.5786 0.5384 0.5878 0.0138  -0.0256 0.0492  77  GLY A O   
631  N N   . ASN A 78  ? 0.5475 0.4928 0.5398 0.0021  -0.0420 0.0453  78  ASN A N   
632  C CA  . ASN A 78  ? 0.6028 0.5491 0.5903 -0.0059 -0.0391 0.0411  78  ASN A CA  
633  C C   . ASN A 78  ? 0.6043 0.5413 0.5781 -0.0044 -0.0444 0.0369  78  ASN A C   
634  O O   . ASN A 78  ? 0.6646 0.5939 0.6306 -0.0109 -0.0536 0.0361  78  ASN A O   
635  C CB  . ASN A 78  ? 0.7054 0.6538 0.6944 -0.0218 -0.0418 0.0409  78  ASN A CB  
636  C CG  . ASN A 78  ? 0.8558 0.8097 0.8462 -0.0277 -0.0342 0.0379  78  ASN A CG  
637  O OD1 . ASN A 78  ? 0.9143 0.8657 0.8975 -0.0361 -0.0360 0.0343  78  ASN A OD1 
638  N ND2 . ASN A 78  ? 0.9527 0.9141 0.9525 -0.0229 -0.0254 0.0395  78  ASN A ND2 
639  N N   . ALA A 79  ? 0.6177 0.5551 0.5885 0.0035  -0.0390 0.0345  79  ALA A N   
640  C CA  . ALA A 79  ? 0.5503 0.4803 0.5094 0.0037  -0.0436 0.0305  79  ALA A CA  
641  C C   . ALA A 79  ? 0.5819 0.5180 0.5430 -0.0068 -0.0403 0.0277  79  ALA A C   
642  O O   . ALA A 79  ? 0.6866 0.6291 0.6523 -0.0035 -0.0322 0.0267  79  ALA A O   
643  C CB  . ALA A 79  ? 0.6397 0.5656 0.5935 0.0185  -0.0405 0.0297  79  ALA A CB  
644  N N   . ALA A 80  ? 0.5926 0.5270 0.5508 -0.0199 -0.0460 0.0267  80  ALA A N   
645  C CA  . ALA A 80  ? 0.6058 0.5455 0.5651 -0.0305 -0.0429 0.0240  80  ALA A CA  
646  C C   . ALA A 80  ? 0.5077 0.4427 0.4588 -0.0324 -0.0485 0.0210  80  ALA A C   
647  O O   . ALA A 80  ? 0.5677 0.4940 0.5105 -0.0358 -0.0578 0.0211  80  ALA A O   
648  C CB  . ALA A 80  ? 0.6162 0.5569 0.5767 -0.0443 -0.0447 0.0249  80  ALA A CB  
649  N N   . LEU A 81  ? 0.5047 0.4451 0.4583 -0.0305 -0.0434 0.0185  81  LEU A N   
650  C CA  . LEU A 81  ? 0.4719 0.4102 0.4203 -0.0334 -0.0482 0.0159  81  LEU A CA  
651  C C   . LEU A 81  ? 0.5481 0.4933 0.5003 -0.0470 -0.0456 0.0144  81  LEU A C   
652  O O   . LEU A 81  ? 0.4702 0.4240 0.4301 -0.0484 -0.0366 0.0136  81  LEU A O   
653  C CB  . LEU A 81  ? 0.4998 0.4399 0.4490 -0.0225 -0.0449 0.0145  81  LEU A CB  
654  C CG  . LEU A 81  ? 0.6093 0.5512 0.5573 -0.0257 -0.0482 0.0120  81  LEU A CG  
655  C CD1 . LEU A 81  ? 0.5533 0.4839 0.4902 -0.0268 -0.0601 0.0117  81  LEU A CD1 
656  C CD2 . LEU A 81  ? 0.5711 0.5171 0.5226 -0.0155 -0.0428 0.0111  81  LEU A CD2 
657  N N   . GLN A 82  ? 0.5384 0.4792 0.4845 -0.0567 -0.0530 0.0139  82  GLN A N   
658  C CA  . GLN A 82  ? 0.6263 0.5733 0.5749 -0.0697 -0.0504 0.0126  82  GLN A CA  
659  C C   . GLN A 82  ? 0.5842 0.5335 0.5329 -0.0710 -0.0535 0.0108  82  GLN A C   
660  O O   . GLN A 82  ? 0.5753 0.5165 0.5168 -0.0695 -0.0629 0.0111  82  GLN A O   
661  C CB  . GLN A 82  ? 0.6961 0.6371 0.6380 -0.0817 -0.0559 0.0140  82  GLN A CB  
662  C CG  . GLN A 82  ? 0.6953 0.6414 0.6376 -0.0954 -0.0532 0.0127  82  GLN A CG  
663  C CD  . GLN A 82  ? 0.8727 0.8114 0.8065 -0.1075 -0.0588 0.0145  82  GLN A CD  
664  O OE1 . GLN A 82  ? 0.9737 0.9043 0.8997 -0.1115 -0.0683 0.0156  82  GLN A OE1 
665  N NE2 . GLN A 82  ? 0.8918 0.8323 0.8260 -0.1135 -0.0534 0.0148  82  GLN A NE2 
666  N N   . ILE A 83  ? 0.6084 0.5686 0.5656 -0.0738 -0.0457 0.0090  83  ILE A N   
667  C CA  . ILE A 83  ? 0.4980 0.4638 0.4589 -0.0760 -0.0474 0.0076  83  ILE A CA  
668  C C   . ILE A 83  ? 0.5187 0.4921 0.4836 -0.0894 -0.0427 0.0068  83  ILE A C   
669  O O   . ILE A 83  ? 0.6365 0.6158 0.6060 -0.0918 -0.0331 0.0059  83  ILE A O   
670  C CB  . ILE A 83  ? 0.6100 0.5828 0.5789 -0.0649 -0.0418 0.0063  83  ILE A CB  
671  C CG1 . ILE A 83  ? 0.6255 0.5895 0.5883 -0.0516 -0.0465 0.0072  83  ILE A CG1 
672  C CG2 . ILE A 83  ? 0.5858 0.5665 0.5612 -0.0682 -0.0433 0.0053  83  ILE A CG2 
673  C CD1 . ILE A 83  ? 0.6833 0.6521 0.6515 -0.0406 -0.0425 0.0063  83  ILE A CD1 
674  N N   . THR A 84  ? 0.6478 0.6203 0.6101 -0.0982 -0.0493 0.0073  84  THR A N   
675  C CA  . THR A 84  ? 0.6092 0.5881 0.5738 -0.1117 -0.0453 0.0071  84  THR A CA  
676  C C   . THR A 84  ? 0.5248 0.5170 0.5016 -0.1120 -0.0406 0.0058  84  THR A C   
677  O O   . THR A 84  ? 0.6200 0.6135 0.6002 -0.1058 -0.0462 0.0059  84  THR A O   
678  C CB  . THR A 84  ? 0.6419 0.6118 0.5965 -0.1225 -0.0552 0.0090  84  THR A CB  
679  O OG1 . THR A 84  ? 0.7400 0.7057 0.6929 -0.1192 -0.0655 0.0097  84  THR A OG1 
680  C CG2 . THR A 84  ? 0.7040 0.6614 0.6474 -0.1231 -0.0596 0.0106  84  THR A CG2 
681  N N   . ASP A 85  ? 0.5489 0.5508 0.5320 -0.1190 -0.0304 0.0046  85  ASP A N   
682  C CA  . ASP A 85  ? 0.5321 0.5482 0.5284 -0.1205 -0.0253 0.0037  85  ASP A CA  
683  C C   . ASP A 85  ? 0.5106 0.5326 0.5164 -0.1068 -0.0228 0.0026  85  ASP A C   
684  O O   . ASP A 85  ? 0.5767 0.6022 0.5881 -0.1028 -0.0290 0.0032  85  ASP A O   
685  C CB  . ASP A 85  ? 0.5911 0.6080 0.5874 -0.1290 -0.0344 0.0057  85  ASP A CB  
686  C CG  . ASP A 85  ? 0.6284 0.6617 0.6396 -0.1336 -0.0283 0.0054  85  ASP A CG  
687  O OD1 . ASP A 85  ? 0.7281 0.7710 0.7474 -0.1322 -0.0159 0.0035  85  ASP A OD1 
688  O OD2 . ASP A 85  ? 0.8033 0.8397 0.8182 -0.1388 -0.0359 0.0073  85  ASP A OD2 
689  N N   . VAL A 86  ? 0.4576 0.4798 0.4646 -0.0999 -0.0142 0.0011  86  VAL A N   
690  C CA  . VAL A 86  ? 0.5169 0.5425 0.5309 -0.0865 -0.0116 0.0003  86  VAL A CA  
691  C C   . VAL A 86  ? 0.6431 0.6826 0.6715 -0.0853 -0.0080 -0.0004 86  VAL A C   
692  O O   . VAL A 86  ? 0.4646 0.5138 0.5004 -0.0924 -0.0001 -0.0014 86  VAL A O   
693  C CB  . VAL A 86  ? 0.5851 0.6085 0.5980 -0.0813 -0.0022 -0.0008 86  VAL A CB  
694  C CG1 . VAL A 86  ? 0.5238 0.5529 0.5457 -0.0691 0.0029  -0.0017 86  VAL A CG1 
695  C CG2 . VAL A 86  ? 0.5997 0.6104 0.6010 -0.0791 -0.0074 0.0006  86  VAL A CG2 
696  N N   . LYS A 87  ? 0.4976 0.5380 0.5300 -0.0758 -0.0137 0.0002  87  LYS A N   
697  C CA  . LYS A 87  ? 0.4896 0.5430 0.5368 -0.0723 -0.0121 0.0000  87  LYS A CA  
698  C C   . LYS A 87  ? 0.5615 0.6169 0.6137 -0.0598 -0.0051 -0.0011 87  LYS A C   
699  O O   . LYS A 87  ? 0.4781 0.5242 0.5219 -0.0533 -0.0033 -0.0013 87  LYS A O   
700  C CB  . LYS A 87  ? 0.5765 0.6282 0.6234 -0.0712 -0.0254 0.0017  87  LYS A CB  
701  C CG  . LYS A 87  ? 0.5705 0.6186 0.6118 -0.0833 -0.0341 0.0032  87  LYS A CG  
702  C CD  . LYS A 87  ? 0.8119 0.8662 0.8557 -0.0956 -0.0258 0.0029  87  LYS A CD  
703  C CE  . LYS A 87  ? 0.7523 0.8246 0.8140 -0.0997 -0.0197 0.0030  87  LYS A CE  
704  N NZ  . LYS A 87  ? 0.8648 0.9421 0.9273 -0.1140 -0.0153 0.0036  87  LYS A NZ  
705  N N   . LEU A 88  ? 0.4384 0.5063 0.5053 -0.0563 -0.0011 -0.0015 88  LEU A N   
706  C CA  . LEU A 88  ? 0.6059 0.6749 0.6774 -0.0439 0.0041  -0.0021 88  LEU A CA  
707  C C   . LEU A 88  ? 0.4940 0.5528 0.5569 -0.0339 -0.0054 -0.0007 88  LEU A C   
708  O O   . LEU A 88  ? 0.4321 0.4853 0.4913 -0.0242 -0.0015 -0.0008 88  LEU A O   
709  C CB  . LEU A 88  ? 0.5110 0.5954 0.6005 -0.0417 0.0092  -0.0025 88  LEU A CB  
710  C CG  . LEU A 88  ? 0.5281 0.6207 0.6251 -0.0464 0.0232  -0.0046 88  LEU A CG  
711  C CD1 . LEU A 88  ? 0.6478 0.7576 0.7642 -0.0465 0.0270  -0.0046 88  LEU A CD1 
712  C CD2 . LEU A 88  ? 0.4946 0.5806 0.5872 -0.0387 0.0322  -0.0062 88  LEU A CD2 
713  N N   . GLN A 89  ? 0.4411 0.4963 0.4998 -0.0362 -0.0177 0.0007  89  GLN A N   
714  C CA  . GLN A 89  ? 0.5410 0.5845 0.5889 -0.0267 -0.0269 0.0017  89  GLN A CA  
715  C C   . GLN A 89  ? 0.5757 0.6049 0.6078 -0.0241 -0.0270 0.0018  89  GLN A C   
716  O O   . GLN A 89  ? 0.4256 0.4444 0.4478 -0.0147 -0.0321 0.0025  89  GLN A O   
717  C CB  . GLN A 89  ? 0.5738 0.6157 0.6199 -0.0304 -0.0407 0.0030  89  GLN A CB  
718  C CG  . GLN A 89  ? 0.7541 0.7946 0.7966 -0.0437 -0.0455 0.0034  89  GLN A CG  
719  C CD  . GLN A 89  ? 0.8388 0.8957 0.8976 -0.0539 -0.0425 0.0037  89  GLN A CD  
720  O OE1 . GLN A 89  ? 0.6378 0.7078 0.7113 -0.0512 -0.0343 0.0033  89  GLN A OE1 
721  N NE2 . GLN A 89  ? 0.8770 0.9330 0.9333 -0.0656 -0.0488 0.0048  89  GLN A NE2 
722  N N   . ASP A 90  ? 0.4200 0.4482 0.4494 -0.0319 -0.0215 0.0012  90  ASP A N   
723  C CA  . ASP A 90  ? 0.4970 0.5134 0.5142 -0.0292 -0.0208 0.0017  90  ASP A CA  
724  C C   . ASP A 90  ? 0.5179 0.5341 0.5366 -0.0205 -0.0111 0.0015  90  ASP A C   
725  O O   . ASP A 90  ? 0.5088 0.5162 0.5190 -0.0164 -0.0104 0.0025  90  ASP A O   
726  C CB  . ASP A 90  ? 0.5016 0.5166 0.5152 -0.0413 -0.0197 0.0015  90  ASP A CB  
727  C CG  . ASP A 90  ? 0.6082 0.6198 0.6168 -0.0497 -0.0305 0.0022  90  ASP A CG  
728  O OD1 . ASP A 90  ? 0.5049 0.5088 0.5067 -0.0447 -0.0404 0.0030  90  ASP A OD1 
729  O OD2 . ASP A 90  ? 0.6348 0.6504 0.6453 -0.0616 -0.0291 0.0021  90  ASP A OD2 
730  N N   . ALA A 91  ? 0.4080 0.4336 0.4379 -0.0176 -0.0035 0.0006  91  ALA A N   
731  C CA  . ALA A 91  ? 0.4365 0.4609 0.4676 -0.0091 0.0052  0.0007  91  ALA A CA  
732  C C   . ALA A 91  ? 0.4651 0.4816 0.4893 0.0033  0.0007  0.0024  91  ALA A C   
733  O O   . ALA A 91  ? 0.4268 0.4429 0.4502 0.0070  -0.0074 0.0028  91  ALA A O   
734  C CB  . ALA A 91  ? 0.4538 0.4891 0.4982 -0.0085 0.0137  -0.0007 91  ALA A CB  
735  N N   . GLY A 92  ? 0.4651 0.4752 0.4839 0.0093  0.0057  0.0035  92  GLY A N   
736  C CA  . GLY A 92  ? 0.5132 0.5152 0.5242 0.0212  0.0031  0.0053  92  GLY A CA  
737  C C   . GLY A 92  ? 0.4782 0.4722 0.4812 0.0240  0.0060  0.0070  92  GLY A C   
738  O O   . GLY A 92  ? 0.4515 0.4469 0.4566 0.0173  0.0108  0.0069  92  GLY A O   
739  N N   . VAL A 93  ? 0.4713 0.4567 0.4648 0.0341  0.0029  0.0087  93  VAL A N   
740  C CA  . VAL A 93  ? 0.4834 0.4620 0.4703 0.0387  0.0064  0.0110  93  VAL A CA  
741  C C   . VAL A 93  ? 0.4227 0.3930 0.3991 0.0384  -0.0023 0.0112  93  VAL A C   
742  O O   . VAL A 93  ? 0.4590 0.4225 0.4266 0.0437  -0.0100 0.0109  93  VAL A O   
743  C CB  . VAL A 93  ? 0.6246 0.5990 0.6079 0.0511  0.0112  0.0131  93  VAL A CB  
744  C CG1 . VAL A 93  ? 0.5980 0.5672 0.5766 0.0554  0.0157  0.0159  93  VAL A CG1 
745  C CG2 . VAL A 93  ? 0.5473 0.5289 0.5409 0.0514  0.0191  0.0128  93  VAL A CG2 
746  N N   . TYR A 94  ? 0.4672 0.4370 0.4439 0.0322  -0.0015 0.0118  94  TYR A N   
747  C CA  . TYR A 94  ? 0.4308 0.3925 0.3983 0.0316  -0.0090 0.0123  94  TYR A CA  
748  C C   . TYR A 94  ? 0.4495 0.4053 0.4119 0.0412  -0.0051 0.0151  94  TYR A C   
749  O O   . TYR A 94  ? 0.4873 0.4473 0.4560 0.0434  0.0038  0.0170  94  TYR A O   
750  C CB  . TYR A 94  ? 0.4363 0.4012 0.4076 0.0188  -0.0108 0.0117  94  TYR A CB  
751  C CG  . TYR A 94  ? 0.4760 0.4460 0.4511 0.0087  -0.0152 0.0093  94  TYR A CG  
752  C CD1 . TYR A 94  ? 0.4504 0.4300 0.4353 0.0055  -0.0093 0.0079  94  TYR A CD1 
753  C CD2 . TYR A 94  ? 0.5185 0.4837 0.4875 0.0022  -0.0248 0.0086  94  TYR A CD2 
754  C CE1 . TYR A 94  ? 0.4342 0.4199 0.4239 -0.0035 -0.0122 0.0060  94  TYR A CE1 
755  C CE2 . TYR A 94  ? 0.4790 0.4498 0.4523 -0.0076 -0.0282 0.0069  94  TYR A CE2 
756  C CZ  . TYR A 94  ? 0.4852 0.4668 0.4693 -0.0103 -0.0215 0.0057  94  TYR A CZ  
757  O OH  . TYR A 94  ? 0.4885 0.4770 0.4782 -0.0198 -0.0239 0.0044  94  TYR A OH  
758  N N   . ARG A 95  ? 0.4805 0.4261 0.4315 0.0469  -0.0117 0.0155  95  ARG A N   
759  C CA  . ARG A 95  ? 0.5860 0.5259 0.5318 0.0561  -0.0084 0.0182  95  ARG A CA  
760  C C   . ARG A 95  ? 0.5587 0.4929 0.4999 0.0529  -0.0148 0.0185  95  ARG A C   
761  O O   . ARG A 95  ? 0.5684 0.4956 0.5015 0.0502  -0.0245 0.0165  95  ARG A O   
762  C CB  . ARG A 95  ? 0.5032 0.4339 0.4371 0.0696  -0.0088 0.0186  95  ARG A CB  
763  C CG  . ARG A 95  ? 0.7063 0.6416 0.6447 0.0756  0.0005  0.0201  95  ARG A CG  
764  C CD  . ARG A 95  ? 0.6496 0.5769 0.5764 0.0853  -0.0023 0.0194  95  ARG A CD  
765  N NE  . ARG A 95  ? 0.9729 0.8933 0.8912 0.0977  0.0038  0.0223  95  ARG A NE  
766  C CZ  . ARG A 95  ? 0.9981 0.9080 0.9020 0.1081  0.0018  0.0222  95  ARG A CZ  
767  N NH1 . ARG A 95  ? 0.9777 0.8837 0.8756 0.1079  -0.0061 0.0197  95  ARG A NH1 
768  N NH2 . ARG A 95  ? 1.1190 1.0218 1.0138 0.1191  0.0076  0.0248  95  ARG A NH2 
769  N N   . CYS A 96  ? 0.4214 0.3585 0.3685 0.0531  -0.0097 0.0214  96  CYS A N   
770  C CA  . CYS A 96  ? 0.4920 0.4237 0.4356 0.0525  -0.0148 0.0225  96  CYS A CA  
771  C C   . CYS A 96  ? 0.5023 0.4280 0.4402 0.0664  -0.0110 0.0251  96  CYS A C   
772  O O   . CYS A 96  ? 0.5590 0.4906 0.5038 0.0716  -0.0015 0.0280  96  CYS A O   
773  C CB  . CYS A 96  ? 0.5558 0.4954 0.5109 0.0422  -0.0128 0.0243  96  CYS A CB  
774  S SG  . CYS A 96  ? 0.6810 0.6298 0.6486 0.0460  -0.0007 0.0285  96  CYS A SG  
775  N N   . MET A 97  ? 0.5983 0.5119 0.5231 0.0726  -0.0180 0.0240  97  MET A N   
776  C CA  . MET A 97  ? 0.4922 0.3976 0.4080 0.0871  -0.0148 0.0257  97  MET A CA  
777  C C   . MET A 97  ? 0.5845 0.4844 0.4983 0.0883  -0.0194 0.0269  97  MET A C   
778  O O   . MET A 97  ? 0.6238 0.5153 0.5298 0.0836  -0.0296 0.0245  97  MET A O   
779  C CB  . MET A 97  ? 0.5364 0.4294 0.4353 0.0947  -0.0196 0.0227  97  MET A CB  
780  C CG  . MET A 97  ? 0.6176 0.5160 0.5190 0.0923  -0.0174 0.0214  97  MET A CG  
781  S SD  . MET A 97  ? 0.7825 0.6658 0.6636 0.1017  -0.0239 0.0186  97  MET A SD  
782  C CE  . MET A 97  ? 0.7778 0.6561 0.6516 0.1182  -0.0128 0.0218  97  MET A CE  
783  N N   . ILE A 98  ? 0.5635 0.4679 0.4847 0.0946  -0.0120 0.0308  98  ILE A N   
784  C CA  . ILE A 98  ? 0.5328 0.4345 0.4559 0.0954  -0.0158 0.0327  98  ILE A CA  
785  C C   . ILE A 98  ? 0.6789 0.5751 0.5968 0.1113  -0.0098 0.0350  98  ILE A C   
786  O O   . ILE A 98  ? 0.5910 0.4944 0.5154 0.1179  0.0010  0.0381  98  ILE A O   
787  C CB  . ILE A 98  ? 0.5458 0.4610 0.4873 0.0848  -0.0138 0.0358  98  ILE A CB  
788  C CG1 . ILE A 98  ? 0.5384 0.4572 0.4825 0.0693  -0.0194 0.0331  98  ILE A CG1 
789  C CG2 . ILE A 98  ? 0.5309 0.4433 0.4749 0.0864  -0.0183 0.0383  98  ILE A CG2 
790  C CD1 . ILE A 98  ? 0.6573 0.5894 0.6176 0.0588  -0.0150 0.0355  98  ILE A CD1 
791  N N   . SER A 99  ? 0.6485 0.5311 0.5536 0.1176  -0.0167 0.0336  99  SER A N   
792  C CA  . SER A 99  ? 0.6878 0.5646 0.5887 0.1324  -0.0117 0.0359  99  SER A CA  
793  C C   . SER A 99  ? 0.6367 0.5167 0.5479 0.1297  -0.0155 0.0386  99  SER A C   
794  O O   . SER A 99  ? 0.6527 0.5240 0.5576 0.1238  -0.0267 0.0363  99  SER A O   
795  C CB  . SER A 99  ? 0.6748 0.5314 0.5515 0.1430  -0.0167 0.0320  99  SER A CB  
796  O OG  . SER A 99  ? 0.8201 0.6702 0.6918 0.1577  -0.0116 0.0339  99  SER A OG  
797  N N   . TYR A 100 ? 0.6298 0.5223 0.5574 0.1338  -0.0066 0.0438  100 TYR A N   
798  C CA  . TYR A 100 ? 0.5429 0.4397 0.4823 0.1328  -0.0096 0.0473  100 TYR A CA  
799  C C   . TYR A 100 ? 0.7411 0.6456 0.6904 0.1462  0.0024  0.0524  100 TYR A C   
800  O O   . TYR A 100 ? 0.7058 0.6265 0.6733 0.1431  0.0106  0.0570  100 TYR A O   
801  C CB  . TYR A 100 ? 0.6086 0.5182 0.5644 0.1161  -0.0134 0.0490  100 TYR A CB  
802  C CG  . TYR A 100 ? 0.5769 0.4895 0.5435 0.1127  -0.0194 0.0524  100 TYR A CG  
803  C CD1 . TYR A 100 ? 0.7385 0.6373 0.6937 0.1123  -0.0308 0.0500  100 TYR A CD1 
804  C CD2 . TYR A 100 ? 0.6702 0.5989 0.6583 0.1089  -0.0147 0.0580  100 TYR A CD2 
805  C CE1 . TYR A 100 ? 0.7435 0.6443 0.7082 0.1091  -0.0370 0.0533  100 TYR A CE1 
806  C CE2 . TYR A 100 ? 0.7069 0.6384 0.7053 0.1055  -0.0212 0.0613  100 TYR A CE2 
807  C CZ  . TYR A 100 ? 0.6376 0.5551 0.6242 0.1058  -0.0323 0.0590  100 TYR A CZ  
808  O OH  . TYR A 100 ? 0.7353 0.6549 0.7317 0.1026  -0.0394 0.0626  100 TYR A OH  
809  N N   . GLY A 101 ? 0.7352 0.6274 0.6716 0.1611  0.0039  0.0517  101 GLY A N   
810  C CA  . GLY A 101 ? 0.8397 0.7381 0.7819 0.1748  0.0174  0.0559  101 GLY A CA  
811  C C   . GLY A 101 ? 0.9490 0.8461 0.8818 0.1775  0.0251  0.0543  101 GLY A C   
812  O O   . GLY A 101 ? 0.8447 0.7254 0.7550 0.1851  0.0236  0.0500  101 GLY A O   
813  N N   . GLY A 102 ? 0.8280 0.7415 0.7773 0.1711  0.0329  0.0580  102 GLY A N   
814  C CA  . GLY A 102 ? 0.6589 0.5723 0.6013 0.1713  0.0392  0.0568  102 GLY A CA  
815  C C   . GLY A 102 ? 0.6933 0.5986 0.6235 0.1611  0.0291  0.0509  102 GLY A C   
816  O O   . GLY A 102 ? 0.6375 0.5344 0.5608 0.1553  0.0174  0.0472  102 GLY A O   
817  N N   . ALA A 103 ? 0.6041 0.5121 0.5323 0.1589  0.0339  0.0503  103 ALA A N   
818  C CA  . ALA A 103 ? 0.6326 0.5352 0.5518 0.1497  0.0257  0.0452  103 ALA A CA  
819  C C   . ALA A 103 ? 0.5791 0.4940 0.5098 0.1421  0.0318  0.0467  103 ALA A C   
820  O O   . ALA A 103 ? 0.6106 0.5320 0.5473 0.1478  0.0430  0.0507  103 ALA A O   
821  C CB  . ALA A 103 ? 0.6848 0.5693 0.5792 0.1591  0.0221  0.0409  103 ALA A CB  
822  N N   . ASP A 104 ? 0.6319 0.5492 0.5653 0.1292  0.0247  0.0435  104 ASP A N   
823  C CA  . ASP A 104 ? 0.5310 0.4587 0.4747 0.1215  0.0299  0.0443  104 ASP A CA  
824  C C   . ASP A 104 ? 0.5273 0.4530 0.4675 0.1105  0.0208  0.0393  104 ASP A C   
825  O O   . ASP A 104 ? 0.5478 0.4662 0.4805 0.1070  0.0108  0.0362  104 ASP A O   
826  C CB  . ASP A 104 ? 0.5215 0.4640 0.4862 0.1145  0.0354  0.0489  104 ASP A CB  
827  C CG  . ASP A 104 ? 0.6468 0.5981 0.6205 0.1112  0.0440  0.0510  104 ASP A CG  
828  O OD1 . ASP A 104 ? 0.6725 0.6350 0.6627 0.1047  0.0482  0.0548  104 ASP A OD1 
829  O OD2 . ASP A 104 ? 0.6876 0.6341 0.6520 0.1149  0.0460  0.0490  104 ASP A OD2 
830  N N   . TYR A 105 ? 0.5868 0.5185 0.5319 0.1056  0.0246  0.0388  105 TYR A N   
831  C CA  . TYR A 105 ? 0.4707 0.4038 0.4164 0.0943  0.0177  0.0348  105 TYR A CA  
832  C C   . TYR A 105 ? 0.5665 0.5106 0.5253 0.0870  0.0245  0.0358  105 TYR A C   
833  O O   . TYR A 105 ? 0.5443 0.4925 0.5081 0.0921  0.0338  0.0392  105 TYR A O   
834  C CB  . TYR A 105 ? 0.5854 0.5082 0.5158 0.0985  0.0115  0.0308  105 TYR A CB  
835  C CG  . TYR A 105 ? 0.5933 0.5152 0.5196 0.1058  0.0178  0.0313  105 TYR A CG  
836  C CD1 . TYR A 105 ? 0.6650 0.5946 0.5996 0.0994  0.0205  0.0305  105 TYR A CD1 
837  C CD2 . TYR A 105 ? 0.7613 0.6737 0.6745 0.1193  0.0210  0.0326  105 TYR A CD2 
838  C CE1 . TYR A 105 ? 0.8686 0.7968 0.7994 0.1063  0.0256  0.0313  105 TYR A CE1 
839  C CE2 . TYR A 105 ? 0.7554 0.6659 0.6635 0.1258  0.0263  0.0333  105 TYR A CE2 
840  C CZ  . TYR A 105 ? 0.7062 0.6247 0.6235 0.1192  0.0282  0.0328  105 TYR A CZ  
841  O OH  . TYR A 105 ? 0.8837 0.7996 0.7958 0.1258  0.0329  0.0338  105 TYR A OH  
842  N N   . LYS A 106 ? 0.5241 0.4723 0.4878 0.0750  0.0198  0.0330  106 LYS A N   
843  C CA  . LYS A 106 ? 0.5406 0.4974 0.5148 0.0677  0.0255  0.0330  106 LYS A CA  
844  C C   . LYS A 106 ? 0.5169 0.4737 0.4887 0.0616  0.0208  0.0286  106 LYS A C   
845  O O   . LYS A 106 ? 0.5925 0.5449 0.5577 0.0584  0.0120  0.0257  106 LYS A O   
846  C CB  . LYS A 106 ? 0.5306 0.4951 0.5171 0.0574  0.0269  0.0349  106 LYS A CB  
847  C CG  . LYS A 106 ? 0.5514 0.5201 0.5460 0.0621  0.0342  0.0403  106 LYS A CG  
848  C CD  . LYS A 106 ? 0.4413 0.4112 0.4369 0.0700  0.0437  0.0426  106 LYS A CD  
849  C CE  . LYS A 106 ? 0.7891 0.7645 0.7943 0.0737  0.0513  0.0486  106 LYS A CE  
850  N NZ  . LYS A 106 ? 0.7341 0.7056 0.7340 0.0850  0.0516  0.0511  106 LYS A NZ  
851  N N   . ARG A 107 ? 0.5060 0.4681 0.4838 0.0599  0.0270  0.0283  107 ARG A N   
852  C CA  . ARG A 107 ? 0.5245 0.4887 0.5030 0.0550  0.0246  0.0246  107 ARG A CA  
853  C C   . ARG A 107 ? 0.4748 0.4463 0.4631 0.0421  0.0262  0.0232  107 ARG A C   
854  O O   . ARG A 107 ? 0.4729 0.4481 0.4685 0.0388  0.0322  0.0254  107 ARG A O   
855  C CB  . ARG A 107 ? 0.6177 0.5819 0.5959 0.0628  0.0305  0.0252  107 ARG A CB  
856  C CG  . ARG A 107 ? 0.8002 0.7558 0.7661 0.0752  0.0284  0.0260  107 ARG A CG  
857  C CD  . ARG A 107 ? 0.9000 0.8552 0.8650 0.0813  0.0322  0.0261  107 ARG A CD  
858  N NE  . ARG A 107 ? 0.9461 0.9091 0.9230 0.0755  0.0391  0.0262  107 ARG A NE  
859  N N   . ILE A 108 ? 0.4674 0.4404 0.4554 0.0348  0.0209  0.0197  108 ILE A N   
860  C CA  . ILE A 108 ? 0.4614 0.4404 0.4566 0.0226  0.0226  0.0178  108 ILE A CA  
861  C C   . ILE A 108 ? 0.4385 0.4214 0.4361 0.0211  0.0226  0.0146  108 ILE A C   
862  O O   . ILE A 108 ? 0.4708 0.4520 0.4640 0.0223  0.0156  0.0130  108 ILE A O   
863  C CB  . ILE A 108 ? 0.4695 0.4472 0.4625 0.0131  0.0158  0.0172  108 ILE A CB  
864  C CG1 . ILE A 108 ? 0.4824 0.4569 0.4744 0.0154  0.0151  0.0206  108 ILE A CG1 
865  C CG2 . ILE A 108 ? 0.4645 0.4471 0.4627 0.0005  0.0181  0.0151  108 ILE A CG2 
866  C CD1 . ILE A 108 ? 0.6282 0.5988 0.6156 0.0089  0.0064  0.0205  108 ILE A CD1 
867  N N   . THR A 109 ? 0.4464 0.4343 0.4512 0.0184  0.0300  0.0137  109 THR A N   
868  C CA  . THR A 109 ? 0.4334 0.4263 0.4426 0.0168  0.0309  0.0107  109 THR A CA  
869  C C   . THR A 109 ? 0.4902 0.4873 0.5023 0.0041  0.0296  0.0081  109 THR A C   
870  O O   . THR A 109 ? 0.4652 0.4625 0.4787 -0.0034 0.0334  0.0080  109 THR A O   
871  C CB  . THR A 109 ? 0.5748 0.5699 0.5898 0.0212  0.0399  0.0109  109 THR A CB  
872  O OG1 . THR A 109 ? 0.5344 0.5249 0.5456 0.0327  0.0412  0.0138  109 THR A OG1 
873  C CG2 . THR A 109 ? 0.4927 0.4938 0.5137 0.0205  0.0407  0.0081  109 THR A CG2 
874  N N   . VAL A 110 ? 0.4108 0.4111 0.4235 0.0016  0.0243  0.0061  110 VAL A N   
875  C CA  . VAL A 110 ? 0.4739 0.4791 0.4895 -0.0102 0.0236  0.0038  110 VAL A CA  
876  C C   . VAL A 110 ? 0.5201 0.5335 0.5446 -0.0096 0.0282  0.0016  110 VAL A C   
877  O O   . VAL A 110 ? 0.4425 0.4582 0.4694 -0.0031 0.0245  0.0017  110 VAL A O   
878  C CB  . VAL A 110 ? 0.4910 0.4937 0.5010 -0.0150 0.0132  0.0039  110 VAL A CB  
879  C CG1 . VAL A 110 ? 0.5557 0.5641 0.5690 -0.0271 0.0132  0.0018  110 VAL A CG1 
880  C CG2 . VAL A 110 ? 0.5118 0.5064 0.5136 -0.0153 0.0089  0.0060  110 VAL A CG2 
881  N N   . LYS A 111 ? 0.3825 0.3998 0.4117 -0.0162 0.0360  -0.0003 111 LYS A N   
882  C CA  . LYS A 111 ? 0.4498 0.4755 0.4882 -0.0167 0.0415  -0.0026 111 LYS A CA  
883  C C   . LYS A 111 ? 0.4989 0.5295 0.5386 -0.0287 0.0413  -0.0046 111 LYS A C   
884  O O   . LYS A 111 ? 0.4587 0.4850 0.4920 -0.0374 0.0414  -0.0047 111 LYS A O   
885  C CB  . LYS A 111 ? 0.4418 0.4667 0.4835 -0.0137 0.0520  -0.0035 111 LYS A CB  
886  C CG  . LYS A 111 ? 0.8509 0.8838 0.9026 -0.0116 0.0584  -0.0058 111 LYS A CG  
887  N N   . VAL A 112 ? 0.4247 0.4644 0.4728 -0.0294 0.0408  -0.0057 112 VAL A N   
888  C CA  . VAL A 112 ? 0.3884 0.4341 0.4386 -0.0407 0.0406  -0.0070 112 VAL A CA  
889  C C   . VAL A 112 ? 0.5705 0.6254 0.6311 -0.0417 0.0509  -0.0095 112 VAL A C   
890  O O   . VAL A 112 ? 0.3848 0.4472 0.4560 -0.0341 0.0522  -0.0095 112 VAL A O   
891  C CB  . VAL A 112 ? 0.3855 0.4345 0.4371 -0.0424 0.0298  -0.0056 112 VAL A CB  
892  C CG1 . VAL A 112 ? 0.4932 0.5488 0.5476 -0.0547 0.0304  -0.0064 112 VAL A CG1 
893  C CG2 . VAL A 112 ? 0.3845 0.4227 0.4245 -0.0407 0.0200  -0.0035 112 VAL A CG2 
894  N N   . ASN A 113 ? 0.4371 0.4910 0.4942 -0.0506 0.0581  -0.0115 113 ASN A N   
895  C CA  . ASN A 113 ? 0.4138 0.4764 0.4794 -0.0533 0.0680  -0.0141 113 ASN A CA  
896  C C   . ASN A 113 ? 0.4398 0.5119 0.5107 -0.0616 0.0649  -0.0137 113 ASN A C   
897  O O   . ASN A 113 ? 0.5112 0.5794 0.5740 -0.0701 0.0579  -0.0124 113 ASN A O   
898  C CB  . ASN A 113 ? 0.4806 0.5362 0.5379 -0.0595 0.0774  -0.0166 113 ASN A CB  
899  C CG  . ASN A 113 ? 0.5284 0.5752 0.5819 -0.0522 0.0814  -0.0169 113 ASN A CG  
900  O OD1 . ASN A 113 ? 0.4944 0.5436 0.5553 -0.0417 0.0833  -0.0166 113 ASN A OD1 
901  N ND2 . ASN A 113 ? 0.4775 0.5138 0.5193 -0.0584 0.0825  -0.0172 113 ASN A ND2 
902  N N   . ALA A 114 ? 0.4193 0.6999 0.3219 -0.0856 0.0887  0.0466  114 ALA A N   
903  C CA  . ALA A 114 ? 0.4419 0.7326 0.4000 -0.0880 0.0663  0.0630  114 ALA A CA  
904  C C   . ALA A 114 ? 0.4387 0.7536 0.4047 -0.0950 0.0551  0.0736  114 ALA A C   
905  O O   . ALA A 114 ? 0.5429 0.8393 0.4607 -0.0970 0.0545  0.0603  114 ALA A O   
906  C CB  . ALA A 114 ? 0.4666 0.6984 0.4175 -0.0839 0.0441  0.0486  114 ALA A CB  
907  N N   . PRO A 115 ? 0.4746 0.8302 0.5004 -0.0988 0.0460  0.0974  115 PRO A N   
908  C CA  . PRO A 115 ? 0.5440 0.9218 0.5807 -0.1055 0.0332  0.1083  115 PRO A CA  
909  C C   . PRO A 115 ? 0.3989 0.7273 0.4165 -0.1061 0.0061  0.0956  115 PRO A C   
910  O O   . PRO A 115 ? 0.4597 0.7399 0.4660 -0.1016 -0.0055 0.0814  115 PRO A O   
911  C CB  . PRO A 115 ? 0.4104 0.8333 0.5164 -0.1058 0.0288  0.1344  115 PRO A CB  
912  C CG  . PRO A 115 ? 0.3778 0.7971 0.4960 -0.0959 0.0433  0.1332  115 PRO A CG  
913  C CD  . PRO A 115 ? 0.3929 0.7824 0.4792 -0.0973 0.0503  0.1168  115 PRO A CD  
914  N N   . TYR A 116 ? 0.5003 0.8427 0.5153 -0.1118 -0.0042 0.1013  116 TYR A N   
915  C CA  . TYR A 116 ? 0.4705 0.7698 0.4646 -0.1130 -0.0293 0.0897  116 TYR A CA  
916  C C   . TYR A 116 ? 0.4418 0.7132 0.4707 -0.1107 -0.0518 0.0911  116 TYR A C   
917  O O   . TYR A 116 ? 0.4395 0.6561 0.4373 -0.1078 -0.0663 0.0720  116 TYR A O   
918  C CB  . TYR A 116 ? 0.4802 0.8100 0.4841 -0.1199 -0.0381 0.1023  116 TYR A CB  
919  C CG  . TYR A 116 ? 0.5398 0.8263 0.5210 -0.1213 -0.0637 0.0904  116 TYR A CG  
920  C CD1 . TYR A 116 ? 0.4443 0.6843 0.3596 -0.1193 -0.0640 0.0657  116 TYR A CD1 
921  C CD2 . TYR A 116 ? 0.5561 0.8474 0.5818 -0.1243 -0.0877 0.1035  116 TYR A CD2 
922  C CE1 . TYR A 116 ? 0.5816 0.7818 0.4758 -0.1203 -0.0873 0.0545  116 TYR A CE1 
923  C CE2 . TYR A 116 ? 0.6151 0.8668 0.6203 -0.1254 -0.1113 0.0925  116 TYR A CE2 
924  C CZ  . TYR A 116 ? 0.5109 0.7172 0.4502 -0.1234 -0.1110 0.0679  116 TYR A CZ  
925  O OH  . TYR A 116 ? 0.6153 0.7823 0.5337 -0.1244 -0.1344 0.0567  116 TYR A OH  
926  N N   . ALA A 117 ? 0.3573 0.6657 0.4510 -0.1121 -0.0560 0.1138  117 ALA A N   
927  C CA  . ALA A 117 ? 0.5590 0.8429 0.6885 -0.1108 -0.0794 0.1166  117 ALA A CA  
928  C C   . ALA A 117 ? 0.4248 0.6591 0.5330 -0.1038 -0.0788 0.0978  117 ALA A C   
929  O O   . ALA A 117 ? 0.5684 0.7536 0.6635 -0.1018 -0.0990 0.0841  117 ALA A O   
930  C CB  . ALA A 117 ? 0.5108 0.8461 0.7138 -0.1132 -0.0807 0.1447  117 ALA A CB  
931  N N   . ALA A 118 ? 0.4755 0.7213 0.5782 -0.0998 -0.0556 0.0962  118 ALA A N   
932  C CA  . ALA A 118 ? 0.6049 0.8058 0.6873 -0.0928 -0.0533 0.0788  118 ALA A CA  
933  C C   . ALA A 118 ? 0.4619 0.6060 0.4749 -0.0903 -0.0574 0.0507  118 ALA A C   
934  O O   . ALA A 118 ? 0.5922 0.6857 0.5920 -0.0866 -0.0735 0.0358  118 ALA A O   
935  C CB  . ALA A 118 ? 0.4586 0.6870 0.5469 -0.0893 -0.0259 0.0832  118 ALA A CB  
936  N N   . HIS A 119 ? 0.4478 0.5996 0.4158 -0.0921 -0.0430 0.0431  119 HIS A N   
937  C CA  . HIS A 119 ? 0.5149 0.6150 0.4157 -0.0899 -0.0462 0.0169  119 HIS A CA  
938  C C   . HIS A 119 ? 0.6084 0.6728 0.5066 -0.0916 -0.0756 0.0107  119 HIS A C   
939  O O   . HIS A 119 ? 0.6189 0.6278 0.4768 -0.0877 -0.0858 -0.0111 119 HIS A O   
940  C CB  . HIS A 119 ? 0.5784 0.7001 0.4395 -0.0931 -0.0286 0.0140  119 HIS A CB  
941  C CG  . HIS A 119 ? 1.1009 1.2233 0.9276 -0.0890 -0.0014 0.0037  119 HIS A CG  
942  N ND1 . HIS A 119 ? 0.8905 1.0654 0.7318 -0.0910 0.0221  0.0177  119 HIS A ND1 
943  C CD2 . HIS A 119 ? 0.9830 1.0600 0.7612 -0.0830 0.0061  -0.0191 119 HIS A CD2 
944  C CE1 . HIS A 119 ? 0.7074 0.8695 0.5110 -0.0866 0.0429  0.0039  119 HIS A CE1 
945  N NE2 . HIS A 119 ? 1.0913 1.1943 0.8562 -0.0817 0.0338  -0.0184 119 HIS A NE2 
946  N N   . HIS A 120 ? 0.5740 0.6705 0.5156 -0.0974 -0.0894 0.0300  120 HIS A N   
947  C CA  . HIS A 120 ? 0.5355 0.6043 0.4789 -0.0998 -0.1174 0.0266  120 HIS A CA  
948  C C   . HIS A 120 ? 0.6217 0.6496 0.5827 -0.0954 -0.1349 0.0196  120 HIS A C   
949  O O   . HIS A 120 ? 0.6981 0.6752 0.6285 -0.0935 -0.1524 0.0018  120 HIS A O   
950  C CB  . HIS A 120 ? 0.6359 0.7544 0.6297 -0.1067 -0.1262 0.0517  120 HIS A CB  
951  C CG  . HIS A 120 ? 0.6668 0.7634 0.6614 -0.1101 -0.1535 0.0498  120 HIS A CG  
952  N ND1 . HIS A 120 ? 0.8107 0.9446 0.8526 -0.1159 -0.1662 0.0713  120 HIS A ND1 
953  C CD2 . HIS A 120 ? 0.8016 0.8454 0.7519 -0.1086 -0.1693 0.0289  120 HIS A CD2 
954  C CE1 . HIS A 120 ? 1.1898 1.2934 1.2187 -0.1179 -0.1895 0.0637  120 HIS A CE1 
955  N NE2 . HIS A 120 ? 1.3017 1.3507 1.2751 -0.1135 -0.1918 0.0380  120 HIS A NE2 
956  N N   . HIS A 121 ? 0.6000 0.6498 0.6106 -0.0936 -0.1304 0.0337  121 HIS A N   
957  C CA  . HIS A 121 ? 0.7357 0.7467 0.7629 -0.0891 -0.1452 0.0269  121 HIS A CA  
958  C C   . HIS A 121 ? 0.7803 0.7372 0.7503 -0.0823 -0.1390 -0.0003 121 HIS A C   
959  O O   . HIS A 121 ? 0.9394 0.8463 0.8965 -0.0790 -0.1569 -0.0152 121 HIS A O   
960  C CB  . HIS A 121 ? 0.7943 0.8404 0.8825 -0.0881 -0.1383 0.0468  121 HIS A CB  
961  C CG  . HIS A 121 ? 0.9596 0.9696 1.0706 -0.0839 -0.1544 0.0420  121 HIS A CG  
962  N ND1 . HIS A 121 ? 1.1654 1.1405 1.2816 -0.0849 -0.1820 0.0363  121 HIS A ND1 
963  C CD2 . HIS A 121 ? 1.0516 1.0539 1.1802 -0.0785 -0.1467 0.0414  121 HIS A CD2 
964  C CE1 . HIS A 121 ? 1.1805 1.1285 1.3174 -0.0805 -0.1907 0.0326  121 HIS A CE1 
965  N NE2 . HIS A 121 ? 1.2318 1.1953 1.3764 -0.0765 -0.1697 0.0357  121 HIS A NE2 
966  N N   . HIS A 122 ? 0.7587 0.7251 0.6941 -0.0800 -0.1135 -0.0071 122 HIS A N   
967  C CA  . HIS A 122 ? 0.8528 0.7705 0.7318 -0.0735 -0.1054 -0.0327 122 HIS A CA  
968  C C   . HIS A 122 ? 1.0253 0.8985 0.8478 -0.0737 -0.1179 -0.0536 122 HIS A C   
969  O O   . HIS A 122 ? 0.9152 0.7351 0.6988 -0.0683 -0.1232 -0.0756 122 HIS A O   
970  C CB  . HIS A 122 ? 0.9109 0.8551 0.7693 -0.0718 -0.0744 -0.0329 122 HIS A CB  
971  C CG  . HIS A 122 ? 0.9138 0.8136 0.7214 -0.0647 -0.0633 -0.0566 122 HIS A CG  
972  N ND1 . HIS A 122 ? 0.8827 0.7482 0.6982 -0.0586 -0.0692 -0.0648 122 HIS A ND1 
973  C CD2 . HIS A 122 ? 0.8326 0.7178 0.5814 -0.0625 -0.0460 -0.0733 122 HIS A CD2 
974  C CE1 . HIS A 122 ? 0.9689 0.8003 0.7324 -0.0530 -0.0563 -0.0858 122 HIS A CE1 
975  N NE2 . HIS A 122 ? 0.9623 0.8048 0.6846 -0.0552 -0.0421 -0.0913 122 HIS A NE2 
976  N N   . HIS A 123 ? 0.8562 0.7510 0.6736 -0.0798 -0.1225 -0.0469 123 HIS A N   
977  C CA  . HIS A 123 ? 0.9137 0.7701 0.6778 -0.0803 -0.1337 -0.0655 123 HIS A CA  
978  C C   . HIS A 123 ? 1.0572 0.8728 0.8310 -0.0797 -0.1637 -0.0721 123 HIS A C   
979  O O   . HIS A 123 ? 0.9578 0.7216 0.6842 -0.0764 -0.1734 -0.0944 123 HIS A O   
980  C CB  . HIS A 123 ? 0.9397 0.8352 0.7000 -0.0871 -0.1294 -0.0545 123 HIS A CB  
981  C CG  . HIS A 123 ? 0.9465 0.8092 0.6448 -0.0874 -0.1334 -0.0736 123 HIS A CG  
982  N ND1 . HIS A 123 ? 0.9946 0.8594 0.6922 -0.0925 -0.1508 -0.0701 123 HIS A ND1 
983  C CD2 . HIS A 123 ? 0.8705 0.6990 0.5055 -0.0832 -0.1215 -0.0961 123 HIS A CD2 
984  C CE1 . HIS A 123 ? 1.0103 0.8429 0.6468 -0.0914 -0.1497 -0.0897 123 HIS A CE1 
985  N NE2 . HIS A 123 ? 1.0365 0.8465 0.6341 -0.0858 -0.1320 -0.1057 123 HIS A NE2 
986  N N   . HIS A 124 ? 1.2022 1.0404 1.0374 -0.0828 -0.1787 -0.0529 124 HIS A N   
987  C CA  . HIS A 124 ? 1.2895 1.0903 1.1386 -0.0823 -0.2072 -0.0582 124 HIS A CA  
988  C C   . HIS A 124 ? 1.4435 1.2030 1.2925 -0.0754 -0.2110 -0.0708 124 HIS A C   
989  O O   . HIS A 124 ? 1.5695 1.2805 1.4018 -0.0729 -0.2312 -0.0860 124 HIS A O   
990  C CB  . HIS A 124 ? 1.1657 1.0035 1.0808 -0.0881 -0.2228 -0.0336 124 HIS A CB  
991  C CG  . HIS A 124 ? 1.2567 1.1331 1.1760 -0.0950 -0.2230 -0.0205 124 HIS A CG  
992  N ND1 . HIS A 124 ? 1.2087 1.1307 1.1867 -0.1007 -0.2310 0.0046  124 HIS A ND1 
993  C CD2 . HIS A 124 ? 1.2399 1.1164 1.1120 -0.0970 -0.2160 -0.0289 124 HIS A CD2 
994  C CE1 . HIS A 124 ? 1.2679 1.2159 1.2344 -0.1059 -0.2294 0.0109  124 HIS A CE1 
995  N NE2 . HIS A 124 ? 1.3114 1.2326 1.2140 -0.1039 -0.2203 -0.0091 124 HIS A NE2 
996  N N   . ALA A 125 ? 1.4083 1.1870 1.2783 -0.0722 -0.1931 -0.0641 125 ALA A N   
997  C CA  . ALA A 125 ? 1.5202 1.2604 1.3899 -0.0654 -0.1957 -0.0759 125 ALA A CA  
998  C C   . ALA A 125 ? 1.6808 1.3653 1.4807 -0.0597 -0.1932 -0.1051 125 ALA A C   
999  O O   . ALA A 125 ? 1.9321 1.5666 1.7167 -0.0563 -0.2117 -0.1208 125 ALA A O   
1000 C CB  . ALA A 125 ? 1.4904 1.2649 1.3918 -0.0632 -0.1741 -0.0631 125 ALA A CB  
1001 N N   . ALA A 126 ? 1.6810 1.3736 1.4375 -0.0586 -0.1705 -0.1127 126 ALA A N   
1002 C CA  . ALA A 126 ? 1.8530 1.4957 1.5410 -0.0533 -0.1661 -0.1399 126 ALA A CA  
1003 C C   . ALA A 126 ? 1.8301 1.4472 1.4824 -0.0560 -0.1830 -0.1512 126 ALA A C   
1004 O O   . ALA A 126 ? 1.6804 1.2459 1.3074 -0.0526 -0.2006 -0.1690 126 ALA A O   
1005 C CB  . ALA A 126 ? 1.7508 1.4128 1.4058 -0.0517 -0.1359 -0.1435 126 ALA A CB  
1006 N N   . PHE B 1   ? 0.7756 0.6246 0.7982 0.1685  -0.1124 -0.0915 1   PHE B N   
1007 C CA  . PHE B 1   ? 0.9164 0.7693 0.9399 0.1678  -0.1007 -0.0970 1   PHE B CA  
1008 C C   . PHE B 1   ? 0.8431 0.7103 0.8766 0.1595  -0.1009 -0.0779 1   PHE B C   
1009 O O   . PHE B 1   ? 0.8907 0.7782 0.9440 0.1623  -0.1000 -0.0665 1   PHE B O   
1010 C CB  . PHE B 1   ? 0.7149 0.5812 0.7552 0.1815  -0.0852 -0.1132 1   PHE B CB  
1011 C CG  . PHE B 1   ? 0.8612 0.7325 0.9039 0.1810  -0.0731 -0.1188 1   PHE B CG  
1012 C CD1 . PHE B 1   ? 0.7806 0.6344 0.8033 0.1787  -0.0709 -0.1308 1   PHE B CD1 
1013 C CD2 . PHE B 1   ? 0.5668 0.4602 0.6308 0.1829  -0.0646 -0.1112 1   PHE B CD2 
1014 C CE1 . PHE B 1   ? 0.8241 0.6828 0.8495 0.1783  -0.0597 -0.1353 1   PHE B CE1 
1015 C CE2 . PHE B 1   ? 0.5823 0.4798 0.6483 0.1820  -0.0539 -0.1160 1   PHE B CE2 
1016 C CZ  . PHE B 1   ? 0.6442 0.5245 0.6914 0.1795  -0.0511 -0.1279 1   PHE B CZ  
1017 N N   . THR B 2   ? 0.7917 0.6487 0.8111 0.1499  -0.1018 -0.0745 2   THR B N   
1018 C CA  . THR B 2   ? 0.7401 0.6075 0.7648 0.1408  -0.1032 -0.0565 2   THR B CA  
1019 C C   . THR B 2   ? 0.7289 0.5966 0.7505 0.1387  -0.0924 -0.0619 2   THR B C   
1020 O O   . THR B 2   ? 0.8603 0.7098 0.8638 0.1369  -0.0917 -0.0722 2   THR B O   
1021 C CB  . THR B 2   ? 0.8212 0.6739 0.8302 0.1282  -0.1195 -0.0412 2   THR B CB  
1022 O OG1 . THR B 2   ? 0.8485 0.6972 0.8574 0.1301  -0.1302 -0.0382 2   THR B OG1 
1023 C CG2 . THR B 2   ? 0.7717 0.6390 0.7895 0.1200  -0.1213 -0.0214 2   THR B CG2 
1024 N N   . VAL B 3   ? 0.6188 0.5075 0.6575 0.1394  -0.0845 -0.0546 3   VAL B N   
1025 C CA  . VAL B 3   ? 0.6063 0.4970 0.6425 0.1349  -0.0760 -0.0548 3   VAL B CA  
1026 C C   . VAL B 3   ? 0.8229 0.7104 0.8503 0.1222  -0.0852 -0.0365 3   VAL B C   
1027 O O   . VAL B 3   ? 0.6277 0.5261 0.6633 0.1192  -0.0927 -0.0211 3   VAL B O   
1028 C CB  . VAL B 3   ? 0.6601 0.5748 0.7190 0.1430  -0.0630 -0.0574 3   VAL B CB  
1029 C CG1 . VAL B 3   ? 0.6530 0.5713 0.7096 0.1368  -0.0559 -0.0541 3   VAL B CG1 
1030 C CG2 . VAL B 3   ? 0.5780 0.4939 0.6447 0.1554  -0.0532 -0.0769 3   VAL B CG2 
1031 N N   . THR B 4   ? 0.7189 0.5914 0.7295 0.1151  -0.0847 -0.0379 4   THR B N   
1032 C CA  . THR B 4   ? 0.8129 0.6807 0.8141 0.1032  -0.0926 -0.0220 4   THR B CA  
1033 C C   . THR B 4   ? 0.6873 0.5587 0.6869 0.1004  -0.0820 -0.0234 4   THR B C   
1034 O O   . THR B 4   ? 0.8268 0.6951 0.8249 0.1056  -0.0713 -0.0377 4   THR B O   
1035 C CB  . THR B 4   ? 0.9169 0.7579 0.8952 0.0963  -0.1062 -0.0203 4   THR B CB  
1036 O OG1 . THR B 4   ? 1.0562 0.8800 1.0203 0.1005  -0.1017 -0.0370 4   THR B OG1 
1037 C CG2 . THR B 4   ? 0.7769 0.6147 0.7564 0.0972  -0.1186 -0.0155 4   THR B CG2 
1038 N N   . VAL B 5   ? 0.6994 0.5779 0.6995 0.0921  -0.0850 -0.0083 5   VAL B N   
1039 C CA  . VAL B 5   ? 0.8153 0.6954 0.8113 0.0878  -0.0767 -0.0078 5   VAL B CA  
1040 C C   . VAL B 5   ? 0.7779 0.6399 0.7547 0.0767  -0.0868 0.0023  5   VAL B C   
1041 O O   . VAL B 5   ? 0.7014 0.5652 0.6779 0.0703  -0.0980 0.0173  5   VAL B O   
1042 C CB  . VAL B 5   ? 0.8382 0.7448 0.8519 0.0890  -0.0700 0.0002  5   VAL B CB  
1043 C CG1 . VAL B 5   ? 0.6767 0.5988 0.7084 0.1008  -0.0583 -0.0121 5   VAL B CG1 
1044 C CG2 . VAL B 5   ? 0.6075 0.5259 0.6282 0.0855  -0.0809 0.0176  5   VAL B CG2 
1045 N N   . PRO B 6   ? 0.7593 0.6035 0.7201 0.0747  -0.0837 -0.0051 6   PRO B N   
1046 C CA  . PRO B 6   ? 0.7443 0.5716 0.6877 0.0649  -0.0927 0.0045  6   PRO B CA  
1047 C C   . PRO B 6   ? 0.6486 0.4900 0.5968 0.0577  -0.0914 0.0183  6   PRO B C   
1048 O O   . PRO B 6   ? 0.8292 0.6635 0.7692 0.0492  -0.1025 0.0315  6   PRO B O   
1049 C CB  . PRO B 6   ? 0.6759 0.4851 0.6041 0.0673  -0.0863 -0.0084 6   PRO B CB  
1050 C CG  . PRO B 6   ? 0.7200 0.5443 0.6614 0.0758  -0.0704 -0.0211 6   PRO B CG  
1051 C CD  . PRO B 6   ? 0.7975 0.6380 0.7565 0.0816  -0.0709 -0.0219 6   PRO B CD  
1052 N N   . LYS B 7   ? 0.6204 0.4820 0.5816 0.0611  -0.0787 0.0157  7   LYS B N   
1053 C CA  . LYS B 7   ? 0.6422 0.5196 0.6081 0.0555  -0.0769 0.0277  7   LYS B CA  
1054 C C   . LYS B 7   ? 0.6976 0.6027 0.6850 0.0621  -0.0713 0.0294  7   LYS B C   
1055 O O   . LYS B 7   ? 0.6646 0.5773 0.6625 0.0707  -0.0611 0.0171  7   LYS B O   
1056 C CB  . LYS B 7   ? 0.7363 0.6092 0.6934 0.0532  -0.0664 0.0224  7   LYS B CB  
1057 C CG  . LYS B 7   ? 0.6383 0.4857 0.5738 0.0467  -0.0714 0.0229  7   LYS B CG  
1058 C CD  . LYS B 7   ? 0.8394 0.6860 0.7688 0.0456  -0.0593 0.0176  7   LYS B CD  
1059 C CE  . LYS B 7   ? 0.9174 0.7832 0.8526 0.0406  -0.0564 0.0281  7   LYS B CE  
1060 N NZ  . LYS B 7   ? 0.8177 0.6899 0.7535 0.0424  -0.0419 0.0203  7   LYS B NZ  
1061 N N   . ASP B 8   ? 0.6021 0.5225 0.5963 0.0585  -0.0784 0.0449  8   ASP B N   
1062 C CA  . ASP B 8   ? 0.6088 0.5566 0.6224 0.0653  -0.0742 0.0485  8   ASP B CA  
1063 C C   . ASP B 8   ? 0.5206 0.4830 0.5344 0.0619  -0.0690 0.0551  8   ASP B C   
1064 O O   . ASP B 8   ? 0.4574 0.4434 0.4855 0.0670  -0.0672 0.0604  8   ASP B O   
1065 C CB  . ASP B 8   ? 0.6381 0.5962 0.6610 0.0664  -0.0857 0.0611  8   ASP B CB  
1066 C CG  . ASP B 8   ? 0.6770 0.6335 0.6905 0.0556  -0.0971 0.0791  8   ASP B CG  
1067 O OD1 . ASP B 8   ? 0.6766 0.6226 0.6757 0.0473  -0.0964 0.0812  8   ASP B OD1 
1068 O OD2 . ASP B 8   ? 0.7827 0.7488 0.8037 0.0556  -0.1068 0.0914  8   ASP B OD2 
1069 N N   . LEU B 9   ? 0.4837 0.4324 0.4813 0.0539  -0.0668 0.0548  9   LEU B N   
1070 C CA  . LEU B 9   ? 0.4500 0.4100 0.4450 0.0504  -0.0609 0.0588  9   LEU B CA  
1071 C C   . LEU B 9   ? 0.5118 0.4557 0.4945 0.0482  -0.0510 0.0469  9   LEU B C   
1072 O O   . LEU B 9   ? 0.5037 0.4243 0.4715 0.0439  -0.0541 0.0438  9   LEU B O   
1073 C CB  . LEU B 9   ? 0.4235 0.3863 0.4097 0.0410  -0.0710 0.0763  9   LEU B CB  
1074 C CG  . LEU B 9   ? 0.4992 0.4745 0.4809 0.0373  -0.0658 0.0810  9   LEU B CG  
1075 C CD1 . LEU B 9   ? 0.5757 0.5803 0.5743 0.0448  -0.0641 0.0857  9   LEU B CD1 
1076 C CD2 . LEU B 9   ? 0.6435 0.6123 0.6103 0.0264  -0.0750 0.0949  9   LEU B CD2 
1077 N N   . TYR B 10  ? 0.4675 0.4240 0.4564 0.0519  -0.0398 0.0408  10  TYR B N   
1078 C CA  . TYR B 10  ? 0.5219 0.4671 0.5008 0.0501  -0.0293 0.0307  10  TYR B CA  
1079 C C   . TYR B 10  ? 0.4598 0.4191 0.4366 0.0465  -0.0249 0.0363  10  TYR B C   
1080 O O   . TYR B 10  ? 0.5284 0.5104 0.5183 0.0506  -0.0245 0.0407  10  TYR B O   
1081 C CB  . TYR B 10  ? 0.4534 0.3994 0.4429 0.0591  -0.0183 0.0149  10  TYR B CB  
1082 C CG  . TYR B 10  ? 0.4682 0.3978 0.4560 0.0630  -0.0209 0.0065  10  TYR B CG  
1083 C CD1 . TYR B 10  ? 0.4454 0.3803 0.4436 0.0677  -0.0282 0.0085  10  TYR B CD1 
1084 C CD2 . TYR B 10  ? 0.5986 0.5077 0.5738 0.0628  -0.0160 -0.0039 10  TYR B CD2 
1085 C CE1 . TYR B 10  ? 0.5518 0.4713 0.5468 0.0714  -0.0309 0.0001  10  TYR B CE1 
1086 C CE2 . TYR B 10  ? 0.5789 0.4731 0.5506 0.0670  -0.0191 -0.0118 10  TYR B CE2 
1087 C CZ  . TYR B 10  ? 0.5964 0.4957 0.5777 0.0710  -0.0266 -0.0101 10  TYR B CZ  
1088 O OH  . TYR B 10  ? 0.5775 0.4616 0.5537 0.0752  -0.0301 -0.0186 10  TYR B OH  
1089 N N   . VAL B 11  ? 0.4253 0.3709 0.3850 0.0394  -0.0222 0.0360  11  VAL B N   
1090 C CA  . VAL B 11  ? 0.4288 0.3849 0.3834 0.0358  -0.0171 0.0392  11  VAL B CA  
1091 C C   . VAL B 11  ? 0.5776 0.5240 0.5274 0.0373  -0.0039 0.0258  11  VAL B C   
1092 O O   . VAL B 11  ? 0.5418 0.4662 0.4773 0.0342  -0.0023 0.0211  11  VAL B O   
1093 C CB  . VAL B 11  ? 0.6242 0.5736 0.5620 0.0259  -0.0251 0.0513  11  VAL B CB  
1094 C CG1 . VAL B 11  ? 0.5778 0.5350 0.5072 0.0223  -0.0185 0.0521  11  VAL B CG1 
1095 C CG2 . VAL B 11  ? 0.5916 0.5538 0.5356 0.0246  -0.0379 0.0660  11  VAL B CG2 
1096 N N   . VAL B 12  ? 0.4793 0.4420 0.4411 0.0425  0.0051  0.0200  12  VAL B N   
1097 C CA  . VAL B 12  ? 0.5156 0.4716 0.4769 0.0451  0.0179  0.0070  12  VAL B CA  
1098 C C   . VAL B 12  ? 0.5446 0.5130 0.5038 0.0430  0.0247  0.0076  12  VAL B C   
1099 O O   . VAL B 12  ? 0.4709 0.4582 0.4354 0.0429  0.0204  0.0157  12  VAL B O   
1100 C CB  . VAL B 12  ? 0.5728 0.5345 0.5523 0.0546  0.0234  -0.0034 12  VAL B CB  
1101 C CG1 . VAL B 12  ? 0.6462 0.5974 0.6272 0.0571  0.0156  -0.0037 12  VAL B CG1 
1102 C CG2 . VAL B 12  ? 0.6979 0.6851 0.6962 0.0604  0.0244  -0.0016 12  VAL B CG2 
1103 N N   . GLU B 13  ? 0.5268 0.4841 0.4775 0.0417  0.0350  -0.0010 13  GLU B N   
1104 C CA  . GLU B 13  ? 0.5159 0.4815 0.4623 0.0392  0.0424  -0.0020 13  GLU B CA  
1105 C C   . GLU B 13  ? 0.4397 0.4208 0.4047 0.0463  0.0508  -0.0099 13  GLU B C   
1106 O O   . GLU B 13  ? 0.4600 0.4365 0.4350 0.0519  0.0565  -0.0190 13  GLU B O   
1107 C CB  . GLU B 13  ? 0.4916 0.4370 0.4193 0.0345  0.0494  -0.0072 13  GLU B CB  
1108 C CG  . GLU B 13  ? 0.5498 0.4768 0.4590 0.0281  0.0411  -0.0005 13  GLU B CG  
1109 C CD  . GLU B 13  ? 0.6186 0.5562 0.5220 0.0223  0.0311  0.0125  13  GLU B CD  
1110 O OE1 . GLU B 13  ? 0.6285 0.5790 0.5289 0.0200  0.0342  0.0146  13  GLU B OE1 
1111 O OE2 . GLU B 13  ? 0.6210 0.5546 0.5226 0.0200  0.0200  0.0208  13  GLU B OE2 
1112 N N   . TYR B 14  ? 0.4975 0.4970 0.4667 0.0463  0.0509  -0.0060 14  TYR B N   
1113 C CA  . TYR B 14  ? 0.5124 0.5257 0.4976 0.0522  0.0587  -0.0131 14  TYR B CA  
1114 C C   . TYR B 14  ? 0.5624 0.5624 0.5449 0.0523  0.0714  -0.0246 14  TYR B C   
1115 O O   . TYR B 14  ? 0.5238 0.5095 0.4885 0.0465  0.0757  -0.0257 14  TYR B O   
1116 C CB  . TYR B 14  ? 0.4745 0.5048 0.4573 0.0504  0.0568  -0.0074 14  TYR B CB  
1117 C CG  . TYR B 14  ? 0.4894 0.5326 0.4859 0.0554  0.0643  -0.0142 14  TYR B CG  
1118 C CD1 . TYR B 14  ? 0.5781 0.6135 0.5684 0.0525  0.0755  -0.0220 14  TYR B CD1 
1119 C CD2 . TYR B 14  ? 0.5084 0.5717 0.5244 0.0633  0.0597  -0.0123 14  TYR B CD2 
1120 C CE1 . TYR B 14  ? 0.5889 0.6361 0.5923 0.0565  0.0817  -0.0275 14  TYR B CE1 
1121 C CE2 . TYR B 14  ? 0.4923 0.5668 0.5214 0.0679  0.0655  -0.0182 14  TYR B CE2 
1122 C CZ  . TYR B 14  ? 0.6951 0.7616 0.7179 0.0640  0.0763  -0.0256 14  TYR B CZ  
1123 O OH  . TYR B 14  ? 0.6644 0.7420 0.7008 0.0681  0.0816  -0.0308 14  TYR B OH  
1124 N N   . GLY B 15  ? 0.5313 0.5362 0.5318 0.0594  0.0775  -0.0330 15  GLY B N   
1125 C CA  . GLY B 15  ? 0.5185 0.5139 0.5193 0.0606  0.0898  -0.0433 15  GLY B CA  
1126 C C   . GLY B 15  ? 0.6047 0.5810 0.5999 0.0623  0.0916  -0.0488 15  GLY B C   
1127 O O   . GLY B 15  ? 0.5845 0.5548 0.5826 0.0653  0.1016  -0.0577 15  GLY B O   
1128 N N   . SER B 16  ? 0.5150 0.4816 0.5017 0.0605  0.0819  -0.0435 16  SER B N   
1129 C CA  . SER B 16  ? 0.5982 0.5459 0.5780 0.0625  0.0817  -0.0484 16  SER B CA  
1130 C C   . SER B 16  ? 0.6176 0.5713 0.6150 0.0705  0.0806  -0.0539 16  SER B C   
1131 O O   . SER B 16  ? 0.4960 0.4679 0.5116 0.0747  0.0803  -0.0538 16  SER B O   
1132 C CB  . SER B 16  ? 0.6748 0.6082 0.6372 0.0569  0.0707  -0.0403 16  SER B CB  
1133 O OG  . SER B 16  ? 0.7447 0.6870 0.7154 0.0578  0.0597  -0.0334 16  SER B OG  
1134 N N   . ASN B 17  ? 0.6082 0.5457 0.5992 0.0731  0.0796  -0.0588 17  ASN B N   
1135 C CA  . ASN B 17  ? 0.5909 0.5306 0.5942 0.0802  0.0771  -0.0641 17  ASN B CA  
1136 C C   . ASN B 17  ? 0.6367 0.5675 0.6317 0.0780  0.0637  -0.0572 17  ASN B C   
1137 O O   . ASN B 17  ? 0.6041 0.5192 0.5807 0.0724  0.0584  -0.0522 17  ASN B O   
1138 C CB  . ASN B 17  ? 0.5072 0.4356 0.5086 0.0856  0.0852  -0.0753 17  ASN B CB  
1139 C CG  . ASN B 17  ? 0.6448 0.5811 0.6538 0.0873  0.0988  -0.0815 17  ASN B CG  
1140 O OD1 . ASN B 17  ? 0.6087 0.5625 0.6319 0.0873  0.1022  -0.0801 17  ASN B OD1 
1141 N ND2 . ASN B 17  ? 0.7394 0.6627 0.7386 0.0892  0.1061  -0.0879 17  ASN B ND2 
1142 N N   . MET B 18  ? 0.6146 0.5547 0.6231 0.0827  0.0580  -0.0568 18  MET B N   
1143 C CA  . MET B 18  ? 0.5379 0.4703 0.5399 0.0809  0.0452  -0.0502 18  MET B CA  
1144 C C   . MET B 18  ? 0.5637 0.4929 0.5733 0.0886  0.0436  -0.0583 18  MET B C   
1145 O O   . MET B 18  ? 0.5697 0.5114 0.5965 0.0957  0.0500  -0.0657 18  MET B O   
1146 C CB  . MET B 18  ? 0.5924 0.5406 0.6013 0.0781  0.0369  -0.0381 18  MET B CB  
1147 C CG  . MET B 18  ? 0.7851 0.7552 0.8167 0.0855  0.0386  -0.0396 18  MET B CG  
1148 S SD  . MET B 18  ? 0.6300 0.6162 0.6671 0.0839  0.0261  -0.0242 18  MET B SD  
1149 C CE  . MET B 18  ? 0.5319 0.5396 0.5961 0.0961  0.0283  -0.0293 18  MET B CE  
1150 N N   . THR B 19  ? 0.5480 0.4599 0.5444 0.0872  0.0347  -0.0571 19  THR B N   
1151 C CA  . THR B 19  ? 0.6483 0.5551 0.6483 0.0937  0.0310  -0.0642 19  THR B CA  
1152 C C   . THR B 19  ? 0.5429 0.4479 0.5405 0.0907  0.0169  -0.0541 19  THR B C   
1153 O O   . THR B 19  ? 0.5747 0.4648 0.5558 0.0841  0.0082  -0.0469 19  THR B O   
1154 C CB  . THR B 19  ? 0.7668 0.6527 0.7511 0.0960  0.0329  -0.0733 19  THR B CB  
1155 O OG1 . THR B 19  ? 0.6051 0.4956 0.5947 0.1001  0.0467  -0.0827 19  THR B OG1 
1156 C CG2 . THR B 19  ? 0.6755 0.5540 0.6593 0.1018  0.0265  -0.0795 19  THR B CG2 
1157 N N   . ILE B 20  ? 0.6292 0.5493 0.6437 0.0958  0.0145  -0.0534 20  ILE B N   
1158 C CA  . ILE B 20  ? 0.5511 0.4714 0.5658 0.0941  0.0017  -0.0441 20  ILE B CA  
1159 C C   . ILE B 20  ? 0.6305 0.5424 0.6462 0.1010  -0.0013 -0.0535 20  ILE B C   
1160 O O   . ILE B 20  ? 0.5388 0.4571 0.5660 0.1093  0.0070  -0.0652 20  ILE B O   
1161 C CB  . ILE B 20  ? 0.5957 0.5398 0.6277 0.0955  -0.0003 -0.0348 20  ILE B CB  
1162 C CG1 . ILE B 20  ? 0.6180 0.5788 0.6709 0.1057  0.0088  -0.0442 20  ILE B CG1 
1163 C CG2 . ILE B 20  ? 0.6514 0.6021 0.6782 0.0878  0.0005  -0.0245 20  ILE B CG2 
1164 C CD1 . ILE B 20  ? 0.7283 0.7127 0.7979 0.1087  0.0068  -0.0354 20  ILE B CD1 
1165 N N   . GLU B 21  ? 0.7052 0.5974 0.6504 0.2294  -0.0692 0.0186  21  GLU B N   
1166 C CA  . GLU B 21  ? 0.8423 0.7342 0.7760 0.2207  -0.0483 0.0234  21  GLU B CA  
1167 C C   . GLU B 21  ? 0.6993 0.5985 0.6102 0.2331  -0.0399 0.0056  21  GLU B C   
1168 O O   . GLU B 21  ? 0.7550 0.6671 0.6483 0.2412  -0.0380 -0.0064 21  GLU B O   
1169 C CB  . GLU B 21  ? 0.8720 0.7753 0.7922 0.2009  -0.0246 0.0386  21  GLU B CB  
1170 C CG  . GLU B 21  ? 0.8979 0.7953 0.8393 0.1883  -0.0329 0.0561  21  GLU B CG  
1171 C CD  . GLU B 21  ? 0.8335 0.7397 0.7638 0.1673  -0.0092 0.0725  21  GLU B CD  
1172 O OE1 . GLU B 21  ? 1.0185 0.9335 0.9268 0.1620  0.0138  0.0716  21  GLU B OE1 
1173 O OE2 . GLU B 21  ? 1.1044 1.0088 1.0480 0.1561  -0.0138 0.0865  21  GLU B OE2 
1174 N N   . CYS B 22  ? 0.8201 0.7109 0.7319 0.2345  -0.0354 0.0038  22  CYS B N   
1175 C CA  . CYS B 22  ? 0.8035 0.7023 0.6912 0.2423  -0.0223 -0.0102 22  CYS B CA  
1176 C C   . CYS B 22  ? 0.8220 0.7173 0.7054 0.2311  -0.0038 -0.0017 22  CYS B C   
1177 O O   . CYS B 22  ? 0.7052 0.5857 0.6097 0.2251  -0.0097 0.0090  22  CYS B O   
1178 C CB  . CYS B 22  ? 0.9495 0.8418 0.8419 0.2632  -0.0425 -0.0292 22  CYS B CB  
1179 S SG  . CYS B 22  ? 0.8923 0.7636 0.8048 0.2720  -0.0574 -0.0330 22  CYS B SG  
1180 N N   . LYS B 23  ? 0.7782 0.6874 0.6343 0.2281  0.0189  -0.0062 23  LYS B N   
1181 C CA  . LYS B 23  ? 0.8080 0.7179 0.6554 0.2157  0.0408  0.0020  23  LYS B CA  
1182 C C   . LYS B 23  ? 0.7661 0.6726 0.6051 0.2267  0.0422  -0.0115 23  LYS B C   
1183 O O   . LYS B 23  ? 0.8202 0.7321 0.6470 0.2417  0.0361  -0.0286 23  LYS B O   
1184 C CB  . LYS B 23  ? 0.8797 0.8086 0.7015 0.2034  0.0669  0.0073  23  LYS B CB  
1185 C CG  . LYS B 23  ? 0.8902 0.8267 0.7134 0.1949  0.0666  0.0169  23  LYS B CG  
1186 C CD  . LYS B 23  ? 1.0273 0.9525 0.8745 0.1807  0.0621  0.0360  23  LYS B CD  
1187 C CE  . LYS B 23  ? 0.9397 0.8771 0.7785 0.1658  0.0749  0.0484  23  LYS B CE  
1188 N NZ  . LYS B 23  ? 0.9332 0.8604 0.7971 0.1559  0.0631  0.0641  23  LYS B NZ  
1189 N N   . PHE B 24  ? 0.9285 0.8256 0.7745 0.2191  0.0500  -0.0038 24  PHE B N   
1190 C CA  . PHE B 24  ? 0.9201 0.8161 0.7551 0.2258  0.0567  -0.0144 24  PHE B CA  
1191 C C   . PHE B 24  ? 0.9320 0.8313 0.7587 0.2094  0.0816  -0.0026 24  PHE B C   
1192 O O   . PHE B 24  ? 0.8180 0.7128 0.6574 0.1945  0.0869  0.0144  24  PHE B O   
1193 C CB  . PHE B 24  ? 0.9448 0.8213 0.8015 0.2376  0.0348  -0.0203 24  PHE B CB  
1194 C CG  . PHE B 24  ? 0.8330 0.6926 0.7170 0.2279  0.0279  -0.0043 24  PHE B CG  
1195 C CD1 . PHE B 24  ? 0.7558 0.6082 0.6612 0.2255  0.0119  0.0047  24  PHE B CD1 
1196 C CD2 . PHE B 24  ? 0.7431 0.5939 0.6319 0.2212  0.0371  0.0016  24  PHE B CD2 
1197 C CE1 . PHE B 24  ? 0.8331 0.6699 0.7636 0.2166  0.0054  0.0193  24  PHE B CE1 
1198 C CE2 . PHE B 24  ? 0.6951 0.5301 0.6091 0.2123  0.0308  0.0161  24  PHE B CE2 
1199 C CZ  . PHE B 24  ? 0.8683 0.6963 0.8030 0.2100  0.0149  0.0250  24  PHE B CZ  
1200 N N   . PRO B 25  ? 0.8478 0.7553 0.6536 0.2115  0.0972  -0.0111 25  PRO B N   
1201 C CA  . PRO B 25  ? 0.8919 0.8051 0.6875 0.1956  0.1227  -0.0005 25  PRO B CA  
1202 C C   . PRO B 25  ? 1.0089 0.9045 0.8261 0.1889  0.1202  0.0095  25  PRO B C   
1203 O O   . PRO B 25  ? 1.0501 0.9323 0.8791 0.1997  0.1055  0.0020  25  PRO B O   
1204 C CB  . PRO B 25  ? 0.8443 0.7703 0.6125 0.2028  0.1362  -0.0151 25  PRO B CB  
1205 C CG  . PRO B 25  ? 1.0219 0.9398 0.7951 0.2224  0.1144  -0.0318 25  PRO B CG  
1206 C CD  . PRO B 25  ? 0.9124 0.8246 0.7026 0.2283  0.0925  -0.0311 25  PRO B CD  
1207 N N   . VAL B 26  ? 0.9153 0.8109 0.7378 0.1709  0.1348  0.0268  26  VAL B N   
1208 C CA  . VAL B 26  ? 1.1519 1.0328 0.9927 0.1620  0.1370  0.0377  26  VAL B CA  
1209 C C   . VAL B 26  ? 1.1704 1.0625 0.9947 0.1466  0.1661  0.0454  26  VAL B C   
1210 O O   . VAL B 26  ? 0.9380 0.8391 0.7573 0.1323  0.1802  0.0574  26  VAL B O   
1211 C CB  . VAL B 26  ? 1.0656 0.9330 0.9342 0.1544  0.1236  0.0525  26  VAL B CB  
1212 C CG1 . VAL B 26  ? 1.0234 0.8810 0.9077 0.1699  0.0948  0.0443  26  VAL B CG1 
1213 C CG2 . VAL B 26  ? 1.1888 1.0677 1.0516 0.1389  0.1370  0.0657  26  VAL B CG2 
1214 N N   . GLU B 27  ? 1.2804 1.1718 1.0962 0.1493  0.1751  0.0387  27  GLU B N   
1215 C CA  . GLU B 27  ? 1.1768 1.0797 0.9758 0.1358  0.2030  0.0445  27  GLU B CA  
1216 C C   . GLU B 27  ? 1.2607 1.1528 1.0784 0.1195  0.2107  0.0618  27  GLU B C   
1217 O O   . GLU B 27  ? 1.2895 1.1884 1.1053 0.1037  0.2256  0.0753  27  GLU B O   
1218 C CB  . GLU B 27  ? 1.3297 1.2368 1.1121 0.1449  0.2096  0.0303  27  GLU B CB  
1219 C CG  . GLU B 27  ? 1.3103 1.2353 1.0679 0.1543  0.2114  0.0152  27  GLU B CG  
1220 C CD  . GLU B 27  ? 1.2681 1.1889 1.0291 0.1717  0.1888  0.0044  27  GLU B CD  
1221 O OE1 . GLU B 27  ? 1.2443 1.1782 0.9849 0.1815  0.1895  -0.0087 27  GLU B OE1 
1222 N N   . LYS B 28  ? 1.3694 1.2443 1.2054 0.1231  0.2004  0.0617  28  LYS B N   
1223 C CA  . LYS B 28  ? 1.2359 1.0981 1.0923 0.1093  0.2050  0.0772  28  LYS B CA  
1224 C C   . LYS B 28  ? 1.2340 1.0815 1.1169 0.1096  0.1837  0.0856  28  LYS B C   
1225 O O   . LYS B 28  ? 1.2918 1.1419 1.1751 0.1174  0.1694  0.0814  28  LYS B O   
1226 C CB  . LYS B 28  ? 1.3510 1.2023 1.2132 0.1130  0.2055  0.0726  28  LYS B CB  
1227 C CG  . LYS B 28  ? 1.3111 1.1763 1.1472 0.1158  0.2230  0.0617  28  LYS B CG  
1228 C CE  . LYS B 28  ? 1.0226 0.8899 0.8867 0.0629  0.2551  0.0860  28  LYS B CE  
1229 N N   . GLN B 29  ? 1.0200 0.8521 0.9258 0.1006  0.1815  0.0978  29  GLN B N   
1230 C CA  . GLN B 29  ? 1.1895 1.0055 1.1225 0.1021  0.1595  0.1051  29  GLN B CA  
1231 C C   . GLN B 29  ? 1.1508 0.9586 1.0901 0.1226  0.1332  0.0908  29  GLN B C   
1232 O O   . GLN B 29  ? 1.0300 0.8366 0.9613 0.1348  0.1300  0.0772  29  GLN B O   
1233 C CB  . GLN B 29  ? 1.1408 0.9396 1.0969 0.0925  0.1598  0.1173  29  GLN B CB  
1234 C CG  . GLN B 29  ? 1.0216 0.8026 1.0070 0.0944  0.1363  0.1249  29  GLN B CG  
1235 C CD  . GLN B 29  ? 1.0486 0.8328 1.0414 0.0796  0.1405  0.1406  29  GLN B CD  
1236 O OE1 . GLN B 29  ? 1.1306 0.9135 1.1315 0.0842  0.1240  0.1412  29  GLN B OE1 
1237 N NE2 . GLN B 29  ? 1.0069 0.7955 0.9973 0.0614  0.1625  0.1534  29  GLN B NE2 
1238 N N   . LEU B 30  ? 1.2563 1.0587 1.2102 0.1262  0.1144  0.0938  30  LEU B N   
1239 C CA  . LEU B 30  ? 1.1565 0.9507 1.1186 0.1452  0.0885  0.0809  30  LEU B CA  
1240 C C   . LEU B 30  ? 1.1461 0.9202 1.1280 0.1517  0.0752  0.0794  30  LEU B C   
1241 O O   . LEU B 30  ? 1.2356 0.9973 1.2367 0.1413  0.0759  0.0926  30  LEU B O   
1242 C CB  . LEU B 30  ? 1.1187 0.9102 1.0954 0.1460  0.0712  0.0864  30  LEU B CB  
1243 C CG  . LEU B 30  ? 1.0933 0.8761 1.0812 0.1649  0.0429  0.0744  30  LEU B CG  
1244 C CD1 . LEU B 30  ? 1.0618 0.8585 1.0260 0.1789  0.0427  0.0562  30  LEU B CD1 
1245 C CD2 . LEU B 30  ? 1.0839 0.8614 1.0912 0.1623  0.0265  0.0837  30  LEU B CD2 
1246 N N   . ASP B 31  ? 1.2117 0.9829 1.1887 0.1687  0.0631  0.0631  31  ASP B N   
1247 C CA  . ASP B 31  ? 1.1340 0.8863 1.1284 0.1773  0.0485  0.0593  31  ASP B CA  
1248 C C   . ASP B 31  ? 1.0762 0.8172 1.0885 0.1916  0.0191  0.0536  31  ASP B C   
1249 O O   . ASP B 31  ? 1.1828 0.9263 1.1867 0.2076  0.0073  0.0377  31  ASP B O   
1250 C CB  . ASP B 31  ? 1.1008 0.8576 1.0768 0.1855  0.0565  0.0452  31  ASP B CB  
1251 C CG  . ASP B 31  ? 1.1573 0.8950 1.1495 0.1964  0.0394  0.0392  31  ASP B CG  
1252 O OD1 . ASP B 31  ? 1.1550 0.8755 1.1732 0.1935  0.0268  0.0491  31  ASP B OD1 
1253 O OD2 . ASP B 31  ? 1.1771 0.9171 1.1561 0.2076  0.0386  0.0246  31  ASP B OD2 
1254 N N   . LEU B 32  ? 0.7674 1.2957 1.0833 0.0641  -0.0190 0.1577  32  LEU B N   
1255 C CA  . LEU B 32  ? 0.7275 1.2767 1.0472 0.0563  -0.0246 0.1473  32  LEU B CA  
1256 C C   . LEU B 32  ? 0.7705 1.3655 1.0822 0.0585  -0.0357 0.1468  32  LEU B C   
1257 O O   . LEU B 32  ? 0.7495 1.3595 1.0533 0.0580  -0.0394 0.1411  32  LEU B O   
1258 C CB  . LEU B 32  ? 0.5530 1.1032 0.8905 0.0395  -0.0284 0.1347  32  LEU B CB  
1259 C CG  . LEU B 32  ? 0.6411 1.1555 0.9838 0.0331  -0.0199 0.1274  32  LEU B CG  
1260 C CD1 . LEU B 32  ? 0.7969 1.3236 1.1542 0.0141  -0.0260 0.1122  32  LEU B CD1 
1261 C CD2 . LEU B 32  ? 0.6883 1.1930 1.0190 0.0404  -0.0143 0.1295  32  LEU B CD2 
1262 N N   . ALA B 33  ? 0.6338 1.2513 0.9455 0.0608  -0.0416 0.1517  33  ALA B N   
1263 C CA  . ALA B 33  ? 0.7003 1.3605 1.0025 0.0623  -0.0530 0.1499  33  ALA B CA  
1264 C C   . ALA B 33  ? 0.6040 1.2648 0.8862 0.0769  -0.0500 0.1566  33  ALA B C   
1265 O O   . ALA B 33  ? 0.5615 1.2504 0.8318 0.0770  -0.0590 0.1503  33  ALA B O   
1266 C CB  . ALA B 33  ? 0.6985 1.3779 1.0045 0.0635  -0.0578 0.1553  33  ALA B CB  
1267 N N   . ALA B 34  ? 0.6598 1.2883 0.9354 0.0887  -0.0378 0.1682  34  ALA B N   
1268 C CA  . ALA B 34  ? 0.6342 1.2592 0.8900 0.1032  -0.0335 0.1760  34  ALA B CA  
1269 C C   . ALA B 34  ? 0.6261 1.2265 0.8749 0.1063  -0.0266 0.1737  34  ALA B C   
1270 O O   . ALA B 34  ? 0.7618 1.3493 0.9938 0.1186  -0.0203 0.1809  34  ALA B O   
1271 C CB  . ALA B 34  ? 0.6594 1.2629 0.9095 0.1124  -0.0243 0.1891  34  ALA B CB  
1272 N N   . LEU B 35  ? 0.5203 1.1132 0.7811 0.0951  -0.0271 0.1635  35  LEU B N   
1273 C CA  . LEU B 35  ? 0.5404 1.1056 0.7970 0.0972  -0.0188 0.1612  35  LEU B CA  
1274 C C   . LEU B 35  ? 0.4267 1.0223 0.6787 0.0921  -0.0282 0.1488  35  LEU B C   
1275 O O   . LEU B 35  ? 0.5232 1.1269 0.7755 0.0742  -0.0370 0.1329  35  LEU B O   
1276 C CB  . LEU B 35  ? 0.4619 0.9896 0.7340 0.0878  -0.0105 0.1581  35  LEU B CB  
1277 C CG  . LEU B 35  ? 0.3892 0.8849 0.6581 0.0886  -0.0009 0.1548  35  LEU B CG  
1278 C CD1 . LEU B 35  ? 0.5085 0.9769 0.7567 0.1040  0.0083  0.1656  35  LEU B CD1 
1279 C CD2 . LEU B 35  ? 0.4580 0.9172 0.7410 0.0780  0.0060  0.1499  35  LEU B CD2 
1280 N N   . ILE B 36  ? 0.3625 0.9345 0.5866 0.1006  -0.0232 0.1471  36  ILE B N   
1281 C CA  . ILE B 36  ? 0.4450 0.9899 0.6369 0.0883  -0.0255 0.1256  36  ILE B CA  
1282 C C   . ILE B 36  ? 0.4766 0.9744 0.6584 0.0931  -0.0116 0.1261  36  ILE B C   
1283 O O   . ILE B 36  ? 0.4225 0.9149 0.6025 0.1115  -0.0036 0.1421  36  ILE B O   
1284 C CB  . ILE B 36  ? 0.5054 1.0701 0.6668 0.0935  -0.0353 0.1209  36  ILE B CB  
1285 C CG1 . ILE B 36  ? 0.5274 1.1393 0.6987 0.0885  -0.0495 0.1200  36  ILE B CG1 
1286 C CG2 . ILE B 36  ? 0.5482 1.0818 0.6754 0.0813  -0.0371 0.0987  36  ILE B CG2 
1287 C CD1 . ILE B 36  ? 0.4524 1.0961 0.6096 0.1043  -0.0559 0.1299  36  ILE B CD1 
1288 N N   . VAL B 37  ? 0.3796 0.8436 0.5550 0.0766  -0.0087 0.1086  37  VAL B N   
1289 C CA  . VAL B 37  ? 0.4134 0.8301 0.5762 0.0784  0.0038  0.1056  37  VAL B CA  
1290 C C   . VAL B 37  ? 0.3535 0.7479 0.4809 0.0660  -0.0004 0.0831  37  VAL B C   
1291 O O   . VAL B 37  ? 0.4034 0.8033 0.5274 0.0478  -0.0095 0.0657  37  VAL B O   
1292 C CB  . VAL B 37  ? 0.3284 0.7202 0.5178 0.0709  0.0131  0.1065  37  VAL B CB  
1293 C CG1 . VAL B 37  ? 0.3355 0.6774 0.5091 0.0712  0.0252  0.1010  37  VAL B CG1 
1294 C CG2 . VAL B 37  ? 0.4120 0.8236 0.6350 0.0848  0.0178  0.1298  37  VAL B CG2 
1295 N N   . TYR B 38  ? 0.3653 0.7352 0.4660 0.0758  0.0058  0.0835  38  TYR B N   
1296 C CA  . TYR B 38  ? 0.4867 0.8351 0.5512 0.0660  0.0021  0.0631  38  TYR B CA  
1297 C C   . TYR B 38  ? 0.4230 0.7240 0.4728 0.0699  0.0155  0.0616  38  TYR B C   
1298 O O   . TYR B 38  ? 0.4537 0.7481 0.5020 0.0881  0.0240  0.0778  38  TYR B O   
1299 C CB  . TYR B 38  ? 0.4081 0.7832 0.4474 0.0748  -0.0076 0.0636  38  TYR B CB  
1300 C CG  . TYR B 38  ? 0.4908 0.8468 0.4924 0.0645  -0.0130 0.0422  38  TYR B CG  
1301 C CD1 . TYR B 38  ? 0.6661 1.0336 0.6610 0.0458  -0.0254 0.0234  38  TYR B CD1 
1302 C CD2 . TYR B 38  ? 0.5428 0.8693 0.5154 0.0735  -0.0058 0.0411  38  TYR B CD2 
1303 C CE1 . TYR B 38  ? 0.7324 1.0818 0.6925 0.0364  -0.0306 0.0038  38  TYR B CE1 
1304 C CE2 . TYR B 38  ? 0.4856 0.7941 0.4230 0.0644  -0.0107 0.0217  38  TYR B CE2 
1305 C CZ  . TYR B 38  ? 0.6510 0.9706 0.5820 0.0459  -0.0232 0.0029  38  TYR B CZ  
1306 O OH  . TYR B 38  ? 0.8489 1.1501 0.7441 0.0369  -0.0284 -0.0166 38  TYR B OH  
1307 N N   . TRP B 39  ? 0.4433 0.7116 0.4826 0.0529  0.0173  0.0424  39  TRP B N   
1308 C CA  . TRP B 39  ? 0.5415 0.7629 0.5645 0.0539  0.0292  0.0377  39  TRP B CA  
1309 C C   . TRP B 39  ? 0.3972 0.6019 0.3797 0.0464  0.0242  0.0184  39  TRP B C   
1310 O O   . TRP B 39  ? 0.4477 0.6567 0.4218 0.0288  0.0144  -0.0003 39  TRP B O   
1311 C CB  . TRP B 39  ? 0.5854 0.7786 0.6288 0.0403  0.0365  0.0309  39  TRP B CB  
1312 C CG  . TRP B 39  ? 0.4935 0.6877 0.5710 0.0507  0.0459  0.0506  39  TRP B CG  
1313 C CD1 . TRP B 39  ? 0.5374 0.7587 0.6489 0.0488  0.0428  0.0595  39  TRP B CD1 
1314 C CD2 . TRP B 39  ? 0.4741 0.6396 0.5553 0.0642  0.0600  0.0638  39  TRP B CD2 
1315 N NE1 . TRP B 39  ? 0.4493 0.6608 0.5850 0.0608  0.0539  0.0776  39  TRP B NE1 
1316 C CE2 . TRP B 39  ? 0.4761 0.6532 0.5940 0.0703  0.0645  0.0805  39  TRP B CE2 
1317 C CE3 . TRP B 39  ? 0.4766 0.6078 0.5334 0.0719  0.0691  0.0633  39  TRP B CE3 
1318 C CZ2 . TRP B 39  ? 0.5990 0.7544 0.7300 0.0836  0.0774  0.0964  39  TRP B CZ2 
1319 C CZ3 . TRP B 39  ? 0.5662 0.6763 0.6365 0.0850  0.0821  0.0794  39  TRP B CZ3 
1320 C CH2 . TRP B 39  ? 0.5803 0.7024 0.6874 0.0907  0.0860  0.0956  39  TRP B CH2 
1321 N N   . GLU B 40  ? 0.4887 0.6727 0.4468 0.0596  0.0312  0.0229  40  GLU B N   
1322 C CA  . GLU B 40  ? 0.4615 0.6256 0.3793 0.0547  0.0281  0.0058  40  GLU B CA  
1323 C C   . GLU B 40  ? 0.6232 0.7436 0.5257 0.0621  0.0421  0.0078  40  GLU B C   
1324 O O   . GLU B 40  ? 0.5750 0.6877 0.4945 0.0759  0.0529  0.0257  40  GLU B O   
1325 C CB  . GLU B 40  ? 0.4628 0.6588 0.3592 0.0649  0.0177  0.0089  40  GLU B CB  
1326 C CG  . GLU B 40  ? 0.6422 0.8514 0.5400 0.0895  0.0235  0.0320  40  GLU B CG  
1327 C CD  . GLU B 40  ? 0.8875 1.0681 0.7514 0.1001  0.0304  0.0314  40  GLU B CD  
1328 O OE1 . GLU B 40  ? 0.9067 1.0587 0.7438 0.0886  0.0299  0.0123  40  GLU B OE1 
1329 O OE2 . GLU B 40  ? 0.8563 1.0437 0.7201 0.1202  0.0362  0.0501  40  GLU B OE2 
1330 N N   . MET B 41  ? 0.5983 0.6892 0.4688 0.0525  0.0418  -0.0111 41  MET B N   
1331 C CA  . MET B 41  ? 0.5814 0.6312 0.4317 0.0595  0.0541  -0.0109 41  MET B CA  
1332 C C   . MET B 41  ? 0.6394 0.6821 0.4468 0.0605  0.0486  -0.0231 41  MET B C   
1333 O O   . MET B 41  ? 0.6647 0.7098 0.4552 0.0450  0.0383  -0.0426 41  MET B O   
1334 C CB  . MET B 41  ? 0.5496 0.5593 0.4071 0.0447  0.0627  -0.0228 41  MET B CB  
1335 C CG  . MET B 41  ? 0.8410 0.8070 0.6794 0.0517  0.0760  -0.0222 41  MET B CG  
1336 S SD  . MET B 41  ? 0.8759 0.8127 0.6649 0.0425  0.0729  -0.0459 41  MET B SD  
1337 C CE  . MET B 41  ? 0.7146 0.6576 0.5069 0.0154  0.0607  -0.0703 41  MET B CE  
1338 N N   . GLU B 42  ? 0.7481 0.7812 0.5378 0.0786  0.0556  -0.0115 42  GLU B N   
1339 C CA  . GLU B 42  ? 0.8751 0.9084 0.6250 0.0832  0.0497  -0.0194 42  GLU B CA  
1340 C C   . GLU B 42  ? 0.9930 1.0721 0.7440 0.0825  0.0343  -0.0200 42  GLU B C   
1341 O O   . GLU B 42  ? 1.1791 1.2901 0.9472 0.0971  0.0332  -0.0012 42  GLU B O   
1342 C CB  . GLU B 42  ? 0.9545 0.9487 0.6750 0.0682  0.0508  -0.0425 42  GLU B CB  
1343 C CG  . GLU B 42  ? 0.8919 0.8459 0.6008 0.0783  0.0662  -0.0363 42  GLU B CG  
1344 C CD  . GLU B 42  ? 1.0215 0.9310 0.7170 0.0625  0.0721  -0.0553 42  GLU B CD  
1345 O OE1 . GLU B 42  ? 1.1782 1.0571 0.8812 0.0671  0.0858  -0.0485 42  GLU B OE1 
1346 O OE2 . GLU B 42  ? 1.1450 1.0497 0.8227 0.0456  0.0633  -0.0766 42  GLU B OE2 
1347 N N   . ASP B 43  ? 0.7370 0.8213 0.4709 0.0663  0.0223  -0.0405 43  ASP B N   
1348 C CA  . ASP B 43  ? 0.9423 1.0715 0.6851 0.0637  0.0078  -0.0403 43  ASP B CA  
1349 C C   . ASP B 43  ? 0.9504 1.0820 0.7015 0.0397  -0.0015 -0.0597 43  ASP B C   
1350 O O   . ASP B 43  ? 0.9949 1.1446 0.7304 0.0305  -0.0151 -0.0730 43  ASP B O   
1351 C CB  . ASP B 43  ? 0.9115 1.0582 0.6217 0.0745  -0.0007 -0.0407 43  ASP B CB  
1352 C CG  . ASP B 43  ? 0.9463 1.1242 0.6688 0.0969  0.0010  -0.0165 43  ASP B CG  
1353 O OD1 . ASP B 43  ? 1.0248 1.2368 0.7776 0.0979  -0.0036 -0.0062 43  ASP B OD1 
1354 O OD2 . ASP B 43  ? 1.2047 1.3722 0.9075 0.1137  0.0074  -0.0071 43  ASP B OD2 
1355 N N   . LYS B 44  ? 0.7628 0.8752 0.5388 0.0293  0.0061  -0.0614 44  LYS B N   
1356 C CA  . LYS B 44  ? 0.7153 0.8299 0.5061 0.0072  -0.0007 -0.0771 44  LYS B CA  
1357 C C   . LYS B 44  ? 0.7737 0.9193 0.6072 0.0084  -0.0015 -0.0626 44  LYS B C   
1358 O O   . LYS B 44  ? 0.7714 0.9114 0.6279 0.0195  0.0097  -0.0455 44  LYS B O   
1359 C CB  . LYS B 44  ? 0.7471 0.8157 0.5346 -0.0059 0.0088  -0.0904 44  LYS B CB  
1360 C CG  . LYS B 44  ? 0.7031 0.7359 0.4502 -0.0048 0.0128  -0.1020 44  LYS B CG  
1361 C CD  . LYS B 44  ? 0.6766 0.6639 0.4270 -0.0104 0.0268  -0.1065 44  LYS B CD  
1362 C CE  . LYS B 44  ? 0.9417 0.8923 0.6518 -0.0159 0.0285  -0.1240 44  LYS B CE  
1363 N NZ  . LYS B 44  ? 1.0658 1.0096 0.7500 0.0039  0.0337  -0.1136 44  LYS B NZ  
1364 N N   . ASN B 45  ? 0.5405 0.7184 0.3847 -0.0028 -0.0148 -0.0692 45  ASN B N   
1365 C CA  . ASN B 45  ? 0.5059 0.7116 0.3909 -0.0041 -0.0158 -0.0575 45  ASN B CA  
1366 C C   . ASN B 45  ? 0.5523 0.7312 0.4587 -0.0185 -0.0082 -0.0642 45  ASN B C   
1367 O O   . ASN B 45  ? 0.5551 0.7201 0.4538 -0.0379 -0.0132 -0.0842 45  ASN B O   
1368 C CB  . ASN B 45  ? 0.5178 0.7652 0.4084 -0.0126 -0.0322 -0.0629 45  ASN B CB  
1369 C CG  . ASN B 45  ? 0.8028 1.0736 0.7353 -0.0187 -0.0333 -0.0550 45  ASN B CG  
1370 O OD1 . ASN B 45  ? 0.9220 1.2187 0.8776 -0.0049 -0.0312 -0.0352 45  ASN B OD1 
1371 N ND2 . ASN B 45  ? 0.8140 1.0745 0.7564 -0.0391 -0.0361 -0.0703 45  ASN B ND2 
1372 N N   . ILE B 46  ? 0.5502 0.7215 0.4835 -0.0091 0.0036  -0.0478 46  ILE B N   
1373 C CA  . ILE B 46  ? 0.5135 0.6636 0.4710 -0.0219 0.0104  -0.0524 46  ILE B CA  
1374 C C   . ILE B 46  ? 0.5977 0.7825 0.5901 -0.0287 0.0035  -0.0474 46  ILE B C   
1375 O O   . ILE B 46  ? 0.6413 0.8222 0.6436 -0.0473 -0.0006 -0.0613 46  ILE B O   
1376 C CB  . ILE B 46  ? 0.6429 0.7629 0.6112 -0.0095 0.0270  -0.0385 46  ILE B CB  
1377 C CG1 . ILE B 46  ? 0.5403 0.6255 0.4734 -0.0032 0.0339  -0.0438 46  ILE B CG1 
1378 C CG2 . ILE B 46  ? 0.4492 0.5470 0.4425 -0.0226 0.0339  -0.0436 46  ILE B CG2 
1379 C CD1 . ILE B 46  ? 0.5003 0.5660 0.4407 0.0147  0.0484  -0.0255 46  ILE B CD1 
1380 N N   . ILE B 47  ? 0.5416 0.7612 0.5535 -0.0139 0.0019  -0.0275 47  ILE B N   
1381 C CA  . ILE B 47  ? 0.6240 0.8767 0.6695 -0.0200 -0.0044 -0.0221 47  ILE B CA  
1382 C C   . ILE B 47  ? 0.4311 0.7288 0.4846 -0.0049 -0.0113 -0.0052 47  ILE B C   
1383 O O   . ILE B 47  ? 0.6278 0.9273 0.6742 0.0140  -0.0060 0.0097  47  ILE B O   
1384 C CB  . ILE B 47  ? 0.7076 0.9432 0.7860 -0.0209 0.0071  -0.0136 47  ILE B CB  
1385 C CG1 . ILE B 47  ? 0.8462 1.1000 0.9499 -0.0379 -0.0002 -0.0208 47  ILE B CG1 
1386 C CG2 . ILE B 47  ? 0.6226 0.8708 0.7212 0.0003  0.0148  0.0119  47  ILE B CG2 
1387 C CD1 . ILE B 47  ? 0.8399 1.0644 0.9313 -0.0590 -0.0013 -0.0442 47  ILE B CD1 
1388 N N   . GLN B 48  ? 0.4625 0.7966 0.5308 -0.0135 -0.0232 -0.0077 48  GLN B N   
1389 C CA  . GLN B 48  ? 0.6246 1.0044 0.7032 -0.0012 -0.0308 0.0075  48  GLN B CA  
1390 C C   . GLN B 48  ? 0.7128 1.1205 0.8292 -0.0075 -0.0344 0.0141  48  GLN B C   
1391 O O   . GLN B 48  ? 0.6832 1.0991 0.8050 -0.0257 -0.0430 -0.0001 48  GLN B O   
1392 C CB  . GLN B 48  ? 0.6293 1.0313 0.6801 -0.0042 -0.0449 -0.0034 48  GLN B CB  
1393 C CG  . GLN B 48  ? 0.7276 1.1796 0.7918 0.0057  -0.0541 0.0104  48  GLN B CG  
1394 C CD  . GLN B 48  ? 0.7960 1.2662 0.8290 0.0106  -0.0648 0.0052  48  GLN B CD  
1395 O OE1 . GLN B 48  ? 0.9684 1.4382 0.9815 -0.0039 -0.0751 -0.0137 48  GLN B OE1 
1396 N NE2 . GLN B 48  ? 0.9794 1.4655 1.0077 0.0313  -0.0625 0.0222  48  GLN B NE2 
1397 N N   . PHE B 49  ? 0.5475 0.9693 0.6899 0.0075  -0.0279 0.0357  49  PHE B N   
1398 C CA  . PHE B 49  ? 0.4912 0.9412 0.6703 0.0048  -0.0304 0.0452  49  PHE B CA  
1399 C C   . PHE B 49  ? 0.4550 0.9513 0.6395 0.0182  -0.0385 0.0599  49  PHE B C   
1400 O O   . PHE B 49  ? 0.5442 1.0460 0.7302 0.0377  -0.0325 0.0778  49  PHE B O   
1401 C CB  . PHE B 49  ? 0.4538 0.8827 0.6593 0.0114  -0.0165 0.0586  49  PHE B CB  
1402 C CG  . PHE B 49  ? 0.4843 0.9377 0.7273 0.0075  -0.0183 0.0672  49  PHE B CG  
1403 C CD1 . PHE B 49  ? 0.6456 1.0926 0.9015 -0.0120 -0.0210 0.0535  49  PHE B CD1 
1404 C CD2 . PHE B 49  ? 0.5069 0.9894 0.7725 0.0237  -0.0170 0.0892  49  PHE B CD2 
1405 C CE1 . PHE B 49  ? 0.6332 1.1026 0.9234 -0.0152 -0.0225 0.0617  49  PHE B CE1 
1406 C CE2 . PHE B 49  ? 0.5412 1.0458 0.8407 0.0206  -0.0186 0.0973  49  PHE B CE2 
1407 C CZ  . PHE B 49  ? 0.6325 1.1305 0.9443 0.0012  -0.0212 0.0837  49  PHE B CZ  
1408 N N   . VAL B 50  ? 0.5984 0.7615 0.9022 0.1098  0.0689  -0.0896 50  VAL B N   
1409 C CA  . VAL B 50  ? 0.6657 0.8528 1.0343 0.1164  0.0468  -0.0962 50  VAL B CA  
1410 C C   . VAL B 50  ? 0.7660 1.0019 1.1916 0.1090  0.0672  -0.1095 50  VAL B C   
1411 O O   . VAL B 50  ? 0.7491 0.9944 1.1616 0.0939  0.0937  -0.1080 50  VAL B O   
1412 C CB  . VAL B 50  ? 0.6753 0.8410 1.0436 0.1060  0.0206  -0.0793 50  VAL B CB  
1413 C CG1 . VAL B 50  ? 0.8202 0.9768 1.1619 0.0813  0.0355  -0.0649 50  VAL B CG1 
1414 C CG2 . VAL B 50  ? 0.6222 0.8177 1.0620 0.1100  0.0011  -0.0866 50  VAL B CG2 
1415 N N   . HIS B 51  ? 0.5743 0.8415 1.0631 0.1202  0.0551  -0.1228 51  HIS B N   
1416 C CA  . HIS B 51  ? 0.8688 1.1844 1.4165 0.1151  0.0728  -0.1368 51  HIS B CA  
1417 C C   . HIS B 51  ? 0.7851 1.1159 1.3159 0.1153  0.1067  -0.1474 51  HIS B C   
1418 O O   . HIS B 51  ? 0.8156 1.1758 1.3692 0.1027  0.1301  -0.1526 51  HIS B O   
1419 C CB  . HIS B 51  ? 0.7536 1.0798 1.3242 0.0929  0.0732  -0.1268 51  HIS B CB  
1420 C CG  . HIS B 51  ? 1.0566 1.3828 1.5965 0.0731  0.1026  -0.1205 51  HIS B CG  
1421 N ND1 . HIS B 51  ? 0.9682 1.3324 1.5380 0.0665  0.1304  -0.1326 51  HIS B ND1 
1422 C CD2 . HIS B 51  ? 1.0071 1.3005 1.4906 0.0579  0.1082  -0.1032 51  HIS B CD2 
1423 C CE1 . HIS B 51  ? 1.0258 1.3803 1.5581 0.0485  0.1521  -0.1230 51  HIS B CE1 
1424 N NE2 . HIS B 51  ? 1.0428 1.3544 1.5223 0.0429  0.1392  -0.1052 51  HIS B NE2 
1425 N N   . GLY B 52  ? 0.7291 1.0401 1.2203 0.1305  0.1092  -0.1511 52  GLY B N   
1426 C CA  . GLY B 52  ? 0.8398 1.1604 1.3083 0.1323  0.1398  -0.1605 52  GLY B CA  
1427 C C   . GLY B 52  ? 0.8711 1.1821 1.2995 0.1112  0.1642  -0.1496 52  GLY B C   
1428 O O   . GLY B 52  ? 0.8242 1.1536 1.2478 0.1079  0.1933  -0.1582 52  GLY B O   
1429 N N   . GLU B 53  ? 0.8282 1.1106 1.2273 0.0965  0.1534  -0.1308 53  GLU B N   
1430 C CA  . GLU B 53  ? 0.9382 1.2097 1.2968 0.0763  0.1764  -0.1199 53  GLU B CA  
1431 C C   . GLU B 53  ? 0.8080 1.0307 1.1058 0.0689  0.1625  -0.0991 53  GLU B C   
1432 O O   . GLU B 53  ? 0.6750 0.8791 0.9769 0.0705  0.1341  -0.0897 53  GLU B O   
1433 C CB  . GLU B 53  ? 0.9903 1.2953 1.3925 0.0574  0.1898  -0.1208 53  GLU B CB  
1434 C CG  . GLU B 53  ? 0.9952 1.3029 1.3637 0.0427  0.2240  -0.1189 53  GLU B CG  
1435 C CD  . GLU B 53  ? 1.1181 1.4681 1.5352 0.0287  0.2442  -0.1264 53  GLU B CD  
1436 O OE1 . GLU B 53  ? 1.1429 1.5303 1.6180 0.0381  0.2445  -0.1428 53  GLU B OE1 
1437 O OE2 . GLU B 53  ? 1.2405 1.5864 1.6376 0.0084  0.2598  -0.1161 53  GLU B OE2 
1438 N N   . GLU B 54  ? 0.8745 1.0782 1.1166 0.0606  0.1843  -0.0927 54  GLU B N   
1439 C CA  . GLU B 54  ? 0.9652 1.1237 1.1393 0.0510  0.1817  -0.0738 54  GLU B CA  
1440 C C   . GLU B 54  ? 0.9130 1.0657 1.0914 0.0292  0.1755  -0.0582 54  GLU B C   
1441 O O   . GLU B 54  ? 1.0651 1.2406 1.2608 0.0126  0.1957  -0.0585 54  GLU B O   
1442 C CB  . GLU B 54  ? 1.1130 1.2712 1.2478 0.0521  0.2128  -0.0799 54  GLU B CB  
1443 C CG  . GLU B 54  ? 1.2139 1.3295 1.2719 0.0566  0.2173  -0.0712 54  GLU B CG  
1444 C CD  . GLU B 54  ? 1.3269 1.4114 1.3291 0.0379  0.2257  -0.0529 54  GLU B CD  
1445 O OE1 . GLU B 54  ? 1.3863 1.4307 1.3377 0.0337  0.2147  -0.0372 54  GLU B OE1 
1446 O OE2 . GLU B 54  ? 1.1253 1.2206 1.1101 0.0345  0.2548  -0.0591 54  GLU B OE2 
1447 N N   . ASP B 55  ? 0.8971 1.0201 1.0629 0.0299  0.1459  -0.0450 55  ASP B N   
1448 C CA  . ASP B 55  ? 0.7897 0.9068 0.9668 0.0122  0.1330  -0.0307 55  ASP B CA  
1449 C C   . ASP B 55  ? 0.9082 0.9816 1.0168 -0.0009 0.1335  -0.0108 55  ASP B C   
1450 O O   . ASP B 55  ? 1.0453 1.0816 1.1147 0.0072  0.1138  -0.0016 55  ASP B O   
1451 C CB  . ASP B 55  ? 0.8191 0.9364 1.0356 0.0218  0.0987  -0.0302 55  ASP B CB  
1452 C CG  . ASP B 55  ? 0.9628 1.0776 1.1968 0.0037  0.0852  -0.0166 55  ASP B CG  
1453 O OD1 . ASP B 55  ? 1.0067 1.1051 1.2054 -0.0149 0.0964  -0.0030 55  ASP B OD1 
1454 O OD2 . ASP B 55  ? 1.0817 1.2107 1.3649 0.0082  0.0628  -0.0192 55  ASP B OD2 
1455 N N   . LEU B 56  ? 0.8990 0.9770 0.9946 -0.0214 0.1552  -0.0039 56  LEU B N   
1456 C CA  . LEU B 56  ? 0.8126 0.8524 0.8403 -0.0343 0.1627  0.0131  56  LEU B CA  
1457 C C   . LEU B 56  ? 0.8274 0.8456 0.8467 -0.0499 0.1442  0.0315  56  LEU B C   
1458 O O   . LEU B 56  ? 0.9579 0.9389 0.9187 -0.0585 0.1442  0.0469  56  LEU B O   
1459 C CB  . LEU B 56  ? 0.9984 1.0535 1.0110 -0.0480 0.1988  0.0105  56  LEU B CB  
1460 C CG  . LEU B 56  ? 0.8818 0.9508 0.8864 -0.0345 0.2206  -0.0051 56  LEU B CG  
1461 C CD1 . LEU B 56  ? 0.9305 0.9630 0.8841 -0.0177 0.2095  -0.0028 56  LEU B CD1 
1462 C CD2 . LEU B 56  ? 0.9663 1.0811 1.0407 -0.0230 0.2222  -0.0251 56  LEU B CD2 
1463 N N   . LYS B 57  ? 0.8210 0.8611 0.8965 -0.0538 0.1284  0.0304  57  LYS B N   
1464 C CA  . LYS B 57  ? 0.8727 0.8971 0.9434 -0.0715 0.1153  0.0475  57  LYS B CA  
1465 C C   . LYS B 57  ? 0.7361 0.7148 0.7641 -0.0665 0.0875  0.0622  57  LYS B C   
1466 O O   . LYS B 57  ? 0.8445 0.7983 0.8426 -0.0819 0.0821  0.0791  57  LYS B O   
1467 C CB  . LYS B 57  ? 0.9994 1.0602 1.1425 -0.0767 0.1060  0.0418  57  LYS B CB  
1468 C CG  . LYS B 57  ? 0.8562 0.9320 1.0485 -0.0579 0.0812  0.0311  57  LYS B CG  
1469 C CD  . LYS B 57  ? 0.8204 0.9408 1.0859 -0.0643 0.0826  0.0219  57  LYS B CD  
1470 C CE  . LYS B 57  ? 0.8304 0.9708 1.1505 -0.0460 0.0601  0.0096  57  LYS B CE  
1471 N NZ  . LYS B 57  ? 0.9711 1.1342 1.3480 -0.0551 0.0461  0.0110  57  LYS B NZ  
1472 N N   . VAL B 58  ? 0.7883 0.7558 0.8141 -0.0453 0.0691  0.0562  58  VAL B N   
1473 C CA  . VAL B 58  ? 0.8035 0.7262 0.7841 -0.0398 0.0442  0.0700  58  VAL B CA  
1474 C C   . VAL B 58  ? 0.7932 0.6819 0.7024 -0.0357 0.0563  0.0748  58  VAL B C   
1475 O O   . VAL B 58  ? 0.8149 0.6643 0.6808 -0.0308 0.0377  0.0861  58  VAL B O   
1476 C CB  . VAL B 58  ? 0.7990 0.7235 0.8128 -0.0198 0.0145  0.0630  58  VAL B CB  
1477 C CG1 . VAL B 58  ? 0.8403 0.7744 0.8554 0.0014  0.0217  0.0467  58  VAL B CG1 
1478 C CG2 . VAL B 58  ? 0.9959 0.8768 0.9720 -0.0182 -0.0140 0.0793  58  VAL B CG2 
1479 N N   . GLN B 59  ? 0.8059 0.7083 0.7013 -0.0373 0.0868  0.0666  59  GLN B N   
1480 C CA  . GLN B 59  ? 0.8288 0.7017 0.6592 -0.0317 0.0991  0.0693  59  GLN B CA  
1481 C C   . GLN B 59  ? 0.7909 0.6224 0.5590 -0.0468 0.0981  0.0897  59  GLN B C   
1482 O O   . GLN B 59  ? 0.9805 0.8155 0.7480 -0.0672 0.1083  0.0989  59  GLN B O   
1483 C CB  . GLN B 59  ? 0.8692 0.7684 0.7015 -0.0322 0.1333  0.0563  59  GLN B CB  
1484 C CG  . GLN B 59  ? 0.9569 0.8269 0.7212 -0.0284 0.1489  0.0594  59  GLN B CG  
1485 C CD  . GLN B 59  ? 0.9530 0.8492 0.7190 -0.0304 0.1833  0.0473  59  GLN B CD  
1486 O OE1 . GLN B 59  ? 1.1515 1.0400 0.8824 -0.0457 0.2054  0.0546  59  GLN B OE1 
1487 N NE2 . GLN B 59  ? 1.0050 0.9325 0.8117 -0.0148 0.1881  0.0287  59  GLN B NE2 
1488 N N   . HIS B 60  ? 0.9020 0.6943 0.6174 -0.0366 0.0862  0.0967  60  HIS B N   
1489 C CA  . HIS B 60  ? 0.9119 0.6614 0.5654 -0.0487 0.0823  0.1161  60  HIS B CA  
1490 C C   . HIS B 60  ? 0.9403 0.6879 0.5553 -0.0633 0.1149  0.1195  60  HIS B C   
1491 O O   . HIS B 60  ? 1.0435 0.8063 0.6540 -0.0567 0.1377  0.1075  60  HIS B O   
1492 C CB  . HIS B 60  ? 1.0330 0.7440 0.6413 -0.0321 0.0633  0.1203  60  HIS B CB  
1493 C CG  . HIS B 60  ? 0.9877 0.6572 0.5392 -0.0417 0.0544  0.1386  60  HIS B CG  
1494 N ND1 . HIS B 60  ? 1.0927 0.7817 0.6421 -0.0463 0.0681  0.1324  60  HIS B ND1 
1495 C CD2 . HIS B 60  ? 1.0311 0.7111 0.6178 -0.0380 0.0239  0.1378  60  HIS B CD2 
1496 C CE1 . HIS B 60  ? 0.8948 0.6004 0.4733 -0.0448 0.0479  0.1296  60  HIS B CE1 
1497 N NE2 . HIS B 60  ? 0.9748 0.6782 0.5763 -0.0401 0.0247  0.1313  60  HIS B NE2 
1498 N N   . SER B 61  ? 0.9887 0.5584 0.6806 -0.1187 -0.1492 -0.1115 61  SER B N   
1499 C CA  . SER B 61  ? 0.9705 0.5599 0.6813 -0.1515 -0.1357 -0.1033 61  SER B CA  
1500 C C   . SER B 61  ? 1.1433 0.7181 0.8507 -0.1407 -0.1059 -0.0945 61  SER B C   
1501 O O   . SER B 61  ? 0.9914 0.6153 0.7345 -0.1538 -0.0919 -0.0884 61  SER B O   
1502 C CB  . SER B 61  ? 1.0364 0.5725 0.7143 -0.1869 -0.1449 -0.1024 61  SER B CB  
1503 O OG  . SER B 61  ? 1.2669 0.7152 0.8909 -0.1817 -0.1338 -0.0990 61  SER B OG  
1504 N N   . SER B 62  ? 1.0381 0.5457 0.7024 -0.1172 -0.0959 -0.0936 62  SER B N   
1505 C CA  . SER B 62  ? 1.1134 0.5998 0.7694 -0.1086 -0.0676 -0.0848 62  SER B CA  
1506 C C   . SER B 62  ? 1.0463 0.6008 0.7464 -0.0863 -0.0540 -0.0832 62  SER B C   
1507 O O   . SER B 62  ? 0.9785 0.5326 0.6831 -0.0841 -0.0300 -0.0753 62  SER B O   
1508 C CB  . SER B 62  ? 1.1367 0.5388 0.7374 -0.0859 -0.0612 -0.0846 62  SER B CB  
1509 O OG  . SER B 62  ? 1.1486 0.5590 0.7494 -0.0484 -0.0674 -0.0911 62  SER B OG  
1510 N N   . TYR B 63  ? 0.9844 0.5978 0.7173 -0.0702 -0.0687 -0.0903 63  TYR B N   
1511 C CA  . TYR B 63  ? 0.9927 0.6719 0.7673 -0.0470 -0.0576 -0.0895 63  TYR B CA  
1512 C C   . TYR B 63  ? 0.9418 0.7088 0.7729 -0.0662 -0.0637 -0.0895 63  TYR B C   
1513 O O   . TYR B 63  ? 0.9417 0.7705 0.8117 -0.0492 -0.0555 -0.0889 63  TYR B O   
1514 C CB  . TYR B 63  ? 0.8424 0.5205 0.6097 -0.0079 -0.0673 -0.0974 63  TYR B CB  
1515 C CG  . TYR B 63  ? 0.9582 0.5635 0.6790 0.0171  -0.0547 -0.0958 63  TYR B CG  
1516 C CD1 . TYR B 63  ? 0.7821 0.3897 0.5070 0.0358  -0.0301 -0.0899 63  TYR B CD1 
1517 C CD2 . TYR B 63  ? 1.0047 0.5380 0.6765 0.0209  -0.0672 -0.1000 63  TYR B CD2 
1518 C CE1 . TYR B 63  ? 1.0679 0.6093 0.7499 0.0582  -0.0185 -0.0881 63  TYR B CE1 
1519 C CE2 . TYR B 63  ? 0.9227 0.3968 0.5561 0.0430  -0.0551 -0.0965 63  TYR B CE2 
1520 C CZ  . TYR B 63  ? 0.9673 0.4724 0.6224 0.0582  -0.0298 -0.0851 63  TYR B CZ  
1521 O OH  . TYR B 63  ? 0.9029 0.4409 0.5735 0.0661  -0.0170 -0.0652 63  TYR B OH  
1522 N N   . ARG B 64  ? 0.9939 0.7679 0.8300 -0.1010 -0.0781 -0.0901 64  ARG B N   
1523 C CA  . ARG B 64  ? 1.0764 0.9343 0.9660 -0.1210 -0.0842 -0.0897 64  ARG B CA  
1524 C C   . ARG B 64  ? 0.9884 0.8762 0.9038 -0.1337 -0.0601 -0.0803 64  ARG B C   
1525 O O   . ARG B 64  ? 0.8416 0.6785 0.7300 -0.1420 -0.0419 -0.0733 64  ARG B O   
1526 C CB  . ARG B 64  ? 1.0782 0.9345 0.9656 -0.1566 -0.1047 -0.0922 64  ARG B CB  
1527 C CG  . ARG B 64  ? 1.2517 1.0561 1.1119 -0.1897 -0.0953 -0.0854 64  ARG B CG  
1528 C CD  . ARG B 64  ? 1.2879 1.0581 1.1237 -0.2163 -0.1177 -0.0898 64  ARG B CD  
1529 N NE  . ARG B 64  ? 1.2341 1.0579 1.1053 -0.2524 -0.1246 -0.0878 64  ARG B NE  
1530 N N   . GLN B 65  ? 0.8887 0.8580 0.8550 -0.1281 -0.0590 -0.0804 65  GLN B N   
1531 C CA  . GLN B 65  ? 0.8766 0.9002 0.8823 -0.1309 -0.0376 -0.0729 65  GLN B CA  
1532 C C   . GLN B 65  ? 0.8747 0.8698 0.8650 -0.1028 -0.0129 -0.0684 65  GLN B C   
1533 O O   . GLN B 65  ? 0.9105 0.9171 0.9141 -0.1127 0.0095  -0.0598 65  GLN B O   
1534 C CB  . GLN B 65  ? 0.9846 1.0111 0.9987 -0.1660 -0.0256 -0.0647 65  GLN B CB  
1535 C CG  . GLN B 65  ? 1.1743 1.2349 1.2112 -0.2038 -0.0361 -0.0634 65  GLN B CG  
1536 C CD  . GLN B 65  ? 1.3491 1.4855 1.4293 -0.2126 -0.0565 -0.0684 65  GLN B CD  
1537 O OE1 . GLN B 65  ? 1.3967 1.5990 1.5158 -0.1920 -0.0562 -0.0703 65  GLN B OE1 
1538 N NE2 . GLN B 65  ? 1.4481 1.5834 1.5269 -0.2484 -0.0735 -0.0696 65  GLN B NE2 
1539 N N   . ARG B 66  ? 0.6650 0.6141 0.6225 -0.0726 -0.0146 -0.0727 66  ARG B N   
1540 C CA  . ARG B 66  ? 0.7386 0.6559 0.6780 -0.0477 0.0084  -0.0683 66  ARG B CA  
1541 C C   . ARG B 66  ? 0.6813 0.6108 0.6231 -0.0059 0.0074  -0.0738 66  ARG B C   
1542 O O   . ARG B 66  ? 0.6300 0.5486 0.5664 0.0154  0.0278  -0.0699 66  ARG B O   
1543 C CB  . ARG B 66  ? 0.7389 0.5613 0.6203 -0.0541 0.0148  -0.0652 66  ARG B CB  
1544 C CG  . ARG B 66  ? 0.7920 0.5954 0.6683 -0.0886 0.0288  -0.0562 66  ARG B CG  
1545 C CD  . ARG B 66  ? 0.8293 0.5451 0.6524 -0.0864 0.0438  -0.0510 66  ARG B CD  
1546 N NE  . ARG B 66  ? 0.8603 0.5111 0.6374 -0.0747 0.0283  -0.0573 66  ARG B NE  
1547 C CZ  . ARG B 66  ? 0.9280 0.5317 0.6723 -0.0436 0.0340  -0.0587 66  ARG B CZ  
1548 N NH1 . ARG B 66  ? 0.7220 0.3289 0.4697 -0.0218 0.0561  -0.0539 66  ARG B NH1 
1549 N NH2 . ARG B 66  ? 0.9059 0.4559 0.6115 -0.0349 0.0174  -0.0649 66  ARG B NH2 
1550 N N   . ALA B 67  ? 0.6123 0.5639 0.5618 0.0062  -0.0150 -0.0826 67  ALA B N   
1551 C CA  . ALA B 67  ? 0.5915 0.5490 0.5390 0.0460  -0.0181 -0.0886 67  ALA B CA  
1552 C C   . ALA B 67  ? 0.5694 0.6172 0.5704 0.0548  -0.0268 -0.0925 67  ALA B C   
1553 O O   . ALA B 67  ? 0.6210 0.7122 0.6484 0.0324  -0.0431 -0.0947 67  ALA B O   
1554 C CB  . ALA B 67  ? 0.6199 0.5185 0.5250 0.0565  -0.0377 -0.0962 67  ALA B CB  
1555 N N   . ARG B 68  ? 0.5343 0.6108 0.5515 0.0870  -0.0154 -0.0929 68  ARG B N   
1556 C CA  . ARG B 68  ? 0.5376 0.6947 0.6010 0.1010  -0.0246 -0.0974 68  ARG B CA  
1557 C C   . ARG B 68  ? 0.6612 0.8136 0.7164 0.1442  -0.0219 -0.1021 68  ARG B C   
1558 O O   . ARG B 68  ? 0.5552 0.6568 0.5795 0.1626  -0.0061 -0.0997 68  ARG B O   
1559 C CB  . ARG B 68  ? 0.5541 0.7829 0.6670 0.0868  -0.0102 -0.0908 68  ARG B CB  
1560 C CG  . ARG B 68  ? 0.8311 1.0506 0.9429 0.0977  0.0187  -0.0833 68  ARG B CG  
1561 C CD  . ARG B 68  ? 0.7570 1.0429 0.9155 0.0766  0.0311  -0.0764 68  ARG B CD  
1562 N NE  . ARG B 68  ? 0.8470 1.2152 1.0533 0.0749  0.0163  -0.0803 68  ARG B NE  
1563 C CZ  . ARG B 68  ? 0.9755 1.3907 1.2059 0.1051  0.0135  -0.0848 68  ARG B CZ  
1564 N NH1 . ARG B 68  ? 0.9340 1.3311 1.1516 0.1383  0.0276  -0.0851 68  ARG B NH1 
1565 N NH2 . ARG B 68  ? 1.0758 1.5604 1.3456 0.1013  -0.0028 -0.0886 68  ARG B NH2 
1566 N N   . LEU B 69  ? 0.5768 0.7815 0.6586 0.1598  -0.0382 -0.1090 69  LEU B N   
1567 C CA  . LEU B 69  ? 0.5297 0.7439 0.6119 0.2006  -0.0370 -0.1139 69  LEU B CA  
1568 C C   . LEU B 69  ? 0.6943 0.9831 0.8240 0.2115  -0.0220 -0.1104 69  LEU B C   
1569 O O   . LEU B 69  ? 0.7021 1.0580 0.8747 0.1930  -0.0266 -0.1090 69  LEU B O   
1570 C CB  . LEU B 69  ? 0.6535 0.8792 0.7352 0.2125  -0.0638 -0.1234 69  LEU B CB  
1571 C CG  . LEU B 69  ? 0.6238 0.8274 0.6852 0.2538  -0.0666 -0.1298 69  LEU B CG  
1572 C CD1 . LEU B 69  ? 0.9125 1.1747 1.0087 0.2809  -0.0535 -0.1291 69  LEU B CD1 
1573 C CD2 . LEU B 69  ? 0.7399 0.8536 0.7468 0.2634  -0.0562 -0.1282 69  LEU B CD2 
1574 N N   . LEU B 70  ? 0.5878 0.8651 0.7097 0.2409  -0.0042 -0.1090 70  LEU B N   
1575 C CA  . LEU B 70  ? 0.7020 1.0447 0.8653 0.2531  0.0108  -0.1054 70  LEU B CA  
1576 C C   . LEU B 70  ? 0.7089 1.0821 0.8848 0.2603  -0.0050 -0.1065 70  LEU B C   
1577 O O   . LEU B 70  ? 0.8847 1.2072 1.0258 0.2645  -0.0066 -0.1014 70  LEU B O   
1578 C CB  . LEU B 70  ? 0.7216 0.9929 0.8480 0.2418  0.0315  -0.0890 70  LEU B CB  
1579 C CG  . LEU B 70  ? 0.7717 0.9907 0.8714 0.2328  0.0470  -0.0855 70  LEU B CG  
1580 C CD1 . LEU B 70  ? 0.6150 0.8038 0.7098 0.2133  0.0654  -0.0700 70  LEU B CD1 
1581 C CD2 . LEU B 70  ? 0.7966 1.0497 0.9178 0.2154  0.0478  -0.0899 70  LEU B CD2 
1582 N N   . LYS B 71  ? 0.6965 1.1556 0.9240 0.2564  -0.0165 -0.1120 71  LYS B N   
1583 C CA  . LYS B 71  ? 0.7529 1.2412 0.9913 0.2637  -0.0343 -0.1155 71  LYS B CA  
1584 C C   . LYS B 71  ? 0.8753 1.3514 1.1061 0.2627  -0.0217 -0.1042 71  LYS B C   
1585 O O   . LYS B 71  ? 0.9717 1.4300 1.1848 0.2720  -0.0298 -0.1053 71  LYS B O   
1586 C CB  . LYS B 71  ? 0.7580 1.3372 1.0518 0.2507  -0.0521 -0.1219 71  LYS B CB  
1587 C CG  . LYS B 71  ? 0.8010 1.3364 1.0693 0.2194  -0.0681 -0.1229 71  LYS B CG  
1588 C CD  . LYS B 71  ? 1.0009 1.5955 1.3080 0.1841  -0.0765 -0.1200 71  LYS B CD  
1589 C CE  . LYS B 71  ? 0.9598 1.5629 1.2808 0.1606  -0.0548 -0.1104 71  LYS B CE  
1590 N NZ  . LYS B 71  ? 1.0930 1.7506 1.4499 0.1246  -0.0631 -0.1074 71  LYS B NZ  
1591 N N   . ASP B 72  ? 1.2548 1.1582 0.8934 0.2885  0.0855  0.0620  72  ASP B N   
1592 C CA  . ASP B 72  ? 1.5036 1.3768 1.1275 0.2896  0.0977  0.0569  72  ASP B CA  
1593 C C   . ASP B 72  ? 1.5129 1.4056 1.1630 0.2892  0.0766  0.0516  72  ASP B C   
1594 O O   . ASP B 72  ? 1.6346 1.5309 1.3061 0.2884  0.0881  0.0521  72  ASP B O   
1595 C CB  . ASP B 72  ? 1.5657 1.3728 1.1158 0.2934  0.1014  0.0475  72  ASP B CB  
1596 C CG  . ASP B 72  ? 1.7527 1.5366 1.2654 0.2960  0.0703  0.0355  72  ASP B CG  
1597 O OD1 . ASP B 72  ? 1.6277 1.4085 1.1447 0.2966  0.0584  0.0289  72  ASP B OD1 
1598 O OD2 . ASP B 72  ? 1.9014 1.6700 1.3803 0.2976  0.0577  0.0326  72  ASP B OD2 
1599 N N   . GLN B 73  ? 1.4440 1.3498 1.0933 0.2897  0.0456  0.0464  73  GLN B N   
1600 C CA  . GLN B 73  ? 1.3807 1.3017 1.0496 0.2895  0.0231  0.0401  73  GLN B CA  
1601 C C   . GLN B 73  ? 1.0927 1.0747 0.8353 0.2858  0.0229  0.0487  73  GLN B C   
1602 O O   . GLN B 73  ? 1.0290 1.0251 0.7929 0.2853  0.0087  0.0444  73  GLN B O   
1603 C CB  . GLN B 73  ? 1.3858 1.3004 1.0285 0.2913  -0.0100 0.0318  73  GLN B CB  
1604 C CG  . GLN B 73  ? 1.4984 1.3980 1.1272 0.2930  -0.0323 0.0205  73  GLN B CG  
1605 C CD  . GLN B 73  ? 1.3678 1.2029 0.9290 0.2967  -0.0293 0.0099  73  GLN B CD  
1606 O OE1 . GLN B 73  ? 1.5369 1.3367 1.0579 0.2983  -0.0127 0.0105  73  GLN B OE1 
1607 N NE2 . GLN B 73  ? 1.3880 1.2072 0.9357 0.2982  -0.0460 0.0000  73  GLN B NE2 
1608 N N   . LEU B 74  ? 1.0531 1.0714 0.8345 0.2831  0.0382  0.0605  74  LEU B N   
1609 C CA  . LEU B 74  ? 0.9799 1.0568 0.8319 0.2794  0.0386  0.0690  74  LEU B CA  
1610 C C   . LEU B 74  ? 1.0993 1.1743 0.9705 0.2789  0.0517  0.0683  74  LEU B C   
1611 O O   . LEU B 74  ? 0.8492 0.9575 0.7619 0.2772  0.0393  0.0683  74  LEU B O   
1612 C CB  . LEU B 74  ? 0.7429 0.8506 0.6271 0.2769  0.0591  0.0819  74  LEU B CB  
1613 C CG  . LEU B 74  ? 0.8085 0.9251 0.6817 0.2769  0.0475  0.0841  74  LEU B CG  
1614 C CD1 . LEU B 74  ? 0.7646 0.9197 0.6798 0.2739  0.0671  0.0975  74  LEU B CD1 
1615 C CD2 . LEU B 74  ? 0.8948 1.0352 0.7796 0.2766  0.0125  0.0792  74  LEU B CD2 
1616 N N   . SER B 75  ? 1.0442 1.0790 0.8839 0.2804  0.0766  0.0674  75  SER B N   
1617 C CA  . SER B 75  ? 1.0719 1.0993 0.9245 0.2802  0.0917  0.0667  75  SER B CA  
1618 C C   . SER B 75  ? 1.1822 1.1971 1.0237 0.2816  0.0694  0.0558  75  SER B C   
1619 O O   . SER B 75  ? 1.2009 1.2296 1.0727 0.2805  0.0740  0.0562  75  SER B O   
1620 C CB  . SER B 75  ? 1.2336 1.2136 1.0445 0.2820  0.1201  0.0663  75  SER B CB  
1621 O OG  . SER B 75  ? 1.2840 1.2346 1.0791 0.2833  0.1272  0.0600  75  SER B OG  
1622 N N   . LEU B 76  ? 1.1106 1.1000 0.9098 0.2840  0.0453  0.0462  76  LEU B N   
1623 C CA  . LEU B 76  ? 1.1517 1.1283 0.9374 0.2855  0.0221  0.0353  76  LEU B CA  
1624 C C   . LEU B 76  ? 1.0820 1.1088 0.9141 0.2834  -0.0046 0.0361  76  LEU B C   
1625 O O   . LEU B 76  ? 1.1490 1.1715 0.9762 0.2843  -0.0259 0.0274  76  LEU B O   
1626 C CB  . LEU B 76  ? 1.2089 1.1312 0.9241 0.2893  0.0094  0.0241  76  LEU B CB  
1627 C CG  . LEU B 76  ? 1.2552 1.1218 0.9200 0.2917  0.0332  0.0208  76  LEU B CG  
1628 C CD1 . LEU B 76  ? 1.3214 1.1417 0.9209 0.2949  0.0253  0.0137  76  LEU B CD1 
1629 C CD2 . LEU B 76  ? 1.0948 0.9395 0.7521 0.2926  0.0355  0.0138  76  LEU B CD2 
1630 N N   . GLY B 77  ? 0.8208 0.8948 0.6976 0.2806  -0.0038 0.0462  77  GLY B N   
1631 C CA  . GLY B 77  ? 0.7919 0.9136 0.7109 0.2785  -0.0296 0.0473  77  GLY B CA  
1632 C C   . GLY B 77  ? 0.8666 0.9806 0.7557 0.2801  -0.0568 0.0412  77  GLY B C   
1633 O O   . GLY B 77  ? 0.8240 0.9565 0.7260 0.2798  -0.0840 0.0359  77  GLY B O   
1634 N N   . ASN B 78  ? 0.9059 0.9930 0.7550 0.2817  -0.0501 0.0418  78  ASN B N   
1635 C CA  . ASN B 78  ? 0.9668 1.0422 0.7825 0.2835  -0.0745 0.0359  78  ASN B CA  
1636 C C   . ASN B 78  ? 0.9769 1.0692 0.7995 0.2823  -0.0657 0.0450  78  ASN B C   
1637 O O   . ASN B 78  ? 0.9083 0.9715 0.7012 0.2834  -0.0435 0.0477  78  ASN B O   
1638 C CB  . ASN B 78  ? 1.0130 1.0247 0.7570 0.2877  -0.0785 0.0241  78  ASN B CB  
1639 C CG  . ASN B 78  ? 1.2245 1.2270 0.9408 0.2896  -0.1119 0.0145  78  ASN B CG  
1640 O OD1 . ASN B 78  ? 1.2927 1.2562 0.9669 0.2924  -0.1233 0.0034  78  ASN B OD1 
1641 N ND2 . ASN B 78  ? 1.0660 1.1045 0.8062 0.2880  -0.1278 0.0186  78  ASN B ND2 
1642 N N   . ALA B 79  ? 0.8094 0.9486 0.6711 0.2799  -0.0829 0.0495  79  ALA B N   
1643 C CA  . ALA B 79  ? 0.7885 0.9453 0.6557 0.2789  -0.0795 0.0572  79  ALA B CA  
1644 C C   . ALA B 79  ? 0.8915 1.0251 0.7137 0.2814  -0.1052 0.0487  79  ALA B C   
1645 O O   . ALA B 79  ? 1.0236 1.1866 0.8658 0.2805  -0.1312 0.0471  79  ALA B O   
1646 C CB  . ALA B 79  ? 0.7364 0.9586 0.6739 0.2747  -0.0819 0.0677  79  ALA B CB  
1647 N N   . ALA B 80  ? 0.7661 0.8468 0.5273 0.2847  -0.0974 0.0435  80  ALA B N   
1648 C CA  . ALA B 80  ? 0.7735 0.8249 0.4849 0.2875  -0.1199 0.0348  80  ALA B CA  
1649 C C   . ALA B 80  ? 0.6870 0.7473 0.3931 0.2870  -0.1165 0.0413  80  ALA B C   
1650 O O   . ALA B 80  ? 0.7504 0.8009 0.4502 0.2867  -0.0903 0.0481  80  ALA B O   
1651 C CB  . ALA B 80  ? 0.8331 0.8198 0.4785 0.2915  -0.1149 0.0246  80  ALA B CB  
1652 N N   . LEU B 81  ? 0.5348 0.6331 0.5065 0.1484  0.0134  0.0096  81  LEU B N   
1653 C CA  . LEU B 81  ? 0.5725 0.6833 0.5582 0.1379  0.0160  0.0096  81  LEU B CA  
1654 C C   . LEU B 81  ? 0.5597 0.6590 0.5392 0.1339  0.0206  0.0104  81  LEU B C   
1655 O O   . LEU B 81  ? 0.4614 0.5400 0.4278 0.1327  0.0181  0.0099  81  LEU B O   
1656 C CB  . LEU B 81  ? 0.4716 0.5831 0.4633 0.1289  0.0095  0.0076  81  LEU B CB  
1657 C CG  . LEU B 81  ? 0.5203 0.6403 0.5242 0.1172  0.0114  0.0072  81  LEU B CG  
1658 C CD1 . LEU B 81  ? 0.5499 0.6949 0.5711 0.1161  0.0153  0.0083  81  LEU B CD1 
1659 C CD2 . LEU B 81  ? 0.5157 0.6308 0.5214 0.1088  0.0048  0.0048  81  LEU B CD2 
1660 N N   . GLN B 82  ? 0.4365 0.5493 0.4255 0.1318  0.0273  0.0120  82  GLN B N   
1661 C CA  . GLN B 82  ? 0.5689 0.6736 0.5544 0.1268  0.0319  0.0130  82  GLN B CA  
1662 C C   . GLN B 82  ? 0.5019 0.6179 0.5022 0.1148  0.0320  0.0126  82  GLN B C   
1663 O O   . GLN B 82  ? 0.5292 0.6662 0.5450 0.1126  0.0332  0.0130  82  GLN B O   
1664 C CB  . GLN B 82  ? 0.6206 0.7311 0.6045 0.1337  0.0398  0.0153  82  GLN B CB  
1665 C CG  . GLN B 82  ? 0.5848 0.6884 0.5658 0.1282  0.0448  0.0166  82  GLN B CG  
1666 C CD  . GLN B 82  ? 0.8620 0.9740 0.8431 0.1344  0.0529  0.0190  82  GLN B CD  
1667 O OE1 . GLN B 82  ? 0.8823 1.0156 0.8778 0.1337  0.0568  0.0203  82  GLN B OE1 
1668 N NE2 . GLN B 82  ? 0.9278 1.0229 0.8927 0.1405  0.0554  0.0197  82  GLN B NE2 
1669 N N   . ILE B 83  ? 0.5049 0.6067 0.5005 0.1069  0.0304  0.0118  83  ILE B N   
1670 C CA  . ILE B 83  ? 0.4326 0.5419 0.4405 0.0952  0.0303  0.0112  83  ILE B CA  
1671 C C   . ILE B 83  ? 0.5601 0.6606 0.5637 0.0913  0.0352  0.0127  83  ILE B C   
1672 O O   . ILE B 83  ? 0.5357 0.6155 0.5245 0.0929  0.0345  0.0127  83  ILE B O   
1673 C CB  . ILE B 83  ? 0.5655 0.6664 0.5732 0.0883  0.0230  0.0085  83  ILE B CB  
1674 C CG1 . ILE B 83  ? 0.5823 0.6977 0.5992 0.0895  0.0187  0.0072  83  ILE B CG1 
1675 C CG2 . ILE B 83  ? 0.6034 0.7047 0.6192 0.0764  0.0232  0.0078  83  ILE B CG2 
1676 C CD1 . ILE B 83  ? 0.8041 0.9063 0.8120 0.0908  0.0116  0.0051  83  ILE B CD1 
1677 N N   . THR B 84  ? 0.4806 0.5969 0.4971 0.0862  0.0397  0.0142  84  THR B N   
1678 C CA  . THR B 84  ? 0.4975 0.6088 0.5119 0.0823  0.0448  0.0160  84  THR B CA  
1679 C C   . THR B 84  ? 0.5757 0.6841 0.5970 0.0698  0.0422  0.0149  84  THR B C   
1680 O O   . THR B 84  ? 0.5680 0.6883 0.6021 0.0637  0.0389  0.0134  84  THR B O   
1681 C CB  . THR B 84  ? 0.5571 0.6879 0.5813 0.0846  0.0518  0.0188  84  THR B CB  
1682 O OG1 . THR B 84  ? 0.6564 0.7879 0.6728 0.0967  0.0548  0.0199  84  THR B OG1 
1683 C CG2 . THR B 84  ? 0.6551 0.7821 0.6787 0.0791  0.0568  0.0208  84  THR B CG2 
1684 N N   . ASP B 85  ? 0.5547 0.6469 0.5673 0.0660  0.0435  0.0155  85  ASP B N   
1685 C CA  . ASP B 85  ? 0.4586 0.5478 0.4779 0.0542  0.0416  0.0146  85  ASP B CA  
1686 C C   . ASP B 85  ? 0.4395 0.5221 0.4595 0.0498  0.0343  0.0113  85  ASP B C   
1687 O O   . ASP B 85  ? 0.5671 0.6618 0.6006 0.0427  0.0317  0.0098  85  ASP B O   
1688 C CB  . ASP B 85  ? 0.5675 0.6785 0.6045 0.0480  0.0450  0.0160  85  ASP B CB  
1689 C CG  . ASP B 85  ? 0.7052 0.8123 0.7481 0.0364  0.0443  0.0157  85  ASP B CG  
1690 O OD1 . ASP B 85  ? 0.7067 0.7947 0.7384 0.0344  0.0443  0.0159  85  ASP B OD1 
1691 O OD2 . ASP B 85  ? 0.7794 0.9024 0.8379 0.0292  0.0438  0.0155  85  ASP B OD2 
1692 N N   . VAL B 86  ? 0.4445 0.5075 0.4494 0.0541  0.0309  0.0103  86  VAL B N   
1693 C CA  . VAL B 86  ? 0.4022 0.4583 0.4059 0.0515  0.0240  0.0074  86  VAL B CA  
1694 C C   . VAL B 86  ? 0.5511 0.6051 0.5628 0.0396  0.0214  0.0057  86  VAL B C   
1695 O O   . VAL B 86  ? 0.5438 0.5877 0.5527 0.0345  0.0232  0.0065  86  VAL B O   
1696 C CB  . VAL B 86  ? 0.4644 0.4982 0.4498 0.0580  0.0211  0.0072  86  VAL B CB  
1697 C CG1 . VAL B 86  ? 0.4689 0.4932 0.4526 0.0535  0.0141  0.0044  86  VAL B CG1 
1698 C CG2 . VAL B 86  ? 0.4552 0.4927 0.4342 0.0698  0.0222  0.0082  86  VAL B CG2 
1699 N N   . LYS B 87  ? 0.4375 0.5007 0.4590 0.0351  0.0170  0.0032  87  LYS B N   
1700 C CA  . LYS B 87  ? 0.4646 0.5266 0.4942 0.0241  0.0138  0.0009  87  LYS B CA  
1701 C C   . LYS B 87  ? 0.4638 0.5106 0.4853 0.0233  0.0077  -0.0017 87  LYS B C   
1702 O O   . LYS B 87  ? 0.4579 0.4986 0.4699 0.0308  0.0054  -0.0018 87  LYS B O   
1703 C CB  . LYS B 87  ? 0.5042 0.5889 0.5517 0.0190  0.0134  -0.0001 87  LYS B CB  
1704 C CG  . LYS B 87  ? 0.6487 0.7506 0.7060 0.0193  0.0192  0.0027  87  LYS B CG  
1705 C CD  . LYS B 87  ? 0.6682 0.7617 0.7227 0.0156  0.0233  0.0048  87  LYS B CD  
1706 C CE  . LYS B 87  ? 0.7848 0.8975 0.8530 0.0123  0.0280  0.0071  87  LYS B CE  
1707 N NZ  . LYS B 87  ? 0.8333 0.9402 0.9038 0.0040  0.0298  0.0080  87  LYS B NZ  
1708 N N   . LEU B 88  ? 0.4020 0.4429 0.4276 0.0139  0.0049  -0.0037 88  LEU B N   
1709 C CA  . LEU B 88  ? 0.4869 0.5150 0.5066 0.0121  -0.0009 -0.0063 88  LEU B CA  
1710 C C   . LEU B 88  ? 0.4491 0.4894 0.4744 0.0139  -0.0047 -0.0084 88  LEU B C   
1711 O O   . LEU B 88  ? 0.4351 0.4660 0.4519 0.0172  -0.0089 -0.0095 88  LEU B O   
1712 C CB  . LEU B 88  ? 0.5855 0.6065 0.6102 0.0015  -0.0028 -0.0082 88  LEU B CB  
1713 C CG  . LEU B 88  ? 0.6542 0.6546 0.6684 -0.0001 -0.0017 -0.0068 88  LEU B CG  
1714 C CD1 . LEU B 88  ? 0.5619 0.5604 0.5848 -0.0112 -0.0024 -0.0083 88  LEU B CD1 
1715 C CD2 . LEU B 88  ? 0.6301 0.6108 0.6291 0.0045  -0.0054 -0.0071 88  LEU B CD2 
1716 N N   . GLN B 89  ? 0.4396 0.5009 0.4790 0.0117  -0.0035 -0.0087 89  GLN B N   
1717 C CA  . GLN B 89  ? 0.4652 0.5390 0.5104 0.0131  -0.0071 -0.0105 89  GLN B CA  
1718 C C   . GLN B 89  ? 0.5732 0.6485 0.6107 0.0241  -0.0069 -0.0089 89  GLN B C   
1719 O O   . GLN B 89  ? 0.4164 0.4995 0.4564 0.0261  -0.0105 -0.0102 89  GLN B O   
1720 C CB  . GLN B 89  ? 0.4500 0.5458 0.5126 0.0078  -0.0059 -0.0110 89  GLN B CB  
1721 C CG  . GLN B 89  ? 0.6299 0.7366 0.6981 0.0096  0.0002  -0.0078 89  GLN B CG  
1722 C CD  . GLN B 89  ? 0.8474 0.9514 0.9208 0.0014  0.0026  -0.0074 89  GLN B CD  
1723 O OE1 . GLN B 89  ? 0.5759 0.6628 0.6420 -0.0021 0.0015  -0.0082 89  GLN B OE1 
1724 N NE2 . GLN B 89  ? 0.7078 0.8290 0.7942 -0.0018 0.0058  -0.0060 89  GLN B NE2 
1725 N N   . ASP B 90  ? 0.4667 0.5346 0.4947 0.0310  -0.0030 -0.0061 90  ASP B N   
1726 C CA  . ASP B 90  ? 0.4040 0.4709 0.4232 0.0418  -0.0031 -0.0047 90  ASP B CA  
1727 C C   . ASP B 90  ? 0.4850 0.5333 0.4900 0.0454  -0.0080 -0.0056 90  ASP B C   
1728 O O   . ASP B 90  ? 0.4759 0.5235 0.4742 0.0539  -0.0094 -0.0049 90  ASP B O   
1729 C CB  . ASP B 90  ? 0.4478 0.5128 0.4614 0.0481  0.0030  -0.0016 90  ASP B CB  
1730 C CG  . ASP B 90  ? 0.4965 0.5821 0.5239 0.0467  0.0080  -0.0001 90  ASP B CG  
1731 O OD1 . ASP B 90  ? 0.5081 0.6114 0.5477 0.0450  0.0067  -0.0010 90  ASP B OD1 
1732 O OD2 . ASP B 90  ? 0.5255 0.6095 0.5513 0.0472  0.0133  0.0021  90  ASP B OD2 
1733 N N   . ALA B 91  ? 0.3753 0.4088 0.3760 0.0392  -0.0107 -0.0070 91  ALA B N   
1734 C CA  . ALA B 91  ? 0.3851 0.4015 0.3732 0.0418  -0.0157 -0.0077 91  ALA B CA  
1735 C C   . ALA B 91  ? 0.4602 0.4856 0.4529 0.0417  -0.0208 -0.0099 91  ALA B C   
1736 O O   . ALA B 91  ? 0.5056 0.5450 0.5111 0.0352  -0.0217 -0.0119 91  ALA B O   
1737 C CB  . ALA B 91  ? 0.4584 0.4579 0.4424 0.0345  -0.0173 -0.0087 91  ALA B CB  
1738 N N   . GLY B 92  ? 0.4630 0.4801 0.4450 0.0488  -0.0243 -0.0093 92  GLY B N   
1739 C CA  . GLY B 92  ? 0.6187 0.6433 0.6037 0.0491  -0.0294 -0.0111 92  GLY B CA  
1740 C C   . GLY B 92  ? 0.5066 0.5288 0.4823 0.0596  -0.0313 -0.0094 92  GLY B C   
1741 O O   . GLY B 92  ? 0.4855 0.4964 0.4503 0.0664  -0.0294 -0.0072 92  GLY B O   
1742 N N   . VAL B 93  ? 0.4159 0.4490 0.3961 0.0607  -0.0352 -0.0105 93  VAL B N   
1743 C CA  . VAL B 93  ? 0.5056 0.5373 0.4780 0.0700  -0.0381 -0.0092 93  VAL B CA  
1744 C C   . VAL B 93  ? 0.5291 0.5806 0.5111 0.0745  -0.0352 -0.0084 93  VAL B C   
1745 O O   . VAL B 93  ? 0.4465 0.5152 0.4415 0.0699  -0.0357 -0.0098 93  VAL B O   
1746 C CB  . VAL B 93  ? 0.6174 0.6462 0.5872 0.0685  -0.0450 -0.0108 93  VAL B CB  
1747 C CG1 . VAL B 93  ? 0.4484 0.4774 0.4114 0.0780  -0.0482 -0.0093 93  VAL B CG1 
1748 C CG2 . VAL B 93  ? 0.6248 0.6337 0.5851 0.0644  -0.0477 -0.0113 93  VAL B CG2 
1749 N N   . TYR B 94  ? 0.4586 0.5077 0.4341 0.0835  -0.0323 -0.0061 94  TYR B N   
1750 C CA  . TYR B 94  ? 0.5085 0.5747 0.4916 0.0893  -0.0293 -0.0049 94  TYR B CA  
1751 C C   . TYR B 94  ? 0.4286 0.4959 0.4069 0.0969  -0.0342 -0.0046 94  TYR B C   
1752 O O   . TYR B 94  ? 0.5079 0.5591 0.4733 0.1006  -0.0382 -0.0043 94  TYR B O   
1753 C CB  . TYR B 94  ? 0.6146 0.6774 0.5931 0.0950  -0.0229 -0.0027 94  TYR B CB  
1754 C CG  . TYR B 94  ? 0.4746 0.5405 0.4601 0.0879  -0.0176 -0.0026 94  TYR B CG  
1755 C CD1 . TYR B 94  ? 0.4074 0.4592 0.3887 0.0808  -0.0183 -0.0036 94  TYR B CD1 
1756 C CD2 . TYR B 94  ? 0.5038 0.5868 0.5004 0.0883  -0.0120 -0.0015 94  TYR B CD2 
1757 C CE1 . TYR B 94  ? 0.4389 0.4933 0.4267 0.0740  -0.0138 -0.0034 94  TYR B CE1 
1758 C CE2 . TYR B 94  ? 0.4761 0.5621 0.4792 0.0816  -0.0074 -0.0012 94  TYR B CE2 
1759 C CZ  . TYR B 94  ? 0.4568 0.5284 0.4555 0.0744  -0.0084 -0.0023 94  TYR B CZ  
1760 O OH  . TYR B 94  ? 0.5188 0.5932 0.5242 0.0676  -0.0041 -0.0019 94  TYR B OH  
1761 N N   . ARG B 95  ? 0.4201 0.5063 0.4090 0.0989  -0.0339 -0.0045 95  ARG B N   
1762 C CA  . ARG B 95  ? 0.4001 0.4894 0.3860 0.1067  -0.0380 -0.0039 95  ARG B CA  
1763 C C   . ARG B 95  ? 0.5623 0.6649 0.5536 0.1141  -0.0333 -0.0021 95  ARG B C   
1764 O O   . ARG B 95  ? 0.5083 0.6275 0.5129 0.1107  -0.0291 -0.0020 95  ARG B O   
1765 C CB  . ARG B 95  ? 0.4389 0.5387 0.4326 0.1018  -0.0437 -0.0056 95  ARG B CB  
1766 C CG  . ARG B 95  ? 0.5241 0.6102 0.5110 0.0959  -0.0489 -0.0073 95  ARG B CG  
1767 C CD  . ARG B 95  ? 0.6196 0.7169 0.6149 0.0900  -0.0539 -0.0092 95  ARG B CD  
1768 N NE  . ARG B 95  ? 0.6539 0.7385 0.6432 0.0838  -0.0581 -0.0109 95  ARG B NE  
1769 C CZ  . ARG B 95  ? 0.6517 0.7298 0.6419 0.0763  -0.0561 -0.0122 95  ARG B CZ  
1770 N NH1 . ARG B 95  ? 0.7637 0.8461 0.7600 0.0738  -0.0501 -0.0119 95  ARG B NH1 
1771 N NH2 . ARG B 95  ? 0.5870 0.6539 0.5718 0.0712  -0.0601 -0.0137 95  ARG B NH2 
1772 N N   . CYS B 96  ? 0.4429 0.5376 0.4238 0.1243  -0.0341 -0.0007 96  CYS B N   
1773 C CA  . CYS B 96  ? 0.4508 0.5576 0.4360 0.1328  -0.0304 0.0009  96  CYS B CA  
1774 C C   . CYS B 96  ? 0.5884 0.7017 0.5749 0.1374  -0.0364 0.0008  96  CYS B C   
1775 O O   . CYS B 96  ? 0.5230 0.6227 0.4982 0.1406  -0.0421 0.0006  96  CYS B O   
1776 C CB  . CYS B 96  ? 0.5940 0.6876 0.5667 0.1414  -0.0264 0.0025  96  CYS B CB  
1777 S SG  . CYS B 96  ? 1.0404 1.1167 0.9959 0.1522  -0.0321 0.0032  96  CYS B SG  
1778 N N   . MET B 97  ? 0.5083 0.6424 0.5089 0.1373  -0.0354 0.0010  97  MET B N   
1779 C CA  . MET B 97  ? 0.4129 0.5568 0.4183 0.1397  -0.0410 0.0008  97  MET B CA  
1780 C C   . MET B 97  ? 0.5038 0.6595 0.5138 0.1491  -0.0378 0.0025  97  MET B C   
1781 O O   . MET B 97  ? 0.5683 0.7377 0.5888 0.1485  -0.0317 0.0034  97  MET B O   
1782 C CB  . MET B 97  ? 0.5494 0.7083 0.5688 0.1299  -0.0430 -0.0006 97  MET B CB  
1783 C CG  . MET B 97  ? 0.6493 0.7976 0.6650 0.1204  -0.0459 -0.0025 97  MET B CG  
1784 S SD  . MET B 97  ? 0.7174 0.8821 0.7479 0.1097  -0.0494 -0.0045 97  MET B SD  
1785 C CE  . MET B 97  ? 0.7726 0.9196 0.7943 0.1012  -0.0529 -0.0068 97  MET B CE  
1786 N N   . ILE B 98  ? 0.5015 0.6521 0.5040 0.1578  -0.0419 0.0031  98  ILE B N   
1787 C CA  . ILE B 98  ? 0.4888 0.6483 0.4941 0.1678  -0.0390 0.0047  98  ILE B CA  
1788 C C   . ILE B 98  ? 0.6132 0.7815 0.6228 0.1712  -0.0454 0.0048  98  ILE B C   
1789 O O   . ILE B 98  ? 0.5122 0.6694 0.5130 0.1719  -0.0524 0.0042  98  ILE B O   
1790 C CB  . ILE B 98  ? 0.4307 0.5732 0.4206 0.1771  -0.0365 0.0055  98  ILE B CB  
1791 C CG1 . ILE B 98  ? 0.5478 0.6824 0.5341 0.1731  -0.0301 0.0056  98  ILE B CG1 
1792 C CG2 . ILE B 98  ? 0.5639 0.7162 0.5570 0.1878  -0.0335 0.0068  98  ILE B CG2 
1793 C CD1 . ILE B 98  ? 0.6962 0.8096 0.6650 0.1798  -0.0289 0.0061  98  ILE B CD1 
1794 N N   . SER B 99  ? 0.5883 0.7769 0.6122 0.1728  -0.0431 0.0056  99  SER B N   
1795 C CA  . SER B 99  ? 0.5799 0.7782 0.6087 0.1781  -0.0480 0.0062  99  SER B CA  
1796 C C   . SER B 99  ? 0.6348 0.8365 0.6628 0.1898  -0.0438 0.0077  99  SER B C   
1797 O O   . SER B 99  ? 0.6845 0.8989 0.7219 0.1908  -0.0368 0.0087  99  SER B O   
1798 C CB  . SER B 99  ? 0.6006 0.8200 0.6469 0.1711  -0.0492 0.0061  99  SER B CB  
1799 O OG  . SER B 99  ? 0.6773 0.9065 0.7287 0.1765  -0.0537 0.0069  99  SER B OG  
1800 N N   . TYR B 100 ? 0.5910 0.7815 0.6079 0.1985  -0.0481 0.0079  100 TYR B N   
1801 C CA  . TYR B 100 ? 0.6606 0.8533 0.6758 0.2104  -0.0451 0.0090  100 TYR B CA  
1802 C C   . TYR B 100 ? 0.6899 0.8777 0.6996 0.2167  -0.0534 0.0091  100 TYR B C   
1803 O O   . TYR B 100 ? 0.7273 0.8962 0.7217 0.2209  -0.0573 0.0088  100 TYR B O   
1804 C CB  . TYR B 100 ? 0.7042 0.8814 0.7063 0.2156  -0.0395 0.0092  100 TYR B CB  
1805 C CG  . TYR B 100 ? 0.7710 0.9519 0.7723 0.2274  -0.0347 0.0102  100 TYR B CG  
1806 C CD1 . TYR B 100 ? 0.6585 0.8600 0.6747 0.2290  -0.0287 0.0112  100 TYR B CD1 
1807 C CD2 . TYR B 100 ? 0.8513 1.0147 0.8367 0.2370  -0.0361 0.0101  100 TYR B CD2 
1808 C CE1 . TYR B 100 ? 0.8684 1.0736 0.8840 0.2399  -0.0240 0.0120  100 TYR B CE1 
1809 C CE2 . TYR B 100 ? 0.8264 0.9929 0.8108 0.2480  -0.0316 0.0107  100 TYR B CE2 
1810 C CZ  . TYR B 100 ? 0.9210 1.1085 0.9205 0.2495  -0.0254 0.0117  100 TYR B CZ  
1811 O OH  . TYR B 100 ? 1.0006 1.1916 0.9992 0.2606  -0.0206 0.0122  100 TYR B OH  
1812 N N   . GLY B 101 ? 0.8091 1.0139 0.8316 0.2167  -0.0565 0.0096  101 GLY B N   
1813 C CA  . GLY B 101 ? 0.7404 0.9403 0.7582 0.2196  -0.0657 0.0095  101 GLY B CA  
1814 C C   . GLY B 101 ? 0.8233 1.0162 0.8379 0.2092  -0.0714 0.0085  101 GLY B C   
1815 O O   . GLY B 101 ? 0.7734 0.9795 0.7997 0.2008  -0.0729 0.0081  101 GLY B O   
1816 N N   . GLY B 102 ? 0.5875 0.7595 0.5861 0.2099  -0.0748 0.0080  102 GLY B N   
1817 C CA  . GLY B 102 ? 0.6330 0.7966 0.6272 0.2002  -0.0793 0.0069  102 GLY B CA  
1818 C C   . GLY B 102 ? 0.6123 0.7787 0.6116 0.1909  -0.0731 0.0060  102 GLY B C   
1819 O O   . GLY B 102 ? 0.6215 0.7993 0.6299 0.1908  -0.0659 0.0063  102 GLY B O   
1820 N N   . ALA B 103 ? 0.6706 0.8262 0.6637 0.1829  -0.0764 0.0049  103 ALA B N   
1821 C CA  . ALA B 103 ? 0.4895 0.6456 0.4863 0.1736  -0.0715 0.0038  103 ALA B CA  
1822 C C   . ALA B 103 ? 0.5757 0.7106 0.5583 0.1701  -0.0740 0.0031  103 ALA B C   
1823 O O   . ALA B 103 ? 0.6086 0.7332 0.5826 0.1708  -0.0811 0.0031  103 ALA B O   
1824 C CB  . ALA B 103 ? 0.4693 0.6426 0.4809 0.1640  -0.0728 0.0029  103 ALA B CB  
1825 N N   . ASP B 104 ? 0.6167 0.7456 0.5974 0.1662  -0.0681 0.0026  104 ASP B N   
1826 C CA  . ASP B 104 ? 0.5803 0.6889 0.5480 0.1627  -0.0698 0.0021  104 ASP B CA  
1827 C C   . ASP B 104 ? 0.5969 0.7053 0.5682 0.1556  -0.0631 0.0013  104 ASP B C   
1828 O O   . ASP B 104 ? 0.5595 0.6815 0.5412 0.1553  -0.0569 0.0015  104 ASP B O   
1829 C CB  . ASP B 104 ? 0.5536 0.6435 0.5051 0.1723  -0.0710 0.0033  104 ASP B CB  
1830 C CG  . ASP B 104 ? 0.7001 0.7690 0.6379 0.1691  -0.0754 0.0031  104 ASP B CG  
1831 O OD1 . ASP B 104 ? 0.6395 0.7091 0.5802 0.1603  -0.0789 0.0020  104 ASP B OD1 
1832 O OD2 . ASP B 104 ? 0.6953 0.7471 0.6196 0.1753  -0.0753 0.0041  104 ASP B OD2 
1833 N N   . TYR B 105 ? 0.6145 0.7081 0.5779 0.1497  -0.0647 0.0005  105 TYR B N   
1834 C CA  . TYR B 105 ? 0.4759 0.5664 0.4409 0.1437  -0.0586 -0.0001 105 TYR B CA  
1835 C C   . TYR B 105 ? 0.5932 0.6607 0.5434 0.1425  -0.0604 -0.0001 105 TYR B C   
1836 O O   . TYR B 105 ? 0.5509 0.6070 0.4920 0.1435  -0.0669 0.0000  105 TYR B O   
1837 C CB  . TYR B 105 ? 0.5418 0.6473 0.5213 0.1330  -0.0576 -0.0018 105 TYR B CB  
1838 C CG  . TYR B 105 ? 0.5404 0.6403 0.5185 0.1243  -0.0631 -0.0035 105 TYR B CG  
1839 C CD1 . TYR B 105 ? 0.5838 0.6705 0.5565 0.1180  -0.0620 -0.0044 105 TYR B CD1 
1840 C CD2 . TYR B 105 ? 0.6054 0.7138 0.5881 0.1224  -0.0692 -0.0042 105 TYR B CD2 
1841 C CE1 . TYR B 105 ? 0.6519 0.7342 0.6240 0.1102  -0.0667 -0.0061 105 TYR B CE1 
1842 C CE2 . TYR B 105 ? 0.6853 0.7892 0.6668 0.1146  -0.0739 -0.0059 105 TYR B CE2 
1843 C CZ  . TYR B 105 ? 0.7803 0.8712 0.7566 0.1086  -0.0725 -0.0069 105 TYR B CZ  
1844 O OH  . TYR B 105 ? 0.7130 0.7997 0.6883 0.1010  -0.0770 -0.0086 105 TYR B OH  
1845 N N   . LYS B 106 ? 0.5023 0.5631 0.4502 0.1404  -0.0546 0.0000  106 LYS B N   
1846 C CA  . LYS B 106 ? 0.5200 0.5591 0.4548 0.1384  -0.0556 0.0001  106 LYS B CA  
1847 C C   . LYS B 106 ? 0.5501 0.5899 0.4909 0.1287  -0.0512 -0.0010 106 LYS B C   
1848 O O   . LYS B 106 ? 0.6561 0.7106 0.6087 0.1256  -0.0459 -0.0013 106 LYS B O   
1849 C CB  . LYS B 106 ? 0.6029 0.6271 0.5241 0.1480  -0.0535 0.0019  106 LYS B CB  
1850 C CG  . LYS B 106 ? 0.6167 0.6331 0.5278 0.1572  -0.0594 0.0030  106 LYS B CG  
1851 C CD  . LYS B 106 ? 0.6644 0.6655 0.5660 0.1541  -0.0669 0.0030  106 LYS B CD  
1852 C CE  . LYS B 106 ? 0.8472 0.8367 0.7364 0.1637  -0.0726 0.0045  106 LYS B CE  
1853 N NZ  . LYS B 106 ? 0.7672 0.7718 0.6632 0.1691  -0.0753 0.0046  106 LYS B NZ  
1854 N N   . ARG B 107 ? 0.5101 0.5332 0.4424 0.1238  -0.0538 -0.0014 107 ARG B N   
1855 C CA  . ARG B 107 ? 0.4382 0.4583 0.3743 0.1144  -0.0509 -0.0026 107 ARG B CA  
1856 C C   . ARG B 107 ? 0.4463 0.4502 0.3721 0.1167  -0.0467 -0.0012 107 ARG B C   
1857 O O   . ARG B 107 ? 0.5651 0.5528 0.4770 0.1234  -0.0488 0.0002  107 ARG B O   
1858 C CB  . ARG B 107 ? 0.4977 0.5101 0.4318 0.1071  -0.0566 -0.0041 107 ARG B CB  
1859 C CG  . ARG B 107 ? 0.6643 0.6928 0.6095 0.1023  -0.0603 -0.0058 107 ARG B CG  
1860 C CD  . ARG B 107 ? 0.7409 0.7606 0.6834 0.0948  -0.0651 -0.0074 107 ARG B CD  
1861 N NE  . ARG B 107 ? 0.7019 0.7018 0.6291 0.0992  -0.0697 -0.0059 107 ARG B NE  
1862 N N   . ILE B 108 ? 0.5231 0.5311 0.4557 0.1108  -0.0411 -0.0017 108 ILE B N   
1863 C CA  . ILE B 108 ? 0.4837 0.4772 0.4079 0.1112  -0.0368 -0.0005 108 ILE B CA  
1864 C C   . ILE B 108 ? 0.5226 0.5141 0.4526 0.1001  -0.0355 -0.0019 108 ILE B C   
1865 O O   . ILE B 108 ? 0.5194 0.5271 0.4634 0.0939  -0.0330 -0.0031 108 ILE B O   
1866 C CB  . ILE B 108 ? 0.5010 0.5030 0.4278 0.1169  -0.0299 0.0009  108 ILE B CB  
1867 C CG1 . ILE B 108 ? 0.5208 0.5224 0.4404 0.1286  -0.0311 0.0022  108 ILE B CG1 
1868 C CG2 . ILE B 108 ? 0.4412 0.4296 0.3608 0.1156  -0.0252 0.0020  108 ILE B CG2 
1869 C CD1 . ILE B 108 ? 0.7461 0.7524 0.6652 0.1353  -0.0242 0.0037  108 ILE B CD1 
1870 N N   . THR B 109 ? 0.4623 0.4339 0.3818 0.0977  -0.0373 -0.0016 109 THR B N   
1871 C CA  . THR B 109 ? 0.4608 0.4287 0.3850 0.0875  -0.0361 -0.0028 109 THR B CA  
1872 C C   . THR B 109 ? 0.4860 0.4505 0.4094 0.0869  -0.0295 -0.0015 109 THR B C   
1873 O O   . THR B 109 ? 0.5020 0.4530 0.4133 0.0933  -0.0280 0.0004  109 THR B O   
1874 C CB  . THR B 109 ? 0.5467 0.4951 0.4608 0.0845  -0.0413 -0.0030 109 THR B CB  
1875 O OG1 . THR B 109 ? 0.5882 0.5401 0.5027 0.0851  -0.0474 -0.0040 109 THR B OG1 
1876 C CG2 . THR B 109 ? 0.5372 0.4825 0.4572 0.0739  -0.0402 -0.0045 109 THR B CG2 
1877 N N   . VAL B 110 ? 0.4948 0.4713 0.4310 0.0792  -0.0258 -0.0026 110 VAL B N   
1878 C CA  . VAL B 110 ? 0.4585 0.4328 0.3955 0.0770  -0.0198 -0.0015 110 VAL B CA  
1879 C C   . VAL B 110 ? 0.5260 0.4927 0.4661 0.0665  -0.0206 -0.0028 110 VAL B C   
1880 O O   . VAL B 110 ? 0.4540 0.4313 0.4057 0.0591  -0.0223 -0.0050 110 VAL B O   
1881 C CB  . VAL B 110 ? 0.5270 0.5230 0.4770 0.0774  -0.0144 -0.0011 110 VAL B CB  
1882 C CG1 . VAL B 110 ? 0.5869 0.5807 0.5383 0.0738  -0.0085 0.0001  110 VAL B CG1 
1883 C CG2 . VAL B 110 ? 0.5064 0.5092 0.4531 0.0883  -0.0133 0.0003  110 VAL B CG2 
1884 N N   . LYS B 111 ? 0.5179 0.4662 0.4478 0.0660  -0.0194 -0.0015 111 LYS B N   
1885 C CA  . LYS B 111 ? 0.4527 0.3924 0.3849 0.0564  -0.0194 -0.0023 111 LYS B CA  
1886 C C   . LYS B 111 ? 0.5226 0.4638 0.4574 0.0545  -0.0131 -0.0008 111 LYS B C   
1887 O O   . LYS B 111 ? 0.4881 0.4253 0.4148 0.0616  -0.0097 0.0014  111 LYS B O   
1888 C CB  . LYS B 111 ? 0.6172 0.5330 0.5355 0.0566  -0.0237 -0.0017 111 LYS B CB  
1889 C CG  . LYS B 111 ? 0.6269 0.5407 0.5445 0.0556  -0.0302 -0.0034 111 LYS B CG  
1890 N N   . VAL B 112 ? 0.4833 0.4305 0.4292 0.0449  -0.0117 -0.0021 112 VAL B N   
1891 C CA  . VAL B 112 ? 0.5406 0.4916 0.4910 0.0418  -0.0059 -0.0007 112 VAL B CA  
1892 C C   . VAL B 112 ? 0.4641 0.3989 0.4114 0.0341  -0.0066 -0.0007 112 VAL B C   
1893 O O   . VAL B 112 ? 0.5250 0.4596 0.4792 0.0261  -0.0098 -0.0030 112 VAL B O   
1894 C CB  . VAL B 112 ? 0.5574 0.5323 0.5253 0.0373  -0.0032 -0.0017 112 VAL B CB  
1895 C CG1 . VAL B 112 ? 0.5157 0.4941 0.4883 0.0335  0.0024  0.0000  112 VAL B CG1 
1896 C CG2 . VAL B 112 ? 0.5177 0.5087 0.4889 0.0451  -0.0025 -0.0013 112 VAL B CG2 
1897 N N   . ASN B 113 ? 0.5725 0.4936 0.5096 0.0364  -0.0036 0.0017  113 ASN B N   
1898 C CA  . ASN B 113 ? 0.4538 0.3614 0.3893 0.0289  -0.0032 0.0021  113 ASN B CA  
1899 C C   . ASN B 113 ? 0.4575 0.3792 0.4056 0.0229  0.0018  0.0025  113 ASN B C   
1900 O O   . ASN B 113 ? 0.6206 0.5553 0.5717 0.0272  0.0064  0.0039  113 ASN B O   
1901 C CB  . ASN B 113 ? 0.5006 0.3866 0.4189 0.0340  -0.0025 0.0048  113 ASN B CB  
1902 C CG  . ASN B 113 ? 0.5209 0.3913 0.4263 0.0395  -0.0078 0.0048  113 ASN B CG  
1903 O OD1 . ASN B 113 ? 0.5509 0.4179 0.4585 0.0355  -0.0127 0.0029  113 ASN B OD1 
1904 N ND2 . ASN B 113 ? 0.5009 0.3616 0.3924 0.0488  -0.0069 0.0069  113 ASN B ND2 
1905 N N   . ALA B 114 ? 0.6221 0.4757 0.6185 0.1928  -0.1237 0.0210  114 ALA B N   
1906 C CA  . ALA B 114 ? 0.5053 0.3839 0.5566 0.1867  -0.0998 -0.0009 114 ALA B CA  
1907 C C   . ALA B 114 ? 0.6430 0.5110 0.6941 0.1732  -0.0638 0.0065  114 ALA B C   
1908 O O   . ALA B 114 ? 0.5912 0.4413 0.6007 0.1643  -0.0604 0.0207  114 ALA B O   
1909 C CB  . ALA B 114 ? 0.5697 0.4772 0.6401 0.1813  -0.1122 -0.0264 114 ALA B CB  
1910 N N   . PRO B 115 ? 0.5031 0.3820 0.6000 0.1715  -0.0365 -0.0030 115 PRO B N   
1911 C CA  . PRO B 115 ? 0.5163 0.3872 0.6167 0.1585  -0.0009 0.0022  115 PRO B CA  
1912 C C   . PRO B 115 ? 0.5168 0.4019 0.6189 0.1431  0.0075  -0.0123 115 PRO B C   
1913 O O   . PRO B 115 ? 0.4822 0.3875 0.5924 0.1421  -0.0112 -0.0300 115 PRO B O   
1914 C CB  . PRO B 115 ? 0.5385 0.4216 0.6927 0.1626  0.0220  -0.0078 115 PRO B CB  
1915 C CG  . PRO B 115 ? 0.5919 0.4813 0.7608 0.1794  -0.0022 -0.0109 115 PRO B CG  
1916 C CD  . PRO B 115 ? 0.5709 0.4686 0.7176 0.1821  -0.0369 -0.0177 115 PRO B CD  
1917 N N   . TYR B 116 ? 0.4753 0.3491 0.5693 0.1309  0.0368  -0.0042 116 TYR B N   
1918 C CA  . TYR B 116 ? 0.5568 0.4412 0.6507 0.1153  0.0490  -0.0158 116 TYR B CA  
1919 C C   . TYR B 116 ? 0.6394 0.5577 0.7834 0.1127  0.0496  -0.0461 116 TYR B C   
1920 O O   . TYR B 116 ? 0.4671 0.3994 0.6059 0.1059  0.0375  -0.0593 116 TYR B O   
1921 C CB  . TYR B 116 ? 0.5787 0.4493 0.6704 0.1041  0.0856  -0.0054 116 TYR B CB  
1922 C CG  . TYR B 116 ? 0.5214 0.4013 0.6122 0.0877  0.1005  -0.0161 116 TYR B CG  
1923 C CD1 . TYR B 116 ? 0.5130 0.3835 0.5581 0.0805  0.0866  -0.0087 116 TYR B CD1 
1924 C CD2 . TYR B 116 ? 0.5946 0.4930 0.7307 0.0794  0.1283  -0.0341 116 TYR B CD2 
1925 C CE1 . TYR B 116 ? 0.5881 0.4672 0.6326 0.0654  0.1003  -0.0187 116 TYR B CE1 
1926 C CE2 . TYR B 116 ? 0.6660 0.5729 0.8018 0.0644  0.1421  -0.0442 116 TYR B CE2 
1927 C CZ  . TYR B 116 ? 0.6534 0.5507 0.7434 0.0575  0.1280  -0.0364 116 TYR B CZ  
1928 O OH  . TYR B 116 ? 0.6917 0.5975 0.7815 0.0426  0.1420  -0.0465 116 TYR B OH  
1929 N N   . ALA B 117 ? 0.5002 0.4322 0.6935 0.1176  0.0648  -0.0574 117 ALA B N   
1930 C CA  . ALA B 117 ? 0.5592 0.5234 0.8027 0.1139  0.0697  -0.0864 117 ALA B CA  
1931 C C   . ALA B 117 ? 0.4381 0.4207 0.6823 0.1205  0.0345  -0.1010 117 ALA B C   
1932 O O   . ALA B 117 ? 0.6032 0.6072 0.8621 0.1125  0.0311  -0.1209 117 ALA B O   
1933 C CB  . ALA B 117 ? 0.5949 0.5691 0.8894 0.1199  0.0896  -0.0944 117 ALA B CB  
1934 N N   . ALA B 118 ? 0.4143 0.3890 0.6433 0.1350  0.0082  -0.0915 118 ALA B N   
1935 C CA  . ALA B 118 ? 0.5898 0.5807 0.8171 0.1423  -0.0264 -0.1040 118 ALA B CA  
1936 C C   . ALA B 118 ? 0.5217 0.5072 0.7047 0.1344  -0.0432 -0.1006 118 ALA B C   
1937 O O   . ALA B 118 ? 0.5177 0.5253 0.7120 0.1301  -0.0554 -0.1201 118 ALA B O   
1938 C CB  . ALA B 118 ? 0.4814 0.4621 0.6985 0.1597  -0.0498 -0.0923 118 ALA B CB  
1939 N N   . HIS B 119 ? 0.5395 0.4960 0.6717 0.1323  -0.0439 -0.0757 119 HIS B N   
1940 C CA  . HIS B 119 ? 0.6616 0.6107 0.7489 0.1246  -0.0589 -0.0704 119 HIS B CA  
1941 C C   . HIS B 119 ? 0.5432 0.5094 0.6461 0.1087  -0.0422 -0.0878 119 HIS B C   
1942 O O   . HIS B 119 ? 0.6016 0.5767 0.6875 0.1039  -0.0597 -0.0961 119 HIS B O   
1943 C CB  . HIS B 119 ? 0.7008 0.6153 0.7360 0.1228  -0.0541 -0.0408 119 HIS B CB  
1944 C CG  . HIS B 119 ? 1.1763 1.0732 1.1721 0.1354  -0.0848 -0.0236 119 HIS B CG  
1945 N ND1 . HIS B 119 ? 1.1214 0.9967 1.1052 0.1454  -0.0833 -0.0035 119 HIS B ND1 
1946 C CD2 . HIS B 119 ? 1.0265 0.9237 0.9916 0.1397  -0.1175 -0.0232 119 HIS B CD2 
1947 C CE1 . HIS B 119 ? 0.9269 0.7898 0.8744 0.1551  -0.1137 0.0083  119 HIS B CE1 
1948 N NE2 . HIS B 119 ? 1.2249 1.1007 1.1604 0.1520  -0.1349 -0.0032 119 HIS B NE2 
1949 N N   . HIS B 120 ? 0.5339 0.5046 0.6688 0.1006  -0.0082 -0.0933 120 HIS B N   
1950 C CA  . HIS B 120 ? 0.5683 0.5534 0.7185 0.0850  0.0113  -0.1087 120 HIS B CA  
1951 C C   . HIS B 120 ? 0.6642 0.6823 0.8496 0.0845  -0.0025 -0.1375 120 HIS B C   
1952 O O   . HIS B 120 ? 0.6487 0.6767 0.8234 0.0750  -0.0086 -0.1477 120 HIS B O   
1953 C CB  . HIS B 120 ? 0.7792 0.7624 0.9604 0.0786  0.0502  -0.1086 120 HIS B CB  
1954 C CG  . HIS B 120 ? 0.7281 0.7156 0.9117 0.0616  0.0750  -0.1157 120 HIS B CG  
1955 N ND1 . HIS B 120 ? 0.7963 0.7944 1.0216 0.0543  0.1078  -0.1269 120 HIS B ND1 
1956 C CD2 . HIS B 120 ? 0.8120 0.7941 0.9611 0.0504  0.0722  -0.1128 120 HIS B CD2 
1957 C CE1 . HIS B 120 ? 0.9742 0.9733 1.1907 0.0394  0.1241  -0.1308 120 HIS B CE1 
1958 N NE2 . HIS B 120 ? 1.0948 1.0845 1.2655 0.0367  0.1030  -0.1224 120 HIS B NE2 
1959 N N   . HIS B 121 ? 0.5943 0.6299 0.8217 0.0948  -0.0076 -0.1510 121 HIS B N   
1960 C CA  . HIS B 121 ? 0.7498 0.8180 1.0146 0.0955  -0.0204 -0.1789 121 HIS B CA  
1961 C C   . HIS B 121 ? 0.6191 0.6919 0.8538 0.0999  -0.0576 -0.1815 121 HIS B C   
1962 O O   . HIS B 121 ? 0.6371 0.6885 0.8267 0.1065  -0.0770 -0.1615 121 HIS B O   
1963 C CB  . HIS B 121 ? 0.7901 0.8731 1.1031 0.1071  -0.0189 -0.1897 121 HIS B CB  
1964 C CG  . HIS B 121 ? 1.0804 1.1894 1.4158 0.1154  -0.0469 -0.2101 121 HIS B CG  
1965 N ND1 . HIS B 121 ? 1.1847 1.2885 1.4930 0.1278  -0.0813 -0.2028 121 HIS B ND1 
1966 C CD2 . HIS B 121 ? 1.2575 1.3981 1.6403 0.1133  -0.0454 -0.2376 121 HIS B CD2 
1967 C CE1 . HIS B 121 ? 1.2147 1.3460 1.5526 0.1331  -0.0999 -0.2249 121 HIS B CE1 
1968 N NE2 . HIS B 121 ? 1.2636 1.4178 1.6470 0.1244  -0.0787 -0.2463 121 HIS B NE2 
# 
