data_9INU
# 
_entry.id   9INU 
# 
_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   9INU         pdb_00009inu 10.2210/pdb9inu/pdb 
WWPDB D_1300047343 ?            ?                   
# 
_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       2025-03-12 
_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                        9INU 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-08 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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              2464316307@qq.com 
_pdbx_contact_author.name_first         Yao 
_pdbx_contact_author.name_last          Cheng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7227-3292 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Cheng, Y.'  1 0000-0001-7227-3292 
'Xiao, Y.B.' 2 0000-0003-4716-5526 
# 
_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            68 
_citation.language                  ? 
_citation.page_first                156 
_citation.page_last                 173 
_citation.title                     'Novel PD-L1/VISTA Dual Inhibitor as Potential Immunotherapy Agents.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1021/acs.jmedchem.4c01640 
_citation.pdbx_database_id_PubMed   39731560 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Sun, C.'           1  ?                   
primary 'Cheng, Y.'         2  ?                   
primary 'Dong, J.'          3  ?                   
primary 'Hu, L.'            4  ?                   
primary 'Zhang, Y.'         5  ?                   
primary 'Shen, H.'          6  ?                   
primary 'Zhang, G.'         7  ?                   
primary 'Jiang, B.'         8  ?                   
primary 'Adam Youssouf, S.' 9  ?                   
primary 'Min, W.'           10 ?                   
primary 'Shen, Y.'          11 ?                   
primary 'Wang, L.'          12 ?                   
primary 'Deng, H.'          13 0000-0002-4398-8819 
primary 'Xiao, Y.'          14 ?                   
primary 'Yang, P.'          15 0000-0002-2613-941X 
# 
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'                                                                               
14678.759 2 ? ? ? ? 
2 non-polymer syn '(2~{S})-2-[[6-methoxy-2-[(2-methyl-3-phenyl-phenyl)amino]pyrimidin-4-yl]methylamino]-3-oxidanyl-propanoic acid' 
408.450   1 ? ? ? ? 
3 water       nat water                                                                                                            
18.015    1 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Immune checkpoint,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       
;AFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNA
ALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYAAALEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;AFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNA
ALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPYAAALEHHHHHH
;
_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~{S})-2-[[6-methoxy-2-[(2-methyl-3-phenyl-phenyl)amino]pyrimidin-4-yl]methylamino]-3-oxidanyl-propanoic acid' A1D9R 
3 water                                                                                                            HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   PHE n 
1 3   THR n 
1 4   VAL n 
1 5   THR n 
1 6   VAL n 
1 7   PRO n 
1 8   LYS n 
1 9   ASP n 
1 10  LEU n 
1 11  TYR n 
1 12  VAL n 
1 13  VAL n 
1 14  GLU n 
1 15  TYR n 
1 16  GLY n 
1 17  SER n 
1 18  ASN n 
1 19  MET n 
1 20  THR n 
1 21  ILE n 
1 22  GLU n 
1 23  CYS n 
1 24  LYS n 
1 25  PHE n 
1 26  PRO n 
1 27  VAL n 
1 28  GLU n 
1 29  LYS n 
1 30  GLN n 
1 31  LEU n 
1 32  ASP n 
1 33  LEU n 
1 34  ALA n 
1 35  ALA n 
1 36  LEU n 
1 37  ILE n 
1 38  VAL n 
1 39  TYR n 
1 40  TRP n 
1 41  GLU n 
1 42  MET n 
1 43  GLU n 
1 44  ASP n 
1 45  LYS n 
1 46  ASN n 
1 47  ILE n 
1 48  ILE n 
1 49  GLN n 
1 50  PHE n 
1 51  VAL n 
1 52  HIS n 
1 53  GLY n 
1 54  GLU n 
1 55  GLU n 
1 56  ASP n 
1 57  LEU n 
1 58  LYS n 
1 59  VAL n 
1 60  GLN n 
1 61  HIS n 
1 62  SER n 
1 63  SER n 
1 64  TYR n 
1 65  ARG n 
1 66  GLN n 
1 67  ARG n 
1 68  ALA n 
1 69  ARG n 
1 70  LEU n 
1 71  LEU n 
1 72  LYS n 
1 73  ASP n 
1 74  GLN n 
1 75  LEU n 
1 76  SER n 
1 77  LEU n 
1 78  GLY n 
1 79  ASN n 
1 80  ALA n 
1 81  ALA n 
1 82  LEU n 
1 83  GLN n 
1 84  ILE n 
1 85  THR n 
1 86  ASP n 
1 87  VAL n 
1 88  LYS n 
1 89  LEU n 
1 90  GLN n 
1 91  ASP n 
1 92  ALA n 
1 93  GLY n 
1 94  VAL n 
1 95  TYR n 
1 96  ARG n 
1 97  CYS n 
1 98  MET n 
1 99  ILE n 
1 100 SER n 
1 101 TYR n 
1 102 GLY n 
1 103 GLY n 
1 104 ALA n 
1 105 ASP n 
1 106 TYR n 
1 107 LYS n 
1 108 ARG n 
1 109 ILE n 
1 110 THR n 
1 111 VAL n 
1 112 LYS n 
1 113 VAL n 
1 114 ASN n 
1 115 ALA n 
1 116 PRO n 
1 117 TYR n 
1 118 ALA n 
1 119 ALA n 
1 120 ALA n 
1 121 LEU n 
1 122 GLU n 
1 123 HIS n 
1 124 HIS n 
1 125 HIS n 
1 126 HIS n 
1 127 HIS n 
1 128 HIS 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                   128 
_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 
A1D9R non-polymer         . 
'(2~{S})-2-[[6-methoxy-2-[(2-methyl-3-phenyl-phenyl)amino]pyrimidin-4-yl]methylamino]-3-oxidanyl-propanoic acid' ? 'C22 H24 N4 O4' 
408.450 
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   ALA 1   18  18  ALA ALA A . n 
A 1 2   PHE 2   19  19  PHE PHE A . n 
A 1 3   THR 3   20  20  THR THR A . n 
A 1 4   VAL 4   21  21  VAL VAL A . n 
A 1 5   THR 5   22  22  THR THR A . n 
A 1 6   VAL 6   23  23  VAL VAL A . n 
A 1 7   PRO 7   24  24  PRO PRO A . n 
A 1 8   LYS 8   25  25  LYS LYS A . n 
A 1 9   ASP 9   26  26  ASP ASP A . n 
A 1 10  LEU 10  27  27  LEU LEU A . n 
A 1 11  TYR 11  28  28  TYR TYR A . n 
A 1 12  VAL 12  29  29  VAL VAL A . n 
A 1 13  VAL 13  30  30  VAL VAL A . n 
A 1 14  GLU 14  31  31  GLU GLU A . n 
A 1 15  TYR 15  32  32  TYR TYR A . n 
A 1 16  GLY 16  33  33  GLY GLY A . n 
A 1 17  SER 17  34  34  SER SER A . n 
A 1 18  ASN 18  35  35  ASN ASN A . n 
A 1 19  MET 19  36  36  MET MET A . n 
A 1 20  THR 20  37  37  THR THR A . n 
A 1 21  ILE 21  38  38  ILE ILE A . n 
A 1 22  GLU 22  39  39  GLU GLU A . n 
A 1 23  CYS 23  40  40  CYS CYS A . n 
A 1 24  LYS 24  41  41  LYS LYS A . n 
A 1 25  PHE 25  42  42  PHE PHE A . n 
A 1 26  PRO 26  43  43  PRO PRO A . n 
A 1 27  VAL 27  44  44  VAL VAL A . n 
A 1 28  GLU 28  45  45  GLU ALA A . n 
A 1 29  LYS 29  46  46  LYS ALA A . n 
A 1 30  GLN 30  47  47  GLN ALA A . n 
A 1 31  LEU 31  48  48  LEU LEU A . n 
A 1 32  ASP 32  49  49  ASP ASP A . n 
A 1 33  LEU 33  50  50  LEU LEU A . n 
A 1 34  ALA 34  51  51  ALA ALA A . n 
A 1 35  ALA 35  52  52  ALA ALA A . n 
A 1 36  LEU 36  53  53  LEU LEU A . n 
A 1 37  ILE 37  54  54  ILE ILE A . n 
A 1 38  VAL 38  55  55  VAL VAL A . n 
A 1 39  TYR 39  56  56  TYR TYR A . n 
A 1 40  TRP 40  57  57  TRP TRP A . n 
A 1 41  GLU 41  58  58  GLU GLU A . n 
A 1 42  MET 42  59  59  MET MET A . n 
A 1 43  GLU 43  60  60  GLU GLU A . n 
A 1 44  ASP 44  61  61  ASP ASP A . n 
A 1 45  LYS 45  62  62  LYS LYS A . n 
A 1 46  ASN 46  63  63  ASN ASN A . n 
A 1 47  ILE 47  64  64  ILE ILE A . n 
A 1 48  ILE 48  65  65  ILE ILE A . n 
A 1 49  GLN 49  66  66  GLN GLN A . n 
A 1 50  PHE 50  67  67  PHE PHE A . n 
A 1 51  VAL 51  68  68  VAL VAL A . n 
A 1 52  HIS 52  69  69  HIS HIS A . n 
A 1 53  GLY 53  70  70  GLY GLY A . n 
A 1 54  GLU 54  71  71  GLU GLU A . n 
A 1 55  GLU 55  72  72  GLU GLU A . n 
A 1 56  ASP 56  73  73  ASP ASP A . n 
A 1 57  LEU 57  74  74  LEU LEU A . n 
A 1 58  LYS 58  75  75  LYS ALA A . n 
A 1 59  VAL 59  76  76  VAL VAL A . n 
A 1 60  GLN 60  77  77  GLN GLN A . n 
A 1 61  HIS 61  78  78  HIS HIS A . n 
A 1 62  SER 62  79  79  SER SER A . n 
A 1 63  SER 63  80  80  SER SER A . n 
A 1 64  TYR 64  81  81  TYR TYR A . n 
A 1 65  ARG 65  82  82  ARG ARG A . n 
A 1 66  GLN 66  83  83  GLN ALA A . n 
A 1 67  ARG 67  84  84  ARG ARG A . n 
A 1 68  ALA 68  85  85  ALA ALA A . n 
A 1 69  ARG 69  86  86  ARG ARG A . n 
A 1 70  LEU 70  87  87  LEU LEU A . n 
A 1 71  LEU 71  88  88  LEU LEU A . n 
A 1 72  LYS 72  89  89  LYS LYS A . n 
A 1 73  ASP 73  90  90  ASP ASP A . n 
A 1 74  GLN 74  91  91  GLN GLN A . n 
A 1 75  LEU 75  92  92  LEU LEU A . n 
A 1 76  SER 76  93  93  SER SER A . n 
A 1 77  LEU 77  94  94  LEU LEU A . n 
A 1 78  GLY 78  95  95  GLY GLY A . n 
A 1 79  ASN 79  96  96  ASN ASN A . n 
A 1 80  ALA 80  97  97  ALA ALA A . n 
A 1 81  ALA 81  98  98  ALA ALA A . n 
A 1 82  LEU 82  99  99  LEU LEU A . n 
A 1 83  GLN 83  100 100 GLN GLN A . n 
A 1 84  ILE 84  101 101 ILE ILE A . n 
A 1 85  THR 85  102 102 THR THR A . n 
A 1 86  ASP 86  103 103 ASP ASP A . n 
A 1 87  VAL 87  104 104 VAL VAL A . n 
A 1 88  LYS 88  105 105 LYS ALA A . n 
A 1 89  LEU 89  106 106 LEU LEU A . n 
A 1 90  GLN 90  107 107 GLN GLN A . n 
A 1 91  ASP 91  108 108 ASP ASP A . n 
A 1 92  ALA 92  109 109 ALA ALA A . n 
A 1 93  GLY 93  110 110 GLY GLY A . n 
A 1 94  VAL 94  111 111 VAL VAL A . n 
A 1 95  TYR 95  112 112 TYR TYR A . n 
A 1 96  ARG 96  113 113 ARG ARG A . n 
A 1 97  CYS 97  114 114 CYS CYS A . n 
A 1 98  MET 98  115 115 MET MET A . n 
A 1 99  ILE 99  116 116 ILE ILE A . n 
A 1 100 SER 100 117 117 SER SER A . n 
A 1 101 TYR 101 118 118 TYR TYR A . n 
A 1 102 GLY 102 119 119 GLY GLY A . n 
A 1 103 GLY 103 120 120 GLY GLY A . n 
A 1 104 ALA 104 121 121 ALA ALA A . n 
A 1 105 ASP 105 122 122 ASP ASP A . n 
A 1 106 TYR 106 123 123 TYR TYR A . n 
A 1 107 LYS 107 124 124 LYS LYS A . n 
A 1 108 ARG 108 125 125 ARG ARG A . n 
A 1 109 ILE 109 126 126 ILE ILE A . n 
A 1 110 THR 110 127 127 THR THR A . n 
A 1 111 VAL 111 128 128 VAL VAL A . n 
A 1 112 LYS 112 129 129 LYS ALA A . n 
A 1 113 VAL 113 130 130 VAL VAL A . n 
A 1 114 ASN 114 131 131 ASN ASN A . n 
A 1 115 ALA 115 132 132 ALA ALA A . n 
A 1 116 PRO 116 133 133 PRO PRO A . n 
A 1 117 TYR 117 134 134 TYR TYR A . n 
A 1 118 ALA 118 135 135 ALA ALA A . n 
A 1 119 ALA 119 136 136 ALA ALA A . n 
A 1 120 ALA 120 137 137 ALA ALA A . n 
A 1 121 LEU 121 138 138 LEU LEU A . n 
A 1 122 GLU 122 139 139 GLU GLU A . n 
A 1 123 HIS 123 140 140 HIS HIS A . n 
A 1 124 HIS 124 141 141 HIS HIS A . n 
A 1 125 HIS 125 142 142 HIS HIS A . n 
A 1 126 HIS 126 143 ?   ?   ?   A . n 
A 1 127 HIS 127 144 ?   ?   ?   A . n 
A 1 128 HIS 128 145 ?   ?   ?   A . n 
B 1 1   ALA 1   18  18  ALA ALA B . n 
B 1 2   PHE 2   19  19  PHE PHE B . n 
B 1 3   THR 3   20  20  THR THR B . n 
B 1 4   VAL 4   21  21  VAL VAL B . n 
B 1 5   THR 5   22  22  THR THR B . n 
B 1 6   VAL 6   23  23  VAL VAL B . n 
B 1 7   PRO 7   24  24  PRO PRO B . n 
B 1 8   LYS 8   25  25  LYS LYS B . n 
B 1 9   ASP 9   26  26  ASP ASP B . n 
B 1 10  LEU 10  27  27  LEU LEU B . n 
B 1 11  TYR 11  28  28  TYR TYR B . n 
B 1 12  VAL 12  29  29  VAL VAL B . n 
B 1 13  VAL 13  30  30  VAL VAL B . n 
B 1 14  GLU 14  31  31  GLU GLU B . n 
B 1 15  TYR 15  32  32  TYR TYR B . n 
B 1 16  GLY 16  33  33  GLY GLY B . n 
B 1 17  SER 17  34  34  SER SER B . n 
B 1 18  ASN 18  35  35  ASN ASN B . n 
B 1 19  MET 19  36  36  MET MET B . n 
B 1 20  THR 20  37  37  THR THR B . n 
B 1 21  ILE 21  38  38  ILE ILE B . n 
B 1 22  GLU 22  39  39  GLU GLU B . n 
B 1 23  CYS 23  40  40  CYS CYS B . n 
B 1 24  LYS 24  41  41  LYS LYS B . n 
B 1 25  PHE 25  42  42  PHE PHE B . n 
B 1 26  PRO 26  43  43  PRO PRO B . n 
B 1 27  VAL 27  44  44  VAL VAL B . n 
B 1 28  GLU 28  45  45  GLU GLU B . n 
B 1 29  LYS 29  46  46  LYS ALA B . n 
B 1 30  GLN 30  47  47  GLN ALA B . n 
B 1 31  LEU 31  48  48  LEU LEU B . n 
B 1 32  ASP 32  49  49  ASP ASP B . n 
B 1 33  LEU 33  50  50  LEU LEU B . n 
B 1 34  ALA 34  51  51  ALA ALA B . n 
B 1 35  ALA 35  52  52  ALA ALA B . n 
B 1 36  LEU 36  53  53  LEU LEU B . n 
B 1 37  ILE 37  54  54  ILE ILE B . n 
B 1 38  VAL 38  55  55  VAL VAL B . n 
B 1 39  TYR 39  56  56  TYR TYR B . n 
B 1 40  TRP 40  57  57  TRP TRP B . n 
B 1 41  GLU 41  58  58  GLU GLU B . n 
B 1 42  MET 42  59  59  MET MET B . n 
B 1 43  GLU 43  60  60  GLU GLU B . n 
B 1 44  ASP 44  61  61  ASP ASP B . n 
B 1 45  LYS 45  62  62  LYS ALA B . n 
B 1 46  ASN 46  63  63  ASN ASN B . n 
B 1 47  ILE 47  64  64  ILE ILE B . n 
B 1 48  ILE 48  65  65  ILE ILE B . n 
B 1 49  GLN 49  66  66  GLN GLN B . n 
B 1 50  PHE 50  67  67  PHE PHE B . n 
B 1 51  VAL 51  68  68  VAL VAL B . n 
B 1 52  HIS 52  69  69  HIS HIS B . n 
B 1 53  GLY 53  70  70  GLY GLY B . n 
B 1 54  GLU 54  71  71  GLU ALA B . n 
B 1 55  GLU 55  72  72  GLU GLU B . n 
B 1 56  ASP 56  73  73  ASP ASP B . n 
B 1 57  LEU 57  74  74  LEU LEU B . n 
B 1 58  LYS 58  75  75  LYS ALA B . n 
B 1 59  VAL 59  76  76  VAL VAL B . n 
B 1 60  GLN 60  77  77  GLN GLN B . n 
B 1 61  HIS 61  78  78  HIS HIS B . n 
B 1 62  SER 62  79  79  SER SER B . n 
B 1 63  SER 63  80  80  SER SER B . n 
B 1 64  TYR 64  81  81  TYR TYR B . n 
B 1 65  ARG 65  82  82  ARG ALA B . n 
B 1 66  GLN 66  83  83  GLN GLN B . n 
B 1 67  ARG 67  84  84  ARG ARG B . n 
B 1 68  ALA 68  85  85  ALA ALA B . n 
B 1 69  ARG 69  86  86  ARG ARG B . n 
B 1 70  LEU 70  87  87  LEU LEU B . n 
B 1 71  LEU 71  88  88  LEU LEU B . n 
B 1 72  LYS 72  89  89  LYS ALA B . n 
B 1 73  ASP 73  90  90  ASP ASP B . n 
B 1 74  GLN 74  91  91  GLN GLN B . n 
B 1 75  LEU 75  92  92  LEU LEU B . n 
B 1 76  SER 76  93  93  SER SER B . n 
B 1 77  LEU 77  94  94  LEU ALA B . n 
B 1 78  GLY 78  95  95  GLY GLY B . n 
B 1 79  ASN 79  96  96  ASN ASN B . n 
B 1 80  ALA 80  97  97  ALA ALA B . n 
B 1 81  ALA 81  98  98  ALA ALA B . n 
B 1 82  LEU 82  99  99  LEU LEU B . n 
B 1 83  GLN 83  100 100 GLN GLN B . n 
B 1 84  ILE 84  101 101 ILE ILE B . n 
B 1 85  THR 85  102 102 THR THR B . n 
B 1 86  ASP 86  103 103 ASP ASP B . n 
B 1 87  VAL 87  104 104 VAL VAL B . n 
B 1 88  LYS 88  105 105 LYS ALA B . n 
B 1 89  LEU 89  106 106 LEU LEU B . n 
B 1 90  GLN 90  107 107 GLN GLN B . n 
B 1 91  ASP 91  108 108 ASP ASP B . n 
B 1 92  ALA 92  109 109 ALA ALA B . n 
B 1 93  GLY 93  110 110 GLY GLY B . n 
B 1 94  VAL 94  111 111 VAL VAL B . n 
B 1 95  TYR 95  112 112 TYR TYR B . n 
B 1 96  ARG 96  113 113 ARG ARG B . n 
B 1 97  CYS 97  114 114 CYS CYS B . n 
B 1 98  MET 98  115 115 MET MET B . n 
B 1 99  ILE 99  116 116 ILE ILE B . n 
B 1 100 SER 100 117 117 SER SER B . n 
B 1 101 TYR 101 118 118 TYR TYR B . n 
B 1 102 GLY 102 119 119 GLY GLY B . n 
B 1 103 GLY 103 120 120 GLY GLY B . n 
B 1 104 ALA 104 121 121 ALA ALA B . n 
B 1 105 ASP 105 122 122 ASP ASP B . n 
B 1 106 TYR 106 123 123 TYR TYR B . n 
B 1 107 LYS 107 124 124 LYS LYS B . n 
B 1 108 ARG 108 125 125 ARG ARG B . n 
B 1 109 ILE 109 126 126 ILE ILE B . n 
B 1 110 THR 110 127 127 THR THR B . n 
B 1 111 VAL 111 128 128 VAL VAL B . n 
B 1 112 LYS 112 129 129 LYS LYS B . n 
B 1 113 VAL 113 130 130 VAL VAL B . n 
B 1 114 ASN 114 131 131 ASN ASN B . n 
B 1 115 ALA 115 132 132 ALA ALA B . n 
B 1 116 PRO 116 133 133 PRO PRO B . n 
B 1 117 TYR 117 134 134 TYR TYR B . n 
B 1 118 ALA 118 135 135 ALA ALA B . n 
B 1 119 ALA 119 136 136 ALA ALA B . n 
B 1 120 ALA 120 137 137 ALA ALA B . n 
B 1 121 LEU 121 138 138 LEU LEU B . n 
B 1 122 GLU 122 139 139 GLU GLU B . n 
B 1 123 HIS 123 140 140 HIS HIS B . n 
B 1 124 HIS 124 141 141 HIS HIS B . n 
B 1 125 HIS 125 142 142 HIS HIS B . n 
B 1 126 HIS 126 143 143 HIS HIS B . n 
B 1 127 HIS 127 144 ?   ?   ?   B . n 
B 1 128 HIS 128 145 ?   ?   ?   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 A1D9R 1 201 201 A1D9R LIG B . 
D 3 HOH   1 301 1   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 45  ? CG  ? A GLU 28  CG  
2  1 Y 1 A GLU 45  ? CD  ? A GLU 28  CD  
3  1 Y 1 A GLU 45  ? OE1 ? A GLU 28  OE1 
4  1 Y 1 A GLU 45  ? OE2 ? A GLU 28  OE2 
5  1 Y 1 A LYS 46  ? CG  ? A LYS 29  CG  
6  1 Y 1 A LYS 46  ? CD  ? A LYS 29  CD  
7  1 Y 1 A LYS 46  ? CE  ? A LYS 29  CE  
8  1 Y 1 A LYS 46  ? NZ  ? A LYS 29  NZ  
9  1 Y 1 A GLN 47  ? CG  ? A GLN 30  CG  
10 1 Y 1 A GLN 47  ? CD  ? A GLN 30  CD  
11 1 Y 1 A GLN 47  ? OE1 ? A GLN 30  OE1 
12 1 Y 1 A GLN 47  ? NE2 ? A GLN 30  NE2 
13 1 Y 1 A LYS 75  ? CG  ? A LYS 58  CG  
14 1 Y 1 A LYS 75  ? CD  ? A LYS 58  CD  
15 1 Y 1 A LYS 75  ? CE  ? A LYS 58  CE  
16 1 Y 1 A LYS 75  ? NZ  ? A LYS 58  NZ  
17 1 Y 1 A GLN 83  ? CG  ? A GLN 66  CG  
18 1 Y 1 A GLN 83  ? CD  ? A GLN 66  CD  
19 1 Y 1 A GLN 83  ? OE1 ? A GLN 66  OE1 
20 1 Y 1 A GLN 83  ? NE2 ? A GLN 66  NE2 
21 1 Y 1 A LYS 105 ? CG  ? A LYS 88  CG  
22 1 Y 1 A LYS 105 ? CD  ? A LYS 88  CD  
23 1 Y 1 A LYS 105 ? CE  ? A LYS 88  CE  
24 1 Y 1 A LYS 105 ? NZ  ? A LYS 88  NZ  
25 1 Y 1 A LYS 129 ? CG  ? A LYS 112 CG  
26 1 Y 1 A LYS 129 ? CD  ? A LYS 112 CD  
27 1 Y 1 A LYS 129 ? CE  ? A LYS 112 CE  
28 1 Y 1 A LYS 129 ? NZ  ? A LYS 112 NZ  
29 1 Y 1 B LYS 46  ? CG  ? B LYS 29  CG  
30 1 Y 1 B LYS 46  ? CD  ? B LYS 29  CD  
31 1 Y 1 B LYS 46  ? CE  ? B LYS 29  CE  
32 1 Y 1 B LYS 46  ? NZ  ? B LYS 29  NZ  
33 1 Y 1 B GLN 47  ? CG  ? B GLN 30  CG  
34 1 Y 1 B GLN 47  ? CD  ? B GLN 30  CD  
35 1 Y 1 B GLN 47  ? OE1 ? B GLN 30  OE1 
36 1 Y 1 B GLN 47  ? NE2 ? B GLN 30  NE2 
37 1 Y 1 B LYS 62  ? CG  ? B LYS 45  CG  
38 1 Y 1 B LYS 62  ? CD  ? B LYS 45  CD  
39 1 Y 1 B LYS 62  ? CE  ? B LYS 45  CE  
40 1 Y 1 B LYS 62  ? NZ  ? B LYS 45  NZ  
41 1 Y 1 B GLU 71  ? CG  ? B GLU 54  CG  
42 1 Y 1 B GLU 71  ? CD  ? B GLU 54  CD  
43 1 Y 1 B GLU 71  ? OE1 ? B GLU 54  OE1 
44 1 Y 1 B GLU 71  ? OE2 ? B GLU 54  OE2 
45 1 Y 1 B LYS 75  ? CG  ? B LYS 58  CG  
46 1 Y 1 B LYS 75  ? CD  ? B LYS 58  CD  
47 1 Y 1 B LYS 75  ? CE  ? B LYS 58  CE  
48 1 Y 1 B LYS 75  ? NZ  ? B LYS 58  NZ  
49 1 Y 1 B ARG 82  ? CG  ? B ARG 65  CG  
50 1 Y 1 B ARG 82  ? CD  ? B ARG 65  CD  
51 1 Y 1 B ARG 82  ? NE  ? B ARG 65  NE  
52 1 Y 1 B ARG 82  ? CZ  ? B ARG 65  CZ  
53 1 Y 1 B ARG 82  ? NH1 ? B ARG 65  NH1 
54 1 Y 1 B ARG 82  ? NH2 ? B ARG 65  NH2 
55 1 Y 1 B LYS 89  ? CG  ? B LYS 72  CG  
56 1 Y 1 B LYS 89  ? CD  ? B LYS 72  CD  
57 1 Y 1 B LYS 89  ? CE  ? B LYS 72  CE  
58 1 Y 1 B LYS 89  ? NZ  ? B LYS 72  NZ  
59 1 Y 1 B LEU 94  ? CG  ? B LEU 77  CG  
60 1 Y 1 B LEU 94  ? CD1 ? B LEU 77  CD1 
61 1 Y 1 B LEU 94  ? CD2 ? B LEU 77  CD2 
62 1 Y 1 B LYS 105 ? CG  ? B LYS 88  CG  
63 1 Y 1 B LYS 105 ? CD  ? B LYS 88  CD  
64 1 Y 1 B LYS 105 ? CE  ? B LYS 88  CE  
65 1 Y 1 B LYS 105 ? NZ  ? B LYS 88  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 reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? AutoSol ? ? ? .                    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                     9INU 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     32.096 
_cell.length_a_esd                 ? 
_cell.length_b                     83.603 
_cell.length_b_esd                 ? 
_cell.length_c                     96.838 
_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                         9INU 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                18 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 2 21 21' 
_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                   9INU 
_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             2.21 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          44.41 
_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, HANGING 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    'Tris, potassium sodium tartrate tetrahydrate' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289.15 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2024-01-27 
_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   0.978530 
_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 BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.978530 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9INU 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.7 
_reflns.d_resolution_low                               48.42 
_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                                     94058 
_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                           99.86 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                12.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          17 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.2223 
_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                        ? 
# 
_reflns_shell.d_res_high                                    2.7 
_reflns_shell.d_res_low                                     2.797 
_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                             9235 
_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                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.955 
_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                                  0.9106 
_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               ? 
# 
_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                                 9INU 
_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                            2.70 
_refine.ls_d_res_low                             48.42 
_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                     13782 
_refine.ls_number_reflns_R_free                  1377 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.88 
_refine.ls_percent_reflns_R_free                 9.99 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2483 
_refine.ls_R_factor_R_free                       0.2871 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2440 
_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                          1.35 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5C3T 
_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                 34.22 
_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                            0.41 
_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.pdbx_number_atoms_protein        1949 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.number_atoms_solvent             1 
_refine_hist.number_atoms_total               1980 
_refine_hist.d_res_high                       2.70 
_refine_hist.d_res_low                        48.42 
# 
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  ? 2022 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.721  ? 2752 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 19.277 ? 702  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 311  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.004  ? 352  ? 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' 2.70 2.80  . . 130 1217 100.00 . . . . 0.3592 . . . . . . . . . . . 0.3931 
'X-RAY DIFFRACTION' 2.80 2.91  . . 135 1274 100.00 . . . . 0.3382 . . . . . . . . . . . 0.3914 
'X-RAY DIFFRACTION' 2.91 3.04  . . 139 1207 100.00 . . . . 0.3306 . . . . . . . . . . . 0.3825 
'X-RAY DIFFRACTION' 3.04 3.20  . . 140 1271 100.00 . . . . 0.3015 . . . . . . . . . . . 0.4162 
'X-RAY DIFFRACTION' 3.20 3.40  . . 136 1220 100.00 . . . . 0.2831 . . . . . . . . . . . 0.3243 
'X-RAY DIFFRACTION' 3.40 3.66  . . 142 1237 100.00 . . . . 0.2426 . . . . . . . . . . . 0.3037 
'X-RAY DIFFRACTION' 3.66 4.03  . . 141 1258 100.00 . . . . 0.2323 . . . . . . . . . . . 0.2837 
'X-RAY DIFFRACTION' 4.03 4.62  . . 140 1240 100.00 . . . . 0.1890 . . . . . . . . . . . 0.2045 
'X-RAY DIFFRACTION' 4.62 5.81  . . 133 1232 100.00 . . . . 0.1968 . . . . . . . . . . . 0.2566 
'X-RAY DIFFRACTION' 5.82 48.42 . . 141 1249 100.00 . . . . 0.2264 . . . . . . . . . . . 0.2294 
# 
_struct.entry_id                     9INU 
_struct.title                        'Novel PD-L1/VISTA dual inhibitor as potential immunotherapy agents' 
_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        9INU 
_struct_keywords.text            'Immune checkpoint, Small molecular inhibitor, Dimer, IMMUNE SYSTEM' 
_struct_keywords.pdbx_keywords   'IMMUNE SYSTEM' 
# 
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 ? 
# 
_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   
;AFTVTVPKDLYVVEYGSNMTIECKFPVEKQLDLAALIVYWEMEDKNIIQFVHGEEDLKVQHSSYRQRARLLKDQLSLGNA
ALQITDVKLQDAGVYRCMISYGGADYKRITVKVNAPY
;
_struct_ref.pdbx_align_begin           18 
# 
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 9INU A 1 ? 117 ? Q9NZQ7 18 ? 134 ? 18 134 
2 1 9INU B 1 ? 117 ? Q9NZQ7 18 ? 134 ? 18 134 
# 
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 9INU ALA A 118 ? UNP Q9NZQ7 ? ? 'expression tag' 135 1  
1 9INU ALA A 119 ? UNP Q9NZQ7 ? ? 'expression tag' 136 2  
1 9INU ALA A 120 ? UNP Q9NZQ7 ? ? 'expression tag' 137 3  
1 9INU LEU A 121 ? UNP Q9NZQ7 ? ? 'expression tag' 138 4  
1 9INU GLU A 122 ? UNP Q9NZQ7 ? ? 'expression tag' 139 5  
1 9INU HIS A 123 ? UNP Q9NZQ7 ? ? 'expression tag' 140 6  
1 9INU HIS A 124 ? UNP Q9NZQ7 ? ? 'expression tag' 141 7  
1 9INU HIS A 125 ? UNP Q9NZQ7 ? ? 'expression tag' 142 8  
1 9INU HIS A 126 ? UNP Q9NZQ7 ? ? 'expression tag' 143 9  
1 9INU HIS A 127 ? UNP Q9NZQ7 ? ? 'expression tag' 144 10 
1 9INU HIS A 128 ? UNP Q9NZQ7 ? ? 'expression tag' 145 11 
2 9INU ALA B 118 ? UNP Q9NZQ7 ? ? 'expression tag' 135 12 
2 9INU ALA B 119 ? UNP Q9NZQ7 ? ? 'expression tag' 136 13 
2 9INU ALA B 120 ? UNP Q9NZQ7 ? ? 'expression tag' 137 14 
2 9INU LEU B 121 ? UNP Q9NZQ7 ? ? 'expression tag' 138 15 
2 9INU GLU B 122 ? UNP Q9NZQ7 ? ? 'expression tag' 139 16 
2 9INU HIS B 123 ? UNP Q9NZQ7 ? ? 'expression tag' 140 17 
2 9INU HIS B 124 ? UNP Q9NZQ7 ? ? 'expression tag' 141 18 
2 9INU HIS B 125 ? UNP Q9NZQ7 ? ? 'expression tag' 142 19 
2 9INU HIS B 126 ? UNP Q9NZQ7 ? ? 'expression tag' 143 20 
2 9INU HIS B 127 ? UNP Q9NZQ7 ? ? 'expression tag' 144 21 
2 9INU HIS B 128 ? UNP Q9NZQ7 ? ? 'expression tag' 145 22 
# 
_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 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_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 HIS A 61  ? ARG A 65  ? HIS A 78  ARG A 82  5 ? 5  
HELX_P HELX_P2 AA2 LEU A 71  ? LEU A 77  ? LEU A 88  LEU A 94  1 ? 7  
HELX_P HELX_P3 AA3 LYS A 88  ? ALA A 92  ? LYS A 105 ALA A 109 5 ? 5  
HELX_P HELX_P4 AA4 PRO A 116 ? HIS A 125 ? PRO A 133 HIS A 142 1 ? 10 
HELX_P HELX_P5 AA5 LEU B 57  ? GLN B 60  ? LEU B 74  GLN B 77  5 ? 4  
HELX_P HELX_P6 AA6 HIS B 61  ? ARG B 65  ? HIS B 78  ARG B 82  5 ? 5  
HELX_P HELX_P7 AA7 LYS B 72  ? LEU B 77  ? LYS B 89  LEU B 94  5 ? 6  
HELX_P HELX_P8 AA8 LYS B 88  ? ALA B 92  ? LYS B 105 ALA B 109 5 ? 5  
HELX_P HELX_P9 AA9 PRO B 116 ? HIS B 125 ? PRO B 133 HIS B 142 1 ? 10 
# 
_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 23 SG ? ? ? 1_555 A CYS 97 SG ? ? A CYS 40 A CYS 114 1_555 ? ? ? ? ? ? ? 2.034 ? ? 
disulf2 disulf ? ? B CYS 23 SG ? ? ? 1_555 B CYS 97 SG ? ? B CYS 40 B CYS 114 1_555 ? ? ? ? ? ? ? 2.033 ? ? 
# 
_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 23 ? CYS A 97 ? CYS A 40 ? 1_555 CYS A 114 ? 1_555 SG SG . . . None 'Disulfide bridge' 
2 CYS B 23 ? CYS B 97 ? CYS B 40 ? 1_555 CYS B 114 ? 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 10  ? GLU A 14  ? LEU A 27  GLU A 31  
AA1 2 ALA A 104 ? ASN A 114 ? ALA A 121 ASN A 131 
AA1 3 GLY A 93  ? SER A 100 ? GLY A 110 SER A 117 
AA1 4 ILE A 37  ? MET A 42  ? ILE A 54  MET A 59  
AA1 5 LYS A 45  ? VAL A 51  ? LYS A 62  VAL A 68  
AA1 6 GLU A 54  ? GLU A 55  ? GLU A 71  GLU A 72  
AA2 1 MET A 19  ? LYS A 24  ? MET A 36  LYS A 41  
AA2 2 ASN A 79  ? ILE A 84  ? ASN A 96  ILE A 101 
AA2 3 ALA A 68  ? LEU A 70  ? ALA A 85  LEU A 87  
AA3 1 LEU B 10  ? GLU B 14  ? LEU B 27  GLU B 31  
AA3 2 ASP B 105 ? ASN B 114 ? ASP B 122 ASN B 131 
AA3 3 GLY B 93  ? SER B 100 ? GLY B 110 SER B 117 
AA3 4 ILE B 37  ? MET B 42  ? ILE B 54  MET B 59  
AA3 5 ASN B 46  ? VAL B 51  ? ASN B 63  VAL B 68  
AA3 6 GLU B 54  ? GLU B 55  ? GLU B 71  GLU B 72  
AA4 1 MET B 19  ? LYS B 24  ? MET B 36  LYS B 41  
AA4 2 ASN B 79  ? ILE B 84  ? ASN B 96  ILE B 101 
AA4 3 ALA B 68  ? LEU B 70  ? ALA B 85  LEU B 87  
# 
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 11  ? N TYR A 28  O LYS A 112 ? O LYS A 129 
AA1 2 3 O ILE A 109 ? O ILE A 126 N TYR A 95  ? N TYR A 112 
AA1 3 4 O ARG A 96  ? O ARG A 113 N GLU A 41  ? N GLU A 58  
AA1 4 5 N VAL A 38  ? N VAL A 55  O PHE A 50  ? O PHE A 67  
AA1 5 6 N VAL A 51  ? N VAL A 68  O GLU A 54  ? O GLU A 71  
AA2 1 2 N ILE A 21  ? N ILE A 38  O LEU A 82  ? O LEU A 99  
AA2 2 3 O GLN A 83  ? O GLN A 100 N ARG A 69  ? N ARG A 86  
AA3 1 2 N TYR B 11  ? N TYR B 28  O LYS B 112 ? O LYS B 129 
AA3 2 3 O ILE B 109 ? O ILE B 126 N TYR B 95  ? N TYR B 112 
AA3 3 4 O MET B 98  ? O MET B 115 N TYR B 39  ? N TYR B 56  
AA3 4 5 N VAL B 38  ? N VAL B 55  O PHE B 50  ? O PHE B 67  
AA3 5 6 N VAL B 51  ? N VAL B 68  O GLU B 54  ? O GLU B 71  
AA4 1 2 N ILE B 21  ? N ILE B 38  O LEU B 82  ? O LEU B 99  
AA4 2 3 O GLN B 83  ? O GLN B 100 N ARG B 69  ? N ARG B 86  
# 
_pdbx_entry_details.entry_id                   9INU 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
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 LYS A 46 ? ? -126.01 -71.50  
2 1 GLN A 47 ? ? -111.12 -165.88 
3 1 HIS A 69 ? ? 52.28   -132.59 
4 1 GLN A 83 ? ? 59.02   6.27    
5 1 LYS B 46 ? ? -117.76 -84.20  
6 1 LEU B 94 ? ? -99.78  31.41   
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         5.2073 
_pdbx_refine_tls.origin_y         17.8986 
_pdbx_refine_tls.origin_z         3.3648 
_pdbx_refine_tls.T[1][1]          0.3933 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0138 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          0.0262 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3806 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          -0.0323 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.6319 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.4072 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          -0.0658 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.0128 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          0.7373 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.2402 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.0496 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          0.0663 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          -0.0198 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.1812 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          0.0152 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          0.0801 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          -0.0435 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.1040 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          0.0413 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          -0.1875 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.beg_auth_asym_id    ? 
_pdbx_refine_tls_group.beg_auth_seq_id     ? 
_pdbx_refine_tls_group.beg_PDB_ins_code    ? 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    ? 
_pdbx_refine_tls_group.end_auth_seq_id     ? 
_pdbx_refine_tls_group.end_PDB_ins_code    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   all 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A HIS 143 ? A HIS 126 
2 1 Y 1 A HIS 144 ? A HIS 127 
3 1 Y 1 A HIS 145 ? A HIS 128 
4 1 Y 1 B HIS 144 ? B HIS 127 
5 1 Y 1 B HIS 145 ? B HIS 128 
# 
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 
A1D9R C10  C Y N 1   
A1D9R C13  C N N 2   
A1D9R C15  C Y N 3   
A1D9R C17  C Y N 4   
A1D9R C21  C N N 5   
A1D9R C24  C N N 6   
A1D9R C01  C Y N 7   
A1D9R C02  C Y N 8   
A1D9R C03  C Y N 9   
A1D9R C04  C Y N 10  
A1D9R C05  C Y N 11  
A1D9R C06  C Y N 12  
A1D9R C07  C Y N 13  
A1D9R C08  C Y N 14  
A1D9R C09  C Y N 15  
A1D9R C11  C Y N 16  
A1D9R C12  C Y N 17  
A1D9R C18  C Y N 18  
A1D9R C19  C Y N 19  
A1D9R C23  C N S 20  
A1D9R C25  C N N 21  
A1D9R C30  C N N 22  
A1D9R N14  N N N 23  
A1D9R N16  N Y N 24  
A1D9R N20  N Y N 25  
A1D9R N22  N N N 26  
A1D9R O26  O N N 27  
A1D9R O27  O N N 28  
A1D9R O28  O N N 29  
A1D9R O29  O N N 30  
A1D9R H1   H N N 31  
A1D9R H2   H N N 32  
A1D9R H3   H N N 33  
A1D9R H4   H N N 34  
A1D9R H5   H N N 35  
A1D9R H6   H N N 36  
A1D9R H7   H N N 37  
A1D9R H8   H N N 38  
A1D9R H9   H N N 39  
A1D9R H10  H N N 40  
A1D9R H11  H N N 41  
A1D9R H12  H N N 42  
A1D9R H13  H N N 43  
A1D9R H14  H N N 44  
A1D9R H15  H N N 45  
A1D9R H16  H N N 46  
A1D9R H17  H N N 47  
A1D9R H18  H N N 48  
A1D9R H19  H N N 49  
A1D9R H20  H N N 50  
A1D9R H21  H N N 51  
A1D9R H22  H N N 52  
A1D9R H24  H N N 53  
A1D9R H25  H N N 54  
ALA   N    N N N 55  
ALA   CA   C N S 56  
ALA   C    C N N 57  
ALA   O    O N N 58  
ALA   CB   C N N 59  
ALA   OXT  O N N 60  
ALA   H    H N N 61  
ALA   H2   H N N 62  
ALA   HA   H N N 63  
ALA   HB1  H N N 64  
ALA   HB2  H N N 65  
ALA   HB3  H N N 66  
ALA   HXT  H N N 67  
ARG   N    N N N 68  
ARG   CA   C N S 69  
ARG   C    C N N 70  
ARG   O    O N N 71  
ARG   CB   C N N 72  
ARG   CG   C N N 73  
ARG   CD   C N N 74  
ARG   NE   N N N 75  
ARG   CZ   C N N 76  
ARG   NH1  N N N 77  
ARG   NH2  N N N 78  
ARG   OXT  O N N 79  
ARG   H    H N N 80  
ARG   H2   H N N 81  
ARG   HA   H N N 82  
ARG   HB2  H N N 83  
ARG   HB3  H N N 84  
ARG   HG2  H N N 85  
ARG   HG3  H N N 86  
ARG   HD2  H N N 87  
ARG   HD3  H N N 88  
ARG   HE   H N N 89  
ARG   HH11 H N N 90  
ARG   HH12 H N N 91  
ARG   HH21 H N N 92  
ARG   HH22 H N N 93  
ARG   HXT  H N N 94  
ASN   N    N N N 95  
ASN   CA   C N S 96  
ASN   C    C N N 97  
ASN   O    O N N 98  
ASN   CB   C N N 99  
ASN   CG   C N N 100 
ASN   OD1  O N N 101 
ASN   ND2  N N N 102 
ASN   OXT  O N N 103 
ASN   H    H N N 104 
ASN   H2   H N N 105 
ASN   HA   H N N 106 
ASN   HB2  H N N 107 
ASN   HB3  H N N 108 
ASN   HD21 H N N 109 
ASN   HD22 H N N 110 
ASN   HXT  H N N 111 
ASP   N    N N N 112 
ASP   CA   C N S 113 
ASP   C    C N N 114 
ASP   O    O N N 115 
ASP   CB   C N N 116 
ASP   CG   C N N 117 
ASP   OD1  O N N 118 
ASP   OD2  O N N 119 
ASP   OXT  O N N 120 
ASP   H    H N N 121 
ASP   H2   H N N 122 
ASP   HA   H N N 123 
ASP   HB2  H N N 124 
ASP   HB3  H N N 125 
ASP   HD2  H N N 126 
ASP   HXT  H N N 127 
CYS   N    N N N 128 
CYS   CA   C N R 129 
CYS   C    C N N 130 
CYS   O    O N N 131 
CYS   CB   C N N 132 
CYS   SG   S N N 133 
CYS   OXT  O N N 134 
CYS   H    H N N 135 
CYS   H2   H N N 136 
CYS   HA   H N N 137 
CYS   HB2  H N N 138 
CYS   HB3  H N N 139 
CYS   HG   H N N 140 
CYS   HXT  H N N 141 
GLN   N    N N N 142 
GLN   CA   C N S 143 
GLN   C    C N N 144 
GLN   O    O N N 145 
GLN   CB   C N N 146 
GLN   CG   C N N 147 
GLN   CD   C N N 148 
GLN   OE1  O N N 149 
GLN   NE2  N N N 150 
GLN   OXT  O N N 151 
GLN   H    H N N 152 
GLN   H2   H N N 153 
GLN   HA   H N N 154 
GLN   HB2  H N N 155 
GLN   HB3  H N N 156 
GLN   HG2  H N N 157 
GLN   HG3  H N N 158 
GLN   HE21 H N N 159 
GLN   HE22 H N N 160 
GLN   HXT  H N N 161 
GLU   N    N N N 162 
GLU   CA   C N S 163 
GLU   C    C N N 164 
GLU   O    O N N 165 
GLU   CB   C N N 166 
GLU   CG   C N N 167 
GLU   CD   C N N 168 
GLU   OE1  O N N 169 
GLU   OE2  O N N 170 
GLU   OXT  O N N 171 
GLU   H    H N N 172 
GLU   H2   H N N 173 
GLU   HA   H N N 174 
GLU   HB2  H N N 175 
GLU   HB3  H N N 176 
GLU   HG2  H N N 177 
GLU   HG3  H N N 178 
GLU   HE2  H N N 179 
GLU   HXT  H N N 180 
GLY   N    N N N 181 
GLY   CA   C N N 182 
GLY   C    C N N 183 
GLY   O    O N N 184 
GLY   OXT  O N N 185 
GLY   H    H N N 186 
GLY   H2   H N N 187 
GLY   HA2  H N N 188 
GLY   HA3  H N N 189 
GLY   HXT  H N N 190 
HIS   N    N N N 191 
HIS   CA   C N S 192 
HIS   C    C N N 193 
HIS   O    O N N 194 
HIS   CB   C N N 195 
HIS   CG   C Y N 196 
HIS   ND1  N Y N 197 
HIS   CD2  C Y N 198 
HIS   CE1  C Y N 199 
HIS   NE2  N Y N 200 
HIS   OXT  O N N 201 
HIS   H    H N N 202 
HIS   H2   H N N 203 
HIS   HA   H N N 204 
HIS   HB2  H N N 205 
HIS   HB3  H N N 206 
HIS   HD1  H N N 207 
HIS   HD2  H N N 208 
HIS   HE1  H N N 209 
HIS   HE2  H N N 210 
HIS   HXT  H N N 211 
HOH   O    O N N 212 
HOH   H1   H N N 213 
HOH   H2   H N N 214 
ILE   N    N N N 215 
ILE   CA   C N S 216 
ILE   C    C N N 217 
ILE   O    O N N 218 
ILE   CB   C N S 219 
ILE   CG1  C N N 220 
ILE   CG2  C N N 221 
ILE   CD1  C N N 222 
ILE   OXT  O N N 223 
ILE   H    H N N 224 
ILE   H2   H N N 225 
ILE   HA   H N N 226 
ILE   HB   H N N 227 
ILE   HG12 H N N 228 
ILE   HG13 H N N 229 
ILE   HG21 H N N 230 
ILE   HG22 H N N 231 
ILE   HG23 H N N 232 
ILE   HD11 H N N 233 
ILE   HD12 H N N 234 
ILE   HD13 H N N 235 
ILE   HXT  H N N 236 
LEU   N    N N N 237 
LEU   CA   C N S 238 
LEU   C    C N N 239 
LEU   O    O N N 240 
LEU   CB   C N N 241 
LEU   CG   C N N 242 
LEU   CD1  C N N 243 
LEU   CD2  C N N 244 
LEU   OXT  O N N 245 
LEU   H    H N N 246 
LEU   H2   H N N 247 
LEU   HA   H N N 248 
LEU   HB2  H N N 249 
LEU   HB3  H N N 250 
LEU   HG   H N N 251 
LEU   HD11 H N N 252 
LEU   HD12 H N N 253 
LEU   HD13 H N N 254 
LEU   HD21 H N N 255 
LEU   HD22 H N N 256 
LEU   HD23 H N N 257 
LEU   HXT  H N N 258 
LYS   N    N N N 259 
LYS   CA   C N S 260 
LYS   C    C N N 261 
LYS   O    O N N 262 
LYS   CB   C N N 263 
LYS   CG   C N N 264 
LYS   CD   C N N 265 
LYS   CE   C N N 266 
LYS   NZ   N N N 267 
LYS   OXT  O N N 268 
LYS   H    H N N 269 
LYS   H2   H N N 270 
LYS   HA   H N N 271 
LYS   HB2  H N N 272 
LYS   HB3  H N N 273 
LYS   HG2  H N N 274 
LYS   HG3  H N N 275 
LYS   HD2  H N N 276 
LYS   HD3  H N N 277 
LYS   HE2  H N N 278 
LYS   HE3  H N N 279 
LYS   HZ1  H N N 280 
LYS   HZ2  H N N 281 
LYS   HZ3  H N N 282 
LYS   HXT  H N N 283 
MET   N    N N N 284 
MET   CA   C N S 285 
MET   C    C N N 286 
MET   O    O N N 287 
MET   CB   C N N 288 
MET   CG   C N N 289 
MET   SD   S N N 290 
MET   CE   C N N 291 
MET   OXT  O N N 292 
MET   H    H N N 293 
MET   H2   H N N 294 
MET   HA   H N N 295 
MET   HB2  H N N 296 
MET   HB3  H N N 297 
MET   HG2  H N N 298 
MET   HG3  H N N 299 
MET   HE1  H N N 300 
MET   HE2  H N N 301 
MET   HE3  H N N 302 
MET   HXT  H N N 303 
PHE   N    N N N 304 
PHE   CA   C N S 305 
PHE   C    C N N 306 
PHE   O    O N N 307 
PHE   CB   C N N 308 
PHE   CG   C Y N 309 
PHE   CD1  C Y N 310 
PHE   CD2  C Y N 311 
PHE   CE1  C Y N 312 
PHE   CE2  C Y N 313 
PHE   CZ   C Y N 314 
PHE   OXT  O N N 315 
PHE   H    H N N 316 
PHE   H2   H N N 317 
PHE   HA   H N N 318 
PHE   HB2  H N N 319 
PHE   HB3  H N N 320 
PHE   HD1  H N N 321 
PHE   HD2  H N N 322 
PHE   HE1  H N N 323 
PHE   HE2  H N N 324 
PHE   HZ   H N N 325 
PHE   HXT  H N N 326 
PRO   N    N N N 327 
PRO   CA   C N S 328 
PRO   C    C N N 329 
PRO   O    O N N 330 
PRO   CB   C N N 331 
PRO   CG   C N N 332 
PRO   CD   C N N 333 
PRO   OXT  O N N 334 
PRO   H    H N N 335 
PRO   HA   H N N 336 
PRO   HB2  H N N 337 
PRO   HB3  H N N 338 
PRO   HG2  H N N 339 
PRO   HG3  H N N 340 
PRO   HD2  H N N 341 
PRO   HD3  H N N 342 
PRO   HXT  H N N 343 
SER   N    N N N 344 
SER   CA   C N S 345 
SER   C    C N N 346 
SER   O    O N N 347 
SER   CB   C N N 348 
SER   OG   O N N 349 
SER   OXT  O N N 350 
SER   H    H N N 351 
SER   H2   H N N 352 
SER   HA   H N N 353 
SER   HB2  H N N 354 
SER   HB3  H N N 355 
SER   HG   H N N 356 
SER   HXT  H N N 357 
THR   N    N N N 358 
THR   CA   C N S 359 
THR   C    C N N 360 
THR   O    O N N 361 
THR   CB   C N R 362 
THR   OG1  O N N 363 
THR   CG2  C N N 364 
THR   OXT  O N N 365 
THR   H    H N N 366 
THR   H2   H N N 367 
THR   HA   H N N 368 
THR   HB   H N N 369 
THR   HG1  H N N 370 
THR   HG21 H N N 371 
THR   HG22 H N N 372 
THR   HG23 H N N 373 
THR   HXT  H N N 374 
TRP   N    N N N 375 
TRP   CA   C N S 376 
TRP   C    C N N 377 
TRP   O    O N N 378 
TRP   CB   C N N 379 
TRP   CG   C Y N 380 
TRP   CD1  C Y N 381 
TRP   CD2  C Y N 382 
TRP   NE1  N Y N 383 
TRP   CE2  C Y N 384 
TRP   CE3  C Y N 385 
TRP   CZ2  C Y N 386 
TRP   CZ3  C Y N 387 
TRP   CH2  C Y N 388 
TRP   OXT  O N N 389 
TRP   H    H N N 390 
TRP   H2   H N N 391 
TRP   HA   H N N 392 
TRP   HB2  H N N 393 
TRP   HB3  H N N 394 
TRP   HD1  H N N 395 
TRP   HE1  H N N 396 
TRP   HE3  H N N 397 
TRP   HZ2  H N N 398 
TRP   HZ3  H N N 399 
TRP   HH2  H N N 400 
TRP   HXT  H N N 401 
TYR   N    N N N 402 
TYR   CA   C N S 403 
TYR   C    C N N 404 
TYR   O    O N N 405 
TYR   CB   C N N 406 
TYR   CG   C Y N 407 
TYR   CD1  C Y N 408 
TYR   CD2  C Y N 409 
TYR   CE1  C Y N 410 
TYR   CE2  C Y N 411 
TYR   CZ   C Y N 412 
TYR   OH   O N N 413 
TYR   OXT  O N N 414 
TYR   H    H N N 415 
TYR   H2   H N N 416 
TYR   HA   H N N 417 
TYR   HB2  H N N 418 
TYR   HB3  H N N 419 
TYR   HD1  H N N 420 
TYR   HD2  H N N 421 
TYR   HE1  H N N 422 
TYR   HE2  H N N 423 
TYR   HH   H N N 424 
TYR   HXT  H N N 425 
VAL   N    N N N 426 
VAL   CA   C N S 427 
VAL   C    C N N 428 
VAL   O    O N N 429 
VAL   CB   C N N 430 
VAL   CG1  C N N 431 
VAL   CG2  C N N 432 
VAL   OXT  O N N 433 
VAL   H    H N N 434 
VAL   H2   H N N 435 
VAL   HA   H N N 436 
VAL   HB   H N N 437 
VAL   HG11 H N N 438 
VAL   HG12 H N N 439 
VAL   HG13 H N N 440 
VAL   HG21 H N N 441 
VAL   HG22 H N N 442 
VAL   HG23 H N N 443 
VAL   HXT  H N N 444 
# 
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 
A1D9R C06 C01  doub Y N 1   
A1D9R C06 C05  sing Y N 2   
A1D9R C01 C02  sing Y N 3   
A1D9R O27 C24  doub N N 4   
A1D9R C30 O29  sing N N 5   
A1D9R C05 C04  doub Y N 6   
A1D9R C13 C12  sing N N 7   
A1D9R O28 C24  sing N N 8   
A1D9R O29 C17  sing N N 9   
A1D9R C24 C23  sing N N 10  
A1D9R C02 C03  doub Y N 11  
A1D9R O26 C25  sing N N 12  
A1D9R C17 N16  doub Y N 13  
A1D9R C17 C18  sing Y N 14  
A1D9R N16 C15  sing Y N 15  
A1D9R C04 C03  sing Y N 16  
A1D9R C04 C07  sing N N 17  
A1D9R C12 C07  doub Y N 18  
A1D9R C12 C11  sing Y N 19  
A1D9R C18 C19  doub Y N 20  
A1D9R N14 C15  sing N N 21  
A1D9R N14 C11  sing N N 22  
A1D9R C15 N20  doub Y N 23  
A1D9R C25 C23  sing N N 24  
A1D9R C07 C08  sing Y N 25  
A1D9R C23 N22  sing N N 26  
A1D9R C11 C10  doub Y N 27  
A1D9R C19 N20  sing Y N 28  
A1D9R C19 C21  sing N N 29  
A1D9R N22 C21  sing N N 30  
A1D9R C08 C09  doub Y N 31  
A1D9R C10 C09  sing Y N 32  
A1D9R C10 H1   sing N N 33  
A1D9R C13 H2   sing N N 34  
A1D9R C13 H3   sing N N 35  
A1D9R C13 H4   sing N N 36  
A1D9R C21 H5   sing N N 37  
A1D9R C21 H6   sing N N 38  
A1D9R C01 H7   sing N N 39  
A1D9R C02 H8   sing N N 40  
A1D9R C03 H9   sing N N 41  
A1D9R C05 H10  sing N N 42  
A1D9R C06 H11  sing N N 43  
A1D9R C08 H12  sing N N 44  
A1D9R C09 H13  sing N N 45  
A1D9R C18 H14  sing N N 46  
A1D9R C23 H15  sing N N 47  
A1D9R C25 H16  sing N N 48  
A1D9R C25 H17  sing N N 49  
A1D9R C30 H18  sing N N 50  
A1D9R C30 H19  sing N N 51  
A1D9R C30 H20  sing N N 52  
A1D9R N14 H21  sing N N 53  
A1D9R N22 H22  sing N N 54  
A1D9R O26 H24  sing N N 55  
A1D9R O28 H25  sing N N 56  
ALA   N   CA   sing N N 57  
ALA   N   H    sing N N 58  
ALA   N   H2   sing N N 59  
ALA   CA  C    sing N N 60  
ALA   CA  CB   sing N N 61  
ALA   CA  HA   sing N N 62  
ALA   C   O    doub N N 63  
ALA   C   OXT  sing N N 64  
ALA   CB  HB1  sing N N 65  
ALA   CB  HB2  sing N N 66  
ALA   CB  HB3  sing N N 67  
ALA   OXT HXT  sing N N 68  
ARG   N   CA   sing N N 69  
ARG   N   H    sing N N 70  
ARG   N   H2   sing N N 71  
ARG   CA  C    sing N N 72  
ARG   CA  CB   sing N N 73  
ARG   CA  HA   sing N N 74  
ARG   C   O    doub N N 75  
ARG   C   OXT  sing N N 76  
ARG   CB  CG   sing N N 77  
ARG   CB  HB2  sing N N 78  
ARG   CB  HB3  sing N N 79  
ARG   CG  CD   sing N N 80  
ARG   CG  HG2  sing N N 81  
ARG   CG  HG3  sing N N 82  
ARG   CD  NE   sing N N 83  
ARG   CD  HD2  sing N N 84  
ARG   CD  HD3  sing N N 85  
ARG   NE  CZ   sing N N 86  
ARG   NE  HE   sing N N 87  
ARG   CZ  NH1  sing N N 88  
ARG   CZ  NH2  doub N N 89  
ARG   NH1 HH11 sing N N 90  
ARG   NH1 HH12 sing N N 91  
ARG   NH2 HH21 sing N N 92  
ARG   NH2 HH22 sing N N 93  
ARG   OXT HXT  sing N N 94  
ASN   N   CA   sing N N 95  
ASN   N   H    sing N N 96  
ASN   N   H2   sing N N 97  
ASN   CA  C    sing N N 98  
ASN   CA  CB   sing N N 99  
ASN   CA  HA   sing N N 100 
ASN   C   O    doub N N 101 
ASN   C   OXT  sing N N 102 
ASN   CB  CG   sing N N 103 
ASN   CB  HB2  sing N N 104 
ASN   CB  HB3  sing N N 105 
ASN   CG  OD1  doub N N 106 
ASN   CG  ND2  sing N N 107 
ASN   ND2 HD21 sing N N 108 
ASN   ND2 HD22 sing N N 109 
ASN   OXT HXT  sing N N 110 
ASP   N   CA   sing N N 111 
ASP   N   H    sing N N 112 
ASP   N   H2   sing N N 113 
ASP   CA  C    sing N N 114 
ASP   CA  CB   sing N N 115 
ASP   CA  HA   sing N N 116 
ASP   C   O    doub N N 117 
ASP   C   OXT  sing N N 118 
ASP   CB  CG   sing N N 119 
ASP   CB  HB2  sing N N 120 
ASP   CB  HB3  sing N N 121 
ASP   CG  OD1  doub N N 122 
ASP   CG  OD2  sing N N 123 
ASP   OD2 HD2  sing N N 124 
ASP   OXT HXT  sing N N 125 
CYS   N   CA   sing N N 126 
CYS   N   H    sing N N 127 
CYS   N   H2   sing N N 128 
CYS   CA  C    sing N N 129 
CYS   CA  CB   sing N N 130 
CYS   CA  HA   sing N N 131 
CYS   C   O    doub N N 132 
CYS   C   OXT  sing N N 133 
CYS   CB  SG   sing N N 134 
CYS   CB  HB2  sing N N 135 
CYS   CB  HB3  sing N N 136 
CYS   SG  HG   sing N N 137 
CYS   OXT HXT  sing N N 138 
GLN   N   CA   sing N N 139 
GLN   N   H    sing N N 140 
GLN   N   H2   sing N N 141 
GLN   CA  C    sing N N 142 
GLN   CA  CB   sing N N 143 
GLN   CA  HA   sing N N 144 
GLN   C   O    doub N N 145 
GLN   C   OXT  sing N N 146 
GLN   CB  CG   sing N N 147 
GLN   CB  HB2  sing N N 148 
GLN   CB  HB3  sing N N 149 
GLN   CG  CD   sing N N 150 
GLN   CG  HG2  sing N N 151 
GLN   CG  HG3  sing N N 152 
GLN   CD  OE1  doub N N 153 
GLN   CD  NE2  sing N N 154 
GLN   NE2 HE21 sing N N 155 
GLN   NE2 HE22 sing N N 156 
GLN   OXT HXT  sing N N 157 
GLU   N   CA   sing N N 158 
GLU   N   H    sing N N 159 
GLU   N   H2   sing N N 160 
GLU   CA  C    sing N N 161 
GLU   CA  CB   sing N N 162 
GLU   CA  HA   sing N N 163 
GLU   C   O    doub N N 164 
GLU   C   OXT  sing N N 165 
GLU   CB  CG   sing N N 166 
GLU   CB  HB2  sing N N 167 
GLU   CB  HB3  sing N N 168 
GLU   CG  CD   sing N N 169 
GLU   CG  HG2  sing N N 170 
GLU   CG  HG3  sing N N 171 
GLU   CD  OE1  doub N N 172 
GLU   CD  OE2  sing N N 173 
GLU   OE2 HE2  sing N N 174 
GLU   OXT HXT  sing N N 175 
GLY   N   CA   sing N N 176 
GLY   N   H    sing N N 177 
GLY   N   H2   sing N N 178 
GLY   CA  C    sing N N 179 
GLY   CA  HA2  sing N N 180 
GLY   CA  HA3  sing N N 181 
GLY   C   O    doub N N 182 
GLY   C   OXT  sing N N 183 
GLY   OXT HXT  sing N N 184 
HIS   N   CA   sing N N 185 
HIS   N   H    sing N N 186 
HIS   N   H2   sing N N 187 
HIS   CA  C    sing N N 188 
HIS   CA  CB   sing N N 189 
HIS   CA  HA   sing N N 190 
HIS   C   O    doub N N 191 
HIS   C   OXT  sing N N 192 
HIS   CB  CG   sing N N 193 
HIS   CB  HB2  sing N N 194 
HIS   CB  HB3  sing N N 195 
HIS   CG  ND1  sing Y N 196 
HIS   CG  CD2  doub Y N 197 
HIS   ND1 CE1  doub Y N 198 
HIS   ND1 HD1  sing N N 199 
HIS   CD2 NE2  sing Y N 200 
HIS   CD2 HD2  sing N N 201 
HIS   CE1 NE2  sing Y N 202 
HIS   CE1 HE1  sing N N 203 
HIS   NE2 HE2  sing N N 204 
HIS   OXT HXT  sing N N 205 
HOH   O   H1   sing N N 206 
HOH   O   H2   sing N N 207 
ILE   N   CA   sing N N 208 
ILE   N   H    sing N N 209 
ILE   N   H2   sing N N 210 
ILE   CA  C    sing N N 211 
ILE   CA  CB   sing N N 212 
ILE   CA  HA   sing N N 213 
ILE   C   O    doub N N 214 
ILE   C   OXT  sing N N 215 
ILE   CB  CG1  sing N N 216 
ILE   CB  CG2  sing N N 217 
ILE   CB  HB   sing N N 218 
ILE   CG1 CD1  sing N N 219 
ILE   CG1 HG12 sing N N 220 
ILE   CG1 HG13 sing N N 221 
ILE   CG2 HG21 sing N N 222 
ILE   CG2 HG22 sing N N 223 
ILE   CG2 HG23 sing N N 224 
ILE   CD1 HD11 sing N N 225 
ILE   CD1 HD12 sing N N 226 
ILE   CD1 HD13 sing N N 227 
ILE   OXT HXT  sing N N 228 
LEU   N   CA   sing N N 229 
LEU   N   H    sing N N 230 
LEU   N   H2   sing N N 231 
LEU   CA  C    sing N N 232 
LEU   CA  CB   sing N N 233 
LEU   CA  HA   sing N N 234 
LEU   C   O    doub N N 235 
LEU   C   OXT  sing N N 236 
LEU   CB  CG   sing N N 237 
LEU   CB  HB2  sing N N 238 
LEU   CB  HB3  sing N N 239 
LEU   CG  CD1  sing N N 240 
LEU   CG  CD2  sing N N 241 
LEU   CG  HG   sing N N 242 
LEU   CD1 HD11 sing N N 243 
LEU   CD1 HD12 sing N N 244 
LEU   CD1 HD13 sing N N 245 
LEU   CD2 HD21 sing N N 246 
LEU   CD2 HD22 sing N N 247 
LEU   CD2 HD23 sing N N 248 
LEU   OXT HXT  sing N N 249 
LYS   N   CA   sing N N 250 
LYS   N   H    sing N N 251 
LYS   N   H2   sing N N 252 
LYS   CA  C    sing N N 253 
LYS   CA  CB   sing N N 254 
LYS   CA  HA   sing N N 255 
LYS   C   O    doub N N 256 
LYS   C   OXT  sing N N 257 
LYS   CB  CG   sing N N 258 
LYS   CB  HB2  sing N N 259 
LYS   CB  HB3  sing N N 260 
LYS   CG  CD   sing N N 261 
LYS   CG  HG2  sing N N 262 
LYS   CG  HG3  sing N N 263 
LYS   CD  CE   sing N N 264 
LYS   CD  HD2  sing N N 265 
LYS   CD  HD3  sing N N 266 
LYS   CE  NZ   sing N N 267 
LYS   CE  HE2  sing N N 268 
LYS   CE  HE3  sing N N 269 
LYS   NZ  HZ1  sing N N 270 
LYS   NZ  HZ2  sing N N 271 
LYS   NZ  HZ3  sing N N 272 
LYS   OXT HXT  sing N N 273 
MET   N   CA   sing N N 274 
MET   N   H    sing N N 275 
MET   N   H2   sing N N 276 
MET   CA  C    sing N N 277 
MET   CA  CB   sing N N 278 
MET   CA  HA   sing N N 279 
MET   C   O    doub N N 280 
MET   C   OXT  sing N N 281 
MET   CB  CG   sing N N 282 
MET   CB  HB2  sing N N 283 
MET   CB  HB3  sing N N 284 
MET   CG  SD   sing N N 285 
MET   CG  HG2  sing N N 286 
MET   CG  HG3  sing N N 287 
MET   SD  CE   sing N N 288 
MET   CE  HE1  sing N N 289 
MET   CE  HE2  sing N N 290 
MET   CE  HE3  sing N N 291 
MET   OXT HXT  sing N N 292 
PHE   N   CA   sing N N 293 
PHE   N   H    sing N N 294 
PHE   N   H2   sing N N 295 
PHE   CA  C    sing N N 296 
PHE   CA  CB   sing N N 297 
PHE   CA  HA   sing N N 298 
PHE   C   O    doub N N 299 
PHE   C   OXT  sing N N 300 
PHE   CB  CG   sing N N 301 
PHE   CB  HB2  sing N N 302 
PHE   CB  HB3  sing N N 303 
PHE   CG  CD1  doub Y N 304 
PHE   CG  CD2  sing Y N 305 
PHE   CD1 CE1  sing Y N 306 
PHE   CD1 HD1  sing N N 307 
PHE   CD2 CE2  doub Y N 308 
PHE   CD2 HD2  sing N N 309 
PHE   CE1 CZ   doub Y N 310 
PHE   CE1 HE1  sing N N 311 
PHE   CE2 CZ   sing Y N 312 
PHE   CE2 HE2  sing N N 313 
PHE   CZ  HZ   sing N N 314 
PHE   OXT HXT  sing N N 315 
PRO   N   CA   sing N N 316 
PRO   N   CD   sing N N 317 
PRO   N   H    sing N N 318 
PRO   CA  C    sing N N 319 
PRO   CA  CB   sing N N 320 
PRO   CA  HA   sing N N 321 
PRO   C   O    doub N N 322 
PRO   C   OXT  sing N N 323 
PRO   CB  CG   sing N N 324 
PRO   CB  HB2  sing N N 325 
PRO   CB  HB3  sing N N 326 
PRO   CG  CD   sing N N 327 
PRO   CG  HG2  sing N N 328 
PRO   CG  HG3  sing N N 329 
PRO   CD  HD2  sing N N 330 
PRO   CD  HD3  sing N N 331 
PRO   OXT HXT  sing N N 332 
SER   N   CA   sing N N 333 
SER   N   H    sing N N 334 
SER   N   H2   sing N N 335 
SER   CA  C    sing N N 336 
SER   CA  CB   sing N N 337 
SER   CA  HA   sing N N 338 
SER   C   O    doub N N 339 
SER   C   OXT  sing N N 340 
SER   CB  OG   sing N N 341 
SER   CB  HB2  sing N N 342 
SER   CB  HB3  sing N N 343 
SER   OG  HG   sing N N 344 
SER   OXT HXT  sing N N 345 
THR   N   CA   sing N N 346 
THR   N   H    sing N N 347 
THR   N   H2   sing N N 348 
THR   CA  C    sing N N 349 
THR   CA  CB   sing N N 350 
THR   CA  HA   sing N N 351 
THR   C   O    doub N N 352 
THR   C   OXT  sing N N 353 
THR   CB  OG1  sing N N 354 
THR   CB  CG2  sing N N 355 
THR   CB  HB   sing N N 356 
THR   OG1 HG1  sing N N 357 
THR   CG2 HG21 sing N N 358 
THR   CG2 HG22 sing N N 359 
THR   CG2 HG23 sing N N 360 
THR   OXT HXT  sing N N 361 
TRP   N   CA   sing N N 362 
TRP   N   H    sing N N 363 
TRP   N   H2   sing N N 364 
TRP   CA  C    sing N N 365 
TRP   CA  CB   sing N N 366 
TRP   CA  HA   sing N N 367 
TRP   C   O    doub N N 368 
TRP   C   OXT  sing N N 369 
TRP   CB  CG   sing N N 370 
TRP   CB  HB2  sing N N 371 
TRP   CB  HB3  sing N N 372 
TRP   CG  CD1  doub Y N 373 
TRP   CG  CD2  sing Y N 374 
TRP   CD1 NE1  sing Y N 375 
TRP   CD1 HD1  sing N N 376 
TRP   CD2 CE2  doub Y N 377 
TRP   CD2 CE3  sing Y N 378 
TRP   NE1 CE2  sing Y N 379 
TRP   NE1 HE1  sing N N 380 
TRP   CE2 CZ2  sing Y N 381 
TRP   CE3 CZ3  doub Y N 382 
TRP   CE3 HE3  sing N N 383 
TRP   CZ2 CH2  doub Y N 384 
TRP   CZ2 HZ2  sing N N 385 
TRP   CZ3 CH2  sing Y N 386 
TRP   CZ3 HZ3  sing N N 387 
TRP   CH2 HH2  sing N N 388 
TRP   OXT HXT  sing N N 389 
TYR   N   CA   sing N N 390 
TYR   N   H    sing N N 391 
TYR   N   H2   sing N N 392 
TYR   CA  C    sing N N 393 
TYR   CA  CB   sing N N 394 
TYR   CA  HA   sing N N 395 
TYR   C   O    doub N N 396 
TYR   C   OXT  sing N N 397 
TYR   CB  CG   sing N N 398 
TYR   CB  HB2  sing N N 399 
TYR   CB  HB3  sing N N 400 
TYR   CG  CD1  doub Y N 401 
TYR   CG  CD2  sing Y N 402 
TYR   CD1 CE1  sing Y N 403 
TYR   CD1 HD1  sing N N 404 
TYR   CD2 CE2  doub Y N 405 
TYR   CD2 HD2  sing N N 406 
TYR   CE1 CZ   doub Y N 407 
TYR   CE1 HE1  sing N N 408 
TYR   CE2 CZ   sing Y N 409 
TYR   CE2 HE2  sing N N 410 
TYR   CZ  OH   sing N N 411 
TYR   OH  HH   sing N N 412 
TYR   OXT HXT  sing N N 413 
VAL   N   CA   sing N N 414 
VAL   N   H    sing N N 415 
VAL   N   H2   sing N N 416 
VAL   CA  C    sing N N 417 
VAL   CA  CB   sing N N 418 
VAL   CA  HA   sing N N 419 
VAL   C   O    doub N N 420 
VAL   C   OXT  sing N N 421 
VAL   CB  CG1  sing N N 422 
VAL   CB  CG2  sing N N 423 
VAL   CB  HB   sing N N 424 
VAL   CG1 HG11 sing N N 425 
VAL   CG1 HG12 sing N N 426 
VAL   CG1 HG13 sing N N 427 
VAL   CG2 HG21 sing N N 428 
VAL   CG2 HG22 sing N N 429 
VAL   CG2 HG23 sing N N 430 
VAL   OXT HXT  sing N N 431 
# 
_pdbx_audit_support.funding_organization   'Not funded' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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   5C3T 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9INU 
_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]   0.031157 
_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]   0.011961 
_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]   0.010327 
_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 
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   . ALA   A 1 1   ? 18.754  30.805  8.207   1.00 97.79  ? 18  ALA   A N   1 
ATOM   2    C CA  . ALA   A 1 1   ? 17.361  31.151  7.954   1.00 97.42  ? 18  ALA   A CA  1 
ATOM   3    C C   . ALA   A 1 1   ? 16.439  30.491  8.973   1.00 89.69  ? 18  ALA   A C   1 
ATOM   4    O O   . ALA   A 1 1   ? 16.889  29.999  10.008  1.00 92.91  ? 18  ALA   A O   1 
ATOM   5    C CB  . ALA   A 1 1   ? 16.962  30.749  6.541   1.00 95.78  ? 18  ALA   A CB  1 
ATOM   6    N N   . PHE   A 1 2   ? 15.143  30.489  8.673   1.00 71.28  ? 19  PHE   A N   1 
ATOM   7    C CA  . PHE   A 1 2   ? 14.152  29.869  9.543   1.00 65.49  ? 19  PHE   A CA  1 
ATOM   8    C C   . PHE   A 1 2   ? 14.204  28.356  9.373   1.00 65.57  ? 19  PHE   A C   1 
ATOM   9    O O   . PHE   A 1 2   ? 13.945  27.839  8.280   1.00 62.99  ? 19  PHE   A O   1 
ATOM   10   C CB  . PHE   A 1 2   ? 12.761  30.406  9.219   1.00 53.83  ? 19  PHE   A CB  1 
ATOM   11   C CG  . PHE   A 1 2   ? 11.673  29.874  10.111  1.00 57.65  ? 19  PHE   A CG  1 
ATOM   12   C CD1 . PHE   A 1 2   ? 10.979  28.723  9.774   1.00 54.53  ? 19  PHE   A CD1 1 
ATOM   13   C CD2 . PHE   A 1 2   ? 11.330  30.538  11.277  1.00 55.54  ? 19  PHE   A CD2 1 
ATOM   14   C CE1 . PHE   A 1 2   ? 9.975   28.237  10.589  1.00 56.02  ? 19  PHE   A CE1 1 
ATOM   15   C CE2 . PHE   A 1 2   ? 10.325  30.058  12.096  1.00 54.29  ? 19  PHE   A CE2 1 
ATOM   16   C CZ  . PHE   A 1 2   ? 9.647   28.905  11.752  1.00 57.92  ? 19  PHE   A CZ  1 
ATOM   17   N N   . THR   A 1 3   ? 14.534  27.646  10.450  1.00 56.87  ? 20  THR   A N   1 
ATOM   18   C CA  . THR   A 1 3   ? 14.631  26.193  10.433  1.00 60.33  ? 20  THR   A CA  1 
ATOM   19   C C   . THR   A 1 3   ? 13.842  25.629  11.603  1.00 55.90  ? 20  THR   A C   1 
ATOM   20   O O   . THR   A 1 3   ? 13.987  26.096  12.737  1.00 49.43  ? 20  THR   A O   1 
ATOM   21   C CB  . THR   A 1 3   ? 16.089  25.713  10.515  1.00 59.67  ? 20  THR   A CB  1 
ATOM   22   O OG1 . THR   A 1 3   ? 16.477  25.589  11.889  1.00 59.13  ? 20  THR   A OG1 1 
ATOM   23   C CG2 . THR   A 1 3   ? 17.031  26.683  9.813   1.00 61.01  ? 20  THR   A CG2 1 
ATOM   24   N N   . VAL   A 1 4   ? 13.014  24.631  11.325  1.00 55.68  ? 21  VAL   A N   1 
ATOM   25   C CA  . VAL   A 1 4   ? 12.287  23.909  12.362  1.00 55.20  ? 21  VAL   A CA  1 
ATOM   26   C C   . VAL   A 1 4   ? 13.170  22.782  12.874  1.00 53.32  ? 21  VAL   A C   1 
ATOM   27   O O   . VAL   A 1 4   ? 13.817  22.074  12.093  1.00 50.60  ? 21  VAL   A O   1 
ATOM   28   C CB  . VAL   A 1 4   ? 10.946  23.377  11.823  1.00 48.84  ? 21  VAL   A CB  1 
ATOM   29   C CG1 . VAL   A 1 4   ? 10.173  22.662  12.919  1.00 50.68  ? 21  VAL   A CG1 1 
ATOM   30   C CG2 . VAL   A 1 4   ? 10.120  24.516  11.244  1.00 45.59  ? 21  VAL   A CG2 1 
ATOM   31   N N   . THR   A 1 5   ? 13.201  22.614  14.193  1.00 51.55  ? 22  THR   A N   1 
ATOM   32   C CA  . THR   A 1 5   ? 14.057  21.637  14.850  1.00 50.26  ? 22  THR   A CA  1 
ATOM   33   C C   . THR   A 1 5   ? 13.186  20.650  15.614  1.00 56.35  ? 22  THR   A C   1 
ATOM   34   O O   . THR   A 1 5   ? 12.255  21.056  16.320  1.00 56.40  ? 22  THR   A O   1 
ATOM   35   C CB  . THR   A 1 5   ? 15.053  22.307  15.800  1.00 49.43  ? 22  THR   A CB  1 
ATOM   36   O OG1 . THR   A 1 5   ? 14.460  22.447  17.097  1.00 53.68  ? 22  THR   A OG1 1 
ATOM   37   C CG2 . THR   A 1 5   ? 15.457  23.678  15.279  1.00 63.85  ? 22  THR   A CG2 1 
ATOM   38   N N   . VAL   A 1 6   ? 13.491  19.373  15.473  1.00 61.14  ? 23  VAL   A N   1 
ATOM   39   C CA  . VAL   A 1 6   ? 12.774  18.294  16.152  1.00 64.30  ? 23  VAL   A CA  1 
ATOM   40   C C   . VAL   A 1 6   ? 13.709  17.695  17.191  1.00 65.93  ? 23  VAL   A C   1 
ATOM   41   O O   . VAL   A 1 6   ? 14.805  17.231  16.841  1.00 67.52  ? 23  VAL   A O   1 
ATOM   42   C CB  . VAL   A 1 6   ? 12.291  17.234  15.148  1.00 65.58  ? 23  VAL   A CB  1 
ATOM   43   C CG1 . VAL   A 1 6   ? 12.179  15.894  15.804  1.00 66.83  ? 23  VAL   A CG1 1 
ATOM   44   C CG2 . VAL   A 1 6   ? 10.955  17.634  14.550  1.00 67.47  ? 23  VAL   A CG2 1 
ATOM   45   N N   . PRO   A 1 7   ? 13.347  17.700  18.480  1.00 55.45  ? 24  PRO   A N   1 
ATOM   46   C CA  . PRO   A 1 7   ? 14.221  17.091  19.495  1.00 59.69  ? 24  PRO   A CA  1 
ATOM   47   C C   . PRO   A 1 7   ? 14.236  15.573  19.468  1.00 57.69  ? 24  PRO   A C   1 
ATOM   48   O O   . PRO   A 1 7   ? 15.138  14.971  20.062  1.00 50.43  ? 24  PRO   A O   1 
ATOM   49   C CB  . PRO   A 1 7   ? 13.641  17.615  20.814  1.00 56.42  ? 24  PRO   A CB  1 
ATOM   50   C CG  . PRO   A 1 7   ? 12.195  17.829  20.511  1.00 55.69  ? 24  PRO   A CG  1 
ATOM   51   C CD  . PRO   A 1 7   ? 12.128  18.280  19.073  1.00 57.64  ? 24  PRO   A CD  1 
ATOM   52   N N   . LYS   A 1 8   ? 13.273  14.937  18.808  1.00 62.25  ? 25  LYS   A N   1 
ATOM   53   C CA  . LYS   A 1 8   ? 13.186  13.482  18.788  1.00 50.00  ? 25  LYS   A CA  1 
ATOM   54   C C   . LYS   A 1 8   ? 12.511  13.081  17.488  1.00 50.92  ? 25  LYS   A C   1 
ATOM   55   O O   . LYS   A 1 8   ? 11.332  13.385  17.287  1.00 51.89  ? 25  LYS   A O   1 
ATOM   56   C CB  . LYS   A 1 8   ? 12.395  12.988  20.001  1.00 48.96  ? 25  LYS   A CB  1 
ATOM   57   C CG  . LYS   A 1 8   ? 12.341  11.492  20.203  1.00 54.90  ? 25  LYS   A CG  1 
ATOM   58   C CD  . LYS   A 1 8   ? 11.482  11.181  21.422  1.00 56.99  ? 25  LYS   A CD  1 
ATOM   59   C CE  . LYS   A 1 8   ? 11.917  9.905   22.118  1.00 56.82  ? 25  LYS   A CE  1 
ATOM   60   N NZ  . LYS   A 1 8   ? 11.367  8.703   21.439  1.00 49.82  ? 25  LYS   A NZ  1 
ATOM   61   N N   . ASP   A 1 9   ? 13.231  12.352  16.637  1.00 61.77  ? 26  ASP   A N   1 
ATOM   62   C CA  . ASP   A 1 9   ? 12.712  11.978  15.328  1.00 62.26  ? 26  ASP   A CA  1 
ATOM   63   C C   . ASP   A 1 9   ? 11.920  10.679  15.340  1.00 58.94  ? 26  ASP   A C   1 
ATOM   64   O O   . ASP   A 1 9   ? 11.254  10.371  14.347  1.00 57.62  ? 26  ASP   A O   1 
ATOM   65   C CB  . ASP   A 1 9   ? 13.857  11.869  14.314  1.00 64.77  ? 26  ASP   A CB  1 
ATOM   66   C CG  . ASP   A 1 9   ? 14.726  10.649  14.543  1.00 65.20  ? 26  ASP   A CG  1 
ATOM   67   O OD1 . ASP   A 1 9   ? 14.933  10.275  15.717  1.00 65.31  ? 26  ASP   A OD1 1 
ATOM   68   O OD2 . ASP   A 1 9   ? 15.200  10.064  13.547  1.00 69.52  ? 26  ASP   A OD2 1 
ATOM   69   N N   . LEU   A 1 10  ? 11.974  9.916   16.427  1.00 52.52  ? 27  LEU   A N   1 
ATOM   70   C CA  . LEU   A 1 10  ? 11.235  8.667   16.523  1.00 50.58  ? 27  LEU   A CA  1 
ATOM   71   C C   . LEU   A 1 10  ? 10.614  8.567   17.904  1.00 50.04  ? 27  LEU   A C   1 
ATOM   72   O O   . LEU   A 1 10  ? 11.298  8.768   18.912  1.00 46.15  ? 27  LEU   A O   1 
ATOM   73   C CB  . LEU   A 1 10  ? 12.138  7.456   16.260  1.00 55.15  ? 27  LEU   A CB  1 
ATOM   74   C CG  . LEU   A 1 10  ? 11.428  6.101   16.218  1.00 55.29  ? 27  LEU   A CG  1 
ATOM   75   C CD1 . LEU   A 1 10  ? 11.016  5.741   14.798  1.00 54.45  ? 27  LEU   A CD1 1 
ATOM   76   C CD2 . LEU   A 1 10  ? 12.304  5.012   16.817  1.00 51.66  ? 27  LEU   A CD2 1 
ATOM   77   N N   . TYR   A 1 11  ? 9.323   8.253   17.945  1.00 46.96  ? 28  TYR   A N   1 
ATOM   78   C CA  . TYR   A 1 11  ? 8.613   7.998   19.188  1.00 50.91  ? 28  TYR   A CA  1 
ATOM   79   C C   . TYR   A 1 11  ? 8.150   6.550   19.198  1.00 52.81  ? 28  TYR   A C   1 
ATOM   80   O O   . TYR   A 1 11  ? 7.639   6.045   18.193  1.00 50.94  ? 28  TYR   A O   1 
ATOM   81   C CB  . TYR   A 1 11  ? 7.404   8.932   19.353  1.00 47.20  ? 28  TYR   A CB  1 
ATOM   82   C CG  . TYR   A 1 11  ? 7.746   10.391  19.570  1.00 45.95  ? 28  TYR   A CG  1 
ATOM   83   C CD1 . TYR   A 1 11  ? 8.216   11.179  18.528  1.00 46.05  ? 28  TYR   A CD1 1 
ATOM   84   C CD2 . TYR   A 1 11  ? 7.583   10.985  20.816  1.00 48.74  ? 28  TYR   A CD2 1 
ATOM   85   C CE1 . TYR   A 1 11  ? 8.523   12.515  18.720  1.00 48.55  ? 28  TYR   A CE1 1 
ATOM   86   C CE2 . TYR   A 1 11  ? 7.888   12.321  21.018  1.00 52.01  ? 28  TYR   A CE2 1 
ATOM   87   C CZ  . TYR   A 1 11  ? 8.357   13.080  19.966  1.00 47.83  ? 28  TYR   A CZ  1 
ATOM   88   O OH  . TYR   A 1 11  ? 8.661   14.407  20.162  1.00 47.26  ? 28  TYR   A OH  1 
ATOM   89   N N   . VAL   A 1 12  ? 8.323   5.889   20.337  1.00 52.93  ? 29  VAL   A N   1 
ATOM   90   C CA  . VAL   A 1 12  ? 7.863   4.521   20.534  1.00 49.53  ? 29  VAL   A CA  1 
ATOM   91   C C   . VAL   A 1 12  ? 6.868   4.552   21.682  1.00 51.53  ? 29  VAL   A C   1 
ATOM   92   O O   . VAL   A 1 12  ? 7.242   4.802   22.835  1.00 52.47  ? 29  VAL   A O   1 
ATOM   93   C CB  . VAL   A 1 12  ? 9.019   3.554   20.824  1.00 50.19  ? 29  VAL   A CB  1 
ATOM   94   C CG1 . VAL   A 1 12  ? 8.481   2.217   21.319  1.00 47.72  ? 29  VAL   A CG1 1 
ATOM   95   C CG2 . VAL   A 1 12  ? 9.869   3.365   19.580  1.00 47.80  ? 29  VAL   A CG2 1 
ATOM   96   N N   . VAL   A 1 13  ? 5.599   4.310   21.368  1.00 51.29  ? 30  VAL   A N   1 
ATOM   97   C CA  . VAL   A 1 13  ? 4.516   4.427   22.332  1.00 53.85  ? 30  VAL   A CA  1 
ATOM   98   C C   . VAL   A 1 13  ? 3.745   3.117   22.376  1.00 54.30  ? 30  VAL   A C   1 
ATOM   99   O O   . VAL   A 1 13  ? 3.749   2.334   21.420  1.00 48.77  ? 30  VAL   A O   1 
ATOM   100  C CB  . VAL   A 1 13  ? 3.577   5.607   21.996  1.00 46.89  ? 30  VAL   A CB  1 
ATOM   101  C CG1 . VAL   A 1 13  ? 4.385   6.861   21.713  1.00 56.54  ? 30  VAL   A CG1 1 
ATOM   102  C CG2 . VAL   A 1 13  ? 2.719   5.267   20.801  1.00 52.72  ? 30  VAL   A CG2 1 
ATOM   103  N N   . GLU   A 1 14  ? 3.094   2.875   23.507  1.00 56.12  ? 31  GLU   A N   1 
ATOM   104  C CA  . GLU   A 1 14  ? 2.308   1.670   23.709  1.00 56.51  ? 31  GLU   A CA  1 
ATOM   105  C C   . GLU   A 1 14  ? 0.856   1.909   23.317  1.00 55.39  ? 31  GLU   A C   1 
ATOM   106  O O   . GLU   A 1 14  ? 0.366   3.042   23.328  1.00 55.57  ? 31  GLU   A O   1 
ATOM   107  C CB  . GLU   A 1 14  ? 2.391   1.208   25.165  1.00 62.13  ? 31  GLU   A CB  1 
ATOM   108  C CG  . GLU   A 1 14  ? 3.814   1.052   25.680  1.00 64.58  ? 31  GLU   A CG  1 
ATOM   109  C CD  . GLU   A 1 14  ? 4.511   -0.170  25.111  1.00 65.84  ? 31  GLU   A CD  1 
ATOM   110  O OE1 . GLU   A 1 14  ? 4.210   -1.294  25.566  1.00 66.69  ? 31  GLU   A OE1 1 
ATOM   111  O OE2 . GLU   A 1 14  ? 5.360   -0.007  24.209  1.00 63.55  ? 31  GLU   A OE2 1 
ATOM   112  N N   . TYR   A 1 15  ? 0.177   0.823   22.951  1.00 53.38  ? 32  TYR   A N   1 
ATOM   113  C CA  . TYR   A 1 15  ? -1.224  0.901   22.564  1.00 51.59  ? 32  TYR   A CA  1 
ATOM   114  C C   . TYR   A 1 15  ? -2.062  1.482   23.696  1.00 49.24  ? 32  TYR   A C   1 
ATOM   115  O O   . TYR   A 1 15  ? -1.898  1.121   24.865  1.00 45.14  ? 32  TYR   A O   1 
ATOM   116  C CB  . TYR   A 1 15  ? -1.736  -0.490  22.184  1.00 51.08  ? 32  TYR   A CB  1 
ATOM   117  C CG  . TYR   A 1 15  ? -3.179  -0.535  21.730  1.00 53.92  ? 32  TYR   A CG  1 
ATOM   118  C CD1 . TYR   A 1 15  ? -3.539  -0.131  20.451  1.00 53.20  ? 32  TYR   A CD1 1 
ATOM   119  C CD2 . TYR   A 1 15  ? -4.179  -0.998  22.577  1.00 49.26  ? 32  TYR   A CD2 1 
ATOM   120  C CE1 . TYR   A 1 15  ? -4.856  -0.178  20.031  1.00 53.10  ? 32  TYR   A CE1 1 
ATOM   121  C CE2 . TYR   A 1 15  ? -5.498  -1.047  22.167  1.00 46.76  ? 32  TYR   A CE2 1 
ATOM   122  C CZ  . TYR   A 1 15  ? -5.831  -0.637  20.893  1.00 51.17  ? 32  TYR   A CZ  1 
ATOM   123  O OH  . TYR   A 1 15  ? -7.143  -0.686  20.481  1.00 54.35  ? 32  TYR   A OH  1 
ATOM   124  N N   . GLY   A 1 16  ? -2.964  2.397   23.340  1.00 53.02  ? 33  GLY   A N   1 
ATOM   125  C CA  . GLY   A 1 16  ? -3.847  3.021   24.299  1.00 53.58  ? 33  GLY   A CA  1 
ATOM   126  C C   . GLY   A 1 16  ? -3.244  4.151   25.103  1.00 54.70  ? 33  GLY   A C   1 
ATOM   127  O O   . GLY   A 1 16  ? -3.985  4.844   25.813  1.00 61.64  ? 33  GLY   A O   1 
ATOM   128  N N   . SER   A 1 17  ? -1.933  4.364   25.028  1.00 53.95  ? 34  SER   A N   1 
ATOM   129  C CA  . SER   A 1 17  ? -1.305  5.428   25.794  1.00 59.05  ? 34  SER   A CA  1 
ATOM   130  C C   . SER   A 1 17  ? -1.482  6.772   25.086  1.00 55.51  ? 34  SER   A C   1 
ATOM   131  O O   . SER   A 1 17  ? -2.032  6.863   23.984  1.00 53.01  ? 34  SER   A O   1 
ATOM   132  C CB  . SER   A 1 17  ? 0.173   5.114   26.020  1.00 49.99  ? 34  SER   A CB  1 
ATOM   133  O OG  . SER   A 1 17  ? 0.901   5.183   24.806  1.00 56.13  ? 34  SER   A OG  1 
ATOM   134  N N   . ASN   A 1 18  ? -1.007  7.832   25.734  1.00 53.19  ? 35  ASN   A N   1 
ATOM   135  C CA  . ASN   A 1 18  ? -1.022  9.178   25.181  1.00 56.52  ? 35  ASN   A CA  1 
ATOM   136  C C   . ASN   A 1 18  ? 0.395   9.601   24.821  1.00 47.35  ? 35  ASN   A C   1 
ATOM   137  O O   . ASN   A 1 18  ? 1.335   9.368   25.589  1.00 44.35  ? 35  ASN   A O   1 
ATOM   138  C CB  . ASN   A 1 18  ? -1.632  10.176  26.170  1.00 52.17  ? 35  ASN   A CB  1 
ATOM   139  C CG  . ASN   A 1 18  ? -2.952  9.697   26.743  1.00 57.35  ? 35  ASN   A CG  1 
ATOM   140  O OD1 . ASN   A 1 18  ? -3.793  9.156   26.026  1.00 53.84  ? 35  ASN   A OD1 1 
ATOM   141  N ND2 . ASN   A 1 18  ? -3.140  9.896   28.042  1.00 56.56  ? 35  ASN   A ND2 1 
ATOM   142  N N   . MET   A 1 19  ? 0.549   10.221  23.655  1.00 45.86  ? 36  MET   A N   1 
ATOM   143  C CA  . MET   A 1 19  ? 1.851   10.682  23.196  1.00 49.53  ? 36  MET   A CA  1 
ATOM   144  C C   . MET   A 1 19  ? 1.771   12.147  22.792  1.00 48.65  ? 36  MET   A C   1 
ATOM   145  O O   . MET   A 1 19  ? 0.788   12.587  22.186  1.00 48.98  ? 36  MET   A O   1 
ATOM   146  C CB  . MET   A 1 19  ? 2.373   9.828   22.026  1.00 45.09  ? 36  MET   A CB  1 
ATOM   147  C CG  . MET   A 1 19  ? 1.696   10.068  20.686  1.00 51.16  ? 36  MET   A CG  1 
ATOM   148  S SD  . MET   A 1 19  ? 2.636   9.367   19.315  1.00 47.65  ? 36  MET   A SD  1 
ATOM   149  C CE  . MET   A 1 19  ? 1.406   9.388   18.013  1.00 51.79  ? 36  MET   A CE  1 
ATOM   150  N N   . THR   A 1 20  ? 2.805   12.901  23.156  1.00 46.89  ? 37  THR   A N   1 
ATOM   151  C CA  . THR   A 1 20  ? 2.954   14.298  22.769  1.00 53.57  ? 37  THR   A CA  1 
ATOM   152  C C   . THR   A 1 20  ? 4.233   14.417  21.956  1.00 46.39  ? 37  THR   A C   1 
ATOM   153  O O   . THR   A 1 20  ? 5.325   14.150  22.468  1.00 49.72  ? 37  THR   A O   1 
ATOM   154  C CB  . THR   A 1 20  ? 3.008   15.218  23.990  1.00 46.59  ? 37  THR   A CB  1 
ATOM   155  O OG1 . THR   A 1 20  ? 1.862   14.987  24.818  1.00 52.48  ? 37  THR   A OG1 1 
ATOM   156  C CG2 . THR   A 1 20  ? 3.035   16.676  23.556  1.00 50.02  ? 37  THR   A CG2 1 
ATOM   157  N N   . ILE   A 1 21  ? 4.095   14.804  20.697  1.00 44.32  ? 38  ILE   A N   1 
ATOM   158  C CA  . ILE   A 1 21  ? 5.221   14.927  19.781  1.00 46.01  ? 38  ILE   A CA  1 
ATOM   159  C C   . ILE   A 1 21  ? 5.560   16.400  19.586  1.00 51.23  ? 38  ILE   A C   1 
ATOM   160  O O   . ILE   A 1 21  ? 4.670   17.260  19.528  1.00 52.31  ? 38  ILE   A O   1 
ATOM   161  C CB  . ILE   A 1 21  ? 4.905   14.182  18.466  1.00 49.60  ? 38  ILE   A CB  1 
ATOM   162  C CG1 . ILE   A 1 21  ? 3.991   14.975  17.539  1.00 44.33  ? 38  ILE   A CG1 1 
ATOM   163  C CG2 . ILE   A 1 21  ? 4.246   12.846  18.768  1.00 51.07  ? 38  ILE   A CG2 1 
ATOM   164  C CD1 . ILE   A 1 21  ? 3.920   14.372  16.148  1.00 51.26  ? 38  ILE   A CD1 1 
ATOM   165  N N   . GLU   A 1 22  ? 6.859   16.696  19.529  1.00 48.03  ? 39  GLU   A N   1 
ATOM   166  C CA  . GLU   A 1 22  ? 7.379   18.055  19.620  1.00 48.57  ? 39  GLU   A CA  1 
ATOM   167  C C   . GLU   A 1 22  ? 8.221   18.397  18.400  1.00 53.41  ? 39  GLU   A C   1 
ATOM   168  O O   . GLU   A 1 22  ? 9.149   17.658  18.058  1.00 56.67  ? 39  GLU   A O   1 
ATOM   169  C CB  . GLU   A 1 22  ? 8.243   18.215  20.876  1.00 47.50  ? 39  GLU   A CB  1 
ATOM   170  C CG  . GLU   A 1 22  ? 7.486   18.467  22.163  1.00 52.32  ? 39  GLU   A CG  1 
ATOM   171  C CD  . GLU   A 1 22  ? 8.419   18.793  23.313  1.00 58.01  ? 39  GLU   A CD  1 
ATOM   172  O OE1 . GLU   A 1 22  ? 9.638   18.553  23.173  1.00 50.12  ? 39  GLU   A OE1 1 
ATOM   173  O OE2 . GLU   A 1 22  ? 7.939   19.288  24.354  1.00 62.07  ? 39  GLU   A OE2 1 
ATOM   174  N N   . CYS   A 1 23  ? 7.885   19.501  17.734  1.00 49.37  ? 40  CYS   A N   1 
ATOM   175  C CA  . CYS   A 1 23  ? 8.827   20.193  16.867  1.00 55.17  ? 40  CYS   A CA  1 
ATOM   176  C C   . CYS   A 1 23  ? 8.853   21.666  17.252  1.00 53.24  ? 40  CYS   A C   1 
ATOM   177  O O   . CYS   A 1 23  ? 7.843   22.229  17.684  1.00 53.25  ? 40  CYS   A O   1 
ATOM   178  C CB  . CYS   A 1 23  ? 8.514   20.016  15.373  1.00 52.98  ? 40  CYS   A CB  1 
ATOM   179  S SG  . CYS   A 1 23  ? 6.931   20.576  14.771  1.00 58.27  ? 40  CYS   A SG  1 
ATOM   180  N N   . LYS   A 1 24  ? 10.019  22.285  17.089  1.00 56.43  ? 41  LYS   A N   1 
ATOM   181  C CA  . LYS   A 1 24  ? 10.297  23.607  17.633  1.00 50.19  ? 41  LYS   A CA  1 
ATOM   182  C C   . LYS   A 1 24  ? 10.673  24.575  16.520  1.00 46.45  ? 41  LYS   A C   1 
ATOM   183  O O   . LYS   A 1 24  ? 11.335  24.196  15.550  1.00 47.47  ? 41  LYS   A O   1 
ATOM   184  C CB  . LYS   A 1 24  ? 11.428  23.546  18.665  1.00 48.53  ? 41  LYS   A CB  1 
ATOM   185  C CG  . LYS   A 1 24  ? 10.957  23.504  20.108  1.00 50.00  ? 41  LYS   A CG  1 
ATOM   186  C CD  . LYS   A 1 24  ? 11.404  22.221  20.786  1.00 54.93  ? 41  LYS   A CD  1 
ATOM   187  C CE  . LYS   A 1 24  ? 10.751  22.056  22.146  1.00 55.12  ? 41  LYS   A CE  1 
ATOM   188  N NZ  . LYS   A 1 24  ? 11.388  20.969  22.940  1.00 65.81  ? 41  LYS   A NZ  1 
ATOM   189  N N   . PHE   A 1 25  ? 10.236  25.822  16.666  1.00 48.15  ? 42  PHE   A N   1 
ATOM   190  C CA  . PHE   A 1 25  ? 10.524  26.890  15.723  1.00 53.53  ? 42  PHE   A CA  1 
ATOM   191  C C   . PHE   A 1 25  ? 11.049  28.105  16.467  1.00 55.75  ? 42  PHE   A C   1 
ATOM   192  O O   . PHE   A 1 25  ? 10.700  28.328  17.633  1.00 56.39  ? 42  PHE   A O   1 
ATOM   193  C CB  . PHE   A 1 25  ? 9.278   27.277  14.908  1.00 54.47  ? 42  PHE   A CB  1 
ATOM   194  C CG  . PHE   A 1 25  ? 8.088   27.660  15.745  1.00 50.31  ? 42  PHE   A CG  1 
ATOM   195  C CD1 . PHE   A 1 25  ? 7.252   26.690  16.274  1.00 51.79  ? 42  PHE   A CD1 1 
ATOM   196  C CD2 . PHE   A 1 25  ? 7.800   28.992  15.992  1.00 51.89  ? 42  PHE   A CD2 1 
ATOM   197  C CE1 . PHE   A 1 25  ? 6.156   27.041  17.039  1.00 57.46  ? 42  PHE   A CE1 1 
ATOM   198  C CE2 . PHE   A 1 25  ? 6.706   29.350  16.757  1.00 53.10  ? 42  PHE   A CE2 1 
ATOM   199  C CZ  . PHE   A 1 25  ? 5.882   28.373  17.280  1.00 59.63  ? 42  PHE   A CZ  1 
ATOM   200  N N   . PRO   A 1 26  ? 11.896  28.914  15.825  1.00 53.21  ? 43  PRO   A N   1 
ATOM   201  C CA  . PRO   A 1 26  ? 12.509  30.056  16.518  1.00 61.74  ? 43  PRO   A CA  1 
ATOM   202  C C   . PRO   A 1 26  ? 11.513  31.196  16.699  1.00 64.74  ? 43  PRO   A C   1 
ATOM   203  O O   . PRO   A 1 26  ? 10.858  31.629  15.748  1.00 63.45  ? 43  PRO   A O   1 
ATOM   204  C CB  . PRO   A 1 26  ? 13.661  30.464  15.591  1.00 53.68  ? 43  PRO   A CB  1 
ATOM   205  C CG  . PRO   A 1 26  ? 13.262  29.957  14.249  1.00 60.07  ? 43  PRO   A CG  1 
ATOM   206  C CD  . PRO   A 1 26  ? 12.489  28.694  14.493  1.00 54.59  ? 43  PRO   A CD  1 
ATOM   207  N N   . VAL   A 1 27  ? 11.409  31.676  17.935  1.00 71.10  ? 44  VAL   A N   1 
ATOM   208  C CA  . VAL   A 1 27  ? 10.566  32.810  18.299  1.00 69.74  ? 44  VAL   A CA  1 
ATOM   209  C C   . VAL   A 1 27  ? 11.468  33.949  18.761  1.00 75.53  ? 44  VAL   A C   1 
ATOM   210  O O   . VAL   A 1 27  ? 12.436  33.726  19.500  1.00 79.42  ? 44  VAL   A O   1 
ATOM   211  C CB  . VAL   A 1 27  ? 9.526   32.427  19.369  1.00 69.81  ? 44  VAL   A CB  1 
ATOM   212  C CG1 . VAL   A 1 27  ? 10.186  32.123  20.708  1.00 65.77  ? 44  VAL   A CG1 1 
ATOM   213  C CG2 . VAL   A 1 27  ? 8.496   33.534  19.525  1.00 82.74  ? 44  VAL   A CG2 1 
ATOM   214  N N   . GLU   A 1 28  ? 11.180  35.161  18.283  1.00 89.91  ? 45  GLU   A N   1 
ATOM   215  C CA  . GLU   A 1 28  ? 12.073  36.296  18.523  1.00 100.58 ? 45  GLU   A CA  1 
ATOM   216  C C   . GLU   A 1 28  ? 11.798  36.945  19.879  1.00 101.86 ? 45  GLU   A C   1 
ATOM   217  O O   . GLU   A 1 28  ? 12.639  36.899  20.781  1.00 103.67 ? 45  GLU   A O   1 
ATOM   218  C CB  . GLU   A 1 28  ? 11.937  37.321  17.407  1.00 98.66  ? 45  GLU   A CB  1 
ATOM   219  N N   . LYS   A 1 29  ? 10.628  37.562  20.038  1.00 101.93 ? 46  LYS   A N   1 
ATOM   220  C CA  . LYS   A 1 29  ? 10.274  38.147  21.326  1.00 100.18 ? 46  LYS   A CA  1 
ATOM   221  C C   . LYS   A 1 29  ? 8.924   37.616  21.804  1.00 105.33 ? 46  LYS   A C   1 
ATOM   222  O O   . LYS   A 1 29  ? 8.869   36.822  22.749  1.00 102.00 ? 46  LYS   A O   1 
ATOM   223  C CB  . LYS   A 1 29  ? 10.251  39.665  21.235  1.00 91.29  ? 46  LYS   A CB  1 
ATOM   224  N N   . GLN   A 1 30  ? 7.835   38.033  21.165  1.00 118.72 ? 47  GLN   A N   1 
ATOM   225  C CA  . GLN   A 1 30  ? 6.512   37.488  21.405  1.00 113.24 ? 47  GLN   A CA  1 
ATOM   226  C C   . GLN   A 1 30  ? 6.077   36.703  20.171  1.00 110.77 ? 47  GLN   A C   1 
ATOM   227  O O   . GLN   A 1 30  ? 6.887   36.390  19.291  1.00 115.85 ? 47  GLN   A O   1 
ATOM   228  C CB  . GLN   A 1 30  ? 5.531   38.610  21.754  1.00 106.49 ? 47  GLN   A CB  1 
ATOM   229  N N   . LEU   A 1 31  ? 4.790   36.383  20.100  1.00 81.27  ? 48  LEU   A N   1 
ATOM   230  C CA  . LEU   A 1 31  ? 4.234   35.644  18.974  1.00 80.09  ? 48  LEU   A CA  1 
ATOM   231  C C   . LEU   A 1 31  ? 3.328   36.571  18.175  1.00 78.34  ? 48  LEU   A C   1 
ATOM   232  O O   . LEU   A 1 31  ? 2.338   37.087  18.706  1.00 82.53  ? 48  LEU   A O   1 
ATOM   233  C CB  . LEU   A 1 31  ? 3.474   34.408  19.455  1.00 82.41  ? 48  LEU   A CB  1 
ATOM   234  C CG  . LEU   A 1 31  ? 3.646   33.158  18.590  1.00 73.36  ? 48  LEU   A CG  1 
ATOM   235  C CD1 . LEU   A 1 31  ? 5.078   32.664  18.658  1.00 72.30  ? 48  LEU   A CD1 1 
ATOM   236  C CD2 . LEU   A 1 31  ? 2.691   32.066  19.037  1.00 71.04  ? 48  LEU   A CD2 1 
ATOM   237  N N   . ASP   A 1 32  ? 3.669   36.779  16.903  1.00 73.98  ? 49  ASP   A N   1 
ATOM   238  C CA  . ASP   A 1 32  ? 2.738   37.344  15.926  1.00 72.65  ? 49  ASP   A CA  1 
ATOM   239  C C   . ASP   A 1 32  ? 1.822   36.226  15.438  1.00 67.09  ? 49  ASP   A C   1 
ATOM   240  O O   . ASP   A 1 32  ? 2.009   35.637  14.369  1.00 62.75  ? 49  ASP   A O   1 
ATOM   241  C CB  . ASP   A 1 32  ? 3.490   38.010  14.780  1.00 71.93  ? 49  ASP   A CB  1 
ATOM   242  C CG  . ASP   A 1 32  ? 2.681   39.106  14.112  1.00 75.57  ? 49  ASP   A CG  1 
ATOM   243  O OD1 . ASP   A 1 32  ? 1.824   39.712  14.791  1.00 69.43  ? 49  ASP   A OD1 1 
ATOM   244  O OD2 . ASP   A 1 32  ? 2.902   39.365  12.910  1.00 72.50  ? 49  ASP   A OD2 1 
ATOM   245  N N   . LEU   A 1 33  ? 0.810   35.927  16.258  1.00 70.76  ? 50  LEU   A N   1 
ATOM   246  C CA  . LEU   A 1 33  ? -0.135  34.858  15.952  1.00 68.80  ? 50  LEU   A CA  1 
ATOM   247  C C   . LEU   A 1 33  ? -0.869  35.076  14.635  1.00 68.43  ? 50  LEU   A C   1 
ATOM   248  O O   . LEU   A 1 33  ? -1.382  34.111  14.059  1.00 67.87  ? 50  LEU   A O   1 
ATOM   249  C CB  . LEU   A 1 33  ? -1.149  34.713  17.088  1.00 73.82  ? 50  LEU   A CB  1 
ATOM   250  C CG  . LEU   A 1 33  ? -0.633  34.114  18.398  1.00 76.02  ? 50  LEU   A CG  1 
ATOM   251  C CD1 . LEU   A 1 33  ? -1.312  34.769  19.590  1.00 73.19  ? 50  LEU   A CD1 1 
ATOM   252  C CD2 . LEU   A 1 33  ? -0.853  32.610  18.415  1.00 68.26  ? 50  LEU   A CD2 1 
ATOM   253  N N   . ALA   A 1 34  ? -0.924  36.313  14.137  1.00 69.20  ? 51  ALA   A N   1 
ATOM   254  C CA  . ALA   A 1 34  ? -1.515  36.560  12.828  1.00 66.85  ? 51  ALA   A CA  1 
ATOM   255  C C   . ALA   A 1 34  ? -0.632  36.083  11.683  1.00 62.10  ? 51  ALA   A C   1 
ATOM   256  O O   . ALA   A 1 34  ? -1.075  36.110  10.530  1.00 58.78  ? 51  ALA   A O   1 
ATOM   257  C CB  . ALA   A 1 34  ? -1.818  38.049  12.661  1.00 60.58  ? 51  ALA   A CB  1 
ATOM   258  N N   . ALA   A 1 35  ? 0.595   35.648  11.969  1.00 59.78  ? 52  ALA   A N   1 
ATOM   259  C CA  . ALA   A 1 35  ? 1.493   35.122  10.955  1.00 59.37  ? 52  ALA   A CA  1 
ATOM   260  C C   . ALA   A 1 35  ? 1.907   33.679  11.202  1.00 57.38  ? 52  ALA   A C   1 
ATOM   261  O O   . ALA   A 1 35  ? 2.559   33.087  10.334  1.00 56.83  ? 52  ALA   A O   1 
ATOM   262  C CB  . ALA   A 1 35  ? 2.756   35.992  10.851  1.00 55.50  ? 52  ALA   A CB  1 
ATOM   263  N N   . LEU   A 1 36  ? 1.548   33.098  12.344  1.00 51.18  ? 53  LEU   A N   1 
ATOM   264  C CA  . LEU   A 1 36  ? 1.893   31.715  12.638  1.00 57.45  ? 53  LEU   A CA  1 
ATOM   265  C C   . LEU   A 1 36  ? 0.990   30.762  11.867  1.00 55.22  ? 53  LEU   A C   1 
ATOM   266  O O   . LEU   A 1 36  ? -0.239  30.872  11.922  1.00 58.22  ? 53  LEU   A O   1 
ATOM   267  C CB  . LEU   A 1 36  ? 1.788   31.451  14.140  1.00 59.93  ? 53  LEU   A CB  1 
ATOM   268  C CG  . LEU   A 1 36  ? 2.228   30.067  14.615  1.00 48.02  ? 53  LEU   A CG  1 
ATOM   269  C CD1 . LEU   A 1 36  ? 3.680   30.109  15.049  1.00 58.36  ? 53  LEU   A CD1 1 
ATOM   270  C CD2 . LEU   A 1 36  ? 1.350   29.589  15.756  1.00 57.09  ? 53  LEU   A CD2 1 
ATOM   271  N N   . ILE   A 1 37  ? 1.604   29.826  11.147  1.00 49.76  ? 54  ILE   A N   1 
ATOM   272  C CA  . ILE   A 1 37  ? 0.891   28.783  10.421  1.00 55.86  ? 54  ILE   A CA  1 
ATOM   273  C C   . ILE   A 1 37  ? 1.505   27.446  10.807  1.00 53.49  ? 54  ILE   A C   1 
ATOM   274  O O   . ILE   A 1 37  ? 2.689   27.206  10.545  1.00 50.98  ? 54  ILE   A O   1 
ATOM   275  C CB  . ILE   A 1 37  ? 0.959   28.989  8.899   1.00 55.33  ? 54  ILE   A CB  1 
ATOM   276  C CG1 . ILE   A 1 37  ? -0.002  30.097  8.468   1.00 55.42  ? 54  ILE   A CG1 1 
ATOM   277  C CG2 . ILE   A 1 37  ? 0.639   27.690  8.168   1.00 52.38  ? 54  ILE   A CG2 1 
ATOM   278  C CD1 . ILE   A 1 37  ? -0.292  30.111  6.985   1.00 60.06  ? 54  ILE   A CD1 1 
ATOM   279  N N   . VAL   A 1 38  ? 0.713   26.587  11.443  1.00 54.33  ? 55  VAL   A N   1 
ATOM   280  C CA  . VAL   A 1 38  ? 1.155   25.260  11.855  1.00 59.01  ? 55  VAL   A CA  1 
ATOM   281  C C   . VAL   A 1 38  ? 0.255   24.234  11.183  1.00 58.84  ? 55  VAL   A C   1 
ATOM   282  O O   . VAL   A 1 38  ? -0.969  24.266  11.360  1.00 60.96  ? 55  VAL   A O   1 
ATOM   283  C CB  . VAL   A 1 38  ? 1.128   25.096  13.383  1.00 59.62  ? 55  VAL   A CB  1 
ATOM   284  C CG1 . VAL   A 1 38  ? 1.477   23.667  13.770  1.00 50.85  ? 55  VAL   A CG1 1 
ATOM   285  C CG2 . VAL   A 1 38  ? 2.081   26.084  14.041  1.00 56.10  ? 55  VAL   A CG2 1 
ATOM   286  N N   . TYR   A 1 39  ? 0.857   23.328  10.414  1.00 61.01  ? 56  TYR   A N   1 
ATOM   287  C CA  . TYR   A 1 39  ? 0.137   22.227  9.785   1.00 63.33  ? 56  TYR   A CA  1 
ATOM   288  C C   . TYR   A 1 39  ? 0.719   20.914  10.285  1.00 59.53  ? 56  TYR   A C   1 
ATOM   289  O O   . TYR   A 1 39  ? 1.900   20.629  10.061  1.00 59.98  ? 56  TYR   A O   1 
ATOM   290  C CB  . TYR   A 1 39  ? 0.215   22.303  8.260   1.00 62.99  ? 56  TYR   A CB  1 
ATOM   291  C CG  . TYR   A 1 39  ? -0.664  21.288  7.565   1.00 63.91  ? 56  TYR   A CG  1 
ATOM   292  C CD1 . TYR   A 1 39  ? -2.047  21.358  7.664   1.00 65.36  ? 56  TYR   A CD1 1 
ATOM   293  C CD2 . TYR   A 1 39  ? -0.113  20.256  6.818   1.00 64.37  ? 56  TYR   A CD2 1 
ATOM   294  C CE1 . TYR   A 1 39  ? -2.858  20.432  7.034   1.00 67.03  ? 56  TYR   A CE1 1 
ATOM   295  C CE2 . TYR   A 1 39  ? -0.916  19.324  6.184   1.00 64.87  ? 56  TYR   A CE2 1 
ATOM   296  C CZ  . TYR   A 1 39  ? -2.287  19.417  6.296   1.00 66.50  ? 56  TYR   A CZ  1 
ATOM   297  O OH  . TYR   A 1 39  ? -3.089  18.493  5.667   1.00 65.83  ? 56  TYR   A OH  1 
ATOM   298  N N   . TRP   A 1 40  ? -0.108  20.122  10.959  1.00 56.26  ? 57  TRP   A N   1 
ATOM   299  C CA  . TRP   A 1 40  ? 0.258   18.788  11.416  1.00 53.65  ? 57  TRP   A CA  1 
ATOM   300  C C   . TRP   A 1 40  ? -0.465  17.747  10.572  1.00 55.58  ? 57  TRP   A C   1 
ATOM   301  O O   . TRP   A 1 40  ? -1.699  17.762  10.491  1.00 58.08  ? 57  TRP   A O   1 
ATOM   302  C CB  . TRP   A 1 40  ? -0.104  18.602  12.888  1.00 52.89  ? 57  TRP   A CB  1 
ATOM   303  C CG  . TRP   A 1 40  ? 0.963   18.977  13.869  1.00 47.53  ? 57  TRP   A CG  1 
ATOM   304  C CD1 . TRP   A 1 40  ? 0.933   20.016  14.753  1.00 51.30  ? 57  TRP   A CD1 1 
ATOM   305  C CD2 . TRP   A 1 40  ? 2.213   18.310  14.075  1.00 48.01  ? 57  TRP   A CD2 1 
ATOM   306  N NE1 . TRP   A 1 40  ? 2.086   20.036  15.499  1.00 57.80  ? 57  TRP   A NE1 1 
ATOM   307  C CE2 . TRP   A 1 40  ? 2.890   19.000  15.101  1.00 51.74  ? 57  TRP   A CE2 1 
ATOM   308  C CE3 . TRP   A 1 40  ? 2.827   17.199  13.491  1.00 52.02  ? 57  TRP   A CE3 1 
ATOM   309  C CZ2 . TRP   A 1 40  ? 4.150   18.615  15.556  1.00 48.17  ? 57  TRP   A CZ2 1 
ATOM   310  C CZ3 . TRP   A 1 40  ? 4.078   16.819  13.939  1.00 45.53  ? 57  TRP   A CZ3 1 
ATOM   311  C CH2 . TRP   A 1 40  ? 4.724   17.522  14.968  1.00 46.06  ? 57  TRP   A CH2 1 
ATOM   312  N N   . GLU   A 1 41  ? 0.292   16.845  9.950   1.00 50.20  ? 58  GLU   A N   1 
ATOM   313  C CA  . GLU   A 1 41  ? -0.302  15.785  9.149   1.00 52.20  ? 58  GLU   A CA  1 
ATOM   314  C C   . GLU   A 1 41  ? 0.464   14.487  9.359   1.00 50.74  ? 58  GLU   A C   1 
ATOM   315  O O   . GLU   A 1 41  ? 1.620   14.483  9.791   1.00 47.35  ? 58  GLU   A O   1 
ATOM   316  C CB  . GLU   A 1 41  ? -0.333  16.137  7.655   1.00 55.13  ? 58  GLU   A CB  1 
ATOM   317  C CG  . GLU   A 1 41  ? 0.971   15.882  6.922   1.00 47.37  ? 58  GLU   A CG  1 
ATOM   318  C CD  . GLU   A 1 41  ? 0.858   16.151  5.435   1.00 52.34  ? 58  GLU   A CD  1 
ATOM   319  O OE1 . GLU   A 1 41  ? -0.268  16.416  4.964   1.00 51.25  ? 58  GLU   A OE1 1 
ATOM   320  O OE2 . GLU   A 1 41  ? 1.890   16.085  4.734   1.00 53.30  ? 58  GLU   A OE2 1 
ATOM   321  N N   . MET   A 1 42  ? -0.203  13.377  9.046   1.00 55.14  ? 59  MET   A N   1 
ATOM   322  C CA  . MET   A 1 42  ? 0.434   12.067  8.969   1.00 54.69  ? 59  MET   A CA  1 
ATOM   323  C C   . MET   A 1 42  ? -0.204  11.304  7.816   1.00 53.93  ? 59  MET   A C   1 
ATOM   324  O O   . MET   A 1 42  ? -1.430  11.159  7.767   1.00 54.56  ? 59  MET   A O   1 
ATOM   325  C CB  . MET   A 1 42  ? 0.337   11.303  10.303  1.00 51.45  ? 59  MET   A CB  1 
ATOM   326  C CG  . MET   A 1 42  ? -0.901  10.449  10.539  1.00 53.45  ? 59  MET   A CG  1 
ATOM   327  S SD  . MET   A 1 42  ? -0.719  8.746   9.965   1.00 64.53  ? 59  MET   A SD  1 
ATOM   328  C CE  . MET   A 1 42  ? -0.021  7.963   11.415  1.00 51.45  ? 59  MET   A CE  1 
ATOM   329  N N   . GLU   A 1 43  ? 0.623   10.876  6.862   1.00 58.49  ? 60  GLU   A N   1 
ATOM   330  C CA  . GLU   A 1 43  ? 0.189   10.103  5.697   1.00 60.91  ? 60  GLU   A CA  1 
ATOM   331  C C   . GLU   A 1 43  ? -1.004  10.773  5.008   1.00 63.16  ? 60  GLU   A C   1 
ATOM   332  O O   . GLU   A 1 43  ? -2.125  10.265  4.984   1.00 70.73  ? 60  GLU   A O   1 
ATOM   333  C CB  . GLU   A 1 43  ? -0.133  8.660   6.102   1.00 57.62  ? 60  GLU   A CB  1 
ATOM   334  C CG  . GLU   A 1 43  ? 0.929   8.025   6.988   1.00 61.48  ? 60  GLU   A CG  1 
ATOM   335  C CD  . GLU   A 1 43  ? 1.397   6.677   6.475   1.00 62.24  ? 60  GLU   A CD  1 
ATOM   336  O OE1 . GLU   A 1 43  ? 0.547   5.892   6.004   1.00 65.19  ? 60  GLU   A OE1 1 
ATOM   337  O OE2 . GLU   A 1 43  ? 2.615   6.405   6.542   1.00 55.58  ? 60  GLU   A OE2 1 
ATOM   338  N N   . ASP   A 1 44  ? -0.709  11.952  4.447   1.00 62.92  ? 61  ASP   A N   1 
ATOM   339  C CA  . ASP   A 1 44  ? -1.639  12.824  3.724   1.00 65.12  ? 61  ASP   A CA  1 
ATOM   340  C C   . ASP   A 1 44  ? -2.990  12.946  4.423   1.00 64.64  ? 61  ASP   A C   1 
ATOM   341  O O   . ASP   A 1 44  ? -4.019  13.128  3.765   1.00 67.35  ? 61  ASP   A O   1 
ATOM   342  C CB  . ASP   A 1 44  ? -1.851  12.413  2.250   1.00 67.17  ? 61  ASP   A CB  1 
ATOM   343  C CG  . ASP   A 1 44  ? -1.955  10.910  2.027   1.00 75.54  ? 61  ASP   A CG  1 
ATOM   344  O OD1 . ASP   A 1 44  ? -1.008  10.164  2.350   1.00 73.07  ? 61  ASP   A OD1 1 
ATOM   345  O OD2 . ASP   A 1 44  ? -3.013  10.472  1.525   1.00 81.02  ? 61  ASP   A OD2 1 
ATOM   346  N N   . LYS   A 1 45  ? -2.999  12.860  5.752   1.00 61.39  ? 62  LYS   A N   1 
ATOM   347  C CA  . LYS   A 1 45  ? -4.211  13.008  6.552   1.00 56.92  ? 62  LYS   A CA  1 
ATOM   348  C C   . LYS   A 1 45  ? -3.976  14.127  7.556   1.00 58.70  ? 62  LYS   A C   1 
ATOM   349  O O   . LYS   A 1 45  ? -3.137  13.994  8.454   1.00 56.64  ? 62  LYS   A O   1 
ATOM   350  C CB  . LYS   A 1 45  ? -4.571  11.702  7.261   1.00 61.93  ? 62  LYS   A CB  1 
ATOM   351  C CG  . LYS   A 1 45  ? -5.390  10.736  6.419   1.00 59.20  ? 62  LYS   A CG  1 
ATOM   352  C CD  . LYS   A 1 45  ? -6.097  9.695   7.280   1.00 63.61  ? 62  LYS   A CD  1 
ATOM   353  C CE  . LYS   A 1 45  ? -5.263  9.290   8.486   1.00 57.49  ? 62  LYS   A CE  1 
ATOM   354  N NZ  . LYS   A 1 45  ? -4.337  8.171   8.164   1.00 59.64  ? 62  LYS   A NZ  1 
ATOM   355  N N   . ASN   A 1 46  ? -4.710  15.226  7.403   1.00 57.14  ? 63  ASN   A N   1 
ATOM   356  C CA  . ASN   A 1 46  ? -4.551  16.354  8.308   1.00 57.44  ? 63  ASN   A CA  1 
ATOM   357  C C   . ASN   A 1 46  ? -4.944  15.954  9.722   1.00 55.06  ? 63  ASN   A C   1 
ATOM   358  O O   . ASN   A 1 46  ? -5.910  15.217  9.937   1.00 56.98  ? 63  ASN   A O   1 
ATOM   359  C CB  . ASN   A 1 46  ? -5.402  17.541  7.855   1.00 67.15  ? 63  ASN   A CB  1 
ATOM   360  C CG  . ASN   A 1 46  ? -5.298  18.743  8.797   1.00 64.56  ? 63  ASN   A CG  1 
ATOM   361  O OD1 . ASN   A 1 46  ? -4.615  18.706  9.823   1.00 63.94  ? 63  ASN   A OD1 1 
ATOM   362  N ND2 . ASN   A 1 46  ? -6.004  19.809  8.456   1.00 65.86  ? 63  ASN   A ND2 1 
ATOM   363  N N   . ILE   A 1 47  ? -4.183  16.451  10.687  1.00 57.66  ? 64  ILE   A N   1 
ATOM   364  C CA  . ILE   A 1 47  ? -4.466  16.257  12.098  1.00 57.71  ? 64  ILE   A CA  1 
ATOM   365  C C   . ILE   A 1 47  ? -4.943  17.553  12.744  1.00 64.33  ? 64  ILE   A C   1 
ATOM   366  O O   . ILE   A 1 47  ? -5.954  17.572  13.447  1.00 65.57  ? 64  ILE   A O   1 
ATOM   367  C CB  . ILE   A 1 47  ? -3.230  15.691  12.831  1.00 51.49  ? 64  ILE   A CB  1 
ATOM   368  C CG1 . ILE   A 1 47  ? -2.687  14.471  12.088  1.00 48.48  ? 64  ILE   A CG1 1 
ATOM   369  C CG2 . ILE   A 1 47  ? -3.592  15.297  14.240  1.00 51.13  ? 64  ILE   A CG2 1 
ATOM   370  C CD1 . ILE   A 1 47  ? -1.472  13.861  12.740  1.00 53.43  ? 64  ILE   A CD1 1 
ATOM   371  N N   . ILE   A 1 48  ? -4.242  18.657  12.483  1.00 62.24  ? 65  ILE   A N   1 
ATOM   372  C CA  . ILE   A 1 48  ? -4.548  19.958  13.073  1.00 61.93  ? 65  ILE   A CA  1 
ATOM   373  C C   . ILE   A 1 48  ? -4.070  21.043  12.115  1.00 64.59  ? 65  ILE   A C   1 
ATOM   374  O O   . ILE   A 1 48  ? -2.992  20.935  11.523  1.00 60.74  ? 65  ILE   A O   1 
ATOM   375  C CB  . ILE   A 1 48  ? -3.899  20.122  14.467  1.00 61.83  ? 65  ILE   A CB  1 
ATOM   376  C CG1 . ILE   A 1 48  ? -4.696  19.381  15.543  1.00 58.75  ? 65  ILE   A CG1 1 
ATOM   377  C CG2 . ILE   A 1 48  ? -3.818  21.580  14.843  1.00 69.91  ? 65  ILE   A CG2 1 
ATOM   378  C CD1 . ILE   A 1 48  ? -5.993  20.063  15.928  1.00 71.45  ? 65  ILE   A CD1 1 
ATOM   379  N N   . GLN   A 1 49  ? -4.878  22.094  11.962  1.00 72.23  ? 66  GLN   A N   1 
ATOM   380  C CA  . GLN   A 1 49  ? -4.543  23.251  11.134  1.00 69.10  ? 66  GLN   A CA  1 
ATOM   381  C C   . GLN   A 1 49  ? -4.607  24.506  11.994  1.00 73.12  ? 66  GLN   A C   1 
ATOM   382  O O   . GLN   A 1 49  ? -5.693  24.915  12.417  1.00 78.64  ? 66  GLN   A O   1 
ATOM   383  C CB  . GLN   A 1 49  ? -5.498  23.378  9.949   1.00 70.35  ? 66  GLN   A CB  1 
ATOM   384  C CG  . GLN   A 1 49  ? -4.995  22.766  8.666   1.00 73.26  ? 66  GLN   A CG  1 
ATOM   385  C CD  . GLN   A 1 49  ? -5.421  23.548  7.442   1.00 72.66  ? 66  GLN   A CD  1 
ATOM   386  O OE1 . GLN   A 1 49  ? -5.966  24.647  7.551   1.00 70.24  ? 66  GLN   A OE1 1 
ATOM   387  N NE2 . GLN   A 1 49  ? -5.198  22.973  6.268   1.00 70.82  ? 66  GLN   A NE2 1 
ATOM   388  N N   . PHE   A 1 50  ? -3.454  25.121  12.246  1.00 70.35  ? 67  PHE   A N   1 
ATOM   389  C CA  . PHE   A 1 50  ? -3.379  26.357  13.023  1.00 70.70  ? 67  PHE   A CA  1 
ATOM   390  C C   . PHE   A 1 50  ? -3.098  27.517  12.073  1.00 63.51  ? 67  PHE   A C   1 
ATOM   391  O O   . PHE   A 1 50  ? -1.959  27.720  11.641  1.00 59.43  ? 67  PHE   A O   1 
ATOM   392  C CB  . PHE   A 1 50  ? -2.323  26.281  14.118  1.00 65.85  ? 67  PHE   A CB  1 
ATOM   393  C CG  . PHE   A 1 50  ? -2.529  27.288  15.214  1.00 64.34  ? 67  PHE   A CG  1 
ATOM   394  C CD1 . PHE   A 1 50  ? -3.361  27.007  16.286  1.00 69.93  ? 67  PHE   A CD1 1 
ATOM   395  C CD2 . PHE   A 1 50  ? -1.923  28.530  15.154  1.00 68.90  ? 67  PHE   A CD2 1 
ATOM   396  C CE1 . PHE   A 1 50  ? -3.561  27.937  17.290  1.00 68.06  ? 67  PHE   A CE1 1 
ATOM   397  C CE2 . PHE   A 1 50  ? -2.121  29.465  16.155  1.00 70.02  ? 67  PHE   A CE2 1 
ATOM   398  C CZ  . PHE   A 1 50  ? -2.940  29.167  17.223  1.00 67.19  ? 67  PHE   A CZ  1 
ATOM   399  N N   . VAL   A 1 51  ? -4.118  28.301  11.792  1.00 68.66  ? 68  VAL   A N   1 
ATOM   400  C CA  . VAL   A 1 51  ? -3.949  29.470  10.965  1.00 71.63  ? 68  VAL   A CA  1 
ATOM   401  C C   . VAL   A 1 51  ? -4.498  30.619  11.777  1.00 76.39  ? 68  VAL   A C   1 
ATOM   402  O O   . VAL   A 1 51  ? -5.332  30.412  12.653  1.00 75.12  ? 68  VAL   A O   1 
ATOM   403  C CB  . VAL   A 1 51  ? -4.709  29.340  9.665   1.00 74.68  ? 68  VAL   A CB  1 
ATOM   404  C CG1 . VAL   A 1 51  ? -3.811  28.745  8.596   1.00 70.65  ? 68  VAL   A CG1 1 
ATOM   405  C CG2 . VAL   A 1 51  ? -5.948  28.485  9.865   1.00 72.53  ? 68  VAL   A CG2 1 
ATOM   406  N N   . HIS   A 1 52  ? -4.028  31.829  11.519  1.00 87.99  ? 69  HIS   A N   1 
ATOM   407  C CA  . HIS   A 1 52  ? -4.447  32.974  12.315  1.00 83.03  ? 69  HIS   A CA  1 
ATOM   408  C C   . HIS   A 1 52  ? -4.229  32.627  13.762  1.00 84.97  ? 69  HIS   A C   1 
ATOM   409  O O   . HIS   A 1 52  ? -3.166  32.124  14.105  1.00 86.57  ? 69  HIS   A O   1 
ATOM   410  C CB  . HIS   A 1 52  ? -5.891  33.352  12.042  1.00 79.56  ? 69  HIS   A CB  1 
ATOM   411  C CG  . HIS   A 1 52  ? -6.257  33.294  10.594  1.00 87.14  ? 69  HIS   A CG  1 
ATOM   412  N ND1 . HIS   A 1 52  ? -7.463  32.803  10.148  1.00 90.40  ? 69  HIS   A ND1 1 
ATOM   413  C CD2 . HIS   A 1 52  ? -5.565  33.653  9.487   1.00 88.71  ? 69  HIS   A CD2 1 
ATOM   414  C CE1 . HIS   A 1 52  ? -7.503  32.868  8.830   1.00 89.27  ? 69  HIS   A CE1 1 
ATOM   415  N NE2 . HIS   A 1 52  ? -6.364  33.380  8.404   1.00 92.38  ? 69  HIS   A NE2 1 
ATOM   416  N N   . GLY   A 1 53  ? -5.205  32.869  14.621  1.00 77.08  ? 70  GLY   A N   1 
ATOM   417  C CA  . GLY   A 1 53  ? -4.981  32.644  16.039  1.00 78.21  ? 70  GLY   A CA  1 
ATOM   418  C C   . GLY   A 1 53  ? -5.624  31.413  16.620  1.00 78.28  ? 70  GLY   A C   1 
ATOM   419  O O   . GLY   A 1 53  ? -5.464  31.111  17.792  1.00 75.42  ? 70  GLY   A O   1 
ATOM   420  N N   . GLU   A 1 54  ? -6.356  30.697  15.801  1.00 75.56  ? 71  GLU   A N   1 
ATOM   421  C CA  . GLU   A 1 54  ? -7.060  29.506  16.261  1.00 79.45  ? 71  GLU   A CA  1 
ATOM   422  C C   . GLU   A 1 54  ? -6.825  28.344  15.301  1.00 81.56  ? 71  GLU   A C   1 
ATOM   423  O O   . GLU   A 1 54  ? -6.088  28.451  14.315  1.00 79.71  ? 71  GLU   A O   1 
ATOM   424  C CB  . GLU   A 1 54  ? -8.564  29.771  16.417  1.00 83.43  ? 71  GLU   A CB  1 
ATOM   425  C CG  . GLU   A 1 54  ? -8.911  31.158  16.935  1.00 84.07  ? 71  GLU   A CG  1 
ATOM   426  C CD  . GLU   A 1 54  ? -8.690  31.288  18.430  1.00 85.66  ? 71  GLU   A CD  1 
ATOM   427  O OE1 . GLU   A 1 54  ? -8.855  30.278  19.147  1.00 84.78  ? 71  GLU   A OE1 1 
ATOM   428  O OE2 . GLU   A 1 54  ? -8.350  32.400  18.887  1.00 76.63  ? 71  GLU   A OE2 1 
ATOM   429  N N   . GLU   A 1 55  ? -7.464  27.221  15.614  1.00 91.70  ? 72  GLU   A N   1 
ATOM   430  C CA  . GLU   A 1 55  ? -7.426  26.018  14.797  1.00 91.87  ? 72  GLU   A CA  1 
ATOM   431  C C   . GLU   A 1 55  ? -8.502  26.067  13.720  1.00 92.74  ? 72  GLU   A C   1 
ATOM   432  O O   . GLU   A 1 55  ? -9.580  26.633  13.915  1.00 96.98  ? 72  GLU   A O   1 
ATOM   433  C CB  . GLU   A 1 55  ? -7.614  24.762  15.652  1.00 97.87  ? 72  GLU   A CB  1 
ATOM   434  C CG  . GLU   A 1 55  ? -6.761  24.707  16.907  1.00 99.28  ? 72  GLU   A CG  1 
ATOM   435  C CD  . GLU   A 1 55  ? -7.291  23.710  17.921  1.00 105.82 ? 72  GLU   A CD  1 
ATOM   436  O OE1 . GLU   A 1 55  ? -8.495  23.379  17.856  1.00 109.01 ? 72  GLU   A OE1 1 
ATOM   437  O OE2 . GLU   A 1 55  ? -6.506  23.253  18.778  1.00 97.85  ? 72  GLU   A OE2 1 
ATOM   438  N N   . ASP   A 1 56  ? -8.194  25.468  12.574  1.00 82.36  ? 73  ASP   A N   1 
ATOM   439  C CA  . ASP   A 1 56  ? -9.133  25.334  11.462  1.00 78.57  ? 73  ASP   A CA  1 
ATOM   440  C C   . ASP   A 1 56  ? -9.511  23.857  11.378  1.00 85.65  ? 73  ASP   A C   1 
ATOM   441  O O   . ASP   A 1 56  ? -8.889  23.077  10.654  1.00 80.78  ? 73  ASP   A O   1 
ATOM   442  C CB  . ASP   A 1 56  ? -8.521  25.832  10.153  1.00 75.64  ? 73  ASP   A CB  1 
ATOM   443  C CG  . ASP   A 1 56  ? -9.454  26.745  9.383   1.00 78.52  ? 73  ASP   A CG  1 
ATOM   444  O OD1 . ASP   A 1 56  ? -10.680 26.516  9.428   1.00 81.01  ? 73  ASP   A OD1 1 
ATOM   445  O OD2 . ASP   A 1 56  ? -8.962  27.687  8.727   1.00 81.40  ? 73  ASP   A OD2 1 
ATOM   446  N N   . LEU   A 1 57  ? -10.545 23.480  12.131  1.00 88.35  ? 74  LEU   A N   1 
ATOM   447  C CA  . LEU   A 1 57  ? -10.976 22.091  12.205  1.00 86.29  ? 74  LEU   A CA  1 
ATOM   448  C C   . LEU   A 1 57  ? -11.853 21.675  11.030  1.00 82.26  ? 74  LEU   A C   1 
ATOM   449  O O   . LEU   A 1 57  ? -12.570 20.673  11.115  1.00 83.35  ? 74  LEU   A O   1 
ATOM   450  C CB  . LEU   A 1 57  ? -11.687 21.836  13.537  1.00 85.49  ? 74  LEU   A CB  1 
ATOM   451  C CG  . LEU   A 1 57  ? -10.870 22.060  14.810  1.00 88.66  ? 74  LEU   A CG  1 
ATOM   452  C CD1 . LEU   A 1 57  ? -11.729 21.817  16.039  1.00 85.48  ? 74  LEU   A CD1 1 
ATOM   453  C CD2 . LEU   A 1 57  ? -9.639  21.167  14.831  1.00 92.74  ? 74  LEU   A CD2 1 
ATOM   454  N N   . LYS   A 1 58  ? -11.805 22.428  9.933   1.00 76.05  ? 75  LYS   A N   1 
ATOM   455  C CA  . LYS   A 1 58  ? -12.582 22.082  8.751   1.00 75.61  ? 75  LYS   A CA  1 
ATOM   456  C C   . LYS   A 1 58  ? -11.984 20.982  7.887   1.00 74.17  ? 75  LYS   A C   1 
ATOM   457  O O   . LYS   A 1 58  ? -12.701 20.400  7.065   1.00 76.52  ? 75  LYS   A O   1 
ATOM   458  C CB  . LYS   A 1 58  ? -12.803 23.335  7.897   1.00 71.53  ? 75  LYS   A CB  1 
ATOM   459  N N   . VAL   A 1 59  ? -10.698 20.679  8.050   1.00 69.10  ? 76  VAL   A N   1 
ATOM   460  C CA  . VAL   A 1 59  ? -10.047 19.621  7.291   1.00 65.61  ? 76  VAL   A CA  1 
ATOM   461  C C   . VAL   A 1 59  ? -9.463  18.541  8.199   1.00 70.55  ? 76  VAL   A C   1 
ATOM   462  O O   . VAL   A 1 59  ? -8.980  17.515  7.705   1.00 68.63  ? 76  VAL   A O   1 
ATOM   463  C CB  . VAL   A 1 59  ? -8.984  20.235  6.345   1.00 70.41  ? 76  VAL   A CB  1 
ATOM   464  C CG1 . VAL   A 1 59  ? -7.861  19.284  5.912   1.00 71.58  ? 76  VAL   A CG1 1 
ATOM   465  C CG2 . VAL   A 1 59  ? -9.673  20.864  5.126   1.00 73.47  ? 76  VAL   A CG2 1 
ATOM   466  N N   . GLN   A 1 60  ? -9.633  18.673  9.515   1.00 67.07  ? 77  GLN   A N   1 
ATOM   467  C CA  . GLN   A 1 60  ? -9.134  17.666  10.443  1.00 68.72  ? 77  GLN   A CA  1 
ATOM   468  C C   . GLN   A 1 60  ? -9.840  16.336  10.206  1.00 67.10  ? 77  GLN   A C   1 
ATOM   469  O O   . GLN   A 1 60  ? -11.068 16.283  10.085  1.00 63.76  ? 77  GLN   A O   1 
ATOM   470  C CB  . GLN   A 1 60  ? -9.344  18.130  11.886  1.00 71.10  ? 77  GLN   A CB  1 
ATOM   471  C CG  . GLN   A 1 60  ? -9.344  17.007  12.919  1.00 74.50  ? 77  GLN   A CG  1 
ATOM   472  C CD  . GLN   A 1 60  ? -9.990  17.412  14.234  1.00 81.37  ? 77  GLN   A CD  1 
ATOM   473  O OE1 . GLN   A 1 60  ? -9.335  17.451  15.277  1.00 74.91  ? 77  GLN   A OE1 1 
ATOM   474  N NE2 . GLN   A 1 60  ? -11.285 17.711  14.191  1.00 85.64  ? 77  GLN   A NE2 1 
ATOM   475  N N   . HIS   A 1 61  ? -9.056  15.263  10.139  1.00 65.17  ? 78  HIS   A N   1 
ATOM   476  C CA  . HIS   A 1 61  ? -9.611  13.933  9.937   1.00 61.98  ? 78  HIS   A CA  1 
ATOM   477  C C   . HIS   A 1 61  ? -10.424 13.481  11.146  1.00 72.60  ? 78  HIS   A C   1 
ATOM   478  O O   . HIS   A 1 61  ? -10.130 13.833  12.292  1.00 74.28  ? 78  HIS   A O   1 
ATOM   479  C CB  . HIS   A 1 61  ? -8.497  12.929  9.650   1.00 58.69  ? 78  HIS   A CB  1 
ATOM   480  C CG  . HIS   A 1 61  ? -8.965  11.705  8.927   1.00 66.96  ? 78  HIS   A CG  1 
ATOM   481  N ND1 . HIS   A 1 61  ? -9.497  10.613  9.578   1.00 67.52  ? 78  HIS   A ND1 1 
ATOM   482  C CD2 . HIS   A 1 61  ? -9.000  11.410  7.606   1.00 64.99  ? 78  HIS   A CD2 1 
ATOM   483  C CE1 . HIS   A 1 61  ? -9.828  9.693   8.690   1.00 65.75  ? 78  HIS   A CE1 1 
ATOM   484  N NE2 . HIS   A 1 61  ? -9.537  10.151  7.486   1.00 68.07  ? 78  HIS   A NE2 1 
ATOM   485  N N   . SER   A 1 62  ? -11.467 12.692  10.870  1.00 73.52  ? 79  SER   A N   1 
ATOM   486  C CA  . SER   A 1 62  ? -12.337 12.201  11.935  1.00 72.90  ? 79  SER   A CA  1 
ATOM   487  C C   . SER   A 1 62  ? -11.565 11.359  12.944  1.00 72.92  ? 79  SER   A C   1 
ATOM   488  O O   . SER   A 1 62  ? -11.810 11.450  14.153  1.00 72.36  ? 79  SER   A O   1 
ATOM   489  C CB  . SER   A 1 62  ? -13.490 11.395  11.335  1.00 80.47  ? 79  SER   A CB  1 
ATOM   490  O OG  . SER   A 1 62  ? -14.310 12.209  10.514  1.00 84.87  ? 79  SER   A OG  1 
ATOM   491  N N   . SER   A 1 63  ? -10.627 10.534  12.467  1.00 78.07  ? 80  SER   A N   1 
ATOM   492  C CA  . SER   A 1 63  ? -9.851  9.684   13.365  1.00 81.00  ? 80  SER   A CA  1 
ATOM   493  C C   . SER   A 1 63  ? -9.036  10.489  14.367  1.00 81.22  ? 80  SER   A C   1 
ATOM   494  O O   . SER   A 1 63  ? -8.631  9.945   15.401  1.00 79.59  ? 80  SER   A O   1 
ATOM   495  C CB  . SER   A 1 63  ? -8.923  8.771   12.560  1.00 77.71  ? 80  SER   A CB  1 
ATOM   496  O OG  . SER   A 1 63  ? -9.662  7.846   11.783  1.00 91.09  ? 80  SER   A OG  1 
ATOM   497  N N   . TYR   A 1 64  ? -8.783  11.767  14.084  1.00 76.23  ? 81  TYR   A N   1 
ATOM   498  C CA  . TYR   A 1 64  ? -7.995  12.616  14.961  1.00 74.17  ? 81  TYR   A CA  1 
ATOM   499  C C   . TYR   A 1 64  ? -8.825  13.676  15.669  1.00 73.29  ? 81  TYR   A C   1 
ATOM   500  O O   . TYR   A 1 64  ? -8.302  14.358  16.556  1.00 71.21  ? 81  TYR   A O   1 
ATOM   501  C CB  . TYR   A 1 64  ? -6.853  13.272  14.171  1.00 62.33  ? 81  TYR   A CB  1 
ATOM   502  C CG  . TYR   A 1 64  ? -5.782  12.275  13.794  1.00 53.39  ? 81  TYR   A CG  1 
ATOM   503  C CD1 . TYR   A 1 64  ? -4.980  11.692  14.767  1.00 49.74  ? 81  TYR   A CD1 1 
ATOM   504  C CD2 . TYR   A 1 64  ? -5.594  11.889  12.473  1.00 54.08  ? 81  TYR   A CD2 1 
ATOM   505  C CE1 . TYR   A 1 64  ? -4.010  10.771  14.435  1.00 53.82  ? 81  TYR   A CE1 1 
ATOM   506  C CE2 . TYR   A 1 64  ? -4.625  10.965  12.131  1.00 51.41  ? 81  TYR   A CE2 1 
ATOM   507  C CZ  . TYR   A 1 64  ? -3.836  10.410  13.118  1.00 54.40  ? 81  TYR   A CZ  1 
ATOM   508  O OH  . TYR   A 1 64  ? -2.869  9.489   12.793  1.00 56.98  ? 81  TYR   A OH  1 
ATOM   509  N N   . ARG   A 1 65  ? -10.096 13.826  15.310  1.00 83.14  ? 82  ARG   A N   1 
ATOM   510  C CA  . ARG   A 1 65  ? -11.008 14.629  16.110  1.00 82.05  ? 82  ARG   A CA  1 
ATOM   511  C C   . ARG   A 1 65  ? -11.220 13.965  17.468  1.00 82.49  ? 82  ARG   A C   1 
ATOM   512  O O   . ARG   A 1 65  ? -11.213 12.735  17.582  1.00 85.54  ? 82  ARG   A O   1 
ATOM   513  C CB  . ARG   A 1 65  ? -12.339 14.801  15.376  1.00 80.60  ? 82  ARG   A CB  1 
ATOM   514  C CG  . ARG   A 1 65  ? -13.521 15.156  16.266  1.00 84.31  ? 82  ARG   A CG  1 
ATOM   515  C CD  . ARG   A 1 65  ? -14.492 16.081  15.560  1.00 85.86  ? 82  ARG   A CD  1 
ATOM   516  N NE  . ARG   A 1 65  ? -15.267 15.367  14.554  1.00 81.10  ? 82  ARG   A NE  1 
ATOM   517  C CZ  . ARG   A 1 65  ? -14.991 15.371  13.257  1.00 84.34  ? 82  ARG   A CZ  1 
ATOM   518  N NH1 . ARG   A 1 65  ? -13.962 16.046  12.772  1.00 84.81  ? 82  ARG   A NH1 1 
ATOM   519  N NH2 . ARG   A 1 65  ? -15.764 14.676  12.428  1.00 76.96  ? 82  ARG   A NH2 1 
ATOM   520  N N   . GLN   A 1 66  ? -11.382 14.791  18.505  1.00 70.21  ? 83  GLN   A N   1 
ATOM   521  C CA  . GLN   A 1 66  ? -11.513 14.417  19.913  1.00 74.53  ? 83  GLN   A CA  1 
ATOM   522  C C   . GLN   A 1 66  ? -10.310 13.639  20.434  1.00 75.16  ? 83  GLN   A C   1 
ATOM   523  O O   . GLN   A 1 66  ? -10.343 13.171  21.578  1.00 75.23  ? 83  GLN   A O   1 
ATOM   524  C CB  . GLN   A 1 66  ? -12.790 13.612  20.200  1.00 70.92  ? 83  GLN   A CB  1 
ATOM   525  N N   . ARG   A 1 67  ? -9.250  13.493  19.644  1.00 67.96  ? 84  ARG   A N   1 
ATOM   526  C CA  . ARG   A 1 67  ? -8.013  12.860  20.075  1.00 67.12  ? 84  ARG   A CA  1 
ATOM   527  C C   . ARG   A 1 67  ? -6.796  13.755  19.921  1.00 60.49  ? 84  ARG   A C   1 
ATOM   528  O O   . ARG   A 1 67  ? -5.822  13.583  20.657  1.00 56.79  ? 84  ARG   A O   1 
ATOM   529  C CB  . ARG   A 1 67  ? -7.761  11.567  19.279  1.00 66.70  ? 84  ARG   A CB  1 
ATOM   530  C CG  . ARG   A 1 67  ? -8.674  10.403  19.618  1.00 63.06  ? 84  ARG   A CG  1 
ATOM   531  C CD  . ARG   A 1 67  ? -8.026  9.074   19.241  1.00 57.94  ? 84  ARG   A CD  1 
ATOM   532  N NE  . ARG   A 1 67  ? -7.569  9.050   17.855  1.00 58.42  ? 84  ARG   A NE  1 
ATOM   533  C CZ  . ARG   A 1 67  ? -6.428  8.506   17.451  1.00 58.37  ? 84  ARG   A CZ  1 
ATOM   534  N NH1 . ARG   A 1 67  ? -5.595  7.933   18.304  1.00 53.06  ? 84  ARG   A NH1 1 
ATOM   535  N NH2 . ARG   A 1 67  ? -6.117  8.535   16.158  1.00 53.37  ? 84  ARG   A NH2 1 
ATOM   536  N N   . ALA   A 1 68  ? -6.826  14.697  18.984  1.00 59.03  ? 85  ALA   A N   1 
ATOM   537  C CA  . ALA   A 1 68  ? -5.689  15.543  18.662  1.00 57.80  ? 85  ALA   A CA  1 
ATOM   538  C C   . ALA   A 1 68  ? -5.883  16.949  19.211  1.00 61.68  ? 85  ALA   A C   1 
ATOM   539  O O   . ALA   A 1 68  ? -6.971  17.525  19.102  1.00 65.35  ? 85  ALA   A O   1 
ATOM   540  C CB  . ALA   A 1 68  ? -5.475  15.614  17.151  1.00 56.71  ? 85  ALA   A CB  1 
ATOM   541  N N   . ARG   A 1 69  ? -4.822  17.494  19.799  1.00 56.42  ? 86  ARG   A N   1 
ATOM   542  C CA  . ARG   A 1 69  ? -4.817  18.874  20.259  1.00 62.08  ? 86  ARG   A CA  1 
ATOM   543  C C   . ARG   A 1 69  ? -3.392  19.403  20.206  1.00 58.59  ? 86  ARG   A C   1 
ATOM   544  O O   . ARG   A 1 69  ? -2.455  18.712  20.617  1.00 56.95  ? 86  ARG   A O   1 
ATOM   545  C CB  . ARG   A 1 69  ? -5.372  18.990  21.685  1.00 60.68  ? 86  ARG   A CB  1 
ATOM   546  C CG  . ARG   A 1 69  ? -4.754  18.006  22.671  1.00 61.73  ? 86  ARG   A CG  1 
ATOM   547  C CD  . ARG   A 1 69  ? -5.266  18.223  24.087  1.00 68.68  ? 86  ARG   A CD  1 
ATOM   548  N NE  . ARG   A 1 69  ? -4.751  19.455  24.673  1.00 77.39  ? 86  ARG   A NE  1 
ATOM   549  C CZ  . ARG   A 1 69  ? -3.998  19.509  25.764  1.00 81.61  ? 86  ARG   A CZ  1 
ATOM   550  N NH1 . ARG   A 1 69  ? -3.640  18.413  26.413  1.00 75.08  ? 86  ARG   A NH1 1 
ATOM   551  N NH2 . ARG   A 1 69  ? -3.592  20.694  26.214  1.00 79.74  ? 86  ARG   A NH2 1 
ATOM   552  N N   . LEU   A 1 70  ? -3.230  20.623  19.698  1.00 60.22  ? 87  LEU   A N   1 
ATOM   553  C CA  . LEU   A 1 70  ? -1.941  21.299  19.749  1.00 62.54  ? 87  LEU   A CA  1 
ATOM   554  C C   . LEU   A 1 70  ? -1.893  22.152  21.008  1.00 61.03  ? 87  LEU   A C   1 
ATOM   555  O O   . LEU   A 1 70  ? -2.862  22.848  21.332  1.00 61.93  ? 87  LEU   A O   1 
ATOM   556  C CB  . LEU   A 1 70  ? -1.670  22.150  18.501  1.00 59.78  ? 87  LEU   A CB  1 
ATOM   557  C CG  . LEU   A 1 70  ? -2.365  23.455  18.089  1.00 66.64  ? 87  LEU   A CG  1 
ATOM   558  C CD1 . LEU   A 1 70  ? -1.990  24.640  18.962  1.00 68.04  ? 87  LEU   A CD1 1 
ATOM   559  C CD2 . LEU   A 1 70  ? -1.956  23.769  16.668  1.00 62.51  ? 87  LEU   A CD2 1 
ATOM   560  N N   . LEU   A 1 71  ? -0.785  22.071  21.732  1.00 58.99  ? 88  LEU   A N   1 
ATOM   561  C CA  . LEU   A 1 71  ? -0.635  22.829  22.970  1.00 59.54  ? 88  LEU   A CA  1 
ATOM   562  C C   . LEU   A 1 71  ? -0.424  24.296  22.614  1.00 61.93  ? 88  LEU   A C   1 
ATOM   563  O O   . LEU   A 1 71  ? 0.678   24.709  22.246  1.00 63.82  ? 88  LEU   A O   1 
ATOM   564  C CB  . LEU   A 1 71  ? 0.523   22.278  23.795  1.00 62.53  ? 88  LEU   A CB  1 
ATOM   565  C CG  . LEU   A 1 71  ? 0.654   20.754  23.888  1.00 66.76  ? 88  LEU   A CG  1 
ATOM   566  C CD1 . LEU   A 1 71  ? 1.731   20.377  24.892  1.00 65.33  ? 88  LEU   A CD1 1 
ATOM   567  C CD2 . LEU   A 1 71  ? -0.672  20.103  24.264  1.00 65.21  ? 88  LEU   A CD2 1 
ATOM   568  N N   . LYS   A 1 72  ? -1.495  25.089  22.712  1.00 63.37  ? 89  LYS   A N   1 
ATOM   569  C CA  . LYS   A 1 72  ? -1.412  26.504  22.363  1.00 59.54  ? 89  LYS   A CA  1 
ATOM   570  C C   . LYS   A 1 72  ? -0.502  27.269  23.313  1.00 56.21  ? 89  LYS   A C   1 
ATOM   571  O O   . LYS   A 1 72  ? 0.129   28.251  22.905  1.00 54.63  ? 89  LYS   A O   1 
ATOM   572  C CB  . LYS   A 1 72  ? -2.806  27.130  22.358  1.00 54.58  ? 89  LYS   A CB  1 
ATOM   573  C CG  . LYS   A 1 72  ? -3.394  27.340  20.971  1.00 54.12  ? 89  LYS   A CG  1 
ATOM   574  C CD  . LYS   A 1 72  ? -4.900  27.563  21.025  1.00 64.38  ? 89  LYS   A CD  1 
ATOM   575  C CE  . LYS   A 1 72  ? -5.317  28.296  22.293  1.00 59.00  ? 89  LYS   A CE  1 
ATOM   576  N NZ  . LYS   A 1 72  ? -6.378  29.306  22.033  1.00 58.94  ? 89  LYS   A NZ  1 
ATOM   577  N N   . ASP   A 1 73  ? -0.426  26.845  24.576  1.00 53.21  ? 90  ASP   A N   1 
ATOM   578  C CA  . ASP   A 1 73  ? 0.460   27.511  25.524  1.00 52.38  ? 90  ASP   A CA  1 
ATOM   579  C C   . ASP   A 1 73  ? 1.914   27.399  25.087  1.00 62.49  ? 90  ASP   A C   1 
ATOM   580  O O   . ASP   A 1 73  ? 2.702   28.334  25.276  1.00 63.48  ? 90  ASP   A O   1 
ATOM   581  C CB  . ASP   A 1 73  ? 0.274   26.916  26.920  1.00 55.10  ? 90  ASP   A CB  1 
ATOM   582  C CG  . ASP   A 1 73  ? 0.444   25.406  26.937  1.00 67.48  ? 90  ASP   A CG  1 
ATOM   583  O OD1 . ASP   A 1 73  ? 0.382   24.786  25.854  1.00 63.02  ? 90  ASP   A OD1 1 
ATOM   584  O OD2 . ASP   A 1 73  ? 0.642   24.837  28.031  1.00 64.75  ? 90  ASP   A OD2 1 
ATOM   585  N N   . GLN   A 1 74  ? 2.289   26.262  24.500  1.00 61.66  ? 91  GLN   A N   1 
ATOM   586  C CA  . GLN   A 1 74  ? 3.661   26.052  24.061  1.00 59.63  ? 91  GLN   A CA  1 
ATOM   587  C C   . GLN   A 1 74  ? 4.001   26.803  22.779  1.00 59.85  ? 91  GLN   A C   1 
ATOM   588  O O   . GLN   A 1 74  ? 5.188   26.926  22.456  1.00 56.37  ? 91  GLN   A O   1 
ATOM   589  C CB  . GLN   A 1 74  ? 3.923   24.557  23.861  1.00 56.17  ? 91  GLN   A CB  1 
ATOM   590  C CG  . GLN   A 1 74  ? 4.061   23.764  25.152  1.00 55.10  ? 91  GLN   A CG  1 
ATOM   591  C CD  . GLN   A 1 74  ? 5.405   23.967  25.825  1.00 56.09  ? 91  GLN   A CD  1 
ATOM   592  O OE1 . GLN   A 1 74  ? 6.430   24.109  25.159  1.00 50.39  ? 91  GLN   A OE1 1 
ATOM   593  N NE2 . GLN   A 1 74  ? 5.407   23.979  27.153  1.00 54.75  ? 91  GLN   A NE2 1 
ATOM   594  N N   . LEU   A 1 75  ? 3.004   27.302  22.040  1.00 65.12  ? 92  LEU   A N   1 
ATOM   595  C CA  . LEU   A 1 75  ? 3.310   28.048  20.824  1.00 62.94  ? 92  LEU   A CA  1 
ATOM   596  C C   . LEU   A 1 75  ? 4.009   29.365  21.132  1.00 67.32  ? 92  LEU   A C   1 
ATOM   597  O O   . LEU   A 1 75  ? 4.826   29.833  20.330  1.00 70.27  ? 92  LEU   A O   1 
ATOM   598  C CB  . LEU   A 1 75  ? 2.028   28.315  20.033  1.00 63.36  ? 92  LEU   A CB  1 
ATOM   599  C CG  . LEU   A 1 75  ? 1.224   27.118  19.524  1.00 63.26  ? 92  LEU   A CG  1 
ATOM   600  C CD1 . LEU   A 1 75  ? 0.138   27.580  18.566  1.00 65.21  ? 92  LEU   A CD1 1 
ATOM   601  C CD2 . LEU   A 1 75  ? 2.134   26.106  18.851  1.00 64.31  ? 92  LEU   A CD2 1 
ATOM   602  N N   . SER   A 1 76  ? 3.696   29.977  22.277  1.00 68.54  ? 93  SER   A N   1 
ATOM   603  C CA  . SER   A 1 76  ? 4.420   31.165  22.717  1.00 64.96  ? 93  SER   A CA  1 
ATOM   604  C C   . SER   A 1 76  ? 5.911   30.878  22.838  1.00 66.11  ? 93  SER   A C   1 
ATOM   605  O O   . SER   A 1 76  ? 6.750   31.670  22.393  1.00 70.24  ? 93  SER   A O   1 
ATOM   606  C CB  . SER   A 1 76  ? 3.849   31.667  24.043  1.00 61.99  ? 93  SER   A CB  1 
ATOM   607  O OG  . SER   A 1 76  ? 3.402   30.586  24.840  1.00 70.13  ? 93  SER   A OG  1 
ATOM   608  N N   . LEU   A 1 77  ? 6.256   29.744  23.447  1.00 57.65  ? 94  LEU   A N   1 
ATOM   609  C CA  . LEU   A 1 77  ? 7.636   29.318  23.633  1.00 58.72  ? 94  LEU   A CA  1 
ATOM   610  C C   . LEU   A 1 77  ? 8.226   28.666  22.389  1.00 54.89  ? 94  LEU   A C   1 
ATOM   611  O O   . LEU   A 1 77  ? 9.305   28.070  22.471  1.00 61.88  ? 94  LEU   A O   1 
ATOM   612  C CB  . LEU   A 1 77  ? 7.725   28.350  24.817  1.00 56.20  ? 94  LEU   A CB  1 
ATOM   613  C CG  . LEU   A 1 77  ? 7.190   28.864  26.156  1.00 61.77  ? 94  LEU   A CG  1 
ATOM   614  C CD1 . LEU   A 1 77  ? 6.740   27.706  27.034  1.00 54.75  ? 94  LEU   A CD1 1 
ATOM   615  C CD2 . LEU   A 1 77  ? 8.236   29.708  26.868  1.00 69.44  ? 94  LEU   A CD2 1 
ATOM   616  N N   . GLY   A 1 78  ? 7.545   28.763  21.252  1.00 54.36  ? 95  GLY   A N   1 
ATOM   617  C CA  . GLY   A 1 78  ? 8.032   28.187  20.010  1.00 55.67  ? 95  GLY   A CA  1 
ATOM   618  C C   . GLY   A 1 78  ? 8.077   26.675  19.988  1.00 53.83  ? 95  GLY   A C   1 
ATOM   619  O O   . GLY   A 1 78  ? 8.991   26.094  19.388  1.00 54.31  ? 95  GLY   A O   1 
ATOM   620  N N   . ASN   A 1 79  ? 7.112   26.021  20.628  1.00 55.92  ? 96  ASN   A N   1 
ATOM   621  C CA  . ASN   A 1 79  ? 7.002   24.563  20.639  1.00 52.83  ? 96  ASN   A CA  1 
ATOM   622  C C   . ASN   A 1 79  ? 5.638   24.192  20.065  1.00 55.69  ? 96  ASN   A C   1 
ATOM   623  O O   . ASN   A 1 79  ? 4.620   24.294  20.756  1.00 51.73  ? 96  ASN   A O   1 
ATOM   624  C CB  . ASN   A 1 79  ? 7.187   24.001  22.045  1.00 52.98  ? 96  ASN   A CB  1 
ATOM   625  C CG  . ASN   A 1 79  ? 7.362   22.492  22.050  1.00 52.93  ? 96  ASN   A CG  1 
ATOM   626  O OD1 . ASN   A 1 79  ? 7.465   21.864  20.996  1.00 50.20  ? 96  ASN   A OD1 1 
ATOM   627  N ND2 . ASN   A 1 79  ? 7.399   21.904  23.240  1.00 51.23  ? 96  ASN   A ND2 1 
ATOM   628  N N   . ALA   A 1 80  ? 5.614   23.761  18.807  1.00 55.39  ? 97  ALA   A N   1 
ATOM   629  C CA  . ALA   A 1 80  ? 4.381   23.267  18.199  1.00 51.70  ? 97  ALA   A CA  1 
ATOM   630  C C   . ALA   A 1 80  ? 4.235   21.804  18.593  1.00 53.00  ? 97  ALA   A C   1 
ATOM   631  O O   . ALA   A 1 80  ? 4.745   20.900  17.930  1.00 60.75  ? 97  ALA   A O   1 
ATOM   632  C CB  . ALA   A 1 80  ? 4.409   23.445  16.686  1.00 47.15  ? 97  ALA   A CB  1 
ATOM   633  N N   . ALA   A 1 81  ? 3.520   21.571  19.690  1.00 52.75  ? 98  ALA   A N   1 
ATOM   634  C CA  . ALA   A 1 81  ? 3.414   20.252  20.299  1.00 57.11  ? 98  ALA   A CA  1 
ATOM   635  C C   . ALA   A 1 81  ? 2.019   19.695  20.058  1.00 55.91  ? 98  ALA   A C   1 
ATOM   636  O O   . ALA   A 1 81  ? 1.023   20.304  20.465  1.00 56.83  ? 98  ALA   A O   1 
ATOM   637  C CB  . ALA   A 1 81  ? 3.718   20.319  21.796  1.00 54.44  ? 98  ALA   A CB  1 
ATOM   638  N N   . LEU   A 1 82  ? 1.953   18.539  19.405  1.00 52.16  ? 99  LEU   A N   1 
ATOM   639  C CA  . LEU   A 1 82  ? 0.698   17.867  19.100  1.00 52.73  ? 99  LEU   A CA  1 
ATOM   640  C C   . LEU   A 1 82  ? 0.522   16.689  20.045  1.00 53.36  ? 99  LEU   A C   1 
ATOM   641  O O   . LEU   A 1 82  ? 1.447   15.890  20.227  1.00 49.67  ? 99  LEU   A O   1 
ATOM   642  C CB  . LEU   A 1 82  ? 0.672   17.374  17.653  1.00 47.71  ? 99  LEU   A CB  1 
ATOM   643  C CG  . LEU   A 1 82  ? -0.620  16.699  17.181  1.00 51.17  ? 99  LEU   A CG  1 
ATOM   644  C CD1 . LEU   A 1 82  ? -1.877  17.404  17.709  1.00 55.62  ? 99  LEU   A CD1 1 
ATOM   645  C CD2 . LEU   A 1 82  ? -0.637  16.576  15.672  1.00 49.49  ? 99  LEU   A CD2 1 
ATOM   646  N N   . GLN   A 1 83  ? -0.660  16.580  20.640  1.00 53.97  ? 100 GLN   A N   1 
ATOM   647  C CA  . GLN   A 1 83  ? -0.971  15.502  21.566  1.00 52.17  ? 100 GLN   A CA  1 
ATOM   648  C C   . GLN   A 1 83  ? -2.060  14.622  20.972  1.00 51.94  ? 100 GLN   A C   1 
ATOM   649  O O   . GLN   A 1 83  ? -3.107  15.122  20.547  1.00 54.85  ? 100 GLN   A O   1 
ATOM   650  C CB  . GLN   A 1 83  ? -1.418  16.061  22.919  1.00 50.53  ? 100 GLN   A CB  1 
ATOM   651  C CG  . GLN   A 1 83  ? -2.415  15.187  23.660  1.00 57.61  ? 100 GLN   A CG  1 
ATOM   652  C CD  . GLN   A 1 83  ? -2.346  15.375  25.160  1.00 62.38  ? 100 GLN   A CD  1 
ATOM   653  O OE1 . GLN   A 1 83  ? -1.264  15.518  25.729  1.00 61.54  ? 100 GLN   A OE1 1 
ATOM   654  N NE2 . GLN   A 1 83  ? -3.504  15.376  25.811  1.00 67.48  ? 100 GLN   A NE2 1 
ATOM   655  N N   . ILE   A 1 84  ? -1.805  13.317  20.935  1.00 55.82  ? 101 ILE   A N   1 
ATOM   656  C CA  . ILE   A 1 84  ? -2.780  12.324  20.498  1.00 53.30  ? 101 ILE   A CA  1 
ATOM   657  C C   . ILE   A 1 84  ? -3.054  11.416  21.687  1.00 52.25  ? 101 ILE   A C   1 
ATOM   658  O O   . ILE   A 1 84  ? -2.129  10.796  22.226  1.00 53.68  ? 101 ILE   A O   1 
ATOM   659  C CB  . ILE   A 1 84  ? -2.281  11.518  19.288  1.00 52.30  ? 101 ILE   A CB  1 
ATOM   660  C CG1 . ILE   A 1 84  ? -1.653  12.448  18.246  1.00 51.82  ? 101 ILE   A CG1 1 
ATOM   661  C CG2 . ILE   A 1 84  ? -3.421  10.717  18.674  1.00 51.00  ? 101 ILE   A CG2 1 
ATOM   662  C CD1 . ILE   A 1 84  ? -2.644  13.357  17.555  1.00 45.98  ? 101 ILE   A CD1 1 
ATOM   663  N N   . THR   A 1 85  ? -4.316  11.335  22.093  1.00 53.92  ? 102 THR   A N   1 
ATOM   664  C CA  . THR   A 1 85  ? -4.727  10.461  23.181  1.00 60.92  ? 102 THR   A CA  1 
ATOM   665  C C   . THR   A 1 85  ? -5.249  9.134   22.641  1.00 59.10  ? 102 THR   A C   1 
ATOM   666  O O   . THR   A 1 85  ? -5.873  9.077   21.578  1.00 54.56  ? 102 THR   A O   1 
ATOM   667  C CB  . THR   A 1 85  ? -5.799  11.130  24.044  1.00 55.91  ? 102 THR   A CB  1 
ATOM   668  O OG1 . THR   A 1 85  ? -6.668  11.909  23.213  1.00 58.54  ? 102 THR   A OG1 1 
ATOM   669  C CG2 . THR   A 1 85  ? -5.153  12.038  25.083  1.00 54.05  ? 102 THR   A CG2 1 
ATOM   670  N N   . ASP   A 1 86  ? -4.982  8.066   23.392  1.00 59.67  ? 103 ASP   A N   1 
ATOM   671  C CA  . ASP   A 1 86  ? -5.336  6.699   23.009  1.00 63.58  ? 103 ASP   A CA  1 
ATOM   672  C C   . ASP   A 1 86  ? -4.760  6.348   21.637  1.00 61.42  ? 103 ASP   A C   1 
ATOM   673  O O   . ASP   A 1 86  ? -5.479  6.095   20.668  1.00 65.28  ? 103 ASP   A O   1 
ATOM   674  C CB  . ASP   A 1 86  ? -6.853  6.498   23.043  1.00 64.46  ? 103 ASP   A CB  1 
ATOM   675  C CG  . ASP   A 1 86  ? -7.241  5.041   23.165  1.00 69.06  ? 103 ASP   A CG  1 
ATOM   676  O OD1 . ASP   A 1 86  ? -7.229  4.515   24.298  1.00 74.03  ? 103 ASP   A OD1 1 
ATOM   677  O OD2 . ASP   A 1 86  ? -7.553  4.422   22.127  1.00 73.87  ? 103 ASP   A OD2 1 
ATOM   678  N N   . VAL   A 1 87  ? -3.428  6.356   21.572  1.00 57.57  ? 104 VAL   A N   1 
ATOM   679  C CA  . VAL   A 1 87  ? -2.721  5.905   20.378  1.00 60.67  ? 104 VAL   A CA  1 
ATOM   680  C C   . VAL   A 1 87  ? -3.122  4.481   20.019  1.00 54.95  ? 104 VAL   A C   1 
ATOM   681  O O   . VAL   A 1 87  ? -3.110  3.577   20.864  1.00 56.04  ? 104 VAL   A O   1 
ATOM   682  C CB  . VAL   A 1 87  ? -1.205  6.020   20.578  1.00 58.78  ? 104 VAL   A CB  1 
ATOM   683  C CG1 . VAL   A 1 87  ? -0.485  5.373   19.413  1.00 53.14  ? 104 VAL   A CG1 1 
ATOM   684  C CG2 . VAL   A 1 87  ? -0.809  7.476   20.711  1.00 57.85  ? 104 VAL   A CG2 1 
ATOM   685  N N   . LYS   A 1 88  ? -3.479  4.279   18.757  1.00 53.20  ? 105 LYS   A N   1 
ATOM   686  C CA  . LYS   A 1 88  ? -3.848  2.983   18.212  1.00 58.20  ? 105 LYS   A CA  1 
ATOM   687  C C   . LYS   A 1 88  ? -2.852  2.593   17.122  1.00 58.79  ? 105 LYS   A C   1 
ATOM   688  O O   . LYS   A 1 88  ? -2.013  3.396   16.704  1.00 58.71  ? 105 LYS   A O   1 
ATOM   689  C CB  . LYS   A 1 88  ? -5.288  3.005   17.686  1.00 58.82  ? 105 LYS   A CB  1 
ATOM   690  N N   . LEU   A 1 89  ? -2.945  1.335   16.668  1.00 57.70  ? 106 LEU   A N   1 
ATOM   691  C CA  . LEU   A 1 89  ? -1.987  0.800   15.698  1.00 58.07  ? 106 LEU   A CA  1 
ATOM   692  C C   . LEU   A 1 89  ? -1.902  1.633   14.426  1.00 58.57  ? 106 LEU   A C   1 
ATOM   693  O O   . LEU   A 1 89  ? -0.832  1.715   13.810  1.00 57.56  ? 106 LEU   A O   1 
ATOM   694  C CB  . LEU   A 1 89  ? -2.363  -0.632  15.317  1.00 61.85  ? 106 LEU   A CB  1 
ATOM   695  C CG  . LEU   A 1 89  ? -1.855  -1.785  16.179  1.00 59.02  ? 106 LEU   A CG  1 
ATOM   696  C CD1 . LEU   A 1 89  ? -0.358  -1.664  16.442  1.00 49.15  ? 106 LEU   A CD1 1 
ATOM   697  C CD2 . LEU   A 1 89  ? -2.649  -1.849  17.470  1.00 56.20  ? 106 LEU   A CD2 1 
ATOM   698  N N   . GLN   A 1 90  ? -3.003  2.260   14.021  1.00 56.80  ? 107 GLN   A N   1 
ATOM   699  C CA  . GLN   A 1 90  ? -3.024  3.050   12.798  1.00 60.43  ? 107 GLN   A CA  1 
ATOM   700  C C   . GLN   A 1 90  ? -2.338  4.400   12.952  1.00 57.56  ? 107 GLN   A C   1 
ATOM   701  O O   . GLN   A 1 90  ? -2.091  5.066   11.941  1.00 53.62  ? 107 GLN   A O   1 
ATOM   702  C CB  . GLN   A 1 90  ? -4.467  3.261   12.312  1.00 67.19  ? 107 GLN   A CB  1 
ATOM   703  C CG  . GLN   A 1 90  ? -5.427  2.057   12.430  1.00 73.29  ? 107 GLN   A CG  1 
ATOM   704  C CD  . GLN   A 1 90  ? -5.803  1.694   13.859  1.00 71.83  ? 107 GLN   A CD  1 
ATOM   705  O OE1 . GLN   A 1 90  ? -5.237  2.219   14.812  1.00 71.36  ? 107 GLN   A OE1 1 
ATOM   706  N NE2 . GLN   A 1 90  ? -6.761  0.787   14.009  1.00 73.94  ? 107 GLN   A NE2 1 
ATOM   707  N N   . ASP   A 1 91  ? -2.016  4.812   14.175  1.00 57.82  ? 108 ASP   A N   1 
ATOM   708  C CA  . ASP   A 1 91  ? -1.293  6.054   14.403  1.00 56.08  ? 108 ASP   A CA  1 
ATOM   709  C C   . ASP   A 1 91  ? 0.209   5.912   14.186  1.00 54.77  ? 108 ASP   A C   1 
ATOM   710  O O   . ASP   A 1 91  ? 0.954   6.861   14.455  1.00 57.58  ? 108 ASP   A O   1 
ATOM   711  C CB  . ASP   A 1 91  ? -1.573  6.570   15.817  1.00 54.92  ? 108 ASP   A CB  1 
ATOM   712  C CG  . ASP   A 1 91  ? -3.009  7.018   15.994  1.00 58.01  ? 108 ASP   A CG  1 
ATOM   713  O OD1 . ASP   A 1 91  ? -3.524  7.719   15.099  1.00 60.28  ? 108 ASP   A OD1 1 
ATOM   714  O OD2 . ASP   A 1 91  ? -3.625  6.668   17.023  1.00 61.30  ? 108 ASP   A OD2 1 
ATOM   715  N N   . ALA   A 1 92  ? 0.667   4.759   13.707  1.00 52.86  ? 109 ALA   A N   1 
ATOM   716  C CA  . ALA   A 1 92  ? 2.071   4.560   13.386  1.00 51.48  ? 109 ALA   A CA  1 
ATOM   717  C C   . ALA   A 1 92  ? 2.331   4.975   11.945  1.00 52.23  ? 109 ALA   A C   1 
ATOM   718  O O   . ALA   A 1 92  ? 1.543   4.670   11.045  1.00 49.94  ? 109 ALA   A O   1 
ATOM   719  C CB  . ALA   A 1 92  ? 2.475   3.100   13.595  1.00 40.11  ? 109 ALA   A CB  1 
ATOM   720  N N   . GLY   A 1 93  ? 3.437   5.669   11.733  1.00 47.62  ? 110 GLY   A N   1 
ATOM   721  C CA  . GLY   A 1 93  ? 3.788   6.150   10.415  1.00 46.28  ? 110 GLY   A CA  1 
ATOM   722  C C   . GLY   A 1 93  ? 4.625   7.408   10.516  1.00 46.88  ? 110 GLY   A C   1 
ATOM   723  O O   . GLY   A 1 93  ? 5.195   7.708   11.561  1.00 42.53  ? 110 GLY   A O   1 
ATOM   724  N N   . VAL   A 1 94  ? 4.680   8.134   9.403   1.00 50.27  ? 111 VAL   A N   1 
ATOM   725  C CA  . VAL   A 1 94  ? 5.497   9.334   9.275   1.00 47.56  ? 111 VAL   A CA  1 
ATOM   726  C C   . VAL   A 1 94  ? 4.605   10.554  9.460   1.00 48.10  ? 111 VAL   A C   1 
ATOM   727  O O   . VAL   A 1 94  ? 3.667   10.772  8.683   1.00 48.38  ? 111 VAL   A O   1 
ATOM   728  C CB  . VAL   A 1 94  ? 6.217   9.376   7.918   1.00 42.62  ? 111 VAL   A CB  1 
ATOM   729  C CG1 . VAL   A 1 94  ? 6.706   10.786  7.614   1.00 50.28  ? 111 VAL   A CG1 1 
ATOM   730  C CG2 . VAL   A 1 94  ? 7.369   8.383   7.900   1.00 43.55  ? 111 VAL   A CG2 1 
ATOM   731  N N   . TYR   A 1 95  ? 4.888   11.342  10.493  1.00 42.29  ? 112 TYR   A N   1 
ATOM   732  C CA  . TYR   A 1 95  ? 4.196   12.597  10.740  1.00 51.18  ? 112 TYR   A CA  1 
ATOM   733  C C   . TYR   A 1 95  ? 5.011   13.748  10.160  1.00 46.81  ? 112 TYR   A C   1 
ATOM   734  O O   . TYR   A 1 95  ? 6.237   13.669  10.058  1.00 46.27  ? 112 TYR   A O   1 
ATOM   735  C CB  . TYR   A 1 95  ? 3.974   12.819  12.239  1.00 50.96  ? 112 TYR   A CB  1 
ATOM   736  C CG  . TYR   A 1 95  ? 2.963   11.884  12.869  1.00 51.61  ? 112 TYR   A CG  1 
ATOM   737  C CD1 . TYR   A 1 95  ? 3.212   10.521  12.967  1.00 50.73  ? 112 TYR   A CD1 1 
ATOM   738  C CD2 . TYR   A 1 95  ? 1.764   12.368  13.374  1.00 51.15  ? 112 TYR   A CD2 1 
ATOM   739  C CE1 . TYR   A 1 95  ? 2.292   9.666   13.544  1.00 53.84  ? 112 TYR   A CE1 1 
ATOM   740  C CE2 . TYR   A 1 95  ? 0.838   11.520  13.953  1.00 47.93  ? 112 TYR   A CE2 1 
ATOM   741  C CZ  . TYR   A 1 95  ? 1.107   10.171  14.035  1.00 53.07  ? 112 TYR   A CZ  1 
ATOM   742  O OH  . TYR   A 1 95  ? 0.188   9.323   14.610  1.00 48.75  ? 112 TYR   A OH  1 
ATOM   743  N N   . ARG   A 1 96  ? 4.321   14.820  9.776   1.00 42.47  ? 113 ARG   A N   1 
ATOM   744  C CA  . ARG   A 1 96  ? 4.970   15.990  9.194   1.00 48.49  ? 113 ARG   A CA  1 
ATOM   745  C C   . ARG   A 1 96  ? 4.406   17.254  9.826   1.00 47.08  ? 113 ARG   A C   1 
ATOM   746  O O   . ARG   A 1 96  ? 3.198   17.502  9.746   1.00 43.78  ? 113 ARG   A O   1 
ATOM   747  C CB  . ARG   A 1 96  ? 4.781   16.022  7.674   1.00 46.59  ? 113 ARG   A CB  1 
ATOM   748  C CG  . ARG   A 1 96  ? 5.869   15.301  6.896   1.00 40.82  ? 113 ARG   A CG  1 
ATOM   749  C CD  . ARG   A 1 96  ? 5.674   15.465  5.396   1.00 45.92  ? 113 ARG   A CD  1 
ATOM   750  N NE  . ARG   A 1 96  ? 6.018   14.254  4.659   1.00 55.79  ? 113 ARG   A NE  1 
ATOM   751  C CZ  . ARG   A 1 96  ? 5.290   13.145  4.648   1.00 56.87  ? 113 ARG   A CZ  1 
ATOM   752  N NH1 . ARG   A 1 96  ? 4.150   13.059  5.315   1.00 49.93  ? 113 ARG   A NH1 1 
ATOM   753  N NH2 . ARG   A 1 96  ? 5.717   12.096  3.951   1.00 57.73  ? 113 ARG   A NH2 1 
ATOM   754  N N   . CYS   A 1 97  ? 5.275   18.048  10.448  1.00 40.24  ? 114 CYS   A N   1 
ATOM   755  C CA  . CYS   A 1 97  ? 4.910   19.356  10.983  1.00 48.27  ? 114 CYS   A CA  1 
ATOM   756  C C   . CYS   A 1 97  ? 5.518   20.442  10.108  1.00 47.72  ? 114 CYS   A C   1 
ATOM   757  O O   . CYS   A 1 97  ? 6.730   20.450  9.867   1.00 42.19  ? 114 CYS   A O   1 
ATOM   758  C CB  . CYS   A 1 97  ? 5.340   19.517  12.441  1.00 45.33  ? 114 CYS   A CB  1 
ATOM   759  S SG  . CYS   A 1 97  ? 7.012   20.080  12.800  1.00 56.26  ? 114 CYS   A SG  1 
ATOM   760  N N   . MET   A 1 98  ? 4.667   21.326  9.600   1.00 43.93  ? 115 MET   A N   1 
ATOM   761  C CA  . MET   A 1 98  ? 5.079   22.424  8.738   1.00 50.92  ? 115 MET   A CA  1 
ATOM   762  C C   . MET   A 1 98  ? 4.709   23.729  9.428   1.00 51.86  ? 115 MET   A C   1 
ATOM   763  O O   . MET   A 1 98  ? 3.542   23.939  9.780   1.00 52.25  ? 115 MET   A O   1 
ATOM   764  C CB  . MET   A 1 98  ? 4.414   22.309  7.366   1.00 47.18  ? 115 MET   A CB  1 
ATOM   765  C CG  . MET   A 1 98  ? 4.013   20.887  7.012   1.00 46.53  ? 115 MET   A CG  1 
ATOM   766  S SD  . MET   A 1 98  ? 3.324   20.724  5.357   1.00 51.70  ? 115 MET   A SD  1 
ATOM   767  C CE  . MET   A 1 98  ? 3.343   18.945  5.162   1.00 40.52  ? 115 MET   A CE  1 
ATOM   768  N N   . ILE   A 1 99  ? 5.696   24.600  9.622   1.00 49.27  ? 116 ILE   A N   1 
ATOM   769  C CA  . ILE   A 1 99  ? 5.520   25.837  10.372  1.00 53.02  ? 116 ILE   A CA  1 
ATOM   770  C C   . ILE   A 1 99  ? 5.932   27.012  9.497   1.00 50.27  ? 116 ILE   A C   1 
ATOM   771  O O   . ILE   A 1 99  ? 6.966   26.967  8.821   1.00 46.60  ? 116 ILE   A O   1 
ATOM   772  C CB  . ILE   A 1 99  ? 6.328   25.821  11.687  1.00 50.46  ? 116 ILE   A CB  1 
ATOM   773  C CG1 . ILE   A 1 99  ? 5.703   24.841  12.680  1.00 52.63  ? 116 ILE   A CG1 1 
ATOM   774  C CG2 . ILE   A 1 99  ? 6.408   27.212  12.300  1.00 50.31  ? 116 ILE   A CG2 1 
ATOM   775  C CD1 . ILE   A 1 99  ? 6.486   23.569  12.843  1.00 45.50  ? 116 ILE   A CD1 1 
ATOM   776  N N   . SER   A 1 100 ? 5.114   28.064  9.516   1.00 54.10  ? 117 SER   A N   1 
ATOM   777  C CA  . SER   A 1 100 ? 5.399   29.314  8.819   1.00 51.35  ? 117 SER   A CA  1 
ATOM   778  C C   . SER   A 1 100 ? 5.284   30.457  9.819   1.00 49.88  ? 117 SER   A C   1 
ATOM   779  O O   . SER   A 1 100 ? 4.186   30.761  10.296  1.00 51.68  ? 117 SER   A O   1 
ATOM   780  C CB  . SER   A 1 100 ? 4.451   29.518  7.636   1.00 45.82  ? 117 SER   A CB  1 
ATOM   781  O OG  . SER   A 1 100 ? 4.792   30.680  6.902   1.00 43.59  ? 117 SER   A OG  1 
ATOM   782  N N   . TYR   A 1 101 ? 6.423   31.082  10.144  1.00 49.98  ? 118 TYR   A N   1 
ATOM   783  C CA  . TYR   A 1 101 ? 6.507   32.198  11.091  1.00 52.87  ? 118 TYR   A CA  1 
ATOM   784  C C   . TYR   A 1 101 ? 7.649   33.094  10.601  1.00 58.45  ? 118 TYR   A C   1 
ATOM   785  O O   . TYR   A 1 101 ? 8.781   33.042  11.087  1.00 57.43  ? 118 TYR   A O   1 
ATOM   786  C CB  . TYR   A 1 101 ? 6.732   31.728  12.528  1.00 53.19  ? 118 TYR   A CB  1 
ATOM   787  C CG  . TYR   A 1 101 ? 6.713   32.842  13.551  1.00 57.60  ? 118 TYR   A CG  1 
ATOM   788  C CD1 . TYR   A 1 101 ? 5.752   33.844  13.499  1.00 63.23  ? 118 TYR   A CD1 1 
ATOM   789  C CD2 . TYR   A 1 101 ? 7.658   32.893  14.568  1.00 59.40  ? 118 TYR   A CD2 1 
ATOM   790  C CE1 . TYR   A 1 101 ? 5.732   34.865  14.432  1.00 65.10  ? 118 TYR   A CE1 1 
ATOM   791  C CE2 . TYR   A 1 101 ? 7.645   33.910  15.506  1.00 68.81  ? 118 TYR   A CE2 1 
ATOM   792  C CZ  . TYR   A 1 101 ? 6.680   34.893  15.433  1.00 67.22  ? 118 TYR   A CZ  1 
ATOM   793  O OH  . TYR   A 1 101 ? 6.664   35.907  16.363  1.00 72.89  ? 118 TYR   A OH  1 
ATOM   794  N N   . GLY   A 1 102 ? 7.334   33.933  9.615   1.00 60.67  ? 119 GLY   A N   1 
ATOM   795  C CA  . GLY   A 1 102 ? 8.344   34.691  8.904   1.00 59.47  ? 119 GLY   A CA  1 
ATOM   796  C C   . GLY   A 1 102 ? 8.945   33.817  7.824   1.00 59.23  ? 119 GLY   A C   1 
ATOM   797  O O   . GLY   A 1 102 ? 8.829   34.112  6.631   1.00 63.32  ? 119 GLY   A O   1 
ATOM   798  N N   . GLY   A 1 103 ? 9.589   32.728  8.241   1.00 55.86  ? 120 GLY   A N   1 
ATOM   799  C CA  . GLY   A 1 103 ? 10.151  31.760  7.329   1.00 53.86  ? 120 GLY   A CA  1 
ATOM   800  C C   . GLY   A 1 103 ? 9.265   30.531  7.228   1.00 54.27  ? 120 GLY   A C   1 
ATOM   801  O O   . GLY   A 1 103 ? 8.121   30.512  7.686   1.00 55.42  ? 120 GLY   A O   1 
ATOM   802  N N   . ALA   A 1 104 ? 9.813   29.483  6.621   1.00 51.82  ? 121 ALA   A N   1 
ATOM   803  C CA  . ALA   A 1 104 ? 9.055   28.250  6.468   1.00 52.40  ? 121 ALA   A CA  1 
ATOM   804  C C   . ALA   A 1 104 ? 10.004  27.065  6.408   1.00 51.79  ? 121 ALA   A C   1 
ATOM   805  O O   . ALA   A 1 104 ? 11.026  27.107  5.717   1.00 53.64  ? 121 ALA   A O   1 
ATOM   806  C CB  . ALA   A 1 104 ? 8.176   28.287  5.212   1.00 52.49  ? 121 ALA   A CB  1 
ATOM   807  N N   . ASP   A 1 105 ? 9.649   26.009  7.135   1.00 45.34  ? 122 ASP   A N   1 
ATOM   808  C CA  . ASP   A 1 105 ? 10.392  24.758  7.124   1.00 48.05  ? 122 ASP   A CA  1 
ATOM   809  C C   . ASP   A 1 105 ? 9.475   23.662  7.646   1.00 53.70  ? 122 ASP   A C   1 
ATOM   810  O O   . ASP   A 1 105 ? 8.399   23.929  8.186   1.00 55.38  ? 122 ASP   A O   1 
ATOM   811  C CB  . ASP   A 1 105 ? 11.677  24.852  7.954   1.00 48.48  ? 122 ASP   A CB  1 
ATOM   812  C CG  . ASP   A 1 105 ? 12.691  23.787  7.579   1.00 52.42  ? 122 ASP   A CG  1 
ATOM   813  O OD1 . ASP   A 1 105 ? 12.744  23.409  6.390   1.00 51.26  ? 122 ASP   A OD1 1 
ATOM   814  O OD2 . ASP   A 1 105 ? 13.432  23.325  8.473   1.00 51.98  ? 122 ASP   A OD2 1 
ATOM   815  N N   . TYR   A 1 106 ? 9.915   22.418  7.475   1.00 53.53  ? 123 TYR   A N   1 
ATOM   816  C CA  . TYR   A 1 106 ? 9.154   21.273  7.946   1.00 46.92  ? 123 TYR   A CA  1 
ATOM   817  C C   . TYR   A 1 106 ? 10.117  20.169  8.356   1.00 47.84  ? 123 TYR   A C   1 
ATOM   818  O O   . TYR   A 1 106 ? 11.241  20.086  7.853   1.00 46.67  ? 123 TYR   A O   1 
ATOM   819  C CB  . TYR   A 1 106 ? 8.188   20.755  6.873   1.00 47.64  ? 123 TYR   A CB  1 
ATOM   820  C CG  . TYR   A 1 106 ? 8.741   19.595  6.075   1.00 55.83  ? 123 TYR   A CG  1 
ATOM   821  C CD1 . TYR   A 1 106 ? 9.635   19.809  5.034   1.00 50.14  ? 123 TYR   A CD1 1 
ATOM   822  C CD2 . TYR   A 1 106 ? 8.374   18.286  6.365   1.00 46.31  ? 123 TYR   A CD2 1 
ATOM   823  C CE1 . TYR   A 1 106 ? 10.147  18.755  4.306   1.00 51.28  ? 123 TYR   A CE1 1 
ATOM   824  C CE2 . TYR   A 1 106 ? 8.882   17.226  5.643   1.00 45.39  ? 123 TYR   A CE2 1 
ATOM   825  C CZ  . TYR   A 1 106 ? 9.767   17.466  4.614   1.00 51.31  ? 123 TYR   A CZ  1 
ATOM   826  O OH  . TYR   A 1 106 ? 10.276  16.414  3.889   1.00 58.84  ? 123 TYR   A OH  1 
ATOM   827  N N   . LYS   A 1 107 ? 9.661   19.323  9.276   1.00 45.97  ? 124 LYS   A N   1 
ATOM   828  C CA  . LYS   A 1 107 ? 10.428  18.172  9.726   1.00 48.64  ? 124 LYS   A CA  1 
ATOM   829  C C   . LYS   A 1 107 ? 9.485   16.992  9.902   1.00 45.43  ? 124 LYS   A C   1 
ATOM   830  O O   . LYS   A 1 107 ? 8.307   17.161  10.224  1.00 47.43  ? 124 LYS   A O   1 
ATOM   831  C CB  . LYS   A 1 107 ? 11.167  18.459  11.040  1.00 50.61  ? 124 LYS   A CB  1 
ATOM   832  C CG  . LYS   A 1 107 ? 12.347  19.406  10.897  1.00 55.00  ? 124 LYS   A CG  1 
ATOM   833  C CD  . LYS   A 1 107 ? 13.658  18.646  10.790  1.00 46.54  ? 124 LYS   A CD  1 
ATOM   834  C CE  . LYS   A 1 107 ? 14.700  19.454  10.037  1.00 50.68  ? 124 LYS   A CE  1 
ATOM   835  N NZ  . LYS   A 1 107 ? 14.145  20.033  8.783   1.00 54.72  ? 124 LYS   A NZ  1 
ATOM   836  N N   . ARG   A 1 108 ? 10.016  15.793  9.690   1.00 44.88  ? 125 ARG   A N   1 
ATOM   837  C CA  . ARG   A 1 108 ? 9.232   14.571  9.757   1.00 47.51  ? 125 ARG   A CA  1 
ATOM   838  C C   . ARG   A 1 108 ? 9.562   13.793  11.023  1.00 47.69  ? 125 ARG   A C   1 
ATOM   839  O O   . ARG   A 1 108 ? 10.705  13.779  11.488  1.00 53.35  ? 125 ARG   A O   1 
ATOM   840  C CB  . ARG   A 1 108 ? 9.471   13.688  8.529   1.00 42.61  ? 125 ARG   A CB  1 
ATOM   841  C CG  . ARG   A 1 108 ? 10.932  13.445  8.215   1.00 50.57  ? 125 ARG   A CG  1 
ATOM   842  C CD  . ARG   A 1 108 ? 11.083  12.503  7.031   1.00 60.91  ? 125 ARG   A CD  1 
ATOM   843  N NE  . ARG   A 1 108 ? 11.153  13.222  5.764   1.00 66.80  ? 125 ARG   A NE  1 
ATOM   844  C CZ  . ARG   A 1 108 ? 12.192  13.942  5.362   1.00 68.48  ? 125 ARG   A CZ  1 
ATOM   845  N NH1 . ARG   A 1 108 ? 13.281  14.063  6.104   1.00 67.28  ? 125 ARG   A NH1 1 
ATOM   846  N NH2 . ARG   A 1 108 ? 12.137  14.557  4.183   1.00 64.88  ? 125 ARG   A NH2 1 
ATOM   847  N N   . ILE   A 1 109 ? 8.542   13.141  11.575  1.00 44.34  ? 126 ILE   A N   1 
ATOM   848  C CA  . ILE   A 1 109 ? 8.681   12.315  12.765  1.00 47.50  ? 126 ILE   A CA  1 
ATOM   849  C C   . ILE   A 1 109 ? 8.049   10.961  12.481  1.00 50.27  ? 126 ILE   A C   1 
ATOM   850  O O   . ILE   A 1 109 ? 6.969   10.883  11.885  1.00 51.51  ? 126 ILE   A O   1 
ATOM   851  C CB  . ILE   A 1 109 ? 8.026   12.976  13.997  1.00 48.04  ? 126 ILE   A CB  1 
ATOM   852  C CG1 . ILE   A 1 109 ? 8.752   14.271  14.365  1.00 48.70  ? 126 ILE   A CG1 1 
ATOM   853  C CG2 . ILE   A 1 109 ? 8.018   12.024  15.179  1.00 41.76  ? 126 ILE   A CG2 1 
ATOM   854  C CD1 . ILE   A 1 109 ? 7.822   15.393  14.774  1.00 49.86  ? 126 ILE   A CD1 1 
ATOM   855  N N   . THR   A 1 110 ? 8.720   9.896   12.910  1.00 49.82  ? 127 THR   A N   1 
ATOM   856  C CA  . THR   A 1 110 ? 8.247   8.533   12.718  1.00 45.01  ? 127 THR   A CA  1 
ATOM   857  C C   . THR   A 1 110 ? 7.774   7.986   14.056  1.00 43.61  ? 127 THR   A C   1 
ATOM   858  O O   . THR   A 1 110 ? 8.495   8.072   15.055  1.00 42.37  ? 127 THR   A O   1 
ATOM   859  C CB  . THR   A 1 110 ? 9.349   7.645   12.134  1.00 50.28  ? 127 THR   A CB  1 
ATOM   860  O OG1 . THR   A 1 110 ? 10.157  8.415   11.236  1.00 54.79  ? 127 THR   A OG1 1 
ATOM   861  C CG2 . THR   A 1 110 ? 8.746   6.469   11.382  1.00 49.55  ? 127 THR   A CG2 1 
ATOM   862  N N   . VAL   A 1 111 ? 6.569   7.424   14.075  1.00 44.00  ? 128 VAL   A N   1 
ATOM   863  C CA  . VAL   A 1 111 ? 5.961   6.895   15.289  1.00 43.19  ? 128 VAL   A CA  1 
ATOM   864  C C   . VAL   A 1 111 ? 5.829   5.386   15.149  1.00 46.30  ? 128 VAL   A C   1 
ATOM   865  O O   . VAL   A 1 111 ? 5.263   4.892   14.166  1.00 49.04  ? 128 VAL   A O   1 
ATOM   866  C CB  . VAL   A 1 111 ? 4.593   7.545   15.562  1.00 49.48  ? 128 VAL   A CB  1 
ATOM   867  C CG1 . VAL   A 1 111 ? 3.777   6.694   16.524  1.00 43.92  ? 128 VAL   A CG1 1 
ATOM   868  C CG2 . VAL   A 1 111 ? 4.776   8.954   16.109  1.00 49.31  ? 128 VAL   A CG2 1 
ATOM   869  N N   . LYS   A 1 112 ? 6.362   4.658   16.126  1.00 48.21  ? 129 LYS   A N   1 
ATOM   870  C CA  . LYS   A 1 112 ? 6.197   3.217   16.228  1.00 45.12  ? 129 LYS   A CA  1 
ATOM   871  C C   . LYS   A 1 112 ? 5.299   2.905   17.415  1.00 45.98  ? 129 LYS   A C   1 
ATOM   872  O O   . LYS   A 1 112 ? 5.472   3.469   18.500  1.00 46.91  ? 129 LYS   A O   1 
ATOM   873  C CB  . LYS   A 1 112 ? 7.547   2.511   16.386  1.00 43.57  ? 129 LYS   A CB  1 
ATOM   874  N N   . VAL   A 1 113 ? 4.335   2.013   17.208  1.00 50.95  ? 130 VAL   A N   1 
ATOM   875  C CA  . VAL   A 1 113 ? 3.325   1.699   18.211  1.00 49.38  ? 130 VAL   A CA  1 
ATOM   876  C C   . VAL   A 1 113 ? 3.433   0.218   18.541  1.00 43.58  ? 130 VAL   A C   1 
ATOM   877  O O   . VAL   A 1 113 ? 3.118   -0.636  17.702  1.00 45.45  ? 130 VAL   A O   1 
ATOM   878  C CB  . VAL   A 1 113 ? 1.911   2.055   17.734  1.00 51.75  ? 130 VAL   A CB  1 
ATOM   879  C CG1 . VAL   A 1 113 ? 0.881   1.679   18.793  1.00 51.74  ? 130 VAL   A CG1 1 
ATOM   880  C CG2 . VAL   A 1 113 ? 1.825   3.532   17.387  1.00 42.24  ? 130 VAL   A CG2 1 
ATOM   881  N N   . ASN   A 1 114 ? 3.879   -0.090  19.756  1.00 44.26  ? 131 ASN   A N   1 
ATOM   882  C CA  . ASN   A 1 114 ? 3.810   -1.454  20.256  1.00 47.52  ? 131 ASN   A CA  1 
ATOM   883  C C   . ASN   A 1 114 ? 2.406   -1.738  20.776  1.00 49.25  ? 131 ASN   A C   1 
ATOM   884  O O   . ASN   A 1 114 ? 1.725   -0.851  21.300  1.00 55.73  ? 131 ASN   A O   1 
ATOM   885  C CB  . ASN   A 1 114 ? 4.835   -1.681  21.368  1.00 45.00  ? 131 ASN   A CB  1 
ATOM   886  C CG  . ASN   A 1 114 ? 6.259   -1.444  20.907  1.00 44.08  ? 131 ASN   A CG  1 
ATOM   887  O OD1 . ASN   A 1 114 ? 6.575   -1.590  19.727  1.00 43.71  ? 131 ASN   A OD1 1 
ATOM   888  N ND2 . ASN   A 1 114 ? 7.129   -1.078  21.841  1.00 44.40  ? 131 ASN   A ND2 1 
ATOM   889  N N   . ALA   A 1 115 ? 1.975   -2.988  20.633  1.00 44.84  ? 132 ALA   A N   1 
ATOM   890  C CA  . ALA   A 1 115 ? 0.611   -3.343  20.992  1.00 47.95  ? 132 ALA   A CA  1 
ATOM   891  C C   . ALA   A 1 115 ? 0.532   -4.824  21.328  1.00 47.23  ? 132 ALA   A C   1 
ATOM   892  O O   . ALA   A 1 115 ? 1.295   -5.624  20.776  1.00 51.37  ? 132 ALA   A O   1 
ATOM   893  C CB  . ALA   A 1 115 ? -0.365  -3.016  19.855  1.00 49.92  ? 132 ALA   A CB  1 
ATOM   894  N N   . PRO   A 1 116 ? -0.381  -5.212  22.214  1.00 51.40  ? 133 PRO   A N   1 
ATOM   895  C CA  . PRO   A 1 116 ? -0.573  -6.638  22.507  1.00 48.74  ? 133 PRO   A CA  1 
ATOM   896  C C   . PRO   A 1 116 ? -1.245  -7.362  21.349  1.00 52.45  ? 133 PRO   A C   1 
ATOM   897  O O   . PRO   A 1 116 ? -1.651  -6.772  20.346  1.00 52.07  ? 133 PRO   A O   1 
ATOM   898  C CB  . PRO   A 1 116 ? -1.462  -6.628  23.753  1.00 51.01  ? 133 PRO   A CB  1 
ATOM   899  C CG  . PRO   A 1 116 ? -2.187  -5.324  23.684  1.00 54.27  ? 133 PRO   A CG  1 
ATOM   900  C CD  . PRO   A 1 116 ? -1.229  -4.353  23.057  1.00 51.88  ? 133 PRO   A CD  1 
ATOM   901  N N   . TYR   A 1 117 ? -1.352  -8.683  21.513  1.00 57.49  ? 134 TYR   A N   1 
ATOM   902  C CA  . TYR   A 1 117 ? -1.902  -9.534  20.461  1.00 59.17  ? 134 TYR   A CA  1 
ATOM   903  C C   . TYR   A 1 117 ? -3.352  -9.179  20.147  1.00 60.12  ? 134 TYR   A C   1 
ATOM   904  O O   . TYR   A 1 117 ? -3.753  -9.163  18.977  1.00 55.94  ? 134 TYR   A O   1 
ATOM   905  C CB  . TYR   A 1 117 ? -1.784  -11.001 20.874  1.00 57.18  ? 134 TYR   A CB  1 
ATOM   906  C CG  . TYR   A 1 117 ? -2.167  -11.987 19.797  1.00 58.37  ? 134 TYR   A CG  1 
ATOM   907  C CD1 . TYR   A 1 117 ? -1.299  -12.279 18.755  1.00 55.58  ? 134 TYR   A CD1 1 
ATOM   908  C CD2 . TYR   A 1 117 ? -3.396  -12.633 19.826  1.00 53.57  ? 134 TYR   A CD2 1 
ATOM   909  C CE1 . TYR   A 1 117 ? -1.645  -13.182 17.769  1.00 53.27  ? 134 TYR   A CE1 1 
ATOM   910  C CE2 . TYR   A 1 117 ? -3.751  -13.537 18.846  1.00 55.11  ? 134 TYR   A CE2 1 
ATOM   911  C CZ  . TYR   A 1 117 ? -2.872  -13.808 17.819  1.00 58.16  ? 134 TYR   A CZ  1 
ATOM   912  O OH  . TYR   A 1 117 ? -3.223  -14.710 16.839  1.00 57.21  ? 134 TYR   A OH  1 
ATOM   913  N N   . ALA   A 1 118 ? -4.157  -8.909  21.180  1.00 75.51  ? 135 ALA   A N   1 
ATOM   914  C CA  . ALA   A 1 118 ? -5.576  -8.629  20.973  1.00 76.36  ? 135 ALA   A CA  1 
ATOM   915  C C   . ALA   A 1 118 ? -5.778  -7.427  20.057  1.00 75.72  ? 135 ALA   A C   1 
ATOM   916  O O   . ALA   A 1 118 ? -6.518  -7.502  19.069  1.00 76.23  ? 135 ALA   A O   1 
ATOM   917  C CB  . ALA   A 1 118 ? -6.269  -8.404  22.317  1.00 77.39  ? 135 ALA   A CB  1 
ATOM   918  N N   . ALA   A 1 119 ? -5.129  -6.303  20.375  1.00 61.61  ? 136 ALA   A N   1 
ATOM   919  C CA  . ALA   A 1 119 ? -5.260  -5.110  19.545  1.00 58.07  ? 136 ALA   A CA  1 
ATOM   920  C C   . ALA   A 1 119 ? -4.700  -5.335  18.147  1.00 58.22  ? 136 ALA   A C   1 
ATOM   921  O O   . ALA   A 1 119 ? -5.226  -4.788  17.171  1.00 55.37  ? 136 ALA   A O   1 
ATOM   922  C CB  . ALA   A 1 119 ? -4.564  -3.924  20.212  1.00 57.29  ? 136 ALA   A CB  1 
ATOM   923  N N   . ALA   A 1 120 ? -3.640  -6.138  18.030  1.00 57.14  ? 137 ALA   A N   1 
ATOM   924  C CA  . ALA   A 1 120 ? -3.040  -6.388  16.724  1.00 54.76  ? 137 ALA   A CA  1 
ATOM   925  C C   . ALA   A 1 120 ? -3.956  -7.247  15.861  1.00 56.99  ? 137 ALA   A C   1 
ATOM   926  O O   . ALA   A 1 120 ? -4.088  -7.007  14.655  1.00 52.32  ? 137 ALA   A O   1 
ATOM   927  C CB  . ALA   A 1 120 ? -1.673  -7.049  16.890  1.00 47.24  ? 137 ALA   A CB  1 
ATOM   928  N N   . LEU   A 1 121 ? -4.580  -8.264  16.461  1.00 57.83  ? 138 LEU   A N   1 
ATOM   929  C CA  . LEU   A 1 121 ? -5.566  -9.065  15.743  1.00 60.58  ? 138 LEU   A CA  1 
ATOM   930  C C   . LEU   A 1 121 ? -6.703  -8.195  15.220  1.00 64.80  ? 138 LEU   A C   1 
ATOM   931  O O   . LEU   A 1 121 ? -7.247  -8.453  14.140  1.00 67.78  ? 138 LEU   A O   1 
ATOM   932  C CB  . LEU   A 1 121 ? -6.110  -10.163 16.657  1.00 62.34  ? 138 LEU   A CB  1 
ATOM   933  C CG  . LEU   A 1 121 ? -6.444  -11.513 16.019  1.00 52.68  ? 138 LEU   A CG  1 
ATOM   934  C CD1 . LEU   A 1 121 ? -5.337  -11.958 15.074  1.00 53.68  ? 138 LEU   A CD1 1 
ATOM   935  C CD2 . LEU   A 1 121 ? -6.696  -12.559 17.092  1.00 53.66  ? 138 LEU   A CD2 1 
ATOM   936  N N   . GLU   A 1 122 ? -7.079  -7.162  15.980  1.00 63.55  ? 139 GLU   A N   1 
ATOM   937  C CA  . GLU   A 1 122 ? -8.133  -6.254  15.541  1.00 61.38  ? 139 GLU   A CA  1 
ATOM   938  C C   . GLU   A 1 122 ? -7.727  -5.498  14.282  1.00 65.40  ? 139 GLU   A C   1 
ATOM   939  O O   . GLU   A 1 122 ? -8.545  -5.303  13.375  1.00 69.78  ? 139 GLU   A O   1 
ATOM   940  C CB  . GLU   A 1 122 ? -8.474  -5.274  16.662  1.00 65.69  ? 139 GLU   A CB  1 
ATOM   941  C CG  . GLU   A 1 122 ? -9.326  -5.859  17.772  1.00 68.53  ? 139 GLU   A CG  1 
ATOM   942  C CD  . GLU   A 1 122 ? -9.371  -4.964  18.994  1.00 70.54  ? 139 GLU   A CD  1 
ATOM   943  O OE1 . GLU   A 1 122 ? -9.382  -3.728  18.824  1.00 67.17  ? 139 GLU   A OE1 1 
ATOM   944  O OE2 . GLU   A 1 122 ? -9.392  -5.494  20.124  1.00 71.97  ? 139 GLU   A OE2 1 
ATOM   945  N N   . HIS   A 1 123 ? -6.465  -5.066  14.205  1.00 75.06  ? 140 HIS   A N   1 
ATOM   946  C CA  . HIS   A 1 123 ? -5.994  -4.399  12.997  1.00 80.37  ? 140 HIS   A CA  1 
ATOM   947  C C   . HIS   A 1 123 ? -5.894  -5.369  11.827  1.00 82.41  ? 140 HIS   A C   1 
ATOM   948  O O   . HIS   A 1 123 ? -6.103  -4.973  10.675  1.00 86.21  ? 140 HIS   A O   1 
ATOM   949  C CB  . HIS   A 1 123 ? -4.639  -3.740  13.259  1.00 78.34  ? 140 HIS   A CB  1 
ATOM   950  C CG  . HIS   A 1 123 ? -4.349  -2.572  12.367  1.00 82.93  ? 140 HIS   A CG  1 
ATOM   951  N ND1 . HIS   A 1 123 ? -3.080  -2.061  12.200  1.00 81.59  ? 140 HIS   A ND1 1 
ATOM   952  C CD2 . HIS   A 1 123 ? -5.164  -1.814  11.596  1.00 89.67  ? 140 HIS   A CD2 1 
ATOM   953  C CE1 . HIS   A 1 123 ? -3.125  -1.040  11.363  1.00 88.02  ? 140 HIS   A CE1 1 
ATOM   954  N NE2 . HIS   A 1 123 ? -4.378  -0.869  10.982  1.00 92.57  ? 140 HIS   A NE2 1 
ATOM   955  N N   . HIS   A 1 124 ? -5.573  -6.635  12.102  1.00 72.88  ? 141 HIS   A N   1 
ATOM   956  C CA  . HIS   A 1 124 ? -5.497  -7.638  11.047  1.00 74.21  ? 141 HIS   A CA  1 
ATOM   957  C C   . HIS   A 1 124 ? -6.867  -7.988  10.481  1.00 78.12  ? 141 HIS   A C   1 
ATOM   958  O O   . HIS   A 1 124 ? -6.944  -8.482  9.350   1.00 82.59  ? 141 HIS   A O   1 
ATOM   959  C CB  . HIS   A 1 124 ? -4.806  -8.900  11.565  1.00 78.17  ? 141 HIS   A CB  1 
ATOM   960  C CG  . HIS   A 1 124 ? -4.539  -9.917  10.499  1.00 81.43  ? 141 HIS   A CG  1 
ATOM   961  N ND1 . HIS   A 1 124 ? -5.501  -10.792 10.043  1.00 89.90  ? 141 HIS   A ND1 1 
ATOM   962  C CD2 . HIS   A 1 124 ? -3.415  -10.194 9.796   1.00 67.10  ? 141 HIS   A CD2 1 
ATOM   963  C CE1 . HIS   A 1 124 ? -4.980  -11.566 9.107   1.00 91.63  ? 141 HIS   A CE1 1 
ATOM   964  N NE2 . HIS   A 1 124 ? -3.717  -11.223 8.937   1.00 80.71  ? 141 HIS   A NE2 1 
ATOM   965  N N   . HIS   A 1 125 ? -7.932  -7.776  11.253  1.00 79.52  ? 142 HIS   A N   1 
ATOM   966  C CA  . HIS   A 1 125 ? -9.313  -7.924  10.790  1.00 78.24  ? 142 HIS   A CA  1 
ATOM   967  C C   . HIS   A 1 125 ? -9.632  -9.387  10.500  1.00 76.73  ? 142 HIS   A C   1 
ATOM   968  O O   . HIS   A 1 125 ? -9.134  -10.285 11.179  1.00 78.33  ? 142 HIS   A O   1 
ATOM   969  C CB  . HIS   A 1 125 ? -9.577  -7.070  9.544   1.00 78.18  ? 142 HIS   A CB  1 
ATOM   970  C CG  . HIS   A 1 125 ? -9.792  -5.619  9.837   1.00 77.61  ? 142 HIS   A CG  1 
ATOM   971  N ND1 . HIS   A 1 125 ? -10.031 -5.141  11.108  1.00 79.72  ? 142 HIS   A ND1 1 
ATOM   972  C CD2 . HIS   A 1 125 ? -9.805  -4.538  9.021   1.00 75.72  ? 142 HIS   A CD2 1 
ATOM   973  C CE1 . HIS   A 1 125 ? -10.182 -3.830  11.062  1.00 83.11  ? 142 HIS   A CE1 1 
ATOM   974  N NE2 . HIS   A 1 125 ? -10.049 -3.438  9.807   1.00 82.13  ? 142 HIS   A NE2 1 
ATOM   975  N N   . ALA   B 1 1   ? -8.671  31.796  1.175   1.00 73.88  ? 18  ALA   B N   1 
ATOM   976  C CA  . ALA   B 1 1   ? -7.344  31.927  1.763   1.00 74.20  ? 18  ALA   B CA  1 
ATOM   977  C C   . ALA   B 1 1   ? -6.253  31.602  0.744   1.00 74.08  ? 18  ALA   B C   1 
ATOM   978  O O   . ALA   B 1 1   ? -6.510  31.541  -0.459  1.00 74.22  ? 18  ALA   B O   1 
ATOM   979  C CB  . ALA   B 1 1   ? -7.214  31.029  2.985   1.00 70.98  ? 18  ALA   B CB  1 
ATOM   980  N N   . PHE   B 1 2   ? -5.036  31.395  1.240   1.00 67.25  ? 19  PHE   B N   1 
ATOM   981  C CA  . PHE   B 1 2   ? -3.899  31.057  0.392   1.00 61.78  ? 19  PHE   B CA  1 
ATOM   982  C C   . PHE   B 1 2   ? -4.001  29.595  -0.028  1.00 58.84  ? 19  PHE   B C   1 
ATOM   983  O O   . PHE   B 1 2   ? -3.971  28.698  0.821   1.00 59.84  ? 19  PHE   B O   1 
ATOM   984  C CB  . PHE   B 1 2   ? -2.597  31.318  1.147   1.00 61.54  ? 19  PHE   B CB  1 
ATOM   985  C CG  . PHE   B 1 2   ? -1.356  31.041  0.347   1.00 55.06  ? 19  PHE   B CG  1 
ATOM   986  C CD1 . PHE   B 1 2   ? -0.901  31.949  -0.595  1.00 52.48  ? 19  PHE   B CD1 1 
ATOM   987  C CD2 . PHE   B 1 2   ? -0.642  29.871  0.539   1.00 60.70  ? 19  PHE   B CD2 1 
ATOM   988  C CE1 . PHE   B 1 2   ? 0.247   31.695  -1.325  1.00 60.49  ? 19  PHE   B CE1 1 
ATOM   989  C CE2 . PHE   B 1 2   ? 0.502   29.609  -0.192  1.00 58.39  ? 19  PHE   B CE2 1 
ATOM   990  C CZ  . PHE   B 1 2   ? 0.946   30.522  -1.126  1.00 60.24  ? 19  PHE   B CZ  1 
ATOM   991  N N   . THR   B 1 3   ? -4.129  29.352  -1.332  1.00 57.00  ? 20  THR   B N   1 
ATOM   992  C CA  . THR   B 1 3   ? -4.253  28.002  -1.870  1.00 53.70  ? 20  THR   B CA  1 
ATOM   993  C C   . THR   B 1 3   ? -3.289  27.821  -3.034  1.00 53.17  ? 20  THR   B C   1 
ATOM   994  O O   . THR   B 1 3   ? -3.218  28.675  -3.924  1.00 54.41  ? 20  THR   B O   1 
ATOM   995  C CB  . THR   B 1 3   ? -5.686  27.704  -2.337  1.00 48.23  ? 20  THR   B CB  1 
ATOM   996  O OG1 . THR   B 1 3   ? -5.985  28.481  -3.503  1.00 57.30  ? 20  THR   B OG1 1 
ATOM   997  C CG2 . THR   B 1 3   ? -6.697  28.018  -1.241  1.00 45.19  ? 20  THR   B CG2 1 
ATOM   998  N N   . VAL   B 1 4   ? -2.554  26.711  -3.023  1.00 51.49  ? 21  VAL   B N   1 
ATOM   999  C CA  . VAL   B 1 4   ? -1.683  26.328  -4.130  1.00 50.80  ? 21  VAL   B CA  1 
ATOM   1000 C C   . VAL   B 1 4   ? -2.507  25.542  -5.140  1.00 50.69  ? 21  VAL   B C   1 
ATOM   1001 O O   . VAL   B 1 4   ? -3.317  24.685  -4.767  1.00 43.81  ? 21  VAL   B O   1 
ATOM   1002 C CB  . VAL   B 1 4   ? -0.478  25.512  -3.622  1.00 50.38  ? 21  VAL   B CB  1 
ATOM   1003 C CG1 . VAL   B 1 4   ? 0.275   24.876  -4.781  1.00 41.75  ? 21  VAL   B CG1 1 
ATOM   1004 C CG2 . VAL   B 1 4   ? 0.452   26.395  -2.802  1.00 50.60  ? 21  VAL   B CG2 1 
ATOM   1005 N N   . THR   B 1 5   ? -2.306  25.830  -6.424  1.00 52.55  ? 22  THR   B N   1 
ATOM   1006 C CA  . THR   B 1 5   ? -3.089  25.235  -7.499  1.00 48.79  ? 22  THR   B CA  1 
ATOM   1007 C C   . THR   B 1 5   ? -2.177  24.457  -8.437  1.00 51.62  ? 22  THR   B C   1 
ATOM   1008 O O   . THR   B 1 5   ? -1.119  24.955  -8.835  1.00 57.02  ? 22  THR   B O   1 
ATOM   1009 C CB  . THR   B 1 5   ? -3.847  26.315  -8.282  1.00 49.95  ? 22  THR   B CB  1 
ATOM   1010 O OG1 . THR   B 1 5   ? -4.894  26.857  -7.467  1.00 55.82  ? 22  THR   B OG1 1 
ATOM   1011 C CG2 . THR   B 1 5   ? -4.449  25.744  -9.558  1.00 49.51  ? 22  THR   B CG2 1 
ATOM   1012 N N   . VAL   B 1 6   ? -2.582  23.241  -8.778  1.00 52.66  ? 23  VAL   B N   1 
ATOM   1013 C CA  . VAL   B 1 6   ? -1.864  22.395  -9.725  1.00 51.25  ? 23  VAL   B CA  1 
ATOM   1014 C C   . VAL   B 1 6   ? -2.731  22.244  -10.980 1.00 50.15  ? 23  VAL   B C   1 
ATOM   1015 O O   . VAL   B 1 6   ? -3.897  21.848  -10.875 1.00 48.43  ? 23  VAL   B O   1 
ATOM   1016 C CB  . VAL   B 1 6   ? -1.495  21.026  -9.125  1.00 49.45  ? 23  VAL   B CB  1 
ATOM   1017 C CG1 . VAL   B 1 6   ? -0.564  21.214  -7.945  1.00 45.06  ? 23  VAL   B CG1 1 
ATOM   1018 C CG2 . VAL   B 1 6   ? -2.731  20.254  -8.675  1.00 52.51  ? 23  VAL   B CG2 1 
ATOM   1019 N N   . PRO   B 1 7   ? -2.224  22.608  -12.160 1.00 52.26  ? 24  PRO   B N   1 
ATOM   1020 C CA  . PRO   B 1 7   ? -3.003  22.382  -13.389 1.00 49.62  ? 24  PRO   B CA  1 
ATOM   1021 C C   . PRO   B 1 7   ? -3.087  20.918  -13.779 1.00 50.35  ? 24  PRO   B C   1 
ATOM   1022 O O   . PRO   B 1 7   ? -3.923  20.566  -14.621 1.00 52.78  ? 24  PRO   B O   1 
ATOM   1023 C CB  . PRO   B 1 7   ? -2.239  23.190  -14.451 1.00 49.12  ? 24  PRO   B CB  1 
ATOM   1024 C CG  . PRO   B 1 7   ? -1.240  24.022  -13.699 1.00 51.82  ? 24  PRO   B CG  1 
ATOM   1025 C CD  . PRO   B 1 7   ? -0.957  23.301  -12.426 1.00 51.00  ? 24  PRO   B CD  1 
ATOM   1026 N N   . LYS   B 1 8   ? -2.252  20.061  -13.192 1.00 50.79  ? 25  LYS   B N   1 
ATOM   1027 C CA  . LYS   B 1 8   ? -2.201  18.645  -13.542 1.00 49.52  ? 25  LYS   B CA  1 
ATOM   1028 C C   . LYS   B 1 8   ? -1.754  17.852  -12.326 1.00 49.28  ? 25  LYS   B C   1 
ATOM   1029 O O   . LYS   B 1 8   ? -0.685  18.121  -11.768 1.00 46.32  ? 25  LYS   B O   1 
ATOM   1030 C CB  . LYS   B 1 8   ? -1.246  18.392  -14.709 1.00 48.25  ? 25  LYS   B CB  1 
ATOM   1031 C CG  . LYS   B 1 8   ? -1.920  18.147  -16.043 1.00 49.07  ? 25  LYS   B CG  1 
ATOM   1032 C CD  . LYS   B 1 8   ? -0.896  18.183  -17.159 1.00 57.39  ? 25  LYS   B CD  1 
ATOM   1033 C CE  . LYS   B 1 8   ? 0.021   16.973  -17.070 1.00 52.13  ? 25  LYS   B CE  1 
ATOM   1034 N NZ  . LYS   B 1 8   ? -0.011  16.136  -18.296 1.00 57.82  ? 25  LYS   B NZ  1 
ATOM   1035 N N   . ASP   B 1 9   ? -2.572  16.889  -11.912 1.00 50.62  ? 26  ASP   B N   1 
ATOM   1036 C CA  . ASP   B 1 9   ? -2.236  16.039  -10.782 1.00 48.71  ? 26  ASP   B CA  1 
ATOM   1037 C C   . ASP   B 1 9   ? -1.438  14.807  -11.192 1.00 45.81  ? 26  ASP   B C   1 
ATOM   1038 O O   . ASP   B 1 9   ? -0.878  14.133  -10.322 1.00 43.10  ? 26  ASP   B O   1 
ATOM   1039 C CB  . ASP   B 1 9   ? -3.514  15.609  -10.052 1.00 49.14  ? 26  ASP   B CB  1 
ATOM   1040 C CG  . ASP   B 1 9   ? -4.379  14.686  -10.889 1.00 65.18  ? 26  ASP   B CG  1 
ATOM   1041 O OD1 . ASP   B 1 9   ? -4.679  15.041  -12.048 1.00 64.61  ? 26  ASP   B OD1 1 
ATOM   1042 O OD2 . ASP   B 1 9   ? -4.752  13.603  -10.393 1.00 74.74  ? 26  ASP   B OD2 1 
ATOM   1043 N N   . LEU   B 1 10  ? -1.364  14.509  -12.490 1.00 47.61  ? 27  LEU   B N   1 
ATOM   1044 C CA  . LEU   B 1 10  ? -0.638  13.352  -12.999 1.00 48.91  ? 27  LEU   B CA  1 
ATOM   1045 C C   . LEU   B 1 10  ? 0.113   13.729  -14.267 1.00 51.72  ? 27  LEU   B C   1 
ATOM   1046 O O   . LEU   B 1 10  ? -0.455  14.361  -15.162 1.00 45.82  ? 27  LEU   B O   1 
ATOM   1047 C CB  . LEU   B 1 10  ? -1.591  12.183  -13.280 1.00 51.46  ? 27  LEU   B CB  1 
ATOM   1048 C CG  . LEU   B 1 10  ? -1.016  11.019  -14.091 1.00 47.99  ? 27  LEU   B CG  1 
ATOM   1049 C CD1 . LEU   B 1 10  ? 0.079   10.310  -13.316 1.00 43.95  ? 27  LEU   B CD1 1 
ATOM   1050 C CD2 . LEU   B 1 10  ? -2.114  10.043  -14.485 1.00 49.56  ? 27  LEU   B CD2 1 
ATOM   1051 N N   . TYR   B 1 11  ? 1.389   13.351  -14.334 1.00 49.39  ? 28  TYR   B N   1 
ATOM   1052 C CA  . TYR   B 1 11  ? 2.210   13.514  -15.527 1.00 47.34  ? 28  TYR   B CA  1 
ATOM   1053 C C   . TYR   B 1 11  ? 2.638   12.148  -16.044 1.00 42.45  ? 28  TYR   B C   1 
ATOM   1054 O O   . TYR   B 1 11  ? 2.995   11.263  -15.260 1.00 46.08  ? 28  TYR   B O   1 
ATOM   1055 C CB  . TYR   B 1 11  ? 3.457   14.366  -15.248 1.00 50.27  ? 28  TYR   B CB  1 
ATOM   1056 C CG  . TYR   B 1 11  ? 3.186   15.837  -15.023 1.00 44.31  ? 28  TYR   B CG  1 
ATOM   1057 C CD1 . TYR   B 1 11  ? 2.543   16.276  -13.875 1.00 45.61  ? 28  TYR   B CD1 1 
ATOM   1058 C CD2 . TYR   B 1 11  ? 3.583   16.787  -15.955 1.00 48.00  ? 28  TYR   B CD2 1 
ATOM   1059 C CE1 . TYR   B 1 11  ? 2.297   17.619  -13.662 1.00 54.58  ? 28  TYR   B CE1 1 
ATOM   1060 C CE2 . TYR   B 1 11  ? 3.342   18.133  -15.751 1.00 49.54  ? 28  TYR   B CE2 1 
ATOM   1061 C CZ  . TYR   B 1 11  ? 2.698   18.543  -14.603 1.00 52.01  ? 28  TYR   B CZ  1 
ATOM   1062 O OH  . TYR   B 1 11  ? 2.453   19.880  -14.391 1.00 51.99  ? 28  TYR   B OH  1 
ATOM   1063 N N   . VAL   B 1 12  ? 2.592   11.975  -17.362 1.00 44.73  ? 29  VAL   B N   1 
ATOM   1064 C CA  . VAL   B 1 12  ? 3.073   10.764  -18.022 1.00 49.43  ? 29  VAL   B CA  1 
ATOM   1065 C C   . VAL   B 1 12  ? 4.184   11.189  -18.973 1.00 51.58  ? 29  VAL   B C   1 
ATOM   1066 O O   . VAL   B 1 12  ? 3.926   11.861  -19.981 1.00 58.92  ? 29  VAL   B O   1 
ATOM   1067 C CB  . VAL   B 1 12  ? 1.955   10.023  -18.766 1.00 47.01  ? 29  VAL   B CB  1 
ATOM   1068 C CG1 . VAL   B 1 12  ? 2.542   8.973   -19.702 1.00 47.68  ? 29  VAL   B CG1 1 
ATOM   1069 C CG2 . VAL   B 1 12  ? 0.997   9.383   -17.775 1.00 46.45  ? 29  VAL   B CG2 1 
ATOM   1070 N N   . VAL   B 1 13  ? 5.421   10.806  -18.653 1.00 48.96  ? 30  VAL   B N   1 
ATOM   1071 C CA  . VAL   B 1 13  ? 6.598   11.249  -19.387 1.00 55.25  ? 30  VAL   B CA  1 
ATOM   1072 C C   . VAL   B 1 13  ? 7.405   10.040  -19.843 1.00 52.66  ? 30  VAL   B C   1 
ATOM   1073 O O   . VAL   B 1 13  ? 7.339   8.957   -19.256 1.00 53.45  ? 30  VAL   B O   1 
ATOM   1074 C CB  . VAL   B 1 13  ? 7.479   12.195  -18.545 1.00 52.20  ? 30  VAL   B CB  1 
ATOM   1075 C CG1 . VAL   B 1 13  ? 6.693   13.434  -18.152 1.00 50.28  ? 30  VAL   B CG1 1 
ATOM   1076 C CG2 . VAL   B 1 13  ? 7.980   11.476  -17.308 1.00 47.93  ? 30  VAL   B CG2 1 
ATOM   1077 N N   . GLU   B 1 14  ? 8.176   10.243  -20.908 1.00 58.03  ? 31  GLU   B N   1 
ATOM   1078 C CA  . GLU   B 1 14  ? 9.012   9.195   -21.472 1.00 57.50  ? 31  GLU   B CA  1 
ATOM   1079 C C   . GLU   B 1 14  ? 10.415  9.236   -20.874 1.00 58.07  ? 31  GLU   B C   1 
ATOM   1080 O O   . GLU   B 1 14  ? 10.900  10.285  -20.441 1.00 55.66  ? 31  GLU   B O   1 
ATOM   1081 C CB  . GLU   B 1 14  ? 9.092   9.330   -22.994 1.00 58.19  ? 31  GLU   B CB  1 
ATOM   1082 C CG  . GLU   B 1 14  ? 7.741   9.385   -23.702 1.00 57.04  ? 31  GLU   B CG  1 
ATOM   1083 C CD  . GLU   B 1 14  ? 6.885   8.156   -23.450 1.00 61.15  ? 31  GLU   B CD  1 
ATOM   1084 O OE1 . GLU   B 1 14  ? 6.179   8.112   -22.420 1.00 60.30  ? 31  GLU   B OE1 1 
ATOM   1085 O OE2 . GLU   B 1 14  ? 6.917   7.229   -24.288 1.00 67.68  ? 31  GLU   B OE2 1 
ATOM   1086 N N   . TYR   B 1 15  ? 11.058  8.070   -20.853 1.00 58.25  ? 32  TYR   B N   1 
ATOM   1087 C CA  . TYR   B 1 15  ? 12.411  7.951   -20.324 1.00 53.27  ? 32  TYR   B CA  1 
ATOM   1088 C C   . TYR   B 1 15  ? 13.385  8.828   -21.103 1.00 48.27  ? 32  TYR   B C   1 
ATOM   1089 O O   . TYR   B 1 15  ? 13.355  8.878   -22.336 1.00 46.45  ? 32  TYR   B O   1 
ATOM   1090 C CB  . TYR   B 1 15  ? 12.859  6.489   -20.370 1.00 47.57  ? 32  TYR   B CB  1 
ATOM   1091 C CG  . TYR   B 1 15  ? 14.315  6.262   -20.030 1.00 45.87  ? 32  TYR   B CG  1 
ATOM   1092 C CD1 . TYR   B 1 15  ? 14.736  6.193   -18.708 1.00 47.16  ? 32  TYR   B CD1 1 
ATOM   1093 C CD2 . TYR   B 1 15  ? 15.266  6.099   -21.030 1.00 45.30  ? 32  TYR   B CD2 1 
ATOM   1094 C CE1 . TYR   B 1 15  ? 16.065  5.980   -18.391 1.00 48.77  ? 32  TYR   B CE1 1 
ATOM   1095 C CE2 . TYR   B 1 15  ? 16.597  5.886   -20.723 1.00 50.26  ? 32  TYR   B CE2 1 
ATOM   1096 C CZ  . TYR   B 1 15  ? 16.990  5.827   -19.403 1.00 49.76  ? 32  TYR   B CZ  1 
ATOM   1097 O OH  . TYR   B 1 15  ? 18.314  5.615   -19.093 1.00 56.26  ? 32  TYR   B OH  1 
ATOM   1098 N N   . GLY   B 1 16  ? 14.256  9.525   -20.372 1.00 43.62  ? 33  GLY   B N   1 
ATOM   1099 C CA  . GLY   B 1 16  ? 15.270  10.364  -20.975 1.00 57.55  ? 33  GLY   B CA  1 
ATOM   1100 C C   . GLY   B 1 16  ? 14.798  11.718  -21.455 1.00 61.29  ? 33  GLY   B C   1 
ATOM   1101 O O   . GLY   B 1 16  ? 15.637  12.558  -21.808 1.00 61.52  ? 33  GLY   B O   1 
ATOM   1102 N N   . SER   B 1 17  ? 13.492  11.964  -21.479 1.00 55.41  ? 34  SER   B N   1 
ATOM   1103 C CA  . SER   B 1 17  ? 12.946  13.225  -21.954 1.00 56.59  ? 34  SER   B CA  1 
ATOM   1104 C C   . SER   B 1 17  ? 13.045  14.294  -20.868 1.00 60.32  ? 34  SER   B C   1 
ATOM   1105 O O   . SER   B 1 17  ? 13.553  14.062  -19.768 1.00 58.48  ? 34  SER   B O   1 
ATOM   1106 C CB  . SER   B 1 17  ? 11.500  13.037  -22.408 1.00 57.52  ? 34  SER   B CB  1 
ATOM   1107 O OG  . SER   B 1 17  ? 10.744  14.217  -22.202 1.00 68.43  ? 34  SER   B OG  1 
ATOM   1108 N N   . ASN   B 1 18  ? 12.566  15.491  -21.191 1.00 59.90  ? 35  ASN   B N   1 
ATOM   1109 C CA  . ASN   B 1 18  ? 12.507  16.601  -20.253 1.00 58.55  ? 35  ASN   B CA  1 
ATOM   1110 C C   . ASN   B 1 18  ? 11.065  16.805  -19.813 1.00 56.45  ? 35  ASN   B C   1 
ATOM   1111 O O   . ASN   B 1 18  ? 10.146  16.782  -20.639 1.00 59.64  ? 35  ASN   B O   1 
ATOM   1112 C CB  . ASN   B 1 18  ? 13.041  17.889  -20.886 1.00 61.55  ? 35  ASN   B CB  1 
ATOM   1113 C CG  . ASN   B 1 18  ? 14.509  18.122  -20.591 1.00 65.52  ? 35  ASN   B CG  1 
ATOM   1114 O OD1 . ASN   B 1 18  ? 15.218  17.219  -20.150 1.00 64.48  ? 35  ASN   B OD1 1 
ATOM   1115 N ND2 . ASN   B 1 18  ? 14.974  19.341  -20.838 1.00 70.76  ? 35  ASN   B ND2 1 
ATOM   1116 N N   . MET   B 1 19  ? 10.868  16.999  -18.511 1.00 52.56  ? 36  MET   B N   1 
ATOM   1117 C CA  . MET   B 1 19  ? 9.540   17.206  -17.955 1.00 55.45  ? 36  MET   B CA  1 
ATOM   1118 C C   . MET   B 1 19  ? 9.536   18.450  -17.078 1.00 56.92  ? 36  MET   B C   1 
ATOM   1119 O O   . MET   B 1 19  ? 10.494  18.710  -16.342 1.00 59.96  ? 36  MET   B O   1 
ATOM   1120 C CB  . MET   B 1 19  ? 9.064   15.974  -17.159 1.00 51.46  ? 36  MET   B CB  1 
ATOM   1121 C CG  . MET   B 1 19  ? 9.373   15.992  -15.669 1.00 53.45  ? 36  MET   B CG  1 
ATOM   1122 S SD  . MET   B 1 19  ? 8.667   14.581  -14.797 1.00 44.22  ? 36  MET   B SD  1 
ATOM   1123 C CE  . MET   B 1 19  ? 9.366   14.803  -13.164 1.00 46.96  ? 36  MET   B CE  1 
ATOM   1124 N N   . THR   B 1 20  ? 8.472   19.240  -17.200 1.00 53.52  ? 37  THR   B N   1 
ATOM   1125 C CA  . THR   B 1 20  ? 8.253   20.415  -16.366 1.00 60.36  ? 37  THR   B CA  1 
ATOM   1126 C C   . THR   B 1 20  ? 6.925   20.262  -15.638 1.00 56.22  ? 37  THR   B C   1 
ATOM   1127 O O   . THR   B 1 20  ? 5.870   20.192  -16.278 1.00 48.19  ? 37  THR   B O   1 
ATOM   1128 C CB  . THR   B 1 20  ? 8.265   21.697  -17.202 1.00 59.44  ? 37  THR   B CB  1 
ATOM   1129 O OG1 . THR   B 1 20  ? 9.494   21.778  -17.937 1.00 61.08  ? 37  THR   B OG1 1 
ATOM   1130 C CG2 . THR   B 1 20  ? 8.138   22.918  -16.305 1.00 53.14  ? 37  THR   B CG2 1 
ATOM   1131 N N   . ILE   B 1 21  ? 6.975   20.214  -14.308 1.00 54.59  ? 38  ILE   B N   1 
ATOM   1132 C CA  . ILE   B 1 21  ? 5.781   20.086  -13.478 1.00 50.40  ? 38  ILE   B CA  1 
ATOM   1133 C C   . ILE   B 1 21  ? 5.464   21.445  -12.874 1.00 56.69  ? 38  ILE   B C   1 
ATOM   1134 O O   . ILE   B 1 21  ? 6.370   22.193  -12.481 1.00 56.78  ? 38  ILE   B O   1 
ATOM   1135 C CB  . ILE   B 1 21  ? 5.961   19.015  -12.385 1.00 56.70  ? 38  ILE   B CB  1 
ATOM   1136 C CG1 . ILE   B 1 21  ? 7.299   19.193  -11.664 1.00 59.60  ? 38  ILE   B CG1 1 
ATOM   1137 C CG2 . ILE   B 1 21  ? 5.856   17.619  -12.987 1.00 57.50  ? 38  ILE   B CG2 1 
ATOM   1138 C CD1 . ILE   B 1 21  ? 7.684   18.013  -10.794 1.00 52.76  ? 38  ILE   B CD1 1 
ATOM   1139 N N   . GLU   B 1 22  ? 4.175   21.768  -12.799 1.00 64.71  ? 39  GLU   B N   1 
ATOM   1140 C CA  . GLU   B 1 22  ? 3.710   23.110  -12.475 1.00 61.94  ? 39  GLU   B CA  1 
ATOM   1141 C C   . GLU   B 1 22  ? 2.824   23.075  -11.238 1.00 61.51  ? 39  GLU   B C   1 
ATOM   1142 O O   . GLU   B 1 22  ? 1.864   22.300  -11.177 1.00 68.64  ? 39  GLU   B O   1 
ATOM   1143 C CB  . GLU   B 1 22  ? 2.945   23.720  -13.655 1.00 66.16  ? 39  GLU   B CB  1 
ATOM   1144 C CG  . GLU   B 1 22  ? 3.777   23.894  -14.915 1.00 69.60  ? 39  GLU   B CG  1 
ATOM   1145 C CD  . GLU   B 1 22  ? 3.482   25.200  -15.628 1.00 80.97  ? 39  GLU   B CD  1 
ATOM   1146 O OE1 . GLU   B 1 22  ? 2.695   26.008  -15.090 1.00 74.38  ? 39  GLU   B OE1 1 
ATOM   1147 O OE2 . GLU   B 1 22  ? 4.034   25.416  -16.728 1.00 83.59  ? 39  GLU   B OE2 1 
ATOM   1148 N N   . CYS   B 1 23  ? 3.156   23.908  -10.255 1.00 53.45  ? 40  CYS   B N   1 
ATOM   1149 C CA  . CYS   B 1 23  ? 2.232   24.287  -9.197  1.00 57.74  ? 40  CYS   B CA  1 
ATOM   1150 C C   . CYS   B 1 23  ? 2.128   25.803  -9.145  1.00 58.16  ? 40  CYS   B C   1 
ATOM   1151 O O   . CYS   B 1 23  ? 3.102   26.519  -9.394  1.00 59.02  ? 40  CYS   B O   1 
ATOM   1152 C CB  . CYS   B 1 23  ? 2.674   23.744  -7.828  1.00 54.32  ? 40  CYS   B CB  1 
ATOM   1153 S SG  . CYS   B 1 23  ? 4.312   24.289  -7.307  1.00 83.53  ? 40  CYS   B SG  1 
ATOM   1154 N N   . LYS   B 1 24  ? 0.939   26.289  -8.816  1.00 55.86  ? 41  LYS   B N   1 
ATOM   1155 C CA  . LYS   B 1 24  ? 0.626   27.700  -8.942  1.00 52.57  ? 41  LYS   B CA  1 
ATOM   1156 C C   . LYS   B 1 24  ? 0.162   28.253  -7.606  1.00 53.39  ? 41  LYS   B C   1 
ATOM   1157 O O   . LYS   B 1 24  ? -0.587  27.596  -6.870  1.00 54.68  ? 41  LYS   B O   1 
ATOM   1158 C CB  . LYS   B 1 24  ? -0.442  27.928  -10.010 1.00 47.84  ? 41  LYS   B CB  1 
ATOM   1159 C CG  . LYS   B 1 24  ? 0.112   27.982  -11.430 1.00 51.80  ? 41  LYS   B CG  1 
ATOM   1160 C CD  . LYS   B 1 24  ? -0.997  28.149  -12.466 1.00 57.86  ? 41  LYS   B CD  1 
ATOM   1161 C CE  . LYS   B 1 24  ? -0.606  27.542  -13.813 1.00 56.54  ? 41  LYS   B CE  1 
ATOM   1162 N NZ  . LYS   B 1 24  ? -0.355  28.574  -14.853 1.00 55.09  ? 41  LYS   B NZ  1 
ATOM   1163 N N   . PHE   B 1 25  ? 0.605   29.471  -7.315  1.00 53.32  ? 42  PHE   B N   1 
ATOM   1164 C CA  . PHE   B 1 25  ? 0.237   30.199  -6.114  1.00 57.25  ? 42  PHE   B CA  1 
ATOM   1165 C C   . PHE   B 1 25  ? -0.192  31.605  -6.460  1.00 60.25  ? 42  PHE   B C   1 
ATOM   1166 O O   . PHE   B 1 25  ? 0.302   32.192  -7.434  1.00 61.10  ? 42  PHE   B O   1 
ATOM   1167 C CB  . PHE   B 1 25  ? 1.393   30.250  -5.096  1.00 60.34  ? 42  PHE   B CB  1 
ATOM   1168 C CG  . PHE   B 1 25  ? 2.637   30.931  -5.588  1.00 59.11  ? 42  PHE   B CG  1 
ATOM   1169 C CD1 . PHE   B 1 25  ? 3.328   30.439  -6.676  1.00 56.14  ? 42  PHE   B CD1 1 
ATOM   1170 C CD2 . PHE   B 1 25  ? 3.143   32.040  -4.924  1.00 59.33  ? 42  PHE   B CD2 1 
ATOM   1171 C CE1 . PHE   B 1 25  ? 4.483   31.045  -7.123  1.00 60.64  ? 42  PHE   B CE1 1 
ATOM   1172 C CE2 . PHE   B 1 25  ? 4.304   32.659  -5.369  1.00 59.51  ? 42  PHE   B CE2 1 
ATOM   1173 C CZ  . PHE   B 1 25  ? 4.975   32.159  -6.471  1.00 63.17  ? 42  PHE   B CZ  1 
ATOM   1174 N N   . PRO   B 1 26  ? -1.118  32.182  -5.702  1.00 65.86  ? 43  PRO   B N   1 
ATOM   1175 C CA  . PRO   B 1 26  ? -1.625  33.514  -6.020  1.00 60.33  ? 43  PRO   B CA  1 
ATOM   1176 C C   . PRO   B 1 26  ? -0.696  34.652  -5.589  1.00 66.76  ? 43  PRO   B C   1 
ATOM   1177 O O   . PRO   B 1 26  ? -0.326  34.760  -4.415  1.00 66.18  ? 43  PRO   B O   1 
ATOM   1178 C CB  . PRO   B 1 26  ? -2.962  33.546  -5.285  1.00 55.82  ? 43  PRO   B CB  1 
ATOM   1179 C CG  . PRO   B 1 26  ? -2.792  32.536  -4.109  1.00 61.74  ? 43  PRO   B CG  1 
ATOM   1180 C CD  . PRO   B 1 26  ? -1.467  31.822  -4.309  1.00 63.80  ? 43  PRO   B CD  1 
ATOM   1181 N N   . VAL   B 1 27  ? -0.314  35.492  -6.554  1.00 72.30  ? 44  VAL   B N   1 
ATOM   1182 C CA  . VAL   B 1 27  ? 0.441   36.714  -6.299  1.00 76.86  ? 44  VAL   B CA  1 
ATOM   1183 C C   . VAL   B 1 27  ? -0.413  37.890  -6.748  1.00 84.49  ? 44  VAL   B C   1 
ATOM   1184 O O   . VAL   B 1 27  ? -0.854  37.942  -7.904  1.00 85.03  ? 44  VAL   B O   1 
ATOM   1185 C CB  . VAL   B 1 27  ? 1.816   36.711  -7.006  1.00 77.79  ? 44  VAL   B CB  1 
ATOM   1186 C CG1 . VAL   B 1 27  ? 1.713   36.396  -8.499  1.00 74.30  ? 44  VAL   B CG1 1 
ATOM   1187 C CG2 . VAL   B 1 27  ? 2.535   38.058  -6.806  1.00 88.63  ? 44  VAL   B CG2 1 
ATOM   1188 N N   . GLU   B 1 28  ? -0.653  38.827  -5.835  1.00 83.81  ? 45  GLU   B N   1 
ATOM   1189 C CA  . GLU   B 1 28  ? -1.539  39.945  -6.124  1.00 93.74  ? 45  GLU   B CA  1 
ATOM   1190 C C   . GLU   B 1 28  ? -0.772  41.138  -6.682  1.00 100.44 ? 45  GLU   B C   1 
ATOM   1191 O O   . GLU   B 1 28  ? -1.205  41.765  -7.654  1.00 97.94  ? 45  GLU   B O   1 
ATOM   1192 C CB  . GLU   B 1 28  ? -2.331  40.333  -4.870  1.00 99.89  ? 45  GLU   B CB  1 
ATOM   1193 C CG  . GLU   B 1 28  ? -3.782  39.852  -4.910  1.00 105.19 ? 45  GLU   B CG  1 
ATOM   1194 C CD  . GLU   B 1 28  ? -4.370  39.584  -3.536  1.00 108.56 ? 45  GLU   B CD  1 
ATOM   1195 O OE1 . GLU   B 1 28  ? -3.860  40.149  -2.546  1.00 108.20 ? 45  GLU   B OE1 1 
ATOM   1196 O OE2 . GLU   B 1 28  ? -5.347  38.809  -3.448  1.00 103.40 ? 45  GLU   B OE2 1 
ATOM   1197 N N   . LYS   B 1 29  ? 0.373   41.452  -6.085  1.00 106.75 ? 46  LYS   B N   1 
ATOM   1198 C CA  . LYS   B 1 29  ? 1.146   42.611  -6.506  1.00 105.93 ? 46  LYS   B CA  1 
ATOM   1199 C C   . LYS   B 1 29  ? 2.519   42.207  -7.027  1.00 104.18 ? 46  LYS   B C   1 
ATOM   1200 O O   . LYS   B 1 29  ? 2.713   42.057  -8.238  1.00 104.39 ? 46  LYS   B O   1 
ATOM   1201 C CB  . LYS   B 1 29  ? 1.290   43.600  -5.349  1.00 106.30 ? 46  LYS   B CB  1 
ATOM   1202 N N   . GLN   B 1 30  ? 3.474   42.034  -6.119  1.00 105.82 ? 47  GLN   B N   1 
ATOM   1203 C CA  . GLN   B 1 30  ? 4.866   41.754  -6.485  1.00 104.69 ? 47  GLN   B CA  1 
ATOM   1204 C C   . GLN   B 1 30  ? 5.327   40.572  -5.604  1.00 105.83 ? 47  GLN   B C   1 
ATOM   1205 O O   . GLN   B 1 30  ? 4.535   39.901  -4.930  1.00 110.51 ? 47  GLN   B O   1 
ATOM   1206 C CB  . GLN   B 1 30  ? 5.740   42.967  -6.278  1.00 98.97  ? 47  GLN   B CB  1 
ATOM   1207 N N   . LEU   B 1 31  ? 6.639   40.347  -5.593  1.00 90.34  ? 48  LEU   B N   1 
ATOM   1208 C CA  . LEU   B 1 31  ? 7.290   39.323  -4.811  1.00 77.92  ? 48  LEU   B CA  1 
ATOM   1209 C C   . LEU   B 1 31  ? 7.870   39.881  -3.528  1.00 74.17  ? 48  LEU   B C   1 
ATOM   1210 O O   . LEU   B 1 31  ? 8.745   40.752  -3.584  1.00 83.11  ? 48  LEU   B O   1 
ATOM   1211 C CB  . LEU   B 1 31  ? 8.413   38.632  -5.588  1.00 80.16  ? 48  LEU   B CB  1 
ATOM   1212 C CG  . LEU   B 1 31  ? 8.328   37.250  -6.233  1.00 82.23  ? 48  LEU   B CG  1 
ATOM   1213 C CD1 . LEU   B 1 31  ? 8.093   36.183  -5.143  1.00 66.34  ? 48  LEU   B CD1 1 
ATOM   1214 C CD2 . LEU   B 1 31  ? 7.325   37.186  -7.391  1.00 88.82  ? 48  LEU   B CD2 1 
ATOM   1215 N N   . ASP   B 1 32  ? 7.406   39.391  -2.381  1.00 71.11  ? 49  ASP   B N   1 
ATOM   1216 C CA  . ASP   B 1 32  ? 8.197   39.497  -1.161  1.00 71.09  ? 49  ASP   B CA  1 
ATOM   1217 C C   . ASP   B 1 32  ? 9.219   38.369  -1.248  1.00 71.31  ? 49  ASP   B C   1 
ATOM   1218 O O   . ASP   B 1 32  ? 9.081   37.310  -0.632  1.00 71.41  ? 49  ASP   B O   1 
ATOM   1219 C CB  . ASP   B 1 32  ? 7.326   39.391  0.084   1.00 75.28  ? 49  ASP   B CB  1 
ATOM   1220 C CG  . ASP   B 1 32  ? 7.908   40.144  1.266   1.00 73.37  ? 49  ASP   B CG  1 
ATOM   1221 O OD1 . ASP   B 1 32  ? 9.146   40.118  1.439   1.00 69.89  ? 49  ASP   B OD1 1 
ATOM   1222 O OD2 . ASP   B 1 32  ? 7.134   40.761  2.024   1.00 81.45  ? 49  ASP   B OD2 1 
ATOM   1223 N N   . LEU   B 1 33  ? 10.262  38.601  -2.055  1.00 69.16  ? 50  LEU   B N   1 
ATOM   1224 C CA  . LEU   B 1 33  ? 11.282  37.579  -2.259  1.00 63.82  ? 50  LEU   B CA  1 
ATOM   1225 C C   . LEU   B 1 33  ? 11.960  37.180  -0.958  1.00 65.28  ? 50  LEU   B C   1 
ATOM   1226 O O   . LEU   B 1 33  ? 12.511  36.077  -0.868  1.00 75.35  ? 50  LEU   B O   1 
ATOM   1227 C CB  . LEU   B 1 33  ? 12.324  38.071  -3.263  1.00 62.74  ? 50  LEU   B CB  1 
ATOM   1228 C CG  . LEU   B 1 33  ? 12.201  37.503  -4.678  1.00 62.98  ? 50  LEU   B CG  1 
ATOM   1229 C CD1 . LEU   B 1 33  ? 13.305  38.040  -5.575  1.00 63.78  ? 50  LEU   B CD1 1 
ATOM   1230 C CD2 . LEU   B 1 33  ? 12.210  35.982  -4.657  1.00 67.85  ? 50  LEU   B CD2 1 
ATOM   1231 N N   . ALA   B 1 34  ? 11.934  38.053  0.048   1.00 65.28  ? 51  ALA   B N   1 
ATOM   1232 C CA  . ALA   B 1 34  ? 12.386  37.695  1.382   1.00 69.60  ? 51  ALA   B CA  1 
ATOM   1233 C C   . ALA   B 1 34  ? 11.373  36.839  2.127   1.00 68.21  ? 51  ALA   B C   1 
ATOM   1234 O O   . ALA   B 1 34  ? 11.685  36.344  3.216   1.00 71.87  ? 51  ALA   B O   1 
ATOM   1235 C CB  . ALA   B 1 34  ? 12.691  38.958  2.194   1.00 70.60  ? 51  ALA   B CB  1 
ATOM   1236 N N   . ALA   B 1 35  ? 10.174  36.651  1.569   1.00 66.86  ? 52  ALA   B N   1 
ATOM   1237 C CA  . ALA   B 1 35  ? 9.146   35.832  2.190   1.00 66.46  ? 52  ALA   B CA  1 
ATOM   1238 C C   . ALA   B 1 35  ? 8.703   34.641  1.352   1.00 64.57  ? 52  ALA   B C   1 
ATOM   1239 O O   . ALA   B 1 35  ? 7.925   33.822  1.852   1.00 63.56  ? 52  ALA   B O   1 
ATOM   1240 C CB  . ALA   B 1 35  ? 7.912   36.685  2.525   1.00 66.79  ? 52  ALA   B CB  1 
ATOM   1241 N N   . LEU   B 1 36  ? 9.147   34.523  0.102   1.00 63.12  ? 53  LEU   B N   1 
ATOM   1242 C CA  . LEU   B 1 36  ? 8.799   33.360  -0.704  1.00 63.70  ? 53  LEU   B CA  1 
ATOM   1243 C C   . LEU   B 1 36  ? 9.655   32.172  -0.288  1.00 60.17  ? 53  LEU   B C   1 
ATOM   1244 O O   . LEU   B 1 36  ? 10.886  32.265  -0.251  1.00 61.13  ? 53  LEU   B O   1 
ATOM   1245 C CB  . LEU   B 1 36  ? 8.994   33.634  -2.196  1.00 65.10  ? 53  LEU   B CB  1 
ATOM   1246 C CG  . LEU   B 1 36  ? 8.672   32.421  -3.083  1.00 56.64  ? 53  LEU   B CG  1 
ATOM   1247 C CD1 . LEU   B 1 36  ? 7.314   31.804  -2.719  1.00 62.86  ? 53  LEU   B CD1 1 
ATOM   1248 C CD2 . LEU   B 1 36  ? 8.758   32.737  -4.571  1.00 52.97  ? 53  LEU   B CD2 1 
ATOM   1249 N N   . ILE   B 1 37  ? 9.002   31.057  0.023   1.00 60.65  ? 54  ILE   B N   1 
ATOM   1250 C CA  . ILE   B 1 37  ? 9.675   29.800  0.327   1.00 57.73  ? 54  ILE   B CA  1 
ATOM   1251 C C   . ILE   B 1 37  ? 9.032   28.722  -0.532  1.00 55.50  ? 54  ILE   B C   1 
ATOM   1252 O O   . ILE   B 1 37  ? 7.835   28.446  -0.389  1.00 56.40  ? 54  ILE   B O   1 
ATOM   1253 C CB  . ILE   B 1 37  ? 9.589   29.433  1.817   1.00 56.48  ? 54  ILE   B CB  1 
ATOM   1254 C CG1 . ILE   B 1 37  ? 10.305  30.478  2.675   1.00 57.79  ? 54  ILE   B CG1 1 
ATOM   1255 C CG2 . ILE   B 1 37  ? 10.191  28.062  2.058   1.00 55.25  ? 54  ILE   B CG2 1 
ATOM   1256 C CD1 . ILE   B 1 37  ? 9.371   31.436  3.378   1.00 56.08  ? 54  ILE   B CD1 1 
ATOM   1257 N N   . VAL   B 1 38  ? 9.817   28.116  -1.420  1.00 65.94  ? 55  VAL   B N   1 
ATOM   1258 C CA  . VAL   B 1 38  ? 9.340   27.068  -2.316  1.00 61.66  ? 55  VAL   B CA  1 
ATOM   1259 C C   . VAL   B 1 38  ? 10.117  25.796  -2.016  1.00 57.83  ? 55  VAL   B C   1 
ATOM   1260 O O   . VAL   B 1 38  ? 11.353  25.789  -2.070  1.00 61.27  ? 55  VAL   B O   1 
ATOM   1261 C CB  . VAL   B 1 38  ? 9.488   27.459  -3.795  1.00 65.18  ? 55  VAL   B CB  1 
ATOM   1262 C CG1 . VAL   B 1 38  ? 8.912   26.369  -4.689  1.00 59.51  ? 55  VAL   B CG1 1 
ATOM   1263 C CG2 . VAL   B 1 38  ? 8.806   28.787  -4.067  1.00 62.55  ? 55  VAL   B CG2 1 
ATOM   1264 N N   . TYR   B 1 39  ? 9.393   24.724  -1.706  1.00 52.42  ? 56  TYR   B N   1 
ATOM   1265 C CA  . TYR   B 1 39  ? 9.976   23.411  -1.462  1.00 55.31  ? 56  TYR   B CA  1 
ATOM   1266 C C   . TYR   B 1 39  ? 9.432   22.437  -2.496  1.00 50.02  ? 56  TYR   B C   1 
ATOM   1267 O O   . TYR   B 1 39  ? 8.219   22.209  -2.560  1.00 51.91  ? 56  TYR   B O   1 
ATOM   1268 C CB  . TYR   B 1 39  ? 9.652   22.910  -0.051  1.00 55.69  ? 56  TYR   B CB  1 
ATOM   1269 C CG  . TYR   B 1 39  ? 10.556  23.428  1.049   1.00 55.56  ? 56  TYR   B CG  1 
ATOM   1270 C CD1 . TYR   B 1 39  ? 11.295  24.593  0.887   1.00 54.97  ? 56  TYR   B CD1 1 
ATOM   1271 C CD2 . TYR   B 1 39  ? 10.662  22.749  2.256   1.00 50.04  ? 56  TYR   B CD2 1 
ATOM   1272 C CE1 . TYR   B 1 39  ? 12.116  25.064  1.896   1.00 51.17  ? 56  TYR   B CE1 1 
ATOM   1273 C CE2 . TYR   B 1 39  ? 11.480  23.213  3.269   1.00 47.34  ? 56  TYR   B CE2 1 
ATOM   1274 C CZ  . TYR   B 1 39  ? 12.203  24.369  3.084   1.00 41.62  ? 56  TYR   B CZ  1 
ATOM   1275 O OH  . TYR   B 1 39  ? 13.018  24.831  4.092   1.00 52.46  ? 56  TYR   B OH  1 
ATOM   1276 N N   . TRP   B 1 40  ? 10.324  21.870  -3.302  1.00 49.86  ? 57  TRP   B N   1 
ATOM   1277 C CA  . TRP   B 1 40  ? 9.985   20.807  -4.239  1.00 51.29  ? 57  TRP   B CA  1 
ATOM   1278 C C   . TRP   B 1 40  ? 10.536  19.511  -3.663  1.00 50.33  ? 57  TRP   B C   1 
ATOM   1279 O O   . TRP   B 1 40  ? 11.732  19.424  -3.362  1.00 57.88  ? 57  TRP   B O   1 
ATOM   1280 C CB  . TRP   B 1 40  ? 10.559  21.079  -5.630  1.00 49.33  ? 57  TRP   B CB  1 
ATOM   1281 C CG  . TRP   B 1 40  ? 9.675   21.921  -6.510  1.00 47.33  ? 57  TRP   B CG  1 
ATOM   1282 C CD1 . TRP   B 1 40  ? 9.849   23.238  -6.824  1.00 56.45  ? 57  TRP   B CD1 1 
ATOM   1283 C CD2 . TRP   B 1 40  ? 8.484   21.502  -7.192  1.00 55.94  ? 57  TRP   B CD2 1 
ATOM   1284 N NE1 . TRP   B 1 40  ? 8.844   23.664  -7.658  1.00 61.12  ? 57  TRP   B NE1 1 
ATOM   1285 C CE2 . TRP   B 1 40  ? 7.993   22.618  -7.898  1.00 57.77  ? 57  TRP   B CE2 1 
ATOM   1286 C CE3 . TRP   B 1 40  ? 7.786   20.293  -7.273  1.00 53.58  ? 57  TRP   B CE3 1 
ATOM   1287 C CZ2 . TRP   B 1 40  ? 6.840   22.560  -8.677  1.00 56.87  ? 57  TRP   B CZ2 1 
ATOM   1288 C CZ3 . TRP   B 1 40  ? 6.639   20.238  -8.047  1.00 49.36  ? 57  TRP   B CZ3 1 
ATOM   1289 C CH2 . TRP   B 1 40  ? 6.177   21.365  -8.737  1.00 50.49  ? 57  TRP   B CH2 1 
ATOM   1290 N N   . GLU   B 1 41  ? 9.670   18.514  -3.502  1.00 43.71  ? 58  GLU   B N   1 
ATOM   1291 C CA  . GLU   B 1 41  ? 10.064  17.258  -2.883  1.00 54.94  ? 58  GLU   B CA  1 
ATOM   1292 C C   . GLU   B 1 41  ? 9.463   16.080  -3.634  1.00 54.42  ? 58  GLU   B C   1 
ATOM   1293 O O   . GLU   B 1 41  ? 8.487   16.219  -4.375  1.00 50.51  ? 58  GLU   B O   1 
ATOM   1294 C CB  . GLU   B 1 41  ? 9.621   17.207  -1.416  1.00 54.12  ? 58  GLU   B CB  1 
ATOM   1295 C CG  . GLU   B 1 41  ? 10.681  16.717  -0.457  1.00 63.16  ? 58  GLU   B CG  1 
ATOM   1296 C CD  . GLU   B 1 41  ? 10.467  17.231  0.950   1.00 62.80  ? 58  GLU   B CD  1 
ATOM   1297 O OE1 . GLU   B 1 41  ? 9.604   16.671  1.659   1.00 63.39  ? 58  GLU   B OE1 1 
ATOM   1298 O OE2 . GLU   B 1 41  ? 11.157  18.194  1.346   1.00 55.33  ? 58  GLU   B OE2 1 
ATOM   1299 N N   . MET   B 1 42  ? 10.069  14.911  -3.429  1.00 62.55  ? 59  MET   B N   1 
ATOM   1300 C CA  . MET   B 1 42  ? 9.506   13.642  -3.877  1.00 57.85  ? 59  MET   B CA  1 
ATOM   1301 C C   . MET   B 1 42  ? 9.800   12.592  -2.819  1.00 65.56  ? 59  MET   B C   1 
ATOM   1302 O O   . MET   B 1 42  ? 10.967  12.270  -2.579  1.00 65.72  ? 59  MET   B O   1 
ATOM   1303 C CB  . MET   B 1 42  ? 10.100  13.213  -5.224  1.00 53.82  ? 59  MET   B CB  1 
ATOM   1304 C CG  . MET   B 1 42  ? 9.413   12.016  -5.875  1.00 63.47  ? 59  MET   B CG  1 
ATOM   1305 S SD  . MET   B 1 42  ? 10.003  10.392  -5.332  1.00 69.10  ? 59  MET   B SD  1 
ATOM   1306 C CE  . MET   B 1 42  ? 11.775  10.642  -5.249  1.00 67.59  ? 59  MET   B CE  1 
ATOM   1307 N N   . GLU   B 1 43  ? 8.745   12.046  -2.215  1.00 79.54  ? 60  GLU   B N   1 
ATOM   1308 C CA  . GLU   B 1 43  ? 8.830   10.961  -1.235  1.00 84.85  ? 60  GLU   B CA  1 
ATOM   1309 C C   . GLU   B 1 43  ? 9.912   11.232  -0.183  1.00 85.81  ? 60  GLU   B C   1 
ATOM   1310 O O   . GLU   B 1 43  ? 10.919  10.530  -0.079  1.00 86.97  ? 60  GLU   B O   1 
ATOM   1311 C CB  . GLU   B 1 43  ? 9.056   9.621   -1.943  1.00 86.33  ? 60  GLU   B CB  1 
ATOM   1312 C CG  . GLU   B 1 43  ? 7.861   9.170   -2.774  1.00 84.22  ? 60  GLU   B CG  1 
ATOM   1313 C CD  . GLU   B 1 43  ? 8.125   7.885   -3.534  1.00 89.82  ? 60  GLU   B CD  1 
ATOM   1314 O OE1 . GLU   B 1 43  ? 9.290   7.436   -3.559  1.00 89.65  ? 60  GLU   B OE1 1 
ATOM   1315 O OE2 . GLU   B 1 43  ? 7.166   7.327   -4.109  1.00 79.52  ? 60  GLU   B OE2 1 
ATOM   1316 N N   . ASP   B 1 44  ? 9.652   12.273  0.611   1.00 76.58  ? 61  ASP   B N   1 
ATOM   1317 C CA  . ASP   B 1 44  ? 10.538  12.701  1.699   1.00 74.60  ? 61  ASP   B CA  1 
ATOM   1318 C C   . ASP   B 1 44  ? 11.994  12.820  1.251   1.00 73.12  ? 61  ASP   B C   1 
ATOM   1319 O O   . ASP   B 1 44  ? 12.925  12.508  1.998   1.00 75.53  ? 61  ASP   B O   1 
ATOM   1320 C CB  . ASP   B 1 44  ? 10.420  11.753  2.894   1.00 78.07  ? 61  ASP   B CB  1 
ATOM   1321 C CG  . ASP   B 1 44  ? 8.998   11.626  3.401   1.00 75.31  ? 61  ASP   B CG  1 
ATOM   1322 O OD1 . ASP   B 1 44  ? 8.257   12.631  3.356   1.00 75.79  ? 61  ASP   B OD1 1 
ATOM   1323 O OD2 . ASP   B 1 44  ? 8.619   10.520  3.841   1.00 69.90  ? 61  ASP   B OD2 1 
ATOM   1324 N N   . LYS   B 1 45  ? 12.198  13.285  0.020   1.00 72.18  ? 62  LYS   B N   1 
ATOM   1325 C CA  . LYS   B 1 45  ? 13.532  13.538  -0.517  1.00 69.69  ? 62  LYS   B CA  1 
ATOM   1326 C C   . LYS   B 1 45  ? 13.516  14.902  -1.192  1.00 65.34  ? 62  LYS   B C   1 
ATOM   1327 O O   . LYS   B 1 45  ? 12.869  15.075  -2.231  1.00 65.12  ? 62  LYS   B O   1 
ATOM   1328 C CB  . LYS   B 1 45  ? 13.959  12.444  -1.496  1.00 69.40  ? 62  LYS   B CB  1 
ATOM   1329 N N   . ASN   B 1 46  ? 14.222  15.866  -0.603  1.00 60.85  ? 63  ASN   B N   1 
ATOM   1330 C CA  . ASN   B 1 46  ? 14.191  17.230  -1.110  1.00 60.01  ? 63  ASN   B CA  1 
ATOM   1331 C C   . ASN   B 1 46  ? 14.790  17.301  -2.509  1.00 62.00  ? 63  ASN   B C   1 
ATOM   1332 O O   . ASN   B 1 46  ? 15.804  16.663  -2.805  1.00 66.54  ? 63  ASN   B O   1 
ATOM   1333 C CB  . ASN   B 1 46  ? 14.947  18.163  -0.163  1.00 66.86  ? 63  ASN   B CB  1 
ATOM   1334 C CG  . ASN   B 1 46  ? 14.438  19.592  -0.222  1.00 66.25  ? 63  ASN   B CG  1 
ATOM   1335 O OD1 . ASN   B 1 46  ? 14.947  20.413  -0.986  1.00 58.83  ? 63  ASN   B OD1 1 
ATOM   1336 N ND2 . ASN   B 1 46  ? 13.427  19.894  0.585   1.00 61.16  ? 63  ASN   B ND2 1 
ATOM   1337 N N   . ILE   B 1 47  ? 14.152  18.088  -3.369  1.00 62.32  ? 64  ILE   B N   1 
ATOM   1338 C CA  . ILE   B 1 47  ? 14.608  18.316  -4.733  1.00 61.66  ? 64  ILE   B CA  1 
ATOM   1339 C C   . ILE   B 1 47  ? 15.140  19.733  -4.911  1.00 62.99  ? 64  ILE   B C   1 
ATOM   1340 O O   . ILE   B 1 47  ? 16.213  19.936  -5.478  1.00 64.28  ? 64  ILE   B O   1 
ATOM   1341 C CB  . ILE   B 1 47  ? 13.480  18.020  -5.746  1.00 50.91  ? 64  ILE   B CB  1 
ATOM   1342 C CG1 . ILE   B 1 47  ? 12.758  16.722  -5.376  1.00 56.39  ? 64  ILE   B CG1 1 
ATOM   1343 C CG2 . ILE   B 1 47  ? 14.037  17.960  -7.160  1.00 53.31  ? 64  ILE   B CG2 1 
ATOM   1344 C CD1 . ILE   B 1 47  ? 11.999  16.096  -6.520  1.00 54.84  ? 64  ILE   B CD1 1 
ATOM   1345 N N   . ILE   B 1 48  ? 14.407  20.725  -4.410  1.00 61.36  ? 65  ILE   B N   1 
ATOM   1346 C CA  . ILE   B 1 48  ? 14.761  22.130  -4.586  1.00 56.50  ? 65  ILE   B CA  1 
ATOM   1347 C C   . ILE   B 1 48  ? 14.234  22.909  -3.390  1.00 57.77  ? 65  ILE   B C   1 
ATOM   1348 O O   . ILE   B 1 48  ? 13.103  22.697  -2.942  1.00 60.18  ? 65  ILE   B O   1 
ATOM   1349 C CB  . ILE   B 1 48  ? 14.189  22.689  -5.911  1.00 54.77  ? 65  ILE   B CB  1 
ATOM   1350 C CG1 . ILE   B 1 48  ? 15.120  22.376  -7.086  1.00 56.74  ? 65  ILE   B CG1 1 
ATOM   1351 C CG2 . ILE   B 1 48  ? 13.919  24.188  -5.809  1.00 58.91  ? 65  ILE   B CG2 1 
ATOM   1352 C CD1 . ILE   B 1 48  ? 16.243  23.370  -7.267  1.00 63.12  ? 65  ILE   B CD1 1 
ATOM   1353 N N   . GLN   B 1 49  ? 15.064  23.812  -2.871  1.00 61.20  ? 66  GLN   B N   1 
ATOM   1354 C CA  . GLN   B 1 49  ? 14.687  24.702  -1.777  1.00 64.22  ? 66  GLN   B CA  1 
ATOM   1355 C C   . GLN   B 1 49  ? 14.936  26.132  -2.235  1.00 63.11  ? 66  GLN   B C   1 
ATOM   1356 O O   . GLN   B 1 49  ? 16.090  26.543  -2.386  1.00 62.58  ? 66  GLN   B O   1 
ATOM   1357 C CB  . GLN   B 1 49  ? 15.480  24.390  -0.508  1.00 64.24  ? 66  GLN   B CB  1 
ATOM   1358 C CG  . GLN   B 1 49  ? 14.812  23.390  0.417   1.00 57.10  ? 66  GLN   B CG  1 
ATOM   1359 C CD  . GLN   B 1 49  ? 15.339  23.470  1.836   1.00 57.51  ? 66  GLN   B CD  1 
ATOM   1360 O OE1 . GLN   B 1 49  ? 16.233  24.263  2.135   1.00 64.26  ? 66  GLN   B OE1 1 
ATOM   1361 N NE2 . GLN   B 1 49  ? 14.790  22.645  2.720   1.00 50.20  ? 66  GLN   B NE2 1 
ATOM   1362 N N   . PHE   B 1 50  ? 13.864  26.891  -2.438  1.00 65.93  ? 67  PHE   B N   1 
ATOM   1363 C CA  . PHE   B 1 50  ? 13.949  28.284  -2.873  1.00 69.43  ? 67  PHE   B CA  1 
ATOM   1364 C C   . PHE   B 1 50  ? 13.636  29.168  -1.671  1.00 64.33  ? 67  PHE   B C   1 
ATOM   1365 O O   . PHE   B 1 50  ? 12.468  29.369  -1.326  1.00 59.90  ? 67  PHE   B O   1 
ATOM   1366 C CB  . PHE   B 1 50  ? 12.988  28.546  -4.030  1.00 68.36  ? 67  PHE   B CB  1 
ATOM   1367 C CG  . PHE   B 1 50  ? 13.140  29.903  -4.657  1.00 68.98  ? 67  PHE   B CG  1 
ATOM   1368 C CD1 . PHE   B 1 50  ? 12.488  31.006  -4.128  1.00 67.54  ? 67  PHE   B CD1 1 
ATOM   1369 C CD2 . PHE   B 1 50  ? 13.927  30.075  -5.783  1.00 75.06  ? 67  PHE   B CD2 1 
ATOM   1370 C CE1 . PHE   B 1 50  ? 12.625  32.255  -4.706  1.00 68.14  ? 67  PHE   B CE1 1 
ATOM   1371 C CE2 . PHE   B 1 50  ? 14.067  31.321  -6.366  1.00 71.64  ? 67  PHE   B CE2 1 
ATOM   1372 C CZ  . PHE   B 1 50  ? 13.414  32.411  -5.827  1.00 65.76  ? 67  PHE   B CZ  1 
ATOM   1373 N N   . VAL   B 1 51  ? 14.681  29.693  -1.034  1.00 73.96  ? 68  VAL   B N   1 
ATOM   1374 C CA  . VAL   B 1 51  ? 14.532  30.592  0.102   1.00 68.55  ? 68  VAL   B CA  1 
ATOM   1375 C C   . VAL   B 1 51  ? 15.312  31.872  -0.169  1.00 67.12  ? 68  VAL   B C   1 
ATOM   1376 O O   . VAL   B 1 51  ? 16.463  31.820  -0.616  1.00 74.73  ? 68  VAL   B O   1 
ATOM   1377 C CB  . VAL   B 1 51  ? 15.013  29.929  1.409   1.00 63.59  ? 68  VAL   B CB  1 
ATOM   1378 C CG1 . VAL   B 1 51  ? 15.366  30.977  2.458   1.00 58.81  ? 68  VAL   B CG1 1 
ATOM   1379 C CG2 . VAL   B 1 51  ? 13.956  28.970  1.938   1.00 65.35  ? 68  VAL   B CG2 1 
ATOM   1380 N N   . HIS   B 1 52  ? 14.678  33.015  0.102   1.00 69.56  ? 69  HIS   B N   1 
ATOM   1381 C CA  . HIS   B 1 52  ? 15.308  34.335  0.012   1.00 74.01  ? 69  HIS   B CA  1 
ATOM   1382 C C   . HIS   B 1 52  ? 15.845  34.652  -1.385  1.00 67.84  ? 69  HIS   B C   1 
ATOM   1383 O O   . HIS   B 1 52  ? 16.906  35.260  -1.535  1.00 69.82  ? 69  HIS   B O   1 
ATOM   1384 C CB  . HIS   B 1 52  ? 16.408  34.485  1.067   1.00 72.72  ? 69  HIS   B CB  1 
ATOM   1385 C CG  . HIS   B 1 52  ? 15.913  35.020  2.376   1.00 80.04  ? 69  HIS   B CG  1 
ATOM   1386 N ND1 . HIS   B 1 52  ? 15.081  36.115  2.464   1.00 75.40  ? 69  HIS   B ND1 1 
ATOM   1387 C CD2 . HIS   B 1 52  ? 16.125  34.606  3.648   1.00 83.46  ? 69  HIS   B CD2 1 
ATOM   1388 C CE1 . HIS   B 1 52  ? 14.804  36.355  3.733   1.00 74.73  ? 69  HIS   B CE1 1 
ATOM   1389 N NE2 . HIS   B 1 52  ? 15.425  35.454  4.472   1.00 79.97  ? 69  HIS   B NE2 1 
ATOM   1390 N N   . GLY   B 1 53  ? 15.112  34.242  -2.420  1.00 73.63  ? 70  GLY   B N   1 
ATOM   1391 C CA  . GLY   B 1 53  ? 15.424  34.614  -3.784  1.00 72.66  ? 70  GLY   B CA  1 
ATOM   1392 C C   . GLY   B 1 53  ? 16.253  33.624  -4.580  1.00 76.41  ? 70  GLY   B C   1 
ATOM   1393 O O   . GLY   B 1 53  ? 16.296  33.736  -5.811  1.00 75.91  ? 70  GLY   B O   1 
ATOM   1394 N N   . GLU   B 1 54  ? 16.916  32.669  -3.932  1.00 85.37  ? 71  GLU   B N   1 
ATOM   1395 C CA  . GLU   B 1 54  ? 17.783  31.735  -4.640  1.00 89.11  ? 71  GLU   B CA  1 
ATOM   1396 C C   . GLU   B 1 54  ? 17.530  30.324  -4.128  1.00 89.49  ? 71  GLU   B C   1 
ATOM   1397 O O   . GLU   B 1 54  ? 16.743  30.106  -3.201  1.00 87.14  ? 71  GLU   B O   1 
ATOM   1398 C CB  . GLU   B 1 54  ? 19.258  32.125  -4.491  1.00 86.61  ? 71  GLU   B CB  1 
ATOM   1399 N N   . GLU   B 1 55  ? 18.207  29.354  -4.741  1.00 82.14  ? 72  GLU   B N   1 
ATOM   1400 C CA  . GLU   B 1 55  ? 18.068  27.960  -4.347  1.00 77.28  ? 72  GLU   B CA  1 
ATOM   1401 C C   . GLU   B 1 55  ? 19.133  27.588  -3.325  1.00 77.96  ? 72  GLU   B C   1 
ATOM   1402 O O   . GLU   B 1 55  ? 20.290  28.003  -3.435  1.00 81.30  ? 72  GLU   B O   1 
ATOM   1403 C CB  . GLU   B 1 55  ? 18.182  27.041  -5.566  1.00 76.13  ? 72  GLU   B CB  1 
ATOM   1404 C CG  . GLU   B 1 55  ? 17.167  27.311  -6.666  1.00 76.20  ? 72  GLU   B CG  1 
ATOM   1405 C CD  . GLU   B 1 55  ? 17.536  26.635  -7.974  1.00 75.33  ? 72  GLU   B CD  1 
ATOM   1406 O OE1 . GLU   B 1 55  ? 18.358  25.695  -7.949  1.00 76.87  ? 72  GLU   B OE1 1 
ATOM   1407 O OE2 . GLU   B 1 55  ? 17.004  27.043  -9.029  1.00 69.13  ? 72  GLU   B OE2 1 
ATOM   1408 N N   . ASP   B 1 56  ? 18.735  26.796  -2.331  1.00 84.31  ? 73  ASP   B N   1 
ATOM   1409 C CA  . ASP   B 1 56  ? 19.645  26.242  -1.329  1.00 88.13  ? 73  ASP   B CA  1 
ATOM   1410 C C   . ASP   B 1 56  ? 19.639  24.724  -1.492  1.00 86.05  ? 73  ASP   B C   1 
ATOM   1411 O O   . ASP   B 1 56  ? 18.858  24.020  -0.847  1.00 80.54  ? 73  ASP   B O   1 
ATOM   1412 C CB  . ASP   B 1 56  ? 19.250  26.663  0.084   1.00 87.90  ? 73  ASP   B CB  1 
ATOM   1413 C CG  . ASP   B 1 56  ? 20.317  26.325  1.108   1.00 92.26  ? 73  ASP   B CG  1 
ATOM   1414 O OD1 . ASP   B 1 56  ? 21.482  26.116  0.705   1.00 84.31  ? 73  ASP   B OD1 1 
ATOM   1415 O OD2 . ASP   B 1 56  ? 19.994  26.271  2.313   1.00 99.98  ? 73  ASP   B OD2 1 
ATOM   1416 N N   . LEU   B 1 57  ? 20.518  24.223  -2.357  1.00 81.67  ? 74  LEU   B N   1 
ATOM   1417 C CA  . LEU   B 1 57  ? 20.588  22.799  -2.664  1.00 73.75  ? 74  LEU   B CA  1 
ATOM   1418 C C   . LEU   B 1 57  ? 21.276  21.958  -1.593  1.00 74.07  ? 74  LEU   B C   1 
ATOM   1419 O O   . LEU   B 1 57  ? 21.604  20.791  -1.833  1.00 80.71  ? 74  LEU   B O   1 
ATOM   1420 C CB  . LEU   B 1 57  ? 21.140  22.595  -4.077  1.00 71.10  ? 74  LEU   B CB  1 
ATOM   1421 C CG  . LEU   B 1 57  ? 20.536  23.538  -5.124  1.00 78.09  ? 74  LEU   B CG  1 
ATOM   1422 C CD1 . LEU   B 1 57  ? 21.510  24.656  -5.482  1.00 77.85  ? 74  LEU   B CD1 1 
ATOM   1423 C CD2 . LEU   B 1 57  ? 20.089  22.786  -6.370  1.00 68.63  ? 74  LEU   B CD2 1 
ATOM   1424 N N   . LYS   B 1 58  ? 21.498  22.536  -0.411  1.00 73.87  ? 75  LYS   B N   1 
ATOM   1425 C CA  . LYS   B 1 58  ? 22.161  21.827  0.677   1.00 75.10  ? 75  LYS   B CA  1 
ATOM   1426 C C   . LYS   B 1 58  ? 21.490  20.574  1.225   1.00 71.12  ? 75  LYS   B C   1 
ATOM   1427 O O   . LYS   B 1 58  ? 22.148  19.797  1.926   1.00 67.49  ? 75  LYS   B O   1 
ATOM   1428 C CB  . LYS   B 1 58  ? 22.415  22.811  1.822   1.00 72.95  ? 75  LYS   B CB  1 
ATOM   1429 N N   . VAL   B 1 59  ? 20.208  20.358  0.928   1.00 70.72  ? 76  VAL   B N   1 
ATOM   1430 C CA  . VAL   B 1 59  ? 19.488  19.161  1.332   1.00 67.62  ? 76  VAL   B CA  1 
ATOM   1431 C C   . VAL   B 1 59  ? 18.984  18.372  0.131   1.00 72.83  ? 76  VAL   B C   1 
ATOM   1432 O O   . VAL   B 1 59  ? 18.263  17.387  0.296   1.00 70.77  ? 76  VAL   B O   1 
ATOM   1433 C CB  . VAL   B 1 59  ? 18.325  19.498  2.288   1.00 70.88  ? 76  VAL   B CB  1 
ATOM   1434 C CG1 . VAL   B 1 59  ? 18.837  19.654  3.711   1.00 72.35  ? 76  VAL   B CG1 1 
ATOM   1435 C CG2 . VAL   B 1 59  ? 17.607  20.755  1.828   1.00 66.61  ? 76  VAL   B CG2 1 
ATOM   1436 N N   . GLN   B 1 60  ? 19.350  18.792  -1.079  1.00 73.36  ? 77  GLN   B N   1 
ATOM   1437 C CA  . GLN   B 1 60  ? 18.934  18.091  -2.286  1.00 76.75  ? 77  GLN   B CA  1 
ATOM   1438 C C   . GLN   B 1 60  ? 19.511  16.682  -2.324  1.00 84.46  ? 77  GLN   B C   1 
ATOM   1439 O O   . GLN   B 1 60  ? 20.691  16.466  -2.032  1.00 86.42  ? 77  GLN   B O   1 
ATOM   1440 C CB  . GLN   B 1 60  ? 19.385  18.860  -3.529  1.00 76.53  ? 77  GLN   B CB  1 
ATOM   1441 C CG  . GLN   B 1 60  ? 19.207  18.078  -4.824  1.00 77.94  ? 77  GLN   B CG  1 
ATOM   1442 C CD  . GLN   B 1 60  ? 19.542  18.890  -6.056  1.00 78.66  ? 77  GLN   B CD  1 
ATOM   1443 O OE1 . GLN   B 1 60  ? 20.488  19.675  -6.054  1.00 80.87  ? 77  GLN   B OE1 1 
ATOM   1444 N NE2 . GLN   B 1 60  ? 18.770  18.701  -7.120  1.00 75.38  ? 77  GLN   B NE2 1 
ATOM   1445 N N   . HIS   B 1 61  ? 18.666  15.720  -2.684  1.00 99.48  ? 78  HIS   B N   1 
ATOM   1446 C CA  . HIS   B 1 61  ? 19.114  14.345  -2.838  1.00 96.00  ? 78  HIS   B CA  1 
ATOM   1447 C C   . HIS   B 1 61  ? 20.097  14.242  -4.000  1.00 100.19 ? 78  HIS   B C   1 
ATOM   1448 O O   . HIS   B 1 61  ? 20.005  14.976  -4.987  1.00 99.72  ? 78  HIS   B O   1 
ATOM   1449 C CB  . HIS   B 1 61  ? 17.918  13.422  -3.076  1.00 98.83  ? 78  HIS   B CB  1 
ATOM   1450 C CG  . HIS   B 1 61  ? 18.091  12.044  -2.518  1.00 108.78 ? 78  HIS   B CG  1 
ATOM   1451 N ND1 . HIS   B 1 61  ? 18.332  10.944  -3.313  1.00 107.08 ? 78  HIS   B ND1 1 
ATOM   1452 C CD2 . HIS   B 1 61  ? 18.047  11.585  -1.245  1.00 111.80 ? 78  HIS   B CD2 1 
ATOM   1453 C CE1 . HIS   B 1 61  ? 18.434  9.868   -2.554  1.00 107.57 ? 78  HIS   B CE1 1 
ATOM   1454 N NE2 . HIS   B 1 61  ? 18.265  10.229  -1.295  1.00 111.33 ? 78  HIS   B NE2 1 
ATOM   1455 N N   . SER   B 1 62  ? 21.056  13.323  -3.864  1.00 100.35 ? 79  SER   B N   1 
ATOM   1456 C CA  . SER   B 1 62  ? 22.072  13.143  -4.898  1.00 90.99  ? 79  SER   B CA  1 
ATOM   1457 C C   . SER   B 1 62  ? 21.446  12.782  -6.240  1.00 88.69  ? 79  SER   B C   1 
ATOM   1458 O O   . SER   B 1 62  ? 21.939  13.196  -7.296  1.00 81.81  ? 79  SER   B O   1 
ATOM   1459 C CB  . SER   B 1 62  ? 23.074  12.071  -4.467  1.00 85.81  ? 79  SER   B CB  1 
ATOM   1460 O OG  . SER   B 1 62  ? 22.440  11.064  -3.699  1.00 93.45  ? 79  SER   B OG  1 
ATOM   1461 N N   . SER   B 1 63  ? 20.364  11.999  -6.217  1.00 84.73  ? 80  SER   B N   1 
ATOM   1462 C CA  . SER   B 1 63  ? 19.707  11.553  -7.441  1.00 78.15  ? 80  SER   B CA  1 
ATOM   1463 C C   . SER   B 1 63  ? 19.204  12.699  -8.313  1.00 79.09  ? 80  SER   B C   1 
ATOM   1464 O O   . SER   B 1 63  ? 18.939  12.482  -9.500  1.00 76.64  ? 80  SER   B O   1 
ATOM   1465 C CB  . SER   B 1 63  ? 18.540  10.628  -7.091  1.00 72.98  ? 80  SER   B CB  1 
ATOM   1466 O OG  . SER   B 1 63  ? 17.544  11.324  -6.361  1.00 82.47  ? 80  SER   B OG  1 
ATOM   1467 N N   . TYR   B 1 64  ? 19.060  13.908  -7.764  1.00 81.23  ? 81  TYR   B N   1 
ATOM   1468 C CA  . TYR   B 1 64  ? 18.520  15.033  -8.515  1.00 76.64  ? 81  TYR   B CA  1 
ATOM   1469 C C   . TYR   B 1 64  ? 19.545  16.098  -8.880  1.00 78.28  ? 81  TYR   B C   1 
ATOM   1470 O O   . TYR   B 1 64  ? 19.199  17.033  -9.612  1.00 77.48  ? 81  TYR   B O   1 
ATOM   1471 C CB  . TYR   B 1 64  ? 17.381  15.696  -7.728  1.00 69.48  ? 81  TYR   B CB  1 
ATOM   1472 C CG  . TYR   B 1 64  ? 16.123  14.866  -7.671  1.00 59.44  ? 81  TYR   B CG  1 
ATOM   1473 C CD1 . TYR   B 1 64  ? 15.385  14.618  -8.818  1.00 60.28  ? 81  TYR   B CD1 1 
ATOM   1474 C CD2 . TYR   B 1 64  ? 15.673  14.331  -6.472  1.00 60.11  ? 81  TYR   B CD2 1 
ATOM   1475 C CE1 . TYR   B 1 64  ? 14.234  13.861  -8.777  1.00 60.17  ? 81  TYR   B CE1 1 
ATOM   1476 C CE2 . TYR   B 1 64  ? 14.521  13.569  -6.419  1.00 61.19  ? 81  TYR   B CE2 1 
ATOM   1477 C CZ  . TYR   B 1 64  ? 13.806  13.338  -7.577  1.00 61.81  ? 81  TYR   B CZ  1 
ATOM   1478 O OH  . TYR   B 1 64  ? 12.657  12.584  -7.541  1.00 60.23  ? 81  TYR   B OH  1 
ATOM   1479 N N   . ARG   B 1 65  ? 20.781  15.991  -8.398  1.00 87.28  ? 82  ARG   B N   1 
ATOM   1480 C CA  . ARG   B 1 65  ? 21.774  17.025  -8.660  1.00 93.55  ? 82  ARG   B CA  1 
ATOM   1481 C C   . ARG   B 1 65  ? 22.050  17.147  -10.155 1.00 92.10  ? 82  ARG   B C   1 
ATOM   1482 O O   . ARG   B 1 65  ? 22.067  16.152  -10.885 1.00 92.29  ? 82  ARG   B O   1 
ATOM   1483 C CB  . ARG   B 1 65  ? 23.068  16.718  -7.907  1.00 88.74  ? 82  ARG   B CB  1 
ATOM   1484 N N   . GLN   B 1 66  ? 22.251  18.387  -10.606 1.00 77.91  ? 83  GLN   B N   1 
ATOM   1485 C CA  . GLN   B 1 66  ? 22.534  18.773  -11.988 1.00 76.13  ? 83  GLN   B CA  1 
ATOM   1486 C C   . GLN   B 1 66  ? 21.366  18.523  -12.934 1.00 76.73  ? 83  GLN   B C   1 
ATOM   1487 O O   . GLN   B 1 66  ? 21.511  18.747  -14.142 1.00 76.93  ? 83  GLN   B O   1 
ATOM   1488 C CB  . GLN   B 1 66  ? 23.780  18.073  -12.550 1.00 76.55  ? 83  GLN   B CB  1 
ATOM   1489 C CG  . GLN   B 1 66  ? 25.060  18.874  -12.399 1.00 68.76  ? 83  GLN   B CG  1 
ATOM   1490 C CD  . GLN   B 1 66  ? 25.831  18.499  -11.151 1.00 63.81  ? 83  GLN   B CD  1 
ATOM   1491 O OE1 . GLN   B 1 66  ? 25.730  17.374  -10.661 1.00 64.50  ? 83  GLN   B OE1 1 
ATOM   1492 N NE2 . GLN   B 1 66  ? 26.605  19.442  -10.627 1.00 53.84  ? 83  GLN   B NE2 1 
ATOM   1493 N N   . ARG   B 1 67  ? 20.215  18.075  -12.437 1.00 73.57  ? 84  ARG   B N   1 
ATOM   1494 C CA  . ARG   B 1 67  ? 19.053  17.818  -13.275 1.00 72.91  ? 84  ARG   B CA  1 
ATOM   1495 C C   . ARG   B 1 67  ? 17.839  18.659  -12.918 1.00 72.40  ? 84  ARG   B C   1 
ATOM   1496 O O   . ARG   B 1 67  ? 17.001  18.904  -13.790 1.00 68.62  ? 84  ARG   B O   1 
ATOM   1497 C CB  . ARG   B 1 67  ? 18.660  16.333  -13.211 1.00 66.12  ? 84  ARG   B CB  1 
ATOM   1498 C CG  . ARG   B 1 67  ? 19.840  15.377  -13.237 1.00 68.56  ? 84  ARG   B CG  1 
ATOM   1499 C CD  . ARG   B 1 67  ? 19.416  13.993  -13.697 1.00 64.24  ? 84  ARG   B CD  1 
ATOM   1500 N NE  . ARG   B 1 67  ? 18.938  13.175  -12.589 1.00 64.09  ? 84  ARG   B NE  1 
ATOM   1501 C CZ  . ARG   B 1 67  ? 17.681  12.782  -12.435 1.00 57.73  ? 84  ARG   B CZ  1 
ATOM   1502 N NH1 . ARG   B 1 67  ? 16.742  13.114  -13.307 1.00 55.14  ? 84  ARG   B NH1 1 
ATOM   1503 N NH2 . ARG   B 1 67  ? 17.357  12.041  -11.380 1.00 55.94  ? 84  ARG   B NH2 1 
ATOM   1504 N N   . ALA   B 1 68  ? 17.719  19.107  -11.673 1.00 69.89  ? 85  ALA   B N   1 
ATOM   1505 C CA  . ALA   B 1 68  ? 16.552  19.844  -11.214 1.00 60.29  ? 85  ALA   B CA  1 
ATOM   1506 C C   . ALA   B 1 68  ? 16.876  21.328  -11.112 1.00 66.65  ? 85  ALA   B C   1 
ATOM   1507 O O   . ALA   B 1 68  ? 17.938  21.711  -10.611 1.00 67.27  ? 85  ALA   B O   1 
ATOM   1508 C CB  . ALA   B 1 68  ? 16.072  19.320  -9.860  1.00 61.21  ? 85  ALA   B CB  1 
ATOM   1509 N N   . ARG   B 1 69  ? 15.954  22.157  -11.592 1.00 67.16  ? 86  ARG   B N   1 
ATOM   1510 C CA  . ARG   B 1 69  ? 16.085  23.603  -11.495 1.00 62.16  ? 86  ARG   B CA  1 
ATOM   1511 C C   . ARG   B 1 69  ? 14.695  24.216  -11.428 1.00 63.20  ? 86  ARG   B C   1 
ATOM   1512 O O   . ARG   B 1 69  ? 13.773  23.759  -12.110 1.00 59.38  ? 86  ARG   B O   1 
ATOM   1513 C CB  . ARG   B 1 69  ? 16.884  24.182  -12.671 1.00 60.74  ? 86  ARG   B CB  1 
ATOM   1514 C CG  . ARG   B 1 69  ? 16.214  24.061  -14.031 1.00 66.57  ? 86  ARG   B CG  1 
ATOM   1515 C CD  . ARG   B 1 69  ? 16.721  25.136  -14.980 1.00 73.84  ? 86  ARG   B CD  1 
ATOM   1516 N NE  . ARG   B 1 69  ? 16.091  25.058  -16.293 1.00 81.39  ? 86  ARG   B NE  1 
ATOM   1517 C CZ  . ARG   B 1 69  ? 16.653  25.479  -17.418 1.00 81.32  ? 86  ARG   B CZ  1 
ATOM   1518 N NH1 . ARG   B 1 69  ? 17.866  26.007  -17.429 1.00 82.86  ? 86  ARG   B NH1 1 
ATOM   1519 N NH2 . ARG   B 1 69  ? 15.982  25.365  -18.561 1.00 84.20  ? 86  ARG   B NH2 1 
ATOM   1520 N N   . LEU   B 1 70  ? 14.547  25.236  -10.589 1.00 70.35  ? 87  LEU   B N   1 
ATOM   1521 C CA  . LEU   B 1 70  ? 13.303  25.985  -10.497 1.00 62.16  ? 87  LEU   B CA  1 
ATOM   1522 C C   . LEU   B 1 70  ? 13.339  27.138  -11.492 1.00 60.53  ? 87  LEU   B C   1 
ATOM   1523 O O   . LEU   B 1 70  ? 14.312  27.898  -11.538 1.00 72.46  ? 87  LEU   B O   1 
ATOM   1524 C CB  . LEU   B 1 70  ? 13.104  26.511  -9.074  1.00 59.71  ? 87  LEU   B CB  1 
ATOM   1525 C CG  . LEU   B 1 70  ? 11.816  27.243  -8.682  1.00 68.01  ? 87  LEU   B CG  1 
ATOM   1526 C CD1 . LEU   B 1 70  ? 10.607  26.728  -9.449  1.00 64.32  ? 87  LEU   B CD1 1 
ATOM   1527 C CD2 . LEU   B 1 70  ? 11.586  27.133  -7.182  1.00 66.29  ? 87  LEU   B CD2 1 
ATOM   1528 N N   . LEU   B 1 71  ? 12.281  27.259  -12.288 1.00 67.64  ? 88  LEU   B N   1 
ATOM   1529 C CA  . LEU   B 1 71  ? 12.187  28.300  -13.309 1.00 69.69  ? 88  LEU   B CA  1 
ATOM   1530 C C   . LEU   B 1 71  ? 11.893  29.628  -12.622 1.00 75.35  ? 88  LEU   B C   1 
ATOM   1531 O O   . LEU   B 1 71  ? 10.751  29.917  -12.261 1.00 80.24  ? 88  LEU   B O   1 
ATOM   1532 C CB  . LEU   B 1 71  ? 11.111  27.946  -14.330 1.00 76.93  ? 88  LEU   B CB  1 
ATOM   1533 C CG  . LEU   B 1 71  ? 11.269  26.637  -15.115 1.00 71.81  ? 88  LEU   B CG  1 
ATOM   1534 C CD1 . LEU   B 1 71  ? 10.566  26.731  -16.460 1.00 67.67  ? 88  LEU   B CD1 1 
ATOM   1535 C CD2 . LEU   B 1 71  ? 12.735  26.268  -15.312 1.00 62.98  ? 88  LEU   B CD2 1 
ATOM   1536 N N   . LYS   B 1 72  ? 12.933  30.445  -12.438 1.00 81.20  ? 89  LYS   B N   1 
ATOM   1537 C CA  . LYS   B 1 72  ? 12.778  31.685  -11.683 1.00 83.19  ? 89  LYS   B CA  1 
ATOM   1538 C C   . LYS   B 1 72  ? 11.966  32.723  -12.446 1.00 89.13  ? 89  LYS   B C   1 
ATOM   1539 O O   . LYS   B 1 72  ? 11.350  33.599  -11.829 1.00 87.26  ? 89  LYS   B O   1 
ATOM   1540 C CB  . LYS   B 1 72  ? 14.150  32.250  -11.316 1.00 75.18  ? 89  LYS   B CB  1 
ATOM   1541 N N   . ASP   B 1 73  ? 11.950  32.647  -13.779 1.00 110.86 ? 90  ASP   B N   1 
ATOM   1542 C CA  . ASP   B 1 73  ? 11.210  33.626  -14.569 1.00 108.62 ? 90  ASP   B CA  1 
ATOM   1543 C C   . ASP   B 1 73  ? 9.703   33.458  -14.417 1.00 108.28 ? 90  ASP   B C   1 
ATOM   1544 O O   . ASP   B 1 73  ? 8.965   34.449  -14.452 1.00 110.35 ? 90  ASP   B O   1 
ATOM   1545 C CB  . ASP   B 1 73  ? 11.609  33.527  -16.042 1.00 108.80 ? 90  ASP   B CB  1 
ATOM   1546 C CG  . ASP   B 1 73  ? 11.800  32.096  -16.500 1.00 120.84 ? 90  ASP   B CG  1 
ATOM   1547 O OD1 . ASP   B 1 73  ? 11.591  31.174  -15.683 1.00 118.47 ? 90  ASP   B OD1 1 
ATOM   1548 O OD2 . ASP   B 1 73  ? 12.159  31.893  -17.679 1.00 135.04 ? 90  ASP   B OD2 1 
ATOM   1549 N N   . GLN   B 1 74  ? 9.228   32.222  -14.246 1.00 95.40  ? 91  GLN   B N   1 
ATOM   1550 C CA  . GLN   B 1 74  ? 7.798   31.955  -14.137 1.00 86.58  ? 91  GLN   B CA  1 
ATOM   1551 C C   . GLN   B 1 74  ? 7.206   32.416  -12.811 1.00 81.42  ? 91  GLN   B C   1 
ATOM   1552 O O   . GLN   B 1 74  ? 5.979   32.425  -12.671 1.00 83.09  ? 91  GLN   B O   1 
ATOM   1553 C CB  . GLN   B 1 74  ? 7.524   30.464  -14.341 1.00 80.89  ? 91  GLN   B CB  1 
ATOM   1554 C CG  . GLN   B 1 74  ? 7.685   29.992  -15.782 1.00 79.85  ? 91  GLN   B CG  1 
ATOM   1555 C CD  . GLN   B 1 74  ? 6.592   30.501  -16.713 1.00 74.36  ? 91  GLN   B CD  1 
ATOM   1556 O OE1 . GLN   B 1 74  ? 5.717   31.271  -16.314 1.00 80.58  ? 91  GLN   B OE1 1 
ATOM   1557 N NE2 . GLN   B 1 74  ? 6.645   30.069  -17.967 1.00 67.72  ? 91  GLN   B NE2 1 
ATOM   1558 N N   . LEU   B 1 75  ? 8.043   32.795  -11.843 1.00 84.41  ? 92  LEU   B N   1 
ATOM   1559 C CA  . LEU   B 1 75  ? 7.560   33.298  -10.561 1.00 81.47  ? 92  LEU   B CA  1 
ATOM   1560 C C   . LEU   B 1 75  ? 6.761   34.587  -10.708 1.00 95.33  ? 92  LEU   B C   1 
ATOM   1561 O O   . LEU   B 1 75  ? 6.074   34.985  -9.760  1.00 92.72  ? 92  LEU   B O   1 
ATOM   1562 C CB  . LEU   B 1 75  ? 8.732   33.518  -9.603  1.00 77.10  ? 92  LEU   B CB  1 
ATOM   1563 C CG  . LEU   B 1 75  ? 9.566   32.284  -9.249  1.00 76.04  ? 92  LEU   B CG  1 
ATOM   1564 C CD1 . LEU   B 1 75  ? 10.630  32.627  -8.215  1.00 72.56  ? 92  LEU   B CD1 1 
ATOM   1565 C CD2 . LEU   B 1 75  ? 8.676   31.155  -8.751  1.00 67.79  ? 92  LEU   B CD2 1 
ATOM   1566 N N   . SER   B 1 76  ? 6.870   35.262  -11.856 1.00 120.93 ? 93  SER   B N   1 
ATOM   1567 C CA  . SER   B 1 76  ? 6.119   36.489  -12.112 1.00 118.95 ? 93  SER   B CA  1 
ATOM   1568 C C   . SER   B 1 76  ? 4.639   36.337  -11.770 1.00 117.48 ? 93  SER   B C   1 
ATOM   1569 O O   . SER   B 1 76  ? 4.121   37.023  -10.882 1.00 120.33 ? 93  SER   B O   1 
ATOM   1570 C CB  . SER   B 1 76  ? 6.284   36.889  -13.581 1.00 124.55 ? 93  SER   B CB  1 
ATOM   1571 O OG  . SER   B 1 76  ? 5.721   35.918  -14.449 1.00 123.03 ? 93  SER   B OG  1 
ATOM   1572 N N   . LEU   B 1 77  ? 3.939   35.439  -12.464 1.00 96.28  ? 94  LEU   B N   1 
ATOM   1573 C CA  . LEU   B 1 77  ? 2.498   35.282  -12.299 1.00 94.27  ? 94  LEU   B CA  1 
ATOM   1574 C C   . LEU   B 1 77  ? 2.135   34.106  -11.400 1.00 83.31  ? 94  LEU   B C   1 
ATOM   1575 O O   . LEU   B 1 77  ? 1.086   33.479  -11.591 1.00 85.79  ? 94  LEU   B O   1 
ATOM   1576 C CB  . LEU   B 1 77  ? 1.820   35.135  -13.661 1.00 100.12 ? 94  LEU   B CB  1 
ATOM   1577 N N   . GLY   B 1 78  ? 2.977   33.791  -10.422 1.00 79.52  ? 95  GLY   B N   1 
ATOM   1578 C CA  . GLY   B 1 78  ? 2.646   32.734  -9.489  1.00 75.86  ? 95  GLY   B CA  1 
ATOM   1579 C C   . GLY   B 1 78  ? 2.782   31.331  -10.037 1.00 62.48  ? 95  GLY   B C   1 
ATOM   1580 O O   . GLY   B 1 78  ? 1.943   30.473  -9.741  1.00 61.20  ? 95  GLY   B O   1 
ATOM   1581 N N   . ASN   B 1 79  ? 3.817   31.068  -10.832 1.00 58.53  ? 96  ASN   B N   1 
ATOM   1582 C CA  . ASN   B 1 79  ? 4.053   29.743  -11.403 1.00 64.35  ? 96  ASN   B CA  1 
ATOM   1583 C C   . ASN   B 1 79  ? 5.395   29.214  -10.906 1.00 65.62  ? 96  ASN   B C   1 
ATOM   1584 O O   . ASN   B 1 79  ? 6.451   29.583  -11.428 1.00 69.64  ? 96  ASN   B O   1 
ATOM   1585 C CB  . ASN   B 1 79  ? 4.014   29.801  -12.928 1.00 66.57  ? 96  ASN   B CB  1 
ATOM   1586 C CG  . ASN   B 1 79  ? 3.978   28.427  -13.563 1.00 71.13  ? 96  ASN   B CG  1 
ATOM   1587 O OD1 . ASN   B 1 79  ? 3.872   27.413  -12.874 1.00 72.39  ? 96  ASN   B OD1 1 
ATOM   1588 N ND2 . ASN   B 1 79  ? 4.066   28.387  -14.887 1.00 72.65  ? 96  ASN   B ND2 1 
ATOM   1589 N N   . ALA   B 1 80  ? 5.350   28.347  -9.894  1.00 62.77  ? 97  ALA   B N   1 
ATOM   1590 C CA  . ALA   B 1 80  ? 6.532   27.635  -9.410  1.00 64.73  ? 97  ALA   B CA  1 
ATOM   1591 C C   . ALA   B 1 80  ? 6.675   26.372  -10.250 1.00 65.93  ? 97  ALA   B C   1 
ATOM   1592 O O   . ALA   B 1 80  ? 6.078   25.336  -9.957  1.00 65.24  ? 97  ALA   B O   1 
ATOM   1593 C CB  . ALA   B 1 80  ? 6.408   27.324  -7.924  1.00 62.41  ? 97  ALA   B CB  1 
ATOM   1594 N N   . ALA   B 1 81  ? 7.478   26.455  -11.308 1.00 75.55  ? 98  ALA   B N   1 
ATOM   1595 C CA  . ALA   B 1 81  ? 7.594   25.393  -12.301 1.00 77.09  ? 98  ALA   B CA  1 
ATOM   1596 C C   . ALA   B 1 81  ? 8.935   24.689  -12.137 1.00 75.58  ? 98  ALA   B C   1 
ATOM   1597 O O   . ALA   B 1 81  ? 9.990   25.326  -12.230 1.00 75.85  ? 98  ALA   B O   1 
ATOM   1598 C CB  . ALA   B 1 81  ? 7.447   25.955  -13.715 1.00 79.08  ? 98  ALA   B CB  1 
ATOM   1599 N N   . LEU   B 1 82  ? 8.893   23.378  -11.905 1.00 62.85  ? 99  LEU   B N   1 
ATOM   1600 C CA  . LEU   B 1 82  ? 10.095  22.578  -11.707 1.00 60.91  ? 99  LEU   B CA  1 
ATOM   1601 C C   . LEU   B 1 82  ? 10.367  21.769  -12.969 1.00 59.63  ? 99  LEU   B C   1 
ATOM   1602 O O   . LEU   B 1 82  ? 9.463   21.117  -13.502 1.00 56.97  ? 99  LEU   B O   1 
ATOM   1603 C CB  . LEU   B 1 82  ? 9.939   21.638  -10.509 1.00 55.44  ? 99  LEU   B CB  1 
ATOM   1604 C CG  . LEU   B 1 82  ? 10.916  20.465  -10.362 1.00 60.79  ? 99  LEU   B CG  1 
ATOM   1605 C CD1 . LEU   B 1 82  ? 12.379  20.938  -10.418 1.00 60.79  ? 99  LEU   B CD1 1 
ATOM   1606 C CD2 . LEU   B 1 82  ? 10.637  19.648  -9.107  1.00 52.53  ? 99  LEU   B CD2 1 
ATOM   1607 N N   . GLN   B 1 83  ? 11.609  21.810  -13.439 1.00 61.24  ? 100 GLN   B N   1 
ATOM   1608 C CA  . GLN   B 1 83  ? 12.034  21.093  -14.632 1.00 63.81  ? 100 GLN   B CA  1 
ATOM   1609 C C   . GLN   B 1 83  ? 13.054  20.033  -14.239 1.00 61.80  ? 100 GLN   B C   1 
ATOM   1610 O O   . GLN   B 1 83  ? 14.010  20.328  -13.514 1.00 68.44  ? 100 GLN   B O   1 
ATOM   1611 C CB  . GLN   B 1 83  ? 12.625  22.055  -15.667 1.00 66.90  ? 100 GLN   B CB  1 
ATOM   1612 C CG  . GLN   B 1 83  ? 12.740  21.477  -17.068 1.00 68.35  ? 100 GLN   B CG  1 
ATOM   1613 C CD  . GLN   B 1 83  ? 13.819  22.157  -17.891 1.00 74.62  ? 100 GLN   B CD  1 
ATOM   1614 O OE1 . GLN   B 1 83  ? 14.973  22.254  -17.468 1.00 75.49  ? 100 GLN   B OE1 1 
ATOM   1615 N NE2 . GLN   B 1 83  ? 13.447  22.635  -19.073 1.00 78.79  ? 100 GLN   B NE2 1 
ATOM   1616 N N   . ILE   B 1 84  ? 12.846  18.806  -14.711 1.00 59.32  ? 101 ILE   B N   1 
ATOM   1617 C CA  . ILE   B 1 84  ? 13.768  17.694  -14.491 1.00 58.74  ? 101 ILE   B CA  1 
ATOM   1618 C C   . ILE   B 1 84  ? 14.349  17.290  -15.838 1.00 59.36  ? 101 ILE   B C   1 
ATOM   1619 O O   . ILE   B 1 84  ? 13.606  17.031  -16.793 1.00 60.37  ? 101 ILE   B O   1 
ATOM   1620 C CB  . ILE   B 1 84  ? 13.086  16.488  -13.814 1.00 61.49  ? 101 ILE   B CB  1 
ATOM   1621 C CG1 . ILE   B 1 84  ? 12.642  16.823  -12.390 1.00 62.12  ? 101 ILE   B CG1 1 
ATOM   1622 C CG2 . ILE   B 1 84  ? 14.035  15.293  -13.734 1.00 56.71  ? 101 ILE   B CG2 1 
ATOM   1623 C CD1 . ILE   B 1 84  ? 11.749  15.808  -11.752 1.00 61.12  ? 101 ILE   B CD1 1 
ATOM   1624 N N   . THR   B 1 85  ? 15.674  17.281  -15.926 1.00 63.33  ? 102 THR   B N   1 
ATOM   1625 C CA  . THR   B 1 85  ? 16.358  16.783  -17.108 1.00 63.99  ? 102 THR   B CA  1 
ATOM   1626 C C   . THR   B 1 85  ? 16.720  15.323  -16.880 1.00 60.88  ? 102 THR   B C   1 
ATOM   1627 O O   . THR   B 1 85  ? 17.051  14.924  -15.760 1.00 67.49  ? 102 THR   B O   1 
ATOM   1628 C CB  . THR   B 1 85  ? 17.617  17.599  -17.405 1.00 65.14  ? 102 THR   B CB  1 
ATOM   1629 O OG1 . THR   B 1 85  ? 18.653  17.237  -16.483 1.00 68.90  ? 102 THR   B OG1 1 
ATOM   1630 C CG2 . THR   B 1 85  ? 17.329  19.087  -17.282 1.00 54.68  ? 102 THR   B CG2 1 
ATOM   1631 N N   . ASP   B 1 86  ? 16.649  14.528  -17.949 1.00 62.87  ? 103 ASP   B N   1 
ATOM   1632 C CA  . ASP   B 1 86  ? 16.872  13.085  -17.877 1.00 63.15  ? 103 ASP   B CA  1 
ATOM   1633 C C   . ASP   B 1 86  ? 15.936  12.435  -16.857 1.00 61.23  ? 103 ASP   B C   1 
ATOM   1634 O O   . ASP   B 1 86  ? 16.366  11.916  -15.824 1.00 61.11  ? 103 ASP   B O   1 
ATOM   1635 C CB  . ASP   B 1 86  ? 18.335  12.763  -17.550 1.00 68.66  ? 103 ASP   B CB  1 
ATOM   1636 C CG  . ASP   B 1 86  ? 19.216  12.735  -18.776 1.00 77.07  ? 103 ASP   B CG  1 
ATOM   1637 O OD1 . ASP   B 1 86  ? 18.672  12.700  -19.899 1.00 81.16  ? 103 ASP   B OD1 1 
ATOM   1638 O OD2 . ASP   B 1 86  ? 20.455  12.745  -18.617 1.00 83.29  ? 103 ASP   B OD2 1 
ATOM   1639 N N   . VAL   B 1 87  ? 14.633  12.508  -17.142 1.00 61.09  ? 104 VAL   B N   1 
ATOM   1640 C CA  . VAL   B 1 87  ? 13.676  11.759  -16.340 1.00 57.96  ? 104 VAL   B CA  1 
ATOM   1641 C C   . VAL   B 1 87  ? 14.077  10.294  -16.343 1.00 56.88  ? 104 VAL   B C   1 
ATOM   1642 O O   . VAL   B 1 87  ? 14.258  9.687   -17.404 1.00 47.21  ? 104 VAL   B O   1 
ATOM   1643 C CB  . VAL   B 1 87  ? 12.245  11.953  -16.871 1.00 56.87  ? 104 VAL   B CB  1 
ATOM   1644 C CG1 . VAL   B 1 87  ? 11.244  11.392  -15.881 1.00 55.31  ? 104 VAL   B CG1 1 
ATOM   1645 C CG2 . VAL   B 1 87  ? 11.964  13.422  -17.124 1.00 59.17  ? 104 VAL   B CG2 1 
ATOM   1646 N N   . LYS   B 1 88  ? 14.218  9.720   -15.156 1.00 59.07  ? 105 LYS   B N   1 
ATOM   1647 C CA  . LYS   B 1 88  ? 14.588  8.324   -15.021 1.00 57.63  ? 105 LYS   B CA  1 
ATOM   1648 C C   . LYS   B 1 88  ? 13.473  7.556   -14.328 1.00 58.32  ? 105 LYS   B C   1 
ATOM   1649 O O   . LYS   B 1 88  ? 12.544  8.139   -13.762 1.00 59.46  ? 105 LYS   B O   1 
ATOM   1650 C CB  . LYS   B 1 88  ? 15.898  8.170   -14.238 1.00 61.48  ? 105 LYS   B CB  1 
ATOM   1651 N N   . LEU   B 1 89  ? 13.571  6.226   -14.402 1.00 51.63  ? 106 LEU   B N   1 
ATOM   1652 C CA  . LEU   B 1 89  ? 12.561  5.375   -13.784 1.00 55.18  ? 106 LEU   B CA  1 
ATOM   1653 C C   . LEU   B 1 89  ? 12.466  5.627   -12.286 1.00 56.28  ? 106 LEU   B C   1 
ATOM   1654 O O   . LEU   B 1 89  ? 11.390  5.471   -11.696 1.00 57.80  ? 106 LEU   B O   1 
ATOM   1655 C CB  . LEU   B 1 89  ? 12.865  3.908   -14.083 1.00 51.95  ? 106 LEU   B CB  1 
ATOM   1656 C CG  . LEU   B 1 89  ? 12.425  3.489   -15.490 1.00 51.73  ? 106 LEU   B CG  1 
ATOM   1657 C CD1 . LEU   B 1 89  ? 13.471  2.607   -16.156 1.00 51.08  ? 106 LEU   B CD1 1 
ATOM   1658 C CD2 . LEU   B 1 89  ? 11.070  2.797   -15.456 1.00 51.87  ? 106 LEU   B CD2 1 
ATOM   1659 N N   . GLN   B 1 90  ? 13.574  6.020   -11.656 1.00 52.29  ? 107 GLN   B N   1 
ATOM   1660 C CA  . GLN   B 1 90  ? 13.577  6.323   -10.232 1.00 56.68  ? 107 GLN   B CA  1 
ATOM   1661 C C   . GLN   B 1 90  ? 12.951  7.675   -9.919  1.00 53.61  ? 107 GLN   B C   1 
ATOM   1662 O O   . GLN   B 1 90  ? 12.674  7.954   -8.747  1.00 49.35  ? 107 GLN   B O   1 
ATOM   1663 C CB  . GLN   B 1 90  ? 15.007  6.282   -9.688  1.00 61.87  ? 107 GLN   B CB  1 
ATOM   1664 C CG  . GLN   B 1 90  ? 16.053  6.805   -10.660 1.00 64.52  ? 107 GLN   B CG  1 
ATOM   1665 C CD  . GLN   B 1 90  ? 17.432  6.905   -10.038 1.00 68.32  ? 107 GLN   B CD  1 
ATOM   1666 O OE1 . GLN   B 1 90  ? 17.633  6.533   -8.882  1.00 72.93  ? 107 GLN   B OE1 1 
ATOM   1667 N NE2 . GLN   B 1 90  ? 18.391  7.413   -10.804 1.00 67.05  ? 107 GLN   B NE2 1 
ATOM   1668 N N   . ASP   B 1 91  ? 12.724  8.515   -10.929 1.00 52.92  ? 108 ASP   B N   1 
ATOM   1669 C CA  . ASP   B 1 91  ? 12.046  9.793   -10.750 1.00 52.95  ? 108 ASP   B CA  1 
ATOM   1670 C C   . ASP   B 1 91  ? 10.530  9.655   -10.717 1.00 52.12  ? 108 ASP   B C   1 
ATOM   1671 O O   . ASP   B 1 91  ? 9.830   10.672  -10.685 1.00 52.85  ? 108 ASP   B O   1 
ATOM   1672 C CB  . ASP   B 1 91  ? 12.450  10.768  -11.861 1.00 50.89  ? 108 ASP   B CB  1 
ATOM   1673 C CG  . ASP   B 1 91  ? 13.897  11.205  -11.756 1.00 54.50  ? 108 ASP   B CG  1 
ATOM   1674 O OD1 . ASP   B 1 91  ? 14.413  11.290  -10.622 1.00 58.28  ? 108 ASP   B OD1 1 
ATOM   1675 O OD2 . ASP   B 1 91  ? 14.517  11.468  -12.808 1.00 57.02  ? 108 ASP   B OD2 1 
ATOM   1676 N N   . ALA   B 1 92  ? 10.014  8.430   -10.726 1.00 53.17  ? 109 ALA   B N   1 
ATOM   1677 C CA  . ALA   B 1 92  ? 8.582   8.188   -10.640 1.00 44.22  ? 109 ALA   B CA  1 
ATOM   1678 C C   . ALA   B 1 92  ? 8.156   8.093   -9.182  1.00 45.47  ? 109 ALA   B C   1 
ATOM   1679 O O   . ALA   B 1 92  ? 8.847   7.487   -8.358  1.00 51.12  ? 109 ALA   B O   1 
ATOM   1680 C CB  . ALA   B 1 92  ? 8.203   6.906   -11.383 1.00 37.79  ? 109 ALA   B CB  1 
ATOM   1681 N N   . GLY   B 1 93  ? 7.020   8.695   -8.872  1.00 41.66  ? 110 GLY   B N   1 
ATOM   1682 C CA  . GLY   B 1 93  ? 6.508   8.705   -7.520  1.00 44.70  ? 110 GLY   B CA  1 
ATOM   1683 C C   . GLY   B 1 93  ? 5.656   9.936   -7.287  1.00 50.71  ? 110 GLY   B C   1 
ATOM   1684 O O   . GLY   B 1 93  ? 5.197   10.576  -8.228  1.00 42.19  ? 110 GLY   B O   1 
ATOM   1685 N N   . VAL   B 1 94  ? 5.460   10.248  -6.010  1.00 50.59  ? 111 VAL   B N   1 
ATOM   1686 C CA  . VAL   B 1 94  ? 4.610   11.354  -5.589  1.00 49.18  ? 111 VAL   B CA  1 
ATOM   1687 C C   . VAL   B 1 94  ? 5.503   12.546  -5.273  1.00 52.35  ? 111 VAL   B C   1 
ATOM   1688 O O   . VAL   B 1 94  ? 6.340   12.486  -4.364  1.00 54.77  ? 111 VAL   B O   1 
ATOM   1689 C CB  . VAL   B 1 94  ? 3.747   10.968  -4.377  1.00 47.99  ? 111 VAL   B CB  1 
ATOM   1690 C CG1 . VAL   B 1 94  ? 3.168   12.210  -3.716  1.00 47.73  ? 111 VAL   B CG1 1 
ATOM   1691 C CG2 . VAL   B 1 94  ? 2.638   10.013  -4.800  1.00 45.53  ? 111 VAL   B CG2 1 
ATOM   1692 N N   . TYR   B 1 95  ? 5.326   13.626  -6.026  1.00 48.06  ? 112 TYR   B N   1 
ATOM   1693 C CA  . TYR   B 1 95  ? 6.038   14.874  -5.803  1.00 46.51  ? 112 TYR   B CA  1 
ATOM   1694 C C   . TYR   B 1 95  ? 5.181   15.805  -4.957  1.00 44.67  ? 112 TYR   B C   1 
ATOM   1695 O O   . TYR   B 1 95  ? 3.952   15.710  -4.954  1.00 46.61  ? 112 TYR   B O   1 
ATOM   1696 C CB  . TYR   B 1 95  ? 6.396   15.553  -7.128  1.00 45.83  ? 112 TYR   B CB  1 
ATOM   1697 C CG  . TYR   B 1 95  ? 7.468   14.836  -7.919  1.00 46.24  ? 112 TYR   B CG  1 
ATOM   1698 C CD1 . TYR   B 1 95  ? 7.220   13.602  -8.504  1.00 50.32  ? 112 TYR   B CD1 1 
ATOM   1699 C CD2 . TYR   B 1 95  ? 8.728   15.395  -8.082  1.00 48.05  ? 112 TYR   B CD2 1 
ATOM   1700 C CE1 . TYR   B 1 95  ? 8.195   12.944  -9.227  1.00 51.91  ? 112 TYR   B CE1 1 
ATOM   1701 C CE2 . TYR   B 1 95  ? 9.710   14.744  -8.805  1.00 49.83  ? 112 TYR   B CE2 1 
ATOM   1702 C CZ  . TYR   B 1 95  ? 9.438   13.520  -9.374  1.00 50.71  ? 112 TYR   B CZ  1 
ATOM   1703 O OH  . TYR   B 1 95  ? 10.413  12.867  -10.094 1.00 50.72  ? 112 TYR   B OH  1 
ATOM   1704 N N   . ARG   B 1 96  ? 5.840   16.702  -4.228  1.00 43.14  ? 113 ARG   B N   1 
ATOM   1705 C CA  . ARG   B 1 96  ? 5.156   17.643  -3.350  1.00 43.35  ? 113 ARG   B CA  1 
ATOM   1706 C C   . ARG   B 1 96  ? 5.716   19.038  -3.575  1.00 45.00  ? 113 ARG   B C   1 
ATOM   1707 O O   . ARG   B 1 96  ? 6.924   19.257  -3.430  1.00 37.83  ? 113 ARG   B O   1 
ATOM   1708 C CB  . ARG   B 1 96  ? 5.296   17.235  -1.880  1.00 45.07  ? 113 ARG   B CB  1 
ATOM   1709 C CG  . ARG   B 1 96  ? 4.125   16.413  -1.359  1.00 48.29  ? 113 ARG   B CG  1 
ATOM   1710 C CD  . ARG   B 1 96  ? 4.265   16.092  0.121   1.00 47.77  ? 113 ARG   B CD  1 
ATOM   1711 N NE  . ARG   B 1 96  ? 3.326   15.056  0.537   1.00 48.18  ? 113 ARG   B NE  1 
ATOM   1712 C CZ  . ARG   B 1 96  ? 2.942   14.847  1.789   1.00 50.14  ? 113 ARG   B CZ  1 
ATOM   1713 N NH1 . ARG   B 1 96  ? 3.391   15.595  2.784   1.00 46.75  ? 113 ARG   B NH1 1 
ATOM   1714 N NH2 . ARG   B 1 96  ? 2.082   13.867  2.050   1.00 51.88  ? 113 ARG   B NH2 1 
ATOM   1715 N N   . CYS   B 1 97  ? 4.838   19.974  -3.921  1.00 53.75  ? 114 CYS   B N   1 
ATOM   1716 C CA  . CYS   B 1 97  ? 5.185   21.382  -4.059  1.00 56.68  ? 114 CYS   B CA  1 
ATOM   1717 C C   . CYS   B 1 97  ? 4.669   22.128  -2.837  1.00 55.58  ? 114 CYS   B C   1 
ATOM   1718 O O   . CYS   B 1 97  ? 3.459   22.158  -2.593  1.00 51.72  ? 114 CYS   B O   1 
ATOM   1719 C CB  . CYS   B 1 97  ? 4.579   21.965  -5.337  1.00 60.57  ? 114 CYS   B CB  1 
ATOM   1720 S SG  . CYS   B 1 97  ? 4.461   23.771  -5.347  1.00 79.84  ? 114 CYS   B SG  1 
ATOM   1721 N N   . MET   B 1 98  ? 5.581   22.737  -2.084  1.00 56.57  ? 115 MET   B N   1 
ATOM   1722 C CA  . MET   B 1 98  ? 5.244   23.470  -0.870  1.00 54.34  ? 115 MET   B CA  1 
ATOM   1723 C C   . MET   B 1 98  ? 5.676   24.919  -1.037  1.00 53.70  ? 115 MET   B C   1 
ATOM   1724 O O   . MET   B 1 98  ? 6.857   25.194  -1.274  1.00 57.68  ? 115 MET   B O   1 
ATOM   1725 C CB  . MET   B 1 98  ? 5.916   22.842  0.353   1.00 53.41  ? 115 MET   B CB  1 
ATOM   1726 C CG  . MET   B 1 98  ? 6.001   21.323  0.296   1.00 58.11  ? 115 MET   B CG  1 
ATOM   1727 S SD  . MET   B 1 98  ? 6.632   20.589  1.818   1.00 54.32  ? 115 MET   B SD  1 
ATOM   1728 C CE  . MET   B 1 98  ? 7.355   19.078  1.186   1.00 58.08  ? 115 MET   B CE  1 
ATOM   1729 N N   . ILE   B 1 99  ? 4.722   25.838  -0.912  1.00 59.35  ? 116 ILE   B N   1 
ATOM   1730 C CA  . ILE   B 1 99  ? 4.961   27.261  -1.118  1.00 52.84  ? 116 ILE   B CA  1 
ATOM   1731 C C   . ILE   B 1 99  ? 4.458   28.027  0.096   1.00 49.53  ? 116 ILE   B C   1 
ATOM   1732 O O   . ILE   B 1 99  ? 3.370   27.747  0.612   1.00 53.47  ? 116 ILE   B O   1 
ATOM   1733 C CB  . ILE   B 1 99  ? 4.278   27.777  -2.403  1.00 50.57  ? 116 ILE   B CB  1 
ATOM   1734 C CG1 . ILE   B 1 99  ? 4.702   26.940  -3.611  1.00 52.96  ? 116 ILE   B CG1 1 
ATOM   1735 C CG2 . ILE   B 1 99  ? 4.602   29.246  -2.632  1.00 55.69  ? 116 ILE   B CG2 1 
ATOM   1736 C CD1 . ILE   B 1 99  ? 4.095   27.404  -4.915  1.00 57.09  ? 116 ILE   B CD1 1 
ATOM   1737 N N   . SER   B 1 100 ? 5.255   28.988  0.557   1.00 52.08  ? 117 SER   B N   1 
ATOM   1738 C CA  . SER   B 1 100 ? 4.849   29.907  1.615   1.00 59.19  ? 117 SER   B CA  1 
ATOM   1739 C C   . SER   B 1 100 ? 5.082   31.323  1.111   1.00 58.68  ? 117 SER   B C   1 
ATOM   1740 O O   . SER   B 1 100 ? 6.231   31.765  1.004   1.00 59.66  ? 117 SER   B O   1 
ATOM   1741 C CB  . SER   B 1 100 ? 5.623   29.649  2.908   1.00 56.26  ? 117 SER   B CB  1 
ATOM   1742 O OG  . SER   B 1 100 ? 5.028   30.324  4.004   1.00 53.19  ? 117 SER   B OG  1 
ATOM   1743 N N   . TYR   B 1 101 ? 3.979   31.993  0.765   1.00 55.62  ? 118 TYR   B N   1 
ATOM   1744 C CA  . TYR   B 1 101 ? 4.034   33.370  0.307   1.00 65.59  ? 118 TYR   B CA  1 
ATOM   1745 C C   . TYR   B 1 101 ? 2.766   34.052  0.754   1.00 61.77  ? 118 TYR   B C   1 
ATOM   1746 O O   . TYR   B 1 101 ? 1.808   34.128  0.006   1.00 62.31  ? 118 TYR   B O   1 
ATOM   1747 C CB  . TYR   B 1 101 ? 4.123   33.457  -1.194  1.00 64.74  ? 118 TYR   B CB  1 
ATOM   1748 C CG  . TYR   B 1 101 ? 4.306   34.859  -1.658  1.00 60.76  ? 118 TYR   B CG  1 
ATOM   1749 C CD1 . TYR   B 1 101 ? 5.311   35.641  -1.130  1.00 69.30  ? 118 TYR   B CD1 1 
ATOM   1750 C CD2 . TYR   B 1 101 ? 3.464   35.413  -2.600  1.00 58.02  ? 118 TYR   B CD2 1 
ATOM   1751 C CE1 . TYR   B 1 101 ? 5.488   36.937  -1.539  1.00 65.47  ? 118 TYR   B CE1 1 
ATOM   1752 C CE2 . TYR   B 1 101 ? 3.633   36.711  -3.018  1.00 69.59  ? 118 TYR   B CE2 1 
ATOM   1753 C CZ  . TYR   B 1 101 ? 4.649   37.464  -2.480  1.00 70.36  ? 118 TYR   B CZ  1 
ATOM   1754 O OH  . TYR   B 1 101 ? 4.827   38.756  -2.877  1.00 82.17  ? 118 TYR   B OH  1 
ATOM   1755 N N   . GLY   B 1 102 ? 2.751   34.563  1.972   1.00 56.72  ? 119 GLY   B N   1 
ATOM   1756 C CA  . GLY   B 1 102 ? 1.528   35.144  2.486   1.00 56.56  ? 119 GLY   B CA  1 
ATOM   1757 C C   . GLY   B 1 102 ? 0.545   34.039  2.803   1.00 63.16  ? 119 GLY   B C   1 
ATOM   1758 O O   . GLY   B 1 102 ? -0.612  34.072  2.376   1.00 68.02  ? 119 GLY   B O   1 
ATOM   1759 N N   . GLY   B 1 103 ? 1.014   33.046  3.544   1.00 66.35  ? 120 GLY   B N   1 
ATOM   1760 C CA  . GLY   B 1 103 ? 0.273   31.863  3.902   1.00 66.57  ? 120 GLY   B CA  1 
ATOM   1761 C C   . GLY   B 1 103 ? 1.095   30.644  3.568   1.00 70.71  ? 120 GLY   B C   1 
ATOM   1762 O O   . GLY   B 1 103 ? 2.292   30.733  3.278   1.00 71.48  ? 120 GLY   B O   1 
ATOM   1763 N N   . ALA   B 1 104 ? 0.459   29.477  3.609   1.00 61.18  ? 121 ALA   B N   1 
ATOM   1764 C CA  . ALA   B 1 104 ? 1.169   28.243  3.312   1.00 57.85  ? 121 ALA   B CA  1 
ATOM   1765 C C   . ALA   B 1 104 ? 0.195   27.195  2.797   1.00 60.84  ? 121 ALA   B C   1 
ATOM   1766 O O   . ALA   B 1 104 ? -0.915  27.062  3.318   1.00 57.38  ? 121 ALA   B O   1 
ATOM   1767 C CB  . ALA   B 1 104 ? 1.909   27.719  4.545   1.00 56.28  ? 121 ALA   B CB  1 
ATOM   1768 N N   . ASP   B 1 105 ? 0.615   26.466  1.767   1.00 57.88  ? 122 ASP   B N   1 
ATOM   1769 C CA  . ASP   B 1 105 ? -0.161  25.350  1.243   1.00 56.95  ? 122 ASP   B CA  1 
ATOM   1770 C C   . ASP   B 1 105 ? 0.777   24.441  0.462   1.00 55.84  ? 122 ASP   B C   1 
ATOM   1771 O O   . ASP   B 1 105 ? 1.897   24.822  0.114   1.00 57.29  ? 122 ASP   B O   1 
ATOM   1772 C CB  . ASP   B 1 105 ? -1.318  25.837  0.364   1.00 54.50  ? 122 ASP   B CB  1 
ATOM   1773 C CG  . ASP   B 1 105 ? -2.383  24.778  0.160   1.00 54.67  ? 122 ASP   B CG  1 
ATOM   1774 O OD1 . ASP   B 1 105 ? -2.485  23.865  1.006   1.00 58.96  ? 122 ASP   B OD1 1 
ATOM   1775 O OD2 . ASP   B 1 105 ? -3.117  24.857  -0.848  1.00 49.50  ? 122 ASP   B OD2 1 
ATOM   1776 N N   . TYR   B 1 106 ? 0.301   23.227  0.188   1.00 51.94  ? 123 TYR   B N   1 
ATOM   1777 C CA  . TYR   B 1 106 ? 1.070   22.265  -0.587  1.00 49.30  ? 123 TYR   B CA  1 
ATOM   1778 C C   . TYR   B 1 106 ? 0.113   21.359  -1.346  1.00 47.11  ? 123 TYR   B C   1 
ATOM   1779 O O   . TYR   B 1 106 ? -1.023  21.132  -0.920  1.00 43.96  ? 123 TYR   B O   1 
ATOM   1780 C CB  . TYR   B 1 106 ? 2.020   21.448  0.306   1.00 51.67  ? 123 TYR   B CB  1 
ATOM   1781 C CG  . TYR   B 1 106 ? 1.439   20.175  0.888   1.00 47.67  ? 123 TYR   B CG  1 
ATOM   1782 C CD1 . TYR   B 1 106 ? 1.484   18.974  0.184   1.00 45.45  ? 123 TYR   B CD1 1 
ATOM   1783 C CD2 . TYR   B 1 106 ? 0.856   20.170  2.148   1.00 49.99  ? 123 TYR   B CD2 1 
ATOM   1784 C CE1 . TYR   B 1 106 ? 0.957   17.812  0.716   1.00 41.66  ? 123 TYR   B CE1 1 
ATOM   1785 C CE2 . TYR   B 1 106 ? 0.328   19.011  2.688   1.00 55.17  ? 123 TYR   B CE2 1 
ATOM   1786 C CZ  . TYR   B 1 106 ? 0.381   17.836  1.968   1.00 44.04  ? 123 TYR   B CZ  1 
ATOM   1787 O OH  . TYR   B 1 106 ? -0.145  16.683  2.504   1.00 45.71  ? 123 TYR   B OH  1 
ATOM   1788 N N   . LYS   B 1 107 ? 0.588   20.841  -2.477  1.00 38.24  ? 124 LYS   B N   1 
ATOM   1789 C CA  . LYS   B 1 107 ? -0.172  19.912  -3.300  1.00 43.33  ? 124 LYS   B CA  1 
ATOM   1790 C C   . LYS   B 1 107 ? 0.766   18.843  -3.840  1.00 44.17  ? 124 LYS   B C   1 
ATOM   1791 O O   . LYS   B 1 107 ? 1.960   19.084  -4.032  1.00 40.65  ? 124 LYS   B O   1 
ATOM   1792 C CB  . LYS   B 1 107 ? -0.885  20.624  -4.459  1.00 43.76  ? 124 LYS   B CB  1 
ATOM   1793 C CG  . LYS   B 1 107 ? -1.860  21.717  -4.037  1.00 41.16  ? 124 LYS   B CG  1 
ATOM   1794 C CD  . LYS   B 1 107 ? -3.286  21.193  -3.968  1.00 41.91  ? 124 LYS   B CD  1 
ATOM   1795 C CE  . LYS   B 1 107 ? -4.158  22.065  -3.075  1.00 39.91  ? 124 LYS   B CE  1 
ATOM   1796 N NZ  . LYS   B 1 107 ? -4.071  21.673  -1.641  1.00 39.58  ? 124 LYS   B NZ  1 
ATOM   1797 N N   . ARG   B 1 108 ? 0.215   17.656  -4.083  1.00 51.15  ? 125 ARG   B N   1 
ATOM   1798 C CA  . ARG   B 1 108 ? 0.990   16.511  -4.539  1.00 47.23  ? 125 ARG   B CA  1 
ATOM   1799 C C   . ARG   B 1 108 ? 0.733   16.242  -6.017  1.00 46.44  ? 125 ARG   B C   1 
ATOM   1800 O O   . ARG   B 1 108 ? -0.385  16.427  -6.508  1.00 51.33  ? 125 ARG   B O   1 
ATOM   1801 C CB  . ARG   B 1 108 ? 0.658   15.259  -3.723  1.00 50.40  ? 125 ARG   B CB  1 
ATOM   1802 C CG  . ARG   B 1 108 ? 0.191   15.539  -2.305  1.00 54.30  ? 125 ARG   B CG  1 
ATOM   1803 C CD  . ARG   B 1 108 ? -0.608  14.366  -1.768  1.00 60.11  ? 125 ARG   B CD  1 
ATOM   1804 N NE  . ARG   B 1 108 ? -1.392  13.731  -2.820  1.00 66.36  ? 125 ARG   B NE  1 
ATOM   1805 C CZ  . ARG   B 1 108 ? -2.031  12.577  -2.687  1.00 69.43  ? 125 ARG   B CZ  1 
ATOM   1806 N NH1 . ARG   B 1 108 ? -2.000  11.895  -1.553  1.00 69.60  ? 125 ARG   B NH1 1 
ATOM   1807 N NH2 . ARG   B 1 108 ? -2.718  12.093  -3.719  1.00 64.40  ? 125 ARG   B NH2 1 
ATOM   1808 N N   . ILE   B 1 109 ? 1.779   15.807  -6.718  1.00 37.62  ? 126 ILE   B N   1 
ATOM   1809 C CA  . ILE   B 1 109 ? 1.713   15.469  -8.134  1.00 39.56  ? 126 ILE   B CA  1 
ATOM   1810 C C   . ILE   B 1 109 ? 2.355   14.102  -8.333  1.00 41.75  ? 126 ILE   B C   1 
ATOM   1811 O O   . ILE   B 1 109 ? 3.390   13.800  -7.728  1.00 44.27  ? 126 ILE   B O   1 
ATOM   1812 C CB  . ILE   B 1 109 ? 2.410   16.542  -9.001  1.00 40.92  ? 126 ILE   B CB  1 
ATOM   1813 C CG1 . ILE   B 1 109 ? 1.607   17.844  -8.988  1.00 48.87  ? 126 ILE   B CG1 1 
ATOM   1814 C CG2 . ILE   B 1 109 ? 2.591   16.057  -10.427 1.00 42.44  ? 126 ILE   B CG2 1 
ATOM   1815 C CD1 . ILE   B 1 109 ? 2.444   19.073  -8.708  1.00 44.93  ? 126 ILE   B CD1 1 
ATOM   1816 N N   . THR   B 1 110 ? 1.742   13.275  -9.176  1.00 39.37  ? 127 THR   B N   1 
ATOM   1817 C CA  . THR   B 1 110 ? 2.221   11.927  -9.453  1.00 42.91  ? 127 THR   B CA  1 
ATOM   1818 C C   . THR   B 1 110 ? 2.822   11.873  -10.852 1.00 42.81  ? 127 THR   B C   1 
ATOM   1819 O O   . THR   B 1 110 ? 2.205   12.341  -11.814 1.00 42.09  ? 127 THR   B O   1 
ATOM   1820 C CB  . THR   B 1 110 ? 1.086   10.907  -9.323  1.00 41.89  ? 127 THR   B CB  1 
ATOM   1821 O OG1 . THR   B 1 110 ? 0.848   10.633  -7.937  1.00 45.67  ? 127 THR   B OG1 1 
ATOM   1822 C CG2 . THR   B 1 110 ? 1.449   9.604   -10.025 1.00 37.03  ? 127 THR   B CG2 1 
ATOM   1823 N N   . VAL   B 1 111 ? 4.025   11.313  -10.958 1.00 37.99  ? 128 VAL   B N   1 
ATOM   1824 C CA  . VAL   B 1 111 ? 4.740   11.191  -12.224 1.00 39.45  ? 128 VAL   B CA  1 
ATOM   1825 C C   . VAL   B 1 111 ? 4.872   9.712   -12.568 1.00 40.82  ? 128 VAL   B C   1 
ATOM   1826 O O   . VAL   B 1 111 ? 5.349   8.917   -11.748 1.00 37.33  ? 128 VAL   B O   1 
ATOM   1827 C CB  . VAL   B 1 111 ? 6.122   11.866  -12.159 1.00 43.03  ? 128 VAL   B CB  1 
ATOM   1828 C CG1 . VAL   B 1 111 ? 6.959   11.494  -13.375 1.00 37.94  ? 128 VAL   B CG1 1 
ATOM   1829 C CG2 . VAL   B 1 111 ? 5.968   13.377  -12.053 1.00 42.70  ? 128 VAL   B CG2 1 
ATOM   1830 N N   . LYS   B 1 112 ? 4.444   9.346   -13.773 1.00 37.74  ? 129 LYS   B N   1 
ATOM   1831 C CA  . LYS   B 1 112 ? 4.625   8.005   -14.311 1.00 37.93  ? 129 LYS   B CA  1 
ATOM   1832 C C   . LYS   B 1 112 ? 5.651   8.054   -15.434 1.00 45.44  ? 129 LYS   B C   1 
ATOM   1833 O O   . LYS   B 1 112 ? 5.627   8.965   -16.268 1.00 47.78  ? 129 LYS   B O   1 
ATOM   1834 C CB  . LYS   B 1 112 ? 3.305   7.430   -14.831 1.00 41.11  ? 129 LYS   B CB  1 
ATOM   1835 C CG  . LYS   B 1 112 ? 2.214   7.314   -13.778 1.00 40.87  ? 129 LYS   B CG  1 
ATOM   1836 C CD  . LYS   B 1 112 ? 2.543   6.243   -12.752 1.00 37.75  ? 129 LYS   B CD  1 
ATOM   1837 C CE  . LYS   B 1 112 ? 1.282   5.692   -12.108 1.00 37.81  ? 129 LYS   B CE  1 
ATOM   1838 N NZ  . LYS   B 1 112 ? 1.333   5.785   -10.623 1.00 37.99  ? 129 LYS   B NZ  1 
ATOM   1839 N N   . VAL   B 1 113 ? 6.551   7.074   -15.457 1.00 45.00  ? 130 VAL   B N   1 
ATOM   1840 C CA  . VAL   B 1 113 ? 7.678   7.062   -16.384 1.00 47.35  ? 130 VAL   B CA  1 
ATOM   1841 C C   . VAL   B 1 113 ? 7.601   5.794   -17.223 1.00 46.77  ? 130 VAL   B C   1 
ATOM   1842 O O   . VAL   B 1 113 ? 7.822   4.688   -16.713 1.00 47.34  ? 130 VAL   B O   1 
ATOM   1843 C CB  . VAL   B 1 113 ? 9.024   7.152   -15.653 1.00 47.96  ? 130 VAL   B CB  1 
ATOM   1844 C CG1 . VAL   B 1 113 ? 10.168  7.213   -16.653 1.00 51.69  ? 130 VAL   B CG1 1 
ATOM   1845 C CG2 . VAL   B 1 113 ? 9.049   8.362   -14.731 1.00 41.68  ? 130 VAL   B CG2 1 
ATOM   1846 N N   . ASN   B 1 114 ? 7.288   5.951   -18.506 1.00 48.70  ? 131 ASN   B N   1 
ATOM   1847 C CA  . ASN   B 1 114 ? 7.418   4.864   -19.464 1.00 43.71  ? 131 ASN   B CA  1 
ATOM   1848 C C   . ASN   B 1 114 ? 8.860   4.770   -19.949 1.00 46.97  ? 131 ASN   B C   1 
ATOM   1849 O O   . ASN   B 1 114 ? 9.572   5.774   -20.040 1.00 53.61  ? 131 ASN   B O   1 
ATOM   1850 C CB  . ASN   B 1 114 ? 6.476   5.071   -20.650 1.00 45.97  ? 131 ASN   B CB  1 
ATOM   1851 C CG  . ASN   B 1 114 ? 5.021   5.138   -20.232 1.00 45.04  ? 131 ASN   B CG  1 
ATOM   1852 O OD1 . ASN   B 1 114 ? 4.608   4.489   -19.272 1.00 39.80  ? 131 ASN   B OD1 1 
ATOM   1853 N ND2 . ASN   B 1 114 ? 4.233   5.928   -20.955 1.00 44.73  ? 131 ASN   B ND2 1 
ATOM   1854 N N   . ALA   B 1 115 ? 9.291   3.550   -20.260 1.00 47.16  ? 132 ALA   B N   1 
ATOM   1855 C CA  . ALA   B 1 115 ? 10.677  3.319   -20.642 1.00 47.89  ? 132 ALA   B CA  1 
ATOM   1856 C C   . ALA   B 1 115 ? 10.749  2.072   -21.503 1.00 50.72  ? 132 ALA   B C   1 
ATOM   1857 O O   . ALA   B 1 115 ? 9.920   1.167   -21.345 1.00 45.36  ? 132 ALA   B O   1 
ATOM   1858 C CB  . ALA   B 1 115 ? 11.573  3.166   -19.404 1.00 48.91  ? 132 ALA   B CB  1 
ATOM   1859 N N   . PRO   B 1 116 ? 11.710  1.988   -22.420 1.00 54.96  ? 133 PRO   B N   1 
ATOM   1860 C CA  . PRO   B 1 116 ? 11.893  0.756   -23.192 1.00 48.52  ? 133 PRO   B CA  1 
ATOM   1861 C C   . PRO   B 1 116 ? 12.458  -0.350  -22.314 1.00 47.03  ? 133 PRO   B C   1 
ATOM   1862 O O   . PRO   B 1 116 ? 12.803  -0.149  -21.148 1.00 47.67  ? 133 PRO   B O   1 
ATOM   1863 C CB  . PRO   B 1 116 ? 12.878  1.154   -24.298 1.00 47.03  ? 133 PRO   B CB  1 
ATOM   1864 C CG  . PRO   B 1 116 ? 12.920  2.657   -24.279 1.00 52.62  ? 133 PRO   B CG  1 
ATOM   1865 C CD  . PRO   B 1 116 ? 12.606  3.064   -22.877 1.00 47.77  ? 133 PRO   B CD  1 
ATOM   1866 N N   . TYR   B 1 117 ? 12.544  -1.547  -22.901 1.00 51.30  ? 134 TYR   B N   1 
ATOM   1867 C CA  . TYR   B 1 117 ? 12.990  -2.710  -22.139 1.00 49.71  ? 134 TYR   B CA  1 
ATOM   1868 C C   . TYR   B 1 117 ? 14.418  -2.540  -21.635 1.00 51.28  ? 134 TYR   B C   1 
ATOM   1869 O O   . TYR   B 1 117 ? 14.726  -2.905  -20.494 1.00 54.08  ? 134 TYR   B O   1 
ATOM   1870 C CB  . TYR   B 1 117 ? 12.875  -3.977  -22.985 1.00 47.40  ? 134 TYR   B CB  1 
ATOM   1871 C CG  . TYR   B 1 117 ? 13.350  -5.215  -22.257 1.00 53.78  ? 134 TYR   B CG  1 
ATOM   1872 C CD1 . TYR   B 1 117 ? 12.956  -5.466  -20.948 1.00 54.30  ? 134 TYR   B CD1 1 
ATOM   1873 C CD2 . TYR   B 1 117 ? 14.197  -6.127  -22.872 1.00 52.36  ? 134 TYR   B CD2 1 
ATOM   1874 C CE1 . TYR   B 1 117 ? 13.389  -6.589  -20.274 1.00 53.40  ? 134 TYR   B CE1 1 
ATOM   1875 C CE2 . TYR   B 1 117 ? 14.635  -7.257  -22.204 1.00 54.30  ? 134 TYR   B CE2 1 
ATOM   1876 C CZ  . TYR   B 1 117 ? 14.227  -7.482  -20.906 1.00 52.06  ? 134 TYR   B CZ  1 
ATOM   1877 O OH  . TYR   B 1 117 ? 14.658  -8.604  -20.235 1.00 54.96  ? 134 TYR   B OH  1 
ATOM   1878 N N   . ALA   B 1 118 ? 15.306  -2.000  -22.474 1.00 48.82  ? 135 ALA   B N   1 
ATOM   1879 C CA  . ALA   B 1 118 ? 16.713  -1.885  -22.100 1.00 50.09  ? 135 ALA   B CA  1 
ATOM   1880 C C   . ALA   B 1 118 ? 16.884  -1.071  -20.823 1.00 50.55  ? 135 ALA   B C   1 
ATOM   1881 O O   . ALA   B 1 118 ? 17.540  -1.515  -19.874 1.00 51.01  ? 135 ALA   B O   1 
ATOM   1882 C CB  . ALA   B 1 118 ? 17.511  -1.264  -23.247 1.00 46.91  ? 135 ALA   B CB  1 
ATOM   1883 N N   . ALA   B 1 119 ? 16.301  0.129   -20.784 1.00 49.01  ? 136 ALA   B N   1 
ATOM   1884 C CA  . ALA   B 1 119 ? 16.411  0.965   -19.594 1.00 46.34  ? 136 ALA   B CA  1 
ATOM   1885 C C   . ALA   B 1 119 ? 15.718  0.329   -18.395 1.00 50.32  ? 136 ALA   B C   1 
ATOM   1886 O O   . ALA   B 1 119 ? 16.175  0.477   -17.255 1.00 47.53  ? 136 ALA   B O   1 
ATOM   1887 C CB  . ALA   B 1 119 ? 15.834  2.353   -19.873 1.00 48.05  ? 136 ALA   B CB  1 
ATOM   1888 N N   . ALA   B 1 120 ? 14.607  -0.375  -18.629 1.00 51.35  ? 137 ALA   B N   1 
ATOM   1889 C CA  . ALA   B 1 120 ? 13.861  -0.965  -17.521 1.00 50.37  ? 137 ALA   B CA  1 
ATOM   1890 C C   . ALA   B 1 120 ? 14.586  -2.171  -16.933 1.00 54.17  ? 137 ALA   B C   1 
ATOM   1891 O O   . ALA   B 1 120 ? 14.688  -2.305  -15.707 1.00 53.42  ? 137 ALA   B O   1 
ATOM   1892 C CB  . ALA   B 1 120 ? 12.457  -1.353  -17.984 1.00 49.56  ? 137 ALA   B CB  1 
ATOM   1893 N N   . LEU   B 1 121 ? 15.089  -3.066  -17.789 1.00 54.77  ? 138 LEU   B N   1 
ATOM   1894 C CA  . LEU   B 1 121 ? 15.872  -4.195  -17.293 1.00 55.40  ? 138 LEU   B CA  1 
ATOM   1895 C C   . LEU   B 1 121 ? 17.110  -3.715  -16.550 1.00 54.50  ? 138 LEU   B C   1 
ATOM   1896 O O   . LEU   B 1 121 ? 17.492  -4.289  -15.523 1.00 58.23  ? 138 LEU   B O   1 
ATOM   1897 C CB  . LEU   B 1 121 ? 16.270  -5.114  -18.449 1.00 50.25  ? 138 LEU   B CB  1 
ATOM   1898 C CG  . LEU   B 1 121 ? 17.201  -6.285  -18.111 1.00 54.11  ? 138 LEU   B CG  1 
ATOM   1899 C CD1 . LEU   B 1 121 ? 16.685  -7.086  -16.918 1.00 61.19  ? 138 LEU   B CD1 1 
ATOM   1900 C CD2 . LEU   B 1 121 ? 17.412  -7.183  -19.322 1.00 55.02  ? 138 LEU   B CD2 1 
ATOM   1901 N N   . GLU   B 1 122 ? 17.744  -2.656  -17.052 1.00 47.69  ? 139 GLU   B N   1 
ATOM   1902 C CA  . GLU   B 1 122 ? 18.902  -2.096  -16.370 1.00 47.62  ? 139 GLU   B CA  1 
ATOM   1903 C C   . GLU   B 1 122 ? 18.505  -1.514  -15.020 1.00 54.37  ? 139 GLU   B C   1 
ATOM   1904 O O   . GLU   B 1 122 ? 19.245  -1.641  -14.039 1.00 50.56  ? 139 GLU   B O   1 
ATOM   1905 C CB  . GLU   B 1 122 ? 19.557  -1.038  -17.254 1.00 53.01  ? 139 GLU   B CB  1 
ATOM   1906 C CG  . GLU   B 1 122 ? 20.834  -0.451  -16.698 1.00 59.15  ? 139 GLU   B CG  1 
ATOM   1907 C CD  . GLU   B 1 122 ? 21.588  0.347   -17.738 1.00 64.60  ? 139 GLU   B CD  1 
ATOM   1908 O OE1 . GLU   B 1 122 ? 22.149  -0.265  -18.672 1.00 60.03  ? 139 GLU   B OE1 1 
ATOM   1909 O OE2 . GLU   B 1 122 ? 21.607  1.589   -17.627 1.00 68.71  ? 139 GLU   B OE2 1 
ATOM   1910 N N   . HIS   B 1 123 ? 17.345  -0.854  -14.960 1.00 60.28  ? 140 HIS   B N   1 
ATOM   1911 C CA  . HIS   B 1 123 ? 16.825  -0.355  -13.692 1.00 55.01  ? 140 HIS   B CA  1 
ATOM   1912 C C   . HIS   B 1 123 ? 16.338  -1.487  -12.795 1.00 66.31  ? 140 HIS   B C   1 
ATOM   1913 O O   . HIS   B 1 123 ? 16.396  -1.367  -11.565 1.00 67.11  ? 140 HIS   B O   1 
ATOM   1914 C CB  . HIS   B 1 123 ? 15.697  0.646   -13.946 1.00 52.96  ? 140 HIS   B CB  1 
ATOM   1915 C CG  . HIS   B 1 123 ? 14.942  1.033   -12.712 1.00 60.89  ? 140 HIS   B CG  1 
ATOM   1916 N ND1 . HIS   B 1 123 ? 15.361  2.039   -11.869 1.00 60.06  ? 140 HIS   B ND1 1 
ATOM   1917 C CD2 . HIS   B 1 123 ? 13.795  0.550   -12.181 1.00 59.18  ? 140 HIS   B CD2 1 
ATOM   1918 C CE1 . HIS   B 1 123 ? 14.505  2.158   -10.870 1.00 59.77  ? 140 HIS   B CE1 1 
ATOM   1919 N NE2 . HIS   B 1 123 ? 13.545  1.266   -11.035 1.00 54.68  ? 140 HIS   B NE2 1 
ATOM   1920 N N   . HIS   B 1 124 ? 15.862  -2.590  -13.384 1.00 68.26  ? 141 HIS   B N   1 
ATOM   1921 C CA  . HIS   B 1 124 ? 15.370  -3.704  -12.577 1.00 68.98  ? 141 HIS   B CA  1 
ATOM   1922 C C   . HIS   B 1 124 ? 16.492  -4.356  -11.782 1.00 71.44  ? 141 HIS   B C   1 
ATOM   1923 O O   . HIS   B 1 124 ? 16.241  -4.949  -10.726 1.00 71.91  ? 141 HIS   B O   1 
ATOM   1924 C CB  . HIS   B 1 124 ? 14.679  -4.732  -13.473 1.00 69.96  ? 141 HIS   B CB  1 
ATOM   1925 C CG  . HIS   B 1 124 ? 14.062  -5.871  -12.722 1.00 72.04  ? 141 HIS   B CG  1 
ATOM   1926 N ND1 . HIS   B 1 124 ? 13.205  -5.685  -11.659 1.00 70.16  ? 141 HIS   B ND1 1 
ATOM   1927 C CD2 . HIS   B 1 124 ? 14.175  -7.211  -12.884 1.00 71.37  ? 141 HIS   B CD2 1 
ATOM   1928 C CE1 . HIS   B 1 124 ? 12.819  -6.860  -11.196 1.00 71.90  ? 141 HIS   B CE1 1 
ATOM   1929 N NE2 . HIS   B 1 124 ? 13.392  -7.803  -11.922 1.00 69.69  ? 141 HIS   B NE2 1 
ATOM   1930 N N   . HIS   B 1 125 ? 17.724  -4.257  -12.265 1.00 72.03  ? 142 HIS   B N   1 
ATOM   1931 C CA  . HIS   B 1 125 ? 18.904  -4.620  -11.499 1.00 73.85  ? 142 HIS   B CA  1 
ATOM   1932 C C   . HIS   B 1 125 ? 19.557  -3.346  -10.979 1.00 82.80  ? 142 HIS   B C   1 
ATOM   1933 O O   . HIS   B 1 125 ? 19.243  -2.239  -11.426 1.00 80.97  ? 142 HIS   B O   1 
ATOM   1934 C CB  . HIS   B 1 125 ? 19.899  -5.415  -12.349 1.00 75.22  ? 142 HIS   B CB  1 
ATOM   1935 C CG  . HIS   B 1 125 ? 19.300  -6.602  -13.038 1.00 82.28  ? 142 HIS   B CG  1 
ATOM   1936 N ND1 . HIS   B 1 125 ? 18.307  -7.372  -12.471 1.00 81.63  ? 142 HIS   B ND1 1 
ATOM   1937 C CD2 . HIS   B 1 125 ? 19.562  -7.157  -14.245 1.00 79.77  ? 142 HIS   B CD2 1 
ATOM   1938 C CE1 . HIS   B 1 125 ? 17.980  -8.347  -13.301 1.00 76.33  ? 142 HIS   B CE1 1 
ATOM   1939 N NE2 . HIS   B 1 125 ? 18.727  -8.239  -14.385 1.00 79.78  ? 142 HIS   B NE2 1 
ATOM   1940 N N   . HIS   B 1 126 ? 20.461  -3.510  -10.017 1.00 88.03  ? 143 HIS   B N   1 
ATOM   1941 C CA  . HIS   B 1 126 ? 21.245  -2.386  -9.507  1.00 96.80  ? 143 HIS   B CA  1 
ATOM   1942 C C   . HIS   B 1 126 ? 20.366  -1.230  -9.026  1.00 92.74  ? 143 HIS   B C   1 
ATOM   1943 O O   . HIS   B 1 126 ? 20.308  -0.928  -7.835  1.00 97.95  ? 143 HIS   B O   1 
ATOM   1944 C CB  . HIS   B 1 126 ? 22.213  -1.897  -10.589 1.00 94.96  ? 143 HIS   B CB  1 
ATOM   1945 C CG  . HIS   B 1 126 ? 23.044  -0.723  -10.177 1.00 103.20 ? 143 HIS   B CG  1 
ATOM   1946 N ND1 . HIS   B 1 126 ? 23.769  -0.697  -9.005  1.00 110.42 ? 143 HIS   B ND1 1 
ATOM   1947 C CD2 . HIS   B 1 126 ? 23.269  0.465   -10.785 1.00 101.80 ? 143 HIS   B CD2 1 
ATOM   1948 C CE1 . HIS   B 1 126 ? 24.404  0.458   -8.908  1.00 108.40 ? 143 HIS   B CE1 1 
ATOM   1949 N NE2 . HIS   B 1 126 ? 24.117  1.181   -9.976  1.00 105.44 ? 143 HIS   B NE2 1 
HETATM 1950 C C10 . A1D9R C 2 .   ? 2.242   24.817  6.494   1.00 49.28  ? 201 A1D9R B C10 1 
HETATM 1951 C C13 . A1D9R C 2 .   ? 3.610   23.500  3.211   1.00 51.87  ? 201 A1D9R B C13 1 
HETATM 1952 C C15 . A1D9R C 2 .   ? -0.128  23.621  4.790   1.00 54.74  ? 201 A1D9R B C15 1 
HETATM 1953 C C17 . A1D9R C 2 .   ? -2.282  23.025  4.175   1.00 63.86  ? 201 A1D9R B C17 1 
HETATM 1954 C C21 . A1D9R C 2 .   ? -2.420  26.285  6.022   1.00 64.81  ? 201 A1D9R B C21 1 
HETATM 1955 C C24 . A1D9R C 2 .   ? -4.546  26.609  3.671   1.00 68.33  ? 201 A1D9R B C24 1 
HETATM 1956 C C01 . A1D9R C 2 .   ? 8.069   25.377  2.777   1.00 47.85  ? 201 A1D9R B C01 1 
HETATM 1957 C C02 . A1D9R C 2 .   ? 7.982   24.476  3.824   1.00 46.40  ? 201 A1D9R B C02 1 
HETATM 1958 C C03 . A1D9R C 2 .   ? 6.808   24.377  4.552   1.00 44.49  ? 201 A1D9R B C03 1 
HETATM 1959 C C04 . A1D9R C 2 .   ? 5.720   25.175  4.233   1.00 42.02  ? 201 A1D9R B C04 1 
HETATM 1960 C C05 . A1D9R C 2 .   ? 5.811   26.081  3.187   1.00 47.12  ? 201 A1D9R B C05 1 
HETATM 1961 C C06 . A1D9R C 2 .   ? 6.985   26.179  2.457   1.00 50.09  ? 201 A1D9R B C06 1 
HETATM 1962 C C07 . A1D9R C 2 .   ? 4.556   25.057  4.978   1.00 44.30  ? 201 A1D9R B C07 1 
HETATM 1963 C C08 . A1D9R C 2 .   ? 4.442   25.730  6.184   1.00 44.21  ? 201 A1D9R B C08 1 
HETATM 1964 C C09 . A1D9R C 2 .   ? 3.287   25.613  6.940   1.00 49.11  ? 201 A1D9R B C09 1 
HETATM 1965 C C11 . A1D9R C 2 .   ? 2.352   24.143  5.286   1.00 48.10  ? 201 A1D9R B C11 1 
HETATM 1966 C C12 . A1D9R C 2 .   ? 3.510   24.258  4.535   1.00 47.04  ? 201 A1D9R B C12 1 
HETATM 1967 C C18 . A1D9R C 2 .   ? -2.746  24.152  4.761   1.00 64.75  ? 201 A1D9R B C18 1 
HETATM 1968 C C19 . A1D9R C 2 .   ? -1.890  25.011  5.363   1.00 63.83  ? 201 A1D9R B C19 1 
HETATM 1969 C C23 . A1D9R C 2 .   ? -4.399  27.272  5.041   1.00 72.75  ? 201 A1D9R B C23 1 
HETATM 1970 C C25 . A1D9R C 2 .   ? -3.489  28.497  4.926   1.00 67.92  ? 201 A1D9R B C25 1 
HETATM 1971 C C30 . A1D9R C 2 .   ? -2.597  20.960  3.091   1.00 53.04  ? 201 A1D9R B C30 1 
HETATM 1972 N N14 . A1D9R C 2 .   ? 1.288   23.289  4.782   1.00 60.08  ? 201 A1D9R B N14 1 
HETATM 1973 N N16 . A1D9R C 2 .   ? -0.988  22.766  4.193   1.00 56.64  ? 201 A1D9R B N16 1 
HETATM 1974 N N20 . A1D9R C 2 .   ? -0.595  24.747  5.375   1.00 60.58  ? 201 A1D9R B N20 1 
HETATM 1975 N N22 . A1D9R C 2 .   ? -3.875  26.303  5.999   1.00 70.49  ? 201 A1D9R B N22 1 
HETATM 1976 O O26 . A1D9R C 2 .   ? -4.105  29.469  4.127   1.00 61.38  ? 201 A1D9R B O26 1 
HETATM 1977 O O27 . A1D9R C 2 .   ? -3.668  26.785  2.788   1.00 65.76  ? 201 A1D9R B O27 1 
HETATM 1978 O O28 . A1D9R C 2 .   ? -5.542  25.879  3.426   1.00 70.95  ? 201 A1D9R B O28 1 
HETATM 1979 O O29 . A1D9R C 2 .   ? -3.178  22.145  3.556   1.00 63.75  ? 201 A1D9R B O29 1 
HETATM 1980 O O   . HOH   D 3 .   ? -1.568  15.362  0.127   1.00 47.86  ? 301 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   . ALA   A 1   ? 1.1590 1.1376 1.4191 -0.1507 0.0642  -0.1288 18  ALA   A N   
2    C CA  . ALA   A 1   ? 1.1693 1.1165 1.4156 -0.1406 0.0673  -0.1195 18  ALA   A CA  
3    C C   . ALA   A 1   ? 1.0723 1.0184 1.3169 -0.1253 0.0610  -0.1186 18  ALA   A C   
4    O O   . ALA   A 1   ? 1.1056 1.0686 1.3560 -0.1242 0.0548  -0.1257 18  ALA   A O   
5    C CB  . ALA   A 1   ? 1.1484 1.0949 1.3960 -0.1352 0.0708  -0.1098 18  ALA   A CB  
6    N N   . PHE   A 2   ? 0.8485 0.7753 1.0846 -0.1136 0.0628  -0.1098 19  PHE   A N   
7    C CA  . PHE   A 2   ? 0.7762 0.7018 1.0102 -0.0995 0.0580  -0.1079 19  PHE   A CA  
8    C C   . PHE   A 2   ? 0.7647 0.7162 1.0103 -0.0905 0.0519  -0.1056 19  PHE   A C   
9    O O   . PHE   A 2   ? 0.7296 0.6853 0.9786 -0.0865 0.0531  -0.0987 19  PHE   A O   
10   C CB  . PHE   A 2   ? 0.6413 0.5406 0.8633 -0.0905 0.0622  -0.0995 19  PHE   A CB  
11   C CG  . PHE   A 2   ? 0.6909 0.5893 0.9104 -0.0771 0.0586  -0.0976 19  PHE   A CG  
12   C CD1 . PHE   A 2   ? 0.6450 0.5563 0.8704 -0.0663 0.0553  -0.0912 19  PHE   A CD1 
13   C CD2 . PHE   A 2   ? 0.6721 0.5560 0.8821 -0.0760 0.0588  -0.1023 19  PHE   A CD2 
14   C CE1 . PHE   A 2   ? 0.6649 0.5761 0.8876 -0.0557 0.0526  -0.0894 19  PHE   A CE1 
15   C CE2 . PHE   A 2   ? 0.6571 0.5413 0.8644 -0.0642 0.0563  -0.1006 19  PHE   A CE2 
16   C CZ  . PHE   A 2   ? 0.6960 0.5945 0.9101 -0.0545 0.0533  -0.0940 19  PHE   A CZ  
17   N N   . THR   A 3   ? 0.6480 0.6150 0.8977 -0.0873 0.0453  -0.1116 20  THR   A N   
18   C CA  . THR   A 3   ? 0.6821 0.6706 0.9397 -0.0784 0.0389  -0.1102 20  THR   A CA  
19   C C   . THR   A 3   ? 0.6289 0.6142 0.8807 -0.0684 0.0342  -0.1102 20  THR   A C   
20   O O   . THR   A 3   ? 0.5500 0.5310 0.7972 -0.0709 0.0326  -0.1166 20  THR   A O   
21   C CB  . THR   A 3   ? 0.6611 0.6763 0.9296 -0.0841 0.0347  -0.1181 20  THR   A CB  
22   O OG1 . THR   A 3   ? 0.6522 0.6746 0.9198 -0.0836 0.0289  -0.1262 20  THR   A OG1 
23   C CG2 . THR   A 3   ? 0.6761 0.6934 0.9488 -0.0987 0.0404  -0.1217 20  THR   A CG2 
24   N N   . VAL   A 4   ? 0.6258 0.6129 0.8769 -0.0581 0.0320  -0.1032 21  VAL   A N   
25   C CA  . VAL   A 4   ? 0.6219 0.6081 0.8673 -0.0493 0.0276  -0.1026 21  VAL   A CA  
26   C C   . VAL   A 4   ? 0.5903 0.5959 0.8395 -0.0466 0.0200  -0.1076 21  VAL   A C   
27   O O   . VAL   A 4   ? 0.5491 0.5687 0.8050 -0.0459 0.0178  -0.1070 21  VAL   A O   
28   C CB  . VAL   A 4   ? 0.5450 0.5239 0.7870 -0.0410 0.0291  -0.0929 21  VAL   A CB  
29   C CG1 . VAL   A 4   ? 0.5708 0.5486 0.8060 -0.0336 0.0255  -0.0923 21  VAL   A CG1 
30   C CG2 . VAL   A 4   ? 0.5110 0.4721 0.7493 -0.0420 0.0362  -0.0881 21  VAL   A CG2 
31   N N   . THR   A 5   ? 0.5698 0.5756 0.8134 -0.0442 0.0157  -0.1127 22  THR   A N   
32   C CA  . THR   A 5   ? 0.5475 0.5698 0.7921 -0.0406 0.0078  -0.1181 22  THR   A CA  
33   C C   . THR   A 5   ? 0.6301 0.6465 0.8643 -0.0310 0.0040  -0.1144 22  THR   A C   
34   O O   . THR   A 5   ? 0.6380 0.6407 0.8643 -0.0298 0.0065  -0.1129 22  THR   A O   
35   C CB  . THR   A 5   ? 0.5343 0.5636 0.7802 -0.0471 0.0051  -0.1286 22  THR   A CB  
36   O OG1 . THR   A 5   ? 0.5956 0.6136 0.8305 -0.0440 0.0035  -0.1306 22  THR   A OG1 
37   C CG2 . THR   A 5   ? 0.7169 0.7414 0.9678 -0.0592 0.0115  -0.1314 22  THR   A CG2 
38   N N   . VAL   A 6   ? 0.6879 0.7139 0.9211 -0.0244 -0.0017 -0.1131 23  VAL   A N   
39   C CA  . VAL   A 6   ? 0.7341 0.7537 0.9554 -0.0163 -0.0057 -0.1096 23  VAL   A CA  
40   C C   . VAL   A 6   ? 0.7533 0.7822 0.9697 -0.0122 -0.0138 -0.1169 23  VAL   A C   
41   O O   . VAL   A 6   ? 0.7663 0.8107 0.9886 -0.0104 -0.0184 -0.1208 23  VAL   A O   
42   C CB  . VAL   A 6   ? 0.7511 0.7695 0.9710 -0.0115 -0.0061 -0.1017 23  VAL   A CB  
43   C CG1 . VAL   A 6   ? 0.7721 0.7880 0.9792 -0.0038 -0.0126 -0.1007 23  VAL   A CG1 
44   C CG2 . VAL   A 6   ? 0.7792 0.7856 0.9986 -0.0132 0.0007  -0.0936 23  VAL   A CG2 
45   N N   . PRO   A 7   ? 0.6268 0.6478 0.8322 -0.0102 -0.0159 -0.1191 24  PRO   A N   
46   C CA  . PRO   A 7   ? 0.6800 0.7092 0.8788 -0.0053 -0.0244 -0.1259 24  PRO   A CA  
47   C C   . PRO   A 7   ? 0.6584 0.6868 0.8469 0.0044  -0.0305 -0.1223 24  PRO   A C   
48   O O   . PRO   A 7   ? 0.5650 0.6022 0.7488 0.0104  -0.0384 -0.1277 24  PRO   A O   
49   C CB  . PRO   A 7   ? 0.6461 0.6636 0.8342 -0.0063 -0.0235 -0.1283 24  PRO   A CB  
50   C CG  . PRO   A 7   ? 0.6430 0.6451 0.8277 -0.0074 -0.0159 -0.1200 24  PRO   A CG  
51   C CD  . PRO   A 7   ? 0.6623 0.6675 0.8604 -0.0116 -0.0105 -0.1159 24  PRO   A CD  
52   N N   . LYS   A 8   ? 0.7214 0.7390 0.9050 0.0064  -0.0275 -0.1135 25  LYS   A N   
53   C CA  . LYS   A 8   ? 0.5725 0.5844 0.7428 0.0146  -0.0328 -0.1096 25  LYS   A CA  
54   C C   . LYS   A 8   ? 0.5848 0.5920 0.7582 0.0136  -0.0287 -0.1016 25  LYS   A C   
55   O O   . LYS   A 8   ? 0.6005 0.5979 0.7733 0.0093  -0.0226 -0.0955 25  LYS   A O   
56   C CB  . LYS   A 8   ? 0.5707 0.5672 0.7222 0.0173  -0.0343 -0.1075 25  LYS   A CB  
57   C CG  . LYS   A 8   ? 0.6556 0.6419 0.7884 0.0253  -0.0403 -0.1041 25  LYS   A CG  
58   C CD  . LYS   A 8   ? 0.6937 0.6641 0.8077 0.0256  -0.0401 -0.1018 25  LYS   A CD  
59   C CE  . LYS   A 8   ? 0.7018 0.6627 0.7942 0.0346  -0.0484 -0.1024 25  LYS   A CE  
60   N NZ  . LYS   A 8   ? 0.6220 0.5691 0.7018 0.0367  -0.0488 -0.0948 25  LYS   A NZ  
61   N N   . ASP   A 9   ? 0.7189 0.7333 0.8946 0.0182  -0.0322 -0.1016 26  ASP   A N   
62   C CA  . ASP   A 9   ? 0.7255 0.7363 0.9040 0.0172  -0.0287 -0.0947 26  ASP   A CA  
63   C C   . ASP   A 9   ? 0.6950 0.6892 0.8552 0.0214  -0.0312 -0.0882 26  ASP   A C   
64   O O   . ASP   A 9   ? 0.6800 0.6688 0.8405 0.0193  -0.0281 -0.0819 26  ASP   A O   
65   C CB  . ASP   A 9   ? 0.7484 0.7748 0.9380 0.0196  -0.0304 -0.0980 26  ASP   A CB  
66   C CG  . ASP   A 9   ? 0.7563 0.7856 0.9353 0.0305  -0.0389 -0.1012 26  ASP   A CG  
67   O OD1 . ASP   A 9   ? 0.7628 0.7884 0.9302 0.0355  -0.0444 -0.1045 26  ASP   A OD1 
68   O OD2 . ASP   A 9   ? 0.8087 0.8432 0.9896 0.0349  -0.0400 -0.1004 26  ASP   A OD2 
69   N N   . LEU   A 10  ? 0.6224 0.6076 0.7655 0.0268  -0.0366 -0.0896 27  LEU   A N   
70   C CA  . LEU   A 10  ? 0.6110 0.5775 0.7335 0.0296  -0.0388 -0.0835 27  LEU   A CA  
71   C C   . LEU   A 10  ? 0.6131 0.5678 0.7206 0.0286  -0.0392 -0.0831 27  LEU   A C   
72   O O   . LEU   A 10  ? 0.5636 0.5221 0.6679 0.0325  -0.0433 -0.0892 27  LEU   A O   
73   C CB  . LEU   A 10  ? 0.6738 0.6373 0.7842 0.0398  -0.0465 -0.0852 27  LEU   A CB  
74   C CG  . LEU   A 10  ? 0.6914 0.6317 0.7777 0.0421  -0.0488 -0.0788 27  LEU   A CG  
75   C CD1 . LEU   A 10  ? 0.6806 0.6181 0.7703 0.0393  -0.0459 -0.0735 27  LEU   A CD1 
76   C CD2 . LEU   A 10  ? 0.6551 0.5865 0.7211 0.0542  -0.0578 -0.0822 27  LEU   A CD2 
77   N N   . TYR   A 11  ? 0.5815 0.5230 0.6799 0.0232  -0.0350 -0.0762 28  TYR   A N   
78   C CA  . TYR   A 11  ? 0.6411 0.5702 0.7229 0.0216  -0.0345 -0.0748 28  TYR   A CA  
79   C C   . TYR   A 11  ? 0.6799 0.5891 0.7376 0.0228  -0.0375 -0.0692 28  TYR   A C   
80   O O   . TYR   A 11  ? 0.6579 0.5625 0.7151 0.0196  -0.0359 -0.0640 28  TYR   A O   
81   C CB  . TYR   A 11  ? 0.5902 0.5221 0.6811 0.0131  -0.0260 -0.0717 28  TYR   A CB  
82   C CG  . TYR   A 11  ? 0.5636 0.5094 0.6729 0.0115  -0.0226 -0.0771 28  TYR   A CG  
83   C CD1 . TYR   A 11  ? 0.5541 0.5123 0.6832 0.0102  -0.0206 -0.0787 28  TYR   A CD1 
84   C CD2 . TYR   A 11  ? 0.6009 0.5452 0.7059 0.0109  -0.0213 -0.0807 28  TYR   A CD2 
85   C CE1 . TYR   A 11  ? 0.5780 0.5455 0.7212 0.0077  -0.0173 -0.0836 28  TYR   A CE1 
86   C CE2 . TYR   A 11  ? 0.6343 0.5882 0.7536 0.0090  -0.0183 -0.0860 28  TYR   A CE2 
87   C CZ  . TYR   A 11  ? 0.5716 0.5363 0.7096 0.0071  -0.0163 -0.0874 28  TYR   A CZ  
88   O OH  . TYR   A 11  ? 0.5584 0.5294 0.7080 0.0041  -0.0131 -0.0926 28  TYR   A OH  
89   N N   . VAL   A 12  ? 0.6931 0.5889 0.7291 0.0271  -0.0421 -0.0705 29  VAL   A N   
90   C CA  . VAL   A 12  ? 0.6672 0.5394 0.6754 0.0275  -0.0447 -0.0653 29  VAL   A CA  
91   C C   . VAL   A 12  ? 0.7002 0.5625 0.6951 0.0209  -0.0406 -0.0626 29  VAL   A C   
92   O O   . VAL   A 12  ? 0.7149 0.5761 0.7025 0.0248  -0.0428 -0.0668 29  VAL   A O   
93   C CB  . VAL   A 12  ? 0.6854 0.5469 0.6748 0.0399  -0.0544 -0.0687 29  VAL   A CB  
94   C CG1 . VAL   A 12  ? 0.6753 0.5071 0.6308 0.0398  -0.0569 -0.0634 29  VAL   A CG1 
95   C CG2 . VAL   A 12  ? 0.6482 0.5189 0.6490 0.0461  -0.0577 -0.0706 29  VAL   A CG2 
96   N N   . VAL   A 13  ? 0.7002 0.5567 0.6920 0.0109  -0.0344 -0.0559 30  VAL   A N   
97   C CA  . VAL   A 13  ? 0.7373 0.5889 0.7200 0.0032  -0.0286 -0.0530 30  VAL   A CA  
98   C C   . VAL   A 13  ? 0.7593 0.5884 0.7155 -0.0031 -0.0284 -0.0464 30  VAL   A C   
99   O O   . VAL   A 13  ? 0.6940 0.5145 0.6447 -0.0041 -0.0307 -0.0431 30  VAL   A O   
100  C CB  . VAL   A 13  ? 0.6343 0.5055 0.6417 -0.0044 -0.0197 -0.0518 30  VAL   A CB  
101  C CG1 . VAL   A 13  ? 0.7421 0.6319 0.7742 0.0008  -0.0199 -0.0579 30  VAL   A CG1 
102  C CG2 . VAL   A 13  ? 0.7053 0.5787 0.7191 -0.0118 -0.0162 -0.0456 30  VAL   A CG2 
103  N N   . GLU   A 14  ? 0.7919 0.6104 0.7301 -0.0079 -0.0255 -0.0445 31  GLU   A N   
104  C CA  . GLU   A 14  ? 0.8137 0.6094 0.7241 -0.0161 -0.0244 -0.0382 31  GLU   A CA  
105  C C   . GLU   A 14  ? 0.7920 0.5991 0.7134 -0.0302 -0.0152 -0.0330 31  GLU   A C   
106  O O   . GLU   A 14  ? 0.7786 0.6087 0.7240 -0.0323 -0.0090 -0.0344 31  GLU   A O   
107  C CB  . GLU   A 14  ? 0.9006 0.6774 0.7826 -0.0143 -0.0260 -0.0388 31  GLU   A CB  
108  C CG  . GLU   A 14  ? 0.9378 0.7065 0.8095 0.0008  -0.0356 -0.0445 31  GLU   A CG  
109  C CD  . GLU   A 14  ? 0.9680 0.7147 0.8189 0.0078  -0.0437 -0.0431 31  GLU   A CD  
110  O OE1 . GLU   A 14  ? 0.9997 0.7174 0.8169 0.0052  -0.0453 -0.0388 31  GLU   A OE1 
111  O OE2 . GLU   A 14  ? 0.9301 0.6875 0.7969 0.0159  -0.0483 -0.0464 31  GLU   A OE2 
112  N N   . TYR   A 15  ? 0.7783 0.5689 0.6809 -0.0395 -0.0145 -0.0272 32  TYR   A N   
113  C CA  . TYR   A 15  ? 0.7487 0.5512 0.6601 -0.0539 -0.0064 -0.0222 32  TYR   A CA  
114  C C   . TYR   A 15  ? 0.7151 0.5280 0.6278 -0.0596 0.0014  -0.0222 32  TYR   A C   
115  O O   . TYR   A 15  ? 0.6762 0.4729 0.5660 -0.0586 0.0008  -0.0228 32  TYR   A O   
116  C CB  . TYR   A 15  ? 0.7590 0.5377 0.6441 -0.0643 -0.0076 -0.0165 32  TYR   A CB  
117  C CG  . TYR   A 15  ? 0.7878 0.5799 0.6809 -0.0806 0.0001  -0.0115 32  TYR   A CG  
118  C CD1 . TYR   A 15  ? 0.7639 0.5759 0.6817 -0.0832 0.0012  -0.0106 32  TYR   A CD1 
119  C CD2 . TYR   A 15  ? 0.7368 0.5227 0.6123 -0.0937 0.0061  -0.0079 32  TYR   A CD2 
120  C CE1 . TYR   A 15  ? 0.7549 0.5818 0.6807 -0.0976 0.0074  -0.0064 32  TYR   A CE1 
121  C CE2 . TYR   A 15  ? 0.6970 0.4988 0.5810 -0.1091 0.0130  -0.0039 32  TYR   A CE2 
122  C CZ  . TYR   A 15  ? 0.7372 0.5602 0.6469 -0.1107 0.0133  -0.0033 32  TYR   A CZ  
123  O OH  . TYR   A 15  ? 0.7681 0.6097 0.6871 -0.1255 0.0195  0.0004  32  TYR   A OH  
124  N N   . GLY   A 16  ? 0.7453 0.5852 0.6840 -0.0648 0.0087  -0.0215 33  GLY   A N   
125  C CA  . GLY   A 16  ? 0.7466 0.6001 0.6893 -0.0696 0.0170  -0.0217 33  GLY   A CA  
126  C C   . GLY   A 16  ? 0.7542 0.6166 0.7077 -0.0587 0.0174  -0.0278 33  GLY   A C   
127  O O   . GLY   A 16  ? 0.8352 0.7115 0.7952 -0.0611 0.0248  -0.0286 33  GLY   A O   
128  N N   . SER   A 17  ? 0.7463 0.6021 0.7014 -0.0470 0.0098  -0.0326 34  SER   A N   
129  C CA  . SER   A 17  ? 0.8053 0.6688 0.7695 -0.0378 0.0096  -0.0390 34  SER   A CA  
130  C C   . SER   A 17  ? 0.7414 0.6296 0.7381 -0.0351 0.0136  -0.0414 34  SER   A C   
131  O O   . SER   A 17  ? 0.7007 0.6004 0.7129 -0.0391 0.0159  -0.0380 34  SER   A O   
132  C CB  . SER   A 17  ? 0.6991 0.5480 0.6524 -0.0271 -0.0004 -0.0435 34  SER   A CB  
133  O OG  . SER   A 17  ? 0.7698 0.6242 0.7385 -0.0223 -0.0053 -0.0446 34  SER   A OG  
134  N N   . ASN   A 18  ? 0.7069 0.6019 0.7122 -0.0282 0.0142  -0.0474 35  ASN   A N   
135  C CA  . ASN   A 18  ? 0.7340 0.6474 0.7661 -0.0245 0.0175  -0.0504 35  ASN   A CA  
136  C C   . ASN   A 18  ? 0.6154 0.5277 0.6559 -0.0165 0.0103  -0.0560 35  ASN   A C   
137  O O   . ASN   A 18  ? 0.5851 0.4872 0.6127 -0.0116 0.0045  -0.0603 35  ASN   A O   
138  C CB  . ASN   A 18  ? 0.6749 0.5967 0.7104 -0.0236 0.0247  -0.0534 35  ASN   A CB  
139  C CG  . ASN   A 18  ? 0.7434 0.6675 0.7683 -0.0315 0.0320  -0.0487 35  ASN   A CG  
140  O OD1 . ASN   A 18  ? 0.6957 0.6261 0.7239 -0.0387 0.0348  -0.0430 35  ASN   A OD1 
141  N ND2 . ASN   A 18  ? 0.7390 0.6590 0.7509 -0.0308 0.0353  -0.0513 35  ASN   A ND2 
142  N N   . MET   A 19  ? 0.5858 0.5093 0.6474 -0.0153 0.0107  -0.0559 36  MET   A N   
143  C CA  . MET   A 19  ? 0.6283 0.5536 0.7000 -0.0093 0.0050  -0.0611 36  MET   A CA  
144  C C   . MET   A 19  ? 0.6057 0.5439 0.6990 -0.0080 0.0098  -0.0639 36  MET   A C   
145  O O   . MET   A 19  ? 0.6032 0.5501 0.7078 -0.0107 0.0159  -0.0600 36  MET   A O   
146  C CB  . MET   A 19  ? 0.5728 0.4952 0.6453 -0.0089 -0.0004 -0.0583 36  MET   A CB  
147  C CG  . MET   A 19  ? 0.6408 0.5732 0.7297 -0.0127 0.0035  -0.0535 36  MET   A CG  
148  S SD  . MET   A 19  ? 0.5961 0.5261 0.6883 -0.0102 -0.0031 -0.0525 36  MET   A SD  
149  C CE  . MET   A 19  ? 0.6417 0.5803 0.7457 -0.0167 0.0021  -0.0453 36  MET   A CE  
150  N N   . THR   A 20  ? 0.5816 0.5205 0.6794 -0.0038 0.0069  -0.0709 37  THR   A N   
151  C CA  . THR   A 20  ? 0.6577 0.6046 0.7731 -0.0029 0.0105  -0.0744 37  THR   A CA  
152  C C   . THR   A 20  ? 0.5625 0.5126 0.6875 -0.0013 0.0051  -0.0778 37  THR   A C   
153  O O   . THR   A 20  ? 0.6073 0.5556 0.7264 0.0013  -0.0013 -0.0831 37  THR   A O   
154  C CB  . THR   A 20  ? 0.5715 0.5160 0.6827 -0.0012 0.0129  -0.0805 37  THR   A CB  
155  O OG1 . THR   A 20  ? 0.6505 0.5927 0.7509 -0.0023 0.0181  -0.0776 37  THR   A OG1 
156  C CG2 . THR   A 20  ? 0.6084 0.5573 0.7350 -0.0007 0.0174  -0.0836 37  THR   A CG2 
157  N N   . ILE   A 21  ? 0.5293 0.4856 0.6690 -0.0027 0.0075  -0.0747 38  ILE   A N   
158  C CA  . ILE   A 21  ? 0.5458 0.5068 0.6957 -0.0021 0.0036  -0.0772 38  ILE   A CA  
159  C C   . ILE   A 21  ? 0.6065 0.5710 0.7692 -0.0034 0.0074  -0.0816 38  ILE   A C   
160  O O   . ILE   A 21  ? 0.6190 0.5825 0.7861 -0.0041 0.0139  -0.0797 38  ILE   A O   
161  C CB  . ILE   A 21  ? 0.5892 0.5522 0.7430 -0.0032 0.0033  -0.0706 38  ILE   A CB  
162  C CG1 . ILE   A 21  ? 0.5168 0.4844 0.6831 -0.0054 0.0099  -0.0660 38  ILE   A CG1 
163  C CG2 . ILE   A 21  ? 0.6153 0.5713 0.7536 -0.0038 0.0013  -0.0656 38  ILE   A CG2 
164  C CD1 . ILE   A 21  ? 0.6019 0.5723 0.7733 -0.0064 0.0087  -0.0607 38  ILE   A CD1 
165  N N   . GLU   A 22  ? 0.5629 0.5314 0.7305 -0.0035 0.0032  -0.0879 39  GLU   A N   
166  C CA  . GLU   A 22  ? 0.5667 0.5362 0.7425 -0.0063 0.0059  -0.0937 39  GLU   A CA  
167  C C   . GLU   A 22  ? 0.6213 0.5978 0.8101 -0.0091 0.0056  -0.0945 39  GLU   A C   
168  O O   . GLU   A 22  ? 0.6595 0.6436 0.8501 -0.0081 0.0001  -0.0961 39  GLU   A O   
169  C CB  . GLU   A 22  ? 0.5555 0.5250 0.7243 -0.0059 0.0013  -0.1022 39  GLU   A CB  
170  C CG  . GLU   A 22  ? 0.6234 0.5843 0.7803 -0.0045 0.0037  -0.1035 39  GLU   A CG  
171  C CD  . GLU   A 22  ? 0.6976 0.6585 0.8481 -0.0047 -0.0010 -0.1127 39  GLU   A CD  
172  O OE1 . GLU   A 22  ? 0.5933 0.5629 0.7480 -0.0051 -0.0074 -0.1175 39  GLU   A OE1 
173  O OE2 . GLU   A 22  ? 0.7545 0.7080 0.8961 -0.0042 0.0015  -0.1153 39  GLU   A OE2 
174  N N   . CYS   A 23  ? 0.5685 0.5419 0.7654 -0.0122 0.0117  -0.0931 40  CYS   A N   
175  C CA  . CYS   A 23  ? 0.6370 0.6148 0.8443 -0.0169 0.0125  -0.0959 40  CYS   A CA  
176  C C   . CYS   A 23  ? 0.6153 0.5845 0.8230 -0.0210 0.0173  -0.1005 40  CYS   A C   
177  O O   . CYS   A 23  ? 0.6206 0.5797 0.8230 -0.0188 0.0219  -0.0985 40  CYS   A O   
178  C CB  . CYS   A 23  ? 0.6062 0.5860 0.8210 -0.0171 0.0151  -0.0889 40  CYS   A CB  
179  S SG  . CYS   A 23  ? 0.6761 0.6469 0.8910 -0.0151 0.0223  -0.0805 40  CYS   A SG  
180  N N   . LYS   A 24  ? 0.6525 0.6258 0.8659 -0.0272 0.0163  -0.1068 41  LYS   A N   
181  C CA  . LYS   A 24  ? 0.5773 0.5414 0.7883 -0.0328 0.0195  -0.1131 41  LYS   A CA  
182  C C   . LYS   A 24  ? 0.5290 0.4889 0.7468 -0.0398 0.0244  -0.1125 41  LYS   A C   
183  O O   . LYS   A 24  ? 0.5354 0.5062 0.7619 -0.0425 0.0233  -0.1112 41  LYS   A O   
184  C CB  . LYS   A 24  ? 0.5541 0.5264 0.7634 -0.0361 0.0134  -0.1228 41  LYS   A CB  
185  C CG  . LYS   A 24  ? 0.5791 0.5443 0.7764 -0.0321 0.0117  -0.1260 41  LYS   A CG  
186  C CD  . LYS   A 24  ? 0.6388 0.6158 0.8325 -0.0270 0.0036  -0.1278 41  LYS   A CD  
187  C CE  . LYS   A 24  ? 0.6487 0.6171 0.8284 -0.0224 0.0027  -0.1292 41  LYS   A CE  
188  N NZ  . LYS   A 24  ? 0.7833 0.7607 0.9566 -0.0181 -0.0059 -0.1325 41  LYS   A NZ  
189  N N   . PHE   A 25  ? 0.5582 0.5009 0.7703 -0.0423 0.0302  -0.1134 42  PHE   A N   
190  C CA  . PHE   A 25  ? 0.6289 0.5618 0.8430 -0.0494 0.0356  -0.1129 42  PHE   A CA  
191  C C   . PHE   A 25  ? 0.6638 0.5837 0.8708 -0.0573 0.0374  -0.1212 42  PHE   A C   
192  O O   . PHE   A 25  ? 0.6773 0.5898 0.8755 -0.0544 0.0366  -0.1252 42  PHE   A O   
193  C CB  . PHE   A 25  ? 0.6464 0.5656 0.8575 -0.0433 0.0415  -0.1039 42  PHE   A CB  
194  C CG  . PHE   A 25  ? 0.6014 0.5076 0.8027 -0.0355 0.0442  -0.1027 42  PHE   A CG  
195  C CD1 . PHE   A 25  ? 0.6175 0.5323 0.8182 -0.0272 0.0419  -0.0992 42  PHE   A CD1 
196  C CD2 . PHE   A 25  ? 0.6317 0.5166 0.8232 -0.0364 0.0495  -0.1050 42  PHE   A CD2 
197  C CE1 . PHE   A 25  ? 0.6950 0.6006 0.8875 -0.0200 0.0450  -0.0983 42  PHE   A CE1 
198  C CE2 . PHE   A 25  ? 0.6536 0.5278 0.8360 -0.0278 0.0523  -0.1042 42  PHE   A CE2 
199  C CZ  . PHE   A 25  ? 0.7319 0.6181 0.9157 -0.0197 0.0502  -0.1009 42  PHE   A CZ  
200  N N   . PRO   A 26  ? 0.6321 0.5483 0.8414 -0.0682 0.0402  -0.1242 43  PRO   A N   
201  C CA  . PRO   A 26  ? 0.7469 0.6505 0.9486 -0.0782 0.0416  -0.1330 43  PRO   A CA  
202  C C   . PRO   A 26  ? 0.7998 0.6732 0.9866 -0.0750 0.0481  -0.1309 43  PRO   A C   
203  O O   . PRO   A 26  ? 0.7890 0.6488 0.9730 -0.0719 0.0535  -0.1237 43  PRO   A O   
204  C CB  . PRO   A 26  ? 0.6401 0.5503 0.8492 -0.0916 0.0434  -0.1355 43  PRO   A CB  
205  C CG  . PRO   A 26  ? 0.7174 0.6320 0.9332 -0.0869 0.0459  -0.1259 43  PRO   A CG  
206  C CD  . PRO   A 26  ? 0.6427 0.5692 0.8621 -0.0733 0.0414  -0.1207 43  PRO   A CD  
207  N N   . VAL   A 27  ? 0.8875 0.7503 1.0637 -0.0748 0.0472  -0.1375 44  VAL   A N   
208  C CA  . VAL   A 27  ? 0.8856 0.7188 1.0455 -0.0711 0.0530  -0.1375 44  VAL   A CA  
209  C C   . VAL   A 27  ? 0.9675 0.7847 1.1175 -0.0849 0.0541  -0.1471 44  VAL   A C   
210  O O   . VAL   A 27  ? 1.0109 0.8421 1.1645 -0.0931 0.0487  -0.1557 44  VAL   A O   
211  C CB  . VAL   A 27  ? 0.8889 0.7210 1.0424 -0.0582 0.0520  -0.1369 44  VAL   A CB  
212  C CG1 . VAL   A 27  ? 0.8355 0.6768 0.9865 -0.0618 0.0461  -0.1462 44  VAL   A CG1 
213  C CG2 . VAL   A 27  ? 1.0677 0.8708 1.2054 -0.0511 0.0587  -0.1352 44  VAL   A CG2 
214  N N   . GLU   A 28  ? 1.1638 0.9516 1.3008 -0.0879 0.0608  -0.1458 45  GLU   A N   
215  C CA  . GLU   A 28  ? 1.3087 1.0782 1.4348 -0.1036 0.0627  -0.1544 45  GLU   A CA  
216  C C   . GLU   A 28  ? 1.3369 1.0873 1.4462 -0.1017 0.0624  -0.1620 45  GLU   A C   
217  O O   . GLU   A 28  ? 1.3565 1.1164 1.4661 -0.1107 0.0575  -0.1716 45  GLU   A O   
218  C CB  . GLU   A 28  ? 1.2968 1.0391 1.4128 -0.1085 0.0701  -0.1496 45  GLU   A CB  
219  N N   . LYS   A 29  ? 1.3516 1.0757 1.4456 -0.0895 0.0675  -0.1583 46  LYS   A N   
220  C CA  . LYS   A 29  ? 1.3414 1.0469 1.4183 -0.0856 0.0677  -0.1654 46  LYS   A CA  
221  C C   . LYS   A 29  ? 1.4055 1.1150 1.4815 -0.0657 0.0685  -0.1599 46  LYS   A C   
222  O O   . LYS   A 29  ? 1.3554 1.0837 1.4363 -0.0614 0.0639  -0.1628 46  LYS   A O   
223  C CB  . LYS   A 29  ? 1.2503 0.9143 1.3041 -0.0914 0.0738  -0.1686 46  LYS   A CB  
224  N N   . GLN   A 30  ? 1.5827 1.2758 1.6523 -0.0535 0.0744  -0.1521 47  GLN   A N   
225  C CA  . GLN   A 30  ? 1.5097 1.2113 1.5815 -0.0351 0.0758  -0.1458 47  GLN   A CA  
226  C C   . GLN   A 30  ? 1.4665 1.1871 1.5549 -0.0296 0.0759  -0.1350 47  GLN   A C   
227  O O   . GLN   A 30  ? 1.5236 1.2549 1.6231 -0.0399 0.0739  -0.1331 47  GLN   A O   
228  C CB  . GLN   A 30  ? 1.4420 1.1116 1.4927 -0.0234 0.0821  -0.1463 47  GLN   A CB  
229  N N   . LEU   A 31  ? 1.0905 0.8167 1.1806 -0.0136 0.0783  -0.1282 48  LEU   A N   
230  C CA  . LEU   A 31  ? 1.0649 0.8088 1.1694 -0.0076 0.0782  -0.1180 48  LEU   A CA  
231  C C   . LEU   A 31  ? 1.0535 0.7754 1.1479 0.0029  0.0842  -0.1121 48  LEU   A C   
232  O O   . LEU   A 31  ? 1.1139 0.8242 1.1974 0.0160  0.0879  -0.1122 48  LEU   A O   
233  C CB  . LEU   A 31  ? 1.0812 0.8530 1.1970 0.0013  0.0756  -0.1146 48  LEU   A CB  
234  C CG  . LEU   A 31  ? 0.9514 0.7501 1.0857 -0.0014 0.0715  -0.1080 48  LEU   A CG  
235  C CD1 . LEU   A 31  ? 0.9321 0.7415 1.0735 -0.0157 0.0660  -0.1132 48  LEU   A CD1 
236  C CD2 . LEU   A 31  ? 0.9122 0.7331 1.0538 0.0077  0.0701  -0.1039 48  LEU   A CD2 
237  N N   . ASP   A 32  ? 0.9991 0.7156 1.0964 -0.0021 0.0852  -0.1069 49  ASP   A N   
238  C CA  . ASP   A 32  ? 0.9889 0.6914 1.0801 0.0096  0.0895  -0.0990 49  ASP   A CA  
239  C C   . ASP   A 32  ? 0.9028 0.6355 1.0109 0.0198  0.0874  -0.0907 49  ASP   A C   
240  O O   . ASP   A 32  ? 0.8395 0.5856 0.9592 0.0164  0.0855  -0.0847 49  ASP   A O   
241  C CB  . ASP   A 32  ? 0.9881 0.6714 1.0735 -0.0006 0.0914  -0.0968 49  ASP   A CB  
242  C CG  . ASP   A 32  ? 1.0501 0.7032 1.1181 0.0109  0.0967  -0.0917 49  ASP   A CG  
243  O OD1 . ASP   A 32  ? 0.9817 0.6199 1.0366 0.0242  0.0995  -0.0933 49  ASP   A OD1 
244  O OD2 . ASP   A 32  ? 1.0149 0.6587 1.0810 0.0075  0.0982  -0.0860 49  ASP   A OD2 
245  N N   . LEU   A 33  ? 0.9454 0.6890 1.0543 0.0320  0.0880  -0.0908 50  LEU   A N   
246  C CA  . LEU   A 33  ? 0.9056 0.6787 1.0297 0.0407  0.0863  -0.0838 50  LEU   A CA  
247  C C   . LEU   A 33  ? 0.9007 0.6725 1.0267 0.0495  0.0880  -0.0748 50  LEU   A C   
248  O O   . LEU   A 33  ? 0.8804 0.6774 1.0207 0.0522  0.0855  -0.0686 50  LEU   A O   
249  C CB  . LEU   A 33  ? 0.9669 0.7491 1.0887 0.0521  0.0881  -0.0858 50  LEU   A CB  
250  C CG  . LEU   A 33  ? 0.9913 0.7831 1.1140 0.0450  0.0854  -0.0930 50  LEU   A CG  
251  C CD1 . LEU   A 33  ? 0.9636 0.7445 1.0729 0.0549  0.0895  -0.0982 50  LEU   A CD1 
252  C CD2 . LEU   A 33  ? 0.8768 0.7011 1.0158 0.0429  0.0813  -0.0890 50  LEU   A CD2 
253  N N   . ALA   A 34  ? 0.9257 0.6676 1.0361 0.0538  0.0918  -0.0741 51  ALA   A N   
254  C CA  . ALA   A 34  ? 0.8971 0.6356 1.0074 0.0620  0.0929  -0.0656 51  ALA   A CA  
255  C C   . ALA   A 34  ? 0.8322 0.5761 0.9511 0.0492  0.0903  -0.0617 51  ALA   A C   
256  O O   . ALA   A 34  ? 0.7896 0.5340 0.9099 0.0548  0.0904  -0.0542 51  ALA   A O   
257  C CB  . ALA   A 34  ? 0.8378 0.5388 0.9254 0.0712  0.0979  -0.0659 51  ALA   A CB  
258  N N   . ALA   A 35  ? 0.7994 0.5482 0.9239 0.0329  0.0878  -0.0668 52  ALA   A N   
259  C CA  . ALA   A 35  ? 0.7883 0.5455 0.9220 0.0209  0.0855  -0.0640 52  ALA   A CA  
260  C C   . ALA   A 35  ? 0.7462 0.5358 0.8983 0.0140  0.0801  -0.0649 52  ALA   A C   
261  O O   . ALA   A 35  ? 0.7327 0.5330 0.8937 0.0060  0.0779  -0.0623 52  ALA   A O   
262  C CB  . ALA   A 35  ? 0.7512 0.4838 0.8739 0.0063  0.0877  -0.0693 52  ALA   A CB  
263  N N   . LEU   A 36  ? 0.6614 0.4654 0.8177 0.0174  0.0782  -0.0686 53  LEU   A N   
264  C CA  . LEU   A 36  ? 0.7270 0.5584 0.8975 0.0120  0.0730  -0.0692 53  LEU   A CA  
265  C C   . LEU   A 36  ? 0.6883 0.5404 0.8694 0.0189  0.0711  -0.0609 53  LEU   A C   
266  O O   . LEU   A 36  ? 0.7254 0.5811 0.9056 0.0305  0.0730  -0.0571 53  LEU   A O   
267  C CB  . LEU   A 36  ? 0.7573 0.5942 0.9257 0.0132  0.0718  -0.0756 53  LEU   A CB  
268  C CG  . LEU   A 36  ? 0.5950 0.4558 0.7740 0.0077  0.0663  -0.0772 53  LEU   A CG  
269  C CD1 . LEU   A 36  ? 0.7270 0.5850 0.9054 -0.0045 0.0634  -0.0849 53  LEU   A CD1 
270  C CD2 . LEU   A 36  ? 0.7070 0.5777 0.8846 0.0149  0.0662  -0.0782 53  LEU   A CD2 
271  N N   . ILE   A 37  ? 0.6109 0.4775 0.8021 0.0116  0.0673  -0.0586 54  ILE   A N   
272  C CA  . ILE   A 37  ? 0.6784 0.5647 0.8791 0.0157  0.0647  -0.0514 54  ILE   A CA  
273  C C   . ILE   A 37  ? 0.6397 0.5444 0.8484 0.0087  0.0595  -0.0537 54  ILE   A C   
274  O O   . ILE   A 37  ? 0.6068 0.5121 0.8182 -0.0001 0.0573  -0.0566 54  ILE   A O   
275  C CB  . ILE   A 37  ? 0.6728 0.5548 0.8746 0.0153  0.0653  -0.0452 54  ILE   A CB  
276  C CG1 . ILE   A 37  ? 0.6819 0.5485 0.8751 0.0261  0.0696  -0.0410 54  ILE   A CG1 
277  C CG2 . ILE   A 37  ? 0.6249 0.5283 0.8370 0.0152  0.0611  -0.0396 54  ILE   A CG2 
278  C CD1 . ILE   A 37  ? 0.7405 0.6069 0.9348 0.0288  0.0694  -0.0333 54  ILE   A CD1 
279  N N   . VAL   A 38  ? 0.6444 0.5638 0.8561 0.0128  0.0576  -0.0524 55  VAL   A N   
280  C CA  . VAL   A 38  ? 0.6973 0.6314 0.9134 0.0076  0.0526  -0.0539 55  VAL   A CA  
281  C C   . VAL   A 38  ? 0.6881 0.6376 0.9098 0.0103  0.0506  -0.0467 55  VAL   A C   
282  O O   . VAL   A 38  ? 0.7129 0.6686 0.9349 0.0167  0.0527  -0.0434 55  VAL   A O   
283  C CB  . VAL   A 38  ? 0.7063 0.6414 0.9175 0.0079  0.0521  -0.0596 55  VAL   A CB  
284  C CG1 . VAL   A 38  ? 0.5903 0.5385 0.8034 0.0038  0.0467  -0.0601 55  VAL   A CG1 
285  C CG2 . VAL   A 38  ? 0.6688 0.5889 0.8739 0.0040  0.0534  -0.0673 55  VAL   A CG2 
286  N N   . TYR   A 39  ? 0.7120 0.6682 0.9379 0.0052  0.0466  -0.0447 56  TYR   A N   
287  C CA  . TYR   A 39  ? 0.7358 0.7051 0.9653 0.0058  0.0439  -0.0387 56  TYR   A CA  
288  C C   . TYR   A 39  ? 0.6861 0.6619 0.9140 0.0009  0.0389  -0.0409 56  TYR   A C   
289  O O   . TYR   A 39  ? 0.6922 0.6661 0.9206 -0.0033 0.0361  -0.0440 56  TYR   A O   
290  C CB  . TYR   A 39  ? 0.7305 0.6994 0.9636 0.0056  0.0436  -0.0335 56  TYR   A CB  
291  C CG  . TYR   A 39  ? 0.7368 0.7185 0.9728 0.0063  0.0410  -0.0273 56  TYR   A CG  
292  C CD1 . TYR   A 39  ? 0.7518 0.7422 0.9893 0.0116  0.0426  -0.0234 56  TYR   A CD1 
293  C CD2 . TYR   A 39  ? 0.7411 0.7268 0.9778 0.0017  0.0368  -0.0257 56  TYR   A CD2 
294  C CE1 . TYR   A 39  ? 0.7677 0.7711 1.0079 0.0107  0.0399  -0.0182 56  TYR   A CE1 
295  C CE2 . TYR   A 39  ? 0.7439 0.7394 0.9814 0.0013  0.0341  -0.0204 56  TYR   A CE2 
296  C CZ  . TYR   A 39  ? 0.7609 0.7656 1.0004 0.0050  0.0356  -0.0167 56  TYR   A CZ  
297  O OH  . TYR   A 39  ? 0.7483 0.7641 0.9888 0.0031  0.0327  -0.0118 56  TYR   A OH  
298  N N   . TRP   A 40  ? 0.6429 0.6266 0.8683 0.0016  0.0379  -0.0394 57  TRP   A N   
299  C CA  . TRP   A 40  ? 0.6102 0.5974 0.8308 -0.0024 0.0332  -0.0404 57  TRP   A CA  
300  C C   . TRP   A 40  ? 0.6318 0.6270 0.8530 -0.0042 0.0309  -0.0340 57  TRP   A C   
301  O O   . TRP   A 40  ? 0.6602 0.6633 0.8834 -0.0026 0.0332  -0.0299 57  TRP   A O   
302  C CB  . TRP   A 40  ? 0.6027 0.5901 0.8167 -0.0020 0.0339  -0.0436 57  TRP   A CB  
303  C CG  . TRP   A 40  ? 0.5388 0.5185 0.7485 -0.0026 0.0328  -0.0510 57  TRP   A CG  
304  C CD1 . TRP   A 40  ? 0.5891 0.5631 0.7968 -0.0003 0.0363  -0.0555 57  TRP   A CD1 
305  C CD2 . TRP   A 40  ? 0.5468 0.5244 0.7531 -0.0054 0.0274  -0.0551 57  TRP   A CD2 
306  N NE1 . TRP   A 40  ? 0.6745 0.6434 0.8781 -0.0025 0.0332  -0.0622 57  TRP   A NE1 
307  C CE2 . TRP   A 40  ? 0.5968 0.5691 0.8001 -0.0053 0.0276  -0.0621 57  TRP   A CE2 
308  C CE3 . TRP   A 40  ? 0.5974 0.5771 0.8021 -0.0073 0.0222  -0.0538 57  TRP   A CE3 
309  C CZ2 . TRP   A 40  ? 0.5527 0.5244 0.7530 -0.0070 0.0225  -0.0678 57  TRP   A CZ2 
310  C CZ3 . TRP   A 40  ? 0.5168 0.4951 0.7181 -0.0078 0.0174  -0.0594 57  TRP   A CZ3 
311  C CH2 . TRP   A 40  ? 0.5249 0.5006 0.7247 -0.0077 0.0174  -0.0663 57  TRP   A CH2 
312  N N   . GLU   A 41  ? 0.5648 0.5587 0.7840 -0.0073 0.0264  -0.0336 58  GLU   A N   
313  C CA  . GLU   A 41  ? 0.5891 0.5878 0.8063 -0.0098 0.0237  -0.0282 58  GLU   A CA  
314  C C   . GLU   A 41  ? 0.5755 0.5692 0.7833 -0.0127 0.0182  -0.0300 58  GLU   A C   
315  O O   . GLU   A 41  ? 0.5349 0.5236 0.7405 -0.0117 0.0161  -0.0351 58  GLU   A O   
316  C CB  . GLU   A 41  ? 0.6235 0.6239 0.8471 -0.0089 0.0241  -0.0243 58  GLU   A CB  
317  C CG  . GLU   A 41  ? 0.5271 0.5224 0.7504 -0.0100 0.0213  -0.0263 58  GLU   A CG  
318  C CD  . GLU   A 41  ? 0.5881 0.5846 0.8158 -0.0095 0.0219  -0.0219 58  GLU   A CD  
319  O OE1 . GLU   A 41  ? 0.5717 0.5734 0.8022 -0.0081 0.0235  -0.0170 58  GLU   A OE1 
320  O OE2 . GLU   A 41  ? 0.6012 0.5947 0.8294 -0.0102 0.0208  -0.0233 58  GLU   A OE2 
321  N N   . MET   A 42  ? 0.6329 0.6279 0.8344 -0.0161 0.0158  -0.0258 59  MET   A N   
322  C CA  . MET   A 42  ? 0.6335 0.6208 0.8236 -0.0182 0.0104  -0.0263 59  MET   A CA  
323  C C   . MET   A 42  ? 0.6242 0.6129 0.8119 -0.0217 0.0085  -0.0209 59  MET   A C   
324  O O   . MET   A 42  ? 0.6298 0.6253 0.8181 -0.0254 0.0102  -0.0168 59  MET   A O   
325  C CB  . MET   A 42  ? 0.5989 0.5800 0.7759 -0.0199 0.0087  -0.0282 59  MET   A CB  
326  C CG  . MET   A 42  ? 0.6267 0.6087 0.7952 -0.0260 0.0092  -0.0237 59  MET   A CG  
327  S SD  . MET   A 42  ? 0.7773 0.7464 0.9283 -0.0305 0.0031  -0.0211 59  MET   A SD  
328  C CE  . MET   A 42  ? 0.6229 0.5768 0.7551 -0.0291 -0.0002 -0.0251 59  MET   A CE  
329  N N   . GLU   A 43  ? 0.6841 0.6682 0.8700 -0.0205 0.0053  -0.0211 60  GLU   A N   
330  C CA  . GLU   A 43  ? 0.7164 0.6996 0.8981 -0.0236 0.0029  -0.0167 60  GLU   A CA  
331  C C   . GLU   A 43  ? 0.7377 0.7324 0.9295 -0.0253 0.0061  -0.0118 60  GLU   A C   
332  O O   . GLU   A 43  ? 0.8330 0.8327 1.0218 -0.0303 0.0058  -0.0082 60  GLU   A O   
333  C CB  . GLU   A 43  ? 0.6838 0.6573 0.8482 -0.0284 -0.0010 -0.0155 60  GLU   A CB  
334  C CG  . GLU   A 43  ? 0.7407 0.7021 0.8931 -0.0252 -0.0044 -0.0202 60  GLU   A CG  
335  C CD  . GLU   A 43  ? 0.7607 0.7080 0.8963 -0.0253 -0.0098 -0.0199 60  GLU   A CD  
336  O OE1 . GLU   A 43  ? 0.8025 0.7452 0.9291 -0.0316 -0.0111 -0.0157 60  GLU   A OE1 
337  O OE2 . GLU   A 43  ? 0.6799 0.6209 0.8108 -0.0189 -0.0129 -0.0241 60  GLU   A OE2 
338  N N   . ASP   A 44  ? 0.7293 0.7285 0.9327 -0.0209 0.0091  -0.0121 61  ASP   A N   
339  C CA  . ASP   A 44  ? 0.7508 0.7596 0.9639 -0.0195 0.0121  -0.0079 61  ASP   A CA  
340  C C   . ASP   A 44  ? 0.7403 0.7596 0.9560 -0.0211 0.0143  -0.0058 61  ASP   A C   
341  O O   . ASP   A 44  ? 0.7694 0.7994 0.9902 -0.0213 0.0148  -0.0016 61  ASP   A O   
342  C CB  . ASP   A 44  ? 0.7767 0.7866 0.9887 -0.0209 0.0096  -0.0037 61  ASP   A CB  
343  C CG  . ASP   A 44  ? 0.8885 0.8934 1.0881 -0.0267 0.0047  -0.0027 61  ASP   A CG  
344  O OD1 . ASP   A 44  ? 0.8639 0.8580 1.0544 -0.0268 0.0021  -0.0060 61  ASP   A OD1 
345  O OD2 . ASP   A 44  ? 0.9562 0.9678 1.1545 -0.0310 0.0032  0.0014  61  ASP   A OD2 
346  N N   . LYS   A 45  ? 0.7008 0.7186 0.9132 -0.0218 0.0156  -0.0089 62  LYS   A N   
347  C CA  . LYS   A 45  ? 0.6398 0.6686 0.8544 -0.0231 0.0186  -0.0076 62  LYS   A CA  
348  C C   . LYS   A 45  ? 0.6611 0.6889 0.8803 -0.0175 0.0230  -0.0116 62  LYS   A C   
349  O O   . LYS   A 45  ? 0.6402 0.6585 0.8535 -0.0175 0.0224  -0.0160 62  LYS   A O   
350  C CB  . LYS   A 45  ? 0.7079 0.7346 0.9107 -0.0309 0.0164  -0.0073 62  LYS   A CB  
351  C CG  . LYS   A 45  ? 0.6727 0.7049 0.8716 -0.0382 0.0135  -0.0028 62  LYS   A CG  
352  C CD  . LYS   A 45  ? 0.7322 0.7647 0.9200 -0.0472 0.0134  -0.0020 62  LYS   A CD  
353  C CE  . LYS   A 45  ? 0.6639 0.6808 0.8395 -0.0469 0.0129  -0.0060 62  LYS   A CE  
354  N NZ  . LYS   A 45  ? 0.7027 0.7006 0.8629 -0.0490 0.0073  -0.0067 62  LYS   A NZ  
355  N N   . ASN   A 46  ? 0.6353 0.6720 0.8638 -0.0120 0.0270  -0.0101 63  ASN   A N   
356  C CA  . ASN   A 46  ? 0.6392 0.6728 0.8704 -0.0062 0.0314  -0.0140 63  ASN   A CA  
357  C C   . ASN   A 46  ? 0.6100 0.6463 0.8357 -0.0087 0.0330  -0.0164 63  ASN   A C   
358  O O   . ASN   A 46  ? 0.6313 0.6785 0.8554 -0.0132 0.0331  -0.0138 63  ASN   A O   
359  C CB  . ASN   A 46  ? 0.7568 0.7983 0.9965 0.0013  0.0353  -0.0116 63  ASN   A CB  
360  C CG  . ASN   A 46  ? 0.7257 0.7613 0.9659 0.0079  0.0400  -0.0157 63  ASN   A CG  
361  O OD1 . ASN   A 46  ? 0.7224 0.7496 0.9573 0.0061  0.0404  -0.0206 63  ASN   A OD1 
362  N ND2 . ASN   A 46  ? 0.7393 0.7788 0.9844 0.0161  0.0434  -0.0140 63  ASN   A ND2 
363  N N   . ILE   A 47  ? 0.6474 0.6738 0.8697 -0.0064 0.0344  -0.0217 64  ILE   A N   
364  C CA  . ILE   A 47  ? 0.6499 0.6769 0.8658 -0.0075 0.0364  -0.0246 64  ILE   A CA  
365  C C   . ILE   A 47  ? 0.7315 0.7611 0.9518 -0.0003 0.0422  -0.0270 64  ILE   A C   
366  O O   . ILE   A 47  ? 0.7436 0.7837 0.9638 0.0006  0.0459  -0.0265 64  ILE   A O   
367  C CB  . ILE   A 47  ? 0.5791 0.5924 0.7850 -0.0102 0.0328  -0.0292 64  ILE   A CB  
368  C CG1 . ILE   A 47  ? 0.5443 0.5530 0.7447 -0.0152 0.0270  -0.0271 64  ILE   A CG1 
369  C CG2 . ILE   A 47  ? 0.5776 0.5908 0.7743 -0.0122 0.0344  -0.0314 64  ILE   A CG2 
370  C CD1 . ILE   A 47  ? 0.6144 0.6110 0.8047 -0.0160 0.0227  -0.0316 64  ILE   A CD1 
371  N N   . ILE   A 48  ? 0.7073 0.7271 0.9306 0.0048  0.0433  -0.0297 65  ILE   A N   
372  C CA  . ILE   A 48  ? 0.7039 0.7207 0.9283 0.0122  0.0484  -0.0327 65  ILE   A CA  
373  C C   . ILE   A 48  ? 0.7395 0.7467 0.9679 0.0166  0.0492  -0.0324 65  ILE   A C   
374  O O   . ILE   A 48  ? 0.6938 0.6921 0.9219 0.0127  0.0462  -0.0333 65  ILE   A O   
375  C CB  . ILE   A 48  ? 0.7087 0.7156 0.9248 0.0114  0.0492  -0.0392 65  ILE   A CB  
376  C CG1 . ILE   A 48  ? 0.6684 0.6846 0.8792 0.0093  0.0507  -0.0392 65  ILE   A CG1 
377  C CG2 . ILE   A 48  ? 0.8144 0.8117 1.0299 0.0183  0.0535  -0.0432 65  ILE   A CG2 
378  C CD1 . ILE   A 48  ? 0.8244 0.8521 1.0385 0.0159  0.0569  -0.0382 65  ILE   A CD1 
379  N N   . GLN   A 49  ? 0.8349 0.8435 1.0660 0.0249  0.0536  -0.0311 66  GLN   A N   
380  C CA  . GLN   A 49  ? 0.7993 0.7952 1.0309 0.0300  0.0552  -0.0306 66  GLN   A CA  
381  C C   . GLN   A 49  ? 0.8563 0.8399 1.0821 0.0369  0.0600  -0.0353 66  GLN   A C   
382  O O   . GLN   A 49  ? 0.9236 0.9148 1.1496 0.0450  0.0637  -0.0346 66  GLN   A O   
383  C CB  . GLN   A 49  ? 0.8098 0.8160 1.0473 0.0354  0.0553  -0.0240 66  GLN   A CB  
384  C CG  . GLN   A 49  ? 0.8455 0.8520 1.0859 0.0300  0.0510  -0.0200 66  GLN   A CG  
385  C CD  . GLN   A 49  ? 0.8382 0.8423 1.0804 0.0369  0.0519  -0.0152 66  GLN   A CD  
386  O OE1 . GLN   A 49  ? 0.8100 0.8089 1.0501 0.0465  0.0556  -0.0152 66  GLN   A OE1 
387  N NE2 . GLN   A 49  ? 0.8132 0.8201 1.0577 0.0330  0.0483  -0.0111 66  GLN   A NE2 
388  N N   . PHE   A 50  ? 0.8293 0.7944 1.0494 0.0336  0.0601  -0.0403 67  PHE   A N   
389  C CA  . PHE   A 50  ? 0.8417 0.7907 1.0538 0.0388  0.0644  -0.0454 67  PHE   A CA  
390  C C   . PHE   A 50  ? 0.7578 0.6890 0.9663 0.0422  0.0665  -0.0440 67  PHE   A C   
391  O O   . PHE   A 50  ? 0.7107 0.6297 0.9175 0.0348  0.0651  -0.0460 67  PHE   A O   
392  C CB  . PHE   A 50  ? 0.7852 0.7254 0.9915 0.0318  0.0631  -0.0529 67  PHE   A CB  
393  C CG  . PHE   A 50  ? 0.7733 0.7011 0.9704 0.0373  0.0674  -0.0585 67  PHE   A CG  
394  C CD1 . PHE   A 50  ? 0.8416 0.7791 1.0364 0.0418  0.0695  -0.0599 67  PHE   A CD1 
395  C CD2 . PHE   A 50  ? 0.8412 0.7464 1.0303 0.0378  0.0698  -0.0624 67  PHE   A CD2 
396  C CE1 . PHE   A 50  ? 0.8250 0.7506 1.0102 0.0476  0.0737  -0.0654 67  PHE   A CE1 
397  C CE2 . PHE   A 50  ? 0.8636 0.7548 1.0421 0.0430  0.0737  -0.0679 67  PHE   A CE2 
398  C CZ  . PHE   A 50  ? 0.8248 0.7265 1.0015 0.0485  0.0756  -0.0695 67  PHE   A CZ  
399  N N   . VAL   A 51  ? 0.8243 0.7535 1.0307 0.0535  0.0701  -0.0410 68  VAL   A N   
400  C CA  . VAL   A 51  ? 0.8712 0.7798 1.0706 0.0582  0.0724  -0.0394 68  VAL   A CA  
401  C C   . VAL   A 51  ? 0.9399 0.8341 1.1286 0.0688  0.0773  -0.0430 68  VAL   A C   
402  O O   . VAL   A 51  ? 0.9188 0.8262 1.1092 0.0750  0.0790  -0.0445 68  VAL   A O   
403  C CB  . VAL   A 51  ? 0.9048 0.8230 1.1095 0.0642  0.0713  -0.0315 68  VAL   A CB  
404  C CG1 . VAL   A 51  ? 0.8524 0.7706 1.0614 0.0539  0.0676  -0.0286 68  VAL   A CG1 
405  C CG2 . VAL   A 51  ? 0.8649 0.8117 1.0794 0.0694  0.0702  -0.0282 68  VAL   A CG2 
406  N N   . HIS   A 52  ? 1.1003 0.9664 1.2767 0.0706  0.0801  -0.0448 69  HIS   A N   
407  C CA  . HIS   A 52  ? 1.0481 0.8955 1.2111 0.0806  0.0848  -0.0490 69  HIS   A CA  
408  C C   . HIS   A 52  ? 1.0710 0.9238 1.2335 0.0764  0.0851  -0.0560 69  HIS   A C   
409  O O   . HIS   A 52  ? 1.0905 0.9433 1.2553 0.0632  0.0822  -0.0599 69  HIS   A O   
410  C CB  . HIS   A 52  ? 1.0014 0.8571 1.1643 0.0983  0.0872  -0.0443 69  HIS   A CB  
411  C CG  . HIS   A 52  ? 1.0944 0.9549 1.2617 0.1024  0.0852  -0.0363 69  HIS   A CG  
412  N ND1 . HIS   A 52  ? 1.1234 1.0104 1.3011 0.1122  0.0840  -0.0307 69  HIS   A ND1 
413  C CD2 . HIS   A 52  ? 1.1218 0.9646 1.2840 0.0973  0.0843  -0.0330 69  HIS   A CD2 
414  C CE1 . HIS   A 52  ? 1.1095 0.9944 1.2881 0.1138  0.0818  -0.0244 69  HIS   A CE1 
415  N NE2 . HIS   A 52  ? 1.1613 1.0188 1.3300 0.1050  0.0822  -0.0255 69  HIS   A NE2 
416  N N   . GLY   A 53  ? 0.9703 0.8288 1.1296 0.0876  0.0883  -0.0578 70  GLY   A N   
417  C CA  . GLY   A 53  ? 0.9851 0.8454 1.1410 0.0839  0.0891  -0.0649 70  GLY   A CA  
418  C C   . GLY   A 53  ? 0.9718 0.8632 1.1393 0.0830  0.0878  -0.0635 70  GLY   A C   
419  O O   . GLY   A 53  ? 0.9358 0.8299 1.0999 0.0797  0.0882  -0.0687 70  GLY   A O   
420  N N   . GLU   A 54  ? 0.9258 0.8398 1.1055 0.0853  0.0862  -0.0565 71  GLU   A N   
421  C CA  . GLU   A 54  ? 0.9620 0.9053 1.1516 0.0833  0.0853  -0.0545 71  GLU   A CA  
422  C C   . GLU   A 54  ? 0.9796 0.9386 1.1809 0.0737  0.0800  -0.0488 71  GLU   A C   
423  O O   . GLU   A 54  ? 0.9593 0.9078 1.1616 0.0690  0.0772  -0.0467 71  GLU   A O   
424  C CB  . GLU   A 54  ? 1.0054 0.9664 1.1982 0.0975  0.0898  -0.0522 71  GLU   A CB  
425  C CG  . GLU   A 54  ? 1.0241 0.9661 1.2041 0.1114  0.0952  -0.0564 71  GLU   A CG  
426  C CD  . GLU   A 54  ? 1.0499 0.9847 1.2203 0.1100  0.0982  -0.0639 71  GLU   A CD  
427  O OE1 . GLU   A 54  ? 1.0304 0.9846 1.2061 0.1033  0.0976  -0.0645 71  GLU   A OE1 
428  O OE2 . GLU   A 54  ? 0.9492 0.8573 1.1051 0.1154  0.1010  -0.0693 71  GLU   A OE2 
429  N N   . GLU   A 55  ? 1.0972 1.0807 1.3061 0.0704  0.0791  -0.0466 72  GLU   A N   
430  C CA  . GLU   A 55  ? 1.0911 1.0903 1.3093 0.0617  0.0743  -0.0413 72  GLU   A CA  
431  C C   . GLU   A 55  ? 1.0937 1.1094 1.3207 0.0690  0.0745  -0.0347 72  GLU   A C   
432  O O   . GLU   A 55  ? 1.1435 1.1694 1.3718 0.0804  0.0785  -0.0341 72  GLU   A O   
433  C CB  . GLU   A 55  ? 1.1614 1.1764 1.3808 0.0536  0.0731  -0.0419 72  GLU   A CB  
434  C CG  . GLU   A 55  ? 1.1870 1.1887 1.3966 0.0486  0.0731  -0.0486 72  GLU   A CG  
435  C CD  . GLU   A 55  ? 1.2655 1.2821 1.4731 0.0441  0.0740  -0.0490 72  GLU   A CD  
436  O OE1 . GLU   A 55  ? 1.2970 1.3344 1.5105 0.0468  0.0768  -0.0452 72  GLU   A OE1 
437  O OE2 . GLU   A 55  ? 1.1700 1.1780 1.3698 0.0377  0.0719  -0.0531 72  GLU   A OE2 
438  N N   . ASP   A 56  ? 0.9593 0.9783 1.1918 0.0630  0.0699  -0.0300 73  ASP   A N   
439  C CA  . ASP   A 56  ? 0.9028 0.9389 1.1437 0.0679  0.0687  -0.0236 73  ASP   A CA  
440  C C   . ASP   A 56  ? 0.9826 1.0410 1.2306 0.0577  0.0653  -0.0206 73  ASP   A C   
441  O O   . ASP   A 56  ? 0.9214 0.9774 1.1706 0.0488  0.0607  -0.0183 73  ASP   A O   
442  C CB  . ASP   A 56  ? 0.8713 0.8919 1.1108 0.0689  0.0662  -0.0205 73  ASP   A CB  
443  C CG  . ASP   A 56  ? 0.9064 0.9302 1.1469 0.0829  0.0679  -0.0165 73  ASP   A CG  
444  O OD1 . ASP   A 56  ? 0.9272 0.9757 1.1752 0.0892  0.0686  -0.0142 73  ASP   A OD1 
445  O OD2 . ASP   A 56  ? 0.9525 0.9544 1.1860 0.0875  0.0684  -0.0158 73  ASP   A OD2 
446  N N   . LEU   A 57  ? 1.0086 1.0882 1.2602 0.0590  0.0681  -0.0208 74  LEU   A N   
447  C CA  . LEU   A 57  ? 0.9745 1.0737 1.2304 0.0480  0.0658  -0.0184 74  LEU   A CA  
448  C C   . LEU   A 57  ? 0.9133 1.0336 1.1788 0.0480  0.0630  -0.0125 74  LEU   A C   
449  O O   . LEU   A 57  ? 0.9186 1.0599 1.1884 0.0401  0.0622  -0.0104 74  LEU   A O   
450  C CB  . LEU   A 57  ? 0.9603 1.0732 1.2148 0.0473  0.0705  -0.0212 74  LEU   A CB  
451  C CG  . LEU   A 57  ? 1.0105 1.1042 1.2541 0.0459  0.0727  -0.0273 74  LEU   A CG  
452  C CD1 . LEU   A 57  ? 0.9654 1.0750 1.2074 0.0459  0.0780  -0.0294 74  LEU   A CD1 
453  C CD2 . LEU   A 57  ? 1.0696 1.1474 1.3066 0.0339  0.0675  -0.0282 74  LEU   A CD2 
454  N N   . LYS   A 58  ? 0.8357 0.9501 1.1035 0.0561  0.0614  -0.0098 75  LYS   A N   
455  C CA  . LYS   A 58  ? 0.8210 0.9546 1.0971 0.0567  0.0580  -0.0043 75  LYS   A CA  
456  C C   . LYS   A 58  ? 0.8043 0.9343 1.0797 0.0440  0.0521  -0.0014 75  LYS   A C   
457  O O   . LYS   A 58  ? 0.8257 0.9745 1.1073 0.0411  0.0488  0.0028  75  LYS   A O   
458  C CB  . LYS   A 58  ? 0.7714 0.8986 1.0480 0.0715  0.0585  -0.0021 75  LYS   A CB  
459  N N   . VAL   A 59  ? 0.7502 0.8575 1.0179 0.0367  0.0504  -0.0037 76  VAL   A N   
460  C CA  . VAL   A 59  ? 0.7085 0.8106 0.9738 0.0259  0.0450  -0.0016 76  VAL   A CA  
461  C C   . VAL   A 59  ? 0.7754 0.8716 1.0338 0.0147  0.0439  -0.0045 76  VAL   A C   
462  O O   . VAL   A 59  ? 0.7537 0.8455 1.0083 0.0057  0.0395  -0.0032 76  VAL   A O   
463  C CB  . VAL   A 59  ? 0.7774 0.8583 1.0394 0.0287  0.0433  -0.0011 76  VAL   A CB  
464  C CG1 . VAL   A 59  ? 0.7979 0.8668 1.0548 0.0185  0.0389  -0.0014 76  VAL   A CG1 
465  C CG2 . VAL   A 59  ? 0.8121 0.9005 1.0788 0.0371  0.0424  0.0037  76  VAL   A CG2 
466  N N   . GLN   A 60  ? 0.7318 0.8291 0.9876 0.0153  0.0479  -0.0082 77  GLN   A N   
467  C CA  . GLN   A 60  ? 0.7576 0.8485 1.0048 0.0056  0.0468  -0.0108 77  GLN   A CA  
468  C C   . GLN   A 60  ? 0.7327 0.8378 0.9791 -0.0050 0.0442  -0.0072 77  GLN   A C   
469  O O   . GLN   A 60  ? 0.6806 0.8081 0.9341 -0.0050 0.0461  -0.0046 77  GLN   A O   
470  C CB  . GLN   A 60  ? 0.7888 0.8798 1.0328 0.0090  0.0520  -0.0151 77  GLN   A CB  
471  C CG  . GLN   A 60  ? 0.8348 0.9260 1.0697 -0.0009 0.0518  -0.0164 77  GLN   A CG  
472  C CD  . GLN   A 60  ? 0.9199 1.0189 1.1531 0.0024  0.0579  -0.0194 77  GLN   A CD  
473  O OE1 . GLN   A 60  ? 0.8456 0.9309 1.0696 0.0019  0.0588  -0.0237 77  GLN   A OE1 
474  N NE2 . GLN   A 60  ? 0.9633 1.0855 1.2052 0.0062  0.0620  -0.0174 77  GLN   A NE2 
475  N N   . HIS   A 61  ? 0.7157 0.8078 0.9528 -0.0140 0.0399  -0.0074 78  HIS   A N   
476  C CA  . HIS   A 61  ? 0.6743 0.7740 0.9065 -0.0253 0.0372  -0.0043 78  HIS   A CA  
477  C C   . HIS   A 61  ? 0.8067 0.9170 1.0348 -0.0311 0.0412  -0.0051 78  HIS   A C   
478  O O   . HIS   A 61  ? 0.8318 0.9353 1.0552 -0.0281 0.0445  -0.0088 78  HIS   A O   
479  C CB  . HIS   A 61  ? 0.6435 0.7227 0.8637 -0.0318 0.0316  -0.0047 78  HIS   A CB  
480  C CG  . HIS   A 61  ? 0.7488 0.8317 0.9637 -0.0421 0.0277  -0.0010 78  HIS   A CG  
481  N ND1 . HIS   A 61  ? 0.7590 0.8431 0.9633 -0.0530 0.0278  -0.0001 78  HIS   A ND1 
482  C CD2 . HIS   A 61  ? 0.7225 0.8070 0.9397 -0.0438 0.0236  0.0021  78  HIS   A CD2 
483  C CE1 . HIS   A 61  ? 0.7376 0.8230 0.9377 -0.0615 0.0238  0.0031  78  HIS   A CE1 
484  N NE2 . HIS   A 61  ? 0.7640 0.8502 0.9720 -0.0558 0.0211  0.0044  78  HIS   A NE2 
485  N N   . SER   A 62  ? 0.8122 0.9398 1.0415 -0.0401 0.0409  -0.0017 79  SER   A N   
486  C CA  . SER   A 62  ? 0.8014 0.9416 1.0267 -0.0476 0.0454  -0.0020 79  SER   A CA  
487  C C   . SER   A 62  ? 0.8154 0.9331 1.0223 -0.0545 0.0446  -0.0041 79  SER   A C   
488  O O   . SER   A 62  ? 0.8093 0.9287 1.0113 -0.0550 0.0494  -0.0063 79  SER   A O   
489  C CB  . SER   A 62  ? 0.8889 1.0508 1.1178 -0.0586 0.0445  0.0020  79  SER   A CB  
490  O OG  . SER   A 62  ? 0.9306 1.1170 1.1769 -0.0509 0.0452  0.0037  79  SER   A OG  
491  N N   . SER   A 63  ? 0.8917 0.9877 1.0870 -0.0590 0.0386  -0.0036 80  SER   A N   
492  C CA  . SER   A 63  ? 0.9429 1.0160 1.1188 -0.0641 0.0369  -0.0055 80  SER   A CA  
493  C C   . SER   A 63  ? 0.9498 1.0122 1.1241 -0.0546 0.0389  -0.0103 80  SER   A C   
494  O O   . SER   A 63  ? 0.9389 0.9873 1.0979 -0.0577 0.0388  -0.0122 80  SER   A O   
495  C CB  . SER   A 63  ? 0.9118 0.9642 1.0765 -0.0674 0.0297  -0.0045 80  SER   A CB  
496  O OG  . SER   A 63  ? 1.0805 1.1386 1.2417 -0.0783 0.0276  -0.0005 80  SER   A OG  
497  N N   . TYR   A 64  ? 0.8802 0.9477 1.0685 -0.0434 0.0404  -0.0123 81  TYR   A N   
498  C CA  . TYR   A 64  ? 0.8581 0.9151 1.0451 -0.0351 0.0421  -0.0174 81  TYR   A CA  
499  C C   . TYR   A 64  ? 0.8391 0.9111 1.0346 -0.0287 0.0491  -0.0191 81  TYR   A C   
500  O O   . TYR   A 64  ? 0.8168 0.8800 1.0091 -0.0228 0.0511  -0.0236 81  TYR   A O   
501  C CB  . TYR   A 64  ? 0.7099 0.7557 0.9027 -0.0278 0.0384  -0.0193 81  TYR   A CB  
502  C CG  . TYR   A 64  ? 0.6060 0.6347 0.7880 -0.0319 0.0319  -0.0194 81  TYR   A CG  
503  C CD1 . TYR   A 64  ? 0.5697 0.5831 0.7371 -0.0332 0.0295  -0.0227 81  TYR   A CD1 
504  C CD2 . TYR   A 64  ? 0.6139 0.6420 0.7991 -0.0335 0.0279  -0.0164 81  TYR   A CD2 
505  C CE1 . TYR   A 64  ? 0.6299 0.6282 0.7866 -0.0350 0.0233  -0.0231 81  TYR   A CE1 
506  C CE2 . TYR   A 64  ? 0.5887 0.6014 0.7633 -0.0360 0.0221  -0.0169 81  TYR   A CE2 
507  C CZ  . TYR   A 64  ? 0.6361 0.6342 0.7966 -0.0362 0.0198  -0.0203 81  TYR   A CZ  
508  O OH  . TYR   A 64  ? 0.6776 0.6607 0.8267 -0.0367 0.0139  -0.0210 81  TYR   A OH  
509  N N   . ARG   A 65  ? 0.9528 1.0477 1.1585 -0.0295 0.0527  -0.0159 82  ARG   A N   
510  C CA  . ARG   A 65  ? 0.9315 1.0428 1.1432 -0.0238 0.0598  -0.0176 82  ARG   A CA  
511  C C   . ARG   A 65  ? 0.9423 1.0513 1.1405 -0.0309 0.0632  -0.0191 82  ARG   A C   
512  O O   . ARG   A 65  ? 0.9866 1.0901 1.1733 -0.0426 0.0608  -0.0169 82  ARG   A O   
513  C CB  . ARG   A 65  ? 0.8989 1.0387 1.1249 -0.0232 0.0623  -0.0138 82  ARG   A CB  
514  C CG  . ARG   A 65  ? 0.9367 1.0995 1.1671 -0.0210 0.0699  -0.0148 82  ARG   A CG  
515  C CD  . ARG   A 65  ? 0.9423 1.1299 1.1899 -0.0107 0.0724  -0.0134 82  ARG   A CD  
516  N NE  . ARG   A 65  ? 0.8727 1.0806 1.1282 -0.0186 0.0696  -0.0087 82  ARG   A NE  
517  C CZ  . ARG   A 65  ? 0.9131 1.1177 1.1738 -0.0174 0.0638  -0.0059 82  ARG   A CZ  
518  N NH1 . ARG   A 65  ? 0.9269 1.1092 1.1862 -0.0090 0.0607  -0.0069 82  ARG   A NH1 
519  N NH2 . ARG   A 65  ? 0.8110 1.0353 1.0778 -0.0256 0.0612  -0.0020 82  ARG   A NH2 
520  N N   . GLN   A 66  ? 0.7863 0.8973 0.9840 -0.0236 0.0687  -0.0230 83  GLN   A N   
521  C CA  . GLN   A 66  ? 0.8468 0.9541 1.0310 -0.0279 0.0727  -0.0254 83  GLN   A CA  
522  C C   . GLN   A 66  ? 0.8699 0.9500 1.0360 -0.0330 0.0674  -0.0271 83  GLN   A C   
523  O O   . GLN   A 66  ? 0.8777 0.9515 1.0292 -0.0374 0.0697  -0.0285 83  GLN   A O   
524  C CB  . GLN   A 66  ? 0.7942 0.9231 0.9774 -0.0384 0.0775  -0.0219 83  GLN   A CB  
525  N N   . ARG   A 67  ? 0.7839 0.8484 0.9498 -0.0319 0.0603  -0.0271 84  ARG   A N   
526  C CA  . ARG   A 67  ? 0.7866 0.8269 0.9368 -0.0340 0.0546  -0.0294 84  ARG   A CA  
527  C C   . ARG   A 67  ? 0.7053 0.7331 0.8599 -0.0249 0.0511  -0.0341 84  ARG   A C   
528  O O   . ARG   A 67  ? 0.6677 0.6794 0.8106 -0.0239 0.0478  -0.0379 84  ARG   A O   
529  C CB  . ARG   A 67  ? 0.7865 0.8187 0.9292 -0.0428 0.0486  -0.0252 84  ARG   A CB  
530  C CG  . ARG   A 67  ? 0.7430 0.7792 0.8739 -0.0550 0.0506  -0.0211 84  ARG   A CG  
531  C CD  . ARG   A 67  ? 0.6904 0.7064 0.8046 -0.0623 0.0437  -0.0189 84  ARG   A CD  
532  N NE  . ARG   A 67  ? 0.6937 0.7087 0.8174 -0.0602 0.0385  -0.0174 84  ARG   A NE  
533  C CZ  . ARG   A 67  ? 0.7024 0.6981 0.8173 -0.0583 0.0315  -0.0183 84  ARG   A CZ  
534  N NH1 . ARG   A 67  ? 0.6481 0.6237 0.7444 -0.0574 0.0282  -0.0207 84  ARG   A NH1 
535  N NH2 . ARG   A 67  ? 0.6354 0.6326 0.7597 -0.0565 0.0278  -0.0168 84  ARG   A NH2 
536  N N   . ALA   A 68  ? 0.6793 0.7140 0.8495 -0.0186 0.0517  -0.0338 85  ALA   A N   
537  C CA  . ALA   A 68  ? 0.6661 0.6892 0.8408 -0.0121 0.0488  -0.0378 85  ALA   A CA  
538  C C   . ALA   A 68  ? 0.7131 0.7378 0.8929 -0.0035 0.0541  -0.0419 85  ALA   A C   
539  O O   . ALA   A 68  ? 0.7522 0.7910 0.9399 0.0005  0.0596  -0.0401 85  ALA   A O   
540  C CB  . ALA   A 68  ? 0.6479 0.6734 0.8335 -0.0115 0.0456  -0.0345 85  ALA   A CB  
541  N N   . ARG   A 69  ? 0.6530 0.6632 0.8276 -0.0005 0.0523  -0.0478 86  ARG   A N   
542  C CA  . ARG   A 69  ? 0.7251 0.7316 0.9021 0.0071  0.0566  -0.0524 86  ARG   A CA  
543  C C   . ARG   A 69  ? 0.6865 0.6774 0.8621 0.0078  0.0523  -0.0577 86  ARG   A C   
544  O O   . ARG   A 69  ? 0.6708 0.6542 0.8387 0.0038  0.0471  -0.0602 86  ARG   A O   
545  C CB  . ARG   A 69  ? 0.7101 0.7179 0.8775 0.0087  0.0614  -0.0556 86  ARG   A CB  
546  C CG  . ARG   A 69  ? 0.7314 0.7303 0.8837 0.0029  0.0576  -0.0577 86  ARG   A CG  
547  C CD  . ARG   A 69  ? 0.8230 0.8219 0.9646 0.0048  0.0628  -0.0611 86  ARG   A CD  
548  N NE  . ARG   A 69  ? 0.9374 0.9260 1.0770 0.0114  0.0643  -0.0680 86  ARG   A NE  
549  C CZ  . ARG   A 69  ? 0.9992 0.9755 1.1260 0.0112  0.0621  -0.0738 86  ARG   A CZ  
550  N NH1 . ARG   A 69  ? 0.9223 0.8941 1.0363 0.0059  0.0582  -0.0735 86  ARG   A NH1 
551  N NH2 . ARG   A 69  ? 0.9792 0.9461 1.1045 0.0165  0.0636  -0.0802 86  ARG   A NH2 
552  N N   . LEU   A 70  ? 0.7064 0.6927 0.8888 0.0129  0.0545  -0.0595 87  LEU   A N   
553  C CA  . LEU   A 70  ? 0.7411 0.7133 0.9219 0.0124  0.0517  -0.0653 87  LEU   A CA  
554  C C   . LEU   A 70  ? 0.7278 0.6911 0.8999 0.0159  0.0549  -0.0719 87  LEU   A C   
555  O O   . LEU   A 70  ? 0.7388 0.7042 0.9103 0.0220  0.0610  -0.0717 87  LEU   A O   
556  C CB  . LEU   A 70  ? 0.7044 0.6726 0.8944 0.0142  0.0523  -0.0637 87  LEU   A CB  
557  C CG  . LEU   A 70  ? 0.7915 0.7559 0.9848 0.0216  0.0581  -0.0628 87  LEU   A CG  
558  C CD1 . LEU   A 70  ? 0.8169 0.7659 1.0022 0.0247  0.0610  -0.0699 87  LEU   A CD1 
559  C CD2 . LEU   A 70  ? 0.7377 0.6989 0.9385 0.0207  0.0566  -0.0595 87  LEU   A CD2 
560  N N   . LEU   A 71  ? 0.7074 0.6619 0.8722 0.0125  0.0507  -0.0780 88  LEU   A N   
561  C CA  . LEU   A 71  ? 0.7209 0.6657 0.8757 0.0149  0.0529  -0.0850 88  LEU   A CA  
562  C C   . LEU   A 71  ? 0.7543 0.6875 0.9114 0.0179  0.0562  -0.0884 88  LEU   A C   
563  O O   . LEU   A 71  ? 0.7803 0.7055 0.9392 0.0137  0.0529  -0.0921 88  LEU   A O   
564  C CB  . LEU   A 71  ? 0.7632 0.7032 0.9095 0.0103  0.0464  -0.0906 88  LEU   A CB  
565  C CG  . LEU   A 71  ? 0.8157 0.7627 0.9582 0.0068  0.0413  -0.0871 88  LEU   A CG  
566  C CD1 . LEU   A 71  ? 0.8032 0.7442 0.9348 0.0049  0.0351  -0.0935 88  LEU   A CD1 
567  C CD2 . LEU   A 71  ? 0.7950 0.7496 0.9330 0.0080  0.0458  -0.0817 88  LEU   A CD2 
568  N N   . LYS   A 72  ? 0.7732 0.7053 0.9293 0.0254  0.0629  -0.0873 89  LYS   A N   
569  C CA  . LYS   A 72  ? 0.7299 0.6472 0.8849 0.0295  0.0665  -0.0900 89  LYS   A CA  
570  C C   . LYS   A 72  ? 0.6972 0.5974 0.8410 0.0269  0.0656  -0.0992 89  LYS   A C   
571  O O   . LYS   A 72  ? 0.6827 0.5679 0.8251 0.0251  0.0659  -0.1024 89  LYS   A O   
572  C CB  . LYS   A 72  ? 0.6662 0.5866 0.8209 0.0402  0.0737  -0.0870 89  LYS   A CB  
573  C CG  . LYS   A 72  ? 0.6551 0.5811 0.8202 0.0444  0.0752  -0.0800 89  LYS   A CG  
574  C CD  . LYS   A 72  ? 0.7803 0.7185 0.9475 0.0553  0.0812  -0.0763 89  LYS   A CD  
575  C CE  . LYS   A 72  ? 0.7187 0.6490 0.8740 0.0625  0.0864  -0.0823 89  LYS   A CE  
576  N NZ  . LYS   A 72  ? 0.7186 0.6478 0.8731 0.0763  0.0925  -0.0809 89  LYS   A NZ  
577  N N   . ASP   A 73  ? 0.6618 0.5633 0.7965 0.0261  0.0644  -0.1035 90  ASP   A N   
578  C CA  . ASP   A 73  ? 0.6601 0.5465 0.7835 0.0230  0.0626  -0.1128 90  ASP   A CA  
579  C C   . ASP   A 73  ? 0.7874 0.6716 0.9154 0.0135  0.0558  -0.1161 90  ASP   A C   
580  O O   . ASP   A 73  ? 0.8064 0.6764 0.9292 0.0095  0.0552  -0.1230 90  ASP   A O   
581  C CB  . ASP   A 73  ? 0.6971 0.5871 0.8095 0.0239  0.0620  -0.1161 90  ASP   A CB  
582  C CG  . ASP   A 73  ? 0.8477 0.7528 0.9633 0.0197  0.0567  -0.1119 90  ASP   A CG  
583  O OD1 . ASP   A 73  ? 0.7842 0.6990 0.9114 0.0177  0.0549  -0.1054 90  ASP   A OD1 
584  O OD2 . ASP   A 73  ? 0.8166 0.7221 0.9216 0.0185  0.0541  -0.1151 90  ASP   A OD2 
585  N N   . GLN   A 74  ? 0.7692 0.6675 0.9062 0.0095  0.0507  -0.1117 91  GLN   A N   
586  C CA  . GLN   A 74  ? 0.7410 0.6411 0.8835 0.0016  0.0443  -0.1149 91  GLN   A CA  
587  C C   . GLN   A 74  ? 0.7425 0.6375 0.8939 -0.0015 0.0461  -0.1131 91  GLN   A C   
588  O O   . GLN   A 74  ? 0.6971 0.5923 0.8525 -0.0090 0.0421  -0.1171 91  GLN   A O   
589  C CB  . GLN   A 74  ? 0.6905 0.6059 0.8377 0.0000  0.0384  -0.1109 91  GLN   A CB  
590  C CG  . GLN   A 74  ? 0.6799 0.5978 0.8159 0.0007  0.0344  -0.1141 91  GLN   A CG  
591  C CD  . GLN   A 74  ? 0.6947 0.6102 0.8263 -0.0040 0.0281  -0.1232 91  GLN   A CD  
592  O OE1 . GLN   A 74  ? 0.6184 0.5376 0.7585 -0.0091 0.0243  -0.1257 91  GLN   A OE1 
593  N NE2 . GLN   A 74  ? 0.6838 0.5944 0.8021 -0.0025 0.0269  -0.1285 91  GLN   A NE2 
594  N N   . LEU   A 75  ? 0.8097 0.7008 0.9638 0.0041  0.0520  -0.1072 92  LEU   A N   
595  C CA  . LEU   A 75  ? 0.7827 0.6662 0.9425 0.0015  0.0539  -0.1051 92  LEU   A CA  
596  C C   . LEU   A 75  ? 0.8477 0.7112 0.9988 -0.0031 0.0557  -0.1126 92  LEU   A C   
597  O O   . LEU   A 75  ? 0.8858 0.7437 1.0406 -0.0103 0.0553  -0.1136 92  LEU   A O   
598  C CB  . LEU   A 75  ? 0.7871 0.6703 0.9498 0.0101  0.0594  -0.0972 92  LEU   A CB  
599  C CG  . LEU   A 75  ? 0.7766 0.6791 0.9481 0.0135  0.0583  -0.0891 92  LEU   A CG  
600  C CD1 . LEU   A 75  ? 0.7999 0.7024 0.9754 0.0211  0.0630  -0.0821 92  LEU   A CD1 
601  C CD2 . LEU   A 75  ? 0.7833 0.6968 0.9633 0.0061  0.0522  -0.0874 92  LEU   A CD2 
602  N N   . SER   A 76  ? 0.8712 0.7231 1.0099 0.0004  0.0581  -0.1182 93  SER   A N   
603  C CA  . SER   A 76  ? 0.8363 0.6677 0.9643 -0.0054 0.0591  -0.1266 93  SER   A CA  
604  C C   . SER   A 76  ? 0.8470 0.6855 0.9794 -0.0178 0.0525  -0.1329 93  SER   A C   
605  O O   . SER   A 76  ? 0.9032 0.7310 1.0347 -0.0268 0.0529  -0.1367 93  SER   A O   
606  C CB  . SER   A 76  ? 0.8074 0.6273 0.9206 0.0008  0.0619  -0.1319 93  SER   A CB  
607  O OG  . SER   A 76  ? 0.9045 0.7413 1.0188 0.0051  0.0596  -0.1307 93  SER   A OG  
608  N N   . LEU   A 77  ? 0.7325 0.5891 0.8688 -0.0185 0.0465  -0.1341 94  LEU   A N   
609  C CA  . LEU   A 77  ? 0.7408 0.6086 0.8819 -0.0280 0.0393  -0.1402 94  LEU   A CA  
610  C C   . LEU   A 77  ? 0.6822 0.5651 0.8383 -0.0321 0.0367  -0.1355 94  LEU   A C   
611  O O   . LEU   A 77  ? 0.7637 0.6613 0.9260 -0.0377 0.0303  -0.1395 94  LEU   A O   
612  C CB  . LEU   A 77  ? 0.7065 0.5857 0.8430 -0.0249 0.0337  -0.1432 94  LEU   A CB  
613  C CG  . LEU   A 77  ? 0.7867 0.6528 0.9073 -0.0207 0.0359  -0.1483 94  LEU   A CG  
614  C CD1 . LEU   A 77  ? 0.6957 0.5727 0.8116 -0.0144 0.0329  -0.1464 94  LEU   A CD1 
615  C CD2 . LEU   A 77  ? 0.8895 0.7464 1.0023 -0.0293 0.0329  -0.1594 94  LEU   A CD2 
616  N N   . GLY   A 78  ? 0.6744 0.5548 0.8361 -0.0287 0.0413  -0.1273 95  GLY   A N   
617  C CA  . GLY   A 78  ? 0.6825 0.5757 0.8571 -0.0322 0.0395  -0.1226 95  GLY   A CA  
618  C C   . GLY   A 78  ? 0.6502 0.5635 0.8316 -0.0286 0.0338  -0.1190 95  GLY   A C   
619  O O   . GLY   A 78  ? 0.6490 0.5754 0.8393 -0.0330 0.0297  -0.1195 95  GLY   A O   
620  N N   . ASN   A 79  ? 0.6778 0.5930 0.8540 -0.0208 0.0339  -0.1156 96  ASN   A N   
621  C CA  . ASN   A 79  ? 0.6329 0.5627 0.8118 -0.0174 0.0291  -0.1115 96  ASN   A CA  
622  C C   . ASN   A 79  ? 0.6683 0.5988 0.8487 -0.0111 0.0334  -0.1022 96  ASN   A C   
623  O O   . ASN   A 79  ? 0.6218 0.5483 0.7953 -0.0059 0.0368  -0.1008 96  ASN   A O   
624  C CB  . ASN   A 79  ? 0.6372 0.5693 0.8064 -0.0156 0.0245  -0.1165 96  ASN   A CB  
625  C CG  . ASN   A 79  ? 0.6325 0.5767 0.8018 -0.0131 0.0185  -0.1133 96  ASN   A CG  
626  O OD1 . ASN   A 79  ? 0.5928 0.5444 0.7702 -0.0132 0.0173  -0.1083 96  ASN   A OD1 
627  N ND2 . ASN   A 79  ? 0.6145 0.5589 0.7730 -0.0106 0.0147  -0.1164 96  ASN   A ND2 
628  N N   . ALA   A 80  ? 0.6593 0.5964 0.8488 -0.0117 0.0332  -0.0962 97  ALA   A N   
629  C CA  . ALA   A 80  ? 0.6105 0.5514 0.8023 -0.0066 0.0360  -0.0875 97  ALA   A CA  
630  C C   . ALA   A 80  ? 0.6249 0.5754 0.8135 -0.0055 0.0313  -0.0851 97  ALA   A C   
631  O O   . ALA   A 80  ? 0.7194 0.6770 0.9119 -0.0072 0.0269  -0.0829 97  ALA   A O   
632  C CB  . ALA   A 80  ? 0.5494 0.4917 0.7502 -0.0079 0.0375  -0.0822 97  ALA   A CB  
633  N N   . ALA   A 81  ? 0.6251 0.5743 0.8049 -0.0025 0.0324  -0.0856 98  ALA   A N   
634  C CA  . ALA   A 81  ? 0.6811 0.6353 0.8535 -0.0022 0.0283  -0.0842 98  ALA   A CA  
635  C C   . ALA   A 81  ? 0.6644 0.6236 0.8364 -0.0002 0.0320  -0.0765 98  ALA   A C   
636  O O   . ALA   A 81  ? 0.6767 0.6354 0.8474 0.0029  0.0378  -0.0756 98  ALA   A O   
637  C CB  . ALA   A 81  ? 0.6528 0.6020 0.8135 -0.0015 0.0266  -0.0907 98  ALA   A CB  
638  N N   . LEU   A 82  ? 0.6150 0.5794 0.7876 -0.0019 0.0286  -0.0714 99  LEU   A N   
639  C CA  . LEU   A 82  ? 0.6203 0.5909 0.7925 -0.0021 0.0313  -0.0643 99  LEU   A CA  
640  C C   . LEU   A 82  ? 0.6334 0.6022 0.7917 -0.0040 0.0286  -0.0637 99  LEU   A C   
641  O O   . LEU   A 82  ? 0.5906 0.5547 0.7418 -0.0050 0.0224  -0.0657 99  LEU   A O   
642  C CB  . LEU   A 82  ? 0.5523 0.5278 0.7326 -0.0039 0.0295  -0.0587 99  LEU   A CB  
643  C CG  . LEU   A 82  ? 0.5932 0.5767 0.7743 -0.0054 0.0317  -0.0514 99  LEU   A CG  
644  C CD1 . LEU   A 82  ? 0.6469 0.6367 0.8298 -0.0026 0.0385  -0.0503 99  LEU   A CD1 
645  C CD2 . LEU   A 82  ? 0.5675 0.5552 0.7578 -0.0063 0.0305  -0.0468 99  LEU   A CD2 
646  N N   . GLN   A 83  ? 0.6413 0.6140 0.7951 -0.0042 0.0335  -0.0610 100 GLN   A N   
647  C CA  . GLN   A 83  ? 0.6246 0.5943 0.7632 -0.0072 0.0323  -0.0598 100 GLN   A CA  
648  C C   . GLN   A 83  ? 0.6192 0.5964 0.7580 -0.0118 0.0343  -0.0524 100 GLN   A C   
649  O O   . GLN   A 83  ? 0.6489 0.6376 0.7975 -0.0114 0.0398  -0.0492 100 GLN   A O   
650  C CB  . GLN   A 83  ? 0.6070 0.5751 0.7377 -0.0050 0.0370  -0.0636 100 GLN   A CB  
651  C CG  . GLN   A 83  ? 0.6999 0.6703 0.8185 -0.0089 0.0401  -0.0599 100 GLN   A CG  
652  C CD  . GLN   A 83  ? 0.7674 0.7310 0.8718 -0.0073 0.0418  -0.0647 100 GLN   A CD  
653  O OE1 . GLN   A 83  ? 0.7624 0.7160 0.8600 -0.0049 0.0368  -0.0703 100 GLN   A OE1 
654  N NE2 . GLN   A 83  ? 0.8312 0.8016 0.9312 -0.0085 0.0488  -0.0627 100 GLN   A NE2 
655  N N   . ILE   A 84  ? 0.6745 0.6450 0.8015 -0.0161 0.0294  -0.0499 101 ILE   A N   
656  C CA  . ILE   A 84  ? 0.6425 0.6171 0.7655 -0.0227 0.0306  -0.0433 101 ILE   A CA  
657  C C   . ILE   A 84  ? 0.6389 0.6048 0.7415 -0.0271 0.0309  -0.0428 101 ILE   A C   
658  O O   . ILE   A 84  ? 0.6669 0.6181 0.7547 -0.0258 0.0252  -0.0453 101 ILE   A O   
659  C CB  . ILE   A 84  ? 0.6309 0.6014 0.7548 -0.0249 0.0249  -0.0402 101 ILE   A CB  
660  C CG1 . ILE   A 84  ? 0.6175 0.5929 0.7587 -0.0199 0.0239  -0.0419 101 ILE   A CG1 
661  C CG2 . ILE   A 84  ? 0.6127 0.5896 0.7354 -0.0325 0.0268  -0.0336 101 ILE   A CG2 
662  C CD1 . ILE   A 84  ? 0.5333 0.5231 0.6905 -0.0190 0.0296  -0.0390 101 ILE   A CD1 
663  N N   . THR   A 85  ? 0.6574 0.6329 0.7585 -0.0319 0.0374  -0.0397 102 THR   A N   
664  C CA  . THR   A 85  ? 0.7554 0.7231 0.8361 -0.0377 0.0390  -0.0384 102 THR   A CA  
665  C C   . THR   A 85  ? 0.7370 0.7008 0.8075 -0.0477 0.0375  -0.0323 102 THR   A C   
666  O O   . THR   A 85  ? 0.6714 0.6473 0.7543 -0.0515 0.0386  -0.0285 102 THR   A O   
667  C CB  . THR   A 85  ? 0.6867 0.6677 0.7701 -0.0380 0.0478  -0.0391 102 THR   A CB  
668  O OG1 . THR   A 85  ? 0.7060 0.7079 0.8106 -0.0365 0.0527  -0.0372 102 THR   A OG1 
669  C CG2 . THR   A 85  ? 0.6662 0.6411 0.7465 -0.0300 0.0483  -0.0458 102 THR   A CG2 
670  N N   . ASP   A 86  ? 0.7586 0.7038 0.8046 -0.0521 0.0347  -0.0315 103 ASP   A N   
671  C CA  . ASP   A 86  ? 0.8171 0.7514 0.8471 -0.0622 0.0326  -0.0261 103 ASP   A CA  
672  C C   . ASP   A 86  ? 0.7888 0.7194 0.8257 -0.0607 0.0262  -0.0246 103 ASP   A C   
673  O O   . ASP   A 86  ? 0.8316 0.7720 0.8768 -0.0672 0.0275  -0.0205 103 ASP   A O   
674  C CB  . ASP   A 86  ? 0.8221 0.7726 0.8545 -0.0735 0.0405  -0.0215 103 ASP   A CB  
675  C CG  . ASP   A 86  ? 0.8941 0.8282 0.9018 -0.0863 0.0396  -0.0167 103 ASP   A CG  
676  O OD1 . ASP   A 86  ? 0.9696 0.8886 0.9545 -0.0896 0.0409  -0.0167 103 ASP   A OD1 
677  O OD2 . ASP   A 86  ? 0.9541 0.8890 0.9636 -0.0933 0.0374  -0.0130 103 ASP   A OD2 
678  N N   . VAL   A 87  ? 0.7453 0.6631 0.7789 -0.0517 0.0191  -0.0284 104 VAL   A N   
679  C CA  . VAL   A 87  ? 0.7857 0.6973 0.8220 -0.0493 0.0128  -0.0276 104 VAL   A CA  
680  C C   . VAL   A 87  ? 0.7253 0.6212 0.7412 -0.0585 0.0105  -0.0224 104 VAL   A C   
681  O O   . VAL   A 87  ? 0.7540 0.6307 0.7444 -0.0621 0.0092  -0.0214 104 VAL   A O   
682  C CB  . VAL   A 87  ? 0.7665 0.6674 0.7994 -0.0384 0.0057  -0.0330 104 VAL   A CB  
683  C CG1 . VAL   A 87  ? 0.6979 0.5912 0.7299 -0.0358 -0.0006 -0.0321 104 VAL   A CG1 
684  C CG2 . VAL   A 87  ? 0.7424 0.6589 0.7969 -0.0313 0.0080  -0.0382 104 VAL   A CG2 
685  N N   . LYS   A 88  ? 0.6978 0.6002 0.7233 -0.0626 0.0099  -0.0193 105 LYS   A N   
686  C CA  . LYS   A 88  ? 0.7722 0.6596 0.7795 -0.0719 0.0073  -0.0147 105 LYS   A CA  
687  C C   . LYS   A 88  ? 0.7833 0.6603 0.7901 -0.0654 0.0001  -0.0156 105 LYS   A C   
688  O O   . LYS   A 88  ? 0.7737 0.6596 0.7976 -0.0551 -0.0019 -0.0192 105 LYS   A O   
689  C CB  . LYS   A 88  ? 0.7704 0.6762 0.7881 -0.0842 0.0132  -0.0102 105 LYS   A CB  
690  N N   . LEU   A 89  ? 0.7832 0.6403 0.7687 -0.0717 -0.0035 -0.0123 106 LEU   A N   
691  C CA  . LEU   A 89  ? 0.7941 0.6380 0.7744 -0.0649 -0.0104 -0.0133 106 LEU   A CA  
692  C C   . LEU   A 89  ? 0.7842 0.6491 0.7921 -0.0613 -0.0099 -0.0138 106 LEU   A C   
693  O O   . LEU   A 89  ? 0.7709 0.6330 0.7830 -0.0515 -0.0145 -0.0167 106 LEU   A O   
694  C CB  . LEU   A 89  ? 0.8591 0.6786 0.8121 -0.0743 -0.0133 -0.0092 106 LEU   A CB  
695  C CG  . LEU   A 89  ? 0.8466 0.6323 0.7638 -0.0729 -0.0177 -0.0092 106 LEU   A CG  
696  C CD1 . LEU   A 89  ? 0.7252 0.5027 0.6397 -0.0553 -0.0239 -0.0144 106 LEU   A CD1 
697  C CD2 . LEU   A 89  ? 0.8156 0.5989 0.7210 -0.0818 -0.0124 -0.0074 106 LEU   A CD2 
698  N N   . GLN   A 90  ? 0.7484 0.6352 0.7747 -0.0687 -0.0044 -0.0112 107 GLN   A N   
699  C CA  . GLN   A 90  ? 0.7801 0.6855 0.8305 -0.0656 -0.0039 -0.0110 107 GLN   A CA  
700  C C   . GLN   A 90  ? 0.7318 0.6517 0.8036 -0.0546 -0.0022 -0.0152 107 GLN   A C   
701  O O   . GLN   A 90  ? 0.6724 0.6036 0.7615 -0.0504 -0.0023 -0.0155 107 GLN   A O   
702  C CB  . GLN   A 90  ? 0.8554 0.7801 0.9175 -0.0762 0.0009  -0.0067 107 GLN   A CB  
703  C CG  . GLN   A 90  ? 0.9426 0.8574 0.9846 -0.0909 0.0012  -0.0027 107 GLN   A CG  
704  C CD  . GLN   A 90  ? 0.9322 0.8390 0.9582 -0.0966 0.0044  -0.0025 107 GLN   A CD  
705  O OE1 . GLN   A 90  ? 0.9264 0.8316 0.9532 -0.0885 0.0055  -0.0058 107 GLN   A OE1 
706  N NE2 . GLN   A 90  ? 0.9659 0.8673 0.9763 -0.1114 0.0062  0.0011  107 GLN   A NE2 
707  N N   . ASP   A 91  ? 0.7362 0.6549 0.8057 -0.0505 -0.0007 -0.0185 108 ASP   A N   
708  C CA  . ASP   A 91  ? 0.7048 0.6343 0.7916 -0.0412 0.0005  -0.0232 108 ASP   A CA  
709  C C   . ASP   A 91  ? 0.6924 0.6124 0.7762 -0.0320 -0.0055 -0.0275 108 ASP   A C   
710  O O   . ASP   A 91  ? 0.7214 0.6490 0.8174 -0.0253 -0.0051 -0.0321 108 ASP   A O   
711  C CB  . ASP   A 91  ? 0.6898 0.6221 0.7747 -0.0408 0.0044  -0.0255 108 ASP   A CB  
712  C CG  . ASP   A 91  ? 0.7207 0.6689 0.8144 -0.0477 0.0115  -0.0222 108 ASP   A CG  
713  O OD1 . ASP   A 91  ? 0.7380 0.7023 0.8501 -0.0476 0.0141  -0.0205 108 ASP   A OD1 
714  O OD2 . ASP   A 91  ? 0.7674 0.7127 0.8491 -0.0528 0.0144  -0.0214 108 ASP   A OD2 
715  N N   . ALA   A 92  ? 0.6789 0.5830 0.7464 -0.0316 -0.0109 -0.0265 109 ALA   A N   
716  C CA  . ALA   A 92  ? 0.6643 0.5622 0.7296 -0.0220 -0.0166 -0.0307 109 ALA   A CA  
717  C C   . ALA   A 92  ? 0.6647 0.5731 0.7465 -0.0203 -0.0164 -0.0301 109 ALA   A C   
718  O O   . ALA   A 92  ? 0.6351 0.5445 0.7177 -0.0265 -0.0152 -0.0256 109 ALA   A O   
719  C CB  . ALA   A 92  ? 0.5376 0.4114 0.5748 -0.0203 -0.0227 -0.0301 109 ALA   A CB  
720  N N   . GLY   A 93  ? 0.5992 0.5161 0.6938 -0.0126 -0.0175 -0.0349 110 GLY   A N   
721  C CA  . GLY   A 93  ? 0.5739 0.5008 0.6837 -0.0109 -0.0167 -0.0347 110 GLY   A CA  
722  C C   . GLY   A 93  ? 0.5705 0.5115 0.6990 -0.0063 -0.0147 -0.0397 110 GLY   A C   
723  O O   . GLY   A 93  ? 0.5155 0.4573 0.6430 -0.0029 -0.0158 -0.0443 110 GLY   A O   
724  N N   . VAL   A 94  ? 0.6049 0.5561 0.7489 -0.0069 -0.0119 -0.0386 111 VAL   A N   
725  C CA  . VAL   A 94  ? 0.5610 0.5241 0.7218 -0.0042 -0.0094 -0.0429 111 VAL   A CA  
726  C C   . VAL   A 94  ? 0.5615 0.5318 0.7345 -0.0081 -0.0033 -0.0411 111 VAL   A C   
727  O O   . VAL   A 94  ? 0.5624 0.5355 0.7403 -0.0113 -0.0003 -0.0359 111 VAL   A O   
728  C CB  . VAL   A 94  ? 0.4945 0.4625 0.6625 -0.0021 -0.0098 -0.0431 111 VAL   A CB  
729  C CG1 . VAL   A 94  ? 0.5817 0.5612 0.7674 -0.0028 -0.0053 -0.0457 111 VAL   A CG1 
730  C CG2 . VAL   A 94  ? 0.5110 0.4747 0.6688 0.0044  -0.0156 -0.0470 111 VAL   A CG2 
731  N N   . TYR   A 95  ? 0.4856 0.4586 0.6626 -0.0071 -0.0017 -0.0455 112 TYR   A N   
732  C CA  . TYR   A 95  ? 0.5931 0.5712 0.7804 -0.0090 0.0041  -0.0449 112 TYR   A CA  
733  C C   . TYR   A 95  ? 0.5315 0.5152 0.7320 -0.0084 0.0066  -0.0481 112 TYR   A C   
734  O O   . TYR   A 95  ? 0.5233 0.5094 0.7254 -0.0068 0.0039  -0.0528 112 TYR   A O   
735  C CB  . TYR   A 95  ? 0.5929 0.5685 0.7747 -0.0087 0.0048  -0.0481 112 TYR   A CB  
736  C CG  . TYR   A 95  ? 0.6072 0.5776 0.7761 -0.0111 0.0043  -0.0443 112 TYR   A CG  
737  C CD1 . TYR   A 95  ? 0.6041 0.5656 0.7579 -0.0110 -0.0010 -0.0434 112 TYR   A CD1 
738  C CD2 . TYR   A 95  ? 0.5996 0.5735 0.7703 -0.0134 0.0093  -0.0418 112 TYR   A CD2 
739  C CE1 . TYR   A 95  ? 0.6503 0.6050 0.7903 -0.0149 -0.0010 -0.0399 112 TYR   A CE1 
740  C CE2 . TYR   A 95  ? 0.5637 0.5346 0.7229 -0.0170 0.0096  -0.0385 112 TYR   A CE2 
741  C CZ  . TYR   A 95  ? 0.6375 0.5980 0.7809 -0.0186 0.0045  -0.0374 112 TYR   A CZ  
742  O OH  . TYR   A 95  ? 0.5890 0.5445 0.7189 -0.0239 0.0052  -0.0340 112 TYR   A OH  
743  N N   . ARG   A 96  ? 0.4730 0.4587 0.6820 -0.0097 0.0120  -0.0455 113 ARG   A N   
744  C CA  . ARG   A 96  ? 0.5453 0.5328 0.7643 -0.0103 0.0153  -0.0478 113 ARG   A CA  
745  C C   . ARG   A 96  ? 0.5273 0.5121 0.7495 -0.0102 0.0204  -0.0488 113 ARG   A C   
746  O O   . ARG   A 96  ? 0.4854 0.4701 0.7078 -0.0090 0.0234  -0.0441 113 ARG   A O   
747  C CB  . ARG   A 96  ? 0.5192 0.5082 0.7428 -0.0109 0.0167  -0.0426 113 ARG   A CB  
748  C CG  . ARG   A 96  ? 0.4454 0.4371 0.6686 -0.0108 0.0132  -0.0441 113 ARG   A CG  
749  C CD  . ARG   A 96  ? 0.5084 0.5009 0.7355 -0.0115 0.0153  -0.0392 113 ARG   A CD  
750  N NE  . ARG   A 96  ? 0.6350 0.6281 0.8566 -0.0104 0.0111  -0.0378 113 ARG   A NE  
751  C CZ  . ARG   A 96  ? 0.6528 0.6425 0.8654 -0.0099 0.0077  -0.0343 113 ARG   A CZ  
752  N NH1 . ARG   A 96  ? 0.5666 0.5546 0.7760 -0.0112 0.0081  -0.0315 113 ARG   A NH1 
753  N NH2 . ARG   A 96  ? 0.6665 0.6543 0.8725 -0.0085 0.0040  -0.0338 113 ARG   A NH2 
754  N N   . CYS   A 97  ? 0.4406 0.4237 0.6648 -0.0113 0.0212  -0.0552 114 CYS   A N   
755  C CA  . CYS   A 97  ? 0.5438 0.5211 0.7694 -0.0113 0.0261  -0.0571 114 CYS   A CA  
756  C C   . CYS   A 97  ? 0.5360 0.5096 0.7675 -0.0141 0.0297  -0.0579 114 CYS   A C   
757  O O   . CYS   A 97  ? 0.4638 0.4407 0.6985 -0.0178 0.0280  -0.0622 114 CYS   A O   
758  C CB  . CYS   A 97  ? 0.5088 0.4841 0.7295 -0.0115 0.0247  -0.0640 114 CYS   A CB  
759  S SG  . CYS   A 97  ? 0.6458 0.6225 0.8695 -0.0159 0.0227  -0.0732 114 CYS   A SG  
760  N N   . MET   A 98  ? 0.4900 0.4571 0.7222 -0.0122 0.0345  -0.0537 115 MET   A N   
761  C CA  . MET   A 98  ? 0.5803 0.5397 0.8149 -0.0148 0.0386  -0.0534 115 MET   A CA  
762  C C   . MET   A 98  ? 0.5978 0.5446 0.8280 -0.0135 0.0432  -0.0559 115 MET   A C   
763  O O   . MET   A 98  ? 0.6045 0.5488 0.8318 -0.0074 0.0452  -0.0529 115 MET   A O   
764  C CB  . MET   A 98  ? 0.5321 0.4921 0.7685 -0.0124 0.0399  -0.0455 115 MET   A CB  
765  C CG  . MET   A 98  ? 0.5199 0.4907 0.7571 -0.0108 0.0353  -0.0415 115 MET   A CG  
766  S SD  . MET   A 98  ? 0.5845 0.5567 0.8233 -0.0089 0.0360  -0.0330 115 MET   A SD  
767  C CE  . MET   A 98  ? 0.4399 0.4224 0.6772 -0.0097 0.0298  -0.0314 115 MET   A CE  
768  N N   . ILE   A 99  ? 0.5680 0.5070 0.7972 -0.0192 0.0450  -0.0616 116 ILE   A N   
769  C CA  . ILE   A 99  ? 0.6227 0.5466 0.8451 -0.0190 0.0490  -0.0654 116 ILE   A CA  
770  C C   . ILE   A 99  ? 0.5938 0.5029 0.8133 -0.0235 0.0538  -0.0648 116 ILE   A C   
771  O O   . ILE   A 99  ? 0.5448 0.4575 0.7683 -0.0311 0.0535  -0.0663 116 ILE   A O   
772  C CB  . ILE   A 99  ? 0.5902 0.5161 0.8108 -0.0233 0.0464  -0.0743 116 ILE   A CB  
773  C CG1 . ILE   A 99  ? 0.6152 0.5503 0.8344 -0.0178 0.0428  -0.0743 116 ILE   A CG1 
774  C CG2 . ILE   A 99  ? 0.5971 0.5047 0.8095 -0.0255 0.0507  -0.0792 116 ILE   A CG2 
775  C CD1 . ILE   A 99  ? 0.5186 0.4686 0.7417 -0.0200 0.0365  -0.0764 116 ILE   A CD1 
776  N N   . SER   A 100 ? 0.6507 0.5428 0.8622 -0.0184 0.0584  -0.0627 117 SER   A N   
777  C CA  . SER   A 100 ? 0.6250 0.4968 0.8291 -0.0220 0.0635  -0.0620 117 SER   A CA  
778  C C   . SER   A 100 ? 0.6168 0.4689 0.8096 -0.0215 0.0668  -0.0674 117 SER   A C   
779  O O   . SER   A 100 ? 0.6435 0.4893 0.8308 -0.0113 0.0684  -0.0656 117 SER   A O   
780  C CB  . SER   A 100 ? 0.5576 0.4238 0.7596 -0.0144 0.0658  -0.0530 117 SER   A CB  
781  O OG  . SER   A 100 ? 0.5398 0.3841 0.7322 -0.0182 0.0707  -0.0519 117 SER   A OG  
782  N N   . TYR   A 101 ? 0.6222 0.4654 0.8114 -0.0327 0.0678  -0.0745 118 TYR   A N   
783  C CA  . TYR   A 101 ? 0.6700 0.4922 0.8466 -0.0347 0.0707  -0.0809 118 TYR   A CA  
784  C C   . TYR   A 101 ? 0.7475 0.5548 0.9185 -0.0487 0.0738  -0.0847 118 TYR   A C   
785  O O   . TYR   A 101 ? 0.7308 0.5457 0.9056 -0.0604 0.0718  -0.0923 118 TYR   A O   
786  C CB  . TYR   A 101 ? 0.6698 0.5028 0.8485 -0.0353 0.0667  -0.0884 118 TYR   A CB  
787  C CG  . TYR   A 101 ? 0.7377 0.5485 0.9021 -0.0363 0.0695  -0.0951 118 TYR   A CG  
788  C CD1 . TYR   A 101 ? 0.8216 0.6083 0.9725 -0.0275 0.0746  -0.0922 118 TYR   A CD1 
789  C CD2 . TYR   A 101 ? 0.7599 0.5736 0.9234 -0.0455 0.0667  -0.1046 118 TYR   A CD2 
790  C CE1 . TYR   A 101 ? 0.8580 0.6218 0.9936 -0.0278 0.0773  -0.0987 118 TYR   A CE1 
791  C CE2 . TYR   A 101 ? 0.8911 0.6833 1.0401 -0.0469 0.0690  -0.1112 118 TYR   A CE2 
792  C CZ  . TYR   A 101 ? 0.8844 0.6506 1.0190 -0.0380 0.0745  -0.1082 118 TYR   A CZ  
793  O OH  . TYR   A 101 ? 0.9696 0.7120 1.0877 -0.0388 0.0770  -0.1151 118 TYR   A OH  
794  N N   . GLY   A 102 ? 0.7858 0.5721 0.9472 -0.0477 0.0788  -0.0792 119 GLY   A N   
795  C CA  . GLY   A 102 ? 0.7772 0.5497 0.9329 -0.0617 0.0826  -0.0809 119 GLY   A CA  
796  C C   . GLY   A 102 ? 0.7621 0.5567 0.9316 -0.0668 0.0810  -0.0771 119 GLY   A C   
797  O O   . GLY   A 102 ? 0.8185 0.6035 0.9837 -0.0671 0.0845  -0.0706 119 GLY   A O   
798  N N   . GLY   A 103 ? 0.7047 0.5283 0.8895 -0.0701 0.0757  -0.0812 120 GLY   A N   
799  C CA  . GLY   A 103 ? 0.6673 0.5139 0.8653 -0.0731 0.0735  -0.0784 120 GLY   A CA  
800  C C   . GLY   A 103 ? 0.6637 0.5281 0.8702 -0.0601 0.0689  -0.0727 120 GLY   A C   
801  O O   . GLY   A 103 ? 0.6816 0.5401 0.8839 -0.0490 0.0683  -0.0696 120 GLY   A O   
802  N N   . ALA   A 104 ? 0.6215 0.5079 0.8395 -0.0619 0.0657  -0.0716 121 ALA   A N   
803  C CA  . ALA   A 104 ? 0.6215 0.5234 0.8460 -0.0514 0.0612  -0.0664 121 ALA   A CA  
804  C C   . ALA   A 104 ? 0.6018 0.5284 0.8377 -0.0547 0.0563  -0.0697 121 ALA   A C   
805  O O   . ALA   A 104 ? 0.6214 0.5550 0.8617 -0.0629 0.0577  -0.0716 121 ALA   A O   
806  C CB  . ALA   A 104 ? 0.6261 0.5209 0.8475 -0.0451 0.0636  -0.0567 121 ALA   A CB  
807  N N   . ASP   A 105 ? 0.5147 0.4540 0.7542 -0.0479 0.0507  -0.0703 122 ASP   A N   
808  C CA  . ASP   A 105 ? 0.5392 0.4996 0.7867 -0.0479 0.0453  -0.0728 122 ASP   A CA  
809  C C   . ASP   A 105 ? 0.6095 0.5752 0.8558 -0.0384 0.0405  -0.0696 122 ASP   A C   
810  O O   . ASP   A 105 ? 0.6355 0.5920 0.8766 -0.0333 0.0415  -0.0670 122 ASP   A O   
811  C CB  . ASP   A 105 ? 0.5398 0.5107 0.7915 -0.0551 0.0429  -0.0826 122 ASP   A CB  
812  C CG  . ASP   A 105 ? 0.5796 0.5724 0.8399 -0.0556 0.0386  -0.0852 122 ASP   A CG  
813  O OD1 . ASP   A 105 ? 0.5626 0.5595 0.8255 -0.0549 0.0400  -0.0804 122 ASP   A OD1 
814  O OD2 . ASP   A 105 ? 0.5685 0.5744 0.8320 -0.0558 0.0336  -0.0922 122 ASP   A OD2 
815  N N   . TYR   A 106 ? 0.6010 0.5815 0.8512 -0.0362 0.0355  -0.0699 123 TYR   A N   
816  C CA  . TYR   A 106 ? 0.5171 0.5014 0.7642 -0.0289 0.0308  -0.0670 123 TYR   A CA  
817  C C   . TYR   A 106 ? 0.5236 0.5217 0.7724 -0.0279 0.0246  -0.0720 123 TYR   A C   
818  O O   . TYR   A 106 ? 0.5035 0.5116 0.7580 -0.0312 0.0240  -0.0756 123 TYR   A O   
819  C CB  . TYR   A 106 ? 0.5272 0.5097 0.7731 -0.0248 0.0314  -0.0583 123 TYR   A CB  
820  C CG  . TYR   A 106 ? 0.6269 0.6196 0.8746 -0.0237 0.0277  -0.0571 123 TYR   A CG  
821  C CD1 . TYR   A 106 ? 0.5518 0.5490 0.8042 -0.0275 0.0297  -0.0578 123 TYR   A CD1 
822  C CD2 . TYR   A 106 ? 0.5066 0.5030 0.7498 -0.0190 0.0224  -0.0555 123 TYR   A CD2 
823  C CE1 . TYR   A 106 ? 0.5630 0.5693 0.8161 -0.0255 0.0266  -0.0571 123 TYR   A CE1 
824  C CE2 . TYR   A 106 ? 0.4931 0.4959 0.7355 -0.0172 0.0189  -0.0548 123 TYR   A CE2 
825  C CZ  . TYR   A 106 ? 0.5645 0.5728 0.8122 -0.0198 0.0210  -0.0557 123 TYR   A CZ  
826  O OH  . TYR   A 106 ? 0.6583 0.6729 0.9045 -0.0169 0.0178  -0.0553 123 TYR   A OH  
827  N N   . LYS   A 107 ? 0.5017 0.5002 0.7449 -0.0229 0.0202  -0.0721 124 LYS   A N   
828  C CA  . LYS   A 107 ? 0.5328 0.5411 0.7740 -0.0196 0.0136  -0.0760 124 LYS   A CA  
829  C C   . LYS   A 107 ? 0.4967 0.5004 0.7289 -0.0140 0.0103  -0.0707 124 LYS   A C   
830  O O   . LYS   A 107 ? 0.5260 0.5219 0.7541 -0.0133 0.0126  -0.0665 124 LYS   A O   
831  C CB  . LYS   A 107 ? 0.5568 0.5689 0.7972 -0.0208 0.0107  -0.0844 124 LYS   A CB  
832  C CG  . LYS   A 107 ? 0.6068 0.6269 0.8560 -0.0277 0.0126  -0.0911 124 LYS   A CG  
833  C CD  . LYS   A 107 ? 0.4922 0.5301 0.7461 -0.0262 0.0073  -0.0966 124 LYS   A CD  
834  C CE  . LYS   A 107 ? 0.5374 0.5861 0.8022 -0.0343 0.0110  -0.1007 124 LYS   A CE  
835  N NZ  . LYS   A 107 ? 0.5910 0.6304 0.8576 -0.0381 0.0179  -0.0938 124 LYS   A NZ  
836  N N   . ARG   A 108 ? 0.4893 0.4981 0.7178 -0.0101 0.0050  -0.0712 125 ARG   A N   
837  C CA  . ARG   A 108 ? 0.5284 0.5308 0.7460 -0.0060 0.0016  -0.0663 125 ARG   A CA  
838  C C   . ARG   A 108 ? 0.5346 0.5354 0.7420 -0.0020 -0.0041 -0.0704 125 ARG   A C   
839  O O   . ARG   A 108 ? 0.6031 0.6117 0.8123 0.0000  -0.0077 -0.0772 125 ARG   A O   
840  C CB  . ARG   A 108 ? 0.4662 0.4704 0.6825 -0.0038 -0.0003 -0.0630 125 ARG   A CB  
841  C CG  . ARG   A 108 ? 0.5618 0.5771 0.7825 -0.0013 -0.0032 -0.0689 125 ARG   A CG  
842  C CD  . ARG   A 108 ? 0.6940 0.7092 0.9110 0.0020  -0.0048 -0.0656 125 ARG   A CD  
843  N NE  . ARG   A 108 ? 0.7639 0.7835 0.9906 -0.0021 0.0005  -0.0631 125 ARG   A NE  
844  C CZ  . ARG   A 108 ? 0.7777 0.8090 1.0152 -0.0048 0.0032  -0.0676 125 ARG   A CZ  
845  N NH1 . ARG   A 108 ? 0.7573 0.8000 0.9992 -0.0039 0.0007  -0.0753 125 ARG   A NH1 
846  N NH2 . ARG   A 108 ? 0.7299 0.7620 0.9733 -0.0089 0.0084  -0.0643 125 ARG   A NH2 
847  N N   . ILE   A 109 ? 0.4992 0.4904 0.6953 -0.0010 -0.0050 -0.0663 126 ILE   A N   
848  C CA  . ILE   A 109 ? 0.5454 0.5313 0.7281 0.0026  -0.0102 -0.0688 126 ILE   A CA  
849  C C   . ILE   A 109 ? 0.5887 0.5643 0.7571 0.0043  -0.0131 -0.0632 126 ILE   A C   
850  O O   . ILE   A 109 ? 0.6056 0.5775 0.7739 0.0006  -0.0097 -0.0569 126 ILE   A O   
851  C CB  . ILE   A 109 ? 0.5544 0.5364 0.7344 0.0005  -0.0075 -0.0700 126 ILE   A CB  
852  C CG1 . ILE   A 109 ? 0.5567 0.5460 0.7478 -0.0015 -0.0054 -0.0766 126 ILE   A CG1 
853  C CG2 . ILE   A 109 ? 0.4832 0.4572 0.6463 0.0040  -0.0125 -0.0713 126 ILE   A CG2 
854  C CD1 . ILE   A 109 ? 0.5715 0.5568 0.7660 -0.0050 0.0009  -0.0754 126 ILE   A CD1 
855  N N   . THR   A 110 ? 0.5890 0.5596 0.7443 0.0100  -0.0195 -0.0656 127 THR   A N   
856  C CA  . THR   A 110 ? 0.5386 0.4954 0.6762 0.0116  -0.0229 -0.0609 127 THR   A CA  
857  C C   . THR   A 110 ? 0.5308 0.4754 0.6510 0.0118  -0.0249 -0.0606 127 THR   A C   
858  O O   . THR   A 110 ? 0.5160 0.4618 0.6322 0.0163  -0.0284 -0.0661 127 THR   A O   
859  C CB  . THR   A 110 ? 0.6075 0.5638 0.7392 0.0192  -0.0287 -0.0635 127 THR   A CB  
860  O OG1 . THR   A 110 ? 0.6531 0.6255 0.8032 0.0196  -0.0266 -0.0666 127 THR   A OG1 
861  C CG2 . THR   A 110 ? 0.6080 0.5497 0.7248 0.0189  -0.0303 -0.0577 127 THR   A CG2 
862  N N   . VAL   A 111 ? 0.5428 0.4766 0.6523 0.0066  -0.0228 -0.0544 128 VAL   A N   
863  C CA  . VAL   A 111 ? 0.5426 0.4641 0.6344 0.0048  -0.0234 -0.0531 128 VAL   A CA  
864  C C   . VAL   A 111 ? 0.5961 0.4986 0.6643 0.0057  -0.0280 -0.0496 128 VAL   A C   
865  O O   . VAL   A 111 ? 0.6328 0.5312 0.6993 0.0014  -0.0270 -0.0448 128 VAL   A O   
866  C CB  . VAL   A 111 ? 0.6187 0.5444 0.7168 -0.0033 -0.0162 -0.0491 128 VAL   A CB  
867  C CG1 . VAL   A 111 ? 0.5600 0.4718 0.6371 -0.0073 -0.0162 -0.0459 128 VAL   A CG1 
868  C CG2 . VAL   A 111 ? 0.6071 0.5454 0.7212 -0.0026 -0.0125 -0.0536 128 VAL   A CG2 
869  N N   . LYS   A 112 ? 0.6313 0.5208 0.6799 0.0113  -0.0333 -0.0520 129 LYS   A N   
870  C CA  . LYS   A 112 ? 0.6092 0.4752 0.6299 0.0121  -0.0376 -0.0487 129 LYS   A CA  
871  C C   . LYS   A 112 ? 0.6303 0.4834 0.6335 0.0059  -0.0354 -0.0458 129 LYS   A C   
872  O O   . LYS   A 112 ? 0.6402 0.4977 0.6445 0.0079  -0.0349 -0.0492 129 LYS   A O   
873  C CB  . LYS   A 112 ? 0.5966 0.4546 0.6042 0.0251  -0.0460 -0.0534 129 LYS   A CB  
874  N N   . VAL   A 113 ? 0.7041 0.5414 0.6905 -0.0023 -0.0339 -0.0397 130 VAL   A N   
875  C CA  . VAL   A 113 ? 0.6932 0.5197 0.6634 -0.0109 -0.0304 -0.0362 130 VAL   A CA  
876  C C   . VAL   A 113 ? 0.6419 0.4374 0.5767 -0.0101 -0.0355 -0.0337 130 VAL   A C   
877  O O   . VAL   A 113 ? 0.6738 0.4561 0.5972 -0.0144 -0.0367 -0.0299 130 VAL   A O   
878  C CB  . VAL   A 113 ? 0.7152 0.5532 0.6977 -0.0240 -0.0227 -0.0311 130 VAL   A CB  
879  C CG1 . VAL   A 113 ? 0.7239 0.5527 0.6893 -0.0335 -0.0184 -0.0277 130 VAL   A CG1 
880  C CG2 . VAL   A 113 ? 0.5748 0.4403 0.5897 -0.0230 -0.0178 -0.0334 130 VAL   A CG2 
881  N N   . ASN   A 114 ? 0.6614 0.4435 0.5768 -0.0045 -0.0389 -0.0359 131 ASN   A N   
882  C CA  . ASN   A 114 ? 0.7263 0.4752 0.6039 -0.0049 -0.0428 -0.0327 131 ASN   A CA  
883  C C   . ASN   A 114 ? 0.7552 0.4957 0.6203 -0.0209 -0.0358 -0.0269 131 ASN   A C   
884  O O   . ASN   A 114 ? 0.8256 0.5849 0.7069 -0.0272 -0.0292 -0.0270 131 ASN   A O   
885  C CB  . ASN   A 114 ? 0.7042 0.4415 0.5641 0.0081  -0.0494 -0.0372 131 ASN   A CB  
886  C CG  . ASN   A 114 ? 0.6848 0.4332 0.5570 0.0240  -0.0566 -0.0435 131 ASN   A CG  
887  O OD1 . ASN   A 114 ? 0.6752 0.4284 0.5572 0.0266  -0.0580 -0.0436 131 ASN   A OD1 
888  N ND2 . ASN   A 114 ? 0.6871 0.4411 0.5588 0.0344  -0.0610 -0.0491 131 ASN   A ND2 
889  N N   . ALA   A 115 ? 0.7188 0.4309 0.5540 -0.0276 -0.0372 -0.0221 132 ALA   A N   
890  C CA  . ALA   A 115 ? 0.7643 0.4697 0.5877 -0.0451 -0.0302 -0.0164 132 ALA   A CA  
891  C C   . ALA   A 115 ? 0.7836 0.4479 0.5629 -0.0490 -0.0337 -0.0125 132 ALA   A C   
892  O O   . ALA   A 115 ? 0.8488 0.4918 0.6111 -0.0403 -0.0409 -0.0131 132 ALA   A O   
893  C CB  . ALA   A 115 ? 0.7749 0.5005 0.6212 -0.0573 -0.0247 -0.0133 132 ALA   A CB  
894  N N   . PRO   A 116 ? 0.8472 0.4991 0.6065 -0.0620 -0.0285 -0.0085 133 PRO   A N   
895  C CA  . PRO   A 116 ? 0.8426 0.4522 0.5571 -0.0685 -0.0309 -0.0040 133 PRO   A CA  
896  C C   . PRO   A 116 ? 0.8947 0.4949 0.6034 -0.0816 -0.0299 0.0000  133 PRO   A C   
897  O O   . PRO   A 116 ? 0.8703 0.4981 0.6098 -0.0862 -0.0271 -0.0002 133 PRO   A O   
898  C CB  . PRO   A 116 ? 0.8771 0.4833 0.5777 -0.0809 -0.0237 -0.0011 133 PRO   A CB  
899  C CG  . PRO   A 116 ? 0.8902 0.5401 0.6318 -0.0868 -0.0156 -0.0024 133 PRO   A CG  
900  C CD  . PRO   A 116 ? 0.8407 0.5153 0.6152 -0.0706 -0.0200 -0.0082 133 PRO   A CD  
901  N N   . TYR   A 117 ? 0.9868 0.5450 0.6527 -0.0875 -0.0326 0.0038  134 TYR   A N   
902  C CA  . TYR   A 117 ? 1.0177 0.5598 0.6708 -0.1000 -0.0328 0.0074  134 TYR   A CA  
903  C C   . TYR   A 117 ? 1.0145 0.5825 0.6874 -0.1225 -0.0236 0.0108  134 TYR   A C   
904  O O   . TYR   A 117 ? 0.9521 0.5327 0.6407 -0.1294 -0.0232 0.0115  134 TYR   A O   
905  C CB  . TYR   A 117 ? 1.0285 0.5166 0.6276 -0.1031 -0.0368 0.0108  134 TYR   A CB  
906  C CG  . TYR   A 117 ? 1.0579 0.5221 0.6377 -0.1141 -0.0386 0.0137  134 TYR   A CG  
907  C CD1 . TYR   A 117 ? 1.0256 0.4808 0.6054 -0.0999 -0.0460 0.0109  134 TYR   A CD1 
908  C CD2 . TYR   A 117 ? 1.0080 0.4587 0.5689 -0.1392 -0.0326 0.0189  134 TYR   A CD2 
909  C CE1 . TYR   A 117 ? 1.0106 0.4422 0.5710 -0.1098 -0.0478 0.0132  134 TYR   A CE1 
910  C CE2 . TYR   A 117 ? 1.0415 0.4691 0.5834 -0.1504 -0.0345 0.0212  134 TYR   A CE2 
911  C CZ  . TYR   A 117 ? 1.0839 0.5010 0.6251 -0.1353 -0.0422 0.0183  134 TYR   A CZ  
912  O OH  . TYR   A 117 ? 1.0868 0.4795 0.6075 -0.1464 -0.0442 0.0202  134 TYR   A OH  
913  N N   . ALA   A 118 ? 1.2068 0.7837 0.8785 -0.1339 -0.0161 0.0128  135 ALA   A N   
914  C CA  . ALA   A 118 ? 1.2031 0.8061 0.8920 -0.1553 -0.0071 0.0159  135 ALA   A CA  
915  C C   . ALA   A 118 ? 1.1632 0.8128 0.9009 -0.1515 -0.0050 0.0133  135 ALA   A C   
916  O O   . ALA   A 118 ? 1.1609 0.8244 0.9111 -0.1634 -0.0032 0.0151  135 ALA   A O   
917  C CB  . ALA   A 118 ? 1.2165 0.8253 0.8987 -0.1647 0.0009  0.0176  135 ALA   A CB  
918  N N   . ALA   A 119 ? 0.9677 0.6410 0.7321 -0.1352 -0.0055 0.0089  136 ALA   A N   
919  C CA  . ALA   A 119 ? 0.8948 0.6088 0.7030 -0.1304 -0.0035 0.0065  136 ALA   A CA  
920  C C   . ALA   A 119 ? 0.8956 0.6061 0.7105 -0.1242 -0.0099 0.0056  136 ALA   A C   
921  O O   . ALA   A 119 ? 0.8415 0.5788 0.6835 -0.1285 -0.0078 0.0060  136 ALA   A O   
922  C CB  . ALA   A 119 ? 0.8709 0.6047 0.7011 -0.1143 -0.0032 0.0017  136 ALA   A CB  
923  N N   . ALA   A 120 ? 0.9011 0.5792 0.6909 -0.1135 -0.0178 0.0044  137 ALA   A N   
924  C CA  . ALA   A 120 ? 0.8710 0.5446 0.6651 -0.1064 -0.0237 0.0031  137 ALA   A CA  
925  C C   . ALA   A 120 ? 0.9073 0.5697 0.6883 -0.1239 -0.0228 0.0073  137 ALA   A C   
926  O O   . ALA   A 120 ? 0.8367 0.5147 0.6367 -0.1248 -0.0238 0.0071  137 ALA   A O   
927  C CB  . ALA   A 120 ? 0.7944 0.4369 0.5637 -0.0891 -0.0322 0.0003  137 ALA   A CB  
928  N N   . LEU   A 121 ? 0.9387 0.5730 0.6856 -0.1385 -0.0212 0.0111  138 LEU   A N   
929  C CA  . LEU   A 121 ? 0.9811 0.6059 0.7148 -0.1586 -0.0197 0.0149  138 LEU   A CA  
930  C C   . LEU   A 121 ? 1.0073 0.6770 0.7780 -0.1709 -0.0132 0.0159  138 LEU   A C   
931  O O   . LEU   A 121 ? 1.0413 0.7170 0.8172 -0.1809 -0.0139 0.0172  138 LEU   A O   
932  C CB  . LEU   A 121 ? 1.0289 0.6187 0.7209 -0.1741 -0.0175 0.0188  138 LEU   A CB  
933  C CG  . LEU   A 121 ? 0.9312 0.4834 0.5871 -0.1885 -0.0205 0.0217  138 LEU   A CG  
934  C CD1 . LEU   A 121 ? 0.9549 0.4842 0.6005 -0.1718 -0.0295 0.0191  138 LEU   A CD1 
935  C CD2 . LEU   A 121 ? 0.9727 0.4835 0.5826 -0.1999 -0.0189 0.0252  138 LEU   A CD2 
936  N N   . GLU   A 122 ? 0.9725 0.6737 0.7682 -0.1696 -0.0070 0.0151  139 GLU   A N   
937  C CA  . GLU   A 122 ? 0.9185 0.6638 0.7499 -0.1782 -0.0009 0.0157  139 GLU   A CA  
938  C C   . GLU   A 122 ? 0.9519 0.7194 0.8137 -0.1667 -0.0044 0.0135  139 GLU   A C   
939  O O   . GLU   A 122 ? 0.9939 0.7840 0.8732 -0.1761 -0.0029 0.0149  139 GLU   A O   
940  C CB  . GLU   A 122 ? 0.9584 0.7296 0.8080 -0.1756 0.0060  0.0146  139 GLU   A CB  
941  C CG  . GLU   A 122 ? 1.0051 0.7668 0.8321 -0.1922 0.0123  0.0176  139 GLU   A CG  
942  C CD  . GLU   A 122 ? 1.0206 0.8001 0.8596 -0.1856 0.0181  0.0158  139 GLU   A CD  
943  O OE1 . GLU   A 122 ? 0.9550 0.7684 0.8288 -0.1754 0.0203  0.0131  139 GLU   A OE1 
944  O OE2 . GLU   A 122 ? 1.0550 0.8127 0.8668 -0.1904 0.0205  0.0171  139 GLU   A OE2 
945  N N   . HIS   A 123 ? 1.0740 0.8361 0.9419 -0.1468 -0.0091 0.0099  140 HIS   A N   
946  C CA  . HIS   A 123 ? 1.1267 0.9066 1.0203 -0.1362 -0.0122 0.0079  140 HIS   A CA  
947  C C   . HIS   A 123 ? 1.1651 0.9244 1.0419 -0.1408 -0.0176 0.0091  140 HIS   A C   
948  O O   . HIS   A 123 ? 1.2002 0.9782 1.0971 -0.1409 -0.0184 0.0092  140 HIS   A O   
949  C CB  . HIS   A 123 ? 1.0982 0.8776 1.0010 -0.1153 -0.0154 0.0034  140 HIS   A CB  
950  C CG  . HIS   A 123 ? 1.1348 0.9437 1.0725 -0.1056 -0.0151 0.0012  140 HIS   A CG  
951  N ND1 . HIS   A 123 ? 1.1146 0.9237 1.0616 -0.0886 -0.0188 -0.0029 140 HIS   A ND1 
952  C CD2 . HIS   A 123 ? 1.2014 1.0399 1.1657 -0.1107 -0.0116 0.0026  140 HIS   A CD2 
953  C CE1 . HIS   A 123 ? 1.1773 1.0129 1.1539 -0.0846 -0.0170 -0.0037 140 HIS   A CE1 
954  N NE2 . HIS   A 123 ? 1.2257 1.0786 1.2128 -0.0970 -0.0129 -0.0003 140 HIS   A NE2 
955  N N   . HIS   A 124 ? 1.0704 0.7896 0.9089 -0.1441 -0.0215 0.0101  141 HIS   A N   
956  C CA  . HIS   A 124 ? 1.1023 0.7972 0.9202 -0.1489 -0.0266 0.0111  141 HIS   A CA  
957  C C   . HIS   A 124 ? 1.1483 0.8532 0.9667 -0.1712 -0.0236 0.0145  141 HIS   A C   
958  O O   . HIS   A 124 ? 1.2096 0.9064 1.0221 -0.1754 -0.0274 0.0149  141 HIS   A O   
959  C CB  . HIS   A 124 ? 1.1836 0.8296 0.9571 -0.1457 -0.0316 0.0111  141 HIS   A CB  
960  C CG  . HIS   A 124 ? 1.2424 0.8593 0.9921 -0.1469 -0.0374 0.0113  141 HIS   A CG  
961  N ND1 . HIS   A 124 ? 1.3615 0.9631 1.0911 -0.1675 -0.0369 0.0144  141 HIS   A ND1 
962  C CD2 . HIS   A 124 ? 1.0689 0.6694 0.8111 -0.1301 -0.0438 0.0083  141 HIS   A CD2 
963  C CE1 . HIS   A 124 ? 1.3991 0.9738 1.1086 -0.1631 -0.0429 0.0134  141 HIS   A CE1 
964  N NE2 . HIS   A 124 ? 1.2585 0.8325 0.9754 -0.1399 -0.0470 0.0097  141 HIS   A NE2 
965  N N   . HIS   A 125 ? 1.1583 0.8806 0.9824 -0.1857 -0.0170 0.0168  142 HIS   A N   
966  C CA  . HIS   A 125 ? 1.1331 0.8752 0.9645 -0.2072 -0.0133 0.0196  142 HIS   A CA  
967  C C   . HIS   A 125 ? 1.1396 0.8439 0.9317 -0.2243 -0.0163 0.0218  142 HIS   A C   
968  O O   . HIS   A 125 ? 1.1857 0.8491 0.9415 -0.2241 -0.0183 0.0223  142 HIS   A O   
969  C CB  . HIS   A 125 ? 1.1088 0.8865 0.9752 -0.2033 -0.0142 0.0187  142 HIS   A CB  
970  C CG  . HIS   A 125 ? 1.0745 0.8945 0.9798 -0.1940 -0.0092 0.0176  142 HIS   A CG  
971  N ND1 . HIS   A 125 ? 1.0960 0.9267 1.0063 -0.1936 -0.0033 0.0175  142 HIS   A ND1 
972  C CD2 . HIS   A 125 ? 1.0287 0.8806 0.9675 -0.1844 -0.0092 0.0165  142 HIS   A CD2 
973  C CE1 . HIS   A 125 ? 1.1152 0.9822 1.0604 -0.1840 0.0000  0.0162  142 HIS   A CE1 
974  N NE2 . HIS   A 125 ? 1.0928 0.9725 1.0554 -0.1783 -0.0034 0.0157  142 HIS   A NE2 
975  N N   . ALA   B 1   ? 0.9021 0.8135 1.0916 0.1237  0.0635  0.0145  18  ALA   B N   
976  C CA  . ALA   B 1   ? 0.9150 0.8051 1.0992 0.1100  0.0666  0.0090  18  ALA   B CA  
977  C C   . ALA   B 1   ? 0.9177 0.7974 1.0997 0.0970  0.0652  0.0114  18  ALA   B C   
978  O O   . ALA   B 1   ? 0.9197 0.8007 1.0997 0.1003  0.0628  0.0175  18  ALA   B O   
979  C CB  . ALA   B 1   ? 0.8636 0.7732 1.0600 0.1014  0.0662  0.0033  18  ALA   B CB  
980  N N   . PHE   B 2   ? 0.8342 0.7047 1.0164 0.0826  0.0668  0.0062  19  PHE   B N   
981  C CA  . PHE   B 2   ? 0.7677 0.6308 0.9490 0.0696  0.0663  0.0072  19  PHE   B CA  
982  C C   . PHE   B 2   ? 0.7160 0.6077 0.9118 0.0636  0.0610  0.0093  19  PHE   B C   
983  O O   . PHE   B 2   ? 0.7192 0.6289 0.9254 0.0583  0.0591  0.0054  19  PHE   B O   
984  C CB  . PHE   B 2   ? 0.7708 0.6186 0.9488 0.0570  0.0695  0.0002  19  PHE   B CB  
985  C CG  . PHE   B 2   ? 0.6908 0.5329 0.8684 0.0435  0.0697  0.0003  19  PHE   B CG  
986  C CD1 . PHE   B 2   ? 0.6710 0.4883 0.8348 0.0421  0.0731  0.0035  19  PHE   B CD1 
987  C CD2 . PHE   B 2   ? 0.7518 0.6129 0.9417 0.0327  0.0667  -0.0028 19  PHE   B CD2 
988  C CE1 . PHE   B 2   ? 0.7734 0.5877 0.9373 0.0292  0.0740  0.0034  19  PHE   B CE1 
989  C CE2 . PHE   B 2   ? 0.7233 0.5817 0.9135 0.0215  0.0671  -0.0031 19  PHE   B CE2 
990  C CZ  . PHE   B 2   ? 0.7582 0.5944 0.9361 0.0193  0.0711  -0.0001 19  PHE   B CZ  
991  N N   . THR   B 3   ? 0.6923 0.5865 0.8869 0.0644  0.0586  0.0153  20  THR   B N   
992  C CA  . THR   B 3   ? 0.6389 0.5570 0.8444 0.0589  0.0535  0.0175  20  THR   B CA  
993  C C   . THR   B 3   ? 0.6369 0.5455 0.8379 0.0506  0.0534  0.0199  20  THR   B C   
994  O O   . THR   B 3   ? 0.6625 0.5528 0.8520 0.0545  0.0555  0.0240  20  THR   B O   
995  C CB  . THR   B 3   ? 0.5613 0.4995 0.7717 0.0696  0.0495  0.0228  20  THR   B CB  
996  O OG1 . THR   B 3   ? 0.6840 0.6091 0.8839 0.0780  0.0496  0.0287  20  THR   B OG1 
997  C CG2 . THR   B 3   ? 0.5180 0.4666 0.7324 0.0792  0.0506  0.0206  20  THR   B CG2 
998  N N   . VAL   B 4   ? 0.6092 0.5294 0.8177 0.0397  0.0511  0.0174  21  VAL   B N   
999  C CA  . VAL   B 4   ? 0.6027 0.5190 0.8085 0.0322  0.0506  0.0193  21  VAL   B CA  
1000 C C   . VAL   B 4   ? 0.5955 0.5270 0.8036 0.0359  0.0455  0.0250  21  VAL   B C   
1001 O O   . VAL   B 4   ? 0.4989 0.4504 0.7152 0.0375  0.0413  0.0251  21  VAL   B O   
1002 C CB  . VAL   B 4   ? 0.5934 0.5154 0.8054 0.0204  0.0504  0.0132  21  VAL   B CB  
1003 C CG1 . VAL   B 4   ? 0.4840 0.4076 0.6947 0.0141  0.0493  0.0151  21  VAL   B CG1 
1004 C CG2 . VAL   B 4   ? 0.6025 0.5089 0.8112 0.0155  0.0554  0.0075  21  VAL   B CG2 
1005 N N   . THR   B 5   ? 0.6251 0.5467 0.8248 0.0365  0.0459  0.0298  22  THR   B N   
1006 C CA  . THR   B 5   ? 0.5736 0.5071 0.7731 0.0406  0.0409  0.0356  22  THR   B CA  
1007 C C   . THR   B 5   ? 0.6101 0.5435 0.8076 0.0317  0.0400  0.0360  22  THR   B C   
1008 O O   . THR   B 5   ? 0.6861 0.6036 0.8768 0.0265  0.0446  0.0352  22  THR   B O   
1009 C CB  . THR   B 5   ? 0.5959 0.5174 0.7847 0.0521  0.0416  0.0417  22  THR   B CB  
1010 O OG1 . THR   B 5   ? 0.6675 0.5944 0.8592 0.0627  0.0414  0.0415  22  THR   B OG1 
1011 C CG2 . THR   B 5   ? 0.5875 0.5194 0.7743 0.0551  0.0363  0.0475  22  THR   B CG2 
1012 N N   . VAL   B 6   ? 0.6157 0.5668 0.8184 0.0296  0.0344  0.0369  23  VAL   B N   
1013 C CA  . VAL   B 6   ? 0.5984 0.5506 0.7981 0.0229  0.0328  0.0374  23  VAL   B CA  
1014 C C   . VAL   B 6   ? 0.5851 0.5414 0.7789 0.0282  0.0285  0.0439  23  VAL   B C   
1015 O O   . VAL   B 6   ? 0.5566 0.5285 0.7552 0.0326  0.0235  0.0458  23  VAL   B O   
1016 C CB  . VAL   B 6   ? 0.5688 0.5342 0.7759 0.0156  0.0295  0.0325  23  VAL   B CB  
1017 C CG1 . VAL   B 6   ? 0.5130 0.4742 0.7248 0.0110  0.0333  0.0261  23  VAL   B CG1 
1018 C CG2 . VAL   B 6   ? 0.5996 0.5828 0.8128 0.0177  0.0239  0.0334  23  VAL   B CG2 
1019 N N   . PRO   B 7   ? 0.6196 0.5632 0.8030 0.0279  0.0305  0.0474  24  PRO   B N   
1020 C CA  . PRO   B 7   ? 0.5869 0.5348 0.7636 0.0328  0.0257  0.0533  24  PRO   B CA  
1021 C C   . PRO   B 7   ? 0.5902 0.5531 0.7698 0.0271  0.0199  0.0523  24  PRO   B C   
1022 O O   . PRO   B 7   ? 0.6195 0.5904 0.7955 0.0304  0.0145  0.0564  24  PRO   B O   
1023 C CB  . PRO   B 7   ? 0.5921 0.5191 0.7550 0.0326  0.0306  0.0568  24  PRO   B CB  
1024 C CG  . PRO   B 7   ? 0.6315 0.5433 0.7942 0.0283  0.0382  0.0529  24  PRO   B CG  
1025 C CD  . PRO   B 7   ? 0.6122 0.5371 0.7885 0.0229  0.0374  0.0461  24  PRO   B CD  
1026 N N   . LYS   B 8   ? 0.5931 0.5591 0.7777 0.0189  0.0205  0.0467  25  LYS   B N   
1027 C CA  . LYS   B 8   ? 0.5740 0.5494 0.7581 0.0134  0.0154  0.0452  25  LYS   B CA  
1028 C C   . LYS   B 8   ? 0.5664 0.5477 0.7584 0.0078  0.0152  0.0390  25  LYS   B C   
1029 O O   . LYS   B 8   ? 0.5304 0.5048 0.7245 0.0050  0.0200  0.0348  25  LYS   B O   
1030 C CB  . LYS   B 8   ? 0.5645 0.5303 0.7386 0.0103  0.0172  0.0459  25  LYS   B CB  
1031 C CG  . LYS   B 8   ? 0.5775 0.5447 0.7423 0.0131  0.0126  0.0513  25  LYS   B CG  
1032 C CD  . LYS   B 8   ? 0.6905 0.6456 0.8443 0.0108  0.0163  0.0521  25  LYS   B CD  
1033 C CE  . LYS   B 8   ? 0.6230 0.5808 0.7769 0.0044  0.0158  0.0467  25  LYS   B CE  
1034 N NZ  . LYS   B 8   ? 0.6991 0.6561 0.8417 0.0035  0.0120  0.0484  25  LYS   B NZ  
1035 N N   . ASP   B 9   ? 0.5779 0.5720 0.7733 0.0058  0.0097  0.0383  26  ASP   B N   
1036 C CA  . ASP   B 9   ? 0.5509 0.5489 0.7509 0.0006  0.0088  0.0330  26  ASP   B CA  
1037 C C   . ASP   B 9   ? 0.5179 0.5121 0.7108 -0.0047 0.0064  0.0302  26  ASP   B C   
1038 O O   . ASP   B 9   ? 0.4833 0.4769 0.6774 -0.0080 0.0062  0.0255  26  ASP   B O   
1039 C CB  . ASP   B 9   ? 0.5497 0.5620 0.7553 0.0000  0.0048  0.0336  26  ASP   B CB  
1040 C CG  . ASP   B 9   ? 0.7515 0.7726 0.9523 -0.0029 -0.0017 0.0365  26  ASP   B CG  
1041 O OD1 . ASP   B 9   ? 0.7461 0.7666 0.9422 0.0006  -0.0031 0.0407  26  ASP   B OD1 
1042 O OD2 . ASP   B 9   ? 0.8708 0.8982 1.0709 -0.0091 -0.0054 0.0345  26  ASP   B OD2 
1043 N N   . LEU   B 10  ? 0.5447 0.5354 0.7289 -0.0047 0.0046  0.0330  27  LEU   B N   
1044 C CA  . LEU   B 10  ? 0.5658 0.5516 0.7411 -0.0084 0.0023  0.0304  27  LEU   B CA  
1045 C C   . LEU   B 10  ? 0.6065 0.5843 0.7744 -0.0066 0.0054  0.0321  27  LEU   B C   
1046 O O   . LEU   B 10  ? 0.5331 0.5101 0.6976 -0.0037 0.0052  0.0372  27  LEU   B O   
1047 C CB  . LEU   B 10  ? 0.5984 0.5894 0.7674 -0.0122 -0.0050 0.0316  27  LEU   B CB  
1048 C CG  . LEU   B 10  ? 0.5616 0.5445 0.7174 -0.0149 -0.0080 0.0298  27  LEU   B CG  
1049 C CD1 . LEU   B 10  ? 0.5132 0.4896 0.6671 -0.0160 -0.0067 0.0238  27  LEU   B CD1 
1050 C CD2 . LEU   B 10  ? 0.5827 0.5695 0.7310 -0.0197 -0.0152 0.0316  27  LEU   B CD2 
1051 N N   . TYR   B 11  ? 0.5797 0.5521 0.7447 -0.0078 0.0083  0.0279  28  TYR   B N   
1052 C CA  . TYR   B 11  ? 0.5585 0.5246 0.7157 -0.0070 0.0117  0.0287  28  TYR   B CA  
1053 C C   . TYR   B 11  ? 0.5009 0.4645 0.6477 -0.0081 0.0080  0.0258  28  TYR   B C   
1054 O O   . TYR   B 11  ? 0.5464 0.5107 0.6935 -0.0092 0.0058  0.0211  28  TYR   B O   
1055 C CB  . TYR   B 11  ? 0.5945 0.5583 0.7573 -0.0074 0.0195  0.0256  28  TYR   B CB  
1056 C CG  . TYR   B 11  ? 0.5182 0.4788 0.6865 -0.0063 0.0242  0.0288  28  TYR   B CG  
1057 C CD1 . TYR   B 11  ? 0.5307 0.4946 0.7078 -0.0055 0.0234  0.0284  28  TYR   B CD1 
1058 C CD2 . TYR   B 11  ? 0.5695 0.5220 0.7322 -0.0062 0.0298  0.0321  28  TYR   B CD2 
1059 C CE1 . TYR   B 11  ? 0.6452 0.6037 0.8251 -0.0035 0.0277  0.0309  28  TYR   B CE1 
1060 C CE2 . TYR   B 11  ? 0.5907 0.5363 0.7552 -0.0050 0.0341  0.0350  28  TYR   B CE2 
1061 C CZ  . TYR   B 11  ? 0.6183 0.5666 0.7913 -0.0032 0.0328  0.0343  28  TYR   B CZ  
1062 O OH  . TYR   B 11  ? 0.6212 0.5603 0.7940 -0.0011 0.0371  0.0369  28  TYR   B OH  
1063 N N   . VAL   B 12  ? 0.5348 0.4940 0.6706 -0.0074 0.0072  0.0287  29  VAL   B N   
1064 C CA  . VAL   B 12  ? 0.6002 0.5546 0.7234 -0.0075 0.0045  0.0260  29  VAL   B CA  
1065 C C   . VAL   B 12  ? 0.6300 0.5811 0.7487 -0.0057 0.0110  0.0255  29  VAL   B C   
1066 O O   . VAL   B 12  ? 0.7258 0.6737 0.8392 -0.0050 0.0130  0.0304  29  VAL   B O   
1067 C CB  . VAL   B 12  ? 0.5740 0.5263 0.6860 -0.0091 -0.0029 0.0293  29  VAL   B CB  
1068 C CG1 . VAL   B 12  ? 0.5906 0.5345 0.6867 -0.0086 -0.0046 0.0269  29  VAL   B CG1 
1069 C CG2 . VAL   B 12  ? 0.5642 0.5208 0.6798 -0.0127 -0.0090 0.0286  29  VAL   B CG2 
1070 N N   . VAL   B 13  ? 0.5959 0.5483 0.7161 -0.0047 0.0145  0.0197  30  VAL   B N   
1071 C CA  . VAL   B 13  ? 0.6758 0.6290 0.7945 -0.0038 0.0220  0.0182  30  VAL   B CA  
1072 C C   . VAL   B 13  ? 0.6470 0.5988 0.7552 -0.0006 0.0208  0.0132  30  VAL   B C   
1073 O O   . VAL   B 13  ? 0.6588 0.6087 0.7635 0.0012  0.0153  0.0095  30  VAL   B O   
1074 C CB  . VAL   B 13  ? 0.6300 0.5902 0.7631 -0.0055 0.0289  0.0152  30  VAL   B CB  
1075 C CG1 . VAL   B 13  ? 0.6038 0.5621 0.7444 -0.0078 0.0304  0.0200  30  VAL   B CG1 
1076 C CG2 . VAL   B 13  ? 0.5715 0.5378 0.7118 -0.0042 0.0264  0.0085  30  VAL   B CG2 
1077 N N   . GLU   B 14  ? 0.7171 0.6688 0.8191 0.0005  0.0264  0.0132  31  GLU   B N   
1078 C CA  . GLU   B 14  ? 0.7142 0.6651 0.8054 0.0049  0.0265  0.0084  31  GLU   B CA  
1079 C C   . GLU   B 14  ? 0.7140 0.6771 0.8155 0.0070  0.0322  0.0014  31  GLU   B C   
1080 O O   . GLU   B 14  ? 0.6759 0.6477 0.7911 0.0034  0.0383  0.0012  31  GLU   B O   
1081 C CB  . GLU   B 14  ? 0.7291 0.6748 0.8068 0.0053  0.0297  0.0117  31  GLU   B CB  
1082 C CG  . GLU   B 14  ? 0.7214 0.6571 0.7888 0.0034  0.0239  0.0186  31  GLU   B CG  
1083 C CD  . GLU   B 14  ? 0.7788 0.7076 0.8371 0.0040  0.0140  0.0176  31  GLU   B CD  
1084 O OE1 . GLU   B 14  ? 0.7645 0.6952 0.8314 0.0017  0.0094  0.0180  31  GLU   B OE1 
1085 O OE2 . GLU   B 14  ? 0.8698 0.7905 0.9113 0.0062  0.0109  0.0163  31  GLU   B OE2 
1086 N N   . TYR   B 15  ? 0.7187 0.6820 0.8127 0.0132  0.0297  -0.0044 32  TYR   B N   
1087 C CA  . TYR   B 15  ? 0.6479 0.6252 0.7509 0.0172  0.0341  -0.0117 32  TYR   B CA  
1088 C C   . TYR   B 15  ? 0.5788 0.5680 0.6873 0.0148  0.0443  -0.0122 32  TYR   B C   
1089 O O   . TYR   B 15  ? 0.5611 0.5453 0.6583 0.0146  0.0474  -0.0092 32  TYR   B O   
1090 C CB  . TYR   B 15  ? 0.5816 0.5544 0.6713 0.0263  0.0293  -0.0174 32  TYR   B CB  
1091 C CG  . TYR   B 15  ? 0.5522 0.5415 0.6492 0.0329  0.0335  -0.0254 32  TYR   B CG  
1092 C CD1 . TYR   B 15  ? 0.5615 0.5598 0.6705 0.0350  0.0314  -0.0301 32  TYR   B CD1 
1093 C CD2 . TYR   B 15  ? 0.5440 0.5413 0.6358 0.0375  0.0394  -0.0285 32  TYR   B CD2 
1094 C CE1 . TYR   B 15  ? 0.5735 0.5896 0.6899 0.0418  0.0345  -0.0378 32  TYR   B CE1 
1095 C CE2 . TYR   B 15  ? 0.5979 0.6141 0.6977 0.0442  0.0432  -0.0363 32  TYR   B CE2 
1096 C CZ  . TYR   B 15  ? 0.5840 0.6101 0.6964 0.0465  0.0404  -0.0410 32  TYR   B CZ  
1097 O OH  . TYR   B 15  ? 0.6563 0.7039 0.7774 0.0539  0.0435  -0.0491 32  TYR   B OH  
1098 N N   . GLY   B 16  ? 0.5090 0.5140 0.6342 0.0122  0.0497  -0.0161 33  GLY   B N   
1099 C CA  . GLY   B 16  ? 0.6790 0.6973 0.8105 0.0081  0.0600  -0.0174 33  GLY   B CA  
1100 C C   . GLY   B 16  ? 0.7279 0.7397 0.8609 -0.0014 0.0657  -0.0103 33  GLY   B C   
1101 O O   . GLY   B 16  ? 0.7257 0.7473 0.8644 -0.0072 0.0750  -0.0112 33  GLY   B O   
1102 N N   . SER   B 17  ? 0.6609 0.6564 0.7880 -0.0031 0.0606  -0.0034 34  SER   B N   
1103 C CA  . SER   B 17  ? 0.6794 0.6658 0.8050 -0.0100 0.0651  0.0038  34  SER   B CA  
1104 C C   . SER   B 17  ? 0.7203 0.7106 0.8610 -0.0161 0.0680  0.0032  34  SER   B C   
1105 O O   . SER   B 17  ? 0.6892 0.6907 0.8422 -0.0155 0.0666  -0.0029 34  SER   B O   
1106 C CB  . SER   B 17  ? 0.7005 0.6706 0.8142 -0.0079 0.0578  0.0110  34  SER   B CB  
1107 O OG  . SER   B 17  ? 0.8403 0.8025 0.9573 -0.0123 0.0589  0.0169  34  SER   B OG  
1108 N N   . ASN   B 18  ? 0.7195 0.6990 0.8576 -0.0216 0.0720  0.0095  35  ASN   B N   
1109 C CA  . ASN   B 18  ? 0.6994 0.6774 0.8481 -0.0275 0.0748  0.0098  35  ASN   B CA  
1110 C C   . ASN   B 18  ? 0.6776 0.6428 0.8243 -0.0245 0.0677  0.0153  35  ASN   B C   
1111 O O   . ASN   B 18  ? 0.7257 0.6798 0.8606 -0.0215 0.0646  0.0218  35  ASN   B O   
1112 C CB  . ASN   B 18  ? 0.7404 0.7128 0.8855 -0.0359 0.0851  0.0127  35  ASN   B CB  
1113 C CG  . ASN   B 18  ? 0.7812 0.7710 0.9371 -0.0427 0.0930  0.0054  35  ASN   B CG  
1114 O OD1 . ASN   B 18  ? 0.7592 0.7668 0.9238 -0.0391 0.0909  -0.0018 35  ASN   B OD1 
1115 N ND2 . ASN   B 18  ? 0.8498 0.8345 1.0043 -0.0526 0.1021  0.0072  35  ASN   B ND2 
1116 N N   . MET   B 19  ? 0.6234 0.5919 0.7818 -0.0251 0.0650  0.0125  36  MET   B N   
1117 C CA  . MET   B 19  ? 0.6629 0.6227 0.8215 -0.0221 0.0589  0.0169  36  MET   B CA  
1118 C C   . MET   B 19  ? 0.6804 0.6358 0.8466 -0.0265 0.0628  0.0168  36  MET   B C   
1119 O O   . MET   B 19  ? 0.7130 0.6766 0.8888 -0.0312 0.0668  0.0109  36  MET   B O   
1120 C CB  . MET   B 19  ? 0.6088 0.5751 0.7713 -0.0172 0.0500  0.0137  36  MET   B CB  
1121 C CG  . MET   B 19  ? 0.6271 0.6010 0.8027 -0.0183 0.0489  0.0079  36  MET   B CG  
1122 S SD  . MET   B 19  ? 0.5090 0.4861 0.6850 -0.0131 0.0388  0.0056  36  MET   B SD  
1123 C CE  . MET   B 19  ? 0.5360 0.5221 0.7260 -0.0148 0.0396  -0.0016 36  MET   B CE  
1124 N N   . THR   B 20  ? 0.6435 0.5858 0.8043 -0.0247 0.0618  0.0233  37  THR   B N   
1125 C CA  . THR   B 20  ? 0.7314 0.6657 0.8964 -0.0271 0.0647  0.0238  37  THR   B CA  
1126 C C   . THR   B 20  ? 0.6783 0.6116 0.8463 -0.0207 0.0574  0.0262  37  THR   B C   
1127 O O   . THR   B 20  ? 0.5808 0.5090 0.7413 -0.0154 0.0534  0.0322  37  THR   B O   
1128 C CB  . THR   B 20  ? 0.7294 0.6464 0.8827 -0.0301 0.0716  0.0296  37  THR   B CB  
1129 O OG1 . THR   B 20  ? 0.7504 0.6700 0.9005 -0.0372 0.0790  0.0275  37  THR   B OG1 
1130 C CG2 . THR   B 20  ? 0.6526 0.5585 0.8082 -0.0328 0.0750  0.0293  37  THR   B CG2 
1131 N N   . ILE   B 21  ? 0.6519 0.5915 0.8309 -0.0214 0.0559  0.0213  38  ILE   B N   
1132 C CA  . ILE   B 21  ? 0.5971 0.5378 0.7800 -0.0162 0.0499  0.0227  38  ILE   B CA  
1133 C C   . ILE   B 21  ? 0.6804 0.6098 0.8637 -0.0161 0.0538  0.0240  38  ILE   B C   
1134 O O   . ILE   B 21  ? 0.6824 0.6072 0.8677 -0.0220 0.0597  0.0204  38  ILE   B O   
1135 C CB  . ILE   B 21  ? 0.6695 0.6232 0.8618 -0.0161 0.0451  0.0165  38  ILE   B CB  
1136 C CG1 . ILE   B 21  ? 0.7018 0.6609 0.9017 -0.0216 0.0495  0.0092  38  ILE   B CG1 
1137 C CG2 . ILE   B 21  ? 0.6786 0.6391 0.8668 -0.0141 0.0396  0.0166  38  ILE   B CG2 
1138 C CD1 . ILE   B 21  ? 0.6090 0.5803 0.8153 -0.0205 0.0446  0.0031  38  ILE   B CD1 
1139 N N   . GLU   B 22  ? 0.7843 0.7094 0.9651 -0.0094 0.0503  0.0289  39  GLU   B N   
1140 C CA  . GLU   B 22  ? 0.7551 0.6661 0.9321 -0.0067 0.0538  0.0315  39  GLU   B CA  
1141 C C   . GLU   B 22  ? 0.7448 0.6621 0.9300 -0.0019 0.0500  0.0298  39  GLU   B C   
1142 O O   . GLU   B 22  ? 0.8302 0.7590 1.0187 0.0028  0.0438  0.0316  39  GLU   B O   
1143 C CB  . GLU   B 22  ? 0.8169 0.7158 0.9810 -0.0008 0.0538  0.0396  39  GLU   B CB  
1144 C CG  . GLU   B 22  ? 0.8671 0.7570 1.0205 -0.0056 0.0585  0.0420  39  GLU   B CG  
1145 C CD  . GLU   B 22  ? 1.0237 0.8912 1.1617 -0.0025 0.0628  0.0484  39  GLU   B CD  
1146 O OE1 . GLU   B 22  ? 0.9440 0.8023 1.0798 0.0040  0.0623  0.0504  39  GLU   B OE1 
1147 O OE2 . GLU   B 22  ? 1.0638 0.9219 1.1904 -0.0060 0.0669  0.0515  39  GLU   B OE2 
1148 N N   . CYS   B 23  ? 0.6444 0.5544 0.8321 -0.0039 0.0539  0.0261  40  CYS   B N   
1149 C CA  . CYS   B 23  ? 0.6972 0.6077 0.8889 0.0020  0.0522  0.0256  40  CYS   B CA  
1150 C C   . CYS   B 23  ? 0.7129 0.6020 0.8950 0.0046  0.0576  0.0276  40  CYS   B C   
1151 O O   . CYS   B 23  ? 0.7306 0.6056 0.9064 -0.0023 0.0635  0.0262  40  CYS   B O   
1152 C CB  . CYS   B 23  ? 0.6467 0.5680 0.8492 -0.0020 0.0510  0.0182  40  CYS   B CB  
1153 S SG  . CYS   B 23  ? 1.0184 0.9331 1.2225 -0.0126 0.0572  0.0110  40  CYS   B SG  
1154 N N   . LYS   B 24  ? 0.6852 0.5718 0.8656 0.0145  0.0557  0.0306  41  LYS   B N   
1155 C CA  . LYS   B 24  ? 0.6553 0.5191 0.8231 0.0201  0.0599  0.0338  41  LYS   B CA  
1156 C C   . LYS   B 24  ? 0.6654 0.5267 0.8364 0.0247  0.0607  0.0301  41  LYS   B C   
1157 O O   . LYS   B 24  ? 0.6721 0.5518 0.8537 0.0291  0.0564  0.0285  41  LYS   B O   
1158 C CB  . LYS   B 24  ? 0.5994 0.4601 0.7583 0.0310  0.0570  0.0418  41  LYS   B CB  
1159 C CG  . LYS   B 24  ? 0.6566 0.5070 0.8045 0.0272  0.0588  0.0464  41  LYS   B CG  
1160 C CD  . LYS   B 24  ? 0.7369 0.5857 0.8757 0.0388  0.0548  0.0543  41  LYS   B CD  
1161 C CE  . LYS   B 24  ? 0.7214 0.5724 0.8546 0.0345  0.0537  0.0579  41  LYS   B CE  
1162 N NZ  . LYS   B 24  ? 0.7184 0.5431 0.8315 0.0361  0.0583  0.0636  41  LYS   B NZ  
1163 N N   . PHE   B 25  ? 0.6760 0.5134 0.8364 0.0232  0.0665  0.0286  42  PHE   B N   
1164 C CA  . PHE   B 25  ? 0.7289 0.5581 0.8884 0.0279  0.0682  0.0250  42  PHE   B CA  
1165 C C   . PHE   B 25  ? 0.7828 0.5829 0.9236 0.0363  0.0720  0.0291  42  PHE   B C   
1166 O O   . PHE   B 25  ? 0.8047 0.5849 0.9318 0.0328  0.0756  0.0329  42  PHE   B O   
1167 C CB  . PHE   B 25  ? 0.7670 0.5942 0.9313 0.0158  0.0714  0.0167  42  PHE   B CB  
1168 C CG  . PHE   B 25  ? 0.7611 0.5690 0.9158 0.0039  0.0774  0.0153  42  PHE   B CG  
1169 C CD1 . PHE   B 25  ? 0.7216 0.5347 0.8766 -0.0033 0.0780  0.0176  42  PHE   B CD1 
1170 C CD2 . PHE   B 25  ? 0.7745 0.5600 0.9197 -0.0010 0.0826  0.0112  42  PHE   B CD2 
1171 C CE1 . PHE   B 25  ? 0.7864 0.5845 0.9333 -0.0153 0.0841  0.0161  42  PHE   B CE1 
1172 C CE2 . PHE   B 25  ? 0.7853 0.5543 0.9216 -0.0140 0.0885  0.0096  42  PHE   B CE2 
1173 C CZ  . PHE   B 25  ? 0.8286 0.6050 0.9664 -0.0213 0.0894  0.0121  42  PHE   B CZ  
1174 N N   . PRO   B 26  ? 0.8562 0.6519 0.9944 0.0479  0.0716  0.0287  43  PRO   B N   
1175 C CA  . PRO   B 26  ? 0.8026 0.5689 0.9209 0.0587  0.0747  0.0329  43  PRO   B CA  
1176 C C   . PRO   B 26  ? 0.9001 0.6335 1.0031 0.0505  0.0817  0.0289  43  PRO   B C   
1177 O O   . PRO   B 26  ? 0.8910 0.6245 0.9989 0.0453  0.0833  0.0219  43  PRO   B O   
1178 C CB  . PRO   B 26  ? 0.7393 0.5186 0.8630 0.0746  0.0714  0.0329  43  PRO   B CB  
1179 C CG  . PRO   B 26  ? 0.7986 0.6050 0.9424 0.0674  0.0693  0.0260  43  PRO   B CG  
1180 C CD  . PRO   B 26  ? 0.8207 0.6322 0.9712 0.0498  0.0700  0.0228  43  PRO   B CD  
1181 N N   . VAL   B 27  ? 0.9864 0.6910 1.0697 0.0484  0.0857  0.0335  44  VAL   B N   
1182 C CA  . VAL   B 27  ? 1.0627 0.7308 1.1268 0.0409  0.0927  0.0309  44  VAL   B CA  
1183 C C   . VAL   B 27  ? 1.1783 0.8140 1.2177 0.0567  0.0941  0.0370  44  VAL   B C   
1184 O O   . VAL   B 27  ? 1.1900 0.8207 1.2202 0.0643  0.0925  0.0448  44  VAL   B O   
1185 C CB  . VAL   B 27  ? 1.0788 0.7383 1.1387 0.0216  0.0974  0.0303  44  VAL   B CB  
1186 C CG1 . VAL   B 27  ? 1.0358 0.6970 1.0905 0.0234  0.0964  0.0384  44  VAL   B CG1 
1187 C CG2 . VAL   B 27  ? 1.2370 0.8562 1.2742 0.0125  0.1050  0.0280  44  VAL   B CG2 
1188 N N   . GLU   B 28  ? 1.1813 0.7944 1.2088 0.0625  0.0968  0.0335  45  GLU   B N   
1189 C CA  . GLU   B 28  ? 1.3257 0.9074 1.3288 0.0804  0.0978  0.0386  45  GLU   B CA  
1190 C C   . GLU   B 28  ? 1.4365 0.9705 1.4094 0.0719  0.1047  0.0407  45  GLU   B C   
1191 O O   . GLU   B 28  ? 1.4200 0.9296 1.3715 0.0821  0.1052  0.0484  45  GLU   B O   
1192 C CB  . GLU   B 28  ? 1.4033 0.9848 1.4072 0.0939  0.0970  0.0339  45  GLU   B CB  
1193 C CG  . GLU   B 28  ? 1.4571 1.0670 1.4728 0.1154  0.0906  0.0377  45  GLU   B CG  
1194 C CD  . GLU   B 28  ? 1.4877 1.1188 1.5183 0.1223  0.0892  0.0312  45  GLU   B CD  
1195 O OE1 . GLU   B 28  ? 1.4917 1.1041 1.5153 0.1163  0.0934  0.0245  45  GLU   B OE1 
1196 O OE2 . GLU   B 28  ? 1.4044 1.0711 1.4531 0.1331  0.0840  0.0326  45  GLU   B OE2 
1197 N N   . LYS   B 29  ? 1.5218 1.0422 1.4921 0.0528  0.1100  0.0339  46  LYS   B N   
1198 C CA  . LYS   B 29  ? 1.5367 1.0107 1.4776 0.0418  0.1173  0.0350  46  LYS   B CA  
1199 C C   . LYS   B 29  ? 1.5097 0.9912 1.4575 0.0170  0.1213  0.0333  46  LYS   B C   
1200 O O   . LYS   B 29  ? 1.5151 0.9944 1.4570 0.0140  0.1222  0.0398  46  LYS   B O   
1201 C CB  . LYS   B 29  ? 1.5565 1.0004 1.4822 0.0404  0.1212  0.0282  46  LYS   B CB  
1202 N N   . GLN   B 30  ? 1.5231 1.0145 1.4831 -0.0004 0.1235  0.0242  47  GLN   B N   
1203 C CA  . GLN   B 30  ? 1.5040 1.0033 1.4705 -0.0246 0.1278  0.0210  47  GLN   B CA  
1204 C C   . GLN   B 30  ? 1.4922 1.0371 1.4920 -0.0319 0.1236  0.0130  47  GLN   B C   
1205 O O   . GLN   B 30  ? 1.5377 1.1072 1.5541 -0.0187 0.1175  0.0115  47  GLN   B O   
1206 C CB  . GLN   B 30  ? 1.4532 0.9118 1.3953 -0.0411 0.1358  0.0174  47  GLN   B CB  
1207 N N   . LEU   B 31  ? 1.2896 0.8450 1.2978 -0.0534 0.1271  0.0075  48  LEU   B N   
1208 C CA  . LEU   B 31  ? 1.1098 0.7046 1.1461 -0.0621 0.1237  -0.0005 48  LEU   B CA  
1209 C C   . LEU   B 31  ? 1.0658 0.6516 1.1007 -0.0725 0.1256  -0.0102 48  LEU   B C   
1210 O O   . LEU   B 31  ? 1.1920 0.7538 1.2120 -0.0891 0.1319  -0.0133 48  LEU   B O   
1211 C CB  . LEU   B 31  ? 1.1263 0.7441 1.1752 -0.0780 0.1257  -0.0012 48  LEU   B CB  
1212 C CG  . LEU   B 31  ? 1.1329 0.7885 1.2029 -0.0731 0.1207  0.0017  48  LEU   B CG  
1213 C CD1 . LEU   B 31  ? 0.9121 0.6020 1.0066 -0.0670 0.1135  -0.0042 48  LEU   B CD1 
1214 C CD2 . LEU   B 31  ? 1.2226 0.8696 1.2824 -0.0582 0.1190  0.0124  48  LEU   B CD2 
1215 N N   . ASP   B 32  ? 1.0160 0.6206 1.0653 -0.0640 0.1202  -0.0152 49  ASP   B N   
1216 C CA  . ASP   B 32  ? 1.0116 0.6219 1.0676 -0.0764 0.1205  -0.0258 49  ASP   B CA  
1217 C C   . ASP   B 32  ? 0.9926 0.6430 1.0736 -0.0888 0.1182  -0.0301 49  ASP   B C   
1218 O O   . ASP   B 32  ? 0.9762 0.6590 1.0781 -0.0833 0.1122  -0.0332 49  ASP   B O   
1219 C CB  . ASP   B 32  ? 1.0616 0.6764 1.1221 -0.0624 0.1159  -0.0294 49  ASP   B CB  
1220 C CG  . ASP   B 32  ? 1.0457 0.6440 1.0981 -0.0729 0.1181  -0.0389 49  ASP   B CG  
1221 O OD1 . ASP   B 32  ? 0.9968 0.6036 1.0552 -0.0924 0.1199  -0.0455 49  ASP   B OD1 
1222 O OD2 . ASP   B 32  ? 1.1589 0.7370 1.1990 -0.0617 0.1179  -0.0402 49  ASP   B OD2 
1223 N N   . LEU   B 33  ? 0.9677 0.6150 1.0452 -0.1055 0.1235  -0.0301 50  LEU   B N   
1224 C CA  . LEU   B 33  ? 0.8799 0.5652 0.9798 -0.1165 0.1220  -0.0341 50  LEU   B CA  
1225 C C   . LEU   B 33  ? 0.8853 0.5937 1.0015 -0.1238 0.1184  -0.0449 50  LEU   B C   
1226 O O   . LEU   B 33  ? 0.9935 0.7384 1.1312 -0.1257 0.1144  -0.0483 50  LEU   B O   
1227 C CB  . LEU   B 33  ? 0.8719 0.5484 0.9634 -0.1346 0.1295  -0.0332 50  LEU   B CB  
1228 C CG  . LEU   B 33  ? 0.8715 0.5569 0.9644 -0.1304 0.1305  -0.0247 50  LEU   B CG  
1229 C CD1 . LEU   B 33  ? 0.8875 0.5646 0.9714 -0.1500 0.1389  -0.0246 50  LEU   B CD1 
1230 C CD2 . LEU   B 33  ? 0.9100 0.6388 1.0291 -0.1228 0.1235  -0.0258 50  LEU   B CD2 
1231 N N   . ALA   B 34  ? 0.8961 0.5830 1.0012 -0.1272 0.1195  -0.0505 51  ALA   B N   
1232 C CA  . ALA   B 34  ? 0.9398 0.6465 1.0583 -0.1311 0.1151  -0.0604 51  ALA   B CA  
1233 C C   . ALA   B 34  ? 0.9129 0.6362 1.0425 -0.1123 0.1079  -0.0595 51  ALA   B C   
1234 O O   . ALA   B 34  ? 0.9486 0.6916 1.0905 -0.1136 0.1033  -0.0670 51  ALA   B O   
1235 C CB  . ALA   B 34  ? 0.9688 0.6445 1.0692 -0.1418 0.1189  -0.0669 51  ALA   B CB  
1236 N N   . ALA   B 35  ? 0.8994 0.6160 1.0248 -0.0954 0.1066  -0.0506 52  ALA   B N   
1237 C CA  . ALA   B 35  ? 0.8854 0.6187 1.0210 -0.0785 0.1004  -0.0491 52  ALA   B CA  
1238 C C   . ALA   B 35  ? 0.8486 0.6071 0.9978 -0.0696 0.0965  -0.0424 52  ALA   B C   
1239 O O   . ALA   B 35  ? 0.8268 0.6025 0.9858 -0.0578 0.0912  -0.0414 52  ALA   B O   
1240 C CB  . ALA   B 35  ? 0.9049 0.6095 1.0233 -0.0643 0.1017  -0.0456 52  ALA   B CB  
1241 N N   . LEU   B 36  ? 0.8299 0.5900 0.9785 -0.0752 0.0991  -0.0377 53  LEU   B N   
1242 C CA  . LEU   B 36  ? 0.8255 0.6090 0.9860 -0.0676 0.0952  -0.0320 53  LEU   B CA  
1243 C C   . LEU   B 36  ? 0.7629 0.5802 0.9431 -0.0734 0.0908  -0.0382 53  LEU   B C   
1244 O O   . LEU   B 36  ? 0.7711 0.5960 0.9557 -0.0873 0.0931  -0.0441 53  LEU   B O   
1245 C CB  . LEU   B 36  ? 0.8496 0.6226 1.0013 -0.0712 0.0996  -0.0251 53  LEU   B CB  
1246 C CG  . LEU   B 36  ? 0.7311 0.5274 0.8937 -0.0640 0.0954  -0.0196 53  LEU   B CG  
1247 C CD1 . LEU   B 36  ? 0.8055 0.6102 0.9728 -0.0473 0.0893  -0.0159 53  LEU   B CD1 
1248 C CD2 . LEU   B 36  ? 0.6924 0.4763 0.8441 -0.0661 0.0997  -0.0123 53  LEU   B CD2 
1249 N N   . ILE   B 37  ? 0.7584 0.5961 0.9497 -0.0627 0.0846  -0.0368 54  ILE   B N   
1250 C CA  . ILE   B 37  ? 0.7061 0.5739 0.9136 -0.0651 0.0797  -0.0414 54  ILE   B CA  
1251 C C   . ILE   B 37  ? 0.6718 0.5529 0.8842 -0.0560 0.0759  -0.0345 54  ILE   B C   
1252 O O   . ILE   B 37  ? 0.6841 0.5638 0.8952 -0.0447 0.0729  -0.0300 54  ILE   B O   
1253 C CB  . ILE   B 37  ? 0.6849 0.5624 0.8987 -0.0624 0.0751  -0.0480 54  ILE   B CB  
1254 C CG1 . ILE   B 37  ? 0.7075 0.5724 0.9160 -0.0726 0.0783  -0.0556 54  ILE   B CG1 
1255 C CG2 . ILE   B 37  ? 0.6550 0.5612 0.8829 -0.0625 0.0694  -0.0516 54  ILE   B CG2 
1256 C CD1 . ILE   B 37  ? 0.6981 0.5387 0.8940 -0.0663 0.0801  -0.0550 54  ILE   B CD1 
1257 N N   . VAL   B 38  ? 0.7977 0.6923 1.0156 -0.0611 0.0763  -0.0342 55  VAL   B N   
1258 C CA  . VAL   B 38  ? 0.7385 0.6446 0.9595 -0.0538 0.0728  -0.0283 55  VAL   B CA  
1259 C C   . VAL   B 38  ? 0.6775 0.6091 0.9108 -0.0551 0.0681  -0.0335 55  VAL   B C   
1260 O O   . VAL   B 38  ? 0.7159 0.6577 0.9543 -0.0639 0.0701  -0.0391 55  VAL   B O   
1261 C CB  . VAL   B 38  ? 0.7889 0.6854 1.0021 -0.0567 0.0775  -0.0223 55  VAL   B CB  
1262 C CG1 . VAL   B 38  ? 0.7128 0.6204 0.9280 -0.0488 0.0734  -0.0165 55  VAL   B CG1 
1263 C CG2 . VAL   B 38  ? 0.7700 0.6383 0.9683 -0.0550 0.0822  -0.0173 55  VAL   B CG2 
1264 N N   . TYR   B 39  ? 0.6043 0.5460 0.8413 -0.0463 0.0620  -0.0318 56  TYR   B N   
1265 C CA  . TYR   B 39  ? 0.6314 0.5935 0.8765 -0.0451 0.0568  -0.0358 56  TYR   B CA  
1266 C C   . TYR   B 39  ? 0.5635 0.5302 0.8067 -0.0392 0.0539  -0.0296 56  TYR   B C   
1267 O O   . TYR   B 39  ? 0.5904 0.5520 0.8299 -0.0324 0.0514  -0.0242 56  TYR   B O   
1268 C CB  . TYR   B 39  ? 0.6333 0.6011 0.8816 -0.0410 0.0516  -0.0399 56  TYR   B CB  
1269 C CG  . TYR   B 39  ? 0.6294 0.6002 0.8815 -0.0473 0.0523  -0.0484 56  TYR   B CG  
1270 C CD1 . TYR   B 39  ? 0.6248 0.5881 0.8757 -0.0567 0.0581  -0.0514 56  TYR   B CD1 
1271 C CD2 . TYR   B 39  ? 0.5552 0.5355 0.8107 -0.0444 0.0470  -0.0535 56  TYR   B CD2 
1272 C CE1 . TYR   B 39  ? 0.5744 0.5413 0.8286 -0.0634 0.0583  -0.0596 56  TYR   B CE1 
1273 C CE2 . TYR   B 39  ? 0.5188 0.5026 0.7772 -0.0499 0.0470  -0.0616 56  TYR   B CE2 
1274 C CZ  . TYR   B 39  ? 0.4484 0.4263 0.7068 -0.0596 0.0525  -0.0648 56  TYR   B CZ  
1275 O OH  . TYR   B 39  ? 0.5832 0.5655 0.8444 -0.0662 0.0520  -0.0733 56  TYR   B OH  
1276 N N   . TRP   B 40  ? 0.5573 0.5343 0.8028 -0.0418 0.0543  -0.0308 57  TRP   B N   
1277 C CA  . TRP   B 40  ? 0.5746 0.5566 0.8175 -0.0365 0.0511  -0.0264 57  TRP   B CA  
1278 C C   . TRP   B 40  ? 0.5559 0.5531 0.8034 -0.0334 0.0453  -0.0317 57  TRP   B C   
1279 O O   . TRP   B 40  ? 0.6457 0.6545 0.8990 -0.0369 0.0460  -0.0383 57  TRP   B O   
1280 C CB  . TRP   B 40  ? 0.5512 0.5321 0.7910 -0.0404 0.0560  -0.0238 57  TRP   B CB  
1281 C CG  . TRP   B 40  ? 0.5345 0.4984 0.7654 -0.0395 0.0595  -0.0158 57  TRP   B CG  
1282 C CD1 . TRP   B 40  ? 0.6564 0.6062 0.8821 -0.0452 0.0661  -0.0143 57  TRP   B CD1 
1283 C CD2 . TRP   B 40  ? 0.6473 0.6061 0.8720 -0.0324 0.0561  -0.0085 57  TRP   B CD2 
1284 N NE1 . TRP   B 40  ? 0.7236 0.6591 0.9397 -0.0406 0.0669  -0.0062 57  TRP   B NE1 
1285 C CE2 . TRP   B 40  ? 0.6787 0.6212 0.8951 -0.0327 0.0606  -0.0027 57  TRP   B CE2 
1286 C CE3 . TRP   B 40  ? 0.6151 0.5810 0.8395 -0.0263 0.0496  -0.0065 57  TRP   B CE3 
1287 C CZ2 . TRP   B 40  ? 0.6719 0.6078 0.8812 -0.0261 0.0583  0.0048  57  TRP   B CZ2 
1288 C CZ3 . TRP   B 40  ? 0.5659 0.5257 0.7838 -0.0214 0.0476  0.0008  57  TRP   B CZ3 
1289 C CH2 . TRP   B 40  ? 0.5870 0.5333 0.7982 -0.0209 0.0517  0.0063  57  TRP   B CH2 
1290 N N   . GLU   B 41  ? 0.4733 0.4703 0.7172 -0.0270 0.0396  -0.0288 58  GLU   B N   
1291 C CA  . GLU   B 41  ? 0.6122 0.6187 0.8566 -0.0232 0.0337  -0.0331 58  GLU   B CA  
1292 C C   . GLU   B 41  ? 0.6087 0.6135 0.8455 -0.0183 0.0295  -0.0286 58  GLU   B C   
1293 O O   . GLU   B 41  ? 0.5631 0.5606 0.7955 -0.0177 0.0300  -0.0221 58  GLU   B O   
1294 C CB  . GLU   B 41  ? 0.6019 0.6071 0.8472 -0.0217 0.0305  -0.0358 58  GLU   B CB  
1295 C CG  . GLU   B 41  ? 0.7117 0.7274 0.9606 -0.0210 0.0274  -0.0438 58  GLU   B CG  
1296 C CD  . GLU   B 41  ? 0.7073 0.7208 0.9582 -0.0221 0.0267  -0.0472 58  GLU   B CD  
1297 O OE1 . GLU   B 41  ? 0.7179 0.7268 0.9638 -0.0185 0.0230  -0.0454 58  GLU   B OE1 
1298 O OE2 . GLU   B 41  ? 0.6100 0.6259 0.8665 -0.0272 0.0300  -0.0518 58  GLU   B OE2 
1299 N N   . MET   B 42  ? 0.7104 0.7217 0.9448 -0.0146 0.0249  -0.0325 59  MET   B N   
1300 C CA  . MET   B 42  ? 0.6555 0.6625 0.8801 -0.0102 0.0198  -0.0294 59  MET   B CA  
1301 C C   . MET   B 42  ? 0.7540 0.7625 0.9744 -0.0060 0.0140  -0.0340 59  MET   B C   
1302 O O   . MET   B 42  ? 0.7525 0.7695 0.9750 -0.0033 0.0130  -0.0401 59  MET   B O   
1303 C CB  . MET   B 42  ? 0.6050 0.6143 0.8257 -0.0088 0.0210  -0.0287 59  MET   B CB  
1304 C CG  . MET   B 42  ? 0.7338 0.7355 0.9423 -0.0053 0.0162  -0.0248 59  MET   B CG  
1305 S SD  . MET   B 42  ? 0.8088 0.8097 1.0072 0.0015  0.0093  -0.0300 59  MET   B SD  
1306 C CE  . MET   B 42  ? 0.7812 0.7982 0.9887 0.0043  0.0122  -0.0381 59  MET   B CE  
1307 N N   . GLU   B 43  ? 0.9360 0.9366 1.1497 -0.0054 0.0101  -0.0311 60  GLU   B N   
1308 C CA  . GLU   B 43  ? 1.0070 1.0045 1.2126 -0.0017 0.0044  -0.0342 60  GLU   B CA  
1309 C C   . GLU   B 43  ? 1.0143 1.0201 1.2260 0.0001  0.0040  -0.0415 60  GLU   B C   
1310 O O   . GLU   B 43  ? 1.0284 1.0390 1.2372 0.0053  0.0010  -0.0464 60  GLU   B O   
1311 C CB  . GLU   B 43  ? 1.0318 1.0237 1.2246 0.0027  0.0001  -0.0339 60  GLU   B CB  
1312 C CG  . GLU   B 43  ? 1.0110 0.9936 1.1953 0.0000  -0.0011 -0.0271 60  GLU   B CG  
1313 C CD  . GLU   B 43  ? 1.0895 1.0641 1.2592 0.0039  -0.0051 -0.0272 60  GLU   B CD  
1314 O OE1 . GLU   B 43  ? 1.0871 1.0647 1.2544 0.0099  -0.0063 -0.0324 60  GLU   B OE1 
1315 O OE2 . GLU   B 43  ? 0.9651 0.9308 1.1253 0.0011  -0.0073 -0.0225 60  GLU   B OE2 
1316 N N   . ASP   B 44  ? 0.8941 0.9017 1.1139 -0.0037 0.0069  -0.0422 61  ASP   B N   
1317 C CA  . ASP   B 44  ? 0.8644 0.8798 1.0904 -0.0035 0.0066  -0.0492 61  ASP   B CA  
1318 C C   . ASP   B 44  ? 0.8389 0.8677 1.0718 -0.0025 0.0077  -0.0550 61  ASP   B C   
1319 O O   . ASP   B 44  ? 0.8659 0.9035 1.1002 0.0009  0.0044  -0.0615 61  ASP   B O   
1320 C CB  . ASP   B 44  ? 0.9130 0.9238 1.1295 0.0009  0.0006  -0.0515 61  ASP   B CB  
1321 C CG  . ASP   B 44  ? 0.8838 0.8837 1.0938 -0.0013 0.0002  -0.0462 61  ASP   B CG  
1322 O OD1 . ASP   B 44  ? 0.8880 0.8872 1.1046 -0.0055 0.0048  -0.0431 61  ASP   B OD1 
1323 O OD2 . ASP   B 44  ? 0.8222 0.8140 1.0196 0.0013  -0.0044 -0.0451 61  ASP   B OD2 
1324 N N   . LYS   B 45  ? 0.8245 0.8563 1.0619 -0.0054 0.0124  -0.0527 62  LYS   B N   
1325 C CA  . LYS   B 45  ? 0.7854 0.8320 1.0306 -0.0062 0.0151  -0.0578 62  LYS   B CA  
1326 C C   . LYS   B 45  ? 0.7277 0.7742 0.9806 -0.0147 0.0227  -0.0556 62  LYS   B C   
1327 O O   . LYS   B 45  ? 0.7290 0.7672 0.9782 -0.0161 0.0257  -0.0492 62  LYS   B O   
1328 C CB  . LYS   B 45  ? 0.7829 0.8322 1.0216 0.0001  0.0129  -0.0575 62  LYS   B CB  
1329 N N   . ASN   B 46  ? 0.6652 0.7197 0.9272 -0.0206 0.0258  -0.0608 63  ASN   B N   
1330 C CA  . ASN   B 46  ? 0.6545 0.7047 0.9210 -0.0295 0.0332  -0.0589 63  ASN   B CA  
1331 C C   . ASN   B 46  ? 0.6773 0.7334 0.9450 -0.0321 0.0380  -0.0574 63  ASN   B C   
1332 O O   . ASN   B 46  ? 0.7283 0.8003 0.9994 -0.0295 0.0370  -0.0620 63  ASN   B O   
1333 C CB  . ASN   B 46  ? 0.7362 0.7935 1.0106 -0.0364 0.0352  -0.0659 63  ASN   B CB  
1334 C CG  . ASN   B 46  ? 0.7335 0.7764 1.0072 -0.0446 0.0414  -0.0629 63  ASN   B CG  
1335 O OD1 . ASN   B 46  ? 0.6389 0.6818 0.9146 -0.0523 0.0478  -0.0627 63  ASN   B OD1 
1336 N ND2 . ASN   B 46  ? 0.6750 0.7044 0.9443 -0.0426 0.0400  -0.0605 63  ASN   B ND2 
1337 N N   . ILE   B 47  ? 0.6869 0.7300 0.9508 -0.0364 0.0433  -0.0509 64  ILE   B N   
1338 C CA  . ILE   B 47  ? 0.6781 0.7235 0.9411 -0.0398 0.0488  -0.0485 64  ILE   B CA  
1339 C C   . ILE   B 47  ? 0.6944 0.7378 0.9610 -0.0511 0.0567  -0.0498 64  ILE   B C   
1340 O O   . ILE   B 47  ? 0.7050 0.7611 0.9763 -0.0569 0.0614  -0.0533 64  ILE   B O   
1341 C CB  . ILE   B 47  ? 0.5502 0.5811 0.8031 -0.0356 0.0484  -0.0396 64  ILE   B CB  
1342 C CG1 . ILE   B 47  ? 0.6219 0.6510 0.8695 -0.0266 0.0404  -0.0382 64  ILE   B CG1 
1343 C CG2 . ILE   B 47  ? 0.5802 0.6150 0.8305 -0.0373 0.0530  -0.0377 64  ILE   B CG2 
1344 C CD1 . ILE   B 47  ? 0.6081 0.6292 0.8463 -0.0226 0.0390  -0.0315 64  ILE   B CD1 
1345 N N   . ILE   B 48  ? 0.6802 0.7073 0.9438 -0.0546 0.0585  -0.0472 65  ILE   B N   
1346 C CA  . ILE   B 48  ? 0.6219 0.6402 0.8847 -0.0655 0.0661  -0.0475 65  ILE   B CA  
1347 C C   . ILE   B 48  ? 0.6423 0.6485 0.9041 -0.0671 0.0653  -0.0491 65  ILE   B C   
1348 O O   . ILE   B 48  ? 0.6776 0.6736 0.9352 -0.0595 0.0613  -0.0452 65  ILE   B O   
1349 C CB  . ILE   B 48  ? 0.6090 0.6106 0.8616 -0.0669 0.0714  -0.0390 65  ILE   B CB  
1350 C CG1 . ILE   B 48  ? 0.6294 0.6433 0.8831 -0.0705 0.0756  -0.0395 65  ILE   B CG1 
1351 C CG2 . ILE   B 48  ? 0.6707 0.6514 0.9164 -0.0745 0.0774  -0.0369 65  ILE   B CG2 
1352 C CD1 . ILE   B 48  ? 0.7078 0.7260 0.9645 -0.0841 0.0837  -0.0438 65  ILE   B CD1 
1353 N N   . GLN   B 49  ? 0.6840 0.6920 0.9493 -0.0774 0.0692  -0.0551 66  GLN   B N   
1354 C CA  . GLN   B 49  ? 0.7276 0.7221 0.9902 -0.0803 0.0693  -0.0574 66  GLN   B CA  
1355 C C   . GLN   B 49  ? 0.7218 0.6988 0.9771 -0.0920 0.0777  -0.0563 66  GLN   B C   
1356 O O   . GLN   B 49  ? 0.7104 0.6972 0.9701 -0.1036 0.0819  -0.0617 66  GLN   B O   
1357 C CB  . GLN   B 49  ? 0.7189 0.7309 0.9909 -0.0822 0.0649  -0.0670 66  GLN   B CB  
1358 C CG  . GLN   B 49  ? 0.6269 0.6429 0.8998 -0.0707 0.0569  -0.0672 66  GLN   B CG  
1359 C CD  . GLN   B 49  ? 0.6276 0.6521 0.9054 -0.0729 0.0532  -0.0758 66  GLN   B CD  
1360 O OE1 . GLN   B 49  ? 0.7103 0.7394 0.9918 -0.0835 0.0563  -0.0821 66  GLN   B OE1 
1361 N NE2 . GLN   B 49  ? 0.5347 0.5612 0.8116 -0.0636 0.0466  -0.0762 66  GLN   B NE2 
1362 N N   . PHE   B 50  ? 0.7702 0.7213 1.0136 -0.0888 0.0800  -0.0496 67  PHE   B N   
1363 C CA  . PHE   B 50  ? 0.8262 0.7539 1.0580 -0.0983 0.0877  -0.0475 67  PHE   B CA  
1364 C C   . PHE   B 50  ? 0.7687 0.6803 0.9953 -0.1001 0.0877  -0.0513 67  PHE   B C   
1365 O O   . PHE   B 50  ? 0.7202 0.6160 0.9398 -0.0902 0.0857  -0.0470 67  PHE   B O   
1366 C CB  . PHE   B 50  ? 0.8233 0.7315 1.0427 -0.0919 0.0902  -0.0372 67  PHE   B CB  
1367 C CG  . PHE   B 50  ? 0.8447 0.7269 1.0493 -0.1013 0.0984  -0.0342 67  PHE   B CG  
1368 C CD1 . PHE   B 50  ? 0.8400 0.6943 1.0317 -0.1004 0.1004  -0.0329 67  PHE   B CD1 
1369 C CD2 . PHE   B 50  ? 0.9222 0.8060 1.1238 -0.1106 0.1045  -0.0326 67  PHE   B CD2 
1370 C CE1 . PHE   B 50  ? 0.8627 0.6889 1.0374 -0.1087 0.1079  -0.0299 67  PHE   B CE1 
1371 C CE2 . PHE   B 50  ? 0.8932 0.7502 1.0785 -0.1201 0.1124  -0.0295 67  PHE   B CE2 
1372 C CZ  . PHE   B 50  ? 0.8335 0.6604 1.0046 -0.1191 0.1139  -0.0280 67  PHE   B CZ  
1373 N N   . VAL   B 51  ? 0.8877 0.8045 1.1179 -0.1128 0.0899  -0.0596 68  VAL   B N   
1374 C CA  . VAL   B 51  ? 0.8268 0.7272 1.0507 -0.1164 0.0902  -0.0643 68  VAL   B CA  
1375 C C   . VAL   B 51  ? 0.8174 0.7010 1.0317 -0.1334 0.0981  -0.0671 68  VAL   B C   
1376 O O   . VAL   B 51  ? 0.9058 0.8062 1.1273 -0.1458 0.1012  -0.0711 68  VAL   B O   
1377 C CB  . VAL   B 51  ? 0.7521 0.6752 0.9887 -0.1157 0.0836  -0.0732 68  VAL   B CB  
1378 C CG1 . VAL   B 51  ? 0.6980 0.6080 0.9287 -0.1255 0.0854  -0.0805 68  VAL   B CG1 
1379 C CG2 . VAL   B 51  ? 0.7718 0.6999 1.0112 -0.0993 0.0767  -0.0700 68  VAL   B CG2 
1380 N N   . HIS   B 52  ? 0.8651 0.7155 1.0625 -0.1339 0.1015  -0.0650 69  HIS   B N   
1381 C CA  . HIS   B 52  ? 0.9336 0.7609 1.1175 -0.1505 0.1089  -0.0679 69  HIS   B CA  
1382 C C   . HIS   B 52  ? 0.8592 0.6813 1.0370 -0.1606 0.1162  -0.0632 69  HIS   B C   
1383 O O   . HIS   B 52  ? 0.8849 0.7072 1.0609 -0.1789 0.1218  -0.0681 69  HIS   B O   
1384 C CB  . HIS   B 52  ? 0.9091 0.7522 1.1018 -0.1643 0.1077  -0.0797 69  HIS   B CB  
1385 C CG  . HIS   B 52  ? 1.0099 0.8362 1.1951 -0.1610 0.1049  -0.0842 69  HIS   B CG  
1386 N ND1 . HIS   B 52  ? 0.9716 0.7580 1.1353 -0.1580 0.1086  -0.0804 69  HIS   B ND1 
1387 C CD2 . HIS   B 52  ? 1.0442 0.8875 1.2394 -0.1593 0.0987  -0.0922 69  HIS   B CD2 
1388 C CE1 . HIS   B 52  ? 0.9661 0.7461 1.1272 -0.1548 0.1052  -0.0861 69  HIS   B CE1 
1389 N NE2 . HIS   B 52  ? 1.0149 0.8289 1.1947 -0.1560 0.0991  -0.0932 69  HIS   B NE2 
1390 N N   . GLY   B 53  ? 0.9350 0.7532 1.1094 -0.1492 0.1162  -0.0537 70  GLY   B N   
1391 C CA  . GLY   B 53  ? 0.9295 0.7372 1.0940 -0.1566 0.1233  -0.0479 70  GLY   B CA  
1392 C C   . GLY   B 53  ? 0.9606 0.8019 1.1408 -0.1602 0.1235  -0.0486 70  GLY   B C   
1393 O O   . GLY   B 53  ? 0.9594 0.7934 1.1314 -0.1624 0.1285  -0.0422 70  GLY   B O   
1394 N N   . GLU   B 54  ? 1.0552 0.9322 1.2561 -0.1602 0.1182  -0.0562 71  GLU   B N   
1395 C CA  . GLU   B 54  ? 1.0869 0.9966 1.3023 -0.1628 0.1185  -0.0580 71  GLU   B CA  
1396 C C   . GLU   B 54  ? 1.0771 1.0143 1.3087 -0.1478 0.1091  -0.0599 71  GLU   B C   
1397 O O   . GLU   B 54  ? 1.0490 0.9809 1.2810 -0.1374 0.1029  -0.0602 71  GLU   B O   
1398 C CB  . GLU   B 54  ? 1.0464 0.9745 1.2697 -0.1827 0.1236  -0.0670 71  GLU   B CB  
1399 N N   . GLU   B 55  ? 0.9706 0.9364 1.2141 -0.1466 0.1083  -0.0613 72  GLU   B N   
1400 C CA  . GLU   B 55  ? 0.8966 0.8866 1.1529 -0.1328 0.0996  -0.0632 72  GLU   B CA  
1401 C C   . GLU   B 55  ? 0.8904 0.9093 1.1623 -0.1376 0.0959  -0.0743 72  GLU   B C   
1402 O O   . GLU   B 55  ? 0.9256 0.9597 1.2036 -0.1516 0.1008  -0.0806 72  GLU   B O   
1403 C CB  . GLU   B 55  ? 0.8768 0.8802 1.1354 -0.1267 0.1001  -0.0588 72  GLU   B CB  
1404 C CG  . GLU   B 55  ? 0.8913 0.8692 1.1347 -0.1214 0.1029  -0.0479 72  GLU   B CG  
1405 C CD  . GLU   B 55  ? 0.8760 0.8663 1.1198 -0.1197 0.1055  -0.0446 72  GLU   B CD  
1406 O OE1 . GLU   B 55  ? 0.8817 0.9009 1.1382 -0.1180 0.1031  -0.0503 72  GLU   B OE1 
1407 O OE2 . GLU   B 55  ? 0.8085 0.7791 1.0389 -0.1193 0.1097  -0.0365 72  GLU   B OE2 
1408 N N   . ASP   B 56  ? 0.9662 0.9933 1.2439 -0.1261 0.0873  -0.0769 73  ASP   B N   
1409 C CA  . ASP   B 56  ? 1.0006 1.0559 1.2922 -0.1267 0.0819  -0.0869 73  ASP   B CA  
1410 C C   . ASP   B 56  ? 0.9651 1.0408 1.2638 -0.1121 0.0751  -0.0864 73  ASP   B C   
1411 O O   . ASP   B 56  ? 0.8975 0.9685 1.1942 -0.0999 0.0681  -0.0847 73  ASP   B O   
1412 C CB  . ASP   B 56  ? 1.0019 1.0466 1.2913 -0.1263 0.0777  -0.0909 73  ASP   B CB  
1413 C CG  . ASP   B 56  ? 1.0434 1.1162 1.3458 -0.1297 0.0728  -0.1019 73  ASP   B CG  
1414 O OD1 . ASP   B 56  ? 0.9303 1.0298 1.2435 -0.1364 0.0746  -0.1074 73  ASP   B OD1 
1415 O OD2 . ASP   B 56  ? 1.1426 1.2119 1.4443 -0.1253 0.0671  -0.1054 73  ASP   B OD2 
1416 N N   . LEU   B 57  ? 0.8999 0.9975 1.2057 -0.1136 0.0775  -0.0882 74  LEU   B N   
1417 C CA  . LEU   B 57  ? 0.7925 0.9072 1.1025 -0.0997 0.0719  -0.0878 74  LEU   B CA  
1418 C C   . LEU   B 57  ? 0.7846 0.9244 1.1051 -0.0931 0.0639  -0.0966 74  LEU   B C   
1419 O O   . LEU   B 57  ? 0.8620 1.0187 1.1859 -0.0822 0.0594  -0.0979 74  LEU   B O   
1420 C CB  . LEU   B 57  ? 0.7552 0.8803 1.0660 -0.1021 0.0779  -0.0855 74  LEU   B CB  
1421 C CG  . LEU   B 57  ? 0.8564 0.9556 1.1551 -0.1096 0.0861  -0.0770 74  LEU   B CG  
1422 C CD1 . LEU   B 57  ? 0.8508 0.9553 1.1520 -0.1279 0.0954  -0.0806 74  LEU   B CD1 
1423 C CD2 . LEU   B 57  ? 0.7402 0.8353 1.0321 -0.1006 0.0866  -0.0697 74  LEU   B CD2 
1424 N N   . LYS   B 58  ? 0.7805 0.9216 1.1045 -0.0990 0.0617  -0.1026 75  LYS   B N   
1425 C CA  . LYS   B 58  ? 0.7855 0.9498 1.1182 -0.0928 0.0537  -0.1112 75  LYS   B CA  
1426 C C   . LYS   B 58  ? 0.7382 0.8984 1.0657 -0.0754 0.0445  -0.1090 75  LYS   B C   
1427 O O   . LYS   B 58  ? 0.6834 0.8642 1.0167 -0.0681 0.0377  -0.1156 75  LYS   B O   
1428 C CB  . LYS   B 58  ? 0.7582 0.9204 1.0931 -0.1036 0.0534  -0.1176 75  LYS   B CB  
1429 N N   . VAL   B 59  ? 0.7455 0.8801 1.0616 -0.0690 0.0442  -0.0999 76  VAL   B N   
1430 C CA  . VAL   B 59  ? 0.7107 0.8389 1.0198 -0.0544 0.0365  -0.0968 76  VAL   B CA  
1431 C C   . VAL   B 59  ? 0.7810 0.9027 1.0837 -0.0471 0.0372  -0.0895 76  VAL   B C   
1432 O O   . VAL   B 59  ? 0.7605 0.8732 1.0552 -0.0365 0.0316  -0.0858 76  VAL   B O   
1433 C CB  . VAL   B 59  ? 0.7621 0.8677 1.0632 -0.0531 0.0342  -0.0935 76  VAL   B CB  
1434 C CG1 . VAL   B 59  ? 0.7764 0.8912 1.0815 -0.0543 0.0295  -0.1017 76  VAL   B CG1 
1435 C CG2 . VAL   B 59  ? 0.7166 0.8010 1.0132 -0.0622 0.0416  -0.0879 76  VAL   B CG2 
1436 N N   . GLN   B 60  ? 0.7859 0.9109 1.0907 -0.0533 0.0442  -0.0874 77  GLN   B N   
1437 C CA  . GLN   B 60  ? 0.8330 0.9521 1.1311 -0.0469 0.0452  -0.0808 77  GLN   B CA  
1438 C C   . GLN   B 60  ? 0.9251 1.0604 1.2234 -0.0347 0.0390  -0.0845 77  GLN   B C   
1439 O O   . GLN   B 60  ? 0.9386 1.0985 1.2462 -0.0339 0.0378  -0.0927 77  GLN   B O   
1440 C CB  . GLN   B 60  ? 0.8287 0.9503 1.1287 -0.0566 0.0543  -0.0788 77  GLN   B CB  
1441 C CG  . GLN   B 60  ? 0.8492 0.9692 1.1428 -0.0499 0.0553  -0.0737 77  GLN   B CG  
1442 C CD  . GLN   B 60  ? 0.8589 0.9781 1.1518 -0.0598 0.0647  -0.0707 77  GLN   B CD  
1443 O OE1 . GLN   B 60  ? 0.8796 1.0123 1.1808 -0.0707 0.0705  -0.0757 77  GLN   B OE1 
1444 N NE2 . GLN   B 60  ? 0.8262 0.9295 1.1086 -0.0565 0.0664  -0.0626 77  GLN   B NE2 
1445 N N   . HIS   B 61  ? 1.1237 1.2450 1.4109 -0.0251 0.0350  -0.0787 78  HIS   B N   
1446 C CA  . HIS   B 61  ? 1.0779 1.2087 1.3610 -0.0128 0.0294  -0.0814 78  HIS   B CA  
1447 C C   . HIS   B 61  ? 1.1234 1.2720 1.4114 -0.0130 0.0344  -0.0837 78  HIS   B C   
1448 O O   . HIS   B 61  ? 1.1184 1.2633 1.4071 -0.0213 0.0419  -0.0798 78  HIS   B O   
1449 C CB  . HIS   B 61  ? 1.1261 1.2347 1.3943 -0.0050 0.0248  -0.0741 78  HIS   B CB  
1450 C CG  . HIS   B 61  ? 1.2546 1.3640 1.5145 0.0077  0.0164  -0.0772 78  HIS   B CG  
1451 N ND1 . HIS   B 61  ? 1.2361 1.3454 1.4870 0.0171  0.0142  -0.0769 78  HIS   B ND1 
1452 C CD2 . HIS   B 61  ? 1.2945 1.4022 1.5513 0.0129  0.0098  -0.0804 78  HIS   B CD2 
1453 C CE1 . HIS   B 61  ? 1.2462 1.3526 1.4882 0.0277  0.0065  -0.0798 78  HIS   B CE1 
1454 N NE2 . HIS   B 61  ? 1.2930 1.3985 1.5384 0.0253  0.0036  -0.0818 78  HIS   B NE2 
1455 N N   . SER   B 62  ? 1.1181 1.2862 1.4084 -0.0032 0.0303  -0.0904 79  SER   B N   
1456 C CA  . SER   B 62  ? 0.9909 1.1797 1.2865 -0.0019 0.0350  -0.0937 79  SER   B CA  
1457 C C   . SER   B 62  ? 0.9710 1.1438 1.2549 0.0002  0.0382  -0.0863 79  SER   B C   
1458 O O   . SER   B 62  ? 0.8795 1.0618 1.1670 -0.0052 0.0457  -0.0859 79  SER   B O   
1459 C CB  . SER   B 62  ? 0.9174 1.1279 1.2150 0.0119  0.0288  -0.1019 79  SER   B CB  
1460 O OG  . SER   B 62  ? 1.0244 1.2175 1.3089 0.0236  0.0195  -0.1005 79  SER   B OG  
1461 N N   . SER   B 63  ? 0.9339 1.0826 1.2030 0.0074  0.0326  -0.0804 80  SER   B N   
1462 C CA  . SER   B 63  ? 0.8601 0.9928 1.1165 0.0099  0.0342  -0.0736 80  SER   B CA  
1463 C C   . SER   B 63  ? 0.8745 0.9983 1.1323 -0.0023 0.0423  -0.0672 80  SER   B C   
1464 O O   . SER   B 63  ? 0.8487 0.9650 1.0981 -0.0014 0.0451  -0.0626 80  SER   B O   
1465 C CB  . SER   B 63  ? 0.8079 0.9161 1.0488 0.0169  0.0265  -0.0687 80  SER   B CB  
1466 O OG  . SER   B 63  ? 0.9323 1.0266 1.1745 0.0097  0.0258  -0.0644 80  SER   B OG  
1467 N N   . TYR   B 64  ? 0.8992 1.0218 1.1655 -0.0132 0.0459  -0.0667 81  TYR   B N   
1468 C CA  . TYR   B 64  ? 0.8457 0.9557 1.1105 -0.0238 0.0531  -0.0602 81  TYR   B CA  
1469 C C   . TYR   B 64  ? 0.8579 0.9835 1.1330 -0.0353 0.0621  -0.0638 81  TYR   B C   
1470 O O   . TYR   B 64  ? 0.8530 0.9665 1.1243 -0.0441 0.0688  -0.0583 81  TYR   B O   
1471 C CB  . TYR   B 64  ? 0.7622 0.8529 1.0249 -0.0278 0.0511  -0.0556 81  TYR   B CB  
1472 C CG  . TYR   B 64  ? 0.6448 0.7175 0.8961 -0.0199 0.0444  -0.0498 81  TYR   B CG  
1473 C CD1 . TYR   B 64  ? 0.6633 0.7231 0.9040 -0.0183 0.0452  -0.0428 81  TYR   B CD1 
1474 C CD2 . TYR   B 64  ? 0.6550 0.7238 0.9052 -0.0150 0.0373  -0.0515 81  TYR   B CD2 
1475 C CE1 . TYR   B 64  ? 0.6701 0.7153 0.9007 -0.0127 0.0390  -0.0379 81  TYR   B CE1 
1476 C CE2 . TYR   B 64  ? 0.6775 0.7306 0.9169 -0.0097 0.0318  -0.0463 81  TYR   B CE2 
1477 C CZ  . TYR   B 64  ? 0.6921 0.7343 0.9223 -0.0090 0.0326  -0.0397 81  TYR   B CZ  
1478 O OH  . TYR   B 64  ? 0.6801 0.7086 0.9000 -0.0052 0.0270  -0.0349 81  TYR   B OH  
1479 N N   . ARG   B 65  ? 0.9591 1.1110 1.2461 -0.0357 0.0624  -0.0727 82  ARG   B N   
1480 C CA  . ARG   B 65  ? 1.0294 1.1981 1.3269 -0.0488 0.0711  -0.0768 82  ARG   B CA  
1481 C C   . ARG   B 65  ? 1.0121 1.1823 1.3048 -0.0522 0.0792  -0.0732 82  ARG   B C   
1482 O O   . ARG   B 65  ? 1.0160 1.1885 1.3022 -0.0418 0.0773  -0.0722 82  ARG   B O   
1483 C CB  . ARG   B 65  ? 0.9528 1.1542 1.2648 -0.0472 0.0690  -0.0877 82  ARG   B CB  
1484 N N   . GLN   B 66  ? 0.8333 0.9998 1.1271 -0.0671 0.0883  -0.0713 83  GLN   B N   
1485 C CA  . GLN   B 66  ? 0.8129 0.9787 1.1010 -0.0737 0.0976  -0.0675 83  GLN   B CA  
1486 C C   . GLN   B 66  ? 0.8353 0.9736 1.1065 -0.0677 0.0966  -0.0574 83  GLN   B C   
1487 O O   . GLN   B 66  ? 0.8414 0.9766 1.1052 -0.0716 0.1037  -0.0536 83  GLN   B O   
1488 C CB  . GLN   B 66  ? 0.8048 1.0029 1.1008 -0.0700 0.1006  -0.0744 83  GLN   B CB  
1489 C CG  . GLN   B 66  ? 0.6922 0.9178 1.0027 -0.0843 0.1085  -0.0820 83  GLN   B CG  
1490 C CD  . GLN   B 66  ? 0.6150 0.8680 0.9414 -0.0806 0.1022  -0.0922 83  GLN   B CD  
1491 O OE1 . GLN   B 66  ? 0.6218 0.8802 0.9485 -0.0645 0.0931  -0.0948 83  GLN   B OE1 
1492 N NE2 . GLN   B 66  ? 0.4793 0.7488 0.8178 -0.0956 0.1069  -0.0981 83  GLN   B NE2 
1493 N N   . ARG   B 67  ? 0.8040 0.9230 1.0684 -0.0590 0.0883  -0.0531 84  ARG   B N   
1494 C CA  . ARG   B 67  ? 0.8086 0.9037 1.0578 -0.0535 0.0864  -0.0439 84  ARG   B CA  
1495 C C   . ARG   B 67  ? 0.8129 0.8822 1.0559 -0.0569 0.0851  -0.0370 84  ARG   B C   
1496 O O   . ARG   B 67  ? 0.7753 0.8257 1.0062 -0.0563 0.0864  -0.0290 84  ARG   B O   
1497 C CB  . ARG   B 67  ? 0.7242 0.8198 0.9684 -0.0389 0.0774  -0.0444 84  ARG   B CB  
1498 C CG  . ARG   B 67  ? 0.7445 0.8656 0.9950 -0.0319 0.0766  -0.0526 84  ARG   B CG  
1499 C CD  . ARG   B 67  ? 0.6960 0.8104 0.9346 -0.0184 0.0700  -0.0511 84  ARG   B CD  
1500 N NE  . ARG   B 67  ? 0.6961 0.8053 0.9337 -0.0099 0.0601  -0.0530 84  ARG   B NE  
1501 C CZ  . ARG   B 67  ? 0.6263 0.7136 0.8535 -0.0065 0.0539  -0.0471 84  ARG   B CZ  
1502 N NH1 . ARG   B 67  ? 0.6026 0.6722 0.8201 -0.0097 0.0556  -0.0391 84  ARG   B NH1 
1503 N NH2 . ARG   B 67  ? 0.6053 0.6891 0.8313 0.0002  0.0458  -0.0493 84  ARG   B NH2 
1504 N N   . ALA   B 68  ? 0.7788 0.8473 1.0292 -0.0596 0.0825  -0.0401 85  ALA   B N   
1505 C CA  . ALA   B 68  ? 0.6668 0.7122 0.9116 -0.0608 0.0808  -0.0344 85  ALA   B CA  
1506 C C   . ALA   B 68  ? 0.7500 0.7873 0.9952 -0.0739 0.0887  -0.0344 85  ALA   B C   
1507 O O   . ALA   B 68  ? 0.7494 0.8023 1.0045 -0.0822 0.0922  -0.0416 85  ALA   B O   
1508 C CB  . ALA   B 68  ? 0.6763 0.7229 0.9263 -0.0543 0.0724  -0.0374 85  ALA   B CB  
1509 N N   . ARG   B 69  ? 0.7685 0.7812 1.0020 -0.0756 0.0913  -0.0264 86  ARG   B N   
1510 C CA  . ARG   B 69  ? 0.7116 0.7092 0.9408 -0.0871 0.0984  -0.0254 86  ARG   B CA  
1511 C C   . ARG   B 69  ? 0.7378 0.7080 0.9555 -0.0821 0.0962  -0.0176 86  ARG   B C   
1512 O O   . ARG   B 69  ? 0.6948 0.6567 0.9047 -0.0732 0.0928  -0.0109 86  ARG   B O   
1513 C CB  . ARG   B 69  ? 0.6958 0.6930 0.9189 -0.0974 0.1081  -0.0239 86  ARG   B CB  
1514 C CG  . ARG   B 69  ? 0.7795 0.7618 0.9879 -0.0923 0.1096  -0.0149 86  ARG   B CG  
1515 C CD  . ARG   B 69  ? 0.8795 0.8494 1.0768 -0.1046 0.1203  -0.0116 86  ARG   B CD  
1516 N NE  . ARG   B 69  ? 0.9854 0.9401 1.1670 -0.0995 0.1215  -0.0028 86  ARG   B NE  
1517 C CZ  . ARG   B 69  ? 0.9892 0.9397 1.1607 -0.1074 0.1302  0.0000  86  ARG   B CZ  
1518 N NH1 . ARG   B 69  ? 1.0035 0.9651 1.1797 -0.1217 0.1389  -0.0053 86  ARG   B NH1 
1519 N NH2 . ARG   B 69  ? 1.0358 0.9715 1.1920 -0.1013 0.1301  0.0081  86  ARG   B NH2 
1520 N N   . LEU   B 70  ? 0.8330 0.7902 1.0497 -0.0874 0.0980  -0.0190 87  LEU   B N   
1521 C CA  . LEU   B 70  ? 0.7419 0.6728 0.9471 -0.0825 0.0970  -0.0122 87  LEU   B CA  
1522 C C   . LEU   B 70  ? 0.7343 0.6421 0.9235 -0.0896 0.1053  -0.0063 87  LEU   B C   
1523 O O   . LEU   B 70  ? 0.8865 0.7924 1.0744 -0.1029 0.1127  -0.0098 87  LEU   B O   
1524 C CB  . LEU   B 70  ? 0.7110 0.6370 0.9206 -0.0835 0.0949  -0.0167 87  LEU   B CB  
1525 C CG  . LEU   B 70  ? 0.8274 0.7294 1.0272 -0.0765 0.0932  -0.0114 87  LEU   B CG  
1526 C CD1 . LEU   B 70  ? 0.7845 0.6814 0.9780 -0.0642 0.0888  -0.0031 87  LEU   B CD1 
1527 C CD2 . LEU   B 70  ? 0.8010 0.7085 1.0094 -0.0737 0.0884  -0.0171 87  LEU   B CD2 
1528 N N   . LEU   B 71  ? 0.8344 0.7249 1.0108 -0.0811 0.1039  0.0025  88  LEU   B N   
1529 C CA  . LEU   B 71  ? 0.8747 0.7403 1.0327 -0.0856 0.1109  0.0092  88  LEU   B CA  
1530 C C   . LEU   B 71  ? 0.9582 0.7980 1.1066 -0.0892 0.1141  0.0096  88  LEU   B C   
1531 O O   . LEU   B 71  ? 1.0269 0.8523 1.1696 -0.0786 0.1098  0.0136  88  LEU   B O   
1532 C CB  . LEU   B 71  ? 0.9729 0.8298 1.1203 -0.0738 0.1071  0.0182  88  LEU   B CB  
1533 C CG  . LEU   B 71  ? 0.8992 0.7770 1.0522 -0.0694 0.1036  0.0185  88  LEU   B CG  
1534 C CD1 . LEU   B 71  ? 0.8572 0.7202 0.9937 -0.0635 0.1037  0.0277  88  LEU   B CD1 
1535 C CD2 . LEU   B 71  ? 0.7781 0.6754 0.9396 -0.0800 0.1090  0.0119  88  LEU   B CD2 
1536 N N   . LYS   B 72  ? 1.0350 0.8693 1.1810 -0.1044 0.1217  0.0051  89  LYS   B N   
1537 C CA  . LYS   B 72  ? 1.0720 0.8808 1.2080 -0.1093 0.1248  0.0040  89  LYS   B CA  
1538 C C   . LYS   B 72  ? 1.1680 0.9397 1.2791 -0.1050 0.1282  0.0133  89  LYS   B C   
1539 O O   . LYS   B 72  ? 1.1558 0.9033 1.2564 -0.1014 0.1281  0.0144  89  LYS   B O   
1540 C CB  . LYS   B 72  ? 0.9679 0.7814 1.1074 -0.1285 0.1321  -0.0038 89  LYS   B CB  
1541 N N   . ASP   B 73  ? 1.4487 1.2146 1.5488 -0.1045 0.1313  0.0201  90  ASP   B N   
1542 C CA  . ASP   B 73  ? 1.4410 1.1706 1.5153 -0.0997 0.1342  0.0294  90  ASP   B CA  
1543 C C   . ASP   B 73  ? 1.4399 1.1629 1.5114 -0.0796 0.1257  0.0350  90  ASP   B C   
1544 O O   . ASP   B 73  ? 1.4828 1.1747 1.5353 -0.0731 0.1267  0.0401  90  ASP   B O   
1545 C CB  . ASP   B 73  ? 1.4481 1.1747 1.5110 -0.1042 0.1394  0.0351  90  ASP   B CB  
1546 C CG  . ASP   B 73  ? 1.5832 1.3446 1.6634 -0.0998 0.1349  0.0336  90  ASP   B CG  
1547 O OD1 . ASP   B 73  ? 1.5384 1.3246 1.6384 -0.0931 0.1274  0.0286  90  ASP   B OD1 
1548 O OD2 . ASP   B 73  ? 1.7655 1.5277 1.8378 -0.1030 0.1388  0.0375  90  ASP   B OD2 
1549 N N   . GLN   B 74  ? 1.2612 1.0128 1.3506 -0.0696 0.1176  0.0338  91  GLN   B N   
1550 C CA  . GLN   B 74  ? 1.1500 0.9008 1.2390 -0.0518 0.1095  0.0387  91  GLN   B CA  
1551 C C   . GLN   B 74  ? 1.0853 0.8301 1.1782 -0.0461 0.1067  0.0353  91  GLN   B C   
1552 O O   . GLN   B 74  ? 1.1083 0.8500 1.1989 -0.0314 0.1011  0.0394  91  GLN   B O   
1553 C CB  . GLN   B 74  ? 1.0617 0.8442 1.1675 -0.0454 0.1020  0.0381  91  GLN   B CB  
1554 C CG  . GLN   B 74  ? 1.0502 0.8354 1.1485 -0.0456 0.1030  0.0434  91  GLN   B CG  
1555 C CD  . GLN   B 74  ? 0.9937 0.7583 1.0732 -0.0341 0.1010  0.0531  91  GLN   B CD  
1556 O OE1 . GLN   B 74  ? 1.0810 0.8283 1.1522 -0.0253 0.0993  0.0561  91  GLN   B OE1 
1557 N NE2 . GLN   B 74  ? 0.9116 0.6781 0.9834 -0.0334 0.1011  0.0579  91  GLN   B NE2 
1558 N N   . LEU   B 75  ? 1.1213 0.8659 1.2199 -0.0574 0.1104  0.0276  92  LEU   B N   
1559 C CA  . LEU   B 75  ? 1.0861 0.8229 1.1863 -0.0528 0.1085  0.0238  92  LEU   B CA  
1560 C C   . LEU   B 75  ? 1.2818 0.9817 1.3587 -0.0450 0.1109  0.0296  92  LEU   B C   
1561 O O   . LEU   B 75  ? 1.2515 0.9439 1.3277 -0.0366 0.1086  0.0278  92  LEU   B O   
1562 C CB  . LEU   B 75  ? 1.0263 0.7685 1.1348 -0.0682 0.1123  0.0143  92  LEU   B CB  
1563 C CG  . LEU   B 75  ? 0.9928 0.7718 1.1245 -0.0744 0.1093  0.0074  92  LEU   B CG  
1564 C CD1 . LEU   B 75  ? 0.9448 0.7285 1.0837 -0.0882 0.1124  -0.0023 92  LEU   B CD1 
1565 C CD2 . LEU   B 75  ? 0.8760 0.6775 1.0222 -0.0608 0.1003  0.0074  92  LEU   B CD2 
1566 N N   . SER   B 76  ? 1.6209 1.2965 1.6772 -0.0472 0.1160  0.0362  93  SER   B N   
1567 C CA  . SER   B 76  ? 1.6174 1.2544 1.6478 -0.0383 0.1182  0.0424  93  SER   B CA  
1568 C C   . SER   B 76  ? 1.5966 1.2378 1.6293 -0.0169 0.1104  0.0459  93  SER   B C   
1569 O O   . SER   B 76  ? 1.6396 1.2658 1.6666 -0.0098 0.1101  0.0439  93  SER   B O   
1570 C CB  . SER   B 76  ? 1.7020 1.3186 1.7115 -0.0406 0.1226  0.0506  93  SER   B CB  
1571 O OG  . SER   B 76  ? 1.6730 1.3112 1.6902 -0.0309 0.1168  0.0557  93  SER   B OG  
1572 N N   . LEU   B 77  ? 1.3182 0.9807 1.3592 -0.0065 0.1042  0.0507  94  LEU   B N   
1573 C CA  . LEU   B 77  ? 1.2897 0.9592 1.3330 0.0133  0.0969  0.0545  94  LEU   B CA  
1574 C C   . LEU   B 77  ? 1.1294 0.8363 1.1996 0.0162  0.0903  0.0492  94  LEU   B C   
1575 O O   . LEU   B 77  ? 1.1522 0.8775 1.2299 0.0288  0.0835  0.0526  94  LEU   B O   
1576 C CB  . LEU   B 77  ? 1.3681 1.0352 1.4006 0.0234  0.0937  0.0636  94  LEU   B CB  
1577 N N   . GLY   B 78  ? 1.0729 0.7916 1.1569 0.0045  0.0921  0.0409  95  GLY   B N   
1578 C CA  . GLY   B 78  ? 1.0086 0.7587 1.1150 0.0072  0.0861  0.0360  95  GLY   B CA  
1579 C C   . GLY   B 78  ? 0.8243 0.6040 0.9456 0.0047  0.0814  0.0364  95  GLY   B C   
1580 O O   . GLY   B 78  ? 0.7967 0.5984 0.9302 0.0127  0.0749  0.0366  95  GLY   B O   
1581 N N   . ASN   B 79  ? 0.7744 0.5550 0.8943 -0.0066 0.0848  0.0363  96  ASN   B N   
1582 C CA  . ASN   B 79  ? 0.8357 0.6418 0.9674 -0.0090 0.0808  0.0362  96  ASN   B CA  
1583 C C   . ASN   B 79  ? 0.8432 0.6633 0.9868 -0.0226 0.0834  0.0282  96  ASN   B C   
1584 O O   . ASN   B 79  ? 0.8984 0.7110 1.0365 -0.0334 0.0896  0.0272  96  ASN   B O   
1585 C CB  . ASN   B 79  ? 0.8713 0.6685 0.9897 -0.0078 0.0820  0.0434  96  ASN   B CB  
1586 C CG  . ASN   B 79  ? 0.9177 0.7392 1.0457 -0.0072 0.0768  0.0441  96  ASN   B CG  
1587 O OD1 . ASN   B 79  ? 0.9211 0.7649 1.0647 -0.0068 0.0718  0.0397  96  ASN   B OD1 
1588 N ND2 . ASN   B 79  ? 0.9428 0.7582 1.0595 -0.0073 0.0779  0.0496  96  ASN   B ND2 
1589 N N   . ALA   B 80  ? 0.7946 0.6359 0.9544 -0.0218 0.0787  0.0227  97  ALA   B N   
1590 C CA  . ALA   B 80  ? 0.8094 0.6684 0.9817 -0.0319 0.0792  0.0151  97  ALA   B CA  
1591 C C   . ALA   B 80  ? 0.8168 0.6941 0.9942 -0.0309 0.0755  0.0165  97  ALA   B C   
1592 O O   . ALA   B 80  ? 0.8002 0.6931 0.9856 -0.0249 0.0689  0.0162  97  ALA   B O   
1593 C CB  . ALA   B 80  ? 0.7725 0.6424 0.9565 -0.0306 0.0757  0.0087  97  ALA   B CB  
1594 N N   . ALA   B 81  ? 0.9415 0.8159 1.1130 -0.0374 0.0801  0.0180  98  ALA   B N   
1595 C CA  . ALA   B 81  ? 0.9565 0.8438 1.1288 -0.0359 0.0775  0.0200  98  ALA   B CA  
1596 C C   . ALA   B 81  ? 0.9280 0.8334 1.1105 -0.0440 0.0792  0.0127  98  ALA   B C   
1597 O O   . ALA   B 81  ? 0.9326 0.8352 1.1142 -0.0539 0.0862  0.0096  98  ALA   B O   
1598 C CB  . ALA   B 81  ? 0.9923 0.8637 1.1488 -0.0355 0.0813  0.0275  98  ALA   B CB  
1599 N N   . LEU   B 82  ? 0.7576 0.6814 0.9489 -0.0399 0.0730  0.0100  99  LEU   B N   
1600 C CA  . LEU   B 82  ? 0.7237 0.6661 0.9243 -0.0445 0.0734  0.0028  99  LEU   B CA  
1601 C C   . LEU   B 82  ? 0.7071 0.6557 0.9027 -0.0429 0.0733  0.0051  99  LEU   B C   
1602 O O   . LEU   B 82  ? 0.6759 0.6226 0.8662 -0.0358 0.0680  0.0099  99  LEU   B O   
1603 C CB  . LEU   B 82  ? 0.6464 0.6025 0.8575 -0.0402 0.0664  -0.0024 99  LEU   B CB  
1604 C CG  . LEU   B 82  ? 0.7052 0.6807 0.9238 -0.0403 0.0640  -0.0088 99  LEU   B CG  
1605 C CD1 . LEU   B 82  ? 0.7004 0.6851 0.9244 -0.0492 0.0707  -0.0148 99  LEU   B CD1 
1606 C CD2 . LEU   B 82  ? 0.5955 0.5794 0.8210 -0.0356 0.0570  -0.0131 99  LEU   B CD2 
1607 N N   . GLN   B 83  ? 0.7243 0.6811 0.9216 -0.0499 0.0791  0.0014  100 GLN   B N   
1608 C CA  . GLN   B 83  ? 0.7563 0.7197 0.9485 -0.0487 0.0802  0.0026  100 GLN   B CA  
1609 C C   . GLN   B 83  ? 0.7199 0.7058 0.9226 -0.0480 0.0784  -0.0055 100 GLN   B C   
1610 O O   . GLN   B 83  ? 0.7967 0.7940 1.0095 -0.0540 0.0814  -0.0122 100 GLN   B O   
1611 C CB  . GLN   B 83  ? 0.8015 0.7558 0.9847 -0.0569 0.0897  0.0056  100 GLN   B CB  
1612 C CG  . GLN   B 83  ? 0.8227 0.7781 0.9961 -0.0544 0.0910  0.0092  100 GLN   B CG  
1613 C CD  . GLN   B 83  ? 0.9035 0.8592 1.0723 -0.0645 0.1015  0.0087  100 GLN   B CD  
1614 O OE1 . GLN   B 83  ? 0.9060 0.8774 1.0851 -0.0721 0.1062  0.0017  100 GLN   B OE1 
1615 N NE2 . GLN   B 83  ? 0.9672 0.9063 1.1200 -0.0650 0.1052  0.0162  100 GLN   B NE2 
1616 N N   . ILE   B 84  ? 0.6876 0.6793 0.8871 -0.0405 0.0731  -0.0051 101 ILE   B N   
1617 C CA  . ILE   B 84  ? 0.6718 0.6823 0.8776 -0.0372 0.0708  -0.0123 101 ILE   B CA  
1618 C C   . ILE   B 84  ? 0.6808 0.6956 0.8791 -0.0366 0.0748  -0.0115 101 ILE   B C   
1619 O O   . ILE   B 84  ? 0.7015 0.7048 0.8877 -0.0330 0.0732  -0.0053 101 ILE   B O   
1620 C CB  . ILE   B 84  ? 0.7064 0.7178 0.9121 -0.0284 0.0610  -0.0134 101 ILE   B CB  
1621 C CG1 . ILE   B 84  ? 0.7123 0.7221 0.9259 -0.0290 0.0575  -0.0153 101 ILE   B CG1 
1622 C CG2 . ILE   B 84  ? 0.6398 0.6669 0.8479 -0.0231 0.0585  -0.0203 101 ILE   B CG2 
1623 C CD1 . ILE   B 84  ? 0.7015 0.7082 0.9126 -0.0221 0.0487  -0.0146 101 ILE   B CD1 
1624 N N   . THR   B 85  ? 0.7228 0.7552 0.9282 -0.0403 0.0804  -0.0179 102 THR   B N   
1625 C CA  . THR   B 85  ? 0.7306 0.7710 0.9300 -0.0388 0.0845  -0.0185 102 THR   B CA  
1626 C C   . THR   B 85  ? 0.6864 0.7396 0.8871 -0.0283 0.0781  -0.0243 102 THR   B C   
1627 O O   . THR   B 85  ? 0.7633 0.8273 0.9739 -0.0252 0.0737  -0.0302 102 THR   B O   
1628 C CB  . THR   B 85  ? 0.7381 0.7927 0.9442 -0.0490 0.0950  -0.0224 102 THR   B CB  
1629 O OG1 . THR   B 85  ? 0.7726 0.8513 0.9938 -0.0486 0.0942  -0.0319 102 THR   B OG1 
1630 C CG2 . THR   B 85  ? 0.6111 0.6507 0.8158 -0.0603 0.1008  -0.0181 102 THR   B CG2 
1631 N N   . ASP   B 86  ? 0.7166 0.7668 0.9055 -0.0222 0.0773  -0.0224 103 ASP   B N   
1632 C CA  . ASP   B 86  ? 0.7194 0.7757 0.9043 -0.0111 0.0709  -0.0270 103 ASP   B CA  
1633 C C   . ASP   B 86  ? 0.6989 0.7448 0.8827 -0.0057 0.0607  -0.0264 103 ASP   B C   
1634 O O   . ASP   B 86  ? 0.6917 0.7472 0.8828 -0.0014 0.0566  -0.0324 103 ASP   B O   
1635 C CB  . ASP   B 86  ? 0.7768 0.8591 0.9729 -0.0086 0.0742  -0.0364 103 ASP   B CB  
1636 C CG  . ASP   B 86  ? 0.8808 0.9744 1.0730 -0.0090 0.0823  -0.0379 103 ASP   B CG  
1637 O OD1 . ASP   B 86  ? 0.9423 1.0212 1.1202 -0.0089 0.0839  -0.0318 103 ASP   B OD1 
1638 O OD2 . ASP   B 86  ? 0.9476 1.0660 1.1510 -0.0093 0.0870  -0.0453 103 ASP   B OD2 
1639 N N   . VAL   B 87  ? 0.7067 0.7335 0.8810 -0.0064 0.0568  -0.0190 104 VAL   B N   
1640 C CA  . VAL   B 87  ? 0.6713 0.6885 0.8423 -0.0019 0.0475  -0.0180 104 VAL   B CA  
1641 C C   . VAL   B 87  ? 0.6598 0.6789 0.8226 0.0074  0.0421  -0.0230 104 VAL   B C   
1642 O O   . VAL   B 87  ? 0.5423 0.5583 0.6933 0.0113  0.0427  -0.0226 104 VAL   B O   
1643 C CB  . VAL   B 87  ? 0.6666 0.6665 0.8280 -0.0037 0.0442  -0.0096 104 VAL   B CB  
1644 C CG1 . VAL   B 87  ? 0.6491 0.6421 0.8101 -0.0018 0.0359  -0.0088 104 VAL   B CG1 
1645 C CG2 . VAL   B 87  ? 0.6954 0.6915 0.8613 -0.0110 0.0504  -0.0045 104 VAL   B CG2 
1646 N N   . LYS   B 88  ? 0.6850 0.7073 0.8520 0.0114  0.0368  -0.0276 105 LYS   B N   
1647 C CA  . LYS   B 88  ? 0.6707 0.6914 0.8276 0.0212  0.0311  -0.0324 105 LYS   B CA  
1648 C C   . LYS   B 88  ? 0.6881 0.6920 0.8356 0.0226  0.0224  -0.0299 105 LYS   B C   
1649 O O   . LYS   B 88  ? 0.7026 0.7012 0.8552 0.0165  0.0210  -0.0256 105 LYS   B O   
1650 C CB  . LYS   B 88  ? 0.7096 0.7494 0.8771 0.0263  0.0322  -0.0409 105 LYS   B CB  
1651 N N   . LEU   B 89  ? 0.6115 0.6064 0.7439 0.0307  0.0167  -0.0326 106 LEU   B N   
1652 C CA  . LEU   B 89  ? 0.6663 0.6436 0.7868 0.0311  0.0086  -0.0305 106 LEU   B CA  
1653 C C   . LEU   B 89  ? 0.6754 0.6566 0.8062 0.0296  0.0063  -0.0323 106 LEU   B C   
1654 O O   . LEU   B 89  ? 0.6996 0.6697 0.8267 0.0253  0.0020  -0.0287 106 LEU   B O   
1655 C CB  . LEU   B 89  ? 0.6363 0.6011 0.7363 0.0404  0.0035  -0.0340 106 LEU   B CB  
1656 C CG  . LEU   B 89  ? 0.6428 0.5956 0.7271 0.0400  0.0034  -0.0306 106 LEU   B CG  
1657 C CD1 . LEU   B 89  ? 0.6389 0.5913 0.7106 0.0511  0.0040  -0.0362 106 LEU   B CD1 
1658 C CD2 . LEU   B 89  ? 0.6568 0.5885 0.7256 0.0351  -0.0037 -0.0259 106 LEU   B CD2 
1659 N N   . GLN   B 90  ? 0.6149 0.6130 0.7587 0.0326  0.0092  -0.0381 107 GLN   B N   
1660 C CA  . GLN   B 90  ? 0.6657 0.6685 0.8193 0.0313  0.0071  -0.0404 107 GLN   B CA  
1661 C C   . GLN   B 90  ? 0.6206 0.6275 0.7887 0.0212  0.0112  -0.0362 107 GLN   B C   
1662 O O   . GLN   B 90  ? 0.5645 0.5719 0.7388 0.0191  0.0093  -0.0370 107 GLN   B O   
1663 C CB  . GLN   B 90  ? 0.7224 0.7436 0.8849 0.0382  0.0082  -0.0486 107 GLN   B CB  
1664 C CG  . GLN   B 90  ? 0.7470 0.7864 0.9182 0.0385  0.0155  -0.0514 107 GLN   B CG  
1665 C CD  . GLN   B 90  ? 0.7833 0.8460 0.9668 0.0436  0.0168  -0.0598 107 GLN   B CD  
1666 O OE1 . GLN   B 90  ? 0.8407 0.9050 1.0251 0.0484  0.0115  -0.0637 107 GLN   B OE1 
1667 N NE2 . GLN   B 90  ? 0.7576 0.8396 0.9506 0.0425  0.0238  -0.0628 107 GLN   B NE2 
1668 N N   . ASP   B 91  ? 0.6102 0.6186 0.7820 0.0156  0.0168  -0.0319 108 ASP   B N   
1669 C CA  . ASP   B 91  ? 0.6071 0.6156 0.7892 0.0073  0.0206  -0.0273 108 ASP   B CA  
1670 C C   . ASP   B 91  ? 0.6037 0.5980 0.7787 0.0045  0.0164  -0.0208 108 ASP   B C   
1671 O O   . ASP   B 91  ? 0.6111 0.6042 0.7925 -0.0007 0.0191  -0.0164 108 ASP   B O   
1672 C CB  . ASP   B 91  ? 0.5777 0.5916 0.7642 0.0029  0.0283  -0.0252 108 ASP   B CB  
1673 C CG  . ASP   B 91  ? 0.6139 0.6455 0.8113 0.0025  0.0339  -0.0317 108 ASP   B CG  
1674 O OD1 . ASP   B 91  ? 0.6557 0.6964 0.8622 0.0030  0.0326  -0.0370 108 ASP   B OD1 
1675 O OD2 . ASP   B 91  ? 0.6441 0.6816 0.8409 0.0012  0.0396  -0.0317 108 ASP   B OD2 
1676 N N   . ALA   B 92  ? 0.6250 0.6088 0.7863 0.0078  0.0100  -0.0202 109 ALA   B N   
1677 C CA  . ALA   B 92  ? 0.5173 0.4905 0.6722 0.0041  0.0057  -0.0146 109 ALA   B CA  
1678 C C   . ALA   B 92  ? 0.5322 0.5045 0.6908 0.0029  0.0026  -0.0159 109 ALA   B C   
1679 O O   . ALA   B 92  ? 0.6044 0.5771 0.7609 0.0071  0.0002  -0.0211 109 ALA   B O   
1680 C CB  . ALA   B 92  ? 0.4461 0.4069 0.5826 0.0062  0.0005  -0.0135 109 ALA   B CB  
1681 N N   . GLY   B 93  ? 0.4825 0.4543 0.6461 -0.0021 0.0027  -0.0113 110 GLY   B N   
1682 C CA  . GLY   B 93  ? 0.5199 0.4916 0.6871 -0.0038 0.0006  -0.0121 110 GLY   B CA  
1683 C C   . GLY   B 93  ? 0.5905 0.5671 0.7691 -0.0076 0.0039  -0.0081 110 GLY   B C   
1684 O O   . GLY   B 93  ? 0.4817 0.4591 0.6621 -0.0090 0.0063  -0.0036 110 GLY   B O   
1685 N N   . VAL   B 94  ? 0.5862 0.5652 0.7709 -0.0085 0.0040  -0.0099 111 VAL   B N   
1686 C CA  . VAL   B 94  ? 0.5638 0.5466 0.7580 -0.0108 0.0069  -0.0068 111 VAL   B CA  
1687 C C   . VAL   B 94  ? 0.5991 0.5862 0.8039 -0.0105 0.0124  -0.0100 111 VAL   B C   
1688 O O   . VAL   B 94  ? 0.6278 0.6176 0.8357 -0.0096 0.0124  -0.0156 111 VAL   B O   
1689 C CB  . VAL   B 94  ? 0.5493 0.5316 0.7424 -0.0125 0.0040  -0.0067 111 VAL   B CB  
1690 C CG1 . VAL   B 94  ? 0.5408 0.5280 0.7446 -0.0131 0.0079  -0.0055 111 VAL   B CG1 
1691 C CG2 . VAL   B 94  ? 0.5226 0.5016 0.7060 -0.0155 -0.0005 -0.0026 111 VAL   B CG2 
1692 N N   . TYR   B 95  ? 0.5432 0.5303 0.7524 -0.0114 0.0169  -0.0066 112 TYR   B N   
1693 C CA  . TYR   B 95  ? 0.5206 0.5089 0.7379 -0.0128 0.0227  -0.0089 112 TYR   B CA  
1694 C C   . TYR   B 95  ? 0.4963 0.4826 0.7184 -0.0130 0.0243  -0.0073 112 TYR   B C   
1695 O O   . TYR   B 95  ? 0.5216 0.5074 0.7420 -0.0116 0.0222  -0.0029 112 TYR   B O   
1696 C CB  . TYR   B 95  ? 0.5132 0.4989 0.7291 -0.0139 0.0272  -0.0059 112 TYR   B CB  
1697 C CG  . TYR   B 95  ? 0.5184 0.5076 0.7308 -0.0136 0.0273  -0.0086 112 TYR   B CG  
1698 C CD1 . TYR   B 95  ? 0.5735 0.5615 0.7770 -0.0110 0.0225  -0.0073 112 TYR   B CD1 
1699 C CD2 . TYR   B 95  ? 0.5380 0.5322 0.7554 -0.0161 0.0325  -0.0128 112 TYR   B CD2 
1700 C CE1 . TYR   B 95  ? 0.5942 0.5848 0.7933 -0.0093 0.0228  -0.0102 112 TYR   B CE1 
1701 C CE2 . TYR   B 95  ? 0.5595 0.5595 0.7742 -0.0150 0.0330  -0.0156 112 TYR   B CE2 
1702 C CZ  . TYR   B 95  ? 0.5745 0.5724 0.7799 -0.0107 0.0282  -0.0143 112 TYR   B CZ  
1703 O OH  . TYR   B 95  ? 0.5741 0.5772 0.7758 -0.0083 0.0289  -0.0174 112 TYR   B OH  
1704 N N   . ARG   B 96  ? 0.4749 0.4611 0.7030 -0.0147 0.0282  -0.0114 113 ARG   B N   
1705 C CA  . ARG   B 96  ? 0.4776 0.4604 0.7091 -0.0142 0.0302  -0.0110 113 ARG   B CA  
1706 C C   . ARG   B 96  ? 0.5000 0.4761 0.7336 -0.0169 0.0365  -0.0117 113 ARG   B C   
1707 O O   . ARG   B 96  ? 0.4075 0.3858 0.6441 -0.0209 0.0389  -0.0169 113 ARG   B O   
1708 C CB  . ARG   B 96  ? 0.4974 0.4838 0.7312 -0.0142 0.0277  -0.0163 113 ARG   B CB  
1709 C CG  . ARG   B 96  ? 0.5385 0.5270 0.7692 -0.0121 0.0234  -0.0136 113 ARG   B CG  
1710 C CD  . ARG   B 96  ? 0.5312 0.5215 0.7624 -0.0122 0.0215  -0.0186 113 ARG   B CD  
1711 N NE  . ARG   B 96  ? 0.5375 0.5295 0.7635 -0.0119 0.0173  -0.0163 113 ARG   B NE  
1712 C CZ  . ARG   B 96  ? 0.5626 0.5553 0.7873 -0.0119 0.0163  -0.0184 113 ARG   B CZ  
1713 N NH1 . ARG   B 96  ? 0.5187 0.5106 0.7470 -0.0115 0.0186  -0.0229 113 ARG   B NH1 
1714 N NH2 . ARG   B 96  ? 0.5862 0.5800 0.8049 -0.0131 0.0130  -0.0159 113 ARG   B NH2 
1715 N N   . CYS   B 97  ? 0.6143 0.5822 0.8456 -0.0146 0.0391  -0.0067 114 CYS   B N   
1716 C CA  . CYS   B 97  ? 0.6558 0.6123 0.8855 -0.0168 0.0452  -0.0067 114 CYS   B CA  
1717 C C   . CYS   B 97  ? 0.6430 0.5945 0.8741 -0.0148 0.0464  -0.0089 114 CYS   B C   
1718 O O   . CYS   B 97  ? 0.5944 0.5461 0.8246 -0.0089 0.0446  -0.0053 114 CYS   B O   
1719 C CB  . CYS   B 97  ? 0.7104 0.6578 0.9331 -0.0141 0.0474  0.0005  114 CYS   B CB  
1720 S SG  . CYS   B 97  ? 0.9635 0.8907 1.1796 -0.0139 0.0541  0.0023  114 CYS   B SG  
1721 N N   . MET   B 98  ? 0.6561 0.6041 0.8891 -0.0199 0.0494  -0.0149 115 MET   B N   
1722 C CA  . MET   B 98  ? 0.6300 0.5718 0.8629 -0.0186 0.0507  -0.0181 115 MET   B CA  
1723 C C   . MET   B 98  ? 0.6294 0.5541 0.8567 -0.0225 0.0569  -0.0188 115 MET   B C   
1724 O O   . MET   B 98  ? 0.6799 0.6037 0.9079 -0.0307 0.0598  -0.0226 115 MET   B O   
1725 C CB  . MET   B 98  ? 0.6131 0.5649 0.8515 -0.0215 0.0477  -0.0255 115 MET   B CB  
1726 C CG  . MET   B 98  ? 0.6668 0.6328 0.9082 -0.0201 0.0420  -0.0256 115 MET   B CG  
1727 S SD  . MET   B 98  ? 0.6146 0.5898 0.8593 -0.0212 0.0378  -0.0336 115 MET   B SD  
1728 C CE  . MET   B 98  ? 0.6583 0.6451 0.9035 -0.0209 0.0329  -0.0343 115 MET   B CE  
1729 N N   . ILE   B 99  ? 0.7077 0.6188 0.9286 -0.0166 0.0592  -0.0154 116 ILE   B N   
1730 C CA  . ILE   B 99  ? 0.6357 0.5250 0.8469 -0.0191 0.0651  -0.0152 116 ILE   B CA  
1731 C C   . ILE   B 99  ? 0.5982 0.4775 0.8060 -0.0153 0.0664  -0.0185 116 ILE   B C   
1732 O O   . ILE   B 99  ? 0.6456 0.5309 0.8553 -0.0063 0.0637  -0.0167 116 ILE   B O   
1733 C CB  . ILE   B 99  ? 0.6141 0.4912 0.8162 -0.0136 0.0671  -0.0069 116 ILE   B CB  
1734 C CG1 . ILE   B 99  ? 0.6400 0.5276 0.8447 -0.0168 0.0656  -0.0036 116 ILE   B CG1 
1735 C CG2 . ILE   B 99  ? 0.6922 0.5427 0.8810 -0.0168 0.0735  -0.0065 116 ILE   B CG2 
1736 C CD1 . ILE   B 99  ? 0.6995 0.5754 0.8942 -0.0117 0.0671  0.0045  116 ILE   B CD1 
1737 N N   . SER   B 100 ? 0.6373 0.5018 0.8396 -0.0226 0.0706  -0.0236 117 SER   B N   
1738 C CA  . SER   B 100 ? 0.7346 0.5842 0.9299 -0.0194 0.0727  -0.0269 117 SER   B CA  
1739 C C   . SER   B 100 ? 0.7430 0.5635 0.9230 -0.0225 0.0788  -0.0256 117 SER   B C   
1740 O O   . SER   B 100 ? 0.7587 0.5720 0.9361 -0.0350 0.0821  -0.0297 117 SER   B O   
1741 C CB  . SER   B 100 ? 0.6927 0.5509 0.8941 -0.0262 0.0710  -0.0359 117 SER   B CB  
1742 O OG  . SER   B 100 ? 0.6597 0.5064 0.8549 -0.0209 0.0721  -0.0389 117 SER   B OG  
1743 N N   . TYR   B 101 ? 0.7131 0.5179 0.8826 -0.0111 0.0803  -0.0197 118 TYR   B N   
1744 C CA  . TYR   B 101 ? 0.8563 0.6288 1.0072 -0.0116 0.0859  -0.0176 118 TYR   B CA  
1745 C C   . TYR   B 101 ? 0.8156 0.5743 0.9570 0.0037  0.0863  -0.0152 118 TYR   B C   
1746 O O   . TYR   B 101 ? 0.8246 0.5812 0.9616 0.0156  0.0853  -0.0080 118 TYR   B O   
1747 C CB  . TYR   B 101 ? 0.8499 0.6155 0.9946 -0.0126 0.0877  -0.0103 118 TYR   B CB  
1748 C CG  . TYR   B 101 ? 0.8186 0.5482 0.9418 -0.0149 0.0938  -0.0083 118 TYR   B CG  
1749 C CD1 . TYR   B 101 ? 0.9353 0.6473 1.0506 -0.0284 0.0984  -0.0148 118 TYR   B CD1 
1750 C CD2 . TYR   B 101 ? 0.7946 0.5064 0.9037 -0.0038 0.0948  0.0000  118 TYR   B CD2 
1751 C CE1 . TYR   B 101 ? 0.9065 0.5819 0.9993 -0.0318 0.1044  -0.0129 118 TYR   B CE1 
1752 C CE2 . TYR   B 101 ? 0.9612 0.6359 1.0471 -0.0056 0.1006  0.0022  118 TYR   B CE2 
1753 C CZ  . TYR   B 101 ? 0.9802 0.6358 1.0575 -0.0201 0.1056  -0.0043 118 TYR   B CZ  
1754 O OH  . TYR   B 101 ? 1.1516 0.7672 1.2035 -0.0233 0.1116  -0.0022 118 TYR   B OH  
1755 N N   . GLY   B 102 ? 0.7560 0.5058 0.8935 0.0042  0.0875  -0.0214 119 GLY   B N   
1756 C CA  . GLY   B 102 ? 0.7600 0.4998 0.8893 0.0201  0.0879  -0.0199 119 GLY   B CA  
1757 C C   . GLY   B 102 ? 0.8276 0.5991 0.9731 0.0301  0.0828  -0.0179 119 GLY   B C   
1758 O O   . GLY   B 102 ? 0.8882 0.6637 1.0325 0.0441  0.0816  -0.0120 119 GLY   B O   
1759 N N   . GLY   B 103 ? 0.8555 0.6499 1.0155 0.0225  0.0797  -0.0229 120 GLY   B N   
1760 C CA  . GLY   B 103 ? 0.8435 0.6676 1.0181 0.0280  0.0750  -0.0217 120 GLY   B CA  
1761 C C   . GLY   B 103 ? 0.8849 0.7295 1.0723 0.0172  0.0713  -0.0225 120 GLY   B C   
1762 O O   . GLY   B 103 ? 0.8969 0.7357 1.0835 0.0056  0.0725  -0.0253 120 GLY   B O   
1763 N N   . ALA   B 104 ? 0.7522 0.6214 0.9509 0.0207  0.0669  -0.0201 121 ALA   B N   
1764 C CA  . ALA   B 104 ? 0.7007 0.5879 0.9094 0.0121  0.0630  -0.0207 121 ALA   B CA  
1765 C C   . ALA   B 104 ? 0.7295 0.6366 0.9455 0.0178  0.0588  -0.0150 121 ALA   B C   
1766 O O   . ALA   B 104 ? 0.6819 0.5980 0.9001 0.0257  0.0580  -0.0136 121 ALA   B O   
1767 C CB  . ALA   B 104 ? 0.6765 0.5716 0.8902 0.0053  0.0612  -0.0284 121 ALA   B CB  
1768 N N   . ASP   B 105 ? 0.6884 0.6028 0.9078 0.0132  0.0564  -0.0119 122 ASP   B N   
1769 C CA  . ASP   B 105 ? 0.6686 0.6014 0.8940 0.0160  0.0519  -0.0072 122 ASP   B CA  
1770 C C   . ASP   B 105 ? 0.6515 0.5902 0.8798 0.0081  0.0494  -0.0071 122 ASP   B C   
1771 O O   . ASP   B 105 ? 0.6737 0.6032 0.8996 0.0018  0.0517  -0.0095 122 ASP   B O   
1772 C CB  . ASP   B 105 ? 0.6390 0.5706 0.8611 0.0256  0.0522  -0.0001 122 ASP   B CB  
1773 C CG  . ASP   B 105 ? 0.6316 0.5848 0.8606 0.0289  0.0475  0.0037  122 ASP   B CG  
1774 O OD1 . ASP   B 105 ? 0.6797 0.6461 0.9143 0.0254  0.0451  0.0007  122 ASP   B OD1 
1775 O OD2 . ASP   B 105 ? 0.5656 0.5221 0.7933 0.0345  0.0460  0.0096  122 ASP   B OD2 
1776 N N   . TYR   B 106 ? 0.5955 0.5498 0.8281 0.0082  0.0447  -0.0046 123 TYR   B N   
1777 C CA  . TYR   B 106 ? 0.5599 0.5195 0.7937 0.0024  0.0419  -0.0043 123 TYR   B CA  
1778 C C   . TYR   B 106 ? 0.5282 0.4991 0.7627 0.0051  0.0376  0.0012  123 TYR   B C   
1779 O O   . TYR   B 106 ? 0.4846 0.4645 0.7212 0.0091  0.0359  0.0032  123 TYR   B O   
1780 C CB  . TYR   B 106 ? 0.5870 0.5523 0.8238 -0.0033 0.0397  -0.0108 123 TYR   B CB  
1781 C CG  . TYR   B 106 ? 0.5318 0.5092 0.7702 -0.0030 0.0349  -0.0109 123 TYR   B CG  
1782 C CD1 . TYR   B 106 ? 0.5019 0.4859 0.7390 -0.0050 0.0307  -0.0087 123 TYR   B CD1 
1783 C CD2 . TYR   B 106 ? 0.5599 0.5405 0.7992 -0.0013 0.0348  -0.0132 123 TYR   B CD2 
1784 C CE1 . TYR   B 106 ? 0.4518 0.4436 0.6877 -0.0059 0.0265  -0.0087 123 TYR   B CE1 
1785 C CE2 . TYR   B 106 ? 0.6225 0.6125 0.8613 -0.0023 0.0310  -0.0130 123 TYR   B CE2 
1786 C CZ  . TYR   B 106 ? 0.4807 0.4754 0.7173 -0.0050 0.0268  -0.0107 123 TYR   B CZ  
1787 O OH  . TYR   B 106 ? 0.5007 0.5016 0.7343 -0.0072 0.0232  -0.0104 123 TYR   B OH  
1788 N N   . LYS   B 107 ? 0.4165 0.3876 0.6488 0.0022  0.0361  0.0035  124 LYS   B N   
1789 C CA  . LYS   B 107 ? 0.4781 0.4586 0.7096 0.0032  0.0316  0.0082  124 LYS   B CA  
1790 C C   . LYS   B 107 ? 0.4890 0.4710 0.7184 -0.0021 0.0290  0.0065  124 LYS   B C   
1791 O O   . LYS   B 107 ? 0.4465 0.4227 0.6752 -0.0053 0.0315  0.0034  124 LYS   B O   
1792 C CB  . LYS   B 107 ? 0.4859 0.4629 0.7138 0.0086  0.0324  0.0146  124 LYS   B CB  
1793 C CG  . LYS   B 107 ? 0.4536 0.4284 0.6821 0.0164  0.0347  0.0166  124 LYS   B CG  
1794 C CD  . LYS   B 107 ? 0.4561 0.4478 0.6886 0.0206  0.0307  0.0199  124 LYS   B CD  
1795 C CE  . LYS   B 107 ? 0.4291 0.4230 0.6643 0.0283  0.0332  0.0195  124 LYS   B CE  
1796 N NZ  . LYS   B 107 ? 0.4216 0.4209 0.6614 0.0249  0.0339  0.0141  124 LYS   B NZ  
1797 N N   . ARG   B 108 ? 0.5752 0.5655 0.8030 -0.0033 0.0239  0.0083  125 ARG   B N   
1798 C CA  . ARG   B 108 ? 0.5268 0.5173 0.7503 -0.0071 0.0209  0.0065  125 ARG   B CA  
1799 C C   . ARG   B 108 ? 0.5188 0.5087 0.7371 -0.0066 0.0191  0.0113  125 ARG   B C   
1800 O O   . ARG   B 108 ? 0.5795 0.5733 0.7974 -0.0042 0.0176  0.0163  125 ARG   B O   
1801 C CB  . ARG   B 108 ? 0.5660 0.5616 0.7874 -0.0096 0.0162  0.0045  125 ARG   B CB  
1802 C CG  . ARG   B 108 ? 0.6129 0.6118 0.8386 -0.0091 0.0173  0.0021  125 ARG   B CG  
1803 C CD  . ARG   B 108 ? 0.6859 0.6903 0.9077 -0.0121 0.0130  0.0027  125 ARG   B CD  
1804 N NE  . ARG   B 108 ? 0.7650 0.7735 0.9830 -0.0138 0.0095  0.0075  125 ARG   B NE  
1805 C CZ  . ARG   B 108 ? 0.8048 0.8164 1.0169 -0.0185 0.0054  0.0084  125 ARG   B CZ  
1806 N NH1 . ARG   B 108 ? 0.8087 0.8187 1.0170 -0.0216 0.0043  0.0055  125 ARG   B NH1 
1807 N NH2 . ARG   B 108 ? 0.7410 0.7564 0.9495 -0.0207 0.0022  0.0124  125 ARG   B NH2 
1808 N N   . ILE   B 109 ? 0.4098 0.3958 0.6239 -0.0085 0.0193  0.0096  126 ILE   B N   
1809 C CA  . ILE   B 109 ? 0.4371 0.4214 0.6445 -0.0083 0.0179  0.0135  126 ILE   B CA  
1810 C C   . ILE   B 109 ? 0.4670 0.4512 0.6681 -0.0105 0.0142  0.0105  126 ILE   B C   
1811 O O   . ILE   B 109 ? 0.4987 0.4824 0.7010 -0.0111 0.0150  0.0051  126 ILE   B O   
1812 C CB  . ILE   B 109 ? 0.4570 0.4343 0.6634 -0.0076 0.0234  0.0150  126 ILE   B CB  
1813 C CG1 . ILE   B 109 ? 0.5583 0.5318 0.7666 -0.0040 0.0263  0.0191  126 ILE   B CG1 
1814 C CG2 . ILE   B 109 ? 0.4798 0.4548 0.6778 -0.0077 0.0222  0.0179  126 ILE   B CG2 
1815 C CD1 . ILE   B 109 ? 0.5108 0.4753 0.7209 -0.0051 0.0330  0.0169  126 ILE   B CD1 
1816 N N   . THR   B 110 ? 0.4395 0.4236 0.6328 -0.0111 0.0098  0.0136  127 THR   B N   
1817 C CA  . THR   B 110 ? 0.4886 0.4694 0.6725 -0.0125 0.0058  0.0111  127 THR   B CA  
1818 C C   . THR   B 110 ? 0.4909 0.4677 0.6680 -0.0113 0.0071  0.0124  127 THR   B C   
1819 O O   . THR   B 110 ? 0.4826 0.4591 0.6576 -0.0108 0.0073  0.0174  127 THR   B O   
1820 C CB  . THR   B 110 ? 0.4773 0.4593 0.6549 -0.0156 -0.0003 0.0131  127 THR   B CB  
1821 O OG1 . THR   B 110 ? 0.5235 0.5075 0.7043 -0.0173 -0.0012 0.0105  127 THR   B OG1 
1822 C CG2 . THR   B 110 ? 0.4231 0.3973 0.5867 -0.0169 -0.0044 0.0118  127 THR   B CG2 
1823 N N   . VAL   B 111 ? 0.4320 0.4063 0.6053 -0.0102 0.0080  0.0078  128 VAL   B N   
1824 C CA  . VAL   B 111 ? 0.4537 0.4251 0.6202 -0.0088 0.0099  0.0080  128 VAL   B CA  
1825 C C   . VAL   B 111 ? 0.4773 0.4431 0.6305 -0.0079 0.0046  0.0059  128 VAL   B C   
1826 O O   . VAL   B 111 ? 0.4345 0.3986 0.5853 -0.0065 0.0022  0.0012  128 VAL   B O   
1827 C CB  . VAL   B 111 ? 0.4955 0.4706 0.6688 -0.0080 0.0164  0.0039  128 VAL   B CB  
1828 C CG1 . VAL   B 111 ? 0.4340 0.4080 0.5994 -0.0063 0.0184  0.0030  128 VAL   B CG1 
1829 C CG2 . VAL   B 111 ? 0.4880 0.4641 0.6703 -0.0099 0.0219  0.0066  128 VAL   B CG2 
1830 N N   . LYS   B 112 ? 0.4433 0.4045 0.5861 -0.0082 0.0025  0.0094  129 LYS   B N   
1831 C CA  . LYS   B 112 ? 0.4537 0.4065 0.5809 -0.0071 -0.0020 0.0074  129 LYS   B CA  
1832 C C   . LYS   B 112 ? 0.5511 0.5028 0.6729 -0.0036 0.0020  0.0060  129 LYS   B C   
1833 O O   . LYS   B 112 ? 0.5788 0.5331 0.7035 -0.0041 0.0062  0.0096  129 LYS   B O   
1834 C CB  . LYS   B 112 ? 0.4988 0.4471 0.6162 -0.0112 -0.0081 0.0117  129 LYS   B CB  
1835 C CG  . LYS   B 112 ? 0.4930 0.4446 0.6154 -0.0157 -0.0117 0.0131  129 LYS   B CG  
1836 C CD  . LYS   B 112 ? 0.4581 0.4026 0.5738 -0.0162 -0.0148 0.0084  129 LYS   B CD  
1837 C CE  . LYS   B 112 ? 0.4599 0.4040 0.5726 -0.0230 -0.0197 0.0104  129 LYS   B CE  
1838 N NZ  . LYS   B 112 ? 0.4588 0.4055 0.5790 -0.0235 -0.0187 0.0080  129 LYS   B NZ  
1839 N N   . VAL   B 113 ? 0.5498 0.4973 0.6627 0.0006  0.0009  0.0008  130 VAL   B N   
1840 C CA  . VAL   B 113 ? 0.5803 0.5295 0.6892 0.0049  0.0055  -0.0018 130 VAL   B CA  
1841 C C   . VAL   B 113 ? 0.5838 0.5207 0.6725 0.0076  0.0008  -0.0027 130 VAL   B C   
1842 O O   . VAL   B 113 ? 0.5971 0.5260 0.6758 0.0109  -0.0037 -0.0068 130 VAL   B O   
1843 C CB  . VAL   B 113 ? 0.5819 0.5406 0.6999 0.0092  0.0094  -0.0083 130 VAL   B CB  
1844 C CG1 . VAL   B 113 ? 0.6281 0.5924 0.7436 0.0131  0.0150  -0.0110 130 VAL   B CG1 
1845 C CG2 . VAL   B 113 ? 0.4928 0.4616 0.6292 0.0054  0.0133  -0.0079 130 VAL   B CG2 
1846 N N   . ASN   B 114 ? 0.6121 0.5456 0.6926 0.0065  0.0016  0.0011  131 ASN   B N   
1847 C CA  . ASN   B 114 ? 0.5596 0.4814 0.6199 0.0097  -0.0015 -0.0005 131 ASN   B CA  
1848 C C   . ASN   B 114 ? 0.5998 0.5264 0.6585 0.0168  0.0043  -0.0055 131 ASN   B C   
1849 O O   . ASN   B 114 ? 0.6751 0.6147 0.7472 0.0168  0.0117  -0.0057 131 ASN   B O   
1850 C CB  . ASN   B 114 ? 0.5927 0.5096 0.6444 0.0056  -0.0034 0.0054  131 ASN   B CB  
1851 C CG  . ASN   B 114 ? 0.5804 0.4964 0.6345 -0.0011 -0.0094 0.0100  131 ASN   B CG  
1852 O OD1 . ASN   B 114 ? 0.5155 0.4279 0.5689 -0.0034 -0.0141 0.0083  131 ASN   B OD1 
1853 N ND2 . ASN   B 114 ? 0.5744 0.4942 0.6309 -0.0041 -0.0093 0.0159  131 ASN   B ND2 
1854 N N   . ALA   B 115 ? 0.6115 0.5276 0.6528 0.0228  0.0012  -0.0099 132 ALA   B N   
1855 C CA  . ALA   B 115 ? 0.6192 0.5417 0.6585 0.0314  0.0063  -0.0156 132 ALA   B CA  
1856 C C   . ALA   B 115 ? 0.6690 0.5748 0.6833 0.0371  0.0025  -0.0180 132 ALA   B C   
1857 O O   . ALA   B 115 ? 0.6122 0.5003 0.6111 0.0351  -0.0052 -0.0173 132 ALA   B O   
1858 C CB  . ALA   B 115 ? 0.6255 0.5574 0.6756 0.0368  0.0069  -0.0217 132 ALA   B CB  
1859 N N   . PRO   B 116 ? 0.7231 0.6336 0.7318 0.0437  0.0078  -0.0212 133 PRO   B N   
1860 C CA  . PRO   B 116 ? 0.6556 0.5492 0.6389 0.0510  0.0044  -0.0245 133 PRO   B CA  
1861 C C   . PRO   B 116 ? 0.6424 0.5279 0.6168 0.0604  0.0001  -0.0312 133 PRO   B C   
1862 O O   . PRO   B 116 ? 0.6424 0.5378 0.6312 0.0618  0.0000  -0.0334 133 PRO   B O   
1863 C CB  . PRO   B 116 ? 0.6326 0.5382 0.6161 0.0559  0.0131  -0.0263 133 PRO   B CB  
1864 C CG  . PRO   B 116 ? 0.6894 0.6140 0.6958 0.0480  0.0203  -0.0220 133 PRO   B CG  
1865 C CD  . PRO   B 116 ? 0.6203 0.5508 0.6441 0.0438  0.0177  -0.0214 133 PRO   B CD  
1866 N N   . TYR   B 117 ? 0.7118 0.5774 0.6601 0.0674  -0.0039 -0.0344 134 TYR   B N   
1867 C CA  . TYR   B 117 ? 0.7010 0.5528 0.6349 0.0774  -0.0091 -0.0403 134 TYR   B CA  
1868 C C   . TYR   B 117 ? 0.7092 0.5822 0.6569 0.0894  -0.0038 -0.0468 134 TYR   B C   
1869 O O   . TYR   B 117 ? 0.7440 0.6167 0.6943 0.0947  -0.0072 -0.0501 134 TYR   B O   
1870 C CB  . TYR   B 117 ? 0.6920 0.5164 0.5927 0.0833  -0.0136 -0.0428 134 TYR   B CB  
1871 C CG  . TYR   B 117 ? 0.7853 0.5910 0.6669 0.0950  -0.0190 -0.0488 134 TYR   B CG  
1872 C CD1 . TYR   B 117 ? 0.7938 0.5920 0.6775 0.0920  -0.0243 -0.0483 134 TYR   B CD1 
1873 C CD2 . TYR   B 117 ? 0.7784 0.5728 0.6381 0.1098  -0.0187 -0.0551 134 TYR   B CD2 
1874 C CE1 . TYR   B 117 ? 0.7955 0.5741 0.6593 0.1032  -0.0294 -0.0534 134 TYR   B CE1 
1875 C CE2 . TYR   B 117 ? 0.8161 0.5911 0.6559 0.1221  -0.0239 -0.0605 134 TYR   B CE2 
1876 C CZ  . TYR   B 117 ? 0.7901 0.5564 0.6315 0.1186  -0.0294 -0.0595 134 TYR   B CZ  
1877 O OH  . TYR   B 117 ? 0.8416 0.5859 0.6607 0.1313  -0.0348 -0.0645 134 TYR   B OH  
1878 N N   . ALA   B 118 ? 0.6688 0.5613 0.6249 0.0937  0.0044  -0.0488 135 ALA   B N   
1879 C CA  . ALA   B 118 ? 0.6726 0.5887 0.6417 0.1052  0.0096  -0.0558 135 ALA   B CA  
1880 C C   . ALA   B 118 ? 0.6632 0.5989 0.6587 0.1004  0.0105  -0.0557 135 ALA   B C   
1881 O O   . ALA   B 118 ? 0.6664 0.6073 0.6644 0.1098  0.0078  -0.0612 135 ALA   B O   
1882 C CB  . ALA   B 118 ? 0.6233 0.5597 0.5995 0.1067  0.0195  -0.0570 135 ALA   B CB  
1883 N N   . ALA   B 119 ? 0.6342 0.5798 0.6481 0.0866  0.0140  -0.0497 136 ALA   B N   
1884 C CA  . ALA   B 119 ? 0.5868 0.5492 0.6246 0.0812  0.0150  -0.0496 136 ALA   B CA  
1885 C C   . ALA   B 119 ? 0.6450 0.5905 0.6763 0.0811  0.0061  -0.0491 136 ALA   B C   
1886 O O   . ALA   B 119 ? 0.6018 0.5585 0.6456 0.0838  0.0050  -0.0525 136 ALA   B O   
1887 C CB  . ALA   B 119 ? 0.5998 0.5714 0.6544 0.0670  0.0204  -0.0429 136 ALA   B CB  
1888 N N   . ALA   B 120 ? 0.6736 0.5925 0.6849 0.0773  -0.0003 -0.0451 137 ALA   B N   
1889 C CA  . ALA   B 120 ? 0.6694 0.5712 0.6733 0.0750  -0.0081 -0.0440 137 ALA   B CA  
1890 C C   . ALA   B 120 ? 0.7268 0.6173 0.7140 0.0890  -0.0130 -0.0506 137 ALA   B C   
1891 O O   . ALA   B 120 ? 0.7158 0.6067 0.7074 0.0911  -0.0164 -0.0525 137 ALA   B O   
1892 C CB  . ALA   B 120 ? 0.6722 0.5509 0.6598 0.0651  -0.0132 -0.0380 137 ALA   B CB  
1893 N N   . LEU   B 121 ? 0.7452 0.6242 0.7116 0.0996  -0.0136 -0.0544 138 LEU   B N   
1894 C CA  . LEU   B 121 ? 0.7627 0.6306 0.7117 0.1156  -0.0180 -0.0611 138 LEU   B CA  
1895 C C   . LEU   B 121 ? 0.7341 0.6318 0.7048 0.1249  -0.0145 -0.0669 138 LEU   B C   
1896 O O   . LEU   B 121 ? 0.7847 0.6777 0.7500 0.1341  -0.0194 -0.0707 138 LEU   B O   
1897 C CB  . LEU   B 121 ? 0.7108 0.5636 0.6347 0.1263  -0.0180 -0.0645 138 LEU   B CB  
1898 C CG  . LEU   B 121 ? 0.7705 0.6116 0.6739 0.1462  -0.0220 -0.0721 138 LEU   B CG  
1899 C CD1 . LEU   B 121 ? 0.8745 0.6892 0.7614 0.1468  -0.0306 -0.0716 138 LEU   B CD1 
1900 C CD2 . LEU   B 121 ? 0.7976 0.6195 0.6733 0.1556  -0.0221 -0.0748 138 LEU   B CD2 
1901 N N   . GLU   B 122 ? 0.6297 0.5582 0.6241 0.1222  -0.0061 -0.0676 139 GLU   B N   
1902 C CA  . GLU   B 122 ? 0.6105 0.5709 0.6279 0.1285  -0.0024 -0.0733 139 GLU   B CA  
1903 C C   . GLU   B 122 ? 0.6890 0.6544 0.7223 0.1203  -0.0051 -0.0713 139 GLU   B C   
1904 O O   . GLU   B 122 ? 0.6343 0.6120 0.6747 0.1287  -0.0074 -0.0766 139 GLU   B O   
1905 C CB  . GLU   B 122 ? 0.6620 0.6522 0.6999 0.1239  0.0079  -0.0738 139 GLU   B CB  
1906 C CG  . GLU   B 122 ? 0.7198 0.7462 0.7816 0.1290  0.0125  -0.0804 139 GLU   B CG  
1907 C CD  . GLU   B 122 ? 0.7751 0.8282 0.8512 0.1257  0.0231  -0.0817 139 GLU   B CD  
1908 O OE1 . GLU   B 122 ? 0.7211 0.7752 0.7847 0.1362  0.0256  -0.0852 139 GLU   B OE1 
1909 O OE2 . GLU   B 122 ? 0.8135 0.8852 0.9119 0.1124  0.0291  -0.0793 139 GLU   B OE2 
1910 N N   . HIS   B 123 ? 0.7647 0.7218 0.8038 0.1045  -0.0050 -0.0639 140 HIS   B N   
1911 C CA  . HIS   B 123 ? 0.6934 0.6519 0.7448 0.0967  -0.0077 -0.0616 140 HIS   B CA  
1912 C C   . HIS   B 123 ? 0.8524 0.7844 0.8826 0.1017  -0.0167 -0.0619 140 HIS   B C   
1913 O O   . HIS   B 123 ? 0.8590 0.7947 0.8963 0.1019  -0.0195 -0.0633 140 HIS   B O   
1914 C CB  . HIS   B 123 ? 0.6643 0.6216 0.7265 0.0800  -0.0048 -0.0538 140 HIS   B CB  
1915 C CG  . HIS   B 123 ? 0.7630 0.7170 0.8335 0.0720  -0.0080 -0.0509 140 HIS   B CG  
1916 N ND1 . HIS   B 123 ? 0.7377 0.7129 0.8312 0.0685  -0.0047 -0.0525 140 HIS   B ND1 
1917 C CD2 . HIS   B 123 ? 0.7527 0.6851 0.8110 0.0664  -0.0138 -0.0467 140 HIS   B CD2 
1918 C CE1 . HIS   B 123 ? 0.7367 0.7029 0.8314 0.0621  -0.0084 -0.0495 140 HIS   B CE1 
1919 N NE2 . HIS   B 123 ? 0.6873 0.6286 0.7615 0.0606  -0.0137 -0.0458 140 HIS   B NE2 
1920 N N   . HIS   B 124 ? 0.8958 0.7995 0.8981 0.1051  -0.0211 -0.0608 141 HIS   B N   
1921 C CA  . HIS   B 124 ? 0.9226 0.7971 0.9011 0.1085  -0.0294 -0.0607 141 HIS   B CA  
1922 C C   . HIS   B 124 ? 0.9550 0.8321 0.9274 0.1257  -0.0327 -0.0680 141 HIS   B C   
1923 O O   . HIS   B 124 ? 0.9709 0.8308 0.9307 0.1280  -0.0388 -0.0682 141 HIS   B O   
1924 C CB  . HIS   B 124 ? 0.9557 0.7983 0.9040 0.1076  -0.0331 -0.0584 141 HIS   B CB  
1925 C CG  . HIS   B 124 ? 1.0026 0.8113 0.9234 0.1081  -0.0411 -0.0577 141 HIS   B CG  
1926 N ND1 . HIS   B 124 ? 0.9793 0.7822 0.9041 0.0972  -0.0438 -0.0537 141 HIS   B ND1 
1927 C CD2 . HIS   B 124 ? 1.0157 0.7930 0.9029 0.1177  -0.0465 -0.0604 141 HIS   B CD2 
1928 C CE1 . HIS   B 124 ? 1.0223 0.7921 0.9173 0.0991  -0.0504 -0.0538 141 HIS   B CE1 
1929 N NE2 . HIS   B 124 ? 1.0082 0.7605 0.8792 0.1115  -0.0524 -0.0577 141 HIS   B NE2 
1930 N N   . HIS   B 125 ? 0.9524 0.8515 0.9328 0.1381  -0.0289 -0.0741 142 HIS   B N   
1931 C CA  . HIS   B 125 ? 0.9707 0.8827 0.9527 0.1548  -0.0313 -0.0816 142 HIS   B CA  
1932 C C   . HIS   B 125 ? 1.0589 1.0108 1.0762 0.1502  -0.0260 -0.0838 142 HIS   B C   
1933 O O   . HIS   B 125 ? 1.0236 0.9916 1.0615 0.1362  -0.0195 -0.0801 142 HIS   B O   
1934 C CB  . HIS   B 125 ? 0.9926 0.9055 0.9599 0.1730  -0.0308 -0.0879 142 HIS   B CB  
1935 C CG  . HIS   B 125 ? 1.1073 0.9804 1.0388 0.1768  -0.0351 -0.0860 142 HIS   B CG  
1936 N ND1 . HIS   B 125 ? 1.1197 0.9552 1.0265 0.1718  -0.0422 -0.0820 142 HIS   B ND1 
1937 C CD2 . HIS   B 125 ? 1.0840 0.9482 0.9989 0.1845  -0.0332 -0.0880 142 HIS   B CD2 
1938 C CE1 . HIS   B 125 ? 1.0731 0.8776 0.9494 0.1755  -0.0448 -0.0816 142 HIS   B CE1 
1939 N NE2 . HIS   B 125 ? 1.1101 0.9308 0.9904 0.1838  -0.0395 -0.0853 142 HIS   B NE2 
1940 N N   . HIS   B 126 ? 1.1185 1.0848 1.1412 0.1622  -0.0292 -0.0900 143 HIS   B N   
1941 C CA  . HIS   B 126 ? 1.2058 1.2114 1.2608 0.1589  -0.0247 -0.0937 143 HIS   B CA  
1942 C C   . HIS   B 126 ? 1.1469 1.1562 1.2206 0.1389  -0.0218 -0.0877 143 HIS   B C   
1943 O O   . HIS   B 126 ? 1.2087 1.2223 1.2906 0.1365  -0.0249 -0.0884 143 HIS   B O   
1944 C CB  . HIS   B 126 ? 1.1671 1.2034 1.2376 0.1619  -0.0166 -0.0979 143 HIS   B CB  
1945 C CG  . HIS   B 126 ? 1.2470 1.3241 1.3500 0.1564  -0.0112 -0.1019 143 HIS   B CG  
1946 N ND1 . HIS   B 126 ? 1.3291 1.4243 1.4421 0.1638  -0.0153 -0.1079 143 HIS   B ND1 
1947 C CD2 . HIS   B 126 ? 1.2132 1.3154 1.3394 0.1435  -0.0020 -0.1010 143 HIS   B CD2 
1948 C CE1 . HIS   B 126 ? 1.2820 1.4128 1.4239 0.1550  -0.0090 -0.1108 143 HIS   B CE1 
1949 N NE2 . HIS   B 126 ? 1.2406 1.3752 1.3904 0.1423  -0.0006 -0.1066 143 HIS   B NE2 
1950 C C10 . A1D9R C .   ? 0.5690 0.5051 0.7983 -0.0004 0.0506  -0.0360 201 A1D9R B C10 
1951 C C13 . A1D9R C .   ? 0.5962 0.5427 0.8319 -0.0094 0.0469  -0.0275 201 A1D9R B C13 
1952 C C15 . A1D9R C .   ? 0.6293 0.5866 0.8640 0.0106  0.0472  -0.0205 201 A1D9R B C15 
1953 C C17 . A1D9R C .   ? 0.7367 0.7138 0.9757 0.0198  0.0451  -0.0114 201 A1D9R B C17 
1954 C C21 . A1D9R C .   ? 0.7653 0.7064 0.9906 0.0331  0.0570  -0.0199 201 A1D9R B C21 
1955 C C24 . A1D9R C .   ? 0.8050 0.7590 1.0325 0.0505  0.0555  -0.0047 201 A1D9R B C24 
1956 C C01 . A1D9R C .   ? 0.5490 0.4827 0.7864 -0.0380 0.0558  -0.0445 201 A1D9R B C01 
1957 C C02 . A1D9R C .   ? 0.5253 0.4710 0.7668 -0.0348 0.0506  -0.0480 201 A1D9R B C02 
1958 C C03 . A1D9R C .   ? 0.5030 0.4457 0.7417 -0.0274 0.0492  -0.0459 201 A1D9R B C03 
1959 C C04 . A1D9R C .   ? 0.4780 0.4077 0.7110 -0.0221 0.0526  -0.0404 201 A1D9R B C04 
1960 C C05 . A1D9R C .   ? 0.5485 0.4652 0.7768 -0.0239 0.0572  -0.0368 201 A1D9R B C05 
1961 C C06 . A1D9R C .   ? 0.5853 0.5029 0.8151 -0.0325 0.0590  -0.0387 201 A1D9R B C06 
1962 C C07 . A1D9R C .   ? 0.5072 0.4375 0.7386 -0.0146 0.0515  -0.0387 201 A1D9R B C07 
1963 C C08 . A1D9R C .   ? 0.5098 0.4324 0.7375 -0.0137 0.0531  -0.0436 201 A1D9R B C08 
1964 C C09 . A1D9R C .   ? 0.5716 0.4965 0.7978 -0.0061 0.0527  -0.0422 201 A1D9R B C09 
1965 C C11 . A1D9R C .   ? 0.5507 0.4936 0.7833 -0.0019 0.0485  -0.0312 201 A1D9R B C11 
1966 C C12 . A1D9R C .   ? 0.5382 0.4776 0.7715 -0.0085 0.0490  -0.0326 201 A1D9R B C12 
1967 C C18 . A1D9R C .   ? 0.7516 0.7210 0.9877 0.0267  0.0492  -0.0128 201 A1D9R B C18 
1968 C C19 . A1D9R C .   ? 0.7471 0.7001 0.9782 0.0249  0.0523  -0.0180 201 A1D9R B C19 
1969 C C23 . A1D9R C .   ? 0.8656 0.8099 1.0888 0.0523  0.0593  -0.0109 201 A1D9R B C23 
1970 C C25 . A1D9R C .   ? 0.8176 0.7333 1.0297 0.0512  0.0630  -0.0135 201 A1D9R B C25 
1971 C C30 . A1D9R C .   ? 0.5917 0.5887 0.8348 0.0131  0.0376  -0.0060 201 A1D9R B C30 
1972 N N14 . A1D9R C .   ? 0.6977 0.6523 0.9329 0.0025  0.0458  -0.0251 201 A1D9R B N14 
1973 N N16 . A1D9R C .   ? 0.6479 0.6184 0.8858 0.0126  0.0442  -0.0152 201 A1D9R B N16 
1974 N N20 . A1D9R C .   ? 0.7077 0.6554 0.9385 0.0162  0.0512  -0.0219 201 A1D9R B N20 
1975 N N22 . A1D9R C .   ? 0.8322 0.7861 1.0601 0.0432  0.0574  -0.0157 201 A1D9R B N22 
1976 O O26 . A1D9R C .   ? 0.7412 0.6449 0.9458 0.0616  0.0650  -0.0088 201 A1D9R B O26 
1977 O O27 . A1D9R C .   ? 0.7779 0.7191 1.0015 0.0454  0.0554  -0.0034 201 A1D9R B O27 
1978 O O28 . A1D9R C .   ? 0.8287 0.8039 1.0632 0.0535  0.0527  -0.0010 201 A1D9R B O28 
1979 O O29 . A1D9R C .   ? 0.7290 0.7215 0.9717 0.0205  0.0418  -0.0063 201 A1D9R B O29 
1980 O O   . HOH   D .   ? 0.5258 0.5370 0.7557 -0.0094 0.0172  0.0007  301 HOH   B O   
# 
