data_8YO6
# 
_entry.id   8YO6 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8YO6         pdb_00008yo6 10.2210/pdb8yo6/pdb 
WWPDB D_1300045811 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-19 ? 
2 'Structure model' 1 1 2025-04-16 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.title'                   
12 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8YO6 
_pdbx_database_status.recvd_initial_deposition_date   2024-03-12 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              shannon-au@cuhk.edu.hk 
_pdbx_contact_author.name_first         'Shannon Wing Ngor' 
_pdbx_contact_author.name_last          Au 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-3573-9273 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Mok, C.Y.'  1 0009-0001-9314-9431 
'Au, S.W.N.' 2 0000-0002-3573-9273 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Structure 
_citation.journal_id_ASTM           STRUE6 
_citation.journal_id_CSD            2005 
_citation.journal_id_ISSN           0969-2126 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            32 
_citation.language                  ? 
_citation.page_first                1725 
_citation.page_last                 1736.e4 
_citation.title                     
'Structural insights into the assembly pathway of the Helicobacter pylori CagT4SS outer membrane core complex.' 
_citation.year                      2024 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.str.2024.06.019 
_citation.pdbx_database_id_PubMed   39032488 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Mok, C.Y.'   1 ? 
primary 'Chu, H.Y.'   2 ? 
primary 'Lam, W.W.L.' 3 ? 
primary 'Au, S.W.N.'  4 ? 
# 
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 'Cag pathogenicity island protein T' 13754.686 2   ? ? ? ? 
2 water   nat water                                18.015    123 ? ? ? ? 
# 
_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       
;HHHHHHMDKLKDTPFMVQVKLPNYKDYLLDNKQVVLTFKLVHHSKKITLIGDANKILQYKNYFQANGARSDIDFYLQPTL
NQKGVVMIASNYNDNPNSKEKPQTFDVLQGSQPMLGANT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;HHHHHHMDKLKDTPFMVQVKLPNYKDYLLDNKQVVLTFKLVHHSKKITLIGDANKILQYKNYFQANGARSDIDFYLQPTL
NQKGVVMIASNYNDNPNSKEKPQTFDVLQGSQPMLGANT
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   HIS n 
1 2   HIS n 
1 3   HIS n 
1 4   HIS n 
1 5   HIS n 
1 6   HIS n 
1 7   MET n 
1 8   ASP n 
1 9   LYS n 
1 10  LEU n 
1 11  LYS n 
1 12  ASP n 
1 13  THR n 
1 14  PRO n 
1 15  PHE n 
1 16  MET n 
1 17  VAL n 
1 18  GLN n 
1 19  VAL n 
1 20  LYS n 
1 21  LEU n 
1 22  PRO n 
1 23  ASN n 
1 24  TYR n 
1 25  LYS n 
1 26  ASP n 
1 27  TYR n 
1 28  LEU n 
1 29  LEU n 
1 30  ASP n 
1 31  ASN n 
1 32  LYS n 
1 33  GLN n 
1 34  VAL n 
1 35  VAL n 
1 36  LEU n 
1 37  THR n 
1 38  PHE n 
1 39  LYS n 
1 40  LEU n 
1 41  VAL n 
1 42  HIS n 
1 43  HIS n 
1 44  SER n 
1 45  LYS n 
1 46  LYS n 
1 47  ILE n 
1 48  THR n 
1 49  LEU n 
1 50  ILE n 
1 51  GLY n 
1 52  ASP n 
1 53  ALA n 
1 54  ASN n 
1 55  LYS n 
1 56  ILE n 
1 57  LEU n 
1 58  GLN n 
1 59  TYR n 
1 60  LYS n 
1 61  ASN n 
1 62  TYR n 
1 63  PHE n 
1 64  GLN n 
1 65  ALA n 
1 66  ASN n 
1 67  GLY n 
1 68  ALA n 
1 69  ARG n 
1 70  SER n 
1 71  ASP n 
1 72  ILE n 
1 73  ASP n 
1 74  PHE n 
1 75  TYR n 
1 76  LEU n 
1 77  GLN n 
1 78  PRO n 
1 79  THR n 
1 80  LEU n 
1 81  ASN n 
1 82  GLN n 
1 83  LYS n 
1 84  GLY n 
1 85  VAL n 
1 86  VAL n 
1 87  MET n 
1 88  ILE n 
1 89  ALA n 
1 90  SER n 
1 91  ASN n 
1 92  TYR n 
1 93  ASN n 
1 94  ASP n 
1 95  ASN n 
1 96  PRO n 
1 97  ASN n 
1 98  SER n 
1 99  LYS n 
1 100 GLU n 
1 101 LYS n 
1 102 PRO n 
1 103 GLN n 
1 104 THR n 
1 105 PHE n 
1 106 ASP n 
1 107 VAL n 
1 108 LEU n 
1 109 GLN n 
1 110 GLY n 
1 111 SER n 
1 112 GLN n 
1 113 PRO n 
1 114 MET n 
1 115 LEU n 
1 116 GLY n 
1 117 ALA n 
1 118 ASN n 
1 119 THR 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                   119 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'cagT, HPG27_491' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    G27 
_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      'Helicobacter pylori (strain G27)' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     563041 
_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 
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 
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 
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   HIS 1   47  ?   ?   ?   A . n 
A 1 2   HIS 2   48  ?   ?   ?   A . n 
A 1 3   HIS 3   49  ?   ?   ?   A . n 
A 1 4   HIS 4   50  ?   ?   ?   A . n 
A 1 5   HIS 5   51  ?   ?   ?   A . n 
A 1 6   HIS 6   52  ?   ?   ?   A . n 
A 1 7   MET 7   53  ?   ?   ?   A . n 
A 1 8   ASP 8   54  ?   ?   ?   A . n 
A 1 9   LYS 9   55  ?   ?   ?   A . n 
A 1 10  LEU 10  56  ?   ?   ?   A . n 
A 1 11  LYS 11  57  57  LYS LYS A . n 
A 1 12  ASP 12  58  58  ASP ASP A . n 
A 1 13  THR 13  59  59  THR THR A . n 
A 1 14  PRO 14  60  60  PRO PRO A . n 
A 1 15  PHE 15  61  61  PHE PHE A . n 
A 1 16  MET 16  62  62  MET MET A . n 
A 1 17  VAL 17  63  63  VAL VAL A . n 
A 1 18  GLN 18  64  64  GLN GLN A . n 
A 1 19  VAL 19  65  65  VAL VAL A . n 
A 1 20  LYS 20  66  66  LYS LYS A . n 
A 1 21  LEU 21  67  67  LEU LEU A . n 
A 1 22  PRO 22  68  68  PRO PRO A . n 
A 1 23  ASN 23  69  69  ASN ASN A . n 
A 1 24  TYR 24  70  70  TYR TYR A . n 
A 1 25  LYS 25  71  71  LYS LYS A . n 
A 1 26  ASP 26  72  72  ASP ASP A . n 
A 1 27  TYR 27  73  73  TYR TYR A . n 
A 1 28  LEU 28  74  74  LEU LEU A . n 
A 1 29  LEU 29  75  75  LEU LEU A . n 
A 1 30  ASP 30  76  76  ASP ASP A . n 
A 1 31  ASN 31  77  77  ASN ASN A . n 
A 1 32  LYS 32  78  78  LYS LYS A . n 
A 1 33  GLN 33  79  79  GLN GLN A . n 
A 1 34  VAL 34  80  80  VAL VAL A . n 
A 1 35  VAL 35  81  81  VAL VAL A . n 
A 1 36  LEU 36  82  82  LEU LEU A . n 
A 1 37  THR 37  83  83  THR THR A . n 
A 1 38  PHE 38  84  84  PHE PHE A . n 
A 1 39  LYS 39  85  85  LYS LYS A . n 
A 1 40  LEU 40  86  86  LEU LEU A . n 
A 1 41  VAL 41  87  87  VAL VAL A . n 
A 1 42  HIS 42  88  88  HIS HIS A . n 
A 1 43  HIS 43  89  89  HIS HIS A . n 
A 1 44  SER 44  90  90  SER SER A . n 
A 1 45  LYS 45  91  91  LYS LYS A . n 
A 1 46  LYS 46  92  92  LYS LYS A . n 
A 1 47  ILE 47  93  93  ILE ILE A . n 
A 1 48  THR 48  94  94  THR THR A . n 
A 1 49  LEU 49  95  95  LEU LEU A . n 
A 1 50  ILE 50  96  96  ILE ILE A . n 
A 1 51  GLY 51  97  97  GLY GLY A . n 
A 1 52  ASP 52  98  98  ASP ASP A . n 
A 1 53  ALA 53  99  99  ALA ALA A . n 
A 1 54  ASN 54  100 100 ASN ASN A . n 
A 1 55  LYS 55  101 101 LYS LYS A . n 
A 1 56  ILE 56  102 102 ILE ILE A . n 
A 1 57  LEU 57  103 103 LEU LEU A . n 
A 1 58  GLN 58  104 104 GLN GLN A . n 
A 1 59  TYR 59  105 105 TYR TYR A . n 
A 1 60  LYS 60  106 106 LYS LYS A . n 
A 1 61  ASN 61  107 107 ASN ASN A . n 
A 1 62  TYR 62  108 108 TYR TYR A . n 
A 1 63  PHE 63  109 109 PHE PHE A . n 
A 1 64  GLN 64  110 110 GLN GLN A . n 
A 1 65  ALA 65  111 111 ALA ALA A . n 
A 1 66  ASN 66  112 112 ASN ASN A . n 
A 1 67  GLY 67  113 113 GLY GLY A . n 
A 1 68  ALA 68  114 114 ALA ALA A . n 
A 1 69  ARG 69  115 115 ARG ARG A . n 
A 1 70  SER 70  116 116 SER SER A . n 
A 1 71  ASP 71  117 117 ASP ASP A . n 
A 1 72  ILE 72  118 118 ILE ILE A . n 
A 1 73  ASP 73  119 119 ASP ASP A . n 
A 1 74  PHE 74  120 120 PHE PHE A . n 
A 1 75  TYR 75  121 121 TYR TYR A . n 
A 1 76  LEU 76  122 122 LEU LEU A . n 
A 1 77  GLN 77  123 123 GLN GLN A . n 
A 1 78  PRO 78  124 124 PRO PRO A . n 
A 1 79  THR 79  125 125 THR THR A . n 
A 1 80  LEU 80  126 126 LEU LEU A . n 
A 1 81  ASN 81  127 127 ASN ASN A . n 
A 1 82  GLN 82  128 128 GLN GLN A . n 
A 1 83  LYS 83  129 129 LYS LYS A . n 
A 1 84  GLY 84  130 130 GLY GLY A . n 
A 1 85  VAL 85  131 131 VAL VAL A . n 
A 1 86  VAL 86  132 132 VAL VAL A . n 
A 1 87  MET 87  133 133 MET MET A . n 
A 1 88  ILE 88  134 134 ILE ILE A . n 
A 1 89  ALA 89  135 135 ALA ALA A . n 
A 1 90  SER 90  136 136 SER SER A . n 
A 1 91  ASN 91  137 137 ASN ASN A . n 
A 1 92  TYR 92  138 138 TYR TYR A . n 
A 1 93  ASN 93  139 ?   ?   ?   A . n 
A 1 94  ASP 94  140 ?   ?   ?   A . n 
A 1 95  ASN 95  141 ?   ?   ?   A . n 
A 1 96  PRO 96  142 ?   ?   ?   A . n 
A 1 97  ASN 97  143 ?   ?   ?   A . n 
A 1 98  SER 98  144 ?   ?   ?   A . n 
A 1 99  LYS 99  145 ?   ?   ?   A . n 
A 1 100 GLU 100 146 ?   ?   ?   A . n 
A 1 101 LYS 101 147 ?   ?   ?   A . n 
A 1 102 PRO 102 148 ?   ?   ?   A . n 
A 1 103 GLN 103 149 ?   ?   ?   A . n 
A 1 104 THR 104 150 ?   ?   ?   A . n 
A 1 105 PHE 105 151 ?   ?   ?   A . n 
A 1 106 ASP 106 152 ?   ?   ?   A . n 
A 1 107 VAL 107 153 ?   ?   ?   A . n 
A 1 108 LEU 108 154 ?   ?   ?   A . n 
A 1 109 GLN 109 155 ?   ?   ?   A . n 
A 1 110 GLY 110 156 ?   ?   ?   A . n 
A 1 111 SER 111 157 ?   ?   ?   A . n 
A 1 112 GLN 112 158 ?   ?   ?   A . n 
A 1 113 PRO 113 159 ?   ?   ?   A . n 
A 1 114 MET 114 160 ?   ?   ?   A . n 
A 1 115 LEU 115 161 ?   ?   ?   A . n 
A 1 116 GLY 116 162 ?   ?   ?   A . n 
A 1 117 ALA 117 163 ?   ?   ?   A . n 
A 1 118 ASN 118 164 ?   ?   ?   A . n 
A 1 119 THR 119 165 ?   ?   ?   A . n 
B 1 1   HIS 1   47  ?   ?   ?   B . n 
B 1 2   HIS 2   48  ?   ?   ?   B . n 
B 1 3   HIS 3   49  ?   ?   ?   B . n 
B 1 4   HIS 4   50  ?   ?   ?   B . n 
B 1 5   HIS 5   51  ?   ?   ?   B . n 
B 1 6   HIS 6   52  ?   ?   ?   B . n 
B 1 7   MET 7   53  ?   ?   ?   B . n 
B 1 8   ASP 8   54  ?   ?   ?   B . n 
B 1 9   LYS 9   55  ?   ?   ?   B . n 
B 1 10  LEU 10  56  ?   ?   ?   B . n 
B 1 11  LYS 11  57  57  LYS LYS B . n 
B 1 12  ASP 12  58  58  ASP ASP B . n 
B 1 13  THR 13  59  59  THR THR B . n 
B 1 14  PRO 14  60  60  PRO PRO B . n 
B 1 15  PHE 15  61  61  PHE PHE B . n 
B 1 16  MET 16  62  62  MET MET B . n 
B 1 17  VAL 17  63  63  VAL VAL B . n 
B 1 18  GLN 18  64  64  GLN GLN B . n 
B 1 19  VAL 19  65  65  VAL VAL B . n 
B 1 20  LYS 20  66  66  LYS LYS B . n 
B 1 21  LEU 21  67  67  LEU LEU B . n 
B 1 22  PRO 22  68  68  PRO PRO B . n 
B 1 23  ASN 23  69  69  ASN ASN B . n 
B 1 24  TYR 24  70  70  TYR TYR B . n 
B 1 25  LYS 25  71  71  LYS LYS B . n 
B 1 26  ASP 26  72  72  ASP ASP B . n 
B 1 27  TYR 27  73  73  TYR TYR B . n 
B 1 28  LEU 28  74  74  LEU LEU B . n 
B 1 29  LEU 29  75  75  LEU LEU B . n 
B 1 30  ASP 30  76  76  ASP ASP B . n 
B 1 31  ASN 31  77  77  ASN ASN B . n 
B 1 32  LYS 32  78  78  LYS LYS B . n 
B 1 33  GLN 33  79  79  GLN GLN B . n 
B 1 34  VAL 34  80  80  VAL VAL B . n 
B 1 35  VAL 35  81  81  VAL VAL B . n 
B 1 36  LEU 36  82  82  LEU LEU B . n 
B 1 37  THR 37  83  83  THR THR B . n 
B 1 38  PHE 38  84  84  PHE PHE B . n 
B 1 39  LYS 39  85  85  LYS LYS B . n 
B 1 40  LEU 40  86  86  LEU LEU B . n 
B 1 41  VAL 41  87  87  VAL VAL B . n 
B 1 42  HIS 42  88  88  HIS HIS B . n 
B 1 43  HIS 43  89  89  HIS HIS B . n 
B 1 44  SER 44  90  90  SER SER B . n 
B 1 45  LYS 45  91  91  LYS LYS B . n 
B 1 46  LYS 46  92  92  LYS LYS B . n 
B 1 47  ILE 47  93  93  ILE ILE B . n 
B 1 48  THR 48  94  94  THR THR B . n 
B 1 49  LEU 49  95  95  LEU LEU B . n 
B 1 50  ILE 50  96  96  ILE ILE B . n 
B 1 51  GLY 51  97  97  GLY GLY B . n 
B 1 52  ASP 52  98  98  ASP ASP B . n 
B 1 53  ALA 53  99  99  ALA ALA B . n 
B 1 54  ASN 54  100 100 ASN ASN B . n 
B 1 55  LYS 55  101 101 LYS LYS B . n 
B 1 56  ILE 56  102 102 ILE ILE B . n 
B 1 57  LEU 57  103 103 LEU LEU B . n 
B 1 58  GLN 58  104 104 GLN GLN B . n 
B 1 59  TYR 59  105 105 TYR TYR B . n 
B 1 60  LYS 60  106 106 LYS LYS B . n 
B 1 61  ASN 61  107 107 ASN ASN B . n 
B 1 62  TYR 62  108 108 TYR TYR B . n 
B 1 63  PHE 63  109 109 PHE PHE B . n 
B 1 64  GLN 64  110 110 GLN GLN B . n 
B 1 65  ALA 65  111 111 ALA ALA B . n 
B 1 66  ASN 66  112 112 ASN ASN B . n 
B 1 67  GLY 67  113 113 GLY GLY B . n 
B 1 68  ALA 68  114 114 ALA ALA B . n 
B 1 69  ARG 69  115 115 ARG ARG B . n 
B 1 70  SER 70  116 116 SER SER B . n 
B 1 71  ASP 71  117 117 ASP ASP B . n 
B 1 72  ILE 72  118 118 ILE ILE B . n 
B 1 73  ASP 73  119 119 ASP ASP B . n 
B 1 74  PHE 74  120 120 PHE PHE B . n 
B 1 75  TYR 75  121 121 TYR TYR B . n 
B 1 76  LEU 76  122 122 LEU LEU B . n 
B 1 77  GLN 77  123 123 GLN GLN B . n 
B 1 78  PRO 78  124 124 PRO PRO B . n 
B 1 79  THR 79  125 125 THR THR B . n 
B 1 80  LEU 80  126 126 LEU LEU B . n 
B 1 81  ASN 81  127 127 ASN ASN B . n 
B 1 82  GLN 82  128 128 GLN GLN B . n 
B 1 83  LYS 83  129 129 LYS LYS B . n 
B 1 84  GLY 84  130 130 GLY GLY B . n 
B 1 85  VAL 85  131 131 VAL VAL B . n 
B 1 86  VAL 86  132 132 VAL VAL B . n 
B 1 87  MET 87  133 133 MET MET B . n 
B 1 88  ILE 88  134 134 ILE ILE B . n 
B 1 89  ALA 89  135 135 ALA ALA B . n 
B 1 90  SER 90  136 136 SER SER B . n 
B 1 91  ASN 91  137 137 ASN ASN B . n 
B 1 92  TYR 92  138 138 TYR TYR B . n 
B 1 93  ASN 93  139 ?   ?   ?   B . n 
B 1 94  ASP 94  140 ?   ?   ?   B . n 
B 1 95  ASN 95  141 ?   ?   ?   B . n 
B 1 96  PRO 96  142 ?   ?   ?   B . n 
B 1 97  ASN 97  143 ?   ?   ?   B . n 
B 1 98  SER 98  144 ?   ?   ?   B . n 
B 1 99  LYS 99  145 ?   ?   ?   B . n 
B 1 100 GLU 100 146 ?   ?   ?   B . n 
B 1 101 LYS 101 147 ?   ?   ?   B . n 
B 1 102 PRO 102 148 ?   ?   ?   B . n 
B 1 103 GLN 103 149 ?   ?   ?   B . n 
B 1 104 THR 104 150 ?   ?   ?   B . n 
B 1 105 PHE 105 151 ?   ?   ?   B . n 
B 1 106 ASP 106 152 ?   ?   ?   B . n 
B 1 107 VAL 107 153 ?   ?   ?   B . n 
B 1 108 LEU 108 154 ?   ?   ?   B . n 
B 1 109 GLN 109 155 ?   ?   ?   B . n 
B 1 110 GLY 110 156 ?   ?   ?   B . n 
B 1 111 SER 111 157 ?   ?   ?   B . n 
B 1 112 GLN 112 158 ?   ?   ?   B . n 
B 1 113 PRO 113 159 ?   ?   ?   B . n 
B 1 114 MET 114 160 ?   ?   ?   B . n 
B 1 115 LEU 115 161 ?   ?   ?   B . n 
B 1 116 GLY 116 162 ?   ?   ?   B . n 
B 1 117 ALA 117 163 ?   ?   ?   B . n 
B 1 118 ASN 118 164 ?   ?   ?   B . n 
B 1 119 THR 119 165 ?   ?   ?   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 HOH 1  201 43  HOH HOH A . 
C 2 HOH 2  202 7   HOH HOH A . 
C 2 HOH 3  203 76  HOH HOH A . 
C 2 HOH 4  204 81  HOH HOH A . 
C 2 HOH 5  205 99  HOH HOH A . 
C 2 HOH 6  206 71  HOH HOH A . 
C 2 HOH 7  207 120 HOH HOH A . 
C 2 HOH 8  208 6   HOH HOH A . 
C 2 HOH 9  209 4   HOH HOH A . 
C 2 HOH 10 210 12  HOH HOH A . 
C 2 HOH 11 211 9   HOH HOH A . 
C 2 HOH 12 212 41  HOH HOH A . 
C 2 HOH 13 213 115 HOH HOH A . 
C 2 HOH 14 214 85  HOH HOH A . 
C 2 HOH 15 215 72  HOH HOH A . 
C 2 HOH 16 216 38  HOH HOH A . 
C 2 HOH 17 217 15  HOH HOH A . 
C 2 HOH 18 218 80  HOH HOH A . 
C 2 HOH 19 219 59  HOH HOH A . 
C 2 HOH 20 220 2   HOH HOH A . 
C 2 HOH 21 221 49  HOH HOH A . 
C 2 HOH 22 222 60  HOH HOH A . 
C 2 HOH 23 223 13  HOH HOH A . 
C 2 HOH 24 224 92  HOH HOH A . 
C 2 HOH 25 225 33  HOH HOH A . 
C 2 HOH 26 226 73  HOH HOH A . 
C 2 HOH 27 227 75  HOH HOH A . 
C 2 HOH 28 228 19  HOH HOH A . 
C 2 HOH 29 229 106 HOH HOH A . 
C 2 HOH 30 230 118 HOH HOH A . 
C 2 HOH 31 231 89  HOH HOH A . 
C 2 HOH 32 232 14  HOH HOH A . 
C 2 HOH 33 233 101 HOH HOH A . 
C 2 HOH 34 234 36  HOH HOH A . 
C 2 HOH 35 235 117 HOH HOH A . 
C 2 HOH 36 236 65  HOH HOH A . 
C 2 HOH 37 237 61  HOH HOH A . 
C 2 HOH 38 238 3   HOH HOH A . 
C 2 HOH 39 239 102 HOH HOH A . 
C 2 HOH 40 240 45  HOH HOH A . 
C 2 HOH 41 241 112 HOH HOH A . 
C 2 HOH 42 242 42  HOH HOH A . 
C 2 HOH 43 243 18  HOH HOH A . 
C 2 HOH 44 244 40  HOH HOH A . 
C 2 HOH 45 245 5   HOH HOH A . 
C 2 HOH 46 246 17  HOH HOH A . 
C 2 HOH 47 247 56  HOH HOH A . 
C 2 HOH 48 248 54  HOH HOH A . 
C 2 HOH 49 249 44  HOH HOH A . 
C 2 HOH 50 250 82  HOH HOH A . 
C 2 HOH 51 251 64  HOH HOH A . 
C 2 HOH 52 252 74  HOH HOH A . 
C 2 HOH 53 253 20  HOH HOH A . 
C 2 HOH 54 254 122 HOH HOH A . 
C 2 HOH 55 255 51  HOH HOH A . 
C 2 HOH 56 256 35  HOH HOH A . 
C 2 HOH 57 257 108 HOH HOH A . 
C 2 HOH 58 258 21  HOH HOH A . 
C 2 HOH 59 259 66  HOH HOH A . 
C 2 HOH 60 260 93  HOH HOH A . 
C 2 HOH 61 261 94  HOH HOH A . 
C 2 HOH 62 262 57  HOH HOH A . 
C 2 HOH 63 263 109 HOH HOH A . 
C 2 HOH 64 264 124 HOH HOH A . 
C 2 HOH 65 265 50  HOH HOH A . 
C 2 HOH 66 266 97  HOH HOH A . 
C 2 HOH 67 267 114 HOH HOH A . 
C 2 HOH 68 268 69  HOH HOH A . 
C 2 HOH 69 269 103 HOH HOH A . 
C 2 HOH 70 270 84  HOH HOH A . 
C 2 HOH 71 271 121 HOH HOH A . 
C 2 HOH 72 272 128 HOH HOH A . 
C 2 HOH 73 273 16  HOH HOH A . 
C 2 HOH 74 274 111 HOH HOH A . 
C 2 HOH 75 275 55  HOH HOH A . 
C 2 HOH 76 276 68  HOH HOH A . 
C 2 HOH 77 277 100 HOH HOH A . 
C 2 HOH 78 278 48  HOH HOH A . 
C 2 HOH 79 279 78  HOH HOH A . 
C 2 HOH 80 280 46  HOH HOH A . 
C 2 HOH 81 281 58  HOH HOH A . 
C 2 HOH 82 282 30  HOH HOH A . 
C 2 HOH 83 283 53  HOH HOH A . 
C 2 HOH 84 284 86  HOH HOH A . 
C 2 HOH 85 285 90  HOH HOH A . 
C 2 HOH 86 286 39  HOH HOH A . 
C 2 HOH 87 287 31  HOH HOH A . 
C 2 HOH 88 288 23  HOH HOH A . 
C 2 HOH 89 289 123 HOH HOH A . 
C 2 HOH 90 290 113 HOH HOH A . 
C 2 HOH 91 291 126 HOH HOH A . 
C 2 HOH 92 292 24  HOH HOH A . 
D 2 HOH 1  201 119 HOH HOH B . 
D 2 HOH 2  202 8   HOH HOH B . 
D 2 HOH 3  203 26  HOH HOH B . 
D 2 HOH 4  204 79  HOH HOH B . 
D 2 HOH 5  205 104 HOH HOH B . 
D 2 HOH 6  206 29  HOH HOH B . 
D 2 HOH 7  207 1   HOH HOH B . 
D 2 HOH 8  208 125 HOH HOH B . 
D 2 HOH 9  209 10  HOH HOH B . 
D 2 HOH 10 210 83  HOH HOH B . 
D 2 HOH 11 211 25  HOH HOH B . 
D 2 HOH 12 212 27  HOH HOH B . 
D 2 HOH 13 213 98  HOH HOH B . 
D 2 HOH 14 214 11  HOH HOH B . 
D 2 HOH 15 215 116 HOH HOH B . 
D 2 HOH 16 216 28  HOH HOH B . 
D 2 HOH 17 217 107 HOH HOH B . 
D 2 HOH 18 218 95  HOH HOH B . 
D 2 HOH 19 219 67  HOH HOH B . 
D 2 HOH 20 220 96  HOH HOH B . 
D 2 HOH 21 221 105 HOH HOH B . 
D 2 HOH 22 222 22  HOH HOH B . 
D 2 HOH 23 223 52  HOH HOH B . 
D 2 HOH 24 224 91  HOH HOH B . 
D 2 HOH 25 225 37  HOH HOH B . 
D 2 HOH 26 226 87  HOH HOH B . 
D 2 HOH 27 227 34  HOH HOH B . 
D 2 HOH 28 228 70  HOH HOH B . 
D 2 HOH 29 229 47  HOH HOH B . 
D 2 HOH 30 230 127 HOH HOH B . 
D 2 HOH 31 231 63  HOH HOH B . 
# 
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' ? ? ? ? ? ? ? ? ? ? ? MOSFLM  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8YO6 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.090 
_cell.length_a_esd                 ? 
_cell.length_b                     86.250 
_cell.length_b_esd                 ? 
_cell.length_c                     105.940 
_cell.length_c_esd                 ? 
_cell.volume                       466825.934 
_cell.volume_esd                   ? 
_cell.Z_PDB                        16 
_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                         8YO6 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                23 
_symmetry.space_group_name_Hall            'I 2 2' 
_symmetry.space_group_name_H-M             'I 2 2 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8YO6 
_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             2.32 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.01 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              6.5 
_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    
'Morpheus III F1 condition 0.6% antibiotics mix, 0.1M buffer system 1, 30% v/v precipitant mix 1, 1% 1,4-dioxane' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX300HE' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2021-11-19 
_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   1.0000 
_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                        'NSRRC BEAMLINE BL15A1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL15A1 
_diffrn_source.pdbx_synchrotron_site       NSRRC 
# 
_reflns.B_iso_Wilson_estimate                          23.44 
_reflns.entry_id                                       8YO6 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.95 
_reflns.d_resolution_low                               33.83 
_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                                     17417 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           99.8 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.6 
_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                                   0.995 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.079 
_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                                    1.95 
_reflns_shell.d_res_low                                     2 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.2 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1210 
_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                               3.3 
_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                                  0.684 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          100 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.464 
_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                               36.03 
_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                                 8YO6 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.95 
_refine.ls_d_res_low                             29.05 
_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                     17403 
_refine.ls_number_reflns_R_free                  810 
_refine.ls_number_reflns_R_work                  16593 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.59 
_refine.ls_percent_reflns_R_free                 4.65 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1937 
_refine.ls_R_factor_R_free                       0.2285 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1919 
_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                          1.34 
_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                      ? 
_refine.pdbx_stereochemistry_target_values       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 22.9260 
_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                            0.1889 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.95 
_refine_hist.d_res_low                        29.05 
_refine_hist.number_atoms_solvent             123 
_refine_hist.number_atoms_total               1465 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        1342 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0078 ? 1370 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.8664 ? 1850 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0617 ? 208  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0064 ? 232  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 4.5967 ? 176  ? f_dihedral_angle_d ? ? 
# 
_refine_ls_restr_ncs.pdbx_ordinal        1 
_refine_ls_restr_ncs.pdbx_refine_id      'X-RAY DIFFRACTION' 
_refine_ls_restr_ncs.dom_id              d_2 
_refine_ls_restr_ncs.pdbx_ens_id         ens_1 
_refine_ls_restr_ncs.rms_dev_position    0.978463879405 
_refine_ls_restr_ncs.weight_position     ? 
_refine_ls_restr_ncs.rms_dev_B_iso       ? 
_refine_ls_restr_ncs.weight_B_iso        ? 
_refine_ls_restr_ncs.pdbx_type           'Torsion NCS' 
_refine_ls_restr_ncs.pdbx_asym_id        A 
_refine_ls_restr_ncs.pdbx_auth_asym_id   A 
_refine_ls_restr_ncs.pdbx_number         ? 
_refine_ls_restr_ncs.pdbx_rms            ? 
_refine_ls_restr_ncs.pdbx_weight         ? 
_refine_ls_restr_ncs.ncs_model_details   ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.95 2.07  . . 129 2725 100.00 . . . . 0.2514 . . . . . . . . . . . 0.2698 
'X-RAY DIFFRACTION' 2.07 2.23  . . 133 2736 99.90  . . . . 0.2283 . . . . . . . . . . . 0.3030 
'X-RAY DIFFRACTION' 2.23 2.46  . . 135 2754 99.90  . . . . 0.2045 . . . . . . . . . . . 0.2321 
'X-RAY DIFFRACTION' 2.46 2.81  . . 135 2740 99.90  . . . . 0.2013 . . . . . . . . . . . 0.2057 
'X-RAY DIFFRACTION' 2.81 3.54  . . 148 2776 99.66  . . . . 0.1886 . . . . . . . . . . . 0.2433 
'X-RAY DIFFRACTION' 3.54 29.05 . . 130 2862 98.29  . . . . 0.1659 . . . . . . . . . . . 0.2012 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.matrix[1][1]   0.936015393294 
_struct_ncs_oper.matrix[1][2]   0.282499594493 
_struct_ncs_oper.matrix[1][3]   -0.209926564846 
_struct_ncs_oper.matrix[2][1]   0.278097721412 
_struct_ncs_oper.matrix[2][2]   -0.959206651141 
_struct_ncs_oper.matrix[2][3]   -0.0508355953342 
_struct_ncs_oper.matrix[3][1]   -0.215723992319 
_struct_ncs_oper.matrix[3][2]   -0.0107971995875 
_struct_ncs_oper.matrix[3][3]   -0.976394684346 
_struct_ncs_oper.vector[1]      -3.92812416621 
_struct_ncs_oper.vector[2]      47.5839454473 
_struct_ncs_oper.vector[3]      25.9027265091 
_struct_ncs_oper.details        ? 
# 
loop_
_struct_ncs_dom.pdbx_ens_id 
_struct_ncs_dom.id 
_struct_ncs_dom.details 
ens_1 d_1 
;(chain "A" and (resid 58 through 65 or resid 67 through 70 or resid 72 through 87 or resid 89 through 113 or resid 116 through 126 or resid 130 through 138))
;
ens_1 d_2 
;(chain "B" and (resid 58 through 65 or resid 67 through 70 or resid 72 through 87 or resid 89 through 113 or resid 116 through 126 or resid 130 through 138))
;
# 
loop_
_struct_ncs_dom_lim.pdbx_ens_id 
_struct_ncs_dom_lim.dom_id 
_struct_ncs_dom_lim.pdbx_component_id 
_struct_ncs_dom_lim.beg_label_asym_id 
_struct_ncs_dom_lim.beg_label_comp_id 
_struct_ncs_dom_lim.beg_label_seq_id 
_struct_ncs_dom_lim.beg_label_alt_id 
_struct_ncs_dom_lim.end_label_asym_id 
_struct_ncs_dom_lim.end_label_comp_id 
_struct_ncs_dom_lim.end_label_seq_id 
_struct_ncs_dom_lim.end_label_alt_id 
_struct_ncs_dom_lim.beg_auth_asym_id 
_struct_ncs_dom_lim.beg_auth_comp_id 
_struct_ncs_dom_lim.beg_auth_seq_id 
_struct_ncs_dom_lim.end_auth_asym_id 
_struct_ncs_dom_lim.end_auth_comp_id 
_struct_ncs_dom_lim.end_auth_seq_id 
_struct_ncs_dom_lim.pdbx_refine_code 
_struct_ncs_dom_lim.selection_details 
ens_1 d_1 1 A ASP 12 . A VAL 19 . A ASP 58  A VAL 65  ? ? 
ens_1 d_1 2 A LEU 21 . A TYR 24 . A LEU 67  A TYR 70  ? ? 
ens_1 d_1 3 A ASP 26 . A VAL 41 . A ASP 72  A VAL 87  ? ? 
ens_1 d_1 4 A HIS 43 . A GLY 67 . A HIS 89  A GLY 113 ? ? 
ens_1 d_1 5 A SER 70 . A LEU 80 . A SER 116 A LEU 126 ? ? 
ens_1 d_1 6 A GLY 84 . A TYR 92 . A GLY 130 A TYR 138 ? ? 
ens_1 d_2 1 B ASP 12 . B VAL 19 . B ASP 58  B VAL 65  ? ? 
ens_1 d_2 2 B LEU 21 . B TYR 24 . B LEU 67  B TYR 70  ? ? 
ens_1 d_2 3 B ASP 26 . B VAL 41 . B ASP 72  B VAL 87  ? ? 
ens_1 d_2 4 B HIS 43 . B GLY 67 . B HIS 89  B GLY 113 ? ? 
ens_1 d_2 5 B SER 70 . B LEU 80 . B SER 116 B LEU 126 ? ? 
ens_1 d_2 6 B GLY 84 . B TYR 92 . B GLY 130 B TYR 138 ? ? 
# 
_struct_ncs_ens.id        ens_1 
_struct_ncs_ens.details   ? 
# 
_struct_ncs_ens_gen.ens_id     ens_1 
_struct_ncs_ens_gen.dom_id_1   d_2 
_struct_ncs_ens_gen.dom_id_2   d_1 
_struct_ncs_ens_gen.oper_id    1 
# 
_struct.entry_id                     8YO6 
_struct.title                        'Crystal structure of CagT from Helicobacter pylori' 
_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        8YO6 
_struct_keywords.text            'Type IV secretion system, Helicobacter pylori, STRUCTURAL PROTEIN' 
_struct_keywords.pdbx_keywords   'STRUCTURAL PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    B5Z6Q4_HELPG 
_struct_ref.pdbx_db_accession          B5Z6Q4 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;DKLKDTPFMVQVKLPNYKDYLLDNKQVVLTFKLVHHSKKITLIGDANKILQYKNYFQANGARSDIDFYLQPTLNQKGVVM
IASNYNDNPNSKEKPQTFDVLQGSQPMLGANT
;
_struct_ref.pdbx_align_begin           54 
# 
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 8YO6 A 8 ? 119 ? B5Z6Q4 54 ? 165 ? 54 165 
2 1 8YO6 B 8 ? 119 ? B5Z6Q4 54 ? 165 ? 54 165 
# 
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 8YO6 HIS A 1 ? UNP B5Z6Q4 ? ? 'expression tag' 47 1  
1 8YO6 HIS A 2 ? UNP B5Z6Q4 ? ? 'expression tag' 48 2  
1 8YO6 HIS A 3 ? UNP B5Z6Q4 ? ? 'expression tag' 49 3  
1 8YO6 HIS A 4 ? UNP B5Z6Q4 ? ? 'expression tag' 50 4  
1 8YO6 HIS A 5 ? UNP B5Z6Q4 ? ? 'expression tag' 51 5  
1 8YO6 HIS A 6 ? UNP B5Z6Q4 ? ? 'expression tag' 52 6  
1 8YO6 MET A 7 ? UNP B5Z6Q4 ? ? 'expression tag' 53 7  
2 8YO6 HIS B 1 ? UNP B5Z6Q4 ? ? 'expression tag' 47 8  
2 8YO6 HIS B 2 ? UNP B5Z6Q4 ? ? 'expression tag' 48 9  
2 8YO6 HIS B 3 ? UNP B5Z6Q4 ? ? 'expression tag' 49 10 
2 8YO6 HIS B 4 ? UNP B5Z6Q4 ? ? 'expression tag' 50 11 
2 8YO6 HIS B 5 ? UNP B5Z6Q4 ? ? 'expression tag' 51 12 
2 8YO6 HIS B 6 ? UNP B5Z6Q4 ? ? 'expression tag' 52 13 
2 8YO6 MET B 7 ? UNP B5Z6Q4 ? ? 'expression tag' 53 14 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1120 ? 
1 MORE         -4   ? 
1 'SSA (A^2)'  9730 ? 
# 
_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                
;Analytical ultracentrifugation confirms the molecule exists in monomeric form, however, it exists as a dimer per asymmetric unit in the crystal.
;
# 
_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 ASN A 23 ? LEU A 28 ? ASN A 69 LEU A 74  1 ? 6  
HELX_P HELX_P2 AA2 ASP A 30 ? HIS A 43 ? ASP A 76 HIS A 89  1 ? 14 
HELX_P HELX_P3 AA3 ASP A 52 ? GLY A 67 ? ASP A 98 GLY A 113 1 ? 16 
HELX_P HELX_P4 AA4 ASN B 23 ? LEU B 29 ? ASN B 69 LEU B 75  1 ? 7  
HELX_P HELX_P5 AA5 ASP B 30 ? SER B 44 ? ASP B 76 SER B 90  1 ? 15 
HELX_P HELX_P6 AA6 ASP B 52 ? ASN B 66 ? ASP B 98 ASN B 112 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
_struct_sheet.id               AA1 
_struct_sheet.type             ? 
_struct_sheet.number_strands   8 
_struct_sheet.details          ? 
# 
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 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? 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 ASP A 73 ? PRO A 78 ? ASP A 119 PRO A 124 
AA1 2 LYS A 46 ? GLY A 51 ? LYS A 92  GLY A 97  
AA1 3 VAL A 85 ? SER A 90 ? VAL A 131 SER A 136 
AA1 4 PHE A 15 ? LEU A 21 ? PHE A 61  LEU A 67  
AA1 5 PHE B 15 ? LEU B 21 ? PHE B 61  LEU B 67  
AA1 6 VAL B 85 ? SER B 90 ? VAL B 131 SER B 136 
AA1 7 LYS B 46 ? GLY B 51 ? LYS B 92  GLY B 97  
AA1 8 ASP B 73 ? PRO B 78 ? ASP B 119 PRO B 124 
# 
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 O GLN A 77 ? O GLN A 123 N LEU A 49 ? N LEU A 95  
AA1 2 3 N THR A 48 ? N THR A 94  O ILE A 88 ? O ILE A 134 
AA1 3 4 O VAL A 85 ? O VAL A 131 N LEU A 21 ? N LEU A 67  
AA1 4 5 N GLN A 18 ? N GLN A 64  O MET B 16 ? O MET B 62  
AA1 5 6 N LEU B 21 ? N LEU B 67  O VAL B 85 ? O VAL B 131 
AA1 6 7 O ILE B 88 ? O ILE B 134 N THR B 48 ? N THR B 94  
AA1 7 8 N ILE B 47 ? N ILE B 93  O ASP B 73 ? O ASP B 119 
# 
_pdbx_entry_details.entry_id                   8YO6 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_ligand_of_interest     ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z               
2 x,-y,-z             
3 -x,y,-z             
4 -x,-y,z             
5 x+1/2,y+1/2,z+1/2   
6 x+1/2,-y+1/2,-z+1/2 
7 -x+1/2,y+1/2,-z+1/2 
8 -x+1/2,-y+1/2,z+1/2 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 14.2528907252 28.4126522235 8.52460342275   0.148358754948  ? 0.0190019343847   ? 0.0425311966439 
? 0.0695014014419 ? 0.0283238596369   ? 0.179382385464 ? 3.38734755425  ? 1.73074518119   ? 2.45264878003   ? 3.85631791818  ? 
1.16063984929   ? 7.3286753499  ? -0.0837891876646 ? -0.166085702585  ? 0.0050031790043 ? 0.44557081691     ? -0.0045555691937 ? 
0.0900695913024  ? -0.113516982476 ? 0.00232625456978 ? 0.277755299048   ? 
2  'X-RAY DIFFRACTION' ? refined 6.23777070706 25.2214123804 -0.455774924341 0.0854682632625 ? 0.0259683176315   ? 
-0.0176455141636   ? 0.161759212847  ? 0.00238386920206  ? 0.242338603272 ? 6.49518619482  ? 2.20619539428   ? 1.01769455972   ? 
8.34256710751  ? 4.52318680062   ? 6.75115651057 ? -0.017338027001  ? 0.227008671814   ? -0.210692321488 ? 0.101418562373    ? 
-0.146621185165  ? 0.626671649417   ? 0.223282575546  ? -0.194998839031  ? 0.0907400135569  ? 
3  'X-RAY DIFFRACTION' ? refined 13.4502248469 34.8294018554 -2.32701503779  0.111193342609  ? -0.00663154051564 ? 
0.00334990696102   ? 0.0859397971718 ? 0.0360800926243   ? 0.165282297106 ? 7.6426677867   ? -1.58756410122  ? -0.808291414128 ? 
4.42407309139  ? 0.904896599729  ? 3.8668274008  ? 0.0549210815754  ? 0.0461627563     ? 0.244755564367  ? -0.029659785182   ? 
-0.0194860466902 ? 0.229813749138   ? -0.084157026716 ? 0.0247844453353  ? -0.0398726817589 ? 
4  'X-RAY DIFFRACTION' ? refined 19.5600821058 28.2831836974 0.25240002396   0.0959646639195 ? 0.0052334532948   ? 
-0.00682146623469  ? 0.140346984873  ? -0.00484958163752 ? 0.184915616519 ? 8.452403951    ? -0.123543679039 ? -3.91647574035  ? 
2.6995992851   ? -2.01320390684  ? 3.42851318463 ? -0.214135636859  ? 0.305417923759   ? -0.634821163663 ? -0.06394472621    ? 
-0.0821108745491 ? -0.0586193325422 ? 0.128415048837  ? 0.0689647879239  ? 0.0821214019407  ? 
5  'X-RAY DIFFRACTION' ? refined 12.6244898885 16.7676814512 5.29786708993   0.482267529071  ? -0.106947808988   ? -0.02006518189 
? 0.18905740506   ? -0.0276423847988  ? 0.565899094165 ? 4.75182419729  ? -2.39587537654  ? -1.71255648697  ? 2.20944769516  ? 
-0.165269974201 ? 1.66729090092 ? -0.0785569429905 ? 0.272863660821   ? -1.82044603334  ? -0.350418175232   ? -0.275104270332  ? 
1.36637660494    ? 2.36903349677   ? -1.10793837373   ? 0.137978232637   ? 
6  'X-RAY DIFFRACTION' ? refined 17.7541348603 28.6008953438 19.7417198862   0.30245217346   ? 0.051643766157    ? 
-1.02589283306e-05 ? 0.248508016346  ? 0.107660272365    ? 0.222419542174 ? 9.08711966517  ? -1.27741253695  ? -1.30908228538  ? 
8.33108398153  ? 5.61779994584   ? 7.43078431122 ? 0.0904813213325  ? -0.62315082958   ? 0.228622569131  ? 1.14828272618     ? 
0.575975196415   ? -0.477475313282  ? 0.484559666052  ? -0.118576079481  ? -0.538919201391  ? 
7  'X-RAY DIFFRACTION' ? refined 11.1901379233 29.1089467002 31.2728373433   1.29379747889   ? 0.227867180321    ? 0.551012362382 
? 0.66958365581   ? 0.0785112405414   ? 0.11036131541  ? 0.814342039321 ? 0.0540023057495 ? 0.536497538098  ? 0.192725049623 ? 
-0.28896055315  ? 0.91866736284 ? 0.0855130647793  ? -0.683153887677  ? 0.196393484271  ? 0.450787926946    ? -0.0100357474526 ? 
0.162787452585   ? -0.6654493067   ? 0.262633297739   ? -0.42023050866   ? 
8  'X-RAY DIFFRACTION' ? refined 7.94169943345 22.9625691379 20.5609986038   0.386375105353  ? -0.0168470304917  ? 0.146808163967 
? 0.487010167239  ? 0.200758830242    ? 0.46923112943  ? 7.36372368758  ? -2.52497827242  ? -6.11578845399  ? 8.08574746494  ? 
0.235880119203  ? 8.36316106741 ? -0.0878423675304 ? 0.359828508646   ? -0.228899917513 ? 0.372752157518    ? 0.521759382118   ? 
2.01074345891    ? -0.198532153039 ? -1.44706939876   ? -0.172703599861  ? 
9  'X-RAY DIFFRACTION' ? refined 21.2649003836 20.1407261646 20.5940725076   0.426802296741  ? 0.052075686664    ? 
-0.0109367547401   ? 0.319169467169  ? 0.149843173442    ? 0.374030167061 ? 6.96248116499  ? 4.07837415191   ? 3.8910439529    ? 
4.54276296122  ? 4.99057445956   ? 5.67999305913 ? 0.245144832515   ? -0.562232274269  ? -0.813166066461 ? 0.996311439064    ? 
-0.0237748009114 ? -0.73672215658   ? 0.936224476671  ? 0.445907902927   ? -0.362620724173  ? 
10 'X-RAY DIFFRACTION' ? refined 17.9976193683 20.0765998666 30.0442300973   0.623958930677  ? 0.00766820650949  ? 
-0.0323816419968   ? 0.606121097217  ? 0.240340329714    ? 0.276792137569 ? 4.24257808476  ? 0.324824751027  ? -1.20370109655  ? 
5.93933564249  ? -0.558302370088 ? 3.64508120118 ? -0.182031105153  ? -1.12019692654   ? -0.415385399878 ? 1.40003925346     ? 
0.152418999064   ? 0.00146067989973 ? 0.495514447361  ? 0.207887474444   ? 0.0122811524652  ? 
11 'X-RAY DIFFRACTION' ? refined 12.9969805467 10.9057584749 22.5185080883   0.729082609035  ? -0.103418651003   ? 0.158570588938 
? 0.552325437966  ? 0.325420786174    ? 0.889517194642 ? 7.0511372835   ? -0.908442783767 ? -2.88782457794  ? 1.10304206942  ? 
2.99154402782   ? 8.13251901181 ? 0.309183737591   ? 0.34434931596    ? -0.711052470441 ? 0.91538308087     ? -0.181121571343  ? 
-0.165183818267  ? 1.2140718792    ? -0.968263442866  ? 0.248194063568   ? 
12 'X-RAY DIFFRACTION' ? refined 26.2950635614 24.0570810461 24.9088524972   0.387659822959  ? 0.0812509652278   ? 
-0.0906019397766   ? 0.506165889904  ? 0.225813731953    ? 0.653705271299 ? 2.85345898145  ? 0.829773033478  ? 2.71469881827   ? 
0.234497200979 ? 0.699956913175  ? 8.14925213158 ? -0.222523533461  ? 0.373516192819   ? 0.406732492449  ? -0.00587374539361 ? 
-0.0214717577924 ? -0.610603956291  ? -0.262106190413 ? 0.850843313517   ? 0.16947342142    ? 
13 'X-RAY DIFFRACTION' ? refined 18.9272435955 21.5167699513 15.6363385227   0.298743961421  ? -0.00184782802519 ? -0.016376366281 
? 0.19692462029   ? 0.100385530451    ? 0.285631723497 ? 7.43857150501  ? 3.80087102623   ? 3.90067321463   ? 4.41142412932  ? 
5.19979409037   ? 6.24851639086 ? -0.127666758168  ? -0.0866784532522 ? -0.469980263161 ? 0.289748747085    ? 0.316245117264   ? 
0.303644822613   ? 0.390301671318  ? 0.522764701935   ? -0.10458595875   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_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 
1  'X-RAY DIFFRACTION' 1  A 1  A 57  ? A 13 A 69  ? ? 
;chain 'A' and (resid 57 through 69 )
;
2  'X-RAY DIFFRACTION' 2  A 14 A 70  ? A 33 A 89  ? ? 
;chain 'A' and (resid 70 through 89 )
;
3  'X-RAY DIFFRACTION' 3  A 34 A 90  ? A 68 A 124 ? ? 
;chain 'A' and (resid 90 through 124 )
;
4  'X-RAY DIFFRACTION' 4  A 69 A 125 ? A 82 A 138 ? ? 
;chain 'A' and (resid 125 through 138 )
;
5  'X-RAY DIFFRACTION' 5  B 1  B 57  ? B 5  B 61  ? ? 
;chain 'B' and (resid 57 through 61 )
;
6  'X-RAY DIFFRACTION' 6  B 6  B 62  ? B 13 B 69  ? ? 
;chain 'B' and (resid 62 through 69 )
;
7  'X-RAY DIFFRACTION' 7  B 14 B 70  ? B 20 B 76  ? ? 
;chain 'B' and (resid 70 through 76 )
;
8  'X-RAY DIFFRACTION' 8  B 21 B 77  ? B 33 B 89  ? ? 
;chain 'B' and (resid 77 through 89 )
;
9  'X-RAY DIFFRACTION' 9  B 34 B 90  ? B 42 B 98  ? ? 
;chain 'B' and (resid 90 through 98 )
;
10 'X-RAY DIFFRACTION' 10 B 43 B 99  ? B 55 B 111 ? ? 
;chain 'B' and (resid 99 through 111 )
;
11 'X-RAY DIFFRACTION' 11 B 56 B 112 ? B 62 B 118 ? ? 
;chain 'B' and (resid 112 through 118 )
;
12 'X-RAY DIFFRACTION' 12 B 63 B 119 ? B 74 B 130 ? ? 
;chain 'B' and (resid 119 through 130 )
;
13 'X-RAY DIFFRACTION' 13 B 75 B 131 ? B 82 B 138 ? ? 
;chain 'B' and (resid 131 through 138 )
;
# 
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 47  ? A HIS 1   
2  1 Y 1 A HIS 48  ? A HIS 2   
3  1 Y 1 A HIS 49  ? A HIS 3   
4  1 Y 1 A HIS 50  ? A HIS 4   
5  1 Y 1 A HIS 51  ? A HIS 5   
6  1 Y 1 A HIS 52  ? A HIS 6   
7  1 Y 1 A MET 53  ? A MET 7   
8  1 Y 1 A ASP 54  ? A ASP 8   
9  1 Y 1 A LYS 55  ? A LYS 9   
10 1 Y 1 A LEU 56  ? A LEU 10  
11 1 Y 1 A ASN 139 ? A ASN 93  
12 1 Y 1 A ASP 140 ? A ASP 94  
13 1 Y 1 A ASN 141 ? A ASN 95  
14 1 Y 1 A PRO 142 ? A PRO 96  
15 1 Y 1 A ASN 143 ? A ASN 97  
16 1 Y 1 A SER 144 ? A SER 98  
17 1 Y 1 A LYS 145 ? A LYS 99  
18 1 Y 1 A GLU 146 ? A GLU 100 
19 1 Y 1 A LYS 147 ? A LYS 101 
20 1 Y 1 A PRO 148 ? A PRO 102 
21 1 Y 1 A GLN 149 ? A GLN 103 
22 1 Y 1 A THR 150 ? A THR 104 
23 1 Y 1 A PHE 151 ? A PHE 105 
24 1 Y 1 A ASP 152 ? A ASP 106 
25 1 Y 1 A VAL 153 ? A VAL 107 
26 1 Y 1 A LEU 154 ? A LEU 108 
27 1 Y 1 A GLN 155 ? A GLN 109 
28 1 Y 1 A GLY 156 ? A GLY 110 
29 1 Y 1 A SER 157 ? A SER 111 
30 1 Y 1 A GLN 158 ? A GLN 112 
31 1 Y 1 A PRO 159 ? A PRO 113 
32 1 Y 1 A MET 160 ? A MET 114 
33 1 Y 1 A LEU 161 ? A LEU 115 
34 1 Y 1 A GLY 162 ? A GLY 116 
35 1 Y 1 A ALA 163 ? A ALA 117 
36 1 Y 1 A ASN 164 ? A ASN 118 
37 1 Y 1 A THR 165 ? A THR 119 
38 1 Y 1 B HIS 47  ? B HIS 1   
39 1 Y 1 B HIS 48  ? B HIS 2   
40 1 Y 1 B HIS 49  ? B HIS 3   
41 1 Y 1 B HIS 50  ? B HIS 4   
42 1 Y 1 B HIS 51  ? B HIS 5   
43 1 Y 1 B HIS 52  ? B HIS 6   
44 1 Y 1 B MET 53  ? B MET 7   
45 1 Y 1 B ASP 54  ? B ASP 8   
46 1 Y 1 B LYS 55  ? B LYS 9   
47 1 Y 1 B LEU 56  ? B LEU 10  
48 1 Y 1 B ASN 139 ? B ASN 93  
49 1 Y 1 B ASP 140 ? B ASP 94  
50 1 Y 1 B ASN 141 ? B ASN 95  
51 1 Y 1 B PRO 142 ? B PRO 96  
52 1 Y 1 B ASN 143 ? B ASN 97  
53 1 Y 1 B SER 144 ? B SER 98  
54 1 Y 1 B LYS 145 ? B LYS 99  
55 1 Y 1 B GLU 146 ? B GLU 100 
56 1 Y 1 B LYS 147 ? B LYS 101 
57 1 Y 1 B PRO 148 ? B PRO 102 
58 1 Y 1 B GLN 149 ? B GLN 103 
59 1 Y 1 B THR 150 ? B THR 104 
60 1 Y 1 B PHE 151 ? B PHE 105 
61 1 Y 1 B ASP 152 ? B ASP 106 
62 1 Y 1 B VAL 153 ? B VAL 107 
63 1 Y 1 B LEU 154 ? B LEU 108 
64 1 Y 1 B GLN 155 ? B GLN 109 
65 1 Y 1 B GLY 156 ? B GLY 110 
66 1 Y 1 B SER 157 ? B SER 111 
67 1 Y 1 B GLN 158 ? B GLN 112 
68 1 Y 1 B PRO 159 ? B PRO 113 
69 1 Y 1 B MET 160 ? B MET 114 
70 1 Y 1 B LEU 161 ? B LEU 115 
71 1 Y 1 B GLY 162 ? B GLY 116 
72 1 Y 1 B ALA 163 ? B ALA 117 
73 1 Y 1 B ASN 164 ? B ASN 118 
74 1 Y 1 B THR 165 ? B THR 119 
# 
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 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
GLN N    N N N 74  
GLN CA   C N S 75  
GLN C    C N N 76  
GLN O    O N N 77  
GLN CB   C N N 78  
GLN CG   C N N 79  
GLN CD   C N N 80  
GLN OE1  O N N 81  
GLN NE2  N N N 82  
GLN OXT  O N N 83  
GLN H    H N N 84  
GLN H2   H N N 85  
GLN HA   H N N 86  
GLN HB2  H N N 87  
GLN HB3  H N N 88  
GLN HG2  H N N 89  
GLN HG3  H N N 90  
GLN HE21 H N N 91  
GLN HE22 H N N 92  
GLN HXT  H N N 93  
GLU N    N N N 94  
GLU CA   C N S 95  
GLU C    C N N 96  
GLU O    O N N 97  
GLU CB   C N N 98  
GLU CG   C N N 99  
GLU CD   C N N 100 
GLU OE1  O N N 101 
GLU OE2  O N N 102 
GLU OXT  O N N 103 
GLU H    H N N 104 
GLU H2   H N N 105 
GLU HA   H N N 106 
GLU HB2  H N N 107 
GLU HB3  H N N 108 
GLU HG2  H N N 109 
GLU HG3  H N N 110 
GLU HE2  H N N 111 
GLU HXT  H N N 112 
GLY N    N N N 113 
GLY CA   C N N 114 
GLY C    C N N 115 
GLY O    O N N 116 
GLY OXT  O N N 117 
GLY H    H N N 118 
GLY H2   H N N 119 
GLY HA2  H N N 120 
GLY HA3  H N N 121 
GLY HXT  H N N 122 
HIS N    N N N 123 
HIS CA   C N S 124 
HIS C    C N N 125 
HIS O    O N N 126 
HIS CB   C N N 127 
HIS CG   C Y N 128 
HIS ND1  N Y N 129 
HIS CD2  C Y N 130 
HIS CE1  C Y N 131 
HIS NE2  N Y N 132 
HIS OXT  O N N 133 
HIS H    H N N 134 
HIS H2   H N N 135 
HIS HA   H N N 136 
HIS HB2  H N N 137 
HIS HB3  H N N 138 
HIS HD1  H N N 139 
HIS HD2  H N N 140 
HIS HE1  H N N 141 
HIS HE2  H N N 142 
HIS HXT  H N N 143 
HOH O    O N N 144 
HOH H1   H N N 145 
HOH H2   H N N 146 
ILE N    N N N 147 
ILE CA   C N S 148 
ILE C    C N N 149 
ILE O    O N N 150 
ILE CB   C N S 151 
ILE CG1  C N N 152 
ILE CG2  C N N 153 
ILE CD1  C N N 154 
ILE OXT  O N N 155 
ILE H    H N N 156 
ILE H2   H N N 157 
ILE HA   H N N 158 
ILE HB   H N N 159 
ILE HG12 H N N 160 
ILE HG13 H N N 161 
ILE HG21 H N N 162 
ILE HG22 H N N 163 
ILE HG23 H N N 164 
ILE HD11 H N N 165 
ILE HD12 H N N 166 
ILE HD13 H N N 167 
ILE HXT  H N N 168 
LEU N    N N N 169 
LEU CA   C N S 170 
LEU C    C N N 171 
LEU O    O N N 172 
LEU CB   C N N 173 
LEU CG   C N N 174 
LEU CD1  C N N 175 
LEU CD2  C N N 176 
LEU OXT  O N N 177 
LEU H    H N N 178 
LEU H2   H N N 179 
LEU HA   H N N 180 
LEU HB2  H N N 181 
LEU HB3  H N N 182 
LEU HG   H N N 183 
LEU HD11 H N N 184 
LEU HD12 H N N 185 
LEU HD13 H N N 186 
LEU HD21 H N N 187 
LEU HD22 H N N 188 
LEU HD23 H N N 189 
LEU HXT  H N N 190 
LYS N    N N N 191 
LYS CA   C N S 192 
LYS C    C N N 193 
LYS O    O N N 194 
LYS CB   C N N 195 
LYS CG   C N N 196 
LYS CD   C N N 197 
LYS CE   C N N 198 
LYS NZ   N N N 199 
LYS OXT  O N N 200 
LYS H    H N N 201 
LYS H2   H N N 202 
LYS HA   H N N 203 
LYS HB2  H N N 204 
LYS HB3  H N N 205 
LYS HG2  H N N 206 
LYS HG3  H N N 207 
LYS HD2  H N N 208 
LYS HD3  H N N 209 
LYS HE2  H N N 210 
LYS HE3  H N N 211 
LYS HZ1  H N N 212 
LYS HZ2  H N N 213 
LYS HZ3  H N N 214 
LYS HXT  H N N 215 
MET N    N N N 216 
MET CA   C N S 217 
MET C    C N N 218 
MET O    O N N 219 
MET CB   C N N 220 
MET CG   C N N 221 
MET SD   S N N 222 
MET CE   C N N 223 
MET OXT  O N N 224 
MET H    H N N 225 
MET H2   H N N 226 
MET HA   H N N 227 
MET HB2  H N N 228 
MET HB3  H N N 229 
MET HG2  H N N 230 
MET HG3  H N N 231 
MET HE1  H N N 232 
MET HE2  H N N 233 
MET HE3  H N N 234 
MET HXT  H N N 235 
PHE N    N N N 236 
PHE CA   C N S 237 
PHE C    C N N 238 
PHE O    O N N 239 
PHE CB   C N N 240 
PHE CG   C Y N 241 
PHE CD1  C Y N 242 
PHE CD2  C Y N 243 
PHE CE1  C Y N 244 
PHE CE2  C Y N 245 
PHE CZ   C Y N 246 
PHE OXT  O N N 247 
PHE H    H N N 248 
PHE H2   H N N 249 
PHE HA   H N N 250 
PHE HB2  H N N 251 
PHE HB3  H N N 252 
PHE HD1  H N N 253 
PHE HD2  H N N 254 
PHE HE1  H N N 255 
PHE HE2  H N N 256 
PHE HZ   H N N 257 
PHE HXT  H N N 258 
PRO N    N N N 259 
PRO CA   C N S 260 
PRO C    C N N 261 
PRO O    O N N 262 
PRO CB   C N N 263 
PRO CG   C N N 264 
PRO CD   C N N 265 
PRO OXT  O N N 266 
PRO H    H N N 267 
PRO HA   H N N 268 
PRO HB2  H N N 269 
PRO HB3  H N N 270 
PRO HG2  H N N 271 
PRO HG3  H N N 272 
PRO HD2  H N N 273 
PRO HD3  H N N 274 
PRO HXT  H N N 275 
SER N    N N N 276 
SER CA   C N S 277 
SER C    C N N 278 
SER O    O N N 279 
SER CB   C N N 280 
SER OG   O N N 281 
SER OXT  O N N 282 
SER H    H N N 283 
SER H2   H N N 284 
SER HA   H N N 285 
SER HB2  H N N 286 
SER HB3  H N N 287 
SER HG   H N N 288 
SER HXT  H N N 289 
THR N    N N N 290 
THR CA   C N S 291 
THR C    C N N 292 
THR O    O N N 293 
THR CB   C N R 294 
THR OG1  O N N 295 
THR CG2  C N N 296 
THR OXT  O N N 297 
THR H    H N N 298 
THR H2   H N N 299 
THR HA   H N N 300 
THR HB   H N N 301 
THR HG1  H N N 302 
THR HG21 H N N 303 
THR HG22 H N N 304 
THR HG23 H N N 305 
THR HXT  H N N 306 
TYR N    N N N 307 
TYR CA   C N S 308 
TYR C    C N N 309 
TYR O    O N N 310 
TYR CB   C N N 311 
TYR CG   C Y N 312 
TYR CD1  C Y N 313 
TYR CD2  C Y N 314 
TYR CE1  C Y N 315 
TYR CE2  C Y N 316 
TYR CZ   C Y N 317 
TYR OH   O N N 318 
TYR OXT  O N N 319 
TYR H    H N N 320 
TYR H2   H N N 321 
TYR HA   H N N 322 
TYR HB2  H N N 323 
TYR HB3  H N N 324 
TYR HD1  H N N 325 
TYR HD2  H N N 326 
TYR HE1  H N N 327 
TYR HE2  H N N 328 
TYR HH   H N N 329 
TYR HXT  H N N 330 
VAL N    N N N 331 
VAL CA   C N S 332 
VAL C    C N N 333 
VAL O    O N N 334 
VAL CB   C N N 335 
VAL CG1  C N N 336 
VAL CG2  C N N 337 
VAL OXT  O N N 338 
VAL H    H N N 339 
VAL H2   H N N 340 
VAL HA   H N N 341 
VAL HB   H N N 342 
VAL HG11 H N N 343 
VAL HG12 H N N 344 
VAL HG13 H N N 345 
VAL HG21 H N N 346 
VAL HG22 H N N 347 
VAL HG23 H N N 348 
VAL HXT  H N N 349 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
GLN N   CA   sing N N 70  
GLN N   H    sing N N 71  
GLN N   H2   sing N N 72  
GLN CA  C    sing N N 73  
GLN CA  CB   sing N N 74  
GLN CA  HA   sing N N 75  
GLN C   O    doub N N 76  
GLN C   OXT  sing N N 77  
GLN CB  CG   sing N N 78  
GLN CB  HB2  sing N N 79  
GLN CB  HB3  sing N N 80  
GLN CG  CD   sing N N 81  
GLN CG  HG2  sing N N 82  
GLN CG  HG3  sing N N 83  
GLN CD  OE1  doub N N 84  
GLN CD  NE2  sing N N 85  
GLN NE2 HE21 sing N N 86  
GLN NE2 HE22 sing N N 87  
GLN OXT HXT  sing N N 88  
GLU N   CA   sing N N 89  
GLU N   H    sing N N 90  
GLU N   H2   sing N N 91  
GLU CA  C    sing N N 92  
GLU CA  CB   sing N N 93  
GLU CA  HA   sing N N 94  
GLU C   O    doub N N 95  
GLU C   OXT  sing N N 96  
GLU CB  CG   sing N N 97  
GLU CB  HB2  sing N N 98  
GLU CB  HB3  sing N N 99  
GLU CG  CD   sing N N 100 
GLU CG  HG2  sing N N 101 
GLU CG  HG3  sing N N 102 
GLU CD  OE1  doub N N 103 
GLU CD  OE2  sing N N 104 
GLU OE2 HE2  sing N N 105 
GLU OXT HXT  sing N N 106 
GLY N   CA   sing N N 107 
GLY N   H    sing N N 108 
GLY N   H2   sing N N 109 
GLY CA  C    sing N N 110 
GLY CA  HA2  sing N N 111 
GLY CA  HA3  sing N N 112 
GLY C   O    doub N N 113 
GLY C   OXT  sing N N 114 
GLY OXT HXT  sing N N 115 
HIS N   CA   sing N N 116 
HIS N   H    sing N N 117 
HIS N   H2   sing N N 118 
HIS CA  C    sing N N 119 
HIS CA  CB   sing N N 120 
HIS CA  HA   sing N N 121 
HIS C   O    doub N N 122 
HIS C   OXT  sing N N 123 
HIS CB  CG   sing N N 124 
HIS CB  HB2  sing N N 125 
HIS CB  HB3  sing N N 126 
HIS CG  ND1  sing Y N 127 
HIS CG  CD2  doub Y N 128 
HIS ND1 CE1  doub Y N 129 
HIS ND1 HD1  sing N N 130 
HIS CD2 NE2  sing Y N 131 
HIS CD2 HD2  sing N N 132 
HIS CE1 NE2  sing Y N 133 
HIS CE1 HE1  sing N N 134 
HIS NE2 HE2  sing N N 135 
HIS OXT HXT  sing N N 136 
HOH O   H1   sing N N 137 
HOH O   H2   sing N N 138 
ILE N   CA   sing N N 139 
ILE N   H    sing N N 140 
ILE N   H2   sing N N 141 
ILE CA  C    sing N N 142 
ILE CA  CB   sing N N 143 
ILE CA  HA   sing N N 144 
ILE C   O    doub N N 145 
ILE C   OXT  sing N N 146 
ILE CB  CG1  sing N N 147 
ILE CB  CG2  sing N N 148 
ILE CB  HB   sing N N 149 
ILE CG1 CD1  sing N N 150 
ILE CG1 HG12 sing N N 151 
ILE CG1 HG13 sing N N 152 
ILE CG2 HG21 sing N N 153 
ILE CG2 HG22 sing N N 154 
ILE CG2 HG23 sing N N 155 
ILE CD1 HD11 sing N N 156 
ILE CD1 HD12 sing N N 157 
ILE CD1 HD13 sing N N 158 
ILE OXT HXT  sing N N 159 
LEU N   CA   sing N N 160 
LEU N   H    sing N N 161 
LEU N   H2   sing N N 162 
LEU CA  C    sing N N 163 
LEU CA  CB   sing N N 164 
LEU CA  HA   sing N N 165 
LEU C   O    doub N N 166 
LEU C   OXT  sing N N 167 
LEU CB  CG   sing N N 168 
LEU CB  HB2  sing N N 169 
LEU CB  HB3  sing N N 170 
LEU CG  CD1  sing N N 171 
LEU CG  CD2  sing N N 172 
LEU CG  HG   sing N N 173 
LEU CD1 HD11 sing N N 174 
LEU CD1 HD12 sing N N 175 
LEU CD1 HD13 sing N N 176 
LEU CD2 HD21 sing N N 177 
LEU CD2 HD22 sing N N 178 
LEU CD2 HD23 sing N N 179 
LEU OXT HXT  sing N N 180 
LYS N   CA   sing N N 181 
LYS N   H    sing N N 182 
LYS N   H2   sing N N 183 
LYS CA  C    sing N N 184 
LYS CA  CB   sing N N 185 
LYS CA  HA   sing N N 186 
LYS C   O    doub N N 187 
LYS C   OXT  sing N N 188 
LYS CB  CG   sing N N 189 
LYS CB  HB2  sing N N 190 
LYS CB  HB3  sing N N 191 
LYS CG  CD   sing N N 192 
LYS CG  HG2  sing N N 193 
LYS CG  HG3  sing N N 194 
LYS CD  CE   sing N N 195 
LYS CD  HD2  sing N N 196 
LYS CD  HD3  sing N N 197 
LYS CE  NZ   sing N N 198 
LYS CE  HE2  sing N N 199 
LYS CE  HE3  sing N N 200 
LYS NZ  HZ1  sing N N 201 
LYS NZ  HZ2  sing N N 202 
LYS NZ  HZ3  sing N N 203 
LYS OXT HXT  sing N N 204 
MET N   CA   sing N N 205 
MET N   H    sing N N 206 
MET N   H2   sing N N 207 
MET CA  C    sing N N 208 
MET CA  CB   sing N N 209 
MET CA  HA   sing N N 210 
MET C   O    doub N N 211 
MET C   OXT  sing N N 212 
MET CB  CG   sing N N 213 
MET CB  HB2  sing N N 214 
MET CB  HB3  sing N N 215 
MET CG  SD   sing N N 216 
MET CG  HG2  sing N N 217 
MET CG  HG3  sing N N 218 
MET SD  CE   sing N N 219 
MET CE  HE1  sing N N 220 
MET CE  HE2  sing N N 221 
MET CE  HE3  sing N N 222 
MET OXT HXT  sing N N 223 
PHE N   CA   sing N N 224 
PHE N   H    sing N N 225 
PHE N   H2   sing N N 226 
PHE CA  C    sing N N 227 
PHE CA  CB   sing N N 228 
PHE CA  HA   sing N N 229 
PHE C   O    doub N N 230 
PHE C   OXT  sing N N 231 
PHE CB  CG   sing N N 232 
PHE CB  HB2  sing N N 233 
PHE CB  HB3  sing N N 234 
PHE CG  CD1  doub Y N 235 
PHE CG  CD2  sing Y N 236 
PHE CD1 CE1  sing Y N 237 
PHE CD1 HD1  sing N N 238 
PHE CD2 CE2  doub Y N 239 
PHE CD2 HD2  sing N N 240 
PHE CE1 CZ   doub Y N 241 
PHE CE1 HE1  sing N N 242 
PHE CE2 CZ   sing Y N 243 
PHE CE2 HE2  sing N N 244 
PHE CZ  HZ   sing N N 245 
PHE OXT HXT  sing N N 246 
PRO N   CA   sing N N 247 
PRO N   CD   sing N N 248 
PRO N   H    sing N N 249 
PRO CA  C    sing N N 250 
PRO CA  CB   sing N N 251 
PRO CA  HA   sing N N 252 
PRO C   O    doub N N 253 
PRO C   OXT  sing N N 254 
PRO CB  CG   sing N N 255 
PRO CB  HB2  sing N N 256 
PRO CB  HB3  sing N N 257 
PRO CG  CD   sing N N 258 
PRO CG  HG2  sing N N 259 
PRO CG  HG3  sing N N 260 
PRO CD  HD2  sing N N 261 
PRO CD  HD3  sing N N 262 
PRO OXT HXT  sing N N 263 
SER N   CA   sing N N 264 
SER N   H    sing N N 265 
SER N   H2   sing N N 266 
SER CA  C    sing N N 267 
SER CA  CB   sing N N 268 
SER CA  HA   sing N N 269 
SER C   O    doub N N 270 
SER C   OXT  sing N N 271 
SER CB  OG   sing N N 272 
SER CB  HB2  sing N N 273 
SER CB  HB3  sing N N 274 
SER OG  HG   sing N N 275 
SER OXT HXT  sing N N 276 
THR N   CA   sing N N 277 
THR N   H    sing N N 278 
THR N   H2   sing N N 279 
THR CA  C    sing N N 280 
THR CA  CB   sing N N 281 
THR CA  HA   sing N N 282 
THR C   O    doub N N 283 
THR C   OXT  sing N N 284 
THR CB  OG1  sing N N 285 
THR CB  CG2  sing N N 286 
THR CB  HB   sing N N 287 
THR OG1 HG1  sing N N 288 
THR CG2 HG21 sing N N 289 
THR CG2 HG22 sing N N 290 
THR CG2 HG23 sing N N 291 
THR OXT HXT  sing N N 292 
TYR N   CA   sing N N 293 
TYR N   H    sing N N 294 
TYR N   H2   sing N N 295 
TYR CA  C    sing N N 296 
TYR CA  CB   sing N N 297 
TYR CA  HA   sing N N 298 
TYR C   O    doub N N 299 
TYR C   OXT  sing N N 300 
TYR CB  CG   sing N N 301 
TYR CB  HB2  sing N N 302 
TYR CB  HB3  sing N N 303 
TYR CG  CD1  doub Y N 304 
TYR CG  CD2  sing Y N 305 
TYR CD1 CE1  sing Y N 306 
TYR CD1 HD1  sing N N 307 
TYR CD2 CE2  doub Y N 308 
TYR CD2 HD2  sing N N 309 
TYR CE1 CZ   doub Y N 310 
TYR CE1 HE1  sing N N 311 
TYR CE2 CZ   sing Y N 312 
TYR CE2 HE2  sing N N 313 
TYR CZ  OH   sing N N 314 
TYR OH  HH   sing N N 315 
TYR OXT HXT  sing N N 316 
VAL N   CA   sing N N 317 
VAL N   H    sing N N 318 
VAL N   H2   sing N N 319 
VAL CA  C    sing N N 320 
VAL CA  CB   sing N N 321 
VAL CA  HA   sing N N 322 
VAL C   O    doub N N 323 
VAL C   OXT  sing N N 324 
VAL CB  CG1  sing N N 325 
VAL CB  CG2  sing N N 326 
VAL CB  HB   sing N N 327 
VAL CG1 HG11 sing N N 328 
VAL CG1 HG12 sing N N 329 
VAL CG1 HG13 sing N N 330 
VAL CG2 HG21 sing N N 331 
VAL CG2 HG22 sing N N 332 
VAL CG2 HG23 sing N N 333 
VAL OXT HXT  sing N N 334 
# 
_pdbx_audit_support.funding_organization   'The University Grants Committee, Research Grants Council (RGC)' 
_pdbx_audit_support.country                'Hong Kong' 
_pdbx_audit_support.grant_number           14121619 
_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   6x6s 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'I 2 2 2' 
_space_group.name_Hall        'I 2 2' 
_space_group.IT_number        23 
_space_group.crystal_system   orthorhombic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8YO6 
_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]   0.019573 
_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]   0.011594 
_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]   0.009439 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C ? ? 3.54356 2.42580 ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N ? ? 4.01032 2.96436 ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O ? ? 4.49882 3.47563 ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S ? ? 9.55732 6.39887 ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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   . LYS A 1 11 ? 9.49597  39.00156 21.57838  1.000 69.81421  ? 57  LYS A N   1 
ATOM   2    C CA  . LYS A 1 11 ? 8.63484  38.02965 22.24111  1.000 71.36380  ? 57  LYS A CA  1 
ATOM   3    C C   . LYS A 1 11 ? 8.67331  36.72048 21.47280  1.000 66.67850  ? 57  LYS A C   1 
ATOM   4    O O   . LYS A 1 11 ? 8.73550  35.64285 22.06969  1.000 70.17373  ? 57  LYS A O   1 
ATOM   5    C CB  . LYS A 1 11 ? 7.19794  38.54717 22.34342  1.000 72.60025  ? 57  LYS A CB  1 
ATOM   6    C CG  . LYS A 1 11 ? 7.06098  39.84380 23.11437  1.000 75.80695  ? 57  LYS A CG  1 
ATOM   7    C CD  . LYS A 1 11 ? 7.51324  39.69576 24.55628  1.000 78.01925  ? 57  LYS A CD  1 
ATOM   8    C CE  . LYS A 1 11 ? 6.52144  38.85856 25.35218  1.000 79.13952  ? 57  LYS A CE  1 
ATOM   9    N NZ  . LYS A 1 11 ? 6.82263  38.87565 26.80892  1.000 81.97853  ? 57  LYS A NZ  1 
ATOM   10   N N   . ASP A 1 12 ? 8.62928  36.81966 20.14551  1.000 62.03161  ? 58  ASP A N   1 
ATOM   11   C CA  . ASP A 1 12 ? 8.81875  35.64217 19.31107  1.000 55.88490  ? 58  ASP A CA  1 
ATOM   12   C C   . ASP A 1 12 ? 10.23423 35.11790 19.46635  1.000 49.17558  ? 58  ASP A C   1 
ATOM   13   O O   . ASP A 1 12 ? 11.19069 35.88794 19.58318  1.000 49.38187  ? 58  ASP A O   1 
ATOM   14   C CB  . ASP A 1 12 ? 8.54006  35.95601 17.84297  1.000 52.85613  ? 58  ASP A CB  1 
ATOM   15   C CG  . ASP A 1 12 ? 7.06899  36.16458 17.56793  1.000 64.89060  ? 58  ASP A CG  1 
ATOM   16   O OD1 . ASP A 1 12 ? 6.65944  37.32995 17.36013  1.000 66.92935  ? 58  ASP A OD1 1 
ATOM   17   O OD2 . ASP A 1 12 ? 6.32428  35.15708 17.55429  1.000 65.59686  ? 58  ASP A OD2 1 
ATOM   18   N N   . THR A 1 13 ? 10.35809 33.80487 19.46436  1.000 43.32793  ? 59  THR A N   1 
ATOM   19   C CA  . THR A 1 13 ? 11.65717 33.17110 19.57980  1.000 37.21523  ? 59  THR A CA  1 
ATOM   20   C C   . THR A 1 13 ? 12.48934 33.50529 18.34977  1.000 33.01616  ? 59  THR A C   1 
ATOM   21   O O   . THR A 1 13 ? 12.03731 33.25554 17.22511  1.000 28.86781  ? 59  THR A O   1 
ATOM   22   C CB  . THR A 1 13 ? 11.47497 31.66196 19.72025  1.000 37.84101  ? 59  THR A CB  1 
ATOM   23   O OG1 . THR A 1 13 ? 10.75207 31.37582 20.92565  1.000 38.22171  ? 59  THR A OG1 1 
ATOM   24   C CG2 . THR A 1 13 ? 12.82315 30.94384 19.72721  1.000 32.39586  ? 59  THR A CG2 1 
ATOM   25   N N   . PRO A 1 14 ? 13.68419 34.07229 18.49793  1.000 30.45319  ? 60  PRO A N   1 
ATOM   26   C CA  . PRO A 1 14 ? 14.54372 34.25886 17.31952  1.000 27.98321  ? 60  PRO A CA  1 
ATOM   27   C C   . PRO A 1 14 ? 14.89284 32.90977 16.71066  1.000 24.45442  ? 60  PRO A C   1 
ATOM   28   O O   . PRO A 1 14 ? 15.28474 31.98151 17.40980  1.000 24.53176  ? 60  PRO A O   1 
ATOM   29   C CB  . PRO A 1 14 ? 15.78159 34.96537 17.88538  1.000 30.79331  ? 60  PRO A CB  1 
ATOM   30   C CG  . PRO A 1 14 ? 15.31661 35.55721 19.23208  1.000 29.56994  ? 60  PRO A CG  1 
ATOM   31   C CD  . PRO A 1 14 ? 14.30362 34.57567 19.73908  1.000 31.42279  ? 60  PRO A CD  1 
ATOM   32   N N   . PHE A 1 15 ? 14.75117 32.79676 15.39578  1.000 22.08234  ? 61  PHE A N   1 
ATOM   33   C CA  . PHE A 1 15 ? 15.00556 31.52898 14.74427  1.000 20.61100  ? 61  PHE A CA  1 
ATOM   34   C C   . PHE A 1 15 ? 15.76743 31.75964 13.45016  1.000 19.85689  ? 61  PHE A C   1 
ATOM   35   O O   . PHE A 1 15 ? 15.73082 32.84578 12.85312  1.000 19.64698  ? 61  PHE A O   1 
ATOM   36   C CB  . PHE A 1 15 ? 13.70755 30.75358 14.45775  1.000 19.50346  ? 61  PHE A CB  1 
ATOM   37   C CG  . PHE A 1 15 ? 12.84360 31.38190 13.38795  1.000 21.08679  ? 61  PHE A CG  1 
ATOM   38   C CD1 . PHE A 1 15 ? 13.11992 31.19160 12.04350  1.000 22.12756  ? 61  PHE A CD1 1 
ATOM   39   C CD2 . PHE A 1 15 ? 11.75483 32.17044 13.73997  1.000 24.43811  ? 61  PHE A CD2 1 
ATOM   40   C CE1 . PHE A 1 15 ? 12.32772 31.77903 11.05689  1.000 19.82458  ? 61  PHE A CE1 1 
ATOM   41   C CE2 . PHE A 1 15 ? 10.94968 32.76075 12.76202  1.000 23.63542  ? 61  PHE A CE2 1 
ATOM   42   C CZ  . PHE A 1 15 ? 11.24957 32.56757 11.41935  1.000 21.46678  ? 61  PHE A CZ  1 
ATOM   43   N N   . MET A 1 16 ? 16.44843 30.70121 13.02223  1.000 19.68340  ? 62  MET A N   1 
ATOM   44   C CA  . MET A 1 16 ? 16.96740 30.61063 11.66548  1.000 20.57425  ? 62  MET A CA  1 
ATOM   45   C C   . MET A 1 16 ? 16.70755 29.18419 11.20648  1.000 17.13019  ? 62  MET A C   1 
ATOM   46   O O   . MET A 1 16 ? 17.08289 28.24000 11.89507  1.000 19.30624  ? 62  MET A O   1 
ATOM   47   C CB  . MET A 1 16 ? 18.45035 31.01654 11.62351  1.000 20.65473  ? 62  MET A CB  1 
ATOM   48   C CG  . MET A 1 16 ? 19.25776 30.63665 10.38298  1.000 24.46968  ? 62  MET A CG  1 
ATOM   49   S SD  . MET A 1 16 ? 21.02908 31.12275 10.57996  1.000 39.84706  ? 62  MET A SD  1 
ATOM   50   C CE  . MET A 1 16 ? 20.89938 32.47380 11.71861  1.000 26.44777  ? 62  MET A CE  1 
ATOM   51   N N   . VAL A 1 17 ? 15.99555 29.02591 10.08937  1.000 17.15762  ? 63  VAL A N   1 
ATOM   52   C CA  . VAL A 1 17 ? 15.60604 27.72099 9.56588   1.000 15.85729  ? 63  VAL A CA  1 
ATOM   53   C C   . VAL A 1 17 ? 16.28796 27.55041 8.21645   1.000 15.23012  ? 63  VAL A C   1 
ATOM   54   O O   . VAL A 1 17 ? 16.18301 28.42350 7.34777   1.000 15.57958  ? 63  VAL A O   1 
ATOM   55   C CB  . VAL A 1 17 ? 14.07201 27.58207 9.41335   1.000 17.91053  ? 63  VAL A CB  1 
ATOM   56   C CG1 . VAL A 1 17 ? 13.71725 26.25137 8.73988   1.000 17.33603  ? 63  VAL A CG1 1 
ATOM   57   C CG2 . VAL A 1 17 ? 13.35536 27.69212 10.75569  1.000 19.45048  ? 63  VAL A CG2 1 
ATOM   58   N N   . GLN A 1 18 ? 17.02357 26.46411 8.05574   1.000 15.09444  ? 64  GLN A N   1 
ATOM   59   C CA  . GLN A 1 18 ? 17.65951 26.13133 6.78205   1.000 14.43423  ? 64  GLN A CA  1 
ATOM   60   C C   . GLN A 1 18 ? 17.00889 24.86881 6.24014   1.000 16.04148  ? 64  GLN A C   1 
ATOM   61   O O   . GLN A 1 18 ? 17.02802 23.83262 6.90875   1.000 15.89174  ? 64  GLN A O   1 
ATOM   62   C CB  . GLN A 1 18 ? 19.16075 25.92164 6.96435   1.000 15.14276  ? 64  GLN A CB  1 
ATOM   63   C CG  . GLN A 1 18 ? 19.90843 25.45836 5.67844   1.000 17.03531  ? 64  GLN A CG  1 
ATOM   64   C CD  . GLN A 1 18 ? 21.38682 25.60967 5.82858   1.000 19.80987  ? 64  GLN A CD  1 
ATOM   65   O OE1 . GLN A 1 18 ? 21.83950 26.47323 6.58073   1.000 18.29231  ? 64  GLN A OE1 1 
ATOM   66   N NE2 . GLN A 1 18 ? 22.16669 24.77167 5.12701   1.000 22.57250  ? 64  GLN A NE2 1 
ATOM   67   N N   . VAL A 1 19 ? 16.44675 24.94145 5.03184   1.000 15.16933  ? 65  VAL A N   1 
ATOM   68   C CA  . VAL A 1 19 ? 15.82118 23.77024 4.43763   1.000 15.42801  ? 65  VAL A CA  1 
ATOM   69   C C   . VAL A 1 19 ? 16.42607 23.51773 3.06808   1.000 17.25333  ? 65  VAL A C   1 
ATOM   70   O O   . VAL A 1 19 ? 16.85576 24.44778 2.37263   1.000 16.06619  ? 65  VAL A O   1 
ATOM   71   C CB  . VAL A 1 19 ? 14.28393 23.90207 4.31497   1.000 16.15251  ? 65  VAL A CB  1 
ATOM   72   C CG1 . VAL A 1 19 ? 13.61850 23.85452 5.69768   1.000 17.68817  ? 65  VAL A CG1 1 
ATOM   73   C CG2 . VAL A 1 19 ? 13.90801 25.16019 3.53080   1.000 16.54307  ? 65  VAL A CG2 1 
ATOM   74   N N   . LYS A 1 20 ? 16.43311 22.25161 2.66696   1.000 16.86185  ? 66  LYS A N   1 
ATOM   75   C CA  . LYS A 1 20 ? 16.94357 21.86226 1.35443   1.000 18.41485  ? 66  LYS A CA  1 
ATOM   76   C C   . LYS A 1 20 ? 15.73179 21.64533 0.44844   1.000 20.99565  ? 66  LYS A C   1 
ATOM   77   O O   . LYS A 1 20 ? 14.84413 20.85576 0.78236   1.000 19.31117  ? 66  LYS A O   1 
ATOM   78   C CB  . LYS A 1 20 ? 17.79441 20.59726 1.45917   1.000 21.23745  ? 66  LYS A CB  1 
ATOM   79   C CG  . LYS A 1 20 ? 18.22100 19.97677 0.12464   1.000 27.68493  ? 66  LYS A CG  1 
ATOM   80   C CD  . LYS A 1 20 ? 18.65427 21.02017 -0.91513  1.000 29.19406  ? 66  LYS A CD  1 
ATOM   81   C CE  . LYS A 1 20 ? 19.04304 20.37582 -2.25972  1.000 28.68759  ? 66  LYS A CE  1 
ATOM   82   N NZ  . LYS A 1 20 ? 17.95838 19.46600 -2.82710  1.000 33.85375  ? 66  LYS A NZ  1 
ATOM   83   N N   . LEU A 1 21 ? 15.69400 22.34288 -0.69275  1.000 19.22039  ? 67  LEU A N   1 
ATOM   84   C CA  . LEU A 1 21 ? 14.55426 22.26346 -1.60076  1.000 18.61242  ? 67  LEU A CA  1 
ATOM   85   C C   . LEU A 1 21 ? 14.98598 21.67057 -2.93763  1.000 20.43788  ? 67  LEU A C   1 
ATOM   86   O O   . LEU A 1 21 ? 16.13217 21.85259 -3.34704  1.000 20.84160  ? 67  LEU A O   1 
ATOM   87   C CB  . LEU A 1 21 ? 13.94803 23.65276 -1.83108  1.000 17.71447  ? 67  LEU A CB  1 
ATOM   88   C CG  . LEU A 1 21 ? 13.41923 24.36519 -0.57614  1.000 17.86399  ? 67  LEU A CG  1 
ATOM   89   C CD1 . LEU A 1 21 ? 12.98729 25.79118 -0.88511  1.000 16.82405  ? 67  LEU A CD1 1 
ATOM   90   C CD2 . LEU A 1 21 ? 12.27492 23.58829 0.06115   1.000 18.79486  ? 67  LEU A CD2 1 
ATOM   91   N N   . PRO A 1 22 ? 14.08897 20.98352 -3.65799  1.000 21.53305  ? 68  PRO A N   1 
ATOM   92   C CA  . PRO A 1 22 ? 14.47693 20.42739 -4.96352  1.000 21.53013  ? 68  PRO A CA  1 
ATOM   93   C C   . PRO A 1 22 ? 14.45254 21.49566 -6.03947  1.000 22.13019  ? 68  PRO A C   1 
ATOM   94   O O   . PRO A 1 22 ? 14.27081 22.68304 -5.73698  1.000 19.99751  ? 68  PRO A O   1 
ATOM   95   C CB  . PRO A 1 22 ? 13.40190 19.36642 -5.22291  1.000 23.22123  ? 68  PRO A CB  1 
ATOM   96   C CG  . PRO A 1 22 ? 12.17373 19.99482 -4.60152  1.000 23.06946  ? 68  PRO A CG  1 
ATOM   97   C CD  . PRO A 1 22 ? 12.69182 20.65640 -3.32267  1.000 21.28093  ? 68  PRO A CD  1 
ATOM   98   N N   . ASN A 1 23 ? 14.60529 21.08445 -7.29980  1.000 21.98781  ? 69  ASN A N   1 
ATOM   99   C CA  . ASN A 1 23 ? 14.41476 22.02129 -8.39334  1.000 25.30947  ? 69  ASN A CA  1 
ATOM   100  C C   . ASN A 1 23 ? 13.01633 22.61561 -8.28824  1.000 24.21442  ? 69  ASN A C   1 
ATOM   101  O O   . ASN A 1 23 ? 12.08864 21.97455 -7.80469  1.000 23.84412  ? 69  ASN A O   1 
ATOM   102  C CB  . ASN A 1 23 ? 14.62038 21.32866 -9.74495  1.000 27.97522  ? 69  ASN A CB  1 
ATOM   103  C CG  . ASN A 1 23 ? 16.08294 20.96830 -9.99538  1.000 31.62694  ? 69  ASN A CG  1 
ATOM   104  O OD1 . ASN A 1 23 ? 16.98816 21.58424 -9.43414  1.000 27.34715  ? 69  ASN A OD1 1 
ATOM   105  N ND2 . ASN A 1 23 ? 16.31414 19.95540 -10.82160 1.000 34.67927  ? 69  ASN A ND2 1 
ATOM   106  N N   . TYR A 1 24 ? 12.89646 23.87513 -8.69882  1.000 25.53871  ? 70  TYR A N   1 
ATOM   107  C CA  . TYR A 1 24 ? 11.63948 24.61194 -8.58731  1.000 26.84814  ? 70  TYR A CA  1 
ATOM   108  C C   . TYR A 1 24 ? 10.45807 23.85694 -9.19503  1.000 27.50463  ? 70  TYR A C   1 
ATOM   109  O O   . TYR A 1 24 ? 9.36212  23.82938 -8.61785  1.000 27.63580  ? 70  TYR A O   1 
ATOM   110  C CB  . TYR A 1 24 ? 11.81186 25.97220 -9.26485  1.000 28.94199  ? 70  TYR A CB  1 
ATOM   111  C CG  . TYR A 1 24 ? 10.58599 26.85756 -9.22394  1.000 28.84935  ? 70  TYR A CG  1 
ATOM   112  C CD1 . TYR A 1 24 ? 10.19516 27.48793 -8.04500  1.000 26.49671  ? 70  TYR A CD1 1 
ATOM   113  C CD2 . TYR A 1 24 ? 9.83430  27.07023 -10.36811 1.000 31.03980  ? 70  TYR A CD2 1 
ATOM   114  C CE1 . TYR A 1 24 ? 9.08058  28.29719 -8.01567  1.000 28.44082  ? 70  TYR A CE1 1 
ATOM   115  C CE2 . TYR A 1 24 ? 8.73208  27.88439 -10.34789 1.000 32.17861  ? 70  TYR A CE2 1 
ATOM   116  C CZ  . TYR A 1 24 ? 8.36309  28.49681 -9.17393  1.000 28.05497  ? 70  TYR A CZ  1 
ATOM   117  O OH  . TYR A 1 24 ? 7.26277  29.30461 -9.17859  1.000 33.85020  ? 70  TYR A OH  1 
ATOM   118  N N   . LYS A 1 25 ? 10.65701 23.22116 -10.35611 1.000 31.77545  ? 71  LYS A N   1 
ATOM   119  C CA  . LYS A 1 25 ? 9.52287  22.58812 -11.01675 1.000 31.11780  ? 71  LYS A CA  1 
ATOM   120  C C   . LYS A 1 25 ? 9.03172  21.36426 -10.25891 1.000 31.64590  ? 71  LYS A C   1 
ATOM   121  O O   . LYS A 1 25 ? 7.83039  21.07357 -10.28463 1.000 32.88561  ? 71  LYS A O   1 
ATOM   122  C CB  . LYS A 1 25 ? 9.86657  22.21778 -12.45752 1.000 36.22409  ? 71  LYS A CB  1 
ATOM   123  C CG  . LYS A 1 25 ? 9.92591  23.42795 -13.39696 1.000 43.98914  ? 71  LYS A CG  1 
ATOM   124  C CD  . LYS A 1 25 ? 8.71320  24.35340 -13.18051 1.000 45.64930  ? 71  LYS A CD  1 
ATOM   125  C CE  . LYS A 1 25 ? 7.39192  23.72909 -13.64264 1.000 49.95149  ? 71  LYS A CE  1 
ATOM   126  N NZ  . LYS A 1 25 ? 6.28439  24.72620 -13.62695 1.000 51.52590  ? 71  LYS A NZ  1 
ATOM   127  N N   . ASP A 1 26 ? 9.92962  20.64536 -9.57362  1.000 32.13393  ? 72  ASP A N   1 
ATOM   128  C CA  . ASP A 1 26 ? 9.51004  19.51195 -8.74972  1.000 29.39160  ? 72  ASP A CA  1 
ATOM   129  C C   . ASP A 1 26 ? 8.88921  19.98656 -7.44483  1.000 29.38762  ? 72  ASP A C   1 
ATOM   130  O O   . ASP A 1 26 ? 7.90749  19.40252 -6.97268  1.000 29.53533  ? 72  ASP A O   1 
ATOM   131  C CB  . ASP A 1 26 ? 10.70009 18.58444 -8.45002  1.000 31.58791  ? 72  ASP A CB  1 
ATOM   132  C CG  . ASP A 1 26 ? 11.36582 18.03246 -9.70439  1.000 33.83511  ? 72  ASP A CG  1 
ATOM   133  O OD1 . ASP A 1 26 ? 10.66280 17.54377 -10.61122 1.000 37.23402  ? 72  ASP A OD1 1 
ATOM   134  O OD2 . ASP A 1 26 ? 12.61083 18.05061 -9.76391  1.000 40.24294  ? 72  ASP A OD2 1 
ATOM   135  N N   . TYR A 1 27 ? 9.44881  21.05062 -6.86104  1.000 26.19282  ? 73  TYR A N   1 
ATOM   136  C CA  . TYR A 1 27 ? 8.90485  21.64029 -5.63821  1.000 26.49004  ? 73  TYR A CA  1 
ATOM   137  C C   . TYR A 1 27 ? 7.43738  21.99440 -5.79424  1.000 26.20025  ? 73  TYR A C   1 
ATOM   138  O O   . TYR A 1 27 ? 6.63762  21.79173 -4.87251  1.000 24.51868  ? 73  TYR A O   1 
ATOM   139  C CB  . TYR A 1 27 ? 9.71450  22.88764 -5.28061  1.000 23.46032  ? 73  TYR A CB  1 
ATOM   140  C CG  . TYR A 1 27 ? 9.00407  23.98302 -4.51691  1.000 21.49450  ? 73  TYR A CG  1 
ATOM   141  C CD1 . TYR A 1 27 ? 8.95678  23.97176 -3.11453  1.000 21.43532  ? 73  TYR A CD1 1 
ATOM   142  C CD2 . TYR A 1 27 ? 8.44959  25.07323 -5.18151  1.000 20.38749  ? 73  TYR A CD2 1 
ATOM   143  C CE1 . TYR A 1 27 ? 8.32998  25.00891 -2.39713  1.000 17.10591  ? 73  TYR A CE1 1 
ATOM   144  C CE2 . TYR A 1 27 ? 7.84334  26.10379 -4.48091  1.000 21.13258  ? 73  TYR A CE2 1 
ATOM   145  C CZ  . TYR A 1 27 ? 7.79229  26.06945 -3.08797  1.000 19.28420  ? 73  TYR A CZ  1 
ATOM   146  O OH  . TYR A 1 27 ? 7.16512  27.09133 -2.39307  1.000 21.40554  ? 73  TYR A OH  1 
ATOM   147  N N   . LEU A 1 28 ? 7.07066  22.55898 -6.94742  1.000 25.73353  ? 74  LEU A N   1 
ATOM   148  C CA  . LEU A 1 28 ? 5.69320  22.96759 -7.17966  1.000 28.69867  ? 74  LEU A CA  1 
ATOM   149  C C   . LEU A 1 28 ? 4.71633  21.80318 -7.09105  1.000 31.06237  ? 74  LEU A C   1 
ATOM   150  O O   . LEU A 1 28 ? 3.53133  22.02877 -6.83683  1.000 30.30883  ? 74  LEU A O   1 
ATOM   151  C CB  . LEU A 1 28 ? 5.55802  23.63201 -8.55192  1.000 31.03456  ? 74  LEU A CB  1 
ATOM   152  C CG  . LEU A 1 28 ? 6.14447  25.02854 -8.75388  1.000 30.47954  ? 74  LEU A CG  1 
ATOM   153  C CD1 . LEU A 1 28 ? 5.83510  25.53521 -10.16210 1.000 33.10577  ? 74  LEU A CD1 1 
ATOM   154  C CD2 . LEU A 1 28 ? 5.65235  26.01125 -7.69613  1.000 32.29245  ? 74  LEU A CD2 1 
ATOM   155  N N   . LEU A 1 29 ? 5.17230  20.57437 -7.32563  1.000 31.36951  ? 75  LEU A N   1 
ATOM   156  C CA  . LEU A 1 29 ? 4.32021  19.39206 -7.26479  1.000 29.24032  ? 75  LEU A CA  1 
ATOM   157  C C   . LEU A 1 29 ? 4.19270  18.80166 -5.86446  1.000 31.52830  ? 75  LEU A C   1 
ATOM   158  O O   . LEU A 1 29 ? 3.38517  17.88809 -5.67608  1.000 33.73424  ? 75  LEU A O   1 
ATOM   159  C CB  . LEU A 1 29 ? 4.87714  18.31311 -8.19481  1.000 31.16776  ? 75  LEU A CB  1 
ATOM   160  C CG  . LEU A 1 29 ? 5.17518  18.76058 -9.62146  1.000 36.33521  ? 75  LEU A CG  1 
ATOM   161  C CD1 . LEU A 1 29 ? 5.93392  17.66601 -10.37809 1.000 34.80524  ? 75  LEU A CD1 1 
ATOM   162  C CD2 . LEU A 1 29 ? 3.89086  19.13105 -10.32862 1.000 35.17261  ? 75  LEU A CD2 1 
ATOM   163  N N   . ASP A 1 30 ? 4.98562  19.27826 -4.89750  1.000 28.04168  ? 76  ASP A N   1 
ATOM   164  C CA  . ASP A 1 30 ? 5.00031  18.78793 -3.51339  1.000 27.46847  ? 76  ASP A CA  1 
ATOM   165  C C   . ASP A 1 30 ? 4.21170  19.77417 -2.65807  1.000 25.76992  ? 76  ASP A C   1 
ATOM   166  O O   . ASP A 1 30 ? 4.76192  20.74299 -2.12577  1.000 22.51246  ? 76  ASP A O   1 
ATOM   167  C CB  . ASP A 1 30 ? 6.44675  18.63516 -3.02619  1.000 25.53661  ? 76  ASP A CB  1 
ATOM   168  C CG  . ASP A 1 30 ? 6.56002  17.89443 -1.69042  1.000 28.89191  ? 76  ASP A CG  1 
ATOM   169  O OD1 . ASP A 1 30 ? 5.57109  17.87029 -0.93041  1.000 28.49584  ? 76  ASP A OD1 1 
ATOM   170  O OD2 . ASP A 1 30 ? 7.64756  17.34961 -1.37859  1.000 28.14281  ? 76  ASP A OD2 1 
ATOM   171  N N   . ASN A 1 31 ? 2.90606  19.51498 -2.52388  1.000 24.96786  ? 77  ASN A N   1 
ATOM   172  C CA  . ASN A 1 31 ? 2.02004  20.45476 -1.84315  1.000 23.08577  ? 77  ASN A CA  1 
ATOM   173  C C   . ASN A 1 31 ? 2.43122  20.65549 -0.39613  1.000 21.17830  ? 77  ASN A C   1 
ATOM   174  O O   . ASN A 1 31 ? 2.31783  21.76194 0.13835   1.000 21.31942  ? 77  ASN A O   1 
ATOM   175  C CB  . ASN A 1 31 ? 0.56805  19.96653 -1.90110  1.000 24.75918  ? 77  ASN A CB  1 
ATOM   176  C CG  . ASN A 1 31 ? 0.04955  19.86920 -3.31732  1.000 28.90390  ? 77  ASN A CG  1 
ATOM   177  O OD1 . ASN A 1 31 ? -0.37647 18.79992 -3.76608  1.000 30.04264  ? 77  ASN A OD1 1 
ATOM   178  N ND2 . ASN A 1 31 ? 0.07995  20.98278 -4.03120  1.000 25.27125  ? 77  ASN A ND2 1 
ATOM   179  N N   . LYS A 1 32 ? 2.86244  19.58611 0.27169   1.000 23.81139  ? 78  LYS A N   1 
ATOM   180  C CA  . LYS A 1 32 ? 3.23675  19.71978 1.67042   1.000 24.37131  ? 78  LYS A CA  1 
ATOM   181  C C   . LYS A 1 32 ? 4.45153  20.62765 1.80904   1.000 23.77065  ? 78  LYS A C   1 
ATOM   182  O O   . LYS A 1 32 ? 4.52099  21.45533 2.72393   1.000 23.87022  ? 78  LYS A O   1 
ATOM   183  C CB  . LYS A 1 32 ? 3.48259  18.33137 2.26977   1.000 28.60507  ? 78  LYS A CB  1 
ATOM   184  C CG  . LYS A 1 32 ? 4.25487  18.33982 3.55578   1.000 32.87937  ? 78  LYS A CG  1 
ATOM   185  C CD  . LYS A 1 32 ? 5.00216  17.02673 3.76243   1.000 36.72779  ? 78  LYS A CD  1 
ATOM   186  C CE  . LYS A 1 32 ? 4.23646  16.10145 4.67280   1.000 43.31504  ? 78  LYS A CE  1 
ATOM   187  N NZ  . LYS A 1 32 ? 4.97720  15.79334 5.94416   1.000 50.15249  ? 78  LYS A NZ  1 
ATOM   188  N N   . GLN A 1 33 ? 5.39974  20.50762 0.87740   1.000 23.33394  ? 79  GLN A N   1 
ATOM   189  C CA  . GLN A 1 33 ? 6.59710  21.34452 0.87460   1.000 21.50478  ? 79  GLN A CA  1 
ATOM   190  C C   . GLN A 1 33 ? 6.27293  22.78858 0.50503   1.000 17.79053  ? 79  GLN A C   1 
ATOM   191  O O   . GLN A 1 33 ? 6.81892  23.71813 1.09923   1.000 20.00129  ? 79  GLN A O   1 
ATOM   192  C CB  . GLN A 1 33 ? 7.63546  20.74217 -0.07219  1.000 21.32331  ? 79  GLN A CB  1 
ATOM   193  C CG  . GLN A 1 33 ? 9.00903  21.36233 0.01689   1.000 21.85482  ? 79  GLN A CG  1 
ATOM   194  C CD  . GLN A 1 33 ? 9.97945  20.58305 -0.81958  1.000 24.20623  ? 79  GLN A CD  1 
ATOM   195  O OE1 . GLN A 1 33 ? 9.89738  20.60920 -2.04841  1.000 24.09907  ? 79  GLN A OE1 1 
ATOM   196  N NE2 . GLN A 1 33 ? 10.85474 19.82255 -0.17086  1.000 22.22405  ? 79  GLN A NE2 1 
ATOM   197  N N   . VAL A 1 34 ? 5.37593  23.00470 -0.45792  1.000 18.72289  ? 80  VAL A N   1 
ATOM   198  C CA  . VAL A 1 34 ? 4.93994  24.36760 -0.76341  1.000 19.91841  ? 80  VAL A CA  1 
ATOM   199  C C   . VAL A 1 34 ? 4.32596  25.03026 0.46949   1.000 20.02182  ? 80  VAL A C   1 
ATOM   200  O O   . VAL A 1 34 ? 4.65510  26.17584 0.81124   1.000 19.56792  ? 80  VAL A O   1 
ATOM   201  C CB  . VAL A 1 34 ? 3.93666  24.36283 -1.92949  1.000 20.24293  ? 80  VAL A CB  1 
ATOM   202  C CG1 . VAL A 1 34 ? 3.25779  25.72571 -2.05076  1.000 21.41194  ? 80  VAL A CG1 1 
ATOM   203  C CG2 . VAL A 1 34 ? 4.60883  23.98089 -3.22453  1.000 22.40442  ? 80  VAL A CG2 1 
ATOM   204  N N   . VAL A 1 35 ? 3.39070  24.34233 1.12929   1.000 20.38589  ? 81  VAL A N   1 
ATOM   205  C CA  . VAL A 1 35 ? 2.74387  24.91994 2.31461   1.000 19.35479  ? 81  VAL A CA  1 
ATOM   206  C C   . VAL A 1 35 ? 3.79152  25.21503 3.39037   1.000 21.41471  ? 81  VAL A C   1 
ATOM   207  O O   . VAL A 1 35 ? 3.80174  26.29681 3.99471   1.000 20.89262  ? 81  VAL A O   1 
ATOM   208  C CB  . VAL A 1 35 ? 1.63688  23.97815 2.82952   1.000 23.39785  ? 81  VAL A CB  1 
ATOM   209  C CG1 . VAL A 1 35 ? 1.19124  24.36785 4.22883   1.000 26.32912  ? 81  VAL A CG1 1 
ATOM   210  C CG2 . VAL A 1 35 ? 0.39659  23.96815 1.86388   1.000 22.63496  ? 81  VAL A CG2 1 
ATOM   211  N N   . LEU A 1 36 ? 4.73383  24.29324 3.59770   1.000 21.79780  ? 82  LEU A N   1 
ATOM   212  C CA  . LEU A 1 36 ? 5.75813  24.52726 4.62113   1.000 23.69065  ? 82  LEU A CA  1 
ATOM   213  C C   . LEU A 1 36 ? 6.58524  25.77245 4.29310   1.000 21.24554  ? 82  LEU A C   1 
ATOM   214  O O   . LEU A 1 36 ? 6.82320  26.60990 5.16984   1.000 21.13735  ? 82  LEU A O   1 
ATOM   215  C CB  . LEU A 1 36 ? 6.64677  23.27793 4.77083   1.000 22.83284  ? 82  LEU A CB  1 
ATOM   216  C CG  . LEU A 1 36 ? 7.99385  23.32318 5.53361   1.000 26.51363  ? 82  LEU A CG  1 
ATOM   217  C CD1 . LEU A 1 36 ? 7.83483  23.81984 6.97129   1.000 29.98384  ? 82  LEU A CD1 1 
ATOM   218  C CD2 . LEU A 1 36 ? 8.64167  21.95107 5.54153   1.000 26.73167  ? 82  LEU A CD2 1 
ATOM   219  N N   . THR A 1 37 ? 7.00604  25.94217 3.02993   1.000 17.66443  ? 83  THR A N   1 
ATOM   220  C CA  . THR A 1 37 ? 7.82333  27.11752 2.72375   1.000 19.03154  ? 83  THR A CA  1 
ATOM   221  C C   . THR A 1 37 ? 7.04731  28.40607 2.93159   1.000 19.34947  ? 83  THR A C   1 
ATOM   222  O O   . THR A 1 37 ? 7.63405  29.42477 3.30620   1.000 18.80994  ? 83  THR A O   1 
ATOM   223  C CB  . THR A 1 37 ? 8.38441  27.08773 1.29823   1.000 17.95940  ? 83  THR A CB  1 
ATOM   224  O OG1 . THR A 1 37 ? 7.31114  27.06203 0.33906   1.000 19.50537  ? 83  THR A OG1 1 
ATOM   225  C CG2 . THR A 1 37 ? 9.33163  25.88712 1.09059   1.000 19.62126  ? 83  THR A CG2 1 
ATOM   226  N N   . PHE A 1 38 ? 5.74073  28.40428 2.66945   1.000 17.45480  ? 84  PHE A N   1 
ATOM   227  C CA  . PHE A 1 38 ? 4.99504  29.62949 2.89754   1.000 19.77955  ? 84  PHE A CA  1 
ATOM   228  C C   . PHE A 1 38 ? 4.74954  29.87502 4.37966   1.000 19.47598  ? 84  PHE A C   1 
ATOM   229  O O   . PHE A 1 38 ? 4.69805  31.03207 4.79650   1.000 21.11165  ? 84  PHE A O   1 
ATOM   230  C CB  . PHE A 1 38 ? 3.69335  29.61781 2.09827   1.000 21.66219  ? 84  PHE A CB  1 
ATOM   231  C CG  . PHE A 1 38 ? 3.91175  30.09351 0.70940   1.000 24.19734  ? 84  PHE A CG  1 
ATOM   232  C CD1 . PHE A 1 38 ? 4.01385  31.44951 0.43899   1.000 22.76758  ? 84  PHE A CD1 1 
ATOM   233  C CD2 . PHE A 1 38 ? 4.18803  29.18779 -0.29420  1.000 24.26015  ? 84  PHE A CD2 1 
ATOM   234  C CE1 . PHE A 1 38 ? 4.28334  31.88960 -0.85014  1.000 24.13197  ? 84  PHE A CE1 1 
ATOM   235  C CE2 . PHE A 1 38 ? 4.45999  29.62035 -1.57218  1.000 23.76362  ? 84  PHE A CE2 1 
ATOM   236  C CZ  . PHE A 1 38 ? 4.51164  30.97543 -1.84616  1.000 24.01186  ? 84  PHE A CZ  1 
ATOM   237  N N   . LYS A 1 39 ? 4.58941  28.82535 5.18818   1.000 18.12100  ? 85  LYS A N   1 
ATOM   238  C CA  . LYS A 1 39 ? 4.58987  29.06120 6.62690   1.000 18.21918  ? 85  LYS A CA  1 
ATOM   239  C C   . LYS A 1 39 ? 5.89613  29.70291 7.07237   1.000 18.72506  ? 85  LYS A C   1 
ATOM   240  O O   . LYS A 1 39 ? 5.87574  30.65851 7.85202   1.000 21.52835  ? 85  LYS A O   1 
ATOM   241  C CB  . LYS A 1 39 ? 4.31346  27.77732 7.41939   1.000 21.92167  ? 85  LYS A CB  1 
ATOM   242  C CG  . LYS A 1 39 ? 2.98316  27.10891 7.09551   1.000 29.28978  ? 85  LYS A CG  1 
ATOM   243  C CD  . LYS A 1 39 ? 2.66423  25.96164 8.06663   1.000 34.55048  ? 85  LYS A CD  1 
ATOM   244  C CE  . LYS A 1 39 ? 1.37183  25.24452 7.67434   1.000 39.57240  ? 85  LYS A CE  1 
ATOM   245  N NZ  . LYS A 1 39 ? 1.32877  23.81899 8.10737   1.000 44.83234  ? 85  LYS A NZ  1 
ATOM   246  N N   . LEU A 1 40 ? 7.03405  29.25474 6.52658   1.000 19.40614  ? 86  LEU A N   1 
ATOM   247  C CA  . LEU A 1 40 ? 8.31325  29.89972 6.84292   1.000 21.39869  ? 86  LEU A CA  1 
ATOM   248  C C   . LEU A 1 40 ? 8.30904  31.36540 6.43303   1.000 19.14928  ? 86  LEU A C   1 
ATOM   249  O O   . LEU A 1 40 ? 8.69262  32.24002 7.21258   1.000 19.72753  ? 86  LEU A O   1 
ATOM   250  C CB  . LEU A 1 40 ? 9.47272  29.17774 6.15535   1.000 18.98788  ? 86  LEU A CB  1 
ATOM   251  C CG  . LEU A 1 40 ? 9.97256  27.89323 6.77379   1.000 22.38094  ? 86  LEU A CG  1 
ATOM   252  C CD1 . LEU A 1 40 ? 11.22136 27.42293 5.97935   1.000 19.27576  ? 86  LEU A CD1 1 
ATOM   253  C CD2 . LEU A 1 40 ? 10.31307 28.12018 8.26256   1.000 22.98030  ? 86  LEU A CD2 1 
ATOM   254  N N   . VAL A 1 41 ? 7.91650  31.64458 5.18755   1.000 18.80628  ? 87  VAL A N   1 
ATOM   255  C CA  . VAL A 1 41 ? 7.87583  33.01908 4.68550   1.000 19.13371  ? 87  VAL A CA  1 
ATOM   256  C C   . VAL A 1 41 ? 7.02653  33.90833 5.58724   1.000 20.54891  ? 87  VAL A C   1 
ATOM   257  O O   . VAL A 1 41 ? 7.42050  35.02527 5.93259   1.000 20.84252  ? 87  VAL A O   1 
ATOM   258  C CB  . VAL A 1 41 ? 7.34652  33.03694 3.24118   1.000 21.63367  ? 87  VAL A CB  1 
ATOM   259  C CG1 . VAL A 1 41 ? 6.97974  34.45037 2.83645   1.000 21.82204  ? 87  VAL A CG1 1 
ATOM   260  C CG2 . VAL A 1 41 ? 8.40354  32.43119 2.29195   1.000 18.42548  ? 87  VAL A CG2 1 
ATOM   261  N N   . HIS A 1 42 ? 5.84610  33.42121 5.97679   1.000 21.81371  ? 88  HIS A N   1 
ATOM   262  C CA  . HIS A 1 42 ? 4.90187  34.20628 6.77291   1.000 22.94716  ? 88  HIS A CA  1 
ATOM   263  C C   . HIS A 1 42 ? 5.47462  34.64332 8.11779   1.000 23.40340  ? 88  HIS A C   1 
ATOM   264  O O   . HIS A 1 42 ? 4.96909  35.59814 8.71473   1.000 26.76134  ? 88  HIS A O   1 
ATOM   265  C CB  . HIS A 1 42 ? 3.63237  33.38608 6.99626   1.000 24.22146  ? 88  HIS A CB  1 
ATOM   266  C CG  . HIS A 1 42 ? 2.80571  33.19226 5.75906   1.000 25.85272  ? 88  HIS A CG  1 
ATOM   267  N ND1 . HIS A 1 42 ? 1.86887  32.18798 5.63853   1.000 28.02260  ? 88  HIS A ND1 1 
ATOM   268  C CD2 . HIS A 1 42 ? 2.77272  33.87781 4.59165   1.000 27.30834  ? 88  HIS A CD2 1 
ATOM   269  C CE1 . HIS A 1 42 ? 1.30519  32.25170 4.44527   1.000 27.40727  ? 88  HIS A CE1 1 
ATOM   270  N NE2 . HIS A 1 42 ? 1.82937  33.27542 3.79393   1.000 28.51357  ? 88  HIS A NE2 1 
ATOM   271  N N   . HIS A 1 43 ? 6.49055  33.95447 8.62417   1.000 20.86967  ? 89  HIS A N   1 
ATOM   272  C CA  . HIS A 1 43 ? 7.07043  34.25233 9.92891   1.000 24.26305  ? 89  HIS A CA  1 
ATOM   273  C C   . HIS A 1 43 ? 8.43902  34.90853 9.83693   1.000 21.92733  ? 89  HIS A C   1 
ATOM   274  O O   . HIS A 1 43 ? 9.05257  35.16390 10.87494  1.000 23.93996  ? 89  HIS A O   1 
ATOM   275  C CB  . HIS A 1 43 ? 7.19913  32.96299 10.74047  1.000 26.98260  ? 89  HIS A CB  1 
ATOM   276  C CG  . HIS A 1 43 ? 5.90149  32.44798 11.26578  1.000 29.54373  ? 89  HIS A CG  1 
ATOM   277  N ND1 . HIS A 1 43 ? 5.50575  31.13699 11.10208  1.000 34.59382  ? 89  HIS A ND1 1 
ATOM   278  C CD2 . HIS A 1 43 ? 4.92625  33.04877 11.98635  1.000 33.08582  ? 89  HIS A CD2 1 
ATOM   279  C CE1 . HIS A 1 43 ? 4.32278  30.96427 11.66563  1.000 34.05968  ? 89  HIS A CE1 1 
ATOM   280  N NE2 . HIS A 1 43 ? 3.95133  32.10727 12.21172  1.000 34.11267  ? 89  HIS A NE2 1 
ATOM   281  N N   . SER A 1 44 ? 8.94199  35.17509 8.63388   1.000 21.97812  ? 90  SER A N   1 
ATOM   282  C CA  . SER A 1 44 ? 10.32203 35.60350 8.44783   1.000 20.94689  ? 90  SER A CA  1 
ATOM   283  C C   . SER A 1 44 ? 10.41029 37.09260 8.12778   1.000 24.38910  ? 90  SER A C   1 
ATOM   284  O O   . SER A 1 44 ? 9.46191  37.69958 7.62101   1.000 23.50887  ? 90  SER A O   1 
ATOM   285  C CB  . SER A 1 44 ? 10.98372 34.78442 7.33400   1.000 21.54131  ? 90  SER A CB  1 
ATOM   286  O OG  . SER A 1 44 ? 11.06543 33.43165 7.75948   1.000 24.52600  ? 90  SER A OG  1 
ATOM   287  N N   . LYS A 1 45 ? 11.57932 37.67128 8.43512   1.000 21.34272  ? 91  LYS A N   1 
ATOM   288  C CA  . LYS A 1 45 ? 11.95584 39.00909 7.99599   1.000 22.52344  ? 91  LYS A CA  1 
ATOM   289  C C   . LYS A 1 45 ? 13.07729 38.98445 6.97046   1.000 20.66136  ? 91  LYS A C   1 
ATOM   290  O O   . LYS A 1 45 ? 13.30471 39.99066 6.28548   1.000 20.80436  ? 91  LYS A O   1 
ATOM   291  C CB  . LYS A 1 45 ? 12.43794 39.85979 9.18551   1.000 24.55136  ? 91  LYS A CB  1 
ATOM   292  C CG  . LYS A 1 45 ? 11.47290 39.98718 10.37735  1.000 31.43177  ? 91  LYS A CG  1 
ATOM   293  C CD  . LYS A 1 45 ? 10.26611 40.88188 10.06899  1.000 31.23528  ? 91  LYS A CD  1 
ATOM   294  C CE  . LYS A 1 45 ? 9.14684  40.72671 11.11249  1.000 34.56694  ? 91  LYS A CE  1 
ATOM   295  N NZ  . LYS A 1 45 ? 7.94938  40.05089 10.49997  1.000 41.36081  ? 91  LYS A NZ  1 
ATOM   296  N N   . LYS A 1 46 ? 13.77171 37.85987 6.85239   1.000 18.62537  ? 92  LYS A N   1 
ATOM   297  C CA  . LYS A 1 46 ? 14.90873 37.69800 5.96470   1.000 18.74418  ? 92  LYS A CA  1 
ATOM   298  C C   . LYS A 1 46 ? 14.83797 36.31285 5.35655   1.000 17.29260  ? 92  LYS A C   1 
ATOM   299  O O   . LYS A 1 46 ? 14.60511 35.33565 6.07311   1.000 17.36966  ? 92  LYS A O   1 
ATOM   300  C CB  . LYS A 1 46 ? 16.22269 37.87680 6.73140   1.000 20.30929  ? 92  LYS A CB  1 
ATOM   301  C CG  . LYS A 1 46 ? 17.45961 37.84401 5.87275   1.000 27.41436  ? 92  LYS A CG  1 
ATOM   302  C CD  . LYS A 1 46 ? 18.67492 38.31725 6.68845   1.000 27.42707  ? 92  LYS A CD  1 
ATOM   303  C CE  . LYS A 1 46 ? 19.96999 37.85498 6.04069   1.000 32.25614  ? 92  LYS A CE  1 
ATOM   304  N NZ  . LYS A 1 46 ? 21.13725 38.36984 6.81323   1.000 33.04111  ? 92  LYS A NZ  1 
ATOM   305  N N   . ILE A 1 47 ? 15.00463 36.23361 4.04772   1.000 15.38306  ? 93  ILE A N   1 
ATOM   306  C CA  . ILE A 1 47 ? 15.07879 34.96436 3.34093   1.000 15.27965  ? 93  ILE A CA  1 
ATOM   307  C C   . ILE A 1 47 ? 16.28721 34.99629 2.40456   1.000 17.16626  ? 93  ILE A C   1 
ATOM   308  O O   . ILE A 1 47 ? 16.41381 35.90111 1.56994   1.000 16.21872  ? 93  ILE A O   1 
ATOM   309  C CB  . ILE A 1 47 ? 13.78211 34.67471 2.56738   1.000 15.74873  ? 93  ILE A CB  1 
ATOM   310  C CG1 . ILE A 1 47 ? 12.64243 34.40499 3.58016   1.000 18.22271  ? 93  ILE A CG1 1 
ATOM   311  C CG2 . ILE A 1 47 ? 13.97008 33.45431 1.66555   1.000 13.24329  ? 93  ILE A CG2 1 
ATOM   312  C CD1 . ILE A 1 47 ? 11.32177 34.47438 2.97296   1.000 22.87459  ? 93  ILE A CD1 1 
ATOM   313  N N   . THR A 1 48 ? 17.14928 33.99512 2.52642   1.000 14.66824  ? 94  THR A N   1 
ATOM   314  C CA  . THR A 1 48 ? 18.31272 33.80413 1.65825   1.000 15.80069  ? 94  THR A CA  1 
ATOM   315  C C   . THR A 1 48 ? 18.10809 32.53795 0.83048   1.000 14.52890  ? 94  THR A C   1 
ATOM   316  O O   . THR A 1 48 ? 17.70669 31.50264 1.37330   1.000 14.23301  ? 94  THR A O   1 
ATOM   317  C CB  . THR A 1 48 ? 19.60559 33.69059 2.48693   1.000 17.36980  ? 94  THR A CB  1 
ATOM   318  O OG1 . THR A 1 48 ? 19.75450 34.86054 3.29894   1.000 16.24652  ? 94  THR A OG1 1 
ATOM   319  C CG2 . THR A 1 48 ? 20.85623 33.55267 1.57169   1.000 15.46957  ? 94  THR A CG2 1 
ATOM   320  N N   . LEU A 1 49 ? 18.39426 32.61617 -0.46975  1.000 13.49688  ? 95  LEU A N   1 
ATOM   321  C CA  . LEU A 1 49 ? 18.28290 31.48520 -1.38262  1.000 12.22698  ? 95  LEU A CA  1 
ATOM   322  C C   . LEU A 1 49 ? 19.65393 31.21637 -2.00998  1.000 13.94912  ? 95  LEU A C   1 
ATOM   323  O O   . LEU A 1 49 ? 20.28350 32.13341 -2.54106  1.000 14.60956  ? 95  LEU A O   1 
ATOM   324  C CB  . LEU A 1 49 ? 17.22789 31.76407 -2.45809  1.000 13.93312  ? 95  LEU A CB  1 
ATOM   325  C CG  . LEU A 1 49 ? 15.79013 31.84873 -1.89714  1.000 14.94239  ? 95  LEU A CG  1 
ATOM   326  C CD1 . LEU A 1 49 ? 14.86109 32.70108 -2.79369  1.000 13.84662  ? 95  LEU A CD1 1 
ATOM   327  C CD2 . LEU A 1 49 ? 15.24574 30.44269 -1.68039  1.000 11.66325  ? 95  LEU A CD2 1 
ATOM   328  N N   . ILE A 1 50 ? 20.12258 29.97211 -1.92252  1.000 12.84395  ? 96  ILE A N   1 
ATOM   329  C CA  . ILE A 1 50 ? 21.48731 29.60059 -2.33941  1.000 14.51390  ? 96  ILE A CA  1 
ATOM   330  C C   . ILE A 1 50 ? 21.38353 28.51026 -3.39953  1.000 15.42706  ? 96  ILE A C   1 
ATOM   331  O O   . ILE A 1 50 ? 20.85313 27.42669 -3.12420  1.000 16.86103  ? 96  ILE A O   1 
ATOM   332  C CB  . ILE A 1 50 ? 22.31403 29.10058 -1.14734  1.000 14.99280  ? 96  ILE A CB  1 
ATOM   333  C CG1 . ILE A 1 50 ? 22.26673 30.10569 0.01930   1.000 14.28246  ? 96  ILE A CG1 1 
ATOM   334  C CG2 . ILE A 1 50 ? 23.74587 28.77726 -1.59126  1.000 16.75007  ? 96  ILE A CG2 1 
ATOM   335  C CD1 . ILE A 1 50 ? 22.88664 29.56238 1.34495   1.000 17.66760  ? 96  ILE A CD1 1 
ATOM   336  N N   . GLY A 1 51 ? 21.91735 28.76730 -4.58621  1.000 14.62329  ? 97  GLY A N   1 
ATOM   337  C CA  . GLY A 1 51 ? 21.85158 27.77455 -5.64882  1.000 15.21856  ? 97  GLY A CA  1 
ATOM   338  C C   . GLY A 1 51 ? 22.06915 28.44239 -6.99756  1.000 17.83987  ? 97  GLY A C   1 
ATOM   339  O O   . GLY A 1 51 ? 22.52471 29.57845 -7.07082  1.000 15.51991  ? 97  GLY A O   1 
ATOM   340  N N   . ASP A 1 52 ? 21.70939 27.71455 -8.05351  1.000 16.09380  ? 98  ASP A N   1 
ATOM   341  C CA  . ASP A 1 52 ? 21.84100 28.23490 -9.40731  1.000 17.83681  ? 98  ASP A CA  1 
ATOM   342  C C   . ASP A 1 52 ? 21.10053 29.56303 -9.52645  1.000 18.69606  ? 98  ASP A C   1 
ATOM   343  O O   . ASP A 1 52 ? 19.98119 29.70442 -9.03328  1.000 17.94738  ? 98  ASP A O   1 
ATOM   344  C CB  . ASP A 1 52 ? 21.22937 27.24158 -10.39182 1.000 18.76585  ? 98  ASP A CB  1 
ATOM   345  C CG  . ASP A 1 52 ? 21.13201 27.78911 -11.78487 1.000 23.30857  ? 98  ASP A CG  1 
ATOM   346  O OD1 . ASP A 1 52 ? 22.14553 27.77011 -12.51313 1.000 24.22087  ? 98  ASP A OD1 1 
ATOM   347  O OD2 . ASP A 1 52 ? 20.06557 28.35625 -12.11992 1.000 24.35269  ? 98  ASP A OD2 1 
ATOM   348  N N   . ALA A 1 53 ? 21.71872 30.53541 -10.20093 1.000 17.29927  ? 99  ALA A N   1 
ATOM   349  C CA  . ALA A 1 53 ? 21.14011 31.87681 -10.27764 1.000 18.27911  ? 99  ALA A CA  1 
ATOM   350  C C   . ALA A 1 53 ? 19.70996 31.85919 -10.83373 1.000 19.38670  ? 99  ALA A C   1 
ATOM   351  O O   . ALA A 1 53 ? 18.84407 32.61008 -10.36502 1.000 19.36111  ? 99  ALA A O   1 
ATOM   352  C CB  . ALA A 1 53 ? 22.03144 32.78239 -11.12885 1.000 23.41108  ? 99  ALA A CB  1 
ATOM   353  N N   . ASN A 1 54 ? 19.44612 31.04974 -11.86212 1.000 20.27219  ? 100 ASN A N   1 
ATOM   354  C CA  . ASN A 1 54 ? 18.09941 31.04003 -12.43111 1.000 21.57597  ? 100 ASN A CA  1 
ATOM   355  C C   . ASN A 1 54 ? 17.09697 30.40171 -11.48062 1.000 22.01488  ? 100 ASN A C   1 
ATOM   356  O O   . ASN A 1 54 ? 15.97876 30.90513 -11.32388 1.000 22.49840  ? 100 ASN A O   1 
ATOM   357  C CB  . ASN A 1 54 ? 18.09243 30.34147 -13.79990 1.000 23.81549  ? 100 ASN A CB  1 
ATOM   358  C CG  . ASN A 1 54 ? 18.78452 31.16583 -14.88025 1.000 33.35004  ? 100 ASN A CG  1 
ATOM   359  O OD1 . ASN A 1 54 ? 18.77230 32.40298 -14.83152 1.000 36.61715  ? 100 ASN A OD1 1 
ATOM   360  N ND2 . ASN A 1 54 ? 19.37993 30.49172 -15.86577 1.000 40.79890  ? 100 ASN A ND2 1 
ATOM   361  N N   . LYS A 1 55 ? 17.49544 29.32751 -10.80060 1.000 20.15789  ? 101 LYS A N   1 
ATOM   362  C CA  . LYS A 1 55 ? 16.59355 28.63960 -9.88545  1.000 18.78228  ? 101 LYS A CA  1 
ATOM   363  C C   . LYS A 1 55 ? 16.26231 29.49443 -8.65985  1.000 19.92325  ? 101 LYS A C   1 
ATOM   364  O O   . LYS A 1 55 ? 15.09635 29.58812 -8.26125  1.000 17.65705  ? 101 LYS A O   1 
ATOM   365  C CB  . LYS A 1 55 ? 17.20371 27.29952 -9.48440  1.000 18.00868  ? 101 LYS A CB  1 
ATOM   366  C CG  . LYS A 1 55 ? 17.33283 26.37782 -10.67087 1.000 21.49452  ? 101 LYS A CG  1 
ATOM   367  C CD  . LYS A 1 55 ? 18.08541 25.11112 -10.33669 1.000 22.69856  ? 101 LYS A CD  1 
ATOM   368  C CE  . LYS A 1 55 ? 18.08849 24.21258 -11.56380 1.000 30.83448  ? 101 LYS A CE  1 
ATOM   369  N NZ  . LYS A 1 55 ? 18.62786 22.88147 -11.25419 1.000 30.72851  ? 101 LYS A NZ  1 
ATOM   370  N N   . ILE A 1 56 ? 17.26577 30.12262 -8.03640  1.000 16.97338  ? 102 ILE A N   1 
ATOM   371  C CA  . ILE A 1 56 ? 16.94024 30.90008 -6.84075  1.000 15.69691  ? 102 ILE A CA  1 
ATOM   372  C C   . ILE A 1 56 ? 16.08552 32.10443 -7.21281  1.000 17.29441  ? 102 ILE A C   1 
ATOM   373  O O   . ILE A 1 56 ? 15.29684 32.59029 -6.39484  1.000 15.29807  ? 102 ILE A O   1 
ATOM   374  C CB  . ILE A 1 56 ? 18.20686 31.33598 -6.07647  1.000 14.67803  ? 102 ILE A CB  1 
ATOM   375  C CG1 . ILE A 1 56 ? 19.11864 32.22824 -6.93083  1.000 14.90365  ? 102 ILE A CG1 1 
ATOM   376  C CG2 . ILE A 1 56 ? 18.97470 30.11358 -5.55629  1.000 14.87298  ? 102 ILE A CG2 1 
ATOM   377  C CD1 . ILE A 1 56 ? 20.51713 32.49443 -6.28020  1.000 14.63510  ? 102 ILE A CD1 1 
ATOM   378  N N   . LEU A 1 57 ? 16.21336 32.60570 -8.44335  1.000 16.78903  ? 103 LEU A N   1 
ATOM   379  C CA  . LEU A 1 57 ? 15.34231 33.69751 -8.87606  1.000 18.92159  ? 103 LEU A CA  1 
ATOM   380  C C   . LEU A 1 57 ? 13.88832 33.24341 -9.01320  1.000 21.32474  ? 103 LEU A C   1 
ATOM   381  O O   . LEU A 1 57 ? 12.96680 33.98268 -8.64661  1.000 20.54880  ? 103 LEU A O   1 
ATOM   382  C CB  . LEU A 1 57 ? 15.84869 34.29284 -10.18952 1.000 20.67046  ? 103 LEU A CB  1 
ATOM   383  C CG  . LEU A 1 57 ? 15.00460 35.39926 -10.83746 1.000 22.86543  ? 103 LEU A CG  1 
ATOM   384  C CD1 . LEU A 1 57 ? 14.84173 36.59744 -9.89326  1.000 25.61730  ? 103 LEU A CD1 1 
ATOM   385  C CD2 . LEU A 1 57 ? 15.60952 35.84307 -12.16982 1.000 23.96519  ? 103 LEU A CD2 1 
ATOM   386  N N   . GLN A 1 58 ? 13.65477 32.05628 -9.56986  1.000 21.97614  ? 104 GLN A N   1 
ATOM   387  C CA  . GLN A 1 58 ? 12.29507 31.51947 -9.62219  1.000 22.55843  ? 104 GLN A CA  1 
ATOM   388  C C   . GLN A 1 58 ? 11.65198 31.49608 -8.23765  1.000 21.58590  ? 104 GLN A C   1 
ATOM   389  O O   . GLN A 1 58 ? 10.50351 31.92701 -8.05823  1.000 19.72978  ? 104 GLN A O   1 
ATOM   390  C CB  . GLN A 1 58 ? 12.31317 30.12409 -10.23099 1.000 23.05115  ? 104 GLN A CB  1 
ATOM   391  C CG  . GLN A 1 58 ? 12.64186 30.08820 -11.70741 1.000 23.75204  ? 104 GLN A CG  1 
ATOM   392  C CD  . GLN A 1 58 ? 12.65295 28.65612 -12.23635 1.000 29.05386  ? 104 GLN A CD  1 
ATOM   393  O OE1 . GLN A 1 58 ? 13.53233 27.86588 -11.89155 1.000 29.04140  ? 104 GLN A OE1 1 
ATOM   394  N NE2 . GLN A 1 58 ? 11.65642 28.31200 -13.05068 1.000 29.88374  ? 104 GLN A NE2 1 
ATOM   395  N N   . TYR A 1 59 ? 12.38379 30.98881 -7.24471  1.000 16.97498  ? 105 TYR A N   1 
ATOM   396  C CA  . TYR A 1 59 ? 11.84764 30.89673 -5.88682  1.000 16.73724  ? 105 TYR A CA  1 
ATOM   397  C C   . TYR A 1 59 ? 11.59128 32.27872 -5.30403  1.000 17.23841  ? 105 TYR A C   1 
ATOM   398  O O   . TYR A 1 59 ? 10.53857 32.52774 -4.69382  1.000 16.33837  ? 105 TYR A O   1 
ATOM   399  C CB  . TYR A 1 59 ? 12.82909 30.14167 -4.99153  1.000 17.91640  ? 105 TYR A CB  1 
ATOM   400  C CG  . TYR A 1 59 ? 12.70243 28.63825 -5.01584  1.000 16.75690  ? 105 TYR A CG  1 
ATOM   401  C CD1 . TYR A 1 59 ? 11.67293 27.99587 -4.34544  1.000 15.60205  ? 105 TYR A CD1 1 
ATOM   402  C CD2 . TYR A 1 59 ? 13.63938 27.85460 -5.69848  1.000 17.42014  ? 105 TYR A CD2 1 
ATOM   403  C CE1 . TYR A 1 59 ? 11.57569 26.60534 -4.34588  1.000 18.65496  ? 105 TYR A CE1 1 
ATOM   404  C CE2 . TYR A 1 59 ? 13.55984 26.46375 -5.70168  1.000 16.75082  ? 105 TYR A CE2 1 
ATOM   405  C CZ  . TYR A 1 59 ? 12.53180 25.84472 -5.01110  1.000 19.20508  ? 105 TYR A CZ  1 
ATOM   406  O OH  . TYR A 1 59 ? 12.42412 24.45408 -5.01685  1.000 20.53555  ? 105 TYR A OH  1 
ATOM   407  N N   . LYS A 1 60 ? 12.55687 33.18818 -5.45191  1.000 14.99993  ? 106 LYS A N   1 
ATOM   408  C CA  . LYS A 1 60 ? 12.37138 34.54378 -4.93482  1.000 15.10235  ? 106 LYS A CA  1 
ATOM   409  C C   . LYS A 1 60 ? 11.10902 35.18692 -5.50675  1.000 16.61048  ? 106 LYS A C   1 
ATOM   410  O O   . LYS A 1 60 ? 10.30682 35.76757 -4.76708  1.000 16.33132  ? 106 LYS A O   1 
ATOM   411  C CB  . LYS A 1 60 ? 13.58592 35.41557 -5.24671  1.000 16.91637  ? 106 LYS A CB  1 
ATOM   412  C CG  . LYS A 1 60 ? 13.37239 36.90333 -4.89792  1.000 17.49815  ? 106 LYS A CG  1 
ATOM   413  C CD  . LYS A 1 60 ? 14.59235 37.73013 -5.27156  1.000 20.45282  ? 106 LYS A CD  1 
ATOM   414  C CE  . LYS A 1 60 ? 14.37663 39.20743 -5.01925  1.000 23.21581  ? 106 LYS A CE  1 
ATOM   415  N NZ  . LYS A 1 60 ? 15.48369 40.02036 -5.62022  1.000 22.64913  ? 106 LYS A NZ  1 
ATOM   416  N N   . ASN A 1 61 ? 10.94298 35.13917 -6.83115  1.000 16.91004  ? 107 ASN A N   1 
ATOM   417  C CA  . ASN A 1 61 ? 9.76489  35.74317 -7.44927  1.000 18.68532  ? 107 ASN A CA  1 
ATOM   418  C C   . ASN A 1 61 ? 8.48149  35.09289 -6.94532  1.000 19.66227  ? 107 ASN A C   1 
ATOM   419  O O   . ASN A 1 61 ? 7.47246  35.77004 -6.73263  1.000 21.23261  ? 107 ASN A O   1 
ATOM   420  C CB  . ASN A 1 61 ? 9.84580  35.62412 -8.96637  1.000 23.15530  ? 107 ASN A CB  1 
ATOM   421  C CG  . ASN A 1 61 ? 10.89008 36.54128 -9.56981  1.000 24.25794  ? 107 ASN A CG  1 
ATOM   422  O OD1 . ASN A 1 61 ? 11.30660 37.51517 -8.94700  1.000 25.02763  ? 107 ASN A OD1 1 
ATOM   423  N ND2 . ASN A 1 61 ? 11.29720 36.24681 -10.80082 1.000 24.40960  ? 107 ASN A ND2 1 
ATOM   424  N N   . TYR A 1 62 ? 8.50407  33.77733 -6.75670  1.000 19.74694  ? 108 TYR A N   1 
ATOM   425  C CA  . TYR A 1 62 ? 7.33044  33.06319 -6.27024  1.000 18.93957  ? 108 TYR A CA  1 
ATOM   426  C C   . TYR A 1 62 ? 6.95283  33.51379 -4.86245  1.000 19.69530  ? 108 TYR A C   1 
ATOM   427  O O   . TYR A 1 62 ? 5.77426  33.74008 -4.56323  1.000 18.42636  ? 108 TYR A O   1 
ATOM   428  C CB  . TYR A 1 62 ? 7.62033  31.56613 -6.29941  1.000 20.97665  ? 108 TYR A CB  1 
ATOM   429  C CG  . TYR A 1 62 ? 6.41886  30.67635 -6.13449  1.000 24.64222  ? 108 TYR A CG  1 
ATOM   430  C CD1 . TYR A 1 62 ? 5.35322  30.74205 -7.01913  1.000 25.34549  ? 108 TYR A CD1 1 
ATOM   431  C CD2 . TYR A 1 62 ? 6.36721  29.74386 -5.11304  1.000 23.43886  ? 108 TYR A CD2 1 
ATOM   432  C CE1 . TYR A 1 62 ? 4.24951  29.90303 -6.86647  1.000 29.99128  ? 108 TYR A CE1 1 
ATOM   433  C CE2 . TYR A 1 62 ? 5.28192  28.90627 -4.96006  1.000 24.46709  ? 108 TYR A CE2 1 
ATOM   434  C CZ  . TYR A 1 62 ? 4.23795  28.98552 -5.83488  1.000 29.85235  ? 108 TYR A CZ  1 
ATOM   435  O OH  . TYR A 1 62 ? 3.16982  28.14815 -5.66189  1.000 35.96119  ? 108 TYR A OH  1 
ATOM   436  N N   . PHE A 1 63 ? 7.94348  33.61132 -3.97331  1.000 17.10958  ? 109 PHE A N   1 
ATOM   437  C CA  . PHE A 1 63 ? 7.70304  34.06534 -2.60110  1.000 19.13383  ? 109 PHE A CA  1 
ATOM   438  C C   . PHE A 1 63 ? 7.28928  35.53219 -2.56067  1.000 16.79531  ? 109 PHE A C   1 
ATOM   439  O O   . PHE A 1 63 ? 6.46150  35.93395 -1.73080  1.000 20.66144  ? 109 PHE A O   1 
ATOM   440  C CB  . PHE A 1 63 ? 8.95158  33.83767 -1.74558  1.000 16.19831  ? 109 PHE A CB  1 
ATOM   441  C CG  . PHE A 1 63 ? 9.31129  32.38286 -1.56513  1.000 16.27360  ? 109 PHE A CG  1 
ATOM   442  C CD1 . PHE A 1 63 ? 8.32756  31.42194 -1.45597  1.000 18.02961  ? 109 PHE A CD1 1 
ATOM   443  C CD2 . PHE A 1 63 ? 10.65543 31.99570 -1.47092  1.000 16.88018  ? 109 PHE A CD2 1 
ATOM   444  C CE1 . PHE A 1 63 ? 8.64421  30.09069 -1.28491  1.000 18.37326  ? 109 PHE A CE1 1 
ATOM   445  C CE2 . PHE A 1 63 ? 10.98753 30.66780 -1.29208  1.000 17.27795  ? 109 PHE A CE2 1 
ATOM   446  C CZ  . PHE A 1 63 ? 9.97903  29.71337 -1.19567  1.000 20.12871  ? 109 PHE A CZ  1 
ATOM   447  N N   . GLN A 1 64 ? 7.87730  36.35987 -3.41219  1.000 17.03445  ? 110 GLN A N   1 
ATOM   448  C CA  . GLN A 1 64 ? 7.45633  37.75439 -3.44733  1.000 18.84811  ? 110 GLN A CA  1 
ATOM   449  C C   . GLN A 1 64 ? 6.03355  37.89422 -3.98409  1.000 21.63449  ? 110 GLN A C   1 
ATOM   450  O O   . GLN A 1 64 ? 5.27251  38.74453 -3.51032  1.000 24.05825  ? 110 GLN A O   1 
ATOM   451  C CB  . GLN A 1 64 ? 8.42383  38.57502 -4.29530  1.000 19.94208  ? 110 GLN A CB  1 
ATOM   452  C CG  . GLN A 1 64 ? 9.71912  38.96723 -3.54124  1.000 20.12436  ? 110 GLN A CG  1 
ATOM   453  C CD  . GLN A 1 64 ? 10.65734 39.82831 -4.39580  1.000 25.81339  ? 110 GLN A CD  1 
ATOM   454  O OE1 . GLN A 1 64 ? 10.68911 39.69930 -5.62039  1.000 23.39224  ? 110 GLN A OE1 1 
ATOM   455  N NE2 . GLN A 1 64 ? 11.39186 40.73744 -3.74828  1.000 24.62376  ? 110 GLN A NE2 1 
ATOM   456  N N   . ALA A 1 65 ? 5.65884  37.10018 -4.98632  1.000 19.82254  ? 111 ALA A N   1 
ATOM   457  C CA  . ALA A 1 65 ? 4.32281  37.27630 -5.55585  1.000 22.97527  ? 111 ALA A CA  1 
ATOM   458  C C   . ALA A 1 65 ? 3.22307  36.72232 -4.65865  1.000 22.14156  ? 111 ALA A C   1 
ATOM   459  O O   . ALA A 1 65 ? 2.12632  37.29286 -4.59750  1.000 25.52756  ? 111 ALA A O   1 
ATOM   460  C CB  . ALA A 1 65 ? 4.23761  36.60065 -6.92282  1.000 25.01478  ? 111 ALA A CB  1 
ATOM   461  N N   . ASN A 1 66 ? 3.48948  35.61685 -3.96555  1.000 20.58949  ? 112 ASN A N   1 
ATOM   462  C CA  . ASN A 1 66 ? 2.44442  34.89263 -3.24731  1.000 25.21755  ? 112 ASN A CA  1 
ATOM   463  C C   . ASN A 1 66 ? 2.63058  34.83551 -1.74262  1.000 22.11431  ? 112 ASN A C   1 
ATOM   464  O O   . ASN A 1 66 ? 1.76412  34.28492 -1.05050  1.000 22.42584  ? 112 ASN A O   1 
ATOM   465  C CB  . ASN A 1 66 ? 2.37355  33.45255 -3.78212  1.000 24.63703  ? 112 ASN A CB  1 
ATOM   466  C CG  . ASN A 1 66 ? 2.13905  33.40570 -5.28708  1.000 26.84997  ? 112 ASN A CG  1 
ATOM   467  O OD1 . ASN A 1 66 ? 1.12618  33.88796 -5.76527  1.000 24.91216  ? 112 ASN A OD1 1 
ATOM   468  N ND2 . ASN A 1 66 ? 3.08416  32.84208 -6.03134  1.000 27.77167  ? 112 ASN A ND2 1 
ATOM   469  N N   . GLY A 1 67 ? 3.67944  35.45838 -1.20933  1.000 22.68793  ? 113 GLY A N   1 
ATOM   470  C CA  . GLY A 1 67 ? 3.97004  35.36332 0.21169   1.000 22.35388  ? 113 GLY A CA  1 
ATOM   471  C C   . GLY A 1 67 ? 3.12310  36.23038 1.11380   1.000 26.14909  ? 113 GLY A C   1 
ATOM   472  O O   . GLY A 1 67 ? 3.12179  36.00802 2.32710   1.000 24.96261  ? 113 GLY A O   1 
ATOM   473  N N   . ALA A 1 68 ? 2.43146  37.22673 0.55758   1.000 23.26781  ? 114 ALA A N   1 
ATOM   474  C CA  . ALA A 1 68 ? 1.54235  38.09501 1.31964   1.000 27.36377  ? 114 ALA A CA  1 
ATOM   475  C C   . ALA A 1 68 ? 2.26617  38.81697 2.45529   1.000 30.37725  ? 114 ALA A C   1 
ATOM   476  O O   . ALA A 1 68 ? 1.64704  39.16109 3.46528   1.000 27.70743  ? 114 ALA A O   1 
ATOM   477  C CB  . ALA A 1 68 ? 0.33268  37.31671 1.86592   1.000 24.98924  ? 114 ALA A CB  1 
ATOM   478  N N   . ARG A 1 69 ? 3.57658  39.06133 2.30627   1.000 26.31869  ? 115 ARG A N   1 
ATOM   479  C CA  . ARG A 1 69 ? 4.33439  39.86162 3.26289   1.000 28.82860  ? 115 ARG A CA  1 
ATOM   480  C C   . ARG A 1 69 ? 5.06411  40.97425 2.52148   1.000 27.33047  ? 115 ARG A C   1 
ATOM   481  O O   . ARG A 1 69 ? 5.64017  40.74502 1.45482   1.000 31.43740  ? 115 ARG A O   1 
ATOM   482  C CB  . ARG A 1 69 ? 5.35843  39.00415 4.05935   1.000 28.07744  ? 115 ARG A CB  1 
ATOM   483  C CG  . ARG A 1 69 ? 4.75684  37.90806 4.95465   1.000 27.82433  ? 115 ARG A CG  1 
ATOM   484  C CD  . ARG A 1 69 ? 3.67320  38.44115 5.84711   1.000 28.86615  ? 115 ARG A CD  1 
ATOM   485  N NE  . ARG A 1 69 ? 3.00098  37.40891 6.63606   1.000 30.36185  ? 115 ARG A NE  1 
ATOM   486  C CZ  . ARG A 1 69 ? 1.75283  37.01042 6.41497   1.000 30.04494  ? 115 ARG A CZ  1 
ATOM   487  N NH1 . ARG A 1 69 ? 1.06878  37.43643 5.36637   1.000 30.96552  ? 115 ARG A NH1 1 
ATOM   488  N NH2 . ARG A 1 69 ? 1.18870  36.12999 7.23943   1.000 34.51977  ? 115 ARG A NH2 1 
ATOM   489  N N   . SER A 1 70 ? 5.05295  42.17937 3.08529   1.000 26.77167  ? 116 SER A N   1 
ATOM   490  C CA  . SER A 1 70 ? 5.73311  43.29880 2.44857   1.000 30.48312  ? 116 SER A CA  1 
ATOM   491  C C   . SER A 1 70 ? 7.02788  43.69408 3.14831   1.000 28.73791  ? 116 SER A C   1 
ATOM   492  O O   . SER A 1 70 ? 7.68391  44.64360 2.70165   1.000 29.06030  ? 116 SER A O   1 
ATOM   493  C CB  . SER A 1 70 ? 4.81211  44.52170 2.39323   1.000 29.23053  ? 116 SER A CB  1 
ATOM   494  O OG  . SER A 1 70 ? 4.22921  44.74768 3.66692   1.000 34.27147  ? 116 SER A OG  1 
ATOM   495  N N   . ASP A 1 71 ? 7.35918  43.06181 4.27876   1.000 27.44719  ? 117 ASP A N   1 
ATOM   496  C CA  . ASP A 1 71 ? 8.52810  43.41938 5.08118   1.000 28.02676  ? 117 ASP A CA  1 
ATOM   497  C C   . ASP A 1 71 ? 9.64105  42.37246 5.07106   1.000 27.18229  ? 117 ASP A C   1 
ATOM   498  O O   . ASP A 1 71 ? 10.37603 42.25402 6.05583   1.000 30.54651  ? 117 ASP A O   1 
ATOM   499  C CB  . ASP A 1 71 ? 8.11334  43.74788 6.51502   1.000 27.71447  ? 117 ASP A CB  1 
ATOM   500  C CG  . ASP A 1 71 ? 7.41712  42.58449 7.22290   1.000 31.65235  ? 117 ASP A CG  1 
ATOM   501  O OD1 . ASP A 1 71 ? 7.13759  41.53680 6.58105   1.000 31.52893  ? 117 ASP A OD1 1 
ATOM   502  O OD2 . ASP A 1 71 ? 7.13753  42.73596 8.43719   1.000 34.60747  ? 117 ASP A OD2 1 
ATOM   503  N N   . ILE A 1 72 ? 9.75309  41.56410 4.02016   1.000 24.13590  ? 118 ILE A N   1 
ATOM   504  C CA  . ILE A 1 72 ? 10.82468 40.56782 3.90114   1.000 25.23901  ? 118 ILE A CA  1 
ATOM   505  C C   . ILE A 1 72 ? 11.96049 41.07136 3.01670   1.000 23.87655  ? 118 ILE A C   1 
ATOM   506  O O   . ILE A 1 72 ? 11.72048 41.58302 1.91615   1.000 21.25731  ? 118 ILE A O   1 
ATOM   507  C CB  . ILE A 1 72 ? 10.29419 39.24474 3.33021   1.000 23.60006  ? 118 ILE A CB  1 
ATOM   508  C CG1 . ILE A 1 72 ? 9.13049  38.72598 4.16555   1.000 25.36862  ? 118 ILE A CG1 1 
ATOM   509  C CG2 . ILE A 1 72 ? 11.44314 38.20425 3.20383   1.000 22.07433  ? 118 ILE A CG2 1 
ATOM   510  C CD1 . ILE A 1 72 ? 8.66142  37.39066 3.70202   1.000 26.40527  ? 118 ILE A CD1 1 
ATOM   511  N N   . ASP A 1 73 ? 13.20332 40.89510 3.48011   1.000 20.70651  ? 119 ASP A N   1 
ATOM   512  C CA  . ASP A 1 73 ? 14.38889 41.16496 2.67304   1.000 21.29109  ? 119 ASP A CA  1 
ATOM   513  C C   . ASP A 1 73 ? 14.88545 39.83828 2.08689   1.000 22.51388  ? 119 ASP A C   1 
ATOM   514  O O   . ASP A 1 73 ? 15.14763 38.88374 2.83388   1.000 19.42064  ? 119 ASP A O   1 
ATOM   515  C CB  . ASP A 1 73 ? 15.47352 41.85100 3.50478   1.000 22.06851  ? 119 ASP A CB  1 
ATOM   516  C CG  . ASP A 1 73 ? 15.04050 43.20365 4.02980   1.000 26.32189  ? 119 ASP A CG  1 
ATOM   517  O OD1 . ASP A 1 73 ? 14.38629 43.99201 3.28868   1.000 24.11602  ? 119 ASP A OD1 1 
ATOM   518  O OD2 . ASP A 1 73 ? 15.35940 43.49297 5.20571   1.000 26.34360  ? 119 ASP A OD2 1 
ATOM   519  N N   . PHE A 1 74 ? 14.97322 39.76434 0.75156   1.000 18.80508  ? 120 PHE A N   1 
ATOM   520  C CA  . PHE A 1 74 ? 15.42317 38.57198 0.03690   1.000 16.49921  ? 120 PHE A CA  1 
ATOM   521  C C   . PHE A 1 74 ? 16.88497 38.73200 -0.38223  1.000 20.28152  ? 120 PHE A C   1 
ATOM   522  O O   . PHE A 1 74 ? 17.27447 39.79467 -0.88633  1.000 20.93039  ? 120 PHE A O   1 
ATOM   523  C CB  . PHE A 1 74 ? 14.53618 38.29866 -1.18397  1.000 19.31823  ? 120 PHE A CB  1 
ATOM   524  C CG  . PHE A 1 74 ? 13.17179 37.74157 -0.84627  1.000 21.63428  ? 120 PHE A CG  1 
ATOM   525  C CD1 . PHE A 1 74 ? 12.09886 38.58765 -0.58467  1.000 20.69749  ? 120 PHE A CD1 1 
ATOM   526  C CD2 . PHE A 1 74 ? 12.96140 36.37643 -0.80741  1.000 18.93671  ? 120 PHE A CD2 1 
ATOM   527  C CE1 . PHE A 1 74 ? 10.84278 38.07919 -0.26585  1.000 21.33305  ? 120 PHE A CE1 1 
ATOM   528  C CE2 . PHE A 1 74 ? 11.71458 35.86655 -0.49267  1.000 19.00079  ? 120 PHE A CE2 1 
ATOM   529  C CZ  . PHE A 1 74 ? 10.65577 36.72387 -0.21681  1.000 22.11116  ? 120 PHE A CZ  1 
ATOM   530  N N   . TYR A 1 75 ? 17.69873 37.69642 -0.12384  1.000 18.53614  ? 121 TYR A N   1 
ATOM   531  C CA  . TYR A 1 75 ? 19.12391 37.66864 -0.44759  1.000 20.04955  ? 121 TYR A CA  1 
ATOM   532  C C   . TYR A 1 75 ? 19.41673 36.48558 -1.36596  1.000 18.73761  ? 121 TYR A C   1 
ATOM   533  O O   . TYR A 1 75 ? 18.99403 35.35893 -1.07932  1.000 17.72980  ? 121 TYR A O   1 
ATOM   534  C CB  . TYR A 1 75 ? 19.96549 37.56321 0.83350   1.000 20.92113  ? 121 TYR A CB  1 
ATOM   535  C CG  . TYR A 1 75 ? 19.88947 38.82446 1.66378   1.000 24.51269  ? 121 TYR A CG  1 
ATOM   536  C CD1 . TYR A 1 75 ? 18.83542 39.02094 2.54984   1.000 23.84947  ? 121 TYR A CD1 1 
ATOM   537  C CD2 . TYR A 1 75 ? 20.86931 39.79600 1.58851   1.000 28.91292  ? 121 TYR A CD2 1 
ATOM   538  C CE1 . TYR A 1 75 ? 18.74996 40.17315 3.32125   1.000 24.55883  ? 121 TYR A CE1 1 
ATOM   539  C CE2 . TYR A 1 75 ? 20.79757 40.93919 2.35812   1.000 29.47956  ? 121 TYR A CE2 1 
ATOM   540  C CZ  . TYR A 1 75 ? 19.72379 41.12789 3.21033   1.000 31.49612  ? 121 TYR A CZ  1 
ATOM   541  O OH  . TYR A 1 75 ? 19.64704 42.27010 3.97858   1.000 37.80742  ? 121 TYR A OH  1 
ATOM   542  N N   . LEU A 1 76 ? 20.09917 36.73898 -2.48194  1.000 16.96252  ? 122 LEU A N   1 
ATOM   543  C CA  . LEU A 1 76 ? 20.42017 35.69890 -3.45928  1.000 17.27648  ? 122 LEU A CA  1 
ATOM   544  C C   . LEU A 1 76 ? 21.90420 35.35991 -3.42136  1.000 16.90995  ? 122 LEU A C   1 
ATOM   545  O O   . LEU A 1 76 ? 22.74686 36.25610 -3.49417  1.000 18.12784  ? 122 LEU A O   1 
ATOM   546  C CB  . LEU A 1 76 ? 20.04067 36.12449 -4.88104  1.000 17.48432  ? 122 LEU A CB  1 
ATOM   547  C CG  . LEU A 1 76 ? 18.54343 36.33731 -5.15375  1.000 19.39202  ? 122 LEU A CG  1 
ATOM   548  C CD1 . LEU A 1 76 ? 18.33826 36.59132 -6.63634  1.000 19.28572  ? 122 LEU A CD1 1 
ATOM   549  C CD2 . LEU A 1 76 ? 17.71159 35.15737 -4.65723  1.000 17.96348  ? 122 LEU A CD2 1 
ATOM   550  N N   . GLN A 1 77 ? 22.23062 34.07500 -3.29422  1.000 16.39220  ? 123 GLN A N   1 
ATOM   551  C CA  . GLN A 1 77 ? 23.62256 33.61642 -3.34515  1.000 15.58708  ? 123 GLN A CA  1 
ATOM   552  C C   . GLN A 1 77 ? 23.76490 32.63022 -4.49138  1.000 16.82292  ? 123 GLN A C   1 
ATOM   553  O O   . GLN A 1 77 ? 23.47208 31.43010 -4.32973  1.000 15.51311  ? 123 GLN A O   1 
ATOM   554  C CB  . GLN A 1 77 ? 24.07156 32.98969 -2.03078  1.000 15.52472  ? 123 GLN A CB  1 
ATOM   555  C CG  . GLN A 1 77 ? 25.55855 32.56137 -2.06839  1.000 16.13079  ? 123 GLN A CG  1 
ATOM   556  C CD  . GLN A 1 77 ? 26.46089 33.71689 -2.39326  1.000 19.30035  ? 123 GLN A CD  1 
ATOM   557  O OE1 . GLN A 1 77 ? 26.66148 34.60180 -1.56887  1.000 23.43256  ? 123 GLN A OE1 1 
ATOM   558  N NE2 . GLN A 1 77 ? 26.99057 33.73674 -3.61290  1.000 20.64203  ? 123 GLN A NE2 1 
ATOM   559  N N   . PRO A 1 78 ? 24.16248 33.08403 -5.68134  1.000 15.47780  ? 124 PRO A N   1 
ATOM   560  C CA  . PRO A 1 78 ? 24.33267 32.15871 -6.81037  1.000 19.40378  ? 124 PRO A CA  1 
ATOM   561  C C   . PRO A 1 78 ? 25.52741 31.23371 -6.61834  1.000 19.97728  ? 124 PRO A C   1 
ATOM   562  O O   . PRO A 1 78 ? 26.58916 31.64152 -6.15215  1.000 20.69788  ? 124 PRO A O   1 
ATOM   563  C CB  . PRO A 1 78 ? 24.55510 33.08675 -8.01087  1.000 22.00048  ? 124 PRO A CB  1 
ATOM   564  C CG  . PRO A 1 78 ? 25.03857 34.38471 -7.43791  1.000 23.74532  ? 124 PRO A CG  1 
ATOM   565  C CD  . PRO A 1 78 ? 24.46675 34.48387 -6.03506  1.000 20.00413  ? 124 PRO A CD  1 
ATOM   566  N N   . THR A 1 79 ? 25.34094 29.97213 -6.97775  1.000 19.06956  ? 125 THR A N   1 
ATOM   567  C CA  . THR A 1 79 ? 26.39074 28.96795 -6.94980  1.000 17.58615  ? 125 THR A CA  1 
ATOM   568  C C   . THR A 1 79 ? 26.30640 28.16079 -8.23922  1.000 20.69900  ? 125 THR A C   1 
ATOM   569  O O   . THR A 1 79 ? 25.44510 28.40667 -9.09298  1.000 20.88272  ? 125 THR A O   1 
ATOM   570  C CB  . THR A 1 79 ? 26.27442 28.04646 -5.73212  1.000 20.13602  ? 125 THR A CB  1 
ATOM   571  O OG1 . THR A 1 79 ? 25.14086 27.19044 -5.89865  1.000 19.90710  ? 125 THR A OG1 1 
ATOM   572  C CG2 . THR A 1 79 ? 26.09908 28.85217 -4.43250  1.000 18.77469  ? 125 THR A CG2 1 
ATOM   573  N N   . LEU A 1 80 ? 27.19096 27.17176 -8.36842  1.000 21.46996  ? 126 LEU A N   1 
ATOM   574  C CA  . LEU A 1 80 ? 27.18904 26.27952 -9.52028  1.000 24.40233  ? 126 LEU A CA  1 
ATOM   575  C C   . LEU A 1 80 ? 26.46695 24.97286 -9.23306  1.000 25.72184  ? 126 LEU A C   1 
ATOM   576  O O   . LEU A 1 80 ? 26.33175 24.15232 -10.13539 1.000 28.73981  ? 126 LEU A O   1 
ATOM   577  C CB  . LEU A 1 80 ? 28.62854 25.97096 -9.96863  1.000 26.02955  ? 126 LEU A CB  1 
ATOM   578  C CG  . LEU A 1 80 ? 29.48948 27.17177 -10.34003 1.000 25.37021  ? 126 LEU A CG  1 
ATOM   579  C CD1 . LEU A 1 80 ? 30.84870 26.73446 -10.88704 1.000 27.48455  ? 126 LEU A CD1 1 
ATOM   580  C CD2 . LEU A 1 80 ? 28.74656 28.02695 -11.36314 1.000 26.31276  ? 126 LEU A CD2 1 
ATOM   581  N N   . ASN A 1 81 ? 25.97828 24.78252 -8.00835  1.000 26.81073  ? 127 ASN A N   1 
ATOM   582  C CA  . ASN A 1 81 ? 25.14848 23.62590 -7.67030  1.000 28.99405  ? 127 ASN A CA  1 
ATOM   583  C C   . ASN A 1 81 ? 23.92759 23.57440 -8.57339  1.000 28.87795  ? 127 ASN A C   1 
ATOM   584  O O   . ASN A 1 81 ? 23.22268 24.57475 -8.73415  1.000 27.98520  ? 127 ASN A O   1 
ATOM   585  C CB  . ASN A 1 81 ? 24.64035 23.71555 -6.22604  1.000 28.10047  ? 127 ASN A CB  1 
ATOM   586  C CG  . ASN A 1 81 ? 25.75079 23.84526 -5.21535  1.000 34.56433  ? 127 ASN A CG  1 
ATOM   587  O OD1 . ASN A 1 81 ? 26.00474 24.94263 -4.69316  1.000 33.21083  ? 127 ASN A OD1 1 
ATOM   588  N ND2 . ASN A 1 81 ? 26.44775 22.73530 -4.94731  1.000 37.62565  ? 127 ASN A ND2 1 
ATOM   589  N N   . GLN A 1 82 ? 23.62806 22.39304 -9.10951  1.000 33.58363  ? 128 GLN A N   1 
ATOM   590  C CA  . GLN A 1 82 ? 22.42403 22.23503 -9.91955  1.000 34.45331  ? 128 GLN A CA  1 
ATOM   591  C C   . GLN A 1 82 ? 21.32901 21.41253 -9.24728  1.000 35.61945  ? 128 GLN A C   1 
ATOM   592  O O   . GLN A 1 82 ? 20.22883 21.29525 -9.80153  1.000 37.64762  ? 128 GLN A O   1 
ATOM   593  C CB  . GLN A 1 82 ? 22.78291 21.62089 -11.27890 1.000 38.85731  ? 128 GLN A CB  1 
ATOM   594  C CG  . GLN A 1 82 ? 23.49910 22.62969 -12.19580 1.000 38.62421  ? 128 GLN A CG  1 
ATOM   595  C CD  . GLN A 1 82 ? 22.69307 23.90512 -12.41549 1.000 38.44085  ? 128 GLN A CD  1 
ATOM   596  O OE1 . GLN A 1 82 ? 21.45530 23.91751 -12.30846 1.000 39.96137  ? 128 GLN A OE1 1 
ATOM   597  N NE2 . GLN A 1 82 ? 23.40311 25.00768 -12.64489 1.000 36.50109  ? 128 GLN A NE2 1 
ATOM   598  N N   . LYS A 1 83 ? 21.56066 20.87188 -8.06041  1.000 32.58306  ? 129 LYS A N   1 
ATOM   599  C CA  . LYS A 1 83 ? 20.56708 19.99958 -7.43615  1.000 35.25057  ? 129 LYS A CA  1 
ATOM   600  C C   . LYS A 1 83 ? 19.80947 20.79327 -6.38615  1.000 33.52206  ? 129 LYS A C   1 
ATOM   601  O O   . LYS A 1 83 ? 20.16720 20.80430 -5.20826  1.000 33.28047  ? 129 LYS A O   1 
ATOM   602  C CB  . LYS A 1 83 ? 21.21780 18.75437 -6.85045  1.000 40.69165  ? 129 LYS A CB  1 
ATOM   603  C CG  . LYS A 1 83 ? 21.31194 17.62095 -7.87518  1.000 49.28163  ? 129 LYS A CG  1 
ATOM   604  C CD  . LYS A 1 83 ? 22.37802 16.58792 -7.53079  1.000 52.47124  ? 129 LYS A CD  1 
ATOM   605  C CE  . LYS A 1 83 ? 22.88331 15.88167 -8.79559  1.000 57.18505  ? 129 LYS A CE  1 
ATOM   606  N NZ  . LYS A 1 83 ? 24.36839 15.86893 -8.88288  1.000 57.84823  ? 129 LYS A NZ  1 
ATOM   607  N N   . GLY A 1 84 ? 18.73433 21.44623 -6.81784  1.000 29.07625  ? 130 GLY A N   1 
ATOM   608  C CA  . GLY A 1 84 ? 17.92202 22.12167 -5.83985  1.000 26.20686  ? 130 GLY A CA  1 
ATOM   609  C C   . GLY A 1 84 ? 18.54078 23.41353 -5.34973  1.000 22.64723  ? 130 GLY A C   1 
ATOM   610  O O   . GLY A 1 84 ? 19.50262 23.95265 -5.90473  1.000 23.99154  ? 130 GLY A O   1 
ATOM   611  N N   . VAL A 1 85 ? 17.91126 23.95368 -4.30673  1.000 20.44077  ? 131 VAL A N   1 
ATOM   612  C CA  . VAL A 1 85 ? 18.36393 25.18193 -3.67528  1.000 18.22691  ? 131 VAL A CA  1 
ATOM   613  C C   . VAL A 1 85 ? 18.28248 25.00473 -2.16351  1.000 20.46072  ? 131 VAL A C   1 
ATOM   614  O O   . VAL A 1 85 ? 17.55543 24.14499 -1.64987  1.000 21.01267  ? 131 VAL A O   1 
ATOM   615  C CB  . VAL A 1 85 ? 17.55973 26.42722 -4.11633  1.000 20.93531  ? 131 VAL A CB  1 
ATOM   616  C CG1 . VAL A 1 85 ? 17.30064 26.41733 -5.65663  1.000 19.50552  ? 131 VAL A CG1 1 
ATOM   617  C CG2 . VAL A 1 85 ? 16.26600 26.50723 -3.35786  1.000 21.83647  ? 131 VAL A CG2 1 
ATOM   618  N N   . VAL A 1 86 ? 19.05945 25.82064 -1.45404  1.000 15.87315  ? 132 VAL A N   1 
ATOM   619  C CA  . VAL A 1 86 ? 19.00298 25.90364 0.00231   1.000 15.48722  ? 132 VAL A CA  1 
ATOM   620  C C   . VAL A 1 86 ? 18.31857 27.21163 0.35000   1.000 15.56298  ? 132 VAL A C   1 
ATOM   621  O O   . VAL A 1 86 ? 18.63624 28.25924 -0.22854  1.000 14.85239  ? 132 VAL A O   1 
ATOM   622  C CB  . VAL A 1 86 ? 20.40769 25.83525 0.63443   1.000 16.70883  ? 132 VAL A CB  1 
ATOM   623  C CG1 . VAL A 1 86 ? 20.32381 26.17012 2.15541   1.000 16.71930  ? 132 VAL A CG1 1 
ATOM   624  C CG2 . VAL A 1 86 ? 21.01531 24.46900 0.40662   1.000 19.34444  ? 132 VAL A CG2 1 
ATOM   625  N N   . MET A 1 87 ? 17.34035 27.15341 1.25339   1.000 13.46088  ? 133 MET A N   1 
ATOM   626  C CA  . MET A 1 87 ? 16.64309 28.35328 1.67724   1.000 13.00195  ? 133 MET A CA  1 
ATOM   627  C C   . MET A 1 87 ? 16.87841 28.56087 3.17012   1.000 14.62200  ? 133 MET A C   1 
ATOM   628  O O   . MET A 1 87 ? 16.74120 27.62513 3.96475   1.000 15.07668  ? 133 MET A O   1 
ATOM   629  C CB  . MET A 1 87 ? 15.15138 28.24891 1.30751   1.000 12.46898  ? 133 MET A CB  1 
ATOM   630  C CG  . MET A 1 87 ? 14.20614 29.25994 1.92881   1.000 15.41479  ? 133 MET A CG  1 
ATOM   631  S SD  . MET A 1 87 ? 12.45941 28.77268 1.75796   1.000 18.10125  ? 133 MET A SD  1 
ATOM   632  C CE  . MET A 1 87 ? 11.67752 30.07060 2.71467   1.000 21.50442  ? 133 MET A CE  1 
ATOM   633  N N   . ILE A 1 88 ? 17.26107 29.77057 3.54581   1.000 14.19931  ? 134 ILE A N   1 
ATOM   634  C CA  . ILE A 1 88 ? 17.46858 30.12535 4.94682   1.000 14.61946  ? 134 ILE A CA  1 
ATOM   635  C C   . ILE A 1 88 ? 16.48726 31.23050 5.29976   1.000 15.81110  ? 134 ILE A C   1 
ATOM   636  O O   . ILE A 1 88 ? 16.47833 32.29008 4.65796   1.000 16.34918  ? 134 ILE A O   1 
ATOM   637  C CB  . ILE A 1 88 ? 18.91256 30.56196 5.23336   1.000 13.81307  ? 134 ILE A CB  1 
ATOM   638  C CG1 . ILE A 1 88 ? 19.88066 29.44447 4.83136   1.000 16.05838  ? 134 ILE A CG1 1 
ATOM   639  C CG2 . ILE A 1 88 ? 19.06845 30.85141 6.72964   1.000 17.11072  ? 134 ILE A CG2 1 
ATOM   640  C CD1 . ILE A 1 88 ? 21.33031 29.86143 4.83675   1.000 19.91833  ? 134 ILE A CD1 1 
ATOM   641  N N   . ALA A 1 89 ? 15.64296 30.97448 6.29972   1.000 15.44263  ? 135 ALA A N   1 
ATOM   642  C CA  . ALA A 1 89 ? 14.61790 31.91603 6.71045   1.000 16.37187  ? 135 ALA A CA  1 
ATOM   643  C C   . ALA A 1 89 ? 14.87123 32.29765 8.16002   1.000 19.41957  ? 135 ALA A C   1 
ATOM   644  O O   . ALA A 1 89 ? 15.19016 31.44249 8.98504   1.000 18.16124  ? 135 ALA A O   1 
ATOM   645  C CB  . ALA A 1 89 ? 13.20666 31.31244 6.53100   1.000 15.63732  ? 135 ALA A CB  1 
ATOM   646  N N   . SER A 1 90 ? 14.71315 33.57838 8.47029   1.000 17.85255  ? 136 SER A N   1 
ATOM   647  C CA  . SER A 1 90 ? 15.03857 34.06539 9.80156   1.000 20.43670  ? 136 SER A CA  1 
ATOM   648  C C   . SER A 1 90 ? 14.12157 35.21893 10.15246  1.000 19.94828  ? 136 SER A C   1 
ATOM   649  O O   . SER A 1 90 ? 13.67540 35.95346 9.26513   1.000 20.72852  ? 136 SER A O   1 
ATOM   650  C CB  . SER A 1 90 ? 16.49911 34.53307 9.86568   1.000 21.26609  ? 136 SER A CB  1 
ATOM   651  O OG  . SER A 1 90 ? 16.78724 34.96779 11.17552  1.000 25.40513  ? 136 SER A OG  1 
ATOM   652  N N   . ASN A 1 91 ? 13.83508 35.38163 11.44619  1.000 20.79340  ? 137 ASN A N   1 
ATOM   653  C CA  . ASN A 1 91 ? 13.04658 36.52224 11.88201  1.000 24.43672  ? 137 ASN A CA  1 
ATOM   654  C C   . ASN A 1 91 ? 13.90911 37.61612 12.48787  1.000 29.97925  ? 137 ASN A C   1 
ATOM   655  O O   . ASN A 1 91 ? 13.39211 38.48577 13.19247  1.000 33.29594  ? 137 ASN A O   1 
ATOM   656  C CB  . ASN A 1 91 ? 11.93454 36.10284 12.85170  1.000 24.59048  ? 137 ASN A CB  1 
ATOM   657  C CG  . ASN A 1 91 ? 12.45741 35.43654 14.10643  1.000 27.34579  ? 137 ASN A CG  1 
ATOM   658  O OD1 . ASN A 1 91 ? 13.64407 35.11069 14.21365  1.000 23.17416  ? 137 ASN A OD1 1 
ATOM   659  N ND2 . ASN A 1 91 ? 11.56741 35.26904 15.09097  1.000 28.11815  ? 137 ASN A ND2 1 
ATOM   660  N N   . TYR A 1 92 ? 15.20917 37.58389 12.23341  1.000 30.33777  ? 138 TYR A N   1 
ATOM   661  C CA  . TYR A 1 92 ? 16.09660 38.68586 12.59037  1.000 34.26519  ? 138 TYR A CA  1 
ATOM   662  C C   . TYR A 1 92 ? 17.17881 38.79693 11.52391  1.000 37.84450  ? 138 TYR A C   1 
ATOM   663  O O   . TYR A 1 92 ? 17.07345 38.15757 10.46265  1.000 35.95073  ? 138 TYR A O   1 
ATOM   664  C CB  . TYR A 1 92 ? 16.68631 38.46677 13.98004  1.000 35.75398  ? 138 TYR A CB  1 
ATOM   665  C CG  . TYR A 1 92 ? 17.54657 37.22329 14.09083  1.000 37.43371  ? 138 TYR A CG  1 
ATOM   666  C CD1 . TYR A 1 92 ? 18.89602 37.24395 13.75268  1.000 39.32588  ? 138 TYR A CD1 1 
ATOM   667  C CD2 . TYR A 1 92 ? 16.98782 36.00793 14.49808  1.000 34.68611  ? 138 TYR A CD2 1 
ATOM   668  C CE1 . TYR A 1 92 ? 19.67873 36.09206 13.85429  1.000 40.19193  ? 138 TYR A CE1 1 
ATOM   669  C CE2 . TYR A 1 92 ? 17.74724 34.85673 14.59766  1.000 32.13559  ? 138 TYR A CE2 1 
ATOM   670  C CZ  . TYR A 1 92 ? 19.09335 34.90132 14.28055  1.000 38.89774  ? 138 TYR A CZ  1 
ATOM   671  O OH  . TYR A 1 92 ? 19.84766 33.75249 14.39018  1.000 40.15785  ? 138 TYR A OH  1 
ATOM   672  N N   . LYS B 1 11 ? 9.50360  12.88691 0.32980   1.000 80.69523  ? 57  LYS B N   1 
ATOM   673  C CA  . LYS B 1 11 ? 9.38729  12.76535 1.77823   1.000 79.89009  ? 57  LYS B CA  1 
ATOM   674  C C   . LYS B 1 11 ? 9.71993  14.08329 2.47092   1.000 73.81717  ? 57  LYS B C   1 
ATOM   675  O O   . LYS B 1 11 ? 9.79051  15.12429 1.81493   1.000 72.55895  ? 57  LYS B O   1 
ATOM   676  C CB  . LYS B 1 11 ? 10.28203 11.63434 2.28592   1.000 85.23223  ? 57  LYS B CB  1 
ATOM   677  C CG  . LYS B 1 11 ? 11.70250 11.65004 1.74287   1.000 87.98782  ? 57  LYS B CG  1 
ATOM   678  C CD  . LYS B 1 11 ? 12.40060 10.34238 2.08915   1.000 93.90350  ? 57  LYS B CD  1 
ATOM   679  C CE  . LYS B 1 11 ? 11.63935 9.16645  1.48761   1.000 96.18111  ? 57  LYS B CE  1 
ATOM   680  N NZ  . LYS B 1 11 ? 12.18863 7.84355  1.89155   1.000 102.05675 ? 57  LYS B NZ  1 
ATOM   681  N N   . ASP B 1 12 ? 9.92036  14.03414 3.79018   1.000 66.72351  ? 58  ASP B N   1 
ATOM   682  C CA  . ASP B 1 12 ? 10.03479 15.25749 4.57514   1.000 58.02608  ? 58  ASP B CA  1 
ATOM   683  C C   . ASP B 1 12 ? 11.19468 16.11986 4.09624   1.000 51.87090  ? 58  ASP B C   1 
ATOM   684  O O   . ASP B 1 12 ? 12.24254 15.61821 3.67835   1.000 51.08360  ? 58  ASP B O   1 
ATOM   685  C CB  . ASP B 1 12 ? 10.20730 14.94560 6.06337   1.000 57.70945  ? 58  ASP B CB  1 
ATOM   686  C CG  . ASP B 1 12 ? 9.41433  13.74885 6.49756   1.000 68.33212  ? 58  ASP B CG  1 
ATOM   687  O OD1 . ASP B 1 12 ? 8.17091  13.86620 6.57494   1.000 72.87481  ? 58  ASP B OD1 1 
ATOM   688  O OD2 . ASP B 1 12 ? 10.02815 12.69335 6.76513   1.000 73.59844  ? 58  ASP B OD2 1 
ATOM   689  N N   . THR B 1 13 ? 10.97598 17.42229 4.13717   1.000 41.56710  ? 59  THR B N   1 
ATOM   690  C CA  . THR B 1 13 ? 11.98354 18.39478 3.77030   1.000 34.67656  ? 59  THR B CA  1 
ATOM   691  C C   . THR B 1 13 ? 13.12980 18.31457 4.77415   1.000 32.86713  ? 59  THR B C   1 
ATOM   692  O O   . THR B 1 13 ? 12.88354 18.43570 5.98370   1.000 29.38529  ? 59  THR B O   1 
ATOM   693  C CB  . THR B 1 13 ? 11.34778 19.79075 3.76873   1.000 31.22235  ? 59  THR B CB  1 
ATOM   694  O OG1 . THR B 1 13 ? 10.32850 19.85084 2.76777   1.000 30.61712  ? 59  THR B OG1 1 
ATOM   695  C CG2 . THR B 1 13 ? 12.38346 20.86818 3.48562   1.000 28.04014  ? 59  THR B CG2 1 
ATOM   696  N N   . PRO B 1 14 ? 14.37310 18.08892 4.34234   1.000 28.72350  ? 60  PRO B N   1 
ATOM   697  C CA  . PRO B 1 14 ? 15.49854 18.14321 5.29251   1.000 31.56042  ? 60  PRO B CA  1 
ATOM   698  C C   . PRO B 1 14 ? 15.64065 19.54351 5.87629   1.000 24.82233  ? 60  PRO B C   1 
ATOM   699  O O   . PRO B 1 14 ? 15.58047 20.54049 5.15752   1.000 21.84728  ? 60  PRO B O   1 
ATOM   700  C CB  . PRO B 1 14 ? 16.71417 17.74499 4.44010   1.000 29.25490  ? 60  PRO B CB  1 
ATOM   701  C CG  . PRO B 1 14 ? 16.16628 17.14048 3.17877   1.000 28.14978  ? 60  PRO B CG  1 
ATOM   702  C CD  . PRO B 1 14 ? 14.81050 17.76785 2.97311   1.000 29.67262  ? 60  PRO B CD  1 
ATOM   703  N N   . PHE B 1 15 ? 15.80548 19.62723 7.19521   1.000 21.54522  ? 61  PHE B N   1 
ATOM   704  C CA  . PHE B 1 15 ? 15.87503 20.93450 7.83405   1.000 22.20562  ? 61  PHE B CA  1 
ATOM   705  C C   . PHE B 1 15 ? 16.93405 20.98033 8.93188   1.000 23.37721  ? 61  PHE B C   1 
ATOM   706  O O   . PHE B 1 15 ? 17.30157 19.96383 9.53620   1.000 23.31402  ? 61  PHE B O   1 
ATOM   707  C CB  . PHE B 1 15 ? 14.51709 21.35575 8.43077   1.000 24.63890  ? 61  PHE B CB  1 
ATOM   708  C CG  . PHE B 1 15 ? 14.09095 20.54083 9.63114   1.000 23.83861  ? 61  PHE B CG  1 
ATOM   709  C CD1 . PHE B 1 15 ? 14.65383 20.75797 10.89167  1.000 25.85311  ? 61  PHE B CD1 1 
ATOM   710  C CD2 . PHE B 1 15 ? 13.13283 19.55398 9.49638   1.000 28.47645  ? 61  PHE B CD2 1 
ATOM   711  C CE1 . PHE B 1 15 ? 14.27005 20.00409 11.97964  1.000 26.80656  ? 61  PHE B CE1 1 
ATOM   712  C CE2 . PHE B 1 15 ? 12.73701 18.80316 10.58770  1.000 29.18989  ? 61  PHE B CE2 1 
ATOM   713  C CZ  . PHE B 1 15 ? 13.31253 19.02482 11.82907  1.000 30.12320  ? 61  PHE B CZ  1 
ATOM   714  N N   . MET B 1 16 ? 17.36306 22.21096 9.21151   1.000 21.00226  ? 62  MET B N   1 
ATOM   715  C CA  . MET B 1 16 ? 18.12085 22.56067 10.40383  1.000 20.98429  ? 62  MET B CA  1 
ATOM   716  C C   . MET B 1 16 ? 17.51006 23.84583 10.94854  1.000 19.50808  ? 62  MET B C   1 
ATOM   717  O O   . MET B 1 16 ? 17.36726 24.82299 10.21009  1.000 20.87332  ? 62  MET B O   1 
ATOM   718  C CB  . MET B 1 16 ? 19.60139 22.77821 10.09304  1.000 22.36677  ? 62  MET B CB  1 
ATOM   719  C CG  . MET B 1 16 ? 20.37500 21.49835 9.84580   1.000 25.48020  ? 62  MET B CG  1 
ATOM   720  S SD  . MET B 1 16 ? 22.09153 21.86048 9.42696   1.000 32.97302  ? 62  MET B SD  1 
ATOM   721  C CE  . MET B 1 16 ? 22.67120 22.01391 11.12098  1.000 31.49525  ? 62  MET B CE  1 
ATOM   722  N N   . VAL B 1 17 ? 17.09759 23.83294 12.21265  1.000 21.23263  ? 63  VAL B N   1 
ATOM   723  C CA  . VAL B 1 17 ? 16.47749 24.98859 12.84890  1.000 20.65436  ? 63  VAL B CA  1 
ATOM   724  C C   . VAL B 1 17 ? 17.32478 25.39117 14.04576  1.000 20.60618  ? 63  VAL B C   1 
ATOM   725  O O   . VAL B 1 17 ? 17.50235 24.59607 14.97671  1.000 21.44079  ? 63  VAL B O   1 
ATOM   726  C CB  . VAL B 1 17 ? 15.03536 24.69388 13.29288  1.000 22.03100  ? 63  VAL B CB  1 
ATOM   727  C CG1 . VAL B 1 17 ? 14.47727 25.89790 14.06400  1.000 21.39621  ? 63  VAL B CG1 1 
ATOM   728  C CG2 . VAL B 1 17 ? 14.17066 24.35779 12.07039  1.000 22.44749  ? 63  VAL B CG2 1 
ATOM   729  N N   . GLN B 1 18 ? 17.76930 26.64150 14.06662  1.000 19.78539  ? 64  GLN B N   1 
ATOM   730  C CA  . GLN B 1 18 ? 18.50880 27.17772 15.19954  1.000 21.08111  ? 64  GLN B CA  1 
ATOM   731  C C   . GLN B 1 18 ? 17.63972 28.21563 15.90257  1.000 21.23869  ? 64  GLN B C   1 
ATOM   732  O O   . GLN B 1 18 ? 17.16874 29.16665 15.26338  1.000 21.14215  ? 64  GLN B O   1 
ATOM   733  C CB  . GLN B 1 18 ? 19.82781 27.78887 14.73878  1.000 21.99102  ? 64  GLN B CB  1 
ATOM   734  C CG  . GLN B 1 18 ? 20.55043 28.51939 15.84713  1.000 25.07319  ? 64  GLN B CG  1 
ATOM   735  C CD  . GLN B 1 18 ? 21.82246 29.15277 15.36775  1.000 24.11299  ? 64  GLN B CD  1 
ATOM   736  O OE1 . GLN B 1 18 ? 22.84802 28.50293 15.32084  1.000 26.12664  ? 64  GLN B OE1 1 
ATOM   737  N NE2 . GLN B 1 18 ? 21.76193 30.42344 15.00401  1.000 25.01424  ? 64  GLN B NE2 1 
ATOM   738  N N   . VAL B 1 19 ? 17.40586 28.02717 17.20552  1.000 19.82238  ? 65  VAL B N   1 
ATOM   739  C CA  . VAL B 1 19 ? 16.59824 28.95975 17.98691  1.000 21.56494  ? 65  VAL B CA  1 
ATOM   740  C C   . VAL B 1 19 ? 17.39263 29.45095 19.19029  1.000 24.76767  ? 65  VAL B C   1 
ATOM   741  O O   . VAL B 1 19 ? 18.15788 28.69556 19.80212  1.000 22.09231  ? 65  VAL B O   1 
ATOM   742  C CB  . VAL B 1 19 ? 15.26247 28.33791 18.45246  1.000 21.89020  ? 65  VAL B CB  1 
ATOM   743  C CG1 . VAL B 1 19 ? 14.32471 28.13759 17.28147  1.000 20.93859  ? 65  VAL B CG1 1 
ATOM   744  C CG2 . VAL B 1 19 ? 15.50412 27.04415 19.17658  1.000 25.14037  ? 65  VAL B CG2 1 
ATOM   745  N N   . LYS B 1 20 ? 17.18652 30.71503 19.54004  1.000 24.74415  ? 66  LYS B N   1 
ATOM   746  C CA  . LYS B 1 20 ? 17.80334 31.30496 20.71693  1.000 28.80091  ? 66  LYS B CA  1 
ATOM   747  C C   . LYS B 1 20 ? 16.80302 31.21785 21.86325  1.000 33.45650  ? 66  LYS B C   1 
ATOM   748  O O   . LYS B 1 20 ? 15.67085 31.71339 21.74647  1.000 29.69477  ? 66  LYS B O   1 
ATOM   749  C CB  . LYS B 1 20 ? 18.22639 32.75111 20.45462  1.000 29.28673  ? 66  LYS B CB  1 
ATOM   750  C CG  . LYS B 1 20 ? 19.22625 32.92928 19.30898  1.000 31.64872  ? 66  LYS B CG  1 
ATOM   751  C CD  . LYS B 1 20 ? 19.41297 34.42853 18.99603  1.000 36.15107  ? 66  LYS B CD  1 
ATOM   752  C CE  . LYS B 1 20 ? 20.52233 34.65960 17.97802  1.000 41.23826  ? 66  LYS B CE  1 
ATOM   753  N NZ  . LYS B 1 20 ? 21.30175 33.40383 17.68415  1.000 39.80777  ? 66  LYS B NZ  1 
ATOM   754  N N   . LEU B 1 21 ? 17.21903 30.55328 22.96665  1.000 31.95339  ? 67  LEU B N   1 
ATOM   755  C CA  . LEU B 1 21 ? 16.38304 30.28479 24.11776  1.000 36.08327  ? 67  LEU B CA  1 
ATOM   756  C C   . LEU B 1 21 ? 16.93923 31.02454 25.33746  1.000 39.73482  ? 67  LEU B C   1 
ATOM   757  O O   . LEU B 1 21 ? 18.15038 31.25234 25.43625  1.000 39.23357  ? 67  LEU B O   1 
ATOM   758  C CB  . LEU B 1 21 ? 16.32215 28.78120 24.43534  1.000 36.28366  ? 67  LEU B CB  1 
ATOM   759  C CG  . LEU B 1 21 ? 15.68261 27.88578 23.36134  1.000 32.15753  ? 67  LEU B CG  1 
ATOM   760  C CD1 . LEU B 1 21 ? 15.84377 26.39281 23.70821  1.000 32.56522  ? 67  LEU B CD1 1 
ATOM   761  C CD2 . LEU B 1 21 ? 14.25109 28.26889 22.98856  1.000 37.70034  ? 67  LEU B CD2 1 
ATOM   762  N N   . PRO B 1 22 ? 16.08305 31.41884 26.26995  1.000 41.07923  ? 68  PRO B N   1 
ATOM   763  C CA  . PRO B 1 22 ? 16.54969 32.13167 27.46615  1.000 45.18467  ? 68  PRO B CA  1 
ATOM   764  C C   . PRO B 1 22 ? 17.07921 31.20459 28.54822  1.000 52.58607  ? 68  PRO B C   1 
ATOM   765  O O   . PRO B 1 22 ? 17.36597 30.02801 28.29860  1.000 49.24994  ? 68  PRO B O   1 
ATOM   766  C CB  . PRO B 1 22 ? 15.28753 32.85708 27.93794  1.000 47.70629  ? 68  PRO B CB  1 
ATOM   767  C CG  . PRO B 1 22 ? 14.19091 31.92974 27.54093  1.000 47.19575  ? 68  PRO B CG  1 
ATOM   768  C CD  . PRO B 1 22 ? 14.61407 31.34951 26.21448  1.000 42.02727  ? 68  PRO B CD  1 
ATOM   769  N N   . ASN B 1 23 ? 17.24513 31.74992 29.75319  1.000 58.94161  ? 69  ASN B N   1 
ATOM   770  C CA  . ASN B 1 23 ? 17.53236 30.91234 30.90499  1.000 59.58170  ? 69  ASN B CA  1 
ATOM   771  C C   . ASN B 1 23 ? 16.41807 29.88443 31.04267  1.000 61.01870  ? 69  ASN B C   1 
ATOM   772  O O   . ASN B 1 23 ? 15.25239 30.18247 30.76788  1.000 61.66200  ? 69  ASN B O   1 
ATOM   773  C CB  . ASN B 1 23 ? 17.61481 31.76337 32.17462  1.000 63.81540  ? 69  ASN B CB  1 
ATOM   774  C CG  . ASN B 1 23 ? 18.98733 32.36389 32.38230  1.000 69.66925  ? 69  ASN B CG  1 
ATOM   775  O OD1 . ASN B 1 23 ? 19.97757 31.86341 31.85195  1.000 71.22704  ? 69  ASN B OD1 1 
ATOM   776  N ND2 . ASN B 1 23 ? 19.06118 33.42004 33.19035  1.000 73.41730  ? 69  ASN B ND2 1 
ATOM   777  N N   . TYR B 1 24 ? 16.77541 28.66743 31.46593  1.000 60.72367  ? 70  TYR B N   1 
ATOM   778  C CA  . TYR B 1 24 ? 15.77926 27.60168 31.56575  1.000 57.50798  ? 70  TYR B CA  1 
ATOM   779  C C   . TYR B 1 24 ? 14.58033 28.04279 32.40308  1.000 60.94952  ? 70  TYR B C   1 
ATOM   780  O O   . TYR B 1 24 ? 13.42805 27.74712 32.06015  1.000 58.18993  ? 70  TYR B O   1 
ATOM   781  C CB  . TYR B 1 24 ? 16.41244 26.34015 32.16134  1.000 57.73366  ? 70  TYR B CB  1 
ATOM   782  C CG  . TYR B 1 24 ? 15.41696 25.23341 32.43177  1.000 56.80933  ? 70  TYR B CG  1 
ATOM   783  C CD1 . TYR B 1 24 ? 14.73274 24.62012 31.38499  1.000 55.33426  ? 70  TYR B CD1 1 
ATOM   784  C CD2 . TYR B 1 24 ? 15.12830 24.82830 33.72634  1.000 58.11930  ? 70  TYR B CD2 1 
ATOM   785  C CE1 . TYR B 1 24 ? 13.81829 23.61433 31.61828  1.000 54.89633  ? 70  TYR B CE1 1 
ATOM   786  C CE2 . TYR B 1 24 ? 14.20827 23.82351 33.96977  1.000 57.43001  ? 70  TYR B CE2 1 
ATOM   787  C CZ  . TYR B 1 24 ? 13.55857 23.22294 32.91397  1.000 55.95401  ? 70  TYR B CZ  1 
ATOM   788  O OH  . TYR B 1 24 ? 12.64569 22.22766 33.14947  1.000 55.56998  ? 70  TYR B OH  1 
ATOM   789  N N   . LYS B 1 25 ? 14.84432 28.77301 33.49643  1.000 63.31260  ? 71  LYS B N   1 
ATOM   790  C CA  . LYS B 1 25 ? 13.79366 29.26663 34.38703  1.000 64.06460  ? 71  LYS B CA  1 
ATOM   791  C C   . LYS B 1 25 ? 12.77908 30.13205 33.64711  1.000 64.27774  ? 71  LYS B C   1 
ATOM   792  O O   . LYS B 1 25 ? 11.56534 29.91448 33.75105  1.000 60.74598  ? 71  LYS B O   1 
ATOM   793  C CB  . LYS B 1 25 ? 14.42972 30.05964 35.53199  1.000 65.08398  ? 71  LYS B CB  1 
ATOM   794  C CG  . LYS B 1 25 ? 13.50091 30.38902 36.68770  1.000 69.99225  ? 71  LYS B CG  1 
ATOM   795  C CD  . LYS B 1 25 ? 12.87198 31.77111 36.52507  1.000 69.62503  ? 71  LYS B CD  1 
ATOM   796  C CE  . LYS B 1 25 ? 11.84221 32.03993 37.60623  1.000 70.43022  ? 71  LYS B CE  1 
ATOM   797  N NZ  . LYS B 1 25 ? 10.76765 31.00592 37.64490  1.000 75.28213  ? 71  LYS B NZ  1 
ATOM   798  N N   . ASP B 1 26 ? 13.25846 31.14472 32.92011  1.000 65.12552  ? 72  ASP B N   1 
ATOM   799  C CA  . ASP B 1 26 ? 12.34927 32.02929 32.19652  1.000 64.85572  ? 72  ASP B CA  1 
ATOM   800  C C   . ASP B 1 26 ? 11.65245 31.29681 31.05975  1.000 63.12988  ? 72  ASP B C   1 
ATOM   801  O O   . ASP B 1 26 ? 10.47997 31.56423 30.76720  1.000 62.91525  ? 72  ASP B O   1 
ATOM   802  C CB  . ASP B 1 26 ? 13.10769 33.24106 31.65938  1.000 68.75826  ? 72  ASP B CB  1 
ATOM   803  C CG  . ASP B 1 26 ? 13.93244 33.92715 32.72606  1.000 71.53725  ? 72  ASP B CG  1 
ATOM   804  O OD1 . ASP B 1 26 ? 13.33083 34.52353 33.64543  1.000 69.65726  ? 72  ASP B OD1 1 
ATOM   805  O OD2 . ASP B 1 26 ? 15.17754 33.87757 32.63454  1.000 71.86361  ? 72  ASP B OD2 1 
ATOM   806  N N   . TYR B 1 27 ? 12.36820 30.37878 30.40562  1.000 60.41433  ? 73  TYR B N   1 
ATOM   807  C CA  . TYR B 1 27 ? 11.80079 29.60238 29.30845  1.000 59.72582  ? 73  TYR B CA  1 
ATOM   808  C C   . TYR B 1 27 ? 10.50790 28.90857 29.71529  1.000 56.79901  ? 73  TYR B C   1 
ATOM   809  O O   . TYR B 1 27 ? 9.53072  28.91104 28.95859  1.000 56.44981  ? 73  TYR B O   1 
ATOM   810  C CB  . TYR B 1 27 ? 12.84330 28.59004 28.83127  1.000 54.78366  ? 73  TYR B CB  1 
ATOM   811  C CG  . TYR B 1 27 ? 12.31445 27.35804 28.13555  1.000 53.32977  ? 73  TYR B CG  1 
ATOM   812  C CD1 . TYR B 1 27 ? 11.92543 27.38906 26.79867  1.000 52.01414  ? 73  TYR B CD1 1 
ATOM   813  C CD2 . TYR B 1 27 ? 12.23040 26.15037 28.81252  1.000 53.30113  ? 73  TYR B CD2 1 
ATOM   814  C CE1 . TYR B 1 27 ? 11.45915 26.24913 26.16603  1.000 50.72625  ? 73  TYR B CE1 1 
ATOM   815  C CE2 . TYR B 1 27 ? 11.76725 25.01182 28.18958  1.000 52.02119  ? 73  TYR B CE2 1 
ATOM   816  C CZ  . TYR B 1 27 ? 11.38292 25.06174 26.87290  1.000 50.74414  ? 73  TYR B CZ  1 
ATOM   817  O OH  . TYR B 1 27 ? 10.92591 23.91551 26.27110  1.000 49.52138  ? 73  TYR B OH  1 
ATOM   818  N N   . LEU B 1 28 ? 10.47983 28.30940 30.90893  1.000 58.70371  ? 74  LEU B N   1 
ATOM   819  C CA  . LEU B 1 28 ? 9.26809  27.62649 31.35154  1.000 57.92118  ? 74  LEU B CA  1 
ATOM   820  C C   . LEU B 1 28 ? 8.09022  28.58783 31.47335  1.000 61.46137  ? 74  LEU B C   1 
ATOM   821  O O   . LEU B 1 28 ? 6.93238  28.16483 31.36212  1.000 60.24850  ? 74  LEU B O   1 
ATOM   822  C CB  . LEU B 1 28 ? 9.50892  26.91682 32.68378  1.000 60.76369  ? 74  LEU B CB  1 
ATOM   823  C CG  . LEU B 1 28 ? 10.48379 25.73989 32.63649  1.000 57.81340  ? 74  LEU B CG  1 
ATOM   824  C CD1 . LEU B 1 28 ? 10.85974 25.31626 34.05363  1.000 58.04594  ? 74  LEU B CD1 1 
ATOM   825  C CD2 . LEU B 1 28 ? 9.90873  24.57446 31.83922  1.000 55.24659  ? 74  LEU B CD2 1 
ATOM   826  N N   . LEU B 1 29 ? 8.36156  29.88063 31.68482  1.000 61.11434  ? 75  LEU B N   1 
ATOM   827  C CA  . LEU B 1 29 ? 7.30195  30.87678 31.81697  1.000 63.58195  ? 75  LEU B CA  1 
ATOM   828  C C   . LEU B 1 29 ? 6.80498  31.40094 30.47985  1.000 61.47863  ? 75  LEU B C   1 
ATOM   829  O O   . LEU B 1 29 ? 5.81752  32.14469 30.46016  1.000 58.34539  ? 75  LEU B O   1 
ATOM   830  C CB  . LEU B 1 29 ? 7.76840  32.05809 32.67455  1.000 63.57228  ? 75  LEU B CB  1 
ATOM   831  C CG  . LEU B 1 29 ? 8.30963  31.73138 34.06831  1.000 64.92384  ? 75  LEU B CG  1 
ATOM   832  C CD1 . LEU B 1 29 ? 8.68799  33.01352 34.79050  1.000 64.97269  ? 75  LEU B CD1 1 
ATOM   833  C CD2 . LEU B 1 29 ? 7.29686  30.93365 34.88406  1.000 66.71077  ? 75  LEU B CD2 1 
ATOM   834  N N   . ASP B 1 30 ? 7.47479  31.04906 29.37853  1.000 59.97470  ? 76  ASP B N   1 
ATOM   835  C CA  . ASP B 1 30 ? 7.08542  31.44640 28.02505  1.000 58.64275  ? 76  ASP B CA  1 
ATOM   836  C C   . ASP B 1 30 ? 6.39322  30.24519 27.38538  1.000 57.20604  ? 76  ASP B C   1 
ATOM   837  O O   . ASP B 1 30 ? 7.03316  29.38478 26.77904  1.000 56.47513  ? 76  ASP B O   1 
ATOM   838  C CB  . ASP B 1 30 ? 8.29961  31.89827 27.21794  1.000 58.14337  ? 76  ASP B CB  1 
ATOM   839  C CG  . ASP B 1 30 ? 7.92411  32.53616 25.88754  1.000 57.18847  ? 76  ASP B CG  1 
ATOM   840  O OD1 . ASP B 1 30 ? 6.88975  32.15907 25.28965  1.000 56.30222  ? 76  ASP B OD1 1 
ATOM   841  O OD2 . ASP B 1 30 ? 8.68213  33.41605 25.42655  1.000 59.74122  ? 76  ASP B OD2 1 
ATOM   842  N N   . ASN B 1 31 ? 5.06583  30.19876 27.51744  1.000 55.04483  ? 77  ASN B N   1 
ATOM   843  C CA  . ASN B 1 31 ? 4.30567  29.03985 27.05944  1.000 56.44498  ? 77  ASN B CA  1 
ATOM   844  C C   . ASN B 1 31 ? 4.44554  28.83652 25.55463  1.000 52.73454  ? 77  ASN B C   1 
ATOM   845  O O   . ASN B 1 31 ? 4.57425  27.70111 25.08357  1.000 51.60109  ? 77  ASN B O   1 
ATOM   846  C CB  . ASN B 1 31 ? 2.82971  29.20180 27.44194  1.000 60.79914  ? 77  ASN B CB  1 
ATOM   847  C CG  . ASN B 1 31 ? 2.12595  27.86792 27.64053  1.000 62.13679  ? 77  ASN B CG  1 
ATOM   848  O OD1 . ASN B 1 31 ? 2.25161  26.96137 26.81759  1.000 65.49592  ? 77  ASN B OD1 1 
ATOM   849  N ND2 . ASN B 1 31 ? 1.35850  27.75573 28.71526  1.000 66.37060  ? 77  ASN B ND2 1 
ATOM   850  N N   . LYS B 1 32 ? 4.43169  29.92212 24.78155  1.000 53.72781  ? 78  LYS B N   1 
ATOM   851  C CA  . LYS B 1 32 ? 4.53088  29.77458 23.33437  1.000 53.52144  ? 78  LYS B CA  1 
ATOM   852  C C   . LYS B 1 32 ? 5.87492  29.17576 22.94278  1.000 47.50435  ? 78  LYS B C   1 
ATOM   853  O O   . LYS B 1 32 ? 5.94601  28.30534 22.06772  1.000 45.19343  ? 78  LYS B O   1 
ATOM   854  C CB  . LYS B 1 32 ? 4.31423  31.12793 22.65460  1.000 55.95986  ? 78  LYS B CB  1 
ATOM   855  C CG  . LYS B 1 32 ? 3.88414  31.03336 21.19170  1.000 61.73075  ? 78  LYS B CG  1 
ATOM   856  C CD  . LYS B 1 32 ? 3.27533  32.35005 20.69534  1.000 64.51457  ? 78  LYS B CD  1 
ATOM   857  C CE  . LYS B 1 32 ? 4.28994  33.24339 19.98729  1.000 66.39952  ? 78  LYS B CE  1 
ATOM   858  N NZ  . LYS B 1 32 ? 4.91613  32.58604 18.79580  1.000 72.28796  ? 78  LYS B NZ  1 
ATOM   859  N N   . GLN B 1 33 ? 6.94283  29.59347 23.62245  1.000 50.26075  ? 79  GLN B N   1 
ATOM   860  C CA  . GLN B 1 33 ? 8.27949  29.08074 23.33435  1.000 45.82156  ? 79  GLN B CA  1 
ATOM   861  C C   . GLN B 1 33 ? 8.39500  27.60532 23.68306  1.000 47.08192  ? 79  GLN B C   1 
ATOM   862  O O   . GLN B 1 33 ? 9.01409  26.83099 22.94217  1.000 41.56203  ? 79  GLN B O   1 
ATOM   863  C CB  . GLN B 1 33 ? 9.30393  29.88191 24.12925  1.000 47.65658  ? 79  GLN B CB  1 
ATOM   864  C CG  . GLN B 1 33 ? 10.75238 29.73229 23.71972  1.000 42.42083  ? 79  GLN B CG  1 
ATOM   865  C CD  . GLN B 1 33 ? 11.61575 30.76251 24.41037  1.000 43.49346  ? 79  GLN B CD  1 
ATOM   866  O OE1 . GLN B 1 33 ? 11.67882 30.80995 25.64212  1.000 48.27319  ? 79  GLN B OE1 1 
ATOM   867  N NE2 . GLN B 1 33 ? 12.27189 31.60188 23.63267  1.000 38.48746  ? 79  GLN B NE2 1 
ATOM   868  N N   . VAL B 1 34 ? 7.79984  27.20191 24.80915  1.000 44.76769  ? 80  VAL B N   1 
ATOM   869  C CA  . VAL B 1 34 ? 7.82784  25.80333 25.22553  1.000 46.56660  ? 80  VAL B CA  1 
ATOM   870  C C   . VAL B 1 34 ? 7.17097  24.91505 24.17515  1.000 44.24862  ? 80  VAL B C   1 
ATOM   871  O O   . VAL B 1 34 ? 7.71501  23.87357 23.78783  1.000 43.75057  ? 80  VAL B O   1 
ATOM   872  C CB  . VAL B 1 34 ? 7.15451  25.64465 26.60110  1.000 46.07920  ? 80  VAL B CB  1 
ATOM   873  C CG1 . VAL B 1 34 ? 6.95326  24.16780 26.92271  1.000 45.55138  ? 80  VAL B CG1 1 
ATOM   874  C CG2 . VAL B 1 34 ? 7.97807  26.34819 27.66928  1.000 47.32360  ? 80  VAL B CG2 1 
ATOM   875  N N   . VAL B 1 35 ? 5.97466  25.29498 23.72687  1.000 43.38837  ? 81  VAL B N   1 
ATOM   876  C CA  . VAL B 1 35 ? 5.27415  24.51319 22.71192  1.000 44.86449  ? 81  VAL B CA  1 
ATOM   877  C C   . VAL B 1 35 ? 6.09692  24.44202 21.42939  1.000 44.53625  ? 81  VAL B C   1 
ATOM   878  O O   . VAL B 1 35 ? 6.15255  23.39831 20.76556  1.000 43.44124  ? 81  VAL B O   1 
ATOM   879  C CB  . VAL B 1 35 ? 3.87577  25.10659 22.45800  1.000 50.29605  ? 81  VAL B CB  1 
ATOM   880  C CG1 . VAL B 1 35 ? 3.22795  24.44678 21.25236  1.000 52.93777  ? 81  VAL B CG1 1 
ATOM   881  C CG2 . VAL B 1 35 ? 3.00417  24.94235 23.69144  1.000 53.99141  ? 81  VAL B CG2 1 
ATOM   882  N N   . LEU B 1 36 ? 6.73994  25.54881 21.05460  1.000 41.24868  ? 82  LEU B N   1 
ATOM   883  C CA  . LEU B 1 36 ? 7.51591  25.56104 19.81962  1.000 40.63634  ? 82  LEU B CA  1 
ATOM   884  C C   . LEU B 1 36 ? 8.68285  24.58916 19.90908  1.000 38.60145  ? 82  LEU B C   1 
ATOM   885  O O   . LEU B 1 36 ? 8.93517  23.81691 18.97615  1.000 36.34124  ? 82  LEU B O   1 
ATOM   886  C CB  . LEU B 1 36 ? 7.99661  26.98252 19.51306  1.000 40.81026  ? 82  LEU B CB  1 
ATOM   887  C CG  . LEU B 1 36 ? 8.97269  27.29138 18.36443  1.000 40.28313  ? 82  LEU B CG  1 
ATOM   888  C CD1 . LEU B 1 36 ? 8.94079  28.78692 18.12542  1.000 45.35930  ? 82  LEU B CD1 1 
ATOM   889  C CD2 . LEU B 1 36 ? 10.41303 26.86320 18.58854  1.000 38.85128  ? 82  LEU B CD2 1 
ATOM   890  N N   . THR B 1 37 ? 9.40948  24.60939 21.03089  1.000 38.69619  ? 83  THR B N   1 
ATOM   891  C CA  . THR B 1 37 ? 10.54705 23.71019 21.15515  1.000 36.68823  ? 83  THR B CA  1 
ATOM   892  C C   . THR B 1 37 ? 10.10536 22.25141 21.11656  1.000 38.37097  ? 83  THR B C   1 
ATOM   893  O O   . THR B 1 37 ? 10.79395 21.41848 20.51608  1.000 35.51097  ? 83  THR B O   1 
ATOM   894  C CB  . THR B 1 37 ? 11.35368 24.01027 22.43401  1.000 39.36048  ? 83  THR B CB  1 
ATOM   895  O OG1 . THR B 1 37 ? 10.52728 23.92077 23.60404  1.000 39.99623  ? 83  THR B OG1 1 
ATOM   896  C CG2 . THR B 1 37 ? 11.97452 25.41203 22.36499  1.000 39.71551  ? 83  THR B CG2 1 
ATOM   897  N N   . PHE B 1 38 ? 8.92480  21.92493 21.66672  1.000 34.20193  ? 84  PHE B N   1 
ATOM   898  C CA  . PHE B 1 38 ? 8.51554  20.52506 21.63558  1.000 34.54350  ? 84  PHE B CA  1 
ATOM   899  C C   . PHE B 1 38 ? 8.11833  20.06856 20.23709  1.000 35.89538  ? 84  PHE B C   1 
ATOM   900  O O   . PHE B 1 38 ? 8.38784  18.91900 19.87150  1.000 36.05663  ? 84  PHE B O   1 
ATOM   901  C CB  . PHE B 1 38 ? 7.37507  20.26920 22.62923  1.000 41.21408  ? 84  PHE B CB  1 
ATOM   902  C CG  . PHE B 1 38 ? 7.85846  19.91043 23.99494  1.000 38.38462  ? 84  PHE B CG  1 
ATOM   903  C CD1 . PHE B 1 38 ? 8.36566  20.88616 24.83718  1.000 40.61184  ? 84  PHE B CD1 1 
ATOM   904  C CD2 . PHE B 1 38 ? 7.87406  18.59175 24.41437  1.000 41.68937  ? 84  PHE B CD2 1 
ATOM   905  C CE1 . PHE B 1 38 ? 8.83227  20.55468 26.09997  1.000 43.79022  ? 84  PHE B CE1 1 
ATOM   906  C CE2 . PHE B 1 38 ? 8.33712  18.25311 25.67496  1.000 45.74881  ? 84  PHE B CE2 1 
ATOM   907  C CZ  . PHE B 1 38 ? 8.81751  19.23504 26.51803  1.000 43.60713  ? 84  PHE B CZ  1 
ATOM   908  N N   . LYS B 1 39 ? 7.50748  20.93986 19.43422  1.000 37.53168  ? 85  LYS B N   1 
ATOM   909  C CA  . LYS B 1 39 ? 7.25994  20.59144 18.03836  1.000 39.30814  ? 85  LYS B CA  1 
ATOM   910  C C   . LYS B 1 39 ? 8.57073  20.36996 17.28610  1.000 36.28127  ? 85  LYS B C   1 
ATOM   911  O O   . LYS B 1 39 ? 8.67206  19.46334 16.45206  1.000 36.31831  ? 85  LYS B O   1 
ATOM   912  C CB  . LYS B 1 39 ? 6.41698  21.67642 17.36666  1.000 43.60545  ? 85  LYS B CB  1 
ATOM   913  C CG  . LYS B 1 39 ? 5.04723  21.88800 18.03692  1.000 47.40288  ? 85  LYS B CG  1 
ATOM   914  C CD  . LYS B 1 39 ? 3.88627  21.84926 17.03867  1.000 55.53244  ? 85  LYS B CD  1 
ATOM   915  C CE  . LYS B 1 39 ? 2.70616  22.67397 17.54057  1.000 58.30417  ? 85  LYS B CE  1 
ATOM   916  N NZ  . LYS B 1 39 ? 1.80238  23.14771 16.44986  1.000 69.17252  ? 85  LYS B NZ  1 
ATOM   917  N N   . LEU B 1 40 ? 9.58229  21.19203 17.56823  1.000 34.20716  ? 86  LEU B N   1 
ATOM   918  C CA  . LEU B 1 40 ? 10.90477 20.98381 16.98229  1.000 33.56977  ? 86  LEU B CA  1 
ATOM   919  C C   . LEU B 1 40 ? 11.47321 19.62073 17.36416  1.000 33.67266  ? 86  LEU B C   1 
ATOM   920  O O   . LEU B 1 40 ? 11.89686 18.84796 16.49636  1.000 32.81387  ? 86  LEU B O   1 
ATOM   921  C CB  . LEU B 1 40 ? 11.84882 22.09148 17.44323  1.000 35.00350  ? 86  LEU B CB  1 
ATOM   922  C CG  . LEU B 1 40 ? 12.01138 23.31273 16.56205  1.000 34.88020  ? 86  LEU B CG  1 
ATOM   923  C CD1 . LEU B 1 40 ? 13.04320 24.25369 17.18579  1.000 31.22318  ? 86  LEU B CD1 1 
ATOM   924  C CD2 . LEU B 1 40 ? 12.42552 22.87329 15.16037  1.000 32.62018  ? 86  LEU B CD2 1 
ATOM   925  N N   . VAL B 1 41 ? 11.51496 19.31847 18.66764  1.000 31.93032  ? 87  VAL B N   1 
ATOM   926  C CA  . VAL B 1 41 ? 12.03796 18.03042 19.12191  1.000 35.13656  ? 87  VAL B CA  1 
ATOM   927  C C   . VAL B 1 41 ? 11.25346 16.88408 18.49872  1.000 37.69073  ? 87  VAL B C   1 
ATOM   928  O O   . VAL B 1 41 ? 11.83000 15.87674 18.07756  1.000 40.93028  ? 87  VAL B O   1 
ATOM   929  C CB  . VAL B 1 41 ? 12.02153 17.94478 20.66135  1.000 36.07545  ? 87  VAL B CB  1 
ATOM   930  C CG1 . VAL B 1 41 ? 12.53170 16.58044 21.12451  1.000 36.98312  ? 87  VAL B CG1 1 
ATOM   931  C CG2 . VAL B 1 41 ? 12.85713 19.03424 21.25785  1.000 31.28082  ? 87  VAL B CG2 1 
ATOM   932  N N   . HIS B 1 42 ? 9.92520  17.02048 18.43832  1.000 38.75157  ? 88  HIS B N   1 
ATOM   933  C CA  . HIS B 1 42 ? 9.07569  15.97943 17.86506  1.000 40.29101  ? 88  HIS B CA  1 
ATOM   934  C C   . HIS B 1 42 ? 9.54550  15.55572 16.47905  1.000 42.55724  ? 88  HIS B C   1 
ATOM   935  O O   . HIS B 1 42 ? 9.49111  14.37083 16.13071  1.000 44.78090  ? 88  HIS B O   1 
ATOM   936  C CB  . HIS B 1 42 ? 7.63701  16.48450 17.79719  1.000 42.79655  ? 88  HIS B CB  1 
ATOM   937  C CG  . HIS B 1 42 ? 6.66213  15.46825 17.29697  1.000 49.29619  ? 88  HIS B CG  1 
ATOM   938  N ND1 . HIS B 1 42 ? 6.12229  15.51920 16.02972  1.000 52.72616  ? 88  HIS B ND1 1 
ATOM   939  C CD2 . HIS B 1 42 ? 6.11554  14.38600 17.89703  1.000 52.96326  ? 88  HIS B CD2 1 
ATOM   940  C CE1 . HIS B 1 42 ? 5.28777  14.50843 15.86884  1.000 58.59423  ? 88  HIS B CE1 1 
ATOM   941  N NE2 . HIS B 1 42 ? 5.26285  13.80753 16.98819  1.000 58.96232  ? 88  HIS B NE2 1 
ATOM   942  N N   . HIS B 1 43 ? 10.00686 16.51042 15.67558  1.000 39.40132  ? 89  HIS B N   1 
ATOM   943  C CA  . HIS B 1 43 ? 10.34074 16.27766 14.27671  1.000 39.71155  ? 89  HIS B CA  1 
ATOM   944  C C   . HIS B 1 43 ? 11.82782 16.03790 14.05289  1.000 35.66344  ? 89  HIS B C   1 
ATOM   945  O O   . HIS B 1 43 ? 12.23467 15.80686 12.91159  1.000 37.38197  ? 89  HIS B O   1 
ATOM   946  C CB  . HIS B 1 43 ? 9.89435  17.47591 13.43230  1.000 40.41835  ? 89  HIS B CB  1 
ATOM   947  C CG  . HIS B 1 43 ? 8.41904  17.54280 13.21138  1.000 46.53373  ? 89  HIS B CG  1 
ATOM   948  N ND1 . HIS B 1 43 ? 7.77587  16.79486 12.25180  1.000 51.16929  ? 89  HIS B ND1 1 
ATOM   949  C CD2 . HIS B 1 43 ? 7.45533  18.25121 13.84718  1.000 47.41809  ? 89  HIS B CD2 1 
ATOM   950  C CE1 . HIS B 1 43 ? 6.47850  17.04322 12.29848  1.000 54.63551  ? 89  HIS B CE1 1 
ATOM   951  N NE2 . HIS B 1 43 ? 6.25899  17.92682 13.25616  1.000 54.61559  ? 89  HIS B NE2 1 
ATOM   952  N N   . SER B 1 44 ? 12.64101 16.06332 15.10041  1.000 34.19885  ? 90  SER B N   1 
ATOM   953  C CA  . SER B 1 44 ? 14.08620 16.02476 14.94867  1.000 33.91026  ? 90  SER B CA  1 
ATOM   954  C C   . SER B 1 44 ? 14.62621 14.64741 15.29702  1.000 39.78292  ? 90  SER B C   1 
ATOM   955  O O   . SER B 1 44 ? 14.00366 13.87733 16.02830  1.000 44.42397  ? 90  SER B O   1 
ATOM   956  C CB  . SER B 1 44 ? 14.75770 17.07410 15.83716  1.000 31.26801  ? 90  SER B CB  1 
ATOM   957  O OG  . SER B 1 44 ? 14.22261 18.35698 15.58096  1.000 33.72380  ? 90  SER B OG  1 
ATOM   958  N N   . LYS B 1 45 ? 15.78973 14.33324 14.73144  1.000 36.30846  ? 91  LYS B N   1 
ATOM   959  C CA  . LYS B 1 45 ? 16.57680 13.18998 15.16456  1.000 42.64692  ? 91  LYS B CA  1 
ATOM   960  C C   . LYS B 1 45 ? 17.88761 13.60030 15.81373  1.000 38.83625  ? 91  LYS B C   1 
ATOM   961  O O   . LYS B 1 45 ? 18.56309 12.75473 16.40381  1.000 40.43258  ? 91  LYS B O   1 
ATOM   962  C CB  . LYS B 1 45 ? 16.83791 12.22250 14.00382  1.000 42.42355  ? 91  LYS B CB  1 
ATOM   963  C CG  . LYS B 1 45 ? 17.45260 12.80992 12.77547  1.000 43.68275  ? 91  LYS B CG  1 
ATOM   964  C CD  . LYS B 1 45 ? 17.59418 11.73606 11.69148  1.000 49.78457  ? 91  LYS B CD  1 
ATOM   965  C CE  . LYS B 1 45 ? 16.53936 10.62736 11.81187  1.000 52.13465  ? 91  LYS B CE  1 
ATOM   966  N NZ  . LYS B 1 45 ? 15.12270 11.09620 11.62898  1.000 51.53287  ? 91  LYS B NZ  1 
ATOM   967  N N   . LYS B 1 46 ? 18.24151 14.87597 15.73972  1.000 33.68840  ? 92  LYS B N   1 
ATOM   968  C CA  . LYS B 1 46 ? 19.46932 15.40575 16.30531  1.000 35.08395  ? 92  LYS B CA  1 
ATOM   969  C C   . LYS B 1 46 ? 19.11818 16.70837 17.00440  1.000 33.77384  ? 92  LYS B C   1 
ATOM   970  O O   . LYS B 1 46 ? 18.46821 17.56858 16.40646  1.000 31.13518  ? 92  LYS B O   1 
ATOM   971  C CB  . LYS B 1 46 ? 20.49820 15.66222 15.20232  1.000 35.89904  ? 92  LYS B CB  1 
ATOM   972  C CG  . LYS B 1 46 ? 21.92127 15.80282 15.65832  1.000 44.07941  ? 92  LYS B CG  1 
ATOM   973  C CD  . LYS B 1 46 ? 22.86967 15.79714 14.45345  1.000 47.43104  ? 92  LYS B CD  1 
ATOM   974  C CE  . LYS B 1 46 ? 24.02875 16.75650 14.66150  1.000 47.03016  ? 92  LYS B CE  1 
ATOM   975  N NZ  . LYS B 1 46 ? 25.23841 16.28825 13.95350  1.000 49.43690  ? 92  LYS B NZ  1 
ATOM   976  N N   . ILE B 1 47 ? 19.55025 16.86222 18.25405  1.000 30.13663  ? 93  ILE B N   1 
ATOM   977  C CA  . ILE B 1 47 ? 19.38517 18.11087 18.99056  1.000 30.63083  ? 93  ILE B CA  1 
ATOM   978  C C   . ILE B 1 47 ? 20.73842 18.51576 19.55495  1.000 31.02161  ? 93  ILE B C   1 
ATOM   979  O O   . ILE B 1 47 ? 21.36810 17.73691 20.27798  1.000 33.55344  ? 93  ILE B O   1 
ATOM   980  C CB  . ILE B 1 47 ? 18.37272 17.99130 20.14955  1.000 32.71157  ? 93  ILE B CB  1 
ATOM   981  C CG1 . ILE B 1 47 ? 16.97306 17.57324 19.67648  1.000 32.44283  ? 93  ILE B CG1 1 
ATOM   982  C CG2 . ILE B 1 47 ? 18.33190 19.31029 20.92141  1.000 28.80124  ? 93  ILE B CG2 1 
ATOM   983  C CD1 . ILE B 1 47 ? 16.33239 18.51104 18.74728  1.000 31.46010  ? 93  ILE B CD1 1 
ATOM   984  N N   . THR B 1 48 ? 21.16909 19.73565 19.25979  1.000 28.24165  ? 94  THR B N   1 
ATOM   985  C CA  . THR B 1 48 ? 22.38694 20.28983 19.83791  1.000 32.59753  ? 94  THR B CA  1 
ATOM   986  C C   . THR B 1 48 ? 22.02956 21.45593 20.74904  1.000 30.01217  ? 94  THR B C   1 
ATOM   987  O O   . THR B 1 48 ? 21.26115 22.33543 20.35568  1.000 26.14047  ? 94  THR B O   1 
ATOM   988  C CB  . THR B 1 48 ? 23.36844 20.74733 18.74529  1.000 33.88044  ? 94  THR B CB  1 
ATOM   989  O OG1 . THR B 1 48 ? 23.78597 19.61015 17.97929  1.000 34.38512  ? 94  THR B OG1 1 
ATOM   990  C CG2 . THR B 1 48 ? 24.58198 21.41022 19.35946  1.000 31.91267  ? 94  THR B CG2 1 
ATOM   991  N N   . LEU B 1 49 ? 22.59797 21.47277 21.95759  1.000 30.85934  ? 95  LEU B N   1 
ATOM   992  C CA  . LEU B 1 49 ? 22.35929 22.55621 22.90246  1.000 30.49391  ? 95  LEU B CA  1 
ATOM   993  C C   . LEU B 1 49 ? 23.68376 23.21727 23.25030  1.000 34.69493  ? 95  LEU B C   1 
ATOM   994  O O   . LEU B 1 49 ? 24.61630 22.53902 23.68130  1.000 35.36539  ? 95  LEU B O   1 
ATOM   995  C CB  . LEU B 1 49 ? 21.66462 22.03939 24.16404  1.000 32.84477  ? 95  LEU B CB  1 
ATOM   996  C CG  . LEU B 1 49 ? 20.26674 21.45443 23.93261  1.000 32.28915  ? 95  LEU B CG  1 
ATOM   997  C CD1 . LEU B 1 49 ? 19.88240 20.46897 25.02621  1.000 36.06892  ? 95  LEU B CD1 1 
ATOM   998  C CD2 . LEU B 1 49 ? 19.22624 22.56572 23.81684  1.000 30.27813  ? 95  LEU B CD2 1 
ATOM   999  N N   . ILE B 1 50 ? 23.75647 24.53570 23.08949  1.000 31.27970  ? 96  ILE B N   1 
ATOM   1000 C CA  . ILE B 1 50 ? 24.99822 25.28782 23.25852  1.000 35.78757  ? 96  ILE B CA  1 
ATOM   1001 C C   . ILE B 1 50 ? 24.79511 26.33901 24.33992  1.000 34.97779  ? 96  ILE B C   1 
ATOM   1002 O O   . ILE B 1 50 ? 23.93128 27.21088 24.21280  1.000 29.71600  ? 96  ILE B O   1 
ATOM   1003 C CB  . ILE B 1 50 ? 25.44547 25.95944 21.94978  1.000 36.02967  ? 96  ILE B CB  1 
ATOM   1004 C CG1 . ILE B 1 50 ? 25.40529 24.96971 20.78711  1.000 35.88463  ? 96  ILE B CG1 1 
ATOM   1005 C CG2 . ILE B 1 50 ? 26.83498 26.55805 22.11610  1.000 37.92377  ? 96  ILE B CG2 1 
ATOM   1006 C CD1 . ILE B 1 50 ? 25.53451 25.64195 19.42934  1.000 39.13027  ? 96  ILE B CD1 1 
ATOM   1007 N N   . GLY B 1 51 ? 25.59727 26.27537 25.39124  1.000 37.48787  ? 97  GLY B N   1 
ATOM   1008 C CA  . GLY B 1 51 ? 25.47404 27.24734 26.45423  1.000 37.79928  ? 97  GLY B CA  1 
ATOM   1009 C C   . GLY B 1 51 ? 26.11410 26.70916 27.71610  1.000 45.45023  ? 97  GLY B C   1 
ATOM   1010 O O   . GLY B 1 51 ? 26.84953 25.72707 27.68503  1.000 43.42317  ? 97  GLY B O   1 
ATOM   1011 N N   . ASP B 1 52 ? 25.80958 27.37270 28.82639  1.000 43.94432  ? 98  ASP B N   1 
ATOM   1012 C CA  . ASP B 1 52 ? 26.38594 26.94704 30.09674  1.000 51.64445  ? 98  ASP B CA  1 
ATOM   1013 C C   . ASP B 1 52 ? 25.99298 25.50058 30.37999  1.000 49.00379  ? 98  ASP B C   1 
ATOM   1014 O O   . ASP B 1 52 ? 24.84295 25.10066 30.17450  1.000 46.50353  ? 98  ASP B O   1 
ATOM   1015 C CB  . ASP B 1 52 ? 25.94604 27.86963 31.23167  1.000 51.24674  ? 98  ASP B CB  1 
ATOM   1016 C CG  . ASP B 1 52 ? 26.28697 27.30602 32.60589  1.000 59.28816  ? 98  ASP B CG  1 
ATOM   1017 O OD1 . ASP B 1 52 ? 25.60234 26.36679 33.08762  1.000 59.15571  ? 98  ASP B OD1 1 
ATOM   1018 O OD2 . ASP B 1 52 ? 27.28068 27.78655 33.19074  1.000 58.28123  ? 98  ASP B OD2 1 
ATOM   1019 N N   . ALA B 1 53 ? 26.96887 24.72346 30.85965  1.000 51.05094  ? 99  ALA B N   1 
ATOM   1020 C CA  . ALA B 1 53 ? 26.81177 23.27641 31.00687  1.000 51.55369  ? 99  ALA B CA  1 
ATOM   1021 C C   . ALA B 1 53 ? 25.57930 22.89954 31.82120  1.000 52.17641  ? 99  ALA B C   1 
ATOM   1022 O O   . ALA B 1 53 ? 24.86959 21.94622 31.47908  1.000 50.98900  ? 99  ALA B O   1 
ATOM   1023 C CB  . ALA B 1 53 ? 28.06851 22.68304 31.64690  1.000 51.74364  ? 99  ALA B CB  1 
ATOM   1024 N N   . ASN B 1 54 ? 25.31689 23.62240 32.91078  1.000 54.73405  ? 100 ASN B N   1 
ATOM   1025 C CA  . ASN B 1 54 ? 24.15744 23.30917 33.73743  1.000 51.80547  ? 100 ASN B CA  1 
ATOM   1026 C C   . ASN B 1 54 ? 22.86079 23.65354 33.01931  1.000 51.85588  ? 100 ASN B C   1 
ATOM   1027 O O   . ASN B 1 54 ? 21.86296 22.93269 33.14329  1.000 48.52852  ? 100 ASN B O   1 
ATOM   1028 C CB  . ASN B 1 54 ? 24.25801 24.04691 35.06991  1.000 58.78907  ? 100 ASN B CB  1 
ATOM   1029 C CG  . ASN B 1 54 ? 25.30866 23.45147 35.97470  1.000 60.80043  ? 100 ASN B CG  1 
ATOM   1030 O OD1 . ASN B 1 54 ? 25.44291 22.22931 36.06624  1.000 65.38980  ? 100 ASN B OD1 1 
ATOM   1031 N ND2 . ASN B 1 54 ? 26.06435 24.30903 36.65322  1.000 65.42911  ? 100 ASN B ND2 1 
ATOM   1032 N N   . LYS B 1 55 ? 22.86549 24.74952 32.25987  1.000 49.89829  ? 101 LYS B N   1 
ATOM   1033 C CA  . LYS B 1 55 ? 21.67410 25.19440 31.54678  1.000 50.88167  ? 101 LYS B CA  1 
ATOM   1034 C C   . LYS B 1 55 ? 21.26978 24.18793 30.47694  1.000 47.05395  ? 101 LYS B C   1 
ATOM   1035 O O   . LYS B 1 55 ? 20.08789 23.84908 30.33650  1.000 44.39035  ? 101 LYS B O   1 
ATOM   1036 C CB  . LYS B 1 55 ? 21.95886 26.55678 30.92064  1.000 50.22499  ? 101 LYS B CB  1 
ATOM   1037 C CG  . LYS B 1 55 ? 22.21563 27.62248 31.96139  1.000 55.79857  ? 101 LYS B CG  1 
ATOM   1038 C CD  . LYS B 1 55 ? 21.55014 28.94385 31.65939  1.000 58.42383  ? 101 LYS B CD  1 
ATOM   1039 C CE  . LYS B 1 55 ? 22.23824 30.02501 32.47121  1.000 65.21425  ? 101 LYS B CE  1 
ATOM   1040 N NZ  . LYS B 1 55 ? 23.67365 30.17801 32.09325  1.000 65.10750  ? 101 LYS B NZ  1 
ATOM   1041 N N   . ILE B 1 56 ? 22.24031 23.71486 29.69521  1.000 44.51756  ? 102 ILE B N   1 
ATOM   1042 C CA  . ILE B 1 56 ? 21.92170 22.78139 28.62305  1.000 43.23314  ? 102 ILE B CA  1 
ATOM   1043 C C   . ILE B 1 56 ? 21.51460 21.42144 29.18066  1.000 45.40028  ? 102 ILE B C   1 
ATOM   1044 O O   . ILE B 1 56 ? 20.73745 20.69588 28.54661  1.000 42.03279  ? 102 ILE B O   1 
ATOM   1045 C CB  . ILE B 1 56 ? 23.10792 22.68988 27.65005  1.000 43.12773  ? 102 ILE B CB  1 
ATOM   1046 C CG1 . ILE B 1 56 ? 24.37974 22.25127 28.38285  1.000 44.59162  ? 102 ILE B CG1 1 
ATOM   1047 C CG2 . ILE B 1 56 ? 23.33283 24.03993 26.98428  1.000 41.62836  ? 102 ILE B CG2 1 
ATOM   1048 C CD1 . ILE B 1 56 ? 25.56753 22.03935 27.45793  1.000 45.59599  ? 102 ILE B CD1 1 
ATOM   1049 N N   . LEU B 1 57 ? 22.00806 21.05375 30.37185  1.000 45.30419  ? 103 LEU B N   1 
ATOM   1050 C CA  . LEU B 1 57 ? 21.53317 19.82677 31.00748  1.000 46.13664  ? 103 LEU B CA  1 
ATOM   1051 C C   . LEU B 1 57 ? 20.07564 19.95619 31.43478  1.000 44.92397  ? 103 LEU B C   1 
ATOM   1052 O O   . LEU B 1 57 ? 19.28392 19.02963 31.22701  1.000 45.25029  ? 103 LEU B O   1 
ATOM   1053 C CB  . LEU B 1 57 ? 22.40949 19.45638 32.20665  1.000 49.40818  ? 103 LEU B CB  1 
ATOM   1054 C CG  . LEU B 1 57 ? 23.82323 18.94310 31.92673  1.000 49.34585  ? 103 LEU B CG  1 
ATOM   1055 C CD1 . LEU B 1 57 ? 24.67932 18.96248 33.19520  1.000 57.17520  ? 103 LEU B CD1 1 
ATOM   1056 C CD2 . LEU B 1 57 ? 23.76234 17.54522 31.34130  1.000 51.63322  ? 103 LEU B CD2 1 
ATOM   1057 N N   . GLN B 1 58 ? 19.70354 21.10283 32.02157  1.000 47.18192  ? 104 GLN B N   1 
ATOM   1058 C CA  . GLN B 1 58 ? 18.29885 21.38208 32.32134  1.000 48.89719  ? 104 GLN B CA  1 
ATOM   1059 C C   . GLN B 1 58 ? 17.41936 21.13790 31.09867  1.000 44.10723  ? 104 GLN B C   1 
ATOM   1060 O O   . GLN B 1 58 ? 16.39184 20.45784 31.17969  1.000 41.94922  ? 104 GLN B O   1 
ATOM   1061 C CB  . GLN B 1 58 ? 18.12912 22.83848 32.77292  1.000 50.18603  ? 104 GLN B CB  1 
ATOM   1062 C CG  . GLN B 1 58 ? 18.92656 23.30390 33.96579  1.000 53.23620  ? 104 GLN B CG  1 
ATOM   1063 C CD  . GLN B 1 58 ? 18.05963 23.52155 35.16975  1.000 62.38169  ? 104 GLN B CD  1 
ATOM   1064 O OE1 . GLN B 1 58 ? 17.00745 22.89989 35.30857  1.000 67.16159  ? 104 GLN B OE1 1 
ATOM   1065 N NE2 . GLN B 1 58 ? 18.47424 24.43218 36.04088  1.000 63.34207  ? 104 GLN B NE2 1 
ATOM   1066 N N   . TYR B 1 59 ? 17.81258 21.68948 29.95338  1.000 41.28534  ? 105 TYR B N   1 
ATOM   1067 C CA  . TYR B 1 59 ? 16.99277 21.55153 28.75078  1.000 41.32678  ? 105 TYR B CA  1 
ATOM   1068 C C   . TYR B 1 59 ? 16.94525 20.10632 28.27609  1.000 40.13828  ? 105 TYR B C   1 
ATOM   1069 O O   . TYR B 1 59 ? 15.86971 19.58397 27.96439  1.000 38.14294  ? 105 TYR B O   1 
ATOM   1070 C CB  . TYR B 1 59 ? 17.51689 22.46286 27.64596  1.000 37.93555  ? 105 TYR B CB  1 
ATOM   1071 C CG  . TYR B 1 59 ? 17.00733 23.88063 27.71383  1.000 39.12344  ? 105 TYR B CG  1 
ATOM   1072 C CD1 . TYR B 1 59 ? 15.70827 24.19404 27.34196  1.000 39.41691  ? 105 TYR B CD1 1 
ATOM   1073 C CD2 . TYR B 1 59 ? 17.83771 24.91039 28.12760  1.000 41.43845  ? 105 TYR B CD2 1 
ATOM   1074 C CE1 . TYR B 1 59 ? 15.24949 25.50200 27.39572  1.000 44.38790  ? 105 TYR B CE1 1 
ATOM   1075 C CE2 . TYR B 1 59 ? 17.39536 26.20926 28.18235  1.000 43.00667  ? 105 TYR B CE2 1 
ATOM   1076 C CZ  . TYR B 1 59 ? 16.10529 26.50752 27.81510  1.000 45.94510  ? 105 TYR B CZ  1 
ATOM   1077 O OH  . TYR B 1 59 ? 15.68512 27.81766 27.87115  1.000 47.12575  ? 105 TYR B OH  1 
ATOM   1078 N N   . LYS B 1 60 ? 18.10580 19.44534 28.21045  1.000 41.59358  ? 106 LYS B N   1 
ATOM   1079 C CA  . LYS B 1 60 ? 18.14778 18.04582 27.79726  1.000 40.98628  ? 106 LYS B CA  1 
ATOM   1080 C C   . LYS B 1 60 ? 17.26308 17.17759 28.67735  1.000 41.93637  ? 106 LYS B C   1 
ATOM   1081 O O   . LYS B 1 60 ? 16.41485 16.43476 28.17152  1.000 40.69450  ? 106 LYS B O   1 
ATOM   1082 C CB  . LYS B 1 60 ? 19.57497 17.50600 27.84578  1.000 39.91817  ? 106 LYS B CB  1 
ATOM   1083 C CG  . LYS B 1 60 ? 19.65504 16.07326 27.35413  1.000 42.57946  ? 106 LYS B CG  1 
ATOM   1084 C CD  . LYS B 1 60 ? 21.04667 15.67894 26.91053  1.000 45.12989  ? 106 LYS B CD  1 
ATOM   1085 C CE  . LYS B 1 60 ? 21.38514 14.29485 27.43486  1.000 46.91188  ? 106 LYS B CE  1 
ATOM   1086 N NZ  . LYS B 1 60 ? 21.27796 14.19854 28.92316  1.000 54.23632  ? 106 LYS B NZ  1 
ATOM   1087 N N   . ASN B 1 61 ? 17.45580 17.25663 30.00248  1.000 42.33894  ? 107 ASN B N   1 
ATOM   1088 C CA  . ASN B 1 61 ? 16.68862 16.42000 30.92018  1.000 45.69287  ? 107 ASN B CA  1 
ATOM   1089 C C   . ASN B 1 61 ? 15.19928 16.69796 30.80370  1.000 45.54673  ? 107 ASN B C   1 
ATOM   1090 O O   . ASN B 1 61 ? 14.38208 15.77116 30.85365  1.000 48.49723  ? 107 ASN B O   1 
ATOM   1091 C CB  . ASN B 1 61 ? 17.14970 16.64344 32.36585  1.000 48.86304  ? 107 ASN B CB  1 
ATOM   1092 C CG  . ASN B 1 61 ? 18.56728 16.15247 32.61510  1.000 50.49161  ? 107 ASN B CG  1 
ATOM   1093 O OD1 . ASN B 1 61 ? 19.09703 15.33575 31.85685  1.000 51.30341  ? 107 ASN B OD1 1 
ATOM   1094 N ND2 . ASN B 1 61 ? 19.19423 16.65916 33.67517  1.000 53.07191  ? 107 ASN B ND2 1 
ATOM   1095 N N   . TYR B 1 62 ? 14.83341 17.96961 30.63230  1.000 45.40380  ? 108 TYR B N   1 
ATOM   1096 C CA  . TYR B 1 62 ? 13.42746 18.35542 30.54968  1.000 45.73378  ? 108 TYR B CA  1 
ATOM   1097 C C   . TYR B 1 62 ? 12.75011 17.72332 29.33932  1.000 45.61421  ? 108 TYR B C   1 
ATOM   1098 O O   . TYR B 1 62 ? 11.65209 17.16612 29.44871  1.000 43.16367  ? 108 TYR B O   1 
ATOM   1099 C CB  . TYR B 1 62 ? 13.32663 19.87920 30.50415  1.000 45.60887  ? 108 TYR B CB  1 
ATOM   1100 C CG  . TYR B 1 62 ? 11.94607 20.43148 30.23432  1.000 47.27769  ? 108 TYR B CG  1 
ATOM   1101 C CD1 . TYR B 1 62 ? 10.93001 20.31254 31.17758  1.000 48.93739  ? 108 TYR B CD1 1 
ATOM   1102 C CD2 . TYR B 1 62 ? 11.67007 21.10931 29.05672  1.000 45.38844  ? 108 TYR B CD2 1 
ATOM   1103 C CE1 . TYR B 1 62 ? 9.66943  20.83547 30.94026  1.000 47.91084  ? 108 TYR B CE1 1 
ATOM   1104 C CE2 . TYR B 1 62 ? 10.41324 21.63549 28.81121  1.000 46.23459  ? 108 TYR B CE2 1 
ATOM   1105 C CZ  . TYR B 1 62 ? 9.42013  21.49372 29.75159  1.000 51.12268  ? 108 TYR B CZ  1 
ATOM   1106 O OH  . TYR B 1 62 ? 8.17045  22.01747 29.50723  1.000 54.58398  ? 108 TYR B OH  1 
ATOM   1107 N N   . PHE B 1 63 ? 13.40395 17.77863 28.17618  1.000 43.09762  ? 109 PHE B N   1 
ATOM   1108 C CA  . PHE B 1 63 ? 12.82714 17.15967 26.98866  1.000 44.78757  ? 109 PHE B CA  1 
ATOM   1109 C C   . PHE B 1 63 ? 12.72533 15.65255 27.16231  1.000 46.16704  ? 109 PHE B C   1 
ATOM   1110 O O   . PHE B 1 63 ? 11.72748 15.04218 26.76519  1.000 45.44902  ? 109 PHE B O   1 
ATOM   1111 C CB  . PHE B 1 63 ? 13.67834 17.47284 25.75101  1.000 37.72258  ? 109 PHE B CB  1 
ATOM   1112 C CG  . PHE B 1 63 ? 13.66799 18.91619 25.34044  1.000 37.43124  ? 109 PHE B CG  1 
ATOM   1113 C CD1 . PHE B 1 63 ? 12.47620 19.61427 25.20979  1.000 39.11283  ? 109 PHE B CD1 1 
ATOM   1114 C CD2 . PHE B 1 63 ? 14.85811 19.57330 25.06405  1.000 34.70765  ? 109 PHE B CD2 1 
ATOM   1115 C CE1 . PHE B 1 63 ? 12.47559 20.94710 24.81673  1.000 35.31544  ? 109 PHE B CE1 1 
ATOM   1116 C CE2 . PHE B 1 63 ? 14.86191 20.90689 24.67455  1.000 36.63204  ? 109 PHE B CE2 1 
ATOM   1117 C CZ  . PHE B 1 63 ? 13.66536 21.59030 24.55897  1.000 38.01431  ? 109 PHE B CZ  1 
ATOM   1118 N N   . GLN B 1 64 ? 13.76099 15.03778 27.74518  1.000 43.68166  ? 110 GLN B N   1 
ATOM   1119 C CA  . GLN B 1 64 ? 13.76046 13.59550 27.97421  1.000 47.10303  ? 110 GLN B CA  1 
ATOM   1120 C C   . GLN B 1 64 ? 12.75767 13.20354 29.04761  1.000 51.09835  ? 110 GLN B C   1 
ATOM   1121 O O   . GLN B 1 64 ? 12.12188 12.14737 28.95018  1.000 55.01415  ? 110 GLN B O   1 
ATOM   1122 C CB  . GLN B 1 64 ? 15.16269 13.11458 28.34622  1.000 46.33553  ? 110 GLN B CB  1 
ATOM   1123 C CG  . GLN B 1 64 ? 16.17369 13.29012 27.22023  1.000 48.50325  ? 110 GLN B CG  1 
ATOM   1124 C CD  . GLN B 1 64 ? 17.52274 12.68188 27.55100  1.000 53.24903  ? 110 GLN B CD  1 
ATOM   1125 O OE1 . GLN B 1 64 ? 18.14430 12.03476 26.70875  1.000 55.78008  ? 110 GLN B OE1 1 
ATOM   1126 N NE2 . GLN B 1 64 ? 17.97665 12.87477 28.78449  1.000 51.20334  ? 110 GLN B NE2 1 
ATOM   1127 N N   . ALA B 1 65 ? 12.60436 14.03719 30.08118  1.000 49.65522  ? 111 ALA B N   1 
ATOM   1128 C CA  . ALA B 1 65 ? 11.67230 13.72468 31.15867  1.000 52.90982  ? 111 ALA B CA  1 
ATOM   1129 C C   . ALA B 1 65 ? 10.23579 13.76123 30.66786  1.000 51.71551  ? 111 ALA B C   1 
ATOM   1130 O O   . ALA B 1 65 ? 9.35769  13.17721 31.30774  1.000 60.40900  ? 111 ALA B O   1 
ATOM   1131 C CB  . ALA B 1 65 ? 11.85006 14.68395 32.33623  1.000 52.92966  ? 111 ALA B CB  1 
ATOM   1132 N N   . ASN B 1 66 ? 9.98309  14.43757 29.54962  1.000 59.89775  ? 112 ASN B N   1 
ATOM   1133 C CA  . ASN B 1 66 ? 8.64229  14.65748 29.03321  1.000 60.29977  ? 112 ASN B CA  1 
ATOM   1134 C C   . ASN B 1 66 ? 8.36608  13.82640 27.78632  1.000 60.52700  ? 112 ASN B C   1 
ATOM   1135 O O   . ASN B 1 66 ? 7.45276  14.15741 27.02186  1.000 60.60633  ? 112 ASN B O   1 
ATOM   1136 C CB  . ASN B 1 66 ? 8.40738  16.14033 28.76361  1.000 58.74061  ? 112 ASN B CB  1 
ATOM   1137 C CG  . ASN B 1 66 ? 8.10142  16.91006 30.03013  1.000 59.62723  ? 112 ASN B CG  1 
ATOM   1138 O OD1 . ASN B 1 66 ? 8.94199  17.65484 30.52769  1.000 58.85393  ? 112 ASN B OD1 1 
ATOM   1139 N ND2 . ASN B 1 66 ? 6.90718  16.71566 30.57299  1.000 61.64428  ? 112 ASN B ND2 1 
ATOM   1140 N N   . GLY B 1 67 ? 9.19687  12.82331 27.50809  1.000 60.86773  ? 113 GLY B N   1 
ATOM   1141 C CA  . GLY B 1 67 ? 8.91522  11.86683 26.45932  1.000 61.89332  ? 113 GLY B CA  1 
ATOM   1142 C C   . GLY B 1 67 ? 9.80528  11.85784 25.23526  1.000 60.55775  ? 113 GLY B C   1 
ATOM   1143 O O   . GLY B 1 67 ? 9.48951  11.13438 24.28385  1.000 65.53434  ? 113 GLY B O   1 
ATOM   1144 N N   . ALA B 1 68 ? 10.89404 12.62498 25.20712  1.000 59.50061  ? 114 ALA B N   1 
ATOM   1145 C CA  . ALA B 1 68 ? 11.77103 12.59062 24.04222  1.000 61.48502  ? 114 ALA B CA  1 
ATOM   1146 C C   . ALA B 1 68 ? 12.32240 11.18186 23.83992  1.000 65.80024  ? 114 ALA B C   1 
ATOM   1147 O O   . ALA B 1 68 ? 12.83905 10.55823 24.77297  1.000 64.89545  ? 114 ALA B O   1 
ATOM   1148 C CB  . ALA B 1 68 ? 12.91005 13.59961 24.18874  1.000 55.98373  ? 114 ALA B CB  1 
ATOM   1149 N N   . ARG B 1 69 ? 12.18969 10.67768 22.61558  1.000 69.88711  ? 115 ARG B N   1 
ATOM   1150 C CA  . ARG B 1 69 ? 12.57198 9.30416  22.31624  1.000 72.57801  ? 115 ARG B CA  1 
ATOM   1151 C C   . ARG B 1 69 ? 14.06687 9.09021  22.52141  1.000 70.54040  ? 115 ARG B C   1 
ATOM   1152 O O   . ARG B 1 69 ? 14.87901 10.00668 22.36344  1.000 64.42915  ? 115 ARG B O   1 
ATOM   1153 C CB  . ARG B 1 69 ? 12.18993 8.95770  20.87668  1.000 73.94499  ? 115 ARG B CB  1 
ATOM   1154 C CG  . ARG B 1 69 ? 10.92548 9.64896  20.40865  1.000 72.67211  ? 115 ARG B CG  1 
ATOM   1155 C CD  . ARG B 1 69 ? 10.61205 9.32913  18.95639  1.000 76.08945  ? 115 ARG B CD  1 
ATOM   1156 N NE  . ARG B 1 69 ? 11.40765 10.12516 18.02829  1.000 74.90121  ? 115 ARG B NE  1 
ATOM   1157 C CZ  . ARG B 1 69 ? 11.37256 11.45152 17.94485  1.000 72.29693  ? 115 ARG B CZ  1 
ATOM   1158 N NH1 . ARG B 1 69 ? 10.56325 12.17483 18.70970  1.000 67.56356  ? 115 ARG B NH1 1 
ATOM   1159 N NH2 . ARG B 1 69 ? 12.16419 12.06963 17.06629  1.000 62.16483  ? 115 ARG B NH2 1 
ATOM   1160 N N   . SER B 1 70 ? 14.42582 7.85110  22.87048  1.000 71.64221  ? 116 SER B N   1 
ATOM   1161 C CA  . SER B 1 70 ? 15.82833 7.48671  23.01525  1.000 70.41984  ? 116 SER B CA  1 
ATOM   1162 C C   . SER B 1 70 ? 16.57623 7.47973  21.68900  1.000 71.18229  ? 116 SER B C   1 
ATOM   1163 O O   . SER B 1 70 ? 17.80206 7.32032  21.69117  1.000 71.09078  ? 116 SER B O   1 
ATOM   1164 C CB  . SER B 1 70 ? 15.95268 6.11723  23.68038  1.000 70.85640  ? 116 SER B CB  1 
ATOM   1165 O OG  . SER B 1 70 ? 15.10746 5.16870  23.05477  1.000 77.78294  ? 116 SER B OG  1 
ATOM   1166 N N   . ASP B 1 71 ? 15.89079 7.68294  20.56650  1.000 70.76479  ? 117 ASP B N   1 
ATOM   1167 C CA  . ASP B 1 71 ? 16.55278 7.68419  19.27483  1.000 71.86323  ? 117 ASP B CA  1 
ATOM   1168 C C   . ASP B 1 71 ? 16.79735 9.10069  18.79042  1.000 69.22881  ? 117 ASP B C   1 
ATOM   1169 O O   . ASP B 1 71 ? 17.08953 9.31274  17.60966  1.000 71.42665  ? 117 ASP B O   1 
ATOM   1170 C CB  . ASP B 1 71 ? 15.72751 6.89809  18.25338  1.000 76.89881  ? 117 ASP B CB  1 
ATOM   1171 C CG  . ASP B 1 71 ? 14.31421 7.44620  18.08377  1.000 79.29224  ? 117 ASP B CG  1 
ATOM   1172 O OD1 . ASP B 1 71 ? 14.09483 8.66510  18.26320  1.000 77.00083  ? 117 ASP B OD1 1 
ATOM   1173 O OD2 . ASP B 1 71 ? 13.40643 6.64400  17.77371  1.000 85.11129  ? 117 ASP B OD2 1 
ATOM   1174 N N   . ILE B 1 72 ? 16.70103 10.06755 19.69325  1.000 64.65537  ? 118 ILE B N   1 
ATOM   1175 C CA  . ILE B 1 72 ? 17.07424 11.44197 19.42654  1.000 56.56832  ? 118 ILE B CA  1 
ATOM   1176 C C   . ILE B 1 72 ? 18.47416 11.57263 19.99854  1.000 55.43696  ? 118 ILE B C   1 
ATOM   1177 O O   . ILE B 1 72 ? 18.71626 11.18262 21.14868  1.000 53.94107  ? 118 ILE B O   1 
ATOM   1178 C CB  . ILE B 1 72 ? 16.09202 12.42629 20.08450  1.000 56.19129  ? 118 ILE B CB  1 
ATOM   1179 C CG1 . ILE B 1 72 ? 14.76830 12.43814 19.32173  1.000 57.91517  ? 118 ILE B CG1 1 
ATOM   1180 C CG2 . ILE B 1 72 ? 16.65660 13.83996 20.06141  1.000 50.47824  ? 118 ILE B CG2 1 
ATOM   1181 C CD1 . ILE B 1 72 ? 13.73808 13.38578 19.89721  1.000 57.33975  ? 118 ILE B CD1 1 
ATOM   1182 N N   . ASP B 1 73 ? 19.39726 12.09613 19.20878  1.000 45.72172  ? 119 ASP B N   1 
ATOM   1183 C CA  . ASP B 1 73 ? 20.77204 12.26045 19.65062  1.000 45.24813  ? 119 ASP B CA  1 
ATOM   1184 C C   . ASP B 1 73 ? 20.96539 13.67491 20.17307  1.000 42.55438  ? 119 ASP B C   1 
ATOM   1185 O O   . ASP B 1 73 ? 20.83743 14.64141 19.41443  1.000 39.10309  ? 119 ASP B O   1 
ATOM   1186 C CB  . ASP B 1 73 ? 21.73073 11.99126 18.49513  1.000 50.15870  ? 119 ASP B CB  1 
ATOM   1187 C CG  . ASP B 1 73 ? 21.91821 10.51987 18.22292  1.000 54.19630  ? 119 ASP B CG  1 
ATOM   1188 O OD1 . ASP B 1 73 ? 21.19647 9.69753  18.83059  1.000 61.37694  ? 119 ASP B OD1 1 
ATOM   1189 O OD2 . ASP B 1 73 ? 22.76325 10.18823 17.36728  1.000 56.13379  ? 119 ASP B OD2 1 
ATOM   1190 N N   . PHE B 1 74 ? 21.30995 13.79271 21.44953  1.000 39.23419  ? 120 PHE B N   1 
ATOM   1191 C CA  . PHE B 1 74 ? 21.59353 15.08058 22.06472  1.000 40.63032  ? 120 PHE B CA  1 
ATOM   1192 C C   . PHE B 1 74 ? 23.09187 15.32950 22.10296  1.000 41.44088  ? 120 PHE B C   1 
ATOM   1193 O O   . PHE B 1 74 ? 23.85618 14.48810 22.58050  1.000 45.30936  ? 120 PHE B O   1 
ATOM   1194 C CB  . PHE B 1 74 ? 21.01135 15.16426 23.47592  1.000 39.33787  ? 120 PHE B CB  1 
ATOM   1195 C CG  . PHE B 1 74 ? 19.51768 15.27599 23.50905  1.000 39.47429  ? 120 PHE B CG  1 
ATOM   1196 C CD1 . PHE B 1 74 ? 18.91346 16.52077 23.42736  1.000 39.62586  ? 120 PHE B CD1 1 
ATOM   1197 C CD2 . PHE B 1 74 ? 18.71361 14.14970 23.56600  1.000 44.56424  ? 120 PHE B CD2 1 
ATOM   1198 C CE1 . PHE B 1 74 ? 17.52635 16.65095 23.43359  1.000 37.43169  ? 120 PHE B CE1 1 
ATOM   1199 C CE2 . PHE B 1 74 ? 17.32239 14.27085 23.57061  1.000 44.56474  ? 120 PHE B CE2 1 
ATOM   1200 C CZ  . PHE B 1 74 ? 16.73454 15.52631 23.50079  1.000 39.79624  ? 120 PHE B CZ  1 
ATOM   1201 N N   . TYR B 1 75 ? 23.50343 16.49566 21.62018  1.000 38.36042  ? 121 TYR B N   1 
ATOM   1202 C CA  . TYR B 1 75 ? 24.89581 16.90617 21.66116  1.000 41.47404  ? 121 TYR B CA  1 
ATOM   1203 C C   . TYR B 1 75 ? 24.96653 18.16131 22.51214  1.000 41.94478  ? 121 TYR B C   1 
ATOM   1204 O O   . TYR B 1 75 ? 24.33320 19.17317 22.18990  1.000 38.07916  ? 121 TYR B O   1 
ATOM   1205 C CB  . TYR B 1 75 ? 25.45735 17.15787 20.25676  1.000 42.49618  ? 121 TYR B CB  1 
ATOM   1206 C CG  . TYR B 1 75 ? 25.34391 15.96837 19.32271  1.000 46.00417  ? 121 TYR B CG  1 
ATOM   1207 C CD1 . TYR B 1 75 ? 24.12506 15.59769 18.76783  1.000 45.08218  ? 121 TYR B CD1 1 
ATOM   1208 C CD2 . TYR B 1 75 ? 26.45615 15.18296 19.03513  1.000 49.10617  ? 121 TYR B CD2 1 
ATOM   1209 C CE1 . TYR B 1 75 ? 24.02484 14.49926 17.93403  1.000 46.93282  ? 121 TYR B CE1 1 
ATOM   1210 C CE2 . TYR B 1 75 ? 26.36031 14.08309 18.19605  1.000 50.20679  ? 121 TYR B CE2 1 
ATOM   1211 C CZ  . TYR B 1 75 ? 25.14119 13.74823 17.64886  1.000 48.92004  ? 121 TYR B CZ  1 
ATOM   1212 O OH  . TYR B 1 75 ? 25.03761 12.65359 16.81631  1.000 53.12111  ? 121 TYR B OH  1 
ATOM   1213 N N   . LEU B 1 76 ? 25.75337 18.10454 23.57863  1.000 40.32193  ? 122 LEU B N   1 
ATOM   1214 C CA  . LEU B 1 76 ? 25.88847 19.22410 24.49039  1.000 41.88145  ? 122 LEU B CA  1 
ATOM   1215 C C   . LEU B 1 76 ? 27.21177 19.91042 24.19986  1.000 44.66245  ? 122 LEU B C   1 
ATOM   1216 O O   . LEU B 1 76 ? 28.26634 19.26832 24.19277  1.000 46.76945  ? 122 LEU B O   1 
ATOM   1217 C CB  . LEU B 1 76 ? 25.82338 18.76259 25.94639  1.000 44.95508  ? 122 LEU B CB  1 
ATOM   1218 C CG  . LEU B 1 76 ? 24.52625 18.06130 26.35905  1.000 47.23489  ? 122 LEU B CG  1 
ATOM   1219 C CD1 . LEU B 1 76 ? 24.51678 17.75150 27.84724  1.000 47.86190  ? 122 LEU B CD1 1 
ATOM   1220 C CD2 . LEU B 1 76 ? 23.32282 18.89491 25.99000  1.000 40.28894  ? 122 LEU B CD2 1 
ATOM   1221 N N   . GLN B 1 77 ? 27.14961 21.21383 23.95384  1.000 41.28474  ? 123 GLN B N   1 
ATOM   1222 C CA  . GLN B 1 77 ? 28.32886 22.02728 23.68422  1.000 44.96717  ? 123 GLN B CA  1 
ATOM   1223 C C   . GLN B 1 77 ? 28.36290 23.03565 24.81876  1.000 44.01852  ? 123 GLN B C   1 
ATOM   1224 O O   . GLN B 1 77 ? 27.77080 24.12325 24.71183  1.000 42.97940  ? 123 GLN B O   1 
ATOM   1225 C CB  . GLN B 1 77 ? 28.23126 22.71157 22.31922  1.000 44.45884  ? 123 GLN B CB  1 
ATOM   1226 C CG  . GLN B 1 77 ? 28.36886 21.74530 21.15027  1.000 47.23115  ? 123 GLN B CG  1 
ATOM   1227 C CD  . GLN B 1 77 ? 28.35971 22.42825 19.78641  1.000 56.03448  ? 123 GLN B CD  1 
ATOM   1228 O OE1 . GLN B 1 77 ? 28.34002 23.66013 19.68217  1.000 55.61874  ? 123 GLN B OE1 1 
ATOM   1229 N NE2 . GLN B 1 77 ? 28.34656 21.62010 18.72822  1.000 56.26318  ? 123 GLN B NE2 1 
ATOM   1230 N N   . PRO B 1 78 ? 29.03089 22.71355 25.92836  1.000 43.85270  ? 124 PRO B N   1 
ATOM   1231 C CA  . PRO B 1 78 ? 29.11053 23.67393 27.02567  1.000 43.95709  ? 124 PRO B CA  1 
ATOM   1232 C C   . PRO B 1 78 ? 29.96909 24.85249 26.61281  1.000 46.26557  ? 124 PRO B C   1 
ATOM   1233 O O   . PRO B 1 78 ? 30.91865 24.71512 25.83664  1.000 48.28056  ? 124 PRO B O   1 
ATOM   1234 C CB  . PRO B 1 78 ? 29.73729 22.86704 28.17114  1.000 44.27690  ? 124 PRO B CB  1 
ATOM   1235 C CG  . PRO B 1 78 ? 30.44461 21.74136 27.51362  1.000 45.49341  ? 124 PRO B CG  1 
ATOM   1236 C CD  . PRO B 1 78 ? 29.61714 21.41323 26.29214  1.000 44.44674  ? 124 PRO B CD  1 
ATOM   1237 N N   . THR B 1 79 ? 29.57315 26.02980 27.07107  1.000 46.32815  ? 125 THR B N   1 
ATOM   1238 C CA  . THR B 1 79 ? 30.34508 27.23549 26.85722  1.000 48.94445  ? 125 THR B CA  1 
ATOM   1239 C C   . THR B 1 79 ? 30.49584 27.94084 28.19186  1.000 51.54563  ? 125 THR B C   1 
ATOM   1240 O O   . THR B 1 79 ? 29.76820 27.66153 29.14885  1.000 52.98977  ? 125 THR B O   1 
ATOM   1241 C CB  . THR B 1 79 ? 29.66123 28.17553 25.84960  1.000 53.14801  ? 125 THR B CB  1 
ATOM   1242 O OG1 . THR B 1 79 ? 28.44608 28.68268 26.41924  1.000 52.15000  ? 125 THR B OG1 1 
ATOM   1243 C CG2 . THR B 1 79 ? 29.33542 27.44342 24.55841  1.000 48.98455  ? 125 THR B CG2 1 
ATOM   1244 N N   . LEU B 1 80 ? 31.43927 28.87343 28.24266  1.000 54.15537  ? 126 LEU B N   1 
ATOM   1245 C CA  . LEU B 1 80 ? 31.70443 29.64810 29.44606  1.000 58.08999  ? 126 LEU B CA  1 
ATOM   1246 C C   . LEU B 1 80 ? 31.30522 31.10339 29.23847  1.000 60.62686  ? 126 LEU B C   1 
ATOM   1247 O O   . LEU B 1 80 ? 31.61737 31.69378 28.19828  1.000 60.75552  ? 126 LEU B O   1 
ATOM   1248 C CB  . LEU B 1 80 ? 33.17445 29.51911 29.84979  1.000 57.65250  ? 126 LEU B CB  1 
ATOM   1249 C CG  . LEU B 1 80 ? 33.53561 28.08967 30.28840  1.000 55.19495  ? 126 LEU B CG  1 
ATOM   1250 C CD1 . LEU B 1 80 ? 34.93730 28.01957 30.83660  1.000 57.02744  ? 126 LEU B CD1 1 
ATOM   1251 C CD2 . LEU B 1 80 ? 32.54034 27.54976 31.31421  1.000 53.07848  ? 126 LEU B CD2 1 
ATOM   1252 N N   . ASN B 1 81 ? 30.61793 31.67402 30.23138  1.000 61.37149  ? 127 ASN B N   1 
ATOM   1253 C CA  . ASN B 1 81 ? 30.25752 33.09263 30.23956  1.000 62.33061  ? 127 ASN B CA  1 
ATOM   1254 C C   . ASN B 1 81 ? 29.43962 33.49292 29.01067  1.000 64.97167  ? 127 ASN B C   1 
ATOM   1255 O O   . ASN B 1 81 ? 29.52761 34.62755 28.53428  1.000 64.70757  ? 127 ASN B O   1 
ATOM   1256 C CB  . ASN B 1 81 ? 31.50590 33.97162 30.37599  1.000 63.41864  ? 127 ASN B CB  1 
ATOM   1257 C CG  . ASN B 1 81 ? 32.55337 33.35395 31.29280  1.000 65.54629  ? 127 ASN B CG  1 
ATOM   1258 O OD1 . ASN B 1 81 ? 33.70812 33.16421 30.90750  1.000 65.20689  ? 127 ASN B OD1 1 
ATOM   1259 N ND2 . ASN B 1 81 ? 32.14891 33.04133 32.51783  1.000 65.05294  ? 127 ASN B ND2 1 
ATOM   1260 N N   . GLN B 1 82 ? 28.63248 32.57266 28.49177  1.000 63.41097  ? 128 GLN B N   1 
ATOM   1261 C CA  . GLN B 1 82 ? 27.69683 32.87259 27.41688  1.000 64.54989  ? 128 GLN B CA  1 
ATOM   1262 C C   . GLN B 1 82 ? 26.28926 32.98707 27.98071  1.000 61.21049  ? 128 GLN B C   1 
ATOM   1263 O O   . GLN B 1 82 ? 25.86419 32.15918 28.79449  1.000 57.95099  ? 128 GLN B O   1 
ATOM   1264 C CB  . GLN B 1 82 ? 27.72979 31.79711 26.32939  1.000 64.42082  ? 128 GLN B CB  1 
ATOM   1265 C CG  . GLN B 1 82 ? 28.42207 32.22939 25.04496  1.000 65.96864  ? 128 GLN B CG  1 
ATOM   1266 C CD  . GLN B 1 82 ? 29.71047 32.99258 25.30809  1.000 69.93428  ? 128 GLN B CD  1 
ATOM   1267 O OE1 . GLN B 1 82 ? 30.76089 32.39569 25.56804  1.000 65.60466  ? 128 GLN B OE1 1 
ATOM   1268 N NE2 . GLN B 1 82 ? 29.64293 34.31972 25.21377  1.000 74.28048  ? 128 GLN B NE2 1 
ATOM   1269 N N   . LYS B 1 83 ? 25.57335 34.01566 27.54070  1.000 61.67937  ? 129 LYS B N   1 
ATOM   1270 C CA  . LYS B 1 83 ? 24.21525 34.27331 27.99324  1.000 59.77838  ? 129 LYS B CA  1 
ATOM   1271 C C   . LYS B 1 83 ? 23.22810 33.47548 27.15448  1.000 58.12625  ? 129 LYS B C   1 
ATOM   1272 O O   . LYS B 1 83 ? 23.29233 33.49383 25.92132  1.000 55.88196  ? 129 LYS B O   1 
ATOM   1273 C CB  . LYS B 1 83 ? 23.88990 35.76441 27.90212  1.000 64.77720  ? 129 LYS B CB  1 
ATOM   1274 C CG  . LYS B 1 83 ? 22.63286 36.16340 28.65524  1.000 66.01599  ? 129 LYS B CG  1 
ATOM   1275 C CD  . LYS B 1 83 ? 22.33005 37.65161 28.50379  1.000 70.75403  ? 129 LYS B CD  1 
ATOM   1276 C CE  . LYS B 1 83 ? 22.44039 38.10941 27.05245  1.000 72.88589  ? 129 LYS B CE  1 
ATOM   1277 N NZ  . LYS B 1 83 ? 21.20216 37.85062 26.26629  1.000 69.24758  ? 129 LYS B NZ  1 
ATOM   1278 N N   . GLY B 1 84 ? 22.31854 32.78354 27.82671  1.000 56.01195  ? 130 GLY B N   1 
ATOM   1279 C CA  . GLY B 1 84 ? 21.26619 32.06288 27.15172  1.000 50.45498  ? 130 GLY B CA  1 
ATOM   1280 C C   . GLY B 1 84 ? 21.71077 30.70702 26.63834  1.000 44.06685  ? 130 GLY B C   1 
ATOM   1281 O O   . GLY B 1 84 ? 22.82652 30.23520 26.87889  1.000 43.89967  ? 130 GLY B O   1 
ATOM   1282 N N   . VAL B 1 85 ? 20.80693 30.08309 25.88123  1.000 36.56494  ? 131 VAL B N   1 
ATOM   1283 C CA  . VAL B 1 85 ? 21.04673 28.77466 25.28679  1.000 31.70669  ? 131 VAL B CA  1 
ATOM   1284 C C   . VAL B 1 85 ? 20.66250 28.85763 23.81324  1.000 30.74012  ? 131 VAL B C   1 
ATOM   1285 O O   . VAL B 1 85 ? 19.69583 29.53856 23.45776  1.000 31.37486  ? 131 VAL B O   1 
ATOM   1286 C CB  . VAL B 1 85 ? 20.22295 27.68368 26.01586  1.000 31.74886  ? 131 VAL B CB  1 
ATOM   1287 C CG1 . VAL B 1 85 ? 20.31723 26.33915 25.31308  1.000 30.75857  ? 131 VAL B CG1 1 
ATOM   1288 C CG2 . VAL B 1 85 ? 20.67836 27.54553 27.47620  1.000 39.54262  ? 131 VAL B CG2 1 
ATOM   1289 N N   . VAL B 1 86 ? 21.41881 28.17234 22.96152  1.000 28.83455  ? 132 VAL B N   1 
ATOM   1290 C CA  . VAL B 1 86 ? 21.08076 28.00558 21.55203  1.000 26.35527  ? 132 VAL B CA  1 
ATOM   1291 C C   . VAL B 1 86 ? 20.73511 26.54381 21.33028  1.000 26.15845  ? 132 VAL B C   1 
ATOM   1292 O O   . VAL B 1 86 ? 21.48543 25.64580 21.74527  1.000 27.22090  ? 132 VAL B O   1 
ATOM   1293 C CB  . VAL B 1 86 ? 22.22673 28.44379 20.62146  1.000 27.49390  ? 132 VAL B CB  1 
ATOM   1294 C CG1 . VAL B 1 86 ? 21.82851 28.21989 19.15278  1.000 23.16747  ? 132 VAL B CG1 1 
ATOM   1295 C CG2 . VAL B 1 86 ? 22.58812 29.89312 20.87389  1.000 26.59970  ? 132 VAL B CG2 1 
ATOM   1296 N N   . MET B 1 87 ? 19.61363 26.29682 20.67141  1.000 22.42741  ? 133 MET B N   1 
ATOM   1297 C CA  . MET B 1 87 ? 19.20891 24.94161 20.34301  1.000 25.15427  ? 133 MET B CA  1 
ATOM   1298 C C   . MET B 1 87 ? 19.21600 24.78259 18.83255  1.000 23.16274  ? 133 MET B C   1 
ATOM   1299 O O   . MET B 1 87 ? 18.69060 25.63938 18.12037  1.000 21.20543  ? 133 MET B O   1 
ATOM   1300 C CB  . MET B 1 87 ? 17.83161 24.64109 20.91127  1.000 23.51424  ? 133 MET B CB  1 
ATOM   1301 C CG  . MET B 1 87 ? 17.39437 23.23018 20.71762  1.000 25.70841  ? 133 MET B CG  1 
ATOM   1302 S SD  . MET B 1 87 ? 15.66496 23.02016 21.20970  1.000 36.74315  ? 133 MET B SD  1 
ATOM   1303 C CE  . MET B 1 87 ? 15.55889 21.25595 21.18360  1.000 32.07058  ? 133 MET B CE  1 
ATOM   1304 N N   . ILE B 1 88 ? 19.84274 23.71258 18.34375  1.000 23.50112  ? 134 ILE B N   1 
ATOM   1305 C CA  . ILE B 1 88 ? 19.84640 23.39439 16.91618  1.000 23.95261  ? 134 ILE B CA  1 
ATOM   1306 C C   . ILE B 1 88 ? 19.20481 22.02441 16.74554  1.000 24.25536  ? 134 ILE B C   1 
ATOM   1307 O O   . ILE B 1 88 ? 19.67685 21.03674 17.31891  1.000 23.99591  ? 134 ILE B O   1 
ATOM   1308 C CB  . ILE B 1 88 ? 21.26155 23.41556 16.31858  1.000 24.76160  ? 134 ILE B CB  1 
ATOM   1309 C CG1 . ILE B 1 88 ? 21.93000 24.75590 16.59273  1.000 27.27714  ? 134 ILE B CG1 1 
ATOM   1310 C CG2 . ILE B 1 88 ? 21.20542 23.19294 14.80972  1.000 22.77198  ? 134 ILE B CG2 1 
ATOM   1311 C CD1 . ILE B 1 88 ? 23.43511 24.73722 16.32019  1.000 30.43330  ? 134 ILE B CD1 1 
ATOM   1312 N N   . ALA B 1 89 ? 18.12992 21.96353 15.97365  1.000 21.48144  ? 135 ALA B N   1 
ATOM   1313 C CA  . ALA B 1 89 ? 17.39476 20.73006 15.76541  1.000 23.94343  ? 135 ALA B CA  1 
ATOM   1314 C C   . ALA B 1 89 ? 17.41762 20.36071 14.29075  1.000 24.29021  ? 135 ALA B C   1 
ATOM   1315 O O   . ALA B 1 89 ? 17.27655 21.22773 13.42504  1.000 23.28907  ? 135 ALA B O   1 
ATOM   1316 C CB  . ALA B 1 89 ? 15.94714 20.87078 16.25524  1.000 24.69091  ? 135 ALA B CB  1 
ATOM   1317 N N   . SER B 1 90 ? 17.57165 19.07221 14.00067  1.000 26.31672  ? 136 SER B N   1 
ATOM   1318 C CA  . SER B 1 90 ? 17.66491 18.64796 12.61155  1.000 28.33475  ? 136 SER B CA  1 
ATOM   1319 C C   . SER B 1 90 ? 17.02544 17.27654 12.44623  1.000 32.98591  ? 136 SER B C   1 
ATOM   1320 O O   . SER B 1 90 ? 17.02848 16.46081 13.37468  1.000 29.80755  ? 136 SER B O   1 
ATOM   1321 C CB  . SER B 1 90 ? 19.12237 18.60508 12.13357  1.000 34.05892  ? 136 SER B CB  1 
ATOM   1322 O OG  . SER B 1 90 ? 19.17824 17.97003 10.86344  1.000 37.40416  ? 136 SER B OG  1 
ATOM   1323 N N   . ASN B 1 91 ? 16.47556 17.02062 11.25133  1.000 30.50861  ? 137 ASN B N   1 
ATOM   1324 C CA  . ASN B 1 91 ? 15.90064 15.71319 10.95048  1.000 34.56588  ? 137 ASN B CA  1 
ATOM   1325 C C   . ASN B 1 91 ? 16.85004 14.85104 10.13686  1.000 39.73804  ? 137 ASN B C   1 
ATOM   1326 O O   . ASN B 1 91 ? 16.42379 13.85852 9.53601   1.000 40.72179  ? 137 ASN B O   1 
ATOM   1327 C CB  . ASN B 1 91 ? 14.54614 15.84280 10.24331  1.000 31.52576  ? 137 ASN B CB  1 
ATOM   1328 C CG  . ASN B 1 91 ? 14.63189 16.51644 8.86778   1.000 30.33696  ? 137 ASN B CG  1 
ATOM   1329 O OD1 . ASN B 1 91 ? 15.66753 17.08359 8.47316   1.000 31.18813  ? 137 ASN B OD1 1 
ATOM   1330 N ND2 . ASN B 1 91 ? 13.52972 16.44646 8.12847   1.000 30.54082  ? 137 ASN B ND2 1 
ATOM   1331 N N   . TYR B 1 92 ? 18.12592 15.21692 10.11016  1.000 45.29108  ? 138 TYR B N   1 
ATOM   1332 C CA  . TYR B 1 92 ? 19.18040 14.39611 9.53120   1.000 48.06530  ? 138 TYR B CA  1 
ATOM   1333 C C   . TYR B 1 92 ? 20.50266 14.60735 10.26144  1.000 47.48372  ? 138 TYR B C   1 
ATOM   1334 O O   . TYR B 1 92 ? 20.66751 15.59221 10.98811  1.000 46.73947  ? 138 TYR B O   1 
ATOM   1335 C CB  . TYR B 1 92 ? 19.31435 14.69453 8.03399   1.000 49.53620  ? 138 TYR B CB  1 
ATOM   1336 C CG  . TYR B 1 92 ? 19.72690 16.11384 7.69428   1.000 46.93225  ? 138 TYR B CG  1 
ATOM   1337 C CD1 . TYR B 1 92 ? 18.76762 17.10907 7.52472   1.000 42.88107  ? 138 TYR B CD1 1 
ATOM   1338 C CD2 . TYR B 1 92 ? 21.05970 16.45672 7.52357   1.000 52.77478  ? 138 TYR B CD2 1 
ATOM   1339 C CE1 . TYR B 1 92 ? 19.12710 18.41592 7.20088   1.000 41.57000  ? 138 TYR B CE1 1 
ATOM   1340 C CE2 . TYR B 1 92 ? 21.43397 17.76726 7.20351   1.000 52.49179  ? 138 TYR B CE2 1 
ATOM   1341 C CZ  . TYR B 1 92 ? 20.45718 18.73823 7.04149   1.000 46.62435  ? 138 TYR B CZ  1 
ATOM   1342 O OH  . TYR B 1 92 ? 20.81826 20.02705 6.70957   1.000 49.90487  ? 138 TYR B OH  1 
HETATM 1343 O O   . HOH C 2 .  ? 9.68554  39.35651 -7.67546  1.000 31.03609  ? 201 HOH A O   1 
HETATM 1344 O O   . HOH C 2 .  ? 14.126   44.190   0.815     1.000 23.23983  ? 202 HOH A O   1 
HETATM 1345 O O   . HOH C 2 .  ? 21.52449 29.78901 -13.88388 1.000 37.03862  ? 203 HOH A O   1 
HETATM 1346 O O   . HOH C 2 .  ? 3.38202  22.82816 7.00936   1.000 40.18534  ? 204 HOH A O   1 
HETATM 1347 O O   . HOH C 2 .  ? 14.28219 18.05162 -11.68204 1.000 40.69725  ? 205 HOH A O   1 
HETATM 1348 O O   . HOH C 2 .  ? 1.02417  21.75627 -6.49650  1.000 36.76871  ? 206 HOH A O   1 
HETATM 1349 O O   . HOH C 2 .  ? 4.02015  42.61203 5.37975   1.000 35.94212  ? 207 HOH A O   1 
HETATM 1350 O O   . HOH C 2 .  ? 0.861    33.521   1.424     1.000 27.84858  ? 208 HOH A O   1 
HETATM 1351 O O   . HOH C 2 .  ? 3.51467  21.34166 5.10072   1.000 33.37156  ? 209 HOH A O   1 
HETATM 1352 O O   . HOH C 2 .  ? 20.76234 25.00267 -8.06778  1.000 21.26816  ? 210 HOH A O   1 
HETATM 1353 O O   . HOH C 2 .  ? 19.05334 31.63908 15.66497  1.000 30.68077  ? 211 HOH A O   1 
HETATM 1354 O O   . HOH C 2 .  ? 24.51133 30.23542 -10.67754 1.000 18.92176  ? 212 HOH A O   1 
HETATM 1355 O O   . HOH C 2 .  ? 5.83133  21.75859 -11.80229 1.000 35.20341  ? 213 HOH A O   1 
HETATM 1356 O O   . HOH C 2 .  ? 5.36247  29.01761 -10.95378 1.000 40.95494  ? 214 HOH A O   1 
HETATM 1357 O O   . HOH C 2 .  ? 19.25841 19.17625 -11.00836 1.000 38.05783  ? 215 HOH A O   1 
HETATM 1358 O O   . HOH C 2 .  ? 7.86047  16.80134 -6.58455  1.000 36.96230  ? 216 HOH A O   1 
HETATM 1359 O O   . HOH C 2 .  ? 8.72113  32.13660 -10.00731 1.000 24.40429  ? 217 HOH A O   1 
HETATM 1360 O O   . HOH C 2 .  ? 18.94707 21.12841 -13.22627 1.000 43.92085  ? 218 HOH A O   1 
HETATM 1361 O O   . HOH C 2 .  ? 28.903   35.246   -4.683    1.000 33.48480  ? 219 HOH A O   1 
HETATM 1362 O O   . HOH C 2 .  ? 9.75778  18.01286 -2.88259  1.000 25.02676  ? 220 HOH A O   1 
HETATM 1363 O O   . HOH C 2 .  ? 3.06809  16.92463 -0.64806  1.000 37.28860  ? 221 HOH A O   1 
HETATM 1364 O O   . HOH C 2 .  ? 26.425   24.364   -12.841   1.000 31.66513  ? 222 HOH A O   1 
HETATM 1365 O O   . HOH C 2 .  ? 13.30101 39.37485 -8.82046  1.000 35.52738  ? 223 HOH A O   1 
HETATM 1366 O O   . HOH C 2 .  ? 1.710    39.919   -5.343    1.000 38.84923  ? 224 HOH A O   1 
HETATM 1367 O O   . HOH C 2 .  ? 24.57447 29.03565 -12.88210 1.000 34.45701  ? 225 HOH A O   1 
HETATM 1368 O O   . HOH C 2 .  ? 7.75160  46.14879 0.38433   1.000 30.04065  ? 226 HOH A O   1 
HETATM 1369 O O   . HOH C 2 .  ? 25.25931 20.16965 -9.30940  1.000 39.31571  ? 227 HOH A O   1 
HETATM 1370 O O   . HOH C 2 .  ? 6.90766  38.71624 7.31270   1.000 26.90439  ? 228 HOH A O   1 
HETATM 1371 O O   . HOH C 2 .  ? 17.52370 39.76626 -3.64678  1.000 23.94973  ? 229 HOH A O   1 
HETATM 1372 O O   . HOH C 2 .  ? 8.00916  31.77089 20.60844  1.000 48.84683  ? 230 HOH A O   1 
HETATM 1373 O O   . HOH C 2 .  ? 17.54162 42.14913 6.34075   1.000 36.53414  ? 231 HOH A O   1 
HETATM 1374 O O   . HOH C 2 .  ? 16.25706 39.61373 -8.28453  1.000 36.98465  ? 232 HOH A O   1 
HETATM 1375 O O   . HOH C 2 .  ? 14.80755 18.36505 -8.01314  1.000 33.30362  ? 233 HOH A O   1 
HETATM 1376 O O   . HOH C 2 .  ? 1.94781  16.73210 -3.54255  1.000 36.67006  ? 234 HOH A O   1 
HETATM 1377 O O   . HOH C 2 .  ? 20.97127 37.28963 9.41826   1.000 41.78393  ? 235 HOH A O   1 
HETATM 1378 O O   . HOH C 2 .  ? 2.96279  38.92799 -1.63776  1.000 26.17108  ? 236 HOH A O   1 
HETATM 1379 O O   . HOH C 2 .  ? 9.41974  32.36971 16.61200  1.000 35.82161  ? 237 HOH A O   1 
HETATM 1380 O O   . HOH C 2 .  ? 13.81914 18.63032 -0.65068  1.000 28.83216  ? 238 HOH A O   1 
HETATM 1381 O O   . HOH C 2 .  ? 12.38426 44.20871 6.59795   1.000 35.86683  ? 239 HOH A O   1 
HETATM 1382 O O   . HOH C 2 .  ? 19.41014 35.67748 10.25703  1.000 33.80278  ? 240 HOH A O   1 
HETATM 1383 O O   . HOH C 2 .  ? 26.32311 16.38241 -6.84383  1.000 56.80941  ? 241 HOH A O   1 
HETATM 1384 O O   . HOH C 2 .  ? 22.26120 24.94007 -3.44726  1.000 22.27506  ? 242 HOH A O   1 
HETATM 1385 O O   . HOH C 2 .  ? 14.79715 32.59730 -13.37338 1.000 30.46316  ? 243 HOH A O   1 
HETATM 1386 O O   . HOH C 2 .  ? 10.794   41.856   -0.836    1.000 34.43974  ? 244 HOH A O   1 
HETATM 1387 O O   . HOH C 2 .  ? 1.09829  31.23242 8.29496   1.000 31.62842  ? 245 HOH A O   1 
HETATM 1388 O O   . HOH C 2 .  ? 10.37321 33.74172 -11.99878 1.000 32.30505  ? 246 HOH A O   1 
HETATM 1389 O O   . HOH C 2 .  ? 23.48684 38.34462 -5.41192  1.000 36.93200  ? 247 HOH A O   1 
HETATM 1390 O O   . HOH C 2 .  ? 20.55725 39.49578 -3.37943  1.000 25.83505  ? 248 HOH A O   1 
HETATM 1391 O O   . HOH C 2 .  ? 5.43532  38.23210 -0.05513  1.000 27.75672  ? 249 HOH A O   1 
HETATM 1392 O O   . HOH C 2 .  ? -0.94853 40.54683 3.13088   1.000 39.01454  ? 250 HOH A O   1 
HETATM 1393 O O   . HOH C 2 .  ? 18.04089 34.54640 5.77322   1.000 21.09606  ? 251 HOH A O   1 
HETATM 1394 O O   . HOH C 2 .  ? 1.14627  17.69027 -7.61419  1.000 41.45080  ? 252 HOH A O   1 
HETATM 1395 O O   . HOH C 2 .  ? 7.35858  38.41435 -8.09698  1.000 32.71552  ? 253 HOH A O   1 
HETATM 1396 O O   . HOH C 2 .  ? 2.22901  35.48535 9.96887   1.000 41.06658  ? 254 HOH A O   1 
HETATM 1397 O O   . HOH C 2 .  ? 27.790   22.299   -2.307    1.000 41.28214  ? 255 HOH A O   1 
HETATM 1398 O O   . HOH C 2 .  ? -0.38888 16.25417 -2.15708  1.000 35.72137  ? 256 HOH A O   1 
HETATM 1399 O O   . HOH C 2 .  ? 8.23430  35.06914 13.79046  1.000 41.35272  ? 257 HOH A O   1 
HETATM 1400 O O   . HOH C 2 .  ? 12.28255 38.59715 -12.44402 1.000 33.91143  ? 258 HOH A O   1 
HETATM 1401 O O   . HOH C 2 .  ? 8.886    41.881   0.877     1.000 32.10912  ? 259 HOH A O   1 
HETATM 1402 O O   . HOH C 2 .  ? 5.69374  35.60389 22.10145  1.000 64.22353  ? 260 HOH A O   1 
HETATM 1403 O O   . HOH C 2 .  ? 22.843   33.823   15.013    1.000 42.56040  ? 261 HOH A O   1 
HETATM 1404 O O   . HOH C 2 .  ? 23.52639 37.89335 -0.99270  1.000 32.58036  ? 262 HOH A O   1 
HETATM 1405 O O   . HOH C 2 .  ? 9.34421  37.44647 14.93105  1.000 46.70406  ? 263 HOH A O   1 
HETATM 1406 O O   . HOH C 2 .  ? 17.53504 17.87420 -5.48806  1.000 41.24504  ? 264 HOH A O   1 
HETATM 1407 O O   . HOH C 2 .  ? 20.81593 22.36450 3.63009   1.000 27.94041  ? 265 HOH A O   1 
HETATM 1408 O O   . HOH C 2 .  ? -1.45227 17.54854 -6.50472  1.000 44.22391  ? 266 HOH A O   1 
HETATM 1409 O O   . HOH C 2 .  ? 26.65507 25.23190 -1.53369  1.000 37.88903  ? 267 HOH A O   1 
HETATM 1410 O O   . HOH C 2 .  ? 28.859   33.715   -7.197    1.000 32.46213  ? 268 HOH A O   1 
HETATM 1411 O O   . HOH C 2 .  ? 17.39461 41.21598 9.10361   1.000 45.47075  ? 269 HOH A O   1 
HETATM 1412 O O   . HOH C 2 .  ? -1.511   24.505   9.804     1.000 44.89746  ? 270 HOH A O   1 
HETATM 1413 O O   . HOH C 2 .  ? 1.921    42.113   1.755     1.000 41.39805  ? 271 HOH A O   1 
HETATM 1414 O O   . HOH C 2 .  ? 6.70762  36.64925 -9.96473  1.000 44.31950  ? 272 HOH A O   1 
HETATM 1415 O O   . HOH C 2 .  ? 6.33801  33.85160 -9.53369  1.000 27.40562  ? 273 HOH A O   1 
HETATM 1416 O O   . HOH C 2 .  ? 0.51172  28.94001 4.91696   1.000 38.35205  ? 274 HOH A O   1 
HETATM 1417 O O   . HOH C 2 .  ? 19.610   45.367   5.802     1.000 39.86204  ? 275 HOH A O   1 
HETATM 1418 O O   . HOH C 2 .  ? 24.32498 26.23642 -15.91255 1.000 35.43212  ? 276 HOH A O   1 
HETATM 1419 O O   . HOH C 2 .  ? 13.39854 19.87358 -13.01141 1.000 44.93174  ? 277 HOH A O   1 
HETATM 1420 O O   . HOH C 2 .  ? 9.86059  16.87835 -5.18453  1.000 34.89536  ? 278 HOH A O   1 
HETATM 1421 O O   . HOH C 2 .  ? 5.560    46.081   7.513     1.000 39.19529  ? 279 HOH A O   1 
HETATM 1422 O O   . HOH C 2 .  ? 12.50553 33.35976 -13.15480 1.000 39.13858  ? 280 HOH A O   1 
HETATM 1423 O O   . HOH C 2 .  ? 23.17735 35.80715 9.18902   1.000 40.30244  ? 281 HOH A O   1 
HETATM 1424 O O   . HOH C 2 .  ? 22.47566 37.78668 -7.29078  1.000 30.26253  ? 282 HOH A O   1 
HETATM 1425 O O   . HOH C 2 .  ? 19.42287 34.38984 7.90041   1.000 26.75877  ? 283 HOH A O   1 
HETATM 1426 O O   . HOH C 2 .  ? 24.20866 30.96482 -14.59915 1.000 40.70487  ? 284 HOH A O   1 
HETATM 1427 O O   . HOH C 2 .  ? -0.98412 41.22676 0.68261   1.000 41.21745  ? 285 HOH A O   1 
HETATM 1428 O O   . HOH C 2 .  ? 3.01194  22.72668 -11.46050 1.000 42.94226  ? 286 HOH A O   1 
HETATM 1429 O O   . HOH C 2 .  ? 21.87552 35.63329 -8.62167  1.000 26.32869  ? 287 HOH A O   1 
HETATM 1430 O O   . HOH C 2 .  ? 26.35852 32.41334 -11.09213 1.000 34.21135  ? 288 HOH A O   1 
HETATM 1431 O O   . HOH C 2 .  ? 18.21649 15.76263 0.51103   1.000 44.89962  ? 289 HOH A O   1 
HETATM 1432 O O   . HOH C 2 .  ? 18.42005 38.15689 -9.56794  1.000 30.14964  ? 290 HOH A O   1 
HETATM 1433 O O   . HOH C 2 .  ? 20.43178 16.25763 0.74757   1.000 48.12515  ? 291 HOH A O   1 
HETATM 1434 O O   . HOH C 2 .  ? 23.72258 36.00878 -10.51559 1.000 36.76186  ? 292 HOH A O   1 
HETATM 1435 O O   . HOH D 2 .  ? 27.04043 28.45552 35.34102  1.000 55.47469  ? 201 HOH B O   1 
HETATM 1436 O O   . HOH D 2 .  ? 19.11354 21.38589 5.64154   1.000 32.50906  ? 202 HOH B O   1 
HETATM 1437 O O   . HOH D 2 .  ? 24.85124 29.93997 28.67213  1.000 47.64691  ? 203 HOH B O   1 
HETATM 1438 O O   . HOH D 2 .  ? 26.12636 19.08707 16.94731  1.000 44.47309  ? 204 HOH B O   1 
HETATM 1439 O O   . HOH D 2 .  ? 16.81666 10.85965 23.90118  1.000 61.13897  ? 205 HOH B O   1 
HETATM 1440 O O   . HOH D 2 .  ? 27.89740 19.03920 18.79348  1.000 47.97872  ? 206 HOH B O   1 
HETATM 1441 O O   . HOH D 2 .  ? 8.01048  18.73514 3.47965   1.000 32.85663  ? 207 HOH B O   1 
HETATM 1442 O O   . HOH D 2 .  ? 13.70155 10.41237 15.64429  1.000 64.23889  ? 208 HOH B O   1 
HETATM 1443 O O   . HOH D 2 .  ? 24.76756 29.73781 23.95305  1.000 38.34404  ? 209 HOH B O   1 
HETATM 1444 O O   . HOH D 2 .  ? 15.17888 13.70874 32.38429  1.000 50.78045  ? 210 HOH B O   1 
HETATM 1445 O O   . HOH D 2 .  ? 18.28572 18.73279 35.14282  1.000 49.08528  ? 211 HOH B O   1 
HETATM 1446 O O   . HOH D 2 .  ? 15.57077 19.71156 33.68694  1.000 50.08804  ? 212 HOH B O   1 
HETATM 1447 O O   . HOH D 2 .  ? 5.89933  20.53544 29.91691  1.000 47.59567  ? 213 HOH B O   1 
HETATM 1448 O O   . HOH D 2 .  ? 14.57755 33.55018 23.46691  1.000 35.65853  ? 214 HOH B O   1 
HETATM 1449 O O   . HOH D 2 .  ? 21.47270 19.44310 15.80708  1.000 34.22065  ? 215 HOH B O   1 
HETATM 1450 O O   . HOH D 2 .  ? 7.51285  16.89406 1.65192   1.000 41.66124  ? 216 HOH B O   1 
HETATM 1451 O O   . HOH D 2 .  ? 20.21813 32.39359 23.19353  1.000 37.42553  ? 217 HOH B O   1 
HETATM 1452 O O   . HOH D 2 .  ? 10.19775 18.35127 7.11908   1.000 43.30184  ? 218 HOH B O   1 
HETATM 1453 O O   . HOH D 2 .  ? 24.878   26.861   14.012    1.000 27.66543  ? 219 HOH B O   1 
HETATM 1454 O O   . HOH D 2 .  ? 19.40200 9.83436  23.67290  1.000 58.03147  ? 220 HOH B O   1 
HETATM 1455 O O   . HOH D 2 .  ? 23.31685 12.53179 14.38062  1.000 49.07015  ? 221 HOH B O   1 
HETATM 1456 O O   . HOH D 2 .  ? 23.952   31.804   13.500    1.000 32.98270  ? 222 HOH B O   1 
HETATM 1457 O O   . HOH D 2 .  ? 22.26525 18.19644 10.96463  1.000 44.87582  ? 223 HOH B O   1 
HETATM 1458 O O   . HOH D 2 .  ? 24.29114 16.47713 10.94451  1.000 50.07687  ? 224 HOH B O   1 
HETATM 1459 O O   . HOH D 2 .  ? 12.44668 16.51599 0.45034   1.000 40.64585  ? 225 HOH B O   1 
HETATM 1460 O O   . HOH D 2 .  ? 27.270   23.858   16.552    1.000 37.69939  ? 226 HOH B O   1 
HETATM 1461 O O   . HOH D 2 .  ? 9.18956  17.00628 9.27076   1.000 49.74943  ? 227 HOH B O   1 
HETATM 1462 O O   . HOH D 2 .  ? 14.19887 17.52867 33.85218  1.000 49.91910  ? 228 HOH B O   1 
HETATM 1463 O O   . HOH D 2 .  ? 8.11129  18.15926 5.81911   1.000 45.03767  ? 229 HOH B O   1 
HETATM 1464 O O   . HOH D 2 .  ? 15.35456 14.80829 34.75502  1.000 54.30167  ? 230 HOH B O   1 
HETATM 1465 O O   . HOH D 2 .  ? 24.85197 21.89453 14.37420  1.000 39.84364  ? 231 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   . LYS A 11 ? 1.05580 0.82844 0.76838 0.12226  0.09961  -0.20922 57  LYS A N   
2    C CA  . LYS A 11 ? 1.04963 0.89244 0.76943 0.11522  0.13222  -0.21858 57  LYS A CA  
3    C C   . LYS A 11 ? 0.97373 0.84477 0.71498 0.10275  0.13757  -0.18847 57  LYS A C   
4    O O   . LYS A 11 ? 1.01879 0.91301 0.73448 0.08080  0.15262  -0.17304 57  LYS A O   
5    C CB  . LYS A 11 ? 1.04009 0.92024 0.79815 0.13282  0.15917  -0.24916 57  LYS A CB  
6    C CG  . LYS A 11 ? 1.10226 0.94486 0.83320 0.14891  0.15811  -0.27786 57  LYS A CG  
7    C CD  . LYS A 11 ? 1.14676 0.99602 0.82160 0.12802  0.16674  -0.29270 57  LYS A CD  
8    C CE  . LYS A 11 ? 1.14878 1.04506 0.81310 0.11139  0.20927  -0.29050 57  LYS A CE  
9    N NZ  . LYS A 11 ? 1.17568 1.13348 0.80565 0.11300  0.19227  -0.31340 57  LYS A NZ  
10   N N   . ASP A 12 ? 0.90291 0.76588 0.68813 0.11364  0.12459  -0.17694 58  ASP A N   
11   C CA  . ASP A 12 ? 0.81396 0.69193 0.61747 0.10077  0.12770  -0.14798 58  ASP A CA  
12   C C   . ASP A 12 ? 0.76194 0.58846 0.51805 0.07721  0.11657  -0.12229 58  ASP A C   
13   O O   . ASP A 12 ? 0.79206 0.56591 0.51831 0.07570  0.09383  -0.12191 58  ASP A O   
14   C CB  . ASP A 12 ? 0.75766 0.63608 0.61455 0.11633  0.11230  -0.14207 58  ASP A CB  
15   C CG  . ASP A 12 ? 0.87430 0.80640 0.78485 0.13195  0.12735  -0.16163 58  ASP A CG  
16   O OD1 . ASP A 12 ? 0.90428 0.81257 0.82615 0.15272  0.11787  -0.17409 58  ASP A OD1 
17   O OD2 . ASP A 12 ? 0.85661 0.84527 0.79051 0.12095  0.14882  -0.15728 58  ASP A OD2 
18   N N   . THR A 13 ? 0.67914 0.52911 0.43802 0.05442  0.12582  -0.09896 59  THR A N   
19   C CA  . THR A 13 ? 0.61869 0.44003 0.35529 0.03154  0.10596  -0.07166 59  THR A CA  
20   C C   . THR A 13 ? 0.56151 0.36301 0.32994 0.03629  0.08057  -0.05873 59  THR A C   
21   O O   . THR A 13 ? 0.48648 0.30976 0.30060 0.04394  0.08243  -0.05346 59  THR A O   
22   C CB  . THR A 13 ? 0.61777 0.46454 0.35548 0.01011  0.11661  -0.04998 59  THR A CB  
23   O OG1 . THR A 13 ? 0.62981 0.49458 0.32786 -0.00285 0.14049  -0.05991 59  THR A OG1 
24   C CG2 . THR A 13 ? 0.56334 0.38136 0.28619 -0.00534 0.09135  -0.02344 59  THR A CG2 
25   N N   . PRO A 14 ? 0.54923 0.31399 0.29387 0.02860  0.05698  -0.05363 60  PRO A N   
26   C CA  . PRO A 14 ? 0.51057 0.26815 0.28451 0.02509  0.03570  -0.03938 60  PRO A CA  
27   C C   . PRO A 14 ? 0.44537 0.23328 0.25051 0.01647  0.03607  -0.01761 60  PRO A C   
28   O O   . PRO A 14 ? 0.45083 0.24262 0.23865 0.00619  0.03549  -0.00664 60  PRO A O   
29   C CB  . PRO A 14 ? 0.57011 0.29292 0.30698 0.01098  0.01266  -0.03810 60  PRO A CB  
30   C CG  . PRO A 14 ? 0.58009 0.27782 0.26562 0.01518  0.02113  -0.05925 60  PRO A CG  
31   C CD  . PRO A 14 ? 0.59101 0.32360 0.27932 0.01899  0.04875  -0.06122 60  PRO A CD  
32   N N   . PHE A 15 ? 0.39614 0.20001 0.24288 0.02129  0.03456  -0.01191 61  PHE A N   
33   C CA  . PHE A 15 ? 0.35976 0.18870 0.23467 0.01649  0.03539  0.00399  61  PHE A CA  
34   C C   . PHE A 15 ? 0.33778 0.17488 0.24181 0.01352  0.02179  0.01055  61  PHE A C   
35   O O   . PHE A 15 ? 0.33894 0.16274 0.24482 0.01397  0.01476  0.00519  61  PHE A O   
36   C CB  . PHE A 15 ? 0.33129 0.18329 0.22647 0.02172  0.05564  0.00304  61  PHE A CB  
37   C CG  . PHE A 15 ? 0.33680 0.20044 0.26396 0.03364  0.05981  -0.00534 61  PHE A CG  
38   C CD1 . PHE A 15 ? 0.33702 0.20946 0.29427 0.03240  0.05148  0.00313  61  PHE A CD1 
39   C CD2 . PHE A 15 ? 0.37860 0.24562 0.30431 0.04766  0.07063  -0.02339 61  PHE A CD2 
40   C CE1 . PHE A 15 ? 0.29797 0.17628 0.27899 0.04191  0.05083  -0.00230 61  PHE A CE1 
41   C CE2 . PHE A 15 ? 0.35532 0.23116 0.31156 0.06264  0.06877  -0.03099 61  PHE A CE2 
42   C CZ  . PHE A 15 ? 0.31872 0.19681 0.30011 0.05814  0.05720  -0.01835 61  PHE A CZ  
43   N N   . MET A 16 ? 0.32257 0.17965 0.24566 0.01008  0.01734  0.02149  62  MET A N   
44   C CA  . MET A 16 ? 0.31605 0.19446 0.27122 0.00753  0.01188  0.02530  62  MET A CA  
45   C C   . MET A 16 ? 0.25999 0.15483 0.23604 0.01367  0.01892  0.03045  62  MET A C   
46   O O   . MET A 16 ? 0.29212 0.18282 0.25861 0.01610  0.01463  0.03555  62  MET A O   
47   C CB  . MET A 16 ? 0.31318 0.20321 0.26840 -0.00397 -0.00529 0.02778  62  MET A CB  
48   C CG  . MET A 16 ? 0.33772 0.26573 0.32629 -0.00873 -0.00866 0.02993  62  MET A CG  
49   S SD  . MET A 16 ? 0.52075 0.48029 0.51297 -0.02583 -0.02749 0.03036  62  MET A SD  
50   C CE  . MET A 16 ? 0.38226 0.29449 0.32815 -0.03836 -0.03721 0.02941  62  MET A CE  
51   N N   . VAL A 17 ? 0.24915 0.15493 0.24783 0.01569  0.02700  0.02941  63  VAL A N   
52   C CA  . VAL A 17 ? 0.22482 0.13890 0.23879 0.01927  0.03300  0.03257  63  VAL A CA  
53   C C   . VAL A 17 ? 0.20122 0.13765 0.23980 0.01842  0.02851  0.03077  63  VAL A C   
54   O O   . VAL A 17 ? 0.20059 0.14483 0.24653 0.01196  0.02831  0.02904  63  VAL A O   
55   C CB  . VAL A 17 ? 0.24937 0.16326 0.26789 0.01926  0.04717  0.03114  63  VAL A CB  
56   C CG1 . VAL A 17 ? 0.23680 0.15441 0.26747 0.01745  0.05034  0.03488  63  VAL A CG1 
57   C CG2 . VAL A 17 ? 0.28019 0.18413 0.27472 0.01792  0.05653  0.02956  63  VAL A CG2 
58   N N   . GLN A 18 ? 0.19370 0.13858 0.24123 0.02510  0.02336  0.03013  64  GLN A N   
59   C CA  . GLN A 18 ? 0.16819 0.14118 0.23907 0.02656  0.02259  0.02347  64  GLN A CA  
60   C C   . GLN A 18 ? 0.19115 0.15215 0.26620 0.03340  0.02698  0.02161  64  GLN A C   
61   O O   . GLN A 18 ? 0.20080 0.13800 0.26501 0.04240  0.02117  0.02402  64  GLN A O   
62   C CB  . GLN A 18 ? 0.16401 0.16441 0.24693 0.03343  0.01148  0.01794  64  GLN A CB  
63   C CG  . GLN A 18 ? 0.16520 0.20703 0.27504 0.03760  0.01387  0.00535  64  GLN A CG  
64   C CD  . GLN A 18 ? 0.17835 0.26660 0.30773 0.04091  0.00487  -0.00262 64  GLN A CD  
65   O OE1 . GLN A 18 ? 0.16026 0.25292 0.28185 0.02982  -0.00240 0.00341  64  GLN A OE1 
66   N NE2 . GLN A 18 ? 0.19160 0.31845 0.34760 0.05675  0.00460  -0.01860 64  GLN A NE2 
67   N N   . VAL A 19 ? 0.17334 0.14462 0.25840 0.02688  0.03411  0.01831  65  VAL A N   
68   C CA  . VAL A 19 ? 0.18098 0.13850 0.26671 0.02979  0.03671  0.01541  65  VAL A CA  
69   C C   . VAL A 19 ? 0.19090 0.17425 0.29040 0.03116  0.03811  0.00308  65  VAL A C   
70   O O   . VAL A 19 ? 0.16375 0.17664 0.27005 0.02115  0.04081  0.00086  65  VAL A O   
71   C CB  . VAL A 19 ? 0.19538 0.14114 0.27720 0.01841  0.04414  0.02205  65  VAL A CB  
72   C CG1 . VAL A 19 ? 0.22557 0.15663 0.28987 0.01539  0.04538  0.02904  65  VAL A CG1 
73   C CG2 . VAL A 19 ? 0.19110 0.15582 0.28164 0.01000  0.04617  0.02257  65  VAL A CG2 
74   N N   . LYS A 20 ? 0.19141 0.15986 0.28941 0.04118  0.03580  -0.00546 66  LYS A N   
75   C CA  . LYS A 20 ? 0.20002 0.19235 0.30731 0.04453  0.03915  -0.02206 66  LYS A CA  
76   C C   . LYS A 20 ? 0.24109 0.21778 0.33887 0.02974  0.04376  -0.01990 66  LYS A C   
77   O O   . LYS A 20 ? 0.23614 0.17574 0.32186 0.02790  0.04044  -0.01438 66  LYS A O   
78   C CB  . LYS A 20 ? 0.23809 0.22037 0.34847 0.07041  0.03045  -0.03795 66  LYS A CB  
79   C CG  . LYS A 20 ? 0.31170 0.31440 0.42580 0.07756  0.03486  -0.06005 66  LYS A CG  
80   C CD  . LYS A 20 ? 0.30609 0.36892 0.43422 0.06063  0.04894  -0.06735 66  LYS A CD  
81   C CE  . LYS A 20 ? 0.29371 0.37823 0.41806 0.06432  0.05545  -0.08992 66  LYS A CE  
82   N NZ  . LYS A 20 ? 0.38173 0.41759 0.48697 0.06340  0.05418  -0.09534 66  LYS A NZ  
83   N N   . LEU A 21 ? 0.20845 0.21335 0.30849 0.01549  0.04955  -0.02294 67  LEU A N   
84   C CA  . LEU A 21 ? 0.20735 0.20139 0.29845 0.00018  0.05025  -0.01975 67  LEU A CA  
85   C C   . LEU A 21 ? 0.22818 0.23608 0.31229 -0.00149 0.05397  -0.03800 67  LEU A C   
86   O O   . LEU A 21 ? 0.21970 0.26289 0.30930 0.00264  0.05972  -0.05116 67  LEU A O   
87   C CB  . LEU A 21 ? 0.19209 0.19755 0.28343 -0.01636 0.04879  -0.00561 67  LEU A CB  
88   C CG  . LEU A 21 ? 0.19604 0.18980 0.29291 -0.01276 0.04633  0.00777  67  LEU A CG  
89   C CD1 . LEU A 21 ? 0.18198 0.18044 0.27682 -0.02284 0.04051  0.01743  67  LEU A CD1 
90   C CD2 . LEU A 21 ? 0.21419 0.18726 0.31266 -0.01123 0.04695  0.01228  67  LEU A CD2 
91   N N   . PRO A 22 ? 0.25359 0.23967 0.32489 -0.00986 0.05154  -0.04078 68  PRO A N   
92   C CA  . PRO A 22 ? 0.25434 0.25118 0.31253 -0.01229 0.05564  -0.06107 68  PRO A CA  
93   C C   . PRO A 22 ? 0.25413 0.28334 0.30337 -0.03576 0.05916  -0.05656 68  PRO A C   
94   O O   . PRO A 22 ? 0.22233 0.26113 0.27636 -0.04657 0.05600  -0.03832 68  PRO A O   
95   C CB  . PRO A 22 ? 0.29556 0.24898 0.33776 -0.01773 0.04812  -0.06229 68  PRO A CB  
96   C CG  . PRO A 22 ? 0.29302 0.23961 0.34391 -0.03240 0.04280  -0.03758 68  PRO A CG  
97   C CD  . PRO A 22 ? 0.26176 0.21752 0.32930 -0.01981 0.04540  -0.02757 68  PRO A CD  
98   N N   . ASN A 23 ? 0.25529 0.29483 0.28532 -0.04487 0.06358  -0.07305 69  ASN A N   
99   C CA  . ASN A 23 ? 0.29714 0.35720 0.30731 -0.07323 0.06322  -0.06521 69  ASN A CA  
100  C C   . ASN A 23 ? 0.29234 0.32624 0.30146 -0.08643 0.04752  -0.04020 69  ASN A C   
101  O O   . ASN A 23 ? 0.29349 0.30064 0.31184 -0.07968 0.04090  -0.03619 69  ASN A O   
102  C CB  . ASN A 23 ? 0.33679 0.40641 0.31973 -0.08254 0.06994  -0.08803 69  ASN A CB  
103  C CG  . ASN A 23 ? 0.36649 0.48085 0.35434 -0.06933 0.08783  -0.11700 69  ASN A CG  
104  O OD1 . ASN A 23 ? 0.29361 0.44388 0.30157 -0.06506 0.09446  -0.11491 69  ASN A OD1 
105  N ND2 . ASN A 23 ? 0.41049 0.52567 0.38150 -0.06176 0.09500  -0.14651 69  ASN A ND2 
106  N N   . TYR A 24 ? 0.23975 0.46856 0.26204 -0.03348 0.01870  -0.11988 70  TYR A N   
107  C CA  . TYR A 24 ? 0.27926 0.47018 0.27066 -0.03336 -0.00391 -0.08120 70  TYR A CA  
108  C C   . TYR A 24 ? 0.29196 0.47462 0.27847 -0.02912 -0.02315 -0.08699 70  TYR A C   
109  O O   . TYR A 24 ? 0.29242 0.45588 0.30174 -0.01562 -0.04220 -0.07063 70  TYR A O   
110  C CB  . TYR A 24 ? 0.33296 0.50944 0.25727 -0.06034 -0.00031 -0.05825 70  TYR A CB  
111  C CG  . TYR A 24 ? 0.35503 0.48921 0.25191 -0.05501 -0.03020 -0.02089 70  TYR A CG  
112  C CD1 . TYR A 24 ? 0.32018 0.43466 0.25192 -0.03764 -0.03930 -0.00004 70  TYR A CD1 
113  C CD2 . TYR A 24 ? 0.40869 0.52443 0.24626 -0.06586 -0.05189 -0.01071 70  TYR A CD2 
114  C CE1 . TYR A 24 ? 0.35909 0.44092 0.28062 -0.02864 -0.06699 0.02532  70  TYR A CE1 
115  C CE2 . TYR A 24 ? 0.43992 0.51924 0.26348 -0.05451 -0.08673 0.01910  70  TYR A CE2 
116  C CZ  . TYR A 24 ? 0.37643 0.44098 0.24855 -0.03471 -0.09296 0.03480  70  TYR A CZ  
117  O OH  . TYR A 24 ? 0.46040 0.49399 0.33176 -0.01956 -0.12840 0.05635  70  TYR A OH  
118  N N   . LYS A 25 ? 0.34789 0.55049 0.30894 -0.04312 -0.01635 -0.11623 71  LYS A N   
119  C CA  . LYS A 25 ? 0.34386 0.54166 0.29681 -0.04271 -0.03785 -0.12497 71  LYS A CA  
120  C C   . LYS A 25 ? 0.32945 0.52160 0.35135 -0.02259 -0.04205 -0.14112 71  LYS A C   
121  O O   . LYS A 25 ? 0.34345 0.52677 0.37928 -0.02003 -0.06210 -0.13829 71  LYS A O   
122  C CB  . LYS A 25 ? 0.41914 0.63872 0.31849 -0.06625 -0.02874 -0.15610 71  LYS A CB  
123  C CG  . LYS A 25 ? 0.55409 0.75938 0.35792 -0.09363 -0.03307 -0.13045 71  LYS A CG  
124  C CD  . LYS A 25 ? 0.59376 0.76221 0.37850 -0.08300 -0.07418 -0.08656 71  LYS A CD  
125  C CE  . LYS A 25 ? 0.64378 0.81310 0.44105 -0.07210 -0.10948 -0.09627 71  LYS A CE  
126  N NZ  . LYS A 25 ? 0.67889 0.81701 0.46185 -0.05902 -0.15223 -0.06016 71  LYS A NZ  
127  N N   . ASP A 26 ? 0.32036 0.51442 0.38616 -0.00922 -0.02561 -0.15845 72  ASP A N   
128  C CA  . ASP A 26 ? 0.27698 0.44518 0.39459 0.00748  -0.03114 -0.16548 72  ASP A CA  
129  C C   . ASP A 26 ? 0.28124 0.42173 0.41362 0.01578  -0.03816 -0.12852 72  ASP A C   
130  O O   . ASP A 26 ? 0.28318 0.40091 0.43811 0.01558  -0.04421 -0.12478 72  ASP A O   
131  C CB  . ASP A 26 ? 0.29207 0.46063 0.44749 0.02406  -0.02013 -0.19469 72  ASP A CB  
132  C CG  . ASP A 26 ? 0.30981 0.51348 0.46228 0.01595  -0.00674 -0.24340 72  ASP A CG  
133  O OD1 . ASP A 26 ? 0.35733 0.56382 0.49358 0.00281  -0.01074 -0.26337 72  ASP A OD1 
134  O OD2 . ASP A 26 ? 0.37486 0.60772 0.54647 0.02158  0.00815  -0.26515 72  ASP A OD2 
135  N N   . TYR A 27 ? 0.24382 0.38789 0.36350 0.01865  -0.03381 -0.10533 73  TYR A N   
136  C CA  . TYR A 27 ? 0.25197 0.37446 0.38007 0.02417  -0.03726 -0.07518 73  TYR A CA  
137  C C   . TYR A 27 ? 0.24772 0.36884 0.37893 0.01703  -0.04866 -0.06510 73  TYR A C   
138  O O   . TYR A 27 ? 0.22346 0.32893 0.37921 0.01779  -0.04668 -0.05708 73  TYR A O   
139  C CB  . TYR A 27 ? 0.21657 0.34831 0.32651 0.02388  -0.03186 -0.05848 73  TYR A CB  
140  C CG  . TYR A 27 ? 0.19738 0.31587 0.30345 0.02374  -0.03631 -0.03157 73  TYR A CG  
141  C CD1 . TYR A 27 ? 0.19786 0.29804 0.31854 0.03162  -0.03215 -0.02028 73  TYR A CD1 
142  C CD2 . TYR A 27 ? 0.19044 0.31056 0.27364 0.01623  -0.04620 -0.01884 73  TYR A CD2 
143  C CE1 . TYR A 27 ? 0.14523 0.23832 0.26639 0.03069  -0.03194 -0.00397 73  TYR A CE1 
144  C CE2 . TYR A 27 ? 0.20191 0.30910 0.29193 0.02050  -0.05156 -0.00065 73  TYR A CE2 
145  C CZ  . TYR A 27 ? 0.17371 0.27218 0.28682 0.02715  -0.04138 0.00324  73  TYR A CZ  
146  O OH  . TYR A 27 ? 0.19954 0.28990 0.32387 0.03063  -0.04296 0.01301  73  TYR A OH  
147  N N   . LEU A 28 ? 0.24472 0.38313 0.34991 0.00895  -0.06159 -0.06699 74  LEU A N   
148  C CA  . LEU A 28 ? 0.27651 0.42023 0.39368 0.00818  -0.08210 -0.06177 74  LEU A CA  
149  C C   . LEU A 28 ? 0.29041 0.43868 0.45114 0.00404  -0.08358 -0.08347 74  LEU A C   
150  O O   . LEU A 28 ? 0.26529 0.42489 0.46142 0.00393  -0.09400 -0.08452 74  LEU A O   
151  C CB  . LEU A 28 ? 0.31960 0.47186 0.38771 0.00148  -0.10460 -0.05943 74  LEU A CB  
152  C CG  . LEU A 28 ? 0.33493 0.47061 0.35255 -0.00108 -0.10851 -0.03205 74  LEU A CG  
153  C CD1 . LEU A 28 ? 0.39196 0.52101 0.34490 -0.01125 -0.13627 -0.02586 74  LEU A CD1 
154  C CD2 . LEU A 28 ? 0.35263 0.47360 0.40074 0.01250  -0.11375 -0.01074 74  LEU A CD2 
155  N N   . LEU A 29 ? 0.29533 0.43621 0.46036 -0.00042 -0.07321 -0.10534 75  LEU A N   
156  C CA  . LEU A 29 ? 0.25752 0.39236 0.46111 -0.00983 -0.07192 -0.12750 75  LEU A CA  
157  C C   . LEU A 29 ? 0.29017 0.38856 0.51921 -0.01230 -0.05233 -0.11699 75  LEU A C   
158  O O   . LEU A 29 ? 0.31238 0.39785 0.57152 -0.02728 -0.04645 -0.13179 75  LEU A O   
159  C CB  . LEU A 29 ? 0.28553 0.41871 0.47999 -0.01388 -0.07070 -0.15916 75  LEU A CB  
160  C CG  . LEU A 29 ? 0.35539 0.51999 0.50519 -0.01828 -0.08401 -0.17273 75  LEU A CG  
161  C CD1 . LEU A 29 ? 0.33757 0.50290 0.48198 -0.02203 -0.07354 -0.21140 75  LEU A CD1 
162  C CD2 . LEU A 29 ? 0.33439 0.52012 0.48189 -0.02515 -0.10998 -0.17387 75  LEU A CD2 
163  N N   . ASP A 30 ? 0.25868 0.33688 0.46989 -0.00183 -0.04229 -0.09263 76  ASP A N   
164  C CA  . ASP A 30 ? 0.26569 0.29995 0.47804 -0.00519 -0.02680 -0.07708 76  ASP A CA  
165  C C   . ASP A 30 ? 0.23689 0.28475 0.45750 -0.01159 -0.01818 -0.06125 76  ASP A C   
166  O O   . ASP A 30 ? 0.20078 0.25210 0.40249 -0.00101 -0.01748 -0.04359 76  ASP A O   
167  C CB  . ASP A 30 ? 0.25873 0.26588 0.44567 0.01307  -0.02789 -0.06637 76  ASP A CB  
168  C CG  . ASP A 30 ? 0.32707 0.27234 0.49835 0.01116  -0.02134 -0.04848 76  ASP A CG  
169  O OD1 . ASP A 30 ? 0.32846 0.25651 0.49774 -0.00929 -0.00686 -0.03788 76  ASP A OD1 
170  O OD2 . ASP A 30 ? 0.33252 0.24544 0.49134 0.02946  -0.03164 -0.04598 76  ASP A OD2 
171  N N   . ASN A 31 ? 0.21081 0.27071 0.46714 -0.03059 -0.00979 -0.07401 77  ASN A N   
172  C CA  . ASN A 31 ? 0.16944 0.25657 0.45114 -0.03609 -0.00004 -0.07190 77  ASN A CA  
173  C C   . ASN A 31 ? 0.16781 0.22006 0.41681 -0.04068 0.02207  -0.05031 77  ASN A C   
174  O O   . ASN A 31 ? 0.16198 0.23375 0.41431 -0.03439 0.02625  -0.04485 77  ASN A O   
175  C CB  . ASN A 31 ? 0.16323 0.27702 0.50049 -0.05938 0.00999  -0.09870 77  ASN A CB  
176  C CG  . ASN A 31 ? 0.20159 0.34568 0.55095 -0.04948 -0.01712 -0.11768 77  ASN A CG  
177  O OD1 . ASN A 31 ? 0.21323 0.35244 0.57582 -0.06415 -0.01486 -0.13632 77  ASN A OD1 
178  N ND2 . ASN A 31 ? 0.15250 0.31906 0.48863 -0.02703 -0.04257 -0.11090 77  ASN A ND2 
179  N N   . LYS A 32 ? 0.23192 0.22697 0.44584 -0.05213 0.03397  -0.03890 78  LYS A N   
180  C CA  . LYS A 32 ? 0.26797 0.22288 0.43515 -0.05866 0.05005  -0.01630 78  LYS A CA  
181  C C   . LYS A 32 ? 0.26758 0.22838 0.40722 -0.03086 0.03288  -0.00116 78  LYS A C   
182  O O   . LYS A 32 ? 0.27423 0.23799 0.39474 -0.03204 0.04242  0.00782  78  LYS A O   
183  C CB  . LYS A 32 ? 0.36205 0.23886 0.48596 -0.07457 0.05675  -0.00229 78  LYS A CB  
184  C CG  . LYS A 32 ? 0.45820 0.27886 0.51221 -0.07263 0.05730  0.02721  78  LYS A CG  
185  C CD  . LYS A 32 ? 0.55003 0.28550 0.55996 -0.06693 0.03976  0.04465  78  LYS A CD  
186  C CE  . LYS A 32 ? 0.67465 0.33455 0.63657 -0.10829 0.06486  0.06004  78  LYS A CE  
187  N NZ  . LYS A 32 ? 0.81007 0.40554 0.68995 -0.10229 0.04984  0.09426  78  LYS A NZ  
188  N N   . GLN A 33 ? 0.25906 0.22715 0.40038 -0.00915 0.01051  -0.00399 79  GLN A N   
189  C CA  . GLN A 33 ? 0.23665 0.21887 0.36156 0.01191  -0.00272 0.00378  79  GLN A CA  
190  C C   . GLN A 33 ? 0.16885 0.19577 0.31135 0.01453  -0.00311 0.00109  79  GLN A C   
191  O O   . GLN A 33 ? 0.20074 0.23122 0.32800 0.02030  -0.00268 0.00979  79  GLN A O   
192  C CB  . GLN A 33 ? 0.23181 0.21689 0.36149 0.02829  -0.01911 -0.00725 79  GLN A CB  
193  C CG  . GLN A 33 ? 0.23641 0.23755 0.35643 0.04565  -0.02908 -0.00555 79  GLN A CG  
194  C CD  . GLN A 33 ? 0.25837 0.26718 0.39418 0.05983  -0.03956 -0.02597 79  GLN A CD  
195  O OE1 . GLN A 33 ? 0.24215 0.28207 0.39144 0.05538  -0.03705 -0.04405 79  GLN A OE1 
196  N NE2 . GLN A 33 ? 0.24422 0.22253 0.37767 0.07749  -0.05338 -0.02610 79  GLN A NE2 
197  N N   . VAL A 34 ? 0.16045 0.21679 0.33415 0.01115  -0.00802 -0.01152 80  VAL A N   
198  C CA  . VAL A 34 ? 0.16108 0.24546 0.35027 0.01699  -0.01555 -0.01139 80  VAL A CA  
199  C C   . VAL A 34 ? 0.15817 0.24294 0.35963 0.01196  0.00133  -0.01110 80  VAL A C   
200  O O   . VAL A 34 ? 0.15385 0.24078 0.34886 0.01983  -0.00046 -0.00541 80  VAL A O   
201  C CB  . VAL A 34 ? 0.14556 0.25726 0.36632 0.01695  -0.03225 -0.02582 80  VAL A CB  
202  C CG1 . VAL A 34 ? 0.15613 0.27625 0.38118 0.02527  -0.04262 -0.02353 80  VAL A CG1 
203  C CG2 . VAL A 34 ? 0.18051 0.29460 0.37616 0.01962  -0.04797 -0.02834 80  VAL A CG2 
204  N N   . VAL A 35 ? 0.15707 0.24034 0.37717 -0.00518 0.02125  -0.02137 81  VAL A N   
205  C CA  . VAL A 35 ? 0.13799 0.22825 0.36915 -0.01584 0.04525  -0.02891 81  VAL A CA  
206  C C   . VAL A 35 ? 0.19361 0.25216 0.36790 -0.01521 0.05269  -0.01127 81  VAL A C   
207  O O   . VAL A 35 ? 0.18292 0.25174 0.35916 -0.01128 0.05874  -0.01594 81  VAL A O   
208  C CB  . VAL A 35 ? 0.18124 0.27389 0.43388 -0.04472 0.07343  -0.04487 81  VAL A CB  
209  C CG1 . VAL A 35 ? 0.22185 0.31430 0.46424 -0.06459 0.10833  -0.05286 81  VAL A CG1 
210  C CG2 . VAL A 35 ? 0.13917 0.27149 0.44936 -0.04135 0.06035  -0.07042 81  VAL A CG2 
211  N N   . LEU A 36 ? 0.22722 0.24709 0.35391 -0.01568 0.04691  0.00612  82  LEU A N   
212  C CA  . LEU A 36 ? 0.27782 0.27053 0.35179 -0.01217 0.04506  0.02083  82  LEU A CA  
213  C C   . LEU A 36 ? 0.23590 0.25280 0.31853 0.00602  0.02967  0.01974  82  LEU A C   
214  O O   . LEU A 36 ? 0.24020 0.25724 0.30568 0.00430  0.03586  0.01828  82  LEU A O   
215  C CB  . LEU A 36 ? 0.29629 0.24262 0.32864 -0.00777 0.03042  0.03718  82  LEU A CB  
216  C CG  . LEU A 36 ? 0.36655 0.28833 0.35252 0.00655  0.01068  0.05069  82  LEU A CG  
217  C CD1 . LEU A 36 ? 0.43343 0.33690 0.36892 -0.00869 0.02436  0.05716  82  LEU A CD1 
218  C CD2 . LEU A 36 ? 0.39425 0.26660 0.35483 0.01645  -0.00992 0.06261  82  LEU A CD2 
219  N N   . THR A 37 ? 0.17703 0.21231 0.28183 0.01871  0.01232  0.01841  83  THR A N   
220  C CA  . THR A 37 ? 0.18965 0.23905 0.29441 0.02726  0.00259  0.01911  83  THR A CA  
221  C C   . THR A 37 ? 0.18327 0.24210 0.30982 0.02643  0.00858  0.01224  83  THR A C   
222  O O   . THR A 37 ? 0.18003 0.23648 0.29818 0.02779  0.00762  0.01182  83  THR A O   
223  C CB  . THR A 37 ? 0.16907 0.23246 0.28085 0.03262  -0.01109 0.01881  83  THR A CB  
224  O OG1 . THR A 37 ? 0.17818 0.25094 0.31200 0.03176  -0.01619 0.01512  83  THR A OG1 
225  C CG2 . THR A 37 ? 0.19441 0.25440 0.29670 0.03787  -0.01708 0.01611  83  THR A CG2 
226  N N   . PHE A 38 ? 0.14312 0.21433 0.30575 0.02544  0.01266  0.00224  84  PHE A N   
227  C CA  . PHE A 38 ? 0.15820 0.23907 0.35426 0.03111  0.01424  -0.01043 84  PHE A CA  
228  C C   . PHE A 38 ? 0.15641 0.23699 0.34660 0.02069  0.04031  -0.02402 84  PHE A C   
229  O O   . PHE A 38 ? 0.17245 0.25333 0.37637 0.02607  0.04241  -0.03548 84  PHE A O   
230  C CB  . PHE A 38 ? 0.16542 0.26084 0.39681 0.03541  0.00325  -0.02191 84  PHE A CB  
231  C CG  . PHE A 38 ? 0.20642 0.29074 0.42223 0.04522  -0.02506 -0.00936 84  PHE A CG  
232  C CD1 . PHE A 38 ? 0.19526 0.26119 0.40862 0.05484  -0.03975 -0.00449 84  PHE A CD1 
233  C CD2 . PHE A 38 ? 0.21177 0.29908 0.41093 0.04251  -0.03503 -0.00181 84  PHE A CD2 
234  C CE1 . PHE A 38 ? 0.22665 0.27416 0.41610 0.05965  -0.06460 0.01148  84  PHE A CE1 
235  C CE2 . PHE A 38 ? 0.21572 0.29376 0.39343 0.04743  -0.05780 0.00943  84  PHE A CE2 
236  C CZ  . PHE A 38 ? 0.22929 0.28493 0.39812 0.05489  -0.07279 0.01864  84  PHE A CZ  
237  N N   . LYS A 39 ? 0.15045 0.22411 0.31396 0.00337  0.06070  -0.02360 85  LYS A N   
238  C CA  . LYS A 39 ? 0.16518 0.23063 0.29643 -0.01172 0.08524  -0.03265 85  LYS A CA  
239  C C   . LYS A 39 ? 0.19107 0.23992 0.28047 -0.00512 0.07199  -0.02314 85  LYS A C   
240  O O   . LYS A 39 ? 0.22587 0.27873 0.31338 -0.00816 0.08278  -0.03967 85  LYS A O   
241  C CB  . LYS A 39 ? 0.23472 0.27789 0.32031 -0.03681 0.10704  -0.02560 85  LYS A CB  
242  C CG  . LYS A 39 ? 0.30599 0.36946 0.43742 -0.05246 0.12720  -0.04123 85  LYS A CG  
243  C CD  . LYS A 39 ? 0.40319 0.43240 0.47716 -0.08805 0.15737  -0.03408 85  LYS A CD  
244  C CE  . LYS A 39 ? 0.44441 0.49342 0.56574 -0.10510 0.17261  -0.05230 85  LYS A CE  
245  N NZ  . LYS A 39 ? 0.54875 0.54493 0.60975 -0.13394 0.18559  -0.03321 85  LYS A NZ  
246  N N   . LEU A 40 ? 0.21142 0.24826 0.27767 0.00407  0.04873  -0.00351 86  LEU A N   
247  C CA  . LEU A 40 ? 0.24564 0.27917 0.28824 0.00920  0.03475  -0.00129 86  LEU A CA  
248  C C   . LEU A 40 ? 0.20248 0.24586 0.27925 0.01412  0.03261  -0.01283 86  LEU A C   
249  O O   . LEU A 40 ? 0.21408 0.25509 0.28038 0.00979  0.03647  -0.02510 86  LEU A O   
250  C CB  . LEU A 40 ? 0.21832 0.25119 0.25194 0.01900  0.01243  0.01208  86  LEU A CB  
251  C CG  . LEU A 40 ? 0.28262 0.29251 0.27525 0.02085  0.00226  0.02360  86  LEU A CG  
252  C CD1 . LEU A 40 ? 0.23395 0.25666 0.24178 0.03655  -0.02141 0.02449  86  LEU A CD1 
253  C CD2 . LEU A 40 ? 0.31332 0.30623 0.25360 0.01346  0.00169  0.02267  86  LEU A CD2 
254  N N   . VAL A 41 ? 0.18529 0.23257 0.29669 0.02235  0.02313  -0.00821 87  VAL A N   
255  C CA  . VAL A 41 ? 0.18490 0.22272 0.31937 0.02729  0.01530  -0.01233 87  VAL A CA  
256  C C   . VAL A 41 ? 0.19460 0.23119 0.35498 0.02918  0.02878  -0.03609 87  VAL A C   
257  O O   . VAL A 41 ? 0.20277 0.22434 0.36481 0.02808  0.02818  -0.04604 87  VAL A O   
258  C CB  . VAL A 41 ? 0.21128 0.24486 0.36585 0.03615  -0.00190 -0.00047 87  VAL A CB  
259  C CG1 . VAL A 41 ? 0.21562 0.22313 0.39039 0.04426  -0.01491 -0.00203 87  VAL A CG1 
260  C CG2 . VAL A 41 ? 0.17974 0.21538 0.30496 0.02990  -0.01065 0.01597  87  VAL A CG2 
261  N N   . HIS A 42 ? 0.19603 0.25082 0.38196 0.02951  0.04404  -0.05086 88  HIS A N   
262  C CA  . HIS A 42 ? 0.19371 0.25946 0.41872 0.03143  0.06198  -0.08385 88  HIS A CA  
263  C C   . HIS A 42 ? 0.21376 0.27432 0.40114 0.01713  0.08115  -0.10015 88  HIS A C   
264  O O   . HIS A 42 ? 0.24451 0.30917 0.46313 0.01967  0.09407  -0.13205 88  HIS A O   
265  C CB  . HIS A 42 ? 0.19273 0.28579 0.44179 0.02356  0.07958  -0.09801 88  HIS A CB  
266  C CG  . HIS A 42 ? 0.20065 0.29865 0.48299 0.03544  0.05433  -0.08991 88  HIS A CG  
267  N ND1 . HIS A 42 ? 0.21665 0.33508 0.51300 0.02564  0.06290  -0.09615 88  HIS A ND1 
268  C CD2 . HIS A 42 ? 0.22021 0.30169 0.51569 0.05305  0.02125  -0.07730 88  HIS A CD2 
269  C CE1 . HIS A 42 ? 0.20028 0.32020 0.52087 0.03911  0.03480  -0.09082 88  HIS A CE1 
270  N NE2 . HIS A 42 ? 0.22411 0.32030 0.53897 0.05548  0.00915  -0.07773 88  HIS A NE2 
271  N N   . HIS A 43 ? 0.20572 0.25824 0.32900 0.00398  0.08044  -0.08301 89  HIS A N   
272  C CA  . HIS A 43 ? 0.26610 0.31415 0.34164 -0.01043 0.09202  -0.09750 89  HIS A CA  
273  C C   . HIS A 43 ? 0.24595 0.28283 0.30436 -0.00863 0.07010  -0.09157 89  HIS A C   
274  O O   . HIS A 43 ? 0.28497 0.32112 0.30352 -0.01976 0.07241  -0.10500 89  HIS A O   
275  C CB  . HIS A 43 ? 0.32521 0.36723 0.33278 -0.02705 0.10119  -0.08379 89  HIS A CB  
276  C CG  . HIS A 43 ? 0.35366 0.40556 0.36331 -0.04371 0.13569  -0.09886 89  HIS A CG  
277  N ND1 . HIS A 43 ? 0.42799 0.47048 0.41594 -0.05416 0.14198  -0.07869 89  HIS A ND1 
278  C CD2 . HIS A 43 ? 0.38377 0.45627 0.41708 -0.05580 0.16977  -0.13717 89  HIS A CD2 
279  C CE1 . HIS A 43 ? 0.41247 0.47084 0.41081 -0.07583 0.18054  -0.10246 89  HIS A CE1 
280  N NE2 . HIS A 43 ? 0.39745 0.47352 0.42516 -0.07423 0.18869  -0.13422 89  HIS A NE2 
281  N N   . SER A 44 ? 0.26082 0.34368 0.23056 0.03099  0.10989  0.00065  90  SER A N   
282  C CA  . SER A 44 ? 0.25511 0.33132 0.20946 0.03129  0.08704  -0.01367 90  SER A CA  
283  C C   . SER A 44 ? 0.29280 0.36166 0.27222 0.02965  0.07803  -0.04648 90  SER A C   
284  O O   . SER A 44 ? 0.27305 0.33245 0.28773 0.02844  0.08425  -0.05185 90  SER A O   
285  C CB  . SER A 44 ? 0.26623 0.32011 0.23214 0.02301  0.07311  0.00629  90  SER A CB  
286  O OG  . SER A 44 ? 0.31076 0.36627 0.25485 0.02649  0.08100  0.03460  90  SER A OG  
287  N N   . LYS A 45 ? 0.25714 0.33084 0.22295 0.03011  0.06290  -0.06821 91  LYS A N   
288  C CA  . LYS A 45 ? 0.26680 0.32475 0.26423 0.02437  0.05308  -0.09630 91  LYS A CA  
289  C C   . LYS A 45 ? 0.24355 0.28458 0.25690 0.01321  0.03682  -0.08810 91  LYS A C   
290  O O   . LYS A 45 ? 0.24104 0.26080 0.28863 0.00563  0.03250  -0.09921 91  LYS A O   
291  C CB  . LYS A 45 ? 0.29055 0.37054 0.27175 0.03035  0.04946  -0.13698 91  LYS A CB  
292  C CG  . LYS A 45 ? 0.37727 0.48310 0.33390 0.04455  0.06732  -0.15245 91  LYS A CG  
293  C CD  . LYS A 45 ? 0.36684 0.45528 0.36467 0.04699  0.08158  -0.16474 91  LYS A CD  
294  C CE  . LYS A 45 ? 0.40610 0.52493 0.38236 0.06139  0.10536  -0.17048 91  LYS A CE  
295  N NZ  . LYS A 45 ? 0.48564 0.59992 0.48596 0.05999  0.12168  -0.13605 91  LYS A NZ  
296  N N   . LYS A 46 ? 0.22224 0.27178 0.21366 0.01323  0.03021  -0.06724 92  LYS A N   
297  C CA  . LYS A 46 ? 0.22207 0.26416 0.22596 0.00501  0.01727  -0.06028 92  LYS A CA  
298  C C   . LYS A 46 ? 0.20924 0.24550 0.20231 0.00697  0.01845  -0.02866 92  LYS A C   
299  O O   . LYS A 46 ? 0.21557 0.26256 0.18184 0.01561  0.02353  -0.01482 92  LYS A O   
300  C CB  . LYS A 46 ? 0.23679 0.30592 0.22895 0.00607  0.00335  -0.08154 92  LYS A CB  
301  C CG  . LYS A 46 ? 0.31963 0.38823 0.33376 -0.00322 -0.00762 -0.07849 92  LYS A CG  
302  C CD  . LYS A 46 ? 0.30765 0.40953 0.32492 -0.00444 -0.02295 -0.10907 92  LYS A CD  
303  C CE  . LYS A 46 ? 0.35875 0.47419 0.39265 -0.00895 -0.03301 -0.10094 92  LYS A CE  
304  N NZ  . LYS A 46 ? 0.35104 0.50596 0.39840 -0.01158 -0.05017 -0.13456 92  LYS A NZ  
305  N N   . ILE A 47 ? 0.18404 0.20251 0.19794 -0.00019 0.01534  -0.01729 93  ILE A N   
306  C CA  . ILE A 47 ? 0.18664 0.19870 0.19522 0.00119  0.01440  0.00449  93  ILE A CA  
307  C C   . ILE A 47 ? 0.20702 0.21944 0.22578 -0.00324 0.00573  0.00455  93  ILE A C   
308  O O   . ILE A 47 ? 0.19134 0.19513 0.22977 -0.01075 0.00578  0.00096  93  ILE A O   
309  C CB  . ILE A 47 ? 0.19290 0.18954 0.21595 -0.00113 0.02108  0.01591  93  ILE A CB  
310  C CG1 . ILE A 47 ? 0.22405 0.22697 0.24136 0.00284  0.03374  0.01861  93  ILE A CG1 
311  C CG2 . ILE A 47 ? 0.16362 0.15227 0.18730 -0.00151 0.01759  0.02965  93  ILE A CG2 
312  C CD1 . ILE A 47 ? 0.27645 0.27348 0.31920 -0.00019 0.03930  0.02215  93  ILE A CD1 
313  N N   . THR A 48 ? 0.17589 0.19850 0.18294 0.00297  0.00050  0.01138  94  THR A N   
314  C CA  . THR A 48 ? 0.18439 0.21353 0.20244 0.00139  -0.00502 0.01173  94  THR A CA  
315  C C   . THR A 48 ? 0.17376 0.18984 0.18843 0.00665  -0.00316 0.02583  94  THR A C   
316  O O   . THR A 48 ? 0.17623 0.18500 0.17956 0.01442  -0.00130 0.03594  94  THR A O   
317  C CB  . THR A 48 ? 0.19570 0.25374 0.21053 0.00755  -0.01485 0.00260  94  THR A CB  
318  O OG1 . THR A 48 ? 0.17477 0.24705 0.19548 0.00160  -0.01860 -0.01825 94  THR A OG1 
319  C CG2 . THR A 48 ? 0.16036 0.23208 0.19533 0.00565  -0.01790 0.00117  94  THR A CG2 
320  N N   . LEU A 49 ? 0.15823 0.17134 0.18325 0.00275  -0.00233 0.02607  95  LEU A N   
321  C CA  . LEU A 49 ? 0.14578 0.14970 0.16909 0.00799  -0.00196 0.03069  95  LEU A CA  
322  C C   . LEU A 49 ? 0.16008 0.18102 0.18891 0.01268  -0.00293 0.02671  95  LEU A C   
323  O O   . LEU A 49 ? 0.16088 0.19567 0.19855 0.00595  0.00018  0.02395  95  LEU A O   
324  C CB  . LEU A 49 ? 0.17035 0.16318 0.19586 0.00273  -0.00046 0.03134  95  LEU A CB  
325  C CG  . LEU A 49 ? 0.18585 0.16709 0.21480 -0.00044 0.00111  0.03390  95  LEU A CG  
326  C CD1 . LEU A 49 ? 0.17019 0.15013 0.20579 -0.00396 -0.00045 0.03416  95  LEU A CD1 
327  C CD2 . LEU A 49 ? 0.14710 0.11646 0.17959 0.00229  0.00233  0.03638  95  LEU A CD2 
328  N N   . ILE A 50 ? 0.14672 0.16633 0.17496 0.02463  -0.00505 0.02756  96  ILE A N   
329  C CA  . ILE A 50 ? 0.15745 0.19839 0.19563 0.03330  -0.00553 0.02212  96  ILE A CA  
330  C C   . ILE A 50 ? 0.17308 0.20164 0.21144 0.04143  -0.00261 0.01669  96  ILE A C   
331  O O   . ILE A 50 ? 0.19922 0.20355 0.23788 0.04851  -0.00420 0.01896  96  ILE A O   
332  C CB  . ILE A 50 ? 0.15781 0.21304 0.19881 0.04633  -0.01310 0.02548  96  ILE A CB  
333  C CG1 . ILE A 50 ? 0.14570 0.21535 0.18162 0.03956  -0.01863 0.02442  96  ILE A CG1 
334  C CG2 . ILE A 50 ? 0.16401 0.24854 0.22387 0.05675  -0.01413 0.01802  96  ILE A CG2 
335  C CD1 . ILE A 50 ? 0.18517 0.27327 0.21284 0.05640  -0.02956 0.02949  96  ILE A CD1 
336  N N   . GLY A 51 ? 0.15680 0.20227 0.19655 0.04077  0.00317  0.00873  97  GLY A N   
337  C CA  . GLY A 51 ? 0.16743 0.20659 0.20422 0.05008  0.00544  -0.00368 97  GLY A CA  
338  C C   . GLY A 51 ? 0.19719 0.25831 0.22233 0.04649  0.01370  -0.00842 97  GLY A C   
339  O O   . GLY A 51 ? 0.16095 0.24083 0.18791 0.03748  0.02036  0.00145  97  GLY A O   
340  N N   . ASP A 52 ? 0.17992 0.23805 0.19352 0.05376  0.01374  -0.02380 98  ASP A N   
341  C CA  . ASP A 52 ? 0.20096 0.28376 0.19300 0.05464  0.02183  -0.02708 98  ASP A CA  
342  C C   . ASP A 52 ? 0.21664 0.29849 0.19524 0.04176  0.02174  -0.00738 98  ASP A C   
343  O O   . ASP A 52 ? 0.21405 0.27414 0.19373 0.03534  0.01139  -0.00357 98  ASP A O   
344  C CB  . ASP A 52 ? 0.21899 0.29747 0.19655 0.06432  0.01592  -0.05202 98  ASP A CB  
345  C CG  . ASP A 52 ? 0.27825 0.38553 0.22184 0.06795  0.02129  -0.05416 98  ASP A CG  
346  O OD1 . ASP A 52 ? 0.28314 0.42013 0.21701 0.07724  0.03580  -0.05881 98  ASP A OD1 
347  O OD2 . ASP A 52 ? 0.29828 0.40267 0.22434 0.06252  0.01245  -0.04691 98  ASP A OD2 
348  N N   . ALA A 53 ? 0.19415 0.29937 0.16377 0.03884  0.03542  0.00662  99  ALA A N   
349  C CA  . ALA A 53 ? 0.21085 0.30970 0.17398 0.02836  0.03771  0.02973  99  ALA A CA  
350  C C   . ALA A 53 ? 0.23620 0.32441 0.17600 0.03250  0.02438  0.02899  99  ALA A C   
351  O O   . ALA A 53 ? 0.23955 0.31041 0.18567 0.02585  0.01812  0.04149  99  ALA A O   
352  C CB  . ALA A 53 ? 0.26950 0.39325 0.22676 0.02598  0.05852  0.04825  99  ALA A CB  
353  N N   . ASN A 54 ? 0.25070 0.35361 0.16594 0.04461  0.01914  0.01151  100 ASN A N   
354  C CA  . ASN A 54 ? 0.27341 0.37575 0.17063 0.04905  0.00272  0.00685  100 ASN A CA  
355  C C   . ASN A 54 ? 0.27828 0.35509 0.20310 0.04217  -0.01270 -0.00730 100 ASN A C   
356  O O   . ASN A 54 ? 0.28486 0.35552 0.21446 0.03890  -0.02298 0.00013  100 ASN A O   
357  C CB  . ASN A 54 ? 0.30353 0.43495 0.16640 0.06423  -0.00125 -0.01474 100 ASN A CB  
358  C CG  . ASN A 54 ? 0.42653 0.58847 0.25216 0.07287  0.01590  0.00755  100 ASN A CG  
359  O OD1 . ASN A 54 ? 0.47020 0.62757 0.29351 0.06785  0.02503  0.04298  100 ASN A OD1 
360  N ND2 . ASN A 54 ? 0.52004 0.71195 0.31818 0.08633  0.02255  -0.01246 100 ASN A ND2 
361  N N   . LYS A 55 ? 0.25249 0.31462 0.19880 0.04082  -0.01225 -0.02427 101 LYS A N   
362  C CA  . LYS A 55 ? 0.23444 0.27105 0.20815 0.03372  -0.02164 -0.03286 101 LYS A CA  
363  C C   . LYS A 55 ? 0.24900 0.27047 0.23753 0.02361  -0.01848 -0.01048 101 LYS A C   
364  O O   . LYS A 55 ? 0.21875 0.23143 0.22070 0.01777  -0.02536 -0.00956 101 LYS A O   
365  C CB  . LYS A 55 ? 0.22387 0.24462 0.21576 0.03780  -0.01898 -0.04986 101 LYS A CB  
366  C CG  . LYS A 55 ? 0.26715 0.29969 0.24986 0.04818  -0.02334 -0.08075 101 LYS A CG  
367  C CD  . LYS A 55 ? 0.28144 0.29495 0.28605 0.05585  -0.01848 -0.09692 101 LYS A CD  
368  C CE  . LYS A 55 ? 0.38307 0.40753 0.38097 0.06645  -0.02355 -0.13570 101 LYS A CE  
369  N NZ  . LYS A 55 ? 0.38075 0.37782 0.40897 0.07493  -0.01981 -0.15497 101 LYS A NZ  
370  N N   . ILE A 56 ? 0.21095 0.23321 0.20075 0.02151  -0.00813 0.00400  102 ILE A N   
371  C CA  . ILE A 56 ? 0.19457 0.20464 0.19720 0.01310  -0.00647 0.01757  102 ILE A CA  
372  C C   . ILE A 56 ? 0.21556 0.22725 0.21430 0.01020  -0.00842 0.02911  102 ILE A C   
373  O O   . ILE A 56 ? 0.18958 0.19050 0.20118 0.00547  -0.00973 0.03364  102 ILE A O   
374  C CB  . ILE A 56 ? 0.17757 0.19335 0.18677 0.01099  0.00139  0.02394  102 ILE A CB  
375  C CG1 . ILE A 56 ? 0.17593 0.21028 0.18006 0.00962  0.01070  0.03159  102 ILE A CG1 
376  C CG2 . ILE A 56 ? 0.17814 0.19297 0.19399 0.01855  0.00079  0.01571  102 ILE A CG2 
377  C CD1 . ILE A 56 ? 0.16172 0.21077 0.18358 0.00615  0.01745  0.03144  102 ILE A CD1 
378  N N   . LEU A 57 ? 0.21048 0.23670 0.19073 0.01554  -0.00754 0.03556  103 LEU A N   
379  C CA  . LEU A 57 ? 0.23880 0.26503 0.21510 0.01761  -0.01088 0.05089  103 LEU A CA  
380  C C   . LEU A 57 ? 0.26609 0.29522 0.24893 0.02111  -0.02650 0.04009  103 LEU A C   
381  O O   . LEU A 57 ? 0.25331 0.27680 0.25065 0.02101  -0.03000 0.04843  103 LEU A O   
382  C CB  . LEU A 57 ? 0.26427 0.30728 0.21383 0.02546  -0.00470 0.06660  103 LEU A CB  
383  C CG  . LEU A 57 ? 0.29499 0.33860 0.23520 0.03342  -0.00859 0.08927  103 LEU A CG  
384  C CD1 . LEU A 57 ? 0.32900 0.34628 0.29806 0.02556  -0.00138 0.10453  103 LEU A CD1 
385  C CD2 . LEU A 57 ? 0.31406 0.37667 0.21984 0.04341  0.00091  0.11002  103 LEU A CD2 
386  N N   . GLN A 58 ? 0.27228 0.31229 0.25042 0.02436  -0.03595 0.01881  104 GLN A N   
387  C CA  . GLN A 58 ? 0.27140 0.31738 0.26834 0.02358  -0.05101 0.00330  104 GLN A CA  
388  C C   . GLN A 58 ? 0.25409 0.28155 0.28452 0.01304  -0.04601 0.00577  104 GLN A C   
389  O O   . GLN A 58 ? 0.22184 0.25586 0.27193 0.01277  -0.05211 0.00765  104 GLN A O   
390  C CB  . GLN A 58 ? 0.27491 0.32867 0.27225 0.02457  -0.05953 -0.02623 104 GLN A CB  
391  C CG  . GLN A 58 ? 0.28654 0.36873 0.24720 0.03797  -0.06731 -0.03577 104 GLN A CG  
392  C CD  . GLN A 58 ? 0.34994 0.43758 0.31640 0.03888  -0.07603 -0.07397 104 GLN A CD  
393  O OE1 . GLN A 58 ? 0.35353 0.42323 0.32668 0.03698  -0.06532 -0.08323 104 GLN A OE1 
394  N NE2 . GLN A 58 ? 0.35118 0.46420 0.32007 0.04268  -0.09691 -0.09864 104 GLN A NE2 
395  N N   . TYR A 59 ? 0.20002 0.20863 0.23632 0.00665  -0.03442 0.00646  105 TYR A N   
396  C CA  . TYR A 59 ? 0.19401 0.18873 0.25320 -0.00112 -0.02687 0.01095  105 TYR A CA  
397  C C   . TYR A 59 ? 0.20001 0.19437 0.26060 -0.00057 -0.02180 0.02479  105 TYR A C   
398  O O   . TYR A 59 ? 0.18108 0.17707 0.26263 -0.00291 -0.02005 0.02514  105 TYR A O   
399  C CB  . TYR A 59 ? 0.21534 0.19409 0.27131 -0.00285 -0.01711 0.01316  105 TYR A CB  
400  C CG  . TYR A 59 ? 0.19958 0.16618 0.27093 -0.00486 -0.01763 0.00176  105 TYR A CG  
401  C CD1 . TYR A 59 ? 0.17883 0.13536 0.27861 -0.01319 -0.01310 0.00198  105 TYR A CD1 
402  C CD2 . TYR A 59 ? 0.21189 0.17576 0.27424 0.00157  -0.01997 -0.00931 105 TYR A CD2 
403  C CE1 . TYR A 59 ? 0.21628 0.15421 0.33831 -0.01693 -0.01091 -0.00665 105 TYR A CE1 
404  C CE2 . TYR A 59 ? 0.20277 0.14826 0.28543 0.00074  -0.01950 -0.02160 105 TYR A CE2 
405  C CZ  . TYR A 59 ? 0.22882 0.15820 0.34269 -0.00940 -0.01489 -0.01904 105 TYR A CZ  
406  O OH  . TYR A 59 ? 0.24452 0.14869 0.38705 -0.01230 -0.01211 -0.02972 105 TYR A OH  
407  N N   . LYS A 60 ? 0.17790 0.17004 0.22198 0.00195  -0.01741 0.03448  106 LYS A N   
408  C CA  . LYS A 60 ? 0.17876 0.16465 0.23041 0.00198  -0.01217 0.04380  106 LYS A CA  
409  C C   . LYS A 60 ? 0.19144 0.18420 0.25549 0.00899  -0.01973 0.04834  106 LYS A C   
410  O O   . LYS A 60 ? 0.18222 0.17185 0.26645 0.00978  -0.01641 0.04776  106 LYS A O   
411  C CB  . LYS A 60 ? 0.20659 0.18825 0.24791 0.00105  -0.00590 0.05314  106 LYS A CB  
412  C CG  . LYS A 60 ? 0.21319 0.18184 0.26982 0.00068  -0.00041 0.06111  106 LYS A CG  
413  C CD  . LYS A 60 ? 0.25269 0.21536 0.30907 -0.00427 0.00835  0.07101  106 LYS A CD  
414  C CE  . LYS A 60 ? 0.28692 0.22898 0.36620 -0.00545 0.01483  0.07826  106 LYS A CE  
415  N NZ  . LYS A 60 ? 0.28018 0.21832 0.36206 -0.01164 0.02480  0.08799  106 LYS A NZ  
416  N N   . ASN A 61 ? 0.19509 0.20133 0.24609 0.01695  -0.03026 0.05251  107 ASN A N   
417  C CA  . ASN A 61 ? 0.20971 0.22899 0.27125 0.02805  -0.04156 0.05858  107 ASN A CA  
418  C C   . ASN A 61 ? 0.20696 0.23984 0.30028 0.02503  -0.04801 0.04266  107 ASN A C   
419  O O   . ASN A 61 ? 0.21619 0.25631 0.33424 0.03175  -0.05075 0.04577  107 ASN A O   
420  C CB  . ASN A 61 ? 0.26876 0.30854 0.30250 0.03953  -0.05423 0.06392  107 ASN A CB  
421  C CG  . ASN A 61 ? 0.29495 0.32462 0.30211 0.04449  -0.04381 0.08828  107 ASN A CG  
422  O OD1 . ASN A 61 ? 0.30850 0.31439 0.32805 0.04022  -0.03041 0.10180  107 ASN A OD1 
423  N ND2 . ASN A 61 ? 0.30175 0.35121 0.27450 0.05323  -0.04864 0.09263  107 ASN A ND2 
424  N N   . TYR A 62 ? 0.20513 0.24135 0.30381 0.01509  -0.04871 0.02606  108 TYR A N   
425  C CA  . TYR A 62 ? 0.17823 0.22655 0.31483 0.00797  -0.05056 0.01234  108 TYR A CA  
426  C C   . TYR A 62 ? 0.18447 0.22286 0.34100 0.00353  -0.03329 0.01819  108 TYR A C   
427  O O   . TYR A 62 ? 0.15137 0.20667 0.34208 0.00472  -0.03302 0.01462  108 TYR A O   
428  C CB  . TYR A 62 ? 0.20438 0.24747 0.34516 -0.00308 -0.05036 -0.00339 108 TYR A CB  
429  C CG  . TYR A 62 ? 0.23068 0.28777 0.41784 -0.01346 -0.05354 -0.01962 108 TYR A CG  
430  C CD1 . TYR A 62 ? 0.22013 0.31100 0.43189 -0.00946 -0.07335 -0.03416 108 TYR A CD1 
431  C CD2 . TYR A 62 ? 0.21419 0.25312 0.42325 -0.02713 -0.03666 -0.01937 108 TYR A CD2 
432  C CE1 . TYR A 62 ? 0.25515 0.36325 0.52113 -0.02251 -0.07602 -0.05269 108 TYR A CE1 
433  C CE2 . TYR A 62 ? 0.20660 0.25644 0.46660 -0.04020 -0.03533 -0.03218 108 TYR A CE2 
434  C CZ  . TYR A 62 ? 0.25317 0.33751 0.54357 -0.03930 -0.05459 -0.05081 108 TYR A CZ  
435  O OH  . TYR A 62 ? 0.31709 0.40648 0.64280 -0.04983 -0.04845 -0.06183 108 TYR A OH  
436  N N   . PHE A 63 ? 0.16571 0.18242 0.30196 -0.00046 -0.01900 0.02460  109 PHE A N   
437  C CA  . PHE A 63 ? 0.19019 0.20155 0.33526 -0.00226 -0.00280 0.02680  109 PHE A CA  
438  C C   . PHE A 63 ? 0.15709 0.16938 0.31167 0.00798  -0.00260 0.02965  109 PHE A C   
439  O O   . PHE A 63 ? 0.19619 0.21606 0.37280 0.01034  0.00733  0.02529  109 PHE A O   
440  C CB  . PHE A 63 ? 0.16782 0.16266 0.28499 -0.00602 0.00707  0.02998  109 PHE A CB  
441  C CG  . PHE A 63 ? 0.17232 0.16135 0.28464 -0.01254 0.00982  0.03066  109 PHE A CG  
442  C CD1 . PHE A 63 ? 0.18372 0.17768 0.32364 -0.01946 0.01394  0.02858  109 PHE A CD1 
443  C CD2 . PHE A 63 ? 0.19222 0.17032 0.27883 -0.01145 0.00943  0.03362  109 PHE A CD2 
444  C CE1 . PHE A 63 ? 0.19187 0.17241 0.33382 -0.02534 0.01851  0.03109  109 PHE A CE1 
445  C CE2 . PHE A 63 ? 0.20077 0.16918 0.28654 -0.01375 0.01227  0.03606  109 PHE A CE2 
446  C CZ  . PHE A 63 ? 0.22872 0.19433 0.34175 -0.02075 0.01745  0.03577  109 PHE A CZ  
447  N N   . GLN A 64 ? 0.16803 0.17112 0.30808 0.01499  -0.01060 0.03798  110 GLN A N   
448  C CA  . GLN A 64 ? 0.18812 0.18470 0.34333 0.02628  -0.00982 0.04369  110 GLN A CA  
449  C C   . GLN A 64 ? 0.20552 0.22547 0.39102 0.03783  -0.02036 0.04401  110 GLN A C   
450  O O   . GLN A 64 ? 0.22673 0.24788 0.43949 0.04742  -0.01531 0.04212  110 GLN A O   
451  C CB  . GLN A 64 ? 0.21443 0.19279 0.35049 0.03028  -0.01274 0.05896  110 GLN A CB  
452  C CG  . GLN A 64 ? 0.22757 0.18477 0.35229 0.02002  -0.00064 0.05511  110 GLN A CG  
453  C CD  . GLN A 64 ? 0.30807 0.24800 0.42472 0.02065  0.00101  0.07229  110 GLN A CD  
454  O OE1 . GLN A 64 ? 0.28016 0.22788 0.38076 0.02692  -0.00592 0.08837  110 GLN A OE1 
455  N NE2 . GLN A 64 ? 0.29584 0.21854 0.42121 0.01332  0.01098  0.06513  110 GLN A NE2 
456  N N   . ALA A 65 ? 0.17557 0.21768 0.35991 0.03874  -0.03638 0.04310  111 ALA A N   
457  C CA  . ALA A 65 ? 0.19438 0.26736 0.41122 0.05133  -0.05104 0.04106  111 ALA A CA  
458  C C   . ALA A 65 ? 0.16168 0.25699 0.42261 0.04369  -0.04277 0.02509  111 ALA A C   
459  O O   . ALA A 65 ? 0.18669 0.30232 0.48092 0.05479  -0.04512 0.02265  111 ALA A O   
460  C CB  . ALA A 65 ? 0.21682 0.31439 0.41924 0.05521  -0.07391 0.03880  111 ALA A CB  
461  N N   . ASN A 66 ? 0.14408 0.23493 0.40330 0.02514  -0.03052 0.01618  112 ASN A N   
462  C CA  . ASN A 66 ? 0.18032 0.29434 0.48349 0.01474  -0.01975 0.00515  112 ASN A CA  
463  C C   . ASN A 66 ? 0.14711 0.24726 0.44587 0.00700  0.00860  0.00740  112 ASN A C   
464  O O   . ASN A 66 ? 0.13451 0.25259 0.46498 -0.00151 0.02357  0.00304  112 ASN A O   
465  C CB  . ASN A 66 ? 0.16613 0.28958 0.48038 -0.00087 -0.02841 -0.00576 112 ASN A CB  
466  C CG  . ASN A 66 ? 0.18709 0.33289 0.50020 0.00786  -0.05856 -0.01444 112 ASN A CG  
467  O OD1 . ASN A 66 ? 0.14829 0.32042 0.47785 0.01833  -0.06988 -0.01831 112 ASN A OD1 
468  N ND2 . ASN A 66 ? 0.21533 0.34742 0.49245 0.00541  -0.06867 -0.01721 112 ASN A ND2 
469  N N   . GLY A 67 ? 0.17700 0.24902 0.43602 0.01066  0.01655  0.01337  113 GLY A N   
470  C CA  . GLY A 67 ? 0.18024 0.24449 0.42461 0.00588  0.03992  0.01326  113 GLY A CA  
471  C C   . GLY A 67 ? 0.21557 0.29536 0.48261 0.01525  0.05607  0.00551  113 GLY A C   
472  O O   . GLY A 67 ? 0.20280 0.28708 0.45859 0.01220  0.07764  0.00409  113 GLY A O   
473  N N   . ALA A 68 ? 0.16627 0.25534 0.46246 0.02944  0.04662  0.00106  114 ALA A N   
474  C CA  . ALA A 68 ? 0.20549 0.30848 0.52573 0.04109  0.06052  -0.00958 114 ALA A CA  
475  C C   . ALA A 68 ? 0.25795 0.34376 0.55248 0.04601  0.07751  -0.02005 114 ALA A C   
476  O O   . ALA A 68 ? 0.21820 0.31817 0.51638 0.05093  0.09483  -0.03202 114 ALA A O   
477  C CB  . ALA A 68 ? 0.15683 0.29135 0.50130 0.03279  0.07403  -0.01240 114 ALA A CB  
478  N N   . ARG A 69 ? 0.23019 0.28436 0.48545 0.04219  0.06856  -0.01766 115 ARG A N   
479  C CA  . ARG A 69 ? 0.27535 0.31331 0.50670 0.04549  0.07765  -0.03366 115 ARG A CA  
480  C C   . ARG A 69 ? 0.26668 0.27114 0.50062 0.05026  0.06363  -0.03374 115 ARG A C   
481  O O   . ARG A 69 ? 0.32632 0.31719 0.55097 0.04506  0.04867  -0.01637 115 ARG A O   
482  C CB  . ARG A 69 ? 0.28160 0.31924 0.46597 0.03386  0.08309  -0.03240 115 ARG A CB  
483  C CG  . ARG A 69 ? 0.27193 0.33694 0.44832 0.02955  0.10234  -0.02595 115 ARG A CG  
484  C CD  . ARG A 69 ? 0.26967 0.36030 0.46681 0.04016  0.12367  -0.04094 115 ARG A CD  
485  N NE  . ARG A 69 ? 0.27987 0.39900 0.47474 0.03505  0.14720  -0.02922 115 ARG A NE  
486  C CZ  . ARG A 69 ? 0.25675 0.39600 0.48883 0.03128  0.15209  -0.02176 115 ARG A CZ  
487  N NH1 . ARG A 69 ? 0.25423 0.39357 0.52875 0.03407  0.13550  -0.02476 115 ARG A NH1 
488  N NH2 . ARG A 69 ? 0.30934 0.46908 0.53317 0.02436  0.17135  -0.00957 115 ARG A NH2 
489  N N   . SER A 70 ? 0.25952 0.24999 0.50770 0.06004  0.07060  -0.05365 116 SER A N   
490  C CA  . SER A 70 ? 0.31748 0.27224 0.56849 0.05967  0.05946  -0.05003 116 SER A CA  
491  C C   . SER A 70 ? 0.30733 0.24440 0.54019 0.04988  0.06195  -0.06980 116 SER A C   
492  O O   . SER A 70 ? 0.31798 0.22827 0.55790 0.04506  0.05557  -0.06694 116 SER A O   
493  C CB  . SER A 70 ? 0.29530 0.24257 0.57276 0.07262  0.05962  -0.05445 116 SER A CB  
494  O OG  . SER A 70 ? 0.35217 0.31641 0.63357 0.07879  0.07408  -0.08160 116 SER A OG  
495  N N   . ASP A 71 ? 0.29266 0.25097 0.49923 0.04586  0.07047  -0.08884 117 ASP A N   
496  C CA  . ASP A 71 ? 0.30807 0.26161 0.49521 0.03789  0.06894  -0.11406 117 ASP A CA  
497  C C   . ASP A 71 ? 0.30612 0.27177 0.45492 0.02490  0.06003  -0.10160 117 ASP A C   
498  O O   . ASP A 71 ? 0.35191 0.33408 0.47464 0.02223  0.05900  -0.12231 117 ASP A O   
499  C CB  . ASP A 71 ? 0.30033 0.27636 0.47633 0.04659  0.08100  -0.14806 117 ASP A CB  
500  C CG  . ASP A 71 ? 0.34692 0.36207 0.49366 0.05157  0.09450  -0.13986 117 ASP A CG  
501  O OD1 . ASP A 71 ? 0.34482 0.36627 0.48687 0.04621  0.09268  -0.10728 117 ASP A OD1 
502  O OD2 . ASP A 71 ? 0.38305 0.42259 0.50928 0.05962  0.10623  -0.16326 117 ASP A OD2 
503  N N   . ILE A 72 ? 0.27030 0.23259 0.41416 0.01946  0.05277  -0.07038 118 ILE A N   
504  C CA  . ILE A 72 ? 0.29138 0.26242 0.40517 0.00985  0.04473  -0.05866 118 ILE A CA  
505  C C   . ILE A 72 ? 0.27690 0.22813 0.40218 0.00027  0.03548  -0.05343 118 ILE A C   
506  O O   . ILE A 72 ? 0.24338 0.17398 0.39033 0.00087  0.03417  -0.03724 118 ILE A O   
507  C CB  . ILE A 72 ? 0.27092 0.25183 0.37394 0.00957  0.04431  -0.03248 118 ILE A CB  
508  C CG1 . ILE A 72 ? 0.28724 0.28863 0.38802 0.01585  0.05796  -0.03365 118 ILE A CG1 
509  C CG2 . ILE A 72 ? 0.25893 0.24499 0.33481 0.00279  0.03669  -0.02180 118 ILE A CG2 
510  C CD1 . ILE A 72 ? 0.29841 0.30724 0.39763 0.01173  0.05877  -0.01157 118 ILE A CD1 
511  N N   . ASP A 73 ? 0.23795 0.19983 0.34897 -0.00743 0.02962  -0.06473 119 ASP A N   
512  C CA  . ASP A 73 ? 0.24424 0.19635 0.36837 -0.01866 0.02376  -0.05816 119 ASP A CA  
513  C C   . ASP A 73 ? 0.26322 0.22924 0.36297 -0.01938 0.01863  -0.03601 119 ASP A C   
514  O O   . ASP A 73 ? 0.22565 0.21297 0.29928 -0.01554 0.01534  -0.03861 119 ASP A O   
515  C CB  . ASP A 73 ? 0.24718 0.20817 0.38315 -0.02733 0.01921  -0.08940 119 ASP A CB  
516  C CG  . ASP A 73 ? 0.29708 0.23926 0.46378 -0.02731 0.02445  -0.11757 119 ASP A CG  
517  O OD1 . ASP A 73 ? 0.27038 0.18111 0.46481 -0.02508 0.03169  -0.10455 119 ASP A OD1 
518  O OD2 . ASP A 73 ? 0.29262 0.25380 0.45451 -0.02711 0.02031  -0.15361 119 ASP A OD2 
519  N N   . PHE A 74 ? 0.21799 0.17180 0.32472 -0.02172 0.01867  -0.01365 120 PHE A N   
520  C CA  . PHE A 74 ? 0.19151 0.15634 0.27904 -0.02111 0.01468  0.00270  120 PHE A CA  
521  C C   . PHE A 74 ? 0.23415 0.20642 0.33004 -0.02988 0.01386  0.00251  120 PHE A C   
522  O O   . PHE A 74 ? 0.23848 0.19799 0.35879 -0.03787 0.01936  0.00484  120 PHE A O   
523  C CB  . PHE A 74 ? 0.23079 0.18692 0.31630 -0.01565 0.01438  0.02261  120 PHE A CB  
524  C CG  . PHE A 74 ? 0.25993 0.21946 0.34261 -0.00857 0.01407  0.02252  120 PHE A CG  
525  C CD1 . PHE A 74 ? 0.24427 0.19675 0.34539 -0.00335 0.01765  0.01868  120 PHE A CD1 
526  C CD2 . PHE A 74 ? 0.22705 0.19662 0.29584 -0.00733 0.01188  0.02598  120 PHE A CD2 
527  C CE1 . PHE A 74 ? 0.24719 0.20973 0.35363 0.00202  0.01966  0.01784  120 PHE A CE1 
528  C CE2 . PHE A 74 ? 0.22398 0.19818 0.29978 -0.00451 0.01458  0.02629  120 PHE A CE2 
529  C CZ  . PHE A 74 ? 0.25696 0.23115 0.35201 -0.00031 0.01879  0.02207  120 PHE A CZ  
530  N N   . TYR A 75 ? 0.21009 0.20325 0.29095 -0.02795 0.00862  0.00059  121 TYR A N   
531  C CA  . TYR A 75 ? 0.21954 0.22985 0.31240 -0.03428 0.00778  -0.00166 121 TYR A CA  
532  C C   . TYR A 75 ? 0.20577 0.22357 0.28260 -0.02736 0.00781  0.01292  121 TYR A C   
533  O O   . TYR A 75 ? 0.19950 0.21793 0.25622 -0.01758 0.00330  0.01556  121 TYR A O   
534  C CB  . TYR A 75 ? 0.22124 0.25767 0.31600 -0.03409 -0.00147 -0.02319 121 TYR A CB  
535  C CG  . TYR A 75 ? 0.26086 0.29424 0.37627 -0.04244 -0.00233 -0.04685 121 TYR A CG  
536  C CD1 . TYR A 75 ? 0.26038 0.28564 0.36015 -0.03557 -0.00242 -0.05672 121 TYR A CD1 
537  C CD2 . TYR A 75 ? 0.30123 0.34138 0.45595 -0.05753 -0.00159 -0.06228 121 TYR A CD2 
538  C CE1 . TYR A 75 ? 0.26384 0.28633 0.38295 -0.04117 -0.00292 -0.08468 121 TYR A CE1 
539  C CE2 . TYR A 75 ? 0.30207 0.33640 0.48162 -0.06597 -0.00309 -0.09028 121 TYR A CE2 
540  C CZ  . TYR A 75 ? 0.33753 0.36204 0.49713 -0.05649 -0.00428 -0.10282 121 TYR A CZ  
541  O OH  . TYR A 75 ? 0.41095 0.42968 0.59588 -0.06301 -0.00542 -0.13665 121 TYR A OH  
542  N N   . LEU A 76 ? 0.17841 0.20052 0.26556 -0.03218 0.01511  0.02230  122 LEU A N   
543  C CA  . LEU A 76 ? 0.18420 0.21623 0.25600 -0.02423 0.01676  0.03090  122 LEU A CA  
544  C C   . LEU A 76 ? 0.16469 0.22597 0.25184 -0.02497 0.01823  0.02385  122 LEU A C   
545  O O   . LEU A 76 ? 0.16661 0.24036 0.28180 -0.03693 0.02532  0.02166  122 LEU A O   
546  C CB  . LEU A 76 ? 0.19227 0.21585 0.25621 -0.02428 0.02561  0.04797  122 LEU A CB  
547  C CG  . LEU A 76 ? 0.22785 0.23047 0.27849 -0.01920 0.02117  0.05580  122 LEU A CG  
548  C CD1 . LEU A 76 ? 0.23106 0.23547 0.26624 -0.01408 0.02657  0.07370  122 LEU A CD1 
549  C CD2 . LEU A 76 ? 0.21497 0.21506 0.25251 -0.01158 0.01089  0.04634  122 LEU A CD2 
550  N N   . GLN A 77 ? 0.15824 0.23064 0.23395 -0.01221 0.01223  0.01995  123 GLN A N   
551  C CA  . GLN A 77 ? 0.13156 0.23600 0.22468 -0.00785 0.01294  0.01327  123 GLN A CA  
552  C C   . GLN A 77 ? 0.15063 0.25785 0.23072 0.00364  0.01926  0.01666  123 GLN A C   
553  O O   . GLN A 77 ? 0.14192 0.23898 0.20853 0.01758  0.01236  0.01367  123 GLN A O   
554  C CB  . GLN A 77 ? 0.12499 0.24439 0.22048 0.00224  -0.00139 0.00384  123 GLN A CB  
555  C CG  . GLN A 77 ? 0.11074 0.27039 0.23177 0.00962  -0.00316 -0.00402 123 GLN A CG  
556  C CD  . GLN A 77 ? 0.12915 0.31602 0.28815 -0.00838 0.00551  -0.01101 123 GLN A CD  
557  O OE1 . GLN A 77 ? 0.17129 0.36863 0.35041 -0.02030 -0.00136 -0.02283 123 GLN A OE1 
558  N NE2 . GLN A 77 ? 0.13827 0.33706 0.30897 -0.01130 0.02248  -0.00482 123 GLN A NE2 
559  N N   . PRO A 78 ? 0.12861 0.24783 0.21164 -0.00114 0.03388  0.02274  124 PRO A N   
560  C CA  . PRO A 78 ? 0.18097 0.30894 0.24735 0.01192  0.04049  0.02028  124 PRO A CA  
561  C C   . PRO A 78 ? 0.17249 0.32834 0.25822 0.02473  0.04031  0.00778  124 PRO A C   
562  O O   . PRO A 78 ? 0.16112 0.34650 0.27881 0.01997  0.04257  0.00484  124 PRO A O   
563  C CB  . PRO A 78 ? 0.21107 0.35155 0.27331 0.00377  0.05924  0.03410  124 PRO A CB  
564  C CG  . PRO A 78 ? 0.22064 0.36531 0.31626 -0.01501 0.06549  0.04193  124 PRO A CG  
565  C CD  . PRO A 78 ? 0.17788 0.30219 0.28000 -0.01829 0.04705  0.03283  124 PRO A CD  
566  N N   . THR A 79 ? 0.16654 0.33213 0.22589 0.03147  0.02423  0.00408  125 THR A N   
567  C CA  . THR A 79 ? 0.14607 0.29848 0.22365 0.03624  0.04040  0.00169  125 THR A CA  
568  C C   . THR A 79 ? 0.18537 0.35294 0.24815 0.03840  0.05808  -0.02666 125 THR A C   
569  O O   . THR A 79 ? 0.18669 0.38396 0.22280 0.03437  0.05305  -0.04346 125 THR A O   
570  C CB  . THR A 79 ? 0.18120 0.30330 0.28057 0.03274  0.04294  -0.00067 125 THR A CB  
571  O OG1 . THR A 79 ? 0.18353 0.29573 0.27711 0.02571  0.04857  -0.03161 125 THR A OG1 
572  C CG2 . THR A 79 ? 0.16509 0.28020 0.26806 0.02732  0.02360  0.01926  125 THR A CG2 
573  N N   . LEU A 80 ? 0.19435 0.34583 0.27559 0.04438  0.08083  -0.03226 126 LEU A N   
574  C CA  . LEU A 80 ? 0.23351 0.39169 0.30197 0.04414  0.10428  -0.06711 126 LEU A CA  
575  C C   . LEU A 80 ? 0.25592 0.38326 0.33813 0.03282  0.11987  -0.10383 126 LEU A C   
576  O O   . LEU A 80 ? 0.29712 0.42506 0.36980 0.02662  0.14141  -0.14303 126 LEU A O   
577  C CB  . LEU A 80 ? 0.24962 0.40485 0.33452 0.05927  0.12892  -0.05245 126 LEU A CB  
578  C CG  . LEU A 80 ? 0.23259 0.41808 0.31329 0.07062  0.11929  -0.01529 126 LEU A CG  
579  C CD1 . LEU A 80 ? 0.25348 0.43882 0.35199 0.08619  0.14731  -0.00266 126 LEU A CD1 
580  C CD2 . LEU A 80 ? 0.24306 0.47257 0.28413 0.06879  0.10676  -0.02333 126 LEU A CD2 
581  N N   . ASN A 81 ? 0.27073 0.37234 0.37561 0.02884  0.11089  -0.09305 127 ASN A N   
582  C CA  . ASN A 81 ? 0.30126 0.37406 0.42633 0.01778  0.12587  -0.12369 127 ASN A CA  
583  C C   . ASN A 81 ? 0.30142 0.39992 0.39589 -0.00118 0.11823  -0.16822 127 ASN A C   
584  O O   . ASN A 81 ? 0.28784 0.42192 0.35355 -0.00515 0.09004  -0.16014 127 ASN A O   
585  C CB  . ASN A 81 ? 0.28894 0.34358 0.43517 0.01788  0.11124  -0.09887 127 ASN A CB  
586  C CG  . ASN A 81 ? 0.36446 0.41126 0.53757 0.03348  0.11248  -0.05313 127 ASN A CG  
587  O OD1 . ASN A 81 ? 0.34586 0.41074 0.50525 0.03554  0.08729  -0.02508 127 ASN A OD1 
588  N ND2 . ASN A 81 ? 0.39911 0.42165 0.60884 0.04227  0.14044  -0.04351 127 ASN A ND2 
589  N N   . GLN A 82 ? 0.36542 0.44382 0.46679 -0.01565 0.13432  -0.20020 128 GLN A N   
590  C CA  . GLN A 82 ? 0.37296 0.48330 0.45281 -0.03876 0.12159  -0.23607 128 GLN A CA  
591  C C   . GLN A 82 ? 0.38384 0.47315 0.49639 -0.05595 0.12368  -0.25080 128 GLN A C   
592  O O   . GLN A 82 ? 0.40093 0.52474 0.50477 -0.07550 0.11245  -0.27580 128 GLN A O   
593  C CB  . GLN A 82 ? 0.43019 0.55332 0.49289 -0.04734 0.13640  -0.26562 128 GLN A CB  
594  C CG  . GLN A 82 ? 0.42687 0.59230 0.44837 -0.03257 0.12788  -0.25124 128 GLN A CG  
595  C CD  . GLN A 82 ? 0.41392 0.64045 0.40621 -0.03293 0.09522  -0.23591 128 GLN A CD  
596  O OE1 . GLN A 82 ? 0.42472 0.67461 0.41902 -0.04869 0.07843  -0.24696 128 GLN A OE1 
597  N NE2 . GLN A 82 ? 0.38685 0.63989 0.36013 -0.01338 0.08843  -0.20274 128 GLN A NE2 
598  N N   . LYS A 83 ? 0.34741 0.39000 0.50060 -0.04774 0.13765  -0.22987 129 LYS A N   
599  C CA  . LYS A 83 ? 0.37485 0.39949 0.56502 -0.06194 0.14504  -0.23899 129 LYS A CA  
600  C C   . LYS A 83 ? 0.35121 0.38161 0.54086 -0.05584 0.12247  -0.21696 129 LYS A C   
601  O O   . LYS A 83 ? 0.34980 0.35194 0.56276 -0.04021 0.12660  -0.18349 129 LYS A O   
602  C CB  . LYS A 83 ? 0.44330 0.41980 0.68299 -0.05719 0.17887  -0.22552 129 LYS A CB  
603  C CG  . LYS A 83 ? 0.54973 0.51933 0.80341 -0.07493 0.20658  -0.26287 129 LYS A CG  
604  C CD  . LYS A 83 ? 0.59117 0.51553 0.88698 -0.06508 0.24376  -0.24318 129 LYS A CD  
605  C CE  . LYS A 83 ? 0.65416 0.57312 0.94549 -0.07660 0.26889  -0.27949 129 LYS A CE  
606  N NZ  . LYS A 83 ? 0.67045 0.56651 0.96101 -0.05452 0.28553  -0.25214 129 LYS A NZ  
607  N N   . GLY A 84 ? 0.28975 0.36214 0.45287 -0.06762 0.09853  -0.23187 130 GLY A N   
608  C CA  . GLY A 84 ? 0.25256 0.32626 0.41692 -0.06332 0.07954  -0.21250 130 GLY A CA  
609  C C   . GLY A 84 ? 0.21433 0.29313 0.35302 -0.04415 0.06068  -0.17535 130 GLY A C   
610  O O   . GLY A 84 ? 0.23445 0.32618 0.35094 -0.03473 0.05892  -0.16549 130 GLY A O   
611  N N   . VAL A 85 ? 0.18724 0.26009 0.32933 -0.03859 0.04563  -0.14728 131 VAL A N   
612  C CA  . VAL A 85 ? 0.16532 0.24079 0.28643 -0.02347 0.02836  -0.10788 131 VAL A CA  
613  C C   . VAL A 85 ? 0.19653 0.24186 0.33902 -0.01475 0.03085  -0.08204 131 VAL A C   
614  O O   . VAL A 85 ? 0.19933 0.22847 0.37059 -0.01892 0.04166  -0.08907 131 VAL A O   
615  C CB  . VAL A 85 ? 0.19711 0.31011 0.28822 -0.02527 0.00629  -0.09954 131 VAL A CB  
616  C CG1 . VAL A 85 ? 0.16926 0.33087 0.24099 -0.03563 0.00350  -0.12598 131 VAL A CG1 
617  C CG2 . VAL A 85 ? 0.20607 0.31639 0.30723 -0.02889 -0.00083 -0.09335 131 VAL A CG2 
618  N N   . VAL A 86 ? 0.14366 0.18610 0.27334 -0.00357 0.02192  -0.05236 132 VAL A N   
619  C CA  . VAL A 86 ? 0.14076 0.16937 0.27832 0.00410  0.01981  -0.02691 132 VAL A CA  
620  C C   . VAL A 86 ? 0.14882 0.18486 0.25764 0.00278  0.00190  -0.01805 132 VAL A C   
621  O O   . VAL A 86 ? 0.14299 0.19144 0.22990 0.00178  -0.00753 -0.01596 132 VAL A O   
622  C CB  . VAL A 86 ? 0.15351 0.18240 0.29895 0.01405  0.02373  -0.00276 132 VAL A CB  
623  C CG1 . VAL A 86 ? 0.15420 0.18560 0.29546 0.01960  0.01618  0.02260  132 VAL A CG1 
624  C CG2 . VAL A 86 ? 0.17774 0.19554 0.36172 0.01980  0.04922  -0.00444 132 VAL A CG2 
625  N N   . MET A 87 ? 0.12363 0.15082 0.23700 0.00406  0.00160  -0.01141 133 MET A N   
626  C CA  . MET A 87 ? 0.12528 0.15334 0.21540 0.00461  -0.00861 -0.00259 133 MET A CA  
627  C C   . MET A 87 ? 0.15175 0.16902 0.23480 0.01054  -0.00832 0.01476  133 MET A C   
628  O O   . MET A 87 ? 0.15245 0.16583 0.25456 0.01618  0.00017  0.02350  133 MET A O   
629  C CB  . MET A 87 ? 0.11328 0.14919 0.21129 0.00060  -0.00878 -0.01045 133 MET A CB  
630  C CG  . MET A 87 ? 0.15624 0.18842 0.24103 0.00504  -0.01155 0.00352  133 MET A CG  
631  S SD  . MET A 87 ? 0.17769 0.22445 0.28562 0.00159  -0.00947 0.00112  133 MET A SD  
632  C CE  . MET A 87 ? 0.23089 0.26403 0.32215 0.01268  -0.00581 0.02422  133 MET A CE  
633  N N   . ILE A 88 ? 0.15525 0.17115 0.21311 0.00866  -0.01523 0.01938  134 ILE A N   
634  C CA  . ILE A 88 ? 0.16649 0.18014 0.20885 0.00970  -0.01621 0.02855  134 ILE A CA  
635  C C   . ILE A 88 ? 0.19330 0.19113 0.21631 0.00861  -0.01356 0.02537  134 ILE A C   
636  O O   . ILE A 88 ? 0.20493 0.19584 0.22042 0.00455  -0.01323 0.02059  134 ILE A O   
637  C CB  . ILE A 88 ? 0.15486 0.18279 0.18718 0.00343  -0.02361 0.03112  134 ILE A CB  
638  C CG1 . ILE A 88 ? 0.16942 0.21360 0.22713 0.00826  -0.02152 0.04006  134 ILE A CG1 
639  C CG2 . ILE A 88 ? 0.19961 0.23861 0.21191 0.00097  -0.02624 0.03630  134 ILE A CG2 
640  C CD1 . ILE A 88 ? 0.21213 0.27720 0.26748 0.00213  -0.02928 0.04570  134 ILE A CD1 
641  N N   . ALA A 89 ? 0.19164 0.18374 0.21137 0.01465  -0.00738 0.03161  135 ALA A N   
642  C CA  . ALA A 89 ? 0.21432 0.18853 0.21921 0.01657  0.00081  0.03063  135 ALA A CA  
643  C C   . ALA A 89 ? 0.26270 0.23544 0.23971 0.01499  0.00416  0.02880  135 ALA A C   
644  O O   . ALA A 89 ? 0.24011 0.23279 0.21715 0.01954  0.00194  0.03847  135 ALA A O   
645  C CB  . ALA A 89 ? 0.19827 0.17116 0.22473 0.02517  0.00752  0.03915  135 ALA A CB  
646  N N   . SER A 90 ? 0.25693 0.20930 0.21209 0.00879  0.01250  0.01691  136 SER A N   
647  C CA  . SER A 90 ? 0.30000 0.25441 0.22210 0.00149  0.01620  0.00510  136 SER A CA  
648  C C   . SER A 90 ? 0.31056 0.22921 0.21817 0.00169  0.03741  -0.00573 136 SER A C   
649  O O   . SER A 90 ? 0.32275 0.21711 0.24772 0.00383  0.04795  -0.00387 136 SER A O   
650  C CB  . SER A 90 ? 0.30899 0.28002 0.21901 -0.01717 0.00452  -0.01025 136 SER A CB  
651  O OG  . SER A 90 ? 0.36864 0.35287 0.24377 -0.02855 0.00620  -0.02653 136 SER A OG  
652  N N   . ASN A 91 ? 0.33131 0.25019 0.20856 0.00131  0.04685  -0.01438 137 ASN A N   
653  C CA  . ASN A 91 ? 0.39559 0.27536 0.25753 0.00079  0.07320  -0.02890 137 ASN A CA  
654  C C   . ASN A 91 ? 0.47925 0.34843 0.31140 -0.02359 0.08004  -0.06576 137 ASN A C   
655  O O   . ASN A 91 ? 0.53858 0.37686 0.34966 -0.02759 0.10562  -0.08634 137 ASN A O   
656  C CB  . ASN A 91 ? 0.40190 0.28175 0.25067 0.01739  0.08694  -0.01718 137 ASN A CB  
657  C CG  . ASN A 91 ? 0.43391 0.35573 0.24938 0.01503  0.07675  -0.02003 137 ASN A CG  
658  O OD1 . ASN A 91 ? 0.37160 0.33012 0.17880 0.00238  0.05619  -0.02550 137 ASN A OD1 
659  N ND2 . ASN A 91 ? 0.44949 0.37234 0.24653 0.02877  0.09294  -0.01263 137 ASN A ND2 
660  N N   . TYR A 92 ? 0.47520 0.36973 0.30777 -0.04141 0.05991  -0.07632 138 TYR A N   
661  C CA  . TYR A 92 ? 0.53356 0.41913 0.34924 -0.07018 0.06553  -0.11408 138 TYR A CA  
662  C C   . TYR A 92 ? 0.56597 0.46047 0.41148 -0.08078 0.05018  -0.11041 138 TYR A C   
663  O O   . TYR A 92 ? 0.53037 0.43005 0.40554 -0.06384 0.04046  -0.08105 138 TYR A O   
664  C CB  . TYR A 92 ? 0.55185 0.48422 0.32242 -0.08676 0.05406  -0.13592 138 TYR A CB  
665  C CG  . TYR A 92 ? 0.54949 0.55058 0.32225 -0.08266 0.02179  -0.11069 138 TYR A CG  
666  C CD1 . TYR A 92 ? 0.55832 0.59370 0.34219 -0.10168 0.00107  -0.11566 138 TYR A CD1 
667  C CD2 . TYR A 92 ? 0.50500 0.53556 0.27735 -0.05743 0.01629  -0.07701 138 TYR A CD2 
668  C CE1 . TYR A 92 ? 0.54516 0.64430 0.33766 -0.09427 -0.02331 -0.08637 138 TYR A CE1 
669  C CE2 . TYR A 92 ? 0.44904 0.53882 0.23315 -0.05005 -0.00538 -0.04842 138 TYR A CE2 
670  C CZ  . TYR A 92 ? 0.51994 0.64446 0.31354 -0.06757 -0.02461 -0.05220 138 TYR A CZ  
671  O OH  . TYR A 92 ? 0.51004 0.69286 0.32291 -0.05650 -0.04084 -0.01806 138 TYR A OH  
672  N N   . LYS B 11 ? 1.15250 0.73009 1.18346 -0.26444 -0.10918 -0.22739 57  LYS B N   
673  C CA  . LYS B 11 ? 1.13904 0.69827 1.19814 -0.27645 -0.08846 -0.18040 57  LYS B CA  
674  C C   . LYS B 11 ? 1.02716 0.66422 1.11333 -0.24904 -0.07772 -0.15285 57  LYS B C   
675  O O   . LYS B 11 ? 0.97991 0.69963 1.07737 -0.22257 -0.09673 -0.16699 57  LYS B O   
676  C CB  . LYS B 11 ? 1.25795 0.70242 1.27807 -0.25636 -0.07599 -0.15633 57  LYS B CB  
677  C CG  . LYS B 11 ? 1.28744 0.73596 1.31974 -0.19757 -0.03021 -0.18280 57  LYS B CG  
678  C CD  . LYS B 11 ? 1.38162 0.74873 1.43755 -0.17353 -0.04761 -0.16182 57  LYS B CD  
679  C CE  . LYS B 11 ? 1.42637 0.73819 1.48989 -0.20847 -0.08168 -0.18958 57  LYS B CE  
680  N NZ  . LYS B 11 ? 1.53586 0.75474 1.58709 -0.20725 -0.06477 -0.17323 57  LYS B NZ  
681  N N   . ASP B 12 ? 0.93933 0.55731 1.03855 -0.24781 -0.05287 -0.10764 58  ASP B N   
682  C CA  . ASP B 12 ? 0.78831 0.49269 0.92373 -0.22693 -0.04008 -0.07880 58  ASP B CA  
683  C C   . ASP B 12 ? 0.71327 0.43065 0.82694 -0.16988 -0.05014 -0.08393 58  ASP B C   
684  O O   . ASP B 12 ? 0.75083 0.38754 0.80257 -0.13514 -0.04729 -0.08922 58  ASP B O   
685  C CB  . ASP B 12 ? 0.79223 0.47067 0.92980 -0.22598 -0.00718 -0.02820 58  ASP B CB  
686  C CG  . ASP B 12 ? 0.93751 0.56963 1.08916 -0.26674 -0.00234 -0.01897 58  ASP B CG  
687  O OD1 . ASP B 12 ? 0.96081 0.65205 1.15605 -0.30547 -0.00962 -0.02316 58  ASP B OD1 
688  O OD2 . ASP B 12 ? 1.04285 0.58664 1.16691 -0.25571 0.00823  -0.00580 58  ASP B OD2 
689  N N   . THR B 13 ? 0.53142 0.35818 0.68976 -0.15588 -0.06257 -0.07854 59  THR B N   
690  C CA  . THR B 13 ? 0.44234 0.30628 0.56894 -0.09327 -0.07010 -0.07201 59  THR B CA  
691  C C   . THR B 13 ? 0.44997 0.26265 0.53618 -0.05411 -0.03915 -0.03040 59  THR B C   
692  O O   . THR B 13 ? 0.38881 0.22443 0.50327 -0.06682 -0.01423 0.00293  59  THR B O   
693  C CB  . THR B 13 ? 0.33238 0.33490 0.51903 -0.09005 -0.08012 -0.06848 59  THR B CB  
694  O OG1 . THR B 13 ? 0.30792 0.35637 0.49902 -0.11285 -0.09886 -0.09493 59  THR B OG1 
695  C CG2 . THR B 13 ? 0.28515 0.33068 0.44956 -0.02465 -0.08174 -0.05738 59  THR B CG2 
696  N N   . PRO B 14 ? 0.44178 0.18737 0.46221 -0.00558 -0.03928 -0.03053 60  PRO B N   
697  C CA  . PRO B 14 ? 0.48902 0.22652 0.48362 0.03351  -0.00673 0.00873  60  PRO B CA  
698  C C   . PRO B 14 ? 0.36452 0.20434 0.37427 0.05815  -0.00932 0.02412  60  PRO B C   
699  O O   . PRO B 14 ? 0.29025 0.21150 0.32835 0.06865  -0.01298 0.01594  60  PRO B O   
700  C CB  . PRO B 14 ? 0.46428 0.21336 0.43391 0.05671  -0.00817 -0.00068 60  PRO B CB  
701  C CG  . PRO B 14 ? 0.48199 0.16798 0.41959 0.04376  -0.02887 -0.03802 60  PRO B CG  
702  C CD  . PRO B 14 ? 0.48160 0.18936 0.45647 0.01443  -0.06148 -0.06483 60  PRO B CD  
703  N N   . PHE B 15 ? 0.30940 0.18031 0.32891 0.05042  0.00571  0.04530  61  PHE B N   
704  C CA  . PHE B 15 ? 0.27671 0.24600 0.32099 0.05046  0.01553  0.04609  61  PHE B CA  
705  C C   . PHE B 15 ? 0.29374 0.28094 0.31354 0.05608  0.04756  0.05836  61  PHE B C   
706  O O   . PHE B 15 ? 0.31162 0.25842 0.31578 0.06421  0.05747  0.06565  61  PHE B O   
707  C CB  . PHE B 15 ? 0.26297 0.28722 0.38597 0.03123  0.02683  0.07183  61  PHE B CB  
708  C CG  . PHE B 15 ? 0.25661 0.25478 0.39437 0.01509  0.04865  0.09743  61  PHE B CG  
709  C CD1 . PHE B 15 ? 0.27575 0.30661 0.39994 0.03744  0.06096  0.09689  61  PHE B CD1 
710  C CD2 . PHE B 15 ? 0.32939 0.27560 0.47699 -0.03617 0.05114  0.09594  61  PHE B CD2 
711  C CE1 . PHE B 15 ? 0.30266 0.30158 0.41428 0.02424  0.07172  0.11126  61  PHE B CE1 
712  C CE2 . PHE B 15 ? 0.35219 0.27424 0.48266 -0.05429 0.06796  0.10799  61  PHE B CE2 
713  C CZ  . PHE B 15 ? 0.36266 0.30892 0.47297 -0.02161 0.07847  0.12043  61  PHE B CZ  
714  N N   . MET B 16 ? 0.15002 0.34968 0.29830 -0.03641 -0.00491 0.03854  62  MET B N   
715  C CA  . MET B 16 ? 0.17229 0.31395 0.31107 -0.02629 -0.01184 0.04852  62  MET B CA  
716  C C   . MET B 16 ? 0.16417 0.30356 0.27349 -0.02031 0.00463  0.08262  62  MET B C   
717  O O   . MET B 16 ? 0.17218 0.34580 0.27511 -0.01622 0.02209  0.09322  62  MET B O   
718  C CB  . MET B 16 ? 0.17886 0.32614 0.34483 -0.01887 -0.01506 0.01930  62  MET B CB  
719  C CG  . MET B 16 ? 0.20798 0.34824 0.41190 -0.01691 -0.03717 -0.02124 62  MET B CG  
720  S SD  . MET B 16 ? 0.27646 0.44615 0.53022 -0.00973 -0.03546 -0.06751 62  MET B SD  
721  C CE  . MET B 16 ? 0.28097 0.38746 0.52824 0.01360  -0.06638 -0.06208 62  MET B CE  
722  N N   . VAL B 17 ? 0.20837 0.30389 0.29449 -0.01846 0.00081  0.10052  63  VAL B N   
723  C CA  . VAL B 17 ? 0.20895 0.30287 0.27295 -0.01186 0.01637  0.12516  63  VAL B CA  
724  C C   . VAL B 17 ? 0.22924 0.27628 0.27743 -0.00049 0.00680  0.12218  63  VAL B C   
725  O O   . VAL B 17 ? 0.26294 0.26498 0.28673 0.00185  -0.01051 0.12189  63  VAL B O   
726  C CB  . VAL B 17 ? 0.22979 0.32691 0.28037 -0.01945 0.02352  0.13131  63  VAL B CB  
727  C CG1 . VAL B 17 ? 0.22995 0.31787 0.26514 -0.00677 0.03171  0.12771  63  VAL B CG1 
728  C CG2 . VAL B 17 ? 0.20629 0.36516 0.28145 -0.02761 0.02770  0.12769  63  VAL B CG2 
729  N N   . GLN B 18 ? 0.21367 0.26726 0.27082 0.00765  0.01847  0.12055  64  GLN B N   
730  C CA  . GLN B 18 ? 0.24248 0.26545 0.29306 0.01861  0.00907  0.10779  64  GLN B CA  
731  C C   . GLN B 18 ? 0.25264 0.27153 0.28280 0.02315  0.02763  0.12535  64  GLN B C   
732  O O   . GLN B 18 ? 0.23958 0.27851 0.28521 0.02337  0.04576  0.12413  64  GLN B O   
733  C CB  . GLN B 18 ? 0.23510 0.27018 0.33027 0.01929  0.01152  0.07759  64  GLN B CB  
734  C CG  . GLN B 18 ? 0.27723 0.29530 0.38014 0.02978  0.00245  0.05352  64  GLN B CG  
735  C CD  . GLN B 18 ? 0.23827 0.27572 0.40219 0.02300  0.01226  0.01528  64  GLN B CD  
736  O OE1 . GLN B 18 ? 0.24821 0.29930 0.44519 0.02709  -0.01042 -0.02073 64  GLN B OE1 
737  N NE2 . GLN B 18 ? 0.24344 0.27990 0.42709 0.01232  0.04860  0.02073  64  GLN B NE2 
738  N N   . VAL B 19 ? 0.25706 0.24813 0.24797 0.02880  0.01807  0.12601  65  VAL B N   
739  C CA  . VAL B 19 ? 0.28388 0.27668 0.25881 0.03200  0.03516  0.12770  65  VAL B CA  
740  C C   . VAL B 19 ? 0.33882 0.30814 0.29410 0.04702  0.02250  0.10957  65  VAL B C   
741  O O   . VAL B 19 ? 0.32235 0.26762 0.24944 0.05572  -0.00735 0.09732  65  VAL B O   
742  C CB  . VAL B 19 ? 0.29743 0.29047 0.24384 0.01863  0.04069  0.12819  65  VAL B CB  
743  C CG1 . VAL B 19 ? 0.26256 0.29086 0.24215 0.01088  0.04751  0.12592  65  VAL B CG1 
744  C CG2 . VAL B 19 ? 0.36966 0.31909 0.26647 0.01164  0.02437  0.13235  65  VAL B CG2 
745  N N   . LYS B 20 ? 0.33042 0.30753 0.30222 0.05261  0.04058  0.09884  66  LYS B N   
746  C CA  . LYS B 20 ? 0.38948 0.35593 0.34890 0.06502  0.02860  0.06592  66  LYS B CA  
747  C C   . LYS B 20 ? 0.47174 0.43209 0.36736 0.06871  0.03738  0.07622  66  LYS B C   
748  O O   . LYS B 20 ? 0.41549 0.39291 0.31987 0.06406  0.06709  0.09050  66  LYS B O   
749  C CB  . LYS B 20 ? 0.37243 0.34569 0.39463 0.06543  0.04763  0.03995  66  LYS B CB  
750  C CG  . LYS B 20 ? 0.38105 0.35778 0.46368 0.05469  0.05200  0.02957  66  LYS B CG  
751  C CD  . LYS B 20 ? 0.42353 0.38858 0.56147 0.04937  0.08486  0.01523  66  LYS B CD  
752  C CE  . LYS B 20 ? 0.46959 0.43350 0.66377 0.03180  0.09914  0.00045  66  LYS B CE  
753  N NZ  . LYS B 20 ? 0.44373 0.43165 0.63713 0.02868  0.07022  -0.01143 66  LYS B NZ  
754  N N   . LEU B 21 ? 0.48331 0.42008 0.31069 0.07943  0.01129  0.06833  67  LEU B N   
755  C CA  . LEU B 21 ? 0.56789 0.49057 0.31255 0.08008  0.02279  0.08126  67  LEU B CA  
756  C C   . LEU B 21 ? 0.62373 0.54978 0.33623 0.10063  0.00697  0.04053  67  LEU B C   
757  O O   . LEU B 21 ? 0.60732 0.53759 0.34579 0.11682  -0.02738 0.00415  67  LEU B O   
758  C CB  . LEU B 21 ? 0.61266 0.48883 0.27712 0.07700  0.00826  0.11489  67  LEU B CB  
759  C CG  . LEU B 21 ? 0.53935 0.42481 0.25768 0.04541  0.02067  0.13745  67  LEU B CG  
760  C CD1 . LEU B 21 ? 0.56460 0.41795 0.25478 0.03506  0.00190  0.15298  67  LEU B CD1 
761  C CD2 . LEU B 21 ? 0.58380 0.50782 0.34082 0.02085  0.05803  0.14061  67  LEU B CD2 
762  N N   . PRO B 22 ? 0.65487 0.58826 0.31770 0.09990  0.03194  0.03762  68  PRO B N   
763  C CA  . PRO B 22 ? 0.71538 0.65928 0.34214 0.12026  0.01709  -0.00811 68  PRO B CA  
764  C C   . PRO B 22 ? 0.86129 0.77003 0.36671 0.14079  -0.01962 -0.00240 68  PRO B C   
765  O O   . PRO B 22 ? 0.84720 0.71388 0.31019 0.14301  -0.04114 0.03386  68  PRO B O   
766  C CB  . PRO B 22 ? 0.74050 0.71002 0.36210 0.11044  0.06434  -0.01277 68  PRO B CB  
767  C CG  . PRO B 22 ? 0.74694 0.70544 0.34084 0.08709  0.09493  0.03955  68  PRO B CG  
768  C CD  . PRO B 22 ? 0.66570 0.61214 0.31900 0.07959  0.07819  0.06526  68  PRO B CD  
769  N N   . ASN B 23 ? 0.95667 0.87964 0.40321 0.16003  -0.02976 -0.04059 69  ASN B N   
770  C CA  . ASN B 23 ? 1.01251 0.90332 0.34800 0.17424  -0.05754 -0.02613 69  ASN B CA  
771  C C   . ASN B 23 ? 1.05614 0.91299 0.34930 0.13812  -0.01824 0.03704  69  ASN B C   
772  O O   . ASN B 23 ? 1.04965 0.92620 0.36702 0.10999  0.03239  0.04892  69  ASN B O   
773  C CB  . ASN B 23 ? 1.06787 0.99252 0.36430 0.18904  -0.06199 -0.07576 69  ASN B CB  
774  C CG  . ASN B 23 ? 1.11413 1.07325 0.45974 0.22139  -0.11672 -0.14264 69  ASN B CG  
775  O OD1 . ASN B 23 ? 1.12331 1.07404 0.50895 0.23598  -0.15807 -0.14510 69  ASN B OD1 
776  N ND2 . ASN B 23 ? 1.14216 1.14636 0.50101 0.22891  -0.11516 -0.20201 69  ASN B ND2 
777  N N   . TYR B 24 ? 1.11486 0.75236 0.44000 0.10527  0.28309  0.04761  70  TYR B N   
778  C CA  . TYR B 24 ? 1.06805 0.70753 0.40945 0.11798  0.28426  0.05489  70  TYR B CA  
779  C C   . TYR B 24 ? 1.11986 0.74467 0.45127 0.12415  0.29202  0.05236  70  TYR B C   
780  O O   . TYR B 24 ? 1.08611 0.69624 0.42861 0.13637  0.29517  0.05691  70  TYR B O   
781  C CB  . TYR B 24 ? 1.05710 0.72963 0.40689 0.11563  0.27887  0.06033  70  TYR B CB  
782  C CG  . TYR B 24 ? 1.03929 0.71555 0.40366 0.12775  0.27989  0.06783  70  TYR B CG  
783  C CD1 . TYR B 24 ? 1.01796 0.68213 0.40235 0.14005  0.27874  0.07418  70  TYR B CD1 
784  C CD2 . TYR B 24 ? 1.05292 0.74463 0.41071 0.12701  0.28205  0.06864  70  TYR B CD2 
785  C CE1 . TYR B 24 ? 1.00686 0.67445 0.40450 0.15129  0.27936  0.08136  70  TYR B CE1 
786  C CE2 . TYR B 24 ? 1.03848 0.73417 0.40944 0.13776  0.28284  0.07600  70  TYR B CE2 
787  C CZ  . TYR B 24 ? 1.01725 0.70066 0.40808 0.14994  0.28141  0.08240  70  TYR B CZ  
788  O OH  . TYR B 24 ? 1.00662 0.69430 0.41048 0.16069  0.28190  0.08997  70  TYR B OH  
789  N N   . LYS B 25 ? 1.15543 0.78464 0.46552 0.11593  0.29510  0.04505  71  LYS B N   
790  C CA  . LYS B 25 ? 1.17271 0.79062 0.47083 0.12091  0.30264  0.04138  71  LYS B CA  
791  C C   . LYS B 25 ? 1.18733 0.77050 0.48443 0.12892  0.30810  0.03950  71  LYS B C   
792  O O   . LYS B 25 ? 1.14385 0.71714 0.44708 0.14007  0.31272  0.04304  71  LYS B O   
793  C CB  . LYS B 25 ? 1.19077 0.81765 0.46448 0.10968  0.30433  0.03227  71  LYS B CB  
794  C CG  . LYS B 25 ? 1.25818 0.88237 0.51884 0.11386  0.31149  0.02814  71  LYS B CG  
795  C CD  . LYS B 25 ? 1.26945 0.86151 0.51447 0.11605  0.31783  0.01989  71  LYS B CD  
796  C CE  . LYS B 25 ? 1.28405 0.87406 0.51792 0.12206  0.32523  0.01607  71  LYS B CE  
797  N NZ  . LYS B 25 ? 1.33730 0.93380 0.58927 0.13404  0.32712  0.02540  71  LYS B NZ  
798  N N   . ASP B 26 ? 1.20703 0.77180 0.49564 0.12296  0.30764  0.03421  72  ASP B N   
799  C CA  . ASP B 26 ? 1.21560 0.74657 0.50205 0.12948  0.31262  0.03254  72  ASP B CA  
800  C C   . ASP B 26 ? 1.18877 0.71080 0.49907 0.14086  0.31125  0.04190  72  ASP B C   
801  O O   . ASP B 26 ? 1.19220 0.69262 0.50567 0.15078  0.31623  0.04410  72  ASP B O   
802  C CB  . ASP B 26 ? 1.27541 0.78989 0.54720 0.11935  0.31171  0.02522  72  ASP B CB  
803  C CG  . ASP B 26 ? 1.31516 0.83950 0.56343 0.10750  0.31183  0.01607  72  ASP B CG  
804  O OD1 . ASP B 26 ? 1.29940 0.81551 0.53174 0.10930  0.31763  0.01003  72  ASP B OD1 
805  O OD2 . ASP B 26 ? 1.31472 0.85546 0.56031 0.09667  0.30601  0.01495  72  ASP B OD2 
806  N N   . TYR B 27 ? 1.14324 0.68207 0.47016 0.13973  0.30437  0.04748  73  TYR B N   
807  C CA  . TYR B 27 ? 1.12899 0.66135 0.47897 0.15066  0.30220  0.05601  73  TYR B CA  
808  C C   . TYR B 27 ? 1.08917 0.62002 0.44891 0.16371  0.30586  0.06228  73  TYR B C   
809  O O   . TYR B 27 ? 1.08784 0.59888 0.45811 0.17408  0.30809  0.06696  73  TYR B O   
810  C CB  . TYR B 27 ? 1.05336 0.61024 0.41792 0.14732  0.29408  0.06025  73  TYR B CB  
811  C CG  . TYR B 27 ? 1.02538 0.58648 0.41443 0.15951  0.29094  0.06955  73  TYR B CG  
812  C CD1 . TYR B 27 ? 1.01027 0.55317 0.41286 0.16664  0.28998  0.07292  73  TYR B CD1 
813  C CD2 . TYR B 27 ? 1.01436 0.59812 0.41272 0.16371  0.28862  0.07497  73  TYR B CD2 
814  C CE1 . TYR B 27 ? 0.98523 0.53227 0.40986 0.17819  0.28681  0.08098  73  TYR B CE1 
815  C CE2 . TYR B 27 ? 0.98969 0.57704 0.40983 0.17505  0.28541  0.08320  73  TYR B CE2 
816  C CZ  . TYR B 27 ? 0.97528 0.54431 0.40846 0.18252  0.28450  0.08596  73  TYR B CZ  
817  O OH  . TYR B 27 ? 0.95135 0.52438 0.40586 0.19424  0.28115  0.09367  73  TYR B OH  
818  N N   . LEU B 28 ? 1.10722 0.65971 0.46354 0.16312  0.30643  0.06289  74  LEU B N   
819  C CA  . LEU B 28 ? 1.09390 0.64769 0.45915 0.17493  0.30978  0.06917  74  LEU B CA  
820  C C   . LEU B 28 ? 1.15053 0.67875 0.50598 0.18103  0.31774  0.06669  74  LEU B C   
821  O O   . LEU B 28 ? 1.13384 0.65531 0.50002 0.19277  0.32050  0.07325  74  LEU B O   
822  C CB  . LEU B 28 ? 1.12176 0.70440 0.48258 0.17145  0.30923  0.06963  74  LEU B CB  
823  C CG  . LEU B 28 ? 1.07131 0.68102 0.44432 0.16758  0.30138  0.07439  74  LEU B CG  
824  C CD1 . LEU B 28 ? 1.06843 0.70534 0.43171 0.16087  0.30131  0.07331  74  LEU B CD1 
825  C CD2 . LEU B 28 ? 1.03047 0.64066 0.42799 0.17978  0.29797  0.08437  74  LEU B CD2 
826  N N   . LEU B 29 ? 1.15772 0.67157 0.49278 0.17340  0.32133  0.05749  75  LEU B N   
827  C CA  . LEU B 29 ? 1.20096 0.69009 0.52478 0.17872  0.32893  0.05435  75  LEU B CA  
828  C C   . LEU B 29 ? 1.18162 0.64155 0.51274 0.18390  0.32964  0.05739  75  LEU B C   
829  O O   . LEU B 29 ? 1.15136 0.58983 0.47567 0.18965  0.33574  0.05670  75  LEU B O   
830  C CB  . LEU B 29 ? 1.21087 0.69627 0.50832 0.16887  0.33256  0.04253  75  LEU B CB  
831  C CG  . LEU B 29 ? 1.22232 0.73573 0.50876 0.16225  0.33232  0.03815  75  LEU B CG  
832  C CD1 . LEU B 29 ? 1.23457 0.73975 0.49435 0.15368  0.33600  0.02582  75  LEU B CD1 
833  C CD2 . LEU B 29 ? 1.23806 0.76543 0.53122 0.17171  0.33578  0.04356  75  LEU B CD2 
834  N N   . ASP B 30 ? 1.15830 0.61793 0.50253 0.18177  0.32360  0.06068  76  ASP B N   
835  C CA  . ASP B 30 ? 1.14697 0.58135 0.49984 0.18614  0.32347  0.06428  76  ASP B CA  
836  C C   . ASP B 30 ? 1.11913 0.55773 0.49671 0.19842  0.32078  0.07524  76  ASP B C   
837  O O   . ASP B 30 ? 1.10027 0.55245 0.49308 0.19835  0.31434  0.07875  76  ASP B O   
838  C CB  . ASP B 30 ? 1.14217 0.57457 0.49244 0.17545  0.31864  0.05993  76  ASP B CB  
839  C CG  . ASP B 30 ? 1.13765 0.54245 0.49280 0.17814  0.31931  0.06228  76  ASP B CG  
840  O OD1 . ASP B 30 ? 1.12566 0.51867 0.49490 0.18954  0.32070  0.07026  76  ASP B OD1 
841  O OD2 . ASP B 30 ? 1.17658 0.57204 0.52128 0.16840  0.31820  0.05646  76  ASP B OD2 
842  N N   . ASN B 31 ? 0.77414 0.57915 0.73817 0.21469  0.42707  0.21947  77  ASN B N   
843  C CA  . ASN B 31 ? 0.73546 0.62564 0.78356 0.20864  0.41274  0.24798  77  ASN B CA  
844  C C   . ASN B 31 ? 0.65106 0.60571 0.74691 0.19769  0.37998  0.26139  77  ASN B C   
845  O O   . ASN B 31 ? 0.60901 0.61691 0.73469 0.16880  0.35042  0.26047  77  ASN B O   
846  C CB  . ASN B 31 ? 0.75654 0.67355 0.88000 0.23712  0.45008  0.28970  77  ASN B CB  
847  C CG  . ASN B 31 ? 0.72969 0.70894 0.92229 0.22037  0.44666  0.30399  77  ASN B CG  
848  O OD1 . ASN B 31 ? 0.73637 0.77853 0.97365 0.19192  0.41425  0.30363  77  ASN B OD1 
849  N ND2 . ASN B 31 ? 0.78759 0.74399 0.99021 0.23579  0.48411  0.31660  77  ASN B ND2 
850  N N   . LYS B 32 ? 0.66609 0.61078 0.76454 0.22109  0.38755  0.27620  78  LYS B N   
851  C CA  . LYS B 32 ? 0.62843 0.63890 0.76624 0.21787  0.35821  0.29631  78  LYS B CA  
852  C C   . LYS B 32 ? 0.58218 0.56846 0.65431 0.17742  0.31979  0.25687  78  LYS B C   
853  O O   . LYS B 32 ? 0.52185 0.57008 0.62521 0.15353  0.28589  0.26780  78  LYS B O   
854  C CB  . LYS B 32 ? 0.66701 0.65553 0.80368 0.26092  0.38104  0.32420  78  LYS B CB  
855  C CG  . LYS B 32 ? 0.68248 0.77615 0.88686 0.27897  0.35743  0.36843  78  LYS B CG  
856  C CD  . LYS B 32 ? 0.72001 0.80147 0.92978 0.33285  0.38549  0.41028  78  LYS B CD  
857  C CE  . LYS B 32 ? 0.80032 0.79932 0.92324 0.34179  0.39908  0.39850  78  LYS B CE  
858  N NZ  . LYS B 32 ? 0.86448 0.90357 0.97857 0.32305  0.33198  0.38763  78  LYS B NZ  
859  N N   . GLN B 33 ? 0.67434 0.57586 0.65948 0.16536  0.32287  0.21171  79  GLN B N   
860  C CA  . GLN B 33 ? 0.64360 0.52614 0.57127 0.12883  0.28650  0.17457  79  GLN B CA  
861  C C   . GLN B 33 ? 0.64479 0.56419 0.57991 0.10159  0.26169  0.16865  79  GLN B C   
862  O O   . GLN B 33 ? 0.57153 0.50915 0.49850 0.07517  0.22759  0.16175  79  GLN B O   
863  C CB  . GLN B 33 ? 0.71734 0.52275 0.57064 0.12114  0.29787  0.13181  79  GLN B CB  
864  C CG  . GLN B 33 ? 0.67255 0.46066 0.47859 0.08937  0.26679  0.09612  79  GLN B CG  
865  C CD  . GLN B 33 ? 0.72427 0.44953 0.47875 0.07928  0.28353  0.05878  79  GLN B CD  
866  O OE1 . GLN B 33 ? 0.79675 0.51283 0.52459 0.07690  0.29258  0.04176  79  GLN B OE1 
867  N NE2 . GLN B 33 ? 0.67904 0.36291 0.42040 0.07105  0.28927  0.04651  79  GLN B NE2 
868  N N   . VAL B 34 ? 0.61143 0.53167 0.55786 0.10983  0.28249  0.17288  80  VAL B N   
869  C CA  . VAL B 34 ? 0.62485 0.56675 0.57771 0.09033  0.27000  0.17116  80  VAL B CA  
870  C C   . VAL B 34 ? 0.54848 0.55492 0.57785 0.07129  0.25495  0.19722  80  VAL B C   
871  O O   . VAL B 34 ? 0.54379 0.55606 0.56247 0.04263  0.23011  0.18731  80  VAL B O   
872  C CB  . VAL B 34 ? 0.62467 0.54876 0.57737 0.10948  0.30353  0.17784  80  VAL B CB  
873  C CG1 . VAL B 34 ? 0.60491 0.54793 0.57790 0.09459  0.30119  0.18490  80  VAL B CG1 
874  C CG2 . VAL B 34 ? 0.68806 0.55414 0.55588 0.11900  0.31070  0.14866  80  VAL B CG2 
875  N N   . VAL B 35 ? 0.49068 0.55258 0.60530 0.08629  0.27044  0.23204  81  VAL B N   
876  C CA  . VAL B 35 ? 0.44782 0.59858 0.65824 0.06219  0.25150  0.25656  81  VAL B CA  
877  C C   . VAL B 35 ? 0.45095 0.60946 0.63176 0.04117  0.20506  0.24748  81  VAL B C   
878  O O   . VAL B 35 ? 0.41856 0.60763 0.62437 0.00436  0.16939  0.23546  81  VAL B O   
879  C CB  . VAL B 35 ? 0.45179 0.68682 0.77241 0.08826  0.26766  0.29451  81  VAL B CB  
880  C CG1 . VAL B 35 ? 0.41230 0.76196 0.83713 0.06037  0.22154  0.30311  81  VAL B CG1 
881  C CG2 . VAL B 35 ? 0.49579 0.71292 0.84272 0.10172  0.30608  0.29840  81  VAL B CG2 
882  N N   . LEU B 36 ? 0.44446 0.55982 0.56298 0.06357  0.20029  0.24230  82  LEU B N   
883  C CA  . LEU B 36 ? 0.45273 0.55986 0.53141 0.04922  0.15246  0.22734  82  LEU B CA  
884  C C   . LEU B 36 ? 0.46307 0.52428 0.47932 0.01393  0.13595  0.19647  82  LEU B C   
885  O O   . LEU B 36 ? 0.42786 0.50696 0.44599 -0.01340 0.09623  0.18582  82  LEU B O   
886  C CB  . LEU B 36 ? 0.49042 0.54500 0.51519 0.08147  0.16746  0.22998  82  LEU B CB  
887  C CG  . LEU B 36 ? 0.51558 0.53441 0.48059 0.07543  0.13728  0.21665  82  LEU B CG  
888  C CD1 . LEU B 36 ? 0.60190 0.57770 0.54385 0.11687  0.17053  0.23372  82  LEU B CD1 
889  C CD2 . LEU B 36 ? 0.54296 0.49884 0.43437 0.04454  0.13203  0.17876  82  LEU B CD2 
890  N N   . THR B 37 ? 0.50255 0.50668 0.46105 0.01673  0.16077  0.17518  83  THR B N   
891  C CA  . THR B 37 ? 0.50496 0.47785 0.41117 -0.00776 0.13913  0.14488  83  THR B CA  
892  C C   . THR B 37 ? 0.50593 0.50258 0.44941 -0.03176 0.13735  0.15495  83  THR B C   
893  O O   . THR B 37 ? 0.48269 0.46473 0.40183 -0.05526 0.11618  0.14375  83  THR B O   
894  C CB  . THR B 37 ? 0.56602 0.50563 0.42386 0.00365  0.14843  0.11641  83  THR B CB  
895  O OG1 . THR B 37 ? 0.56712 0.50965 0.44290 0.02114  0.17843  0.12667  83  THR B OG1 
896  C CG2 . THR B 37 ? 0.59104 0.50071 0.41726 0.01523  0.15305  0.09825  83  THR B CG2 
897  N N   . PHE B 38 ? 0.41942 0.45049 0.42961 -0.02851 0.16317  0.17490  84  PHE B N   
898  C CA  . PHE B 38 ? 0.40476 0.45000 0.45773 -0.05808 0.16733  0.17669  84  PHE B CA  
899  C C   . PHE B 38 ? 0.38357 0.48226 0.49804 -0.09436 0.13180  0.17724  84  PHE B C   
900  O O   . PHE B 38 ? 0.39181 0.47356 0.50462 -0.12811 0.12423  0.16250  84  PHE B O   
901  C CB  . PHE B 38 ? 0.46379 0.52785 0.57430 -0.04766 0.20372  0.18932  84  PHE B CB  
902  C CG  . PHE B 38 ? 0.46852 0.47683 0.51309 -0.02536 0.22361  0.17851  84  PHE B CG  
903  C CD1 . PHE B 38 ? 0.52597 0.50583 0.51127 0.00734  0.22787  0.16999  84  PHE B CD1 
904  C CD2 . PHE B 38 ? 0.51809 0.50449 0.56142 -0.03685 0.23697  0.17680  84  PHE B CD2 
905  C CE1 . PHE B 38 ? 0.59593 0.53949 0.52841 0.02811  0.24119  0.16254  84  PHE B CE1 
906  C CE2 . PHE B 38 ? 0.60212 0.54631 0.58981 -0.00790 0.25466  0.17496  84  PHE B CE2 
907  C CZ  . PHE B 38 ? 0.59838 0.52656 0.53193 0.02414  0.25408  0.16833  84  PHE B CZ  
908  N N   . LYS B 39 ? 0.37092 0.52825 0.52686 -0.08389 0.10260  0.18366  85  LYS B N   
909  C CA  . LYS B 39 ? 0.36626 0.57500 0.55227 -0.11145 0.05015  0.16938  85  LYS B CA  
910  C C   . LYS B 39 ? 0.38055 0.52620 0.47177 -0.12291 0.02307  0.14645  85  LYS B C   
911  O O   . LYS B 39 ? 0.37938 0.52978 0.47078 -0.15898 -0.00432 0.12496  85  LYS B O   
912  C CB  . LYS B 39 ? 0.37868 0.66513 0.61300 -0.08248 0.02492  0.18857  85  LYS B CB  
913  C CG  . LYS B 39 ? 0.36433 0.72778 0.70899 -0.06836 0.05286  0.21411  85  LYS B CG  
914  C CD  . LYS B 39 ? 0.38996 0.88303 0.83698 -0.07663 0.00729  0.21796  85  LYS B CD  
915  C CE  . LYS B 39 ? 0.36763 0.93862 0.90904 -0.03545 0.03377  0.25530  85  LYS B CE  
916  N NZ  . LYS B 39 ? 0.43789 1.13863 1.05172 -0.01551 -0.01801 0.26960  85  LYS B NZ  
917  N N   . LEU B 40 ? 0.40027 0.48620 0.41324 -0.09503 0.03406  0.14743  86  LEU B N   
918  C CA  . LEU B 40 ? 0.43879 0.46606 0.37065 -0.10433 0.01753  0.12718  86  LEU B CA  
919  C C   . LEU B 40 ? 0.45991 0.44761 0.37188 -0.13029 0.03101  0.11391  86  LEU B C   
920  O O   . LEU B 40 ? 0.46277 0.43166 0.35235 -0.15586 0.01068  0.09675  86  LEU B O   
921  C CB  . LEU B 40 ? 0.49345 0.47231 0.36422 -0.07535 0.03580  0.12618  86  LEU B CB  
922  C CG  . LEU B 40 ? 0.50183 0.47425 0.34921 -0.05454 0.02360  0.13091  86  LEU B CG  
923  C CD1 . LEU B 40 ? 0.48614 0.40864 0.29156 -0.03626 0.05055  0.11630  86  LEU B CD1 
924  C CD2 . LEU B 40 ? 0.48501 0.45251 0.30189 -0.07128 -0.01317 0.12068  86  LEU B CD2 
925  N N   . VAL B 41 ? 0.44503 0.41254 0.35563 -0.11882 0.07027  0.12378  87  VAL B N   
926  C CA  . VAL B 41 ? 0.49976 0.43276 0.40251 -0.11640 0.08677  0.11320  87  VAL B CA  
927  C C   . VAL B 41 ? 0.51325 0.45449 0.46434 -0.16219 0.08732  0.10844  87  VAL B C   
928  O O   . VAL B 41 ? 0.57284 0.47871 0.50361 -0.17155 0.08471  0.09187  87  VAL B O   
929  C CB  . VAL B 41 ? 0.50909 0.44945 0.41216 -0.08857 0.11056  0.12666  87  VAL B CB  
930  C CG1 . VAL B 41 ? 0.53417 0.44752 0.42350 -0.08565 0.12118  0.12255  87  VAL B CG1 
931  C CG2 . VAL B 41 ? 0.46144 0.40399 0.32310 -0.06005 0.09998  0.11440  87  VAL B CG2 
932  N N   . HIS B 42 ? 0.47994 0.48105 0.51138 -0.18669 0.08912  0.11850  88  HIS B N   
933  C CA  . HIS B 42 ? 0.46598 0.49543 0.56946 -0.23536 0.08597  0.10200  88  HIS B CA  
934  C C   . HIS B 42 ? 0.51003 0.52833 0.57863 -0.26528 0.04249  0.07003  88  HIS B C   
935  O O   . HIS B 42 ? 0.54345 0.53314 0.62488 -0.28691 0.05055  0.04543  88  HIS B O   
936  C CB  . HIS B 42 ? 0.42867 0.55762 0.63978 -0.24126 0.07515  0.10962  88  HIS B CB  
937  C CG  . HIS B 42 ? 0.46343 0.64090 0.76870 -0.29645 0.07155  0.08534  88  HIS B CG  
938  N ND1 . HIS B 42 ? 0.46688 0.72364 0.81283 -0.32578 0.01279  0.05822  88  HIS B ND1 
939  C CD2 . HIS B 42 ? 0.49844 0.65297 0.86096 -0.31082 0.11230  0.08529  88  HIS B CD2 
940  C CE1 . HIS B 42 ? 0.50702 0.78434 0.93496 -0.35991 0.02251  0.02904  88  HIS B CE1 
941  N NE2 . HIS B 42 ? 0.52738 0.74170 0.97121 -0.35403 0.08181  0.05211  88  HIS B NE2 
942  N N   . HIS B 43 ? 0.48126 0.51373 0.50208 -0.24608 0.00016  0.06785  89  HIS B N   
943  C CA  . HIS B 43 ? 0.49991 0.52839 0.48056 -0.26897 -0.04280 0.04048  89  HIS B CA  
944  C C   . HIS B 43 ? 0.51187 0.44986 0.39332 -0.25909 -0.03367 0.03386  89  HIS B C   
945  O O   . HIS B 43 ? 0.55512 0.47494 0.39029 -0.26873 -0.05937 0.01241  89  HIS B O   
946  C CB  . HIS B 43 ? 0.48439 0.58231 0.46901 -0.24552 -0.08970 0.04791  89  HIS B CB  
947  C CG  . HIS B 43 ? 0.49112 0.69967 0.57728 -0.25990 -0.11442 0.04755  89  HIS B CG  
948  N ND1 . HIS B 43 ? 0.51916 0.78387 0.64116 -0.30533 -0.15284 0.01367  89  HIS B ND1 
949  C CD2 . HIS B 43 ? 0.45192 0.73231 0.61744 -0.23545 -0.10496 0.07471  89  HIS B CD2 
950  C CE1 . HIS B 43 ? 0.48920 0.86931 0.71739 -0.30899 -0.17089 0.01968  89  HIS B CE1 
951  N NE2 . HIS B 43 ? 0.47619 0.86548 0.73348 -0.26411 -0.13974 0.06006  89  HIS B NE2 
952  N N   . SER B 44 ? 0.50636 0.32953 0.46351 -0.02180 0.14407  0.06332  90  SER B N   
953  C CA  . SER B 44 ? 0.49885 0.31420 0.47539 -0.00500 0.13473  0.07972  90  SER B CA  
954  C C   . SER B 44 ? 0.59067 0.35774 0.56316 0.00180  0.12217  0.09781  90  SER B C   
955  O O   . SER B 44 ? 0.67206 0.40734 0.60852 -0.01484 0.11500  0.10817  90  SER B O   
956  C CB  . SER B 44 ? 0.46704 0.29192 0.42908 -0.00485 0.12191  0.09192  90  SER B CB  
957  O OG  . SER B 44 ? 0.48490 0.34340 0.45305 -0.01128 0.12570  0.07497  90  SER B OG  
958  N N   . LYS B 45 ? 0.53378 0.29531 0.55046 0.02605  0.11500  0.09862  91  LYS B N   
959  C CA  . LYS B 45 ? 0.62650 0.34070 0.65318 0.04387  0.08440  0.11027  91  LYS B CA  
960  C C   . LYS B 45 ? 0.57273 0.29057 0.61231 0.06522  0.05538  0.12041  91  LYS B C   
961  O O   . LYS B 45 ? 0.60713 0.27936 0.64976 0.08215  0.01780  0.13232  91  LYS B O   
962  C CB  . LYS B 45 ? 0.60156 0.31942 0.69092 0.06243  0.08750  0.08460  91  LYS B CB  
963  C CG  . LYS B 45 ? 0.57201 0.36477 0.72297 0.07248  0.10495  0.05046  91  LYS B CG  
964  C CD  . LYS B 45 ? 0.62428 0.42928 0.83803 0.08581  0.10984  0.01662  91  LYS B CD  
965  C CE  . LYS B 45 ? 0.68267 0.43308 0.86513 0.07420  0.10849  0.02715  91  LYS B CE  
966  N NZ  . LYS B 45 ? 0.68833 0.44515 0.82453 0.04439  0.14200  0.03532  91  LYS B NZ  
967  N N   . LYS B 46 ? 0.48678 0.26173 0.53149 0.06222  0.06397  0.11204  92  LYS B N   
968  C CA  . LYS B 46 ? 0.49210 0.29059 0.55035 0.07793  0.03780  0.11330  92  LYS B CA  
969  C C   . LYS B 46 ? 0.48379 0.30125 0.49821 0.05812  0.04648  0.12515  92  LYS B C   
970  O O   . LYS B 46 ? 0.44029 0.28851 0.45420 0.04239  0.07087  0.11364  92  LYS B O   
971  C CB  . LYS B 46 ? 0.45593 0.32306 0.58502 0.09256  0.04098  0.07701  92  LYS B CB  
972  C CG  . LYS B 46 ? 0.53892 0.43345 0.70245 0.11484  0.01024  0.06663  92  LYS B CG  
973  C CD  . LYS B 46 ? 0.52970 0.50220 0.77026 0.12277  0.01856  0.01879  92  LYS B CD  
974  C CE  . LYS B 46 ? 0.49743 0.53136 0.75814 0.12275  0.00957  0.00367  92  LYS B CE  
975  N NZ  . LYS B 46 ? 0.47624 0.57965 0.82249 0.14007  0.00142  -0.04949 92  LYS B NZ  
976  N N   . ILE B 47 ? 0.45541 0.25375 0.43589 0.05922  0.02206  0.14562  93  ILE B N   
977  C CA  . ILE B 47 ? 0.46328 0.28798 0.41257 0.04333  0.02663  0.14948  93  ILE B CA  
978  C C   . ILE B 47 ? 0.45518 0.30254 0.42096 0.06101  -0.00214 0.15055  93  ILE B C   
979  O O   . ILE B 47 ? 0.50219 0.31488 0.45780 0.07511  -0.03448 0.16663  93  ILE B O   
980  C CB  . ILE B 47 ? 0.52431 0.31463 0.40395 0.01572  0.03095  0.16882  93  ILE B CB  
981  C CG1 . ILE B 47 ? 0.53096 0.30600 0.39572 -0.00518 0.06074  0.16142  93  ILE B CG1 
982  C CG2 . ILE B 47 ? 0.46749 0.29733 0.32949 0.00295  0.03297  0.16195  93  ILE B CG2 
983  C CD1 . ILE B 47 ? 0.49356 0.31145 0.39033 -0.00790 0.08552  0.13411  93  ILE B CD1 
984  N N   . THR B 48 ? 0.39474 0.29498 0.38333 0.05848  0.00495  0.13426  94  THR B N   
985  C CA  . THR B 48 ? 0.43498 0.36537 0.43820 0.07038  -0.01825 0.13125  94  THR B CA  
986  C C   . THR B 48 ? 0.41011 0.35339 0.37683 0.05226  -0.01595 0.13652  94  THR B C   
987  O O   . THR B 48 ? 0.35679 0.31455 0.32187 0.03538  0.00369  0.12604  94  THR B O   
988  C CB  . THR B 48 ? 0.41194 0.40024 0.47512 0.07671  -0.01331 0.10273  94  THR B CB  
989  O OG1 . THR B 48 ? 0.40316 0.39245 0.51087 0.09512  -0.01700 0.08687  94  THR B OG1 
990  C CG2 . THR B 48 ? 0.36886 0.39537 0.44830 0.08493  -0.03419 0.09492  94  THR B CG2 
991  N N   . LEU B 49 ? 0.43081 0.36939 0.37231 0.05663  -0.04047 0.14934  95  LEU B N   
992  C CA  . LEU B 49 ? 0.42866 0.38889 0.34108 0.03958  -0.03945 0.14775  95  LEU B CA  
993  C C   . LEU B 49 ? 0.46024 0.45911 0.39890 0.05300  -0.06075 0.13959  95  LEU B C   
994  O O   . LEU B 49 ? 0.46987 0.46049 0.41336 0.07244  -0.08910 0.14817  95  LEU B O   
995  C CB  . LEU B 49 ? 0.49217 0.41938 0.33640 0.02013  -0.04500 0.16855  95  LEU B CB  
996  C CG  . LEU B 49 ? 0.50505 0.40242 0.31937 -0.00157 -0.01979 0.17127  95  LEU B CG  
997  C CD1 . LEU B 49 ? 0.59316 0.44413 0.33316 -0.02508 -0.03174 0.20015  95  LEU B CD1 
998  C CD2 . LEU B 49 ? 0.46417 0.39923 0.28703 -0.02031 0.00713  0.14190  95  LEU B CD2 
999  N N   . ILE B 50 ? 0.39798 0.43547 0.35504 0.04264  -0.05179 0.12155  96  ILE B N   
1000 C CA  . ILE B 50 ? 0.43113 0.51107 0.41757 0.04983  -0.06712 0.10914  96  ILE B CA  
1001 C C   . ILE B 50 ? 0.42259 0.52039 0.38602 0.03627  -0.07175 0.10418  96  ILE B C   
1002 O O   . ILE B 50 ? 0.35536 0.45584 0.31787 0.01974  -0.05842 0.09189  96  ILE B O   
1003 C CB  . ILE B 50 ? 0.40912 0.51973 0.44011 0.04233  -0.05488 0.09014  96  ILE B CB  
1004 C CG1 . ILE B 50 ? 0.40260 0.50458 0.45627 0.04892  -0.04329 0.08757  96  ILE B CG1 
1005 C CG2 . ILE B 50 ? 0.40656 0.56602 0.46836 0.04575  -0.06918 0.07428  96  ILE B CG2 
1006 C CD1 . ILE B 50 ? 0.42651 0.55525 0.50501 0.02702  -0.02665 0.07214  96  ILE B CD1 
1007 N N   . GLY B 51 ? 0.45394 0.56607 0.40437 0.04451  -0.09441 0.10916  97  GLY B N   
1008 C CA  . GLY B 51 ? 0.45564 0.59371 0.38686 0.03048  -0.09840 0.09960  97  GLY B CA  
1009 C C   . GLY B 51 ? 0.56459 0.70297 0.45934 0.03659  -0.12574 0.11544  97  GLY B C   
1010 O O   . GLY B 51 ? 0.54498 0.66299 0.44191 0.05728  -0.14889 0.13115  97  GLY B O   
1011 N N   . ASP B 52 ? 0.54800 0.71023 0.41145 0.01780  -0.12677 0.10781  98  ASP B N   
1012 C CA  . ASP B 52 ? 0.66050 0.82410 0.47765 0.01633  -0.15566 0.12499  98  ASP B CA  
1013 C C   . ASP B 52 ? 0.66736 0.76955 0.42501 0.01138  -0.16973 0.16212  98  ASP B C   
1014 O O   . ASP B 52 ? 0.65447 0.72992 0.38253 -0.00933 -0.14654 0.16818  98  ASP B O   
1015 C CB  . ASP B 52 ? 0.65087 0.85740 0.43888 -0.01154 -0.14876 0.10589  98  ASP B CB  
1016 C CG  . ASP B 52 ? 0.77772 0.98025 0.49470 -0.02580 -0.17707 0.12940  98  ASP B CG  
1017 O OD1 . ASP B 52 ? 0.81314 0.97576 0.45874 -0.05021 -0.17956 0.15686  98  ASP B OD1 
1018 O OD2 . ASP B 52 ? 0.74974 0.98636 0.47832 -0.01561 -0.19984 0.12222  98  ASP B OD2 
1019 N N   . ALA B 53 ? 0.66599 0.82768 0.44603 0.03393  -0.25448 0.10929  99  ALA B N   
1020 C CA  . ALA B 53 ? 0.68489 0.82379 0.45013 0.05257  -0.24661 0.13755  99  ALA B CA  
1021 C C   . ALA B 53 ? 0.73149 0.82895 0.42203 0.05390  -0.22635 0.14964  99  ALA B C   
1022 O O   . ALA B 53 ? 0.72583 0.79749 0.41402 0.05752  -0.20265 0.16970  99  ALA B O   
1023 C CB  . ALA B 53 ? 0.67921 0.83509 0.45172 0.07194  -0.27797 0.14472  99  ALA B CB  
1024 N N   . ASN B 54 ? 0.78690 0.87684 0.41591 0.05022  -0.23323 0.13674  100 ASN B N   
1025 C CA  . ASN B 54 ? 0.78743 0.83780 0.34315 0.05181  -0.20935 0.14798  100 ASN B CA  
1026 C C   . ASN B 54 ? 0.78768 0.82854 0.35407 0.03598  -0.17243 0.14686  100 ASN B C   
1027 O O   . ASN B 54 ? 0.76323 0.77473 0.30590 0.03698  -0.14413 0.16495  100 ASN B O   
1028 C CB  . ASN B 54 ? 0.89809 0.94940 0.38623 0.05286  -0.22213 0.13179  100 ASN B CB  
1029 C CG  . ASN B 54 ? 0.92476 0.98880 0.39658 0.07074  -0.25199 0.14055  100 ASN B CG  
1030 O OD1 . ASN B 54 ? 0.99142 1.03238 0.46071 0.08559  -0.25192 0.16666  100 ASN B OD1 
1031 N ND2 . ASN B 54 ? 0.97498 1.07556 0.43547 0.06656  -0.27892 0.11891  100 ASN B ND2 
1032 N N   . LYS B 55 ? 0.74162 0.80759 0.34670 0.02047  -0.17257 0.12636  101 LYS B N   
1033 C CA  . LYS B 55 ? 0.75026 0.81405 0.36896 0.00682  -0.14082 0.12538  101 LYS B CA  
1034 C C   . LYS B 55 ? 0.68641 0.74737 0.35405 0.00927  -0.12304 0.14614  101 LYS B C   
1035 O O   . LYS B 55 ? 0.66000 0.70551 0.32113 0.00536  -0.09303 0.15760  101 LYS B O   
1036 C CB  . LYS B 55 ? 0.72244 0.80788 0.37800 -0.00772 -0.14778 0.09777  101 LYS B CB  
1037 C CG  . LYS B 55 ? 0.81172 0.89193 0.41644 -0.01443 -0.16101 0.07113  101 LYS B CG  
1038 C CD  . LYS B 55 ? 0.84326 0.91349 0.46309 -0.02582 -0.13739 0.04373  101 LYS B CD  
1039 C CE  . LYS B 55 ? 0.94167 1.00934 0.52684 -0.03562 -0.15981 0.01175  101 LYS B CE  
1040 N NZ  . LYS B 55 ? 0.91413 1.01398 0.54567 -0.04158 -0.19967 0.00439  101 LYS B NZ  
1041 N N   . ILE B 56 ? 0.63205 0.70811 0.35130 0.01466  -0.13968 0.14920  102 ILE B N   
1042 C CA  . ILE B 56 ? 0.60423 0.67375 0.36468 0.01523  -0.12318 0.16422  102 ILE B CA  
1043 C C   . ILE B 56 ? 0.65275 0.68887 0.38338 0.02556  -0.11074 0.18597  102 ILE B C   
1044 O O   . ILE B 56 ? 0.60973 0.63025 0.35707 0.02068  -0.08853 0.19687  102 ILE B O   
1045 C CB  . ILE B 56 ? 0.57568 0.66857 0.39441 0.01842  -0.14030 0.16020  102 ILE B CB  
1046 C CG1 . ILE B 56 ? 0.59307 0.69314 0.40807 0.03460  -0.16732 0.16289  102 ILE B CG1 
1047 C CG2 . ILE B 56 ? 0.53685 0.65718 0.38766 0.00448  -0.14660 0.13994  102 ILE B CG2 
1048 C CD1 . ILE B 56 ? 0.57604 0.70153 0.45487 0.04011  -0.17952 0.16173  102 ILE B CD1 
1049 N N   . LEU B 57 ? 0.67162 0.69350 0.35624 0.03829  -0.12558 0.19239  103 LEU B N   
1050 C CA  . LEU B 57 ? 0.70739 0.69030 0.35529 0.04571  -0.11226 0.21463  103 LEU B CA  
1051 C C   . LEU B 57 ? 0.71108 0.67238 0.32344 0.03384  -0.08024 0.21786  103 LEU B C   
1052 O O   . LEU B 57 ? 0.72156 0.65881 0.33894 0.02909  -0.05700 0.23266  103 LEU B O   
1053 C CB  . LEU B 57 ? 0.76870 0.73842 0.37017 0.06119  -0.13866 0.22270  103 LEU B CB  
1054 C CG  . LEU B 57 ? 0.74925 0.73644 0.38922 0.07733  -0.16786 0.22743  103 LEU B CG  
1055 C CD1 . LEU B 57 ? 0.86506 0.84919 0.45815 0.09121  -0.20047 0.23010  103 LEU B CD1 
1056 C CD2 . LEU B 57 ? 0.77761 0.74076 0.44345 0.08403  -0.15413 0.24929  103 LEU B CD2 
1057 N N   . GLN B 58 ? 0.74768 0.71794 0.32708 0.02776  -0.07714 0.20309  104 GLN B N   
1058 C CA  . GLN B 58 ? 0.78119 0.73878 0.33790 0.01647  -0.04212 0.20443  104 GLN B CA  
1059 C C   . GLN B 58 ? 0.69643 0.66431 0.31514 0.00578  -0.01904 0.20827  104 GLN B C   
1060 O O   . GLN B 58 ? 0.67545 0.62419 0.29424 -0.00119 0.00799  0.22053  104 GLN B O   
1061 C CB  . GLN B 58 ? 0.80157 0.77550 0.32977 0.01167  -0.04086 0.18299  104 GLN B CB  
1062 C CG  . GLN B 58 ? 0.86517 0.82983 0.32773 0.01885  -0.06511 0.17155  104 GLN B CG  
1063 C CD  . GLN B 58 ? 1.01031 0.95309 0.40682 0.00724  -0.04094 0.17128  104 GLN B CD  
1064 O OE1 . GLN B 58 ? 1.07128 1.00977 0.47078 -0.00079 -0.00863 0.18946  104 GLN B OE1 
1065 N NE2 . GLN B 58 ? 1.01873 1.00267 0.38531 0.00914  -0.05192 0.15452  104 GLN B NE2 
1066 N N   . TYR B 59 ? 0.63295 0.63054 0.30517 0.00141  -0.03107 0.19719  105 TYR B N   
1067 C CA  . TYR B 59 ? 0.61226 0.61902 0.33894 -0.01075 -0.01393 0.19902  105 TYR B CA  
1068 C C   . TYR B 59 ? 0.59839 0.58272 0.34396 -0.01048 -0.00890 0.21287  105 TYR B C   
1069 O O   . TYR B 59 ? 0.57063 0.54514 0.33350 -0.02129 0.01339  0.21919  105 TYR B O   
1070 C CB  . TYR B 59 ? 0.54476 0.58177 0.31485 -0.01651 -0.02985 0.18513  105 TYR B CB  
1071 C CG  . TYR B 59 ? 0.55343 0.60389 0.32919 -0.02180 -0.02140 0.16443  105 TYR B CG  
1072 C CD1 . TYR B 59 ? 0.54714 0.60185 0.34868 -0.03007 0.00381  0.16449  105 TYR B CD1 
1073 C CD2 . TYR B 59 ? 0.58486 0.64376 0.34585 -0.01860 -0.03915 0.14457  105 TYR B CD2 
1074 C CE1 . TYR B 59 ? 0.60352 0.66775 0.41527 -0.03135 0.01340  0.14700  105 TYR B CE1 
1075 C CE2 . TYR B 59 ? 0.60120 0.66481 0.36805 -0.02291 -0.02911 0.12452  105 TYR B CE2 
1076 C CZ  . TYR B 59 ? 0.62955 0.69445 0.42171 -0.02748 -0.00177 0.12652  105 TYR B CZ  
1077 O OH  . TYR B 59 ? 0.64053 0.70740 0.44263 -0.02838 0.00974  0.10791  105 TYR B OH  
1078 N N   . LYS B 60 ? 0.61933 0.59622 0.36482 0.00128  -0.02923 0.21723  106 LYS B N   
1079 C CA  . LYS B 60 ? 0.61615 0.56660 0.37454 0.00296  -0.02313 0.23101  106 LYS B CA  
1080 C C   . LYS B 60 ? 0.65157 0.56702 0.37480 0.00003  -0.00204 0.24632  106 LYS B C   
1081 O O   . LYS B 60 ? 0.63434 0.53402 0.37784 -0.01241 0.01723  0.25165  106 LYS B O   
1082 C CB  . LYS B 60 ? 0.60315 0.55065 0.36291 0.02050  -0.04679 0.23664  106 LYS B CB  
1083 C CG  . LYS B 60 ? 0.64250 0.55870 0.41663 0.02331  -0.03826 0.25140  106 LYS B CG  
1084 C CD  . LYS B 60 ? 0.66408 0.58667 0.46398 0.03995  -0.05789 0.25487  106 LYS B CD  
1085 C CE  . LYS B 60 ? 0.70520 0.58886 0.48837 0.05387  -0.05683 0.27609  106 LYS B CE  
1086 N NZ  . LYS B 60 ? 0.82151 0.68961 0.54961 0.06028  -0.06367 0.28725  106 LYS B NZ  
1087 N N   . ASN B 61 ? 0.67944 0.58124 0.34800 0.00850  -0.00669 0.25298  107 ASN B N   
1088 C CA  . ASN B 61 ? 0.74605 0.61351 0.37657 0.00221  0.01222  0.26999  107 ASN B CA  
1089 C C   . ASN B 61 ? 0.73742 0.61045 0.38270 -0.01636 0.04376  0.26672  107 ASN B C   
1090 O O   . ASN B 61 ? 0.77942 0.63231 0.43094 -0.02856 0.06351  0.27872  107 ASN B O   
1091 C CB  . ASN B 61 ? 0.81156 0.66868 0.37634 0.00962  -0.00123 0.27679  107 ASN B CB  
1092 C CG  . ASN B 61 ? 0.83825 0.68859 0.39161 0.02784  -0.03446 0.28488  107 ASN B CG  
1093 O OD1 . ASN B 61 ? 0.83820 0.68254 0.42856 0.03557  -0.04039 0.29134  107 ASN B OD1 
1094 N ND2 . ASN B 61 ? 0.88655 0.73943 0.39051 0.03395  -0.05676 0.28432  107 ASN B ND2 
1095 N N   . TYR B 62 ? 0.72167 0.62491 0.37856 -0.01916 0.04831  0.25111  108 TYR B N   
1096 C CA  . TYR B 62 ? 0.71441 0.62989 0.39338 -0.03415 0.07795  0.24840  108 TYR B CA  
1097 C C   . TYR B 62 ? 0.69078 0.61123 0.43112 -0.04778 0.08648  0.24861  108 TYR B C   
1098 O O   . TYR B 62 ? 0.65741 0.57072 0.41189 -0.06201 0.10935  0.25542  108 TYR B O   
1099 C CB  . TYR B 62 ? 0.70048 0.64797 0.38449 -0.03169 0.07840  0.23252  108 TYR B CB  
1100 C CG  . TYR B 62 ? 0.70153 0.67030 0.42450 -0.04360 0.10714  0.22909  108 TYR B CG  
1101 C CD1 . TYR B 62 ? 0.73178 0.69266 0.43496 -0.04964 0.13749  0.23543  108 TYR B CD1 
1102 C CD2 . TYR B 62 ? 0.64680 0.64789 0.42986 -0.04907 0.10258  0.22008  108 TYR B CD2 
1103 C CE1 . TYR B 62 ? 0.69506 0.68081 0.44453 -0.05795 0.16410  0.23196  108 TYR B CE1 
1104 C CE2 . TYR B 62 ? 0.63531 0.65957 0.46183 -0.05767 0.12588  0.21818  108 TYR B CE2 
1105 C CZ  . TYR B 62 ? 0.70407 0.72132 0.51704 -0.06086 0.15716  0.22360  108 TYR B CZ  
1106 O OH  . TYR B 62 ? 0.72080 0.76592 0.58722 -0.06716 0.17998  0.22129  108 TYR B OH  
1107 N N   . PHE B 63 ? 0.64222 0.57629 0.41901 -0.04608 0.06694  0.24043  109 PHE B N   
1108 C CA  . PHE B 63 ? 0.64630 0.58239 0.47304 -0.06130 0.07127  0.23830  109 PHE B CA  
1109 C C   . PHE B 63 ? 0.68125 0.57693 0.49595 -0.06613 0.08044  0.25156  109 PHE B C   
1110 O O   . PHE B 63 ? 0.66508 0.55492 0.50685 -0.08416 0.09584  0.25285  109 PHE B O   
1111 C CB  . PHE B 63 ? 0.54121 0.49449 0.39759 -0.05982 0.04823  0.22708  109 PHE B CB  
1112 C CG  . PHE B 63 ? 0.51838 0.50951 0.39433 -0.06058 0.03927  0.21431  109 PHE B CG  
1113 C CD1 . PHE B 63 ? 0.52287 0.53724 0.42600 -0.07109 0.05293  0.21099  109 PHE B CD1 
1114 C CD2 . PHE B 63 ? 0.48118 0.48478 0.35277 -0.05088 0.01765  0.20660  109 PHE B CD2 
1115 C CE1 . PHE B 63 ? 0.45835 0.50341 0.38006 -0.07060 0.04591  0.20178  109 PHE B CE1 
1116 C CE2 . PHE B 63 ? 0.49019 0.52345 0.37820 -0.05325 0.01076  0.19589  109 PHE B CE2 
1117 C CZ  . PHE B 63 ? 0.49391 0.54561 0.40485 -0.06255 0.02549  0.19446  109 PHE B CZ  
1118 N N   . GLN B 64 ? 0.67152 0.53988 0.44830 -0.05104 0.06919  0.26183  110 GLN B N   
1119 C CA  . GLN B 64 ? 0.73337 0.55979 0.49654 -0.05468 0.07606  0.27750  110 GLN B CA  
1120 C C   . GLN B 64 ? 0.79671 0.60929 0.53550 -0.06625 0.09734  0.29097  110 GLN B C   
1121 O O   . GLN B 64 ? 0.84996 0.63989 0.60044 -0.08154 0.11096  0.30061  110 GLN B O   
1122 C CB  . GLN B 64 ? 0.73929 0.54628 0.47497 -0.03313 0.05516  0.28768  110 GLN B CB  
1123 C CG  . GLN B 64 ? 0.75149 0.57214 0.51927 -0.02348 0.03732  0.27713  110 GLN B CG  
1124 C CD  . GLN B 64 ? 0.82223 0.62592 0.57507 -0.00110 0.01848  0.28923  110 GLN B CD  
1125 O OE1 . GLN B 64 ? 0.84982 0.64067 0.62890 0.00385  0.01485  0.29022  110 GLN B OE1 
1126 N NE2 . GLN B 64 ? 0.81034 0.61338 0.52177 0.01239  0.00630  0.29886  110 GLN B NE2 
1127 N N   . ALA B 65 ? 0.78470 0.61179 0.49019 -0.06078 0.10108  0.29206  111 ALA B N   
1128 C CA  . ALA B 65 ? 0.83598 0.65605 0.51831 -0.07132 0.12375  0.30640  111 ALA B CA  
1129 C C   . ALA B 65 ? 0.79883 0.63684 0.52928 -0.09279 0.14876  0.30072  111 ALA B C   
1130 O O   . ALA B 65 ? 0.91200 0.74322 0.64005 -0.10492 0.17055  0.31428  111 ALA B O   
1131 C CB  . ALA B 65 ? 0.84828 0.68138 0.48142 -0.06117 0.12362  0.30638  111 ALA B CB  
1132 N N   . ASN B 66 ? 0.81256 0.66908 0.79420 -0.16080 0.19253  0.34057  112 ASN B N   
1133 C CA  . ASN B 66 ? 0.79202 0.71334 0.78576 -0.17386 0.21358  0.33124  112 ASN B CA  
1134 C C   . ASN B 66 ? 0.78565 0.71871 0.79538 -0.18232 0.21604  0.32746  112 ASN B C   
1135 O O   . ASN B 66 ? 0.75281 0.76052 0.78944 -0.18063 0.23365  0.31914  112 ASN B O   
1136 C CB  . ASN B 66 ? 0.73745 0.72027 0.77416 -0.14229 0.22878  0.32530  112 ASN B CB  
1137 C CG  . ASN B 66 ? 0.74991 0.74418 0.77147 -0.14748 0.23820  0.32460  112 ASN B CG  
1138 O OD1 . ASN B 66 ? 0.74143 0.71752 0.77723 -0.12962 0.23754  0.32631  112 ASN B OD1 
1139 N ND2 . ASN B 66 ? 0.77275 0.80172 0.76773 -0.17488 0.25076  0.31957  112 ASN B ND2 
1140 N N   . GLY B 67 ? 0.81491 0.68366 0.81413 -0.18590 0.19967  0.33305  113 GLY B N   
1141 C CA  . GLY B 67 ? 0.82185 0.69497 0.83484 -0.20330 0.20533  0.32902  113 GLY B CA  
1142 C C   . GLY B 67 ? 0.78691 0.66589 0.84812 -0.17331 0.19713  0.32955  113 GLY B C   
1143 O O   . GLY B 67 ? 0.83562 0.73535 0.91904 -0.18916 0.20651  0.32489  113 GLY B O   
1144 N N   . ALA B 68 ? 0.77014 0.63827 0.85235 -0.13478 0.18394  0.33254  114 ALA B N   
1145 C CA  . ALA B 68 ? 0.77812 0.65315 0.90487 -0.10871 0.17840  0.33228  114 ALA B CA  
1146 C C   . ALA B 68 ? 0.86021 0.66599 0.97390 -0.12271 0.16354  0.33353  114 ALA B C   
1147 O O   . ALA B 68 ? 0.88964 0.61815 0.95794 -0.12739 0.14555  0.33751  114 ALA B O   
1148 C CB  . ALA B 68 ? 0.70375 0.57262 0.85077 -0.07308 0.16964  0.33142  114 ALA B CB  
1149 N N   . ARG B 69 ? 0.88951 0.72743 1.03845 -0.12572 0.16969  0.32382  115 ARG B N   
1150 C CA  . ARG B 69 ? 0.94920 0.72274 1.08570 -0.13964 0.15648  0.31141  115 ARG B CA  
1151 C C   . ARG B 69 ? 0.94756 0.65224 1.08041 -0.10664 0.12874  0.31621  115 ARG B C   
1152 O O   . ARG B 69 ? 0.85081 0.58571 1.01149 -0.07360 0.12132  0.31788  115 ARG B O   
1153 C CB  . ARG B 69 ? 0.92845 0.77387 1.10725 -0.14415 0.16477  0.28338  115 ARG B CB  
1154 C CG  . ARG B 69 ? 0.86720 0.82728 1.06674 -0.15406 0.18972  0.27666  115 ARG B CG  
1155 C CD  . ARG B 69 ? 0.86644 0.91621 1.10840 -0.15312 0.19612  0.24663  115 ARG B CD  
1156 N NE  . ARG B 69 ? 0.82079 0.92234 1.10278 -0.10594 0.18925  0.25064  115 ARG B NE  
1157 C CZ  . ARG B 69 ? 0.76561 0.92022 1.06112 -0.07253 0.19952  0.27212  115 ARG B CZ  
1158 N NH1 . ARG B 69 ? 0.70647 0.87771 0.98293 -0.07658 0.21494  0.28866  115 ARG B NH1 
1159 N NH2 . ARG B 69 ? 0.61496 0.80407 0.94294 -0.03439 0.19702  0.27658  115 ARG B NH2 
1160 N N   . SER B 70 ? 1.00466 0.61577 1.10165 -0.11553 0.11578  0.31690  116 SER B N   
1161 C CA  . SER B 70 ? 1.01098 0.56251 1.10214 -0.07863 0.08727  0.31813  116 SER B CA  
1162 C C   . SER B 70 ? 0.98706 0.58447 1.13308 -0.05301 0.07700  0.29168  116 SER B C   
1163 O O   . SER B 70 ? 0.99336 0.56363 1.14414 -0.01848 0.05295  0.28690  116 SER B O   
1164 C CB  . SER B 70 ? 1.07550 0.50800 1.10872 -0.08819 0.07912  0.32929  116 SER B CB  
1165 O OG  . SER B 70 ? 1.17027 0.58187 1.20325 -0.12643 0.09792  0.31244  116 SER B OG  
1166 N N   . ASP B 71 ? 0.94109 0.61923 1.12841 -0.06638 0.09417  0.27313  117 ASP B N   
1167 C CA  . ASP B 71 ? 0.91995 0.65255 1.15797 -0.04317 0.08620  0.24840  117 ASP B CA  
1168 C C   . ASP B 71 ? 0.84352 0.66598 1.12088 -0.01948 0.09434  0.25417  117 ASP B C   
1169 O O   . ASP B 71 ? 0.83420 0.72524 1.15445 -0.00398 0.09606  0.23795  117 ASP B O   
1170 C CB  . ASP B 71 ? 0.96418 0.73515 1.22247 -0.07029 0.10000  0.22027  117 ASP B CB  
1171 C CG  . ASP B 71 ? 0.96440 0.81948 1.22886 -0.09811 0.12800  0.22190  117 ASP B CG  
1172 O OD1 . ASP B 71 ? 0.91426 0.82508 1.18634 -0.08315 0.13731  0.24204  117 ASP B OD1 
1173 O OD2 . ASP B 71 ? 1.03493 0.90201 1.29690 -0.13517 0.14263  0.19979  117 ASP B OD2 
1174 N N   . ILE B 72 ? 0.79186 0.61124 1.05351 -0.01664 0.10179  0.27679  118 ILE B N   
1175 C CA  . ILE B 72 ? 0.66000 0.53671 0.95262 0.00570  0.11338  0.28402  118 ILE B CA  
1176 C C   . ILE B 72 ? 0.66026 0.49483 0.95126 0.02708  0.09224  0.28011  118 ILE B C   
1177 O O   . ILE B 72 ? 0.67509 0.44677 0.92766 0.02396  0.07751  0.28716  118 ILE B O   
1178 C CB  . ILE B 72 ? 0.65236 0.55121 0.93144 -0.00494 0.13762  0.30438  118 ILE B CB  
1179 C CG1 . ILE B 72 ? 0.64697 0.61744 0.93610 -0.01738 0.15898  0.30344  118 ILE B CG1 
1180 C CG2 . ILE B 72 ? 0.56272 0.48850 0.86673 0.01796  0.15195  0.31227  118 ILE B CG2 
1181 C CD1 . ILE B 72 ? 0.63325 0.63512 0.91028 -0.02208 0.18275  0.32086  118 ILE B CD1 
1182 N N   . ASP B 73 ? 0.69098 0.54014 0.50610 0.12217  -0.01946 0.16510  119 ASP B N   
1183 C CA  . ASP B 73 ? 0.66722 0.52785 0.52415 0.15201  -0.02666 0.16145  119 ASP B CA  
1184 C C   . ASP B 73 ? 0.59408 0.51011 0.51268 0.14620  -0.02286 0.17040  119 ASP B C   
1185 O O   . ASP B 73 ? 0.52272 0.48620 0.47682 0.14074  -0.00736 0.17690  119 ASP B O   
1186 C CB  . ASP B 73 ? 0.71568 0.59905 0.59107 0.18193  -0.01565 0.15277  119 ASP B CB  
1187 C CG  . ASP B 73 ? 0.80944 0.62611 0.62367 0.20154  -0.02770 0.13838  119 ASP B CG  
1188 O OD1 . ASP B 73 ? 0.94568 0.69025 0.69611 0.18419  -0.04448 0.13870  119 ASP B OD1 
1189 O OD2 . ASP B 73 ? 0.82352 0.66021 0.64910 0.23310  -0.02175 0.12624  119 ASP B OD2 
1190 N N   . PHE B 74 ? 0.55272 0.45779 0.48021 0.14734  -0.03914 0.17087  120 PHE B N   
1191 C CA  . PHE B 74 ? 0.53857 0.48613 0.51907 0.14323  -0.03982 0.17708  120 PHE B CA  
1192 C C   . PHE B 74 ? 0.52345 0.50092 0.55019 0.16644  -0.04145 0.17591  120 PHE B C   
1193 O O   . PHE B 74 ? 0.58362 0.53901 0.59892 0.18667  -0.05364 0.16876  120 PHE B O   
1194 C CB  . PHE B 74 ? 0.53387 0.46274 0.49806 0.12744  -0.05616 0.17727  120 PHE B CB  
1195 C CG  . PHE B 74 ? 0.54657 0.47582 0.47745 0.10170  -0.05353 0.17824  120 PHE B CG  
1196 C CD1 . PHE B 74 ? 0.52552 0.49545 0.48463 0.09465  -0.04727 0.18044  120 PHE B CD1 
1197 C CD2 . PHE B 74 ? 0.64508 0.53559 0.51257 0.08460  -0.05892 0.17650  120 PHE B CD2 
1198 C CE1 . PHE B 74 ? 0.50254 0.48702 0.43268 0.07620  -0.04515 0.17846  120 PHE B CE1 
1199 C CE2 . PHE B 74 ? 0.64927 0.55727 0.48672 0.05789  -0.05560 0.17704  120 PHE B CE2 
1200 C CZ  . PHE B 74 ? 0.55964 0.52100 0.43144 0.05657  -0.04783 0.17682  120 PHE B CZ  
1201 N N   . TYR B 75 ? 0.45130 0.47974 0.52648 0.16216  -0.03142 0.18343  121 TYR B N   
1202 C CA  . TYR B 75 ? 0.46062 0.53339 0.58181 0.17512  -0.03252 0.18459  121 TYR B CA  
1203 C C   . TYR B 75 ? 0.45112 0.53830 0.60430 0.15794  -0.04092 0.19286  121 TYR B C   
1204 O O   . TYR B 75 ? 0.39761 0.49051 0.55872 0.13968  -0.03677 0.20110  121 TYR B O   
1205 C CB  . TYR B 75 ? 0.44841 0.57295 0.59330 0.17877  -0.01523 0.18770  121 TYR B CB  
1206 C CG  . TYR B 75 ? 0.50844 0.61960 0.61990 0.19763  -0.00673 0.17657  121 TYR B CG  
1207 C CD1 . TYR B 75 ? 0.52250 0.59701 0.59340 0.18595  0.00042  0.17660  121 TYR B CD1 
1208 C CD2 . TYR B 75 ? 0.53771 0.67346 0.65464 0.22941  -0.00792 0.16367  121 TYR B CD2 
1209 C CE1 . TYR B 75 ? 0.56439 0.61950 0.59935 0.20144  0.00612  0.16540  121 TYR B CE1 
1210 C CE2 . TYR B 75 ? 0.57020 0.68633 0.65109 0.25101  -0.00329 0.14990  121 TYR B CE2 
1211 C CZ  . TYR B 75 ? 0.58290 0.65423 0.62161 0.23497  0.00356  0.15142  121 TYR B CZ  
1212 O OH  . TYR B 75 ? 0.65845 0.70368 0.65623 0.25428  0.00648  0.13697  121 TYR B OH  
1213 N N   . LEU B 76 ? 0.42436 0.51468 0.59302 0.16571  -0.05468 0.18985  122 LEU B N   
1214 C CA  . LEU B 76 ? 0.43235 0.53152 0.62743 0.15020  -0.06523 0.19527  122 LEU B CA  
1215 C C   . LEU B 76 ? 0.43403 0.58894 0.67400 0.14775  -0.06343 0.20202  122 LEU B C   
1216 O O   . LEU B 76 ? 0.44561 0.63259 0.69883 0.16667  -0.06379 0.19684  122 LEU B O   
1217 C CB  . LEU B 76 ? 0.48586 0.55578 0.66645 0.15455  -0.08260 0.18842  122 LEU B CB  
1218 C CG  . LEU B 76 ? 0.54679 0.56975 0.67817 0.14887  -0.08690 0.18325  122 LEU B CG  
1219 C CD1 . LEU B 76 ? 0.56576 0.56821 0.68457 0.14688  -0.10556 0.17899  122 LEU B CD1 
1220 C CD2 . LEU B 76 ? 0.46110 0.48433 0.58537 0.13162  -0.08034 0.18556  122 LEU B CD2 
1221 N N   . GLN B 77 ? 0.38082 0.54795 0.63986 0.12409  -0.06364 0.21329  123 GLN B N   
1222 C CA  . GLN B 77 ? 0.39778 0.61740 0.69337 0.10919  -0.06430 0.22361  123 GLN B CA  
1223 C C   . GLN B 77 ? 0.38968 0.58848 0.69435 0.09192  -0.08239 0.22659  123 GLN B C   
1224 O O   . GLN B 77 ? 0.38833 0.55849 0.68621 0.07250  -0.08886 0.23404  123 GLN B O   
1225 C CB  . GLN B 77 ? 0.38269 0.62419 0.68235 0.08987  -0.05266 0.23715  123 GLN B CB  
1226 C CG  . GLN B 77 ? 0.40840 0.68316 0.70301 0.10676  -0.03420 0.23263  123 GLN B CG  
1227 C CD  . GLN B 77 ? 0.50747 0.81392 0.80766 0.08438  -0.02258 0.24751  123 GLN B CD  
1228 O OE1 . GLN B 77 ? 0.50234 0.80263 0.80828 0.05400  -0.03047 0.26374  123 GLN B OE1 
1229 N NE2 . GLN B 77 ? 0.50333 0.83795 0.79647 0.09887  -0.00595 0.24198  123 GLN B NE2 
1230 N N   . PRO B 78 ? 0.38030 0.58900 0.69690 0.10059  -0.09307 0.21975  124 PRO B N   
1231 C CA  . PRO B 78 ? 0.38475 0.57590 0.70951 0.08363  -0.11073 0.22096  124 PRO B CA  
1232 C C   . PRO B 78 ? 0.39579 0.61875 0.74334 0.05308  -0.11487 0.23587  124 PRO B C   
1233 O O   . PRO B 78 ? 0.39437 0.67811 0.76196 0.04723  -0.10523 0.24345  124 PRO B O   
1234 C CB  . PRO B 78 ? 0.38204 0.58596 0.71433 0.10129  -0.11915 0.21115  124 PRO B CB  
1235 C CG  . PRO B 78 ? 0.38231 0.62621 0.72002 0.12525  -0.10786 0.20781  124 PRO B CG  
1236 C CD  . PRO B 78 ? 0.38224 0.60826 0.69828 0.12944  -0.09238 0.20887  124 PRO B CD  
1237 N N   . THR B 79 ? 0.41344 0.59435 0.75246 0.03235  -0.13064 0.23965  125 THR B N   
1238 C CA  . THR B 79 ? 0.43905 0.63202 0.78860 -0.00375 -0.14144 0.25523  125 THR B CA  
1239 C C   . THR B 79 ? 0.48203 0.64523 0.83124 -0.01386 -0.16354 0.24942  125 THR B C   
1240 O O   . THR B 79 ? 0.51565 0.64412 0.85360 0.00687  -0.17004 0.23352  125 THR B O   
1241 C CB  . THR B 79 ? 0.51357 0.66544 0.84037 -0.02277 -0.14413 0.26806  125 THR B CB  
1242 O OG1 . THR B 79 ? 0.53461 0.61309 0.83376 -0.01079 -0.15818 0.25720  125 THR B OG1 
1243 C CG2 . THR B 79 ? 0.45291 0.63106 0.77722 -0.01097 -0.12164 0.27177  125 THR B CG2 
1244 N N   . LEU B 80 ? 0.50636 0.68626 0.86504 -0.04949 -0.17589 0.26260  126 LEU B N   
1245 C CA  . LEU B 80 ? 0.56649 0.71796 0.92271 -0.06467 -0.19867 0.25804  126 LEU B CA  
1246 C C   . LEU B 80 ? 0.63343 0.71186 0.95825 -0.09363 -0.22097 0.26703  126 LEU B C   
1247 O O   . LEU B 80 ? 0.63732 0.71775 0.95337 -0.12408 -0.22175 0.28707  126 LEU B O   
1248 C CB  . LEU B 80 ? 0.52521 0.75284 0.91249 -0.08388 -0.19929 0.26434  126 LEU B CB  
1249 C CG  . LEU B 80 ? 0.46669 0.75200 0.87846 -0.04643 -0.18455 0.25142  126 LEU B CG  
1250 C CD1 . LEU B 80 ? 0.45417 0.81678 0.89584 -0.05987 -0.18856 0.25453  126 LEU B CD1 
1251 C CD2 . LEU B 80 ? 0.46249 0.69497 0.85928 -0.01420 -0.18930 0.23244  126 LEU B CD2 
1252 N N   . ASN B 81 ? 0.67155 0.68465 0.97564 -0.08343 -0.24125 0.25154  127 ASN B N   
1253 C CA  . ASN B 81 ? 0.72385 0.65355 0.99089 -0.10407 -0.26979 0.25497  127 ASN B CA  
1254 C C   . ASN B 81 ? 0.78155 0.66660 1.02048 -0.10202 -0.26926 0.26482  127 ASN B C   
1255 O O   . ASN B 81 ? 0.80788 0.63516 1.01555 -0.13174 -0.29124 0.27964  127 ASN B O   
1256 C CB  . ASN B 81 ? 0.73583 0.67146 1.00234 -0.15554 -0.28766 0.27280  127 ASN B CB  
1257 C CG  . ASN B 81 ? 0.72487 0.73668 1.02891 -0.16017 -0.28061 0.26837  127 ASN B CG  
1258 O OD1 . ASN B 81 ? 0.68741 0.77476 1.01539 -0.18888 -0.27148 0.28481  127 ASN B OD1 
1259 N ND2 . ASN B 81 ? 0.72148 0.72036 1.02987 -0.13141 -0.28568 0.24551  127 ASN B ND2 
1260 N N   . GLN B 82 ? 0.75244 0.65942 0.99747 -0.06897 -0.24649 0.25761  128 GLN B N   
1261 C CA  . GLN B 82 ? 0.78875 0.65665 1.00720 -0.06050 -0.24526 0.26344  128 GLN B CA  
1262 C C   . GLN B 82 ? 0.77106 0.58956 0.96510 -0.02013 -0.25507 0.23830  128 GLN B C   
1263 O O   . GLN B 82 ? 0.71587 0.56334 0.92266 0.00707  -0.24498 0.21834  128 GLN B O   
1264 C CB  . GLN B 82 ? 0.75929 0.69069 0.99772 -0.05382 -0.21315 0.27254  128 GLN B CB  
1265 C CG  . GLN B 82 ? 0.77299 0.72360 1.00992 -0.09153 -0.20964 0.30049  128 GLN B CG  
1266 C CD  . GLN B 82 ? 0.81727 0.78049 1.05942 -0.13822 -0.22598 0.31705  128 GLN B CD  
1267 O OE1 . GLN B 82 ? 0.72512 0.76623 1.00133 -0.14807 -0.21344 0.31869  128 GLN B OE1 
1268 N NE2 . GLN B 82 ? 0.91066 0.79688 1.11479 -0.16790 -0.25612 0.32962  128 GLN B NE2 
1269 N N   . LYS B 83 ? 0.81352 0.56065 0.96936 -0.01674 -0.27659 0.23939  129 LYS B N   
1270 C CA  . LYS B 83 ? 0.81166 0.51863 0.94102 0.02491  -0.28929 0.21338  129 LYS B CA  
1271 C C   . LYS B 83 ? 0.77967 0.51968 0.90919 0.04975  -0.26521 0.21104  129 LYS B C   
1272 O O   . LYS B 83 ? 0.75227 0.49351 0.87748 0.03574  -0.25559 0.23180  129 LYS B O   
1273 C CB  . LYS B 83 ? 0.92162 0.53617 1.00345 0.02314  -0.32466 0.21010  129 LYS B CB  
1274 C CG  . LYS B 83 ? 0.95428 0.54606 1.00797 0.06773  -0.33460 0.17002  129 LYS B CG  
1275 C CD  . LYS B 83 ? 1.06093 0.56454 1.06286 0.06916  -0.36691 0.16120  129 LYS B CD  
1276 C CE  . LYS B 83 ? 1.10469 0.57904 1.08559 0.04579  -0.36610 0.18751  129 LYS B CE  
1277 N NZ  . LYS B 83 ? 1.05515 0.55081 1.02513 0.07949  -0.34842 0.17705  129 LYS B NZ  
1278 N N   . GLY B 84 ? 0.74167 0.51401 0.87252 0.08181  -0.25390 0.18465  130 GLY B N   
1279 C CA  . GLY B 84 ? 0.66290 0.46856 0.78559 0.10225  -0.23090 0.17761  130 GLY B CA  
1280 C C   . GLY B 84 ? 0.55325 0.41560 0.70548 0.09215  -0.20288 0.19362  130 GLY B C   
1281 O O   . GLY B 84 ? 0.53362 0.42201 0.71236 0.07311  -0.19482 0.20344  130 GLY B O   
1282 N N   . VAL B 85 ? 0.41536 0.58802 0.38592 -0.00522 0.05156  -0.00813 131 VAL B N   
1283 C CA  . VAL B 85 ? 0.37902 0.51379 0.31190 -0.00035 0.04715  0.02603  131 VAL B CA  
1284 C C   . VAL B 85 ? 0.37169 0.46484 0.33146 -0.00151 0.03256  0.03185  131 VAL B C   
1285 O O   . VAL B 85 ? 0.36760 0.45318 0.37132 -0.00770 0.02759  0.01682  131 VAL B O   
1286 C CB  . VAL B 85 ? 0.38884 0.52207 0.29540 -0.01146 0.06214  0.04215  131 VAL B CB  
1287 C CG1 . VAL B 85 ? 0.40268 0.48496 0.28105 -0.00583 0.05194  0.07496  131 VAL B CG1 
1288 C CG2 . VAL B 85 ? 0.48964 0.66076 0.35204 -0.01794 0.07224  0.04291  131 VAL B CG2 
1289 N N   . VAL B 86 ? 0.36297 0.43342 0.29919 0.00430  0.02247  0.04898  132 VAL B N   
1290 C CA  . VAL B 86 ? 0.33842 0.37465 0.28831 -0.00188 0.01041  0.05715  132 VAL B CA  
1291 C C   . VAL B 86 ? 0.34820 0.36173 0.28397 0.00420  0.01368  0.07624  132 VAL B C   
1292 O O   . VAL B 86 ? 0.37083 0.38583 0.27761 0.01665  0.01213  0.08483  132 VAL B O   
1293 C CB  . VAL B 86 ? 0.35576 0.39580 0.29309 -0.00914 -0.00221 0.05244  132 VAL B CB  
1294 C CG1 . VAL B 86 ? 0.30929 0.31913 0.25184 -0.02317 -0.01429 0.06170  132 VAL B CG1 
1295 C CG2 . VAL B 86 ? 0.33722 0.38987 0.28359 -0.02039 -0.00800 0.03642  132 VAL B CG2 
1296 N N   . MET B 87 ? 0.30143 0.29039 0.26032 -0.00330 0.01319  0.08103  133 MET B N   
1297 C CA  . MET B 87 ? 0.34759 0.31037 0.29778 -0.00094 0.01526  0.09736  133 MET B CA  
1298 C C   . MET B 87 ? 0.32370 0.26914 0.28725 -0.00467 0.00224  0.09752  133 MET B C   
1299 O O   . MET B 87 ? 0.29352 0.23322 0.27897 -0.01588 -0.00673 0.09148  133 MET B O   
1300 C CB  . MET B 87 ? 0.32347 0.28214 0.28783 -0.01222 0.03027  0.09858  133 MET B CB  
1301 C CG  . MET B 87 ? 0.36677 0.29309 0.31694 -0.01544 0.03302  0.11739  133 MET B CG  
1302 S SD  . MET B 87 ? 0.49663 0.43061 0.46883 -0.04008 0.05494  0.10985  133 MET B SD  
1303 C CE  . MET B 87 ? 0.46684 0.35034 0.40135 -0.04805 0.05452  0.14068  133 MET B CE  
1304 N N   . ILE B 88 ? 0.33477 0.27250 0.28567 0.00401  -0.00332 0.10167  134 ILE B N   
1305 C CA  . ILE B 88 ? 0.33820 0.27089 0.30101 -0.00326 -0.01250 0.09657  134 ILE B CA  
1306 C C   . ILE B 88 ? 0.34871 0.25285 0.32003 0.00347  -0.01121 0.10540  134 ILE B C   
1307 O O   . ILE B 88 ? 0.35403 0.24511 0.31260 0.01912  -0.01523 0.11028  134 ILE B O   
1308 C CB  . ILE B 88 ? 0.34098 0.30705 0.29279 -0.00290 -0.02045 0.07809  134 ILE B CB  
1309 C CG1 . ILE B 88 ? 0.36890 0.36025 0.30726 -0.01488 -0.02038 0.07045  134 ILE B CG1 
1310 C CG2 . ILE B 88 ? 0.31042 0.28411 0.27070 -0.02072 -0.02686 0.06827  134 ILE B CG2 
1311 C CD1 . ILE B 88 ? 0.39694 0.43542 0.32397 -0.01590 -0.02305 0.04505  134 ILE B CD1 
1312 N N   . ALA B 89 ? 0.31135 0.20073 0.30411 -0.00844 -0.01035 0.10742  135 ALA B N   
1313 C CA  . ALA B 89 ? 0.34781 0.20985 0.35207 -0.00686 -0.00746 0.11385  135 ALA B CA  
1314 C C   . ALA B 89 ? 0.34441 0.21239 0.36612 -0.01236 -0.01685 0.10169  135 ALA B C   
1315 O O   . ALA B 89 ? 0.32553 0.20822 0.35113 -0.02762 -0.02356 0.09626  135 ALA B O   
1316 C CB  . ALA B 89 ? 0.35603 0.20622 0.37589 -0.01896 0.00586  0.11969  135 ALA B CB  
1317 N N   . SER B 90 ? 0.37185 0.22558 0.40249 -0.00259 -0.02099 0.09714  136 SER B N   
1318 C CA  . SER B 90 ? 0.38470 0.25642 0.43547 -0.00883 -0.02820 0.07757  136 SER B CA  
1319 C C   . SER B 90 ? 0.44718 0.28598 0.52016 -0.00228 -0.02925 0.07762  136 SER B C   
1320 O O   . SER B 90 ? 0.42258 0.22220 0.48776 0.01002  -0.03183 0.09097  136 SER B O   
1321 C CB  . SER B 90 ? 0.44313 0.35922 0.49174 -0.00318 -0.03727 0.04970  136 SER B CB  
1322 O OG  . SER B 90 ? 0.46906 0.41099 0.54114 -0.01122 -0.04186 0.02349  136 SER B OG  
1323 N N   . ASN B 91 ? 0.40403 0.25490 0.50026 -0.01429 -0.03018 0.06417  137 ASN B N   
1324 C CA  . ASN B 91 ? 0.45575 0.27886 0.57874 -0.00990 -0.03184 0.05856  137 ASN B CA  
1325 C C   . ASN B 91 ? 0.50417 0.35313 0.65257 0.00249  -0.04587 0.02344  137 ASN B C   
1326 O O   . ASN B 91 ? 0.50994 0.34766 0.68964 0.00383  -0.04994 0.00867  137 ASN B O   
1327 C CB  . ASN B 91 ? 0.41147 0.23349 0.55287 -0.02891 -0.02403 0.06049  137 ASN B CB  
1328 C CG  . ASN B 91 ? 0.38019 0.24774 0.52474 -0.04559 -0.03141 0.04354  137 ASN B CG  
1329 O OD1 . ASN B 91 ? 0.38496 0.28928 0.51077 -0.05130 -0.03764 0.03247  137 ASN B OD1 
1330 N ND2 . ASN B 91 ? 0.37657 0.24319 0.54065 -0.05846 -0.03184 0.04106  137 ASN B ND2 
1331 N N   . TYR B 92 ? 0.56291 0.45342 0.70452 0.01077  -0.05311 0.00287  138 TYR B N   
1332 C CA  . TYR B 92 ? 0.57393 0.50237 0.74996 0.02703  -0.06827 -0.04369 138 TYR B CA  
1333 C C   . TYR B 92 ? 0.56219 0.51135 0.73063 0.04827  -0.07976 -0.05795 138 TYR B C   
1334 O O   . TYR B 92 ? 0.56586 0.51337 0.69666 0.04257  -0.07139 -0.03293 138 TYR B O   
1335 C CB  . TYR B 92 ? 0.56373 0.56621 0.75221 -0.00079 -0.06136 -0.07937 138 TYR B CB  
1336 C CG  . TYR B 92 ? 0.52884 0.57915 0.67523 -0.03252 -0.05157 -0.07436 138 TYR B CG  
1337 C CD1 . TYR B 92 ? 0.49649 0.52314 0.60966 -0.05855 -0.04556 -0.03680 138 TYR B CD1 
1338 C CD2 . TYR B 92 ? 0.58179 0.69922 0.72418 -0.03830 -0.05227 -0.11037 138 TYR B CD2 
1339 C CE1 . TYR B 92 ? 0.48497 0.53860 0.55590 -0.09035 -0.04524 -0.02790 138 TYR B CE1 
1340 C CE2 . TYR B 92 ? 0.58157 0.73536 0.67752 -0.07625 -0.04431 -0.10244 138 TYR B CE2 
1341 C CZ  . TYR B 92 ? 0.53335 0.64730 0.59086 -0.10256 -0.04320 -0.05749 138 TYR B CZ  
1342 O OH  . TYR B 92 ? 0.58458 0.71855 0.59303 -0.14237 -0.04385 -0.04594 138 TYR B OH  
# 
